data_6A9O
# 
_entry.id   6A9O 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.313 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6A9O         
WWPDB D_1300008384 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6A9O 
_pdbx_database_status.recvd_initial_deposition_date   2018-07-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Manjula, R.'     1 ? 
'Padmanabhan, B.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biomol.Struct.Dyn. 
_citation.journal_id_ASTM           JBSDD6 
_citation.journal_id_CSD            0646 
_citation.journal_id_ISSN           1538-0254 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            37 
_citation.language                  ? 
_citation.page_first                3936 
_citation.page_last                 3946 
_citation.title                     
'Rational discovery of a SOD1 tryptophan oxidation inhibitor with therapeutic potential for amyotrophic lateral sclerosis.' 
_citation.year                      2019 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1080/07391102.2018.1531787 
_citation.pdbx_database_id_PubMed   30286701 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Manjula, R.'     1 ? 
primary 'Unni, S.'        2 ? 
primary 'Wright, G.S.A.'  3 ? 
primary 'Bharath M M, S.' 4 ? 
primary 'Padmanabhan, B.' 5 ? 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6A9O 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     164.367 
_cell.length_a_esd                 ? 
_cell.length_b                     203.692 
_cell.length_b_esd                 ? 
_cell.length_c                     144.211 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        80 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6A9O 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Superoxide dismutase [Cu-Zn]'                                                         15958.757 10   1.15.1.1 ? 
? ? 
2 non-polymer man 'ZINC ION'                                                                             65.409    9    ?        ? 
? ? 
3 non-polymer man 'DIMETHYL SULFOXIDE'                                                                   78.133    2    ?        ? 
? ? 
4 non-polymer man GLYCEROL                                                                               92.094    4    ?        ? 
? ? 
5 non-polymer syn 'Dihydrogen tetrasulfide'                                                              130.276   3    ?        ? 
? ? 
6 non-polymer syn 
;2'-[(6-oxo-5,6-dihydrophenanthridin-3-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
;
434.443   1    ?        ? ? ? 
7 water       nat water                                                                                  18.015    1234 ?        ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
_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       
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   CYS n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 CYS n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   154 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
# 
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 6A9O A 1 ? 154 ? P00441 1 ? 154 ? 0 153 
2  1 6A9O B 1 ? 154 ? P00441 1 ? 154 ? 0 153 
3  1 6A9O C 1 ? 154 ? P00441 1 ? 154 ? 0 153 
4  1 6A9O D 1 ? 154 ? P00441 1 ? 154 ? 0 153 
5  1 6A9O E 1 ? 154 ? P00441 1 ? 154 ? 0 153 
6  1 6A9O F 1 ? 154 ? P00441 1 ? 154 ? 0 153 
7  1 6A9O G 1 ? 154 ? P00441 1 ? 154 ? 0 153 
8  1 6A9O H 1 ? 154 ? P00441 1 ? 154 ? 0 153 
9  1 6A9O I 1 ? 154 ? P00441 1 ? 154 ? 0 153 
10 1 6A9O J 1 ? 154 ? P00441 1 ? 154 ? 0 153 
# 
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 
6B3 non-polymer         . 
;2'-[(6-oxo-5,6-dihydrophenanthridin-3-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
;
?                               'C27 H18 N2 O4'  434.443 
ALA 'L-peptide linking' y ALANINE                                                                                ? 'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                                               ? 
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                             ? 'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                        ? 'C4 H7 N O4' 
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                               ? 'C3 H7 N O2 S' 
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                   ? 'C2 H6 O S' 
78.133  
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  
GOL non-polymer         . GLYCEROL                                                                               
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE                                                                              ? 
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                                                  ? 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                             ? 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                ? 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                                                 ? 
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                                             ? 'C5 H11 N O2 S' 
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                          ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                                ? 'C5 H9 N O2' 
115.130 
S4P non-polymer         . 'Dihydrogen tetrasulfide'                                                              Tetrasulfane 
'H2 S4'          130.276 
SER 'L-peptide linking' y SERINE                                                                                 ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                              ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                             ? 'C11 H12 N2 O2' 
204.225 
VAL 'L-peptide linking' y VALINE                                                                                 ? 'C5 H11 N O2' 
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                             ? 'Zn 2' 65.409  
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   6A9O 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.80 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         67.60 
_exptl_crystal.description                 'THE ENTRY CONTAINS FRIEDEL PAIRS IN I/F_PLUS/MINUS COLUMNS.' 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.5M Sodium Citrate, pH 6.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS IV++' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-09-22 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        RIGAKU 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate            39.10 
_reflns.entry_id                         6A9O 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.500 
_reflns.d_resolution_low                 20.000 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       83750 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             100.0 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.500 
_reflns.pdbx_Rmerge_I_obs                0.07900 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            19.7000 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.50 
_reflns_shell.d_res_low                   2.50 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         2.000 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           4231 
_reflns_shell.percent_possible_all        100.0 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.54800 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             5.70 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            1.30 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.48 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.78 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               42.145 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.924 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 6A9O 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             20.00 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     79255 
_refine.ls_number_reflns_R_free                  4172 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.73 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16611 
_refine.ls_R_factor_R_free                       0.23712 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16342 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5YTO 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.272 
_refine.pdbx_overall_ESU_R_Free                  0.238 
_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_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             8.265 
_refine.overall_SU_ML                            0.180 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        10936 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         77 
_refine_hist.number_atoms_solvent             1234 
_refine_hist.number_atoms_total               12247 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        20.00 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.024  0.019  11228 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.319  1.948  15162 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.353  5.000  1512  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 43.504 25.581 473   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.763 15.000 1802  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 22.129 15.000 40    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.147  0.200  1677  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.021  8577  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'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       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'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' ? 3.401  4.051  6063  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.632  6.049  7567  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.120  4.333  5165  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.536  56.666 16737 ? 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          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.500 
_refine_ls_shell.d_res_low                        2.564 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             280 
_refine_ls_shell.number_reflns_R_work             5780 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.344 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.280 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6A9O 
_struct.title                        
'Rational discovery of a SOD1 tryptophan oxidation inhibitor with therapeutic potential for amyotrophic lateral sclerosis' 
_struct.pdbx_descriptor              'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6A9O 
_struct_keywords.text            'dismutase, dimer, oxidation, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 5 ? 
O  N N 2 ? 
P  N N 4 ? 
Q  N N 2 ? 
R  N N 4 ? 
S  N N 5 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 4 ? 
W  N N 2 ? 
X  N N 6 ? 
Y  N N 2 ? 
Z  N N 5 ? 
AA N N 2 ? 
BA N N 2 ? 
CA N N 2 ? 
DA N N 7 ? 
EA N N 7 ? 
FA N N 7 ? 
GA N N 7 ? 
HA N N 7 ? 
IA N N 7 ? 
JA N N 7 ? 
KA N N 7 ? 
LA N N 7 ? 
MA N N 7 ? 
# 
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  AA1 ALA A 56  ? GLY A 62  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  AA2 SER A 108 ? CYS A 112 ? SER A 107 CYS A 111 5 ? 5 
HELX_P HELX_P3  AA3 ASN A 132 ? THR A 138 ? ASN A 131 THR A 137 1 ? 7 
HELX_P HELX_P4  AA4 ALA B 56  ? GLY B 62  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P5  AA5 GLU B 134 ? GLY B 139 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P6  AA6 ALA C 56  ? GLY C 62  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P7  AA7 ALA D 56  ? GLY D 62  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P8  AA8 SER D 108 ? CYS D 112 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P9  AA9 ASN D 132 ? GLY D 139 ? ASN D 131 GLY D 138 1 ? 8 
HELX_P HELX_P10 AB1 CYS E 58  ? GLY E 62  ? CYS E 57  GLY E 61  5 ? 5 
HELX_P HELX_P11 AB2 SER E 108 ? CYS E 112 ? SER E 107 CYS E 111 5 ? 5 
HELX_P HELX_P12 AB3 GLU E 134 ? GLY E 139 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P13 AB4 ALA F 56  ? GLY F 62  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P14 AB5 SER F 108 ? CYS F 112 ? SER F 107 CYS F 111 5 ? 5 
HELX_P HELX_P15 AB6 GLU F 134 ? GLY F 139 ? GLU F 133 GLY F 138 1 ? 6 
HELX_P HELX_P16 AB7 ALA G 56  ? GLY G 62  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P17 AB8 ALA H 56  ? GLY H 62  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P18 AB9 ASN H 132 ? THR H 138 ? ASN H 131 THR H 137 1 ? 7 
HELX_P HELX_P19 AC1 CYS I 58  ? GLY I 62  ? CYS I 57  GLY I 61  5 ? 5 
HELX_P HELX_P20 AC2 GLU I 133 ? THR I 138 ? GLU I 132 THR I 137 1 ? 6 
HELX_P HELX_P21 AC3 ALA J 56  ? GLY J 62  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P22 AC4 SER J 108 ? CYS J 112 ? SER J 107 CYS J 111 5 ? 5 
HELX_P HELX_P23 AC5 GLU J 134 ? GLY J 139 ? GLU J 133 GLY J 138 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 58 SG  ? ? ? 1_555 A  CYS 147 SG ? ? A CYS 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.202 ? 
disulf2  disulf ? ? B CYS 58 SG  ? ? ? 1_555 B  CYS 147 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.251 ? 
disulf3  disulf ? ? C CYS 58 SG  ? ? ? 1_555 C  CYS 147 SG ? ? C CYS 57 C CYS 146 1_555 ? ? ? ? ? ? ? 2.211 ? 
disulf4  disulf ? ? D CYS 58 SG  ? ? ? 1_555 D  CYS 147 SG ? ? D CYS 57 D CYS 146 1_555 ? ? ? ? ? ? ? 2.194 ? 
disulf5  disulf ? ? E CYS 58 SG  ? ? ? 1_555 E  CYS 147 SG ? ? E CYS 57 E CYS 146 1_555 ? ? ? ? ? ? ? 2.214 ? 
disulf6  disulf ? ? F CYS 58 SG  ? ? ? 1_555 F  CYS 147 SG ? ? F CYS 57 F CYS 146 1_555 ? ? ? ? ? ? ? 2.233 ? 
disulf7  disulf ? ? G CYS 58 SG  ? ? ? 1_555 G  CYS 147 SG ? ? G CYS 57 G CYS 146 1_555 ? ? ? ? ? ? ? 2.250 ? 
disulf8  disulf ? ? H CYS 58 SG  ? ? ? 1_555 H  CYS 147 SG ? ? H CYS 57 H CYS 146 1_555 ? ? ? ? ? ? ? 2.251 ? 
disulf9  disulf ? ? I CYS 58 SG  ? ? ? 1_555 I  CYS 147 SG ? ? I CYS 57 I CYS 146 1_555 ? ? ? ? ? ? ? 2.164 ? 
disulf10 disulf ? ? J CYS 58 SG  ? ? ? 1_555 J  CYS 147 SG ? ? J CYS 57 J CYS 146 1_555 ? ? ? ? ? ? ? 2.180 ? 
metalc1  metalc ? ? A HIS 64 ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 63 A ZN  201 1_555 ? ? ? ? ? ? ? 2.140 ? 
metalc2  metalc ? ? A HIS 72 ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 71 A ZN  201 1_555 ? ? ? ? ? ? ? 2.243 ? 
metalc3  metalc ? ? A HIS 81 ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 80 A ZN  201 1_555 ? ? ? ? ? ? ? 2.076 ? 
metalc4  metalc ? ? A ASP 84 OD1 ? ? ? 1_555 K  ZN  .   ZN ? ? A ASP 83 A ZN  201 1_555 ? ? ? ? ? ? ? 2.188 ? 
metalc5  metalc ? ? B HIS 64 ND1 ? ? ? 1_555 O  ZN  .   ZN ? ? B HIS 63 B ZN  201 1_555 ? ? ? ? ? ? ? 2.036 ? 
metalc6  metalc ? ? B HIS 72 ND1 ? ? ? 1_555 O  ZN  .   ZN ? ? B HIS 71 B ZN  201 1_555 ? ? ? ? ? ? ? 2.168 ? 
metalc7  metalc ? ? B HIS 81 ND1 ? ? ? 1_555 O  ZN  .   ZN ? ? B HIS 80 B ZN  201 1_555 ? ? ? ? ? ? ? 2.047 ? 
metalc8  metalc ? ? B ASP 84 OD1 ? ? ? 1_555 O  ZN  .   ZN ? ? B ASP 83 B ZN  201 1_555 ? ? ? ? ? ? ? 2.048 ? 
metalc9  metalc ? ? C HIS 64 ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? C HIS 63 C ZN  201 1_555 ? ? ? ? ? ? ? 2.444 ? 
metalc10 metalc ? ? C HIS 72 ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? C HIS 71 C ZN  201 1_555 ? ? ? ? ? ? ? 2.288 ? 
metalc11 metalc ? ? C HIS 81 ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? C HIS 80 C ZN  201 1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc12 metalc ? ? C ASP 84 OD1 ? ? ? 1_555 Q  ZN  .   ZN ? ? C ASP 83 C ZN  201 1_555 ? ? ? ? ? ? ? 2.125 ? 
metalc13 metalc ? ? D HIS 64 ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 63 D ZN  201 1_555 ? ? ? ? ? ? ? 2.152 ? 
metalc14 metalc ? ? D HIS 72 ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 71 D ZN  201 1_555 ? ? ? ? ? ? ? 2.173 ? 
metalc15 metalc ? ? D HIS 81 ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 80 D ZN  201 1_555 ? ? ? ? ? ? ? 2.155 ? 
metalc16 metalc ? ? D ASP 84 OD1 ? ? ? 1_555 T  ZN  .   ZN ? ? D ASP 83 D ZN  201 1_555 ? ? ? ? ? ? ? 1.903 ? 
metalc17 metalc ? ? E HIS 64 ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? E HIS 63 E ZN  201 1_555 ? ? ? ? ? ? ? 2.291 ? 
metalc18 metalc ? ? E HIS 72 ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? E HIS 71 E ZN  201 1_555 ? ? ? ? ? ? ? 2.510 ? 
metalc19 metalc ? ? E HIS 81 ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? E HIS 80 E ZN  201 1_555 ? ? ? ? ? ? ? 2.177 ? 
metalc20 metalc ? ? E ASP 84 OD1 ? ? ? 1_555 W  ZN  .   ZN ? ? E ASP 83 E ZN  201 1_555 ? ? ? ? ? ? ? 2.426 ? 
metalc21 metalc ? ? F HIS 64 ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? F HIS 63 F ZN  202 1_555 ? ? ? ? ? ? ? 2.091 ? 
metalc22 metalc ? ? F HIS 72 ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? F HIS 71 F ZN  202 1_555 ? ? ? ? ? ? ? 2.220 ? 
metalc23 metalc ? ? F HIS 81 ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? F HIS 80 F ZN  202 1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc24 metalc ? ? F ASP 84 OD1 ? ? ? 1_555 Y  ZN  .   ZN ? ? F ASP 83 F ZN  202 1_555 ? ? ? ? ? ? ? 1.986 ? 
metalc25 metalc ? ? H HIS 64 ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? H HIS 63 H ZN  201 1_555 ? ? ? ? ? ? ? 2.245 ? 
metalc26 metalc ? ? H HIS 72 ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? H HIS 71 H ZN  201 1_555 ? ? ? ? ? ? ? 2.091 ? 
metalc27 metalc ? ? H HIS 81 ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? H HIS 80 H ZN  201 1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc28 metalc ? ? H ASP 84 OD1 ? ? ? 1_555 AA ZN  .   ZN ? ? H ASP 83 H ZN  201 1_555 ? ? ? ? ? ? ? 1.984 ? 
metalc29 metalc ? ? I HIS 64 ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 63 I ZN  201 1_555 ? ? ? ? ? ? ? 2.221 ? 
metalc30 metalc ? ? I HIS 72 ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 71 I ZN  201 1_555 ? ? ? ? ? ? ? 2.614 ? 
metalc31 metalc ? ? I HIS 81 ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 80 I ZN  201 1_555 ? ? ? ? ? ? ? 2.383 ? 
metalc32 metalc ? ? I ASP 84 OD1 ? ? ? 1_555 BA ZN  .   ZN ? ? I ASP 83 I ZN  201 1_555 ? ? ? ? ? ? ? 2.273 ? 
metalc33 metalc ? ? J HIS 64 ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? J HIS 63 J ZN  201 1_555 ? ? ? ? ? ? ? 2.163 ? 
metalc34 metalc ? ? J HIS 72 ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? J HIS 71 J ZN  201 1_555 ? ? ? ? ? ? ? 2.094 ? 
metalc35 metalc ? ? J HIS 81 ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? J HIS 80 J ZN  201 1_555 ? ? ? ? ? ? ? 2.104 ? 
metalc36 metalc ? ? J ASP 84 OD1 ? ? ? 1_555 CA ZN  .   ZN ? ? J ASP 83 J ZN  201 1_555 ? ? ? ? ? ? ? 2.008 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 5 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 5 ? 
AB1 ? 4 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 8 ? 
AB5 ? 5 ? 
AB6 ? 4 ? 
AB7 ? 5 ? 
AB8 ? 4 ? 
AB9 ? 5 ? 
AC1 ? 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 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB4 6 7 ? anti-parallel 
AB4 7 8 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB7 4 5 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 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 
AA1 1 ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
AA1 2 VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
AA1 3 GLN A 16  ? GLU A 22  ? GLN A 15  GLU A 21  
AA1 4 LYS A 4   ? LYS A 10  ? LYS A 3   LYS A 9   
AA1 5 GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
AA2 1 ASP A 84  ? ALA A 90  ? ASP A 83  ALA A 89  
AA2 2 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
AA2 3 THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
AA2 4 ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
AA3 1 ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
AA3 2 VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
AA3 3 GLN B 16  ? GLU B 22  ? GLN B 15  GLU B 21  
AA3 4 LYS B 4   ? LEU B 9   ? LYS B 3   LEU B 8   
AA3 5 GLY B 151 ? ILE B 152 ? GLY B 150 ILE B 151 
AA4 1 ASP B 84  ? ALA B 90  ? ASP B 83  ALA B 89  
AA4 2 GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
AA4 3 THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
AA4 4 ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
AA5 1 ALA C 96  ? ASP C 102 ? ALA C 95  ASP C 101 
AA5 2 VAL C 30  ? LYS C 37  ? VAL C 29  LYS C 36  
AA5 3 GLN C 16  ? GLU C 22  ? GLN C 15  GLU C 21  
AA5 4 LYS C 4   ? LEU C 9   ? LYS C 3   LEU C 8   
AA5 5 GLY C 151 ? ILE C 152 ? GLY C 150 ILE C 151 
AA6 1 ASP C 84  ? ALA C 90  ? ASP C 83  ALA C 89  
AA6 2 GLY C 42  ? HIS C 49  ? GLY C 41  HIS C 48  
AA6 3 THR C 117 ? HIS C 121 ? THR C 116 HIS C 120 
AA6 4 ARG C 144 ? VAL C 149 ? ARG C 143 VAL C 148 
AA7 1 ALA D 96  ? ASP D 102 ? ALA D 95  ASP D 101 
AA7 2 VAL D 30  ? LYS D 37  ? VAL D 29  LYS D 36  
AA7 3 GLN D 16  ? GLU D 22  ? GLN D 15  GLU D 21  
AA7 4 LYS D 4   ? LEU D 9   ? LYS D 3   LEU D 8   
AA7 5 GLY D 151 ? ILE D 152 ? GLY D 150 ILE D 151 
AA8 1 ASP D 84  ? ALA D 90  ? ASP D 83  ALA D 89  
AA8 2 GLY D 42  ? HIS D 49  ? GLY D 41  HIS D 48  
AA8 3 THR D 117 ? HIS D 121 ? THR D 116 HIS D 120 
AA8 4 ARG D 144 ? VAL D 149 ? ARG D 143 VAL D 148 
AA9 1 ALA E 96  ? ASP E 102 ? ALA E 95  ASP E 101 
AA9 2 VAL E 30  ? LYS E 37  ? VAL E 29  LYS E 36  
AA9 3 GLN E 16  ? GLU E 22  ? GLN E 15  GLU E 21  
AA9 4 LYS E 4   ? LEU E 9   ? LYS E 3   LEU E 8   
AA9 5 GLY E 151 ? ILE E 152 ? GLY E 150 ILE E 151 
AB1 1 ASP E 84  ? ALA E 90  ? ASP E 83  ALA E 89  
AB1 2 GLY E 42  ? HIS E 49  ? GLY E 41  HIS E 48  
AB1 3 THR E 117 ? HIS E 121 ? THR E 116 HIS E 120 
AB1 4 ARG E 144 ? VAL E 149 ? ARG E 143 VAL E 148 
AB2 1 ALA F 96  ? ASP F 102 ? ALA F 95  ASP F 101 
AB2 2 VAL F 30  ? LYS F 37  ? VAL F 29  LYS F 36  
AB2 3 GLN F 16  ? GLU F 22  ? GLN F 15  GLU F 21  
AB2 4 LYS F 4   ? LYS F 10  ? LYS F 3   LYS F 9   
AB2 5 GLY F 151 ? ILE F 152 ? GLY F 150 ILE F 151 
AB3 1 ASP F 84  ? ALA F 90  ? ASP F 83  ALA F 89  
AB3 2 GLY F 42  ? HIS F 49  ? GLY F 41  HIS F 48  
AB3 3 THR F 117 ? HIS F 121 ? THR F 116 HIS F 120 
AB3 4 ARG F 144 ? VAL F 149 ? ARG F 143 VAL F 148 
AB4 1 ASP G 84  ? ALA G 90  ? ASP G 83  ALA G 89  
AB4 2 GLY G 42  ? HIS G 49  ? GLY G 41  HIS G 48  
AB4 3 THR G 117 ? HIS G 121 ? THR G 116 HIS G 120 
AB4 4 ARG G 144 ? ILE G 152 ? ARG G 143 ILE G 151 
AB4 5 LYS G 4   ? LEU G 9   ? LYS G 3   LEU G 8   
AB4 6 GLN G 16  ? GLU G 22  ? GLN G 15  GLU G 21  
AB4 7 VAL G 30  ? LYS G 37  ? VAL G 29  LYS G 36  
AB4 8 ALA G 96  ? ASP G 102 ? ALA G 95  ASP G 101 
AB5 1 ALA H 96  ? ASP H 102 ? ALA H 95  ASP H 101 
AB5 2 VAL H 30  ? LYS H 37  ? VAL H 29  LYS H 36  
AB5 3 GLN H 16  ? GLN H 23  ? GLN H 15  GLN H 22  
AB5 4 LYS H 4   ? LEU H 9   ? LYS H 3   LEU H 8   
AB5 5 GLY H 151 ? ILE H 152 ? GLY H 150 ILE H 151 
AB6 1 ASP H 84  ? ALA H 90  ? ASP H 83  ALA H 89  
AB6 2 GLY H 42  ? HIS H 49  ? GLY H 41  HIS H 48  
AB6 3 THR H 117 ? HIS H 121 ? THR H 116 HIS H 120 
AB6 4 ARG H 144 ? VAL H 149 ? ARG H 143 VAL H 148 
AB7 1 ALA I 96  ? ASP I 102 ? ALA I 95  ASP I 101 
AB7 2 VAL I 30  ? LYS I 37  ? VAL I 29  LYS I 36  
AB7 3 GLN I 16  ? GLU I 22  ? GLN I 15  GLU I 21  
AB7 4 LYS I 4   ? LEU I 9   ? LYS I 3   LEU I 8   
AB7 5 GLY I 151 ? ILE I 152 ? GLY I 150 ILE I 151 
AB8 1 ASP I 84  ? ALA I 90  ? ASP I 83  ALA I 89  
AB8 2 GLY I 42  ? HIS I 49  ? GLY I 41  HIS I 48  
AB8 3 THR I 117 ? HIS I 121 ? THR I 116 HIS I 120 
AB8 4 ARG I 144 ? VAL I 149 ? ARG I 143 VAL I 148 
AB9 1 ALA J 96  ? ASP J 102 ? ALA J 95  ASP J 101 
AB9 2 VAL J 30  ? LYS J 37  ? VAL J 29  LYS J 36  
AB9 3 GLN J 16  ? GLU J 22  ? GLN J 15  GLU J 21  
AB9 4 LYS J 4   ? LYS J 10  ? LYS J 3   LYS J 9   
AB9 5 GLY J 151 ? ILE J 152 ? GLY J 150 ILE J 151 
AC1 1 ASP J 84  ? ALA J 90  ? ASP J 83  ALA J 89  
AC1 2 GLY J 42  ? HIS J 49  ? GLY J 41  HIS J 48  
AC1 3 THR J 117 ? HIS J 121 ? THR J 116 HIS J 120 
AC1 4 ARG J 144 ? VAL J 149 ? ARG J 143 VAL J 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 
AA1 1 2 O ASP A 102 ? O ASP A 101 N VAL A 30  ? N VAL A 29  
AA1 2 3 O TRP A 33  ? O TRP A 32  N ASN A 20  ? N ASN A 19  
AA1 3 4 O GLY A 17  ? O GLY A 16  N LEU A 9   ? N LEU A 8   
AA1 4 5 N VAL A 6   ? N VAL A 5   O GLY A 151 ? O GLY A 150 
AA2 1 2 O ALA A 90  ? O ALA A 89  N GLY A 42  ? N GLY A 41  
AA2 2 3 N GLY A 45  ? N GLY A 44  O HIS A 121 ? O HIS A 120 
AA2 3 4 N LEU A 118 ? N LEU A 117 O GLY A 148 ? O GLY A 147 
AA3 1 2 O ASP B 102 ? O ASP B 101 N VAL B 30  ? N VAL B 29  
AA3 2 3 O LYS B 31  ? O LYS B 30  N GLU B 22  ? N GLU B 21  
AA3 3 4 O GLY B 17  ? O GLY B 16  N LEU B 9   ? N LEU B 8   
AA3 4 5 N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
AA4 1 2 O ALA B 90  ? O ALA B 89  N GLY B 42  ? N GLY B 41  
AA4 2 3 N GLY B 45  ? N GLY B 44  O HIS B 121 ? O HIS B 120 
AA4 3 4 N LEU B 118 ? N LEU B 117 O GLY B 148 ? O GLY B 147 
AA5 1 2 O VAL C 98  ? O VAL C 97  N GLY C 34  ? N GLY C 33  
AA5 2 3 O TRP C 33  ? O TRP C 32  N ASN C 20  ? N ASN C 19  
AA5 3 4 O GLY C 17  ? O GLY C 16  N LEU C 9   ? N LEU C 8   
AA5 4 5 N VAL C 6   ? N VAL C 5   O GLY C 151 ? O GLY C 150 
AA6 1 2 O ALA C 90  ? O ALA C 89  N GLY C 42  ? N GLY C 41  
AA6 2 3 N HIS C 49  ? N HIS C 48  O THR C 117 ? O THR C 116 
AA6 3 4 N LEU C 118 ? N LEU C 117 O GLY C 148 ? O GLY C 147 
AA7 1 2 O ASP D 102 ? O ASP D 101 N VAL D 30  ? N VAL D 29  
AA7 2 3 O TRP D 33  ? O TRP D 32  N ASN D 20  ? N ASN D 19  
AA7 3 4 O GLY D 17  ? O GLY D 16  N LEU D 9   ? N LEU D 8   
AA7 4 5 N VAL D 6   ? N VAL D 5   O GLY D 151 ? O GLY D 150 
AA8 1 2 O VAL D 88  ? O VAL D 87  N HIS D 44  ? N HIS D 43  
AA8 2 3 N HIS D 49  ? N HIS D 48  O THR D 117 ? O THR D 116 
AA8 3 4 N VAL D 120 ? N VAL D 119 O ALA D 146 ? O ALA D 145 
AA9 1 2 O ALA E 96  ? O ALA E 95  N ILE E 36  ? N ILE E 35  
AA9 2 3 O TRP E 33  ? O TRP E 32  N ASN E 20  ? N ASN E 19  
AA9 3 4 O GLY E 17  ? O GLY E 16  N LEU E 9   ? N LEU E 8   
AA9 4 5 N VAL E 6   ? N VAL E 5   O GLY E 151 ? O GLY E 150 
AB1 1 2 O ALA E 90  ? O ALA E 89  N GLY E 42  ? N GLY E 41  
AB1 2 3 N GLY E 45  ? N GLY E 44  O HIS E 121 ? O HIS E 120 
AB1 3 4 N LEU E 118 ? N LEU E 117 O GLY E 148 ? O GLY E 147 
AB2 1 2 O ALA F 96  ? O ALA F 95  N ILE F 36  ? N ILE F 35  
AB2 2 3 O TRP F 33  ? O TRP F 32  N ASN F 20  ? N ASN F 19  
AB2 3 4 O PHE F 21  ? O PHE F 20  N ALA F 5   ? N ALA F 4   
AB2 4 5 N VAL F 6   ? N VAL F 5   O GLY F 151 ? O GLY F 150 
AB3 1 2 O ALA F 90  ? O ALA F 89  N GLY F 42  ? N GLY F 41  
AB3 2 3 N HIS F 49  ? N HIS F 48  O THR F 117 ? O THR F 116 
AB3 3 4 N VAL F 120 ? N VAL F 119 O ALA F 146 ? O ALA F 145 
AB4 1 2 O ALA G 90  ? O ALA G 89  N GLY G 42  ? N GLY G 41  
AB4 2 3 N HIS G 49  ? N HIS G 48  O THR G 117 ? O THR G 116 
AB4 3 4 N LEU G 118 ? N LEU G 117 O GLY G 148 ? O GLY G 147 
AB4 4 5 O GLY G 151 ? O GLY G 150 N VAL G 6   ? N VAL G 5   
AB4 5 6 N LEU G 9   ? N LEU G 8   O GLY G 17  ? O GLY G 16  
AB4 6 7 N ASN G 20  ? N ASN G 19  O TRP G 33  ? O TRP G 32  
AB4 7 8 N GLY G 34  ? N GLY G 33  O VAL G 98  ? O VAL G 97  
AB5 1 2 O ALA H 96  ? O ALA H 95  N ILE H 36  ? N ILE H 35  
AB5 2 3 O TRP H 33  ? O TRP H 32  N ASN H 20  ? N ASN H 19  
AB5 3 4 O PHE H 21  ? O PHE H 20  N ALA H 5   ? N ALA H 4   
AB5 4 5 N VAL H 6   ? N VAL H 5   O GLY H 151 ? O GLY H 150 
AB6 1 2 O VAL H 88  ? O VAL H 87  N HIS H 44  ? N HIS H 43  
AB6 2 3 N HIS H 49  ? N HIS H 48  O THR H 117 ? O THR H 116 
AB6 3 4 N LEU H 118 ? N LEU H 117 O GLY H 148 ? O GLY H 147 
AB7 1 2 O ASP I 102 ? O ASP I 101 N VAL I 30  ? N VAL I 29  
AB7 2 3 O TRP I 33  ? O TRP I 32  N ASN I 20  ? N ASN I 19  
AB7 3 4 O GLY I 17  ? O GLY I 16  N LEU I 9   ? N LEU I 8   
AB7 4 5 N VAL I 6   ? N VAL I 5   O GLY I 151 ? O GLY I 150 
AB8 1 2 O ALA I 90  ? O ALA I 89  N GLY I 42  ? N GLY I 41  
AB8 2 3 N HIS I 49  ? N HIS I 48  O THR I 117 ? O THR I 116 
AB8 3 4 N VAL I 120 ? N VAL I 119 O LEU I 145 ? O LEU I 144 
AB9 1 2 O VAL J 98  ? O VAL J 97  N GLY J 34  ? N GLY J 33  
AB9 2 3 O TRP J 33  ? O TRP J 32  N ASN J 20  ? N ASN J 19  
AB9 3 4 O GLY J 17  ? O GLY J 16  N LEU J 9   ? N LEU J 8   
AB9 4 5 N VAL J 6   ? N VAL J 5   O GLY J 151 ? O GLY J 150 
AC1 1 2 O ALA J 90  ? O ALA J 89  N GLY J 42  ? N GLY J 41  
AC1 2 3 N HIS J 47  ? N HIS J 46  O VAL J 119 ? O VAL J 118 
AC1 3 4 N LEU J 118 ? N LEU J 117 O GLY J 148 ? O GLY J 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  201 ? 4  'binding site for residue ZN A 201'                   
AC2 Software A DMS 202 ? 2  'binding site for residue DMS A 202'                  
AC3 Software A GOL 203 ? 4  'binding site for residue GOL A 203'                  
AC4 Software A S4P 204 ? 3  'binding site for residue S4P A 204'                  
AC5 Software B ZN  201 ? 4  'binding site for residue ZN B 201'                   
AC6 Software B GOL 202 ? 8  'binding site for residue GOL B 202'                  
AC7 Software C ZN  201 ? 4  'binding site for residue ZN C 201'                   
AC8 Software C GOL 202 ? 5  'binding site for residue GOL C 202'                  
AC9 Software D ZN  201 ? 4  'binding site for residue ZN D 201'                   
AD1 Software D DMS 202 ? 6  'binding site for residue DMS D 202'                  
AD2 Software D GOL 203 ? 7  'binding site for residue GOL D 203'                  
AD3 Software E ZN  201 ? 4  'binding site for residue ZN E 201'                   
AD4 Software F 6B3 201 ? 10 'binding site for residue 6B3 F 201'                  
AD5 Software F ZN  202 ? 4  'binding site for residue ZN F 202'                   
AD6 Software H ZN  201 ? 4  'binding site for residue ZN H 201'                   
AD7 Software I ZN  201 ? 4  'binding site for residue ZN I 201'                   
AD8 Software J ZN  201 ? 5  'binding site for residue ZN J 201'                   
AD9 Software C S4P 203 ? 10 'binding site for Di-peptide S4P C 203 and CYS C 111' 
AE1 Software F S4P 203 ? 11 'binding site for Di-peptide S4P F 203 and CYS F 111' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 4  HIS A  64  ? HIS A 63  . ? 1_555 ? 
2   AC1 4  HIS A  72  ? HIS A 71  . ? 1_555 ? 
3   AC1 4  HIS A  81  ? HIS A 80  . ? 1_555 ? 
4   AC1 4  ASP A  84  ? ASP A 83  . ? 1_555 ? 
5   AC2 2  ASP A  12  ? ASP A 11  . ? 1_555 ? 
6   AC2 2  ASN A  54  ? ASN A 53  . ? 1_555 ? 
7   AC3 4  HIS A  121 ? HIS A 120 . ? 1_555 ? 
8   AC3 4  GLY A  142 ? GLY A 141 . ? 1_555 ? 
9   AC3 4  ARG A  144 ? ARG A 143 . ? 1_555 ? 
10  AC3 4  HOH DA .   ? HOH A 307 . ? 1_555 ? 
11  AC4 3  CYS A  112 ? CYS A 111 . ? 1_555 ? 
12  AC4 3  HOH DA .   ? HOH A 407 . ? 1_555 ? 
13  AC4 3  CYS B  112 ? CYS B 111 . ? 1_555 ? 
14  AC5 4  HIS B  64  ? HIS B 63  . ? 1_555 ? 
15  AC5 4  HIS B  72  ? HIS B 71  . ? 1_555 ? 
16  AC5 4  HIS B  81  ? HIS B 80  . ? 1_555 ? 
17  AC5 4  ASP B  84  ? ASP B 83  . ? 1_555 ? 
18  AC6 8  LEU B  39  ? LEU B 38  . ? 1_555 ? 
19  AC6 8  THR B  40  ? THR B 39  . ? 1_555 ? 
20  AC6 8  GLU B  41  ? GLU B 40  . ? 1_555 ? 
21  AC6 8  GLY B  94  ? GLY B 93  . ? 1_555 ? 
22  AC6 8  ASP G  12  ? ASP G 11  . ? 1_555 ? 
23  AC6 8  GLY G  13  ? GLY G 12  . ? 1_555 ? 
24  AC6 8  PRO G  14  ? PRO G 13  . ? 1_555 ? 
25  AC6 8  HOH JA .   ? HOH G 213 . ? 1_555 ? 
26  AC7 4  HIS C  64  ? HIS C 63  . ? 1_555 ? 
27  AC7 4  HIS C  72  ? HIS C 71  . ? 1_555 ? 
28  AC7 4  HIS C  81  ? HIS C 80  . ? 1_555 ? 
29  AC7 4  ASP C  84  ? ASP C 83  . ? 1_555 ? 
30  AC8 5  THR C  138 ? THR C 137 . ? 1_555 ? 
31  AC8 5  ARG C  144 ? ARG C 143 . ? 1_555 ? 
32  AC8 5  HOH FA .   ? HOH C 349 . ? 1_555 ? 
33  AC8 5  HOH FA .   ? HOH C 384 . ? 1_555 ? 
34  AC8 5  HOH FA .   ? HOH C 397 . ? 1_555 ? 
35  AC9 4  HIS D  64  ? HIS D 63  . ? 1_555 ? 
36  AC9 4  HIS D  72  ? HIS D 71  . ? 1_555 ? 
37  AC9 4  HIS D  81  ? HIS D 80  . ? 1_555 ? 
38  AC9 4  ASP D  84  ? ASP D 83  . ? 1_555 ? 
39  AD1 6  LYS D  10  ? LYS D 9   . ? 1_555 ? 
40  AD1 6  ASP D  12  ? ASP D 11  . ? 1_555 ? 
41  AD1 6  ASN D  54  ? ASN D 53  . ? 1_555 ? 
42  AD1 6  HOH GA .   ? HOH D 378 . ? 1_555 ? 
43  AD1 6  HOH GA .   ? HOH D 401 . ? 1_555 ? 
44  AD1 6  HOH GA .   ? HOH D 408 . ? 4_575 ? 
45  AD2 7  HIS D  49  ? HIS D 48  . ? 1_555 ? 
46  AD2 7  HIS D  121 ? HIS D 120 . ? 1_555 ? 
47  AD2 7  GLY D  142 ? GLY D 141 . ? 1_555 ? 
48  AD2 7  ARG D  144 ? ARG D 143 . ? 1_555 ? 
49  AD2 7  HOH GA .   ? HOH D 305 . ? 1_555 ? 
50  AD2 7  HOH GA .   ? HOH D 333 . ? 1_555 ? 
51  AD2 7  HOH GA .   ? HOH D 338 . ? 1_555 ? 
52  AD3 4  HIS E  64  ? HIS E 63  . ? 1_555 ? 
53  AD3 4  HIS E  72  ? HIS E 71  . ? 1_555 ? 
54  AD3 4  HIS E  81  ? HIS E 80  . ? 1_555 ? 
55  AD3 4  ASP E  84  ? ASP E 83  . ? 1_555 ? 
56  AD4 10 LYS D  71  ? LYS D 70  . ? 3_555 ? 
57  AD4 10 GLU D  133 ? GLU D 132 . ? 3_555 ? 
58  AD4 10 LYS F  31  ? LYS F 30  . ? 1_555 ? 
59  AD4 10 TRP F  33  ? TRP F 32  . ? 1_555 ? 
60  AD4 10 SER F  99  ? SER F 98  . ? 1_555 ? 
61  AD4 10 ILE F  100 ? ILE F 99  . ? 1_555 ? 
62  AD4 10 GLU F  101 ? GLU F 100 . ? 1_555 ? 
63  AD4 10 HOH IA .   ? HOH F 357 . ? 1_555 ? 
64  AD4 10 GLY I  34  ? GLY I 33  . ? 1_555 ? 
65  AD4 10 ASP I  97  ? ASP I 96  . ? 1_555 ? 
66  AD5 4  HIS F  64  ? HIS F 63  . ? 1_555 ? 
67  AD5 4  HIS F  72  ? HIS F 71  . ? 1_555 ? 
68  AD5 4  HIS F  81  ? HIS F 80  . ? 1_555 ? 
69  AD5 4  ASP F  84  ? ASP F 83  . ? 1_555 ? 
70  AD6 4  HIS H  64  ? HIS H 63  . ? 1_555 ? 
71  AD6 4  HIS H  72  ? HIS H 71  . ? 1_555 ? 
72  AD6 4  HIS H  81  ? HIS H 80  . ? 1_555 ? 
73  AD6 4  ASP H  84  ? ASP H 83  . ? 1_555 ? 
74  AD7 4  HIS I  64  ? HIS I 63  . ? 1_555 ? 
75  AD7 4  HIS I  72  ? HIS I 71  . ? 1_555 ? 
76  AD7 4  HIS I  81  ? HIS I 80  . ? 1_555 ? 
77  AD7 4  ASP I  84  ? ASP I 83  . ? 1_555 ? 
78  AD8 5  HIS J  64  ? HIS J 63  . ? 1_555 ? 
79  AD8 5  HIS J  72  ? HIS J 71  . ? 1_555 ? 
80  AD8 5  HIS J  81  ? HIS J 80  . ? 1_555 ? 
81  AD8 5  ASP J  84  ? ASP J 83  . ? 1_555 ? 
82  AD8 5  LYS J  137 ? LYS J 136 . ? 1_555 ? 
83  AD9 10 SER C  106 ? SER C 105 . ? 1_555 ? 
84  AD9 10 GLY C  109 ? GLY C 108 . ? 1_555 ? 
85  AD9 10 ASP C  110 ? ASP C 109 . ? 1_555 ? 
86  AD9 10 HIS C  111 ? HIS C 110 . ? 1_555 ? 
87  AD9 10 ILE C  113 ? ILE C 112 . ? 1_555 ? 
88  AD9 10 ILE C  114 ? ILE C 113 . ? 1_555 ? 
89  AD9 10 ARG C  116 ? ARG C 115 . ? 1_555 ? 
90  AD9 10 HOH FA .   ? HOH C 417 . ? 1_555 ? 
91  AD9 10 CYS D  112 ? CYS D 111 . ? 1_555 ? 
92  AD9 10 ILE D  114 ? ILE D 113 . ? 1_555 ? 
93  AE1 11 CYS E  112 ? CYS E 111 . ? 1_555 ? 
94  AE1 11 PHE F  65  ? PHE F 64  . ? 1_555 ? 
95  AE1 11 SER F  106 ? SER F 105 . ? 1_555 ? 
96  AE1 11 LEU F  107 ? LEU F 106 . ? 1_555 ? 
97  AE1 11 SER F  108 ? SER F 107 . ? 1_555 ? 
98  AE1 11 GLY F  109 ? GLY F 108 . ? 1_555 ? 
99  AE1 11 ASP F  110 ? ASP F 109 . ? 1_555 ? 
100 AE1 11 HIS F  111 ? HIS F 110 . ? 1_555 ? 
101 AE1 11 ILE F  113 ? ILE F 112 . ? 1_555 ? 
102 AE1 11 ILE F  114 ? ILE F 113 . ? 1_555 ? 
103 AE1 11 ARG F  116 ? ARG F 115 . ? 1_555 ? 
# 
_atom_sites.entry_id                    6A9O 
_atom_sites.fract_transf_matrix[1][1]   0.006084 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.004909 
_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]   0.006934 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
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   . MET A  1 1   ? 30.087  247.160 33.016  1.00 59.67  ? 0   MET A N   1 
ATOM   2     C  CA  . MET A  1 1   ? 29.656  246.101 32.000  1.00 66.22  ? 0   MET A CA  1 
ATOM   3     C  C   . MET A  1 1   ? 30.657  246.035 30.803  1.00 68.73  ? 0   MET A C   1 
ATOM   4     O  O   . MET A  1 1   ? 31.416  245.029 30.682  1.00 67.44  ? 0   MET A O   1 
ATOM   5     C  CB  . MET A  1 1   ? 28.140  246.152 31.540  1.00 47.10  ? 0   MET A CB  1 
ATOM   6     N  N   . ALA A  1 2   ? 30.701  247.084 29.954  1.00 55.24  ? 1   ALA A N   1 
ATOM   7     C  CA  . ALA A  1 2   ? 31.312  246.944 28.565  1.00 50.95  ? 1   ALA A CA  1 
ATOM   8     C  C   . ALA A  1 2   ? 32.866  247.060 28.509  1.00 42.56  ? 1   ALA A C   1 
ATOM   9     O  O   . ALA A  1 2   ? 33.431  247.902 29.179  1.00 42.05  ? 1   ALA A O   1 
ATOM   10    C  CB  . ALA A  1 2   ? 30.652  247.917 27.588  1.00 47.35  ? 1   ALA A CB  1 
ATOM   11    N  N   . THR A  1 3   ? 33.559  246.212 27.771  1.00 35.12  ? 2   THR A N   1 
ATOM   12    C  CA  . THR A  1 3   ? 34.995  246.383 27.717  1.00 36.47  ? 2   THR A CA  1 
ATOM   13    C  C   . THR A  1 3   ? 35.468  246.783 26.324  1.00 38.26  ? 2   THR A C   1 
ATOM   14    O  O   . THR A  1 3   ? 36.660  247.176 26.192  1.00 36.12  ? 2   THR A O   1 
ATOM   15    C  CB  . THR A  1 3   ? 35.839  245.154 28.203  1.00 37.62  ? 2   THR A CB  1 
ATOM   16    O  OG1 . THR A  1 3   ? 35.667  244.035 27.334  1.00 39.50  ? 2   THR A OG1 1 
ATOM   17    C  CG2 . THR A  1 3   ? 35.513  244.741 29.570  1.00 37.03  ? 2   THR A CG2 1 
ATOM   18    N  N   . LYS A  1 4   ? 34.581  246.613 25.308  1.00 35.71  ? 3   LYS A N   1 
ATOM   19    C  CA  . LYS A  1 4   ? 34.857  246.955 23.899  1.00 36.66  ? 3   LYS A CA  1 
ATOM   20    C  C   . LYS A  1 4   ? 33.689  247.654 23.264  1.00 32.72  ? 3   LYS A C   1 
ATOM   21    O  O   . LYS A  1 4   ? 32.566  247.266 23.447  1.00 33.08  ? 3   LYS A O   1 
ATOM   22    C  CB  . LYS A  1 4   ? 35.301  245.753 23.019  1.00 38.89  ? 3   LYS A CB  1 
ATOM   23    C  CG  . LYS A  1 4   ? 36.411  244.874 23.616  1.00 49.65  ? 3   LYS A CG  1 
ATOM   24    C  CD  . LYS A  1 4   ? 36.902  243.741 22.706  1.00 56.79  ? 3   LYS A CD  1 
ATOM   25    C  CE  . LYS A  1 4   ? 37.230  244.256 21.283  1.00 63.15  ? 3   LYS A CE  1 
ATOM   26    N  NZ  . LYS A  1 4   ? 38.705  244.506 21.069  1.00 69.22  ? 3   LYS A NZ  1 
ATOM   27    N  N   . ALA A  1 5   ? 33.970  248.692 22.501  1.00 30.54  ? 4   ALA A N   1 
ATOM   28    C  CA  . ALA A  1 5   ? 32.948  249.341 21.765  1.00 30.96  ? 4   ALA A CA  1 
ATOM   29    C  C   . ALA A  1 5   ? 33.474  249.507 20.308  1.00 33.59  ? 4   ALA A C   1 
ATOM   30    O  O   . ALA A  1 5   ? 34.655  249.247 20.042  1.00 29.93  ? 4   ALA A O   1 
ATOM   31    C  CB  . ALA A  1 5   ? 32.615  250.635 22.443  1.00 26.80  ? 4   ALA A CB  1 
ATOM   32    N  N   . VAL A  1 6   ? 32.600  249.852 19.362  1.00 31.94  ? 5   VAL A N   1 
ATOM   33    C  CA  . VAL A  1 6   ? 33.037  250.041 17.982  1.00 29.61  ? 5   VAL A CA  1 
ATOM   34    C  C   . VAL A  1 6   ? 32.138  251.087 17.393  1.00 32.27  ? 5   VAL A C   1 
ATOM   35    O  O   . VAL A  1 6   ? 30.976  251.309 17.872  1.00 30.13  ? 5   VAL A O   1 
ATOM   36    C  CB  . VAL A  1 6   ? 32.983  248.714 17.226  1.00 30.74  ? 5   VAL A CB  1 
ATOM   37    C  CG1 . VAL A  1 6   ? 31.563  248.126 17.255  1.00 34.32  ? 5   VAL A CG1 1 
ATOM   38    C  CG2 . VAL A  1 6   ? 33.555  248.760 15.832  1.00 28.36  ? 5   VAL A CG2 1 
ATOM   39    N  N   . CYS A  1 7   ? 32.677  251.800 16.403  1.00 32.02  ? 6   CYS A N   1 
ATOM   40    C  CA  . CYS A  1 7   ? 31.911  252.843 15.722  1.00 31.50  ? 6   CYS A CA  1 
ATOM   41    C  C   . CYS A  1 7   ? 32.210  252.867 14.213  1.00 30.74  ? 6   CYS A C   1 
ATOM   42    O  O   . CYS A  1 7   ? 33.355  252.890 13.774  1.00 29.95  ? 6   CYS A O   1 
ATOM   43    C  CB  . CYS A  1 7   ? 32.180  254.185 16.402  1.00 33.55  ? 6   CYS A CB  1 
ATOM   44    S  SG  . CYS A  1 7   ? 31.228  255.493 15.637  1.00 34.23  ? 6   CYS A SG  1 
ATOM   45    N  N   . VAL A  1 8   ? 31.158  252.777 13.421  1.00 31.92  ? 7   VAL A N   1 
ATOM   46    C  CA  . VAL A  1 8   ? 31.264  252.772 11.962  1.00 32.26  ? 7   VAL A CA  1 
ATOM   47    C  C   . VAL A  1 8   ? 30.967  254.204 11.574  1.00 30.59  ? 7   VAL A C   1 
ATOM   48    O  O   . VAL A  1 8   ? 29.891  254.679 11.853  1.00 33.32  ? 7   VAL A O   1 
ATOM   49    C  CB  . VAL A  1 8   ? 30.325  251.736 11.258  1.00 27.69  ? 7   VAL A CB  1 
ATOM   50    C  CG1 . VAL A  1 8   ? 30.391  251.880 9.781   1.00 26.33  ? 7   VAL A CG1 1 
ATOM   51    C  CG2 . VAL A  1 8   ? 30.910  250.413 11.484  1.00 30.08  ? 7   VAL A CG2 1 
ATOM   52    N  N   . LEU A  1 9   ? 31.932  254.907 10.996  1.00 30.86  ? 8   LEU A N   1 
ATOM   53    C  CA  . LEU A  1 9   ? 31.662  256.295 10.538  1.00 32.89  ? 8   LEU A CA  1 
ATOM   54    C  C   . LEU A  1 9   ? 31.292  256.360 9.092   1.00 31.77  ? 8   LEU A C   1 
ATOM   55    O  O   . LEU A  1 9   ? 31.909  255.727 8.220   1.00 29.95  ? 8   LEU A O   1 
ATOM   56    C  CB  . LEU A  1 9   ? 32.797  257.241 10.821  1.00 34.63  ? 8   LEU A CB  1 
ATOM   57    C  CG  . LEU A  1 9   ? 33.443  257.163 12.200  1.00 33.83  ? 8   LEU A CG  1 
ATOM   58    C  CD1 . LEU A  1 9   ? 34.849  257.570 11.976  1.00 35.89  ? 8   LEU A CD1 1 
ATOM   59    C  CD2 . LEU A  1 9   ? 32.794  258.181 13.044  1.00 33.30  ? 8   LEU A CD2 1 
ATOM   60    N  N   . LYS A  1 10  ? 30.216  257.084 8.849   1.00 34.41  ? 9   LYS A N   1 
ATOM   61    C  CA  . LYS A  1 10  ? 29.685  257.242 7.476   1.00 37.43  ? 9   LYS A CA  1 
ATOM   62    C  C   . LYS A  1 10  ? 29.253  258.679 7.353   1.00 32.05  ? 9   LYS A C   1 
ATOM   63    O  O   . LYS A  1 10  ? 28.832  259.280 8.319   1.00 33.52  ? 9   LYS A O   1 
ATOM   64    C  CB  . LYS A  1 10  ? 28.465  256.321 7.244   1.00 37.44  ? 9   LYS A CB  1 
ATOM   65    C  CG  . LYS A  1 10  ? 28.806  254.867 7.177   1.00 44.04  ? 9   LYS A CG  1 
ATOM   66    C  CD  . LYS A  1 10  ? 27.990  254.133 6.123   1.00 52.10  ? 9   LYS A CD  1 
ATOM   67    C  CE  . LYS A  1 10  ? 28.331  252.608 6.069   1.00 63.73  ? 9   LYS A CE  1 
ATOM   68    N  NZ  . LYS A  1 10  ? 27.675  251.705 7.114   1.00 43.63  ? 9   LYS A NZ  1 
ATOM   69    N  N   . GLY A  1 11  ? 29.331  259.229 6.166   1.00 30.84  ? 10  GLY A N   1 
ATOM   70    C  CA  . GLY A  1 11  ? 28.798  260.551 5.904   1.00 32.31  ? 10  GLY A CA  1 
ATOM   71    C  C   . GLY A  1 11  ? 28.199  260.721 4.499   1.00 38.19  ? 10  GLY A C   1 
ATOM   72    O  O   . GLY A  1 11  ? 27.935  259.766 3.820   1.00 37.52  ? 10  GLY A O   1 
ATOM   73    N  N   . ASP A  1 12  ? 27.960  261.972 4.080   1.00 44.55  ? 11  ASP A N   1 
ATOM   74    C  CA  . ASP A  1 12  ? 27.508  262.279 2.724   1.00 43.96  ? 11  ASP A CA  1 
ATOM   75    C  C   . ASP A  1 12  ? 28.622  262.270 1.700   1.00 48.23  ? 11  ASP A C   1 
ATOM   76    O  O   . ASP A  1 12  ? 28.351  261.988 0.529   1.00 52.39  ? 11  ASP A O   1 
ATOM   77    C  CB  . ASP A  1 12  ? 26.849  263.602 2.699   1.00 44.66  ? 11  ASP A CB  1 
ATOM   78    C  CG  . ASP A  1 12  ? 25.506  263.585 3.409   1.00 51.95  ? 11  ASP A CG  1 
ATOM   79    O  OD1 . ASP A  1 12  ? 24.741  262.540 3.494   1.00 50.96  ? 11  ASP A OD1 1 
ATOM   80    O  OD2 . ASP A  1 12  ? 25.207  264.669 3.900   1.00 50.66  ? 11  ASP A OD2 1 
ATOM   81    N  N   . GLY A  1 13  ? 29.863  262.500 2.141   1.00 40.43  ? 12  GLY A N   1 
ATOM   82    C  CA  . GLY A  1 13  ? 31.009  262.509 1.251   1.00 39.69  ? 12  GLY A CA  1 
ATOM   83    C  C   . GLY A  1 13  ? 31.669  261.159 1.296   1.00 40.49  ? 12  GLY A C   1 
ATOM   84    O  O   . GLY A  1 13  ? 31.013  260.175 1.659   1.00 43.65  ? 12  GLY A O   1 
ATOM   85    N  N   . PRO A  1 14  ? 32.967  261.113 0.951   1.00 37.42  ? 13  PRO A N   1 
ATOM   86    C  CA  . PRO A  1 14  ? 33.805  259.890 0.899   1.00 34.79  ? 13  PRO A CA  1 
ATOM   87    C  C   . PRO A  1 14  ? 34.408  259.408 2.258   1.00 34.78  ? 13  PRO A C   1 
ATOM   88    O  O   . PRO A  1 14  ? 34.985  258.308 2.326   1.00 36.80  ? 13  PRO A O   1 
ATOM   89    C  CB  . PRO A  1 14  ? 34.958  260.317 -0.035  1.00 31.99  ? 13  PRO A CB  1 
ATOM   90    C  CG  . PRO A  1 14  ? 35.074  261.784 0.259   1.00 33.50  ? 13  PRO A CG  1 
ATOM   91    C  CD  . PRO A  1 14  ? 33.662  262.301 0.386   1.00 32.05  ? 13  PRO A CD  1 
ATOM   92    N  N   . VAL A  1 15  ? 34.320  260.214 3.312   1.00 33.34  ? 14  VAL A N   1 
ATOM   93    C  CA  . VAL A  1 15  ? 34.890  259.836 4.614   1.00 36.27  ? 14  VAL A CA  1 
ATOM   94    C  C   . VAL A  1 15  ? 34.211  258.614 5.238   1.00 38.81  ? 14  VAL A C   1 
ATOM   95    O  O   . VAL A  1 15  ? 32.991  258.526 5.301   1.00 36.76  ? 14  VAL A O   1 
ATOM   96    C  CB  . VAL A  1 15  ? 34.829  260.974 5.630   1.00 35.36  ? 14  VAL A CB  1 
ATOM   97    C  CG1 . VAL A  1 15  ? 35.504  260.526 6.901   1.00 32.45  ? 14  VAL A CG1 1 
ATOM   98    C  CG2 . VAL A  1 15  ? 35.447  262.265 5.071   1.00 32.85  ? 14  VAL A CG2 1 
ATOM   99    N  N   . GLN A  1 16  ? 35.007  257.645 5.655   1.00 37.57  ? 15  GLN A N   1 
ATOM   100   C  CA  . GLN A  1 16  ? 34.449  256.469 6.194   1.00 37.11  ? 15  GLN A CA  1 
ATOM   101   C  C   . GLN A  1 16  ? 35.452  255.777 7.053   1.00 35.17  ? 15  GLN A C   1 
ATOM   102   O  O   . GLN A  1 16  ? 36.591  255.813 6.754   1.00 37.39  ? 15  GLN A O   1 
ATOM   103   C  CB  . GLN A  1 16  ? 33.867  255.553 5.089   1.00 37.99  ? 15  GLN A CB  1 
ATOM   104   C  CG  . GLN A  1 16  ? 34.728  255.079 3.929   1.00 45.90  ? 15  GLN A CG  1 
ATOM   105   C  CD  . GLN A  1 16  ? 33.926  254.072 3.066   1.00 51.68  ? 15  GLN A CD  1 
ATOM   106   O  OE1 . GLN A  1 16  ? 33.181  253.272 3.605   1.00 56.38  ? 15  GLN A OE1 1 
ATOM   107   N  NE2 . GLN A  1 16  ? 34.062  254.123 1.746   1.00 44.20  ? 15  GLN A NE2 1 
ATOM   108   N  N   . GLY A  1 17  ? 35.026  255.134 8.120   1.00 34.93  ? 16  GLY A N   1 
ATOM   109   C  CA  . GLY A  1 17  ? 35.955  254.328 8.869   1.00 34.88  ? 16  GLY A CA  1 
ATOM   110   C  C   . GLY A  1 17  ? 35.385  253.577 10.046  1.00 36.46  ? 16  GLY A C   1 
ATOM   111   O  O   . GLY A  1 17  ? 34.189  253.696 10.384  1.00 37.10  ? 16  GLY A O   1 
ATOM   112   N  N   . ILE A  1 18  ? 36.258  252.771 10.636  1.00 34.19  ? 17  ILE A N   1 
ATOM   113   C  CA  . ILE A  1 18  ? 35.952  251.967 11.769  1.00 33.01  ? 17  ILE A CA  1 
ATOM   114   C  C   . ILE A  1 18  ? 36.899  252.345 12.914  1.00 34.50  ? 17  ILE A C   1 
ATOM   115   O  O   . ILE A  1 18  ? 38.122  252.261 12.773  1.00 33.48  ? 17  ILE A O   1 
ATOM   116   C  CB  . ILE A  1 18  ? 36.028  250.472 11.392  1.00 30.23  ? 17  ILE A CB  1 
ATOM   117   C  CG1 . ILE A  1 18  ? 34.952  250.144 10.331  1.00 28.65  ? 17  ILE A CG1 1 
ATOM   118   C  CG2 . ILE A  1 18  ? 35.952  249.608 12.636  1.00 25.69  ? 17  ILE A CG2 1 
ATOM   119   C  CD1 . ILE A  1 18  ? 35.288  248.977 9.490   1.00 23.80  ? 17  ILE A CD1 1 
ATOM   120   N  N   . ILE A  1 19  ? 36.309  252.750 14.034  1.00 31.90  ? 18  ILE A N   1 
ATOM   121   C  CA  . ILE A  1 19  ? 37.029  252.989 15.261  1.00 31.90  ? 18  ILE A CA  1 
ATOM   122   C  C   . ILE A  1 19  ? 36.615  252.011 16.374  1.00 35.23  ? 18  ILE A C   1 
ATOM   123   O  O   . ILE A  1 19  ? 35.425  251.879 16.697  1.00 34.25  ? 18  ILE A O   1 
ATOM   124   C  CB  . ILE A  1 19  ? 36.771  254.420 15.716  1.00 30.63  ? 18  ILE A CB  1 
ATOM   125   C  CG1 . ILE A  1 19  ? 37.182  255.407 14.603  1.00 32.08  ? 18  ILE A CG1 1 
ATOM   126   C  CG2 . ILE A  1 19  ? 37.396  254.675 17.063  1.00 27.83  ? 18  ILE A CG2 1 
ATOM   127   C  CD1 . ILE A  1 19  ? 38.675  255.724 14.604  1.00 35.50  ? 18  ILE A CD1 1 
ATOM   128   N  N   . ASN A  1 20  ? 37.612  251.332 16.930  1.00 33.46  ? 19  ASN A N   1 
ATOM   129   C  CA  . ASN A  1 20  ? 37.466  250.517 18.100  1.00 33.17  ? 19  ASN A CA  1 
ATOM   130   C  C   . ASN A  1 20  ? 37.769  251.236 19.399  1.00 32.91  ? 19  ASN A C   1 
ATOM   131   O  O   . ASN A  1 20  ? 38.487  252.207 19.416  1.00 34.34  ? 19  ASN A O   1 
ATOM   132   C  CB  . ASN A  1 20  ? 38.446  249.377 17.965  1.00 34.94  ? 19  ASN A CB  1 
ATOM   133   C  CG  . ASN A  1 20  ? 38.311  248.705 16.655  1.00 36.30  ? 19  ASN A CG  1 
ATOM   134   O  OD1 . ASN A  1 20  ? 39.191  248.799 15.833  1.00 39.89  ? 19  ASN A OD1 1 
ATOM   135   N  ND2 . ASN A  1 20  ? 37.158  248.121 16.398  1.00 37.03  ? 19  ASN A ND2 1 
ATOM   136   N  N   . PHE A  1 21  ? 37.215  250.734 20.493  1.00 32.24  ? 20  PHE A N   1 
ATOM   137   C  CA  . PHE A  1 21  ? 37.396  251.282 21.804  1.00 30.00  ? 20  PHE A CA  1 
ATOM   138   C  C   . PHE A  1 21  ? 37.646  250.117 22.697  1.00 33.70  ? 20  PHE A C   1 
ATOM   139   O  O   . PHE A  1 21  ? 36.969  249.088 22.590  1.00 37.28  ? 20  PHE A O   1 
ATOM   140   C  CB  . PHE A  1 21  ? 36.157  251.934 22.287  1.00 26.68  ? 20  PHE A CB  1 
ATOM   141   C  CG  . PHE A  1 21  ? 35.805  253.149 21.563  1.00 29.24  ? 20  PHE A CG  1 
ATOM   142   C  CD1 . PHE A  1 21  ? 34.991  253.086 20.415  1.00 28.92  ? 20  PHE A CD1 1 
ATOM   143   C  CD2 . PHE A  1 21  ? 36.272  254.389 21.992  1.00 29.12  ? 20  PHE A CD2 1 
ATOM   144   C  CE1 . PHE A  1 21  ? 34.668  254.250 19.732  1.00 28.17  ? 20  PHE A CE1 1 
ATOM   145   C  CE2 . PHE A  1 21  ? 35.931  255.546 21.317  1.00 26.57  ? 20  PHE A CE2 1 
ATOM   146   C  CZ  . PHE A  1 21  ? 35.120  255.470 20.194  1.00 28.11  ? 20  PHE A CZ  1 
ATOM   147   N  N   . GLU A  1 22  ? 38.643  250.236 23.566  1.00 33.90  ? 21  GLU A N   1 
ATOM   148   C  CA  . GLU A  1 22  ? 38.913  249.127 24.501  1.00 34.87  ? 21  GLU A CA  1 
ATOM   149   C  C   . GLU A  1 22  ? 39.235  249.650 25.894  1.00 34.42  ? 21  GLU A C   1 
ATOM   150   O  O   . GLU A  1 22  ? 39.960  250.641 26.027  1.00 34.14  ? 21  GLU A O   1 
ATOM   151   C  CB  . GLU A  1 22  ? 39.932  248.144 23.941  1.00 36.60  ? 21  GLU A CB  1 
ATOM   152   C  CG  . GLU A  1 22  ? 40.135  246.912 24.789  1.00 43.69  ? 21  GLU A CG  1 
ATOM   153   C  CD  . GLU A  1 22  ? 41.274  246.000 24.302  1.00 57.04  ? 21  GLU A CD  1 
ATOM   154   O  OE1 . GLU A  1 22  ? 42.423  246.484 24.187  1.00 64.52  ? 21  GLU A OE1 1 
ATOM   155   O  OE2 . GLU A  1 22  ? 41.034  244.776 24.056  1.00 62.86  ? 21  GLU A OE2 1 
ATOM   156   N  N   . GLN A  1 23  ? 38.614  249.054 26.909  1.00 32.06  ? 22  GLN A N   1 
ATOM   157   C  CA  . GLN A  1 23  ? 38.807  249.492 28.273  1.00 33.33  ? 22  GLN A CA  1 
ATOM   158   C  C   . GLN A  1 23  ? 38.716  248.287 29.147  1.00 36.52  ? 22  GLN A C   1 
ATOM   159   O  O   . GLN A  1 23  ? 37.616  247.875 29.556  1.00 41.62  ? 22  GLN A O   1 
ATOM   160   C  CB  . GLN A  1 23  ? 37.735  250.491 28.658  1.00 33.29  ? 22  GLN A CB  1 
ATOM   161   C  CG  . GLN A  1 23  ? 37.985  251.142 29.989  1.00 32.12  ? 22  GLN A CG  1 
ATOM   162   C  CD  . GLN A  1 23  ? 36.858  252.037 30.422  1.00 34.09  ? 22  GLN A CD  1 
ATOM   163   O  OE1 . GLN A  1 23  ? 35.707  251.858 30.016  1.00 37.69  ? 22  GLN A OE1 1 
ATOM   164   N  NE2 . GLN A  1 23  ? 37.170  253.019 31.254  1.00 32.86  ? 22  GLN A NE2 1 
ATOM   165   N  N   . LYS A  1 24  ? 39.866  247.699 29.423  1.00 41.31  ? 23  LYS A N   1 
ATOM   166   C  CA  . LYS A  1 24  ? 39.994  246.480 30.256  1.00 41.80  ? 23  LYS A CA  1 
ATOM   167   C  C   . LYS A  1 24  ? 39.591  246.689 31.713  1.00 41.94  ? 23  LYS A C   1 
ATOM   168   O  O   . LYS A  1 24  ? 39.083  245.755 32.303  1.00 48.69  ? 23  LYS A O   1 
ATOM   169   C  CB  . LYS A  1 24  ? 41.440  245.983 30.229  1.00 49.97  ? 23  LYS A CB  1 
ATOM   170   C  CG  . LYS A  1 24  ? 41.895  245.297 28.963  1.00 52.54  ? 23  LYS A CG  1 
ATOM   171   C  CD  . LYS A  1 24  ? 43.396  245.487 28.948  1.00 67.12  ? 23  LYS A CD  1 
ATOM   172   C  CE  . LYS A  1 24  ? 43.919  245.571 27.495  1.00 80.95  ? 23  LYS A CE  1 
ATOM   173   N  NZ  . LYS A  1 24  ? 44.392  244.235 26.946  1.00 75.68  ? 23  LYS A NZ  1 
ATOM   174   N  N   . GLU A  1 25  ? 39.811  247.887 32.279  1.00 34.18  ? 24  GLU A N   1 
ATOM   175   C  CA  . GLU A  1 25  ? 39.452  248.197 33.641  1.00 35.82  ? 24  GLU A CA  1 
ATOM   176   C  C   . GLU A  1 25  ? 38.473  249.346 33.644  1.00 37.38  ? 24  GLU A C   1 
ATOM   177   O  O   . GLU A  1 25  ? 38.727  250.383 33.044  1.00 36.26  ? 24  GLU A O   1 
ATOM   178   C  CB  . GLU A  1 25  ? 40.686  248.620 34.519  1.00 41.60  ? 24  GLU A CB  1 
ATOM   179   C  CG  . GLU A  1 25  ? 41.961  247.760 34.440  1.00 43.18  ? 24  GLU A CG  1 
ATOM   180   C  CD  . GLU A  1 25  ? 41.653  246.343 34.855  1.00 54.73  ? 24  GLU A CD  1 
ATOM   181   O  OE1 . GLU A  1 25  ? 40.711  246.131 35.669  1.00 60.44  ? 24  GLU A OE1 1 
ATOM   182   O  OE2 . GLU A  1 25  ? 42.318  245.417 34.367  1.00 63.59  ? 24  GLU A OE2 1 
ATOM   183   N  N   . SER A  1 26  ? 37.392  249.196 34.401  1.00 34.82  ? 25  SER A N   1 
ATOM   184   C  CA  . SER A  1 26  ? 36.355  250.159 34.355  1.00 34.45  ? 25  SER A CA  1 
ATOM   185   C  C   . SER A  1 26  ? 36.859  251.528 34.754  1.00 35.49  ? 25  SER A C   1 
ATOM   186   O  O   . SER A  1 26  ? 36.210  252.534 34.441  1.00 33.66  ? 25  SER A O   1 
ATOM   187   C  CB  . SER A  1 26  ? 35.157  249.695 35.226  1.00 33.42  ? 25  SER A CB  1 
ATOM   188   O  OG  . SER A  1 26  ? 35.536  249.482 36.573  1.00 36.68  ? 25  SER A OG  1 
ATOM   189   N  N   . ASN A  1 27  ? 37.960  251.544 35.514  1.00 35.75  ? 26  ASN A N   1 
ATOM   190   C  CA  . ASN A  1 27  ? 38.481  252.751 36.119  1.00 38.63  ? 26  ASN A CA  1 
ATOM   191   C  C   . ASN A  1 27  ? 39.837  253.088 35.510  1.00 42.26  ? 26  ASN A C   1 
ATOM   192   O  O   . ASN A  1 27  ? 40.507  254.042 35.979  1.00 46.13  ? 26  ASN A O   1 
ATOM   193   C  CB  . ASN A  1 27  ? 38.603  252.667 37.642  1.00 36.36  ? 26  ASN A CB  1 
ATOM   194   C  CG  . ASN A  1 27  ? 39.656  251.670 38.088  1.00 36.03  ? 26  ASN A CG  1 
ATOM   195   O  OD1 . ASN A  1 27  ? 39.797  250.631 37.464  1.00 40.99  ? 26  ASN A OD1 1 
ATOM   196   N  ND2 . ASN A  1 27  ? 40.380  251.964 39.175  1.00 33.78  ? 26  ASN A ND2 1 
ATOM   197   N  N   . GLY A  1 28  ? 40.219  252.282 34.517  1.00 41.59  ? 27  GLY A N   1 
ATOM   198   C  CA  . GLY A  1 28  ? 41.321  252.546 33.611  1.00 39.99  ? 27  GLY A CA  1 
ATOM   199   C  C   . GLY A  1 28  ? 41.004  253.326 32.315  1.00 44.43  ? 27  GLY A C   1 
ATOM   200   O  O   . GLY A  1 28  ? 39.866  253.763 32.037  1.00 36.24  ? 27  GLY A O   1 
ATOM   201   N  N   . PRO A  1 29  ? 42.062  253.572 31.528  1.00 45.02  ? 28  PRO A N   1 
ATOM   202   C  CA  . PRO A  1 29  ? 41.866  254.442 30.352  1.00 38.90  ? 28  PRO A CA  1 
ATOM   203   C  C   . PRO A  1 29  ? 41.232  253.691 29.191  1.00 37.87  ? 28  PRO A C   1 
ATOM   204   O  O   . PRO A  1 29  ? 41.318  252.443 29.116  1.00 40.90  ? 28  PRO A O   1 
ATOM   205   C  CB  . PRO A  1 29  ? 43.299  254.846 29.984  1.00 38.38  ? 28  PRO A CB  1 
ATOM   206   C  CG  . PRO A  1 29  ? 44.211  253.819 30.605  1.00 37.09  ? 28  PRO A CG  1 
ATOM   207   C  CD  . PRO A  1 29  ? 43.487  253.235 31.781  1.00 38.35  ? 28  PRO A CD  1 
ATOM   208   N  N   . VAL A  1 30  ? 40.652  254.440 28.263  1.00 34.62  ? 29  VAL A N   1 
ATOM   209   C  CA  . VAL A  1 30  ? 40.103  253.860 27.080  1.00 33.79  ? 29  VAL A CA  1 
ATOM   210   C  C   . VAL A  1 30  ? 41.105  253.940 25.884  1.00 34.74  ? 29  VAL A C   1 
ATOM   211   O  O   . VAL A  1 30  ? 41.543  255.006 25.555  1.00 32.89  ? 29  VAL A O   1 
ATOM   212   C  CB  . VAL A  1 30  ? 38.759  254.544 26.704  1.00 33.07  ? 29  VAL A CB  1 
ATOM   213   C  CG1 . VAL A  1 30  ? 38.121  253.820 25.523  1.00 30.25  ? 29  VAL A CG1 1 
ATOM   214   C  CG2 . VAL A  1 30  ? 37.802  254.594 27.874  1.00 29.68  ? 29  VAL A CG2 1 
ATOM   215   N  N   . LYS A  1 31  ? 41.447  252.827 25.236  1.00 34.73  ? 30  LYS A N   1 
ATOM   216   C  CA  . LYS A  1 31  ? 42.144  252.860 23.929  1.00 36.77  ? 30  LYS A CA  1 
ATOM   217   C  C   . LYS A  1 31  ? 41.203  253.080 22.737  1.00 37.93  ? 30  LYS A C   1 
ATOM   218   O  O   . LYS A  1 31  ? 40.150  252.400 22.607  1.00 38.70  ? 30  LYS A O   1 
ATOM   219   C  CB  . LYS A  1 31  ? 42.978  251.586 23.712  1.00 39.32  ? 30  LYS A CB  1 
ATOM   220   C  CG  . LYS A  1 31  ? 44.214  251.629 24.593  1.00 42.90  ? 30  LYS A CG  1 
ATOM   221   C  CD  . LYS A  1 31  ? 44.946  250.312 24.734  1.00 48.67  ? 30  LYS A CD  1 
ATOM   222   C  CE  . LYS A  1 31  ? 46.132  250.469 25.697  1.00 48.62  ? 30  LYS A CE  1 
ATOM   223   N  NZ  . LYS A  1 31  ? 46.571  249.061 25.867  1.00 57.09  ? 30  LYS A NZ  1 
ATOM   224   N  N   . VAL A  1 32  ? 41.584  254.019 21.876  1.00 35.11  ? 31  VAL A N   1 
ATOM   225   C  CA  . VAL A  1 32  ? 40.824  254.366 20.661  1.00 35.16  ? 31  VAL A CA  1 
ATOM   226   C  C   . VAL A  1 32  ? 41.667  254.165 19.405  1.00 37.61  ? 31  VAL A C   1 
ATOM   227   O  O   . VAL A  1 32  ? 42.707  254.794 19.237  1.00 41.11  ? 31  VAL A O   1 
ATOM   228   C  CB  . VAL A  1 32  ? 40.272  255.783 20.773  1.00 32.79  ? 31  VAL A CB  1 
ATOM   229   C  CG1 . VAL A  1 32  ? 39.313  256.075 19.661  1.00 27.96  ? 31  VAL A CG1 1 
ATOM   230   C  CG2 . VAL A  1 32  ? 39.591  255.928 22.138  1.00 28.85  ? 31  VAL A CG2 1 
ATOM   231   N  N   . TRP A  1 33  ? 41.273  253.273 18.516  1.00 35.09  ? 32  TRP A N   1 
ATOM   232   C  CA  . TRP A  1 33  ? 42.085  253.117 17.363  1.00 32.94  ? 32  TRP A CA  1 
ATOM   233   C  C   . TRP A  1 33  ? 41.296  252.625 16.168  1.00 33.88  ? 32  TRP A C   1 
ATOM   234   O  O   . TRP A  1 33  ? 40.228  252.000 16.280  1.00 35.49  ? 32  TRP A O   1 
ATOM   235   C  CB  . TRP A  1 33  ? 43.263  252.199 17.671  1.00 31.84  ? 32  TRP A CB  1 
ATOM   236   C  CG  . TRP A  1 33  ? 42.889  250.742 17.576  1.00 35.92  ? 32  TRP A CG  1 
ATOM   237   C  CD1 . TRP A  1 33  ? 43.019  249.944 16.505  1.00 34.58  ? 32  TRP A CD1 1 
ATOM   238   C  CD2 . TRP A  1 33  ? 42.294  249.945 18.590  1.00 39.45  ? 32  TRP A CD2 1 
ATOM   239   N  NE1 . TRP A  1 33  ? 42.584  248.698 16.764  1.00 35.61  ? 32  TRP A NE1 1 
ATOM   240   C  CE2 . TRP A  1 33  ? 42.138  248.645 18.049  1.00 37.39  ? 32  TRP A CE2 1 
ATOM   241   C  CE3 . TRP A  1 33  ? 41.862  250.201 19.914  1.00 43.06  ? 32  TRP A CE3 1 
ATOM   242   C  CZ2 . TRP A  1 33  ? 41.545  247.579 18.758  1.00 38.70  ? 32  TRP A CZ2 1 
ATOM   243   C  CZ3 . TRP A  1 33  ? 41.284  249.112 20.661  1.00 48.36  ? 32  TRP A CZ3 1 
ATOM   244   C  CH2 . TRP A  1 33  ? 41.125  247.820 20.057  1.00 45.08  ? 32  TRP A CH2 1 
ATOM   245   N  N   . GLY A  1 34  ? 41.890  252.860 15.017  1.00 33.20  ? 33  GLY A N   1 
ATOM   246   C  CA  . GLY A  1 34  ? 41.443  252.273 13.788  1.00 37.04  ? 33  GLY A CA  1 
ATOM   247   C  C   . GLY A  1 34  ? 41.638  253.220 12.620  1.00 39.83  ? 33  GLY A C   1 
ATOM   248   O  O   . GLY A  1 34  ? 42.424  254.133 12.690  1.00 39.44  ? 33  GLY A O   1 
ATOM   249   N  N   . SER A  1 35  ? 40.946  253.032 11.507  1.00 40.26  ? 34  SER A N   1 
ATOM   250   C  CA  . SER A  1 35  ? 41.264  253.977 10.499  1.00 39.58  ? 34  SER A CA  1 
ATOM   251   C  C   . SER A  1 35  ? 40.113  254.653 9.859   1.00 39.93  ? 34  SER A C   1 
ATOM   252   O  O   . SER A  1 35  ? 39.021  254.075 9.746   1.00 42.13  ? 34  SER A O   1 
ATOM   253   C  CB  . SER A  1 35  ? 42.261  253.416 9.504   1.00 41.23  ? 34  SER A CB  1 
ATOM   254   O  OG  . SER A  1 35  ? 41.653  252.528 8.658   1.00 43.13  ? 34  SER A OG  1 
ATOM   255   N  N   . ILE A  1 36  ? 40.352  255.883 9.460   1.00 34.43  ? 35  ILE A N   1 
ATOM   256   C  CA  . ILE A  1 36  ? 39.350  256.574 8.727   1.00 35.38  ? 35  ILE A CA  1 
ATOM   257   C  C   . ILE A  1 36  ? 39.975  256.946 7.408   1.00 37.87  ? 35  ILE A C   1 
ATOM   258   O  O   . ILE A  1 36  ? 41.128  257.399 7.374   1.00 38.37  ? 35  ILE A O   1 
ATOM   259   C  CB  . ILE A  1 36  ? 38.914  257.835 9.468   1.00 33.52  ? 35  ILE A CB  1 
ATOM   260   C  CG1 . ILE A  1 36  ? 38.640  257.549 10.970  1.00 31.94  ? 35  ILE A CG1 1 
ATOM   261   C  CG2 . ILE A  1 36  ? 37.805  258.572 8.708   1.00 26.87  ? 35  ILE A CG2 1 
ATOM   262   C  CD1 . ILE A  1 36  ? 38.658  258.866 11.750  1.00 35.24  ? 35  ILE A CD1 1 
ATOM   263   N  N   . LYS A  1 37  ? 39.237  256.783 6.323   1.00 35.26  ? 36  LYS A N   1 
ATOM   264   C  CA  . LYS A  1 37  ? 39.789  257.131 5.035   1.00 34.40  ? 36  LYS A CA  1 
ATOM   265   C  C   . LYS A  1 37  ? 38.940  258.194 4.352   1.00 34.07  ? 36  LYS A C   1 
ATOM   266   O  O   . LYS A  1 37  ? 37.932  258.670 4.924   1.00 34.27  ? 36  LYS A O   1 
ATOM   267   C  CB  . LYS A  1 37  ? 40.080  255.867 4.234   1.00 34.71  ? 36  LYS A CB  1 
ATOM   268   C  CG  . LYS A  1 37  ? 38.840  255.136 3.823   1.00 39.57  ? 36  LYS A CG  1 
ATOM   269   C  CD  . LYS A  1 37  ? 39.224  253.745 3.376   1.00 43.07  ? 36  LYS A CD  1 
ATOM   270   C  CE  . LYS A  1 37  ? 38.099  253.146 2.509   1.00 49.93  ? 36  LYS A CE  1 
ATOM   271   N  NZ  . LYS A  1 37  ? 38.327  251.668 2.274   1.00 54.14  ? 36  LYS A NZ  1 
ATOM   272   N  N   . GLY A  1 38  ? 39.406  258.661 3.197   1.00 35.25  ? 37  GLY A N   1 
ATOM   273   C  CA  . GLY A  1 38  ? 38.722  259.667 2.436   1.00 31.83  ? 37  GLY A CA  1 
ATOM   274   C  C   . GLY A  1 38  ? 38.822  261.054 3.023   1.00 32.74  ? 37  GLY A C   1 
ATOM   275   O  O   . GLY A  1 38  ? 38.006  261.943 2.693   1.00 31.78  ? 37  GLY A O   1 
ATOM   276   N  N   . LEU A  1 39  ? 39.833  261.275 3.857   1.00 33.02  ? 38  LEU A N   1 
ATOM   277   C  CA  . LEU A  1 39  ? 39.972  262.604 4.476   1.00 35.58  ? 38  LEU A CA  1 
ATOM   278   C  C   . LEU A  1 39  ? 41.024  263.499 3.740   1.00 38.35  ? 38  LEU A C   1 
ATOM   279   O  O   . LEU A  1 39  ? 41.970  262.962 3.129   1.00 35.85  ? 38  LEU A O   1 
ATOM   280   C  CB  . LEU A  1 39  ? 40.366  262.415 5.921   1.00 33.98  ? 38  LEU A CB  1 
ATOM   281   C  CG  . LEU A  1 39  ? 39.396  261.910 6.979   1.00 30.55  ? 38  LEU A CG  1 
ATOM   282   C  CD1 . LEU A  1 39  ? 40.231  261.472 8.162   1.00 29.66  ? 38  LEU A CD1 1 
ATOM   283   C  CD2 . LEU A  1 39  ? 38.392  263.016 7.373   1.00 30.81  ? 38  LEU A CD2 1 
ATOM   284   N  N   . THR A  1 40  ? 40.894  264.829 3.801   1.00 38.20  ? 39  THR A N   1 
ATOM   285   C  CA  . THR A  1 40  ? 42.010  265.665 3.301   1.00 39.29  ? 39  THR A CA  1 
ATOM   286   C  C   . THR A  1 40  ? 43.219  265.604 4.251   1.00 38.97  ? 39  THR A C   1 
ATOM   287   O  O   . THR A  1 40  ? 43.045  265.494 5.472   1.00 38.36  ? 39  THR A O   1 
ATOM   288   C  CB  . THR A  1 40  ? 41.638  267.115 3.193   1.00 38.88  ? 39  THR A CB  1 
ATOM   289   O  OG1 . THR A  1 40  ? 41.419  267.582 4.509   1.00 41.63  ? 39  THR A OG1 1 
ATOM   290   C  CG2 . THR A  1 40  ? 40.341  267.312 2.340   1.00 38.78  ? 39  THR A CG2 1 
ATOM   291   N  N   . GLU A  1 41  ? 44.448  265.624 3.701   1.00 46.66  ? 40  GLU A N   1 
ATOM   292   C  CA  . GLU A  1 41  ? 45.692  265.562 4.532   1.00 42.49  ? 40  GLU A CA  1 
ATOM   293   C  C   . GLU A  1 41  ? 45.714  266.648 5.617   1.00 40.00  ? 40  GLU A C   1 
ATOM   294   O  O   . GLU A  1 41  ? 45.251  267.814 5.381   1.00 35.56  ? 40  GLU A O   1 
ATOM   295   C  CB  . GLU A  1 41  ? 46.900  265.679 3.662   1.00 47.60  ? 40  GLU A CB  1 
ATOM   296   C  CG  . GLU A  1 41  ? 48.212  265.623 4.443   1.00 54.19  ? 40  GLU A CG  1 
ATOM   297   C  CD  . GLU A  1 41  ? 49.523  265.656 3.596   1.00 58.23  ? 40  GLU A CD  1 
ATOM   298   O  OE1 . GLU A  1 41  ? 49.524  265.805 2.321   1.00 50.30  ? 40  GLU A OE1 1 
ATOM   299   O  OE2 . GLU A  1 41  ? 50.582  265.514 4.274   1.00 54.61  ? 40  GLU A OE2 1 
ATOM   300   N  N   . GLY A  1 42  ? 46.149  266.276 6.827   1.00 35.27  ? 41  GLY A N   1 
ATOM   301   C  CA  . GLY A  1 42  ? 46.014  267.277 7.886   1.00 34.37  ? 41  GLY A CA  1 
ATOM   302   C  C   . GLY A  1 42  ? 45.189  266.902 9.092   1.00 37.39  ? 41  GLY A C   1 
ATOM   303   O  O   . GLY A  1 42  ? 44.809  265.748 9.246   1.00 39.47  ? 41  GLY A O   1 
ATOM   304   N  N   . LEU A  1 43  ? 44.908  267.902 9.915   1.00 36.30  ? 42  LEU A N   1 
ATOM   305   C  CA  . LEU A  1 43  ? 44.236  267.747 11.173  1.00 37.95  ? 42  LEU A CA  1 
ATOM   306   C  C   . LEU A  1 43  ? 42.699  267.781 11.036  1.00 42.95  ? 42  LEU A C   1 
ATOM   307   O  O   . LEU A  1 43  ? 42.137  268.680 10.370  1.00 39.75  ? 42  LEU A O   1 
ATOM   308   C  CB  . LEU A  1 43  ? 44.666  268.862 12.134  1.00 37.63  ? 42  LEU A CB  1 
ATOM   309   C  CG  . LEU A  1 43  ? 46.116  268.951 12.646  1.00 43.29  ? 42  LEU A CG  1 
ATOM   310   C  CD1 . LEU A  1 43  ? 46.316  270.200 13.534  1.00 40.13  ? 42  LEU A CD1 1 
ATOM   311   C  CD2 . LEU A  1 43  ? 46.646  267.695 13.340  1.00 34.52  ? 42  LEU A CD2 1 
ATOM   312   N  N   . HIS A  1 44  ? 42.033  266.855 11.755  1.00 39.79  ? 43  HIS A N   1 
ATOM   313   C  CA  . HIS A  1 44  ? 40.589  266.818 11.856  1.00 33.61  ? 43  HIS A CA  1 
ATOM   314   C  C   . HIS A  1 44  ? 40.141  266.645 13.298  1.00 32.09  ? 43  HIS A C   1 
ATOM   315   O  O   . HIS A  1 44  ? 40.643  265.773 14.039  1.00 30.01  ? 43  HIS A O   1 
ATOM   316   C  CB  . HIS A  1 44  ? 40.074  265.698 10.963  1.00 32.03  ? 43  HIS A CB  1 
ATOM   317   C  CG  . HIS A  1 44  ? 40.380  265.911 9.503   1.00 38.65  ? 43  HIS A CG  1 
ATOM   318   N  ND1 . HIS A  1 44  ? 39.536  266.602 8.651   1.00 36.10  ? 43  HIS A ND1 1 
ATOM   319   C  CD2 . HIS A  1 44  ? 41.459  265.559 8.750   1.00 37.84  ? 43  HIS A CD2 1 
ATOM   320   C  CE1 . HIS A  1 44  ? 40.062  266.628 7.438   1.00 36.07  ? 43  HIS A CE1 1 
ATOM   321   N  NE2 . HIS A  1 44  ? 41.214  265.987 7.467   1.00 37.37  ? 43  HIS A NE2 1 
ATOM   322   N  N   . GLY A  1 45  ? 39.188  267.479 13.674  1.00 30.40  ? 44  GLY A N   1 
ATOM   323   C  CA  . GLY A  1 45  ? 38.513  267.373 14.968  1.00 34.72  ? 44  GLY A CA  1 
ATOM   324   C  C   . GLY A  1 45  ? 37.830  266.037 15.113  1.00 32.84  ? 44  GLY A C   1 
ATOM   325   O  O   . GLY A  1 45  ? 37.227  265.569 14.167  1.00 33.91  ? 44  GLY A O   1 
ATOM   326   N  N   . PHE A  1 46  ? 38.026  265.412 16.264  1.00 32.62  ? 45  PHE A N   1 
ATOM   327   C  CA  . PHE A  1 46  ? 37.580  264.052 16.578  1.00 32.97  ? 45  PHE A CA  1 
ATOM   328   C  C   . PHE A  1 46  ? 36.897  264.123 17.943  1.00 33.95  ? 45  PHE A C   1 
ATOM   329   O  O   . PHE A  1 46  ? 37.551  264.227 18.971  1.00 32.27  ? 45  PHE A O   1 
ATOM   330   C  CB  . PHE A  1 46  ? 38.792  263.210 16.681  1.00 31.95  ? 45  PHE A CB  1 
ATOM   331   C  CG  . PHE A  1 46  ? 38.543  261.773 16.680  1.00 34.77  ? 45  PHE A CG  1 
ATOM   332   C  CD1 . PHE A  1 46  ? 37.944  261.158 15.567  1.00 34.14  ? 45  PHE A CD1 1 
ATOM   333   C  CD2 . PHE A  1 46  ? 39.015  260.962 17.754  1.00 34.00  ? 45  PHE A CD2 1 
ATOM   334   C  CE1 . PHE A  1 46  ? 37.781  259.770 15.527  1.00 31.42  ? 45  PHE A CE1 1 
ATOM   335   C  CE2 . PHE A  1 46  ? 38.884  259.567 17.717  1.00 31.45  ? 45  PHE A CE2 1 
ATOM   336   C  CZ  . PHE A  1 46  ? 38.252  258.983 16.592  1.00 36.14  ? 45  PHE A CZ  1 
ATOM   337   N  N   . HIS A  1 47  ? 35.572  264.117 17.928  1.00 32.06  ? 46  HIS A N   1 
ATOM   338   C  CA  . HIS A  1 47  ? 34.771  264.354 19.125  1.00 32.59  ? 46  HIS A CA  1 
ATOM   339   C  C   . HIS A  1 47  ? 33.652  263.380 19.339  1.00 32.20  ? 46  HIS A C   1 
ATOM   340   O  O   . HIS A  1 47  ? 33.046  262.883 18.403  1.00 32.61  ? 46  HIS A O   1 
ATOM   341   C  CB  . HIS A  1 47  ? 34.122  265.721 19.063  1.00 31.46  ? 46  HIS A CB  1 
ATOM   342   C  CG  . HIS A  1 47  ? 35.079  266.802 18.758  1.00 37.44  ? 46  HIS A CG  1 
ATOM   343   N  ND1 . HIS A  1 47  ? 34.880  267.691 17.732  1.00 39.40  ? 46  HIS A ND1 1 
ATOM   344   C  CD2 . HIS A  1 47  ? 36.281  267.104 19.302  1.00 36.74  ? 46  HIS A CD2 1 
ATOM   345   C  CE1 . HIS A  1 47  ? 35.885  268.543 17.702  1.00 39.14  ? 46  HIS A CE1 1 
ATOM   346   N  NE2 . HIS A  1 47  ? 36.759  268.191 18.628  1.00 38.62  ? 46  HIS A NE2 1 
ATOM   347   N  N   . VAL A  1 48  ? 33.344  263.159 20.595  1.00 30.22  ? 47  VAL A N   1 
ATOM   348   C  CA  . VAL A  1 48  ? 32.164  262.418 20.913  1.00 29.53  ? 47  VAL A CA  1 
ATOM   349   C  C   . VAL A  1 48  ? 31.114  263.468 21.179  1.00 29.13  ? 47  VAL A C   1 
ATOM   350   O  O   . VAL A  1 48  ? 31.277  264.297 22.112  1.00 29.58  ? 47  VAL A O   1 
ATOM   351   C  CB  . VAL A  1 48  ? 32.403  261.571 22.170  1.00 29.66  ? 47  VAL A CB  1 
ATOM   352   C  CG1 . VAL A  1 48  ? 31.114  260.941 22.614  1.00 27.35  ? 47  VAL A CG1 1 
ATOM   353   C  CG2 . VAL A  1 48  ? 33.532  260.559 21.992  1.00 27.94  ? 47  VAL A CG2 1 
ATOM   354   N  N   . HIS A  1 49  ? 30.055  263.435 20.391  1.00 28.57  ? 48  HIS A N   1 
ATOM   355   C  CA  . HIS A  1 49  ? 28.887  264.344 20.600  1.00 32.06  ? 48  HIS A CA  1 
ATOM   356   C  C   . HIS A  1 49  ? 27.813  263.736 21.497  1.00 32.63  ? 48  HIS A C   1 
ATOM   357   O  O   . HIS A  1 49  ? 27.778  262.532 21.683  1.00 35.71  ? 48  HIS A O   1 
ATOM   358   C  CB  . HIS A  1 49  ? 28.293  264.876 19.273  1.00 27.98  ? 48  HIS A CB  1 
ATOM   359   C  CG  . HIS A  1 49  ? 29.262  265.726 18.492  1.00 28.48  ? 48  HIS A CG  1 
ATOM   360   N  ND1 . HIS A  1 49  ? 29.000  267.022 18.131  1.00 27.55  ? 48  HIS A ND1 1 
ATOM   361   C  CD2 . HIS A  1 49  ? 30.518  265.459 18.052  1.00 28.58  ? 48  HIS A CD2 1 
ATOM   362   C  CE1 . HIS A  1 49  ? 30.047  267.494 17.472  1.00 32.78  ? 48  HIS A CE1 1 
ATOM   363   N  NE2 . HIS A  1 49  ? 30.977  266.557 17.402  1.00 27.05  ? 48  HIS A NE2 1 
ATOM   364   N  N   . GLU A  1 50  ? 26.939  264.558 22.043  1.00 33.91  ? 49  GLU A N   1 
ATOM   365   C  CA  . GLU A  1 50  ? 25.983  264.124 23.082  1.00 34.30  ? 49  GLU A CA  1 
ATOM   366   C  C   . GLU A  1 50  ? 24.960  262.993 22.736  1.00 33.80  ? 49  GLU A C   1 
ATOM   367   O  O   . GLU A  1 50  ? 24.780  262.102 23.569  1.00 33.16  ? 49  GLU A O   1 
ATOM   368   C  CB  . GLU A  1 50  ? 25.181  265.325 23.607  1.00 33.99  ? 49  GLU A CB  1 
ATOM   369   C  CG  . GLU A  1 50  ? 24.620  265.032 24.970  1.00 36.95  ? 49  GLU A CG  1 
ATOM   370   C  CD  . GLU A  1 50  ? 23.793  266.126 25.636  1.00 40.97  ? 49  GLU A CD  1 
ATOM   371   O  OE1 . GLU A  1 50  ? 23.654  267.279 25.118  1.00 39.28  ? 49  GLU A OE1 1 
ATOM   372   O  OE2 . GLU A  1 50  ? 23.231  265.745 26.723  1.00 41.61  ? 49  GLU A OE2 1 
ATOM   373   N  N   . PHE A  1 51  ? 24.291  263.092 21.580  1.00 27.85  ? 50  PHE A N   1 
ATOM   374   C  CA  . PHE A  1 51  ? 23.208  262.224 21.187  1.00 30.02  ? 50  PHE A CA  1 
ATOM   375   C  C   . PHE A  1 51  ? 23.599  261.233 20.153  1.00 31.26  ? 50  PHE A C   1 
ATOM   376   O  O   . PHE A  1 51  ? 24.278  261.577 19.222  1.00 36.33  ? 50  PHE A O   1 
ATOM   377   C  CB  . PHE A  1 51  ? 21.990  263.040 20.753  1.00 29.18  ? 50  PHE A CB  1 
ATOM   378   C  CG  . PHE A  1 51  ? 21.579  264.088 21.801  1.00 33.45  ? 50  PHE A CG  1 
ATOM   379   C  CD1 . PHE A  1 51  ? 21.175  263.699 23.079  1.00 33.23  ? 50  PHE A CD1 1 
ATOM   380   C  CD2 . PHE A  1 51  ? 21.591  265.463 21.504  1.00 33.67  ? 50  PHE A CD2 1 
ATOM   381   C  CE1 . PHE A  1 51  ? 20.855  264.645 24.034  1.00 33.84  ? 50  PHE A CE1 1 
ATOM   382   C  CE2 . PHE A  1 51  ? 21.224  266.406 22.438  1.00 34.18  ? 50  PHE A CE2 1 
ATOM   383   C  CZ  . PHE A  1 51  ? 20.872  265.994 23.720  1.00 35.36  ? 50  PHE A CZ  1 
ATOM   384   N  N   . GLY A  1 52  ? 23.235  259.976 20.339  1.00 29.81  ? 51  GLY A N   1 
ATOM   385   C  CA  . GLY A  1 52  ? 23.389  258.994 19.258  1.00 28.27  ? 51  GLY A CA  1 
ATOM   386   C  C   . GLY A  1 52  ? 22.226  258.989 18.322  1.00 28.63  ? 51  GLY A C   1 
ATOM   387   O  O   . GLY A  1 52  ? 21.593  257.980 18.123  1.00 31.32  ? 51  GLY A O   1 
ATOM   388   N  N   . ASP A  1 53  ? 21.953  260.134 17.752  1.00 32.13  ? 52  ASP A N   1 
ATOM   389   C  CA  . ASP A  1 53  ? 20.755  260.373 16.954  1.00 33.92  ? 52  ASP A CA  1 
ATOM   390   C  C   . ASP A  1 53  ? 21.161  260.843 15.576  1.00 34.50  ? 52  ASP A C   1 
ATOM   391   O  O   . ASP A  1 53  ? 21.729  261.904 15.426  1.00 38.10  ? 52  ASP A O   1 
ATOM   392   C  CB  . ASP A  1 53  ? 19.871  261.430 17.637  1.00 33.16  ? 52  ASP A CB  1 
ATOM   393   C  CG  . ASP A  1 53  ? 18.618  261.854 16.811  1.00 34.36  ? 52  ASP A CG  1 
ATOM   394   O  OD1 . ASP A  1 53  ? 18.502  261.646 15.578  1.00 36.03  ? 52  ASP A OD1 1 
ATOM   395   O  OD2 . ASP A  1 53  ? 17.731  262.457 17.445  1.00 35.98  ? 52  ASP A OD2 1 
ATOM   396   N  N   . ASN A  1 54  ? 20.794  260.065 14.580  1.00 34.05  ? 53  ASN A N   1 
ATOM   397   C  CA  . ASN A  1 54  ? 21.279  260.229 13.249  1.00 33.69  ? 53  ASN A CA  1 
ATOM   398   C  C   . ASN A  1 54  ? 20.144  260.490 12.302  1.00 31.27  ? 53  ASN A C   1 
ATOM   399   O  O   . ASN A  1 54  ? 20.336  260.430 11.094  1.00 33.16  ? 53  ASN A O   1 
ATOM   400   C  CB  . ASN A  1 54  ? 22.114  259.007 12.885  1.00 36.49  ? 53  ASN A CB  1 
ATOM   401   C  CG  . ASN A  1 54  ? 22.903  259.153 11.559  1.00 45.99  ? 53  ASN A CG  1 
ATOM   402   O  OD1 . ASN A  1 54  ? 23.532  260.177 11.275  1.00 49.92  ? 53  ASN A OD1 1 
ATOM   403   N  ND2 . ASN A  1 54  ? 22.866  258.094 10.723  1.00 48.73  ? 53  ASN A ND2 1 
ATOM   404   N  N   . THR A  1 55  ? 18.980  260.868 12.854  1.00 33.68  ? 54  THR A N   1 
ATOM   405   C  CA  . THR A  1 55  ? 17.734  261.056 12.081  1.00 33.23  ? 54  THR A CA  1 
ATOM   406   C  C   . THR A  1 55  ? 17.830  262.135 11.067  1.00 36.27  ? 54  THR A C   1 
ATOM   407   O  O   . THR A  1 55  ? 17.089  262.150 10.116  1.00 34.49  ? 54  THR A O   1 
ATOM   408   C  CB  . THR A  1 55  ? 16.483  261.355 12.939  1.00 34.37  ? 54  THR A CB  1 
ATOM   409   O  OG1 . THR A  1 55  ? 16.700  262.496 13.746  1.00 33.14  ? 54  THR A OG1 1 
ATOM   410   C  CG2 . THR A  1 55  ? 16.090  260.159 13.838  1.00 35.72  ? 54  THR A CG2 1 
ATOM   411   N  N   . ALA A  1 56  ? 18.726  263.078 11.306  1.00 38.32  ? 55  ALA A N   1 
ATOM   412   C  CA  . ALA A  1 56  ? 18.992  264.162 10.361  1.00 39.36  ? 55  ALA A CA  1 
ATOM   413   C  C   . ALA A  1 56  ? 20.517  264.188 10.052  1.00 40.33  ? 55  ALA A C   1 
ATOM   414   O  O   . ALA A  1 56  ? 21.140  265.232 10.094  1.00 43.41  ? 55  ALA A O   1 
ATOM   415   C  CB  . ALA A  1 56  ? 18.482  265.495 10.943  1.00 33.02  ? 55  ALA A CB  1 
ATOM   416   N  N   . GLY A  1 57  ? 21.108  263.019 9.764   1.00 38.28  ? 56  GLY A N   1 
ATOM   417   C  CA  . GLY A  1 57  ? 22.540  262.882 9.629   1.00 31.67  ? 56  GLY A CA  1 
ATOM   418   C  C   . GLY A  1 57  ? 23.310  263.256 10.878  1.00 36.40  ? 56  GLY A C   1 
ATOM   419   O  O   . GLY A  1 57  ? 22.806  263.154 12.027  1.00 34.70  ? 56  GLY A O   1 
ATOM   420   N  N   . CYS A  1 58  ? 24.531  263.748 10.667  1.00 37.91  ? 57  CYS A N   1 
ATOM   421   C  CA  . CYS A  1 58  ? 25.436  264.098 11.786  1.00 34.98  ? 57  CYS A CA  1 
ATOM   422   C  C   . CYS A  1 58  ? 24.987  265.276 12.671  1.00 36.08  ? 57  CYS A C   1 
ATOM   423   O  O   . CYS A  1 58  ? 25.435  265.401 13.813  1.00 34.91  ? 57  CYS A O   1 
ATOM   424   C  CB  . CYS A  1 58  ? 26.845  264.259 11.260  1.00 35.83  ? 57  CYS A CB  1 
ATOM   425   S  SG  . CYS A  1 58  ? 27.608  262.748 10.543  1.00 44.34  ? 57  CYS A SG  1 
ATOM   426   N  N   . THR A  1 59  ? 24.050  266.092 12.169  1.00 34.74  ? 58  THR A N   1 
ATOM   427   C  CA  . THR A  1 59  ? 23.615  267.362 12.806  1.00 34.38  ? 58  THR A CA  1 
ATOM   428   C  C   . THR A  1 59  ? 22.894  267.015 14.060  1.00 37.61  ? 58  THR A C   1 
ATOM   429   O  O   . THR A  1 59  ? 22.990  267.737 15.022  1.00 42.04  ? 58  THR A O   1 
ATOM   430   C  CB  . THR A  1 59  ? 22.639  268.152 11.869  1.00 35.08  ? 58  THR A CB  1 
ATOM   431   O  OG1 . THR A  1 59  ? 23.304  268.416 10.653  1.00 42.78  ? 58  THR A OG1 1 
ATOM   432   C  CG2 . THR A  1 59  ? 22.176  269.462 12.384  1.00 27.84  ? 58  THR A CG2 1 
ATOM   433   N  N   . SER A  1 60  ? 22.157  265.900 14.049  1.00 41.66  ? 59  SER A N   1 
ATOM   434   C  CA  . SER A  1 60  ? 21.259  265.580 15.133  1.00 35.49  ? 59  SER A CA  1 
ATOM   435   C  C   . SER A  1 60  ? 21.983  264.936 16.311  1.00 34.12  ? 59  SER A C   1 
ATOM   436   O  O   . SER A  1 60  ? 21.379  264.736 17.330  1.00 31.81  ? 59  SER A O   1 
ATOM   437   C  CB  . SER A  1 60  ? 20.022  264.830 14.642  1.00 36.87  ? 59  SER A CB  1 
ATOM   438   O  OG  . SER A  1 60  ? 20.338  263.818 13.741  1.00 41.59  ? 59  SER A OG  1 
ATOM   439   N  N   . ALA A  1 61  ? 23.293  264.698 16.191  1.00 33.41  ? 60  ALA A N   1 
ATOM   440   C  CA  . ALA A  1 61  ? 24.113  264.367 17.378  1.00 30.32  ? 60  ALA A CA  1 
ATOM   441   C  C   . ALA A  1 61  ? 24.198  265.482 18.418  1.00 33.11  ? 60  ALA A C   1 
ATOM   442   O  O   . ALA A  1 61  ? 24.488  265.196 19.554  1.00 34.48  ? 60  ALA A O   1 
ATOM   443   C  CB  . ALA A  1 61  ? 25.463  263.915 16.981  1.00 23.16  ? 60  ALA A CB  1 
ATOM   444   N  N   . GLY A  1 62  ? 23.920  266.754 18.051  1.00 35.60  ? 61  GLY A N   1 
ATOM   445   C  CA  . GLY A  1 62  ? 24.050  267.850 18.991  1.00 33.05  ? 61  GLY A CA  1 
ATOM   446   C  C   . GLY A  1 62  ? 25.479  268.214 19.340  1.00 34.49  ? 61  GLY A C   1 
ATOM   447   O  O   . GLY A  1 62  ? 26.432  267.919 18.603  1.00 35.73  ? 61  GLY A O   1 
ATOM   448   N  N   . PRO A  1 63  ? 25.663  268.865 20.484  1.00 36.35  ? 62  PRO A N   1 
ATOM   449   C  CA  . PRO A  1 63  ? 26.979  269.482 20.785  1.00 35.40  ? 62  PRO A CA  1 
ATOM   450   C  C   . PRO A  1 63  ? 27.920  268.447 21.334  1.00 35.56  ? 62  PRO A C   1 
ATOM   451   O  O   . PRO A  1 63  ? 27.572  267.258 21.403  1.00 37.03  ? 62  PRO A O   1 
ATOM   452   C  CB  . PRO A  1 63  ? 26.635  270.494 21.868  1.00 33.97  ? 62  PRO A CB  1 
ATOM   453   C  CG  . PRO A  1 63  ? 25.266  270.112 22.384  1.00 34.76  ? 62  PRO A CG  1 
ATOM   454   C  CD  . PRO A  1 63  ? 24.772  268.912 21.649  1.00 34.45  ? 62  PRO A CD  1 
ATOM   455   N  N   . HIS A  1 64  ? 29.082  268.863 21.780  1.00 35.42  ? 63  HIS A N   1 
ATOM   456   C  CA  . HIS A  1 64  ? 30.051  267.882 22.264  1.00 34.39  ? 63  HIS A CA  1 
ATOM   457   C  C   . HIS A  1 64  ? 29.508  267.224 23.551  1.00 33.66  ? 63  HIS A C   1 
ATOM   458   O  O   . HIS A  1 64  ? 28.833  267.863 24.317  1.00 35.05  ? 63  HIS A O   1 
ATOM   459   C  CB  . HIS A  1 64  ? 31.379  268.590 22.517  1.00 32.91  ? 63  HIS A CB  1 
ATOM   460   C  CG  . HIS A  1 64  ? 32.114  269.014 21.266  1.00 41.81  ? 63  HIS A CG  1 
ATOM   461   N  ND1 . HIS A  1 64  ? 33.394  269.528 21.288  1.00 41.98  ? 63  HIS A ND1 1 
ATOM   462   C  CD2 . HIS A  1 64  ? 31.768  268.977 19.951  1.00 46.35  ? 63  HIS A CD2 1 
ATOM   463   C  CE1 . HIS A  1 64  ? 33.810  269.767 20.055  1.00 45.18  ? 63  HIS A CE1 1 
ATOM   464   N  NE2 . HIS A  1 64  ? 32.838  269.446 19.223  1.00 44.00  ? 63  HIS A NE2 1 
ATOM   465   N  N   . PHE A  1 65  ? 29.787  265.954 23.797  1.00 34.56  ? 64  PHE A N   1 
ATOM   466   C  CA  . PHE A  1 65  ? 29.387  265.358 25.068  1.00 34.52  ? 64  PHE A CA  1 
ATOM   467   C  C   . PHE A  1 65  ? 30.114  266.080 26.217  1.00 36.59  ? 64  PHE A C   1 
ATOM   468   O  O   . PHE A  1 65  ? 31.361  266.034 26.362  1.00 34.46  ? 64  PHE A O   1 
ATOM   469   C  CB  . PHE A  1 65  ? 29.575  263.802 25.053  1.00 33.65  ? 64  PHE A CB  1 
ATOM   470   C  CG  . PHE A  1 65  ? 29.245  263.090 26.362  1.00 29.75  ? 64  PHE A CG  1 
ATOM   471   C  CD1 . PHE A  1 65  ? 28.027  263.289 27.035  1.00 30.63  ? 64  PHE A CD1 1 
ATOM   472   C  CD2 . PHE A  1 65  ? 30.115  262.158 26.873  1.00 29.41  ? 64  PHE A CD2 1 
ATOM   473   C  CE1 . PHE A  1 65  ? 27.752  262.631 28.240  1.00 29.61  ? 64  PHE A CE1 1 
ATOM   474   C  CE2 . PHE A  1 65  ? 29.829  261.478 28.067  1.00 27.76  ? 64  PHE A CE2 1 
ATOM   475   C  CZ  . PHE A  1 65  ? 28.664  261.717 28.733  1.00 27.52  ? 64  PHE A CZ  1 
ATOM   476   N  N   . ASN A  1 66  ? 29.288  266.732 27.022  1.00 37.18  ? 65  ASN A N   1 
ATOM   477   C  CA  . ASN A  1 66  ? 29.720  267.600 28.054  1.00 37.94  ? 65  ASN A CA  1 
ATOM   478   C  C   . ASN A  1 66  ? 28.950  267.391 29.411  1.00 38.45  ? 65  ASN A C   1 
ATOM   479   O  O   . ASN A  1 66  ? 28.206  268.262 29.949  1.00 37.82  ? 65  ASN A O   1 
ATOM   480   C  CB  . ASN A  1 66  ? 29.573  268.992 27.486  1.00 40.29  ? 65  ASN A CB  1 
ATOM   481   C  CG  . ASN A  1 66  ? 30.195  270.033 28.360  1.00 42.19  ? 65  ASN A CG  1 
ATOM   482   O  OD1 . ASN A  1 66  ? 31.064  269.730 29.213  1.00 40.52  ? 65  ASN A OD1 1 
ATOM   483   N  ND2 . ASN A  1 66  ? 29.753  271.276 28.173  1.00 38.47  ? 65  ASN A ND2 1 
ATOM   484   N  N   . PRO A  1 67  ? 29.096  266.216 29.984  1.00 38.85  ? 66  PRO A N   1 
ATOM   485   C  CA  . PRO A  1 67  ? 28.217  266.047 31.148  1.00 39.65  ? 66  PRO A CA  1 
ATOM   486   C  C   . PRO A  1 67  ? 28.573  266.955 32.342  1.00 47.07  ? 66  PRO A C   1 
ATOM   487   O  O   . PRO A  1 67  ? 27.710  267.165 33.160  1.00 45.52  ? 66  PRO A O   1 
ATOM   488   C  CB  . PRO A  1 67  ? 28.428  264.592 31.506  1.00 39.39  ? 66  PRO A CB  1 
ATOM   489   C  CG  . PRO A  1 67  ? 29.836  264.293 31.082  1.00 37.69  ? 66  PRO A CG  1 
ATOM   490   C  CD  . PRO A  1 67  ? 30.006  265.073 29.788  1.00 37.72  ? 66  PRO A CD  1 
ATOM   491   N  N   . LEU A  1 68  ? 29.824  267.486 32.442  1.00 52.30  ? 67  LEU A N   1 
ATOM   492   C  CA  . LEU A  1 68  ? 30.255  268.433 33.549  1.00 42.85  ? 67  LEU A CA  1 
ATOM   493   C  C   . LEU A  1 68  ? 30.173  269.935 33.232  1.00 48.94  ? 67  LEU A C   1 
ATOM   494   O  O   . LEU A  1 68  ? 30.641  270.781 33.987  1.00 51.43  ? 67  LEU A O   1 
ATOM   495   C  CB  . LEU A  1 68  ? 31.633  268.130 34.074  1.00 36.85  ? 67  LEU A CB  1 
ATOM   496   C  CG  . LEU A  1 68  ? 31.847  266.684 34.514  1.00 44.01  ? 67  LEU A CG  1 
ATOM   497   C  CD1 . LEU A  1 68  ? 33.338  266.393 34.723  1.00 38.71  ? 67  LEU A CD1 1 
ATOM   498   C  CD2 . LEU A  1 68  ? 30.967  266.268 35.722  1.00 45.12  ? 67  LEU A CD2 1 
ATOM   499   N  N   . SER A  1 69  ? 29.538  270.293 32.136  1.00 49.55  ? 68  SER A N   1 
ATOM   500   C  CA  . SER A  1 69  ? 29.284  271.693 31.856  1.00 51.02  ? 68  SER A CA  1 
ATOM   501   C  C   . SER A  1 69  ? 30.517  272.538 31.872  1.00 49.94  ? 68  SER A C   1 
ATOM   502   O  O   . SER A  1 69  ? 30.558  273.493 32.591  1.00 52.64  ? 68  SER A O   1 
ATOM   503   C  CB  . SER A  1 69  ? 28.253  272.241 32.837  1.00 48.79  ? 68  SER A CB  1 
ATOM   504   O  OG  . SER A  1 69  ? 27.034  272.273 32.103  1.00 52.90  ? 68  SER A OG  1 
ATOM   505   N  N   . ARG A  1 70  ? 31.535  272.146 31.113  1.00 49.19  ? 69  ARG A N   1 
ATOM   506   C  CA  . ARG A  1 70  ? 32.799  272.891 31.023  1.00 43.74  ? 69  ARG A CA  1 
ATOM   507   C  C   . ARG A  1 70  ? 32.981  273.417 29.598  1.00 43.99  ? 69  ARG A C   1 
ATOM   508   O  O   . ARG A  1 70  ? 32.047  273.346 28.754  1.00 42.93  ? 69  ARG A O   1 
ATOM   509   C  CB  . ARG A  1 70  ? 33.988  272.026 31.507  1.00 43.16  ? 69  ARG A CB  1 
ATOM   510   C  CG  . ARG A  1 70  ? 33.699  271.447 32.892  1.00 49.22  ? 69  ARG A CG  1 
ATOM   511   C  CD  . ARG A  1 70  ? 34.884  271.483 33.862  1.00 59.35  ? 69  ARG A CD  1 
ATOM   512   N  NE  . ARG A  1 70  ? 34.927  270.275 34.744  1.00 66.09  ? 69  ARG A NE  1 
ATOM   513   C  CZ  . ARG A  1 70  ? 36.022  269.506 34.953  1.00 76.64  ? 69  ARG A CZ  1 
ATOM   514   N  NH1 . ARG A  1 70  ? 37.184  269.803 34.364  1.00 73.85  ? 69  ARG A NH1 1 
ATOM   515   N  NH2 . ARG A  1 70  ? 35.997  268.434 35.762  1.00 63.28  ? 69  ARG A NH2 1 
ATOM   516   N  N   . LYS A  1 71  ? 34.168  273.961 29.330  1.00 44.77  ? 70  LYS A N   1 
ATOM   517   C  CA  . LYS A  1 71  ? 34.453  274.588 28.046  1.00 48.23  ? 70  LYS A CA  1 
ATOM   518   C  C   . LYS A  1 71  ? 35.336  273.698 27.202  1.00 48.74  ? 70  LYS A C   1 
ATOM   519   O  O   . LYS A  1 71  ? 36.148  272.893 27.747  1.00 44.70  ? 70  LYS A O   1 
ATOM   520   C  CB  . LYS A  1 71  ? 35.154  275.903 28.276  1.00 53.65  ? 70  LYS A CB  1 
ATOM   521   C  CG  . LYS A  1 71  ? 34.205  276.913 28.887  1.00 60.40  ? 70  LYS A CG  1 
ATOM   522   C  CD  . LYS A  1 71  ? 34.938  278.169 29.252  1.00 59.81  ? 70  LYS A CD  1 
ATOM   523   C  CE  . LYS A  1 71  ? 33.856  279.178 29.516  1.00 83.13  ? 70  LYS A CE  1 
ATOM   524   N  NZ  . LYS A  1 71  ? 34.509  280.523 29.545  1.00 104.41 ? 70  LYS A NZ  1 
ATOM   525   N  N   . HIS A  1 72  ? 35.233  273.861 25.881  1.00 38.93  ? 71  HIS A N   1 
ATOM   526   C  CA  . HIS A  1 72  ? 35.996  272.987 25.032  1.00 37.23  ? 71  HIS A CA  1 
ATOM   527   C  C   . HIS A  1 72  ? 37.507  273.048 25.375  1.00 38.66  ? 71  HIS A C   1 
ATOM   528   O  O   . HIS A  1 72  ? 38.001  274.106 25.701  1.00 38.41  ? 71  HIS A O   1 
ATOM   529   C  CB  . HIS A  1 72  ? 35.719  273.357 23.612  1.00 36.16  ? 71  HIS A CB  1 
ATOM   530   C  CG  . HIS A  1 72  ? 36.497  272.559 22.655  1.00 35.47  ? 71  HIS A CG  1 
ATOM   531   N  ND1 . HIS A  1 72  ? 36.180  271.270 22.360  1.00 39.29  ? 71  HIS A ND1 1 
ATOM   532   C  CD2 . HIS A  1 72  ? 37.616  272.830 21.965  1.00 37.32  ? 71  HIS A CD2 1 
ATOM   533   C  CE1 . HIS A  1 72  ? 37.078  270.763 21.540  1.00 37.00  ? 71  HIS A CE1 1 
ATOM   534   N  NE2 . HIS A  1 72  ? 37.958  271.696 21.276  1.00 37.99  ? 71  HIS A NE2 1 
ATOM   535   N  N   . GLY A  1 73  ? 38.224  271.927 25.314  1.00 37.04  ? 72  GLY A N   1 
ATOM   536   C  CA  . GLY A  1 73  ? 39.652  271.952 25.482  1.00 34.09  ? 72  GLY A CA  1 
ATOM   537   C  C   . GLY A  1 73  ? 40.256  270.880 24.602  1.00 40.26  ? 72  GLY A C   1 
ATOM   538   O  O   . GLY A  1 73  ? 39.525  270.239 23.825  1.00 38.96  ? 72  GLY A O   1 
ATOM   539   N  N   . GLY A  1 74  ? 41.584  270.687 24.746  1.00 39.00  ? 73  GLY A N   1 
ATOM   540   C  CA  . GLY A  1 74  ? 42.349  269.556 24.198  1.00 38.06  ? 73  GLY A CA  1 
ATOM   541   C  C   . GLY A  1 74  ? 42.159  268.406 25.164  1.00 41.41  ? 73  GLY A C   1 
ATOM   542   O  O   . GLY A  1 74  ? 41.720  268.647 26.302  1.00 40.08  ? 73  GLY A O   1 
ATOM   543   N  N   . PRO A  1 75  ? 42.420  267.134 24.720  1.00 40.68  ? 74  PRO A N   1 
ATOM   544   C  CA  . PRO A  1 75  ? 42.306  266.070 25.661  1.00 39.60  ? 74  PRO A CA  1 
ATOM   545   C  C   . PRO A  1 75  ? 43.276  266.223 26.850  1.00 43.46  ? 74  PRO A C   1 
ATOM   546   O  O   . PRO A  1 75  ? 42.948  265.694 27.934  1.00 43.62  ? 74  PRO A O   1 
ATOM   547   C  CB  . PRO A  1 75  ? 42.696  264.833 24.839  1.00 38.58  ? 74  PRO A CB  1 
ATOM   548   C  CG  . PRO A  1 75  ? 43.417  265.367 23.631  1.00 32.43  ? 74  PRO A CG  1 
ATOM   549   C  CD  . PRO A  1 75  ? 42.652  266.593 23.369  1.00 35.13  ? 74  PRO A CD  1 
ATOM   550   N  N   . LYS A  1 76  ? 44.437  266.903 26.689  1.00 43.29  ? 75  LYS A N   1 
ATOM   551   C  CA  . LYS A  1 76  ? 45.413  266.945 27.829  1.00 42.27  ? 75  LYS A CA  1 
ATOM   552   C  C   . LYS A  1 76  ? 45.036  268.036 28.870  1.00 42.63  ? 75  LYS A C   1 
ATOM   553   O  O   . LYS A  1 76  ? 45.538  268.074 29.981  1.00 44.65  ? 75  LYS A O   1 
ATOM   554   C  CB  . LYS A  1 76  ? 46.875  266.951 27.406  1.00 40.94  ? 75  LYS A CB  1 
ATOM   555   C  CG  . LYS A  1 76  ? 47.255  266.169 26.123  1.00 48.04  ? 75  LYS A CG  1 
ATOM   556   C  CD  . LYS A  1 76  ? 47.622  264.682 26.306  1.00 51.33  ? 75  LYS A CD  1 
ATOM   557   C  CE  . LYS A  1 76  ? 48.935  264.297 25.529  1.00 61.65  ? 75  LYS A CE  1 
ATOM   558   N  NZ  . LYS A  1 76  ? 48.927  263.580 24.153  1.00 46.35  ? 75  LYS A NZ  1 
ATOM   559   N  N   . ASP A  1 77  ? 44.081  268.873 28.515  1.00 39.29  ? 76  ASP A N   1 
ATOM   560   C  CA  . ASP A  1 77  ? 43.534  269.836 29.431  1.00 44.23  ? 76  ASP A CA  1 
ATOM   561   C  C   . ASP A  1 77  ? 42.669  269.311 30.533  1.00 50.63  ? 76  ASP A C   1 
ATOM   562   O  O   . ASP A  1 77  ? 42.089  268.210 30.469  1.00 52.96  ? 76  ASP A O   1 
ATOM   563   C  CB  . ASP A  1 77  ? 42.738  270.941 28.669  1.00 47.73  ? 76  ASP A CB  1 
ATOM   564   C  CG  . ASP A  1 77  ? 43.618  271.674 27.628  1.00 52.40  ? 76  ASP A CG  1 
ATOM   565   O  OD1 . ASP A  1 77  ? 44.838  271.883 27.937  1.00 50.48  ? 76  ASP A OD1 1 
ATOM   566   O  OD2 . ASP A  1 77  ? 43.127  271.981 26.492  1.00 49.00  ? 76  ASP A OD2 1 
ATOM   567   N  N   . GLU A  1 78  ? 42.563  270.150 31.551  1.00 49.23  ? 77  GLU A N   1 
ATOM   568   C  CA  . GLU A  1 78  ? 41.719  269.882 32.663  1.00 50.80  ? 77  GLU A CA  1 
ATOM   569   C  C   . GLU A  1 78  ? 40.362  270.519 32.363  1.00 53.29  ? 77  GLU A C   1 
ATOM   570   O  O   . GLU A  1 78  ? 39.331  269.994 32.763  1.00 53.83  ? 77  GLU A O   1 
ATOM   571   C  CB  . GLU A  1 78  ? 42.335  270.500 33.919  1.00 54.72  ? 77  GLU A CB  1 
ATOM   572   C  CG  . GLU A  1 78  ? 41.327  270.722 35.050  1.00 59.22  ? 77  GLU A CG  1 
ATOM   573   C  CD  . GLU A  1 78  ? 41.004  269.383 35.750  1.00 78.64  ? 77  GLU A CD  1 
ATOM   574   O  OE1 . GLU A  1 78  ? 41.981  268.565 35.883  1.00 83.75  ? 77  GLU A OE1 1 
ATOM   575   O  OE2 . GLU A  1 78  ? 39.808  269.107 36.140  1.00 69.89  ? 77  GLU A OE2 1 
ATOM   576   N  N   . GLU A  1 79  ? 40.362  271.652 31.670  1.00 46.89  ? 78  GLU A N   1 
ATOM   577   C  CA  . GLU A  1 79  ? 39.113  272.291 31.313  1.00 45.41  ? 78  GLU A CA  1 
ATOM   578   C  C   . GLU A  1 79  ? 38.787  271.765 29.877  1.00 49.60  ? 78  GLU A C   1 
ATOM   579   O  O   . GLU A  1 79  ? 39.266  272.264 28.855  1.00 47.41  ? 78  GLU A O   1 
ATOM   580   C  CB  . GLU A  1 79  ? 39.247  273.825 31.502  1.00 42.38  ? 78  GLU A CB  1 
ATOM   581   C  CG  . GLU A  1 79  ? 38.042  274.685 31.139  1.00 46.54  ? 78  GLU A CG  1 
ATOM   582   C  CD  . GLU A  1 79  ? 36.827  274.573 32.071  1.00 56.70  ? 78  GLU A CD  1 
ATOM   583   O  OE1 . GLU A  1 79  ? 36.910  274.031 33.235  1.00 56.76  ? 78  GLU A OE1 1 
ATOM   584   O  OE2 . GLU A  1 79  ? 35.733  275.038 31.615  1.00 57.38  ? 78  GLU A OE2 1 
ATOM   585   N  N   . ARG A  1 80  ? 38.049  270.662 29.829  1.00 49.27  ? 79  ARG A N   1 
ATOM   586   C  CA  . ARG A  1 80  ? 37.624  270.025 28.547  1.00 43.31  ? 79  ARG A CA  1 
ATOM   587   C  C   . ARG A  1 80  ? 36.288  269.375 28.772  1.00 39.96  ? 79  ARG A C   1 
ATOM   588   O  O   . ARG A  1 80  ? 36.024  268.930 29.881  1.00 44.64  ? 79  ARG A O   1 
ATOM   589   C  CB  . ARG A  1 80  ? 38.593  268.917 28.111  1.00 39.03  ? 79  ARG A CB  1 
ATOM   590   C  CG  . ARG A  1 80  ? 38.753  267.850 29.166  1.00 36.91  ? 79  ARG A CG  1 
ATOM   591   C  CD  . ARG A  1 80  ? 39.580  266.705 28.644  1.00 39.26  ? 79  ARG A CD  1 
ATOM   592   N  NE  . ARG A  1 80  ? 38.766  265.702 27.953  1.00 39.49  ? 79  ARG A NE  1 
ATOM   593   C  CZ  . ARG A  1 80  ? 39.220  264.528 27.510  1.00 37.21  ? 79  ARG A CZ  1 
ATOM   594   N  NH1 . ARG A  1 80  ? 40.468  264.132 27.692  1.00 36.79  ? 79  ARG A NH1 1 
ATOM   595   N  NH2 . ARG A  1 80  ? 38.395  263.697 26.920  1.00 39.05  ? 79  ARG A NH2 1 
ATOM   596   N  N   . HIS A  1 81  ? 35.465  269.333 27.732  1.00 38.97  ? 80  HIS A N   1 
ATOM   597   C  CA  . HIS A  1 81  ? 34.364  268.359 27.542  1.00 34.54  ? 80  HIS A CA  1 
ATOM   598   C  C   . HIS A  1 81  ? 34.837  266.896 27.686  1.00 32.72  ? 80  HIS A C   1 
ATOM   599   O  O   . HIS A  1 81  ? 35.987  266.555 27.238  1.00 35.94  ? 80  HIS A O   1 
ATOM   600   C  CB  . HIS A  1 81  ? 33.821  268.620 26.141  1.00 37.98  ? 80  HIS A CB  1 
ATOM   601   C  CG  . HIS A  1 81  ? 33.354  270.045 25.892  1.00 38.85  ? 80  HIS A CG  1 
ATOM   602   N  ND1 . HIS A  1 81  ? 33.229  270.573 24.623  1.00 34.87  ? 80  HIS A ND1 1 
ATOM   603   C  CD2 . HIS A  1 81  ? 32.898  271.012 26.732  1.00 40.27  ? 80  HIS A CD2 1 
ATOM   604   C  CE1 . HIS A  1 81  ? 32.706  271.780 24.676  1.00 33.57  ? 80  HIS A CE1 1 
ATOM   605   N  NE2 . HIS A  1 81  ? 32.494  272.075 25.951  1.00 37.82  ? 80  HIS A NE2 1 
ATOM   606   N  N   . VAL A  1 82  ? 34.029  266.027 28.315  1.00 30.72  ? 81  VAL A N   1 
ATOM   607   C  CA  . VAL A  1 82  ? 34.323  264.562 28.290  1.00 30.28  ? 81  VAL A CA  1 
ATOM   608   C  C   . VAL A  1 82  ? 34.588  264.128 26.845  1.00 29.28  ? 81  VAL A C   1 
ATOM   609   O  O   . VAL A  1 82  ? 35.573  263.500 26.588  1.00 29.00  ? 81  VAL A O   1 
ATOM   610   C  CB  . VAL A  1 82  ? 33.239  263.726 29.006  1.00 27.37  ? 81  VAL A CB  1 
ATOM   611   C  CG1 . VAL A  1 82  ? 33.450  262.205 28.815  1.00 24.19  ? 81  VAL A CG1 1 
ATOM   612   C  CG2 . VAL A  1 82  ? 33.295  264.081 30.481  1.00 24.76  ? 81  VAL A CG2 1 
ATOM   613   N  N   . GLY A  1 83  ? 33.748  264.594 25.921  1.00 29.74  ? 82  GLY A N   1 
ATOM   614   C  CA  . GLY A  1 83  ? 33.888  264.341 24.494  1.00 33.77  ? 82  GLY A CA  1 
ATOM   615   C  C   . GLY A  1 83  ? 35.078  264.897 23.690  1.00 35.20  ? 82  GLY A C   1 
ATOM   616   O  O   . GLY A  1 83  ? 35.134  264.710 22.454  1.00 34.59  ? 82  GLY A O   1 
ATOM   617   N  N   . ASP A  1 84  ? 36.053  265.499 24.360  1.00 34.88  ? 83  ASP A N   1 
ATOM   618   C  CA  . ASP A  1 84  ? 37.219  266.133 23.674  1.00 34.70  ? 83  ASP A CA  1 
ATOM   619   C  C   . ASP A  1 84  ? 38.362  265.240 23.379  1.00 32.37  ? 83  ASP A C   1 
ATOM   620   O  O   . ASP A  1 84  ? 39.295  265.157 24.144  1.00 38.57  ? 83  ASP A O   1 
ATOM   621   C  CB  . ASP A  1 84  ? 37.697  267.386 24.427  1.00 35.06  ? 83  ASP A CB  1 
ATOM   622   C  CG  . ASP A  1 84  ? 36.662  268.491 24.359  1.00 36.93  ? 83  ASP A CG  1 
ATOM   623   O  OD1 . ASP A  1 84  ? 35.864  268.335 23.433  1.00 35.10  ? 83  ASP A OD1 1 
ATOM   624   O  OD2 . ASP A  1 84  ? 36.595  269.482 25.138  1.00 36.94  ? 83  ASP A OD2 1 
ATOM   625   N  N   . LEU A  1 85  ? 38.331  264.581 22.249  1.00 33.59  ? 84  LEU A N   1 
ATOM   626   C  CA  . LEU A  1 85  ? 39.466  263.742 21.943  1.00 34.71  ? 84  LEU A CA  1 
ATOM   627   C  C   . LEU A  1 85  ? 40.539  264.476 21.080  1.00 35.07  ? 84  LEU A C   1 
ATOM   628   O  O   . LEU A  1 85  ? 41.456  263.851 20.581  1.00 37.35  ? 84  LEU A O   1 
ATOM   629   C  CB  . LEU A  1 85  ? 38.918  262.427 21.331  1.00 33.29  ? 84  LEU A CB  1 
ATOM   630   C  CG  . LEU A  1 85  ? 37.947  261.585 22.203  1.00 31.54  ? 84  LEU A CG  1 
ATOM   631   C  CD1 . LEU A  1 85  ? 37.618  260.239 21.602  1.00 30.31  ? 84  LEU A CD1 1 
ATOM   632   C  CD2 . LEU A  1 85  ? 38.522  261.278 23.594  1.00 32.93  ? 84  LEU A CD2 1 
ATOM   633   N  N   . GLY A  1 86  ? 40.397  265.795 20.866  1.00 33.88  ? 85  GLY A N   1 
ATOM   634   C  CA  . GLY A  1 86  ? 41.313  266.547 20.002  1.00 33.90  ? 85  GLY A CA  1 
ATOM   635   C  C   . GLY A  1 86  ? 41.282  266.231 18.529  1.00 35.11  ? 85  GLY A C   1 
ATOM   636   O  O   . GLY A  1 86  ? 40.184  266.250 17.903  1.00 35.76  ? 85  GLY A O   1 
ATOM   637   N  N   . ASN A  1 87  ? 42.457  265.955 17.957  1.00 32.52  ? 86  ASN A N   1 
ATOM   638   C  CA  . ASN A  1 87  ? 42.513  265.816 16.490  1.00 34.75  ? 86  ASN A CA  1 
ATOM   639   C  C   . ASN A  1 87  ? 43.028  264.508 16.093  1.00 36.63  ? 86  ASN A C   1 
ATOM   640   O  O   . ASN A  1 87  ? 43.870  263.935 16.789  1.00 35.31  ? 86  ASN A O   1 
ATOM   641   C  CB  . ASN A  1 87  ? 43.487  266.801 15.823  1.00 34.69  ? 86  ASN A CB  1 
ATOM   642   C  CG  . ASN A  1 87  ? 43.071  268.233 15.977  1.00 40.42  ? 86  ASN A CG  1 
ATOM   643   O  OD1 . ASN A  1 87  ? 42.247  268.733 15.218  1.00 43.88  ? 86  ASN A OD1 1 
ATOM   644   N  ND2 . ASN A  1 87  ? 43.619  268.907 16.971  1.00 40.73  ? 86  ASN A ND2 1 
ATOM   645   N  N   . VAL A  1 88  ? 42.621  264.086 14.907  1.00 35.00  ? 87  VAL A N   1 
ATOM   646   C  CA  . VAL A  1 88  ? 43.308  262.990 14.252  1.00 33.50  ? 87  VAL A CA  1 
ATOM   647   C  C   . VAL A  1 88  ? 44.027  263.572 12.998  1.00 35.41  ? 87  VAL A C   1 
ATOM   648   O  O   . VAL A  1 88  ? 43.670  264.643 12.429  1.00 32.93  ? 87  VAL A O   1 
ATOM   649   C  CB  . VAL A  1 88  ? 42.334  261.805 13.951  1.00 35.29  ? 87  VAL A CB  1 
ATOM   650   C  CG1 . VAL A  1 88  ? 41.796  261.171 15.239  1.00 30.78  ? 87  VAL A CG1 1 
ATOM   651   C  CG2 . VAL A  1 88  ? 41.175  262.270 13.047  1.00 33.89  ? 87  VAL A CG2 1 
ATOM   652   N  N   . THR A  1 89  ? 45.031  262.865 12.537  1.00 37.87  ? 88  THR A N   1 
ATOM   653   C  CA  . THR A  1 89  ? 45.807  263.377 11.392  1.00 36.47  ? 88  THR A CA  1 
ATOM   654   C  C   . THR A  1 89  ? 45.687  262.476 10.180  1.00 34.46  ? 88  THR A C   1 
ATOM   655   O  O   . THR A  1 89  ? 46.097  261.323 10.206  1.00 36.72  ? 88  THR A O   1 
ATOM   656   C  CB  . THR A  1 89  ? 47.276  263.463 11.851  1.00 36.90  ? 88  THR A CB  1 
ATOM   657   O  OG1 . THR A  1 89  ? 47.324  264.482 12.850  1.00 37.94  ? 88  THR A OG1 1 
ATOM   658   C  CG2 . THR A  1 89  ? 48.230  263.808 10.703  1.00 35.82  ? 88  THR A CG2 1 
ATOM   659   N  N   . ALA A  1 90  ? 45.163  262.989 9.098   1.00 37.06  ? 89  ALA A N   1 
ATOM   660   C  CA  . ALA A  1 90  ? 45.109  262.178 7.870   1.00 38.19  ? 89  ALA A CA  1 
ATOM   661   C  C   . ALA A  1 90  ? 46.435  262.369 7.119   1.00 40.73  ? 89  ALA A C   1 
ATOM   662   O  O   . ALA A  1 90  ? 46.977  263.493 7.005   1.00 44.26  ? 89  ALA A O   1 
ATOM   663   C  CB  . ALA A  1 90  ? 43.942  262.629 7.045   1.00 37.38  ? 89  ALA A CB  1 
ATOM   664   N  N   . ASP A  1 91  ? 46.993  261.265 6.670   1.00 41.77  ? 90  ASP A N   1 
ATOM   665   C  CA  . ASP A  1 91  ? 48.243  261.289 5.915   1.00 41.72  ? 90  ASP A CA  1 
ATOM   666   C  C   . ASP A  1 91  ? 48.048  261.777 4.455   1.00 44.35  ? 90  ASP A C   1 
ATOM   667   O  O   . ASP A  1 91  ? 47.006  262.366 4.126   1.00 49.06  ? 90  ASP A O   1 
ATOM   668   C  CB  . ASP A  1 91  ? 48.944  259.930 6.006   1.00 38.15  ? 90  ASP A CB  1 
ATOM   669   C  CG  . ASP A  1 91  ? 48.230  258.810 5.255   1.00 36.31  ? 90  ASP A CG  1 
ATOM   670   O  OD1 . ASP A  1 91  ? 47.412  259.086 4.375   1.00 34.53  ? 90  ASP A OD1 1 
ATOM   671   O  OD2 . ASP A  1 91  ? 48.554  257.621 5.537   1.00 35.63  ? 90  ASP A OD2 1 
ATOM   672   N  N   . LYS A  1 92  ? 49.021  261.555 3.578   1.00 47.23  ? 91  LYS A N   1 
ATOM   673   C  CA  . LYS A  1 92  ? 48.962  262.251 2.245   1.00 55.51  ? 91  LYS A CA  1 
ATOM   674   C  C   . LYS A  1 92  ? 48.068  261.472 1.287   1.00 47.99  ? 91  LYS A C   1 
ATOM   675   O  O   . LYS A  1 92  ? 47.505  262.040 0.338   1.00 47.10  ? 91  LYS A O   1 
ATOM   676   C  CB  . LYS A  1 92  ? 50.353  262.544 1.647   1.00 52.14  ? 91  LYS A CB  1 
ATOM   677   C  CG  . LYS A  1 92  ? 50.968  261.278 1.090   1.00 59.77  ? 91  LYS A CG  1 
ATOM   678   C  CD  . LYS A  1 92  ? 52.256  261.470 0.303   1.00 67.42  ? 91  LYS A CD  1 
ATOM   679   C  CE  . LYS A  1 92  ? 53.112  260.213 0.579   1.00 71.15  ? 91  LYS A CE  1 
ATOM   680   N  NZ  . LYS A  1 92  ? 54.570  260.367 0.230   1.00 77.80  ? 91  LYS A NZ  1 
ATOM   681   N  N   . ASP A  1 93  ? 47.913  260.185 1.594   1.00 45.99  ? 92  ASP A N   1 
ATOM   682   C  CA  . ASP A  1 93  ? 46.905  259.318 0.982   1.00 43.78  ? 92  ASP A CA  1 
ATOM   683   C  C   . ASP A  1 93  ? 45.486  259.454 1.559   1.00 40.54  ? 92  ASP A C   1 
ATOM   684   O  O   . ASP A  1 93  ? 44.674  258.596 1.313   1.00 41.15  ? 92  ASP A O   1 
ATOM   685   C  CB  . ASP A  1 93  ? 47.348  257.886 1.143   1.00 43.64  ? 92  ASP A CB  1 
ATOM   686   C  CG  . ASP A  1 93  ? 48.620  257.626 0.411   1.00 59.68  ? 92  ASP A CG  1 
ATOM   687   O  OD1 . ASP A  1 93  ? 48.821  258.250 -0.705  1.00 49.74  ? 92  ASP A OD1 1 
ATOM   688   O  OD2 . ASP A  1 93  ? 49.424  256.820 0.972   1.00 54.68  ? 92  ASP A OD2 1 
ATOM   689   N  N   . GLY A  1 94  ? 45.221  260.485 2.356   1.00 40.26  ? 93  GLY A N   1 
ATOM   690   C  CA  . GLY A  1 94  ? 43.916  260.657 3.009   1.00 44.94  ? 93  GLY A CA  1 
ATOM   691   C  C   . GLY A  1 94  ? 43.451  259.690 4.106   1.00 45.10  ? 93  GLY A C   1 
ATOM   692   O  O   . GLY A  1 94  ? 42.246  259.635 4.350   1.00 47.95  ? 93  GLY A O   1 
ATOM   693   N  N   . VAL A  1 95  ? 44.379  258.953 4.740   1.00 38.35  ? 94  VAL A N   1 
ATOM   694   C  CA  . VAL A  1 95  ? 44.124  258.032 5.831   1.00 35.60  ? 94  VAL A CA  1 
ATOM   695   C  C   . VAL A  1 95  ? 44.585  258.578 7.203   1.00 37.00  ? 94  VAL A C   1 
ATOM   696   O  O   . VAL A  1 95  ? 45.704  259.063 7.322   1.00 41.35  ? 94  VAL A O   1 
ATOM   697   C  CB  . VAL A  1 95  ? 44.794  256.661 5.546   1.00 38.45  ? 94  VAL A CB  1 
ATOM   698   C  CG1 . VAL A  1 95  ? 44.859  255.801 6.781   1.00 36.71  ? 94  VAL A CG1 1 
ATOM   699   C  CG2 . VAL A  1 95  ? 44.051  255.875 4.476   1.00 35.76  ? 94  VAL A CG2 1 
ATOM   700   N  N   . ALA A  1 96  ? 43.692  258.540 8.210   1.00 36.05  ? 95  ALA A N   1 
ATOM   701   C  CA  . ALA A  1 96  ? 43.988  258.774 9.633   1.00 33.07  ? 95  ALA A CA  1 
ATOM   702   C  C   . ALA A  1 96  ? 44.053  257.383 10.280  1.00 38.42  ? 95  ALA A C   1 
ATOM   703   O  O   . ALA A  1 96  ? 43.023  256.672 10.357  1.00 43.95  ? 95  ALA A O   1 
ATOM   704   C  CB  . ALA A  1 96  ? 42.978  259.718 10.314  1.00 27.18  ? 95  ALA A CB  1 
ATOM   705   N  N   . ASP A  1 97  ? 45.261  256.948 10.657  1.00 34.49  ? 96  ASP A N   1 
ATOM   706   C  CA  . ASP A  1 97  ? 45.389  255.775 11.445  1.00 33.81  ? 96  ASP A CA  1 
ATOM   707   C  C   . ASP A  1 97  ? 45.393  256.184 12.886  1.00 35.91  ? 96  ASP A C   1 
ATOM   708   O  O   . ASP A  1 97  ? 46.492  256.451 13.490  1.00 36.12  ? 96  ASP A O   1 
ATOM   709   C  CB  . ASP A  1 97  ? 46.643  255.034 11.113  1.00 38.94  ? 96  ASP A CB  1 
ATOM   710   C  CG  . ASP A  1 97  ? 46.549  254.382 9.757   1.00 49.11  ? 96  ASP A CG  1 
ATOM   711   O  OD1 . ASP A  1 97  ? 45.496  253.670 9.435   1.00 43.55  ? 96  ASP A OD1 1 
ATOM   712   O  OD2 . ASP A  1 97  ? 47.537  254.603 8.999   1.00 48.74  ? 96  ASP A OD2 1 
ATOM   713   N  N   . VAL A  1 98  ? 44.166  256.203 13.416  1.00 31.87  ? 97  VAL A N   1 
ATOM   714   C  CA  . VAL A  1 98  ? 43.866  256.678 14.728  1.00 32.62  ? 97  VAL A CA  1 
ATOM   715   C  C   . VAL A  1 98  ? 44.472  255.830 15.829  1.00 33.04  ? 97  VAL A C   1 
ATOM   716   O  O   . VAL A  1 98  ? 44.393  254.628 15.798  1.00 30.47  ? 97  VAL A O   1 
ATOM   717   C  CB  . VAL A  1 98  ? 42.383  256.880 14.935  1.00 30.20  ? 97  VAL A CB  1 
ATOM   718   C  CG1 . VAL A  1 98  ? 42.136  257.527 16.284  1.00 26.29  ? 97  VAL A CG1 1 
ATOM   719   C  CG2 . VAL A  1 98  ? 41.808  257.739 13.829  1.00 27.50  ? 97  VAL A CG2 1 
ATOM   720   N  N   . SER A  1 99  ? 45.142  256.501 16.756  1.00 32.39  ? 98  SER A N   1 
ATOM   721   C  CA  . SER A  1 99  ? 45.647  255.828 17.942  1.00 37.61  ? 98  SER A CA  1 
ATOM   722   C  C   . SER A  1 99  ? 45.688  256.799 19.097  1.00 35.75  ? 98  SER A C   1 
ATOM   723   O  O   . SER A  1 99  ? 46.438  257.716 19.049  1.00 42.13  ? 98  SER A O   1 
ATOM   724   C  CB  . SER A  1 99  ? 47.038  255.320 17.701  1.00 36.30  ? 98  SER A CB  1 
ATOM   725   O  OG  . SER A  1 99  ? 47.479  254.666 18.857  1.00 40.42  ? 98  SER A OG  1 
ATOM   726   N  N   . ILE A  1 100 ? 44.845  256.616 20.101  1.00 37.76  ? 99  ILE A N   1 
ATOM   727   C  CA  . ILE A  1 100 ? 44.518  257.628 21.133  1.00 35.33  ? 99  ILE A CA  1 
ATOM   728   C  C   . ILE A  1 100 ? 44.273  256.868 22.414  1.00 35.48  ? 99  ILE A C   1 
ATOM   729   O  O   . ILE A  1 100 ? 43.725  255.805 22.395  1.00 32.93  ? 99  ILE A O   1 
ATOM   730   C  CB  . ILE A  1 100 ? 43.254  258.401 20.763  1.00 36.07  ? 99  ILE A CB  1 
ATOM   731   C  CG1 . ILE A  1 100 ? 43.615  259.542 19.864  1.00 36.35  ? 99  ILE A CG1 1 
ATOM   732   C  CG2 . ILE A  1 100 ? 42.479  258.876 21.980  1.00 35.76  ? 99  ILE A CG2 1 
ATOM   733   C  CD1 . ILE A  1 100 ? 42.413  260.267 19.268  1.00 34.53  ? 99  ILE A CD1 1 
ATOM   734   N  N   . GLU A  1 101 ? 44.737  257.420 23.529  1.00 41.77  ? 100 GLU A N   1 
ATOM   735   C  CA  . GLU A  1 101 ? 44.501  256.843 24.827  1.00 38.04  ? 100 GLU A CA  1 
ATOM   736   C  C   . GLU A  1 101 ? 43.927  257.949 25.674  1.00 41.27  ? 100 GLU A C   1 
ATOM   737   O  O   . GLU A  1 101 ? 44.484  259.045 25.720  1.00 39.45  ? 100 GLU A O   1 
ATOM   738   C  CB  . GLU A  1 101 ? 45.769  256.338 25.398  1.00 37.18  ? 100 GLU A CB  1 
ATOM   739   C  CG  . GLU A  1 101 ? 45.470  255.044 26.057  1.00 47.57  ? 100 GLU A CG  1 
ATOM   740   C  CD  . GLU A  1 101 ? 46.570  254.489 26.954  1.00 53.12  ? 100 GLU A CD  1 
ATOM   741   O  OE1 . GLU A  1 101 ? 47.216  253.463 26.472  1.00 54.35  ? 100 GLU A OE1 1 
ATOM   742   O  OE2 . GLU A  1 101 ? 46.711  255.057 28.113  1.00 42.06  ? 100 GLU A OE2 1 
ATOM   743   N  N   . ASP A  1 102 ? 42.791  257.692 26.315  1.00 39.54  ? 101 ASP A N   1 
ATOM   744   C  CA  . ASP A  1 102 ? 42.096  258.739 27.015  1.00 37.43  ? 101 ASP A CA  1 
ATOM   745   C  C   . ASP A  1 102 ? 41.568  258.244 28.347  1.00 41.26  ? 101 ASP A C   1 
ATOM   746   O  O   . ASP A  1 102 ? 41.166  257.073 28.444  1.00 43.15  ? 101 ASP A O   1 
ATOM   747   C  CB  . ASP A  1 102 ? 40.969  259.333 26.186  1.00 35.61  ? 101 ASP A CB  1 
ATOM   748   C  CG  . ASP A  1 102 ? 40.467  260.674 26.784  1.00 42.01  ? 101 ASP A CG  1 
ATOM   749   O  OD1 . ASP A  1 102 ? 41.141  261.715 26.641  1.00 46.15  ? 101 ASP A OD1 1 
ATOM   750   O  OD2 . ASP A  1 102 ? 39.423  260.718 27.472  1.00 45.21  ? 101 ASP A OD2 1 
ATOM   751   N  N   . SER A  1 103 ? 41.526  259.150 29.338  1.00 40.19  ? 102 SER A N   1 
ATOM   752   C  CA  . SER A  1 103 ? 41.291  258.805 30.758  1.00 38.81  ? 102 SER A CA  1 
ATOM   753   C  C   . SER A  1 103 ? 40.068  259.473 31.237  1.00 34.32  ? 102 SER A C   1 
ATOM   754   O  O   . SER A  1 103 ? 39.726  259.361 32.392  1.00 36.76  ? 102 SER A O   1 
ATOM   755   C  CB  . SER A  1 103 ? 42.496  259.250 31.629  1.00 40.85  ? 102 SER A CB  1 
ATOM   756   O  OG  . SER A  1 103 ? 43.459  258.186 31.644  1.00 44.83  ? 102 SER A OG  1 
ATOM   757   N  N   . VAL A  1 104 ? 39.409  260.193 30.353  1.00 34.23  ? 103 VAL A N   1 
ATOM   758   C  CA  . VAL A  1 104 ? 38.194  260.923 30.738  1.00 34.78  ? 103 VAL A CA  1 
ATOM   759   C  C   . VAL A  1 104 ? 36.920  260.246 30.198  1.00 37.99  ? 103 VAL A C   1 
ATOM   760   O  O   . VAL A  1 104 ? 35.871  260.147 30.874  1.00 38.64  ? 103 VAL A O   1 
ATOM   761   C  CB  . VAL A  1 104 ? 38.372  262.379 30.320  1.00 30.46  ? 103 VAL A CB  1 
ATOM   762   C  CG1 . VAL A  1 104 ? 37.136  263.184 30.523  1.00 28.60  ? 103 VAL A CG1 1 
ATOM   763   C  CG2 . VAL A  1 104 ? 39.536  262.932 31.113  1.00 27.95  ? 103 VAL A CG2 1 
ATOM   764   N  N   . ILE A  1 105 ? 37.013  259.773 28.962  1.00 36.37  ? 104 ILE A N   1 
ATOM   765   C  CA  . ILE A  1 105 ? 35.930  259.019 28.394  1.00 34.47  ? 104 ILE A CA  1 
ATOM   766   C  C   . ILE A  1 105 ? 35.915  257.674 29.104  1.00 37.38  ? 104 ILE A C   1 
ATOM   767   O  O   . ILE A  1 105 ? 36.963  257.200 29.646  1.00 35.39  ? 104 ILE A O   1 
ATOM   768   C  CB  . ILE A  1 105 ? 36.060  258.853 26.854  1.00 33.07  ? 104 ILE A CB  1 
ATOM   769   C  CG1 . ILE A  1 105 ? 37.399  258.257 26.454  1.00 30.13  ? 104 ILE A CG1 1 
ATOM   770   C  CG2 . ILE A  1 105 ? 35.772  260.151 26.139  1.00 30.70  ? 104 ILE A CG2 1 
ATOM   771   C  CD1 . ILE A  1 105 ? 37.358  257.500 25.174  1.00 31.45  ? 104 ILE A CD1 1 
ATOM   772   N  N   . SER A  1 106 ? 34.723  257.070 29.119  1.00 38.05  ? 105 SER A N   1 
ATOM   773   C  CA  . SER A  1 106 ? 34.570  255.730 29.678  1.00 34.00  ? 105 SER A CA  1 
ATOM   774   C  C   . SER A  1 106 ? 33.559  254.899 28.908  1.00 31.21  ? 105 SER A C   1 
ATOM   775   O  O   . SER A  1 106 ? 32.680  255.466 28.305  1.00 31.69  ? 105 SER A O   1 
ATOM   776   C  CB  . SER A  1 106 ? 34.209  255.798 31.177  1.00 29.86  ? 105 SER A CB  1 
ATOM   777   O  OG  . SER A  1 106 ? 34.462  254.501 31.666  1.00 30.47  ? 105 SER A OG  1 
ATOM   778   N  N   . LEU A  1 107 ? 33.700  253.564 28.959  1.00 33.71  ? 106 LEU A N   1 
ATOM   779   C  CA  . LEU A  1 107 ? 32.744  252.637 28.374  1.00 32.09  ? 106 LEU A CA  1 
ATOM   780   C  C   . LEU A  1 107 ? 31.641  252.210 29.370  1.00 37.70  ? 106 LEU A C   1 
ATOM   781   O  O   . LEU A  1 107 ? 30.840  251.384 29.040  1.00 48.44  ? 106 LEU A O   1 
ATOM   782   C  CB  . LEU A  1 107 ? 33.445  251.441 27.753  1.00 29.24  ? 106 LEU A CB  1 
ATOM   783   C  CG  . LEU A  1 107 ? 34.479  251.782 26.673  1.00 35.32  ? 106 LEU A CG  1 
ATOM   784   C  CD1 . LEU A  1 107 ? 35.007  250.580 25.894  1.00 30.68  ? 106 LEU A CD1 1 
ATOM   785   C  CD2 . LEU A  1 107 ? 33.948  252.790 25.675  1.00 32.71  ? 106 LEU A CD2 1 
ATOM   786   N  N   . SER A  1 108 ? 31.566  252.822 30.549  1.00 37.34  ? 107 SER A N   1 
ATOM   787   C  CA  . SER A  1 108 ? 30.617  252.507 31.659  1.00 38.35  ? 107 SER A CA  1 
ATOM   788   C  C   . SER A  1 108 ? 30.527  253.704 32.570  1.00 40.22  ? 107 SER A C   1 
ATOM   789   O  O   . SER A  1 108 ? 31.329  254.651 32.435  1.00 40.04  ? 107 SER A O   1 
ATOM   790   C  CB  . SER A  1 108 ? 31.055  251.321 32.528  1.00 36.88  ? 107 SER A CB  1 
ATOM   791   O  OG  . SER A  1 108 ? 32.470  251.192 32.648  1.00 41.35  ? 107 SER A OG  1 
ATOM   792   N  N   . GLY A  1 109 ? 29.543  253.677 33.466  1.00 38.05  ? 108 GLY A N   1 
ATOM   793   C  CA  . GLY A  1 109 ? 29.245  254.772 34.357  1.00 40.47  ? 108 GLY A CA  1 
ATOM   794   C  C   . GLY A  1 109 ? 28.674  256.017 33.705  1.00 52.65  ? 108 GLY A C   1 
ATOM   795   O  O   . GLY A  1 109 ? 28.078  255.987 32.675  1.00 61.98  ? 108 GLY A O   1 
ATOM   796   N  N   . ASP A  1 110 ? 28.940  257.162 34.279  1.00 58.48  ? 109 ASP A N   1 
ATOM   797   C  CA  . ASP A  1 110 ? 28.267  258.395 33.898  1.00 60.57  ? 109 ASP A CA  1 
ATOM   798   C  C   . ASP A  1 110 ? 29.009  259.228 32.882  1.00 56.14  ? 109 ASP A C   1 
ATOM   799   O  O   . ASP A  1 110 ? 28.650  260.337 32.623  1.00 54.02  ? 109 ASP A O   1 
ATOM   800   C  CB  . ASP A  1 110 ? 28.177  259.247 35.190  1.00 68.77  ? 109 ASP A CB  1 
ATOM   801   C  CG  . ASP A  1 110 ? 27.070  258.746 36.189  1.00 72.68  ? 109 ASP A CG  1 
ATOM   802   O  OD1 . ASP A  1 110 ? 26.487  257.555 36.100  1.00 50.69  ? 109 ASP A OD1 1 
ATOM   803   O  OD2 . ASP A  1 110 ? 26.831  259.627 37.074  1.00 63.89  ? 109 ASP A OD2 1 
ATOM   804   N  N   . HIS A  1 111 ? 30.089  258.727 32.350  1.00 55.18  ? 110 HIS A N   1 
ATOM   805   C  CA  . HIS A  1 111 ? 30.880  259.459 31.362  1.00 51.72  ? 110 HIS A CA  1 
ATOM   806   C  C   . HIS A  1 111 ? 30.827  258.555 30.215  1.00 44.53  ? 110 HIS A C   1 
ATOM   807   O  O   . HIS A  1 111 ? 31.782  258.606 29.352  1.00 41.76  ? 110 HIS A O   1 
ATOM   808   C  CB  . HIS A  1 111 ? 32.415  259.513 31.754  1.00 54.24  ? 110 HIS A CB  1 
ATOM   809   C  CG  . HIS A  1 111 ? 32.806  260.694 32.586  1.00 55.29  ? 110 HIS A CG  1 
ATOM   810   N  ND1 . HIS A  1 111 ? 34.116  261.094 32.735  1.00 62.78  ? 110 HIS A ND1 1 
ATOM   811   C  CD2 . HIS A  1 111 ? 32.064  261.577 33.307  1.00 55.73  ? 110 HIS A CD2 1 
ATOM   812   C  CE1 . HIS A  1 111 ? 34.176  262.151 33.536  1.00 55.03  ? 110 HIS A CE1 1 
ATOM   813   N  NE2 . HIS A  1 111 ? 32.939  262.475 33.881  1.00 51.76  ? 110 HIS A NE2 1 
ATOM   814   N  N   . CYS A  1 112 ? 29.861  257.637 30.294  1.00 35.99  ? 111 CYS A N   1 
ATOM   815   C  CA  . CYS A  1 112 ? 29.883  256.520 29.419  1.00 35.68  ? 111 CYS A CA  1 
ATOM   816   C  C   . CYS A  1 112 ? 29.561  257.026 28.020  1.00 30.78  ? 111 CYS A C   1 
ATOM   817   O  O   . CYS A  1 112 ? 28.576  257.758 27.846  1.00 26.40  ? 111 CYS A O   1 
ATOM   818   C  CB  . CYS A  1 112 ? 28.860  255.530 29.907  1.00 39.75  ? 111 CYS A CB  1 
ATOM   819   S  SG  . CYS A  1 112 ? 28.462  254.167 28.769  1.00 44.34  ? 111 CYS A SG  1 
ATOM   820   N  N   . ILE A  1 113 ? 30.407  256.664 27.061  1.00 26.74  ? 112 ILE A N   1 
ATOM   821   C  CA  . ILE A  1 113 ? 30.151  257.119 25.706  1.00 32.27  ? 112 ILE A CA  1 
ATOM   822   C  C   . ILE A  1 113 ? 29.345  256.172 24.846  1.00 28.95  ? 112 ILE A C   1 
ATOM   823   O  O   . ILE A  1 113 ? 29.052  256.516 23.776  1.00 32.10  ? 112 ILE A O   1 
ATOM   824   C  CB  . ILE A  1 113 ? 31.446  257.606 24.992  1.00 32.70  ? 112 ILE A CB  1 
ATOM   825   C  CG1 . ILE A  1 113 ? 32.531  256.502 25.021  1.00 30.90  ? 112 ILE A CG1 1 
ATOM   826   C  CG2 . ILE A  1 113 ? 31.886  258.869 25.701  1.00 30.23  ? 112 ILE A CG2 1 
ATOM   827   C  CD1 . ILE A  1 113 ? 33.609  256.646 23.989  1.00 28.77  ? 112 ILE A CD1 1 
ATOM   828   N  N   . ILE A  1 114 ? 29.033  254.970 25.321  1.00 31.92  ? 113 ILE A N   1 
ATOM   829   C  CA  . ILE A  1 114 ? 28.251  254.008 24.592  1.00 32.68  ? 113 ILE A CA  1 
ATOM   830   C  C   . ILE A  1 114 ? 26.883  254.625 24.254  1.00 33.79  ? 113 ILE A C   1 
ATOM   831   O  O   . ILE A  1 114 ? 26.172  255.114 25.138  1.00 33.94  ? 113 ILE A O   1 
ATOM   832   C  CB  . ILE A  1 114 ? 27.996  252.731 25.404  1.00 34.38  ? 113 ILE A CB  1 
ATOM   833   C  CG1 . ILE A  1 114 ? 29.301  252.050 25.839  1.00 31.39  ? 113 ILE A CG1 1 
ATOM   834   C  CG2 . ILE A  1 114 ? 27.027  251.775 24.655  1.00 30.98  ? 113 ILE A CG2 1 
ATOM   835   C  CD1 . ILE A  1 114 ? 30.091  251.548 24.708  1.00 25.67  ? 113 ILE A CD1 1 
ATOM   836   N  N   . GLY A  1 115 ? 26.559  254.653 22.959  1.00 32.10  ? 114 GLY A N   1 
ATOM   837   C  CA  . GLY A  1 115 ? 25.277  255.144 22.528  1.00 31.04  ? 114 GLY A CA  1 
ATOM   838   C  C   . GLY A  1 115 ? 25.244  256.614 22.215  1.00 31.99  ? 114 GLY A C   1 
ATOM   839   O  O   . GLY A  1 115 ? 24.169  257.186 21.906  1.00 29.26  ? 114 GLY A O   1 
ATOM   840   N  N   . ARG A  1 116 ? 26.431  257.225 22.272  1.00 31.73  ? 115 ARG A N   1 
ATOM   841   C  CA  . ARG A  1 116 ? 26.612  258.595 21.783  1.00 32.00  ? 115 ARG A CA  1 
ATOM   842   C  C   . ARG A  1 116 ? 27.226  258.565 20.372  1.00 29.81  ? 115 ARG A C   1 
ATOM   843   O  O   . ARG A  1 116 ? 27.483  257.445 19.819  1.00 30.55  ? 115 ARG A O   1 
ATOM   844   C  CB  . ARG A  1 116 ? 27.487  259.347 22.716  1.00 31.52  ? 115 ARG A CB  1 
ATOM   845   C  CG  . ARG A  1 116 ? 27.237  259.037 24.163  1.00 32.05  ? 115 ARG A CG  1 
ATOM   846   C  CD  . ARG A  1 116 ? 26.697  260.224 24.836  1.00 30.21  ? 115 ARG A CD  1 
ATOM   847   N  NE  . ARG A  1 116 ? 26.376  260.030 26.244  1.00 31.18  ? 115 ARG A NE  1 
ATOM   848   C  CZ  . ARG A  1 116 ? 25.349  260.650 26.853  1.00 31.06  ? 115 ARG A CZ  1 
ATOM   849   N  NH1 . ARG A  1 116 ? 24.494  261.488 26.199  1.00 29.01  ? 115 ARG A NH1 1 
ATOM   850   N  NH2 . ARG A  1 116 ? 25.157  260.421 28.129  1.00 33.59  ? 115 ARG A NH2 1 
ATOM   851   N  N   . THR A  1 117 ? 27.446  259.744 19.785  1.00 28.80  ? 116 THR A N   1 
ATOM   852   C  CA  . THR A  1 117 ? 28.050  259.804 18.418  1.00 31.14  ? 116 THR A CA  1 
ATOM   853   C  C   . THR A  1 117 ? 29.523  260.181 18.329  1.00 27.35  ? 116 THR A C   1 
ATOM   854   O  O   . THR A  1 117 ? 29.925  261.163 18.813  1.00 30.24  ? 116 THR A O   1 
ATOM   855   C  CB  . THR A  1 117 ? 27.244  260.690 17.480  1.00 28.51  ? 116 THR A CB  1 
ATOM   856   O  OG1 . THR A  1 117 ? 25.908  260.254 17.473  1.00 28.79  ? 116 THR A OG1 1 
ATOM   857   C  CG2 . THR A  1 117 ? 27.755  260.628 16.053  1.00 27.34  ? 116 THR A CG2 1 
ATOM   858   N  N   . LEU A  1 118 ? 30.296  259.406 17.646  1.00 29.67  ? 117 LEU A N   1 
ATOM   859   C  CA  . LEU A  1 118 ? 31.647  259.815 17.307  1.00 32.76  ? 117 LEU A CA  1 
ATOM   860   C  C   . LEU A  1 118 ? 31.601  260.625 15.958  1.00 34.31  ? 117 LEU A C   1 
ATOM   861   O  O   . LEU A  1 118 ? 31.048  260.142 14.988  1.00 34.03  ? 117 LEU A O   1 
ATOM   862   C  CB  . LEU A  1 118 ? 32.566  258.577 17.232  1.00 30.72  ? 117 LEU A CB  1 
ATOM   863   C  CG  . LEU A  1 118 ? 34.033  258.818 16.894  1.00 31.45  ? 117 LEU A CG  1 
ATOM   864   C  CD1 . LEU A  1 118 ? 34.711  259.723 17.948  1.00 27.59  ? 117 LEU A CD1 1 
ATOM   865   C  CD2 . LEU A  1 118 ? 34.793  257.546 16.571  1.00 26.28  ? 117 LEU A CD2 1 
ATOM   866   N  N   . VAL A  1 119 ? 32.118  261.858 15.946  1.00 33.22  ? 118 VAL A N   1 
ATOM   867   C  CA  . VAL A  1 119 ? 32.228  262.705 14.746  1.00 32.98  ? 118 VAL A CA  1 
ATOM   868   C  C   . VAL A  1 119 ? 33.684  263.026 14.360  1.00 32.69  ? 118 VAL A C   1 
ATOM   869   O  O   . VAL A  1 119 ? 34.516  263.322 15.198  1.00 36.00  ? 118 VAL A O   1 
ATOM   870   C  CB  . VAL A  1 119 ? 31.409  264.015 14.895  1.00 34.12  ? 118 VAL A CB  1 
ATOM   871   C  CG1 . VAL A  1 119 ? 31.438  264.840 13.608  1.00 30.02  ? 118 VAL A CG1 1 
ATOM   872   C  CG2 . VAL A  1 119 ? 29.979  263.699 15.272  1.00 32.04  ? 118 VAL A CG2 1 
ATOM   873   N  N   . VAL A  1 120 ? 34.006  262.885 13.099  1.00 31.77  ? 119 VAL A N   1 
ATOM   874   C  CA  . VAL A  1 120 ? 35.231  263.374 12.560  1.00 31.44  ? 119 VAL A CA  1 
ATOM   875   C  C   . VAL A  1 120 ? 34.910  264.651 11.798  1.00 32.80  ? 119 VAL A C   1 
ATOM   876   O  O   . VAL A  1 120 ? 34.012  264.680 10.974  1.00 31.41  ? 119 VAL A O   1 
ATOM   877   C  CB  . VAL A  1 120 ? 35.903  262.388 11.618  1.00 34.11  ? 119 VAL A CB  1 
ATOM   878   C  CG1 . VAL A  1 120 ? 35.003  262.041 10.447  1.00 32.23  ? 119 VAL A CG1 1 
ATOM   879   C  CG2 . VAL A  1 120 ? 37.190  263.002 11.072  1.00 35.52  ? 119 VAL A CG2 1 
ATOM   880   N  N   . HIS A  1 121 ? 35.636  265.720 12.126  1.00 37.97  ? 120 HIS A N   1 
ATOM   881   C  CA  . HIS A  1 121 ? 35.369  267.053 11.540  1.00 37.13  ? 120 HIS A CA  1 
ATOM   882   C  C   . HIS A  1 121 ? 36.193  267.486 10.316  1.00 41.74  ? 120 HIS A C   1 
ATOM   883   O  O   . HIS A  1 121 ? 37.201  266.851 9.891   1.00 39.51  ? 120 HIS A O   1 
ATOM   884   C  CB  . HIS A  1 121 ? 35.350  268.146 12.568  1.00 35.12  ? 120 HIS A CB  1 
ATOM   885   C  CG  . HIS A  1 121 ? 34.271  268.005 13.588  1.00 37.89  ? 120 HIS A CG  1 
ATOM   886   N  ND1 . HIS A  1 121 ? 33.112  268.744 13.548  1.00 36.79  ? 120 HIS A ND1 1 
ATOM   887   C  CD2 . HIS A  1 121 ? 34.172  267.211 14.686  1.00 37.05  ? 120 HIS A CD2 1 
ATOM   888   C  CE1 . HIS A  1 121 ? 32.358  268.434 14.594  1.00 36.02  ? 120 HIS A CE1 1 
ATOM   889   N  NE2 . HIS A  1 121 ? 32.982  267.519 15.308  1.00 36.41  ? 120 HIS A NE2 1 
ATOM   890   N  N   . GLU A  1 122 ? 35.708  268.576 9.720   1.00 43.07  ? 121 GLU A N   1 
ATOM   891   C  CA  . GLU A  1 122 ? 36.294  269.164 8.510   1.00 43.28  ? 121 GLU A CA  1 
ATOM   892   C  C   . GLU A  1 122 ? 37.747  269.718 8.715   1.00 41.36  ? 121 GLU A C   1 
ATOM   893   O  O   . GLU A  1 122 ? 38.646  269.495 7.917   1.00 42.72  ? 121 GLU A O   1 
ATOM   894   C  CB  . GLU A  1 122 ? 35.368  270.272 8.140   1.00 41.38  ? 121 GLU A CB  1 
ATOM   895   C  CG  . GLU A  1 122 ? 35.559  270.831 6.756   1.00 46.78  ? 121 GLU A CG  1 
ATOM   896   C  CD  . GLU A  1 122 ? 34.845  272.204 6.592   1.00 54.54  ? 121 GLU A CD  1 
ATOM   897   O  OE1 . GLU A  1 122 ? 34.831  272.657 5.431   1.00 56.81  ? 121 GLU A OE1 1 
ATOM   898   O  OE2 . GLU A  1 122 ? 34.276  272.838 7.568   1.00 48.07  ? 121 GLU A OE2 1 
ATOM   899   N  N   . LYS A  1 123 ? 37.943  270.418 9.814   1.00 40.18  ? 122 LYS A N   1 
ATOM   900   C  CA  . LYS A  1 123 ? 39.170  271.160 10.085  1.00 45.02  ? 122 LYS A CA  1 
ATOM   901   C  C   . LYS A  1 123 ? 39.718  270.800 11.454  1.00 42.04  ? 122 LYS A C   1 
ATOM   902   O  O   . LYS A  1 123 ? 39.050  270.153 12.256  1.00 40.39  ? 122 LYS A O   1 
ATOM   903   C  CB  . LYS A  1 123 ? 38.920  272.677 10.117  1.00 41.66  ? 122 LYS A CB  1 
ATOM   904   C  CG  . LYS A  1 123 ? 38.013  273.262 9.081   1.00 43.60  ? 122 LYS A CG  1 
ATOM   905   C  CD  . LYS A  1 123 ? 38.092  274.745 9.411   1.00 54.11  ? 122 LYS A CD  1 
ATOM   906   C  CE  . LYS A  1 123 ? 36.717  275.445 9.340   1.00 58.13  ? 122 LYS A CE  1 
ATOM   907   N  NZ  . LYS A  1 123 ? 36.467  276.381 10.497  1.00 60.41  ? 122 LYS A NZ  1 
ATOM   908   N  N   . ALA A  1 124 ? 40.910  271.324 11.724  1.00 43.02  ? 123 ALA A N   1 
ATOM   909   C  CA  . ALA A  1 124 ? 41.578  271.136 12.973  1.00 39.67  ? 123 ALA A CA  1 
ATOM   910   C  C   . ALA A  1 124 ? 40.776  271.642 14.107  1.00 36.84  ? 123 ALA A C   1 
ATOM   911   O  O   . ALA A  1 124 ? 40.063  272.681 14.011  1.00 43.27  ? 123 ALA A O   1 
ATOM   912   C  CB  . ALA A  1 124 ? 42.892  271.854 12.931  1.00 43.73  ? 123 ALA A CB  1 
ATOM   913   N  N   . ASP A  1 125 ? 40.879  270.929 15.201  1.00 35.23  ? 124 ASP A N   1 
ATOM   914   C  CA  . ASP A  1 125 ? 40.340  271.435 16.446  1.00 37.75  ? 124 ASP A CA  1 
ATOM   915   C  C   . ASP A  1 125 ? 41.437  272.328 17.054  1.00 38.83  ? 124 ASP A C   1 
ATOM   916   O  O   . ASP A  1 125 ? 42.594  271.882 17.237  1.00 36.63  ? 124 ASP A O   1 
ATOM   917   C  CB  . ASP A  1 125 ? 40.033  270.238 17.339  1.00 41.96  ? 124 ASP A CB  1 
ATOM   918   C  CG  . ASP A  1 125 ? 39.520  270.614 18.746  1.00 43.26  ? 124 ASP A CG  1 
ATOM   919   O  OD1 . ASP A  1 125 ? 39.437  271.796 19.190  1.00 40.77  ? 124 ASP A OD1 1 
ATOM   920   O  OD2 . ASP A  1 125 ? 39.188  269.632 19.443  1.00 49.51  ? 124 ASP A OD2 1 
ATOM   921   N  N   . ASP A  1 126 ? 41.098  273.593 17.330  1.00 39.17  ? 125 ASP A N   1 
ATOM   922   C  CA  . ASP A  1 126 ? 42.100  274.536 17.879  1.00 37.90  ? 125 ASP A CA  1 
ATOM   923   C  C   . ASP A  1 126 ? 42.332  274.331 19.387  1.00 41.19  ? 125 ASP A C   1 
ATOM   924   O  O   . ASP A  1 126 ? 43.032  275.112 20.020  1.00 41.23  ? 125 ASP A O   1 
ATOM   925   C  CB  . ASP A  1 126 ? 41.709  275.981 17.583  1.00 33.13  ? 125 ASP A CB  1 
ATOM   926   C  CG  . ASP A  1 126 ? 40.453  276.425 18.337  1.00 39.21  ? 125 ASP A CG  1 
ATOM   927   O  OD1 . ASP A  1 126 ? 40.165  276.027 19.511  1.00 37.72  ? 125 ASP A OD1 1 
ATOM   928   O  OD2 . ASP A  1 126 ? 39.738  277.257 17.765  1.00 40.71  ? 125 ASP A OD2 1 
ATOM   929   N  N   . LEU A  1 127 ? 41.693  273.316 19.968  1.00 40.72  ? 126 LEU A N   1 
ATOM   930   C  CA  . LEU A  1 127 ? 41.775  273.013 21.406  1.00 38.64  ? 126 LEU A CA  1 
ATOM   931   C  C   . LEU A  1 127 ? 41.245  274.128 22.329  1.00 37.94  ? 126 LEU A C   1 
ATOM   932   O  O   . LEU A  1 127 ? 41.595  274.208 23.511  1.00 40.10  ? 126 LEU A O   1 
ATOM   933   C  CB  . LEU A  1 127 ? 43.193  272.526 21.770  1.00 34.95  ? 126 LEU A CB  1 
ATOM   934   C  CG  . LEU A  1 127 ? 43.787  271.524 20.764  1.00 37.55  ? 126 LEU A CG  1 
ATOM   935   C  CD1 . LEU A  1 127 ? 45.110  271.074 21.327  1.00 36.10  ? 126 LEU A CD1 1 
ATOM   936   C  CD2 . LEU A  1 127 ? 42.891  270.318 20.429  1.00 38.23  ? 126 LEU A CD2 1 
ATOM   937   N  N   . GLY A  1 128 ? 40.412  275.011 21.797  1.00 35.50  ? 127 GLY A N   1 
ATOM   938   C  CA  . GLY A  1 128 ? 39.848  276.077 22.644  1.00 40.35  ? 127 GLY A CA  1 
ATOM   939   C  C   . GLY A  1 128 ? 40.815  277.255 22.798  1.00 46.00  ? 127 GLY A C   1 
ATOM   940   O  O   . GLY A  1 128 ? 40.614  278.089 23.663  1.00 43.27  ? 127 GLY A O   1 
ATOM   941   N  N   . LYS A  1 129 ? 41.841  277.344 21.935  1.00 43.63  ? 128 LYS A N   1 
ATOM   942   C  CA  . LYS A  1 129 ? 42.847  278.411 22.033  1.00 44.26  ? 128 LYS A CA  1 
ATOM   943   C  C   . LYS A  1 129 ? 42.731  279.453 20.914  1.00 43.91  ? 128 LYS A C   1 
ATOM   944   O  O   . LYS A  1 129 ? 43.665  280.213 20.714  1.00 50.78  ? 128 LYS A O   1 
ATOM   945   C  CB  . LYS A  1 129 ? 44.230  277.808 22.038  1.00 39.74  ? 128 LYS A CB  1 
ATOM   946   C  CG  . LYS A  1 129 ? 44.392  276.895 23.220  1.00 43.95  ? 128 LYS A CG  1 
ATOM   947   C  CD  . LYS A  1 129 ? 45.698  276.164 23.068  1.00 49.71  ? 128 LYS A CD  1 
ATOM   948   C  CE  . LYS A  1 129 ? 46.203  275.783 24.462  1.00 58.71  ? 128 LYS A CE  1 
ATOM   949   N  NZ  . LYS A  1 129 ? 46.701  276.900 25.335  1.00 58.33  ? 128 LYS A NZ  1 
ATOM   950   N  N   . GLY A  1 130 ? 41.567  279.527 20.274  1.00 38.00  ? 129 GLY A N   1 
ATOM   951   C  CA  . GLY A  1 130 ? 41.348  280.298 19.055  1.00 41.43  ? 129 GLY A CA  1 
ATOM   952   C  C   . GLY A  1 130 ? 40.771  281.716 19.207  1.00 42.50  ? 129 GLY A C   1 
ATOM   953   O  O   . GLY A  1 130 ? 40.511  282.409 18.196  1.00 41.68  ? 129 GLY A O   1 
ATOM   954   N  N   . GLY A  1 131 ? 40.532  282.156 20.435  1.00 39.12  ? 130 GLY A N   1 
ATOM   955   C  CA  . GLY A  1 131 ? 40.110  283.528 20.610  1.00 45.29  ? 130 GLY A CA  1 
ATOM   956   C  C   . GLY A  1 131 ? 38.659  283.891 20.365  1.00 53.17  ? 130 GLY A C   1 
ATOM   957   O  O   . GLY A  1 131 ? 38.152  284.749 21.072  1.00 57.96  ? 130 GLY A O   1 
ATOM   958   N  N   . ASN A  1 132 ? 37.970  283.300 19.376  1.00 53.82  ? 131 ASN A N   1 
ATOM   959   C  CA  . ASN A  1 132 ? 36.470  283.447 19.286  1.00 51.15  ? 131 ASN A CA  1 
ATOM   960   C  C   . ASN A  1 132 ? 35.593  282.627 20.313  1.00 55.95  ? 131 ASN A C   1 
ATOM   961   O  O   . ASN A  1 132 ? 36.113  281.735 21.016  1.00 54.98  ? 131 ASN A O   1 
ATOM   962   C  CB  . ASN A  1 132 ? 35.975  283.252 17.836  1.00 43.26  ? 131 ASN A CB  1 
ATOM   963   C  CG  . ASN A  1 132 ? 36.330  281.913 17.275  1.00 50.96  ? 131 ASN A CG  1 
ATOM   964   O  OD1 . ASN A  1 132 ? 36.435  280.907 18.021  1.00 54.59  ? 131 ASN A OD1 1 
ATOM   965   N  ND2 . ASN A  1 132 ? 36.480  281.855 15.935  1.00 50.88  ? 131 ASN A ND2 1 
ATOM   966   N  N   . GLU A  1 133 ? 34.272  282.908 20.374  1.00 58.32  ? 132 GLU A N   1 
ATOM   967   C  CA  . GLU A  1 133 ? 33.301  282.065 21.139  1.00 53.01  ? 132 GLU A CA  1 
ATOM   968   C  C   . GLU A  1 133 ? 33.184  280.643 20.608  1.00 47.65  ? 132 GLU A C   1 
ATOM   969   O  O   . GLU A  1 133 ? 33.087  279.697 21.373  1.00 42.10  ? 132 GLU A O   1 
ATOM   970   C  CB  . GLU A  1 133 ? 31.899  282.674 21.107  1.00 66.08  ? 132 GLU A CB  1 
ATOM   971   C  CG  . GLU A  1 133 ? 31.089  282.435 22.410  1.00 72.83  ? 132 GLU A CG  1 
ATOM   972   C  CD  . GLU A  1 133 ? 29.524  282.393 22.236  1.00 84.32  ? 132 GLU A CD  1 
ATOM   973   O  OE1 . GLU A  1 133 ? 28.961  282.912 21.164  1.00 60.05  ? 132 GLU A OE1 1 
ATOM   974   O  OE2 . GLU A  1 133 ? 28.848  281.844 23.212  1.00 67.59  ? 132 GLU A OE2 1 
ATOM   975   N  N   . GLU A  1 134 ? 33.218  280.483 19.287  1.00 46.72  ? 133 GLU A N   1 
ATOM   976   C  CA  . GLU A  1 134 ? 33.274  279.156 18.692  1.00 45.80  ? 133 GLU A CA  1 
ATOM   977   C  C   . GLU A  1 134 ? 34.375  278.220 19.296  1.00 48.49  ? 133 GLU A C   1 
ATOM   978   O  O   . GLU A  1 134 ? 34.230  277.016 19.380  1.00 48.76  ? 133 GLU A O   1 
ATOM   979   C  CB  . GLU A  1 134 ? 33.414  279.308 17.187  1.00 50.50  ? 133 GLU A CB  1 
ATOM   980   C  CG  . GLU A  1 134 ? 32.475  278.421 16.313  1.00 59.50  ? 133 GLU A CG  1 
ATOM   981   C  CD  . GLU A  1 134 ? 31.171  277.977 17.001  1.00 64.55  ? 133 GLU A CD  1 
ATOM   982   O  OE1 . GLU A  1 134 ? 30.483  278.842 17.648  1.00 63.55  ? 133 GLU A OE1 1 
ATOM   983   O  OE2 . GLU A  1 134 ? 30.877  276.746 16.947  1.00 60.18  ? 133 GLU A OE2 1 
ATOM   984   N  N   . SER A  1 135 ? 35.456  278.792 19.774  1.00 45.27  ? 134 SER A N   1 
ATOM   985   C  CA  . SER A  1 135 ? 36.576  277.988 20.092  1.00 45.36  ? 134 SER A CA  1 
ATOM   986   C  C   . SER A  1 135 ? 36.281  277.282 21.413  1.00 43.20  ? 134 SER A C   1 
ATOM   987   O  O   . SER A  1 135 ? 36.710  276.147 21.683  1.00 42.16  ? 134 SER A O   1 
ATOM   988   C  CB  . SER A  1 135 ? 37.843  278.879 20.148  1.00 44.31  ? 134 SER A CB  1 
ATOM   989   O  OG  . SER A  1 135 ? 38.993  278.094 20.405  1.00 43.67  ? 134 SER A OG  1 
ATOM   990   N  N   . THR A  1 136 ? 35.541  277.958 22.264  1.00 43.16  ? 135 THR A N   1 
ATOM   991   C  CA  . THR A  1 136 ? 35.332  277.384 23.582  1.00 47.27  ? 135 THR A CA  1 
ATOM   992   C  C   . THR A  1 136 ? 34.148  276.379 23.601  1.00 43.01  ? 135 THR A C   1 
ATOM   993   O  O   . THR A  1 136 ? 33.918  275.711 24.602  1.00 47.64  ? 135 THR A O   1 
ATOM   994   C  CB  . THR A  1 136 ? 35.114  278.534 24.565  1.00 50.88  ? 135 THR A CB  1 
ATOM   995   O  OG1 . THR A  1 136 ? 33.890  279.175 24.200  1.00 52.80  ? 135 THR A OG1 1 
ATOM   996   C  CG2 . THR A  1 136 ? 36.200  279.556 24.406  1.00 47.18  ? 135 THR A CG2 1 
ATOM   997   N  N   . LYS A  1 137 ? 33.435  276.311 22.479  1.00 44.93  ? 136 LYS A N   1 
ATOM   998   C  CA  . LYS A  1 137 ? 32.284  275.432 22.206  1.00 46.35  ? 136 LYS A CA  1 
ATOM   999   C  C   . LYS A  1 137 ? 32.659  274.259 21.270  1.00 41.44  ? 136 LYS A C   1 
ATOM   1000  O  O   . LYS A  1 137 ? 32.366  273.111 21.562  1.00 46.60  ? 136 LYS A O   1 
ATOM   1001  C  CB  . LYS A  1 137 ? 31.108  276.244 21.602  1.00 43.30  ? 136 LYS A CB  1 
ATOM   1002  C  CG  . LYS A  1 137 ? 30.502  277.236 22.575  1.00 43.63  ? 136 LYS A CG  1 
ATOM   1003  C  CD  . LYS A  1 137 ? 29.147  277.839 22.166  1.00 58.39  ? 136 LYS A CD  1 
ATOM   1004  C  CE  . LYS A  1 137 ? 29.020  278.387 20.710  1.00 66.53  ? 136 LYS A CE  1 
ATOM   1005  N  NZ  . LYS A  1 137 ? 27.573  278.223 20.231  1.00 67.00  ? 136 LYS A NZ  1 
ATOM   1006  N  N   . THR A  1 138 ? 33.346  274.535 20.174  1.00 40.26  ? 137 THR A N   1 
ATOM   1007  C  CA  . THR A  1 138 ? 33.629  273.494 19.175  1.00 40.03  ? 137 THR A CA  1 
ATOM   1008  C  C   . THR A  1 138 ? 35.089  273.455 18.690  1.00 38.50  ? 137 THR A C   1 
ATOM   1009  O  O   . THR A  1 138 ? 35.450  272.611 17.867  1.00 44.10  ? 137 THR A O   1 
ATOM   1010  C  CB  . THR A  1 138 ? 32.664  273.569 17.936  1.00 39.04  ? 137 THR A CB  1 
ATOM   1011  O  OG1 . THR A  1 138 ? 32.967  274.746 17.173  1.00 44.80  ? 137 THR A OG1 1 
ATOM   1012  C  CG2 . THR A  1 138 ? 31.246  273.716 18.333  1.00 37.02  ? 137 THR A CG2 1 
ATOM   1013  N  N   . GLY A  1 139 ? 35.944  274.341 19.183  1.00 40.20  ? 138 GLY A N   1 
ATOM   1014  C  CA  . GLY A  1 139 ? 37.335  274.370 18.756  1.00 37.69  ? 138 GLY A CA  1 
ATOM   1015  C  C   . GLY A  1 139 ? 37.531  274.763 17.278  1.00 37.26  ? 138 GLY A C   1 
ATOM   1016  O  O   . GLY A  1 139 ? 38.598  274.486 16.713  1.00 41.92  ? 138 GLY A O   1 
ATOM   1017  N  N   . ASN A  1 140 ? 36.513  275.383 16.670  1.00 37.53  ? 139 ASN A N   1 
ATOM   1018  C  CA  . ASN A  1 140 ? 36.426  275.683 15.216  1.00 40.26  ? 139 ASN A CA  1 
ATOM   1019  C  C   . ASN A  1 140 ? 36.713  274.520 14.245  1.00 41.22  ? 139 ASN A C   1 
ATOM   1020  O  O   . ASN A  1 140 ? 37.214  274.735 13.136  1.00 42.78  ? 139 ASN A O   1 
ATOM   1021  C  CB  . ASN A  1 140 ? 37.290  276.925 14.844  1.00 41.30  ? 139 ASN A CB  1 
ATOM   1022  C  CG  . ASN A  1 140 ? 36.881  278.150 15.616  1.00 47.91  ? 139 ASN A CG  1 
ATOM   1023  O  OD1 . ASN A  1 140 ? 35.869  278.782 15.256  1.00 44.03  ? 139 ASN A OD1 1 
ATOM   1024  N  ND2 . ASN A  1 140 ? 37.601  278.452 16.761  1.00 43.37  ? 139 ASN A ND2 1 
ATOM   1025  N  N   . ALA A  1 141 ? 36.352  273.311 14.635  1.00 38.92  ? 140 ALA A N   1 
ATOM   1026  C  CA  . ALA A  1 141 ? 36.656  272.130 13.844  1.00 37.74  ? 140 ALA A CA  1 
ATOM   1027  C  C   . ALA A  1 141 ? 35.748  272.048 12.599  1.00 35.72  ? 140 ALA A C   1 
ATOM   1028  O  O   . ALA A  1 141 ? 36.002  271.233 11.694  1.00 37.87  ? 140 ALA A O   1 
ATOM   1029  C  CB  . ALA A  1 141 ? 36.585  270.860 14.729  1.00 36.88  ? 140 ALA A CB  1 
ATOM   1030  N  N   . GLY A  1 142 ? 34.712  272.896 12.546  1.00 31.91  ? 141 GLY A N   1 
ATOM   1031  C  CA  . GLY A  1 142 ? 33.878  272.970 11.383  1.00 35.32  ? 141 GLY A CA  1 
ATOM   1032  C  C   . GLY A  1 142 ? 32.859  271.857 11.192  1.00 41.88  ? 141 GLY A C   1 
ATOM   1033  O  O   . GLY A  1 142 ? 32.488  271.151 12.149  1.00 39.44  ? 141 GLY A O   1 
ATOM   1034  N  N   . SER A  1 143 ? 32.418  271.691 9.947   1.00 40.55  ? 142 SER A N   1 
ATOM   1035  C  CA  . SER A  1 143 ? 31.313  270.803 9.668   1.00 42.09  ? 142 SER A CA  1 
ATOM   1036  C  C   . SER A  1 143 ? 31.681  269.283 9.943   1.00 42.12  ? 142 SER A C   1 
ATOM   1037  O  O   . SER A  1 143 ? 32.844  268.924 10.125  1.00 44.29  ? 142 SER A O   1 
ATOM   1038  C  CB  . SER A  1 143 ? 30.857  271.062 8.247   1.00 39.16  ? 142 SER A CB  1 
ATOM   1039  O  OG  . SER A  1 143 ? 31.875  270.588 7.399   1.00 45.60  ? 142 SER A OG  1 
ATOM   1040  N  N   . ARG A  1 144 ? 30.664  268.424 10.010  1.00 41.20  ? 143 ARG A N   1 
ATOM   1041  C  CA  . ARG A  1 144 ? 30.762  267.049 10.446  1.00 35.51  ? 143 ARG A CA  1 
ATOM   1042  C  C   . ARG A  1 144 ? 30.895  266.211 9.183   1.00 34.22  ? 143 ARG A C   1 
ATOM   1043  O  O   . ARG A  1 144 ? 30.017  266.224 8.367   1.00 34.72  ? 143 ARG A O   1 
ATOM   1044  C  CB  . ARG A  1 144 ? 29.492  266.731 11.259  1.00 31.88  ? 143 ARG A CB  1 
ATOM   1045  C  CG  . ARG A  1 144 ? 29.334  267.582 12.492  1.00 30.66  ? 143 ARG A CG  1 
ATOM   1046  C  CD  . ARG A  1 144 ? 27.988  267.533 13.123  1.00 32.09  ? 143 ARG A CD  1 
ATOM   1047  N  NE  . ARG A  1 144 ? 27.950  268.535 14.213  1.00 35.32  ? 143 ARG A NE  1 
ATOM   1048  C  CZ  . ARG A  1 144 ? 27.288  268.441 15.366  1.00 32.38  ? 143 ARG A CZ  1 
ATOM   1049  N  NH1 . ARG A  1 144 ? 26.547  267.365 15.703  1.00 35.91  ? 143 ARG A NH1 1 
ATOM   1050  N  NH2 . ARG A  1 144 ? 27.403  269.407 16.227  1.00 29.09  ? 143 ARG A NH2 1 
ATOM   1051  N  N   . LEU A  1 145 ? 31.969  265.470 9.022   1.00 34.93  ? 144 LEU A N   1 
ATOM   1052  C  CA  . LEU A  1 145 ? 32.171  264.780 7.756   1.00 38.13  ? 144 LEU A CA  1 
ATOM   1053  C  C   . LEU A  1 145 ? 31.593  263.381 7.789   1.00 39.34  ? 144 LEU A C   1 
ATOM   1054  O  O   . LEU A  1 145 ? 31.118  262.857 6.780   1.00 38.04  ? 144 LEU A O   1 
ATOM   1055  C  CB  . LEU A  1 145 ? 33.696  264.758 7.406   1.00 40.46  ? 144 LEU A CB  1 
ATOM   1056  C  CG  . LEU A  1 145 ? 34.436  266.137 7.182   1.00 41.83  ? 144 LEU A CG  1 
ATOM   1057  C  CD1 . LEU A  1 145 ? 35.857  265.926 6.710   1.00 44.16  ? 144 LEU A CD1 1 
ATOM   1058  C  CD2 . LEU A  1 145 ? 33.781  267.112 6.211   1.00 37.53  ? 144 LEU A CD2 1 
ATOM   1059  N  N   . ALA A  1 146 ? 31.669  262.752 8.961   1.00 35.98  ? 145 ALA A N   1 
ATOM   1060  C  CA  . ALA A  1 146 ? 31.208  261.403 9.108   1.00 33.79  ? 145 ALA A CA  1 
ATOM   1061  C  C   . ALA A  1 146 ? 30.897  261.166 10.594  1.00 33.58  ? 145 ALA A C   1 
ATOM   1062  O  O   . ALA A  1 146 ? 31.532  261.744 11.475  1.00 35.22  ? 145 ALA A O   1 
ATOM   1063  C  CB  . ALA A  1 146 ? 32.263  260.426 8.568   1.00 26.70  ? 145 ALA A CB  1 
ATOM   1064  N  N   . CYS A  1 147 ? 29.927  260.328 10.891  1.00 32.18  ? 146 CYS A N   1 
ATOM   1065  C  CA  . CYS A  1 147 ? 29.692  259.972 12.249  1.00 30.94  ? 146 CYS A CA  1 
ATOM   1066  C  C   . CYS A  1 147 ? 29.087  258.602 12.334  1.00 33.64  ? 146 CYS A C   1 
ATOM   1067  O  O   . CYS A  1 147 ? 28.761  257.995 11.311  1.00 34.71  ? 146 CYS A O   1 
ATOM   1068  C  CB  . CYS A  1 147 ? 28.777  260.987 12.888  1.00 33.76  ? 146 CYS A CB  1 
ATOM   1069  S  SG  . CYS A  1 147 ? 27.225  261.122 11.978  1.00 36.69  ? 146 CYS A SG  1 
ATOM   1070  N  N   . GLY A  1 148 ? 28.899  258.155 13.575  1.00 32.93  ? 147 GLY A N   1 
ATOM   1071  C  CA  . GLY A  1 148 ? 28.317  256.892 13.905  1.00 30.30  ? 147 GLY A CA  1 
ATOM   1072  C  C   . GLY A  1 148 ? 28.049  256.839 15.397  1.00 35.69  ? 147 GLY A C   1 
ATOM   1073  O  O   . GLY A  1 148 ? 28.695  257.572 16.242  1.00 35.30  ? 147 GLY A O   1 
ATOM   1074  N  N   . VAL A  1 149 ? 27.081  255.984 15.731  1.00 31.37  ? 148 VAL A N   1 
ATOM   1075  C  CA  . VAL A  1 149 ? 26.783  255.676 17.084  1.00 29.69  ? 148 VAL A CA  1 
ATOM   1076  C  C   . VAL A  1 149 ? 27.843  254.731 17.638  1.00 25.44  ? 148 VAL A C   1 
ATOM   1077  O  O   . VAL A  1 149 ? 28.232  253.825 16.959  1.00 23.98  ? 148 VAL A O   1 
ATOM   1078  C  CB  . VAL A  1 149 ? 25.358  255.157 17.214  1.00 29.51  ? 148 VAL A CB  1 
ATOM   1079  C  CG1 . VAL A  1 149 ? 25.014  255.005 18.670  1.00 26.08  ? 148 VAL A CG1 1 
ATOM   1080  C  CG2 . VAL A  1 149 ? 24.439  256.144 16.561  1.00 29.05  ? 148 VAL A CG2 1 
ATOM   1081  N  N   . ILE A  1 150 ? 28.349  255.019 18.839  1.00 26.11  ? 149 ILE A N   1 
ATOM   1082  C  CA  . ILE A  1 150 ? 29.314  254.128 19.504  1.00 28.36  ? 149 ILE A CA  1 
ATOM   1083  C  C   . ILE A  1 150 ? 28.539  252.915 20.134  1.00 28.91  ? 149 ILE A C   1 
ATOM   1084  O  O   . ILE A  1 150 ? 27.666  253.080 21.000  1.00 28.75  ? 149 ILE A O   1 
ATOM   1085  C  CB  . ILE A  1 150 ? 30.112  254.908 20.561  1.00 29.25  ? 149 ILE A CB  1 
ATOM   1086  C  CG1 . ILE A  1 150 ? 30.804  256.132 19.922  1.00 31.08  ? 149 ILE A CG1 1 
ATOM   1087  C  CG2 . ILE A  1 150 ? 31.085  254.001 21.247  1.00 25.59  ? 149 ILE A CG2 1 
ATOM   1088  C  CD1 . ILE A  1 150 ? 31.276  257.224 20.864  1.00 26.03  ? 149 ILE A CD1 1 
ATOM   1089  N  N   . GLY A  1 151 ? 28.836  251.713 19.678  1.00 27.82  ? 150 GLY A N   1 
ATOM   1090  C  CA  . GLY A  1 151 ? 28.114  250.511 20.080  1.00 26.64  ? 150 GLY A CA  1 
ATOM   1091  C  C   . GLY A  1 151 ? 28.962  249.497 20.829  1.00 28.20  ? 150 GLY A C   1 
ATOM   1092  O  O   . GLY A  1 151 ? 30.267  249.448 20.656  1.00 30.95  ? 150 GLY A O   1 
ATOM   1093  N  N   . ILE A  1 152 ? 28.256  248.716 21.674  1.00 28.08  ? 151 ILE A N   1 
ATOM   1094  C  CA  . ILE A  1 152 ? 28.835  247.609 22.387  1.00 29.24  ? 151 ILE A CA  1 
ATOM   1095  C  C   . ILE A  1 152 ? 29.394  246.610 21.363  1.00 30.47  ? 151 ILE A C   1 
ATOM   1096  O  O   . ILE A  1 152 ? 28.717  246.269 20.367  1.00 28.53  ? 151 ILE A O   1 
ATOM   1097  C  CB  . ILE A  1 152 ? 27.862  247.018 23.372  1.00 34.02  ? 151 ILE A CB  1 
ATOM   1098  C  CG1 . ILE A  1 152 ? 27.501  248.110 24.356  1.00 36.20  ? 151 ILE A CG1 1 
ATOM   1099  C  CG2 . ILE A  1 152 ? 28.477  245.932 24.279  1.00 29.96  ? 151 ILE A CG2 1 
ATOM   1100  C  CD1 . ILE A  1 152 ? 26.143  247.909 25.002  1.00 40.54  ? 151 ILE A CD1 1 
ATOM   1101  N  N   . ALA A  1 153 ? 30.678  246.263 21.567  1.00 30.13  ? 152 ALA A N   1 
ATOM   1102  C  CA  . ALA A  1 153 ? 31.416  245.306 20.730  1.00 32.29  ? 152 ALA A CA  1 
ATOM   1103  C  C   . ALA A  1 153 ? 31.761  244.032 21.512  1.00 32.63  ? 152 ALA A C   1 
ATOM   1104  O  O   . ALA A  1 153 ? 31.832  244.027 22.737  1.00 32.57  ? 152 ALA A O   1 
ATOM   1105  C  CB  . ALA A  1 153 ? 32.639  245.925 20.094  1.00 24.39  ? 152 ALA A CB  1 
ATOM   1106  N  N   . GLN A  1 154 ? 31.855  242.948 20.759  1.00 38.38  ? 153 GLN A N   1 
ATOM   1107  C  CA  . GLN A  1 154 ? 32.275  241.624 21.230  1.00 42.47  ? 153 GLN A CA  1 
ATOM   1108  C  C   . GLN A  1 154 ? 33.766  241.549 21.404  1.00 49.50  ? 153 GLN A C   1 
ATOM   1109  O  O   . GLN A  1 154 ? 34.566  241.918 20.478  1.00 45.70  ? 153 GLN A O   1 
ATOM   1110  C  CB  . GLN A  1 154 ? 31.977  240.553 20.200  1.00 43.18  ? 153 GLN A CB  1 
ATOM   1111  C  CG  . GLN A  1 154 ? 32.448  239.184 20.676  1.00 50.83  ? 153 GLN A CG  1 
ATOM   1112  C  CD  . GLN A  1 154 ? 31.909  238.059 19.825  1.00 52.60  ? 153 GLN A CD  1 
ATOM   1113  O  OE1 . GLN A  1 154 ? 32.105  238.043 18.595  1.00 48.03  ? 153 GLN A OE1 1 
ATOM   1114  N  NE2 . GLN A  1 154 ? 31.176  237.120 20.473  1.00 50.59  ? 153 GLN A NE2 1 
ATOM   1115  O  OXT . GLN A  1 154 ? 34.125  240.974 22.449  1.00 54.01  ? 153 GLN A OXT 1 
ATOM   1116  N  N   . MET B  1 1   ? 20.929  258.148 33.749  1.00 54.23  ? 0   MET B N   1 
ATOM   1117  C  CA  . MET B  1 1   ? 20.453  259.426 33.117  1.00 60.80  ? 0   MET B CA  1 
ATOM   1118  C  C   . MET B  1 1   ? 19.391  259.205 31.953  1.00 65.27  ? 0   MET B C   1 
ATOM   1119  O  O   . MET B  1 1   ? 18.363  259.925 31.931  1.00 59.64  ? 0   MET B O   1 
ATOM   1120  C  CB  . MET B  1 1   ? 21.648  260.347 32.663  1.00 50.49  ? 0   MET B CB  1 
ATOM   1121  N  N   . ALA B  1 2   ? 19.605  258.239 31.024  1.00 61.36  ? 1   ALA B N   1 
ATOM   1122  C  CA  . ALA B  1 2   ? 18.794  258.154 29.723  1.00 56.52  ? 1   ALA B CA  1 
ATOM   1123  C  C   . ALA B  1 2   ? 17.259  257.796 29.771  1.00 49.26  ? 1   ALA B C   1 
ATOM   1124  O  O   . ALA B  1 2   ? 16.873  256.729 30.236  1.00 42.56  ? 1   ALA B O   1 
ATOM   1125  C  CB  . ALA B  1 2   ? 19.502  257.276 28.679  1.00 55.54  ? 1   ALA B CB  1 
ATOM   1126  N  N   . THR B  1 3   ? 16.394  258.685 29.267  1.00 43.82  ? 2   THR B N   1 
ATOM   1127  C  CA  . THR B  1 3   ? 14.982  258.378 29.236  1.00 39.98  ? 2   THR B CA  1 
ATOM   1128  C  C   . THR B  1 3   ? 14.409  258.225 27.790  1.00 38.82  ? 2   THR B C   1 
ATOM   1129  O  O   . THR B  1 3   ? 13.225  257.811 27.610  1.00 33.37  ? 2   THR B O   1 
ATOM   1130  C  CB  . THR B  1 3   ? 14.204  259.400 30.066  1.00 42.35  ? 2   THR B CB  1 
ATOM   1131  O  OG1 . THR B  1 3   ? 14.253  260.649 29.422  1.00 38.17  ? 2   THR B OG1 1 
ATOM   1132  C  CG2 . THR B  1 3   ? 14.851  259.589 31.421  1.00 43.39  ? 2   THR B CG2 1 
ATOM   1133  N  N   . LYS B  1 4   ? 15.257  258.548 26.791  1.00 35.21  ? 3   LYS B N   1 
ATOM   1134  C  CA  . LYS B  1 4   ? 14.886  258.530 25.368  1.00 33.40  ? 3   LYS B CA  1 
ATOM   1135  C  C   . LYS B  1 4   ? 15.976  257.962 24.538  1.00 31.65  ? 3   LYS B C   1 
ATOM   1136  O  O   . LYS B  1 4   ? 17.133  258.246 24.787  1.00 32.70  ? 3   LYS B O   1 
ATOM   1137  C  CB  . LYS B  1 4   ? 14.591  259.902 24.879  1.00 33.11  ? 3   LYS B CB  1 
ATOM   1138  C  CG  . LYS B  1 4   ? 13.231  260.320 25.312  1.00 43.45  ? 3   LYS B CG  1 
ATOM   1139  C  CD  . LYS B  1 4   ? 12.970  261.767 24.913  1.00 62.08  ? 3   LYS B CD  1 
ATOM   1140  C  CE  . LYS B  1 4   ? 11.716  262.314 25.604  1.00 76.74  ? 3   LYS B CE  1 
ATOM   1141  N  NZ  . LYS B  1 4   ? 11.582  263.781 25.326  1.00 88.61  ? 3   LYS B NZ  1 
ATOM   1142  N  N   . ALA B  1 5   ? 15.633  257.156 23.555  1.00 28.54  ? 4   ALA B N   1 
ATOM   1143  C  CA  . ALA B  1 5   ? 16.645  256.619 22.717  1.00 31.34  ? 4   ALA B CA  1 
ATOM   1144  C  C   . ALA B  1 5   ? 16.099  256.665 21.263  1.00 33.79  ? 4   ALA B C   1 
ATOM   1145  O  O   . ALA B  1 5   ? 14.919  256.902 21.071  1.00 32.91  ? 4   ALA B O   1 
ATOM   1146  C  CB  . ALA B  1 5   ? 17.032  255.219 23.216  1.00 26.93  ? 4   ALA B CB  1 
ATOM   1147  N  N   . VAL B  1 6   ? 16.946  256.485 20.254  1.00 28.71  ? 5   VAL B N   1 
ATOM   1148  C  CA  . VAL B  1 6   ? 16.459  256.495 18.961  1.00 28.45  ? 5   VAL B CA  1 
ATOM   1149  C  C   . VAL B  1 6   ? 17.340  255.557 18.130  1.00 31.79  ? 5   VAL B C   1 
ATOM   1150  O  O   . VAL B  1 6   ? 18.507  255.321 18.520  1.00 29.82  ? 5   VAL B O   1 
ATOM   1151  C  CB  . VAL B  1 6   ? 16.491  257.945 18.433  1.00 30.42  ? 5   VAL B CB  1 
ATOM   1152  C  CG1 . VAL B  1 6   ? 17.921  258.444 18.306  1.00 25.82  ? 5   VAL B CG1 1 
ATOM   1153  C  CG2 . VAL B  1 6   ? 15.680  258.055 17.138  1.00 26.66  ? 5   VAL B CG2 1 
ATOM   1154  N  N   . CYS B  1 7   ? 16.793  255.054 17.007  1.00 28.08  ? 6   CYS B N   1 
ATOM   1155  C  CA  . CYS B  1 7   ? 17.523  254.184 16.123  1.00 30.01  ? 6   CYS B CA  1 
ATOM   1156  C  C   . CYS B  1 7   ? 17.211  254.407 14.624  1.00 30.26  ? 6   CYS B C   1 
ATOM   1157  O  O   . CYS B  1 7   ? 16.061  254.396 14.219  1.00 29.14  ? 6   CYS B O   1 
ATOM   1158  C  CB  . CYS B  1 7   ? 17.246  252.742 16.512  1.00 32.65  ? 6   CYS B CB  1 
ATOM   1159  S  SG  . CYS B  1 7   ? 18.122  251.556 15.529  1.00 35.11  ? 6   CYS B SG  1 
ATOM   1160  N  N   . VAL B  1 8   ? 18.246  254.601 13.824  1.00 26.97  ? 7   VAL B N   1 
ATOM   1161  C  CA  . VAL B  1 8   ? 18.019  254.678 12.406  1.00 27.97  ? 7   VAL B CA  1 
ATOM   1162  C  C   . VAL B  1 8   ? 18.282  253.326 11.714  1.00 28.55  ? 7   VAL B C   1 
ATOM   1163  O  O   . VAL B  1 8   ? 19.348  252.773 11.826  1.00 29.85  ? 7   VAL B O   1 
ATOM   1164  C  CB  . VAL B  1 8   ? 18.793  255.866 11.775  1.00 28.21  ? 7   VAL B CB  1 
ATOM   1165  C  CG1 . VAL B  1 8   ? 18.455  255.948 10.295  1.00 23.54  ? 7   VAL B CG1 1 
ATOM   1166  C  CG2 . VAL B  1 8   ? 18.479  257.157 12.551  1.00 23.45  ? 7   VAL B CG2 1 
ATOM   1167  N  N   . LEU B  1 9   ? 17.304  252.772 11.008  1.00 29.67  ? 8   LEU B N   1 
ATOM   1168  C  CA  . LEU B  1 9   ? 17.523  251.501 10.411  1.00 29.76  ? 8   LEU B CA  1 
ATOM   1169  C  C   . LEU B  1 9   ? 17.839  251.656 8.940   1.00 31.07  ? 8   LEU B C   1 
ATOM   1170  O  O   . LEU B  1 9   ? 17.097  252.336 8.234   1.00 30.34  ? 8   LEU B O   1 
ATOM   1171  C  CB  . LEU B  1 9   ? 16.277  250.660 10.598  1.00 34.66  ? 8   LEU B CB  1 
ATOM   1172  C  CG  . LEU B  1 9   ? 15.815  250.346 12.032  1.00 39.18  ? 8   LEU B CG  1 
ATOM   1173  C  CD1 . LEU B  1 9   ? 14.355  250.029 12.008  1.00 42.10  ? 8   LEU B CD1 1 
ATOM   1174  C  CD2 . LEU B  1 9   ? 16.414  249.048 12.477  1.00 44.19  ? 8   LEU B CD2 1 
ATOM   1175  N  N   . LYS B  1 10  ? 18.936  251.026 8.499   1.00 31.81  ? 9   LYS B N   1 
ATOM   1176  C  CA  . LYS B  1 10  ? 19.309  250.931 7.074   1.00 33.36  ? 9   LYS B CA  1 
ATOM   1177  C  C   . LYS B  1 10  ? 19.814  249.572 6.765   1.00 33.00  ? 9   LYS B C   1 
ATOM   1178  O  O   . LYS B  1 10  ? 20.317  248.882 7.655   1.00 31.75  ? 9   LYS B O   1 
ATOM   1179  C  CB  . LYS B  1 10  ? 20.440  251.886 6.706   1.00 34.71  ? 9   LYS B CB  1 
ATOM   1180  C  CG  . LYS B  1 10  ? 19.985  253.296 6.583   1.00 47.84  ? 9   LYS B CG  1 
ATOM   1181  C  CD  . LYS B  1 10  ? 21.167  254.238 6.587   1.00 59.24  ? 9   LYS B CD  1 
ATOM   1182  C  CE  . LYS B  1 10  ? 20.613  255.691 6.585   1.00 74.36  ? 9   LYS B CE  1 
ATOM   1183  N  NZ  . LYS B  1 10  ? 21.595  256.656 7.213   1.00 89.41  ? 9   LYS B NZ  1 
ATOM   1184  N  N   . GLY B  1 11  ? 19.758  249.194 5.495   1.00 32.51  ? 10  GLY B N   1 
ATOM   1185  C  CA  . GLY B  1 11  ? 20.384  247.944 5.097   1.00 34.61  ? 10  GLY B CA  1 
ATOM   1186  C  C   . GLY B  1 11  ? 20.863  248.107 3.674   1.00 36.96  ? 10  GLY B C   1 
ATOM   1187  O  O   . GLY B  1 11  ? 20.978  249.251 3.169   1.00 35.57  ? 10  GLY B O   1 
ATOM   1188  N  N   . ASP B  1 12  ? 21.092  246.953 3.032   1.00 37.21  ? 11  ASP B N   1 
ATOM   1189  C  CA  . ASP B  1 12  ? 21.403  246.863 1.577   1.00 39.66  ? 11  ASP B CA  1 
ATOM   1190  C  C   . ASP B  1 12  ? 20.220  247.068 0.663   1.00 37.73  ? 11  ASP B C   1 
ATOM   1191  O  O   . ASP B  1 12  ? 20.401  247.511 -0.414  1.00 42.29  ? 11  ASP B O   1 
ATOM   1192  C  CB  . ASP B  1 12  ? 22.107  245.563 1.232   1.00 39.90  ? 11  ASP B CB  1 
ATOM   1193  C  CG  . ASP B  1 12  ? 23.418  245.426 1.996   1.00 52.95  ? 11  ASP B CG  1 
ATOM   1194  O  OD1 . ASP B  1 12  ? 24.173  246.438 1.991   1.00 52.59  ? 11  ASP B OD1 1 
ATOM   1195  O  OD2 . ASP B  1 12  ? 23.698  244.364 2.603   1.00 52.00  ? 11  ASP B OD2 1 
ATOM   1196  N  N   . GLY B  1 13  ? 19.010  246.770 1.091   1.00 34.62  ? 12  GLY B N   1 
ATOM   1197  C  CA  . GLY B  1 13  ? 17.907  246.977 0.247   1.00 32.22  ? 12  GLY B CA  1 
ATOM   1198  C  C   . GLY B  1 13  ? 17.266  248.296 0.598   1.00 35.45  ? 12  GLY B C   1 
ATOM   1199  O  O   . GLY B  1 13  ? 17.889  249.189 1.171   1.00 35.96  ? 12  GLY B O   1 
ATOM   1200  N  N   . PRO B  1 14  ? 15.978  248.375 0.314   1.00 32.86  ? 13  PRO B N   1 
ATOM   1201  C  CA  . PRO B  1 14  ? 15.174  249.539 0.508   1.00 30.57  ? 13  PRO B CA  1 
ATOM   1202  C  C   . PRO B  1 14  ? 14.619  249.681 1.909   1.00 28.61  ? 13  PRO B C   1 
ATOM   1203  O  O   . PRO B  1 14  ? 13.883  250.596 2.162   1.00 32.48  ? 13  PRO B O   1 
ATOM   1204  C  CB  . PRO B  1 14  ? 14.000  249.290 -0.486  1.00 29.86  ? 13  PRO B CB  1 
ATOM   1205  C  CG  . PRO B  1 14  ? 13.949  247.780 -0.669  1.00 25.63  ? 13  PRO B CG  1 
ATOM   1206  C  CD  . PRO B  1 14  ? 15.219  247.195 -0.205  1.00 27.01  ? 13  PRO B CD  1 
ATOM   1207  N  N   . VAL B  1 15  ? 14.893  248.785 2.823   1.00 29.85  ? 14  VAL B N   1 
ATOM   1208  C  CA  . VAL B  1 15  ? 14.188  248.883 4.093   1.00 32.10  ? 14  VAL B CA  1 
ATOM   1209  C  C   . VAL B  1 15  ? 14.820  249.994 4.870   1.00 31.05  ? 14  VAL B C   1 
ATOM   1210  O  O   . VAL B  1 15  ? 16.033  250.025 5.030   1.00 35.21  ? 14  VAL B O   1 
ATOM   1211  C  CB  . VAL B  1 15  ? 14.154  247.533 4.884   1.00 34.82  ? 14  VAL B CB  1 
ATOM   1212  C  CG1 . VAL B  1 15  ? 13.616  247.727 6.299   1.00 30.67  ? 14  VAL B CG1 1 
ATOM   1213  C  CG2 . VAL B  1 15  ? 13.300  246.507 4.152   1.00 31.43  ? 14  VAL B CG2 1 
ATOM   1214  N  N   . GLN B  1 16  ? 14.026  250.925 5.358   1.00 31.52  ? 15  GLN B N   1 
ATOM   1215  C  CA  . GLN B  1 16  ? 14.621  251.930 6.243   1.00 34.30  ? 15  GLN B CA  1 
ATOM   1216  C  C   . GLN B  1 16  ? 13.567  252.507 7.195   1.00 33.75  ? 15  GLN B C   1 
ATOM   1217  O  O   . GLN B  1 16  ? 12.364  252.410 6.906   1.00 32.34  ? 15  GLN B O   1 
ATOM   1218  C  CB  . GLN B  1 16  ? 15.315  253.032 5.427   1.00 36.36  ? 15  GLN B CB  1 
ATOM   1219  C  CG  . GLN B  1 16  ? 14.358  253.750 4.551   1.00 43.39  ? 15  GLN B CG  1 
ATOM   1220  C  CD  . GLN B  1 16  ? 14.893  255.052 4.040   1.00 52.25  ? 15  GLN B CD  1 
ATOM   1221  O  OE1 . GLN B  1 16  ? 15.663  255.053 3.092   1.00 44.49  ? 15  GLN B OE1 1 
ATOM   1222  N  NE2 . GLN B  1 16  ? 14.462  256.190 4.663   1.00 55.00  ? 15  GLN B NE2 1 
ATOM   1223  N  N   . GLY B  1 17  ? 14.015  253.100 8.309   1.00 29.76  ? 16  GLY B N   1 
ATOM   1224  C  CA  . GLY B  1 17  ? 13.104  253.754 9.222   1.00 27.68  ? 16  GLY B CA  1 
ATOM   1225  C  C   . GLY B  1 17  ? 13.733  254.326 10.447  1.00 28.83  ? 16  GLY B C   1 
ATOM   1226  O  O   . GLY B  1 17  ? 14.936  254.206 10.634  1.00 34.25  ? 16  GLY B O   1 
ATOM   1227  N  N   . ILE B  1 18  ? 12.903  254.912 11.284  1.00 27.64  ? 17  ILE B N   1 
ATOM   1228  C  CA  . ILE B  1 18  ? 13.302  255.538 12.512  1.00 27.93  ? 17  ILE B CA  1 
ATOM   1229  C  C   . ILE B  1 18  ? 12.496  254.948 13.679  1.00 29.07  ? 17  ILE B C   1 
ATOM   1230  O  O   . ILE B  1 18  ? 11.224  254.974 13.661  1.00 30.75  ? 17  ILE B O   1 
ATOM   1231  C  CB  . ILE B  1 18  ? 13.100  257.107 12.388  1.00 31.56  ? 17  ILE B CB  1 
ATOM   1232  C  CG1 . ILE B  1 18  ? 14.081  257.735 11.341  1.00 34.50  ? 17  ILE B CG1 1 
ATOM   1233  C  CG2 . ILE B  1 18  ? 13.167  257.827 13.731  1.00 29.05  ? 17  ILE B CG2 1 
ATOM   1234  C  CD1 . ILE B  1 18  ? 13.778  259.194 11.021  1.00 32.23  ? 17  ILE B CD1 1 
ATOM   1235  N  N   . ILE B  1 19  ? 13.179  254.465 14.722  1.00 28.84  ? 18  ILE B N   1 
ATOM   1236  C  CA  . ILE B  1 19  ? 12.451  253.997 15.881  1.00 27.36  ? 18  ILE B CA  1 
ATOM   1237  C  C   . ILE B  1 19  ? 12.828  254.726 17.131  1.00 28.17  ? 18  ILE B C   1 
ATOM   1238  O  O   . ILE B  1 19  ? 14.015  254.916 17.432  1.00 29.79  ? 18  ILE B O   1 
ATOM   1239  C  CB  . ILE B  1 19  ? 12.626  252.491 16.032  1.00 27.32  ? 18  ILE B CB  1 
ATOM   1240  C  CG1 . ILE B  1 19  ? 12.087  251.719 14.804  1.00 26.93  ? 18  ILE B CG1 1 
ATOM   1241  C  CG2 . ILE B  1 19  ? 11.958  252.021 17.282  1.00 24.28  ? 18  ILE B CG2 1 
ATOM   1242  C  CD1 . ILE B  1 19  ? 10.559  251.706 14.694  1.00 27.04  ? 18  ILE B CD1 1 
ATOM   1243  N  N   . ASN B  1 20  ? 11.806  255.127 17.868  1.00 29.61  ? 19  ASN B N   1 
ATOM   1244  C  CA  . ASN B  1 20  ? 11.954  255.834 19.166  1.00 28.32  ? 19  ASN B CA  1 
ATOM   1245  C  C   . ASN B  1 20  ? 11.708  254.945 20.364  1.00 28.59  ? 19  ASN B C   1 
ATOM   1246  O  O   . ASN B  1 20  ? 10.944  253.965 20.288  1.00 26.20  ? 19  ASN B O   1 
ATOM   1247  C  CB  . ASN B  1 20  ? 11.096  257.062 19.248  1.00 27.70  ? 19  ASN B CB  1 
ATOM   1248  C  CG  . ASN B  1 20  ? 11.226  257.937 17.999  1.00 33.24  ? 19  ASN B CG  1 
ATOM   1249  O  OD1 . ASN B  1 20  ? 10.418  257.823 17.049  1.00 34.51  ? 19  ASN B OD1 1 
ATOM   1250  N  ND2 . ASN B  1 20  ? 12.267  258.749 17.944  1.00 28.09  ? 19  ASN B ND2 1 
ATOM   1251  N  N   . PHE B  1 21  ? 12.443  255.248 21.430  1.00 28.05  ? 20  PHE B N   1 
ATOM   1252  C  CA  . PHE B  1 21  ? 12.323  254.587 22.679  1.00 28.82  ? 20  PHE B CA  1 
ATOM   1253  C  C   . PHE B  1 21  ? 12.132  255.637 23.754  1.00 31.17  ? 20  PHE B C   1 
ATOM   1254  O  O   . PHE B  1 21  ? 12.769  256.661 23.760  1.00 28.79  ? 20  PHE B O   1 
ATOM   1255  C  CB  . PHE B  1 21  ? 13.573  253.789 22.989  1.00 26.81  ? 20  PHE B CB  1 
ATOM   1256  C  CG  . PHE B  1 21  ? 13.884  252.698 22.004  1.00 30.50  ? 20  PHE B CG  1 
ATOM   1257  C  CD1 . PHE B  1 21  ? 14.617  252.968 20.848  1.00 28.77  ? 20  PHE B CD1 1 
ATOM   1258  C  CD2 . PHE B  1 21  ? 13.451  251.356 22.237  1.00 29.46  ? 20  PHE B CD2 1 
ATOM   1259  C  CE1 . PHE B  1 21  ? 14.911  251.951 19.979  1.00 30.43  ? 20  PHE B CE1 1 
ATOM   1260  C  CE2 . PHE B  1 21  ? 13.703  250.342 21.343  1.00 28.93  ? 20  PHE B CE2 1 
ATOM   1261  C  CZ  . PHE B  1 21  ? 14.455  250.624 20.232  1.00 33.30  ? 20  PHE B CZ  1 
ATOM   1262  N  N   . GLU B  1 22  ? 11.222  255.354 24.670  1.00 36.94  ? 21  GLU B N   1 
ATOM   1263  C  CA  . GLU B  1 22  ? 10.995  256.198 25.831  1.00 35.62  ? 21  GLU B CA  1 
ATOM   1264  C  C   . GLU B  1 22  ? 10.671  255.399 27.087  1.00 36.13  ? 21  GLU B C   1 
ATOM   1265  O  O   . GLU B  1 22  ? 9.797   254.524 27.112  1.00 32.69  ? 21  GLU B O   1 
ATOM   1266  C  CB  . GLU B  1 22  ? 9.931   257.207 25.559  1.00 35.44  ? 21  GLU B CB  1 
ATOM   1267  C  CG  . GLU B  1 22  ? 9.817   258.345 26.558  1.00 40.32  ? 21  GLU B CG  1 
ATOM   1268  C  CD  . GLU B  1 22  ? 8.536   259.149 26.260  1.00 52.65  ? 21  GLU B CD  1 
ATOM   1269  O  OE1 . GLU B  1 22  ? 8.581   260.008 25.317  1.00 51.96  ? 21  GLU B OE1 1 
ATOM   1270  O  OE2 . GLU B  1 22  ? 7.459   258.851 26.888  1.00 53.11  ? 21  GLU B OE2 1 
ATOM   1271  N  N   . GLN B  1 23  ? 11.437  255.728 28.119  1.00 35.55  ? 22  GLN B N   1 
ATOM   1272  C  CA  . GLN B  1 23  ? 11.327  255.139 29.420  1.00 37.88  ? 22  GLN B CA  1 
ATOM   1273  C  C   . GLN B  1 23  ? 11.330  256.263 30.438  1.00 38.41  ? 22  GLN B C   1 
ATOM   1274  O  O   . GLN B  1 23  ? 12.361  256.799 30.822  1.00 36.41  ? 22  GLN B O   1 
ATOM   1275  C  CB  . GLN B  1 23  ? 12.502  254.189 29.658  1.00 34.54  ? 22  GLN B CB  1 
ATOM   1276  C  CG  . GLN B  1 23  ? 12.131  253.102 30.596  1.00 31.12  ? 22  GLN B CG  1 
ATOM   1277  C  CD  . GLN B  1 23  ? 13.296  252.263 31.025  1.00 31.57  ? 22  GLN B CD  1 
ATOM   1278  O  OE1 . GLN B  1 23  ? 14.437  252.571 30.727  1.00 31.76  ? 22  GLN B OE1 1 
ATOM   1279  N  NE2 . GLN B  1 23  ? 13.013  251.189 31.730  1.00 28.11  ? 22  GLN B NE2 1 
ATOM   1280  N  N   . LYS B  1 24  ? 10.153  256.613 30.891  1.00 44.63  ? 23  LYS B N   1 
ATOM   1281  C  CA  . LYS B  1 24  ? 10.075  257.644 31.943  1.00 48.26  ? 23  LYS B CA  1 
ATOM   1282  C  C   . LYS B  1 24  ? 10.570  257.290 33.318  1.00 42.96  ? 23  LYS B C   1 
ATOM   1283  O  O   . LYS B  1 24  ? 11.161  258.109 33.971  1.00 43.41  ? 23  LYS B O   1 
ATOM   1284  C  CB  . LYS B  1 24  ? 8.727   258.323 31.971  1.00 47.61  ? 23  LYS B CB  1 
ATOM   1285  C  CG  . LYS B  1 24  ? 8.718   259.447 30.941  1.00 51.82  ? 23  LYS B CG  1 
ATOM   1286  C  CD  . LYS B  1 24  ? 7.312   259.509 30.345  1.00 66.05  ? 23  LYS B CD  1 
ATOM   1287  C  CE  . LYS B  1 24  ? 6.937   260.946 29.924  1.00 69.45  ? 23  LYS B CE  1 
ATOM   1288  N  NZ  . LYS B  1 24  ? 5.537   260.939 29.377  1.00 66.06  ? 23  LYS B NZ  1 
ATOM   1289  N  N   . GLU B  1 25  ? 10.426  256.049 33.739  1.00 43.95  ? 24  GLU B N   1 
ATOM   1290  C  CA  . GLU B  1 25  ? 10.965  255.660 35.056  1.00 41.64  ? 24  GLU B CA  1 
ATOM   1291  C  C   . GLU B  1 25  ? 11.855  254.504 34.777  1.00 41.62  ? 24  GLU B C   1 
ATOM   1292  O  O   . GLU B  1 25  ? 11.527  253.689 33.893  1.00 39.96  ? 24  GLU B O   1 
ATOM   1293  C  CB  . GLU B  1 25  ? 9.798   255.183 35.934  1.00 45.95  ? 24  GLU B CB  1 
ATOM   1294  C  CG  . GLU B  1 25  ? 8.625   256.163 36.083  1.00 53.64  ? 24  GLU B CG  1 
ATOM   1295  C  CD  . GLU B  1 25  ? 9.077   257.450 36.814  1.00 69.49  ? 24  GLU B CD  1 
ATOM   1296  O  OE1 . GLU B  1 25  ? 10.171  257.427 37.480  1.00 61.76  ? 24  GLU B OE1 1 
ATOM   1297  O  OE2 . GLU B  1 25  ? 8.370   258.496 36.710  1.00 67.81  ? 24  GLU B OE2 1 
ATOM   1298  N  N   . SER B  1 26  ? 12.938  254.354 35.531  1.00 41.70  ? 25  SER B N   1 
ATOM   1299  C  CA  . SER B  1 26  ? 13.863  253.236 35.265  1.00 40.48  ? 25  SER B CA  1 
ATOM   1300  C  C   . SER B  1 26  ? 13.235  251.881 35.618  1.00 41.29  ? 25  SER B C   1 
ATOM   1301  O  O   . SER B  1 26  ? 13.677  250.806 35.172  1.00 41.55  ? 25  SER B O   1 
ATOM   1302  C  CB  . SER B  1 26  ? 15.178  253.427 36.031  1.00 44.44  ? 25  SER B CB  1 
ATOM   1303  O  OG  . SER B  1 26  ? 14.904  253.707 37.392  1.00 41.46  ? 25  SER B OG  1 
ATOM   1304  N  N   . ASN B  1 27  ? 12.220  251.904 36.465  1.00 41.11  ? 26  ASN B N   1 
ATOM   1305  C  CA  . ASN B  1 27  ? 11.535  250.638 36.830  1.00 45.68  ? 26  ASN B CA  1 
ATOM   1306  C  C   . ASN B  1 27  ? 10.220  250.432 36.004  1.00 47.14  ? 26  ASN B C   1 
ATOM   1307  O  O   . ASN B  1 27  ? 9.288   249.771 36.485  1.00 45.42  ? 26  ASN B O   1 
ATOM   1308  C  CB  . ASN B  1 27  ? 11.234  250.653 38.339  1.00 42.39  ? 26  ASN B CB  1 
ATOM   1309  C  CG  . ASN B  1 27  ? 10.124  251.663 38.709  1.00 43.67  ? 26  ASN B CG  1 
ATOM   1310  O  OD1 . ASN B  1 27  ? 9.909   252.651 38.008  1.00 44.61  ? 26  ASN B OD1 1 
ATOM   1311  N  ND2 . ASN B  1 27  ? 9.408   251.408 39.802  1.00 45.76  ? 26  ASN B ND2 1 
ATOM   1312  N  N   . GLY B  1 28  ? 10.133  251.045 34.810  1.00 43.51  ? 27  GLY B N   1 
ATOM   1313  C  CA  . GLY B  1 28  ? 8.909   251.101 34.087  1.00 36.53  ? 27  GLY B CA  1 
ATOM   1314  C  C   . GLY B  1 28  ? 9.118   250.654 32.695  1.00 37.11  ? 27  GLY B C   1 
ATOM   1315  O  O   . GLY B  1 28  ? 10.212  250.427 32.235  1.00 36.89  ? 27  GLY B O   1 
ATOM   1316  N  N   . PRO B  1 29  ? 8.030   250.486 31.996  1.00 41.15  ? 28  PRO B N   1 
ATOM   1317  C  CA  . PRO B  1 29  ? 8.179   249.997 30.643  1.00 35.31  ? 28  PRO B CA  1 
ATOM   1318  C  C   . PRO B  1 29  ? 8.770   251.011 29.658  1.00 33.61  ? 28  PRO B C   1 
ATOM   1319  O  O   . PRO B  1 29  ? 8.727   252.235 29.884  1.00 32.19  ? 28  PRO B O   1 
ATOM   1320  C  CB  . PRO B  1 29  ? 6.772   249.655 30.268  1.00 36.46  ? 28  PRO B CB  1 
ATOM   1321  C  CG  . PRO B  1 29  ? 5.922   250.505 31.118  1.00 34.98  ? 28  PRO B CG  1 
ATOM   1322  C  CD  . PRO B  1 29  ? 6.628   250.677 32.397  1.00 35.85  ? 28  PRO B CD  1 
ATOM   1323  N  N   . VAL B  1 30  ? 9.333   250.465 28.583  1.00 31.39  ? 29  VAL B N   1 
ATOM   1324  C  CA  . VAL B  1 30  ? 9.813   251.228 27.482  1.00 30.36  ? 29  VAL B CA  1 
ATOM   1325  C  C   . VAL B  1 30  ? 8.807   251.289 26.341  1.00 31.27  ? 29  VAL B C   1 
ATOM   1326  O  O   . VAL B  1 30  ? 8.326   250.249 25.877  1.00 35.46  ? 29  VAL B O   1 
ATOM   1327  C  CB  . VAL B  1 30  ? 11.063  250.588 26.986  1.00 28.75  ? 29  VAL B CB  1 
ATOM   1328  C  CG1 . VAL B  1 30  ? 11.719  251.502 25.940  1.00 26.65  ? 29  VAL B CG1 1 
ATOM   1329  C  CG2 . VAL B  1 30  ? 11.945  250.343 28.185  1.00 26.77  ? 29  VAL B CG2 1 
ATOM   1330  N  N   . LYS B  1 31  ? 8.476   252.493 25.911  1.00 30.44  ? 30  LYS B N   1 
ATOM   1331  C  CA  . LYS B  1 31  ? 7.643   252.697 24.728  1.00 31.64  ? 30  LYS B CA  1 
ATOM   1332  C  C   . LYS B  1 31  ? 8.459   252.703 23.488  1.00 30.58  ? 30  LYS B C   1 
ATOM   1333  O  O   . LYS B  1 31  ? 9.466   253.401 23.434  1.00 30.95  ? 30  LYS B O   1 
ATOM   1334  C  CB  . LYS B  1 31  ? 6.866   254.002 24.803  1.00 34.31  ? 30  LYS B CB  1 
ATOM   1335  C  CG  . LYS B  1 31  ? 5.636   253.860 25.620  1.00 38.74  ? 30  LYS B CG  1 
ATOM   1336  C  CD  . LYS B  1 31  ? 5.192   255.197 26.205  1.00 48.89  ? 30  LYS B CD  1 
ATOM   1337  C  CE  . LYS B  1 31  ? 3.894   255.045 27.020  1.00 54.78  ? 30  LYS B CE  1 
ATOM   1338  N  NZ  . LYS B  1 31  ? 3.643   253.562 27.256  1.00 57.18  ? 30  LYS B NZ  1 
ATOM   1339  N  N   . VAL B  1 32  ? 8.040   251.924 22.498  1.00 30.53  ? 31  VAL B N   1 
ATOM   1340  C  CA  . VAL B  1 32  ? 8.784   251.795 21.245  1.00 29.77  ? 31  VAL B CA  1 
ATOM   1341  C  C   . VAL B  1 32  ? 7.877   252.132 20.084  1.00 28.36  ? 31  VAL B C   1 
ATOM   1342  O  O   . VAL B  1 32  ? 6.870   251.489 19.923  1.00 32.36  ? 31  VAL B O   1 
ATOM   1343  C  CB  . VAL B  1 32  ? 9.374   250.384 21.056  1.00 28.68  ? 31  VAL B CB  1 
ATOM   1344  C  CG1 . VAL B  1 32  ? 10.319  250.382 19.871  1.00 26.88  ? 31  VAL B CG1 1 
ATOM   1345  C  CG2 . VAL B  1 32  ? 10.038  249.868 22.315  1.00 23.88  ? 31  VAL B CG2 1 
ATOM   1346  N  N   . TRP B  1 33  ? 8.223   253.122 19.276  1.00 27.49  ? 32  TRP B N   1 
ATOM   1347  C  CA  . TRP B  1 33  ? 7.316   253.544 18.226  1.00 29.24  ? 32  TRP B CA  1 
ATOM   1348  C  C   . TRP B  1 33  ? 8.022   254.194 17.089  1.00 29.09  ? 32  TRP B C   1 
ATOM   1349  O  O   . TRP B  1 33  ? 9.028   254.809 17.301  1.00 32.39  ? 32  TRP B O   1 
ATOM   1350  C  CB  . TRP B  1 33  ? 6.156   254.459 18.753  1.00 27.45  ? 32  TRP B CB  1 
ATOM   1351  C  CG  . TRP B  1 33  ? 6.527   255.840 18.920  1.00 31.70  ? 32  TRP B CG  1 
ATOM   1352  C  CD1 . TRP B  1 33  ? 6.322   256.862 18.045  1.00 30.91  ? 32  TRP B CD1 1 
ATOM   1353  C  CD2 . TRP B  1 33  ? 7.293   256.393 20.020  1.00 33.90  ? 32  TRP B CD2 1 
