data_5YTO
# 
_entry.id   5YTO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.299 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5YTO         
WWPDB D_1300005873 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5YTO 
_pdbx_database_status.recvd_initial_deposition_date   2017-11-19 
_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 
'Padmanabhan, B.' 1 ? 
'Manjula, R.'     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                   NE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'FEBS Lett.' 
_citation.journal_id_ASTM           FEBLAL 
_citation.journal_id_CSD            0165 
_citation.journal_id_ISSN           1873-3468 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            592 
_citation.language                  ? 
_citation.page_first                1725 
_citation.page_last                 1737 
_citation.title                     'Assessment of ligand binding at a site relevant to SOD1 oxidation and aggregation' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/1873-3468.13055 
_citation.pdbx_database_id_PubMed   29679384 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Manjula, R.'     1 ? 
primary 'Wright, G.S.A.'  2 ? 
primary 'Strange, R.W.'   3 ? 
primary 'Padmanabhan, B.' 4 ? 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5YTO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     243.941 
_cell.length_a_esd                 ? 
_cell.length_b                     243.941 
_cell.length_b_esd                 ? 
_cell.length_c                     144.775 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        120 
_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                         5YTO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                182 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 63 2 2' 
_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]'                                                19092.219 10   1.15.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                    65.409    9    ?        ? ? ? 
3 non-polymer syn GLYCEROL                                                                      92.094    3    ?        ? ? ? 
4 non-polymer syn '4-[(1~{R})-2-(naphthalen-2-ylmethylamino)-1-oxidanyl-ethyl]benzene-1,2-diol' 309.359   3    ?        ? ? ? 
5 non-polymer syn PENTASULFIDE-SULFUR                                                           160.325   3    ?        ? ? ? 
6 water       nat water                                                                         18.015    1489 ?        ? ? ? 
# 
_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       
;MKHHHHHHPMSDYDIPTTENLYFQGAMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDN
TAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEE
STKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKHHHHHHPMSDYDIPTTENLYFQGAMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDN
TAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEE
STKTGNAGSRLACGVIGIAQ
;
_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   LYS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   PRO n 
1 10  MET n 
1 11  SER n 
1 12  ASP n 
1 13  TYR n 
1 14  ASP n 
1 15  ILE n 
1 16  PRO n 
1 17  THR n 
1 18  THR n 
1 19  GLU n 
1 20  ASN n 
1 21  LEU n 
1 22  TYR n 
1 23  PHE n 
1 24  GLN n 
1 25  GLY n 
1 26  ALA n 
1 27  MET n 
1 28  ALA n 
1 29  THR n 
1 30  LYS n 
1 31  ALA n 
1 32  VAL n 
1 33  CYS n 
1 34  VAL n 
1 35  LEU n 
1 36  LYS n 
1 37  GLY n 
1 38  ASP n 
1 39  GLY n 
1 40  PRO n 
1 41  VAL n 
1 42  GLN n 
1 43  GLY n 
1 44  ILE n 
1 45  ILE n 
1 46  ASN n 
1 47  PHE n 
1 48  GLU n 
1 49  GLN n 
1 50  LYS n 
1 51  GLU n 
1 52  SER n 
1 53  ASN n 
1 54  GLY n 
1 55  PRO n 
1 56  VAL n 
1 57  LYS n 
1 58  VAL n 
1 59  TRP n 
1 60  GLY n 
1 61  SER n 
1 62  ILE n 
1 63  LYS n 
1 64  GLY n 
1 65  LEU n 
1 66  THR n 
1 67  GLU n 
1 68  GLY n 
1 69  LEU n 
1 70  HIS n 
1 71  GLY n 
1 72  PHE n 
1 73  HIS n 
1 74  VAL n 
1 75  HIS n 
1 76  GLU n 
1 77  PHE n 
1 78  GLY n 
1 79  ASP n 
1 80  ASN n 
1 81  THR n 
1 82  ALA n 
1 83  GLY n 
1 84  CYS n 
1 85  THR n 
1 86  SER n 
1 87  ALA n 
1 88  GLY n 
1 89  PRO n 
1 90  HIS n 
1 91  PHE n 
1 92  ASN n 
1 93  PRO n 
1 94  LEU n 
1 95  SER n 
1 96  ARG n 
1 97  LYS n 
1 98  HIS n 
1 99  GLY n 
1 100 GLY n 
1 101 PRO n 
1 102 LYS n 
1 103 ASP n 
1 104 GLU n 
1 105 GLU n 
1 106 ARG n 
1 107 HIS n 
1 108 VAL n 
1 109 GLY n 
1 110 ASP n 
1 111 LEU n 
1 112 GLY n 
1 113 ASN n 
1 114 VAL n 
1 115 THR n 
1 116 ALA n 
1 117 ASP n 
1 118 LYS n 
1 119 ASP n 
1 120 GLY n 
1 121 VAL n 
1 122 ALA n 
1 123 ASP n 
1 124 VAL n 
1 125 SER n 
1 126 ILE n 
1 127 GLU n 
1 128 ASP n 
1 129 SER n 
1 130 VAL n 
1 131 ILE n 
1 132 SER n 
1 133 LEU n 
1 134 SER n 
1 135 GLY n 
1 136 ASP n 
1 137 HIS n 
1 138 CYS n 
1 139 ILE n 
1 140 ILE n 
1 141 GLY n 
1 142 ARG n 
1 143 THR n 
1 144 LEU n 
1 145 VAL n 
1 146 VAL n 
1 147 HIS n 
1 148 GLU n 
1 149 LYS n 
1 150 ALA n 
1 151 ASP n 
1 152 ASP n 
1 153 LEU n 
1 154 GLY n 
1 155 LYS n 
1 156 GLY n 
1 157 GLY n 
1 158 ASN n 
1 159 GLU n 
1 160 GLU n 
1 161 SER n 
1 162 THR n 
1 163 LYS n 
1 164 THR n 
1 165 GLY n 
1 166 ASN n 
1 167 ALA n 
1 168 GLY n 
1 169 SER n 
1 170 ARG n 
1 171 LEU n 
1 172 ALA n 
1 173 CYS n 
1 174 GLY n 
1 175 VAL n 
1 176 ILE n 
1 177 GLY n 
1 178 ILE n 
1 179 ALA n 
1 180 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                   180 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_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 
_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                       pETM11 
_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 5YTO A 27 ? 180 ? P00441 1 ? 154 ? 0 153 
2  1 5YTO B 27 ? 180 ? P00441 1 ? 154 ? 0 153 
3  1 5YTO C 27 ? 180 ? P00441 1 ? 154 ? 0 153 
4  1 5YTO D 27 ? 180 ? P00441 1 ? 154 ? 0 153 