ATOM   1354  N  NE1 . TRP B  1 33  ? 6.814   258.013 18.572  1.00 30.88  ? 32  TRP B NE1 1 
ATOM   1355  C  CE2 . TRP B  1 33  ? 7.415   257.762 19.781  1.00 31.07  ? 32  TRP B CE2 1 
ATOM   1356  C  CE3 . TRP B  1 33  ? 7.835   255.851 21.216  1.00 32.02  ? 32  TRP B CE3 1 
ATOM   1357  C  CZ2 . TRP B  1 33  ? 8.076   258.630 20.686  1.00 35.28  ? 32  TRP B CZ2 1 
ATOM   1358  C  CZ3 . TRP B  1 33  ? 8.479   256.705 22.120  1.00 34.22  ? 32  TRP B CZ3 1 
ATOM   1359  C  CH2 . TRP B  1 33  ? 8.609   258.082 21.852  1.00 34.85  ? 32  TRP B CH2 1 
ATOM   1360  N  N   . GLY B  1 34  ? 7.463   254.086 15.890  1.00 29.17  ? 33  GLY B N   1 
ATOM   1361  C  CA  . GLY B  1 34  ? 8.018   254.791 14.728  1.00 29.21  ? 33  GLY B CA  1 
ATOM   1362  C  C   . GLY B  1 34  ? 7.591   254.162 13.443  1.00 26.50  ? 33  GLY B C   1 
ATOM   1363  O  O   . GLY B  1 34  ? 6.732   253.409 13.451  1.00 31.59  ? 33  GLY B O   1 
ATOM   1364  N  N   . SER B  1 35  ? 8.268   254.418 12.352  1.00 30.27  ? 34  SER B N   1 
ATOM   1365  C  CA  . SER B  1 35  ? 7.885   253.942 11.014  1.00 31.58  ? 34  SER B CA  1 
ATOM   1366  C  C   . SER B  1 35  ? 9.016   253.241 10.306  1.00 33.62  ? 34  SER B C   1 
ATOM   1367  O  O   . SER B  1 35  ? 10.143  253.745 10.389  1.00 35.18  ? 34  SER B O   1 
ATOM   1368  C  CB  . SER B  1 35  ? 7.510   255.115 10.182  1.00 31.69  ? 34  SER B CB  1 
ATOM   1369  O  OG  . SER B  1 35  ? 6.138   255.138 10.127  1.00 40.01  ? 34  SER B OG  1 
ATOM   1370  N  N   . ILE B  1 36  ? 8.752   252.077 9.694   1.00 29.65  ? 35  ILE B N   1 
ATOM   1371  C  CA  . ILE B  1 36  ? 9.693   251.426 8.826   1.00 29.62  ? 35  ILE B CA  1 
ATOM   1372  C  C   . ILE B  1 36  ? 9.001   251.249 7.443   1.00 33.88  ? 35  ILE B C   1 
ATOM   1373  O  O   . ILE B  1 36  ? 7.819   250.849 7.333   1.00 34.49  ? 35  ILE B O   1 
ATOM   1374  C  CB  . ILE B  1 36  ? 10.075  250.069 9.404   1.00 33.26  ? 35  ILE B CB  1 
ATOM   1375  C  CG1 . ILE B  1 36  ? 10.334  250.172 10.925  1.00 32.00  ? 35  ILE B CG1 1 
ATOM   1376  C  CG2 . ILE B  1 36  ? 11.216  249.400 8.603   1.00 27.52  ? 35  ILE B CG2 1 
ATOM   1377  C  CD1 . ILE B  1 36  ? 10.694  248.845 11.590  1.00 30.47  ? 35  ILE B CD1 1 
ATOM   1378  N  N   . LYS B  1 37  ? 9.715   251.591 6.388   1.00 35.67  ? 36  LYS B N   1 
ATOM   1379  C  CA  . LYS B  1 37  ? 9.176   251.540 5.060   1.00 34.22  ? 36  LYS B CA  1 
ATOM   1380  C  C   . LYS B  1 37  ? 10.028  250.684 4.217   1.00 34.15  ? 36  LYS B C   1 
ATOM   1381  O  O   . LYS B  1 37  ? 11.087  250.272 4.656   1.00 37.62  ? 36  LYS B O   1 
ATOM   1382  C  CB  . LYS B  1 37  ? 8.952   252.909 4.459   1.00 34.36  ? 36  LYS B CB  1 
ATOM   1383  C  CG  . LYS B  1 37  ? 10.062  253.895 4.544   1.00 41.36  ? 36  LYS B CG  1 
ATOM   1384  C  CD  . LYS B  1 37  ? 9.507   255.358 4.475   1.00 47.29  ? 36  LYS B CD  1 
ATOM   1385  C  CE  . LYS B  1 37  ? 10.503  256.194 3.625   1.00 55.86  ? 36  LYS B CE  1 
ATOM   1386  N  NZ  . LYS B  1 37  ? 10.186  257.655 3.339   1.00 55.77  ? 36  LYS B NZ  1 
ATOM   1387  N  N   . GLY B  1 38  ? 9.523   250.337 3.041   1.00 32.42  ? 37  GLY B N   1 
ATOM   1388  C  CA  . GLY B  1 38  ? 10.197  249.459 2.134   1.00 30.45  ? 37  GLY B CA  1 
ATOM   1389  C  C   . GLY B  1 38  ? 10.019  248.031 2.520   1.00 31.19  ? 37  GLY B C   1 
ATOM   1390  O  O   . GLY B  1 38  ? 10.825  247.209 2.095   1.00 31.74  ? 37  GLY B O   1 
ATOM   1391  N  N   . LEU B  1 39  ? 8.990   247.708 3.323   1.00 32.01  ? 38  LEU B N   1 
ATOM   1392  C  CA  . LEU B  1 39  ? 8.840   246.327 3.772   1.00 33.29  ? 38  LEU B CA  1 
ATOM   1393  C  C   . LEU B  1 39  ? 7.823   245.607 2.924   1.00 32.85  ? 38  LEU B C   1 
ATOM   1394  O  O   . LEU B  1 39  ? 6.908   246.244 2.446   1.00 38.22  ? 38  LEU B O   1 
ATOM   1395  C  CB  . LEU B  1 39  ? 8.488   246.210 5.265   1.00 31.52  ? 38  LEU B CB  1 
ATOM   1396  C  CG  . LEU B  1 39  ? 9.539   246.373 6.362   1.00 34.51  ? 38  LEU B CG  1 
ATOM   1397  C  CD1 . LEU B  1 39  ? 8.868   246.702 7.695   1.00 35.11  ? 38  LEU B CD1 1 
ATOM   1398  C  CD2 . LEU B  1 39  ? 10.499  245.189 6.541   1.00 35.30  ? 38  LEU B CD2 1 
ATOM   1399  N  N   . THR B  1 40  ? 7.925   244.292 2.784   1.00 32.34  ? 39  THR B N   1 
ATOM   1400  C  CA  . THR B  1 40  ? 6.780   243.526 2.281   1.00 34.82  ? 39  THR B CA  1 
ATOM   1401  C  C   . THR B  1 40  ? 5.631   243.391 3.291   1.00 34.94  ? 39  THR B C   1 
ATOM   1402  O  O   . THR B  1 40  ? 5.862   243.277 4.502   1.00 33.95  ? 39  THR B O   1 
ATOM   1403  C  CB  . THR B  1 40  ? 7.189   242.133 1.865   1.00 34.95  ? 39  THR B CB  1 
ATOM   1404  O  OG1 . THR B  1 40  ? 7.793   241.521 2.979   1.00 42.48  ? 39  THR B OG1 1 
ATOM   1405  C  CG2 . THR B  1 40  ? 8.211   242.191 0.797   1.00 36.66  ? 39  THR B CG2 1 
ATOM   1406  N  N   . GLU B  1 41  ? 4.396   243.354 2.784   1.00 37.70  ? 40  GLU B N   1 
ATOM   1407  C  CA  . GLU B  1 41  ? 3.207   243.190 3.627   1.00 37.52  ? 40  GLU B CA  1 
ATOM   1408  C  C   . GLU B  1 41  ? 3.301   242.020 4.568   1.00 32.31  ? 40  GLU B C   1 
ATOM   1409  O  O   . GLU B  1 41  ? 3.784   240.997 4.181   1.00 33.63  ? 40  GLU B O   1 
ATOM   1410  C  CB  . GLU B  1 41  ? 2.036   242.947 2.762   1.00 38.87  ? 40  GLU B CB  1 
ATOM   1411  C  CG  . GLU B  1 41  ? 0.733   243.229 3.475   1.00 45.62  ? 40  GLU B CG  1 
ATOM   1412  C  CD  . GLU B  1 41  ? -0.395  243.401 2.480   1.00 50.91  ? 40  GLU B CD  1 
ATOM   1413  O  OE1 . GLU B  1 41  ? -0.091  243.455 1.250   1.00 51.37  ? 40  GLU B OE1 1 
ATOM   1414  O  OE2 . GLU B  1 41  ? -1.548  243.512 2.929   1.00 49.04  ? 40  GLU B OE2 1 
ATOM   1415  N  N   . GLY B  1 42  ? 2.857   242.198 5.807   1.00 32.43  ? 41  GLY B N   1 
ATOM   1416  C  CA  . GLY B  1 42  ? 2.857   241.126 6.833   1.00 29.92  ? 41  GLY B CA  1 
ATOM   1417  C  C   . GLY B  1 42  ? 3.832   241.278 7.968   1.00 30.50  ? 41  GLY B C   1 
ATOM   1418  O  O   . GLY B  1 42  ? 4.421   242.344 8.196   1.00 34.36  ? 41  GLY B O   1 
ATOM   1419  N  N   . LEU B  1 43  ? 4.020   240.195 8.662   1.00 29.99  ? 42  LEU B N   1 
ATOM   1420  C  CA  . LEU B  1 43  ? 4.831   240.136 9.824   1.00 29.92  ? 42  LEU B CA  1 
ATOM   1421  C  C   . LEU B  1 43  ? 6.325   240.154 9.582   1.00 31.62  ? 42  LEU B C   1 
ATOM   1422  O  O   . LEU B  1 43  ? 6.828   239.503 8.659   1.00 29.37  ? 42  LEU B O   1 
ATOM   1423  C  CB  . LEU B  1 43  ? 4.503   238.862 10.524  1.00 28.20  ? 42  LEU B CB  1 
ATOM   1424  C  CG  . LEU B  1 43  ? 3.061   238.805 10.996  1.00 32.66  ? 42  LEU B CG  1 
ATOM   1425  C  CD1 . LEU B  1 43  ? 2.811   237.479 11.689  1.00 28.58  ? 42  LEU B CD1 1 
ATOM   1426  C  CD2 . LEU B  1 43  ? 2.678   240.008 11.879  1.00 39.84  ? 42  LEU B CD2 1 
ATOM   1427  N  N   . HIS B  1 44  ? 7.035   240.903 10.429  1.00 31.01  ? 43  HIS B N   1 
ATOM   1428  C  CA  . HIS B  1 44  ? 8.514   240.868 10.398  1.00 29.98  ? 43  HIS B CA  1 
ATOM   1429  C  C   . HIS B  1 44  ? 9.084   240.827 11.791  1.00 26.31  ? 43  HIS B C   1 
ATOM   1430  O  O   . HIS B  1 44  ? 8.738   241.642 12.635  1.00 26.41  ? 43  HIS B O   1 
ATOM   1431  C  CB  . HIS B  1 44  ? 9.061   242.096 9.662   1.00 30.56  ? 43  HIS B CB  1 
ATOM   1432  C  CG  . HIS B  1 44  ? 8.753   242.134 8.201   1.00 31.70  ? 43  HIS B CG  1 
ATOM   1433  N  ND1 . HIS B  1 44  ? 9.575   241.548 7.247   1.00 32.37  ? 43  HIS B ND1 1 
ATOM   1434  C  CD2 . HIS B  1 44  ? 7.732   242.702 7.522   1.00 29.53  ? 43  HIS B CD2 1 
ATOM   1435  C  CE1 . HIS B  1 44  ? 9.069   241.756 6.051   1.00 29.85  ? 43  HIS B CE1 1 
ATOM   1436  N  NE2 . HIS B  1 44  ? 7.966   242.472 6.184   1.00 32.61  ? 43  HIS B NE2 1 
ATOM   1437  N  N   . GLY B  1 45  ? 9.956   239.888 12.031  1.00 24.39  ? 44  GLY B N   1 
ATOM   1438  C  CA  . GLY B  1 45  ? 10.640  239.851 13.301  1.00 26.89  ? 44  GLY B CA  1 
ATOM   1439  C  C   . GLY B  1 45  ? 11.378  241.158 13.588  1.00 27.54  ? 44  GLY B C   1 
ATOM   1440  O  O   . GLY B  1 45  ? 11.918  241.793 12.669  1.00 28.17  ? 44  GLY B O   1 
ATOM   1441  N  N   . PHE B  1 46  ? 11.337  241.563 14.855  1.00 26.47  ? 45  PHE B N   1 
ATOM   1442  C  CA  . PHE B  1 46  ? 11.781  242.855 15.321  1.00 26.24  ? 45  PHE B CA  1 
ATOM   1443  C  C   . PHE B  1 46  ? 12.531  242.557 16.586  1.00 26.68  ? 45  PHE B C   1 
ATOM   1444  O  O   . PHE B  1 46  ? 11.919  242.251 17.575  1.00 25.36  ? 45  PHE B O   1 
ATOM   1445  C  CB  . PHE B  1 46  ? 10.600  243.675 15.642  1.00 25.28  ? 45  PHE B CB  1 
ATOM   1446  C  CG  . PHE B  1 46  ? 10.863  245.121 15.836  1.00 26.95  ? 45  PHE B CG  1 
ATOM   1447  C  CD1 . PHE B  1 46  ? 11.361  245.898 14.818  1.00 28.53  ? 45  PHE B CD1 1 
ATOM   1448  C  CD2 . PHE B  1 46  ? 10.506  245.744 17.021  1.00 24.43  ? 45  PHE B CD2 1 
ATOM   1449  C  CE1 . PHE B  1 46  ? 11.516  247.267 14.988  1.00 28.24  ? 45  PHE B CE1 1 
ATOM   1450  C  CE2 . PHE B  1 46  ? 10.651  247.107 17.210  1.00 25.36  ? 45  PHE B CE2 1 
ATOM   1451  C  CZ  . PHE B  1 46  ? 11.168  247.888 16.185  1.00 27.45  ? 45  PHE B CZ  1 
ATOM   1452  N  N   . HIS B  1 47  ? 13.872  242.604 16.501  1.00 25.11  ? 46  HIS B N   1 
ATOM   1453  C  CA  . HIS B  1 47  ? 14.756  242.170 17.585  1.00 27.24  ? 46  HIS B CA  1 
ATOM   1454  C  C   . HIS B  1 47  ? 15.926  243.101 17.942  1.00 26.25  ? 46  HIS B C   1 
ATOM   1455  O  O   . HIS B  1 47  ? 16.510  243.755 17.101  1.00 29.14  ? 46  HIS B O   1 
ATOM   1456  C  CB  . HIS B  1 47  ? 15.297  240.724 17.386  1.00 25.73  ? 46  HIS B CB  1 
ATOM   1457  C  CG  . HIS B  1 47  ? 14.272  239.744 16.941  1.00 28.78  ? 46  HIS B CG  1 
ATOM   1458  N  ND1 . HIS B  1 47  ? 14.266  239.196 15.674  1.00 30.37  ? 46  HIS B ND1 1 
ATOM   1459  C  CD2 . HIS B  1 47  ? 13.185  239.251 17.571  1.00 28.38  ? 46  HIS B CD2 1 
ATOM   1460  C  CE1 . HIS B  1 47  ? 13.227  238.404 15.551  1.00 27.89  ? 46  HIS B CE1 1 
ATOM   1461  N  NE2 . HIS B  1 47  ? 12.552  238.426 16.688  1.00 28.78  ? 46  HIS B NE2 1 
ATOM   1462  N  N   . VAL B  1 48  ? 16.236  243.144 19.219  1.00 26.30  ? 47  VAL B N   1 
ATOM   1463  C  CA  . VAL B  1 48  ? 17.437  243.772 19.715  1.00 27.65  ? 47  VAL B CA  1 
ATOM   1464  C  C   . VAL B  1 48  ? 18.482  242.673 19.767  1.00 27.79  ? 47  VAL B C   1 
ATOM   1465  O  O   . VAL B  1 48  ? 18.371  241.689 20.532  1.00 27.57  ? 47  VAL B O   1 
ATOM   1466  C  CB  . VAL B  1 48  ? 17.251  244.474 21.105  1.00 28.01  ? 47  VAL B CB  1 
ATOM   1467  C  CG1 . VAL B  1 48  ? 18.553  245.123 21.540  1.00 23.30  ? 47  VAL B CG1 1 
ATOM   1468  C  CG2 . VAL B  1 48  ? 16.049  245.458 21.140  1.00 25.22  ? 47  VAL B CG2 1 
ATOM   1469  N  N   . HIS B  1 49  ? 19.480  242.833 18.921  1.00 27.00  ? 48  HIS B N   1 
ATOM   1470  C  CA  . HIS B  1 49  ? 20.657  241.961 18.914  1.00 26.25  ? 48  HIS B CA  1 
ATOM   1471  C  C   . HIS B  1 49  ? 21.768  242.438 19.786  1.00 26.83  ? 48  HIS B C   1 
ATOM   1472  O  O   . HIS B  1 49  ? 21.801  243.569 20.094  1.00 26.49  ? 48  HIS B O   1 
ATOM   1473  C  CB  . HIS B  1 49  ? 21.161  241.808 17.537  1.00 22.70  ? 48  HIS B CB  1 
ATOM   1474  C  CG  . HIS B  1 49  ? 20.215  241.071 16.661  1.00 24.79  ? 48  HIS B CG  1 
ATOM   1475  N  ND1 . HIS B  1 49  ? 20.558  239.903 16.026  1.00 21.87  ? 48  HIS B ND1 1 
ATOM   1476  C  CD2 . HIS B  1 49  ? 18.909  241.316 16.349  1.00 25.49  ? 48  HIS B CD2 1 
ATOM   1477  C  CE1 . HIS B  1 49  ? 19.548  239.523 15.273  1.00 26.07  ? 48  HIS B CE1 1 
ATOM   1478  N  NE2 . HIS B  1 49  ? 18.537  240.371 15.439  1.00 26.33  ? 48  HIS B NE2 1 
ATOM   1479  N  N   . GLU B  1 50  ? 22.676  241.536 20.174  1.00 29.90  ? 49  GLU B N   1 
ATOM   1480  C  CA  . GLU B  1 50  ? 23.606  241.767 21.233  1.00 29.04  ? 49  GLU B CA  1 
ATOM   1481  C  C   . GLU B  1 50  ? 24.604  242.946 21.031  1.00 31.59  ? 49  GLU B C   1 
ATOM   1482  O  O   . GLU B  1 50  ? 24.825  243.715 21.966  1.00 30.50  ? 49  GLU B O   1 
ATOM   1483  C  CB  . GLU B  1 50  ? 24.307  240.478 21.584  1.00 30.08  ? 49  GLU B CB  1 
ATOM   1484  C  CG  . GLU B  1 50  ? 25.317  240.677 22.668  1.00 30.91  ? 49  GLU B CG  1 
ATOM   1485  C  CD  . GLU B  1 50  ? 25.954  239.429 23.190  1.00 37.49  ? 49  GLU B CD  1 
ATOM   1486  O  OE1 . GLU B  1 50  ? 25.926  238.306 22.671  1.00 35.12  ? 49  GLU B OE1 1 
ATOM   1487  O  OE2 . GLU B  1 50  ? 26.616  239.631 24.185  1.00 45.82  ? 49  GLU B OE2 1 
ATOM   1488  N  N   . PHE B  1 51  ? 25.137  243.144 19.823  1.00 31.84  ? 50  PHE B N   1 
ATOM   1489  C  CA  . PHE B  1 51  ? 26.260  244.079 19.600  1.00 30.87  ? 50  PHE B CA  1 
ATOM   1490  C  C   . PHE B  1 51  ? 25.879  245.243 18.733  1.00 31.19  ? 50  PHE B C   1 
ATOM   1491  O  O   . PHE B  1 51  ? 25.207  245.065 17.736  1.00 33.20  ? 50  PHE B O   1 
ATOM   1492  C  CB  . PHE B  1 51  ? 27.469  243.375 18.965  1.00 31.30  ? 50  PHE B CB  1 
ATOM   1493  C  CG  . PHE B  1 51  ? 27.922  242.141 19.709  1.00 31.85  ? 50  PHE B CG  1 
ATOM   1494  C  CD1 . PHE B  1 51  ? 28.327  242.226 21.050  1.00 33.55  ? 50  PHE B CD1 1 
ATOM   1495  C  CD2 . PHE B  1 51  ? 27.933  240.897 19.078  1.00 33.21  ? 50  PHE B CD2 1 
ATOM   1496  C  CE1 . PHE B  1 51  ? 28.713  241.092 21.751  1.00 33.26  ? 50  PHE B CE1 1 
ATOM   1497  C  CE2 . PHE B  1 51  ? 28.316  239.753 19.767  1.00 36.76  ? 50  PHE B CE2 1 
ATOM   1498  C  CZ  . PHE B  1 51  ? 28.685  239.854 21.113  1.00 35.21  ? 50  PHE B CZ  1 
ATOM   1499  N  N   . GLY B  1 52  ? 26.356  246.425 19.085  1.00 27.49  ? 51  GLY B N   1 
ATOM   1500  C  CA  . GLY B  1 52  ? 26.155  247.625 18.287  1.00 29.02  ? 51  GLY B CA  1 
ATOM   1501  C  C   . GLY B  1 52  ? 27.291  247.723 17.259  1.00 29.78  ? 51  GLY B C   1 
ATOM   1502  O  O   . GLY B  1 52  ? 27.992  248.732 17.151  1.00 27.70  ? 51  GLY B O   1 
ATOM   1503  N  N   . ASP B  1 53  ? 27.516  246.606 16.583  1.00 31.28  ? 52  ASP B N   1 
ATOM   1504  C  CA  . ASP B  1 53  ? 28.623  246.410 15.718  1.00 30.91  ? 52  ASP B CA  1 
ATOM   1505  C  C   . ASP B  1 53  ? 28.082  246.331 14.315  1.00 31.38  ? 52  ASP B C   1 
ATOM   1506  O  O   . ASP B  1 53  ? 27.459  245.370 13.908  1.00 34.93  ? 52  ASP B O   1 
ATOM   1507  C  CB  . ASP B  1 53  ? 29.389  245.166 16.132  1.00 29.53  ? 52  ASP B CB  1 
ATOM   1508  C  CG  . ASP B  1 53  ? 30.699  244.994 15.349  1.00 34.08  ? 52  ASP B CG  1 
ATOM   1509  O  OD1 . ASP B  1 53  ? 30.802  245.389 14.145  1.00 35.04  ? 52  ASP B OD1 1 
ATOM   1510  O  OD2 . ASP B  1 53  ? 31.661  244.486 15.950  1.00 34.41  ? 52  ASP B OD2 1 
ATOM   1511  N  N   . ASN B  1 54  ? 28.330  247.357 13.569  1.00 32.57  ? 53  ASN B N   1 
ATOM   1512  C  CA  . ASN B  1 54  ? 27.968  247.342 12.202  1.00 32.54  ? 53  ASN B CA  1 
ATOM   1513  C  C   . ASN B  1 54  ? 29.143  247.230 11.207  1.00 31.79  ? 53  ASN B C   1 
ATOM   1514  O  O   . ASN B  1 54  ? 29.012  247.563 10.075  1.00 32.35  ? 53  ASN B O   1 
ATOM   1515  C  CB  . ASN B  1 54  ? 27.041  248.494 11.935  1.00 35.43  ? 53  ASN B CB  1 
ATOM   1516  C  CG  . ASN B  1 54  ? 26.222  248.308 10.639  1.00 50.30  ? 53  ASN B CG  1 
ATOM   1517  O  OD1 . ASN B  1 54  ? 25.478  247.305 10.506  1.00 53.22  ? 53  ASN B OD1 1 
ATOM   1518  N  ND2 . ASN B  1 54  ? 26.369  249.268 9.645   1.00 43.61  ? 53  ASN B ND2 1 
ATOM   1519  N  N   . THR B  1 55  ? 30.280  246.685 11.600  1.00 33.04  ? 54  THR B N   1 
ATOM   1520  C  CA  . THR B  1 55  ? 31.378  246.660 10.647  1.00 33.89  ? 54  THR B CA  1 
ATOM   1521  C  C   . THR B  1 55  ? 31.136  245.834 9.415   1.00 34.61  ? 54  THR B C   1 
ATOM   1522  O  O   . THR B  1 55  ? 31.596  246.172 8.371   1.00 39.05  ? 54  THR B O   1 
ATOM   1523  C  CB  . THR B  1 55  ? 32.671  246.230 11.297  1.00 33.79  ? 54  THR B CB  1 
ATOM   1524  O  OG1 . THR B  1 55  ? 32.466  244.972 11.869  1.00 35.34  ? 54  THR B OG1 1 
ATOM   1525  C  CG2 . THR B  1 55  ? 32.999  247.163 12.376  1.00 29.16  ? 54  THR B CG2 1 
ATOM   1526  N  N   . ALA B  1 56  ? 30.406  244.740 9.543   1.00 38.36  ? 55  ALA B N   1 
ATOM   1527  C  CA  . ALA B  1 56  ? 30.095  243.866 8.443   1.00 36.71  ? 55  ALA B CA  1 
ATOM   1528  C  C   . ALA B  1 56  ? 28.622  243.943 8.150   1.00 35.91  ? 55  ALA B C   1 
ATOM   1529  O  O   . ALA B  1 56  ? 27.987  242.948 7.845   1.00 40.76  ? 55  ALA B O   1 
ATOM   1530  C  CB  . ALA B  1 56  ? 30.504  242.432 8.754   1.00 32.24  ? 55  ALA B CB  1 
ATOM   1531  N  N   . GLY B  1 57  ? 28.053  245.126 8.217   1.00 35.64  ? 56  GLY B N   1 
ATOM   1532  C  CA  . GLY B  1 57  ? 26.596  245.177 8.057   1.00 40.67  ? 56  GLY B CA  1 
ATOM   1533  C  C   . GLY B  1 57  ? 25.850  244.551 9.268   1.00 39.95  ? 56  GLY B C   1 
ATOM   1534  O  O   . GLY B  1 57  ? 26.438  244.458 10.376  1.00 42.52  ? 56  GLY B O   1 
ATOM   1535  N  N   . CYS B  1 58  ? 24.608  244.107 9.049   1.00 33.64  ? 57  CYS B N   1 
ATOM   1536  C  CA  . CYS B  1 58  ? 23.704  243.597 10.102  1.00 31.94  ? 57  CYS B CA  1 
ATOM   1537  C  C   . CYS B  1 58  ? 24.205  242.303 10.740  1.00 31.90  ? 57  CYS B C   1 
ATOM   1538  O  O   . CYS B  1 58  ? 23.933  242.094 11.894  1.00 30.17  ? 57  CYS B O   1 
ATOM   1539  C  CB  . CYS B  1 58  ? 22.274  243.467 9.610   1.00 30.82  ? 57  CYS B CB  1 
ATOM   1540  S  SG  . CYS B  1 58  ? 21.496  245.053 9.117   1.00 40.71  ? 57  CYS B SG  1 
ATOM   1541  N  N   . THR B  1 59  ? 25.015  241.524 10.019  1.00 28.70  ? 58  THR B N   1 
ATOM   1542  C  CA  . THR B  1 59  ? 25.534  240.283 10.465  1.00 32.51  ? 58  THR B CA  1 
ATOM   1543  C  C   . THR B  1 59  ? 26.386  240.471 11.729  1.00 32.60  ? 58  THR B C   1 
ATOM   1544  O  O   . THR B  1 59  ? 26.417  239.595 12.525  1.00 33.77  ? 58  THR B O   1 
ATOM   1545  C  CB  . THR B  1 59  ? 26.461  239.697 9.378   1.00 41.47  ? 58  THR B CB  1 
ATOM   1546  O  OG1 . THR B  1 59  ? 25.848  239.826 8.129   1.00 50.33  ? 58  THR B OG1 1 
ATOM   1547  C  CG2 . THR B  1 59  ? 26.696  238.265 9.528   1.00 40.49  ? 58  THR B CG2 1 
ATOM   1548  N  N   . SER B  1 60  ? 27.074  241.602 11.886  1.00 31.72  ? 59  SER B N   1 
ATOM   1549  C  CA  . SER B  1 60  ? 27.992  241.875 13.019  1.00 33.72  ? 59  SER B CA  1 
ATOM   1550  C  C   . SER B  1 60  ? 27.311  242.116 14.363  1.00 33.52  ? 59  SER B C   1 
ATOM   1551  O  O   . SER B  1 60  ? 27.956  242.184 15.395  1.00 32.82  ? 59  SER B O   1 
ATOM   1552  C  CB  . SER B  1 60  ? 28.789  243.150 12.750  1.00 33.60  ? 59  SER B CB  1 
ATOM   1553  O  OG  . SER B  1 60  ? 29.346  243.177 11.501  1.00 34.58  ? 59  SER B OG  1 
ATOM   1554  N  N   . ALA B  1 61  ? 26.008  242.357 14.311  1.00 33.85  ? 60  ALA B N   1 
ATOM   1555  C  CA  . ALA B  1 61  ? 25.209  242.622 15.503  1.00 31.37  ? 60  ALA B CA  1 
ATOM   1556  C  C   . ALA B  1 61  ? 25.079  241.386 16.379  1.00 30.15  ? 60  ALA B C   1 
ATOM   1557  O  O   . ALA B  1 61  ? 24.778  241.497 17.538  1.00 29.83  ? 60  ALA B O   1 
ATOM   1558  C  CB  . ALA B  1 61  ? 23.855  243.168 15.109  1.00 27.06  ? 60  ALA B CB  1 
ATOM   1559  N  N   . GLY B  1 62  ? 25.377  240.209 15.850  1.00 31.23  ? 61  GLY B N   1 
ATOM   1560  C  CA  . GLY B  1 62  ? 25.418  239.035 16.707  1.00 32.50  ? 61  GLY B CA  1 
ATOM   1561  C  C   . GLY B  1 62  ? 24.039  238.471 16.908  1.00 29.72  ? 61  GLY B C   1 
ATOM   1562  O  O   . GLY B  1 62  ? 23.135  238.834 16.165  1.00 29.83  ? 61  GLY B O   1 
ATOM   1563  N  N   . PRO B  1 63  ? 23.872  237.580 17.900  1.00 31.71  ? 62  PRO B N   1 
ATOM   1564  C  CA  . PRO B  1 63  ? 22.582  236.964 18.146  1.00 30.90  ? 62  PRO B CA  1 
ATOM   1565  C  C   . PRO B  1 63  ? 21.643  237.906 18.880  1.00 28.29  ? 62  PRO B C   1 
ATOM   1566  O  O   . PRO B  1 63  ? 21.981  239.019 19.141  1.00 27.21  ? 62  PRO B O   1 
ATOM   1567  C  CB  . PRO B  1 63  ? 22.968  235.709 18.944  1.00 27.18  ? 62  PRO B CB  1 
ATOM   1568  C  CG  . PRO B  1 63  ? 24.130  236.140 19.684  1.00 26.72  ? 62  PRO B CG  1 
ATOM   1569  C  CD  . PRO B  1 63  ? 24.900  236.919 18.713  1.00 29.49  ? 62  PRO B CD  1 
ATOM   1570  N  N   . HIS B  1 64  ? 20.429  237.478 19.163  1.00 31.28  ? 63  HIS B N   1 
ATOM   1571  C  CA  . HIS B  1 64  ? 19.552  238.266 20.023  1.00 30.76  ? 63  HIS B CA  1 
ATOM   1572  C  C   . HIS B  1 64  ? 20.185  238.669 21.342  1.00 32.14  ? 63  HIS B C   1 
ATOM   1573  O  O   . HIS B  1 64  ? 20.983  237.916 21.855  1.00 35.23  ? 63  HIS B O   1 
ATOM   1574  C  CB  . HIS B  1 64  ? 18.272  237.512 20.238  1.00 28.99  ? 63  HIS B CB  1 
ATOM   1575  C  CG  . HIS B  1 64  ? 17.480  237.319 18.978  1.00 31.22  ? 63  HIS B CG  1 
ATOM   1576  N  ND1 . HIS B  1 64  ? 16.317  236.592 18.932  1.00 30.60  ? 63  HIS B ND1 1 
ATOM   1577  C  CD2 . HIS B  1 64  ? 17.695  237.747 17.709  1.00 29.80  ? 63  HIS B CD2 1 
ATOM   1578  C  CE1 . HIS B  1 64  ? 15.848  236.570 17.699  1.00 29.04  ? 63  HIS B CE1 1 
ATOM   1579  N  NE2 . HIS B  1 64  ? 16.654  237.277 16.939  1.00 30.52  ? 63  HIS B NE2 1 
ATOM   1580  N  N   . PHE B  1 65  ? 19.866  239.864 21.865  1.00 30.72  ? 64  PHE B N   1 
ATOM   1581  C  CA  . PHE B  1 65  ? 20.338  240.229 23.138  1.00 28.39  ? 64  PHE B CA  1 
ATOM   1582  C  C   . PHE B  1 65  ? 19.673  239.332 24.185  1.00 30.05  ? 64  PHE B C   1 
ATOM   1583  O  O   . PHE B  1 65  ? 18.434  239.286 24.314  1.00 27.13  ? 64  PHE B O   1 
ATOM   1584  C  CB  . PHE B  1 65  ? 20.130  241.728 23.378  1.00 30.02  ? 64  PHE B CB  1 
ATOM   1585  C  CG  . PHE B  1 65  ? 20.611  242.203 24.757  1.00 27.68  ? 64  PHE B CG  1 
ATOM   1586  C  CD1 . PHE B  1 65  ? 21.844  241.806 25.272  1.00 26.77  ? 64  PHE B CD1 1 
ATOM   1587  C  CD2 . PHE B  1 65  ? 19.842  243.054 25.493  1.00 26.39  ? 64  PHE B CD2 1 
ATOM   1588  C  CE1 . PHE B  1 65  ? 22.273  242.235 26.547  1.00 26.83  ? 64  PHE B CE1 1 
ATOM   1589  C  CE2 . PHE B  1 65  ? 20.251  243.523 26.736  1.00 26.73  ? 64  PHE B CE2 1 
ATOM   1590  C  CZ  . PHE B  1 65  ? 21.464  243.087 27.281  1.00 27.72  ? 64  PHE B CZ  1 
ATOM   1591  N  N   . ASN B  1 66  ? 20.526  238.579 24.879  1.00 30.17  ? 65  ASN B N   1 
ATOM   1592  C  CA  . ASN B  1 66  ? 20.107  237.404 25.657  1.00 31.04  ? 65  ASN B CA  1 
ATOM   1593  C  C   . ASN B  1 66  ? 20.949  237.295 26.909  1.00 32.07  ? 65  ASN B C   1 
ATOM   1594  O  O   . ASN B  1 66  ? 21.576  236.314 27.131  1.00 34.05  ? 65  ASN B O   1 
ATOM   1595  C  CB  . ASN B  1 66  ? 20.228  236.073 24.859  1.00 30.65  ? 65  ASN B CB  1 
ATOM   1596  C  CG  . ASN B  1 66  ? 19.514  234.859 25.557  1.00 35.94  ? 65  ASN B CG  1 
ATOM   1597  O  OD1 . ASN B  1 66  ? 18.709  235.034 26.463  1.00 35.54  ? 65  ASN B OD1 1 
ATOM   1598  N  ND2 . ASN B  1 66  ? 19.828  233.625 25.135  1.00 36.32  ? 65  ASN B ND2 1 
ATOM   1599  N  N   . PRO B  1 67  ? 20.953  238.286 27.758  1.00 33.28  ? 66  PRO B N   1 
ATOM   1600  C  CA  . PRO B  1 67  ? 21.856  238.147 28.950  1.00 36.34  ? 66  PRO B CA  1 
ATOM   1601  C  C   . PRO B  1 67  ? 21.411  237.094 30.000  1.00 36.97  ? 66  PRO B C   1 
ATOM   1602  O  O   . PRO B  1 67  ? 22.240  236.603 30.732  1.00 35.55  ? 66  PRO B O   1 
ATOM   1603  C  CB  . PRO B  1 67  ? 21.817  239.550 29.563  1.00 35.90  ? 66  PRO B CB  1 
ATOM   1604  C  CG  . PRO B  1 67  ? 20.410  240.025 29.199  1.00 35.74  ? 66  PRO B CG  1 
ATOM   1605  C  CD  . PRO B  1 67  ? 20.172  239.533 27.784  1.00 31.79  ? 66  PRO B CD  1 
ATOM   1606  N  N   . LEU B  1 68  ? 20.139  236.727 30.050  1.00 34.04  ? 67  LEU B N   1 
ATOM   1607  C  CA  . LEU B  1 68  ? 19.738  235.653 30.909  1.00 32.20  ? 67  LEU B CA  1 
ATOM   1608  C  C   . LEU B  1 68  ? 19.859  234.283 30.282  1.00 35.06  ? 67  LEU B C   1 
ATOM   1609  O  O   . LEU B  1 68  ? 19.457  233.311 30.872  1.00 42.06  ? 67  LEU B O   1 
ATOM   1610  C  CB  . LEU B  1 68  ? 18.334  235.874 31.448  1.00 31.82  ? 67  LEU B CB  1 
ATOM   1611  C  CG  . LEU B  1 68  ? 18.392  237.107 32.341  1.00 35.71  ? 67  LEU B CG  1 
ATOM   1612  C  CD1 . LEU B  1 68  ? 16.957  237.455 32.697  1.00 32.03  ? 67  LEU B CD1 1 
ATOM   1613  C  CD2 . LEU B  1 68  ? 19.317  236.814 33.542  1.00 32.44  ? 67  LEU B CD2 1 
ATOM   1614  N  N   . SER B  1 69  ? 20.420  234.154 29.098  1.00 35.73  ? 68  SER B N   1 
ATOM   1615  C  CA  . SER B  1 69  ? 20.576  232.808 28.490  1.00 36.66  ? 68  SER B CA  1 
ATOM   1616  C  C   . SER B  1 69  ? 19.302  231.930 28.401  1.00 34.31  ? 68  SER B C   1 
ATOM   1617  O  O   . SER B  1 69  ? 19.323  230.757 28.655  1.00 38.92  ? 68  SER B O   1 
ATOM   1618  C  CB  . SER B  1 69  ? 21.725  232.046 29.163  1.00 36.72  ? 68  SER B CB  1 
ATOM   1619  O  OG  . SER B  1 69  ? 22.970  232.416 28.621  1.00 41.47  ? 68  SER B OG  1 
ATOM   1620  N  N   . ARG B  1 70  ? 18.214  232.512 27.977  1.00 32.94  ? 69  ARG B N   1 
ATOM   1621  C  CA  . ARG B  1 70  ? 17.006  231.813 27.742  1.00 34.79  ? 69  ARG B CA  1 
ATOM   1622  C  C   . ARG B  1 70  ? 16.812  231.400 26.308  1.00 33.37  ? 69  ARG B C   1 
ATOM   1623  O  O   . ARG B  1 70  ? 17.521  231.804 25.434  1.00 38.47  ? 69  ARG B O   1 
ATOM   1624  C  CB  . ARG B  1 70  ? 15.923  232.771 28.097  1.00 37.36  ? 69  ARG B CB  1 
ATOM   1625  C  CG  . ARG B  1 70  ? 16.191  233.377 29.413  1.00 39.30  ? 69  ARG B CG  1 
ATOM   1626  C  CD  . ARG B  1 70  ? 15.716  232.455 30.504  1.00 47.55  ? 69  ARG B CD  1 
ATOM   1627  N  NE  . ARG B  1 70  ? 15.063  233.273 31.536  1.00 57.68  ? 69  ARG B NE  1 
ATOM   1628  C  CZ  . ARG B  1 70  ? 15.562  233.457 32.771  1.00 69.97  ? 69  ARG B CZ  1 
ATOM   1629  N  NH1 . ARG B  1 70  ? 16.762  232.840 33.137  1.00 50.54  ? 69  ARG B NH1 1 
ATOM   1630  N  NH2 . ARG B  1 70  ? 14.858  234.275 33.621  1.00 56.09  ? 69  ARG B NH2 1 
ATOM   1631  N  N   . LYS B  1 71  ? 15.818  230.613 26.052  1.00 34.21  ? 70  LYS B N   1 
ATOM   1632  C  CA  . LYS B  1 71  ? 15.427  230.356 24.678  1.00 38.53  ? 70  LYS B CA  1 
ATOM   1633  C  C   . LYS B  1 71  ? 14.555  231.497 24.134  1.00 35.30  ? 70  LYS B C   1 
ATOM   1634  O  O   . LYS B  1 71  ? 13.884  232.197 24.903  1.00 32.64  ? 70  LYS B O   1 
ATOM   1635  C  CB  . LYS B  1 71  ? 14.637  229.041 24.602  1.00 43.37  ? 70  LYS B CB  1 
ATOM   1636  C  CG  . LYS B  1 71  ? 15.452  227.776 24.910  1.00 47.65  ? 70  LYS B CG  1 
ATOM   1637  C  CD  . LYS B  1 71  ? 14.413  226.701 25.195  1.00 59.12  ? 70  LYS B CD  1 
ATOM   1638  C  CE  . LYS B  1 71  ? 15.067  225.362 25.516  1.00 79.03  ? 70  LYS B CE  1 
ATOM   1639  N  NZ  . LYS B  1 71  ? 14.252  224.169 25.044  1.00 73.47  ? 70  LYS B NZ  1 
ATOM   1640  N  N   . HIS B  1 72  ? 14.566  231.638 22.813  1.00 31.18  ? 71  HIS B N   1 
ATOM   1641  C  CA  . HIS B  1 72  ? 13.754  232.575 22.102  1.00 29.49  ? 71  HIS B CA  1 
ATOM   1642  C  C   . HIS B  1 72  ? 12.242  232.436 22.409  1.00 28.79  ? 71  HIS B C   1 
ATOM   1643  O  O   . HIS B  1 72  ? 11.748  231.346 22.571  1.00 31.57  ? 71  HIS B O   1 
ATOM   1644  C  CB  . HIS B  1 72  ? 14.016  232.442 20.611  1.00 25.63  ? 71  HIS B CB  1 
ATOM   1645  C  CG  . HIS B  1 72  ? 13.216  233.416 19.797  1.00 28.71  ? 71  HIS B CG  1 
ATOM   1646  N  ND1 . HIS B  1 72  ? 13.548  234.740 19.658  1.00 28.40  ? 71  HIS B ND1 1 
ATOM   1647  C  CD2 . HIS B  1 72  ? 12.038  233.275 19.167  1.00 27.56  ? 71  HIS B CD2 1 
ATOM   1648  C  CE1 . HIS B  1 72  ? 12.627  235.358 18.961  1.00 27.12  ? 71  HIS B CE1 1 
ATOM   1649  N  NE2 . HIS B  1 72  ? 11.692  234.495 18.673  1.00 27.61  ? 71  HIS B NE2 1 
ATOM   1650  N  N   . GLY B  1 73  ? 11.532  233.557 22.463  1.00 26.74  ? 72  GLY B N   1 
ATOM   1651  C  CA  . GLY B  1 73  ? 10.112  233.599 22.719  1.00 26.45  ? 72  GLY B CA  1 
ATOM   1652  C  C   . GLY B  1 73  ? 9.499   234.842 22.130  1.00 29.22  ? 72  GLY B C   1 
ATOM   1653  O  O   . GLY B  1 73  ? 10.091  235.499 21.316  1.00 35.74  ? 72  GLY B O   1 
ATOM   1654  N  N   . GLY B  1 74  ? 8.279   235.141 22.497  1.00 29.88  ? 73  GLY B N   1 
ATOM   1655  C  CA  . GLY B  1 74  ? 7.636   236.341 22.104  1.00 28.98  ? 73  GLY B CA  1 
ATOM   1656  C  C   . GLY B  1 74  ? 7.707   237.289 23.319  1.00 30.26  ? 73  GLY B C   1 
ATOM   1657  O  O   . GLY B  1 74  ? 8.123   236.888 24.425  1.00 30.82  ? 73  GLY B O   1 
ATOM   1658  N  N   . PRO B  1 75  ? 7.334   238.560 23.115  1.00 29.73  ? 74  PRO B N   1 
ATOM   1659  C  CA  . PRO B  1 75  ? 7.457   239.498 24.182  1.00 30.42  ? 74  PRO B CA  1 
ATOM   1660  C  C   . PRO B  1 75  ? 6.529   239.211 25.340  1.00 32.57  ? 74  PRO B C   1 
ATOM   1661  O  O   . PRO B  1 75  ? 6.832   239.648 26.395  1.00 32.91  ? 74  PRO B O   1 
ATOM   1662  C  CB  . PRO B  1 75  ? 7.196   240.850 23.505  1.00 27.85  ? 74  PRO B CB  1 
ATOM   1663  C  CG  . PRO B  1 75  ? 6.389   240.512 22.308  1.00 25.54  ? 74  PRO B CG  1 
ATOM   1664  C  CD  . PRO B  1 75  ? 7.017   239.242 21.848  1.00 27.80  ? 74  PRO B CD  1 
ATOM   1665  N  N   . LYS B  1 76  ? 5.469   238.414 25.171  1.00 33.12  ? 75  LYS B N   1 
ATOM   1666  C  CA  . LYS B  1 76  ? 4.630   238.034 26.327  1.00 32.97  ? 75  LYS B CA  1 
ATOM   1667  C  C   . LYS B  1 76  ? 5.149   236.893 27.200  1.00 33.17  ? 75  LYS B C   1 
ATOM   1668  O  O   . LYS B  1 76  ? 4.723   236.721 28.322  1.00 34.22  ? 75  LYS B O   1 
ATOM   1669  C  CB  . LYS B  1 76  ? 3.187   237.802 25.888  1.00 35.33  ? 75  LYS B CB  1 
ATOM   1670  C  CG  . LYS B  1 76  ? 2.543   239.063 25.307  1.00 35.55  ? 75  LYS B CG  1 
ATOM   1671  C  CD  . LYS B  1 76  ? 1.527   238.717 24.234  1.00 39.44  ? 75  LYS B CD  1 
ATOM   1672  C  CE  . LYS B  1 76  ? 0.057   238.627 24.782  1.00 43.89  ? 75  LYS B CE  1 
ATOM   1673  N  NZ  . LYS B  1 76  ? -0.691  237.340 24.571  1.00 41.20  ? 75  LYS B NZ  1 
ATOM   1674  N  N   . ASP B  1 77  ? 6.106   236.145 26.704  1.00 32.28  ? 76  ASP B N   1 
ATOM   1675  C  CA  . ASP B  1 77  ? 6.653   235.048 27.405  1.00 34.88  ? 76  ASP B CA  1 
ATOM   1676  C  C   . ASP B  1 77  ? 7.575   235.346 28.586  1.00 37.32  ? 76  ASP B C   1 
ATOM   1677  O  O   . ASP B  1 77  ? 8.378   236.281 28.590  1.00 34.30  ? 76  ASP B O   1 
ATOM   1678  C  CB  . ASP B  1 77  ? 7.422   234.244 26.357  1.00 39.37  ? 76  ASP B CB  1 
ATOM   1679  C  CG  . ASP B  1 77  ? 6.483   233.550 25.372  1.00 43.32  ? 76  ASP B CG  1 
ATOM   1680  O  OD1 . ASP B  1 77  ? 5.408   233.078 25.814  1.00 45.81  ? 76  ASP B OD1 1 
ATOM   1681  O  OD2 . ASP B  1 77  ? 6.775   233.482 24.170  1.00 38.39  ? 76  ASP B OD2 1 
ATOM   1682  N  N   . GLU B  1 78  ? 7.542   234.474 29.569  1.00 45.49  ? 77  GLU B N   1 
ATOM   1683  C  CA  . GLU B  1 78  ? 8.609   234.521 30.585  1.00 47.13  ? 77  GLU B CA  1 
ATOM   1684  C  C   . GLU B  1 78  ? 9.920   233.940 30.016  1.00 40.91  ? 77  GLU B C   1 
ATOM   1685  O  O   . GLU B  1 78  ? 10.959  234.582 30.145  1.00 41.34  ? 77  GLU B O   1 
ATOM   1686  C  CB  . GLU B  1 78  ? 8.166   233.934 31.921  1.00 50.02  ? 77  GLU B CB  1 
ATOM   1687  C  CG  . GLU B  1 78  ? 9.325   233.557 32.837  1.00 63.37  ? 77  GLU B CG  1 
ATOM   1688  C  CD  . GLU B  1 78  ? 9.240   234.162 34.248  1.00 85.16  ? 77  GLU B CD  1 
ATOM   1689  O  OE1 . GLU B  1 78  ? 8.140   233.984 34.950  1.00 72.72  ? 77  GLU B OE1 1 
ATOM   1690  O  OE2 . GLU B  1 78  ? 10.305  234.803 34.638  1.00 71.07  ? 77  GLU B OE2 1 
ATOM   1691  N  N   . GLU B  1 79  ? 9.854   232.793 29.356  1.00 35.98  ? 78  GLU B N   1 
ATOM   1692  C  CA  . GLU B  1 79  ? 10.965  232.284 28.545  1.00 36.36  ? 78  GLU B CA  1 
ATOM   1693  C  C   . GLU B  1 79  ? 11.107  233.086 27.243  1.00 34.77  ? 78  GLU B C   1 
ATOM   1694  O  O   . GLU B  1 79  ? 10.411  232.834 26.260  1.00 38.70  ? 78  GLU B O   1 
ATOM   1695  C  CB  . GLU B  1 79  ? 10.752  230.789 28.220  1.00 33.62  ? 78  GLU B CB  1 
ATOM   1696  C  CG  . GLU B  1 79  ? 12.016  230.091 27.720  1.00 42.61  ? 78  GLU B CG  1 
ATOM   1697  C  CD  . GLU B  1 79  ? 13.179  230.068 28.748  1.00 44.14  ? 78  GLU B CD  1 
ATOM   1698  O  OE1 . GLU B  1 79  ? 12.970  230.448 29.949  1.00 52.52  ? 78  GLU B OE1 1 
ATOM   1699  O  OE2 . GLU B  1 79  ? 14.295  229.633 28.396  1.00 36.98  ? 78  GLU B OE2 1 
ATOM   1700  N  N   . ARG B  1 80  ? 12.035  234.034 27.251  1.00 35.77  ? 79  ARG B N   1 
ATOM   1701  C  CA  . ARG B  1 80  ? 12.381  234.929 26.106  1.00 29.83  ? 79  ARG B CA  1 
ATOM   1702  C  C   . ARG B  1 80  ? 13.780  235.505 26.228  1.00 30.71  ? 79  ARG B C   1 
ATOM   1703  O  O   . ARG B  1 80  ? 14.381  235.577 27.281  1.00 30.07  ? 79  ARG B O   1 
ATOM   1704  C  CB  . ARG B  1 80  ? 11.396  236.082 25.959  1.00 29.29  ? 79  ARG B CB  1 
ATOM   1705  C  CG  . ARG B  1 80  ? 11.285  237.017 27.171  1.00 27.34  ? 79  ARG B CG  1 
ATOM   1706  C  CD  . ARG B  1 80  ? 10.485  238.217 26.762  1.00 28.19  ? 79  ARG B CD  1 
ATOM   1707  N  NE  . ARG B  1 80  ? 11.320  239.301 26.243  1.00 25.63  ? 79  ARG B NE  1 
ATOM   1708  C  CZ  . ARG B  1 80  ? 10.875  240.537 26.112  1.00 25.47  ? 79  ARG B CZ  1 
ATOM   1709  N  NH1 . ARG B  1 80  ? 9.625   240.797 26.464  1.00 21.67  ? 79  ARG B NH1 1 
ATOM   1710  N  NH2 . ARG B  1 80  ? 11.675  241.522 25.659  1.00 25.57  ? 79  ARG B NH2 1 
ATOM   1711  N  N   . HIS B  1 81  ? 14.305  235.941 25.115  1.00 30.59  ? 80  HIS B N   1 
ATOM   1712  C  CA  . HIS B  1 81  ? 15.452  236.777 25.154  1.00 26.82  ? 80  HIS B CA  1 
ATOM   1713  C  C   . HIS B  1 81  ? 14.971  238.181 25.526  1.00 26.22  ? 80  HIS B C   1 
ATOM   1714  O  O   . HIS B  1 81  ? 13.810  238.570 25.200  1.00 23.79  ? 80  HIS B O   1 
ATOM   1715  C  CB  . HIS B  1 81  ? 16.104  236.798 23.754  1.00 28.81  ? 80  HIS B CB  1 
ATOM   1716  C  CG  . HIS B  1 81  ? 16.515  235.449 23.241  1.00 30.46  ? 80  HIS B CG  1 
ATOM   1717  N  ND1 . HIS B  1 81  ? 16.430  235.099 21.919  1.00 30.29  ? 80  HIS B ND1 1 
ATOM   1718  C  CD2 . HIS B  1 81  ? 17.086  234.402 23.860  1.00 29.94  ? 80  HIS B CD2 1 
ATOM   1719  C  CE1 . HIS B  1 81  ? 16.966  233.919 21.739  1.00 28.43  ? 80  HIS B CE1 1 
ATOM   1720  N  NE2 . HIS B  1 81  ? 17.377  233.483 22.902  1.00 31.79  ? 80  HIS B NE2 1 
ATOM   1721  N  N   . VAL B  1 82  ? 15.854  238.925 26.198  1.00 25.91  ? 81  VAL B N   1 
ATOM   1722  C  CA  . VAL B  1 82  ? 15.678  240.356 26.461  1.00 26.64  ? 81  VAL B CA  1 
ATOM   1723  C  C   . VAL B  1 82  ? 15.382  241.084 25.170  1.00 28.23  ? 81  VAL B C   1 
ATOM   1724  O  O   . VAL B  1 82  ? 14.496  241.896 25.143  1.00 29.55  ? 81  VAL B O   1 
ATOM   1725  C  CB  . VAL B  1 82  ? 16.819  240.997 27.317  1.00 27.61  ? 81  VAL B CB  1 
ATOM   1726  C  CG1 . VAL B  1 82  ? 16.695  242.515 27.414  1.00 25.78  ? 81  VAL B CG1 1 
ATOM   1727  C  CG2 . VAL B  1 82  ? 16.854  240.383 28.716  1.00 24.45  ? 81  VAL B CG2 1 
ATOM   1728  N  N   . GLY B  1 83  ? 16.030  240.746 24.068  1.00 29.65  ? 82  GLY B N   1 
ATOM   1729  C  CA  . GLY B  1 83  ? 15.762  241.452 22.825  1.00 29.38  ? 82  GLY B CA  1 
ATOM   1730  C  C   . GLY B  1 83  ? 14.579  241.024 21.952  1.00 31.16  ? 82  GLY B C   1 
ATOM   1731  O  O   . GLY B  1 83  ? 14.421  241.508 20.798  1.00 30.22  ? 82  GLY B O   1 
ATOM   1732  N  N   . ASP B  1 84  ? 13.762  240.138 22.485  1.00 29.55  ? 83  ASP B N   1 
ATOM   1733  C  CA  . ASP B  1 84  ? 12.549  239.622 21.842  1.00 28.55  ? 83  ASP B CA  1 
ATOM   1734  C  C   . ASP B  1 84  ? 11.424  240.588 21.852  1.00 27.58  ? 83  ASP B C   1 
ATOM   1735  O  O   . ASP B  1 84  ? 10.600  240.612 22.780  1.00 30.09  ? 83  ASP B O   1 
ATOM   1736  C  CB  . ASP B  1 84  ? 12.106  238.212 22.443  1.00 28.47  ? 83  ASP B CB  1 
ATOM   1737  C  CG  . ASP B  1 84  ? 13.123  237.103 22.116  1.00 27.52  ? 83  ASP B CG  1 
ATOM   1738  O  OD1 . ASP B  1 84  ? 13.967  237.322 21.238  1.00 25.85  ? 83  ASP B OD1 1 
ATOM   1739  O  OD2 . ASP B  1 84  ? 13.086  235.988 22.666  1.00 30.44  ? 83  ASP B OD2 1 
ATOM   1740  N  N   . LEU B  1 85  ? 11.272  241.324 20.765  1.00 28.40  ? 84  LEU B N   1 
ATOM   1741  C  CA  . LEU B  1 85  ? 10.124  242.215 20.691  1.00 24.80  ? 84  LEU B CA  1 
ATOM   1742  C  C   . LEU B  1 85  ? 9.070   241.689 19.703  1.00 26.31  ? 84  LEU B C   1 
ATOM   1743  O  O   . LEU B  1 85  ? 8.193   242.409 19.316  1.00 32.32  ? 84  LEU B O   1 
ATOM   1744  C  CB  . LEU B  1 85  ? 10.533  243.636 20.442  1.00 22.29  ? 84  LEU B CB  1 
ATOM   1745  C  CG  . LEU B  1 85  ? 11.585  244.234 21.383  1.00 25.47  ? 84  LEU B CG  1 
ATOM   1746  C  CD1 . LEU B  1 85  ? 12.092  245.587 20.955  1.00 25.14  ? 84  LEU B CD1 1 
ATOM   1747  C  CD2 . LEU B  1 85  ? 11.027  244.410 22.773  1.00 24.63  ? 84  LEU B CD2 1 
ATOM   1748  N  N   . GLY B  1 86  ? 9.132   240.440 19.311  1.00 23.46  ? 85  GLY B N   1 
ATOM   1749  C  CA  . GLY B  1 86  ? 8.029   239.854 18.565  1.00 26.13  ? 85  GLY B CA  1 
ATOM   1750  C  C   . GLY B  1 86  ? 7.969   240.329 17.154  1.00 28.21  ? 85  GLY B C   1 
ATOM   1751  O  O   . GLY B  1 86  ? 9.002   240.508 16.512  1.00 27.05  ? 85  GLY B O   1 
ATOM   1752  N  N   . ASN B  1 87  ? 6.769   240.607 16.670  1.00 29.22  ? 86  ASN B N   1 
ATOM   1753  C  CA  . ASN B  1 87  ? 6.682   241.035 15.275  1.00 28.58  ? 86  ASN B CA  1 
ATOM   1754  C  C   . ASN B  1 87  ? 6.281   242.511 15.124  1.00 28.97  ? 86  ASN B C   1 
ATOM   1755  O  O   . ASN B  1 87  ? 5.692   243.127 16.057  1.00 31.69  ? 86  ASN B O   1 
ATOM   1756  C  CB  . ASN B  1 87  ? 5.717   240.106 14.501  1.00 25.87  ? 86  ASN B CB  1 
ATOM   1757  C  CG  . ASN B  1 87  ? 6.311   238.749 14.257  1.00 30.54  ? 86  ASN B CG  1 
ATOM   1758  O  OD1 . ASN B  1 87  ? 7.294   238.602 13.501  1.00 28.98  ? 86  ASN B OD1 1 
ATOM   1759  N  ND2 . ASN B  1 87  ? 5.731   237.720 14.892  1.00 30.71  ? 86  ASN B ND2 1 
ATOM   1760  N  N   . VAL B  1 88  ? 6.522   243.048 13.940  1.00 25.69  ? 87  VAL B N   1 
ATOM   1761  C  CA  . VAL B  1 88  ? 5.868   244.260 13.520  1.00 24.83  ? 87  VAL B CA  1 
ATOM   1762  C  C   . VAL B  1 88  ? 5.198   243.943 12.200  1.00 26.48  ? 87  VAL B C   1 
ATOM   1763  O  O   . VAL B  1 88  ? 5.609   243.016 11.468  1.00 28.92  ? 87  VAL B O   1 
ATOM   1764  C  CB  . VAL B  1 88  ? 6.851   245.474 13.392  1.00 23.88  ? 87  VAL B CB  1 
ATOM   1765  C  CG1 . VAL B  1 88  ? 7.431   245.855 14.730  1.00 25.16  ? 87  VAL B CG1 1 
ATOM   1766  C  CG2 . VAL B  1 88  ? 8.000   245.173 12.435  1.00 22.64  ? 87  VAL B CG2 1 
ATOM   1767  N  N   . THR B  1 89  ? 4.209   244.742 11.856  1.00 27.25  ? 88  THR B N   1 
ATOM   1768  C  CA  . THR B  1 89  ? 3.303   244.410 10.774  1.00 29.79  ? 88  THR B CA  1 
ATOM   1769  C  C   . THR B  1 89  ? 3.366   245.462 9.729   1.00 29.74  ? 88  THR B C   1 
ATOM   1770  O  O   . THR B  1 89  ? 3.065   246.594 10.027  1.00 32.29  ? 88  THR B O   1 
ATOM   1771  C  CB  . THR B  1 89  ? 1.838   244.269 11.304  1.00 29.26  ? 88  THR B CB  1 
ATOM   1772  O  OG1 . THR B  1 89  ? 1.779   243.132 12.138  1.00 29.37  ? 88  THR B OG1 1 
ATOM   1773  C  CG2 . THR B  1 89  ? 0.770   244.080 10.160  1.00 25.44  ? 88  THR B CG2 1 
ATOM   1774  N  N   . ALA B  1 90  ? 3.756   245.113 8.510   1.00 30.68  ? 89  ALA B N   1 
ATOM   1775  C  CA  . ALA B  1 90  ? 3.744   246.097 7.415   1.00 31.42  ? 89  ALA B CA  1 
ATOM   1776  C  C   . ALA B  1 90  ? 2.457   246.021 6.638   1.00 29.04  ? 89  ALA B C   1 
ATOM   1777  O  O   . ALA B  1 90  ? 2.059   244.935 6.210   1.00 33.88  ? 89  ALA B O   1 
ATOM   1778  C  CB  . ALA B  1 90  ? 4.957   245.940 6.482   1.00 30.43  ? 89  ALA B CB  1 
ATOM   1779  N  N   . ASP B  1 91  ? 1.813   247.167 6.486   1.00 31.06  ? 90  ASP B N   1 
ATOM   1780  C  CA  . ASP B  1 91  ? 0.624   247.363 5.641   1.00 33.03  ? 90  ASP B CA  1 
ATOM   1781  C  C   . ASP B  1 91  ? 0.898   247.204 4.154   1.00 34.36  ? 90  ASP B C   1 
ATOM   1782  O  O   . ASP B  1 91  ? 2.050   246.995 3.747   1.00 39.60  ? 90  ASP B O   1 
ATOM   1783  C  CB  . ASP B  1 91  ? -0.021  248.706 5.918   1.00 33.07  ? 90  ASP B CB  1 
ATOM   1784  C  CG  . ASP B  1 91  ? 0.786   249.917 5.370   1.00 40.00  ? 90  ASP B CG  1 
ATOM   1785  O  OD1 . ASP B  1 91  ? 1.546   249.886 4.340   1.00 39.24  ? 90  ASP B OD1 1 
ATOM   1786  O  OD2 . ASP B  1 91  ? 0.601   250.978 5.998   1.00 40.26  ? 90  ASP B OD2 1 
ATOM   1787  N  N   . LYS B  1 92  ? -0.133  247.322 3.327   1.00 39.55  ? 91  LYS B N   1 
ATOM   1788  C  CA  . LYS B  1 92  ? 0.002   247.025 1.816   1.00 43.17  ? 91  LYS B CA  1 
ATOM   1789  C  C   . LYS B  1 92  ? 0.840   248.054 1.001   1.00 36.96  ? 91  LYS B C   1 
ATOM   1790  O  O   . LYS B  1 92  ? 1.187   247.799 -0.144  1.00 40.22  ? 91  LYS B O   1 
ATOM   1791  C  CB  . LYS B  1 92  ? -1.351  246.734 1.128   1.00 38.93  ? 91  LYS B CB  1 
ATOM   1792  C  CG  . LYS B  1 92  ? -2.347  247.832 1.467   1.00 51.35  ? 91  LYS B CG  1 
ATOM   1793  C  CD  . LYS B  1 92  ? -3.273  248.354 0.348   1.00 59.34  ? 91  LYS B CD  1 
ATOM   1794  C  CE  . LYS B  1 92  ? -4.299  249.359 0.950   1.00 59.16  ? 91  LYS B CE  1 
ATOM   1795  N  NZ  . LYS B  1 92  ? -4.743  250.446 -0.002  1.00 63.74  ? 91  LYS B NZ  1 
ATOM   1796  N  N   . ASP B  1 93  ? 1.144   249.173 1.636   1.00 35.25  ? 92  ASP B N   1 
ATOM   1797  C  CA  . ASP B  1 93  ? 2.169   250.104 1.224   1.00 41.56  ? 92  ASP B CA  1 
ATOM   1798  C  C   . ASP B  1 93  ? 3.575   249.898 1.761   1.00 41.42  ? 92  ASP B C   1 
ATOM   1799  O  O   . ASP B  1 93  ? 4.380   250.750 1.539   1.00 42.22  ? 92  ASP B O   1 
ATOM   1800  C  CB  . ASP B  1 93  ? 1.759   251.492 1.687   1.00 47.57  ? 92  ASP B CB  1 
ATOM   1801  C  CG  . ASP B  1 93  ? 0.490   251.923 1.033   1.00 55.39  ? 92  ASP B CG  1 
ATOM   1802  O  OD1 . ASP B  1 93  ? 0.441   251.721 -0.203  1.00 53.49  ? 92  ASP B OD1 1 
ATOM   1803  O  OD2 . ASP B  1 93  ? -0.454  252.404 1.704   1.00 55.70  ? 92  ASP B OD2 1 
ATOM   1804  N  N   . GLY B  1 94  ? 3.870   248.818 2.483   1.00 38.29  ? 93  GLY B N   1 
ATOM   1805  C  CA  . GLY B  1 94  ? 5.225   248.544 2.896   1.00 34.04  ? 93  GLY B CA  1 
ATOM   1806  C  C   . GLY B  1 94  ? 5.578   249.268 4.191   1.00 36.66  ? 93  GLY B C   1 
ATOM   1807  O  O   . GLY B  1 94  ? 6.745   249.329 4.556   1.00 39.63  ? 93  GLY B O   1 
ATOM   1808  N  N   . VAL B  1 95  ? 4.593   249.780 4.912   1.00 31.01  ? 94  VAL B N   1 
ATOM   1809  C  CA  . VAL B  1 95  ? 4.890   250.560 6.048   1.00 31.06  ? 94  VAL B CA  1 
ATOM   1810  C  C   . VAL B  1 95  ? 4.457   249.848 7.309   1.00 33.25  ? 94  VAL B C   1 
ATOM   1811  O  O   . VAL B  1 95  ? 3.285   249.404 7.431   1.00 31.62  ? 94  VAL B O   1 
ATOM   1812  C  CB  . VAL B  1 95  ? 4.238   251.940 6.006   1.00 33.24  ? 94  VAL B CB  1 
ATOM   1813  C  CG1 . VAL B  1 95  ? 4.489   252.678 7.327   1.00 29.44  ? 94  VAL B CG1 1 
ATOM   1814  C  CG2 . VAL B  1 95  ? 4.789   252.732 4.856   1.00 28.57  ? 94  VAL B CG2 1 
ATOM   1815  N  N   . ALA B  1 96  ? 5.419   249.735 8.239   1.00 30.41  ? 95  ALA B N   1 
ATOM   1816  C  CA  . ALA B  1 96  ? 5.137   249.282 9.580   1.00 29.20  ? 95  ALA B CA  1 
ATOM   1817  C  C   . ALA B  1 96  ? 5.182   250.480 10.468  1.00 30.62  ? 95  ALA B C   1 
ATOM   1818  O  O   . ALA B  1 96  ? 6.289   251.015 10.716  1.00 33.68  ? 95  ALA B O   1 
ATOM   1819  C  CB  . ALA B  1 96  ? 6.131   248.242 10.052  1.00 28.72  ? 95  ALA B CB  1 
ATOM   1820  N  N   . ASP B  1 97  ? 4.003   250.915 10.914  1.00 29.07  ? 96  ASP B N   1 
ATOM   1821  C  CA  . ASP B  1 97  ? 3.833   251.871 12.044  1.00 32.94  ? 96  ASP B CA  1 
ATOM   1822  C  C   . ASP B  1 97  ? 3.996   251.231 13.423  1.00 30.24  ? 96  ASP B C   1 
ATOM   1823  O  O   . ASP B  1 97  ? 3.032   250.904 14.068  1.00 36.89  ? 96  ASP B O   1 
ATOM   1824  C  CB  . ASP B  1 97  ? 2.461   252.610 11.932  1.00 31.02  ? 96  ASP B CB  1 
ATOM   1825  C  CG  . ASP B  1 97  ? 2.395   253.449 10.642  1.00 38.72  ? 96  ASP B CG  1 
ATOM   1826  O  OD1 . ASP B  1 97  ? 3.383   254.231 10.354  1.00 37.56  ? 96  ASP B OD1 1 
ATOM   1827  O  OD2 . ASP B  1 97  ? 1.406   253.299 9.848   1.00 40.59  ? 96  ASP B OD2 1 
ATOM   1828  N  N   . VAL B  1 98  ? 5.201   251.066 13.884  1.00 29.69  ? 97  VAL B N   1 
ATOM   1829  C  CA  . VAL B  1 98  ? 5.453   250.321 15.090  1.00 30.04  ? 97  VAL B CA  1 
ATOM   1830  C  C   . VAL B  1 98  ? 4.932   251.023 16.302  1.00 30.30  ? 97  VAL B C   1 
ATOM   1831  O  O   . VAL B  1 98  ? 5.107   252.208 16.417  1.00 33.96  ? 97  VAL B O   1 
ATOM   1832  C  CB  . VAL B  1 98  ? 6.974   250.146 15.207  1.00 27.62  ? 97  VAL B CB  1 
ATOM   1833  C  CG1 . VAL B  1 98  ? 7.346   249.383 16.471  1.00 21.65  ? 97  VAL B CG1 1 
ATOM   1834  C  CG2 . VAL B  1 98  ? 7.532   249.528 13.887  1.00 25.52  ? 97  VAL B CG2 1 
ATOM   1835  N  N   . SER B  1 99  ? 4.300   250.288 17.188  1.00 31.44  ? 98  SER B N   1 
ATOM   1836  C  CA  . SER B  1 99  ? 3.865   250.765 18.523  1.00 35.27  ? 98  SER B CA  1 
ATOM   1837  C  C   . SER B  1 99  ? 3.929   249.569 19.470  1.00 36.96  ? 98  SER B C   1 
ATOM   1838  O  O   . SER B  1 99  ? 3.067   248.733 19.374  1.00 39.32  ? 98  SER B O   1 
ATOM   1839  C  CB  . SER B  1 99  ? 2.384   251.124 18.514  1.00 35.60  ? 98  SER B CB  1 
ATOM   1840  O  OG  . SER B  1 99  ? 1.991   251.948 19.582  1.00 37.33  ? 98  SER B OG  1 
ATOM   1841  N  N   . ILE B  1 100 ? 4.893   249.523 20.397  1.00 35.36  ? 99  ILE B N   1 
ATOM   1842  C  CA  . ILE B  1 100 ? 5.112   248.388 21.277  1.00 32.92  ? 99  ILE B CA  1 
ATOM   1843  C  C   . ILE B  1 100 ? 5.408   248.960 22.643  1.00 36.46  ? 99  ILE B C   1 
ATOM   1844  O  O   . ILE B  1 100 ? 5.922   250.075 22.781  1.00 37.60  ? 99  ILE B O   1 
ATOM   1845  C  CB  . ILE B  1 100 ? 6.301   247.555 20.731  1.00 34.84  ? 99  ILE B CB  1 
ATOM   1846  C  CG1 . ILE B  1 100 ? 5.812   246.529 19.690  1.00 35.11  ? 99  ILE B CG1 1 
ATOM   1847  C  CG2 . ILE B  1 100 ? 7.153   246.881 21.780  1.00 29.18  ? 99  ILE B CG2 1 
ATOM   1848  C  CD1 . ILE B  1 100 ? 6.977   246.086 18.843  1.00 32.82  ? 99  ILE B CD1 1 
ATOM   1849  N  N   . GLU B  1 101 ? 5.064   248.195 23.668  1.00 37.04  ? 100 GLU B N   1 
ATOM   1850  C  CA  . GLU B  1 101 ? 5.416   248.517 25.018  1.00 34.83  ? 100 GLU B CA  1 
ATOM   1851  C  C   . GLU B  1 101 ? 6.000   247.272 25.641  1.00 31.27  ? 100 GLU B C   1 
ATOM   1852  O  O   . GLU B  1 101 ? 5.468   246.200 25.511  1.00 30.17  ? 100 GLU B O   1 
ATOM   1853  C  CB  . GLU B  1 101 ? 4.183   248.917 25.722  1.00 35.05  ? 100 GLU B CB  1 
ATOM   1854  C  CG  . GLU B  1 101 ? 4.460   250.008 26.653  1.00 46.99  ? 100 GLU B CG  1 
ATOM   1855  C  CD  . GLU B  1 101 ? 3.209   250.400 27.419  1.00 53.99  ? 100 GLU B CD  1 
ATOM   1856  O  OE1 . GLU B  1 101 ? 2.362   251.216 26.845  1.00 53.59  ? 100 GLU B OE1 1 
ATOM   1857  O  OE2 . GLU B  1 101 ? 3.110   249.893 28.571  1.00 47.21  ? 100 GLU B OE2 1 
ATOM   1858  N  N   . ASP B  1 102 ? 7.116   247.419 26.304  1.00 30.24  ? 101 ASP B N   1 
ATOM   1859  C  CA  . ASP B  1 102 ? 7.805   246.258 26.774  1.00 29.77  ? 101 ASP B CA  1 
ATOM   1860  C  C   . ASP B  1 102 ? 8.535   246.646 28.047  1.00 30.53  ? 101 ASP B C   1 
ATOM   1861  O  O   . ASP B  1 102 ? 9.166   247.718 28.110  1.00 30.46  ? 101 ASP B O   1 
ATOM   1862  C  CB  . ASP B  1 102 ? 8.808   245.757 25.715  1.00 30.20  ? 101 ASP B CB  1 
ATOM   1863  C  CG  . ASP B  1 102 ? 9.373   244.392 26.078  1.00 34.07  ? 101 ASP B CG  1 
ATOM   1864  O  OD1 . ASP B  1 102 ? 8.696   243.375 25.851  1.00 31.14  ? 101 ASP B OD1 1 
ATOM   1865  O  OD2 . ASP B  1 102 ? 10.495  244.328 26.648  1.00 35.99  ? 101 ASP B OD2 1 
ATOM   1866  N  N   A SER B  1 103 ? 8.451   245.782 29.060  0.50 30.33  ? 102 SER B N   1 
ATOM   1867  N  N   B SER B  1 103 ? 8.488   245.766 29.038  0.50 30.45  ? 102 SER B N   1 
ATOM   1868  C  CA  A SER B  1 103 ? 9.063   246.038 30.383  0.50 29.46  ? 102 SER B CA  1 
ATOM   1869  C  CA  B SER B  1 103 ? 9.053   246.046 30.361  0.50 29.73  ? 102 SER B CA  1 
ATOM   1870  C  C   A SER B  1 103 ? 10.232  245.164 30.682  0.50 30.52  ? 102 SER B C   1 
ATOM   1871  C  C   B SER B  1 103 ? 10.220  245.168 30.677  0.50 30.67  ? 102 SER B C   1 
ATOM   1872  O  O   A SER B  1 103 ? 10.668  245.151 31.835  0.50 31.89  ? 102 SER B O   1 
ATOM   1873  O  O   B SER B  1 103 ? 10.638  245.155 31.836  0.50 31.96  ? 102 SER B O   1 
ATOM   1874  C  CB  A SER B  1 103 ? 8.105   245.778 31.519  0.50 28.73  ? 102 SER B CB  1 
ATOM   1875  C  CB  B SER B  1 103 ? 8.044   245.729 31.416  0.50 29.36  ? 102 SER B CB  1 
ATOM   1876  O  OG  A SER B  1 103 ? 7.051   246.709 31.526  0.50 32.68  ? 102 SER B OG  1 
ATOM   1877  O  OG  B SER B  1 103 ? 7.590   244.411 31.174  0.50 33.14  ? 102 SER B OG  1 
ATOM   1878  N  N   . VAL B  1 104 ? 10.733  244.431 29.680  1.00 30.21  ? 103 VAL B N   1 
ATOM   1879  C  CA  . VAL B  1 104 ? 11.893  243.560 29.867  1.00 30.46  ? 103 VAL B CA  1 
ATOM   1880  C  C   . VAL B  1 104 ? 13.199  244.263 29.391  1.00 30.24  ? 103 VAL B C   1 
ATOM   1881  O  O   . VAL B  1 104 ? 14.229  244.235 30.096  1.00 35.24  ? 103 VAL B O   1 
ATOM   1882  C  CB  . VAL B  1 104 ? 11.694  242.147 29.244  1.00 27.99  ? 103 VAL B CB  1 
ATOM   1883  C  CG1 . VAL B  1 104 ? 12.971  241.343 29.279  1.00 27.57  ? 103 VAL B CG1 1 
ATOM   1884  C  CG2 . VAL B  1 104 ? 10.636  241.412 29.944  1.00 25.16  ? 103 VAL B CG2 1 
ATOM   1885  N  N   . ILE B  1 105 ? 13.150  244.859 28.211  1.00 32.31  ? 104 ILE B N   1 
ATOM   1886  C  CA  . ILE B  1 105 ? 14.198  245.760 27.712  1.00 30.79  ? 104 ILE B CA  1 
ATOM   1887  C  C   . ILE B  1 105 ? 14.219  247.047 28.568  1.00 32.39  ? 104 ILE B C   1 
ATOM   1888  O  O   . ILE B  1 105 ? 13.260  247.402 29.213  1.00 29.32  ? 104 ILE B O   1 
ATOM   1889  C  CB  . ILE B  1 105 ? 13.949  246.219 26.266  1.00 27.56  ? 104 ILE B CB  1 
ATOM   1890  C  CG1 . ILE B  1 105 ? 12.611  246.952 26.086  1.00 24.07  ? 104 ILE B CG1 1 
ATOM   1891  C  CG2 . ILE B  1 105 ? 14.234  245.125 25.281  1.00 23.90  ? 104 ILE B CG2 1 
ATOM   1892  C  CD1 . ILE B  1 105 ? 12.463  247.711 24.759  1.00 21.36  ? 104 ILE B CD1 1 
ATOM   1893  N  N   . SER B  1 106 ? 15.332  247.742 28.572  1.00 33.59  ? 105 SER B N   1 
ATOM   1894  C  CA  . SER B  1 106 ? 15.428  248.920 29.368  1.00 29.56  ? 105 SER B CA  1 
ATOM   1895  C  C   . SER B  1 106 ? 16.359  249.924 28.759  1.00 28.35  ? 105 SER B C   1 
ATOM   1896  O  O   . SER B  1 106 ? 17.291  249.568 28.018  1.00 28.77  ? 105 SER B O   1 
ATOM   1897  C  CB  . SER B  1 106 ? 15.985  248.534 30.737  1.00 29.97  ? 105 SER B CB  1 
ATOM   1898  O  OG  . SER B  1 106 ? 15.698  249.552 31.694  1.00 31.68  ? 105 SER B OG  1 
ATOM   1899  N  N   . LEU B  1 107 ? 16.192  251.182 29.145  1.00 28.14  ? 106 LEU B N   1 
ATOM   1900  C  CA  . LEU B  1 107 ? 17.272  252.126 28.818  1.00 29.57  ? 106 LEU B CA  1 
ATOM   1901  C  C   . LEU B  1 107 ? 18.394  252.347 29.868  1.00 33.35  ? 106 LEU B C   1 
ATOM   1902  O  O   . LEU B  1 107 ? 19.086  253.368 29.793  1.00 34.33  ? 106 LEU B O   1 
ATOM   1903  C  CB  . LEU B  1 107 ? 16.726  253.410 28.322  1.00 26.81  ? 106 LEU B CB  1 
ATOM   1904  C  CG  . LEU B  1 107 ? 15.654  253.305 27.243  1.00 26.90  ? 106 LEU B CG  1 
ATOM   1905  C  CD1 . LEU B  1 107 ? 15.181  254.695 26.877  1.00 27.66  ? 106 LEU B CD1 1 
ATOM   1906  C  CD2 . LEU B  1 107 ? 16.011  252.491 26.003  1.00 25.32  ? 106 LEU B CD2 1 
ATOM   1907  N  N   . SER B  1 108 ? 18.532  251.426 30.842  1.00 30.81  ? 107 SER B N   1 
ATOM   1908  C  CA  . SER B  1 108 ? 19.611  251.423 31.815  1.00 33.22  ? 107 SER B CA  1 
ATOM   1909  C  C   . SER B  1 108 ? 19.689  250.067 32.485  1.00 33.30  ? 107 SER B C   1 
ATOM   1910  O  O   . SER B  1 108 ? 18.785  249.278 32.366  1.00 34.33  ? 107 SER B O   1 
ATOM   1911  C  CB  . SER B  1 108 ? 19.437  252.538 32.886  1.00 34.35  ? 107 SER B CB  1 
ATOM   1912  O  OG  . SER B  1 108 ? 18.357  252.233 33.780  1.00 34.01  ? 107 SER B OG  1 
ATOM   1913  N  N   . GLY B  1 109 ? 20.773  249.812 33.190  1.00 32.96  ? 108 GLY B N   1 
ATOM   1914  C  CA  . GLY B  1 109 ? 20.901  248.602 33.954  1.00 33.35  ? 108 GLY B CA  1 
ATOM   1915  C  C   . GLY B  1 109 ? 21.351  247.485 33.014  1.00 36.75  ? 108 GLY B C   1 
ATOM   1916  O  O   . GLY B  1 109 ? 21.844  247.711 31.899  1.00 32.72  ? 108 GLY B O   1 
ATOM   1917  N  N   . ASP B  1 110 ? 21.168  246.270 33.496  1.00 37.51  ? 109 ASP B N   1 
ATOM   1918  C  CA  . ASP B  1 110 ? 21.596  245.050 32.814  1.00 39.86  ? 109 ASP B CA  1 
ATOM   1919  C  C   . ASP B  1 110 ? 20.884  244.850 31.494  1.00 37.72  ? 109 ASP B C   1 
ATOM   1920  O  O   . ASP B  1 110 ? 21.443  244.266 30.627  1.00 40.38  ? 109 ASP B O   1 
ATOM   1921  C  CB  . ASP B  1 110 ? 21.124  243.835 33.663  1.00 45.56  ? 109 ASP B CB  1 
ATOM   1922  C  CG  . ASP B  1 110 ? 21.873  243.669 34.973  1.00 49.22  ? 109 ASP B CG  1 
ATOM   1923  O  OD1 . ASP B  1 110 ? 22.942  244.301 35.112  1.00 51.40  ? 109 ASP B OD1 1 
ATOM   1924  O  OD2 . ASP B  1 110 ? 21.389  242.842 35.820  1.00 47.70  ? 109 ASP B OD2 1 
ATOM   1925  N  N   . HIS B  1 111 ? 19.612  245.219 31.421  1.00 32.18  ? 110 HIS B N   1 
ATOM   1926  C  CA  . HIS B  1 111 ? 18.823  244.905 30.307  1.00 35.30  ? 110 HIS B CA  1 
ATOM   1927  C  C   . HIS B  1 111 ? 18.875  246.087 29.372  1.00 34.34  ? 110 HIS B C   1 
ATOM   1928  O  O   . HIS B  1 111 ? 18.132  246.153 28.399  1.00 38.19  ? 110 HIS B O   1 
ATOM   1929  C  CB  . HIS B  1 111 ? 17.381  244.544 30.707  1.00 34.55  ? 110 HIS B CB  1 
ATOM   1930  C  CG  . HIS B  1 111 ? 17.274  243.247 31.458  1.00 41.77  ? 110 HIS B CG  1 
ATOM   1931  N  ND1 . HIS B  1 111 ? 16.057  242.646 31.749  1.00 44.41  ? 110 HIS B ND1 1 
ATOM   1932  C  CD2 . HIS B  1 111 ? 18.237  242.423 31.955  1.00 35.86  ? 110 HIS B CD2 1 
ATOM   1933  C  CE1 . HIS B  1 111 ? 16.289  241.533 32.421  1.00 43.54  ? 110 HIS B CE1 1 
ATOM   1934  N  NE2 . HIS B  1 111 ? 17.599  241.387 32.564  1.00 37.56  ? 110 HIS B NE2 1 
ATOM   1935  N  N   . CYS B  1 112 ? 19.768  247.007 29.642  1.00 30.72  ? 111 CYS B N   1 
ATOM   1936  C  CA  . CYS B  1 112 ? 19.927  248.122 28.796  1.00 31.69  ? 111 CYS B CA  1 
ATOM   1937  C  C   . CYS B  1 112 ? 20.279  247.862 27.289  1.00 29.66  ? 111 CYS B C   1 
ATOM   1938  O  O   . CYS B  1 112 ? 21.272  247.195 26.942  1.00 31.09  ? 111 CYS B O   1 
ATOM   1939  C  CB  . CYS B  1 112 ? 21.039  248.900 29.367  1.00 35.03  ? 111 CYS B CB  1 
ATOM   1940  S  SG  . CYS B  1 112 ? 20.968  250.505 28.587  1.00 39.90  ? 111 CYS B SG  1 
ATOM   1941  N  N   . ILE B  1 113 ? 19.494  248.462 26.428  1.00 27.73  ? 112 ILE B N   1 
ATOM   1942  C  CA  . ILE B  1 113 ? 19.587  248.243 24.991  1.00 31.02  ? 112 ILE B CA  1 
ATOM   1943  C  C   . ILE B  1 113 ? 20.275  249.377 24.234  1.00 27.07  ? 112 ILE B C   1 
ATOM   1944  O  O   . ILE B  1 113 ? 20.482  249.307 23.038  1.00 27.20  ? 112 ILE B O   1 
ATOM   1945  C  CB  . ILE B  1 113 ? 18.209  247.888 24.382  1.00 29.41  ? 112 ILE B CB  1 
ATOM   1946  C  CG1 . ILE B  1 113 ? 17.256  249.073 24.595  1.00 27.12  ? 112 ILE B CG1 1 
ATOM   1947  C  CG2 . ILE B  1 113 ? 17.757  246.530 24.965  1.00 25.02  ? 112 ILE B CG2 1 
ATOM   1948  C  CD1 . ILE B  1 113 ? 16.063  249.037 23.680  1.00 31.45  ? 112 ILE B CD1 1 
ATOM   1949  N  N   . ILE B  1 114 ? 20.697  250.375 24.978  1.00 27.50  ? 113 ILE B N   1 
ATOM   1950  C  CA  . ILE B  1 114 ? 21.493  251.459 24.440  1.00 30.31  ? 113 ILE B CA  1 
ATOM   1951  C  C   . ILE B  1 114 ? 22.857  250.990 23.986  1.00 28.04  ? 113 ILE B C   1 
ATOM   1952  O  O   . ILE B  1 114 ? 23.536  250.214 24.694  1.00 29.76  ? 113 ILE B O   1 
ATOM   1953  C  CB  . ILE B  1 114 ? 21.462  252.703 25.357  1.00 32.66  ? 113 ILE B CB  1 
ATOM   1954  C  CG1 . ILE B  1 114 ? 20.052  253.333 25.247  1.00 29.07  ? 113 ILE B CG1 1 
ATOM   1955  C  CG2 . ILE B  1 114 ? 22.514  253.758 24.945  1.00 28.52  ? 113 ILE B CG2 1 
ATOM   1956  C  CD1 . ILE B  1 114 ? 19.808  254.292 26.354  1.00 27.94  ? 113 ILE B CD1 1 
ATOM   1957  N  N   . GLY B  1 115 ? 23.200  251.379 22.765  1.00 26.73  ? 114 GLY B N   1 
ATOM   1958  C  CA  . GLY B  1 115 ? 24.446  250.862 22.119  1.00 26.03  ? 114 GLY B CA  1 
ATOM   1959  C  C   . GLY B  1 115 ? 24.414  249.386 21.625  1.00 27.57  ? 114 GLY B C   1 
ATOM   1960  O  O   . GLY B  1 115 ? 25.443  248.809 21.335  1.00 28.27  ? 114 GLY B O   1 
ATOM   1961  N  N   . ARG B  1 116 ? 23.219  248.794 21.511  1.00 28.52  ? 115 ARG B N   1 
ATOM   1962  C  CA  . ARG B  1 116 ? 22.992  247.524 20.852  1.00 28.29  ? 115 ARG B CA  1 
ATOM   1963  C  C   . ARG B  1 116 ? 22.244  247.769 19.555  1.00 27.76  ? 115 ARG B C   1 
ATOM   1964  O  O   . ARG B  1 116 ? 22.017  248.899 19.209  1.00 30.62  ? 115 ARG B O   1 
ATOM   1965  C  CB  . ARG B  1 116 ? 22.238  246.584 21.783  1.00 29.75  ? 115 ARG B CB  1 
ATOM   1966  C  CG  . ARG B  1 116 ? 22.849  246.561 23.177  1.00 31.61  ? 115 ARG B CG  1 
ATOM   1967  C  CD  . ARG B  1 116 ? 22.600  245.263 23.895  1.00 31.03  ? 115 ARG B CD  1 
ATOM   1968  N  NE  . ARG B  1 116 ? 23.185  245.243 25.236  1.00 35.74  ? 115 ARG B NE  1 
ATOM   1969  C  CZ  . ARG B  1 116 ? 24.310  244.601 25.616  1.00 32.07  ? 115 ARG B CZ  1 
ATOM   1970  N  NH1 . ARG B  1 116 ? 25.091  243.926 24.790  1.00 27.65  ? 115 ARG B NH1 1 
ATOM   1971  N  NH2 . ARG B  1 116 ? 24.678  244.709 26.862  1.00 31.21  ? 115 ARG B NH2 1 
ATOM   1972  N  N   . THR B  1 117 ? 21.889  246.714 18.833  1.00 29.54  ? 116 THR B N   1 
ATOM   1973  C  CA  . THR B  1 117 ? 21.366  246.834 17.488  1.00 29.91  ? 116 THR B CA  1 
ATOM   1974  C  C   . THR B  1 117 ? 19.927  246.412 17.330  1.00 29.45  ? 116 THR B C   1 
ATOM   1975  O  O   . THR B  1 117 ? 19.556  245.340 17.767  1.00 31.07  ? 116 THR B O   1 
ATOM   1976  C  CB  . THR B  1 117 ? 22.235  246.077 16.522  1.00 29.36  ? 116 THR B CB  1 
ATOM   1977  O  OG1 . THR B  1 117 ? 23.539  246.678 16.540  1.00 26.89  ? 116 THR B OG1 1 
ATOM   1978  C  CG2 . THR B  1 117 ? 21.634  246.152 15.082  1.00 26.63  ? 116 THR B CG2 1 
ATOM   1979  N  N   . LEU B  1 118 ? 19.102  247.294 16.786  1.00 28.89  ? 117 LEU B N   1 
ATOM   1980  C  CA  . LEU B  1 118 ? 17.733  246.948 16.535  1.00 27.96  ? 117 LEU B CA  1 
ATOM   1981  C  C   . LEU B  1 118 ? 17.768  246.383 15.119  1.00 27.85  ? 117 LEU B C   1 
ATOM   1982  O  O   . LEU B  1 118 ? 18.333  247.012 14.258  1.00 29.85  ? 117 LEU B O   1 
ATOM   1983  C  CB  . LEU B  1 118 ? 16.864  248.182 16.633  1.00 25.35  ? 117 LEU B CB  1 
ATOM   1984  C  CG  . LEU B  1 118 ? 15.374  247.970 16.402  1.00 27.00  ? 117 LEU B CG  1 
ATOM   1985  C  CD1 . LEU B  1 118 ? 14.688  247.120 17.458  1.00 26.48  ? 117 LEU B CD1 1 
ATOM   1986  C  CD2 . LEU B  1 118 ? 14.692  249.263 16.329  1.00 24.95  ? 117 LEU B CD2 1 
ATOM   1987  N  N   . VAL B  1 119 ? 17.201  245.213 14.876  1.00 26.99  ? 118 VAL B N   1 
ATOM   1988  C  CA  . VAL B  1 119 ? 17.086  244.642 13.534  1.00 24.19  ? 118 VAL B CA  1 
ATOM   1989  C  C   . VAL B  1 119 ? 15.648  244.321 13.131  1.00 26.92  ? 118 VAL B C   1 
ATOM   1990  O  O   . VAL B  1 119 ? 14.858  243.754 13.915  1.00 31.12  ? 118 VAL B O   1 
ATOM   1991  C  CB  . VAL B  1 119 ? 17.932  243.325 13.436  1.00 25.62  ? 118 VAL B CB  1 
ATOM   1992  C  CG1 . VAL B  1 119 ? 17.892  242.662 12.053  1.00 22.58  ? 118 VAL B CG1 1 
ATOM   1993  C  CG2 . VAL B  1 119 ? 19.382  243.486 13.951  1.00 21.73  ? 118 VAL B CG2 1 
ATOM   1994  N  N   . VAL B  1 120 ? 15.294  244.595 11.884  1.00 28.81  ? 119 VAL B N   1 
ATOM   1995  C  CA  . VAL B  1 120 ? 14.030  244.148 11.365  1.00 26.06  ? 119 VAL B CA  1 
ATOM   1996  C  C   . VAL B  1 120 ? 14.273  243.047 10.389  1.00 27.53  ? 119 VAL B C   1 
ATOM   1997  O  O   . VAL B  1 120 ? 15.108  243.171 9.537   1.00 30.86  ? 119 VAL B O   1 
ATOM   1998  C  CB  . VAL B  1 120 ? 13.153  245.279 10.820  1.00 28.05  ? 119 VAL B CB  1 
ATOM   1999  C  CG1 . VAL B  1 120 ? 13.841  246.163 9.744   1.00 26.81  ? 119 VAL B CG1 1 
ATOM   2000  C  CG2 . VAL B  1 120 ? 11.863  244.688 10.285  1.00 30.93  ? 119 VAL B CG2 1 
ATOM   2001  N  N   . HIS B  1 121 ? 13.561  241.933 10.537  1.00 32.21  ? 120 HIS B N   1 
ATOM   2002  C  CA  . HIS B  1 121 ? 13.867  240.727 9.772   1.00 29.81  ? 120 HIS B CA  1 
ATOM   2003  C  C   . HIS B  1 121 ? 12.979  240.489 8.587   1.00 30.63  ? 120 HIS B C   1 
ATOM   2004  O  O   . HIS B  1 121 ? 11.880  241.018 8.493   1.00 31.57  ? 120 HIS B O   1 
ATOM   2005  C  CB  . HIS B  1 121 ? 13.884  239.532 10.678  1.00 25.83  ? 120 HIS B CB  1 
ATOM   2006  C  CG  . HIS B  1 121 ? 15.024  239.543 11.641  1.00 27.98  ? 120 HIS B CG  1 
ATOM   2007  N  ND1 . HIS B  1 121 ? 16.183  238.818 11.434  1.00 26.56  ? 120 HIS B ND1 1 
ATOM   2008  C  CD2 . HIS B  1 121 ? 15.169  240.148 12.837  1.00 26.45  ? 120 HIS B CD2 1 
ATOM   2009  C  CE1 . HIS B  1 121 ? 16.971  238.937 12.470  1.00 24.43  ? 120 HIS B CE1 1 
ATOM   2010  N  NE2 . HIS B  1 121 ? 16.378  239.722 13.343  1.00 29.61  ? 120 HIS B NE2 1 
ATOM   2011  N  N   . GLU B  1 122 ? 13.479  239.685 7.670   1.00 31.73  ? 121 GLU B N   1 
ATOM   2012  C  CA  . GLU B  1 122 ? 12.752  239.228 6.471   1.00 30.65  ? 121 GLU B CA  1 
ATOM   2013  C  C   . GLU B  1 122 ? 11.319  238.653 6.648   1.00 31.16  ? 121 GLU B C   1 
ATOM   2014  O  O   . GLU B  1 122 ? 10.420  239.079 5.940   1.00 33.59  ? 121 GLU B O   1 
ATOM   2015  C  CB  . GLU B  1 122 ? 13.640  238.182 5.852   1.00 32.65  ? 121 GLU B CB  1 
ATOM   2016  C  CG  . GLU B  1 122 ? 13.389  237.815 4.422   1.00 38.12  ? 121 GLU B CG  1 
ATOM   2017  C  CD  . GLU B  1 122 ? 13.898  236.398 4.106   1.00 47.67  ? 121 GLU B CD  1 
ATOM   2018  O  OE1 . GLU B  1 122 ? 14.712  235.737 4.884   1.00 40.35  ? 121 GLU B OE1 1 
ATOM   2019  O  OE2 . GLU B  1 122 ? 13.414  235.937 3.046   1.00 50.11  ? 121 GLU B OE2 1 
ATOM   2020  N  N   . LYS B  1 123 ? 11.141  237.693 7.568   1.00 28.90  ? 122 LYS B N   1 
ATOM   2021  C  CA  . LYS B  1 123 ? 9.929   236.860 7.720   1.00 31.13  ? 122 LYS B CA  1 
ATOM   2022  C  C   . LYS B  1 123 ? 9.341   237.031 9.129   1.00 31.45  ? 122 LYS B C   1 
ATOM   2023  O  O   . LYS B  1 123 ? 9.955   237.652 10.012  1.00 31.70  ? 122 LYS B O   1 
ATOM   2024  C  CB  . LYS B  1 123 ? 10.241  235.316 7.545   1.00 28.43  ? 122 LYS B CB  1 
ATOM   2025  C  CG  . LYS B  1 123 ? 10.922  234.911 6.275   1.00 31.33  ? 122 LYS B CG  1 
ATOM   2026  C  CD  . LYS B  1 123 ? 11.171  233.421 5.979   1.00 33.82  ? 122 LYS B CD  1 
ATOM   2027  C  CE  . LYS B  1 123 ? 11.643  232.685 7.243   1.00 44.18  ? 122 LYS B CE  1 
ATOM   2028  N  NZ  . LYS B  1 123 ? 12.749  231.669 7.228   1.00 41.55  ? 122 LYS B NZ  1 
ATOM   2029  N  N   . ALA B  1 124 ? 8.198   236.421 9.371   1.00 27.55  ? 123 ALA B N   1 
ATOM   2030  C  CA  . ALA B  1 124 ? 7.668   236.470 10.692  1.00 30.30  ? 123 ALA B CA  1 
ATOM   2031  C  C   . ALA B  1 124 ? 8.527   235.700 11.671  1.00 28.79  ? 123 ALA B C   1 
ATOM   2032  O  O   . ALA B  1 124 ? 9.174   234.727 11.331  1.00 32.46  ? 123 ALA B O   1 
ATOM   2033  C  CB  . ALA B  1 124 ? 6.276   235.894 10.709  1.00 28.15  ? 123 ALA B CB  1 
ATOM   2034  N  N   . ASP B  1 125 ? 8.478   236.146 12.896  1.00 28.03  ? 124 ASP B N   1 
ATOM   2035  C  CA  . ASP B  1 125 ? 9.037   235.512 14.070  1.00 28.70  ? 124 ASP B CA  1 
ATOM   2036  C  C   . ASP B  1 125 ? 7.930   234.534 14.538  1.00 30.69  ? 124 ASP B C   1 
ATOM   2037  O  O   . ASP B  1 125 ? 6.738   234.927 14.703  1.00 29.63  ? 124 ASP B O   1 
ATOM   2038  C  CB  . ASP B  1 125 ? 9.278   236.609 15.145  1.00 26.08  ? 124 ASP B CB  1 
ATOM   2039  C  CG  . ASP B  1 125 ? 9.916   236.084 16.443  1.00 28.77  ? 124 ASP B CG  1 
ATOM   2040  O  OD1 . ASP B  1 125 ? 10.003  234.859 16.682  1.00 27.43  ? 124 ASP B OD1 1 
ATOM   2041  O  OD2 . ASP B  1 125 ? 10.328  236.942 17.269  1.00 29.79  ? 124 ASP B OD2 1 
ATOM   2042  N  N   . ASP B  1 126 ? 8.315   233.269 14.749  1.00 31.17  ? 125 ASP B N   1 
ATOM   2043  C  CA  . ASP B  1 126 ? 7.334   232.275 15.165  1.00 32.23  ? 125 ASP B CA  1 
ATOM   2044  C  C   . ASP B  1 126 ? 7.193   232.266 16.700  1.00 33.21  ? 125 ASP B C   1 
ATOM   2045  O  O   . ASP B  1 126 ? 6.516   231.375 17.257  1.00 32.70  ? 125 ASP B O   1 
ATOM   2046  C  CB  . ASP B  1 126 ? 7.567   230.894 14.548  1.00 28.45  ? 125 ASP B CB  1 
ATOM   2047  C  CG  . ASP B  1 126 ? 8.835   230.175 15.108  1.00 31.89  ? 125 ASP B CG  1 
ATOM   2048  O  OD1 . ASP B  1 126 ? 9.335   230.506 16.205  1.00 32.97  ? 125 ASP B OD1 1 
ATOM   2049  O  OD2 . ASP B  1 126 ? 9.348   229.260 14.449  1.00 30.73  ? 125 ASP B OD2 1 
ATOM   2050  N  N   . LEU B  1 127 ? 7.799   233.269 17.346  1.00 28.07  ? 126 LEU B N   1 
ATOM   2051  C  CA  . LEU B  1 127 ? 7.687   233.463 18.771  1.00 28.31  ? 126 LEU B CA  1 
ATOM   2052  C  C   . LEU B  1 127 ? 8.159   232.264 19.576  1.00 28.78  ? 126 LEU B C   1 
ATOM   2053  O  O   . LEU B  1 127 ? 7.725   232.050 20.739  1.00 31.49  ? 126 LEU B O   1 
ATOM   2054  C  CB  . LEU B  1 127 ? 6.278   233.955 19.182  1.00 27.88  ? 126 LEU B CB  1 
ATOM   2055  C  CG  . LEU B  1 127 ? 5.658   235.118 18.321  1.00 29.31  ? 126 LEU B CG  1 
ATOM   2056  C  CD1 . LEU B  1 127 ? 4.302   235.634 18.766  1.00 25.91  ? 126 LEU B CD1 1 
ATOM   2057  C  CD2 . LEU B  1 127 ? 6.551   236.310 18.152  1.00 27.30  ? 126 LEU B CD2 1 
ATOM   2058  N  N   . GLY B  1 128 ? 9.039   231.476 18.959  1.00 26.87  ? 127 GLY B N   1 
ATOM   2059  C  CA  . GLY B  1 128 ? 9.663   230.296 19.612  1.00 28.74  ? 127 GLY B CA  1 
ATOM   2060  C  C   . GLY B  1 128 ? 8.797   229.060 19.667  1.00 26.90  ? 127 GLY B C   1 
ATOM   2061  O  O   . GLY B  1 128 ? 9.031   228.166 20.416  1.00 29.76  ? 127 GLY B O   1 
ATOM   2062  N  N   . LYS B  1 129 ? 7.770   229.030 18.873  1.00 28.47  ? 128 LYS B N   1 
ATOM   2063  C  CA  . LYS B  1 129 ? 6.774   227.996 18.916  1.00 29.64  ? 128 LYS B CA  1 
ATOM   2064  C  C   . LYS B  1 129 ? 6.838   227.103 17.694  1.00 26.79  ? 128 LYS B C   1 
ATOM   2065  O  O   . LYS B  1 129 ? 5.912   226.395 17.407  1.00 30.01  ? 128 LYS B O   1 
ATOM   2066  C  CB  . LYS B  1 129 ? 5.386   228.664 19.006  1.00 30.64  ? 128 LYS B CB  1 
ATOM   2067  C  CG  . LYS B  1 129 ? 5.046   229.126 20.399  1.00 35.63  ? 128 LYS B CG  1 
ATOM   2068  C  CD  . LYS B  1 129 ? 4.009   230.206 20.453  1.00 38.44  ? 128 LYS B CD  1 
ATOM   2069  C  CE  . LYS B  1 129 ? 2.587   229.665 20.447  1.00 45.48  ? 128 LYS B CE  1 
ATOM   2070  N  NZ  . LYS B  1 129 ? 1.804   230.321 21.553  1.00 52.82  ? 128 LYS B NZ  1 
ATOM   2071  N  N   . GLY B  1 130 ? 7.891   227.221 16.916  1.00 28.46  ? 129 GLY B N   1 
ATOM   2072  C  CA  . GLY B  1 130 ? 8.056   226.458 15.705  1.00 28.82  ? 129 GLY B CA  1 
ATOM   2073  C  C   . GLY B  1 130 ? 8.457   224.979 15.811  1.00 32.46  ? 129 GLY B C   1 
ATOM   2074  O  O   . GLY B  1 130 ? 8.250   224.278 14.833  1.00 33.64  ? 129 GLY B O   1 
ATOM   2075  N  N   . GLY B  1 131 ? 9.010   224.478 16.934  1.00 26.48  ? 130 GLY B N   1 
ATOM   2076  C  CA  . GLY B  1 131 ? 9.365   223.074 16.977  1.00 25.84  ? 130 GLY B CA  1 
ATOM   2077  C  C   . GLY B  1 131 ? 10.655  222.598 16.302  1.00 28.17  ? 130 GLY B C   1 
ATOM   2078  O  O   . GLY B  1 131 ? 10.969  221.415 16.367  1.00 28.51  ? 130 GLY B O   1 
ATOM   2079  N  N   . ASN B  1 132 ? 11.453  223.506 15.744  1.00 28.64  ? 131 ASN B N   1 
ATOM   2080  C  CA  . ASN B  1 132 ? 12.814  223.198 15.345  1.00 30.63  ? 131 ASN B CA  1 
ATOM   2081  C  C   . ASN B  1 132 ? 13.857  223.990 16.156  1.00 34.73  ? 131 ASN B C   1 
ATOM   2082  O  O   . ASN B  1 132 ? 13.489  224.907 16.903  1.00 35.02  ? 131 ASN B O   1 
ATOM   2083  C  CB  . ASN B  1 132 ? 12.950  223.478 13.846  1.00 33.75  ? 131 ASN B CB  1 
ATOM   2084  C  CG  . ASN B  1 132 ? 12.734  224.955 13.490  1.00 34.86  ? 131 ASN B CG  1 
ATOM   2085  O  OD1 . ASN B  1 132 ? 12.457  225.781 14.360  1.00 33.93  ? 131 ASN B OD1 1 
ATOM   2086  N  ND2 . ASN B  1 132 ? 12.871  225.284 12.216  1.00 35.64  ? 131 ASN B ND2 1 
ATOM   2087  N  N   A GLU B  1 133 ? 15.131  223.632 15.944  0.50 33.71  ? 132 GLU B N   1 
ATOM   2088  N  N   B GLU B  1 133 ? 15.146  223.682 16.011  0.50 36.03  ? 132 GLU B N   1 
ATOM   2089  C  CA  A GLU B  1 133 ? 16.288  224.190 16.657  0.50 33.20  ? 132 GLU B CA  1 
ATOM   2090  C  CA  B GLU B  1 133 ? 16.161  224.342 16.851  0.50 36.68  ? 132 GLU B CA  1 
ATOM   2091  C  C   A GLU B  1 133 ? 16.264  225.720 16.491  0.50 34.75  ? 132 GLU B C   1 
ATOM   2092  C  C   B GLU B  1 133 ? 16.200  225.825 16.532  0.50 36.66  ? 132 GLU B C   1 
ATOM   2093  O  O   A GLU B  1 133 ? 16.400  226.486 17.443  0.50 36.64  ? 132 GLU B O   1 
ATOM   2094  O  O   B GLU B  1 133 ? 16.367  226.673 17.411  0.50 37.16  ? 132 GLU B O   1 
ATOM   2095  C  CB  A GLU B  1 133 ? 17.637  223.531 16.158  0.50 28.97  ? 132 GLU B CB  1 
ATOM   2096  C  CB  B GLU B  1 133 ? 17.568  223.703 16.701  0.50 37.67  ? 132 GLU B CB  1 
ATOM   2097  C  CG  A GLU B  1 133 ? 17.604  222.011 15.876  0.50 27.08  ? 132 GLU B CG  1 
ATOM   2098  C  CG  B GLU B  1 133 ? 18.350  223.697 18.023  0.50 40.82  ? 132 GLU B CG  1 
ATOM   2099  C  CD  A GLU B  1 133 ? 18.990  221.336 15.661  0.50 28.86  ? 132 GLU B CD  1 
ATOM   2100  C  CD  B GLU B  1 133 ? 19.879  223.627 17.848  0.50 44.55  ? 132 GLU B CD  1 
ATOM   2101  O  OE1 A GLU B  1 133 ? 19.254  220.792 14.576  0.50 26.25  ? 132 GLU B OE1 1 
ATOM   2102  O  OE1 B GLU B  1 133 ? 20.389  223.414 16.709  0.50 40.92  ? 132 GLU B OE1 1 
ATOM   2103  O  OE2 A GLU B  1 133 ? 19.853  221.322 16.566  0.50 29.99  ? 132 GLU B OE2 1 
ATOM   2104  O  OE2 B GLU B  1 133 ? 20.586  223.795 18.867  0.50 39.99  ? 132 GLU B OE2 1 
ATOM   2105  N  N   . GLU B  1 134 ? 16.030  226.133 15.256  1.00 36.52  ? 133 GLU B N   1 
ATOM   2106  C  CA  . GLU B  1 134 ? 16.045  227.486 14.829  1.00 36.89  ? 133 GLU B CA  1 
ATOM   2107  C  C   . GLU B  1 134 ? 14.981  228.353 15.500  1.00 38.00  ? 133 GLU B C   1 
ATOM   2108  O  O   . GLU B  1 134 ? 15.274  229.477 15.782  1.00 42.20  ? 133 GLU B O   1 
ATOM   2109  C  CB  . GLU B  1 134 ? 15.807  227.517 13.320  1.00 38.58  ? 133 GLU B CB  1 
ATOM   2110  C  CG  . GLU B  1 134 ? 16.182  228.826 12.633  1.00 39.68  ? 133 GLU B CG  1 
ATOM   2111  C  CD  . GLU B  1 134 ? 17.648  229.238 12.931  1.00 46.49  ? 133 GLU B CD  1 
ATOM   2112  O  OE1 . GLU B  1 134 ? 18.574  228.367 12.875  1.00 44.13  ? 133 GLU B OE1 1 
ATOM   2113  O  OE2 . GLU B  1 134 ? 17.865  230.425 13.263  1.00 46.35  ? 133 GLU B OE2 1 
ATOM   2114  N  N   . SER B  1 135 ? 13.762  227.852 15.695  1.00 34.51  ? 134 SER B N   1 
ATOM   2115  C  CA  . SER B  1 135 ? 12.747  228.514 16.442  1.00 32.16  ? 134 SER B CA  1 
ATOM   2116  C  C   . SER B  1 135 ? 13.260  229.019 17.820  1.00 34.60  ? 134 SER B C   1 
ATOM   2117  O  O   . SER B  1 135 ? 12.950  230.160 18.231  1.00 32.51  ? 134 SER B O   1 
ATOM   2118  C  CB  . SER B  1 135 ? 11.591  227.572 16.682  1.00 29.85  ? 134 SER B CB  1 
ATOM   2119  O  OG  . SER B  1 135 ? 10.508  228.304 17.128  1.00 26.80  ? 134 SER B OG  1 
ATOM   2120  N  N   . THR B  1 136 ? 14.036  228.197 18.520  1.00 31.66  ? 135 THR B N   1 
ATOM   2121  C  CA  . THR B  1 136 ? 14.420  228.518 19.891  1.00 33.86  ? 135 THR B CA  1 
ATOM   2122  C  C   . THR B  1 136 ? 15.601  229.478 19.890  1.00 35.84  ? 135 THR B C   1 
ATOM   2123  O  O   . THR B  1 136 ? 16.038  229.913 20.950  1.00 36.13  ? 135 THR B O   1 
ATOM   2124  C  CB  . THR B  1 136 ? 14.840  227.275 20.713  1.00 38.50  ? 135 THR B CB  1 
ATOM   2125  O  OG1 . THR B  1 136 ? 15.984  226.615 20.095  1.00 36.02  ? 135 THR B OG1 1 
ATOM   2126  C  CG2 . THR B  1 136 ? 13.725  226.337 20.826  1.00 34.24  ? 135 THR B CG2 1 
ATOM   2127  N  N   . LYS B  1 137 ? 16.136  229.759 18.699  1.00 36.22  ? 136 LYS B N   1 
ATOM   2128  C  CA  . LYS B  1 137 ? 17.260  230.674 18.550  1.00 35.60  ? 136 LYS B CA  1 
ATOM   2129  C  C   . LYS B  1 137 ? 16.847  232.060 18.023  1.00 35.78  ? 136 LYS B C   1 
ATOM   2130  O  O   . LYS B  1 137 ? 17.137  233.086 18.647  1.00 35.66  ? 136 LYS B O   1 
ATOM   2131  C  CB  . LYS B  1 137 ? 18.291  230.053 17.662  1.00 33.83  ? 136 LYS B CB  1 
ATOM   2132  C  CG  . LYS B  1 137 ? 19.026  228.932 18.358  1.00 41.76  ? 136 LYS B CG  1 
ATOM   2133  C  CD  . LYS B  1 137 ? 20.242  228.611 17.498  1.00 47.08  ? 136 LYS B CD  1 
ATOM   2134  C  CE  . LYS B  1 137 ? 20.490  227.104 17.333  1.00 52.29  ? 136 LYS B CE  1 
ATOM   2135  N  NZ  . LYS B  1 137 ? 20.935  226.873 15.889  1.00 53.74  ? 136 LYS B NZ  1 
ATOM   2136  N  N   . THR B  1 138 ? 16.100  232.084 16.929  1.00 32.33  ? 137 THR B N   1 
ATOM   2137  C  CA  . THR B  1 138 ? 15.837  233.296 16.181  1.00 30.77  ? 137 THR B CA  1 
ATOM   2138  C  C   . THR B  1 138 ? 14.391  233.358 15.793  1.00 30.33  ? 137 THR B C   1 
ATOM   2139  O  O   . THR B  1 138 ? 14.044  234.207 15.007  1.00 28.86  ? 137 THR B O   1 
ATOM   2140  C  CB  . THR B  1 138 ? 16.609  233.320 14.804  1.00 31.38  ? 137 THR B CB  1 
ATOM   2141  O  OG1 . THR B  1 138 ? 16.059  232.323 13.905  1.00 36.84  ? 137 THR B OG1 1 
ATOM   2142  C  CG2 . THR B  1 138 ? 18.086  233.085 14.919  1.00 24.45  ? 137 THR B CG2 1 
ATOM   2143  N  N   . GLY B  1 139 ? 13.561  232.398 16.256  1.00 31.53  ? 138 GLY B N   1 
ATOM   2144  C  CA  . GLY B  1 139 ? 12.181  232.227 15.784  1.00 26.33  ? 138 GLY B CA  1 
ATOM   2145  C  C   . GLY B  1 139 ? 11.904  232.150 14.289  1.00 27.80  ? 138 GLY B C   1 
ATOM   2146  O  O   . GLY B  1 139 ? 10.821  232.530 13.841  1.00 28.56  ? 138 GLY B O   1 
ATOM   2147  N  N   . ASN B  1 140 ? 12.866  231.632 13.535  1.00 28.31  ? 139 ASN B N   1 
ATOM   2148  C  CA  . ASN B  1 140 ? 12.790  231.465 12.096  1.00 29.01  ? 139 ASN B CA  1 
ATOM   2149  C  C   . ASN B  1 140 ? 12.491  232.771 11.329  1.00 30.16  ? 139 ASN B C   1 
ATOM   2150  O  O   . ASN B  1 140 ? 11.799  232.746 10.290  1.00 29.49  ? 139 ASN B O   1 
ATOM   2151  C  CB  . ASN B  1 140 ? 11.748  230.390 11.755  1.00 29.97  ? 139 ASN B CB  1 
ATOM   2152  C  CG  . ASN B  1 140 ? 12.216  229.011 12.098  1.00 33.00  ? 139 ASN B CG  1 
ATOM   2153  O  OD1 . ASN B  1 140 ? 13.163  228.550 11.535  1.00 41.94  ? 139 ASN B OD1 1 
ATOM   2154  N  ND2 . ASN B  1 140 ? 11.591  228.369 13.048  1.00 36.76  ? 139 ASN B ND2 1 
ATOM   2155  N  N   . ALA B  1 141 ? 12.995  233.901 11.807  1.00 27.23  ? 140 ALA B N   1 
ATOM   2156  C  CA  . ALA B  1 141 ? 12.649  235.166 11.158  1.00 29.20  ? 140 ALA B CA  1 
ATOM   2157  C  C   . ALA B  1 141 ? 13.518  235.605 9.946   1.00 26.62  ? 140 ALA B C   1 
ATOM   2158  O  O   . ALA B  1 141 ? 13.234  236.625 9.303   1.00 23.90  ? 140 ALA B O   1 
ATOM   2159  C  CB  . ALA B  1 141 ? 12.455  236.292 12.183  1.00 30.97  ? 140 ALA B CB  1 
ATOM   2160  N  N   . GLY B  1 142 ? 14.517  234.782 9.651   1.00 26.92  ? 141 GLY B N   1 
ATOM   2161  C  CA  . GLY B  1 142 ? 15.314  234.907 8.442   1.00 30.69  ? 141 GLY B CA  1 
ATOM   2162  C  C   . GLY B  1 142 ? 16.253  236.072 8.412   1.00 29.24  ? 141 GLY B C   1 
ATOM   2163  O  O   . GLY B  1 142 ? 16.775  236.517 9.437   1.00 32.45  ? 141 GLY B O   1 
ATOM   2164  N  N   . SER B  1 143 ? 16.453  236.577 7.232   1.00 30.97  ? 142 SER B N   1 
ATOM   2165  C  CA  . SER B  1 143 ? 17.401  237.697 6.993   1.00 35.38  ? 142 SER B CA  1 
ATOM   2166  C  C   . SER B  1 143 ? 17.212  238.964 7.799   1.00 32.90  ? 142 SER B C   1 
ATOM   2167  O  O   . SER B  1 143 ? 16.088  239.383 8.120   1.00 32.73  ? 142 SER B O   1 
ATOM   2168  C  CB  . SER B  1 143 ? 17.252  238.127 5.550   1.00 32.12  ? 142 SER B CB  1 
ATOM   2169  O  OG  . SER B  1 143 ? 17.978  237.132 5.100   1.00 39.43  ? 142 SER B OG  1 
ATOM   2170  N  N   . ARG B  1 144 ? 18.340  239.607 8.008   1.00 34.03  ? 143 ARG B N   1 
ATOM   2171  C  CA  . ARG B  1 144 ? 18.386  240.936 8.544   1.00 33.40  ? 143 ARG B CA  1 
ATOM   2172  C  C   . ARG B  1 144 ? 18.197  241.966 7.423   1.00 30.56  ? 143 ARG B C   1 
ATOM   2173  O  O   . ARG B  1 144 ? 19.048  242.111 6.632   1.00 34.97  ? 143 ARG B O   1 
ATOM   2174  C  CB  . ARG B  1 144 ? 19.712  241.057 9.276   1.00 33.12  ? 143 ARG B CB  1 
ATOM   2175  C  CG  . ARG B  1 144 ? 19.947  239.941 10.281  1.00 29.16  ? 143 ARG B CG  1 
ATOM   2176  C  CD  . ARG B  1 144 ? 21.241  240.117 11.038  1.00 27.14  ? 143 ARG B CD  1 
ATOM   2177  N  NE  . ARG B  1 144 ? 21.328  238.943 11.875  1.00 29.21  ? 143 ARG B NE  1 
ATOM   2178  C  CZ  . ARG B  1 144 ? 22.099  238.807 12.938  1.00 28.98  ? 143 ARG B CZ  1 
ATOM   2179  N  NH1 . ARG B  1 144 ? 22.913  239.793 13.357  1.00 30.26  ? 143 ARG B NH1 1 
ATOM   2180  N  NH2 . ARG B  1 144 ? 22.058  237.670 13.599  1.00 26.03  ? 143 ARG B NH2 1 
ATOM   2181  N  N   . LEU B  1 145 ? 17.072  242.642 7.343   1.00 32.05  ? 144 LEU B N   1 
ATOM   2182  C  CA  . LEU B  1 145 ? 16.807  243.611 6.272   1.00 33.37  ? 144 LEU B CA  1 
ATOM   2183  C  C   . LEU B  1 145 ? 17.392  245.000 6.471   1.00 33.94  ? 144 LEU B C   1 
ATOM   2184  O  O   . LEU B  1 145 ? 17.851  245.572 5.506   1.00 33.91  ? 144 LEU B O   1 
ATOM   2185  C  CB  . LEU B  1 145 ? 15.289  243.743 6.018   1.00 33.35  ? 144 LEU B CB  1 
ATOM   2186  C  CG  . LEU B  1 145 ? 14.622  242.413 5.604   1.00 35.49  ? 144 LEU B CG  1 
ATOM   2187  C  CD1 . LEU B  1 145 ? 13.241  242.720 5.126   1.00 33.47  ? 144 LEU B CD1 1 
ATOM   2188  C  CD2 . LEU B  1 145 ? 15.328  241.595 4.515   1.00 31.96  ? 144 LEU B CD2 1 
ATOM   2189  N  N   . ALA B  1 146 ? 17.328  245.533 7.705   1.00 31.14  ? 145 ALA B N   1 
ATOM   2190  C  CA  . ALA B  1 146 ? 17.816  246.844 8.099   1.00 26.88  ? 145 ALA B CA  1 
ATOM   2191  C  C   . ALA B  1 146 ? 18.119  246.750 9.575   1.00 30.36  ? 145 ALA B C   1 
ATOM   2192  O  O   . ALA B  1 146 ? 17.443  246.025 10.306  1.00 35.27  ? 145 ALA B O   1 
ATOM   2193  C  CB  . ALA B  1 146 ? 16.780  247.955 7.835   1.00 23.74  ? 145 ALA B CB  1 
ATOM   2194  N  N   . CYS B  1 147 ? 19.109  247.495 10.023  1.00 31.07  ? 146 CYS B N   1 
ATOM   2195  C  CA  . CYS B  1 147 ? 19.479  247.579 11.405  1.00 31.07  ? 146 CYS B CA  1 
ATOM   2196  C  C   . CYS B  1 147 ? 20.048  248.955 11.709  1.00 32.88  ? 146 CYS B C   1 
ATOM   2197  O  O   . CYS B  1 147 ? 20.293  249.730 10.805  1.00 31.39  ? 146 CYS B O   1 
ATOM   2198  C  CB  . CYS B  1 147 ? 20.500  246.517 11.752  1.00 31.05  ? 146 CYS B CB  1 
ATOM   2199  S  SG  . CYS B  1 147 ? 21.953  246.593 10.694  1.00 36.24  ? 146 CYS B SG  1 
ATOM   2200  N  N   . GLY B  1 148 ? 20.205  249.245 12.998  1.00 30.66  ? 147 GLY B N   1 
ATOM   2201  C  CA  . GLY B  1 148 ? 20.875  250.391 13.431  1.00 27.64  ? 147 GLY B CA  1 
ATOM   2202  C  C   . GLY B  1 148 ? 21.307  250.190 14.862  1.00 32.34  ? 147 GLY B C   1 
ATOM   2203  O  O   . GLY B  1 148 ? 20.729  249.362 15.603  1.00 32.03  ? 147 GLY B O   1 
ATOM   2204  N  N   . VAL B  1 149 ? 22.320  250.966 15.246  1.00 27.87  ? 148 VAL B N   1 
ATOM   2205  C  CA  . VAL B  1 149 ? 22.695  251.088 16.605  1.00 28.42  ? 148 VAL B CA  1 
ATOM   2206  C  C   . VAL B  1 149 ? 21.718  251.963 17.458  1.00 28.78  ? 148 VAL B C   1 
ATOM   2207  O  O   . VAL B  1 149 ? 21.419  253.089 17.089  1.00 25.15  ? 148 VAL B O   1 
ATOM   2208  C  CB  . VAL B  1 149 ? 24.164  251.525 16.742  1.00 27.19  ? 148 VAL B CB  1 
ATOM   2209  C  CG1 . VAL B  1 149 ? 24.547  251.484 18.197  1.00 23.57  ? 148 VAL B CG1 1 
ATOM   2210  C  CG2 . VAL B  1 149 ? 25.076  250.582 15.995  1.00 22.47  ? 148 VAL B CG2 1 
ATOM   2211  N  N   . ILE B  1 150 ? 21.253  251.444 18.597  1.00 27.27  ? 149 ILE B N   1 
ATOM   2212  C  CA  . ILE B  1 150 ? 20.333  252.212 19.447  1.00 29.65  ? 149 ILE B CA  1 
ATOM   2213  C  C   . ILE B  1 150 ? 21.084  253.316 20.211  1.00 29.69  ? 149 ILE B C   1 
ATOM   2214  O  O   . ILE B  1 150 ? 21.995  253.044 20.992  1.00 33.00  ? 149 ILE B O   1 
ATOM   2215  C  CB  . ILE B  1 150 ? 19.471  251.288 20.402  1.00 29.88  ? 149 ILE B CB  1 
ATOM   2216  C  CG1 . ILE B  1 150 ? 18.788  250.131 19.637  1.00 26.21  ? 149 ILE B CG1 1 
ATOM   2217  C  CG2 . ILE B  1 150 ? 18.566  252.107 21.337  1.00 25.63  ? 149 ILE B CG2 1 
ATOM   2218  C  CD1 . ILE B  1 150 ? 18.303  248.968 20.523  1.00 27.05  ? 149 ILE B CD1 1 
ATOM   2219  N  N   . GLY B  1 151 ? 20.683  254.553 19.988  1.00 30.47  ? 150 GLY B N   1 
ATOM   2220  C  CA  . GLY B  1 151 ? 21.436  255.747 20.451  1.00 28.66  ? 150 GLY B CA  1 
ATOM   2221  C  C   . GLY B  1 151 ? 20.720  256.566 21.487  1.00 27.21  ? 150 GLY B C   1 
ATOM   2222  O  O   . GLY B  1 151 ? 19.496  256.572 21.513  1.00 31.05  ? 150 GLY B O   1 
ATOM   2223  N  N   . ILE B  1 152 ? 21.455  257.226 22.382  1.00 29.38  ? 151 ILE B N   1 
ATOM   2224  C  CA  . ILE B  1 152 ? 20.862  258.154 23.390  1.00 31.02  ? 151 ILE B CA  1 
ATOM   2225  C  C   . ILE B  1 152 ? 20.220  259.316 22.679  1.00 29.56  ? 151 ILE B C   1 
ATOM   2226  O  O   . ILE B  1 152 ? 20.775  259.868 21.748  1.00 30.57  ? 151 ILE B O   1 
ATOM   2227  C  CB  . ILE B  1 152 ? 21.851  258.635 24.500  1.00 35.54  ? 151 ILE B CB  1 
ATOM   2228  C  CG1 . ILE B  1 152 ? 22.177  257.468 25.400  1.00 39.99  ? 151 ILE B CG1 1 
ATOM   2229  C  CG2 . ILE B  1 152 ? 21.225  259.664 25.441  1.00 31.15  ? 151 ILE B CG2 1 
ATOM   2230  C  CD1 . ILE B  1 152 ? 23.457  257.607 26.171  1.00 42.70  ? 151 ILE B CD1 1 
ATOM   2231  N  N   . ALA B  1 153 ? 19.017  259.669 23.082  1.00 31.09  ? 152 ALA B N   1 
ATOM   2232  C  CA  . ALA B  1 153 ? 18.301  260.760 22.371  1.00 33.05  ? 152 ALA B CA  1 
ATOM   2233  C  C   . ALA B  1 153 ? 17.859  261.867 23.284  1.00 34.64  ? 152 ALA B C   1 
ATOM   2234  O  O   . ALA B  1 153 ? 17.665  261.670 24.479  1.00 35.90  ? 152 ALA B O   1 
ATOM   2235  C  CB  . ALA B  1 153 ? 17.112  260.216 21.623  1.00 32.61  ? 152 ALA B CB  1 
ATOM   2236  N  N   . GLN B  1 154 ? 17.694  263.025 22.698  1.00 39.51  ? 153 GLN B N   1 
ATOM   2237  C  CA  . GLN B  1 154 ? 17.309  264.204 23.454  1.00 49.29  ? 153 GLN B CA  1 
ATOM   2238  C  C   . GLN B  1 154 ? 15.830  264.272 23.906  1.00 56.46  ? 153 GLN B C   1 
ATOM   2239  O  O   . GLN B  1 154 ? 14.821  264.295 23.110  1.00 60.58  ? 153 GLN B O   1 
ATOM   2240  C  CB  . GLN B  1 154 ? 17.599  265.451 22.642  1.00 43.06  ? 153 GLN B CB  1 
ATOM   2241  C  CG  . GLN B  1 154 ? 16.962  266.598 23.351  1.00 45.83  ? 153 GLN B CG  1 
ATOM   2242  C  CD  . GLN B  1 154 ? 17.611  267.887 23.030  1.00 53.41  ? 153 GLN B CD  1 
ATOM   2243  O  OE1 . GLN B  1 154 ? 17.562  268.353 21.866  1.00 47.29  ? 153 GLN B OE1 1 
ATOM   2244  N  NE2 . GLN B  1 154 ? 18.253  268.489 24.056  1.00 47.10  ? 153 GLN B NE2 1 
ATOM   2245  O  OXT . GLN B  1 154 ? 15.638  264.386 25.121  1.00 58.51  ? 153 GLN B OXT 1 
ATOM   2246  N  N   . MET C  1 1   ? -2.656  198.673 32.881  1.00 50.81  ? 0   MET C N   1 
ATOM   2247  C  CA  . MET C  1 1   ? -3.227  199.657 31.914  1.00 58.70  ? 0   MET C CA  1 
ATOM   2248  C  C   . MET C  1 1   ? -3.756  199.062 30.536  1.00 61.99  ? 0   MET C C   1 
ATOM   2249  O  O   . MET C  1 1   ? -4.993  199.092 30.204  1.00 55.39  ? 0   MET C O   1 
ATOM   2250  C  CB  . MET C  1 1   ? -2.208  200.797 31.667  1.00 59.17  ? 0   MET C CB  1 
ATOM   2251  C  CG  . MET C  1 1   ? -2.910  202.069 31.139  1.00 70.08  ? 0   MET C CG  1 
ATOM   2252  S  SD  . MET C  1 1   ? -4.392  202.660 32.140  1.00 80.27  ? 0   MET C SD  1 
ATOM   2253  C  CE  . MET C  1 1   ? -5.913  202.458 31.084  1.00 59.72  ? 0   MET C CE  1 
ATOM   2254  N  N   . ALA C  1 2   ? -2.801  198.583 29.728  1.00 52.07  ? 1   ALA C N   1 
ATOM   2255  C  CA  . ALA C  1 2   ? -3.061  198.054 28.384  1.00 49.22  ? 1   ALA C CA  1 
ATOM   2256  C  C   . ALA C  1 2   ? -3.718  196.599 28.419  1.00 46.46  ? 1   ALA C C   1 
ATOM   2257  O  O   . ALA C  1 2   ? -3.210  195.710 29.095  1.00 41.63  ? 1   ALA C O   1 
ATOM   2258  C  CB  . ALA C  1 2   ? -1.722  198.029 27.682  1.00 44.22  ? 1   ALA C CB  1 
ATOM   2259  N  N   . THR C  1 3   ? -4.827  196.395 27.719  1.00 38.97  ? 2   THR C N   1 
ATOM   2260  C  CA  . THR C  1 3   ? -5.432  195.076 27.584  1.00 39.81  ? 2   THR C CA  1 
ATOM   2261  C  C   . THR C  1 3   ? -5.315  194.534 26.148  1.00 38.91  ? 2   THR C C   1 
ATOM   2262  O  O   . THR C  1 3   ? -5.564  193.352 25.933  1.00 39.27  ? 2   THR C O   1 
ATOM   2263  C  CB  . THR C  1 3   ? -6.942  195.028 28.008  1.00 39.22  ? 2   THR C CB  1 
ATOM   2264  O  OG1 . THR C  1 3   ? -7.691  195.994 27.282  1.00 38.60  ? 2   THR C OG1 1 
ATOM   2265  C  CG2 . THR C  1 3   ? -7.116  195.313 29.428  1.00 35.09  ? 2   THR C CG2 1 
ATOM   2266  N  N   . LYS C  1 4   ? -4.894  195.377 25.205  1.00 38.33  ? 3   LYS C N   1 
ATOM   2267  C  CA  . LYS C  1 4   ? -4.779  195.030 23.789  1.00 37.11  ? 3   LYS C CA  1 
ATOM   2268  C  C   . LYS C  1 4   ? -3.602  195.647 23.140  1.00 35.82  ? 3   LYS C C   1 
ATOM   2269  O  O   . LYS C  1 4   ? -3.332  196.835 23.312  1.00 39.13  ? 3   LYS C O   1 
ATOM   2270  C  CB  . LYS C  1 4   ? -6.001  195.479 23.035  1.00 39.77  ? 3   LYS C CB  1 
ATOM   2271  C  CG  . LYS C  1 4   ? -7.112  194.450 23.073  1.00 49.40  ? 3   LYS C CG  1 
ATOM   2272  C  CD  . LYS C  1 4   ? -8.487  195.116 22.954  1.00 55.74  ? 3   LYS C CD  1 
ATOM   2273  C  CE  . LYS C  1 4   ? -9.681  194.215 23.330  1.00 61.12  ? 3   LYS C CE  1 
ATOM   2274  N  NZ  . LYS C  1 4   ? -9.960  193.042 22.381  1.00 58.82  ? 3   LYS C NZ  1 
ATOM   2275  N  N   . ALA C  1 5   ? -2.924  194.859 22.325  1.00 34.58  ? 4   ALA C N   1 
ATOM   2276  C  CA  . ALA C  1 5   ? -1.812  195.358 21.544  1.00 32.49  ? 4   ALA C CA  1 
ATOM   2277  C  C   . ALA C  1 5   ? -1.939  194.873 20.066  1.00 34.34  ? 4   ALA C C   1 
ATOM   2278  O  O   . ALA C  1 5   ? -2.791  194.001 19.791  1.00 33.19  ? 4   ALA C O   1 
ATOM   2279  C  CB  . ALA C  1 5   ? -0.522  194.941 22.216  1.00 26.05  ? 4   ALA C CB  1 
ATOM   2280  N  N   . VAL C  1 6   ? -1.142  195.438 19.134  1.00 30.49  ? 5   VAL C N   1 
ATOM   2281  C  CA  . VAL C  1 6   ? -1.152  195.034 17.736  1.00 26.63  ? 5   VAL C CA  1 
ATOM   2282  C  C   . VAL C  1 6   ? 0.246   195.200 17.149  1.00 28.58  ? 5   VAL C C   1 
ATOM   2283  O  O   . VAL C  1 6   ? 1.000   196.021 17.570  1.00 30.49  ? 5   VAL C O   1 
ATOM   2284  C  CB  . VAL C  1 6   ? -2.256  195.770 16.968  1.00 28.09  ? 5   VAL C CB  1 
ATOM   2285  C  CG1 . VAL C  1 6   ? -1.856  197.214 16.665  1.00 31.34  ? 5   VAL C CG1 1 
ATOM   2286  C  CG2 . VAL C  1 6   ? -2.646  195.068 15.674  1.00 26.39  ? 5   VAL C CG2 1 
ATOM   2287  N  N   . CYS C  1 7   ? 0.632   194.387 16.198  1.00 29.78  ? 6   CYS C N   1 
ATOM   2288  C  CA  . CYS C  1 7   ? 1.965   194.525 15.582  1.00 32.43  ? 6   CYS C CA  1 
ATOM   2289  C  C   . CYS C  1 7   ? 1.856   194.303 14.062  1.00 31.49  ? 6   CYS C C   1 
ATOM   2290  O  O   . CYS C  1 7   ? 1.362   193.252 13.666  1.00 32.85  ? 6   CYS C O   1 
ATOM   2291  C  CB  . CYS C  1 7   ? 2.988   193.529 16.152  1.00 32.56  ? 6   CYS C CB  1 
ATOM   2292  S  SG  . CYS C  1 7   ? 4.686   193.803 15.544  1.00 30.78  ? 6   CYS C SG  1 
ATOM   2293  N  N   . VAL C  1 8   ? 2.251   195.296 13.250  1.00 27.74  ? 7   VAL C N   1 
ATOM   2294  C  CA  . VAL C  1 8   ? 2.283   195.135 11.855  1.00 28.51  ? 7   VAL C CA  1 
ATOM   2295  C  C   . VAL C  1 8   ? 3.682   194.677 11.441  1.00 29.40  ? 7   VAL C C   1 
ATOM   2296  O  O   . VAL C  1 8   ? 4.635   195.383 11.613  1.00 32.81  ? 7   VAL C O   1 
ATOM   2297  C  CB  . VAL C  1 8   ? 1.831   196.410 11.129  1.00 31.30  ? 7   VAL C CB  1 
ATOM   2298  C  CG1 . VAL C  1 8   ? 1.929   196.182 9.627   1.00 24.75  ? 7   VAL C CG1 1 
ATOM   2299  C  CG2 . VAL C  1 8   ? 0.410   196.853 11.528  1.00 26.74  ? 7   VAL C CG2 1 
ATOM   2300  N  N   . LEU C  1 9   ? 3.827   193.464 10.946  1.00 30.82  ? 8   LEU C N   1 
ATOM   2301  C  CA  . LEU C  1 9   ? 5.148   192.990 10.544  1.00 32.54  ? 8   LEU C CA  1 
ATOM   2302  C  C   . LEU C  1 9   ? 5.444   193.337 9.086   1.00 32.60  ? 8   LEU C C   1 
ATOM   2303  O  O   . LEU C  1 9   ? 4.570   193.117 8.212   1.00 33.01  ? 8   LEU C O   1 
ATOM   2304  C  CB  . LEU C  1 9   ? 5.278   191.487 10.777  1.00 35.49  ? 8   LEU C CB  1 
ATOM   2305  C  CG  . LEU C  1 9   ? 4.951   190.956 12.174  1.00 36.20  ? 8   LEU C CG  1 
ATOM   2306  C  CD1 . LEU C  1 9   ? 4.424   189.550 12.110  1.00 36.86  ? 8   LEU C CD1 1 
ATOM   2307  C  CD2 . LEU C  1 9   ? 6.263   190.914 12.870  1.00 35.99  ? 8   LEU C CD2 1 
ATOM   2308  N  N   . LYS C  1 10  ? 6.650   193.877 8.847   1.00 29.89  ? 9   LYS C N   1 
ATOM   2309  C  CA  . LYS C  1 10  ? 7.101   194.268 7.520   1.00 30.27  ? 9   LYS C CA  1 
ATOM   2310  C  C   . LYS C  1 10  ? 8.541   193.946 7.389   1.00 30.55  ? 9   LYS C C   1 
ATOM   2311  O  O   . LYS C  1 10  ? 9.298   194.000 8.339   1.00 32.29  ? 9   LYS C O   1 
ATOM   2312  C  CB  . LYS C  1 10  ? 6.959   195.764 7.294   1.00 33.53  ? 9   LYS C CB  1 
ATOM   2313  C  CG  . LYS C  1 10  ? 5.530   196.221 7.319   1.00 42.64  ? 9   LYS C CG  1 
ATOM   2314  C  CD  . LYS C  1 10  ? 5.244   197.299 6.286   1.00 46.19  ? 9   LYS C CD  1 
ATOM   2315  C  CE  . LYS C  1 10  ? 3.757   197.721 6.195   1.00 43.30  ? 9   LYS C CE  1 
ATOM   2316  N  NZ  . LYS C  1 10  ? 3.761   198.924 7.077   1.00 40.57  ? 9   LYS C NZ  1 
ATOM   2317  N  N   . GLY C  1 11  ? 8.954   193.627 6.187   1.00 31.53  ? 10  GLY C N   1 
ATOM   2318  C  CA  . GLY C  1 11  ? 10.376  193.601 5.931   1.00 35.13  ? 10  GLY C CA  1 
ATOM   2319  C  C   . GLY C  1 11  ? 10.819  194.050 4.561   1.00 33.90  ? 10  GLY C C   1 
ATOM   2320  O  O   . GLY C  1 11  ? 10.112  194.682 3.887   1.00 34.91  ? 10  GLY C O   1 
ATOM   2321  N  N   . ASP C  1 12  ? 12.027  193.687 4.204   1.00 37.62  ? 11  ASP C N   1 
ATOM   2322  C  CA  . ASP C  1 12  ? 12.570  193.801 2.893   1.00 44.30  ? 11  ASP C CA  1 
ATOM   2323  C  C   . ASP C  1 12  ? 11.997  192.860 1.804   1.00 42.83  ? 11  ASP C C   1 
ATOM   2324  O  O   . ASP C  1 12  ? 11.910  193.218 0.651   1.00 45.16  ? 11  ASP C O   1 
ATOM   2325  C  CB  . ASP C  1 12  ? 14.011  193.422 3.057   1.00 54.19  ? 11  ASP C CB  1 
ATOM   2326  C  CG  . ASP C  1 12  ? 14.936  194.610 2.929   1.00 71.46  ? 11  ASP C CG  1 
ATOM   2327  O  OD1 . ASP C  1 12  ? 14.928  195.494 3.862   1.00 61.46  ? 11  ASP C OD1 1 
ATOM   2328  O  OD2 . ASP C  1 12  ? 15.665  194.635 1.875   1.00 70.82  ? 11  ASP C OD2 1 
ATOM   2329  N  N   . GLY C  1 13  ? 11.716  191.625 2.157   1.00 39.78  ? 12  GLY C N   1 
ATOM   2330  C  CA  . GLY C  1 13  ? 11.180  190.664 1.249   1.00 35.97  ? 12  GLY C CA  1 
ATOM   2331  C  C   . GLY C  1 13  ? 9.686   190.614 1.378   1.00 35.06  ? 12  GLY C C   1 
ATOM   2332  O  O   . GLY C  1 13  ? 9.045   191.606 1.754   1.00 35.92  ? 12  GLY C O   1 
ATOM   2333  N  N   . PRO C  1 14  ? 9.121   189.446 1.090   1.00 33.40  ? 13  PRO C N   1 
ATOM   2334  C  CA  . PRO C  1 14  ? 7.683   189.379 0.939   1.00 33.19  ? 13  PRO C CA  1 
ATOM   2335  C  C   . PRO C  1 14  ? 6.926   189.118 2.226   1.00 34.22  ? 13  PRO C C   1 
ATOM   2336  O  O   . PRO C  1 14  ? 5.690   189.073 2.199   1.00 34.59  ? 13  PRO C O   1 
ATOM   2337  C  CB  . PRO C  1 14  ? 7.483   188.263 -0.065  1.00 27.71  ? 13  PRO C CB  1 
ATOM   2338  C  CG  . PRO C  1 14  ? 8.698   187.458 0.034   1.00 29.26  ? 13  PRO C CG  1 
ATOM   2339  C  CD  . PRO C  1 14  ? 9.801   188.234 0.650   1.00 30.17  ? 13  PRO C CD  1 
ATOM   2340  N  N   . VAL C  1 15  ? 7.631   188.986 3.338   1.00 32.48  ? 14  VAL C N   1 
ATOM   2341  C  CA  . VAL C  1 15  ? 6.965   188.561 4.596   1.00 35.24  ? 14  VAL C CA  1 
ATOM   2342  C  C   . VAL C  1 15  ? 6.208   189.708 5.215   1.00 36.76  ? 14  VAL C C   1 
ATOM   2343  O  O   . VAL C  1 15  ? 6.773   190.779 5.451   1.00 35.54  ? 14  VAL C O   1 
ATOM   2344  C  CB  . VAL C  1 15  ? 7.947   187.962 5.647   1.00 33.34  ? 14  VAL C CB  1 
ATOM   2345  C  CG1 . VAL C  1 15  ? 7.212   187.569 6.895   1.00 32.83  ? 14  VAL C CG1 1 
ATOM   2346  C  CG2 . VAL C  1 15  ? 8.707   186.751 5.105   1.00 32.06  ? 14  VAL C CG2 1 
ATOM   2347  N  N   . GLN C  1 16  ? 4.938   189.482 5.503   1.00 37.26  ? 15  GLN C N   1 
ATOM   2348  C  CA  . GLN C  1 16  ? 4.188   190.486 6.192   1.00 38.10  ? 15  GLN C CA  1 
ATOM   2349  C  C   . GLN C  1 16  ? 2.979   189.898 6.961   1.00 40.27  ? 15  GLN C C   1 
ATOM   2350  O  O   . GLN C  1 16  ? 2.498   188.804 6.665   1.00 35.12  ? 15  GLN C O   1 
ATOM   2351  C  CB  . GLN C  1 16  ? 3.791   191.612 5.220   1.00 38.52  ? 15  GLN C CB  1 
ATOM   2352  C  CG  . GLN C  1 16  ? 3.134   191.122 3.949   1.00 44.40  ? 15  GLN C CG  1 
ATOM   2353  C  CD  . GLN C  1 16  ? 3.017   192.159 2.812   1.00 44.69  ? 15  GLN C CD  1 
ATOM   2354  O  OE1 . GLN C  1 16  ? 2.947   193.341 3.052   1.00 48.49  ? 15  GLN C OE1 1 
ATOM   2355  N  NE2 . GLN C  1 16  ? 2.939   191.697 1.579   1.00 44.72  ? 15  GLN C NE2 1 
ATOM   2356  N  N   . GLY C  1 17  ? 2.551   190.618 8.005   1.00 37.53  ? 16  GLY C N   1 
ATOM   2357  C  CA  . GLY C  1 17  ? 1.365   190.237 8.699   1.00 34.87  ? 16  GLY C CA  1 
ATOM   2358  C  C   . GLY C  1 17  ? 0.974   191.092 9.906   1.00 39.41  ? 16  GLY C C   1 
ATOM   2359  O  O   . GLY C  1 17  ? 1.629   192.079 10.261  1.00 40.02  ? 16  GLY C O   1 
ATOM   2360  N  N   . ILE C  1 18  ? -0.095  190.664 10.544  1.00 35.62  ? 17  ILE C N   1 
ATOM   2361  C  CA  . ILE C  1 18  ? -0.670  191.359 11.603  1.00 36.07  ? 17  ILE C CA  1 
ATOM   2362  C  C   . ILE C  1 18  ? -0.858  190.392 12.758  1.00 36.85  ? 17  ILE C C   1 
ATOM   2363  O  O   . ILE C  1 18  ? -1.566  189.390 12.640  1.00 35.58  ? 17  ILE C O   1 
ATOM   2364  C  CB  . ILE C  1 18  ? -1.992  192.016 11.155  1.00 35.23  ? 17  ILE C CB  1 
ATOM   2365  C  CG1 . ILE C  1 18  ? -1.676  192.967 10.022  1.00 32.22  ? 17  ILE C CG1 1 
ATOM   2366  C  CG2 . ILE C  1 18  ? -2.680  192.719 12.337  1.00 30.73  ? 17  ILE C CG2 1 
ATOM   2367  C  CD1 . ILE C  1 18  ? -2.884  193.697 9.497   1.00 34.24  ? 17  ILE C CD1 1 
ATOM   2368  N  N   . ILE C  1 19  ? -0.247  190.732 13.896  1.00 36.08  ? 18  ILE C N   1 
ATOM   2369  C  CA  . ILE C  1 19  ? -0.428  189.965 15.099  1.00 32.52  ? 18  ILE C CA  1 
ATOM   2370  C  C   . ILE C  1 19  ? -1.131  190.786 16.170  1.00 31.80  ? 18  ILE C C   1 
ATOM   2371  O  O   . ILE C  1 19  ? -0.745  191.872 16.471  1.00 33.38  ? 18  ILE C O   1 
ATOM   2372  C  CB  . ILE C  1 19  ? 0.950   189.470 15.545  1.00 32.05  ? 18  ILE C CB  1 
ATOM   2373  C  CG1 . ILE C  1 19  ? 1.587   188.624 14.436  1.00 31.56  ? 18  ILE C CG1 1 
ATOM   2374  C  CG2 . ILE C  1 19  ? 0.933   188.794 16.914  1.00 27.23  ? 18  ILE C CG2 1 
ATOM   2375  C  CD1 . ILE C  1 19  ? 0.830   187.375 14.032  1.00 29.47  ? 18  ILE C CD1 1 
ATOM   2376  N  N   . ASN C  1 20  ? -2.173  190.239 16.750  1.00 35.46  ? 19  ASN C N   1 
ATOM   2377  C  CA  . ASN C  1 20  ? -2.887  190.859 17.845  1.00 31.08  ? 19  ASN C CA  1 
ATOM   2378  C  C   . ASN C  1 20  ? -2.469  190.267 19.191  1.00 32.89  ? 19  ASN C C   1 
ATOM   2379  O  O   . ASN C  1 20  ? -2.070  189.120 19.266  1.00 34.54  ? 19  ASN C O   1 
ATOM   2380  C  CB  . ASN C  1 20  ? -4.334  190.630 17.641  1.00 30.01  ? 19  ASN C CB  1 
ATOM   2381  C  CG  . ASN C  1 20  ? -4.805  191.061 16.293  1.00 34.48  ? 19  ASN C CG  1 
ATOM   2382  O  OD1 . ASN C  1 20  ? -5.031  190.240 15.409  1.00 38.25  ? 19  ASN C OD1 1 
ATOM   2383  N  ND2 . ASN C  1 20  ? -4.966  192.333 16.112  1.00 34.65  ? 19  ASN C ND2 1 
ATOM   2384  N  N   . PHE C  1 21  ? -2.501  191.078 20.257  1.00 36.49  ? 20  PHE C N   1 
ATOM   2385  C  CA  . PHE C  1 21  ? -2.280  190.626 21.647  1.00 31.82  ? 20  PHE C CA  1 
ATOM   2386  C  C   . PHE C  1 21  ? -3.456  191.023 22.464  1.00 34.93  ? 20  PHE C C   1 
ATOM   2387  O  O   . PHE C  1 21  ? -4.126  191.966 22.121  1.00 36.36  ? 20  PHE C O   1 
ATOM   2388  C  CB  . PHE C  1 21  ? -1.076  191.195 22.268  1.00 27.99  ? 20  PHE C CB  1 
ATOM   2389  C  CG  . PHE C  1 21  ? 0.150   190.967 21.481  1.00 29.24  ? 20  PHE C CG  1 
ATOM   2390  C  CD1 . PHE C  1 21  ? 0.405   191.699 20.300  1.00 28.66  ? 20  PHE C CD1 1 
ATOM   2391  C  CD2 . PHE C  1 21  ? 1.087   190.100 21.933  1.00 29.23  ? 20  PHE C CD2 1 
ATOM   2392  C  CE1 . PHE C  1 21  ? 1.555   191.487 19.607  1.00 27.40  ? 20  PHE C CE1 1 
ATOM   2393  C  CE2 . PHE C  1 21  ? 2.256   189.885 21.252  1.00 30.83  ? 20  PHE C CE2 1 
ATOM   2394  C  CZ  . PHE C  1 21  ? 2.495   190.573 20.087  1.00 29.22  ? 20  PHE C CZ  1 
ATOM   2395  N  N   . GLU C  1 22  ? -3.793  190.198 23.452  1.00 37.94  ? 21  GLU C N   1 
ATOM   2396  C  CA  . GLU C  1 22  ? -4.963  190.428 24.316  1.00 37.81  ? 21  GLU C CA  1 
ATOM   2397  C  C   . GLU C  1 22  ? -4.785  189.870 25.726  1.00 38.30  ? 21  GLU C C   1 
ATOM   2398  O  O   . GLU C  1 22  ? -4.478  188.673 25.893  1.00 38.37  ? 21  GLU C O   1 
ATOM   2399  C  CB  . GLU C  1 22  ? -6.260  189.977 23.714  1.00 37.81  ? 21  GLU C CB  1 
ATOM   2400  C  CG  . GLU C  1 22  ? -7.363  190.288 24.689  1.00 47.50  ? 21  GLU C CG  1 
ATOM   2401  C  CD  . GLU C  1 22  ? -8.725  189.952 24.166  1.00 56.72  ? 21  GLU C CD  1 
ATOM   2402  O  OE1 . GLU C  1 22  ? -9.052  188.750 23.919  1.00 56.45  ? 21  GLU C OE1 1 
ATOM   2403  O  OE2 . GLU C  1 22  ? -9.459  190.929 24.004  1.00 59.80  ? 21  GLU C OE2 1 
ATOM   2404  N  N   . GLN C  1 23  ? -4.871  190.764 26.715  1.00 35.34  ? 22  GLN C N   1 
ATOM   2405  C  CA  . GLN C  1 23  ? -4.653  190.350 28.100  1.00 39.21  ? 22  GLN C CA  1 
ATOM   2406  C  C   . GLN C  1 23  ? -5.766  190.928 28.966  1.00 42.54  ? 22  GLN C C   1 
ATOM   2407  O  O   . GLN C  1 23  ? -5.670  192.077 29.390  1.00 42.65  ? 22  GLN C O   1 
ATOM   2408  C  CB  . GLN C  1 23  ? -3.298  190.803 28.568  1.00 33.59  ? 22  GLN C CB  1 
ATOM   2409  C  CG  . GLN C  1 23  ? -2.810  190.161 29.788  1.00 31.32  ? 22  GLN C CG  1 
ATOM   2410  C  CD  . GLN C  1 23  ? -1.496  190.751 30.255  1.00 35.09  ? 22  GLN C CD  1 
ATOM   2411  O  OE1 . GLN C  1 23  ? -1.058  191.781 29.770  1.00 32.98  ? 22  GLN C OE1 1 
ATOM   2412  N  NE2 . GLN C  1 23  ? -0.847  190.087 31.230  1.00 35.09  ? 22  GLN C NE2 1 
ATOM   2413  N  N   . LYS C  1 24  ? -6.828  190.140 29.203  1.00 43.62  ? 23  LYS C N   1 
ATOM   2414  C  CA  . LYS C  1 24  ? -7.969  190.637 29.978  1.00 42.91  ? 23  LYS C CA  1 
ATOM   2415  C  C   . LYS C  1 24  ? -7.590  190.988 31.380  1.00 41.60  ? 23  LYS C C   1 
ATOM   2416  O  O   . LYS C  1 24  ? -8.107  191.956 31.871  1.00 40.92  ? 23  LYS C O   1 
ATOM   2417  C  CB  . LYS C  1 24  ? -9.123  189.647 30.012  1.00 49.61  ? 23  LYS C CB  1 
ATOM   2418  C  CG  . LYS C  1 24  ? -10.006 189.881 28.818  1.00 51.58  ? 23  LYS C CG  1 
ATOM   2419  C  CD  . LYS C  1 24  ? -10.733 188.605 28.478  1.00 58.14  ? 23  LYS C CD  1 
ATOM   2420  C  CE  . LYS C  1 24  ? -11.836 188.979 27.481  1.00 68.27  ? 23  LYS C CE  1 
ATOM   2421  N  NZ  . LYS C  1 24  ? -12.662 187.792 27.077  1.00 68.32  ? 23  LYS C NZ  1 
ATOM   2422  N  N   . GLU C  1 25  ? -6.664  190.233 31.994  1.00 39.80  ? 24  GLU C N   1 
ATOM   2423  C  CA  . GLU C  1 25  ? -6.249  190.446 33.385  1.00 39.28  ? 24  GLU C CA  1 
ATOM   2424  C  C   . GLU C  1 25  ? -4.806  190.715 33.429  1.00 41.17  ? 24  GLU C C   1 
ATOM   2425  O  O   . GLU C  1 25  ? -4.028  189.996 32.771  1.00 39.54  ? 24  GLU C O   1 
ATOM   2426  C  CB  . GLU C  1 25  ? -6.455  189.187 34.230  1.00 47.89  ? 24  GLU C CB  1 
ATOM   2427  C  CG  . GLU C  1 25  ? -7.901  188.657 34.220  1.00 51.77  ? 24  GLU C CG  1 
ATOM   2428  C  CD  . GLU C  1 25  ? -8.787  189.518 35.081  1.00 60.83  ? 24  GLU C CD  1 
ATOM   2429  O  OE1 . GLU C  1 25  ? -8.212  190.225 36.003  1.00 54.30  ? 24  GLU C OE1 1 
ATOM   2430  O  OE2 . GLU C  1 25  ? -10.030 189.482 34.835  1.00 62.90  ? 24  GLU C OE2 1 
ATOM   2431  N  N   . SER C  1 26  ? -4.422  191.714 34.222  1.00 33.12  ? 25  SER C N   1 
ATOM   2432  C  CA  . SER C  1 26  ? -3.024  192.087 34.244  1.00 35.20  ? 25  SER C CA  1 
ATOM   2433  C  C   . SER C  1 26  ? -2.079  191.022 34.764  1.00 35.53  ? 25  SER C C   1 
ATOM   2434  O  O   . SER C  1 26  ? -0.844  191.136 34.653  1.00 34.28  ? 25  SER C O   1 
ATOM   2435  C  CB  . SER C  1 26  ? -2.866  193.296 35.144  1.00 39.96  ? 25  SER C CB  1 
ATOM   2436  O  OG  . SER C  1 26  ? -3.459  193.025 36.390  1.00 40.57  ? 25  SER C OG  1 
ATOM   2437  N  N   . ASN C  1 27  ? -2.657  190.043 35.454  1.00 41.34  ? 26  ASN C N   1 
ATOM   2438  C  CA  . ASN C  1 27  ? -1.881  188.973 36.122  1.00 46.09  ? 26  ASN C CA  1 
ATOM   2439  C  C   . ASN C  1 27  ? -2.159  187.641 35.406  1.00 43.17  ? 26  ASN C C   1 
ATOM   2440  O  O   . ASN C  1 27  ? -1.625  186.623 35.757  1.00 49.58  ? 26  ASN C O   1 
ATOM   2441  C  CB  . ASN C  1 27  ? -2.093  188.955 37.662  1.00 43.79  ? 26  ASN C CB  1 
ATOM   2442  C  CG  . ASN C  1 27  ? -3.486  188.478 38.096  1.00 45.37  ? 26  ASN C CG  1 
ATOM   2443  O  OD1 . ASN C  1 27  ? -4.509  188.602 37.379  1.00 42.49  ? 26  ASN C OD1 1 
ATOM   2444  N  ND2 . ASN C  1 27  ? -3.509  187.872 39.301  1.00 45.38  ? 26  ASN C ND2 1 
ATOM   2445  N  N   . GLY C  1 28  ? -2.970  187.726 34.360  1.00 41.59  ? 27  GLY C N   1 
ATOM   2446  C  CA  . GLY C  1 28  ? -3.204  186.641 33.477  1.00 44.05  ? 27  GLY C CA  1 
ATOM   2447  C  C   . GLY C  1 28  ? -2.386  186.504 32.181  1.00 46.25  ? 27  GLY C C   1 
ATOM   2448  O  O   . GLY C  1 28  ? -1.401  187.196 31.916  1.00 41.65  ? 27  GLY C O   1 
ATOM   2449  N  N   . PRO C  1 29  ? -2.794  185.545 31.356  1.00 51.87  ? 28  PRO C N   1 
ATOM   2450  C  CA  . PRO C  1 29  ? -1.940  185.289 30.195  1.00 44.36  ? 28  PRO C CA  1 
ATOM   2451  C  C   . PRO C  1 29  ? -2.356  186.164 28.994  1.00 39.49  ? 28  PRO C C   1 
ATOM   2452  O  O   . PRO C  1 29  ? -3.522  186.679 28.929  1.00 35.34  ? 28  PRO C O   1 
ATOM   2453  C  CB  . PRO C  1 29  ? -2.228  183.792 29.940  1.00 45.21  ? 28  PRO C CB  1 
ATOM   2454  C  CG  . PRO C  1 29  ? -3.723  183.621 30.326  1.00 42.48  ? 28  PRO C CG  1 
ATOM   2455  C  CD  . PRO C  1 29  ? -3.907  184.543 31.500  1.00 41.24  ? 28  PRO C CD  1 
ATOM   2456  N  N   . VAL C  1 30  ? -1.412  186.323 28.055  1.00 38.22  ? 29  VAL C N   1 
ATOM   2457  C  CA  . VAL C  1 30  ? -1.698  187.001 26.766  1.00 33.72  ? 29  VAL C CA  1 
ATOM   2458  C  C   . VAL C  1 30  ? -2.112  186.048 25.628  1.00 33.16  ? 29  VAL C C   1 
ATOM   2459  O  O   . VAL C  1 30  ? -1.435  185.078 25.361  1.00 33.52  ? 29  VAL C O   1 
ATOM   2460  C  CB  . VAL C  1 30  ? -0.497  187.863 26.372  1.00 32.99  ? 29  VAL C CB  1 
ATOM   2461  C  CG1 . VAL C  1 30  ? -0.912  188.852 25.268  1.00 27.88  ? 29  VAL C CG1 1 
ATOM   2462  C  CG2 . VAL C  1 30  ? 0.084   188.533 27.652  1.00 30.17  ? 29  VAL C CG2 1 
ATOM   2463  N  N   . LYS C  1 31  ? -3.242  186.304 24.992  1.00 32.20  ? 30  LYS C N   1 
ATOM   2464  C  CA  . LYS C  1 31  ? -3.587  185.637 23.733  1.00 36.50  ? 30  LYS C CA  1 
ATOM   2465  C  C   . LYS C  1 31  ? -2.863  186.304 22.560  1.00 38.29  ? 30  LYS C C   1 
ATOM   2466  O  O   . LYS C  1 31  ? -3.014  187.507 22.363  1.00 39.11  ? 30  LYS C O   1 
ATOM   2467  C  CB  . LYS C  1 31  ? -5.064  185.766 23.386  1.00 37.96  ? 30  LYS C CB  1 
ATOM   2468  C  CG  . LYS C  1 31  ? -6.001  184.794 24.083  1.00 49.47  ? 30  LYS C CG  1 
ATOM   2469  C  CD  . LYS C  1 31  ? -7.413  184.784 23.408  1.00 62.43  ? 30  LYS C CD  1 
ATOM   2470  C  CE  . LYS C  1 31  ? -7.395  184.522 21.850  1.00 67.35  ? 30  LYS C CE  1 
ATOM   2471  N  NZ  . LYS C  1 31  ? -8.417  185.187 20.940  1.00 61.68  ? 30  LYS C NZ  1 
ATOM   2472  N  N   . VAL C  1 32  ? -2.158  185.535 21.734  1.00 37.16  ? 31  VAL C N   1 
ATOM   2473  C  CA  . VAL C  1 32  ? -1.433  186.099 20.600  1.00 37.61  ? 31  VAL C CA  1 
ATOM   2474  C  C   . VAL C  1 32  ? -1.994  185.498 19.325  1.00 39.40  ? 31  VAL C C   1 
ATOM   2475  O  O   . VAL C  1 32  ? -1.874  184.305 19.096  1.00 43.93  ? 31  VAL C O   1 
ATOM   2476  C  CB  . VAL C  1 32  ? 0.099   185.853 20.774  1.00 37.36  ? 31  VAL C CB  1 
ATOM   2477  C  CG1 . VAL C  1 32  ? 0.895   186.451 19.662  1.00 33.55  ? 31  VAL C CG1 1 
ATOM   2478  C  CG2 . VAL C  1 32  ? 0.617   186.436 22.096  1.00 30.53  ? 31  VAL C CG2 1 
ATOM   2479  N  N   . TRP C  1 33  ? -2.624  186.290 18.486  1.00 38.07  ? 32  TRP C N   1 
ATOM   2480  C  CA  . TRP C  1 33  ? -3.153  185.695 17.266  1.00 36.03  ? 32  TRP C CA  1 
ATOM   2481  C  C   . TRP C  1 33  ? -2.987  186.541 16.013  1.00 34.68  ? 32  TRP C C   1 
ATOM   2482  O  O   . TRP C  1 33  ? -2.714  187.725 16.092  1.00 37.67  ? 32  TRP C O   1 
ATOM   2483  C  CB  . TRP C  1 33  ? -4.622  185.248 17.451  1.00 33.57  ? 32  TRP C CB  1 
ATOM   2484  C  CG  . TRP C  1 33  ? -5.635  186.307 17.403  1.00 31.55  ? 32  TRP C CG  1 
ATOM   2485  C  CD1 . TRP C  1 33  ? -6.501  186.615 16.379  1.00 32.88  ? 32  TRP C CD1 1 
ATOM   2486  C  CD2 . TRP C  1 33  ? -5.918  187.216 18.445  1.00 33.12  ? 32  TRP C CD2 1 
ATOM   2487  N  NE1 . TRP C  1 33  ? -7.320  187.718 16.732  1.00 31.30  ? 32  TRP C NE1 1 
ATOM   2488  C  CE2 . TRP C  1 33  ? -6.966  188.080 18.003  1.00 33.27  ? 32  TRP C CE2 1 
ATOM   2489  C  CE3 . TRP C  1 33  ? -5.359  187.428 19.699  1.00 33.38  ? 32  TRP C CE3 1 
ATOM   2490  C  CZ2 . TRP C  1 33  ? -7.441  189.115 18.792  1.00 36.84  ? 32  TRP C CZ2 1 
ATOM   2491  C  CZ3 . TRP C  1 33  ? -5.826  188.462 20.457  1.00 37.32  ? 32  TRP C CZ3 1 
ATOM   2492  C  CH2 . TRP C  1 33  ? -6.875  189.289 20.014  1.00 36.17  ? 32  TRP C CH2 1 
ATOM   2493  N  N   . GLY C  1 34  ? -3.158  185.898 14.872  1.00 31.44  ? 33  GLY C N   1 
ATOM   2494  C  CA  . GLY C  1 34  ? -3.192  186.529 13.556  1.00 34.79  ? 33  GLY C CA  1 
ATOM   2495  C  C   . GLY C  1 34  ? -2.488  185.716 12.473  1.00 36.69  ? 33  GLY C C   1 
ATOM   2496  O  O   . GLY C  1 34  ? -2.368  184.531 12.551  1.00 39.51  ? 33  GLY C O   1 
ATOM   2497  N  N   . SER C  1 35  ? -1.942  186.381 11.488  1.00 38.42  ? 34  SER C N   1 
ATOM   2498  C  CA  . SER C  1 35  ? -1.579  185.743 10.275  1.00 37.04  ? 34  SER C CA  1 
ATOM   2499  C  C   . SER C  1 35  ? -0.279  186.346 9.712   1.00 37.66  ? 34  SER C C   1 
ATOM   2500  O  O   . SER C  1 35  ? -0.110  187.549 9.671   1.00 38.07  ? 34  SER C O   1 
ATOM   2501  C  CB  . SER C  1 35  ? -2.738  186.019 9.354   1.00 35.18  ? 34  SER C CB  1 
ATOM   2502  O  OG  . SER C  1 35  ? -2.605  185.142 8.297   1.00 47.42  ? 34  SER C OG  1 
ATOM   2503  N  N   . ILE C  1 36  ? 0.648   185.512 9.308   1.00 35.69  ? 35  ILE C N   1 
ATOM   2504  C  CA  . ILE C  1 36  ? 1.821   185.964 8.568   1.00 33.47  ? 35  ILE C CA  1 
ATOM   2505  C  C   . ILE C  1 36  ? 1.838   185.285 7.201   1.00 35.05  ? 35  ILE C C   1 
ATOM   2506  O  O   . ILE C  1 36  ? 1.528   184.108 7.077   1.00 30.12  ? 35  ILE C O   1 
ATOM   2507  C  CB  . ILE C  1 36  ? 3.082   185.639 9.314   1.00 31.26  ? 35  ILE C CB  1 
ATOM   2508  C  CG1 . ILE C  1 36  ? 2.904   186.090 10.776  1.00 32.40  ? 35  ILE C CG1 1 
ATOM   2509  C  CG2 . ILE C  1 36  ? 4.277   186.320 8.666   1.00 27.26  ? 35  ILE C CG2 1 
ATOM   2510  C  CD1 . ILE C  1 36  ? 4.063   185.797 11.736  1.00 28.00  ? 35  ILE C CD1 1 
ATOM   2511  N  N   . LYS C  1 37  ? 2.149   186.046 6.154   1.00 36.41  ? 36  LYS C N   1 
ATOM   2512  C  CA  . LYS C  1 37  ? 2.191   185.481 4.795   1.00 33.74  ? 36  LYS C CA  1 
ATOM   2513  C  C   . LYS C  1 37  ? 3.517   185.805 4.196   1.00 31.93  ? 36  LYS C C   1 
ATOM   2514  O  O   . LYS C  1 37  ? 4.258   186.580 4.817   1.00 33.92  ? 36  LYS C O   1 
ATOM   2515  C  CB  . LYS C  1 37  ? 1.012   185.948 3.985   1.00 37.24  ? 36  LYS C CB  1 
ATOM   2516  C  CG  . LYS C  1 37  ? 1.173   187.357 3.490   1.00 45.44  ? 36  LYS C CG  1 
ATOM   2517  C  CD  . LYS C  1 37  ? -0.184  187.967 3.201   1.00 44.68  ? 36  LYS C CD  1 
ATOM   2518  C  CE  . LYS C  1 37  ? -0.092  189.504 3.190   1.00 47.85  ? 36  LYS C CE  1 
ATOM   2519  N  NZ  . LYS C  1 37  ? -1.041  189.985 2.139   1.00 44.67  ? 36  LYS C NZ  1 
ATOM   2520  N  N   . GLY C  1 38  ? 3.887   185.141 3.097   1.00 30.24  ? 37  GLY C N   1 
ATOM   2521  C  CA  . GLY C  1 38  ? 5.187   185.316 2.499   1.00 28.36  ? 37  GLY C CA  1 
ATOM   2522  C  C   . GLY C  1 38  ? 6.323   184.440 2.982   1.00 32.48  ? 37  GLY C C   1 
ATOM   2523  O  O   . GLY C  1 38  ? 7.530   184.693 2.724   1.00 32.03  ? 37  GLY C O   1 
ATOM   2524  N  N   . LEU C  1 39  ? 5.953   183.389 3.686   1.00 34.01  ? 38  LEU C N   1 
ATOM   2525  C  CA  . LEU C  1 39  ? 6.937   182.593 4.330   1.00 34.86  ? 38  LEU C CA  1 
ATOM   2526  C  C   . LEU C  1 39  ? 7.164   181.313 3.535   1.00 37.16  ? 38  LEU C C   1 
ATOM   2527  O  O   . LEU C  1 39  ? 6.249   180.877 2.801   1.00 33.90  ? 38  LEU C O   1 
ATOM   2528  C  CB  . LEU C  1 39  ? 6.458   182.301 5.747   1.00 36.18  ? 38  LEU C CB  1 
ATOM   2529  C  CG  . LEU C  1 39  ? 6.515   183.439 6.767   1.00 32.87  ? 38  LEU C CG  1 
ATOM   2530  C  CD1 . LEU C  1 39  ? 5.521   183.046 7.819   1.00 32.23  ? 38  LEU C CD1 1 
ATOM   2531  C  CD2 . LEU C  1 39  ? 7.908   183.600 7.396   1.00 30.72  ? 38  LEU C CD2 1 
ATOM   2532  N  N   . THR C  1 40  ? 8.384   180.765 3.654   1.00 33.52  ? 39  THR C N   1 
ATOM   2533  C  CA  . THR C  1 40  ? 8.708   179.484 3.109   1.00 37.75  ? 39  THR C CA  1 
ATOM   2534  C  C   . THR C  1 40  ? 8.047   178.456 4.024   1.00 43.73  ? 39  THR C C   1 
ATOM   2535  O  O   . THR C  1 40  ? 8.119   178.577 5.245   1.00 47.32  ? 39  THR C O   1 
ATOM   2536  C  CB  . THR C  1 40  ? 10.202  179.205 3.137   1.00 38.81  ? 39  THR C CB  1 
ATOM   2537  O  OG1 . THR C  1 40  ? 10.610  179.136 4.478   1.00 35.70  ? 39  THR C OG1 1 
ATOM   2538  C  CG2 . THR C  1 40  ? 11.012  180.305 2.446   1.00 38.29  ? 39  THR C CG2 1 
ATOM   2539  N  N   . GLU C  1 41  ? 7.382   177.469 3.437   1.00 43.20  ? 40  GLU C N   1 
ATOM   2540  C  CA  . GLU C  1 41  ? 6.675   176.466 4.190   1.00 42.14  ? 40  GLU C CA  1 
ATOM   2541  C  C   . GLU C  1 41  ? 7.518   175.819 5.308   1.00 43.20  ? 40  GLU C C   1 
ATOM   2542  O  O   . GLU C  1 41  ? 8.736   175.564 5.160   1.00 38.29  ? 40  GLU C O   1 
ATOM   2543  C  CB  . GLU C  1 41  ? 6.041   175.464 3.231   1.00 40.54  ? 40  GLU C CB  1 
ATOM   2544  C  CG  . GLU C  1 41  ? 5.896   174.055 3.765   1.00 50.16  ? 40  GLU C CG  1 
ATOM   2545  C  CD  . GLU C  1 41  ? 4.989   173.190 2.920   1.00 56.81  ? 40  GLU C CD  1 
ATOM   2546  O  OE1 . GLU C  1 41  ? 5.319   172.905 1.747   1.00 52.89  ? 40  GLU C OE1 1 
ATOM   2547  O  OE2 . GLU C  1 41  ? 3.925   172.788 3.439   1.00 58.58  ? 40  GLU C OE2 1 
ATOM   2548  N  N   . GLY C  1 42  ? 6.883   175.648 6.472   1.00 41.59  ? 41  GLY C N   1 
ATOM   2549  C  CA  . GLY C  1 42  ? 7.610   175.060 7.578   1.00 37.02  ? 41  GLY C CA  1 
ATOM   2550  C  C   . GLY C  1 42  ? 7.679   176.040 8.699   1.00 39.39  ? 41  GLY C C   1 
ATOM   2551  O  O   . GLY C  1 42  ? 6.835   176.955 8.777   1.00 38.18  ? 41  GLY C O   1 
ATOM   2552  N  N   . LEU C  1 43  ? 8.688   175.850 9.554   1.00 37.12  ? 42  LEU C N   1 
ATOM   2553  C  CA  . LEU C  1 43  ? 8.755   176.489 10.820  1.00 37.40  ? 42  LEU C CA  1 
ATOM   2554  C  C   . LEU C  1 43  ? 9.641   177.787 10.879  1.00 41.68  ? 42  LEU C C   1 
ATOM   2555  O  O   . LEU C  1 43  ? 10.791  177.807 10.320  1.00 39.17  ? 42  LEU C O   1 
ATOM   2556  C  CB  . LEU C  1 43  ? 9.236   175.467 11.871  1.00 41.04  ? 42  LEU C CB  1 
ATOM   2557  C  CG  . LEU C  1 43  ? 8.531   174.146 12.272  1.00 42.89  ? 42  LEU C CG  1 
ATOM   2558  C  CD1 . LEU C  1 43  ? 8.925   173.730 13.678  1.00 36.12  ? 42  LEU C CD1 1 
ATOM   2559  C  CD2 . LEU C  1 43  ? 7.055   174.329 12.185  1.00 49.49  ? 42  LEU C CD2 1 
ATOM   2560  N  N   . HIS C  1 44  ? 9.170   178.811 11.628  1.00 34.19  ? 43  HIS C N   1 
ATOM   2561  C  CA  . HIS C  1 44  ? 9.968   180.027 11.798  1.00 32.15  ? 43  HIS C CA  1 
ATOM   2562  C  C   . HIS C  1 44  ? 9.968   180.523 13.190  1.00 34.23  ? 43  HIS C C   1 
ATOM   2563  O  O   . HIS C  1 44  ? 8.889   180.622 13.872  1.00 34.53  ? 43  HIS C O   1 
ATOM   2564  C  CB  . HIS C  1 44  ? 9.345   181.099 10.933  1.00 36.80  ? 43  HIS C CB  1 
ATOM   2565  C  CG  . HIS C  1 44  ? 9.373   180.783 9.471   1.00 38.03  ? 43  HIS C CG  1 
ATOM   2566  N  ND1 . HIS C  1 44  ? 10.488  181.015 8.685   1.00 33.78  ? 43  HIS C ND1 1 
ATOM   2567  C  CD2 . HIS C  1 44  ? 8.462   180.164 8.679   1.00 34.17  ? 43  HIS C CD2 1 
ATOM   2568  C  CE1 . HIS C  1 44  ? 10.226  180.614 7.457   1.00 35.17  ? 43  HIS C CE1 1 
ATOM   2569  N  NE2 . HIS C  1 44  ? 9.010   180.087 7.427   1.00 36.73  ? 43  HIS C NE2 1 
ATOM   2570  N  N   . GLY C  1 45  ? 11.163  180.852 13.661  1.00 33.83  ? 44  GLY C N   1 
ATOM   2571  C  CA  . GLY C  1 45  ? 11.282  181.435 15.045  1.00 36.14  ? 44  GLY C CA  1 
ATOM   2572  C  C   . GLY C  1 45  ? 10.526  182.759 15.224  1.00 35.84  ? 44  GLY C C   1 
ATOM   2573  O  O   . GLY C  1 45  ? 10.489  183.563 14.308  1.00 38.06  ? 44  GLY C O   1 
ATOM   2574  N  N   . PHE C  1 46  ? 9.928   182.989 16.383  1.00 34.55  ? 45  PHE C N   1 
ATOM   2575  C  CA  . PHE C  1 46  ? 8.959   184.051 16.570  1.00 33.02  ? 45  PHE C CA  1 
ATOM   2576  C  C   . PHE C  1 46  ? 9.306   184.627 17.948  1.00 34.50  ? 45  PHE C C   1 
ATOM   2577  O  O   . PHE C  1 46  ? 9.091   184.009 18.929  1.00 39.83  ? 45  PHE C O   1 
ATOM   2578  C  CB  . PHE C  1 46  ? 7.590   183.403 16.540  1.00 30.47  ? 45  PHE C CB  1 
ATOM   2579  C  CG  . PHE C  1 46  ? 6.456   184.333 16.449  1.00 32.30  ? 45  PHE C CG  1 
ATOM   2580  C  CD1 . PHE C  1 46  ? 6.329   185.175 15.365  1.00 32.04  ? 45  PHE C CD1 1 
ATOM   2581  C  CD2 . PHE C  1 46  ? 5.452   184.363 17.457  1.00 31.30  ? 45  PHE C CD2 1 
ATOM   2582  C  CE1 . PHE C  1 46  ? 5.234   186.026 15.261  1.00 30.59  ? 45  PHE C CE1 1 
ATOM   2583  C  CE2 . PHE C  1 46  ? 4.334   185.192 17.328  1.00 32.16  ? 45  PHE C CE2 1 
ATOM   2584  C  CZ  . PHE C  1 46  ? 4.221   186.027 16.208  1.00 31.84  ? 45  PHE C CZ  1 
ATOM   2585  N  N   . HIS C  1 47  ? 9.885   185.795 18.000  1.00 33.97  ? 46  HIS C N   1 
ATOM   2586  C  CA  . HIS C  1 47  ? 10.404  186.367 19.224  1.00 33.68  ? 46  HIS C CA  1 
ATOM   2587  C  C   . HIS C  1 47  ? 10.099  187.810 19.382  1.00 34.86  ? 46  HIS C C   1 
ATOM   2588  O  O   . HIS C  1 47  ? 9.927   188.549 18.372  1.00 34.42  ? 46  HIS C O   1 
ATOM   2589  C  CB  . HIS C  1 47  ? 11.893  186.305 19.203  1.00 32.97  ? 46  HIS C CB  1 
ATOM   2590  C  CG  . HIS C  1 47  ? 12.415  184.955 18.870  1.00 42.65  ? 46  HIS C CG  1 
ATOM   2591  N  ND1 . HIS C  1 47  ? 13.241  184.732 17.794  1.00 46.55  ? 46  HIS C ND1 1 
ATOM   2592  C  CD2 . HIS C  1 47  ? 12.239  183.755 19.476  1.00 42.62  ? 46  HIS C CD2 1 
ATOM   2593  C  CE1 . HIS C  1 47  ? 13.563  183.451 17.758  1.00 49.12  ? 46  HIS C CE1 1 
ATOM   2594  N  NE2 . HIS C  1 47  ? 12.973  182.841 18.772  1.00 46.84  ? 46  HIS C NE2 1 
ATOM   2595  N  N   . VAL C  1 48  ? 10.053  188.214 20.659  1.00 35.06  ? 47  VAL C N   1 
ATOM   2596  C  CA  . VAL C  1 48  ? 9.993   189.616 21.045  1.00 30.29  ? 47  VAL C CA  1 
ATOM   2597  C  C   . VAL C  1 48  ? 11.418  190.016 21.266  1.00 31.14  ? 47  VAL C C   1 
ATOM   2598  O  O   . VAL C  1 48  ? 12.103  189.391 22.068  1.00 30.49  ? 47  VAL C O   1 
ATOM   2599  C  CB  . VAL C  1 48  ? 9.128   189.888 22.284  1.00 30.74  ? 47  VAL C CB  1 
ATOM   2600  C  CG1 . VAL C  1 48  ? 9.224   191.362 22.608  1.00 28.72  ? 47  VAL C CG1 1 
ATOM   2601  C  CG2 . VAL C  1 48  ? 7.654   189.493 22.074  1.00 26.54  ? 47  VAL C CG2 1 
ATOM   2602  N  N   . HIS C  1 49  ? 11.908  190.987 20.496  1.00 31.36  ? 48  HIS C N   1 
ATOM   2603  C  CA  . HIS C  1 49  ? 13.283  191.481 20.702  1.00 30.64  ? 48  HIS C CA  1 
ATOM   2604  C  C   . HIS C  1 49  ? 13.237  192.719 21.566  1.00 34.57  ? 48  HIS C C   1 
ATOM   2605  O  O   . HIS C  1 49  ? 12.151  193.338 21.715  1.00 33.86  ? 48  HIS C O   1 
ATOM   2606  C  CB  . HIS C  1 49  ? 14.008  191.749 19.387  1.00 30.39  ? 48  HIS C CB  1 
ATOM   2607  C  CG  . HIS C  1 49  ? 14.300  190.501 18.594  1.00 32.04  ? 48  HIS C CG  1 
ATOM   2608  N  ND1 . HIS C  1 49  ? 15.569  190.148 18.210  1.00 30.79  ? 48  HIS C ND1 1 
ATOM   2609  C  CD2 . HIS C  1 49  ? 13.495  189.496 18.169  1.00 31.52  ? 48  HIS C CD2 1 
ATOM   2610  C  CE1 . HIS C  1 49  ? 15.529  188.997 17.560  1.00 31.45  ? 48  HIS C CE1 1 
ATOM   2611  N  NE2 . HIS C  1 49  ? 14.290  188.567 17.540  1.00 28.88  ? 48  HIS C NE2 1 
ATOM   2612  N  N   . GLU C  1 50  ? 14.405  193.103 22.115  1.00 35.92  ? 49  GLU C N   1 
ATOM   2613  C  CA  . GLU C  1 50  ? 14.482  194.100 23.188  1.00 34.17  ? 49  GLU C CA  1 
ATOM   2614  C  C   . GLU C  1 50  ? 13.979  195.491 22.808  1.00 34.86  ? 49  GLU C C   1 
ATOM   2615  O  O   . GLU C  1 50  ? 13.203  196.049 23.545  1.00 32.99  ? 49  GLU C O   1 
ATOM   2616  C  CB  . GLU C  1 50  ? 15.889  194.205 23.769  1.00 32.89  ? 49  GLU C CB  1 
ATOM   2617  C  CG  . GLU C  1 50  ? 15.965  195.060 25.005  1.00 33.48  ? 49  GLU C CG  1 
ATOM   2618  C  CD  . GLU C  1 50  ? 17.329  195.045 25.712  1.00 45.10  ? 49  GLU C CD  1 
ATOM   2619  O  OE1 . GLU C  1 50  ? 18.262  194.295 25.324  1.00 46.46  ? 49  GLU C OE1 1 
ATOM   2620  O  OE2 . GLU C  1 50  ? 17.522  195.802 26.704  1.00 45.38  ? 49  GLU C OE2 1 
ATOM   2621  N  N   . PHE C  1 51  ? 14.425  196.014 21.671  1.00 29.84  ? 50  PHE C N   1 
ATOM   2622  C  CA  . PHE C  1 51  ? 14.158  197.376 21.320  1.00 30.35  ? 50  PHE C CA  1 
ATOM   2623  C  C   . PHE C  1 51  ? 13.095  197.577 20.254  1.00 32.64  ? 50  PHE C C   1 
ATOM   2624  O  O   . PHE C  1 51  ? 13.023  196.860 19.214  1.00 32.15  ? 50  PHE C O   1 
ATOM   2625  C  CB  . PHE C  1 51  ? 15.458  198.031 20.854  1.00 32.73  ? 50  PHE C CB  1 
ATOM   2626  C  CG  . PHE C  1 51  ? 16.581  197.854 21.826  1.00 32.94  ? 50  PHE C CG  1 
ATOM   2627  C  CD1 . PHE C  1 51  ? 16.487  198.382 23.112  1.00 35.15  ? 50  PHE C CD1 1 
ATOM   2628  C  CD2 . PHE C  1 51  ? 17.744  197.165 21.458  1.00 35.78  ? 50  PHE C CD2 1 
ATOM   2629  C  CE1 . PHE C  1 51  ? 17.521  198.203 24.054  1.00 36.53  ? 50  PHE C CE1 1 
ATOM   2630  C  CE2 . PHE C  1 51  ? 18.785  197.001 22.366  1.00 35.49  ? 50  PHE C CE2 1 
ATOM   2631  C  CZ  . PHE C  1 51  ? 18.658  197.496 23.681  1.00 36.23  ? 50  PHE C CZ  1 
ATOM   2632  N  N   . GLY C  1 52  ? 12.277  198.587 20.454  1.00 30.03  ? 51  GLY C N   1 
ATOM   2633  C  CA  . GLY C  1 52  ? 11.381  198.913 19.381  1.00 28.07  ? 51  GLY C CA  1 
ATOM   2634  C  C   . GLY C  1 52  ? 11.997  199.891 18.432  1.00 29.72  ? 51  GLY C C   1 
ATOM   2635  O  O   . GLY C  1 52  ? 11.399  200.855 18.168  1.00 31.79  ? 51  GLY C O   1 
ATOM   2636  N  N   . ASP C  1 53  ? 13.199  199.635 17.924  1.00 32.37  ? 52  ASP C N   1 
ATOM   2637  C  CA  . ASP C  1 53  ? 13.944  200.540 17.129  1.00 30.58  ? 52  ASP C CA  1 
ATOM   2638  C  C   . ASP C  1 53  ? 14.079  199.889 15.763  1.00 35.82  ? 52  ASP C C   1 
ATOM   2639  O  O   . ASP C  1 53  ? 14.745  198.868 15.602  1.00 38.14  ? 52  ASP C O   1 
ATOM   2640  C  CB  . ASP C  1 53  ? 15.288  200.758 17.788  1.00 29.26  ? 52  ASP C CB  1 
ATOM   2641  C  CG  . ASP C  1 53  ? 16.191  201.711 17.045  1.00 30.98  ? 52  ASP C CG  1 
ATOM   2642  O  OD1 . ASP C  1 53  ? 16.051  201.957 15.816  1.00 35.18  ? 52  ASP C OD1 1 
ATOM   2643  O  OD2 . ASP C  1 53  ? 17.133  202.186 17.694  1.00 31.07  ? 52  ASP C OD2 1 
ATOM   2644  N  N   . ASN C  1 54  ? 13.455  200.506 14.772  1.00 35.79  ? 53  ASN C N   1 
ATOM   2645  C  CA  . ASN C  1 54  ? 13.455  200.022 13.419  1.00 36.75  ? 53  ASN C CA  1 
ATOM   2646  C  C   . ASN C  1 54  ? 14.240  200.965 12.474  1.00 37.79  ? 53  ASN C C   1 
ATOM   2647  O  O   . ASN C  1 54  ? 14.040  200.885 11.259  1.00 36.26  ? 53  ASN C O   1 
ATOM   2648  C  CB  . ASN C  1 54  ? 12.012  199.847 12.980  1.00 39.82  ? 53  ASN C CB  1 
ATOM   2649  C  CG  . ASN C  1 54  ? 11.858  199.302 11.509  1.00 54.00  ? 53  ASN C CG  1 
ATOM   2650  O  OD1 . ASN C  1 54  ? 12.290  198.167 11.211  1.00 55.30  ? 53  ASN C OD1 1 
ATOM   2651  N  ND2 . ASN C  1 54  ? 11.232  200.121 10.578  1.00 43.90  ? 53  ASN C ND2 1 
ATOM   2652  N  N   . THR C  1 55  ? 15.135  201.818 13.020  1.00 33.92  ? 54  THR C N   1 
ATOM   2653  C  CA  . THR C  1 55  ? 15.846  202.809 12.234  1.00 30.25  ? 54  THR C CA  1 
ATOM   2654  C  C   . THR C  1 55  ? 16.823  202.172 11.309  1.00 33.56  ? 54  THR C C   1 
ATOM   2655  O  O   . THR C  1 55  ? 17.291  202.783 10.348  1.00 36.84  ? 54  THR C O   1 
ATOM   2656  C  CB  . THR C  1 55  ? 16.703  203.730 13.093  1.00 33.68  ? 54  THR C CB  1 
ATOM   2657  O  OG1 . THR C  1 55  ? 17.719  202.983 13.758  1.00 31.18  ? 54  THR C OG1 1 
ATOM   2658  C  CG2 . THR C  1 55  ? 15.894  204.446 14.132  1.00 35.39  ? 54  THR C CG2 1 
ATOM   2659  N  N   . ALA C  1 56  ? 17.164  200.926 11.569  1.00 35.18  ? 55  ALA C N   1 
ATOM   2660  C  CA  . ALA C  1 56  ? 18.067  200.202 10.660  1.00 34.99  ? 55  ALA C CA  1 
ATOM   2661  C  C   . ALA C  1 56  ? 17.406  198.916 10.279  1.00 34.71  ? 55  ALA C C   1 
ATOM   2662  O  O   . ALA C  1 56  ? 18.073  197.898 10.253  1.00 42.85  ? 55  ALA C O   1 
ATOM   2663  C  CB  . ALA C  1 56  ? 19.403  199.947 11.358  1.00 31.53  ? 55  ALA C CB  1 
ATOM   2664  N  N   . GLY C  1 57  ? 16.093  198.957 10.019  1.00 35.01  ? 56  GLY C N   1 
ATOM   2665  C  CA  . GLY C  1 57  ? 15.248  197.778 9.840   1.00 33.24  ? 56  GLY C CA  1 
ATOM   2666  C  C   . GLY C  1 57  ? 15.270  196.866 11.057  1.00 37.75  ? 56  GLY C C   1 
ATOM   2667  O  O   . GLY C  1 57  ? 15.512  197.336 12.174  1.00 46.12  ? 56  GLY C O   1 
ATOM   2668  N  N   . CYS C  1 58  ? 15.073  195.561 10.868  1.00 38.18  ? 57  CYS C N   1 
ATOM   2669  C  CA  . CYS C  1 58  ? 14.994  194.616 11.996  1.00 36.78  ? 57  CYS C CA  1 
ATOM   2670  C  C   . CYS C  1 58  ? 16.279  194.447 12.780  1.00 37.20  ? 57  CYS C C   1 
ATOM   2671  O  O   . CYS C  1 58  ? 16.212  193.987 13.897  1.00 40.19  ? 57  CYS C O   1 
ATOM   2672  C  CB  . CYS C  1 58  ? 14.489  193.248 11.565  1.00 35.94  ? 57  CYS C CB  1 
ATOM   2673  S  SG  . CYS C  1 58  ? 12.870  193.310 10.739  1.00 39.88  ? 57  CYS C SG  1 
ATOM   2674  N  N   . THR C  1 59  ? 17.429  194.810 12.213  1.00 33.83  ? 58  THR C N   1 
ATOM   2675  C  CA  . THR C  1 59  ? 18.714  194.628 12.895  1.00 37.01  ? 58  THR C CA  1 
ATOM   2676  C  C   . THR C  1 59  ? 18.790  195.429 14.190  1.00 40.38  ? 58  THR C C   1 
ATOM   2677  O  O   . THR C  1 59  ? 19.473  195.009 15.188  1.00 42.83  ? 58  THR C O   1 
ATOM   2678  C  CB  . THR C  1 59  ? 19.865  195.119 11.976  1.00 38.45  ? 58  THR C CB  1 
ATOM   2679  O  OG1 . THR C  1 59  ? 19.798  194.374 10.785  1.00 43.94  ? 58  THR C OG1 1 
ATOM   2680  C  CG2 . THR C  1 59  ? 21.272  194.950 12.573  1.00 32.25  ? 58  THR C CG2 1 
ATOM   2681  N  N   . SER C  1 60  ? 18.080  196.561 14.187  1.00 35.93  ? 59  SER C N   1 
ATOM   2682  C  CA  . SER C  1 60  ? 18.268  197.505 15.270  1.00 39.37  ? 59  SER C CA  1 
ATOM   2683  C  C   . SER C  1 60  ? 17.367  197.198 16.478  1.00 35.56  ? 59  SER C C   1 
ATOM   2684  O  O   . SER C  1 60  ? 17.430  197.906 17.459  1.00 33.72  ? 59  SER C O   1 
ATOM   2685  C  CB  . SER C  1 60  ? 18.256  199.008 14.806  1.00 34.98  ? 59  SER C CB  1 
ATOM   2686  O  OG  . SER C  1 60  ? 17.141  199.261 13.976  1.00 35.91  ? 59  SER C OG  1 
ATOM   2687  N  N   . ALA C  1 61  ? 16.574  196.126 16.375  1.00 33.92  ? 60  ALA C N   1 
ATOM   2688  C  CA  . ALA C  1 61  ? 15.760  195.612 17.489  1.00 33.85  ? 60  ALA C CA  1 
ATOM   2689  C  C   . ALA C  1 61  ? 16.584  194.950 18.587  1.00 33.24  ? 60  ALA C C   1 
ATOM   2690  O  O   . ALA C  1 61  ? 16.046  194.663 19.648  1.00 37.64  ? 60  ALA C O   1 
ATOM   2691  C  CB  . ALA C  1 61  ? 14.709  194.645 16.974  1.00 32.99  ? 60  ALA C CB  1 
ATOM   2692  N  N   . GLY C  1 62  ? 17.881  194.738 18.351  1.00 34.00  ? 61  GLY C N   1 
ATOM   2693  C  CA  . GLY C  1 62  ? 18.735  194.038 19.284  1.00 34.64  ? 61  GLY C CA  1 
ATOM   2694  C  C   . GLY C  1 62  ? 18.415  192.575 19.617  1.00 36.81  ? 61  GLY C C   1 
ATOM   2695  O  O   . GLY C  1 62  ? 17.812  191.820 18.795  1.00 32.56  ? 61  GLY C O   1 
ATOM   2696  N  N   . PRO C  1 63  ? 18.851  192.121 20.823  1.00 39.47  ? 62  PRO C N   1 
ATOM   2697  C  CA  . PRO C  1 63  ? 18.715  190.667 21.002  1.00 36.15  ? 62  PRO C CA  1 
ATOM   2698  C  C   . PRO C  1 63  ? 17.300  190.354 21.458  1.00 38.21  ? 62  PRO C C   1 
ATOM   2699  O  O   . PRO C  1 63  ? 16.460  191.277 21.514  1.00 37.17  ? 62  PRO C O   1 
ATOM   2700  C  CB  . PRO C  1 63  ? 19.706  190.376 22.070  1.00 33.39  ? 62  PRO C CB  1 
ATOM   2701  C  CG  . PRO C  1 63  ? 19.651  191.623 22.917  1.00 35.13  ? 62  PRO C CG  1 
ATOM   2702  C  CD  . PRO C  1 63  ? 19.668  192.722 21.906  1.00 37.18  ? 62  PRO C CD  1 
ATOM   2703  N  N   . HIS C  1 64  ? 17.020  189.071 21.720  1.00 38.27  ? 63  HIS C N   1 
ATOM   2704  C  CA  . HIS C  1 64  ? 15.750  188.643 22.354  1.00 40.58  ? 63  HIS C CA  1 
ATOM   2705  C  C   . HIS C  1 64  ? 15.528  189.376 23.675  1.00 38.72  ? 63  HIS C C   1 
ATOM   2706  O  O   . HIS C  1 64  ? 16.500  189.621 24.404  1.00 37.28  ? 63  HIS C O   1 
ATOM   2707  C  CB  . HIS C  1 64  ? 15.732  187.122 22.559  1.00 42.64  ? 63  HIS C CB  1 
ATOM   2708  C  CG  . HIS C  1 64  ? 15.787  186.327 21.279  1.00 40.83  ? 63  HIS C CG  1 
ATOM   2709  N  ND1 . HIS C  1 64  ? 15.501  184.989 21.221  1.00 46.06  ? 63  HIS C ND1 1 
ATOM   2710  C  CD2 . HIS C  1 64  ? 16.087  186.683 20.013  1.00 46.41  ? 63  HIS C CD2 1 
ATOM   2711  C  CE1 . HIS C  1 64  ? 15.572  184.557 19.974  1.00 48.56  ? 63  HIS C CE1 1 
ATOM   2712  N  NE2 . HIS C  1 64  ? 15.965  185.562 19.222  1.00 48.21  ? 63  HIS C NE2 1 
ATOM   2713  N  N   . PHE C  1 65  ? 14.265  189.785 23.913  1.00 37.02  ? 64  PHE C N   1 
ATOM   2714  C  CA  . PHE C  1 65  ? 13.862  190.419 25.146  1.00 32.98  ? 64  PHE C CA  1 
ATOM   2715  C  C   . PHE C  1 65  ? 14.033  189.449 26.284  1.00 35.93  ? 64  PHE C C   1 
ATOM   2716  O  O   . PHE C  1 65  ? 13.404  188.369 26.329  1.00 34.33  ? 64  PHE C O   1 
ATOM   2717  C  CB  . PHE C  1 65  ? 12.412  190.825 25.068  1.00 33.02  ? 64  PHE C CB  1 
ATOM   2718  C  CG  . PHE C  1 65  ? 11.919  191.581 26.294  1.00 32.42  ? 64  PHE C CG  1 
ATOM   2719  C  CD1 . PHE C  1 65  ? 12.764  192.507 26.969  1.00 33.07  ? 64  PHE C CD1 1 
ATOM   2720  C  CD2 . PHE C  1 65  ? 10.601  191.364 26.783  1.00 30.47  ? 64  PHE C CD2 1 
ATOM   2721  C  CE1 . PHE C  1 65  ? 12.300  193.170 28.119  1.00 31.37  ? 64  PHE C CE1 1 
ATOM   2722  C  CE2 . PHE C  1 65  ? 10.124  192.068 27.886  1.00 29.68  ? 64  PHE C CE2 1 
ATOM   2723  C  CZ  . PHE C  1 65  ? 10.991  192.945 28.565  1.00 29.19  ? 64  PHE C CZ  1 
ATOM   2724  N  N   . ASN C  1 66  ? 14.875  189.869 27.207  1.00 37.92  ? 65  ASN C N   1 
ATOM   2725  C  CA  . ASN C  1 66  ? 15.457  188.998 28.192  1.00 39.54  ? 65  ASN C CA  1 
ATOM   2726  C  C   . ASN C  1 66  ? 15.737  189.765 29.504  1.00 38.36  ? 65  ASN C C   1 
ATOM   2727  O  O   . ASN C  1 66  ? 16.874  189.755 30.019  1.00 38.55  ? 65  ASN C O   1 
ATOM   2728  C  CB  . ASN C  1 66  ? 16.775  188.396 27.606  1.00 42.66  ? 65  ASN C CB  1 
ATOM   2729  C  CG  . ASN C  1 66  ? 17.441  187.304 28.541  1.00 45.68  ? 65  ASN C CG  1 
ATOM   2730  O  OD1 . ASN C  1 66  ? 16.756  186.600 29.367  1.00 39.49  ? 65  ASN C OD1 1 
ATOM   2731  N  ND2 . ASN C  1 66  ? 18.774  187.148 28.376  1.00 38.48  ? 65  ASN C ND2 1 
ATOM   2732  N  N   . PRO C  1 67  ? 14.718  190.424 30.067  1.00 35.84  ? 66  PRO C N   1 
ATOM   2733  C  CA  . PRO C  1 67  ? 14.927  191.156 31.339  1.00 37.89  ? 66  PRO C CA  1 
ATOM   2734  C  C   . PRO C  1 67  ? 15.308  190.274 32.572  1.00 42.41  ? 66  PRO C C   1 
ATOM   2735  O  O   . PRO C  1 67  ? 15.887  190.788 33.516  1.00 43.72  ? 66  PRO C O   1 
ATOM   2736  C  CB  . PRO C  1 67  ? 13.591  191.811 31.588  1.00 34.32  ? 66  PRO C CB  1 
ATOM   2737  C  CG  . PRO C  1 67  ? 12.604  190.859 30.962  1.00 34.05  ? 66  PRO C CG  1 
ATOM   2738  C  CD  . PRO C  1 67  ? 13.303  190.184 29.798  1.00 34.41  ? 66  PRO C CD  1 
ATOM   2739  N  N   . LEU C  1 68  ? 15.026  188.973 32.581  1.00 45.39  ? 67  LEU C N   1 
ATOM   2740  C  CA  . LEU C  1 68  ? 15.587  188.150 33.675  1.00 48.45  ? 67  LEU C CA  1 
ATOM   2741  C  C   . LEU C  1 68  ? 16.950  187.479 33.415  1.00 49.75  ? 67  LEU C C   1 
ATOM   2742  O  O   . LEU C  1 68  ? 17.340  186.619 34.172  1.00 51.59  ? 67  LEU C O   1 
ATOM   2743  C  CB  . LEU C  1 68  ? 14.580  187.135 34.152  1.00 46.90  ? 67  LEU C CB  1 
ATOM   2744  C  CG  . LEU C  1 68  ? 13.434  187.522 35.077  1.00 52.62  ? 67  LEU C CG  1 
ATOM   2745  C  CD1 . LEU C  1 68  ? 12.838  188.952 35.079  1.00 58.69  ? 67  LEU C CD1 1 
ATOM   2746  C  CD2 . LEU C  1 68  ? 12.419  186.532 34.548  1.00 48.53  ? 67  LEU C CD2 1 
ATOM   2747  N  N   . SER C  1 69  ? 17.693  187.882 32.387  1.00 50.62  ? 68  SER C N   1 
ATOM   2748  C  CA  . SER C  1 69  ? 19.024  187.244 32.035  1.00 52.60  ? 68  SER C CA  1 
ATOM   2749  C  C   . SER C  1 69  ? 19.130  185.658 32.041  1.00 54.36  ? 68  SER C C   1 
ATOM   2750  O  O   . SER C  1 69  ? 20.203  185.106 32.400  1.00 53.62  ? 68  SER C O   1 
ATOM   2751  C  CB  . SER C  1 69  ? 20.205  187.893 32.792  1.00 48.29  ? 68  SER C CB  1 
ATOM   2752  O  OG  . SER C  1 69  ? 19.865  189.225 33.180  1.00 47.99  ? 68  SER C OG  1 
ATOM   2753  N  N   . ARG C  1 70  ? 18.044  184.974 31.614  1.00 43.06  ? 69  ARG C N   1 
ATOM   2754  C  CA  . ARG C  1 70  ? 18.038  183.566 31.199  1.00 43.67  ? 69  ARG C CA  1 
ATOM   2755  C  C   . ARG C  1 70  ? 18.759  183.214 29.853  1.00 51.44  ? 69  ARG C C   1 
ATOM   2756  O  O   . ARG C  1 70  ? 19.236  184.080 29.088  1.00 54.31  ? 69  ARG C O   1 
ATOM   2757  C  CB  . ARG C  1 70  ? 16.602  183.031 31.126  1.00 47.79  ? 69  ARG C CB  1 
ATOM   2758  C  CG  . ARG C  1 70  ? 15.737  183.435 32.295  1.00 52.14  ? 69  ARG C CG  1 
ATOM   2759  C  CD  . ARG C  1 70  ? 15.718  182.481 33.476  1.00 49.70  ? 69  ARG C CD  1 
ATOM   2760  N  NE  . ARG C  1 70  ? 14.799  183.123 34.410  1.00 59.92  ? 69  ARG C NE  1 
ATOM   2761  C  CZ  . ARG C  1 70  ? 13.554  182.709 34.738  1.00 70.08  ? 69  ARG C CZ  1 
ATOM   2762  N  NH1 . ARG C  1 70  ? 13.036  181.547 34.290  1.00 66.95  ? 69  ARG C NH1 1 
ATOM   2763  N  NH2 . ARG C  1 70  ? 12.810  183.458 35.559  1.00 60.13  ? 69  ARG C NH2 1 
ATOM   2764  N  N   . LYS C  1 71  ? 18.835  181.904 29.597  1.00 53.35  ? 70  LYS C N   1 
ATOM   2765  C  CA  . LYS C  1 71  ? 19.284  181.347 28.343  1.00 51.15  ? 70  LYS C CA  1 
ATOM   2766  C  C   . LYS C  1 71  ? 18.010  181.075 27.555  1.00 49.10  ? 70  LYS C C   1 
ATOM   2767  O  O   . LYS C  1 71  ? 16.876  180.880 28.140  1.00 47.01  ? 70  LYS C O   1 
ATOM   2768  C  CB  . LYS C  1 71  ? 20.024  179.981 28.571  1.00 55.75  ? 70  LYS C CB  1 
ATOM   2769  C  CG  . LYS C  1 71  ? 21.261  179.948 29.476  1.00 62.63  ? 70  LYS C CG  1 
ATOM   2770  C  CD  . LYS C  1 71  ? 22.389  180.891 29.040  1.00 65.14  ? 70  LYS C CD  1 
ATOM   2771  C  CE  . LYS C  1 71  ? 23.560  180.800 30.036  1.00 68.67  ? 70  LYS C CE  1 
ATOM   2772  N  NZ  . LYS C  1 71  ? 24.621  181.744 29.581  1.00 78.14  ? 70  LYS C NZ  1 
ATOM   2773  N  N   . HIS C  1 72  ? 18.200  181.025 26.232  1.00 42.95  ? 71  HIS C N   1 
ATOM   2774  C  CA  . HIS C  1 72  ? 17.102  180.918 25.306  1.00 40.68  ? 71  HIS C CA  1 
ATOM   2775  C  C   . HIS C  1 72  ? 16.479  179.533 25.500  1.00 43.18  ? 71  HIS C C   1 
ATOM   2776  O  O   . HIS C  1 72  ? 17.179  178.544 25.634  1.00 48.75  ? 71  HIS C O   1 
ATOM   2777  C  CB  . HIS C  1 72  ? 17.643  181.096 23.860  1.00 41.15  ? 71  HIS C CB  1 
ATOM   2778  C  CG  . HIS C  1 72  ? 16.629  180.768 22.815  1.00 41.47  ? 71  HIS C CG  1 
ATOM   2779  N  ND1 . HIS C  1 72  ? 15.664  181.655 22.400  1.00 42.72  ? 71  HIS C ND1 1 
ATOM   2780  C  CD2 . HIS C  1 72  ? 16.348  179.610 22.183  1.00 44.40  ? 71  HIS C CD2 1 
ATOM   2781  C  CE1 . HIS C  1 72  ? 14.831  181.069 21.567  1.00 41.99  ? 71  HIS C CE1 1 
ATOM   2782  N  NE2 . HIS C  1 72  ? 15.260  179.839 21.375  1.00 44.27  ? 71  HIS C NE2 1 
ATOM   2783  N  N   . GLY C  1 73  ? 15.161  179.448 25.483  1.00 43.89  ? 72  GLY C N   1 
ATOM   2784  C  CA  . GLY C  1 73  ? 14.485  178.171 25.237  1.00 39.92  ? 72  GLY C CA  1 
ATOM   2785  C  C   . GLY C  1 73  ? 13.164  178.314 24.486  1.00 41.31  ? 72  GLY C C   1 
ATOM   2786  O  O   . GLY C  1 73  ? 12.915  179.358 23.896  1.00 45.44  ? 72  GLY C O   1 
ATOM   2787  N  N   . GLY C  1 74  ? 12.316  177.278 24.510  1.00 40.61  ? 73  GLY C N   1 
ATOM   2788  C  CA  . GLY C  1 74  ? 10.939  177.269 23.913  1.00 37.94  ? 73  GLY C CA  1 
ATOM   2789  C  C   . GLY C  1 74  ? 9.995   178.022 24.822  1.00 38.87  ? 73  GLY C C   1 
ATOM   2790  O  O   . GLY C  1 74  ? 10.357  178.341 25.970  1.00 38.66  ? 73  GLY C O   1 
ATOM   2791  N  N   . PRO C  1 75  ? 8.781   178.356 24.341  1.00 40.86  ? 74  PRO C N   1 
ATOM   2792  C  CA  . PRO C  1 75  ? 7.849   179.126 25.250  1.00 40.39  ? 74  PRO C CA  1 
ATOM   2793  C  C   . PRO C  1 75  ? 7.372   178.366 26.531  1.00 45.38  ? 74  PRO C C   1 
ATOM   2794  O  O   . PRO C  1 75  ? 6.764   178.975 27.462  1.00 46.04  ? 74  PRO C O   1 
ATOM   2795  C  CB  . PRO C  1 75  ? 6.649   179.417 24.345  1.00 37.29  ? 74  PRO C CB  1 
ATOM   2796  C  CG  . PRO C  1 75  ? 6.727   178.384 23.260  1.00 37.03  ? 74  PRO C CG  1 
ATOM   2797  C  CD  . PRO C  1 75  ? 8.198   178.170 23.006  1.00 37.65  ? 74  PRO C CD  1 
ATOM   2798  N  N   . LYS C  1 76  ? 7.631   177.045 26.537  1.00 50.20  ? 75  LYS C N   1 
ATOM   2799  C  CA  . LYS C  1 76  ? 7.074   176.077 27.506  1.00 45.46  ? 75  LYS C CA  1 
ATOM   2800  C  C   . LYS C  1 76  ? 8.100   175.774 28.545  1.00 47.50  ? 75  LYS C C   1 
ATOM   2801  O  O   . LYS C  1 76  ? 7.729   175.415 29.662  1.00 50.20  ? 75  LYS C O   1 
ATOM   2802  C  CB  . LYS C  1 76  ? 6.510   174.835 26.793  1.00 49.09  ? 75  LYS C CB  1 
ATOM   2803  C  CG  . LYS C  1 76  ? 5.136   175.125 26.152  1.00 50.92  ? 75  LYS C CG  1 
ATOM   2804  C  CD  . LYS C  1 76  ? 4.493   176.303 26.977  1.00 55.99  ? 75  LYS C CD  1 
ATOM   2805  C  CE  . LYS C  1 76  ? 2.967   176.381 27.061  1.00 52.12  ? 75  LYS C CE  1 
ATOM   2806  N  NZ  . LYS C  1 76  ? 2.454   176.893 25.726  1.00 48.66  ? 75  LYS C NZ  1 
ATOM   2807  N  N   . ASP C  1 77  ? 9.373   176.033 28.207  1.00 41.56  ? 76  ASP C N   1 
ATOM   2808  C  CA  . ASP C  1 77  ? 10.438  175.911 29.160  1.00 43.42  ? 76  ASP C CA  1 
ATOM   2809  C  C   . ASP C  1 77  ? 10.443  176.973 30.240  1.00 55.17  ? 76  ASP C C   1 
ATOM   2810  O  O   . ASP C  1 77  ? 9.773   178.033 30.162  1.00 56.59  ? 76  ASP C O   1 
ATOM   2811  C  CB  . ASP C  1 77  ? 11.827  175.731 28.521  1.00 46.67  ? 76  ASP C CB  1 
ATOM   2812  C  CG  . ASP C  1 77  ? 11.798  174.744 27.313  1.00 52.16  ? 76  ASP C CG  1 
ATOM   2813  O  OD1 . ASP C  1 77  ? 10.994  173.751 27.252  1.00 50.35  ? 76  ASP C OD1 1 
ATOM   2814  O  OD2 . ASP C  1 77  ? 12.562  175.031 26.361  1.00 51.84  ? 76  ASP C OD2 1 
ATOM   2815  N  N   . GLU C  1 78  ? 11.173  176.652 31.293  1.00 54.27  ? 77  GLU C N   1 
ATOM   2816  C  CA  . GLU C  1 78  ? 11.225  177.512 32.429  1.00 57.66  ? 77  GLU C CA  1 
ATOM   2817  C  C   . GLU C  1 78  ? 12.371  178.433 32.138  1.00 57.05  ? 77  GLU C C   1 
ATOM   2818  O  O   . GLU C  1 78  ? 12.179  179.668 32.235  1.00 58.87  ? 77  GLU C O   1 
ATOM   2819  C  CB  . GLU C  1 78  ? 11.468  176.711 33.735  1.00 70.21  ? 77  GLU C CB  1 
ATOM   2820  C  CG  . GLU C  1 78  ? 10.858  177.294 35.003  1.00 69.57  ? 77  GLU C CG  1 
ATOM   2821  C  CD  . GLU C  1 78  ? 11.728  178.409 35.627  1.00 81.55  ? 77  GLU C CD  1 
ATOM   2822  O  OE1 . GLU C  1 78  ? 12.959  178.172 35.881  1.00 70.11  ? 77  GLU C OE1 1 
ATOM   2823  O  OE2 . GLU C  1 78  ? 11.178  179.541 35.856  1.00 70.01  ? 77  GLU C OE2 1 
ATOM   2824  N  N   . GLU C  1 79  ? 13.545  177.859 31.812  1.00 49.68  ? 78  GLU C N   1 
ATOM   2825  C  CA  . GLU C  1 79  ? 14.655  178.644 31.354  1.00 50.70  ? 78  GLU C CA  1 
ATOM   2826  C  C   . GLU C  1 79  ? 14.229  179.055 29.838  1.00 55.82  ? 78  GLU C C   1 
ATOM   2827  O  O   . GLU C  1 79  ? 14.281  178.257 28.872  1.00 58.81  ? 78  GLU C O   1 
ATOM   2828  C  CB  . GLU C  1 79  ? 15.945  177.836 31.565  1.00 48.66  ? 78  GLU C CB  1 
ATOM   2829  C  CG  . GLU C  1 79  ? 17.275  178.520 31.223  1.00 51.22  ? 78  GLU C CG  1 
ATOM   2830  C  CD  . GLU C  1 79  ? 17.698  179.421 32.362  1.00 61.46  ? 78  GLU C CD  1 
ATOM   2831  O  OE1 . GLU C  1 79  ? 16.895  179.381 33.366  1.00 57.52  ? 78  GLU C OE1 1 
ATOM   2832  O  OE2 . GLU C  1 79  ? 18.769  180.151 32.247  1.00 50.05  ? 78  GLU C OE2 1 
ATOM   2833  N  N   . ARG C  1 80  ? 13.719  180.287 29.701  1.00 49.82  ? 79  ARG C N   1 
ATOM   2834  C  CA  . ARG C  1 80  ? 13.402  180.943 28.423  1.00 48.02  ? 79  ARG C CA  1 
ATOM   2835  C  C   . ARG C  1 80  ? 13.642  182.405 28.664  1.00 48.36  ? 79  ARG C C   1 
ATOM   2836  O  O   . ARG C  1 80  ? 13.581  182.880 29.821  1.00 47.07  ? 79  ARG C O   1 
ATOM   2837  C  CB  . ARG C  1 80  ? 11.931  180.724 27.969  1.00 41.46  ? 79  ARG C CB  1 
ATOM   2838  C  CG  . ARG C  1 80  ? 10.870  181.048 29.006  1.00 41.14  ? 79  ARG C CG  1 
ATOM   2839  C  CD  . ARG C  1 80  ? 9.463   180.910 28.397  1.00 42.14  ? 79  ARG C CD  1 
ATOM   2840  N  NE  . ARG C  1 80  ? 9.158   182.174 27.771  1.00 39.97  ? 79  ARG C NE  1 
ATOM   2841  C  CZ  . ARG C  1 80  ? 7.995   182.594 27.283  1.00 39.66  ? 79  ARG C CZ  1 
ATOM   2842  N  NH1 . ARG C  1 80  ? 6.886   181.846 27.273  1.00 34.53  ? 79  ARG C NH1 1 
ATOM   2843  N  NH2 . ARG C  1 80  ? 7.960   183.834 26.797  1.00 38.49  ? 79  ARG C NH2 1 
ATOM   2844  N  N   . HIS C  1 81  ? 13.938  183.109 27.572  1.00 46.86  ? 80  HIS C N   1 
ATOM   2845  C  CA  . HIS C  1 81  ? 13.887  184.597 27.500  1.00 39.62  ? 80  HIS C CA  1 
ATOM   2846  C  C   . HIS C  1 81  ? 12.384  185.000 27.575  1.00 35.91  ? 80  HIS C C   1 
ATOM   2847  O  O   . HIS C  1 81  ? 11.523  184.255 27.048  1.00 36.12  ? 80  HIS C O   1 
ATOM   2848  C  CB  . HIS C  1 81  ? 14.531  185.078 26.192  1.00 39.73  ? 80  HIS C CB  1 
ATOM   2849  C  CG  . HIS C  1 81  ? 16.009  184.802 26.058  1.00 45.49  ? 80  HIS C CG  1 
ATOM   2850  N  ND1 . HIS C  1 81  ? 16.608  184.471 24.853  1.00 44.52  ? 80  HIS C ND1 1 
ATOM   2851  C  CD2 . HIS C  1 81  ? 17.024  184.880 26.949  1.00 51.13  ? 80  HIS C CD2 1 
ATOM   2852  C  CE1 . HIS C  1 81  ? 17.915  184.404 24.986  1.00 43.60  ? 80  HIS C CE1 1 
ATOM   2853  N  NE2 . HIS C  1 81  ? 18.196  184.633 26.258  1.00 54.80  ? 80  HIS C NE2 1 
ATOM   2854  N  N   . VAL C  1 82  ? 12.044  186.115 28.225  1.00 30.44  ? 81  VAL C N   1 
ATOM   2855  C  CA  . VAL C  1 82  ? 10.662  186.549 28.188  1.00 33.80  ? 81  VAL C CA  1 
ATOM   2856  C  C   . VAL C  1 82  ? 10.142  186.630 26.751  1.00 35.76  ? 81  VAL C C   1 
ATOM   2857  O  O   . VAL C  1 82  ? 8.970   186.345 26.487  1.00 33.69  ? 81  VAL C O   1 
ATOM   2858  C  CB  . VAL C  1 82  ? 10.422  187.914 28.909  1.00 36.07  ? 81  VAL C CB  1 
ATOM   2859  C  CG1 . VAL C  1 82  ? 9.020   188.431 28.627  1.00 28.04  ? 81  VAL C CG1 1 
ATOM   2860  C  CG2 . VAL C  1 82  ? 10.634  187.730 30.418  1.00 34.11  ? 81  VAL C CG2 1 
ATOM   2861  N  N   . GLY C  1 83  ? 11.005  187.002 25.806  1.00 33.37  ? 82  GLY C N   1 
ATOM   2862  C  CA  . GLY C  1 83  ? 10.531  187.033 24.390  1.00 37.50  ? 82  GLY C CA  1 
ATOM   2863  C  C   . GLY C  1 83  ? 10.411  185.753 23.531  1.00 39.54  ? 82  GLY C C   1 
ATOM   2864  O  O   . GLY C  1 83  ? 10.027  185.849 22.368  1.00 42.58  ? 82  GLY C O   1 
ATOM   2865  N  N   . ASP C  1 84  ? 10.726  184.568 24.082  1.00 37.69  ? 83  ASP C N   1 
ATOM   2866  C  CA  . ASP C  1 84  ? 10.715  183.310 23.365  1.00 32.38  ? 83  ASP C CA  1 
ATOM   2867  C  C   . ASP C  1 84  ? 9.338   182.780 23.106  1.00 34.52  ? 83  ASP C C   1 
ATOM   2868  O  O   . ASP C  1 84  ? 8.789   182.080 23.909  1.00 31.91  ? 83  ASP C O   1 
ATOM   2869  C  CB  . ASP C  1 84  ? 11.550  182.287 24.111  1.00 34.94  ? 83  ASP C CB  1 
ATOM   2870  C  CG  . ASP C  1 84  ? 13.012  182.694 24.175  1.00 39.89  ? 83  ASP C CG  1 
ATOM   2871  O  OD1 . ASP C  1 84  ? 13.337  183.512 23.299  1.00 40.08  ? 83  ASP C OD1 1 
ATOM   2872  O  OD2 . ASP C  1 84  ? 13.830  182.235 25.044  1.00 37.57  ? 83  ASP C OD2 1 
ATOM   2873  N  N   . LEU C  1 85  ? 8.780   183.077 21.944  1.00 37.73  ? 84  LEU C N   1 
ATOM   2874  C  CA  . LEU C  1 85  ? 7.446   182.601 21.676  1.00 37.54  ? 84  LEU C CA  1 
ATOM   2875  C  C   . LEU C  1 85  ? 7.480   181.384 20.767  1.00 38.09  ? 84  LEU C C   1 
ATOM   2876  O  O   . LEU C  1 85  ? 6.406   180.996 20.245  1.00 35.44  ? 84  LEU C O   1 
ATOM   2877  C  CB  . LEU C  1 85  ? 6.525   183.739 21.188  1.00 34.37  ? 84  LEU C CB  1 
ATOM   2878  C  CG  . LEU C  1 85  ? 6.426   184.954 22.095  1.00 38.12  ? 84  LEU C CG  1 
ATOM   2879  C  CD1 . LEU C  1 85  ? 5.439   185.940 21.525  1.00 35.18  ? 84  LEU C CD1 1 
ATOM   2880  C  CD2 . LEU C  1 85  ? 5.892   184.505 23.449  1.00 36.73  ? 84  LEU C CD2 1 
ATOM   2881  N  N   . GLY C  1 86  ? 8.675   180.768 20.596  1.00 37.22  ? 85  GLY C N   1 
ATOM   2882  C  CA  . GLY C  1 86  ? 8.777   179.499 19.795  1.00 38.64  ? 85  GLY C CA  1 
ATOM   2883  C  C   . GLY C  1 86  ? 8.610   179.566 18.265  1.00 42.57  ? 85  GLY C C   1 
ATOM   2884  O  O   . GLY C  1 86  ? 9.285   180.428 17.637  1.00 44.87  ? 85  GLY C O   1 
ATOM   2885  N  N   . ASN C  1 87  ? 7.802   178.682 17.626  1.00 34.49  ? 86  ASN C N   1 
ATOM   2886  C  CA  . ASN C  1 87  ? 7.779   178.723 16.175  1.00 33.25  ? 86  ASN C CA  1 
ATOM   2887  C  C   . ASN C  1 87  ? 6.364   178.851 15.725  1.00 35.54  ? 86  ASN C C   1 
ATOM   2888  O  O   . ASN C  1 87  ? 5.415   178.400 16.391  1.00 34.02  ? 86  ASN C O   1 
ATOM   2889  C  CB  . ASN C  1 87  ? 8.425   177.511 15.484  1.00 34.39  ? 86  ASN C CB  1 
ATOM   2890  C  CG  . ASN C  1 87  ? 9.880   177.288 15.862  1.00 40.96  ? 86  ASN C CG  1 
ATOM   2891  O  OD1 . ASN C  1 87  ? 10.827  177.893 15.297  1.00 38.26  ? 86  ASN C OD1 1 
ATOM   2892  N  ND2 . ASN C  1 87  ? 10.090  176.364 16.798  1.00 40.27  ? 86  ASN C ND2 1 
ATOM   2893  N  N   . VAL C  1 88  ? 6.237   179.489 14.576  1.00 31.82  ? 87  VAL C N   1 
ATOM   2894  C  CA  . VAL C  1 88  ? 4.999   179.525 13.868  1.00 33.93  ? 87  VAL C CA  1 
ATOM   2895  C  C   . VAL C  1 88  ? 5.256   178.705 12.603  1.00 34.23  ? 87  VAL C C   1 
ATOM   2896  O  O   . VAL C  1 88  ? 6.418   178.513 12.220  1.00 32.73  ? 87  VAL C O   1 
ATOM   2897  C  CB  . VAL C  1 88  ? 4.580   180.967 13.489  1.00 36.75  ? 87  VAL C CB  1 
ATOM   2898  C  CG1 . VAL C  1 88  ? 4.173   181.732 14.753  1.00 36.59  ? 87  VAL C CG1 1 
ATOM   2899  C  CG2 . VAL C  1 88  ? 5.699   181.682 12.661  1.00 37.93  ? 87  VAL C CG2 1 
ATOM   2900  N  N   . THR C  1 89  ? 4.177   178.271 11.971  1.00 32.79  ? 88  THR C N   1 
ATOM   2901  C  CA  . THR C  1 89  ? 4.211   177.245 10.967  1.00 37.16  ? 88  THR C CA  1 
ATOM   2902  C  C   . THR C  1 89  ? 3.574   177.808 9.749   1.00 34.93  ? 88  THR C C   1 
ATOM   2903  O  O   . THR C  1 89  ? 2.409   178.139 9.755   1.00 34.17  ? 88  THR C O   1 
ATOM   2904  C  CB  . THR C  1 89  ? 3.378   175.998 11.426  1.00 42.18  ? 88  THR C CB  1 
ATOM   2905  O  OG1 . THR C  1 89  ? 3.999   175.473 12.588  1.00 42.13  ? 88  THR C OG1 1 
ATOM   2906  C  CG2 . THR C  1 89  ? 3.301   174.876 10.346  1.00 43.29  ? 88  THR C CG2 1 
ATOM   2907  N  N   . ALA C  1 90  ? 4.355   177.877 8.689   1.00 35.62  ? 89  ALA C N   1 
ATOM   2908  C  CA  . ALA C  1 90  ? 3.811   178.234 7.406   1.00 36.69  ? 89  ALA C CA  1 
ATOM   2909  C  C   . ALA C  1 90  ? 3.440   176.988 6.629   1.00 37.77  ? 89  ALA C C   1 
ATOM   2910  O  O   . ALA C  1 90  ? 4.233   176.029 6.506   1.00 36.67  ? 89  ALA C O   1 
ATOM   2911  C  CB  . ALA C  1 90  ? 4.799   179.083 6.620   1.00 37.76  ? 89  ALA C CB  1 
ATOM   2912  N  N   . ASP C  1 91  ? 2.227   177.044 6.120   1.00 37.27  ? 90  ASP C N   1 
ATOM   2913  C  CA  . ASP C  1 91  ? 1.652   176.024 5.314   1.00 40.51  ? 90  ASP C CA  1 
ATOM   2914  C  C   . ASP C  1 91  ? 2.223   176.038 3.852   1.00 42.88  ? 90  ASP C C   1 
ATOM   2915  O  O   . ASP C  1 91  ? 3.137   176.818 3.508   1.00 44.91  ? 90  ASP C O   1 
ATOM   2916  C  CB  . ASP C  1 91  ? 0.120   176.191 5.361   1.00 33.33  ? 90  ASP C CB  1 
ATOM   2917  C  CG  . ASP C  1 91  ? -0.353  177.276 4.485   1.00 38.94  ? 90  ASP C CG  1 
ATOM   2918  O  OD1 . ASP C  1 91  ? 0.375   177.815 3.627   1.00 43.21  ? 90  ASP C OD1 1 
ATOM   2919  O  OD2 . ASP C  1 91  ? -1.503  177.655 4.595   1.00 46.37  ? 90  ASP C OD2 1 
ATOM   2920  N  N   . LYS C  1 92  ? 1.654   175.188 2.987   1.00 50.78  ? 91  LYS C N   1 
ATOM   2921  C  CA  . LYS C  1 92  ? 2.208   174.990 1.613   1.00 50.89  ? 91  LYS C CA  1 
ATOM   2922  C  C   . LYS C  1 92  ? 2.048   176.308 0.815   1.00 44.92  ? 91  LYS C C   1 
ATOM   2923  O  O   . LYS C  1 92  ? 2.876   176.578 -0.026  1.00 42.24  ? 91  LYS C O   1 
ATOM   2924  C  CB  . LYS C  1 92  ? 1.660   173.702 0.903   1.00 50.36  ? 91  LYS C CB  1 
ATOM   2925  C  CG  . LYS C  1 92  ? 0.687   173.928 -0.294  1.00 59.17  ? 91  LYS C CG  1 
ATOM   2926  C  CD  . LYS C  1 92  ? -0.837  173.770 -0.009  1.00 64.23  ? 91  LYS C CD  1 
ATOM   2927  C  CE  . LYS C  1 92  ? -1.616  173.328 -1.291  1.00 71.20  ? 91  LYS C CE  1 
ATOM   2928  N  NZ  . LYS C  1 92  ? -2.070  174.432 -2.227  1.00 61.16  ? 91  LYS C NZ  1 
ATOM   2929  N  N   . ASP C  1 93  ? 1.027   177.130 1.126   1.00 44.02  ? 92  ASP C N   1 
ATOM   2930  C  CA  . ASP C  1 93  ? 0.892   178.509 0.575   1.00 42.16  ? 92  ASP C CA  1 
ATOM   2931  C  C   . ASP C  1 93  ? 1.719   179.676 1.247   1.00 41.30  ? 92  ASP C C   1 
ATOM   2932  O  O   . ASP C  1 93  ? 1.464   180.858 0.928   1.00 36.59  ? 92  ASP C O   1 
ATOM   2933  C  CB  . ASP C  1 93  ? -0.570  178.897 0.598   1.00 45.64  ? 92  ASP C CB  1 
ATOM   2934  C  CG  . ASP C  1 93  ? -1.465  177.865 -0.098  1.00 56.55  ? 92  ASP C CG  1 
ATOM   2935  O  OD1 . ASP C  1 93  ? -1.206  177.510 -1.284  1.00 50.67  ? 92  ASP C OD1 1 
ATOM   2936  O  OD2 . ASP C  1 93  ? -2.440  177.415 0.563   1.00 60.24  ? 92  ASP C OD2 1 
ATOM   2937  N  N   . GLY C  1 94  ? 2.668   179.365 2.157   1.00 33.57  ? 93  GLY C N   1 
ATOM   2938  C  CA  . GLY C  1 94  ? 3.404   180.411 2.867   1.00 37.10  ? 93  GLY C CA  1 
ATOM   2939  C  C   . GLY C  1 94  ? 2.686   181.236 3.967   1.00 42.81  ? 93  GLY C C   1 
ATOM   2940  O  O   . GLY C  1 94  ? 3.157   182.297 4.308   1.00 41.36  ? 93  GLY C O   1 
ATOM   2941  N  N   . VAL C  1 95  ? 1.568   180.739 4.504   1.00 36.26  ? 94  VAL C N   1 
ATOM   2942  C  CA  . VAL C  1 95  ? 0.773   181.401 5.466   1.00 37.42  ? 94  VAL C CA  1 
ATOM   2943  C  C   . VAL C  1 95  ? 0.915   180.674 6.816   1.00 39.86  ? 94  VAL C C   1 
ATOM   2944  O  O   . VAL C  1 95  ? 0.917   179.474 6.890   1.00 41.74  ? 94  VAL C O   1 
ATOM   2945  C  CB  . VAL C  1 95  ? -0.696  181.464 4.994   1.00 36.95  ? 94  VAL C CB  1 
ATOM   2946  C  CG1 . VAL C  1 95  ? -1.575  182.156 6.005   1.00 32.90  ? 94  VAL C CG1 1 
ATOM   2947  C  CG2 . VAL C  1 95  ? -0.787  182.214 3.689   1.00 37.26  ? 94  VAL C CG2 1 
ATOM   2948  N  N   . ALA C  1 96  ? 1.099   181.437 7.873   1.00 40.91  ? 95  ALA C N   1 
ATOM   2949  C  CA  . ALA C  1 96  ? 1.213   180.941 9.218   1.00 41.40  ? 95  ALA C CA  1 
ATOM   2950  C  C   . ALA C  1 96  ? 0.050   181.552 9.972   1.00 37.34  ? 95  ALA C C   1 
ATOM   2951  O  O   . ALA C  1 96  ? -0.055  182.752 10.005  1.00 37.06  ? 95  ALA C O   1 
ATOM   2952  C  CB  . ALA C  1 96  ? 2.547   181.375 9.813   1.00 37.85  ? 95  ALA C CB  1 
ATOM   2953  N  N   . ASP C  1 97  ? -0.861  180.729 10.480  1.00 38.33  ? 96  ASP C N   1 
ATOM   2954  C  CA  . ASP C  1 97  ? -1.903  181.177 11.385  1.00 39.03  ? 96  ASP C CA  1 
ATOM   2955  C  C   . ASP C  1 97  ? -1.378  181.034 12.795  1.00 42.85  ? 96  ASP C C   1 
ATOM   2956  O  O   . ASP C  1 97  ? -0.936  179.973 13.191  1.00 42.36  ? 96  ASP C O   1 
ATOM   2957  C  CB  . ASP C  1 97  ? -3.153  180.356 11.219  1.00 43.41  ? 96  ASP C CB  1 
ATOM   2958  C  CG  . ASP C  1 97  ? -3.828  180.649 9.897   1.00 58.74  ? 96  ASP C CG  1 
ATOM   2959  O  OD1 . ASP C  1 97  ? -3.787  181.842 9.414   1.00 53.99  ? 96  ASP C OD1 1 
ATOM   2960  O  OD2 . ASP C  1 97  ? -4.394  179.688 9.302   1.00 58.22  ? 96  ASP C OD2 1 
ATOM   2961  N  N   . VAL C  1 98  ? -1.410  182.116 13.555  1.00 41.05  ? 97  VAL C N   1 
ATOM   2962  C  CA  . VAL C  1 98  ? -0.763  182.153 14.865  1.00 39.19  ? 97  VAL C CA  1 
ATOM   2963  C  C   . VAL C  1 98  ? -1.865  182.071 15.917  1.00 40.22  ? 97  VAL C C   1 
ATOM   2964  O  O   . VAL C  1 98  ? -2.904  182.777 15.829  1.00 39.98  ? 97  VAL C O   1 
ATOM   2965  C  CB  . VAL C  1 98  ? 0.074   183.441 14.969  1.00 38.97  ? 97  VAL C CB  1 
ATOM   2966  C  CG1 . VAL C  1 98  ? 0.784   183.576 16.290  1.00 35.94  ? 97  VAL C CG1 1 
ATOM   2967  C  CG2 . VAL C  1 98  ? 1.098   183.479 13.828  1.00 34.28  ? 97  VAL C CG2 1 
ATOM   2968  N  N   . SER C  1 99  ? -1.693  181.140 16.847  1.00 36.68  ? 98  SER C N   1 
ATOM   2969  C  CA  . SER C  1 99  ? -2.555  181.088 18.029  1.00 41.45  ? 98  SER C CA  1 
ATOM   2970  C  C   . SER C  1 99  ? -1.692  180.698 19.210  1.00 42.24  ? 98  SER C C   1 
ATOM   2971  O  O   . SER C  1 99  ? -1.221  179.602 19.279  1.00 51.95  ? 98  SER C O   1 
ATOM   2972  C  CB  . SER C  1 99  ? -3.646  180.082 17.806  1.00 42.75  ? 98  SER C CB  1 
ATOM   2973  O  OG  . SER C  1 99  ? -4.826  180.579 18.372  1.00 50.83  ? 98  SER C OG  1 
ATOM   2974  N  N   . ILE C  1 100 ? -1.366  181.607 20.099  1.00 40.09  ? 99  ILE C N   1 
ATOM   2975  C  CA  . ILE C  1 100 ? -0.445  181.257 21.175  1.00 37.64  ? 99  ILE C CA  1 
ATOM   2976  C  C   . ILE C  1 100 ? -1.156  181.748 22.424  1.00 41.00  ? 99  ILE C C   1 
ATOM   2977  O  O   . ILE C  1 100 ? -1.989  182.654 22.341  1.00 41.14  ? 99  ILE C O   1 
ATOM   2978  C  CB  . ILE C  1 100 ? 0.895   181.976 20.982  1.00 37.54  ? 99  ILE C CB  1 
ATOM   2979  C  CG1 . ILE C  1 100 ? 1.593   181.418 19.785  1.00 38.82  ? 99  ILE C CG1 1 
ATOM   2980  C  CG2 . ILE C  1 100 ? 1.859   181.801 22.126  1.00 33.05  ? 99  ILE C CG2 1 
ATOM   2981  C  CD1 . ILE C  1 100 ? 2.914   182.147 19.561  1.00 39.36  ? 99  ILE C CD1 1 
ATOM   2982  N  N   . GLU C  1 101 ? -0.903  181.091 23.555  1.00 40.03  ? 100 GLU C N   1 
ATOM   2983  C  CA  . GLU C  1 101 ? -1.267  181.626 24.831  1.00 35.21  ? 100 GLU C CA  1 
ATOM   2984  C  C   . GLU C  1 101 ? 0.002   181.620 25.560  1.00 36.90  ? 100 GLU C C   1 
ATOM   2985  O  O   . GLU C  1 101 ? 0.737   180.694 25.486  1.00 41.24  ? 100 GLU C O   1 
ATOM   2986  C  CB  . GLU C  1 101 ? -2.231  180.762 25.489  1.00 38.71  ? 100 GLU C CB  1 
ATOM   2987  C  CG  . GLU C  1 101 ? -3.460  181.547 25.881  1.00 51.05  ? 100 GLU C CG  1 
ATOM   2988  C  CD  . GLU C  1 101 ? -3.986  181.243 27.316  1.00 60.12  ? 100 GLU C CD  1 
ATOM   2989  O  OE1 . GLU C  1 101 ? -3.275  180.569 28.168  1.00 47.36  ? 100 GLU C OE1 1 
ATOM   2990  O  OE2 . GLU C  1 101 ? -5.154  181.709 27.576  1.00 58.91  ? 100 GLU C OE2 1 
ATOM   2991  N  N   . ASP C  1 102 ? 0.365   182.721 26.160  1.00 38.10  ? 101 ASP C N   1 
ATOM   2992  C  CA  . ASP C  1 102 ? 1.619   182.768 26.820  1.00 35.57  ? 101 ASP C CA  1 
ATOM   2993  C  C   . ASP C  1 102 ? 1.393   183.466 28.185  1.00 38.61  ? 101 ASP C C   1 
ATOM   2994  O  O   . ASP C  1 102 ? 0.538   184.365 28.314  1.00 38.65  ? 101 ASP C O   1 
ATOM   2995  C  CB  . ASP C  1 102 ? 2.636   183.514 25.982  1.00 30.52  ? 101 ASP C CB  1 
ATOM   2996  C  CG  . ASP C  1 102 ? 4.014   183.338 26.523  1.00 33.26  ? 101 ASP C CG  1 
ATOM   2997  O  OD1 . ASP C  1 102 ? 4.505   182.191 26.564  1.00 40.69  ? 101 ASP C OD1 1 
ATOM   2998  O  OD2 . ASP C  1 102 ? 4.659   184.290 26.935  1.00 33.35  ? 101 ASP C OD2 1 
ATOM   2999  N  N   . SER C  1 103 ? 2.171   183.045 29.167  1.00 38.25  ? 102 SER C N   1 
ATOM   3000  C  CA  . SER C  1 103 ? 2.059   183.476 30.569  1.00 38.78  ? 102 SER C CA  1 
ATOM   3001  C  C   . SER C  1 103 ? 3.289   184.166 31.037  1.00 37.61  ? 102 SER C C   1 
ATOM   3002  O  O   . SER C  1 103 ? 3.292   184.604 32.137  1.00 40.93  ? 102 SER C O   1 
ATOM   3003  C  CB  . SER C  1 103 ? 1.898   182.278 31.501  1.00 36.15  ? 102 SER C CB  1 
ATOM   3004  O  OG  . SER C  1 103 ? 0.532   181.940 31.515  1.00 46.49  ? 102 SER C OG  1 
ATOM   3005  N  N   . VAL C  1 104 ? 4.363   184.207 30.255  1.00 39.78  ? 103 VAL C N   1 
ATOM   3006  C  CA  . VAL C  1 104 ? 5.565   184.914 30.698  1.00 38.86  ? 103 VAL C CA  1 
ATOM   3007  C  C   . VAL C  1 104 ? 5.520   186.378 30.241  1.00 41.78  ? 103 VAL C C   1 
ATOM   3008  O  O   . VAL C  1 104 ? 5.850   187.286 31.027  1.00 40.37  ? 103 VAL C O   1 
ATOM   3009  C  CB  . VAL C  1 104 ? 6.859   184.191 30.245  1.00 39.41  ? 103 VAL C CB  1 
ATOM   3010  C  CG1 . VAL C  1 104 ? 8.105   184.989 30.510  1.00 34.60  ? 103 VAL C CG1 1 
ATOM   3011  C  CG2 . VAL C  1 104 ? 6.998   182.859 30.941  1.00 32.90  ? 103 VAL C CG2 1 
ATOM   3012  N  N   . ILE C  1 105 ? 5.112   186.597 28.986  1.00 38.84  ? 104 ILE C N   1 
ATOM   3013  C  CA  . ILE C  1 105 ? 5.030   187.948 28.397  1.00 38.21  ? 104 ILE C CA  1 
ATOM   3014  C  C   . ILE C  1 105 ? 3.845   188.630 29.037  1.00 37.21  ? 104 ILE C C   1 
ATOM   3015  O  O   . ILE C  1 105 ? 2.887   187.973 29.382  1.00 35.98  ? 104 ILE C O   1 
ATOM   3016  C  CB  . ILE C  1 105 ? 4.828   187.973 26.819  1.00 35.12  ? 104 ILE C CB  1 
ATOM   3017  C  CG1 . ILE C  1 105 ? 3.519   187.247 26.407  1.00 34.84  ? 104 ILE C CG1 1 
ATOM   3018  C  CG2 . ILE C  1 105 ? 6.054   187.462 26.100  1.00 31.62  ? 104 ILE C CG2 1 
ATOM   3019  C  CD1 . ILE C  1 105 ? 2.964   187.443 25.036  1.00 29.97  ? 104 ILE C CD1 1 
ATOM   3020  N  N   . SER C  1 106 ? 3.908   189.965 29.110  1.00 37.68  ? 105 SER C N   1 
ATOM   3021  C  CA  . SER C  1 106 ? 2.794   190.803 29.598  1.00 35.45  ? 105 SER C CA  1 
ATOM   3022  C  C   . SER C  1 106 ? 2.591   192.117 28.813  1.00 33.34  ? 105 SER C C   1 
ATOM   3023  O  O   . SER C  1 106 ? 3.529   192.613 28.213  1.00 32.16  ? 105 SER C O   1 
ATOM   3024  C  CB  . SER C  1 106 ? 2.982   191.162 31.089  1.00 29.42  ? 105 SER C CB  1 
ATOM   3025  O  OG  . SER C  1 106 ? 1.685   191.454 31.549  1.00 32.69  ? 105 SER C OG  1 
ATOM   3026  N  N   . LEU C  1 107 ? 1.379   192.679 28.885  1.00 31.60  ? 106 LEU C N   1 
ATOM   3027  C  CA  . LEU C  1 107 ? 1.142   194.003 28.364  1.00 31.11  ? 106 LEU C CA  1 
ATOM   3028  C  C   . LEU C  1 107 ? 1.259   195.128 29.410  1.00 32.85  ? 106 LEU C C   1 
ATOM   3029  O  O   . LEU C  1 107 ? 0.956   196.202 29.053  1.00 38.80  ? 106 LEU C O   1 
ATOM   3030  C  CB  . LEU C  1 107 ? -0.156  194.085 27.532  1.00 29.35  ? 106 LEU C CB  1 
ATOM   3031  C  CG  . LEU C  1 107 ? -0.485  192.978 26.463  1.00 29.95  ? 106 LEU C CG  1 
ATOM   3032  C  CD1 . LEU C  1 107 ? -1.787  193.183 25.684  1.00 27.01  ? 106 LEU C CD1 1 
ATOM   3033  C  CD2 . LEU C  1 107 ? 0.635   192.554 25.513  1.00 26.65  ? 106 LEU C CD2 1 
ATOM   3034  N  N   . SER C  1 108 ? 1.791   194.891 30.626  1.00 33.17  ? 107 SER C N   1 
ATOM   3035  C  CA  . SER C  1 108 ? 1.928   195.852 31.755  1.00 33.83  ? 107 SER C CA  1 
ATOM   3036  C  C   . SER C  1 108 ? 3.046   195.350 32.574  1.00 38.05  ? 107 SER C C   1 
ATOM   3037  O  O   . SER C  1 108 ? 3.339   194.179 32.475  1.00 41.96  ? 107 SER C O   1 
ATOM   3038  C  CB  . SER C  1 108 ? 0.798   195.704 32.730  1.00 38.47  ? 107 SER C CB  1 
ATOM   3039  O  OG  . SER C  1 108 ? -0.318  195.106 32.134  1.00 40.70  ? 107 SER C OG  1 
ATOM   3040  N  N   . GLY C  1 109 ? 3.675   196.207 33.393  1.00 41.57  ? 108 GLY C N   1 
ATOM   3041  C  CA  . GLY C  1 109 ? 4.845   195.861 34.267  1.00 42.34  ? 108 GLY C CA  1 
ATOM   3042  C  C   . GLY C  1 109 ? 6.235   195.664 33.678  1.00 51.22  ? 108 GLY C C   1 
ATOM   3043  O  O   . GLY C  1 109 ? 6.569   196.240 32.698  1.00 58.93  ? 108 GLY C O   1 
ATOM   3044  N  N   . ASP C  1 110 ? 7.052   194.814 34.285  1.00 52.85  ? 109 ASP C N   1 
ATOM   3045  C  CA  . ASP C  1 110 ? 8.462   194.602 33.893  1.00 56.87  ? 109 ASP C CA  1 
ATOM   3046  C  C   . ASP C  1 110 ? 8.624   193.770 32.643  1.00 53.28  ? 109 ASP C C   1 
ATOM   3047  O  O   . ASP C  1 110 ? 9.588   193.901 31.930  1.00 56.85  ? 109 ASP C O   1 
ATOM   3048  C  CB  . ASP C  1 110 ? 9.313   193.944 35.086  1.00 66.36  ? 109 ASP C CB  1 
ATOM   3049  C  CG  . ASP C  1 110 ? 10.680  193.189 34.585  1.00 66.34  ? 109 ASP C CG  1 
ATOM   3050  O  OD1 . ASP C  1 110 ? 11.466  193.736 33.730  1.00 56.51  ? 109 ASP C OD1 1 
ATOM   3051  O  OD2 . ASP C  1 110 ? 10.987  192.051 35.060  1.00 62.50  ? 109 ASP C OD2 1 
ATOM   3052  N  N   . HIS C  1 111 ? 7.721   192.855 32.409  1.00 56.25  ? 110 HIS C N   1 
ATOM   3053  C  CA  . HIS C  1 111 ? 7.796   191.981 31.218  1.00 60.49  ? 110 HIS C CA  1 
ATOM   3054  C  C   . HIS C  1 111 ? 6.950   192.627 30.162  1.00 55.44  ? 110 HIS C C   1 
ATOM   3055  O  O   . HIS C  1 111 ? 6.409   191.858 29.280  1.00 54.83  ? 110 HIS C O   1 
ATOM   3056  C  CB  . HIS C  1 111 ? 7.236   190.502 31.473  1.00 55.21  ? 110 HIS C CB  1 
ATOM   3057  C  CG  . HIS C  1 111 ? 8.102   189.661 32.357  1.00 55.79  ? 110 HIS C CG  1 
ATOM   3058  N  ND1 . HIS C  1 111 ? 7.802   188.345 32.668  1.00 67.89  ? 110 HIS C ND1 1 
ATOM   3059  C  CD2 . HIS C  1 111 ? 9.258   189.950 33.018  1.00 53.59  ? 110 HIS C CD2 1 
ATOM   3060  C  CE1 . HIS C  1 111 ? 8.720   187.866 33.503  1.00 62.64  ? 110 HIS C CE1 1 
ATOM   3061  N  NE2 . HIS C  1 111 ? 9.623   188.820 33.720  1.00 58.69  ? 110 HIS C NE2 1 
ATOM   3062  N  N   . CYS C  1 112 ? 6.740   193.957 30.297  1.00 42.33  ? 111 CYS C N   1 
ATOM   3063  C  CA  . CYS C  1 112 ? 5.823   194.616 29.385  1.00 41.05  ? 111 CYS C CA  1 
ATOM   3064  C  C   . CYS C  1 112 ? 6.389   194.569 27.933  1.00 34.59  ? 111 CYS C C   1 
ATOM   3065  O  O   . CYS C  1 112 ? 7.544   194.878 27.733  1.00 31.48  ? 111 CYS C O   1 
ATOM   3066  C  CB  . CYS C  1 112 ? 5.610   196.016 29.841  1.00 40.61  ? 111 CYS C CB  1 
ATOM   3067  S  SG  . CYS C  1 112 ? 4.600   196.924 28.655  1.00 41.85  ? 111 CYS C SG  1 
ATOM   3068  N  N   . ILE C  1 113 ? 5.618   194.086 26.965  1.00 32.16  ? 112 ILE C N   1 
ATOM   3069  C  CA  . ILE C  1 113 ? 6.181   194.019 25.610  1.00 36.02  ? 112 ILE C CA  1 
ATOM   3070  C  C   . ILE C  1 113 ? 5.880   195.208 24.698  1.00 33.22  ? 112 ILE C C   1 
ATOM   3071  O  O   . ILE C  1 113 ? 6.473   195.317 23.612  1.00 33.34  ? 112 ILE C O   1 
ATOM   3072  C  CB  . ILE C  1 113 ? 6.024   192.650 24.901  1.00 34.34  ? 112 ILE C CB  1 
ATOM   3073  C  CG1 . ILE C  1 113 ? 4.531   192.303 24.680  1.00 29.66  ? 112 ILE C CG1 1 
ATOM   3074  C  CG2 . ILE C  1 113 ? 6.906   191.652 25.669  1.00 33.49  ? 112 ILE C CG2 1 
ATOM   3075  C  CD1 . ILE C  1 113 ? 4.306   191.082 23.838  1.00 28.17  ? 112 ILE C CD1 1 
ATOM   3076  N  N   . ILE C  1 114 ? 4.971   196.072 25.166  1.00 33.99  ? 113 ILE C N   1 
ATOM   3077  C  CA  . ILE C  1 114 ? 4.606   197.295 24.473  1.00 33.58  ? 113 ILE C CA  1 
ATOM   3078  C  C   . ILE C  1 114 ? 5.862   198.105 24.203  1.00 32.27  ? 113 ILE C C   1 
ATOM   3079  O  O   . ILE C  1 114 ? 6.765   198.198 25.016  1.00 33.37  ? 113 ILE C O   1 
ATOM   3080  C  CB  . ILE C  1 114 ? 3.611   198.093 25.267  1.00 35.89  ? 113 ILE C CB  1 
ATOM   3081  C  CG1 . ILE C  1 114 ? 2.499   197.153 25.731  1.00 36.63  ? 113 ILE C CG1 1 
ATOM   3082  C  CG2 . ILE C  1 114 ? 3.150   199.375 24.519  1.00 33.84  ? 113 ILE C CG2 1 
ATOM   3083  C  CD1 . ILE C  1 114 ? 1.271   197.107 24.881  1.00 38.97  ? 113 ILE C CD1 1 
ATOM   3084  N  N   . GLY C  1 115 ? 5.963   198.516 22.956  1.00 28.94  ? 114 GLY C N   1 
ATOM   3085  C  CA  . GLY C  1 115 ? 7.090   199.220 22.460  1.00 27.75  ? 114 GLY C CA  1 
ATOM   3086  C  C   . GLY C  1 115 ? 8.348   198.464 22.166  1.00 31.00  ? 114 GLY C C   1 
ATOM   3087  O  O   . GLY C  1 115 ? 9.435   199.101 21.948  1.00 32.96  ? 114 GLY C O   1 
ATOM   3088  N  N   . ARG C  1 116 ? 8.255   197.134 22.140  1.00 32.55  ? 115 ARG C N   1 
ATOM   3089  C  CA  . ARG C  1 116 ? 9.406   196.359 21.703  1.00 32.42  ? 115 ARG C CA  1 
ATOM   3090  C  C   . ARG C  1 116 ? 9.038   195.850 20.335  1.00 30.74  ? 115 ARG C C   1 
ATOM   3091  O  O   . ARG C  1 116 ? 7.964   196.224 19.847  1.00 29.64  ? 115 ARG C O   1 
ATOM   3092  C  CB  . ARG C  1 116 ? 9.763   195.266 22.708  1.00 32.39  ? 115 ARG C CB  1 
ATOM   3093  C  CG  . ARG C  1 116 ? 9.690   195.741 24.142  1.00 36.85  ? 115 ARG C CG  1 
ATOM   3094  C  CD  . ARG C  1 116 ? 10.597  195.014 25.109  1.00 36.89  ? 115 ARG C CD  1 
ATOM   3095  N  NE  . ARG C  1 116 ? 10.680  195.676 26.424  1.00 32.71  ? 115 ARG C NE  1 
ATOM   3096  C  CZ  . ARG C  1 116 ? 11.743  196.372 26.900  1.00 31.59  ? 115 ARG C CZ  1 
ATOM   3097  N  NH1 . ARG C  1 116 ? 12.862  196.590 26.230  1.00 26.21  ? 115 ARG C NH1 1 
ATOM   3098  N  NH2 . ARG C  1 116 ? 11.671  196.874 28.116  1.00 31.57  ? 115 ARG C NH2 1 
ATOM   3099  N  N   . THR C  1 117 ? 9.895   194.976 19.763  1.00 33.42  ? 116 THR C N   1 
ATOM   3100  C  CA  . THR C  1 117 ? 9.745   194.455 18.399  1.00 33.52  ? 116 THR C CA  1 
ATOM   3101  C  C   . THR C  1 117 ? 9.426   193.014 18.332  1.00 33.32  ? 116 THR C C   1 
ATOM   3102  O  O   . THR C  1 117 ? 10.076  192.218 18.988  1.00 36.62  ? 116 THR C O   1 
ATOM   3103  C  CB  . THR C  1 117 ? 10.981  194.765 17.544  1.00 34.32  ? 116 THR C CB  1 
ATOM   3104  O  OG1 . THR C  1 117 ? 11.235  196.171 17.620  1.00 34.18  ? 116 THR C OG1 1 
ATOM   3105  C  CG2 . THR C  1 117 ? 10.810  194.356 16.046  1.00 29.28  ? 116 THR C CG2 1 
ATOM   3106  N  N   . LEU C  1 118 ? 8.413   192.682 17.551  1.00 32.23  ? 117 LEU C N   1 
ATOM   3107  C  CA  . LEU C  1 118 ? 8.139   191.288 17.192  1.00 31.72  ? 117 LEU C CA  1 
ATOM   3108  C  C   . LEU C  1 118 ? 8.903   190.973 15.939  1.00 32.44  ? 117 LEU C C   1 
ATOM   3109  O  O   . LEU C  1 118 ? 8.856   191.721 14.991  1.00 33.96  ? 117 LEU C O   1 
ATOM   3110  C  CB  . LEU C  1 118 ? 6.684   191.126 16.884  1.00 29.24  ? 117 LEU C CB  1 
ATOM   3111  C  CG  . LEU C  1 118 ? 6.004   189.787 16.743  1.00 31.34  ? 117 LEU C CG  1 
ATOM   3112  C  CD1 . LEU C  1 118 ? 6.307   188.833 17.894  1.00 28.76  ? 117 LEU C CD1 1 
ATOM   3113  C  CD2 . LEU C  1 118 ? 4.538   190.069 16.606  1.00 28.00  ? 117 LEU C CD2 1 
ATOM   3114  N  N   . VAL C  1 119 ? 9.582   189.844 15.911  1.00 34.42  ? 118 VAL C N   1 
ATOM   3115  C  CA  . VAL C  1 119 ? 10.379  189.435 14.735  1.00 33.57  ? 118 VAL C CA  1 
ATOM   3116  C  C   . VAL C  1 119 ? 9.994   188.004 14.390  1.00 38.40  ? 118 VAL C C   1 
ATOM   3117  O  O   . VAL C  1 119 ? 9.932   187.154 15.304  1.00 41.95  ? 118 VAL C O   1 
ATOM   3118  C  CB  . VAL C  1 119 ? 11.892  189.491 15.048  1.00 30.59  ? 118 VAL C CB  1 
ATOM   3119  C  CG1 . VAL C  1 119 ? 12.731  188.997 13.902  1.00 27.21  ? 118 VAL C CG1 1 
ATOM   3120  C  CG2 . VAL C  1 119 ? 12.268  190.891 15.440  1.00 28.80  ? 118 VAL C CG2 1 
ATOM   3121  N  N   . VAL C  1 120 ? 9.720   187.747 13.106  1.00 33.83  ? 119 VAL C N   1 
ATOM   3122  C  CA  . VAL C  1 120 ? 9.617   186.413 12.575  1.00 31.66  ? 119 VAL C CA  1 
ATOM   3123  C  C   . VAL C  1 120 ? 10.919  186.044 11.870  1.00 32.52  ? 119 VAL C C   1 
ATOM   3124  O  O   . VAL C  1 120 ? 11.456  186.833 11.121  1.00 32.77  ? 119 VAL C O   1 
ATOM   3125  C  CB  . VAL C  1 120 ? 8.381   186.144 11.731  1.00 31.39  ? 119 VAL C CB  1 
ATOM   3126  C  CG1 . VAL C  1 120 ? 8.301   187.024 10.503  1.00 32.53  ? 119 VAL C CG1 1 
ATOM   3127  C  CG2 . VAL C  1 120 ? 8.381   184.715 11.301  1.00 30.74  ? 119 VAL C CG2 1 
ATOM   3128  N  N   . HIS C  1 121 ? 11.464  184.859 12.170  1.00 34.09  ? 120 HIS C N   1 
ATOM   3129  C  CA  . HIS C  1 121 ? 12.795  184.531 11.673  1.00 31.95  ? 120 HIS C CA  1 
ATOM   3130  C  C   . HIS C  1 121 ? 12.873  183.615 10.478  1.00 36.94  ? 120 HIS C C   1 
ATOM   3131  O  O   . HIS C  1 121 ? 11.882  182.966 10.020  1.00 36.57  ? 120 HIS C O   1 
ATOM   3132  C  CB  . HIS C  1 121 ? 13.664  184.011 12.769  1.00 32.99  ? 120 HIS C CB  1 
ATOM   3133  C  CG  . HIS C  1 121 ? 14.116  185.040 13.769  1.00 31.93  ? 120 HIS C CG  1 
ATOM   3134  N  ND1 . HIS C  1 121 ? 15.420  185.469 13.850  1.00 32.93  ? 120 HIS C ND1 1 
ATOM   3135  C  CD2 . HIS C  1 121 ? 13.444  185.697 14.736  1.00 31.77  ? 120 HIS C CD2 1 
ATOM   3136  C  CE1 . HIS C  1 121 ? 15.533  186.354 14.822  1.00 33.85  ? 120 HIS C CE1 1 
ATOM   3137  N  NE2 . HIS C  1 121 ? 14.352  186.493 15.390  1.00 35.60  ? 120 HIS C NE2 1 
ATOM   3138  N  N   . GLU C  1 122 ? 14.081  183.594 9.931   1.00 42.76  ? 121 GLU C N   1 
ATOM   3139  C  CA  . GLU C  1 122 ? 14.348  182.839 8.707   1.00 40.49  ? 121 GLU C CA  1 
ATOM   3140  C  C   . GLU C  1 122 ? 14.080  181.323 8.844   1.00 42.68  ? 121 GLU C C   1 
ATOM   3141  O  O   . GLU C  1 122 ? 13.295  180.779 8.026   1.00 38.71  ? 121 GLU C O   1 
ATOM   3142  C  CB  . GLU C  1 122 ? 15.749  183.123 8.271   1.00 40.03  ? 121 GLU C CB  1 
ATOM   3143  C  CG  . GLU C  1 122 ? 16.007  182.506 6.930   1.00 45.09  ? 121 GLU C CG  1 
ATOM   3144  C  CD  . GLU C  1 122 ? 17.487  182.606 6.622   1.00 56.92  ? 121 GLU C CD  1 
ATOM   3145  O  OE1 . GLU C  1 122 ? 17.855  183.096 5.505   1.00 66.66  ? 121 GLU C OE1 1 
ATOM   3146  O  OE2 . GLU C  1 122 ? 18.290  182.254 7.527   1.00 52.52  ? 121 GLU C OE2 1 
ATOM   3147  N  N   . LYS C  1 123 ? 14.632  180.721 9.933   1.00 39.81  ? 122 LYS C N   1 
ATOM   3148  C  CA  . LYS C  1 123 ? 14.675  179.242 10.225  1.00 46.65  ? 122 LYS C CA  1 
ATOM   3149  C  C   . LYS C  1 123 ? 13.918  178.952 11.472  1.00 42.09  ? 122 LYS C C   1 
ATOM   3150  O  O   . LYS C  1 123 ? 13.757  179.834 12.293  1.00 41.83  ? 122 LYS C O   1 
ATOM   3151  C  CB  . LYS C  1 123 ? 16.127  178.729 10.521  1.00 47.22  ? 122 LYS C CB  1 
ATOM   3152  C  CG  . LYS C  1 123 ? 17.044  178.593 9.303   1.00 55.77  ? 122 LYS C CG  1 
ATOM   3153  C  CD  . LYS C  1 123 ? 18.550  178.798 9.603   1.00 57.14  ? 122 LYS C CD  1 
ATOM   3154  C  CE  . LYS C  1 123 ? 19.298  178.999 8.270   1.00 61.67  ? 122 LYS C CE  1 
ATOM   3155  N  NZ  . LYS C  1 123 ? 20.800  179.202 8.296   1.00 62.03  ? 122 LYS C NZ  1 
ATOM   3156  N  N   . ALA C  1 124 ? 13.544  177.686 11.625  1.00 43.86  ? 123 ALA C N   1 
ATOM   3157  C  CA  . ALA C  1 124 ? 13.045  177.118 12.887  1.00 46.53  ? 123 ALA C CA  1 
ATOM   3158  C  C   . ALA C  1 124 ? 13.952  177.459 14.069  1.00 48.30  ? 123 ALA C C   1 
ATOM   3159  O  O   . ALA C  1 124 ? 15.214  177.554 13.956  1.00 47.39  ? 123 ALA C O   1 
ATOM   3160  C  CB  . ALA C  1 124 ? 12.839  175.598 12.788  1.00 40.16  ? 123 ALA C CB  1 
ATOM   3161  N  N   . ASP C  1 125 ? 13.278  177.755 15.180  1.00 46.35  ? 124 ASP C N   1 
ATOM   3162  C  CA  . ASP C  1 125 ? 13.953  178.012 16.438  1.00 47.35  ? 124 ASP C CA  1 
ATOM   3163  C  C   . ASP C  1 125 ? 14.178  176.600 17.026  1.00 47.01  ? 124 ASP C C   1 
ATOM   3164  O  O   . ASP C  1 125 ? 13.181  175.858 17.155  1.00 44.18  ? 124 ASP C O   1 
ATOM   3165  C  CB  . ASP C  1 125 ? 12.966  178.754 17.334  1.00 45.18  ? 124 ASP C CB  1 
ATOM   3166  C  CG  . ASP C  1 125 ? 13.560  179.189 18.678  1.00 44.59  ? 124 ASP C CG  1 
ATOM   3167  O  OD1 . ASP C  1 125 ? 14.630  178.696 19.125  1.00 47.07  ? 124 ASP C OD1 1 
ATOM   3168  O  OD2 . ASP C  1 125 ? 12.932  180.072 19.303  1.00 44.31  ? 124 ASP C OD2 1 
ATOM   3169  N  N   . ASP C  1 126 ? 15.426  176.249 17.390  1.00 42.37  ? 125 ASP C N   1 
ATOM   3170  C  CA  . ASP C  1 126 ? 15.697  174.961 18.104  1.00 46.57  ? 125 ASP C CA  1 
ATOM   3171  C  C   . ASP C  1 126 ? 15.400  174.931 19.618  1.00 49.63  ? 125 ASP C C   1 
ATOM   3172  O  O   . ASP C  1 126 ? 15.885  174.016 20.328  1.00 48.04  ? 125 ASP C O   1 
ATOM   3173  C  CB  . ASP C  1 126 ? 17.130  174.483 17.896  1.00 40.61  ? 125 ASP C CB  1 
ATOM   3174  C  CG  . ASP C  1 126 ? 18.158  175.378 18.597  1.00 45.10  ? 125 ASP C CG  1 
ATOM   3175  O  OD1 . ASP C  1 126 ? 17.860  175.904 19.721  1.00 39.29  ? 125 ASP C OD1 1 
ATOM   3176  O  OD2 . ASP C  1 126 ? 19.283  175.541 18.007  1.00 43.06  ? 125 ASP C OD2 1 
ATOM   3177  N  N   . LEU C  1 127 ? 14.667  175.946 20.104  1.00 44.69  ? 126 LEU C N   1 
ATOM   3178  C  CA  . LEU C  1 127 ? 14.154  176.012 21.472  1.00 43.20  ? 126 LEU C CA  1 
ATOM   3179  C  C   . LEU C  1 127 ? 15.284  175.871 22.506  1.00 41.36  ? 126 LEU C C   1 
ATOM   3180  O  O   . LEU C  1 127 ? 15.045  175.448 23.622  1.00 48.17  ? 126 LEU C O   1 
ATOM   3181  C  CB  . LEU C  1 127 ? 13.048  174.947 21.684  1.00 41.35  ? 126 LEU C CB  1 
ATOM   3182  C  CG  . LEU C  1 127 ? 11.993  174.858 20.561  1.00 45.81  ? 126 LEU C CG  1 
ATOM   3183  C  CD1 . LEU C  1 127 ? 10.861  173.824 20.822  1.00 45.08  ? 126 LEU C CD1 1 
ATOM   3184  C  CD2 . LEU C  1 127 ? 11.378  176.210 20.184  1.00 44.52  ? 126 LEU C CD2 1 
ATOM   3185  N  N   . GLY C  1 128 ? 16.517  176.179 22.133  1.00 38.12  ? 127 GLY C N   1 
ATOM   3186  C  CA  . GLY C  1 128 ? 17.625  176.072 23.084  1.00 44.69  ? 127 GLY C CA  1 
ATOM   3187  C  C   . GLY C  1 128 ? 18.303  174.686 23.147  1.00 52.19  ? 127 GLY C C   1 
ATOM   3188  O  O   . GLY C  1 128 ? 19.378  174.538 23.749  1.00 55.77  ? 127 GLY C O   1 
ATOM   3189  N  N   . LYS C  1 129 ? 17.748  173.680 22.478  1.00 47.98  ? 128 LYS C N   1 
ATOM   3190  C  CA  . LYS C  1 129 ? 18.254  172.304 22.651  1.00 56.03  ? 128 LYS C CA  1 
ATOM   3191  C  C   . LYS C  1 129 ? 19.053  171.876 21.376  1.00 55.23  ? 128 LYS C C   1 
ATOM   3192  O  O   . LYS C  1 129 ? 18.872  170.788 20.806  1.00 51.98  ? 128 LYS C O   1 
ATOM   3193  C  CB  . LYS C  1 129 ? 17.074  171.353 23.047  1.00 53.47  ? 128 LYS C CB  1 
ATOM   3194  C  CG  . LYS C  1 129 ? 16.045  172.005 23.981  1.00 48.97  ? 128 LYS C CG  1 
ATOM   3195  C  CD  . LYS C  1 129 ? 14.976  171.030 24.465  1.00 61.20  ? 128 LYS C CD  1 
ATOM   3196  C  CE  . LYS C  1 129 ? 13.506  171.425 24.130  1.00 62.11  ? 128 LYS C CE  1 
ATOM   3197  N  NZ  . LYS C  1 129 ? 13.195  172.613 24.996  1.00 54.70  ? 128 LYS C NZ  1 
ATOM   3198  N  N   . GLY C  1 130 ? 19.903  172.775 20.889  1.00 56.07  ? 129 GLY C N   1 
ATOM   3199  C  CA  . GLY C  1 130 ? 20.665  172.479 19.675  1.00 54.69  ? 129 GLY C CA  1 
ATOM   3200  C  C   . GLY C  1 130 ? 22.092  172.036 19.944  1.00 56.63  ? 129 GLY C C   1 
ATOM   3201  O  O   . GLY C  1 130 ? 22.769  171.590 19.004  1.00 64.35  ? 129 GLY C O   1 
ATOM   3202  N  N   . GLY C  1 131 ? 22.548  172.182 21.200  1.00 58.43  ? 130 GLY C N   1 
ATOM   3203  C  CA  . GLY C  1 131 ? 23.900  171.780 21.686  1.00 56.37  ? 130 GLY C CA  1 
ATOM   3204  C  C   . GLY C  1 131 ? 25.095  172.688 21.394  1.00 65.02  ? 130 GLY C C   1 
ATOM   3205  O  O   . GLY C  1 131 ? 26.246  172.343 21.726  1.00 70.08  ? 130 GLY C O   1 
ATOM   3206  N  N   . ASN C  1 132 ? 24.894  173.837 20.755  1.00 62.72  ? 131 ASN C N   1 
ATOM   3207  C  CA  . ASN C  1 132 ? 26.019  174.827 20.687  1.00 60.84  ? 131 ASN C CA  1 
ATOM   3208  C  C   . ASN C  1 132 ? 25.639  176.143 21.387  1.00 62.28  ? 131 ASN C C   1 
ATOM   3209  O  O   . ASN C  1 132 ? 24.493  176.344 21.880  1.00 66.16  ? 131 ASN C O   1 
ATOM   3210  C  CB  . ASN C  1 132 ? 26.431  175.096 19.247  1.00 58.57  ? 131 ASN C CB  1 
ATOM   3211  C  CG  . ASN C  1 132 ? 25.232  175.471 18.385  1.00 65.06  ? 131 ASN C CG  1 
ATOM   3212  O  OD1 . ASN C  1 132 ? 24.178  174.783 18.412  1.00 55.14  ? 131 ASN C OD1 1 
ATOM   3213  N  ND2 . ASN C  1 132 ? 25.360  176.600 17.648  1.00 67.56  ? 131 ASN C ND2 1 
ATOM   3214  N  N   . GLU C  1 133 ? 26.587  177.054 21.451  1.00 59.24  ? 132 GLU C N   1 
ATOM   3215  C  CA  . GLU C  1 133 ? 26.360  178.225 22.283  1.00 61.31  ? 132 GLU C CA  1 
ATOM   3216  C  C   . GLU C  1 133 ? 25.292  179.192 21.662  1.00 62.85  ? 132 GLU C C   1 
ATOM   3217  O  O   . GLU C  1 133 ? 24.651  179.948 22.406  1.00 62.70  ? 132 GLU C O   1 
ATOM   3218  C  CB  . GLU C  1 133 ? 27.683  178.943 22.459  1.00 68.10  ? 132 GLU C CB  1 
ATOM   3219  C  CG  . GLU C  1 133 ? 27.999  179.859 21.255  1.00 73.16  ? 132 GLU C CG  1 
ATOM   3220  C  CD  . GLU C  1 133 ? 29.291  180.616 21.455  1.00 90.06  ? 132 GLU C CD  1 
ATOM   3221  O  OE1 . GLU C  1 133 ? 29.479  181.184 22.596  1.00 72.86  ? 132 GLU C OE1 1 
ATOM   3222  O  OE2 . GLU C  1 133 ? 30.111  180.606 20.475  1.00 83.84  ? 132 GLU C OE2 1 
ATOM   3223  N  N   . GLU C  1 134 ? 25.159  179.179 20.318  1.00 57.88  ? 133 GLU C N   1 
ATOM   3224  C  CA  . GLU C  1 134 ? 24.171  179.975 19.521  1.00 54.93  ? 133 GLU C CA  1 
ATOM   3225  C  C   . GLU C  1 134 ? 22.736  179.514 19.898  1.00 55.62  ? 133 GLU C C   1 
ATOM   3226  O  O   . GLU C  1 134 ? 21.846  180.358 20.173  1.00 50.88  ? 133 GLU C O   1 
ATOM   3227  C  CB  . GLU C  1 134 ? 24.457  179.827 17.975  1.00 58.47  ? 133 GLU C CB  1 
ATOM   3228  C  CG  . GLU C  1 134 ? 23.985  180.901 16.969  1.00 54.00  ? 133 GLU C CG  1 
ATOM   3229  C  CD  . GLU C  1 134 ? 24.024  182.317 17.559  1.00 65.69  ? 133 GLU C CD  1 
ATOM   3230  O  OE1 . GLU C  1 134 ? 22.936  182.950 17.694  1.00 55.55  ? 133 GLU C OE1 1 
ATOM   3231  O  OE2 . GLU C  1 134 ? 25.127  182.781 17.968  1.00 66.76  ? 133 GLU C OE2 1 
ATOM   3232  N  N   . SER C  1 135 ? 22.516  178.191 19.948  1.00 56.64  ? 134 SER C N   1 
ATOM   3233  C  CA  . SER C  1 135 ? 21.198  177.629 20.360  1.00 58.51  ? 134 SER C CA  1 
ATOM   3234  C  C   . SER C  1 135 ? 20.741  178.226 21.720  1.00 59.79  ? 134 SER C C   1 
ATOM   3235  O  O   . SER C  1 135 ? 19.544  178.401 22.015  1.00 54.29  ? 134 SER C O   1 
ATOM   3236  C  CB  . SER C  1 135 ? 21.283  176.101 20.413  1.00 57.65  ? 134 SER C CB  1 
ATOM   3237  O  OG  . SER C  1 135 ? 20.147  175.538 21.026  1.00 44.97  ? 134 SER C OG  1 
ATOM   3238  N  N   . THR C  1 136 ? 21.746  178.584 22.505  1.00 55.59  ? 135 THR C N   1 
ATOM   3239  C  CA  . THR C  1 136 ? 21.602  179.228 23.800  1.00 53.93  ? 135 THR C CA  1 
ATOM   3240  C  C   . THR C  1 136 ? 21.206  180.732 23.828  1.00 63.52  ? 135 THR C C   1 
ATOM   3241  O  O   . THR C  1 136 ? 20.631  181.221 24.848  1.00 62.89  ? 135 THR C O   1 
ATOM   3242  C  CB  . THR C  1 136 ? 22.950  179.014 24.491  1.00 54.79  ? 135 THR C CB  1 
ATOM   3243  O  OG1 . THR C  1 136 ? 22.748  177.963 25.391  1.00 49.88  ? 135 THR C OG1 1 
ATOM   3244  C  CG2 . THR C  1 136 ? 23.595  180.313 25.188  1.00 53.18  ? 135 THR C CG2 1 
ATOM   3245  N  N   . LYS C  1 137 ? 21.566  181.472 22.764  1.00 58.47  ? 136 LYS C N   1 
ATOM   3246  C  CA  . LYS C  1 137 ? 21.139  182.904 22.586  1.00 54.74  ? 136 LYS C CA  1 
ATOM   3247  C  C   . LYS C  1 137 ? 19.936  183.104 21.647  1.00 50.88  ? 136 LYS C C   1 
ATOM   3248  O  O   . LYS C  1 137 ? 19.047  183.850 21.991  1.00 54.21  ? 136 LYS C O   1 
ATOM   3249  C  CB  . LYS C  1 137 ? 22.305  183.772 22.157  1.00 48.05  ? 136 LYS C CB  1 
ATOM   3250  C  CG  . LYS C  1 137 ? 23.589  183.288 22.825  1.00 51.58  ? 136 LYS C CG  1 
ATOM   3251  C  CD  . LYS C  1 137 ? 24.735  184.297 22.779  1.00 51.84  ? 136 LYS C CD  1 
ATOM   3252  C  CE  . LYS C  1 137 ? 25.625  184.106 21.537  1.00 61.19  ? 136 LYS C CE  1 
ATOM   3253  N  NZ  . LYS C  1 137 ? 26.953  184.800 21.682  1.00 58.15  ? 136 LYS C NZ  1 
ATOM   3254  N  N   . THR C  1 138 ? 19.881  182.393 20.513  1.00 46.62  ? 137 THR C N   1 
ATOM   3255  C  CA  . THR C  1 138 ? 18.833  182.617 19.516  1.00 43.64  ? 137 THR C CA  1 
ATOM   3256  C  C   . THR C  1 138 ? 18.076  181.405 19.079  1.00 49.31  ? 137 THR C C   1 
ATOM   3257  O  O   . THR C  1 138 ? 17.156  181.539 18.201  1.00 46.83  ? 137 THR C O   1 
ATOM   3258  C  CB  . THR C  1 138 ? 19.421  183.157 18.184  1.00 44.11  ? 137 THR C CB  1 
ATOM   3259  O  OG1 . THR C  1 138 ? 20.364  182.226 17.684  1.00 43.07  ? 137 THR C OG1 1 
ATOM   3260  C  CG2 . THR C  1 138 ? 20.175  184.519 18.403  1.00 42.34  ? 137 THR C CG2 1 
ATOM   3261  N  N   . GLY C  1 139 ? 18.470  180.229 19.608  1.00 42.11  ? 138 GLY C N   1 
ATOM   3262  C  CA  . GLY C  1 139 ? 17.905  179.002 19.100  1.00 40.27  ? 138 GLY C CA  1 
ATOM   3263  C  C   . GLY C  1 139 ? 18.168  178.742 17.597  1.00 41.11  ? 138 GLY C C   1 
ATOM   3264  O  O   . GLY C  1 139 ? 17.354  178.019 16.924  1.00 40.36  ? 138 GLY C O   1 
ATOM   3265  N  N   . ASN C  1 140 ? 19.261  179.320 17.065  1.00 35.99  ? 139 ASN C N   1 
ATOM   3266  C  CA  . ASN C  1 140 ? 19.617  179.182 15.619  1.00 45.99  ? 139 ASN C CA  1 
ATOM   3267  C  C   . ASN C  1 140 ? 18.478  179.466 14.604  1.00 49.58  ? 139 ASN C C   1 
ATOM   3268  O  O   . ASN C  1 140 ? 18.411  178.765 13.547  1.00 47.56  ? 139 ASN C O   1 
ATOM   3269  C  CB  . ASN C  1 140 ? 20.268  177.785 15.318  1.00 46.56  ? 139 ASN C CB  1 
ATOM   3270  C  CG  . ASN C  1 140 ? 21.545  177.594 16.087  1.00 51.73  ? 139 ASN C CG  1 
ATOM   3271  O  OD1 . ASN C  1 140 ? 22.535  178.281 15.813  1.00 53.10  ? 139 ASN C OD1 1 
ATOM   3272  N  ND2 . ASN C  1 140 ? 21.499  176.781 17.159  1.00 49.20  ? 139 ASN C ND2 1 
ATOM   3273  N  N   . ALA C  1 141 ? 17.594  180.447 14.917  1.00 43.45  ? 140 ALA C N   1 
ATOM   3274  C  CA  . ALA C  1 141 ? 16.451  180.825 14.006  1.00 41.84  ? 140 ALA C CA  1 
ATOM   3275  C  C   . ALA C  1 141 ? 16.901  181.682 12.795  1.00 41.75  ? 140 ALA C C   1 
ATOM   3276  O  O   . ALA C  1 141 ? 16.115  181.884 11.843  1.00 36.70  ? 140 ALA C O   1 
ATOM   3277  C  CB  . ALA C  1 141 ? 15.342  181.551 14.763  1.00 40.83  ? 140 ALA C CB  1 
ATOM   3278  N  N   . GLY C  1 142 ? 18.163  182.151 12.856  1.00 41.69  ? 141 GLY C N   1 
ATOM   3279  C  CA  . GLY C  1 142 ? 18.793  182.853 11.775  1.00 40.30  ? 141 GLY C CA  1 
ATOM   3280  C  C   . GLY C  1 142 ? 18.275  184.317 11.647  1.00 51.36  ? 141 GLY C C   1 
ATOM   3281  O  O   . GLY C  1 142 ? 17.992  185.062 12.673  1.00 43.69  ? 141 GLY C O   1 
ATOM   3282  N  N   . SER C  1 143 ? 18.152  184.728 10.378  1.00 43.72  ? 142 SER C N   1 
ATOM   3283  C  CA  . SER C  1 143 ? 17.962  186.111 10.072  1.00 44.22  ? 142 SER C CA  1 
ATOM   3284  C  C   . SER C  1 143 ? 16.504  186.589 10.312  1.00 36.58  ? 142 SER C C   1 
ATOM   3285  O  O   . SER C  1 143 ? 15.543  185.804 10.423  1.00 33.70  ? 142 SER C O   1 
ATOM   3286  C  CB  . SER C  1 143 ? 18.454  186.383 8.639   1.00 45.78  ? 142 SER C CB  1 
ATOM   3287  O  OG  . SER C  1 143 ? 17.540  185.844 7.701   1.00 49.18  ? 142 SER C OG  1 
ATOM   3288  N  N   . ARG C  1 144 ? 16.400  187.901 10.409  1.00 36.86  ? 143 ARG C N   1 
ATOM   3289  C  CA  . ARG C  1 144 ? 15.150  188.600 10.642  1.00 35.64  ? 143 ARG C CA  1 
ATOM   3290  C  C   . ARG C  1 144 ? 14.422  188.862 9.344   1.00 33.79  ? 143 ARG C C   1 
ATOM   3291  O  O   . ARG C  1 144 ? 14.941  189.532 8.510   1.00 33.68  ? 143 ARG C O   1 
ATOM   3292  C  CB  . ARG C  1 144 ? 15.485  189.840 11.424  1.00 31.20  ? 143 ARG C CB  1 
ATOM   3293  C  CG  . ARG C  1 144 ? 16.325  189.424 12.590  1.00 29.07  ? 143 ARG C CG  1 
ATOM   3294  C  CD  . ARG C  1 144 ? 16.849  190.596 13.337  1.00 29.12  ? 143 ARG C CD  1 
ATOM   3295  N  NE  . ARG C  1 144 ? 17.617  190.135 14.476  1.00 31.52  ? 143 ARG C NE  1 
ATOM   3296  C  CZ  . ARG C  1 144 ? 17.912  190.851 15.555  1.00 34.30  ? 143 ARG C CZ  1 
ATOM   3297  N  NH1 . ARG C  1 144 ? 17.470  192.123 15.719  1.00 34.21  ? 143 ARG C NH1 1 
ATOM   3298  N  NH2 . ARG C  1 144 ? 18.698  190.305 16.472  1.00 32.77  ? 143 ARG C NH2 1 
ATOM   3299  N  N   . LEU C  1 145 ? 13.245  188.275 9.158   1.00 33.63  ? 144 LEU C N   1 
ATOM   3300  C  CA  . LEU C  1 145 ? 12.536  188.421 7.897   1.00 31.96  ? 144 LEU C CA  1 
ATOM   3301  C  C   . LEU C  1 145 ? 11.573  189.546 7.919   1.00 35.66  ? 144 LEU C C   1 
ATOM   3302  O  O   . LEU C  1 145 ? 11.443  190.213 6.948   1.00 38.95  ? 144 LEU C O   1 
ATOM   3303  C  CB  . LEU C  1 145 ? 11.731  187.187 7.579   1.00 31.94  ? 144 LEU C CB  1 
ATOM   3304  C  CG  . LEU C  1 145 ? 12.429  185.853 7.348   1.00 34.65  ? 144 LEU C CG  1 
ATOM   3305  C  CD1 . LEU C  1 145 ? 11.423  184.900 6.754   1.00 33.21  ? 144 LEU C CD1 1 
ATOM   3306  C  CD2 . LEU C  1 145 ? 13.625  185.984 6.434   1.00 32.01  ? 144 LEU C CD2 1 
ATOM   3307  N  N   . ALA C  1 146 ? 10.799  189.684 8.993   1.00 34.69  ? 145 ALA C N   1 
ATOM   3308  C  CA  . ALA C  1 146 ? 9.933   190.804 9.154   1.00 30.15  ? 145 ALA C CA  1 
ATOM   3309  C  C   . ALA C  1 146 ? 9.915   191.224 10.637  1.00 31.52  ? 145 ALA C C   1 
ATOM   3310  O  O   . ALA C  1 146 ? 10.399  190.503 11.505  1.00 32.18  ? 145 ALA C O   1 
ATOM   3311  C  CB  . ALA C  1 146 ? 8.575   190.508 8.591   1.00 24.20  ? 145 ALA C CB  1 
ATOM   3312  N  N   . CYS C  1 147 ? 9.435   192.430 10.904  1.00 34.16  ? 146 CYS C N   1 
ATOM   3313  C  CA  . CYS C  1 147 ? 9.302   192.950 12.285  1.00 36.10  ? 146 CYS C CA  1 
ATOM   3314  C  C   . CYS C  1 147 ? 8.380   194.119 12.326  1.00 33.99  ? 146 CYS C C   1 
ATOM   3315  O  O   . CYS C  1 147 ? 7.933   194.587 11.290  1.00 37.26  ? 146 CYS C O   1 
ATOM   3316  C  CB  . CYS C  1 147 ? 10.640  193.291 12.916  1.00 35.00  ? 146 CYS C CB  1 
ATOM   3317  S  SG  . CYS C  1 147 ? 11.550  194.527 12.029  1.00 36.35  ? 146 CYS C SG  1 
ATOM   3318  N  N   . GLY C  1 148 ? 8.087   194.569 13.527  1.00 32.46  ? 147 GLY C N   1 
ATOM   3319  C  CA  . GLY C  1 148 ? 7.238   195.714 13.764  1.00 29.61  ? 147 GLY C CA  1 
ATOM   3320  C  C   . GLY C  1 148 ? 7.316   196.018 15.237  1.00 31.95  ? 147 GLY C C   1 
ATOM   3321  O  O   . GLY C  1 148 ? 7.600   195.111 16.057  1.00 31.94  ? 147 GLY C O   1 
ATOM   3322  N  N   . VAL C  1 149 ? 7.021   197.272 15.578  1.00 29.88  ? 148 VAL C N   1 
ATOM   3323  C  CA  . VAL C  1 149 ? 6.824   197.690 16.941  1.00 27.24  ? 148 VAL C CA  1 
ATOM   3324  C  C   . VAL C  1 149 ? 5.453   197.275 17.506  1.00 27.32  ? 148 VAL C C   1 
ATOM   3325  O  O   . VAL C  1 149 ? 4.448   197.389 16.846  1.00 25.80  ? 148 VAL C O   1 
ATOM   3326  C  CB  . VAL C  1 149 ? 7.165   199.181 17.158  1.00 29.31  ? 148 VAL C CB  1 
ATOM   3327  C  CG1 . VAL C  1 149 ? 7.294   199.452 18.642  1.00 27.02  ? 148 VAL C CG1 1 
ATOM   3328  C  CG2 . VAL C  1 149 ? 8.492   199.565 16.474  1.00 26.10  ? 148 VAL C CG2 1 
ATOM   3329  N  N   . ILE C  1 150 ? 5.450   196.725 18.736  1.00 28.18  ? 149 ILE C N   1 
ATOM   3330  C  CA  . ILE C  1 150 ? 4.211   196.263 19.343  1.00 28.62  ? 149 ILE C CA  1 
ATOM   3331  C  C   . ILE C  1 150 ? 3.538   197.467 19.906  1.00 27.25  ? 149 ILE C C   1 
ATOM   3332  O  O   . ILE C  1 150 ? 4.099   198.105 20.738  1.00 30.83  ? 149 ILE C O   1 
ATOM   3333  C  CB  . ILE C  1 150 ? 4.476   195.206 20.437  1.00 29.91  ? 149 ILE C CB  1 
ATOM   3334  C  CG1 . ILE C  1 150 ? 5.210   194.000 19.840  1.00 28.39  ? 149 ILE C CG1 1 
ATOM   3335  C  CG2 . ILE C  1 150 ? 3.161   194.744 21.018  1.00 25.31  ? 149 ILE C CG2 1 
ATOM   3336  C  CD1 . ILE C  1 150 ? 5.574   192.924 20.797  1.00 26.96  ? 149 ILE C CD1 1 
ATOM   3337  N  N   . GLY C  1 151 ? 2.351   197.807 19.459  1.00 28.65  ? 150 GLY C N   1 
ATOM   3338  C  CA  . GLY C  1 151 ? 1.700   199.043 19.888  1.00 29.88  ? 150 GLY C CA  1 
ATOM   3339  C  C   . GLY C  1 151 ? 0.403   198.878 20.621  1.00 29.07  ? 150 GLY C C   1 
ATOM   3340  O  O   . GLY C  1 151 ? -0.232  197.857 20.435  1.00 33.68  ? 150 GLY C O   1 
ATOM   3341  N  N   . ILE C  1 152 ? 0.019   199.828 21.469  1.00 28.02  ? 151 ILE C N   1 
ATOM   3342  C  CA  . ILE C  1 152 ? -1.260  199.747 22.185  1.00 30.70  ? 151 ILE C CA  1 
ATOM   3343  C  C   . ILE C  1 152 ? -2.385  199.798 21.157  1.00 33.19  ? 151 ILE C C   1 
ATOM   3344  O  O   . ILE C  1 152 ? -2.330  200.573 20.182  1.00 30.24  ? 151 ILE C O   1 
ATOM   3345  C  CB  . ILE C  1 152 ? -1.434  200.926 23.209  1.00 36.14  ? 151 ILE C CB  1 
ATOM   3346  C  CG1 . ILE C  1 152 ? -0.365  200.802 24.234  1.00 40.71  ? 151 ILE C CG1 1 
ATOM   3347  C  CG2 . ILE C  1 152 ? -2.651  200.781 24.158  1.00 31.98  ? 151 ILE C CG2 1 
ATOM   3348  C  CD1 . ILE C  1 152 ? -0.191  202.079 24.991  1.00 42.67  ? 151 ILE C CD1 1 
ATOM   3349  N  N   . ALA C  1 153 ? -3.377  198.940 21.353  1.00 34.65  ? 152 ALA C N   1 
ATOM   3350  C  CA  . ALA C  1 153 ? -4.521  198.859 20.433  1.00 34.08  ? 152 ALA C CA  1 
ATOM   3351  C  C   . ALA C  1 153 ? -5.777  199.085 21.203  1.00 36.21  ? 152 ALA C C   1 
ATOM   3352  O  O   . ALA C  1 153 ? -5.794  198.996 22.441  1.00 37.61  ? 152 ALA C O   1 
ATOM   3353  C  CB  . ALA C  1 153 ? -4.589  197.532 19.739  1.00 31.57  ? 152 ALA C CB  1 
ATOM   3354  N  N   . GLN C  1 154 ? -6.800  199.452 20.459  1.00 35.75  ? 153 GLN C N   1 
ATOM   3355  C  CA  . GLN C  1 154 ? -8.110  199.781 20.972  1.00 38.42  ? 153 GLN C CA  1 
ATOM   3356  C  C   . GLN C  1 154 ? -8.963  198.484 21.208  1.00 46.36  ? 153 GLN C C   1 
ATOM   3357  O  O   . GLN C  1 154 ? -8.947  197.542 20.316  1.00 43.79  ? 153 GLN C O   1 
ATOM   3358  C  CB  . GLN C  1 154 ? -8.827  200.662 19.959  1.00 35.30  ? 153 GLN C CB  1 
ATOM   3359  C  CG  . GLN C  1 154 ? -10.305 200.708 20.223  1.00 41.56  ? 153 GLN C CG  1 
ATOM   3360  C  CD  . GLN C  1 154 ? -10.972 201.944 19.666  1.00 50.17  ? 153 GLN C CD  1 
ATOM   3361  O  OE1 . GLN C  1 154 ? -11.187 202.059 18.451  1.00 50.80  ? 153 GLN C OE1 1 
ATOM   3362  N  NE2 . GLN C  1 154 ? -11.312 202.884 20.552  1.00 50.07  ? 153 GLN C NE2 1 
ATOM   3363  O  OXT . GLN C  1 154 ? -9.701  198.385 22.270  1.00 43.79  ? 153 GLN C OXT 1 
ATOM   3364  N  N   . MET D  1 1   ? 11.399  201.049 33.243  1.00 58.81  ? 0   MET D N   1 
ATOM   3365  C  CA  . MET D  1 1   ? 12.584  201.971 33.523  1.00 65.49  ? 0   MET D CA  1 
ATOM   3366  C  C   . MET D  1 1   ? 13.219  202.620 32.204  1.00 68.39  ? 0   MET D C   1 
ATOM   3367  O  O   . MET D  1 1   ? 14.481  202.824 32.131  1.00 55.90  ? 0   MET D O   1 
ATOM   3368  C  CB  . MET D  1 1   ? 13.650  201.233 34.429  1.00 54.90  ? 0   MET D CB  1 
ATOM   3369  N  N   . ALA D  1 2   ? 12.383  202.952 31.174  1.00 59.35  ? 1   ALA D N   1 
ATOM   3370  C  CA  . ALA D  1 2   ? 12.916  203.495 29.829  1.00 49.41  ? 1   ALA D CA  1 
ATOM   3371  C  C   . ALA D  1 2   ? 13.390  204.951 29.866  1.00 42.79  ? 1   ALA D C   1 
ATOM   3372  O  O   . ALA D  1 2   ? 12.690  205.786 30.404  1.00 41.97  ? 1   ALA D O   1 
ATOM   3373  C  CB  . ALA D  1 2   ? 11.913  203.335 28.702  1.00 44.98  ? 1   ALA D CB  1 
ATOM   3374  N  N   . THR D  1 3   ? 14.563  205.245 29.312  1.00 37.45  ? 2   THR D N   1 
ATOM   3375  C  CA  . THR D  1 3   ? 15.020  206.602 29.245  1.00 39.70  ? 2   THR D CA  1 
ATOM   3376  C  C   . THR D  1 3   ? 15.120  207.078 27.795  1.00 40.18  ? 2   THR D C   1 
ATOM   3377  O  O   . THR D  1 3   ? 15.310  208.323 27.530  1.00 34.58  ? 2   THR D O   1 
ATOM   3378  C  CB  . THR D  1 3   ? 16.398  206.792 29.901  1.00 46.88  ? 2   THR D CB  1 
ATOM   3379  O  OG1 . THR D  1 3   ? 17.277  205.762 29.412  1.00 52.56  ? 2   THR D OG1 1 
ATOM   3380  C  CG2 . THR D  1 3   ? 16.309  206.740 31.414  1.00 40.99  ? 2   THR D CG2 1 
ATOM   3381  N  N   . LYS D  1 4   ? 14.994  206.106 26.871  1.00 35.07  ? 3   LYS D N   1 
ATOM   3382  C  CA  . LYS D  1 4   ? 15.086  206.415 25.453  1.00 33.66  ? 3   LYS D CA  1 
ATOM   3383  C  C   . LYS D  1 4   ? 14.047  205.792 24.587  1.00 30.61  ? 3   LYS D C   1 
ATOM   3384  O  O   . LYS D  1 4   ? 13.673  204.638 24.752  1.00 28.68  ? 3   LYS D O   1 
ATOM   3385  C  CB  . LYS D  1 4   ? 16.476  206.130 24.910  1.00 36.37  ? 3   LYS D CB  1 
ATOM   3386  C  CG  . LYS D  1 4   ? 17.494  207.150 25.322  1.00 39.01  ? 3   LYS D CG  1 
ATOM   3387  C  CD  . LYS D  1 4   ? 18.878  206.558 25.126  1.00 51.87  ? 3   LYS D CD  1 
ATOM   3388  C  CE  . LYS D  1 4   ? 19.963  207.639 25.169  1.00 58.91  ? 3   LYS D CE  1 
ATOM   3389  N  NZ  . LYS D  1 4   ? 20.853  207.300 24.010  1.00 60.53  ? 3   LYS D NZ  1 
ATOM   3390  N  N   . ALA D  1 5   ? 13.598  206.570 23.626  1.00 28.49  ? 4   ALA D N   1 
ATOM   3391  C  CA  . ALA D  1 5   ? 12.656  206.014 22.706  1.00 29.45  ? 4   ALA D CA  1 
ATOM   3392  C  C   . ALA D  1 5   ? 12.976  206.490 21.296  1.00 27.52  ? 4   ALA D C   1 
ATOM   3393  O  O   . ALA D  1 5   ? 13.766  207.395 21.133  1.00 28.15  ? 4   ALA D O   1 
ATOM   3394  C  CB  . ALA D  1 5   ? 11.200  206.305 23.157  1.00 27.56  ? 4   ALA D CB  1 
ATOM   3395  N  N   . VAL D  1 6   ? 12.420  205.809 20.297  1.00 28.94  ? 5   VAL D N   1 
ATOM   3396  C  CA  . VAL D  1 6   ? 12.582  206.149 18.906  1.00 27.77  ? 5   VAL D CA  1 
ATOM   3397  C  C   . VAL D  1 6   ? 11.365  205.888 18.058  1.00 26.81  ? 5   VAL D C   1 
ATOM   3398  O  O   . VAL D  1 6   ? 10.575  205.058 18.376  1.00 26.37  ? 5   VAL D O   1 
ATOM   3399  C  CB  . VAL D  1 6   ? 13.871  205.518 18.343  1.00 29.61  ? 5   VAL D CB  1 
ATOM   3400  C  CG1 . VAL D  1 6   ? 13.702  204.027 18.062  1.00 31.21  ? 5   VAL D CG1 1 
ATOM   3401  C  CG2 . VAL D  1 6   ? 14.283  206.248 17.085  1.00 28.73  ? 5   VAL D CG2 1 
ATOM   3402  N  N   . CYS D  1 7   ? 11.228  206.621 16.969  1.00 30.73  ? 6   CYS D N   1 
ATOM   3403  C  CA  . CYS D  1 7   ? 10.120  206.458 16.063  1.00 28.94  ? 6   CYS D CA  1 
ATOM   3404  C  C   . CYS D  1 7   ? 10.545  206.674 14.618  1.00 29.31  ? 6   CYS D C   1 
ATOM   3405  O  O   . CYS D  1 7   ? 11.103  207.693 14.291  1.00 31.87  ? 6   CYS D O   1 
ATOM   3406  C  CB  . CYS D  1 7   ? 9.066   207.472 16.418  1.00 28.32  ? 6   CYS D CB  1 
ATOM   3407  S  SG  . CYS D  1 7   ? 7.550   207.219 15.484  1.00 34.48  ? 6   CYS D SG  1 
ATOM   3408  N  N   . VAL D  1 8   ? 10.274  205.717 13.736  1.00 33.08  ? 7   VAL D N   1 
ATOM   3409  C  CA  . VAL D  1 8   ? 10.489  205.874 12.281  1.00 29.36  ? 7   VAL D CA  1 
ATOM   3410  C  C   . VAL D  1 8   ? 9.184   206.316 11.656  1.00 28.87  ? 7   VAL D C   1 
ATOM   3411  O  O   . VAL D  1 8   ? 8.199   205.632 11.743  1.00 29.17  ? 7   VAL D O   1 
ATOM   3412  C  CB  . VAL D  1 8   ? 11.019  204.566 11.615  1.00 25.78  ? 7   VAL D CB  1 
ATOM   3413  C  CG1 . VAL D  1 8   ? 11.378  204.765 10.134  1.00 24.32  ? 7   VAL D CG1 1 
ATOM   3414  C  CG2 . VAL D  1 8   ? 12.227  204.025 12.325  1.00 24.80  ? 7   VAL D CG2 1 
ATOM   3415  N  N   . LEU D  1 9   ? 9.167   207.471 11.016  1.00 30.92  ? 8   LEU D N   1 
ATOM   3416  C  CA  . LEU D  1 9   ? 7.907   207.935 10.460  1.00 30.90  ? 8   LEU D CA  1 
ATOM   3417  C  C   . LEU D  1 9   ? 7.878   207.636 8.952   1.00 34.80  ? 8   LEU D C   1 
ATOM   3418  O  O   . LEU D  1 9   ? 8.841   207.921 8.257   1.00 36.51  ? 8   LEU D O   1 
ATOM   3419  C  CB  . LEU D  1 9   ? 7.714   209.391 10.730  1.00 28.45  ? 8   LEU D CB  1 
ATOM   3420  C  CG  . LEU D  1 9   ? 7.671   209.927 12.145  1.00 32.95  ? 8   LEU D CG  1 
ATOM   3421  C  CD1 . LEU D  1 9   ? 8.043   211.374 12.095  1.00 39.99  ? 8   LEU D CD1 1 
ATOM   3422  C  CD2 . LEU D  1 9   ? 6.279   209.930 12.626  1.00 30.14  ? 8   LEU D CD2 1 
ATOM   3423  N  N   . LYS D  1 10  ? 6.776   207.048 8.482   1.00 34.34  ? 9   LYS D N   1 
ATOM   3424  C  CA  . LYS D  1 10  ? 6.594   206.681 7.089   1.00 36.27  ? 9   LYS D CA  1 
ATOM   3425  C  C   . LYS D  1 10  ? 5.219   207.014 6.684   1.00 36.22  ? 9   LYS D C   1 
ATOM   3426  O  O   . LYS D  1 10  ? 4.286   207.041 7.518   1.00 34.00  ? 9   LYS D O   1 
ATOM   3427  C  CB  . LYS D  1 10  ? 6.795   205.197 6.833   1.00 37.49  ? 9   LYS D CB  1 
ATOM   3428  C  CG  . LYS D  1 10  ? 8.229   204.803 6.981   1.00 46.01  ? 9   LYS D CG  1 
ATOM   3429  C  CD  . LYS D  1 10  ? 8.582   203.536 6.222   1.00 52.52  ? 9   LYS D CD  1 
ATOM   3430  C  CE  . LYS D  1 10  ? 9.524   202.668 7.077   1.00 58.09  ? 9   LYS D CE  1 
ATOM   3431  N  NZ  . LYS D  1 10  ? 10.867  202.520 6.457   1.00 53.61  ? 9   LYS D NZ  1 
ATOM   3432  N  N   . GLY D  1 11  ? 5.089   207.286 5.391   1.00 35.53  ? 10  GLY D N   1 
ATOM   3433  C  CA  . GLY D  1 11  ? 3.789   207.497 4.840   1.00 38.04  ? 10  GLY D CA  1 
ATOM   3434  C  C   . GLY D  1 11  ? 3.681   207.011 3.418   1.00 40.16  ? 10  GLY D C   1 
ATOM   3435  O  O   . GLY D  1 11  ? 4.572   206.319 2.909   1.00 37.00  ? 10  GLY D O   1 
ATOM   3436  N  N   . ASP D  1 12  ? 2.567   207.391 2.786   1.00 40.92  ? 11  ASP D N   1 
ATOM   3437  C  CA  . ASP D  1 12  ? 2.347   207.094 1.358   1.00 46.98  ? 11  ASP D CA  1 
ATOM   3438  C  C   . ASP D  1 12  ? 2.956   208.083 0.416   1.00 43.74  ? 11  ASP D C   1 
ATOM   3439  O  O   . ASP D  1 12  ? 2.928   207.816 -0.725  1.00 53.29  ? 11  ASP D O   1 
ATOM   3440  C  CB  . ASP D  1 12  ? 0.851   206.998 0.975   1.00 43.46  ? 11  ASP D CB  1 
ATOM   3441  C  CG  . ASP D  1 12  ? 0.158   205.891 1.680   1.00 50.25  ? 11  ASP D CG  1 
ATOM   3442  O  OD1 . ASP D  1 12  ? 0.754   204.747 1.775   1.00 46.79  ? 11  ASP D OD1 1 
ATOM   3443  O  OD2 . ASP D  1 12  ? -0.965  206.198 2.175   1.00 49.22  ? 11  ASP D OD2 1 
ATOM   3444  N  N   . GLY D  1 13  ? 3.448   209.224 0.855   1.00 39.43  ? 12  GLY D N   1 
ATOM   3445  C  CA  . GLY D  1 13  ? 3.984   210.210 -0.081  1.00 36.67  ? 12  GLY D CA  1 
ATOM   3446  C  C   . GLY D  1 13  ? 5.432   210.389 0.278   1.00 37.58  ? 12  GLY D C   1 
ATOM   3447  O  O   . GLY D  1 13  ? 6.124   209.432 0.713   1.00 40.71  ? 12  GLY D O   1 
ATOM   3448  N  N   . PRO D  1 14  ? 5.909   211.611 0.144   1.00 34.62  ? 13  PRO D N   1 
ATOM   3449  C  CA  . PRO D  1 14  ? 7.335   211.760 0.370   1.00 31.24  ? 13  PRO D CA  1 
ATOM   3450  C  C   . PRO D  1 14  ? 7.784   211.959 1.831   1.00 28.04  ? 13  PRO D C   1 
ATOM   3451  O  O   . PRO D  1 14  ? 8.985   211.968 2.071   1.00 30.10  ? 13  PRO D O   1 
ATOM   3452  C  CB  . PRO D  1 14  ? 7.666   212.992 -0.488  1.00 27.66  ? 13  PRO D CB  1 
ATOM   3453  C  CG  . PRO D  1 14  ? 6.445   213.798 -0.373  1.00 29.50  ? 13  PRO D CG  1 
ATOM   3454  C  CD  . PRO D  1 14  ? 5.285   212.839 -0.374  1.00 32.54  ? 13  PRO D CD  1 
ATOM   3455  N  N   . VAL D  1 15  ? 6.872   212.217 2.765   1.00 29.03  ? 14  VAL D N   1 
ATOM   3456  C  CA  . VAL D  1 15  ? 7.206   212.571 4.165   1.00 27.78  ? 14  VAL D CA  1 
ATOM   3457  C  C   . VAL D  1 15  ? 7.772   211.364 4.874   1.00 27.72  ? 14  VAL D C   1 
ATOM   3458  O  O   . VAL D  1 15  ? 7.114   210.325 4.909   1.00 26.37  ? 14  VAL D O   1 
ATOM   3459  C  CB  . VAL D  1 15  ? 5.999   213.071 4.992   1.00 25.22  ? 14  VAL D CB  1 
ATOM   3460  C  CG1 . VAL D  1 15  ? 6.414   213.338 6.451   1.00 21.63  ? 14  VAL D CG1 1 
ATOM   3461  C  CG2 . VAL D  1 15  ? 5.400   214.290 4.376   1.00 23.06  ? 14  VAL D CG2 1 
ATOM   3462  N  N   . GLN D  1 16  ? 8.991   211.492 5.402   1.00 28.17  ? 15  GLN D N   1 
ATOM   3463  C  CA  . GLN D  1 16  ? 9.575   210.395 6.234   1.00 32.52  ? 15  GLN D CA  1 
ATOM   3464  C  C   . GLN D  1 16  ? 10.653  210.932 7.159   1.00 29.94  ? 15  GLN D C   1 
ATOM   3465  O  O   . GLN D  1 16  ? 11.252  211.950 6.832   1.00 28.75  ? 15  GLN D O   1 
ATOM   3466  C  CB  . GLN D  1 16  ? 10.184  209.294 5.398   1.00 35.79  ? 15  GLN D CB  1 
ATOM   3467  C  CG  . GLN D  1 16  ? 11.171  209.843 4.429   1.00 39.36  ? 15  GLN D CG  1 
ATOM   3468  C  CD  . GLN D  1 16  ? 12.097  208.796 3.876   1.00 56.54  ? 15  GLN D CD  1 
ATOM   3469  O  OE1 . GLN D  1 16  ? 11.739  208.123 2.913   1.00 55.37  ? 15  GLN D OE1 1 
ATOM   3470  N  NE2 . GLN D  1 16  ? 13.326  208.653 4.475   1.00 56.52  ? 15  GLN D NE2 1 
ATOM   3471  N  N   . GLY D  1 17  ? 10.858  210.274 8.301   1.00 26.71  ? 16  GLY D N   1 
ATOM   3472  C  CA  . GLY D  1 17  ? 11.968  210.631 9.148   1.00 25.69  ? 16  GLY D CA  1 
ATOM   3473  C  C   . GLY D  1 17  ? 12.130  209.839 10.423  1.00 25.88  ? 16  GLY D C   1 
ATOM   3474  O  O   . GLY D  1 17  ? 11.468  208.838 10.596  1.00 27.78  ? 16  GLY D O   1 
ATOM   3475  N  N   . ILE D  1 18  ? 13.060  210.267 11.279  1.00 27.48  ? 17  ILE D N   1 
ATOM   3476  C  CA  . ILE D  1 18  ? 13.398  209.531 12.443  1.00 29.69  ? 17  ILE D CA  1 
ATOM   3477  C  C   . ILE D  1 18  ? 13.276  210.485 13.633  1.00 35.47  ? 17  ILE D C   1 
ATOM   3478  O  O   . ILE D  1 18  ? 13.874  211.553 13.619  1.00 36.84  ? 17  ILE D O   1 
ATOM   3479  C  CB  . ILE D  1 18  ? 14.749  208.874 12.327  1.00 31.18  ? 17  ILE D CB  1 
ATOM   3480  C  CG1 . ILE D  1 18  ? 14.738  207.809 11.236  1.00 29.52  ? 17  ILE D CG1 1 
ATOM   3481  C  CG2 . ILE D  1 18  ? 15.176  208.280 13.677  1.00 30.19  ? 17  ILE D CG2 1 
ATOM   3482  C  CD1 . ILE D  1 18  ? 16.087  207.195 10.987  1.00 25.02  ? 17  ILE D CD1 1 
ATOM   3483  N  N   . ILE D  1 19  ? 12.437  210.154 14.621  1.00 31.68  ? 18  ILE D N   1 
ATOM   3484  C  CA  . ILE D  1 19  ? 12.332  211.014 15.817  1.00 29.08  ? 18  ILE D CA  1 
ATOM   3485  C  C   . ILE D  1 19  ? 12.865  210.325 17.095  1.00 28.14  ? 18  ILE D C   1 
ATOM   3486  O  O   . ILE D  1 19  ? 12.511  209.188 17.412  1.00 24.82  ? 18  ILE D O   1 
ATOM   3487  C  CB  . ILE D  1 19  ? 10.912  211.620 15.962  1.00 27.27  ? 18  ILE D CB  1 
ATOM   3488  C  CG1 . ILE D  1 19  ? 10.587  212.514 14.762  1.00 26.90  ? 18  ILE D CG1 1 
ATOM   3489  C  CG2 . ILE D  1 19  ? 10.699  212.350 17.319  1.00 25.89  ? 18  ILE D CG2 1 
ATOM   3490  C  CD1 . ILE D  1 19  ? 11.435  213.781 14.607  1.00 26.93  ? 18  ILE D CD1 1 
ATOM   3491  N  N   . ASN D  1 20  ? 13.739  211.016 17.805  1.00 29.67  ? 19  ASN D N   1 
ATOM   3492  C  CA  . ASN D  1 20  ? 14.283  210.480 19.077  1.00 29.18  ? 19  ASN D CA  1 
ATOM   3493  C  C   . ASN D  1 20  ? 13.675  211.093 20.315  1.00 25.49  ? 19  ASN D C   1 
ATOM   3494  O  O   . ASN D  1 20  ? 13.244  212.201 20.264  1.00 25.97  ? 19  ASN D O   1 
ATOM   3495  C  CB  . ASN D  1 20  ? 15.781  210.612 19.141  1.00 30.22  ? 19  ASN D CB  1 
ATOM   3496  C  CG  . ASN D  1 20  ? 16.451  210.046 17.927  1.00 30.96  ? 19  ASN D CG  1 
ATOM   3497  O  OD1 . ASN D  1 20  ? 16.767  210.773 17.006  1.00 32.34  ? 19  ASN D OD1 1 
ATOM   3498  N  ND2 . ASN D  1 20  ? 16.667  208.773 17.913  1.00 31.33  ? 19  ASN D ND2 1 
ATOM   3499  N  N   . PHE D  1 21  ? 13.547  210.303 21.365  1.00 25.67  ? 20  PHE D N   1 
ATOM   3500  C  CA  . PHE D  1 21  ? 13.058  210.719 22.623  1.00 27.65  ? 20  PHE D CA  1 
ATOM   3501  C  C   . PHE D  1 21  ? 14.043  210.348 23.688  1.00 29.36  ? 20  PHE D C   1 
ATOM   3502  O  O   . PHE D  1 21  ? 14.561  209.215 23.728  1.00 31.02  ? 20  PHE D O   1 
ATOM   3503  C  CB  . PHE D  1 21  ? 11.776  210.011 22.979  1.00 26.24  ? 20  PHE D CB  1 
ATOM   3504  C  CG  . PHE D  1 21  ? 10.683  210.301 22.082  1.00 29.06  ? 20  PHE D CG  1 
ATOM   3505  C  CD1 . PHE D  1 21  ? 10.537  209.572 20.880  1.00 30.53  ? 20  PHE D CD1 1 
ATOM   3506  C  CD2 . PHE D  1 21  ? 9.826   211.331 22.345  1.00 28.35  ? 20  PHE D CD2 1 
ATOM   3507  C  CE1 . PHE D  1 21  ? 9.526   209.871 19.995  1.00 26.14  ? 20  PHE D CE1 1 
ATOM   3508  C  CE2 . PHE D  1 21  ? 8.780   211.599 21.476  1.00 28.00  ? 20  PHE D CE2 1 
ATOM   3509  C  CZ  . PHE D  1 21  ? 8.622   210.867 20.324  1.00 27.60  ? 20  PHE D CZ  1 
ATOM   3510  N  N   . GLU D  1 22  ? 14.179  211.278 24.616  1.00 30.87  ? 21  GLU D N   1 
ATOM   3511  C  CA  . GLU D  1 22  ? 15.023  211.116 25.796  1.00 33.81  ? 21  GLU D CA  1 
ATOM   3512  C  C   . GLU D  1 22  ? 14.468  211.740 27.109  1.00 32.81  ? 21  GLU D C   1 
ATOM   3513  O  O   . GLU D  1 22  ? 14.218  212.936 27.204  1.00 33.81  ? 21  GLU D O   1 
ATOM   3514  C  CB  . GLU D  1 22  ? 16.423  211.639 25.519  1.00 31.99  ? 21  GLU D CB  1 
ATOM   3515  C  CG  . GLU D  1 22  ? 17.371  211.090 26.537  1.00 40.06  ? 21  GLU D CG  1 
ATOM   3516  C  CD  . GLU D  1 22  ? 18.745  211.713 26.442  1.00 50.13  ? 21  GLU D CD  1 
ATOM   3517  O  OE1 . GLU D  1 22  ? 18.847  212.975 26.313  1.00 52.27  ? 21  GLU D OE1 1 
ATOM   3518  O  OE2 . GLU D  1 22  ? 19.714  210.915 26.491  1.00 48.06  ? 21  GLU D OE2 1 
ATOM   3519  N  N   . GLN D  1 23  ? 14.361  210.905 28.125  1.00 32.15  ? 22  GLN D N   1 
ATOM   3520  C  CA  . GLN D  1 23  ? 13.919  211.334 29.424  1.00 34.25  ? 22  GLN D CA  1 
ATOM   3521  C  C   . GLN D  1 23  ? 14.887  210.828 30.491  1.00 33.85  ? 22  GLN D C   1 
ATOM   3522  O  O   . GLN D  1 23  ? 14.734  209.775 30.993  1.00 32.76  ? 22  GLN D O   1 
ATOM   3523  C  CB  . GLN D  1 23  ? 12.501  210.801 29.667  1.00 31.10  ? 22  GLN D CB  1 
ATOM   3524  C  CG  . GLN D  1 23  ? 11.811  211.514 30.786  1.00 30.81  ? 22  GLN D CG  1 
ATOM   3525  C  CD  . GLN D  1 23  ? 10.447  210.948 31.114  1.00 31.60  ? 22  GLN D CD  1 
ATOM   3526  O  OE1 . GLN D  1 23  ? 10.136  209.809 30.805  1.00 35.76  ? 22  GLN D OE1 1 
ATOM   3527  N  NE2 . GLN D  1 23  ? 9.608   211.757 31.700  1.00 30.78  ? 22  GLN D NE2 1 
ATOM   3528  N  N   . LYS D  1 24  ? 15.907  211.588 30.833  1.00 42.41  ? 23  LYS D N   1 
ATOM   3529  C  CA  . LYS D  1 24  ? 16.899  211.091 31.822  1.00 45.18  ? 23  LYS D CA  1 
ATOM   3530  C  C   . LYS D  1 24  ? 16.306  210.876 33.206  1.00 46.36  ? 23  LYS D C   1 
ATOM   3531  O  O   . LYS D  1 24  ? 16.783  210.006 33.911  1.00 48.59  ? 23  LYS D O   1 
ATOM   3532  C  CB  . LYS D  1 24  ? 18.086  212.042 32.012  1.00 48.47  ? 23  LYS D CB  1 
ATOM   3533  C  CG  . LYS D  1 24  ? 18.926  212.369 30.779  1.00 54.07  ? 23  LYS D CG  1 
ATOM   3534  C  CD  . LYS D  1 24  ? 19.510  213.802 30.911  1.00 61.43  ? 23  LYS D CD  1 
ATOM   3535  C  CE  . LYS D  1 24  ? 20.111  214.390 29.621  1.00 68.33  ? 23  LYS D CE  1 
ATOM   3536  N  NZ  . LYS D  1 24  ? 21.569  214.029 29.520  1.00 66.53  ? 23  LYS D NZ  1 
ATOM   3537  N  N   . GLU D  1 25  ? 15.293  211.636 33.619  1.00 41.78  ? 24  GLU D N   1 
ATOM   3538  C  CA  . GLU D  1 25  ? 14.678  211.356 34.914  1.00 42.10  ? 24  GLU D CA  1 
ATOM   3539  C  C   . GLU D  1 25  ? 13.203  211.180 34.724  1.00 41.74  ? 24  GLU D C   1 
ATOM   3540  O  O   . GLU D  1 25  ? 12.642  211.890 33.946  1.00 44.09  ? 24  GLU D O   1 
ATOM   3541  C  CB  . GLU D  1 25  ? 14.884  212.506 35.878  1.00 45.98  ? 24  GLU D CB  1 
ATOM   3542  C  CG  . GLU D  1 25  ? 16.264  213.133 36.040  1.00 51.78  ? 24  GLU D CG  1 
ATOM   3543  C  CD  . GLU D  1 25  ? 16.224  214.490 36.866  1.00 79.47  ? 24  GLU D CD  1 
ATOM   3544  O  OE1 . GLU D  1 25  ? 15.181  215.294 36.833  1.00 70.78  ? 24  GLU D OE1 1 
ATOM   3545  O  OE2 . GLU D  1 25  ? 17.256  214.796 37.589  1.00 78.06  ? 24  GLU D OE2 1 
ATOM   3546  N  N   . SER D  1 26  ? 12.546  210.298 35.469  1.00 40.80  ? 25  SER D N   1 
ATOM   3547  C  CA  . SER D  1 26  ? 11.101  210.014 35.224  1.00 41.98  ? 25  SER D CA  1 
ATOM   3548  C  C   . SER D  1 26  ? 10.144  211.178 35.568  1.00 40.37  ? 25  SER D C   1 
ATOM   3549  O  O   . SER D  1 26  ? 9.066   211.317 34.992  1.00 37.07  ? 25  SER D O   1 
ATOM   3550  C  CB  . SER D  1 26  ? 10.649  208.750 35.969  1.00 45.72  ? 25  SER D CB  1 
ATOM   3551  O  OG  . SER D  1 26  ? 10.985  208.771 37.357  1.00 52.84  ? 25  SER D OG  1 
ATOM   3552  N  N   . ASN D  1 27  ? 10.548  212.024 36.497  1.00 38.38  ? 26  ASN D N   1 
ATOM   3553  C  CA  . ASN D  1 27  ? 9.773   213.245 36.767  1.00 48.05  ? 26  ASN D CA  1 
ATOM   3554  C  C   . ASN D  1 27  ? 10.257  214.451 35.905  1.00 47.02  ? 26  ASN D C   1 
ATOM   3555  O  O   . ASN D  1 27  ? 10.073  215.600 36.327  1.00 52.40  ? 26  ASN D O   1 
ATOM   3556  C  CB  . ASN D  1 27  ? 9.955   213.630 38.249  1.00 49.69  ? 26  ASN D CB  1 
ATOM   3557  C  CG  . ASN D  1 27  ? 11.404  214.111 38.553  1.00 53.22  ? 26  ASN D CG  1 
ATOM   3558  O  OD1 . ASN D  1 27  ? 12.401  213.600 38.011  1.00 54.72  ? 26  ASN D OD1 1 
ATOM   3559  N  ND2 . ASN D  1 27  ? 11.515  215.078 39.420  1.00 51.49  ? 26  ASN D ND2 1 
ATOM   3560  N  N   . GLY D  1 28  ? 10.918  214.199 34.766  1.00 44.13  ? 27  GLY D N   1 
ATOM   3561  C  CA  . GLY D  1 28  ? 11.622  215.257 34.049  1.00 43.90  ? 27  GLY D CA  1 
ATOM   3562  C  C   . GLY D  1 28  ? 11.088  215.344 32.661  1.00 38.62  ? 27  GLY D C   1 
ATOM   3563  O  O   . GLY D  1 28  ? 10.351  214.508 32.230  1.00 42.70  ? 27  GLY D O   1 
ATOM   3564  N  N   . PRO D  1 29  ? 11.471  216.360 31.948  1.00 39.19  ? 28  PRO D N   1 
ATOM   3565  C  CA  . PRO D  1 29  ? 10.956  216.556 30.594  1.00 35.92  ? 28  PRO D CA  1 
ATOM   3566  C  C   . PRO D  1 29  ? 11.537  215.583 29.606  1.00 37.41  ? 28  PRO D C   1 
ATOM   3567  O  O   . PRO D  1 29  ? 12.624  214.981 29.834  1.00 37.50  ? 28  PRO D O   1 
ATOM   3568  C  CB  . PRO D  1 29  ? 11.445  217.936 30.237  1.00 37.94  ? 28  PRO D CB  1 
ATOM   3569  C  CG  . PRO D  1 29  ? 12.461  218.351 31.290  1.00 33.08  ? 28  PRO D CG  1 
ATOM   3570  C  CD  . PRO D  1 29  ? 12.447  217.373 32.384  1.00 35.25  ? 28  PRO D CD  1 
ATOM   3571  N  N   . VAL D  1 30  ? 10.808  215.428 28.513  1.00 31.78  ? 29  VAL D N   1 
ATOM   3572  C  CA  . VAL D  1 30  ? 11.271  214.614 27.430  1.00 30.70  ? 29  VAL D CA  1 
ATOM   3573  C  C   . VAL D  1 30  ? 11.854  215.503 26.323  1.00 28.10  ? 29  VAL D C   1 
ATOM   3574  O  O   . VAL D  1 30  ? 11.203  216.410 25.867  1.00 26.08  ? 29  VAL D O   1 
ATOM   3575  C  CB  . VAL D  1 30  ? 10.107  213.715 26.896  1.00 29.72  ? 29  VAL D CB  1 
ATOM   3576  C  CG1 . VAL D  1 30  ? 10.647  212.714 25.894  1.00 26.04  ? 29  VAL D CG1 1 
ATOM   3577  C  CG2 . VAL D  1 30  ? 9.396   212.974 28.059  1.00 25.66  ? 29  VAL D CG2 1 
ATOM   3578  N  N   . LYS D  1 31  ? 13.071  215.226 25.915  1.00 27.22  ? 30  LYS D N   1 
ATOM   3579  C  CA  . LYS D  1 31  ? 13.598  215.810 24.710  1.00 32.16  ? 30  LYS D CA  1 
ATOM   3580  C  C   . LYS D  1 31  ? 13.166  215.016 23.473  1.00 31.99  ? 30  LYS D C   1 
ATOM   3581  O  O   . LYS D  1 31  ? 13.236  213.805 23.483  1.00 31.28  ? 30  LYS D O   1 
ATOM   3582  C  CB  . LYS D  1 31  ? 15.100  215.891 24.726  1.00 36.15  ? 30  LYS D CB  1 
ATOM   3583  C  CG  . LYS D  1 31  ? 15.593  216.402 26.056  1.00 54.12  ? 30  LYS D CG  1 
ATOM   3584  C  CD  . LYS D  1 31  ? 16.218  217.800 26.006  1.00 63.89  ? 30  LYS D CD  1 
ATOM   3585  C  CE  . LYS D  1 31  ? 17.127  217.989 27.244  1.00 70.25  ? 30  LYS D CE  1 
ATOM   3586  N  NZ  . LYS D  1 31  ? 18.265  216.987 27.422  1.00 71.50  ? 30  LYS D NZ  1 
ATOM   3587  N  N   . VAL D  1 32  ? 12.675  215.732 22.455  1.00 29.24  ? 31  VAL D N   1 
ATOM   3588  C  CA  . VAL D  1 32  ? 12.204  215.163 21.224  1.00 29.85  ? 31  VAL D CA  1 
ATOM   3589  C  C   . VAL D  1 32  ? 12.990  215.837 20.098  1.00 32.15  ? 31  VAL D C   1 
ATOM   3590  O  O   . VAL D  1 32  ? 12.898  217.065 19.925  1.00 37.54  ? 31  VAL D O   1 
ATOM   3591  C  CB  . VAL D  1 32  ? 10.728  215.460 21.003  1.00 26.42  ? 31  VAL D CB  1 
ATOM   3592  C  CG1 . VAL D  1 32  ? 10.247  214.611 19.875  1.00 24.60  ? 31  VAL D CG1 1 
ATOM   3593  C  CG2 . VAL D  1 32  ? 9.884   215.217 22.251  1.00 23.78  ? 31  VAL D CG2 1 
ATOM   3594  N  N   . TRP D  1 33  ? 13.789  215.068 19.368  1.00 27.74  ? 32  TRP D N   1 
ATOM   3595  C  CA  . TRP D  1 33  ? 14.532  215.624 18.282  1.00 27.51  ? 32  TRP D CA  1 
ATOM   3596  C  C   . TRP D  1 33  ? 14.727  214.626 17.108  1.00 25.78  ? 32  TRP D C   1 
ATOM   3597  O  O   . TRP D  1 33  ? 14.662  213.418 17.265  1.00 28.13  ? 32  TRP D O   1 
ATOM   3598  C  CB  . TRP D  1 33  ? 15.836  216.269 18.816  1.00 25.71  ? 32  TRP D CB  1 
ATOM   3599  C  CG  . TRP D  1 33  ? 16.886  215.256 19.045  1.00 29.21  ? 32  TRP D CG  1 
ATOM   3600  C  CD1 . TRP D  1 33  ? 17.877  214.927 18.179  1.00 28.11  ? 32  TRP D CD1 1 
ATOM   3601  C  CD2 . TRP D  1 33  ? 16.952  214.320 20.102  1.00 29.11  ? 32  TRP D CD2 1 
ATOM   3602  N  NE1 . TRP D  1 33  ? 18.610  213.888 18.656  1.00 32.69  ? 32  TRP D NE1 1 
ATOM   3603  C  CE2 . TRP D  1 33  ? 18.088  213.483 19.841  1.00 33.73  ? 32  TRP D CE2 1 
ATOM   3604  C  CE3 . TRP D  1 33  ? 16.199  214.114 21.251  1.00 30.12  ? 32  TRP D CE3 1 
ATOM   3605  C  CZ2 . TRP D  1 33  ? 18.514  212.434 20.703  1.00 34.62  ? 32  TRP D CZ2 1 
ATOM   3606  C  CZ3 . TRP D  1 33  ? 16.600  213.076 22.142  1.00 38.59  ? 32  TRP D CZ3 1 
ATOM   3607  C  CH2 . TRP D  1 33  ? 17.759  212.210 21.842  1.00 36.56  ? 32  TRP D CH2 1 
ATOM   3608  N  N   . GLY D  1 34  ? 14.974  215.146 15.948  1.00 24.96  ? 33  GLY D N   1 
ATOM   3609  C  CA  . GLY D  1 34  ? 15.342  214.342 14.801  1.00 26.67  ? 33  GLY D CA  1 
ATOM   3610  C  C   . GLY D  1 34  ? 15.005  215.135 13.545  1.00 28.14  ? 33  GLY D C   1 
ATOM   3611  O  O   . GLY D  1 34  ? 14.943  216.313 13.531  1.00 29.66  ? 33  GLY D O   1 
ATOM   3612  N  N   . SER D  1 35  ? 14.719  214.465 12.471  1.00 34.43  ? 34  SER D N   1 
ATOM   3613  C  CA  . SER D  1 35  ? 14.641  215.111 11.178  1.00 33.76  ? 34  SER D CA  1 
ATOM   3614  C  C   . SER D  1 35  ? 13.552  214.447 10.395  1.00 33.06  ? 34  SER D C   1 
ATOM   3615  O  O   . SER D  1 35  ? 13.503  213.210 10.323  1.00 35.91  ? 34  SER D O   1 
ATOM   3616  C  CB  . SER D  1 35  ? 15.952  214.851 10.501  1.00 33.95  ? 34  SER D CB  1 
ATOM   3617  O  OG  . SER D  1 35  ? 16.045  215.693 9.446   1.00 42.86  ? 34  SER D OG  1 
ATOM   3618  N  N   . ILE D  1 36  ? 12.690  215.239 9.802   1.00 30.75  ? 35  ILE D N   1 
ATOM   3619  C  CA  . ILE D  1 36  ? 11.665  214.692 8.946   1.00 32.53  ? 35  ILE D CA  1 
ATOM   3620  C  C   . ILE D  1 36  ? 11.830  215.412 7.602   1.00 34.28  ? 35  ILE D C   1 
ATOM   3621  O  O   . ILE D  1 36  ? 11.954  216.622 7.614   1.00 38.75  ? 35  ILE D O   1 
ATOM   3622  C  CB  . ILE D  1 36  ? 10.256  214.957 9.526   1.00 34.38  ? 35  ILE D CB  1 
ATOM   3623  C  CG1 . ILE D  1 36  ? 10.085  214.372 10.915  1.00 32.63  ? 35  ILE D CG1 1 
ATOM   3624  C  CG2 . ILE D  1 36  ? 9.163   214.380 8.659   1.00 29.57  ? 35  ILE D CG2 1 
ATOM   3625  C  CD1 . ILE D  1 36  ? 9.049   215.137 11.699  1.00 32.91  ? 35  ILE D CD1 1 
ATOM   3626  N  N   . LYS D  1 37  ? 11.888  214.707 6.472   1.00 31.23  ? 36  LYS D N   1 
ATOM   3627  C  CA  . LYS D  1 37  ? 11.970  215.396 5.189   1.00 31.38  ? 36  LYS D CA  1 
ATOM   3628  C  C   . LYS D  1 37  ? 10.667  215.245 4.425   1.00 31.07  ? 36  LYS D C   1 
ATOM   3629  O  O   . LYS D  1 37  ? 9.785   214.453 4.816   1.00 32.78  ? 36  LYS D O   1 
ATOM   3630  C  CB  . LYS D  1 37  ? 13.207  214.992 4.352   1.00 32.49  ? 36  LYS D CB  1 
ATOM   3631  C  CG  . LYS D  1 37  ? 13.261  213.495 4.093   1.00 37.01  ? 36  LYS D CG  1 
ATOM   3632  C  CD  . LYS D  1 37  ? 13.774  213.055 2.742   1.00 40.68  ? 36  LYS D CD  1 
ATOM   3633  C  CE  . LYS D  1 37  ? 13.011  211.818 2.202   1.00 46.89  ? 36  LYS D CE  1 
ATOM   3634  N  NZ  . LYS D  1 37  ? 11.815  211.975 1.189   1.00 41.29  ? 36  LYS D NZ  1 
ATOM   3635  N  N   . GLY D  1 38  ? 10.544  216.024 3.349   1.00 32.33  ? 37  GLY D N   1 
ATOM   3636  C  CA  . GLY D  1 38  ? 9.419   215.895 2.396   1.00 31.49  ? 37  GLY D CA  1 
ATOM   3637  C  C   . GLY D  1 38  ? 8.176   216.678 2.746   1.00 30.11  ? 37  GLY D C   1 
ATOM   3638  O  O   . GLY D  1 38  ? 7.129   216.424 2.228   1.00 29.90  ? 37  GLY D O   1 
ATOM   3639  N  N   . LEU D  1 39  ? 8.316   217.603 3.688   1.00 32.82  ? 38  LEU D N   1 
ATOM   3640  C  CA  . LEU D  1 39  ? 7.248   218.439 4.180   1.00 29.74  ? 38  LEU D CA  1 
ATOM   3641  C  C   . LEU D  1 39  ? 7.285   219.756 3.454   1.00 29.62  ? 38  LEU D C   1 
ATOM   3642  O  O   . LEU D  1 39  ? 8.383   220.306 3.181   1.00 28.75  ? 38  LEU D O   1 
ATOM   3643  C  CB  . LEU D  1 39  ? 7.380   218.674 5.674   1.00 29.14  ? 38  LEU D CB  1 
ATOM   3644  C  CG  . LEU D  1 39  ? 7.203   217.496 6.665   1.00 33.64  ? 38  LEU D CG  1 
ATOM   3645  C  CD1 . LEU D  1 39  ? 7.791   217.832 8.029   1.00 27.80  ? 38  LEU D CD1 1 
ATOM   3646  C  CD2 . LEU D  1 39  ? 5.741   217.072 6.821   1.00 29.10  ? 38  LEU D CD2 1 
ATOM   3647  N  N   . THR D  1 40  ? 6.100   220.245 3.112   1.00 26.23  ? 39  THR D N   1 
ATOM   3648  C  CA  . THR D  1 40  ? 5.996   221.615 2.674   1.00 30.29  ? 39  THR D CA  1 
ATOM   3649  C  C   . THR D  1 40  ? 6.484   222.608 3.728   1.00 31.50  ? 39  THR D C   1 
ATOM   3650  O  O   . THR D  1 40  ? 6.287   222.445 4.966   1.00 35.38  ? 39  THR D O   1 
ATOM   3651  C  CB  . THR D  1 40  ? 4.582   222.013 2.308   1.00 27.42  ? 39  THR D CB  1 
ATOM   3652  O  OG1 . THR D  1 40  ? 3.851   222.024 3.503   1.00 33.17  ? 39  THR D OG1 1 
ATOM   3653  C  CG2 . THR D  1 40  ? 3.945   221.027 1.321   1.00 25.58  ? 39  THR D CG2 1 
ATOM   3654  N  N   . GLU D  1 41  ? 7.083   223.659 3.216   1.00 32.47  ? 40  GLU D N   1 
ATOM   3655  C  CA  . GLU D  1 41  ? 7.635   224.721 4.033   1.00 34.38  ? 40  GLU D CA  1 
ATOM   3656  C  C   . GLU D  1 41  ? 6.624   225.327 5.005   1.00 29.54  ? 40  GLU D C   1 
ATOM   3657  O  O   . GLU D  1 41  ? 5.506   225.611 4.638   1.00 29.89  ? 40  GLU D O   1 
ATOM   3658  C  CB  . GLU D  1 41  ? 8.227   225.803 3.144   1.00 34.02  ? 40  GLU D CB  1 
ATOM   3659  C  CG  . GLU D  1 41  ? 9.006   226.745 3.995   1.00 40.16  ? 40  GLU D CG  1 
ATOM   3660  C  CD  . GLU D  1 41  ? 9.775   227.822 3.252   1.00 49.59  ? 40  GLU D CD  1 
ATOM   3661  O  OE1 . GLU D  1 41  ? 9.879   227.792 1.990   1.00 48.32  ? 40  GLU D OE1 1 
ATOM   3662  O  OE2 . GLU D  1 41  ? 10.295  228.722 3.980   1.00 51.66  ? 40  GLU D OE2 1 
ATOM   3663  N  N   . GLY D  1 42  ? 7.067   225.518 6.236   1.00 26.52  ? 41  GLY D N   1 
ATOM   3664  C  CA  . GLY D  1 42  ? 6.224   226.003 7.257   1.00 25.79  ? 41  GLY D CA  1 
ATOM   3665  C  C   . GLY D  1 42  ? 5.773   224.976 8.268   1.00 26.86  ? 41  GLY D C   1 
ATOM   3666  O  O   . GLY D  1 42  ? 6.395   223.941 8.452   1.00 29.39  ? 41  GLY D O   1 
ATOM   3667  N  N   . LEU D  1 43  ? 4.659   225.271 8.902   1.00 29.46  ? 42  LEU D N   1 
ATOM   3668  C  CA  . LEU D  1 43  ? 4.258   224.633 10.138  1.00 31.25  ? 42  LEU D CA  1 
ATOM   3669  C  C   . LEU D  1 43  ? 3.426   223.386 9.900   1.00 31.28  ? 42  LEU D C   1 
ATOM   3670  O  O   . LEU D  1 43  ? 2.556   223.397 9.013   1.00 32.73  ? 42  LEU D O   1 
ATOM   3671  C  CB  . LEU D  1 43  ? 3.509   225.656 10.989  1.00 30.19  ? 42  LEU D CB  1 
ATOM   3672  C  CG  . LEU D  1 43  ? 4.229   226.892 11.590  1.00 27.33  ? 42  LEU D CG  1 
ATOM   3673  C  CD1 . LEU D  1 43  ? 3.166   227.875 12.120  1.00 26.82  ? 42  LEU D CD1 1 
ATOM   3674  C  CD2 . LEU D  1 43  ? 5.109   226.490 12.743  1.00 29.09  ? 42  LEU D CD2 1 
ATOM   3675  N  N   . HIS D  1 44  ? 3.721   222.323 10.673  1.00 28.46  ? 43  HIS D N   1 
ATOM   3676  C  CA  . HIS D  1 44  ? 3.002   221.046 10.604  1.00 25.95  ? 43  HIS D CA  1 
ATOM   3677  C  C   . HIS D  1 44  ? 2.691   220.552 12.008  1.00 26.96  ? 43  HIS D C   1 
ATOM   3678  O  O   . HIS D  1 44  ? 3.613   220.444 12.841  1.00 26.51  ? 43  HIS D O   1 
ATOM   3679  C  CB  . HIS D  1 44  ? 3.835   220.005 9.866   1.00 23.75  ? 43  HIS D CB  1 
ATOM   3680  C  CG  . HIS D  1 44  ? 4.077   220.335 8.431   1.00 27.49  ? 43  HIS D CG  1 
ATOM   3681  N  ND1 . HIS D  1 44  ? 3.205   219.976 7.424   1.00 27.05  ? 43  HIS D ND1 1 
ATOM   3682  C  CD2 . HIS D  1 44  ? 5.072   221.049 7.841   1.00 28.73  ? 43  HIS D CD2 1 
ATOM   3683  C  CE1 . HIS D  1 44  ? 3.665   220.446 6.277   1.00 30.84  ? 43  HIS D CE1 1 
ATOM   3684  N  NE2 . HIS D  1 44  ? 4.804   221.094 6.502   1.00 30.85  ? 43  HIS D NE2 1 
ATOM   3685  N  N   . GLY D  1 45  ? 1.410   220.234 12.265  1.00 25.04  ? 44  GLY D N   1 
ATOM   3686  C  CA  . GLY D  1 45  ? 0.966   219.650 13.552  1.00 26.34  ? 44  GLY D CA  1 
ATOM   3687  C  C   . GLY D  1 45  ? 1.745   218.368 13.802  1.00 26.63  ? 44  GLY D C   1 
ATOM   3688  O  O   . GLY D  1 45  ? 2.023   217.628 12.868  1.00 27.42  ? 44  GLY D O   1 
ATOM   3689  N  N   . PHE D  1 46  ? 2.125   218.140 15.047  1.00 27.03  ? 45  PHE D N   1 
ATOM   3690  C  CA  . PHE D  1 46  ? 3.031   217.087 15.447  1.00 28.73  ? 45  PHE D CA  1 
ATOM   3691  C  C   . PHE D  1 46  ? 2.459   216.501 16.755  1.00 30.36  ? 45  PHE D C   1 
ATOM   3692  O  O   . PHE D  1 46  ? 2.530   217.142 17.792  1.00 31.10  ? 45  PHE D O   1 
ATOM   3693  C  CB  . PHE D  1 46  ? 4.387   217.717 15.640  1.00 26.87  ? 45  PHE D CB  1 
ATOM   3694  C  CG  . PHE D  1 46  ? 5.490   216.777 15.860  1.00 26.17  ? 45  PHE D CG  1 
ATOM   3695  C  CD1 . PHE D  1 46  ? 5.868   215.924 14.889  1.00 25.69  ? 45  PHE D CD1 1 
ATOM   3696  C  CD2 . PHE D  1 46  ? 6.206   216.779 17.077  1.00 24.62  ? 45  PHE D CD2 1 
ATOM   3697  C  CE1 . PHE D  1 46  ? 6.972   215.098 15.072  1.00 24.99  ? 45  PHE D CE1 1 
ATOM   3698  C  CE2 . PHE D  1 46  ? 7.301   215.948 17.266  1.00 23.70  ? 45  PHE D CE2 1 
ATOM   3699  C  CZ  . PHE D  1 46  ? 7.697   215.125 16.243  1.00 24.21  ? 45  PHE D CZ  1 
ATOM   3700  N  N   . HIS D  1 47  ? 1.886   215.298 16.684  1.00 27.72  ? 46  HIS D N   1 
ATOM   3701  C  CA  . HIS D  1 47  ? 1.103   214.777 17.784  1.00 29.83  ? 46  HIS D CA  1 
ATOM   3702  C  C   . HIS D  1 47  ? 1.362   213.333 18.144  1.00 27.28  ? 46  HIS D C   1 
ATOM   3703  O  O   . HIS D  1 47  ? 1.552   212.475 17.245  1.00 28.39  ? 46  HIS D O   1 
ATOM   3704  C  CB  . HIS D  1 47  ? -0.399  214.962 17.489  1.00 29.59  ? 46  HIS D CB  1 
ATOM   3705  C  CG  . HIS D  1 47  ? -0.762  216.352 17.118  1.00 29.84  ? 46  HIS D CG  1 
ATOM   3706  N  ND1 . HIS D  1 47  ? -1.375  216.669 15.933  1.00 33.91  ? 46  HIS D ND1 1 
ATOM   3707  C  CD2 . HIS D  1 47  ? -0.522  217.524 17.737  1.00 27.59  ? 46  HIS D CD2 1 
ATOM   3708  C  CE1 . HIS D  1 47  ? -1.532  217.975 15.855  1.00 28.58  ? 46  HIS D CE1 1 
ATOM   3709  N  NE2 . HIS D  1 47  ? -0.993  218.516 16.928  1.00 27.22  ? 46  HIS D NE2 1 
ATOM   3710  N  N   . VAL D  1 48  ? 1.309   213.044 19.437  1.00 25.17  ? 47  VAL D N   1 
ATOM   3711  C  CA  . VAL D  1 48  ? 1.140   211.653 19.871  1.00 26.30  ? 47  VAL D CA  1 
ATOM   3712  C  C   . VAL D  1 48  ? -0.324  211.254 19.793  1.00 28.41  ? 47  VAL D C   1 
ATOM   3713  O  O   . VAL D  1 48  ? -1.167  211.920 20.388  1.00 29.37  ? 47  VAL D O   1 
ATOM   3714  C  CB  . VAL D  1 48  ? 1.767   211.373 21.210  1.00 26.10  ? 47  VAL D CB  1 
ATOM   3715  C  CG1 . VAL D  1 48  ? 1.561   209.931 21.561  1.00 21.80  ? 47  VAL D CG1 1 
ATOM   3716  C  CG2 . VAL D  1 48  ? 3.245   211.715 21.126  1.00 24.51  ? 47  VAL D CG2 1 
ATOM   3717  N  N   . HIS D  1 49  ? -0.634  210.229 18.986  1.00 27.09  ? 48  HIS D N   1 
ATOM   3718  C  CA  . HIS D  1 49  ? -1.997  209.749 18.911  1.00 27.62  ? 48  HIS D CA  1 
ATOM   3719  C  C   . HIS D  1 49  ? -2.152  208.486 19.777  1.00 27.23  ? 48  HIS D C   1 
ATOM   3720  O  O   . HIS D  1 49  ? -1.202  207.788 20.131  1.00 24.67  ? 48  HIS D O   1 
ATOM   3721  C  CB  . HIS D  1 49  ? -2.430  209.454 17.454  1.00 28.71  ? 48  HIS D CB  1 
ATOM   3722  C  CG  . HIS D  1 49  ? -2.659  210.655 16.596  1.00 26.38  ? 48  HIS D CG  1 
ATOM   3723  N  ND1 . HIS D  1 49  ? -3.857  210.879 15.963  1.00 24.26  ? 48  HIS D ND1 1 
ATOM   3724  C  CD2 . HIS D  1 49  ? -1.850  211.697 16.254  1.00 27.16  ? 48  HIS D CD2 1 
ATOM   3725  C  CE1 . HIS D  1 49  ? -3.792  212.022 15.285  1.00 23.38  ? 48  HIS D CE1 1 
ATOM   3726  N  NE2 . HIS D  1 49  ? -2.573  212.520 15.414  1.00 23.64  ? 48  HIS D NE2 1 
ATOM   3727  N  N   . GLU D  1 50  ? -3.392  208.170 20.058  1.00 30.89  ? 49  GLU D N   1 
ATOM   3728  C  CA  . GLU D  1 50  ? -3.684  207.226 21.096  1.00 33.45  ? 49  GLU D CA  1 
ATOM   3729  C  C   . GLU D  1 50  ? -3.189  205.773 20.833  1.00 33.61  ? 49  GLU D C   1 
ATOM   3730  O  O   . GLU D  1 50  ? -2.616  205.135 21.726  1.00 33.31  ? 49  GLU D O   1 
ATOM   3731  C  CB  . GLU D  1 50  ? -5.160  207.271 21.436  1.00 33.20  ? 49  GLU D CB  1 
ATOM   3732  C  CG  . GLU D  1 50  ? -5.432  206.488 22.703  1.00 36.21  ? 49  GLU D CG  1 
ATOM   3733  C  CD  . GLU D  1 50  ? -6.872  206.292 23.051  1.00 36.50  ? 49  GLU D CD  1 
ATOM   3734  O  OE1 . GLU D  1 50  ? -7.818  206.846 22.411  1.00 36.88  ? 49  GLU D OE1 1 
ATOM   3735  O  OE2 . GLU D  1 50  ? -7.048  205.551 24.050  1.00 43.08  ? 49  GLU D OE2 1 
ATOM   3736  N  N   . PHE D  1 51  ? -3.336  205.287 19.619  1.00 29.28  ? 50  PHE D N   1 
ATOM   3737  C  CA  . PHE D  1 51  ? -3.037  203.913 19.407  1.00 30.32  ? 50  PHE D CA  1 
ATOM   3738  C  C   . PHE D  1 51  ? -1.809  203.686 18.579  1.00 32.07  ? 50  PHE D C   1 
ATOM   3739  O  O   . PHE D  1 51  ? -1.664  204.329 17.533  1.00 34.98  ? 50  PHE D O   1 
ATOM   3740  C  CB  . PHE D  1 51  ? -4.246  203.164 18.823  1.00 29.98  ? 50  PHE D CB  1 
ATOM   3741  C  CG  . PHE D  1 51  ? -5.507  203.317 19.643  1.00 27.91  ? 50  PHE D CG  1 
ATOM   3742  C  CD1 . PHE D  1 51  ? -5.596  202.793 20.895  1.00 27.75  ? 50  PHE D CD1 1 
ATOM   3743  C  CD2 . PHE D  1 51  ? -6.598  204.000 19.124  1.00 29.26  ? 50  PHE D CD2 1 
ATOM   3744  C  CE1 . PHE D  1 51  ? -6.738  202.971 21.671  1.00 30.36  ? 50  PHE D CE1 1 
ATOM   3745  C  CE2 . PHE D  1 51  ? -7.741  204.187 19.869  1.00 32.33  ? 50  PHE D CE2 1 
ATOM   3746  C  CZ  . PHE D  1 51  ? -7.815  203.655 21.167  1.00 30.02  ? 50  PHE D CZ  1 
ATOM   3747  N  N   . GLY D  1 52  ? -0.946  202.769 19.046  1.00 28.14  ? 51  GLY D N   1 
ATOM   3748  C  CA  . GLY D  1 52  ? 0.134   202.254 18.223  1.00 28.72  ? 51  GLY D CA  1 
ATOM   3749  C  C   . GLY D  1 52  ? -0.255  201.121 17.274  1.00 25.35  ? 51  GLY D C   1 
ATOM   3750  O  O   . GLY D  1 52  ? 0.286   200.048 17.346  1.00 27.82  ? 51  GLY D O   1 
ATOM   3751  N  N   . ASP D  1 53  ? -1.193  201.422 16.405  1.00 25.66  ? 52  ASP D N   1 
ATOM   3752  C  CA  . ASP D  1 53  ? -1.905  200.560 15.539  1.00 27.80  ? 52  ASP D CA  1 
ATOM   3753  C  C   . ASP D  1 53  ? -1.787  201.109 14.138  1.00 31.32  ? 52  ASP D C   1 
ATOM   3754  O  O   . ASP D  1 53  ? -2.498  202.036 13.729  1.00 31.62  ? 52  ASP D O   1 
ATOM   3755  C  CB  . ASP D  1 53  ? -3.391  200.582 15.906  1.00 31.42  ? 52  ASP D CB  1 
ATOM   3756  C  CG  . ASP D  1 53  ? -4.273  199.619 15.029  1.00 32.81  ? 52  ASP D CG  1 
ATOM   3757  O  OD1 . ASP D  1 53  ? -3.944  199.273 13.866  1.00 36.21  ? 52  ASP D OD1 1 
ATOM   3758  O  OD2 . ASP D  1 53  ? -5.331  199.183 15.506  1.00 34.58  ? 52  ASP D OD2 1 
ATOM   3759  N  N   . ASN D  1 54  ? -0.978  200.437 13.355  1.00 33.08  ? 53  ASN D N   1 
ATOM   3760  C  CA  . ASN D  1 54  ? -0.727  200.849 12.029  1.00 33.52  ? 53  ASN D CA  1 
ATOM   3761  C  C   . ASN D  1 54  ? -1.421  199.939 10.974  1.00 34.19  ? 53  ASN D C   1 
ATOM   3762  O  O   . ASN D  1 54  ? -1.063  199.979 9.822   1.00 33.15  ? 53  ASN D O   1 
ATOM   3763  C  CB  . ASN D  1 54  ? 0.786   200.877 11.858  1.00 38.00  ? 53  ASN D CB  1 
ATOM   3764  C  CG  . ASN D  1 54  ? 1.218   201.464 10.494  1.00 54.93  ? 53  ASN D CG  1 
ATOM   3765  O  OD1 . ASN D  1 54  ? 0.987   202.653 10.193  1.00 52.75  ? 53  ASN D OD1 1 
ATOM   3766  N  ND2 . ASN D  1 54  ? 1.798   200.601 9.623   1.00 58.38  ? 53  ASN D ND2 1 
ATOM   3767  N  N   . THR D  1 55  ? -2.425  199.154 11.354  1.00 35.21  ? 54  THR D N   1 
ATOM   3768  C  CA  . THR D  1 55  ? -3.034  198.165 10.419  1.00 34.82  ? 54  THR D CA  1 
ATOM   3769  C  C   . THR D  1 55  ? -3.785  198.851 9.283   1.00 34.94  ? 54  THR D C   1 
ATOM   3770  O  O   . THR D  1 55  ? -4.050  198.247 8.280   1.00 33.94  ? 54  THR D O   1 
ATOM   3771  C  CB  . THR D  1 55  ? -4.023  197.211 11.125  1.00 31.64  ? 54  THR D CB  1 
ATOM   3772  O  OG1 . THR D  1 55  ? -5.093  198.002 11.597  1.00 33.59  ? 54  THR D OG1 1 
ATOM   3773  C  CG2 . THR D  1 55  ? -3.441  196.582 12.343  1.00 29.03  ? 54  THR D CG2 1 
ATOM   3774  N  N   . ALA D  1 56  ? -4.150  200.112 9.431   1.00 31.53  ? 55  ALA D N   1 
ATOM   3775  C  CA  . ALA D  1 56  ? -4.800  200.785 8.334   1.00 32.59  ? 55  ALA D CA  1 
ATOM   3776  C  C   . ALA D  1 56  ? -4.038  202.115 8.133   1.00 33.39  ? 55  ALA D C   1 
ATOM   3777  O  O   . ALA D  1 56  ? -4.611  203.179 7.994   1.00 41.26  ? 55  ALA D O   1 
ATOM   3778  C  CB  . ALA D  1 56  ? -6.292  201.001 8.642   1.00 29.61  ? 55  ALA D CB  1 
ATOM   3779  N  N   . GLY D  1 57  ? -2.728  202.065 8.180   1.00 33.34  ? 56  GLY D N   1 
ATOM   3780  C  CA  . GLY D  1 57  ? -1.913  203.272 8.011   1.00 32.53  ? 56  GLY D CA  1 
ATOM   3781  C  C   . GLY D  1 57  ? -2.058  204.166 9.228   1.00 36.08  ? 56  GLY D C   1 
ATOM   3782  O  O   . GLY D  1 57  ? -2.386  203.702 10.324  1.00 37.62  ? 56  GLY D O   1 
ATOM   3783  N  N   . CYS D  1 58  ? -1.917  205.461 9.009   1.00 34.02  ? 57  CYS D N   1 
ATOM   3784  C  CA  . CYS D  1 58  ? -2.105  206.419 10.042  1.00 30.64  ? 57  CYS D CA  1 
ATOM   3785  C  C   . CYS D  1 58  ? -3.542  206.520 10.594  1.00 31.47  ? 57  CYS D C   1 
ATOM   3786  O  O   . CYS D  1 58  ? -3.711  206.902 11.722  1.00 31.04  ? 57  CYS D O   1 
ATOM   3787  C  CB  . CYS D  1 58  ? -1.495  207.756 9.624   1.00 33.86  ? 57  CYS D CB  1 
ATOM   3788  S  SG  . CYS D  1 58  ? 0.249   207.646 9.095   1.00 38.60  ? 57  CYS D SG  1 
ATOM   3789  N  N   . THR D  1 59  ? -4.553  206.129 9.846   1.00 31.07  ? 58  THR D N   1 
ATOM   3790  C  CA  . THR D  1 59  ? -5.934  206.283 10.276  1.00 32.11  ? 58  THR D CA  1 
ATOM   3791  C  C   . THR D  1 59  ? -6.170  205.490 11.512  1.00 32.04  ? 58  THR D C   1 
ATOM   3792  O  O   . THR D  1 59  ? -6.882  205.952 12.400  1.00 34.75  ? 58  THR D O   1 
ATOM   3793  C  CB  . THR D  1 59  ? -6.908  205.771 9.190   1.00 35.07  ? 58  THR D CB  1 
ATOM   3794  O  OG1 . THR D  1 59  ? -6.530  206.372 7.974   1.00 44.79  ? 58  THR D OG1 1 
ATOM   3795  C  CG2 . THR D  1 59  ? -8.276  206.187 9.418   1.00 30.98  ? 58  THR D CG2 1 
ATOM   3796  N  N   . SER D  1 60  ? -5.551  204.322 11.626  1.00 32.33  ? 59  SER D N   1 
ATOM   3797  C  CA  . SER D  1 60  ? -5.782  203.517 12.814  1.00 32.10  ? 59  SER D CA  1 
ATOM   3798  C  C   . SER D  1 60  ? -5.103  203.896 14.123  1.00 31.56  ? 59  SER D C   1 
ATOM   3799  O  O   . SER D  1 60  ? -5.347  203.253 15.160  1.00 32.47  ? 59  SER D O   1 
ATOM   3800  C  CB  . SER D  1 60  ? -5.658  202.030 12.557  1.00 30.33  ? 59  SER D CB  1 
ATOM   3801  O  OG  . SER D  1 60  ? -4.755  201.745 11.602  1.00 32.88  ? 59  SER D OG  1 
ATOM   3802  N  N   . ALA D  1 61  ? -4.290  204.939 14.102  1.00 28.98  ? 60  ALA D N   1 
ATOM   3803  C  CA  . ALA D  1 61  ? -3.762  205.442 15.346  1.00 29.06  ? 60  ALA D CA  1 
ATOM   3804  C  C   . ALA D  1 61  ? -4.822  206.189 16.225  1.00 27.65  ? 60  ALA D C   1 
ATOM   3805  O  O   . ALA D  1 61  ? -4.611  206.392 17.366  1.00 26.55  ? 60  ALA D O   1 
ATOM   3806  C  CB  . ALA D  1 61  ? -2.535  206.268 15.096  1.00 28.20  ? 60  ALA D CB  1 
ATOM   3807  N  N   . GLY D  1 62  ? -5.992  206.526 15.709  1.00 32.05  ? 61  GLY D N   1 
ATOM   3808  C  CA  . GLY D  1 62  ? -7.038  207.071 16.565  1.00 31.12  ? 61  GLY D CA  1 
ATOM   3809  C  C   . GLY D  1 62  ? -6.846  208.552 16.861  1.00 27.53  ? 61  GLY D C   1 
ATOM   3810  O  O   . GLY D  1 62  ? -6.080  209.218 16.185  1.00 28.77  ? 61  GLY D O   1 
ATOM   3811  N  N   . PRO D  1 63  ? -7.527  209.070 17.863  1.00 28.53  ? 62  PRO D N   1 
ATOM   3812  C  CA  . PRO D  1 63  ? -7.418  210.521 18.127  1.00 31.87  ? 62  PRO D CA  1 
ATOM   3813  C  C   . PRO D  1 63  ? -6.046  210.852 18.834  1.00 31.18  ? 62  PRO D C   1 
ATOM   3814  O  O   . PRO D  1 63  ? -5.203  209.970 19.052  1.00 30.79  ? 62  PRO D O   1 
ATOM   3815  C  CB  . PRO D  1 63  ? -8.619  210.786 19.066  1.00 29.27  ? 62  PRO D CB  1 
ATOM   3816  C  CG  . PRO D  1 63  ? -8.889  209.467 19.715  1.00 26.28  ? 62  PRO D CG  1 
ATOM   3817  C  CD  . PRO D  1 63  ? -8.269  208.363 18.922  1.00 27.21  ? 62  PRO D CD  1 
ATOM   3818  N  N   . HIS D  1 64  ? -5.803  212.106 19.132  1.00 31.44  ? 63  HIS D N   1 
ATOM   3819  C  CA  . HIS D  1 64  ? -4.652  212.478 19.967  1.00 32.59  ? 63  HIS D CA  1 
ATOM   3820  C  C   . HIS D  1 64  ? -4.797  211.752 21.304  1.00 28.59  ? 63  HIS D C   1 
ATOM   3821  O  O   . HIS D  1 64  ? -5.871  211.648 21.820  1.00 28.84  ? 63  HIS D O   1 
ATOM   3822  C  CB  . HIS D  1 64  ? -4.672  214.007 20.180  1.00 31.31  ? 63  HIS D CB  1 
ATOM   3823  C  CG  . HIS D  1 64  ? -4.540  214.785 18.911  1.00 33.77  ? 63  HIS D CG  1 
ATOM   3824  N  ND1 . HIS D  1 64  ? -4.460  216.145 18.873  1.00 31.53  ? 63  HIS D ND1 1 
ATOM   3825  C  CD2 . HIS D  1 64  ? -4.411  214.382 17.629  1.00 35.95  ? 63  HIS D CD2 1 
ATOM   3826  C  CE1 . HIS D  1 64  ? -4.289  216.555 17.635  1.00 27.42  ? 63  HIS D CE1 1 
ATOM   3827  N  NE2 . HIS D  1 64  ? -4.264  215.507 16.857  1.00 30.57  ? 63  HIS D NE2 1 
ATOM   3828  N  N   . PHE D  1 65  ? -3.686  211.292 21.834  1.00 27.60  ? 64  PHE D N   1 
ATOM   3829  C  CA  . PHE D  1 65  ? -3.579  210.732 23.094  1.00 25.58  ? 64  PHE D CA  1 
ATOM   3830  C  C   . PHE D  1 65  ? -4.043  211.724 24.144  1.00 29.26  ? 64  PHE D C   1 
ATOM   3831  O  O   . PHE D  1 65  ? -3.379  212.723 24.420  1.00 29.28  ? 64  PHE D O   1 
ATOM   3832  C  CB  . PHE D  1 65  ? -2.136  210.344 23.315  1.00 24.81  ? 64  PHE D CB  1 
ATOM   3833  C  CG  . PHE D  1 65  ? -1.908  209.654 24.646  1.00 27.73  ? 64  PHE D CG  1 
ATOM   3834  C  CD1 . PHE D  1 65  ? -2.836  208.742 25.158  1.00 27.41  ? 64  PHE D CD1 1 
ATOM   3835  C  CD2 . PHE D  1 65  ? -0.758  209.888 25.384  1.00 31.23  ? 64  PHE D CD2 1 
ATOM   3836  C  CE1 . PHE D  1 65  ? -2.637  208.099 26.370  1.00 27.84  ? 64  PHE D CE1 1 
ATOM   3837  C  CE2 . PHE D  1 65  ? -0.524  209.221 26.619  1.00 30.37  ? 64  PHE D CE2 1 
ATOM   3838  C  CZ  . PHE D  1 65  ? -1.487  208.328 27.100  1.00 29.80  ? 64  PHE D CZ  1 
ATOM   3839  N  N   . ASN D  1 66  ? -5.188  211.412 24.749  1.00 30.35  ? 65  ASN D N   1 
ATOM   3840  C  CA  . ASN D  1 66  ? -5.917  212.308 25.608  1.00 29.33  ? 65  ASN D CA  1 
ATOM   3841  C  C   . ASN D  1 66  ? -6.416  211.631 26.894  1.00 30.78  ? 65  ASN D C   1 
ATOM   3842  O  O   . ASN D  1 66  ? -7.600  211.551 27.112  1.00 34.65  ? 65  ASN D O   1 
ATOM   3843  C  CB  . ASN D  1 66  ? -7.076  212.924 24.846  1.00 27.31  ? 65  ASN D CB  1 
ATOM   3844  C  CG  . ASN D  1 66  ? -7.733  214.095 25.592  1.00 30.65  ? 65  ASN D CG  1 
ATOM   3845  O  OD1 . ASN D  1 66  ? -7.154  214.706 26.500  1.00 33.56  ? 65  ASN D OD1 1 
ATOM   3846  N  ND2 . ASN D  1 66  ? -8.917  214.443 25.178  1.00 29.94  ? 65  ASN D ND2 1 
ATOM   3847  N  N   . PRO D  1 67  ? -5.509  211.154 27.757  1.00 30.64  ? 66  PRO D N   1 
ATOM   3848  C  CA  . PRO D  1 67  ? -6.058  210.275 28.802  1.00 28.83  ? 66  PRO D CA  1 
ATOM   3849  C  C   . PRO D  1 67  ? -6.842  211.064 29.812  1.00 34.22  ? 66  PRO D C   1 
ATOM   3850  O  O   . PRO D  1 67  ? -7.799  210.513 30.359  1.00 41.16  ? 66  PRO D O   1 
ATOM   3851  C  CB  . PRO D  1 67  ? -4.833  209.610 29.428  1.00 26.24  ? 66  PRO D CB  1 
ATOM   3852  C  CG  . PRO D  1 67  ? -3.690  210.464 28.999  1.00 27.11  ? 66  PRO D CG  1 
ATOM   3853  C  CD  . PRO D  1 67  ? -4.030  211.196 27.749  1.00 25.41  ? 66  PRO D CD  1 
ATOM   3854  N  N   . LEU D  1 68  ? -6.537  212.351 29.990  1.00 35.25  ? 67  LEU D N   1 
ATOM   3855  C  CA  . LEU D  1 68  ? -7.280  213.266 30.889  1.00 31.73  ? 67  LEU D CA  1 
ATOM   3856  C  C   . LEU D  1 68  ? -8.523  213.931 30.292  1.00 36.46  ? 67  LEU D C   1 
ATOM   3857  O  O   . LEU D  1 68  ? -9.131  214.779 30.943  1.00 38.91  ? 67  LEU D O   1 
ATOM   3858  C  CB  . LEU D  1 68  ? -6.360  214.359 31.406  1.00 32.38  ? 67  LEU D CB  1 
ATOM   3859  C  CG  . LEU D  1 68  ? -5.322  213.823 32.408  1.00 37.08  ? 67  LEU D CG  1 
ATOM   3860  C  CD1 . LEU D  1 68  ? -4.369  214.930 32.867  1.00 34.81  ? 67  LEU D CD1 1 
ATOM   3861  C  CD2 . LEU D  1 68  ? -6.042  213.165 33.599  1.00 38.70  ? 67  LEU D CD2 1 
ATOM   3862  N  N   . SER D  1 69  ? -8.906  213.576 29.055  1.00 35.44  ? 68  SER D N   1 
ATOM   3863  C  CA  . SER D  1 69  ? -10.124 214.131 28.395  1.00 38.09  ? 68  SER D CA  1 
ATOM   3864  C  C   . SER D  1 69  ? -10.219 215.664 28.400  1.00 37.86  ? 68  SER D C   1 
ATOM   3865  O  O   . SER D  1 69  ? -11.235 216.232 28.801  1.00 39.81  ? 68  SER D O   1 
ATOM   3866  C  CB  . SER D  1 69  ? -11.441 213.572 28.959  1.00 37.45  ? 68  SER D CB  1 
ATOM   3867  O  OG  . SER D  1 69  ? -11.493 212.211 28.877  1.00 37.63  ? 68  SER D OG  1 
ATOM   3868  N  N   . ARG D  1 70  ? -9.154  216.315 27.947  1.00 35.99  ? 69  ARG D N   1 
ATOM   3869  C  CA  A ARG D  1 70  ? -9.124  217.765 27.846  0.50 31.98  ? 69  ARG D CA  1 
ATOM   3870  C  CA  B ARG D  1 70  ? -9.136  217.761 27.870  0.50 32.95  ? 69  ARG D CA  1 
ATOM   3871  C  C   . ARG D  1 70  ? -9.423  218.228 26.423  1.00 31.17  ? 69  ARG D C   1 
ATOM   3872  O  O   . ARG D  1 70  ? -9.635  217.425 25.500  1.00 32.29  ? 69  ARG D O   1 
ATOM   3873  C  CB  A ARG D  1 70  ? -7.795  218.293 28.371  0.50 29.78  ? 69  ARG D CB  1 
ATOM   3874  C  CB  B ARG D  1 70  ? -7.861  218.327 28.541  0.50 32.27  ? 69  ARG D CB  1 
ATOM   3875  C  CG  A ARG D  1 70  ? -7.466  217.799 29.775  0.50 31.13  ? 69  ARG D CG  1 
ATOM   3876  C  CG  B ARG D  1 70  ? -7.629  217.781 29.976  0.50 35.20  ? 69  ARG D CG  1 
ATOM   3877  C  CD  A ARG D  1 70  ? -8.248  218.471 30.911  0.50 29.33  ? 69  ARG D CD  1 
ATOM   3878  C  CD  B ARG D  1 70  ? -7.140  218.786 31.051  0.50 35.45  ? 69  ARG D CD  1 
ATOM   3879  N  NE  A ARG D  1 70  ? -7.615  218.176 32.190  0.50 28.83  ? 69  ARG D NE  1 
ATOM   3880  N  NE  B ARG D  1 70  ? -6.016  218.268 31.867  0.50 35.72  ? 69  ARG D NE  1 
ATOM   3881  C  CZ  A ARG D  1 70  ? -8.217  217.609 33.218  0.50 26.10  ? 69  ARG D CZ  1 
ATOM   3882  C  CZ  B ARG D  1 70  ? -5.186  219.013 32.606  0.50 33.35  ? 69  ARG D CZ  1 
ATOM   3883  N  NH1 A ARG D  1 70  ? -9.501  217.314 33.172  0.50 24.05  ? 69  ARG D NH1 1 
ATOM   3884  N  NH1 B ARG D  1 70  ? -5.293  220.313 32.669  0.50 34.08  ? 69  ARG D NH1 1 
ATOM   3885  N  NH2 A ARG D  1 70  ? -7.525  217.357 34.297  0.50 25.94  ? 69  ARG D NH2 1 
ATOM   3886  N  NH2 B ARG D  1 70  ? -4.214  218.462 33.276  0.50 33.58  ? 69  ARG D NH2 1 
ATOM   3887  N  N   . LYS D  1 71  ? -9.533  219.516 26.239  1.00 32.66  ? 70  LYS D N   1 
ATOM   3888  C  CA  . LYS D  1 71  ? -9.650  220.017 24.904  1.00 37.49  ? 70  LYS D CA  1 
ATOM   3889  C  C   . LYS D  1 71  ? -8.245  220.147 24.232  1.00 34.89  ? 70  LYS D C   1 
ATOM   3890  O  O   . LYS D  1 71  ? -7.249  220.194 24.927  1.00 30.70  ? 70  LYS D O   1 
ATOM   3891  C  CB  . LYS D  1 71  ? -10.389 221.322 24.945  1.00 38.98  ? 70  LYS D CB  1 
ATOM   3892  C  CG  . LYS D  1 71  ? -11.855 221.157 25.321  1.00 43.63  ? 70  LYS D CG  1 
ATOM   3893  C  CD  . LYS D  1 71  ? -12.280 222.498 25.941  1.00 51.94  ? 70  LYS D CD  1 
ATOM   3894  C  CE  . LYS D  1 71  ? -13.805 222.616 26.002  1.00 61.26  ? 70  LYS D CE  1 
ATOM   3895  N  NZ  . LYS D  1 71  ? -14.363 224.019 25.874  1.00 57.53  ? 70  LYS D NZ  1 
ATOM   3896  N  N   . HIS D  1 72  ? -8.181  220.183 22.896  1.00 32.35  ? 71  HIS D N   1 
ATOM   3897  C  CA  . HIS D  1 72  ? -6.919  220.402 22.211  1.00 30.62  ? 71  HIS D CA  1 
ATOM   3898  C  C   . HIS D  1 72  ? -6.277  221.760 22.562  1.00 29.36  ? 71  HIS D C   1 
ATOM   3899  O  O   . HIS D  1 72  ? -6.964  222.759 22.640  1.00 30.28  ? 71  HIS D O   1 
ATOM   3900  C  CB  . HIS D  1 72  ? -7.112  220.215 20.687  1.00 28.45  ? 71  HIS D CB  1 
ATOM   3901  C  CG  . HIS D  1 72  ? -5.864  220.456 19.894  1.00 30.10  ? 71  HIS D CG  1 
ATOM   3902  N  ND1 . HIS D  1 72  ? -4.896  219.488 19.697  1.00 31.83  ? 71  HIS D ND1 1 
ATOM   3903  C  CD2 . HIS D  1 72  ? -5.375  221.592 19.343  1.00 27.10  ? 71  HIS D CD2 1 
ATOM   3904  C  CE1 . HIS D  1 72  ? -3.883  220.005 19.020  1.00 28.96  ? 71  HIS D CE1 1 
ATOM   3905  N  NE2 . HIS D  1 72  ? -4.164  221.276 18.788  1.00 31.49  ? 71  HIS D NE2 1 
ATOM   3906  N  N   . GLY D  1 73  ? -4.969  221.809 22.723  1.00 27.40  ? 72  GLY D N   1 
ATOM   3907  C  CA  . GLY D  1 73  ? -4.275  223.045 22.999  1.00 24.91  ? 72  GLY D CA  1 
ATOM   3908  C  C   . GLY D  1 73  ? -2.872  222.941 22.419  1.00 30.58  ? 72  GLY D C   1 
ATOM   3909  O  O   . GLY D  1 73  ? -2.559  222.002 21.665  1.00 31.42  ? 72  GLY D O   1 
ATOM   3910  N  N   . GLY D  1 74  ? -2.027  223.917 22.755  1.00 29.51  ? 73  GLY D N   1 
ATOM   3911  C  CA  . GLY D  1 74  ? -0.626  223.909 22.429  1.00 28.69  ? 73  GLY D CA  1 
ATOM   3912  C  C   . GLY D  1 74  ? 0.204   223.293 23.516  1.00 28.76  ? 73  GLY D C   1 
ATOM   3913  O  O   . GLY D  1 74  ? -0.247  223.155 24.628  1.00 30.79  ? 73  GLY D O   1 
ATOM   3914  N  N   . PRO D  1 75  ? 1.440   222.934 23.224  1.00 29.51  ? 74  PRO D N   1 
ATOM   3915  C  CA  . PRO D  1 75  ? 2.153   222.299 24.320  1.00 27.83  ? 74  PRO D CA  1 
ATOM   3916  C  C   . PRO D  1 75  ? 2.374   223.184 25.560  1.00 33.26  ? 74  PRO D C   1 
ATOM   3917  O  O   . PRO D  1 75  ? 2.548   222.663 26.634  1.00 34.15  ? 74  PRO D O   1 
ATOM   3918  C  CB  . PRO D  1 75  ? 3.476   221.886 23.714  1.00 27.50  ? 74  PRO D CB  1 
ATOM   3919  C  CG  . PRO D  1 75  ? 3.620   222.734 22.478  1.00 31.65  ? 74  PRO D CG  1 
ATOM   3920  C  CD  . PRO D  1 75  ? 2.221   223.002 21.977  1.00 28.63  ? 74  PRO D CD  1 
ATOM   3921  N  N   . LYS D  1 76  ? 2.346   224.500 25.413  1.00 33.77  ? 75  LYS D N   1 
ATOM   3922  C  CA  . LYS D  1 76  ? 2.408   225.436 26.530  1.00 37.57  ? 75  LYS D CA  1 
ATOM   3923  C  C   . LYS D  1 76  ? 1.112   225.609 27.343  1.00 38.01  ? 75  LYS D C   1 
ATOM   3924  O  O   . LYS D  1 76  ? 1.180   226.197 28.399  1.00 36.81  ? 75  LYS D O   1 
ATOM   3925  C  CB  . LYS D  1 76  ? 2.792   226.863 26.051  1.00 41.70  ? 75  LYS D CB  1 
ATOM   3926  C  CG  . LYS D  1 76  ? 4.259   227.031 25.664  1.00 43.56  ? 75  LYS D CG  1 
ATOM   3927  C  CD  . LYS D  1 76  ? 4.468   228.105 24.576  1.00 50.21  ? 75  LYS D CD  1 
ATOM   3928  C  CE  . LYS D  1 76  ? 5.045   229.445 25.126  1.00 47.03  ? 75  LYS D CE  1 
ATOM   3929  N  NZ  . LYS D  1 76  ? 4.460   230.664 24.482  1.00 42.21  ? 75  LYS D NZ  1 
ATOM   3930  N  N   . ASP D  1 77  ? -0.041  225.167 26.855  1.00 33.22  ? 76  ASP D N   1 
ATOM   3931  C  CA  . ASP D  1 77  ? -1.272  225.383 27.561  1.00 34.93  ? 76  ASP D CA  1 
ATOM   3932  C  C   . ASP D  1 77  ? -1.385  224.350 28.642  1.00 40.01  ? 76  ASP D C   1 
ATOM   3933  O  O   . ASP D  1 77  ? -0.817  223.224 28.553  1.00 42.42  ? 76  ASP D O   1 
ATOM   3934  C  CB  . ASP D  1 77  ? -2.501  225.227 26.597  1.00 39.09  ? 76  ASP D CB  1 
ATOM   3935  C  CG  . ASP D  1 77  ? -2.618  226.361 25.560  1.00 43.25  ? 76  ASP D CG  1 
ATOM   3936  O  OD1 . ASP D  1 77  ? -2.611  227.546 25.959  1.00 45.36  ? 76  ASP D OD1 1 
ATOM   3937  O  OD2 . ASP D  1 77  ? -2.736  226.133 24.330  1.00 49.87  ? 76  ASP D OD2 1 
ATOM   3938  N  N   . GLU D  1 78  ? -2.197  224.664 29.639  1.00 40.21  ? 77  GLU D N   1 
ATOM   3939  C  CA  . GLU D  1 78  ? -2.570  223.672 30.634  1.00 39.07  ? 77  GLU D CA  1 
ATOM   3940  C  C   . GLU D  1 78  ? -3.767  222.851 30.118  1.00 38.13  ? 77  GLU D C   1 
ATOM   3941  O  O   . GLU D  1 78  ? -3.793  221.623 30.235  1.00 33.83  ? 77  GLU D O   1 
ATOM   3942  C  CB  . GLU D  1 78  ? -2.821  224.363 31.941  1.00 41.34  ? 77  GLU D CB  1 
ATOM   3943  C  CG  . GLU D  1 78  ? -3.658  223.573 32.934  1.00 56.79  ? 77  GLU D CG  1 
ATOM   3944  C  CD  . GLU D  1 78  ? -3.717  224.213 34.346  1.00 72.70  ? 77  GLU D CD  1 
ATOM   3945  O  OE1 . GLU D  1 78  ? -3.375  225.451 34.520  1.00 66.28  ? 77  GLU D OE1 1 
ATOM   3946  O  OE2 . GLU D  1 78  ? -4.121  223.471 35.301  1.00 70.33  ? 77  GLU D OE2 1 
ATOM   3947  N  N   . GLU D  1 79  ? -4.720  223.526 29.485  1.00 35.58  ? 78  GLU D N   1 
ATOM   3948  C  CA  . GLU D  1 79  ? -5.738  222.814 28.776  1.00 33.59  ? 78  GLU D CA  1 
ATOM   3949  C  C   . GLU D  1 79  ? -5.162  222.234 27.467  1.00 31.89  ? 78  GLU D C   1 
ATOM   3950  O  O   . GLU D  1 79  ? -5.067  222.913 26.494  1.00 31.39  ? 78  GLU D O   1 
ATOM   3951  C  CB  . GLU D  1 79  ? -6.921  223.728 28.527  1.00 28.99  ? 78  GLU D CB  1 
ATOM   3952  C  CG  . GLU D  1 79  ? -8.124  223.014 27.930  1.00 33.11  ? 78  GLU D CG  1 
ATOM   3953  C  CD  . GLU D  1 79  ? -8.907  222.085 28.899  1.00 37.33  ? 78  GLU D CD  1 
ATOM   3954  O  OE1 . GLU D  1 79  ? -8.709  222.159 30.157  1.00 43.97  ? 78  GLU D OE1 1 
ATOM   3955  O  OE2 . GLU D  1 79  ? -9.726  221.239 28.422  1.00 37.78  ? 78  GLU D OE2 1 
ATOM   3956  N  N   . ARG D  1 80  ? -4.785  220.961 27.476  1.00 34.58  ? 79  ARG D N   1 
ATOM   3957  C  CA  . ARG D  1 80  ? -4.192  220.263 26.296  1.00 32.83  ? 79  ARG D CA  1 
ATOM   3958  C  C   . ARG D  1 80  ? -4.337  218.744 26.386  1.00 33.05  ? 79  ARG D C   1 
ATOM   3959  O  O   . ARG D  1 80  ? -4.467  218.201 27.485  1.00 35.98  ? 79  ARG D O   1 
ATOM   3960  C  CB  . ARG D  1 80  ? -2.699  220.616 26.092  1.00 30.00  ? 79  ARG D CB  1 
ATOM   3961  C  CG  . ARG D  1 80  ? -1.833  220.319 27.303  1.00 26.14  ? 79  ARG D CG  1 
ATOM   3962  C  CD  . ARG D  1 80  ? -0.345  220.406 27.013  1.00 27.51  ? 79  ARG D CD  1 
ATOM   3963  N  NE  . ARG D  1 80  ? 0.208   219.241 26.345  1.00 29.04  ? 79  ARG D NE  1 
ATOM   3964  C  CZ  . ARG D  1 80  ? 1.504   218.978 26.256  1.00 28.88  ? 79  ARG D CZ  1 
ATOM   3965  N  NH1 . ARG D  1 80  ? 2.400   219.822 26.739  1.00 30.16  ? 79  ARG D NH1 1 
ATOM   3966  N  NH2 . ARG D  1 80  ? 1.921   217.870 25.690  1.00 28.72  ? 79  ARG D NH2 1 
ATOM   3967  N  N   . HIS D  1 81  ? -4.257  218.065 25.246  1.00 30.09  ? 80  HIS D N   1 
ATOM   3968  C  CA  . HIS D  1 81  ? -4.062  216.633 25.222  1.00 31.02  ? 80  HIS D CA  1 
ATOM   3969  C  C   . HIS D  1 81  ? -2.642  216.342 25.674  1.00 29.49  ? 80  HIS D C   1 
ATOM   3970  O  O   . HIS D  1 81  ? -1.736  217.172 25.483  1.00 30.49  ? 80  HIS D O   1 
ATOM   3971  C  CB  . HIS D  1 81  ? -4.409  216.045 23.823  1.00 30.07  ? 80  HIS D CB  1 
ATOM   3972  C  CG  . HIS D  1 81  ? -5.774  216.446 23.329  1.00 29.99  ? 80  HIS D CG  1 
ATOM   3973  N  ND1 . HIS D  1 81  ? -6.058  216.740 22.023  1.00 30.85  ? 80  HIS D ND1 1 
ATOM   3974  C  CD2 . HIS D  1 81  ? -6.924  216.651 23.993  1.00 32.65  ? 80  HIS D CD2 1 
ATOM   3975  C  CE1 . HIS D  1 81  ? -7.321  217.041 21.888  1.00 27.79  ? 80  HIS D CE1 1 
ATOM   3976  N  NE2 . HIS D  1 81  ? -7.870  216.988 23.071  1.00 31.94  ? 80  HIS D NE2 1 
ATOM   3977  N  N   . VAL D  1 82  ? -2.449  215.189 26.308  1.00 28.10  ? 81  VAL D N   1 
ATOM   3978  C  CA  . VAL D  1 82  ? -1.073  214.762 26.574  1.00 27.23  ? 81  VAL D CA  1 
ATOM   3979  C  C   . VAL D  1 82  ? -0.267  214.796 25.260  1.00 27.45  ? 81  VAL D C   1 
ATOM   3980  O  O   . VAL D  1 82  ? 0.840   215.320 25.234  1.00 27.78  ? 81  VAL D O   1 
ATOM   3981  C  CB  . VAL D  1 82  ? -0.977  213.404 27.333  1.00 25.82  ? 81  VAL D CB  1 
ATOM   3982  C  CG1 . VAL D  1 82  ? 0.447   212.848 27.304  1.00 23.00  ? 81  VAL D CG1 1 
ATOM   3983  C  CG2 . VAL D  1 82  ? -1.459  213.568 28.773  1.00 24.62  ? 81  VAL D CG2 1 
ATOM   3984  N  N   . GLY D  1 83  ? -0.851  214.292 24.172  1.00 25.83  ? 82  GLY D N   1 
ATOM   3985  C  CA  . GLY D  1 83  ? -0.137  214.189 22.915  1.00 27.82  ? 82  GLY D CA  1 
ATOM   3986  C  C   . GLY D  1 83  ? 0.017   215.481 22.098  1.00 29.04  ? 82  GLY D C   1 
ATOM   3987  O  O   . GLY D  1 83  ? 0.467   215.416 20.944  1.00 31.40  ? 82  GLY D O   1 
ATOM   3988  N  N   . ASP D  1 84  ? -0.371  216.630 22.660  1.00 27.29  ? 83  ASP D N   1 
ATOM   3989  C  CA  . ASP D  1 84  ? -0.305  217.913 21.952  1.00 27.17  ? 83  ASP D CA  1 
ATOM   3990  C  C   . ASP D  1 84  ? 1.116   218.528 21.933  1.00 26.11  ? 83  ASP D C   1 
ATOM   3991  O  O   . ASP D  1 84  ? 1.477   219.212 22.833  1.00 24.27  ? 83  ASP D O   1 
ATOM   3992  C  CB  . ASP D  1 84  ? -1.340  218.871 22.563  1.00 30.75  ? 83  ASP D CB  1 
ATOM   3993  C  CG  . ASP D  1 84  ? -2.761  218.569 22.159  1.00 30.12  ? 83  ASP D CG  1 
ATOM   3994  O  OD1 . ASP D  1 84  ? -2.966  217.761 21.283  1.00 33.10  ? 83  ASP D OD1 1 
ATOM   3995  O  OD2 . ASP D  1 84  ? -3.726  219.147 22.678  1.00 31.56  ? 83  ASP D OD2 1 
ATOM   3996  N  N   . LEU D  1 85  ? 1.935   218.245 20.917  1.00 27.45  ? 84  LEU D N   1 
ATOM   3997  C  CA  . LEU D  1 85  ? 3.286   218.757 20.870  1.00 25.29  ? 84  LEU D CA  1 
ATOM   3998  C  C   . LEU D  1 85  ? 3.401   219.960 20.006  1.00 24.41  ? 84  LEU D C   1 
ATOM   3999  O  O   . LEU D  1 85  ? 4.496   220.348 19.685  1.00 27.25  ? 84  LEU D O   1 
ATOM   4000  C  CB  . LEU D  1 85  ? 4.313   217.670 20.478  1.00 24.81  ? 84  LEU D CB  1 
ATOM   4001  C  CG  . LEU D  1 85  ? 4.438   216.440 21.383  1.00 27.83  ? 84  LEU D CG  1 
ATOM   4002  C  CD1 . LEU D  1 85  ? 5.448   215.424 20.855  1.00 24.50  ? 84  LEU D CD1 1 
ATOM   4003  C  CD2 . LEU D  1 85  ? 4.682   216.707 22.883  1.00 23.98  ? 84  LEU D CD2 1 
ATOM   4004  N  N   . GLY D  1 86  ? 2.276   220.509 19.570  1.00 25.58  ? 85  GLY D N   1 
ATOM   4005  C  CA  . GLY D  1 86  ? 2.235   221.707 18.707  1.00 26.39  ? 85  GLY D CA  1 
ATOM   4006  C  C   . GLY D  1 86  ? 2.716   221.521 17.304  1.00 26.47  ? 85  GLY D C   1 
ATOM   4007  O  O   . GLY D  1 86  ? 2.319   220.567 16.700  1.00 30.90  ? 85  GLY D O   1 
ATOM   4008  N  N   . ASN D  1 87  ? 3.555   222.420 16.788  1.00 26.31  ? 86  ASN D N   1 
ATOM   4009  C  CA  . ASN D  1 87  ? 4.040   222.328 15.430  1.00 27.60  ? 86  ASN D CA  1 
ATOM   4010  C  C   . ASN D  1 87  ? 5.493   222.032 15.295  1.00 29.88  ? 86  ASN D C   1 
ATOM   4011  O  O   . ASN D  1 87  ? 6.244   222.342 16.194  1.00 33.49  ? 86  ASN D O   1 
ATOM   4012  C  CB  . ASN D  1 87  ? 3.769   223.597 14.656  1.00 26.87  ? 86  ASN D CB  1 
ATOM   4013  C  CG  . ASN D  1 87  ? 2.307   223.873 14.502  1.00 29.22  ? 86  ASN D CG  1 
ATOM   4014  O  OD1 . ASN D  1 87  ? 1.615   223.150 13.823  1.00 30.22  ? 86  ASN D OD1 1 
ATOM   4015  N  ND2 . ASN D  1 87  ? 1.826   224.945 15.113  1.00 27.10  ? 86  ASN D ND2 1 
ATOM   4016  N  N   . VAL D  1 88  ? 5.895   221.505 14.147  1.00 27.11  ? 87  VAL D N   1 
ATOM   4017  C  CA  . VAL D  1 88  ? 7.278   221.415 13.764  1.00 25.73  ? 87  VAL D CA  1 
ATOM   4018  C  C   . VAL D  1 88  ? 7.322   222.226 12.475  1.00 28.67  ? 87  VAL D C   1 
ATOM   4019  O  O   . VAL D  1 88  ? 6.301   222.386 11.815  1.00 29.74  ? 87  VAL D O   1 
ATOM   4020  C  CB  . VAL D  1 88  ? 7.753   219.940 13.523  1.00 28.81  ? 87  VAL D CB  1 
ATOM   4021  C  CG1 . VAL D  1 88  ? 7.827   219.118 14.815  1.00 26.40  ? 87  VAL D CG1 1 
ATOM   4022  C  CG2 . VAL D  1 88  ? 6.987   219.202 12.399  1.00 23.13  ? 87  VAL D CG2 1 
ATOM   4023  N  N   . THR D  1 89  ? 8.479   222.803 12.139  1.00 30.87  ? 88  THR D N   1 
ATOM   4024  C  CA  . THR D  1 89  ? 8.649   223.717 11.011  1.00 27.34  ? 88  THR D CA  1 
ATOM   4025  C  C   . THR D  1 89  ? 9.601   223.105 10.024  1.00 27.91  ? 88  THR D C   1 
ATOM   4026  O  O   . THR D  1 89  ? 10.723  222.774 10.394  1.00 29.77  ? 88  THR D O   1 
ATOM   4027  C  CB  . THR D  1 89  ? 9.336   224.948 11.524  1.00 34.00  ? 88  THR D CB  1 
ATOM   4028  O  OG1 . THR D  1 89  ? 8.422   225.676 12.328  1.00 35.66  ? 88  THR D OG1 1 
ATOM   4029  C  CG2 . THR D  1 89  ? 9.873   225.878 10.346  1.00 32.13  ? 88  THR D CG2 1 
ATOM   4030  N  N   . ALA D  1 90  ? 9.152   222.902 8.784   1.00 28.65  ? 89  ALA D N   1 
ATOM   4031  C  CA  . ALA D  1 90  ? 10.027  222.500 7.673   1.00 28.93  ? 89  ALA D CA  1 
ATOM   4032  C  C   . ALA D  1 90  ? 10.624  223.755 7.034   1.00 27.72  ? 89  ALA D C   1 
ATOM   4033  O  O   . ALA D  1 90  ? 9.950   224.752 6.806   1.00 26.63  ? 89  ALA D O   1 
ATOM   4034  C  CB  . ALA D  1 90  ? 9.279   221.697 6.623   1.00 25.98  ? 89  ALA D CB  1 
ATOM   4035  N  N   . ASP D  1 91  ? 11.902  223.668 6.739   1.00 30.16  ? 90  ASP D N   1 
ATOM   4036  C  CA  . ASP D  1 91  ? 12.617  224.698 6.037   1.00 29.91  ? 90  ASP D CA  1 
ATOM   4037  C  C   . ASP D  1 91  ? 12.289  224.704 4.521   1.00 32.19  ? 90  ASP D C   1 
ATOM   4038  O  O   . ASP D  1 91  ? 11.436  223.943 4.070   1.00 36.72  ? 90  ASP D O   1 
ATOM   4039  C  CB  . ASP D  1 91  ? 14.100  224.576 6.377   1.00 30.71  ? 90  ASP D CB  1 
ATOM   4040  C  CG  . ASP D  1 91  ? 14.797  223.386 5.703   1.00 35.54  ? 90  ASP D CG  1 
ATOM   4041  O  OD1 . ASP D  1 91  ? 14.280  222.741 4.721   1.00 33.87  ? 90  ASP D OD1 1 
ATOM   4042  O  OD2 . ASP D  1 91  ? 15.929  223.101 6.178   1.00 37.01  ? 90  ASP D OD2 1 
ATOM   4043  N  N   . LYS D  1 92  ? 12.920  225.561 3.735   1.00 35.08  ? 91  LYS D N   1 
ATOM   4044  C  CA  . LYS D  1 92  ? 12.648  225.639 2.263   1.00 42.47  ? 91  LYS D CA  1 
ATOM   4045  C  C   . LYS D  1 92  ? 12.967  224.363 1.476   1.00 38.98  ? 91  LYS D C   1 
ATOM   4046  O  O   . LYS D  1 92  ? 12.379  224.168 0.427   1.00 35.04  ? 91  LYS D O   1 
ATOM   4047  C  CB  . LYS D  1 92  ? 13.416  226.786 1.622   1.00 47.91  ? 91  LYS D CB  1 
ATOM   4048  C  CG  . LYS D  1 92  ? 14.910  226.756 1.928   1.00 51.56  ? 91  LYS D CG  1 
ATOM   4049  C  CD  . LYS D  1 92  ? 15.654  227.841 1.125   1.00 70.21  ? 91  LYS D CD  1 
ATOM   4050  C  CE  . LYS D  1 92  ? 17.084  227.411 0.679   1.00 74.48  ? 91  LYS D CE  1 
ATOM   4051  N  NZ  . LYS D  1 92  ? 18.042  227.319 1.852   1.00 67.10  ? 91  LYS D NZ  1 
ATOM   4052  N  N   . ASP D  1 93  ? 13.871  223.516 2.002   1.00 34.26  ? 92  ASP D N   1 
ATOM   4053  C  CA  . ASP D  1 93  ? 14.104  222.227 1.413   1.00 33.72  ? 92  ASP D CA  1 
ATOM   4054  C  C   . ASP D  1 93  ? 13.102  221.152 1.754   1.00 36.28  ? 92  ASP D C   1 
ATOM   4055  O  O   . ASP D  1 93  ? 13.248  220.067 1.197   1.00 37.30  ? 92  ASP D O   1 
ATOM   4056  C  CB  . ASP D  1 93  ? 15.472  221.713 1.755   1.00 36.55  ? 92  ASP D CB  1 
ATOM   4057  C  CG  . ASP D  1 93  ? 16.573  222.608 1.225   1.00 43.03  ? 92  ASP D CG  1 
ATOM   4058  O  OD1 . ASP D  1 93  ? 16.429  223.105 0.068   1.00 44.58  ? 92  ASP D OD1 1 
ATOM   4059  O  OD2 . ASP D  1 93  ? 17.584  222.796 1.957   1.00 42.42  ? 92  ASP D OD2 1 
ATOM   4060  N  N   . GLY D  1 94  ? 12.110  221.429 2.644   1.00 35.90  ? 93  GLY D N   1 
ATOM   4061  C  CA  . GLY D  1 94  ? 11.110  220.459 3.113   1.00 29.60  ? 93  GLY D CA  1 
ATOM   4062  C  C   . GLY D  1 94  ? 11.588  219.632 4.322   1.00 28.78  ? 93  GLY D C   1 
ATOM   4063  O  O   . GLY D  1 94  ? 10.968  218.615 4.661   1.00 30.31  ? 93  GLY D O   1 
ATOM   4064  N  N   . VAL D  1 95  ? 12.668  220.049 4.950   1.00 24.50  ? 94  VAL D N   1 
ATOM   4065  C  CA  . VAL D  1 95  ? 13.245  219.374 6.058   1.00 27.99  ? 94  VAL D CA  1 
ATOM   4066  C  C   . VAL D  1 95  ? 12.805  220.100 7.388   1.00 30.82  ? 94  VAL D C   1 
ATOM   4067  O  O   . VAL D  1 95  ? 12.931  221.311 7.506   1.00 28.65  ? 94  VAL D O   1 
ATOM   4068  C  CB  . VAL D  1 95  ? 14.820  219.265 5.897   1.00 31.59  ? 94  VAL D CB  1 
ATOM   4069  C  CG1 . VAL D  1 95  ? 15.478  218.605 7.115   1.00 29.94  ? 94  VAL D CG1 1 
ATOM   4070  C  CG2 . VAL D  1 95  ? 15.218  218.511 4.645   1.00 24.79  ? 94  VAL D CG2 1 
ATOM   4071  N  N   . ALA D  1 96  ? 12.213  219.342 8.333   1.00 31.16  ? 95  ALA D N   1 
ATOM   4072  C  CA  . ALA D  1 96  ? 11.956  219.739 9.730   1.00 27.12  ? 95  ALA D CA  1 
ATOM   4073  C  C   . ALA D  1 96  ? 13.036  219.129 10.615  1.00 30.34  ? 95  ALA D C   1 
ATOM   4074  O  O   . ALA D  1 96  ? 13.086  217.899 10.811  1.00 31.30  ? 95  ALA D O   1 
ATOM   4075  C  CB  . ALA D  1 96  ? 10.581  219.279 10.182  1.00 26.22  ? 95  ALA D CB  1 
ATOM   4076  N  N   . ASP D  1 97  ? 13.935  219.978 11.122  1.00 32.79  ? 96  ASP D N   1 
ATOM   4077  C  CA  . ASP D  1 97  ? 14.904  219.545 12.096  1.00 31.86  ? 96  ASP D CA  1 
ATOM   4078  C  C   . ASP D  1 97  ? 14.323  219.717 13.518  1.00 32.58  ? 96  ASP D C   1 
ATOM   4079  O  O   . ASP D  1 97  ? 14.467  220.772 14.097  1.00 36.78  ? 96  ASP D O   1 
ATOM   4080  C  CB  . ASP D  1 97  ? 16.181  220.340 11.922  1.00 34.63  ? 96  ASP D CB  1 
ATOM   4081  C  CG  . ASP D  1 97  ? 16.997  219.879 10.700  1.00 45.18  ? 96  ASP D CG  1 
ATOM   4082  O  OD1 . ASP D  1 97  ? 17.271  218.631 10.444  1.00 44.39  ? 96  ASP D OD1 1 
ATOM   4083  O  OD2 . ASP D  1 97  ? 17.383  220.796 9.948   1.00 46.15  ? 96  ASP D OD2 1 
ATOM   4084  N  N   . VAL D  1 98  ? 13.703  218.683 14.076  1.00 31.36  ? 97  VAL D N   1 
ATOM   4085  C  CA  . VAL D  1 98  ? 12.842  218.810 15.221  1.00 30.17  ? 97  VAL D CA  1 
ATOM   4086  C  C   . VAL D  1 98  ? 13.587  219.008 16.519  1.00 33.16  ? 97  VAL D C   1 
ATOM   4087  O  O   . VAL D  1 98  ? 14.574  218.324 16.804  1.00 37.50  ? 97  VAL D O   1 
ATOM   4088  C  CB  . VAL D  1 98  ? 11.890  217.599 15.325  1.00 29.56  ? 97  VAL D CB  1 
ATOM   4089  C  CG1 . VAL D  1 98  ? 11.046  217.644 16.595  1.00 28.77  ? 97  VAL D CG1 1 
ATOM   4090  C  CG2 . VAL D  1 98  ? 10.980  217.537 14.118  1.00 24.23  ? 97  VAL D CG2 1 
ATOM   4091  N  N   . SER D  1 99  ? 13.123  219.942 17.322  1.00 32.11  ? 98  SER D N   1 
ATOM   4092  C  CA  . SER D  1 99  ? 13.735  220.116 18.640  1.00 35.82  ? 98  SER D CA  1 
ATOM   4093  C  C   . SER D  1 99  ? 12.678  220.562 19.593  1.00 36.29  ? 98  SER D C   1 
ATOM   4094  O  O   . SER D  1 99  ? 12.239  221.696 19.536  1.00 36.91  ? 98  SER D O   1 
ATOM   4095  C  CB  . SER D  1 99  ? 14.747  221.244 18.548  1.00 34.17  ? 98  SER D CB  1 
ATOM   4096  O  OG  . SER D  1 99  ? 15.676  221.007 19.505  1.00 41.76  ? 98  SER D OG  1 
ATOM   4097  N  N   . ILE D  1 100 ? 12.199  219.703 20.448  1.00 40.68  ? 99  ILE D N   1 
ATOM   4098  C  CA  . ILE D  1 100 ? 11.065  220.115 21.339  1.00 34.80  ? 99  ILE D CA  1 
ATOM   4099  C  C   . ILE D  1 100 ? 11.431  219.634 22.717  1.00 32.77  ? 99  ILE D C   1 
ATOM   4100  O  O   . ILE D  1 100 ? 12.106  218.638 22.883  1.00 34.12  ? 99  ILE D O   1 
ATOM   4101  C  CB  . ILE D  1 100 ? 9.764   219.501 20.830  1.00 33.41  ? 99  ILE D CB  1 
ATOM   4102  C  CG1 . ILE D  1 100 ? 9.186   220.402 19.769  1.00 32.75  ? 99  ILE D CG1 1 
ATOM   4103  C  CG2 . ILE D  1 100 ? 8.722   219.299 21.910  1.00 35.17  ? 99  ILE D CG2 1 
ATOM   4104  C  CD1 . ILE D  1 100 ? 8.168   219.642 18.939  1.00 34.24  ? 99  ILE D CD1 1 
ATOM   4105  N  N   . GLU D  1 101 ? 11.020  220.350 23.709  1.00 32.66  ? 100 GLU D N   1 
ATOM   4106  C  CA  . GLU D  1 101 ? 11.157  219.807 25.013  1.00 34.67  ? 100 GLU D CA  1 
ATOM   4107  C  C   . GLU D  1 101 ? 9.815   219.798 25.758  1.00 29.78  ? 100 GLU D C   1 
ATOM   4108  O  O   . GLU D  1 101 ? 9.107   220.783 25.751  1.00 28.26  ? 100 GLU D O   1 
ATOM   4109  C  CB  . GLU D  1 101 ? 12.276  220.531 25.712  1.00 37.21  ? 100 GLU D CB  1 
ATOM   4110  C  CG  . GLU D  1 101 ? 12.634  219.836 26.961  1.00 48.40  ? 100 GLU D CG  1 
ATOM   4111  C  CD  . GLU D  1 101 ? 13.670  220.566 27.784  1.00 59.39  ? 100 GLU D CD  1 
ATOM   4112  O  OE1 . GLU D  1 101 ? 13.222  221.248 28.769  1.00 54.84  ? 100 GLU D OE1 1 
ATOM   4113  O  OE2 . GLU D  1 101 ? 14.893  220.412 27.436  1.00 57.81  ? 100 GLU D OE2 1 
ATOM   4114  N  N   . ASP D  1 102 ? 9.410   218.676 26.336  1.00 28.09  ? 101 ASP D N   1 
ATOM   4115  C  CA  . ASP D  1 102 ? 8.021   218.662 26.822  1.00 28.96  ? 101 ASP D CA  1 
ATOM   4116  C  C   . ASP D  1 102 ? 7.916   217.969 28.115  1.00 31.26  ? 101 ASP D C   1 
ATOM   4117  O  O   . ASP D  1 102 ? 8.573   216.948 28.292  1.00 34.90  ? 101 ASP D O   1 
ATOM   4118  C  CB  . ASP D  1 102 ? 7.046   217.993 25.838  1.00 29.68  ? 101 ASP D CB  1 
ATOM   4119  C  CG  . ASP D  1 102 ? 5.535   218.180 26.262  1.00 33.04  ? 101 ASP D CG  1 
ATOM   4120  O  OD1 . ASP D  1 102 ? 5.056   219.304 26.230  1.00 34.02  ? 101 ASP D OD1 1 
ATOM   4121  O  OD2 . ASP D  1 102 ? 4.822   217.203 26.641  1.00 33.73  ? 101 ASP D OD2 1 
ATOM   4122  N  N   . SER D  1 103 ? 7.008   218.431 28.977  1.00 32.04  ? 102 SER D N   1 
ATOM   4123  C  CA  . SER D  1 103 ? 6.913   217.861 30.345  1.00 35.01  ? 102 SER D CA  1 
ATOM   4124  C  C   . SER D  1 103 ? 5.627   217.186 30.713  1.00 32.81  ? 102 SER D C   1 
ATOM   4125  O  O   . SER D  1 103 ? 5.435   216.882 31.869  1.00 31.73  ? 102 SER D O   1 
ATOM   4126  C  CB  . SER D  1 103 ? 7.231   218.932 31.409  1.00 33.93  ? 102 SER D CB  1 
ATOM   4127  O  OG  . SER D  1 103 ? 8.615   219.010 31.475  1.00 38.67  ? 102 SER D OG  1 
ATOM   4128  N  N   . VAL D  1 104 ? 4.749   217.043 29.730  1.00 35.65  ? 103 VAL D N   1 
ATOM   4129  C  CA  . VAL D  1 104 ? 3.440   216.433 29.896  1.00 36.10  ? 103 VAL D CA  1 
ATOM   4130  C  C   . VAL D  1 104 ? 3.494   215.025 29.369  1.00 33.72  ? 103 VAL D C   1 
ATOM   4131  O  O   . VAL D  1 104 ? 3.139   214.152 30.083  1.00 35.65  ? 103 VAL D O   1 
ATOM   4132  C  CB  . VAL D  1 104 ? 2.262   217.291 29.369  1.00 33.03  ? 103 VAL D CB  1 
ATOM   4133  C  CG1 . VAL D  1 104 ? 0.972   216.505 29.313  1.00 29.69  ? 103 VAL D CG1 1 
ATOM   4134  C  CG2 . VAL D  1 104 ? 2.114   218.449 30.306  1.00 29.49  ? 103 VAL D CG2 1 
ATOM   4135  N  N   . ILE D  1 105 ? 3.977   214.811 28.165  1.00 36.80  ? 104 ILE D N   1 
ATOM   4136  C  CA  . ILE D  1 105 ? 4.358   213.438 27.749  1.00 35.20  ? 104 ILE D CA  1 
ATOM   4137  C  C   . ILE D  1 105 ? 5.471   212.802 28.634  1.00 32.62  ? 104 ILE D C   1 
ATOM   4138  O  O   . ILE D  1 105 ? 6.326   213.494 29.220  1.00 33.18  ? 104 ILE D O   1 
ATOM   4139  C  CB  . ILE D  1 105 ? 4.828   213.396 26.271  1.00 30.51  ? 104 ILE D CB  1 
ATOM   4140  C  CG1 . ILE D  1 105 ? 6.176   214.142 26.098  1.00 32.11  ? 104 ILE D CG1 1 
ATOM   4141  C  CG2 . ILE D  1 105 ? 3.694   213.798 25.334  1.00 27.30  ? 104 ILE D CG2 1 
ATOM   4142  C  CD1 . ILE D  1 105 ? 6.809   213.941 24.721  1.00 31.43  ? 104 ILE D CD1 1 
ATOM   4143  N  N   . SER D  1 106 ? 5.489   211.485 28.670  1.00 31.11  ? 105 SER D N   1 
ATOM   4144  C  CA  . SER D  1 106 ? 6.505   210.785 29.407  1.00 30.81  ? 105 SER D CA  1 
ATOM   4145  C  C   . SER D  1 106 ? 6.894   209.453 28.759  1.00 28.27  ? 105 SER D C   1 
ATOM   4146  O  O   . SER D  1 106 ? 6.116   208.895 28.015  1.00 27.75  ? 105 SER D O   1 
ATOM   4147  C  CB  . SER D  1 106 ? 5.920   210.488 30.793  1.00 28.50  ? 105 SER D CB  1 
ATOM   4148  O  OG  . SER D  1 106 ? 6.970   210.105 31.609  1.00 29.36  ? 105 SER D OG  1 
ATOM   4149  N  N   . LEU D  1 107 ? 8.049   208.933 29.149  1.00 27.43  ? 106 LEU D N   1 
ATOM   4150  C  CA  . LEU D  1 107 ? 8.375   207.530 28.874  1.00 29.80  ? 106 LEU D CA  1 
ATOM   4151  C  C   . LEU D  1 107 ? 7.968   206.482 29.937  1.00 31.86  ? 106 LEU D C   1 
ATOM   4152  O  O   . LEU D  1 107 ? 8.346   205.339 29.828  1.00 35.58  ? 106 LEU D O   1 
ATOM   4153  C  CB  . LEU D  1 107 ? 9.836   207.359 28.415  1.00 25.85  ? 106 LEU D CB  1 
ATOM   4154  C  CG  . LEU D  1 107 ? 10.327  208.399 27.368  1.00 28.80  ? 106 LEU D CG  1 
ATOM   4155  C  CD1 . LEU D  1 107 ? 11.622  207.920 26.793  1.00 29.69  ? 106 LEU D CD1 1 
ATOM   4156  C  CD2 . LEU D  1 107 ? 9.389   208.690 26.193  1.00 28.27  ? 106 LEU D CD2 1 
ATOM   4157  N  N   . SER D  1 108 ? 7.215   206.861 30.963  1.00 33.05  ? 107 SER D N   1 
ATOM   4158  C  CA  . SER D  1 108 ? 6.611   205.900 31.902  1.00 34.61  ? 107 SER D CA  1 
ATOM   4159  C  C   . SER D  1 108 ? 5.349   206.490 32.471  1.00 34.90  ? 107 SER D C   1 
ATOM   4160  O  O   . SER D  1 108 ? 5.013   207.653 32.195  1.00 36.51  ? 107 SER D O   1 
ATOM   4161  C  CB  . SER D  1 108 ? 7.557   205.532 33.025  1.00 31.84  ? 107 SER D CB  1 
ATOM   4162  O  OG  . SER D  1 108 ? 8.216   206.713 33.395  1.00 37.87  ? 107 SER D OG  1 
ATOM   4163  N  N   . GLY D  1 109 ? 4.653   205.668 33.246  1.00 34.40  ? 108 GLY D N   1 
ATOM   4164  C  CA  . GLY D  1 109 ? 3.449   206.070 33.935  1.00 30.58  ? 108 GLY D CA  1 
ATOM   4165  C  C   . GLY D  1 109 ? 2.262   206.257 33.023  1.00 32.33  ? 108 GLY D C   1 
ATOM   4166  O  O   . GLY D  1 109 ? 2.216   205.773 31.916  1.00 33.46  ? 108 GLY D O   1 
ATOM   4167  N  N   . ASP D  1 110 ? 1.287   206.973 33.522  1.00 34.02  ? 109 ASP D N   1 
ATOM   4168  C  CA  . ASP D  1 110 ? 0.038   207.200 32.844  1.00 37.01  ? 109 ASP D CA  1 
ATOM   4169  C  C   . ASP D  1 110 ? 0.154   207.900 31.478  1.00 38.93  ? 109 ASP D C   1 
ATOM   4170  O  O   . ASP D  1 110 ? -0.674  207.713 30.610  1.00 37.25  ? 109 ASP D O   1 
ATOM   4171  C  CB  . ASP D  1 110 ? -0.762  208.143 33.730  1.00 40.37  ? 109 ASP D CB  1 
ATOM   4172  C  CG  . ASP D  1 110 ? -1.431  207.454 34.855  1.00 45.86  ? 109 ASP D CG  1 
ATOM   4173  O  OD1 . ASP D  1 110 ? -1.268  206.207 34.897  1.00 48.11  ? 109 ASP D OD1 1 
ATOM   4174  O  OD2 . ASP D  1 110 ? -2.109  208.175 35.678  1.00 42.87  ? 109 ASP D OD2 1 
ATOM   4175  N  N   . HIS D  1 111 ? 1.176   208.734 31.362  1.00 36.93  ? 110 HIS D N   1 
ATOM   4176  C  CA  . HIS D  1 111 ? 1.372   209.617 30.273  1.00 37.17  ? 110 HIS D CA  1 
ATOM   4177  C  C   . HIS D  1 111 ? 2.410   209.073 29.326  1.00 32.95  ? 110 HIS D C   1 
ATOM   4178  O  O   . HIS D  1 111 ? 2.899   209.765 28.473  1.00 33.01  ? 110 HIS D O   1 
ATOM   4179  C  CB  . HIS D  1 111 ? 1.729   211.013 30.793  1.00 34.40  ? 110 HIS D CB  1 
ATOM   4180  C  CG  . HIS D  1 111 ? 0.558   211.699 31.410  1.00 40.51  ? 110 HIS D CG  1 
ATOM   4181  N  ND1 . HIS D  1 111 ? 0.645   212.911 32.074  1.00 43.63  ? 110 HIS D ND1 1 
ATOM   4182  C  CD2 . HIS D  1 111 ? -0.742  211.313 31.503  1.00 42.62  ? 110 HIS D CD2 1 
ATOM   4183  C  CE1 . HIS D  1 111 ? -0.552  213.257 32.524  1.00 38.90  ? 110 HIS D CE1 1 
ATOM   4184  N  NE2 . HIS D  1 111 ? -1.411  212.303 32.194  1.00 39.66  ? 110 HIS D NE2 1 
ATOM   4185  N  N   . CYS D  1 112 ? 2.755   207.834 29.519  1.00 31.40  ? 111 CYS D N   1 
ATOM   4186  C  CA  . CYS D  1 112 ? 3.684   207.180 28.671  1.00 30.72  ? 111 CYS D CA  1 
ATOM   4187  C  C   . CYS D  1 112 ? 3.138   207.119 27.260  1.00 31.24  ? 111 CYS D C   1 
ATOM   4188  O  O   . CYS D  1 112 ? 1.944   206.769 27.001  1.00 30.26  ? 111 CYS D O   1 
ATOM   4189  C  CB  . CYS D  1 112 ? 3.754   205.767 29.109  1.00 29.86  ? 111 CYS D CB  1 
ATOM   4190  S  SG  . CYS D  1 112 ? 5.192   204.974 28.454  1.00 36.47  ? 111 CYS D SG  1 
ATOM   4191  N  N   . ILE D  1 113 ? 4.035   207.440 26.354  1.00 31.58  ? 112 ILE D N   1 
ATOM   4192  C  CA  . ILE D  1 113 ? 3.753   207.468 24.932  1.00 31.23  ? 112 ILE D CA  1 
ATOM   4193  C  C   . ILE D  1 113 ? 4.445   206.329 24.142  1.00 32.87  ? 112 ILE D C   1 
ATOM   4194  O  O   . ILE D  1 113 ? 4.292   206.279 22.908  1.00 34.32  ? 112 ILE D O   1 
ATOM   4195  C  CB  . ILE D  1 113 ? 4.127   208.871 24.338  1.00 32.14  ? 112 ILE D CB  1 
ATOM   4196  C  CG1 . ILE D  1 113 ? 5.631   209.147 24.515  1.00 30.13  ? 112 ILE D CG1 1 
ATOM   4197  C  CG2 . ILE D  1 113 ? 3.200   209.989 24.838  1.00 22.71  ? 112 ILE D CG2 1 
ATOM   4198  C  CD1 . ILE D  1 113 ? 6.172   210.175 23.550  1.00 28.49  ? 112 ILE D CD1 1 
ATOM   4199  N  N   . ILE D  1 114 ? 5.186   205.425 24.834  1.00 33.39  ? 113 ILE D N   1 
ATOM   4200  C  CA  . ILE D  1 114 ? 5.861   204.279 24.222  1.00 29.94  ? 113 ILE D CA  1 
ATOM   4201  C  C   . ILE D  1 114 ? 4.746   203.393 23.818  1.00 32.33  ? 113 ILE D C   1 
ATOM   4202  O  O   . ILE D  1 114 ? 3.802   203.199 24.563  1.00 33.44  ? 113 ILE D O   1 
ATOM   4203  C  CB  . ILE D  1 114 ? 6.672   203.462 25.221  1.00 30.89  ? 113 ILE D CB  1 
ATOM   4204  C  CG1 . ILE D  1 114 ? 7.856   204.227 25.884  1.00 31.87  ? 113 ILE D CG1 1 
ATOM   4205  C  CG2 . ILE D  1 114 ? 7.080   202.123 24.667  1.00 29.14  ? 113 ILE D CG2 1 
ATOM   4206  C  CD1 . ILE D  1 114 ? 8.907   204.797 25.026  1.00 26.48  ? 113 ILE D CD1 1 
ATOM   4207  N  N   . GLY D  1 115 ? 4.808   202.929 22.586  1.00 33.06  ? 114 GLY D N   1 
ATOM   4208  C  CA  . GLY D  1 115 ? 3.782   202.070 22.046  1.00 30.06  ? 114 GLY D CA  1 
ATOM   4209  C  C   . GLY D  1 115 ? 2.580   202.798 21.457  1.00 31.09  ? 114 GLY D C   1 
ATOM   4210  O  O   . GLY D  1 115 ? 1.568   202.151 21.066  1.00 30.71  ? 114 GLY D O   1 
ATOM   4211  N  N   . ARG D  1 116 ? 2.677   204.120 21.389  1.00 27.05  ? 115 ARG D N   1 
ATOM   4212  C  CA  . ARG D  1 116 ? 1.649   204.899 20.788  1.00 28.43  ? 115 ARG D CA  1 
ATOM   4213  C  C   . ARG D  1 116 ? 2.185   205.489 19.466  1.00 29.95  ? 115 ARG D C   1 
ATOM   4214  O  O   . ARG D  1 116 ? 3.315   205.230 19.093  1.00 34.32  ? 115 ARG D O   1 
ATOM   4215  C  CB  . ARG D  1 116 ? 1.205   205.967 21.773  1.00 30.09  ? 115 ARG D CB  1 
ATOM   4216  C  CG  . ARG D  1 116 ? 0.891   205.472 23.148  1.00 29.09  ? 115 ARG D CG  1 
ATOM   4217  C  CD  . ARG D  1 116 ? -0.251  206.222 23.799  1.00 33.34  ? 115 ARG D CD  1 
ATOM   4218  N  NE  . ARG D  1 116 ? -0.552  205.688 25.145  1.00 33.66  ? 115 ARG D NE  1 
ATOM   4219  C  CZ  . ARG D  1 116 ? -1.681  205.071 25.549  1.00 30.54  ? 115 ARG D CZ  1 
ATOM   4220  N  NH1 . ARG D  1 116 ? -2.770  204.884 24.792  1.00 26.89  ? 115 ARG D NH1 1 
ATOM   4221  N  NH2 . ARG D  1 116 ? -1.745  204.689 26.794  1.00 32.13  ? 115 ARG D NH2 1 
ATOM   4222  N  N   . THR D  1 117 ? 1.393   206.235 18.724  1.00 29.76  ? 116 THR D N   1 
ATOM   4223  C  CA  . THR D  1 117 ? 1.810   206.649 17.398  1.00 29.13  ? 116 THR D CA  1 
ATOM   4224  C  C   . THR D  1 117 ? 2.161   208.111 17.289  1.00 28.02  ? 116 THR D C   1 
ATOM   4225  O  O   . THR D  1 117 ? 1.376   208.940 17.695  1.00 30.35  ? 116 THR D O   1 
ATOM   4226  C  CB  . THR D  1 117 ? 0.772   206.255 16.349  1.00 28.28  ? 116 THR D CB  1 
ATOM   4227  O  OG1 . THR D  1 117 ? 0.655   204.863 16.335  1.00 29.38  ? 116 THR D OG1 1 
ATOM   4228  C  CG2 . THR D  1 117 ? 1.105   206.711 14.911  1.00 23.62  ? 116 THR D CG2 1 
ATOM   4229  N  N   . LEU D  1 118 ? 3.329   208.399 16.725  1.00 26.00  ? 117 LEU D N   1 
ATOM   4230  C  CA  . LEU D  1 118 ? 3.728   209.738 16.488  1.00 25.04  ? 117 LEU D CA  1 
ATOM   4231  C  C   . LEU D  1 118 ? 3.256   210.068 15.042  1.00 27.51  ? 117 LEU D C   1 
ATOM   4232  O  O   . LEU D  1 118 ? 3.523   209.314 14.105  1.00 27.43  ? 117 LEU D O   1 
ATOM   4233  C  CB  . LEU D  1 118 ? 5.220   209.856 16.664  1.00 21.96  ? 117 LEU D CB  1 
ATOM   4234  C  CG  . LEU D  1 118 ? 5.767   211.219 16.277  1.00 22.45  ? 117 LEU D CG  1 
ATOM   4235  C  CD1 . LEU D  1 118 ? 5.161   212.306 17.168  1.00 24.53  ? 117 LEU D CD1 1 
ATOM   4236  C  CD2 . LEU D  1 118 ? 7.263   211.284 16.348  1.00 22.59  ? 117 LEU D CD2 1 
ATOM   4237  N  N   . VAL D  1 119 ? 2.487   211.128 14.882  1.00 25.83  ? 118 VAL D N   1 
ATOM   4238  C  CA  . VAL D  1 119 ? 1.990   211.559 13.594  1.00 25.42  ? 118 VAL D CA  1 
ATOM   4239  C  C   . VAL D  1 119 ? 2.400   212.961 13.192  1.00 26.61  ? 118 VAL D C   1 
ATOM   4240  O  O   . VAL D  1 119 ? 2.197   213.902 13.973  1.00 24.79  ? 118 VAL D O   1 
ATOM   4241  C  CB  . VAL D  1 119 ? 0.457   211.512 13.568  1.00 24.57  ? 118 VAL D CB  1 
ATOM   4242  C  CG1 . VAL D  1 119 ? -0.067  211.851 12.201  1.00 21.17  ? 118 VAL D CG1 1 
ATOM   4243  C  CG2 . VAL D  1 119 ? -0.003  210.154 14.019  1.00 23.22  ? 118 VAL D CG2 1 
ATOM   4244  N  N   . VAL D  1 120 ? 2.915   213.114 11.963  1.00 26.89  ? 119 VAL D N   1 
ATOM   4245  C  CA  . VAL D  1 120 ? 3.124   214.459 11.416  1.00 27.40  ? 119 VAL D CA  1 
ATOM   4246  C  C   . VAL D  1 120 ? 2.018   214.854 10.409  1.00 27.62  ? 119 VAL D C   1 
ATOM   4247  O  O   . VAL D  1 120 ? 1.614   214.092 9.566   1.00 26.78  ? 119 VAL D O   1 
ATOM   4248  C  CB  . VAL D  1 120 ? 4.561   214.727 10.911  1.00 29.00  ? 119 VAL D CB  1 
ATOM   4249  C  CG1 . VAL D  1 120 ? 4.921   213.780 9.760   1.00 29.19  ? 119 VAL D CG1 1 
ATOM   4250  C  CG2 . VAL D  1 120 ? 4.739   216.155 10.436  1.00 27.09  ? 119 VAL D CG2 1 
ATOM   4251  N  N   . HIS D  1 121 ? 1.507   216.056 10.582  1.00 30.20  ? 120 HIS D N   1 
ATOM   4252  C  CA  . HIS D  1 121 ? 0.314   216.502 9.870   1.00 30.50  ? 120 HIS D CA  1 
ATOM   4253  C  C   . HIS D  1 121 ? 0.556   217.435 8.693   1.00 31.78  ? 120 HIS D C   1 
ATOM   4254  O  O   . HIS D  1 121 ? 1.626   218.074 8.556   1.00 30.45  ? 120 HIS D O   1 
ATOM   4255  C  CB  . HIS D  1 121 ? -0.708  217.093 10.805  1.00 26.59  ? 120 HIS D CB  1 
ATOM   4256  C  CG  . HIS D  1 121 ? -1.355  216.077 11.662  1.00 30.10  ? 120 HIS D CG  1 
ATOM   4257  N  ND1 . HIS D  1 121 ? -2.610  215.565 11.390  1.00 31.18  ? 120 HIS D ND1 1 
ATOM   4258  C  CD2 . HIS D  1 121 ? -0.913  215.443 12.775  1.00 26.49  ? 120 HIS D CD2 1 
ATOM   4259  C  CE1 . HIS D  1 121 ? -2.931  214.697 12.331  1.00 26.19  ? 120 HIS D CE1 1 
ATOM   4260  N  NE2 . HIS D  1 121 ? -1.928  214.626 13.190  1.00 28.76  ? 120 HIS D NE2 1 
ATOM   4261  N  N   . GLU D  1 122 ? -0.447  217.420 7.824   1.00 31.57  ? 121 GLU D N   1 
ATOM   4262  C  CA  . GLU D  1 122 ? -0.538  218.180 6.618   1.00 33.36  ? 121 GLU D CA  1 
ATOM   4263  C  C   . GLU D  1 122 ? -0.391  219.689 6.831   1.00 35.65  ? 121 GLU D C   1 
ATOM   4264  O  O   . GLU D  1 122 ? 0.410   220.326 6.193   1.00 36.60  ? 121 GLU D O   1 
ATOM   4265  C  CB  . GLU D  1 122 ? -1.925  217.892 6.112   1.00 36.28  ? 121 GLU D CB  1 
ATOM   4266  C  CG  . GLU D  1 122 ? -2.167  218.224 4.645   1.00 44.43  ? 121 GLU D CG  1 
ATOM   4267  C  CD  . GLU D  1 122 ? -3.657  218.516 4.391   1.00 56.70  ? 121 GLU D CD  1 
ATOM   4268  O  OE1 . GLU D  1 122 ? -4.618  218.115 5.184   1.00 47.53  ? 121 GLU D OE1 1 
ATOM   4269  O  OE2 . GLU D  1 122 ? -3.884  219.201 3.377   1.00 61.62  ? 121 GLU D OE2 1 
ATOM   4270  N  N   . LYS D  1 123 ? -1.157  220.234 7.759   1.00 34.60  ? 122 LYS D N   1 
ATOM   4271  C  CA  . LYS D  1 123 ? -1.228  221.665 7.961   1.00 36.85  ? 122 LYS D CA  1 
ATOM   4272  C  C   . LYS D  1 123 ? -0.714  222.066 9.351   1.00 34.02  ? 122 LYS D C   1 
ATOM   4273  O  O   . LYS D  1 123 ? -0.372  221.249 10.156  1.00 34.60  ? 122 LYS D O   1 
ATOM   4274  C  CB  . LYS D  1 123 ? -2.684  222.180 7.853   1.00 36.37  ? 122 LYS D CB  1 
ATOM   4275  C  CG  . LYS D  1 123 ? -3.435  222.020 6.567   1.00 36.56  ? 122 LYS D CG  1 
ATOM   4276  C  CD  . LYS D  1 123 ? -4.833  221.692 7.013   1.00 43.28  ? 122 LYS D CD  1 
ATOM   4277  C  CE  . LYS D  1 123 ? -5.966  222.570 6.461   1.00 50.49  ? 122 LYS D CE  1 
ATOM   4278  N  NZ  . LYS D  1 123 ? -6.673  221.919 5.305   1.00 50.53  ? 122 LYS D NZ  1 
ATOM   4279  N  N   . ALA D  1 124 ? -0.698  223.366 9.600   1.00 33.05  ? 123 ALA D N   1 
ATOM   4280  C  CA  . ALA D  1 124 ? -0.420  223.924 10.888  1.00 31.40  ? 123 ALA D CA  1 
ATOM   4281  C  C   . ALA D  1 124 ? -1.498  223.599 11.879  1.00 29.66  ? 123 ALA D C   1 
ATOM   4282  O  O   . ALA D  1 124 ? -2.697  223.572 11.527  1.00 26.46  ? 123 ALA D O   1 
ATOM   4283  C  CB  . ALA D  1 124 ? -0.295  225.404 10.777  1.00 28.09  ? 123 ALA D CB  1 
ATOM   4284  N  N   . ASP D  1 125 ? -1.051  223.315 13.104  1.00 27.14  ? 124 ASP D N   1 
ATOM   4285  C  CA  . ASP D  1 125 ? -1.928  223.122 14.200  1.00 27.39  ? 124 ASP D CA  1 
ATOM   4286  C  C   . ASP D  1 125 ? -2.176  224.502 14.807  1.00 26.83  ? 124 ASP D C   1 
ATOM   4287  O  O   . ASP D  1 125 ? -1.233  225.225 15.108  1.00 31.83  ? 124 ASP D O   1 
ATOM   4288  C  CB  . ASP D  1 125 ? -1.269  222.202 15.168  1.00 28.25  ? 124 ASP D CB  1 
ATOM   4289  C  CG  . ASP D  1 125 ? -2.018  222.073 16.485  1.00 28.06  ? 124 ASP D CG  1 
ATOM   4290  O  OD1 . ASP D  1 125 ? -3.041  222.722 16.803  1.00 29.55  ? 124 ASP D OD1 1 
ATOM   4291  O  OD2 . ASP D  1 125 ? -1.544  221.258 17.234  1.00 29.42  ? 124 ASP D OD2 1 
ATOM   4292  N  N   . ASP D  1 126 ? -3.436  224.871 14.956  1.00 26.65  ? 125 ASP D N   1 
ATOM   4293  C  CA  . ASP D  1 126 ? -3.815  226.211 15.462  1.00 28.06  ? 125 ASP D CA  1 
ATOM   4294  C  C   . ASP D  1 126 ? -3.832  226.339 16.980  1.00 29.60  ? 125 ASP D C   1 
ATOM   4295  O  O   . ASP D  1 126 ? -4.208  227.364 17.480  1.00 28.44  ? 125 ASP D O   1 
ATOM   4296  C  CB  . ASP D  1 126 ? -5.122  226.704 14.874  1.00 23.77  ? 125 ASP D CB  1 
ATOM   4297  C  CG  . ASP D  1 126 ? -6.341  225.936 15.386  1.00 28.31  ? 125 ASP D CG  1 
ATOM   4298  O  OD1 . ASP D  1 126 ? -6.380  225.173 16.463  1.00 25.96  ? 125 ASP D OD1 1 
ATOM   4299  O  OD2 . ASP D  1 126 ? -7.297  226.115 14.646  1.00 29.03  ? 125 ASP D OD2 1 
ATOM   4300  N  N   . LEU D  1 127 ? -3.409  225.273 17.680  1.00 33.93  ? 126 LEU D N   1 
ATOM   4301  C  CA  . LEU D  1 127 ? -3.198  225.257 19.127  1.00 29.94  ? 126 LEU D CA  1 
ATOM   4302  C  C   . LEU D  1 127 ? -4.495  225.531 19.917  1.00 29.96  ? 126 LEU D C   1 
ATOM   4303  O  O   . LEU D  1 127 ? -4.494  225.982 21.073  1.00 29.68  ? 126 LEU D O   1 
ATOM   4304  C  CB  . LEU D  1 127 ? -1.987  226.110 19.505  1.00 31.32  ? 126 LEU D CB  1 
ATOM   4305  C  CG  . LEU D  1 127 ? -0.706  225.998 18.629  1.00 30.72  ? 126 LEU D CG  1 
ATOM   4306  C  CD1 . LEU D  1 127 ? 0.282   227.094 18.926  1.00 27.44  ? 126 LEU D CD1 1 
ATOM   4307  C  CD2 . LEU D  1 127 ? -0.007  224.641 18.658  1.00 30.50  ? 126 LEU D CD2 1 
ATOM   4308  N  N   . GLY D  1 128 ? -5.591  225.124 19.275  1.00 29.86  ? 127 GLY D N   1 
ATOM   4309  C  CA  . GLY D  1 128 ? -6.903  225.243 19.813  1.00 31.24  ? 127 GLY D CA  1 
ATOM   4310  C  C   . GLY D  1 128 ? -7.469  226.646 19.804  1.00 29.19  ? 127 GLY D C   1 
ATOM   4311  O  O   . GLY D  1 128 ? -8.419  226.913 20.525  1.00 28.81  ? 127 GLY D O   1 
ATOM   4312  N  N   . LYS D  1 129 ? -6.885  227.518 18.997  1.00 28.37  ? 128 LYS D N   1 
ATOM   4313  C  CA  . LYS D  1 129 ? -7.272  228.930 18.892  1.00 30.71  ? 128 LYS D CA  1 
ATOM   4314  C  C   . LYS D  1 129 ? -8.045  229.303 17.641  1.00 31.66  ? 128 LYS D C   1 
ATOM   4315  O  O   . LYS D  1 129 ? -8.192  230.481 17.343  1.00 34.66  ? 128 LYS D O   1 
ATOM   4316  C  CB  . LYS D  1 129 ? -6.066  229.821 18.996  1.00 30.22  ? 128 LYS D CB  1 
ATOM   4317  C  CG  . LYS D  1 129 ? -5.381  229.567 20.349  1.00 37.05  ? 128 LYS D CG  1 
ATOM   4318  C  CD  . LYS D  1 129 ? -3.989  230.187 20.427  1.00 38.10  ? 128 LYS D CD  1 
ATOM   4319  C  CE  . LYS D  1 129 ? -4.002  231.659 20.836  1.00 41.60  ? 128 LYS D CE  1 
ATOM   4320  N  NZ  . LYS D  1 129 ? -2.791  232.361 20.304  1.00 45.33  ? 128 LYS D NZ  1 
ATOM   4321  N  N   . GLY D  1 130 ? -8.556  228.305 16.928  1.00 29.38  ? 129 GLY D N   1 
ATOM   4322  C  CA  . GLY D  1 130 ? -9.269  228.531 15.709  1.00 28.79  ? 129 GLY D CA  1 
ATOM   4323  C  C   . GLY D  1 130 ? -10.736 228.842 15.869  1.00 30.47  ? 129 GLY D C   1 
ATOM   4324  O  O   . GLY D  1 130 ? -11.340 229.268 14.905  1.00 31.83  ? 129 GLY D O   1 
ATOM   4325  N  N   . GLY D  1 131 ? -11.317 228.627 17.051  1.00 28.97  ? 130 GLY D N   1 
ATOM   4326  C  CA  . GLY D  1 131 ? -12.697 229.007 17.284  1.00 29.48  ? 130 GLY D CA  1 
ATOM   4327  C  C   . GLY D  1 131 ? -13.787 228.202 16.572  1.00 30.61  ? 130 GLY D C   1 
ATOM   4328  O  O   . GLY D  1 131 ? -14.969 228.522 16.654  1.00 32.48  ? 130 GLY D O   1 
ATOM   4329  N  N   . ASN D  1 132 ? -13.425 227.112 15.921  1.00 32.10  ? 131 ASN D N   1 
ATOM   4330  C  CA  . ASN D  1 132 ? -14.432 226.197 15.403  1.00 32.78  ? 131 ASN D CA  1 
ATOM   4331  C  C   . ASN D  1 132 ? -14.393 224.867 16.201  1.00 35.02  ? 131 ASN D C   1 
ATOM   4332  O  O   . ASN D  1 132 ? -13.497 224.685 16.998  1.00 38.08  ? 131 ASN D O   1 
ATOM   4333  C  CB  . ASN D  1 132 ? -14.278 226.078 13.879  1.00 28.63  ? 131 ASN D CB  1 
ATOM   4334  C  CG  . ASN D  1 132 ? -13.021 225.306 13.454  1.00 30.30  ? 131 ASN D CG  1 
ATOM   4335  O  OD1 . ASN D  1 132 ? -12.048 225.083 14.199  1.00 30.74  ? 131 ASN D OD1 1 
ATOM   4336  N  ND2 . ASN D  1 132 ? -13.064 224.878 12.236  1.00 30.57  ? 131 ASN D ND2 1 
ATOM   4337  N  N   . GLU D  1 133 ? -15.329 223.941 16.008  1.00 37.38  ? 132 GLU D N   1 
ATOM   4338  C  CA  . GLU D  1 133 ? -15.281 222.715 16.774  1.00 33.17  ? 132 GLU D CA  1 
ATOM   4339  C  C   . GLU D  1 133 ? -14.003 221.940 16.457  1.00 33.94  ? 132 GLU D C   1 
ATOM   4340  O  O   . GLU D  1 133 ? -13.387 221.296 17.332  1.00 33.19  ? 132 GLU D O   1 
ATOM   4341  C  CB  . GLU D  1 133 ? -16.468 221.855 16.417  1.00 37.65  ? 132 GLU D CB  1 
ATOM   4342  C  CG  . GLU D  1 133 ? -17.889 222.378 16.684  1.00 47.46  ? 132 GLU D CG  1 
ATOM   4343  C  CD  . GLU D  1 133 ? -18.950 221.504 15.941  1.00 57.81  ? 132 GLU D CD  1 
ATOM   4344  O  OE1 . GLU D  1 133 ? -18.620 220.288 15.744  1.00 55.17  ? 132 GLU D OE1 1 
ATOM   4345  O  OE2 . GLU D  1 133 ? -20.064 222.004 15.508  1.00 47.55  ? 132 GLU D OE2 1 
ATOM   4346  N  N   . GLU D  1 134 ? -13.586 221.982 15.198  1.00 33.68  ? 133 GLU D N   1 
ATOM   4347  C  CA  . GLU D  1 134 ? -12.428 221.216 14.827  1.00 35.94  ? 133 GLU D CA  1 
ATOM   4348  C  C   . GLU D  1 134 ? -11.145 221.622 15.628  1.00 37.36  ? 133 GLU D C   1 
ATOM   4349  O  O   . GLU D  1 134 ? -10.326 220.742 16.037  1.00 34.97  ? 133 GLU D O   1 
ATOM   4350  C  CB  . GLU D  1 134 ? -12.239 221.203 13.314  1.00 33.51  ? 133 GLU D CB  1 
ATOM   4351  C  CG  . GLU D  1 134 ? -11.454 220.012 12.772  1.00 38.67  ? 133 GLU D CG  1 
ATOM   4352  C  CD  . GLU D  1 134 ? -12.025 218.653 13.191  1.00 45.10  ? 133 GLU D CD  1 
ATOM   4353  O  OE1 . GLU D  1 134 ? -13.241 218.356 12.989  1.00 48.42  ? 133 GLU D OE1 1 
ATOM   4354  O  OE2 . GLU D  1 134 ? -11.260 217.865 13.766  1.00 41.49  ? 133 GLU D OE2 1 
ATOM   4355  N  N   . SER D  1 135 ? -11.003 222.929 15.873  1.00 34.26  ? 134 SER D N   1 
ATOM   4356  C  CA  . SER D  1 135 ? -9.913  223.433 16.634  1.00 33.30  ? 134 SER D CA  1 
ATOM   4357  C  C   . SER D  1 135 ? -9.772  222.806 18.024  1.00 34.69  ? 134 SER D C   1 
ATOM   4358  O  O   . SER D  1 135 ? -8.612  222.568 18.499  1.00 31.49  ? 134 SER D O   1 
ATOM   4359  C  CB  . SER D  1 135 ? -10.080 224.913 16.793  1.00 35.09  ? 134 SER D CB  1 
ATOM   4360  O  OG  . SER D  1 135 ? -8.974  225.460 17.472  1.00 30.34  ? 134 SER D OG  1 
ATOM   4361  N  N   . THR D  1 136 ? -10.909 222.517 18.672  1.00 30.78  ? 135 THR D N   1 
ATOM   4362  C  CA  . THR D  1 136 ? -10.827 221.988 20.040  1.00 34.88  ? 135 THR D CA  1 
ATOM   4363  C  C   . THR D  1 136 ? -10.518 220.460 20.062  1.00 33.26  ? 135 THR D C   1 
ATOM   4364  O  O   . THR D  1 136 ? -10.313 219.913 21.127  1.00 38.77  ? 135 THR D O   1 
ATOM   4365  C  CB  . THR D  1 136 ? -12.123 222.239 20.805  1.00 37.07  ? 135 THR D CB  1 
ATOM   4366  O  OG1 . THR D  1 136 ? -13.116 221.455 20.164  1.00 49.58  ? 135 THR D OG1 1 
ATOM   4367  C  CG2 . THR D  1 136 ? -12.646 223.642 20.628  1.00 35.29  ? 135 THR D CG2 1 
ATOM   4368  N  N   . LYS D  1 137 ? -10.565 219.803 18.897  1.00 32.60  ? 136 LYS D N   1 
ATOM   4369  C  CA  . LYS D  1 137 ? -10.227 218.376 18.653  1.00 35.42  ? 136 LYS D CA  1 
ATOM   4370  C  C   . LYS D  1 137 ? -8.842  218.147 17.995  1.00 33.72  ? 136 LYS D C   1 
ATOM   4371  O  O   . LYS D  1 137 ? -8.033  217.446 18.544  1.00 32.58  ? 136 LYS D O   1 
ATOM   4372  C  CB  . LYS D  1 137 ? -11.308 217.667 17.822  1.00 37.04  ? 136 LYS D CB  1 
ATOM   4373  C  CG  . LYS D  1 137 ? -12.702 217.641 18.478  1.00 44.31  ? 136 LYS D CG  1 
ATOM   4374  C  CD  . LYS D  1 137 ? -13.720 216.799 17.686  1.00 49.26  ? 136 LYS D CD  1 
ATOM   4375  C  CE  . LYS D  1 137 ? -14.775 217.655 16.997  1.00 51.21  ? 136 LYS D CE  1 
ATOM   4376  N  NZ  . LYS D  1 137 ? -16.144 217.049 16.779  1.00 55.41  ? 136 LYS D NZ  1 
ATOM   4377  N  N   . THR D  1 138 ? -8.547  218.780 16.872  1.00 32.80  ? 137 THR D N   1 
ATOM   4378  C  CA  . THR D  1 138 ? -7.339  218.444 16.149  1.00 33.56  ? 137 THR D CA  1 
ATOM   4379  C  C   . THR D  1 138 ? -6.466  219.630 15.807  1.00 32.52  ? 137 THR D C   1 
ATOM   4380  O  O   . THR D  1 138 ? -5.487  219.478 15.096  1.00 28.83  ? 137 THR D O   1 
ATOM   4381  C  CB  . THR D  1 138 ? -7.697  217.787 14.824  1.00 33.54  ? 137 THR D CB  1 
ATOM   4382  O  OG1 . THR D  1 138 ? -8.461  218.691 14.004  1.00 33.67  ? 137 THR D OG1 1 
ATOM   4383  C  CG2 . THR D  1 138 ? -8.504  216.564 15.074  1.00 31.17  ? 137 THR D CG2 1 
ATOM   4384  N  N   . GLY D  1 139 ? -6.882  220.808 16.294  1.00 35.99  ? 138 GLY D N   1 
ATOM   4385  C  CA  . GLY D  1 139 ? -6.330  222.107 15.928  1.00 31.63  ? 138 GLY D CA  1 
ATOM   4386  C  C   . GLY D  1 139 ? -6.239  222.379 14.439  1.00 29.89  ? 138 GLY D C   1 
ATOM   4387  O  O   . GLY D  1 139 ? -5.381  223.172 14.053  1.00 28.26  ? 138 GLY D O   1 
ATOM   4388  N  N   . ASN D  1 140 ? -7.103  221.723 13.640  1.00 27.76  ? 139 ASN D N   1 
ATOM   4389  C  CA  . ASN D  1 140 ? -7.269  221.906 12.181  1.00 27.64  ? 139 ASN D CA  1 
ATOM   4390  C  C   . ASN D  1 140 ? -6.027  221.506 11.408  1.00 29.93  ? 139 ASN D C   1 
ATOM   4391  O  O   . ASN D  1 140 ? -5.748  222.072 10.353  1.00 30.16  ? 139 ASN D O   1 
ATOM   4392  C  CB  . ASN D  1 140 ? -7.659  223.352 11.811  1.00 27.12  ? 139 ASN D CB  1 
ATOM   4393  C  CG  . ASN D  1 140 ? -9.073  223.710 12.261  1.00 30.72  ? 139 ASN D CG  1 
ATOM   4394  O  OD1 . ASN D  1 140 ? -10.034 223.158 11.777  1.00 30.82  ? 139 ASN D OD1 1 
ATOM   4395  N  ND2 . ASN D  1 140 ? -9.188  224.587 13.266  1.00 32.38  ? 139 ASN D ND2 1 
ATOM   4396  N  N   . ALA D  1 141 ? -5.259  220.565 11.943  1.00 28.14  ? 140 ALA D N   1 
ATOM   4397  C  CA  . ALA D  1 141 ? -4.017  220.247 11.368  1.00 27.03  ? 140 ALA D CA  1 
ATOM   4398  C  C   . ALA D  1 141 ? -4.128  219.333 10.126  1.00 29.37  ? 140 ALA D C   1 
ATOM   4399  O  O   . ALA D  1 141 ? -3.113  219.146 9.384   1.00 30.52  ? 140 ALA D O   1 
ATOM   4400  C  CB  . ALA D  1 141 ? -3.151  219.672 12.426  1.00 26.44  ? 140 ALA D CB  1 
ATOM   4401  N  N   . GLY D  1 142 ? -5.345  218.823 9.886   1.00 26.84  ? 141 GLY D N   1 
ATOM   4402  C  CA  . GLY D  1 142 ? -5.657  218.032 8.714   1.00 25.38  ? 141 GLY D CA  1 
ATOM   4403  C  C   . GLY D  1 142 ? -5.042  216.636 8.685   1.00 29.08  ? 141 GLY D C   1 
ATOM   4404  O  O   . GLY D  1 142 ? -4.854  215.932 9.698   1.00 27.37  ? 141 GLY D O   1 
ATOM   4405  N  N   . SER D  1 143 ? -4.680  216.250 7.488   1.00 29.97  ? 142 SER D N   1 
ATOM   4406  C  CA  . SER D  1 143 ? -4.391  214.874 7.249   1.00 30.56  ? 142 SER D CA  1 
ATOM   4407  C  C   . SER D  1 143 ? -3.026  214.336 7.819   1.00 31.73  ? 142 SER D C   1 
ATOM   4408  O  O   . SER D  1 143 ? -2.137  215.095 8.262   1.00 32.74  ? 142 SER D O   1 
ATOM   4409  C  CB  . SER D  1 143 ? -4.741  214.528 5.798   1.00 26.97  ? 142 SER D CB  1 
ATOM   4410  O  OG  . SER D  1 143 ? -3.692  214.892 4.947   1.00 32.35  ? 142 SER D OG  1 
ATOM   4411  N  N   . ARG D  1 144 ? -2.922  213.009 7.885   1.00 29.60  ? 143 ARG D N   1 
ATOM   4412  C  CA  . ARG D  1 144 ? -1.793  212.403 8.494   1.00 31.33  ? 143 ARG D CA  1 
ATOM   4413  C  C   . ARG D  1 144 ? -0.807  212.086 7.369   1.00 30.76  ? 143 ARG D C   1 
ATOM   4414  O  O   . ARG D  1 144 ? -1.050  211.245 6.584   1.00 32.27  ? 143 ARG D O   1 
ATOM   4415  C  CB  . ARG D  1 144 ? -2.215  211.190 9.330   1.00 30.43  ? 143 ARG D CB  1 
ATOM   4416  C  CG  . ARG D  1 144 ? -3.500  211.471 10.063  1.00 31.07  ? 143 ARG D CG  1 
ATOM   4417  C  CD  . ARG D  1 144 ? -3.803  210.446 11.055  1.00 30.96  ? 143 ARG D CD  1 
ATOM   4418  N  NE  . ARG D  1 144 ? -4.965  210.844 11.780  1.00 32.48  ? 143 ARG D NE  1 
ATOM   4419  C  CZ  . ARG D  1 144 ? -5.476  210.188 12.828  1.00 32.52  ? 143 ARG D CZ  1 
ATOM   4420  N  NH1 . ARG D  1 144 ? -4.932  209.057 13.263  1.00 35.55  ? 143 ARG D NH1 1 
ATOM   4421  N  NH2 . ARG D  1 144 ? -6.556  210.654 13.446  1.00 29.05  ? 143 ARG D NH2 1 
ATOM   4422  N  N   . LEU D  1 145 ? 0.297   212.797 7.304   1.00 31.03  ? 144 LEU D N   1 
ATOM   4423  C  CA  . LEU D  1 145 ? 1.231   212.591 6.247   1.00 31.08  ? 144 LEU D CA  1 
ATOM   4424  C  C   . LEU D  1 145 ? 2.148   211.438 6.526   1.00 30.39  ? 144 LEU D C   1 
ATOM   4425  O  O   . LEU D  1 145 ? 2.476   210.775 5.622   1.00 35.28  ? 144 LEU D O   1 
ATOM   4426  C  CB  . LEU D  1 145 ? 2.002   213.857 5.984   1.00 30.01  ? 144 LEU D CB  1 
ATOM   4427  C  CG  . LEU D  1 145 ? 1.140   215.016 5.567   1.00 29.86  ? 144 LEU D CG  1 
ATOM   4428  C  CD1 . LEU D  1 145 ? 2.067   216.089 5.075   1.00 27.80  ? 144 LEU D CD1 1 
ATOM   4429  C  CD2 . LEU D  1 145 ? 0.110   214.750 4.493   1.00 24.89  ? 144 LEU D CD2 1 
ATOM   4430  N  N   . ALA D  1 146 ? 2.543   211.204 7.777   1.00 29.59  ? 145 ALA D N   1 
ATOM   4431  C  CA  . ALA D  1 146 ? 3.459   210.134 8.161   1.00 29.96  ? 145 ALA D CA  1 
ATOM   4432  C  C   . ALA D  1 146 ? 3.360   209.814 9.631   1.00 30.28  ? 145 ALA D C   1 
ATOM   4433  O  O   . ALA D  1 146 ? 3.055   210.666 10.432  1.00 35.62  ? 145 ALA D O   1 
ATOM   4434  C  CB  . ALA D  1 146 ? 4.900   210.440 7.756   1.00 23.91  ? 145 ALA D CB  1 
ATOM   4435  N  N   . CYS D  1 147 ? 3.604   208.581 9.984   1.00 30.88  ? 146 CYS D N   1 
ATOM   4436  C  CA  . CYS D  1 147 ? 3.432   208.143 11.330  1.00 30.26  ? 146 CYS D CA  1 
ATOM   4437  C  C   . CYS D  1 147 ? 4.335   206.964 11.620  1.00 30.65  ? 146 CYS D C   1 
ATOM   4438  O  O   . CYS D  1 147 ? 5.010   206.444 10.737  1.00 31.83  ? 146 CYS D O   1 
ATOM   4439  C  CB  . CYS D  1 147 ? 1.973   207.868 11.638  1.00 29.65  ? 146 CYS D CB  1 
ATOM   4440  S  SG  . CYS D  1 147 ? 1.286   206.545 10.685  1.00 37.09  ? 146 CYS D SG  1 
ATOM   4441  N  N   . GLY D  1 148 ? 4.373   206.591 12.885  1.00 29.94  ? 147 GLY D N   1 
ATOM   4442  C  CA  . GLY D  1 148 ? 5.154   205.450 13.355  1.00 28.58  ? 147 GLY D CA  1 
ATOM   4443  C  C   . GLY D  1 148 ? 4.787   205.128 14.787  1.00 30.28  ? 147 GLY D C   1 
ATOM   4444  O  O   . GLY D  1 148 ? 4.312   205.979 15.558  1.00 28.43  ? 147 GLY D O   1 
ATOM   4445  N  N   . VAL D  1 149 ? 5.035   203.889 15.141  1.00 30.56  ? 148 VAL D N   1 
ATOM   4446  C  CA  . VAL D  1 149 ? 4.882   203.456 16.483  1.00 29.85  ? 148 VAL D CA  1 
ATOM   4447  C  C   . VAL D  1 149 ? 6.139   203.815 17.283  1.00 28.97  ? 148 VAL D C   1 
ATOM   4448  O  O   . VAL D  1 149 ? 7.243   203.597 16.855  1.00 27.76  ? 148 VAL D O   1 
ATOM   4449  C  CB  . VAL D  1 149 ? 4.470   201.964 16.570  1.00 29.84  ? 148 VAL D CB  1 
ATOM   4450  C  CG1 . VAL D  1 149 ? 4.221   201.660 18.043  1.00 27.70  ? 148 VAL D CG1 1 
ATOM   4451  C  CG2 . VAL D  1 149 ? 3.238   201.654 15.669  1.00 23.77  ? 148 VAL D CG2 1 
ATOM   4452  N  N   . ILE D  1 150 ? 5.929   204.430 18.433  1.00 28.99  ? 149 ILE D N   1 
ATOM   4453  C  CA  . ILE D  1 150 ? 7.012   204.825 19.292  1.00 28.63  ? 149 ILE D CA  1 
ATOM   4454  C  C   . ILE D  1 150 ? 7.529   203.597 20.084  1.00 28.88  ? 149 ILE D C   1 
ATOM   4455  O  O   . ILE D  1 150 ? 6.814   203.091 20.915  1.00 28.94  ? 149 ILE D O   1 
ATOM   4456  C  CB  . ILE D  1 150 ? 6.539   205.940 20.242  1.00 28.20  ? 149 ILE D CB  1 
ATOM   4457  C  CG1 . ILE D  1 150 ? 6.012   207.129 19.424  1.00 25.89  ? 149 ILE D CG1 1 
ATOM   4458  C  CG2 . ILE D  1 150 ? 7.649   206.359 21.192  1.00 26.24  ? 149 ILE D CG2 1 
ATOM   4459  C  CD1 . ILE D  1 150 ? 5.322   208.182 20.232  1.00 26.25  ? 149 ILE D CD1 1 
ATOM   4460  N  N   . GLY D  1 151 ? 8.775   203.171 19.829  1.00 28.07  ? 150 GLY D N   1 
ATOM   4461  C  CA  . GLY D  1 151 ? 9.429   202.008 20.468  1.00 29.27  ? 150 GLY D CA  1 
ATOM   4462  C  C   . GLY D  1 151 ? 10.547  202.371 21.459  1.00 29.94  ? 150 GLY D C   1 
ATOM   4463  O  O   . GLY D  1 151 ? 11.154  203.435 21.380  1.00 25.70  ? 150 GLY D O   1 
ATOM   4464  N  N   . ILE D  1 152 ? 10.808  201.487 22.409  1.00 31.67  ? 151 ILE D N   1 
ATOM   4465  C  CA  . ILE D  1 152 ? 11.900  201.661 23.357  1.00 32.76  ? 151 ILE D CA  1 
ATOM   4466  C  C   . ILE D  1 152 ? 13.185  201.572 22.648  1.00 31.09  ? 151 ILE D C   1 
ATOM   4467  O  O   . ILE D  1 152 ? 13.373  200.660 21.874  1.00 36.10  ? 151 ILE D O   1 
ATOM   4468  C  CB  . ILE D  1 152 ? 11.915  200.546 24.424  1.00 39.91  ? 151 ILE D CB  1 
ATOM   4469  C  CG1 . ILE D  1 152 ? 10.603  200.620 25.187  1.00 41.29  ? 151 ILE D CG1 1 
ATOM   4470  C  CG2 . ILE D  1 152 ? 13.026  200.807 25.489  1.00 39.82  ? 151 ILE D CG2 1 
ATOM   4471  C  CD1 . ILE D  1 152 ? 10.212  199.300 25.778  1.00 50.12  ? 151 ILE D CD1 1 
ATOM   4472  N  N   . ALA D  1 153 ? 14.091  202.478 22.934  1.00 30.27  ? 152 ALA D N   1 
ATOM   4473  C  CA  . ALA D  1 153 ? 15.404  202.434 22.296  1.00 31.34  ? 152 ALA D CA  1 
ATOM   4474  C  C   . ALA D  1 153 ? 16.561  202.229 23.308  1.00 34.26  ? 152 ALA D C   1 
ATOM   4475  O  O   . ALA D  1 153 ? 16.450  202.475 24.525  1.00 34.17  ? 152 ALA D O   1 
ATOM   4476  C  CB  . ALA D  1 153 ? 15.619  203.677 21.494  1.00 28.87  ? 152 ALA D CB  1 
ATOM   4477  N  N   . GLN D  1 154 ? 17.676  201.756 22.793  1.00 36.46  ? 153 GLN D N   1 
ATOM   4478  C  CA  . GLN D  1 154 ? 18.866  201.552 23.599  1.00 41.26  ? 153 GLN D CA  1 
ATOM   4479  C  C   . GLN D  1 154 ? 19.557  202.873 23.790  1.00 48.58  ? 153 GLN D C   1 
ATOM   4480  O  O   . GLN D  1 154 ? 19.700  203.726 22.855  1.00 47.97  ? 153 GLN D O   1 
ATOM   4481  C  CB  . GLN D  1 154 ? 19.819  200.611 22.898  1.00 40.83  ? 153 GLN D CB  1 
ATOM   4482  C  CG  . GLN D  1 154 ? 21.040  200.253 23.715  1.00 43.55  ? 153 GLN D CG  1 
ATOM   4483  C  CD  . GLN D  1 154 ? 21.916  199.262 22.943  1.00 55.05  ? 153 GLN D CD  1 
ATOM   4484  O  OE1 . GLN D  1 154 ? 22.319  199.524 21.770  1.00 53.24  ? 153 GLN D OE1 1 
ATOM   4485  N  NE2 . GLN D  1 154 ? 22.215  198.108 23.577  1.00 51.02  ? 153 GLN D NE2 1 
ATOM   4486  O  OXT . GLN D  1 154 ? 19.965  203.115 24.937  1.00 63.64  ? 153 GLN D OXT 1 
ATOM   4487  N  N   . MET E  1 1   ? 27.452  252.048 39.386  1.00 56.06  ? 0   MET E N   1 
ATOM   4488  C  CA  . MET E  1 1   ? 26.381  251.811 40.407  1.00 54.95  ? 0   MET E CA  1 
ATOM   4489  C  C   . MET E  1 1   ? 26.848  252.523 41.703  1.00 60.66  ? 0   MET E C   1 
ATOM   4490  O  O   . MET E  1 1   ? 26.163  253.467 42.167  1.00 56.41  ? 0   MET E O   1 
ATOM   4491  C  CB  . MET E  1 1   ? 26.203  250.307 40.665  1.00 51.09  ? 0   MET E CB  1 
ATOM   4492  N  N   . ALA E  1 2   ? 27.969  252.086 42.324  1.00 48.68  ? 1   ALA E N   1 
ATOM   4493  C  CA  . ALA E  1 2   ? 28.196  252.595 43.716  1.00 47.14  ? 1   ALA E CA  1 
ATOM   4494  C  C   . ALA E  1 2   ? 29.226  253.728 43.750  1.00 42.68  ? 1   ALA E C   1 
ATOM   4495  O  O   . ALA E  1 2   ? 30.215  253.706 43.025  1.00 43.58  ? 1   ALA E O   1 
ATOM   4496  C  CB  . ALA E  1 2   ? 28.516  251.474 44.717  1.00 42.36  ? 1   ALA E CB  1 
ATOM   4497  N  N   . THR E  1 3   ? 28.923  254.768 44.489  1.00 40.02  ? 2   THR E N   1 
ATOM   4498  C  CA  . THR E  1 3   ? 29.806  255.897 44.602  1.00 37.37  ? 2   THR E CA  1 
ATOM   4499  C  C   . THR E  1 3   ? 30.326  256.037 46.059  1.00 39.63  ? 2   THR E C   1 
ATOM   4500  O  O   . THR E  1 3   ? 31.280  256.820 46.283  1.00 40.47  ? 2   THR E O   1 
ATOM   4501  C  CB  . THR E  1 3   ? 29.131  257.233 44.199  1.00 36.02  ? 2   THR E CB  1 
ATOM   4502  O  OG1 . THR E  1 3   ? 28.024  257.461 45.045  1.00 36.38  ? 2   THR E OG1 1 
ATOM   4503  C  CG2 . THR E  1 3   ? 28.702  257.304 42.742  1.00 31.97  ? 2   THR E CG2 1 
ATOM   4504  N  N   . LYS E  1 4   ? 29.717  255.309 47.013  1.00 36.01  ? 3   LYS E N   1 
ATOM   4505  C  CA  . LYS E  1 4   ? 30.132  255.312 48.381  1.00 35.99  ? 3   LYS E CA  1 
ATOM   4506  C  C   . LYS E  1 4   ? 30.205  253.968 49.066  1.00 35.17  ? 3   LYS E C   1 
ATOM   4507  O  O   . LYS E  1 4   ? 29.416  253.110 48.842  1.00 37.05  ? 3   LYS E O   1 
ATOM   4508  C  CB  . LYS E  1 4   ? 29.199  256.176 49.160  1.00 39.03  ? 3   LYS E CB  1 
ATOM   4509  C  CG  . LYS E  1 4   ? 29.542  257.634 49.155  1.00 45.68  ? 3   LYS E CG  1 
ATOM   4510  C  CD  . LYS E  1 4   ? 28.210  258.351 49.275  1.00 56.36  ? 3   LYS E CD  1 
ATOM   4511  C  CE  . LYS E  1 4   ? 28.332  259.764 49.865  1.00 63.59  ? 3   LYS E CE  1 
ATOM   4512  N  NZ  . LYS E  1 4   ? 27.041  260.467 49.523  1.00 59.77  ? 3   LYS E NZ  1 
ATOM   4513  N  N   . ALA E  1 5   ? 31.138  253.808 49.973  1.00 35.66  ? 4   ALA E N   1 
ATOM   4514  C  CA  . ALA E  1 5   ? 31.284  252.559 50.668  1.00 33.88  ? 4   ALA E CA  1 
ATOM   4515  C  C   . ALA E  1 5   ? 31.757  252.865 52.085  1.00 34.05  ? 4   ALA E C   1 
ATOM   4516  O  O   . ALA E  1 5   ? 32.204  253.957 52.345  1.00 33.42  ? 4   ALA E O   1 
ATOM   4517  C  CB  . ALA E  1 5   ? 32.252  251.646 49.919  1.00 27.82  ? 4   ALA E CB  1 
ATOM   4518  N  N   . VAL E  1 6   ? 31.599  251.913 53.011  1.00 35.57  ? 5   VAL E N   1 
ATOM   4519  C  CA  . VAL E  1 6   ? 32.033  252.096 54.374  1.00 33.08  ? 5   VAL E CA  1 
ATOM   4520  C  C   . VAL E  1 6   ? 32.618  250.789 54.945  1.00 35.83  ? 5   VAL E C   1 
ATOM   4521  O  O   . VAL E  1 6   ? 32.286  249.731 54.454  1.00 36.77  ? 5   VAL E O   1 
ATOM   4522  C  CB  . VAL E  1 6   ? 30.916  252.721 55.189  1.00 30.00  ? 5   VAL E CB  1 
ATOM   4523  C  CG1 . VAL E  1 6   ? 29.798  251.718 55.322  1.00 32.11  ? 5   VAL E CG1 1 
ATOM   4524  C  CG2 . VAL E  1 6   ? 31.459  253.231 56.506  1.00 28.38  ? 5   VAL E CG2 1 
ATOM   4525  N  N   . CYS E  1 7   ? 33.537  250.848 55.904  1.00 31.77  ? 6   CYS E N   1 
ATOM   4526  C  CA  . CYS E  1 7   ? 34.008  249.603 56.489  1.00 32.50  ? 6   CYS E CA  1 
ATOM   4527  C  C   . CYS E  1 7   ? 34.152  249.789 57.989  1.00 33.74  ? 6   CYS E C   1 
ATOM   4528  O  O   . CYS E  1 7   ? 34.753  250.746 58.430  1.00 30.63  ? 6   CYS E O   1 
ATOM   4529  C  CB  . CYS E  1 7   ? 35.368  249.241 55.926  1.00 34.22  ? 6   CYS E CB  1 
ATOM   4530  S  SG  . CYS E  1 7   ? 35.885  247.627 56.483  1.00 34.79  ? 6   CYS E SG  1 
ATOM   4531  N  N   . VAL E  1 8   ? 33.559  248.905 58.766  1.00 32.60  ? 7   VAL E N   1 
ATOM   4532  C  CA  . VAL E  1 8   ? 33.699  248.952 60.174  1.00 32.15  ? 7   VAL E CA  1 
ATOM   4533  C  C   . VAL E  1 8   ? 34.709  247.887 60.537  1.00 37.07  ? 7   VAL E C   1 
ATOM   4534  O  O   . VAL E  1 8   ? 34.526  246.700 60.205  1.00 37.72  ? 7   VAL E O   1 
ATOM   4535  C  CB  . VAL E  1 8   ? 32.359  248.636 60.811  1.00 35.69  ? 7   VAL E CB  1 
ATOM   4536  C  CG1 . VAL E  1 8   ? 32.504  248.581 62.335  1.00 31.24  ? 7   VAL E CG1 1 
ATOM   4537  C  CG2 . VAL E  1 8   ? 31.364  249.732 60.424  1.00 30.28  ? 7   VAL E CG2 1 
ATOM   4538  N  N   . LEU E  1 9   ? 35.820  248.298 61.138  1.00 36.12  ? 8   LEU E N   1 
ATOM   4539  C  CA  . LEU E  1 9   ? 36.858  247.339 61.511  1.00 35.11  ? 8   LEU E CA  1 
ATOM   4540  C  C   . LEU E  1 9   ? 36.760  246.863 62.986  1.00 35.77  ? 8   LEU E C   1 
ATOM   4541  O  O   . LEU E  1 9   ? 36.526  247.703 63.897  1.00 34.16  ? 8   LEU E O   1 
ATOM   4542  C  CB  . LEU E  1 9   ? 38.199  247.956 61.241  1.00 37.44  ? 8   LEU E CB  1 
ATOM   4543  C  CG  . LEU E  1 9   ? 38.576  248.542 59.871  1.00 39.58  ? 8   LEU E CG  1 
ATOM   4544  C  CD1 . LEU E  1 9   ? 39.279  249.823 60.168  1.00 39.70  ? 8   LEU E CD1 1 
ATOM   4545  C  CD2 . LEU E  1 9   ? 39.614  247.662 59.277  1.00 38.13  ? 8   LEU E CD2 1 
ATOM   4546  N  N   . LYS E  1 10  ? 36.886  245.534 63.198  1.00 31.57  ? 9   LYS E N   1 
ATOM   4547  C  CA  . LYS E  1 10  ? 36.871  244.926 64.513  1.00 31.50  ? 9   LYS E CA  1 
ATOM   4548  C  C   . LYS E  1 10  ? 37.858  243.858 64.493  1.00 34.01  ? 9   LYS E C   1 
ATOM   4549  O  O   . LYS E  1 10  ? 38.215  243.307 63.435  1.00 36.87  ? 9   LYS E O   1 
ATOM   4550  C  CB  . LYS E  1 10  ? 35.529  244.252 64.898  1.00 35.38  ? 9   LYS E CB  1 
ATOM   4551  C  CG  . LYS E  1 10  ? 34.337  245.154 64.876  1.00 40.27  ? 9   LYS E CG  1 
ATOM   4552  C  CD  . LYS E  1 10  ? 33.433  244.930 66.099  1.00 60.56  ? 9   LYS E CD  1 
ATOM   4553  C  CE  . LYS E  1 10  ? 32.688  246.235 66.562  1.00 66.00  ? 9   LYS E CE  1 
ATOM   4554  N  NZ  . LYS E  1 10  ? 31.429  246.538 65.790  1.00 53.28  ? 9   LYS E NZ  1 
ATOM   4555  N  N   . GLY E  1 11  ? 38.317  243.527 65.685  1.00 38.73  ? 10  GLY E N   1 
ATOM   4556  C  CA  . GLY E  1 11  ? 39.345  242.505 65.820  1.00 40.82  ? 10  GLY E CA  1 
ATOM   4557  C  C   . GLY E  1 11  ? 39.134  241.738 67.091  1.00 41.35  ? 10  GLY E C   1 
ATOM   4558  O  O   . GLY E  1 11  ? 38.150  241.998 67.829  1.00 39.40  ? 10  GLY E O   1 
ATOM   4559  N  N   . ASP E  1 12  ? 40.028  240.777 67.324  1.00 42.36  ? 11  ASP E N   1 
ATOM   4560  C  CA  . ASP E  1 12  ? 40.049  240.024 68.599  1.00 51.50  ? 11  ASP E CA  1 
ATOM   4561  C  C   . ASP E  1 12  ? 40.479  240.910 69.782  1.00 51.18  ? 11  ASP E C   1 
ATOM   4562  O  O   . ASP E  1 12  ? 40.017  240.690 70.892  1.00 46.65  ? 11  ASP E O   1 
ATOM   4563  C  CB  . ASP E  1 12  ? 40.887  238.727 68.492  1.00 54.14  ? 11  ASP E CB  1 
ATOM   4564  C  CG  . ASP E  1 12  ? 40.107  237.575 67.766  1.00 68.25  ? 11  ASP E CG  1 
ATOM   4565  O  OD1 . ASP E  1 12  ? 38.841  237.545 67.944  1.00 66.96  ? 11  ASP E OD1 1 
ATOM   4566  O  OD2 . ASP E  1 12  ? 40.730  236.732 67.017  1.00 61.45  ? 11  ASP E OD2 1 
ATOM   4567  N  N   . GLY E  1 13  ? 41.283  241.949 69.485  1.00 48.26  ? 12  GLY E N   1 
ATOM   4568  C  CA  . GLY E  1 13  ? 41.849  242.853 70.484  1.00 44.44  ? 12  GLY E CA  1 
ATOM   4569  C  C   . GLY E  1 13  ? 41.095  244.168 70.576  1.00 43.52  ? 12  GLY E C   1 
ATOM   4570  O  O   . GLY E  1 13  ? 39.857  244.210 70.366  1.00 47.01  ? 12  GLY E O   1 
ATOM   4571  N  N   . PRO E  1 14  ? 41.834  245.261 70.875  1.00 39.89  ? 13  PRO E N   1 
ATOM   4572  C  CA  . PRO E  1 14  ? 41.200  246.597 71.024  1.00 37.89  ? 13  PRO E CA  1 
ATOM   4573  C  C   . PRO E  1 14  ? 41.047  247.440 69.719  1.00 38.12  ? 13  PRO E C   1 
ATOM   4574  O  O   . PRO E  1 14  ? 40.404  248.498 69.755  1.00 37.16  ? 13  PRO E O   1 
ATOM   4575  C  CB  . PRO E  1 14  ? 42.157  247.309 71.967  1.00 33.33  ? 13  PRO E CB  1 
ATOM   4576  C  CG  . PRO E  1 14  ? 43.493  246.618 71.767  1.00 33.72  ? 13  PRO E CG  1 
ATOM   4577  C  CD  . PRO E  1 14  ? 43.296  245.293 71.146  1.00 35.96  ? 13  PRO E CD  1 
ATOM   4578  N  N   . VAL E  1 15  ? 41.643  247.002 68.613  1.00 32.67  ? 14  VAL E N   1 
ATOM   4579  C  CA  . VAL E  1 15  ? 41.737  247.851 67.450  1.00 36.44  ? 14  VAL E CA  1 
ATOM   4580  C  C   . VAL E  1 15  ? 40.403  247.932 66.743  1.00 38.47  ? 14  VAL E C   1 
ATOM   4581  O  O   . VAL E  1 15  ? 39.764  246.916 66.504  1.00 38.46  ? 14  VAL E O   1 
ATOM   4582  C  CB  . VAL E  1 15  ? 42.749  247.305 66.444  1.00 36.47  ? 14  VAL E CB  1 
ATOM   4583  C  CG1 . VAL E  1 15  ? 42.746  248.140 65.179  1.00 34.82  ? 14  VAL E CG1 1 
ATOM   4584  C  CG2 . VAL E  1 15  ? 44.135  247.178 67.071  1.00 33.09  ? 14  VAL E CG2 1 
ATOM   4585  N  N   . GLN E  1 16  ? 39.987  249.156 66.421  1.00 40.96  ? 15  GLN E N   1 
ATOM   4586  C  CA  . GLN E  1 16  ? 38.705  249.400 65.816  1.00 38.21  ? 15  GLN E CA  1 
ATOM   4587  C  C   . GLN E  1 16  ? 38.647  250.708 65.070  1.00 35.45  ? 15  GLN E C   1 
ATOM   4588  O  O   . GLN E  1 16  ? 39.358  251.662 65.380  1.00 36.02  ? 15  GLN E O   1 
ATOM   4589  C  CB  . GLN E  1 16  ? 37.597  249.268 66.874  1.00 41.75  ? 15  GLN E CB  1 
ATOM   4590  C  CG  . GLN E  1 16  ? 37.481  250.424 67.808  1.00 49.04  ? 15  GLN E CG  1 
ATOM   4591  C  CD  . GLN E  1 16  ? 36.533  250.094 68.985  1.00 64.20  ? 15  GLN E CD  1 
ATOM   4592  O  OE1 . GLN E  1 16  ? 35.579  250.846 69.292  1.00 61.85  ? 15  GLN E OE1 1 
ATOM   4593  N  NE2 . GLN E  1 16  ? 36.787  248.951 69.646  1.00 57.46  ? 15  GLN E NE2 1 
ATOM   4594  N  N   . GLY E  1 17  ? 37.778  250.749 64.071  1.00 35.33  ? 16  GLY E N   1 
ATOM   4595  C  CA  . GLY E  1 17  ? 37.559  251.970 63.299  1.00 32.59  ? 16  GLY E CA  1 
ATOM   4596  C  C   . GLY E  1 17  ? 36.563  251.940 62.145  1.00 32.85  ? 16  GLY E C   1 
ATOM   4597  O  O   . GLY E  1 17  ? 36.050  250.913 61.770  1.00 34.31  ? 16  GLY E O   1 
ATOM   4598  N  N   . ILE E  1 18  ? 36.384  253.104 61.539  1.00 34.87  ? 17  ILE E N   1 
ATOM   4599  C  CA  . ILE E  1 18  ? 35.405  253.382 60.523  1.00 34.79  ? 17  ILE E CA  1 
ATOM   4600  C  C   . ILE E  1 18  ? 36.165  253.990 59.339  1.00 36.99  ? 17  ILE E C   1 
ATOM   4601  O  O   . ILE E  1 18  ? 36.779  255.053 59.472  1.00 35.65  ? 17  ILE E O   1 
ATOM   4602  C  CB  . ILE E  1 18  ? 34.271  254.283 61.079  1.00 31.12  ? 17  ILE E CB  1 
ATOM   4603  C  CG1 . ILE E  1 18  ? 33.590  253.598 62.310  1.00 33.56  ? 17  ILE E CG1 1 
ATOM   4604  C  CG2 . ILE E  1 18  ? 33.305  254.578 59.981  1.00 29.37  ? 17  ILE E CG2 1 
ATOM   4605  C  CD1 . ILE E  1 18  ? 32.320  254.248 62.838  1.00 32.81  ? 17  ILE E CD1 1 
ATOM   4606  N  N   . ILE E  1 19  ? 36.158  253.284 58.210  1.00 33.34  ? 18  ILE E N   1 
ATOM   4607  C  CA  . ILE E  1 19  ? 36.801  253.789 57.017  1.00 35.01  ? 18  ILE E CA  1 
ATOM   4608  C  C   . ILE E  1 19  ? 35.763  254.090 55.948  1.00 36.41  ? 18  ILE E C   1 
ATOM   4609  O  O   . ILE E  1 19  ? 34.954  253.192 55.602  1.00 36.21  ? 18  ILE E O   1 
ATOM   4610  C  CB  . ILE E  1 19  ? 37.901  252.831 56.487  1.00 36.29  ? 18  ILE E CB  1 
ATOM   4611  C  CG1 . ILE E  1 19  ? 39.010  252.628 57.544  1.00 33.74  ? 18  ILE E CG1 1 
ATOM   4612  C  CG2 . ILE E  1 19  ? 38.546  253.388 55.226  1.00 30.34  ? 18  ILE E CG2 1 
ATOM   4613  C  CD1 . ILE E  1 19  ? 39.679  253.930 57.938  1.00 32.39  ? 18  ILE E CD1 1 
ATOM   4614  N  N   . ASN E  1 20  ? 35.795  255.322 55.432  1.00 32.79  ? 19  ASN E N   1 
ATOM   4615  C  CA  . ASN E  1 20  ? 34.945  255.717 54.329  1.00 31.93  ? 19  ASN E CA  1 
ATOM   4616  C  C   . ASN E  1 20  ? 35.541  255.691 52.957  1.00 33.67  ? 19  ASN E C   1 
ATOM   4617  O  O   . ASN E  1 20  ? 36.762  255.808 52.765  1.00 34.91  ? 19  ASN E O   1 
ATOM   4618  C  CB  . ASN E  1 20  ? 34.354  257.061 54.581  1.00 37.03  ? 19  ASN E CB  1 
ATOM   4619  C  CG  . ASN E  1 20  ? 33.591  257.118 55.911  1.00 39.61  ? 19  ASN E CG  1 
ATOM   4620  O  OD1 . ASN E  1 20  ? 34.172  257.510 56.902  1.00 42.09  ? 19  ASN E OD1 1 
ATOM   4621  N  ND2 . ASN E  1 20  ? 32.305  256.699 55.935  1.00 35.88  ? 19  ASN E ND2 1 
ATOM   4622  N  N   . PHE E  1 21  ? 34.677  255.497 51.969  1.00 36.09  ? 20  PHE E N   1 
ATOM   4623  C  CA  . PHE E  1 21  ? 35.118  255.487 50.562  1.00 35.46  ? 20  PHE E CA  1 
ATOM   4624  C  C   . PHE E  1 21  ? 34.164  256.279 49.749  1.00 36.41  ? 20  PHE E C   1 
ATOM   4625  O  O   . PHE E  1 21  ? 32.981  256.165 49.961  1.00 35.99  ? 20  PHE E O   1 
ATOM   4626  C  CB  . PHE E  1 21  ? 35.159  254.114 49.930  1.00 30.72  ? 20  PHE E CB  1 
ATOM   4627  C  CG  . PHE E  1 21  ? 36.033  253.185 50.606  1.00 30.40  ? 20  PHE E CG  1 
ATOM   4628  C  CD1 . PHE E  1 21  ? 35.622  252.562 51.808  1.00 29.67  ? 20  PHE E CD1 1 
ATOM   4629  C  CD2 . PHE E  1 21  ? 37.247  252.855 50.045  1.00 29.87  ? 20  PHE E CD2 1 
ATOM   4630  C  CE1 . PHE E  1 21  ? 36.453  251.637 52.448  1.00 29.91  ? 20  PHE E CE1 1 
ATOM   4631  C  CE2 . PHE E  1 21  ? 38.079  251.926 50.673  1.00 31.56  ? 20  PHE E CE2 1 
ATOM   4632  C  CZ  . PHE E  1 21  ? 37.684  251.308 51.877  1.00 31.39  ? 20  PHE E CZ  1 
ATOM   4633  N  N   . GLU E  1 22  ? 34.706  257.024 48.788  1.00 35.13  ? 21  GLU E N   1 
ATOM   4634  C  CA  . GLU E  1 22  ? 33.926  257.780 47.873  1.00 35.24  ? 21  GLU E CA  1 
ATOM   4635  C  C   . GLU E  1 22  ? 34.597  257.882 46.541  1.00 37.33  ? 21  GLU E C   1 
ATOM   4636  O  O   . GLU E  1 22  ? 35.821  258.014 46.449  1.00 35.22  ? 21  GLU E O   1 
ATOM   4637  C  CB  . GLU E  1 22  ? 33.706  259.124 48.406  1.00 37.95  ? 21  GLU E CB  1 
ATOM   4638  C  CG  . GLU E  1 22  ? 32.490  259.755 47.823  1.00 46.24  ? 21  GLU E CG  1 
ATOM   4639  C  CD  . GLU E  1 22  ? 32.542  261.271 47.990  1.00 56.85  ? 21  GLU E CD  1 
ATOM   4640  O  OE1 . GLU E  1 22  ? 33.495  261.946 47.452  1.00 61.11  ? 21  GLU E OE1 1 
ATOM   4641  O  OE2 . GLU E  1 22  ? 31.641  261.781 48.682  1.00 54.62  ? 21  GLU E OE2 1 
ATOM   4642  N  N   . GLN E  1 23  ? 33.770  257.788 45.501  1.00 35.80  ? 22  GLN E N   1 
ATOM   4643  C  CA  . GLN E  1 23  ? 34.261  257.702 44.164  1.00 34.18  ? 22  GLN E CA  1 
ATOM   4644  C  C   . GLN E  1 23  ? 33.153  258.251 43.293  1.00 36.53  ? 22  GLN E C   1 
ATOM   4645  O  O   . GLN E  1 23  ? 32.264  257.520 42.888  1.00 45.11  ? 22  GLN E O   1 
ATOM   4646  C  CB  . GLN E  1 23  ? 34.644  256.267 43.782  1.00 29.65  ? 22  GLN E CB  1 
ATOM   4647  C  CG  . GLN E  1 23  ? 35.366  256.218 42.460  1.00 30.60  ? 22  GLN E CG  1 
ATOM   4648  C  CD  . GLN E  1 23  ? 35.394  254.836 41.840  1.00 34.87  ? 22  GLN E CD  1 
ATOM   4649  O  OE1 . GLN E  1 23  ? 34.686  253.950 42.288  1.00 36.78  ? 22  GLN E OE1 1 
ATOM   4650  N  NE2 . GLN E  1 23  ? 36.206  254.642 40.809  1.00 31.64  ? 22  GLN E NE2 1 
ATOM   4651  N  N   . LYS E  1 24  ? 33.245  259.525 42.981  1.00 37.04  ? 23  LYS E N   1 
ATOM   4652  C  CA  . LYS E  1 24  ? 32.253  260.291 42.228  1.00 40.14  ? 23  LYS E CA  1 
ATOM   4653  C  C   . LYS E  1 24  ? 32.121  259.901 40.802  1.00 39.47  ? 23  LYS E C   1 
ATOM   4654  O  O   . LYS E  1 24  ? 31.062  260.089 40.269  1.00 44.88  ? 23  LYS E O   1 
ATOM   4655  C  CB  . LYS E  1 24  ? 32.671  261.742 42.188  1.00 45.87  ? 23  LYS E CB  1 
ATOM   4656  C  CG  . LYS E  1 24  ? 32.274  262.516 43.434  1.00 56.58  ? 23  LYS E CG  1 
ATOM   4657  C  CD  . LYS E  1 24  ? 33.367  263.575 43.721  1.00 61.24  ? 23  LYS E CD  1 
ATOM   4658  C  CE  . LYS E  1 24  ? 32.848  264.854 44.417  1.00 53.70  ? 23  LYS E CE  1 
ATOM   4659  N  NZ  . LYS E  1 24  ? 34.036  265.751 44.485  1.00 51.67  ? 23  LYS E NZ  1 
ATOM   4660  N  N   . GLU E  1 25  ? 33.190  259.412 40.190  1.00 37.50  ? 24  GLU E N   1 
ATOM   4661  C  CA  . GLU E  1 25  ? 33.217  259.001 38.803  1.00 42.82  ? 24  GLU E CA  1 
ATOM   4662  C  C   . GLU E  1 25  ? 33.688  257.595 38.782  1.00 43.52  ? 24  GLU E C   1 
ATOM   4663  O  O   . GLU E  1 25  ? 34.667  257.304 39.485  1.00 40.50  ? 24  GLU E O   1 
ATOM   4664  C  CB  . GLU E  1 25  ? 34.261  259.800 37.986  1.00 46.77  ? 24  GLU E CB  1 
ATOM   4665  C  CG  . GLU E  1 25  ? 33.941  261.280 37.814  1.00 48.49  ? 24  GLU E CG  1 
ATOM   4666  C  CD  . GLU E  1 25  ? 32.704  261.500 36.945  1.00 66.66  ? 24  GLU E CD  1 
ATOM   4667  O  OE1 . GLU E  1 25  ? 32.150  260.470 36.351  1.00 59.73  ? 24  GLU E OE1 1 
ATOM   4668  O  OE2 . GLU E  1 25  ? 32.278  262.718 36.867  1.00 68.75  ? 24  GLU E OE2 1 
ATOM   4669  N  N   . SER E  1 26  ? 33.047  256.747 37.949  1.00 37.53  ? 25  SER E N   1 
ATOM   4670  C  CA  . SER E  1 26  ? 33.387  255.327 37.900  1.00 34.04  ? 25  SER E CA  1 
ATOM   4671  C  C   . SER E  1 26  ? 34.808  255.135 37.427  1.00 33.69  ? 25  SER E C   1 
ATOM   4672  O  O   . SER E  1 26  ? 35.405  254.094 37.686  1.00 34.43  ? 25  SER E O   1 
ATOM   4673  C  CB  . SER E  1 26  ? 32.425  254.569 36.987  1.00 37.06  ? 25  SER E CB  1 
ATOM   4674  O  OG  . SER E  1 26  ? 32.566  254.822 35.577  1.00 37.38  ? 25  SER E OG  1 
ATOM   4675  N  N   . ASN E  1 27  ? 35.317  256.120 36.687  1.00 31.05  ? 26  ASN E N   1 
ATOM   4676  C  CA  . ASN E  1 27  ? 36.628  256.003 36.114  1.00 35.88  ? 26  ASN E CA  1 
ATOM   4677  C  C   . ASN E  1 27  ? 37.688  256.890 36.817  1.00 39.71  ? 26  ASN E C   1 
ATOM   4678  O  O   . ASN E  1 27  ? 38.887  256.936 36.445  1.00 38.63  ? 26  ASN E O   1 
ATOM   4679  C  CB  . ASN E  1 27  ? 36.625  256.115 34.585  1.00 33.94  ? 26  ASN E CB  1 
ATOM   4680  C  CG  . ASN E  1 27  ? 36.351  257.497 34.077  1.00 34.27  ? 26  ASN E CG  1 
ATOM   4681  O  OD1 . ASN E  1 27  ? 35.552  258.243 34.635  1.00 39.06  ? 26  ASN E OD1 1 
ATOM   4682  N  ND2 . ASN E  1 27  ? 36.967  257.824 32.957  1.00 32.79  ? 26  ASN E ND2 1 
ATOM   4683  N  N   . GLY E  1 28  ? 37.217  257.508 37.884  1.00 39.33  ? 27  GLY E N   1 
ATOM   4684  C  CA  . GLY E  1 28  ? 38.021  258.314 38.719  1.00 39.51  ? 27  GLY E CA  1 
ATOM   4685  C  C   . GLY E  1 28  ? 38.570  257.593 39.952  1.00 48.03  ? 27  GLY E C   1 
ATOM   4686  O  O   . GLY E  1 28  ? 38.461  256.360 40.172  1.00 40.40  ? 27  GLY E O   1 
ATOM   4687  N  N   . PRO E  1 29  ? 39.234  258.380 40.774  1.00 48.61  ? 28  PRO E N   1 
ATOM   4688  C  CA  . PRO E  1 29  ? 39.919  257.816 41.953  1.00 46.01  ? 28  PRO E CA  1 
ATOM   4689  C  C   . PRO E  1 29  ? 38.929  257.694 43.100  1.00 41.17  ? 28  PRO E C   1 
ATOM   4690  O  O   . PRO E  1 29  ? 37.872  258.330 43.061  1.00 37.73  ? 28  PRO E O   1 
ATOM   4691  C  CB  . PRO E  1 29  ? 40.969  258.879 42.261  1.00 43.76  ? 28  PRO E CB  1 
ATOM   4692  C  CG  . PRO E  1 29  ? 40.418  260.137 41.663  1.00 39.19  ? 28  PRO E CG  1 
ATOM   4693  C  CD  . PRO E  1 29  ? 39.538  259.797 40.531  1.00 37.91  ? 28  PRO E CD  1 
ATOM   4694  N  N   . VAL E  1 30  ? 39.296  256.897 44.093  1.00 38.11  ? 29  VAL E N   1 
ATOM   4695  C  CA  . VAL E  1 30  ? 38.515  256.627 45.341  1.00 35.22  ? 29  VAL E CA  1 
ATOM   4696  C  C   . VAL E  1 30  ? 39.173  257.393 46.508  1.00 34.13  ? 29  VAL E C   1 
ATOM   4697  O  O   . VAL E  1 30  ? 40.348  257.175 46.807  1.00 34.76  ? 29  VAL E O   1 
ATOM   4698  C  CB  . VAL E  1 30  ? 38.524  255.092 45.668  1.00 30.25  ? 29  VAL E CB  1 
ATOM   4699  C  CG1 . VAL E  1 30  ? 37.632  254.806 46.809  1.00 27.94  ? 29  VAL E CG1 1 
ATOM   4700  C  CG2 . VAL E  1 30  ? 38.183  254.247 44.417  1.00 29.75  ? 29  VAL E CG2 1 
ATOM   4701  N  N   . LYS E  1 31  ? 38.440  258.272 47.164  1.00 35.38  ? 30  LYS E N   1 
ATOM   4702  C  CA  . LYS E  1 31  ? 38.893  258.800 48.454  1.00 40.39  ? 30  LYS E CA  1 
ATOM   4703  C  C   . LYS E  1 31  ? 38.640  257.799 49.568  1.00 39.01  ? 30  LYS E C   1 
ATOM   4704  O  O   . LYS E  1 31  ? 37.573  257.215 49.650  1.00 35.55  ? 30  LYS E O   1 
ATOM   4705  C  CB  . LYS E  1 31  ? 38.194  260.096 48.805  1.00 40.45  ? 30  LYS E CB  1 
ATOM   4706  C  CG  . LYS E  1 31  ? 38.771  261.271 48.017  1.00 50.03  ? 30  LYS E CG  1 
ATOM   4707  C  CD  . LYS E  1 31  ? 37.881  262.555 48.113  1.00 56.04  ? 30  LYS E CD  1 
ATOM   4708  C  CE  . LYS E  1 31  ? 37.890  263.381 46.786  1.00 61.42  ? 30  LYS E CE  1 
ATOM   4709  N  NZ  . LYS E  1 31  ? 36.611  264.099 46.381  1.00 60.29  ? 30  LYS E NZ  1 
ATOM   4710  N  N   . VAL E  1 32  ? 39.655  257.597 50.404  1.00 38.20  ? 31  VAL E N   1 
ATOM   4711  C  CA  . VAL E  1 32  ? 39.566  256.718 51.564  1.00 35.40  ? 31  VAL E CA  1 
ATOM   4712  C  C   . VAL E  1 32  ? 39.886  257.514 52.843  1.00 40.12  ? 31  VAL E C   1 
ATOM   4713  O  O   . VAL E  1 32  ? 40.961  258.123 52.930  1.00 45.99  ? 31  VAL E O   1 
ATOM   4714  C  CB  . VAL E  1 32  ? 40.550  255.570 51.399  1.00 32.55  ? 31  VAL E CB  1 
ATOM   4715  C  CG1 . VAL E  1 32  ? 40.346  254.569 52.508  1.00 28.34  ? 31  VAL E CG1 1 
ATOM   4716  C  CG2 . VAL E  1 32  ? 40.440  254.960 50.016  1.00 26.53  ? 31  VAL E CG2 1 
ATOM   4717  N  N   . TRP E  1 33  ? 38.995  257.527 53.835  1.00 37.60  ? 32  TRP E N   1 
ATOM   4718  C  CA  . TRP E  1 33  ? 39.250  258.280 55.005  1.00 32.55  ? 32  TRP E CA  1 
ATOM   4719  C  C   . TRP E  1 33  ? 38.491  257.872 56.176  1.00 33.91  ? 32  TRP E C   1 
ATOM   4720  O  O   . TRP E  1 33  ? 37.406  257.359 56.080  1.00 37.08  ? 32  TRP E O   1 
ATOM   4721  C  CB  . TRP E  1 33  ? 38.936  259.755 54.740  1.00 36.88  ? 32  TRP E CB  1 
ATOM   4722  C  CG  . TRP E  1 33  ? 37.473  260.100 54.794  1.00 38.80  ? 32  TRP E CG  1 
ATOM   4723  C  CD1 . TRP E  1 33  ? 36.748  260.578 55.882  1.00 35.93  ? 32  TRP E CD1 1 
ATOM   4724  C  CD2 . TRP E  1 33  ? 36.559  260.008 53.720  1.00 38.48  ? 32  TRP E CD2 1 
ATOM   4725  N  NE1 . TRP E  1 33  ? 35.451  260.787 55.522  1.00 36.13  ? 32  TRP E NE1 1 
ATOM   4726  C  CE2 . TRP E  1 33  ? 35.303  260.460 54.197  1.00 39.24  ? 32  TRP E CE2 1 
ATOM   4727  C  CE3 . TRP E  1 33  ? 36.665  259.554 52.395  1.00 39.75  ? 32  TRP E CE3 1 
ATOM   4728  C  CZ2 . TRP E  1 33  ? 34.140  260.452 53.386  1.00 42.29  ? 32  TRP E CZ2 1 
ATOM   4729  C  CZ3 . TRP E  1 33  ? 35.522  259.557 51.577  1.00 41.49  ? 32  TRP E CZ3 1 
ATOM   4730  C  CH2 . TRP E  1 33  ? 34.270  260.012 52.072  1.00 40.07  ? 32  TRP E CH2 1 
ATOM   4731  N  N   . GLY E  1 34  ? 39.030  258.238 57.321  1.00 38.43  ? 33  GLY E N   1 
ATOM   4732  C  CA  . GLY E  1 34  ? 38.376  258.041 58.614  1.00 35.42  ? 33  GLY E CA  1 
ATOM   4733  C  C   . GLY E  1 34  ? 39.436  257.749 59.657  1.00 39.20  ? 33  GLY E C   1 
ATOM   4734  O  O   . GLY E  1 34  ? 40.493  258.346 59.669  1.00 39.35  ? 33  GLY E O   1 
ATOM   4735  N  N   . SER E  1 35  ? 39.231  256.736 60.479  1.00 39.93  ? 34  SER E N   1 
ATOM   4736  C  CA  . SER E  1 35  ? 39.959  256.704 61.689  1.00 37.83  ? 34  SER E CA  1 
ATOM   4737  C  C   . SER E  1 35  ? 40.047  255.336 62.290  1.00 38.45  ? 34  SER E C   1 
ATOM   4738  O  O   . SER E  1 35  ? 38.993  254.710 62.469  1.00 41.62  ? 34  SER E O   1 
ATOM   4739  C  CB  . SER E  1 35  ? 39.142  257.553 62.659  1.00 39.06  ? 34  SER E CB  1 
ATOM   4740  O  OG  . SER E  1 35  ? 40.022  257.916 63.661  1.00 48.01  ? 34  SER E OG  1 
ATOM   4741  N  N   . ILE E  1 36  ? 41.257  254.916 62.678  1.00 34.66  ? 35  ILE E N   1 
ATOM   4742  C  CA  . ILE E  1 36  ? 41.469  253.681 63.436  1.00 34.92  ? 35  ILE E CA  1 
ATOM   4743  C  C   . ILE E  1 36  ? 42.088  253.992 64.801  1.00 39.54  ? 35  ILE E C   1 
ATOM   4744  O  O   . ILE E  1 36  ? 42.933  254.904 64.943  1.00 39.71  ? 35  ILE E O   1 
ATOM   4745  C  CB  . ILE E  1 36  ? 42.321  252.707 62.622  1.00 35.26  ? 35  ILE E CB  1 
ATOM   4746  C  CG1 . ILE E  1 36  ? 41.783  252.638 61.169  1.00 35.25  ? 35  ILE E CG1 1 
ATOM   4747  C  CG2 . ILE E  1 36  ? 42.264  251.322 63.228  1.00 32.42  ? 35  ILE E CG2 1 
ATOM   4748  C  CD1 . ILE E  1 36  ? 42.679  251.871 60.234  1.00 36.95  ? 35  ILE E CD1 1 
ATOM   4749  N  N   . LYS E  1 37  ? 41.648  253.272 65.824  1.00 40.24  ? 36  LYS E N   1 
ATOM   4750  C  CA  . LYS E  1 37  ? 42.157  253.456 67.201  1.00 33.98  ? 36  LYS E CA  1 
ATOM   4751  C  C   . LYS E  1 37  ? 42.454  252.106 67.875  1.00 36.31  ? 36  LYS E C   1 
ATOM   4752  O  O   . LYS E  1 37  ? 42.057  251.026 67.395  1.00 33.18  ? 36  LYS E O   1 
ATOM   4753  C  CB  . LYS E  1 37  ? 41.196  254.327 68.010  1.00 33.51  ? 36  LYS E CB  1 
ATOM   4754  C  CG  . LYS E  1 37  ? 40.043  253.553 68.586  1.00 37.98  ? 36  LYS E CG  1 
ATOM   4755  C  CD  . LYS E  1 37  ? 38.980  254.493 69.076  1.00 38.92  ? 36  LYS E CD  1 
ATOM   4756  C  CE  . LYS E  1 37  ? 37.695  253.721 69.382  1.00 45.07  ? 36  LYS E CE  1 
ATOM   4757  N  NZ  . LYS E  1 37  ? 36.599  254.562 70.005  1.00 45.32  ? 36  LYS E NZ  1 
ATOM   4758  N  N   . GLY E  1 38  ? 43.233  252.154 68.954  1.00 40.24  ? 37  GLY E N   1 
ATOM   4759  C  CA  . GLY E  1 38  ? 43.621  250.922 69.680  1.00 36.71  ? 37  GLY E CA  1 
ATOM   4760  C  C   . GLY E  1 38  ? 44.930  250.352 69.146  1.00 36.28  ? 37  GLY E C   1 
ATOM   4761  O  O   . GLY E  1 38  ? 45.289  249.213 69.459  1.00 36.59  ? 37  GLY E O   1 
ATOM   4762  N  N   . LEU E  1 39  ? 45.658  251.159 68.386  1.00 34.50  ? 38  LEU E N   1 
ATOM   4763  C  CA  . LEU E  1 39  ? 46.842  250.701 67.655  1.00 39.95  ? 38  LEU E CA  1 
ATOM   4764  C  C   . LEU E  1 39  ? 48.123  251.118 68.403  1.00 44.44  ? 38  LEU E C   1 
ATOM   4765  O  O   . LEU E  1 39  ? 48.150  252.170 69.054  1.00 41.36  ? 38  LEU E O   1 
ATOM   4766  C  CB  . LEU E  1 39  ? 46.852  251.317 66.259  1.00 39.22  ? 38  LEU E CB  1 
ATOM   4767  C  CG  . LEU E  1 39  ? 45.943  250.734 65.172  1.00 39.05  ? 38  LEU E CG  1 
ATOM   4768  C  CD1 . LEU E  1 39  ? 45.946  251.692 63.999  1.00 35.94  ? 38  LEU E CD1 1 
ATOM   4769  C  CD2 . LEU E  1 39  ? 46.472  249.409 64.717  1.00 34.47  ? 38  LEU E CD2 1 
ATOM   4770  N  N   . THR E  1 40  ? 49.163  250.280 68.348  1.00 40.63  ? 39  THR E N   1 
ATOM   4771  C  CA  . THR E  1 40  ? 50.428  250.660 68.919  1.00 37.59  ? 39  THR E CA  1 
ATOM   4772  C  C   . THR E  1 40  ? 50.936  251.807 68.006  1.00 43.22  ? 39  THR E C   1 
ATOM   4773  O  O   . THR E  1 40  ? 50.719  251.766 66.783  1.00 42.01  ? 39  THR E O   1 
ATOM   4774  C  CB  . THR E  1 40  ? 51.459  249.536 68.823  1.00 40.26  ? 39  THR E CB  1 
ATOM   4775  O  OG1 . THR E  1 40  ? 51.646  249.154 67.456  1.00 38.82  ? 39  THR E OG1 1 
ATOM   4776  C  CG2 . THR E  1 40  ? 51.157  248.298 69.750  1.00 39.24  ? 39  THR E CG2 1 
ATOM   4777  N  N   . GLU E  1 41  ? 51.631  252.806 68.585  1.00 46.58  ? 40  GLU E N   1 
ATOM   4778  C  CA  . GLU E  1 41  ? 52.236  253.952 67.839  1.00 42.37  ? 40  GLU E CA  1 
ATOM   4779  C  C   . GLU E  1 41  ? 53.145  253.424 66.775  1.00 39.97  ? 40  GLU E C   1 
ATOM   4780  O  O   . GLU E  1 41  ? 53.751  252.390 66.976  1.00 43.68  ? 40  GLU E O   1 
ATOM   4781  C  CB  . GLU E  1 41  ? 53.013  254.838 68.803  1.00 46.73  ? 40  GLU E CB  1 
ATOM   4782  C  CG  . GLU E  1 41  ? 53.499  256.185 68.301  1.00 49.14  ? 40  GLU E CG  1 
ATOM   4783  C  CD  . GLU E  1 41  ? 54.360  256.955 69.316  1.00 56.94  ? 40  GLU E CD  1 
ATOM   4784  O  OE1 . GLU E  1 41  ? 54.676  256.437 70.438  1.00 54.28  ? 40  GLU E OE1 1 
ATOM   4785  O  OE2 . GLU E  1 41  ? 54.719  258.117 68.974  1.00 56.98  ? 40  GLU E OE2 1 
ATOM   4786  N  N   . GLY E  1 42  ? 53.168  254.082 65.624  1.00 40.82  ? 41  GLY E N   1 
ATOM   4787  C  CA  . GLY E  1 42  ? 53.943  253.626 64.444  1.00 40.81  ? 41  GLY E CA  1 
ATOM   4788  C  C   . GLY E  1 42  ? 53.097  253.307 63.189  1.00 43.15  ? 41  GLY E C   1 
ATOM   4789  O  O   . GLY E  1 42  ? 51.914  253.665 63.048  1.00 41.69  ? 41  GLY E O   1 
ATOM   4790  N  N   . LEU E  1 43  ? 53.709  252.575 62.294  1.00 42.28  ? 42  LEU E N   1 
ATOM   4791  C  CA  . LEU E  1 43  ? 53.129  252.274 61.024  1.00 42.25  ? 42  LEU E CA  1 
ATOM   4792  C  C   . LEU E  1 43  ? 52.417  250.900 61.060  1.00 42.87  ? 42  LEU E C   1 
ATOM   4793  O  O   . LEU E  1 43  ? 52.871  249.962 61.726  1.00 43.81  ? 42  LEU E O   1 
ATOM   4794  C  CB  . LEU E  1 43  ? 54.253  252.273 59.992  1.00 40.52  ? 42  LEU E CB  1 
ATOM   4795  C  CG  . LEU E  1 43  ? 55.004  253.545 59.613  1.00 38.09  ? 42  LEU E CG  1 
ATOM   4796  C  CD1 . LEU E  1 43  ? 56.070  253.105 58.617  1.00 39.06  ? 42  LEU E CD1 1 
ATOM   4797  C  CD2 . LEU E  1 43  ? 54.100  254.541 58.938  1.00 36.33  ? 42  LEU E CD2 1 
ATOM   4798  N  N   . HIS E  1 44  ? 51.294  250.808 60.346  1.00 39.12  ? 43  HIS E N   1 
ATOM   4799  C  CA  . HIS E  1 44  ? 50.540  249.552 60.202  1.00 40.26  ? 43  HIS E CA  1 
ATOM   4800  C  C   . HIS E  1 44  ? 50.112  249.386 58.760  1.00 37.61  ? 43  HIS E C   1 
ATOM   4801  O  O   . HIS E  1 44  ? 49.519  250.319 58.147  1.00 37.47  ? 43  HIS E O   1 
ATOM   4802  C  CB  . HIS E  1 44  ? 49.352  249.519 61.179  1.00 39.93  ? 43  HIS E CB  1 
ATOM   4803  C  CG  . HIS E  1 44  ? 49.763  249.626 62.612  1.00 44.37  ? 43  HIS E CG  1 
ATOM   4804  N  ND1 . HIS E  1 44  ? 50.288  248.559 63.330  1.00 48.18  ? 43  HIS E ND1 1 
ATOM   4805  C  CD2 . HIS E  1 44  ? 49.785  250.688 63.455  1.00 42.84  ? 43  HIS E CD2 1 
ATOM   4806  C  CE1 . HIS E  1 44  ? 50.572  248.950 64.564  1.00 39.64  ? 43  HIS E CE1 1 
ATOM   4807  N  NE2 . HIS E  1 44  ? 50.258  250.233 64.670  1.00 44.35  ? 43  HIS E NE2 1 
ATOM   4808  N  N   . GLY E  1 45  ? 50.451  248.232 58.189  1.00 36.42  ? 44  GLY E N   1 
ATOM   4809  C  CA  . GLY E  1 45  ? 50.016  247.948 56.796  1.00 41.01  ? 44  GLY E CA  1 
ATOM   4810  C  C   . GLY E  1 45  ? 48.476  247.892 56.734  1.00 42.34  ? 44  GLY E C   1 
ATOM   4811  O  O   . GLY E  1 45  ? 47.787  247.477 57.693  1.00 39.31  ? 44  GLY E O   1 
ATOM   4812  N  N   . PHE E  1 46  ? 47.953  248.356 55.622  1.00 38.55  ? 45  PHE E N   1 
ATOM   4813  C  CA  . PHE E  1 46  ? 46.542  248.600 55.442  1.00 37.67  ? 45  PHE E CA  1 
ATOM   4814  C  C   . PHE E  1 46  ? 46.262  248.017 54.039  1.00 38.36  ? 45  PHE E C   1 
ATOM   4815  O  O   . PHE E  1 46  ? 46.711  248.567 53.007  1.00 37.81  ? 45  PHE E O   1 
ATOM   4816  C  CB  . PHE E  1 46  ? 46.401  250.117 55.445  1.00 35.94  ? 45  PHE E CB  1 
ATOM   4817  C  CG  . PHE E  1 46  ? 45.025  250.634 55.566  1.00 35.19  ? 45  PHE E CG  1 
ATOM   4818  C  CD1 . PHE E  1 46  ? 44.206  250.209 56.565  1.00 36.14  ? 45  PHE E CD1 1 
ATOM   4819  C  CD2 . PHE E  1 46  ? 44.572  251.634 54.710  1.00 34.73  ? 45  PHE E CD2 1 
ATOM   4820  C  CE1 . PHE E  1 46  ? 42.947  250.766 56.737  1.00 35.08  ? 45  PHE E CE1 1 
ATOM   4821  C  CE2 . PHE E  1 46  ? 43.333  252.203 54.885  1.00 35.89  ? 45  PHE E CE2 1 