5  1 5YTO E 27 ? 180 ? P00441 1 ? 154 ? 0 153 
6  1 5YTO F 27 ? 180 ? P00441 1 ? 154 ? 0 153 
7  1 5YTO G 27 ? 180 ? P00441 1 ? 154 ? 0 153 
8  1 5YTO H 27 ? 180 ? P00441 1 ? 154 ? 0 153 
9  1 5YTO I 27 ? 180 ? P00441 1 ? 154 ? 0 153 
10 1 5YTO J 27 ? 180 ? P00441 1 ? 154 ? 0 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1  5YTO MET A 1  ? UNP P00441 ? ? 'initiating methionine' -26 1   
1  5YTO LYS A 2  ? UNP P00441 ? ? 'expression tag'        -25 2   
1  5YTO HIS A 3  ? UNP P00441 ? ? 'expression tag'        -24 3   
1  5YTO HIS A 4  ? UNP P00441 ? ? 'expression tag'        -23 4   
1  5YTO HIS A 5  ? UNP P00441 ? ? 'expression tag'        -22 5   
1  5YTO HIS A 6  ? UNP P00441 ? ? 'expression tag'        -21 6   
1  5YTO HIS A 7  ? UNP P00441 ? ? 'expression tag'        -20 7   
1  5YTO HIS A 8  ? UNP P00441 ? ? 'expression tag'        -19 8   
1  5YTO PRO A 9  ? UNP P00441 ? ? 'expression tag'        -18 9   
1  5YTO MET A 10 ? UNP P00441 ? ? 'expression tag'        -17 10  
1  5YTO SER A 11 ? UNP P00441 ? ? 'expression tag'        -16 11  
1  5YTO ASP A 12 ? UNP P00441 ? ? 'expression tag'        -15 12  
1  5YTO TYR A 13 ? UNP P00441 ? ? 'expression tag'        -14 13  
1  5YTO ASP A 14 ? UNP P00441 ? ? 'expression tag'        -13 14  
1  5YTO ILE A 15 ? UNP P00441 ? ? 'expression tag'        -12 15  
1  5YTO PRO A 16 ? UNP P00441 ? ? 'expression tag'        -11 16  
1  5YTO THR A 17 ? UNP P00441 ? ? 'expression tag'        -10 17  
1  5YTO THR A 18 ? UNP P00441 ? ? 'expression tag'        -9  18  
1  5YTO GLU A 19 ? UNP P00441 ? ? 'expression tag'        -8  19  
1  5YTO ASN A 20 ? UNP P00441 ? ? 'expression tag'        -7  20  
1  5YTO LEU A 21 ? UNP P00441 ? ? 'expression tag'        -6  21  
1  5YTO TYR A 22 ? UNP P00441 ? ? 'expression tag'        -5  22  
1  5YTO PHE A 23 ? UNP P00441 ? ? 'expression tag'        -4  23  
1  5YTO GLN A 24 ? UNP P00441 ? ? 'expression tag'        -3  24  
1  5YTO GLY A 25 ? UNP P00441 ? ? 'expression tag'        -2  25  
1  5YTO ALA A 26 ? UNP P00441 ? ? 'expression tag'        -1  26  
2  5YTO MET B 1  ? UNP P00441 ? ? 'initiating methionine' -26 27  
2  5YTO LYS B 2  ? UNP P00441 ? ? 'expression tag'        -25 28  
2  5YTO HIS B 3  ? UNP P00441 ? ? 'expression tag'        -24 29  
2  5YTO HIS B 4  ? UNP P00441 ? ? 'expression tag'        -23 30  
2  5YTO HIS B 5  ? UNP P00441 ? ? 'expression tag'        -22 31  
2  5YTO HIS B 6  ? UNP P00441 ? ? 'expression tag'        -21 32  
2  5YTO HIS B 7  ? UNP P00441 ? ? 'expression tag'        -20 33  
2  5YTO HIS B 8  ? UNP P00441 ? ? 'expression tag'        -19 34  
2  5YTO PRO B 9  ? UNP P00441 ? ? 'expression tag'        -18 35  
2  5YTO MET B 10 ? UNP P00441 ? ? 'expression tag'        -17 36  
2  5YTO SER B 11 ? UNP P00441 ? ? 'expression tag'        -16 37  
2  5YTO ASP B 12 ? UNP P00441 ? ? 'expression tag'        -15 38  