ATOM   4822  C  CZ  . PHE E  1 46  ? 42.505  251.753 55.896  1.00 34.75  ? 45  PHE E CZ  1 
ATOM   4823  N  N   . HIS E  1 47  ? 45.598  246.876 53.989  1.00 36.06  ? 46  HIS E N   1 
ATOM   4824  C  CA  . HIS E  1 47  ? 45.324  246.238 52.699  1.00 35.76  ? 46  HIS E CA  1 
ATOM   4825  C  C   . HIS E  1 47  ? 43.897  245.757 52.555  1.00 38.08  ? 46  HIS E C   1 
ATOM   4826  O  O   . HIS E  1 47  ? 43.255  245.343 53.552  1.00 35.75  ? 46  HIS E O   1 
ATOM   4827  C  CB  . HIS E  1 47  ? 46.251  245.048 52.411  1.00 36.03  ? 46  HIS E CB  1 
ATOM   4828  C  CG  . HIS E  1 47  ? 47.683  245.295 52.760  1.00 45.46  ? 46  HIS E CG  1 
ATOM   4829  N  ND1 . HIS E  1 47  ? 48.203  244.988 54.005  1.00 47.22  ? 46  HIS E ND1 1 
ATOM   4830  C  CD2 . HIS E  1 47  ? 48.681  245.894 52.070  1.00 45.87  ? 46  HIS E CD2 1 
ATOM   4831  C  CE1 . HIS E  1 47  ? 49.469  245.356 54.054  1.00 49.95  ? 46  HIS E CE1 1 
ATOM   4832  N  NE2 . HIS E  1 47  ? 49.776  245.925 52.900  1.00 51.77  ? 46  HIS E NE2 1 
ATOM   4833  N  N   . VAL E  1 48  ? 43.434  245.795 51.297  1.00 34.52  ? 47  VAL E N   1 
ATOM   4834  C  CA  . VAL E  1 48  ? 42.292  245.046 50.896  1.00 32.73  ? 47  VAL E CA  1 
ATOM   4835  C  C   . VAL E  1 48  ? 42.611  243.559 50.639  1.00 33.48  ? 47  VAL E C   1 
ATOM   4836  O  O   . VAL E  1 48  ? 43.427  243.226 49.769  1.00 34.78  ? 47  VAL E O   1 
ATOM   4837  C  CB  . VAL E  1 48  ? 41.593  245.691 49.697  1.00 33.36  ? 47  VAL E CB  1 
ATOM   4838  C  CG1 . VAL E  1 48  ? 40.322  244.904 49.392  1.00 30.23  ? 47  VAL E CG1 1 
ATOM   4839  C  CG2 . VAL E  1 48  ? 41.281  247.177 49.963  1.00 30.24  ? 47  VAL E CG2 1 
ATOM   4840  N  N   . HIS E  1 49  ? 41.952  242.655 51.360  1.00 32.98  ? 48  HIS E N   1 
ATOM   4841  C  CA  . HIS E  1 49  ? 42.174  241.196 51.102  1.00 33.70  ? 48  HIS E CA  1 
ATOM   4842  C  C   . HIS E  1 49  ? 41.087  240.643 50.232  1.00 32.06  ? 48  HIS E C   1 
ATOM   4843  O  O   . HIS E  1 49  ? 40.056  241.282 50.137  1.00 30.92  ? 48  HIS E O   1 
ATOM   4844  C  CB  . HIS E  1 49  ? 42.370  240.386 52.373  1.00 29.61  ? 48  HIS E CB  1 
ATOM   4845  C  CG  . HIS E  1 49  ? 43.586  240.799 53.135  1.00 32.43  ? 48  HIS E CG  1 
ATOM   4846  N  ND1 . HIS E  1 49  ? 44.555  239.902 53.534  1.00 30.84  ? 48  HIS E ND1 1 
ATOM   4847  C  CD2 . HIS E  1 49  ? 43.999  242.031 53.565  1.00 35.13  ? 48  HIS E CD2 1 
ATOM   4848  C  CE1 . HIS E  1 49  ? 45.504  240.557 54.179  1.00 33.61  ? 48  HIS E CE1 1 
ATOM   4849  N  NE2 . HIS E  1 49  ? 45.196  241.852 54.211  1.00 33.09  ? 48  HIS E NE2 1 
ATOM   4850  N  N   . GLU E  1 50  ? 41.359  239.502 49.573  1.00 33.27  ? 49  GLU E N   1 
ATOM   4851  C  CA  . GLU E  1 50  ? 40.482  238.946 48.592  1.00 33.20  ? 49  GLU E CA  1 
ATOM   4852  C  C   . GLU E  1 50  ? 39.021  238.685 49.026  1.00 33.45  ? 49  GLU E C   1 
ATOM   4853  O  O   . GLU E  1 50  ? 38.137  239.135 48.347  1.00 33.34  ? 49  GLU E O   1 
ATOM   4854  C  CB  . GLU E  1 50  ? 41.060  237.729 47.968  1.00 34.94  ? 49  GLU E CB  1 
ATOM   4855  C  CG  . GLU E  1 50  ? 40.511  237.587 46.556  1.00 39.84  ? 49  GLU E CG  1 
ATOM   4856  C  CD  . GLU E  1 50  ? 40.961  236.332 45.854  1.00 43.19  ? 49  GLU E CD  1 
ATOM   4857  O  OE1 . GLU E  1 50  ? 42.001  235.794 46.255  1.00 41.36  ? 49  GLU E OE1 1 
ATOM   4858  O  OE2 . GLU E  1 50  ? 40.279  235.879 44.889  1.00 42.35  ? 49  GLU E OE2 1 
ATOM   4859  N  N   . PHE E  1 51  ? 38.774  238.031 50.154  1.00 30.45  ? 50  PHE E N   1 
ATOM   4860  C  CA  . PHE E  1 51  ? 37.465  237.626 50.476  1.00 29.25  ? 50  PHE E CA  1 
ATOM   4861  C  C   . PHE E  1 51  ? 36.836  238.458 51.539  1.00 33.35  ? 50  PHE E C   1 
ATOM   4862  O  O   . PHE E  1 51  ? 37.454  238.800 52.585  1.00 36.06  ? 50  PHE E O   1 
ATOM   4863  C  CB  . PHE E  1 51  ? 37.477  236.152 50.875  1.00 29.47  ? 50  PHE E CB  1 
ATOM   4864  C  CG  . PHE E  1 51  ? 38.094  235.278 49.827  1.00 32.91  ? 50  PHE E CG  1 
ATOM   4865  C  CD1 . PHE E  1 51  ? 37.457  235.092 48.599  1.00 33.70  ? 50  PHE E CD1 1 
ATOM   4866  C  CD2 . PHE E  1 51  ? 39.381  234.711 50.029  1.00 34.34  ? 50  PHE E CD2 1 
ATOM   4867  C  CE1 . PHE E  1 51  ? 38.090  234.339 47.595  1.00 39.78  ? 50  PHE E CE1 1 
ATOM   4868  C  CE2 . PHE E  1 51  ? 40.023  233.947 49.052  1.00 31.88  ? 50  PHE E CE2 1 
ATOM   4869  C  CZ  . PHE E  1 51  ? 39.363  233.760 47.834  1.00 39.02  ? 50  PHE E CZ  1 
ATOM   4870  N  N   . GLY E  1 52  ? 35.558  238.738 51.362  1.00 31.98  ? 51  GLY E N   1 
ATOM   4871  C  CA  . GLY E  1 52  ? 34.861  239.246 52.508  1.00 29.45  ? 51  GLY E CA  1 
ATOM   4872  C  C   . GLY E  1 52  ? 34.289  238.195 53.391  1.00 29.26  ? 51  GLY E C   1 
ATOM   4873  O  O   . GLY E  1 52  ? 33.080  238.221 53.651  1.00 38.33  ? 51  GLY E O   1 
ATOM   4874  N  N   . ASP E  1 53  ? 35.107  237.268 53.840  1.00 30.28  ? 52  ASP E N   1 
ATOM   4875  C  CA  . ASP E  1 53  ? 34.687  236.122 54.638  1.00 29.54  ? 52  ASP E CA  1 
ATOM   4876  C  C   . ASP E  1 53  ? 35.231  236.333 56.027  1.00 32.02  ? 52  ASP E C   1 
ATOM   4877  O  O   . ASP E  1 53  ? 36.436  236.153 56.255  1.00 32.17  ? 52  ASP E O   1 
ATOM   4878  C  CB  . ASP E  1 53  ? 35.268  234.885 54.000  1.00 31.79  ? 52  ASP E CB  1 
ATOM   4879  C  CG  . ASP E  1 53  ? 34.848  233.603 54.679  1.00 35.05  ? 52  ASP E CG  1 
ATOM   4880  O  OD1 . ASP E  1 53  ? 34.531  233.645 55.902  1.00 38.75  ? 52  ASP E OD1 1 
ATOM   4881  O  OD2 . ASP E  1 53  ? 34.837  232.551 53.970  1.00 33.19  ? 52  ASP E OD2 1 
ATOM   4882  N  N   A ASN E  1 54  ? 34.346  236.734 56.954  0.50 31.09  ? 53  ASN E N   1 
ATOM   4883  N  N   B ASN E  1 54  ? 34.401  236.772 56.955  0.50 31.60  ? 53  ASN E N   1 
ATOM   4884  C  CA  A ASN E  1 54  ? 34.690  237.006 58.374  0.50 30.46  ? 53  ASN E CA  1 
ATOM   4885  C  CA  B ASN E  1 54  ? 34.944  236.947 58.285  0.50 31.30  ? 53  ASN E CA  1 
ATOM   4886  C  C   A ASN E  1 54  ? 34.427  235.779 59.282  0.50 30.10  ? 53  ASN E C   1 
ATOM   4887  C  C   B ASN E  1 54  ? 34.466  235.804 59.243  0.50 30.64  ? 53  ASN E C   1 
ATOM   4888  O  O   A ASN E  1 54  ? 34.354  235.918 60.487  0.50 29.61  ? 53  ASN E O   1 
ATOM   4889  O  O   B ASN E  1 54  ? 34.289  236.022 60.428  0.50 30.12  ? 53  ASN E O   1 
ATOM   4890  C  CB  A ASN E  1 54  ? 33.914  238.246 58.902  0.50 31.44  ? 53  ASN E CB  1 
ATOM   4891  C  CB  B ASN E  1 54  ? 34.735  238.391 58.816  0.50 32.58  ? 53  ASN E CB  1 
ATOM   4892  C  CG  A ASN E  1 54  ? 34.531  238.865 60.185  0.50 30.84  ? 53  ASN E CG  1 
ATOM   4893  C  CG  B ASN E  1 54  ? 35.409  239.513 57.951  0.50 33.84  ? 53  ASN E CG  1 
ATOM   4894  O  OD1 A ASN E  1 54  ? 35.727  238.825 60.394  0.50 29.57  ? 53  ASN E OD1 1 
ATOM   4895  O  OD1 B ASN E  1 54  ? 36.268  239.313 57.043  0.50 29.47  ? 53  ASN E OD1 1 
ATOM   4896  N  ND2 A ASN E  1 54  ? 33.693  239.435 61.028  0.50 29.38  ? 53  ASN E ND2 1 
ATOM   4897  N  ND2 B ASN E  1 54  ? 35.009  240.744 58.278  0.50 34.99  ? 53  ASN E ND2 1 
ATOM   4898  N  N   . THR E  1 55  ? 34.293  234.588 58.707  1.00 30.34  ? 54  THR E N   1 
ATOM   4899  C  CA  . THR E  1 55  ? 33.810  233.439 59.478  1.00 33.64  ? 54  THR E CA  1 
ATOM   4900  C  C   . THR E  1 55  ? 34.879  232.946 60.440  1.00 37.23  ? 54  THR E C   1 
ATOM   4901  O  O   . THR E  1 55  ? 34.606  232.248 61.429  1.00 37.58  ? 54  THR E O   1 
ATOM   4902  C  CB  . THR E  1 55  ? 33.339  232.212 58.608  1.00 34.71  ? 54  THR E CB  1 
ATOM   4903  O  OG1 . THR E  1 55  ? 34.407  231.706 57.794  1.00 32.99  ? 54  THR E OG1 1 
ATOM   4904  C  CG2 . THR E  1 55  ? 32.076  232.486 57.729  1.00 28.15  ? 54  THR E CG2 1 
ATOM   4905  N  N   . ALA E  1 56  ? 36.120  233.272 60.128  1.00 36.46  ? 55  ALA E N   1 
ATOM   4906  C  CA  . ALA E  1 56  ? 37.216  232.946 61.015  1.00 36.92  ? 55  ALA E CA  1 
ATOM   4907  C  C   . ALA E  1 56  ? 37.927  234.239 61.371  1.00 38.95  ? 55  ALA E C   1 
ATOM   4908  O  O   . ALA E  1 56  ? 39.153  234.297 61.343  1.00 43.03  ? 55  ALA E O   1 
ATOM   4909  C  CB  . ALA E  1 56  ? 38.166  231.970 60.344  1.00 36.74  ? 55  ALA E CB  1 
ATOM   4910  N  N   . GLY E  1 57  ? 37.149  235.287 61.657  1.00 38.24  ? 56  GLY E N   1 
ATOM   4911  C  CA  . GLY E  1 57  ? 37.710  236.596 61.911  1.00 36.60  ? 56  GLY E CA  1 
ATOM   4912  C  C   . GLY E  1 57  ? 38.450  237.097 60.696  1.00 40.10  ? 56  GLY E C   1 
ATOM   4913  O  O   . GLY E  1 57  ? 37.950  236.983 59.597  1.00 43.69  ? 56  GLY E O   1 
ATOM   4914  N  N   . CYS E  1 58  ? 39.639  237.655 60.871  1.00 39.41  ? 57  CYS E N   1 
ATOM   4915  C  CA  . CYS E  1 58  ? 40.382  238.215 59.737  1.00 35.08  ? 57  CYS E CA  1 
ATOM   4916  C  C   . CYS E  1 58  ? 41.124  237.147 58.978  1.00 39.01  ? 57  CYS E C   1 
ATOM   4917  O  O   . CYS E  1 58  ? 41.564  237.345 57.841  1.00 38.45  ? 57  CYS E O   1 
ATOM   4918  C  CB  . CYS E  1 58  ? 41.368  239.242 60.212  1.00 35.35  ? 57  CYS E CB  1 
ATOM   4919  S  SG  . CYS E  1 58  ? 40.553  240.594 61.085  1.00 42.11  ? 57  CYS E SG  1 
ATOM   4920  N  N   . THR E  1 59  ? 41.283  235.998 59.605  1.00 36.21  ? 58  THR E N   1 
ATOM   4921  C  CA  . THR E  1 59  ? 42.071  234.983 58.981  1.00 41.32  ? 58  THR E CA  1 
ATOM   4922  C  C   . THR E  1 59  ? 41.490  234.519 57.663  1.00 42.03  ? 58  THR E C   1 
ATOM   4923  O  O   . THR E  1 59  ? 42.205  234.266 56.703  1.00 46.45  ? 58  THR E O   1 
ATOM   4924  C  CB  . THR E  1 59  ? 42.126  233.824 59.921  1.00 44.99  ? 58  THR E CB  1 
ATOM   4925  O  OG1 . THR E  1 59  ? 42.559  234.372 61.159  1.00 45.19  ? 58  THR E OG1 1 
ATOM   4926  C  CG2 . THR E  1 59  ? 43.050  232.748 59.367  1.00 39.55  ? 58  THR E CG2 1 
ATOM   4927  N  N   . SER E  1 60  ? 40.176  234.460 57.624  1.00 39.25  ? 59  SER E N   1 
ATOM   4928  C  CA  . SER E  1 60  ? 39.504  233.938 56.493  1.00 36.55  ? 59  SER E CA  1 
ATOM   4929  C  C   . SER E  1 60  ? 39.402  234.922 55.311  1.00 33.63  ? 59  SER E C   1 
ATOM   4930  O  O   . SER E  1 60  ? 38.893  234.574 54.264  1.00 33.27  ? 59  SER E O   1 
ATOM   4931  C  CB  . SER E  1 60  ? 38.166  233.352 56.925  1.00 32.90  ? 59  SER E CB  1 
ATOM   4932  O  OG  . SER E  1 60  ? 37.414  234.295 57.692  1.00 34.59  ? 59  SER E OG  1 
ATOM   4933  N  N   . ALA E  1 61  ? 39.896  236.132 55.459  1.00 33.55  ? 60  ALA E N   1 
ATOM   4934  C  CA  . ALA E  1 61  ? 39.847  237.084 54.352  1.00 29.23  ? 60  ALA E CA  1 
ATOM   4935  C  C   . ALA E  1 61  ? 40.823  236.659 53.225  1.00 32.31  ? 60  ALA E C   1 
ATOM   4936  O  O   . ALA E  1 61  ? 40.789  237.211 52.134  1.00 31.82  ? 60  ALA E O   1 
ATOM   4937  C  CB  . ALA E  1 61  ? 40.185  238.454 54.889  1.00 27.77  ? 60  ALA E CB  1 
ATOM   4938  N  N   . GLY E  1 62  ? 41.705  235.685 53.488  1.00 33.76  ? 61  GLY E N   1 
ATOM   4939  C  CA  . GLY E  1 62  ? 42.697  235.283 52.497  1.00 39.29  ? 61  GLY E CA  1 
ATOM   4940  C  C   . GLY E  1 62  ? 43.786  236.304 52.120  1.00 40.64  ? 61  GLY E C   1 
ATOM   4941  O  O   . GLY E  1 62  ? 44.171  237.155 52.903  1.00 40.68  ? 61  GLY E O   1 
ATOM   4942  N  N   . PRO E  1 63  ? 44.321  236.181 50.923  1.00 38.16  ? 62  PRO E N   1 
ATOM   4943  C  CA  . PRO E  1 63  ? 45.523  236.947 50.591  1.00 37.95  ? 62  PRO E CA  1 
ATOM   4944  C  C   . PRO E  1 63  ? 45.156  238.336 50.218  1.00 34.83  ? 62  PRO E C   1 
ATOM   4945  O  O   . PRO E  1 63  ? 44.015  238.618 50.128  1.00 38.76  ? 62  PRO E O   1 
ATOM   4946  C  CB  . PRO E  1 63  ? 46.128  236.192 49.380  1.00 34.65  ? 62  PRO E CB  1 
ATOM   4947  C  CG  . PRO E  1 63  ? 45.082  235.226 48.969  1.00 36.00  ? 62  PRO E CG  1 
ATOM   4948  C  CD  . PRO E  1 63  ? 44.121  235.004 50.080  1.00 35.29  ? 62  PRO E CD  1 
ATOM   4949  N  N   . HIS E  1 64  ? 46.126  239.200 49.974  1.00 38.71  ? 63  HIS E N   1 
ATOM   4950  C  CA  . HIS E  1 64  ? 45.858  240.516 49.426  1.00 37.80  ? 63  HIS E CA  1 
ATOM   4951  C  C   . HIS E  1 64  ? 45.064  240.412 48.166  1.00 33.73  ? 63  HIS E C   1 
ATOM   4952  O  O   . HIS E  1 64  ? 45.362  239.587 47.331  1.00 35.89  ? 63  HIS E O   1 
ATOM   4953  C  CB  . HIS E  1 64  ? 47.171  241.284 49.200  1.00 36.68  ? 63  HIS E CB  1 
ATOM   4954  C  CG  . HIS E  1 64  ? 47.825  241.648 50.482  1.00 42.46  ? 63  HIS E CG  1 
ATOM   4955  N  ND1 . HIS E  1 64  ? 49.105  242.122 50.576  1.00 43.16  ? 63  HIS E ND1 1 
ATOM   4956  C  CD2 . HIS E  1 64  ? 47.389  241.524 51.758  1.00 49.36  ? 63  HIS E CD2 1 
ATOM   4957  C  CE1 . HIS E  1 64  ? 49.422  242.337 51.841  1.00 50.52  ? 63  HIS E CE1 1 
ATOM   4958  N  NE2 . HIS E  1 64  ? 48.414  241.934 52.586  1.00 54.27  ? 63  HIS E NE2 1 
ATOM   4959  N  N   . PHE E  1 65  ? 44.059  241.252 48.034  1.00 31.76  ? 64  PHE E N   1 
ATOM   4960  C  CA  . PHE E  1 65  ? 43.346  241.303 46.774  1.00 34.30  ? 64  PHE E CA  1 
ATOM   4961  C  C   . PHE E  1 65  ? 44.248  241.621 45.580  1.00 37.59  ? 64  PHE E C   1 
ATOM   4962  O  O   . PHE E  1 65  ? 44.877  242.719 45.468  1.00 34.76  ? 64  PHE E O   1 
ATOM   4963  C  CB  . PHE E  1 65  ? 42.212  242.305 46.820  1.00 31.62  ? 64  PHE E CB  1 
ATOM   4964  C  CG  . PHE E  1 65  ? 41.385  242.378 45.543  1.00 31.97  ? 64  PHE E CG  1 
ATOM   4965  C  CD1 . PHE E  1 65  ? 40.898  241.205 44.903  1.00 30.89  ? 64  PHE E CD1 1 
ATOM   4966  C  CD2 . PHE E  1 65  ? 40.999  243.633 45.033  1.00 32.52  ? 64  PHE E CD2 1 
ATOM   4967  C  CE1 . PHE E  1 65  ? 40.134  241.305 43.788  1.00 29.07  ? 64  PHE E CE1 1 
ATOM   4968  C  CE2 . PHE E  1 65  ? 40.180  243.738 43.919  1.00 31.85  ? 64  PHE E CE2 1 
ATOM   4969  C  CZ  . PHE E  1 65  ? 39.760  242.550 43.288  1.00 32.39  ? 64  PHE E CZ  1 
ATOM   4970  N  N   . ASN E  1 66  ? 44.234  240.686 44.643  1.00 39.80  ? 65  ASN E N   1 
ATOM   4971  C  CA  . ASN E  1 66  ? 45.188  240.748 43.569  1.00 44.96  ? 65  ASN E CA  1 
ATOM   4972  C  C   . ASN E  1 66  ? 44.748  240.152 42.245  1.00 51.44  ? 65  ASN E C   1 
ATOM   4973  O  O   . ASN E  1 66  ? 45.307  239.087 41.870  1.00 52.63  ? 65  ASN E O   1 
ATOM   4974  C  CB  . ASN E  1 66  ? 46.408  239.934 43.975  1.00 47.13  ? 65  ASN E CB  1 
ATOM   4975  C  CG  . ASN E  1 66  ? 47.532  240.155 43.031  1.00 46.86  ? 65  ASN E CG  1 
ATOM   4976  O  OD1 . ASN E  1 66  ? 47.545  241.221 42.342  1.00 47.11  ? 65  ASN E OD1 1 
ATOM   4977  N  ND2 . ASN E  1 66  ? 48.493  239.202 42.995  1.00 40.52  ? 65  ASN E ND2 1 
ATOM   4978  N  N   . PRO E  1 67  ? 43.828  240.824 41.506  1.00 43.91  ? 66  PRO E N   1 
ATOM   4979  C  CA  . PRO E  1 67  ? 43.295  240.190 40.298  1.00 42.75  ? 66  PRO E CA  1 
ATOM   4980  C  C   . PRO E  1 67  ? 44.246  240.075 39.087  1.00 54.84  ? 66  PRO E C   1 
ATOM   4981  O  O   . PRO E  1 67  ? 44.024  239.201 38.200  1.00 53.41  ? 66  PRO E O   1 
ATOM   4982  C  CB  . PRO E  1 67  ? 42.073  241.009 39.969  1.00 40.74  ? 66  PRO E CB  1 
ATOM   4983  C  CG  . PRO E  1 67  ? 42.282  242.299 40.651  1.00 40.18  ? 66  PRO E CG  1 
ATOM   4984  C  CD  . PRO E  1 67  ? 43.140  242.071 41.842  1.00 39.18  ? 66  PRO E CD  1 
ATOM   4985  N  N   . LEU E  1 68  ? 45.290  240.904 38.999  1.00 58.82  ? 67  LEU E N   1 
ATOM   4986  C  CA  . LEU E  1 68  ? 46.135  240.769 37.758  1.00 66.83  ? 67  LEU E CA  1 
ATOM   4987  C  C   . LEU E  1 68  ? 47.473  240.044 38.034  1.00 66.76  ? 67  LEU E C   1 
ATOM   4988  O  O   . LEU E  1 68  ? 48.474  240.254 37.330  1.00 60.32  ? 67  LEU E O   1 
ATOM   4989  C  CB  . LEU E  1 68  ? 46.319  242.089 36.963  1.00 61.41  ? 67  LEU E CB  1 
ATOM   4990  C  CG  . LEU E  1 68  ? 45.342  243.218 37.263  1.00 63.68  ? 67  LEU E CG  1 
ATOM   4991  C  CD1 . LEU E  1 68  ? 46.151  244.540 37.301  1.00 53.12  ? 67  LEU E CD1 1 
ATOM   4992  C  CD2 . LEU E  1 68  ? 44.062  243.194 36.371  1.00 53.34  ? 67  LEU E CD2 1 
ATOM   4993  N  N   . SER E  1 69  ? 47.463  239.199 39.079  1.00 70.94  ? 68  SER E N   1 
ATOM   4994  C  CA  . SER E  1 69  ? 48.676  238.437 39.560  1.00 73.24  ? 68  SER E CA  1 
ATOM   4995  C  C   . SER E  1 69  ? 50.045  239.223 39.533  1.00 73.35  ? 68  SER E C   1 
ATOM   4996  O  O   . SER E  1 69  ? 51.004  238.818 38.859  1.00 73.59  ? 68  SER E O   1 
ATOM   4997  C  CB  . SER E  1 69  ? 48.772  237.059 38.854  1.00 69.83  ? 68  SER E CB  1 
ATOM   4998  O  OG  . SER E  1 69  ? 47.574  236.305 39.044  1.00 64.23  ? 68  SER E OG  1 
ATOM   4999  N  N   . ARG E  1 70  ? 50.102  240.364 40.243  1.00 69.85  ? 69  ARG E N   1 
ATOM   5000  C  CA  . ARG E  1 70  ? 51.332  241.172 40.427  1.00 62.98  ? 69  ARG E CA  1 
ATOM   5001  C  C   . ARG E  1 70  ? 52.095  240.760 41.714  1.00 63.05  ? 69  ARG E C   1 
ATOM   5002  O  O   . ARG E  1 70  ? 51.701  239.808 42.434  1.00 58.67  ? 69  ARG E O   1 
ATOM   5003  C  CB  . ARG E  1 70  ? 50.971  242.696 40.485  1.00 69.31  ? 69  ARG E CB  1 
ATOM   5004  C  CG  . ARG E  1 70  ? 50.107  243.203 39.325  1.00 67.09  ? 69  ARG E CG  1 
ATOM   5005  C  CD  . ARG E  1 70  ? 50.781  242.928 37.987  1.00 69.28  ? 69  ARG E CD  1 
ATOM   5006  N  NE  . ARG E  1 70  ? 51.611  244.074 37.599  1.00 75.06  ? 69  ARG E NE  1 
ATOM   5007  C  CZ  . ARG E  1 70  ? 51.394  244.841 36.522  1.00 81.26  ? 69  ARG E CZ  1 
ATOM   5008  N  NH1 . ARG E  1 70  ? 50.367  244.546 35.676  1.00 61.68  ? 69  ARG E NH1 1 
ATOM   5009  N  NH2 . ARG E  1 70  ? 52.233  245.883 36.272  1.00 68.99  ? 69  ARG E NH2 1 
ATOM   5010  N  N   . LYS E  1 71  ? 53.192  241.474 42.011  1.00 64.06  ? 70  LYS E N   1 
ATOM   5011  C  CA  . LYS E  1 71  ? 53.906  241.281 43.279  1.00 58.66  ? 70  LYS E CA  1 
ATOM   5012  C  C   . LYS E  1 71  ? 53.487  242.392 44.297  1.00 68.17  ? 70  LYS E C   1 
ATOM   5013  O  O   . LYS E  1 71  ? 52.806  243.433 43.930  1.00 63.21  ? 70  LYS E O   1 
ATOM   5014  C  CB  . LYS E  1 71  ? 55.408  241.137 43.000  1.00 69.60  ? 70  LYS E CB  1 
ATOM   5015  C  CG  . LYS E  1 71  ? 55.813  239.803 42.316  1.00 66.19  ? 70  LYS E CG  1 
ATOM   5016  C  CD  . LYS E  1 71  ? 57.350  239.669 42.283  1.00 70.08  ? 70  LYS E CD  1 
ATOM   5017  C  CE  . LYS E  1 71  ? 57.788  238.542 41.320  1.00 79.69  ? 70  LYS E CE  1 
ATOM   5018  N  NZ  . LYS E  1 71  ? 59.269  238.412 41.009  1.00 65.33  ? 70  LYS E NZ  1 
ATOM   5019  N  N   . HIS E  1 72  ? 53.757  242.138 45.584  1.00 64.77  ? 71  HIS E N   1 
ATOM   5020  C  CA  . HIS E  1 72  ? 53.395  243.125 46.617  1.00 62.30  ? 71  HIS E CA  1 
ATOM   5021  C  C   . HIS E  1 72  ? 54.226  244.388 46.313  1.00 63.78  ? 71  HIS E C   1 
ATOM   5022  O  O   . HIS E  1 72  ? 55.398  244.274 45.917  1.00 68.16  ? 71  HIS E O   1 
ATOM   5023  C  CB  . HIS E  1 72  ? 53.614  242.605 48.079  1.00 61.79  ? 71  HIS E CB  1 
ATOM   5024  C  CG  . HIS E  1 72  ? 53.325  243.649 49.131  1.00 67.75  ? 71  HIS E CG  1 
ATOM   5025  N  ND1 . HIS E  1 72  ? 52.052  244.109 49.391  1.00 60.49  ? 71  HIS E ND1 1 
ATOM   5026  C  CD2 . HIS E  1 72  ? 54.146  244.374 49.937  1.00 73.95  ? 71  HIS E CD2 1 
ATOM   5027  C  CE1 . HIS E  1 72  ? 52.088  245.060 50.310  1.00 64.97  ? 71  HIS E CE1 1 
ATOM   5028  N  NE2 . HIS E  1 72  ? 53.348  245.232 50.669  1.00 68.58  ? 71  HIS E NE2 1 
ATOM   5029  N  N   . GLY E  1 73  ? 53.596  245.556 46.440  1.00 56.31  ? 72  GLY E N   1 
ATOM   5030  C  CA  . GLY E  1 73  ? 54.274  246.847 46.318  1.00 54.54  ? 72  GLY E CA  1 
ATOM   5031  C  C   . GLY E  1 73  ? 53.494  247.844 47.189  1.00 68.34  ? 72  GLY E C   1 
ATOM   5032  O  O   . GLY E  1 73  ? 52.472  247.489 47.909  1.00 63.90  ? 72  GLY E O   1 
ATOM   5033  N  N   . GLY E  1 74  ? 53.974  249.085 47.167  1.00 58.62  ? 73  GLY E N   1 
ATOM   5034  C  CA  . GLY E  1 74  ? 53.285  250.188 47.826  1.00 59.14  ? 73  GLY E CA  1 
ATOM   5035  C  C   . GLY E  1 74  ? 52.241  250.735 46.856  1.00 66.54  ? 73  GLY E C   1 
ATOM   5036  O  O   . GLY E  1 74  ? 52.151  250.225 45.678  1.00 61.63  ? 73  GLY E O   1 
ATOM   5037  N  N   . PRO E  1 75  ? 51.440  251.756 47.314  1.00 65.39  ? 74  PRO E N   1 
ATOM   5038  C  CA  . PRO E  1 75  ? 50.367  252.364 46.475  1.00 66.08  ? 74  PRO E CA  1 
ATOM   5039  C  C   . PRO E  1 75  ? 50.875  253.081 45.211  1.00 68.16  ? 74  PRO E C   1 
ATOM   5040  O  O   . PRO E  1 75  ? 50.161  253.112 44.204  1.00 65.85  ? 74  PRO E O   1 
ATOM   5041  C  CB  . PRO E  1 75  ? 49.671  253.353 47.428  1.00 70.67  ? 74  PRO E CB  1 
ATOM   5042  C  CG  . PRO E  1 75  ? 50.037  252.878 48.814  1.00 70.08  ? 74  PRO E CG  1 
ATOM   5043  C  CD  . PRO E  1 75  ? 51.408  252.277 48.704  1.00 66.10  ? 74  PRO E CD  1 
ATOM   5044  N  N   . LYS E  1 76  ? 52.084  253.648 45.255  1.00 66.21  ? 75  LYS E N   1 
ATOM   5045  C  CA  . LYS E  1 76  ? 52.595  254.345 44.070  1.00 66.70  ? 75  LYS E CA  1 
ATOM   5046  C  C   . LYS E  1 76  ? 53.313  253.409 43.068  1.00 67.53  ? 75  LYS E C   1 
ATOM   5047  O  O   . LYS E  1 76  ? 53.592  253.816 41.929  1.00 64.44  ? 75  LYS E O   1 
ATOM   5048  C  CB  . LYS E  1 76  ? 53.517  255.496 44.472  1.00 72.74  ? 75  LYS E CB  1 
ATOM   5049  C  CG  . LYS E  1 76  ? 52.755  256.702 44.964  1.00 74.63  ? 75  LYS E CG  1 
ATOM   5050  C  CD  . LYS E  1 76  ? 53.712  257.563 45.769  1.00 79.46  ? 75  LYS E CD  1 
ATOM   5051  C  CE  . LYS E  1 76  ? 53.113  258.968 45.854  1.00 75.41  ? 75  LYS E CE  1 
ATOM   5052  N  NZ  . LYS E  1 76  ? 54.109  259.761 46.633  1.00 68.80  ? 75  LYS E NZ  1 
ATOM   5053  N  N   . ASP E  1 77  ? 53.625  252.174 43.459  1.00 59.67  ? 76  ASP E N   1 
ATOM   5054  C  CA  . ASP E  1 77  ? 54.200  251.205 42.485  1.00 61.92  ? 76  ASP E CA  1 
ATOM   5055  C  C   . ASP E  1 77  ? 53.303  250.830 41.275  1.00 70.04  ? 76  ASP E C   1 
ATOM   5056  O  O   . ASP E  1 77  ? 52.058  250.631 41.441  1.00 65.40  ? 76  ASP E O   1 
ATOM   5057  C  CB  . ASP E  1 77  ? 54.664  249.946 43.212  1.00 61.03  ? 76  ASP E CB  1 
ATOM   5058  C  CG  . ASP E  1 77  ? 55.843  250.237 44.162  1.00 75.15  ? 76  ASP E CG  1 
ATOM   5059  O  OD1 . ASP E  1 77  ? 56.147  251.453 44.390  1.00 74.45  ? 76  ASP E OD1 1 
ATOM   5060  O  OD2 . ASP E  1 77  ? 56.469  249.262 44.666  1.00 66.86  ? 76  ASP E OD2 1 
ATOM   5061  N  N   . GLU E  1 78  ? 53.924  250.768 40.073  1.00 63.89  ? 77  GLU E N   1 
ATOM   5062  C  CA  . GLU E  1 78  ? 53.315  250.082 38.885  1.00 72.03  ? 77  GLU E CA  1 
ATOM   5063  C  C   . GLU E  1 78  ? 52.984  248.555 39.190  1.00 72.76  ? 77  GLU E C   1 
ATOM   5064  O  O   . GLU E  1 78  ? 51.945  247.994 38.726  1.00 63.71  ? 77  GLU E O   1 
ATOM   5065  C  CB  . GLU E  1 78  ? 54.198  250.239 37.614  1.00 63.23  ? 77  GLU E CB  1 
ATOM   5066  N  N   . GLU E  1 79  ? 53.877  247.930 39.979  1.00 64.24  ? 78  GLU E N   1 
ATOM   5067  C  CA  . GLU E  1 79  ? 53.788  246.517 40.415  1.00 67.52  ? 78  GLU E CA  1 
ATOM   5068  C  C   . GLU E  1 79  ? 53.291  246.526 41.892  1.00 72.25  ? 78  GLU E C   1 
ATOM   5069  O  O   . GLU E  1 79  ? 54.122  246.597 42.830  1.00 65.41  ? 78  GLU E O   1 
ATOM   5070  C  CB  . GLU E  1 79  ? 55.217  245.889 40.312  1.00 62.55  ? 78  GLU E CB  1 
ATOM   5071  C  CG  . GLU E  1 79  ? 55.361  244.389 40.473  1.00 58.11  ? 78  GLU E CG  1 
ATOM   5072  C  CD  . GLU E  1 79  ? 54.674  243.576 39.355  1.00 76.23  ? 78  GLU E CD  1 
ATOM   5073  O  OE1 . GLU E  1 79  ? 54.254  244.150 38.265  1.00 66.18  ? 78  GLU E OE1 1 
ATOM   5074  O  OE2 . GLU E  1 79  ? 54.547  242.317 39.576  1.00 68.66  ? 78  GLU E OE2 1 
ATOM   5075  N  N   . ARG E  1 80  ? 51.966  246.501 42.103  1.00 57.80  ? 79  ARG E N   1 
ATOM   5076  C  CA  . ARG E  1 80  ? 51.367  246.287 43.457  1.00 53.20  ? 79  ARG E CA  1 
ATOM   5077  C  C   . ARG E  1 80  ? 50.143  245.386 43.296  1.00 49.60  ? 79  ARG E C   1 
ATOM   5078  O  O   . ARG E  1 80  ? 49.561  245.338 42.193  1.00 50.37  ? 79  ARG E O   1 
ATOM   5079  C  CB  . ARG E  1 80  ? 50.909  247.608 44.029  1.00 44.56  ? 79  ARG E CB  1 
ATOM   5080  C  CG  . ARG E  1 80  ? 50.152  248.387 42.984  1.00 41.15  ? 79  ARG E CG  1 
ATOM   5081  C  CD  . ARG E  1 80  ? 49.499  249.584 43.624  1.00 48.05  ? 79  ARG E CD  1 
ATOM   5082  N  NE  . ARG E  1 80  ? 48.188  249.351 44.262  1.00 46.20  ? 79  ARG E NE  1 
ATOM   5083  C  CZ  . ARG E  1 80  ? 47.374  250.364 44.636  1.00 54.00  ? 79  ARG E CZ  1 
ATOM   5084  N  NH1 . ARG E  1 80  ? 47.769  251.646 44.428  1.00 46.82  ? 79  ARG E NH1 1 
ATOM   5085  N  NH2 . ARG E  1 80  ? 46.155  250.139 45.200  1.00 42.31  ? 79  ARG E NH2 1 
ATOM   5086  N  N   . HIS E  1 81  ? 49.717  244.719 44.358  1.00 44.40  ? 80  HIS E N   1 
ATOM   5087  C  CA  . HIS E  1 81  ? 48.320  244.221 44.398  1.00 43.15  ? 80  HIS E CA  1 
ATOM   5088  C  C   . HIS E  1 81  ? 47.331  245.406 44.360  1.00 39.95  ? 80  HIS E C   1 
ATOM   5089  O  O   . HIS E  1 81  ? 47.679  246.513 44.774  1.00 41.86  ? 80  HIS E O   1 
ATOM   5090  C  CB  . HIS E  1 81  ? 48.111  243.293 45.597  1.00 45.42  ? 80  HIS E CB  1 
ATOM   5091  C  CG  . HIS E  1 81  ? 49.169  242.202 45.712  1.00 59.04  ? 80  HIS E CG  1 
ATOM   5092  N  ND1 . HIS E  1 81  ? 50.013  242.076 46.804  1.00 52.47  ? 80  HIS E ND1 1 
ATOM   5093  C  CD2 . HIS E  1 81  ? 49.536  241.201 44.866  1.00 62.04  ? 80  HIS E CD2 1 
ATOM   5094  C  CE1 . HIS E  1 81  ? 50.798  241.026 46.665  1.00 50.76  ? 80  HIS E CE1 1 
ATOM   5095  N  NE2 . HIS E  1 81  ? 50.541  240.481 45.488  1.00 62.89  ? 80  HIS E NE2 1 
ATOM   5096  N  N   . VAL E  1 82  ? 46.136  245.193 43.811  1.00 39.82  ? 81  VAL E N   1 
ATOM   5097  C  CA  . VAL E  1 82  ? 45.041  246.168 43.873  1.00 35.19  ? 81  VAL E CA  1 
ATOM   5098  C  C   . VAL E  1 82  ? 44.739  246.429 45.330  1.00 35.73  ? 81  VAL E C   1 
ATOM   5099  O  O   . VAL E  1 82  ? 44.595  247.564 45.724  1.00 38.53  ? 81  VAL E O   1 
ATOM   5100  C  CB  . VAL E  1 82  ? 43.754  245.689 43.138  1.00 34.94  ? 81  VAL E CB  1 
ATOM   5101  C  CG1 . VAL E  1 82  ? 42.618  246.695 43.358  1.00 32.87  ? 81  VAL E CG1 1 
ATOM   5102  C  CG2 . VAL E  1 82  ? 44.013  245.508 41.648  1.00 31.01  ? 81  VAL E CG2 1 
ATOM   5103  N  N   . GLY E  1 83  ? 44.675  245.385 46.148  1.00 38.42  ? 82  GLY E N   1 
ATOM   5104  C  CA  . GLY E  1 83  ? 44.762  245.537 47.607  1.00 45.84  ? 82  GLY E CA  1 
ATOM   5105  C  C   . GLY E  1 83  ? 45.701  246.550 48.369  1.00 49.05  ? 82  GLY E C   1 
ATOM   5106  O  O   . GLY E  1 83  ? 45.488  246.848 49.606  1.00 42.26  ? 82  GLY E O   1 
ATOM   5107  N  N   . ASP E  1 84  ? 46.697  247.111 47.683  1.00 39.78  ? 83  ASP E N   1 
ATOM   5108  C  CA  . ASP E  1 84  ? 47.792  247.754 48.421  1.00 38.35  ? 83  ASP E CA  1 
ATOM   5109  C  C   . ASP E  1 84  ? 47.641  249.125 48.788  1.00 35.31  ? 83  ASP E C   1 
ATOM   5110  O  O   . ASP E  1 84  ? 48.124  249.965 48.114  1.00 40.32  ? 83  ASP E O   1 
ATOM   5111  C  CB  . ASP E  1 84  ? 49.134  247.517 47.775  1.00 41.40  ? 83  ASP E CB  1 
ATOM   5112  C  CG  . ASP E  1 84  ? 49.479  246.016 47.795  1.00 53.59  ? 83  ASP E CG  1 
ATOM   5113  O  OD1 . ASP E  1 84  ? 48.624  245.258 48.408  1.00 46.66  ? 83  ASP E OD1 1 
ATOM   5114  O  OD2 . ASP E  1 84  ? 50.533  245.610 47.181  1.00 55.27  ? 83  ASP E OD2 1 
ATOM   5115  N  N   . LEU E  1 85  ? 47.034  249.375 49.924  1.00 37.97  ? 84  LEU E N   1 
ATOM   5116  C  CA  . LEU E  1 85  ? 46.889  250.737 50.299  1.00 40.02  ? 84  LEU E CA  1 
ATOM   5117  C  C   . LEU E  1 85  ? 48.000  251.273 51.232  1.00 44.06  ? 84  LEU E C   1 
ATOM   5118  O  O   . LEU E  1 85  ? 47.751  252.227 51.933  1.00 41.86  ? 84  LEU E O   1 
ATOM   5119  C  CB  . LEU E  1 85  ? 45.492  250.990 50.849  1.00 42.09  ? 84  LEU E CB  1 
ATOM   5120  C  CG  . LEU E  1 85  ? 44.317  250.506 50.010  1.00 40.84  ? 84  LEU E CG  1 
ATOM   5121  C  CD1 . LEU E  1 85  ? 43.081  250.808 50.833  1.00 38.84  ? 84  LEU E CD1 1 
ATOM   5122  C  CD2 . LEU E  1 85  ? 44.343  251.315 48.743  1.00 36.91  ? 84  LEU E CD2 1 
ATOM   5123  N  N   . GLY E  1 86  ? 49.216  250.688 51.224  1.00 44.05  ? 85  GLY E N   1 
ATOM   5124  C  CA  . GLY E  1 86  ? 50.340  251.271 51.983  1.00 46.14  ? 85  GLY E CA  1 
ATOM   5125  C  C   . GLY E  1 86  ? 50.234  251.087 53.476  1.00 41.44  ? 85  GLY E C   1 
ATOM   5126  O  O   . GLY E  1 86  ? 49.860  250.007 53.930  1.00 45.58  ? 85  GLY E O   1 
ATOM   5127  N  N   . ASN E  1 87  ? 50.552  252.123 54.249  1.00 39.45  ? 86  ASN E N   1 
ATOM   5128  C  CA  . ASN E  1 87  ? 50.561  252.012 55.713  1.00 36.70  ? 86  ASN E CA  1 
ATOM   5129  C  C   . ASN E  1 87  ? 49.725  253.145 56.265  1.00 38.04  ? 86  ASN E C   1 
ATOM   5130  O  O   . ASN E  1 87  ? 49.620  254.210 55.663  1.00 36.31  ? 86  ASN E O   1 
ATOM   5131  C  CB  . ASN E  1 87  ? 51.959  252.258 56.265  1.00 38.13  ? 86  ASN E CB  1 
ATOM   5132  C  CG  . ASN E  1 87  ? 52.919  251.146 56.004  1.00 38.17  ? 86  ASN E CG  1 
ATOM   5133  O  OD1 . ASN E  1 87  ? 52.762  250.033 56.524  1.00 39.77  ? 86  ASN E OD1 1 
ATOM   5134  N  ND2 . ASN E  1 87  ? 53.965  251.446 55.258  1.00 35.31  ? 86  ASN E ND2 1 
ATOM   5135  N  N   . VAL E  1 88  ? 49.146  252.927 57.429  1.00 37.16  ? 87  VAL E N   1 
ATOM   5136  C  CA  . VAL E  1 88  ? 48.586  254.044 58.151  1.00 39.63  ? 87  VAL E CA  1 
ATOM   5137  C  C   . VAL E  1 88  ? 49.454  254.282 59.420  1.00 40.26  ? 87  VAL E C   1 
ATOM   5138  O  O   . VAL E  1 88  ? 50.219  253.417 59.831  1.00 40.29  ? 87  VAL E O   1 
ATOM   5139  C  CB  . VAL E  1 88  ? 47.128  253.784 58.563  1.00 40.64  ? 87  VAL E CB  1 
ATOM   5140  C  CG1 . VAL E  1 88  ? 46.209  253.741 57.342  1.00 37.96  ? 87  VAL E CG1 1 
ATOM   5141  C  CG2 . VAL E  1 88  ? 47.077  252.531 59.424  1.00 38.69  ? 87  VAL E CG2 1 
ATOM   5142  N  N   . THR E  1 89  ? 49.305  255.438 60.037  1.00 36.00  ? 88  THR E N   1 
ATOM   5143  C  CA  . THR E  1 89  ? 50.222  255.869 61.051  1.00 40.86  ? 88  THR E CA  1 
ATOM   5144  C  C   . THR E  1 89  ? 49.502  256.146 62.344  1.00 39.43  ? 88  THR E C   1 
ATOM   5145  O  O   . THR E  1 89  ? 48.694  257.077 62.433  1.00 37.28  ? 88  THR E O   1 
ATOM   5146  C  CB  . THR E  1 89  ? 50.915  257.200 60.648  1.00 45.73  ? 88  THR E CB  1 
ATOM   5147  O  OG1 . THR E  1 89  ? 51.438  257.062 59.308  1.00 51.30  ? 88  THR E OG1 1 
ATOM   5148  C  CG2 . THR E  1 89  ? 52.057  257.556 61.661  1.00 36.04  ? 88  THR E CG2 1 
ATOM   5149  N  N   . ALA E  1 90  ? 49.849  255.392 63.376  1.00 38.55  ? 89  ALA E N   1 
ATOM   5150  C  CA  . ALA E  1 90  ? 49.220  255.675 64.645  1.00 41.78  ? 89  ALA E CA  1 
ATOM   5151  C  C   . ALA E  1 90  ? 50.087  256.633 65.441  1.00 44.10  ? 89  ALA E C   1 
ATOM   5152  O  O   . ALA E  1 90  ? 51.336  256.495 65.495  1.00 43.73  ? 89  ALA E O   1 
ATOM   5153  C  CB  . ALA E  1 90  ? 48.959  254.395 65.401  1.00 40.67  ? 89  ALA E CB  1 
ATOM   5154  N  N   . ASP E  1 91  ? 49.413  257.593 66.064  1.00 42.13  ? 90  ASP E N   1 
ATOM   5155  C  CA  . ASP E  1 91  ? 50.072  258.535 66.934  1.00 43.01  ? 90  ASP E CA  1 
ATOM   5156  C  C   . ASP E  1 91  ? 50.332  257.968 68.352  1.00 44.09  ? 90  ASP E C   1 
ATOM   5157  O  O   . ASP E  1 91  ? 50.182  256.757 68.631  1.00 43.11  ? 90  ASP E O   1 
ATOM   5158  C  CB  . ASP E  1 91  ? 49.251  259.847 66.978  1.00 42.66  ? 90  ASP E CB  1 
ATOM   5159  C  CG  . ASP E  1 91  ? 47.909  259.691 67.716  1.00 46.06  ? 90  ASP E CG  1 
ATOM   5160  O  OD1 . ASP E  1 91  ? 47.650  258.708 68.468  1.00 44.60  ? 90  ASP E OD1 1 
ATOM   5161  O  OD2 . ASP E  1 91  ? 47.077  260.577 67.546  1.00 43.81  ? 90  ASP E OD2 1 
ATOM   5162  N  N   . LYS E  1 92  ? 50.645  258.849 69.289  1.00 43.52  ? 91  LYS E N   1 
ATOM   5163  C  CA  . LYS E  1 92  ? 51.108  258.338 70.564  1.00 45.36  ? 91  LYS E CA  1 
ATOM   5164  C  C   . LYS E  1 92  ? 49.881  257.902 71.372  1.00 42.03  ? 91  LYS E C   1 
ATOM   5165  O  O   . LYS E  1 92  ? 49.978  257.094 72.291  1.00 39.43  ? 91  LYS E O   1 
ATOM   5166  C  CB  . LYS E  1 92  ? 51.973  259.385 71.302  1.00 46.38  ? 91  LYS E CB  1 
ATOM   5167  C  CG  . LYS E  1 92  ? 51.316  260.744 71.321  1.00 55.19  ? 91  LYS E CG  1 
ATOM   5168  C  CD  . LYS E  1 92  ? 51.292  261.448 72.658  1.00 59.91  ? 91  LYS E CD  1 
ATOM   5169  C  CE  . LYS E  1 92  ? 51.097  262.947 72.373  1.00 65.34  ? 91  LYS E CE  1 
ATOM   5170  N  NZ  . LYS E  1 92  ? 50.614  263.614 73.620  1.00 68.03  ? 91  LYS E NZ  1 
ATOM   5171  N  N   . ASP E  1 93  ? 48.725  258.476 71.048  1.00 47.25  ? 92  ASP E N   1 
ATOM   5172  C  CA  . ASP E  1 93  ? 47.424  258.007 71.598  1.00 44.97  ? 92  ASP E CA  1 
ATOM   5173  C  C   . ASP E  1 93  ? 46.819  256.684 71.009  1.00 40.45  ? 92  ASP E C   1 
ATOM   5174  O  O   . ASP E  1 93  ? 45.763  256.253 71.409  1.00 39.90  ? 92  ASP E O   1 
ATOM   5175  C  CB  . ASP E  1 93  ? 46.457  259.166 71.574  1.00 42.43  ? 92  ASP E CB  1 
ATOM   5176  C  CG  . ASP E  1 93  ? 46.813  260.202 72.664  1.00 56.79  ? 92  ASP E CG  1 
ATOM   5177  O  OD1 . ASP E  1 93  ? 47.002  259.816 73.863  1.00 58.21  ? 92  ASP E OD1 1 
ATOM   5178  O  OD2 . ASP E  1 93  ? 46.959  261.403 72.342  1.00 55.46  ? 92  ASP E OD2 1 
ATOM   5179  N  N   . GLY E  1 94  ? 47.543  256.050 70.102  1.00 36.34  ? 93  GLY E N   1 
ATOM   5180  C  CA  . GLY E  1 94  ? 47.067  254.925 69.336  1.00 37.75  ? 93  GLY E CA  1 
ATOM   5181  C  C   . GLY E  1 94  ? 46.047  255.145 68.235  1.00 39.92  ? 93  GLY E C   1 
ATOM   5182  O  O   . GLY E  1 94  ? 45.509  254.151 67.741  1.00 41.81  ? 93  GLY E O   1 
ATOM   5183  N  N   . VAL E  1 95  ? 45.756  256.411 67.895  1.00 36.30  ? 94  VAL E N   1 
ATOM   5184  C  CA  . VAL E  1 95  ? 44.862  256.773 66.840  1.00 38.03  ? 94  VAL E CA  1 
ATOM   5185  C  C   . VAL E  1 95  ? 45.557  257.022 65.435  1.00 41.42  ? 94  VAL E C   1 
ATOM   5186  O  O   . VAL E  1 95  ? 46.450  257.867 65.343  1.00 46.31  ? 94  VAL E O   1 
ATOM   5187  C  CB  . VAL E  1 95  ? 44.037  257.995 67.277  1.00 41.88  ? 94  VAL E CB  1 
ATOM   5188  C  CG1 . VAL E  1 95  ? 43.369  258.615 66.053  1.00 42.17  ? 94  VAL E CG1 1 
ATOM   5189  C  CG2 . VAL E  1 95  ? 42.971  257.637 68.339  1.00 38.63  ? 94  VAL E CG2 1 
ATOM   5190  N  N   . ALA E  1 96  ? 45.145  256.301 64.365  1.00 37.40  ? 95  ALA E N   1 
ATOM   5191  C  CA  . ALA E  1 96  ? 45.531  256.622 62.968  1.00 34.83  ? 95  ALA E CA  1 
ATOM   5192  C  C   . ALA E  1 96  ? 44.452  257.418 62.266  1.00 37.17  ? 95  ALA E C   1 
ATOM   5193  O  O   . ALA E  1 96  ? 43.295  256.984 62.153  1.00 41.90  ? 95  ALA E O   1 
ATOM   5194  C  CB  . ALA E  1 96  ? 45.852  255.384 62.182  1.00 34.56  ? 95  ALA E CB  1 
ATOM   5195  N  N   . ASP E  1 97  ? 44.778  258.622 61.839  1.00 41.29  ? 96  ASP E N   1 
ATOM   5196  C  CA  . ASP E  1 97  ? 43.872  259.291 60.917  1.00 44.67  ? 96  ASP E CA  1 
ATOM   5197  C  C   . ASP E  1 97  ? 44.169  258.943 59.485  1.00 44.75  ? 96  ASP E C   1 
ATOM   5198  O  O   . ASP E  1 97  ? 45.326  259.051 59.004  1.00 41.47  ? 96  ASP E O   1 
ATOM   5199  C  CB  . ASP E  1 97  ? 43.742  260.759 61.160  1.00 45.74  ? 96  ASP E CB  1 
ATOM   5200  C  CG  . ASP E  1 97  ? 43.169  261.053 62.580  1.00 59.69  ? 96  ASP E CG  1 
ATOM   5201  O  OD1 . ASP E  1 97  ? 42.226  260.336 63.134  1.00 54.09  ? 96  ASP E OD1 1 
ATOM   5202  O  OD2 . ASP E  1 97  ? 43.705  262.038 63.163  1.00 60.47  ? 96  ASP E OD2 1 
ATOM   5203  N  N   . VAL E  1 98  ? 43.122  258.430 58.833  1.00 46.65  ? 97  VAL E N   1 
ATOM   5204  C  CA  . VAL E  1 98  ? 43.299  257.839 57.492  1.00 44.96  ? 97  VAL E CA  1 
ATOM   5205  C  C   . VAL E  1 98  ? 42.817  258.848 56.497  1.00 38.74  ? 97  VAL E C   1 
ATOM   5206  O  O   . VAL E  1 98  ? 41.747  259.466 56.681  1.00 39.31  ? 97  VAL E O   1 
ATOM   5207  C  CB  . VAL E  1 98  ? 42.719  256.412 57.402  1.00 44.60  ? 97  VAL E CB  1 
ATOM   5208  C  CG1 . VAL E  1 98  ? 42.891  255.798 55.996  1.00 42.49  ? 97  VAL E CG1 1 
ATOM   5209  C  CG2 . VAL E  1 98  ? 43.444  255.559 58.435  1.00 39.03  ? 97  VAL E CG2 1 
ATOM   5210  N  N   . SER E  1 99  ? 43.691  259.124 55.543  1.00 37.77  ? 98  SER E N   1 
ATOM   5211  C  CA  . SER E  1 99  ? 43.308  259.998 54.415  1.00 43.41  ? 98  SER E CA  1 
ATOM   5212  C  C   . SER E  1 99  ? 44.113  259.724 53.134  1.00 44.95  ? 98  SER E C   1 
ATOM   5213  O  O   . SER E  1 99  ? 45.199  260.169 53.055  1.00 46.98  ? 98  SER E O   1 
ATOM   5214  C  CB  . SER E  1 99  ? 43.440  261.437 54.772  1.00 34.60  ? 98  SER E CB  1 
ATOM   5215  O  OG  . SER E  1 99  ? 43.241  262.079 53.586  1.00 38.58  ? 98  SER E OG  1 
ATOM   5216  N  N   . ILE E  1 100 ? 43.529  259.025 52.161  1.00 43.65  ? 99  ILE E N   1 
ATOM   5217  C  CA  . ILE E  1 100 ? 44.203  258.435 51.049  1.00 42.69  ? 99  ILE E CA  1 
ATOM   5218  C  C   . ILE E  1 100 ? 43.376  258.771 49.828  1.00 42.85  ? 99  ILE E C   1 
ATOM   5219  O  O   . ILE E  1 100 ? 42.137  258.908 49.851  1.00 40.30  ? 99  ILE E O   1 
ATOM   5220  C  CB  . ILE E  1 100 ? 44.151  256.887 51.251  1.00 51.34  ? 99  ILE E CB  1 
ATOM   5221  C  CG1 . ILE E  1 100 ? 44.987  256.511 52.478  1.00 55.60  ? 99  ILE E CG1 1 
ATOM   5222  C  CG2 . ILE E  1 100 ? 44.642  256.073 50.051  1.00 51.95  ? 99  ILE E CG2 1 
ATOM   5223  C  CD1 . ILE E  1 100 ? 45.201  255.024 52.694  1.00 53.85  ? 99  ILE E CD1 1 
ATOM   5224  N  N   . GLU E  1 101 ? 44.061  258.834 48.709  1.00 44.13  ? 100 GLU E N   1 
ATOM   5225  C  CA  . GLU E  1 101 ? 43.363  258.924 47.446  1.00 41.79  ? 100 GLU E CA  1 
ATOM   5226  C  C   . GLU E  1 101 ? 43.982  257.857 46.489  1.00 39.14  ? 100 GLU E C   1 
ATOM   5227  O  O   . GLU E  1 101 ? 45.180  257.834 46.249  1.00 41.52  ? 100 GLU E O   1 
ATOM   5228  C  CB  . GLU E  1 101 ? 43.346  260.394 46.981  1.00 42.92  ? 100 GLU E CB  1 
ATOM   5229  C  CG  . GLU E  1 101 ? 43.207  260.490 45.483  1.00 58.17  ? 100 GLU E CG  1 
ATOM   5230  C  CD  . GLU E  1 101 ? 42.598  261.767 44.953  1.00 55.15  ? 100 GLU E CD  1 
ATOM   5231  O  OE1 . GLU E  1 101 ? 41.635  262.258 45.577  1.00 53.79  ? 100 GLU E OE1 1 
ATOM   5232  O  OE2 . GLU E  1 101 ? 43.064  262.194 43.850  1.00 55.48  ? 100 GLU E OE2 1 
ATOM   5233  N  N   . ASP E  1 102 ? 43.199  256.895 46.035  1.00 36.86  ? 101 ASP E N   1 
ATOM   5234  C  CA  . ASP E  1 102 ? 43.807  255.838 45.256  1.00 38.46  ? 101 ASP E CA  1 
ATOM   5235  C  C   . ASP E  1 102 ? 43.086  255.659 43.904  1.00 41.17  ? 101 ASP E C   1 
ATOM   5236  O  O   . ASP E  1 102 ? 41.865  255.853 43.804  1.00 38.62  ? 101 ASP E O   1 
ATOM   5237  C  CB  . ASP E  1 102 ? 43.918  254.541 46.064  1.00 36.28  ? 101 ASP E CB  1 
ATOM   5238  C  CG  . ASP E  1 102 ? 44.767  253.470 45.361  1.00 42.96  ? 101 ASP E CG  1 
ATOM   5239  O  OD1 . ASP E  1 102 ? 46.019  253.399 45.505  1.00 50.48  ? 101 ASP E OD1 1 
ATOM   5240  O  OD2 . ASP E  1 102 ? 44.181  252.670 44.635  1.00 48.27  ? 101 ASP E OD2 1 
ATOM   5241  N  N   . SER E  1 103 ? 43.866  255.305 42.886  1.00 40.56  ? 102 SER E N   1 
ATOM   5242  C  CA  . SER E  1 103 ? 43.391  255.176 41.489  1.00 43.62  ? 102 SER E CA  1 
ATOM   5243  C  C   . SER E  1 103 ? 43.458  253.741 41.070  1.00 42.29  ? 102 SER E C   1 
ATOM   5244  O  O   . SER E  1 103 ? 43.080  253.450 39.962  1.00 47.10  ? 102 SER E O   1 
ATOM   5245  C  CB  . SER E  1 103 ? 44.270  255.955 40.496  1.00 41.03  ? 102 SER E CB  1 
ATOM   5246  O  OG  . SER E  1 103 ? 44.120  257.325 40.769  1.00 48.78  ? 102 SER E OG  1 
ATOM   5247  N  N   . VAL E  1 104 ? 43.965  252.850 41.905  1.00 36.15  ? 103 VAL E N   1 
ATOM   5248  C  CA  . VAL E  1 104 ? 44.007  251.486 41.488  1.00 35.92  ? 103 VAL E CA  1 
ATOM   5249  C  C   . VAL E  1 104 ? 42.717  250.744 41.886  1.00 38.17  ? 103 VAL E C   1 
ATOM   5250  O  O   . VAL E  1 104 ? 42.047  250.113 41.005  1.00 39.10  ? 103 VAL E O   1 
ATOM   5251  C  CB  . VAL E  1 104 ? 45.311  250.862 41.934  1.00 34.87  ? 103 VAL E CB  1 
ATOM   5252  C  CG1 . VAL E  1 104 ? 45.331  249.359 41.707  1.00 34.58  ? 103 VAL E CG1 1 
ATOM   5253  C  CG2 . VAL E  1 104 ? 46.391  251.542 41.147  1.00 30.44  ? 103 VAL E CG2 1 
ATOM   5254  N  N   . ILE E  1 105 ? 42.367  250.836 43.175  1.00 36.28  ? 104 ILE E N   1 
ATOM   5255  C  CA  . ILE E  1 105 ? 41.095  250.316 43.699  1.00 34.02  ? 104 ILE E CA  1 
ATOM   5256  C  C   . ILE E  1 105 ? 39.900  251.038 43.002  1.00 34.15  ? 104 ILE E C   1 
ATOM   5257  O  O   . ILE E  1 105 ? 40.059  252.128 42.481  1.00 38.96  ? 104 ILE E O   1 
ATOM   5258  C  CB  . ILE E  1 105 ? 41.009  250.467 45.229  1.00 30.40  ? 104 ILE E CB  1 
ATOM   5259  C  CG1 . ILE E  1 105 ? 41.079  251.933 45.638  1.00 31.98  ? 104 ILE E CG1 1 
ATOM   5260  C  CG2 . ILE E  1 105 ? 42.128  249.755 45.927  1.00 29.68  ? 104 ILE E CG2 1 
ATOM   5261  C  CD1 . ILE E  1 105 ? 40.601  252.241 47.080  1.00 27.05  ? 104 ILE E CD1 1 
ATOM   5262  N  N   . SER E  1 106 ? 38.734  250.405 42.960  1.00 33.37  ? 105 SER E N   1 
ATOM   5263  C  CA  . SER E  1 106 ? 37.501  250.998 42.440  1.00 32.28  ? 105 SER E CA  1 
ATOM   5264  C  C   . SER E  1 106 ? 36.294  250.485 43.241  1.00 34.74  ? 105 SER E C   1 
ATOM   5265  O  O   . SER E  1 106 ? 36.305  249.375 43.775  1.00 38.73  ? 105 SER E O   1 
ATOM   5266  C  CB  . SER E  1 106 ? 37.299  250.625 40.964  1.00 28.79  ? 105 SER E CB  1 
ATOM   5267  O  OG  . SER E  1 106 ? 36.282  251.426 40.423  1.00 33.10  ? 105 SER E OG  1 
ATOM   5268  N  N   . LEU E  1 107 ? 35.239  251.268 43.286  1.00 33.70  ? 106 LEU E N   1 
ATOM   5269  C  CA  . LEU E  1 107 ? 33.996  250.807 43.857  1.00 35.12  ? 106 LEU E CA  1 
ATOM   5270  C  C   . LEU E  1 107 ? 33.069  250.068 42.857  1.00 37.63  ? 106 LEU E C   1 
ATOM   5271  O  O   . LEU E  1 107 ? 31.975  249.689 43.225  1.00 36.54  ? 106 LEU E O   1 
ATOM   5272  C  CB  . LEU E  1 107 ? 33.260  251.968 44.538  1.00 30.82  ? 106 LEU E CB  1 
ATOM   5273  C  CG  . LEU E  1 107 ? 34.108  252.574 45.656  1.00 32.07  ? 106 LEU E CG  1 
ATOM   5274  C  CD1 . LEU E  1 107 ? 33.278  253.666 46.289  1.00 30.79  ? 106 LEU E CD1 1 
ATOM   5275  C  CD2 . LEU E  1 107 ? 34.727  251.607 46.659  1.00 26.68  ? 106 LEU E CD2 1 
ATOM   5276  N  N   . SER E  1 108 ? 33.502  249.899 41.608  1.00 40.00  ? 107 SER E N   1 
ATOM   5277  C  CA  . SER E  1 108 ? 32.758  249.138 40.565  1.00 41.22  ? 107 SER E CA  1 
ATOM   5278  C  C   . SER E  1 108 ? 33.733  248.450 39.619  1.00 40.76  ? 107 SER E C   1 
ATOM   5279  O  O   . SER E  1 108 ? 34.932  248.806 39.646  1.00 37.27  ? 107 SER E O   1 
ATOM   5280  C  CB  . SER E  1 108 ? 31.761  250.013 39.802  1.00 36.15  ? 107 SER E CB  1 
ATOM   5281  O  OG  . SER E  1 108 ? 32.212  251.342 39.650  1.00 35.73  ? 107 SER E OG  1 
ATOM   5282  N  N   . GLY E  1 109 ? 33.219  247.465 38.845  1.00 40.21  ? 108 GLY E N   1 
ATOM   5283  C  CA  . GLY E  1 109 ? 33.951  246.712 37.819  1.00 39.32  ? 108 GLY E CA  1 
ATOM   5284  C  C   . GLY E  1 109 ? 34.861  245.646 38.355  1.00 48.63  ? 108 GLY E C   1 
ATOM   5285  O  O   . GLY E  1 109 ? 34.668  245.195 39.473  1.00 55.96  ? 108 GLY E O   1 
ATOM   5286  N  N   . ASP E  1 110 ? 35.885  245.265 37.570  1.00 55.46  ? 109 ASP E N   1 
ATOM   5287  C  CA  . ASP E  1 110 ? 36.917  244.206 37.913  1.00 52.72  ? 109 ASP E CA  1 
ATOM   5288  C  C   . ASP E  1 110 ? 37.753  244.474 39.128  1.00 47.80  ? 109 ASP E C   1 
ATOM   5289  O  O   . ASP E  1 110 ? 38.352  243.572 39.678  1.00 50.97  ? 109 ASP E O   1 
ATOM   5290  C  CB  . ASP E  1 110 ? 37.906  243.989 36.686  1.00 57.47  ? 109 ASP E CB  1 
ATOM   5291  C  CG  . ASP E  1 110 ? 39.248  243.139 37.039  1.00 61.40  ? 109 ASP E CG  1 
ATOM   5292  O  OD1 . ASP E  1 110 ? 39.273  242.033 37.646  1.00 61.83  ? 109 ASP E OD1 1 
ATOM   5293  O  OD2 . ASP E  1 110 ? 40.352  243.567 36.685  1.00 64.08  ? 109 ASP E OD2 1 
ATOM   5294  N  N   . HIS E  1 111 ? 37.887  245.736 39.470  1.00 49.74  ? 110 HIS E N   1 
ATOM   5295  C  CA  . HIS E  1 111 ? 38.820  246.168 40.519  1.00 53.45  ? 110 HIS E CA  1 
ATOM   5296  C  C   . HIS E  1 111 ? 38.034  246.531 41.774  1.00 53.90  ? 110 HIS E C   1 
ATOM   5297  O  O   . HIS E  1 111 ? 38.579  247.329 42.658  1.00 43.70  ? 110 HIS E O   1 
ATOM   5298  C  CB  . HIS E  1 111 ? 39.660  247.407 40.061  1.00 50.70  ? 110 HIS E CB  1 
ATOM   5299  C  CG  . HIS E  1 111 ? 40.942  247.051 39.367  1.00 57.71  ? 110 HIS E CG  1 
ATOM   5300  N  ND1 . HIS E  1 111 ? 41.982  247.950 39.197  1.00 60.39  ? 110 HIS E ND1 1 
ATOM   5301  C  CD2 . HIS E  1 111 ? 41.364  245.881 38.824  1.00 52.66  ? 110 HIS E CD2 1 
ATOM   5302  C  CE1 . HIS E  1 111 ? 42.965  247.360 38.534  1.00 56.97  ? 110 HIS E CE1 1 
ATOM   5303  N  NE2 . HIS E  1 111 ? 42.628  246.094 38.329  1.00 53.95  ? 110 HIS E NE2 1 
ATOM   5304  N  N   . CYS E  1 112 ? 36.781  246.005 41.803  1.00 39.68  ? 111 CYS E N   1 
ATOM   5305  C  CA  . CYS E  1 112 ? 35.811  246.449 42.753  1.00 38.15  ? 111 CYS E CA  1 
ATOM   5306  C  C   . CYS E  1 112 ? 36.165  245.854 44.099  1.00 34.60  ? 111 CYS E C   1 
ATOM   5307  O  O   . CYS E  1 112 ? 36.355  244.666 44.235  1.00 36.79  ? 111 CYS E O   1 
ATOM   5308  C  CB  . CYS E  1 112 ? 34.472  245.965 42.298  1.00 41.35  ? 111 CYS E CB  1 
ATOM   5309  S  SG  . CYS E  1 112 ? 33.146  246.300 43.456  1.00 39.52  ? 111 CYS E SG  1 
ATOM   5310  N  N   . ILE E  1 113 ? 36.303  246.693 45.095  1.00 35.95  ? 112 ILE E N   1 
ATOM   5311  C  CA  . ILE E  1 113 ? 36.649  246.190 46.438  1.00 39.20  ? 112 ILE E CA  1 
ATOM   5312  C  C   . ILE E  1 113 ? 35.421  245.989 47.355  1.00 35.98  ? 112 ILE E C   1 
ATOM   5313  O  O   . ILE E  1 113 ? 35.564  245.544 48.479  1.00 34.52  ? 112 ILE E O   1 
ATOM   5314  C  CB  . ILE E  1 113 ? 37.728  247.055 47.080  1.00 34.51  ? 112 ILE E CB  1 
ATOM   5315  C  CG1 . ILE E  1 113 ? 37.239  248.470 47.146  1.00 33.58  ? 112 ILE E CG1 1 
ATOM   5316  C  CG2 . ILE E  1 113 ? 39.032  246.888 46.301  1.00 32.50  ? 112 ILE E CG2 1 
ATOM   5317  C  CD1 . ILE E  1 113 ? 38.073  249.335 48.083  1.00 39.26  ? 112 ILE E CD1 1 
ATOM   5318  N  N   . ILE E  1 114 ? 34.226  246.290 46.847  1.00 31.92  ? 113 ILE E N   1 
ATOM   5319  C  CA  . ILE E  1 114 ? 33.035  246.050 47.606  1.00 33.99  ? 113 ILE E CA  1 
ATOM   5320  C  C   . ILE E  1 114 ? 32.827  244.581 47.837  1.00 34.85  ? 113 ILE E C   1 
ATOM   5321  O  O   . ILE E  1 114 ? 33.039  243.779 46.942  1.00 32.72  ? 113 ILE E O   1 
ATOM   5322  C  CB  . ILE E  1 114 ? 31.856  246.707 46.946  1.00 36.04  ? 113 ILE E CB  1 
ATOM   5323  C  CG1 . ILE E  1 114 ? 31.997  248.186 47.234  1.00 34.68  ? 113 ILE E CG1 1 
ATOM   5324  C  CG2 . ILE E  1 114 ? 30.548  246.178 47.496  1.00 34.09  ? 113 ILE E CG2 1 
ATOM   5325  C  CD1 . ILE E  1 114 ? 30.935  249.022 46.624  1.00 34.94  ? 113 ILE E CD1 1 
ATOM   5326  N  N   . GLY E  1 115 ? 32.512  244.233 49.088  1.00 33.85  ? 114 GLY E N   1 
ATOM   5327  C  CA  . GLY E  1 115 ? 32.356  242.856 49.478  1.00 32.91  ? 114 GLY E CA  1 
ATOM   5328  C  C   . GLY E  1 115 ? 33.664  242.078 49.698  1.00 33.57  ? 114 GLY E C   1 
ATOM   5329  O  O   . GLY E  1 115 ? 33.630  240.840 49.955  1.00 30.72  ? 114 GLY E O   1 
ATOM   5330  N  N   . ARG E  1 116 ? 34.788  242.788 49.590  1.00 28.49  ? 115 ARG E N   1 
ATOM   5331  C  CA  . ARG E  1 116 ? 36.055  242.317 50.121  1.00 32.15  ? 115 ARG E CA  1 
ATOM   5332  C  C   . ARG E  1 116 ? 36.343  242.821 51.523  1.00 32.34  ? 115 ARG E C   1 
ATOM   5333  O  O   . ARG E  1 116 ? 35.558  243.561 52.071  1.00 33.46  ? 115 ARG E O   1 
ATOM   5334  C  CB  . ARG E  1 116 ? 37.172  242.673 49.161  1.00 31.23  ? 115 ARG E CB  1 
ATOM   5335  C  CG  . ARG E  1 116 ? 36.736  242.267 47.808  1.00 33.17  ? 115 ARG E CG  1 
ATOM   5336  C  CD  . ARG E  1 116 ? 37.829  242.136 46.787  1.00 35.31  ? 115 ARG E CD  1 
ATOM   5337  N  NE  . ARG E  1 116 ? 37.276  241.808 45.443  1.00 33.76  ? 115 ARG E NE  1 
ATOM   5338  C  CZ  . ARG E  1 116 ? 37.073  240.579 44.973  1.00 30.33  ? 115 ARG E CZ  1 
ATOM   5339  N  NH1 . ARG E  1 116 ? 37.360  239.482 45.622  1.00 30.79  ? 115 ARG E NH1 1 
ATOM   5340  N  NH2 . ARG E  1 116 ? 36.619  240.434 43.797  1.00 35.72  ? 115 ARG E NH2 1 
ATOM   5341  N  N   . THR E  1 117 ? 37.479  242.427 52.105  1.00 33.21  ? 116 THR E N   1 
ATOM   5342  C  CA  . THR E  1 117 ? 37.849  242.857 53.458  1.00 30.70  ? 116 THR E CA  1 
ATOM   5343  C  C   . THR E  1 117 ? 38.969  243.867 53.540  1.00 29.92  ? 116 THR E C   1 
ATOM   5344  O  O   . THR E  1 117 ? 39.959  243.804 52.884  1.00 30.36  ? 116 THR E O   1 
ATOM   5345  C  CB  . THR E  1 117 ? 38.218  241.653 54.304  1.00 32.80  ? 116 THR E CB  1 
ATOM   5346  O  OG1 . THR E  1 117 ? 37.161  240.707 54.256  1.00 30.93  ? 116 THR E OG1 1 
ATOM   5347  C  CG2 . THR E  1 117 ? 38.528  242.072 55.800  1.00 31.85  ? 116 THR E CG2 1 
ATOM   5348  N  N   . LEU E  1 118 ? 38.771  244.844 54.358  1.00 31.92  ? 117 LEU E N   1 
ATOM   5349  C  CA  . LEU E  1 118 ? 39.810  245.759 54.638  1.00 31.75  ? 117 LEU E CA  1 
ATOM   5350  C  C   . LEU E  1 118 ? 40.482  245.313 55.946  1.00 33.68  ? 117 LEU E C   1 
ATOM   5351  O  O   . LEU E  1 118 ? 39.805  244.940 56.904  1.00 33.65  ? 117 LEU E O   1 
ATOM   5352  C  CB  . LEU E  1 118 ? 39.230  247.133 54.758  1.00 30.30  ? 117 LEU E CB  1 
ATOM   5353  C  CG  . LEU E  1 118 ? 40.184  248.281 55.090  1.00 32.36  ? 117 LEU E CG  1 
ATOM   5354  C  CD1 . LEU E  1 118 ? 41.248  248.479 53.991  1.00 28.80  ? 117 LEU E CD1 1 
ATOM   5355  C  CD2 . LEU E  1 118 ? 39.384  249.529 55.375  1.00 29.18  ? 117 LEU E CD2 1 
ATOM   5356  N  N   . VAL E  1 119 ? 41.812  245.294 55.949  1.00 35.49  ? 118 VAL E N   1 
ATOM   5357  C  CA  . VAL E  1 119 ? 42.591  244.763 57.083  1.00 34.01  ? 118 VAL E CA  1 
ATOM   5358  C  C   . VAL E  1 119 ? 43.718  245.690 57.439  1.00 33.02  ? 118 VAL E C   1 
ATOM   5359  O  O   . VAL E  1 119 ? 44.489  246.147 56.566  1.00 31.96  ? 118 VAL E O   1 
ATOM   5360  C  CB  . VAL E  1 119 ? 43.170  243.385 56.797  1.00 33.68  ? 118 VAL E CB  1 
ATOM   5361  C  CG1 . VAL E  1 119 ? 43.980  242.842 57.949  1.00 33.23  ? 118 VAL E CG1 1 
ATOM   5362  C  CG2 . VAL E  1 119 ? 42.083  242.432 56.441  1.00 37.40  ? 118 VAL E CG2 1 
ATOM   5363  N  N   . VAL E  1 120 ? 43.740  246.030 58.721  1.00 35.07  ? 119 VAL E N   1 
ATOM   5364  C  CA  . VAL E  1 120 ? 44.829  246.745 59.320  1.00 36.36  ? 119 VAL E CA  1 
ATOM   5365  C  C   . VAL E  1 120 ? 45.756  245.728 60.019  1.00 35.23  ? 119 VAL E C   1 
ATOM   5366  O  O   . VAL E  1 120 ? 45.338  244.954 60.827  1.00 37.38  ? 119 VAL E O   1 
ATOM   5367  C  CB  . VAL E  1 120 ? 44.333  247.905 60.191  1.00 38.23  ? 119 VAL E CB  1 
ATOM   5368  C  CG1 . VAL E  1 120 ? 43.455  247.397 61.308  1.00 37.92  ? 119 VAL E CG1 1 
ATOM   5369  C  CG2 . VAL E  1 120 ? 45.531  248.643 60.760  1.00 44.12  ? 119 VAL E CG2 1 
ATOM   5370  N  N   . HIS E  1 121 ? 47.002  245.709 59.619  1.00 37.05  ? 120 HIS E N   1 
ATOM   5371  C  CA  . HIS E  1 121 ? 48.008  244.789 60.139  1.00 40.02  ? 120 HIS E CA  1 
ATOM   5372  C  C   . HIS E  1 121 ? 48.844  245.255 61.323  1.00 36.54  ? 120 HIS E C   1 
ATOM   5373  O  O   . HIS E  1 121 ? 48.966  246.464 61.606  1.00 40.40  ? 120 HIS E O   1 
ATOM   5374  C  CB  . HIS E  1 121 ? 48.936  244.400 59.006  1.00 38.05  ? 120 HIS E CB  1 
ATOM   5375  C  CG  . HIS E  1 121 ? 48.266  243.615 57.951  1.00 39.39  ? 120 HIS E CG  1 
ATOM   5376  N  ND1 . HIS E  1 121 ? 48.366  242.236 57.877  1.00 40.42  ? 120 HIS E ND1 1 
ATOM   5377  C  CD2 . HIS E  1 121 ? 47.428  244.000 56.956  1.00 39.84  ? 120 HIS E CD2 1 
ATOM   5378  C  CE1 . HIS E  1 121 ? 47.657  241.817 56.836  1.00 42.80  ? 120 HIS E CE1 1 
ATOM   5379  N  NE2 . HIS E  1 121 ? 47.072  242.867 56.265  1.00 38.77  ? 120 HIS E NE2 1 
ATOM   5380  N  N   . GLU E  1 122 ? 49.403  244.278 62.012  1.00 38.06  ? 121 GLU E N   1 
ATOM   5381  C  CA  . GLU E  1 122 ? 50.217  244.493 63.231  1.00 45.53  ? 121 GLU E CA  1 
ATOM   5382  C  C   . GLU E  1 122 ? 51.480  245.335 62.963  1.00 48.55  ? 121 GLU E C   1 
ATOM   5383  O  O   . GLU E  1 122 ? 51.755  246.261 63.683  1.00 50.08  ? 121 GLU E O   1 
ATOM   5384  C  CB  . GLU E  1 122 ? 50.621  243.139 63.776  1.00 49.43  ? 121 GLU E CB  1 
ATOM   5385  C  CG  . GLU E  1 122 ? 51.403  243.129 65.070  1.00 51.00  ? 121 GLU E CG  1 
ATOM   5386  C  CD  . GLU E  1 122 ? 52.183  241.801 65.256  1.00 59.16  ? 121 GLU E CD  1 
ATOM   5387  O  OE1 . GLU E  1 122 ? 52.375  241.417 66.432  1.00 61.09  ? 121 GLU E OE1 1 
ATOM   5388  O  OE2 . GLU E  1 122 ? 52.618  241.125 64.261  1.00 52.35  ? 121 GLU E OE2 1 
ATOM   5389  N  N   . LYS E  1 123 ? 52.210  245.020 61.906  1.00 45.79  ? 122 LYS E N   1 
ATOM   5390  C  CA  . LYS E  1 123 ? 53.479  245.660 61.581  1.00 50.40  ? 122 LYS E CA  1 
ATOM   5391  C  C   . LYS E  1 123 ? 53.417  246.529 60.306  1.00 51.13  ? 122 LYS E C   1 
ATOM   5392  O  O   . LYS E  1 123 ? 52.468  246.456 59.522  1.00 49.12  ? 122 LYS E O   1 
ATOM   5393  C  CB  . LYS E  1 123 ? 54.571  244.574 61.385  1.00 49.32  ? 122 LYS E CB  1 
ATOM   5394  C  CG  . LYS E  1 123 ? 54.991  243.829 62.644  1.00 47.06  ? 122 LYS E CG  1 
ATOM   5395  C  CD  . LYS E  1 123 ? 56.351  243.097 62.438  1.00 63.86  ? 122 LYS E CD  1 
ATOM   5396  C  CE  . LYS E  1 123 ? 56.344  241.537 62.328  1.00 60.49  ? 122 LYS E CE  1 
ATOM   5397  N  NZ  . LYS E  1 123 ? 56.416  240.944 60.940  1.00 61.05  ? 122 LYS E NZ  1 
ATOM   5398  N  N   . ALA E  1 124 ? 54.463  247.335 60.121  1.00 46.25  ? 123 ALA E N   1 
ATOM   5399  C  CA  . ALA E  1 124 ? 54.609  248.239 59.000  1.00 44.95  ? 123 ALA E CA  1 
ATOM   5400  C  C   . ALA E  1 124 ? 54.819  247.399 57.795  1.00 49.26  ? 123 ALA E C   1 
ATOM   5401  O  O   . ALA E  1 124 ? 55.446  246.338 57.834  1.00 46.49  ? 123 ALA E O   1 
ATOM   5402  C  CB  . ALA E  1 124 ? 55.828  249.160 59.174  1.00 45.90  ? 123 ALA E CB  1 
ATOM   5403  N  N   . ASP E  1 125 ? 54.287  247.903 56.701  1.00 55.25  ? 124 ASP E N   1 
ATOM   5404  C  CA  . ASP E  1 125 ? 54.349  247.238 55.422  1.00 52.26  ? 124 ASP E CA  1 
ATOM   5405  C  C   . ASP E  1 125 ? 55.565  247.866 54.766  1.00 54.09  ? 124 ASP E C   1 
ATOM   5406  O  O   . ASP E  1 125 ? 55.608  249.097 54.535  1.00 46.49  ? 124 ASP E O   1 
ATOM   5407  C  CB  . ASP E  1 125 ? 53.062  247.583 54.641  1.00 54.35  ? 124 ASP E CB  1 
ATOM   5408  C  CG  . ASP E  1 125 ? 53.066  247.048 53.232  1.00 62.90  ? 124 ASP E CG  1 
ATOM   5409  O  OD1 . ASP E  1 125 ? 54.035  246.318 52.884  1.00 62.35  ? 124 ASP E OD1 1 
ATOM   5410  O  OD2 . ASP E  1 125 ? 52.119  247.381 52.470  1.00 60.22  ? 124 ASP E OD2 1 
ATOM   5411  N  N   . ASP E  1 126 ? 56.546  247.012 54.466  1.00 55.89  ? 125 ASP E N   1 
ATOM   5412  C  CA  . ASP E  1 126 ? 57.838  247.465 53.883  1.00 62.15  ? 125 ASP E CA  1 
ATOM   5413  C  C   . ASP E  1 126 ? 57.726  247.930 52.402  1.00 70.98  ? 125 ASP E C   1 
ATOM   5414  O  O   . ASP E  1 126 ? 58.759  248.327 51.758  1.00 66.09  ? 125 ASP E O   1 
ATOM   5415  C  CB  . ASP E  1 126 ? 58.982  246.425 54.090  1.00 60.79  ? 125 ASP E CB  1 
ATOM   5416  C  CG  . ASP E  1 126 ? 58.681  245.024 53.476  1.00 68.59  ? 125 ASP E CG  1 
ATOM   5417  O  OD1 . ASP E  1 126 ? 57.992  244.953 52.401  1.00 69.31  ? 125 ASP E OD1 1 
ATOM   5418  O  OD2 . ASP E  1 126 ? 59.153  243.983 54.077  1.00 61.73  ? 125 ASP E OD2 1 
ATOM   5419  N  N   . LEU E  1 127 ? 56.474  247.878 51.886  1.00 71.18  ? 126 LEU E N   1 
ATOM   5420  C  CA  . LEU E  1 127 ? 56.121  248.224 50.475  1.00 69.27  ? 126 LEU E CA  1 
ATOM   5421  C  C   . LEU E  1 127 ? 56.813  247.204 49.476  1.00 73.47  ? 126 LEU E C   1 
ATOM   5422  O  O   . LEU E  1 127 ? 57.211  247.531 48.315  1.00 66.18  ? 126 LEU E O   1 
ATOM   5423  C  CB  . LEU E  1 127 ? 56.300  249.777 50.197  1.00 58.54  ? 126 LEU E CB  1 
ATOM   5424  C  CG  . LEU E  1 127 ? 55.598  250.671 51.305  1.00 59.21  ? 126 LEU E CG  1 
ATOM   5425  C  CD1 . LEU E  1 127 ? 55.872  252.211 51.250  1.00 48.41  ? 126 LEU E CD1 1 
ATOM   5426  C  CD2 . LEU E  1 127 ? 54.097  250.353 51.471  1.00 51.67  ? 126 LEU E CD2 1 
ATOM   5427  N  N   . GLY E  1 128 ? 56.953  245.955 49.947  1.00 62.81  ? 127 GLY E N   1 
ATOM   5428  C  CA  . GLY E  1 128 ? 57.576  244.920 49.107  1.00 73.41  ? 127 GLY E CA  1 
ATOM   5429  C  C   . GLY E  1 128 ? 59.027  245.167 48.656  1.00 76.16  ? 127 GLY E C   1 
ATOM   5430  O  O   . GLY E  1 128 ? 59.489  244.477 47.732  1.00 66.77  ? 127 GLY E O   1 
ATOM   5431  N  N   . LYS E  1 129 ? 59.719  246.140 49.298  1.00 76.31  ? 128 LYS E N   1 
ATOM   5432  C  CA  . LYS E  1 129 ? 61.157  246.519 49.049  1.00 81.01  ? 128 LYS E CA  1 
ATOM   5433  C  C   . LYS E  1 129 ? 62.153  245.937 50.155  1.00 83.36  ? 128 LYS E C   1 
ATOM   5434  O  O   . LYS E  1 129 ? 63.363  246.315 50.203  1.00 68.78  ? 128 LYS E O   1 
ATOM   5435  C  CB  . LYS E  1 129 ? 61.301  248.064 48.847  1.00 62.26  ? 128 LYS E CB  1 
ATOM   5436  N  N   . GLY E  1 130 ? 61.634  244.997 50.984  1.00 77.54  ? 129 GLY E N   1 
ATOM   5437  C  CA  . GLY E  1 130 ? 62.296  244.479 52.219  1.00 75.15  ? 129 GLY E CA  1 
ATOM   5438  C  C   . GLY E  1 130 ? 63.283  243.329 52.007  1.00 78.47  ? 129 GLY E C   1 
ATOM   5439  O  O   . GLY E  1 130 ? 64.036  242.986 52.958  1.00 70.56  ? 129 GLY E O   1 
ATOM   5440  N  N   . GLY E  1 131 ? 63.264  242.750 50.780  1.00 79.34  ? 130 GLY E N   1 
ATOM   5441  C  CA  . GLY E  1 131 ? 64.345  241.874 50.197  1.00 80.35  ? 130 GLY E CA  1 
ATOM   5442  C  C   . GLY E  1 131 ? 64.359  240.408 50.658  1.00 81.72  ? 130 GLY E C   1 
ATOM   5443  O  O   . GLY E  1 131 ? 65.423  239.881 51.006  1.00 88.12  ? 130 GLY E O   1 
ATOM   5444  N  N   . ASN E  1 132 ? 63.180  239.765 50.673  1.00 76.36  ? 131 ASN E N   1 
ATOM   5445  C  CA  . ASN E  1 132 ? 62.923  238.319 51.049  1.00 69.95  ? 131 ASN E CA  1 
ATOM   5446  C  C   . ASN E  1 132 ? 61.542  237.883 50.457  1.00 72.17  ? 131 ASN E C   1 
ATOM   5447  O  O   . ASN E  1 132 ? 60.575  238.716 50.346  1.00 64.32  ? 131 ASN E O   1 
ATOM   5448  C  CB  . ASN E  1 132 ? 62.937  238.089 52.594  1.00 69.45  ? 131 ASN E CB  1 
ATOM   5449  C  CG  . ASN E  1 132 ? 62.178  239.196 53.385  1.00 76.77  ? 131 ASN E CG  1 
ATOM   5450  O  OD1 . ASN E  1 132 ? 60.924  239.235 53.432  1.00 66.36  ? 131 ASN E OD1 1 
ATOM   5451  N  ND2 . ASN E  1 132 ? 62.951  240.115 54.000  1.00 71.79  ? 131 ASN E ND2 1 
ATOM   5452  N  N   . GLU E  1 133 ? 61.428  236.608 50.062  1.00 72.32  ? 132 GLU E N   1 
ATOM   5453  C  CA  . GLU E  1 133 ? 60.128  236.085 49.585  1.00 77.91  ? 132 GLU E CA  1 
ATOM   5454  C  C   . GLU E  1 133 ? 58.823  236.715 50.217  1.00 76.21  ? 132 GLU E C   1 
ATOM   5455  O  O   . GLU E  1 133 ? 57.931  237.228 49.456  1.00 65.75  ? 132 GLU E O   1 
ATOM   5456  C  CB  . GLU E  1 133 ? 60.084  234.606 49.817  1.00 81.40  ? 132 GLU E CB  1 
ATOM   5457  C  CG  . GLU E  1 133 ? 59.157  233.897 48.849  1.00 75.44  ? 132 GLU E CG  1 
ATOM   5458  C  CD  . GLU E  1 133 ? 59.612  232.457 48.735  1.00 92.65  ? 132 GLU E CD  1 
ATOM   5459  O  OE1 . GLU E  1 133 ? 59.791  231.796 49.841  1.00 65.53  ? 132 GLU E OE1 1 
ATOM   5460  O  OE2 . GLU E  1 133 ? 59.840  232.039 47.546  1.00 81.98  ? 132 GLU E OE2 1 
ATOM   5461  N  N   . GLU E  1 134 ? 58.744  236.693 51.573  1.00 66.86  ? 133 GLU E N   1 
ATOM   5462  C  CA  . GLU E  1 134 ? 57.551  237.167 52.306  1.00 65.11  ? 133 GLU E CA  1 
ATOM   5463  C  C   . GLU E  1 134 ? 57.177  238.656 51.988  1.00 69.95  ? 133 GLU E C   1 
ATOM   5464  O  O   . GLU E  1 134 ? 55.962  239.001 51.918  1.00 62.28  ? 133 GLU E O   1 
ATOM   5465  C  CB  . GLU E  1 134 ? 57.606  236.861 53.821  1.00 62.59  ? 133 GLU E CB  1 
ATOM   5466  C  CG  . GLU E  1 134 ? 56.206  236.998 54.497  1.00 70.90  ? 133 GLU E CG  1 
ATOM   5467  C  CD  . GLU E  1 134 ? 55.176  235.894 54.078  1.00 90.94  ? 133 GLU E CD  1 
ATOM   5468  O  OE1 . GLU E  1 134 ? 55.561  234.664 54.167  1.00 77.50  ? 133 GLU E OE1 1 
ATOM   5469  O  OE2 . GLU E  1 134 ? 53.973  236.230 53.682  1.00 72.35  ? 133 GLU E OE2 1 
ATOM   5470  N  N   . SER E  1 135 ? 58.209  239.495 51.728  1.00 68.15  ? 134 SER E N   1 
ATOM   5471  C  CA  . SER E  1 135 ? 58.062  240.949 51.441  1.00 63.17  ? 134 SER E CA  1 
ATOM   5472  C  C   . SER E  1 135 ? 57.265  241.262 50.132  1.00 69.51  ? 134 SER E C   1 
ATOM   5473  O  O   . SER E  1 135 ? 56.467  242.252 50.072  1.00 65.02  ? 134 SER E O   1 
ATOM   5474  C  CB  . SER E  1 135 ? 59.445  241.649 51.523  1.00 70.47  ? 134 SER E CB  1 
ATOM   5475  O  OG  . SER E  1 135 ? 59.589  242.782 50.655  1.00 69.69  ? 134 SER E OG  1 
ATOM   5476  N  N   . THR E  1 136 ? 57.466  240.399 49.123  1.00 64.29  ? 135 THR E N   1 
ATOM   5477  C  CA  . THR E  1 136 ? 56.761  240.464 47.821  1.00 65.01  ? 135 THR E CA  1 
ATOM   5478  C  C   . THR E  1 136 ? 55.430  239.650 47.822  1.00 74.11  ? 135 THR E C   1 
ATOM   5479  O  O   . THR E  1 136 ? 54.794  239.491 46.728  1.00 68.96  ? 135 THR E O   1 
ATOM   5480  C  CB  . THR E  1 136 ? 57.605  239.833 46.680  1.00 64.15  ? 135 THR E CB  1 
ATOM   5481  O  OG1 . THR E  1 136 ? 57.586  238.386 46.842  1.00 58.85  ? 135 THR E OG1 1 
ATOM   5482  C  CG2 . THR E  1 136 ? 59.104  240.416 46.627  1.00 58.62  ? 135 THR E CG2 1 
ATOM   5483  N  N   . LYS E  1 137 ? 55.046  239.079 48.983  1.00 64.69  ? 136 LYS E N   1 
ATOM   5484  C  CA  . LYS E  1 137 ? 53.653  238.550 49.136  1.00 64.99  ? 136 LYS E CA  1 
ATOM   5485  C  C   . LYS E  1 137 ? 52.754  239.411 50.094  1.00 64.70  ? 136 LYS E C   1 
ATOM   5486  O  O   . LYS E  1 137 ? 51.548  239.522 49.840  1.00 61.49  ? 136 LYS E O   1 
ATOM   5487  C  CB  . LYS E  1 137 ? 53.613  237.084 49.594  1.00 63.74  ? 136 LYS E CB  1 
ATOM   5488  C  CG  . LYS E  1 137 ? 54.619  236.159 48.946  1.00 66.14  ? 136 LYS E CG  1 
ATOM   5489  C  CD  . LYS E  1 137 ? 54.558  234.805 49.666  1.00 69.20  ? 136 LYS E CD  1 
ATOM   5490  C  CE  . LYS E  1 137 ? 55.780  233.966 49.261  1.00 78.13  ? 136 LYS E CE  1 
ATOM   5491  N  NZ  . LYS E  1 137 ? 56.140  232.621 49.877  1.00 67.93  ? 136 LYS E NZ  1 
ATOM   5492  N  N   . THR E  1 138 ? 53.357  240.013 51.146  1.00 56.80  ? 137 THR E N   1 
ATOM   5493  C  CA  . THR E  1 138 ? 52.662  240.595 52.351  1.00 61.10  ? 137 THR E CA  1 
ATOM   5494  C  C   . THR E  1 138 ? 53.279  241.932 52.867  1.00 68.53  ? 137 THR E C   1 
ATOM   5495  O  O   . THR E  1 138 ? 52.696  242.676 53.750  1.00 55.65  ? 137 THR E O   1 
ATOM   5496  C  CB  . THR E  1 138 ? 52.582  239.577 53.579  1.00 70.42  ? 137 THR E CB  1 
ATOM   5497  O  OG1 . THR E  1 138 ? 53.917  239.231 54.110  1.00 64.00  ? 137 THR E OG1 1 
ATOM   5498  C  CG2 . THR E  1 138 ? 51.671  238.294 53.243  1.00 56.67  ? 137 THR E CG2 1 
ATOM   5499  N  N   . GLY E  1 139 ? 54.475  242.222 52.316  1.00 76.90  ? 138 GLY E N   1 
ATOM   5500  C  CA  . GLY E  1 139 ? 55.382  243.264 52.853  1.00 66.43  ? 138 GLY E CA  1 
ATOM   5501  C  C   . GLY E  1 139 ? 55.738  243.050 54.335  1.00 68.71  ? 138 GLY E C   1 
ATOM   5502  O  O   . GLY E  1 139 ? 56.134  244.048 54.966  1.00 64.07  ? 138 GLY E O   1 
ATOM   5503  N  N   . ASN E  1 140 ? 55.597  241.789 54.876  1.00 60.97  ? 139 ASN E N   1 
ATOM   5504  C  CA  . ASN E  1 140 ? 55.741  241.437 56.349  1.00 63.91  ? 139 ASN E CA  1 
ATOM   5505  C  C   . ASN E  1 140 ? 55.021  242.508 57.226  1.00 64.06  ? 139 ASN E C   1 
ATOM   5506  O  O   . ASN E  1 140 ? 55.685  243.351 57.873  1.00 51.13  ? 139 ASN E O   1 
ATOM   5507  C  CB  . ASN E  1 140 ? 57.230  241.295 56.856  1.00 69.07  ? 139 ASN E CB  1 
ATOM   5508  C  CG  . ASN E  1 140 ? 58.177  240.688 55.820  1.00 70.74  ? 139 ASN E CG  1 
ATOM   5509  O  OD1 . ASN E  1 140 ? 58.205  239.442 55.659  1.00 65.86  ? 139 ASN E OD1 1 
ATOM   5510  N  ND2 . ASN E  1 140 ? 58.968  241.561 55.106  1.00 60.92  ? 139 ASN E ND2 1 
ATOM   5511  N  N   . ALA E  1 141 ? 53.679  242.528 57.155  1.00 60.55  ? 140 ALA E N   1 
ATOM   5512  C  CA  . ALA E  1 141 ? 52.856  243.459 57.952  1.00 54.99  ? 140 ALA E CA  1 
ATOM   5513  C  C   . ALA E  1 141 ? 52.318  242.696 59.233  1.00 52.04  ? 140 ALA E C   1 
ATOM   5514  O  O   . ALA E  1 141 ? 51.706  243.281 60.102  1.00 53.97  ? 140 ALA E O   1 
ATOM   5515  C  CB  . ALA E  1 141 ? 51.757  244.134 57.065  1.00 52.35  ? 140 ALA E CB  1 
ATOM   5516  N  N   . GLY E  1 142 ? 52.628  241.406 59.371  1.00 52.03  ? 141 GLY E N   1 
ATOM   5517  C  CA  . GLY E  1 142 ? 52.391  240.691 60.608  1.00 54.39  ? 141 GLY E CA  1 
ATOM   5518  C  C   . GLY E  1 142 ? 50.947  240.234 60.659  1.00 60.37  ? 141 GLY E C   1 
ATOM   5519  O  O   . GLY E  1 142 ? 50.279  240.056 59.599  1.00 58.28  ? 141 GLY E O   1 
ATOM   5520  N  N   . SER E  1 143 ? 50.475  240.072 61.896  1.00 51.32  ? 142 SER E N   1 
ATOM   5521  C  CA  . SER E  1 143 ? 49.161  239.582 62.165  1.00 49.29  ? 142 SER E CA  1 
ATOM   5522  C  C   . SER E  1 143 ? 48.059  240.578 61.736  1.00 47.59  ? 142 SER E C   1 
ATOM   5523  O  O   . SER E  1 143 ? 48.322  241.769 61.527  1.00 44.08  ? 142 SER E O   1 
ATOM   5524  C  CB  . SER E  1 143 ? 49.073  239.248 63.648  1.00 48.06  ? 142 SER E CB  1 
ATOM   5525  O  OG  . SER E  1 143 ? 48.179  240.144 64.306  1.00 49.59  ? 142 SER E OG  1 
ATOM   5526  N  N   . ARG E  1 144 ? 46.831  240.077 61.624  1.00 45.16  ? 143 ARG E N   1 
ATOM   5527  C  CA  . ARG E  1 144 ? 45.730  240.915 61.221  1.00 40.45  ? 143 ARG E CA  1 
ATOM   5528  C  C   . ARG E  1 144 ? 45.060  241.379 62.482  1.00 36.97  ? 143 ARG E C   1 
ATOM   5529  O  O   . ARG E  1 144 ? 44.486  240.609 63.199  1.00 37.86  ? 143 ARG E O   1 
ATOM   5530  C  CB  . ARG E  1 144 ? 44.787  240.093 60.363  1.00 40.46  ? 143 ARG E CB  1 
ATOM   5531  C  CG  . ARG E  1 144 ? 45.428  239.718 59.054  1.00 42.75  ? 143 ARG E CG  1 
ATOM   5532  C  CD  . ARG E  1 144 ? 44.759  238.521 58.438  1.00 38.43  ? 143 ARG E CD  1 
ATOM   5533  N  NE  . ARG E  1 144 ? 45.614  238.054 57.347  1.00 37.90  ? 143 ARG E NE  1 
ATOM   5534  C  CZ  . ARG E  1 144 ? 45.171  237.437 56.264  1.00 39.46  ? 143 ARG E CZ  1 
ATOM   5535  N  NH1 . ARG E  1 144 ? 43.858  237.234 56.049  1.00 43.66  ? 143 ARG E NH1 1 
ATOM   5536  N  NH2 . ARG E  1 144 ? 46.035  237.032 55.366  1.00 38.72  ? 143 ARG E NH2 1 
ATOM   5537  N  N   . LEU E  1 145 ? 45.095  242.667 62.730  1.00 39.63  ? 144 LEU E N   1 
ATOM   5538  C  CA  . LEU E  1 145 ? 44.549  243.227 63.959  1.00 37.93  ? 144 LEU E CA  1 
ATOM   5539  C  C   . LEU E  1 145 ? 43.065  243.445 63.948  1.00 36.55  ? 144 LEU E C   1 
ATOM   5540  O  O   . LEU E  1 145 ? 42.423  243.220 64.941  1.00 34.99  ? 144 LEU E O   1 
ATOM   5541  C  CB  . LEU E  1 145 ? 45.251  244.556 64.207  1.00 38.69  ? 144 LEU E CB  1 
ATOM   5542  C  CG  . LEU E  1 145 ? 46.753  244.428 64.445  1.00 40.48  ? 144 LEU E CG  1 
ATOM   5543  C  CD1 . LEU E  1 145 ? 47.352  245.818 64.597  1.00 42.45  ? 144 LEU E CD1 1 
ATOM   5544  C  CD2 . LEU E  1 145 ? 46.951  243.620 65.740  1.00 35.55  ? 144 LEU E CD2 1 
ATOM   5545  N  N   . ALA E  1 146 ? 42.547  244.009 62.853  1.00 35.52  ? 145 ALA E N   1 
ATOM   5546  C  CA  . ALA E  1 146 ? 41.108  244.275 62.690  1.00 35.76  ? 145 ALA E CA  1 
ATOM   5547  C  C   . ALA E  1 146 ? 40.765  244.312 61.231  1.00 36.23  ? 145 ALA E C   1 
ATOM   5548  O  O   . ALA E  1 146 ? 41.609  244.593 60.367  1.00 33.61  ? 145 ALA E O   1 
ATOM   5549  C  CB  . ALA E  1 146 ? 40.649  245.555 63.368  1.00 32.52  ? 145 ALA E CB  1 
ATOM   5550  N  N   . CYS E  1 147 ? 39.518  243.958 60.950  1.00 37.36  ? 146 CYS E N   1 
ATOM   5551  C  CA  . CYS E  1 147 ? 39.062  243.943 59.580  1.00 33.56  ? 146 CYS E CA  1 
ATOM   5552  C  C   . CYS E  1 147 ? 37.609  244.157 59.538  1.00 32.23  ? 146 CYS E C   1 
ATOM   5553  O  O   . CYS E  1 147 ? 36.952  244.097 60.556  1.00 30.48  ? 146 CYS E O   1 
ATOM   5554  C  CB  . CYS E  1 147 ? 39.401  242.581 58.945  1.00 34.53  ? 146 CYS E CB  1 
ATOM   5555  S  SG  . CYS E  1 147 ? 38.804  241.160 59.851  1.00 33.55  ? 146 CYS E SG  1 
ATOM   5556  N  N   . GLY E  1 148 ? 37.121  244.372 58.322  1.00 34.24  ? 147 GLY E N   1 
ATOM   5557  C  CA  . GLY E  1 148 ? 35.731  244.322 58.023  1.00 30.81  ? 147 GLY E CA  1 
ATOM   5558  C  C   . GLY E  1 148 ? 35.464  244.296 56.542  1.00 34.50  ? 147 GLY E C   1 
ATOM   5559  O  O   . GLY E  1 148 ? 36.313  244.607 55.699  1.00 32.04  ? 147 GLY E O   1 
ATOM   5560  N  N   . VAL E  1 149 ? 34.225  243.947 56.244  1.00 33.59  ? 148 VAL E N   1 
ATOM   5561  C  CA  . VAL E  1 149 ? 33.789  243.847 54.907  1.00 32.32  ? 148 VAL E CA  1 
ATOM   5562  C  C   . VAL E  1 149 ? 33.356  245.210 54.450  1.00 31.67  ? 148 VAL E C   1 
ATOM   5563  O  O   . VAL E  1 149 ? 32.748  245.942 55.201  1.00 28.73  ? 148 VAL E O   1 
ATOM   5564  C  CB  . VAL E  1 149 ? 32.648  242.864 54.773  1.00 32.24  ? 148 VAL E CB  1 
ATOM   5565  C  CG1 . VAL E  1 149 ? 32.329  242.677 53.282  1.00 31.32  ? 148 VAL E CG1 1 
ATOM   5566  C  CG2 . VAL E  1 149 ? 33.046  241.557 55.431  1.00 29.03  ? 148 VAL E CG2 1 
ATOM   5567  N  N   . ILE E  1 150 ? 33.684  245.518 53.202  1.00 32.33  ? 149 ILE E N   1 
ATOM   5568  C  CA  . ILE E  1 150 ? 33.462  246.822 52.634  1.00 31.58  ? 149 ILE E CA  1 
ATOM   5569  C  C   . ILE E  1 150 ? 32.059  246.779 52.095  1.00 31.02  ? 149 ILE E C   1 
ATOM   5570  O  O   . ILE E  1 150 ? 31.783  246.027 51.211  1.00 33.70  ? 149 ILE E O   1 
ATOM   5571  C  CB  . ILE E  1 150 ? 34.480  247.130 51.536  1.00 31.74  ? 149 ILE E CB  1 
ATOM   5572  C  CG1 . ILE E  1 150 ? 35.879  247.127 52.122  1.00 33.84  ? 149 ILE E CG1 1 
ATOM   5573  C  CG2 . ILE E  1 150 ? 34.201  248.498 50.921  1.00 31.74  ? 149 ILE E CG2 1 
ATOM   5574  C  CD1 . ILE E  1 150 ? 37.012  247.280 51.104  1.00 31.89  ? 149 ILE E CD1 1 
ATOM   5575  N  N   . GLY E  1 151 ? 31.176  247.573 52.689  1.00 34.39  ? 150 GLY E N   1 
ATOM   5576  C  CA  . GLY E  1 151 ? 29.792  247.699 52.305  1.00 31.91  ? 150 GLY E CA  1 
ATOM   5577  C  C   . GLY E  1 151 ? 29.432  248.952 51.527  1.00 32.60  ? 150 GLY E C   1 
ATOM   5578  O  O   . GLY E  1 151 ? 30.084  249.979 51.653  1.00 32.37  ? 150 GLY E O   1 
ATOM   5579  N  N   . ILE E  1 152 ? 28.366  248.869 50.734  1.00 34.69  ? 151 ILE E N   1 
ATOM   5580  C  CA  . ILE E  1 152 ? 27.822  249.980 49.974  1.00 34.71  ? 151 ILE E CA  1 
ATOM   5581  C  C   . ILE E  1 152 ? 27.229  250.975 50.951  1.00 34.17  ? 151 ILE E C   1 
ATOM   5582  O  O   . ILE E  1 152 ? 26.479  250.554 51.817  1.00 31.26  ? 151 ILE E O   1 
ATOM   5583  C  CB  . ILE E  1 152 ? 26.733  249.457 49.048  1.00 36.48  ? 151 ILE E CB  1 
ATOM   5584  C  CG1 . ILE E  1 152 ? 27.398  248.708 47.900  1.00 41.61  ? 151 ILE E CG1 1 
ATOM   5585  C  CG2 . ILE E  1 152 ? 25.988  250.589 48.410  1.00 32.02  ? 151 ILE E CG2 1 
ATOM   5586  C  CD1 . ILE E  1 152 ? 26.551  247.599 47.329  1.00 40.75  ? 151 ILE E CD1 1 
ATOM   5587  N  N   . ALA E  1 153 ? 27.566  252.262 50.816  1.00 29.52  ? 152 ALA E N   1 
ATOM   5588  C  CA  . ALA E  1 153 ? 27.028  253.237 51.728  1.00 33.11  ? 152 ALA E CA  1 
ATOM   5589  C  C   . ALA E  1 153 ? 26.115  254.307 51.081  1.00 34.34  ? 152 ALA E C   1 
ATOM   5590  O  O   . ALA E  1 153 ? 26.063  254.459 49.859  1.00 35.34  ? 152 ALA E O   1 
ATOM   5591  C  CB  . ALA E  1 153 ? 28.131  253.846 52.617  1.00 32.03  ? 152 ALA E CB  1 
ATOM   5592  N  N   . GLN E  1 154 ? 25.335  254.964 51.927  1.00 33.81  ? 153 GLN E N   1 
ATOM   5593  C  CA  . GLN E  1 154 ? 24.399  255.972 51.506  1.00 41.28  ? 153 GLN E CA  1 
ATOM   5594  C  C   . GLN E  1 154 ? 25.092  257.335 51.365  1.00 53.23  ? 153 GLN E C   1 
ATOM   5595  O  O   . GLN E  1 154 ? 25.793  257.833 52.321  1.00 45.10  ? 153 GLN E O   1 
ATOM   5596  C  CB  . GLN E  1 154 ? 23.265  256.121 52.515  1.00 40.86  ? 153 GLN E CB  1 
ATOM   5597  C  CG  . GLN E  1 154 ? 22.308  257.222 52.069  1.00 46.49  ? 153 GLN E CG  1 
ATOM   5598  C  CD  . GLN E  1 154 ? 20.952  257.269 52.834  1.00 56.04  ? 153 GLN E CD  1 
ATOM   5599  O  OE1 . GLN E  1 154 ? 20.903  257.383 54.083  1.00 53.49  ? 153 GLN E OE1 1 
ATOM   5600  N  NE2 . GLN E  1 154 ? 19.840  257.198 52.071  1.00 48.19  ? 153 GLN E NE2 1 
ATOM   5601  O  OXT . GLN E  1 154 ? 24.890  257.942 50.277  1.00 55.42  ? 153 GLN E OXT 1 
ATOM   5602  N  N   . MET F  1 1   ? 31.284  237.767 38.157  1.00 54.75  ? 0   MET F N   1 
ATOM   5603  C  CA  . MET F  1 1   ? 32.649  237.406 38.728  1.00 59.63  ? 0   MET F CA  1 
ATOM   5604  C  C   . MET F  1 1   ? 32.400  236.393 39.913  1.00 70.16  ? 0   MET F C   1 
ATOM   5605  O  O   . MET F  1 1   ? 32.955  235.245 39.898  1.00 61.66  ? 0   MET F O   1 
ATOM   5606  C  CB  . MET F  1 1   ? 33.502  238.674 39.145  1.00 52.38  ? 0   MET F CB  1 
ATOM   5607  N  N   . ALA F  1 2   ? 31.531  236.779 40.889  1.00 60.93  ? 1   ALA F N   1 
ATOM   5608  C  CA  . ALA F  1 2   ? 31.266  235.991 42.162  1.00 48.00  ? 1   ALA F CA  1 
ATOM   5609  C  C   . ALA F  1 2   ? 30.330  234.820 42.009  1.00 43.03  ? 1   ALA F C   1 
ATOM   5610  O  O   . ALA F  1 2   ? 29.295  234.999 41.419  1.00 38.88  ? 1   ALA F O   1 
ATOM   5611  C  CB  . ALA F  1 2   ? 30.680  236.907 43.214  1.00 54.25  ? 1   ALA F CB  1 
ATOM   5612  N  N   . THR F  1 3   ? 30.681  233.627 42.549  1.00 43.56  ? 2   THR F N   1 
ATOM   5613  C  CA  . THR F  1 3   ? 29.738  232.521 42.574  1.00 37.98  ? 2   THR F CA  1 
ATOM   5614  C  C   . THR F  1 3   ? 29.368  232.114 44.026  1.00 37.38  ? 2   THR F C   1 
ATOM   5615  O  O   . THR F  1 3   ? 28.424  231.365 44.244  1.00 41.68  ? 2   THR F O   1 
ATOM   5616  C  CB  . THR F  1 3   ? 30.212  231.326 41.682  1.00 43.44  ? 2   THR F CB  1 
ATOM   5617  O  OG1 . THR F  1 3   ? 31.434  230.799 42.181  1.00 44.31  ? 2   THR F OG1 1 
ATOM   5618  C  CG2 . THR F  1 3   ? 30.425  231.718 40.207  1.00 39.44  ? 2   THR F CG2 1 
ATOM   5619  N  N   . LYS F  1 4   ? 30.103  232.605 45.013  1.00 34.73  ? 3   LYS F N   1 
ATOM   5620  C  CA  . LYS F  1 4   ? 29.885  232.279 46.400  1.00 34.79  ? 3   LYS F CA  1 
ATOM   5621  C  C   . LYS F  1 4   ? 29.966  233.575 47.242  1.00 36.04  ? 3   LYS F C   1 
ATOM   5622  O  O   . LYS F  1 4   ? 30.815  234.435 46.982  1.00 34.00  ? 3   LYS F O   1 
ATOM   5623  C  CB  . LYS F  1 4   ? 30.908  231.267 46.907  1.00 38.20  ? 3   LYS F CB  1 
ATOM   5624  C  CG  . LYS F  1 4   ? 30.797  229.884 46.277  1.00 45.44  ? 3   LYS F CG  1 
ATOM   5625  C  CD  . LYS F  1 4   ? 31.778  228.880 46.916  1.00 47.47  ? 3   LYS F CD  1 
ATOM   5626  C  CE  . LYS F  1 4   ? 31.122  228.204 48.127  1.00 52.67  ? 3   LYS F CE  1 
ATOM   5627  N  NZ  . LYS F  1 4   ? 32.115  227.734 49.152  1.00 49.56  ? 3   LYS F NZ  1 
ATOM   5628  N  N   . ALA F  1 5   ? 29.054  233.721 48.217  1.00 30.12  ? 4   ALA F N   1 
ATOM   5629  C  CA  . ALA F  1 5   ? 29.158  234.794 49.129  1.00 30.23  ? 4   ALA F CA  1 
ATOM   5630  C  C   . ALA F  1 5   ? 28.893  234.227 50.495  1.00 29.82  ? 4   ALA F C   1 
ATOM   5631  O  O   . ALA F  1 5   ? 28.443  233.124 50.624  1.00 30.21  ? 4   ALA F O   1 
ATOM   5632  C  CB  . ALA F  1 5   ? 28.181  235.914 48.753  1.00 27.58  ? 4   ALA F CB  1 
ATOM   5633  N  N   . VAL F  1 6   ? 29.178  235.014 51.512  1.00 30.44  ? 5   VAL F N   1 
ATOM   5634  C  CA  . VAL F  1 6   ? 29.065  234.597 52.875  1.00 30.73  ? 5   VAL F CA  1 
ATOM   5635  C  C   . VAL F  1 6   ? 28.706  235.778 53.770  1.00 30.36  ? 5   VAL F C   1 
ATOM   5636  O  O   . VAL F  1 6   ? 29.068  236.900 53.496  1.00 27.37  ? 5   VAL F O   1 
ATOM   5637  C  CB  . VAL F  1 6   ? 30.310  233.818 53.341  1.00 32.12  ? 5   VAL F CB  1 
ATOM   5638  C  CG1 . VAL F  1 6   ? 31.500  234.711 53.547  1.00 26.19  ? 5   VAL F CG1 1 
ATOM   5639  C  CG2 . VAL F  1 6   ? 30.016  233.091 54.624  1.00 32.96  ? 5   VAL F CG2 1 
ATOM   5640  N  N   . CYS F  1 7   ? 27.948  235.512 54.824  1.00 31.12  ? 6   CYS F N   1 
ATOM   5641  C  CA  . CYS F  1 7   ? 27.574  236.556 55.745  1.00 31.83  ? 6   CYS F CA  1 
ATOM   5642  C  C   . CYS F  1 7   ? 27.636  236.071 57.208  1.00 32.38  ? 6   CYS F C   1 
ATOM   5643  O  O   . CYS F  1 7   ? 27.040  235.009 57.569  1.00 32.55  ? 6   CYS F O   1 
ATOM   5644  C  CB  . CYS F  1 7   ? 26.173  237.002 55.416  1.00 30.48  ? 6   CYS F CB  1 
ATOM   5645  S  SG  . CYS F  1 7   ? 25.710  238.442 56.357  1.00 29.46  ? 6   CYS F SG  1 
ATOM   5646  N  N   . VAL F  1 8   ? 28.320  236.852 58.046  1.00 29.60  ? 7   VAL F N   1 
ATOM   5647  C  CA  . VAL F  1 8   ? 28.376  236.545 59.478  1.00 29.37  ? 7   VAL F CA  1 
ATOM   5648  C  C   . VAL F  1 8   ? 27.390  237.424 60.192  1.00 30.41  ? 7   VAL F C   1 
ATOM   5649  O  O   . VAL F  1 8   ? 27.522  238.638 60.194  1.00 30.07  ? 7   VAL F O   1 
ATOM   5650  C  CB  . VAL F  1 8   ? 29.796  236.744 60.042  1.00 29.90  ? 7   VAL F CB  1 
ATOM   5651  C  CG1 . VAL F  1 8   ? 29.843  236.573 61.572  1.00 23.55  ? 7   VAL F CG1 1 
ATOM   5652  C  CG2 . VAL F  1 8   ? 30.773  235.819 59.316  1.00 26.26  ? 7   VAL F CG2 1 
ATOM   5653  N  N   . LEU F  1 9   ? 26.367  236.832 60.792  1.00 34.46  ? 8   LEU F N   1 
ATOM   5654  C  CA  . LEU F  1 9   ? 25.303  237.660 61.433  1.00 34.99  ? 8   LEU F CA  1 
ATOM   5655  C  C   . LEU F  1 9   ? 25.605  237.893 62.902  1.00 33.94  ? 8   LEU F C   1 
ATOM   5656  O  O   . LEU F  1 9   ? 25.842  236.938 63.654  1.00 33.88  ? 8   LEU F O   1 
ATOM   5657  C  CB  . LEU F  1 9   ? 23.925  237.033 61.251  1.00 34.55  ? 8   LEU F CB  1 
ATOM   5658  C  CG  . LEU F  1 9   ? 23.407  236.945 59.812  1.00 38.17  ? 8   LEU F CG  1 
ATOM   5659  C  CD1 . LEU F  1 9   ? 22.459  235.784 59.731  1.00 43.31  ? 8   LEU F CD1 1 
ATOM   5660  C  CD2 . LEU F  1 9   ? 22.579  238.126 59.462  1.00 35.47  ? 8   LEU F CD2 1 
ATOM   5661  N  N   . LYS F  1 10  ? 25.605  239.158 63.299  1.00 34.51  ? 9   LYS F N   1 
ATOM   5662  C  CA  . LYS F  1 10  ? 25.916  239.551 64.654  1.00 35.91  ? 9   LYS F CA  1 
ATOM   5663  C  C   . LYS F  1 10  ? 24.961  240.583 65.124  1.00 33.88  ? 9   LYS F C   1 
ATOM   5664  O  O   . LYS F  1 10  ? 24.531  241.429 64.373  1.00 30.93  ? 9   LYS F O   1 
ATOM   5665  C  CB  . LYS F  1 10  ? 27.367  240.041 64.798  1.00 38.74  ? 9   LYS F CB  1 
ATOM   5666  C  CG  . LYS F  1 10  ? 28.119  239.099 65.718  1.00 50.46  ? 9   LYS F CG  1 
ATOM   5667  C  CD  . LYS F  1 10  ? 29.615  238.909 65.360  1.00 63.00  ? 9   LYS F CD  1 
ATOM   5668  C  CE  . LYS F  1 10  ? 30.202  237.516 65.777  1.00 63.89  ? 9   LYS F CE  1 
ATOM   5669  N  NZ  . LYS F  1 10  ? 31.343  237.025 64.893  1.00 51.41  ? 9   LYS F NZ  1 
ATOM   5670  N  N   . GLY F  1 11  ? 24.607  240.486 66.390  1.00 34.65  ? 10  GLY F N   1 
ATOM   5671  C  CA  . GLY F  1 11  ? 23.851  241.539 67.006  1.00 37.69  ? 10  GLY F CA  1 
ATOM   5672  C  C   . GLY F  1 11  ? 24.241  241.839 68.422  1.00 37.79  ? 10  GLY F C   1 
ATOM   5673  O  O   . GLY F  1 11  ? 25.194  241.260 68.956  1.00 41.88  ? 10  GLY F O   1 
ATOM   5674  N  N   . ASP F  1 12  ? 23.445  242.701 69.048  1.00 41.54  ? 11  ASP F N   1 
ATOM   5675  C  CA  . ASP F  1 12  ? 23.480  242.932 70.543  1.00 45.78  ? 11  ASP F CA  1 
ATOM   5676  C  C   . ASP F  1 12  ? 23.169  241.740 71.412  1.00 46.07  ? 11  ASP F C   1 
ATOM   5677  O  O   . ASP F  1 12  ? 23.865  241.486 72.422  1.00 53.07  ? 11  ASP F O   1 
ATOM   5678  C  CB  . ASP F  1 12  ? 22.566  244.090 70.928  1.00 47.37  ? 11  ASP F CB  1 
ATOM   5679  C  CG  . ASP F  1 12  ? 23.125  245.447 70.409  1.00 60.24  ? 11  ASP F CG  1 
ATOM   5680  O  OD1 . ASP F  1 12  ? 24.353  245.489 70.106  1.00 52.94  ? 11  ASP F OD1 1 
ATOM   5681  O  OD2 . ASP F  1 12  ? 22.381  246.458 70.329  1.00 60.57  ? 11  ASP F OD2 1 
ATOM   5682  N  N   . GLY F  1 13  ? 22.163  240.973 71.013  1.00 42.76  ? 12  GLY F N   1 
ATOM   5683  C  CA  . GLY F  1 13  ? 21.668  239.904 71.880  1.00 40.70  ? 12  GLY F CA  1 
ATOM   5684  C  C   . GLY F  1 13  ? 22.427  238.662 71.502  1.00 37.86  ? 12  GLY F C   1 
ATOM   5685  O  O   . GLY F  1 13  ? 23.456  238.774 70.864  1.00 39.20  ? 12  GLY F O   1 
ATOM   5686  N  N   . PRO F  1 14  ? 21.852  237.478 71.800  1.00 39.64  ? 13  PRO F N   1 
ATOM   5687  C  CA  . PRO F  1 14  ? 22.446  236.159 71.456  1.00 36.23  ? 13  PRO F CA  1 
ATOM   5688  C  C   . PRO F  1 14  ? 22.292  235.704 69.968  1.00 34.65  ? 13  PRO F C   1 
ATOM   5689  O  O   . PRO F  1 14  ? 22.666  234.582 69.665  1.00 39.05  ? 13  PRO F O   1 
ATOM   5690  C  CB  . PRO F  1 14  ? 21.657  235.204 72.355  1.00 32.74  ? 13  PRO F CB  1 
ATOM   5691  C  CG  . PRO F  1 14  ? 20.269  235.864 72.355  1.00 34.31  ? 13  PRO F CG  1 
ATOM   5692  C  CD  . PRO F  1 14  ? 20.478  237.352 72.371  1.00 30.71  ? 13  PRO F CD  1 
ATOM   5693  N  N   . VAL F  1 15  ? 21.728  236.504 69.068  1.00 33.41  ? 14  VAL F N   1 
ATOM   5694  C  CA  . VAL F  1 15  ? 21.453  235.981 67.726  1.00 33.94  ? 14  VAL F CA  1 
ATOM   5695  C  C   . VAL F  1 15  ? 22.720  236.032 66.950  1.00 34.29  ? 14  VAL F C   1 
ATOM   5696  O  O   . VAL F  1 15  ? 23.356  237.082 66.903  1.00 32.22  ? 14  VAL F O   1 
ATOM   5697  C  CB  . VAL F  1 15  ? 20.303  236.670 66.955  1.00 33.04  ? 14  VAL F CB  1 
ATOM   5698  C  CG1 . VAL F  1 15  ? 20.134  236.031 65.588  1.00 27.28  ? 14  VAL F CG1 1 
ATOM   5699  C  CG2 . VAL F  1 15  ? 19.003  236.564 67.743  1.00 29.39  ? 14  VAL F CG2 1 
ATOM   5700  N  N   . GLN F  1 16  ? 23.106  234.884 66.381  1.00 34.01  ? 15  GLN F N   1 
ATOM   5701  C  CA  . GLN F  1 16  ? 24.267  234.867 65.531  1.00 34.71  ? 15  GLN F CA  1 
ATOM   5702  C  C   . GLN F  1 16  ? 24.218  233.720 64.598  1.00 34.49  ? 15  GLN F C   1 
ATOM   5703  O  O   . GLN F  1 16  ? 23.566  232.702 64.873  1.00 37.38  ? 15  GLN F O   1 
ATOM   5704  C  CB  . GLN F  1 16  ? 25.527  234.787 66.382  1.00 35.92  ? 15  GLN F CB  1 
ATOM   5705  C  CG  . GLN F  1 16  ? 25.410  233.719 67.394  1.00 45.31  ? 15  GLN F CG  1 
ATOM   5706  C  CD  . GLN F  1 16  ? 26.747  233.222 67.806  1.00 54.78  ? 15  GLN F CD  1 
ATOM   5707  O  OE1 . GLN F  1 16  ? 27.448  233.853 68.618  1.00 48.15  ? 15  GLN F OE1 1 
ATOM   5708  N  NE2 . GLN F  1 16  ? 27.151  232.091 67.196  1.00 59.77  ? 15  GLN F NE2 1 
ATOM   5709  N  N   . GLY F  1 17  ? 24.950  233.862 63.507  1.00 33.49  ? 16  GLY F N   1 
ATOM   5710  C  CA  . GLY F  1 17  ? 25.216  232.738 62.628  1.00 32.64  ? 16  GLY F CA  1 
ATOM   5711  C  C   . GLY F  1 17  ? 25.916  233.066 61.336  1.00 30.57  ? 16  GLY F C   1 
ATOM   5712  O  O   . GLY F  1 17  ? 26.493  234.080 61.216  1.00 32.88  ? 16  GLY F O   1 
ATOM   5713  N  N   . ILE F  1 18  ? 25.838  232.167 60.376  1.00 32.29  ? 17  ILE F N   1 
ATOM   5714  C  CA  . ILE F  1 18  ? 26.612  232.192 59.161  1.00 30.54  ? 17  ILE F CA  1 
ATOM   5715  C  C   . ILE F  1 18  ? 25.699  231.727 58.010  1.00 30.47  ? 17  ILE F C   1 
ATOM   5716  O  O   . ILE F  1 18  ? 25.159  230.626 58.017  1.00 28.22  ? 17  ILE F O   1 
ATOM   5717  C  CB  . ILE F  1 18  ? 27.844  231.256 59.280  1.00 32.76  ? 17  ILE F CB  1 
ATOM   5718  C  CG1 . ILE F  1 18  ? 28.853  231.826 60.292  1.00 30.57  ? 17  ILE F CG1 1 
ATOM   5719  C  CG2 . ILE F  1 18  ? 28.483  231.106 57.909  1.00 31.71  ? 17  ILE F CG2 1 
ATOM   5720  C  CD1 . ILE F  1 18  ? 29.902  230.820 60.776  1.00 33.47  ? 17  ILE F CD1 1 
ATOM   5721  N  N   . ILE F  1 19  ? 25.535  232.602 57.033  1.00 31.34  ? 18  ILE F N   1 
ATOM   5722  C  CA  . ILE F  1 19  ? 24.727  232.332 55.883  1.00 29.29  ? 18  ILE F CA  1 
ATOM   5723  C  C   . ILE F  1 19  ? 25.598  232.346 54.669  1.00 30.96  ? 18  ILE F C   1 
ATOM   5724  O  O   . ILE F  1 19  ? 26.373  233.274 54.486  1.00 29.42  ? 18  ILE F O   1 
ATOM   5725  C  CB  . ILE F  1 19  ? 23.573  233.367 55.698  1.00 27.86  ? 18  ILE F CB  1 
ATOM   5726  C  CG1 . ILE F  1 19  ? 22.593  233.326 56.909  1.00 27.69  ? 18  ILE F CG1 1 
ATOM   5727  C  CG2 . ILE F  1 19  ? 22.836  233.081 54.372  1.00 24.41  ? 18  ILE F CG2 1 
ATOM   5728  C  CD1 . ILE F  1 19  ? 21.949  231.978 57.182  1.00 25.95  ? 18  ILE F CD1 1 
ATOM   5729  N  N   . ASN F  1 20  ? 25.430  231.325 53.834  1.00 33.68  ? 19  ASN F N   1 
ATOM   5730  C  CA  . ASN F  1 20  ? 26.155  231.202 52.588  1.00 29.90  ? 19  ASN F CA  1 
ATOM   5731  C  C   . ASN F  1 20  ? 25.258  231.460 51.449  1.00 31.35  ? 19  ASN F C   1 
ATOM   5732  O  O   . ASN F  1 20  ? 24.062  231.166 51.486  1.00 30.39  ? 19  ASN F O   1 
ATOM   5733  C  CB  . ASN F  1 20  ? 26.757  229.819 52.419  1.00 31.10  ? 19  ASN F CB  1 
ATOM   5734  C  CG  . ASN F  1 20  ? 27.588  229.378 53.636  1.00 33.64  ? 19  ASN F CG  1 
ATOM   5735  O  OD1 . ASN F  1 20  ? 27.140  228.535 54.420  1.00 33.93  ? 19  ASN F OD1 1 
ATOM   5736  N  ND2 . ASN F  1 20  ? 28.782  229.915 53.784  1.00 31.34  ? 19  ASN F ND2 1 
ATOM   5737  N  N   . PHE F  1 21  ? 25.861  232.024 50.402  1.00 34.98  ? 20  PHE F N   1 
ATOM   5738  C  CA  . PHE F  1 21  ? 25.205  232.215 49.127  1.00 33.22  ? 20  PHE F CA  1 
ATOM   5739  C  C   . PHE F  1 21  ? 25.951  231.533 48.005  1.00 37.46  ? 20  PHE F C   1 
ATOM   5740  O  O   . PHE F  1 21  ? 27.193  231.506 47.979  1.00 39.75  ? 20  PHE F O   1 
ATOM   5741  C  CB  . PHE F  1 21  ? 25.056  233.673 48.814  1.00 31.38  ? 20  PHE F CB  1 
ATOM   5742  C  CG  . PHE F  1 21  ? 24.334  234.452 49.873  1.00 32.68  ? 20  PHE F CG  1 
ATOM   5743  C  CD1 . PHE F  1 21  ? 24.963  234.820 51.059  1.00 29.93  ? 20  PHE F CD1 1 
ATOM   5744  C  CD2 . PHE F  1 21  ? 23.028  234.846 49.670  1.00 33.09  ? 20  PHE F CD2 1 
ATOM   5745  C  CE1 . PHE F  1 21  ? 24.289  235.569 51.980  1.00 34.31  ? 20  PHE F CE1 1 
ATOM   5746  C  CE2 . PHE F  1 21  ? 22.338  235.575 50.604  1.00 32.69  ? 20  PHE F CE2 1 
ATOM   5747  C  CZ  . PHE F  1 21  ? 22.970  235.968 51.756  1.00 33.94  ? 20  PHE F CZ  1 
ATOM   5748  N  N   . GLU F  1 22  ? 25.188  230.966 47.093  1.00 37.72  ? 21  GLU F N   1 
ATOM   5749  C  CA  . GLU F  1 22  ? 25.715  230.256 45.969  1.00 36.54  ? 21  GLU F CA  1 
ATOM   5750  C  C   . GLU F  1 22  ? 24.947  230.524 44.735  1.00 34.36  ? 21  GLU F C   1 
ATOM   5751  O  O   . GLU F  1 22  ? 23.777  230.371 44.715  1.00 33.27  ? 21  GLU F O   1 
ATOM   5752  C  CB  . GLU F  1 22  ? 25.617  228.787 46.231  1.00 43.97  ? 21  GLU F CB  1 
ATOM   5753  C  CG  . GLU F  1 22  ? 26.938  228.113 46.431  1.00 60.02  ? 21  GLU F CG  1 
ATOM   5754  C  CD  . GLU F  1 22  ? 26.808  226.818 47.179  1.00 67.21  ? 21  GLU F CD  1 
ATOM   5755  O  OE1 . GLU F  1 22  ? 26.832  225.772 46.523  1.00 62.51  ? 21  GLU F OE1 1 
ATOM   5756  O  OE2 . GLU F  1 22  ? 26.681  226.849 48.408  1.00 53.43  ? 21  GLU F OE2 1 
ATOM   5757  N  N   . GLN F  1 23  ? 25.644  230.893 43.687  1.00 31.76  ? 22  GLN F N   1 
ATOM   5758  C  CA  . GLN F  1 23  ? 25.048  231.156 42.407  1.00 34.47  ? 22  GLN F CA  1 
ATOM   5759  C  C   . GLN F  1 23  ? 25.981  230.657 41.339  1.00 35.39  ? 22  GLN F C   1 
ATOM   5760  O  O   . GLN F  1 23  ? 26.899  231.323 40.994  1.00 38.27  ? 22  GLN F O   1 
ATOM   5761  C  CB  . GLN F  1 23  ? 24.795  232.638 42.221  1.00 33.82  ? 22  GLN F CB  1 
ATOM   5762  C  CG  . GLN F  1 23  ? 23.872  232.947 41.077  1.00 33.19  ? 22  GLN F CG  1 
ATOM   5763  C  CD  . GLN F  1 23  ? 23.736  234.398 40.795  1.00 32.69  ? 22  GLN F CD  1 
ATOM   5764  O  OE1 . GLN F  1 23  ? 24.661  235.137 40.930  1.00 36.51  ? 22  GLN F OE1 1 
ATOM   5765  N  NE2 . GLN F  1 23  ? 22.579  234.799 40.391  1.00 29.20  ? 22  GLN F NE2 1 
ATOM   5766  N  N   . LYS F  1 24  ? 25.732  229.485 40.794  1.00 38.30  ? 23  LYS F N   1 
ATOM   5767  C  CA  . LYS F  1 24  ? 26.636  228.947 39.794  1.00 42.88  ? 23  LYS F CA  1 
ATOM   5768  C  C   . LYS F  1 24  ? 26.577  229.584 38.426  1.00 46.10  ? 23  LYS F C   1 
ATOM   5769  O  O   . LYS F  1 24  ? 27.541  229.610 37.724  1.00 49.50  ? 23  LYS F O   1 
ATOM   5770  C  CB  . LYS F  1 24  ? 26.631  227.417 39.735  1.00 30.00  ? 23  LYS F CB  1 
ATOM   5771  C  CG  . LYS F  1 24  ? 25.326  226.722 39.418  1.00 30.00  ? 23  LYS F CG  1 
ATOM   5772  C  CD  . LYS F  1 24  ? 25.224  225.394 40.176  1.00 30.00  ? 23  LYS F CD  1 
ATOM   5773  C  CE  . LYS F  1 24  ? 24.184  224.442 39.598  1.00 30.00  ? 23  LYS F CE  1 
ATOM   5774  N  NZ  . LYS F  1 24  ? 23.067  224.109 40.534  1.00 30.00  ? 23  LYS F NZ  1 
ATOM   5775  N  N   . GLU F  1 25  ? 25.449  230.127 38.060  1.00 44.99  ? 24  GLU F N   1 
ATOM   5776  C  CA  . GLU F  1 25  ? 25.345  230.777 36.795  1.00 48.43  ? 24  GLU F CA  1 
ATOM   5777  C  C   . GLU F  1 25  ? 24.839  232.169 37.051  1.00 45.24  ? 24  GLU F C   1 
ATOM   5778  O  O   . GLU F  1 25  ? 24.077  232.375 37.917  1.00 45.15  ? 24  GLU F O   1 
ATOM   5779  C  CB  . GLU F  1 25  ? 24.379  230.021 35.897  1.00 49.89  ? 24  GLU F CB  1 
ATOM   5780  C  CG  . GLU F  1 25  ? 24.721  228.573 35.634  1.00 57.67  ? 24  GLU F CG  1 
ATOM   5781  C  CD  . GLU F  1 25  ? 25.933  228.377 34.740  1.00 76.05  ? 24  GLU F CD  1 
ATOM   5782  O  OE1 . GLU F  1 25  ? 26.086  229.115 33.760  1.00 70.08  ? 24  GLU F OE1 1 
ATOM   5783  O  OE2 . GLU F  1 25  ? 26.743  227.476 35.011  1.00 69.28  ? 24  GLU F OE2 1 
ATOM   5784  N  N   . SER F  1 26  ? 25.212  233.134 36.245  1.00 46.45  ? 25  SER F N   1 
ATOM   5785  C  CA  . SER F  1 26  ? 24.761  234.502 36.444  1.00 53.67  ? 25  SER F CA  1 
ATOM   5786  C  C   . SER F  1 26  ? 23.253  234.719 36.255  1.00 56.54  ? 25  SER F C   1 
ATOM   5787  O  O   . SER F  1 26  ? 22.651  235.587 36.856  1.00 53.56  ? 25  SER F O   1 
ATOM   5788  C  CB  . SER F  1 26  ? 25.562  235.440 35.557  1.00 50.42  ? 25  SER F CB  1 
ATOM   5789  O  OG  . SER F  1 26  ? 24.817  235.816 34.434  1.00 48.85  ? 25  SER F OG  1 
ATOM   5790  N  N   . ASN F  1 27  ? 22.655  233.887 35.425  1.00 55.17  ? 26  ASN F N   1 
ATOM   5791  C  CA  . ASN F  1 27  ? 21.253  233.873 35.134  1.00 63.98  ? 26  ASN F CA  1 
ATOM   5792  C  C   . ASN F  1 27  ? 20.521  232.880 36.007  1.00 61.41  ? 26  ASN F C   1 
ATOM   5793  O  O   . ASN F  1 27  ? 19.482  232.402 35.626  1.00 63.63  ? 26  ASN F O   1 
ATOM   5794  C  CB  . ASN F  1 27  ? 21.095  233.338 33.725  1.00 56.85  ? 26  ASN F CB  1 
ATOM   5795  C  CG  . ASN F  1 27  ? 21.302  231.839 33.655  1.00 61.06  ? 26  ASN F CG  1 
ATOM   5796  O  OD1 . ASN F  1 27  ? 22.400  231.359 33.747  1.00 59.13  ? 26  ASN F OD1 1 
ATOM   5797  N  ND2 . ASN F  1 27  ? 20.240  231.109 33.518  1.00 63.30  ? 26  ASN F ND2 1 
ATOM   5798  N  N   . GLY F  1 28  ? 21.048  232.539 37.162  1.00 53.17  ? 27  GLY F N   1 
ATOM   5799  C  CA  . GLY F  1 28  ? 20.402  231.532 37.949  1.00 45.32  ? 27  GLY F CA  1 
ATOM   5800  C  C   . GLY F  1 28  ? 20.052  231.851 39.353  1.00 40.63  ? 27  GLY F C   1 
ATOM   5801  O  O   . GLY F  1 28  ? 20.381  232.865 39.879  1.00 35.86  ? 27  GLY F O   1 
ATOM   5802  N  N   . PRO F  1 29  ? 19.373  230.927 39.974  1.00 41.74  ? 28  PRO F N   1 
ATOM   5803  C  CA  . PRO F  1 29  ? 18.918  231.037 41.340  1.00 41.57  ? 28  PRO F CA  1 
ATOM   5804  C  C   . PRO F  1 29  ? 20.063  231.038 42.307  1.00 38.87  ? 28  PRO F C   1 
ATOM   5805  O  O   . PRO F  1 29  ? 21.066  230.456 42.059  1.00 38.71  ? 28  PRO F O   1 
ATOM   5806  C  CB  . PRO F  1 29  ? 18.056  229.807 41.507  1.00 44.11  ? 28  PRO F CB  1 
ATOM   5807  C  CG  . PRO F  1 29  ? 18.529  228.879 40.490  1.00 38.16  ? 28  PRO F CG  1 
ATOM   5808  C  CD  . PRO F  1 29  ? 18.909  229.706 39.340  1.00 37.59  ? 28  PRO F CD  1 
ATOM   5809  N  N   . VAL F  1 30  ? 19.893  231.725 43.408  1.00 33.18  ? 29  VAL F N   1 
ATOM   5810  C  CA  . VAL F  1 30  ? 20.915  231.785 44.393  1.00 31.03  ? 29  VAL F CA  1 
ATOM   5811  C  C   . VAL F  1 30  ? 20.485  230.924 45.513  1.00 29.95  ? 29  VAL F C   1 
ATOM   5812  O  O   . VAL F  1 30  ? 19.411  231.039 45.972  1.00 34.41  ? 29  VAL F O   1 
ATOM   5813  C  CB  . VAL F  1 30  ? 21.117  233.195 44.922  1.00 31.86  ? 29  VAL F CB  1 
ATOM   5814  C  CG1 . VAL F  1 30  ? 22.160  233.193 46.002  1.00 27.33  ? 29  VAL F CG1 1 
ATOM   5815  C  CG2 . VAL F  1 30  ? 21.491  234.142 43.812  1.00 24.65  ? 29  VAL F CG2 1 
ATOM   5816  N  N   . LYS F  1 31  ? 21.351  230.035 45.927  1.00 32.33  ? 30  LYS F N   1 
ATOM   5817  C  CA  . LYS F  1 31  ? 21.068  229.165 47.018  1.00 32.30  ? 30  LYS F CA  1 
ATOM   5818  C  C   . LYS F  1 31  ? 21.465  229.872 48.280  1.00 29.78  ? 30  LYS F C   1 
ATOM   5819  O  O   . LYS F  1 31  ? 22.451  230.524 48.320  1.00 30.77  ? 30  LYS F O   1 
ATOM   5820  C  CB  . LYS F  1 31  ? 21.829  227.883 46.841  1.00 36.19  ? 30  LYS F CB  1 
ATOM   5821  C  CG  . LYS F  1 31  ? 20.951  226.734 46.450  1.00 45.05  ? 30  LYS F CG  1 
ATOM   5822  C  CD  . LYS F  1 31  ? 21.185  226.303 45.023  1.00 59.49  ? 30  LYS F CD  1 
ATOM   5823  C  CE  . LYS F  1 31  ? 21.732  224.894 44.934  1.00 59.29  ? 30  LYS F CE  1 
ATOM   5824  N  NZ  . LYS F  1 31  ? 20.709  223.880 44.603  1.00 59.50  ? 30  LYS F NZ  1 
ATOM   5825  N  N   . VAL F  1 32  ? 20.631  229.801 49.294  1.00 28.98  ? 31  VAL F N   1 
ATOM   5826  C  CA  . VAL F  1 32  ? 20.892  230.463 50.555  1.00 29.50  ? 31  VAL F CA  1 
ATOM   5827  C  C   . VAL F  1 32  ? 20.752  229.469 51.681  1.00 29.12  ? 31  VAL F C   1 
ATOM   5828  O  O   . VAL F  1 32  ? 19.721  228.949 51.900  1.00 29.51  ? 31  VAL F O   1 
ATOM   5829  C  CB  . VAL F  1 32  ? 19.969  231.685 50.783  1.00 29.14  ? 31  VAL F CB  1 
ATOM   5830  C  CG1 . VAL F  1 32  ? 20.394  232.504 51.964  1.00 25.30  ? 31  VAL F CG1 1 
ATOM   5831  C  CG2 . VAL F  1 32  ? 19.897  232.581 49.575  1.00 27.27  ? 31  VAL F CG2 1 
ATOM   5832  N  N   . TRP F  1 33  ? 21.819  229.211 52.396  1.00 30.09  ? 32  TRP F N   1 
ATOM   5833  C  CA  . TRP F  1 33  ? 21.760  228.254 53.457  1.00 33.73  ? 32  TRP F CA  1 
ATOM   5834  C  C   . TRP F  1 33  ? 22.737  228.524 54.570  1.00 33.60  ? 32  TRP F C   1 
ATOM   5835  O  O   . TRP F  1 33  ? 23.679  229.226 54.412  1.00 34.45  ? 32  TRP F O   1 
ATOM   5836  C  CB  . TRP F  1 33  ? 22.006  226.859 52.884  1.00 34.37  ? 32  TRP F CB  1 
ATOM   5837  C  CG  . TRP F  1 33  ? 23.321  226.739 52.253  1.00 38.94  ? 32  TRP F CG  1 
ATOM   5838  C  CD1 . TRP F  1 33  ? 23.693  227.225 51.057  1.00 36.18  ? 32  TRP F CD1 1 
ATOM   5839  C  CD2 . TRP F  1 33  ? 24.461  226.140 52.807  1.00 34.02  ? 32  TRP F CD2 1 
ATOM   5840  N  NE1 . TRP F  1 33  ? 24.985  226.964 50.827  1.00 35.40  ? 32  TRP F NE1 1 
ATOM   5841  C  CE2 . TRP F  1 33  ? 25.486  226.291 51.893  1.00 34.92  ? 32  TRP F CE2 1 
ATOM   5842  C  CE3 . TRP F  1 33  ? 24.715  225.492 53.997  1.00 38.24  ? 32  TRP F CE3 1 
ATOM   5843  C  CZ2 . TRP F  1 33  ? 26.734  225.820 52.117  1.00 41.01  ? 32  TRP F CZ2 1 
ATOM   5844  C  CZ3 . TRP F  1 33  ? 25.945  225.031 54.223  1.00 45.23  ? 32  TRP F CZ3 1 
ATOM   5845  C  CH2 . TRP F  1 33  ? 26.950  225.188 53.294  1.00 45.95  ? 32  TRP F CH2 1 
ATOM   5846  N  N   . GLY F  1 34  ? 22.454  227.978 55.725  1.00 31.88  ? 33  GLY F N   1 
ATOM   5847  C  CA  . GLY F  1 34  ? 23.353  228.074 56.857  1.00 28.28  ? 33  GLY F CA  1 
ATOM   5848  C  C   . GLY F  1 34  ? 22.547  228.025 58.109  1.00 28.28  ? 33  GLY F C   1 
ATOM   5849  O  O   . GLY F  1 34  ? 21.421  227.659 58.086  1.00 32.28  ? 33  GLY F O   1 
ATOM   5850  N  N   . SER F  1 35  ? 23.107  228.481 59.198  1.00 30.09  ? 34  SER F N   1 
ATOM   5851  C  CA  . SER F  1 35  ? 22.558  228.260 60.497  1.00 31.03  ? 34  SER F CA  1 
ATOM   5852  C  C   . SER F  1 35  ? 22.515  229.521 61.328  1.00 34.20  ? 34  SER F C   1 
ATOM   5853  O  O   . SER F  1 35  ? 23.478  230.312 61.365  1.00 39.15  ? 34  SER F O   1 
ATOM   5854  C  CB  . SER F  1 35  ? 23.514  227.333 61.181  1.00 33.51  ? 34  SER F CB  1 
ATOM   5855  O  OG  . SER F  1 35  ? 22.794  226.416 61.857  1.00 40.03  ? 34  SER F OG  1 
ATOM   5856  N  N   . ILE F  1 36  ? 21.422  229.753 62.008  1.00 33.25  ? 35  ILE F N   1 
ATOM   5857  C  CA  . ILE F  1 36  ? 21.384  230.912 62.868  1.00 32.45  ? 35  ILE F CA  1 
ATOM   5858  C  C   . ILE F  1 36  ? 20.859  230.424 64.186  1.00 34.64  ? 35  ILE F C   1 
ATOM   5859  O  O   . ILE F  1 36  ? 19.804  229.752 64.248  1.00 36.59  ? 35  ILE F O   1 
ATOM   5860  C  CB  . ILE F  1 36  ? 20.429  231.986 62.394  1.00 30.30  ? 35  ILE F CB  1 
ATOM   5861  C  CG1 . ILE F  1 36  ? 20.592  232.286 60.901  1.00 28.29  ? 35  ILE F CG1 1 
ATOM   5862  C  CG2 . ILE F  1 36  ? 20.693  233.239 63.192  1.00 28.93  ? 35  ILE F CG2 1 
ATOM   5863  C  CD1 . ILE F  1 36  ? 19.588  233.259 60.296  1.00 23.52  ? 35  ILE F CD1 1 
ATOM   5864  N  N   . LYS F  1 37  ? 21.560  230.758 65.250  1.00 33.54  ? 36  LYS F N   1 
ATOM   5865  C  CA  . LYS F  1 37  ? 21.084  230.275 66.567  1.00 38.54  ? 36  LYS F CA  1 
ATOM   5866  C  C   . LYS F  1 37  ? 20.716  231.367 67.479  1.00 31.60  ? 36  LYS F C   1 
ATOM   5867  O  O   . LYS F  1 37  ? 20.922  232.487 67.101  1.00 35.11  ? 36  LYS F O   1 
ATOM   5868  C  CB  . LYS F  1 37  ? 22.021  229.233 67.191  1.00 42.79  ? 36  LYS F CB  1 
ATOM   5869  C  CG  . LYS F  1 37  ? 23.401  229.736 67.637  1.00 51.40  ? 36  LYS F CG  1 
ATOM   5870  C  CD  . LYS F  1 37  ? 24.296  228.524 67.974  1.00 65.46  ? 36  LYS F CD  1 
ATOM   5871  C  CE  . LYS F  1 37  ? 25.720  228.916 68.459  1.00 79.36  ? 36  LYS F CE  1 
ATOM   5872  N  NZ  . LYS F  1 37  ? 25.814  229.740 69.738  1.00 74.37  ? 36  LYS F NZ  1 
ATOM   5873  N  N   . GLY F  1 38  ? 20.106  231.063 68.625  1.00 33.36  ? 37  GLY F N   1 
ATOM   5874  C  CA  . GLY F  1 38  ? 19.726  232.065 69.622  1.00 28.17  ? 37  GLY F CA  1 
ATOM   5875  C  C   . GLY F  1 38  ? 18.405  232.755 69.320  1.00 31.79  ? 37  GLY F C   1 
ATOM   5876  O  O   . GLY F  1 38  ? 18.110  233.763 69.900  1.00 34.92  ? 37  GLY F O   1 
ATOM   5877  N  N   . LEU F  1 39  ? 17.596  232.248 68.400  1.00 35.12  ? 38  LEU F N   1 
ATOM   5878  C  CA  . LEU F  1 39  ? 16.328  232.895 68.106  1.00 31.94  ? 38  LEU F CA  1 
ATOM   5879  C  C   . LEU F  1 39  ? 15.206  232.271 68.901  1.00 32.28  ? 38  LEU F C   1 
ATOM   5880  O  O   . LEU F  1 39  ? 15.351  231.123 69.369  1.00 34.48  ? 38  LEU F O   1 
ATOM   5881  C  CB  . LEU F  1 39  ? 16.003  232.724 66.634  1.00 33.20  ? 38  LEU F CB  1 
ATOM   5882  C  CG  . LEU F  1 39  ? 16.854  233.334 65.533  1.00 34.27  ? 38  LEU F CG  1 
ATOM   5883  C  CD1 . LEU F  1 39  ? 16.745  232.596 64.193  1.00 35.14  ? 38  LEU F CD1 1 
ATOM   5884  C  CD2 . LEU F  1 39  ? 16.469  234.766 65.331  1.00 30.54  ? 38  LEU F CD2 1 
ATOM   5885  N  N   . THR F  1 40  ? 14.095  232.991 69.030  1.00 29.42  ? 39  THR F N   1 
ATOM   5886  C  CA  . THR F  1 40  ? 12.813  232.431 69.544  1.00 32.62  ? 39  THR F CA  1 
ATOM   5887  C  C   . THR F  1 40  ? 12.206  231.421 68.550  1.00 31.82  ? 39  THR F C   1 
ATOM   5888  O  O   . THR F  1 40  ? 12.312  231.620 67.388  1.00 35.02  ? 39  THR F O   1 
ATOM   5889  C  CB  . THR F  1 40  ? 11.789  233.559 69.857  1.00 31.58  ? 39  THR F CB  1 
ATOM   5890  O  OG1 . THR F  1 40  ? 11.378  234.261 68.650  1.00 30.86  ? 39  THR F OG1 1 
ATOM   5891  C  CG2 . THR F  1 40  ? 12.421  234.547 70.810  1.00 27.70  ? 39  THR F CG2 1 
ATOM   5892  N  N   . GLU F  1 41  ? 11.595  230.344 69.000  1.00 32.27  ? 40  GLU F N   1 
ATOM   5893  C  CA  . GLU F  1 41  ? 10.991  229.384 68.119  1.00 32.19  ? 40  GLU F CA  1 
ATOM   5894  C  C   . GLU F  1 41  ? 9.968   230.138 67.241  1.00 34.97  ? 40  GLU F C   1 
ATOM   5895  O  O   . GLU F  1 41  ? 9.242   230.954 67.744  1.00 33.48  ? 40  GLU F O   1 
ATOM   5896  C  CB  . GLU F  1 41  ? 10.279  228.333 68.954  1.00 32.45  ? 40  GLU F CB  1 
ATOM   5897  C  CG  . GLU F  1 41  ? 9.688   227.168 68.163  1.00 35.55  ? 40  GLU F CG  1 
ATOM   5898  C  CD  . GLU F  1 41  ? 9.099   226.040 69.028  1.00 40.15  ? 40  GLU F CD  1 
ATOM   5899  O  OE1 . GLU F  1 41  ? 8.936   226.189 70.252  1.00 40.70  ? 40  GLU F OE1 1 
ATOM   5900  O  OE2 . GLU F  1 41  ? 8.770   224.970 68.463  1.00 47.13  ? 40  GLU F OE2 1 
ATOM   5901  N  N   . GLY F  1 42  ? 9.968   229.902 65.924  1.00 36.42  ? 41  GLY F N   1 
ATOM   5902  C  CA  . GLY F  1 42  ? 8.917   230.400 65.017  1.00 32.27  ? 41  GLY F CA  1 
ATOM   5903  C  C   . GLY F  1 42  ? 9.522   231.162 63.868  1.00 32.31  ? 41  GLY F C   1 
ATOM   5904  O  O   . GLY F  1 42  ? 10.697  231.000 63.607  1.00 32.80  ? 41  GLY F O   1 
ATOM   5905  N  N   . LEU F  1 43  ? 8.725   232.015 63.236  1.00 30.24  ? 42  LEU F N   1 
ATOM   5906  C  CA  . LEU F  1 43  ? 9.084   232.747 62.049  1.00 28.70  ? 42  LEU F CA  1 
ATOM   5907  C  C   . LEU F  1 43  ? 9.817   234.035 62.339  1.00 28.20  ? 42  LEU F C   1 
ATOM   5908  O  O   . LEU F  1 43  ? 9.479   234.708 63.235  1.00 31.31  ? 42  LEU F O   1 
ATOM   5909  C  CB  . LEU F  1 43  ? 7.827   233.077 61.303  1.00 28.35  ? 42  LEU F CB  1 
ATOM   5910  C  CG  . LEU F  1 43  ? 7.083   231.862 60.738  1.00 33.14  ? 42  LEU F CG  1 
ATOM   5911  C  CD1 . LEU F  1 43  ? 5.683   232.229 60.272  1.00 32.98  ? 42  LEU F CD1 1 
ATOM   5912  C  CD2 . LEU F  1 43  ? 7.776   231.134 59.609  1.00 34.97  ? 42  LEU F CD2 1 
ATOM   5913  N  N   . HIS F  1 44  ? 10.838  234.357 61.562  1.00 29.78  ? 43  HIS F N   1 
ATOM   5914  C  CA  . HIS F  1 44  ? 11.598  235.608 61.643  1.00 28.04  ? 43  HIS F CA  1 
ATOM   5915  C  C   . HIS F  1 44  ? 11.852  236.095 60.217  1.00 28.91  ? 43  HIS F C   1 
ATOM   5916  O  O   . HIS F  1 44  ? 12.365  235.333 59.350  1.00 31.27  ? 43  HIS F O   1 
ATOM   5917  C  CB  . HIS F  1 44  ? 12.947  235.323 62.313  1.00 27.18  ? 43  HIS F CB  1 
ATOM   5918  C  CG  . HIS F  1 44  ? 12.836  234.863 63.752  1.00 31.22  ? 43  HIS F CG  1 
ATOM   5919  N  ND1 . HIS F  1 44  ? 12.686  235.749 64.820  1.00 28.90  ? 43  HIS F ND1 1 
ATOM   5920  C  CD2 . HIS F  1 44  ? 12.879  233.623 64.296  1.00 27.95  ? 43  HIS F CD2 1 
ATOM   5921  C  CE1 . HIS F  1 44  ? 12.665  235.072 65.945  1.00 29.24  ? 43  HIS F CE1 1 
ATOM   5922  N  NE2 . HIS F  1 44  ? 12.773  233.786 65.663  1.00 32.74  ? 43  HIS F NE2 1 
ATOM   5923  N  N   . GLY F  1 45  ? 11.524  237.355 59.945  1.00 29.40  ? 44  GLY F N   1 
ATOM   5924  C  CA  . GLY F  1 45  ? 11.747  237.974 58.633  1.00 25.08  ? 44  GLY F CA  1 
ATOM   5925  C  C   . GLY F  1 45  ? 13.211  237.935 58.329  1.00 26.89  ? 44  GLY F C   1 
ATOM   5926  O  O   . GLY F  1 45  ? 14.005  238.056 59.204  1.00 29.59  ? 44  GLY F O   1 
ATOM   5927  N  N   . PHE F  1 46  ? 13.557  237.744 57.077  1.00 28.03  ? 45  PHE F N   1 
ATOM   5928  C  CA  . PHE F  1 46  ? 14.900  237.508 56.664  1.00 30.16  ? 45  PHE F CA  1 
ATOM   5929  C  C   . PHE F  1 46  ? 15.057  238.358 55.397  1.00 29.51  ? 45  PHE F C   1 
ATOM   5930  O  O   . PHE F  1 46  ? 14.478  238.032 54.378  1.00 28.10  ? 45  PHE F O   1 
ATOM   5931  C  CB  . PHE F  1 46  ? 15.035  236.013 56.400  1.00 28.97  ? 45  PHE F CB  1 
ATOM   5932  C  CG  . PHE F  1 46  ? 16.411  235.512 56.131  1.00 29.62  ? 45  PHE F CG  1 
ATOM   5933  C  CD1 . PHE F  1 46  ? 17.379  235.536 57.133  1.00 29.30  ? 45  PHE F CD1 1 
ATOM   5934  C  CD2 . PHE F  1 46  ? 16.728  234.889 54.901  1.00 25.55  ? 45  PHE F CD2 1 
ATOM   5935  C  CE1 . PHE F  1 46  ? 18.633  234.962 56.914  1.00 28.48  ? 45  PHE F CE1 1 
ATOM   5936  C  CE2 . PHE F  1 46  ? 17.984  234.308 54.678  1.00 24.48  ? 45  PHE F CE2 1 
ATOM   5937  C  CZ  . PHE F  1 46  ? 18.953  234.377 55.675  1.00 28.03  ? 45  PHE F CZ  1 
ATOM   5938  N  N   . HIS F  1 47  ? 15.778  239.494 55.504  1.00 28.50  ? 46  HIS F N   1 
ATOM   5939  C  CA  . HIS F  1 47  ? 15.846  240.486 54.389  1.00 29.47  ? 46  HIS F CA  1 
ATOM   5940  C  C   . HIS F  1 47  ? 17.253  240.916 54.031  1.00 27.90  ? 46  HIS F C   1 
ATOM   5941  O  O   . HIS F  1 47  ? 18.136  241.023 54.915  1.00 30.93  ? 46  HIS F O   1 
ATOM   5942  C  CB  . HIS F  1 47  ? 14.916  241.716 54.657  1.00 26.91  ? 46  HIS F CB  1 
ATOM   5943  C  CG  . HIS F  1 47  ? 13.554  241.337 55.185  1.00 29.65  ? 46  HIS F CG  1 
ATOM   5944  N  ND1 . HIS F  1 47  ? 13.142  241.593 56.481  1.00 30.52  ? 46  HIS F ND1 1 
ATOM   5945  C  CD2 . HIS F  1 47  ? 12.536  240.648 54.605  1.00 25.40  ? 46  HIS F CD2 1 
ATOM   5946  C  CE1 . HIS F  1 47  ? 11.927  241.102 56.665  1.00 25.81  ? 46  HIS F CE1 1 
ATOM   5947  N  NE2 . HIS F  1 47  ? 11.541  240.521 55.544  1.00 26.53  ? 46  HIS F NE2 1 
ATOM   5948  N  N   . VAL F  1 48  ? 17.469  241.190 52.765  1.00 24.59  ? 47  VAL F N   1 
ATOM   5949  C  CA  . VAL F  1 48  ? 18.611  241.956 52.408  1.00 25.62  ? 47  VAL F CA  1 
ATOM   5950  C  C   . VAL F  1 48  ? 18.276  243.447 52.452  1.00 28.39  ? 47  VAL F C   1 
ATOM   5951  O  O   . VAL F  1 48  ? 17.288  243.905 51.890  1.00 29.49  ? 47  VAL F O   1 
ATOM   5952  C  CB  . VAL F  1 48  ? 19.157  241.581 51.040  1.00 28.54  ? 47  VAL F CB  1 
ATOM   5953  C  CG1 . VAL F  1 48  ? 20.484  242.319 50.763  1.00 24.11  ? 47  VAL F CG1 1 
ATOM   5954  C  CG2 . VAL F  1 48  ? 19.313  240.077 50.921  1.00 26.37  ? 47  VAL F CG2 1 
ATOM   5955  N  N   . HIS F  1 49  ? 19.080  244.232 53.144  1.00 30.46  ? 48  HIS F N   1 
ATOM   5956  C  CA  . HIS F  1 49  ? 18.807  245.686 53.259  1.00 30.24  ? 48  HIS F CA  1 
ATOM   5957  C  C   . HIS F  1 49  ? 19.820  246.413 52.361  1.00 28.88  ? 48  HIS F C   1 
ATOM   5958  O  O   . HIS F  1 49  ? 20.843  245.843 52.016  1.00 27.07  ? 48  HIS F O   1 
ATOM   5959  C  CB  . HIS F  1 49  ? 18.907  246.185 54.737  1.00 27.38  ? 48  HIS F CB  1 
ATOM   5960  C  CG  . HIS F  1 49  ? 17.787  245.708 55.608  1.00 30.36  ? 48  HIS F CG  1 
ATOM   5961  N  ND1 . HIS F  1 49  ? 16.995  246.573 56.323  1.00 26.48  ? 48  HIS F ND1 1 
ATOM   5962  C  CD2 . HIS F  1 49  ? 17.338  244.452 55.906  1.00 30.68  ? 48  HIS F CD2 1 
ATOM   5963  C  CE1 . HIS F  1 49  ? 16.089  245.884 56.991  1.00 27.87  ? 48  HIS F CE1 1 
ATOM   5964  N  NE2 . HIS F  1 49  ? 16.288  244.594 56.788  1.00 28.15  ? 48  HIS F NE2 1 
ATOM   5965  N  N   . GLU F  1 50  ? 19.510  247.660 52.016  1.00 28.33  ? 49  GLU F N   1 
ATOM   5966  C  CA  . GLU F  1 50  ? 20.185  248.398 51.005  1.00 29.87  ? 49  GLU F CA  1 
ATOM   5967  C  C   . GLU F  1 50  ? 21.688  248.625 51.272  1.00 30.89  ? 49  GLU F C   1 
ATOM   5968  O  O   . GLU F  1 50  ? 22.494  248.412 50.385  1.00 31.94  ? 49  GLU F O   1 
ATOM   5969  C  CB  . GLU F  1 50  ? 19.413  249.700 50.726  1.00 29.61  ? 49  GLU F CB  1 
ATOM   5970  C  CG  . GLU F  1 50  ? 19.931  250.371 49.504  1.00 29.73  ? 49  GLU F CG  1 
ATOM   5971  C  CD  . GLU F  1 50  ? 19.288  251.689 49.157  1.00 32.76  ? 49  GLU F CD  1 
ATOM   5972  O  OE1 . GLU F  1 50  ? 18.393  252.232 49.867  1.00 34.91  ? 49  GLU F OE1 1 
ATOM   5973  O  OE2 . GLU F  1 50  ? 19.773  252.245 48.153  1.00 33.89  ? 49  GLU F OE2 1 
ATOM   5974  N  N   . PHE F  1 51  ? 22.059  249.002 52.500  1.00 30.72  ? 50  PHE F N   1 
ATOM   5975  C  CA  . PHE F  1 51  ? 23.446  249.365 52.801  1.00 28.64  ? 50  PHE F CA  1 
ATOM   5976  C  C   . PHE F  1 51  ? 24.268  248.417 53.608  1.00 30.60  ? 50  PHE F C   1 
ATOM   5977  O  O   . PHE F  1 51  ? 23.873  247.986 54.671  1.00 33.48  ? 50  PHE F O   1 
ATOM   5978  C  CB  . PHE F  1 51  ? 23.506  250.751 53.441  1.00 29.40  ? 50  PHE F CB  1 
ATOM   5979  C  CG  . PHE F  1 51  ? 22.723  251.785 52.677  1.00 30.53  ? 50  PHE F CG  1 
ATOM   5980  C  CD1 . PHE F  1 51  ? 23.135  252.217 51.439  1.00 27.58  ? 50  PHE F CD1 1 
ATOM   5981  C  CD2 . PHE F  1 51  ? 21.475  252.243 53.167  1.00 33.98  ? 50  PHE F CD2 1 
ATOM   5982  C  CE1 . PHE F  1 51  ? 22.349  253.130 50.709  1.00 30.20  ? 50  PHE F CE1 1 
ATOM   5983  C  CE2 . PHE F  1 51  ? 20.688  253.157 52.443  1.00 31.13  ? 50  PHE F CE2 1 
ATOM   5984  C  CZ  . PHE F  1 51  ? 21.145  253.615 51.210  1.00 28.78  ? 50  PHE F CZ  1 
ATOM   5985  N  N   . GLY F  1 52  ? 25.454  248.111 53.089  1.00 32.40  ? 51  GLY F N   1 
ATOM   5986  C  CA  . GLY F  1 52  ? 26.461  247.430 53.845  1.00 31.19  ? 51  GLY F CA  1 
ATOM   5987  C  C   . GLY F  1 52  ? 27.068  248.297 54.939  1.00 31.53  ? 51  GLY F C   1 
ATOM   5988  O  O   . GLY F  1 52  ? 28.260  248.340 55.054  1.00 32.81  ? 51  GLY F O   1 
ATOM   5989  N  N   . ASP F  1 53  ? 26.241  248.992 55.714  1.00 34.18  ? 52  ASP F N   1 
ATOM   5990  C  CA  . ASP F  1 53  ? 26.667  250.018 56.620  1.00 31.59  ? 52  ASP F CA  1 
ATOM   5991  C  C   . ASP F  1 53  ? 26.363  249.653 58.038  1.00 33.88  ? 52  ASP F C   1 
ATOM   5992  O  O   . ASP F  1 53  ? 25.232  249.708 58.514  1.00 34.97  ? 52  ASP F O   1 
ATOM   5993  C  CB  . ASP F  1 53  ? 26.041  251.333 56.263  1.00 29.97  ? 52  ASP F CB  1 
ATOM   5994  C  CG  . ASP F  1 53  ? 26.601  252.484 57.083  1.00 34.25  ? 52  ASP F CG  1 
ATOM   5995  O  OD1 . ASP F  1 53  ? 27.123  252.266 58.172  1.00 36.94  ? 52  ASP F OD1 1 
ATOM   5996  O  OD2 . ASP F  1 53  ? 26.549  253.651 56.651  1.00 37.27  ? 52  ASP F OD2 1 
ATOM   5997  N  N   . ASN F  1 54  ? 27.420  249.293 58.728  1.00 34.60  ? 53  ASN F N   1 
ATOM   5998  C  CA  . ASN F  1 54  ? 27.262  248.841 60.038  1.00 33.91  ? 53  ASN F CA  1 
ATOM   5999  C  C   . ASN F  1 54  ? 27.738  249.837 61.048  1.00 31.03  ? 53  ASN F C   1 
ATOM   6000  O  O   . ASN F  1 54  ? 27.925  249.496 62.147  1.00 32.09  ? 53  ASN F O   1 
ATOM   6001  C  CB  . ASN F  1 54  ? 28.045  247.578 60.182  1.00 38.09  ? 53  ASN F CB  1 
ATOM   6002  C  CG  . ASN F  1 54  ? 27.661  246.833 61.442  1.00 54.63  ? 53  ASN F CG  1 
ATOM   6003  O  OD1 . ASN F  1 54  ? 26.447  246.603 61.686  1.00 55.63  ? 53  ASN F OD1 1 
ATOM   6004  N  ND2 . ASN F  1 54  ? 28.661  246.533 62.312  1.00 44.86  ? 53  ASN F ND2 1 
ATOM   6005  N  N   . THR F  1 55  ? 27.972  251.080 60.674  1.00 34.27  ? 54  THR F N   1 
ATOM   6006  C  CA  . THR F  1 55  ? 28.416  252.092 61.656  1.00 35.07  ? 54  THR F CA  1 
ATOM   6007  C  C   . THR F  1 55  ? 27.462  252.343 62.858  1.00 35.44  ? 54  THR F C   1 
ATOM   6008  O  O   . THR F  1 55  ? 27.909  252.684 63.928  1.00 38.37  ? 54  THR F O   1 
ATOM   6009  C  CB  . THR F  1 55  ? 28.692  253.440 61.033  1.00 32.77  ? 54  THR F CB  1 
ATOM   6010  O  OG1 . THR F  1 55  ? 27.465  253.966 60.536  1.00 28.98  ? 54  THR F OG1 1 
ATOM   6011  C  CG2 . THR F  1 55  ? 29.801  253.358 59.970  1.00 27.54  ? 54  THR F CG2 1 
ATOM   6012  N  N   . ALA F  1 56  ? 26.171  252.174 62.701  1.00 32.40  ? 55  ALA F N   1 
ATOM   6013  C  CA  . ALA F  1 56  ? 25.317  252.299 63.829  1.00 32.84  ? 55  ALA F CA  1 
ATOM   6014  C  C   . ALA F  1 56  ? 24.670  250.921 64.137  1.00 35.30  ? 55  ALA F C   1 
ATOM   6015  O  O   . ALA F  1 56  ? 23.505  250.852 64.428  1.00 41.82  ? 55  ALA F O   1 
ATOM   6016  C  CB  . ALA F  1 56  ? 24.276  253.377 63.537  1.00 28.62  ? 55  ALA F CB  1 
ATOM   6017  N  N   . GLY F  1 57  ? 25.397  249.816 64.050  1.00 36.45  ? 56  GLY F N   1 
ATOM   6018  C  CA  . GLY F  1 57  ? 24.746  248.504 64.105  1.00 39.35  ? 56  GLY F CA  1 
ATOM   6019  C  C   . GLY F  1 57  ? 23.767  248.271 62.909  1.00 42.57  ? 56  GLY F C   1 
ATOM   6020  O  O   . GLY F  1 57  ? 23.998  248.726 61.775  1.00 42.10  ? 56  GLY F O   1 
ATOM   6021  N  N   . CYS F  1 58  ? 22.694  247.545 63.164  1.00 35.66  ? 57  CYS F N   1 
ATOM   6022  C  CA  . CYS F  1 58  ? 21.858  247.114 62.133  1.00 34.63  ? 57  CYS F CA  1 
ATOM   6023  C  C   . CYS F  1 58  ? 20.982  248.243 61.621  1.00 35.08  ? 57  CYS F C   1 
ATOM   6024  O  O   . CYS F  1 58  ? 20.542  248.190 60.492  1.00 32.40  ? 57  CYS F O   1 
ATOM   6025  C  CB  . CYS F  1 58  ? 21.031  245.984 62.629  1.00 38.96  ? 57  CYS F CB  1 
ATOM   6026  S  SG  . CYS F  1 58  ? 21.937  244.455 62.982  1.00 41.52  ? 57  CYS F SG  1 
ATOM   6027  N  N   . THR F  1 59  ? 20.793  249.288 62.409  1.00 33.97  ? 58  THR F N   1 
ATOM   6028  C  CA  . THR F  1 59  ? 19.955  250.425 62.003  1.00 34.84  ? 58  THR F CA  1 
ATOM   6029  C  C   . THR F  1 59  ? 20.480  251.109 60.745  1.00 37.50  ? 58  THR F C   1 
ATOM   6030  O  O   . THR F  1 59  ? 19.693  251.687 59.956  1.00 38.91  ? 58  THR F O   1 
ATOM   6031  C  CB  . THR F  1 59  ? 19.917  251.552 63.065  1.00 36.28  ? 58  THR F CB  1 
ATOM   6032  O  OG1 . THR F  1 59  ? 19.919  250.996 64.373  1.00 47.40  ? 58  THR F OG1 1 
ATOM   6033  C  CG2 . THR F  1 59  ? 18.729  252.351 62.921  1.00 33.55  ? 58  THR F CG2 1 
ATOM   6034  N  N   . SER F  1 60  ? 21.802  251.104 60.574  1.00 34.53  ? 59  SER F N   1 
ATOM   6035  C  CA  . SER F  1 60  ? 22.380  251.825 59.454  1.00 30.97  ? 59  SER F CA  1 
ATOM   6036  C  C   . SER F  1 60  ? 22.345  251.145 58.107  1.00 30.03  ? 59  SER F C   1 
ATOM   6037  O  O   . SER F  1 60  ? 22.774  251.703 57.117  1.00 34.20  ? 59  SER F O   1 
ATOM   6038  C  CB  . SER F  1 60  ? 23.743  252.420 59.801  1.00 30.77  ? 59  SER F CB  1 
ATOM   6039  O  OG  . SER F  1 60  ? 24.462  251.652 60.701  1.00 32.31  ? 59  SER F OG  1 
ATOM   6040  N  N   . ALA F  1 61  ? 21.757  249.968 58.071  1.00 32.02  ? 60  ALA F N   1 
ATOM   6041  C  CA  . ALA F  1 61  ? 21.618  249.174 56.882  1.00 27.75  ? 60  ALA F CA  1 
ATOM   6042  C  C   . ALA F  1 61  ? 20.510  249.744 55.988  1.00 28.39  ? 60  ALA F C   1 
ATOM   6043  O  O   . ALA F  1 61  ? 20.423  249.433 54.799  1.00 28.16  ? 60  ALA F O   1 
ATOM   6044  C  CB  . ALA F  1 61  ? 21.335  247.740 57.274  1.00 23.86  ? 60  ALA F CB  1 
ATOM   6045  N  N   . GLY F  1 62  ? 19.691  250.611 56.543  1.00 27.30  ? 61  GLY F N   1 
ATOM   6046  C  CA  . GLY F  1 62  ? 18.674  251.240 55.749  1.00 28.57  ? 61  GLY F CA  1 
ATOM   6047  C  C   . GLY F  1 62  ? 17.494  250.316 55.557  1.00 30.81  ? 61  GLY F C   1 
ATOM   6048  O  O   . GLY F  1 62  ? 17.336  249.319 56.279  1.00 32.22  ? 61  GLY F O   1 
ATOM   6049  N  N   . PRO F  1 63  ? 16.619  250.657 54.615  1.00 33.22  ? 62  PRO F N   1 
ATOM   6050  C  CA  . PRO F  1 63  ? 15.501  249.757 54.300  1.00 31.41  ? 62  PRO F CA  1 
ATOM   6051  C  C   . PRO F  1 63  ? 15.894  248.553 53.444  1.00 30.31  ? 62  PRO F C   1 
ATOM   6052  O  O   . PRO F  1 63  ? 17.050  248.390 53.043  1.00 30.23  ? 62  PRO F O   1 
ATOM   6053  C  CB  . PRO F  1 63  ? 14.548  250.658 53.489  1.00 31.14  ? 62  PRO F CB  1 
ATOM   6054  C  CG  . PRO F  1 63  ? 15.417  251.730 52.887  1.00 28.07  ? 62  PRO F CG  1 
ATOM   6055  C  CD  . PRO F  1 63  ? 16.731  251.767 53.641  1.00 31.86  ? 62  PRO F CD  1 
ATOM   6056  N  N   . HIS F  1 64  ? 14.893  247.736 53.178  1.00 30.12  ? 63  HIS F N   1 
ATOM   6057  C  CA  . HIS F  1 64  ? 14.989  246.647 52.275  1.00 33.12  ? 63  HIS F CA  1 
ATOM   6058  C  C   . HIS F  1 64  ? 15.541  247.099 50.938  1.00 30.40  ? 63  HIS F C   1 
ATOM   6059  O  O   . HIS F  1 64  ? 15.243  248.155 50.490  1.00 35.00  ? 63  HIS F O   1 
ATOM   6060  C  CB  . HIS F  1 64  ? 13.604  246.068 52.120  1.00 32.82  ? 63  HIS F CB  1 
ATOM   6061  C  CG  . HIS F  1 64  ? 13.063  245.410 53.357  1.00 33.41  ? 63  HIS F CG  1 
ATOM   6062  N  ND1 . HIS F  1 64  ? 11.909  244.669 53.340  1.00 33.19  ? 63  HIS F ND1 1 
ATOM   6063  C  CD2 . HIS F  1 64  ? 13.509  245.370 54.641  1.00 32.21  ? 63  HIS F CD2 1 
ATOM   6064  C  CE1 . HIS F  1 64  ? 11.641  244.233 54.564  1.00 31.63  ? 63  HIS F CE1 1 
ATOM   6065  N  NE2 . HIS F  1 64  ? 12.618  244.609 55.360  1.00 31.06  ? 63  HIS F NE2 1 
ATOM   6066  N  N   . PHE F  1 65  ? 16.458  246.337 50.412  1.00 30.05  ? 64  PHE F N   1 
ATOM   6067  C  CA  . PHE F  1 65  ? 17.033  246.542 49.125  1.00 30.97  ? 64  PHE F CA  1 
ATOM   6068  C  C   . PHE F  1 65  ? 15.905  246.454 48.114  1.00 31.99  ? 64  PHE F C   1 
ATOM   6069  O  O   . PHE F  1 65  ? 15.274  245.388 47.932  1.00 26.86  ? 64  PHE F O   1 
ATOM   6070  C  CB  . PHE F  1 65  ? 18.145  245.508 48.826  1.00 27.20  ? 64  PHE F CB  1 
ATOM   6071  C  CG  . PHE F  1 65  ? 18.803  245.719 47.486  1.00 27.69  ? 64  PHE F CG  1 
ATOM   6072  C  CD1 . PHE F  1 65  ? 19.076  247.010 47.026  1.00 26.15  ? 64  PHE F CD1 1 
ATOM   6073  C  CD2 . PHE F  1 65  ? 19.242  244.641 46.734  1.00 27.95  ? 64  PHE F CD2 1 
ATOM   6074  C  CE1 . PHE F  1 65  ? 19.717  247.210 45.805  1.00 28.17  ? 64  PHE F CE1 1 
ATOM   6075  C  CE2 . PHE F  1 65  ? 19.887  244.833 45.493  1.00 30.89  ? 64  PHE F CE2 1 
ATOM   6076  C  CZ  . PHE F  1 65  ? 20.089  246.131 45.003  1.00 27.52  ? 64  PHE F CZ  1 
ATOM   6077  N  N   . ASN F  1 66  ? 15.666  247.620 47.489  1.00 34.42  ? 65  ASN F N   1 
ATOM   6078  C  CA  . ASN F  1 66  ? 14.475  247.878 46.675  1.00 30.78  ? 65  ASN F CA  1 
ATOM   6079  C  C   . ASN F  1 66  ? 14.796  248.649 45.389  1.00 31.62  ? 65  ASN F C   1 
ATOM   6080  O  O   . ASN F  1 66  ? 14.218  249.691 45.121  1.00 30.49  ? 65  ASN F O   1 
ATOM   6081  C  CB  . ASN F  1 66  ? 13.404  248.593 47.472  1.00 25.73  ? 65  ASN F CB  1 
ATOM   6082  C  CG  . ASN F  1 66  ? 12.062  248.574 46.762  1.00 28.64  ? 65  ASN F CG  1 
ATOM   6083  O  OD1 . ASN F  1 66  ? 11.833  247.791 45.835  1.00 33.37  ? 65  ASN F OD1 1 
ATOM   6084  N  ND2 . ASN F  1 66  ? 11.162  249.400 47.195  1.00 28.37  ? 65  ASN F ND2 1 
ATOM   6085  N  N   . PRO F  1 67  ? 15.709  248.125 44.568  1.00 34.86  ? 66  PRO F N   1 
ATOM   6086  C  CA  . PRO F  1 67  ? 16.064  248.938 43.390  1.00 35.13  ? 66  PRO F CA  1 
ATOM   6087  C  C   . PRO F  1 67  ? 14.933  249.190 42.399  1.00 36.08  ? 66  PRO F C   1 
ATOM   6088  O  O   . PRO F  1 67  ? 14.983  250.176 41.711  1.00 41.32  ? 66  PRO F O   1 
ATOM   6089  C  CB  . PRO F  1 67  ? 17.198  248.162 42.741  1.00 32.19  ? 66  PRO F CB  1 
ATOM   6090  C  CG  . PRO F  1 67  ? 16.985  246.747 43.183  1.00 31.86  ? 66  PRO F CG  1 
ATOM   6091  C  CD  . PRO F  1 67  ? 16.432  246.837 44.581  1.00 32.02  ? 66  PRO F CD  1 
ATOM   6092  N  N   . LEU F  1 68  ? 13.904  248.368 42.360  1.00 35.26  ? 67  LEU F N   1 
ATOM   6093  C  CA  . LEU F  1 68  ? 12.822  248.626 41.445  1.00 34.60  ? 67  LEU F CA  1 
ATOM   6094  C  C   . LEU F  1 68  ? 11.691  249.390 42.122  1.00 36.24  ? 67  LEU F C   1 
ATOM   6095  O  O   . LEU F  1 68  ? 10.593  249.530 41.534  1.00 37.08  ? 67  LEU F O   1 
ATOM   6096  C  CB  . LEU F  1 68  ? 12.325  247.309 40.834  1.00 34.63  ? 67  LEU F CB  1 
ATOM   6097  C  CG  . LEU F  1 68  ? 13.354  246.583 39.934  1.00 38.85  ? 67  LEU F CG  1 
ATOM   6098  C  CD1 . LEU F  1 68  ? 12.929  245.141 39.576  1.00 37.61  ? 67  LEU F CD1 1 
ATOM   6099  C  CD2 . LEU F  1 68  ? 13.633  247.427 38.663  1.00 36.95  ? 67  LEU F CD2 1 
ATOM   6100  N  N   . SER F  1 69  ? 11.930  249.894 43.334  1.00 30.40  ? 68  SER F N   1 
ATOM   6101  C  CA  . SER F  1 69  ? 10.821  250.440 44.154  1.00 33.84  ? 68  SER F CA  1 
ATOM   6102  C  C   . SER F  1 69  ? 9.463   249.838 44.039  1.00 36.70  ? 68  SER F C   1 
ATOM   6103  O  O   . SER F  1 69  ? 8.524   250.506 43.597  1.00 39.31  ? 68  SER F O   1 
ATOM   6104  C  CB  . SER F  1 69  ? 10.576  251.920 43.978  1.00 34.71  ? 68  SER F CB  1 
ATOM   6105  O  OG  . SER F  1 69  ? 11.389  252.412 42.989  1.00 40.45  ? 68  SER F OG  1 
ATOM   6106  N  N   . ARG F  1 70  ? 9.344   248.590 44.458  1.00 34.21  ? 69  ARG F N   1 
ATOM   6107  C  CA  . ARG F  1 70  ? 8.084   247.944 44.539  1.00 32.47  ? 69  ARG F CA  1 
ATOM   6108  C  C   . ARG F  1 70  ? 7.580   247.994 45.977  1.00 32.12  ? 69  ARG F C   1 
ATOM   6109  O  O   . ARG F  1 70  ? 8.277   248.425 46.862  1.00 31.63  ? 69  ARG F O   1 
ATOM   6110  C  CB  . ARG F  1 70  ? 8.247   246.513 44.034  1.00 37.15  ? 69  ARG F CB  1 
ATOM   6111  C  CG  . ARG F  1 70  ? 8.984   246.390 42.718  1.00 39.05  ? 69  ARG F CG  1 
ATOM   6112  C  CD  . ARG F  1 70  ? 8.053   246.630 41.575  1.00 42.40  ? 69  ARG F CD  1 
ATOM   6113  N  NE  . ARG F  1 70  ? 8.687   246.229 40.324  1.00 51.10  ? 69  ARG F NE  1 
ATOM   6114  C  CZ  . ARG F  1 70  ? 8.972   247.038 39.274  1.00 48.60  ? 69  ARG F CZ  1 
ATOM   6115  N  NH1 . ARG F  1 70  ? 8.645   248.325 39.264  1.00 37.80  ? 69  ARG F NH1 1 
ATOM   6116  N  NH2 . ARG F  1 70  ? 9.593   246.528 38.179  1.00 49.65  ? 69  ARG F NH2 1 
ATOM   6117  N  N   . LYS F  1 71  ? 6.353   247.587 46.213  1.00 34.12  ? 70  LYS F N   1 
ATOM   6118  C  CA  . LYS F  1 71  ? 5.932   247.288 47.584  1.00 37.13  ? 70  LYS F CA  1 
ATOM   6119  C  C   . LYS F  1 71  ? 6.497   245.928 48.089  1.00 35.10  ? 70  LYS F C   1 
ATOM   6120  O  O   . LYS F  1 71  ? 6.820   245.022 47.294  1.00 31.00  ? 70  LYS F O   1 
ATOM   6121  C  CB  . LYS F  1 71  ? 4.400   247.284 47.683  1.00 39.33  ? 70  LYS F CB  1 
ATOM   6122  C  CG  . LYS F  1 71  ? 3.849   248.657 47.430  1.00 46.58  ? 70  LYS F CG  1 
ATOM   6123  C  CD  . LYS F  1 71  ? 2.392   248.612 47.035  1.00 56.90  ? 70  LYS F CD  1 
ATOM   6124  C  CE  . LYS F  1 71  ? 1.996   250.098 46.857  1.00 73.91  ? 70  LYS F CE  1 
ATOM   6125  N  NZ  . LYS F  1 71  ? 0.512   250.353 46.768  1.00 79.25  ? 70  LYS F NZ  1 
ATOM   6126  N  N   . HIS F  1 72  ? 6.576   245.817 49.419  1.00 32.43  ? 71  HIS F N   1 
ATOM   6127  C  CA  . HIS F  1 72  ? 6.997   244.626 50.125  1.00 29.32  ? 71  HIS F CA  1 
ATOM   6128  C  C   . HIS F  1 72  ? 6.113   243.430 49.837  1.00 31.24  ? 71  HIS F C   1 
ATOM   6129  O  O   . HIS F  1 72  ? 4.895   243.582 49.882  1.00 38.83  ? 71  HIS F O   1 
ATOM   6130  C  CB  . HIS F  1 72  ? 7.010   244.897 51.627  1.00 27.34  ? 71  HIS F CB  1 
ATOM   6131  C  CG  . HIS F  1 72  ? 7.462   243.721 52.415  1.00 26.07  ? 71  HIS F CG  1 
ATOM   6132  N  ND1 . HIS F  1 72  ? 8.779   243.351 52.491  1.00 25.28  ? 71  HIS F ND1 1 
ATOM   6133  C  CD2 . HIS F  1 72  ? 6.765   242.780 53.079  1.00 24.20  ? 71  HIS F CD2 1 
ATOM   6134  C  CE1 . HIS F  1 72  ? 8.879   242.233 53.175  1.00 26.88  ? 71  HIS F CE1 1 
ATOM   6135  N  NE2 . HIS F  1 72  ? 7.666   241.866 53.532  1.00 28.33  ? 71  HIS F NE2 1 
ATOM   6136  N  N   . GLY F  1 73  ? 6.709   242.271 49.547  1.00 26.33  ? 72  GLY F N   1 
ATOM   6137  C  CA  . GLY F  1 73  ? 5.981   241.065 49.377  1.00 25.46  ? 72  GLY F CA  1 
ATOM   6138  C  C   . GLY F  1 73  ? 6.817   239.901 49.862  1.00 30.03  ? 72  GLY F C   1 
ATOM   6139  O  O   . GLY F  1 73  ? 7.819   240.089 50.544  1.00 29.23  ? 72  GLY F O   1 
ATOM   6140  N  N   . GLY F  1 74  ? 6.372   238.696 49.528  1.00 28.40  ? 73  GLY F N   1 
ATOM   6141  C  CA  . GLY F  1 74  ? 7.049   237.506 49.854  1.00 29.26  ? 73  GLY F CA  1 
ATOM   6142  C  C   . GLY F  1 74  ? 7.872   237.071 48.636  1.00 33.12  ? 73  GLY F C   1 
ATOM   6143  O  O   . GLY F  1 74  ? 7.709   237.593 47.523  1.00 33.87  ? 73  GLY F O   1 
ATOM   6144  N  N   . PRO F  1 75  ? 8.772   236.106 48.826  1.00 33.48  ? 74  PRO F N   1 
ATOM   6145  C  CA  . PRO F  1 75  ? 9.668   235.734 47.708  1.00 33.43  ? 74  PRO F CA  1 
ATOM   6146  C  C   . PRO F  1 75  ? 8.944   235.224 46.496  1.00 32.27  ? 74  PRO F C   1 
ATOM   6147  O  O   . PRO F  1 75  ? 9.398   235.414 45.454  1.00 37.12  ? 74  PRO F O   1 
ATOM   6148  C  CB  . PRO F  1 75  ? 10.588  234.647 48.300  1.00 30.75  ? 74  PRO F CB  1 
ATOM   6149  C  CG  . PRO F  1 75  ? 10.067  234.371 49.674  1.00 33.12  ? 74  PRO F CG  1 
ATOM   6150  C  CD  . PRO F  1 75  ? 9.140   235.476 50.101  1.00 31.09  ? 74  PRO F CD  1 
ATOM   6151  N  N   . LYS F  1 76  ? 7.799   234.610 46.653  1.00 35.19  ? 75  LYS F N   1 
ATOM   6152  C  CA  . LYS F  1 76  ? 7.052   234.050 45.564  1.00 34.93  ? 75  LYS F CA  1 
ATOM   6153  C  C   . LYS F  1 76  ? 6.279   235.114 44.796  1.00 32.92  ? 75  LYS F C   1 
ATOM   6154  O  O   . LYS F  1 76  ? 5.860   234.810 43.750  1.00 34.90  ? 75  LYS F O   1 
ATOM   6155  C  CB  . LYS F  1 76  ? 6.055   233.014 46.118  1.00 35.96  ? 75  LYS F CB  1 
ATOM   6156  C  CG  . LYS F  1 76  ? 6.659   231.682 46.419  1.00 39.21  ? 75  LYS F CG  1 
ATOM   6157  C  CD  . LYS F  1 76  ? 5.856   230.931 47.463  1.00 40.45  ? 75  LYS F CD  1 
ATOM   6158  C  CE  . LYS F  1 76  ? 5.033   229.795 46.850  1.00 44.47  ? 75  LYS F CE  1 
ATOM   6159  N  NZ  . LYS F  1 76  ? 3.761   229.687 47.615  1.00 40.99  ? 75  LYS F NZ  1 
ATOM   6160  N  N   . ASP F  1 77  ? 6.070   236.314 45.339  1.00 30.28  ? 76  ASP F N   1 
ATOM   6161  C  CA  . ASP F  1 77  ? 5.391   237.396 44.640  1.00 30.93  ? 76  ASP F CA  1 
ATOM   6162  C  C   . ASP F  1 77  ? 6.207   238.133 43.576  1.00 35.53  ? 76  ASP F C   1 
ATOM   6163  O  O   . ASP F  1 77  ? 7.421   238.283 43.623  1.00 33.27  ? 76  ASP F O   1 
ATOM   6164  C  CB  . ASP F  1 77  ? 4.885   238.490 45.602  1.00 30.80  ? 76  ASP F CB  1 
ATOM   6165  C  CG  . ASP F  1 77  ? 4.003   237.975 46.659  1.00 34.81  ? 76  ASP F CG  1 
ATOM   6166  O  OD1 . ASP F  1 77  ? 3.133   237.192 46.331  1.00 41.16  ? 76  ASP F OD1 1 
ATOM   6167  O  OD2 . ASP F  1 77  ? 4.162   238.302 47.858  1.00 36.83  ? 76  ASP F OD2 1 
ATOM   6168  N  N   . GLU F  1 78  ? 5.484   238.728 42.662  1.00 39.10  ? 77  GLU F N   1 
ATOM   6169  C  CA  . GLU F  1 78  ? 6.106   239.450 41.656  1.00 39.07  ? 77  GLU F CA  1 
ATOM   6170  C  C   . GLU F  1 78  ? 6.309   240.868 42.165  1.00 34.87  ? 77  GLU F C   1 
ATOM   6171  O  O   . GLU F  1 78  ? 7.403   241.433 41.993  1.00 34.31  ? 77  GLU F O   1 
ATOM   6172  C  CB  . GLU F  1 78  ? 5.296   239.318 40.410  1.00 41.05  ? 77  GLU F CB  1 
ATOM   6173  C  CG  . GLU F  1 78  ? 6.063   239.819 39.222  1.00 60.31  ? 77  GLU F CG  1 
ATOM   6174  C  CD  . GLU F  1 78  ? 5.165   240.045 38.001  1.00 78.44  ? 77  GLU F CD  1 
ATOM   6175  O  OE1 . GLU F  1 78  ? 4.058   239.388 37.860  1.00 73.87  ? 77  GLU F OE1 1 
ATOM   6176  O  OE2 . GLU F  1 78  ? 5.586   240.900 37.170  1.00 70.62  ? 77  GLU F OE2 1 
ATOM   6177  N  N   . GLU F  1 79  ? 5.321   241.392 42.880  1.00 32.06  ? 78  GLU F N   1 
ATOM   6178  C  CA  . GLU F  1 79  ? 5.468   242.651 43.602  1.00 30.11  ? 78  GLU F CA  1 
ATOM   6179  C  C   . GLU F  1 79  ? 6.273   242.344 44.898  1.00 30.57  ? 78  GLU F C   1 
ATOM   6180  O  O   . GLU F  1 79  ? 5.725   241.844 45.847  1.00 30.59  ? 78  GLU F O   1 
ATOM   6181  C  CB  . GLU F  1 79  ? 4.086   243.196 43.936  1.00 27.81  ? 78  GLU F CB  1 
ATOM   6182  C  CG  . GLU F  1 79  ? 4.006   244.634 44.403  1.00 30.98  ? 78  GLU F CG  1 
ATOM   6183  C  CD  . GLU F  1 79  ? 4.611   245.662 43.389  1.00 39.04  ? 78  GLU F CD  1 
ATOM   6184  O  OE1 . GLU F  1 79  ? 4.691   245.371 42.119  1.00 42.48  ? 78  GLU F OE1 1 
ATOM   6185  O  OE2 . GLU F  1 79  ? 4.978   246.798 43.855  1.00 33.72  ? 78  GLU F OE2 1 
ATOM   6186  N  N   . ARG F  1 80  ? 7.562   242.641 44.901  1.00 30.24  ? 79  ARG F N   1 
ATOM   6187  C  CA  . ARG F  1 80  ? 8.443   242.446 46.057  1.00 31.84  ? 79  ARG F CA  1 
ATOM   6188  C  C   . ARG F  1 80  ? 9.661   243.341 45.900  1.00 33.17  ? 79  ARG F C   1 
ATOM   6189  O  O   . ARG F  1 80  ? 9.981   243.770 44.816  1.00 32.89  ? 79  ARG F O   1 
ATOM   6190  C  CB  . ARG F  1 80  ? 8.868   240.985 46.239  1.00 30.35  ? 79  ARG F CB  1 
ATOM   6191  C  CG  . ARG F  1 80  ? 9.552   240.377 45.016  1.00 27.69  ? 79  ARG F CG  1 
ATOM   6192  C  CD  . ARG F  1 80  ? 10.100  238.992 45.283  1.00 28.88  ? 79  ARG F CD  1 
ATOM   6193  N  NE  . ARG F  1 80  ? 11.459  239.111 45.805  1.00 32.03  ? 79  ARG F NE  1 
ATOM   6194  C  CZ  . ARG F  1 80  ? 12.337  238.110 45.919  1.00 31.76  ? 79  ARG F CZ  1 
ATOM   6195  N  NH1 . ARG F  1 80  ? 12.032  236.852 45.550  1.00 28.90  ? 79  ARG F NH1 1 
ATOM   6196  N  NH2 . ARG F  1 80  ? 13.555  238.386 46.348  1.00 27.41  ? 79  ARG F NH2 1 
ATOM   6197  N  N   . HIS F  1 81  ? 10.311  243.639 47.007  1.00 31.89  ? 80  HIS F N   1 
ATOM   6198  C  CA  . HIS F  1 81  ? 11.621  244.220 47.029  1.00 28.53  ? 80  HIS F CA  1 
ATOM   6199  C  C   . HIS F  1 81  ? 12.608  243.169 46.573  1.00 28.77  ? 80  HIS F C   1 
ATOM   6200  O  O   . HIS F  1 81  ? 12.358  241.958 46.807  1.00 29.33  ? 80  HIS F O   1 
ATOM   6201  C  CB  . HIS F  1 81  ? 11.908  244.592 48.485  1.00 25.88  ? 80  HIS F CB  1 
ATOM   6202  C  CG  . HIS F  1 81  ? 10.987  245.632 49.035  1.00 28.25  ? 80  HIS F CG  1 
ATOM   6203  N  ND1 . HIS F  1 81  ? 10.731  245.775 50.381  1.00 31.06  ? 80  HIS F ND1 1 
ATOM   6204  C  CD2 . HIS F  1 81  ? 10.230  246.570 48.413  1.00 29.64  ? 80  HIS F CD2 1 
ATOM   6205  C  CE1 . HIS F  1 81  ? 9.896   246.771 50.570  1.00 28.82  ? 80  HIS F CE1 1 
ATOM   6206  N  NE2 . HIS F  1 81  ? 9.605   247.289 49.392  1.00 29.74  ? 80  HIS F NE2 1 
ATOM   6207  N  N   . VAL F  1 82  ? 13.732  243.578 45.974  1.00 27.17  ? 81  VAL F N   1 
ATOM   6208  C  CA  . VAL F  1 82  ? 14.718  242.561 45.587  1.00 28.34  ? 81  VAL F CA  1 
ATOM   6209  C  C   . VAL F  1 82  ? 15.185  241.774 46.816  1.00 28.17  ? 81  VAL F C   1 
ATOM   6210  O  O   . VAL F  1 82  ? 15.409  240.608 46.702  1.00 28.87  ? 81  VAL F O   1 
ATOM   6211  C  CB  . VAL F  1 82  ? 15.943  243.085 44.768  1.00 29.03  ? 81  VAL F CB  1 
ATOM   6212  C  CG1 . VAL F  1 82  ? 17.104  242.031 44.786  1.00 27.96  ? 81  VAL F CG1 1 
ATOM   6213  C  CG2 . VAL F  1 82  ? 15.544  243.462 43.344  1.00 24.80  ? 81  VAL F CG2 1 
ATOM   6214  N  N   . GLY F  1 83  ? 15.262  242.420 47.982  1.00 29.64  ? 82  GLY F N   1 
ATOM   6215  C  CA  . GLY F  1 83  ? 15.724  241.806 49.226  1.00 31.79  ? 82  GLY F CA  1 
ATOM   6216  C  C   . GLY F  1 83  ? 14.720  241.024 50.099  1.00 30.92  ? 82  GLY F C   1 
ATOM   6217  O  O   . GLY F  1 83  ? 15.069  240.587 51.206  1.00 31.41  ? 82  GLY F O   1 
ATOM   6218  N  N   . ASP F  1 84  ? 13.498  240.849 49.616  1.00 28.31  ? 83  ASP F N   1 
ATOM   6219  C  CA  . ASP F  1 84  ? 12.463  240.096 50.283  1.00 28.38  ? 83  ASP F CA  1 
ATOM   6220  C  C   . ASP F  1 84  ? 12.661  238.574 50.232  1.00 29.34  ? 83  ASP F C   1 
ATOM   6221  O  O   . ASP F  1 84  ? 12.134  237.906 49.357  1.00 32.07  ? 83  ASP F O   1 
ATOM   6222  C  CB  . ASP F  1 84  ? 11.107  240.463 49.662  1.00 30.62  ? 83  ASP F CB  1 
ATOM   6223  C  CG  . ASP F  1 84  ? 10.620  241.812 50.108  1.00 33.92  ? 83  ASP F CG  1 
ATOM   6224  O  OD1 . ASP F  1 84  ? 11.239  242.364 51.020  1.00 31.25  ? 83  ASP F OD1 1 
ATOM   6225  O  OD2 . ASP F  1 84  ? 9.602   242.340 49.592  1.00 39.18  ? 83  ASP F OD2 1 
ATOM   6226  N  N   . LEU F  1 85  ? 13.358  238.011 51.195  1.00 29.73  ? 84  LEU F N   1 
ATOM   6227  C  CA  . LEU F  1 85  ? 13.578  236.622 51.197  1.00 27.57  ? 84  LEU F CA  1 
ATOM   6228  C  C   . LEU F  1 85  ? 12.605  235.927 52.109  1.00 29.04  ? 84  LEU F C   1 
ATOM   6229  O  O   . LEU F  1 85  ? 12.729  234.753 52.270  1.00 31.94  ? 84  LEU F O   1 
ATOM   6230  C  CB  . LEU F  1 85  ? 15.040  236.322 51.520  1.00 27.15  ? 84  LEU F CB  1 
ATOM   6231  C  CG  . LEU F  1 85  ? 16.127  236.793 50.524  1.00 25.68  ? 84  LEU F CG  1 
ATOM   6232  C  CD1 . LEU F  1 85  ? 17.453  236.364 51.052  1.00 23.72  ? 84  LEU F CD1 1 
ATOM   6233  C  CD2 . LEU F  1 85  ? 15.892  236.291 49.087  1.00 24.08  ? 84  LEU F CD2 1 
ATOM   6234  N  N   . GLY F  1 86  ? 11.590  236.624 52.647  1.00 29.54  ? 85  GLY F N   1 
ATOM   6235  C  CA  . GLY F  1 86  ? 10.504  235.969 53.430  1.00 28.72  ? 85  GLY F CA  1 
ATOM   6236  C  C   . GLY F  1 86  ? 10.856  235.712 54.877  1.00 30.45  ? 85  GLY F C   1 
ATOM   6237  O  O   . GLY F  1 86  ? 11.478  236.545 55.551  1.00 32.42  ? 85  GLY F O   1 
ATOM   6238  N  N   . ASN F  1 87  ? 10.472  234.549 55.372  1.00 30.82  ? 86  ASN F N   1 
ATOM   6239  C  CA  . ASN F  1 87  ? 10.846  234.099 56.712  1.00 28.02  ? 86  ASN F CA  1 
ATOM   6240  C  C   . ASN F  1 87  ? 11.841  232.940 56.734  1.00 27.10  ? 86  ASN F C   1 
ATOM   6241  O  O   . ASN F  1 87  ? 11.886  232.158 55.788  1.00 28.17  ? 86  ASN F O   1 
ATOM   6242  C  CB  . ASN F  1 87  ? 9.606   233.663 57.411  1.00 25.42  ? 86  ASN F CB  1 
ATOM   6243  C  CG  . ASN F  1 87  ? 8.672   234.794 57.638  1.00 27.88  ? 86  ASN F CG  1 
ATOM   6244  O  OD1 . ASN F  1 87  ? 8.938   235.673 58.428  1.00 29.30  ? 86  ASN F OD1 1 
ATOM   6245  N  ND2 . ASN F  1 87  ? 7.558   234.760 56.988  1.00 27.12  ? 86  ASN F ND2 1 
ATOM   6246  N  N   . VAL F  1 88  ? 12.580  232.836 57.830  1.00 24.12  ? 87  VAL F N   1 
ATOM   6247  C  CA  . VAL F  1 88  ? 13.274  231.651 58.243  1.00 23.76  ? 87  VAL F CA  1 
ATOM   6248  C  C   . VAL F  1 88  ? 12.633  231.107 59.566  1.00 28.15  ? 87  VAL F C   1 
ATOM   6249  O  O   . VAL F  1 88  ? 12.044  231.862 60.348  1.00 26.88  ? 87  VAL F O   1 
ATOM   6250  C  CB  . VAL F  1 88  ? 14.807  231.924 58.361  1.00 23.77  ? 87  VAL F CB  1 
ATOM   6251  C  CG1 . VAL F  1 88  ? 15.460  232.294 57.011  1.00 20.45  ? 87  VAL F CG1 1 
ATOM   6252  C  CG2 . VAL F  1 88  ? 15.132  232.961 59.466  1.00 21.91  ? 87  VAL F CG2 1 
ATOM   6253  N  N   . THR F  1 89  ? 12.708  229.796 59.797  1.00 28.56  ? 88  THR F N   1 
ATOM   6254  C  CA  . THR F  1 89  ? 12.049  229.186 60.935  1.00 28.88  ? 88  THR F CA  1 
ATOM   6255  C  C   . THR F  1 89  ? 13.047  228.694 61.977  1.00 29.14  ? 88  THR F C   1 
ATOM   6256  O  O   . THR F  1 89  ? 13.958  227.956 61.665  1.00 29.21  ? 88  THR F O   1 
ATOM   6257  C  CB  . THR F  1 89  ? 11.085  228.058 60.432  1.00 27.89  ? 88  THR F CB  1 
ATOM   6258  O  OG1 . THR F  1 89  ? 9.967   228.671 59.846  1.00 29.26  ? 88  THR F OG1 1 
ATOM   6259  C  CG2 . THR F  1 89  ? 10.515  227.169 61.523  1.00 24.80  ? 88  THR F CG2 1 
ATOM   6260  N  N   . ALA F  1 90  ? 12.870  229.087 63.226  1.00 32.12  ? 89  ALA F N   1 
ATOM   6261  C  CA  . ALA F  1 90  ? 13.722  228.571 64.310  1.00 30.94  ? 89  ALA F CA  1 
ATOM   6262  C  C   . ALA F  1 90  ? 12.942  227.486 65.000  1.00 31.27  ? 89  ALA F C   1 
ATOM   6263  O  O   . ALA F  1 90  ? 11.729  227.604 65.232  1.00 33.79  ? 89  ALA F O   1 
ATOM   6264  C  CB  . ALA F  1 90  ? 14.172  229.648 65.280  1.00 27.22  ? 89  ALA F CB  1 
ATOM   6265  N  N   . ASP F  1 91  ? 13.657  226.401 65.258  1.00 32.97  ? 90  ASP F N   1 
ATOM   6266  C  CA  . ASP F  1 91  ? 13.133  225.239 65.949  1.00 34.84  ? 90  ASP F CA  1 
ATOM   6267  C  C   . ASP F  1 91  ? 13.047  225.506 67.451  1.00 36.18  ? 90  ASP F C   1 
ATOM   6268  O  O   . ASP F  1 91  ? 13.403  226.580 67.919  1.00 35.65  ? 90  ASP F O   1 
ATOM   6269  C  CB  . ASP F  1 91  ? 13.937  223.988 65.573  1.00 31.85  ? 90  ASP F CB  1 
ATOM   6270  C  CG  . ASP F  1 91  ? 15.343  223.945 66.169  1.00 34.48  ? 90  ASP F CG  1 
ATOM   6271  O  OD1 . ASP F  1 91  ? 15.693  224.692 67.152  1.00 34.45  ? 90  ASP F OD1 1 
ATOM   6272  O  OD2 . ASP F  1 91  ? 16.122  223.107 65.613  1.00 33.74  ? 90  ASP F OD2 1 
ATOM   6273  N  N   . LYS F  1 92  ? 12.607  224.526 68.214  1.00 41.41  ? 91  LYS F N   1 
ATOM   6274  C  CA  . LYS F  1 92  ? 12.427  224.750 69.652  1.00 40.39  ? 91  LYS F CA  1 
ATOM   6275  C  C   . LYS F  1 92  ? 13.746  224.993 70.365  1.00 37.01  ? 91  LYS F C   1 
ATOM   6276  O  O   . LYS F  1 92  ? 13.733  225.499 71.441  1.00 37.88  ? 91  LYS F O   1 
ATOM   6277  C  CB  . LYS F  1 92  ? 11.620  223.609 70.297  1.00 42.23  ? 91  LYS F CB  1 
ATOM   6278  C  CG  . LYS F  1 92  ? 12.420  222.307 70.436  1.00 49.43  ? 91  LYS F CG  1 
ATOM   6279  C  CD  . LYS F  1 92  ? 11.572  221.022 70.539  1.00 50.61  ? 91  LYS F CD  1 
ATOM   6280  C  CE  . LYS F  1 92  ? 12.492  219.834 70.805  1.00 56.30  ? 91  LYS F CE  1 
ATOM   6281  N  NZ  . LYS F  1 92  ? 11.807  218.874 71.761  1.00 65.08  ? 91  LYS F NZ  1 
ATOM   6282  N  N   . ASP F  1 93  ? 14.892  224.669 69.778  1.00 37.06  ? 92  ASP F N   1 
ATOM   6283  C  CA  . ASP F  1 93  ? 16.181  225.013 70.427  1.00 35.90  ? 92  ASP F CA  1 
ATOM   6284  C  C   . ASP F  1 93  ? 16.745  226.377 70.014  1.00 35.46  ? 92  ASP F C   1 
ATOM   6285  O  O   . ASP F  1 93  ? 17.900  226.629 70.295  1.00 31.96  ? 92  ASP F O   1 
ATOM   6286  C  CB  . ASP F  1 93  ? 17.260  223.968 70.109  1.00 39.70  ? 92  ASP F CB  1 
ATOM   6287  C  CG  . ASP F  1 93  ? 16.912  222.529 70.591  1.00 46.39  ? 92  ASP F CG  1 
ATOM   6288  O  OD1 . ASP F  1 93  ? 16.252  222.313 71.647  1.00 43.43  ? 92  ASP F OD1 1 
ATOM   6289  O  OD2 . ASP F  1 93  ? 17.362  221.583 69.903  1.00 44.62  ? 92  ASP F OD2 1 
ATOM   6290  N  N   . GLY F  1 94  ? 15.951  227.214 69.312  1.00 34.18  ? 93  GLY F N   1 
ATOM   6291  C  CA  . GLY F  1 94  ? 16.367  228.502 68.792  1.00 33.94  ? 93  GLY F CA  1 
ATOM   6292  C  C   . GLY F  1 94  ? 17.236  228.519 67.526  1.00 34.78  ? 93  GLY F C   1 
ATOM   6293  O  O   . GLY F  1 94  ? 17.874  229.543 67.254  1.00 32.29  ? 93  GLY F O   1 
ATOM   6294  N  N   . VAL F  1 95  ? 17.228  227.410 66.764  1.00 34.54  ? 94  VAL F N   1 
ATOM   6295  C  CA  . VAL F  1 95  ? 18.103  227.211 65.620  1.00 33.06  ? 94  VAL F CA  1 
ATOM   6296  C  C   . VAL F  1 95  ? 17.305  227.244 64.325  1.00 32.12  ? 94  VAL F C   1 
ATOM   6297  O  O   . VAL F  1 95  ? 16.333  226.525 64.169  1.00 33.86  ? 94  VAL F O   1 
ATOM   6298  C  CB  . VAL F  1 95  ? 18.872  225.894 65.690  1.00 34.78  ? 94  VAL F CB  1 
ATOM   6299  C  CG1 . VAL F  1 95  ? 19.696  225.733 64.417  1.00 36.75  ? 94  VAL F CG1 1 
ATOM   6300  C  CG2 . VAL F  1 95  ? 19.787  225.835 66.921  1.00 28.15  ? 94  VAL F CG2 1 
ATOM   6301  N  N   . ALA F  1 96  ? 17.689  228.157 63.443  1.00 32.18  ? 95  ALA F N   1 
ATOM   6302  C  CA  . ALA F  1 96  ? 17.190  228.210 62.060  1.00 32.73  ? 95  ALA F CA  1 
ATOM   6303  C  C   . ALA F  1 96  ? 18.192  227.608 61.091  1.00 31.80  ? 95  ALA F C   1 
ATOM   6304  O  O   . ALA F  1 96  ? 19.275  228.133 60.902  1.00 32.27  ? 95  ALA F O   1 
ATOM   6305  C  CB  . ALA F  1 96  ? 16.841  229.611 61.644  1.00 31.16  ? 95  ALA F CB  1 
ATOM   6306  N  N   . ASP F  1 97  ? 17.796  226.497 60.493  1.00 30.73  ? 96  ASP F N   1 
ATOM   6307  C  CA  . ASP F  1 97  ? 18.577  225.846 59.507  1.00 30.86  ? 96  ASP F CA  1 
ATOM   6308  C  C   . ASP F  1 97  ? 18.119  226.340 58.174  1.00 28.69  ? 96  ASP F C   1 
ATOM   6309  O  O   . ASP F  1 97  ? 17.266  225.728 57.516  1.00 29.65  ? 96  ASP F O   1 
ATOM   6310  C  CB  . ASP F  1 97  ? 18.462  224.320 59.700  1.00 30.99  ? 96  ASP F CB  1 
ATOM   6311  C  CG  . ASP F  1 97  ? 19.346  223.825 60.872  1.00 38.91  ? 96  ASP F CG  1 
ATOM   6312  O  OD1 . ASP F  1 97  ? 20.542  224.284 61.027  1.00 43.05  ? 96  ASP F OD1 1 
ATOM   6313  O  OD2 . ASP F  1 97  ? 18.856  222.987 61.678  1.00 41.36  ? 96  ASP F OD2 1 
ATOM   6314  N  N   . VAL F  1 98  ? 18.656  227.487 57.797  1.00 29.19  ? 97  VAL F N   1 
ATOM   6315  C  CA  . VAL F  1 98  ? 18.138  228.185 56.640  1.00 29.19  ? 97  VAL F CA  1 
ATOM   6316  C  C   . VAL F  1 98  ? 18.380  227.423 55.368  1.00 30.37  ? 97  VAL F C   1 
ATOM   6317  O  O   . VAL F  1 98  ? 19.469  226.873 55.141  1.00 30.56  ? 97  VAL F O   1 
ATOM   6318  C  CB  . VAL F  1 98  ? 18.742  229.572 56.497  1.00 28.00  ? 97  VAL F CB  1 
ATOM   6319  C  CG1 . VAL F  1 98  ? 18.201  230.297 55.256  1.00 23.32  ? 97  VAL F CG1 1 
ATOM   6320  C  CG2 . VAL F  1 98  ? 18.497  230.390 57.752  1.00 22.61  ? 97  VAL F CG2 1 
ATOM   6321  N  N   . SER F  1 99  ? 17.354  227.397 54.535  1.00 30.11  ? 98  SER F N   1 
ATOM   6322  C  CA  . SER F  1 99  ? 17.520  226.819 53.225  1.00 34.50  ? 98  SER F CA  1 
ATOM   6323  C  C   . SER F  1 99  ? 16.531  227.407 52.238  1.00 34.64  ? 98  SER F C   1 
ATOM   6324  O  O   . SER F  1 99  ? 15.381  227.040 52.238  1.00 33.23  ? 98  SER F O   1 
ATOM   6325  C  CB  . SER F  1 99  ? 17.384  225.305 53.295  1.00 34.10  ? 98  SER F CB  1 
ATOM   6326  O  OG  . SER F  1 99  ? 17.293  224.787 51.995  1.00 37.43  ? 98  SER F OG  1 
ATOM   6327  N  N   . ILE F  1 100 ? 16.990  228.341 51.425  1.00 34.42  ? 99  ILE F N   1 
ATOM   6328  C  CA  . ILE F  1 100 ? 16.122  229.134 50.564  1.00 32.41  ? 99  ILE F CA  1 
ATOM   6329  C  C   . ILE F  1 100 ? 16.707  229.142 49.177  1.00 33.79  ? 99  ILE F C   1 
ATOM   6330  O  O   . ILE F  1 100 ? 17.911  229.150 49.014  1.00 33.36  ? 99  ILE F O   1 
ATOM   6331  C  CB  . ILE F  1 100 ? 16.091  230.582 51.090  1.00 33.54  ? 99  ILE F CB  1 
ATOM   6332  C  CG1 . ILE F  1 100 ? 15.116  230.658 52.268  1.00 36.85  ? 99  ILE F CG1 1 
ATOM   6333  C  CG2 . ILE F  1 100 ? 15.664  231.616 50.030  1.00 30.24  ? 99  ILE F CG2 1 
ATOM   6334  C  CD1 . ILE F  1 100 ? 15.367  231.851 53.165  1.00 32.67  ? 99  ILE F CD1 1 
ATOM   6335  N  N   . GLU F  1 101 ? 15.880  229.207 48.156  1.00 36.38  ? 100 GLU F N   1 
ATOM   6336  C  CA  . GLU F  1 101 ? 16.395  229.426 46.816  1.00 34.63  ? 100 GLU F CA  1 
ATOM   6337  C  C   . GLU F  1 101 ? 15.649  230.579 46.189  1.00 29.28  ? 100 GLU F C   1 
ATOM   6338  O  O   . GLU F  1 101 ? 14.493  230.589 46.246  1.00 28.20  ? 100 GLU F O   1 
ATOM   6339  C  CB  . GLU F  1 101 ? 16.149  228.198 46.024  1.00 36.92  ? 100 GLU F CB  1 
ATOM   6340  C  CG  . GLU F  1 101 ? 17.213  227.871 44.997  1.00 52.54  ? 100 GLU F CG  1 
ATOM   6341  C  CD  . GLU F  1 101 ? 16.739  226.748 44.061  1.00 54.80  ? 100 GLU F CD  1 
ATOM   6342  O  OE1 . GLU F  1 101 ? 16.944  225.541 44.383  1.00 55.49  ? 100 GLU F OE1 1 
ATOM   6343  O  OE2 . GLU F  1 101 ? 16.053  227.108 43.078  1.00 47.45  ? 100 GLU F OE2 1 
ATOM   6344  N  N   . ASP F  1 102 ? 16.341  231.563 45.633  1.00 29.57  ? 101 ASP F N   1 
ATOM   6345  C  CA  . ASP F  1 102 ? 15.709  232.750 45.159  1.00 29.78  ? 101 ASP F CA  1 
ATOM   6346  C  C   . ASP F  1 102 ? 16.244  233.176 43.819  1.00 30.11  ? 101 ASP F C   1 
ATOM   6347  O  O   . ASP F  1 102 ? 17.400  233.151 43.619  1.00 31.17  ? 101 ASP F O   1 
ATOM   6348  C  CB  . ASP F  1 102 ? 15.955  233.900 46.116  1.00 30.09  ? 101 ASP F CB  1 
ATOM   6349  C  CG  . ASP F  1 102 ? 15.004  235.017 45.841  1.00 29.49  ? 101 ASP F CG  1 
ATOM   6350  O  OD1 . ASP F  1 102 ? 13.813  234.822 46.026  1.00 31.44  ? 101 ASP F OD1 1 
ATOM   6351  O  OD2 . ASP F  1 102 ? 15.404  236.045 45.309  1.00 31.98  ? 101 ASP F OD2 1 
ATOM   6352  N  N   A SER F  1 103 ? 15.401  233.561 42.885  0.50 30.27  ? 102 SER F N   1 
ATOM   6353  N  N   B SER F  1 103 ? 15.395  233.585 42.907  0.50 30.29  ? 102 SER F N   1 
ATOM   6354  C  CA  A SER F  1 103 ? 15.962  233.968 41.601  0.50 33.58  ? 102 SER F CA  1 
ATOM   6355  C  CA  B SER F  1 103 ? 15.909  233.951 41.598  0.50 33.73  ? 102 SER F CA  1 
ATOM   6356  C  C   A SER F  1 103 ? 15.830  235.443 41.334  0.50 34.63  ? 102 SER F C   1 
ATOM   6357  C  C   B SER F  1 103 ? 15.836  235.436 41.339  0.50 34.71  ? 102 SER F C   1 
ATOM   6358  O  O   A SER F  1 103 ? 15.968  235.833 40.191  0.50 31.83  ? 102 SER F O   1 
ATOM   6359  O  O   B SER F  1 103 ? 16.018  235.825 40.200  0.50 31.77  ? 102 SER F O   1 
ATOM   6360  C  CB  A SER F  1 103 ? 15.392  233.179 40.428  0.50 32.75  ? 102 SER F CB  1 
ATOM   6361  C  CB  B SER F  1 103 ? 15.163  233.219 40.502  0.50 33.24  ? 102 SER F CB  1 
ATOM   6362  O  OG  A SER F  1 103 ? 15.388  231.803 40.745  0.50 35.97  ? 102 SER F OG  1 
ATOM   6363  O  OG  B SER F  1 103 ? 13.809  233.110 40.891  0.50 36.35  ? 102 SER F OG  1 
ATOM   6364  N  N   . VAL F  1 104 ? 15.579  236.243 42.386  1.00 35.08  ? 103 VAL F N   1 
ATOM   6365  C  CA  . VAL F  1 104 ? 15.550  237.683 42.263  1.00 31.42  ? 103 VAL F CA  1 
ATOM   6366  C  C   . VAL F  1 104 ? 16.774  238.337 42.805  1.00 31.90  ? 103 VAL F C   1 
ATOM   6367  O  O   . VAL F  1 104 ? 17.262  239.212 42.130  1.00 32.96  ? 103 VAL F O   1 
ATOM   6368  C  CB  . VAL F  1 104 ? 14.251  238.336 42.794  1.00 32.61  ? 103 VAL F CB  1 
ATOM   6369  C  CG1 . VAL F  1 104 ? 14.296  239.900 42.754  1.00 26.55  ? 103 VAL F CG1 1 
ATOM   6370  C  CG2 . VAL F  1 104 ? 13.085  237.794 41.988  1.00 29.26  ? 103 VAL F CG2 1 
ATOM   6371  N  N   . ILE F  1 105 ? 17.228  237.994 44.021  1.00 32.67  ? 104 ILE F N   1 
ATOM   6372  C  CA  . ILE F  1 105 ? 18.571  238.403 44.455  1.00 31.16  ? 104 ILE F CA  1 
ATOM   6373  C  C   . ILE F  1 105 ? 19.617  237.836 43.465  1.00 30.08  ? 104 ILE F C   1 
ATOM   6374  O  O   . ILE F  1 105 ? 19.321  236.896 42.730  1.00 29.11  ? 104 ILE F O   1 
ATOM   6375  C  CB  . ILE F  1 105 ? 18.898  237.917 45.866  1.00 31.29  ? 104 ILE F CB  1 
ATOM   6376  C  CG1 . ILE F  1 105 ? 18.781  236.355 45.984  1.00 28.12  ? 104 ILE F CG1 1 
ATOM   6377  C  CG2 . ILE F  1 105 ? 18.121  238.750 46.873  1.00 26.26  ? 104 ILE F CG2 1 
ATOM   6378  C  CD1 . ILE F  1 105 ? 19.517  235.802 47.187  1.00 25.99  ? 104 ILE F CD1 1 
ATOM   6379  N  N   . SER F  1 106 ? 20.822  238.385 43.450  1.00 29.49  ? 105 SER F N   1 
ATOM   6380  C  CA  . SER F  1 106 ? 21.891  237.866 42.584  1.00 30.25  ? 105 SER F CA  1 
ATOM   6381  C  C   . SER F  1 106 ? 23.224  238.224 43.191  1.00 31.38  ? 105 SER F C   1 
ATOM   6382  O  O   . SER F  1 106 ? 23.320  239.173 43.970  1.00 32.78  ? 105 SER F O   1 
ATOM   6383  C  CB  . SER F  1 106 ? 21.776  238.455 41.164  1.00 30.32  ? 105 SER F CB  1 
ATOM   6384  O  OG  . SER F  1 106 ? 22.716  237.946 40.249  1.00 30.49  ? 105 SER F OG  1 
ATOM   6385  N  N   . LEU F  1 107 ? 24.270  237.500 42.801  1.00 33.87  ? 106 LEU F N   1 
ATOM   6386  C  CA  . LEU F  1 107 ? 25.604  237.901 43.189  1.00 32.76  ? 106 LEU F CA  1 
ATOM   6387  C  C   . LEU F  1 107 ? 26.305  238.753 42.140  1.00 32.95  ? 106 LEU F C   1 
ATOM   6388  O  O   . LEU F  1 107 ? 27.517  238.871 42.186  1.00 33.00  ? 106 LEU F O   1 
ATOM   6389  C  CB  . LEU F  1 107 ? 26.480  236.703 43.583  1.00 30.65  ? 106 LEU F CB  1 
ATOM   6390  C  CG  . LEU F  1 107 ? 25.842  235.812 44.649  1.00 29.71  ? 106 LEU F CG  1 
ATOM   6391  C  CD1 . LEU F  1 107 ? 26.712  234.621 44.991  1.00 26.49  ? 106 LEU F CD1 1 
ATOM   6392  C  CD2 . LEU F  1 107 ? 25.568  236.653 45.859  1.00 28.60  ? 106 LEU F CD2 1 
ATOM   6393  N  N   . SER F  1 108 ? 25.583  239.289 41.178  1.00 32.50  ? 107 SER F N   1 
ATOM   6394  C  CA  . SER F  1 108 ? 26.206  240.249 40.230  1.00 38.49  ? 107 SER F CA  1 
ATOM   6395  C  C   . SER F  1 108 ? 25.119  241.060 39.606  1.00 37.65  ? 107 SER F C   1 
ATOM   6396  O  O   . SER F  1 108 ? 23.947  240.752 39.819  1.00 41.45  ? 107 SER F O   1 
ATOM   6397  C  CB  . SER F  1 108 ? 27.055  239.562 39.162  1.00 38.85  ? 107 SER F CB  1 
ATOM   6398  O  OG  . SER F  1 108 ? 26.263  238.712 38.376  1.00 40.26  ? 107 SER F OG  1 
ATOM   6399  N  N   . GLY F  1 109 ? 25.483  242.108 38.889  1.00 35.90  ? 108 GLY F N   1 
ATOM   6400  C  CA  . GLY F  1 109 ? 24.494  242.948 38.205  1.00 33.44  ? 108 GLY F CA  1 
ATOM   6401  C  C   . GLY F  1 109 ? 23.734  243.874 39.154  1.00 33.66  ? 108 GLY F C   1 
ATOM   6402  O  O   . GLY F  1 109 ? 24.173  244.169 40.220  1.00 33.30  ? 108 GLY F O   1 
ATOM   6403  N  N   . ASP F  1 110 ? 22.566  244.297 38.728  1.00 35.58  ? 109 ASP F N   1 
ATOM   6404  C  CA  . ASP F  1 110 ? 21.726  245.310 39.336  1.00 36.91  ? 109 ASP F CA  1 
ATOM   6405  C  C   . ASP F  1 110 ? 21.152  244.763 40.616  1.00 35.86  ? 109 ASP F C   1 
ATOM   6406  O  O   . ASP F  1 110 ? 20.841  245.519 41.475  1.00 35.99  ? 109 ASP F O   1 
ATOM   6407  C  CB  . ASP F  1 110 ? 20.459  245.534 38.427  1.00 40.96  ? 109 ASP F CB  1 
ATOM   6408  C  CG  . ASP F  1 110 ? 20.729  246.312 37.161  1.00 43.06  ? 109 ASP F CG  1 
ATOM   6409  O  OD1 . ASP F  1 110 ? 21.809  246.905 37.140  1.00 51.67  ? 109 ASP F OD1 1 
ATOM   6410  O  OD2 . ASP F  1 110 ? 19.849  246.352 36.215  1.00 46.17  ? 109 ASP F OD2 1 
ATOM   6411  N  N   . HIS F  1 111 ? 20.836  243.477 40.652  1.00 33.57  ? 110 HIS F N   1 
ATOM   6412  C  CA  . HIS F  1 111 ? 20.275  242.866 41.812  1.00 31.81  ? 110 HIS F CA  1 
ATOM   6413  C  C   . HIS F  1 111 ? 21.314  242.301 42.737  1.00 34.61  ? 110 HIS F C   1 
ATOM   6414  O  O   . HIS F  1 111 ? 20.947  241.610 43.695  1.00 36.39  ? 110 HIS F O   1 
ATOM   6415  C  CB  . HIS F  1 111 ? 19.205  241.863 41.447  1.00 31.56  ? 110 HIS F CB  1 
ATOM   6416  C  CG  . HIS F  1 111 ? 18.056  242.518 40.761  1.00 35.41  ? 110 HIS F CG  1 
ATOM   6417  N  ND1 . HIS F  1 111 ? 16.916  241.844 40.390  1.00 32.33  ? 110 HIS F ND1 1 
ATOM   6418  C  CD2 . HIS F  1 111 ? 17.903  243.801 40.346  1.00 32.12  ? 110 HIS F CD2 1 
ATOM   6419  C  CE1 . HIS F  1 111 ? 16.108  242.692 39.795  1.00 34.17  ? 110 HIS F CE1 1 
ATOM   6420  N  NE2 . HIS F  1 111 ? 16.679  243.885 39.773  1.00 34.12  ? 110 HIS F NE2 1 
ATOM   6421  N  N   . CYS F  1 112 ? 22.576  242.656 42.501  1.00 31.71  ? 111 CYS F N   1 
ATOM   6422  C  CA  . CYS F  1 112 ? 23.645  242.277 43.387  1.00 34.62  ? 111 CYS F CA  1 
ATOM   6423  C  C   . CYS F  1 112 ? 23.496  242.653 44.864  1.00 31.42  ? 111 CYS F C   1 
ATOM   6424  O  O   . CYS F  1 112 ? 23.309  243.817 45.189  1.00 32.96  ? 111 CYS F O   1 
ATOM   6425  C  CB  . CYS F  1 112 ? 24.989  242.785 42.901  1.00 29.96  ? 111 CYS F CB  1 
ATOM   6426  S  SG  . CYS F  1 112 ? 26.361  241.739 43.629  1.00 39.50  ? 111 CYS F SG  1 
ATOM   6427  N  N   . ILE F  1 113 ? 23.626  241.649 45.722  1.00 28.01  ? 112 ILE F N   1 
ATOM   6428  C  CA  . ILE F  1 113 ? 23.541  241.844 47.149  1.00 29.39  ? 112 ILE F CA  1 
ATOM   6429  C  C   . ILE F  1 113 ? 24.911  241.813 47.859  1.00 31.35  ? 112 ILE F C   1 
ATOM   6430  O  O   . ILE F  1 113 ? 24.954  241.905 49.070  1.00 30.69  ? 112 ILE F O   1 
ATOM   6431  C  CB  . ILE F  1 113 ? 22.586  240.797 47.756  1.00 27.98  ? 112 ILE F CB  1 
ATOM   6432  C  CG1 . ILE F  1 113 ? 23.019  239.392 47.379  1.00 28.24  ? 112 ILE F CG1 1 
ATOM   6433  C  CG2 . ILE F  1 113 ? 21.176  241.051 47.263  1.00 25.35  ? 112 ILE F CG2 1 
ATOM   6434  C  CD1 . ILE F  1 113 ? 22.299  238.316 48.185  1.00 31.51  ? 112 ILE F CD1 1 
ATOM   6435  N  N   . ILE F  1 114 ? 26.018  241.608 47.122  1.00 32.18  ? 113 ILE F N   1 
ATOM   6436  C  CA  . ILE F  1 114 ? 27.374  241.619 47.697  1.00 34.59  ? 113 ILE F CA  1 
ATOM   6437  C  C   . ILE F  1 114 ? 27.530  243.069 48.168  1.00 34.00  ? 113 ILE F C   1 
ATOM   6438  O  O   . ILE F  1 114 ? 27.161  243.969 47.441  1.00 35.09  ? 113 ILE F O   1 
ATOM   6439  C  CB  . ILE F  1 114 ? 28.506  241.349 46.662  1.00 37.59  ? 113 ILE F CB  1 
ATOM   6440  C  CG1 . ILE F  1 114 ? 28.359  239.998 45.888  1.00 37.25  ? 113 ILE F CG1 1 
ATOM   6441  C  CG2 . ILE F  1 114 ? 29.861  241.579 47.256  1.00 31.52  ? 113 ILE F CG2 1 
ATOM   6442  C  CD1 . ILE F  1 114 ? 28.850  238.766 46.505  1.00 33.40  ? 113 ILE F CD1 1 
ATOM   6443  N  N   . GLY F  1 115 ? 27.968  243.278 49.413  1.00 31.44  ? 114 GLY F N   1 
ATOM   6444  C  CA  . GLY F  1 115 ? 28.207  244.594 49.929  1.00 28.15  ? 114 GLY F CA  1 
ATOM   6445  C  C   . GLY F  1 115 ? 26.979  245.180 50.556  1.00 27.64  ? 114 GLY F C   1 
ATOM   6446  O  O   . GLY F  1 115 ? 26.955  246.305 50.936  1.00 29.39  ? 114 GLY F O   1 
ATOM   6447  N  N   . ARG F  1 116 ? 25.946  244.404 50.703  1.00 29.68  ? 115 ARG F N   1 
ATOM   6448  C  CA  . ARG F  1 116 ? 24.730  244.903 51.385  1.00 31.96  ? 115 ARG F CA  1 
ATOM   6449  C  C   . ARG F  1 116 ? 24.589  244.069 52.634  1.00 30.21  ? 115 ARG F C   1 
ATOM   6450  O  O   . ARG F  1 116 ? 25.518  243.318 52.960  1.00 30.30  ? 115 ARG F O   1 
ATOM   6451  C  CB  . ARG F  1 116 ? 23.500  244.828 50.469  1.00 30.82  ? 115 ARG F CB  1 
ATOM   6452  C  CG  . ARG F  1 116 ? 23.832  245.283 49.083  1.00 31.57  ? 115 ARG F CG  1 
ATOM   6453  C  CD  . ARG F  1 116 ? 22.599  245.714 48.358  1.00 34.06  ? 115 ARG F CD  1 
ATOM   6454  N  NE  . ARG F  1 116 ? 22.838  246.199 47.016  1.00 30.06  ? 115 ARG F NE  1 
ATOM   6455  C  CZ  . ARG F  1 116 ? 22.812  247.484 46.679  1.00 32.43  ? 115 ARG F CZ  1 
ATOM   6456  N  NH1 . ARG F  1 116 ? 22.535  248.413 47.586  1.00 31.61  ? 115 ARG F NH1 1 
ATOM   6457  N  NH2 . ARG F  1 116 ? 23.016  247.849 45.416  1.00 28.51  ? 115 ARG F NH2 1 
ATOM   6458  N  N   . THR F  1 117 ? 23.473  244.181 53.330  1.00 30.50  ? 116 THR F N   1 
ATOM   6459  C  CA  . THR F  1 117 ? 23.375  243.598 54.660  1.00 31.24  ? 116 THR F CA  1 
ATOM   6460  C  C   . THR F  1 117 ? 22.237  242.641 54.774  1.00 29.75  ? 116 THR F C   1 
ATOM   6461  O  O   . THR F  1 117 ? 21.136  242.929 54.389  1.00 27.81  ? 116 THR F O   1 
ATOM   6462  C  CB  . THR F  1 117 ? 23.234  244.701 55.717  1.00 32.98  ? 116 THR F CB  1 
ATOM   6463  O  OG1 . THR F  1 117 ? 24.393  245.585 55.712  1.00 31.04  ? 116 THR F OG1 1 
ATOM   6464  C  CG2 . THR F  1 117 ? 22.999  244.116 57.099  1.00 29.60  ? 116 THR F CG2 1 
ATOM   6465  N  N   . LEU F  1 118 ? 22.543  241.473 55.304  1.00 31.22  ? 117 LEU F N   1 
ATOM   6466  C  CA  . LEU F  1 118 ? 21.507  240.502 55.611  1.00 30.31  ? 117 LEU F CA  1 
ATOM   6467  C  C   . LEU F  1 118 ? 21.069  240.735 57.072  1.00 28.14  ? 117 LEU F C   1 
ATOM   6468  O  O   . LEU F  1 118 ? 21.874  240.872 57.949  1.00 27.10  ? 117 LEU F O   1 
ATOM   6469  C  CB  . LEU F  1 118 ? 22.022  239.094 55.374  1.00 28.09  ? 117 LEU F CB  1 
ATOM   6470  C  CG  . LEU F  1 118 ? 21.019  237.993 55.641  1.00 32.04  ? 117 LEU F CG  1 
ATOM   6471  C  CD1 . LEU F  1 118 ? 19.844  238.026 54.665  1.00 26.36  ? 117 LEU F CD1 1 
ATOM   6472  C  CD2 . LEU F  1 118 ? 21.701  236.623 55.699  1.00 29.14  ? 117 LEU F CD2 1 
ATOM   6473  N  N   . VAL F  1 119 ? 19.781  240.825 57.281  1.00 29.13  ? 118 VAL F N   1 
ATOM   6474  C  CA  . VAL F  1 119 ? 19.196  241.067 58.561  1.00 28.14  ? 118 VAL F CA  1 
ATOM   6475  C  C   . VAL F  1 119 ? 18.202  239.976 58.879  1.00 27.65  ? 118 VAL F C   1 
ATOM   6476  O  O   . VAL F  1 119 ? 17.287  239.658 58.082  1.00 27.75  ? 118 VAL F O   1 
ATOM   6477  C  CB  . VAL F  1 119 ? 18.488  242.460 58.603  1.00 27.38  ? 118 VAL F CB  1 
ATOM   6478  C  CG1 . VAL F  1 119 ? 17.823  242.723 59.945  1.00 21.71  ? 118 VAL F CG1 1 
ATOM   6479  C  CG2 . VAL F  1 119 ? 19.468  243.585 58.295  1.00 25.37  ? 118 VAL F CG2 1 
ATOM   6480  N  N   . VAL F  1 120 ? 18.361  239.400 60.060  1.00 28.92  ? 119 VAL F N   1 
ATOM   6481  C  CA  . VAL F  1 120 ? 17.295  238.535 60.594  1.00 29.29  ? 119 VAL F CA  1 
ATOM   6482  C  C   . VAL F  1 120 ? 16.530  239.368 61.651  1.00 27.81  ? 119 VAL F C   1 
ATOM   6483  O  O   . VAL F  1 120 ? 17.132  239.993 62.478  1.00 26.61  ? 119 VAL F O   1 
ATOM   6484  C  CB  . VAL F  1 120 ? 17.777  237.157 61.125  1.00 30.23  ? 119 VAL F CB  1 
ATOM   6485  C  CG1 . VAL F  1 120 ? 18.915  237.306 62.157  1.00 29.00  ? 119 VAL F CG1 1 
ATOM   6486  C  CG2 . VAL F  1 120 ? 16.599  236.422 61.758  1.00 31.51  ? 119 VAL F CG2 1 
ATOM   6487  N  N   . HIS F  1 121 ? 15.211  239.358 61.526  1.00 27.76  ? 120 HIS F N   1 
ATOM   6488  C  CA  . HIS F  1 121 ? 14.259  240.121 62.307  1.00 27.59  ? 120 HIS F CA  1 
ATOM   6489  C  C   . HIS F  1 121 ? 13.577  239.408 63.464  1.00 27.54  ? 120 HIS F C   1 
ATOM   6490  O  O   . HIS F  1 121 ? 13.553  238.207 63.579  1.00 28.43  ? 120 HIS F O   1 
ATOM   6491  C  CB  . HIS F  1 121 ? 13.196  240.773 61.391  1.00 25.85  ? 120 HIS F CB  1 
ATOM   6492  C  CG  . HIS F  1 121 ? 13.741  241.866 60.507  1.00 29.30  ? 120 HIS F CG  1 
ATOM   6493  N  ND1 . HIS F  1 121 ? 13.665  243.214 60.828  1.00 27.06  ? 120 HIS F ND1 1 
ATOM   6494  C  CD2 . HIS F  1 121 ? 14.378  241.805 59.311  1.00 25.68  ? 120 HIS F CD2 1 
ATOM   6495  C  CE1 . HIS F  1 121 ? 14.217  243.923 59.863  1.00 24.34  ? 120 HIS F CE1 1 
ATOM   6496  N  NE2 . HIS F  1 121 ? 14.640  243.101 58.924  1.00 25.77  ? 120 HIS F NE2 1 
ATOM   6497  N  N   . GLU F  1 122 ? 12.993  240.238 64.304  1.00 33.72  ? 121 GLU F N   1 
ATOM   6498  C  CA  . GLU F  1 122 ? 12.318  239.917 65.559  1.00 33.11  ? 121 GLU F CA  1 
ATOM   6499  C  C   . GLU F  1 122 ? 11.076  239.097 65.388  1.00 32.72  ? 121 GLU F C   1 
ATOM   6500  O  O   . GLU F  1 122 ? 10.856  238.213 66.170  1.00 33.64  ? 121 GLU F O   1 
ATOM   6501  C  CB  . GLU F  1 122 ? 11.952  241.237 66.228  1.00 36.35  ? 121 GLU F CB  1 
ATOM   6502  C  CG  . GLU F  1 122 ? 11.338  241.110 67.617  1.00 41.37  ? 121 GLU F CG  1 
ATOM   6503  C  CD  . GLU F  1 122 ? 10.521  242.351 68.090  1.00 49.16  ? 121 GLU F CD  1 
ATOM   6504  O  OE1 . GLU F  1 122 ? 10.423  243.468 67.451  1.00 43.66  ? 121 GLU F OE1 1 
ATOM   6505  O  OE2 . GLU F  1 122 ? 9.941   242.180 69.183  1.00 49.76  ? 121 GLU F OE2 1 
ATOM   6506  N  N   . LYS F  1 123 ? 10.248  239.386 64.380  1.00 32.84  ? 122 LYS F N   1 
ATOM   6507  C  CA  . LYS F  1 123 ? 9.067   238.559 64.173  1.00 35.04  ? 122 LYS F CA  1 
ATOM   6508  C  C   . LYS F  1 123 ? 8.883   238.127 62.759  1.00 33.16  ? 122 LYS F C   1 
ATOM   6509  O  O   . LYS F  1 123 ? 9.727   238.418 61.900  1.00 33.56  ? 122 LYS F O   1 
ATOM   6510  C  CB  . LYS F  1 123 ? 7.798   239.301 64.568  1.00 39.91  ? 122 LYS F CB  1 
ATOM   6511  C  CG  . LYS F  1 123 ? 7.954   240.218 65.737  1.00 40.65  ? 122 LYS F CG  1 
ATOM   6512  C  CD  . LYS F  1 123 ? 7.120   241.368 65.336  1.00 43.00  ? 122 LYS F CD  1 
ATOM   6513  C  CE  . LYS F  1 123 ? 6.290   241.885 66.475  1.00 45.62  ? 122 LYS F CE  1 
ATOM   6514  N  NZ  . LYS F  1 123 ? 5.371   242.757 65.680  1.00 48.14  ? 122 LYS F NZ  1 
ATOM   6515  N  N   . ALA F  1 124 ? 7.748   237.458 62.543  1.00 29.19  ? 123 ALA F N   1 
ATOM   6516  C  CA  . ALA F  1 124 ? 7.304   237.027 61.232  1.00 31.91  ? 123 ALA F CA  1 
ATOM   6517  C  C   . ALA F  1 124 ? 7.075   238.138 60.266  1.00 29.38  ? 123 ALA F C   1 
ATOM   6518  O  O   . ALA F  1 124 ? 6.605   239.185 60.627  1.00 30.57  ? 123 ALA F O   1 
ATOM   6519  C  CB  . ALA F  1 124 ? 6.063   236.203 61.334  1.00 31.13  ? 123 ALA F CB  1 
ATOM   6520  N  N   . ASP F  1 125 ? 7.453   237.901 59.032  1.00 30.14  ? 124 ASP F N   1 
ATOM   6521  C  CA  . ASP F  1 125 ? 7.195   238.819 57.977  1.00 29.93  ? 124 ASP F CA  1 
ATOM   6522  C  C   . ASP F  1 125 ? 5.820   238.428 57.530  1.00 29.89  ? 124 ASP F C   1 
ATOM   6523  O  O   . ASP F  1 125 ? 5.545   237.242 57.267  1.00 29.77  ? 124 ASP F O   1 
ATOM   6524  C  CB  . ASP F  1 125 ? 8.228   238.575 56.888  1.00 32.83  ? 124 ASP F CB  1 
ATOM   6525  C  CG  . ASP F  1 125 ? 8.072   239.487 55.634  1.00 29.75  ? 124 ASP F CG  1 
ATOM   6526  O  OD1 . ASP F  1 125 ? 7.032   240.066 55.359  1.00 26.63  ? 124 ASP F OD1 1 
ATOM   6527  O  OD2 . ASP F  1 125 ? 9.051   239.571 54.897  1.00 30.94  ? 124 ASP F OD2 1 
ATOM   6528  N  N   . ASP F  1 126 ? 4.937   239.415 57.414  1.00 31.91  ? 125 ASP F N   1 
ATOM   6529  C  CA  . ASP F  1 126 ? 3.555   239.111 56.996  1.00 31.21  ? 125 ASP F CA  1 
ATOM   6530  C  C   . ASP F  1 126 ? 3.398   238.938 55.481  1.00 30.50  ? 125 ASP F C   1 
ATOM   6531  O  O   . ASP F  1 126 ? 2.292   238.659 54.985  1.00 33.39  ? 125 ASP F O   1 
ATOM   6532  C  CB  . ASP F  1 126 ? 2.503   240.030 57.659  1.00 27.85  ? 125 ASP F CB  1 
ATOM   6533  C  CG  . ASP F  1 126 ? 2.592   241.502 57.182  1.00 29.98  ? 125 ASP F CG  1 
ATOM   6534  O  OD1 . ASP F  1 126 ? 3.261   241.808 56.166  1.00 31.46  ? 125 ASP F OD1 1 
ATOM   6535  O  OD2 . ASP F  1 126 ? 1.974   242.380 57.812  1.00 30.62  ? 125 ASP F OD2 1 
ATOM   6536  N  N   . LEU F  1 127 ? 4.516   239.095 54.778  1.00 31.78  ? 126 LEU F N   1 
ATOM   6537  C  CA  . LEU F  1 127 ? 4.681   238.927 53.325  1.00 29.05  ? 126 LEU F CA  1 
ATOM   6538  C  C   . LEU F  1 127 ? 3.920   239.914 52.532  1.00 28.48  ? 126 LEU F C   1 
ATOM   6539  O  O   . LEU F  1 127 ? 3.558   239.680 51.412  1.00 32.86  ? 126 LEU F O   1 
ATOM   6540  C  CB  . LEU F  1 127 ? 4.409   237.495 52.905  1.00 29.06  ? 126 LEU F CB  1 
ATOM   6541  C  CG  . LEU F  1 127 ? 5.176   236.476 53.763  1.00 30.48  ? 126 LEU F CG  1 
ATOM   6542  C  CD1 . LEU F  1 127 ? 4.841   235.098 53.221  1.00 31.93  ? 126 LEU F CD1 1 
ATOM   6543  C  CD2 . LEU F  1 127 ? 6.705   236.690 53.890  1.00 31.26  ? 126 LEU F CD2 1 
ATOM   6544  N  N   . GLY F  1 128 ? 3.628   241.025 53.172  1.00 30.83  ? 127 GLY F N   1 
ATOM   6545  C  CA  . GLY F  1 128 ? 2.923   242.140 52.599  1.00 27.14  ? 127 GLY F CA  1 
ATOM   6546  C  C   . GLY F  1 128 ? 1.439   241.942 52.608  1.00 27.31  ? 127 GLY F C   1 
ATOM   6547  O  O   . GLY F  1 128 ? 0.780   242.519 51.820  1.00 29.02  ? 127 GLY F O   1 
ATOM   6548  N  N   . LYS F  1 129 ? 0.893   241.150 53.502  1.00 28.59  ? 128 LYS F N   1 
ATOM   6549  C  CA  . LYS F  1 129 ? -0.532  240.744 53.419  1.00 28.46  ? 128 LYS F CA  1 
ATOM   6550  C  C   . LYS F  1 129 ? -1.259  241.190 54.671  1.00 28.91  ? 128 LYS F C   1 
ATOM   6551  O  O   . LYS F  1 129 ? -2.301  240.643 55.048  1.00 27.64  ? 128 LYS F O   1 
ATOM   6552  C  CB  . LYS F  1 129 ? -0.616  239.212 53.319  1.00 29.51  ? 128 LYS F CB  1 
ATOM   6553  C  CG  . LYS F  1 129 ? -0.043  238.739 51.998  1.00 33.46  ? 128 LYS F CG  1 
ATOM   6554  C  CD  . LYS F  1 129 ? 0.064   237.259 52.075  1.00 35.84  ? 128 LYS F CD  1 
ATOM   6555  C  CE  . LYS F  1 129 ? -0.946  236.579 51.224  1.00 39.56  ? 128 LYS F CE  1 
ATOM   6556  N  NZ  . LYS F  1 129 ? -1.057  235.290 51.956  1.00 45.66  ? 128 LYS F NZ  1 
ATOM   6557  N  N   . GLY F  1 130 ? -0.635  242.126 55.377  1.00 27.62  ? 129 GLY F N   1 
ATOM   6558  C  CA  . GLY F  1 130 ? -1.139  242.576 56.661  1.00 31.33  ? 129 GLY F CA  1 
ATOM   6559  C  C   . GLY F  1 130 ? -2.155  243.730 56.692  1.00 34.24  ? 129 GLY F C   1 
ATOM   6560  O  O   . GLY F  1 130 ? -2.757  243.995 57.743  1.00 34.24  ? 129 GLY F O   1 
ATOM   6561  N  N   . GLY F  1 131 ? -2.316  244.429 55.568  1.00 30.59  ? 130 GLY F N   1 
ATOM   6562  C  CA  . GLY F  1 131 ? -3.431  245.277 55.399  1.00 29.99  ? 130 GLY F CA  1 
ATOM   6563  C  C   . GLY F  1 131 ? -3.165  246.629 55.959  1.00 30.48  ? 130 GLY F C   1 
ATOM   6564  O  O   . GLY F  1 131 ? -3.980  247.508 55.812  1.00 32.26  ? 130 GLY F O   1 
ATOM   6565  N  N   . ASN F  1 132 ? -2.028  246.819 56.596  1.00 32.54  ? 131 ASN F N   1 
ATOM   6566  C  CA  . ASN F  1 132 ? -1.627  248.166 57.012  1.00 30.88  ? 131 ASN F CA  1 
ATOM   6567  C  C   . ASN F  1 132 ? -0.469  248.662 56.182  1.00 32.51  ? 131 ASN F C   1 
ATOM   6568  O  O   . ASN F  1 132 ? -0.007  247.967 55.288  1.00 36.16  ? 131 ASN F O   1 
ATOM   6569  C  CB  . ASN F  1 132 ? -1.368  248.222 58.503  1.00 33.11  ? 131 ASN F CB  1 
ATOM   6570  C  CG  . ASN F  1 132 ? -0.140  247.433 58.949  1.00 35.29  ? 131 ASN F CG  1 
ATOM   6571  O  OD1 . ASN F  1 132 ? 0.582   246.786 58.169  1.00 36.44  ? 131 ASN F OD1 1 
ATOM   6572  N  ND2 . ASN F  1 132 ? 0.104   247.505 60.226  1.00 35.57  ? 131 ASN F ND2 1 
ATOM   6573  N  N   . GLU F  1 133 ? 0.006   249.851 56.453  1.00 34.48  ? 132 GLU F N   1 
ATOM   6574  C  CA  . GLU F  1 133 ? 1.028   250.450 55.599  1.00 39.64  ? 132 GLU F CA  1 
ATOM   6575  C  C   . GLU F  1 133 ? 2.355   249.854 55.835  1.00 39.07  ? 132 GLU F C   1 
ATOM   6576  O  O   . GLU F  1 133 ? 3.162   249.768 54.934  1.00 40.78  ? 132 GLU F O   1 
ATOM   6577  C  CB  . GLU F  1 133 ? 1.202   251.905 55.927  1.00 44.82  ? 132 GLU F CB  1 
ATOM   6578  C  CG  . GLU F  1 133 ? -0.046  252.534 56.545  1.00 54.34  ? 132 GLU F CG  1 
ATOM   6579  C  CD  . GLU F  1 133 ? 0.090   254.072 56.591  1.00 71.36  ? 132 GLU F CD  1 
ATOM   6580  O  OE1 . GLU F  1 133 ? 1.065   254.604 55.883  1.00 60.50  ? 132 GLU F OE1 1 
ATOM   6581  O  OE2 . GLU F  1 133 ? -0.760  254.718 57.335  1.00 58.77  ? 132 GLU F OE2 1 
ATOM   6582  N  N   . GLU F  1 134 ? 2.582   249.487 57.073  1.00 35.92  ? 133 GLU F N   1 
ATOM   6583  C  CA  . GLU F  1 134 ? 3.799   248.916 57.512  1.00 34.27  ? 133 GLU F CA  1 
ATOM   6584  C  C   . GLU F  1 134 ? 4.025   247.627 56.757  1.00 34.04  ? 133 GLU F C   1 
ATOM   6585  O  O   . GLU F  1 134 ? 5.123   247.326 56.427  1.00 35.81  ? 133 GLU F O   1 
ATOM   6586  C  CB  . GLU F  1 134 ? 3.688   248.688 59.017  1.00 32.12  ? 133 GLU F CB  1 
ATOM   6587  C  CG  . GLU F  1 134 ? 4.962   248.552 59.768  1.00 36.65  ? 133 GLU F CG  1 
ATOM   6588  C  CD  . GLU F  1 134 ? 5.988   249.633 59.407  1.00 49.57  ? 133 GLU F CD  1 
ATOM   6589  O  OE1 . GLU F  1 134 ? 5.651   250.845 59.547  1.00 54.21  ? 133 GLU F OE1 1 
ATOM   6590  O  OE2 . GLU F  1 134 ? 7.127   249.277 58.976  1.00 43.25  ? 133 GLU F OE2 1 
ATOM   6591  N  N   . SER F  1 135 ? 2.967   246.897 56.458  1.00 34.52  ? 134 SER F N   1 
ATOM   6592  C  CA  . SER F  1 135 ? 3.066   245.629 55.776  1.00 35.16  ? 134 SER F CA  1 
ATOM   6593  C  C   . SER F  1 135 ? 3.731   245.795 54.413  1.00 35.14  ? 134 SER F C   1 
ATOM   6594  O  O   . SER F  1 135 ? 4.522   244.949 54.029  1.00 30.19  ? 134 SER F O   1 
ATOM   6595  C  CB  . SER F  1 135 ? 1.658   245.099 55.591  1.00 34.71  ? 134 SER F CB  1 
ATOM   6596  O  OG  . SER F  1 135 ? 1.647   243.772 55.210  1.00 31.61  ? 134 SER F OG  1 
ATOM   6597  N  N   . THR F  1 136 ? 3.368   246.889 53.713  1.00 34.94  ? 135 THR F N   1 
ATOM   6598  C  CA  . THR F  1 136 ? 3.816   247.227 52.355  1.00 34.70  ? 135 THR F CA  1 
ATOM   6599  C  C   . THR F  1 136 ? 5.262   247.755 52.425  1.00 34.27  ? 135 THR F C   1 
ATOM   6600  O  O   . THR F  1 136 ? 5.928   247.956 51.415  1.00 33.30  ? 135 THR F O   1 
ATOM   6601  C  CB  . THR F  1 136 ? 2.935   248.336 51.682  1.00 35.15  ? 135 THR F CB  1 
ATOM   6602  O  OG1 . THR F  1 136 ? 3.150   249.600 52.328  1.00 38.33  ? 135 THR F OG1 1 
ATOM   6603  C  CG2 . THR F  1 136 ? 1.454   248.054 51.722  1.00 31.38  ? 135 THR F CG2 1 
ATOM   6604  N  N   . LYS F  1 137 ? 5.726   247.999 53.632  1.00 32.50  ? 136 LYS F N   1 
ATOM   6605  C  CA  . LYS F  1 137 ? 7.085   248.478 53.815  1.00 33.86  ? 136 LYS F CA  1 
ATOM   6606  C  C   . LYS F  1 137 ? 8.056   247.424 54.391  1.00 32.75  ? 136 LYS F C   1 
ATOM   6607  O  O   . LYS F  1 137 ? 9.076   247.141 53.812  1.00 32.36  ? 136 LYS F O   1 
ATOM   6608  C  CB  . LYS F  1 137 ? 7.041   249.733 54.661  1.00 34.47  ? 136 LYS F CB  1 
ATOM   6609  C  CG  . LYS F  1 137 ? 6.410   250.891 53.894  1.00 41.09  ? 136 LYS F CG  1 
ATOM   6610  C  CD  . LYS F  1 137 ? 6.819   252.189 54.534  1.00 47.56  ? 136 LYS F CD  1 
ATOM   6611  C  CE  . LYS F  1 137 ? 5.635   252.947 55.107  1.00 53.31  ? 136 LYS F CE  1 
ATOM   6612  N  NZ  . LYS F  1 137 ? 5.849   253.346 56.550  1.00 55.35  ? 136 LYS F NZ  1 
ATOM   6613  N  N   . THR F  1 138 ? 7.706   246.816 55.515  1.00 32.53  ? 137 THR F N   1 
ATOM   6614  C  CA  . THR F  1 138 ? 8.613   245.951 56.219  1.00 33.47  ? 137 THR F CA  1 
ATOM   6615  C  C   . THR F  1 138 ? 8.070   244.567 56.528  1.00 32.39  ? 137 THR F C   1 
ATOM   6616  O  O   . THR F  1 138 ? 8.772   243.740 57.123  1.00 30.71  ? 137 THR F O   1 
ATOM   6617  C  CB  . THR F  1 138 ? 9.020   246.603 57.533  1.00 31.62  ? 137 THR F CB  1 
ATOM   6618  O  OG1 . THR F  1 138 ? 7.867   246.698 58.386  1.00 34.03  ? 137 THR F OG1 1 
ATOM   6619  C  CG2 . THR F  1 138 ? 9.702   247.974 57.281  1.00 24.23  ? 137 THR F CG2 1 
ATOM   6620  N  N   . GLY F  1 139 ? 6.834   244.347 56.089  1.00 29.12  ? 138 GLY F N   1 
ATOM   6621  C  CA  . GLY F  1 139 ? 5.997   243.249 56.461  1.00 28.79  ? 138 GLY F CA  1 
ATOM   6622  C  C   . GLY F  1 139 ? 5.790   243.034 57.937  1.00 28.75  ? 138 GLY F C   1 
ATOM   6623  O  O   . GLY F  1 139 ? 5.562   241.893 58.332  1.00 30.13  ? 138 GLY F O   1 
ATOM   6624  N  N   . ASN F  1 140 ? 5.911   244.091 58.748  1.00 30.14  ? 139 ASN F N   1 
ATOM   6625  C  CA  . ASN F  1 140 ? 5.720   244.023 60.221  1.00 30.33  ? 139 ASN F CA  1 
ATOM   6626  C  C   . ASN F  1 140 ? 6.716   243.115 60.946  1.00 31.89  ? 139 ASN F C   1 
ATOM   6627  O  O   . ASN F  1 140 ? 6.394   242.513 61.972  1.00 31.99  ? 139 ASN F O   1 
ATOM   6628  C  CB  . ASN F  1 140 ? 4.256   243.676 60.573  1.00 26.13  ? 139 ASN F CB  1 
ATOM   6629  C  CG  . ASN F  1 140 ? 3.314   244.854 60.256  1.00 30.01  ? 139 ASN F CG  1 
ATOM   6630  O  OD1 . ASN F  1 140 ? 3.538   245.985 60.732  1.00 34.67  ? 139 ASN F OD1 1 
ATOM   6631  N  ND2 . ASN F  1 140 ? 2.306   244.623 59.462  1.00 26.09  ? 139 ASN F ND2 1 
ATOM   6632  N  N   . ALA F  1 141 ? 7.917   242.999 60.417  1.00 28.59  ? 140 ALA F N   1 
ATOM   6633  C  CA  . ALA F  1 141 ? 8.841   242.045 61.000  1.00 28.98  ? 140 ALA F CA  1 
ATOM   6634  C  C   . ALA F  1 141 ? 9.603   242.530 62.235  1.00 28.75  ? 140 ALA F C   1 
ATOM   6635  O  O   . ALA F  1 141 ? 10.328  241.741 62.863  1.00 29.16  ? 140 ALA F O   1 
ATOM   6636  C  CB  . ALA F  1 141 ? 9.813   241.533 59.959  1.00 29.05  ? 140 ALA F CB  1 
ATOM   6637  N  N   . GLY F  1 142 ? 9.433   243.798 62.609  1.00 28.56  ? 141 GLY F N   1 
ATOM   6638  C  CA  . GLY F  1 142 ? 9.962   244.220 63.869  1.00 29.37  ? 141 GLY F CA  1 
ATOM   6639  C  C   . GLY F  1 142 ? 11.457  244.457 63.834  1.00 34.03  ? 141 GLY F C   1 
ATOM   6640  O  O   . GLY F  1 142 ? 12.075  244.663 62.798  1.00 33.76  ? 141 GLY F O   1 
ATOM   6641  N  N   . SER F  1 143 ? 12.055  244.415 64.991  1.00 35.33  ? 142 SER F N   1 
ATOM   6642  C  CA  . SER F  1 143 ? 13.371  244.919 65.098  1.00 34.62  ? 142 SER F CA  1 
ATOM   6643  C  C   . SER F  1 143 ? 14.423  243.987 64.454  1.00 32.22  ? 142 SER F C   1 
ATOM   6644  O  O   . SER F  1 143 ? 14.132  242.875 64.065  1.00 31.18  ? 142 SER F O   1 
ATOM   6645  C  CB  . SER F  1 143 ? 13.633  245.251 66.560  1.00 32.73  ? 142 SER F CB  1 
ATOM   6646  O  OG  . SER F  1 143 ? 13.562  244.084 67.282  1.00 35.89  ? 142 SER F OG  1 
ATOM   6647  N  N   . ARG F  1 144 ? 15.616  244.535 64.297  1.00 31.83  ? 143 ARG F N   1 
ATOM   6648  C  CA  . ARG F  1 144 ? 16.759  243.847 63.698  1.00 35.03  ? 143 ARG F CA  1 
ATOM   6649  C  C   . ARG F  1 144 ? 17.581  243.101 64.752  1.00 31.94  ? 143 ARG F C   1 
ATOM   6650  O  O   . ARG F  1 144 ? 18.224  243.691 65.530  1.00 37.81  ? 143 ARG F O   1 
ATOM   6651  C  CB  . ARG F  1 144 ? 17.598  244.936 63.035  1.00 31.02  ? 143 ARG F CB  1 
ATOM   6652  C  CG  . ARG F  1 144 ? 16.750  245.726 62.087  1.00 27.38  ? 143 ARG F CG  1 
ATOM   6653  C  CD  . ARG F  1 144 ? 17.460  246.868 61.455  1.00 25.55  ? 143 ARG F CD  1 
ATOM   6654  N  NE  . ARG F  1 144 ? 16.479  247.562 60.654  1.00 27.41  ? 143 ARG F NE  1 
ATOM   6655  C  CZ  . ARG F  1 144 ? 16.771  248.288 59.592  1.00 28.49  ? 143 ARG F CZ  1 
ATOM   6656  N  NH1 . ARG F  1 144 ? 18.030  248.445 59.226  1.00 31.81  ? 143 ARG F NH1 1 
ATOM   6657  N  NH2 . ARG F  1 144 ? 15.832  248.830 58.849  1.00 24.88  ? 143 ARG F NH2 1 
ATOM   6658  N  N   . LEU F  1 145 ? 17.534  241.807 64.802  1.00 34.79  ? 144 LEU F N   1 
ATOM   6659  C  CA  . LEU F  1 145 ? 18.265  241.095 65.828  1.00 34.19  ? 144 LEU F CA  1 
ATOM   6660  C  C   . LEU F  1 145 ? 19.688  240.895 65.485  1.00 32.92  ? 144 LEU F C   1 
ATOM   6661  O  O   . LEU F  1 145 ? 20.461  240.898 66.387  1.00 35.98  ? 144 LEU F O   1 
ATOM   6662  C  CB  . LEU F  1 145 ? 17.634  239.719 66.104  1.00 35.18  ? 144 LEU F CB  1 
ATOM   6663  C  CG  . LEU F  1 145 ? 16.120  239.687 66.281  1.00 37.43  ? 144 LEU F CG  1 
ATOM   6664  C  CD1 . LEU F  1 145 ? 15.586  238.288 66.446  1.00 37.99  ? 144 LEU F CD1 1 
ATOM   6665  C  CD2 . LEU F  1 145 ? 15.689  240.512 67.479  1.00 38.69  ? 144 LEU F CD2 1 
ATOM   6666  N  N   . ALA F  1 146 ? 20.050  240.700 64.207  1.00 29.74  ? 145 ALA F N   1 
ATOM   6667  C  CA  . ALA F  1 146 ? 21.448  240.469 63.841  1.00 28.12  ? 145 ALA F CA  1 
ATOM   6668  C  C   . ALA F  1 146 ? 21.628  240.729 62.376  1.00 30.43  ? 145 ALA F C   1 
ATOM   6669  O  O   . ALA F  1 146 ? 20.701  240.550 61.591  1.00 34.06  ? 145 ALA F O   1 
ATOM   6670  C  CB  . ALA F  1 146 ? 21.921  239.075 64.225  1.00 24.54  ? 145 ALA F CB  1 
ATOM   6671  N  N   . CYS F  1 147 ? 22.814  241.183 62.009  1.00 31.31  ? 146 CYS F N   1 
ATOM   6672  C  CA  . CYS F  1 147 ? 23.105  241.526 60.641  1.00 33.09  ? 146 CYS F CA  1 
ATOM   6673  C  C   . CYS F  1 147 ? 24.605  241.301 60.337  1.00 33.68  ? 146 CYS F C   1 
ATOM   6674  O  O   . CYS F  1 147 ? 25.366  241.086 61.236  1.00 31.25  ? 146 CYS F O   1 
ATOM   6675  C  CB  . CYS F  1 147 ? 22.661  242.953 60.300  1.00 28.76  ? 146 CYS F CB  1 
ATOM   6676  S  SG  . CYS F  1 147 ? 23.449  244.170 61.364  1.00 34.55  ? 146 CYS F SG  1 
ATOM   6677  N  N   . GLY F  1 148 ? 24.979  241.389 59.054  1.00 32.04  ? 147 GLY F N   1 
ATOM   6678  C  CA  . GLY F  1 148 ? 26.332  241.309 58.630  1.00 28.89  ? 147 GLY F CA  1 
ATOM   6679  C  C   . GLY F  1 148 ? 26.308  241.789 57.212  1.00 33.83  ? 147 GLY F C   1 
ATOM   6680  O  O   . GLY F  1 148 ? 25.236  241.738 56.521  1.00 34.35  ? 147 GLY F O   1 
ATOM   6681  N  N   . VAL F  1 149 ? 27.480  242.278 56.793  1.00 28.92  ? 148 VAL F N   1 
ATOM   6682  C  CA  . VAL F  1 149 ? 27.741  242.629 55.428  1.00 29.03  ? 148 VAL F CA  1 
ATOM   6683  C  C   . VAL F  1 149 ? 27.967  241.371 54.555  1.00 31.53  ? 148 VAL F C   1 
ATOM   6684  O  O   . VAL F  1 149 ? 28.720  240.511 54.927  1.00 32.01  ? 148 VAL F O   1 
ATOM   6685  C  CB  . VAL F  1 149 ? 28.889  243.659 55.282  1.00 30.16  ? 148 VAL F CB  1 
ATOM   6686  C  CG1 . VAL F  1 149 ? 28.936  244.141 53.849  1.00 28.02  ? 148 VAL F CG1 1 
ATOM   6687  C  CG2 . VAL F  1 149 ? 28.691  244.904 56.166  1.00 25.57  ? 148 VAL F CG2 1 
ATOM   6688  N  N   . ILE F  1 150 ? 27.286  241.259 53.414  1.00 28.61  ? 149 ILE F N   1 
ATOM   6689  C  CA  . ILE F  1 150 ? 27.440  240.108 52.568  1.00 29.18  ? 149 ILE F CA  1 
ATOM   6690  C  C   . ILE F  1 150 ? 28.683  240.288 51.765  1.00 29.71  ? 149 ILE F C   1 
ATOM   6691  O  O   . ILE F  1 150 ? 28.802  241.261 51.043  1.00 30.73  ? 149 ILE F O   1 
ATOM   6692  C  CB  . ILE F  1 150 ? 26.249  239.942 51.618  1.00 29.17  ? 149 ILE F CB  1 
ATOM   6693  C  CG1 . ILE F  1 150 ? 24.957  239.899 52.471  1.00 28.89  ? 149 ILE F CG1 1 
ATOM   6694  C  CG2 . ILE F  1 150 ? 26.442  238.743 50.727  1.00 22.64  ? 149 ILE F CG2 1 
ATOM   6695  C  CD1 . ILE F  1 150 ? 23.687  240.268 51.740  1.00 27.81  ? 149 ILE F CD1 1 
ATOM   6696  N  N   . GLY F  1 151 ? 29.605  239.337 51.894  1.00 32.81  ? 150 GLY F N   1 
ATOM   6697  C  CA  . GLY F  1 151 ? 31.000  239.423 51.354  1.00 32.52  ? 150 GLY F CA  1 
ATOM   6698  C  C   . GLY F  1 151 ? 31.368  238.405 50.319  1.00 29.02  ? 150 GLY F C   1 
ATOM   6699  O  O   . GLY F  1 151 ? 30.804  237.381 50.315  1.00 31.92  ? 150 GLY F O   1 
ATOM   6700  N  N   . ILE F  1 152 ? 32.277  238.676 49.403  1.00 33.90  ? 151 ILE F N   1 
ATOM   6701  C  CA  . ILE F  1 152 ? 32.685  237.657 48.388  1.00 33.72  ? 151 ILE F CA  1 
ATOM   6702  C  C   . ILE F  1 152 ? 33.364  236.522 49.049  1.00 31.66  ? 151 ILE F C   1 
ATOM   6703  O  O   . ILE F  1 152 ? 34.188  236.770 49.896  1.00 35.41  ? 151 ILE F O   1 
ATOM   6704  C  CB  . ILE F  1 152 ? 33.695  238.226 47.415  1.00 37.12  ? 151 ILE F CB  1 
ATOM   6705  C  CG1 . ILE F  1 152 ? 33.081  239.457 46.741  1.00 39.90  ? 151 ILE F CG1 1 
ATOM   6706  C  CG2 . ILE F  1 152 ? 34.146  237.168 46.439  1.00 35.01  ? 151 ILE F CG2 1 
ATOM   6707  C  CD1 . ILE F  1 152 ? 32.759  239.230 45.296  1.00 48.29  ? 151 ILE F CD1 1 
ATOM   6708  N  N   . ALA F  1 153 ? 33.032  235.287 48.698  1.00 32.21  ? 152 ALA F N   1 
ATOM   6709  C  CA  . ALA F  1 153 ? 33.696  234.118 49.358  1.00 34.22  ? 152 ALA F CA  1 
ATOM   6710  C  C   . ALA F  1 153 ? 34.435  233.254 48.329  1.00 39.72  ? 152 ALA F C   1 
ATOM   6711  O  O   . ALA F  1 153 ? 34.219  233.371 47.115  1.00 43.21  ? 152 ALA F O   1 
ATOM   6712  C  CB  . ALA F  1 153 ? 32.703  233.274 50.169  1.00 27.74  ? 152 ALA F CB  1 
ATOM   6713  N  N   . GLN F  1 154 ? 35.275  232.358 48.840  1.00 51.21  ? 153 GLN F N   1 
ATOM   6714  C  CA  . GLN F  1 154 ? 36.109  231.365 48.077  1.00 53.57  ? 153 GLN F CA  1 
ATOM   6715  C  C   . GLN F  1 154 ? 35.399  230.024 47.906  1.00 56.46  ? 153 GLN F C   1 
ATOM   6716  O  O   . GLN F  1 154 ? 34.806  229.362 48.823  1.00 45.92  ? 153 GLN F O   1 
ATOM   6717  C  CB  . GLN F  1 154 ? 37.459  231.098 48.805  1.00 51.71  ? 153 GLN F CB  1 
ATOM   6718  C  CG  . GLN F  1 154 ? 38.600  230.453 47.991  1.00 54.55  ? 153 GLN F CG  1 
ATOM   6719  C  CD  . GLN F  1 154 ? 39.935  230.395 48.802  1.00 65.39  ? 153 GLN F CD  1 
ATOM   6720  O  OE1 . GLN F  1 154 ? 39.950  230.640 50.048  1.00 55.34  ? 153 GLN F OE1 1 
ATOM   6721  N  NE2 . GLN F  1 154 ? 41.073  230.094 48.101  1.00 59.55  ? 153 GLN F NE2 1 
ATOM   6722  O  OXT . GLN F  1 154 ? 35.515  229.589 46.754  1.00 62.82  ? 153 GLN F OXT 1 
ATOM   6723  N  N   . ALA G  1 2   ? -5.050  257.181 -28.535 1.00 61.64  ? 1   ALA G N   1 
ATOM   6724  C  CA  . ALA G  1 2   ? -5.635  258.484 -27.964 1.00 67.23  ? 1   ALA G CA  1 
ATOM   6725  C  C   . ALA G  1 2   ? -4.545  259.343 -27.187 1.00 61.74  ? 1   ALA G C   1 
ATOM   6726  O  O   . ALA G  1 2   ? -3.354  259.192 -27.474 1.00 57.12  ? 1   ALA G O   1 
ATOM   6727  C  CB  . ALA G  1 2   ? -6.914  258.213 -27.132 1.00 56.98  ? 1   ALA G CB  1 
ATOM   6728  N  N   . THR G  1 3   ? -4.921  260.223 -26.240 1.00 60.35  ? 2   THR G N   1 
ATOM   6729  C  CA  . THR G  1 3   ? -4.002  261.285 -25.752 1.00 56.32  ? 2   THR G CA  1 
ATOM   6730  C  C   . THR G  1 3   ? -3.423  261.138 -24.307 1.00 58.55  ? 2   THR G C   1 
ATOM   6731  O  O   . THR G  1 3   ? -2.529  261.919 -23.932 1.00 56.21  ? 2   THR G O   1 
ATOM   6732  C  CB  . THR G  1 3   ? -4.684  262.690 -25.808 1.00 62.55  ? 2   THR G CB  1 
ATOM   6733  O  OG1 . THR G  1 3   ? -5.378  262.941 -24.572 1.00 59.74  ? 2   THR G OG1 1 
ATOM   6734  C  CG2 . THR G  1 3   ? -5.684  262.846 -26.948 1.00 57.15  ? 2   THR G CG2 1 
ATOM   6735  N  N   . LYS G  1 4   ? -3.959  260.219 -23.488 1.00 52.27  ? 3   LYS G N   1 
ATOM   6736  C  CA  . LYS G  1 4   ? -3.459  260.024 -22.120 1.00 48.73  ? 3   LYS G CA  1 
ATOM   6737  C  C   . LYS G  1 4   ? -3.337  258.552 -21.683 1.00 51.76  ? 3   LYS G C   1 
ATOM   6738  O  O   . LYS G  1 4   ? -4.228  257.716 -21.975 1.00 51.77  ? 3   LYS G O   1 
ATOM   6739  C  CB  . LYS G  1 4   ? -4.374  260.718 -21.188 1.00 50.51  ? 3   LYS G CB  1 
ATOM   6740  C  CG  . LYS G  1 4   ? -3.633  261.631 -20.220 1.00 68.78  ? 3   LYS G CG  1 
ATOM   6741  C  CD  . LYS G  1 4   ? -3.954  263.130 -20.489 1.00 81.22  ? 3   LYS G CD  1 
ATOM   6742  C  CE  . LYS G  1 4   ? -5.371  263.583 -20.048 1.00 74.54  ? 3   LYS G CE  1 
ATOM   6743  N  NZ  . LYS G  1 4   ? -5.519  263.567 -18.564 1.00 70.75  ? 3   LYS G NZ  1 
ATOM   6744  N  N   . ALA G  1 5   ? -2.253  258.217 -20.979 1.00 48.75  ? 4   ALA G N   1 
ATOM   6745  C  CA  . ALA G  1 5   ? -2.063  256.831 -20.508 1.00 46.90  ? 4   ALA G CA  1 
ATOM   6746  C  C   . ALA G  1 5   ? -1.597  256.744 -19.065 1.00 47.09  ? 4   ALA G C   1 
ATOM   6747  O  O   . ALA G  1 5   ? -1.168  257.728 -18.467 1.00 43.46  ? 4   ALA G O   1 
ATOM   6748  C  CB  . ALA G  1 5   ? -1.159  256.050 -21.439 1.00 47.98  ? 4   ALA G CB  1 
ATOM   6749  N  N   . VAL G  1 6   ? -1.739  255.576 -18.465 1.00 43.22  ? 5   VAL G N   1 
ATOM   6750  C  CA  . VAL G  1 6   ? -1.333  255.491 -17.111 1.00 39.06  ? 5   VAL G CA  1 
ATOM   6751  C  C   . VAL G  1 6   ? -0.778  254.108 -16.844 1.00 38.59  ? 5   VAL G C   1 
ATOM   6752  O  O   . VAL G  1 6   ? -1.121  253.162 -17.548 1.00 36.60  ? 5   VAL G O   1 
ATOM   6753  C  CB  . VAL G  1 6   ? -2.478  255.906 -16.206 1.00 36.53  ? 5   VAL G CB  1 
ATOM   6754  C  CG1 . VAL G  1 6   ? -3.496  254.807 -16.122 1.00 36.61  ? 5   VAL G CG1 1 
ATOM   6755  C  CG2 . VAL G  1 6   ? -1.924  256.297 -14.850 1.00 37.12  ? 5   VAL G CG2 1 
ATOM   6756  N  N   . CYS G  1 7   ? 0.111   254.021 -15.860 1.00 38.26  ? 6   CYS G N   1 
ATOM   6757  C  CA  . CYS G  1 7   ? 0.720   252.759 -15.456 1.00 38.01  ? 6   CYS G CA  1 
ATOM   6758  C  C   . CYS G  1 7   ? 0.824   252.631 -13.933 1.00 38.22  ? 6   CYS G C   1 
ATOM   6759  O  O   . CYS G  1 7   ? 1.455   253.496 -13.303 1.00 35.74  ? 6   CYS G O   1 
ATOM   6760  C  CB  . CYS G  1 7   ? 2.089   252.679 -16.058 1.00 35.19  ? 6   CYS G CB  1 
ATOM   6761  S  SG  . CYS G  1 7   ? 2.640   250.992 -16.002 1.00 39.99  ? 6   CYS G SG  1 
ATOM   6762  N  N   . VAL G  1 8   ? 0.192   251.603 -13.345 1.00 35.76  ? 7   VAL G N   1 
ATOM   6763  C  CA  . VAL G  1 8   ? 0.412   251.294 -11.908 1.00 36.05  ? 7   VAL G CA  1 
ATOM   6764  C  C   . VAL G  1 8   ? 1.521   250.262 -11.853 1.00 36.45  ? 7   VAL G C   1 
ATOM   6765  O  O   . VAL G  1 8   ? 1.319   249.134 -12.347 1.00 35.31  ? 7   VAL G O   1 
ATOM   6766  C  CB  . VAL G  1 8   ? -0.848  250.752 -11.204 1.00 36.68  ? 7   VAL G CB  1 
ATOM   6767  C  CG1 . VAL G  1 8   ? -0.609  250.534 -9.726  1.00 34.40  ? 7   VAL G CG1 1 
ATOM   6768  C  CG2 . VAL G  1 8   ? -1.981  251.749 -11.336 1.00 36.37  ? 7   VAL G CG2 1 
ATOM   6769  N  N   . LEU G  1 9   ? 2.689   250.632 -11.309 1.00 35.84  ? 8   LEU G N   1 
ATOM   6770  C  CA  . LEU G  1 9   ? 3.735   249.598 -11.097 1.00 41.15  ? 8   LEU G CA  1 
ATOM   6771  C  C   . LEU G  1 9   ? 3.642   248.858 -9.754  1.00 38.62  ? 8   LEU G C   1 
ATOM   6772  O  O   . LEU G  1 9   ? 3.501   249.514 -8.722  1.00 38.49  ? 8   LEU G O   1 
ATOM   6773  C  CB  . LEU G  1 9   ? 5.103   250.216 -11.238 1.00 43.31  ? 8   LEU G CB  1 
ATOM   6774  C  CG  . LEU G  1 9   ? 5.350   251.231 -12.347 1.00 47.63  ? 8   LEU G CG  1 
ATOM   6775  C  CD1 . LEU G  1 9   ? 6.289   252.280 -11.764 1.00 45.42  ? 8   LEU G CD1 1 
ATOM   6776  C  CD2 . LEU G  1 9   ? 6.021   250.495 -13.480 1.00 43.30  ? 8   LEU G CD2 1 
ATOM   6777  N  N   . LYS G  1 10  ? 3.703   247.521 -9.776  1.00 41.48  ? 9   LYS G N   1 
ATOM   6778  C  CA  . LYS G  1 10  ? 3.818   246.669 -8.539  1.00 43.79  ? 9   LYS G CA  1 
ATOM   6779  C  C   . LYS G  1 10  ? 4.789   245.566 -8.849  1.00 42.51  ? 9   LYS G C   1 
ATOM   6780  O  O   . LYS G  1 10  ? 5.042   245.274 -10.023 1.00 42.46  ? 9   LYS G O   1 
ATOM   6781  C  CB  . LYS G  1 10  ? 2.526   245.896 -8.145  1.00 41.23  ? 9   LYS G CB  1 
ATOM   6782  C  CG  . LYS G  1 10  ? 1.241   246.633 -8.152  1.00 43.21  ? 9   LYS G CG  1 
ATOM   6783  C  CD  . LYS G  1 10  ? 0.766   246.815 -6.731  1.00 55.05  ? 9   LYS G CD  1 
ATOM   6784  C  CE  . LYS G  1 10  ? 0.040   248.181 -6.572  1.00 60.80  ? 9   LYS G CE  1 
ATOM   6785  N  NZ  . LYS G  1 10  ? -1.429  247.940 -6.765  1.00 51.29  ? 9   LYS G NZ  1 
ATOM   6786  N  N   . GLY G  1 11  ? 5.279   244.920 -7.799  1.00 42.22  ? 10  GLY G N   1 
ATOM   6787  C  CA  . GLY G  1 11  ? 6.021   243.692 -7.954  1.00 42.26  ? 10  GLY G CA  1 
ATOM   6788  C  C   . GLY G  1 11  ? 6.016   242.886 -6.680  1.00 40.14  ? 10  GLY G C   1 
ATOM   6789  O  O   . GLY G  1 11  ? 5.130   243.051 -5.879  1.00 40.27  ? 10  GLY G O   1 
ATOM   6790  N  N   . ASP G  1 12  ? 7.011   242.017 -6.535  1.00 39.39  ? 11  ASP G N   1 
ATOM   6791  C  CA  . ASP G  1 12  ? 7.119   241.057 -5.455  1.00 46.07  ? 11  ASP G CA  1 
ATOM   6792  C  C   . ASP G  1 12  ? 7.596   241.717 -4.160  1.00 50.22  ? 11  ASP G C   1 
ATOM   6793  O  O   . ASP G  1 12  ? 7.475   241.114 -3.085  1.00 52.22  ? 11  ASP G O   1 
ATOM   6794  C  CB  . ASP G  1 12  ? 8.084   239.910 -5.830  1.00 44.64  ? 11  ASP G CB  1 
ATOM   6795  C  CG  . ASP G  1 12  ? 7.590   239.089 -7.017  1.00 57.76  ? 11  ASP G CG  1 
ATOM   6796  O  OD1 . ASP G  1 12  ? 6.342   238.862 -7.129  1.00 56.94  ? 11  ASP G OD1 1 
ATOM   6797  O  OD2 . ASP G  1 12  ? 8.440   238.696 -7.878  1.00 53.06  ? 11  ASP G OD2 1 
ATOM   6798  N  N   . GLY G  1 13  ? 8.134   242.935 -4.276  1.00 47.02  ? 12  GLY G N   1 
ATOM   6799  C  CA  . GLY G  1 13  ? 8.736   243.676 -3.171  1.00 40.56  ? 12  GLY G CA  1 
ATOM   6800  C  C   . GLY G  1 13  ? 7.814   244.884 -2.929  1.00 43.31  ? 12  GLY G C   1 
ATOM   6801  O  O   . GLY G  1 13  ? 6.595   244.841 -3.222  1.00 37.58  ? 12  GLY G O   1 
ATOM   6802  N  N   . PRO G  1 14  ? 8.403   245.971 -2.403  1.00 39.18  ? 13  PRO G N   1 
ATOM   6803  C  CA  . PRO G  1 14  ? 7.727   247.185 -2.001  1.00 37.51  ? 13  PRO G CA  1 
ATOM   6804  C  C   . PRO G  1 14  ? 7.668   248.269 -3.062  1.00 35.07  ? 13  PRO G C   1 
ATOM   6805  O  O   . PRO G  1 14  ? 7.066   249.336 -2.834  1.00 35.77  ? 13  PRO G O   1 
ATOM   6806  C  CB  . PRO G  1 14  ? 8.612   247.675 -0.852  1.00 38.02  ? 13  PRO G CB  1 
ATOM   6807  C  CG  . PRO G  1 14  ? 9.973   247.132 -1.198  1.00 34.86  ? 13  PRO G CG  1 
ATOM   6808  C  CD  . PRO G  1 14  ? 9.780   245.871 -1.886  1.00 35.08  ? 13  PRO G CD  1 
ATOM   6809  N  N   . VAL G  1 15  ? 8.371   248.075 -4.171  1.00 38.23  ? 14  VAL G N   1 
ATOM   6810  C  CA  . VAL G  1 15  ? 8.410   249.116 -5.208  1.00 38.75  ? 14  VAL G CA  1 
ATOM   6811  C  C   . VAL G  1 15  ? 7.000   249.264 -5.824  1.00 39.89  ? 14  VAL G C   1 
ATOM   6812  O  O   . VAL G  1 15  ? 6.440   248.292 -6.394  1.00 44.82  ? 14  VAL G O   1 
ATOM   6813  C  CB  . VAL G  1 15  ? 9.459   248.787 -6.268  1.00 35.81  ? 14  VAL G CB  1 
ATOM   6814  C  CG1 . VAL G  1 15  ? 9.460   249.820 -7.350  1.00 31.82  ? 14  VAL G CG1 1 
ATOM   6815  C  CG2 . VAL G  1 15  ? 10.824  248.669 -5.631  1.00 33.29  ? 14  VAL G CG2 1 
ATOM   6816  N  N   . GLN G  1 16  ? 6.441   250.450 -5.639  1.00 38.83  ? 15  GLN G N   1 
ATOM   6817  C  CA  . GLN G  1 16  ? 5.112   250.892 -6.090  1.00 43.87  ? 15  GLN G CA  1 
ATOM   6818  C  C   . GLN G  1 16  ? 5.231   252.256 -6.814  1.00 46.97  ? 15  GLN G C   1 
ATOM   6819  O  O   . GLN G  1 16  ? 6.093   253.105 -6.480  1.00 47.17  ? 15  GLN G O   1 
ATOM   6820  C  CB  . GLN G  1 16  ? 4.164   251.121 -4.913  1.00 44.86  ? 15  GLN G CB  1 
ATOM   6821  C  CG  . GLN G  1 16  ? 3.435   249.864 -4.528  1.00 65.41  ? 15  GLN G CG  1 
ATOM   6822  C  CD  . GLN G  1 16  ? 2.525   250.025 -3.309  1.00 77.11  ? 15  GLN G CD  1 
ATOM   6823  O  OE1 . GLN G  1 16  ? 2.850   250.789 -2.368  1.00 66.71  ? 15  GLN G OE1 1 
ATOM   6824  N  NE2 . GLN G  1 16  ? 1.355   249.304 -3.320  1.00 72.10  ? 15  GLN G NE2 1 
ATOM   6825  N  N   . GLY G  1 17  ? 4.375   252.454 -7.804  1.00 45.42  ? 16  GLY G N   1 
ATOM   6826  C  CA  . GLY G  1 17  ? 4.273   253.742 -8.423  1.00 42.15  ? 16  GLY G CA  1 
ATOM   6827  C  C   . GLY G  1 17  ? 3.190   253.922 -9.465  1.00 39.79  ? 16  GLY G C   1 
ATOM   6828  O  O   . GLY G  1 17  ? 2.622   252.962 -9.983  1.00 38.39  ? 16  GLY G O   1 
ATOM   6829  N  N   . ILE G  1 18  ? 2.978   255.197 -9.778  1.00 39.00  ? 17  ILE G N   1 
ATOM   6830  C  CA  . ILE G  1 18  ? 2.103   255.634 -10.793 1.00 38.19  ? 17  ILE G CA  1 
ATOM   6831  C  C   . ILE G  1 18  ? 2.853   256.548 -11.710 1.00 40.46  ? 17  ILE G C   1 
ATOM   6832  O  O   . ILE G  1 18  ? 3.191   257.678 -11.300 1.00 44.50  ? 17  ILE G O   1 
ATOM   6833  C  CB  . ILE G  1 18  ? 0.942   256.377 -10.167 1.00 39.92  ? 17  ILE G CB  1 
ATOM   6834  C  CG1 . ILE G  1 18  ? 0.271   255.438 -9.142  1.00 45.39  ? 17  ILE G CG1 1 
ATOM   6835  C  CG2 . ILE G  1 18  ? 0.005   256.771 -11.271 1.00 38.74  ? 17  ILE G CG2 1 
ATOM   6836  C  CD1 . ILE G  1 18  ? -0.988  255.914 -8.476  1.00 46.19  ? 17  ILE G CD1 1 
ATOM   6837  N  N   . ILE G  1 19  ? 3.083   256.061 -12.927 1.00 36.37  ? 18  ILE G N   1 
ATOM   6838  C  CA  . ILE G  1 19  ? 3.580   256.840 -14.036 1.00 38.86  ? 18  ILE G CA  1 
ATOM   6839  C  C   . ILE G  1 19  ? 2.472   257.223 -15.072 1.00 45.46  ? 18  ILE G C   1 
ATOM   6840  O  O   . ILE G  1 19  ? 1.655   256.378 -15.522 1.00 43.20  ? 18  ILE G O   1 
ATOM   6841  C  CB  . ILE G  1 19  ? 4.770   256.116 -14.696 1.00 45.78  ? 18  ILE G CB  1 
ATOM   6842  C  CG1 . ILE G  1 19  ? 5.997   256.101 -13.745 1.00 48.60  ? 18  ILE G CG1 1 
ATOM   6843  C  CG2 . ILE G  1 19  ? 5.164   256.776 -16.008 1.00 45.74  ? 18  ILE G CG2 1 
ATOM   6844  C  CD1 . ILE G  1 19  ? 6.474   257.511 -13.306 1.00 48.92  ? 18  ILE G CD1 1 
ATOM   6845  N  N   . ASN G  1 20  ? 2.470   258.513 -15.438 1.00 43.07  ? 19  ASN G N   1 
ATOM   6846  C  CA  . ASN G  1 20  ? 1.470   259.162 -16.258 1.00 38.66  ? 19  ASN G CA  1 
ATOM   6847  C  C   . ASN G  1 20  ? 2.057   259.511 -17.603 1.00 45.51  ? 19  ASN G C   1 
ATOM   6848  O  O   . ASN G  1 20  ? 3.231   259.932 -17.700 1.00 46.54  ? 19  ASN G O   1 
ATOM   6849  C  CB  . ASN G  1 20  ? 1.162   260.477 -15.631 1.00 40.11  ? 19  ASN G CB  1 
ATOM   6850  C  CG  . ASN G  1 20  ? 0.229   260.360 -14.475 1.00 46.83  ? 19  ASN G CG  1 
ATOM   6851  O  OD1 . ASN G  1 20  ? -0.953  260.064 -14.689 1.00 53.18  ? 19  ASN G OD1 1 
ATOM   6852  N  ND2 . ASN G  1 20  ? 0.716   260.634 -13.225 1.00 43.71  ? 19  ASN G ND2 1 
ATOM   6853  N  N   . PHE G  1 21  ? 1.240   259.388 -18.648 1.00 46.66  ? 20  PHE G N   1 
ATOM   6854  C  CA  . PHE G  1 21  ? 1.673   259.678 -20.033 1.00 49.59  ? 20  PHE G CA  1 
ATOM   6855  C  C   . PHE G  1 21  ? 0.669   260.605 -20.664 1.00 48.98  ? 20  PHE G C   1 
ATOM   6856  O  O   . PHE G  1 21  ? -0.551  260.408 -20.553 1.00 49.08  ? 20  PHE G O   1 
ATOM   6857  C  CB  . PHE G  1 21  ? 1.761   258.437 -20.894 1.00 44.18  ? 20  PHE G CB  1 
ATOM   6858  C  CG  . PHE G  1 21  ? 2.749   257.454 -20.426 1.00 44.64  ? 20  PHE G CG  1 
ATOM   6859  C  CD1 . PHE G  1 21  ? 4.063   257.491 -20.897 1.00 44.92  ? 20  PHE G CD1 1 
ATOM   6860  C  CD2 . PHE G  1 21  ? 2.370   256.420 -19.541 1.00 45.38  ? 20  PHE G CD2 1 
ATOM   6861  C  CE1 . PHE G  1 21  ? 5.004   256.497 -20.488 1.00 46.95  ? 20  PHE G CE1 1 
ATOM   6862  C  CE2 . PHE G  1 21  ? 3.312   255.440 -19.115 1.00 43.57  ? 20  PHE G CE2 1 
ATOM   6863  C  CZ  . PHE G  1 21  ? 4.628   255.466 -19.599 1.00 39.80  ? 20  PHE G CZ  1 
ATOM   6864  N  N   . GLU G  1 22  ? 1.190   261.660 -21.279 1.00 52.70  ? 21  GLU G N   1 
ATOM   6865  C  CA  . GLU G  1 22  ? 0.334   262.632 -21.981 1.00 54.25  ? 21  GLU G CA  1 
ATOM   6866  C  C   . GLU G  1 22  ? 1.055   262.941 -23.297 1.00 57.65  ? 21  GLU G C   1 
ATOM   6867  O  O   . GLU G  1 22  ? 2.276   263.244 -23.296 1.00 55.62  ? 21  GLU G O   1 
ATOM   6868  C  CB  . GLU G  1 22  ? 0.005   263.869 -21.133 1.00 51.31  ? 21  GLU G CB  1 
ATOM   6869  C  CG  . GLU G  1 22  ? -0.440  265.083 -21.938 1.00 63.37  ? 21  GLU G CG  1 
ATOM   6870  C  CD  . GLU G  1 22  ? -1.089  266.182 -21.077 1.00 82.41  ? 21  GLU G CD  1 
ATOM   6871  O  OE1 . GLU G  1 22  ? -0.371  267.153 -20.665 1.00 75.97  ? 21  GLU G OE1 1 
ATOM   6872  O  OE2 . GLU G  1 22  ? -2.324  266.073 -20.802 1.00 80.74  ? 21  GLU G OE2 1 
ATOM   6873  N  N   . GLN G  1 23  ? 0.289   262.751 -24.385 1.00 57.58  ? 22  GLN G N   1 
ATOM   6874  C  CA  . GLN G  1 23  ? 0.652   262.991 -25.811 1.00 61.52  ? 22  GLN G CA  1 
ATOM   6875  C  C   . GLN G  1 23  ? -0.494  263.792 -26.517 1.00 74.11  ? 22  GLN G C   1 
ATOM   6876  O  O   . GLN G  1 23  ? -1.477  263.193 -27.075 1.00 72.91  ? 22  GLN G O   1 
ATOM   6877  C  CB  . GLN G  1 23  ? 0.919   261.677 -26.531 1.00 53.49  ? 22  GLN G CB  1 
ATOM   6878  C  CG  . GLN G  1 23  ? 0.739   261.805 -28.022 1.00 47.34  ? 22  GLN G CG  1 
ATOM   6879  C  CD  . GLN G  1 23  ? 1.700   260.906 -28.725 1.00 55.83  ? 22  GLN G CD  1 
ATOM   6880  O  OE1 . GLN G  1 23  ? 1.461   259.667 -28.875 1.00 53.07  ? 22  GLN G OE1 1 
ATOM   6881  N  NE2 . GLN G  1 23  ? 2.815   261.494 -29.149 1.00 44.15  ? 22  GLN G NE2 1 
ATOM   6882  N  N   . LYS G  1 24  ? -0.386  265.139 -26.418 1.00 77.42  ? 23  LYS G N   1 
ATOM   6883  C  CA  . LYS G  1 24  ? -1.441  266.123 -26.838 1.00 80.43  ? 23  LYS G CA  1 
ATOM   6884  C  C   . LYS G  1 24  ? -1.579  266.235 -28.401 1.00 80.84  ? 23  LYS G C   1 
ATOM   6885  O  O   . LYS G  1 24  ? -2.697  266.267 -28.946 1.00 71.59  ? 23  LYS G O   1 
ATOM   6886  C  CB  . LYS G  1 24  ? -1.216  267.515 -26.175 1.00 68.16  ? 23  LYS G CB  1 
ATOM   6887  N  N   . GLU G  1 25  ? -0.444  266.245 -29.103 1.00 80.03  ? 24  GLU G N   1 
ATOM   6888  C  CA  . GLU G  1 25  ? -0.419  266.389 -30.551 1.00 75.37  ? 24  GLU G CA  1 
ATOM   6889  C  C   . GLU G  1 25  ? -0.215  264.999 -31.138 1.00 73.05  ? 24  GLU G C   1 
ATOM   6890  O  O   . GLU G  1 25  ? 0.682   264.259 -30.685 1.00 62.92  ? 24  GLU G O   1 
ATOM   6891  C  CB  . GLU G  1 25  ? 0.771   267.267 -30.894 1.00 87.10  ? 24  GLU G CB  1 
ATOM   6892  C  CG  . GLU G  1 25  ? 0.627   268.330 -31.991 1.00 87.62  ? 24  GLU G CG  1 
ATOM   6893  C  CD  . GLU G  1 25  ? 2.032   268.616 -32.561 1.00 93.35  ? 24  GLU G CD  1 
ATOM   6894  O  OE1 . GLU G  1 25  ? 3.030   268.444 -31.791 1.00 76.72  ? 24  GLU G OE1 1 
ATOM   6895  O  OE2 . GLU G  1 25  ? 2.174   268.961 -33.772 1.00 83.25  ? 24  GLU G OE2 1 
ATOM   6896  N  N   . SER G  1 26  ? -1.023  264.681 -32.171 1.00 77.92  ? 25  SER G N   1 
ATOM   6897  C  CA  . SER G  1 26  ? -1.056  263.356 -32.848 1.00 69.32  ? 25  SER G CA  1 
ATOM   6898  C  C   . SER G  1 26  ? 0.304   262.689 -32.915 1.00 66.10  ? 25  SER G C   1 
ATOM   6899  O  O   . SER G  1 26  ? 0.405   261.491 -32.543 1.00 75.72  ? 25  SER G O   1 
ATOM   6900  C  CB  . SER G  1 26  ? -1.700  263.364 -34.272 1.00 72.38  ? 25  SER G CB  1 
ATOM   6901  O  OG  . SER G  1 26  ? -1.414  262.119 -34.986 1.00 60.01  ? 25  SER G OG  1 
ATOM   6902  N  N   . ASN G  1 27  ? 1.342   263.369 -33.398 1.00 57.37  ? 26  ASN G N   1 
ATOM   6903  C  CA  . ASN G  1 27  ? 2.613   262.602 -33.288 1.00 72.43  ? 26  ASN G CA  1 
ATOM   6904  C  C   . ASN G  1 27  ? 3.786   263.153 -32.494 1.00 66.97  ? 26  ASN G C   1 
ATOM   6905  O  O   . ASN G  1 27  ? 4.972   262.730 -32.667 1.00 57.60  ? 26  ASN G O   1 
ATOM   6906  C  CB  . ASN G  1 27  ? 3.024   261.748 -34.503 1.00 63.70  ? 26  ASN G CB  1 
ATOM   6907  C  CG  . ASN G  1 27  ? 3.664   260.453 -34.033 1.00 70.65  ? 26  ASN G CG  1 
ATOM   6908  O  OD1 . ASN G  1 27  ? 4.903   260.399 -33.887 1.00 68.40  ? 26  ASN G OD1 1 
ATOM   6909  N  ND2 . ASN G  1 27  ? 2.827   259.447 -33.633 1.00 68.15  ? 26  ASN G ND2 1 
ATOM   6910  N  N   . GLY G  1 28  ? 3.382   264.005 -31.546 1.00 65.76  ? 27  GLY G N   1 
ATOM   6911  C  CA  . GLY G  1 28  ? 4.282   264.728 -30.670 1.00 72.44  ? 27  GLY G CA  1 
ATOM   6912  C  C   . GLY G  1 28  ? 5.149   263.892 -29.736 1.00 72.82  ? 27  GLY G C   1 
ATOM   6913  O  O   . GLY G  1 28  ? 5.028   262.653 -29.646 1.00 65.90  ? 27  GLY G O   1 
ATOM   6914  N  N   . PRO G  1 29  ? 6.081   264.575 -29.061 1.00 74.57  ? 28  PRO G N   1 
ATOM   6915  C  CA  . PRO G  1 29  ? 6.688   264.086 -27.798 1.00 69.07  ? 28  PRO G CA  1 
ATOM   6916  C  C   . PRO G  1 29  ? 5.617   263.713 -26.734 1.00 66.38  ? 28  PRO G C   1 
ATOM   6917  O  O   . PRO G  1 29  ? 4.559   264.435 -26.572 1.00 53.47  ? 28  PRO G O   1 
ATOM   6918  C  CB  . PRO G  1 29  ? 7.518   265.298 -27.333 1.00 78.05  ? 28  PRO G CB  1 
ATOM   6919  C  CG  . PRO G  1 29  ? 7.960   265.930 -28.655 1.00 80.62  ? 28  PRO G CG  1 
ATOM   6920  C  CD  . PRO G  1 29  ? 6.741   265.811 -29.557 1.00 70.34  ? 28  PRO G CD  1 
ATOM   6921  N  N   . VAL G  1 30  ? 5.870   262.560 -26.078 1.00 55.66  ? 29  VAL G N   1 
ATOM   6922  C  CA  . VAL G  1 30  ? 5.108   262.179 -24.878 1.00 55.18  ? 29  VAL G CA  1 
ATOM   6923  C  C   . VAL G  1 30  ? 5.807   262.641 -23.595 1.00 51.78  ? 29  VAL G C   1 
ATOM   6924  O  O   . VAL G  1 30  ? 7.012   262.394 -23.407 1.00 50.68  ? 29  VAL G O   1 
ATOM   6925  C  CB  . VAL G  1 30  ? 4.972   260.677 -24.773 1.00 53.93  ? 29  VAL G CB  1 
ATOM   6926  C  CG1 . VAL G  1 30  ? 3.734   260.363 -23.932 1.00 55.64  ? 29  VAL G CG1 1 
ATOM   6927  C  CG2 . VAL G  1 30  ? 4.941   260.069 -26.177 1.00 56.00  ? 29  VAL G CG2 1 
ATOM   6928  N  N   . LYS G  1 31  ? 5.064   263.322 -22.733 1.00 53.22  ? 30  LYS G N   1 
ATOM   6929  C  CA  . LYS G  1 31  ? 5.555   263.588 -21.355 1.00 62.39  ? 30  LYS G CA  1 
ATOM   6930  C  C   . LYS G  1 31  ? 5.129   262.448 -20.415 1.00 64.20  ? 30  LYS G C   1 
ATOM   6931  O  O   . LYS G  1 31  ? 3.881   262.186 -20.235 1.00 63.63  ? 30  LYS G O   1 
ATOM   6932  C  CB  . LYS G  1 31  ? 5.065   264.938 -20.787 1.00 58.22  ? 30  LYS G CB  1 
ATOM   6933  C  CG  . LYS G  1 31  ? 4.434   265.790 -21.850 1.00 66.23  ? 30  LYS G CG  1 
ATOM   6934  C  CD  . LYS G  1 31  ? 4.516   267.243 -21.473 1.00 69.66  ? 30  LYS G CD  1 
ATOM   6935  C  CE  . LYS G  1 31  ? 3.189   267.951 -21.741 1.00 71.40  ? 30  LYS G CE  1 
ATOM   6936  N  NZ  . LYS G  1 31  ? 3.264   269.259 -21.004 1.00 71.55  ? 30  LYS G NZ  1 
ATOM   6937  N  N   . VAL G  1 32  ? 6.168   261.817 -19.833 1.00 52.17  ? 31  VAL G N   1 
ATOM   6938  C  CA  . VAL G  1 32  ? 6.089   260.793 -18.791 1.00 43.09  ? 31  VAL G CA  1 
ATOM   6939  C  C   . VAL G  1 32  ? 6.328   261.425 -17.432 1.00 45.77  ? 31  VAL G C   1 
ATOM   6940  O  O   . VAL G  1 32  ? 7.300   262.168 -17.235 1.00 48.25  ? 31  VAL G O   1 
ATOM   6941  C  CB  . VAL G  1 32  ? 7.182   259.809 -19.094 1.00 47.66  ? 31  VAL G CB  1 
ATOM   6942  C  CG1 . VAL G  1 32  ? 6.935   258.502 -18.367 1.00 46.01  ? 31  VAL G CG1 1 
ATOM   6943  C  CG2 . VAL G  1 32  ? 7.274   259.614 -20.617 1.00 40.46  ? 31  VAL G CG2 1 
ATOM   6944  N  N   . TRP G  1 33  ? 5.461   261.168 -16.467 1.00 47.40  ? 32  TRP G N   1 
ATOM   6945  C  CA  . TRP G  1 33  ? 5.693   261.715 -15.110 1.00 47.78  ? 32  TRP G CA  1 
ATOM   6946  C  C   . TRP G  1 33  ? 4.944   261.002 -13.971 1.00 53.78  ? 32  TRP G C   1 
ATOM   6947  O  O   . TRP G  1 33  ? 3.919   260.367 -14.216 1.00 53.27  ? 32  TRP G O   1 
ATOM   6948  C  CB  . TRP G  1 33  ? 5.330   263.212 -15.051 1.00 47.98  ? 32  TRP G CB  1 
ATOM   6949  C  CG  . TRP G  1 33  ? 3.864   263.490 -14.857 1.00 48.96  ? 32  TRP G CG  1 
ATOM   6950  C  CD1 . TRP G  1 33  ? 3.183   263.683 -13.662 1.00 48.33  ? 32  TRP G CD1 1 
ATOM   6951  C  CD2 . TRP G  1 33  ? 2.907   263.587 -15.880 1.00 45.29  ? 32  TRP G CD2 1 
ATOM   6952  N  NE1 . TRP G  1 33  ? 1.831   263.891 -13.904 1.00 45.98  ? 32  TRP G NE1 1 
ATOM   6953  C  CE2 . TRP G  1 33  ? 1.641   263.875 -15.260 1.00 47.76  ? 32  TRP G CE2 1 
ATOM   6954  C  CE3 . TRP G  1 33  ? 2.992   263.526 -17.268 1.00 50.83  ? 32  TRP G CE3 1 
ATOM   6955  C  CZ2 . TRP G  1 33  ? 0.442   264.064 -16.003 1.00 52.37  ? 32  TRP G CZ2 1 
ATOM   6956  C  CZ3 . TRP G  1 33  ? 1.788   263.705 -18.035 1.00 57.35  ? 32  TRP G CZ3 1 
ATOM   6957  C  CH2 . TRP G  1 33  ? 0.529   263.965 -17.392 1.00 50.69  ? 32  TRP G CH2 1 
ATOM   6958  N  N   . GLY G  1 34  ? 5.420   261.176 -12.731 1.00 51.00  ? 33  GLY G N   1 
ATOM   6959  C  CA  . GLY G  1 34  ? 4.780   260.651 -11.532 1.00 45.83  ? 33  GLY G CA  1 
ATOM   6960  C  C   . GLY G  1 34  ? 5.915   260.226 -10.642 1.00 50.24  ? 33  GLY G C   1 
ATOM   6961  O  O   . GLY G  1 34  ? 7.014   260.843 -10.620 1.00 47.48  ? 33  GLY G O   1 
ATOM   6962  N  N   . SER G  1 35  ? 5.710   259.118 -9.956  1.00 50.94  ? 34  SER G N   1 
ATOM   6963  C  CA  . SER G  1 35  ? 6.541   258.824 -8.823  1.00 46.03  ? 34  SER G CA  1 
ATOM   6964  C  C   . SER G  1 35  ? 6.660   257.330 -8.542  1.00 48.79  ? 34  SER G C   1 
ATOM   6965  O  O   . SER G  1 35  ? 5.632   256.597 -8.592  1.00 46.88  ? 34  SER G O   1 
ATOM   6966  C  CB  . SER G  1 35  ? 5.841   259.518 -7.670  1.00 49.26  ? 34  SER G CB  1 
ATOM   6967  O  OG  . SER G  1 35  ? 6.787   259.965 -6.743  1.00 54.75  ? 34  SER G OG  1 
ATOM   6968  N  N   . ILE G  1 36  ? 7.871   256.874 -8.212  1.00 42.67  ? 35  ILE G N   1 
ATOM   6969  C  CA  . ILE G  1 36  ? 8.088   255.463 -7.872  1.00 39.02  ? 35  ILE G CA  1 
ATOM   6970  C  C   . ILE G  1 36  ? 8.666   255.450 -6.463  1.00 45.98  ? 35  ILE G C   1 
ATOM   6971  O  O   . ILE G  1 36  ? 9.708   256.146 -6.223  1.00 44.94  ? 35  ILE G O   1 
ATOM   6972  C  CB  . ILE G  1 36  ? 9.087   254.773 -8.829  1.00 37.73  ? 35  ILE G CB  1 
ATOM   6973  C  CG1 . ILE G  1 36  ? 8.653   254.985 -10.268 1.00 36.93  ? 35  ILE G CG1 1 
ATOM   6974  C  CG2 . ILE G  1 36  ? 9.270   253.292 -8.452  1.00 36.60  ? 35  ILE G CG2 1 
ATOM   6975  C  CD1 . ILE G  1 36  ? 9.493   254.309 -11.350 1.00 36.51  ? 35  ILE G CD1 1 
ATOM   6976  N  N   . LYS G  1 37  ? 8.034   254.720 -5.519  1.00 43.59  ? 36  LYS G N   1 
ATOM   6977  C  CA  . LYS G  1 37  ? 8.617   254.628 -4.159  1.00 40.28  ? 36  LYS G CA  1 
ATOM   6978  C  C   . LYS G  1 37  ? 9.124   253.189 -3.832  1.00 37.64  ? 36  LYS G C   1 
ATOM   6979  O  O   . LYS G  1 37  ? 8.942   252.246 -4.644  1.00 38.66  ? 36  LYS G O   1 
ATOM   6980  C  CB  . LYS G  1 37  ? 7.691   255.293 -3.131  1.00 39.63  ? 36  LYS G CB  1 
ATOM   6981  C  CG  . LYS G  1 37  ? 6.599   254.370 -2.607  1.00 47.66  ? 36  LYS G CG  1 
ATOM   6982  C  CD  . LYS G  1 37  ? 5.396   255.143 -2.145  1.00 52.08  ? 36  LYS G CD  1 
ATOM   6983  C  CE  . LYS G  1 37  ? 4.275   254.152 -1.832  1.00 62.97  ? 36  LYS G CE  1 
ATOM   6984  N  NZ  . LYS G  1 37  ? 2.997   254.829 -1.370  1.00 51.67  ? 36  LYS G NZ  1 
ATOM   6985  N  N   . GLY G  1 38  ? 9.813   253.024 -2.704  1.00 34.02  ? 37  GLY G N   1 
ATOM   6986  C  CA  . GLY G  1 38  ? 10.351  251.721 -2.309  1.00 30.75  ? 37  GLY G CA  1 
ATOM   6987  C  C   . GLY G  1 38  ? 11.623  251.301 -3.018  1.00 33.51  ? 37  GLY G C   1 
ATOM   6988  O  O   . GLY G  1 38  ? 12.032  250.119 -3.017  1.00 34.98  ? 37  GLY G O   1 
ATOM   6989  N  N   . LEU G  1 39  ? 12.280  252.248 -3.655  1.00 35.00  ? 38  LEU G N   1 
ATOM   6990  C  CA  . LEU G  1 39  ? 13.537  251.963 -4.381  1.00 39.61  ? 38  LEU G CA  1 
ATOM   6991  C  C   . LEU G  1 39  ? 14.815  252.102 -3.490  1.00 37.91  ? 38  LEU G C   1 
ATOM   6992  O  O   . LEU G  1 39  ? 14.761  252.828 -2.534  1.00 40.41  ? 38  LEU G O   1 
ATOM   6993  C  CB  . LEU G  1 39  ? 13.612  252.962 -5.525  1.00 37.14  ? 38  LEU G CB  1 
ATOM   6994  C  CG  . LEU G  1 39  ? 12.696  252.580 -6.657  1.00 37.19  ? 38  LEU G CG  1 
ATOM   6995  C  CD1 . LEU G  1 39  ? 12.572  253.791 -7.551  1.00 37.34  ? 38  LEU G CD1 1 
ATOM   6996  C  CD2 . LEU G  1 39  ? 13.193  251.368 -7.468  1.00 42.53  ? 38  LEU G CD2 1 
ATOM   6997  N  N   . THR G  1 40  ? 15.930  251.422 -3.761  1.00 37.27  ? 39  THR G N   1 
ATOM   6998  C  CA  . THR G  1 40  ? 17.235  251.817 -3.107  1.00 42.04  ? 39  THR G CA  1 
ATOM   6999  C  C   . THR G  1 40  ? 17.696  253.127 -3.775  1.00 45.19  ? 39  THR G C   1 
ATOM   7000  O  O   . THR G  1 40  ? 17.643  253.257 -5.038  1.00 44.69  ? 39  THR G O   1 
ATOM   7001  C  CB  . THR G  1 40  ? 18.374  250.799 -3.306  1.00 41.87  ? 39  THR G CB  1 
ATOM   7002  O  OG1 . THR G  1 40  ? 18.559  250.581 -4.727  1.00 43.24  ? 39  THR G OG1 1 
ATOM   7003  C  CG2 . THR G  1 40  ? 18.084  249.437 -2.588  1.00 38.46  ? 39  THR G CG2 1 
ATOM   7004  N  N   . GLU G  1 41  ? 18.073  254.101 -2.945  1.00 42.41  ? 40  GLU G N   1 
ATOM   7005  C  CA  . GLU G  1 41  ? 18.686  255.350 -3.431  1.00 47.35  ? 40  GLU G CA  1 
ATOM   7006  C  C   . GLU G  1 41  ? 19.720  255.120 -4.522  1.00 45.46  ? 40  GLU G C   1 
ATOM   7007  O  O   . GLU G  1 41  ? 20.596  254.216 -4.422  1.00 42.35  ? 40  GLU G O   1 
ATOM   7008  C  CB  . GLU G  1 41  ? 19.370  256.090 -2.276  1.00 51.89  ? 40  GLU G CB  1 
ATOM   7009  C  CG  . GLU G  1 41  ? 20.307  257.227 -2.711  1.00 56.98  ? 40  GLU G CG  1 
ATOM   7010  C  CD  . GLU G  1 41  ? 20.961  257.978 -1.533  1.00 62.40  ? 40  GLU G CD  1 
ATOM   7011  O  OE1 . GLU G  1 41  ? 21.091  257.380 -0.452  1.00 57.44  ? 40  GLU G OE1 1 
ATOM   7012  O  OE2 . GLU G  1 41  ? 21.363  259.171 -1.677  1.00 63.09  ? 40  GLU G OE2 1 
ATOM   7013  N  N   . GLY G  1 42  ? 19.640  255.940 -5.555  1.00 43.15  ? 41  GLY G N   1 
ATOM   7014  C  CA  . GLY G  1 42  ? 20.523  255.674 -6.677  1.00 42.24  ? 41  GLY G CA  1 
ATOM   7015  C  C   . GLY G  1 42  ? 19.683  255.498 -7.904  1.00 45.44  ? 41  GLY G C   1 
ATOM   7016  O  O   . GLY G  1 42  ? 18.509  255.929 -7.937  1.00 46.21  ? 41  GLY G O   1 
ATOM   7017  N  N   . LEU G  1 43  ? 20.274  254.852 -8.904  1.00 45.96  ? 42  LEU G N   1 
ATOM   7018  C  CA  . LEU G  1 43  ? 19.731  254.871 -10.258 1.00 46.16  ? 42  LEU G CA  1 
ATOM   7019  C  C   . LEU G  1 43  ? 19.123  253.554 -10.600 1.00 47.56  ? 42  LEU G C   1 
ATOM   7020  O  O   . LEU G  1 43  ? 19.712  252.502 -10.232 1.00 48.95  ? 42  LEU G O   1 
ATOM   7021  C  CB  . LEU G  1 43  ? 20.859  255.075 -11.277 1.00 54.48  ? 42  LEU G CB  1 
ATOM   7022  C  CG  . LEU G  1 43  ? 21.577  256.416 -11.444 1.00 58.17  ? 42  LEU G CG  1 
ATOM   7023  C  CD1 . LEU G  1 43  ? 22.495  256.230 -12.658 1.00 55.44  ? 42  LEU G CD1 1 
ATOM   7024  C  CD2 . LEU G  1 43  ? 20.593  257.591 -11.594 1.00 51.81  ? 42  LEU G CD2 1 
ATOM   7025  N  N   . HIS G  1 44  ? 18.016  253.582 -11.361 1.00 41.87  ? 43  HIS G N   1 
ATOM   7026  C  CA  . HIS G  1 44  ? 17.369  252.323 -11.791 1.00 42.37  ? 43  HIS G CA  1 
ATOM   7027  C  C   . HIS G  1 44  ? 16.975  252.299 -13.283 1.00 39.76  ? 43  HIS G C   1 
ATOM   7028  O  O   . HIS G  1 44  ? 16.464  253.267 -13.794 1.00 43.60  ? 43  HIS G O   1 
ATOM   7029  C  CB  . HIS G  1 44  ? 16.160  252.020 -10.861 1.00 39.39  ? 43  HIS G CB  1 
ATOM   7030  C  CG  . HIS G  1 44  ? 16.538  251.867 -9.425  1.00 41.53  ? 43  HIS G CG  1 
ATOM   7031  N  ND1 . HIS G  1 44  ? 17.046  250.688 -8.913  1.00 38.20  ? 43  HIS G ND1 1 
ATOM   7032  C  CD2 . HIS G  1 44  ? 16.532  252.763 -8.399  1.00 41.19  ? 43  HIS G CD2 1 
ATOM   7033  C  CE1 . HIS G  1 44  ? 17.327  250.868 -7.630  1.00 43.14  ? 43  HIS G CE1 1 
ATOM   7034  N  NE2 . HIS G  1 44  ? 17.037  252.116 -7.295  1.00 42.32  ? 43  HIS G NE2 1 
ATOM   7035  N  N   . GLY G  1 45  ? 17.144  251.174 -13.972 1.00 43.63  ? 44  GLY G N   1 
ATOM   7036  C  CA  . GLY G  1 45  ? 16.732  251.074 -15.375 1.00 42.17  ? 44  GLY G CA  1 
ATOM   7037  C  C   . GLY G  1 45  ? 15.237  251.352 -15.451 1.00 47.16  ? 44  GLY G C   1 
ATOM   7038  O  O   . GLY G  1 45  ? 14.507  251.054 -14.493 1.00 48.73  ? 44  GLY G O   1 
ATOM   7039  N  N   . PHE G  1 46  ? 14.780  251.930 -16.559 1.00 40.21  ? 45  PHE G N   1 
ATOM   7040  C  CA  . PHE G  1 46  ? 13.400  252.325 -16.722 1.00 40.44  ? 45  PHE G CA  1 
ATOM   7041  C  C   . PHE G  1 46  ? 13.053  252.107 -18.202 1.00 46.05  ? 45  PHE G C   1 
ATOM   7042  O  O   . PHE G  1 46  ? 13.314  252.969 -19.036 1.00 46.90  ? 45  PHE G O   1 
ATOM   7043  C  CB  . PHE G  1 46  ? 13.245  253.808 -16.331 1.00 39.73  ? 45  PHE G CB  1 
ATOM   7044  C  CG  . PHE G  1 46  ? 11.841  254.233 -16.046 1.00 40.41  ? 45  PHE G CG  1 
ATOM   7045  C  CD1 . PHE G  1 46  ? 10.966  253.399 -15.391 1.00 40.11  ? 45  PHE G CD1 1 
ATOM   7046  C  CD2 . PHE G  1 46  ? 11.390  255.516 -16.404 1.00 42.58  ? 45  PHE G CD2 1 
ATOM   7047  C  CE1 . PHE G  1 46  ? 9.649   253.817 -15.123 1.00 39.83  ? 45  PHE G CE1 1 
ATOM   7048  C  CE2 . PHE G  1 46  ? 10.084  255.940 -16.122 1.00 35.10  ? 45  PHE G CE2 1 
ATOM   7049  C  CZ  . PHE G  1 46  ? 9.215   255.086 -15.484 1.00 35.04  ? 45  PHE G CZ  1 
ATOM   7050  N  N   . HIS G  1 47  ? 12.453  250.964 -18.522 1.00 45.80  ? 46  HIS G N   1 
ATOM   7051  C  CA  . HIS G  1 47  ? 12.197  250.572 -19.894 1.00 44.87  ? 46  HIS G CA  1 
ATOM   7052  C  C   . HIS G  1 47  ? 10.767  250.112 -20.107 1.00 47.62  ? 46  HIS G C   1 
ATOM   7053  O  O   . HIS G  1 47  ? 10.147  249.563 -19.208 1.00 49.40  ? 46  HIS G O   1 
ATOM   7054  C  CB  . HIS G  1 47  ? 13.147  249.430 -20.253 1.00 50.75  ? 46  HIS G CB  1 
ATOM   7055  C  CG  . HIS G  1 47  ? 14.598  249.806 -20.109 1.00 58.03  ? 46  HIS G CG  1 
ATOM   7056  N  ND1 . HIS G  1 47  ? 15.313  250.457 -21.104 1.00 55.49  ? 46  HIS G ND1 1 
ATOM   7057  C  CD2 . HIS G  1 47  ? 15.440  249.700 -19.050 1.00 56.99  ? 46  HIS G CD2 1 
ATOM   7058  C  CE1 . HIS G  1 47  ? 16.539  250.697 -20.679 1.00 60.61  ? 46  HIS G CE1 1 
ATOM   7059  N  NE2 . HIS G  1 47  ? 16.648  250.237 -19.437 1.00 57.23  ? 46  HIS G NE2 1 
ATOM   7060  N  N   . VAL G  1 48  ? 10.256  250.346 -21.316 1.00 48.06  ? 47  VAL G N   1 
ATOM   7061  C  CA  . VAL G  1 48  ? 9.011   249.764 -21.847 1.00 39.96  ? 47  VAL G CA  1 
ATOM   7062  C  C   . VAL G  1 48  ? 9.424   248.417 -22.440 1.00 41.98  ? 47  VAL G C   1 
ATOM   7063  O  O   . VAL G  1 48  ? 10.333  248.355 -23.296 1.00 39.48  ? 47  VAL G O   1 
ATOM   7064  C  CB  . VAL G  1 48  ? 8.408   250.632 -22.971 1.00 38.79  ? 47  VAL G CB  1 
ATOM   7065  C  CG1 . VAL G  1 48  ? 7.205   249.961 -23.526 1.00 34.69  ? 47  VAL G CG1 1 
ATOM   7066  C  CG2 . VAL G  1 48  ? 8.016   252.021 -22.489 1.00 39.53  ? 47  VAL G CG2 1 
ATOM   7067  N  N   . HIS G  1 49  ? 8.806   247.334 -21.966 1.00 37.86  ? 48  HIS G N   1 
ATOM   7068  C  CA  . HIS G  1 49  ? 9.128   246.049 -22.510 1.00 36.77  ? 48  HIS G CA  1 
ATOM   7069  C  C   . HIS G  1 49  ? 8.078   245.676 -23.474 1.00 41.91  ? 48  HIS G C   1 
ATOM   7070  O  O   . HIS G  1 49  ? 7.037   246.353 -23.545 1.00 45.20  ? 48  HIS G O   1 
ATOM   7071  C  CB  . HIS G  1 49  ? 9.249   245.056 -21.406 1.00 36.24  ? 48  HIS G CB  1 
ATOM   7072  C  CG  . HIS G  1 49  ? 10.519  245.213 -20.648 1.00 35.95  ? 48  HIS G CG  1 
ATOM   7073  N  ND1 . HIS G  1 49  ? 11.419  244.178 -20.505 1.00 36.16  ? 48  HIS G ND1 1 
ATOM   7074  C  CD2 . HIS G  1 49  ? 11.078  246.301 -20.038 1.00 34.99  ? 48  HIS G CD2 1 
ATOM   7075  C  CE1 . HIS G  1 49  ? 12.463  244.613 -19.796 1.00 39.74  ? 48  HIS G CE1 1 
ATOM   7076  N  NE2 . HIS G  1 49  ? 12.280  245.893 -19.496 1.00 34.52  ? 48  HIS G NE2 1 
ATOM   7077  N  N   . GLU G  1 50  ? 8.305   244.602 -24.213 1.00 41.16  ? 49  GLU G N   1 
ATOM   7078  C  CA  . GLU G  1 50  ? 7.376   244.269 -25.328 1.00 50.50  ? 49  GLU G CA  1 
ATOM   7079  C  C   . GLU G  1 50  ? 5.910   243.777 -25.023 1.00 46.90  ? 49  GLU G C   1 
ATOM   7080  O  O   . GLU G  1 50  ? 4.984   244.140 -25.742 1.00 41.40  ? 49  GLU G O   1 
ATOM   7081  C  CB  . GLU G  1 50  ? 8.040   243.326 -26.336 1.00 50.38  ? 49  GLU G CB  1 
ATOM   7082  C  CG  . GLU G  1 50  ? 7.091   242.930 -27.435 1.00 50.13  ? 49  GLU G CG  1 
ATOM   7083  C  CD  . GLU G  1 50  ? 7.760   242.317 -28.660 1.00 57.81  ? 49  GLU G CD  1 
ATOM   7084  O  OE1 . GLU G  1 50  ? 8.765   241.571 -28.490 1.00 54.74  ? 49  GLU G OE1 1 
ATOM   7085  O  OE2 . GLU G  1 50  ? 7.235   242.539 -29.791 1.00 54.74  ? 49  GLU G OE2 1 
ATOM   7086  N  N   . PHE G  1 51  ? 5.719   242.931 -24.013 1.00 42.43  ? 50  PHE G N   1 
ATOM   7087  C  CA  . PHE G  1 51  ? 4.377   242.358 -23.738 1.00 40.62  ? 50  PHE G CA  1 
ATOM   7088  C  C   . PHE G  1 51  ? 3.741   242.881 -22.469 1.00 39.68  ? 50  PHE G C   1 
ATOM   7089  O  O   . PHE G  1 51  ? 4.418   243.043 -21.436 1.00 45.03  ? 50  PHE G O   1 
ATOM   7090  C  CB  . PHE G  1 51  ? 4.464   240.845 -23.687 1.00 42.38  ? 50  PHE G CB  1 
ATOM   7091  C  CG  . PHE G  1 51  ? 5.142   240.271 -24.879 1.00 45.79  ? 50  PHE G CG  1 
ATOM   7092  C  CD1 . PHE G  1 51  ? 4.580   240.447 -26.169 1.00 44.56  ? 50  PHE G CD1 1 
ATOM   7093  C  CD2 . PHE G  1 51  ? 6.408   239.634 -24.740 1.00 49.92  ? 50  PHE G CD2 1 
ATOM   7094  C  CE1 . PHE G  1 51  ? 5.267   239.966 -27.286 1.00 47.05  ? 50  PHE G CE1 1 
ATOM   7095  C  CE2 . PHE G  1 51  ? 7.087   239.150 -25.856 1.00 43.57  ? 50  PHE G CE2 1 
ATOM   7096  C  CZ  . PHE G  1 51  ? 6.518   239.326 -27.118 1.00 44.77  ? 50  PHE G CZ  1 
ATOM   7097  N  N   . GLY G  1 52  ? 2.453   243.184 -22.559 1.00 39.16  ? 51  GLY G N   1 
ATOM   7098  C  CA  . GLY G  1 52  ? 1.611   243.541 -21.411 1.00 33.99  ? 51  GLY G CA  1 
ATOM   7099  C  C   . GLY G  1 52  ? 1.078   242.263 -20.783 1.00 36.88  ? 51  GLY G C   1 
ATOM   7100  O  O   . GLY G  1 52  ? -0.081  242.154 -20.555 1.00 40.46  ? 51  GLY G O   1 
ATOM   7101  N  N   . ASP G  1 53  ? 1.949   241.296 -20.555 1.00 35.86  ? 52  ASP G N   1 
ATOM   7102  C  CA  . ASP G  1 53  ? 1.683   240.030 -19.972 1.00 37.31  ? 52  ASP G CA  1 
ATOM   7103  C  C   . ASP G  1 53  ? 2.349   240.018 -18.549 1.00 40.80  ? 52  ASP G C   1 
ATOM   7104  O  O   . ASP G  1 53  ? 3.611   240.082 -18.397 1.00 38.78  ? 52  ASP G O   1 
ATOM   7105  C  CB  . ASP G  1 53  ? 2.285   238.965 -20.880 1.00 33.26  ? 52  ASP G CB  1 
ATOM   7106  C  CG  . ASP G  1 53  ? 2.080   237.546 -20.381 1.00 38.81  ? 52  ASP G CG  1 
ATOM   7107  O  OD1 . ASP G  1 53  ? 1.910   237.275 -19.138 1.00 46.36  ? 52  ASP G OD1 1 
ATOM   7108  O  OD2 . ASP G  1 53  ? 2.126   236.653 -21.248 1.00 39.41  ? 52  ASP G OD2 1 
ATOM   7109  N  N   A ASN G  1 54  ? 1.509   239.909 -17.512 0.50 37.14  ? 53  ASN G N   1 
ATOM   7110  N  N   B ASN G  1 54  ? 1.521   239.956 -17.519 0.50 36.87  ? 53  ASN G N   1 
ATOM   7111  C  CA  A ASN G  1 54  ? 2.006   239.938 -16.124 0.50 36.78  ? 53  ASN G CA  1 
ATOM   7112  C  CA  B ASN G  1 54  ? 2.074   240.036 -16.185 0.50 36.16  ? 53  ASN G CA  1 
ATOM   7113  C  C   A ASN G  1 54  ? 1.719   238.613 -15.465 0.50 36.68  ? 53  ASN G C   1 
ATOM   7114  C  C   B ASN G  1 54  ? 1.696   238.677 -15.488 0.50 36.23  ? 53  ASN G C   1 
ATOM   7115  O  O   A ASN G  1 54  ? 1.853   238.483 -14.259 0.50 38.25  ? 53  ASN G O   1 
ATOM   7116  O  O   B ASN G  1 54  ? 1.772   238.585 -14.273 0.50 38.00  ? 53  ASN G O   1 
ATOM   7117  C  CB  A ASN G  1 54  ? 1.395   241.096 -15.299 0.50 38.33  ? 53  ASN G CB  1 
ATOM   7118  C  CB  B ASN G  1 54  ? 1.642   241.380 -15.448 0.50 36.15  ? 53  ASN G CB  1 
ATOM   7119  C  CG  A ASN G  1 54  ? 2.025   241.221 -13.902 0.50 39.49  ? 53  ASN G CG  1 
ATOM   7120  C  CG  B ASN G  1 54  ? 2.414   242.703 -15.919 0.50 36.94  ? 53  ASN G CG  1 
ATOM   7121  O  OD1 A ASN G  1 54  ? 3.215   241.514 -13.771 0.50 41.83  ? 53  ASN G OD1 1 
ATOM   7122  O  OD1 B ASN G  1 54  ? 3.364   242.706 -16.729 0.50 33.03  ? 53  ASN G OD1 1 
ATOM   7123  N  ND2 A ASN G  1 54  ? 1.229   240.990 -12.861 0.50 34.35  ? 53  ASN G ND2 1 
ATOM   7124  N  ND2 B ASN G  1 54  ? 1.961   243.852 -15.369 0.50 37.91  ? 53  ASN G ND2 1 
ATOM   7125  N  N   . THR G  1 55  ? 1.339   237.627 -16.269 1.00 39.05  ? 54  THR G N   1 
ATOM   7126  C  CA  . THR G  1 55  ? 0.974   236.243 -15.734 1.00 40.97  ? 54  THR G CA  1 
ATOM   7127  C  C   . THR G  1 55  ? 2.097   235.513 -15.017 1.00 44.12  ? 54  THR G C   1 
ATOM   7128  O  O   . THR G  1 55  ? 1.840   234.528 -14.354 1.00 47.22  ? 54  THR G O   1 
ATOM   7129  C  CB  . THR G  1 55  ? 0.566   235.171 -16.819 1.00 36.85  ? 54  THR G CB  1 
ATOM   7130  O  OG1 . THR G  1 55  ? 1.518   235.177 -17.854 1.00 36.16  ? 54  THR G OG1 1 
ATOM   7131  C  CG2 . THR G  1 55  ? -0.686  235.456 -17.438 1.00 34.53  ? 54  THR G CG2 1 
ATOM   7132  N  N   . ALA G  1 56  ? 3.354   235.906 -15.252 1.00 46.72  ? 55  ALA G N   1 
ATOM   7133  C  CA  . ALA G  1 56  ? 4.497   235.337 -14.524 1.00 40.52  ? 55  ALA G CA  1 
ATOM   7134  C  C   . ALA G  1 56  ? 5.269   236.502 -13.871 1.00 39.14  ? 55  ALA G C   1 
ATOM   7135  O  O   . ALA G  1 56  ? 6.504   236.526 -13.810 1.00 40.50  ? 55  ALA G O   1 
ATOM   7136  C  CB  . ALA G  1 56  ? 5.331   234.507 -15.485 1.00 34.67  ? 55  ALA G CB  1 
ATOM   7137  N  N   . GLY G  1 57  ? 4.508   237.495 -13.395 1.00 40.91  ? 56  GLY G N   1 
ATOM   7138  C  CA  . GLY G  1 57  ? 5.068   238.755 -12.863 1.00 39.01  ? 56  GLY G CA  1 
ATOM   7139  C  C   . GLY G  1 57  ? 5.767   239.487 -14.011 1.00 39.84  ? 56  GLY G C   1 
ATOM   7140  O  O   . GLY G  1 57  ? 5.354   239.363 -15.166 1.00 36.36  ? 56  GLY G O   1 
ATOM   7141  N  N   . CYS G  1 58  ? 6.823   240.232 -13.688 1.00 39.24  ? 57  CYS G N   1 
ATOM   7142  C  CA  . CYS G  1 58  ? 7.551   241.046 -14.670 1.00 40.16  ? 57  CYS G CA  1 
ATOM   7143  C  C   . CYS G  1 58  ? 8.407   240.273 -15.698 1.00 42.28  ? 57  CYS G C   1 
ATOM   7144  O  O   . CYS G  1 58  ? 8.756   240.802 -16.741 1.00 45.27  ? 57  CYS G O   1 
ATOM   7145  C  CB  . CYS G  1 58  ? 8.415   242.059 -13.964 1.00 39.40  ? 57  CYS G CB  1 
ATOM   7146  S  SG  . CYS G  1 58  ? 7.523   243.180 -12.876 1.00 44.79  ? 57  CYS G SG  1 
ATOM   7147  N  N   . THR G  1 59  ? 8.717   239.019 -15.434 1.00 45.28  ? 58  THR G N   1 
ATOM   7148  C  CA  . THR G  1 59  ? 9.413   238.174 -16.427 1.00 43.64  ? 58  THR G CA  1 
ATOM   7149  C  C   . THR G  1 59  ? 8.620   238.083 -17.695 1.00 42.44  ? 58  THR G C   1 
ATOM   7150  O  O   . THR G  1 59  ? 9.192   238.137 -18.773 1.00 49.03  ? 58  THR G O   1 
ATOM   7151  C  CB  . THR G  1 59  ? 9.706   236.766 -15.813 1.00 43.06  ? 58  THR G CB  1 
ATOM   7152  O  OG1 . THR G  1 59  ? 10.610  236.994 -14.759 1.00 46.07  ? 58  THR G OG1 1 
ATOM   7153  C  CG2 . THR G  1 59  ? 10.387  235.699 -16.763 1.00 38.48  ? 58  THR G CG2 1 
ATOM   7154  N  N   . SER G  1 60  ? 7.310   237.927 -17.614 1.00 40.21  ? 59  SER G N   1 
ATOM   7155  C  CA  . SER G  1 60  ? 6.596   237.654 -18.857 1.00 41.73  ? 59  SER G CA  1 
ATOM   7156  C  C   . SER G  1 60  ? 6.386   238.893 -19.750 1.00 40.18  ? 59  SER G C   1 
ATOM   7157  O  O   . SER G  1 60  ? 5.821   238.785 -20.827 1.00 39.30  ? 59  SER G O   1 
ATOM   7158  C  CB  . SER G  1 60  ? 5.346   236.832 -18.622 1.00 37.98  ? 59  SER G CB  1 
ATOM   7159  O  OG  . SER G  1 60  ? 4.617   237.464 -17.590 1.00 47.93  ? 59  SER G OG  1 
ATOM   7160  N  N   . ALA G  1 61  ? 6.909   240.051 -19.335 1.00 38.06  ? 60  ALA G N   1 
ATOM   7161  C  CA  . ALA G  1 61  ? 6.858   241.238 -20.169 1.00 35.21  ? 60  ALA G CA  1 
ATOM   7162  C  C   . ALA G  1 61  ? 7.866   241.168 -21.329 1.00 40.07  ? 60  ALA G C   1 
ATOM   7163  O  O   . ALA G  1 61  ? 7.896   242.067 -22.149 1.00 42.88  ? 60  ALA G O   1 
ATOM   7164  C  CB  . ALA G  1 61  ? 7.093   242.460 -19.345 1.00 33.44  ? 60  ALA G CB  1 
ATOM   7165  N  N   . GLY G  1 62  ? 8.678   240.107 -21.377 1.00 40.69  ? 61  GLY G N   1 
ATOM   7166  C  CA  . GLY G  1 62  ? 9.657   239.875 -22.430 1.00 47.23  ? 61  GLY G CA  1 
ATOM   7167  C  C   . GLY G  1 62  ? 10.813  240.872 -22.554 1.00 52.04  ? 61  GLY G C   1 
ATOM   7168  O  O   . GLY G  1 62  ? 11.264  241.490 -21.543 1.00 53.74  ? 61  GLY G O   1 
ATOM   7169  N  N   . PRO G  1 63  ? 11.292  241.073 -23.798 1.00 48.25  ? 62  PRO G N   1 
ATOM   7170  C  CA  . PRO G  1 63  ? 12.453  241.982 -23.944 1.00 43.53  ? 62  PRO G CA  1 
ATOM   7171  C  C   . PRO G  1 63  ? 12.022  243.430 -24.012 1.00 39.98  ? 62  PRO G C   1 
ATOM   7172  O  O   . PRO G  1 63  ? 10.827  243.718 -23.945 1.00 39.29  ? 62  PRO G O   1 
ATOM   7173  C  CB  . PRO G  1 63  ? 13.059  241.544 -25.246 1.00 38.00  ? 62  PRO G CB  1 
ATOM   7174  C  CG  . PRO G  1 63  ? 11.916  240.954 -26.024 1.00 41.85  ? 62  PRO G CG  1 
ATOM   7175  C  CD  . PRO G  1 63  ? 10.932  240.392 -25.061 1.00 42.78  ? 62  PRO G CD  1 
ATOM   7176  N  N   . HIS G  1 64  ? 12.997  244.321 -24.109 1.00 42.04  ? 63  HIS G N   1 
ATOM   7177  C  CA  . HIS G  1 64  ? 12.734  245.756 -24.406 1.00 51.43  ? 63  HIS G CA  1 
ATOM   7178  C  C   . HIS G  1 64  ? 11.894  245.878 -25.671 1.00 48.15  ? 63  HIS G C   1 
ATOM   7179  O  O   . HIS G  1 64  ? 12.156  245.151 -26.645 1.00 43.40  ? 63  HIS G O   1 
ATOM   7180  C  CB  . HIS G  1 64  ? 14.070  246.541 -24.621 1.00 53.33  ? 63  HIS G CB  1 
ATOM   7181  C  CG  . HIS G  1 64  ? 14.936  246.640 -23.398 1.00 59.52  ? 63  HIS G CG  1 
ATOM   7182  N  ND1 . HIS G  1 64  ? 16.024  247.492 -23.331 1.00 57.01  ? 63  HIS G ND1 1 
ATOM   7183  C  CD2 . HIS G  1 64  ? 14.853  246.027 -22.178 1.00 58.42  ? 63  HIS G CD2 1 
ATOM   7184  C  CE1 . HIS G  1 64  ? 16.577  247.383 -22.125 1.00 60.99  ? 63  HIS G CE1 1 
ATOM   7185  N  NE2 . HIS G  1 64  ? 15.884  246.509 -21.406 1.00 55.68  ? 63  HIS G NE2 1 
ATOM   7186  N  N   . PHE G  1 65  ? 10.904  246.771 -25.648 1.00 46.94  ? 64  PHE G N   1 
ATOM   7187  C  CA  . PHE G  1 65  ? 10.105  247.013 -26.819 1.00 48.14  ? 64  PHE G CA  1 
ATOM   7188  C  C   . PHE G  1 65  ? 11.033  247.630 -27.863 1.00 55.71  ? 64  PHE G C   1 
ATOM   7189  O  O   . PHE G  1 65  ? 11.345  248.855 -27.788 1.00 51.56  ? 64  PHE G O   1 
ATOM   7190  C  CB  . PHE G  1 65  ? 9.058   248.035 -26.524 1.00 46.56  ? 64  PHE G CB  1 
ATOM   7191  C  CG  . PHE G  1 65  ? 8.119   248.289 -27.683 1.00 54.80  ? 64  PHE G CG  1 
ATOM   7192  C  CD1 . PHE G  1 65  ? 7.646   247.196 -28.503 1.00 58.44  ? 64  PHE G CD1 1 
ATOM   7193  C  CD2 . PHE G  1 65  ? 7.607   249.587 -27.910 1.00 50.99  ? 64  PHE G CD2 1 
ATOM   7194  C  CE1 . PHE G  1 65  ? 6.718   247.439 -29.528 1.00 60.18  ? 64  PHE G CE1 1 
ATOM   7195  C  CE2 . PHE G  1 65  ? 6.684   249.826 -28.936 1.00 53.76  ? 64  PHE G CE2 1 
ATOM   7196  C  CZ  . PHE G  1 65  ? 6.236   248.759 -29.734 1.00 59.16  ? 64  PHE G CZ  1 
ATOM   7197  N  N   . ASN G  1 66  ? 11.470  246.787 -28.811 1.00 58.59  ? 65  ASN G N   1 
ATOM   7198  C  CA  . ASN G  1 66  ? 12.576  247.161 -29.696 1.00 66.99  ? 65  ASN G CA  1 
ATOM   7199  C  C   . ASN G  1 66  ? 12.318  247.257 -31.166 1.00 80.29  ? 65  ASN G C   1 
ATOM   7200  O  O   . ASN G  1 66  ? 12.861  246.367 -31.908 1.00 73.04  ? 65  ASN G O   1 
ATOM   7201  C  CB  . ASN G  1 66  ? 13.805  246.262 -29.623 1.00 58.91  ? 65  ASN G CB  1 
ATOM   7202  C  CG  . ASN G  1 66  ? 14.969  246.932 -30.343 1.00 68.69  ? 65  ASN G CG  1 
ATOM   7203  O  OD1 . ASN G  1 66  ? 14.783  248.016 -30.984 1.00 62.82  ? 65  ASN G OD1 1 
ATOM   7204  N  ND2 . ASN G  1 66  ? 16.158  246.355 -30.234 1.00 69.25  ? 65  ASN G ND2 1 
ATOM   7205  N  N   . PRO G  1 67  ? 11.574  248.315 -31.622 1.00 87.07  ? 66  PRO G N   1 
ATOM   7206  C  CA  . PRO G  1 67  ? 11.461  248.544 -33.126 1.00 90.64  ? 66  PRO G CA  1 
ATOM   7207  C  C   . PRO G  1 67  ? 12.580  249.534 -33.699 1.00 95.58  ? 66  PRO G C   1 
ATOM   7208  O  O   . PRO G  1 67  ? 13.711  249.696 -33.107 1.00 69.99  ? 66  PRO G O   1 
ATOM   7209  C  CB  . PRO G  1 67  ? 9.990   249.074 -33.314 1.00 76.26  ? 66  PRO G CB  1 
ATOM   7210  C  CG  . PRO G  1 67  ? 9.495   249.398 -31.922 1.00 79.90  ? 66  PRO G CG  1 
ATOM   7211  C  CD  . PRO G  1 67  ? 10.662  249.218 -30.897 1.00 77.25  ? 66  PRO G CD  1 
ATOM   7212  N  N   . ARG G  1 80  ? 19.264  251.160 -27.904 1.00 67.93  ? 79  ARG G N   1 
ATOM   7213  C  CA  . ARG G  1 80  ? 18.089  252.078 -28.022 1.00 69.54  ? 79  ARG G CA  1 
ATOM   7214  C  C   . ARG G  1 80  ? 16.888  251.393 -28.743 1.00 69.79  ? 79  ARG G C   1 
ATOM   7215  O  O   . ARG G  1 80  ? 16.938  251.052 -29.948 1.00 70.56  ? 79  ARG G O   1 
ATOM   7216  C  CB  . ARG G  1 80  ? 18.478  253.454 -28.665 1.00 65.03  ? 79  ARG G CB  1 
ATOM   7217  C  CG  . ARG G  1 80  ? 18.133  254.695 -27.827 1.00 62.23  ? 79  ARG G CG  1 
ATOM   7218  C  CD  . ARG G  1 80  ? 16.724  255.161 -28.120 1.00 64.09  ? 79  ARG G CD  1 
ATOM   7219  N  NE  . ARG G  1 80  ? 16.425  256.491 -27.531 1.00 75.46  ? 79  ARG G NE  1 
ATOM   7220  C  CZ  . ARG G  1 80  ? 15.209  256.861 -27.031 1.00 80.15  ? 79  ARG G CZ  1 
ATOM   7221  N  NH1 . ARG G  1 80  ? 14.161  256.008 -26.990 1.00 70.25  ? 79  ARG G NH1 1 
ATOM   7222  N  NH2 . ARG G  1 80  ? 14.991  258.099 -26.545 1.00 64.36  ? 79  ARG G NH2 1 
ATOM   7223  N  N   . HIS G  1 81  ? 15.814  251.191 -27.987 1.00 67.62  ? 80  HIS G N   1 
ATOM   7224  C  CA  . HIS G  1 81  ? 14.527  250.620 -28.477 1.00 59.45  ? 80  HIS G CA  1 
ATOM   7225  C  C   . HIS G  1 81  ? 13.519  251.716 -28.260 1.00 54.75  ? 80  HIS G C   1 
ATOM   7226  O  O   . HIS G  1 81  ? 13.914  252.761 -27.711 1.00 52.19  ? 80  HIS G O   1 
ATOM   7227  C  CB  . HIS G  1 81  ? 14.154  249.519 -27.515 1.00 57.47  ? 80  HIS G CB  1 
ATOM   7228  C  CG  . HIS G  1 81  ? 13.761  250.023 -26.144 1.00 61.82  ? 80  HIS G CG  1 
ATOM   7229  N  ND1 . HIS G  1 81  ? 14.697  250.260 -25.141 1.00 58.49  ? 80  HIS G ND1 1 
ATOM   7230  C  CD2 . HIS G  1 81  ? 12.548  250.365 -25.626 1.00 52.54  ? 80  HIS G CD2 1 
ATOM   7231  C  CE1 . HIS G  1 81  ? 14.065  250.657 -24.051 1.00 53.32  ? 80  HIS G CE1 1 
ATOM   7232  N  NE2 . HIS G  1 81  ? 12.767  250.749 -24.322 1.00 51.07  ? 80  HIS G NE2 1 
ATOM   7233  N  N   . VAL G  1 82  ? 12.223  251.480 -28.537 1.00 56.40  ? 81  VAL G N   1 
ATOM   7234  C  CA  . VAL G  1 82  ? 11.287  252.610 -28.442 1.00 58.70  ? 81  VAL G CA  1 
ATOM   7235  C  C   . VAL G  1 82  ? 11.353  253.258 -27.064 1.00 65.23  ? 81  VAL G C   1 
ATOM   7236  O  O   . VAL G  1 82  ? 12.016  254.294 -26.929 1.00 64.92  ? 81  VAL G O   1 
ATOM   7237  C  CB  . VAL G  1 82  ? 9.843   252.339 -28.952 1.00 60.20  ? 81  VAL G CB  1 
ATOM   7238  C  CG1 . VAL G  1 82  ? 8.873   253.515 -28.659 1.00 51.99  ? 81  VAL G CG1 1 
ATOM   7239  C  CG2 . VAL G  1 82  ? 9.905   252.175 -30.450 1.00 62.60  ? 81  VAL G CG2 1 
ATOM   7240  N  N   . GLY G  1 83  ? 10.743  252.651 -26.043 1.00 69.22  ? 82  GLY G N   1 
ATOM   7241  C  CA  . GLY G  1 83  ? 10.684  253.310 -24.718 1.00 72.28  ? 82  GLY G CA  1 
ATOM   7242  C  C   . GLY G  1 83  ? 11.901  253.156 -23.809 1.00 69.19  ? 82  GLY G C   1 
ATOM   7243  O  O   . GLY G  1 83  ? 11.804  252.507 -22.752 1.00 56.84  ? 82  GLY G O   1 
ATOM   7244  N  N   . ASP G  1 84  ? 13.066  253.662 -24.248 1.00 64.18  ? 83  ASP G N   1 
ATOM   7245  C  CA  . ASP G  1 84  ? 14.282  253.586 -23.424 1.00 57.54  ? 83  ASP G CA  1 
ATOM   7246  C  C   . ASP G  1 84  ? 14.186  254.879 -22.713 1.00 56.99  ? 83  ASP G C   1 
ATOM   7247  O  O   . ASP G  1 84  ? 14.566  255.922 -23.263 1.00 61.98  ? 83  ASP G O   1 
ATOM   7248  C  CB  . ASP G  1 84  ? 15.563  253.529 -24.279 1.00 56.96  ? 83  ASP G CB  1 
ATOM   7249  C  CG  . ASP G  1 84  ? 16.850  253.574 -23.428 1.00 71.91  ? 83  ASP G CG  1 
ATOM   7250  O  OD1 . ASP G  1 84  ? 16.796  253.841 -22.189 1.00 77.54  ? 83  ASP G OD1 1 
ATOM   7251  O  OD2 . ASP G  1 84  ? 17.944  253.312 -23.989 1.00 68.20  ? 83  ASP G OD2 1 
ATOM   7252  N  N   . LEU G  1 85  ? 13.668  254.865 -21.508 1.00 48.73  ? 84  LEU G N   1 
ATOM   7253  C  CA  . LEU G  1 85  ? 13.535  256.151 -20.838 1.00 51.17  ? 84  LEU G CA  1 
ATOM   7254  C  C   . LEU G  1 85  ? 14.808  256.318 -20.026 1.00 55.59  ? 84  LEU G C   1 
ATOM   7255  O  O   . LEU G  1 85  ? 14.921  257.227 -19.175 1.00 58.17  ? 84  LEU G O   1 
ATOM   7256  C  CB  . LEU G  1 85  ? 12.237  256.201 -20.014 1.00 51.58  ? 84  LEU G CB  1 
ATOM   7257  C  CG  . LEU G  1 85  ? 11.107  255.458 -20.775 1.00 56.66  ? 84  LEU G CG  1 
ATOM   7258  C  CD1 . LEU G  1 85  ? 9.782   255.323 -20.028 1.00 54.15  ? 84  LEU G CD1 1 
ATOM   7259  C  CD2 . LEU G  1 85  ? 10.884  256.132 -22.115 1.00 54.12  ? 84  LEU G CD2 1 
ATOM   7260  N  N   . GLY G  1 86  ? 15.773  255.424 -20.280 1.00 48.85  ? 85  GLY G N   1 
ATOM   7261  C  CA  . GLY G  1 86  ? 17.063  255.492 -19.572 1.00 55.84  ? 85  GLY G CA  1 
ATOM   7262  C  C   . GLY G  1 86  ? 17.001  255.090 -18.105 1.00 56.87  ? 85  GLY G C   1 
ATOM   7263  O  O   . GLY G  1 86  ? 16.908  253.890 -17.811 1.00 55.86  ? 85  GLY G O   1 
ATOM   7264  N  N   . ASN G  1 87  ? 17.082  256.064 -17.196 1.00 50.43  ? 86  ASN G N   1 
ATOM   7265  C  CA  . ASN G  1 87  ? 17.311  255.729 -15.795 1.00 46.32  ? 86  ASN G CA  1 
ATOM   7266  C  C   . ASN G  1 87  ? 16.495  256.676 -14.886 1.00 48.41  ? 86  ASN G C   1 
ATOM   7267  O  O   . ASN G  1 87  ? 16.479  257.890 -15.103 1.00 45.41  ? 86  ASN G O   1 
ATOM   7268  C  CB  . ASN G  1 87  ? 18.739  255.987 -15.399 1.00 44.92  ? 86  ASN G CB  1 
ATOM   7269  C  CG  . ASN G  1 87  ? 19.731  254.853 -15.704 1.00 54.36  ? 86  ASN G CG  1 
ATOM   7270  O  OD1 . ASN G  1 87  ? 19.653  253.720 -15.177 1.00 49.82  ? 86  ASN G OD1 1 
ATOM   7271  N  ND2 . ASN G  1 87  ? 20.806  255.227 -16.440 1.00 53.17  ? 86  ASN G ND2 1 
ATOM   7272  N  N   . VAL G  1 88  ? 15.842  256.142 -13.855 1.00 42.30  ? 87  VAL G N   1 
ATOM   7273  C  CA  . VAL G  1 88  ? 15.314  257.035 -12.806 1.00 47.13  ? 87  VAL G CA  1 
ATOM   7274  C  C   . VAL G  1 88  ? 16.253  257.082 -11.595 1.00 43.23  ? 87  VAL G C   1 
ATOM   7275  O  O   . VAL G  1 88  ? 17.135  256.233 -11.461 1.00 40.30  ? 87  VAL G O   1 
ATOM   7276  C  CB  . VAL G  1 88  ? 13.858  256.687 -12.416 1.00 50.12  ? 87  VAL G CB  1 
ATOM   7277  C  CG1 . VAL G  1 88  ? 12.946  257.054 -13.585 1.00 49.64  ? 87  VAL G CG1 1 
ATOM   7278  C  CG2 . VAL G  1 88  ? 13.702  255.193 -12.025 1.00 44.84  ? 87  VAL G CG2 1 
ATOM   7279  N  N   . THR G  1 89  ? 16.030  258.042 -10.719 1.00 40.06  ? 88  THR G N   1 
ATOM   7280  C  CA  . THR G  1 89  ? 16.955  258.272 -9.638  1.00 42.71  ? 88  THR G CA  1 
ATOM   7281  C  C   . THR G  1 89  ? 16.166  258.383 -8.377  1.00 45.77  ? 88  THR G C   1 
ATOM   7282  O  O   . THR G  1 89  ? 15.392  259.328 -8.205  1.00 48.49  ? 88  THR G O   1 
ATOM   7283  C  CB  . THR G  1 89  ? 17.678  259.622 -9.804  1.00 46.54  ? 88  THR G CB  1 
ATOM   7284  O  OG1 . THR G  1 89  ? 18.351  259.637 -11.074 1.00 47.53  ? 88  THR G OG1 1 
ATOM   7285  C  CG2 . THR G  1 89  ? 18.712  259.831 -8.641  1.00 41.25  ? 88  THR G CG2 1 
ATOM   7286  N  N   . ALA G  1 90  ? 16.328  257.432 -7.473  1.00 47.31  ? 89  ALA G N   1 
ATOM   7287  C  CA  . ALA G  1 90  ? 15.618  257.574 -6.222  1.00 43.68  ? 89  ALA G CA  1 
ATOM   7288  C  C   . ALA G  1 90  ? 16.597  258.287 -5.293  1.00 41.43  ? 89  ALA G C   1 
ATOM   7289  O  O   . ALA G  1 90  ? 17.808  257.923 -5.200  1.00 38.53  ? 89  ALA G O   1 
ATOM   7290  C  CB  . ALA G  1 90  ? 15.210  256.234 -5.664  1.00 42.69  ? 89  ALA G CB  1 
ATOM   7291  N  N   . ASP G  1 91  ? 16.014  259.288 -4.638  1.00 38.39  ? 90  ASP G N   1 
ATOM   7292  C  CA  . ASP G  1 91  ? 16.564  260.032 -3.553  1.00 37.45  ? 90  ASP G CA  1 
ATOM   7293  C  C   . ASP G  1 91  ? 16.843  259.173 -2.300  1.00 41.50  ? 90  ASP G C   1 
ATOM   7294  O  O   . ASP G  1 91  ? 16.673  257.981 -2.318  1.00 43.14  ? 90  ASP G O   1 
ATOM   7295  C  CB  . ASP G  1 91  ? 15.598  261.176 -3.269  1.00 36.18  ? 90  ASP G CB  1 
ATOM   7296  C  CG  . ASP G  1 91  ? 14.350  260.759 -2.462  1.00 45.74  ? 90  ASP G CG  1 
ATOM   7297  O  OD1 . ASP G  1 91  ? 14.273  259.729 -1.776  1.00 45.81  ? 90  ASP G OD1 1 
ATOM   7298  O  OD2 . ASP G  1 91  ? 13.395  261.549 -2.444  1.00 55.47  ? 90  ASP G OD2 1 
ATOM   7299  N  N   . LYS G  1 92  ? 17.217  259.772 -1.185  1.00 44.79  ? 91  LYS G N   1 
ATOM   7300  C  CA  . LYS G  1 92  ? 17.635  258.966 -0.017  1.00 51.30  ? 91  LYS G CA  1 
ATOM   7301  C  C   . LYS G  1 92  ? 16.426  258.333 0.738   1.00 50.84  ? 91  LYS G C   1 
ATOM   7302  O  O   . LYS G  1 92  ? 16.613  257.469 1.590   1.00 46.87  ? 91  LYS G O   1 
ATOM   7303  C  CB  . LYS G  1 92  ? 18.519  259.779 0.932   1.00 46.77  ? 91  LYS G CB  1 
ATOM   7304  C  CG  . LYS G  1 92  ? 17.866  261.112 1.289   1.00 52.57  ? 91  LYS G CG  1 
ATOM   7305  C  CD  . LYS G  1 92  ? 18.046  261.518 2.743   1.00 54.82  ? 91  LYS G CD  1 
ATOM   7306  C  CE  . LYS G  1 92  ? 17.252  262.822 2.946   1.00 57.65  ? 91  LYS G CE  1 
ATOM   7307  N  NZ  . LYS G  1 92  ? 18.048  263.903 3.651   1.00 58.75  ? 91  LYS G NZ  1 
ATOM   7308  N  N   . ASP G  1 93  ? 15.217  258.781 0.419   1.00 46.82  ? 92  ASP G N   1 
ATOM   7309  C  CA  . ASP G  1 93  ? 14.001  258.152 0.926   1.00 45.60  ? 92  ASP G CA  1 
ATOM   7310  C  C   . ASP G  1 93  ? 13.446  257.081 0.039   1.00 42.84  ? 92  ASP G C   1 
ATOM   7311  O  O   . ASP G  1 93  ? 12.329  256.672 0.291   1.00 41.68  ? 92  ASP G O   1 
ATOM   7312  C  CB  . ASP G  1 93  ? 12.949  259.193 1.089   1.00 42.52  ? 92  ASP G CB  1 
ATOM   7313  C  CG  . ASP G  1 93  ? 13.347  260.170 2.107   1.00 59.16  ? 92  ASP G CG  1 
ATOM   7314  O  OD1 . ASP G  1 93  ? 14.075  259.768 3.065   1.00 64.18  ? 92  ASP G OD1 1 
ATOM   7315  O  OD2 . ASP G  1 93  ? 12.990  261.349 1.955   1.00 63.66  ? 92  ASP G OD2 1 
ATOM   7316  N  N   . GLY G  1 94  ? 14.226  256.652 -0.973  1.00 42.66  ? 93  GLY G N   1 
ATOM   7317  C  CA  . GLY G  1 94  ? 13.825  255.668 -1.999  1.00 44.28  ? 93  GLY G CA  1 
ATOM   7318  C  C   . GLY G  1 94  ? 12.755  256.133 -2.985  1.00 45.44  ? 93  GLY G C   1 
ATOM   7319  O  O   . GLY G  1 94  ? 12.059  255.298 -3.584  1.00 43.08  ? 93  GLY G O   1 
ATOM   7320  N  N   . VAL G  1 95  ? 12.618  257.449 -3.134  1.00 40.40  ? 94  VAL G N   1 
ATOM   7321  C  CA  . VAL G  1 95  ? 11.571  258.008 -3.948  1.00 42.09  ? 94  VAL G CA  1 
ATOM   7322  C  C   . VAL G  1 95  ? 12.207  258.649 -5.166  1.00 47.69  ? 94  VAL G C   1 
ATOM   7323  O  O   . VAL G  1 95  ? 12.882  259.710 -5.044  1.00 48.65  ? 94  VAL G O   1 
ATOM   7324  C  CB  . VAL G  1 95  ? 10.740  259.073 -3.193  1.00 38.33  ? 94  VAL G CB  1 
ATOM   7325  C  CG1 . VAL G  1 95  ? 9.682   259.612 -4.106  1.00 32.27  ? 94  VAL G CG1 1 
ATOM   7326  C  CG2 . VAL G  1 95  ? 10.066  258.441 -1.990  1.00 35.16  ? 94  VAL G CG2 1 
ATOM   7327  N  N   . ALA G  1 96  ? 11.989  257.992 -6.312  1.00 42.59  ? 95  ALA G N   1 
ATOM   7328  C  CA  . ALA G  1 96  ? 12.227  258.564 -7.630  1.00 42.82  ? 95  ALA G CA  1 
ATOM   7329  C  C   . ALA G  1 96  ? 11.048  259.373 -8.221  1.00 44.61  ? 95  ALA G C   1 
ATOM   7330  O  O   . ALA G  1 96  ? 10.065  258.819 -8.740  1.00 50.59  ? 95  ALA G O   1 
ATOM   7331  C  CB  . ALA G  1 96  ? 12.617  257.472 -8.577  1.00 40.19  ? 95  ALA G CB  1 
ATOM   7332  N  N   . ASP G  1 97  ? 11.152  260.691 -8.156  1.00 45.78  ? 96  ASP G N   1 
ATOM   7333  C  CA  . ASP G  1 97  ? 10.343  261.580 -9.000  1.00 46.37  ? 96  ASP G CA  1 
ATOM   7334  C  C   . ASP G  1 97  ? 10.695  261.557 -10.488 1.00 45.44  ? 96  ASP G C   1 
ATOM   7335  O  O   . ASP G  1 97  ? 11.865  261.644 -10.845 1.00 42.63  ? 96  ASP G O   1 
ATOM   7336  C  CB  . ASP G  1 97  ? 10.252  262.956 -8.368  1.00 45.69  ? 96  ASP G CB  1 
ATOM   7337  C  CG  . ASP G  1 97  ? 9.422   262.880 -7.031  1.00 68.46  ? 96  ASP G CG  1 
ATOM   7338  O  OD1 . ASP G  1 97  ? 8.256   262.331 -7.051  1.00 63.78  ? 96  ASP G OD1 1 
ATOM   7339  O  OD2 . ASP G  1 97  ? 9.932   263.275 -5.929  1.00 73.07  ? 96  ASP G OD2 1 
ATOM   7340  N  N   . VAL G  1 98  ? 9.681   261.324 -11.331 1.00 41.24  ? 97  VAL G N   1 
ATOM   7341  C  CA  . VAL G  1 98  ? 9.887   261.223 -12.768 1.00 38.54  ? 97  VAL G CA  1 
ATOM   7342  C  C   . VAL G  1 98  ? 9.232   262.388 -13.477 1.00 43.47  ? 97  VAL G C   1 
ATOM   7343  O  O   . VAL G  1 98  ? 8.054   262.678 -13.235 1.00 43.90  ? 97  VAL G O   1 
ATOM   7344  C  CB  . VAL G  1 98  ? 9.322   259.937 -13.312 1.00 36.25  ? 97  VAL G CB  1 
ATOM   7345  C  CG1 . VAL G  1 98  ? 9.482   259.905 -14.807 1.00 37.96  ? 97  VAL G CG1 1 
ATOM   7346  C  CG2 . VAL G  1 98  ? 10.065  258.779 -12.702 1.00 36.37  ? 97  VAL G CG2 1 
ATOM   7347  N  N   . SER G  1 99  ? 10.016  263.077 -14.309 1.00 48.89  ? 98  SER G N   1 
ATOM   7348  C  CA  . SER G  1 99  ? 9.532   264.147 -15.229 1.00 51.07  ? 98  SER G CA  1 
ATOM   7349  C  C   . SER G  1 99  ? 10.379  264.150 -16.519 1.00 54.82  ? 98  SER G C   1 
ATOM   7350  O  O   . SER G  1 99  ? 11.359  264.845 -16.627 1.00 57.35  ? 98  SER G O   1 
ATOM   7351  C  CB  . SER G  1 99  ? 9.649   265.499 -14.552 1.00 51.53  ? 98  SER G CB  1 
ATOM   7352  O  OG  . SER G  1 99  ? 8.461   266.292 -14.742 1.00 54.38  ? 98  SER G OG  1 
ATOM   7353  N  N   . ILE G  1 100 ? 10.031  263.303 -17.454 1.00 53.43  ? 99  ILE G N   1 
ATOM   7354  C  CA  . ILE G  1 100 ? 10.778  263.109 -18.651 1.00 56.71  ? 99  ILE G CA  1 
ATOM   7355  C  C   . ILE G  1 100 ? 9.939   263.499 -19.904 1.00 62.57  ? 99  ILE G C   1 
ATOM   7356  O  O   . ILE G  1 100 ? 8.710   263.667 -19.836 1.00 59.50  ? 99  ILE G O   1 
ATOM   7357  C  CB  . ILE G  1 100 ? 11.169  261.642 -18.660 1.00 58.14  ? 99  ILE G CB  1 
ATOM   7358  C  CG1 . ILE G  1 100 ? 12.364  261.520 -17.735 1.00 64.77  ? 99  ILE G CG1 1 
ATOM   7359  C  CG2 . ILE G  1 100 ? 11.404  261.072 -20.075 1.00 50.09  ? 99  ILE G CG2 1 
ATOM   7360  C  CD1 . ILE G  1 100 ? 12.718  260.056 -17.376 1.00 77.71  ? 99  ILE G CD1 1 
ATOM   7361  N  N   . GLU G  1 101 ? 10.609  263.651 -21.046 1.00 57.50  ? 100 GLU G N   1 
ATOM   7362  C  CA  . GLU G  1 101 ? 9.921   263.927 -22.309 1.00 56.67  ? 100 GLU G CA  1 
ATOM   7363  C  C   . GLU G  1 101 ? 10.576  263.075 -23.401 1.00 55.36  ? 100 GLU G C   1 
ATOM   7364  O  O   . GLU G  1 101 ? 11.840  263.065 -23.527 1.00 51.94  ? 100 GLU G O   1 
ATOM   7365  C  CB  . GLU G  1 101 ? 9.965   265.397 -22.619 1.00 53.69  ? 100 GLU G CB  1 
ATOM   7366  C  CG  . GLU G  1 101 ? 8.817   265.707 -23.522 1.00 69.68  ? 100 GLU G CG  1 
ATOM   7367  C  CD  . GLU G  1 101 ? 8.355   267.146 -23.423 1.00 81.52  ? 100 GLU G CD  1 
ATOM   7368  O  OE1 . GLU G  1 101 ? 8.580   267.840 -24.452 1.00 72.14  ? 100 GLU G OE1 1 
ATOM   7369  O  OE2 . GLU G  1 101 ? 7.773   267.561 -22.339 1.00 77.16  ? 100 GLU G OE2 1 
ATOM   7370  N  N   . ASP G  1 102 ? 9.766   262.255 -24.091 1.00 53.27  ? 101 ASP G N   1 
ATOM   7371  C  CA  . ASP G  1 102 ? 10.361  261.228 -24.987 1.00 55.88  ? 101 ASP G CA  1 
ATOM   7372  C  C   . ASP G  1 102 ? 9.706   261.348 -26.304 1.00 66.64  ? 101 ASP G C   1 
ATOM   7373  O  O   . ASP G  1 102 ? 8.450   261.367 -26.396 1.00 61.89  ? 101 ASP G O   1 
ATOM   7374  C  CB  . ASP G  1 102 ? 10.262  259.774 -24.539 1.00 53.58  ? 101 ASP G CB  1 
ATOM   7375  C  CG  . ASP G  1 102 ? 11.234  258.892 -25.287 1.00 60.98  ? 101 ASP G CG  1 
ATOM   7376  O  OD1 . ASP G  1 102 ? 12.424  259.263 -25.286 1.00 76.00  ? 101 ASP G OD1 1 
ATOM   7377  O  OD2 . ASP G  1 102 ? 10.890  257.845 -25.888 1.00 61.08  ? 101 ASP G OD2 1 
ATOM   7378  N  N   . SER G  1 103 ? 10.600  261.453 -27.292 1.00 67.84  ? 102 SER G N   1 
ATOM   7379  C  CA  . SER G  1 103 ? 10.289  261.755 -28.675 1.00 63.40  ? 102 SER G CA  1 
ATOM   7380  C  C   . SER G  1 103 ? 10.060  260.486 -29.370 1.00 57.25  ? 102 SER G C   1 
ATOM   7381  O  O   . SER G  1 103 ? 9.315   260.488 -30.320 1.00 60.34  ? 102 SER G O   1 
ATOM   7382  C  CB  . SER G  1 103 ? 11.464  262.458 -29.383 1.00 60.06  ? 102 SER G CB  1 
ATOM   7383  O  OG  . SER G  1 103 ? 11.233  263.856 -29.287 1.00 63.14  ? 102 SER G OG  1 
ATOM   7384  N  N   . VAL G  1 104 ? 10.722  259.413 -28.941 1.00 52.88  ? 103 VAL G N   1 
ATOM   7385  C  CA  . VAL G  1 104 ? 10.562  258.133 -29.644 1.00 53.63  ? 103 VAL G CA  1 
ATOM   7386  C  C   . VAL G  1 104 ? 9.204   257.417 -29.401 1.00 60.75  ? 103 VAL G C   1 
ATOM   7387  O  O   . VAL G  1 104 ? 8.527   256.940 -30.347 1.00 67.25  ? 103 VAL G O   1 
ATOM   7388  C  CB  . VAL G  1 104 ? 11.738  257.238 -29.329 1.00 56.67  ? 103 VAL G CB  1 
ATOM   7389  C  CG1 . VAL G  1 104 ? 11.629  255.883 -30.066 1.00 54.65  ? 103 VAL G CG1 1 
ATOM   7390  C  CG2 . VAL G  1 104 ? 13.017  258.012 -29.684 1.00 53.00  ? 103 VAL G CG2 1 
ATOM   7391  N  N   . ILE G  1 105 ? 8.784   257.360 -28.142 1.00 55.85  ? 104 ILE G N   1 
ATOM   7392  C  CA  . ILE G  1 105 ? 7.554   256.627 -27.771 1.00 49.63  ? 104 ILE G CA  1 
ATOM   7393  C  C   . ILE G  1 105 ? 6.327   257.362 -28.288 1.00 51.90  ? 104 ILE G C   1 
ATOM   7394  O  O   . ILE G  1 105 ? 6.354   258.598 -28.459 1.00 51.32  ? 104 ILE G O   1 
ATOM   7395  C  CB  . ILE G  1 105 ? 7.471   256.377 -26.208 1.00 44.31  ? 104 ILE G CB  1 
ATOM   7396  C  CG1 . ILE G  1 105 ? 7.310   257.695 -25.429 1.00 39.11  ? 104 ILE G CG1 1 
ATOM   7397  C  CG2 . ILE G  1 105 ? 8.674   255.544 -25.738 1.00 43.14  ? 104 ILE G CG2 1 
ATOM   7398  C  CD1 . ILE G  1 105 ? 6.963   257.592 -23.936 1.00 41.11  ? 104 ILE G CD1 1 
ATOM   7399  N  N   . SER G  1 106 ? 5.224   256.632 -28.443 1.00 51.00  ? 105 SER G N   1 
ATOM   7400  C  CA  . SER G  1 106 ? 3.928   257.284 -28.701 1.00 50.49  ? 105 SER G CA  1 
ATOM   7401  C  C   . SER G  1 106 ? 2.734   256.565 -28.066 1.00 48.25  ? 105 SER G C   1 
ATOM   7402  O  O   . SER G  1 106 ? 2.758   255.350 -27.789 1.00 47.22  ? 105 SER G O   1 
ATOM   7403  C  CB  . SER G  1 106 ? 3.696   257.373 -30.240 1.00 51.95  ? 105 SER G CB  1 
ATOM   7404  O  OG  . SER G  1 106 ? 2.685   258.305 -30.530 1.00 47.77  ? 105 SER G OG  1 
ATOM   7405  N  N   . LEU G  1 107 ? 1.644   257.303 -27.925 1.00 46.62  ? 106 LEU G N   1 
ATOM   7406  C  CA  . LEU G  1 107 ? 0.394   256.683 -27.503 1.00 48.43  ? 106 LEU G CA  1 
ATOM   7407  C  C   . LEU G  1 107 ? -0.427  256.273 -28.758 1.00 50.72  ? 106 LEU G C   1 
ATOM   7408  O  O   . LEU G  1 107 ? -1.657  256.208 -28.725 1.00 53.00  ? 106 LEU G O   1 
ATOM   7409  C  CB  . LEU G  1 107 ? -0.400  257.646 -26.596 1.00 46.44  ? 106 LEU G CB  1 
ATOM   7410  C  CG  . LEU G  1 107 ? 0.317   258.203 -25.368 1.00 52.50  ? 106 LEU G CG  1 
ATOM   7411  C  CD1 . LEU G  1 107 ? -0.638  258.919 -24.393 1.00 49.70  ? 106 LEU G CD1 1 
ATOM   7412  C  CD2 . LEU G  1 107 ? 1.222   257.141 -24.711 1.00 48.88  ? 106 LEU G CD2 1 
ATOM   7413  N  N   . SER G  1 108 ? 0.227   256.071 -29.883 1.00 51.59  ? 107 SER G N   1 
ATOM   7414  C  CA  . SER G  1 108 ? -0.488  255.653 -31.095 1.00 61.25  ? 107 SER G CA  1 
ATOM   7415  C  C   . SER G  1 108 ? 0.562   255.473 -32.130 1.00 65.02  ? 107 SER G C   1 
ATOM   7416  O  O   . SER G  1 108 ? 1.801   255.577 -31.856 1.00 64.50  ? 107 SER G O   1 
ATOM   7417  C  CB  . SER G  1 108 ? -1.418  256.756 -31.645 1.00 63.25  ? 107 SER G CB  1 
ATOM   7418  O  OG  . SER G  1 108 ? -0.604  257.857 -32.085 1.00 74.03  ? 107 SER G OG  1 
ATOM   7419  N  N   . GLY G  1 109 ? 0.062   255.266 -33.348 1.00 58.30  ? 108 GLY G N   1 
ATOM   7420  C  CA  . GLY G  1 109 ? 0.969   255.137 -34.468 1.00 64.08  ? 108 GLY G CA  1 
ATOM   7421  C  C   . GLY G  1 109 ? 1.664   253.842 -34.169 1.00 59.61  ? 108 GLY G C   1 
ATOM   7422  O  O   . GLY G  1 109 ? 1.039   252.994 -33.532 1.00 58.92  ? 108 GLY G O   1 
ATOM   7423  N  N   . ASP G  1 110 ? 2.938   253.709 -34.581 1.00 61.71  ? 109 ASP G N   1 
ATOM   7424  C  CA  . ASP G  1 110 ? 3.597   252.347 -34.696 1.00 71.60  ? 109 ASP G CA  1 
ATOM   7425  C  C   . ASP G  1 110 ? 4.544   252.087 -33.530 1.00 66.01  ? 109 ASP G C   1 
ATOM   7426  O  O   . ASP G  1 110 ? 4.982   250.937 -33.268 1.00 55.67  ? 109 ASP G O   1 
ATOM   7427  C  CB  . ASP G  1 110 ? 4.337   252.177 -36.067 1.00 78.15  ? 109 ASP G CB  1 
ATOM   7428  C  CG  . ASP G  1 110 ? 3.457   252.674 -37.274 1.00 89.46  ? 109 ASP G CG  1 
ATOM   7429  O  OD1 . ASP G  1 110 ? 2.404   252.007 -37.571 1.00 77.62  ? 109 ASP G OD1 1 
ATOM   7430  O  OD2 . ASP G  1 110 ? 3.768   253.754 -37.890 1.00 72.12  ? 109 ASP G OD2 1 
ATOM   7431  N  N   . HIS G  1 111 ? 4.875   253.204 -32.878 1.00 60.05  ? 110 HIS G N   1 
ATOM   7432  C  CA  . HIS G  1 111 ? 5.540   253.223 -31.570 1.00 61.79  ? 110 HIS G CA  1 
ATOM   7433  C  C   . HIS G  1 111 ? 4.493   253.288 -30.369 1.00 57.86  ? 110 HIS G C   1 
ATOM   7434  O  O   . HIS G  1 111 ? 4.726   254.002 -29.365 1.00 49.01  ? 110 HIS G O   1 
ATOM   7435  C  CB  . HIS G  1 111 ? 6.557   254.391 -31.590 1.00 59.49  ? 110 HIS G CB  1 
ATOM   7436  C  CG  . HIS G  1 111 ? 7.665   254.196 -32.580 1.00 58.55  ? 110 HIS G CG  1 
ATOM   7437  N  ND1 . HIS G  1 111 ? 8.776   255.014 -32.627 1.00 58.23  ? 110 HIS G ND1 1 
ATOM   7438  C  CD2 . HIS G  1 111 ? 7.835   253.269 -33.562 1.00 57.29  ? 110 HIS G CD2 1 
ATOM   7439  C  CE1 . HIS G  1 111 ? 9.596   254.580 -33.577 1.00 59.80  ? 110 HIS G CE1 1 
ATOM   7440  N  NE2 . HIS G  1 111 ? 9.053   253.513 -34.147 1.00 56.54  ? 110 HIS G NE2 1 
ATOM   7441  N  N   . CYS G  1 112 ? 3.362   252.544 -30.514 1.00 57.10  ? 111 CYS G N   1 
ATOM   7442  C  CA  . CYS G  1 112 ? 2.304   252.453 -29.489 1.00 52.11  ? 111 CYS G CA  1 
ATOM   7443  C  C   . CYS G  1 112 ? 2.936   251.720 -28.327 1.00 53.03  ? 111 CYS G C   1 
ATOM   7444  O  O   . CYS G  1 112 ? 3.394   250.513 -28.466 1.00 49.03  ? 111 CYS G O   1 
ATOM   7445  C  CB  . CYS G  1 112 ? 1.072   251.643 -29.933 1.00 54.54  ? 111 CYS G CB  1 
ATOM   7446  S  SG  . CYS G  1 112 ? -0.423  252.252 -29.060 1.00 60.61  ? 111 CYS G SG  1 
ATOM   7447  N  N   . ILE G  1 113 ? 2.997   252.442 -27.193 1.00 48.27  ? 112 ILE G N   1 
ATOM   7448  C  CA  . ILE G  1 113 ? 3.349   251.758 -25.930 1.00 49.12  ? 112 ILE G CA  1 
ATOM   7449  C  C   . ILE G  1 113 ? 2.140   251.187 -25.115 1.00 51.54  ? 112 ILE G C   1 
ATOM   7450  O  O   . ILE G  1 113 ? 2.343   250.273 -24.279 1.00 51.82  ? 112 ILE G O   1 
ATOM   7451  C  CB  . ILE G  1 113 ? 4.382   252.531 -25.103 1.00 43.35  ? 112 ILE G CB  1 
ATOM   7452  C  CG1 . ILE G  1 113 ? 3.785   253.842 -24.584 1.00 40.06  ? 112 ILE G CG1 1 
ATOM   7453  C  CG2 . ILE G  1 113 ? 5.677   252.645 -25.896 1.00 40.11  ? 112 ILE G CG2 1 
ATOM   7454  C  CD1 . ILE G  1 113 ? 4.760   254.570 -23.681 1.00 40.35  ? 112 ILE G CD1 1 
ATOM   7455  N  N   . ILE G  1 114 ? 0.911   251.688 -25.392 1.00 47.14  ? 113 ILE G N   1 
ATOM   7456  C  CA  . ILE G  1 114 ? -0.351  251.161 -24.797 1.00 44.60  ? 113 ILE G CA  1 
ATOM   7457  C  C   . ILE G  1 114 ? -0.408  249.650 -24.930 1.00 46.05  ? 113 ILE G C   1 
ATOM   7458  O  O   . ILE G  1 114 ? -0.317  249.179 -26.031 1.00 43.04  ? 113 ILE G O   1 
ATOM   7459  C  CB  . ILE G  1 114 ? -1.607  251.682 -25.522 1.00 40.90  ? 113 ILE G CB  1 
ATOM   7460  C  CG1 . ILE G  1 114 ? -1.542  253.186 -25.761 1.00 42.52  ? 113 ILE G CG1 1 
ATOM   7461  C  CG2 . ILE G  1 114 ? -2.843  251.360 -24.731 1.00 35.89  ? 113 ILE G CG2 1 
ATOM   7462  C  CD1 . ILE G  1 114 ? -1.954  254.094 -24.608 1.00 42.64  ? 113 ILE G CD1 1 
ATOM   7463  N  N   . GLY G  1 115 ? -0.551  248.898 -23.825 1.00 48.57  ? 114 GLY G N   1 
ATOM   7464  C  CA  . GLY G  1 115 ? -0.764  247.430 -23.885 1.00 39.81  ? 114 GLY G CA  1 
ATOM   7465  C  C   . GLY G  1 115 ? 0.562   246.693 -23.733 1.00 41.48  ? 114 GLY G C   1 
ATOM   7466  O  O   . GLY G  1 115 ? 0.637   245.465 -23.774 1.00 39.71  ? 114 GLY G O   1 
ATOM   7467  N  N   . ARG G  1 116 ? 1.613   247.478 -23.530 1.00 40.83  ? 115 ARG G N   1 
ATOM   7468  C  CA  . ARG G  1 116 ? 2.952   246.971 -23.178 1.00 46.73  ? 115 ARG G CA  1 
ATOM   7469  C  C   . ARG G  1 116 ? 3.214   247.188 -21.697 1.00 43.30  ? 115 ARG G C   1 
ATOM   7470  O  O   . ARG G  1 116 ? 2.355   247.756 -21.023 1.00 42.21  ? 115 ARG G O   1 
ATOM   7471  C  CB  . ARG G  1 116 ? 3.998   247.696 -24.074 1.00 48.01  ? 115 ARG G CB  1 
ATOM   7472  C  CG  . ARG G  1 116 ? 3.456   247.673 -25.515 1.00 41.13  ? 115 ARG G CG  1 
ATOM   7473  C  CD  . ARG G  1 116 ? 4.469   247.690 -26.605 1.00 47.82  ? 115 ARG G CD  1 
ATOM   7474  N  NE  . ARG G  1 116 ? 3.791   247.473 -27.902 1.00 52.11  ? 115 ARG G NE  1 
ATOM   7475  C  CZ  . ARG G  1 116 ? 3.796   246.344 -28.638 1.00 43.12  ? 115 ARG G CZ  1 
ATOM   7476  N  NH1 . ARG G  1 116 ? 4.464   245.240 -28.325 1.00 38.12  ? 115 ARG G NH1 1 
ATOM   7477  N  NH2 . ARG G  1 116 ? 3.124   246.351 -29.748 1.00 43.34  ? 115 ARG G NH2 1 
ATOM   7478  N  N   . THR G  1 117 ? 4.390   246.779 -21.208 1.00 40.21  ? 116 THR G N   1 
ATOM   7479  C  CA  . THR G  1 117 ? 4.755   246.840 -19.764 1.00 39.65  ? 116 THR G CA  1 
ATOM   7480  C  C   . THR G  1 117 ? 5.889   247.841 -19.502 1.00 40.46  ? 116 THR G C   1 
ATOM   7481  O  O   . THR G  1 117 ? 6.863   247.866 -20.214 1.00 43.75  ? 116 THR G O   1 
ATOM   7482  C  CB  . THR G  1 117 ? 5.129   245.442 -19.191 1.00 42.16  ? 116 THR G CB  1 
ATOM   7483  O  OG1 . THR G  1 117 ? 4.104   244.488 -19.534 1.00 44.91  ? 116 THR G OG1 1 
ATOM   7484  C  CG2 . THR G  1 117 ? 5.310   245.440 -17.659 1.00 40.36  ? 116 THR G CG2 1 
ATOM   7485  N  N   . LEU G  1 118 ? 5.719   248.706 -18.509 1.00 42.08  ? 117 LEU G N   1 
ATOM   7486  C  CA  . LEU G  1 118 ? 6.769   249.579 -18.016 1.00 36.03  ? 117 LEU G CA  1 
ATOM   7487  C  C   . LEU G  1 118 ? 7.363   248.776 -16.891 1.00 37.79  ? 117 LEU G C   1 
ATOM   7488  O  O   . LEU G  1 118 ? 6.641   248.175 -16.128 1.00 39.90  ? 117 LEU G O   1 
ATOM   7489  C  CB  . LEU G  1 118 ? 6.102   250.849 -17.537 1.00 35.06  ? 117 LEU G CB  1 
ATOM   7490  C  CG  . LEU G  1 118 ? 7.059   251.956 -17.182 1.00 38.98  ? 117 LEU G CG  1 
ATOM   7491  C  CD1 . LEU G  1 118 ? 7.784   252.474 -18.393 1.00 38.08  ? 117 LEU G CD1 1 
ATOM   7492  C  CD2 . LEU G  1 118 ? 6.363   253.112 -16.510 1.00 37.53  ? 117 LEU G CD2 1 
ATOM   7493  N  N   . VAL G  1 119 ? 8.676   248.699 -16.848 1.00 40.37  ? 118 VAL G N   1 
ATOM   7494  C  CA  . VAL G  1 119 ? 9.480   248.004 -15.827 1.00 37.00  ? 118 VAL G CA  1 
ATOM   7495  C  C   . VAL G  1 119 ? 10.513  248.991 -15.235 1.00 41.43  ? 118 VAL G C   1 
ATOM   7496  O  O   . VAL G  1 119 ? 11.207  249.707 -15.962 1.00 39.45  ? 118 VAL G O   1 
ATOM   7497  C  CB  . VAL G  1 119 ? 10.264  246.842 -16.419 1.00 38.58  ? 118 VAL G CB  1 
ATOM   7498  C  CG1 . VAL G  1 119 ? 10.994  246.057 -15.332 1.00 37.74  ? 118 VAL G CG1 1 
ATOM   7499  C  CG2 . VAL G  1 119 ? 9.356   245.908 -17.228 1.00 37.16  ? 118 VAL G CG2 1 
ATOM   7500  N  N   . VAL G  1 120 ? 10.562  249.071 -13.905 1.00 43.19  ? 119 VAL G N   1 
ATOM   7501  C  CA  . VAL G  1 120 ? 11.693  249.668 -13.252 1.00 40.33  ? 119 VAL G CA  1 
ATOM   7502  C  C   . VAL G  1 120 ? 12.638  248.547 -12.840 1.00 38.14  ? 119 VAL G C   1 
ATOM   7503  O  O   . VAL G  1 120 ? 12.180  247.532 -12.420 1.00 38.50  ? 119 VAL G O   1 
ATOM   7504  C  CB  . VAL G  1 120 ? 11.320  250.636 -12.151 1.00 38.70  ? 119 VAL G CB  1 
ATOM   7505  C  CG1 . VAL G  1 120 ? 10.372  249.977 -11.206 1.00 43.13  ? 119 VAL G CG1 1 
ATOM   7506  C  CG2 . VAL G  1 120 ? 12.588  251.097 -11.439 1.00 42.16  ? 119 VAL G CG2 1 
ATOM   7507  N  N   . HIS G  1 121 ? 13.944  248.708 -13.091 1.00 41.12  ? 120 HIS G N   1 
ATOM   7508  C  CA  . HIS G  1 121 ? 14.930  247.635 -12.918 1.00 39.46  ? 120 HIS G CA  1 
ATOM   7509  C  C   . HIS G  1 121 ? 15.759  247.923 -11.728 1.00 41.27  ? 120 HIS G C   1 
ATOM   7510  O  O   . HIS G  1 121 ? 15.888  249.082 -11.331 1.00 42.48  ? 120 HIS G O   1 
ATOM   7511  C  CB  . HIS G  1 121 ? 15.807  247.499 -14.105 1.00 36.52  ? 120 HIS G CB  1 
ATOM   7512  C  CG  . HIS G  1 121 ? 15.094  246.963 -15.292 1.00 44.12  ? 120 HIS G CG  1 
ATOM   7513  N  ND1 . HIS G  1 121 ? 15.176  245.636 -15.683 1.00 45.52  ? 120 HIS G ND1 1 
ATOM   7514  C  CD2 . HIS G  1 121 ? 14.251  247.561 -16.163 1.00 43.43  ? 120 HIS G CD2 1 
ATOM   7515  C  CE1 . HIS G  1 121 ? 14.472  245.457 -16.787 1.00 42.64  ? 120 HIS G CE1 1 
ATOM   7516  N  NE2 . HIS G  1 121 ? 13.893  246.608 -17.096 1.00 45.92  ? 120 HIS G NE2 1 
ATOM   7517  N  N   . GLU G  1 122 ? 16.264  246.860 -11.116 1.00 41.48  ? 121 GLU G N   1 
ATOM   7518  C  CA  . GLU G  1 122 ? 16.986  247.011 -9.886  1.00 46.82  ? 121 GLU G CA  1 
ATOM   7519  C  C   . GLU G  1 122 ? 18.332  247.618 -10.213 1.00 51.56  ? 121 GLU G C   1 
ATOM   7520  O  O   . GLU G  1 122 ? 18.837  248.417 -9.442  1.00 52.50  ? 121 GLU G O   1 
ATOM   7521  C  CB  . GLU G  1 122 ? 17.119  245.678 -9.203  1.00 49.00  ? 121 GLU G CB  1 
ATOM   7522  C  CG  . GLU G  1 122 ? 18.259  245.497 -8.195  1.00 57.78  ? 121 GLU G CG  1 
ATOM   7523  C  CD  . GLU G  1 122 ? 18.858  244.119 -8.420  1.00 64.76  ? 121 GLU G CD  1 
ATOM   7524  O  OE1 . GLU G  1 122 ? 19.041  243.838 -9.644  1.00 54.68  ? 121 GLU G OE1 1 
ATOM   7525  O  OE2 . GLU G  1 122 ? 19.083  243.321 -7.441  1.00 59.58  ? 121 GLU G OE2 1 
ATOM   7526  N  N   . LYS G  1 123 ? 18.873  247.265 -11.374 1.00 52.07  ? 122 LYS G N   1 
ATOM   7527  C  CA  . LYS G  1 123 ? 20.195  247.701 -11.744 1.00 54.01  ? 122 LYS G CA  1 
ATOM   7528  C  C   . LYS G  1 123 ? 20.104  248.925 -12.645 1.00 63.07  ? 122 LYS G C   1 
ATOM   7529  O  O   . LYS G  1 123 ? 19.261  248.975 -13.596 1.00 54.76  ? 122 LYS G O   1 
ATOM   7530  C  CB  . LYS G  1 123 ? 20.958  246.588 -12.464 1.00 50.65  ? 122 LYS G CB  1 
ATOM   7531  C  CG  . LYS G  1 123 ? 22.379  246.425 -11.940 1.00 54.94  ? 122 LYS G CG  1 
ATOM   7532  C  CD  . LYS G  1 123 ? 22.419  246.585 -10.409 1.00 55.71  ? 122 LYS G CD  1 
ATOM   7533  C  CE  . LYS G  1 123 ? 22.639  245.226 -9.701  1.00 64.45  ? 122 LYS G CE  1 
ATOM   7534  N  NZ  . LYS G  1 123 ? 22.758  245.169 -8.182  1.00 53.71  ? 122 LYS G NZ  1 
ATOM   7535  N  N   . ALA G  1 124 ? 21.001  249.888 -12.373 1.00 62.24  ? 123 ALA G N   1 
ATOM   7536  C  CA  . ALA G  1 124 ? 21.114  251.070 -13.206 1.00 58.16  ? 123 ALA G CA  1 
ATOM   7537  C  C   . ALA G  1 124 ? 21.555  250.600 -14.590 1.00 58.52  ? 123 ALA G C   1 
ATOM   7538  O  O   . ALA G  1 124 ? 22.218  249.556 -14.792 1.00 55.46  ? 123 ALA G O   1 
ATOM   7539  C  CB  . ALA G  1 124 ? 22.086  252.064 -12.614 1.00 60.61  ? 123 ALA G CB  1 
ATOM   7540  N  N   . ASP G  1 125 ? 21.068  251.318 -15.564 1.00 56.14  ? 124 ASP G N   1 
ATOM   7541  C  CA  . ASP G  1 125 ? 21.401  251.031 -16.922 1.00 60.78  ? 124 ASP G CA  1 
ATOM   7542  C  C   . ASP G  1 125 ? 22.570  252.031 -17.190 1.00 72.51  ? 124 ASP G C   1 
ATOM   7543  O  O   . ASP G  1 125 ? 22.467  253.260 -16.917 1.00 67.04  ? 124 ASP G O   1 
ATOM   7544  C  CB  . ASP G  1 125 ? 20.143  251.377 -17.729 1.00 70.09  ? 124 ASP G CB  1 
ATOM   7545  C  CG  . ASP G  1 125 ? 20.354  251.240 -19.190 1.00 87.21  ? 124 ASP G CG  1 
ATOM   7546  O  OD1 . ASP G  1 125 ? 21.561  251.063 -19.567 1.00 80.61  ? 124 ASP G OD1 1 
ATOM   7547  O  OD2 . ASP G  1 125 ? 19.339  251.305 -19.958 1.00 75.22  ? 124 ASP G OD2 1 
ATOM   7548  N  N   . ASP G  1 126 ? 23.709  251.515 -17.671 1.00 79.44  ? 125 ASP G N   1 
ATOM   7549  C  CA  . ASP G  1 126 ? 24.906  252.390 -18.018 1.00 77.85  ? 125 ASP G CA  1 
ATOM   7550  C  C   . ASP G  1 126 ? 24.847  253.193 -19.359 1.00 65.83  ? 125 ASP G C   1 
ATOM   7551  O  O   . ASP G  1 126 ? 25.627  254.122 -19.524 1.00 64.81  ? 125 ASP G O   1 
ATOM   7552  C  CB  . ASP G  1 126 ? 26.220  251.580 -17.966 1.00 74.11  ? 125 ASP G CB  1 
ATOM   7553  C  CG  . ASP G  1 126 ? 26.209  250.311 -18.894 1.00 82.62  ? 125 ASP G CG  1 
ATOM   7554  O  OD1 . ASP G  1 126 ? 25.566  250.264 -20.007 1.00 71.56  ? 125 ASP G OD1 1 
ATOM   7555  O  OD2 . ASP G  1 126 ? 26.917  249.339 -18.497 1.00 87.23  ? 125 ASP G OD2 1 
ATOM   7556  N  N   . LEU G  1 127 ? 23.939  252.800 -20.278 1.00 68.04  ? 126 LEU G N   1 
ATOM   7557  C  CA  . LEU G  1 127 ? 23.791  253.326 -21.678 1.00 73.69  ? 126 LEU G CA  1 
ATOM   7558  C  C   . LEU G  1 127 ? 25.072  253.173 -22.531 1.00 85.79  ? 126 LEU G C   1 
ATOM   7559  O  O   . LEU G  1 127 ? 25.100  252.456 -23.567 1.00 88.48  ? 126 LEU G O   1 
ATOM   7560  C  CB  . LEU G  1 127 ? 23.249  254.789 -21.717 1.00 76.25  ? 126 LEU G CB  1 
ATOM   7561  C  CG  . LEU G  1 127 ? 22.014  255.232 -20.871 1.00 79.32  ? 126 LEU G CG  1 
ATOM   7562  C  CD1 . LEU G  1 127 ? 21.951  256.760 -20.748 1.00 80.05  ? 126 LEU G CD1 1 
ATOM   7563  C  CD2 . LEU G  1 127 ? 20.650  254.655 -21.335 1.00 88.84  ? 126 LEU G CD2 1 
ATOM   7564  N  N   . GLY G  1 142 ? 18.742  244.988 -14.010 1.00 63.40  ? 141 GLY G N   1 
ATOM   7565  C  CA  . GLY G  1 142 ? 19.174  243.682 -13.418 1.00 66.49  ? 141 GLY G CA  1 
ATOM   7566  C  C   . GLY G  1 142 ? 17.981  242.707 -13.206 1.00 74.26  ? 141 GLY G C   1 
ATOM   7567  O  O   . GLY G  1 142 ? 17.489  242.098 -14.187 1.00 67.03  ? 141 GLY G O   1 
ATOM   7568  N  N   . SER G  1 143 ? 17.496  242.545 -11.961 1.00 55.61  ? 142 SER G N   1 
ATOM   7569  C  CA  . SER G  1 143 ? 16.223  241.880 -11.735 1.00 51.91  ? 142 SER G CA  1 
ATOM   7570  C  C   . SER G  1 143 ? 15.027  242.920 -11.910 1.00 52.47  ? 142 SER G C   1 
ATOM   7571  O  O   . SER G  1 143 ? 15.222  244.158 -11.779 1.00 46.13  ? 142 SER G O   1 
ATOM   7572  C  CB  . SER G  1 143 ? 16.202  241.219 -10.357 1.00 50.81  ? 142 SER G CB  1 
ATOM   7573  O  OG  . SER G  1 143 ? 15.746  242.198 -9.454  1.00 50.43  ? 142 SER G OG  1 
ATOM   7574  N  N   . ARG G  1 144 ? 13.807  242.442 -12.193 1.00 41.22  ? 143 ARG G N   1 
ATOM   7575  C  CA  . ARG G  1 144 ? 12.795  243.395 -12.454 1.00 39.12  ? 143 ARG G CA  1 
ATOM   7576  C  C   . ARG G  1 144 ? 12.001  243.725 -11.226 1.00 42.99  ? 143 ARG G C   1 
ATOM   7577  O  O   . ARG G  1 144 ? 11.259  242.897 -10.803 1.00 49.38  ? 143 ARG G O   1 
ATOM   7578  C  CB  . ARG G  1 144 ? 11.923  242.865 -13.503 1.00 40.76  ? 143 ARG G CB  1 
ATOM   7579  C  CG  . ARG G  1 144 ? 12.704  242.718 -14.784 1.00 44.64  ? 143 ARG G CG  1 
ATOM   7580  C  CD  . ARG G  1 144 ? 11.956  241.858 -15.776 1.00 39.18  ? 143 ARG G CD  1 
ATOM   7581  N  NE  . ARG G  1 144 ? 12.672  241.851 -17.044 1.00 46.79  ? 143 ARG G NE  1 
ATOM   7582  C  CZ  . ARG G  1 144 ? 12.182  241.463 -18.224 1.00 47.68  ? 143 ARG G CZ  1 
ATOM   7583  N  NH1 . ARG G  1 144 ? 10.926  241.027 -18.399 1.00 47.25  ? 143 ARG G NH1 1 
ATOM   7584  N  NH2 . ARG G  1 144 ? 12.968  241.513 -19.253 1.00 45.29  ? 143 ARG G NH2 1 
ATOM   7585  N  N   . LEU G  1 145 ? 12.123  244.932 -10.673 1.00 38.21  ? 144 LEU G N   1 
ATOM   7586  C  CA  . LEU G  1 145 ? 11.535  245.250 -9.384  1.00 39.98  ? 144 LEU G CA  1 
ATOM   7587  C  C   . LEU G  1 145 ? 10.039  245.477 -9.412  1.00 41.22  ? 144 LEU G C   1 
ATOM   7588  O  O   . LEU G  1 145 ? 9.330   245.058 -8.506  1.00 43.76  ? 144 LEU G O   1 
ATOM   7589  C  CB  . LEU G  1 145 ? 12.189  246.516 -8.787  1.00 41.91  ? 144 LEU G CB  1 
ATOM   7590  C  CG  . LEU G  1 145 ? 13.668  246.467 -8.389  1.00 40.80  ? 144 LEU G CG  1 
ATOM   7591  C  CD1 . LEU G  1 145 ? 13.995  247.731 -7.703  1.00 42.40  ? 144 LEU G CD1 1 
ATOM   7592  C  CD2 . LEU G  1 145 ? 13.990  245.338 -7.429  1.00 39.71  ? 144 LEU G CD2 1 
ATOM   7593  N  N   . ALA G  1 146 ? 9.550   246.198 -10.408 1.00 38.03  ? 145 ALA G N   1 
ATOM   7594  C  CA  . ALA G  1 146 ? 8.114   246.428 -10.540 1.00 38.20  ? 145 ALA G CA  1 
ATOM   7595  C  C   . ALA G  1 146 ? 7.753   246.654 -11.983 1.00 42.24  ? 145 ALA G C   1 
ATOM   7596  O  O   . ALA G  1 146 ? 8.604   247.055 -12.821 1.00 39.15  ? 145 ALA G O   1 
ATOM   7597  C  CB  . ALA G  1 146 ? 7.661   247.614 -9.693  1.00 34.16  ? 145 ALA G CB  1 
ATOM   7598  N  N   . CYS G  1 147 ? 6.484   246.410 -12.274 1.00 42.68  ? 146 CYS G N   1 
ATOM   7599  C  CA  . CYS G  1 147 ? 5.990   246.623 -13.607 1.00 41.13  ? 146 CYS G CA  1 
ATOM   7600  C  C   . CYS G  1 147 ? 4.502   246.819 -13.620 1.00 40.81  ? 146 CYS G C   1 
ATOM   7601  O  O   . CYS G  1 147 ? 3.849   246.550 -12.638 1.00 44.45  ? 146 CYS G O   1 
ATOM   7602  C  CB  . CYS G  1 147 ? 6.364   245.474 -14.501 1.00 36.24  ? 146 CYS G CB  1 
ATOM   7603  S  SG  . CYS G  1 147 ? 5.687   243.960 -13.916 1.00 40.71  ? 146 CYS G SG  1 
ATOM   7604  N  N   . GLY G  1 148 ? 3.990   247.318 -14.739 1.00 41.08  ? 147 GLY G N   1 
ATOM   7605  C  CA  . GLY G  1 148 ? 2.579   247.385 -14.954 1.00 40.47  ? 147 GLY G CA  1 
ATOM   7606  C  C   . GLY G  1 148 ? 2.328   247.618 -16.410 1.00 47.02  ? 147 GLY G C   1 
ATOM   7607  O  O   . GLY G  1 148 ? 3.182   248.140 -17.150 1.00 43.14  ? 147 GLY G O   1 
ATOM   7608  N  N   . VAL G  1 149 ? 1.117   247.272 -16.798 1.00 46.24  ? 148 VAL G N   1 
ATOM   7609  C  CA  . VAL G  1 149 ? 0.606   247.533 -18.138 1.00 39.79  ? 148 VAL G CA  1 
ATOM   7610  C  C   . VAL G  1 149 ? 0.214   248.983 -18.304 1.00 38.67  ? 148 VAL G C   1 
ATOM   7611  O  O   . VAL G  1 149 ? -0.269  249.620 -17.386 1.00 40.26  ? 148 VAL G O   1 
ATOM   7612  C  CB  . VAL G  1 149 ? -0.525  246.545 -18.536 1.00 39.78  ? 148 VAL G CB  1 
ATOM   7613  C  CG1 . VAL G  1 149 ? -0.685  246.555 -20.042 1.00 37.61  ? 148 VAL G CG1 1 
ATOM   7614  C  CG2 . VAL G  1 149 ? -0.160  245.114 -18.131 1.00 31.29  ? 148 VAL G CG2 1 
ATOM   7615  N  N   . ILE G  1 150 ? 0.494   249.506 -19.490 1.00 40.56  ? 149 ILE G N   1 
ATOM   7616  C  CA  . ILE G  1 150 ? 0.331   250.915 -19.789 1.00 39.59  ? 149 ILE G CA  1 
ATOM   7617  C  C   . ILE G  1 150 ? -1.011  250.919 -20.449 1.00 39.15  ? 149 ILE G C   1 
ATOM   7618  O  O   . ILE G  1 150 ? -1.172  250.185 -21.436 1.00 38.75  ? 149 ILE G O   1 
ATOM   7619  C  CB  . ILE G  1 150 ? 1.382   251.433 -20.790 1.00 37.67  ? 149 ILE G CB  1 
ATOM   7620  C  CG1 . ILE G  1 150 ? 2.800   250.993 -20.301 1.00 35.38  ? 149 ILE G CG1 1 
ATOM   7621  C  CG2 . ILE G  1 150 ? 1.081   252.909 -21.108 1.00 29.62  ? 149 ILE G CG2 1 
ATOM   7622  C  CD1 . ILE G  1 150 ? 4.018   251.624 -20.933 1.00 33.76  ? 149 ILE G CD1 1 
ATOM   7623  N  N   . GLY G  1 151 ? -1.942  251.673 -19.859 1.00 34.65  ? 150 GLY G N   1 
ATOM   7624  C  CA  . GLY G  1 151 ? -3.358  251.588 -20.154 1.00 39.87  ? 150 GLY G CA  1 
ATOM   7625  C  C   . GLY G  1 151 ? -3.884  252.949 -20.531 1.00 42.40  ? 150 GLY G C   1 
ATOM   7626  O  O   . GLY G  1 151 ? -3.274  253.975 -20.180 1.00 42.74  ? 150 GLY G O   1 
ATOM   7627  N  N   . ILE G  1 152 ? -4.954  252.973 -21.324 1.00 43.42  ? 151 ILE G N   1 
ATOM   7628  C  CA  . ILE G  1 152 ? -5.549  254.260 -21.718 1.00 45.03  ? 151 ILE G CA  1 
ATOM   7629  C  C   . ILE G  1 152 ? -6.138  254.937 -20.470 1.00 46.03  ? 151 ILE G C   1 
ATOM   7630  O  O   . ILE G  1 152 ? -6.824  254.265 -19.695 1.00 44.33  ? 151 ILE G O   1 
ATOM   7631  C  CB  . ILE G  1 152 ? -6.665  254.115 -22.782 1.00 44.49  ? 151 ILE G CB  1 
ATOM   7632  C  CG1 . ILE G  1 152 ? -6.091  253.709 -24.114 1.00 46.46  ? 151 ILE G CG1 1 
ATOM   7633  C  CG2 . ILE G  1 152 ? -7.415  255.429 -23.014 1.00 45.10  ? 151 ILE G CG2 1 
ATOM   7634  C  CD1 . ILE G  1 152 ? -6.924  252.671 -24.853 1.00 50.84  ? 151 ILE G CD1 1 
ATOM   7635  N  N   . ALA G  1 153 ? -5.842  256.236 -20.279 1.00 43.85  ? 152 ALA G N   1 
ATOM   7636  C  CA  . ALA G  1 153 ? -6.505  257.069 -19.262 1.00 47.53  ? 152 ALA G CA  1 
ATOM   7637  C  C   . ALA G  1 153 ? -7.378  258.118 -19.885 1.00 45.57  ? 152 ALA G C   1 
ATOM   7638  O  O   . ALA G  1 153 ? -7.124  258.596 -20.967 1.00 44.85  ? 152 ALA G O   1 
ATOM   7639  C  CB  . ALA G  1 153 ? -5.526  257.737 -18.250 1.00 43.96  ? 152 ALA G CB  1 
ATOM   7640  N  N   . GLN G  1 154 ? -8.404  258.474 -19.131 1.00 53.37  ? 153 GLN G N   1 
ATOM   7641  C  CA  . GLN G  1 154 ? -9.317  259.573 -19.435 1.00 61.87  ? 153 GLN G CA  1 
ATOM   7642  C  C   . GLN G  1 154 ? -8.575  260.920 -19.565 1.00 75.79  ? 153 GLN G C   1 
ATOM   7643  O  O   . GLN G  1 154 ? -7.968  261.459 -18.571 1.00 63.65  ? 153 GLN G O   1 
ATOM   7644  C  CB  . GLN G  1 154 ? -10.356 259.665 -18.316 1.00 56.69  ? 153 GLN G CB  1 
ATOM   7645  C  CG  . GLN G  1 154 ? -11.271 260.893 -18.258 1.00 49.83  ? 153 GLN G CG  1 
ATOM   7646  C  CD  . GLN G  1 154 ? -12.258 260.622 -17.117 1.00 63.09  ? 153 GLN G CD  1 
ATOM   7647  O  OE1 . GLN G  1 154 ? -11.808 260.386 -15.967 1.00 59.97  ? 153 GLN G OE1 1 
ATOM   7648  N  NE2 . GLN G  1 154 ? -13.589 260.535 -17.421 1.00 55.35  ? 153 GLN G NE2 1 
ATOM   7649  O  OXT . GLN G  1 154 ? -8.579  261.463 -20.699 1.00 71.69  ? 153 GLN G OXT 1 
ATOM   7650  N  N   . ALA H  1 2   ? -1.716  243.198 -33.494 1.00 52.95  ? 1   ALA H N   1 
ATOM   7651  C  CA  . ALA H  1 2   ? -2.020  242.417 -32.201 1.00 54.90  ? 1   ALA H CA  1 
ATOM   7652  C  C   . ALA H  1 2   ? -3.009  241.226 -32.413 1.00 51.30  ? 1   ALA H C   1 
ATOM   7653  O  O   . ALA H  1 2   ? -4.134  241.443 -32.832 1.00 49.06  ? 1   ALA H O   1 
ATOM   7654  C  CB  . ALA H  1 2   ? -2.597  243.368 -31.164 1.00 52.85  ? 1   ALA H CB  1 
ATOM   7655  N  N   . THR H  1 3   ? -2.603  239.983 -32.170 1.00 50.32  ? 2   THR H N   1 
ATOM   7656  C  CA  . THR H  1 3   ? -3.507  238.814 -32.391 1.00 47.09  ? 2   THR H CA  1 
ATOM   7657  C  C   . THR H  1 3   ? -3.741  237.940 -31.094 1.00 43.15  ? 2   THR H C   1 
ATOM   7658  O  O   . THR H  1 3   ? -4.675  237.114 -31.013 1.00 43.70  ? 2   THR H O   1 
ATOM   7659  C  CB  . THR H  1 3   ? -3.035  237.910 -33.593 1.00 48.77  ? 2   THR H CB  1 
ATOM   7660  O  OG1 . THR H  1 3   ? -2.055  236.942 -33.154 1.00 49.85  ? 2   THR H OG1 1 
ATOM   7661  C  CG2 . THR H  1 3   ? -2.448  238.706 -34.761 1.00 47.39  ? 2   THR H CG2 1 
ATOM   7662  N  N   . LYS H  1 4   ? -2.855  238.069 -30.120 1.00 42.11  ? 3   LYS H N   1 
ATOM   7663  C  CA  . LYS H  1 4   ? -3.061  237.462 -28.800 1.00 44.70  ? 3   LYS H CA  1 
ATOM   7664  C  C   . LYS H  1 4   ? -3.028  238.576 -27.729 1.00 42.31  ? 3   LYS H C   1 
ATOM   7665  O  O   . LYS H  1 4   ? -2.267  239.528 -27.853 1.00 41.84  ? 3   LYS H O   1 
ATOM   7666  C  CB  . LYS H  1 4   ? -2.034  236.392 -28.533 1.00 47.32  ? 3   LYS H CB  1 
ATOM   7667  C  CG  . LYS H  1 4   ? -2.491  234.952 -28.753 1.00 56.15  ? 3   LYS H CG  1 
ATOM   7668  C  CD  . LYS H  1 4   ? -1.304  233.954 -28.937 1.00 55.50  ? 3   LYS H CD  1 
ATOM   7669  C  CE  . LYS H  1 4   ? -1.672  232.487 -28.620 1.00 62.13  ? 3   LYS H CE  1 
ATOM   7670  N  NZ  . LYS H  1 4   ? -1.850  232.189 -27.146 1.00 59.22  ? 3   LYS H NZ  1 
ATOM   7671  N  N   . ALA H  1 5   ? -3.933  238.525 -26.748 1.00 39.68  ? 4   ALA H N   1 
ATOM   7672  C  CA  . ALA H  1 5   ? -3.845  239.405 -25.554 1.00 35.57  ? 4   ALA H CA  1 
ATOM   7673  C  C   . ALA H  1 5   ? -4.086  238.639 -24.233 1.00 36.53  ? 4   ALA H C   1 
ATOM   7674  O  O   . ALA H  1 5   ? -4.459  237.416 -24.211 1.00 33.27  ? 4   ALA H O   1 
ATOM   7675  C  CB  . ALA H  1 5   ? -4.730  240.634 -25.688 1.00 32.10  ? 4   ALA H CB  1 
ATOM   7676  N  N   . VAL H  1 6   ? -3.785  239.315 -23.125 1.00 34.43  ? 5   VAL H N   1 
ATOM   7677  C  CA  . VAL H  1 6   ? -3.819  238.645 -21.827 1.00 34.74  ? 5   VAL H CA  1 
ATOM   7678  C  C   . VAL H  1 6   ? -4.167  239.635 -20.732 1.00 35.21  ? 5   VAL H C   1 
ATOM   7679  O  O   . VAL H  1 6   ? -3.804  240.793 -20.824 1.00 37.35  ? 5   VAL H O   1 
ATOM   7680  C  CB  . VAL H  1 6   ? -2.483  237.903 -21.557 1.00 31.75  ? 5   VAL H CB  1 
ATOM   7681  C  CG1 . VAL H  1 6   ? -1.387  238.877 -21.166 1.00 30.57  ? 5   VAL H CG1 1 
ATOM   7682  C  CG2 . VAL H  1 6   ? -2.679  236.857 -20.504 1.00 28.44  ? 5   VAL H CG2 1 
ATOM   7683  N  N   . CYS H  1 7   ? -4.874  239.179 -19.710 1.00 33.43  ? 6   CYS H N   1 
ATOM   7684  C  CA  . CYS H  1 7   ? -5.268  240.030 -18.643 1.00 32.69  ? 6   CYS H CA  1 
ATOM   7685  C  C   . CYS H  1 7   ? -5.071  239.315 -17.347 1.00 34.18  ? 6   CYS H C   1 
ATOM   7686  O  O   . CYS H  1 7   ? -5.638  238.192 -17.160 1.00 31.00  ? 6   CYS H O   1 
ATOM   7687  C  CB  . CYS H  1 7   ? -6.765  240.287 -18.736 1.00 34.34  ? 6   CYS H CB  1 
ATOM   7688  S  SG  . CYS H  1 7   ? -7.302  241.585 -17.605 1.00 37.50  ? 6   CYS H SG  1 
ATOM   7689  N  N   . VAL H  1 8   ? -4.370  239.984 -16.411 1.00 31.31  ? 7   VAL H N   1 
ATOM   7690  C  CA  . VAL H  1 8   ? -4.373  239.464 -15.044 1.00 32.25  ? 7   VAL H CA  1 
ATOM   7691  C  C   . VAL H  1 8   ? -5.310  240.161 -14.113 1.00 31.23  ? 7   VAL H C   1 
ATOM   7692  O  O   . VAL H  1 8   ? -5.172  241.343 -13.851 1.00 34.96  ? 7   VAL H O   1 
ATOM   7693  C  CB  . VAL H  1 8   ? -2.971  239.410 -14.410 1.00 37.19  ? 7   VAL H CB  1 
ATOM   7694  C  CG1 . VAL H  1 8   ? -3.116  238.844 -12.988 1.00 32.45  ? 7   VAL H CG1 1 
ATOM   7695  C  CG2 . VAL H  1 8   ? -1.973  238.607 -15.308 1.00 29.68  ? 7   VAL H CG2 1 
ATOM   7696  N  N   . LEU H  1 9   ? -6.266  239.439 -13.601 1.00 32.28  ? 8   LEU H N   1 
ATOM   7697  C  CA  . LEU H  1 9   ? -7.301  240.060 -12.762 1.00 34.30  ? 8   LEU H CA  1 
ATOM   7698  C  C   . LEU H  1 9   ? -7.049  239.927 -11.240 1.00 31.94  ? 8   LEU H C   1 
ATOM   7699  O  O   . LEU H  1 9   ? -6.932  238.820 -10.727 1.00 32.59  ? 8   LEU H O   1 
ATOM   7700  C  CB  . LEU H  1 9   ? -8.613  239.384 -13.079 1.00 35.79  ? 8   LEU H CB  1 
ATOM   7701  C  CG  . LEU H  1 9   ? -9.220  239.523 -14.456 1.00 39.21  ? 8   LEU H CG  1 
ATOM   7702  C  CD1 . LEU H  1 9   ? -10.440 238.649 -14.549 1.00 41.31  ? 8   LEU H CD1 1 
ATOM   7703  C  CD2 . LEU H  1 9   ? -9.733  240.929 -14.580 1.00 46.61  ? 8   LEU H CD2 1 
ATOM   7704  N  N   . LYS H  1 10  ? -6.947  241.050 -10.551 1.00 33.67  ? 9   LYS H N   1 
ATOM   7705  C  CA  . LYS H  1 10  ? -6.788  241.097 -9.082  1.00 39.01  ? 9   LYS H CA  1 
ATOM   7706  C  C   . LYS H  1 10  ? -7.821  241.987 -8.482  1.00 41.60  ? 9   LYS H C   1 
ATOM   7707  O  O   . LYS H  1 10  ? -8.295  242.929 -9.134  1.00 42.66  ? 9   LYS H O   1 
ATOM   7708  C  CB  . LYS H  1 10  ? -5.436  241.690 -8.666  1.00 36.77  ? 9   LYS H CB  1 
ATOM   7709  C  CG  . LYS H  1 10  ? -4.252  240.990 -9.278  1.00 43.83  ? 9   LYS H CG  1 
ATOM   7710  C  CD  . LYS H  1 10  ? -3.981  239.597 -8.633  1.00 52.59  ? 9   LYS H CD  1 
ATOM   7711  C  CE  . LYS H  1 10  ? -2.637  238.985 -9.063  1.00 56.38  ? 9   LYS H CE  1 
ATOM   7712  N  NZ  . LYS H  1 10  ? -1.624  240.098 -9.321  1.00 50.69  ? 9   LYS H NZ  1 
ATOM   7713  N  N   . GLY H  1 11  ? -8.141  241.753 -7.213  1.00 43.65  ? 10  GLY H N   1 
ATOM   7714  C  CA  . GLY H  1 11  ? -8.950  242.748 -6.496  1.00 43.37  ? 10  GLY H CA  1 
ATOM   7715  C  C   . GLY H  1 11  ? -8.525  242.945 -5.068  1.00 43.03  ? 10  GLY H C   1 
ATOM   7716  O  O   . GLY H  1 11  ? -7.474  242.499 -4.665  1.00 40.66  ? 10  GLY H O   1 
ATOM   7717  N  N   . ASP H  1 12  ? -9.365  243.617 -4.293  1.00 45.80  ? 11  ASP H N   1 
ATOM   7718  C  CA  . ASP H  1 12  ? -9.199  243.626 -2.824  1.00 50.32  ? 11  ASP H CA  1 
ATOM   7719  C  C   . ASP H  1 12  ? -9.472  242.370 -2.094  1.00 47.39  ? 11  ASP H C   1 
ATOM   7720  O  O   . ASP H  1 12  ? -9.015  242.278 -0.986  1.00 55.96  ? 11  ASP H O   1 
ATOM   7721  C  CB  . ASP H  1 12  ? -10.037 244.695 -2.218  1.00 49.71  ? 11  ASP H CB  1 
ATOM   7722  C  CG  . ASP H  1 12  ? -9.633  246.006 -2.748  1.00 62.21  ? 11  ASP H CG  1 
ATOM   7723  O  OD1 . ASP H  1 12  ? -8.384  246.187 -2.967  1.00 65.19  ? 11  ASP H OD1 1 
ATOM   7724  O  OD2 . ASP H  1 12  ? -10.539 246.800 -3.045  1.00 57.22  ? 11  ASP H OD2 1 
ATOM   7725  N  N   . GLY H  1 13  ? -10.173 241.414 -2.691  1.00 37.92  ? 12  GLY H N   1 
ATOM   7726  C  CA  . GLY H  1 13  ? -10.553 240.243 -1.976  1.00 38.78  ? 12  GLY H CA  1 
ATOM   7727  C  C   . GLY H  1 13  ? -9.936  239.075 -2.653  1.00 45.18  ? 12  GLY H C   1 
ATOM   7728  O  O   . GLY H  1 13  ? -8.909  239.206 -3.334  1.00 47.69  ? 12  GLY H O   1 
ATOM   7729  N  N   . PRO H  1 14  ? -10.584 237.931 -2.529  1.00 40.93  ? 13  PRO H N   1 
ATOM   7730  C  CA  . PRO H  1 14  ? -9.957  236.706 -2.967  1.00 40.99  ? 13  PRO H CA  1 
ATOM   7731  C  C   . PRO H  1 14  ? -10.085 236.442 -4.495  1.00 43.27  ? 13  PRO H C   1 
ATOM   7732  O  O   . PRO H  1 14  ? -9.659  235.348 -4.957  1.00 39.11  ? 13  PRO H O   1 
ATOM   7733  C  CB  . PRO H  1 14  ? -10.788 235.650 -2.231  1.00 40.59  ? 13  PRO H CB  1 
ATOM   7734  C  CG  . PRO H  1 14  ? -12.191 236.224 -2.274  1.00 39.73  ? 13  PRO H CG  1 
ATOM   7735  C  CD  . PRO H  1 14  ? -11.977 237.731 -2.072  1.00 38.88  ? 13  PRO H CD  1 
ATOM   7736  N  N   . VAL H  1 15  ? -10.714 237.355 -5.254  1.00 36.53  ? 14  VAL H N   1 
ATOM   7737  C  CA  . VAL H  1 15  ? -11.009 237.017 -6.652  1.00 35.46  ? 14  VAL H CA  1 
ATOM   7738  C  C   . VAL H  1 15  ? -9.784  237.264 -7.554  1.00 35.61  ? 14  VAL H C   1 
ATOM   7739  O  O   . VAL H  1 15  ? -9.190  238.314 -7.538  1.00 33.72  ? 14  VAL H O   1 
ATOM   7740  C  CB  . VAL H  1 15  ? -12.217 237.762 -7.207  1.00 35.00  ? 14  VAL H CB  1 
ATOM   7741  C  CG1 . VAL H  1 15  ? -12.378 237.458 -8.671  1.00 37.54  ? 14  VAL H CG1 1 
ATOM   7742  C  CG2 . VAL H  1 15  ? -13.489 237.366 -6.519  1.00 34.77  ? 14  VAL H CG2 1 
ATOM   7743  N  N   . GLN H  1 16  ? -9.382  236.272 -8.330  1.00 39.71  ? 15  GLN H N   1 
ATOM   7744  C  CA  . GLN H  1 16  ? -8.223  236.443 -9.227  1.00 38.23  ? 15  GLN H CA  1 
ATOM   7745  C  C   . GLN H  1 16  ? -8.209  235.438 -10.367 1.00 34.78  ? 15  GLN H C   1 
ATOM   7746  O  O   . GLN H  1 16  ? -8.773  234.329 -10.246 1.00 37.27  ? 15  GLN H O   1 
ATOM   7747  C  CB  . GLN H  1 16  ? -6.944  236.367 -8.417  1.00 39.90  ? 15  GLN H CB  1 
ATOM   7748  C  CG  . GLN H  1 16  ? -6.738  235.013 -7.800  1.00 44.09  ? 15  GLN H CG  1 
ATOM   7749  C  CD  . GLN H  1 16  ? -5.278  234.836 -7.412  1.00 55.10  ? 15  GLN H CD  1 
ATOM   7750  O  OE1 . GLN H  1 16  ? -4.929  234.917 -6.218  1.00 45.50  ? 15  GLN H OE1 1 
ATOM   7751  N  NE2 . GLN H  1 16  ? -4.393  234.624 -8.434  1.00 59.99  ? 15  GLN H NE2 1 
ATOM   7752  N  N   . GLY H  1 17  ? -7.628  235.840 -11.492 1.00 33.01  ? 16  GLY H N   1 
ATOM   7753  C  CA  . GLY H  1 17  ? -7.506  234.907 -12.598 1.00 30.63  ? 16  GLY H CA  1 
ATOM   7754  C  C   . GLY H  1 17  ? -6.727  235.446 -13.727 1.00 28.80  ? 16  GLY H C   1 
ATOM   7755  O  O   . GLY H  1 17  ? -6.145  236.500 -13.631 1.00 27.53  ? 16  GLY H O   1 
ATOM   7756  N  N   . ILE H  1 18  ? -6.767  234.711 -14.820 1.00 31.00  ? 17  ILE H N   1 
ATOM   7757  C  CA  . ILE H  1 18  ? -6.010  235.056 -16.006 1.00 32.13  ? 17  ILE H CA  1 
ATOM   7758  C  C   . ILE H  1 18  ? -6.930  234.690 -17.128 1.00 32.58  ? 17  ILE H C   1 
ATOM   7759  O  O   . ILE H  1 18  ? -7.381  233.544 -17.230 1.00 34.22  ? 17  ILE H O   1 
ATOM   7760  C  CB  . ILE H  1 18  ? -4.765  234.141 -16.146 1.00 35.93  ? 17  ILE H CB  1 
ATOM   7761  C  CG1 . ILE H  1 18  ? -3.764  234.440 -15.037 1.00 33.65  ? 17  ILE H CG1 1 
ATOM   7762  C  CG2 . ILE H  1 18  ? -4.143  234.196 -17.561 1.00 32.72  ? 17  ILE H CG2 1 
ATOM   7763  C  CD1 . ILE H  1 18  ? -2.742  233.361 -14.812 1.00 28.95  ? 17  ILE H CD1 1 
ATOM   7764  N  N   . ILE H  1 19  ? -7.093  235.638 -18.023 1.00 32.91  ? 18  ILE H N   1 
ATOM   7765  C  CA  . ILE H  1 19  ? -7.964  235.526 -19.154 1.00 33.78  ? 18  ILE H CA  1 
ATOM   7766  C  C   . ILE H  1 19  ? -7.182  235.798 -20.437 1.00 35.32  ? 18  ILE H C   1 
ATOM   7767  O  O   . ILE H  1 19  ? -6.410  236.816 -20.562 1.00 36.38  ? 18  ILE H O   1 
ATOM   7768  C  CB  . ILE H  1 19  ? -9.048  236.606 -19.086 1.00 34.46  ? 18  ILE H CB  1 
ATOM   7769  C  CG1 . ILE H  1 19  ? -9.892  236.450 -17.822 1.00 34.56  ? 18  ILE H CG1 1 
ATOM   7770  C  CG2 . ILE H  1 19  ? -9.985  236.446 -20.273 1.00 35.08  ? 18  ILE H CG2 1 
ATOM   7771  C  CD1 . ILE H  1 19  ? -10.708 235.190 -17.815 1.00 30.28  ? 18  ILE H CD1 1 
ATOM   7772  N  N   . ASN H  1 20  ? -7.394  234.924 -21.408 1.00 30.47  ? 19  ASN H N   1 
ATOM   7773  C  CA  . ASN H  1 20  ? -6.647  235.016 -22.662 1.00 34.02  ? 19  ASN H CA  1 
ATOM   7774  C  C   . ASN H  1 20  ? -7.536  235.480 -23.783 1.00 35.69  ? 19  ASN H C   1 
ATOM   7775  O  O   . ASN H  1 20  ? -8.737  235.176 -23.844 1.00 39.87  ? 19  ASN H O   1 
ATOM   7776  C  CB  . ASN H  1 20  ? -5.974  233.670 -23.007 1.00 30.84  ? 19  ASN H CB  1 
ATOM   7777  C  CG  . ASN H  1 20  ? -5.080  233.168 -21.883 1.00 33.73  ? 19  ASN H CG  1 
ATOM   7778  O  OD1 . ASN H  1 20  ? -5.481  232.302 -21.053 1.00 40.03  ? 19  ASN H OD1 1 
ATOM   7779  N  ND2 . ASN H  1 20  ? -3.895  233.726 -21.798 1.00 29.96  ? 19  ASN H ND2 1 
ATOM   7780  N  N   . PHE H  1 21  ? -6.940  236.182 -24.712 1.00 37.01  ? 20  PHE H N   1 
ATOM   7781  C  CA  . PHE H  1 21  ? -7.687  236.678 -25.847 1.00 35.90  ? 20  PHE H CA  1 
ATOM   7782  C  C   . PHE H  1 21  ? -6.891  236.315 -27.102 1.00 38.64  ? 20  PHE H C   1 
ATOM   7783  O  O   . PHE H  1 21  ? -5.692  236.658 -27.282 1.00 37.61  ? 20  PHE H O   1 
ATOM   7784  C  CB  . PHE H  1 21  ? -7.849  238.195 -25.806 1.00 34.16  ? 20  PHE H CB  1 
ATOM   7785  C  CG  . PHE H  1 21  ? -8.605  238.756 -24.594 1.00 39.56  ? 20  PHE H CG  1 
ATOM   7786  C  CD1 . PHE H  1 21  ? -7.918  239.129 -23.423 1.00 35.72  ? 20  PHE H CD1 1 
ATOM   7787  C  CD2 . PHE H  1 21  ? -9.975  239.074 -24.674 1.00 38.96  ? 20  PHE H CD2 1 
ATOM   7788  C  CE1 . PHE H  1 21  ? -8.578  239.734 -22.344 1.00 36.54  ? 20  PHE H CE1 1 
ATOM   7789  C  CE2 . PHE H  1 21  ? -10.651 239.650 -23.599 1.00 39.09  ? 20  PHE H CE2 1 
ATOM   7790  C  CZ  . PHE H  1 21  ? -9.949  239.987 -22.430 1.00 41.12  ? 20  PHE H CZ  1 
ATOM   7791  N  N   . GLU H  1 22  ? -7.586  235.643 -28.003 1.00 41.72  ? 21  GLU H N   1 
ATOM   7792  C  CA  . GLU H  1 22  ? -7.023  235.286 -29.305 1.00 43.57  ? 21  GLU H CA  1 
ATOM   7793  C  C   . GLU H  1 22  ? -7.932  235.740 -30.464 1.00 46.39  ? 21  GLU H C   1 
ATOM   7794  O  O   . GLU H  1 22  ? -9.171  235.441 -30.470 1.00 47.63  ? 21  GLU H O   1 
ATOM   7795  C  CB  . GLU H  1 22  ? -6.780  233.807 -29.323 1.00 38.59  ? 21  GLU H CB  1 
ATOM   7796  C  CG  . GLU H  1 22  ? -5.707  233.433 -30.293 1.00 53.39  ? 21  GLU H CG  1 
ATOM   7797  C  CD  . GLU H  1 22  ? -5.631  231.918 -30.615 1.00 67.57  ? 21  GLU H CD  1 
ATOM   7798  O  OE1 . GLU H  1 22  ? -6.445  231.028 -30.150 1.00 64.19  ? 21  GLU H OE1 1 
ATOM   7799  O  OE2 . GLU H  1 22  ? -4.721  231.624 -31.409 1.00 64.01  ? 21  GLU H OE2 1 
ATOM   7800  N  N   . GLN H  1 23  ? -7.333  236.518 -31.377 1.00 43.70  ? 22  GLN H N   1 
ATOM   7801  C  CA  . GLN H  1 23  ? -7.938  236.882 -32.678 1.00 42.76  ? 22  GLN H CA  1 
ATOM   7802  C  C   . GLN H  1 23  ? -7.081  236.405 -33.873 1.00 46.00  ? 22  GLN H C   1 
ATOM   7803  O  O   . GLN H  1 23  ? -6.048  237.018 -34.180 1.00 47.33  ? 22  GLN H O   1 
ATOM   7804  C  CB  . GLN H  1 23  ? -8.111  238.369 -32.798 1.00 35.42  ? 22  GLN H CB  1 
ATOM   7805  C  CG  . GLN H  1 23  ? -9.235  238.782 -33.701 1.00 39.04  ? 22  GLN H CG  1 
ATOM   7806  C  CD  . GLN H  1 23  ? -9.479  240.278 -33.643 1.00 44.28  ? 22  GLN H CD  1 
ATOM   7807  O  OE1 . GLN H  1 23  ? -8.629  241.040 -33.173 1.00 47.13  ? 22  GLN H OE1 1 
ATOM   7808  N  NE2 . GLN H  1 23  ? -10.662 240.715 -34.073 1.00 46.78  ? 22  GLN H NE2 1 
ATOM   7809  N  N   . LYS H  1 24  ? -7.528  235.343 -34.545 1.00 47.26  ? 23  LYS H N   1 
ATOM   7810  C  CA  . LYS H  1 24  ? -6.973  234.938 -35.871 1.00 55.62  ? 23  LYS H CA  1 
ATOM   7811  C  C   . LYS H  1 24  ? -7.091  236.025 -37.023 1.00 54.24  ? 23  LYS H C   1 
ATOM   7812  O  O   . LYS H  1 24  ? -6.097  236.449 -37.615 1.00 50.46  ? 23  LYS H O   1 
ATOM   7813  C  CB  . LYS H  1 24  ? -7.608  233.620 -36.307 1.00 55.17  ? 23  LYS H CB  1 
ATOM   7814  C  CG  . LYS H  1 24  ? -7.582  232.534 -35.216 1.00 58.03  ? 23  LYS H CG  1 
ATOM   7815  C  CD  . LYS H  1 24  ? -6.229  231.830 -35.160 1.00 57.26  ? 23  LYS H CD  1 
ATOM   7816  C  CE  . LYS H  1 24  ? -6.296  230.498 -34.392 1.00 71.32  ? 23  LYS H CE  1 
ATOM   7817  N  NZ  . LYS H  1 24  ? -6.995  229.355 -35.105 1.00 73.54  ? 23  LYS H NZ  1 
ATOM   7818  N  N   . GLU H  1 25  ? -8.285  236.520 -37.312 1.00 52.58  ? 24  GLU H N   1 
ATOM   7819  C  CA  . GLU H  1 25  ? -8.464  237.457 -38.442 1.00 51.31  ? 24  GLU H CA  1 
ATOM   7820  C  C   . GLU H  1 25  ? -8.864  238.822 -37.902 1.00 52.57  ? 24  GLU H C   1 
ATOM   7821  O  O   . GLU H  1 25  ? -9.509  238.871 -36.843 1.00 60.08  ? 24  GLU H O   1 
ATOM   7822  C  CB  . GLU H  1 25  ? -9.552  236.902 -39.377 1.00 58.38  ? 24  GLU H CB  1 
ATOM   7823  C  CG  . GLU H  1 25  ? -9.300  235.439 -39.841 1.00 63.01  ? 24  GLU H CG  1 
ATOM   7824  C  CD  . GLU H  1 25  ? -10.600 234.663 -40.145 1.00 73.86  ? 24  GLU H CD  1 
ATOM   7825  O  OE1 . GLU H  1 25  ? -11.396 235.071 -41.103 1.00 58.97  ? 24  GLU H OE1 1 
ATOM   7826  O  OE2 . GLU H  1 25  ? -10.815 233.638 -39.408 1.00 63.13  ? 24  GLU H OE2 1 
ATOM   7827  N  N   . SER H  1 26  ? -8.526  239.905 -38.611 1.00 49.09  ? 25  SER H N   1 
ATOM   7828  C  CA  . SER H  1 26  ? -8.711  241.320 -38.140 1.00 57.22  ? 25  SER H CA  1 
ATOM   7829  C  C   . SER H  1 26  ? -10.125 241.761 -37.947 1.00 61.28  ? 25  SER H C   1 
ATOM   7830  O  O   . SER H  1 26  ? -10.432 242.541 -37.061 1.00 59.16  ? 25  SER H O   1 
ATOM   7831  C  CB  . SER H  1 26  ? -8.094  242.324 -39.111 1.00 60.22  ? 25  SER H CB  1 
ATOM   7832  O  OG  . SER H  1 26  ? -6.775  241.865 -39.327 1.00 78.86  ? 25  SER H OG  1 
ATOM   7833  N  N   . ASN H  1 27  ? -11.002 241.323 -38.819 1.00 67.36  ? 26  ASN H N   1 
ATOM   7834  C  CA  . ASN H  1 27  ? -12.394 241.697 -38.630 1.00 66.47  ? 26  ASN H CA  1 
ATOM   7835  C  C   . ASN H  1 27  ? -13.152 240.689 -37.721 1.00 59.35  ? 26  ASN H C   1 
ATOM   7836  O  O   . ASN H  1 27  ? -14.188 241.064 -37.132 1.00 61.08  ? 26  ASN H O   1 
ATOM   7837  C  CB  . ASN H  1 27  ? -13.074 241.992 -40.010 1.00 77.22  ? 26  ASN H CB  1 
ATOM   7838  C  CG  . ASN H  1 27  ? -12.910 240.843 -41.087 1.00 89.86  ? 26  ASN H CG  1 
ATOM   7839  O  OD1 . ASN H  1 27  ? -12.391 239.701 -40.801 1.00 77.47  ? 26  ASN H OD1 1 
ATOM   7840  N  ND2 . ASN H  1 27  ? -13.368 241.151 -42.360 1.00 65.69  ? 26  ASN H ND2 1 
ATOM   7841  N  N   . GLY H  1 28  ? -12.600 239.476 -37.543 1.00 50.23  ? 27  GLY H N   1 
ATOM   7842  C  CA  . GLY H  1 28  ? -13.368 238.324 -37.067 1.00 48.15  ? 27  GLY H CA  1 
ATOM   7843  C  C   . GLY H  1 28  ? -13.382 238.068 -35.558 1.00 50.12  ? 27  GLY H C   1 
ATOM   7844  O  O   . GLY H  1 28  ? -12.860 238.893 -34.751 1.00 43.95  ? 27  GLY H O   1 
ATOM   7845  N  N   . PRO H  1 29  ? -13.926 236.900 -35.145 1.00 46.81  ? 28  PRO H N   1 
ATOM   7846  C  CA  . PRO H  1 29  ? -14.172 236.792 -33.722 1.00 46.22  ? 28  PRO H CA  1 
ATOM   7847  C  C   . PRO H  1 29  ? -12.885 236.652 -32.799 1.00 53.68  ? 28  PRO H C   1 
ATOM   7848  O  O   . PRO H  1 29  ? -11.799 236.072 -33.214 1.00 44.60  ? 28  PRO H O   1 
ATOM   7849  C  CB  . PRO H  1 29  ? -15.115 235.566 -33.629 1.00 45.12  ? 28  PRO H CB  1 
ATOM   7850  C  CG  . PRO H  1 29  ? -14.803 234.710 -34.834 1.00 41.72  ? 28  PRO H CG  1 
ATOM   7851  C  CD  . PRO H  1 29  ? -13.929 235.561 -35.762 1.00 46.31  ? 28  PRO H CD  1 
ATOM   7852  N  N   . VAL H  1 30  ? -13.023 237.208 -31.565 1.00 45.28  ? 29  VAL H N   1 
ATOM   7853  C  CA  . VAL H  1 30  ? -12.066 236.984 -30.479 1.00 39.42  ? 29  VAL H CA  1 
ATOM   7854  C  C   . VAL H  1 30  ? -12.520 235.833 -29.568 1.00 38.34  ? 29  VAL H C   1 
ATOM   7855  O  O   . VAL H  1 30  ? -13.666 235.827 -29.051 1.00 41.84  ? 29  VAL H O   1 
ATOM   7856  C  CB  . VAL H  1 30  ? -11.827 238.278 -29.716 1.00 39.07  ? 29  VAL H CB  1 
ATOM   7857  C  CG1 . VAL H  1 30  ? -10.686 238.079 -28.746 1.00 33.31  ? 29  VAL H CG1 1 
ATOM   7858  C  CG2 . VAL H  1 30  ? -11.510 239.407 -30.704 1.00 32.25  ? 29  VAL H CG2 1 
ATOM   7859  N  N   . LYS H  1 31  ? -11.670 234.811 -29.451 1.00 37.94  ? 30  LYS H N   1 
ATOM   7860  C  CA  . LYS H  1 31  ? -11.887 233.688 -28.491 1.00 38.82  ? 30  LYS H CA  1 
ATOM   7861  C  C   . LYS H  1 31  ? -11.368 234.282 -27.122 1.00 37.03  ? 30  LYS H C   1 
ATOM   7862  O  O   . LYS H  1 31  ? -10.324 234.970 -27.083 1.00 33.29  ? 30  LYS H O   1 
ATOM   7863  C  CB  . LYS H  1 31  ? -11.115 232.414 -28.916 1.00 38.73  ? 30  LYS H CB  1 
ATOM   7864  N  N   . VAL H  1 32  ? -12.172 234.123 -26.058 1.00 34.85  ? 31  VAL H N   1 
ATOM   7865  C  CA  . VAL H  1 32  ? -11.864 234.616 -24.712 1.00 34.58  ? 31  VAL H CA  1 
ATOM   7866  C  C   . VAL H  1 32  ? -11.910 233.458 -23.719 1.00 38.23  ? 31  VAL H C   1 
ATOM   7867  O  O   . VAL H  1 32  ? -12.949 232.814 -23.566 1.00 35.57  ? 31  VAL H O   1 
ATOM   7868  C  CB  . VAL H  1 32  ? -12.802 235.741 -24.232 1.00 34.29  ? 31  VAL H CB  1 
ATOM   7869  C  CG1 . VAL H  1 32  ? -12.408 236.197 -22.822 1.00 28.69  ? 31  VAL H CG1 1 
ATOM   7870  C  CG2 . VAL H  1 32  ? -12.805 236.927 -25.198 1.00 29.47  ? 31  VAL H CG2 1 
ATOM   7871  N  N   . TRP H  1 33  ? -10.786 233.173 -23.055 1.00 38.69  ? 32  TRP H N   1 
ATOM   7872  C  CA  . TRP H  1 33  ? -10.737 231.959 -22.201 1.00 38.97  ? 32  TRP H CA  1 
ATOM   7873  C  C   . TRP H  1 33  ? -9.751  232.042 -21.059 1.00 35.81  ? 32  TRP H C   1 
ATOM   7874  O  O   . TRP H  1 33  ? -8.740  232.754 -21.159 1.00 35.73  ? 32  TRP H O   1 
ATOM   7875  C  CB  . TRP H  1 33  ? -10.465 230.683 -23.037 1.00 34.76  ? 32  TRP H CB  1 
ATOM   7876  C  CG  . TRP H  1 33  ? -9.084  230.679 -23.663 1.00 42.97  ? 32  TRP H CG  1 
ATOM   7877  C  CD1 . TRP H  1 33  ? -8.654  231.373 -24.790 1.00 44.59  ? 32  TRP H CD1 1 
ATOM   7878  C  CD2 . TRP H  1 33  ? -7.945  229.997 -23.169 1.00 40.18  ? 32  TRP H CD2 1 
ATOM   7879  N  NE1 . TRP H  1 33  ? -7.321  231.081 -25.048 1.00 42.95  ? 32  TRP H NE1 1 
ATOM   7880  C  CE2 . TRP H  1 33  ? -6.867  230.254 -24.060 1.00 40.70  ? 32  TRP H CE2 1 
ATOM   7881  C  CE3 . TRP H  1 33  ? -7.738  229.144 -22.078 1.00 47.22  ? 32  TRP H CE3 1 
ATOM   7882  C  CZ2 . TRP H  1 33  ? -5.559  229.709 -23.873 1.00 52.45  ? 32  TRP H CZ2 1 
ATOM   7883  C  CZ3 . TRP H  1 33  ? -6.396  228.570 -21.868 1.00 60.14  ? 32  TRP H CZ3 1 
ATOM   7884  C  CH2 . TRP H  1 33  ? -5.331  228.863 -22.790 1.00 51.98  ? 32  TRP H CH2 1 
ATOM   7885  N  N   . GLY H  1 34  ? -10.006 231.264 -20.007 1.00 34.66  ? 33  GLY H N   1 
ATOM   7886  C  CA  . GLY H  1 34  ? -9.087  231.205 -18.876 1.00 31.40  ? 33  GLY H CA  1 
ATOM   7887  C  C   . GLY H  1 34  ? -9.897  230.991 -17.626 1.00 34.34  ? 33  GLY H C   1 
ATOM   7888  O  O   . GLY H  1 34  ? -10.993 230.534 -17.671 1.00 37.13  ? 33  GLY H O   1 
ATOM   7889  N  N   . SER H  1 35  ? -9.387  231.364 -16.485 1.00 38.11  ? 34  SER H N   1 
ATOM   7890  C  CA  . SER H  1 35  ? -9.938  230.802 -15.274 1.00 38.11  ? 34  SER H CA  1 
ATOM   7891  C  C   . SER H  1 35  ? -9.934  231.844 -14.177 1.00 36.94  ? 34  SER H C   1 
ATOM   7892  O  O   . SER H  1 35  ? -8.927  232.575 -14.018 1.00 37.36  ? 34  SER H O   1 
ATOM   7893  C  CB  . SER H  1 35  ? -9.083  229.615 -14.923 1.00 40.09  ? 34  SER H CB  1 
ATOM   7894  O  OG  . SER H  1 35  ? -9.429  229.075 -13.689 1.00 47.12  ? 34  SER H OG  1 
ATOM   7895  N  N   . ILE H  1 36  ? -11.062 231.980 -13.482 1.00 32.95  ? 35  ILE H N   1 
ATOM   7896  C  CA  . ILE H  1 36  ? -11.128 232.983 -12.396 1.00 33.79  ? 35  ILE H CA  1 
ATOM   7897  C  C   . ILE H  1 36  ? -11.561 232.301 -11.158 1.00 29.60  ? 35  ILE H C   1 
ATOM   7898  O  O   . ILE H  1 36  ? -12.581 231.625 -11.159 1.00 31.33  ? 35  ILE H O   1 
ATOM   7899  C  CB  . ILE H  1 36  ? -12.162 234.111 -12.705 1.00 33.53  ? 35  ILE H CB  1 
ATOM   7900  C  CG1 . ILE H  1 36  ? -11.793 234.845 -13.993 1.00 36.52  ? 35  ILE H CG1 1 
ATOM   7901  C  CG2 . ILE H  1 36  ? -12.216 235.128 -11.580 1.00 26.11  ? 35  ILE H CG2 1 
ATOM   7902  C  CD1 . ILE H  1 36  ? -12.921 235.683 -14.557 1.00 33.67  ? 35  ILE H CD1 1 
ATOM   7903  N  N   . LYS H  1 37  ? -10.837 232.480 -10.074 1.00 35.07  ? 36  LYS H N   1 
ATOM   7904  C  CA  . LYS H  1 37  ? -11.311 231.812 -8.802  1.00 36.93  ? 36  LYS H CA  1 
ATOM   7905  C  C   . LYS H  1 37  ? -11.641 232.756 -7.691  1.00 32.93  ? 36  LYS H C   1 
ATOM   7906  O  O   . LYS H  1 37  ? -11.380 233.954 -7.793  1.00 29.45  ? 36  LYS H O   1 
ATOM   7907  C  CB  . LYS H  1 37  ? -10.303 230.803 -8.293  1.00 39.37  ? 36  LYS H CB  1 
ATOM   7908  C  CG  . LYS H  1 37  ? -9.050  231.508 -7.834  1.00 44.58  ? 36  LYS H CG  1 
ATOM   7909  C  CD  . LYS H  1 37  ? -7.875  230.575 -7.752  1.00 47.49  ? 36  LYS H CD  1 
ATOM   7910  C  CE  . LYS H  1 37  ? -6.767  231.367 -7.088  1.00 51.18  ? 36  LYS H CE  1 
ATOM   7911  N  NZ  . LYS H  1 37  ? -5.820  230.332 -6.627  1.00 48.18  ? 36  LYS H NZ  1 
ATOM   7912  N  N   . GLY H  1 38  ? -12.194 232.197 -6.618  1.00 33.34  ? 37  GLY H N   1 
ATOM   7913  C  CA  . GLY H  1 38  ? -12.611 233.007 -5.503  1.00 32.34  ? 37  GLY H CA  1 
ATOM   7914  C  C   . GLY H  1 38  ? -13.955 233.707 -5.703  1.00 34.86  ? 37  GLY H C   1 
ATOM   7915  O  O   . GLY H  1 38  ? -14.225 234.689 -5.068  1.00 37.75  ? 37  GLY H O   1 
ATOM   7916  N  N   . LEU H  1 39  ? -14.826 233.198 -6.560  1.00 36.13  ? 38  LEU H N   1 
ATOM   7917  C  CA  . LEU H  1 39  ? -16.098 233.881 -6.833  1.00 39.28  ? 38  LEU H CA  1 
ATOM   7918  C  C   . LEU H  1 39  ? -17.182 233.112 -6.148  1.00 38.66  ? 38  LEU H C   1 
ATOM   7919  O  O   . LEU H  1 39  ? -17.016 231.896 -5.942  1.00 36.07  ? 38  LEU H O   1 
ATOM   7920  C  CB  . LEU H  1 39  ? -16.451 233.901 -8.356  1.00 38.21  ? 38  LEU H CB  1 
ATOM   7921  C  CG  . LEU H  1 39  ? -15.547 234.657 -9.307  1.00 42.30  ? 38  LEU H CG  1 
ATOM   7922  C  CD1 . LEU H  1 39  ? -15.741 233.886 -10.600 1.00 44.40  ? 38  LEU H CD1 1 
ATOM   7923  C  CD2 . LEU H  1 39  ? -15.933 236.106 -9.482  1.00 39.73  ? 38  LEU H CD2 1 
ATOM   7924  N  N   . THR H  1 40  ? -18.330 233.766 -5.923  1.00 37.84  ? 39  THR H N   1 
ATOM   7925  C  CA  . THR H  1 40  ? -19.507 233.051 -5.392  1.00 36.48  ? 39  THR H CA  1 
ATOM   7926  C  C   . THR H  1 40  ? -20.059 232.190 -6.546  1.00 33.31  ? 39  THR H C   1 
ATOM   7927  O  O   . THR H  1 40  ? -20.008 232.546 -7.730  1.00 34.27  ? 39  THR H O   1 
ATOM   7928  C  CB  . THR H  1 40  ? -20.559 234.046 -4.837  1.00 37.89  ? 39  THR H CB  1 
ATOM   7929  O  OG1 . THR H  1 40  ? -20.900 234.927 -5.885  1.00 40.07  ? 39  THR H OG1 1 
ATOM   7930  C  CG2 . THR H  1 40  ? -20.009 234.955 -3.703  1.00 31.29  ? 39  THR H CG2 1 
ATOM   7931  N  N   . GLU H  1 41  ? -20.544 231.029 -6.211  1.00 33.87  ? 40  GLU H N   1 
ATOM   7932  C  CA  . GLU H  1 41  ? -21.202 230.164 -7.184  1.00 38.91  ? 40  GLU H CA  1 
ATOM   7933  C  C   . GLU H  1 41  ? -22.270 230.941 -7.987  1.00 41.86  ? 40  GLU H C   1 
ATOM   7934  O  O   . GLU H  1 41  ? -23.007 231.727 -7.411  1.00 40.39  ? 40  GLU H O   1 
ATOM   7935  C  CB  . GLU H  1 41  ? -21.820 228.980 -6.481  1.00 34.47  ? 40  GLU H CB  1 
ATOM   7936  C  CG  . GLU H  1 41  ? -22.613 228.129 -7.394  1.00 40.58  ? 40  GLU H CG  1 
ATOM   7937  C  CD  . GLU H  1 41  ? -23.091 226.918 -6.698  1.00 49.24  ? 40  GLU H CD  1 
ATOM   7938  O  OE1 . GLU H  1 41  ? -23.275 227.013 -5.465  1.00 54.57  ? 40  GLU H OE1 1 
ATOM   7939  O  OE2 . GLU H  1 41  ? -23.287 225.883 -7.362  1.00 49.32  ? 40  GLU H OE2 1 
ATOM   7940  N  N   . GLY H  1 42  ? -22.326 230.742 -9.303  1.00 42.26  ? 41  GLY H N   1 
ATOM   7941  C  CA  . GLY H  1 42  ? -23.331 231.423 -10.132 1.00 39.50  ? 41  GLY H CA  1 
ATOM   7942  C  C   . GLY H  1 42  ? -22.805 232.508 -11.068 1.00 39.86  ? 41  GLY H C   1 
ATOM   7943  O  O   . GLY H  1 42  ? -21.581 232.593 -11.362 1.00 40.26  ? 41  GLY H O   1 
ATOM   7944  N  N   . LEU H  1 43  ? -23.733 233.358 -11.510 1.00 41.11  ? 42  LEU H N   1 
ATOM   7945  C  CA  . LEU H  1 43  ? -23.530 234.232 -12.658 1.00 36.99  ? 42  LEU H CA  1 
ATOM   7946  C  C   . LEU H  1 43  ? -22.833 235.516 -12.215 1.00 37.73  ? 42  LEU H C   1 
ATOM   7947  O  O   . LEU H  1 43  ? -23.225 236.102 -11.168 1.00 36.48  ? 42  LEU H O   1 
ATOM   7948  C  CB  . LEU H  1 43  ? -24.864 234.587 -13.260 1.00 37.32  ? 42  LEU H CB  1 
ATOM   7949  C  CG  . LEU H  1 43  ? -25.679 233.561 -14.037 1.00 39.25  ? 42  LEU H CG  1 
ATOM   7950  C  CD1 . LEU H  1 43  ? -27.069 234.085 -14.362 1.00 35.87  ? 42  LEU H CD1 1 
ATOM   7951  C  CD2 . LEU H  1 43  ? -24.965 233.255 -15.327 1.00 38.81  ? 42  LEU H CD2 1 
ATOM   7952  N  N   . HIS H  1 44  ? -21.795 235.914 -12.983 1.00 34.13  ? 43  HIS H N   1 
ATOM   7953  C  CA  . HIS H  1 44  ? -21.069 237.192 -12.788 1.00 35.72  ? 43  HIS H CA  1 
ATOM   7954  C  C   . HIS H  1 44  ? -20.903 237.957 -14.097 1.00 36.94  ? 43  HIS H C   1 
ATOM   7955  O  O   . HIS H  1 44  ? -20.466 237.397 -15.131 1.00 38.76  ? 43  HIS H O   1 
ATOM   7956  C  CB  . HIS H  1 44  ? -19.691 236.989 -12.158 1.00 32.47  ? 43  HIS H CB  1 
ATOM   7957  C  CG  . HIS H  1 44  ? -19.739 236.364 -10.806 1.00 34.83  ? 43  HIS H CG  1 
ATOM   7958  N  ND1 . HIS H  1 44  ? -19.649 237.109 -9.639  1.00 33.96  ? 43  HIS H ND1 1 
ATOM   7959  C  CD2 . HIS H  1 44  ? -19.907 235.076 -10.424 1.00 29.24  ? 43  HIS H CD2 1 
ATOM   7960  C  CE1 . HIS H  1 44  ? -19.765 236.307 -8.601  1.00 28.29  ? 43  HIS H CE1 1 
ATOM   7961  N  NE2 . HIS H  1 44  ? -19.923 235.074 -9.045  1.00 32.25  ? 43  HIS H NE2 1 
ATOM   7962  N  N   . GLY H  1 45  ? -21.265 239.232 -14.051 1.00 37.79  ? 44  GLY H N   1 
ATOM   7963  C  CA  . GLY H  1 45  ? -21.035 240.176 -15.167 1.00 36.66  ? 44  GLY H CA  1 
ATOM   7964  C  C   . GLY H  1 45  ? -19.556 240.203 -15.500 1.00 37.79  ? 44  GLY H C   1 
ATOM   7965  O  O   . GLY H  1 45  ? -18.730 240.127 -14.618 1.00 37.88  ? 44  GLY H O   1 
ATOM   7966  N  N   . PHE H  1 46  ? -19.242 240.289 -16.782 1.00 35.97  ? 45  PHE H N   1 
ATOM   7967  C  CA  . PHE H  1 46  ? -17.911 240.190 -17.288 1.00 34.60  ? 45  PHE H CA  1 
ATOM   7968  C  C   . PHE H  1 46  ? -17.841 241.244 -18.390 1.00 35.50  ? 45  PHE H C   1 
ATOM   7969  O  O   . PHE H  1 46  ? -18.361 240.980 -19.478 1.00 38.66  ? 45  PHE H O   1 
ATOM   7970  C  CB  . PHE H  1 46  ? -17.779 238.813 -17.907 1.00 33.38  ? 45  PHE H CB  1 
ATOM   7971  C  CG  . PHE H  1 46  ? -16.379 238.406 -18.256 1.00 39.42  ? 45  PHE H CG  1 
ATOM   7972  C  CD1 . PHE H  1 46  ? -15.361 238.337 -17.249 1.00 42.92  ? 45  PHE H CD1 1 
ATOM   7973  C  CD2 . PHE H  1 46  ? -16.074 237.942 -19.538 1.00 34.63  ? 45  PHE H CD2 1 
ATOM   7974  C  CE1 . PHE H  1 46  ? -14.080 237.876 -17.556 1.00 39.13  ? 45  PHE H CE1 1 
ATOM   7975  C  CE2 . PHE H  1 46  ? -14.788 237.480 -19.833 1.00 38.39  ? 45  PHE H CE2 1 
ATOM   7976  C  CZ  . PHE H  1 46  ? -13.784 237.456 -18.850 1.00 38.28  ? 45  PHE H CZ  1 
ATOM   7977  N  N   . HIS H  1 47  ? -17.195 242.390 -18.144 1.00 29.24  ? 46  HIS H N   1 
ATOM   7978  C  CA  . HIS H  1 47  ? -17.197 243.473 -19.081 1.00 29.07  ? 46  HIS H CA  1 
ATOM   7979  C  C   . HIS H  1 47  ? -15.883 244.153 -19.225 1.00 32.20  ? 46  HIS H C   1 
ATOM   7980  O  O   . HIS H  1 47  ? -15.107 244.254 -18.288 1.00 35.75  ? 46  HIS H O   1 
ATOM   7981  C  CB  . HIS H  1 47  ? -18.105 244.582 -18.620 1.00 31.16  ? 46  HIS H CB  1 
ATOM   7982  C  CG  . HIS H  1 47  ? -19.432 244.105 -18.142 1.00 36.16  ? 46  HIS H CG  1 
ATOM   7983  N  ND1 . HIS H  1 47  ? -19.894 244.372 -16.869 1.00 33.17  ? 46  HIS H ND1 1 
ATOM   7984  C  CD2 . HIS H  1 47  ? -20.365 243.315 -18.735 1.00 35.95  ? 46  HIS H CD2 1 
ATOM   7985  C  CE1 . HIS H  1 47  ? -21.072 243.786 -16.714 1.00 38.36  ? 46  HIS H CE1 1 
ATOM   7986  N  NE2 . HIS H  1 47  ? -21.375 243.128 -17.826 1.00 36.29  ? 46  HIS H NE2 1 
ATOM   7987  N  N   . VAL H  1 48  ? -15.661 244.681 -20.421 1.00 31.79  ? 47  VAL H N   1 
ATOM   7988  C  CA  . VAL H  1 48  ? -14.535 245.527 -20.731 1.00 32.98  ? 47  VAL H CA  1 
ATOM   7989  C  C   . VAL H  1 48  ? -14.943 246.993 -20.483 1.00 39.81  ? 47  VAL H C   1 
ATOM   7990  O  O   . VAL H  1 48  ? -15.913 247.497 -21.069 1.00 43.68  ? 47  VAL H O   1 
ATOM   7991  C  CB  . VAL H  1 48  ? -14.103 245.315 -22.176 1.00 29.89  ? 47  VAL H CB  1 
ATOM   7992  C  CG1 . VAL H  1 48  ? -12.915 246.171 -22.478 1.00 26.10  ? 47  VAL H CG1 1 
ATOM   7993  C  CG2 . VAL H  1 48  ? -13.826 243.840 -22.451 1.00 28.66  ? 47  VAL H CG2 1 
ATOM   7994  N  N   . HIS H  1 49  ? -14.249 247.645 -19.564 1.00 38.85  ? 48  HIS H N   1 
ATOM   7995  C  CA  . HIS H  1 49  ? -14.534 249.001 -19.176 1.00 33.51  ? 48  HIS H CA  1 
ATOM   7996  C  C   . HIS H  1 49  ? -13.558 249.900 -19.928 1.00 38.54  ? 48  HIS H C   1 
ATOM   7997  O  O   . HIS H  1 49  ? -12.527 249.454 -20.449 1.00 40.13  ? 48  HIS H O   1 
ATOM   7998  C  CB  . HIS H  1 49  ? -14.376 249.179 -17.648 1.00 32.62  ? 48  HIS H CB  1 
ATOM   7999  C  CG  . HIS H  1 49  ? -15.465 248.549 -16.839 1.00 30.89  ? 48  HIS H CG  1 
ATOM   8000  N  ND1 . HIS H  1 49  ? -16.301 249.280 -16.027 1.00 28.33  ? 48  HIS H ND1 1 
ATOM   8001  C  CD2 . HIS H  1 49  ? -15.866 247.256 -16.722 1.00 30.49  ? 48  HIS H CD2 1 
ATOM   8002  C  CE1 . HIS H  1 49  ? -17.176 248.469 -15.457 1.00 27.77  ? 48  HIS H CE1 1 
ATOM   8003  N  NE2 . HIS H  1 49  ? -16.936 247.235 -15.861 1.00 27.75  ? 48  HIS H NE2 1 
ATOM   8004  N  N   . GLU H  1 50  ? -13.872 251.190 -19.978 1.00 46.70  ? 49  GLU H N   1 
ATOM   8005  C  CA  . GLU H  1 50  ? -13.142 252.152 -20.837 1.00 46.15  ? 49  GLU H CA  1 
ATOM   8006  C  C   . GLU H  1 50  ? -11.657 252.463 -20.553 1.00 44.23  ? 49  GLU H C   1 
ATOM   8007  O  O   . GLU H  1 50  ? -10.926 252.617 -21.480 1.00 42.29  ? 49  GLU H O   1 
ATOM   8008  C  CB  . GLU H  1 50  ? -13.917 253.435 -20.863 1.00 48.39  ? 49  GLU H CB  1 
ATOM   8009  C  CG  . GLU H  1 50  ? -13.521 254.334 -22.005 1.00 50.80  ? 49  GLU H CG  1 
ATOM   8010  C  CD  . GLU H  1 50  ? -14.311 255.634 -22.053 1.00 48.97  ? 49  GLU H CD  1 
ATOM   8011  O  OE1 . GLU H  1 50  ? -15.334 255.872 -21.309 1.00 45.81  ? 49  GLU H OE1 1 
ATOM   8012  O  OE2 . GLU H  1 50  ? -13.864 256.413 -22.906 1.00 52.31  ? 49  GLU H OE2 1 
ATOM   8013  N  N   . PHE H  1 51  ? -11.214 252.606 -19.295 1.00 45.93  ? 50  PHE H N   1 
ATOM   8014  C  CA  . PHE H  1 51  ? -9.810  252.990 -19.040 1.00 39.72  ? 50  PHE H CA  1 
ATOM   8015  C  C   . PHE H  1 51  ? -9.008  251.845 -18.461 1.00 38.73  ? 50  PHE H C   1 
ATOM   8016  O  O   . PHE H  1 51  ? -9.470  251.124 -17.593 1.00 40.67  ? 50  PHE H O   1 
ATOM   8017  C  CB  . PHE H  1 51  ? -9.755  254.249 -18.198 1.00 38.24  ? 50  PHE H CB  1 
ATOM   8018  C  CG  . PHE H  1 51  ? -10.709 255.313 -18.674 1.00 42.82  ? 50  PHE H CG  1 
ATOM   8019  C  CD1 . PHE H  1 51  ? -10.474 256.011 -19.896 1.00 42.67  ? 50  PHE H CD1 1 
ATOM   8020  C  CD2 . PHE H  1 51  ? -11.837 255.647 -17.914 1.00 42.76  ? 50  PHE H CD2 1 
ATOM   8021  C  CE1 . PHE H  1 51  ? -11.382 256.957 -20.385 1.00 40.18  ? 50  PHE H CE1 1 
ATOM   8022  C  CE2 . PHE H  1 51  ? -12.725 256.642 -18.384 1.00 43.14  ? 50  PHE H CE2 1 
ATOM   8023  C  CZ  . PHE H  1 51  ? -12.498 257.271 -19.625 1.00 42.90  ? 50  PHE H CZ  1 
ATOM   8024  N  N   . GLY H  1 52  ? -7.820  251.645 -18.985 1.00 39.77  ? 51  GLY H N   1 
ATOM   8025  C  CA  . GLY H  1 52  ? -6.815  250.818 -18.302 1.00 40.51  ? 51  GLY H CA  1 
ATOM   8026  C  C   . GLY H  1 52  ? -6.191  251.658 -17.162 1.00 41.04  ? 51  GLY H C   1 
ATOM   8027  O  O   . GLY H  1 52  ? -4.948  251.833 -17.073 1.00 38.31  ? 51  GLY H O   1 
ATOM   8028  N  N   . ASP H  1 53  ? -7.061  252.210 -16.316 1.00 38.05  ? 52  ASP H N   1 
ATOM   8029  C  CA  . ASP H  1 53  ? -6.591  253.067 -15.285 1.00 39.88  ? 52  ASP H CA  1 
ATOM   8030  C  C   . ASP H  1 53  ? -6.896  252.440 -13.951 1.00 42.45  ? 52  ASP H C   1 
ATOM   8031  O  O   . ASP H  1 53  ? -8.069  252.287 -13.511 1.00 39.79  ? 52  ASP H O   1 
ATOM   8032  C  CB  . ASP H  1 53  ? -7.123  254.491 -15.363 1.00 39.95  ? 52  ASP H CB  1 
ATOM   8033  C  CG  . ASP H  1 53  ? -6.664  255.321 -14.168 1.00 47.10  ? 52  ASP H CG  1 
ATOM   8034  O  OD1 . ASP H  1 53  ? -6.044  254.740 -13.223 1.00 52.04  ? 52  ASP H OD1 1 
ATOM   8035  O  OD2 . ASP H  1 53  ? -6.897  256.548 -14.121 1.00 48.67  ? 52  ASP H OD2 1 
ATOM   8036  N  N   . ASN H  1 54  ? -5.800  252.068 -13.313 1.00 38.33  ? 53  ASN H N   1 
ATOM   8037  C  CA  . ASN H  1 54  ? -5.935  251.319 -12.124 1.00 41.06  ? 53  ASN H CA  1 
ATOM   8038  C  C   . ASN H  1 54  ? -5.477  252.110 -10.885 1.00 41.48  ? 53  ASN H C   1 
ATOM   8039  O  O   . ASN H  1 54  ? -5.246  251.514 -9.837  1.00 40.24  ? 53  ASN H O   1 
ATOM   8040  C  CB  . ASN H  1 54  ? -5.103  250.063 -12.295 1.00 46.49  ? 53  ASN H CB  1 
ATOM   8041  C  CG  . ASN H  1 54  ? -5.377  249.037 -11.194 1.00 57.90  ? 53  ASN H CG  1 
ATOM   8042  O  OD1 . ASN H  1 54  ? -6.500  248.554 -11.093 1.00 60.90  ? 53  ASN H OD1 1 
ATOM   8043  N  ND2 . ASN H  1 54  ? -4.371  248.743 -10.318 1.00 54.19  ? 53  ASN H ND2 1 
ATOM   8044  N  N   . THR H  1 55  ? -5.299  253.424 -11.004 1.00 37.70  ? 54  THR H N   1 
ATOM   8045  C  CA  . THR H  1 55  ? -4.792  254.229 -9.914  1.00 37.31  ? 54  THR H CA  1 
ATOM   8046  C  C   . THR H  1 55  ? -5.735  254.155 -8.759  1.00 40.01  ? 54  THR H C   1 
ATOM   8047  O  O   . THR H  1 55  ? -5.346  254.131 -7.643  1.00 46.18  ? 54  THR H O   1 
ATOM   8048  C  CB  . THR H  1 55  ? -4.553  255.707 -10.327 1.00 42.52  ? 54  THR H CB  1 
ATOM   8049  O  OG1 . THR H  1 55  ? -5.674  256.254 -11.033 1.00 43.61  ? 54  THR H OG1 1 
ATOM   8050  C  CG2 . THR H  1 55  ? -3.396  255.832 -11.311 1.00 40.48  ? 54  THR H CG2 1 
ATOM   8051  N  N   . ALA H  1 56  ? -7.011  254.006 -8.979  1.00 44.42  ? 55  ALA H N   1 
ATOM   8052  C  CA  . ALA H  1 56  ? -7.859  253.863 -7.793  1.00 43.58  ? 55  ALA H CA  1 
ATOM   8053  C  C   . ALA H  1 56  ? -8.474  252.494 -7.639  1.00 40.53  ? 55  ALA H C   1 
ATOM   8054  O  O   . ALA H  1 56  ? -9.610  252.405 -7.205  1.00 49.68  ? 55  ALA H O   1 
ATOM   8055  C  CB  . ALA H  1 56  ? -8.960  254.937 -7.803  1.00 41.49  ? 55  ALA H CB  1 
ATOM   8056  N  N   . GLY H  1 57  ? -7.757  251.434 -7.985  1.00 39.11  ? 56  GLY H N   1 
ATOM   8057  C  CA  . GLY H  1 57  ? -8.366  250.088 -8.100  1.00 39.67  ? 56  GLY H CA  1 
ATOM   8058  C  C   . GLY H  1 57  ? -9.358  250.010 -9.277  1.00 41.44  ? 56  GLY H C   1 
ATOM   8059  O  O   . GLY H  1 57  ? -9.261  250.787 -10.224 1.00 43.31  ? 56  GLY H O   1 
ATOM   8060  N  N   . CYS H  1 58  ? -10.320 249.101 -9.208  1.00 38.64  ? 57  CYS H N   1 
ATOM   8061  C  CA  . CYS H  1 58  ? -11.230 248.921 -10.284 1.00 40.10  ? 57  CYS H CA  1 
ATOM   8062  C  C   . CYS H  1 58  ? -12.128 250.157 -10.570 1.00 47.27  ? 57  CYS H C   1 
ATOM   8063  O  O   . CYS H  1 58  ? -12.557 250.373 -11.730 1.00 42.27  ? 57  CYS H O   1 
ATOM   8064  C  CB  . CYS H  1 58  ? -12.050 247.702 -10.046 1.00 38.83  ? 57  CYS H CB  1 
ATOM   8065  S  SG  . CYS H  1 58  ? -10.997 246.244 -10.042 1.00 45.44  ? 57  CYS H SG  1 
ATOM   8066  N  N   . THR H  1 59  ? -12.335 250.994 -9.548  1.00 45.97  ? 58  THR H N   1 
ATOM   8067  C  CA  . THR H  1 59  ? -13.116 252.248 -9.693  1.00 46.47  ? 58  THR H CA  1 
ATOM   8068  C  C   . THR H  1 59  ? -12.654 253.144 -10.857 1.00 45.83  ? 58  THR H C   1 
ATOM   8069  O  O   . THR H  1 59  ? -13.461 253.633 -11.614 1.00 43.20  ? 58  THR H O   1 
ATOM   8070  C  CB  . THR H  1 59  ? -13.135 253.009 -8.352  1.00 47.61  ? 58  THR H CB  1 
ATOM   8071  O  OG1 . THR H  1 59  ? -13.968 252.270 -7.474  1.00 50.24  ? 58  THR H OG1 1 
ATOM   8072  C  CG2 . THR H  1 59  ? -13.744 254.422 -8.460  1.00 49.73  ? 58  THR H CG2 1 
ATOM   8073  N  N   . SER H  1 60  ? -11.360 253.309 -11.034 1.00 44.09  ? 59  SER H N   1 
ATOM   8074  C  CA  . SER H  1 60  ? -10.862 254.202 -12.060 1.00 42.87  ? 59  SER H CA  1 
ATOM   8075  C  C   . SER H  1 60  ? -10.914 253.657 -13.510 1.00 37.87  ? 59  SER H C   1 
ATOM   8076  O  O   . SER H  1 60  ? -10.515 254.327 -14.440 1.00 41.05  ? 59  SER H O   1 
ATOM   8077  C  CB  . SER H  1 60  ? -9.466  254.683 -11.656 1.00 39.67  ? 59  SER H CB  1 
ATOM   8078  O  OG  . SER H  1 60  ? -8.759  253.662 -10.983 1.00 41.62  ? 59  SER H OG  1 
ATOM   8079  N  N   . ALA H  1 61  ? -11.433 252.462 -13.702 1.00 36.58  ? 60  ALA H N   1 
ATOM   8080  C  CA  . ALA H  1 61  ? -11.590 251.936 -15.072 1.00 38.81  ? 60  ALA H CA  1 
ATOM   8081  C  C   . ALA H  1 61  ? -12.751 252.608 -15.890 1.00 39.42  ? 60  ALA H C   1 
ATOM   8082  O  O   . ALA H  1 61  ? -12.864 252.366 -17.073 1.00 37.38  ? 60  ALA H O   1 
ATOM   8083  C  CB  . ALA H  1 61  ? -11.751 250.399 -15.054 1.00 32.47  ? 60  ALA H CB  1 
ATOM   8084  N  N   . GLY H  1 62  ? -13.602 253.411 -15.235 1.00 40.32  ? 61  GLY H N   1 
ATOM   8085  C  CA  . GLY H  1 62  ? -14.713 254.117 -15.874 1.00 39.65  ? 61  GLY H CA  1 
ATOM   8086  C  C   . GLY H  1 62  ? -15.868 253.151 -16.103 1.00 47.55  ? 61  GLY H C   1 
ATOM   8087  O  O   . GLY H  1 62  ? -15.943 252.036 -15.471 1.00 46.34  ? 61  GLY H O   1 
ATOM   8088  N  N   . PRO H  1 63  ? -16.779 253.540 -17.009 1.00 40.56  ? 62  PRO H N   1 
ATOM   8089  C  CA  . PRO H  1 63  ? -17.975 252.770 -17.423 1.00 39.31  ? 62  PRO H CA  1 
ATOM   8090  C  C   . PRO H  1 63  ? -17.578 251.679 -18.427 1.00 36.45  ? 62  PRO H C   1 
ATOM   8091  O  O   . PRO H  1 63  ? -16.423 251.639 -18.836 1.00 33.58  ? 62  PRO H O   1 
ATOM   8092  C  CB  . PRO H  1 63  ? -18.828 253.853 -18.109 1.00 37.06  ? 62  PRO H CB  1 
ATOM   8093  C  CG  . PRO H  1 63  ? -17.773 254.722 -18.748 1.00 36.74  ? 62  PRO H CG  1 
ATOM   8094  C  CD  . PRO H  1 63  ? -16.651 254.799 -17.752 1.00 36.61  ? 62  PRO H CD  1 
ATOM   8095  N  N   . HIS H  1 64  ? -18.512 250.801 -18.783 1.00 34.38  ? 63  HIS H N   1 
ATOM   8096  C  CA  . HIS H  1 64  ? -18.388 249.892 -19.919 1.00 37.16  ? 63  HIS H CA  1 
ATOM   8097  C  C   . HIS H  1 64  ? -17.825 250.609 -21.114 1.00 37.45  ? 63  HIS H C   1 
ATOM   8098  O  O   . HIS H  1 64  ? -18.275 251.680 -21.393 1.00 43.71  ? 63  HIS H O   1 
ATOM   8099  C  CB  . HIS H  1 64  ? -19.764 249.215 -20.196 1.00 35.96  ? 63  HIS H CB  1 
ATOM   8100  C  CG  . HIS H  1 64  ? -20.197 248.405 -19.026 1.00 38.01  ? 63  HIS H CG  1 
ATOM   8101  N  ND1 . HIS H  1 64  ? -21.292 247.580 -19.027 1.00 37.03  ? 63  HIS H ND1 1 
ATOM   8102  C  CD2 . HIS H  1 64  ? -19.597 248.235 -17.810 1.00 36.89  ? 63  HIS H CD2 1 
ATOM   8103  C  CE1 . HIS H  1 64  ? -21.365 246.938 -17.874 1.00 35.75  ? 63  HIS H CE1 1 
ATOM   8104  N  NE2 . HIS H  1 64  ? -20.355 247.335 -17.106 1.00 37.70  ? 63  HIS H NE2 1 
ATOM   8105  N  N   . PHE H  1 65  ? -16.783 250.059 -21.751 1.00 40.04  ? 64  PHE H N   1 
ATOM   8106  C  CA  . PHE H  1 65  ? -16.286 250.531 -23.025 1.00 42.16  ? 64  PHE H CA  1 
ATOM   8107  C  C   . PHE H  1 65  ? -17.427 250.572 -24.029 1.00 46.99  ? 64  PHE H C   1 
ATOM   8108  O  O   . PHE H  1 65  ? -17.989 249.510 -24.414 1.00 46.17  ? 64  PHE H O   1 
ATOM   8109  C  CB  . PHE H  1 65  ? -15.248 249.582 -23.545 1.00 39.12  ? 64  PHE H CB  1 
ATOM   8110  C  CG  . PHE H  1 65  ? -14.600 250.047 -24.784 1.00 36.48  ? 64  PHE H CG  1 
ATOM   8111  C  CD1 . PHE H  1 65  ? -14.225 251.396 -24.930 1.00 40.10  ? 64  PHE H CD1 1 
ATOM   8112  C  CD2 . PHE H  1 65  ? -14.328 249.161 -25.809 1.00 38.09  ? 64  PHE H CD2 1 
ATOM   8113  C  CE1 . PHE H  1 65  ? -13.603 251.835 -26.088 1.00 35.99  ? 64  PHE H CE1 1 
ATOM   8114  C  CE2 . PHE H  1 65  ? -13.689 249.592 -26.999 1.00 33.96  ? 64  PHE H CE2 1 
ATOM   8115  C  CZ  . PHE H  1 65  ? -13.322 250.922 -27.110 1.00 36.13  ? 64  PHE H CZ  1 
ATOM   8116  N  N   . ASN H  1 66  ? -17.779 251.796 -24.419 1.00 45.45  ? 65  ASN H N   1 
ATOM   8117  C  CA  . ASN H  1 66  ? -18.947 252.050 -25.266 1.00 44.78  ? 65  ASN H CA  1 
ATOM   8118  C  C   . ASN H  1 66  ? -18.736 253.139 -26.344 1.00 45.46  ? 65  ASN H C   1 
ATOM   8119  O  O   . ASN H  1 66  ? -19.358 254.252 -26.273 1.00 43.58  ? 65  ASN H O   1 
ATOM   8120  C  CB  . ASN H  1 66  ? -20.022 252.600 -24.371 1.00 47.22  ? 65  ASN H CB  1 
ATOM   8121  C  CG  . ASN H  1 66  ? -21.341 252.729 -25.079 1.00 49.62  ? 65  ASN H CG  1 
ATOM   8122  O  OD1 . ASN H  1 66  ? -21.525 252.233 -26.200 1.00 54.64  ? 65  ASN H OD1 1 
ATOM   8123  N  ND2 . ASN H  1 66  ? -22.277 253.370 -24.433 1.00 48.24  ? 65  ASN H ND2 1 
ATOM   8124  N  N   . PRO H  1 67  ? -17.858 252.879 -27.313 1.00 42.54  ? 66  PRO H N   1 
ATOM   8125  C  CA  . PRO H  1 67  ? -17.549 254.028 -28.217 1.00 46.83  ? 66  PRO H CA  1 
ATOM   8126  C  C   . PRO H  1 67  ? -18.638 254.378 -29.279 1.00 52.27  ? 66  PRO H C   1 
ATOM   8127  O  O   . PRO H  1 67  ? -18.580 255.446 -29.857 1.00 50.93  ? 66  PRO H O   1 
ATOM   8128  C  CB  . PRO H  1 67  ? -16.283 253.578 -28.929 1.00 41.46  ? 66  PRO H CB  1 
ATOM   8129  C  CG  . PRO H  1 67  ? -16.426 252.071 -28.923 1.00 49.37  ? 66  PRO H CG  1 
ATOM   8130  C  CD  . PRO H  1 67  ? -17.062 251.687 -27.627 1.00 40.99  ? 66  PRO H CD  1 
ATOM   8131  N  N   . LEU H  1 68  ? -19.592 253.492 -29.539 1.00 47.71  ? 67  LEU H N   1 
ATOM   8132  C  CA  . LEU H  1 68  ? -20.655 253.802 -30.449 1.00 46.17  ? 67  LEU H CA  1 
ATOM   8133  C  C   . LEU H  1 68  ? -21.819 254.341 -29.617 1.00 50.21  ? 67  LEU H C   1 
ATOM   8134  O  O   . LEU H  1 68  ? -22.981 254.275 -30.036 1.00 53.70  ? 67  LEU H O   1 
ATOM   8135  C  CB  . LEU H  1 68  ? -21.097 252.559 -31.231 1.00 41.08  ? 67  LEU H CB  1 
ATOM   8136  C  CG  . LEU H  1 68  ? -20.076 251.694 -31.987 1.00 49.06  ? 67  LEU H CG  1 
ATOM   8137  C  CD1 . LEU H  1 68  ? -20.697 250.462 -32.668 1.00 43.47  ? 67  LEU H CD1 1 
ATOM   8138  C  CD2 . LEU H  1 68  ? -19.114 252.489 -32.916 1.00 50.85  ? 67  LEU H CD2 1 
ATOM   8139  N  N   . SER H  1 69  ? -21.541 254.821 -28.423 1.00 44.20  ? 68  SER H N   1 
ATOM   8140  C  CA  . SER H  1 69  ? -22.619 255.320 -27.538 1.00 48.70  ? 68  SER H CA  1 
ATOM   8141  C  C   . SER H  1 69  ? -23.976 254.608 -27.499 1.00 47.65  ? 68  SER H C   1 
ATOM   8142  O  O   . SER H  1 69  ? -24.988 255.277 -27.584 1.00 49.47  ? 68  SER H O   1 
ATOM   8143  C  CB  . SER H  1 69  ? -22.890 256.789 -27.845 1.00 51.05  ? 68  SER H CB  1 
ATOM   8144  O  OG  . SER H  1 69  ? -21.821 257.561 -27.384 1.00 52.40  ? 68  SER H OG  1 
ATOM   8145  N  N   . ARG H  1 70  ? -24.011 253.285 -27.317 1.00 46.58  ? 69  ARG H N   1 
ATOM   8146  C  CA  . ARG H  1 70  ? -25.286 252.556 -27.186 1.00 45.53  ? 69  ARG H CA  1 
ATOM   8147  C  C   . ARG H  1 70  ? -25.763 252.294 -25.772 1.00 44.29  ? 69  ARG H C   1 
ATOM   8148  O  O   . ARG H  1 70  ? -25.197 252.788 -24.819 1.00 44.69  ? 69  ARG H O   1 
ATOM   8149  C  CB  . ARG H  1 70  ? -25.216 251.269 -27.935 1.00 49.56  ? 69  ARG H CB  1 
ATOM   8150  C  CG  . ARG H  1 70  ? -24.566 251.485 -29.283 1.00 55.37  ? 69  ARG H CG  1 
ATOM   8151  C  CD  . ARG H  1 70  ? -25.209 250.662 -30.370 1.00 57.53  ? 69  ARG H CD  1 
ATOM   8152  N  NE  . ARG H  1 70  ? -24.990 251.456 -31.543 1.00 69.47  ? 69  ARG H NE  1 
ATOM   8153  C  CZ  . ARG H  1 70  ? -24.587 250.983 -32.718 1.00 76.94  ? 69  ARG H CZ  1 
ATOM   8154  N  NH1 . ARG H  1 70  ? -24.375 249.669 -32.864 1.00 64.53  ? 69  ARG H NH1 1 
ATOM   8155  N  NH2 . ARG H  1 70  ? -24.384 251.858 -33.731 1.00 65.27  ? 69  ARG H NH2 1 
ATOM   8156  N  N   . LYS H  1 71  ? -26.852 251.575 -25.647 1.00 40.31  ? 70  LYS H N   1 
ATOM   8157  C  CA  . LYS H  1 71  ? -27.321 251.140 -24.355 1.00 46.19  ? 70  LYS H CA  1 
ATOM   8158  C  C   . LYS H  1 71  ? -26.709 249.730 -24.026 1.00 46.50  ? 70  LYS H C   1 
ATOM   8159  O  O   . LYS H  1 71  ? -26.320 248.964 -24.963 1.00 40.72  ? 70  LYS H O   1 
ATOM   8160  C  CB  . LYS H  1 71  ? -28.867 251.169 -24.336 1.00 45.87  ? 70  LYS H CB  1 
ATOM   8161  C  CG  . LYS H  1 71  ? -29.399 252.565 -24.640 1.00 53.89  ? 70  LYS H CG  1 
ATOM   8162  C  CD  . LYS H  1 71  ? -30.790 252.832 -24.053 1.00 64.67  ? 70  LYS H CD  1 
ATOM   8163  C  CE  . LYS H  1 71  ? -31.942 252.192 -24.865 1.00 68.95  ? 70  LYS H CE  1 
ATOM   8164  N  NZ  . LYS H  1 71  ? -32.824 251.342 -23.989 1.00 67.74  ? 70  LYS H NZ  1 
ATOM   8165  N  N   . HIS H  1 72  ? -26.583 249.416 -22.719 1.00 41.93  ? 71  HIS H N   1 
ATOM   8166  C  CA  . HIS H  1 72  ? -25.989 248.139 -22.275 1.00 40.95  ? 71  HIS H CA  1 
ATOM   8167  C  C   . HIS H  1 72  ? -26.788 246.953 -22.855 1.00 42.50  ? 71  HIS H C   1 
ATOM   8168  O  O   . HIS H  1 72  ? -28.045 246.982 -22.834 1.00 46.32  ? 71  HIS H O   1 
ATOM   8169  C  CB  . HIS H  1 72  ? -25.953 248.071 -20.744 1.00 36.18  ? 71  HIS H CB  1 
ATOM   8170  C  CG  . HIS H  1 72  ? -25.484 246.753 -20.226 1.00 39.54  ? 71  HIS H CG  1 
ATOM   8171  N  ND1 . HIS H  1 72  ? -24.150 246.380 -20.214 1.00 35.51  ? 71  HIS H ND1 1 
ATOM   8172  C  CD2 . HIS H  1 72  ? -26.181 245.694 -19.739 1.00 38.72  ? 71  HIS H CD2 1 
ATOM   8173  C  CE1 . HIS H  1 72  ? -24.046 245.166 -19.715 1.00 39.46  ? 71  HIS H CE1 1 
ATOM   8174  N  NE2 . HIS H  1 72  ? -25.268 244.724 -19.425 1.00 39.22  ? 71  HIS H NE2 1 
ATOM   8175  N  N   . GLY H  1 73  ? -26.108 245.926 -23.372 1.00 40.23  ? 72  GLY H N   1 
ATOM   8176  C  CA  . GLY H  1 73  ? -26.836 244.705 -23.826 1.00 39.57  ? 72  GLY H CA  1 
ATOM   8177  C  C   . GLY H  1 73  ? -26.172 243.377 -23.473 1.00 39.75  ? 72  GLY H C   1 
ATOM   8178  O  O   . GLY H  1 73  ? -25.187 243.386 -22.742 1.00 37.29  ? 72  GLY H O   1 
ATOM   8179  N  N   . GLY H  1 74  ? -26.722 242.242 -23.937 1.00 35.27  ? 73  GLY H N   1 
ATOM   8180  C  CA  . GLY H  1 74  ? -26.003 241.000 -23.872 1.00 35.83  ? 73  GLY H CA  1 
ATOM   8181  C  C   . GLY H  1 74  ? -24.992 240.938 -25.034 1.00 41.51  ? 73  GLY H C   1 
ATOM   8182  O  O   . GLY H  1 74  ? -25.014 241.797 -25.963 1.00 41.42  ? 73  GLY H O   1 
ATOM   8183  N  N   . PRO H  1 75  ? -24.068 239.947 -25.022 1.00 38.83  ? 74  PRO H N   1 
ATOM   8184  C  CA  . PRO H  1 75  ? -23.171 239.951 -26.171 1.00 40.76  ? 74  PRO H CA  1 
ATOM   8185  C  C   . PRO H  1 75  ? -23.919 239.588 -27.494 1.00 46.29  ? 74  PRO H C   1 
ATOM   8186  O  O   . PRO H  1 75  ? -23.540 240.037 -28.545 1.00 45.59  ? 74  PRO H O   1 
ATOM   8187  C  CB  . PRO H  1 75  ? -22.152 238.923 -25.812 1.00 37.59  ? 74  PRO H CB  1 
ATOM   8188  C  CG  . PRO H  1 75  ? -22.834 238.039 -24.839 1.00 37.12  ? 74  PRO H CG  1 
ATOM   8189  C  CD  . PRO H  1 75  ? -23.692 238.939 -24.032 1.00 38.30  ? 74  PRO H CD  1 
ATOM   8190  N  N   . LYS H  1 76  ? -25.013 238.845 -27.417 1.00 47.65  ? 75  LYS H N   1 
ATOM   8191  C  CA  . LYS H  1 76  ? -25.724 238.443 -28.624 1.00 49.48  ? 75  LYS H CA  1 
ATOM   8192  C  C   . LYS H  1 76  ? -26.639 239.531 -29.170 1.00 50.64  ? 75  LYS H C   1 
ATOM   8193  O  O   . LYS H  1 76  ? -27.182 239.344 -30.240 1.00 52.20  ? 75  LYS H O   1 
ATOM   8194  C  CB  . LYS H  1 76  ? -26.513 237.108 -28.440 1.00 46.97  ? 75  LYS H CB  1 
ATOM   8195  C  CG  . LYS H  1 76  ? -25.730 235.782 -28.564 1.00 54.50  ? 75  LYS H CG  1 
ATOM   8196  C  CD  . LYS H  1 76  ? -24.543 235.822 -29.579 1.00 66.31  ? 75  LYS H CD  1 
ATOM   8197  C  CE  . LYS H  1 76  ? -23.132 235.844 -28.898 1.00 67.98  ? 75  LYS H CE  1 
ATOM   8198  N  NZ  . LYS H  1 76  ? -21.935 236.290 -29.721 1.00 63.49  ? 75  LYS H NZ  1 
ATOM   8199  N  N   . ASP H  1 77  ? -26.849 240.624 -28.431 1.00 50.65  ? 76  ASP H N   1 
ATOM   8200  C  CA  . ASP H  1 77  ? -27.809 241.672 -28.813 1.00 46.65  ? 76  ASP H CA  1 
ATOM   8201  C  C   . ASP H  1 77  ? -27.113 242.598 -29.826 1.00 48.83  ? 76  ASP H C   1 
ATOM   8202  O  O   . ASP H  1 77  ? -25.868 242.599 -29.979 1.00 55.57  ? 76  ASP H O   1 
ATOM   8203  C  CB  . ASP H  1 77  ? -28.290 242.468 -27.576 1.00 45.42  ? 76  ASP H CB  1 
ATOM   8204  C  CG  . ASP H  1 77  ? -29.223 241.652 -26.641 1.00 56.78  ? 76  ASP H CG  1 
ATOM   8205  O  OD1 . ASP H  1 77  ? -29.934 240.733 -27.151 1.00 54.10  ? 76  ASP H OD1 1 
ATOM   8206  O  OD2 . ASP H  1 77  ? -29.270 241.927 -25.378 1.00 54.90  ? 76  ASP H OD2 1 
ATOM   8207  N  N   . GLU H  1 78  ? -27.879 243.380 -30.549 1.00 48.25  ? 77  GLU H N   1 
ATOM   8208  C  CA  . GLU H  1 78  ? -27.219 244.272 -31.465 1.00 52.96  ? 77  GLU H CA  1 
ATOM   8209  C  C   . GLU H  1 78  ? -27.044 245.637 -30.754 1.00 53.37  ? 77  GLU H C   1 
ATOM   8210  O  O   . GLU H  1 78  ? -26.015 246.335 -30.915 1.00 47.98  ? 77  GLU H O   1 
ATOM   8211  C  CB  . GLU H  1 78  ? -28.008 244.303 -32.780 1.00 57.75  ? 77  GLU H CB  1 
ATOM   8212  C  CG  . GLU H  1 78  ? -28.423 245.697 -33.279 1.00 73.28  ? 77  GLU H CG  1 
ATOM   8213  C  CD  . GLU H  1 78  ? -27.310 246.476 -34.009 1.00 82.73  ? 77  GLU H CD  1 
ATOM   8214  O  OE1 . GLU H  1 78  ? -26.222 245.858 -34.289 1.00 71.68  ? 77  GLU H OE1 1 
ATOM   8215  O  OE2 . GLU H  1 78  ? -27.542 247.700 -34.306 1.00 71.14  ? 77  GLU H OE2 1 
ATOM   8216  N  N   . GLU H  1 79  ? -28.049 246.006 -29.964 1.00 47.29  ? 78  GLU H N   1 
ATOM   8217  C  CA  . GLU H  1 79  ? -27.899 247.164 -29.097 1.00 47.47  ? 78  GLU H CA  1 
ATOM   8218  C  C   . GLU H  1 79  ? -27.080 246.693 -27.884 1.00 44.02  ? 78  GLU H C   1 
ATOM   8219  O  O   . GLU H  1 79  ? -27.621 246.082 -26.918 1.00 43.39  ? 78  GLU H O   1 
ATOM   8220  C  CB  . GLU H  1 79  ? -29.286 247.714 -28.703 1.00 48.65  ? 78  GLU H CB  1 
ATOM   8221  C  CG  . GLU H  1 79  ? -29.371 249.072 -27.961 1.00 52.29  ? 78  GLU H CG  1 
ATOM   8222  C  CD  . GLU H  1 79  ? -28.735 250.294 -28.675 1.00 60.30  ? 78  GLU H CD  1 
ATOM   8223  O  OE1 . GLU H  1 79  ? -28.459 250.301 -29.939 1.00 62.14  ? 78  GLU H OE1 1 
ATOM   8224  O  OE2 . GLU H  1 79  ? -28.514 251.288 -27.937 1.00 52.64  ? 78  GLU H OE2 1 
ATOM   8225  N  N   . ARG H  1 80  ? -25.775 246.917 -27.974 1.00 38.98  ? 79  ARG H N   1 
ATOM   8226  C  CA  . ARG H  1 80  ? -24.855 246.615 -26.860 1.00 42.51  ? 79  ARG H CA  1 
ATOM   8227  C  C   . ARG H  1 80  ? -23.705 247.595 -26.775 1.00 39.21  ? 79  ARG H C   1 
ATOM   8228  O  O   . ARG H  1 80  ? -23.381 248.246 -27.759 1.00 38.90  ? 79  ARG H O   1 
ATOM   8229  C  CB  . ARG H  1 80  ? -24.294 245.188 -26.922 1.00 37.61  ? 79  ARG H CB  1 
ATOM   8230  C  CG  . ARG H  1 80  ? -23.494 244.877 -28.175 1.00 33.16  ? 79  ARG H CG  1 
ATOM   8231  C  CD  . ARG H  1 80  ? -22.940 243.447 -28.031 1.00 38.93  ? 79  ARG H CD  1 
ATOM   8232  N  NE  . ARG H  1 80  ? -21.549 243.526 -27.585 1.00 38.02  ? 79  ARG H NE  1 
ATOM   8233  C  CZ  . ARG H  1 80  ? -20.644 242.553 -27.648 1.00 38.55  ? 79  ARG H CZ  1 
ATOM   8234  N  NH1 . ARG H  1 80  ? -20.949 241.345 -28.098 1.00 40.44  ? 79  ARG H NH1 1 
ATOM   8235  N  NH2 . ARG H  1 80  ? -19.416 242.803 -27.245 1.00 36.01  ? 79  ARG H NH2 1 
ATOM   8236  N  N   . HIS H  1 81  ? -23.052 247.657 -25.610 1.00 38.77  ? 80  HIS H N   1 
ATOM   8237  C  CA  . HIS H  1 81  ? -21.771 248.294 -25.516 1.00 34.13  ? 80  HIS H CA  1 
ATOM   8238  C  C   . HIS H  1 81  ? -20.831 247.294 -26.155 1.00 33.65  ? 80  HIS H C   1 
ATOM   8239  O  O   . HIS H  1 81  ? -21.076 246.051 -26.078 1.00 33.39  ? 80  HIS H O   1 
ATOM   8240  C  CB  . HIS H  1 81  ? -21.367 248.489 -24.050 1.00 39.77  ? 80  HIS H CB  1 
ATOM   8241  C  CG  . HIS H  1 81  ? -22.279 249.370 -23.249 1.00 44.23  ? 80  HIS H CG  1 
ATOM   8242  N  ND1 . HIS H  1 81  ? -22.399 249.262 -21.873 1.00 45.34  ? 80  HIS H ND1 1 
ATOM   8243  C  CD2 . HIS H  1 81  ? -23.066 250.405 -23.602 1.00 43.16  ? 80  HIS H CD2 1 
ATOM   8244  C  CE1 . HIS H  1 81  ? -23.280 250.139 -21.434 1.00 37.46  ? 80  HIS H CE1 1 
ATOM   8245  N  NE2 . HIS H  1 81  ? -23.675 250.865 -22.453 1.00 38.85  ? 80  HIS H NE2 1 
ATOM   8246  N  N   . VAL H  1 82  ? -19.750 247.815 -26.752 1.00 32.72  ? 81  VAL H N   1 
ATOM   8247  C  CA  . VAL H  1 82  ? -18.653 246.998 -27.228 1.00 34.37  ? 81  VAL H CA  1 
ATOM   8248  C  C   . VAL H  1 82  ? -18.148 246.073 -26.109 1.00 36.18  ? 81  VAL H C   1 
ATOM   8249  O  O   . VAL H  1 82  ? -17.830 244.918 -26.367 1.00 36.53  ? 81  VAL H O   1 
ATOM   8250  C  CB  . VAL H  1 82  ? -17.485 247.836 -27.768 1.00 37.47  ? 81  VAL H CB  1 
ATOM   8251  C  CG1 . VAL H  1 82  ? -16.288 246.926 -28.079 1.00 37.74  ? 81  VAL H CG1 1 
ATOM   8252  C  CG2 . VAL H  1 82  ? -17.889 248.606 -29.030 1.00 36.62  ? 81  VAL H CG2 1 
ATOM   8253  N  N   . GLY H  1 83  ? -18.115 246.581 -24.875 1.00 34.53  ? 82  GLY H N   1 
ATOM   8254  C  CA  . GLY H  1 83  ? -17.567 245.844 -23.766 1.00 34.36  ? 82  GLY H CA  1 
ATOM   8255  C  C   . GLY H  1 83  ? -18.451 244.814 -23.128 1.00 33.02  ? 82  GLY H C   1 
ATOM   8256  O  O   . GLY H  1 83  ? -17.980 244.118 -22.266 1.00 37.16  ? 82  GLY H O   1 
ATOM   8257  N  N   . ASP H  1 84  ? -19.706 244.698 -23.545 1.00 31.68  ? 83  ASP H N   1 
ATOM   8258  C  CA  . ASP H  1 84  ? -20.638 243.701 -23.005 1.00 33.31  ? 83  ASP H CA  1 
ATOM   8259  C  C   . ASP H  1 84  ? -20.357 242.254 -23.396 1.00 35.84  ? 83  ASP H C   1 
ATOM   8260  O  O   . ASP H  1 84  ? -20.947 241.724 -24.305 1.00 39.33  ? 83  ASP H O   1 
ATOM   8261  C  CB  . ASP H  1 84  ? -22.073 244.083 -23.386 1.00 37.88  ? 83  ASP H CB  1 
ATOM   8262  C  CG  . ASP H  1 84  ? -22.463 245.479 -22.876 1.00 39.27  ? 83  ASP H CG  1 
ATOM   8263  O  OD1 . ASP H  1 84  ? -21.707 245.976 -22.076 1.00 36.31  ? 83  ASP H OD1 1 
ATOM   8264  O  OD2 . ASP H  1 84  ? -23.468 246.110 -23.279 1.00 42.58  ? 83  ASP H OD2 1 
ATOM   8265  N  N   . LEU H  1 85  ? -19.474 241.587 -22.667 1.00 38.17  ? 84  LEU H N   1 
ATOM   8266  C  CA  . LEU H  1 85  ? -19.253 240.182 -22.829 1.00 34.53  ? 84  LEU H CA  1 
ATOM   8267  C  C   . LEU H  1 85  ? -20.217 239.359 -22.061 1.00 34.33  ? 84  LEU H C   1 
ATOM   8268  O  O   . LEU H  1 85  ? -20.152 238.136 -22.141 1.00 36.36  ? 84  LEU H O   1 
ATOM   8269  C  CB  . LEU H  1 85  ? -17.814 239.840 -22.458 1.00 36.07  ? 84  LEU H CB  1 
ATOM   8270  C  CG  . LEU H  1 85  ? -16.831 240.591 -23.368 1.00 37.47  ? 84  LEU H CG  1 
ATOM   8271  C  CD1 . LEU H  1 85  ? -15.425 240.352 -22.885 1.00 35.57  ? 84  LEU H CD1 1 
ATOM   8272  C  CD2 . LEU H  1 85  ? -16.970 240.277 -24.875 1.00 37.80  ? 84  LEU H CD2 1 
ATOM   8273  N  N   . GLY H  1 86  ? -21.135 239.978 -21.316 1.00 34.10  ? 85  GLY H N   1 
ATOM   8274  C  CA  . GLY H  1 86  ? -22.241 239.202 -20.717 1.00 29.03  ? 85  GLY H CA  1 
ATOM   8275  C  C   . GLY H  1 86  ? -21.844 238.686 -19.371 1.00 31.43  ? 85  GLY H C   1 
ATOM   8276  O  O   . GLY H  1 86  ? -21.107 239.371 -18.629 1.00 31.49  ? 85  GLY H O   1 
ATOM   8277  N  N   . ASN H  1 87  ? -22.342 237.495 -19.052 1.00 31.98  ? 86  ASN H N   1 
ATOM   8278  C  CA  . ASN H  1 87  ? -21.919 236.723 -17.871 1.00 33.04  ? 86  ASN H CA  1 
ATOM   8279  C  C   . ASN H  1 87  ? -20.826 235.622 -18.012 1.00 32.85  ? 86  ASN H C   1 
ATOM   8280  O  O   . ASN H  1 87  ? -20.702 234.957 -19.044 1.00 30.06  ? 86  ASN H O   1 
ATOM   8281  C  CB  . ASN H  1 87  ? -23.121 236.067 -17.233 1.00 31.43  ? 86  ASN H CB  1 
ATOM   8282  C  CG  . ASN H  1 87  ? -24.108 237.079 -16.671 1.00 34.94  ? 86  ASN H CG  1 
ATOM   8283  O  OD1 . ASN H  1 87  ? -23.788 237.959 -15.801 1.00 34.41  ? 86  ASN H OD1 1 
ATOM   8284  N  ND2 . ASN H  1 87  ? -25.339 236.982 -17.190 1.00 34.56  ? 86  ASN H ND2 1 
ATOM   8285  N  N   . VAL H  1 88  ? -20.073 235.436 -16.933 1.00 30.49  ? 87  VAL H N   1 
ATOM   8286  C  CA  . VAL H  1 88  ? -19.351 234.166 -16.699 1.00 33.16  ? 87  VAL H CA  1 
ATOM   8287  C  C   . VAL H  1 88  ? -19.954 233.383 -15.533 1.00 35.45  ? 87  VAL H C   1 
ATOM   8288  O  O   . VAL H  1 88  ? -20.622 233.977 -14.650 1.00 38.37  ? 87  VAL H O   1 
ATOM   8289  C  CB  . VAL H  1 88  ? -17.841 234.369 -16.443 1.00 33.28  ? 87  VAL H CB  1 
ATOM   8290  C  CG1 . VAL H  1 88  ? -17.173 234.982 -17.661 1.00 32.09  ? 87  VAL H CG1 1 