2  5YTO TYR B 13 ? UNP P00441 ? ? 'expression tag'        -14 39  
2  5YTO ASP B 14 ? UNP P00441 ? ? 'expression tag'        -13 40  
2  5YTO ILE B 15 ? UNP P00441 ? ? 'expression tag'        -12 41  
2  5YTO PRO B 16 ? UNP P00441 ? ? 'expression tag'        -11 42  
2  5YTO THR B 17 ? UNP P00441 ? ? 'expression tag'        -10 43  
2  5YTO THR B 18 ? UNP P00441 ? ? 'expression tag'        -9  44  
2  5YTO GLU B 19 ? UNP P00441 ? ? 'expression tag'        -8  45  
2  5YTO ASN B 20 ? UNP P00441 ? ? 'expression tag'        -7  46  
2  5YTO LEU B 21 ? UNP P00441 ? ? 'expression tag'        -6  47  
2  5YTO TYR B 22 ? UNP P00441 ? ? 'expression tag'        -5  48  
2  5YTO PHE B 23 ? UNP P00441 ? ? 'expression tag'        -4  49  
2  5YTO GLN B 24 ? UNP P00441 ? ? 'expression tag'        -3  50  
2  5YTO GLY B 25 ? UNP P00441 ? ? 'expression tag'        -2  51  
2  5YTO ALA B 26 ? UNP P00441 ? ? 'expression tag'        -1  52  
3  5YTO MET C 1  ? UNP P00441 ? ? 'initiating methionine' -26 53  
3  5YTO LYS C 2  ? UNP P00441 ? ? 'expression tag'        -25 54  
3  5YTO HIS C 3  ? UNP P00441 ? ? 'expression tag'        -24 55  
3  5YTO HIS C 4  ? UNP P00441 ? ? 'expression tag'        -23 56  
3  5YTO HIS C 5  ? UNP P00441 ? ? 'expression tag'        -22 57  
3  5YTO HIS C 6  ? UNP P00441 ? ? 'expression tag'        -21 58  
3  5YTO HIS C 7  ? UNP P00441 ? ? 'expression tag'        -20 59  
3  5YTO HIS C 8  ? UNP P00441 ? ? 'expression tag'        -19 60  
3  5YTO PRO C 9  ? UNP P00441 ? ? 'expression tag'        -18 61  
3  5YTO MET C 10 ? UNP P00441 ? ? 'expression tag'        -17 62  
3  5YTO SER C 11 ? UNP P00441 ? ? 'expression tag'        -16 63  
3  5YTO ASP C 12 ? UNP P00441 ? ? 'expression tag'        -15 64  
3  5YTO TYR C 13 ? UNP P00441 ? ? 'expression tag'        -14 65  
3  5YTO ASP C 14 ? UNP P00441 ? ? 'expression tag'        -13 66  
3  5YTO ILE C 15 ? UNP P00441 ? ? 'expression tag'        -12 67  
3  5YTO PRO C 16 ? UNP P00441 ? ? 'expression tag'        -11 68  
3  5YTO THR C 17 ? UNP P00441 ? ? 'expression tag'        -10 69  
3  5YTO THR C 18 ? UNP P00441 ? ? 'expression tag'        -9  70  
3  5YTO GLU C 19 ? UNP P00441 ? ? 'expression tag'        -8  71  
3  5YTO ASN C 20 ? UNP P00441 ? ? 'expression tag'        -7  72  
3  5YTO LEU C 21 ? UNP P00441 ? ? 'expression tag'        -6  73  
3  5YTO TYR C 22 ? UNP P00441 ? ? 'expression tag'        -5  74  
3  5YTO PHE C 23 ? UNP P00441 ? ? 'expression tag'        -4  75  
3  5YTO GLN C 24 ? UNP P00441 ? ? 'expression tag'        -3  76  
3  5YTO GLY C 25 ? UNP P00441 ? ? 'expression tag'        -2  77  
3  5YTO ALA C 26 ? UNP P00441 ? ? 'expression tag'        -1  78  
4  5YTO MET D 1  ? UNP P00441 ? ? 'initiating methionine' -26 79  
4  5YTO LYS D 2  ? UNP P00441 ? ? 'expression tag'        -25 80  
4  5YTO HIS D 3  ? UNP P00441 ? ? 'expression tag'        -24 81  
4  5YTO HIS D 4  ? UNP P00441 ? ? 'expression tag'        -23 82  