ATOM   8291  C  CG2 . VAL H  1 88  ? -17.531 235.189 -15.199 1.00 30.80  ? 87  VAL H CG2 1 
ATOM   8292  N  N   . THR H  1 89  ? -19.775 232.073 -15.528 1.00 33.93  ? 88  THR H N   1 
ATOM   8293  C  CA  . THR H  1 89  ? -20.335 231.233 -14.482 1.00 34.09  ? 88  THR H CA  1 
ATOM   8294  C  C   . THR H  1 89  ? -19.314 230.577 -13.575 1.00 35.04  ? 88  THR H C   1 
ATOM   8295  O  O   . THR H  1 89  ? -18.504 229.776 -14.025 1.00 34.87  ? 88  THR H O   1 
ATOM   8296  C  CB  . THR H  1 89  ? -21.275 230.146 -15.062 1.00 34.38  ? 88  THR H CB  1 
ATOM   8297  O  OG1 . THR H  1 89  ? -22.386 230.781 -15.654 1.00 40.51  ? 88  THR H OG1 1 
ATOM   8298  C  CG2 . THR H  1 89  ? -21.880 229.179 -13.982 1.00 34.18  ? 88  THR H CG2 1 
ATOM   8299  N  N   . ALA H  1 90  ? -19.425 230.861 -12.282 1.00 36.05  ? 89  ALA H N   1 
ATOM   8300  C  CA  . ALA H  1 90  ? -18.615 230.145 -11.322 1.00 35.42  ? 89  ALA H CA  1 
ATOM   8301  C  C   . ALA H  1 90  ? -19.365 228.942 -10.834 1.00 38.52  ? 89  ALA H C   1 
ATOM   8302  O  O   . ALA H  1 90  ? -20.565 229.020 -10.598 1.00 39.56  ? 89  ALA H O   1 
ATOM   8303  C  CB  . ALA H  1 90  ? -18.226 231.022 -10.184 1.00 33.12  ? 89  ALA H CB  1 
ATOM   8304  N  N   . ASP H  1 91  ? -18.641 227.837 -10.660 1.00 38.88  ? 90  ASP H N   1 
ATOM   8305  C  CA  . ASP H  1 91  ? -19.200 226.574 -10.224 1.00 37.62  ? 90  ASP H CA  1 
ATOM   8306  C  C   . ASP H  1 91  ? -19.243 226.522 -8.689  1.00 41.68  ? 90  ASP H C   1 
ATOM   8307  O  O   . ASP H  1 91  ? -18.856 227.505 -8.034  1.00 43.53  ? 90  ASP H O   1 
ATOM   8308  C  CB  . ASP H  1 91  ? -18.304 225.463 -10.776 1.00 38.74  ? 90  ASP H CB  1 
ATOM   8309  C  CG  . ASP H  1 91  ? -16.871 225.426 -10.135 1.00 45.55  ? 90  ASP H CG  1 
ATOM   8310  O  OD1 . ASP H  1 91  ? -16.647 225.885 -8.973  1.00 47.17  ? 90  ASP H OD1 1 
ATOM   8311  O  OD2 . ASP H  1 91  ? -15.946 224.906 -10.811 1.00 41.83  ? 90  ASP H OD2 1 
ATOM   8312  N  N   . LYS H  1 92  ? -19.568 225.352 -8.113  1.00 43.62  ? 91  LYS H N   1 
ATOM   8313  C  CA  . LYS H  1 92  ? -19.622 225.209 -6.639  1.00 43.95  ? 91  LYS H CA  1 
ATOM   8314  C  C   . LYS H  1 92  ? -18.326 225.465 -5.829  1.00 41.32  ? 91  LYS H C   1 
ATOM   8315  O  O   . LYS H  1 92  ? -18.402 225.897 -4.683  1.00 39.11  ? 91  LYS H O   1 
ATOM   8316  C  CB  . LYS H  1 92  ? -20.356 223.954 -6.182  1.00 44.45  ? 91  LYS H CB  1 
ATOM   8317  C  CG  . LYS H  1 92  ? -19.603 222.655 -6.247  1.00 49.85  ? 91  LYS H CG  1 
ATOM   8318  C  CD  . LYS H  1 92  ? -20.432 221.508 -5.610  1.00 60.88  ? 91  LYS H CD  1 
ATOM   8319  C  CE  . LYS H  1 92  ? -19.793 220.136 -5.907  1.00 69.26  ? 91  LYS H CE  1 
ATOM   8320  N  NZ  . LYS H  1 92  ? -20.126 219.770 -7.332  1.00 72.65  ? 91  LYS H NZ  1 
ATOM   8321  N  N   . ASP H  1 93  ? -17.161 225.283 -6.452  1.00 44.93  ? 92  ASP H N   1 
ATOM   8322  C  CA  . ASP H  1 93  ? -15.859 225.581 -5.838  1.00 39.62  ? 92  ASP H CA  1 
ATOM   8323  C  C   . ASP H  1 93  ? -15.418 226.998 -6.122  1.00 39.23  ? 92  ASP H C   1 
ATOM   8324  O  O   . ASP H  1 93  ? -14.288 227.323 -5.863  1.00 40.07  ? 92  ASP H O   1 
ATOM   8325  C  CB  . ASP H  1 93  ? -14.811 224.590 -6.341  1.00 47.46  ? 92  ASP H CB  1 
ATOM   8326  C  CG  . ASP H  1 93  ? -15.130 223.098 -5.931  1.00 54.67  ? 92  ASP H CG  1 
ATOM   8327  O  OD1 . ASP H  1 93  ? -15.576 222.887 -4.790  1.00 52.10  ? 92  ASP H OD1 1 
ATOM   8328  O  OD2 . ASP H  1 93  ? -14.936 222.137 -6.738  1.00 53.87  ? 92  ASP H OD2 1 
ATOM   8329  N  N   . GLY H  1 94  ? -16.301 227.847 -6.669  1.00 39.69  ? 93  GLY H N   1 
ATOM   8330  C  CA  . GLY H  1 94  ? -15.951 229.258 -6.981  1.00 36.71  ? 93  GLY H CA  1 
ATOM   8331  C  C   . GLY H  1 94  ? -15.019 229.584 -8.165  1.00 35.33  ? 93  GLY H C   1 
ATOM   8332  O  O   . GLY H  1 94  ? -14.370 230.678 -8.191  1.00 34.70  ? 93  GLY H O   1 
ATOM   8333  N  N   . VAL H  1 95  ? -14.961 228.660 -9.133  1.00 33.57  ? 94  VAL H N   1 
ATOM   8334  C  CA  . VAL H  1 95  ? -14.069 228.729 -10.272 1.00 33.68  ? 94  VAL H CA  1 
ATOM   8335  C  C   . VAL H  1 95  ? -14.924 228.949 -11.483 1.00 34.25  ? 94  VAL H C   1 
ATOM   8336  O  O   . VAL H  1 95  ? -15.934 228.213 -11.735 1.00 33.88  ? 94  VAL H O   1 
ATOM   8337  C  CB  . VAL H  1 95  ? -13.203 227.415 -10.443 1.00 37.81  ? 94  VAL H CB  1 
ATOM   8338  C  CG1 . VAL H  1 95  ? -12.360 227.391 -11.737 1.00 27.50  ? 94  VAL H CG1 1 
ATOM   8339  C  CG2 . VAL H  1 95  ? -12.328 227.183 -9.213  1.00 30.50  ? 94  VAL H CG2 1 
ATOM   8340  N  N   . ALA H  1 96  ? -14.513 229.964 -12.242 1.00 32.16  ? 95  ALA H N   1 
ATOM   8341  C  CA  . ALA H  1 96  ? -15.164 230.238 -13.519 1.00 32.35  ? 95  ALA H CA  1 
ATOM   8342  C  C   . ALA H  1 96  ? -14.238 229.882 -14.665 1.00 33.50  ? 95  ALA H C   1 
ATOM   8343  O  O   . ALA H  1 96  ? -13.220 230.552 -14.857 1.00 36.07  ? 95  ALA H O   1 
ATOM   8344  C  CB  . ALA H  1 96  ? -15.608 231.678 -13.590 1.00 29.75  ? 95  ALA H CB  1 
ATOM   8345  N  N   . ASP H  1 97  ? -14.542 228.783 -15.357 1.00 34.97  ? 96  ASP H N   1 
ATOM   8346  C  CA  . ASP H  1 97  ? -13.773 228.390 -16.550 1.00 39.47  ? 96  ASP H CA  1 
ATOM   8347  C  C   . ASP H  1 97  ? -14.388 229.068 -17.727 1.00 36.11  ? 96  ASP H C   1 
ATOM   8348  O  O   . ASP H  1 97  ? -15.301 228.497 -18.397 1.00 42.70  ? 96  ASP H O   1 
ATOM   8349  C  CB  . ASP H  1 97  ? -13.725 226.855 -16.746 1.00 44.02  ? 96  ASP H CB  1 
ATOM   8350  C  CG  . ASP H  1 97  ? -12.955 226.123 -15.583 1.00 53.90  ? 96  ASP H CG  1 
ATOM   8351  O  OD1 . ASP H  1 97  ? -11.867 226.649 -15.119 1.00 48.75  ? 96  ASP H OD1 1 
ATOM   8352  O  OD2 . ASP H  1 97  ? -13.434 225.025 -15.144 1.00 47.97  ? 96  ASP H OD2 1 
ATOM   8353  N  N   . VAL H  1 98  ? -13.930 230.282 -17.951 1.00 31.14  ? 97  VAL H N   1 
ATOM   8354  C  CA  . VAL H  1 98  ? -14.515 231.202 -18.978 1.00 35.29  ? 97  VAL H CA  1 
ATOM   8355  C  C   . VAL H  1 98  ? -14.276 230.650 -20.367 1.00 36.97  ? 97  VAL H C   1 
ATOM   8356  O  O   . VAL H  1 98  ? -13.175 230.275 -20.707 1.00 41.51  ? 97  VAL H O   1 
ATOM   8357  C  CB  . VAL H  1 98  ? -13.836 232.595 -18.885 1.00 32.01  ? 97  VAL H CB  1 
ATOM   8358  C  CG1 . VAL H  1 98  ? -14.189 233.536 -20.016 1.00 29.23  ? 97  VAL H CG1 1 
ATOM   8359  C  CG2 . VAL H  1 98  ? -14.099 233.216 -17.519 1.00 29.74  ? 97  VAL H CG2 1 
ATOM   8360  N  N   . SER H  1 99  ? -15.295 230.606 -21.192 1.00 42.53  ? 98  SER H N   1 
ATOM   8361  C  CA  . SER H  1 99  ? -15.088 230.234 -22.611 1.00 39.42  ? 98  SER H CA  1 
ATOM   8362  C  C   . SER H  1 99  ? -16.103 231.065 -23.343 1.00 40.00  ? 98  SER H C   1 
ATOM   8363  O  O   . SER H  1 99  ? -17.261 230.844 -23.184 1.00 44.81  ? 98  SER H O   1 
ATOM   8364  C  CB  . SER H  1 99  ? -15.427 228.796 -22.804 1.00 37.66  ? 98  SER H CB  1 
ATOM   8365  O  OG  . SER H  1 99  ? -14.659 228.299 -23.863 1.00 44.03  ? 98  SER H OG  1 
ATOM   8366  N  N   . ILE H  1 100 ? -15.697 232.087 -24.066 1.00 38.47  ? 99  ILE H N   1 
ATOM   8367  C  CA  . ILE H  1 100 ? -16.656 233.003 -24.656 1.00 41.49  ? 99  ILE H CA  1 
ATOM   8368  C  C   . ILE H  1 100 ? -16.079 233.173 -26.046 1.00 41.42  ? 99  ILE H C   1 
ATOM   8369  O  O   . ILE H  1 100 ? -14.876 233.100 -26.190 1.00 38.29  ? 99  ILE H O   1 
ATOM   8370  C  CB  . ILE H  1 100 ? -16.697 234.355 -23.851 1.00 39.07  ? 99  ILE H CB  1 
ATOM   8371  C  CG1 . ILE H  1 100 ? -17.751 234.288 -22.771 1.00 38.46  ? 99  ILE H CG1 1 
ATOM   8372  C  CG2 . ILE H  1 100 ? -16.914 235.562 -24.744 1.00 34.44  ? 99  ILE H CG2 1 
ATOM   8373  C  CD1 . ILE H  1 100 ? -17.607 235.384 -21.739 1.00 34.48  ? 99  ILE H CD1 1 
ATOM   8374  N  N   . GLU H  1 101 ? -16.927 233.434 -27.048 1.00 44.86  ? 100 GLU H N   1 
ATOM   8375  C  CA  . GLU H  1 101 ? -16.463 233.824 -28.373 1.00 41.79  ? 100 GLU H CA  1 
ATOM   8376  C  C   . GLU H  1 101 ? -17.210 235.093 -28.685 1.00 40.25  ? 100 GLU H C   1 
ATOM   8377  O  O   . GLU H  1 101 ? -18.402 235.167 -28.420 1.00 42.25  ? 100 GLU H O   1 
ATOM   8378  C  CB  . GLU H  1 101 ? -16.750 232.685 -29.339 1.00 45.24  ? 100 GLU H CB  1 
ATOM   8379  C  CG  . GLU H  1 101 ? -15.635 232.521 -30.373 1.00 64.01  ? 100 GLU H CG  1 
ATOM   8380  C  CD  . GLU H  1 101 ? -15.983 231.600 -31.571 1.00 73.89  ? 100 GLU H CD  1 
ATOM   8381  O  OE1 . GLU H  1 101 ? -15.831 230.336 -31.433 1.00 72.99  ? 100 GLU H OE1 1 
ATOM   8382  O  OE2 . GLU H  1 101 ? -16.382 232.142 -32.654 1.00 58.13  ? 100 GLU H OE2 1 
ATOM   8383  N  N   . ASP H  1 102 ? -16.546 236.145 -29.138 1.00 36.63  ? 101 ASP H N   1 
ATOM   8384  C  CA  . ASP H  1 102 ? -17.300 237.371 -29.322 1.00 37.65  ? 101 ASP H CA  1 
ATOM   8385  C  C   . ASP H  1 102 ? -16.829 238.112 -30.564 1.00 45.44  ? 101 ASP H C   1 
ATOM   8386  O  O   . ASP H  1 102 ? -15.620 238.291 -30.716 1.00 49.22  ? 101 ASP H O   1 
ATOM   8387  C  CB  . ASP H  1 102 ? -17.161 238.299 -28.129 1.00 37.15  ? 101 ASP H CB  1 
ATOM   8388  C  CG  . ASP H  1 102 ? -18.146 239.499 -28.188 1.00 41.35  ? 101 ASP H CG  1 
ATOM   8389  O  OD1 . ASP H  1 102 ? -19.357 239.235 -28.018 1.00 41.50  ? 101 ASP H OD1 1 
ATOM   8390  O  OD2 . ASP H  1 102 ? -17.746 240.692 -28.437 1.00 40.18  ? 101 ASP H OD2 1 
ATOM   8391  N  N   . SER H  1 103 ? -17.740 238.595 -31.435 1.00 46.61  ? 102 SER H N   1 
ATOM   8392  C  CA  . SER H  1 103 ? -17.260 239.316 -32.661 1.00 50.56  ? 102 SER H CA  1 
ATOM   8393  C  C   . SER H  1 103 ? -17.361 240.816 -32.633 1.00 50.32  ? 102 SER H C   1 
ATOM   8394  O  O   . SER H  1 103 ? -17.084 241.428 -33.678 1.00 47.22  ? 102 SER H O   1 
ATOM   8395  C  CB  . SER H  1 103 ? -17.864 238.831 -34.008 1.00 50.88  ? 102 SER H CB  1 
ATOM   8396  O  OG  . SER H  1 103 ? -18.350 237.472 -33.944 1.00 55.46  ? 102 SER H OG  1 
ATOM   8397  N  N   . VAL H  1 104 ? -17.740 241.412 -31.497 1.00 41.75  ? 103 VAL H N   1 
ATOM   8398  C  CA  . VAL H  1 104 ? -17.843 242.858 -31.466 1.00 39.43  ? 103 VAL H CA  1 
ATOM   8399  C  C   . VAL H  1 104 ? -16.636 243.447 -30.821 1.00 44.34  ? 103 VAL H C   1 
ATOM   8400  O  O   . VAL H  1 104 ? -16.184 244.481 -31.247 1.00 48.41  ? 103 VAL H O   1 
ATOM   8401  C  CB  . VAL H  1 104 ? -19.124 243.339 -30.796 1.00 41.20  ? 103 VAL H CB  1 
ATOM   8402  C  CG1 . VAL H  1 104 ? -19.114 244.849 -30.646 1.00 36.71  ? 103 VAL H CG1 1 
ATOM   8403  C  CG2 . VAL H  1 104 ? -20.318 242.803 -31.565 1.00 37.55  ? 103 VAL H CG2 1 
ATOM   8404  N  N   . ILE H  1 105 ? -16.086 242.818 -29.786 1.00 45.82  ? 104 ILE H N   1 
ATOM   8405  C  CA  . ILE H  1 105 ? -14.776 243.290 -29.332 1.00 43.34  ? 104 ILE H CA  1 
ATOM   8406  C  C   . ILE H  1 105 ? -13.696 242.979 -30.369 1.00 41.82  ? 104 ILE H C   1 
ATOM   8407  O  O   . ILE H  1 105 ? -13.840 242.040 -31.158 1.00 38.24  ? 104 ILE H O   1 
ATOM   8408  C  CB  . ILE H  1 105 ? -14.313 242.629 -28.011 1.00 40.81  ? 104 ILE H CB  1 
ATOM   8409  C  CG1 . ILE H  1 105 ? -14.418 241.096 -28.072 1.00 40.73  ? 104 ILE H CG1 1 
ATOM   8410  C  CG2 . ILE H  1 105 ? -15.092 243.226 -26.883 1.00 45.94  ? 104 ILE H CG2 1 
ATOM   8411  C  CD1 . ILE H  1 105 ? -13.346 240.356 -27.279 1.00 44.28  ? 104 ILE H CD1 1 
ATOM   8412  N  N   . SER H  1 106 ? -12.573 243.681 -30.262 1.00 38.30  ? 105 SER H N   1 
ATOM   8413  C  CA  . SER H  1 106 ? -11.470 243.436 -31.130 1.00 37.61  ? 105 SER H CA  1 
ATOM   8414  C  C   . SER H  1 106 ? -10.089 243.644 -30.463 1.00 38.63  ? 105 SER H C   1 
ATOM   8415  O  O   . SER H  1 106 ? -9.952  244.454 -29.538 1.00 38.32  ? 105 SER H O   1 
ATOM   8416  C  CB  . SER H  1 106 ? -11.585 244.454 -32.266 1.00 37.69  ? 105 SER H CB  1 
ATOM   8417  O  OG  . SER H  1 106 ? -10.642 244.101 -33.229 1.00 46.30  ? 105 SER H OG  1 
ATOM   8418  N  N   . LEU H  1 107 ? -9.054  242.993 -30.998 1.00 39.57  ? 106 LEU H N   1 
ATOM   8419  C  CA  . LEU H  1 107 ? -7.691  243.289 -30.553 1.00 39.70  ? 106 LEU H CA  1 
ATOM   8420  C  C   . LEU H  1 107 ? -7.030  244.334 -31.414 1.00 44.69  ? 106 LEU H C   1 
ATOM   8421  O  O   . LEU H  1 107 ? -5.830  244.577 -31.262 1.00 47.19  ? 106 LEU H O   1 
ATOM   8422  C  CB  . LEU H  1 107 ? -6.823  242.011 -30.450 1.00 36.62  ? 106 LEU H CB  1 
ATOM   8423  C  CG  . LEU H  1 107 ? -7.358  240.948 -29.473 1.00 38.84  ? 106 LEU H CG  1 
ATOM   8424  C  CD1 . LEU H  1 107 ? -6.396  239.745 -29.466 1.00 37.11  ? 106 LEU H CD1 1 
ATOM   8425  C  CD2 . LEU H  1 107 ? -7.780  241.406 -28.042 1.00 32.36  ? 106 LEU H CD2 1 
ATOM   8426  N  N   . SER H  1 108 ? -7.768  244.938 -32.359 1.00 47.83  ? 107 SER H N   1 
ATOM   8427  C  CA  . SER H  1 108 ? -7.202  246.093 -33.146 1.00 50.02  ? 107 SER H CA  1 
ATOM   8428  C  C   . SER H  1 108 ? -8.318  246.873 -33.783 1.00 48.88  ? 107 SER H C   1 
ATOM   8429  O  O   . SER H  1 108 ? -9.436  246.403 -33.764 1.00 52.82  ? 107 SER H O   1 
ATOM   8430  C  CB  . SER H  1 108 ? -6.128  245.679 -34.185 1.00 49.22  ? 107 SER H CB  1 
ATOM   8431  O  OG  . SER H  1 108 ? -6.707  244.816 -35.105 1.00 50.84  ? 107 SER H OG  1 
ATOM   8432  N  N   . GLY H  1 109 ? -8.044  248.075 -34.281 1.00 45.71  ? 108 GLY H N   1 
ATOM   8433  C  CA  . GLY H  1 109 ? -9.119  248.882 -34.754 1.00 47.16  ? 108 GLY H CA  1 
ATOM   8434  C  C   . GLY H  1 109 ? -9.552  249.979 -33.783 1.00 58.06  ? 108 GLY H C   1 
ATOM   8435  O  O   . GLY H  1 109 ? -8.771  250.484 -32.986 1.00 60.52  ? 108 GLY H O   1 
ATOM   8436  N  N   . ASP H  1 110 ? -10.814 250.386 -33.926 1.00 62.11  ? 109 ASP H N   1 
ATOM   8437  C  CA  . ASP H  1 110 ? -11.500 251.425 -33.148 1.00 62.72  ? 109 ASP H CA  1 
ATOM   8438  C  C   . ASP H  1 110 ? -12.079 250.744 -31.919 1.00 62.29  ? 109 ASP H C   1 
ATOM   8439  O  O   . ASP H  1 110 ? -12.120 251.305 -30.820 1.00 51.68  ? 109 ASP H O   1 
ATOM   8440  C  CB  . ASP H  1 110 ? -12.731 251.907 -33.991 1.00 75.08  ? 109 ASP H CB  1 
ATOM   8441  C  CG  . ASP H  1 110 ? -12.380 253.013 -35.036 1.00 81.42  ? 109 ASP H CG  1 
ATOM   8442  O  OD1 . ASP H  1 110 ? -11.148 253.222 -35.363 1.00 66.64  ? 109 ASP H OD1 1 
ATOM   8443  O  OD2 . ASP H  1 110 ? -13.380 253.670 -35.501 1.00 71.28  ? 109 ASP H OD2 1 
ATOM   8444  N  N   . HIS H  1 111 ? -12.607 249.541 -32.166 1.00 54.26  ? 110 HIS H N   1 
ATOM   8445  C  CA  . HIS H  1 111 ? -13.113 248.686 -31.119 1.00 56.24  ? 110 HIS H CA  1 
ATOM   8446  C  C   . HIS H  1 111 ? -11.943 248.038 -30.326 1.00 54.04  ? 110 HIS H C   1 
ATOM   8447  O  O   . HIS H  1 111 ? -12.214 247.020 -29.646 1.00 50.03  ? 110 HIS H O   1 
ATOM   8448  C  CB  . HIS H  1 111 ? -14.086 247.596 -31.688 1.00 50.63  ? 110 HIS H CB  1 
ATOM   8449  C  CG  . HIS H  1 111 ? -15.366 248.132 -32.264 1.00 58.28  ? 110 HIS H CG  1 
ATOM   8450  N  ND1 . HIS H  1 111 ? -16.409 247.303 -32.662 1.00 60.33  ? 110 HIS H ND1 1 
ATOM   8451  C  CD2 . HIS H  1 111 ? -15.787 249.406 -32.503 1.00 60.17  ? 110 HIS H CD2 1 
ATOM   8452  C  CE1 . HIS H  1 111 ? -17.420 248.036 -33.101 1.00 57.77  ? 110 HIS H CE1 1 
ATOM   8453  N  NE2 . HIS H  1 111 ? -17.068 249.318 -33.022 1.00 60.73  ? 110 HIS H NE2 1 
ATOM   8454  N  N   . CYS H  1 112 ? -10.700 248.591 -30.406 1.00 49.88  ? 111 CYS H N   1 
ATOM   8455  C  CA  . CYS H  1 112 ? -9.497  247.967 -29.754 1.00 48.60  ? 111 CYS H CA  1 
ATOM   8456  C  C   . CYS H  1 112 ? -9.705  247.811 -28.211 1.00 43.98  ? 111 CYS H C   1 
ATOM   8457  O  O   . CYS H  1 112 ? -10.039 248.809 -27.506 1.00 41.18  ? 111 CYS H O   1 
ATOM   8458  C  CB  . CYS H  1 112 ? -8.249  248.809 -30.042 1.00 50.29  ? 111 CYS H CB  1 
ATOM   8459  S  SG  . CYS H  1 112 ? -6.754  247.871 -29.702 1.00 54.90  ? 111 CYS H SG  1 
ATOM   8460  N  N   . ILE H  1 113 ? -9.595  246.585 -27.682 1.00 40.22  ? 112 ILE H N   1 
ATOM   8461  C  CA  . ILE H  1 113 ? -9.796  246.434 -26.219 1.00 38.68  ? 112 ILE H CA  1 
ATOM   8462  C  C   . ILE H  1 113 ? -8.465  246.477 -25.463 1.00 39.04  ? 112 ILE H C   1 
ATOM   8463  O  O   . ILE H  1 113 ? -8.476  246.481 -24.227 1.00 40.29  ? 112 ILE H O   1 
ATOM   8464  C  CB  . ILE H  1 113 ? -10.630 245.191 -25.767 1.00 35.55  ? 112 ILE H CB  1 
ATOM   8465  C  CG1 . ILE H  1 113 ? -9.921  243.946 -26.210 1.00 34.42  ? 112 ILE H CG1 1 
ATOM   8466  C  CG2 . ILE H  1 113 ? -12.088 245.283 -26.201 1.00 34.78  ? 112 ILE H CG2 1 
ATOM   8467  C  CD1 . ILE H  1 113 ? -10.420 242.672 -25.601 1.00 38.57  ? 112 ILE H CD1 1 
ATOM   8468  N  N   . ILE H  1 114 ? -7.335  246.519 -26.187 1.00 36.93  ? 113 ILE H N   1 
ATOM   8469  C  CA  . ILE H  1 114 ? -6.021  246.526 -25.582 1.00 39.07  ? 113 ILE H CA  1 
ATOM   8470  C  C   . ILE H  1 114 ? -5.733  247.876 -24.923 1.00 42.18  ? 113 ILE H C   1 
ATOM   8471  O  O   . ILE H  1 114 ? -6.051  248.901 -25.518 1.00 40.54  ? 113 ILE H O   1 
ATOM   8472  C  CB  . ILE H  1 114 ? -4.980  246.169 -26.599 1.00 44.65  ? 113 ILE H CB  1 
ATOM   8473  C  CG1 . ILE H  1 114 ? -5.253  244.693 -27.013 1.00 44.71  ? 113 ILE H CG1 1 
ATOM   8474  C  CG2 . ILE H  1 114 ? -3.610  246.385 -25.991 1.00 41.13  ? 113 ILE H CG2 1 
ATOM   8475  C  CD1 . ILE H  1 114 ? -4.185  244.042 -27.858 1.00 39.82  ? 113 ILE H CD1 1 
ATOM   8476  N  N   . GLY H  1 115 ? -5.189  247.863 -23.691 1.00 37.83  ? 114 GLY H N   1 
ATOM   8477  C  CA  . GLY H  1 115 ? -5.018  249.078 -22.899 1.00 39.65  ? 114 GLY H CA  1 
ATOM   8478  C  C   . GLY H  1 115 ? -6.238  249.486 -22.082 1.00 39.34  ? 114 GLY H C   1 
ATOM   8479  O  O   . GLY H  1 115 ? -6.244  250.540 -21.463 1.00 38.45  ? 114 GLY H O   1 
ATOM   8480  N  N   . ARG H  1 116 ? -7.232  248.610 -22.079 1.00 36.46  ? 115 ARG H N   1 
ATOM   8481  C  CA  . ARG H  1 116 ? -8.524  248.784 -21.393 1.00 39.55  ? 115 ARG H CA  1 
ATOM   8482  C  C   . ARG H  1 116 ? -8.640  247.804 -20.263 1.00 37.95  ? 115 ARG H C   1 
ATOM   8483  O  O   . ARG H  1 116 ? -7.724  247.012 -20.061 1.00 41.71  ? 115 ARG H O   1 
ATOM   8484  C  CB  . ARG H  1 116 ? -9.711  248.653 -22.394 1.00 37.59  ? 115 ARG H CB  1 
ATOM   8485  C  CG  . ARG H  1 116 ? -9.780  249.943 -23.206 1.00 38.03  ? 115 ARG H CG  1 
ATOM   8486  C  CD  . ARG H  1 116 ? -10.909 249.991 -24.176 1.00 42.13  ? 115 ARG H CD  1 
ATOM   8487  N  NE  . ARG H  1 116 ? -10.546 250.846 -25.305 1.00 43.34  ? 115 ARG H NE  1 
ATOM   8488  C  CZ  . ARG H  1 116 ? -10.533 252.186 -25.303 1.00 45.53  ? 115 ARG H CZ  1 
ATOM   8489  N  NH1 . ARG H  1 116 ? -10.877 252.930 -24.278 1.00 45.21  ? 115 ARG H NH1 1 
ATOM   8490  N  NH2 . ARG H  1 116 ? -10.197 252.826 -26.378 1.00 46.59  ? 115 ARG H NH2 1 
ATOM   8491  N  N   . THR H  1 117 ? -9.715  247.860 -19.483 1.00 38.40  ? 116 THR H N   1 
ATOM   8492  C  CA  . THR H  1 117 ? -9.790  247.001 -18.298 1.00 35.42  ? 116 THR H CA  1 
ATOM   8493  C  C   . THR H  1 117 ? -10.863 245.958 -18.412 1.00 37.05  ? 116 THR H C   1 
ATOM   8494  O  O   . THR H  1 117 ? -11.997 246.275 -18.772 1.00 38.20  ? 116 THR H O   1 
ATOM   8495  C  CB  . THR H  1 117 ? -9.957  247.835 -17.023 1.00 36.93  ? 116 THR H CB  1 
ATOM   8496  O  OG1 . THR H  1 117 ? -8.895  248.772 -16.963 1.00 33.05  ? 116 THR H OG1 1 
ATOM   8497  C  CG2 . THR H  1 117 ? -9.925  246.953 -15.688 1.00 35.48  ? 116 THR H CG2 1 
ATOM   8498  N  N   . LEU H  1 118 ? -10.493 244.715 -18.136 1.00 35.51  ? 117 LEU H N   1 
ATOM   8499  C  CA  . LEU H  1 118 ? -11.463 243.627 -17.985 1.00 36.35  ? 117 LEU H CA  1 
ATOM   8500  C  C   . LEU H  1 118 ? -11.917 243.581 -16.498 1.00 33.35  ? 117 LEU H C   1 
ATOM   8501  O  O   . LEU H  1 118 ? -11.100 243.774 -15.607 1.00 34.51  ? 117 LEU H O   1 
ATOM   8502  C  CB  . LEU H  1 118 ? -10.795 242.333 -18.425 1.00 34.98  ? 117 LEU H CB  1 
ATOM   8503  C  CG  . LEU H  1 118 ? -11.679 241.111 -18.394 1.00 38.35  ? 117 LEU H CG  1 
ATOM   8504  C  CD1 . LEU H  1 118 ? -12.914 241.222 -19.308 1.00 31.46  ? 117 LEU H CD1 1 
ATOM   8505  C  CD2 . LEU H  1 118 ? -10.781 239.914 -18.682 1.00 32.71  ? 117 LEU H CD2 1 
ATOM   8506  N  N   . VAL H  1 119 ? -13.200 243.384 -16.223 1.00 31.75  ? 118 VAL H N   1 
ATOM   8507  C  CA  . VAL H  1 119 ? -13.701 243.532 -14.865 1.00 30.44  ? 118 VAL H CA  1 
ATOM   8508  C  C   . VAL H  1 119 ? -14.729 242.492 -14.684 1.00 33.33  ? 118 VAL H C   1 
ATOM   8509  O  O   . VAL H  1 119 ? -15.685 242.467 -15.451 1.00 36.61  ? 118 VAL H O   1 
ATOM   8510  C  CB  . VAL H  1 119 ? -14.383 244.891 -14.581 1.00 29.84  ? 118 VAL H CB  1 
ATOM   8511  C  CG1 . VAL H  1 119 ? -15.017 244.907 -13.204 1.00 27.73  ? 118 VAL H CG1 1 
ATOM   8512  C  CG2 . VAL H  1 119 ? -13.437 246.088 -14.682 1.00 29.01  ? 118 VAL H CG2 1 
ATOM   8513  N  N   . VAL H  1 120 ? -14.530 241.606 -13.702 1.00 35.26  ? 119 VAL H N   1 
ATOM   8514  C  CA  . VAL H  1 120 ? -15.565 240.618 -13.291 1.00 32.28  ? 119 VAL H CA  1 
ATOM   8515  C  C   . VAL H  1 120 ? -16.310 241.222 -12.082 1.00 35.27  ? 119 VAL H C   1 
ATOM   8516  O  O   . VAL H  1 120 ? -15.687 241.814 -11.155 1.00 36.08  ? 119 VAL H O   1 
ATOM   8517  C  CB  . VAL H  1 120 ? -15.033 239.182 -13.061 1.00 30.58  ? 119 VAL H CB  1 
ATOM   8518  C  CG1 . VAL H  1 120 ? -13.885 239.180 -12.085 1.00 31.00  ? 119 VAL H CG1 1 
ATOM   8519  C  CG2 . VAL H  1 120 ? -16.114 238.213 -12.537 1.00 32.05  ? 119 VAL H CG2 1 
ATOM   8520  N  N   . HIS H  1 121 ? -17.639 241.109 -12.135 1.00 33.32  ? 120 HIS H N   1 
ATOM   8521  C  CA  . HIS H  1 121 ? -18.536 241.837 -11.258 1.00 31.96  ? 120 HIS H CA  1 
ATOM   8522  C  C   . HIS H  1 121 ? -19.131 240.914 -10.240 1.00 35.39  ? 120 HIS H C   1 
ATOM   8523  O  O   . HIS H  1 121 ? -19.223 239.669 -10.388 1.00 34.62  ? 120 HIS H O   1 
ATOM   8524  C  CB  . HIS H  1 121 ? -19.670 242.573 -12.065 1.00 34.22  ? 120 HIS H CB  1 
ATOM   8525  C  CG  . HIS H  1 121 ? -19.206 243.804 -12.770 1.00 29.46  ? 120 HIS H CG  1 
ATOM   8526  N  ND1 . HIS H  1 121 ? -19.192 245.040 -12.162 1.00 31.51  ? 120 HIS H ND1 1 
ATOM   8527  C  CD2 . HIS H  1 121 ? -18.614 243.978 -13.977 1.00 29.15  ? 120 HIS H CD2 1 
ATOM   8528  C  CE1 . HIS H  1 121 ? -18.658 245.946 -12.983 1.00 30.01  ? 120 HIS H CE1 1 
ATOM   8529  N  NE2 . HIS H  1 121 ? -18.295 245.325 -14.092 1.00 30.67  ? 120 HIS H NE2 1 
ATOM   8530  N  N   . GLU H  1 122 ? -19.586 241.578 -9.196  1.00 40.78  ? 121 GLU H N   1 
ATOM   8531  C  CA  . GLU H  1 122 ? -20.219 240.998 -8.045  1.00 39.81  ? 121 GLU H CA  1 
ATOM   8532  C  C   . GLU H  1 122 ? -21.403 240.119 -8.334  1.00 38.38  ? 121 GLU H C   1 
ATOM   8533  O  O   . GLU H  1 122 ? -21.483 239.059 -7.749  1.00 41.16  ? 121 GLU H O   1 
ATOM   8534  C  CB  . GLU H  1 122 ? -20.650 242.138 -7.154  1.00 42.56  ? 121 GLU H CB  1 
ATOM   8535  C  CG  . GLU H  1 122 ? -21.452 241.687 -5.964  1.00 40.10  ? 121 GLU H CG  1 
ATOM   8536  C  CD  . GLU H  1 122 ? -22.219 242.835 -5.316  1.00 47.18  ? 121 GLU H CD  1 
ATOM   8537  O  OE1 . GLU H  1 122 ? -22.258 244.053 -5.741  1.00 44.58  ? 121 GLU H OE1 1 
ATOM   8538  O  OE2 . GLU H  1 122 ? -22.870 242.469 -4.339  1.00 52.88  ? 121 GLU H OE2 1 
ATOM   8539  N  N   . LYS H  1 123 ? -22.345 240.573 -9.160  1.00 35.87  ? 122 LYS H N   1 
ATOM   8540  C  CA  . LYS H  1 123 ? -23.499 239.748 -9.491  1.00 37.19  ? 122 LYS H CA  1 
ATOM   8541  C  C   . LYS H  1 123 ? -23.826 239.651 -10.965 1.00 39.39  ? 122 LYS H C   1 
ATOM   8542  O  O   . LYS H  1 123 ? -23.110 240.219 -11.821 1.00 37.50  ? 122 LYS H O   1 
ATOM   8543  C  CB  . LYS H  1 123 ? -24.756 240.122 -8.709  1.00 39.97  ? 122 LYS H CB  1 
ATOM   8544  C  CG  . LYS H  1 123 ? -25.105 241.589 -8.741  1.00 46.07  ? 122 LYS H CG  1 
ATOM   8545  C  CD  . LYS H  1 123 ? -25.374 242.006 -7.313  1.00 43.51  ? 122 LYS H CD  1 
ATOM   8546  C  CE  . LYS H  1 123 ? -26.408 243.125 -7.217  1.00 46.10  ? 122 LYS H CE  1 
ATOM   8547  N  NZ  . LYS H  1 123 ? -26.826 243.219 -5.761  1.00 49.84  ? 122 LYS H NZ  1 
ATOM   8548  N  N   . ALA H  1 124 ? -24.911 238.898 -11.222 1.00 36.59  ? 123 ALA H N   1 
ATOM   8549  C  CA  . ALA H  1 124 ? -25.398 238.654 -12.541 1.00 36.69  ? 123 ALA H CA  1 
ATOM   8550  C  C   . ALA H  1 124 ? -25.670 239.944 -13.340 1.00 36.77  ? 123 ALA H C   1 
ATOM   8551  O  O   . ALA H  1 124 ? -26.182 240.933 -12.809 1.00 35.61  ? 123 ALA H O   1 
ATOM   8552  C  CB  . ALA H  1 124 ? -26.600 237.722 -12.508 1.00 33.51  ? 123 ALA H CB  1 
ATOM   8553  N  N   . ASP H  1 125 ? -25.211 239.949 -14.586 1.00 36.02  ? 124 ASP H N   1 
ATOM   8554  C  CA  . ASP H  1 125 ? -25.615 240.953 -15.518 1.00 36.79  ? 124 ASP H CA  1 
ATOM   8555  C  C   . ASP H  1 125 ? -27.035 240.563 -16.049 1.00 36.40  ? 124 ASP H C   1 
ATOM   8556  O  O   . ASP H  1 125 ? -27.269 239.413 -16.553 1.00 32.93  ? 124 ASP H O   1 
ATOM   8557  C  CB  . ASP H  1 125 ? -24.566 240.998 -16.598 1.00 39.80  ? 124 ASP H CB  1 
ATOM   8558  C  CG  . ASP H  1 125 ? -24.857 241.998 -17.715 1.00 42.08  ? 124 ASP H CG  1 
ATOM   8559  O  OD1 . ASP H  1 125 ? -25.968 242.545 -17.862 1.00 42.79  ? 124 ASP H OD1 1 
ATOM   8560  O  OD2 . ASP H  1 125 ? -23.939 242.215 -18.521 1.00 41.39  ? 124 ASP H OD2 1 
ATOM   8561  N  N   . ASP H  1 126 ? -27.981 241.518 -15.897 1.00 34.07  ? 125 ASP H N   1 
ATOM   8562  C  CA  . ASP H  1 126 ? -29.393 241.330 -16.409 1.00 35.94  ? 125 ASP H CA  1 
ATOM   8563  C  C   . ASP H  1 126 ? -29.479 241.442 -17.930 1.00 36.17  ? 125 ASP H C   1 
ATOM   8564  O  O   . ASP H  1 126 ? -30.523 241.140 -18.486 1.00 36.93  ? 125 ASP H O   1 
ATOM   8565  C  CB  . ASP H  1 126 ? -30.504 242.170 -15.679 1.00 33.43  ? 125 ASP H CB  1 
ATOM   8566  C  CG  . ASP H  1 126 ? -30.339 243.716 -15.847 1.00 36.55  ? 125 ASP H CG  1 
ATOM   8567  O  OD1 . ASP H  1 126 ? -29.697 244.241 -16.804 1.00 35.83  ? 125 ASP H OD1 1 
ATOM   8568  O  OD2 . ASP H  1 126 ? -30.858 244.444 -14.978 1.00 37.46  ? 125 ASP H OD2 1 
ATOM   8569  N  N   . LEU H  1 127 ? -28.354 241.805 -18.576 1.00 35.16  ? 126 LEU H N   1 
ATOM   8570  C  CA  . LEU H  1 127 ? -28.162 241.834 -20.023 1.00 35.51  ? 126 LEU H CA  1 
ATOM   8571  C  C   . LEU H  1 127 ? -28.972 242.960 -20.661 1.00 38.03  ? 126 LEU H C   1 
ATOM   8572  O  O   . LEU H  1 127 ? -29.333 242.882 -21.826 1.00 40.47  ? 126 LEU H O   1 
ATOM   8573  C  CB  . LEU H  1 127 ? -28.417 240.459 -20.678 1.00 36.30  ? 126 LEU H CB  1 
ATOM   8574  C  CG  . LEU H  1 127 ? -27.671 239.214 -20.151 1.00 38.17  ? 126 LEU H CG  1 
ATOM   8575  C  CD1 . LEU H  1 127 ? -27.872 238.002 -21.019 1.00 43.31  ? 126 LEU H CD1 1 
ATOM   8576  C  CD2 . LEU H  1 127 ? -26.179 239.392 -20.098 1.00 40.00  ? 126 LEU H CD2 1 
ATOM   8577  N  N   . GLY H  1 128 ? -29.214 244.006 -19.855 1.00 39.50  ? 127 GLY H N   1 
ATOM   8578  C  CA  . GLY H  1 128 ? -29.954 245.198 -20.217 1.00 37.14  ? 127 GLY H CA  1 
ATOM   8579  C  C   . GLY H  1 128 ? -31.444 244.973 -20.345 1.00 37.99  ? 127 GLY H C   1 
ATOM   8580  O  O   . GLY H  1 128 ? -32.130 245.777 -20.920 1.00 42.53  ? 127 GLY H O   1 
ATOM   8581  N  N   . LYS H  1 129 ? -31.935 243.880 -19.807 1.00 36.52  ? 128 LYS H N   1 
ATOM   8582  C  CA  . LYS H  1 129 ? -33.350 243.555 -19.760 1.00 37.14  ? 128 LYS H CA  1 
ATOM   8583  C  C   . LYS H  1 129 ? -34.051 243.808 -18.404 1.00 35.47  ? 128 LYS H C   1 
ATOM   8584  O  O   . LYS H  1 129 ? -35.104 243.256 -18.168 1.00 36.64  ? 128 LYS H O   1 
ATOM   8585  C  CB  . LYS H  1 129 ? -33.535 242.081 -20.129 1.00 39.14  ? 128 LYS H CB  1 
ATOM   8586  C  CG  . LYS H  1 129 ? -32.970 241.767 -21.494 1.00 43.69  ? 128 LYS H CG  1 
ATOM   8587  C  CD  . LYS H  1 129 ? -33.057 240.262 -21.654 1.00 51.07  ? 128 LYS H CD  1 
ATOM   8588  C  CE  . LYS H  1 129 ? -32.584 239.955 -23.054 1.00 56.66  ? 128 LYS H CE  1 
ATOM   8589  N  NZ  . LYS H  1 129 ? -33.730 239.146 -23.573 1.00 60.20  ? 128 LYS H NZ  1 
ATOM   8590  N  N   . GLY H  1 130 ? -33.457 244.598 -17.520 1.00 35.75  ? 129 GLY H N   1 
ATOM   8591  C  CA  . GLY H  1 130 ? -34.049 244.841 -16.231 1.00 36.37  ? 129 GLY H CA  1 
ATOM   8592  C  C   . GLY H  1 130 ? -35.063 245.979 -16.108 1.00 39.28  ? 129 GLY H C   1 
ATOM   8593  O  O   . GLY H  1 130 ? -35.618 246.145 -15.030 1.00 36.38  ? 129 GLY H O   1 
ATOM   8594  N  N   . GLY H  1 131 ? -35.323 246.714 -17.210 1.00 37.23  ? 130 GLY H N   1 
ATOM   8595  C  CA  . GLY H  1 131 ? -36.275 247.821 -17.259 1.00 36.84  ? 130 GLY H CA  1 
ATOM   8596  C  C   . GLY H  1 131 ? -36.079 249.040 -16.373 1.00 37.95  ? 130 GLY H C   1 
ATOM   8597  O  O   . GLY H  1 131 ? -36.980 249.824 -16.180 1.00 38.22  ? 130 GLY H O   1 
ATOM   8598  N  N   . ASN H  1 132 ? -34.912 249.196 -15.792 1.00 41.62  ? 131 ASN H N   1 
ATOM   8599  C  CA  . ASN H  1 132 ? -34.631 250.401 -15.006 1.00 42.14  ? 131 ASN H CA  1 
ATOM   8600  C  C   . ASN H  1 132 ? -33.412 251.017 -15.624 1.00 41.47  ? 131 ASN H C   1 
ATOM   8601  O  O   . ASN H  1 132 ? -32.861 250.435 -16.545 1.00 41.42  ? 131 ASN H O   1 
ATOM   8602  C  CB  . ASN H  1 132 ? -34.511 250.145 -13.481 1.00 45.46  ? 131 ASN H CB  1 
ATOM   8603  C  CG  . ASN H  1 132 ? -33.258 249.298 -13.056 1.00 46.79  ? 131 ASN H CG  1 
ATOM   8604  O  OD1 . ASN H  1 132 ? -32.300 249.072 -13.805 1.00 42.52  ? 131 ASN H OD1 1 
ATOM   8605  N  ND2 . ASN H  1 132 ? -33.286 248.866 -11.806 1.00 42.83  ? 131 ASN H ND2 1 
ATOM   8606  N  N   . GLU H  1 133 ? -33.007 252.190 -15.160 1.00 44.37  ? 132 GLU H N   1 
ATOM   8607  C  CA  . GLU H  1 133 ? -31.951 252.922 -15.868 1.00 52.20  ? 132 GLU H CA  1 
ATOM   8608  C  C   . GLU H  1 133 ? -30.589 252.241 -15.674 1.00 49.81  ? 132 GLU H C   1 
ATOM   8609  O  O   . GLU H  1 133 ? -29.724 252.228 -16.607 1.00 45.80  ? 132 GLU H O   1 
ATOM   8610  C  CB  . GLU H  1 133 ? -31.859 254.384 -15.430 1.00 51.59  ? 132 GLU H CB  1 
ATOM   8611  C  CG  . GLU H  1 133 ? -33.079 254.846 -14.664 1.00 61.44  ? 132 GLU H CG  1 
ATOM   8612  C  CD  . GLU H  1 133 ? -33.052 256.320 -14.199 1.00 69.49  ? 132 GLU H CD  1 
ATOM   8613  O  OE1 . GLU H  1 133 ? -31.965 256.981 -14.111 1.00 65.18  ? 132 GLU H OE1 1 
ATOM   8614  O  OE2 . GLU H  1 133 ? -34.173 256.819 -13.912 1.00 63.68  ? 132 GLU H OE2 1 
ATOM   8615  N  N   . GLU H  1 134 ? -30.445 251.660 -14.486 1.00 42.17  ? 133 GLU H N   1 
ATOM   8616  C  CA  . GLU H  1 134 ? -29.223 250.992 -14.089 1.00 44.36  ? 133 GLU H CA  1 
ATOM   8617  C  C   . GLU H  1 134 ? -28.948 249.831 -15.088 1.00 43.59  ? 133 GLU H C   1 
ATOM   8618  O  O   . GLU H  1 134 ? -27.839 249.736 -15.644 1.00 41.85  ? 133 GLU H O   1 
ATOM   8619  C  CB  . GLU H  1 134 ? -29.359 250.504 -12.637 1.00 44.13  ? 133 GLU H CB  1 
ATOM   8620  C  CG  . GLU H  1 134 ? -28.028 250.141 -12.038 1.00 52.16  ? 133 GLU H CG  1 
ATOM   8621  C  CD  . GLU H  1 134 ? -27.042 251.303 -12.144 1.00 61.16  ? 133 GLU H CD  1 
ATOM   8622  O  OE1 . GLU H  1 134 ? -27.285 252.364 -11.508 1.00 69.03  ? 133 GLU H OE1 1 
ATOM   8623  O  OE2 . GLU H  1 134 ? -26.049 251.183 -12.905 1.00 58.24  ? 133 GLU H OE2 1 
ATOM   8624  N  N   . SER H  1 135 ? -29.987 249.021 -15.362 1.00 39.30  ? 134 SER H N   1 
ATOM   8625  C  CA  . SER H  1 135 ? -29.966 247.967 -16.351 1.00 35.51  ? 134 SER H CA  1 
ATOM   8626  C  C   . SER H  1 135 ? -29.406 248.442 -17.637 1.00 36.58  ? 134 SER H C   1 
ATOM   8627  O  O   . SER H  1 135 ? -28.752 247.661 -18.319 1.00 38.84  ? 134 SER H O   1 
ATOM   8628  C  CB  . SER H  1 135 ? -31.358 247.408 -16.610 1.00 38.94  ? 134 SER H CB  1 
ATOM   8629  O  OG  . SER H  1 135 ? -31.369 246.329 -17.546 1.00 35.46  ? 134 SER H OG  1 
ATOM   8630  N  N   . THR H  1 136 ? -29.599 249.717 -17.985 1.00 39.97  ? 135 THR H N   1 
ATOM   8631  C  CA  . THR H  1 136 ? -29.300 250.161 -19.357 1.00 40.19  ? 135 THR H CA  1 
ATOM   8632  C  C   . THR H  1 136 ? -27.882 250.667 -19.397 1.00 36.12  ? 135 THR H C   1 
ATOM   8633  O  O   . THR H  1 136 ? -27.372 250.980 -20.455 1.00 35.21  ? 135 THR H O   1 
ATOM   8634  C  CB  . THR H  1 136 ? -30.309 251.238 -19.885 1.00 43.38  ? 135 THR H CB  1 
ATOM   8635  O  OG1 . THR H  1 136 ? -30.072 252.452 -19.169 1.00 47.47  ? 135 THR H OG1 1 
ATOM   8636  C  CG2 . THR H  1 136 ? -31.792 250.843 -19.656 1.00 40.97  ? 135 THR H CG2 1 
ATOM   8637  N  N   . LYS H  1 137 ? -27.295 250.823 -18.215 1.00 38.47  ? 136 LYS H N   1 
ATOM   8638  C  CA  . LYS H  1 137 ? -25.884 251.249 -18.038 1.00 43.57  ? 136 LYS H CA  1 
ATOM   8639  C  C   . LYS H  1 137 ? -24.901 250.096 -17.686 1.00 39.37  ? 136 LYS H C   1 
ATOM   8640  O  O   . LYS H  1 137 ? -23.852 249.998 -18.240 1.00 38.89  ? 136 LYS H O   1 
ATOM   8641  C  CB  . LYS H  1 137 ? -25.764 252.346 -16.972 1.00 43.81  ? 136 LYS H CB  1 
ATOM   8642  C  CG  . LYS H  1 137 ? -26.279 253.681 -17.467 1.00 51.02  ? 136 LYS H CG  1 
ATOM   8643  C  CD  . LYS H  1 137 ? -26.469 254.722 -16.339 1.00 58.73  ? 136 LYS H CD  1 
ATOM   8644  C  CE  . LYS H  1 137 ? -27.018 254.116 -15.025 1.00 64.59  ? 136 LYS H CE  1 
ATOM   8645  N  NZ  . LYS H  1 137 ? -27.509 255.014 -13.890 1.00 62.96  ? 136 LYS H NZ  1 
ATOM   8646  N  N   . THR H  1 138 ? -25.264 249.229 -16.764 1.00 40.70  ? 137 THR H N   1 
ATOM   8647  C  CA  . THR H  1 138 ? -24.308 248.321 -16.137 1.00 39.43  ? 137 THR H CA  1 
ATOM   8648  C  C   . THR H  1 138 ? -24.919 246.921 -16.102 1.00 39.63  ? 137 THR H C   1 
ATOM   8649  O  O   . THR H  1 138 ? -24.276 245.955 -15.690 1.00 38.43  ? 137 THR H O   1 
ATOM   8650  C  CB  . THR H  1 138 ? -24.022 248.762 -14.681 1.00 38.13  ? 137 THR H CB  1 
ATOM   8651  O  OG1 . THR H  1 138 ? -25.143 248.433 -13.823 1.00 36.37  ? 137 THR H OG1 1 
ATOM   8652  C  CG2 . THR H  1 138 ? -23.566 250.278 -14.551 1.00 32.06  ? 137 THR H CG2 1 
ATOM   8653  N  N   . GLY H  1 139 ? -26.184 246.820 -16.499 1.00 35.04  ? 138 GLY H N   1 
ATOM   8654  C  CA  . GLY H  1 139 ? -26.916 245.563 -16.389 1.00 35.49  ? 138 GLY H CA  1 
ATOM   8655  C  C   . GLY H  1 139 ? -27.059 245.117 -14.943 1.00 36.39  ? 138 GLY H C   1 
ATOM   8656  O  O   . GLY H  1 139 ? -27.165 243.896 -14.659 1.00 37.61  ? 138 GLY H O   1 
ATOM   8657  N  N   . ASN H  1 140 ? -27.045 246.086 -14.018 1.00 37.11  ? 139 ASN H N   1 
ATOM   8658  C  CA  . ASN H  1 140 ? -27.219 245.778 -12.572 1.00 42.02  ? 139 ASN H CA  1 
ATOM   8659  C  C   . ASN H  1 140 ? -26.245 244.771 -12.015 1.00 39.56  ? 139 ASN H C   1 
ATOM   8660  O  O   . ASN H  1 140 ? -26.659 243.976 -11.146 1.00 43.05  ? 139 ASN H O   1 
ATOM   8661  C  CB  . ASN H  1 140 ? -28.677 245.279 -12.253 1.00 37.24  ? 139 ASN H CB  1 
ATOM   8662  C  CG  . ASN H  1 140 ? -29.672 246.438 -12.211 1.00 42.14  ? 139 ASN H CG  1 
ATOM   8663  O  OD1 . ASN H  1 140 ? -29.416 247.487 -11.574 1.00 44.37  ? 139 ASN H OD1 1 
ATOM   8664  N  ND2 . ASN H  1 140 ? -30.765 246.300 -12.955 1.00 40.72  ? 139 ASN H ND2 1 
ATOM   8665  N  N   . ALA H  1 141 ? -25.006 244.737 -12.535 1.00 39.87  ? 140 ALA H N   1 
ATOM   8666  C  CA  . ALA H  1 141 ? -24.056 243.650 -12.168 1.00 40.35  ? 140 ALA H CA  1 
ATOM   8667  C  C   . ALA H  1 141 ? -23.237 243.930 -10.871 1.00 39.88  ? 140 ALA H C   1 
ATOM   8668  O  O   . ALA H  1 141 ? -22.530 243.053 -10.356 1.00 40.78  ? 140 ALA H O   1 
ATOM   8669  C  CB  . ALA H  1 141 ? -23.163 243.322 -13.301 1.00 38.71  ? 140 ALA H CB  1 
ATOM   8670  N  N   . GLY H  1 142 ? -23.391 245.148 -10.351 1.00 36.64  ? 141 GLY H N   1 
ATOM   8671  C  CA  . GLY H  1 142 ? -22.990 245.471 -9.039  1.00 35.63  ? 141 GLY H CA  1 
ATOM   8672  C  C   . GLY H  1 142 ? -21.518 245.735 -8.986  1.00 41.16  ? 141 GLY H C   1 
ATOM   8673  O  O   . GLY H  1 142 ? -20.935 246.246 -9.960  1.00 39.20  ? 141 GLY H O   1 
ATOM   8674  N  N   . SER H  1 143 ? -20.875 245.393 -7.869  1.00 41.14  ? 142 SER H N   1 
ATOM   8675  C  CA  . SER H  1 143 ? -19.518 245.959 -7.696  1.00 40.47  ? 142 SER H CA  1 
ATOM   8676  C  C   . SER H  1 143 ? -18.429 245.188 -8.483  1.00 36.65  ? 142 SER H C   1 
ATOM   8677  O  O   . SER H  1 143 ? -18.656 244.132 -9.094  1.00 38.12  ? 142 SER H O   1 
ATOM   8678  C  CB  . SER H  1 143 ? -19.185 246.147 -6.222  1.00 36.66  ? 142 SER H CB  1 
ATOM   8679  O  OG  . SER H  1 143 ? -19.203 244.847 -5.694  1.00 41.80  ? 142 SER H OG  1 
ATOM   8680  N  N   . ARG H  1 144 ? -17.254 245.769 -8.491  1.00 33.35  ? 143 ARG H N   1 
ATOM   8681  C  CA  . ARG H  1 144 ? -16.205 245.288 -9.294  1.00 36.14  ? 143 ARG H CA  1 
ATOM   8682  C  C   . ARG H  1 144 ? -15.314 244.382 -8.454  1.00 35.40  ? 143 ARG H C   1 
ATOM   8683  O  O   . ARG H  1 144 ? -14.646 244.897 -7.578  1.00 36.35  ? 143 ARG H O   1 
ATOM   8684  C  CB  . ARG H  1 144 ? -15.456 246.520 -9.777  1.00 36.71  ? 143 ARG H CB  1 
ATOM   8685  C  CG  . ARG H  1 144 ? -16.341 247.381 -10.641 1.00 35.21  ? 143 ARG H CG  1 
ATOM   8686  C  CD  . ARG H  1 144 ? -15.644 248.644 -11.101 1.00 34.30  ? 143 ARG H CD  1 
ATOM   8687  N  NE  . ARG H  1 144 ? -16.618 249.499 -11.742 1.00 38.14  ? 143 ARG H NE  1 
ATOM   8688  C  CZ  . ARG H  1 144 ? -16.323 250.445 -12.635 1.00 40.83  ? 143 ARG H CZ  1 
ATOM   8689  N  NH1 . ARG H  1 144 ? -15.065 250.667 -12.998 1.00 39.71  ? 143 ARG H NH1 1 
ATOM   8690  N  NH2 . ARG H  1 144 ? -17.292 251.170 -13.187 1.00 36.67  ? 143 ARG H NH2 1 
ATOM   8691  N  N   . LEU H  1 145 ? -15.292 243.064 -8.677  1.00 35.02  ? 144 LEU H N   1 
ATOM   8692  C  CA  . LEU H  1 145 ? -14.518 242.219 -7.740  1.00 36.78  ? 144 LEU H CA  1 
ATOM   8693  C  C   . LEU H  1 145 ? -13.046 242.153 -8.032  1.00 36.44  ? 144 LEU H C   1 
ATOM   8694  O  O   . LEU H  1 145 ? -12.276 242.138 -7.126  1.00 43.04  ? 144 LEU H O   1 
ATOM   8695  C  CB  . LEU H  1 145 ? -15.052 240.810 -7.581  1.00 35.69  ? 144 LEU H CB  1 
ATOM   8696  C  CG  . LEU H  1 145 ? -16.518 240.612 -7.349  1.00 38.61  ? 144 LEU H CG  1 
ATOM   8697  C  CD1 . LEU H  1 145 ? -16.791 239.114 -7.295  1.00 46.33  ? 144 LEU H CD1 1 
ATOM   8698  C  CD2 . LEU H  1 145 ? -16.983 241.253 -6.064  1.00 39.75  ? 144 LEU H CD2 1 
ATOM   8699  N  N   . ALA H  1 146 ? -12.662 242.136 -9.294  1.00 37.85  ? 145 ALA H N   1 
ATOM   8700  C  CA  . ALA H  1 146 ? -11.268 242.034 -9.713  1.00 37.32  ? 145 ALA H CA  1 
ATOM   8701  C  C   . ALA H  1 146 ? -11.205 242.633 -11.112 1.00 37.76  ? 145 ALA H C   1 
ATOM   8702  O  O   . ALA H  1 146 ? -12.228 242.671 -11.842 1.00 38.28  ? 145 ALA H O   1 
ATOM   8703  C  CB  . ALA H  1 146 ? -10.775 240.591 -9.693  1.00 27.41  ? 145 ALA H CB  1 
ATOM   8704  N  N   . CYS H  1 147 ? -10.026 243.120 -11.471 1.00 36.97  ? 146 CYS H N   1 
ATOM   8705  C  CA  . CYS H  1 147 ? -9.818  243.735 -12.762 1.00 40.50  ? 146 CYS H CA  1 
ATOM   8706  C  C   . CYS H  1 147 ? -8.344  243.735 -13.109 1.00 39.51  ? 146 CYS H C   1 
ATOM   8707  O  O   . CYS H  1 147 ? -7.504  243.523 -12.235 1.00 33.70  ? 146 CYS H O   1 
ATOM   8708  C  CB  . CYS H  1 147 ? -10.394 245.148 -12.812 1.00 33.84  ? 146 CYS H CB  1 
ATOM   8709  S  SG  . CYS H  1 147 ? -9.520  246.288 -11.740 1.00 37.60  ? 146 CYS H SG  1 
ATOM   8710  N  N   . GLY H  1 148 ? -8.070  243.982 -14.388 1.00 37.98  ? 147 GLY H N   1 
ATOM   8711  C  CA  . GLY H  1 148 ? -6.716  244.201 -14.878 1.00 38.87  ? 147 GLY H CA  1 
ATOM   8712  C  C   . GLY H  1 148 ? -6.763  244.828 -16.274 1.00 41.97  ? 147 GLY H C   1 
ATOM   8713  O  O   . GLY H  1 148 ? -7.807  244.761 -16.993 1.00 41.25  ? 147 GLY H O   1 
ATOM   8714  N  N   . VAL H  1 149 ? -5.644  245.429 -16.674 1.00 38.48  ? 148 VAL H N   1 
ATOM   8715  C  CA  . VAL H  1 149 ? -5.509  246.033 -18.003 1.00 37.68  ? 148 VAL H CA  1 
ATOM   8716  C  C   . VAL H  1 149 ? -5.189  244.944 -18.994 1.00 39.44  ? 148 VAL H C   1 
ATOM   8717  O  O   . VAL H  1 149 ? -4.365  244.054 -18.708 1.00 36.34  ? 148 VAL H O   1 
ATOM   8718  C  CB  . VAL H  1 149 ? -4.371  247.016 -18.010 1.00 40.09  ? 148 VAL H CB  1 
ATOM   8719  C  CG1 . VAL H  1 149 ? -4.431  247.953 -19.216 1.00 37.42  ? 148 VAL H CG1 1 
ATOM   8720  C  CG2 . VAL H  1 149 ? -4.415  247.794 -16.712 1.00 38.50  ? 148 VAL H CG2 1 
ATOM   8721  N  N   . ILE H  1 150 ? -5.898  244.983 -20.119 1.00 36.26  ? 149 ILE H N   1 
ATOM   8722  C  CA  . ILE H  1 150 ? -5.722  244.003 -21.205 1.00 39.37  ? 149 ILE H CA  1 
ATOM   8723  C  C   . ILE H  1 150 ? -4.404  244.365 -21.942 1.00 38.41  ? 149 ILE H C   1 
ATOM   8724  O  O   . ILE H  1 150 ? -4.215  245.523 -22.320 1.00 37.87  ? 149 ILE H O   1 
ATOM   8725  C  CB  . ILE H  1 150 ? -6.959  244.015 -22.146 1.00 39.88  ? 149 ILE H CB  1 
ATOM   8726  C  CG1 . ILE H  1 150 ? -8.245  243.563 -21.416 1.00 36.07  ? 149 ILE H CG1 1 
ATOM   8727  C  CG2 . ILE H  1 150 ? -6.757  243.116 -23.340 1.00 35.00  ? 149 ILE H CG2 1 
ATOM   8728  C  CD1 . ILE H  1 150 ? -9.549  244.143 -21.971 1.00 35.48  ? 149 ILE H CD1 1 
ATOM   8729  N  N   . GLY H  1 151 ? -3.471  243.422 -22.053 1.00 36.03  ? 150 GLY H N   1 
ATOM   8730  C  CA  . GLY H  1 151 ? -2.114  243.713 -22.568 1.00 36.72  ? 150 GLY H CA  1 
ATOM   8731  C  C   . GLY H  1 151 ? -1.721  242.776 -23.708 1.00 39.55  ? 150 GLY H C   1 
ATOM   8732  O  O   . GLY H  1 151 ? -2.189  241.605 -23.758 1.00 39.67  ? 150 GLY H O   1 
ATOM   8733  N  N   . ILE H  1 152 ? -0.876  243.282 -24.614 1.00 38.03  ? 151 ILE H N   1 
ATOM   8734  C  CA  . ILE H  1 152 ? -0.362  242.542 -25.754 1.00 35.61  ? 151 ILE H CA  1 
ATOM   8735  C  C   . ILE H  1 152 ? 0.349   241.283 -25.333 1.00 38.05  ? 151 ILE H C   1 
ATOM   8736  O  O   . ILE H  1 152 ? 1.252   241.328 -24.515 1.00 37.96  ? 151 ILE H O   1 
ATOM   8737  C  CB  . ILE H  1 152 ? 0.504   243.442 -26.719 1.00 40.71  ? 151 ILE H CB  1 
ATOM   8738  C  CG1 . ILE H  1 152 ? -0.407  244.504 -27.348 1.00 38.93  ? 151 ILE H CG1 1 
ATOM   8739  C  CG2 . ILE H  1 152 ? 0.988   242.669 -27.983 1.00 36.33  ? 151 ILE H CG2 1 
ATOM   8740  C  CD1 . ILE H  1 152 ? 0.227   245.872 -27.507 1.00 45.86  ? 151 ILE H CD1 1 
ATOM   8741  N  N   . ALA H  1 153 ? -0.044  240.149 -25.916 1.00 41.51  ? 152 ALA H N   1 
ATOM   8742  C  CA  . ALA H  1 153 ? 0.550   238.823 -25.549 1.00 43.39  ? 152 ALA H CA  1 
ATOM   8743  C  C   . ALA H  1 153 ? 1.347   238.239 -26.709 1.00 49.05  ? 152 ALA H C   1 
ATOM   8744  O  O   . ALA H  1 153 ? 1.218   238.698 -27.841 1.00 49.86  ? 152 ALA H O   1 
ATOM   8745  C  CB  . ALA H  1 153 ? -0.558  237.852 -25.199 1.00 39.80  ? 152 ALA H CB  1 
ATOM   8746  N  N   . GLN H  1 154 ? 2.110   237.177 -26.462 1.00 50.99  ? 153 GLN H N   1 
ATOM   8747  C  CA  . GLN H  1 154 ? 2.991   236.655 -27.507 1.00 59.46  ? 153 GLN H CA  1 
ATOM   8748  C  C   . GLN H  1 154 ? 2.395   235.465 -28.345 1.00 69.58  ? 153 GLN H C   1 
ATOM   8749  O  O   . GLN H  1 154 ? 1.823   234.443 -27.853 1.00 63.35  ? 153 GLN H O   1 
ATOM   8750  C  CB  . GLN H  1 154 ? 4.367   236.340 -26.902 1.00 58.42  ? 153 GLN H CB  1 
ATOM   8751  C  CG  . GLN H  1 154 ? 5.569   236.362 -27.872 1.00 57.61  ? 153 GLN H CG  1 
ATOM   8752  C  CD  . GLN H  1 154 ? 6.876   235.832 -27.235 1.00 57.00  ? 153 GLN H CD  1 
ATOM   8753  O  OE1 . GLN H  1 154 ? 6.941   235.585 -26.019 1.00 52.63  ? 153 GLN H OE1 1 
ATOM   8754  N  NE2 . GLN H  1 154 ? 7.892   235.568 -28.078 1.00 58.50  ? 153 GLN H NE2 1 
ATOM   8755  O  OXT . GLN H  1 154 ? 2.488   235.490 -29.605 1.00 68.90  ? 153 GLN H OXT 1 
ATOM   8756  N  N   . MET I  1 1   ? 29.235  202.543 35.475  1.00 64.42  ? 0   MET I N   1 
ATOM   8757  C  CA  . MET I  1 1   ? 28.430  203.811 35.346  1.00 77.62  ? 0   MET I CA  1 
ATOM   8758  C  C   . MET I  1 1   ? 28.570  204.480 36.746  1.00 86.34  ? 0   MET I C   1 
ATOM   8759  O  O   . MET I  1 1   ? 27.928  204.037 37.768  1.00 77.81  ? 0   MET I O   1 
ATOM   8760  C  CB  . MET I  1 1   ? 26.942  203.509 34.936  1.00 63.25  ? 0   MET I CB  1 
ATOM   8761  N  N   . ALA I  1 2   ? 29.468  205.471 36.854  1.00 75.26  ? 1   ALA I N   1 
ATOM   8762  C  CA  . ALA I  1 2   ? 29.629  206.149 38.183  1.00 77.40  ? 1   ALA I CA  1 
ATOM   8763  C  C   . ALA I  1 2   ? 29.153  207.645 38.232  1.00 66.73  ? 1   ALA I C   1 
ATOM   8764  O  O   . ALA I  1 2   ? 29.691  208.458 37.497  1.00 58.90  ? 1   ALA I O   1 
ATOM   8765  C  CB  . ALA I  1 2   ? 31.052  205.964 38.737  1.00 74.41  ? 1   ALA I CB  1 
ATOM   8766  N  N   . THR I  1 3   ? 28.140  207.969 39.063  1.00 58.71  ? 2   THR I N   1 
ATOM   8767  C  CA  . THR I  1 3   ? 27.626  209.343 39.180  1.00 55.27  ? 2   THR I CA  1 
ATOM   8768  C  C   . THR I  1 3   ? 27.705  209.915 40.630  1.00 56.35  ? 2   THR I C   1 
ATOM   8769  O  O   . THR I  1 3   ? 27.392  211.093 40.826  1.00 59.02  ? 2   THR I O   1 
ATOM   8770  C  CB  . THR I  1 3   ? 26.153  209.473 38.719  1.00 50.83  ? 2   THR I CB  1 
ATOM   8771  O  OG1 . THR I  1 3   ? 25.372  208.728 39.620  1.00 51.01  ? 2   THR I OG1 1 
ATOM   8772  C  CG2 . THR I  1 3   ? 25.911  208.931 37.336  1.00 52.28  ? 2   THR I CG2 1 
ATOM   8773  N  N   . LYS I  1 4   ? 28.083  209.117 41.633  1.00 53.79  ? 3   LYS I N   1 
ATOM   8774  C  CA  . LYS I  1 4   ? 28.138  209.583 43.038  1.00 51.37  ? 3   LYS I CA  1 
ATOM   8775  C  C   . LYS I  1 4   ? 29.315  208.980 43.762  1.00 49.83  ? 3   LYS I C   1 
ATOM   8776  O  O   . LYS I  1 4   ? 29.627  207.841 43.595  1.00 56.15  ? 3   LYS I O   1 
ATOM   8777  C  CB  . LYS I  1 4   ? 26.840  209.292 43.802  1.00 53.96  ? 3   LYS I CB  1 
ATOM   8778  C  CG  . LYS I  1 4   ? 25.596  210.009 43.246  1.00 58.78  ? 3   LYS I CG  1 
ATOM   8779  C  CD  . LYS I  1 4   ? 24.480  210.270 44.270  1.00 64.38  ? 3   LYS I CD  1 
ATOM   8780  C  CE  . LYS I  1 4   ? 23.131  209.857 43.636  1.00 73.96  ? 3   LYS I CE  1 
ATOM   8781  N  NZ  . LYS I  1 4   ? 22.033  209.416 44.584  1.00 71.02  ? 3   LYS I NZ  1 
ATOM   8782  N  N   . ALA I  1 5   ? 29.993  209.745 44.580  1.00 51.26  ? 4   ALA I N   1 
ATOM   8783  C  CA  . ALA I  1 5   ? 31.152  209.209 45.281  1.00 47.37  ? 4   ALA I CA  1 
ATOM   8784  C  C   . ALA I  1 5   ? 31.160  209.808 46.686  1.00 46.62  ? 4   ALA I C   1 
ATOM   8785  O  O   . ALA I  1 5   ? 30.428  210.769 46.950  1.00 47.93  ? 4   ALA I O   1 
ATOM   8786  C  CB  . ALA I  1 5   ? 32.427  209.515 44.513  1.00 46.21  ? 4   ALA I CB  1 
ATOM   8787  N  N   . VAL I  1 6   ? 31.928  209.228 47.594  1.00 40.01  ? 5   VAL I N   1 
ATOM   8788  C  CA  . VAL I  1 6   ? 31.923  209.739 48.939  1.00 40.61  ? 5   VAL I CA  1 
ATOM   8789  C  C   . VAL I  1 6   ? 33.292  209.431 49.521  1.00 42.13  ? 5   VAL I C   1 
ATOM   8790  O  O   . VAL I  1 6   ? 34.013  208.583 48.993  1.00 43.08  ? 5   VAL I O   1 
ATOM   8791  C  CB  . VAL I  1 6   ? 30.744  209.151 49.758  1.00 41.14  ? 5   VAL I CB  1 
ATOM   8792  C  CG1 . VAL I  1 6   ? 30.882  207.671 49.869  1.00 41.94  ? 5   VAL I CG1 1 
ATOM   8793  C  CG2 . VAL I  1 6   ? 30.574  209.786 51.154  1.00 44.31  ? 5   VAL I CG2 1 
ATOM   8794  N  N   . CYS I  1 7   ? 33.672  210.158 50.559  1.00 38.63  ? 6   CYS I N   1 
ATOM   8795  C  CA  . CYS I  1 7   ? 34.926  209.959 51.192  1.00 38.39  ? 6   CYS I CA  1 
ATOM   8796  C  C   . CYS I  1 7   ? 34.722  210.340 52.628  1.00 41.57  ? 6   CYS I C   1 
ATOM   8797  O  O   . CYS I  1 7   ? 34.001  211.301 52.899  1.00 45.26  ? 6   CYS I O   1 
ATOM   8798  C  CB  . CYS I  1 7   ? 36.001  210.793 50.495  1.00 44.19  ? 6   CYS I CB  1 
ATOM   8799  S  SG  . CYS I  1 7   ? 37.564  210.973 51.365  1.00 45.79  ? 6   CYS I SG  1 
ATOM   8800  N  N   . VAL I  1 8   ? 35.273  209.536 53.550  1.00 40.56  ? 7   VAL I N   1 
ATOM   8801  C  CA  . VAL I  1 8   ? 35.197  209.827 54.977  1.00 39.40  ? 7   VAL I CA  1 
ATOM   8802  C  C   . VAL I  1 8   ? 36.615  210.271 55.388  1.00 48.31  ? 7   VAL I C   1 
ATOM   8803  O  O   . VAL I  1 8   ? 37.615  209.567 55.076  1.00 49.36  ? 7   VAL I O   1 
ATOM   8804  C  CB  . VAL I  1 8   ? 34.756  208.596 55.747  1.00 40.56  ? 7   VAL I CB  1 
ATOM   8805  C  CG1 . VAL I  1 8   ? 34.789  208.817 57.257  1.00 36.69  ? 7   VAL I CG1 1 
ATOM   8806  C  CG2 . VAL I  1 8   ? 33.381  208.193 55.296  1.00 42.06  ? 7   VAL I CG2 1 
ATOM   8807  N  N   . LEU I  1 9   ? 36.753  211.452 55.996  1.00 44.33  ? 8   LEU I N   1 
ATOM   8808  C  CA  . LEU I  1 9   ? 38.100  211.920 56.260  1.00 41.50  ? 8   LEU I CA  1 
ATOM   8809  C  C   . LEU I  1 9   ? 38.360  211.700 57.717  1.00 40.26  ? 8   LEU I C   1 
ATOM   8810  O  O   . LEU I  1 9   ? 37.599  212.172 58.535  1.00 43.09  ? 8   LEU I O   1 
ATOM   8811  C  CB  . LEU I  1 9   ? 38.336  213.375 55.780  1.00 45.11  ? 8   LEU I CB  1 
ATOM   8812  C  CG  . LEU I  1 9   ? 38.139  213.682 54.286  1.00 45.76  ? 8   LEU I CG  1 
ATOM   8813  C  CD1 . LEU I  1 9   ? 37.018  214.666 54.223  1.00 44.24  ? 8   LEU I CD1 1 
ATOM   8814  C  CD2 . LEU I  1 9   ? 39.313  214.460 53.766  1.00 45.57  ? 8   LEU I CD2 1 
ATOM   8815  N  N   . LYS I  1 10  ? 39.369  210.889 58.041  1.00 45.76  ? 9   LYS I N   1 
ATOM   8816  C  CA  . LYS I  1 10  ? 39.845  210.729 59.448  1.00 48.80  ? 9   LYS I CA  1 
ATOM   8817  C  C   . LYS I  1 10  ? 41.335  211.067 59.477  1.00 49.15  ? 9   LYS I C   1 
ATOM   8818  O  O   . LYS I  1 10  ? 42.042  211.027 58.435  1.00 44.51  ? 9   LYS I O   1 
ATOM   8819  C  CB  . LYS I  1 10  ? 39.613  209.321 60.069  1.00 47.41  ? 9   LYS I CB  1 
ATOM   8820  C  CG  . LYS I  1 10  ? 38.313  208.564 59.768  1.00 54.34  ? 9   LYS I CG  1 
ATOM   8821  N  N   . GLY I  1 11  ? 41.829  211.416 60.645  1.00 51.13  ? 10  GLY I N   1 
ATOM   8822  C  CA  . GLY I  1 11  ? 43.298  211.471 60.756  1.00 60.38  ? 10  GLY I CA  1 
ATOM   8823  C  C   . GLY I  1 11  ? 43.789  211.069 62.139  1.00 63.47  ? 10  GLY I C   1 
ATOM   8824  O  O   . GLY I  1 11  ? 42.970  210.593 62.965  1.00 62.28  ? 10  GLY I O   1 
ATOM   8825  N  N   . ASP I  1 12  ? 45.097  211.285 62.404  1.00 60.78  ? 11  ASP I N   1 
ATOM   8826  C  CA  . ASP I  1 12  ? 45.665  211.194 63.782  1.00 62.05  ? 11  ASP I CA  1 
ATOM   8827  C  C   . ASP I  1 12  ? 44.976  212.100 64.790  1.00 60.80  ? 11  ASP I C   1 
ATOM   8828  O  O   . ASP I  1 12  ? 44.426  211.599 65.774  1.00 70.51  ? 11  ASP I O   1 
ATOM   8829  C  CB  . ASP I  1 12  ? 47.143  211.511 63.795  1.00 64.20  ? 11  ASP I CB  1 
ATOM   8830  C  CG  . ASP I  1 12  ? 47.957  210.411 63.210  1.00 70.33  ? 11  ASP I CG  1 
ATOM   8831  O  OD1 . ASP I  1 12  ? 47.368  209.419 62.660  1.00 68.04  ? 11  ASP I OD1 1 
ATOM   8832  O  OD2 . ASP I  1 12  ? 49.209  210.553 63.315  1.00 65.58  ? 11  ASP I OD2 1 
ATOM   8833  N  N   . GLY I  1 13  ? 44.962  213.409 64.524  1.00 55.48  ? 12  GLY I N   1 
ATOM   8834  C  CA  . GLY I  1 13  ? 44.189  214.362 65.307  1.00 50.11  ? 12  GLY I CA  1 
ATOM   8835  C  C   . GLY I  1 13  ? 42.663  214.280 65.185  1.00 50.97  ? 12  GLY I C   1 
ATOM   8836  O  O   . GLY I  1 13  ? 42.069  213.240 64.732  1.00 47.22  ? 12  GLY I O   1 
ATOM   8837  N  N   . PRO I  1 14  ? 42.007  215.396 65.580  1.00 50.92  ? 13  PRO I N   1 
ATOM   8838  C  CA  . PRO I  1 14  ? 40.526  215.584 65.741  1.00 49.76  ? 13  PRO I CA  1 
ATOM   8839  C  C   . PRO I  1 14  ? 39.721  215.882 64.424  1.00 48.04  ? 13  PRO I C   1 
ATOM   8840  O  O   . PRO I  1 14  ? 38.477  215.753 64.380  1.00 45.95  ? 13  PRO I O   1 
ATOM   8841  C  CB  . PRO I  1 14  ? 40.447  216.766 66.729  1.00 49.99  ? 13  PRO I CB  1 
ATOM   8842  C  CG  . PRO I  1 14  ? 41.772  217.511 66.579  1.00 54.03  ? 13  PRO I CG  1 
ATOM   8843  C  CD  . PRO I  1 14  ? 42.758  216.660 65.795  1.00 46.80  ? 13  PRO I CD  1 
ATOM   8844  N  N   . VAL I  1 15  ? 40.460  216.250 63.380  1.00 44.48  ? 14  VAL I N   1 
ATOM   8845  C  CA  . VAL I  1 15  ? 39.922  216.581 62.076  1.00 47.18  ? 14  VAL I CA  1 
ATOM   8846  C  C   . VAL I  1 15  ? 39.135  215.439 61.452  1.00 51.25  ? 14  VAL I C   1 
ATOM   8847  O  O   . VAL I  1 15  ? 39.714  214.414 61.107  1.00 54.71  ? 14  VAL I O   1 
ATOM   8848  C  CB  . VAL I  1 15  ? 41.035  217.015 61.096  1.00 42.29  ? 14  VAL I CB  1 
ATOM   8849  C  CG1 . VAL I  1 15  ? 40.404  217.216 59.714  1.00 33.68  ? 14  VAL I CG1 1 
ATOM   8850  C  CG2 . VAL I  1 15  ? 41.783  218.283 61.649  1.00 40.02  ? 14  VAL I CG2 1 
ATOM   8851  N  N   . GLN I  1 16  ? 37.833  215.611 61.265  1.00 49.02  ? 15  GLN I N   1 
ATOM   8852  C  CA  . GLN I  1 16  ? 37.086  214.574 60.501  1.00 52.31  ? 15  GLN I CA  1 
ATOM   8853  C  C   . GLN I  1 16  ? 35.903  215.116 59.626  1.00 46.08  ? 15  GLN I C   1 
ATOM   8854  O  O   . GLN I  1 16  ? 35.381  216.173 59.882  1.00 43.87  ? 15  GLN I O   1 
ATOM   8855  C  CB  . GLN I  1 16  ? 36.630  213.489 61.472  1.00 47.19  ? 15  GLN I CB  1 
ATOM   8856  C  CG  . GLN I  1 16  ? 35.624  214.038 62.418  1.00 50.07  ? 15  GLN I CG  1 
ATOM   8857  C  CD  . GLN I  1 16  ? 35.688  213.374 63.771  1.00 64.86  ? 15  GLN I CD  1 
ATOM   8858  O  OE1 . GLN I  1 16  ? 35.123  212.300 63.966  1.00 60.66  ? 15  GLN I OE1 1 
ATOM   8859  N  NE2 . GLN I  1 16  ? 36.356  214.035 64.741  1.00 66.46  ? 15  GLN I NE2 1 
ATOM   8860  N  N   . GLY I  1 17  ? 35.502  214.404 58.584  1.00 50.06  ? 16  GLY I N   1 
ATOM   8861  C  CA  . GLY I  1 17  ? 34.383  214.882 57.726  1.00 45.69  ? 16  GLY I CA  1 
ATOM   8862  C  C   . GLY I  1 17  ? 33.930  213.955 56.609  1.00 41.70  ? 16  GLY I C   1 
ATOM   8863  O  O   . GLY I  1 17  ? 34.510  212.890 56.395  1.00 43.94  ? 16  GLY I O   1 
ATOM   8864  N  N   . ILE I  1 18  ? 32.907  214.364 55.881  1.00 37.51  ? 17  ILE I N   1 
ATOM   8865  C  CA  . ILE I  1 18  ? 32.317  213.523 54.899  1.00 37.97  ? 17  ILE I CA  1 
ATOM   8866  C  C   . ILE I  1 18  ? 32.194  214.420 53.686  1.00 42.97  ? 17  ILE I C   1 
ATOM   8867  O  O   . ILE I  1 18  ? 31.742  215.550 53.790  1.00 47.10  ? 17  ILE I O   1 
ATOM   8868  C  CB  . ILE I  1 18  ? 30.924  213.003 55.373  1.00 36.61  ? 17  ILE I CB  1 
ATOM   8869  C  CG1 . ILE I  1 18  ? 31.065  212.100 56.602  1.00 35.72  ? 17  ILE I CG1 1 
ATOM   8870  C  CG2 . ILE I  1 18  ? 30.205  212.319 54.231  1.00 30.78  ? 17  ILE I CG2 1 
ATOM   8871  C  CD1 . ILE I  1 18  ? 29.782  211.445 56.964  1.00 38.74  ? 17  ILE I CD1 1 
ATOM   8872  N  N   . ILE I  1 19  ? 32.608  213.950 52.530  1.00 42.32  ? 18  ILE I N   1 
ATOM   8873  C  CA  . ILE I  1 19  ? 32.503  214.771 51.374  1.00 39.82  ? 18  ILE I CA  1 
ATOM   8874  C  C   . ILE I  1 19  ? 31.835  213.930 50.298  1.00 44.10  ? 18  ILE I C   1 
ATOM   8875  O  O   . ILE I  1 19  ? 32.273  212.766 50.053  1.00 43.11  ? 18  ILE I O   1 
ATOM   8876  C  CB  . ILE I  1 19  ? 33.911  215.231 50.919  1.00 39.35  ? 18  ILE I CB  1 
ATOM   8877  C  CG1 . ILE I  1 19  ? 34.622  216.054 52.015  1.00 31.80  ? 18  ILE I CG1 1 
ATOM   8878  C  CG2 . ILE I  1 19  ? 33.855  215.915 49.533  1.00 36.31  ? 18  ILE I CG2 1 
ATOM   8879  C  CD1 . ILE I  1 19  ? 34.139  217.480 52.160  1.00 32.60  ? 18  ILE I CD1 1 
ATOM   8880  N  N   . ASN I  1 20  ? 30.804  214.520 49.675  1.00 38.98  ? 19  ASN I N   1 
ATOM   8881  C  CA  . ASN I  1 20  ? 30.051  213.899 48.593  1.00 40.43  ? 19  ASN I CA  1 
ATOM   8882  C  C   . ASN I  1 20  ? 30.493  214.396 47.212  1.00 40.97  ? 19  ASN I C   1 
ATOM   8883  O  O   . ASN I  1 20  ? 31.015  215.502 47.069  1.00 43.32  ? 19  ASN I O   1 
ATOM   8884  C  CB  . ASN I  1 20  ? 28.554  214.084 48.818  1.00 39.81  ? 19  ASN I CB  1 
ATOM   8885  C  CG  . ASN I  1 20  ? 28.149  213.728 50.230  1.00 46.49  ? 19  ASN I CG  1 
ATOM   8886  O  OD1 . ASN I  1 20  ? 28.043  214.616 51.086  1.00 50.46  ? 19  ASN I OD1 1 
ATOM   8887  N  ND2 . ASN I  1 20  ? 28.002  212.421 50.520  1.00 45.79  ? 19  ASN I ND2 1 
ATOM   8888  N  N   . PHE I  1 21  ? 30.364  213.541 46.209  1.00 39.01  ? 20  PHE I N   1 
ATOM   8889  C  CA  . PHE I  1 21  ? 30.640  213.915 44.816  1.00 39.39  ? 20  PHE I CA  1 
ATOM   8890  C  C   . PHE I  1 21  ? 29.389  213.580 44.028  1.00 45.89  ? 20  PHE I C   1 
ATOM   8891  O  O   . PHE I  1 21  ? 28.635  212.596 44.329  1.00 45.83  ? 20  PHE I O   1 
ATOM   8892  C  CB  . PHE I  1 21  ? 31.847  213.144 44.283  1.00 40.43  ? 20  PHE I CB  1 
ATOM   8893  C  CG  . PHE I  1 21  ? 33.105  213.391 45.080  1.00 38.94  ? 20  PHE I CG  1 
ATOM   8894  C  CD1 . PHE I  1 21  ? 33.285  212.798 46.348  1.00 38.12  ? 20  PHE I CD1 1 
ATOM   8895  C  CD2 . PHE I  1 21  ? 34.087  214.278 44.603  1.00 37.07  ? 20  PHE I CD2 1 
ATOM   8896  C  CE1 . PHE I  1 21  ? 34.416  213.074 47.099  1.00 36.19  ? 20  PHE I CE1 1 
ATOM   8897  C  CE2 . PHE I  1 21  ? 35.220  214.553 45.355  1.00 35.13  ? 20  PHE I CE2 1 
ATOM   8898  C  CZ  . PHE I  1 21  ? 35.383  213.950 46.589  1.00 37.88  ? 20  PHE I CZ  1 
ATOM   8899  N  N   . GLU I  1 22  ? 29.076  214.430 43.076  1.00 44.56  ? 21  GLU I N   1 
ATOM   8900  C  CA  . GLU I  1 22  ? 27.980  214.077 42.223  1.00 43.56  ? 21  GLU I CA  1 
ATOM   8901  C  C   . GLU I  1 22  ? 28.370  214.507 40.871  1.00 46.24  ? 21  GLU I C   1 
ATOM   8902  O  O   . GLU I  1 22  ? 29.028  215.559 40.703  1.00 48.90  ? 21  GLU I O   1 
ATOM   8903  C  CB  . GLU I  1 22  ? 26.694  214.709 42.662  1.00 50.15  ? 21  GLU I CB  1 
ATOM   8904  C  CG  . GLU I  1 22  ? 25.609  214.732 41.562  1.00 60.86  ? 21  GLU I CG  1 
ATOM   8905  C  CD  . GLU I  1 22  ? 24.247  214.941 42.182  1.00 71.51  ? 21  GLU I CD  1 
ATOM   8906  O  OE1 . GLU I  1 22  ? 23.964  216.136 42.540  1.00 70.47  ? 21  GLU I OE1 1 
ATOM   8907  O  OE2 . GLU I  1 22  ? 23.521  213.916 42.372  1.00 60.92  ? 21  GLU I OE2 1 
ATOM   8908  N  N   . GLN I  1 23  ? 28.028  213.672 39.901  1.00 43.85  ? 22  GLN I N   1 
ATOM   8909  C  CA  . GLN I  1 23  ? 28.359  214.012 38.537  1.00 51.01  ? 22  GLN I CA  1 
ATOM   8910  C  C   . GLN I  1 23  ? 27.335  213.444 37.533  1.00 56.19  ? 22  GLN I C   1 
ATOM   8911  O  O   . GLN I  1 23  ? 27.590  212.425 36.879  1.00 58.54  ? 22  GLN I O   1 
ATOM   8912  C  CB  . GLN I  1 23  ? 29.813  213.685 38.188  1.00 46.65  ? 22  GLN I CB  1 
ATOM   8913  C  CG  . GLN I  1 23  ? 30.173  214.113 36.767  1.00 47.32  ? 22  GLN I CG  1 
ATOM   8914  C  CD  . GLN I  1 23  ? 31.478  213.518 36.241  1.00 55.24  ? 22  GLN I CD  1 
ATOM   8915  O  OE1 . GLN I  1 23  ? 31.815  212.351 36.527  1.00 60.23  ? 22  GLN I OE1 1 
ATOM   8916  N  NE2 . GLN I  1 23  ? 32.213  214.302 35.432  1.00 55.03  ? 22  GLN I NE2 1 
ATOM   8917  N  N   . LYS I  1 24  ? 26.183  214.125 37.432  1.00 58.75  ? 23  LYS I N   1 
ATOM   8918  C  CA  . LYS I  1 24  ? 25.079  213.790 36.493  1.00 64.00  ? 23  LYS I CA  1 
ATOM   8919  C  C   . LYS I  1 24  ? 25.519  213.446 35.070  1.00 63.58  ? 23  LYS I C   1 
ATOM   8920  O  O   . LYS I  1 24  ? 25.311  212.309 34.611  1.00 67.27  ? 23  LYS I O   1 
ATOM   8921  C  CB  . LYS I  1 24  ? 24.066  214.937 36.453  1.00 72.99  ? 23  LYS I CB  1 
ATOM   8922  C  CG  . LYS I  1 24  ? 23.006  214.878 37.555  1.00 72.39  ? 23  LYS I CG  1 
ATOM   8923  C  CD  . LYS I  1 24  ? 22.255  216.239 37.607  1.00 77.53  ? 23  LYS I CD  1 
ATOM   8924  C  CE  . LYS I  1 24  ? 20.916  216.122 38.353  1.00 70.07  ? 23  LYS I CE  1 
ATOM   8925  N  NZ  . LYS I  1 24  ? 21.093  215.069 39.428  1.00 70.05  ? 23  LYS I NZ  1 
ATOM   8926  N  N   . GLU I  1 25  ? 26.159  214.409 34.404  1.00 60.15  ? 24  GLU I N   1 
ATOM   8927  C  CA  . GLU I  1 25  ? 26.646  214.218 33.048  1.00 58.06  ? 24  GLU I CA  1 
ATOM   8928  C  C   . GLU I  1 25  ? 27.994  213.571 33.065  1.00 62.43  ? 24  GLU I C   1 
ATOM   8929  O  O   . GLU I  1 25  ? 28.973  214.105 33.655  1.00 60.35  ? 24  GLU I O   1 
ATOM   8930  C  CB  . GLU I  1 25  ? 26.811  215.571 32.328  1.00 66.74  ? 24  GLU I CB  1 
ATOM   8931  C  CG  . GLU I  1 25  ? 25.632  216.569 32.365  1.00 69.57  ? 24  GLU I CG  1 
ATOM   8932  C  CD  . GLU I  1 25  ? 24.271  215.934 32.031  1.00 82.14  ? 24  GLU I CD  1 
ATOM   8933  O  OE1 . GLU I  1 25  ? 24.264  214.729 31.558  1.00 71.51  ? 24  GLU I OE1 1 
ATOM   8934  O  OE2 . GLU I  1 25  ? 23.209  216.638 32.277  1.00 75.02  ? 24  GLU I OE2 1 
ATOM   8935  N  N   . SER I  1 26  ? 28.091  212.458 32.358  1.00 63.14  ? 25  SER I N   1 
ATOM   8936  C  CA  . SER I  1 26  ? 29.370  211.721 32.294  1.00 65.34  ? 25  SER I CA  1 
ATOM   8937  C  C   . SER I  1 26  ? 30.652  212.613 32.114  1.00 66.06  ? 25  SER I C   1 
ATOM   8938  O  O   . SER I  1 26  ? 31.726  212.304 32.686  1.00 68.73  ? 25  SER I O   1 
ATOM   8939  C  CB  . SER I  1 26  ? 29.273  210.579 31.231  1.00 66.48  ? 25  SER I CB  1 
ATOM   8940  O  OG  . SER I  1 26  ? 30.370  210.616 30.289  1.00 66.24  ? 25  SER I OG  1 
ATOM   8941  N  N   . ASN I  1 27  ? 30.567  213.693 31.331  1.00 63.35  ? 26  ASN I N   1 
ATOM   8942  C  CA  . ASN I  1 27  ? 31.790  214.425 31.007  1.00 61.71  ? 26  ASN I CA  1 
ATOM   8943  C  C   . ASN I  1 27  ? 31.791  215.842 31.593  1.00 70.83  ? 26  ASN I C   1 
ATOM   8944  O  O   . ASN I  1 27  ? 32.858  216.538 31.606  1.00 66.75  ? 26  ASN I O   1 
ATOM   8945  C  CB  . ASN I  1 27  ? 32.049  214.409 29.488  1.00 75.86  ? 26  ASN I CB  1 
ATOM   8946  C  CG  . ASN I  1 27  ? 33.471  213.843 29.118  1.00 85.43  ? 26  ASN I CG  1 
ATOM   8947  O  OD1 . ASN I  1 27  ? 34.528  214.352 29.605  1.00 76.82  ? 26  ASN I OD1 1 
ATOM   8948  N  ND2 . ASN I  1 27  ? 33.502  212.798 28.240  1.00 63.56  ? 26  ASN I ND2 1 
ATOM   8949  N  N   . GLY I  1 28  ? 30.623  216.245 32.133  1.00 67.76  ? 27  GLY I N   1 
ATOM   8950  C  CA  . GLY I  1 28  ? 30.445  217.567 32.798  1.00 60.66  ? 27  GLY I CA  1 
ATOM   8951  C  C   . GLY I  1 28  ? 30.976  217.808 34.240  1.00 61.12  ? 27  GLY I C   1 
ATOM   8952  O  O   . GLY I  1 28  ? 31.863  217.067 34.776  1.00 54.87  ? 27  GLY I O   1 
ATOM   8953  N  N   . PRO I  1 29  ? 30.453  218.869 34.889  1.00 57.45  ? 28  PRO I N   1 
ATOM   8954  C  CA  . PRO I  1 29  ? 31.063  219.350 36.153  1.00 56.30  ? 28  PRO I CA  1 
ATOM   8955  C  C   . PRO I  1 29  ? 30.786  218.387 37.341  1.00 52.25  ? 28  PRO I C   1 
ATOM   8956  O  O   . PRO I  1 29  ? 29.665  217.723 37.408  1.00 50.67  ? 28  PRO I O   1 
ATOM   8957  C  CB  . PRO I  1 29  ? 30.393  220.741 36.366  1.00 55.27  ? 28  PRO I CB  1 
ATOM   8958  C  CG  . PRO I  1 29  ? 29.052  220.634 35.669  1.00 52.88  ? 28  PRO I CG  1 
ATOM   8959  C  CD  . PRO I  1 29  ? 29.204  219.602 34.552  1.00 57.27  ? 28  PRO I CD  1 
ATOM   8960  N  N   . VAL I  1 30  ? 31.792  218.304 38.236  1.00 45.84  ? 29  VAL I N   1 
ATOM   8961  C  CA  . VAL I  1 30  ? 31.629  217.550 39.500  1.00 48.31  ? 29  VAL I CA  1 
ATOM   8962  C  C   . VAL I  1 30  ? 31.292  218.469 40.682  1.00 44.48  ? 29  VAL I C   1 
ATOM   8963  O  O   . VAL I  1 30  ? 32.086  219.376 40.997  1.00 44.61  ? 29  VAL I O   1 
ATOM   8964  C  CB  . VAL I  1 30  ? 32.826  216.605 39.861  1.00 47.72  ? 29  VAL I CB  1 
ATOM   8965  C  CG1 . VAL I  1 30  ? 32.412  215.780 41.083  1.00 44.78  ? 29  VAL I CG1 1 
ATOM   8966  C  CG2 . VAL I  1 30  ? 33.171  215.668 38.685  1.00 44.81  ? 29  VAL I CG2 1 
ATOM   8967  N  N   . LYS I  1 31  ? 30.112  218.238 41.267  1.00 42.10  ? 30  LYS I N   1 
ATOM   8968  C  CA  . LYS I  1 31  ? 29.612  218.833 42.539  1.00 44.21  ? 30  LYS I CA  1 
ATOM   8969  C  C   . LYS I  1 31  ? 30.331  218.183 43.716  1.00 43.22  ? 30  LYS I C   1 
ATOM   8970  O  O   . LYS I  1 31  ? 30.339  216.970 43.849  1.00 50.52  ? 30  LYS I O   1 
ATOM   8971  C  CB  . LYS I  1 31  ? 28.117  218.506 42.658  1.00 48.02  ? 30  LYS I CB  1 
ATOM   8972  C  CG  . LYS I  1 31  ? 27.170  219.503 43.358  1.00 55.04  ? 30  LYS I CG  1 
ATOM   8973  C  CD  . LYS I  1 31  ? 25.669  219.074 43.266  1.00 61.58  ? 30  LYS I CD  1 
ATOM   8974  C  CE  . LYS I  1 31  ? 25.028  219.063 41.828  1.00 67.94  ? 30  LYS I CE  1 
ATOM   8975  N  NZ  . LYS I  1 31  ? 24.468  220.397 41.349  1.00 58.91  ? 30  LYS I NZ  1 
ATOM   8976  N  N   . VAL I  1 32  ? 30.980  218.985 44.539  1.00 43.55  ? 31  VAL I N   1 
ATOM   8977  C  CA  . VAL I  1 32  ? 31.759  218.502 45.702  1.00 43.27  ? 31  VAL I CA  1 
ATOM   8978  C  C   . VAL I  1 32  ? 31.220  219.264 46.896  1.00 46.40  ? 31  VAL I C   1 
ATOM   8979  O  O   . VAL I  1 32  ? 31.282  220.493 46.899  1.00 48.94  ? 31  VAL I O   1 
ATOM   8980  C  CB  . VAL I  1 32  ? 33.314  218.763 45.613  1.00 41.66  ? 31  VAL I CB  1 
ATOM   8981  C  CG1 . VAL I  1 32  ? 34.053  218.154 46.834  1.00 37.88  ? 31  VAL I CG1 1 
ATOM   8982  C  CG2 . VAL I  1 32  ? 33.917  218.243 44.296  1.00 36.41  ? 31  VAL I CG2 1 
ATOM   8983  N  N   . TRP I  1 33  ? 30.679  218.554 47.891  1.00 44.21  ? 32  TRP I N   1 
ATOM   8984  C  CA  . TRP I  1 33  ? 30.225  219.222 49.085  1.00 42.24  ? 32  TRP I CA  1 
ATOM   8985  C  C   . TRP I  1 33  ? 30.194  218.279 50.295  1.00 41.83  ? 32  TRP I C   1 
ATOM   8986  O  O   . TRP I  1 33  ? 29.951  217.073 50.160  1.00 45.11  ? 32  TRP I O   1 
ATOM   8987  C  CB  . TRP I  1 33  ? 28.821  219.820 48.865  1.00 37.45  ? 32  TRP I CB  1 
ATOM   8988  C  CG  . TRP I  1 33  ? 27.716  218.763 49.030  1.00 38.20  ? 32  TRP I CG  1 
ATOM   8989  C  CD1 . TRP I  1 33  ? 26.967  218.526 50.140  1.00 39.89  ? 32  TRP I CD1 1 
ATOM   8990  C  CD2 . TRP I  1 33  ? 27.316  217.786 48.058  1.00 38.78  ? 32  TRP I CD2 1 
ATOM   8991  N  NE1 . TRP I  1 33  ? 26.111  217.452 49.922  1.00 44.84  ? 32  TRP I NE1 1 
ATOM   8992  C  CE2 . TRP I  1 33  ? 26.282  217.006 48.644  1.00 36.89  ? 32  TRP I CE2 1 
ATOM   8993  C  CE3 . TRP I  1 33  ? 27.753  217.483 46.738  1.00 44.78  ? 32  TRP I CE3 1 
ATOM   8994  C  CZ2 . TRP I  1 33  ? 25.637  215.950 47.975  1.00 42.97  ? 32  TRP I CZ2 1 
ATOM   8995  C  CZ3 . TRP I  1 33  ? 27.114  216.398 46.039  1.00 50.34  ? 32  TRP I CZ3 1 
ATOM   8996  C  CH2 . TRP I  1 33  ? 26.059  215.634 46.684  1.00 47.52  ? 32  TRP I CH2 1 
ATOM   8997  N  N   . GLY I  1 34  ? 30.290  218.901 51.465  1.00 36.41  ? 33  GLY I N   1 
ATOM   8998  C  CA  . GLY I  1 34  ? 30.061  218.270 52.716  1.00 36.26  ? 33  GLY I CA  1 
ATOM   8999  C  C   . GLY I  1 34  ? 30.657  219.120 53.803  1.00 38.33  ? 33  GLY I C   1 
ATOM   9000  O  O   . GLY I  1 34  ? 30.763  220.368 53.726  1.00 40.15  ? 33  GLY I O   1 
ATOM   9001  N  N   . SER I  1 35  ? 31.123  218.455 54.826  1.00 38.50  ? 34  SER I N   1 
ATOM   9002  C  CA  . SER I  1 35  ? 31.573  219.221 55.945  1.00 40.14  ? 34  SER I CA  1 
ATOM   9003  C  C   . SER I  1 35  ? 32.791  218.521 56.615  1.00 43.27  ? 34  SER I C   1 
ATOM   9004  O  O   . SER I  1 35  ? 32.922  217.290 56.584  1.00 43.13  ? 34  SER I O   1 
ATOM   9005  C  CB  . SER I  1 35  ? 30.372  219.371 56.860  1.00 38.96  ? 34  SER I CB  1 
ATOM   9006  O  OG  . SER I  1 35  ? 30.758  220.095 57.964  1.00 44.67  ? 34  SER I OG  1 
ATOM   9007  N  N   . ILE I  1 36  ? 33.696  219.329 57.166  1.00 44.99  ? 35  ILE I N   1 
ATOM   9008  C  CA  . ILE I  1 36  ? 34.876  218.884 57.946  1.00 44.36  ? 35  ILE I CA  1 
ATOM   9009  C  C   . ILE I  1 36  ? 34.911  219.618 59.302  1.00 44.70  ? 35  ILE I C   1 
ATOM   9010  O  O   . ILE I  1 36  ? 34.846  220.860 59.333  1.00 46.57  ? 35  ILE I O   1 
ATOM   9011  C  CB  . ILE I  1 36  ? 36.197  219.174 57.189  1.00 42.35  ? 35  ILE I CB  1 
ATOM   9012  C  CG1 . ILE I  1 36  ? 36.100  218.701 55.726  1.00 39.94  ? 35  ILE I CG1 1 
ATOM   9013  C  CG2 . ILE I  1 36  ? 37.332  218.517 57.946  1.00 42.78  ? 35  ILE I CG2 1 
ATOM   9014  C  CD1 . ILE I  1 36  ? 37.336  218.889 54.862  1.00 45.58  ? 35  ILE I CD1 1 
ATOM   9015  N  N   . LYS I  1 37  ? 34.985  218.895 60.414  1.00 41.72  ? 36  LYS I N   1 
ATOM   9016  C  CA  . LYS I  1 37  ? 35.170  219.550 61.708  1.00 40.99  ? 36  LYS I CA  1 
ATOM   9017  C  C   . LYS I  1 37  ? 36.571  219.333 62.294  1.00 41.16  ? 36  LYS I C   1 
ATOM   9018  O  O   . LYS I  1 37  ? 37.375  218.599 61.720  1.00 44.00  ? 36  LYS I O   1 
ATOM   9019  C  CB  . LYS I  1 37  ? 34.092  219.138 62.704  1.00 47.10  ? 36  LYS I CB  1 
ATOM   9020  C  CG  . LYS I  1 37  ? 33.649  217.678 62.694  1.00 56.57  ? 36  LYS I CG  1 
ATOM   9021  C  CD  . LYS I  1 37  ? 32.797  217.241 63.930  1.00 60.62  ? 36  LYS I CD  1 
ATOM   9022  C  CE  . LYS I  1 37  ? 31.981  215.935 63.662  1.00 69.80  ? 36  LYS I CE  1 
ATOM   9023  N  NZ  . LYS I  1 37  ? 32.591  214.865 62.734  1.00 61.93  ? 36  LYS I NZ  1 
ATOM   9024  N  N   . GLY I  1 38  ? 36.830  219.995 63.415  1.00 40.43  ? 37  GLY I N   1 
ATOM   9025  C  CA  . GLY I  1 38  ? 38.052  219.950 64.209  1.00 43.09  ? 37  GLY I CA  1 
ATOM   9026  C  C   . GLY I  1 38  ? 39.292  220.617 63.608  1.00 46.23  ? 37  GLY I C   1 
ATOM   9027  O  O   . GLY I  1 38  ? 40.464  220.262 63.965  1.00 40.66  ? 37  GLY I O   1 
ATOM   9028  N  N   . LEU I  1 39  ? 39.036  221.531 62.672  1.00 42.02  ? 38  LEU I N   1 
ATOM   9029  C  CA  . LEU I  1 39  ? 40.096  222.210 61.991  1.00 39.99  ? 38  LEU I CA  1 
ATOM   9030  C  C   . LEU I  1 39  ? 40.429  223.442 62.788  1.00 43.40  ? 38  LEU I C   1 
ATOM   9031  O  O   . LEU I  1 39  ? 39.605  223.934 63.520  1.00 45.88  ? 38  LEU I O   1 
ATOM   9032  C  CB  . LEU I  1 39  ? 39.651  222.632 60.614  1.00 41.99  ? 38  LEU I CB  1 
ATOM   9033  C  CG  . LEU I  1 39  ? 39.681  221.552 59.536  1.00 44.61  ? 38  LEU I CG  1 
ATOM   9034  C  CD1 . LEU I  1 39  ? 38.709  221.950 58.423  1.00 40.49  ? 38  LEU I CD1 1 
ATOM   9035  C  CD2 . LEU I  1 39  ? 41.099  221.227 59.026  1.00 37.46  ? 38  LEU I CD2 1 
ATOM   9036  N  N   . THR I  1 40  ? 41.659  223.930 62.677  1.00 43.48  ? 39  THR I N   1 
ATOM   9037  C  CA  . THR I  1 40  ? 41.975  225.281 63.113  1.00 47.63  ? 39  THR I CA  1 
ATOM   9038  C  C   . THR I  1 40  ? 41.285  226.270 62.131  1.00 44.46  ? 39  THR I C   1 
ATOM   9039  O  O   . THR I  1 40  ? 41.213  225.964 60.925  1.00 46.05  ? 39  THR I O   1 
ATOM   9040  C  CB  . THR I  1 40  ? 43.530  225.508 63.158  1.00 48.01  ? 39  THR I CB  1 
ATOM   9041  O  OG1 . THR I  1 40  ? 44.114  225.152 61.880  1.00 43.62  ? 39  THR I OG1 1 
ATOM   9042  C  CG2 . THR I  1 40  ? 44.176  224.667 64.355  1.00 42.72  ? 39  THR I CG2 1 
ATOM   9043  N  N   . GLU I  1 41  ? 40.767  227.402 62.649  1.00 44.66  ? 40  GLU I N   1 
ATOM   9044  C  CA  . GLU I  1 41  ? 40.273  228.587 61.864  1.00 44.95  ? 40  GLU I CA  1 
ATOM   9045  C  C   . GLU I  1 41  ? 41.052  228.917 60.597  1.00 44.19  ? 40  GLU I C   1 
ATOM   9046  O  O   . GLU I  1 41  ? 42.277  229.018 60.638  1.00 42.95  ? 40  GLU I O   1 
ATOM   9047  C  CB  . GLU I  1 41  ? 40.507  229.814 62.707  1.00 45.03  ? 40  GLU I CB  1 
ATOM   9048  C  CG  . GLU I  1 41  ? 39.408  230.130 63.667  1.00 56.06  ? 40  GLU I CG  1 
ATOM   9049  C  CD  . GLU I  1 41  ? 39.573  231.532 64.252  1.00 68.29  ? 40  GLU I CD  1 
ATOM   9050  O  OE1 . GLU I  1 41  ? 40.712  232.092 64.161  1.00 67.43  ? 40  GLU I OE1 1 
ATOM   9051  O  OE2 . GLU I  1 41  ? 38.564  232.112 64.765  1.00 66.88  ? 40  GLU I OE2 1 
ATOM   9052  N  N   . GLY I  1 42  ? 40.382  229.164 59.491  1.00 42.50  ? 41  GLY I N   1 
ATOM   9053  C  CA  . GLY I  1 42  ? 41.114  229.681 58.296  1.00 39.03  ? 41  GLY I CA  1 
ATOM   9054  C  C   . GLY I  1 42  ? 41.201  228.740 57.108  1.00 37.42  ? 41  GLY I C   1 
ATOM   9055  O  O   . GLY I  1 42  ? 40.448  227.733 57.009  1.00 42.17  ? 41  GLY I O   1 
ATOM   9056  N  N   . LEU I  1 43  ? 42.108  229.046 56.194  1.00 37.64  ? 42  LEU I N   1 
ATOM   9057  C  CA  . LEU I  1 43  ? 42.144  228.279 54.943  1.00 40.58  ? 42  LEU I CA  1 
ATOM   9058  C  C   . LEU I  1 43  ? 42.947  226.998 55.114  1.00 41.12  ? 42  LEU I C   1 
ATOM   9059  O  O   . LEU I  1 43  ? 43.923  226.952 55.887  1.00 44.33  ? 42  LEU I O   1 
ATOM   9060  C  CB  . LEU I  1 43  ? 42.593  229.107 53.722  1.00 39.34  ? 42  LEU I CB  1 
ATOM   9061  C  CG  . LEU I  1 43  ? 42.207  230.577 53.621  1.00 39.02  ? 42  LEU I CG  1 
ATOM   9062  C  CD1 . LEU I  1 43  ? 42.502  231.103 52.241  1.00 35.14  ? 42  LEU I CD1 1 
ATOM   9063  C  CD2 . LEU I  1 43  ? 40.814  230.919 54.100  1.00 34.81  ? 42  LEU I CD2 1 
ATOM   9064  N  N   . HIS I  1 44  ? 42.504  225.940 54.458  1.00 39.83  ? 43  HIS I N   1 
ATOM   9065  C  CA  . HIS I  1 44  ? 43.260  224.702 54.491  1.00 38.66  ? 43  HIS I CA  1 
ATOM   9066  C  C   . HIS I  1 44  ? 43.229  224.183 53.071  1.00 41.52  ? 43  HIS I C   1 
ATOM   9067  O  O   . HIS I  1 44  ? 42.147  224.177 52.455  1.00 40.85  ? 43  HIS I O   1 
ATOM   9068  C  CB  . HIS I  1 44  ? 42.567  223.721 55.412  1.00 36.26  ? 43  HIS I CB  1 
ATOM   9069  C  CG  . HIS I  1 44  ? 42.627  224.107 56.852  1.00 37.66  ? 43  HIS I CG  1 
ATOM   9070  N  ND1 . HIS I  1 44  ? 43.592  223.627 57.721  1.00 40.38  ? 43  HIS I ND1 1 
ATOM   9071  C  CD2 . HIS I  1 44  ? 41.848  224.932 57.581  1.00 37.42  ? 43  HIS I CD2 1 
ATOM   9072  C  CE1 . HIS I  1 44  ? 43.391  224.123 58.928  1.00 38.34  ? 43  HIS I CE1 1 
ATOM   9073  N  NE2 . HIS I  1 44  ? 42.339  224.922 58.868  1.00 39.01  ? 43  HIS I NE2 1 
ATOM   9074  N  N   . GLY I  1 45  ? 44.382  223.762 52.526  1.00 40.50  ? 44  GLY I N   1 
ATOM   9075  C  CA  . GLY I  1 45  ? 44.419  223.065 51.210  1.00 37.74  ? 44  GLY I CA  1 
ATOM   9076  C  C   . GLY I  1 45  ? 43.559  221.810 51.133  1.00 37.99  ? 44  GLY I C   1 
ATOM   9077  O  O   . GLY I  1 45  ? 43.356  221.091 52.112  1.00 41.69  ? 44  GLY I O   1 
ATOM   9078  N  N   . PHE I  1 46  ? 43.061  221.530 49.956  1.00 38.47  ? 45  PHE I N   1 
ATOM   9079  C  CA  . PHE I  1 46  ? 42.076  220.504 49.806  1.00 40.09  ? 45  PHE I CA  1 
ATOM   9080  C  C   . PHE I  1 46  ? 42.428  219.973 48.464  1.00 42.61  ? 45  PHE I C   1 
ATOM   9081  O  O   . PHE I  1 46  ? 42.119  220.611 47.438  1.00 43.91  ? 45  PHE I O   1 
ATOM   9082  C  CB  . PHE I  1 46  ? 40.746  221.199 49.704  1.00 40.29  ? 45  PHE I CB  1 
ATOM   9083  C  CG  . PHE I  1 46  ? 39.562  220.304 49.807  1.00 39.49  ? 45  PHE I CG  1 
ATOM   9084  C  CD1 . PHE I  1 46  ? 39.293  219.644 50.995  1.00 38.25  ? 45  PHE I CD1 1 
ATOM   9085  C  CD2 . PHE I  1 46  ? 38.652  220.203 48.746  1.00 41.29  ? 45  PHE I CD2 1 
ATOM   9086  C  CE1 . PHE I  1 46  ? 38.164  218.868 51.131  1.00 40.70  ? 45  PHE I CE1 1 
ATOM   9087  C  CE2 . PHE I  1 46  ? 37.502  219.421 48.860  1.00 42.74  ? 45  PHE I CE2 1 
ATOM   9088  C  CZ  . PHE I  1 46  ? 37.264  218.745 50.063  1.00 44.86  ? 45  PHE I CZ  1 
ATOM   9089  N  N   . HIS I  1 47  ? 43.163  218.866 48.465  1.00 45.04  ? 46  HIS I N   1 
ATOM   9090  C  CA  . HIS I  1 47  ? 43.595  218.228 47.193  1.00 48.65  ? 46  HIS I CA  1 
ATOM   9091  C  C   . HIS I  1 47  ? 43.249  216.723 47.063  1.00 50.67  ? 46  HIS I C   1 
ATOM   9092  O  O   . HIS I  1 47  ? 43.178  215.951 48.068  1.00 49.49  ? 46  HIS I O   1 
ATOM   9093  C  CB  . HIS I  1 47  ? 45.105  218.474 46.914  1.00 45.48  ? 46  HIS I CB  1 
ATOM   9094  C  CG  . HIS I  1 47  ? 45.573  219.818 47.345  1.00 47.23  ? 46  HIS I CG  1 
ATOM   9095  N  ND1 . HIS I  1 47  ? 46.376  219.998 48.449  1.00 50.46  ? 46  HIS I ND1 1 
ATOM   9096  C  CD2 . HIS I  1 47  ? 45.290  221.060 46.874  1.00 50.48  ? 46  HIS I CD2 1 
ATOM   9097  C  CE1 . HIS I  1 47  ? 46.600  221.294 48.626  1.00 49.41  ? 46  HIS I CE1 1 
ATOM   9098  N  NE2 . HIS I  1 47  ? 45.939  221.962 47.693  1.00 49.83  ? 46  HIS I NE2 1 
ATOM   9099  N  N   . VAL I  1 48  ? 43.006  216.321 45.821  1.00 46.23  ? 47  VAL I N   1 
ATOM   9100  C  CA  . VAL I  1 48  ? 42.970  214.901 45.497  1.00 45.01  ? 47  VAL I CA  1 
ATOM   9101  C  C   . VAL I  1 48  ? 44.447  214.444 45.264  1.00 49.42  ? 47  VAL I C   1 
ATOM   9102  O  O   . VAL I  1 48  ? 45.161  214.936 44.357  1.00 43.53  ? 47  VAL I O   1 
ATOM   9103  C  CB  . VAL I  1 48  ? 42.081  214.610 44.242  1.00 41.31  ? 47  VAL I CB  1 
ATOM   9104  C  CG1 . VAL I  1 48  ? 42.204  213.140 43.881  1.00 38.63  ? 47  VAL I CG1 1 
ATOM   9105  C  CG2 . VAL I  1 48  ? 40.602  215.005 44.433  1.00 33.88  ? 47  VAL I CG2 1 
ATOM   9106  N  N   . HIS I  1 49  ? 44.922  213.527 46.091  1.00 50.12  ? 48  HIS I N   1 
ATOM   9107  C  CA  . HIS I  1 49  ? 46.257  212.949 45.861  1.00 46.75  ? 48  HIS I CA  1 
ATOM   9108  C  C   . HIS I  1 49  ? 46.213  211.691 44.978  1.00 51.49  ? 48  HIS I C   1 
ATOM   9109  O  O   . HIS I  1 49  ? 45.110  211.128 44.714  1.00 49.35  ? 48  HIS I O   1 
ATOM   9110  C  CB  . HIS I  1 49  ? 46.916  212.677 47.200  1.00 47.61  ? 48  HIS I CB  1 
ATOM   9111  C  CG  . HIS I  1 49  ? 47.260  213.929 47.952  1.00 49.44  ? 48  HIS I CG  1 
ATOM   9112  N  ND1 . HIS I  1 49  ? 48.554  214.286 48.261  1.00 50.81  ? 48  HIS I ND1 1 
ATOM   9113  C  CD2 . HIS I  1 49  ? 46.479  214.912 48.453  1.00 49.93  ? 48  HIS I CD2 1 
ATOM   9114  C  CE1 . HIS I  1 49  ? 48.560  215.425 48.933  1.00 47.23  ? 48  HIS I CE1 1 
ATOM   9115  N  NE2 . HIS I  1 49  ? 47.312  215.833 49.054  1.00 48.39  ? 48  HIS I NE2 1 
ATOM   9116  N  N   . GLU I  1 50  ? 47.389  211.230 44.520  1.00 50.63  ? 49  GLU I N   1 
ATOM   9117  C  CA  . GLU I  1 50  ? 47.419  210.125 43.538  1.00 53.17  ? 49  GLU I CA  1 
ATOM   9118  C  C   . GLU I  1 50  ? 46.867  208.743 43.956  1.00 50.68  ? 49  GLU I C   1 
ATOM   9119  O  O   . GLU I  1 50  ? 46.126  208.078 43.155  1.00 47.45  ? 49  GLU I O   1 
ATOM   9120  C  CB  . GLU I  1 50  ? 48.788  209.961 42.881  1.00 54.56  ? 49  GLU I CB  1 
ATOM   9121  C  CG  . GLU I  1 50  ? 48.613  209.271 41.540  1.00 52.83  ? 49  GLU I CG  1 
ATOM   9122  C  CD  . GLU I  1 50  ? 49.886  209.149 40.743  1.00 58.06  ? 49  GLU I CD  1 
ATOM   9123  O  OE1 . GLU I  1 50  ? 50.983  209.388 41.350  1.00 55.11  ? 49  GLU I OE1 1 
ATOM   9124  O  OE2 . GLU I  1 50  ? 49.752  208.816 39.511  1.00 52.60  ? 49  GLU I OE2 1 
ATOM   9125  N  N   . PHE I  1 51  ? 47.247  208.323 45.166  1.00 45.64  ? 50  PHE I N   1 
ATOM   9126  C  CA  . PHE I  1 51  ? 46.971  206.959 45.625  1.00 48.86  ? 50  PHE I CA  1 
ATOM   9127  C  C   . PHE I  1 51  ? 45.896  206.863 46.692  1.00 54.30  ? 50  PHE I C   1 
ATOM   9128  O  O   . PHE I  1 51  ? 45.819  207.697 47.629  1.00 54.43  ? 50  PHE I O   1 
ATOM   9129  C  CB  . PHE I  1 51  ? 48.273  206.198 46.036  1.00 44.79  ? 50  PHE I CB  1 
ATOM   9130  C  CG  . PHE I  1 51  ? 49.378  206.363 45.026  1.00 46.18  ? 50  PHE I CG  1 
ATOM   9131  C  CD1 . PHE I  1 51  ? 49.224  205.910 43.709  1.00 46.09  ? 50  PHE I CD1 1 
ATOM   9132  C  CD2 . PHE I  1 51  ? 50.550  207.068 45.361  1.00 49.61  ? 50  PHE I CD2 1 
ATOM   9133  C  CE1 . PHE I  1 51  ? 50.209  206.140 42.742  1.00 48.00  ? 50  PHE I CE1 1 
ATOM   9134  C  CE2 . PHE I  1 51  ? 51.550  207.276 44.413  1.00 46.47  ? 50  PHE I CE2 1 
ATOM   9135  C  CZ  . PHE I  1 51  ? 51.375  206.813 43.100  1.00 46.65  ? 50  PHE I CZ  1 
ATOM   9136  N  N   . GLY I  1 52  ? 45.069  205.827 46.517  1.00 53.89  ? 51  GLY I N   1 
ATOM   9137  C  CA  . GLY I  1 52  ? 44.117  205.418 47.505  1.00 53.82  ? 51  GLY I CA  1 
ATOM   9138  C  C   . GLY I  1 52  ? 44.793  204.493 48.505  1.00 54.49  ? 51  GLY I C   1 
ATOM   9139  O  O   . GLY I  1 52  ? 44.257  203.415 48.831  1.00 56.79  ? 51  GLY I O   1 
ATOM   9140  N  N   . ASP I  1 53  ? 45.927  204.932 49.029  1.00 47.22  ? 52  ASP I N   1 
ATOM   9141  C  CA  . ASP I  1 53  ? 46.721  204.101 49.846  1.00 49.71  ? 52  ASP I CA  1 
ATOM   9142  C  C   . ASP I  1 53  ? 46.830  204.763 51.186  1.00 49.67  ? 52  ASP I C   1 
ATOM   9143  O  O   . ASP I  1 53  ? 47.427  205.857 51.345  1.00 53.02  ? 52  ASP I O   1 
ATOM   9144  C  CB  . ASP I  1 53  ? 48.084  203.902 49.173  1.00 48.73  ? 52  ASP I CB  1 
ATOM   9145  C  CG  . ASP I  1 53  ? 49.028  202.989 49.963  1.00 50.79  ? 52  ASP I CG  1 
ATOM   9146  O  OD1 . ASP I  1 53  ? 49.090  202.943 51.270  1.00 49.01  ? 52  ASP I OD1 1 
ATOM   9147  O  OD2 . ASP I  1 53  ? 49.743  202.320 49.203  1.00 49.72  ? 52  ASP I OD2 1 
ATOM   9148  N  N   . ASN I  1 54  ? 46.323  204.065 52.174  1.00 44.59  ? 53  ASN I N   1 
ATOM   9149  C  CA  . ASN I  1 54  ? 46.276  204.649 53.481  1.00 47.77  ? 53  ASN I CA  1 
ATOM   9150  C  C   . ASN I  1 54  ? 47.027  203.751 54.454  1.00 48.85  ? 53  ASN I C   1 
ATOM   9151  O  O   . ASN I  1 54  ? 46.773  203.774 55.676  1.00 47.16  ? 53  ASN I O   1 
ATOM   9152  C  CB  . ASN I  1 54  ? 44.802  204.818 53.874  1.00 57.65  ? 53  ASN I CB  1 
ATOM   9153  C  CG  . ASN I  1 54  ? 44.604  205.476 55.269  1.00 72.08  ? 53  ASN I CG  1 
ATOM   9154  O  OD1 . ASN I  1 54  ? 44.643  206.723 55.377  1.00 72.47  ? 53  ASN I OD1 1 
ATOM   9155  N  ND2 . ASN I  1 54  ? 44.358  204.641 56.348  1.00 58.69  ? 53  ASN I ND2 1 
ATOM   9156  N  N   . THR I  1 55  ? 47.937  202.931 53.949  1.00 45.05  ? 54  THR I N   1 
ATOM   9157  C  CA  . THR I  1 55  ? 48.614  201.955 54.870  1.00 45.55  ? 54  THR I CA  1 
ATOM   9158  C  C   . THR I  1 55  ? 49.535  202.638 55.897  1.00 47.11  ? 54  THR I C   1 
ATOM   9159  O  O   . THR I  1 55  ? 49.635  202.184 57.022  1.00 49.41  ? 54  THR I O   1 
ATOM   9160  C  CB  . THR I  1 55  ? 49.384  200.952 54.051  1.00 44.99  ? 54  THR I CB  1 
ATOM   9161  O  OG1 . THR I  1 55  ? 50.019  201.673 52.982  1.00 43.23  ? 54  THR I OG1 1 
ATOM   9162  C  CG2 . THR I  1 55  ? 48.397  199.974 53.393  1.00 42.10  ? 54  THR I CG2 1 
ATOM   9163  N  N   . ALA I  1 56  ? 50.135  203.781 55.542  1.00 53.68  ? 55  ALA I N   1 
ATOM   9164  C  CA  . ALA I  1 56  ? 50.926  204.628 56.493  1.00 57.20  ? 55  ALA I CA  1 
ATOM   9165  C  C   . ALA I  1 56  ? 50.272  206.036 56.725  1.00 61.21  ? 55  ALA I C   1 
ATOM   9166  O  O   . ALA I  1 56  ? 50.954  207.101 56.601  1.00 58.13  ? 55  ALA I O   1 
ATOM   9167  C  CB  . ALA I  1 56  ? 52.348  204.786 55.932  1.00 59.47  ? 55  ALA I CB  1 
ATOM   9168  N  N   . GLY I  1 57  ? 48.955  206.028 57.019  1.00 60.85  ? 56  GLY I N   1 
ATOM   9169  C  CA  . GLY I  1 57  ? 48.110  207.231 57.109  1.00 53.79  ? 56  GLY I CA  1 
ATOM   9170  C  C   . GLY I  1 57  ? 48.093  207.924 55.734  1.00 59.90  ? 56  GLY I C   1 
ATOM   9171  O  O   . GLY I  1 57  ? 48.060  207.260 54.681  1.00 59.88  ? 56  GLY I O   1 
ATOM   9172  N  N   . CYS I  1 58  ? 48.207  209.251 55.740  1.00 57.52  ? 57  CYS I N   1 
ATOM   9173  C  CA  . CYS I  1 58  ? 47.967  210.089 54.538  1.00 56.17  ? 57  CYS I CA  1 
ATOM   9174  C  C   . CYS I  1 58  ? 49.193  210.242 53.636  1.00 52.36  ? 57  CYS I C   1 
ATOM   9175  O  O   . CYS I  1 58  ? 49.063  210.596 52.450  1.00 47.85  ? 57  CYS I O   1 
ATOM   9176  C  CB  . CYS I  1 58  ? 47.353  211.477 54.982  1.00 63.61  ? 57  CYS I CB  1 
ATOM   9177  S  SG  . CYS I  1 58  ? 45.776  211.383 55.984  1.00 55.47  ? 57  CYS I SG  1 
ATOM   9178  N  N   . THR I  1 59  ? 50.387  209.971 54.204  1.00 61.42  ? 58  THR I N   1 
ATOM   9179  C  CA  . THR I  1 59  ? 51.725  210.018 53.482  1.00 52.95  ? 58  THR I CA  1 
ATOM   9180  C  C   . THR I  1 59  ? 51.699  209.118 52.275  1.00 50.91  ? 58  THR I C   1 
ATOM   9181  O  O   . THR I  1 59  ? 52.172  209.479 51.192  1.00 52.69  ? 58  THR I O   1 
ATOM   9182  C  CB  . THR I  1 59  ? 52.849  209.439 54.323  1.00 52.66  ? 58  THR I CB  1 
ATOM   9183  O  OG1 . THR I  1 59  ? 52.661  209.818 55.688  1.00 58.60  ? 58  THR I OG1 1 
ATOM   9184  C  CG2 . THR I  1 59  ? 54.191  209.944 53.841  1.00 53.63  ? 58  THR I CG2 1 
ATOM   9185  N  N   . SER I  1 60  ? 51.060  207.967 52.444  1.00 52.33  ? 59  SER I N   1 
ATOM   9186  C  CA  . SER I  1 60  ? 51.068  206.933 51.411  1.00 51.75  ? 59  SER I CA  1 
ATOM   9187  C  C   . SER I  1 60  ? 50.191  207.280 50.197  1.00 53.64  ? 59  SER I C   1 
ATOM   9188  O  O   . SER I  1 60  ? 50.213  206.517 49.179  1.00 53.39  ? 59  SER I O   1 
ATOM   9189  C  CB  . SER I  1 60  ? 50.698  205.575 52.020  1.00 48.99  ? 59  SER I CB  1 
ATOM   9190  O  OG  . SER I  1 60  ? 50.652  205.623 53.445  1.00 45.44  ? 59  SER I OG  1 
ATOM   9191  N  N   . ALA I  1 61  ? 49.456  208.412 50.267  1.00 48.10  ? 60  ALA I N   1 
ATOM   9192  C  CA  . ALA I  1 61  ? 48.547  208.824 49.151  1.00 47.49  ? 60  ALA I CA  1 
ATOM   9193  C  C   . ALA I  1 61  ? 49.326  209.471 48.009  1.00 49.82  ? 60  ALA I C   1 
ATOM   9194  O  O   . ALA I  1 61  ? 48.810  209.606 46.858  1.00 46.96  ? 60  ALA I O   1 
ATOM   9195  C  CB  . ALA I  1 61  ? 47.481  209.771 49.642  1.00 46.76  ? 60  ALA I CB  1 
ATOM   9196  N  N   . GLY I  1 62  ? 50.585  209.836 48.326  1.00 48.65  ? 61  GLY I N   1 
ATOM   9197  C  CA  . GLY I  1 62  ? 51.499  210.414 47.344  1.00 52.14  ? 61  GLY I CA  1 
ATOM   9198  C  C   . GLY I  1 62  ? 51.211  211.907 47.183  1.00 53.48  ? 61  GLY I C   1 
ATOM   9199  O  O   . GLY I  1 62  ? 50.845  212.558 48.166  1.00 49.62  ? 61  GLY I O   1 
ATOM   9200  N  N   . PRO I  1 63  ? 51.417  212.445 45.967  1.00 49.62  ? 62  PRO I N   1 
ATOM   9201  C  CA  . PRO I  1 63  ? 51.321  213.871 45.607  1.00 51.65  ? 62  PRO I CA  1 
ATOM   9202  C  C   . PRO I  1 63  ? 49.991  214.185 44.935  1.00 49.62  ? 62  PRO I C   1 
ATOM   9203  O  O   . PRO I  1 63  ? 49.143  213.309 44.728  1.00 49.00  ? 62  PRO I O   1 
ATOM   9204  C  CB  . PRO I  1 63  ? 52.478  214.045 44.568  1.00 46.98  ? 62  PRO I CB  1 
ATOM   9205  C  CG  . PRO I  1 63  ? 52.483  212.722 43.849  1.00 48.64  ? 62  PRO I CG  1 
ATOM   9206  C  CD  . PRO I  1 63  ? 52.026  211.654 44.858  1.00 54.22  ? 62  PRO I CD  1 
ATOM   9207  N  N   . HIS I  1 64  ? 49.824  215.432 44.542  1.00 48.98  ? 63  HIS I N   1 
ATOM   9208  C  CA  . HIS I  1 64  ? 48.554  215.848 43.976  1.00 48.01  ? 63  HIS I CA  1 
ATOM   9209  C  C   . HIS I  1 64  ? 48.277  214.932 42.741  1.00 47.52  ? 63  HIS I C   1 
ATOM   9210  O  O   . HIS I  1 64  ? 49.178  214.655 41.967  1.00 55.33  ? 63  HIS I O   1 
ATOM   9211  C  CB  . HIS I  1 64  ? 48.554  217.404 43.802  1.00 46.47  ? 63  HIS I CB  1 
ATOM   9212  C  CG  . HIS I  1 64  ? 48.727  218.182 45.124  1.00 51.99  ? 63  HIS I CG  1 
ATOM   9213  N  ND1 . HIS I  1 64  ? 48.749  219.565 45.204  1.00 49.46  ? 63  HIS I ND1 1 
ATOM   9214  C  CD2 . HIS I  1 64  ? 48.888  217.759 46.407  1.00 53.36  ? 63  HIS I CD2 1 
ATOM   9215  C  CE1 . HIS I  1 64  ? 48.919  219.956 46.457  1.00 54.65  ? 63  HIS I CE1 1 
ATOM   9216  N  NE2 . HIS I  1 64  ? 49.022  218.877 47.209  1.00 51.72  ? 63  HIS I NE2 1 
ATOM   9217  N  N   . PHE I  1 65  ? 47.097  214.332 42.640  1.00 49.05  ? 64  PHE I N   1 
ATOM   9218  C  CA  . PHE I  1 65  ? 46.745  213.620 41.435  1.00 46.39  ? 64  PHE I CA  1 
ATOM   9219  C  C   . PHE I  1 65  ? 47.083  214.564 40.275  1.00 56.28  ? 64  PHE I C   1 
ATOM   9220  O  O   . PHE I  1 65  ? 46.508  215.670 40.115  1.00 57.66  ? 64  PHE I O   1 
ATOM   9221  C  CB  . PHE I  1 65  ? 45.259  213.242 41.379  1.00 44.30  ? 64  PHE I CB  1 
ATOM   9222  C  CG  . PHE I  1 65  ? 44.842  212.484 40.108  1.00 46.75  ? 64  PHE I CG  1 
ATOM   9223  C  CD1 . PHE I  1 65  ? 45.717  211.546 39.455  1.00 49.58  ? 64  PHE I CD1 1 
ATOM   9224  C  CD2 . PHE I  1 65  ? 43.546  212.630 39.591  1.00 48.55  ? 64  PHE I CD2 1 
ATOM   9225  C  CE1 . PHE I  1 65  ? 45.302  210.843 38.301  1.00 47.76  ? 64  PHE I CE1 1 
ATOM   9226  C  CE2 . PHE I  1 65  ? 43.128  211.930 38.433  1.00 49.99  ? 64  PHE I CE2 1 
ATOM   9227  C  CZ  . PHE I  1 65  ? 44.003  211.042 37.788  1.00 52.66  ? 64  PHE I CZ  1 
ATOM   9228  N  N   . ASN I  1 66  ? 48.030  214.115 39.461  1.00 62.65  ? 65  ASN I N   1 
ATOM   9229  C  CA  . ASN I  1 66  ? 48.565  214.955 38.414  1.00 60.09  ? 65  ASN I CA  1 
ATOM   9230  C  C   . ASN I  1 66  ? 48.725  214.177 37.097  1.00 58.14  ? 65  ASN I C   1 
ATOM   9231  O  O   . ASN I  1 66  ? 49.818  214.189 36.511  1.00 54.75  ? 65  ASN I O   1 
ATOM   9232  C  CB  . ASN I  1 66  ? 49.903  215.575 38.875  1.00 52.82  ? 65  ASN I CB  1 
ATOM   9233  C  CG  . ASN I  1 66  ? 50.399  216.659 37.920  1.00 66.48  ? 65  ASN I CG  1 
ATOM   9234  O  OD1 . ASN I  1 66  ? 49.613  217.242 37.101  1.00 59.31  ? 65  ASN I OD1 1 
ATOM   9235  N  ND2 . ASN I  1 66  ? 51.710  216.939 37.998  1.00 62.13  ? 65  ASN I ND2 1 
ATOM   9236  N  N   . PRO I  1 67  ? 47.643  213.532 36.605  1.00 54.85  ? 66  PRO I N   1 
ATOM   9237  C  CA  . PRO I  1 67  ? 47.767  212.813 35.292  1.00 65.28  ? 66  PRO I CA  1 
ATOM   9238  C  C   . PRO I  1 67  ? 48.435  213.652 34.145  1.00 68.02  ? 66  PRO I C   1 
ATOM   9239  O  O   . PRO I  1 67  ? 49.295  213.124 33.423  1.00 64.25  ? 66  PRO I O   1 
ATOM   9240  C  CB  . PRO I  1 67  ? 46.290  212.491 34.895  1.00 55.08  ? 66  PRO I CB  1 
ATOM   9241  C  CG  . PRO I  1 67  ? 45.513  213.530 35.597  1.00 50.96  ? 66  PRO I CG  1 
ATOM   9242  C  CD  . PRO I  1 67  ? 46.233  213.790 36.931  1.00 52.00  ? 66  PRO I CD  1 
ATOM   9243  N  N   . LEU I  1 68  ? 48.036  214.918 33.973  1.00 64.22  ? 67  LEU I N   1 
ATOM   9244  C  CA  . LEU I  1 68  ? 48.511  215.705 32.828  1.00 62.59  ? 67  LEU I CA  1 
ATOM   9245  C  C   . LEU I  1 68  ? 49.909  216.365 33.002  1.00 65.18  ? 67  LEU I C   1 
ATOM   9246  O  O   . LEU I  1 68  ? 50.316  217.214 32.156  1.00 61.12  ? 67  LEU I O   1 
ATOM   9247  C  CB  . LEU I  1 68  ? 47.452  216.708 32.384  1.00 56.88  ? 67  LEU I CB  1 
ATOM   9248  C  CG  . LEU I  1 68  ? 46.459  216.116 31.384  1.00 67.05  ? 67  LEU I CG  1 
ATOM   9249  C  CD1 . LEU I  1 68  ? 45.204  216.989 31.370  1.00 68.28  ? 67  LEU I CD1 1 
ATOM   9250  C  CD2 . LEU I  1 68  ? 47.034  215.950 29.965  1.00 62.14  ? 67  LEU I CD2 1 
ATOM   9251  N  N   . SER I  1 69  ? 50.641  215.981 34.064  1.00 61.41  ? 68  SER I N   1 
ATOM   9252  C  CA  . SER I  1 69  ? 52.000  216.580 34.368  1.00 71.69  ? 68  SER I CA  1 
ATOM   9253  C  C   . SER I  1 69  ? 52.055  218.139 34.242  1.00 70.82  ? 68  SER I C   1 
ATOM   9254  O  O   . SER I  1 69  ? 52.671  218.702 33.323  1.00 59.53  ? 68  SER I O   1 
ATOM   9255  C  CB  . SER I  1 69  ? 53.136  215.894 33.534  1.00 66.46  ? 68  SER I CB  1 
ATOM   9256  O  OG  . SER I  1 69  ? 53.910  214.988 34.353  1.00 63.87  ? 68  SER I OG  1 
ATOM   9257  N  N   . ARG I  1 70  ? 51.343  218.836 35.132  1.00 74.56  ? 69  ARG I N   1 
ATOM   9258  C  CA  . ARG I  1 70  ? 51.338  220.316 35.108  1.00 60.27  ? 69  ARG I CA  1 
ATOM   9259  C  C   . ARG I  1 70  ? 51.934  220.828 36.428  1.00 58.03  ? 69  ARG I C   1 
ATOM   9260  O  O   . ARG I  1 70  ? 52.437  220.041 37.235  1.00 56.34  ? 69  ARG I O   1 
ATOM   9261  C  CB  . ARG I  1 70  ? 49.970  220.898 34.701  1.00 51.48  ? 69  ARG I CB  1 
ATOM   9262  C  CG  . ARG I  1 70  ? 49.585  220.453 33.294  1.00 56.33  ? 69  ARG I CG  1 
ATOM   9263  C  CD  . ARG I  1 70  ? 48.738  221.471 32.546  1.00 65.36  ? 69  ARG I CD  1 
ATOM   9264  N  NE  . ARG I  1 70  ? 47.488  220.876 31.992  1.00 69.67  ? 69  ARG I NE  1 
ATOM   9265  C  CZ  . ARG I  1 70  ? 46.479  221.534 31.349  1.00 75.77  ? 69  ARG I CZ  1 
ATOM   9266  N  NH1 . ARG I  1 70  ? 46.514  222.863 31.132  1.00 72.56  ? 69  ARG I NH1 1 
ATOM   9267  N  NH2 . ARG I  1 70  ? 45.392  220.859 30.903  1.00 69.77  ? 69  ARG I NH2 1 
ATOM   9268  N  N   . LYS I  1 71  ? 51.965  222.140 36.624  1.00 68.00  ? 70  LYS I N   1 
ATOM   9269  C  CA  . LYS I  1 71  ? 52.376  222.670 37.931  1.00 68.28  ? 70  LYS I CA  1 
ATOM   9270  C  C   . LYS I  1 71  ? 51.132  223.013 38.780  1.00 66.27  ? 70  LYS I C   1 
ATOM   9271  O  O   . LYS I  1 71  ? 49.941  222.960 38.283  1.00 52.67  ? 70  LYS I O   1 
ATOM   9272  C  CB  . LYS I  1 71  ? 53.335  223.845 37.759  1.00 65.50  ? 70  LYS I CB  1 
ATOM   9273  C  CG  . LYS I  1 71  ? 54.271  223.646 36.567  1.00 74.28  ? 70  LYS I CG  1 
ATOM   9274  C  CD  . LYS I  1 71  ? 55.419  222.658 36.855  1.00 85.23  ? 70  LYS I CD  1 
ATOM   9275  C  CE  . LYS I  1 71  ? 56.762  223.251 36.388  1.00 87.34  ? 70  LYS I CE  1 
ATOM   9276  N  NZ  . LYS I  1 71  ? 57.219  224.387 37.279  1.00 80.24  ? 70  LYS I NZ  1 
ATOM   9277  N  N   . HIS I  1 72  ? 51.437  223.325 40.054  1.00 65.76  ? 71  HIS I N   1 
ATOM   9278  C  CA  . HIS I  1 72  ? 50.446  223.693 41.058  1.00 63.08  ? 71  HIS I CA  1 
ATOM   9279  C  C   . HIS I  1 72  ? 49.668  224.947 40.583  1.00 66.08  ? 71  HIS I C   1 
ATOM   9280  O  O   . HIS I  1 72  ? 50.177  225.764 39.731  1.00 62.54  ? 71  HIS I O   1 
ATOM   9281  C  CB  . HIS I  1 72  ? 51.118  223.891 42.421  1.00 58.85  ? 71  HIS I CB  1 
ATOM   9282  C  CG  . HIS I  1 72  ? 50.137  223.982 43.528  1.00 65.86  ? 71  HIS I CG  1 
ATOM   9283  N  ND1 . HIS I  1 72  ? 49.495  222.872 44.037  1.00 65.18  ? 71  HIS I ND1 1 
ATOM   9284  C  CD2 . HIS I  1 72  ? 49.595  225.056 44.150  1.00 60.50  ? 71  HIS I CD2 1 
ATOM   9285  C  CE1 . HIS I  1 72  ? 48.622  223.255 44.955  1.00 70.12  ? 71  HIS I CE1 1 
ATOM   9286  N  NE2 . HIS I  1 72  ? 48.661  224.579 45.037  1.00 67.66  ? 71  HIS I NE2 1 
ATOM   9287  N  N   . GLY I  1 73  ? 48.429  225.063 41.069  1.00 60.30  ? 72  GLY I N   1 
ATOM   9288  C  CA  . GLY I  1 73  ? 47.494  226.165 40.689  1.00 57.43  ? 72  GLY I CA  1 
ATOM   9289  C  C   . GLY I  1 73  ? 46.253  226.102 41.570  1.00 62.28  ? 72  GLY I C   1 
ATOM   9290  O  O   . GLY I  1 73  ? 46.048  225.092 42.332  1.00 61.99  ? 72  GLY I O   1 
ATOM   9291  N  N   . GLY I  1 74  ? 45.422  227.144 41.525  1.00 55.62  ? 73  GLY I N   1 
ATOM   9292  C  CA  . GLY I  1 74  ? 44.099  227.066 42.201  1.00 51.12  ? 73  GLY I CA  1 
ATOM   9293  C  C   . GLY I  1 74  ? 43.142  226.347 41.251  1.00 52.90  ? 73  GLY I C   1 
ATOM   9294  O  O   . GLY I  1 74  ? 43.481  226.126 40.079  1.00 53.86  ? 73  GLY I O   1 
ATOM   9295  N  N   . PRO I  1 75  ? 41.945  225.937 41.739  1.00 57.69  ? 74  PRO I N   1 
ATOM   9296  C  CA  . PRO I  1 75  ? 40.943  225.348 40.815  1.00 54.22  ? 74  PRO I CA  1 
ATOM   9297  C  C   . PRO I  1 75  ? 40.714  226.189 39.550  1.00 55.86  ? 74  PRO I C   1 
ATOM   9298  O  O   . PRO I  1 75  ? 40.539  225.608 38.456  1.00 54.11  ? 74  PRO I O   1 
ATOM   9299  C  CB  . PRO I  1 75  ? 39.632  225.275 41.665  1.00 48.01  ? 74  PRO I CB  1 
ATOM   9300  C  CG  . PRO I  1 75  ? 39.976  225.879 43.019  1.00 48.07  ? 74  PRO I CG  1 
ATOM   9301  C  CD  . PRO I  1 75  ? 41.491  225.830 43.149  1.00 56.15  ? 74  PRO I CD  1 
ATOM   9302  N  N   . LYS I  1 76  ? 40.696  227.528 39.682  1.00 59.20  ? 75  LYS I N   1 
ATOM   9303  C  CA  . LYS I  1 76  ? 40.283  228.417 38.533  1.00 59.66  ? 75  LYS I CA  1 
ATOM   9304  C  C   . LYS I  1 76  ? 41.385  228.544 37.457  1.00 63.50  ? 75  LYS I C   1 
ATOM   9305  O  O   . LYS I  1 76  ? 41.056  228.814 36.269  1.00 61.75  ? 75  LYS I O   1 
ATOM   9306  C  CB  . LYS I  1 76  ? 39.825  229.797 38.993  1.00 55.36  ? 75  LYS I CB  1 
ATOM   9307  C  CG  . LYS I  1 76  ? 38.860  229.757 40.154  1.00 61.30  ? 75  LYS I CG  1 
ATOM   9308  C  CD  . LYS I  1 76  ? 38.800  231.106 40.876  1.00 64.02  ? 75  LYS I CD  1 
ATOM   9309  C  CE  . LYS I  1 76  ? 37.468  231.832 40.563  1.00 64.31  ? 75  LYS I CE  1 
ATOM   9310  N  NZ  . LYS I  1 76  ? 36.940  232.583 41.764  1.00 65.07  ? 75  LYS I NZ  1 
ATOM   9311  N  N   . ASP I  1 77  ? 42.657  228.312 37.856  1.00 51.99  ? 76  ASP I N   1 
ATOM   9312  C  CA  . ASP I  1 77  ? 43.795  228.237 36.925  1.00 51.33  ? 76  ASP I CA  1 
ATOM   9313  C  C   . ASP I  1 77  ? 43.684  227.153 35.820  1.00 56.40  ? 76  ASP I C   1 
ATOM   9314  O  O   . ASP I  1 77  ? 43.108  226.046 36.018  1.00 52.72  ? 76  ASP I O   1 
ATOM   9315  C  CB  . ASP I  1 77  ? 45.089  228.033 37.721  1.00 52.17  ? 76  ASP I CB  1 
ATOM   9316  C  CG  . ASP I  1 77  ? 45.293  229.114 38.812  1.00 61.73  ? 76  ASP I CG  1 
ATOM   9317  O  OD1 . ASP I  1 77  ? 44.658  230.207 38.700  1.00 60.15  ? 76  ASP I OD1 1 
ATOM   9318  O  OD2 . ASP I  1 77  ? 46.086  228.887 39.783  1.00 59.92  ? 76  ASP I OD2 1 
ATOM   9319  N  N   . GLU I  1 78  ? 44.222  227.488 34.647  1.00 60.18  ? 77  GLU I N   1 
ATOM   9320  C  CA  . GLU I  1 78  ? 44.478  226.487 33.590  1.00 67.00  ? 77  GLU I CA  1 
ATOM   9321  C  C   . GLU I  1 78  ? 45.662  225.616 34.034  1.00 64.79  ? 77  GLU I C   1 
ATOM   9322  O  O   . GLU I  1 78  ? 45.535  224.376 34.137  1.00 66.42  ? 77  GLU I O   1 
ATOM   9323  C  CB  . GLU I  1 78  ? 44.775  227.159 32.229  1.00 73.45  ? 77  GLU I CB  1 
ATOM   9324  C  CG  . GLU I  1 78  ? 44.756  226.193 31.022  1.00 89.55  ? 77  GLU I CG  1 
ATOM   9325  C  CD  . GLU I  1 78  ? 43.329  225.902 30.469  1.00 91.91  ? 77  GLU I CD  1 
ATOM   9326  O  OE1 . GLU I  1 78  ? 42.656  226.904 30.042  1.00 77.82  ? 77  GLU I OE1 1 
ATOM   9327  O  OE2 . GLU I  1 78  ? 42.882  224.690 30.433  1.00 76.66  ? 77  GLU I OE2 1 
ATOM   9328  N  N   . GLU I  1 79  ? 46.795  226.268 34.335  1.00 60.88  ? 78  GLU I N   1 
ATOM   9329  C  CA  . GLU I  1 79  ? 47.971  225.545 34.831  1.00 59.30  ? 78  GLU I CA  1 
ATOM   9330  C  C   . GLU I  1 79  ? 47.789  225.119 36.344  1.00 63.89  ? 78  GLU I C   1 
ATOM   9331  O  O   . GLU I  1 79  ? 48.181  225.863 37.277  1.00 68.49  ? 78  GLU I O   1 
ATOM   9332  C  CB  . GLU I  1 79  ? 49.207  226.402 34.572  1.00 55.10  ? 78  GLU I CB  1 
ATOM   9333  C  CG  . GLU I  1 79  ? 50.546  225.801 34.994  1.00 65.07  ? 78  GLU I CG  1 
ATOM   9334  C  CD  . GLU I  1 79  ? 50.997  224.633 34.083  1.00 81.94  ? 78  GLU I CD  1 
ATOM   9335  O  OE1 . GLU I  1 79  ? 51.950  223.899 34.517  1.00 63.23  ? 78  GLU I OE1 1 
ATOM   9336  O  OE2 . GLU I  1 79  ? 50.409  224.452 32.945  1.00 75.86  ? 78  GLU I OE2 1 
ATOM   9337  N  N   . ARG I  1 80  ? 47.176  223.940 36.544  1.00 58.88  ? 79  ARG I N   1 
ATOM   9338  C  CA  . ARG I  1 80  ? 46.904  223.281 37.851  1.00 55.74  ? 79  ARG I CA  1 
ATOM   9339  C  C   . ARG I  1 80  ? 47.023  221.720 37.657  1.00 57.79  ? 79  ARG I C   1 
ATOM   9340  O  O   . ARG I  1 80  ? 46.843  221.191 36.517  1.00 59.45  ? 79  ARG I O   1 
ATOM   9341  C  CB  . ARG I  1 80  ? 45.453  223.620 38.276  1.00 53.11  ? 79  ARG I CB  1 
ATOM   9342  C  CG  . ARG I  1 80  ? 44.438  223.256 37.162  1.00 52.62  ? 79  ARG I CG  1 
ATOM   9343  C  CD  . ARG I  1 80  ? 42.957  223.281 37.568  1.00 54.27  ? 79  ARG I CD  1 
ATOM   9344  N  NE  . ARG I  1 80  ? 42.585  222.179 38.474  1.00 53.68  ? 79  ARG I NE  1 
ATOM   9345  C  CZ  . ARG I  1 80  ? 41.353  221.950 38.945  1.00 57.11  ? 79  ARG I CZ  1 
ATOM   9346  N  NH1 . ARG I  1 80  ? 40.324  222.753 38.620  1.00 56.63  ? 79  ARG I NH1 1 
ATOM   9347  N  NH2 . ARG I  1 80  ? 41.140  220.909 39.756  1.00 53.21  ? 79  ARG I NH2 1 
ATOM   9348  N  N   . HIS I  1 81  ? 47.233  221.002 38.766  1.00 54.53  ? 80  HIS I N   1 
ATOM   9349  C  CA  . HIS I  1 81  ? 47.090  219.521 38.876  1.00 50.25  ? 80  HIS I CA  1 
ATOM   9350  C  C   . HIS I  1 81  ? 45.615  219.130 38.722  1.00 56.74  ? 80  HIS I C   1 
ATOM   9351  O  O   . HIS I  1 81  ? 44.743  220.037 38.706  1.00 66.18  ? 80  HIS I O   1 
ATOM   9352  C  CB  . HIS I  1 81  ? 47.661  219.072 40.225  1.00 47.73  ? 80  HIS I CB  1 
ATOM   9353  C  CG  . HIS I  1 81  ? 49.131  219.385 40.381  1.00 52.55  ? 80  HIS I CG  1 
ATOM   9354  N  ND1 . HIS I  1 81  ? 49.757  219.511 41.606  1.00 52.28  ? 80  HIS I ND1 1 
ATOM   9355  C  CD2 . HIS I  1 81  ? 50.109  219.574 39.448  1.00 51.56  ? 80  HIS I CD2 1 
ATOM   9356  C  CE1 . HIS I  1 81  ? 51.044  219.786 41.428  1.00 53.38  ? 80  HIS I CE1 1 
ATOM   9357  N  NE2 . HIS I  1 81  ? 51.286  219.807 40.127  1.00 53.62  ? 80  HIS I NE2 1 
ATOM   9358  N  N   . VAL I  1 82  ? 45.279  217.840 38.554  1.00 53.62  ? 81  VAL I N   1 
ATOM   9359  C  CA  . VAL I  1 82  ? 43.845  217.511 38.416  1.00 48.90  ? 81  VAL I CA  1 
ATOM   9360  C  C   . VAL I  1 82  ? 43.262  217.579 39.821  1.00 50.24  ? 81  VAL I C   1 
ATOM   9361  O  O   . VAL I  1 82  ? 42.111  217.967 40.013  1.00 44.06  ? 81  VAL I O   1 
ATOM   9362  C  CB  . VAL I  1 82  ? 43.531  216.190 37.675  1.00 47.92  ? 81  VAL I CB  1 
ATOM   9363  C  CG1 . VAL I  1 82  ? 42.034  215.842 37.845  1.00 46.82  ? 81  VAL I CG1 1 
ATOM   9364  C  CG2 . VAL I  1 82  ? 43.849  216.340 36.180  1.00 42.64  ? 81  VAL I CG2 1 
ATOM   9365  N  N   . GLY I  1 83  ? 44.121  217.275 40.797  1.00 49.63  ? 82  GLY I N   1 
ATOM   9366  C  CA  . GLY I  1 83  ? 43.706  217.252 42.163  1.00 51.47  ? 82  GLY I CA  1 
ATOM   9367  C  C   . GLY I  1 83  ? 43.598  218.588 42.885  1.00 51.62  ? 82  GLY I C   1 
ATOM   9368  O  O   . GLY I  1 83  ? 43.591  218.573 44.120  1.00 52.79  ? 82  GLY I O   1 
ATOM   9369  N  N   . ASP I  1 84  ? 43.480  219.722 42.165  1.00 51.88  ? 83  ASP I N   1 
ATOM   9370  C  CA  . ASP I  1 84  ? 43.705  221.100 42.771  1.00 49.45  ? 83  ASP I CA  1 
ATOM   9371  C  C   . ASP I  1 84  ? 42.389  221.769 43.100  1.00 52.17  ? 83  ASP I C   1 
ATOM   9372  O  O   . ASP I  1 84  ? 41.701  222.321 42.206  1.00 53.90  ? 83  ASP I O   1 
ATOM   9373  C  CB  . ASP I  1 84  ? 44.624  222.018 41.909  1.00 48.78  ? 83  ASP I CB  1 
ATOM   9374  C  CG  . ASP I  1 84  ? 46.097  221.581 41.949  1.00 57.62  ? 83  ASP I CG  1 
ATOM   9375  O  OD1 . ASP I  1 84  ? 46.299  220.472 42.527  1.00 59.35  ? 83  ASP I OD1 1 
ATOM   9376  O  OD2 . ASP I  1 84  ? 47.041  222.268 41.423  1.00 54.57  ? 83  ASP I OD2 1 
ATOM   9377  N  N   . LEU I  1 85  ? 41.991  221.674 44.365  1.00 48.56  ? 84  LEU I N   1 
ATOM   9378  C  CA  . LEU I  1 85  ? 40.627  222.070 44.675  1.00 49.48  ? 84  LEU I CA  1 
ATOM   9379  C  C   . LEU I  1 85  ? 40.688  223.251 45.649  1.00 50.42  ? 84  LEU I C   1 
ATOM   9380  O  O   . LEU I  1 85  ? 39.730  223.532 46.366  1.00 50.25  ? 84  LEU I O   1 
ATOM   9381  C  CB  . LEU I  1 85  ? 39.867  220.839 45.185  1.00 45.57  ? 84  LEU I CB  1 
ATOM   9382  C  CG  . LEU I  1 85  ? 39.592  219.727 44.161  1.00 47.02  ? 84  LEU I CG  1 
ATOM   9383  C  CD1 . LEU I  1 85  ? 38.741  218.627 44.754  1.00 45.57  ? 84  LEU I CD1 1 
ATOM   9384  C  CD2 . LEU I  1 85  ? 38.851  220.255 42.935  1.00 52.54  ? 84  LEU I CD2 1 
ATOM   9385  N  N   . GLY I  1 86  ? 41.867  223.891 45.661  1.00 49.41  ? 85  GLY I N   1 
ATOM   9386  C  CA  . GLY I  1 86  ? 42.311  224.966 46.569  1.00 45.04  ? 85  GLY I CA  1 
ATOM   9387  C  C   . GLY I  1 86  ? 42.017  224.933 48.058  1.00 50.00  ? 85  GLY I C   1 
ATOM   9388  O  O   . GLY I  1 86  ? 42.529  224.087 48.812  1.00 52.59  ? 85  GLY I O   1 
ATOM   9389  N  N   . ASN I  1 87  ? 41.229  225.889 48.521  1.00 45.24  ? 86  ASN I N   1 
ATOM   9390  C  CA  . ASN I  1 87  ? 41.085  225.989 49.947  1.00 42.73  ? 86  ASN I CA  1 
ATOM   9391  C  C   . ASN I  1 87  ? 39.652  225.740 50.352  1.00 42.76  ? 86  ASN I C   1 
ATOM   9392  O  O   . ASN I  1 87  ? 38.730  226.022 49.588  1.00 40.96  ? 86  ASN I O   1 
ATOM   9393  C  CB  . ASN I  1 87  ? 41.602  227.335 50.450  1.00 41.26  ? 86  ASN I CB  1 
ATOM   9394  C  CG  . ASN I  1 87  ? 43.120  227.481 50.274  1.00 46.25  ? 86  ASN I CG  1 
ATOM   9395  O  OD1 . ASN I  1 87  ? 43.966  226.896 51.027  1.00 42.02  ? 86  ASN I OD1 1 
ATOM   9396  N  ND2 . ASN I  1 87  ? 43.484  228.295 49.280  1.00 46.15  ? 86  ASN I ND2 1 
ATOM   9397  N  N   . VAL I  1 88  ? 39.498  225.096 51.493  1.00 40.76  ? 87  VAL I N   1 
ATOM   9398  C  CA  . VAL I  1 88  ? 38.268  225.095 52.234  1.00 41.89  ? 87  VAL I CA  1 
ATOM   9399  C  C   . VAL I  1 88  ? 38.591  225.979 53.428  1.00 40.38  ? 87  VAL I C   1 
ATOM   9400  O  O   . VAL I  1 88  ? 39.792  226.090 53.820  1.00 37.34  ? 87  VAL I O   1 
ATOM   9401  C  CB  . VAL I  1 88  ? 37.790  223.674 52.657  1.00 42.48  ? 87  VAL I CB  1 
ATOM   9402  C  CG1 . VAL I  1 88  ? 37.599  222.802 51.430  1.00 39.03  ? 87  VAL I CG1 1 
ATOM   9403  C  CG2 . VAL I  1 88  ? 38.713  223.026 53.674  1.00 36.61  ? 87  VAL I CG2 1 
ATOM   9404  N  N   . THR I  1 89  ? 37.530  226.588 53.992  1.00 37.08  ? 88  THR I N   1 
ATOM   9405  C  CA  . THR I  1 89  ? 37.687  227.636 54.997  1.00 38.58  ? 88  THR I CA  1 
ATOM   9406  C  C   . THR I  1 89  ? 37.028  227.258 56.289  1.00 38.23  ? 88  THR I C   1 
ATOM   9407  O  O   . THR I  1 89  ? 35.806  227.082 56.321  1.00 39.58  ? 88  THR I O   1 
ATOM   9408  C  CB  . THR I  1 89  ? 37.220  229.030 54.482  1.00 37.47  ? 88  THR I CB  1 
ATOM   9409  O  OG1 . THR I  1 89  ? 38.041  229.436 53.363  1.00 36.89  ? 88  THR I OG1 1 
ATOM   9410  C  CG2 . THR I  1 89  ? 37.377  230.046 55.544  1.00 34.01  ? 88  THR I CG2 1 
ATOM   9411  N  N   . ALA I  1 90  ? 37.816  227.073 57.344  1.00 34.48  ? 89  ALA I N   1 
ATOM   9412  C  CA  . ALA I  1 90  ? 37.154  226.686 58.563  1.00 37.30  ? 89  ALA I CA  1 
ATOM   9413  C  C   . ALA I  1 90  ? 36.771  227.898 59.346  1.00 39.24  ? 89  ALA I C   1 
ATOM   9414  O  O   . ALA I  1 90  ? 37.539  228.831 59.537  1.00 39.03  ? 89  ALA I O   1 
ATOM   9415  C  CB  . ALA I  1 90  ? 37.968  225.722 59.405  1.00 36.79  ? 89  ALA I CB  1 
ATOM   9416  N  N   . ASP I  1 91  ? 35.549  227.874 59.815  1.00 40.54  ? 90  ASP I N   1 
ATOM   9417  C  CA  . ASP I  1 91  ? 35.070  228.923 60.690  1.00 43.62  ? 90  ASP I CA  1 
ATOM   9418  C  C   . ASP I  1 91  ? 35.685  228.968 62.136  1.00 41.75  ? 90  ASP I C   1 
ATOM   9419  O  O   . ASP I  1 91  ? 36.570  228.198 62.476  1.00 39.28  ? 90  ASP I O   1 
ATOM   9420  C  CB  . ASP I  1 91  ? 33.528  228.904 60.656  1.00 43.42  ? 90  ASP I CB  1 
ATOM   9421  C  CG  . ASP I  1 91  ? 32.904  227.864 61.595  1.00 45.63  ? 90  ASP I CG  1 
ATOM   9422  O  OD1 . ASP I  1 91  ? 33.516  227.536 62.632  1.00 46.78  ? 90  ASP I OD1 1 
ATOM   9423  O  OD2 . ASP I  1 91  ? 31.749  227.424 61.322  1.00 48.04  ? 90  ASP I OD2 1 
ATOM   9424  N  N   . LYS I  1 92  ? 35.205  229.879 62.973  1.00 46.97  ? 91  LYS I N   1 
ATOM   9425  C  CA  . LYS I  1 92  ? 35.780  230.136 64.307  1.00 46.30  ? 91  LYS I CA  1 
ATOM   9426  C  C   . LYS I  1 92  ? 35.646  228.849 65.150  1.00 53.18  ? 91  LYS I C   1 
ATOM   9427  O  O   . LYS I  1 92  ? 36.505  228.585 65.985  1.00 54.81  ? 91  LYS I O   1 
ATOM   9428  C  CB  . LYS I  1 92  ? 35.019  231.309 64.964  1.00 47.01  ? 91  LYS I CB  1 
ATOM   9429  C  CG  . LYS I  1 92  ? 35.824  232.235 65.873  1.00 53.91  ? 91  LYS I CG  1 
ATOM   9430  C  CD  . LYS I  1 92  ? 35.327  233.723 65.898  1.00 58.77  ? 91  LYS I CD  1 
ATOM   9431  C  CE  . LYS I  1 92  ? 36.194  234.769 65.137  1.00 55.05  ? 91  LYS I CE  1 
ATOM   9432  N  NZ  . LYS I  1 92  ? 37.703  234.723 65.411  1.00 55.18  ? 91  LYS I NZ  1 
ATOM   9433  N  N   . ASP I  1 93  ? 34.588  228.045 64.934  1.00 47.54  ? 92  ASP I N   1 
ATOM   9434  C  CA  . ASP I  1 93  ? 34.399  226.764 65.673  1.00 47.54  ? 92  ASP I CA  1 
ATOM   9435  C  C   . ASP I  1 93  ? 35.076  225.483 65.107  1.00 46.50  ? 92  ASP I C   1 
ATOM   9436  O  O   . ASP I  1 93  ? 34.807  224.353 65.560  1.00 45.52  ? 92  ASP I O   1 
ATOM   9437  C  CB  . ASP I  1 93  ? 32.902  226.457 65.787  1.00 48.41  ? 92  ASP I CB  1 
ATOM   9438  C  CG  . ASP I  1 93  ? 32.186  227.431 66.649  1.00 53.08  ? 92  ASP I CG  1 
ATOM   9439  O  OD1 . ASP I  1 93  ? 32.697  227.804 67.735  1.00 59.11  ? 92  ASP I OD1 1 
ATOM   9440  O  OD2 . ASP I  1 93  ? 31.091  227.823 66.242  1.00 55.25  ? 92  ASP I OD2 1 
ATOM   9441  N  N   . GLY I  1 94  ? 35.893  225.648 64.096  1.00 41.44  ? 93  GLY I N   1 
ATOM   9442  C  CA  . GLY I  1 94  ? 36.559  224.539 63.502  1.00 42.04  ? 93  GLY I CA  1 
ATOM   9443  C  C   . GLY I  1 94  ? 35.895  223.833 62.366  1.00 42.77  ? 93  GLY I C   1 
ATOM   9444  O  O   . GLY I  1 94  ? 36.465  222.821 61.875  1.00 40.14  ? 93  GLY I O   1 
ATOM   9445  N  N   . VAL I  1 95  ? 34.732  224.360 61.932  1.00 40.34  ? 94  VAL I N   1 
ATOM   9446  C  CA  . VAL I  1 95  ? 33.924  223.714 60.909  1.00 35.41  ? 94  VAL I CA  1 
ATOM   9447  C  C   . VAL I  1 95  ? 34.157  224.336 59.557  1.00 38.17  ? 94  VAL I C   1 
ATOM   9448  O  O   . VAL I  1 95  ? 34.142  225.529 59.406  1.00 41.88  ? 94  VAL I O   1 
ATOM   9449  C  CB  . VAL I  1 95  ? 32.436  223.651 61.307  1.00 35.81  ? 94  VAL I CB  1 
ATOM   9450  C  CG1 . VAL I  1 95  ? 31.616  222.911 60.245  1.00 30.12  ? 94  VAL I CG1 1 
ATOM   9451  C  CG2 . VAL I  1 95  ? 32.293  222.945 62.687  1.00 34.22  ? 94  VAL I CG2 1 
ATOM   9452  N  N   . ALA I  1 96  ? 34.433  223.517 58.562  1.00 41.19  ? 95  ALA I N   1 
ATOM   9453  C  CA  . ALA I  1 96  ? 34.470  224.005 57.179  1.00 43.26  ? 95  ALA I CA  1 
ATOM   9454  C  C   . ALA I  1 96  ? 33.382  223.273 56.371  1.00 45.30  ? 95  ALA I C   1 
ATOM   9455  O  O   . ALA I  1 96  ? 33.445  222.034 56.186  1.00 50.23  ? 95  ALA I O   1 
ATOM   9456  C  CB  . ALA I  1 96  ? 35.831  223.791 56.569  1.00 37.81  ? 95  ALA I CB  1 
ATOM   9457  N  N   . ASP I  1 97  ? 32.368  224.027 55.948  1.00 43.23  ? 96  ASP I N   1 
ATOM   9458  C  CA  . ASP I  1 97  ? 31.354  223.563 55.032  1.00 41.26  ? 96  ASP I CA  1 
ATOM   9459  C  C   . ASP I  1 97  ? 31.895  223.766 53.605  1.00 46.38  ? 96  ASP I C   1 
ATOM   9460  O  O   . ASP I  1 97  ? 32.299  224.874 53.209  1.00 42.19  ? 96  ASP I O   1 
ATOM   9461  C  CB  . ASP I  1 97  ? 30.030  224.289 55.249  1.00 45.68  ? 96  ASP I CB  1 
ATOM   9462  C  CG  . ASP I  1 97  ? 29.369  223.972 56.635  1.00 55.82  ? 96  ASP I CG  1 
ATOM   9463  O  OD1 . ASP I  1 97  ? 29.476  222.843 57.250  1.00 56.44  ? 96  ASP I OD1 1 
ATOM   9464  O  OD2 . ASP I  1 97  ? 28.706  224.904 57.132  1.00 53.27  ? 96  ASP I OD2 1 
ATOM   9465  N  N   . VAL I  1 98  ? 31.884  222.670 52.843  1.00 42.09  ? 97  VAL I N   1 
ATOM   9466  C  CA  . VAL I  1 98  ? 32.532  222.630 51.576  1.00 39.54  ? 97  VAL I CA  1 
ATOM   9467  C  C   . VAL I  1 98  ? 31.450  222.620 50.491  1.00 43.03  ? 97  VAL I C   1 
ATOM   9468  O  O   . VAL I  1 98  ? 30.445  221.862 50.550  1.00 42.75  ? 97  VAL I O   1 
ATOM   9469  C  CB  . VAL I  1 98  ? 33.449  221.369 51.509  1.00 37.59  ? 97  VAL I CB  1 
ATOM   9470  C  CG1 . VAL I  1 98  ? 34.082  221.231 50.125  1.00 34.58  ? 97  VAL I CG1 1 
ATOM   9471  C  CG2 . VAL I  1 98  ? 34.475  221.370 52.651  1.00 30.39  ? 97  VAL I CG2 1 
ATOM   9472  N  N   . SER I  1 99  ? 31.656  223.460 49.487  1.00 44.96  ? 98  SER I N   1 
ATOM   9473  C  CA  . SER I  1 99  ? 30.741  223.529 48.357  1.00 46.22  ? 98  SER I CA  1 
ATOM   9474  C  C   . SER I  1 99  ? 31.488  224.052 47.144  1.00 49.89  ? 98  SER I C   1 
ATOM   9475  O  O   . SER I  1 99  ? 31.865  225.211 47.089  1.00 48.33  ? 98  SER I O   1 
ATOM   9476  C  CB  . SER I  1 99  ? 29.581  224.423 48.700  1.00 43.69  ? 98  SER I CB  1 
ATOM   9477  O  OG  . SER I  1 99  ? 28.622  224.158 47.737  1.00 52.55  ? 98  SER I OG  1 
ATOM   9478  N  N   . ILE I  1 100 ? 31.753  223.165 46.196  1.00 53.91  ? 99  ILE I N   1 
ATOM   9479  C  CA  . ILE I  1 100 ? 32.724  223.398 45.110  1.00 46.47  ? 99  ILE I CA  1 
ATOM   9480  C  C   . ILE I  1 100 ? 32.047  222.770 43.909  1.00 48.31  ? 99  ILE I C   1 
ATOM   9481  O  O   . ILE I  1 100 ? 31.152  221.915 44.055  1.00 43.67  ? 99  ILE I O   1 
ATOM   9482  C  CB  . ILE I  1 100 ? 34.089  222.722 45.426  1.00 50.42  ? 99  ILE I CB  1 
ATOM   9483  C  CG1 . ILE I  1 100 ? 34.727  223.416 46.627  1.00 54.68  ? 99  ILE I CG1 1 
ATOM   9484  C  CG2 . ILE I  1 100 ? 35.079  222.727 44.256  1.00 46.45  ? 99  ILE I CG2 1 
ATOM   9485  C  CD1 . ILE I  1 100 ? 36.075  222.800 46.980  1.00 61.95  ? 99  ILE I CD1 1 
ATOM   9486  N  N   . GLU I  1 101 ? 32.395  223.292 42.735  1.00 51.15  ? 100 GLU I N   1 
ATOM   9487  C  CA  . GLU I  1 101 ? 32.025  222.697 41.464  1.00 49.24  ? 100 GLU I CA  1 
ATOM   9488  C  C   . GLU I  1 101 ? 33.313  222.676 40.721  1.00 56.03  ? 100 GLU I C   1 
ATOM   9489  O  O   . GLU I  1 101 ? 34.047  223.691 40.669  1.00 51.32  ? 100 GLU I O   1 
ATOM   9490  C  CB  . GLU I  1 101 ? 30.995  223.499 40.713  1.00 46.56  ? 100 GLU I CB  1 
ATOM   9491  C  CG  . GLU I  1 101 ? 29.564  223.077 41.066  1.00 59.36  ? 100 GLU I CG  1 
ATOM   9492  C  CD  . GLU I  1 101 ? 28.593  223.037 39.863  1.00 67.73  ? 100 GLU I CD  1 
ATOM   9493  O  OE1 . GLU I  1 101 ? 28.941  223.589 38.743  1.00 63.60  ? 100 GLU I OE1 1 
ATOM   9494  O  OE2 . GLU I  1 101 ? 27.466  222.443 40.048  1.00 61.36  ? 100 GLU I OE2 1 
ATOM   9495  N  N   . ASP I  1 102 ? 33.656  221.499 40.219  1.00 53.66  ? 101 ASP I N   1 
ATOM   9496  C  CA  . ASP I  1 102 ? 34.891  221.422 39.487  1.00 54.78  ? 101 ASP I CA  1 
ATOM   9497  C  C   . ASP I  1 102 ? 34.644  220.789 38.120  1.00 55.38  ? 101 ASP I C   1 
ATOM   9498  O  O   . ASP I  1 102 ? 33.716  219.952 37.958  1.00 51.37  ? 101 ASP I O   1 
ATOM   9499  C  CB  . ASP I  1 102 ? 35.991  220.746 40.283  1.00 48.56  ? 101 ASP I CB  1 
ATOM   9500  C  CG  . ASP I  1 102 ? 37.361  220.965 39.644  1.00 56.53  ? 101 ASP I CG  1 
ATOM   9501  O  OD1 . ASP I  1 102 ? 37.965  222.049 39.775  1.00 56.35  ? 101 ASP I OD1 1 
ATOM   9502  O  OD2 . ASP I  1 102 ? 37.852  220.055 38.962  1.00 63.91  ? 101 ASP I OD2 1 
ATOM   9503  N  N   . SER I  1 103 ? 35.453  221.232 37.154  1.00 54.53  ? 102 SER I N   1 
ATOM   9504  C  CA  . SER I  1 103 ? 35.327  220.744 35.795  1.00 62.21  ? 102 SER I CA  1 
ATOM   9505  C  C   . SER I  1 103 ? 36.447  219.874 35.271  1.00 56.01  ? 102 SER I C   1 
ATOM   9506  O  O   . SER I  1 103 ? 36.319  219.311 34.184  1.00 55.56  ? 102 SER I O   1 
ATOM   9507  C  CB  . SER I  1 103 ? 34.989  221.867 34.833  1.00 59.33  ? 102 SER I CB  1 
ATOM   9508  O  OG  . SER I  1 103 ? 33.611  221.633 34.523  1.00 64.51  ? 102 SER I OG  1 
ATOM   9509  N  N   . VAL I  1 104 ? 37.504  219.754 36.067  1.00 48.01  ? 103 VAL I N   1 
ATOM   9510  C  CA  . VAL I  1 104 ? 38.730  219.051 35.680  1.00 49.79  ? 103 VAL I CA  1 
ATOM   9511  C  C   . VAL I  1 104 ? 38.734  217.623 36.223  1.00 48.06  ? 103 VAL I C   1 
ATOM   9512  O  O   . VAL I  1 104 ? 38.964  216.688 35.486  1.00 49.06  ? 103 VAL I O   1 
ATOM   9513  C  CB  . VAL I  1 104 ? 39.950  219.827 36.205  1.00 51.73  ? 103 VAL I CB  1 
ATOM   9514  C  CG1 . VAL I  1 104 ? 41.237  218.964 36.190  1.00 50.09  ? 103 VAL I CG1 1 
ATOM   9515  C  CG2 . VAL I  1 104 ? 40.044  221.183 35.488  1.00 40.05  ? 103 VAL I CG2 1 
ATOM   9516  N  N   . ILE I  1 105 ? 38.498  217.486 37.525  1.00 51.79  ? 104 ILE I N   1 
ATOM   9517  C  CA  . ILE I  1 105 ? 38.243  216.200 38.191  1.00 47.10  ? 104 ILE I CA  1 
ATOM   9518  C  C   . ILE I  1 105 ? 36.972  215.598 37.527  1.00 53.19  ? 104 ILE I C   1 
ATOM   9519  O  O   . ILE I  1 105 ? 36.098  216.337 36.965  1.00 46.15  ? 104 ILE I O   1 
ATOM   9520  C  CB  . ILE I  1 105 ? 38.119  216.329 39.757  1.00 46.43  ? 104 ILE I CB  1 
ATOM   9521  C  CG1 . ILE I  1 105 ? 36.843  217.080 40.197  1.00 44.50  ? 104 ILE I CG1 1 
ATOM   9522  C  CG2 . ILE I  1 105 ? 39.349  216.978 40.417  1.00 42.90  ? 104 ILE I CG2 1 
ATOM   9523  C  CD1 . ILE I  1 105 ? 36.519  216.878 41.692  1.00 45.16  ? 104 ILE I CD1 1 
ATOM   9524  N  N   . SER I  1 106 ? 36.907  214.250 37.548  1.00 53.48  ? 105 SER I N   1 
ATOM   9525  C  CA  . SER I  1 106 ? 35.756  213.505 37.055  1.00 45.82  ? 105 SER I CA  1 
ATOM   9526  C  C   . SER I  1 106 ? 35.567  212.247 37.880  1.00 48.76  ? 105 SER I C   1 
ATOM   9527  O  O   . SER I  1 106 ? 36.472  211.822 38.621  1.00 49.22  ? 105 SER I O   1 
ATOM   9528  C  CB  . SER I  1 106 ? 35.877  213.158 35.541  1.00 46.01  ? 105 SER I CB  1 
ATOM   9529  O  OG  . SER I  1 106 ? 34.691  212.442 35.134  1.00 47.38  ? 105 SER I OG  1 
ATOM   9530  N  N   . LEU I  1 107 ? 34.399  211.640 37.682  1.00 47.21  ? 106 LEU I N   1 
ATOM   9531  C  CA  . LEU I  1 107 ? 34.013  210.438 38.366  1.00 52.19  ? 106 LEU I CA  1 
ATOM   9532  C  C   . LEU I  1 107 ? 33.996  209.277 37.346  1.00 63.16  ? 106 LEU I C   1 
ATOM   9533  O  O   . LEU I  1 107 ? 33.406  208.164 37.626  1.00 53.92  ? 106 LEU I O   1 
ATOM   9534  C  CB  . LEU I  1 107 ? 32.639  210.610 39.019  1.00 51.13  ? 106 LEU I CB  1 
ATOM   9535  C  CG  . LEU I  1 107 ? 32.465  211.407 40.319  1.00 50.07  ? 106 LEU I CG  1 
ATOM   9536  C  CD1 . LEU I  1 107 ? 31.154  210.906 40.979  1.00 52.55  ? 106 LEU I CD1 1 
ATOM   9537  C  CD2 . LEU I  1 107 ? 33.628  211.230 41.263  1.00 47.28  ? 106 LEU I CD2 1 
ATOM   9538  N  N   . SER I  1 108 ? 34.607  209.549 36.171  1.00 52.25  ? 107 SER I N   1 
ATOM   9539  C  CA  . SER I  1 108 ? 34.950  208.511 35.202  1.00 53.78  ? 107 SER I CA  1 
ATOM   9540  C  C   . SER I  1 108 ? 35.923  209.075 34.136  1.00 60.99  ? 107 SER I C   1 
ATOM   9541  O  O   . SER I  1 108 ? 35.991  210.310 33.921  1.00 64.19  ? 107 SER I O   1 
ATOM   9542  C  CB  . SER I  1 108 ? 33.680  207.975 34.549  1.00 53.20  ? 107 SER I CB  1 
ATOM   9543  O  OG  . SER I  1 108 ? 33.535  208.620 33.308  1.00 58.11  ? 107 SER I OG  1 
ATOM   9544  N  N   . GLY I  1 109 ? 36.667  208.196 33.452  1.00 60.92  ? 108 GLY I N   1 
ATOM   9545  C  CA  . GLY I  1 109 ? 37.606  208.632 32.358  1.00 53.49  ? 108 GLY I CA  1 
ATOM   9546  C  C   . GLY I  1 109 ? 39.028  208.608 32.850  1.00 55.62  ? 108 GLY I C   1 
ATOM   9547  O  O   . GLY I  1 109 ? 39.316  208.037 33.911  1.00 57.42  ? 108 GLY I O   1 
ATOM   9548  N  N   . ASP I  1 110 ? 39.941  209.210 32.102  1.00 60.17  ? 109 ASP I N   1 
ATOM   9549  C  CA  . ASP I  1 110 ? 41.293  209.329 32.631  1.00 63.86  ? 109 ASP I CA  1 
ATOM   9550  C  C   . ASP I  1 110 ? 41.377  210.135 33.966  1.00 73.47  ? 109 ASP I C   1 
ATOM   9551  O  O   . ASP I  1 110 ? 42.104  209.742 34.931  1.00 71.89  ? 109 ASP I O   1 
ATOM   9552  C  CB  . ASP I  1 110 ? 42.257  209.914 31.593  1.00 68.51  ? 109 ASP I CB  1 
ATOM   9553  C  CG  . ASP I  1 110 ? 43.745  210.019 32.155  1.00 78.33  ? 109 ASP I CG  1 
ATOM   9554  O  OD1 . ASP I  1 110 ? 44.075  209.532 33.332  1.00 58.63  ? 109 ASP I OD1 1 
ATOM   9555  O  OD2 . ASP I  1 110 ? 44.591  210.610 31.401  1.00 71.12  ? 109 ASP I OD2 1 
ATOM   9556  N  N   . HIS I  1 111 ? 40.626  211.243 34.029  1.00 71.92  ? 110 HIS I N   1 
ATOM   9557  C  CA  . HIS I  1 111 ? 40.708  212.139 35.194  1.00 70.25  ? 110 HIS I CA  1 
ATOM   9558  C  C   . HIS I  1 111 ? 39.993  211.546 36.440  1.00 69.19  ? 110 HIS I C   1 
ATOM   9559  O  O   . HIS I  1 111 ? 39.946  212.200 37.502  1.00 63.94  ? 110 HIS I O   1 
ATOM   9560  C  CB  . HIS I  1 111 ? 40.143  213.536 34.822  1.00 74.38  ? 110 HIS I CB  1 
ATOM   9561  C  CG  . HIS I  1 111 ? 41.020  214.337 33.888  1.00 81.12  ? 110 HIS I CG  1 
ATOM   9562  N  ND1 . HIS I  1 111 ? 40.734  215.646 33.538  1.00 75.33  ? 110 HIS I ND1 1 
ATOM   9563  C  CD2 . HIS I  1 111 ? 42.169  214.020 33.238  1.00 78.21  ? 110 HIS I CD2 1 
ATOM   9564  C  CE1 . HIS I  1 111 ? 41.668  216.100 32.721  1.00 77.17  ? 110 HIS I CE1 1 
ATOM   9565  N  NE2 . HIS I  1 111 ? 42.548  215.132 32.522  1.00 81.43  ? 110 HIS I NE2 1 
ATOM   9566  N  N   . CYS I  1 112 ? 39.425  210.333 36.312  1.00 60.53  ? 111 CYS I N   1 
ATOM   9567  C  CA  . CYS I  1 112 ? 38.588  209.767 37.369  1.00 55.10  ? 111 CYS I CA  1 
ATOM   9568  C  C   . CYS I  1 112 ? 39.392  209.771 38.695  1.00 50.76  ? 111 CYS I C   1 
ATOM   9569  O  O   . CYS I  1 112 ? 40.601  209.464 38.697  1.00 49.27  ? 111 CYS I O   1 
ATOM   9570  C  CB  . CYS I  1 112 ? 38.102  208.397 36.953  1.00 52.18  ? 111 CYS I CB  1 
ATOM   9571  S  SG  . CYS I  1 112 ? 37.671  207.324 38.328  1.00 54.70  ? 111 CYS I SG  1 
ATOM   9572  N  N   . ILE I  1 113 ? 38.743  210.232 39.770  1.00 44.22  ? 112 ILE I N   1 
ATOM   9573  C  CA  . ILE I  1 113 ? 39.359  210.361 41.098  1.00 43.47  ? 112 ILE I CA  1 
ATOM   9574  C  C   . ILE I  1 113 ? 38.957  209.282 42.108  1.00 41.89  ? 112 ILE I C   1 
ATOM   9575  O  O   . ILE I  1 113 ? 39.466  209.256 43.238  1.00 42.37  ? 112 ILE I O   1 
ATOM   9576  C  CB  . ILE I  1 113 ? 39.079  211.768 41.701  1.00 47.84  ? 112 ILE I CB  1 
ATOM   9577  C  CG1 . ILE I  1 113 ? 37.598  212.117 41.605  1.00 46.34  ? 112 ILE I CG1 1 
ATOM   9578  C  CG2 . ILE I  1 113 ? 39.931  212.877 41.033  1.00 46.61  ? 112 ILE I CG2 1 
ATOM   9579  C  CD1 . ILE I  1 113 ? 37.171  213.064 42.690  1.00 44.94  ? 112 ILE I CD1 1 
ATOM   9580  N  N   . ILE I  1 114 ? 38.044  208.394 41.694  1.00 47.29  ? 113 ILE I N   1 
ATOM   9581  C  CA  . ILE I  1 114 ? 37.513  207.250 42.506  1.00 49.33  ? 113 ILE I CA  1 
ATOM   9582  C  C   . ILE I  1 114 ? 38.705  206.372 42.860  1.00 50.07  ? 113 ILE I C   1 
ATOM   9583  O  O   . ILE I  1 114 ? 39.570  206.075 42.021  1.00 50.15  ? 113 ILE I O   1 
ATOM   9584  C  CB  . ILE I  1 114 ? 36.490  206.371 41.703  1.00 45.52  ? 113 ILE I CB  1 
ATOM   9585  C  CG1 . ILE I  1 114 ? 35.369  207.197 41.071  1.00 44.32  ? 113 ILE I CG1 1 
ATOM   9586  C  CG2 . ILE I  1 114 ? 35.891  205.275 42.566  1.00 40.58  ? 113 ILE I CG2 1 
ATOM   9587  C  CD1 . ILE I  1 114 ? 34.228  207.444 42.013  1.00 43.62  ? 113 ILE I CD1 1 
ATOM   9588  N  N   . GLY I  1 115 ? 38.802  205.987 44.107  1.00 49.28  ? 114 GLY I N   1 
ATOM   9589  C  CA  . GLY I  1 115 ? 39.962  205.156 44.501  1.00 47.61  ? 114 GLY I CA  1 
ATOM   9590  C  C   . GLY I  1 115 ? 41.261  205.881 44.730  1.00 49.82  ? 114 GLY I C   1 
ATOM   9591  O  O   . GLY I  1 115 ? 42.301  205.264 45.072  1.00 52.54  ? 114 GLY I O   1 
ATOM   9592  N  N   . ARG I  1 116 ? 41.213  207.195 44.598  1.00 47.37  ? 115 ARG I N   1 
ATOM   9593  C  CA  . ARG I  1 116 ? 42.320  208.004 45.073  1.00 46.97  ? 115 ARG I CA  1 
ATOM   9594  C  C   . ARG I  1 116 ? 41.991  208.609 46.408  1.00 42.81  ? 115 ARG I C   1 
ATOM   9595  O  O   . ARG I  1 116 ? 40.899  208.372 46.902  1.00 40.64  ? 115 ARG I O   1 
ATOM   9596  C  CB  . ARG I  1 116 ? 42.675  209.049 44.056  1.00 46.63  ? 115 ARG I CB  1 
ATOM   9597  C  CG  . ARG I  1 116 ? 43.101  208.396 42.767  1.00 46.80  ? 115 ARG I CG  1 
ATOM   9598  C  CD  . ARG I  1 116 ? 43.058  209.415 41.656  1.00 50.20  ? 115 ARG I CD  1 
ATOM   9599  N  NE  . ARG I  1 116 ? 43.152  208.780 40.344  1.00 54.83  ? 115 ARG I NE  1 
ATOM   9600  C  CZ  . ARG I  1 116 ? 44.212  208.093 39.869  1.00 54.87  ? 115 ARG I CZ  1 
ATOM   9601  N  NH1 . ARG I  1 116 ? 45.379  207.860 40.581  1.00 43.34  ? 115 ARG I NH1 1 
ATOM   9602  N  NH2 . ARG I  1 116 ? 44.067  207.635 38.643  1.00 45.12  ? 115 ARG I NH2 1 
ATOM   9603  N  N   . THR I  1 117 ? 42.942  209.346 46.990  1.00 41.54  ? 116 THR I N   1 
ATOM   9604  C  CA  . THR I  1 117 ? 42.739  209.863 48.337  1.00 48.45  ? 116 THR I CA  1 
ATOM   9605  C  C   . THR I  1 117 ? 42.476  211.380 48.407  1.00 53.38  ? 116 THR I C   1 
ATOM   9606  O  O   . THR I  1 117 ? 43.212  212.188 47.785  1.00 50.17  ? 116 THR I O   1 
ATOM   9607  C  CB  . THR I  1 117 ? 43.865  209.465 49.294  1.00 43.70  ? 116 THR I CB  1 
ATOM   9608  O  OG1 . THR I  1 117 ? 43.774  208.061 49.541  1.00 46.59  ? 116 THR I OG1 1 
ATOM   9609  C  CG2 . THR I  1 117 ? 43.748  210.229 50.655  1.00 41.54  ? 116 THR I CG2 1 
ATOM   9610  N  N   . LEU I  1 118 ? 41.447  211.760 49.179  1.00 46.45  ? 117 LEU I N   1 
ATOM   9611  C  CA  . LEU I  1 118 ? 41.157  213.185 49.346  1.00 46.48  ? 117 LEU I CA  1 
ATOM   9612  C  C   . LEU I  1 118 ? 41.777  213.582 50.682  1.00 44.98  ? 117 LEU I C   1 
ATOM   9613  O  O   . LEU I  1 118 ? 41.593  212.883 51.704  1.00 42.94  ? 117 LEU I O   1 
ATOM   9614  C  CB  . LEU I  1 118 ? 39.652  213.475 49.218  1.00 45.47  ? 117 LEU I CB  1 
ATOM   9615  C  CG  . LEU I  1 118 ? 39.114  214.842 49.628  1.00 47.07  ? 117 LEU I CG  1 
ATOM   9616  C  CD1 . LEU I  1 118 ? 39.388  215.894 48.553  1.00 47.62  ? 117 LEU I CD1 1 
ATOM   9617  C  CD2 . LEU I  1 118 ? 37.622  214.742 49.894  1.00 45.77  ? 117 LEU I CD2 1 
ATOM   9618  N  N   . VAL I  1 119 ? 42.560  214.675 50.666  1.00 43.67  ? 118 VAL I N   1 
ATOM   9619  C  CA  . VAL I  1 119 ? 43.341  215.073 51.853  1.00 41.41  ? 118 VAL I CA  1 
ATOM   9620  C  C   . VAL I  1 119 ? 43.009  216.493 52.161  1.00 37.85  ? 118 VAL I C   1 
ATOM   9621  O  O   . VAL I  1 119 ? 42.986  217.299 51.256  1.00 40.42  ? 118 VAL I O   1 
ATOM   9622  C  CB  . VAL I  1 119 ? 44.863  215.087 51.555  1.00 44.57  ? 118 VAL I CB  1 
ATOM   9623  C  CG1 . VAL I  1 119 ? 45.681  215.462 52.809  1.00 42.60  ? 118 VAL I CG1 1 
ATOM   9624  C  CG2 . VAL I  1 119 ? 45.315  213.774 50.903  1.00 44.38  ? 118 VAL I CG2 1 
ATOM   9625  N  N   . VAL I  1 120 ? 42.790  216.795 53.427  1.00 38.01  ? 119 VAL I N   1 
ATOM   9626  C  CA  . VAL I  1 120 ? 42.698  218.178 53.874  1.00 39.46  ? 119 VAL I CA  1 
ATOM   9627  C  C   . VAL I  1 120 ? 44.000  218.499 54.640  1.00 46.21  ? 119 VAL I C   1 
ATOM   9628  O  O   . VAL I  1 120 ? 44.387  217.785 55.631  1.00 44.41  ? 119 VAL I O   1 
ATOM   9629  C  CB  . VAL I  1 120 ? 41.458  218.454 54.765  1.00 41.81  ? 119 VAL I CB  1 
ATOM   9630  C  CG1 . VAL I  1 120 ? 41.405  217.506 55.995  1.00 36.25  ? 119 VAL I CG1 1 
ATOM   9631  C  CG2 . VAL I  1 120 ? 41.466  219.937 55.233  1.00 40.24  ? 119 VAL I CG2 1 
ATOM   9632  N  N   . HIS I  1 121 ? 44.663  219.582 54.193  1.00 44.36  ? 120 HIS I N   1 
ATOM   9633  C  CA  . HIS I  1 121 ? 45.956  220.017 54.739  1.00 42.70  ? 120 HIS I CA  1 
ATOM   9634  C  C   . HIS I  1 121 ? 45.972  220.990 55.910  1.00 43.11  ? 120 HIS I C   1 
ATOM   9635  O  O   . HIS I  1 121 ? 45.006  221.677 56.234  1.00 47.41  ? 120 HIS I O   1 
ATOM   9636  C  CB  . HIS I  1 121 ? 46.779  220.620 53.602  1.00 48.23  ? 120 HIS I CB  1 
ATOM   9637  C  CG  . HIS I  1 121 ? 47.200  219.624 52.578  1.00 46.37  ? 120 HIS I CG  1 
ATOM   9638  N  ND1 . HIS I  1 121 ? 48.488  219.137 52.517  1.00 46.11  ? 120 HIS I ND1 1 
ATOM   9639  C  CD2 . HIS I  1 121 ? 46.491  218.958 51.633  1.00 46.45  ? 120 HIS I CD2 1 
ATOM   9640  C  CE1 . HIS I  1 121 ? 48.564  218.245 51.542  1.00 45.10  ? 120 HIS I CE1 1 
ATOM   9641  N  NE2 . HIS I  1 121 ? 47.370  218.118 50.989  1.00 47.48  ? 120 HIS I NE2 1 
ATOM   9642  N  N   . GLU I  1 122 ? 47.131  221.096 56.517  1.00 50.76  ? 121 GLU I N   1 
ATOM   9643  C  CA  . GLU I  1 122 ? 47.377  221.936 57.719  1.00 55.08  ? 121 GLU I CA  1 
ATOM   9644  C  C   . GLU I  1 122 ? 47.249  223.494 57.535  1.00 56.57  ? 121 GLU I C   1 
ATOM   9645  O  O   . GLU I  1 122 ? 46.759  224.208 58.471  1.00 56.96  ? 121 GLU I O   1 
ATOM   9646  C  CB  . GLU I  1 122 ? 48.754  221.513 58.223  1.00 54.11  ? 121 GLU I CB  1 
ATOM   9647  C  CG  . GLU I  1 122 ? 49.361  222.261 59.379  1.00 56.19  ? 121 GLU I CG  1 
ATOM   9648  C  CD  . GLU I  1 122 ? 50.905  222.257 59.301  1.00 70.60  ? 121 GLU I CD  1 
ATOM   9649  O  OE1 . GLU I  1 122 ? 51.493  222.832 60.265  1.00 61.38  ? 121 GLU I OE1 1 
ATOM   9650  O  OE2 . GLU I  1 122 ? 51.531  221.721 58.290  1.00 58.58  ? 121 GLU I OE2 1 
ATOM   9651  N  N   . LYS I  1 123 ? 47.655  223.993 56.349  1.00 48.99  ? 122 LYS I N   1 
ATOM   9652  C  CA  . LYS I  1 123 ? 47.747  225.448 56.060  1.00 51.80  ? 122 LYS I CA  1 
ATOM   9653  C  C   . LYS I  1 123 ? 47.071  225.854 54.757  1.00 51.79  ? 122 LYS I C   1 
ATOM   9654  O  O   . LYS I  1 123 ? 46.543  225.019 54.011  1.00 54.25  ? 122 LYS I O   1 
ATOM   9655  C  CB  . LYS I  1 123 ? 49.210  225.878 55.845  1.00 60.16  ? 122 LYS I CB  1 
ATOM   9656  C  CG  . LYS I  1 123 ? 50.212  225.719 56.979  1.00 55.40  ? 122 LYS I CG  1 
ATOM   9657  C  CD  . LYS I  1 123 ? 51.558  225.804 56.273  1.00 62.66  ? 122 LYS I CD  1 
ATOM   9658  C  CE  . LYS I  1 123 ? 52.745  225.478 57.176  1.00 64.12  ? 122 LYS I CE  1 
ATOM   9659  N  NZ  . LYS I  1 123 ? 53.892  224.954 56.356  1.00 58.56  ? 122 LYS I NZ  1 
ATOM   9660  N  N   . ALA I  1 124 ? 47.119  227.137 54.415  1.00 47.90  ? 123 ALA I N   1 
ATOM   9661  C  CA  . ALA I  1 124 ? 46.450  227.465 53.156  1.00 48.08  ? 123 ALA I CA  1 
ATOM   9662  C  C   . ALA I  1 124 ? 47.302  227.065 51.934  1.00 50.85  ? 123 ALA I C   1 
ATOM   9663  O  O   . ALA I  1 124 ? 48.528  227.141 51.964  1.00 53.68  ? 123 ALA I O   1 
ATOM   9664  C  CB  . ALA I  1 124 ? 46.043  228.933 53.109  1.00 43.32  ? 123 ALA I CB  1 
ATOM   9665  N  N   . ASP I  1 125 ? 46.645  226.624 50.881  1.00 45.60  ? 124 ASP I N   1 
ATOM   9666  C  CA  . ASP I  1 125 ? 47.282  226.406 49.611  1.00 47.79  ? 124 ASP I CA  1 
ATOM   9667  C  C   . ASP I  1 125 ? 47.427  227.857 49.018  1.00 53.22  ? 124 ASP I C   1 
ATOM   9668  O  O   . ASP I  1 125 ? 46.437  228.593 48.867  1.00 51.52  ? 124 ASP I O   1 
ATOM   9669  C  CB  . ASP I  1 125 ? 46.385  225.449 48.795  1.00 42.95  ? 124 ASP I CB  1 
ATOM   9670  C  CG  . ASP I  1 125 ? 46.792  225.307 47.334  1.00 53.66  ? 124 ASP I CG  1 
ATOM   9671  O  OD1 . ASP I  1 125 ? 47.795  225.935 46.912  1.00 51.83  ? 124 ASP I OD1 1 
ATOM   9672  O  OD2 . ASP I  1 125 ? 46.092  224.556 46.575  1.00 50.10  ? 124 ASP I OD2 1 
ATOM   9673  N  N   . ASP I  1 126 ? 48.657  228.273 48.717  1.00 48.32  ? 125 ASP I N   1 
ATOM   9674  C  CA  . ASP I  1 126 ? 48.910  229.597 48.129  1.00 48.87  ? 125 ASP I CA  1 
ATOM   9675  C  C   . ASP I  1 126 ? 48.543  229.603 46.631  1.00 46.15  ? 125 ASP I C   1 
ATOM   9676  O  O   . ASP I  1 126 ? 48.851  230.561 45.965  1.00 47.21  ? 125 ASP I O   1 
ATOM   9677  C  CB  . ASP I  1 126 ? 50.384  230.045 48.314  1.00 46.03  ? 125 ASP I CB  1 
ATOM   9678  C  CG  . ASP I  1 126 ? 51.416  229.071 47.573  1.00 53.65  ? 125 ASP I CG  1 
ATOM   9679  O  OD1 . ASP I  1 126 ? 51.019  228.384 46.565  1.00 46.60  ? 125 ASP I OD1 1 
ATOM   9680  O  OD2 . ASP I  1 126 ? 52.619  228.976 48.000  1.00 52.98  ? 125 ASP I OD2 1 
ATOM   9681  N  N   . LEU I  1 127 ? 47.901  228.565 46.098  1.00 43.58  ? 126 LEU I N   1 
ATOM   9682  C  CA  . LEU I  1 127 ? 47.456  228.535 44.662  1.00 46.56  ? 126 LEU I CA  1 
ATOM   9683  C  C   . LEU I  1 127 ? 48.650  228.544 43.627  1.00 50.49  ? 126 LEU I C   1 
ATOM   9684  O  O   . LEU I  1 127 ? 48.517  228.660 42.370  1.00 49.37  ? 126 LEU I O   1 
ATOM   9685  C  CB  . LEU I  1 127 ? 46.319  229.546 44.391  1.00 45.95  ? 126 LEU I CB  1 
ATOM   9686  C  CG  . LEU I  1 127 ? 45.167  229.487 45.441  1.00 48.09  ? 126 LEU I CG  1 
ATOM   9687  C  CD1 . LEU I  1 127 ? 43.884  230.134 44.955  1.00 43.89  ? 126 LEU I CD1 1 
ATOM   9688  C  CD2 . LEU I  1 127 ? 44.889  228.058 45.946  1.00 47.47  ? 126 LEU I CD2 1 
ATOM   9689  N  N   . GLY I  1 128 ? 49.832  228.317 44.190  1.00 52.93  ? 127 GLY I N   1 
ATOM   9690  C  CA  . GLY I  1 128 ? 51.059  228.227 43.388  1.00 64.18  ? 127 GLY I CA  1 
ATOM   9691  C  C   . GLY I  1 128 ? 51.516  229.573 42.852  1.00 63.90  ? 127 GLY I C   1 
ATOM   9692  O  O   . GLY I  1 128 ? 52.277  229.577 41.892  1.00 61.73  ? 127 GLY I O   1 
ATOM   9693  N  N   . LYS I  1 129 ? 50.991  230.668 43.447  1.00 55.89  ? 128 LYS I N   1 
ATOM   9694  C  CA  . LYS I  1 129 ? 51.445  232.083 43.299  1.00 59.92  ? 128 LYS I CA  1 
ATOM   9695  C  C   . LYS I  1 129 ? 52.330  232.428 44.533  1.00 62.15  ? 128 LYS I C   1 
ATOM   9696  O  O   . LYS I  1 129 ? 52.507  233.602 44.900  1.00 59.76  ? 128 LYS I O   1 
ATOM   9697  C  CB  . LYS I  1 129 ? 50.231  233.071 43.230  1.00 60.27  ? 128 LYS I CB  1 
ATOM   9698  C  CG  . LYS I  1 129 ? 49.524  233.180 41.857  1.00 70.47  ? 128 LYS I CG  1 
ATOM   9699  C  CD  . LYS I  1 129 ? 48.339  232.229 41.774  1.00 70.99  ? 128 LYS I CD  1 
ATOM   9700  C  CE  . LYS I  1 129 ? 47.953  231.880 40.335  1.00 73.16  ? 128 LYS I CE  1 
ATOM   9701  N  NZ  . LYS I  1 129 ? 46.787  230.975 40.519  1.00 64.71  ? 128 LYS I NZ  1 
ATOM   9702  N  N   . GLY I  1 130 ? 52.868  231.410 45.207  1.00 56.36  ? 129 GLY I N   1 
ATOM   9703  C  CA  . GLY I  1 130 ? 53.662  231.681 46.408  1.00 56.72  ? 129 GLY I CA  1 
ATOM   9704  C  C   . GLY I  1 130 ? 55.100  232.197 46.169  1.00 70.83  ? 129 GLY I C   1 
ATOM   9705  O  O   . GLY I  1 130 ? 55.777  232.488 47.160  1.00 69.71  ? 129 GLY I O   1 
ATOM   9706  N  N   . GLY I  1 131 ? 55.603  232.313 44.918  1.00 59.83  ? 130 GLY I N   1 
ATOM   9707  C  CA  . GLY I  1 131 ? 57.012  232.690 44.729  1.00 62.88  ? 130 GLY I CA  1 
ATOM   9708  C  C   . GLY I  1 131 ? 57.869  231.437 44.506  1.00 79.53  ? 130 GLY I C   1 
ATOM   9709  O  O   . GLY I  1 131 ? 57.993  230.988 43.348  1.00 80.48  ? 130 GLY I O   1 
ATOM   9710  N  N   . ASN I  1 132 ? 58.419  230.853 45.604  1.00 78.40  ? 131 ASN I N   1 
ATOM   9711  C  CA  . ASN I  1 132 ? 59.358  229.638 45.641  1.00 73.85  ? 131 ASN I CA  1 
ATOM   9712  C  C   . ASN I  1 132 ? 59.101  228.307 44.808  1.00 77.84  ? 131 ASN I C   1 
ATOM   9713  O  O   . ASN I  1 132 ? 58.045  228.143 44.098  1.00 75.22  ? 131 ASN I O   1 
ATOM   9714  C  CB  . ASN I  1 132 ? 59.724  229.257 47.130  1.00 78.57  ? 131 ASN I CB  1 
ATOM   9715  C  CG  . ASN I  1 132 ? 58.523  228.644 47.951  1.00 90.27  ? 131 ASN I CG  1 
ATOM   9716  O  OD1 . ASN I  1 132 ? 57.579  227.964 47.412  1.00 71.23  ? 131 ASN I OD1 1 
ATOM   9717  N  ND2 . ASN I  1 132 ? 58.579  228.863 49.275  1.00 67.58  ? 131 ASN I ND2 1 
ATOM   9718  N  N   . GLU I  1 133 ? 60.086  227.376 44.939  1.00 72.04  ? 132 GLU I N   1 
ATOM   9719  C  CA  . GLU I  1 133 ? 60.055  225.982 44.377  1.00 70.88  ? 132 GLU I CA  1 
ATOM   9720  C  C   . GLU I  1 133 ? 58.855  225.143 44.914  1.00 67.62  ? 132 GLU I C   1 
ATOM   9721  O  O   . GLU I  1 133 ? 58.166  224.418 44.145  1.00 56.63  ? 132 GLU I O   1 
ATOM   9722  C  CB  . GLU I  1 133 ? 61.389  225.226 44.639  1.00 61.61  ? 132 GLU I CB  1 
ATOM   9723  N  N   . GLU I  1 134 ? 58.625  225.258 46.234  1.00 66.46  ? 133 GLU I N   1 
ATOM   9724  C  CA  . GLU I  1 134 ? 57.612  224.462 46.947  1.00 64.59  ? 133 GLU I CA  1 
ATOM   9725  C  C   . GLU I  1 134 ? 56.220  224.729 46.379  1.00 68.83  ? 133 GLU I C   1 
ATOM   9726  O  O   . GLU I  1 134 ? 55.438  223.785 46.061  1.00 64.21  ? 133 GLU I O   1 
ATOM   9727  C  CB  . GLU I  1 134 ? 57.642  224.777 48.454  1.00 66.33  ? 133 GLU I CB  1 
ATOM   9728  C  CG  . GLU I  1 134 ? 56.888  223.742 49.290  1.00 69.30  ? 133 GLU I CG  1 
ATOM   9729  C  CD  . GLU I  1 134 ? 57.514  222.358 49.163  1.00 79.61  ? 133 GLU I CD  1 
ATOM   9730  O  OE1 . GLU I  1 134 ? 58.356  222.034 50.064  1.00 71.12  ? 133 GLU I OE1 1 
ATOM   9731  O  OE2 . GLU I  1 134 ? 57.198  221.629 48.150  1.00 75.69  ? 133 GLU I OE2 1 
ATOM   9732  N  N   . SER I  1 135 ? 55.982  226.040 46.204  1.00 68.59  ? 134 SER I N   1 
ATOM   9733  C  CA  . SER I  1 135 ? 54.726  226.625 45.744  1.00 65.23  ? 134 SER I CA  1 
ATOM   9734  C  C   . SER I  1 135 ? 54.183  226.102 44.397  1.00 63.76  ? 134 SER I C   1 
ATOM   9735  O  O   . SER I  1 135 ? 52.958  226.196 44.135  1.00 61.29  ? 134 SER I O   1 
ATOM   9736  C  CB  . SER I  1 135 ? 54.849  228.166 45.739  1.00 60.05  ? 134 SER I CB  1 
ATOM   9737  O  OG  . SER I  1 135 ? 53.664  228.735 45.185  1.00 64.04  ? 134 SER I OG  1 
ATOM   9738  N  N   . THR I  1 136 ? 55.087  225.612 43.545  1.00 58.53  ? 135 THR I N   1 
ATOM   9739  C  CA  . THR I  1 136 ? 54.741  225.088 42.200  1.00 60.35  ? 135 THR I CA  1 
ATOM   9740  C  C   . THR I  1 136 ? 54.393  223.568 42.264  1.00 61.95  ? 135 THR I C   1 
ATOM   9741  O  O   . THR I  1 136 ? 53.768  223.013 41.319  1.00 57.58  ? 135 THR I O   1 
ATOM   9742  C  CB  . THR I  1 136 ? 55.959  225.282 41.270  1.00 68.24  ? 135 THR I CB  1 
ATOM   9743  O  OG1 . THR I  1 136 ? 57.117  224.633 41.884  1.00 57.15  ? 135 THR I OG1 1 
ATOM   9744  C  CG2 . THR I  1 136 ? 56.219  226.858 41.059  1.00 60.62  ? 135 THR I CG2 1 
ATOM   9745  N  N   . LYS I  1 137 ? 54.771  222.934 43.389  1.00 55.32  ? 136 LYS I N   1 
ATOM   9746  C  CA  . LYS I  1 137 ? 54.599  221.498 43.627  1.00 64.70  ? 136 LYS I CA  1 
ATOM   9747  C  C   . LYS I  1 137 ? 53.308  221.140 44.458  1.00 66.54  ? 136 LYS I C   1 
ATOM   9748  O  O   . LYS I  1 137 ? 52.419  220.363 43.979  1.00 60.65  ? 136 LYS I O   1 
ATOM   9749  C  CB  . LYS I  1 137 ? 55.873  220.944 44.317  1.00 67.36  ? 136 LYS I CB  1 
ATOM   9750  C  CG  . LYS I  1 137 ? 56.923  220.415 43.337  1.00 71.23  ? 136 LYS I CG  1 
ATOM   9751  C  CD  . LYS I  1 137 ? 58.236  220.208 44.114  1.00 79.66  ? 136 LYS I CD  1 
ATOM   9752  C  CE  . LYS I  1 137 ? 59.154  219.117 43.531  1.00 74.29  ? 136 LYS I CE  1 
ATOM   9753  N  NZ  . LYS I  1 137 ? 60.151  218.833 44.619  1.00 63.36  ? 136 LYS I NZ  1 
ATOM   9754  N  N   . THR I  1 138 ? 53.243  221.709 45.682  1.00 56.13  ? 137 THR I N   1 
ATOM   9755  C  CA  . THR I  1 138 ? 52.268  221.390 46.752  1.00 52.68  ? 137 THR I CA  1 
ATOM   9756  C  C   . THR I  1 138 ? 51.443  222.640 47.193  1.00 58.53  ? 137 THR I C   1 
ATOM   9757  O  O   . THR I  1 138 ? 50.488  222.580 48.053  1.00 57.06  ? 137 THR I O   1 
ATOM   9758  C  CB  . THR I  1 138 ? 53.016  220.797 47.989  1.00 53.90  ? 137 THR I CB  1 
ATOM   9759  O  OG1 . THR I  1 138 ? 53.269  221.828 48.962  1.00 55.66  ? 137 THR I OG1 1 
ATOM   9760  C  CG2 . THR I  1 138 ? 54.395  220.120 47.564  1.00 58.09  ? 137 THR I CG2 1 
ATOM   9761  N  N   . GLY I  1 139 ? 51.846  223.780 46.625  1.00 60.35  ? 138 GLY I N   1 
ATOM   9762  C  CA  . GLY I  1 139 ? 51.404  225.091 47.086  1.00 53.34  ? 138 GLY I CA  1 
ATOM   9763  C  C   . GLY I  1 139 ? 51.657  225.468 48.533  1.00 50.94  ? 138 GLY I C   1 
ATOM   9764  O  O   . GLY I  1 139 ? 50.978  226.388 49.008  1.00 48.95  ? 138 GLY I O   1 
ATOM   9765  N  N   . ASN I  1 140 ? 52.617  224.815 49.227  1.00 51.95  ? 139 ASN I N   1 
ATOM   9766  C  CA  . ASN I  1 140 ? 52.950  225.110 50.693  1.00 54.05  ? 139 ASN I CA  1 
ATOM   9767  C  C   . ASN I  1 140 ? 51.790  224.844 51.694  1.00 56.82  ? 139 ASN I C   1 
ATOM   9768  O  O   . ASN I  1 140 ? 51.758  225.385 52.857  1.00 56.62  ? 139 ASN I O   1 
ATOM   9769  C  CB  . ASN I  1 140 ? 53.460  226.551 50.903  1.00 52.50  ? 139 ASN I CB  1 
ATOM   9770  C  CG  . ASN I  1 140 ? 54.787  226.810 50.194  1.00 58.51  ? 139 ASN I CG  1 
ATOM   9771  O  OD1 . ASN I  1 140 ? 54.839  227.308 49.029  1.00 47.25  ? 139 ASN I OD1 1 
ATOM   9772  N  ND2 . ASN I  1 140 ? 55.889  226.435 50.884  1.00 57.68  ? 139 ASN I ND2 1 
ATOM   9773  N  N   . ALA I  1 141 ? 50.850  223.985 51.285  1.00 54.86  ? 140 ALA I N   1 
ATOM   9774  C  CA  . ALA I  1 141 ? 49.758  223.628 52.204  1.00 55.08  ? 140 ALA I CA  1 
ATOM   9775  C  C   . ALA I  1 141 ? 50.259  222.892 53.479  1.00 52.35  ? 140 ALA I C   1 
ATOM   9776  O  O   . ALA I  1 141 ? 49.507  222.802 54.475  1.00 56.08  ? 140 ALA I O   1 
ATOM   9777  C  CB  . ALA I  1 141 ? 48.586  222.911 51.485  1.00 51.21  ? 140 ALA I CB  1 
ATOM   9778  N  N   . GLY I  1 142 ? 51.515  222.435 53.494  1.00 45.46  ? 141 GLY I N   1 
ATOM   9779  C  CA  . GLY I  1 142 ? 52.012  221.716 54.667  1.00 45.88  ? 141 GLY I CA  1 
ATOM   9780  C  C   . GLY I  1 142 ? 51.412  220.306 54.911  1.00 55.21  ? 141 GLY I C   1 
ATOM   9781  O  O   . GLY I  1 142 ? 51.062  219.548 53.966  1.00 53.29  ? 141 GLY I O   1 
ATOM   9782  N  N   . SER I  1 143 ? 51.290  219.924 56.189  1.00 53.49  ? 142 SER I N   1 
ATOM   9783  C  CA  . SER I  1 143 ? 51.105  218.501 56.490  1.00 53.17  ? 142 SER I CA  1 
ATOM   9784  C  C   . SER I  1 143 ? 49.635  218.017 56.252  1.00 55.95  ? 142 SER I C   1 
ATOM   9785  O  O   . SER I  1 143 ? 48.700  218.810 56.098  1.00 51.38  ? 142 SER I O   1 
ATOM   9786  C  CB  . SER I  1 143 ? 51.629  218.219 57.878  1.00 50.40  ? 142 SER I CB  1 
ATOM   9787  O  OG  . SER I  1 143 ? 50.863  218.984 58.805  1.00 58.18  ? 142 SER I OG  1 
ATOM   9788  N  N   . ARG I  1 144 ? 49.476  216.709 56.144  1.00 54.59  ? 143 ARG I N   1 
ATOM   9789  C  CA  . ARG I  1 144 ? 48.184  216.080 55.891  1.00 48.69  ? 143 ARG I CA  1 
ATOM   9790  C  C   . ARG I  1 144 ? 47.439  215.848 57.216  1.00 48.47  ? 143 ARG I C   1 
ATOM   9791  O  O   . ARG I  1 144 ? 48.024  215.292 58.170  1.00 46.15  ? 143 ARG I O   1 
ATOM   9792  C  CB  . ARG I  1 144 ? 48.469  214.809 55.140  1.00 47.99  ? 143 ARG I CB  1 
ATOM   9793  C  CG  . ARG I  1 144 ? 49.306  215.091 53.898  1.00 43.44  ? 143 ARG I CG  1 
ATOM   9794  C  CD  . ARG I  1 144 ? 49.665  213.817 53.140  1.00 46.36  ? 143 ARG I CD  1 
ATOM   9795  N  NE  . ARG I  1 144 ? 50.565  214.239 52.077  1.00 48.58  ? 143 ARG I NE  1 
ATOM   9796  C  CZ  . ARG I  1 144 ? 50.774  213.610 50.921  1.00 52.96  ? 143 ARG I CZ  1 
ATOM   9797  N  NH1 . ARG I  1 144 ? 50.175  212.435 50.612  1.00 46.44  ? 143 ARG I NH1 1 
ATOM   9798  N  NH2 . ARG I  1 144 ? 51.644  214.172 50.073  1.00 48.55  ? 143 ARG I NH2 1 
ATOM   9799  N  N   . LEU I  1 145 ? 46.194  216.364 57.319  1.00 48.84  ? 144 LEU I N   1 
ATOM   9800  C  CA  . LEU I  1 145 ? 45.468  216.414 58.612  1.00 41.56  ? 144 LEU I CA  1 
ATOM   9801  C  C   . LEU I  1 145 ? 44.470  215.284 58.719  1.00 43.30  ? 144 LEU I C   1 
ATOM   9802  O  O   . LEU I  1 145 ? 44.236  214.782 59.837  1.00 40.77  ? 144 LEU I O   1 
ATOM   9803  C  CB  . LEU I  1 145 ? 44.722  217.725 58.777  1.00 44.96  ? 144 LEU I CB  1 
ATOM   9804  C  CG  . LEU I  1 145 ? 45.440  218.992 59.241  1.00 50.44  ? 144 LEU I CG  1 
ATOM   9805  C  CD1 . LEU I  1 145 ? 44.412  220.103 59.402  1.00 45.32  ? 144 LEU I CD1 1 
ATOM   9806  C  CD2 . LEU I  1 145 ? 46.217  218.750 60.547  1.00 52.68  ? 144 LEU I CD2 1 
ATOM   9807  N  N   . ALA I  1 146 ? 43.872  214.923 57.557  1.00 41.00  ? 145 ALA I N   1 
ATOM   9808  C  CA  . ALA I  1 146 ? 42.868  213.850 57.425  1.00 41.42  ? 145 ALA I CA  1 
ATOM   9809  C  C   . ALA I  1 146 ? 42.777  213.493 55.987  1.00 43.96  ? 145 ALA I C   1 
ATOM   9810  O  O   . ALA I  1 146 ? 43.069  214.335 55.129  1.00 47.69  ? 145 ALA I O   1 
ATOM   9811  C  CB  . ALA I  1 146 ? 41.474  214.253 57.942  1.00 36.73  ? 145 ALA I CB  1 
ATOM   9812  N  N   . CYS I  1 147 ? 42.344  212.258 55.713  1.00 43.68  ? 146 CYS I N   1 
ATOM   9813  C  CA  . CYS I  1 147 ? 42.156  211.816 54.342  1.00 42.84  ? 146 CYS I CA  1 
ATOM   9814  C  C   . CYS I  1 147 ? 41.248  210.599 54.400  1.00 41.65  ? 146 CYS I C   1 
ATOM   9815  O  O   . CYS I  1 147 ? 40.948  210.087 55.469  1.00 40.51  ? 146 CYS I O   1 
ATOM   9816  C  CB  . CYS I  1 147 ? 43.508  211.381 53.741  1.00 49.06  ? 146 CYS I CB  1 
ATOM   9817  S  SG  . CYS I  1 147 ? 44.440  210.184 54.776  1.00 53.43  ? 146 CYS I SG  1 
ATOM   9818  N  N   . GLY I  1 148 ? 40.838  210.130 53.235  1.00 38.31  ? 147 GLY I N   1 
ATOM   9819  C  CA  . GLY I  1 148 ? 40.196  208.870 53.144  1.00 39.11  ? 147 GLY I CA  1 
ATOM   9820  C  C   . GLY I  1 148 ? 40.152  208.561 51.681  1.00 38.11  ? 147 GLY I C   1 
ATOM   9821  O  O   . GLY I  1 148 ? 40.534  209.375 50.838  1.00 42.99  ? 147 GLY I O   1 
ATOM   9822  N  N   . VAL I  1 149 ? 39.652  207.399 51.345  1.00 37.49  ? 148 VAL I N   1 
ATOM   9823  C  CA  . VAL I  1 149 ? 39.642  207.049 49.941  1.00 41.88  ? 148 VAL I CA  1 
ATOM   9824  C  C   . VAL I  1 149 ? 38.299  207.399 49.382  1.00 41.69  ? 148 VAL I C   1 
ATOM   9825  O  O   . VAL I  1 149 ? 37.265  207.187 50.015  1.00 47.62  ? 148 VAL I O   1 
ATOM   9826  C  CB  . VAL I  1 149 ? 39.979  205.527 49.791  1.00 43.68  ? 148 VAL I CB  1 
ATOM   9827  C  CG1 . VAL I  1 149 ? 40.025  205.088 48.349  1.00 38.95  ? 148 VAL I CG1 1 
ATOM   9828  C  CG2 . VAL I  1 149 ? 41.323  205.234 50.472  1.00 41.31  ? 148 VAL I CG2 1 
ATOM   9829  N  N   . ILE I  1 150 ? 38.307  207.878 48.165  1.00 42.67  ? 149 ILE I N   1 
ATOM   9830  C  CA  . ILE I  1 150 ? 37.093  208.241 47.468  1.00 39.26  ? 149 ILE I CA  1 
ATOM   9831  C  C   . ILE I  1 150 ? 36.483  206.977 46.893  1.00 44.35  ? 149 ILE I C   1 
ATOM   9832  O  O   . ILE I  1 150 ? 37.068  206.367 45.949  1.00 46.84  ? 149 ILE I O   1 
ATOM   9833  C  CB  . ILE I  1 150 ? 37.396  209.220 46.314  1.00 38.66  ? 149 ILE I CB  1 
ATOM   9834  C  CG1 . ILE I  1 150 ? 38.319  210.370 46.828  1.00 38.07  ? 149 ILE I CG1 1 
ATOM   9835  C  CG2 . ILE I  1 150 ? 36.094  209.627 45.586  1.00 34.11  ? 149 ILE I CG2 1 
ATOM   9836  C  CD1 . ILE I  1 150 ? 38.519  211.581 45.903  1.00 38.96  ? 149 ILE I CD1 1 
ATOM   9837  N  N   . GLY I  1 151 ? 35.292  206.636 47.412  1.00 43.64  ? 150 GLY I N   1 
ATOM   9838  C  CA  . GLY I  1 151 ? 34.487  205.473 46.991  1.00 40.40  ? 150 GLY I CA  1 
ATOM   9839  C  C   . GLY I  1 151 ? 33.155  205.758 46.337  1.00 46.45  ? 150 GLY I C   1 
ATOM   9840  O  O   . GLY I  1 151 ? 32.494  206.774 46.610  1.00 51.44  ? 150 GLY I O   1 
ATOM   9841  N  N   . ILE I  1 152 ? 32.786  204.846 45.437  1.00 49.24  ? 151 ILE I N   1 
ATOM   9842  C  CA  . ILE I  1 152 ? 31.527  204.830 44.709  1.00 50.19  ? 151 ILE I CA  1 
ATOM   9843  C  C   . ILE I  1 152 ? 30.377  204.796 45.720  1.00 51.99  ? 151 ILE I C   1 
ATOM   9844  O  O   . ILE I  1 152 ? 30.350  203.933 46.618  1.00 47.47  ? 151 ILE I O   1 
ATOM   9845  C  CB  . ILE I  1 152 ? 31.455  203.623 43.704  1.00 50.81  ? 151 ILE I CB  1 
ATOM   9846  C  CG1 . ILE I  1 152 ? 32.614  203.726 42.679  1.00 54.06  ? 151 ILE I CG1 1 
ATOM   9847  C  CG2 . ILE I  1 152 ? 30.133  203.627 42.907  1.00 42.28  ? 151 ILE I CG2 1 
ATOM   9848  C  CD1 . ILE I  1 152 ? 32.986  202.461 41.882  1.00 56.82  ? 151 ILE I CD1 1 
ATOM   9849  N  N   . ALA I  1 153 ? 29.464  205.761 45.566  1.00 47.89  ? 152 ALA I N   1 
ATOM   9850  C  CA  . ALA I  1 153 ? 28.296  205.907 46.440  1.00 47.46  ? 152 ALA I CA  1 
ATOM   9851  C  C   . ALA I  1 153 ? 27.026  205.485 45.673  1.00 50.12  ? 152 ALA I C   1 
ATOM   9852  O  O   . ALA I  1 153 ? 26.947  205.531 44.394  1.00 48.18  ? 152 ALA I O   1 
ATOM   9853  C  CB  . ALA I  1 153 ? 28.210  207.364 46.936  1.00 42.94  ? 152 ALA I CB  1 
ATOM   9854  N  N   . GLN I  1 154 ? 26.024  205.088 46.451  1.00 48.30  ? 153 GLN I N   1 
ATOM   9855  C  CA  . GLN I  1 154 ? 24.759  204.625 45.903  1.00 50.62  ? 153 GLN I CA  1 
ATOM   9856  C  C   . GLN I  1 154 ? 24.073  205.756 45.170  1.00 65.93  ? 153 GLN I C   1 
ATOM   9857  O  O   . GLN I  1 154 ? 23.733  206.810 45.798  1.00 58.82  ? 153 GLN I O   1 
ATOM   9858  C  CB  . GLN I  1 154 ? 23.806  204.167 46.993  1.00 50.28  ? 153 GLN I CB  1 
ATOM   9859  C  CG  . GLN I  1 154 ? 22.453  203.709 46.395  1.00 57.35  ? 153 GLN I CG  1 
ATOM   9860  C  CD  . GLN I  1 154 ? 21.763  202.666 47.302  1.00 71.64  ? 153 GLN I CD  1 
ATOM   9861  O  OE1 . GLN I  1 154 ? 21.439  202.982 48.469  1.00 65.37  ? 153 GLN I OE1 1 
ATOM   9862  N  NE2 . GLN I  1 154 ? 21.571  201.406 46.793  1.00 61.80  ? 153 GLN I NE2 1 
ATOM   9863  O  OXT . GLN I  1 154 ? 23.819  205.568 43.945  1.00 73.28  ? 153 GLN I OXT 1 
ATOM   9864  N  N   . MET J  1 1   ? 43.126  201.035 33.173  1.00 64.80  ? 0   MET J N   1 
ATOM   9865  C  CA  . MET J  1 1   ? 43.552  201.924 34.316  1.00 76.25  ? 0   MET J CA  1 
ATOM   9866  C  C   . MET J  1 1   ? 44.834  201.287 35.011  1.00 83.96  ? 0   MET J C   1 
ATOM   9867  O  O   . MET J  1 1   ? 45.739  200.746 34.303  1.00 75.24  ? 0   MET J O   1 
ATOM   9868  C  CB  . MET J  1 1   ? 42.343  202.225 35.272  1.00 63.87  ? 0   MET J CB  1 
ATOM   9869  N  N   . ALA J  1 2   ? 44.911  201.309 36.355  1.00 73.73  ? 1   ALA J N   1 
ATOM   9870  C  CA  . ALA J  1 2   ? 46.098  200.783 37.098  1.00 71.98  ? 1   ALA J CA  1 
ATOM   9871  C  C   . ALA J  1 2   ? 46.127  199.231 37.368  1.00 68.32  ? 1   ALA J C   1 
ATOM   9872  O  O   . ALA J  1 2   ? 45.229  198.454 36.983  1.00 57.84  ? 1   ALA J O   1 
ATOM   9873  C  CB  . ALA J  1 2   ? 46.321  201.576 38.396  1.00 71.43  ? 1   ALA J CB  1 
ATOM   9874  N  N   . THR J  1 3   ? 47.198  198.794 38.023  1.00 60.36  ? 2   THR J N   1 
ATOM   9875  C  CA  . THR J  1 3   ? 47.520  197.382 38.068  1.00 55.28  ? 2   THR J CA  1 
ATOM   9876  C  C   . THR J  1 3   ? 47.823  197.055 39.545  1.00 52.82  ? 2   THR J C   1 
ATOM   9877  O  O   . THR J  1 3   ? 48.295  195.974 39.889  1.00 56.22  ? 2   THR J O   1 
ATOM   9878  C  CB  . THR J  1 3   ? 48.781  197.067 37.171  1.00 58.57  ? 2   THR J CB  1 
ATOM   9879  O  OG1 . THR J  1 3   ? 49.969  197.622 37.786  1.00 58.23  ? 2   THR J OG1 1 
ATOM   9880  C  CG2 . THR J  1 3   ? 48.658  197.582 35.688  1.00 55.45  ? 2   THR J CG2 1 
ATOM   9881  N  N   . LYS J  1 4   ? 47.612  197.986 40.443  1.00 48.33  ? 3   LYS J N   1 
ATOM   9882  C  CA  . LYS J  1 4   ? 47.837  197.645 41.844  1.00 50.30  ? 3   LYS J CA  1 
ATOM   9883  C  C   . LYS J  1 4   ? 46.739  198.369 42.595  1.00 57.27  ? 3   LYS J C   1 
ATOM   9884  O  O   . LYS J  1 4   ? 46.230  199.383 42.101  1.00 55.25  ? 3   LYS J O   1 
ATOM   9885  C  CB  . LYS J  1 4   ? 49.168  198.182 42.304  1.00 52.43  ? 3   LYS J CB  1 
ATOM   9886  C  CG  . LYS J  1 4   ? 50.349  197.283 42.077  1.00 59.72  ? 3   LYS J CG  1 
ATOM   9887  C  CD  . LYS J  1 4   ? 50.860  196.774 43.454  1.00 66.59  ? 3   LYS J CD  1 
ATOM   9888  C  CE  . LYS J  1 4   ? 52.377  196.606 43.411  1.00 69.99  ? 3   LYS J CE  1 
ATOM   9889  N  NZ  . LYS J  1 4   ? 52.750  196.330 41.980  1.00 61.82  ? 3   LYS J NZ  1 
ATOM   9890  N  N   . ALA J  1 5   ? 46.381  197.856 43.773  1.00 53.25  ? 4   ALA J N   1 
ATOM   9891  C  CA  . ALA J  1 5   ? 45.292  198.382 44.579  1.00 49.35  ? 4   ALA J CA  1 
ATOM   9892  C  C   . ALA J  1 5   ? 45.609  197.903 46.011  1.00 49.02  ? 4   ALA J C   1 
ATOM   9893  O  O   . ALA J  1 5   ? 46.590  197.155 46.217  1.00 52.90  ? 4   ALA J O   1 
ATOM   9894  C  CB  . ALA J  1 5   ? 43.943  197.915 44.016  1.00 43.86  ? 4   ALA J CB  1 
ATOM   9895  N  N   . VAL J  1 6   ? 44.877  198.385 47.007  1.00 44.73  ? 5   VAL J N   1 
ATOM   9896  C  CA  . VAL J  1 6   ? 45.217  198.112 48.421  1.00 43.47  ? 5   VAL J CA  1 
ATOM   9897  C  C   . VAL J  1 6   ? 43.977  198.626 49.187  1.00 47.67  ? 5   VAL J C   1 
ATOM   9898  O  O   . VAL J  1 6   ? 43.155  199.402 48.609  1.00 45.59  ? 5   VAL J O   1 
ATOM   9899  C  CB  . VAL J  1 6   ? 46.526  198.822 48.876  1.00 39.50  ? 5   VAL J CB  1 
ATOM   9900  C  CG1 . VAL J  1 6   ? 46.418  200.334 48.692  1.00 46.26  ? 5   VAL J CG1 1 
ATOM   9901  C  CG2 . VAL J  1 6   ? 46.789  198.622 50.339  1.00 38.70  ? 5   VAL J CG2 1 
ATOM   9902  N  N   . CYS J  1 7   ? 43.866  198.222 50.458  1.00 40.59  ? 6   CYS J N   1 
ATOM   9903  C  CA  . CYS J  1 7   ? 42.719  198.451 51.264  1.00 41.01  ? 6   CYS J CA  1 
ATOM   9904  C  C   . CYS J  1 7   ? 43.098  198.222 52.719  1.00 41.12  ? 6   CYS J C   1 
ATOM   9905  O  O   . CYS J  1 7   ? 43.665  197.218 53.073  1.00 45.75  ? 6   CYS J O   1 
ATOM   9906  C  CB  . CYS J  1 7   ? 41.619  197.475 50.831  1.00 43.80  ? 6   CYS J CB  1 
ATOM   9907  S  SG  . CYS J  1 7   ? 40.099  197.550 51.834  1.00 48.46  ? 6   CYS J SG  1 
ATOM   9908  N  N   . VAL J  1 8   ? 42.732  199.151 53.573  1.00 44.41  ? 7   VAL J N   1 
ATOM   9909  C  CA  . VAL J  1 8   ? 43.058  199.076 54.987  1.00 43.22  ? 7   VAL J CA  1 
ATOM   9910  C  C   . VAL J  1 8   ? 41.772  198.715 55.652  1.00 47.34  ? 7   VAL J C   1 
ATOM   9911  O  O   . VAL J  1 8   ? 40.797  199.443 55.545  1.00 51.27  ? 7   VAL J O   1 
ATOM   9912  C  CB  . VAL J  1 8   ? 43.525  200.442 55.452  1.00 40.62  ? 7   VAL J CB  1 
ATOM   9913  C  CG1 . VAL J  1 8   ? 43.842  200.421 56.930  1.00 38.90  ? 7   VAL J CG1 1 
ATOM   9914  C  CG2 . VAL J  1 8   ? 44.726  200.882 54.579  1.00 42.23  ? 7   VAL J CG2 1 
ATOM   9915  N  N   . LEU J  1 9   ? 41.724  197.542 56.259  1.00 52.49  ? 8   LEU J N   1 
ATOM   9916  C  CA  . LEU J  1 9   ? 40.483  197.062 56.876  1.00 48.80  ? 8   LEU J CA  1 
ATOM   9917  C  C   . LEU J  1 9   ? 40.435  197.568 58.275  1.00 50.49  ? 8   LEU J C   1 
ATOM   9918  O  O   . LEU J  1 9   ? 41.449  197.501 58.959  1.00 59.88  ? 8   LEU J O   1 
ATOM   9919  C  CB  . LEU J  1 9   ? 40.372  195.551 56.804  1.00 47.73  ? 8   LEU J CB  1 
ATOM   9920  C  CG  . LEU J  1 9   ? 39.921  195.282 55.364  1.00 48.52  ? 8   LEU J CG  1 
ATOM   9921  C  CD1 . LEU J  1 9   ? 41.051  194.656 54.604  1.00 53.57  ? 8   LEU J CD1 1 
ATOM   9922  C  CD2 . LEU J  1 9   ? 38.833  194.252 55.400  1.00 52.60  ? 8   LEU J CD2 1 
ATOM   9923  N  N   . LYS J  1 10  ? 39.296  198.128 58.684  1.00 49.03  ? 9   LYS J N   1 
ATOM   9924  C  CA  . LYS J  1 10  ? 39.110  198.681 60.045  1.00 44.74  ? 9   LYS J CA  1 
ATOM   9925  C  C   . LYS J  1 10  ? 37.692  198.412 60.467  1.00 44.97  ? 9   LYS J C   1 
ATOM   9926  O  O   . LYS J  1 10  ? 36.808  198.414 59.589  1.00 42.41  ? 9   LYS J O   1 
ATOM   9927  C  CB  . LYS J  1 10  ? 39.277  200.193 60.015  1.00 46.75  ? 9   LYS J CB  1 
ATOM   9928  C  CG  . LYS J  1 10  ? 40.452  200.642 60.813  1.00 54.60  ? 9   LYS J CG  1 
ATOM   9929  C  CD  . LYS J  1 10  ? 41.575  201.129 59.928  1.00 62.56  ? 9   LYS J CD  1 
ATOM   9930  C  CE  . LYS J  1 10  ? 42.800  201.517 60.783  1.00 62.20  ? 9   LYS J CE  1 
ATOM   9931  N  NZ  . LYS J  1 10  ? 43.509  202.590 59.991  1.00 63.46  ? 9   LYS J NZ  1 
ATOM   9932  N  N   . GLY J  1 11  ? 37.449  198.211 61.774  1.00 48.23  ? 10  GLY J N   1 
ATOM   9933  C  CA  . GLY J  1 11  ? 36.072  198.102 62.301  1.00 52.81  ? 10  GLY J CA  1 
ATOM   9934  C  C   . GLY J  1 11  ? 35.826  198.924 63.565  1.00 56.35  ? 10  GLY J C   1 
ATOM   9935  O  O   . GLY J  1 11  ? 36.640  199.783 63.868  1.00 58.58  ? 10  GLY J O   1 
ATOM   9936  N  N   . ASP J  1 12  ? 34.708  198.690 64.284  1.00 54.42  ? 11  ASP J N   1 
ATOM   9937  C  CA  . ASP J  1 12  ? 34.560  199.080 65.754  1.00 57.26  ? 11  ASP J CA  1 
ATOM   9938  C  C   . ASP J  1 12  ? 35.483  198.271 66.683  1.00 64.33  ? 11  ASP J C   1 
ATOM   9939  O  O   . ASP J  1 12  ? 36.331  198.864 67.383  1.00 71.28  ? 11  ASP J O   1 
ATOM   9940  C  CB  . ASP J  1 12  ? 33.087  198.954 66.218  1.00 57.25  ? 11  ASP J CB  1 
ATOM   9941  C  CG  . ASP J  1 12  ? 32.097  199.656 65.194  1.00 69.12  ? 11  ASP J CG  1 
ATOM   9942  O  OD1 . ASP J  1 12  ? 32.452  200.796 64.682  1.00 57.09  ? 11  ASP J OD1 1 
ATOM   9943  O  OD2 . ASP J  1 12  ? 31.016  199.047 64.861  1.00 57.75  ? 11  ASP J OD2 1 
ATOM   9944  N  N   . GLY J  1 13  ? 35.330  196.933 66.664  1.00 59.68  ? 12  GLY J N   1 
ATOM   9945  C  CA  . GLY J  1 13  ? 36.165  195.977 67.390  1.00 51.71  ? 12  GLY J CA  1 
ATOM   9946  C  C   . GLY J  1 13  ? 37.640  195.863 66.983  1.00 50.94  ? 12  GLY J C   1 
ATOM   9947  O  O   . GLY J  1 13  ? 38.208  196.779 66.300  1.00 47.65  ? 12  GLY J O   1 
ATOM   9948  N  N   . PRO J  1 14  ? 38.272  194.733 67.411  1.00 53.04  ? 13  PRO J N   1 
ATOM   9949  C  CA  . PRO J  1 14  ? 39.738  194.460 67.234  1.00 51.47  ? 13  PRO J CA  1 
ATOM   9950  C  C   . PRO J  1 14  ? 40.157  194.161 65.799  1.00 51.13  ? 13  PRO J C   1 
ATOM   9951  O  O   . PRO J  1 14  ? 41.370  194.224 65.474  1.00 51.29  ? 13  PRO J O   1 
ATOM   9952  C  CB  . PRO J  1 14  ? 40.002  193.220 68.125  1.00 48.29  ? 13  PRO J CB  1 
ATOM   9953  C  CG  . PRO J  1 14  ? 38.640  192.596 68.417  1.00 49.36  ? 13  PRO J CG  1 
ATOM   9954  C  CD  . PRO J  1 14  ? 37.599  193.693 68.249  1.00 50.92  ? 13  PRO J CD  1 
ATOM   9955  N  N   . VAL J  1 15  ? 39.210  193.850 64.920  1.00 45.15  ? 14  VAL J N   1 
ATOM   9956  C  CA  . VAL J  1 15  ? 39.697  193.365 63.612  1.00 44.63  ? 14  VAL J CA  1 
ATOM   9957  C  C   . VAL J  1 15  ? 40.335  194.495 62.819  1.00 42.86  ? 14  VAL J C   1 
ATOM   9958  O  O   . VAL J  1 15  ? 39.743  195.556 62.738  1.00 53.77  ? 14  VAL J O   1 
ATOM   9959  C  CB  . VAL J  1 15  ? 38.565  192.698 62.820  1.00 42.02  ? 14  VAL J CB  1 
ATOM   9960  C  CG1 . VAL J  1 15  ? 39.074  192.209 61.463  1.00 42.08  ? 14  VAL J CG1 1 
ATOM   9961  C  CG2 . VAL J  1 15  ? 37.949  191.575 63.652  1.00 43.92  ? 14  VAL J CG2 1 
ATOM   9962  N  N   . GLN J  1 16  ? 41.514  194.288 62.239  1.00 44.03  ? 15  GLN J N   1 
ATOM   9963  C  CA  . GLN J  1 16  ? 42.077  195.202 61.192  1.00 43.45  ? 15  GLN J CA  1 
ATOM   9964  C  C   . GLN J  1 16  ? 43.082  194.494 60.307  1.00 46.59  ? 15  GLN J C   1 
ATOM   9965  O  O   . GLN J  1 16  ? 43.585  193.422 60.654  1.00 49.34  ? 15  GLN J O   1 
ATOM   9966  C  CB  . GLN J  1 16  ? 42.751  196.413 61.797  1.00 44.93  ? 15  GLN J CB  1 
ATOM   9967  C  CG  . GLN J  1 16  ? 43.034  196.254 63.271  1.00 57.89  ? 15  GLN J CG  1 
ATOM   9968  C  CD  . GLN J  1 16  ? 44.404  196.763 63.632  1.00 73.10  ? 15  GLN J CD  1 
ATOM   9969  O  OE1 . GLN J  1 16  ? 45.264  196.989 62.756  1.00 71.72  ? 15  GLN J OE1 1 
ATOM   9970  N  NE2 . GLN J  1 16  ? 44.634  196.939 64.931  1.00 71.34  ? 15  GLN J NE2 1 
ATOM   9971  N  N   . GLY J  1 17  ? 43.365  195.048 59.141  1.00 46.12  ? 16  GLY J N   1 
ATOM   9972  C  CA  . GLY J  1 17  ? 44.397  194.450 58.300  1.00 44.87  ? 16  GLY J CA  1 
ATOM   9973  C  C   . GLY J  1 17  ? 44.696  195.200 57.010  1.00 45.05  ? 16  GLY J C   1 
ATOM   9974  O  O   . GLY J  1 17  ? 44.104  196.234 56.752  1.00 46.34  ? 16  GLY J O   1 
ATOM   9975  N  N   . ILE J  1 18  ? 45.600  194.670 56.182  1.00 43.90  ? 17  ILE J N   1 
ATOM   9976  C  CA  . ILE J  1 18  ? 45.933  195.319 54.924  1.00 42.83  ? 17  ILE J CA  1 
ATOM   9977  C  C   . ILE J  1 18  ? 45.825  194.280 53.876  1.00 47.57  ? 17  ILE J C   1 
ATOM   9978  O  O   . ILE J  1 18  ? 46.322  193.164 54.115  1.00 59.90  ? 17  ILE J O   1 
ATOM   9979  C  CB  . ILE J  1 18  ? 47.372  195.874 54.972  1.00 43.76  ? 17  ILE J CB  1 
ATOM   9980  C  CG1 . ILE J  1 18  ? 47.489  196.919 56.116  1.00 48.30  ? 17  ILE J CG1 1 
ATOM   9981  C  CG2 . ILE J  1 18  ? 47.770  196.472 53.636  1.00 43.40  ? 17  ILE J CG2 1 
ATOM   9982  C  CD1 . ILE J  1 18  ? 48.781  197.734 56.136  1.00 49.27  ? 17  ILE J CD1 1 
ATOM   9983  N  N   . ILE J  1 19  ? 45.226  194.604 52.725  1.00 42.88  ? 18  ILE J N   1 
ATOM   9984  C  CA  . ILE J  1 19  ? 45.127  193.645 51.645  1.00 41.66  ? 18  ILE J CA  1 
ATOM   9985  C  C   . ILE J  1 19  ? 45.629  194.265 50.337  1.00 47.70  ? 18  ILE J C   1 
ATOM   9986  O  O   . ILE J  1 19  ? 45.283  195.404 50.083  1.00 57.36  ? 18  ILE J O   1 
ATOM   9987  C  CB  . ILE J  1 19  ? 43.666  193.186 51.473  1.00 37.80  ? 18  ILE J CB  1 
ATOM   9988  C  CG1 . ILE J  1 19  ? 43.160  192.403 52.687  1.00 40.95  ? 18  ILE J CG1 1 
ATOM   9989  C  CG2 . ILE J  1 19  ? 43.461  192.437 50.174  1.00 39.74  ? 18  ILE J CG2 1 
ATOM   9990  C  CD1 . ILE J  1 19  ? 43.808  191.069 53.037  1.00 45.17  ? 18  ILE J CD1 1 
ATOM   9991  N  N   . ASN J  1 20  ? 46.373  193.523 49.486  1.00 42.45  ? 19  ASN J N   1 
ATOM   9992  C  CA  . ASN J  1 20  ? 46.886  194.084 48.237  1.00 45.07  ? 19  ASN J CA  1 
ATOM   9993  C  C   . ASN J  1 20  ? 46.252  193.413 47.095  1.00 42.91  ? 19  ASN J C   1 
ATOM   9994  O  O   . ASN J  1 20  ? 45.710  192.327 47.254  1.00 46.73  ? 19  ASN J O   1 
ATOM   9995  C  CB  . ASN J  1 20  ? 48.396  194.004 48.113  1.00 46.07  ? 19  ASN J CB  1 
ATOM   9996  C  CG  . ASN J  1 20  ? 49.089  194.611 49.291  1.00 47.76  ? 19  ASN J CG  1 
ATOM   9997  O  OD1 . ASN J  1 20  ? 49.440  193.921 50.273  1.00 45.10  ? 19  ASN J OD1 1 
ATOM   9998  N  ND2 . ASN J  1 20  ? 49.229  195.927 49.248  1.00 50.98  ? 19  ASN J ND2 1 
ATOM   9999  N  N   . PHE J  1 21  ? 46.248  194.103 45.969  1.00 40.00  ? 20  PHE J N   1 
ATOM   10000 C  CA  . PHE J  1 21  ? 45.731  193.554 44.741  1.00 44.27  ? 20  PHE J CA  1 
ATOM   10001 C  C   . PHE J  1 21  ? 46.746  193.914 43.703  1.00 52.33  ? 20  PHE J C   1 
ATOM   10002 O  O   . PHE J  1 21  ? 47.512  194.895 43.871  1.00 49.00  ? 20  PHE J O   1 
ATOM   10003 C  CB  . PHE J  1 21  ? 44.429  194.152 44.339  1.00 41.40  ? 20  PHE J CB  1 
ATOM   10004 C  CG  . PHE J  1 21  ? 43.348  194.026 45.372  1.00 42.38  ? 20  PHE J CG  1 
ATOM   10005 C  CD1 . PHE J  1 21  ? 43.304  194.881 46.510  1.00 43.35  ? 20  PHE J CD1 1 
ATOM   10006 C  CD2 . PHE J  1 21  ? 42.319  193.121 45.182  1.00 40.39  ? 20  PHE J CD2 1 
ATOM   10007 C  CE1 . PHE J  1 21  ? 42.305  194.764 47.450  1.00 39.96  ? 20  PHE J CE1 1 
ATOM   10008 C  CE2 . PHE J  1 21  ? 41.283  193.035 46.113  1.00 39.31  ? 20  PHE J CE2 1 
ATOM   10009 C  CZ  . PHE J  1 21  ? 41.293  193.840 47.248  1.00 38.61  ? 20  PHE J CZ  1 
ATOM   10010 N  N   . GLU J  1 22  ? 46.805  193.059 42.680  1.00 55.93  ? 21  GLU J N   1 
ATOM   10011 C  CA  . GLU J  1 22  ? 47.824  193.142 41.634  1.00 51.64  ? 21  GLU J CA  1 
ATOM   10012 C  C   . GLU J  1 22  ? 47.252  192.458 40.406  1.00 53.47  ? 21  GLU J C   1 
ATOM   10013 O  O   . GLU J  1 22  ? 46.853  191.288 40.480  1.00 53.72  ? 21  GLU J O   1 
ATOM   10014 C  CB  . GLU J  1 22  ? 49.088  192.490 42.127  1.00 55.46  ? 21  GLU J CB  1 
ATOM   10015 C  CG  . GLU J  1 22  ? 50.355  193.194 41.668  1.00 73.32  ? 21  GLU J CG  1 
ATOM   10016 C  CD  . GLU J  1 22  ? 51.166  192.374 40.635  1.00 90.26  ? 21  GLU J CD  1 
ATOM   10017 O  OE1 . GLU J  1 22  ? 52.377  192.062 40.914  1.00 79.66  ? 21  GLU J OE1 1 
ATOM   10018 O  OE2 . GLU J  1 22  ? 50.598  192.036 39.541  1.00 80.42  ? 21  GLU J OE2 1 
ATOM   10019 N  N   . GLN J  1 23  ? 47.123  193.208 39.306  1.00 46.96  ? 22  GLN J N   1 
ATOM   10020 C  CA  . GLN J  1 23  ? 46.524  192.673 38.098  1.00 50.36  ? 22  GLN J CA  1 
ATOM   10021 C  C   . GLN J  1 23  ? 47.423  193.025 36.892  1.00 63.67  ? 22  GLN J C   1 
ATOM   10022 O  O   . GLN J  1 23  ? 47.209  194.081 36.243  1.00 64.39  ? 22  GLN J O   1 
ATOM   10023 C  CB  . GLN J  1 23  ? 45.101  193.225 37.886  1.00 41.23  ? 22  GLN J CB  1 
ATOM   10024 C  CG  . GLN J  1 23  ? 44.363  192.422 36.878  1.00 42.52  ? 22  GLN J CG  1 
ATOM   10025 C  CD  . GLN J  1 23  ? 43.087  193.072 36.377  1.00 51.21  ? 22  GLN J CD  1 
ATOM   10026 O  OE1 . GLN J  1 23  ? 42.856  194.271 36.523  1.00 54.80  ? 22  GLN J OE1 1 
ATOM   10027 N  NE2 . GLN J  1 23  ? 42.264  192.274 35.732  1.00 45.72  ? 22  GLN J NE2 1 
ATOM   10028 N  N   . LYS J  1 24  ? 48.395  192.152 36.557  1.00 64.04  ? 23  LYS J N   1 
ATOM   10029 C  CA  . LYS J  1 24  ? 49.327  192.475 35.446  1.00 63.73  ? 23  LYS J CA  1 
ATOM   10030 C  C   . LYS J  1 24  ? 48.608  192.608 34.101  1.00 70.84  ? 23  LYS J C   1 
ATOM   10031 O  O   . LYS J  1 24  ? 48.793  193.599 33.374  1.00 67.92  ? 23  LYS J O   1 
ATOM   10032 C  CB  . LYS J  1 24  ? 50.510  191.521 35.397  1.00 64.16  ? 23  LYS J CB  1 
ATOM   10033 C  CG  . LYS J  1 24  ? 51.570  191.969 36.388  1.00 65.51  ? 23  LYS J CG  1 
ATOM   10034 C  CD  . LYS J  1 24  ? 52.367  190.783 36.908  1.00 75.92  ? 23  LYS J CD  1 
ATOM   10035 C  CE  . LYS J  1 24  ? 53.482  191.285 37.874  1.00 82.05  ? 23  LYS J CE  1 
ATOM   10036 N  NZ  . LYS J  1 24  ? 54.867  191.351 37.240  1.00 67.65  ? 23  LYS J NZ  1 
ATOM   10037 N  N   . GLU J  1 25  ? 47.704  191.679 33.827  1.00 66.58  ? 24  GLU J N   1 
ATOM   10038 C  CA  . GLU J  1 25  ? 47.034  191.660 32.548  1.00 67.29  ? 24  GLU J CA  1 
ATOM   10039 C  C   . GLU J  1 25  ? 45.593  192.150 32.640  1.00 67.69  ? 24  GLU J C   1 
ATOM   10040 O  O   . GLU J  1 25  ? 44.825  191.629 33.462  1.00 65.20  ? 24  GLU J O   1 
ATOM   10041 C  CB  . GLU J  1 25  ? 47.106  190.211 32.016  1.00 73.26  ? 24  GLU J CB  1 
ATOM   10042 C  CG  . GLU J  1 25  ? 48.495  189.831 31.513  1.00 75.04  ? 24  GLU J CG  1 
ATOM   10043 C  CD  . GLU J  1 25  ? 48.894  190.702 30.290  1.00 95.32  ? 24  GLU J CD  1 
ATOM   10044 O  OE1 . GLU J  1 25  ? 48.175  190.645 29.227  1.00 77.68  ? 24  GLU J OE1 1 
ATOM   10045 O  OE2 . GLU J  1 25  ? 49.904  191.482 30.393  1.00 85.77  ? 24  GLU J OE2 1 
ATOM   10046 N  N   . SER J  1 26  ? 45.224  193.100 31.773  1.00 65.58  ? 25  SER J N   1 
ATOM   10047 C  CA  . SER J  1 26  ? 43.835  193.674 31.682  1.00 71.05  ? 25  SER J CA  1 
ATOM   10048 C  C   . SER J  1 26  ? 42.649  192.699 31.812  1.00 76.06  ? 25  SER J C   1 
ATOM   10049 O  O   . SER J  1 26  ? 41.693  193.019 32.519  1.00 76.19  ? 25  SER J O   1 
ATOM   10050 C  CB  . SER J  1 26  ? 43.568  194.459 30.368  1.00 72.00  ? 25  SER J CB  1 
ATOM   10051 O  OG  . SER J  1 26  ? 44.759  194.738 29.641  1.00 71.57  ? 25  SER J OG  1 
ATOM   10052 N  N   . ASN J  1 27  ? 42.668  191.583 31.078  1.00 74.09  ? 26  ASN J N   1 
ATOM   10053 C  CA  . ASN J  1 27  ? 41.594  190.532 31.165  1.00 84.11  ? 26  ASN J CA  1 
ATOM   10054 C  C   . ASN J  1 27  ? 42.110  189.299 31.976  1.00 85.89  ? 26  ASN J C   1 
ATOM   10055 O  O   . ASN J  1 27  ? 41.795  188.108 31.642  1.00 70.89  ? 26  ASN J O   1 
ATOM   10056 C  CB  . ASN J  1 27  ? 41.153  190.066 29.736  1.00 80.82  ? 26  ASN J CB  1 
ATOM   10057 C  CG  . ASN J  1 27  ? 39.886  190.777 29.228  1.00 88.13  ? 26  ASN J CG  1 
ATOM   10058 O  OD1 . ASN J  1 27  ? 39.837  192.017 29.156  1.00 86.75  ? 26  ASN J OD1 1 
ATOM   10059 N  ND2 . ASN J  1 27  ? 38.855  189.992 28.856  1.00 70.56  ? 26  ASN J ND2 1 
ATOM   10060 N  N   . GLY J  1 28  ? 42.934  189.582 32.995  1.00 65.53  ? 27  GLY J N   1 
ATOM   10061 C  CA  . GLY J  1 28  ? 43.706  188.530 33.658  1.00 64.28  ? 27  GLY J CA  1 
ATOM   10062 C  C   . GLY J  1 28  ? 43.539  188.470 35.164  1.00 64.75  ? 27  GLY J C   1 
ATOM   10063 O  O   . GLY J  1 28  ? 43.074  189.431 35.806  1.00 59.17  ? 27  GLY J O   1 
ATOM   10064 N  N   . PRO J  1 29  ? 43.923  187.334 35.741  1.00 60.76  ? 28  PRO J N   1 
ATOM   10065 C  CA  . PRO J  1 29  ? 43.906  187.077 37.186  1.00 56.55  ? 28  PRO J CA  1 
ATOM   10066 C  C   . PRO J  1 29  ? 44.366  188.292 38.006  1.00 55.12  ? 28  PRO J C   1 
ATOM   10067 O  O   . PRO J  1 29  ? 45.288  189.033 37.583  1.00 50.17  ? 28  PRO J O   1 
ATOM   10068 C  CB  . PRO J  1 29  ? 44.971  185.973 37.353  1.00 60.69  ? 28  PRO J CB  1 
ATOM   10069 C  CG  . PRO J  1 29  ? 45.843  186.061 36.095  1.00 62.68  ? 28  PRO J CG  1 
ATOM   10070 C  CD  . PRO J  1 29  ? 44.832  186.417 35.026  1.00 60.41  ? 28  PRO J CD  1 
ATOM   10071 N  N   . VAL J  1 30  ? 43.724  188.451 39.172  1.00 51.88  ? 29  VAL J N   1 
ATOM   10072 C  CA  . VAL J  1 30  ? 44.060  189.450 40.173  1.00 45.31  ? 29  VAL J CA  1 
ATOM   10073 C  C   . VAL J  1 30  ? 44.516  188.678 41.406  1.00 47.43  ? 29  VAL J C   1 
ATOM   10074 O  O   . VAL J  1 30  ? 43.853  187.722 41.817  1.00 47.61  ? 29  VAL J O   1 
ATOM   10075 C  CB  . VAL J  1 30  ? 42.802  190.224 40.620  1.00 49.53  ? 29  VAL J CB  1 
ATOM   10076 C  CG1 . VAL J  1 30  ? 43.187  191.213 41.733  1.00 49.84  ? 29  VAL J CG1 1 
ATOM   10077 C  CG2 . VAL J  1 30  ? 42.010  190.872 39.448  1.00 42.78  ? 29  VAL J CG2 1 
ATOM   10078 N  N   . LYS J  1 31  ? 45.601  189.117 42.031  1.00 44.13  ? 30  LYS J N   1 
ATOM   10079 C  CA  . LYS J  1 31  ? 46.127  188.433 43.170  1.00 44.69  ? 30  LYS J CA  1 
ATOM   10080 C  C   . LYS J  1 31  ? 45.818  189.300 44.325  1.00 49.92  ? 30  LYS J C   1 
ATOM   10081 O  O   . LYS J  1 31  ? 46.082  190.526 44.260  1.00 51.90  ? 30  LYS J O   1 
ATOM   10082 C  CB  . LYS J  1 31  ? 47.673  188.321 43.091  1.00 51.23  ? 30  LYS J CB  1 
ATOM   10083 C  CG  . LYS J  1 31  ? 48.217  187.620 41.838  1.00 55.86  ? 30  LYS J CG  1 
ATOM   10084 C  CD  . LYS J  1 31  ? 49.738  187.840 41.661  1.00 59.19  ? 30  LYS J CD  1 
ATOM   10085 C  CE  . LYS J  1 31  ? 50.442  186.757 40.801  1.00 56.71  ? 30  LYS J CE  1 
ATOM   10086 N  NZ  . LYS J  1 31  ? 51.900  187.121 40.708  1.00 51.18  ? 30  LYS J NZ  1 
ATOM   10087 N  N   . VAL J  1 32  ? 45.354  188.658 45.406  1.00 46.65  ? 31  VAL J N   1 
ATOM   10088 C  CA  . VAL J  1 32  ? 44.900  189.340 46.597  1.00 43.36  ? 31  VAL J CA  1 
ATOM   10089 C  C   . VAL J  1 32  ? 45.625  188.722 47.739  1.00 46.87  ? 31  VAL J C   1 
ATOM   10090 O  O   . VAL J  1 32  ? 45.383  187.568 48.093  1.00 48.58  ? 31  VAL J O   1 
ATOM   10091 C  CB  . VAL J  1 32  ? 43.391  189.098 46.872  1.00 43.61  ? 31  VAL J CB  1 
ATOM   10092 C  CG1 . VAL J  1 32  ? 42.896  189.990 48.004  1.00 38.06  ? 31  VAL J CG1 1 
ATOM   10093 C  CG2 . VAL J  1 32  ? 42.536  189.278 45.623  1.00 38.81  ? 31  VAL J CG2 1 
ATOM   10094 N  N   . TRP J  1 33  ? 46.491  189.490 48.360  1.00 47.99  ? 32  TRP J N   1 
ATOM   10095 C  CA  . TRP J  1 33  ? 47.213  188.960 49.515  1.00 45.73  ? 32  TRP J CA  1 
ATOM   10096 C  C   . TRP J  1 33  ? 47.350  189.995 50.607  1.00 41.99  ? 32  TRP J C   1 
ATOM   10097 O  O   . TRP J  1 33  ? 47.390  191.187 50.325  1.00 43.81  ? 32  TRP J O   1 
ATOM   10098 C  CB  . TRP J  1 33  ? 48.605  188.450 49.091  1.00 41.31  ? 32  TRP J CB  1 
ATOM   10099 C  CG  . TRP J  1 33  ? 49.623  189.543 48.823  1.00 41.12  ? 32  TRP J CG  1 
ATOM   10100 C  CD1 . TRP J  1 33  ? 50.591  190.062 49.725  1.00 38.93  ? 32  TRP J CD1 1 
ATOM   10101 C  CD2 . TRP J  1 33  ? 49.718  190.325 47.632  1.00 41.60  ? 32  TRP J CD2 1 
ATOM   10102 N  NE1 . TRP J  1 33  ? 51.270  191.075 49.117  1.00 41.50  ? 32  TRP J NE1 1 
ATOM   10103 C  CE2 . TRP J  1 33  ? 50.784  191.247 47.824  1.00 45.29  ? 32  TRP J CE2 1 
ATOM   10104 C  CE3 . TRP J  1 33  ? 48.964  190.373 46.416  1.00 51.41  ? 32  TRP J CE3 1 
ATOM   10105 C  CZ2 . TRP J  1 33  ? 51.175  192.199 46.793  1.00 49.09  ? 32  TRP J CZ2 1 
ATOM   10106 C  CZ3 . TRP J  1 33  ? 49.354  191.310 45.370  1.00 54.11  ? 32  TRP J CZ3 1 
ATOM   10107 C  CH2 . TRP J  1 33  ? 50.468  192.211 45.581  1.00 55.16  ? 32  TRP J CH2 1 
ATOM   10108 N  N   . GLY J  1 34  ? 47.471  189.551 51.843  1.00 38.74  ? 33  GLY J N   1 
ATOM   10109 C  CA  . GLY J  1 34  ? 47.967  190.435 52.869  1.00 36.09  ? 33  GLY J CA  1 
ATOM   10110 C  C   . GLY J  1 34  ? 47.592  189.723 54.135  1.00 40.71  ? 33  GLY J C   1 
ATOM   10111 O  O   . GLY J  1 34  ? 47.436  188.507 54.127  1.00 42.50  ? 33  GLY J O   1 
ATOM   10112 N  N   . SER J  1 35  ? 47.400  190.477 55.209  1.00 39.06  ? 34  SER J N   1 
ATOM   10113 C  CA  . SER J  1 35  ? 47.260  189.923 56.509  1.00 40.61  ? 34  SER J CA  1 
ATOM   10114 C  C   . SER J  1 35  ? 46.181  190.708 57.280  1.00 46.70  ? 34  SER J C   1 
ATOM   10115 O  O   . SER J  1 35  ? 45.911  191.901 57.035  1.00 45.17  ? 34  SER J O   1 
ATOM   10116 C  CB  . SER J  1 35  ? 48.595  190.028 57.227  1.00 47.01  ? 34  SER J CB  1 
ATOM   10117 O  OG  . SER J  1 35  ? 48.323  189.948 58.626  1.00 58.15  ? 34  SER J OG  1 
ATOM   10118 N  N   . ILE J  1 36  ? 45.540  190.033 58.204  1.00 43.68  ? 35  ILE J N   1 
ATOM   10119 C  CA  . ILE J  1 36  ? 44.384  190.625 58.817  1.00 48.44  ? 35  ILE J CA  1 
ATOM   10120 C  C   . ILE J  1 36  ? 44.472  190.020 60.201  1.00 52.81  ? 35  ILE J C   1 
ATOM   10121 O  O   . ILE J  1 36  ? 44.534  188.811 60.310  1.00 54.72  ? 35  ILE J O   1 
ATOM   10122 C  CB  . ILE J  1 36  ? 43.030  190.186 58.155  1.00 47.39  ? 35  ILE J CB  1 
ATOM   10123 C  CG1 . ILE J  1 36  ? 42.896  190.564 56.643  1.00 47.30  ? 35  ILE J CG1 1 
ATOM   10124 C  CG2 . ILE J  1 36  ? 41.835  190.675 58.988  1.00 46.87  ? 35  ILE J CG2 1 
ATOM   10125 C  CD1 . ILE J  1 36  ? 41.606  190.031 55.988  1.00 46.26  ? 35  ILE J CD1 1 
ATOM   10126 N  N   . LYS J  1 37  ? 44.484  190.846 61.251  1.00 53.46  ? 36  LYS J N   1 
ATOM   10127 C  CA  . LYS J  1 37  ? 44.704  190.381 62.624  1.00 50.19  ? 36  LYS J CA  1 
ATOM   10128 C  C   . LYS J  1 37  ? 43.446  190.725 63.403  1.00 48.41  ? 36  LYS J C   1 
ATOM   10129 O  O   . LYS J  1 37  ? 42.607  191.419 62.853  1.00 53.65  ? 36  LYS J O   1 
ATOM   10130 C  CB  . LYS J  1 37  ? 45.998  191.043 63.139  1.00 55.07  ? 36  LYS J CB  1 
ATOM   10131 C  CG  . LYS J  1 37  ? 45.851  192.409 63.814  1.00 63.41  ? 36  LYS J CG  1 
ATOM   10132 C  CD  . LYS J  1 37  ? 46.819  193.500 63.270  1.00 62.65  ? 36  LYS J CD  1 
ATOM   10133 C  CE  . LYS J  1 37  ? 47.635  194.188 64.397  1.00 66.78  ? 36  LYS J CE  1 
ATOM   10134 N  NZ  . LYS J  1 37  ? 46.860  194.529 65.668  1.00 65.36  ? 36  LYS J NZ  1 
ATOM   10135 N  N   . GLY J  1 38  ? 43.276  190.244 64.629  1.00 50.20  ? 37  GLY J N   1 
ATOM   10136 C  CA  . GLY J  1 38  ? 42.058  190.501 65.422  1.00 39.76  ? 37  GLY J CA  1 
ATOM   10137 C  C   . GLY J  1 38  ? 40.959  189.454 65.290  1.00 47.45  ? 37  GLY J C   1 
ATOM   10138 O  O   . GLY J  1 38  ? 39.996  189.437 66.121  1.00 46.04  ? 37  GLY J O   1 
ATOM   10139 N  N   . LEU J  1 39  ? 41.018  188.581 64.271  1.00 42.93  ? 38  LEU J N   1 
ATOM   10140 C  CA  . LEU J  1 39  ? 39.875  187.595 64.086  1.00 44.67  ? 38  LEU J CA  1 
ATOM   10141 C  C   . LEU J  1 39  ? 39.736  186.428 65.120  1.00 47.67  ? 38  LEU J C   1 
ATOM   10142 O  O   . LEU J  1 39  ? 40.747  186.034 65.752  1.00 50.25  ? 38  LEU J O   1 
ATOM   10143 C  CB  . LEU J  1 39  ? 39.914  187.022 62.699  1.00 42.60  ? 38  LEU J CB  1 
ATOM   10144 C  CG  . LEU J  1 39  ? 39.764  188.079 61.619  1.00 43.93  ? 38  LEU J CG  1 
ATOM   10145 C  CD1 . LEU J  1 39  ? 40.517  187.469 60.452  1.00 35.53  ? 38  LEU J CD1 1 
ATOM   10146 C  CD2 . LEU J  1 39  ? 38.257  188.294 61.378  1.00 44.28  ? 38  LEU J CD2 1 
ATOM   10147 N  N   . THR J  1 40  ? 38.519  185.880 65.310  1.00 45.26  ? 39  THR J N   1 
ATOM   10148 C  CA  . THR J  1 40  ? 38.343  184.560 66.009  1.00 47.68  ? 39  THR J CA  1 
ATOM   10149 C  C   . THR J  1 40  ? 38.844  183.439 65.061  1.00 54.81  ? 39  THR J C   1 
ATOM   10150 O  O   . THR J  1 40  ? 38.913  183.628 63.819  1.00 54.19  ? 39  THR J O   1 
ATOM   10151 C  CB  . THR J  1 40  ? 36.884  184.174 66.350  1.00 49.19  ? 39  THR J CB  1 
ATOM   10152 O  OG1 . THR J  1 40  ? 36.118  184.069 65.130  1.00 55.50  ? 39  THR J OG1 1 
ATOM   10153 C  CG2 . THR J  1 40  ? 36.247  185.123 67.286  1.00 42.60  ? 39  THR J CG2 1 
ATOM   10154 N  N   . GLU J  1 41  ? 39.148  182.264 65.612  1.00 58.67  ? 40  GLU J N   1 
ATOM   10155 C  CA  . GLU J  1 41  ? 39.811  181.202 64.809  1.00 55.86  ? 40  GLU J CA  1 
ATOM   10156 C  C   . GLU J  1 41  ? 38.859  180.517 63.832  1.00 49.62  ? 40  GLU J C   1 
ATOM   10157 O  O   . GLU J  1 41  ? 37.712  180.156 64.185  1.00 49.75  ? 40  GLU J O   1 
ATOM   10158 C  CB  . GLU J  1 41  ? 40.329  180.135 65.756  1.00 63.17  ? 40  GLU J CB  1 
ATOM   10159 C  CG  . GLU J  1 41  ? 41.227  179.087 65.101  1.00 64.90  ? 40  GLU J CG  1 
ATOM   10160 C  CD  . GLU J  1 41  ? 41.739  178.094 66.128  1.00 71.70  ? 40  GLU J CD  1 
ATOM   10161 O  OE1 . GLU J  1 41  ? 40.929  177.783 67.090  1.00 64.25  ? 40  GLU J OE1 1 
ATOM   10162 O  OE2 . GLU J  1 41  ? 42.911  177.640 65.948  1.00 57.96  ? 40  GLU J OE2 1 
ATOM   10163 N  N   . GLY J  1 42  ? 39.334  180.320 62.616  1.00 50.56  ? 41  GLY J N   1 
ATOM   10164 C  CA  . GLY J  1 42  ? 38.538  179.611 61.627  1.00 46.12  ? 41  GLY J CA  1 
ATOM   10165 C  C   . GLY J  1 42  ? 38.217  180.497 60.439  1.00 48.20  ? 41  GLY J C   1 
ATOM   10166 O  O   . GLY J  1 42  ? 39.014  181.383 60.061  1.00 48.59  ? 41  GLY J O   1 
ATOM   10167 N  N   . LEU J  1 43  ? 37.023  180.255 59.884  1.00 48.67  ? 42  LEU J N   1 
ATOM   10168 C  CA  . LEU J  1 43  ? 36.604  180.777 58.574  1.00 49.45  ? 42  LEU J CA  1 
ATOM   10169 C  C   . LEU J  1 43  ? 35.726  182.041 58.691  1.00 49.02  ? 42  LEU J C   1 
ATOM   10170 O  O   . LEU J  1 43  ? 34.753  182.090 59.475  1.00 47.23  ? 42  LEU J O   1 
ATOM   10171 C  CB  . LEU J  1 43  ? 35.898  179.691 57.720  1.00 44.20  ? 42  LEU J CB  1 
ATOM   10172 C  CG  . LEU J  1 43  ? 36.727  178.454 57.271  1.00 45.97  ? 42  LEU J CG  1 
ATOM   10173 C  CD1 . LEU J  1 43  ? 35.875  177.332 56.640  1.00 38.15  ? 42  LEU J CD1 1 
ATOM   10174 C  CD2 . LEU J  1 43  ? 37.933  178.866 56.417  1.00 43.60  ? 42  LEU J CD2 1 
ATOM   10175 N  N   . HIS J  1 44  ? 36.106  183.038 57.890  1.00 45.35  ? 43  HIS J N   1 
ATOM   10176 C  CA  . HIS J  1 44  ? 35.406  184.306 57.773  1.00 43.78  ? 43  HIS J CA  1 
ATOM   10177 C  C   . HIS J  1 44  ? 35.232  184.605 56.314  1.00 40.92  ? 43  HIS J C   1 
ATOM   10178 O  O   . HIS J  1 44  ? 36.203  184.463 55.553  1.00 36.63  ? 43  HIS J O   1 
ATOM   10179 C  CB  . HIS J  1 44  ? 36.188  185.419 58.484  1.00 41.49  ? 43  HIS J CB  1 
ATOM   10180 C  CG  . HIS J  1 44  ? 36.393  185.151 59.938  1.00 42.98  ? 43  HIS J CG  1 
ATOM   10181 N  ND1 . HIS J  1 44  ? 35.443  185.456 60.889  1.00 46.88  ? 43  HIS J ND1 1 
ATOM   10182 C  CD2 . HIS J  1 44  ? 37.396  184.529 60.595  1.00 48.34  ? 43  HIS J CD2 1 
ATOM   10183 C  CE1 . HIS J  1 44  ? 35.870  185.077 62.080  1.00 50.23  ? 43  HIS J CE1 1 
ATOM   10184 N  NE2 . HIS J  1 44  ? 37.047  184.499 61.931  1.00 54.30  ? 43  HIS J NE2 1 
ATOM   10185 N  N   . GLY J  1 45  ? 33.993  184.989 55.948  1.00 37.96  ? 44  GLY J N   1 
ATOM   10186 C  CA  . GLY J  1 45  ? 33.646  185.424 54.584  1.00 34.62  ? 44  GLY J CA  1 
ATOM   10187 C  C   . GLY J  1 45  ? 34.436  186.688 54.271  1.00 36.09  ? 44  GLY J C   1 
ATOM   10188 O  O   . GLY J  1 45  ? 34.687  187.538 55.159  1.00 32.60  ? 44  GLY J O   1 
ATOM   10189 N  N   . PHE J  1 46  ? 34.813  186.811 53.001  1.00 34.63  ? 45  PHE J N   1 
ATOM   10190 C  CA  . PHE J  1 46  ? 35.708  187.827 52.549  1.00 36.72  ? 45  PHE J CA  1 
ATOM   10191 C  C   . PHE J  1 46  ? 35.038  188.263 51.225  1.00 39.71  ? 45  PHE J C   1 
ATOM   10192 O  O   . PHE J  1 46  ? 34.958  187.495 50.256  1.00 39.97  ? 45  PHE J O   1 
ATOM   10193 C  CB  . PHE J  1 46  ? 37.124  187.170 52.457  1.00 39.89  ? 45  PHE J CB  1 
ATOM   10194 C  CG  . PHE J  1 46  ? 38.249  188.092 52.076  1.00 39.23  ? 45  PHE J CG  1 
ATOM   10195 C  CD1 . PHE J  1 46  ? 38.712  189.067 52.960  1.00 43.11  ? 45  PHE J CD1 1 
ATOM   10196 C  CD2 . PHE J  1 46  ? 38.911  187.935 50.845  1.00 38.20  ? 45  PHE J CD2 1 
ATOM   10197 C  CE1 . PHE J  1 46  ? 39.791  189.907 52.600  1.00 41.63  ? 45  PHE J CE1 1 
ATOM   10198 C  CE2 . PHE J  1 46  ? 39.961  188.772 50.462  1.00 44.24  ? 45  PHE J CE2 1 
ATOM   10199 C  CZ  . PHE J  1 46  ? 40.409  189.780 51.345  1.00 43.36  ? 45  PHE J CZ  1 
ATOM   10200 N  N   . HIS J  1 47  ? 34.462  189.476 51.190  1.00 38.58  ? 46  HIS J N   1 
ATOM   10201 C  CA  . HIS J  1 47  ? 33.749  189.884 49.972  1.00 37.83  ? 46  HIS J CA  1 
ATOM   10202 C  C   . HIS J  1 47  ? 34.009  191.319 49.580  1.00 36.46  ? 46  HIS J C   1 
ATOM   10203 O  O   . HIS J  1 47  ? 34.387  192.147 50.409  1.00 39.90  ? 46  HIS J O   1 
ATOM   10204 C  CB  . HIS J  1 47  ? 32.244  189.620 50.066  1.00 38.95  ? 46  HIS J CB  1 
ATOM   10205 C  CG  . HIS J  1 47  ? 31.866  188.299 50.667  1.00 42.07  ? 46  HIS J CG  1 
ATOM   10206 N  ND1 . HIS J  1 47  ? 31.380  188.185 51.952  1.00 40.47  ? 46  HIS J ND1 1 
ATOM   10207 C  CD2 . HIS J  1 47  ? 31.866  187.042 50.150  1.00 43.64  ? 46  HIS J CD2 1 
ATOM   10208 C  CE1 . HIS J  1 47  ? 31.116  186.911 52.210  1.00 43.67  ? 46  HIS J CE1 1 
ATOM   10209 N  NE2 . HIS J  1 47  ? 31.389  186.199 51.128  1.00 44.79  ? 46  HIS J NE2 1 
ATOM   10210 N  N   . VAL J  1 48  ? 33.861  191.568 48.298  1.00 34.62  ? 47  VAL J N   1 
ATOM   10211 C  CA  . VAL J  1 48  ? 33.796  192.895 47.756  1.00 37.80  ? 47  VAL J CA  1 
ATOM   10212 C  C   . VAL J  1 48  ? 32.305  193.237 47.667  1.00 39.15  ? 47  VAL J C   1 
ATOM   10213 O  O   . VAL J  1 48  ? 31.516  192.571 46.913  1.00 33.88  ? 47  VAL J O   1 
ATOM   10214 C  CB  . VAL J  1 48  ? 34.507  193.057 46.370  1.00 40.10  ? 47  VAL J CB  1 
ATOM   10215 C  CG1 . VAL J  1 48  ? 34.427  194.505 45.912  1.00 37.19  ? 47  VAL J CG1 1 
ATOM   10216 C  CG2 . VAL J  1 48  ? 35.993  192.692 46.420  1.00 36.64  ? 47  VAL J CG2 1 
ATOM   10217 N  N   . HIS J  1 49  ? 31.947  194.236 48.491  1.00 36.23  ? 48  HIS J N   1 
ATOM   10218 C  CA  . HIS J  1 49  ? 30.605  194.831 48.519  1.00 39.26  ? 48  HIS J CA  1 
ATOM   10219 C  C   . HIS J  1 49  ? 30.534  196.058 47.587  1.00 40.84  ? 48  HIS J C   1 
ATOM   10220 O  O   . HIS J  1 49  ? 31.518  196.744 47.372  1.00 40.61  ? 48  HIS J O   1 
ATOM   10221 C  CB  . HIS J  1 49  ? 30.182  195.225 49.936  1.00 38.29  ? 48  HIS J CB  1 
ATOM   10222 C  CG  . HIS J  1 49  ? 29.998  194.075 50.859  1.00 37.53  ? 48  HIS J CG  1 
ATOM   10223 N  ND1 . HIS J  1 49  ? 28.788  193.754 51.416  1.00 41.90  ? 48  HIS J ND1 1 
ATOM   10224 C  CD2 . HIS J  1 49  ? 30.872  193.156 51.331  1.00 41.00  ? 48  HIS J CD2 1 
ATOM   10225 C  CE1 . HIS J  1 49  ? 28.915  192.698 52.208  1.00 39.31  ? 48  HIS J CE1 1 
ATOM   10226 N  NE2 . HIS J  1 49  ? 30.177  192.319 52.179  1.00 38.99  ? 48  HIS J NE2 1 
ATOM   10227 N  N   . GLU J  1 50  ? 29.339  196.344 47.074  1.00 43.82  ? 49  GLU J N   1 
ATOM   10228 C  CA  . GLU J  1 50  ? 29.125  197.288 45.946  1.00 42.23  ? 49  GLU J CA  1 
ATOM   10229 C  C   . GLU J  1 50  ? 29.630  198.750 46.122  1.00 42.13  ? 49  GLU J C   1 
ATOM   10230 O  O   . GLU J  1 50  ? 30.277  199.316 45.221  1.00 38.81  ? 49  GLU J O   1 
ATOM   10231 C  CB  . GLU J  1 50  ? 27.666  197.258 45.598  1.00 43.58  ? 49  GLU J CB  1 
ATOM   10232 C  CG  . GLU J  1 50  ? 27.299  198.165 44.474  1.00 48.80  ? 49  GLU J CG  1 
ATOM   10233 C  CD  . GLU J  1 50  ? 25.832  198.102 44.156  1.00 52.54  ? 49  GLU J CD  1 
ATOM   10234 O  OE1 . GLU J  1 50  ? 24.939  197.731 45.013  1.00 49.91  ? 49  GLU J OE1 1 
ATOM   10235 O  OE2 . GLU J  1 50  ? 25.600  198.447 42.998  1.00 50.40  ? 49  GLU J OE2 1 
ATOM   10236 N  N   . PHE J  1 51  ? 29.415  199.313 47.301  1.00 37.96  ? 50  PHE J N   1 
ATOM   10237 C  CA  . PHE J  1 51  ? 29.742  200.708 47.552  1.00 38.89  ? 50  PHE J CA  1 
ATOM   10238 C  C   . PHE J  1 51  ? 30.935  200.997 48.485  1.00 41.48  ? 50  PHE J C   1 
ATOM   10239 O  O   . PHE J  1 51  ? 30.976  200.521 49.632  1.00 37.88  ? 50  PHE J O   1 
ATOM   10240 C  CB  . PHE J  1 51  ? 28.486  201.432 48.122  1.00 36.87  ? 50  PHE J CB  1 
ATOM   10241 C  CG  . PHE J  1 51  ? 27.245  201.221 47.300  1.00 35.53  ? 50  PHE J CG  1 
ATOM   10242 C  CD1 . PHE J  1 51  ? 27.213  201.596 45.917  1.00 36.73  ? 50  PHE J CD1 1 
ATOM   10243 C  CD2 . PHE J  1 51  ? 26.091  200.684 47.898  1.00 36.50  ? 50  PHE J CD2 1 
ATOM   10244 C  CE1 . PHE J  1 51  ? 26.072  201.397 45.157  1.00 37.06  ? 50  PHE J CE1 1 
ATOM   10245 C  CE2 . PHE J  1 51  ? 24.909  200.550 47.143  1.00 39.10  ? 50  PHE J CE2 1 
ATOM   10246 C  CZ  . PHE J  1 51  ? 24.908  200.881 45.777  1.00 37.24  ? 50  PHE J CZ  1 
ATOM   10247 N  N   . GLY J  1 52  ? 31.860  201.848 47.998  1.00 45.27  ? 51  GLY J N   1 
ATOM   10248 C  CA  . GLY J  1 52  ? 32.980  202.404 48.798  1.00 47.00  ? 51  GLY J CA  1 
ATOM   10249 C  C   . GLY J  1 52  ? 32.519  203.595 49.662  1.00 54.27  ? 51  GLY J C   1 
ATOM   10250 O  O   . GLY J  1 52  ? 33.102  204.719 49.620  1.00 44.16  ? 51  GLY J O   1 
ATOM   10251 N  N   . ASP J  1 53  ? 31.476  203.320 50.459  1.00 47.62  ? 52  ASP J N   1 
ATOM   10252 C  CA  . ASP J  1 53  ? 30.855  204.266 51.353  1.00 43.91  ? 52  ASP J CA  1 
ATOM   10253 C  C   . ASP J  1 53  ? 30.894  203.774 52.788  1.00 40.70  ? 52  ASP J C   1 
ATOM   10254 O  O   . ASP J  1 53  ? 30.223  202.840 53.169  1.00 46.22  ? 52  ASP J O   1 
ATOM   10255 C  CB  . ASP J  1 53  ? 29.422  204.484 50.842  1.00 46.57  ? 52  ASP J CB  1 
ATOM   10256 C  CG  . ASP J  1 53  ? 28.554  205.387 51.736  1.00 48.08  ? 52  ASP J CG  1 
ATOM   10257 O  OD1 . ASP J  1 53  ? 28.819  205.566 52.979  1.00 44.88  ? 52  ASP J OD1 1 
ATOM   10258 O  OD2 . ASP J  1 53  ? 27.523  205.869 51.132  1.00 48.99  ? 52  ASP J OD2 1 
ATOM   10259 N  N   . ASN J  1 54  ? 31.597  204.488 53.611  1.00 37.83  ? 53  ASN J N   1 
ATOM   10260 C  CA  . ASN J  1 54  ? 31.743  204.110 54.966  1.00 41.78  ? 53  ASN J CA  1 
ATOM   10261 C  C   . ASN J  1 54  ? 31.145  205.122 55.964  1.00 41.85  ? 53  ASN J C   1 
ATOM   10262 O  O   . ASN J  1 54  ? 31.517  205.167 57.165  1.00 37.11  ? 53  ASN J O   1 
ATOM   10263 C  CB  . ASN J  1 54  ? 33.241  203.982 55.184  1.00 46.53  ? 53  ASN J CB  1 
ATOM   10264 C  CG  . ASN J  1 54  ? 33.569  203.445 56.549  1.00 58.56  ? 53  ASN J CG  1 
ATOM   10265 O  OD1 . ASN J  1 54  ? 33.311  202.271 56.841  1.00 61.79  ? 53  ASN J OD1 1 
ATOM   10266 N  ND2 . ASN J  1 54  ? 34.113  204.320 57.433  1.00 62.45  ? 53  ASN J ND2 1 
ATOM   10267 N  N   . THR J  1 55  ? 30.205  205.940 55.502  1.00 43.53  ? 54  THR J N   1 
ATOM   10268 C  CA  . THR J  1 55  ? 29.582  206.973 56.403  1.00 44.00  ? 54  THR J CA  1 
ATOM   10269 C  C   . THR J  1 55  ? 28.864  206.330 57.594  1.00 43.27  ? 54  THR J C   1 
ATOM   10270 O  O   . THR J  1 55  ? 28.915  206.826 58.723  1.00 43.71  ? 54  THR J O   1 
ATOM   10271 C  CB  . THR J  1 55  ? 28.563  207.814 55.665  1.00 46.64  ? 54  THR J CB  1 
ATOM   10272 O  OG1 . THR J  1 55  ? 27.592  206.906 55.144  1.00 51.71  ? 54  THR J OG1 1 
ATOM   10273 C  CG2 . THR J  1 55  ? 29.178  208.589 54.477  1.00 44.86  ? 54  THR J CG2 1 
ATOM   10274 N  N   . ALA J  1 56  ? 28.229  205.190 57.365  1.00 45.43  ? 55  ALA J N   1 
ATOM   10275 C  CA  . ALA J  1 56  ? 27.598  204.463 58.468  1.00 46.04  ? 55  ALA J CA  1 
ATOM   10276 C  C   . ALA J  1 56  ? 28.438  203.186 58.831  1.00 47.25  ? 55  ALA J C   1 
ATOM   10277 O  O   . ALA J  1 56  ? 27.889  202.090 59.008  1.00 50.61  ? 55  ALA J O   1 
ATOM   10278 C  CB  . ALA J  1 56  ? 26.169  204.115 58.030  1.00 44.11  ? 55  ALA J CB  1 
ATOM   10279 N  N   . GLY J  1 57  ? 29.762  203.322 58.946  1.00 44.32  ? 56  GLY J N   1 
ATOM   10280 C  CA  . GLY J  1 57  ? 30.664  202.171 58.890  1.00 43.43  ? 56  GLY J CA  1 
ATOM   10281 C  C   . GLY J  1 57  ? 30.386  201.125 57.753  1.00 43.58  ? 56  GLY J C   1 
ATOM   10282 O  O   . GLY J  1 57  ? 29.996  201.467 56.644  1.00 44.89  ? 56  GLY J O   1 
ATOM   10283 N  N   . CYS J  1 58  ? 30.554  199.846 58.067  1.00 41.66  ? 57  CYS J N   1 
ATOM   10284 C  CA  . CYS J  1 58  ? 30.545  198.790 57.078  1.00 41.47  ? 57  CYS J CA  1 
ATOM   10285 C  C   . CYS J  1 58  ? 29.179  198.583 56.385  1.00 41.81  ? 57  CYS J C   1 
ATOM   10286 O  O   . CYS J  1 58  ? 29.128  198.255 55.181  1.00 41.44  ? 57  CYS J O   1 
ATOM   10287 C  CB  . CYS J  1 58  ? 31.102  197.507 57.710  1.00 45.32  ? 57  CYS J CB  1 
ATOM   10288 S  SG  . CYS J  1 58  ? 32.903  197.443 58.015  1.00 46.13  ? 57  CYS J SG  1 
ATOM   10289 N  N   . THR J  1 59  ? 28.104  198.859 57.116  1.00 39.43  ? 58  THR J N   1 
ATOM   10290 C  CA  . THR J  1 59  ? 26.739  198.864 56.598  1.00 39.48  ? 58  THR J CA  1 
ATOM   10291 C  C   . THR J  1 59  ? 26.498  199.725 55.393  1.00 38.00  ? 58  THR J C   1 
ATOM   10292 O  O   . THR J  1 59  ? 25.725  199.314 54.554  1.00 42.04  ? 58  THR J O   1 
ATOM   10293 C  CB  . THR J  1 59  ? 25.752  199.338 57.669  1.00 46.12  ? 58  THR J CB  1 
ATOM   10294 O  OG1 . THR J  1 59  ? 25.994  198.561 58.852  1.00 47.49  ? 58  THR J OG1 1 
ATOM   10295 C  CG2 . THR J  1 59  ? 24.263  199.180 57.169  1.00 44.52  ? 58  THR J CG2 1 
ATOM   10296 N  N   . SER J  1 60  ? 27.141  200.885 55.241  1.00 39.18  ? 59  SER J N   1 
ATOM   10297 C  CA  . SER J  1 60  ? 26.865  201.649 54.015  1.00 36.46  ? 59  SER J CA  1 
ATOM   10298 C  C   . SER J  1 60  ? 27.542  201.084 52.776  1.00 41.19  ? 59  SER J C   1 
ATOM   10299 O  O   . SER J  1 60  ? 27.389  201.675 51.708  1.00 44.33  ? 59  SER J O   1 
ATOM   10300 C  CB  . SER J  1 60  ? 27.072  203.161 54.136  1.00 38.12  ? 59  SER J CB  1 
ATOM   10301 O  OG  . SER J  1 60  ? 28.003  203.554 55.120  1.00 44.75  ? 59  SER J OG  1 
ATOM   10302 N  N   . ALA J  1 61  ? 28.234  199.921 52.873  1.00 43.98  ? 60  ALA J N   1 
ATOM   10303 C  CA  . ALA J  1 61  ? 28.969  199.350 51.725  1.00 37.57  ? 60  ALA J CA  1 
ATOM   10304 C  C   . ALA J  1 61  ? 28.032  198.631 50.820  1.00 40.39  ? 60  ALA J C   1 
ATOM   10305 O  O   . ALA J  1 61  ? 28.338  198.392 49.639  1.00 41.85  ? 60  ALA J O   1 
ATOM   10306 C  CB  . ALA J  1 61  ? 30.055  198.423 52.187  1.00 45.88  ? 60  ALA J CB  1 
ATOM   10307 N  N   . GLY J  1 62  ? 26.870  198.278 51.345  1.00 41.36  ? 61  GLY J N   1 
ATOM   10308 C  CA  . GLY J  1 62  ? 25.823  197.758 50.460  1.00 42.86  ? 61  GLY J CA  1 
ATOM   10309 C  C   . GLY J  1 62  ? 25.921  196.254 50.351  1.00 40.75  ? 61  GLY J C   1 
ATOM   10310 O  O   . GLY J  1 62  ? 26.536  195.640 51.222  1.00 40.57  ? 61  GLY J O   1 
ATOM   10311 N  N   . PRO J  1 63  ? 25.247  195.642 49.344  1.00 42.50  ? 62  PRO J N   1 
ATOM   10312 C  CA  . PRO J  1 63  ? 25.370  194.169 49.245  1.00 42.13  ? 62  PRO J CA  1 
ATOM   10313 C  C   . PRO J  1 63  ? 26.676  193.768 48.554  1.00 44.59  ? 62  PRO J C   1 
ATOM   10314 O  O   . PRO J  1 63  ? 27.520  194.615 48.191  1.00 46.56  ? 62  PRO J O   1 
ATOM   10315 C  CB  . PRO J  1 63  ? 24.156  193.776 48.424  1.00 38.74  ? 62  PRO J CB  1 
ATOM   10316 C  CG  . PRO J  1 63  ? 23.947  194.943 47.509  1.00 38.43  ? 62  PRO J CG  1 
ATOM   10317 C  CD  . PRO J  1 63  ? 24.350  196.178 48.304  1.00 38.62  ? 62  PRO J CD  1 
ATOM   10318 N  N   . HIS J  1 64  ? 26.881  192.481 48.392  1.00 45.56  ? 63  HIS J N   1 
ATOM   10319 C  CA  . HIS J  1 64  ? 28.032  192.022 47.611  1.00 45.84  ? 63  HIS J CA  1 
ATOM   10320 C  C   . HIS J  1 64  ? 27.999  192.622 46.208  1.00 41.35  ? 63  HIS J C   1 
ATOM   10321 O  O   . HIS J  1 64  ? 26.942  192.825 45.645  1.00 39.59  ? 63  HIS J O   1 
ATOM   10322 C  CB  . HIS J  1 64  ? 28.010  190.493 47.500  1.00 48.73  ? 63  HIS J CB  1 
ATOM   10323 C  CG  . HIS J  1 64  ? 28.218  189.766 48.799  1.00 45.81  ? 63  HIS J CG  1 
ATOM   10324 N  ND1 . HIS J  1 64  ? 28.302  188.396 48.852  1.00 42.56  ? 63  HIS J ND1 1 
ATOM   10325 C  CD2 . HIS J  1 64  ? 28.399  190.198 50.072  1.00 45.34  ? 63  HIS J CD2 1 
ATOM   10326 C  CE1 . HIS J  1 64  ? 28.451  188.008 50.106  1.00 46.42  ? 63  HIS J CE1 1 
ATOM   10327 N  NE2 . HIS J  1 64  ? 28.514  189.080 50.871  1.00 42.55  ? 63  HIS J NE2 1 
ATOM   10328 N  N   . PHE J  1 65  ? 29.164  192.903 45.658  1.00 41.94  ? 64  PHE J N   1 
ATOM   10329 C  CA  . PHE J  1 65  ? 29.230  193.457 44.333  1.00 42.61  ? 64  PHE J CA  1 
ATOM   10330 C  C   . PHE J  1 65  ? 28.645  192.507 43.233  1.00 48.59  ? 64  PHE J C   1 
ATOM   10331 O  O   . PHE J  1 65  ? 29.139  191.398 42.927  1.00 51.42  ? 64  PHE J O   1 
ATOM   10332 C  CB  . PHE J  1 65  ? 30.658  193.859 44.082  1.00 42.18  ? 64  PHE J CB  1 
ATOM   10333 C  CG  . PHE J  1 65  ? 30.874  194.499 42.765  1.00 45.59  ? 64  PHE J CG  1 
ATOM   10334 C  CD1 . PHE J  1 65  ? 30.036  195.535 42.333  1.00 49.61  ? 64  PHE J CD1 1 
ATOM   10335 C  CD2 . PHE J  1 65  ? 31.946  194.108 41.958  1.00 47.22  ? 64  PHE J CD2 1 
ATOM   10336 C  CE1 . PHE J  1 65  ? 30.217  196.130 41.090  1.00 51.25  ? 64  PHE J CE1 1 
ATOM   10337 C  CE2 . PHE J  1 65  ? 32.176  194.727 40.726  1.00 48.35  ? 64  PHE J CE2 1 
ATOM   10338 C  CZ  . PHE J  1 65  ? 31.304  195.742 40.293  1.00 52.29  ? 64  PHE J CZ  1 
ATOM   10339 N  N   . ASN J  1 66  ? 27.546  192.922 42.648  1.00 48.09  ? 65  ASN J N   1 
ATOM   10340 C  CA  . ASN J  1 66  ? 26.810  191.966 41.849  1.00 46.80  ? 65  ASN J CA  1 
ATOM   10341 C  C   . ASN J  1 66  ? 26.355  192.463 40.416  1.00 43.72  ? 65  ASN J C   1 
ATOM   10342 O  O   . ASN J  1 66  ? 25.297  192.122 39.976  1.00 42.17  ? 65  ASN J O   1 
ATOM   10343 C  CB  . ASN J  1 66  ? 25.693  191.403 42.752  1.00 44.08  ? 65  ASN J CB  1 
ATOM   10344 C  CG  . ASN J  1 66  ? 24.971  190.226 42.158  1.00 49.57  ? 65  ASN J CG  1 
ATOM   10345 O  OD1 . ASN J  1 66  ? 25.528  189.442 41.352  1.00 51.30  ? 65  ASN J OD1 1 
ATOM   10346 N  ND2 . ASN J  1 66  ? 23.690  190.112 42.514  1.00 46.60  ? 65  ASN J ND2 1 
ATOM   10347 N  N   . PRO J  1 67  ? 27.243  193.123 39.630  1.00 45.75  ? 66  PRO J N   1 
ATOM   10348 C  CA  . PRO J  1 67  ? 26.739  193.717 38.380  1.00 45.80  ? 66  PRO J CA  1 
ATOM   10349 C  C   . PRO J  1 67  ? 26.073  192.715 37.452  1.00 51.68  ? 66  PRO J C   1 
ATOM   10350 O  O   . PRO J  1 67  ? 25.213  193.125 36.675  1.00 57.02  ? 66  PRO J O   1 
ATOM   10351 C  CB  . PRO J  1 67  ? 27.971  194.275 37.684  1.00 44.11  ? 66  PRO J CB  1 
ATOM   10352 C  CG  . PRO J  1 67  ? 29.154  193.680 38.393  1.00 44.73  ? 66  PRO J CG  1 
ATOM   10353 C  CD  . PRO J  1 67  ? 28.726  193.005 39.655  1.00 45.23  ? 66  PRO J CD  1 
ATOM   10354 N  N   . LEU J  1 68  ? 26.411  191.426 37.538  1.00 54.84  ? 67  LEU J N   1 
ATOM   10355 C  CA  . LEU J  1 68  ? 25.698  190.394 36.698  1.00 53.52  ? 67  LEU J CA  1 
ATOM   10356 C  C   . LEU J  1 68  ? 24.384  189.881 37.284  1.00 50.92  ? 67  LEU J C   1 
ATOM   10357 O  O   . LEU J  1 68  ? 23.727  189.077 36.662  1.00 48.65  ? 67  LEU J O   1 
ATOM   10358 C  CB  . LEU J  1 68  ? 26.650  189.247 36.236  1.00 55.31  ? 67  LEU J CB  1 
ATOM   10359 C  CG  . LEU J  1 68  ? 27.809  189.780 35.304  1.00 62.19  ? 67  LEU J CG  1 
ATOM   10360 C  CD1 . LEU J  1 68  ? 28.871  188.716 34.947  1.00 59.53  ? 67  LEU J CD1 1 
ATOM   10361 C  CD2 . LEU J  1 68  ? 27.278  190.504 34.016  1.00 58.52  ? 67  LEU J CD2 1 
ATOM   10362 N  N   . SER J  1 69  ? 23.968  190.364 38.464  1.00 47.79  ? 68  SER J N   1 
ATOM   10363 C  CA  . SER J  1 69  ? 22.749  189.820 39.130  1.00 51.28  ? 68  SER J CA  1 
ATOM   10364 C  C   . SER J  1 69  ? 22.639  188.283 39.152  1.00 59.85  ? 68  SER J C   1 
ATOM   10365 O  O   . SER J  1 69  ? 21.568  187.730 38.741  1.00 58.03  ? 68  SER J O   1 
ATOM   10366 C  CB  . SER J  1 69  ? 21.447  190.314 38.487  1.00 54.97  ? 68  SER J CB  1 
ATOM   10367 O  OG  . SER J  1 69  ? 21.741  191.391 37.628  1.00 63.62  ? 68  SER J OG  1 
ATOM   10368 N  N   . ARG J  1 70  ? 23.698  187.620 39.653  1.00 50.32  ? 69  ARG J N   1 
ATOM   10369 C  CA  . ARG J  1 70  ? 23.715  186.160 39.846  1.00 53.41  ? 69  ARG J CA  1 
ATOM   10370 C  C   . ARG J  1 70  ? 23.399  185.888 41.330  1.00 53.65  ? 69  ARG J C   1 
ATOM   10371 O  O   . ARG J  1 70  ? 23.502  186.829 42.100  1.00 52.49  ? 69  ARG J O   1 
ATOM   10372 C  CB  . ARG J  1 70  ? 25.087  185.615 39.458  1.00 48.74  ? 69  ARG J CB  1 
ATOM   10373 C  CG  . ARG J  1 70  ? 25.414  185.963 38.037  1.00 51.54  ? 69  ARG J CG  1 
ATOM   10374 C  CD  . ARG J  1 70  ? 24.675  185.083 37.035  1.00 59.05  ? 69  ARG J CD  1 
ATOM   10375 N  NE  . ARG J  1 70  ? 25.438  185.117 35.764  1.00 68.38  ? 69  ARG J NE  1 
ATOM   10376 C  CZ  . ARG J  1 70  ? 26.719  184.686 35.592  1.00 71.19  ? 69  ARG J CZ  1 
ATOM   10377 N  NH1 . ARG J  1 70  ? 27.429  184.136 36.579  1.00 57.70  ? 69  ARG J NH1 1 
ATOM   10378 N  NH2 . ARG J  1 70  ? 27.322  184.790 34.399  1.00 72.40  ? 69  ARG J NH2 1 
ATOM   10379 N  N   . LYS J  1 71  ? 22.999  184.652 41.718  1.00 50.94  ? 70  LYS J N   1 
ATOM   10380 C  CA  . LYS J  1 71  ? 23.023  184.177 43.138  1.00 46.40  ? 70  LYS J CA  1 
ATOM   10381 C  C   . LYS J  1 71  ? 24.445  184.092 43.657  1.00 44.37  ? 70  LYS J C   1 
ATOM   10382 O  O   . LYS J  1 71  ? 25.436  184.170 42.870  1.00 42.25  ? 70  LYS J O   1 
ATOM   10383 C  CB  . LYS J  1 71  ? 22.317  182.846 43.320  1.00 43.22  ? 70  LYS J CB  1 
ATOM   10384 C  CG  . LYS J  1 71  ? 21.231  182.722 42.274  1.00 52.74  ? 70  LYS J CG  1 
ATOM   10385 C  CD  . LYS J  1 71  ? 19.968  182.048 42.760  1.00 57.75  ? 70  LYS J CD  1 
ATOM   10386 C  CE  . LYS J  1 71  ? 18.884  183.115 42.936  1.00 68.96  ? 70  LYS J CE  1 
ATOM   10387 N  NZ  . LYS J  1 71  ? 17.830  182.802 43.966  1.00 69.32  ? 70  LYS J NZ  1 
ATOM   10388 N  N   . HIS J  1 72  ? 24.550  183.940 44.979  1.00 42.85  ? 71  HIS J N   1 
ATOM   10389 C  CA  . HIS J  1 72  ? 25.846  184.021 45.663  1.00 43.22  ? 71  HIS J CA  1 
ATOM   10390 C  C   . HIS J  1 72  ? 26.480  182.625 45.671  1.00 45.33  ? 71  HIS J C   1 
ATOM   10391 O  O   . HIS J  1 72  ? 25.780  181.669 45.971  1.00 47.31  ? 71  HIS J O   1 
ATOM   10392 C  CB  . HIS J  1 72  ? 25.611  184.522 47.090  1.00 42.58  ? 71  HIS J CB  1 
ATOM   10393 C  CG  . HIS J  1 72  ? 26.733  184.234 48.028  1.00 40.47  ? 71  HIS J CG  1 
ATOM   10394 N  ND1 . HIS J  1 72  ? 27.808  185.089 48.202  1.00 38.09  ? 71  HIS J ND1 1 
ATOM   10395 C  CD2 . HIS J  1 72  ? 26.984  183.154 48.794  1.00 39.55  ? 71  HIS J CD2 1 
ATOM   10396 C  CE1 . HIS J  1 72  ? 28.645  184.584 49.083  1.00 37.07  ? 71  HIS J CE1 1 
ATOM   10397 N  NE2 . HIS J  1 72  ? 28.175  183.396 49.443  1.00 47.92  ? 71  HIS J NE2 1 
ATOM   10398 N  N   . GLY J  1 73  ? 27.775  182.508 45.366  1.00 41.58  ? 72  GLY J N   1 
ATOM   10399 C  CA  . GLY J  1 73  ? 28.451  181.210 45.381  1.00 38.87  ? 72  GLY J CA  1 
ATOM   10400 C  C   . GLY J  1 73  ? 29.857  181.309 45.954  1.00 44.28  ? 72  GLY J C   1 
ATOM   10401 O  O   . GLY J  1 73  ? 30.200  182.274 46.679  1.00 40.77  ? 72  GLY J O   1 
ATOM   10402 N  N   . GLY J  1 74  ? 30.673  180.289 45.669  1.00 43.51  ? 73  GLY J N   1 
ATOM   10403 C  CA  . GLY J  1 74  ? 32.080  180.290 46.081  1.00 38.48  ? 73  GLY J CA  1 
ATOM   10404 C  C   . GLY J  1 74  ? 32.870  180.811 44.902  1.00 41.05  ? 73  GLY J C   1 
ATOM   10405 O  O   . GLY J  1 74  ? 32.374  180.815 43.765  1.00 41.25  ? 73  GLY J O   1 
ATOM   10406 N  N   . PRO J  1 75  ? 34.088  181.274 45.154  1.00 40.40  ? 74  PRO J N   1 
ATOM   10407 C  CA  . PRO J  1 75  ? 34.889  181.873 44.100  1.00 42.00  ? 74  PRO J CA  1 
ATOM   10408 C  C   . PRO J  1 75  ? 35.067  180.927 42.919  1.00 48.87  ? 74  PRO J C   1 
ATOM   10409 O  O   . PRO J  1 75  ? 35.036  181.360 41.732  1.00 50.79  ? 74  PRO J O   1 
ATOM   10410 C  CB  . PRO J  1 75  ? 36.226  182.171 44.766  1.00 41.80  ? 74  PRO J CB  1 
ATOM   10411 C  CG  . PRO J  1 75  ? 36.130  181.641 46.165  1.00 40.62  ? 74  PRO J CG  1 
ATOM   10412 C  CD  . PRO J  1 75  ? 34.695  181.414 46.490  1.00 41.49  ? 74  PRO J CD  1 
ATOM   10413 N  N   . LYS J  1 76  ? 35.160  179.629 43.208  1.00 56.13  ? 75  LYS J N   1 
ATOM   10414 C  CA  . LYS J  1 76  ? 35.356  178.638 42.123  1.00 51.46  ? 75  LYS J CA  1 
ATOM   10415 C  C   . LYS J  1 76  ? 34.062  178.266 41.402  1.00 52.97  ? 75  LYS J C   1 
ATOM   10416 O  O   . LYS J  1 76  ? 34.147  177.604 40.379  1.00 52.69  ? 75  LYS J O   1 
ATOM   10417 C  CB  . LYS J  1 76  ? 36.173  177.431 42.602  1.00 51.52  ? 75  LYS J CB  1 
ATOM   10418 C  CG  . LYS J  1 76  ? 37.622  177.794 43.064  1.00 61.19  ? 75  LYS J CG  1 
ATOM   10419 C  CD  . LYS J  1 76  ? 38.275  176.718 44.008  1.00 64.44  ? 75  LYS J CD  1 
ATOM   10420 C  CE  . LYS J  1 76  ? 39.265  177.264 45.099  1.00 64.74  ? 75  LYS J CE  1 
ATOM   10421 N  NZ  . LYS J  1 76  ? 40.792  177.217 44.914  1.00 50.33  ? 75  LYS J NZ  1 
ATOM   10422 N  N   . ASP J  1 77  ? 32.883  178.698 41.888  1.00 48.13  ? 76  ASP J N   1 
ATOM   10423 C  CA  . ASP J  1 77  ? 31.608  178.515 41.127  1.00 46.77  ? 76  ASP J CA  1 
ATOM   10424 C  C   . ASP J  1 77  ? 31.400  179.461 39.935  1.00 52.67  ? 76  ASP J C   1 
ATOM   10425 O  O   . ASP J  1 77  ? 31.967  180.553 39.844  1.00 46.86  ? 76  ASP J O   1 
ATOM   10426 C  CB  . ASP J  1 77  ? 30.376  178.618 42.059  1.00 50.39  ? 76  ASP J CB  1 
ATOM   10427 C  CG  . ASP J  1 77  ? 30.448  177.633 43.202  1.00 51.17  ? 76  ASP J CG  1 
ATOM   10428 O  OD1 . ASP J  1 77  ? 31.068  176.573 42.915  1.00 50.66  ? 76  ASP J OD1 1 
ATOM   10429 O  OD2 . ASP J  1 77  ? 29.962  177.917 44.353  1.00 46.20  ? 76  ASP J OD2 1 
ATOM   10430 N  N   . GLU J  1 78  ? 30.567  179.035 38.997  1.00 56.26  ? 77  GLU J N   1 
ATOM   10431 C  CA  . GLU J  1 78  ? 30.333  179.867 37.825  1.00 52.60  ? 77  GLU J CA  1 
ATOM   10432 C  C   . GLU J  1 78  ? 29.173  180.745 38.264  1.00 50.91  ? 77  GLU J C   1 
ATOM   10433 O  O   . GLU J  1 78  ? 29.157  181.962 38.005  1.00 57.00  ? 77  GLU J O   1 
ATOM   10434 C  CB  . GLU J  1 78  ? 29.967  179.003 36.599  1.00 55.93  ? 77  GLU J CB  1 
ATOM   10435 C  CG  . GLU J  1 78  ? 30.304  179.630 35.238  1.00 66.44  ? 77  GLU J CG  1 
ATOM   10436 C  CD  . GLU J  1 78  ? 29.106  179.507 34.278  1.00 85.39  ? 77  GLU J CD  1 
ATOM   10437 O  OE1 . GLU J  1 78  ? 29.064  178.535 33.460  1.00 70.27  ? 77  GLU J OE1 1 
ATOM   10438 O  OE2 . GLU J  1 78  ? 28.158  180.360 34.384  1.00 82.41  ? 77  GLU J OE2 1 
ATOM   10439 N  N   . GLU J  1 79  ? 28.209  180.151 38.963  1.00 45.22  ? 78  GLU J N   1 
ATOM   10440 C  CA  . GLU J  1 79  ? 27.143  180.942 39.587  1.00 45.18  ? 78  GLU J CA  1 
ATOM   10441 C  C   . GLU J  1 79  ? 27.692  181.635 40.868  1.00 48.85  ? 78  GLU J C   1 
ATOM   10442 O  O   . GLU J  1 79  ? 27.674  181.044 41.982  1.00 45.73  ? 78  GLU J O   1 
ATOM   10443 C  CB  . GLU J  1 79  ? 25.910  180.066 39.883  1.00 43.79  ? 78  GLU J CB  1 
ATOM   10444 C  CG  . GLU J  1 79  ? 24.686  180.835 40.400  1.00 49.33  ? 78  GLU J CG  1 
ATOM   10445 C  CD  . GLU J  1 79  ? 23.958  181.680 39.333  1.00 54.56  ? 78  GLU J CD  1 
ATOM   10446 O  OE1 . GLU J  1 79  ? 24.342  181.707 38.116  1.00 60.94  ? 78  GLU J OE1 1 
ATOM   10447 O  OE2 . GLU J  1 79  ? 22.984  182.348 39.719  1.00 50.04  ? 78  GLU J OE2 1 
ATOM   10448 N  N   . ARG J  1 80  ? 28.224  182.856 40.690  1.00 43.59  ? 79  ARG J N   1 
ATOM   10449 C  CA  . ARG J  1 80  ? 28.690  183.667 41.816  1.00 43.46  ? 79  ARG J CA  1 
ATOM   10450 C  C   . ARG J  1 80  ? 28.519  185.182 41.508  1.00 48.65  ? 79  ARG J C   1 
ATOM   10451 O  O   . ARG J  1 80  ? 28.423  185.597 40.306  1.00 44.58  ? 79  ARG J O   1 
ATOM   10452 C  CB  . ARG J  1 80  ? 30.151  183.382 42.095  1.00 37.96  ? 79  ARG J CB  1 
ATOM   10453 C  CG  . ARG J  1 80  ? 30.983  183.678 40.877  1.00 36.39  ? 79  ARG J CG  1 
ATOM   10454 C  CD  . ARG J  1 80  ? 32.464  183.625 41.173  1.00 36.91  ? 79  ARG J CD  1 
ATOM   10455 N  NE  . ARG J  1 80  ? 32.929  184.845 41.737  1.00 37.15  ? 79  ARG J NE  1 
ATOM   10456 C  CZ  . ARG J  1 80  ? 34.198  185.099 42.032  1.00 45.23  ? 79  ARG J CZ  1 
ATOM   10457 N  NH1 . ARG J  1 80  ? 35.160  184.203 41.778  1.00 44.38  ? 79  ARG J NH1 1 
ATOM   10458 N  NH2 . ARG J  1 80  ? 34.522  186.295 42.548  1.00 46.18  ? 79  ARG J NH2 1 
ATOM   10459 N  N   . HIS J  1 81  ? 28.499  185.970 42.594  1.00 41.91  ? 80  HIS J N   1 
ATOM   10460 C  CA  . HIS J  1 81  ? 28.637  187.419 42.552  1.00 42.66  ? 80  HIS J CA  1 
ATOM   10461 C  C   . HIS J  1 81  ? 30.072  187.736 42.214  1.00 45.31  ? 80  HIS J C   1 
ATOM   10462 O  O   . HIS J  1 81  ? 31.004  186.991 42.650  1.00 47.24  ? 80  HIS J O   1 
ATOM   10463 C  CB  . HIS J  1 81  ? 28.316  188.103 43.905  1.00 42.12  ? 80  HIS J CB  1 
ATOM   10464 C  CG  . HIS J  1 81  ? 26.932  187.836 44.440  1.00 38.76  ? 80  HIS J CG  1 
ATOM   10465 N  ND1 . HIS J  1 81  ? 26.662  187.777 45.794  1.00 38.02  ? 80  HIS J ND1 1 
ATOM   10466 C  CD2 . HIS J  1 81  ? 25.748  187.606 43.818  1.00 38.47  ? 80  HIS J CD2 1 
ATOM   10467 C  CE1 . HIS J  1 81  ? 25.380  187.493 45.979  1.00 39.76  ? 80  HIS J CE1 1 
ATOM   10468 N  NE2 . HIS J  1 81  ? 24.802  187.384 44.795  1.00 37.68  ? 80  HIS J NE2 1 
ATOM   10469 N  N   . VAL J  1 82  ? 30.258  188.823 41.450  1.00 41.74  ? 81  VAL J N   1 
ATOM   10470 C  CA  . VAL J  1 82  ? 31.606  189.285 41.091  1.00 43.11  ? 81  VAL J CA  1 
ATOM   10471 C  C   . VAL J  1 82  ? 32.449  189.373 42.401  1.00 43.97  ? 81  VAL J C   1 
ATOM   10472 O  O   . VAL J  1 82  ? 33.543  188.768 42.517  1.00 40.41  ? 81  VAL J O   1 
ATOM   10473 C  CB  . VAL J  1 82  ? 31.638  190.627 40.296  1.00 41.68  ? 81  VAL J CB  1 
ATOM   10474 C  CG1 . VAL J  1 82  ? 33.058  191.091 40.136  1.00 39.88  ? 81  VAL J CG1 1 
ATOM   10475 C  CG2 . VAL J  1 82  ? 31.015  190.518 38.903  1.00 40.16  ? 81  VAL J CG2 1 
ATOM   10476 N  N   . GLY J  1 83  ? 31.885  190.031 43.399  1.00 37.43  ? 82  GLY J N   1 
ATOM   10477 C  CA  . GLY J  1 83  ? 32.569  190.095 44.690  1.00 40.95  ? 82  GLY J CA  1 
ATOM   10478 C  C   . GLY J  1 83  ? 32.704  188.891 45.611  1.00 37.55  ? 82  GLY J C   1 
ATOM   10479 O  O   . GLY J  1 83  ? 33.306  189.005 46.660  1.00 39.39  ? 82  GLY J O   1 
ATOM   10480 N  N   . ASP J  1 84  ? 32.175  187.732 45.242  1.00 42.82  ? 83  ASP J N   1 
ATOM   10481 C  CA  . ASP J  1 84  ? 32.367  186.496 46.079  1.00 48.07  ? 83  ASP J CA  1 
ATOM   10482 C  C   . ASP J  1 84  ? 33.785  185.912 46.151  1.00 43.02  ? 83  ASP J C   1 
ATOM   10483 O  O   . ASP J  1 84  ? 34.149  185.132 45.324  1.00 45.94  ? 83  ASP J O   1 
ATOM   10484 C  CB  . ASP J  1 84  ? 31.381  185.378 45.658  1.00 44.15  ? 83  ASP J CB  1 
ATOM   10485 C  CG  . ASP J  1 84  ? 29.974  185.795 45.847  1.00 43.17  ? 83  ASP J CG  1 
ATOM   10486 O  OD1 . ASP J  1 84  ? 29.807  186.749 46.644  1.00 48.42  ? 83  ASP J OD1 1 
ATOM   10487 O  OD2 . ASP J  1 84  ? 29.060  185.216 45.236  1.00 41.68  ? 83  ASP J OD2 1 
ATOM   10488 N  N   . LEU J  1 85  ? 34.559  186.233 47.152  1.00 39.03  ? 84  LEU J N   1 
ATOM   10489 C  CA  . LEU J  1 85  ? 35.898  185.690 47.162  1.00 40.03  ? 84  LEU J CA  1 
ATOM   10490 C  C   . LEU J  1 85  ? 36.045  184.653 48.219  1.00 41.07  ? 84  LEU J C   1 
ATOM   10491 O  O   . LEU J  1 85  ? 37.165  184.450 48.685  1.00 47.89  ? 84  LEU J O   1 
ATOM   10492 C  CB  . LEU J  1 85  ? 36.908  186.788 47.478  1.00 37.25  ? 84  LEU J CB  1 
ATOM   10493 C  CG  . LEU J  1 85  ? 37.108  187.931 46.466  1.00 37.75  ? 84  LEU J CG  1 
ATOM   10494 C  CD1 . LEU J  1 85  ? 38.036  188.983 47.064  1.00 34.43  ? 84  LEU J CD1 1 
ATOM   10495 C  CD2 . LEU J  1 85  ? 37.668  187.488 45.133  1.00 37.14  ? 84  LEU J CD2 1 
ATOM   10496 N  N   . GLY J  1 86  ? 34.929  184.093 48.699  1.00 38.49  ? 85  GLY J N   1 
ATOM   10497 C  CA  . GLY J  1 86  ? 34.939  182.989 49.679  1.00 37.88  ? 85  GLY J CA  1 
ATOM   10498 C  C   . GLY J  1 86  ? 35.348  183.256 51.109  1.00 39.20  ? 85  GLY J C   1 
ATOM   10499 O  O   . GLY J  1 86  ? 34.842  184.176 51.743  1.00 41.46  ? 85  GLY J O   1 
ATOM   10500 N  N   . ASN J  1 87  ? 36.227  182.429 51.665  1.00 37.99  ? 86  ASN J N   1 
ATOM   10501 C  CA  . ASN J  1 87  ? 36.546  182.612 53.061  1.00 35.08  ? 86  ASN J CA  1 
ATOM   10502 C  C   . ASN J  1 87  ? 38.018  182.800 53.121  1.00 37.93  ? 86  ASN J C   1 
ATOM   10503 O  O   . ASN J  1 87  ? 38.749  182.371 52.201  1.00 39.09  ? 86  ASN J O   1 
ATOM   10504 C  CB  . ASN J  1 87  ? 36.182  181.388 53.896  1.00 39.59  ? 86  ASN J CB  1 
ATOM   10505 C  CG  . ASN J  1 87  ? 34.686  181.222 54.080  1.00 47.02  ? 86  ASN J CG  1 
ATOM   10506 O  OD1 . ASN J  1 87  ? 34.088  181.853 54.991  1.00 51.75  ? 86  ASN J OD1 1 
ATOM   10507 N  ND2 . ASN J  1 87  ? 34.047  180.385 53.224  1.00 39.18  ? 86  ASN J ND2 1 
ATOM   10508 N  N   . VAL J  1 88  ? 38.440  183.444 54.209  1.00 39.58  ? 87  VAL J N   1 
ATOM   10509 C  CA  . VAL J  1 88  ? 39.791  183.385 54.735  1.00 37.63  ? 87  VAL J CA  1 
ATOM   10510 C  C   . VAL J  1 88  ? 39.842  182.751 56.137  1.00 37.72  ? 87  VAL J C   1 
ATOM   10511 O  O   . VAL J  1 88  ? 38.838  182.573 56.858  1.00 39.60  ? 87  VAL J O   1 
ATOM   10512 C  CB  . VAL J  1 88  ? 40.475  184.770 54.710  1.00 40.13  ? 87  VAL J CB  1 
ATOM   10513 C  CG1 . VAL J  1 88  ? 40.379  185.349 53.317  1.00 44.03  ? 87  VAL J CG1 1 
ATOM   10514 C  CG2 . VAL J  1 88  ? 39.893  185.697 55.736  1.00 34.20  ? 87  VAL J CG2 1 
ATOM   10515 N  N   . THR J  1 89  ? 41.041  182.381 56.527  1.00 40.42  ? 88  THR J N   1 
ATOM   10516 C  CA  . THR J  1 89  ? 41.182  181.527 57.696  1.00 39.35  ? 88  THR J CA  1 
ATOM   10517 C  C   . THR J  1 89  ? 42.132  182.189 58.685  1.00 44.66  ? 88  THR J C   1 
ATOM   10518 O  O   . THR J  1 89  ? 43.280  182.540 58.343  1.00 41.13  ? 88  THR J O   1 
ATOM   10519 C  CB  . THR J  1 89  ? 41.752  180.105 57.326  1.00 42.31  ? 88  THR J CB  1 
ATOM   10520 O  OG1 . THR J  1 89  ? 41.169  179.549 56.098  1.00 40.49  ? 88  THR J OG1 1 
ATOM   10521 C  CG2 . THR J  1 89  ? 41.613  179.126 58.533  1.00 40.34  ? 88  THR J CG2 1 
ATOM   10522 N  N   . ALA J  1 90  ? 41.665  182.344 59.915  1.00 44.91  ? 89  ALA J N   1 
ATOM   10523 C  CA  . ALA J  1 90  ? 42.542  182.767 60.978  1.00 45.82  ? 89  ALA J CA  1 
ATOM   10524 C  C   . ALA J  1 90  ? 43.064  181.581 61.821  1.00 53.39  ? 89  ALA J C   1 
ATOM   10525 O  O   . ALA J  1 90  ? 42.262  180.693 62.279  1.00 49.59  ? 89  ALA J O   1 
ATOM   10526 C  CB  . ALA J  1 90  ? 41.804  183.726 61.899  1.00 45.65  ? 89  ALA J CB  1 
ATOM   10527 N  N   . ASP J  1 91  ? 44.369  181.627 62.125  1.00 51.54  ? 90  ASP J N   1 
ATOM   10528 C  CA  . ASP J  1 91  ? 44.963  180.699 63.104  1.00 55.83  ? 90  ASP J CA  1 
ATOM   10529 C  C   . ASP J  1 91  ? 44.469  181.009 64.486  1.00 59.97  ? 90  ASP J C   1 
ATOM   10530 O  O   . ASP J  1 91  ? 43.675  181.950 64.697  1.00 55.54  ? 90  ASP J O   1 
ATOM   10531 C  CB  . ASP J  1 91  ? 46.505  180.703 63.101  1.00 54.19  ? 90  ASP J CB  1 
ATOM   10532 C  CG  . ASP J  1 91  ? 47.059  182.077 63.290  1.00 62.91  ? 90  ASP J CG  1 
ATOM   10533 O  OD1 . ASP J  1 91  ? 46.679  182.758 64.286  1.00 57.06  ? 90  ASP J OD1 1 
ATOM   10534 O  OD2 . ASP J  1 91  ? 47.858  182.495 62.418  1.00 61.27  ? 90  ASP J OD2 1 
ATOM   10535 N  N   . LYS J  1 92  ? 44.957  180.200 65.433  1.00 65.31  ? 91  LYS J N   1 
ATOM   10536 C  CA  . LYS J  1 92  ? 44.570  180.302 66.841  1.00 64.00  ? 91  LYS J CA  1 
ATOM   10537 C  C   . LYS J  1 92  ? 45.011  181.689 67.476  1.00 58.14  ? 91  LYS J C   1 
ATOM   10538 O  O   . LYS J  1 92  ? 44.456  182.132 68.492  1.00 51.90  ? 91  LYS J O   1 
ATOM   10539 C  CB  . LYS J  1 92  ? 45.144  179.073 67.564  1.00 67.35  ? 91  LYS J CB  1 
ATOM   10540 C  CG  . LYS J  1 92  ? 46.640  178.845 67.351  1.00 64.96  ? 91  LYS J CG  1 
ATOM   10541 C  CD  . LYS J  1 92  ? 47.253  177.942 68.448  1.00 64.75  ? 91  LYS J CD  1 
ATOM   10542 C  CE  . LYS J  1 92  ? 48.794  177.946 68.322  1.00 74.69  ? 91  LYS J CE  1 
ATOM   10543 N  NZ  . LYS J  1 92  ? 49.557  177.000 69.217  1.00 76.12  ? 91  LYS J NZ  1 
ATOM   10544 N  N   . ASP J  1 93  ? 45.992  182.344 66.847  1.00 53.21  ? 92  ASP J N   1 
ATOM   10545 C  CA  . ASP J  1 93  ? 46.355  183.777 67.101  1.00 60.46  ? 92  ASP J CA  1 
ATOM   10546 C  C   . ASP J  1 93  ? 45.535  184.884 66.357  1.00 64.18  ? 92  ASP J C   1 
ATOM   10547 O  O   . ASP J  1 93  ? 45.787  186.092 66.562  1.00 60.36  ? 92  ASP J O   1 
ATOM   10548 C  CB  . ASP J  1 93  ? 47.834  183.991 66.703  1.00 64.87  ? 92  ASP J CB  1 
ATOM   10549 C  CG  . ASP J  1 93  ? 48.775  183.402 67.709  1.00 68.93  ? 92  ASP J CG  1 
ATOM   10550 O  OD1 . ASP J  1 93  ? 48.552  183.709 68.933  1.00 68.28  ? 92  ASP J OD1 1 
ATOM   10551 O  OD2 . ASP J  1 93  ? 49.684  182.630 67.277  1.00 59.57  ? 92  ASP J OD2 1 
ATOM   10552 N  N   . GLY J  1 94  ? 44.644  184.485 65.440  1.00 53.22  ? 93  GLY J N   1 
ATOM   10553 C  CA  . GLY J  1 94  ? 43.576  185.383 64.980  1.00 52.24  ? 93  GLY J CA  1 
ATOM   10554 C  C   . GLY J  1 94  ? 44.057  186.147 63.801  1.00 53.74  ? 93  GLY J C   1 
ATOM   10555 O  O   . GLY J  1 94  ? 43.524  187.209 63.470  1.00 58.29  ? 93  GLY J O   1 
ATOM   10556 N  N   . VAL J  1 95  ? 45.090  185.605 63.180  1.00 48.14  ? 94  VAL J N   1 
ATOM   10557 C  CA  . VAL J  1 95  ? 45.684  186.207 62.025  1.00 45.55  ? 94  VAL J CA  1 
ATOM   10558 C  C   . VAL J  1 95  ? 45.232  185.325 60.868  1.00 51.12  ? 94  VAL J C   1 
ATOM   10559 O  O   . VAL J  1 95  ? 44.984  184.132 61.016  1.00 51.47  ? 94  VAL J O   1 
ATOM   10560 C  CB  . VAL J  1 95  ? 47.256  186.252 62.173  1.00 48.28  ? 94  VAL J CB  1 
ATOM   10561 C  CG1 . VAL J  1 95  ? 47.981  186.622 60.866  1.00 37.13  ? 94  VAL J CG1 1 
ATOM   10562 C  CG2 . VAL J  1 95  ? 47.678  187.109 63.410  1.00 47.13  ? 94  VAL J CG2 1 
ATOM   10563 N  N   . ALA J  1 96  ? 45.156  185.926 59.702  1.00 48.55  ? 95  ALA J N   1 
ATOM   10564 C  CA  . ALA J  1 96  ? 44.640  185.286 58.577  1.00 50.09  ? 95  ALA J CA  1 
ATOM   10565 C  C   . ALA J  1 96  ? 45.551  185.937 57.580  1.00 55.25  ? 95  ALA J C   1 
ATOM   10566 O  O   . ALA J  1 96  ? 45.430  187.156 57.334  1.00 56.84  ? 95  ALA J O   1 
ATOM   10567 C  CB  . ALA J  1 96  ? 43.156  185.674 58.344  1.00 43.34  ? 95  ALA J CB  1 
ATOM   10568 N  N   . ASP J  1 97  ? 46.496  185.154 57.055  1.00 46.95  ? 96  ASP J N   1 
ATOM   10569 C  CA  . ASP J  1 97  ? 47.272  185.624 55.929  1.00 50.99  ? 96  ASP J CA  1 
ATOM   10570 C  C   . ASP J  1 97  ? 46.450  185.294 54.732  1.00 54.52  ? 96  ASP J C   1 
ATOM   10571 O  O   . ASP J  1 97  ? 45.994  184.194 54.591  1.00 66.29  ? 96  ASP J O   1 
ATOM   10572 C  CB  . ASP J  1 97  ? 48.650  184.926 55.849  1.00 52.40  ? 96  ASP J CB  1 
ATOM   10573 C  CG  . ASP J  1 97  ? 49.455  185.180 57.093  1.00 61.24  ? 96  ASP J CG  1 
ATOM   10574 O  OD1 . ASP J  1 97  ? 50.113  186.280 57.092  1.00 54.80  ? 96  ASP J OD1 1 
ATOM   10575 O  OD2 . ASP J  1 97  ? 49.355  184.340 58.080  1.00 56.11  ? 96  ASP J OD2 1 
ATOM   10576 N  N   . VAL J  1 98  ? 46.261  186.225 53.837  1.00 49.72  ? 97  VAL J N   1 
ATOM   10577 C  CA  . VAL J  1 98  ? 45.361  185.939 52.774  1.00 45.73  ? 97  VAL J CA  1 
ATOM   10578 C  C   . VAL J  1 98  ? 46.217  185.802 51.561  1.00 47.75  ? 97  VAL J C   1 
ATOM   10579 O  O   . VAL J  1 98  ? 47.241  186.486 51.424  1.00 46.65  ? 97  VAL J O   1 
ATOM   10580 C  CB  . VAL J  1 98  ? 44.318  187.078 52.665  1.00 40.61  ? 97  VAL J CB  1 
ATOM   10581 C  CG1 . VAL J  1 98  ? 43.516  186.999 51.372  1.00 38.41  ? 97  VAL J CG1 1 
ATOM   10582 C  CG2 . VAL J  1 98  ? 43.463  187.044 53.925  1.00 39.07  ? 97  VAL J CG2 1 
ATOM   10583 N  N   . SER J  1 99  ? 45.792  184.910 50.684  1.00 46.07  ? 98  SER J N   1 
ATOM   10584 C  CA  . SER J  1 99  ? 46.446  184.763 49.450  1.00 47.32  ? 98  SER J CA  1 
ATOM   10585 C  C   . SER J  1 99  ? 45.469  184.039 48.572  1.00 46.47  ? 98  SER J C   1 
ATOM   10586 O  O   . SER J  1 99  ? 45.163  182.864 48.793  1.00 48.02  ? 98  SER J O   1 
ATOM   10587 C  CB  . SER J  1 99  ? 47.744  183.974 49.647  1.00 51.78  ? 98  SER J CB  1 
ATOM   10588 O  OG  . SER J  1 99  ? 48.493  184.050 48.464  1.00 53.58  ? 98  SER J OG  1 
ATOM   10589 N  N   . ILE J  1 100 ? 44.975  184.739 47.569  1.00 43.02  ? 99  ILE J N   1 
ATOM   10590 C  CA  . ILE J  1 100 ? 43.905  184.212 46.766  1.00 47.58  ? 99  ILE J CA  1 
ATOM   10591 C  C   . ILE J  1 100 ? 44.282  184.659 45.389  1.00 47.62  ? 99  ILE J C   1 
ATOM   10592 O  O   . ILE J  1 100 ? 44.905  185.705 45.224  1.00 46.74  ? 99  ILE J O   1 
ATOM   10593 C  CB  . ILE J  1 100 ? 42.536  184.841 47.273  1.00 51.07  ? 99  ILE J CB  1 
ATOM   10594 C  CG1 . ILE J  1 100 ? 41.894  183.997 48.396  1.00 52.13  ? 99  ILE J CG1 1 
ATOM   10595 C  CG2 . ILE J  1 100 ? 41.479  185.094 46.195  1.00 45.40  ? 99  ILE J CG2 1 
ATOM   10596 C  CD1 . ILE J  1 100 ? 40.942  184.801 49.305  1.00 53.56  ? 99  ILE J CD1 1 
ATOM   10597 N  N   . GLU J  1 101 ? 43.858  183.915 44.389  1.00 50.68  ? 100 GLU J N   1 
ATOM   10598 C  CA  . GLU J  1 101 ? 43.995  184.432 43.056  1.00 50.30  ? 100 GLU J CA  1 
ATOM   10599 C  C   . GLU J  1 101 ? 42.625  184.345 42.465  1.00 48.51  ? 100 GLU J C   1 
ATOM   10600 O  O   . GLU J  1 101 ? 41.977  183.317 42.625  1.00 47.12  ? 100 GLU J O   1 
ATOM   10601 C  CB  . GLU J  1 101 ? 45.030  183.593 42.299  1.00 54.87  ? 100 GLU J CB  1 
ATOM   10602 C  CG  . GLU J  1 101 ? 45.511  184.247 41.004  1.00 64.45  ? 100 GLU J CG  1 
ATOM   10603 C  CD  . GLU J  1 101 ? 46.882  183.734 40.493  1.00 67.35  ? 100 GLU J CD  1 
ATOM   10604 O  OE1 . GLU J  1 101 ? 47.772  183.368 41.341  1.00 52.00  ? 100 GLU J OE1 1 
ATOM   10605 O  OE2 . GLU J  1 101 ? 47.032  183.736 39.217  1.00 55.72  ? 100 GLU J OE2 1 
ATOM   10606 N  N   . ASP J  1 102 ? 42.139  185.433 41.850  1.00 47.00  ? 101 ASP J N   1 
ATOM   10607 C  CA  . ASP J  1 102 ? 40.781  185.423 41.269  1.00 46.41  ? 101 ASP J CA  1 
ATOM   10608 C  C   . ASP J  1 102 ? 40.780  186.105 39.910  1.00 47.54  ? 101 ASP J C   1 
ATOM   10609 O  O   . ASP J  1 102 ? 41.588  187.027 39.662  1.00 49.69  ? 101 ASP J O   1 
ATOM   10610 C  CB  . ASP J  1 102 ? 39.740  186.049 42.218  1.00 46.32  ? 101 ASP J CB  1 
ATOM   10611 C  CG  . ASP J  1 102 ? 38.296  185.753 41.777  1.00 50.72  ? 101 ASP J CG  1 
ATOM   10612 O  OD1 . ASP J  1 102 ? 37.814  184.644 42.039  1.00 55.03  ? 101 ASP J OD1 1 
ATOM   10613 O  OD2 . ASP J  1 102 ? 37.616  186.608 41.163  1.00 51.57  ? 101 ASP J OD2 1 
ATOM   10614 N  N   . SER J  1 103 ? 39.856  185.677 39.055  1.00 46.96  ? 102 SER J N   1 
ATOM   10615 C  CA  . SER J  1 103 ? 39.850  186.027 37.625  1.00 54.64  ? 102 SER J CA  1 
ATOM   10616 C  C   . SER J  1 103 ? 38.518  186.579 37.181  1.00 58.74  ? 102 SER J C   1 
ATOM   10617 O  O   . SER J  1 103 ? 38.299  186.811 35.967  1.00 54.92  ? 102 SER J O   1 
ATOM   10618 C  CB  . SER J  1 103 ? 40.220  184.808 36.748  1.00 57.97  ? 102 SER J CB  1 
ATOM   10619 O  OG  . SER J  1 103 ? 41.654  184.780 36.603  1.00 63.49  ? 102 SER J OG  1 
ATOM   10620 N  N   . VAL J  1 104 ? 37.648  186.804 38.171  1.00 53.57  ? 103 VAL J N   1 
ATOM   10621 C  CA  . VAL J  1 104 ? 36.332  187.383 37.951  1.00 51.30  ? 103 VAL J CA  1 
ATOM   10622 C  C   . VAL J  1 104 ? 36.421  188.860 38.376  1.00 52.62  ? 103 VAL J C   1 
ATOM   10623 O  O   . VAL J  1 104 ? 35.971  189.772 37.636  1.00 47.13  ? 103 VAL J O   1 
ATOM   10624 C  CB  . VAL J  1 104 ? 35.238  186.627 38.727  1.00 50.03  ? 103 VAL J CB  1 
ATOM   10625 C  CG1 . VAL J  1 104 ? 33.961  187.471 38.833  1.00 46.93  ? 103 VAL J CG1 1 
ATOM   10626 C  CG2 . VAL J  1 104 ? 34.997  185.271 38.050  1.00 52.20  ? 103 VAL J CG2 1 
ATOM   10627 N  N   . ILE J  1 105 ? 37.017  189.098 39.549  1.00 46.53  ? 104 ILE J N   1 
ATOM   10628 C  CA  . ILE J  1 105 ? 37.173  190.455 39.985  1.00 44.86  ? 104 ILE J CA  1 
ATOM   10629 C  C   . ILE J  1 105 ? 38.114  191.100 38.928  1.00 55.18  ? 104 ILE J C   1 
ATOM   10630 O  O   . ILE J  1 105 ? 38.722  190.353 38.094  1.00 59.32  ? 104 ILE J O   1 
ATOM   10631 C  CB  . ILE J  1 105 ? 37.630  190.576 41.467  1.00 42.38  ? 104 ILE J CB  1 
ATOM   10632 C  CG1 . ILE J  1 105 ? 38.943  189.864 41.805  1.00 42.41  ? 104 ILE J CG1 1 
ATOM   10633 C  CG2 . ILE J  1 105 ? 36.552  190.087 42.417  1.00 43.77  ? 104 ILE J CG2 1 
ATOM   10634 C  CD1 . ILE J  1 105 ? 39.629  190.429 43.062  1.00 35.35  ? 104 ILE J CD1 1 
ATOM   10635 N  N   . SER J  1 106 ? 38.178  192.445 38.890  1.00 53.84  ? 105 SER J N   1 
ATOM   10636 C  CA  . SER J  1 106 ? 39.146  193.177 38.067  1.00 47.97  ? 105 SER J CA  1 
ATOM   10637 C  C   . SER J  1 106 ? 39.593  194.498 38.654  1.00 49.88  ? 105 SER J C   1 
ATOM   10638 O  O   . SER J  1 106 ? 38.856  195.125 39.443  1.00 51.15  ? 105 SER J O   1 
ATOM   10639 C  CB  . SER J  1 106 ? 38.589  193.423 36.676  1.00 47.54  ? 105 SER J CB  1 
ATOM   10640 O  OG  . SER J  1 106 ? 39.693  193.698 35.797  1.00 52.85  ? 105 SER J OG  1 
ATOM   10641 N  N   . LEU J  1 107 ? 40.785  194.939 38.251  1.00 45.23  ? 106 LEU J N   1 
ATOM   10642 C  CA  . LEU J  1 107 ? 41.151  196.318 38.525  1.00 46.15  ? 106 LEU J CA  1 
ATOM   10643 C  C   . LEU J  1 107 ? 40.765  197.301 37.386  1.00 54.50  ? 106 LEU J C   1 
ATOM   10644 O  O   . LEU J  1 107 ? 41.087  198.485 37.471  1.00 53.34  ? 106 LEU J O   1 
ATOM   10645 C  CB  . LEU J  1 107 ? 42.609  196.431 38.942  1.00 41.57  ? 106 LEU J CB  1 
ATOM   10646 C  CG  . LEU J  1 107 ? 42.969  195.559 40.149  1.00 42.09  ? 106 LEU J CG  1 
ATOM   10647 C  CD1 . LEU J  1 107 ? 44.348  195.911 40.646  1.00 42.09  ? 106 LEU J CD1 1 
ATOM   10648 C  CD2 . LEU J  1 107 ? 42.005  195.639 41.330  1.00 39.33  ? 106 LEU J CD2 1 
ATOM   10649 N  N   . SER J  1 108 ? 40.044  196.835 36.358  1.00 46.80  ? 107 SER J N   1 
ATOM   10650 C  CA  . SER J  1 108 ? 39.559  197.716 35.326  1.00 49.37  ? 107 SER J CA  1 
ATOM   10651 C  C   . SER J  1 108 ? 38.233  197.194 34.657  1.00 57.03  ? 107 SER J C   1 
ATOM   10652 O  O   . SER J  1 108 ? 37.750  196.065 34.939  1.00 58.84  ? 107 SER J O   1 
ATOM   10653 C  CB  . SER J  1 108 ? 40.681  197.925 34.287  1.00 58.71  ? 107 SER J CB  1 
ATOM   10654 O  OG  . SER J  1 108 ? 40.627  196.911 33.272  1.00 58.85  ? 107 SER J OG  1 
ATOM   10655 N  N   . GLY J  1 109 ? 37.633  198.023 33.793  1.00 52.26  ? 108 GLY J N   1 
ATOM   10656 C  CA  . GLY J  1 109 ? 36.417  197.634 33.075  1.00 54.32  ? 108 GLY J CA  1 
ATOM   10657 C  C   . GLY J  1 109 ? 35.186  197.503 33.969  1.00 60.99  ? 108 GLY J C   1 
ATOM   10658 O  O   . GLY J  1 109 ? 35.181  198.027 35.096  1.00 57.46  ? 108 GLY J O   1 
ATOM   10659 N  N   . ASP J  1 110 ? 34.151  196.818 33.451  1.00 60.95  ? 109 ASP J N   1 
ATOM   10660 C  CA  . ASP J  1 110 ? 32.821  196.618 34.120  1.00 65.36  ? 109 ASP J CA  1 
ATOM   10661 C  C   . ASP J  1 110 ? 32.856  195.946 35.511  1.00 69.09  ? 109 ASP J C   1 
ATOM   10662 O  O   . ASP J  1 110 ? 31.849  195.970 36.233  1.00 63.33  ? 109 ASP J O   1 
ATOM   10663 C  CB  . ASP J  1 110 ? 31.894  195.701 33.267  1.00 69.47  ? 109 ASP J CB  1 
ATOM   10664 C  CG  . ASP J  1 110 ? 32.034  195.941 31.749  1.00 82.12  ? 109 ASP J CG  1 
ATOM   10665 O  OD1 . ASP J  1 110 ? 32.969  195.287 31.135  1.00 68.40  ? 109 ASP J OD1 1 
ATOM   10666 O  OD2 . ASP J  1 110 ? 31.202  196.773 31.204  1.00 64.54  ? 109 ASP J OD2 1 
ATOM   10667 N  N   . HIS J  1 111 ? 33.956  195.244 35.805  1.00 62.00  ? 110 HIS J N   1 
ATOM   10668 C  CA  . HIS J  1 111 ? 34.074  194.445 37.014  1.00 57.58  ? 110 HIS J CA  1 
ATOM   10669 C  C   . HIS J  1 111 ? 35.137  195.104 37.886  1.00 59.11  ? 110 HIS J C   1 
ATOM   10670 O  O   . HIS J  1 111 ? 35.625  194.468 38.905  1.00 51.39  ? 110 HIS J O   1 
ATOM   10671 C  CB  . HIS J  1 111 ? 34.494  192.995 36.684  1.00 58.69  ? 110 HIS J CB  1 
ATOM   10672 C  CG  . HIS J  1 111 ? 33.432  192.179 36.021  1.00 63.71  ? 110 HIS J CG  1 
ATOM   10673 N  ND1 . HIS J  1 111 ? 33.555  190.808 35.849  1.00 65.56  ? 110 HIS J ND1 1 
ATOM   10674 C  CD2 . HIS J  1 111 ? 32.235  192.528 35.473  1.00 67.59  ? 110 HIS J CD2 1 
ATOM   10675 C  CE1 . HIS J  1 111 ? 32.490  190.351 35.205  1.00 66.46  ? 110 HIS J CE1 1 
ATOM   10676 N  NE2 . HIS J  1 111 ? 31.669  191.370 34.972  1.00 69.16  ? 110 HIS J NE2 1 
ATOM   10677 N  N   . CYS J  1 112 ? 35.540  196.333 37.483  1.00 46.89  ? 111 CYS J N   1 
ATOM   10678 C  CA  . CYS J  1 112 ? 36.448  197.080 38.319  1.00 44.92  ? 111 CYS J CA  1 
ATOM   10679 C  C   . CYS J  1 112 ? 35.923  197.121 39.758  1.00 46.25  ? 111 CYS J C   1 
ATOM   10680 O  O   . CYS J  1 112 ? 34.733  197.369 39.989  1.00 44.58  ? 111 CYS J O   1 
ATOM   10681 C  CB  . CYS J  1 112 ? 36.654  198.477 37.802  1.00 48.23  ? 111 CYS J CB  1 
ATOM   10682 S  SG  . CYS J  1 112 ? 38.035  199.280 38.681  1.00 55.58  ? 111 CYS J SG  1 
ATOM   10683 N  N   . ILE J  1 113 ? 36.788  196.793 40.709  1.00 46.07  ? 112 ILE J N   1 
ATOM   10684 C  CA  . ILE J  1 113 ? 36.405  196.863 42.118  1.00 45.57  ? 112 ILE J CA  1 
ATOM   10685 C  C   . ILE J  1 113 ? 37.132  197.999 42.814  1.00 47.47  ? 112 ILE J C   1 
ATOM   10686 O  O   . ILE J  1 113 ? 37.093  198.124 44.071  1.00 46.38  ? 112 ILE J O   1 
ATOM   10687 C  CB  . ILE J  1 113 ? 36.751  195.571 42.875  1.00 46.39  ? 112 ILE J CB  1 
ATOM   10688 C  CG1 . ILE J  1 113 ? 38.267  195.290 42.730  1.00 47.68  ? 112 ILE J CG1 1 
ATOM   10689 C  CG2 . ILE J  1 113 ? 35.806  194.458 42.478  1.00 41.04  ? 112 ILE J CG2 1 
ATOM   10690 C  CD1 . ILE J  1 113 ? 38.806  194.490 43.900  1.00 48.67  ? 112 ILE J CD1 1 
ATOM   10691 N  N   . ILE J  1 114 ? 37.827  198.822 42.019  1.00 50.42  ? 113 ILE J N   1 
ATOM   10692 C  CA  . ILE J  1 114 ? 38.517  199.994 42.598  1.00 51.77  ? 113 ILE J CA  1 
ATOM   10693 C  C   . ILE J  1 114 ? 37.421  200.907 43.104  1.00 48.71  ? 113 ILE J C   1 
ATOM   10694 O  O   . ILE J  1 114 ? 36.463  201.128 42.391  1.00 50.86  ? 113 ILE J O   1 
ATOM   10695 C  CB  . ILE J  1 114 ? 39.375  200.780 41.575  1.00 50.79  ? 113 ILE J CB  1 
ATOM   10696 C  CG1 . ILE J  1 114 ? 40.491  199.899 41.005  1.00 56.06  ? 113 ILE J CG1 1 
ATOM   10697 C  CG2 . ILE J  1 114 ? 40.060  201.976 42.268  1.00 47.32  ? 113 ILE J CG2 1 
ATOM   10698 C  CD1 . ILE J  1 114 ? 41.521  199.473 42.046  1.00 53.35  ? 113 ILE J CD1 1 
ATOM   10699 N  N   . GLY J  1 115 ? 37.536  201.421 44.312  1.00 45.92  ? 114 GLY J N   1 
ATOM   10700 C  CA  . GLY J  1 115 ? 36.474  202.304 44.817  1.00 49.72  ? 114 GLY J CA  1 
ATOM   10701 C  C   . GLY J  1 115 ? 35.318  201.587 45.543  1.00 55.55  ? 114 GLY J C   1 
ATOM   10702 O  O   . GLY J  1 115 ? 34.443  202.251 46.164  1.00 48.56  ? 114 GLY J O   1 
ATOM   10703 N  N   . ARG J  1 116 ? 35.312  200.243 45.507  1.00 48.16  ? 115 ARG J N   1 
ATOM   10704 C  CA  . ARG J  1 116 ? 34.302  199.515 46.269  1.00 43.54  ? 115 ARG J CA  1 
ATOM   10705 C  C   . ARG J  1 116 ? 34.887  199.156 47.576  1.00 39.71  ? 115 ARG J C   1 
ATOM   10706 O  O   . ARG J  1 116 ? 36.012  199.616 47.874  1.00 42.57  ? 115 ARG J O   1 
ATOM   10707 C  CB  . ARG J  1 116 ? 33.711  198.334 45.505  1.00 40.05  ? 115 ARG J CB  1 
ATOM   10708 C  CG  . ARG J  1 116 ? 33.696  198.600 44.036  1.00 38.62  ? 115 ARG J CG  1 
ATOM   10709 C  CD  . ARG J  1 116 ? 32.659  197.781 43.344  1.00 39.62  ? 115 ARG J CD  1 
ATOM   10710 N  NE  . ARG J  1 116 ? 32.370  198.403 42.061  1.00 46.93  ? 115 ARG J NE  1 
ATOM   10711 C  CZ  . ARG J  1 116 ? 31.239  199.059 41.720  1.00 47.51  ? 115 ARG J CZ  1 
ATOM   10712 N  NH1 . ARG J  1 116 ? 30.165  199.124 42.527  1.00 42.58  ? 115 ARG J NH1 1 
ATOM   10713 N  NH2 . ARG J  1 116 ? 31.162  199.591 40.502  1.00 43.31  ? 115 ARG J NH2 1 
ATOM   10714 N  N   . THR J  1 117 ? 34.115  198.374 48.348  1.00 38.75  ? 116 THR J N   1 
ATOM   10715 C  CA  . THR J  1 117 ? 34.482  198.015 49.726  1.00 43.68  ? 116 THR J CA  1 
ATOM   10716 C  C   . THR J  1 117 ? 34.829  196.550 49.991  1.00 42.95  ? 116 THR J C   1 
ATOM   10717 O  O   . THR J  1 117 ? 34.028  195.648 49.759  1.00 49.73  ? 116 THR J O   1 
ATOM   10718 C  CB  . THR J  1 117 ? 33.402  198.495 50.742  1.00 41.11  ? 116 THR J CB  1 
ATOM   10719 O  OG1 . THR J  1 117 ? 33.491  199.929 50.860  1.00 41.99  ? 116 THR J OG1 1 
ATOM   10720 C  CG2 . THR J  1 117 ? 33.636  197.902 52.158  1.00 38.31  ? 116 THR J CG2 1 
ATOM   10721 N  N   . LEU J  1 118 ? 35.968  196.310 50.586  1.00 38.58  ? 117 LEU J N   1 
ATOM   10722 C  CA  . LEU J  1 118 ? 36.234  194.982 50.941  1.00 37.56  ? 117 LEU J CA  1 
ATOM   10723 C  C   . LEU J  1 118 ? 35.782  194.734 52.354  1.00 35.60  ? 117 LEU J C   1 
ATOM   10724 O  O   . LEU J  1 118 ? 36.169  195.468 53.205  1.00 38.79  ? 117 LEU J O   1 
ATOM   10725 C  CB  . LEU J  1 118 ? 37.728  194.713 50.757  1.00 40.90  ? 117 LEU J CB  1 
ATOM   10726 C  CG  . LEU J  1 118 ? 38.251  193.321 51.109  1.00 42.83  ? 117 LEU J CG  1 
ATOM   10727 C  CD1 . LEU J  1 118 ? 37.788  192.338 50.017  1.00 38.03  ? 117 LEU J CD1 1 
ATOM   10728 C  CD2 . LEU J  1 118 ? 39.770  193.436 51.359  1.00 38.19  ? 117 LEU J CD2 1 
ATOM   10729 N  N   . VAL J  1 119 ? 35.040  193.649 52.611  1.00 37.90  ? 118 VAL J N   1 
ATOM   10730 C  CA  . VAL J  1 119 ? 34.560  193.299 53.980  1.00 37.76  ? 118 VAL J CA  1 
ATOM   10731 C  C   . VAL J  1 119 ? 34.918  191.891 54.513  1.00 39.84  ? 118 VAL J C   1 
ATOM   10732 O  O   . VAL J  1 119 ? 34.705  190.883 53.824  1.00 38.90  ? 118 VAL J O   1 
ATOM   10733 C  CB  . VAL J  1 119 ? 33.011  193.382 53.999  1.00 36.59  ? 118 VAL J CB  1 
ATOM   10734 C  CG1 . VAL J  1 119 ? 32.429  193.048 55.363  1.00 31.73  ? 118 VAL J CG1 1 
ATOM   10735 C  CG2 . VAL J  1 119 ? 32.570  194.728 53.498  1.00 34.42  ? 118 VAL J CG2 1 
ATOM   10736 N  N   . VAL J  1 120 ? 35.389  191.810 55.748  1.00 36.17  ? 119 VAL J N   1 
ATOM   10737 C  CA  . VAL J  1 120 ? 35.610  190.520 56.356  1.00 40.78  ? 119 VAL J CA  1 
ATOM   10738 C  C   . VAL J  1 120 ? 34.483  190.290 57.329  1.00 41.89  ? 119 VAL J C   1 
ATOM   10739 O  O   . VAL J  1 120 ? 34.218  191.122 58.205  1.00 45.85  ? 119 VAL J O   1 
ATOM   10740 C  CB  . VAL J  1 120 ? 37.050  190.346 56.976  1.00 40.19  ? 119 VAL J CB  1 
ATOM   10741 C  CG1 . VAL J  1 120 ? 37.445  191.549 57.771  1.00 41.33  ? 119 VAL J CG1 1 
ATOM   10742 C  CG2 . VAL J  1 120 ? 37.173  189.151 57.912  1.00 38.48  ? 119 VAL J CG2 1 
ATOM   10743 N  N   . HIS J  1 121 ? 33.830  189.152 57.185  1.00 43.37  ? 120 HIS J N   1 
ATOM   10744 C  CA  . HIS J  1 121 ? 32.650  188.827 58.004  1.00 42.97  ? 120 HIS J CA  1 
ATOM   10745 C  C   . HIS J  1 121 ? 32.892  187.956 59.247  1.00 47.58  ? 120 HIS J C   1 
ATOM   10746 O  O   . HIS J  1 121 ? 33.994  187.405 59.471  1.00 44.03  ? 120 HIS J O   1 
ATOM   10747 C  CB  . HIS J  1 121 ? 31.600  188.164 57.159  1.00 39.01  ? 120 HIS J CB  1 
ATOM   10748 C  CG  . HIS J  1 121 ? 31.024  189.058 56.114  1.00 42.47  ? 120 HIS J CG  1 
ATOM   10749 N  ND1 . HIS J  1 121 ? 29.774  189.629 56.225  1.00 42.54  ? 120 HIS J ND1 1 
ATOM   10750 C  CD2 . HIS J  1 121 ? 31.527  189.485 54.928  1.00 44.34  ? 120 HIS J CD2 1 
ATOM   10751 C  CE1 . HIS J  1 121 ? 29.513  190.327 55.134  1.00 43.00  ? 120 HIS J CE1 1 
ATOM   10752 N  NE2 . HIS J  1 121 ? 30.570  190.273 54.342  1.00 43.79  ? 120 HIS J NE2 1 
ATOM   10753 N  N   . GLU J  1 122 ? 31.824  187.848 60.030  1.00 45.92  ? 121 GLU J N   1 
ATOM   10754 C  CA  . GLU J  1 122 ? 31.866  187.343 61.387  1.00 49.37  ? 121 GLU J CA  1 
ATOM   10755 C  C   . GLU J  1 122 ? 31.971  185.856 61.352  1.00 51.84  ? 121 GLU J C   1 
ATOM   10756 O  O   . GLU J  1 122 ? 32.701  185.305 62.170  1.00 54.63  ? 121 GLU J O   1 
ATOM   10757 C  CB  . GLU J  1 122 ? 30.616  187.792 62.159  1.00 48.15  ? 121 GLU J CB  1 
ATOM   10758 C  CG  . GLU J  1 122 ? 30.182  186.975 63.375  1.00 48.55  ? 121 GLU J CG  1 
ATOM   10759 C  CD  . GLU J  1 122 ? 28.768  187.393 63.823  1.00 56.95  ? 121 GLU J CD  1 
ATOM   10760 O  OE1 . GLU J  1 122 ? 27.700  187.074 63.195  1.00 54.63  ? 121 GLU J OE1 1 
ATOM   10761 O  OE2 . GLU J  1 122 ? 28.723  188.157 64.788  1.00 59.21  ? 121 GLU J OE2 1 
ATOM   10762 N  N   . LYS J  1 123 ? 31.242  185.236 60.408  1.00 51.78  ? 122 LYS J N   1 
ATOM   10763 C  CA  . LYS J  1 123 ? 31.190  183.759 60.187  1.00 50.14  ? 122 LYS J CA  1 
ATOM   10764 C  C   . LYS J  1 123 ? 31.749  183.264 58.857  1.00 44.71  ? 122 LYS J C   1 
ATOM   10765 O  O   . LYS J  1 123 ? 32.217  184.045 57.982  1.00 46.30  ? 122 LYS J O   1 
ATOM   10766 C  CB  . LYS J  1 123 ? 29.741  183.219 60.352  1.00 50.31  ? 122 LYS J CB  1 
ATOM   10767 C  CG  . LYS J  1 123 ? 29.170  183.473 61.733  1.00 47.26  ? 122 LYS J CG  1 
ATOM   10768 C  CD  . LYS J  1 123 ? 27.791  182.881 61.827  1.00 54.73  ? 122 LYS J CD  1 
ATOM   10769 C  CE  . LYS J  1 123 ? 26.753  183.737 61.105  1.00 57.19  ? 122 LYS J CE  1 
ATOM   10770 N  NZ  . LYS J  1 123 ? 25.374  183.299 61.468  1.00 54.12  ? 122 LYS J NZ  1 
ATOM   10771 N  N   . ALA J  1 124 ? 31.681  181.953 58.716  1.00 40.45  ? 123 ALA J N   1 
ATOM   10772 C  CA  . ALA J  1 124 ? 31.996  181.297 57.468  1.00 40.27  ? 123 ALA J CA  1 
ATOM   10773 C  C   . ALA J  1 124 ? 30.974  181.711 56.450  1.00 42.81  ? 123 ALA J C   1 
ATOM   10774 O  O   . ALA J  1 124 ? 29.763  181.761 56.765  1.00 39.21  ? 123 ALA J O   1 
ATOM   10775 C  CB  . ALA J  1 124 ? 31.927  179.803 57.634  1.00 31.99  ? 123 ALA J CB  1 
ATOM   10776 N  N   . ASP J  1 125 ? 31.466  182.011 55.244  1.00 38.34  ? 124 ASP J N   1 
ATOM   10777 C  CA  . ASP J  1 125 ? 30.653  181.921 54.050  1.00 37.14  ? 124 ASP J CA  1 
ATOM   10778 C  C   . ASP J  1 125 ? 30.366  180.441 53.702  1.00 37.83  ? 124 ASP J C   1 
ATOM   10779 O  O   . ASP J  1 125 ? 31.305  179.715 53.421  1.00 40.68  ? 124 ASP J O   1 
ATOM   10780 C  CB  . ASP J  1 125 ? 31.435  182.550 52.911  1.00 34.43  ? 124 ASP J CB  1 
ATOM   10781 C  CG  . ASP J  1 125 ? 30.594  182.715 51.640  1.00 37.17  ? 124 ASP J CG  1 
ATOM   10782 O  OD1 . ASP J  1 125 ? 29.476  182.109 51.490  1.00 33.98  ? 124 ASP J OD1 1 
ATOM   10783 O  OD2 . ASP J  1 125 ? 31.118  183.444 50.777  1.00 37.12  ? 124 ASP J OD2 1 
ATOM   10784 N  N   . ASP J  1 126 ? 29.106  180.016 53.643  1.00 35.90  ? 125 ASP J N   1 
ATOM   10785 C  CA  . ASP J  1 126 ? 28.759  178.631 53.221  1.00 36.08  ? 125 ASP J CA  1 
ATOM   10786 C  C   . ASP J  1 126 ? 28.756  178.397 51.709  1.00 35.97  ? 125 ASP J C   1 
ATOM   10787 O  O   . ASP J  1 126 ? 28.235  177.388 51.266  1.00 35.63  ? 125 ASP J O   1 
ATOM   10788 C  CB  . ASP J  1 126 ? 27.447  178.144 53.844  1.00 34.55  ? 125 ASP J CB  1 
ATOM   10789 C  CG  . ASP J  1 126 ? 26.172  178.806 53.213  1.00 40.43  ? 125 ASP J CG  1 
ATOM   10790 O  OD1 . ASP J  1 126 ? 26.161  179.398 52.081  1.00 37.73  ? 125 ASP J OD1 1 
ATOM   10791 O  OD2 . ASP J  1 126 ? 25.142  178.691 53.885  1.00 40.47  ? 125 ASP J OD2 1 
ATOM   10792 N  N   . LEU J  1 127 ? 29.292  179.350 50.938  1.00 33.97  ? 126 LEU J N   1 
ATOM   10793 C  CA  . LEU J  1 127 ? 29.438  179.213 49.476  1.00 38.30  ? 126 LEU J CA  1 
ATOM   10794 C  C   . LEU J  1 127 ? 28.190  178.844 48.682  1.00 40.41  ? 126 LEU J C   1 
ATOM   10795 O  O   . LEU J  1 127 ? 28.291  178.380 47.499  1.00 41.06  ? 126 LEU J O   1 
ATOM   10796 C  CB  . LEU J  1 127 ? 30.654  178.342 49.068  1.00 38.11  ? 126 LEU J CB  1 
ATOM   10797 C  CG  . LEU J  1 127 ? 31.827  178.403 50.082  1.00 42.49  ? 126 LEU J CG  1 
ATOM   10798 C  CD1 . LEU J  1 127 ? 33.005  177.548 49.694  1.00 43.39  ? 126 LEU J CD1 1 
ATOM   10799 C  CD2 . LEU J  1 127 ? 32.351  179.813 50.238  1.00 41.79  ? 126 LEU J CD2 1 
ATOM   10800 N  N   . GLY J  1 128 ? 27.030  179.105 49.292  1.00 42.03  ? 127 GLY J N   1 
ATOM   10801 C  CA  . GLY J  1 128 ? 25.724  179.005 48.594  1.00 39.07  ? 127 GLY J CA  1 
ATOM   10802 C  C   . GLY J  1 128 ? 25.167  177.618 48.835  1.00 38.23  ? 127 GLY J C   1 
ATOM   10803 O  O   . GLY J  1 128 ? 24.218  177.188 48.167  1.00 32.75  ? 127 GLY J O   1 
ATOM   10804 N  N   . LYS J  1 129 ? 25.739  176.917 49.823  1.00 38.04  ? 128 LYS J N   1 
ATOM   10805 C  CA  . LYS J  1 129 ? 25.360  175.504 50.054  1.00 38.68  ? 128 LYS J CA  1 
ATOM   10806 C  C   . LYS J  1 129 ? 24.483  175.266 51.266  1.00 34.31  ? 128 LYS J C   1 
ATOM   10807 O  O   . LYS J  1 129 ? 24.261  174.143 51.637  1.00 34.06  ? 128 LYS J O   1 
ATOM   10808 C  CB  . LYS J  1 129 ? 26.638  174.658 50.073  1.00 38.40  ? 128 LYS J CB  1 
ATOM   10809 C  CG  . LYS J  1 129 ? 27.297  174.716 48.697  1.00 43.36  ? 128 LYS J CG  1 
ATOM   10810 C  CD  . LYS J  1 129 ? 28.693  174.123 48.719  1.00 51.20  ? 128 LYS J CD  1 
ATOM   10811 C  CE  . LYS J  1 129 ? 28.652  172.625 48.349  1.00 58.02  ? 128 LYS J CE  1 
ATOM   10812 N  NZ  . LYS J  1 129 ? 29.515  171.799 49.269  1.00 57.20  ? 128 LYS J NZ  1 
ATOM   10813 N  N   . GLY J  1 130 ? 24.029  176.358 51.885  1.00 35.83  ? 129 GLY J N   1 
ATOM   10814 C  CA  . GLY J  1 130 ? 23.297  176.355 53.160  1.00 35.41  ? 129 GLY J CA  1 
ATOM   10815 C  C   . GLY J  1 130 ? 21.858  175.897 53.044  1.00 36.63  ? 129 GLY J C   1 
ATOM   10816 O  O   . GLY J  1 130 ? 21.279  175.510 54.059  1.00 36.12  ? 129 GLY J O   1 
ATOM   10817 N  N   . GLY J  1 131 ? 21.290  175.901 51.821  1.00 34.07  ? 130 GLY J N   1 
ATOM   10818 C  CA  . GLY J  1 131 ? 19.914  175.442 51.607  1.00 34.94  ? 130 GLY J CA  1 
ATOM   10819 C  C   . GLY J  1 131 ? 18.797  176.354 52.169  1.00 35.63  ? 130 GLY J C   1 
ATOM   10820 O  O   . GLY J  1 131 ? 17.660  175.972 52.260  1.00 38.78  ? 130 GLY J O   1 
ATOM   10821 N  N   . ASN J  1 132 ? 19.122  177.574 52.535  1.00 37.30  ? 131 ASN J N   1 
ATOM   10822 C  CA  . ASN J  1 132 ? 18.102  178.554 52.937  1.00 44.26  ? 131 ASN J CA  1 
ATOM   10823 C  C   . ASN J  1 132 ? 18.246  179.707 51.962  1.00 43.26  ? 131 ASN J C   1 
ATOM   10824 O  O   . ASN J  1 132 ? 19.266  179.816 51.227  1.00 43.53  ? 131 ASN J O   1 
ATOM   10825 C  CB  . ASN J  1 132 ? 18.259  179.014 54.427  1.00 43.82  ? 131 ASN J CB  1 
ATOM   10826 C  CG  . ASN J  1 132 ? 19.597  179.799 54.715  1.00 46.94  ? 131 ASN J CG  1 
ATOM   10827 O  OD1 . ASN J  1 132 ? 20.527  179.957 53.875  1.00 41.69  ? 131 ASN J OD1 1 
ATOM   10828 N  ND2 . ASN J  1 132 ? 19.673  180.304 55.930  1.00 46.20  ? 131 ASN J ND2 1 
ATOM   10829 N  N   . GLU J  1 133 ? 17.272  180.601 51.991  1.00 47.00  ? 132 GLU J N   1 
ATOM   10830 C  CA  . GLU J  1 133 ? 17.238  181.701 50.997  1.00 48.97  ? 132 GLU J CA  1 
ATOM   10831 C  C   . GLU J  1 133 ? 18.447  182.560 51.132  1.00 42.86  ? 132 GLU J C   1 
ATOM   10832 O  O   . GLU J  1 133 ? 18.987  182.995 50.139  1.00 46.27  ? 132 GLU J O   1 
ATOM   10833 C  CB  . GLU J  1 133 ? 15.999  182.582 51.124  1.00 48.97  ? 132 GLU J CB  1 
ATOM   10834 C  CG  . GLU J  1 133 ? 14.713  181.782 51.306  1.00 67.59  ? 132 GLU J CG  1 
ATOM   10835 C  CD  . GLU J  1 133 ? 13.464  182.677 51.155  1.00 82.21  ? 132 GLU J CD  1 
ATOM   10836 O  OE1 . GLU J  1 133 ? 12.901  183.033 52.253  1.00 70.82  ? 132 GLU J OE1 1 
ATOM   10837 O  OE2 . GLU J  1 133 ? 13.088  183.030 49.965  1.00 62.68  ? 132 GLU J OE2 1 
ATOM   10838 N  N   . GLU J  1 134 ? 18.901  182.750 52.368  1.00 43.37  ? 133 GLU J N   1 
ATOM   10839 C  CA  . GLU J  1 134 ? 20.018  183.643 52.691  1.00 42.05  ? 133 GLU J CA  1 
ATOM   10840 C  C   . GLU J  1 134 ? 21.375  183.124 52.195  1.00 45.09  ? 133 GLU J C   1 
ATOM   10841 O  O   . GLU J  1 134 ? 22.314  183.907 51.992  1.00 44.75  ? 133 GLU J O   1 
ATOM   10842 C  CB  . GLU J  1 134 ? 20.023  183.825 54.189  1.00 40.56  ? 133 GLU J CB  1 
ATOM   10843 C  CG  . GLU J  1 134 ? 21.112  184.726 54.718  1.00 45.64  ? 133 GLU J CG  1 
ATOM   10844 C  CD  . GLU J  1 134 ? 20.880  186.195 54.363  1.00 57.51  ? 133 GLU J CD  1 
ATOM   10845 O  OE1 . GLU J  1 134 ? 19.678  186.636 54.229  1.00 48.56  ? 133 GLU J OE1 1 
ATOM   10846 O  OE2 . GLU J  1 134 ? 21.924  186.908 54.223  1.00 53.49  ? 133 GLU J OE2 1 
ATOM   10847 N  N   . SER J  1 135 ? 21.456  181.803 51.991  1.00 43.85  ? 134 SER J N   1 
ATOM   10848 C  CA  . SER J  1 135 ? 22.677  181.185 51.575  1.00 40.99  ? 134 SER J CA  1 
ATOM   10849 C  C   . SER J  1 135 ? 23.045  181.694 50.217  1.00 44.75  ? 134 SER J C   1 
ATOM   10850 O  O   . SER J  1 135 ? 24.209  182.016 49.946  1.00 39.95  ? 134 SER J O   1 
ATOM   10851 C  CB  . SER J  1 135 ? 22.490  179.702 51.447  1.00 37.97  ? 134 SER J CB  1 
ATOM   10852 O  OG  . SER J  1 135 ? 23.768  179.170 51.204  1.00 38.16  ? 134 SER J OG  1 
ATOM   10853 N  N   . THR J  1 136 ? 22.035  181.708 49.354  1.00 41.85  ? 135 THR J N   1 
ATOM   10854 C  CA  . THR J  1 136 ? 22.142  182.293 48.022  1.00 45.62  ? 135 THR J CA  1 
ATOM   10855 C  C   . THR J  1 136 ? 22.278  183.851 47.920  1.00 41.73  ? 135 THR J C   1 
ATOM   10856 O  O   . THR J  1 136 ? 22.421  184.360 46.837  1.00 39.85  ? 135 THR J O   1 
ATOM   10857 C  CB  . THR J  1 136 ? 20.857  181.932 47.287  1.00 50.26  ? 135 THR J CB  1 
ATOM   10858 O  OG1 . THR J  1 136 ? 19.776  182.388 48.105  1.00 56.97  ? 135 THR J OG1 1 
ATOM   10859 C  CG2 . THR J  1 136 ? 20.712  180.431 47.144  1.00 49.46  ? 135 THR J CG2 1 
ATOM   10860 N  N   . LYS J  1 137 ? 22.184  184.609 49.015  1.00 44.25  ? 136 LYS J N   1 
ATOM   10861 C  CA  . LYS J  1 137 ? 22.483  186.073 48.971  1.00 43.54  ? 136 LYS J CA  1 
ATOM   10862 C  C   . LYS J  1 137 ? 23.860  186.392 49.556  1.00 50.51  ? 136 LYS J C   1 
ATOM   10863 O  O   . LYS J  1 137 ? 24.706  187.054 48.902  1.00 45.29  ? 136 LYS J O   1 
ATOM   10864 C  CB  . LYS J  1 137 ? 21.424  186.930 49.733  1.00 44.10  ? 136 LYS J CB  1 
ATOM   10865 C  CG  . LYS J  1 137 ? 20.020  187.068 49.090  1.00 49.30  ? 136 LYS J CG  1 
ATOM   10866 C  CD  . LYS J  1 137 ? 18.920  186.638 50.060  1.00 52.13  ? 136 LYS J CD  1 
ATOM   10867 C  CE  . LYS J  1 137 ? 17.518  186.861 49.491  1.00 61.93  ? 136 LYS J CE  1 
ATOM   10868 N  NZ  . LYS J  1 137 ? 16.519  187.221 50.562  1.00 55.68  ? 136 LYS J NZ  1 
ATOM   10869 N  N   . THR J  1 138 ? 24.083  185.906 50.792  1.00 47.10  ? 137 THR J N   1 
ATOM   10870 C  CA  . THR J  1 138 ? 25.248  186.303 51.566  1.00 44.22  ? 137 THR J CA  1 
ATOM   10871 C  C   . THR J  1 138 ? 26.156  185.148 52.000  1.00 43.33  ? 137 THR J C   1 
ATOM   10872 O  O   . THR J  1 138 ? 27.141  185.362 52.715  1.00 42.27  ? 137 THR J O   1 
ATOM   10873 C  CB  . THR J  1 138 ? 24.796  187.001 52.867  1.00 49.89  ? 137 THR J CB  1 
ATOM   10874 O  OG1 . THR J  1 138 ? 24.062  186.069 53.713  1.00 38.93  ? 137 THR J OG1 1 
ATOM   10875 C  CG2 . THR J  1 138 ? 24.008  188.324 52.540  1.00 42.99  ? 137 THR J CG2 1 
ATOM   10876 N  N   . GLY J  1 139 ? 25.794  183.929 51.636  1.00 42.42  ? 138 GLY J N   1 
ATOM   10877 C  CA  . GLY J  1 139 ? 26.383  182.753 52.287  1.00 42.43  ? 138 GLY J CA  1 
ATOM   10878 C  C   . GLY J  1 139 ? 26.184  182.575 53.808  1.00 40.08  ? 138 GLY J C   1 
ATOM   10879 O  O   . GLY J  1 139 ? 26.750  181.640 54.380  1.00 42.24  ? 138 GLY J O   1 
ATOM   10880 N  N   . ASN J  1 140 ? 25.387  183.416 54.474  1.00 36.16  ? 139 ASN J N   1 
ATOM   10881 C  CA  . ASN J  1 140 ? 25.105  183.256 55.943  1.00 34.47  ? 139 ASN J CA  1 
ATOM   10882 C  C   . ASN J  1 140 ? 26.379  183.600 56.736  1.00 38.17  ? 139 ASN J C   1 
ATOM   10883 O  O   . ASN J  1 140 ? 26.574  183.054 57.817  1.00 38.96  ? 139 ASN J O   1 
ATOM   10884 C  CB  . ASN J  1 140 ? 24.609  181.841 56.354  1.00 37.16  ? 139 ASN J CB  1 
ATOM   10885 C  CG  . ASN J  1 140 ? 23.289  181.470 55.738  1.00 39.85  ? 139 ASN J CG  1 
ATOM   10886 O  OD1 . ASN J  1 140 ? 22.299  182.015 56.124  1.00 48.92  ? 139 ASN J OD1 1 
ATOM   10887 N  ND2 . ASN J  1 140 ? 23.261  180.533 54.812  1.00 38.63  ? 139 ASN J ND2 1 
ATOM   10888 N  N   . ALA J  1 141 ? 27.242  184.454 56.145  1.00 38.73  ? 140 ALA J N   1 
ATOM   10889 C  CA  . ALA J  1 141 ? 28.481  184.943 56.707  1.00 36.92  ? 140 ALA J CA  1 
ATOM   10890 C  C   . ALA J  1 141 ? 28.268  185.912 57.864  1.00 40.56  ? 140 ALA J C   1 
ATOM   10891 O  O   . ALA J  1 141 ? 29.255  186.319 58.514  1.00 39.78  ? 140 ALA J O   1 
ATOM   10892 C  CB  . ALA J  1 141 ? 29.350  185.605 55.613  1.00 34.89  ? 140 ALA J CB  1 
ATOM   10893 N  N   . GLY J  1 142 ? 27.010  186.310 58.107  1.00 41.71  ? 141 GLY J N   1 
ATOM   10894 C  CA  . GLY J  1 142 ? 26.723  187.248 59.217  1.00 44.15  ? 141 GLY J CA  1 
ATOM   10895 C  C   . GLY J  1 142 ? 27.358  188.655 59.070  1.00 45.72  ? 141 GLY J C   1 
ATOM   10896 O  O   . GLY J  1 142 ? 27.688  189.138 57.929  1.00 39.00  ? 141 GLY J O   1 
ATOM   10897 N  N   . SER J  1 143 ? 27.552  189.276 60.240  1.00 43.70  ? 142 SER J N   1 
ATOM   10898 C  CA  . SER J  1 143 ? 27.803  190.713 60.377  1.00 44.74  ? 142 SER J CA  1 
ATOM   10899 C  C   . SER J  1 143 ? 29.207  191.094 59.851  1.00 46.03  ? 142 SER J C   1 
ATOM   10900 O  O   . SER J  1 143 ? 30.010  190.211 59.558  1.00 46.07  ? 142 SER J O   1 
ATOM   10901 C  CB  . SER J  1 143 ? 27.604  191.117 61.838  1.00 44.95  ? 142 SER J CB  1 
ATOM   10902 O  OG  . SER J  1 143 ? 28.495  190.342 62.631  1.00 50.93  ? 142 SER J OG  1 
ATOM   10903 N  N   . ARG J  1 144 ? 29.494  192.400 59.722  1.00 43.97  ? 143 ARG J N   1 
ATOM   10904 C  CA  . ARG J  1 144 ? 30.676  192.864 58.999  1.00 40.51  ? 143 ARG J CA  1 
ATOM   10905 C  C   . ARG J  1 144 ? 31.680  193.284 60.044  1.00 43.11  ? 143 ARG J C   1 
ATOM   10906 O  O   . ARG J  1 144 ? 31.454  194.275 60.677  1.00 48.91  ? 143 ARG J O   1 
ATOM   10907 C  CB  . ARG J  1 144 ? 30.331  194.048 58.094  1.00 31.92  ? 143 ARG J CB  1 
ATOM   10908 C  CG  . ARG J  1 144 ? 29.061  193.863 57.376  1.00 32.13  ? 143 ARG J CG  1 
ATOM   10909 C  CD  . ARG J  1 144 ? 28.719  194.914 56.329  1.00 34.41  ? 143 ARG J CD  1 
ATOM   10910 N  NE  . ARG J  1 144 ? 27.573  194.421 55.543  1.00 35.24  ? 143 ARG J NE  1 
ATOM   10911 C  CZ  . ARG J  1 144 ? 27.146  194.910 54.373  1.00 36.40  ? 143 ARG J CZ  1 
ATOM   10912 N  NH1 . ARG J  1 144 ? 27.671  196.010 53.833  1.00 36.36  ? 143 ARG J NH1 1 
ATOM   10913 N  NH2 . ARG J  1 144 ? 26.160  194.292 53.718  1.00 35.70  ? 143 ARG J NH2 1 
ATOM   10914 N  N   . LEU J  1 145 ? 32.784  192.559 60.238  1.00 45.18  ? 144 LEU J N   1 
ATOM   10915 C  CA  . LEU J  1 145 ? 33.737  192.931 61.297  1.00 38.52  ? 144 LEU J CA  1 
ATOM   10916 C  C   . LEU J  1 145 ? 34.677  194.106 60.968  1.00 36.86  ? 144 LEU J C   1 
ATOM   10917 O  O   . LEU J  1 145 ? 35.013  194.835 61.863  1.00 39.13  ? 144 LEU J O   1 
ATOM   10918 C  CB  . LEU J  1 145 ? 34.540  191.705 61.719  1.00 41.74  ? 144 LEU J CB  1 
ATOM   10919 C  CG  . LEU J  1 145 ? 33.717  190.509 62.236  1.00 44.99  ? 144 LEU J CG  1 
ATOM   10920 C  CD1 . LEU J  1 145 ? 34.707  189.376 62.464  1.00 40.27  ? 144 LEU J CD1 1 
ATOM   10921 C  CD2 . LEU J  1 145 ? 32.870  190.776 63.493  1.00 38.79  ? 144 LEU J CD2 1 
ATOM   10922 N  N   . ALA J  1 146 ? 35.099  194.284 59.713  1.00 32.27  ? 145 ALA J N   1 
ATOM   10923 C  CA  . ALA J  1 146 ? 36.014  195.350 59.315  1.00 34.28  ? 145 ALA J CA  1 
ATOM   10924 C  C   . ALA J  1 146 ? 35.896  195.538 57.820  1.00 34.41  ? 145 ALA J C   1 
ATOM   10925 O  O   . ALA J  1 146 ? 35.471  194.656 57.166  1.00 42.32  ? 145 ALA J O   1 
ATOM   10926 C  CB  . ALA J  1 146 ? 37.476  195.071 59.682  1.00 33.47  ? 145 ALA J CB  1 
ATOM   10927 N  N   . CYS J  1 147 ? 36.197  196.713 57.308  1.00 32.77  ? 146 CYS J N   1 
ATOM   10928 C  CA  . CYS J  1 147 ? 36.130  196.985 55.889  1.00 34.63  ? 146 CYS J CA  1 
ATOM   10929 C  C   . CYS J  1 147 ? 37.048  198.177 55.622  1.00 32.26  ? 146 CYS J C   1 
ATOM   10930 O  O   . CYS J  1 147 ? 37.720  198.740 56.523  1.00 30.56  ? 146 CYS J O   1 
ATOM   10931 C  CB  . CYS J  1 147 ? 34.665  197.306 55.438  1.00 44.08  ? 146 CYS J CB  1 
ATOM   10932 S  SG  . CYS J  1 147 ? 33.786  198.613 56.402  1.00 44.05  ? 146 CYS J SG  1 
ATOM   10933 N  N   . GLY J  1 148 ? 37.091  198.544 54.371  1.00 34.26  ? 147 GLY J N   1 
ATOM   10934 C  CA  . GLY J  1 148 ? 37.839  199.731 53.928  1.00 34.90  ? 147 GLY J CA  1 
ATOM   10935 C  C   . GLY J  1 148 ? 37.587  199.777 52.431  1.00 36.83  ? 147 GLY J C   1 
ATOM   10936 O  O   . GLY J  1 148 ? 37.081  198.776 51.840  1.00 35.22  ? 147 GLY J O   1 
ATOM   10937 N  N   . VAL J  1 149 ? 37.934  200.915 51.826  1.00 38.29  ? 148 VAL J N   1 
ATOM   10938 C  CA  . VAL J  1 149 ? 37.695  201.173 50.397  1.00 40.78  ? 148 VAL J CA  1 
ATOM   10939 C  C   . VAL J  1 149 ? 38.894  200.768 49.543  1.00 42.00  ? 148 VAL J C   1 
ATOM   10940 O  O   . VAL J  1 149 ? 40.027  200.988 49.922  1.00 42.06  ? 148 VAL J O   1 
ATOM   10941 C  CB  . VAL J  1 149 ? 37.410  202.660 50.160  1.00 36.58  ? 148 VAL J CB  1 
ATOM   10942 C  CG1 . VAL J  1 149 ? 36.893  202.878 48.729  1.00 35.18  ? 148 VAL J CG1 1 
ATOM   10943 C  CG2 . VAL J  1 149 ? 36.405  203.124 51.173  1.00 32.88  ? 148 VAL J CG2 1 
ATOM   10944 N  N   . ILE J  1 150 ? 38.644  200.201 48.380  1.00 44.55  ? 149 ILE J N   1 
ATOM   10945 C  CA  . ILE J  1 150 ? 39.731  199.614 47.603  1.00 43.88  ? 149 ILE J CA  1 
ATOM   10946 C  C   . ILE J  1 150 ? 40.252  200.759 46.756  1.00 43.90  ? 149 ILE J C   1 
ATOM   10947 O  O   . ILE J  1 150 ? 39.574  201.225 45.832  1.00 42.82  ? 149 ILE J O   1 
ATOM   10948 C  CB  . ILE J  1 150 ? 39.234  198.431 46.743  1.00 45.26  ? 149 ILE J CB  1 
ATOM   10949 C  CG1 . ILE J  1 150 ? 38.718  197.284 47.646  1.00 42.29  ? 149 ILE J CG1 1 
ATOM   10950 C  CG2 . ILE J  1 150 ? 40.337  197.946 45.819  1.00 40.21  ? 149 ILE J CG2 1 
ATOM   10951 C  CD1 . ILE J  1 150 ? 37.793  196.385 46.879  1.00 36.35  ? 149 ILE J CD1 1 
ATOM   10952 N  N   . GLY J  1 151 ? 41.439  201.226 47.114  1.00 42.66  ? 150 GLY J N   1 
ATOM   10953 C  CA  . GLY J  1 151 ? 42.040  202.367 46.460  1.00 49.14  ? 150 GLY J CA  1 
ATOM   10954 C  C   . GLY J  1 151 ? 43.246  202.035 45.622  1.00 54.30  ? 150 GLY J C   1 
ATOM   10955 O  O   . GLY J  1 151 ? 44.033  201.178 46.022  1.00 54.96  ? 150 GLY J O   1 
ATOM   10956 N  N   . ILE J  1 152 ? 43.389  202.734 44.478  1.00 56.10  ? 151 ILE J N   1 
ATOM   10957 C  CA  . ILE J  1 152 ? 44.559  202.622 43.538  1.00 52.03  ? 151 ILE J CA  1 
ATOM   10958 C  C   . ILE J  1 152 ? 45.924  202.831 44.243  1.00 56.24  ? 151 ILE J C   1 
ATOM   10959 O  O   . ILE J  1 152 ? 46.087  203.762 45.043  1.00 55.90  ? 151 ILE J O   1 
ATOM   10960 C  CB  . ILE J  1 152 ? 44.442  203.619 42.377  1.00 50.47  ? 151 ILE J CB  1 
ATOM   10961 C  CG1 . ILE J  1 152 ? 43.334  203.179 41.432  1.00 59.18  ? 151 ILE J CG1 1 
ATOM   10962 C  CG2 . ILE J  1 152 ? 45.766  203.709 41.600  1.00 56.72  ? 151 ILE J CG2 1 
ATOM   10963 C  CD1 . ILE J  1 152 ? 42.720  204.264 40.534  1.00 63.58  ? 151 ILE J CD1 1 
ATOM   10964 N  N   . ALA J  1 153 ? 46.879  201.929 43.982  1.00 56.89  ? 152 ALA J N   1 
ATOM   10965 C  CA  . ALA J  1 153 ? 48.183  201.952 44.656  1.00 54.14  ? 152 ALA J CA  1 
ATOM   10966 C  C   . ALA J  1 153 ? 49.371  202.096 43.664  1.00 57.61  ? 152 ALA J C   1 
ATOM   10967 O  O   . ALA J  1 153 ? 49.278  201.859 42.411  1.00 49.87  ? 152 ALA J O   1 
ATOM   10968 C  CB  . ALA J  1 153 ? 48.345  200.719 45.550  1.00 56.88  ? 152 ALA J CB  1 
ATOM   10969 N  N   . GLN J  1 154 ? 50.496  202.503 44.229  1.00 57.89  ? 153 GLN J N   1 
ATOM   10970 C  CA  . GLN J  1 154 ? 51.687  202.732 43.414  1.00 69.91  ? 153 GLN J CA  1 
ATOM   10971 C  C   . GLN J  1 154 ? 52.407  201.421 43.069  1.00 76.11  ? 153 GLN J C   1 
ATOM   10972 O  O   . GLN J  1 154 ? 52.942  200.704 43.985  1.00 66.65  ? 153 GLN J O   1 
ATOM   10973 C  CB  . GLN J  1 154 ? 52.692  203.651 44.103  1.00 68.88  ? 153 GLN J CB  1 
ATOM   10974 C  CG  . GLN J  1 154 ? 53.923  203.735 43.226  1.00 66.02  ? 153 GLN J CG  1 
ATOM   10975 C  CD  . GLN J  1 154 ? 54.798  204.852 43.646  1.00 71.57  ? 153 GLN J CD  1 
ATOM   10976 O  OE1 . GLN J  1 154 ? 55.275  204.876 44.822  1.00 62.28  ? 153 GLN J OE1 1 
ATOM   10977 N  NE2 . GLN J  1 154 ? 55.030  205.816 42.699  1.00 55.72  ? 153 GLN J NE2 1 
ATOM   10978 O  OXT . GLN J  1 154 ? 52.459  201.144 41.850  1.00 68.89  ? 153 GLN J OXT 1 
HETATM 10979 ZN ZN  . ZN  K  2 .   ? 34.481  269.991 23.072  1.00 49.51  ? 201 ZN  A ZN  1 
HETATM 10980 S  S   . DMS L  3 .   ? 25.192  259.689 6.999   1.00 74.29  ? 202 DMS A S   1 
HETATM 10981 O  O   . DMS L  3 .   ? 24.888  259.555 8.513   1.00 61.49  ? 202 DMS A O   1 
HETATM 10982 C  C1  . DMS L  3 .   ? 24.873  258.275 5.971   1.00 63.72  ? 202 DMS A C1  1 
HETATM 10983 C  C2  . DMS L  3 .   ? 24.141  260.878 6.269   1.00 76.65  ? 202 DMS A C2  1 
HETATM 10984 C  C1  . GOL M  4 .   ? 28.192  271.801 12.894  1.00 56.02  ? 203 GOL A C1  1 
HETATM 10985 O  O1  . GOL M  4 .   ? 28.659  272.722 11.869  1.00 63.73  ? 203 GOL A O1  1 
HETATM 10986 C  C2  . GOL M  4 .   ? 29.046  272.144 14.122  1.00 58.33  ? 203 GOL A C2  1 
HETATM 10987 O  O2  . GOL M  4 .   ? 28.203  272.522 15.245  1.00 59.56  ? 203 GOL A O2  1 
HETATM 10988 C  C3  . GOL M  4 .   ? 29.992  270.997 14.481  1.00 58.81  ? 203 GOL A C3  1 
HETATM 10989 O  O3  . GOL M  4 .   ? 30.490  270.883 15.859  1.00 56.19  ? 203 GOL A O3  1 
HETATM 10990 S  S4  . S4P N  5 .   ? 26.462  254.176 28.985  1.00 66.54  ? 204 S4P A S4  1 
HETATM 10991 S  S3  . S4P N  5 .   ? 24.582  253.303 29.253  1.00 73.74  ? 204 S4P A S3  1 
HETATM 10992 S  S2  . S4P N  5 .   ? 24.727  251.312 28.603  1.00 73.52  ? 204 S4P A S2  1 
HETATM 10993 S  S1  . S4P N  5 .   ? 22.666  250.906 28.387  1.00 62.92  ? 204 S4P A S1  1 
HETATM 10994 ZN ZN  . ZN  O  2 .   ? 15.202  235.876 20.478  1.00 39.58  ? 201 ZN  B ZN  1 
HETATM 10995 C  C1  . GOL P  4 .   ? 4.543   242.628 -0.879  1.00 55.13  ? 202 GOL B C1  1 
HETATM 10996 O  O1  . GOL P  4 .   ? 5.156   242.119 -2.108  1.00 56.70  ? 202 GOL B O1  1 
HETATM 10997 C  C2  . GOL P  4 .   ? 4.284   244.118 -1.029  1.00 51.73  ? 202 GOL B C2  1 
HETATM 10998 O  O2  . GOL P  4 .   ? 2.877   244.290 -1.098  1.00 68.14  ? 202 GOL B O2  1 
HETATM 10999 C  C3  . GOL P  4 .   ? 4.716   244.943 0.187   1.00 57.44  ? 202 GOL B C3  1 
HETATM 11000 O  O3  . GOL P  4 .   ? 4.933   246.382 -0.026  1.00 49.06  ? 202 GOL B O3  1 
HETATM 11001 ZN ZN  . ZN  Q  2 .   ? 15.450  183.739 23.320  1.00 49.17  ? 201 ZN  C ZN  1 
HETATM 11002 C  C1  . GOL R  4 .   ? 20.163  188.142 13.829  1.00 64.27  ? 202 GOL C C1  1 
HETATM 11003 O  O1  . GOL R  4 .   ? 20.131  188.294 12.374  1.00 65.33  ? 202 GOL C O1  1 
HETATM 11004 C  C2  . GOL R  4 .   ? 21.246  187.114 14.282  1.00 70.10  ? 202 GOL C C2  1 
HETATM 11005 O  O2  . GOL R  4 .   ? 22.633  187.506 13.982  1.00 62.94  ? 202 GOL C O2  1 
HETATM 11006 C  C3  . GOL R  4 .   ? 21.139  186.880 15.792  1.00 62.94  ? 202 GOL C C3  1 
HETATM 11007 O  O3  . GOL R  4 .   ? 21.426  188.117 16.523  1.00 56.15  ? 202 GOL C O3  1 
HETATM 11008 S  S4  . S4P S  5 .   ? 5.637   198.667 29.056  1.00 75.26  ? 203 S4P C S4  1 
HETATM 11009 S  S3  . S4P S  5 .   ? 4.236   200.214 29.527  1.00 74.05  ? 203 S4P C S3  1 
HETATM 11010 S  S2  . S4P S  5 .   ? 5.409   201.787 28.991  1.00 70.46  ? 203 S4P C S2  1 
HETATM 11011 S  S1  . S4P S  5 .   ? 3.992   203.125 28.243  1.00 66.17  ? 203 S4P C S1  1 
HETATM 11012 ZN ZN  . ZN  T  2 .   ? -4.695  217.493 20.534  1.00 41.07  ? 201 ZN  D ZN  1 
HETATM 11013 S  S   . DMS U  3 .   ? 2.460   203.316 6.430   1.00 74.41  ? 202 DMS D S   1 
HETATM 11014 O  O   . DMS U  3 .   ? 1.921   204.423 7.405   1.00 67.22  ? 202 DMS D O   1 
HETATM 11015 C  C1  . DMS U  3 .   ? 2.254   203.461 4.678   1.00 63.45  ? 202 DMS D C1  1 
HETATM 11016 C  C2  . DMS U  3 .   ? 4.170   202.875 6.522   1.00 66.36  ? 202 DMS D C2  1 
HETATM 11017 C  C1  . GOL V  4 .   ? -6.818  213.284 10.175  1.00 52.31  ? 203 GOL D C1  1 
HETATM 11018 O  O1  . GOL V  4 .   ? -7.702  212.504 9.365   1.00 56.28  ? 203 GOL D O1  1 
HETATM 11019 C  C2  . GOL V  4 .   ? -7.491  213.753 11.460  1.00 53.42  ? 203 GOL D C2  1 
HETATM 11020 O  O2  . GOL V  4 .   ? -8.781  213.097 11.672  1.00 53.80  ? 203 GOL D O2  1 
HETATM 11021 C  C3  . GOL V  4 .   ? -6.529  213.326 12.580  1.00 51.40  ? 203 GOL D C3  1 
HETATM 11022 O  O3  . GOL V  4 .   ? -5.940  214.174 13.639  1.00 40.12  ? 203 GOL D O3  1 
HETATM 11023 ZN ZN  . ZN  W  2 .   ? 49.835  243.173 48.676  1.00 62.79  ? 201 ZN  E ZN  1 
HETATM 11024 C  C15 . 6B3 X  6 .   ? 25.523  221.887 53.016  1.00 72.44  ? 201 6B3 F C15 1 
HETATM 11025 C  C14 . 6B3 X  6 .   ? 19.233  224.697 49.154  1.00 82.79  ? 201 6B3 F C14 1 
HETATM 11026 C  C13 . 6B3 X  6 .   ? 20.216  224.225 50.213  1.00 83.19  ? 201 6B3 F C13 1 
HETATM 11027 C  C17 . 6B3 X  6 .   ? 23.856  221.884 54.963  1.00 85.84  ? 201 6B3 F C17 1 
HETATM 11028 C  C18 . 6B3 X  6 .   ? 18.468  223.703 48.396  1.00 82.33  ? 201 6B3 F C18 1 
HETATM 11029 C  C7  . 6B3 X  6 .   ? 26.300  221.165 55.273  1.00 69.81  ? 201 6B3 F C7  1 
HETATM 11030 C  C6  . 6B3 X  6 .   ? 24.749  222.658 50.707  1.00 74.36  ? 201 6B3 F C6  1 
HETATM 11031 C  C5  . 6B3 X  6 .   ? 24.491  222.383 52.125  1.00 77.05  ? 201 6B3 F C5  1 
HETATM 11032 C  C2  . 6B3 X  6 .   ? 22.445  223.321 50.469  1.00 76.83  ? 201 6B3 F C2  1 
HETATM 11033 C  C4  . 6B3 X  6 .   ? 23.165  222.595 52.713  1.00 78.39  ? 201 6B3 F C4  1 
HETATM 11034 C  C3  . 6B3 X  6 .   ? 22.171  223.056 51.851  1.00 71.13  ? 201 6B3 F C3  1 
HETATM 11035 C  C1  . 6B3 X  6 .   ? 23.733  223.140 49.861  1.00 66.86  ? 201 6B3 F C1  1 
HETATM 11036 C  C21 . 6B3 X  6 .   ? 18.202  226.444 48.012  1.00 82.58  ? 201 6B3 F C21 1 
HETATM 11037 C  C22 . 6B3 X  6 .   ? 19.127  226.081 48.994  1.00 63.84  ? 201 6B3 F C22 1 
HETATM 11038 N  N9  . 6B3 X  6 .   ? 22.856  222.362 54.069  1.00 73.02  ? 201 6B3 F N9  1 
HETATM 11039 C  C16 . 6B3 X  6 .   ? 25.226  221.641 54.434  1.00 81.67  ? 201 6B3 F C16 1 
HETATM 11040 C  C8  . 6B3 X  6 .   ? 27.576  220.947 54.726  1.00 63.51  ? 201 6B3 F C8  1 
HETATM 11041 C  C10 . 6B3 X  6 .   ? 26.839  221.670 52.521  1.00 64.40  ? 201 6B3 F C10 1 
HETATM 11042 C  C11 . 6B3 X  6 .   ? 27.837  221.203 53.367  1.00 60.78  ? 201 6B3 F C11 1 
HETATM 11043 O  O9  . 6B3 X  6 .   ? 23.552  221.684 56.220  1.00 70.83  ? 201 6B3 F O9  1 
HETATM 11044 N  N12 . 6B3 X  6 .   ? 21.397  223.767 49.704  1.00 78.15  ? 201 6B3 F N12 1 
HETATM 11045 C  C19 . 6B3 X  6 .   ? 17.545  224.092 47.426  1.00 76.18  ? 201 6B3 F C19 1 
HETATM 11046 C  C20 . 6B3 X  6 .   ? 17.446  225.482 47.275  1.00 86.19  ? 201 6B3 F C20 1 
HETATM 11047 O  O29 . 6B3 X  6 .   ? 19.866  224.261 51.441  1.00 66.53  ? 201 6B3 F O29 1 
HETATM 11048 ZN ZN  . ZN  Y  2 .   ? 10.702  244.145 51.715  1.00 39.52  ? 202 ZN  F ZN  1 
HETATM 11049 S  S4  . S4P Z  5 .   ? 31.601  244.699 43.006  1.00 61.20  ? 203 S4P F S4  1 
HETATM 11050 S  S3  . S4P Z  5 .   ? 29.644  245.023 43.656  1.00 60.70  ? 203 S4P F S3  1 
HETATM 11051 S  S2  . S4P Z  5 .   ? 28.850  243.280 42.938  1.00 65.74  ? 203 S4P F S2  1 
HETATM 11052 S  S1  . S4P Z  5 .   ? 26.936  243.593 43.691  1.00 61.52  ? 203 S4P F S1  1 
HETATM 11053 ZN ZN  . ZN  AA 2 .   ? -22.472 247.402 -20.929 1.00 48.32  ? 201 ZN  H ZN  1 
HETATM 11054 ZN ZN  . ZN  BA 2 .   ? 48.444  220.606 43.266  1.00 59.85  ? 201 ZN  I ZN  1 
HETATM 11055 ZN ZN  . ZN  CA 2 .   ? 27.914  186.965 47.277  1.00 50.87  ? 201 ZN  J ZN  1 
HETATM 11056 O  O   . HOH DA 7 .   ? 28.365  261.920 34.488  1.00 41.72  ? 301 HOH A O   1 
HETATM 11057 O  O   . HOH DA 7 .   ? 34.095  249.778 31.440  1.00 36.19  ? 302 HOH A O   1 
HETATM 11058 O  O   . HOH DA 7 .   ? 30.814  258.096 4.382   1.00 52.44  ? 303 HOH A O   1 
HETATM 11059 O  O   . HOH DA 7 .   ? 43.971  263.823 19.124  1.00 42.43  ? 304 HOH A O   1 
HETATM 11060 O  O   . HOH DA 7 .   ? 36.914  264.141 2.665   1.00 42.04  ? 305 HOH A O   1 
HETATM 11061 O  O   . HOH DA 7 .   ? 34.983  251.434 38.055  1.00 35.20  ? 306 HOH A O   1 
HETATM 11062 O  O   . HOH DA 7 .   ? 27.256  272.675 17.588  1.00 49.82  ? 307 HOH A O   1 
HETATM 11063 O  O   . HOH DA 7 .   ? 43.938  273.769 24.912  1.00 46.14  ? 308 HOH A O   1 
HETATM 11064 O  O   . HOH DA 7 .   ? 34.576  267.340 31.339  1.00 35.64  ? 309 HOH A O   1 
HETATM 11065 O  O   . HOH DA 7 .   ? 33.467  270.399 16.840  1.00 46.12  ? 310 HOH A O   1 
HETATM 11066 O  O   . HOH DA 7 .   ? 43.414  261.712 25.412  1.00 37.52  ? 311 HOH A O   1 
HETATM 11067 O  O   . HOH DA 7 .   ? 39.436  268.309 21.705  1.00 32.52  ? 312 HOH A O   1 
HETATM 11068 O  O   . HOH DA 7 .   ? 28.571  252.480 14.713  1.00 25.97  ? 313 HOH A O   1 
HETATM 11069 O  O   . HOH DA 7 .   ? 31.094  248.083 35.375  1.00 43.61  ? 314 HOH A O   1 
HETATM 11070 O  O   . HOH DA 7 .   ? 32.158  267.468 30.277  1.00 40.89  ? 315 HOH A O   1 
HETATM 11071 O  O   . HOH DA 7 .   ? 19.444  266.022 18.545  1.00 43.24  ? 316 HOH A O   1 
HETATM 11072 O  O   . HOH DA 7 .   ? 27.354  254.695 10.867  1.00 37.97  ? 317 HOH A O   1 
HETATM 11073 O  O   . HOH DA 7 .   ? 48.448  257.235 8.230   1.00 46.19  ? 318 HOH A O   1 
HETATM 11074 O  O   . HOH DA 7 .   ? 37.637  248.162 37.686  1.00 51.69  ? 319 HOH A O   1 
HETATM 11075 O  O   . HOH DA 7 .   ? 38.967  256.303 31.543  1.00 35.05  ? 320 HOH A O   1 
HETATM 11076 O  O   . HOH DA 7 .   ? 46.330  247.149 27.664  1.00 53.93  ? 321 HOH A O   1 
HETATM 11077 O  O   . HOH DA 7 .   ? 26.849  258.701 29.726  1.00 37.15  ? 322 HOH A O   1 
HETATM 11078 O  O   . HOH DA 7 .   ? 26.222  257.365 10.472  1.00 40.43  ? 323 HOH A O   1 
HETATM 11079 O  O   . HOH DA 7 .   ? 26.961  252.620 9.554   1.00 48.32  ? 324 HOH A O   1 
HETATM 11080 O  O   . HOH DA 7 .   ? 30.109  271.393 21.570  1.00 40.24  ? 325 HOH A O   1 
HETATM 11081 O  O   . HOH DA 7 .   ? 35.816  246.945 18.566  1.00 33.03  ? 326 HOH A O   1 
HETATM 11082 O  O   . HOH DA 7 .   ? 15.000  262.108 17.789  1.00 39.13  ? 327 HOH A O   1 
HETATM 11083 O  O   . HOH DA 7 .   ? 20.318  259.245 8.496   1.00 50.56  ? 328 HOH A O   1 
HETATM 11084 O  O   . HOH DA 7 .   ? 27.263  260.092 -1.186  1.00 47.22  ? 329 HOH A O   1 
HETATM 11085 O  O   . HOH DA 7 .   ? 32.137  262.222 4.214   1.00 45.58  ? 330 HOH A O   1 
HETATM 11086 O  O   . HOH DA 7 .   ? 18.001  263.616 19.955  1.00 30.60  ? 331 HOH A O   1 
HETATM 11087 O  O   . HOH DA 7 .   ? 32.241  244.543 25.505  1.00 38.43  ? 332 HOH A O   1 
HETATM 11088 O  O   . HOH DA 7 .   ? 26.537  266.401 27.367  1.00 35.65  ? 333 HOH A O   1 
HETATM 11089 O  O   . HOH DA 7 .   ? 39.441  250.223 11.420  1.00 37.43  ? 334 HOH A O   1 
HETATM 11090 O  O   . HOH DA 7 .   ? 28.233  269.473 9.252   1.00 44.29  ? 335 HOH A O   1 
HETATM 11091 O  O   A HOH DA 7 .   ? 22.600  263.062 27.478  0.50 28.73  ? 336 HOH A O   1 
HETATM 11092 O  O   B HOH DA 7 .   ? 22.520  260.945 29.122  0.50 30.44  ? 336 HOH A O   1 
HETATM 11093 O  O   . HOH DA 7 .   ? 32.686  282.456 17.432  1.00 48.81  ? 337 HOH A O   1 
HETATM 11094 O  O   A HOH DA 7 .   ? 38.322  265.948 4.477   0.50 8.01   ? 338 HOH A O   1 
HETATM 11095 O  O   B HOH DA 7 .   ? 38.408  268.101 5.220   0.50 24.60  ? 338 HOH A O   1 
HETATM 11096 O  O   . HOH DA 7 .   ? 40.280  280.753 22.980  1.00 48.38  ? 339 HOH A O   1 
HETATM 11097 O  O   . HOH DA 7 .   ? 31.619  257.325 33.682  1.00 48.13  ? 340 HOH A O   1 
HETATM 11098 O  O   . HOH DA 7 .   ? 45.421  257.654 29.633  1.00 45.91  ? 341 HOH A O   1 
HETATM 11099 O  O   . HOH DA 7 .   ? 41.963  265.879 32.074  1.00 41.93  ? 342 HOH A O   1 
HETATM 11100 O  O   . HOH DA 7 .   ? 26.048  254.440 13.577  1.00 41.14  ? 343 HOH A O   1 
HETATM 11101 O  O   . HOH DA 7 .   ? 47.369  258.779 9.881   1.00 37.02  ? 344 HOH A O   1 
HETATM 11102 O  O   . HOH DA 7 .   ? 28.600  264.296 5.716   1.00 50.11  ? 345 HOH A O   1 
HETATM 11103 O  O   . HOH DA 7 .   ? 44.973  271.562 32.114  1.00 49.69  ? 346 HOH A O   1 
HETATM 11104 O  O   . HOH DA 7 .   ? 20.430  257.336 15.518  1.00 24.85  ? 347 HOH A O   1 
HETATM 11105 O  O   . HOH DA 7 .   ? 31.438  274.618 25.860  1.00 44.65  ? 348 HOH A O   1 
HETATM 11106 O  O   . HOH DA 7 .   ? 51.636  257.273 -1.384  1.00 54.03  ? 349 HOH A O   1 
HETATM 11107 O  O   . HOH DA 7 .   ? 30.340  285.585 21.404  1.00 58.36  ? 350 HOH A O   1 
HETATM 11108 O  O   . HOH DA 7 .   ? 29.454  236.565 22.757  1.00 44.17  ? 351 HOH A O   1 
HETATM 11109 O  O   . HOH DA 7 .   ? 35.817  247.681 31.767  1.00 40.68  ? 352 HOH A O   1 
HETATM 11110 O  O   . HOH DA 7 .   ? 41.430  250.500 31.261  1.00 51.07  ? 353 HOH A O   1 
HETATM 11111 O  O   . HOH DA 7 .   ? 45.488  268.192 24.225  1.00 41.17  ? 354 HOH A O   1 
HETATM 11112 O  O   . HOH DA 7 .   ? 28.680  249.573 29.836  1.00 42.06  ? 355 HOH A O   1 
HETATM 11113 O  O   . HOH DA 7 .   ? 46.355  259.840 23.288  1.00 39.66  ? 356 HOH A O   1 
HETATM 11114 O  O   . HOH DA 7 .   ? 22.171  255.351 10.015  1.00 41.58  ? 357 HOH A O   1 
HETATM 11115 O  O   . HOH DA 7 .   ? 25.544  263.641 7.746   1.00 48.00  ? 358 HOH A O   1 
HETATM 11116 O  O   . HOH DA 7 .   ? 42.743  273.363 31.560  1.00 54.39  ? 359 HOH A O   1 
HETATM 11117 O  O   . HOH DA 7 .   ? 36.097  246.295 14.200  1.00 35.29  ? 360 HOH A O   1 
HETATM 11118 O  O   A HOH DA 7 .   ? 41.535  278.358 15.592  0.50 23.31  ? 361 HOH A O   1 
HETATM 11119 O  O   B HOH DA 7 .   ? 40.435  277.917 13.450  0.50 37.03  ? 361 HOH A O   1 
HETATM 11120 O  O   . HOH DA 7 .   ? 50.478  259.846 -3.885  1.00 55.93  ? 362 HOH A O   1 
HETATM 11121 O  O   . HOH DA 7 .   ? 46.400  270.381 9.542   1.00 51.77  ? 363 HOH A O   1 
HETATM 11122 O  O   . HOH DA 7 .   ? 22.380  269.724 24.274  1.00 55.17  ? 364 HOH A O   1 
HETATM 11123 O  O   . HOH DA 7 .   ? 27.068  269.783 34.596  1.00 60.40  ? 365 HOH A O   1 
HETATM 11124 O  O   . HOH DA 7 .   ? 42.069  275.547 26.193  1.00 47.17  ? 366 HOH A O   1 
HETATM 11125 O  O   . HOH DA 7 .   ? 25.027  276.885 21.448  1.00 57.11  ? 367 HOH A O   1 
HETATM 11126 O  O   . HOH DA 7 .   ? 41.255  250.449 2.420   1.00 46.78  ? 368 HOH A O   1 
HETATM 11127 O  O   . HOH DA 7 .   ? 29.288  258.098 -0.096  1.00 40.73  ? 369 HOH A O   1 
HETATM 11128 O  O   . HOH DA 7 .   ? 43.177  264.300 30.688  1.00 36.78  ? 370 HOH A O   1 
HETATM 11129 O  O   . HOH DA 7 .   ? 43.324  261.802 28.992  1.00 41.03  ? 371 HOH A O   1 
HETATM 11130 O  O   . HOH DA 7 .   ? 27.544  271.429 26.061  1.00 49.39  ? 372 HOH A O   1 
HETATM 11131 O  O   . HOH DA 7 .   ? 45.227  255.569 1.066   1.00 51.50  ? 373 HOH A O   1 
HETATM 11132 O  O   . HOH DA 7 .   ? 40.253  275.596 12.838  1.00 44.96  ? 374 HOH A O   1 
HETATM 11133 O  O   . HOH DA 7 .   ? 25.040  257.548 12.942  1.00 40.04  ? 375 HOH A O   1 
HETATM 11134 O  O   . HOH DA 7 .   ? 51.650  257.091 5.601   1.00 56.45  ? 376 HOH A O   1 
HETATM 11135 O  O   . HOH DA 7 .   ? 41.442  252.377 5.561   1.00 52.46  ? 377 HOH A O   1 
HETATM 11136 O  O   . HOH DA 7 .   ? 24.782  259.664 14.462  1.00 42.60  ? 378 HOH A O   1 
HETATM 11137 O  O   . HOH DA 7 .   ? 45.163  260.089 28.735  1.00 50.36  ? 379 HOH A O   1 
HETATM 11138 O  O   . HOH DA 7 .   ? 27.533  251.166 33.026  1.00 37.62  ? 380 HOH A O   1 
HETATM 11139 O  O   . HOH DA 7 .   ? 24.890  271.174 18.242  1.00 38.73  ? 381 HOH A O   1 
HETATM 11140 O  O   . HOH DA 7 .   ? 44.542  266.266 0.510   1.00 41.71  ? 382 HOH A O   1 
HETATM 11141 O  O   . HOH DA 7 .   ? 44.449  251.694 11.842  1.00 50.56  ? 383 HOH A O   1 
HETATM 11142 O  O   . HOH DA 7 .   ? 29.213  243.293 32.451  1.00 59.61  ? 384 HOH A O   1 
HETATM 11143 O  O   . HOH DA 7 .   ? 52.181  261.494 4.680   1.00 50.25  ? 385 HOH A O   1 
HETATM 11144 O  O   . HOH DA 7 .   ? 42.520  271.010 7.867   1.00 42.62  ? 386 HOH A O   1 
HETATM 11145 O  O   . HOH DA 7 .   ? 46.747  269.872 17.987  1.00 51.27  ? 387 HOH A O   1 
HETATM 11146 O  O   . HOH DA 7 .   ? 29.035  256.364 38.371  1.00 41.04  ? 388 HOH A O   1 
HETATM 11147 O  O   . HOH DA 7 .   ? 28.481  235.790 18.832  1.00 46.35  ? 389 HOH A O   1 
HETATM 11148 O  O   . HOH DA 7 .   ? 26.642  265.802 8.419   1.00 56.57  ? 390 HOH A O   1 
HETATM 11149 O  O   . HOH DA 7 .   ? 45.415  273.350 15.645  1.00 48.36  ? 391 HOH A O   1 
HETATM 11150 O  O   . HOH DA 7 .   ? 50.433  263.782 7.865   1.00 39.18  ? 392 HOH A O   1 
HETATM 11151 O  O   . HOH DA 7 .   ? 31.749  239.680 24.683  1.00 45.91  ? 393 HOH A O   1 
HETATM 11152 O  O   . HOH DA 7 .   ? 43.226  250.831 37.109  1.00 52.00  ? 394 HOH A O   1 
HETATM 11153 O  O   . HOH DA 7 .   ? 41.302  274.829 10.747  1.00 44.35  ? 395 HOH A O   1 
HETATM 11154 O  O   . HOH DA 7 .   ? 35.575  246.071 33.893  1.00 39.10  ? 396 HOH A O   1 
HETATM 11155 O  O   . HOH DA 7 .   ? 45.435  280.222 24.550  1.00 55.72  ? 397 HOH A O   1 
HETATM 11156 O  O   . HOH DA 7 .   ? 36.775  266.213 32.552  1.00 44.69  ? 398 HOH A O   1 
HETATM 11157 O  O   . HOH DA 7 .   ? 14.541  264.609 17.310  1.00 48.77  ? 399 HOH A O   1 
HETATM 11158 O  O   . HOH DA 7 .   ? 24.675  262.712 31.321  1.00 48.23  ? 400 HOH A O   1 
HETATM 11159 O  O   . HOH DA 7 .   ? 36.944  264.002 34.529  1.00 47.08  ? 401 HOH A O   1 
HETATM 11160 O  O   . HOH DA 7 .   ? 40.722  253.405 -0.861  1.00 37.57  ? 402 HOH A O   1 
HETATM 11161 O  O   . HOH DA 7 .   ? 39.872  271.420 3.823   1.00 48.56  ? 403 HOH A O   1 
HETATM 11162 O  O   . HOH DA 7 .   ? 33.972  264.848 3.135   1.00 55.07  ? 404 HOH A O   1 
HETATM 11163 O  O   . HOH DA 7 .   ? 34.587  268.783 3.110   1.00 48.68  ? 405 HOH A O   1 
HETATM 11164 O  O   . HOH DA 7 .   ? 45.051  248.411 20.611  1.00 51.92  ? 406 HOH A O   1 
HETATM 11165 O  O   . HOH DA 7 .   ? 23.651  256.078 29.318  1.00 49.53  ? 407 HOH A O   1 
HETATM 11166 O  O   . HOH DA 7 .   ? 28.120  273.908 23.445  1.00 44.21  ? 408 HOH A O   1 
HETATM 11167 O  O   . HOH DA 7 .   ? 39.313  239.322 22.788  1.00 51.86  ? 409 HOH A O   1 
HETATM 11168 O  O   . HOH DA 7 .   ? 45.694  274.090 12.915  1.00 52.12  ? 410 HOH A O   1 
HETATM 11169 O  O   . HOH DA 7 .   ? 25.530  275.322 26.131  1.00 53.46  ? 411 HOH A O   1 
HETATM 11170 O  O   . HOH EA 7 .   ? 5.486   232.431 22.500  1.00 33.80  ? 301 HOH B O   1 
HETATM 11171 O  O   . HOH EA 7 .   ? 1.344   247.044 19.328  1.00 41.32  ? 302 HOH B O   1 
HETATM 11172 O  O   . HOH EA 7 .   ? 16.158  253.107 32.444  1.00 46.41  ? 303 HOH B O   1 
HETATM 11173 O  O   . HOH EA 7 .   ? 1.888   231.274 23.897  1.00 39.89  ? 304 HOH B O   1 
HETATM 11174 O  O   . HOH EA 7 .   ? 8.023   228.623 12.378  1.00 30.92  ? 305 HOH B O   1 
HETATM 11175 O  O   . HOH EA 7 .   ? 16.203  228.377 29.429  1.00 43.87  ? 306 HOH B O   1 
HETATM 11176 O  O   . HOH EA 7 .   ? 13.461  259.400 20.110  1.00 38.47  ? 307 HOH B O   1 
HETATM 11177 O  O   . HOH EA 7 .   ? 20.613  235.341 21.687  1.00 54.16  ? 308 HOH B O   1 
HETATM 11178 O  O   . HOH EA 7 .   ? 12.163  223.827 23.162  1.00 49.81  ? 309 HOH B O   1 
HETATM 11179 O  O   . HOH EA 7 .   ? 20.311  219.324 12.799  1.00 54.12  ? 310 HOH B O   1 
HETATM 11180 O  O   . HOH EA 7 .   ? 5.539   242.858 18.630  1.00 31.59  ? 311 HOH B O   1 
HETATM 11181 O  O   . HOH EA 7 .   ? 10.436  237.765 19.734  1.00 26.77  ? 312 HOH B O   1 
HETATM 11182 O  O   . HOH EA 7 .   ? 9.920   230.691 24.900  1.00 30.81  ? 313 HOH B O   1 
HETATM 11183 O  O   . HOH EA 7 .   ? 28.895  249.709 14.859  1.00 26.89  ? 314 HOH B O   1 
HETATM 11184 O  O   . HOH EA 7 .   ? 23.327  246.083 28.627  1.00 42.70  ? 315 HOH B O   1 
HETATM 11185 O  O   . HOH EA 7 .   ? 18.086  237.039 28.070  1.00 38.76  ? 316 HOH B O   1 
HETATM 11186 O  O   . HOH EA 7 .   ? 18.235  250.347 3.597   1.00 33.87  ? 317 HOH B O   1 
HETATM 11187 O  O   . HOH EA 7 .   ? 6.141   243.690 25.001  1.00 42.26  ? 318 HOH B O   1 
HETATM 11188 O  O   . HOH EA 7 .   ? 18.035  246.522 33.138  1.00 28.93  ? 319 HOH B O   1 
HETATM 11189 O  O   . HOH EA 7 .   ? 12.133  258.868 22.448  1.00 44.99  ? 320 HOH B O   1 
HETATM 11190 O  O   . HOH EA 7 .   ? 31.543  242.886 18.081  1.00 32.89  ? 321 HOH B O   1 
HETATM 11191 O  O   . HOH EA 7 .   ? 27.277  241.857 25.420  1.00 38.14  ? 322 HOH B O   1 
HETATM 11192 O  O   . HOH EA 7 .   ? 4.313   256.313 8.617   1.00 50.37  ? 323 HOH B O   1 
HETATM 11193 O  O   . HOH EA 7 .   ? 24.145  244.303 6.397   1.00 54.42  ? 324 HOH B O   1 
HETATM 11194 O  O   . HOH EA 7 .   ? 19.381  234.562 18.698  1.00 30.55  ? 325 HOH B O   1 
HETATM 11195 O  O   . HOH EA 7 .   ? 0.168   234.976 23.387  1.00 38.55  ? 326 HOH B O   1 
HETATM 11196 O  O   . HOH EA 7 .   ? 8.084   236.898 34.596  1.00 59.60  ? 327 HOH B O   1 
HETATM 11197 O  O   . HOH EA 7 .   ? 21.779  252.871 10.661  1.00 32.24  ? 328 HOH B O   1 
HETATM 11198 O  O   . HOH EA 7 .   ? 7.363   253.221 37.271  1.00 46.25  ? 329 HOH B O   1 
HETATM 11199 O  O   . HOH EA 7 .   ? 20.746  254.592 14.857  1.00 22.22  ? 330 HOH B O   1 
HETATM 11200 O  O   . HOH EA 7 .   ? -0.125  228.666 22.563  1.00 39.64  ? 331 HOH B O   1 
HETATM 11201 O  O   . HOH EA 7 .   ? 20.800  238.662 7.059   1.00 33.59  ? 332 HOH B O   1 
HETATM 11202 O  O   . HOH EA 7 .   ? 0.774   250.850 8.838   1.00 46.08  ? 333 HOH B O   1 
HETATM 11203 O  O   A HOH EA 7 .   ? 23.304  238.604 24.767  0.50 18.26  ? 334 HOH B O   1 
HETATM 11204 O  O   B HOH EA 7 .   ? 23.936  237.074 23.725  0.50 29.60  ? 334 HOH B O   1 
HETATM 11205 O  O   . HOH EA 7 .   ? 25.432  237.023 12.763  1.00 42.17  ? 335 HOH B O   1 
HETATM 11206 O  O   . HOH EA 7 .   ? 8.518   232.786 9.534   1.00 35.91  ? 336 HOH B O   1 
HETATM 11207 O  O   . HOH EA 7 .   ? 23.334  252.829 13.572  1.00 36.61  ? 337 HOH B O   1 
HETATM 11208 O  O   . HOH EA 7 .   ? 18.238  230.707 22.454  1.00 34.39  ? 338 HOH B O   1 
HETATM 11209 O  O   . HOH EA 7 .   ? 9.252   225.549 19.573  1.00 25.29  ? 339 HOH B O   1 
HETATM 11210 O  O   . HOH EA 7 .   ? 4.493   237.254 22.802  1.00 25.45  ? 340 HOH B O   1 
HETATM 11211 O  O   . HOH EA 7 .   ? 5.308   246.446 29.438  1.00 40.49  ? 341 HOH B O   1 
HETATM 11212 O  O   . HOH EA 7 .   ? 19.397  225.747 13.900  1.00 39.12  ? 342 HOH B O   1 
HETATM 11213 O  O   . HOH EA 7 .   ? 15.886  236.616 14.313  1.00 33.77  ? 343 HOH B O   1 
HETATM 11214 O  O   . HOH EA 7 .   ? 11.749  244.626 1.460   1.00 31.60  ? 344 HOH B O   1 
HETATM 11215 O  O   . HOH EA 7 .   ? -2.343  251.101 3.381   1.00 47.81  ? 345 HOH B O   1 
HETATM 11216 O  O   . HOH EA 7 .   ? 0.795   250.201 21.405  1.00 53.81  ? 346 HOH B O   1 
HETATM 11217 O  O   . HOH EA 7 .   ? 6.828   243.462 28.648  1.00 42.52  ? 347 HOH B O   1 
HETATM 11218 O  O   . HOH EA 7 .   ? 16.685  246.676 2.999   1.00 29.32  ? 348 HOH B O   1 
HETATM 11219 O  O   . HOH EA 7 .   ? 1.814   249.179 10.339  1.00 31.60  ? 349 HOH B O   1 
HETATM 11220 O  O   . HOH EA 7 .   ? 10.488  243.128 3.181   1.00 27.40  ? 350 HOH B O   1 
HETATM 11221 O  O   . HOH EA 7 .   ? 7.381   231.489 28.965  1.00 42.04  ? 351 HOH B O   1 
HETATM 11222 O  O   . HOH EA 7 .   ? 16.995  235.350 12.001  1.00 39.88  ? 352 HOH B O   1 
HETATM 11223 O  O   . HOH EA 7 .   ? 34.470  244.520 15.318  1.00 40.02  ? 353 HOH B O   1 
HETATM 11224 O  O   . HOH EA 7 .   ? 26.044  244.407 4.266   1.00 51.05  ? 354 HOH B O   1 
HETATM 11225 O  O   . HOH EA 7 .   ? 7.181   251.109 1.652   1.00 41.61  ? 355 HOH B O   1 
HETATM 11226 O  O   . HOH EA 7 .   ? 4.092   224.645 18.742  1.00 33.23  ? 356 HOH B O   1 
HETATM 11227 O  O   . HOH EA 7 .   ? 4.691   232.085 28.392  1.00 42.22  ? 357 HOH B O   1 
HETATM 11228 O  O   . HOH EA 7 .   ? 13.056  260.799 16.154  1.00 35.18  ? 358 HOH B O   1 
HETATM 11229 O  O   . HOH EA 7 .   ? 29.979  240.539 16.433  1.00 43.34  ? 359 HOH B O   1 
HETATM 11230 O  O   . HOH EA 7 .   ? 4.732   239.976 18.616  1.00 34.15  ? 360 HOH B O   1 
HETATM 11231 O  O   . HOH EA 7 .   ? 11.901  247.979 31.766  1.00 51.17  ? 361 HOH B O   1 
HETATM 11232 O  O   . HOH EA 7 .   ? 4.298   254.667 14.329  1.00 45.64  ? 362 HOH B O   1 
HETATM 11233 O  O   . HOH EA 7 .   ? 17.733  260.476 27.401  1.00 38.52  ? 363 HOH B O   1 
HETATM 11234 O  O   . HOH EA 7 .   ? 22.908  250.467 9.752   1.00 45.07  ? 364 HOH B O   1 
HETATM 11235 O  O   A HOH EA 7 .   ? 15.880  232.450 10.847  0.50 18.76  ? 365 HOH B O   1 
HETATM 11236 O  O   B HOH EA 7 .   ? 14.956  230.971 9.262   0.50 23.11  ? 365 HOH B O   1 
HETATM 11237 O  O   . HOH EA 7 .   ? 21.977  249.778 -1.393  1.00 39.07  ? 366 HOH B O   1 
HETATM 11238 O  O   . HOH EA 7 .   ? 22.822  251.935 33.478  1.00 33.65  ? 367 HOH B O   1 
HETATM 11239 O  O   . HOH EA 7 .   ? 20.274  250.902 0.537   1.00 53.42  ? 368 HOH B O   1 
HETATM 11240 O  O   . HOH EA 7 .   ? -0.146  232.247 22.721  1.00 46.22  ? 369 HOH B O   1 
HETATM 11241 O  O   . HOH EA 7 .   ? 21.006  255.567 30.641  1.00 45.92  ? 370 HOH B O   1 
HETATM 11242 O  O   . HOH EA 7 .   ? 23.301  233.964 31.333  1.00 50.31  ? 371 HOH B O   1 
HETATM 11243 O  O   . HOH EA 7 .   ? 15.130  264.733 20.264  1.00 48.65  ? 372 HOH B O   1 
HETATM 11244 O  O   . HOH EA 7 .   ? 8.693   253.928 32.410  1.00 38.29  ? 373 HOH B O   1 
HETATM 11245 O  O   . HOH EA 7 .   ? 11.448  231.293 32.401  1.00 46.90  ? 374 HOH B O   1 
HETATM 11246 O  O   . HOH EA 7 .   ? 18.975  228.199 27.198  1.00 49.89  ? 375 HOH B O   1 
HETATM 11247 O  O   . HOH EA 7 .   ? 15.556  237.345 29.412  1.00 31.12  ? 376 HOH B O   1 
HETATM 11248 O  O   . HOH EA 7 .   ? -2.847  247.361 4.450   1.00 58.03  ? 377 HOH B O   1 
HETATM 11249 O  O   . HOH EA 7 .   ? 14.942  229.257 31.736  1.00 40.69  ? 378 HOH B O   1 
HETATM 11250 O  O   . HOH EA 7 .   ? 10.783  240.563 3.357   1.00 35.40  ? 379 HOH B O   1 
HETATM 11251 O  O   . HOH EA 7 .   ? 18.417  226.761 10.366  1.00 38.43  ? 380 HOH B O   1 
HETATM 11252 O  O   . HOH EA 7 .   ? 12.025  228.510 21.769  1.00 43.64  ? 381 HOH B O   1 
HETATM 11253 O  O   . HOH EA 7 .   ? 20.789  244.380 4.754   1.00 47.22  ? 382 HOH B O   1 
HETATM 11254 O  O   . HOH EA 7 .   ? 23.692  242.283 30.832  1.00 46.00  ? 383 HOH B O   1 
HETATM 11255 O  O   . HOH EA 7 .   ? 2.730   237.726 7.395   1.00 33.42  ? 384 HOH B O   1 
HETATM 11256 O  O   . HOH EA 7 .   ? 19.446  229.497 24.906  1.00 47.44  ? 385 HOH B O   1 
HETATM 11257 O  O   A HOH EA 7 .   ? 20.254  236.231 11.134  0.50 19.39  ? 386 HOH B O   1 
HETATM 11258 O  O   B HOH EA 7 .   ? 20.117  234.554 9.687   0.50 31.21  ? 386 HOH B O   1 
HETATM 11259 O  O   . HOH EA 7 .   ? 7.541   238.775 29.960  1.00 39.22  ? 387 HOH B O   1 
HETATM 11260 O  O   . HOH EA 7 .   ? 3.352   245.732 23.183  1.00 31.52  ? 388 HOH B O   1 
HETATM 11261 O  O   . HOH EA 7 .   ? 7.818   255.336 29.430  1.00 39.19  ? 389 HOH B O   1 
HETATM 11262 O  O   . HOH EA 7 .   ? 23.751  247.996 8.026   1.00 41.94  ? 390 HOH B O   1 
HETATM 11263 O  O   . HOH EA 7 .   ? -2.463  251.366 6.245   1.00 44.56  ? 391 HOH B O   1 
HETATM 11264 O  O   A HOH EA 7 .   ? 4.197   252.643 22.372  0.50 14.17  ? 392 HOH B O   1 
HETATM 11265 O  O   B HOH EA 7 .   ? 3.088   252.237 24.364  0.50 42.59  ? 392 HOH B O   1 
HETATM 11266 O  O   . HOH EA 7 .   ? 24.807  248.599 31.270  1.00 45.86  ? 393 HOH B O   1 
HETATM 11267 O  O   . HOH EA 7 .   ? 13.857  245.038 33.161  1.00 52.53  ? 394 HOH B O   1 
HETATM 11268 O  O   . HOH EA 7 .   ? 6.806   247.446 34.566  1.00 51.17  ? 395 HOH B O   1 
HETATM 11269 O  O   . HOH EA 7 .   ? 24.993  237.914 31.357  1.00 51.32  ? 396 HOH B O   1 
HETATM 11270 O  O   . HOH EA 7 .   ? 23.415  223.682 16.098  1.00 51.54  ? 397 HOH B O   1 
HETATM 11271 O  O   . HOH EA 7 .   ? 19.105  236.386 13.288  1.00 36.24  ? 398 HOH B O   1 
HETATM 11272 O  O   . HOH EA 7 .   ? -0.921  243.988 6.745   1.00 41.34  ? 399 HOH B O   1 
HETATM 11273 O  O   . HOH EA 7 .   ? 27.746  236.142 21.091  1.00 48.15  ? 400 HOH B O   1 
HETATM 11274 O  O   . HOH EA 7 .   ? 11.975  231.994 34.802  1.00 57.92  ? 401 HOH B O   1 
HETATM 11275 O  O   . HOH EA 7 .   ? 7.790   227.189 23.278  1.00 37.55  ? 402 HOH B O   1 
HETATM 11276 O  O   . HOH EA 7 .   ? 18.580  241.083 35.875  1.00 45.78  ? 403 HOH B O   1 
HETATM 11277 O  O   . HOH EA 7 .   ? 10.032  242.604 33.814  1.00 41.68  ? 404 HOH B O   1 
HETATM 11278 O  O   . HOH EA 7 .   ? 7.697   230.020 23.283  1.00 40.00  ? 405 HOH B O   1 
HETATM 11279 O  O   . HOH EA 7 .   ? 16.305  224.157 12.614  1.00 35.22  ? 406 HOH B O   1 
HETATM 11280 O  O   A HOH EA 7 .   ? 24.210  248.433 13.385  0.50 16.15  ? 407 HOH B O   1 
HETATM 11281 O  O   B HOH EA 7 .   ? 24.951  246.544 13.153  0.50 20.63  ? 407 HOH B O   1 
HETATM 11282 O  O   . HOH EA 7 .   ? 24.471  235.861 14.951  1.00 32.58  ? 408 HOH B O   1 
HETATM 11283 O  O   . HOH EA 7 .   ? 10.783  256.612 8.831   1.00 52.98  ? 409 HOH B O   1 
HETATM 11284 O  O   A HOH EA 7 .   ? 15.303  256.350 7.987   0.50 22.47  ? 410 HOH B O   1 
HETATM 11285 O  O   B HOH EA 7 .   ? 13.184  256.751 7.446   0.50 24.44  ? 410 HOH B O   1 
HETATM 11286 O  O   . HOH EA 7 .   ? 4.152   239.142 -3.274  1.00 50.27  ? 411 HOH B O   1 
HETATM 11287 O  O   . HOH EA 7 .   ? 4.197   233.800 30.321  1.00 44.86  ? 412 HOH B O   1 
HETATM 11288 O  O   . HOH EA 7 .   ? 9.451   257.606 12.491  1.00 48.06  ? 413 HOH B O   1 
HETATM 11289 O  O   . HOH EA 7 .   ? 15.784  225.266 10.430  1.00 37.79  ? 414 HOH B O   1 
HETATM 11290 O  O   . HOH EA 7 .   ? 22.538  242.203 7.010   1.00 50.52  ? 415 HOH B O   1 
HETATM 11291 O  O   . HOH EA 7 .   ? 24.306  250.725 12.112  1.00 45.20  ? 416 HOH B O   1 
HETATM 11292 O  O   A HOH EA 7 .   ? 7.642   237.630 4.287   0.50 23.20  ? 417 HOH B O   1 
HETATM 11293 O  O   B HOH EA 7 .   ? 6.264   238.321 6.093   0.50 25.82  ? 417 HOH B O   1 
HETATM 11294 O  O   . HOH EA 7 .   ? 12.998  242.512 33.566  1.00 55.58  ? 418 HOH B O   1 
HETATM 11295 O  O   . HOH EA 7 .   ? 3.270   234.378 14.942  1.00 39.10  ? 419 HOH B O   1 
HETATM 11296 O  O   . HOH EA 7 .   ? 8.281   256.732 0.451   1.00 45.52  ? 420 HOH B O   1 
HETATM 11297 O  O   . HOH EA 7 .   ? 7.314   233.539 7.478   1.00 45.16  ? 421 HOH B O   1 
HETATM 11298 O  O   . HOH EA 7 .   ? -0.081  251.895 29.460  1.00 47.89  ? 422 HOH B O   1 
HETATM 11299 O  O   . HOH EA 7 .   ? 17.496  223.825 30.228  1.00 57.14  ? 423 HOH B O   1 
HETATM 11300 O  O   . HOH EA 7 .   ? 20.220  235.624 15.991  1.00 34.52  ? 424 HOH B O   1 
HETATM 11301 O  O   . HOH EA 7 .   ? 23.555  249.363 6.100   1.00 36.88  ? 425 HOH B O   1 
HETATM 11302 O  O   . HOH EA 7 .   ? 10.614  260.002 14.163  1.00 41.97  ? 426 HOH B O   1 
HETATM 11303 O  O   . HOH EA 7 .   ? -0.226  255.947 2.193   1.00 49.94  ? 427 HOH B O   1 
HETATM 11304 O  O   . HOH EA 7 .   ? 3.663   234.504 22.709  1.00 38.05  ? 428 HOH B O   1 
HETATM 11305 O  O   . HOH EA 7 .   ? 12.254  247.489 34.411  1.00 44.88  ? 429 HOH B O   1 
HETATM 11306 O  O   . HOH EA 7 .   ? 8.066   261.198 17.441  1.00 50.51  ? 430 HOH B O   1 
HETATM 11307 O  O   . HOH EA 7 .   ? 12.418  237.885 30.791  1.00 36.71  ? 431 HOH B O   1 
HETATM 11308 O  O   . HOH EA 7 .   ? 21.124  230.903 14.865  1.00 45.33  ? 432 HOH B O   1 
HETATM 11309 O  O   . HOH EA 7 .   ? 22.207  234.401 15.302  1.00 49.74  ? 433 HOH B O   1 
HETATM 11310 O  O   . HOH EA 7 .   ? 8.733   255.011 40.837  1.00 51.15  ? 434 HOH B O   1 
HETATM 11311 O  O   . HOH EA 7 .   ? 18.296  255.434 35.900  1.00 43.02  ? 435 HOH B O   1 
HETATM 11312 O  O   . HOH EA 7 .   ? 14.129  262.067 20.009  1.00 44.59  ? 436 HOH B O   1 
HETATM 11313 O  O   . HOH EA 7 .   ? 13.753  239.537 1.364   1.00 52.34  ? 437 HOH B O   1 
HETATM 11314 O  O   . HOH EA 7 .   ? 10.277  262.059 18.753  1.00 46.94  ? 438 HOH B O   1 
HETATM 11315 O  O   . HOH EA 7 .   ? 20.671  268.999 19.445  1.00 45.84  ? 439 HOH B O   1 
HETATM 11316 O  O   . HOH EA 7 .   ? 2.591   255.729 18.360  1.00 48.11  ? 440 HOH B O   1 
HETATM 11317 O  O   . HOH EA 7 .   ? 17.440  239.117 1.693   1.00 45.40  ? 441 HOH B O   1 
HETATM 11318 O  O   . HOH EA 7 .   ? 27.384  247.070 4.701   1.00 52.35  ? 442 HOH B O   1 
HETATM 11319 O  O   . HOH EA 7 .   ? 21.412  234.173 11.912  1.00 53.85  ? 443 HOH B O   1 
HETATM 11320 O  O   . HOH EA 7 .   ? 28.979  238.336 15.438  1.00 47.63  ? 444 HOH B O   1 
HETATM 11321 O  O   . HOH EA 7 .   ? -0.164  239.899 4.160   1.00 46.97  ? 445 HOH B O   1 
HETATM 11322 O  O   . HOH EA 7 .   ? 22.452  228.285 29.714  1.00 49.79  ? 446 HOH B O   1 
HETATM 11323 O  O   . HOH EA 7 .   ? 6.738   254.166 1.890   1.00 46.40  ? 447 HOH B O   1 
HETATM 11324 O  O   . HOH EA 7 .   ? 15.616  244.330 1.722   1.00 39.93  ? 448 HOH B O   1 
HETATM 11325 O  O   . HOH EA 7 .   ? 7.503   223.968 20.895  1.00 35.76  ? 449 HOH B O   1 
HETATM 11326 O  O   . HOH EA 7 .   ? 3.541   238.857 21.124  1.00 32.33  ? 450 HOH B O   1 
HETATM 11327 O  O   . HOH EA 7 .   ? 26.211  247.685 29.446  1.00 48.06  ? 451 HOH B O   1 
HETATM 11328 O  O   . HOH EA 7 .   ? 3.761   226.118 21.083  1.00 34.80  ? 452 HOH B O   1 
HETATM 11329 O  O   . HOH EA 7 .   ? 6.080   225.550 22.280  1.00 36.48  ? 453 HOH B O   1 
HETATM 11330 O  O   . HOH EA 7 .   ? 3.096   241.851 27.315  1.00 48.21  ? 454 HOH B O   1 
HETATM 11331 O  O   . HOH EA 7 .   ? 14.045  257.511 39.483  1.00 52.52  ? 455 HOH B O   1 
HETATM 11332 O  O   A HOH EA 7 .   ? 4.749   258.131 22.827  0.50 23.61  ? 456 HOH B O   1 
HETATM 11333 O  O   B HOH EA 7 .   ? 3.999   257.537 21.257  0.50 34.04  ? 456 HOH B O   1 
HETATM 11334 O  O   . HOH EA 7 .   ? 5.732   230.755 33.249  1.00 56.20  ? 457 HOH B O   1 
HETATM 11335 O  O   . HOH EA 7 .   ? -0.291  238.087 8.775   1.00 45.07  ? 458 HOH B O   1 
HETATM 11336 O  O   . HOH EA 7 .   ? 3.688   234.880 8.418   1.00 50.67  ? 459 HOH B O   1 
HETATM 11337 O  O   . HOH EA 7 .   ? 4.423   230.820 12.622  1.00 48.45  ? 460 HOH B O   1 
HETATM 11338 O  O   . HOH EA 7 .   ? 29.179  234.581 25.170  1.00 51.30  ? 461 HOH B O   1 
HETATM 11339 O  O   . HOH FA 7 .   ? -1.784  193.891 31.074  1.00 34.31  ? 301 HOH C O   1 
HETATM 11340 O  O   . HOH FA 7 .   ? 4.661   179.319 20.032  1.00 45.55  ? 302 HOH C O   1 
HETATM 11341 O  O   . HOH FA 7 .   ? 3.758   189.502 0.694   1.00 34.20  ? 303 HOH C O   1 
HETATM 11342 O  O   . HOH FA 7 .   ? -3.230  178.800 3.205   1.00 43.06  ? 304 HOH C O   1 
HETATM 11343 O  O   . HOH FA 7 .   ? -3.657  188.998 11.239  1.00 48.29  ? 305 HOH C O   1 
HETATM 11344 O  O   . HOH FA 7 .   ? 1.855   172.333 4.914   1.00 43.34  ? 306 HOH C O   1 
HETATM 11345 O  O   . HOH FA 7 .   ? 1.101   192.721 34.146  1.00 36.73  ? 307 HOH C O   1 
HETATM 11346 O  O   . HOH FA 7 .   ? 5.449   192.597 33.694  1.00 52.61  ? 308 HOH C O   1 
HETATM 11347 O  O   . HOH FA 7 .   ? -5.118  193.801 18.212  1.00 39.77  ? 309 HOH C O   1 
HETATM 11348 O  O   . HOH FA 7 .   ? -8.043  183.841 18.661  1.00 49.46  ? 310 HOH C O   1 
HETATM 11349 O  O   . HOH FA 7 .   ? 1.127   186.834 31.300  1.00 27.80  ? 311 HOH C O   1 
HETATM 11350 O  O   . HOH FA 7 .   ? 5.996   197.479 10.814  1.00 33.05  ? 312 HOH C O   1 
HETATM 11351 O  O   . HOH FA 7 .   ? 3.330   180.351 25.106  1.00 41.36  ? 313 HOH C O   1 
HETATM 11352 O  O   . HOH FA 7 .   ? 20.816  194.648 25.204  1.00 49.60  ? 314 HOH C O   1 
HETATM 11353 O  O   . HOH FA 7 .   ? 7.833   192.613 3.821   1.00 33.39  ? 315 HOH C O   1 
HETATM 11354 O  O   . HOH FA 7 .   ? -0.795  180.393 28.943  1.00 42.05  ? 316 HOH C O   1 
HETATM 11355 O  O   . HOH FA 7 .   ? 1.949   178.893 13.363  1.00 40.21  ? 317 HOH C O   1 
HETATM 11356 O  O   . HOH FA 7 .   ? 16.599  184.180 16.963  1.00 45.67  ? 318 HOH C O   1 
HETATM 11357 O  O   . HOH FA 7 .   ? 3.288   197.783 14.476  1.00 25.60  ? 319 HOH C O   1 
HETATM 11358 O  O   . HOH FA 7 .   ? 18.886  184.659 15.178  1.00 55.97  ? 320 HOH C O   1 
HETATM 11359 O  O   . HOH FA 7 .   ? 14.083  187.053 30.068  1.00 41.36  ? 321 HOH C O   1 
HETATM 11360 O  O   . HOH FA 7 .   ? -0.121  177.809 10.753  1.00 41.41  ? 322 HOH C O   1 
HETATM 11361 O  O   . HOH FA 7 .   ? -6.805  200.111 17.775  1.00 37.45  ? 323 HOH C O   1 
HETATM 11362 O  O   . HOH FA 7 .   ? 18.204  204.712 17.698  1.00 44.80  ? 324 HOH C O   1 
HETATM 11363 O  O   . HOH FA 7 .   ? 20.844  176.543 7.328   1.00 53.56  ? 325 HOH C O   1 
HETATM 11364 O  O   . HOH FA 7 .   ? 11.388  180.525 21.493  1.00 37.82  ? 326 HOH C O   1 
HETATM 11365 O  O   . HOH FA 7 .   ? 10.207  184.586 2.680   1.00 36.51  ? 327 HOH C O   1 
HETATM 11366 O  O   . HOH FA 7 .   ? 15.210  197.256 27.449  1.00 38.11  ? 328 HOH C O   1 
HETATM 11367 O  O   . HOH FA 7 .   ? 2.435   183.557 1.331   1.00 38.61  ? 329 HOH C O   1 
HETATM 11368 O  O   . HOH FA 7 .   ? -5.726  187.827 30.949  1.00 50.33  ? 330 HOH C O   1 
HETATM 11369 O  O   . HOH FA 7 .   ? -2.014  197.135 35.028  1.00 42.38  ? 331 HOH C O   1 
HETATM 11370 O  O   . HOH FA 7 .   ? 18.712  189.337 9.726   1.00 37.38  ? 332 HOH C O   1 
HETATM 11371 O  O   . HOH FA 7 .   ? 21.148  181.766 32.925  1.00 51.32  ? 333 HOH C O   1 
HETATM 11372 O  O   . HOH FA 7 .   ? 19.954  173.834 15.869  1.00 48.75  ? 334 HOH C O   1 
HETATM 11373 O  O   . HOH FA 7 .   ? 18.930  191.740 10.956  1.00 52.11  ? 335 HOH C O   1 
HETATM 11374 O  O   . HOH FA 7 .   ? 16.296  192.313 27.132  1.00 45.36  ? 336 HOH C O   1 
HETATM 11375 O  O   . HOH FA 7 .   ? 12.874  185.101 31.383  1.00 40.42  ? 337 HOH C O   1 
HETATM 11376 O  O   . HOH FA 7 .   ? 2.975   179.024 17.759  1.00 42.65  ? 338 HOH C O   1 
HETATM 11377 O  O   . HOH FA 7 .   ? -6.581  193.243 35.342  1.00 45.28  ? 339 HOH C O   1 
HETATM 11378 O  O   . HOH FA 7 .   ? 13.603  191.794 6.064   1.00 47.77  ? 340 HOH C O   1 
HETATM 11379 O  O   . HOH FA 7 .   ? 19.536  199.008 18.937  1.00 40.54  ? 341 HOH C O   1 
HETATM 11380 O  O   . HOH FA 7 .   ? -5.587  182.597 20.216  1.00 51.67  ? 342 HOH C O   1 
HETATM 11381 O  O   . HOH FA 7 .   ? 12.675  197.021 14.795  1.00 47.01  ? 343 HOH C O   1 
HETATM 11382 O  O   . HOH FA 7 .   ? 28.971  172.564 21.027  1.00 55.23  ? 344 HOH C O   1 
HETATM 11383 O  O   . HOH FA 7 .   ? 6.123   199.002 13.483  1.00 30.93  ? 345 HOH C O   1 
HETATM 11384 O  O   . HOH FA 7 .   ? 7.972   174.532 17.754  1.00 44.25  ? 346 HOH C O   1 
HETATM 11385 O  O   . HOH FA 7 .   ? -9.774  191.254 20.058  1.00 50.25  ? 347 HOH C O   1 
HETATM 11386 O  O   . HOH FA 7 .   ? 11.305  202.421 15.583  1.00 25.71  ? 348 HOH C O   1 
HETATM 11387 O  O   . HOH FA 7 .   ? 20.912  185.653 11.202  1.00 48.42  ? 349 HOH C O   1 
HETATM 11388 O  O   . HOH FA 7 .   ? 7.205   178.980 31.337  1.00 42.46  ? 350 HOH C O   1 
HETATM 11389 O  O   . HOH FA 7 .   ? 10.529  182.547 4.661   1.00 39.86  ? 351 HOH C O   1 
HETATM 11390 O  O   . HOH FA 7 .   ? -14.351 187.552 29.708  1.00 61.33  ? 352 HOH C O   1 
HETATM 11391 O  O   . HOH FA 7 .   ? 3.450   180.369 28.550  1.00 53.65  ? 353 HOH C O   1 
HETATM 11392 O  O   . HOH FA 7 .   ? 10.442  189.626 4.104   1.00 38.79  ? 354 HOH C O   1 
HETATM 11393 O  O   A HOH FA 7 .   ? 12.318  176.141 8.169   0.50 27.90  ? 355 HOH C O   1 
HETATM 11394 O  O   B HOH FA 7 .   ? 11.432  176.827 6.808   0.50 29.05  ? 355 HOH C O   1 
HETATM 11395 O  O   . HOH FA 7 .   ? 22.136  184.875 29.749  1.00 49.88  ? 356 HOH C O   1 
HETATM 11396 O  O   . HOH FA 7 .   ? -11.057 204.281 23.235  1.00 42.93  ? 357 HOH C O   1 
HETATM 11397 O  O   . HOH FA 7 .   ? 5.625   182.056 0.226   1.00 41.40  ? 358 HOH C O   1 
HETATM 11398 O  O   . HOH FA 7 .   ? -6.392  186.310 37.323  1.00 56.33  ? 359 HOH C O   1 
HETATM 11399 O  O   . HOH FA 7 .   ? -6.622  187.379 27.949  1.00 39.98  ? 360 HOH C O   1 
HETATM 11400 O  O   . HOH FA 7 .   ? 20.156  185.004 5.360   1.00 48.76  ? 361 HOH C O   1 
HETATM 11401 O  O   . HOH FA 7 .   ? 10.530  173.478 9.266   1.00 39.48  ? 362 HOH C O   1 
HETATM 11402 O  O   . HOH FA 7 .   ? 20.230  196.411 8.567   1.00 53.91  ? 363 HOH C O   1 
HETATM 11403 O  O   . HOH FA 7 .   ? -5.459  198.429 25.375  1.00 42.82  ? 364 HOH C O   1 
HETATM 11404 O  O   . HOH FA 7 .   ? 9.021   197.232 10.016  1.00 42.15  ? 365 HOH C O   1 
HETATM 11405 O  O   . HOH FA 7 .   ? 8.057   183.626 -0.115  1.00 35.09  ? 366 HOH C O   1 
HETATM 11406 O  O   . HOH FA 7 .   ? 0.835   179.406 16.433  1.00 31.57  ? 367 HOH C O   1 
HETATM 11407 O  O   . HOH FA 7 .   ? -1.128  177.974 8.368   1.00 45.90  ? 368 HOH C O   1 
HETATM 11408 O  O   . HOH FA 7 .   ? 7.964   197.181 35.981  1.00 50.24  ? 369 HOH C O   1 
HETATM 11409 O  O   . HOH FA 7 .   ? 1.922   193.942 6.908   1.00 43.32  ? 370 HOH C O   1 
HETATM 11410 O  O   . HOH FA 7 .   ? 32.554  181.720 19.124  1.00 48.01  ? 371 HOH C O   1 
HETATM 11411 O  O   . HOH FA 7 .   ? 1.010   188.260 0.476   1.00 40.71  ? 372 HOH C O   1 
HETATM 11412 O  O   . HOH FA 7 .   ? 7.863   177.360 0.280   1.00 40.49  ? 373 HOH C O   1 
HETATM 11413 O  O   . HOH FA 7 .   ? 6.085   176.861 19.579  1.00 44.35  ? 374 HOH C O   1 
HETATM 11414 O  O   . HOH FA 7 .   ? 8.344   175.180 24.104  1.00 54.29  ? 375 HOH C O   1 
HETATM 11415 O  O   . HOH FA 7 .   ? -0.272  184.613 33.665  1.00 45.29  ? 376 HOH C O   1 
HETATM 11416 O  O   . HOH FA 7 .   ? -2.500  177.562 14.411  1.00 48.53  ? 377 HOH C O   1 
HETATM 11417 O  O   . HOH FA 7 .   ? -7.305  178.915 17.503  1.00 45.89  ? 378 HOH C O   1 
HETATM 11418 O  O   . HOH FA 7 .   ? -5.929  194.372 13.891  1.00 42.06  ? 379 HOH C O   1 
HETATM 11419 O  O   . HOH FA 7 .   ? -9.853  204.450 16.858  1.00 49.47  ? 380 HOH C O   1 
HETATM 11420 O  O   . HOH FA 7 .   ? 10.404  184.654 33.890  1.00 64.05  ? 381 HOH C O   1 
HETATM 11421 O  O   A HOH FA 7 .   ? 10.988  197.563 8.332   0.50 27.38  ? 382 HOH C O   1 
HETATM 11422 O  O   B HOH FA 7 .   ? 11.479  197.319 6.780   0.50 31.32  ? 382 HOH C O   1 
HETATM 11423 O  O   . HOH FA 7 .   ? 14.320  191.666 -0.595  1.00 40.12  ? 383 HOH C O   1 
HETATM 11424 O  O   . HOH FA 7 .   ? 18.241  187.086 16.120  1.00 45.68  ? 384 HOH C O   1 
HETATM 11425 O  O   . HOH FA 7 .   ? 1.657   181.702 -2.233  1.00 46.05  ? 385 HOH C O   1 
HETATM 11426 O  O   . HOH FA 7 .   ? 17.056  188.579 6.081   1.00 54.82  ? 386 HOH C O   1 
HETATM 11427 O  O   . HOH FA 7 .   ? 13.160  196.283 35.233  1.00 46.85  ? 387 HOH C O   1 
HETATM 11428 O  O   . HOH FA 7 .   ? 15.183  200.538 7.322   1.00 48.60  ? 388 HOH C O   1 
HETATM 11429 O  O   . HOH FA 7 .   ? -2.997  172.265 -4.577  1.00 54.46  ? 389 HOH C O   1 
HETATM 11430 O  O   . HOH FA 7 .   ? 0.746   178.288 22.875  1.00 43.84  ? 390 HOH C O   1 
HETATM 11431 O  O   . HOH FA 7 .   ? 2.717   199.373 32.847  1.00 44.53  ? 391 HOH C O   1 
HETATM 11432 O  O   . HOH FA 7 .   ? -5.568  190.300 12.086  1.00 38.97  ? 392 HOH C O   1 
HETATM 11433 O  O   . HOH FA 7 .   ? 14.764  175.394 9.518   1.00 53.41  ? 393 HOH C O   1 
HETATM 11434 O  O   . HOH FA 7 .   ? 8.939   198.776 12.733  1.00 37.25  ? 394 HOH C O   1 
HETATM 11435 O  O   . HOH FA 7 .   ? 2.547   192.974 -1.625  1.00 40.77  ? 395 HOH C O   1 
HETATM 11436 O  O   . HOH FA 7 .   ? -5.568  183.389 13.256  1.00 54.77  ? 396 HOH C O   1 
HETATM 11437 O  O   A HOH FA 7 .   ? 21.311  191.646 18.325  0.25 1.00   ? 397 HOH C O   1 
HETATM 11438 O  O   B HOH FA 7 .   ? 21.186  189.253 18.726  0.25 11.51  ? 397 HOH C O   1 
HETATM 11439 O  O   C HOH FA 7 .   ? 21.200  192.973 16.543  0.50 31.14  ? 397 HOH C O   1 
HETATM 11440 O  O   . HOH FA 7 .   ? 18.037  186.319 4.409   1.00 49.32  ? 398 HOH C O   1 
HETATM 11441 O  O   . HOH FA 7 .   ? 18.966  187.700 18.918  1.00 46.02  ? 399 HOH C O   1 
HETATM 11442 O  O   . HOH FA 7 .   ? 10.384  197.484 14.359  1.00 42.83  ? 400 HOH C O   1 
HETATM 11443 O  O   . HOH FA 7 .   ? 26.862  175.938 24.685  1.00 53.84  ? 401 HOH C O   1 
HETATM 11444 O  O   . HOH FA 7 .   ? 22.013  187.460 29.618  1.00 47.63  ? 402 HOH C O   1 
HETATM 11445 O  O   . HOH FA 7 .   ? 0.288   190.951 -1.043  1.00 41.04  ? 403 HOH C O   1 
HETATM 11446 O  O   . HOH FA 7 .   ? 19.955  189.515 25.985  1.00 48.46  ? 404 HOH C O   1 
HETATM 11447 O  O   . HOH FA 7 .   ? 3.470   178.812 22.791  1.00 49.24  ? 405 HOH C O   1 
HETATM 11448 O  O   . HOH FA 7 .   ? 20.467  201.286 16.231  1.00 57.17  ? 406 HOH C O   1 
HETATM 11449 O  O   . HOH FA 7 .   ? 6.121   195.161 3.742   1.00 41.69  ? 407 HOH C O   1 
HETATM 11450 O  O   . HOH FA 7 .   ? -0.248  192.723 6.609   1.00 42.57  ? 408 HOH C O   1 
HETATM 11451 O  O   . HOH FA 7 .   ? -5.595  181.698 22.633  1.00 47.91  ? 409 HOH C O   1 
HETATM 11452 O  O   . HOH FA 7 .   ? 1.947   173.373 7.714   1.00 56.99  ? 410 HOH C O   1 
HETATM 11453 O  O   . HOH FA 7 .   ? -2.128  183.072 34.741  1.00 50.05  ? 411 HOH C O   1 
HETATM 11454 O  O   . HOH FA 7 .   ? -8.375  181.633 22.409  1.00 62.18  ? 412 HOH C O   1 
HETATM 11455 O  O   . HOH FA 7 .   ? 30.472  176.786 19.507  1.00 55.54  ? 413 HOH C O   1 
HETATM 11456 O  O   . HOH FA 7 .   ? 22.469  168.011 20.632  1.00 45.77  ? 414 HOH C O   1 
HETATM 11457 O  O   . HOH FA 7 .   ? -5.989  195.342 33.876  1.00 43.56  ? 415 HOH C O   1 
HETATM 11458 O  O   . HOH FA 7 .   ? -1.122  190.529 6.470   1.00 58.42  ? 416 HOH C O   1 
HETATM 11459 O  O   A HOH FA 7 .   ? 9.203   199.329 30.291  0.50 27.84  ? 417 HOH C O   1 
HETATM 11460 O  O   B HOH FA 7 .   ? 8.295   200.047 28.513  0.50 31.84  ? 417 HOH C O   1 
HETATM 11461 O  O   . HOH FA 7 .   ? -8.771  192.582 14.778  1.00 35.33  ? 418 HOH C O   1 
HETATM 11462 O  O   . HOH FA 7 .   ? 22.581  170.337 24.912  1.00 47.61  ? 419 HOH C O   1 
HETATM 11463 O  O   . HOH FA 7 .   ? -1.677  176.051 12.132  1.00 43.79  ? 420 HOH C O   1 
HETATM 11464 O  O   . HOH FA 7 .   ? 12.025  187.674 3.597   1.00 46.38  ? 421 HOH C O   1 
HETATM 11465 O  O   . HOH FA 7 .   ? 19.679  176.941 35.472  1.00 49.13  ? 422 HOH C O   1 
HETATM 11466 O  O   . HOH FA 7 .   ? 15.726  178.144 5.494   1.00 46.99  ? 423 HOH C O   1 
HETATM 11467 O  O   . HOH FA 7 .   ? 6.263   199.448 36.013  1.00 45.99  ? 424 HOH C O   1 
HETATM 11468 O  O   . HOH FA 7 .   ? 13.033  173.025 10.828  1.00 47.44  ? 425 HOH C O   1 
HETATM 11469 O  O   . HOH FA 7 .   ? -0.424  195.149 6.136   1.00 47.35  ? 426 HOH C O   1 
HETATM 11470 O  O   . HOH FA 7 .   ? 0.499   176.824 -6.454  1.00 44.81  ? 427 HOH C O   1 
HETATM 11471 O  O   . HOH FA 7 .   ? 25.104  181.113 11.253  1.00 56.18  ? 428 HOH C O   1 
HETATM 11472 O  O   . HOH FA 7 .   ? 21.682  193.856 30.818  1.00 53.06  ? 429 HOH C O   1 
HETATM 11473 O  O   . HOH FA 7 .   ? 25.711  181.847 6.272   1.00 53.87  ? 430 HOH C O   1 
HETATM 11474 O  O   . HOH FA 7 .   ? 35.292  182.300 18.376  1.00 52.23  ? 431 HOH C O   1 
HETATM 11475 O  O   . HOH FA 7 .   ? 15.330  193.990 39.873  1.00 44.49  ? 432 HOH C O   1 
HETATM 11476 O  O   . HOH FA 7 .   ? -13.500 190.049 14.597  1.00 49.44  ? 433 HOH C O   1 
HETATM 11477 O  O   . HOH GA 7 .   ? 3.958   199.641 9.647   1.00 44.14  ? 301 HOH D O   1 
HETATM 11478 O  O   . HOH GA 7 .   ? -15.188 218.805 14.227  1.00 51.69  ? 302 HOH D O   1 
HETATM 11479 O  O   . HOH GA 7 .   ? 11.645  224.026 20.000  1.00 42.16  ? 303 HOH D O   1 
HETATM 11480 O  O   . HOH GA 7 .   ? -2.529  217.327 31.332  1.00 40.90  ? 304 HOH D O   1 
HETATM 11481 O  O   . HOH GA 7 .   ? -7.372  213.276 7.038   1.00 51.56  ? 305 HOH D O   1 
HETATM 11482 O  O   A HOH GA 7 .   ? -5.421  204.182 25.359  0.50 22.23  ? 306 HOH D O   1 
HETATM 11483 O  O   B HOH GA 7 .   ? -5.192  203.109 26.833  0.50 22.95  ? 306 HOH D O   1 
HETATM 11484 O  O   . HOH GA 7 .   ? 7.707   213.354 34.603  1.00 44.69  ? 307 HOH D O   1 
HETATM 11485 O  O   . HOH GA 7 .   ? -3.773  216.480 29.264  1.00 25.67  ? 308 HOH D O   1 
HETATM 11486 O  O   . HOH GA 7 .   ? -0.174  205.541 28.670  1.00 39.47  ? 309 HOH D O   1 
HETATM 11487 O  O   . HOH GA 7 .   ? 17.838  201.202 20.304  1.00 40.39  ? 310 HOH D O   1 
HETATM 11488 O  O   . HOH GA 7 .   ? -7.432  227.539 12.470  1.00 27.53  ? 311 HOH D O   1 
HETATM 11489 O  O   . HOH GA 7 .   ? 3.383   209.295 33.330  1.00 36.80  ? 312 HOH D O   1 
HETATM 11490 O  O   . HOH GA 7 .   ? -10.666 227.988 19.504  1.00 22.84  ? 313 HOH D O   1 
HETATM 11491 O  O   . HOH GA 7 .   ? -5.084  214.245 28.047  1.00 24.13  ? 314 HOH D O   1 
HETATM 11492 O  O   . HOH GA 7 .   ? 5.986   222.440 19.167  1.00 28.68  ? 315 HOH D O   1 
HETATM 11493 O  O   . HOH GA 7 .   ? -10.306 206.607 21.793  1.00 41.06  ? 316 HOH D O   1 
HETATM 11494 O  O   . HOH GA 7 .   ? 4.589   216.737 1.614   1.00 28.53  ? 317 HOH D O   1 
HETATM 11495 O  O   . HOH GA 7 .   ? 17.780  214.356 40.228  1.00 51.25  ? 318 HOH D O   1 
HETATM 11496 O  O   . HOH GA 7 .   ? -7.625  198.203 10.888  1.00 45.53  ? 319 HOH D O   1 
HETATM 11497 O  O   . HOH GA 7 .   ? -0.694  229.354 25.385  1.00 59.65  ? 320 HOH D O   1 
HETATM 11498 O  O   . HOH GA 7 .   ? 0.941   209.225 3.839   1.00 41.56  ? 321 HOH D O   1 
HETATM 11499 O  O   . HOH GA 7 .   ? -6.558  224.586 25.030  1.00 36.11  ? 322 HOH D O   1 
HETATM 11500 O  O   A HOH GA 7 .   ? 16.336  207.450 20.291  0.50 16.68  ? 323 HOH D O   1 
HETATM 11501 O  O   B HOH GA 7 .   ? 17.067  208.090 22.128  0.50 20.02  ? 323 HOH D O   1 
HETATM 11502 O  O   . HOH GA 7 .   ? 16.821  218.292 15.320  1.00 33.42  ? 324 HOH D O   1 
HETATM 11503 O  O   . HOH GA 7 .   ? -1.379  210.925 35.847  1.00 44.14  ? 325 HOH D O   1 
HETATM 11504 O  O   . HOH GA 7 .   ? 8.850   203.298 14.715  1.00 26.58  ? 326 HOH D O   1 
HETATM 11505 O  O   . HOH GA 7 .   ? 16.029  223.016 9.083   1.00 37.64  ? 327 HOH D O   1 
HETATM 11506 O  O   . HOH GA 7 .   ? -6.348  219.366 2.299   1.00 50.39  ? 328 HOH D O   1 
HETATM 11507 O  O   . HOH GA 7 .   ? 0.704   198.775 14.654  1.00 28.80  ? 329 HOH D O   1 
HETATM 11508 O  O   . HOH GA 7 .   ? -2.639  229.138 28.179  1.00 40.18  ? 330 HOH D O   1 
HETATM 11509 O  O   . HOH GA 7 .   ? 4.061   218.465 3.475   1.00 23.86  ? 331 HOH D O   1 
HETATM 11510 O  O   . HOH GA 7 .   ? -11.785 219.942 29.681  1.00 51.85  ? 332 HOH D O   1 
HETATM 11511 O  O   . HOH GA 7 .   ? -6.123  216.676 12.046  1.00 41.90  ? 333 HOH D O   1 
HETATM 11512 O  O   . HOH GA 7 .   ? 3.158   226.882 16.571  1.00 35.45  ? 334 HOH D O   1 
HETATM 11513 O  O   . HOH GA 7 .   ? 14.229  214.187 31.985  1.00 41.21  ? 335 HOH D O   1 
HETATM 11514 O  O   . HOH GA 7 .   ? 9.786   222.814 23.386  1.00 31.57  ? 336 HOH D O   1 
HETATM 11515 O  O   . HOH GA 7 .   ? 4.093   211.139 2.842   1.00 38.56  ? 337 HOH D O   1 
HETATM 11516 O  O   . HOH GA 7 .   ? -7.164  213.214 15.941  1.00 47.52  ? 338 HOH D O   1 
HETATM 11517 O  O   . HOH GA 7 .   ? 7.630   227.397 0.311   1.00 48.23  ? 339 HOH D O   1 
HETATM 11518 O  O   . HOH GA 7 .   ? 9.608   202.862 30.949  1.00 51.47  ? 340 HOH D O   1 
HETATM 11519 O  O   . HOH GA 7 .   ? 6.547   221.562 25.278  1.00 38.16  ? 341 HOH D O   1 
HETATM 11520 O  O   . HOH GA 7 .   ? -6.560  232.373 16.266  1.00 29.73  ? 342 HOH D O   1 
HETATM 11521 O  O   . HOH GA 7 .   ? -4.348  224.972 9.767   1.00 40.06  ? 343 HOH D O   1 
HETATM 11522 O  O   . HOH GA 7 .   ? -7.728  202.171 16.164  1.00 38.89  ? 344 HOH D O   1 
HETATM 11523 O  O   A HOH GA 7 .   ? 1.563   225.123 7.019   0.50 30.95  ? 345 HOH D O   1 
HETATM 11524 O  O   B HOH GA 7 .   ? 2.405   224.285 5.830   0.50 31.79  ? 345 HOH D O   1 
HETATM 11525 O  O   . HOH GA 7 .   ? 18.766  217.615 8.391   1.00 45.83  ? 346 HOH D O   1 
HETATM 11526 O  O   . HOH GA 7 .   ? 17.873  221.720 4.890   1.00 48.20  ? 347 HOH D O   1 
HETATM 11527 O  O   . HOH GA 7 .   ? -6.659  209.045 24.421  1.00 31.20  ? 348 HOH D O   1 
HETATM 11528 O  O   . HOH GA 7 .   ? 18.171  207.281 16.230  1.00 39.59  ? 349 HOH D O   1 
HETATM 11529 O  O   . HOH GA 7 .   ? -4.678  226.321 29.305  1.00 36.38  ? 350 HOH D O   1 
HETATM 11530 O  O   . HOH GA 7 .   ? -0.683  220.678 19.827  1.00 28.40  ? 351 HOH D O   1 
HETATM 11531 O  O   . HOH GA 7 .   ? -10.656 211.095 31.213  1.00 45.70  ? 352 HOH D O   1 
HETATM 11532 O  O   . HOH GA 7 .   ? 12.512  217.363 1.788   1.00 28.10  ? 353 HOH D O   1 
HETATM 11533 O  O   . HOH GA 7 .   ? -3.302  206.622 30.277  1.00 39.05  ? 354 HOH D O   1 
HETATM 11534 O  O   . HOH GA 7 .   ? -5.900  227.114 23.274  1.00 39.58  ? 355 HOH D O   1 
HETATM 11535 O  O   . HOH GA 7 .   ? -10.709 217.103 22.557  1.00 39.76  ? 356 HOH D O   1 
HETATM 11536 O  O   . HOH GA 7 .   ? -0.483  203.914 12.956  1.00 41.72  ? 357 HOH D O   1 
HETATM 11537 O  O   . HOH GA 7 .   ? -7.293  217.339 4.689   1.00 48.52  ? 358 HOH D O   1 
HETATM 11538 O  O   . HOH GA 7 .   ? 13.752  222.802 10.443  1.00 29.60  ? 359 HOH D O   1 
HETATM 11539 O  O   . HOH GA 7 .   ? 14.150  227.774 4.924   1.00 42.10  ? 360 HOH D O   1 
HETATM 11540 O  O   . HOH GA 7 .   ? -1.464  206.310 6.349   1.00 36.05  ? 361 HOH D O   1 
HETATM 11541 O  O   . HOH GA 7 .   ? 3.419   226.336 30.111  1.00 49.42  ? 362 HOH D O   1 
HETATM 11542 O  O   . HOH GA 7 .   ? 2.984   227.478 8.129   1.00 33.98  ? 363 HOH D O   1 
HETATM 11543 O  O   . HOH GA 7 .   ? -14.732 219.336 21.299  1.00 50.67  ? 364 HOH D O   1 
HETATM 11544 O  O   . HOH GA 7 .   ? -5.179  211.326 7.112   1.00 36.67  ? 365 HOH D O   1 
HETATM 11545 O  O   . HOH GA 7 .   ? -8.777  232.951 18.799  1.00 31.67  ? 366 HOH D O   1 
HETATM 11546 O  O   A HOH GA 7 .   ? 15.821  214.471 29.068  0.50 17.58  ? 367 HOH D O   1 
HETATM 11547 O  O   B HOH GA 7 .   ? 15.986  216.181 29.794  0.50 31.84  ? 367 HOH D O   1 
HETATM 11548 O  O   . HOH GA 7 .   ? 6.087   201.828 13.380  1.00 29.92  ? 368 HOH D O   1 
HETATM 11549 O  O   . HOH GA 7 .   ? -6.667  222.433 32.317  1.00 50.60  ? 369 HOH D O   1 
HETATM 11550 O  O   . HOH GA 7 .   ? -15.197 222.829 12.840  1.00 37.52  ? 370 HOH D O   1 
HETATM 11551 O  O   . HOH GA 7 .   ? 1.732   219.594 3.678   1.00 36.84  ? 371 HOH D O   1 
HETATM 11552 O  O   . HOH GA 7 .   ? 1.600   226.068 23.014  1.00 27.99  ? 372 HOH D O   1 
HETATM 11553 O  O   . HOH GA 7 .   ? -2.215  221.378 34.349  1.00 47.66  ? 373 HOH D O   1 
HETATM 11554 O  O   . HOH GA 7 .   ? -4.374  216.826 14.239  1.00 33.04  ? 374 HOH D O   1 
HETATM 11555 O  O   . HOH GA 7 .   ? 6.356   210.406 34.478  1.00 38.05  ? 375 HOH D O   1 
HETATM 11556 O  O   . HOH GA 7 .   ? -6.393  196.407 15.548  1.00 40.18  ? 376 HOH D O   1 
HETATM 11557 O  O   . HOH GA 7 .   ? -0.632  208.558 5.515   1.00 40.01  ? 377 HOH D O   1 
HETATM 11558 O  O   . HOH GA 7 .   ? 0.078   205.276 4.830   1.00 63.87  ? 378 HOH D O   1 
HETATM 11559 O  O   . HOH GA 7 .   ? 4.021   218.674 33.832  1.00 48.65  ? 379 HOH D O   1 
HETATM 11560 O  O   . HOH GA 7 .   ? 1.341   222.453 30.468  1.00 36.99  ? 380 HOH D O   1 
HETATM 11561 O  O   . HOH GA 7 .   ? 5.781   221.203 29.073  1.00 39.53  ? 381 HOH D O   1 
HETATM 11562 O  O   . HOH GA 7 .   ? -0.314  220.792 30.414  1.00 59.25  ? 382 HOH D O   1 
HETATM 11563 O  O   . HOH GA 7 .   ? 12.771  207.900 32.596  1.00 47.65  ? 383 HOH D O   1 
HETATM 11564 O  O   . HOH GA 7 .   ? 16.742  211.860 12.613  1.00 35.38  ? 384 HOH D O   1 
HETATM 11565 O  O   . HOH GA 7 .   ? -7.890  214.213 18.468  1.00 32.66  ? 385 HOH D O   1 
HETATM 11566 O  O   A HOH GA 7 .   ? -8.122  218.794 10.900  0.50 15.25  ? 386 HOH D O   1 
HETATM 11567 O  O   B HOH GA 7 .   ? -9.461  217.225 9.930   0.50 28.88  ? 386 HOH D O   1 
HETATM 11568 O  O   . HOH GA 7 .   ? 18.767  220.328 7.411   1.00 45.43  ? 387 HOH D O   1 
HETATM 11569 O  O   . HOH GA 7 .   ? -8.783  208.319 12.710  1.00 45.31  ? 388 HOH D O   1 
HETATM 11570 O  O   . HOH GA 7 .   ? -8.371  213.364 21.071  1.00 53.78  ? 389 HOH D O   1 
HETATM 11571 O  O   . HOH GA 7 .   ? -3.202  213.944 2.163   1.00 47.23  ? 390 HOH D O   1 
HETATM 11572 O  O   . HOH GA 7 .   ? -2.520  229.736 16.554  1.00 31.58  ? 391 HOH D O   1 
HETATM 11573 O  O   . HOH GA 7 .   ? 1.738   203.290 13.210  1.00 39.29  ? 392 HOH D O   1 
HETATM 11574 O  O   . HOH GA 7 .   ? -4.938  203.995 5.038   1.00 57.03  ? 393 HOH D O   1 
HETATM 11575 O  O   . HOH GA 7 .   ? 7.524   216.078 34.072  1.00 46.27  ? 394 HOH D O   1 
HETATM 11576 O  O   . HOH GA 7 .   ? -3.348  234.718 22.262  1.00 41.15  ? 395 HOH D O   1 
HETATM 11577 O  O   . HOH GA 7 .   ? 10.478  228.195 7.049   1.00 34.10  ? 396 HOH D O   1 
HETATM 11578 O  O   . HOH GA 7 .   ? 17.987  216.886 13.201  1.00 43.77  ? 397 HOH D O   1 
HETATM 11579 O  O   . HOH GA 7 .   ? 17.698  225.554 6.649   1.00 38.06  ? 398 HOH D O   1 
HETATM 11580 O  O   A HOH GA 7 .   ? 17.934  203.207 27.271  0.50 26.32  ? 399 HOH D O   1 
HETATM 11581 O  O   B HOH GA 7 .   ? 15.657  203.022 27.200  0.50 22.85  ? 399 HOH D O   1 
HETATM 11582 O  O   . HOH GA 7 .   ? 6.794   214.044 32.279  1.00 38.64  ? 400 HOH D O   1 
HETATM 11583 O  O   . HOH GA 7 .   ? 4.509   203.569 9.421   1.00 47.19  ? 401 HOH D O   1 
HETATM 11584 O  O   . HOH GA 7 .   ? 6.058   206.280 0.183   1.00 53.70  ? 402 HOH D O   1 
HETATM 11585 O  O   . HOH GA 7 .   ? 18.234  219.109 19.450  1.00 46.84  ? 403 HOH D O   1 
HETATM 11586 O  O   . HOH GA 7 .   ? -10.599 210.980 26.039  1.00 40.80  ? 404 HOH D O   1 
HETATM 11587 O  O   . HOH GA 7 .   ? 20.827  211.622 18.221  1.00 54.78  ? 405 HOH D O   1 
HETATM 11588 O  O   . HOH GA 7 .   ? -4.094  204.676 34.746  1.00 55.61  ? 406 HOH D O   1 
HETATM 11589 O  O   . HOH GA 7 .   ? 16.042  211.533 9.669   1.00 49.56  ? 407 HOH D O   1 
HETATM 11590 O  O   . HOH GA 7 .   ? 3.445   205.038 -2.270  1.00 45.56  ? 408 HOH D O   1 
HETATM 11591 O  O   . HOH GA 7 .   ? 3.828   202.503 11.843  1.00 37.28  ? 409 HOH D O   1 
HETATM 11592 O  O   . HOH GA 7 .   ? 18.178  210.451 14.055  1.00 43.13  ? 410 HOH D O   1 
HETATM 11593 O  O   . HOH GA 7 .   ? 15.243  218.982 22.616  1.00 56.92  ? 411 HOH D O   1 
HETATM 11594 O  O   . HOH GA 7 .   ? -6.598  207.372 26.713  1.00 38.27  ? 412 HOH D O   1 
HETATM 11595 O  O   . HOH GA 7 .   ? 11.308  205.789 5.793   1.00 60.56  ? 413 HOH D O   1 
HETATM 11596 O  O   . HOH GA 7 .   ? -16.995 220.726 13.049  1.00 40.87  ? 414 HOH D O   1 
HETATM 11597 O  O   . HOH GA 7 .   ? -1.780  227.859 30.285  1.00 49.60  ? 415 HOH D O   1 
HETATM 11598 O  O   . HOH GA 7 .   ? 8.719   207.508 0.173   1.00 46.66  ? 416 HOH D O   1 
HETATM 11599 O  O   . HOH GA 7 .   ? -1.102  233.901 17.900  1.00 47.08  ? 417 HOH D O   1 
HETATM 11600 O  O   . HOH GA 7 .   ? -9.364  212.397 14.888  1.00 38.05  ? 418 HOH D O   1 
HETATM 11601 O  O   . HOH GA 7 .   ? 12.514  217.955 36.760  1.00 50.83  ? 419 HOH D O   1 
HETATM 11602 O  O   . HOH GA 7 .   ? -9.493  209.644 15.119  1.00 36.19  ? 420 HOH D O   1 
HETATM 11603 O  O   . HOH GA 7 .   ? 14.390  222.620 22.384  1.00 41.99  ? 421 HOH D O   1 
HETATM 11604 O  O   . HOH GA 7 .   ? 20.253  222.756 9.772   1.00 56.76  ? 422 HOH D O   1 
HETATM 11605 O  O   . HOH GA 7 .   ? 12.972  205.834 0.782   1.00 51.63  ? 423 HOH D O   1 
HETATM 11606 O  O   . HOH GA 7 .   ? 13.014  207.284 7.639   1.00 44.36  ? 424 HOH D O   1 
HETATM 11607 O  O   . HOH GA 7 .   ? -12.518 215.442 25.120  1.00 42.29  ? 425 HOH D O   1 
HETATM 11608 O  O   . HOH GA 7 .   ? -8.167  228.651 23.668  1.00 38.48  ? 426 HOH D O   1 
HETATM 11609 O  O   . HOH GA 7 .   ? 8.851   231.820 3.098   1.00 46.64  ? 427 HOH D O   1 
HETATM 11610 O  O   . HOH GA 7 .   ? 5.480   202.139 33.267  1.00 43.47  ? 428 HOH D O   1 
HETATM 11611 O  O   . HOH GA 7 .   ? 0.911   202.477 32.361  1.00 47.59  ? 429 HOH D O   1 
HETATM 11612 O  O   . HOH GA 7 .   ? 0.001   228.645 14.606  1.00 37.59  ? 430 HOH D O   1 
HETATM 11613 O  O   . HOH GA 7 .   ? -2.809  225.652 7.912   1.00 44.26  ? 431 HOH D O   1 
HETATM 11614 O  O   . HOH GA 7 .   ? 7.791   229.270 6.600   1.00 48.32  ? 432 HOH D O   1 
HETATM 11615 O  O   . HOH GA 7 .   ? -14.015 221.963 10.250  1.00 34.69  ? 433 HOH D O   1 
HETATM 11616 O  O   . HOH GA 7 .   ? 6.803   210.251 -3.127  1.00 44.16  ? 434 HOH D O   1 
HETATM 11617 O  O   . HOH GA 7 .   ? 15.029  212.570 7.159   1.00 49.87  ? 435 HOH D O   1 
HETATM 11618 O  O   . HOH GA 7 .   ? -9.320  202.700 24.808  1.00 51.39  ? 436 HOH D O   1 
HETATM 11619 O  O   . HOH GA 7 .   ? 14.422  223.964 -3.049  1.00 49.57  ? 437 HOH D O   1 
HETATM 11620 O  O   . HOH GA 7 .   ? -6.515  226.401 31.097  1.00 35.43  ? 438 HOH D O   1 
HETATM 11621 O  O   . HOH GA 7 .   ? 5.523   229.411 4.669   1.00 42.75  ? 439 HOH D O   1 
HETATM 11622 O  O   . HOH GA 7 .   ? -1.862  228.388 13.032  1.00 43.53  ? 440 HOH D O   1 
HETATM 11623 O  O   . HOH GA 7 .   ? -9.465  210.970 22.983  1.00 52.79  ? 441 HOH D O   1 
HETATM 11624 O  O   . HOH GA 7 .   ? 20.494  208.558 18.566  1.00 47.73  ? 442 HOH D O   1 
HETATM 11625 O  O   . HOH GA 7 .   ? 21.150  216.158 16.778  1.00 43.40  ? 443 HOH D O   1 
HETATM 11626 O  O   . HOH GA 7 .   ? -8.674  202.147 11.003  1.00 49.90  ? 444 HOH D O   1 
HETATM 11627 O  O   . HOH GA 7 .   ? -10.524 215.018 20.329  1.00 42.57  ? 445 HOH D O   1 
HETATM 11628 O  O   . HOH GA 7 .   ? -3.592  201.139 4.326   1.00 50.23  ? 446 HOH D O   1 
HETATM 11629 O  O   . HOH GA 7 .   ? -8.963  230.638 22.239  1.00 27.54  ? 447 HOH D O   1 
HETATM 11630 O  O   . HOH GA 7 .   ? -5.792  209.766 34.022  1.00 45.23  ? 448 HOH D O   1 
HETATM 11631 O  O   . HOH GA 7 .   ? 5.354   213.281 34.361  1.00 46.46  ? 449 HOH D O   1 
HETATM 11632 O  O   . HOH GA 7 .   ? -11.264 230.332 20.973  1.00 27.56  ? 450 HOH D O   1 
HETATM 11633 O  O   . HOH GA 7 .   ? -0.911  223.773 4.022   1.00 44.13  ? 451 HOH D O   1 
HETATM 11634 O  O   . HOH GA 7 .   ? 1.576   229.010 16.577  1.00 39.30  ? 452 HOH D O   1 
HETATM 11635 O  O   . HOH GA 7 .   ? -0.203  211.375 1.803   1.00 45.09  ? 453 HOH D O   1 
HETATM 11636 O  O   . HOH GA 7 .   ? -12.353 210.474 12.146  1.00 51.91  ? 454 HOH D O   1 
HETATM 11637 O  O   . HOH GA 7 .   ? -7.222  232.576 21.068  1.00 28.91  ? 455 HOH D O   1 
HETATM 11638 O  O   . HOH GA 7 .   ? 19.474  215.745 22.602  1.00 42.39  ? 456 HOH D O   1 
HETATM 11639 O  O   . HOH GA 7 .   ? -9.780  226.237 28.469  1.00 46.25  ? 457 HOH D O   1 
HETATM 11640 O  O   . HOH GA 7 .   ? -4.634  228.863 11.945  1.00 45.55  ? 458 HOH D O   1 
HETATM 11641 O  O   . HOH GA 7 .   ? -7.676  211.739 4.615   1.00 53.34  ? 459 HOH D O   1 
HETATM 11642 O  O   . HOH GA 7 .   ? 15.214  203.970 4.146   1.00 49.18  ? 460 HOH D O   1 
HETATM 11643 O  O   . HOH GA 7 .   ? -8.661  227.182 30.298  1.00 55.04  ? 461 HOH D O   1 
HETATM 11644 O  O   . HOH GA 7 .   ? -15.549 215.226 26.400  1.00 47.60  ? 462 HOH D O   1 
HETATM 11645 O  O   . HOH GA 7 .   ? 18.075  211.083 41.262  1.00 52.52  ? 463 HOH D O   1 
HETATM 11646 O  O   . HOH GA 7 .   ? 22.049  220.907 7.470   1.00 47.83  ? 464 HOH D O   1 
HETATM 11647 O  O   . HOH GA 7 .   ? -8.771  226.312 36.306  1.00 54.46  ? 465 HOH D O   1 
HETATM 11648 O  O   . HOH GA 7 .   ? -18.857 217.093 22.010  1.00 54.25  ? 466 HOH D O   1 
HETATM 11649 O  O   . HOH GA 7 .   ? -11.707 214.463 5.445   1.00 47.48  ? 467 HOH D O   1 
HETATM 11650 O  O   . HOH GA 7 .   ? -13.244 208.566 14.124  1.00 47.76  ? 468 HOH D O   1 
HETATM 11651 O  O   . HOH GA 7 .   ? -6.845  215.127 -3.483  1.00 48.98  ? 469 HOH D O   1 
HETATM 11652 O  O   . HOH HA 7 .   ? 32.477  253.158 40.912  1.00 39.82  ? 301 HOH E O   1 
HETATM 11653 O  O   . HOH HA 7 .   ? 39.567  250.498 70.613  1.00 51.34  ? 302 HOH E O   1 
HETATM 11654 O  O   . HOH HA 7 .   ? 33.786  253.390 34.158  1.00 28.65  ? 303 HOH E O   1 
HETATM 11655 O  O   . HOH HA 7 .   ? 40.121  254.632 40.617  1.00 42.75  ? 304 HOH E O   1 
HETATM 11656 O  O   . HOH HA 7 .   ? 33.044  244.940 61.211  1.00 41.79  ? 305 HOH E O   1 
HETATM 11657 O  O   . HOH HA 7 .   ? 40.983  233.548 44.139  1.00 55.37  ? 306 HOH E O   1 
HETATM 11658 O  O   . HOH HA 7 .   ? 49.823  241.110 54.544  1.00 50.56  ? 307 HOH E O   1 
HETATM 11659 O  O   . HOH HA 7 .   ? 50.298  265.560 75.102  1.00 46.99  ? 308 HOH E O   1 
HETATM 11660 O  O   . HOH HA 7 .   ? 50.804  248.507 49.669  1.00 54.81  ? 309 HOH E O   1 
HETATM 11661 O  O   . HOH HA 7 .   ? 49.250  238.441 50.190  1.00 45.54  ? 310 HOH E O   1 
HETATM 11662 O  O   . HOH HA 7 .   ? 53.256  234.106 52.244  1.00 56.34  ? 311 HOH E O   1 
HETATM 11663 O  O   . HOH HA 7 .   ? 42.709  233.304 46.048  1.00 41.82  ? 312 HOH E O   1 
HETATM 11664 O  O   . HOH HA 7 .   ? 60.487  238.206 43.291  1.00 59.21  ? 313 HOH E O   1 
HETATM 11665 O  O   . HOH HA 7 .   ? 35.558  256.184 68.332  1.00 46.59  ? 314 HOH E O   1 
HETATM 11666 O  O   . HOH HA 7 .   ? 48.821  254.592 51.694  1.00 49.58  ? 315 HOH E O   1 
HETATM 11667 O  O   . HOH HA 7 .   ? 54.898  251.431 69.149  1.00 47.54  ? 316 HOH E O   1 
HETATM 11668 O  O   . HOH HA 7 .   ? 45.103  261.261 69.153  1.00 47.47  ? 317 HOH E O   1 
HETATM 11669 O  O   . HOH HA 7 .   ? 31.841  246.850 57.558  1.00 30.62  ? 318 HOH E O   1 
HETATM 11670 O  O   . HOH HA 7 .   ? 36.172  242.993 42.221  1.00 43.21  ? 319 HOH E O   1 
HETATM 11671 O  O   . HOH HA 7 .   ? 41.573  238.249 37.871  1.00 46.21  ? 320 HOH E O   1 
HETATM 11672 O  O   . HOH HA 7 .   ? 29.089  251.943 37.239  1.00 47.59  ? 321 HOH E O   1 
HETATM 11673 O  O   . HOH HA 7 .   ? 45.888  237.541 37.099  1.00 61.91  ? 322 HOH E O   1 
HETATM 11674 O  O   . HOH HA 7 .   ? 41.057  240.497 36.426  1.00 58.01  ? 323 HOH E O   1 
HETATM 11675 O  O   . HOH HA 7 .   ? 47.010  247.119 68.899  1.00 32.31  ? 324 HOH E O   1 
HETATM 11676 O  O   . HOH HA 7 .   ? 40.472  257.024 34.216  1.00 39.10  ? 325 HOH E O   1 
HETATM 11677 O  O   . HOH HA 7 .   ? 30.402  255.896 54.070  1.00 41.92  ? 326 HOH E O   1 
HETATM 11678 O  O   . HOH HA 7 .   ? 38.315  245.352 68.252  1.00 46.39  ? 327 HOH E O   1 
HETATM 11679 O  O   . HOH HA 7 .   ? 43.801  254.483 70.628  1.00 41.11  ? 328 HOH E O   1 
HETATM 11680 O  O   . HOH HA 7 .   ? 33.306  230.357 54.536  1.00 34.07  ? 329 HOH E O   1 
HETATM 11681 O  O   . HOH HA 7 .   ? 30.815  257.887 36.661  1.00 43.05  ? 330 HOH E O   1 
HETATM 11682 O  O   . HOH HA 7 .   ? 35.782  259.419 41.178  1.00 47.78  ? 331 HOH E O   1 
HETATM 11683 O  O   . HOH HA 7 .   ? 52.281  260.869 68.377  1.00 41.12  ? 332 HOH E O   1 
HETATM 11684 O  O   . HOH HA 7 .   ? 46.853  259.323 49.075  1.00 37.76  ? 333 HOH E O   1 
HETATM 11685 O  O   . HOH HA 7 .   ? 50.211  252.877 41.317  1.00 50.52  ? 334 HOH E O   1 
HETATM 11686 O  O   . HOH HA 7 .   ? 48.068  256.559 55.132  1.00 47.03  ? 335 HOH E O   1 
HETATM 11687 O  O   . HOH HA 7 .   ? 45.217  258.677 42.973  1.00 56.68  ? 336 HOH E O   1 
HETATM 11688 O  O   . HOH HA 7 .   ? 47.567  257.207 58.652  1.00 38.80  ? 337 HOH E O   1 
HETATM 11689 O  O   . HOH HA 7 .   ? 46.595  261.291 57.768  1.00 51.05  ? 338 HOH E O   1 
HETATM 11690 O  O   . HOH HA 7 .   ? 31.740  237.477 56.049  1.00 22.80  ? 339 HOH E O   1 
HETATM 11691 O  O   . HOH HA 7 .   ? 48.855  247.676 67.134  1.00 38.07  ? 340 HOH E O   1 
HETATM 11692 O  O   . HOH HA 7 .   ? 32.352  232.684 63.048  1.00 43.18  ? 341 HOH E O   1 
HETATM 11693 O  O   . HOH HA 7 .   ? 43.473  237.896 44.794  1.00 38.83  ? 342 HOH E O   1 
HETATM 11694 O  O   . HOH HA 7 .   ? 40.861  261.168 58.920  1.00 50.30  ? 343 HOH E O   1 
HETATM 11695 O  O   . HOH HA 7 .   ? 31.084  255.955 40.757  1.00 40.67  ? 344 HOH E O   1 
HETATM 11696 O  O   . HOH HA 7 .   ? 46.305  257.900 55.560  1.00 47.82  ? 345 HOH E O   1 
HETATM 11697 O  O   . HOH HA 7 .   ? 56.327  251.804 62.935  1.00 41.24  ? 346 HOH E O   1 
HETATM 11698 O  O   . HOH HA 7 .   ? 33.923  243.462 36.263  1.00 45.39  ? 347 HOH E O   1 
HETATM 11699 O  O   . HOH HA 7 .   ? 33.611  229.120 56.712  1.00 45.96  ? 348 HOH E O   1 
HETATM 11700 O  O   . HOH HA 7 .   ? 42.521  244.190 67.758  1.00 46.88  ? 349 HOH E O   1 
HETATM 11701 O  O   . HOH HA 7 .   ? 33.661  258.487 59.646  1.00 35.32  ? 350 HOH E O   1 
HETATM 11702 O  O   . HOH HA 7 .   ? 37.571  236.853 44.342  1.00 39.44  ? 351 HOH E O   1 
HETATM 11703 O  O   . HOH HA 7 .   ? 35.613  257.346 60.910  1.00 43.56  ? 352 HOH E O   1 
HETATM 11704 O  O   . HOH HA 7 .   ? 35.086  261.186 44.713  1.00 44.86  ? 353 HOH E O   1 
HETATM 11705 O  O   . HOH HA 7 .   ? 51.203  246.142 66.592  1.00 48.87  ? 354 HOH E O   1 
HETATM 11706 O  O   . HOH HA 7 .   ? 44.694  262.453 41.236  1.00 49.94  ? 355 HOH E O   1 
HETATM 11707 O  O   . HOH HA 7 .   ? 48.603  237.774 57.316  1.00 44.46  ? 356 HOH E O   1 
HETATM 11708 O  O   . HOH HA 7 .   ? 35.209  264.644 48.941  1.00 48.71  ? 357 HOH E O   1 
HETATM 11709 O  O   . HOH HA 7 .   ? 30.718  256.779 58.545  1.00 47.73  ? 358 HOH E O   1 
HETATM 11710 O  O   . HOH HA 7 .   ? 50.419  257.634 56.569  1.00 47.71  ? 359 HOH E O   1 
HETATM 11711 O  O   . HOH HA 7 .   ? 46.805  255.718 42.822  1.00 41.00  ? 360 HOH E O   1 
HETATM 11712 O  O   . HOH HA 7 .   ? 31.339  257.429 52.116  1.00 47.96  ? 361 HOH E O   1 
HETATM 11713 O  O   . HOH HA 7 .   ? 54.166  238.988 57.195  1.00 57.08  ? 362 HOH E O   1 
HETATM 11714 O  O   . HOH HA 7 .   ? 38.189  245.653 72.569  1.00 42.04  ? 363 HOH E O   1 
HETATM 11715 O  O   . HOH HA 7 .   ? 26.516  254.812 46.886  1.00 42.79  ? 364 HOH E O   1 
HETATM 11716 O  O   . HOH HA 7 .   ? 46.964  237.041 62.111  1.00 43.96  ? 365 HOH E O   1 
HETATM 11717 O  O   . HOH HA 7 .   ? 47.647  256.167 47.321  1.00 57.56  ? 366 HOH E O   1 
HETATM 11718 O  O   . HOH HA 7 .   ? 47.410  245.139 39.971  1.00 52.00  ? 367 HOH E O   1 
HETATM 11719 O  O   . HOH HA 7 .   ? 32.105  244.038 58.532  1.00 39.29  ? 368 HOH E O   1 
HETATM 11720 O  O   . HOH HA 7 .   ? 30.240  246.520 38.676  1.00 46.25  ? 369 HOH E O   1 
HETATM 11721 O  O   . HOH HA 7 .   ? 48.754  238.717 55.330  1.00 37.64  ? 370 HOH E O   1 
HETATM 11722 O  O   . HOH HA 7 .   ? 41.431  256.612 38.218  1.00 43.48  ? 371 HOH E O   1 
HETATM 11723 O  O   . HOH HA 7 .   ? 51.013  252.707 71.742  1.00 35.25  ? 372 HOH E O   1 
HETATM 11724 O  O   . HOH HA 7 .   ? 47.689  260.560 55.119  1.00 45.25  ? 373 HOH E O   1 
HETATM 11725 O  O   . HOH HA 7 .   ? 61.312  240.658 57.227  1.00 55.84  ? 374 HOH E O   1 
HETATM 11726 O  O   . HOH HA 7 .   ? 36.470  242.297 35.750  1.00 52.17  ? 375 HOH E O   1 
HETATM 11727 O  O   A HOH HA 7 .   ? 36.278  239.835 63.378  0.50 29.58  ? 376 HOH E O   1 
HETATM 11728 O  O   B HOH HA 7 .   ? 35.951  240.350 64.711  0.50 37.49  ? 376 HOH E O   1 
HETATM 11729 O  O   . HOH HA 7 .   ? 51.648  254.843 52.821  1.00 49.46  ? 377 HOH E O   1 
HETATM 11730 O  O   . HOH HA 7 .   ? 41.833  237.770 63.288  1.00 50.27  ? 378 HOH E O   1 
HETATM 11731 O  O   . HOH HA 7 .   ? 37.083  261.236 34.791  1.00 45.66  ? 379 HOH E O   1 
HETATM 11732 O  O   . HOH HA 7 .   ? 48.072  262.041 52.844  1.00 51.43  ? 380 HOH E O   1 
HETATM 11733 O  O   . HOH HA 7 .   ? 48.171  238.044 52.670  1.00 53.02  ? 381 HOH E O   1 
HETATM 11734 O  O   . HOH HA 7 .   ? 52.367  237.365 59.959  1.00 61.49  ? 382 HOH E O   1 
HETATM 11735 O  O   . HOH HA 7 .   ? 44.940  265.187 43.442  1.00 51.61  ? 383 HOH E O   1 
HETATM 11736 O  O   . HOH HA 7 .   ? 48.188  258.327 44.422  1.00 41.96  ? 384 HOH E O   1 
HETATM 11737 O  O   . HOH HA 7 .   ? 54.677  258.234 60.241  1.00 52.29  ? 385 HOH E O   1 
HETATM 11738 O  O   A HOH HA 7 .   ? 45.842  233.631 52.806  0.50 23.12  ? 386 HOH E O   1 
HETATM 11739 O  O   B HOH HA 7 .   ? 45.817  234.469 53.684  0.50 30.17  ? 386 HOH E O   1 
HETATM 11740 O  O   . HOH HA 7 .   ? 48.170  237.682 46.630  1.00 57.22  ? 387 HOH E O   1 
HETATM 11741 O  O   . HOH HA 7 .   ? 29.855  259.317 56.115  1.00 43.12  ? 388 HOH E O   1 
HETATM 11742 O  O   . HOH HA 7 .   ? 48.450  235.479 53.045  1.00 45.36  ? 389 HOH E O   1 
HETATM 11743 O  O   . HOH HA 7 .   ? 43.243  236.073 42.142  1.00 48.19  ? 390 HOH E O   1 
HETATM 11744 O  O   . HOH HA 7 .   ? 35.209  252.698 65.802  1.00 48.16  ? 391 HOH E O   1 
HETATM 11745 O  O   . HOH HA 7 .   ? 34.056  250.364 64.965  1.00 49.06  ? 392 HOH E O   1 
HETATM 11746 O  O   . HOH HA 7 .   ? 47.186  260.659 45.047  1.00 49.25  ? 393 HOH E O   1 
HETATM 11747 O  O   . HOH HA 7 .   ? 22.636  261.015 49.773  1.00 53.29  ? 394 HOH E O   1 
HETATM 11748 O  O   . HOH HA 7 .   ? 35.348  245.666 68.276  1.00 52.50  ? 395 HOH E O   1 
HETATM 11749 O  O   . HOH HA 7 .   ? 43.350  260.350 71.435  1.00 49.54  ? 396 HOH E O   1 
HETATM 11750 O  O   . HOH HA 7 .   ? 35.756  255.158 64.875  1.00 45.49  ? 397 HOH E O   1 
HETATM 11751 O  O   . HOH HA 7 .   ? 38.665  239.159 40.618  1.00 49.19  ? 398 HOH E O   1 
HETATM 11752 O  O   . HOH HA 7 .   ? 58.611  242.637 44.231  1.00 54.61  ? 399 HOH E O   1 
HETATM 11753 O  O   . HOH HA 7 .   ? 52.076  251.163 36.346  1.00 60.22  ? 400 HOH E O   1 
HETATM 11754 O  O   . HOH HA 7 .   ? 32.441  241.453 64.494  1.00 49.01  ? 401 HOH E O   1 
HETATM 11755 O  O   . HOH HA 7 .   ? 43.255  264.988 56.474  1.00 47.80  ? 402 HOH E O   1 
HETATM 11756 O  O   . HOH HA 7 .   ? 49.461  235.981 61.369  1.00 54.50  ? 403 HOH E O   1 
HETATM 11757 O  O   . HOH HA 7 .   ? 47.844  256.955 49.952  1.00 59.35  ? 404 HOH E O   1 
HETATM 11758 O  O   . HOH HA 7 .   ? 45.417  243.782 68.775  1.00 45.06  ? 405 HOH E O   1 