4  5YTO HIS D 5  ? UNP P00441 ? ? 'expression tag'        -22 83  
4  5YTO HIS D 6  ? UNP P00441 ? ? 'expression tag'        -21 84  
4  5YTO HIS D 7  ? UNP P00441 ? ? 'expression tag'        -20 85  
4  5YTO HIS D 8  ? UNP P00441 ? ? 'expression tag'        -19 86  
4  5YTO PRO D 9  ? UNP P00441 ? ? 'expression tag'        -18 87  
4  5YTO MET D 10 ? UNP P00441 ? ? 'expression tag'        -17 88  
4  5YTO SER D 11 ? UNP P00441 ? ? 'expression tag'        -16 89  
4  5YTO ASP D 12 ? UNP P00441 ? ? 'expression tag'        -15 90  
4  5YTO TYR D 13 ? UNP P00441 ? ? 'expression tag'        -14 91  
4  5YTO ASP D 14 ? UNP P00441 ? ? 'expression tag'        -13 92  
4  5YTO ILE D 15 ? UNP P00441 ? ? 'expression tag'        -12 93  
4  5YTO PRO D 16 ? UNP P00441 ? ? 'expression tag'        -11 94  
4  5YTO THR D 17 ? UNP P00441 ? ? 'expression tag'        -10 95  
4  5YTO THR D 18 ? UNP P00441 ? ? 'expression tag'        -9  96  
4  5YTO GLU D 19 ? UNP P00441 ? ? 'expression tag'        -8  97  
4  5YTO ASN D 20 ? UNP P00441 ? ? 'expression tag'        -7  98  
4  5YTO LEU D 21 ? UNP P00441 ? ? 'expression tag'        -6  99  
4  5YTO TYR D 22 ? UNP P00441 ? ? 'expression tag'        -5  100 
4  5YTO PHE D 23 ? UNP P00441 ? ? 'expression tag'        -4  101 
4  5YTO GLN D 24 ? UNP P00441 ? ? 'expression tag'        -3  102 
4  5YTO GLY D 25 ? UNP P00441 ? ? 'expression tag'        -2  103 
4  5YTO ALA D 26 ? UNP P00441 ? ? 'expression tag'        -1  104 
5  5YTO MET E 1  ? UNP P00441 ? ? 'initiating methionine' -26 105 
5  5YTO LYS E 2  ? UNP P00441 ? ? 'expression tag'        -25 106 
5  5YTO HIS E 3  ? UNP P00441 ? ? 'expression tag'        -24 107 
5  5YTO HIS E 4  ? UNP P00441 ? ? 'expression tag'        -23 108 
5  5YTO HIS E 5  ? UNP P00441 ? ? 'expression tag'        -22 109 
5  5YTO HIS E 6  ? UNP P00441 ? ? 'expression tag'        -21 110 
5  5YTO HIS E 7  ? UNP P00441 ? ? 'expression tag'        -20 111 
5  5YTO HIS E 8  ? UNP P00441 ? ? 'expression tag'        -19 112 
5  5YTO PRO E 9  ? UNP P00441 ? ? 'expression tag'        -18 113 
5  5YTO MET E 10 ? UNP P00441 ? ? 'expression tag'        -17 114 
5  5YTO SER E 11 ? UNP P00441 ? ? 'expression tag'        -16 115 
5  5YTO ASP E 12 ? UNP P00441 ? ? 'expression tag'        -15 116 
5  5YTO TYR E 13 ? UNP P00441 ? ? 'expression tag'        -14 117 
5  5YTO ASP E 14 ? UNP P00441 ? ? 'expression tag'        -13 118 
5  5YTO ILE E 15 ? UNP P00441 ? ? 'expression tag'        -12 119 
5  5YTO PRO E 16 ? UNP P00441 ? ? 'expression tag'        -11 120 
5  5YTO THR E 17 ? UNP P00441 ? ? 'expression tag'        -10 121 
5  5YTO THR E 18 ? UNP P00441 ? ? 'expression tag'        -9  122 
5  5YTO GLU E 19 ? UNP P00441 ? ? 'expression tag'        -8  123 
5  5YTO ASN E 20 ? UNP P00441 ? ? 'expression tag'        -7  124 
5  5YTO LEU E 21 ? UNP P00441 ? ? 'expression tag'        -6  125 