HETATM 11759 O  O   . HOH HA 7 .   ? 58.073  260.435 67.423  1.00 50.45  ? 406 HOH E O   1 
HETATM 11760 O  O   . HOH HA 7 .   ? 40.133  254.579 73.161  1.00 39.75  ? 407 HOH E O   1 
HETATM 11761 O  O   . HOH HA 7 .   ? 51.517  261.360 49.692  1.00 62.63  ? 408 HOH E O   1 
HETATM 11762 O  O   . HOH HA 7 .   ? 56.531  236.177 58.828  1.00 48.04  ? 409 HOH E O   1 
HETATM 11763 O  O   . HOH HA 7 .   ? 51.099  263.860 46.166  1.00 53.86  ? 410 HOH E O   1 
HETATM 11764 O  O   . HOH HA 7 .   ? 49.539  257.823 51.942  1.00 50.51  ? 411 HOH E O   1 
HETATM 11765 O  O   . HOH HA 7 .   ? 37.429  262.952 63.685  1.00 51.05  ? 412 HOH E O   1 
HETATM 11766 O  O   . HOH HA 7 .   ? 54.880  235.313 61.580  1.00 46.06  ? 413 HOH E O   1 
HETATM 11767 O  O   . HOH HA 7 .   ? 53.969  265.076 46.280  1.00 51.00  ? 414 HOH E O   1 
HETATM 11768 O  O   . HOH HA 7 .   ? 57.266  264.074 48.625  1.00 55.29  ? 415 HOH E O   1 
HETATM 11769 O  O   . HOH HA 7 .   ? 55.527  267.178 48.945  1.00 55.40  ? 416 HOH E O   1 
HETATM 11770 O  O   . HOH IA 7 .   ? 13.204  226.520 52.625  1.00 42.62  ? 301 HOH F O   1 
HETATM 11771 O  O   . HOH IA 7 .   ? 9.362   240.372 70.704  1.00 46.34  ? 302 HOH F O   1 
HETATM 11772 O  O   . HOH IA 7 .   ? 2.902   237.521 49.807  1.00 34.88  ? 303 HOH F O   1 
HETATM 11773 O  O   . HOH IA 7 .   ? 21.629  228.999 34.633  1.00 49.78  ? 304 HOH F O   1 
HETATM 11774 O  O   . HOH IA 7 .   ? 30.956  226.838 51.255  1.00 50.53  ? 305 HOH F O   1 
HETATM 11775 O  O   . HOH IA 7 .   ? 26.310  235.786 39.491  1.00 50.63  ? 306 HOH F O   1 
HETATM 11776 O  O   . HOH IA 7 .   ? -1.980  246.444 45.838  1.00 55.14  ? 307 HOH F O   1 
HETATM 11777 O  O   . HOH IA 7 .   ? 16.712  235.901 70.488  1.00 45.02  ? 308 HOH F O   1 
HETATM 11778 O  O   . HOH IA 7 .   ? 12.689  233.189 43.231  1.00 36.63  ? 309 HOH F O   1 
HETATM 11779 O  O   . HOH IA 7 .   ? 25.149  254.498 54.588  1.00 38.48  ? 310 HOH F O   1 
HETATM 11780 O  O   . HOH IA 7 .   ? 21.973  238.164 37.292  1.00 44.68  ? 311 HOH F O   1 
HETATM 11781 O  O   . HOH IA 7 .   ? 1.947   231.309 48.312  1.00 45.86  ? 312 HOH F O   1 
HETATM 11782 O  O   . HOH IA 7 .   ? 25.175  238.470 68.183  1.00 39.23  ? 313 HOH F O   1 
HETATM 11783 O  O   . HOH IA 7 .   ? 28.919  240.605 61.349  1.00 43.08  ? 314 HOH F O   1 
HETATM 11784 O  O   . HOH IA 7 .   ? 0.651   241.543 59.941  1.00 27.96  ? 315 HOH F O   1 
HETATM 11785 O  O   . HOH IA 7 .   ? 4.520   249.255 42.955  1.00 46.21  ? 316 HOH F O   1 
HETATM 11786 O  O   . HOH IA 7 .   ? 20.783  248.131 41.395  1.00 43.07  ? 317 HOH F O   1 
HETATM 11787 O  O   . HOH IA 7 .   ? 16.421  223.196 62.854  1.00 30.67  ? 318 HOH F O   1 
HETATM 11788 O  O   . HOH IA 7 .   ? 35.649  232.262 51.486  1.00 39.64  ? 319 HOH F O   1 
HETATM 11789 O  O   . HOH IA 7 .   ? 12.700  232.514 46.696  1.00 40.30  ? 320 HOH F O   1 
HETATM 11790 O  O   . HOH IA 7 .   ? 1.089   236.294 55.412  1.00 32.40  ? 321 HOH F O   1 
HETATM 11791 O  O   . HOH IA 7 .   ? 29.908  230.491 51.373  1.00 48.88  ? 322 HOH F O   1 
HETATM 11792 O  O   . HOH IA 7 .   ? -3.175  238.281 55.960  1.00 36.23  ? 323 HOH F O   1 
HETATM 11793 O  O   . HOH IA 7 .   ? 3.360   241.923 47.196  1.00 35.13  ? 324 HOH F O   1 
HETATM 11794 O  O   . HOH IA 7 .   ? 16.982  249.976 47.828  1.00 34.28  ? 325 HOH F O   1 
HETATM 11795 O  O   . HOH IA 7 .   ? 11.176  245.149 60.298  1.00 39.50  ? 326 HOH F O   1 
HETATM 11796 O  O   . HOH IA 7 .   ? 4.804   243.656 40.029  1.00 45.79  ? 327 HOH F O   1 
HETATM 11797 O  O   . HOH IA 7 .   ? 11.921  244.176 42.964  1.00 28.39  ? 328 HOH F O   1 
HETATM 11798 O  O   . HOH IA 7 .   ? 15.525  225.405 61.568  1.00 28.89  ? 329 HOH F O   1 
HETATM 11799 O  O   . HOH IA 7 .   ? 9.811   238.943 52.299  1.00 27.83  ? 330 HOH F O   1 
HETATM 11800 O  O   . HOH IA 7 .   ? 19.803  228.553 69.789  1.00 37.01  ? 331 HOH F O   1 
HETATM 11801 O  O   . HOH IA 7 .   ? 3.663   252.521 58.748  1.00 41.86  ? 332 HOH F O   1 
HETATM 11802 O  O   . HOH IA 7 .   ? 6.242   231.997 64.404  1.00 29.39  ? 333 HOH F O   1 
HETATM 11803 O  O   . HOH IA 7 .   ? 29.739  239.142 57.065  1.00 23.09  ? 334 HOH F O   1 
HETATM 11804 O  O   . HOH IA 7 .   ? 4.718   247.300 40.120  1.00 44.63  ? 335 HOH F O   1 
HETATM 11805 O  O   . HOH IA 7 .   ? 9.122   237.108 41.826  1.00 40.78  ? 336 HOH F O   1 
HETATM 11806 O  O   . HOH IA 7 .   ? 21.319  241.369 38.923  1.00 36.00  ? 337 HOH F O   1 
HETATM 11807 O  O   . HOH IA 7 .   ? 29.803  248.580 57.502  1.00 26.30  ? 338 HOH F O   1 
HETATM 11808 O  O   . HOH IA 7 .   ? 15.747  239.687 39.149  1.00 53.52  ? 339 HOH F O   1 
HETATM 11809 O  O   . HOH IA 7 .   ? 23.543  240.210 74.889  1.00 45.64  ? 340 HOH F O   1 
HETATM 11810 O  O   . HOH IA 7 .   ? 13.206  246.022 44.159  1.00 27.26  ? 341 HOH F O   1 
HETATM 11811 O  O   . HOH IA 7 .   ? 11.859  229.955 71.797  1.00 32.52  ? 342 HOH F O   1 
HETATM 11812 O  O   . HOH IA 7 .   ? 11.501  232.309 53.058  1.00 33.36  ? 343 HOH F O   1 
HETATM 11813 O  O   . HOH IA 7 .   ? 14.539  235.737 68.525  1.00 27.38  ? 344 HOH F O   1 
HETATM 11814 O  O   . HOH IA 7 .   ? 24.580  247.093 59.079  1.00 39.86  ? 345 HOH F O   1 
HETATM 11815 O  O   . HOH IA 7 .   ? 28.596  255.574 56.638  1.00 44.32  ? 346 HOH F O   1 
HETATM 11816 O  O   . HOH IA 7 .   ? 8.012   249.488 50.076  1.00 35.78  ? 347 HOH F O   1 
HETATM 11817 O  O   . HOH IA 7 .   ? 13.144  252.491 40.961  1.00 47.95  ? 348 HOH F O   1 
HETATM 11818 O  O   . HOH IA 7 .   ? 8.609   223.939 71.794  1.00 55.05  ? 349 HOH F O   1 
HETATM 11819 O  O   . HOH IA 7 .   ? 11.509  244.133 57.875  1.00 32.47  ? 350 HOH F O   1 
HETATM 11820 O  O   . HOH IA 7 .   ? 8.754   245.860 66.976  1.00 48.72  ? 351 HOH F O   1 
HETATM 11821 O  O   . HOH IA 7 .   ? 20.867  224.767 56.380  1.00 38.94  ? 352 HOH F O   1 
HETATM 11822 O  O   . HOH IA 7 .   ? 33.303  235.481 63.462  1.00 48.12  ? 353 HOH F O   1 
HETATM 11823 O  O   . HOH IA 7 .   ? 16.964  251.810 59.739  1.00 42.58  ? 354 HOH F O   1 
HETATM 11824 O  O   . HOH IA 7 .   ? 20.863  243.259 68.029  1.00 49.48  ? 355 HOH F O   1 
HETATM 11825 O  O   . HOH IA 7 .   ? 23.062  229.803 39.680  1.00 41.63  ? 356 HOH F O   1 
HETATM 11826 O  O   . HOH IA 7 .   ? 22.448  221.356 58.712  1.00 46.42  ? 357 HOH F O   1 
HETATM 11827 O  O   . HOH IA 7 .   ? 8.295   251.792 58.424  1.00 43.58  ? 358 HOH F O   1 
HETATM 11828 O  O   . HOH IA 7 .   ? 2.914   239.953 43.078  1.00 43.73  ? 359 HOH F O   1 
HETATM 11829 O  O   . HOH IA 7 .   ? 32.976  233.672 44.527  1.00 43.26  ? 360 HOH F O   1 
HETATM 11830 O  O   . HOH IA 7 .   ? 14.403  229.935 42.642  1.00 46.13  ? 361 HOH F O   1 
HETATM 11831 O  O   . HOH IA 7 .   ? -1.277  247.557 49.136  1.00 54.78  ? 362 HOH F O   1 
HETATM 11832 O  O   . HOH IA 7 .   ? 22.193  251.408 46.928  1.00 31.15  ? 363 HOH F O   1 
HETATM 11833 O  O   . HOH IA 7 .   ? 30.823  228.934 55.506  1.00 42.23  ? 364 HOH F O   1 
HETATM 11834 O  O   . HOH IA 7 .   ? 17.956  238.773 39.385  1.00 42.33  ? 365 HOH F O   1 
HETATM 11835 O  O   . HOH IA 7 .   ? -1.406  244.181 52.740  1.00 22.98  ? 366 HOH F O   1 
HETATM 11836 O  O   . HOH IA 7 .   ? 20.645  239.218 69.026  1.00 35.86  ? 367 HOH F O   1 
HETATM 11837 O  O   . HOH IA 7 .   ? 29.784  242.148 58.594  1.00 41.28  ? 368 HOH F O   1 
HETATM 11838 O  O   . HOH IA 7 .   ? 27.794  231.517 64.339  1.00 61.40  ? 369 HOH F O   1 
HETATM 11839 O  O   . HOH IA 7 .   ? 13.062  228.735 48.908  1.00 36.39  ? 370 HOH F O   1 
HETATM 11840 O  O   . HOH IA 7 .   ? 16.187  247.244 65.364  1.00 35.56  ? 371 HOH F O   1 
HETATM 11841 O  O   . HOH IA 7 .   ? 12.291  237.315 68.533  1.00 30.84  ? 372 HOH F O   1 
HETATM 11842 O  O   . HOH IA 7 .   ? 5.965   236.971 64.810  1.00 33.49  ? 373 HOH F O   1 
HETATM 11843 O  O   . HOH IA 7 .   ? 22.265  246.671 65.918  1.00 39.47  ? 374 HOH F O   1 
HETATM 11844 O  O   . HOH IA 7 .   ? 27.587  233.687 39.257  1.00 39.45  ? 375 HOH F O   1 
HETATM 11845 O  O   . HOH IA 7 .   ? 26.359  245.253 58.964  1.00 39.29  ? 376 HOH F O   1 
HETATM 11846 O  O   . HOH IA 7 .   ? 22.622  254.435 56.190  1.00 38.64  ? 377 HOH F O   1 
HETATM 11847 O  O   . HOH IA 7 .   ? 22.220  226.596 69.861  1.00 37.71  ? 378 HOH F O   1 
HETATM 11848 O  O   . HOH IA 7 .   ? 18.777  222.505 66.987  1.00 42.19  ? 379 HOH F O   1 
HETATM 11849 O  O   . HOH IA 7 .   ? 6.795   249.739 41.174  1.00 41.61  ? 380 HOH F O   1 
HETATM 11850 O  O   . HOH IA 7 .   ? 26.266  227.867 58.697  1.00 41.23  ? 381 HOH F O   1 
HETATM 11851 O  O   . HOH IA 7 .   ? 6.173   234.497 49.252  1.00 27.35  ? 382 HOH F O   1 
HETATM 11852 O  O   . HOH IA 7 .   ? 11.977  248.343 53.750  1.00 34.64  ? 383 HOH F O   1 
HETATM 11853 O  O   . HOH IA 7 .   ? 10.115  240.172 41.452  1.00 40.45  ? 384 HOH F O   1 
HETATM 11854 O  O   . HOH IA 7 .   ? 3.608   238.630 61.002  1.00 50.35  ? 385 HOH F O   1 
HETATM 11855 O  O   . HOH IA 7 .   ? 43.423  232.247 48.367  1.00 43.02  ? 386 HOH F O   1 
HETATM 11856 O  O   . HOH IA 7 .   ? 22.681  228.076 42.548  1.00 50.23  ? 387 HOH F O   1 
HETATM 11857 O  O   . HOH IA 7 .   ? 13.310  247.648 60.097  1.00 42.73  ? 388 HOH F O   1 
HETATM 11858 O  O   . HOH IA 7 .   ? 22.490  223.150 66.177  1.00 41.94  ? 389 HOH F O   1 
HETATM 11859 O  O   . HOH IA 7 .   ? 8.091   234.630 65.870  1.00 47.47  ? 390 HOH F O   1 
HETATM 11860 O  O   . HOH IA 7 .   ? 17.627  251.630 41.294  1.00 45.63  ? 391 HOH F O   1 
HETATM 11861 O  O   . HOH IA 7 .   ? 20.167  222.165 64.272  1.00 56.78  ? 392 HOH F O   1 
HETATM 11862 O  O   . HOH IA 7 .   ? 1.096   250.649 59.525  1.00 32.76  ? 393 HOH F O   1 
HETATM 11863 O  O   . HOH IA 7 .   ? 22.288  224.435 58.443  1.00 44.83  ? 394 HOH F O   1 
HETATM 11864 O  O   . HOH IA 7 .   ? 20.073  225.157 71.933  1.00 42.07  ? 395 HOH F O   1 
HETATM 11865 O  O   . HOH IA 7 .   ? 26.370  246.493 39.788  1.00 53.81  ? 396 HOH F O   1 
HETATM 11866 O  O   . HOH IA 7 .   ? 11.476  221.948 66.779  1.00 41.43  ? 397 HOH F O   1 
HETATM 11867 O  O   . HOH IA 7 .   ? 2.714   237.544 41.861  1.00 42.52  ? 398 HOH F O   1 
HETATM 11868 O  O   . HOH IA 7 .   ? 7.860   246.354 61.644  1.00 44.28  ? 399 HOH F O   1 
HETATM 11869 O  O   . HOH IA 7 .   ? 12.979  244.937 70.134  1.00 49.83  ? 400 HOH F O   1 
HETATM 11870 O  O   . HOH IA 7 .   ? 28.623  242.760 38.627  1.00 41.75  ? 401 HOH F O   1 
HETATM 11871 O  O   . HOH IA 7 .   ? 15.519  251.835 57.428  1.00 38.48  ? 402 HOH F O   1 
HETATM 11872 O  O   . HOH IA 7 .   ? 23.075  251.076 44.580  1.00 42.58  ? 403 HOH F O   1 
HETATM 11873 O  O   . HOH IA 7 .   ? 19.705  254.883 59.462  1.00 46.54  ? 404 HOH F O   1 
HETATM 11874 O  O   . HOH IA 7 .   ? 1.879   249.449 62.237  1.00 35.75  ? 405 HOH F O   1 
HETATM 11875 O  O   . HOH IA 7 .   ? 19.473  236.048 39.704  1.00 47.26  ? 406 HOH F O   1 
HETATM 11876 O  O   . HOH IA 7 .   ? -1.065  257.377 59.006  1.00 47.88  ? 407 HOH F O   1 
HETATM 11877 O  O   . HOH IA 7 .   ? 14.447  229.556 72.137  1.00 43.39  ? 408 HOH F O   1 
HETATM 11878 O  O   . HOH IA 7 .   ? 10.679  216.028 73.070  1.00 55.88  ? 409 HOH F O   1 
HETATM 11879 O  O   . HOH IA 7 .   ? 1.442   240.530 49.016  1.00 30.22  ? 410 HOH F O   1 
HETATM 11880 O  O   . HOH IA 7 .   ? 2.257   245.393 50.534  1.00 39.78  ? 411 HOH F O   1 
HETATM 11881 O  O   . HOH IA 7 .   ? 6.038   227.760 70.486  1.00 54.03  ? 412 HOH F O   1 
HETATM 11882 O  O   . HOH IA 7 .   ? 28.463  235.421 64.812  1.00 56.52  ? 413 HOH F O   1 
HETATM 11883 O  O   . HOH IA 7 .   ? 20.593  249.827 44.120  1.00 47.10  ? 414 HOH F O   1 
HETATM 11884 O  O   . HOH IA 7 .   ? 16.290  231.418 37.564  1.00 50.94  ? 415 HOH F O   1 
HETATM 11885 O  O   . HOH IA 7 .   ? 22.537  237.847 74.992  1.00 42.74  ? 416 HOH F O   1 
HETATM 11886 O  O   . HOH IA 7 .   ? 3.354   237.141 35.507  1.00 60.56  ? 417 HOH F O   1 
HETATM 11887 O  O   . HOH IA 7 .   ? 18.290  250.565 45.562  1.00 41.18  ? 418 HOH F O   1 
HETATM 11888 O  O   . HOH IA 7 .   ? 4.998   250.460 62.781  1.00 48.25  ? 419 HOH F O   1 
HETATM 11889 O  O   . HOH IA 7 .   ? 13.144  248.345 56.090  1.00 31.41  ? 420 HOH F O   1 
HETATM 11890 O  O   . HOH IA 7 .   ? 19.787  247.220 65.115  1.00 54.77  ? 421 HOH F O   1 
HETATM 11891 O  O   . HOH IA 7 .   ? 9.328   225.194 64.466  1.00 40.44  ? 422 HOH F O   1 
HETATM 11892 O  O   . HOH IA 7 .   ? 24.169  255.507 58.349  1.00 46.73  ? 423 HOH F O   1 
HETATM 11893 O  O   . HOH IA 7 .   ? 8.827   249.558 62.146  1.00 48.54  ? 424 HOH F O   1 
HETATM 11894 O  O   . HOH IA 7 .   ? 3.069   235.429 58.985  1.00 39.92  ? 425 HOH F O   1 
HETATM 11895 O  O   . HOH IA 7 .   ? 1.839   246.182 63.919  1.00 47.36  ? 426 HOH F O   1 
HETATM 11896 O  O   . HOH IA 7 .   ? -0.636  241.946 48.554  1.00 35.76  ? 427 HOH F O   1 
HETATM 11897 O  O   . HOH IA 7 .   ? 16.190  233.975 73.003  1.00 43.36  ? 428 HOH F O   1 
HETATM 11898 O  O   . HOH IA 7 .   ? 27.961  243.435 69.962  1.00 47.48  ? 429 HOH F O   1 
HETATM 11899 O  O   . HOH IA 7 .   ? 9.071   252.354 46.758  1.00 42.88  ? 430 HOH F O   1 
HETATM 11900 O  O   . HOH IA 7 .   ? 19.005  249.870 36.629  1.00 45.74  ? 431 HOH F O   1 
HETATM 11901 O  O   A HOH IA 7 .   ? 27.028  243.945 65.248  0.50 31.99  ? 432 HOH F O   1 
HETATM 11902 O  O   B HOH IA 7 .   ? 26.008  244.878 64.404  0.50 31.60  ? 432 HOH F O   1 
HETATM 11903 O  O   . HOH IA 7 .   ? 26.873  229.050 62.211  1.00 53.30  ? 433 HOH F O   1 
HETATM 11904 O  O   . HOH IA 7 .   ? 32.524  240.224 41.898  1.00 54.05  ? 434 HOH F O   1 
HETATM 11905 O  O   . HOH IA 7 .   ? 29.013  233.270 37.381  1.00 44.79  ? 435 HOH F O   1 
HETATM 11906 O  O   . HOH IA 7 .   ? 7.080   227.524 64.764  1.00 51.71  ? 436 HOH F O   1 
HETATM 11907 O  O   . HOH IA 7 .   ? 25.296  234.740 72.521  1.00 55.49  ? 437 HOH F O   1 
HETATM 11908 O  O   . HOH IA 7 .   ? 13.274  241.475 38.893  1.00 37.42  ? 438 HOH F O   1 
HETATM 11909 O  O   . HOH IA 7 .   ? 2.197   232.089 45.060  1.00 51.12  ? 439 HOH F O   1 
HETATM 11910 O  O   . HOH IA 7 .   ? 28.216  231.882 72.057  1.00 55.76  ? 440 HOH F O   1 
HETATM 11911 O  O   . HOH IA 7 .   ? 6.251   228.263 67.385  1.00 48.18  ? 441 HOH F O   1 
HETATM 11912 O  O   . HOH IA 7 .   ? 29.585  227.562 44.006  1.00 44.57  ? 442 HOH F O   1 
HETATM 11913 O  O   . HOH IA 7 .   ? 14.965  254.338 49.552  1.00 50.67  ? 443 HOH F O   1 
HETATM 11914 O  O   . HOH IA 7 .   ? 10.554  250.942 53.592  1.00 43.25  ? 444 HOH F O   1 
HETATM 11915 O  O   . HOH IA 7 .   ? 18.341  239.417 70.562  1.00 40.16  ? 445 HOH F O   1 
HETATM 11916 O  O   . HOH IA 7 .   ? 15.122  253.651 46.348  1.00 46.08  ? 446 HOH F O   1 
HETATM 11917 O  O   . HOH IA 7 .   ? 23.935  249.688 39.531  1.00 54.08  ? 447 HOH F O   1 
HETATM 11918 O  O   . HOH IA 7 .   ? 26.204  257.646 58.104  1.00 43.23  ? 448 HOH F O   1 
HETATM 11919 O  O   . HOH IA 7 .   ? 7.909   237.208 38.516  1.00 52.00  ? 449 HOH F O   1 
HETATM 11920 O  O   . HOH IA 7 .   ? -3.441  243.377 51.517  1.00 30.22  ? 450 HOH F O   1 
HETATM 11921 O  O   . HOH IA 7 .   ? -2.805  241.171 49.843  1.00 43.35  ? 451 HOH F O   1 
HETATM 11922 O  O   . HOH IA 7 .   ? 13.437  240.192 70.895  1.00 47.74  ? 452 HOH F O   1 
HETATM 11923 O  O   . HOH IA 7 .   ? 13.704  242.718 71.345  1.00 45.90  ? 453 HOH F O   1 
HETATM 11924 O  O   . HOH IA 7 .   ? 20.236  254.639 44.416  1.00 43.17  ? 454 HOH F O   1 
HETATM 11925 O  O   . HOH IA 7 .   ? 24.957  221.554 60.149  1.00 54.39  ? 455 HOH F O   1 
HETATM 11926 O  O   . HOH IA 7 .   ? 4.897   229.651 63.132  1.00 41.01  ? 456 HOH F O   1 
HETATM 11927 O  O   . HOH IA 7 .   ? 9.767   251.429 51.147  1.00 50.18  ? 457 HOH F O   1 
HETATM 11928 O  O   . HOH IA 7 .   ? 11.877  242.018 41.113  1.00 36.12  ? 458 HOH F O   1 
HETATM 11929 O  O   . HOH IA 7 .   ? 4.712   252.886 63.467  1.00 50.44  ? 459 HOH F O   1 
HETATM 11930 O  O   . HOH IA 7 .   ? 11.620  249.767 60.831  1.00 48.70  ? 460 HOH F O   1 
HETATM 11931 O  O   . HOH IA 7 .   ? 0.956   238.528 60.299  1.00 36.02  ? 461 HOH F O   1 
HETATM 11932 O  O   . HOH IA 7 .   ? 17.894  249.284 68.232  1.00 52.14  ? 462 HOH F O   1 
HETATM 11933 O  O   . HOH IA 7 .   ? 22.834  221.201 36.750  1.00 44.70  ? 463 HOH F O   1 
HETATM 11934 O  O   . HOH IA 7 .   ? 10.406  251.666 56.107  1.00 46.33  ? 464 HOH F O   1 
HETATM 11935 O  O   . HOH IA 7 .   ? 21.290  218.687 60.498  1.00 51.25  ? 465 HOH F O   1 
HETATM 11936 O  O   . HOH IA 7 .   ? 12.584  253.013 60.225  1.00 53.22  ? 466 HOH F O   1 
HETATM 11937 O  O   . HOH IA 7 .   ? 25.238  229.352 72.417  1.00 44.41  ? 467 HOH F O   1 
HETATM 11938 O  O   . HOH IA 7 .   ? 14.557  256.456 57.580  1.00 57.88  ? 468 HOH F O   1 
HETATM 11939 O  O   . HOH IA 7 .   ? 0.362   233.178 35.170  1.00 51.04  ? 469 HOH F O   1 
HETATM 11940 O  O   . HOH JA 7 .   ? 13.634  248.434 -3.794  1.00 36.57  ? 201 HOH G O   1 
HETATM 11941 O  O   . HOH JA 7 .   ? 0.162   246.936 -12.086 1.00 45.05  ? 202 HOH G O   1 
HETATM 11942 O  O   . HOH JA 7 .   ? 2.643   265.704 -25.454 1.00 44.30  ? 203 HOH G O   1 
HETATM 11943 O  O   . HOH JA 7 .   ? 16.778  248.838 -25.680 1.00 50.54  ? 204 HOH G O   1 
HETATM 11944 O  O   . HOH JA 7 .   ? -1.372  249.555 -15.029 1.00 37.70  ? 205 HOH G O   1 
HETATM 11945 O  O   . HOH JA 7 .   ? 21.212  257.522 -17.481 1.00 50.85  ? 206 HOH G O   1 
HETATM 11946 O  O   . HOH JA 7 .   ? 20.311  252.696 -25.964 1.00 54.88  ? 207 HOH G O   1 
HETATM 11947 O  O   . HOH JA 7 .   ? 14.981  252.806 0.146   1.00 49.56  ? 208 HOH G O   1 
HETATM 11948 O  O   . HOH JA 7 .   ? 15.755  249.396 -5.419  1.00 37.78  ? 209 HOH G O   1 
HETATM 11949 O  O   . HOH JA 7 .   ? 15.212  251.744 -32.164 1.00 44.54  ? 210 HOH G O   1 
HETATM 11950 O  O   . HOH JA 7 .   ? 20.598  252.036 -5.957  1.00 51.64  ? 211 HOH G O   1 
HETATM 11951 O  O   . HOH JA 7 .   ? 13.137  261.599 -26.456 1.00 57.81  ? 212 HOH G O   1 
HETATM 11952 O  O   . HOH JA 7 .   ? 6.176   239.228 -1.748  1.00 52.68  ? 213 HOH G O   1 
HETATM 11953 O  O   . HOH JA 7 .   ? 16.411  243.272 -16.468 1.00 61.50  ? 214 HOH G O   1 
HETATM 11954 O  O   . HOH JA 7 .   ? 6.823   262.290 -4.728  1.00 50.64  ? 215 HOH G O   1 
HETATM 11955 O  O   . HOH JA 7 .   ? 5.270   246.378 -4.998  1.00 41.43  ? 216 HOH G O   1 
HETATM 11956 O  O   . HOH JA 7 .   ? 3.274   236.770 -23.747 1.00 44.79  ? 217 HOH G O   1 
HETATM 11957 O  O   . HOH JA 7 .   ? 16.571  247.147 -18.775 1.00 58.69  ? 218 HOH G O   1 
HETATM 11958 O  O   . HOH JA 7 .   ? 13.898  259.964 -11.837 1.00 44.38  ? 219 HOH G O   1 
HETATM 11959 O  O   . HOH JA 7 .   ? 9.283   245.297 -5.716  1.00 43.59  ? 220 HOH G O   1 
HETATM 11960 O  O   . HOH JA 7 .   ? 19.405  256.166 1.563   1.00 48.11  ? 221 HOH G O   1 
HETATM 11961 O  O   . HOH JA 7 .   ? 10.272  255.030 -0.842  1.00 39.28  ? 222 HOH G O   1 
HETATM 11962 O  O   . HOH JA 7 .   ? -1.160  241.019 -18.198 1.00 36.86  ? 223 HOH G O   1 
HETATM 11963 O  O   . HOH JA 7 .   ? 7.082   258.988 -32.599 1.00 52.23  ? 224 HOH G O   1 
HETATM 11964 O  O   . HOH JA 7 .   ? 24.131  259.439 -0.759  1.00 55.28  ? 225 HOH G O   1 
HETATM 11965 O  O   . HOH JA 7 .   ? 18.838  262.022 -1.747  1.00 43.74  ? 226 HOH G O   1 
HETATM 11966 O  O   . HOH JA 7 .   ? -2.309  259.441 -30.140 1.00 55.92  ? 227 HOH G O   1 
HETATM 11967 O  O   . HOH JA 7 .   ? 7.900   236.321 -9.424  1.00 52.32  ? 228 HOH G O   1 
HETATM 11968 O  O   . HOH JA 7 .   ? 8.809   237.789 -12.545 1.00 53.12  ? 229 HOH G O   1 
HETATM 11969 O  O   . HOH JA 7 .   ? 8.088   239.558 -10.644 1.00 54.11  ? 230 HOH G O   1 
HETATM 11970 O  O   A HOH JA 7 .   ? 2.133   259.857 -9.540  0.50 27.54  ? 231 HOH G O   1 
HETATM 11971 O  O   B HOH JA 7 .   ? 0.504   260.393 -10.229 0.50 30.88  ? 231 HOH G O   1 
HETATM 11972 O  O   . HOH JA 7 .   ? 2.086   244.125 -12.045 1.00 46.95  ? 232 HOH G O   1 
HETATM 11973 O  O   . HOH JA 7 .   ? 28.238  254.764 -20.924 1.00 47.36  ? 233 HOH G O   1 
HETATM 11974 O  O   . HOH JA 7 .   ? 22.185  251.727 -8.566  1.00 49.39  ? 234 HOH G O   1 
HETATM 11975 O  O   . HOH JA 7 .   ? 6.093   236.282 -22.470 1.00 45.75  ? 235 HOH G O   1 
HETATM 11976 O  O   . HOH JA 7 .   ? -7.142  259.125 -24.010 1.00 49.92  ? 236 HOH G O   1 
HETATM 11977 O  O   . HOH JA 7 .   ? 23.335  254.157 -8.503  1.00 48.66  ? 237 HOH G O   1 
HETATM 11978 O  O   . HOH JA 7 .   ? 18.241  253.189 0.014   1.00 41.78  ? 238 HOH G O   1 
HETATM 11979 O  O   . HOH JA 7 .   ? -1.036  246.606 -14.651 1.00 38.13  ? 239 HOH G O   1 
HETATM 11980 O  O   . HOH JA 7 .   ? 15.828  241.725 -18.100 1.00 51.27  ? 240 HOH G O   1 
HETATM 11981 O  O   A HOH JA 7 .   ? 1.374   231.547 -15.334 0.50 27.70  ? 241 HOH G O   1 
HETATM 11982 O  O   B HOH JA 7 .   ? 3.290   231.075 -14.844 0.50 30.64  ? 241 HOH G O   1 
HETATM 11983 O  O   . HOH JA 7 .   ? 13.178  267.336 -17.551 1.00 51.69  ? 242 HOH G O   1 
HETATM 11984 O  O   . HOH JA 7 .   ? -4.996  266.558 -16.900 1.00 48.17  ? 243 HOH G O   1 
HETATM 11985 O  O   . HOH JA 7 .   ? 4.060   254.578 1.707   1.00 46.25  ? 244 HOH G O   1 
HETATM 11986 O  O   . HOH JA 7 .   ? -8.001  260.815 -26.961 1.00 56.76  ? 245 HOH G O   1 
HETATM 11987 O  O   . HOH JA 7 .   ? 10.160  266.346 -6.912  1.00 54.42  ? 246 HOH G O   1 
HETATM 11988 O  O   . HOH JA 7 .   ? 5.437   267.282 -13.891 1.00 46.82  ? 247 HOH G O   1 
HETATM 11989 O  O   . HOH JA 7 .   ? 22.082  252.156 -2.351  1.00 44.96  ? 248 HOH G O   1 
HETATM 11990 O  O   . HOH JA 7 .   ? 0.903   237.791 -11.145 1.00 48.89  ? 249 HOH G O   1 
HETATM 11991 O  O   . HOH JA 7 .   ? 17.227  246.534 -27.068 1.00 40.40  ? 250 HOH G O   1 
HETATM 11992 O  O   . HOH JA 7 .   ? 17.674  257.054 -23.422 1.00 48.80  ? 251 HOH G O   1 
HETATM 11993 O  O   A HOH JA 7 .   ? 3.441   256.952 -6.198  0.50 32.02  ? 252 HOH G O   1 
HETATM 11994 O  O   B HOH JA 7 .   ? 2.158   255.807 -5.950  0.50 32.93  ? 252 HOH G O   1 
HETATM 11995 O  O   . HOH JA 7 .   ? 16.697  259.079 4.992   1.00 50.89  ? 253 HOH G O   1 
HETATM 11996 O  O   . HOH JA 7 .   ? 19.186  247.805 -30.103 1.00 55.30  ? 254 HOH G O   1 
HETATM 11997 O  O   . HOH JA 7 .   ? 0.985   252.154 -6.905  1.00 54.06  ? 255 HOH G O   1 
HETATM 11998 O  O   . HOH JA 7 .   ? -14.947 261.632 -14.651 1.00 58.87  ? 256 HOH G O   1 
HETATM 11999 O  O   . HOH JA 7 .   ? -7.165  255.661 -30.788 1.00 46.68  ? 257 HOH G O   1 
HETATM 12000 O  O   . HOH JA 7 .   ? 17.986  238.962 -15.619 1.00 49.82  ? 258 HOH G O   1 
HETATM 12001 O  O   . HOH JA 7 .   ? 10.499  238.493 -28.013 1.00 64.45  ? 259 HOH G O   1 
HETATM 12002 O  O   . HOH JA 7 .   ? 21.222  252.309 -23.088 1.00 58.76  ? 260 HOH G O   1 
HETATM 12003 O  O   . HOH JA 7 .   ? 2.014   253.445 -4.789  1.00 59.88  ? 261 HOH G O   1 
HETATM 12004 O  O   . HOH JA 7 .   ? 19.340  248.965 -23.444 1.00 45.46  ? 262 HOH G O   1 
HETATM 12005 O  O   . HOH JA 7 .   ? 21.149  259.303 -5.758  1.00 45.13  ? 263 HOH G O   1 
HETATM 12006 O  O   A HOH JA 7 .   ? 23.879  255.720 -4.060  0.50 33.10  ? 264 HOH G O   1 
HETATM 12007 O  O   B HOH JA 7 .   ? 25.031  254.690 -4.541  0.50 41.71  ? 264 HOH G O   1 
HETATM 12008 O  O   A HOH JA 7 .   ? 2.921   242.304 -9.616  0.50 25.71  ? 265 HOH G O   1 
HETATM 12009 O  O   B HOH JA 7 .   ? 3.941   242.097 -10.813 0.50 28.41  ? 265 HOH G O   1 
HETATM 12010 O  O   . HOH JA 7 .   ? 17.473  251.004 -33.681 1.00 51.07  ? 266 HOH G O   1 
HETATM 12011 O  O   . HOH JA 7 .   ? 7.554   235.657 -5.672  1.00 52.69  ? 267 HOH G O   1 
HETATM 12012 O  O   . HOH JA 7 .   ? 14.721  240.446 -22.384 1.00 58.11  ? 268 HOH G O   1 
HETATM 12013 O  O   . HOH JA 7 .   ? 18.274  246.621 -33.560 1.00 54.43  ? 269 HOH G O   1 
HETATM 12014 O  O   . HOH JA 7 .   ? 11.755  244.789 -4.523  1.00 39.75  ? 270 HOH G O   1 
HETATM 12015 O  O   . HOH JA 7 .   ? -4.396  258.810 -32.981 1.00 54.59  ? 271 HOH G O   1 
HETATM 12016 O  O   . HOH JA 7 .   ? 19.799  259.214 -27.940 1.00 51.16  ? 272 HOH G O   1 
HETATM 12017 O  O   . HOH JA 7 .   ? 16.537  244.919 -4.397  1.00 55.11  ? 273 HOH G O   1 
HETATM 12018 O  O   . HOH JA 7 .   ? -0.547  235.586 -10.967 1.00 44.44  ? 274 HOH G O   1 
HETATM 12019 O  O   . HOH JA 7 .   ? 11.981  241.988 -6.546  1.00 49.47  ? 275 HOH G O   1 
HETATM 12020 O  O   . HOH JA 7 .   ? 0.732   267.810 -16.339 1.00 49.63  ? 276 HOH G O   1 
HETATM 12021 O  O   . HOH JA 7 .   ? 3.124   267.347 -16.695 1.00 51.83  ? 277 HOH G O   1 
HETATM 12022 O  O   . HOH JA 7 .   ? -6.537  266.980 -32.010 1.00 44.41  ? 278 HOH G O   1 
HETATM 12023 O  O   . HOH JA 7 .   ? 20.073  254.479 -32.555 1.00 55.05  ? 279 HOH G O   1 
HETATM 12024 O  O   . HOH JA 7 .   ? 20.516  259.511 -31.330 1.00 56.35  ? 280 HOH G O   1 
HETATM 12025 O  O   . HOH KA 7 .   ? -5.010  233.118 -10.327 1.00 48.77  ? 301 HOH H O   1 
HETATM 12026 O  O   . HOH KA 7 .   ? -25.779 252.593 -21.521 1.00 40.61  ? 302 HOH H O   1 
HETATM 12027 O  O   . HOH KA 7 .   ? -21.584 249.216 -29.287 1.00 39.15  ? 303 HOH H O   1 
HETATM 12028 O  O   . HOH KA 7 .   ? -21.313 218.540 -9.422  1.00 50.64  ? 304 HOH H O   1 
HETATM 12029 O  O   . HOH KA 7 .   ? -20.257 250.914 -28.001 1.00 44.76  ? 305 HOH H O   1 
HETATM 12030 O  O   . HOH KA 7 .   ? -21.075 235.522 -21.563 1.00 44.49  ? 306 HOH H O   1 
HETATM 12031 O  O   . HOH KA 7 .   ? -23.092 242.391 -20.932 1.00 33.43  ? 307 HOH H O   1 
HETATM 12032 O  O   . HOH KA 7 .   ? -20.569 230.318 -3.781  1.00 39.70  ? 308 HOH H O   1 
HETATM 12033 O  O   . HOH KA 7 .   ? -10.034 239.530 -42.008 1.00 63.86  ? 309 HOH H O   1 
HETATM 12034 O  O   . HOH KA 7 .   ? -36.810 256.861 -14.210 1.00 43.01  ? 310 HOH H O   1 
HETATM 12035 O  O   . HOH KA 7 .   ? -15.740 236.542 -3.976  1.00 32.64  ? 311 HOH H O   1 
HETATM 12036 O  O   . HOH KA 7 .   ? -34.357 246.835 -19.979 1.00 36.90  ? 312 HOH H O   1 
HETATM 12037 O  O   . HOH KA 7 .   ? -11.906 243.925 -5.157  1.00 42.93  ? 313 HOH H O   1 
HETATM 12038 O  O   . HOH KA 7 .   ? -12.295 227.202 -24.116 1.00 46.32  ? 314 HOH H O   1 
HETATM 12039 O  O   . HOH KA 7 .   ? -26.604 237.965 -25.386 1.00 35.62  ? 315 HOH H O   1 
HETATM 12040 O  O   . HOH KA 7 .   ? -15.866 224.994 -13.847 1.00 49.94  ? 316 HOH H O   1 
HETATM 12041 O  O   . HOH KA 7 .   ? -32.079 239.368 -26.220 1.00 54.12  ? 317 HOH H O   1 
HETATM 12042 O  O   . HOH KA 7 .   ? -30.505 256.742 -16.410 1.00 42.98  ? 318 HOH H O   1 
HETATM 12043 O  O   . HOH KA 7 .   ? -3.982  243.173 -12.289 1.00 46.11  ? 319 HOH H O   1 
HETATM 12044 O  O   . HOH KA 7 .   ? -26.394 237.576 -9.432  1.00 45.65  ? 320 HOH H O   1 
HETATM 12045 O  O   . HOH KA 7 .   ? -14.893 229.736 -28.942 1.00 58.53  ? 321 HOH H O   1 
HETATM 12046 O  O   . HOH KA 7 .   ? -3.463  251.598 -14.648 1.00 39.24  ? 322 HOH H O   1 
HETATM 12047 O  O   . HOH KA 7 .   ? -7.526  239.512 -5.760  1.00 39.20  ? 323 HOH H O   1 
HETATM 12048 O  O   . HOH KA 7 .   ? -6.578  241.047 -0.526  1.00 50.04  ? 324 HOH H O   1 
HETATM 12049 O  O   . HOH KA 7 .   ? -3.062  242.350 -17.006 1.00 39.80  ? 325 HOH H O   1 
HETATM 12050 O  O   . HOH KA 7 .   ? -2.127  247.266 -10.512 1.00 45.27  ? 326 HOH H O   1 
HETATM 12051 O  O   . HOH KA 7 .   ? -16.531 254.167 -23.741 1.00 45.53  ? 327 HOH H O   1 
HETATM 12052 O  O   . HOH KA 7 .   ? -2.881  235.173 -23.876 1.00 40.21  ? 328 HOH H O   1 
HETATM 12053 O  O   . HOH KA 7 .   ? -20.078 236.072 -31.778 1.00 44.48  ? 329 HOH H O   1 
HETATM 12054 O  O   . HOH KA 7 .   ? -12.427 229.497 -5.872  1.00 29.68  ? 330 HOH H O   1 
HETATM 12055 O  O   . HOH KA 7 .   ? -9.788  234.040 -33.200 1.00 45.35  ? 331 HOH H O   1 
HETATM 12056 O  O   . HOH KA 7 .   ? -29.872 246.176 -25.248 1.00 46.02  ? 332 HOH H O   1 
HETATM 12057 O  O   . HOH KA 7 .   ? -21.178 251.309 -18.031 1.00 35.40  ? 333 HOH H O   1 
HETATM 12058 O  O   . HOH KA 7 .   ? -10.613 235.830 -35.823 1.00 48.03  ? 334 HOH H O   1 
HETATM 12059 O  O   . HOH KA 7 .   ? -17.894 236.507 -5.942  1.00 43.41  ? 335 HOH H O   1 
HETATM 12060 O  O   . HOH KA 7 .   ? -31.750 238.665 -18.326 1.00 39.71  ? 336 HOH H O   1 
HETATM 12061 O  O   . HOH KA 7 .   ? -16.978 227.435 -14.685 1.00 41.57  ? 337 HOH H O   1 
HETATM 12062 O  O   . HOH KA 7 .   ? -15.384 243.578 -34.508 1.00 46.70  ? 338 HOH H O   1 
HETATM 12063 O  O   . HOH KA 7 .   ? -6.677  248.087 -13.899 1.00 45.50  ? 339 HOH H O   1 
HETATM 12064 O  O   . HOH KA 7 .   ? -19.721 232.811 -26.608 1.00 36.72  ? 340 HOH H O   1 
HETATM 12065 O  O   . HOH KA 7 .   ? -26.321 235.029 -19.100 1.00 49.44  ? 341 HOH H O   1 
HETATM 12066 O  O   . HOH KA 7 .   ? -32.514 242.971 -13.138 1.00 35.29  ? 342 HOH H O   1 
HETATM 12067 O  O   . HOH KA 7 .   ? -11.628 255.972 -24.649 1.00 44.31  ? 343 HOH H O   1 
HETATM 12068 O  O   . HOH KA 7 .   ? -21.400 246.273 -14.622 1.00 40.12  ? 344 HOH H O   1 
HETATM 12069 O  O   . HOH KA 7 .   ? -9.968  225.213 -13.432 1.00 54.51  ? 345 HOH H O   1 
HETATM 12070 O  O   . HOH KA 7 .   ? -26.368 233.036 -10.315 1.00 42.47  ? 346 HOH H O   1 
HETATM 12071 O  O   . HOH KA 7 .   ? -13.604 223.559 -9.673  1.00 49.75  ? 347 HOH H O   1 
HETATM 12072 O  O   . HOH KA 7 .   ? -12.033 240.043 -4.961  1.00 42.96  ? 348 HOH H O   1 
HETATM 12073 O  O   . HOH KA 7 .   ? -20.187 237.858 -5.397  1.00 39.48  ? 349 HOH H O   1 
HETATM 12074 O  O   . HOH KA 7 .   ? -7.354  238.935 -41.223 1.00 41.16  ? 350 HOH H O   1 
HETATM 12075 O  O   . HOH KA 7 .   ? -1.388  242.094 -11.654 1.00 44.84  ? 351 HOH H O   1 
HETATM 12076 O  O   . HOH KA 7 .   ? -32.148 252.180 -12.061 1.00 39.04  ? 352 HOH H O   1 
HETATM 12077 O  O   . HOH KA 7 .   ? -3.275  244.972 -14.832 1.00 39.49  ? 353 HOH H O   1 
HETATM 12078 O  O   . HOH KA 7 .   ? -16.531 257.912 -19.529 1.00 46.84  ? 354 HOH H O   1 
HETATM 12079 O  O   . HOH KA 7 .   ? -29.224 237.071 -17.266 1.00 41.62  ? 355 HOH H O   1 
HETATM 12080 O  O   . HOH KA 7 .   ? -11.449 233.221 -36.472 1.00 51.42  ? 356 HOH H O   1 
HETATM 12081 O  O   . HOH KA 7 .   ? -24.956 256.026 -24.519 1.00 53.31  ? 357 HOH H O   1 
HETATM 12082 O  O   . HOH KA 7 .   ? -10.241 257.350 -15.085 1.00 47.74  ? 358 HOH H O   1 
HETATM 12083 O  O   . HOH KA 7 .   ? -24.573 235.584 -8.422  1.00 45.83  ? 359 HOH H O   1 
HETATM 12084 O  O   . HOH KA 7 .   ? -6.024  230.770 -17.012 1.00 35.52  ? 360 HOH H O   1 
HETATM 12085 O  O   . HOH KA 7 .   ? -30.491 248.441 -21.622 1.00 43.13  ? 361 HOH H O   1 
HETATM 12086 O  O   . HOH KA 7 .   ? -31.496 247.854 -9.248  1.00 47.42  ? 362 HOH H O   1 
HETATM 12087 O  O   . HOH KA 7 .   ? -7.195  259.279 -12.675 1.00 50.46  ? 363 HOH H O   1 
HETATM 12088 O  O   . HOH KA 7 .   ? -8.821  257.620 -11.944 1.00 52.29  ? 364 HOH H O   1 
HETATM 12089 O  O   . HOH KA 7 .   ? -16.948 248.645 -7.335  1.00 46.32  ? 365 HOH H O   1 
HETATM 12090 O  O   A HOH KA 7 .   ? -20.023 248.791 -14.165 0.50 25.40  ? 366 HOH H O   1 
HETATM 12091 O  O   B HOH KA 7 .   ? -19.567 249.625 -12.584 0.50 30.88  ? 366 HOH H O   1 
HETATM 12092 O  O   . HOH KA 7 .   ? -17.440 254.329 -13.921 1.00 47.79  ? 367 HOH H O   1 
HETATM 12093 O  O   . HOH KA 7 .   ? -25.220 247.949 -10.700 1.00 51.29  ? 368 HOH H O   1 
HETATM 12094 O  O   . HOH KA 7 .   ? 2.561   240.467 -30.181 1.00 41.92  ? 369 HOH H O   1 
HETATM 12095 O  O   . HOH KA 7 .   ? -3.957  230.738 -18.689 1.00 39.38  ? 370 HOH H O   1 
HETATM 12096 O  O   . HOH KA 7 .   ? -4.959  244.865 -37.700 1.00 58.48  ? 371 HOH H O   1 
HETATM 12097 O  O   . HOH KA 7 .   ? -4.949  245.793 -11.945 1.00 49.63  ? 372 HOH H O   1 
HETATM 12098 O  O   . HOH KA 7 .   ? -16.216 244.820 -4.582  1.00 46.48  ? 373 HOH H O   1 
HETATM 12099 O  O   . HOH KA 7 .   ? -24.445 256.092 -14.635 1.00 63.98  ? 374 HOH H O   1 
HETATM 12100 O  O   . HOH KA 7 .   ? -19.527 249.601 -10.129 1.00 54.59  ? 375 HOH H O   1 
HETATM 12101 O  O   . HOH KA 7 .   ? -17.543 228.860 -3.335  1.00 44.70  ? 376 HOH H O   1 
HETATM 12102 O  O   . HOH KA 7 .   ? -19.499 257.480 -24.981 1.00 50.14  ? 377 HOH H O   1 
HETATM 12103 O  O   . HOH KA 7 .   ? -30.221 241.446 -31.755 1.00 54.58  ? 378 HOH H O   1 
HETATM 12104 O  O   . HOH KA 7 .   ? -11.354 225.738 -4.963  1.00 44.22  ? 379 HOH H O   1 
HETATM 12105 O  O   . HOH KA 7 .   ? -31.321 250.622 -9.690  1.00 43.98  ? 380 HOH H O   1 
HETATM 12106 O  O   . HOH KA 7 .   ? -31.129 244.776 -28.846 1.00 57.33  ? 381 HOH H O   1 
HETATM 12107 O  O   . HOH KA 7 .   ? -7.448  237.865 -0.590  1.00 50.24  ? 382 HOH H O   1 
HETATM 12108 O  O   . HOH KA 7 .   ? -20.057 251.012 -15.528 1.00 45.07  ? 383 HOH H O   1 
HETATM 12109 O  O   . HOH KA 7 .   ? -5.842  251.779 -5.076  1.00 48.34  ? 384 HOH H O   1 
HETATM 12110 O  O   . HOH KA 7 .   ? -8.267  228.244 -32.174 1.00 60.46  ? 385 HOH H O   1 
HETATM 12111 O  O   . HOH KA 7 .   ? -27.049 255.507 -23.218 1.00 48.76  ? 386 HOH H O   1 
HETATM 12112 O  O   . HOH KA 7 .   ? 4.815   237.983 -30.694 1.00 50.01  ? 387 HOH H O   1 
HETATM 12113 O  O   . HOH KA 7 .   ? -14.016 232.820 -1.889  1.00 50.64  ? 388 HOH H O   1 
HETATM 12114 O  O   . HOH KA 7 .   ? 0.403   239.776 -34.261 1.00 61.44  ? 389 HOH H O   1 
HETATM 12115 O  O   . HOH KA 7 .   ? -11.412 238.654 1.067   1.00 40.95  ? 390 HOH H O   1 
HETATM 12116 O  O   . HOH KA 7 .   ? -8.610  250.663 -3.980  1.00 59.89  ? 391 HOH H O   1 
HETATM 12117 O  O   . HOH KA 7 .   ? -23.541 250.385 -10.223 1.00 51.49  ? 392 HOH H O   1 
HETATM 12118 O  O   . HOH KA 7 .   ? -29.691 236.892 -15.032 1.00 46.70  ? 393 HOH H O   1 
HETATM 12119 O  O   . HOH KA 7 .   ? -27.278 246.963 -8.500  1.00 52.28  ? 394 HOH H O   1 
HETATM 12120 O  O   . HOH KA 7 .   ? -6.736  246.265 -7.788  1.00 47.82  ? 395 HOH H O   1 
HETATM 12121 O  O   . HOH KA 7 .   ? -18.986 242.765 -2.320  1.00 53.58  ? 396 HOH H O   1 
HETATM 12122 O  O   . HOH KA 7 .   ? -2.580  229.851 -22.442 1.00 49.96  ? 397 HOH H O   1 
HETATM 12123 O  O   . HOH KA 7 .   ? -8.804  228.238 -27.539 1.00 53.27  ? 398 HOH H O   1 
HETATM 12124 O  O   . HOH KA 7 .   ? -25.820 258.385 -15.728 1.00 49.87  ? 399 HOH H O   1 
HETATM 12125 O  O   . HOH KA 7 .   ? -3.926  248.099 -33.238 1.00 58.87  ? 400 HOH H O   1 
HETATM 12126 O  O   . HOH KA 7 .   ? -20.263 244.119 -34.680 1.00 49.03  ? 401 HOH H O   1 
HETATM 12127 O  O   . HOH KA 7 .   ? -14.256 239.693 -3.373  1.00 47.75  ? 402 HOH H O   1 
HETATM 12128 O  O   . HOH KA 7 .   ? -20.806 231.759 -28.872 1.00 45.16  ? 403 HOH H O   1 
HETATM 12129 O  O   . HOH KA 7 .   ? -15.500 257.230 -14.608 1.00 48.92  ? 404 HOH H O   1 
HETATM 12130 O  O   . HOH KA 7 .   ? -36.101 242.679 -22.332 1.00 40.06  ? 405 HOH H O   1 
HETATM 12131 O  O   . HOH KA 7 .   ? -5.899  252.385 -28.048 1.00 45.22  ? 406 HOH H O   1 
HETATM 12132 O  O   . HOH KA 7 .   ? -22.618 255.597 -34.707 1.00 51.06  ? 407 HOH H O   1 
HETATM 12133 O  O   . HOH KA 7 .   ? -4.935  225.584 -33.986 1.00 44.05  ? 408 HOH H O   1 
HETATM 12134 O  O   . HOH KA 7 .   ? -19.710 229.997 -26.827 1.00 44.55  ? 409 HOH H O   1 
HETATM 12135 O  O   . HOH KA 7 .   ? -14.398 244.162 -2.870  1.00 46.57  ? 410 HOH H O   1 
HETATM 12136 O  O   . HOH KA 7 .   ? -32.296 240.253 -13.556 1.00 49.25  ? 411 HOH H O   1 
HETATM 12137 O  O   . HOH KA 7 .   ? -9.738  227.381 -6.619  1.00 38.73  ? 412 HOH H O   1 
HETATM 12138 O  O   . HOH KA 7 .   ? -26.055 238.739 -4.582  1.00 46.35  ? 413 HOH H O   1 
HETATM 12139 O  O   . HOH KA 7 .   ? -4.156  240.218 -2.206  1.00 51.01  ? 414 HOH H O   1 
HETATM 12140 O  O   . HOH KA 7 .   ? -31.436 251.728 -33.306 1.00 51.22  ? 415 HOH H O   1 
HETATM 12141 O  O   . HOH KA 7 .   ? -21.384 251.793 -10.969 1.00 49.75  ? 416 HOH H O   1 
HETATM 12142 O  O   . HOH KA 7 .   ? -22.137 259.294 -23.043 1.00 52.25  ? 417 HOH H O   1 
HETATM 12143 O  O   . HOH KA 7 .   ? -11.518 232.140 -1.799  1.00 39.97  ? 418 HOH H O   1 
HETATM 12144 O  O   . HOH KA 7 .   ? -18.657 240.230 -2.635  1.00 46.78  ? 419 HOH H O   1 
HETATM 12145 O  O   . HOH KA 7 .   ? -28.554 254.453 -6.941  1.00 43.97  ? 420 HOH H O   1 
HETATM 12146 O  O   . HOH KA 7 .   ? -19.481 252.323 -6.023  1.00 59.37  ? 421 HOH H O   1 
HETATM 12147 O  O   . HOH KA 7 .   ? -26.549 260.010 -24.552 1.00 60.42  ? 422 HOH H O   1 
HETATM 12148 O  O   . HOH KA 7 .   ? -19.701 252.688 -37.145 1.00 50.33  ? 423 HOH H O   1 
HETATM 12149 O  O   . HOH KA 7 .   ? -33.194 251.014 -35.137 1.00 45.98  ? 424 HOH H O   1 
HETATM 12150 O  O   . HOH LA 7 .   ? 44.497  223.872 44.773  1.00 46.17  ? 301 HOH I O   1 
HETATM 12151 O  O   . HOH LA 7 .   ? 39.328  205.676 53.111  1.00 44.63  ? 302 HOH I O   1 
HETATM 12152 O  O   . HOH LA 7 .   ? 36.212  207.196 52.292  1.00 43.12  ? 303 HOH I O   1 
HETATM 12153 O  O   . HOH LA 7 .   ? 42.193  203.664 57.870  1.00 45.89  ? 304 HOH I O   1 
HETATM 12154 O  O   . HOH LA 7 .   ? 26.190  204.840 49.046  1.00 37.88  ? 305 HOH I O   1 
HETATM 12155 O  O   . HOH LA 7 .   ? 44.168  202.443 51.274  1.00 48.48  ? 306 HOH I O   1 
HETATM 12156 O  O   . HOH LA 7 .   ? 37.920  228.569 50.940  1.00 54.27  ? 307 HOH I O   1 
HETATM 12157 O  O   . HOH LA 7 .   ? 38.142  231.998 52.771  1.00 38.08  ? 308 HOH I O   1 
HETATM 12158 O  O   . HOH LA 7 .   ? 28.485  227.462 57.144  1.00 35.68  ? 309 HOH I O   1 
HETATM 12159 O  O   . HOH LA 7 .   ? 40.129  235.031 64.300  1.00 47.41  ? 310 HOH I O   1 
HETATM 12160 O  O   . HOH LA 7 .   ? 34.754  216.929 33.511  1.00 51.86  ? 311 HOH I O   1 
HETATM 12161 O  O   . HOH LA 7 .   ? 53.935  220.327 40.100  1.00 59.05  ? 312 HOH I O   1 
HETATM 12162 O  O   . HOH LA 7 .   ? 49.974  220.032 49.436  1.00 52.31  ? 313 HOH I O   1 
HETATM 12163 O  O   A HOH LA 7 .   ? 27.644  210.954 48.324  0.50 21.59  ? 314 HOH I O   1 
HETATM 12164 O  O   B HOH LA 7 .   ? 27.165  211.642 46.856  0.50 29.66  ? 314 HOH I O   1 
HETATM 12165 O  O   . HOH LA 7 .   ? 43.692  215.065 62.435  1.00 46.75  ? 315 HOH I O   1 
HETATM 12166 O  O   . HOH LA 7 .   ? 51.939  217.676 43.888  1.00 61.75  ? 316 HOH I O   1 
HETATM 12167 O  O   . HOH LA 7 .   ? 35.285  221.800 64.877  1.00 46.68  ? 317 HOH I O   1 
HETATM 12168 O  O   . HOH LA 7 .   ? 34.646  228.166 69.512  1.00 44.56  ? 318 HOH I O   1 
HETATM 12169 O  O   . HOH LA 7 .   ? 38.830  207.340 56.127  1.00 47.34  ? 319 HOH I O   1 
HETATM 12170 O  O   . HOH LA 7 .   ? 56.346  224.301 52.489  1.00 61.65  ? 320 HOH I O   1 
HETATM 12171 O  O   . HOH LA 7 .   ? 39.898  223.729 66.290  1.00 53.83  ? 321 HOH I O   1 
HETATM 12172 O  O   . HOH LA 7 .   ? 50.578  199.555 49.398  1.00 53.20  ? 322 HOH I O   1 
HETATM 12173 O  O   . HOH LA 7 .   ? 26.878  217.379 38.278  1.00 48.80  ? 323 HOH I O   1 
HETATM 12174 O  O   . HOH LA 7 .   ? 30.759  227.713 58.460  1.00 47.64  ? 324 HOH I O   1 
HETATM 12175 O  O   . HOH LA 7 .   ? 33.978  225.005 49.671  1.00 46.67  ? 325 HOH I O   1 
HETATM 12176 O  O   . HOH LA 7 .   ? 49.508  210.308 33.707  1.00 50.06  ? 326 HOH I O   1 
HETATM 12177 O  O   . HOH LA 7 .   ? 54.981  230.788 42.446  1.00 49.31  ? 327 HOH I O   1 
HETATM 12178 O  O   . HOH LA 7 .   ? 52.354  204.793 48.076  1.00 41.25  ? 328 HOH I O   1 
HETATM 12179 O  O   . HOH LA 7 .   ? 43.892  231.041 57.037  1.00 40.29  ? 329 HOH I O   1 
HETATM 12180 O  O   . HOH LA 7 .   ? 44.982  227.402 58.506  1.00 49.36  ? 330 HOH I O   1 
HETATM 12181 O  O   . HOH LA 7 .   ? 41.551  228.875 42.115  1.00 53.14  ? 331 HOH I O   1 
HETATM 12182 O  O   A HOH LA 7 .   ? 43.698  222.257 61.404  0.50 23.25  ? 332 HOH I O   1 
HETATM 12183 O  O   B HOH LA 7 .   ? 45.812  223.158 60.793  0.50 33.27  ? 332 HOH I O   1 
HETATM 12184 O  O   . HOH LA 7 .   ? 50.927  228.493 53.009  1.00 53.87  ? 333 HOH I O   1 
HETATM 12185 O  O   . HOH LA 7 .   ? 37.709  225.590 46.650  1.00 42.99  ? 334 HOH I O   1 
HETATM 12186 O  O   . HOH LA 7 .   ? 32.878  213.125 60.228  1.00 50.77  ? 335 HOH I O   1 
HETATM 12187 O  O   . HOH LA 7 .   ? 53.610  212.069 49.039  1.00 51.54  ? 336 HOH I O   1 
HETATM 12188 O  O   . HOH LA 7 .   ? 30.939  229.559 63.674  1.00 46.15  ? 337 HOH I O   1 
HETATM 12189 O  O   . HOH LA 7 .   ? 34.764  226.318 52.201  1.00 44.15  ? 338 HOH I O   1 
HETATM 12190 O  O   . HOH LA 7 .   ? 28.179  222.277 44.701  1.00 53.16  ? 339 HOH I O   1 
HETATM 12191 O  O   . HOH LA 7 .   ? 33.025  227.273 54.951  1.00 50.19  ? 340 HOH I O   1 
HETATM 12192 O  O   . HOH LA 7 .   ? 36.791  205.995 58.058  1.00 54.43  ? 341 HOH I O   1 
HETATM 12193 O  O   . HOH LA 7 .   ? 54.750  217.302 36.500  1.00 54.91  ? 342 HOH I O   1 
HETATM 12194 O  O   . HOH LA 7 .   ? 26.823  210.718 52.979  1.00 51.65  ? 343 HOH I O   1 
HETATM 12195 O  O   . HOH LA 7 .   ? 33.820  226.008 43.135  1.00 49.75  ? 344 HOH I O   1 
HETATM 12196 O  O   . HOH LA 7 .   ? 47.174  232.961 47.158  1.00 43.49  ? 345 HOH I O   1 
HETATM 12197 O  O   . HOH LA 7 .   ? 29.159  217.415 29.611  1.00 53.83  ? 346 HOH I O   1 
HETATM 12198 O  O   . HOH LA 7 .   ? 39.444  227.607 46.539  1.00 46.31  ? 347 HOH I O   1 
HETATM 12199 O  O   . HOH LA 7 .   ? 20.857  215.830 42.946  1.00 51.59  ? 348 HOH I O   1 
HETATM 12200 O  O   . HOH LA 7 .   ? 42.607  213.507 29.805  1.00 58.58  ? 349 HOH I O   1 
HETATM 12201 O  O   . HOH LA 7 .   ? 27.098  214.063 54.119  1.00 56.25  ? 350 HOH I O   1 
HETATM 12202 O  O   . HOH LA 7 .   ? 47.805  206.170 39.377  1.00 51.13  ? 351 HOH I O   1 
HETATM 12203 O  O   . HOH LA 7 .   ? 43.928  230.499 33.533  1.00 46.76  ? 352 HOH I O   1 
HETATM 12204 O  O   . HOH LA 7 .   ? 48.533  200.805 59.744  1.00 52.11  ? 353 HOH I O   1 
HETATM 12205 O  O   . HOH LA 7 .   ? 51.065  217.274 49.364  1.00 43.14  ? 354 HOH I O   1 
HETATM 12206 O  O   . HOH LA 7 .   ? 63.014  227.456 46.187  1.00 54.15  ? 355 HOH I O   1 
HETATM 12207 O  O   . HOH LA 7 .   ? 31.536  217.869 60.251  1.00 61.54  ? 356 HOH I O   1 
HETATM 12208 O  O   . HOH LA 7 .   ? 47.577  209.868 58.831  1.00 53.53  ? 357 HOH I O   1 
HETATM 12209 O  O   . HOH LA 7 .   ? 38.536  225.993 66.657  1.00 54.75  ? 358 HOH I O   1 
HETATM 12210 O  O   . HOH LA 7 .   ? 60.322  229.581 41.881  1.00 51.37  ? 359 HOH I O   1 
HETATM 12211 O  O   . HOH LA 7 .   ? 52.826  236.119 42.692  1.00 51.15  ? 360 HOH I O   1 
HETATM 12212 O  O   . HOH LA 7 .   ? 22.387  219.437 38.911  1.00 46.26  ? 361 HOH I O   1 
HETATM 12213 O  O   . HOH LA 7 .   ? 37.246  224.486 37.391  1.00 46.57  ? 362 HOH I O   1 
HETATM 12214 O  O   . HOH LA 7 .   ? 39.811  214.302 68.193  1.00 67.41  ? 363 HOH I O   1 
HETATM 12215 O  O   . HOH LA 7 .   ? 39.983  228.635 66.411  1.00 56.78  ? 364 HOH I O   1 
HETATM 12216 O  O   . HOH LA 7 .   ? 36.303  215.819 32.224  1.00 54.43  ? 365 HOH I O   1 
HETATM 12217 O  O   . HOH LA 7 .   ? 42.403  231.135 67.134  1.00 51.25  ? 366 HOH I O   1 
HETATM 12218 O  O   . HOH LA 7 .   ? 53.107  207.101 39.499  1.00 53.29  ? 367 HOH I O   1 
HETATM 12219 O  O   . HOH LA 7 .   ? 38.925  220.598 67.361  1.00 56.37  ? 368 HOH I O   1 
HETATM 12220 O  O   . HOH LA 7 .   ? 29.877  215.398 57.946  1.00 52.79  ? 369 HOH I O   1 
HETATM 12221 O  O   . HOH LA 7 .   ? 52.817  211.756 36.955  1.00 55.57  ? 370 HOH I O   1 
HETATM 12222 O  O   . HOH LA 7 .   ? 54.136  217.213 53.485  1.00 46.41  ? 371 HOH I O   1 
HETATM 12223 O  O   . HOH LA 7 .   ? 36.159  210.196 29.927  1.00 57.55  ? 372 HOH I O   1 
HETATM 12224 O  O   . HOH LA 7 .   ? 40.241  219.351 31.706  1.00 53.57  ? 373 HOH I O   1 
HETATM 12225 O  O   . HOH LA 7 .   ? 47.757  208.933 35.968  1.00 49.47  ? 374 HOH I O   1 
HETATM 12226 O  O   . HOH LA 7 .   ? 31.743  223.480 68.273  1.00 50.68  ? 375 HOH I O   1 
HETATM 12227 O  O   . HOH LA 7 .   ? 23.884  218.840 46.303  1.00 47.26  ? 376 HOH I O   1 
HETATM 12228 O  O   . HOH LA 7 .   ? 53.405  200.037 50.587  1.00 43.16  ? 377 HOH I O   1 
HETATM 12229 O  O   . HOH LA 7 .   ? 50.415  217.916 63.378  1.00 47.10  ? 378 HOH I O   1 
HETATM 12230 O  O   . HOH LA 7 .   ? 40.478  212.251 28.058  1.00 52.27  ? 379 HOH I O   1 
HETATM 12231 O  O   . HOH LA 7 .   ? 47.168  221.121 63.391  1.00 44.62  ? 380 HOH I O   1 
HETATM 12232 O  O   . HOH MA 7 .   ? 41.337  201.539 51.696  1.00 41.24  ? 301 HOH J O   1 
HETATM 12233 O  O   . HOH MA 7 .   ? 29.783  176.321 46.107  1.00 40.41  ? 302 HOH J O   1 
HETATM 12234 O  O   . HOH MA 7 .   ? 36.451  187.194 64.818  1.00 48.88  ? 303 HOH J O   1 
HETATM 12235 O  O   . HOH MA 7 .   ? 28.533  187.167 38.394  1.00 56.41  ? 304 HOH J O   1 
HETATM 12236 O  O   . HOH MA 7 .   ? 28.326  180.381 58.229  1.00 43.10  ? 305 HOH J O   1 
HETATM 12237 O  O   . HOH MA 7 .   ? 38.270  189.275 35.292  1.00 56.71  ? 306 HOH J O   1 
HETATM 12238 O  O   . HOH MA 7 .   ? 38.905  202.625 53.330  1.00 45.54  ? 307 HOH J O   1 
HETATM 12239 O  O   . HOH MA 7 .   ? 39.251  193.720 32.546  1.00 55.07  ? 308 HOH J O   1 
HETATM 12240 O  O   . HOH MA 7 .   ? 50.610  202.970 46.761  1.00 45.18  ? 309 HOH J O   1 
HETATM 12241 O  O   . HOH MA 7 .   ? 31.960  183.474 48.371  1.00 38.90  ? 310 HOH J O   1 
HETATM 12242 O  O   . HOH MA 7 .   ? 42.832  178.184 62.031  1.00 55.90  ? 311 HOH J O   1 
HETATM 12243 O  O   . HOH MA 7 .   ? 21.976  176.415 49.356  1.00 29.26  ? 312 HOH J O   1 
HETATM 12244 O  O   . HOH MA 7 .   ? 33.333  206.148 51.777  1.00 38.17  ? 313 HOH J O   1 
HETATM 12245 O  O   . HOH MA 7 .   ? 36.498  195.051 64.103  1.00 53.86  ? 314 HOH J O   1 
HETATM 12246 O  O   . HOH MA 7 .   ? 42.761  199.520 31.140  1.00 50.08  ? 315 HOH J O   1 
HETATM 12247 O  O   . HOH MA 7 .   ? 44.670  182.503 38.618  1.00 55.38  ? 316 HOH J O   1 
HETATM 12248 O  O   . HOH MA 7 .   ? 43.341  184.593 68.476  1.00 47.42  ? 317 HOH J O   1 
HETATM 12249 O  O   . HOH MA 7 .   ? 29.480  197.103 36.708  1.00 48.80  ? 318 HOH J O   1 
HETATM 12250 O  O   . HOH MA 7 .   ? 48.284  201.040 40.058  1.00 48.11  ? 319 HOH J O   1 
HETATM 12251 O  O   . HOH MA 7 .   ? 26.499  195.358 42.649  1.00 46.32  ? 320 HOH J O   1 
HETATM 12252 O  O   . HOH MA 7 .   ? 22.244  186.973 45.169  1.00 46.14  ? 321 HOH J O   1 
HETATM 12253 O  O   . HOH MA 7 .   ? 24.897  177.684 56.398  1.00 37.94  ? 322 HOH J O   1 
HETATM 12254 O  O   . HOH MA 7 .   ? 44.211  180.435 48.462  1.00 49.29  ? 323 HOH J O   1 
HETATM 12255 O  O   . HOH MA 7 .   ? 28.096  188.161 53.317  1.00 43.08  ? 324 HOH J O   1 
HETATM 12256 O  O   . HOH MA 7 .   ? 39.737  201.696 56.508  1.00 53.40  ? 325 HOH J O   1 
HETATM 12257 O  O   . HOH MA 7 .   ? 24.120  186.434 56.394  1.00 46.21  ? 326 HOH J O   1 
HETATM 12258 O  O   . HOH MA 7 .   ? 42.514  191.386 26.788  1.00 55.88  ? 327 HOH J O   1 
HETATM 12259 O  O   . HOH MA 7 .   ? 39.488  183.011 43.751  1.00 44.06  ? 328 HOH J O   1 
HETATM 12260 O  O   . HOH MA 7 .   ? 48.711  189.710 39.062  1.00 55.36  ? 329 HOH J O   1 
HETATM 12261 O  O   . HOH MA 7 .   ? 43.067  181.454 45.394  1.00 41.09  ? 330 HOH J O   1 
HETATM 12262 O  O   . HOH MA 7 .   ? 38.858  182.027 49.426  1.00 55.73  ? 331 HOH J O   1 
HETATM 12263 O  O   . HOH MA 7 .   ? 17.194  182.551 54.633  1.00 47.69  ? 332 HOH J O   1 
HETATM 12264 O  O   . HOH MA 7 .   ? 27.232  194.164 60.201  1.00 46.58  ? 333 HOH J O   1 
HETATM 12265 O  O   . HOH MA 7 .   ? 24.487  189.934 48.860  1.00 44.34  ? 334 HOH J O   1 
HETATM 12266 O  O   . HOH MA 7 .   ? 26.107  179.252 43.511  1.00 42.92  ? 335 HOH J O   1 
HETATM 12267 O  O   . HOH MA 7 .   ? 30.160  175.438 52.090  1.00 42.20  ? 336 HOH J O   1 
HETATM 12268 O  O   . HOH MA 7 .   ? 34.519  178.186 45.678  1.00 39.21  ? 337 HOH J O   1 
HETATM 12269 O  O   . HOH MA 7 .   ? 33.752  186.320 64.566  1.00 53.91  ? 338 HOH J O   1 
HETATM 12270 O  O   . HOH MA 7 .   ? 41.359  186.398 68.568  1.00 46.56  ? 339 HOH J O   1 
HETATM 12271 O  O   . HOH MA 7 .   ? 24.073  171.327 50.816  1.00 38.72  ? 340 HOH J O   1 
HETATM 12272 O  O   . HOH MA 7 .   ? 31.727  179.999 60.910  1.00 47.22  ? 341 HOH J O   1 
HETATM 12273 O  O   . HOH MA 7 .   ? 35.637  178.025 52.221  1.00 46.29  ? 342 HOH J O   1 
HETATM 12274 O  O   . HOH MA 7 .   ? 18.407  186.797 56.921  1.00 49.01  ? 343 HOH J O   1 
HETATM 12275 O  O   . HOH MA 7 .   ? 39.401  182.405 68.651  1.00 44.33  ? 344 HOH J O   1 
HETATM 12276 O  O   . HOH MA 7 .   ? 36.931  189.478 66.155  1.00 46.65  ? 345 HOH J O   1 
HETATM 12277 O  O   . HOH MA 7 .   ? 26.119  191.752 56.089  1.00 51.34  ? 346 HOH J O   1 
HETATM 12278 O  O   . HOH MA 7 .   ? 34.322  201.421 59.555  1.00 43.78  ? 347 HOH J O   1 
HETATM 12279 O  O   . HOH MA 7 .   ? 26.597  208.782 51.338  1.00 42.79  ? 348 HOH J O   1 
HETATM 12280 O  O   . HOH MA 7 .   ? 25.370  191.152 50.823  1.00 42.04  ? 349 HOH J O   1 
HETATM 12281 O  O   . HOH MA 7 .   ? 35.084  181.964 62.997  1.00 56.93  ? 350 HOH J O   1 
HETATM 12282 O  O   . HOH MA 7 .   ? 29.175  201.606 61.757  1.00 54.62  ? 351 HOH J O   1 
HETATM 12283 O  O   . HOH MA 7 .   ? 35.366  177.576 60.198  1.00 55.17  ? 352 HOH J O   1 
HETATM 12284 O  O   . HOH MA 7 .   ? 38.748  182.776 39.636  1.00 49.33  ? 353 HOH J O   1 
HETATM 12285 O  O   . HOH MA 7 .   ? 35.560  181.129 38.638  1.00 48.16  ? 354 HOH J O   1 
HETATM 12286 O  O   . HOH MA 7 .   ? 33.396  201.194 53.798  1.00 59.44  ? 355 HOH J O   1 
HETATM 12287 O  O   . HOH MA 7 .   ? 23.456  195.802 52.019  1.00 40.55  ? 356 HOH J O   1 
HETATM 12288 O  O   . HOH MA 7 .   ? 30.330  175.254 40.095  1.00 44.56  ? 357 HOH J O   1 
HETATM 12289 O  O   . HOH MA 7 .   ? 50.923  197.673 51.444  1.00 53.64  ? 358 HOH J O   1 
HETATM 12290 O  O   . HOH MA 7 .   ? 27.516  177.090 40.034  1.00 52.34  ? 359 HOH J O   1 
HETATM 12291 O  O   . HOH MA 7 .   ? 35.872  202.428 54.610  1.00 42.51  ? 360 HOH J O   1 
HETATM 12292 O  O   . HOH MA 7 .   ? 41.238  181.910 39.656  1.00 51.45  ? 361 HOH J O   1 
HETATM 12293 O  O   . HOH MA 7 .   ? 15.109  184.424 54.308  1.00 53.63  ? 362 HOH J O   1 
HETATM 12294 O  O   . HOH MA 7 .   ? 41.331  205.339 60.268  1.00 53.45  ? 363 HOH J O   1 
HETATM 12295 O  O   . HOH MA 7 .   ? 28.887  197.274 60.011  1.00 53.87  ? 364 HOH J O   1 
HETATM 12296 O  O   . HOH MA 7 .   ? 26.485  190.883 53.378  1.00 46.39  ? 365 HOH J O   1 
HETATM 12297 O  O   . HOH MA 7 .   ? 25.848  179.835 62.307  1.00 51.17  ? 366 HOH J O   1 
HETATM 12298 O  O   . HOH MA 7 .   ? 31.752  174.152 47.517  1.00 51.72  ? 367 HOH J O   1 
HETATM 12299 O  O   . HOH MA 7 .   ? 24.710  174.901 45.292  1.00 48.71  ? 368 HOH J O   1 
HETATM 12300 O  O   . HOH MA 7 .   ? 25.514  192.980 58.507  1.00 52.58  ? 369 HOH J O   1 
HETATM 12301 O  O   . HOH MA 7 .   ? 24.402  195.117 57.277  1.00 46.87  ? 370 HOH J O   1 
HETATM 12302 O  O   . HOH MA 7 .   ? 18.361  183.566 57.343  1.00 44.01  ? 371 HOH J O   1 
HETATM 12303 O  O   . HOH MA 7 .   ? 27.457  175.004 44.980  1.00 51.96  ? 372 HOH J O   1 
HETATM 12304 O  O   . HOH MA 7 .   ? 45.281  199.979 67.353  1.00 49.14  ? 373 HOH J O   1 
HETATM 12305 O  O   . HOH MA 7 .   ? 25.637  171.202 48.589  1.00 46.68  ? 374 HOH J O   1 
HETATM 12306 O  O   . HOH MA 7 .   ? 26.703  194.154 33.102  1.00 55.93  ? 375 HOH J O   1 
HETATM 12307 O  O   . HOH MA 7 .   ? 17.529  178.893 45.097  1.00 49.37  ? 376 HOH J O   1 
HETATM 12308 O  O   . HOH MA 7 .   ? 24.620  179.516 59.941  1.00 53.48  ? 377 HOH J O   1 
HETATM 12309 O  O   . HOH MA 7 .   ? 39.623  180.097 47.662  1.00 47.44  ? 378 HOH J O   1 
HETATM 12310 O  O   . HOH MA 7 .   ? 31.721  187.215 34.775  1.00 54.29  ? 379 HOH J O   1 
HETATM 12311 O  O   . HOH MA 7 .   ? 34.841  192.833 65.805  1.00 45.95  ? 380 HOH J O   1 
HETATM 12312 O  O   . HOH MA 7 .   ? 27.074  178.088 57.635  1.00 46.11  ? 381 HOH J O   1 
HETATM 12313 O  O   . HOH MA 7 .   ? 46.767  180.829 45.526  1.00 54.60  ? 382 HOH J O   1 
HETATM 12314 O  O   . HOH MA 7 .   ? 23.229  190.545 56.211  1.00 58.80  ? 383 HOH J O   1 
HETATM 12315 O  O   . HOH MA 7 .   ? 26.047  198.495 63.302  1.00 56.24  ? 384 HOH J O   1 
HETATM 12316 O  O   . HOH MA 7 .   ? 53.001  188.480 45.881  1.00 60.52  ? 385 HOH J O   1 
HETATM 12317 O  O   . HOH MA 7 .   ? 53.710  194.591 47.620  1.00 49.95  ? 386 HOH J O   1 
HETATM 12318 O  O   . HOH MA 7 .   ? 29.276  176.184 56.374  1.00 50.15  ? 387 HOH J O   1 
HETATM 12319 O  O   . HOH MA 7 .   ? 25.320  189.686 67.826  1.00 49.23  ? 388 HOH J O   1 
HETATM 12320 O  O   . HOH MA 7 .   ? 54.467  189.281 58.444  1.00 54.48  ? 389 HOH J O   1 
HETATM 12321 O  O   . HOH MA 7 .   ? 32.638  173.091 54.649  1.00 44.94  ? 390 HOH J O   1 
HETATM 12322 O  O   . HOH MA 7 .   ? 21.262  207.794 56.320  1.00 46.75  ? 391 HOH J O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   0   MET MET A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 CYS 112 111 111 CYS CYS A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   MET 1   0   0   MET MET B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   ALA 5   4   4   ALA ALA B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   CYS 7   6   6   CYS CYS B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  68  SER SER B . n 
B 1 70  ARG 70  69  69  ARG ARG B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  GLY 74  73  73  GLY GLY B . n 
B 1 75  PRO 75  74  74  PRO PRO B . n 
B 1 76  LYS 76  75  75  LYS LYS B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  GLU 78  77  77  GLU GLU B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  ASP 84  83  83  ASP ASP B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 CYS 112 111 111 CYS CYS B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 132 GLU GLU B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 THR 136 135 135 THR THR B . n 
B 1 137 LYS 137 136 136 LYS LYS B . n 
B 1 138 THR 138 137 137 THR THR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ASN 140 139 139 ASN ASN B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
C 1 1   MET 1   0   0   MET MET C . n 
C 1 2   ALA 2   1   1   ALA ALA C . n 
C 1 3   THR 3   2   2   THR THR C . n 
C 1 4   LYS 4   3   3   LYS LYS C . n 
C 1 5   ALA 5   4   4   ALA ALA C . n 
C 1 6   VAL 6   5   5   VAL VAL C . n 
C 1 7   CYS 7   6   6   CYS CYS C . n 
C 1 8   VAL 8   7   7   VAL VAL C . n 
C 1 9   LEU 9   8   8   LEU LEU C . n 
C 1 10  LYS 10  9   9   LYS LYS C . n 
C 1 11  GLY 11  10  10  GLY GLY C . n 
C 1 12  ASP 12  11  11  ASP ASP C . n 
C 1 13  GLY 13  12  12  GLY GLY C . n 
C 1 14  PRO 14  13  13  PRO PRO C . n 
C 1 15  VAL 15  14  14  VAL VAL C . n 
C 1 16  GLN 16  15  15  GLN GLN C . n 
C 1 17  GLY 17  16  16  GLY GLY C . n 
C 1 18  ILE 18  17  17  ILE ILE C . n 
C 1 19  ILE 19  18  18  ILE ILE C . n 
C 1 20  ASN 20  19  19  ASN ASN C . n 
C 1 21  PHE 21  20  20  PHE PHE C . n 
C 1 22  GLU 22  21  21  GLU GLU C . n 
C 1 23  GLN 23  22  22  GLN GLN C . n 
C 1 24  LYS 24  23  23  LYS LYS C . n 
C 1 25  GLU 25  24  24  GLU GLU C . n 
C 1 26  SER 26  25  25  SER SER C . n 
C 1 27  ASN 27  26  26  ASN ASN C . n 
C 1 28  GLY 28  27  27  GLY GLY C . n 
C 1 29  PRO 29  28  28  PRO PRO C . n 
C 1 30  VAL 30  29  29  VAL VAL C . n 
C 1 31  LYS 31  30  30  LYS LYS C . n 
C 1 32  VAL 32  31  31  VAL VAL C . n 
C 1 33  TRP 33  32  32  TRP TRP C . n 
C 1 34  GLY 34  33  33  GLY GLY C . n 
C 1 35  SER 35  34  34  SER SER C . n 
C 1 36  ILE 36  35  35  ILE ILE C . n 
C 1 37  LYS 37  36  36  LYS LYS C . n 
C 1 38  GLY 38  37  37  GLY GLY C . n 
C 1 39  LEU 39  38  38  LEU LEU C . n 
C 1 40  THR 40  39  39  THR THR C . n 
C 1 41  GLU 41  40  40  GLU GLU C . n 
C 1 42  GLY 42  41  41  GLY GLY C . n 
C 1 43  LEU 43  42  42  LEU LEU C . n 
C 1 44  HIS 44  43  43  HIS HIS C . n 
C 1 45  GLY 45  44  44  GLY GLY C . n 
C 1 46  PHE 46  45  45  PHE PHE C . n 
C 1 47  HIS 47  46  46  HIS HIS C . n 
C 1 48  VAL 48  47  47  VAL VAL C . n 
C 1 49  HIS 49  48  48  HIS HIS C . n 
C 1 50  GLU 50  49  49  GLU GLU C . n 
C 1 51  PHE 51  50  50  PHE PHE C . n 
C 1 52  GLY 52  51  51  GLY GLY C . n 
C 1 53  ASP 53  52  52  ASP ASP C . n 
C 1 54  ASN 54  53  53  ASN ASN C . n 
C 1 55  THR 55  54  54  THR THR C . n 
C 1 56  ALA 56  55  55  ALA ALA C . n 
C 1 57  GLY 57  56  56  GLY GLY C . n 
C 1 58  CYS 58  57  57  CYS CYS C . n 
C 1 59  THR 59  58  58  THR THR C . n 
C 1 60  SER 60  59  59  SER SER C . n 
C 1 61  ALA 61  60  60  ALA ALA C . n 
C 1 62  GLY 62  61  61  GLY GLY C . n 
C 1 63  PRO 63  62  62  PRO PRO C . n 
C 1 64  HIS 64  63  63  HIS HIS C . n 
C 1 65  PHE 65  64  64  PHE PHE C . n 
C 1 66  ASN 66  65  65  ASN ASN C . n 
C 1 67  PRO 67  66  66  PRO PRO C . n 
C 1 68  LEU 68  67  67  LEU LEU C . n 
C 1 69  SER 69  68  68  SER SER C . n 
C 1 70  ARG 70  69  69  ARG ARG C . n 
C 1 71  LYS 71  70  70  LYS LYS C . n 
C 1 72  HIS 72  71  71  HIS HIS C . n 
C 1 73  GLY 73  72  72  GLY GLY C . n 
C 1 74  GLY 74  73  73  GLY GLY C . n 
C 1 75  PRO 75  74  74  PRO PRO C . n 
C 1 76  LYS 76  75  75  LYS LYS C . n 
C 1 77  ASP 77  76  76  ASP ASP C . n 
C 1 78  GLU 78  77  77  GLU GLU C . n 
C 1 79  GLU 79  78  78  GLU GLU C . n 
C 1 80  ARG 80  79  79  ARG ARG C . n 
C 1 81  HIS 81  80  80  HIS HIS C . n 
C 1 82  VAL 82  81  81  VAL VAL C . n 
C 1 83  GLY 83  82  82  GLY GLY C . n 
C 1 84  ASP 84  83  83  ASP ASP C . n 
C 1 85  LEU 85  84  84  LEU LEU C . n 
C 1 86  GLY 86  85  85  GLY GLY C . n 
C 1 87  ASN 87  86  86  ASN ASN C . n 
C 1 88  VAL 88  87  87  VAL VAL C . n 
C 1 89  THR 89  88  88  THR THR C . n 
C 1 90  ALA 90  89  89  ALA ALA C . n 
C 1 91  ASP 91  90  90  ASP ASP C . n 
C 1 92  LYS 92  91  91  LYS LYS C . n 
C 1 93  ASP 93  92  92  ASP ASP C . n 
C 1 94  GLY 94  93  93  GLY GLY C . n 
C 1 95  VAL 95  94  94  VAL VAL C . n 
C 1 96  ALA 96  95  95  ALA ALA C . n 
C 1 97  ASP 97  96  96  ASP ASP C . n 
C 1 98  VAL 98  97  97  VAL VAL C . n 
C 1 99  SER 99  98  98  SER SER C . n 
C 1 100 ILE 100 99  99  ILE ILE C . n 
C 1 101 GLU 101 100 100 GLU GLU C . n 
C 1 102 ASP 102 101 101 ASP ASP C . n 
C 1 103 SER 103 102 102 SER SER C . n 
C 1 104 VAL 104 103 103 VAL VAL C . n 
C 1 105 ILE 105 104 104 ILE ILE C . n 
C 1 106 SER 106 105 105 SER SER C . n 
C 1 107 LEU 107 106 106 LEU LEU C . n 
C 1 108 SER 108 107 107 SER SER C . n 
C 1 109 GLY 109 108 108 GLY GLY C . n 
C 1 110 ASP 110 109 109 ASP ASP C . n 
C 1 111 HIS 111 110 110 HIS HIS C . n 
C 1 112 CYS 112 111 111 CYS CYS C . n 
C 1 113 ILE 113 112 112 ILE ILE C . n 
C 1 114 ILE 114 113 113 ILE ILE C . n 
C 1 115 GLY 115 114 114 GLY GLY C . n 
C 1 116 ARG 116 115 115 ARG ARG C . n 
C 1 117 THR 117 116 116 THR THR C . n 
C 1 118 LEU 118 117 117 LEU LEU C . n 
C 1 119 VAL 119 118 118 VAL VAL C . n 
C 1 120 VAL 120 119 119 VAL VAL C . n 
C 1 121 HIS 121 120 120 HIS HIS C . n 
C 1 122 GLU 122 121 121 GLU GLU C . n 
C 1 123 LYS 123 122 122 LYS LYS C . n 
C 1 124 ALA 124 123 123 ALA ALA C . n 
C 1 125 ASP 125 124 124 ASP ASP C . n 
C 1 126 ASP 126 125 125 ASP ASP C . n 
C 1 127 LEU 127 126 126 LEU LEU C . n 
C 1 128 GLY 128 127 127 GLY GLY C . n 
C 1 129 LYS 129 128 128 LYS LYS C . n 
C 1 130 GLY 130 129 129 GLY GLY C . n 
C 1 131 GLY 131 130 130 GLY GLY C . n 
C 1 132 ASN 132 131 131 ASN ASN C . n 
C 1 133 GLU 133 132 132 GLU GLU C . n 
C 1 134 GLU 134 133 133 GLU GLU C . n 
C 1 135 SER 135 134 134 SER SER C . n 
C 1 136 THR 136 135 135 THR THR C . n 
C 1 137 LYS 137 136 136 LYS LYS C . n 
C 1 138 THR 138 137 137 THR THR C . n 
C 1 139 GLY 139 138 138 GLY GLY C . n 
C 1 140 ASN 140 139 139 ASN ASN C . n 
C 1 141 ALA 141 140 140 ALA ALA C . n 
C 1 142 GLY 142 141 141 GLY GLY C . n 
C 1 143 SER 143 142 142 SER SER C . n 
C 1 144 ARG 144 143 143 ARG ARG C . n 
C 1 145 LEU 145 144 144 LEU LEU C . n 
C 1 146 ALA 146 145 145 ALA ALA C . n 
C 1 147 CYS 147 146 146 CYS CYS C . n 
C 1 148 GLY 148 147 147 GLY GLY C . n 
C 1 149 VAL 149 148 148 VAL VAL C . n 
C 1 150 ILE 150 149 149 ILE ILE C . n 
C 1 151 GLY 151 150 150 GLY GLY C . n 
C 1 152 ILE 152 151 151 ILE ILE C . n 
C 1 153 ALA 153 152 152 ALA ALA C . n 
C 1 154 GLN 154 153 153 GLN GLN C . n 
D 1 1   MET 1   0   0   MET MET D . n 
D 1 2   ALA 2   1   1   ALA ALA D . n 
D 1 3   THR 3   2   2   THR THR D . n 
D 1 4   LYS 4   3   3   LYS LYS D . n 
D 1 5   ALA 5   4   4   ALA ALA D . n 
D 1 6   VAL 6   5   5   VAL VAL D . n 
D 1 7   CYS 7   6   6   CYS CYS D . n 
D 1 8   VAL 8   7   7   VAL VAL D . n 
D 1 9   LEU 9   8   8   LEU LEU D . n 
D 1 10  LYS 10  9   9   LYS LYS D . n 
D 1 11  GLY 11  10  10  GLY GLY D . n 
D 1 12  ASP 12  11  11  ASP ASP D . n 
D 1 13  GLY 13  12  12  GLY GLY D . n 
D 1 14  PRO 14  13  13  PRO PRO D . n 
D 1 15  VAL 15  14  14  VAL VAL D . n 
D 1 16  GLN 16  15  15  GLN GLN D . n 
D 1 17  GLY 17  16  16  GLY GLY D . n 
D 1 18  ILE 18  17  17  ILE ILE D . n 
D 1 19  ILE 19  18  18  ILE ILE D . n 
D 1 20  ASN 20  19  19  ASN ASN D . n 
D 1 21  PHE 21  20  20  PHE PHE D . n 
D 1 22  GLU 22  21  21  GLU GLU D . n 
D 1 23  GLN 23  22  22  GLN GLN D . n 
D 1 24  LYS 24  23  23  LYS LYS D . n 
D 1 25  GLU 25  24  24  GLU GLU D . n 
D 1 26  SER 26  25  25  SER SER D . n 
D 1 27  ASN 27  26  26  ASN ASN D . n 
D 1 28  GLY 28  27  27  GLY GLY D . n 
D 1 29  PRO 29  28  28  PRO PRO D . n 
D 1 30  VAL 30  29  29  VAL VAL D . n 
D 1 31  LYS 31  30  30  LYS LYS D . n 
D 1 32  VAL 32  31  31  VAL VAL D . n 
D 1 33  TRP 33  32  32  TRP TRP D . n 
D 1 34  GLY 34  33  33  GLY GLY D . n 
D 1 35  SER 35  34  34  SER SER D . n 
D 1 36  ILE 36  35  35  ILE ILE D . n 
D 1 37  LYS 37  36  36  LYS LYS D . n 
D 1 38  GLY 38  37  37  GLY GLY D . n 
D 1 39  LEU 39  38  38  LEU LEU D . n 
D 1 40  THR 40  39  39  THR THR D . n 
D 1 41  GLU 41  40  40  GLU GLU D . n 
D 1 42  GLY 42  41  41  GLY GLY D . n 
D 1 43  LEU 43  42  42  LEU LEU D . n 
D 1 44  HIS 44  43  43  HIS HIS D . n 
D 1 45  GLY 45  44  44  GLY GLY D . n 
D 1 46  PHE 46  45  45  PHE PHE D . n 
D 1 47  HIS 47  46  46  HIS HIS D . n 
D 1 48  VAL 48  47  47  VAL VAL D . n 
D 1 49  HIS 49  48  48  HIS HIS D . n 
D 1 50  GLU 50  49  49  GLU GLU D . n 
D 1 51  PHE 51  50  50  PHE PHE D . n 
D 1 52  GLY 52  51  51  GLY GLY D . n 
D 1 53  ASP 53  52  52  ASP ASP D . n 
D 1 54  ASN 54  53  53  ASN ASN D . n 
D 1 55  THR 55  54  54  THR THR D . n 
D 1 56  ALA 56  55  55  ALA ALA D . n 
D 1 57  GLY 57  56  56  GLY GLY D . n 
D 1 58  CYS 58  57  57  CYS CYS D . n 
D 1 59  THR 59  58  58  THR THR D . n 
D 1 60  SER 60  59  59  SER SER D . n 
D 1 61  ALA 61  60  60  ALA ALA D . n 
D 1 62  GLY 62  61  61  GLY GLY D . n 
D 1 63  PRO 63  62  62  PRO PRO D . n 
D 1 64  HIS 64  63  63  HIS HIS D . n 
D 1 65  PHE 65  64  64  PHE PHE D . n 
D 1 66  ASN 66  65  65  ASN ASN D . n 
D 1 67  PRO 67  66  66  PRO PRO D . n 
D 1 68  LEU 68  67  67  LEU LEU D . n 
D 1 69  SER 69  68  68  SER SER D . n 
D 1 70  ARG 70  69  69  ARG ARG D . n 
D 1 71  LYS 71  70  70  LYS LYS D . n 
D 1 72  HIS 72  71  71  HIS HIS D . n 
D 1 73  GLY 73  72  72  GLY GLY D . n 
D 1 74  GLY 74  73  73  GLY GLY D . n 
D 1 75  PRO 75  74  74  PRO PRO D . n 
D 1 76  LYS 76  75  75  LYS LYS D . n 
D 1 77  ASP 77  76  76  ASP ASP D . n 
D 1 78  GLU 78  77  77  GLU GLU D . n 
D 1 79  GLU 79  78  78  GLU GLU D . n 
D 1 80  ARG 80  79  79  ARG ARG D . n 
D 1 81  HIS 81  80  80  HIS HIS D . n 
D 1 82  VAL 82  81  81  VAL VAL D . n 
D 1 83  GLY 83  82  82  GLY GLY D . n 
D 1 84  ASP 84  83  83  ASP ASP D . n 
D 1 85  LEU 85  84  84  LEU LEU D . n 
D 1 86  GLY 86  85  85  GLY GLY D . n 
D 1 87  ASN 87  86  86  ASN ASN D . n 
D 1 88  VAL 88  87  87  VAL VAL D . n 
D 1 89  THR 89  88  88  THR THR D . n 
D 1 90  ALA 90  89  89  ALA ALA D . n 
D 1 91  ASP 91  90  90  ASP ASP D . n 
D 1 92  LYS 92  91  91  LYS LYS D . n 
D 1 93  ASP 93  92  92  ASP ASP D . n 
D 1 94  GLY 94  93  93  GLY GLY D . n 
D 1 95  VAL 95  94  94  VAL VAL D . n 
D 1 96  ALA 96  95  95  ALA ALA D . n 
D 1 97  ASP 97  96  96  ASP ASP D . n 
D 1 98  VAL 98  97  97  VAL VAL D . n 
D 1 99  SER 99  98  98  SER SER D . n 
D 1 100 ILE 100 99  99  ILE ILE D . n 
D 1 101 GLU 101 100 100 GLU GLU D . n 
D 1 102 ASP 102 101 101 ASP ASP D . n 
D 1 103 SER 103 102 102 SER SER D . n 
D 1 104 VAL 104 103 103 VAL VAL D . n 
D 1 105 ILE 105 104 104 ILE ILE D . n 
D 1 106 SER 106 105 105 SER SER D . n 
D 1 107 LEU 107 106 106 LEU LEU D . n 
D 1 108 SER 108 107 107 SER SER D . n 
D 1 109 GLY 109 108 108 GLY GLY D . n 
D 1 110 ASP 110 109 109 ASP ASP D . n 
D 1 111 HIS 111 110 110 HIS HIS D . n 
D 1 112 CYS 112 111 111 CYS CYS D . n 
D 1 113 ILE 113 112 112 ILE ILE D . n 
D 1 114 ILE 114 113 113 ILE ILE D . n 
D 1 115 GLY 115 114 114 GLY GLY D . n 
D 1 116 ARG 116 115 115 ARG ARG D . n 
D 1 117 THR 117 116 116 THR THR D . n 
D 1 118 LEU 118 117 117 LEU LEU D . n 
D 1 119 VAL 119 118 118 VAL VAL D . n 
D 1 120 VAL 120 119 119 VAL VAL D . n 
D 1 121 HIS 121 120 120 HIS HIS D . n 
D 1 122 GLU 122 121 121 GLU GLU D . n 
D 1 123 LYS 123 122 122 LYS LYS D . n 
D 1 124 ALA 124 123 123 ALA ALA D . n 
D 1 125 ASP 125 124 124 ASP ASP D . n 
D 1 126 ASP 126 125 125 ASP ASP D . n 
D 1 127 LEU 127 126 126 LEU LEU D . n 
D 1 128 GLY 128 127 127 GLY GLY D . n 
D 1 129 LYS 129 128 128 LYS LYS D . n 
D 1 130 GLY 130 129 129 GLY GLY D . n 
D 1 131 GLY 131 130 130 GLY GLY D . n 
D 1 132 ASN 132 131 131 ASN ASN D . n 
D 1 133 GLU 133 132 132 GLU GLU D . n 
D 1 134 GLU 134 133 133 GLU GLU D . n 
D 1 135 SER 135 134 134 SER SER D . n 
D 1 136 THR 136 135 135 THR THR D . n 
D 1 137 LYS 137 136 136 LYS LYS D . n 
D 1 138 THR 138 137 137 THR THR D . n 
D 1 139 GLY 139 138 138 GLY GLY D . n 
D 1 140 ASN 140 139 139 ASN ASN D . n 
D 1 141 ALA 141 140 140 ALA ALA D . n 
D 1 142 GLY 142 141 141 GLY GLY D . n 
D 1 143 SER 143 142 142 SER SER D . n 
D 1 144 ARG 144 143 143 ARG ARG D . n 
D 1 145 LEU 145 144 144 LEU LEU D . n 
D 1 146 ALA 146 145 145 ALA ALA D . n 
D 1 147 CYS 147 146 146 CYS CYS D . n 
D 1 148 GLY 148 147 147 GLY GLY D . n 
D 1 149 VAL 149 148 148 VAL VAL D . n 
D 1 150 ILE 150 149 149 ILE ILE D . n 
D 1 151 GLY 151 150 150 GLY GLY D . n 
D 1 152 ILE 152 151 151 ILE ILE D . n 
D 1 153 ALA 153 152 152 ALA ALA D . n 
D 1 154 GLN 154 153 153 GLN GLN D . n 
E 1 1   MET 1   0   0   MET ALA E . n 
E 1 2   ALA 2   1   1   ALA ALA E . n 
E 1 3   THR 3   2   2   THR THR E . n 
E 1 4   LYS 4   3   3   LYS LYS E . n 
E 1 5   ALA 5   4   4   ALA ALA E . n 
E 1 6   VAL 6   5   5   VAL VAL E . n 
E 1 7   CYS 7   6   6   CYS CYS E . n 
E 1 8   VAL 8   7   7   VAL VAL E . n 
E 1 9   LEU 9   8   8   LEU LEU E . n 
E 1 10  LYS 10  9   9   LYS LYS E . n 
E 1 11  GLY 11  10  10  GLY GLY E . n 
E 1 12  ASP 12  11  11  ASP ASP E . n 
E 1 13  GLY 13  12  12  GLY GLY E . n 
E 1 14  PRO 14  13  13  PRO PRO E . n 
E 1 15  VAL 15  14  14  VAL VAL E . n 
E 1 16  GLN 16  15  15  GLN GLN E . n 
E 1 17  GLY 17  16  16  GLY GLY E . n 
E 1 18  ILE 18  17  17  ILE ILE E . n 
E 1 19  ILE 19  18  18  ILE ILE E . n 
E 1 20  ASN 20  19  19  ASN ASN E . n 
E 1 21  PHE 21  20  20  PHE PHE E . n 
E 1 22  GLU 22  21  21  GLU GLU E . n 
E 1 23  GLN 23  22  22  GLN GLN E . n 
E 1 24  LYS 24  23  23  LYS LYS E . n 
E 1 25  GLU 25  24  24  GLU GLU E . n 
E 1 26  SER 26  25  25  SER SER E . n 
E 1 27  ASN 27  26  26  ASN ASN E . n 
E 1 28  GLY 28  27  27  GLY GLY E . n 
E 1 29  PRO 29  28  28  PRO PRO E . n 
E 1 30  VAL 30  29  29  VAL VAL E . n 
E 1 31  LYS 31  30  30  LYS LYS E . n 
E 1 32  VAL 32  31  31  VAL VAL E . n 
E 1 33  TRP 33  32  32  TRP TRP E . n 
E 1 34  GLY 34  33  33  GLY GLY E . n 
E 1 35  SER 35  34  34  SER SER E . n 
E 1 36  ILE 36  35  35  ILE ILE E . n 
E 1 37  LYS 37  36  36  LYS LYS E . n 
E 1 38  GLY 38  37  37  GLY GLY E . n 
E 1 39  LEU 39  38  38  LEU LEU E . n 
E 1 40  THR 40  39  39  THR THR E . n 
E 1 41  GLU 41  40  40  GLU GLU E . n 
E 1 42  GLY 42  41  41  GLY GLY E . n 
E 1 43  LEU 43  42  42  LEU LEU E . n 
E 1 44  HIS 44  43  43  HIS HIS E . n 
E 1 45  GLY 45  44  44  GLY GLY E . n 
E 1 46  PHE 46  45  45  PHE PHE E . n 
E 1 47  HIS 47  46  46  HIS HIS E . n 
E 1 48  VAL 48  47  47  VAL VAL E . n 
E 1 49  HIS 49  48  48  HIS HIS E . n 
E 1 50  GLU 50  49  49  GLU GLU E . n 
E 1 51  PHE 51  50  50  PHE PHE E . n 
E 1 52  GLY 52  51  51  GLY GLY E . n 
E 1 53  ASP 53  52  52  ASP ASP E . n 
E 1 54  ASN 54  53  53  ASN ASN E . n 
E 1 55  THR 55  54  54  THR THR E . n 
E 1 56  ALA 56  55  55  ALA ALA E . n 
E 1 57  GLY 57  56  56  GLY GLY E . n 
E 1 58  CYS 58  57  57  CYS CYS E . n 
E 1 59  THR 59  58  58  THR THR E . n 
E 1 60  SER 60  59  59  SER SER E . n 
E 1 61  ALA 61  60  60  ALA ALA E . n 
E 1 62  GLY 62  61  61  GLY GLY E . n 
E 1 63  PRO 63  62  62  PRO PRO E . n 
E 1 64  HIS 64  63  63  HIS HIS E . n 
E 1 65  PHE 65  64  64  PHE PHE E . n 
E 1 66  ASN 66  65  65  ASN ASN E . n 
E 1 67  PRO 67  66  66  PRO PRO E . n 
E 1 68  LEU 68  67  67  LEU LEU E . n 
E 1 69  SER 69  68  68  SER SER E . n 
E 1 70  ARG 70  69  69  ARG ARG E . n 
E 1 71  LYS 71  70  70  LYS LYS E . n 
E 1 72  HIS 72  71  71  HIS HIS E . n 
E 1 73  GLY 73  72  72  GLY GLY E . n 
E 1 74  GLY 74  73  73  GLY GLY E . n 
E 1 75  PRO 75  74  74  PRO PRO E . n 
E 1 76  LYS 76  75  75  LYS LYS E . n 
E 1 77  ASP 77  76  76  ASP ASP E . n 
E 1 78  GLU 78  77  77  GLU ALA E . n 
E 1 79  GLU 79  78  78  GLU GLU E . n 
E 1 80  ARG 80  79  79  ARG ARG E . n 
E 1 81  HIS 81  80  80  HIS HIS E . n 
E 1 82  VAL 82  81  81  VAL VAL E . n 
E 1 83  GLY 83  82  82  GLY GLY E . n 
E 1 84  ASP 84  83  83  ASP ASP E . n 
E 1 85  LEU 85  84  84  LEU LEU E . n 
E 1 86  GLY 86  85  85  GLY GLY E . n 
E 1 87  ASN 87  86  86  ASN ASN E . n 
E 1 88  VAL 88  87  87  VAL VAL E . n 
E 1 89  THR 89  88  88  THR THR E . n 
E 1 90  ALA 90  89  89  ALA ALA E . n 
E 1 91  ASP 91  90  90  ASP ASP E . n 
E 1 92  LYS 92  91  91  LYS LYS E . n 
E 1 93  ASP 93  92  92  ASP ASP E . n 
E 1 94  GLY 94  93  93  GLY GLY E . n 
E 1 95  VAL 95  94  94  VAL VAL E . n 
E 1 96  ALA 96  95  95  ALA ALA E . n 
E 1 97  ASP 97  96  96  ASP ASP E . n 
E 1 98  VAL 98  97  97  VAL VAL E . n 
E 1 99  SER 99  98  98  SER SER E . n 
E 1 100 ILE 100 99  99  ILE ILE E . n 
E 1 101 GLU 101 100 100 GLU GLU E . n 
E 1 102 ASP 102 101 101 ASP ASP E . n 
E 1 103 SER 103 102 102 SER SER E . n 
E 1 104 VAL 104 103 103 VAL VAL E . n 
E 1 105 ILE 105 104 104 ILE ILE E . n 
E 1 106 SER 106 105 105 SER SER E . n 
E 1 107 LEU 107 106 106 LEU LEU E . n 
E 1 108 SER 108 107 107 SER SER E . n 
E 1 109 GLY 109 108 108 GLY GLY E . n 
E 1 110 ASP 110 109 109 ASP ASP E . n 
E 1 111 HIS 111 110 110 HIS HIS E . n 
E 1 112 CYS 112 111 111 CYS CYS E . n 
E 1 113 ILE 113 112 112 ILE ILE E . n 
E 1 114 ILE 114 113 113 ILE ILE E . n 
E 1 115 GLY 115 114 114 GLY GLY E . n 
E 1 116 ARG 116 115 115 ARG ARG E . n 
E 1 117 THR 117 116 116 THR THR E . n 
E 1 118 LEU 118 117 117 LEU LEU E . n 
E 1 119 VAL 119 118 118 VAL VAL E . n 
E 1 120 VAL 120 119 119 VAL VAL E . n 
E 1 121 HIS 121 120 120 HIS HIS E . n 
E 1 122 GLU 122 121 121 GLU GLU E . n 
E 1 123 LYS 123 122 122 LYS LYS E . n 
E 1 124 ALA 124 123 123 ALA ALA E . n 
E 1 125 ASP 125 124 124 ASP ASP E . n 
E 1 126 ASP 126 125 125 ASP ASP E . n 
E 1 127 LEU 127 126 126 LEU LEU E . n 
E 1 128 GLY 128 127 127 GLY GLY E . n 
E 1 129 LYS 129 128 128 LYS LYS E . n 
E 1 130 GLY 130 129 129 GLY GLY E . n 
E 1 131 GLY 131 130 130 GLY GLY E . n 
E 1 132 ASN 132 131 131 ASN ASN E . n 
E 1 133 GLU 133 132 132 GLU GLU E . n 
E 1 134 GLU 134 133 133 GLU GLU E . n 
E 1 135 SER 135 134 134 SER SER E . n 
E 1 136 THR 136 135 135 THR THR E . n 
E 1 137 LYS 137 136 136 LYS LYS E . n 
E 1 138 THR 138 137 137 THR THR E . n 
E 1 139 GLY 139 138 138 GLY GLY E . n 
E 1 140 ASN 140 139 139 ASN ASN E . n 
E 1 141 ALA 141 140 140 ALA ALA E . n 
E 1 142 GLY 142 141 141 GLY GLY E . n 
E 1 143 SER 143 142 142 SER SER E . n 
E 1 144 ARG 144 143 143 ARG ARG E . n 
E 1 145 LEU 145 144 144 LEU LEU E . n 
E 1 146 ALA 146 145 145 ALA ALA E . n 
E 1 147 CYS 147 146 146 CYS CYS E . n 
E 1 148 GLY 148 147 147 GLY GLY E . n 
E 1 149 VAL 149 148 148 VAL VAL E . n 
E 1 150 ILE 150 149 149 ILE ILE E . n 
E 1 151 GLY 151 150 150 GLY GLY E . n 
E 1 152 ILE 152 151 151 ILE ILE E . n 
E 1 153 ALA 153 152 152 ALA ALA E . n 
E 1 154 GLN 154 153 153 GLN GLN E . n 
F 1 1   MET 1   0   0   MET MET F . n 
F 1 2   ALA 2   1   1   ALA ALA F . n 
F 1 3   THR 3   2   2   THR THR F . n 
F 1 4   LYS 4   3   3   LYS LYS F . n 
F 1 5   ALA 5   4   4   ALA ALA F . n 
F 1 6   VAL 6   5   5   VAL VAL F . n 
F 1 7   CYS 7   6   6   CYS CYS F . n 
F 1 8   VAL 8   7   7   VAL VAL F . n 
F 1 9   LEU 9   8   8   LEU LEU F . n 
F 1 10  LYS 10  9   9   LYS LYS F . n 
F 1 11  GLY 11  10  10  GLY GLY F . n 
F 1 12  ASP 12  11  11  ASP ASP F . n 
F 1 13  GLY 13  12  12  GLY GLY F . n 
F 1 14  PRO 14  13  13  PRO PRO F . n 
F 1 15  VAL 15  14  14  VAL VAL F . n 
F 1 16  GLN 16  15  15  GLN GLN F . n 
F 1 17  GLY 17  16  16  GLY GLY F . n 
F 1 18  ILE 18  17  17  ILE ILE F . n 
F 1 19  ILE 19  18  18  ILE ILE F . n 
F 1 20  ASN 20  19  19  ASN ASN F . n 
F 1 21  PHE 21  20  20  PHE PHE F . n 
F 1 22  GLU 22  21  21  GLU GLU F . n 
F 1 23  GLN 23  22  22  GLN GLN F . n 
F 1 24  LYS 24  23  23  LYS LYS F . n 
F 1 25  GLU 25  24  24  GLU GLU F . n 
F 1 26  SER 26  25  25  SER SER F . n 
F 1 27  ASN 27  26  26  ASN ASN F . n 
F 1 28  GLY 28  27  27  GLY GLY F . n 
F 1 29  PRO 29  28  28  PRO PRO F . n 
F 1 30  VAL 30  29  29  VAL VAL F . n 
F 1 31  LYS 31  30  30  LYS LYS F . n 
F 1 32  VAL 32  31  31  VAL VAL F . n 
F 1 33  TRP 33  32  32  TRP TRP F . n 
F 1 34  GLY 34  33  33  GLY GLY F . n 
F 1 35  SER 35  34  34  SER SER F . n 
F 1 36  ILE 36  35  35  ILE ILE F . n 
F 1 37  LYS 37  36  36  LYS LYS F . n 
F 1 38  GLY 38  37  37  GLY GLY F . n 
F 1 39  LEU 39  38  38  LEU LEU F . n 
F 1 40  THR 40  39  39  THR THR F . n 
F 1 41  GLU 41  40  40  GLU GLU F . n 
F 1 42  GLY 42  41  41  GLY GLY F . n 
F 1 43  LEU 43  42  42  LEU LEU F . n 
F 1 44  HIS 44  43  43  HIS HIS F . n 
F 1 45  GLY 45  44  44  GLY GLY F . n 
F 1 46  PHE 46  45  45  PHE PHE F . n 
F 1 47  HIS 47  46  46  HIS HIS F . n 
F 1 48  VAL 48  47  47  VAL VAL F . n 
F 1 49  HIS 49  48  48  HIS HIS F . n 
F 1 50  GLU 50  49  49  GLU GLU F . n 
F 1 51  PHE 51  50  50  PHE PHE F . n 
F 1 52  GLY 52  51  51  GLY GLY F . n 
F 1 53  ASP 53  52  52  ASP ASP F . n 
F 1 54  ASN 54  53  53  ASN ASN F . n 
F 1 55  THR 55  54  54  THR THR F . n 
F 1 56  ALA 56  55  55  ALA ALA F . n 
F 1 57  GLY 57  56  56  GLY GLY F . n 
F 1 58  CYS 58  57  57  CYS CYS F . n 
F 1 59  THR 59  58  58  THR THR F . n 
F 1 60  SER 60  59  59  SER SER F . n 
F 1 61  ALA 61  60  60  ALA ALA F . n 
F 1 62  GLY 62  61  61  GLY GLY F . n 
F 1 63  PRO 63  62  62  PRO PRO F . n 
F 1 64  HIS 64  63  63  HIS HIS F . n 
F 1 65  PHE 65  64  64  PHE PHE F . n 
F 1 66  ASN 66  65  65  ASN ASN F . n 
F 1 67  PRO 67  66  66  PRO PRO F . n 
F 1 68  LEU 68  67  67  LEU LEU F . n 
F 1 69  SER 69  68  68  SER SER F . n 
F 1 70  ARG 70  69  69  ARG ARG F . n 
F 1 71  LYS 71  70  70  LYS LYS F . n 
F 1 72  HIS 72  71  71  HIS HIS F . n 
F 1 73  GLY 73  72  72  GLY GLY F . n 
F 1 74  GLY 74  73  73  GLY GLY F . n 
F 1 75  PRO 75  74  74  PRO PRO F . n 
F 1 76  LYS 76  75  75  LYS LYS F . n 
F 1 77  ASP 77  76  76  ASP ASP F . n 
F 1 78  GLU 78  77  77  GLU GLU F . n 
F 1 79  GLU 79  78  78  GLU GLU F . n 
F 1 80  ARG 80  79  79  ARG ARG F . n 
F 1 81  HIS 81  80  80  HIS HIS F . n 
F 1 82  VAL 82  81  81  VAL VAL F . n 
F 1 83  GLY 83  82  82  GLY GLY F . n 
F 1 84  ASP 84  83  83  ASP ASP F . n 
F 1 85  LEU 85  84  84  LEU LEU F . n 
F 1 86  GLY 86  85  85  GLY GLY F . n 
F 1 87  ASN 87  86  86  ASN ASN F . n 
F 1 88  VAL 88  87  87  VAL VAL F . n 
F 1 89  THR 89  88  88  THR THR F . n 
F 1 90  ALA 90  89  89  ALA ALA F . n 
F 1 91  ASP 91  90  90  ASP ASP F . n 
F 1 92  LYS 92  91  91  LYS LYS F . n 
F 1 93  ASP 93  92  92  ASP ASP F . n 
F 1 94  GLY 94  93  93  GLY GLY F . n 
F 1 95  VAL 95  94  94  VAL VAL F . n 
F 1 96  ALA 96  95  95  ALA ALA F . n 
F 1 97  ASP 97  96  96  ASP ASP F . n 
F 1 98  VAL 98  97  97  VAL VAL F . n 
F 1 99  SER 99  98  98  SER SER F . n 
F 1 100 ILE 100 99  99  ILE ILE F . n 
F 1 101 GLU 101 100 100 GLU GLU F . n 
F 1 102 ASP 102 101 101 ASP ASP F . n 
F 1 103 SER 103 102 102 SER SER F . n 
F 1 104 VAL 104 103 103 VAL VAL F . n 
F 1 105 ILE 105 104 104 ILE ILE F . n 
F 1 106 SER 106 105 105 SER SER F . n 
F 1 107 LEU 107 106 106 LEU LEU F . n 
F 1 108 SER 108 107 107 SER SER F . n 
F 1 109 GLY 109 108 108 GLY GLY F . n 
F 1 110 ASP 110 109 109 ASP ASP F . n 
F 1 111 HIS 111 110 110 HIS HIS F . n 
F 1 112 CYS 112 111 111 CYS CYS F . n 
F 1 113 ILE 113 112 112 ILE ILE F . n 
F 1 114 ILE 114 113 113 ILE ILE F . n 
F 1 115 GLY 115 114 114 GLY GLY F . n 
F 1 116 ARG 116 115 115 ARG ARG F . n 
F 1 117 THR 117 116 116 THR THR F . n 
F 1 118 LEU 118 117 117 LEU LEU F . n 
F 1 119 VAL 119 118 118 VAL VAL F . n 
F 1 120 VAL 120 119 119 VAL VAL F . n 
F 1 121 HIS 121 120 120 HIS HIS F . n 
F 1 122 GLU 122 121 121 GLU GLU F . n 
F 1 123 LYS 123 122 122 LYS LYS F . n 
F 1 124 ALA 124 123 123 ALA ALA F . n 
F 1 125 ASP 125 124 124 ASP ASP F . n 
F 1 126 ASP 126 125 125 ASP ASP F . n 
F 1 127 LEU 127 126 126 LEU LEU F . n 
F 1 128 GLY 128 127 127 GLY GLY F . n 
F 1 129 LYS 129 128 128 LYS LYS F . n 
F 1 130 GLY 130 129 129 GLY GLY F . n 
F 1 131 GLY 131 130 130 GLY GLY F . n 
F 1 132 ASN 132 131 131 ASN ASN F . n 
F 1 133 GLU 133 132 132 GLU GLU F . n 
F 1 134 GLU 134 133 133 GLU GLU F . n 
F 1 135 SER 135 134 134 SER SER F . n 
F 1 136 THR 136 135 135 THR THR F . n 
F 1 137 LYS 137 136 136 LYS LYS F . n 
F 1 138 THR 138 137 137 THR THR F . n 
F 1 139 GLY 139 138 138 GLY GLY F . n 
F 1 140 ASN 140 139 139 ASN ASN F . n 
F 1 141 ALA 141 140 140 ALA ALA F . n 
F 1 142 GLY 142 141 141 GLY GLY F . n 
F 1 143 SER 143 142 142 SER SER F . n 
F 1 144 ARG 144 143 143 ARG ARG F . n 
F 1 145 LEU 145 144 144 LEU LEU F . n 
F 1 146 ALA 146 145 145 ALA ALA F . n 
F 1 147 CYS 147 146 146 CYS CYS F . n 
F 1 148 GLY 148 147 147 GLY GLY F . n 
F 1 149 VAL 149 148 148 VAL VAL F . n 
F 1 150 ILE 150 149 149 ILE ILE F . n 
F 1 151 GLY 151 150 150 GLY GLY F . n 
F 1 152 ILE 152 151 151 ILE ILE F . n 
F 1 153 ALA 153 152 152 ALA ALA F . n 
F 1 154 GLN 154 153 153 GLN GLN F . n 
G 1 1   MET 1   0   ?   ?   ?   G . n 
G 1 2   ALA 2   1   1   ALA ALA G . n 
G 1 3   THR 3   2   2   THR THR G . n 
G 1 4   LYS 4   3   3   LYS LYS G . n 
G 1 5   ALA 5   4   4   ALA ALA G . n 
G 1 6   VAL 6   5   5   VAL VAL G . n 
G 1 7   CYS 7   6   6   CYS CYS G . n 
G 1 8   VAL 8   7   7   VAL VAL G . n 
G 1 9   LEU 9   8   8   LEU LEU G . n 
G 1 10  LYS 10  9   9   LYS LYS G . n 
G 1 11  GLY 11  10  10  GLY GLY G . n 
G 1 12  ASP 12  11  11  ASP ASP G . n 
G 1 13  GLY 13  12  12  GLY GLY G . n 
G 1 14  PRO 14  13  13  PRO PRO G . n 
G 1 15  VAL 15  14  14  VAL VAL G . n 
G 1 16  GLN 16  15  15  GLN GLN G . n 
G 1 17  GLY 17  16  16  GLY GLY G . n 
G 1 18  ILE 18  17  17  ILE ILE G . n 
G 1 19  ILE 19  18  18  ILE ILE G . n 
G 1 20  ASN 20  19  19  ASN ASN G . n 
G 1 21  PHE 21  20  20  PHE PHE G . n 
G 1 22  GLU 22  21  21  GLU GLU G . n 
G 1 23  GLN 23  22  22  GLN GLN G . n 
G 1 24  LYS 24  23  23  LYS LYS G . n 
G 1 25  GLU 25  24  24  GLU GLU G . n 
G 1 26  SER 26  25  25  SER SER G . n 
G 1 27  ASN 27  26  26  ASN ASN G . n 
G 1 28  GLY 28  27  27  GLY GLY G . n 
G 1 29  PRO 29  28  28  PRO PRO G . n 
G 1 30  VAL 30  29  29  VAL VAL G . n 
G 1 31  LYS 31  30  30  LYS LYS G . n 
G 1 32  VAL 32  31  31  VAL VAL G . n 
G 1 33  TRP 33  32  32  TRP TRP G . n 
G 1 34  GLY 34  33  33  GLY GLY G . n 
G 1 35  SER 35  34  34  SER SER G . n 
G 1 36  ILE 36  35  35  ILE ILE G . n 
G 1 37  LYS 37  36  36  LYS LYS G . n 
G 1 38  GLY 38  37  37  GLY GLY G . n 
G 1 39  LEU 39  38  38  LEU LEU G . n 
G 1 40  THR 40  39  39  THR THR G . n 
G 1 41  GLU 41  40  40  GLU GLU G . n 
G 1 42  GLY 42  41  41  GLY GLY G . n 
G 1 43  LEU 43  42  42  LEU LEU G . n 
G 1 44  HIS 44  43  43  HIS HIS G . n 
G 1 45  GLY 45  44  44  GLY GLY G . n 
G 1 46  PHE 46  45  45  PHE PHE G . n 
G 1 47  HIS 47  46  46  HIS HIS G . n 
G 1 48  VAL 48  47  47  VAL VAL G . n 
G 1 49  HIS 49  48  48  HIS HIS G . n 
G 1 50  GLU 50  49  49  GLU GLU G . n 
G 1 51  PHE 51  50  50  PHE PHE G . n 
G 1 52  GLY 52  51  51  GLY GLY G . n 
G 1 53  ASP 53  52  52  ASP ASP G . n 
G 1 54  ASN 54  53  53  ASN ASN G . n 
G 1 55  THR 55  54  54  THR THR G . n 
G 1 56  ALA 56  55  55  ALA ALA G . n 
G 1 57  GLY 57  56  56  GLY GLY G . n 
G 1 58  CYS 58  57  57  CYS CYS G . n 
G 1 59  THR 59  58  58  THR THR G . n 
G 1 60  SER 60  59  59  SER SER G . n 
G 1 61  ALA 61  60  60  ALA ALA G . n 
G 1 62  GLY 62  61  61  GLY GLY G . n 
G 1 63  PRO 63  62  62  PRO PRO G . n 
G 1 64  HIS 64  63  63  HIS HIS G . n 
G 1 65  PHE 65  64  64  PHE PHE G . n 
G 1 66  ASN 66  65  65  ASN ASN G . n 
G 1 67  PRO 67  66  66  PRO PRO G . n 
G 1 68  LEU 68  67  ?   ?   ?   G . n 
G 1 69  SER 69  68  ?   ?   ?   G . n 
G 1 70  ARG 70  69  ?   ?   ?   G . n 
G 1 71  LYS 71  70  ?   ?   ?   G . n 
G 1 72  HIS 72  71  ?   ?   ?   G . n 
G 1 73  GLY 73  72  ?   ?   ?   G . n 
G 1 74  GLY 74  73  ?   ?   ?   G . n 
G 1 75  PRO 75  74  ?   ?   ?   G . n 
G 1 76  LYS 76  75  ?   ?   ?   G . n 
G 1 77  ASP 77  76  ?   ?   ?   G . n 
G 1 78  GLU 78  77  ?   ?   ?   G . n 
G 1 79  GLU 79  78  ?   ?   ?   G . n 
G 1 80  ARG 80  79  79  ARG ARG G . n 
G 1 81  HIS 81  80  80  HIS HIS G . n 
G 1 82  VAL 82  81  81  VAL VAL G . n 
G 1 83  GLY 83  82  82  GLY GLY G . n 
G 1 84  ASP 84  83  83  ASP ASP G . n 
G 1 85  LEU 85  84  84  LEU LEU G . n 
G 1 86  GLY 86  85  85  GLY GLY G . n 
G 1 87  ASN 87  86  86  ASN ASN G . n 
G 1 88  VAL 88  87  87  VAL VAL G . n 
G 1 89  THR 89  88  88  THR THR G . n 
G 1 90  ALA 90  89  89  ALA ALA G . n 
G 1 91  ASP 91  90  90  ASP ASP G . n 
G 1 92  LYS 92  91  91  LYS LYS G . n 
G 1 93  ASP 93  92  92  ASP ASP G . n 
G 1 94  GLY 94  93  93  GLY GLY G . n 
G 1 95  VAL 95  94  94  VAL VAL G . n 
G 1 96  ALA 96  95  95  ALA ALA G . n 
G 1 97  ASP 97  96  96  ASP ASP G . n 
G 1 98  VAL 98  97  97  VAL VAL G . n 
G 1 99  SER 99  98  98  SER SER G . n 
G 1 100 ILE 100 99  99  ILE ILE G . n 
G 1 101 GLU 101 100 100 GLU GLU G . n 
G 1 102 ASP 102 101 101 ASP ASP G . n 
G 1 103 SER 103 102 102 SER SER G . n 
G 1 104 VAL 104 103 103 VAL VAL G . n 
G 1 105 ILE 105 104 104 ILE ILE G . n 
G 1 106 SER 106 105 105 SER SER G . n 
G 1 107 LEU 107 106 106 LEU LEU G . n 
G 1 108 SER 108 107 107 SER SER G . n 
G 1 109 GLY 109 108 108 GLY GLY G . n 
G 1 110 ASP 110 109 109 ASP ASP G . n 
G 1 111 HIS 111 110 110 HIS HIS G . n 
G 1 112 CYS 112 111 111 CYS CYS G . n 
G 1 113 ILE 113 112 112 ILE ILE G . n 
G 1 114 ILE 114 113 113 ILE ILE G . n 
G 1 115 GLY 115 114 114 GLY GLY G . n 
G 1 116 ARG 116 115 115 ARG ARG G . n 
G 1 117 THR 117 116 116 THR THR G . n 
G 1 118 LEU 118 117 117 LEU LEU G . n 
G 1 119 VAL 119 118 118 VAL VAL G . n 
G 1 120 VAL 120 119 119 VAL VAL G . n 
G 1 121 HIS 121 120 120 HIS HIS G . n 
G 1 122 GLU 122 121 121 GLU GLU G . n 
G 1 123 LYS 123 122 122 LYS LYS G . n 
G 1 124 ALA 124 123 123 ALA ALA G . n 
G 1 125 ASP 125 124 124 ASP ASP G . n 
G 1 126 ASP 126 125 125 ASP ASP G . n 
G 1 127 LEU 127 126 126 LEU LEU G . n 
G 1 128 GLY 128 127 ?   ?   ?   G . n 
G 1 129 LYS 129 128 ?   ?   ?   G . n 
G 1 130 GLY 130 129 ?   ?   ?   G . n 
G 1 131 GLY 131 130 ?   ?   ?   G . n 
G 1 132 ASN 132 131 ?   ?   ?   G . n 
G 1 133 GLU 133 132 ?   ?   ?   G . n 
G 1 134 GLU 134 133 ?   ?   ?   G . n 
G 1 135 SER 135 134 ?   ?   ?   G . n 
G 1 136 THR 136 135 ?   ?   ?   G . n 
G 1 137 LYS 137 136 ?   ?   ?   G . n 
G 1 138 THR 138 137 ?   ?   ?   G . n 
G 1 139 GLY 139 138 ?   ?   ?   G . n 
G 1 140 ASN 140 139 ?   ?   ?   G . n 
G 1 141 ALA 141 140 ?   ?   ?   G . n 
G 1 142 GLY 142 141 141 GLY GLY G . n 
G 1 143 SER 143 142 142 SER SER G . n 
G 1 144 ARG 144 143 143 ARG ARG G . n 
G 1 145 LEU 145 144 144 LEU LEU G . n 
G 1 146 ALA 146 145 145 ALA ALA G . n 
G 1 147 CYS 147 146 146 CYS CYS G . n 
G 1 148 GLY 148 147 147 GLY GLY G . n 
G 1 149 VAL 149 148 148 VAL VAL G . n 
G 1 150 ILE 150 149 149 ILE ILE G . n 
G 1 151 GLY 151 150 150 GLY GLY G . n 
G 1 152 ILE 152 151 151 ILE ILE G . n 
G 1 153 ALA 153 152 152 ALA ALA G . n 
G 1 154 GLN 154 153 153 GLN GLN G . n 
H 1 1   MET 1   0   ?   ?   ?   H . n 
H 1 2   ALA 2   1   1   ALA ALA H . n 
H 1 3   THR 3   2   2   THR THR H . n 
H 1 4   LYS 4   3   3   LYS LYS H . n 
H 1 5   ALA 5   4   4   ALA ALA H . n 
H 1 6   VAL 6   5   5   VAL VAL H . n 
H 1 7   CYS 7   6   6   CYS CYS H . n 
H 1 8   VAL 8   7   7   VAL VAL H . n 
H 1 9   LEU 9   8   8   LEU LEU H . n 
H 1 10  LYS 10  9   9   LYS LYS H . n 
H 1 11  GLY 11  10  10  GLY GLY H . n 
H 1 12  ASP 12  11  11  ASP ASP H . n 
H 1 13  GLY 13  12  12  GLY GLY H . n 
H 1 14  PRO 14  13  13  PRO PRO H . n 
H 1 15  VAL 15  14  14  VAL VAL H . n 
H 1 16  GLN 16  15  15  GLN GLN H . n 
H 1 17  GLY 17  16  16  GLY GLY H . n 
H 1 18  ILE 18  17  17  ILE ILE H . n 
H 1 19  ILE 19  18  18  ILE ILE H . n 
H 1 20  ASN 20  19  19  ASN ASN H . n 
H 1 21  PHE 21  20  20  PHE PHE H . n 
H 1 22  GLU 22  21  21  GLU GLU H . n 
H 1 23  GLN 23  22  22  GLN GLN H . n 
H 1 24  LYS 24  23  23  LYS LYS H . n 
H 1 25  GLU 25  24  24  GLU GLU H . n 
H 1 26  SER 26  25  25  SER SER H . n 
H 1 27  ASN 27  26  26  ASN ASN H . n 
H 1 28  GLY 28  27  27  GLY GLY H . n 
H 1 29  PRO 29  28  28  PRO PRO H . n 
H 1 30  VAL 30  29  29  VAL VAL H . n 
H 1 31  LYS 31  30  30  LYS ALA H . n 
H 1 32  VAL 32  31  31  VAL VAL H . n 
H 1 33  TRP 33  32  32  TRP TRP H . n 
H 1 34  GLY 34  33  33  GLY GLY H . n 
H 1 35  SER 35  34  34  SER SER H . n 
H 1 36  ILE 36  35  35  ILE ILE H . n 
H 1 37  LYS 37  36  36  LYS LYS H . n 
H 1 38  GLY 38  37  37  GLY GLY H . n 
H 1 39  LEU 39  38  38  LEU LEU H . n 
H 1 40  THR 40  39  39  THR THR H . n 
H 1 41  GLU 41  40  40  GLU GLU H . n 
H 1 42  GLY 42  41  41  GLY GLY H . n 
H 1 43  LEU 43  42  42  LEU LEU H . n 
H 1 44  HIS 44  43  43  HIS HIS H . n 
H 1 45  GLY 45  44  44  GLY GLY H . n 
H 1 46  PHE 46  45  45  PHE PHE H . n 
H 1 47  HIS 47  46  46  HIS HIS H . n 
H 1 48  VAL 48  47  47  VAL VAL H . n 
H 1 49  HIS 49  48  48  HIS HIS H . n 
H 1 50  GLU 50  49  49  GLU GLU H . n 
H 1 51  PHE 51  50  50  PHE PHE H . n 
H 1 52  GLY 52  51  51  GLY GLY H . n 
H 1 53  ASP 53  52  52  ASP ASP H . n 
H 1 54  ASN 54  53  53  ASN ASN H . n 
H 1 55  THR 55  54  54  THR THR H . n 
H 1 56  ALA 56  55  55  ALA ALA H . n 
H 1 57  GLY 57  56  56  GLY GLY H . n 
H 1 58  CYS 58  57  57  CYS CYS H . n 
H 1 59  THR 59  58  58  THR THR H . n 
H 1 60  SER 60  59  59  SER SER H . n 
H 1 61  ALA 61  60  60  ALA ALA H . n 
H 1 62  GLY 62  61  61  GLY GLY H . n 
H 1 63  PRO 63  62  62  PRO PRO H . n 
H 1 64  HIS 64  63  63  HIS HIS H . n 
H 1 65  PHE 65  64  64  PHE PHE H . n 
H 1 66  ASN 66  65  65  ASN ASN H . n 
H 1 67  PRO 67  66  66  PRO PRO H . n 
H 1 68  LEU 68  67  67  LEU LEU H . n 
H 1 69  SER 69  68  68  SER SER H . n 
H 1 70  ARG 70  69  69  ARG ARG H . n 
H 1 71  LYS 71  70  70  LYS LYS H . n 
H 1 72  HIS 72  71  71  HIS HIS H . n 
H 1 73  GLY 73  72  72  GLY GLY H . n 
H 1 74  GLY 74  73  73  GLY GLY H . n 
H 1 75  PRO 75  74  74  PRO PRO H . n 
H 1 76  LYS 76  75  75  LYS LYS H . n 
H 1 77  ASP 77  76  76  ASP ASP H . n 
H 1 78  GLU 78  77  77  GLU GLU H . n 
H 1 79  GLU 79  78  78  GLU GLU H . n 
H 1 80  ARG 80  79  79  ARG ARG H . n 
H 1 81  HIS 81  80  80  HIS HIS H . n 
H 1 82  VAL 82  81  81  VAL VAL H . n 
H 1 83  GLY 83  82  82  GLY GLY H . n 
H 1 84  ASP 84  83  83  ASP ASP H . n 
H 1 85  LEU 85  84  84  LEU LEU H . n 
H 1 86  GLY 86  85  85  GLY GLY H . n 
H 1 87  ASN 87  86  86  ASN ASN H . n 
H 1 88  VAL 88  87  87  VAL VAL H . n 
H 1 89  THR 89  88  88  THR THR H . n 
H 1 90  ALA 90  89  89  ALA ALA H . n 
H 1 91  ASP 91  90  90  ASP ASP H . n 
H 1 92  LYS 92  91  91  LYS LYS H . n 
H 1 93  ASP 93  92  92  ASP ASP H . n 
H 1 94  GLY 94  93  93  GLY GLY H . n 
H 1 95  VAL 95  94  94  VAL VAL H . n 
H 1 96  ALA 96  95  95  ALA ALA H . n 
H 1 97  ASP 97  96  96  ASP ASP H . n 
H 1 98  VAL 98  97  97  VAL VAL H . n 
H 1 99  SER 99  98  98  SER SER H . n 
H 1 100 ILE 100 99  99  ILE ILE H . n 
H 1 101 GLU 101 100 100 GLU GLU H . n 
H 1 102 ASP 102 101 101 ASP ASP H . n 
H 1 103 SER 103 102 102 SER SER H . n 
H 1 104 VAL 104 103 103 VAL VAL H . n 
H 1 105 ILE 105 104 104 ILE ILE H . n 
H 1 106 SER 106 105 105 SER SER H . n 
H 1 107 LEU 107 106 106 LEU LEU H . n 
H 1 108 SER 108 107 107 SER SER H . n 
H 1 109 GLY 109 108 108 GLY GLY H . n 
H 1 110 ASP 110 109 109 ASP ASP H . n 
H 1 111 HIS 111 110 110 HIS HIS H . n 
H 1 112 CYS 112 111 111 CYS CYS H . n 
H 1 113 ILE 113 112 112 ILE ILE H . n 
H 1 114 ILE 114 113 113 ILE ILE H . n 
H 1 115 GLY 115 114 114 GLY GLY H . n 
H 1 116 ARG 116 115 115 ARG ARG H . n 
H 1 117 THR 117 116 116 THR THR H . n 
H 1 118 LEU 118 117 117 LEU LEU H . n 
H 1 119 VAL 119 118 118 VAL VAL H . n 
H 1 120 VAL 120 119 119 VAL VAL H . n 
H 1 121 HIS 121 120 120 HIS HIS H . n 
H 1 122 GLU 122 121 121 GLU GLU H . n 
H 1 123 LYS 123 122 122 LYS LYS H . n 
H 1 124 ALA 124 123 123 ALA ALA H . n 
H 1 125 ASP 125 124 124 ASP ASP H . n 
H 1 126 ASP 126 125 125 ASP ASP H . n 
H 1 127 LEU 127 126 126 LEU LEU H . n 
H 1 128 GLY 128 127 127 GLY GLY H . n 
H 1 129 LYS 129 128 128 LYS LYS H . n 
H 1 130 GLY 130 129 129 GLY GLY H . n 
H 1 131 GLY 131 130 130 GLY GLY H . n 
H 1 132 ASN 132 131 131 ASN ASN H . n 
H 1 133 GLU 133 132 132 GLU GLU H . n 
H 1 134 GLU 134 133 133 GLU GLU H . n 
H 1 135 SER 135 134 134 SER SER H . n 
H 1 136 THR 136 135 135 THR THR H . n 
H 1 137 LYS 137 136 136 LYS LYS H . n 
H 1 138 THR 138 137 137 THR THR H . n 
H 1 139 GLY 139 138 138 GLY GLY H . n 
H 1 140 ASN 140 139 139 ASN ASN H . n 
H 1 141 ALA 141 140 140 ALA ALA H . n 
H 1 142 GLY 142 141 141 GLY GLY H . n 
H 1 143 SER 143 142 142 SER SER H . n 
H 1 144 ARG 144 143 143 ARG ARG H . n 
H 1 145 LEU 145 144 144 LEU LEU H . n 
H 1 146 ALA 146 145 145 ALA ALA H . n 
H 1 147 CYS 147 146 146 CYS CYS H . n 
H 1 148 GLY 148 147 147 GLY GLY H . n 
H 1 149 VAL 149 148 148 VAL VAL H . n 
H 1 150 ILE 150 149 149 ILE ILE H . n 
H 1 151 GLY 151 150 150 GLY GLY H . n 
H 1 152 ILE 152 151 151 ILE ILE H . n 
H 1 153 ALA 153 152 152 ALA ALA H . n 
H 1 154 GLN 154 153 153 GLN GLN H . n 
I 1 1   MET 1   0   0   MET MET I . n 
I 1 2   ALA 2   1   1   ALA ALA I . n 
I 1 3   THR 3   2   2   THR THR I . n 
I 1 4   LYS 4   3   3   LYS LYS I . n 
I 1 5   ALA 5   4   4   ALA ALA I . n 
I 1 6   VAL 6   5   5   VAL VAL I . n 
I 1 7   CYS 7   6   6   CYS CYS I . n 
I 1 8   VAL 8   7   7   VAL VAL I . n 
I 1 9   LEU 9   8   8   LEU LEU I . n 
I 1 10  LYS 10  9   9   LYS LYS I . n 
I 1 11  GLY 11  10  10  GLY GLY I . n 
I 1 12  ASP 12  11  11  ASP ASP I . n 
I 1 13  GLY 13  12  12  GLY GLY I . n 
I 1 14  PRO 14  13  13  PRO PRO I . n 
I 1 15  VAL 15  14  14  VAL VAL I . n 
I 1 16  GLN 16  15  15  GLN GLN I . n 
I 1 17  GLY 17  16  16  GLY GLY I . n 
I 1 18  ILE 18  17  17  ILE ILE I . n 
I 1 19  ILE 19  18  18  ILE ILE I . n 
I 1 20  ASN 20  19  19  ASN ASN I . n 
I 1 21  PHE 21  20  20  PHE PHE I . n 
I 1 22  GLU 22  21  21  GLU GLU I . n 
I 1 23  GLN 23  22  22  GLN GLN I . n 
I 1 24  LYS 24  23  23  LYS LYS I . n 
I 1 25  GLU 25  24  24  GLU GLU I . n 
I 1 26  SER 26  25  25  SER SER I . n 
I 1 27  ASN 27  26  26  ASN ASN I . n 
I 1 28  GLY 28  27  27  GLY GLY I . n 
I 1 29  PRO 29  28  28  PRO PRO I . n 
I 1 30  VAL 30  29  29  VAL VAL I . n 
I 1 31  LYS 31  30  30  LYS LYS I . n 
I 1 32  VAL 32  31  31  VAL VAL I . n 
I 1 33  TRP 33  32  32  TRP TRP I . n 
I 1 34  GLY 34  33  33  GLY GLY I . n 
I 1 35  SER 35  34  34  SER SER I . n 
I 1 36  ILE 36  35  35  ILE ILE I . n 
I 1 37  LYS 37  36  36  LYS LYS I . n 
I 1 38  GLY 38  37  37  GLY GLY I . n 
I 1 39  LEU 39  38  38  LEU LEU I . n 
I 1 40  THR 40  39  39  THR THR I . n 
I 1 41  GLU 41  40  40  GLU GLU I . n 
I 1 42  GLY 42  41  41  GLY GLY I . n 
I 1 43  LEU 43  42  42  LEU LEU I . n 
I 1 44  HIS 44  43  43  HIS HIS I . n 
I 1 45  GLY 45  44  44  GLY GLY I . n 
I 1 46  PHE 46  45  45  PHE PHE I . n 
I 1 47  HIS 47  46  46  HIS HIS I . n 
I 1 48  VAL 48  47  47  VAL VAL I . n 
I 1 49  HIS 49  48  48  HIS HIS I . n 
I 1 50  GLU 50  49  49  GLU GLU I . n 
I 1 51  PHE 51  50  50  PHE PHE I . n 
I 1 52  GLY 52  51  51  GLY GLY I . n 
I 1 53  ASP 53  52  52  ASP ASP I . n 
I 1 54  ASN 54  53  53  ASN ASN I . n 
I 1 55  THR 55  54  54  THR THR I . n 
I 1 56  ALA 56  55  55  ALA ALA I . n 
I 1 57  GLY 57  56  56  GLY GLY I . n 
I 1 58  CYS 58  57  57  CYS CYS I . n 
I 1 59  THR 59  58  58  THR THR I . n 
I 1 60  SER 60  59  59  SER SER I . n 
I 1 61  ALA 61  60  60  ALA ALA I . n 
I 1 62  GLY 62  61  61  GLY GLY I . n 
I 1 63  PRO 63  62  62  PRO PRO I . n 
I 1 64  HIS 64  63  63  HIS HIS I . n 
I 1 65  PHE 65  64  64  PHE PHE I . n 
I 1 66  ASN 66  65  65  ASN ASN I . n 
I 1 67  PRO 67  66  66  PRO PRO I . n 
I 1 68  LEU 68  67  67  LEU LEU I . n 
I 1 69  SER 69  68  68  SER SER I . n 
I 1 70  ARG 70  69  69  ARG ARG I . n 
I 1 71  LYS 71  70  70  LYS LYS I . n 
I 1 72  HIS 72  71  71  HIS HIS I . n 
I 1 73  GLY 73  72  72  GLY GLY I . n 
I 1 74  GLY 74  73  73  GLY GLY I . n 
I 1 75  PRO 75  74  74  PRO PRO I . n 
I 1 76  LYS 76  75  75  LYS LYS I . n 
I 1 77  ASP 77  76  76  ASP ASP I . n 
I 1 78  GLU 78  77  77  GLU GLU I . n 
I 1 79  GLU 79  78  78  GLU GLU I . n 
I 1 80  ARG 80  79  79  ARG ARG I . n 
I 1 81  HIS 81  80  80  HIS HIS I . n 
I 1 82  VAL 82  81  81  VAL VAL I . n 
I 1 83  GLY 83  82  82  GLY GLY I . n 
I 1 84  ASP 84  83  83  ASP ASP I . n 
I 1 85  LEU 85  84  84  LEU LEU I . n 
I 1 86  GLY 86  85  85  GLY GLY I . n 
I 1 87  ASN 87  86  86  ASN ASN I . n 
I 1 88  VAL 88  87  87  VAL VAL I . n 
I 1 89  THR 89  88  88  THR THR I . n 
I 1 90  ALA 90  89  89  ALA ALA I . n 
I 1 91  ASP 91  90  90  ASP ASP I . n 
I 1 92  LYS 92  91  91  LYS LYS I . n 
I 1 93  ASP 93  92  92  ASP ASP I . n 
I 1 94  GLY 94  93  93  GLY GLY I . n 
I 1 95  VAL 95  94  94  VAL VAL I . n 
I 1 96  ALA 96  95  95  ALA ALA I . n 
I 1 97  ASP 97  96  96  ASP ASP I . n 
I 1 98  VAL 98  97  97  VAL VAL I . n 
I 1 99  SER 99  98  98  SER SER I . n 
I 1 100 ILE 100 99  99  ILE ILE I . n 
I 1 101 GLU 101 100 100 GLU GLU I . n 
I 1 102 ASP 102 101 101 ASP ASP I . n 
I 1 103 SER 103 102 102 SER SER I . n 
I 1 104 VAL 104 103 103 VAL VAL I . n 
I 1 105 ILE 105 104 104 ILE ILE I . n 
I 1 106 SER 106 105 105 SER SER I . n 
I 1 107 LEU 107 106 106 LEU LEU I . n 
I 1 108 SER 108 107 107 SER SER I . n 
I 1 109 GLY 109 108 108 GLY GLY I . n 
I 1 110 ASP 110 109 109 ASP ASP I . n 
I 1 111 HIS 111 110 110 HIS HIS I . n 
I 1 112 CYS 112 111 111 CYS CYS I . n 
I 1 113 ILE 113 112 112 ILE ILE I . n 
I 1 114 ILE 114 113 113 ILE ILE I . n 
I 1 115 GLY 115 114 114 GLY GLY I . n 
I 1 116 ARG 116 115 115 ARG ARG I . n 
I 1 117 THR 117 116 116 THR THR I . n 
I 1 118 LEU 118 117 117 LEU LEU I . n 
I 1 119 VAL 119 118 118 VAL VAL I . n 
I 1 120 VAL 120 119 119 VAL VAL I . n 
I 1 121 HIS 121 120 120 HIS HIS I . n 
I 1 122 GLU 122 121 121 GLU GLU I . n 
I 1 123 LYS 123 122 122 LYS LYS I . n 
I 1 124 ALA 124 123 123 ALA ALA I . n 
I 1 125 ASP 125 124 124 ASP ASP I . n 
I 1 126 ASP 126 125 125 ASP ASP I . n 
I 1 127 LEU 127 126 126 LEU LEU I . n 
I 1 128 GLY 128 127 127 GLY GLY I . n 
I 1 129 LYS 129 128 128 LYS LYS I . n 
I 1 130 GLY 130 129 129 GLY GLY I . n 
I 1 131 GLY 131 130 130 GLY GLY I . n 
I 1 132 ASN 132 131 131 ASN ASN I . n 
I 1 133 GLU 133 132 132 GLU GLU I . n 
I 1 134 GLU 134 133 133 GLU GLU I . n 
I 1 135 SER 135 134 134 SER SER I . n 
I 1 136 THR 136 135 135 THR THR I . n 
I 1 137 LYS 137 136 136 LYS LYS I . n 
I 1 138 THR 138 137 137 THR THR I . n 
I 1 139 GLY 139 138 138 GLY GLY I . n 
I 1 140 ASN 140 139 139 ASN ASN I . n 
I 1 141 ALA 141 140 140 ALA ALA I . n 
I 1 142 GLY 142 141 141 GLY GLY I . n 
I 1 143 SER 143 142 142 SER SER I . n 
I 1 144 ARG 144 143 143 ARG ARG I . n 
I 1 145 LEU 145 144 144 LEU LEU I . n 
I 1 146 ALA 146 145 145 ALA ALA I . n 
I 1 147 CYS 147 146 146 CYS CYS I . n 
I 1 148 GLY 148 147 147 GLY GLY I . n 
I 1 149 VAL 149 148 148 VAL VAL I . n 
I 1 150 ILE 150 149 149 ILE ILE I . n 
I 1 151 GLY 151 150 150 GLY GLY I . n 
I 1 152 ILE 152 151 151 ILE ILE I . n 
I 1 153 ALA 153 152 152 ALA ALA I . n 
I 1 154 GLN 154 153 153 GLN GLN I . n 
J 1 1   MET 1   0   0   MET MET J . n 
J 1 2   ALA 2   1   1   ALA ALA J . n 
J 1 3   THR 3   2   2   THR THR J . n 
J 1 4   LYS 4   3   3   LYS LYS J . n 
J 1 5   ALA 5   4   4   ALA ALA J . n 
J 1 6   VAL 6   5   5   VAL VAL J . n 
J 1 7   CYS 7   6   6   CYS CYS J . n 
J 1 8   VAL 8   7   7   VAL VAL J . n 
J 1 9   LEU 9   8   8   LEU LEU J . n 
J 1 10  LYS 10  9   9   LYS LYS J . n 
J 1 11  GLY 11  10  10  GLY GLY J . n 
J 1 12  ASP 12  11  11  ASP ASP J . n 
J 1 13  GLY 13  12  12  GLY GLY J . n 
J 1 14  PRO 14  13  13  PRO PRO J . n 
J 1 15  VAL 15  14  14  VAL VAL J . n 
J 1 16  GLN 16  15  15  GLN GLN J . n 
J 1 17  GLY 17  16  16  GLY GLY J . n 
J 1 18  ILE 18  17  17  ILE ILE J . n 
J 1 19  ILE 19  18  18  ILE ILE J . n 
J 1 20  ASN 20  19  19  ASN ASN J . n 
J 1 21  PHE 21  20  20  PHE PHE J . n 
J 1 22  GLU 22  21  21  GLU GLU J . n 
J 1 23  GLN 23  22  22  GLN GLN J . n 
J 1 24  LYS 24  23  23  LYS LYS J . n 
J 1 25  GLU 25  24  24  GLU GLU J . n 
J 1 26  SER 26  25  25  SER SER J . n 
J 1 27  ASN 27  26  26  ASN ASN J . n 
J 1 28  GLY 28  27  27  GLY GLY J . n 
J 1 29  PRO 29  28  28  PRO PRO J . n 
J 1 30  VAL 30  29  29  VAL VAL J . n 
J 1 31  LYS 31  30  30  LYS LYS J . n 
J 1 32  VAL 32  31  31  VAL VAL J . n 
J 1 33  TRP 33  32  32  TRP TRP J . n 
J 1 34  GLY 34  33  33  GLY GLY J . n 
J 1 35  SER 35  34  34  SER SER J . n 
J 1 36  ILE 36  35  35  ILE ILE J . n 
J 1 37  LYS 37  36  36  LYS LYS J . n 
J 1 38  GLY 38  37  37  GLY GLY J . n 
J 1 39  LEU 39  38  38  LEU LEU J . n 
J 1 40  THR 40  39  39  THR THR J . n 
J 1 41  GLU 41  40  40  GLU GLU J . n 
J 1 42  GLY 42  41  41  GLY GLY J . n 
J 1 43  LEU 43  42  42  LEU LEU J . n 
J 1 44  HIS 44  43  43  HIS HIS J . n 
J 1 45  GLY 45  44  44  GLY GLY J . n 
J 1 46  PHE 46  45  45  PHE PHE J . n 
J 1 47  HIS 47  46  46  HIS HIS J . n 
J 1 48  VAL 48  47  47  VAL VAL J . n 
J 1 49  HIS 49  48  48  HIS HIS J . n 
J 1 50  GLU 50  49  49  GLU GLU J . n 
J 1 51  PHE 51  50  50  PHE PHE J . n 
J 1 52  GLY 52  51  51  GLY GLY J . n 
J 1 53  ASP 53  52  52  ASP ASP J . n 
J 1 54  ASN 54  53  53  ASN ASN J . n 
J 1 55  THR 55  54  54  THR THR J . n 
J 1 56  ALA 56  55  55  ALA ALA J . n 
J 1 57  GLY 57  56  56  GLY GLY J . n 
J 1 58  CYS 58  57  57  CYS CYS J . n 
J 1 59  THR 59  58  58  THR THR J . n 
J 1 60  SER 60  59  59  SER SER J . n 
J 1 61  ALA 61  60  60  ALA ALA J . n 
J 1 62  GLY 62  61  61  GLY GLY J . n 
J 1 63  PRO 63  62  62  PRO PRO J . n 
J 1 64  HIS 64  63  63  HIS HIS J . n 
J 1 65  PHE 65  64  64  PHE PHE J . n 
J 1 66  ASN 66  65  65  ASN ASN J . n 
J 1 67  PRO 67  66  66  PRO PRO J . n 
J 1 68  LEU 68  67  67  LEU LEU J . n 
J 1 69  SER 69  68  68  SER SER J . n 
J 1 70  ARG 70  69  69  ARG ARG J . n 
J 1 71  LYS 71  70  70  LYS LYS J . n 
J 1 72  HIS 72  71  71  HIS HIS J . n 
J 1 73  GLY 73  72  72  GLY GLY J . n 
J 1 74  GLY 74  73  73  GLY GLY J . n 
J 1 75  PRO 75  74  74  PRO PRO J . n 
J 1 76  LYS 76  75  75  LYS LYS J . n 
J 1 77  ASP 77  76  76  ASP ASP J . n 
J 1 78  GLU 78  77  77  GLU GLU J . n 
J 1 79  GLU 79  78  78  GLU GLU J . n 
J 1 80  ARG 80  79  79  ARG ARG J . n 
J 1 81  HIS 81  80  80  HIS HIS J . n 
J 1 82  VAL 82  81  81  VAL VAL J . n 
J 1 83  GLY 83  82  82  GLY GLY J . n 
J 1 84  ASP 84  83  83  ASP ASP J . n 
J 1 85  LEU 85  84  84  LEU LEU J . n 
J 1 86  GLY 86  85  85  GLY GLY J . n 
J 1 87  ASN 87  86  86  ASN ASN J . n 
J 1 88  VAL 88  87  87  VAL VAL J . n 
J 1 89  THR 89  88  88  THR THR J . n 
J 1 90  ALA 90  89  89  ALA ALA J . n 
J 1 91  ASP 91  90  90  ASP ASP J . n 
J 1 92  LYS 92  91  91  LYS LYS J . n 
J 1 93  ASP 93  92  92  ASP ASP J . n 
J 1 94  GLY 94  93  93  GLY GLY J . n 
J 1 95  VAL 95  94  94  VAL VAL J . n 
J 1 96  ALA 96  95  95  ALA ALA J . n 
J 1 97  ASP 97  96  96  ASP ASP J . n 
J 1 98  VAL 98  97  97  VAL VAL J . n 
J 1 99  SER 99  98  98  SER SER J . n 
J 1 100 ILE 100 99  99  ILE ILE J . n 
J 1 101 GLU 101 100 100 GLU GLU J . n 
J 1 102 ASP 102 101 101 ASP ASP J . n 
J 1 103 SER 103 102 102 SER SER J . n 
J 1 104 VAL 104 103 103 VAL VAL J . n 
J 1 105 ILE 105 104 104 ILE ILE J . n 
J 1 106 SER 106 105 105 SER SER J . n 
J 1 107 LEU 107 106 106 LEU LEU J . n 
J 1 108 SER 108 107 107 SER SER J . n 
J 1 109 GLY 109 108 108 GLY GLY J . n 
J 1 110 ASP 110 109 109 ASP ASP J . n 
J 1 111 HIS 111 110 110 HIS HIS J . n 
J 1 112 CYS 112 111 111 CYS CYS J . n 
J 1 113 ILE 113 112 112 ILE ILE J . n 
J 1 114 ILE 114 113 113 ILE ILE J . n 
J 1 115 GLY 115 114 114 GLY GLY J . n 
J 1 116 ARG 116 115 115 ARG ARG J . n 
J 1 117 THR 117 116 116 THR THR J . n 
J 1 118 LEU 118 117 117 LEU LEU J . n 
J 1 119 VAL 119 118 118 VAL VAL J . n 
J 1 120 VAL 120 119 119 VAL VAL J . n 
J 1 121 HIS 121 120 120 HIS HIS J . n 
J 1 122 GLU 122 121 121 GLU GLU J . n 
J 1 123 LYS 123 122 122 LYS LYS J . n 
J 1 124 ALA 124 123 123 ALA ALA J . n 
J 1 125 ASP 125 124 124 ASP ASP J . n 
J 1 126 ASP 126 125 125 ASP ASP J . n 
J 1 127 LEU 127 126 126 LEU LEU J . n 
J 1 128 GLY 128 127 127 GLY GLY J . n 
J 1 129 LYS 129 128 128 LYS LYS J . n 
J 1 130 GLY 130 129 129 GLY GLY J . n 
J 1 131 GLY 131 130 130 GLY GLY J . n 
J 1 132 ASN 132 131 131 ASN ASN J . n 
J 1 133 GLU 133 132 132 GLU GLU J . n 
J 1 134 GLU 134 133 133 GLU GLU J . n 
J 1 135 SER 135 134 134 SER SER J . n 
J 1 136 THR 136 135 135 THR THR J . n 
J 1 137 LYS 137 136 136 LYS LYS J . n 
J 1 138 THR 138 137 137 THR THR J . n 
J 1 139 GLY 139 138 138 GLY GLY J . n 
J 1 140 ASN 140 139 139 ASN ASN J . n 
J 1 141 ALA 141 140 140 ALA ALA J . n 
J 1 142 GLY 142 141 141 GLY GLY J . n 
J 1 143 SER 143 142 142 SER SER J . n 
J 1 144 ARG 144 143 143 ARG ARG J . n 
J 1 145 LEU 145 144 144 LEU LEU J . n 
J 1 146 ALA 146 145 145 ALA ALA J . n 
J 1 147 CYS 147 146 146 CYS CYS J . n 
J 1 148 GLY 148 147 147 GLY GLY J . n 
J 1 149 VAL 149 148 148 VAL VAL J . n 
J 1 150 ILE 150 149 149 ILE ILE J . n 
J 1 151 GLY 151 150 150 GLY GLY J . n 
J 1 152 ILE 152 151 151 ILE ILE J . n 
J 1 153 ALA 153 152 152 ALA ALA J . n 
J 1 154 GLN 154 153 153 GLN GLN J . 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 
K  2 ZN  1   201 201 ZN  ZN  A . 
L  3 DMS 1   202 202 DMS DMS A . 
M  4 GOL 1   203 203 GOL GOL A . 
N  5 S4P 1   204 204 S4P S4P A . 
O  2 ZN  1   201 201 ZN  ZN  B . 
P  4 GOL 1   202 202 GOL GOL B . 
Q  2 ZN  1   201 201 ZN  ZN  C . 
R  4 GOL 1   202 202 GOL GOL C . 
S  5 S4P 1   203 203 S4P S4P C . 
T  2 ZN  1   201 201 ZN  ZN  D . 
U  3 DMS 1   202 202 DMS DMS D . 
V  4 GOL 1   203 203 GOL GOL D . 
W  2 ZN  1   201 201 ZN  ZN  E . 
X  6 6B3 1   201 201 6B3 6B3 F . 
Y  2 ZN  1   202 202 ZN  ZN  F . 
Z  5 S4P 1   203 203 S4P S4P F . 
AA 2 ZN  1   201 201 ZN  ZN  H . 
BA 2 ZN  1   201 201 ZN  ZN  I . 
CA 2 ZN  1   201 201 ZN  ZN  J . 
DA 7 HOH 1   301 301 HOH HOH A . 
DA 7 HOH 2   302 302 HOH HOH A . 
DA 7 HOH 3   303 303 HOH HOH A . 
DA 7 HOH 4   304 304 HOH HOH A . 
DA 7 HOH 5   305 305 HOH HOH A . 
DA 7 HOH 6   306 306 HOH HOH A . 
DA 7 HOH 7   307 307 HOH HOH A . 
DA 7 HOH 8   308 308 HOH HOH A . 
DA 7 HOH 9   309 309 HOH HOH A . 
DA 7 HOH 10  310 310 HOH HOH A . 
DA 7 HOH 11  311 311 HOH HOH A . 
DA 7 HOH 12  312 312 HOH HOH A . 
DA 7 HOH 13  313 313 HOH HOH A . 
DA 7 HOH 14  314 314 HOH HOH A . 
DA 7 HOH 15  315 315 HOH HOH A . 
DA 7 HOH 16  316 316 HOH HOH A . 
DA 7 HOH 17  317 317 HOH HOH A . 
DA 7 HOH 18  318 318 HOH HOH A . 
DA 7 HOH 19  319 319 HOH HOH A . 
DA 7 HOH 20  320 320 HOH HOH A . 
DA 7 HOH 21  321 321 HOH HOH A . 
DA 7 HOH 22  322 322 HOH HOH A . 
DA 7 HOH 23  323 323 HOH HOH A . 
DA 7 HOH 24  324 324 HOH HOH A . 
DA 7 HOH 25  325 325 HOH HOH A . 
DA 7 HOH 26  326 326 HOH HOH A . 
DA 7 HOH 27  327 327 HOH HOH A . 
DA 7 HOH 28  328 328 HOH HOH A . 
DA 7 HOH 29  329 329 HOH HOH A . 
DA 7 HOH 30  330 330 HOH HOH A . 
DA 7 HOH 31  331 331 HOH HOH A . 
DA 7 HOH 32  332 332 HOH HOH A . 
DA 7 HOH 33  333 333 HOH HOH A . 
DA 7 HOH 34  334 334 HOH HOH A . 
DA 7 HOH 35  335 335 HOH HOH A . 
DA 7 HOH 36  336 336 HOH HOH A . 
DA 7 HOH 37  337 337 HOH HOH A . 
DA 7 HOH 38  338 338 HOH HOH A . 
DA 7 HOH 39  339 339 HOH HOH A . 
DA 7 HOH 40  340 340 HOH HOH A . 
DA 7 HOH 41  341 341 HOH HOH A . 
DA 7 HOH 42  342 342 HOH HOH A . 
DA 7 HOH 43  343 343 HOH HOH A . 
DA 7 HOH 44  344 344 HOH HOH A . 
DA 7 HOH 45  345 345 HOH HOH A . 
DA 7 HOH 46  346 346 HOH HOH A . 
DA 7 HOH 47  347 347 HOH HOH A . 
DA 7 HOH 48  348 348 HOH HOH A . 
DA 7 HOH 49  349 349 HOH HOH A . 
DA 7 HOH 50  350 350 HOH HOH A . 
DA 7 HOH 51  351 351 HOH HOH A . 
DA 7 HOH 52  352 352 HOH HOH A . 
DA 7 HOH 53  353 353 HOH HOH A . 
DA 7 HOH 54  354 354 HOH HOH A . 
DA 7 HOH 55  355 355 HOH HOH A . 
DA 7 HOH 56  356 356 HOH HOH A . 
DA 7 HOH 57  357 357 HOH HOH A . 
DA 7 HOH 58  358 358 HOH HOH A . 
DA 7 HOH 59  359 359 HOH HOH A . 
DA 7 HOH 60  360 360 HOH HOH A . 
DA 7 HOH 61  361 361 HOH HOH A . 
DA 7 HOH 62  362 362 HOH HOH A . 
DA 7 HOH 63  363 363 HOH HOH A . 
DA 7 HOH 64  364 364 HOH HOH A . 
DA 7 HOH 65  365 365 HOH HOH A . 
DA 7 HOH 66  366 366 HOH HOH A . 
DA 7 HOH 67  367 367 HOH HOH A . 
DA 7 HOH 68  368 368 HOH HOH A . 
DA 7 HOH 69  369 369 HOH HOH A . 
DA 7 HOH 70  370 370 HOH HOH A . 
DA 7 HOH 71  371 371 HOH HOH A . 
DA 7 HOH 72  372 372 HOH HOH A . 
DA 7 HOH 73  373 373 HOH HOH A . 
DA 7 HOH 74  374 374 HOH HOH A . 
DA 7 HOH 75  375 375 HOH HOH A . 
DA 7 HOH 76  376 376 HOH HOH A . 
DA 7 HOH 77  377 377 HOH HOH A . 
DA 7 HOH 78  378 378 HOH HOH A . 
DA 7 HOH 79  379 379 HOH HOH A . 
DA 7 HOH 80  380 380 HOH HOH A . 
DA 7 HOH 81  381 381 HOH HOH A . 
DA 7 HOH 82  382 382 HOH HOH A . 
DA 7 HOH 83  383 383 HOH HOH A . 
DA 7 HOH 84  384 384 HOH HOH A . 
DA 7 HOH 85  385 385 HOH HOH A . 
DA 7 HOH 86  386 386 HOH HOH A . 
DA 7 HOH 87  387 387 HOH HOH A . 
DA 7 HOH 88  388 388 HOH HOH A . 
DA 7 HOH 89  389 389 HOH HOH A . 
DA 7 HOH 90  390 390 HOH HOH A . 
DA 7 HOH 91  391 391 HOH HOH A . 
DA 7 HOH 92  392 392 HOH HOH A . 
DA 7 HOH 93  393 393 HOH HOH A . 
DA 7 HOH 94  394 394 HOH HOH A . 
DA 7 HOH 95  395 395 HOH HOH A . 
DA 7 HOH 96  396 396 HOH HOH A . 
DA 7 HOH 97  397 397 HOH HOH A . 
DA 7 HOH 98  398 398 HOH HOH A . 
DA 7 HOH 99  399 399 HOH HOH A . 
DA 7 HOH 100 400 400 HOH HOH A . 
DA 7 HOH 101 401 401 HOH HOH A . 
DA 7 HOH 102 402 402 HOH HOH A . 
DA 7 HOH 103 403 403 HOH HOH A . 
DA 7 HOH 104 404 404 HOH HOH A . 
DA 7 HOH 105 405 405 HOH HOH A . 
DA 7 HOH 106 406 406 HOH HOH A . 
DA 7 HOH 107 407 407 HOH HOH A . 
DA 7 HOH 108 408 408 HOH HOH A . 
DA 7 HOH 109 409 409 HOH HOH A . 
DA 7 HOH 110 410 410 HOH HOH A . 
DA 7 HOH 111 411 411 HOH HOH A . 
EA 7 HOH 1   301 301 HOH HOH B . 
EA 7 HOH 2   302 302 HOH HOH B . 
EA 7 HOH 3   303 303 HOH HOH B . 
EA 7 HOH 4   304 304 HOH HOH B . 
EA 7 HOH 5   305 305 HOH HOH B . 
EA 7 HOH 6   306 306 HOH HOH B . 
EA 7 HOH 7   307 307 HOH HOH B . 
EA 7 HOH 8   308 308 HOH HOH B . 
EA 7 HOH 9   309 309 HOH HOH B . 
EA 7 HOH 10  310 310 HOH HOH B . 
EA 7 HOH 11  311 311 HOH HOH B . 
EA 7 HOH 12  312 312 HOH HOH B . 
EA 7 HOH 13  313 313 HOH HOH B . 
EA 7 HOH 14  314 314 HOH HOH B . 
EA 7 HOH 15  315 315 HOH HOH B . 
EA 7 HOH 16  316 316 HOH HOH B . 
EA 7 HOH 17  317 317 HOH HOH B . 
EA 7 HOH 18  318 318 HOH HOH B . 
EA 7 HOH 19  319 319 HOH HOH B . 
EA 7 HOH 20  320 320 HOH HOH B . 
EA 7 HOH 21  321 321 HOH HOH B . 
EA 7 HOH 22  322 322 HOH HOH B . 
EA 7 HOH 23  323 323 HOH HOH B . 
EA 7 HOH 24  324 324 HOH HOH B . 
EA 7 HOH 25  325 325 HOH HOH B . 
EA 7 HOH 26  326 326 HOH HOH B . 
EA 7 HOH 27  327 327 HOH HOH B . 
EA 7 HOH 28  328 328 HOH HOH B . 
EA 7 HOH 29  329 329 HOH HOH B . 
EA 7 HOH 30  330 330 HOH HOH B . 
EA 7 HOH 31  331 331 HOH HOH B . 
EA 7 HOH 32  332 332 HOH HOH B . 
EA 7 HOH 33  333 333 HOH HOH B . 
EA 7 HOH 34  334 334 HOH HOH B . 
EA 7 HOH 35  335 335 HOH HOH B . 
EA 7 HOH 36  336 336 HOH HOH B . 
EA 7 HOH 37  337 337 HOH HOH B . 
EA 7 HOH 38  338 338 HOH HOH B . 
EA 7 HOH 39  339 339 HOH HOH B . 
EA 7 HOH 40  340 340 HOH HOH B . 
EA 7 HOH 41  341 341 HOH HOH B . 
EA 7 HOH 42  342 342 HOH HOH B . 
EA 7 HOH 43  343 343 HOH HOH B . 
EA 7 HOH 44  344 344 HOH HOH B . 
EA 7 HOH 45  345 345 HOH HOH B . 
EA 7 HOH 46  346 346 HOH HOH B . 
EA 7 HOH 47  347 347 HOH HOH B . 
EA 7 HOH 48  348 348 HOH HOH B . 
EA 7 HOH 49  349 349 HOH HOH B . 
EA 7 HOH 50  350 350 HOH HOH B . 
EA 7 HOH 51  351 351 HOH HOH B . 
EA 7 HOH 52  352 352 HOH HOH B . 
EA 7 HOH 53  353 353 HOH HOH B . 
EA 7 HOH 54  354 354 HOH HOH B . 
EA 7 HOH 55  355 355 HOH HOH B . 
EA 7 HOH 56  356 356 HOH HOH B . 
EA 7 HOH 57  357 357 HOH HOH B . 
EA 7 HOH 58  358 358 HOH HOH B . 
EA 7 HOH 59  359 359 HOH HOH B . 
EA 7 HOH 60  360 360 HOH HOH B . 
EA 7 HOH 61  361 361 HOH HOH B . 
EA 7 HOH 62  362 362 HOH HOH B . 
EA 7 HOH 63  363 363 HOH HOH B . 
EA 7 HOH 64  364 364 HOH HOH B . 
EA 7 HOH 65  365 365 HOH HOH B . 
EA 7 HOH 66  366 366 HOH HOH B . 
EA 7 HOH 67  367 367 HOH HOH B . 
EA 7 HOH 68  368 368 HOH HOH B . 
EA 7 HOH 69  369 369 HOH HOH B . 
EA 7 HOH 70  370 370 HOH HOH B . 
EA 7 HOH 71  371 371 HOH HOH B . 
EA 7 HOH 72  372 372 HOH HOH B . 
EA 7 HOH 73  373 373 HOH HOH B . 
EA 7 HOH 74  374 374 HOH HOH B . 
EA 7 HOH 75  375 375 HOH HOH B . 
EA 7 HOH 76  376 376 HOH HOH B . 
EA 7 HOH 77  377 377 HOH HOH B . 
EA 7 HOH 78  378 378 HOH HOH B . 
EA 7 HOH 79  379 379 HOH HOH B . 
EA 7 HOH 80  380 380 HOH HOH B . 
EA 7 HOH 81  381 381 HOH HOH B . 
EA 7 HOH 82  382 382 HOH HOH B . 
EA 7 HOH 83  383 383 HOH HOH B . 
EA 7 HOH 84  384 384 HOH HOH B . 
EA 7 HOH 85  385 385 HOH HOH B . 
EA 7 HOH 86  386 386 HOH HOH B . 
EA 7 HOH 87  387 387 HOH HOH B . 
EA 7 HOH 88  388 388 HOH HOH B . 
EA 7 HOH 89  389 389 HOH HOH B . 
EA 7 HOH 90  390 390 HOH HOH B . 
EA 7 HOH 91  391 391 HOH HOH B . 
EA 7 HOH 92  392 392 HOH HOH B . 
EA 7 HOH 93  393 393 HOH HOH B . 
EA 7 HOH 94  394 394 HOH HOH B . 
EA 7 HOH 95  395 395 HOH HOH B . 
EA 7 HOH 96  396 396 HOH HOH B . 
EA 7 HOH 97  397 397 HOH HOH B . 
EA 7 HOH 98  398 398 HOH HOH B . 
EA 7 HOH 99  399 399 HOH HOH B . 
EA 7 HOH 100 400 400 HOH HOH B . 
EA 7 HOH 101 401 401 HOH HOH B . 
EA 7 HOH 102 402 402 HOH HOH B . 
EA 7 HOH 103 403 403 HOH HOH B . 
EA 7 HOH 104 404 404 HOH HOH B . 
EA 7 HOH 105 405 405 HOH HOH B . 
EA 7 HOH 106 406 406 HOH HOH B . 
EA 7 HOH 107 407 407 HOH HOH B . 
EA 7 HOH 108 408 408 HOH HOH B . 
EA 7 HOH 109 409 409 HOH HOH B . 
EA 7 HOH 110 410 410 HOH HOH B . 
EA 7 HOH 111 411 411 HOH HOH B . 
EA 7 HOH 112 412 412 HOH HOH B . 
EA 7 HOH 113 413 413 HOH HOH B . 
EA 7 HOH 114 414 414 HOH HOH B . 
EA 7 HOH 115 415 415 HOH HOH B . 
EA 7 HOH 116 416 416 HOH HOH B . 
EA 7 HOH 117 417 417 HOH HOH B . 
EA 7 HOH 118 418 418 HOH HOH B . 
EA 7 HOH 119 419 419 HOH HOH B . 
EA 7 HOH 120 420 420 HOH HOH B . 
EA 7 HOH 121 421 421 HOH HOH B . 
EA 7 HOH 122 422 422 HOH HOH B . 
EA 7 HOH 123 423 423 HOH HOH B . 
EA 7 HOH 124 424 424 HOH HOH B . 
EA 7 HOH 125 425 425 HOH HOH B . 
EA 7 HOH 126 426 426 HOH HOH B . 
EA 7 HOH 127 427 427 HOH HOH B . 
EA 7 HOH 128 428 428 HOH HOH B . 
EA 7 HOH 129 429 429 HOH HOH B . 
EA 7 HOH 130 430 430 HOH HOH B . 
EA 7 HOH 131 431 431 HOH HOH B . 
EA 7 HOH 132 432 432 HOH HOH B . 
EA 7 HOH 133 433 433 HOH HOH B . 
EA 7 HOH 134 434 434 HOH HOH B . 
EA 7 HOH 135 435 435 HOH HOH B . 
EA 7 HOH 136 436 436 HOH HOH B . 
EA 7 HOH 137 437 437 HOH HOH B . 
EA 7 HOH 138 438 438 HOH HOH B . 
EA 7 HOH 139 439 439 HOH HOH B . 
EA 7 HOH 140 440 440 HOH HOH B . 
EA 7 HOH 141 441 441 HOH HOH B . 
EA 7 HOH 142 442 442 HOH HOH B . 
EA 7 HOH 143 443 443 HOH HOH B . 
EA 7 HOH 144 444 444 HOH HOH B . 
EA 7 HOH 145 445 445 HOH HOH B . 
EA 7 HOH 146 446 446 HOH HOH B . 
EA 7 HOH 147 447 447 HOH HOH B . 
EA 7 HOH 148 448 448 HOH HOH B . 
EA 7 HOH 149 449 449 HOH HOH B . 
EA 7 HOH 150 450 450 HOH HOH B . 
EA 7 HOH 151 451 451 HOH HOH B . 
EA 7 HOH 152 452 452 HOH HOH B . 
EA 7 HOH 153 453 453 HOH HOH B . 
EA 7 HOH 154 454 454 HOH HOH B . 
EA 7 HOH 155 455 455 HOH HOH B . 
EA 7 HOH 156 456 456 HOH HOH B . 
EA 7 HOH 157 457 457 HOH HOH B . 
EA 7 HOH 158 458 458 HOH HOH B . 
EA 7 HOH 159 459 459 HOH HOH B . 
EA 7 HOH 160 460 460 HOH HOH B . 
EA 7 HOH 161 461 461 HOH HOH B . 
FA 7 HOH 1   301 301 HOH HOH C . 
FA 7 HOH 2   302 302 HOH HOH C . 
FA 7 HOH 3   303 303 HOH HOH C . 
FA 7 HOH 4   304 304 HOH HOH C . 
FA 7 HOH 5   305 305 HOH HOH C . 
FA 7 HOH 6   306 306 HOH HOH C . 
FA 7 HOH 7   307 307 HOH HOH C . 
FA 7 HOH 8   308 308 HOH HOH C . 
FA 7 HOH 9   309 309 HOH HOH C . 
FA 7 HOH 10  310 310 HOH HOH C . 
FA 7 HOH 11  311 311 HOH HOH C . 
FA 7 HOH 12  312 312 HOH HOH C . 
FA 7 HOH 13  313 313 HOH HOH C . 
FA 7 HOH 14  314 314 HOH HOH C . 
FA 7 HOH 15  315 315 HOH HOH C . 
FA 7 HOH 16  316 316 HOH HOH C . 
FA 7 HOH 17  317 317 HOH HOH C . 
FA 7 HOH 18  318 318 HOH HOH C . 
FA 7 HOH 19  319 319 HOH HOH C . 
FA 7 HOH 20  320 320 HOH HOH C . 
FA 7 HOH 21  321 321 HOH HOH C . 
FA 7 HOH 22  322 322 HOH HOH C . 
FA 7 HOH 23  323 323 HOH HOH C . 
FA 7 HOH 24  324 324 HOH HOH C . 
FA 7 HOH 25  325 325 HOH HOH C . 
FA 7 HOH 26  326 326 HOH HOH C . 
FA 7 HOH 27  327 327 HOH HOH C . 
FA 7 HOH 28  328 328 HOH HOH C . 
FA 7 HOH 29  329 329 HOH HOH C . 
FA 7 HOH 30  330 330 HOH HOH C . 
FA 7 HOH 31  331 331 HOH HOH C . 
FA 7 HOH 32  332 332 HOH HOH C . 
FA 7 HOH 33  333 333 HOH HOH C . 
FA 7 HOH 34  334 334 HOH HOH C . 
FA 7 HOH 35  335 335 HOH HOH C . 
FA 7 HOH 36  336 336 HOH HOH C . 
FA 7 HOH 37  337 337 HOH HOH C . 
FA 7 HOH 38  338 338 HOH HOH C . 
FA 7 HOH 39  339 339 HOH HOH C . 
FA 7 HOH 40  340 340 HOH HOH C . 
FA 7 HOH 41  341 341 HOH HOH C . 
FA 7 HOH 42  342 342 HOH HOH C . 
FA 7 HOH 43  343 343 HOH HOH C . 
FA 7 HOH 44  344 344 HOH HOH C . 
FA 7 HOH 45  345 345 HOH HOH C . 
FA 7 HOH 46  346 346 HOH HOH C . 
FA 7 HOH 47  347 347 HOH HOH C . 
FA 7 HOH 48  348 348 HOH HOH C . 
FA 7 HOH 49  349 349 HOH HOH C . 
FA 7 HOH 50  350 350 HOH HOH C . 
FA 7 HOH 51  351 351 HOH HOH C . 
FA 7 HOH 52  352 352 HOH HOH C . 
FA 7 HOH 53  353 353 HOH HOH C . 
FA 7 HOH 54  354 354 HOH HOH C . 
FA 7 HOH 55  355 355 HOH HOH C . 
FA 7 HOH 56  356 356 HOH HOH C . 
FA 7 HOH 57  357 357 HOH HOH C . 
FA 7 HOH 58  358 358 HOH HOH C . 
FA 7 HOH 59  359 359 HOH HOH C . 
FA 7 HOH 60  360 360 HOH HOH C . 
FA 7 HOH 61  361 361 HOH HOH C . 
FA 7 HOH 62  362 362 HOH HOH C . 
FA 7 HOH 63  363 363 HOH HOH C . 
FA 7 HOH 64  364 364 HOH HOH C . 
FA 7 HOH 65  365 365 HOH HOH C . 
FA 7 HOH 66  366 366 HOH HOH C . 
FA 7 HOH 67  367 367 HOH HOH C . 
FA 7 HOH 68  368 368 HOH HOH C . 
FA 7 HOH 69  369 369 HOH HOH C . 
FA 7 HOH 70  370 370 HOH HOH C . 
FA 7 HOH 71  371 371 HOH HOH C . 
FA 7 HOH 72  372 372 HOH HOH C . 
FA 7 HOH 73  373 373 HOH HOH C . 
FA 7 HOH 74  374 374 HOH HOH C . 
FA 7 HOH 75  375 375 HOH HOH C . 
FA 7 HOH 76  376 376 HOH HOH C . 
FA 7 HOH 77  377 377 HOH HOH C . 
FA 7 HOH 78  378 378 HOH HOH C . 
FA 7 HOH 79  379 379 HOH HOH C . 
FA 7 HOH 80  380 380 HOH HOH C . 
FA 7 HOH 81  381 381 HOH HOH C . 
FA 7 HOH 82  382 382 HOH HOH C . 
FA 7 HOH 83  383 383 HOH HOH C . 
FA 7 HOH 84  384 384 HOH HOH C . 
FA 7 HOH 85  385 385 HOH HOH C . 
FA 7 HOH 86  386 386 HOH HOH C . 
FA 7 HOH 87  387 387 HOH HOH C . 
FA 7 HOH 88  388 388 HOH HOH C . 
FA 7 HOH 89  389 389 HOH HOH C . 
FA 7 HOH 90  390 390 HOH HOH C . 
FA 7 HOH 91  391 391 HOH HOH C . 
FA 7 HOH 92  392 392 HOH HOH C . 
FA 7 HOH 93  393 393 HOH HOH C . 
FA 7 HOH 94  394 394 HOH HOH C . 
FA 7 HOH 95  395 395 HOH HOH C . 
FA 7 HOH 96  396 396 HOH HOH C . 
FA 7 HOH 97  397 397 HOH HOH C . 
FA 7 HOH 98  398 398 HOH HOH C . 
FA 7 HOH 99  399 399 HOH HOH C . 
FA 7 HOH 100 400 400 HOH HOH C . 
FA 7 HOH 101 401 401 HOH HOH C . 
FA 7 HOH 102 402 402 HOH HOH C . 
FA 7 HOH 103 403 403 HOH HOH C . 
FA 7 HOH 104 404 404 HOH HOH C . 
FA 7 HOH 105 405 405 HOH HOH C . 
FA 7 HOH 106 406 406 HOH HOH C . 
FA 7 HOH 107 407 407 HOH HOH C . 
FA 7 HOH 108 408 408 HOH HOH C . 
FA 7 HOH 109 409 409 HOH HOH C . 
FA 7 HOH 110 410 410 HOH HOH C . 
FA 7 HOH 111 411 411 HOH HOH C . 
FA 7 HOH 112 412 412 HOH HOH C . 
FA 7 HOH 113 413 413 HOH HOH C . 
FA 7 HOH 114 414 414 HOH HOH C . 
FA 7 HOH 115 415 415 HOH HOH C . 
FA 7 HOH 116 416 416 HOH HOH C . 
FA 7 HOH 117 417 417 HOH HOH C . 
FA 7 HOH 118 418 418 HOH HOH C . 
FA 7 HOH 119 419 419 HOH HOH C . 
FA 7 HOH 120 420 420 HOH HOH C . 
FA 7 HOH 121 421 421 HOH HOH C . 
FA 7 HOH 122 422 422 HOH HOH C . 
FA 7 HOH 123 423 423 HOH HOH C . 
FA 7 HOH 124 424 424 HOH HOH C . 
FA 7 HOH 125 425 425 HOH HOH C . 
FA 7 HOH 126 426 426 HOH HOH C . 
FA 7 HOH 127 427 427 HOH HOH C . 
FA 7 HOH 128 428 428 HOH HOH C . 
FA 7 HOH 129 429 429 HOH HOH C . 
FA 7 HOH 130 430 430 HOH HOH C . 
FA 7 HOH 131 431 431 HOH HOH C . 
FA 7 HOH 132 432 432 HOH HOH C . 
FA 7 HOH 133 433 433 HOH HOH C . 
GA 7 HOH 1   301 301 HOH HOH D . 
GA 7 HOH 2   302 302 HOH HOH D . 
GA 7 HOH 3   303 303 HOH HOH D . 
GA 7 HOH 4   304 304 HOH HOH D . 
GA 7 HOH 5   305 305 HOH HOH D . 
GA 7 HOH 6   306 306 HOH HOH D . 
GA 7 HOH 7   307 307 HOH HOH D . 
GA 7 HOH 8   308 308 HOH HOH D . 
GA 7 HOH 9   309 309 HOH HOH D . 
GA 7 HOH 10  310 310 HOH HOH D . 
GA 7 HOH 11  311 311 HOH HOH D . 
GA 7 HOH 12  312 312 HOH HOH D . 
GA 7 HOH 13  313 313 HOH HOH D . 
GA 7 HOH 14  314 314 HOH HOH D . 
GA 7 HOH 15  315 315 HOH HOH D . 
GA 7 HOH 16  316 316 HOH HOH D . 
GA 7 HOH 17  317 317 HOH HOH D . 
GA 7 HOH 18  318 318 HOH HOH D . 
GA 7 HOH 19  319 319 HOH HOH D . 
GA 7 HOH 20  320 320 HOH HOH D . 
GA 7 HOH 21  321 321 HOH HOH D . 
GA 7 HOH 22  322 322 HOH HOH D . 
GA 7 HOH 23  323 323 HOH HOH D . 
GA 7 HOH 24  324 324 HOH HOH D . 
GA 7 HOH 25  325 325 HOH HOH D . 
GA 7 HOH 26  326 326 HOH HOH D . 
GA 7 HOH 27  327 327 HOH HOH D . 
GA 7 HOH 28  328 328 HOH HOH D . 
GA 7 HOH 29  329 329 HOH HOH D . 
GA 7 HOH 30  330 330 HOH HOH D . 
GA 7 HOH 31  331 331 HOH HOH D . 
GA 7 HOH 32  332 332 HOH HOH D . 
GA 7 HOH 33  333 333 HOH HOH D . 
GA 7 HOH 34  334 334 HOH HOH D . 
GA 7 HOH 35  335 335 HOH HOH D . 
GA 7 HOH 36  336 336 HOH HOH D . 
GA 7 HOH 37  337 337 HOH HOH D . 
GA 7 HOH 38  338 338 HOH HOH D . 
GA 7 HOH 39  339 339 HOH HOH D . 
GA 7 HOH 40  340 340 HOH HOH D . 
GA 7 HOH 41  341 341 HOH HOH D . 
GA 7 HOH 42  342 342 HOH HOH D . 
GA 7 HOH 43  343 343 HOH HOH D . 
GA 7 HOH 44  344 344 HOH HOH D . 
GA 7 HOH 45  345 345 HOH HOH D . 
GA 7 HOH 46  346 346 HOH HOH D . 
GA 7 HOH 47  347 347 HOH HOH D . 
GA 7 HOH 48  348 348 HOH HOH D . 
GA 7 HOH 49  349 349 HOH HOH D . 
GA 7 HOH 50  350 350 HOH HOH D . 
GA 7 HOH 51  351 351 HOH HOH D . 
GA 7 HOH 52  352 352 HOH HOH D . 
GA 7 HOH 53  353 353 HOH HOH D . 
GA 7 HOH 54  354 354 HOH HOH D . 
GA 7 HOH 55  355 355 HOH HOH D . 
GA 7 HOH 56  356 356 HOH HOH D . 
GA 7 HOH 57  357 357 HOH HOH D . 
GA 7 HOH 58  358 358 HOH HOH D . 
GA 7 HOH 59  359 359 HOH HOH D . 
GA 7 HOH 60  360 360 HOH HOH D . 
GA 7 HOH 61  361 361 HOH HOH D . 
GA 7 HOH 62  362 362 HOH HOH D . 
GA 7 HOH 63  363 363 HOH HOH D . 
GA 7 HOH 64  364 364 HOH HOH D . 
GA 7 HOH 65  365 365 HOH HOH D . 
GA 7 HOH 66  366 366 HOH HOH D . 
GA 7 HOH 67  367 367 HOH HOH D . 
GA 7 HOH 68  368 368 HOH HOH D . 
GA 7 HOH 69  369 369 HOH HOH D . 
GA 7 HOH 70  370 370 HOH HOH D . 
GA 7 HOH 71  371 371 HOH HOH D . 
GA 7 HOH 72  372 372 HOH HOH D . 
GA 7 HOH 73  373 373 HOH HOH D . 
GA 7 HOH 74  374 374 HOH HOH D . 
GA 7 HOH 75  375 375 HOH HOH D . 
GA 7 HOH 76  376 376 HOH HOH D . 
GA 7 HOH 77  377 377 HOH HOH D . 
GA 7 HOH 78  378 378 HOH HOH D . 
GA 7 HOH 79  379 379 HOH HOH D . 
GA 7 HOH 80  380 380 HOH HOH D . 
GA 7 HOH 81  381 381 HOH HOH D . 
GA 7 HOH 82  382 382 HOH HOH D . 
GA 7 HOH 83  383 383 HOH HOH D . 
GA 7 HOH 84  384 384 HOH HOH D . 
GA 7 HOH 85  385 385 HOH HOH D . 
GA 7 HOH 86  386 386 HOH HOH D . 
GA 7 HOH 87  387 387 HOH HOH D . 
GA 7 HOH 88  388 388 HOH HOH D . 
GA 7 HOH 89  389 389 HOH HOH D . 
GA 7 HOH 90  390 390 HOH HOH D . 
GA 7 HOH 91  391 391 HOH HOH D . 
GA 7 HOH 92  392 392 HOH HOH D . 
GA 7 HOH 93  393 393 HOH HOH D . 
GA 7 HOH 94  394 394 HOH HOH D . 
GA 7 HOH 95  395 395 HOH HOH D . 
GA 7 HOH 96  396 396 HOH HOH D . 
GA 7 HOH 97  397 397 HOH HOH D . 
GA 7 HOH 98  398 398 HOH HOH D . 
GA 7 HOH 99  399 399 HOH HOH D . 
GA 7 HOH 100 400 400 HOH HOH D . 
GA 7 HOH 101 401 401 HOH HOH D . 
GA 7 HOH 102 402 402 HOH HOH D . 
GA 7 HOH 103 403 403 HOH HOH D . 
GA 7 HOH 104 404 404 HOH HOH D . 
GA 7 HOH 105 405 405 HOH HOH D . 
GA 7 HOH 106 406 406 HOH HOH D . 
GA 7 HOH 107 407 407 HOH HOH D . 
GA 7 HOH 108 408 408 HOH HOH D . 
GA 7 HOH 109 409 409 HOH HOH D . 
GA 7 HOH 110 410 410 HOH HOH D . 
GA 7 HOH 111 411 411 HOH HOH D . 
GA 7 HOH 112 412 412 HOH HOH D . 
GA 7 HOH 113 413 413 HOH HOH D . 
GA 7 HOH 114 414 414 HOH HOH D . 
GA 7 HOH 115 415 415 HOH HOH D . 
GA 7 HOH 116 416 416 HOH HOH D . 
GA 7 HOH 117 417 417 HOH HOH D . 
GA 7 HOH 118 418 418 HOH HOH D . 
GA 7 HOH 119 419 419 HOH HOH D . 
GA 7 HOH 120 420 420 HOH HOH D . 
GA 7 HOH 121 421 421 HOH HOH D . 
GA 7 HOH 122 422 422 HOH HOH D . 
GA 7 HOH 123 423 423 HOH HOH D . 
GA 7 HOH 124 424 424 HOH HOH D . 
GA 7 HOH 125 425 425 HOH HOH D . 
GA 7 HOH 126 426 426 HOH HOH D . 
GA 7 HOH 127 427 427 HOH HOH D . 
GA 7 HOH 128 428 428 HOH HOH D . 
GA 7 HOH 129 429 429 HOH HOH D . 
GA 7 HOH 130 430 430 HOH HOH D . 
GA 7 HOH 131 431 431 HOH HOH D . 
GA 7 HOH 132 432 432 HOH HOH D . 
GA 7 HOH 133 433 433 HOH HOH D . 
GA 7 HOH 134 434 434 HOH HOH D . 
GA 7 HOH 135 435 435 HOH HOH D . 
GA 7 HOH 136 436 436 HOH HOH D . 
GA 7 HOH 137 437 437 HOH HOH D . 
GA 7 HOH 138 438 438 HOH HOH D . 
GA 7 HOH 139 439 439 HOH HOH D . 
GA 7 HOH 140 440 440 HOH HOH D . 
GA 7 HOH 141 441 441 HOH HOH D . 
GA 7 HOH 142 442 442 HOH HOH D . 
GA 7 HOH 143 443 443 HOH HOH D . 
GA 7 HOH 144 444 444 HOH HOH D . 
GA 7 HOH 145 445 445 HOH HOH D . 
GA 7 HOH 146 446 446 HOH HOH D . 
GA 7 HOH 147 447 447 HOH HOH D . 
GA 7 HOH 148 448 448 HOH HOH D . 
GA 7 HOH 149 449 449 HOH HOH D . 
GA 7 HOH 150 450 450 HOH HOH D . 
GA 7 HOH 151 451 451 HOH HOH D . 
GA 7 HOH 152 452 452 HOH HOH D . 
GA 7 HOH 153 453 453 HOH HOH D . 
GA 7 HOH 154 454 454 HOH HOH D . 
GA 7 HOH 155 455 455 HOH HOH D . 
GA 7 HOH 156 456 456 HOH HOH D . 
GA 7 HOH 157 457 457 HOH HOH D . 
GA 7 HOH 158 458 458 HOH HOH D . 
GA 7 HOH 159 459 459 HOH HOH D . 
GA 7 HOH 160 460 460 HOH HOH D . 
GA 7 HOH 161 461 461 HOH HOH D . 
GA 7 HOH 162 462 462 HOH HOH D . 
GA 7 HOH 163 463 463 HOH HOH D . 
GA 7 HOH 164 464 464 HOH HOH D . 
GA 7 HOH 165 465 465 HOH HOH D . 
GA 7 HOH 166 466 466 HOH HOH D . 
GA 7 HOH 167 467 467 HOH HOH D . 
GA 7 HOH 168 468 468 HOH HOH D . 
GA 7 HOH 169 469 469 HOH HOH D . 
HA 7 HOH 1   301 301 HOH HOH E . 
HA 7 HOH 2   302 302 HOH HOH E . 
HA 7 HOH 3   303 303 HOH HOH E . 
HA 7 HOH 4   304 304 HOH HOH E . 
HA 7 HOH 5   305 305 HOH HOH E . 
HA 7 HOH 6   306 306 HOH HOH E . 
HA 7 HOH 7   307 307 HOH HOH E . 
HA 7 HOH 8   308 308 HOH HOH E . 
HA 7 HOH 9   309 309 HOH HOH E . 
HA 7 HOH 10  310 310 HOH HOH E . 
HA 7 HOH 11  311 311 HOH HOH E . 
HA 7 HOH 12  312 312 HOH HOH E . 
HA 7 HOH 13  313 313 HOH HOH E . 
HA 7 HOH 14  314 314 HOH HOH E . 
HA 7 HOH 15  315 315 HOH HOH E . 
HA 7 HOH 16  316 316 HOH HOH E . 
HA 7 HOH 17  317 317 HOH HOH E . 
HA 7 HOH 18  318 318 HOH HOH E . 
HA 7 HOH 19  319 319 HOH HOH E . 
HA 7 HOH 20  320 320 HOH HOH E . 
HA 7 HOH 21  321 321 HOH HOH E . 
HA 7 HOH 22  322 322 HOH HOH E . 
HA 7 HOH 23  323 323 HOH HOH E . 
HA 7 HOH 24  324 324 HOH HOH E . 
HA 7 HOH 25  325 325 HOH HOH E . 
HA 7 HOH 26  326 326 HOH HOH E . 
HA 7 HOH 27  327 327 HOH HOH E . 
HA 7 HOH 28  328 328 HOH HOH E . 
HA 7 HOH 29  329 329 HOH HOH E . 
HA 7 HOH 30  330 330 HOH HOH E . 
HA 7 HOH 31  331 331 HOH HOH E . 
HA 7 HOH 32  332 332 HOH HOH E . 
HA 7 HOH 33  333 333 HOH HOH E . 
HA 7 HOH 34  334 334 HOH HOH E . 
HA 7 HOH 35  335 335 HOH HOH E . 
HA 7 HOH 36  336 336 HOH HOH E . 
HA 7 HOH 37  337 337 HOH HOH E . 
HA 7 HOH 38  338 338 HOH HOH E . 
HA 7 HOH 39  339 339 HOH HOH E . 
HA 7 HOH 40  340 340 HOH HOH E . 
HA 7 HOH 41  341 341 HOH HOH E . 
HA 7 HOH 42  342 342 HOH HOH E . 
HA 7 HOH 43  343 343 HOH HOH E . 
HA 7 HOH 44  344 344 HOH HOH E . 
HA 7 HOH 45  345 345 HOH HOH E . 
HA 7 HOH 46  346 346 HOH HOH E . 
HA 7 HOH 47  347 347 HOH HOH E . 
HA 7 HOH 48  348 348 HOH HOH E . 
HA 7 HOH 49  349 349 HOH HOH E . 
HA 7 HOH 50  350 350 HOH HOH E . 
HA 7 HOH 51  351 351 HOH HOH E . 
HA 7 HOH 52  352 352 HOH HOH E . 
HA 7 HOH 53  353 353 HOH HOH E . 
HA 7 HOH 54  354 354 HOH HOH E . 
HA 7 HOH 55  355 355 HOH HOH E . 
HA 7 HOH 56  356 356 HOH HOH E . 
HA 7 HOH 57  357 357 HOH HOH E . 
HA 7 HOH 58  358 358 HOH HOH E . 
HA 7 HOH 59  359 359 HOH HOH E . 
HA 7 HOH 60  360 360 HOH HOH E . 
HA 7 HOH 61  361 361 HOH HOH E . 
HA 7 HOH 62  362 362 HOH HOH E . 
HA 7 HOH 63  363 363 HOH HOH E . 
HA 7 HOH 64  364 364 HOH HOH E . 
HA 7 HOH 65  365 365 HOH HOH E . 
HA 7 HOH 66  366 366 HOH HOH E . 
HA 7 HOH 67  367 367 HOH HOH E . 
HA 7 HOH 68  368 368 HOH HOH E . 
HA 7 HOH 69  369 369 HOH HOH E . 
HA 7 HOH 70  370 370 HOH HOH E . 
HA 7 HOH 71  371 371 HOH HOH E . 
HA 7 HOH 72  372 372 HOH HOH E . 
HA 7 HOH 73  373 373 HOH HOH E . 
HA 7 HOH 74  374 374 HOH HOH E . 
HA 7 HOH 75  375 375 HOH HOH E . 
HA 7 HOH 76  376 376 HOH HOH E . 
HA 7 HOH 77  377 377 HOH HOH E . 
HA 7 HOH 78  378 378 HOH HOH E . 
HA 7 HOH 79  379 379 HOH HOH E . 
HA 7 HOH 80  380 380 HOH HOH E . 
HA 7 HOH 81  381 381 HOH HOH E . 
HA 7 HOH 82  382 382 HOH HOH E . 
HA 7 HOH 83  383 383 HOH HOH E . 
HA 7 HOH 84  384 384 HOH HOH E . 
HA 7 HOH 85  385 385 HOH HOH E . 
HA 7 HOH 86  386 386 HOH HOH E . 
HA 7 HOH 87  387 387 HOH HOH E . 
HA 7 HOH 88  388 388 HOH HOH E . 
HA 7 HOH 89  389 389 HOH HOH E . 
HA 7 HOH 90  390 390 HOH HOH E . 
HA 7 HOH 91  391 391 HOH HOH E . 
HA 7 HOH 92  392 392 HOH HOH E . 
HA 7 HOH 93  393 393 HOH HOH E . 
HA 7 HOH 94  394 394 HOH HOH E . 
HA 7 HOH 95  395 395 HOH HOH E . 
HA 7 HOH 96  396 396 HOH HOH E . 
HA 7 HOH 97  397 397 HOH HOH E . 
HA 7 HOH 98  398 398 HOH HOH E . 
HA 7 HOH 99  399 399 HOH HOH E . 
HA 7 HOH 100 400 400 HOH HOH E . 
HA 7 HOH 101 401 401 HOH HOH E . 
HA 7 HOH 102 402 402 HOH HOH E . 
HA 7 HOH 103 403 403 HOH HOH E . 
HA 7 HOH 104 404 404 HOH HOH E . 
HA 7 HOH 105 405 405 HOH HOH E . 
HA 7 HOH 106 406 406 HOH HOH E . 
HA 7 HOH 107 407 407 HOH HOH E . 
HA 7 HOH 108 408 408 HOH HOH E . 
HA 7 HOH 109 409 409 HOH HOH E . 
HA 7 HOH 110 410 410 HOH HOH E . 
HA 7 HOH 111 411 411 HOH HOH E . 
HA 7 HOH 112 412 412 HOH HOH E . 
HA 7 HOH 113 413 413 HOH HOH E . 
HA 7 HOH 114 414 414 HOH HOH E . 
HA 7 HOH 115 415 415 HOH HOH E . 
HA 7 HOH 116 416 416 HOH HOH E . 
IA 7 HOH 1   301 301 HOH HOH F . 
IA 7 HOH 2   302 302 HOH HOH F . 
IA 7 HOH 3   303 303 HOH HOH F . 
IA 7 HOH 4   304 304 HOH HOH F . 
IA 7 HOH 5   305 305 HOH HOH F . 
IA 7 HOH 6   306 306 HOH HOH F . 
IA 7 HOH 7   307 307 HOH HOH F . 
IA 7 HOH 8   308 308 HOH HOH F . 
IA 7 HOH 9   309 309 HOH HOH F . 
IA 7 HOH 10  310 310 HOH HOH F . 
IA 7 HOH 11  311 311 HOH HOH F . 
IA 7 HOH 12  312 312 HOH HOH F . 
IA 7 HOH 13  313 313 HOH HOH F . 
IA 7 HOH 14  314 314 HOH HOH F . 
IA 7 HOH 15  315 315 HOH HOH F . 
IA 7 HOH 16  316 316 HOH HOH F . 
IA 7 HOH 17  317 317 HOH HOH F . 
IA 7 HOH 18  318 318 HOH HOH F . 
IA 7 HOH 19  319 319 HOH HOH F . 
IA 7 HOH 20  320 320 HOH HOH F . 
IA 7 HOH 21  321 321 HOH HOH F . 
IA 7 HOH 22  322 322 HOH HOH F . 
IA 7 HOH 23  323 323 HOH HOH F . 
IA 7 HOH 24  324 324 HOH HOH F . 
IA 7 HOH 25  325 325 HOH HOH F . 
IA 7 HOH 26  326 326 HOH HOH F . 
IA 7 HOH 27  327 327 HOH HOH F . 
IA 7 HOH 28  328 328 HOH HOH F . 
IA 7 HOH 29  329 329 HOH HOH F . 
IA 7 HOH 30  330 330 HOH HOH F . 
IA 7 HOH 31  331 331 HOH HOH F . 
IA 7 HOH 32  332 332 HOH HOH F . 
IA 7 HOH 33  333 333 HOH HOH F . 
IA 7 HOH 34  334 334 HOH HOH F . 
IA 7 HOH 35  335 335 HOH HOH F . 
IA 7 HOH 36  336 336 HOH HOH F . 
IA 7 HOH 37  337 337 HOH HOH F . 
IA 7 HOH 38  338 338 HOH HOH F . 
IA 7 HOH 39  339 339 HOH HOH F . 
IA 7 HOH 40  340 340 HOH HOH F . 
IA 7 HOH 41  341 341 HOH HOH F . 
IA 7 HOH 42  342 342 HOH HOH F . 
IA 7 HOH 43  343 343 HOH HOH F . 
IA 7 HOH 44  344 344 HOH HOH F . 
IA 7 HOH 45  345 345 HOH HOH F . 
IA 7 HOH 46  346 346 HOH HOH F . 
IA 7 HOH 47  347 347 HOH HOH F . 
IA 7 HOH 48  348 348 HOH HOH F . 
IA 7 HOH 49  349 349 HOH HOH F . 
IA 7 HOH 50  350 350 HOH HOH F . 
IA 7 HOH 51  351 351 HOH HOH F . 
IA 7 HOH 52  352 352 HOH HOH F . 
IA 7 HOH 53  353 353 HOH HOH F . 
IA 7 HOH 54  354 354 HOH HOH F . 
IA 7 HOH 55  355 355 HOH HOH F . 
IA 7 HOH 56  356 356 HOH HOH F . 
IA 7 HOH 57  357 357 HOH HOH F . 
IA 7 HOH 58  358 358 HOH HOH F . 
IA 7 HOH 59  359 359 HOH HOH F . 
IA 7 HOH 60  360 360 HOH HOH F . 
IA 7 HOH 61  361 361 HOH HOH F . 
IA 7 HOH 62  362 362 HOH HOH F . 
IA 7 HOH 63  363 363 HOH HOH F . 
IA 7 HOH 64  364 364 HOH HOH F . 
IA 7 HOH 65  365 365 HOH HOH F . 
IA 7 HOH 66  366 366 HOH HOH F . 
IA 7 HOH 67  367 367 HOH HOH F . 
IA 7 HOH 68  368 368 HOH HOH F . 
IA 7 HOH 69  369 369 HOH HOH F . 
IA 7 HOH 70  370 370 HOH HOH F . 
IA 7 HOH 71  371 371 HOH HOH F . 
IA 7 HOH 72  372 372 HOH HOH F . 
IA 7 HOH 73  373 373 HOH HOH F . 
IA 7 HOH 74  374 374 HOH HOH F . 
IA 7 HOH 75  375 375 HOH HOH F . 
IA 7 HOH 76  376 376 HOH HOH F . 
IA 7 HOH 77  377 377 HOH HOH F . 
IA 7 HOH 78  378 378 HOH HOH F . 
IA 7 HOH 79  379 379 HOH HOH F . 
IA 7 HOH 80  380 380 HOH HOH F . 
IA 7 HOH 81  381 381 HOH HOH F . 
IA 7 HOH 82  382 382 HOH HOH F . 
IA 7 HOH 83  383 383 HOH HOH F . 
IA 7 HOH 84  384 384 HOH HOH F . 
IA 7 HOH 85  385 385 HOH HOH F . 
IA 7 HOH 86  386 386 HOH HOH F . 
IA 7 HOH 87  387 387 HOH HOH F . 
IA 7 HOH 88  388 388 HOH HOH F . 
IA 7 HOH 89  389 389 HOH HOH F . 
IA 7 HOH 90  390 390 HOH HOH F . 
IA 7 HOH 91  391 391 HOH HOH F . 
IA 7 HOH 92  392 392 HOH HOH F . 
IA 7 HOH 93  393 393 HOH HOH F . 
IA 7 HOH 94  394 394 HOH HOH F . 
IA 7 HOH 95  395 395 HOH HOH F . 
IA 7 HOH 96  396 396 HOH HOH F . 
IA 7 HOH 97  397 397 HOH HOH F . 
IA 7 HOH 98  398 398 HOH HOH F . 
IA 7 HOH 99  399 399 HOH HOH F . 
IA 7 HOH 100 400 400 HOH HOH F . 
IA 7 HOH 101 401 401 HOH HOH F . 
IA 7 HOH 102 402 402 HOH HOH F . 
IA 7 HOH 103 403 403 HOH HOH F . 
IA 7 HOH 104 404 404 HOH HOH F . 
IA 7 HOH 105 405 405 HOH HOH F . 
IA 7 HOH 106 406 406 HOH HOH F . 
IA 7 HOH 107 407 407 HOH HOH F . 
IA 7 HOH 108 408 408 HOH HOH F . 
IA 7 HOH 109 409 409 HOH HOH F . 
IA 7 HOH 110 410 410 HOH HOH F . 
IA 7 HOH 111 411 411 HOH HOH F . 
IA 7 HOH 112 412 412 HOH HOH F . 
IA 7 HOH 113 413 413 HOH HOH F . 
IA 7 HOH 114 414 414 HOH HOH F . 
IA 7 HOH 115 415 415 HOH HOH F . 
IA 7 HOH 116 416 416 HOH HOH F . 
IA 7 HOH 117 417 417 HOH HOH F . 
IA 7 HOH 118 418 418 HOH HOH F . 
IA 7 HOH 119 419 419 HOH HOH F . 
IA 7 HOH 120 420 420 HOH HOH F . 
IA 7 HOH 121 421 421 HOH HOH F . 
IA 7 HOH 122 422 422 HOH HOH F . 
IA 7 HOH 123 423 423 HOH HOH F . 
IA 7 HOH 124 424 424 HOH HOH F . 
IA 7 HOH 125 425 425 HOH HOH F . 
IA 7 HOH 126 426 426 HOH HOH F . 
IA 7 HOH 127 427 427 HOH HOH F . 
IA 7 HOH 128 428 428 HOH HOH F . 
IA 7 HOH 129 429 429 HOH HOH F . 
IA 7 HOH 130 430 430 HOH HOH F . 
IA 7 HOH 131 431 431 HOH HOH F . 
IA 7 HOH 132 432 432 HOH HOH F . 
IA 7 HOH 133 433 433 HOH HOH F . 
IA 7 HOH 134 434 434 HOH HOH F . 
IA 7 HOH 135 435 435 HOH HOH F . 
IA 7 HOH 136 436 436 HOH HOH F . 
IA 7 HOH 137 437 437 HOH HOH F . 
IA 7 HOH 138 438 438 HOH HOH F . 
IA 7 HOH 139 439 439 HOH HOH F . 
IA 7 HOH 140 440 440 HOH HOH F . 
IA 7 HOH 141 441 441 HOH HOH F . 
IA 7 HOH 142 442 442 HOH HOH F . 
IA 7 HOH 143 443 443 HOH HOH F . 
IA 7 HOH 144 444 444 HOH HOH F . 
IA 7 HOH 145 445 445 HOH HOH F . 
IA 7 HOH 146 446 446 HOH HOH F . 
IA 7 HOH 147 447 447 HOH HOH F . 
IA 7 HOH 148 448 448 HOH HOH F . 
IA 7 HOH 149 449 449 HOH HOH F . 
IA 7 HOH 150 450 450 HOH HOH F . 
IA 7 HOH 151 451 451 HOH HOH F . 
IA 7 HOH 152 452 452 HOH HOH F . 
IA 7 HOH 153 453 453 HOH HOH F . 
IA 7 HOH 154 454 454 HOH HOH F . 
IA 7 HOH 155 455 455 HOH HOH F . 
IA 7 HOH 156 456 456 HOH HOH F . 
IA 7 HOH 157 457 457 HOH HOH F . 
IA 7 HOH 158 458 458 HOH HOH F . 
IA 7 HOH 159 459 459 HOH HOH F . 
IA 7 HOH 160 460 460 HOH HOH F . 
IA 7 HOH 161 461 461 HOH HOH F . 
IA 7 HOH 162 462 462 HOH HOH F . 
IA 7 HOH 163 463 463 HOH HOH F . 
IA 7 HOH 164 464 464 HOH HOH F . 
IA 7 HOH 165 465 465 HOH HOH F . 
IA 7 HOH 166 466 466 HOH HOH F . 
IA 7 HOH 167 467 467 HOH HOH F . 
IA 7 HOH 168 468 468 HOH HOH F . 
IA 7 HOH 169 469 469 HOH HOH F . 
JA 7 HOH 1   201 201 HOH HOH G . 
JA 7 HOH 2   202 202 HOH HOH G . 
JA 7 HOH 3   203 203 HOH HOH G . 
JA 7 HOH 4   204 204 HOH HOH G . 
JA 7 HOH 5   205 205 HOH HOH G . 
JA 7 HOH 6   206 206 HOH HOH G . 
JA 7 HOH 7   207 207 HOH HOH G . 
JA 7 HOH 8   208 208 HOH HOH G . 
JA 7 HOH 9   209 209 HOH HOH G . 
JA 7 HOH 10  210 210 HOH HOH G . 
JA 7 HOH 11  211 211 HOH HOH G . 
JA 7 HOH 12  212 212 HOH HOH G . 
JA 7 HOH 13  213 213 HOH HOH G . 
JA 7 HOH 14  214 214 HOH HOH G . 
JA 7 HOH 15  215 215 HOH HOH G . 
JA 7 HOH 16  216 216 HOH HOH G . 
JA 7 HOH 17  217 217 HOH HOH G . 
JA 7 HOH 18  218 218 HOH HOH G . 
JA 7 HOH 19  219 219 HOH HOH G . 
JA 7 HOH 20  220 220 HOH HOH G . 
JA 7 HOH 21  221 221 HOH HOH G . 
JA 7 HOH 22  222 222 HOH HOH G . 
JA 7 HOH 23  223 223 HOH HOH G . 
JA 7 HOH 24  224 224 HOH HOH G . 
JA 7 HOH 25  225 225 HOH HOH G . 
JA 7 HOH 26  226 226 HOH HOH G . 
JA 7 HOH 27  227 227 HOH HOH G . 
JA 7 HOH 28  228 228 HOH HOH G . 
JA 7 HOH 29  229 229 HOH HOH G . 
JA 7 HOH 30  230 230 HOH HOH G . 
JA 7 HOH 31  231 231 HOH HOH G . 
JA 7 HOH 32  232 232 HOH HOH G . 
JA 7 HOH 33  233 233 HOH HOH G . 
JA 7 HOH 34  234 234 HOH HOH G . 
JA 7 HOH 35  235 235 HOH HOH G . 
JA 7 HOH 36  236 236 HOH HOH G . 
JA 7 HOH 37  237 237 HOH HOH G . 
JA 7 HOH 38  238 238 HOH HOH G . 
JA 7 HOH 39  239 239 HOH HOH G . 
JA 7 HOH 40  240 240 HOH HOH G . 
JA 7 HOH 41  241 241 HOH HOH G . 
JA 7 HOH 42  242 242 HOH HOH G . 
JA 7 HOH 43  243 243 HOH HOH G . 
JA 7 HOH 44  244 244 HOH HOH G . 
JA 7 HOH 45  245 245 HOH HOH G . 
JA 7 HOH 46  246 246 HOH HOH G . 
JA 7 HOH 47  247 247 HOH HOH G . 
JA 7 HOH 48  248 248 HOH HOH G . 
JA 7 HOH 49  249 249 HOH HOH G . 
JA 7 HOH 50  250 250 HOH HOH G . 
JA 7 HOH 51  251 251 HOH HOH G . 
JA 7 HOH 52  252 252 HOH HOH G . 
JA 7 HOH 53  253 253 HOH HOH G . 
JA 7 HOH 54  254 254 HOH HOH G . 
JA 7 HOH 55  255 255 HOH HOH G . 
JA 7 HOH 56  256 256 HOH HOH G . 
JA 7 HOH 57  257 257 HOH HOH G . 
JA 7 HOH 58  258 258 HOH HOH G . 
JA 7 HOH 59  259 259 HOH HOH G . 
JA 7 HOH 60  260 260 HOH HOH G . 
JA 7 HOH 61  261 261 HOH HOH G . 
JA 7 HOH 62  262 262 HOH HOH G . 
JA 7 HOH 63  263 263 HOH HOH G . 
JA 7 HOH 64  264 264 HOH HOH G . 
JA 7 HOH 65  265 265 HOH HOH G . 
JA 7 HOH 66  266 266 HOH HOH G . 
JA 7 HOH 67  267 267 HOH HOH G . 
JA 7 HOH 68  268 268 HOH HOH G . 
JA 7 HOH 69  269 269 HOH HOH G . 
JA 7 HOH 70  270 270 HOH HOH G . 
JA 7 HOH 71  271 271 HOH HOH G . 
JA 7 HOH 72  272 272 HOH HOH G . 
JA 7 HOH 73  273 273 HOH HOH G . 
JA 7 HOH 74  274 274 HOH HOH G . 
JA 7 HOH 75  275 275 HOH HOH G . 
JA 7 HOH 76  276 276 HOH HOH G . 
JA 7 HOH 77  277 277 HOH HOH G . 
JA 7 HOH 78  278 278 HOH HOH G . 
JA 7 HOH 79  279 279 HOH HOH G . 
JA 7 HOH 80  280 280 HOH HOH G . 
KA 7 HOH 1   301 301 HOH HOH H . 
KA 7 HOH 2   302 302 HOH HOH H . 
KA 7 HOH 3   303 303 HOH HOH H . 
KA 7 HOH 4   304 304 HOH HOH H . 
KA 7 HOH 5   305 305 HOH HOH H . 
KA 7 HOH 6   306 306 HOH HOH H . 
KA 7 HOH 7   307 307 HOH HOH H . 
KA 7 HOH 8   308 308 HOH HOH H . 
KA 7 HOH 9   309 309 HOH HOH H . 
KA 7 HOH 10  310 310 HOH HOH H . 
KA 7 HOH 11  311 311 HOH HOH H . 
KA 7 HOH 12  312 312 HOH HOH H . 
KA 7 HOH 13  313 313 HOH HOH H . 
KA 7 HOH 14  314 314 HOH HOH H . 
KA 7 HOH 15  315 315 HOH HOH H . 
KA 7 HOH 16  316 316 HOH HOH H . 
KA 7 HOH 17  317 317 HOH HOH H . 
KA 7 HOH 18  318 318 HOH HOH H . 
KA 7 HOH 19  319 319 HOH HOH H . 
KA 7 HOH 20  320 320 HOH HOH H . 
KA 7 HOH 21  321 321 HOH HOH H . 
KA 7 HOH 22  322 322 HOH HOH H . 
KA 7 HOH 23  323 323 HOH HOH H . 
KA 7 HOH 24  324 324 HOH HOH H . 
KA 7 HOH 25  325 325 HOH HOH H . 
KA 7 HOH 26  326 326 HOH HOH H . 
KA 7 HOH 27  327 327 HOH HOH H . 
KA 7 HOH 28  328 328 HOH HOH H . 
KA 7 HOH 29  329 329 HOH HOH H . 
KA 7 HOH 30  330 330 HOH HOH H . 
KA 7 HOH 31  331 331 HOH HOH H . 
KA 7 HOH 32  332 332 HOH HOH H . 
KA 7 HOH 33  333 333 HOH HOH H . 
KA 7 HOH 34  334 334 HOH HOH H . 
KA 7 HOH 35  335 335 HOH HOH H . 
KA 7 HOH 36  336 336 HOH HOH H . 
KA 7 HOH 37  337 337 HOH HOH H . 
KA 7 HOH 38  338 338 HOH HOH H . 
KA 7 HOH 39  339 339 HOH HOH H . 
KA 7 HOH 40  340 340 HOH HOH H . 
KA 7 HOH 41  341 341 HOH HOH H . 
KA 7 HOH 42  342 342 HOH HOH H . 
KA 7 HOH 43  343 343 HOH HOH H . 
KA 7 HOH 44  344 344 HOH HOH H . 
KA 7 HOH 45  345 345 HOH HOH H . 
KA 7 HOH 46  346 346 HOH HOH H . 
KA 7 HOH 47  347 347 HOH HOH H . 
KA 7 HOH 48  348 348 HOH HOH H . 
KA 7 HOH 49  349 349 HOH HOH H . 
KA 7 HOH 50  350 350 HOH HOH H . 
KA 7 HOH 51  351 351 HOH HOH H . 
KA 7 HOH 52  352 352 HOH HOH H . 
KA 7 HOH 53  353 353 HOH HOH H . 
KA 7 HOH 54  354 354 HOH HOH H . 
KA 7 HOH 55  355 355 HOH HOH H . 
KA 7 HOH 56  356 356 HOH HOH H . 
KA 7 HOH 57  357 357 HOH HOH H . 
KA 7 HOH 58  358 358 HOH HOH H . 
KA 7 HOH 59  359 359 HOH HOH H . 
KA 7 HOH 60  360 360 HOH HOH H . 
KA 7 HOH 61  361 361 HOH HOH H . 
KA 7 HOH 62  362 362 HOH HOH H . 
KA 7 HOH 63  363 363 HOH HOH H . 
KA 7 HOH 64  364 364 HOH HOH H . 
KA 7 HOH 65  365 365 HOH HOH H . 
KA 7 HOH 66  366 366 HOH HOH H . 
KA 7 HOH 67  367 367 HOH HOH H . 
KA 7 HOH 68  368 368 HOH HOH H . 
KA 7 HOH 69  369 369 HOH HOH H . 
KA 7 HOH 70  370 370 HOH HOH H . 
KA 7 HOH 71  371 371 HOH HOH H . 
KA 7 HOH 72  372 372 HOH HOH H . 
KA 7 HOH 73  373 373 HOH HOH H . 
KA 7 HOH 74  374 374 HOH HOH H . 
KA 7 HOH 75  375 375 HOH HOH H . 
KA 7 HOH 76  376 376 HOH HOH H . 
KA 7 HOH 77  377 377 HOH HOH H . 
KA 7 HOH 78  378 378 HOH HOH H . 
KA 7 HOH 79  379 379 HOH HOH H . 
KA 7 HOH 80  380 380 HOH HOH H . 
KA 7 HOH 81  381 381 HOH HOH H . 
KA 7 HOH 82  382 382 HOH HOH H . 
KA 7 HOH 83  383 383 HOH HOH H . 
KA 7 HOH 84  384 384 HOH HOH H . 
KA 7 HOH 85  385 385 HOH HOH H . 
KA 7 HOH 86  386 386 HOH HOH H . 
KA 7 HOH 87  387 387 HOH HOH H . 
KA 7 HOH 88  388 388 HOH HOH H . 
KA 7 HOH 89  389 389 HOH HOH H . 
KA 7 HOH 90  390 390 HOH HOH H . 
KA 7 HOH 91  391 391 HOH HOH H . 
KA 7 HOH 92  392 392 HOH HOH H . 
KA 7 HOH 93  393 393 HOH HOH H . 
KA 7 HOH 94  394 394 HOH HOH H . 
KA 7 HOH 95  395 395 HOH HOH H . 
KA 7 HOH 96  396 396 HOH HOH H . 
KA 7 HOH 97  397 397 HOH HOH H . 
KA 7 HOH 98  398 398 HOH HOH H . 
KA 7 HOH 99  399 399 HOH HOH H . 
KA 7 HOH 100 400 400 HOH HOH H . 
KA 7 HOH 101 401 401 HOH HOH H . 
KA 7 HOH 102 402 402 HOH HOH H . 
KA 7 HOH 103 403 403 HOH HOH H . 
KA 7 HOH 104 404 404 HOH HOH H . 
KA 7 HOH 105 405 405 HOH HOH H . 
KA 7 HOH 106 406 406 HOH HOH H . 
KA 7 HOH 107 407 407 HOH HOH H . 
KA 7 HOH 108 408 408 HOH HOH H . 
KA 7 HOH 109 409 409 HOH HOH H . 
KA 7 HOH 110 410 410 HOH HOH H . 
KA 7 HOH 111 411 411 HOH HOH H . 
KA 7 HOH 112 412 412 HOH HOH H . 
KA 7 HOH 113 413 413 HOH HOH H . 
KA 7 HOH 114 414 414 HOH HOH H . 
KA 7 HOH 115 415 415 HOH HOH H . 
KA 7 HOH 116 416 416 HOH HOH H . 
KA 7 HOH 117 417 417 HOH HOH H . 
KA 7 HOH 118 418 418 HOH HOH H . 
KA 7 HOH 119 419 419 HOH HOH H . 
KA 7 HOH 120 420 420 HOH HOH H . 
KA 7 HOH 121 421 421 HOH HOH H . 
KA 7 HOH 122 422 422 HOH HOH H . 
KA 7 HOH 123 423 423 HOH HOH H . 
KA 7 HOH 124 424 424 HOH HOH H . 
LA 7 HOH 1   301 301 HOH HOH I . 
LA 7 HOH 2   302 302 HOH HOH I . 
LA 7 HOH 3   303 303 HOH HOH I . 
LA 7 HOH 4   304 304 HOH HOH I . 
LA 7 HOH 5   305 305 HOH HOH I . 
LA 7 HOH 6   306 306 HOH HOH I . 
LA 7 HOH 7   307 307 HOH HOH I . 
LA 7 HOH 8   308 308 HOH HOH I . 
LA 7 HOH 9   309 309 HOH HOH I . 
LA 7 HOH 10  310 310 HOH HOH I . 
LA 7 HOH 11  311 311 HOH HOH I . 
LA 7 HOH 12  312 312 HOH HOH I . 
LA 7 HOH 13  313 313 HOH HOH I . 
LA 7 HOH 14  314 314 HOH HOH I . 
LA 7 HOH 15  315 315 HOH HOH I . 
LA 7 HOH 16  316 316 HOH HOH I . 
LA 7 HOH 17  317 317 HOH HOH I . 
LA 7 HOH 18  318 318 HOH HOH I . 
LA 7 HOH 19  319 319 HOH HOH I . 
LA 7 HOH 20  320 320 HOH HOH I . 
LA 7 HOH 21  321 321 HOH HOH I . 
LA 7 HOH 22  322 322 HOH HOH I . 
LA 7 HOH 23  323 323 HOH HOH I . 
LA 7 HOH 24  324 324 HOH HOH I . 
LA 7 HOH 25  325 325 HOH HOH I . 
LA 7 HOH 26  326 326 HOH HOH I . 
LA 7 HOH 27  327 327 HOH HOH I . 
LA 7 HOH 28  328 328 HOH HOH I . 
LA 7 HOH 29  329 329 HOH HOH I . 
LA 7 HOH 30  330 330 HOH HOH I . 
LA 7 HOH 31  331 331 HOH HOH I . 
LA 7 HOH 32  332 332 HOH HOH I . 
LA 7 HOH 33  333 333 HOH HOH I . 
LA 7 HOH 34  334 334 HOH HOH I . 
LA 7 HOH 35  335 335 HOH HOH I . 
LA 7 HOH 36  336 336 HOH HOH I . 
LA 7 HOH 37  337 337 HOH HOH I . 
LA 7 HOH 38  338 338 HOH HOH I . 
LA 7 HOH 39  339 339 HOH HOH I . 
LA 7 HOH 40  340 340 HOH HOH I . 
LA 7 HOH 41  341 341 HOH HOH I . 
LA 7 HOH 42  342 342 HOH HOH I . 
LA 7 HOH 43  343 343 HOH HOH I . 
LA 7 HOH 44  344 344 HOH HOH I . 
LA 7 HOH 45  345 345 HOH HOH I . 
LA 7 HOH 46  346 346 HOH HOH I . 
LA 7 HOH 47  347 347 HOH HOH I . 
LA 7 HOH 48  348 348 HOH HOH I . 
LA 7 HOH 49  349 349 HOH HOH I . 
LA 7 HOH 50  350 350 HOH HOH I . 
LA 7 HOH 51  351 351 HOH HOH I . 
LA 7 HOH 52  352 352 HOH HOH I . 
LA 7 HOH 53  353 353 HOH HOH I . 
LA 7 HOH 54  354 354 HOH HOH I . 
LA 7 HOH 55  355 355 HOH HOH I . 
LA 7 HOH 56  356 356 HOH HOH I . 
LA 7 HOH 57  357 357 HOH HOH I . 
LA 7 HOH 58  358 358 HOH HOH I . 
LA 7 HOH 59  359 359 HOH HOH I . 
LA 7 HOH 60  360 360 HOH HOH I . 
LA 7 HOH 61  361 361 HOH HOH I . 
LA 7 HOH 62  362 362 HOH HOH I . 
LA 7 HOH 63  363 363 HOH HOH I . 
LA 7 HOH 64  364 364 HOH HOH I . 
LA 7 HOH 65  365 365 HOH HOH I . 
LA 7 HOH 66  366 366 HOH HOH I . 
LA 7 HOH 67  367 367 HOH HOH I . 
LA 7 HOH 68  368 368 HOH HOH I . 
LA 7 HOH 69  369 369 HOH HOH I . 
LA 7 HOH 70  370 370 HOH HOH I . 
LA 7 HOH 71  371 371 HOH HOH I . 
LA 7 HOH 72  372 372 HOH HOH I . 
LA 7 HOH 73  373 373 HOH HOH I . 
LA 7 HOH 74  374 374 HOH HOH I . 
LA 7 HOH 75  375 375 HOH HOH I . 
LA 7 HOH 76  376 376 HOH HOH I . 
LA 7 HOH 77  377 377 HOH HOH I . 
LA 7 HOH 78  378 378 HOH HOH I . 
LA 7 HOH 79  379 379 HOH HOH I . 
LA 7 HOH 80  380 380 HOH HOH I . 
MA 7 HOH 1   301 301 HOH HOH J . 
MA 7 HOH 2   302 302 HOH HOH J . 
MA 7 HOH 3   303 303 HOH HOH J . 
MA 7 HOH 4   304 304 HOH HOH J . 
MA 7 HOH 5   305 305 HOH HOH J . 
MA 7 HOH 6   306 306 HOH HOH J . 
MA 7 HOH 7   307 307 HOH HOH J . 
MA 7 HOH 8   308 308 HOH HOH J . 
MA 7 HOH 9   309 309 HOH HOH J . 
MA 7 HOH 10  310 310 HOH HOH J . 
MA 7 HOH 11  311 311 HOH HOH J . 
MA 7 HOH 12  312 312 HOH HOH J . 
MA 7 HOH 13  313 313 HOH HOH J . 
MA 7 HOH 14  314 314 HOH HOH J . 
MA 7 HOH 15  315 315 HOH HOH J . 
MA 7 HOH 16  316 316 HOH HOH J . 
MA 7 HOH 17  317 317 HOH HOH J . 
MA 7 HOH 18  318 318 HOH HOH J . 
MA 7 HOH 19  319 319 HOH HOH J . 
MA 7 HOH 20  320 320 HOH HOH J . 
MA 7 HOH 21  321 321 HOH HOH J . 
MA 7 HOH 22  322 322 HOH HOH J . 
MA 7 HOH 23  323 323 HOH HOH J . 
MA 7 HOH 24  324 324 HOH HOH J . 
MA 7 HOH 25  325 325 HOH HOH J . 
MA 7 HOH 26  326 326 HOH HOH J . 
MA 7 HOH 27  327 327 HOH HOH J . 
MA 7 HOH 28  328 328 HOH HOH J . 
MA 7 HOH 29  329 329 HOH HOH J . 
MA 7 HOH 30  330 330 HOH HOH J . 
MA 7 HOH 31  331 331 HOH HOH J . 
MA 7 HOH 32  332 332 HOH HOH J . 
MA 7 HOH 33  333 333 HOH HOH J . 
MA 7 HOH 34  334 334 HOH HOH J . 
MA 7 HOH 35  335 335 HOH HOH J . 
MA 7 HOH 36  336 336 HOH HOH J . 
MA 7 HOH 37  337 337 HOH HOH J . 
MA 7 HOH 38  338 338 HOH HOH J . 
MA 7 HOH 39  339 339 HOH HOH J . 
MA 7 HOH 40  340 340 HOH HOH J . 
MA 7 HOH 41  341 341 HOH HOH J . 
MA 7 HOH 42  342 342 HOH HOH J . 
MA 7 HOH 43  343 343 HOH HOH J . 
MA 7 HOH 44  344 344 HOH HOH J . 
MA 7 HOH 45  345 345 HOH HOH J . 
MA 7 HOH 46  346 346 HOH HOH J . 
MA 7 HOH 47  347 347 HOH HOH J . 
MA 7 HOH 48  348 348 HOH HOH J . 
MA 7 HOH 49  349 349 HOH HOH J . 
MA 7 HOH 50  350 350 HOH HOH J . 
MA 7 HOH 51  351 351 HOH HOH J . 
MA 7 HOH 52  352 352 HOH HOH J . 
MA 7 HOH 53  353 353 HOH HOH J . 
MA 7 HOH 54  354 354 HOH HOH J . 
MA 7 HOH 55  355 355 HOH HOH J . 
MA 7 HOH 56  356 356 HOH HOH J . 
MA 7 HOH 57  357 357 HOH HOH J . 
MA 7 HOH 58  358 358 HOH HOH J . 
MA 7 HOH 59  359 359 HOH HOH J . 
MA 7 HOH 60  360 360 HOH HOH J . 
MA 7 HOH 61  361 361 HOH HOH J . 
MA 7 HOH 62  362 362 HOH HOH J . 
MA 7 HOH 63  363 363 HOH HOH J . 
MA 7 HOH 64  364 364 HOH HOH J . 
MA 7 HOH 65  365 365 HOH HOH J . 
MA 7 HOH 66  366 366 HOH HOH J . 
MA 7 HOH 67  367 367 HOH HOH J . 
MA 7 HOH 68  368 368 HOH HOH J . 
MA 7 HOH 69  369 369 HOH HOH J . 
MA 7 HOH 70  370 370 HOH HOH J . 
MA 7 HOH 71  371 371 HOH HOH J . 
MA 7 HOH 72  372 372 HOH HOH J . 
MA 7 HOH 73  373 373 HOH HOH J . 
MA 7 HOH 74  374 374 HOH HOH J . 
MA 7 HOH 75  375 375 HOH HOH J . 
MA 7 HOH 76  376 376 HOH HOH J . 
MA 7 HOH 77  377 377 HOH HOH J . 
MA 7 HOH 78  378 378 HOH HOH J . 
MA 7 HOH 79  379 379 HOH HOH J . 
MA 7 HOH 80  380 380 HOH HOH J . 
MA 7 HOH 81  381 381 HOH HOH J . 
MA 7 HOH 82  382 382 HOH HOH J . 
MA 7 HOH 83  383 383 HOH HOH J . 
MA 7 HOH 84  384 384 HOH HOH J . 
MA 7 HOH 85  385 385 HOH HOH J . 
MA 7 HOH 86  386 386 HOH HOH J . 
MA 7 HOH 87  387 387 HOH HOH J . 
MA 7 HOH 88  388 388 HOH HOH J . 
MA 7 HOH 89  389 389 HOH HOH J . 
MA 7 HOH 90  390 390 HOH HOH J . 
MA 7 HOH 91  391 391 HOH HOH J . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_and_software_defined_assembly PISA dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,K,L,M,N,O,P,DA,EA 
2 1 C,D,Q,R,S,T,U,V,FA,GA 
3 1 E,F,W,X,Y,Z,HA,IA     
4 1 G,H,AA,JA,KA          
5 1 I,J,BA,CA,LA,MA       
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2110  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  14050 ? 
2 'ABSA (A^2)' 2040  ? 
2 MORE         -14   ? 
2 'SSA (A^2)'  14210 ? 
3 'ABSA (A^2)' 1540  ? 
3 MORE         -12   ? 
3 'SSA (A^2)'  14190 ? 
4 'ABSA (A^2)' 1570  ? 
4 MORE         -11   ? 
4 'SSA (A^2)'  12810 ? 
5 'ABSA (A^2)' 1430  ? 
5 MORE         -10   ? 
5 'SSA (A^2)'  14100 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 72 ? A HIS 71 ? 1_555 104.1 ? 
2  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 112.2 ? 
3  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 122.3 ? 
4  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 107.2 ? 
5  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 90.3  ? 
6  ND1 ? A HIS 81 ? A HIS 80 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 84 ? A ASP 83 ? 1_555 118.0 ? 
7  ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? O  ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 108.4 ? 
8  ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? O  ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 109.8 ? 
9  ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? O  ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 121.7 ? 
10 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? O  ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 111.3 ? 
11 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? O  ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 92.9  ? 
12 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 ZN ? O  ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 111.6 ? 
13 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 72 ? C HIS 71 ? 1_555 96.8  ? 
14 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 81 ? C HIS 80 ? 1_555 116.5 ? 
15 ND1 ? C HIS 72 ? C HIS 71 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 81 ? C HIS 80 ? 1_555 124.8 ? 
16 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 84 ? C ASP 83 ? 1_555 93.8  ? 
17 ND1 ? C HIS 72 ? C HIS 71 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 84 ? C ASP 83 ? 1_555 89.5  ? 
18 ND1 ? C HIS 81 ? C HIS 80 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 84 ? C ASP 83 ? 1_555 127.3 ? 
19 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 106.7 ? 
20 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 112.6 ? 
21 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 121.9 ? 
22 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 107.0 ? 
23 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 96.1  ? 
24 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 84 ? D ASP 83 ? 1_555 110.6 ? 
25 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? W  ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 102.5 ? 
26 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? W  ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 120.5 ? 
27 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 ZN ? W  ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 111.1 ? 
28 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? W  ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 109.1 ? 
29 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 ZN ? W  ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 98.7  ? 
30 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 ZN ? W  ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 84 ? E ASP 83 ? 1_555 112.3 ? 
31 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? Y  ZN . ? F ZN 202 ? 1_555 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 108.5 ? 
32 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? Y  ZN . ? F ZN 202 ? 1_555 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 106.9 ? 
33 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 ZN ? Y  ZN . ? F ZN 202 ? 1_555 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 120.7 ? 
34 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? Y  ZN . ? F ZN 202 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 109.9 ? 
35 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 ZN ? Y  ZN . ? F ZN 202 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 92.1  ? 
36 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 ZN ? Y  ZN . ? F ZN 202 ? 1_555 OD1 ? F ASP 84 ? F ASP 83 ? 1_555 117.9 ? 
37 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? AA ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 72 ? H HIS 71 ? 1_555 99.8  ? 
38 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? AA ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 81 ? H HIS 80 ? 1_555 107.1 ? 
39 ND1 ? H HIS 72 ? H HIS 71 ? 1_555 ZN ? AA ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 81 ? H HIS 80 ? 1_555 128.2 ? 
40 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? AA ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 84 ? H ASP 83 ? 1_555 110.1 ? 
41 ND1 ? H HIS 72 ? H HIS 71 ? 1_555 ZN ? AA ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 84 ? H ASP 83 ? 1_555 99.0  ? 
42 ND1 ? H HIS 81 ? H HIS 80 ? 1_555 ZN ? AA ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 84 ? H ASP 83 ? 1_555 111.4 ? 
43 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 95.4  ? 
44 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 108.5 ? 
45 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 112.5 ? 
46 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 112.7 ? 
47 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 121.8 ? 
48 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 84 ? I ASP 83 ? 1_555 105.5 ? 
49 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? CA ZN . ? J ZN 201 ? 1_555 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 106.3 ? 
50 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? CA ZN . ? J ZN 201 ? 1_555 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 111.4 ? 
51 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 ZN ? CA ZN . ? J ZN 201 ? 1_555 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 128.8 ? 
52 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? CA ZN . ? J ZN 201 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 97.6  ? 
53 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 ZN ? CA ZN . ? J ZN 201 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 95.2  ? 
54 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 ZN ? CA ZN . ? J ZN 201 ? 1_555 OD1 ? J ASP 84 ? J ASP 83 ? 1_555 112.4 ? 
# 
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 2019-07-17 
2 'Structure model' 1 1 2019-08-14 
# 
_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' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
4 2 'Structure model' '_citation.year'           
5 2 'Structure model' '_citation_author.name'    
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .        4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 SG B CYS 111 ? ? S1 A S4P 204 ? ? 1.76 
2 1 SG F CYS 111 ? ? S1 F S4P 203 ? ? 1.94 
3 1 SG A CYS 111 ? ? S4 A S4P 204 ? ? 2.01 
4 1 SG C CYS 111 ? ? S4 C S4P 203 ? ? 2.07 
5 1 OG C SER 107 ? ? O  C HOH 301 ? ? 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 F HOH 469 ? ? 1_555 O F HOH 469 ? ? 3_555 1.91 
2 1 O C HOH 407 ? ? 1_555 O D HOH 434 ? ? 4_575 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 B SER 142 ? ? OG B SER 142 ? ? 1.311 1.418 -0.107 0.013 N 
2 1 CB C ASP 109 ? ? CG C ASP 109 ? ? 1.640 1.513 0.127  0.021 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 ASP 11  ? ? CG A ASP 11  ? ? OD1 A ASP 11  ? ? 124.10 118.30 5.80   0.90 N 
2  1 CB  A ASP 83  ? ? CG A ASP 83  ? ? OD1 A ASP 83  ? ? 112.56 118.30 -5.74  0.90 N 
3  1 CB  A ASP 83  ? ? CG A ASP 83  ? ? OD2 A ASP 83  ? ? 125.52 118.30 7.22   0.90 N 
4  1 CB  A ASP 109 ? ? CG A ASP 109 ? ? OD2 A ASP 109 ? ? 110.71 118.30 -7.59  0.90 N 
5  1 CB  A ASP 124 ? ? CG A ASP 124 ? ? OD1 A ASP 124 ? ? 124.68 118.30 6.38   0.90 N 
6  1 CB  B ASP 90  ? ? CG B ASP 90  ? ? OD1 B ASP 90  ? ? 124.94 118.30 6.64   0.90 N 
7  1 NE  B ARG 115 ? ? CZ B ARG 115 ? ? NH1 B ARG 115 ? ? 124.01 120.30 3.71   0.50 N 
8  1 CA  B SER 142 ? ? CB B SER 142 ? ? OG  B SER 142 ? ? 93.27  111.20 -17.93 2.70 N 
9  1 CB  C LEU 67  ? ? CG C LEU 67  ? ? CD1 C LEU 67  ? ? 121.66 111.00 10.66  1.70 N 
10 1 CB  C LEU 67  ? ? CG C LEU 67  ? ? CD2 C LEU 67  ? ? 97.25  111.00 -13.75 1.70 N 
11 1 NE  C ARG 79  ? ? CZ C ARG 79  ? ? NH1 C ARG 79  ? ? 123.46 120.30 3.16   0.50 N 
12 1 NE  C ARG 79  ? ? CZ C ARG 79  ? ? NH2 C ARG 79  ? ? 116.81 120.30 -3.49  0.50 N 
13 1 NE  C ARG 115 ? ? CZ C ARG 115 ? ? NH1 C ARG 115 ? ? 124.74 120.30 4.44   0.50 N 
14 1 CG1 C ILE 151 ? ? CB C ILE 151 ? ? CG2 C ILE 151 ? ? 97.74  111.40 -13.66 2.20 N 
15 1 NE  D ARG 115 ? ? CZ D ARG 115 ? ? NH1 D ARG 115 ? ? 125.12 120.30 4.82   0.50 N 
16 1 CB  D ASP 124 ? ? CG D ASP 124 ? ? OD1 D ASP 124 ? ? 125.33 118.30 7.03   0.90 N 
17 1 CB  D ASP 125 ? ? CG D ASP 125 ? ? OD1 D ASP 125 ? ? 125.94 118.30 7.64   0.90 N 
18 1 CB  D ASP 125 ? ? CG D ASP 125 ? ? OD2 D ASP 125 ? ? 110.32 118.30 -7.98  0.90 N 
19 1 CB  E ASP 109 ? ? CG E ASP 109 ? ? OD1 E ASP 109 ? ? 125.35 118.30 7.05   0.90 N 
20 1 NE  E ARG 115 ? ? CZ E ARG 115 ? ? NH1 E ARG 115 ? ? 124.49 120.30 4.19   0.50 N 
21 1 CD  F LYS 122 ? ? CE F LYS 122 ? ? NZ  F LYS 122 ? ? 97.89  111.70 -13.81 2.30 N 
22 1 CB  G ASP 90  ? ? CG G ASP 90  ? ? OD1 G ASP 90  ? ? 124.32 118.30 6.02   0.90 N 
23 1 NE  G ARG 115 ? ? CZ G ARG 115 ? ? NH1 G ARG 115 ? ? 124.73 120.30 4.43   0.50 N 
24 1 NE  G ARG 143 ? ? CZ G ARG 143 ? ? NH1 G ARG 143 ? ? 123.61 120.30 3.31   0.50 N 
25 1 NE  H ARG 115 ? ? CZ H ARG 115 ? ? NH1 H ARG 115 ? ? 124.44 120.30 4.14   0.50 N 
26 1 CB  I ASP 52  ? ? CG I ASP 52  ? ? OD1 I ASP 52  ? ? 124.38 118.30 6.08   0.90 N 
27 1 CB  I ASP 52  ? ? CG I ASP 52  ? ? OD2 I ASP 52  ? ? 111.15 118.30 -7.15  0.90 N 
28 1 CB  I ASP 96  ? ? CG I ASP 96  ? ? OD1 I ASP 96  ? ? 124.29 118.30 5.99   0.90 N 
29 1 NE  I ARG 115 ? ? CZ I ARG 115 ? ? NH1 I ARG 115 ? ? 124.46 120.30 4.16   0.50 N 
30 1 NE  I ARG 115 ? ? CZ I ARG 115 ? ? NH2 I ARG 115 ? ? 114.73 120.30 -5.57  0.50 N 
31 1 NE  I ARG 143 ? ? CZ I ARG 143 ? ? NH2 I ARG 143 ? ? 116.96 120.30 -3.34  0.50 N 
32 1 CB  J ASP 125 ? ? CG J ASP 125 ? ? OD1 J ASP 125 ? ? 123.98 118.30 5.68   0.90 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 ASP A 90  ? ? -75.41  -164.52 
2  1 ASN B 65  ? ? -144.70 58.75   
3  1 ASN C 65  ? ? -149.48 54.36   
4  1 LYS C 128 ? ? -106.81 44.72   
5  1 ASN E 65  ? ? -150.65 72.83   
6  1 SER E 68  ? ? 39.08   58.13   
7  1 THR E 137 ? ? -140.86 -11.73  
8  1 SER F 68  ? ? 32.35   65.87   
9  1 ASN G 65  ? ? -117.86 72.16   
10 1 VAL G 81  ? ? -55.49  -77.31  
11 1 ASP G 90  ? ? -62.87  -172.80 
12 1 SER G 107 ? ? -177.80 -171.48 
13 1 HIS G 110 ? ? -92.24  39.20   
14 1 SER H 68  ? ? 37.41   50.73   
15 1 GLU I 40  ? ? -35.88  133.53  
16 1 ASP I 90  ? ? -69.80  -176.51 
17 1 ASN I 131 ? ? -45.83  177.26  
18 1 ALA J 55  ? ? -106.37 46.09   
19 1 ASP J 83  ? ? -68.30  95.66   
20 1 SER J 98  ? ? -161.88 111.93  
# 
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 411 ? 6.19 .    
2  1 O ? C HOH 430 ? 5.93 .    
3  1 O ? C HOH 431 ? 5.84 .    
4  1 O ? C HOH 432 ? 6.77 .    
5  1 O ? C HOH 433 ? 6.94 .    
6  1 O ? D HOH 466 ? 5.89 .    
7  1 O ? D HOH 467 ? .    5.94 
8  1 O ? D HOH 468 ? .    6.82 
9  1 O ? D HOH 469 ? 8.51 .    
10 1 O ? E HOH 413 ? 5.87 .    
11 1 O ? E HOH 416 ? 7.90 .    
12 1 O ? F HOH 468 ? 6.83 .    
13 1 O ? F HOH 469 ? 7.71 .    
14 1 O ? G HOH 280 ? 6.35 .    
15 1 O ? H HOH 422 ? 5.83 .    
16 1 O ? H HOH 423 ? 5.85 .    
17 1 O ? H HOH 424 ? 6.60 .    
18 1 O ? J HOH 390 ? 6.35 .    
19 1 O ? J HOH 391 ? 6.50 .    
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A MET 0   ? CG  ? A MET 1   CG  
2  1 Y 1 A MET 0   ? SD  ? A MET 1   SD  
3  1 Y 1 A MET 0   ? CE  ? A MET 1   CE  
4  1 Y 1 B MET 0   ? CG  ? B MET 1   CG  
5  1 Y 1 B MET 0   ? SD  ? B MET 1   SD  
6  1 Y 1 B MET 0   ? CE  ? B MET 1   CE  
7  1 Y 1 D MET 0   ? CG  ? D MET 1   CG  
8  1 Y 1 D MET 0   ? SD  ? D MET 1   SD  
9  1 Y 1 D MET 0   ? CE  ? D MET 1   CE  
10 1 Y 1 E MET 0   ? CG  ? E MET 1   CG  
11 1 Y 1 E MET 0   ? SD  ? E MET 1   SD  
12 1 Y 1 E MET 0   ? CE  ? E MET 1   CE  
13 1 Y 1 E GLU 77  ? CG  ? E GLU 78  CG  
14 1 Y 1 E GLU 77  ? CD  ? E GLU 78  CD  
15 1 Y 1 E GLU 77  ? OE1 ? E GLU 78  OE1 
16 1 Y 1 E GLU 77  ? OE2 ? E GLU 78  OE2 
17 1 Y 1 E LYS 128 ? CG  ? E LYS 129 CG  
18 1 Y 1 E LYS 128 ? CD  ? E LYS 129 CD  
19 1 Y 1 E LYS 128 ? CE  ? E LYS 129 CE  
20 1 Y 1 E LYS 128 ? NZ  ? E LYS 129 NZ  
21 1 Y 1 F MET 0   ? CG  ? F MET 1   CG  
22 1 Y 1 F MET 0   ? SD  ? F MET 1   SD  
23 1 Y 1 F MET 0   ? CE  ? F MET 1   CE  
24 1 Y 1 G LYS 23  ? CG  ? G LYS 24  CG  
25 1 Y 1 G LYS 23  ? CD  ? G LYS 24  CD  
26 1 Y 1 G LYS 23  ? CE  ? G LYS 24  CE  
27 1 Y 1 G LYS 23  ? NZ  ? G LYS 24  NZ  
28 1 Y 1 H LYS 30  ? CG  ? H LYS 31  CG  
29 1 Y 1 H LYS 30  ? CD  ? H LYS 31  CD  
30 1 Y 1 H LYS 30  ? CE  ? H LYS 31  CE  
31 1 Y 1 H LYS 30  ? NZ  ? H LYS 31  NZ  
32 1 Y 1 I MET 0   ? CG  ? I MET 1   CG  
33 1 Y 1 I MET 0   ? SD  ? I MET 1   SD  
34 1 Y 1 I MET 0   ? CE  ? I MET 1   CE  
35 1 Y 1 I LYS 9   ? CD  ? I LYS 10  CD  
36 1 Y 1 I LYS 9   ? CE  ? I LYS 10  CE  
37 1 Y 1 I LYS 9   ? NZ  ? I LYS 10  NZ  
38 1 Y 1 I GLU 132 ? CG  ? I GLU 133 CG  
39 1 Y 1 I GLU 132 ? CD  ? I GLU 133 CD  
40 1 Y 1 I GLU 132 ? OE1 ? I GLU 133 OE1 
41 1 Y 1 I GLU 132 ? OE2 ? I GLU 133 OE2 
42 1 Y 1 J MET 0   ? CG  ? J MET 1   CG  
43 1 Y 1 J MET 0   ? SD  ? J MET 1   SD  
44 1 Y 1 J MET 0   ? CE  ? J MET 1   CE  
45 1 N 1 F 6B3 201 ? C12 ? X 6B3 1   C12 
46 1 N 1 F 6B3 201 ? C9  ? X 6B3 1   C9  
47 1 N 1 F 6B3 201 ? C26 ? X 6B3 1   C26 
48 1 N 1 F 6B3 201 ? C25 ? X 6B3 1   C25 
49 1 N 1 F 6B3 201 ? C24 ? X 6B3 1   C24 
50 1 N 1 F 6B3 201 ? C23 ? X 6B3 1   C23 
51 1 N 1 F 6B3 201 ? C28 ? X 6B3 1   C28 
52 1 N 1 F 6B3 201 ? O35 ? X 6B3 1   O35 
53 1 N 1 F 6B3 201 ? O30 ? X 6B3 1   O30 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 G MET 0   ? G MET 1   
2  1 Y 1 G LEU 67  ? G LEU 68  
3  1 Y 1 G SER 68  ? G SER 69  
4  1 Y 1 G ARG 69  ? G ARG 70  
5  1 Y 1 G LYS 70  ? G LYS 71  
6  1 Y 1 G HIS 71  ? G HIS 72  
7  1 Y 1 G GLY 72  ? G GLY 73  
8  1 Y 1 G GLY 73  ? G GLY 74  
9  1 Y 1 G PRO 74  ? G PRO 75  
10 1 Y 1 G LYS 75  ? G LYS 76  
11 1 Y 1 G ASP 76  ? G ASP 77  
12 1 Y 1 G GLU 77  ? G GLU 78  
13 1 Y 1 G GLU 78  ? G GLU 79  
14 1 Y 1 G GLY 127 ? G GLY 128 
15 1 Y 1 G LYS 128 ? G LYS 129 
16 1 Y 1 G GLY 129 ? G GLY 130 
17 1 Y 1 G GLY 130 ? G GLY 131 
18 1 Y 1 G ASN 131 ? G ASN 132 
19 1 Y 1 G GLU 132 ? G GLU 133 
20 1 Y 1 G GLU 133 ? G GLU 134 
21 1 Y 1 G SER 134 ? G SER 135 
22 1 Y 1 G THR 135 ? G THR 136 
23 1 Y 1 G LYS 136 ? G LYS 137 
24 1 Y 1 G THR 137 ? G THR 138 
25 1 Y 1 G GLY 138 ? G GLY 139 
26 1 Y 1 G ASN 139 ? G ASN 140 
27 1 Y 1 G ALA 140 ? G ALA 141 
28 1 Y 1 H MET 0   ? H MET 1   
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                             ZN  
3 'DIMETHYL SULFOXIDE'                                                                   DMS 
4 GLYCEROL                                                                               GOL 
5 'Dihydrogen tetrasulfide'                                                              S4P 
6 
;2'-[(6-oxo-5,6-dihydrophenanthridin-3-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
;
6B3 
7 water                                                                                  HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