5  5YTO TYR E 22 ? UNP P00441 ? ? 'expression tag'        -5  126 
5  5YTO PHE E 23 ? UNP P00441 ? ? 'expression tag'        -4  127 
5  5YTO GLN E 24 ? UNP P00441 ? ? 'expression tag'        -3  128 
5  5YTO GLY E 25 ? UNP P00441 ? ? 'expression tag'        -2  129 
5  5YTO ALA E 26 ? UNP P00441 ? ? 'expression tag'        -1  130 
6  5YTO MET F 1  ? UNP P00441 ? ? 'initiating methionine' -26 131 
6  5YTO LYS F 2  ? UNP P00441 ? ? 'expression tag'        -25 132 
6  5YTO HIS F 3  ? UNP P00441 ? ? 'expression tag'        -24 133 
6  5YTO HIS F 4  ? UNP P00441 ? ? 'expression tag'        -23 134 
6  5YTO HIS F 5  ? UNP P00441 ? ? 'expression tag'        -22 135 
6  5YTO HIS F 6  ? UNP P00441 ? ? 'expression tag'        -21 136 
6  5YTO HIS F 7  ? UNP P00441 ? ? 'expression tag'        -20 137 
6  5YTO HIS F 8  ? UNP P00441 ? ? 'expression tag'        -19 138 
6  5YTO PRO F 9  ? UNP P00441 ? ? 'expression tag'        -18 139 
6  5YTO MET F 10 ? UNP P00441 ? ? 'expression tag'        -17 140 
6  5YTO SER F 11 ? UNP P00441 ? ? 'expression tag'        -16 141 
6  5YTO ASP F 12 ? UNP P00441 ? ? 'expression tag'        -15 142 
6  5YTO TYR F 13 ? UNP P00441 ? ? 'expression tag'        -14 143 
6  5YTO ASP F 14 ? UNP P00441 ? ? 'expression tag'        -13 144 
6  5YTO ILE F 15 ? UNP P00441 ? ? 'expression tag'        -12 145 
6  5YTO PRO F 16 ? UNP P00441 ? ? 'expression tag'        -11 146 
6  5YTO THR F 17 ? UNP P00441 ? ? 'expression tag'        -10 147 
6  5YTO THR F 18 ? UNP P00441 ? ? 'expression tag'        -9  148 
6  5YTO GLU F 19 ? UNP P00441 ? ? 'expression tag'        -8  149 
6  5YTO ASN F 20 ? UNP P00441 ? ? 'expression tag'        -7  150 
6  5YTO LEU F 21 ? UNP P00441 ? ? 'expression tag'        -6  151 
6  5YTO TYR F 22 ? UNP P00441 ? ? 'expression tag'        -5  152 
6  5YTO PHE F 23 ? UNP P00441 ? ? 'expression tag'        -4  153 
6  5YTO GLN F 24 ? UNP P00441 ? ? 'expression tag'        -3  154 
6  5YTO GLY F 25 ? UNP P00441 ? ? 'expression tag'        -2  155 
6  5YTO ALA F 26 ? UNP P00441 ? ? 'expression tag'        -1  156 
7  5YTO MET G 1  ? UNP P00441 ? ? 'initiating methionine' -26 157 
7  5YTO LYS G 2  ? UNP P00441 ? ? 'expression tag'        -25 158 
7  5YTO HIS G 3  ? UNP P00441 ? ? 'expression tag'        -24 159 
7  5YTO HIS G 4  ? UNP P00441 ? ? 'expression tag'        -23 160 
7  5YTO HIS G 5  ? UNP P00441 ? ? 'expression tag'        -22 161 
7  5YTO HIS G 6  ? UNP P00441 ? ? 'expression tag'        -21 162 
7  5YTO HIS G 7  ? UNP P00441 ? ? 'expression tag'        -20 163 
7  5YTO HIS G 8  ? UNP P00441 ? ? 'expression tag'        -19 164 
7  5YTO PRO G 9  ? UNP P00441 ? ? 'expression tag'        -18 165 
7  5YTO MET G 10 ? UNP P00441 ? ? 'expression tag'        -17 166 
7  5YTO SER G 11 ? UNP P00441 ? ? 'expression tag'        -16 167 
7  5YTO ASP G 12 ? UNP P00441 ? ? 'expression tag'        -15 168 
7  5YTO TYR G 13 ? UNP P00441 ? ? 'expression tag'        -14 169 
7  5YTO ASP G 14 ? UNP P00441 ? ? 'expression tag'        -13 170 
7  5YTO ILE G 15 ? UNP P00441 ? ? 'expression tag'        -12 171 
7  5YTO PRO G 16 ? UNP P00441 ? ? 'expression tag'        -11 172 
7  5YTO THR G 17 ? UNP P00441 ? ? 'expression tag'        -10 173 
7  5YTO THR G 18 ? UNP P00441 ? ? 'expression tag'        -9  174 
7  5YTO GLU G 19 ? UNP P00441 ? ? 'expression tag'        -8  175 
7  5YTO ASN G 20 ? UNP P00441 ? ? 'expression tag'        -7  176 
7  5YTO LEU G 21 ? UNP P00441 ? ? 'expression tag'        -6  177 
7  5YTO TYR G 22 ? UNP P00441 ? ? 'expression tag'        -5  178 
7  5YTO PHE G 23 ? UNP P00441 ? ? 'expression tag'        -4  179 
7  5YTO GLN G 24 ? UNP P00441 ? ? 'expression tag'        -3  180 
7  5YTO GLY G 25 ? UNP P00441 ? ? 'expression tag'        -2  181 
7  5YTO ALA G 26 ? UNP P00441 ? ? 'expression tag'        -1  182 
8  5YTO MET H 1  ? UNP P00441 ? ? 'initiating methionine' -26 183 
8  5YTO LYS H 2  ? UNP P00441 ? ? 'expression tag'        -25 184 
8  5YTO HIS H 3  ? UNP P00441 ? ? 'expression tag'        -24 185 
8  5YTO HIS H 4  ? UNP P00441 ? ? 'expression tag'        -23 186 
8  5YTO HIS H 5  ? UNP P00441 ? ? 'expression tag'        -22 187 
8  5YTO HIS H 6  ? UNP P00441 ? ? 'expression tag'        -21 188 
8  5YTO HIS H 7  ? UNP P00441 ? ? 'expression tag'        -20 189 
8  5YTO HIS H 8  ? UNP P00441 ? ? 'expression tag'        -19 190 
8  5YTO PRO H 9  ? UNP P00441 ? ? 'expression tag'        -18 191 
8  5YTO MET H 10 ? UNP P00441 ? ? 'expression tag'        -17 192 
8  5YTO SER H 11 ? UNP P00441 ? ? 'expression tag'        -16 193 
8  5YTO ASP H 12 ? UNP P00441 ? ? 'expression tag'        -15 194 
8  5YTO TYR H 13 ? UNP P00441 ? ? 'expression tag'        -14 195 
8  5YTO ASP H 14 ? UNP P00441 ? ? 'expression tag'        -13 196 
8  5YTO ILE H 15 ? UNP P00441 ? ? 'expression tag'        -12 197 
8  5YTO PRO H 16 ? UNP P00441 ? ? 'expression tag'        -11 198 
8  5YTO THR H 17 ? UNP P00441 ? ? 'expression tag'        -10 199 
8  5YTO THR H 18 ? UNP P00441 ? ? 'expression tag'        -9  200 
8  5YTO GLU H 19 ? UNP P00441 ? ? 'expression tag'        -8  201 
8  5YTO ASN H 20 ? UNP P00441 ? ? 'expression tag'        -7  202 
8  5YTO LEU H 21 ? UNP P00441 ? ? 'expression tag'        -6  203 
8  5YTO TYR H 22 ? UNP P00441 ? ? 'expression tag'        -5  204 
8  5YTO PHE H 23 ? UNP P00441 ? ? 'expression tag'        -4  205 
8  5YTO GLN H 24 ? UNP P00441 ? ? 'expression tag'        -3  206 
8  5YTO GLY H 25 ? UNP P00441 ? ? 'expression tag'        -2  207 
8  5YTO ALA H 26 ? UNP P00441 ? ? 'expression tag'        -1  208 
9  5YTO MET I 1  ? UNP P00441 ? ? 'initiating methionine' -26 209 
9  5YTO LYS I 2  ? UNP P00441 ? ? 'expression tag'        -25 210 
9  5YTO HIS I 3  ? UNP P00441 ? ? 'expression tag'        -24 211 
9  5YTO HIS I 4  ? UNP P00441 ? ? 'expression tag'        -23 212 
9  5YTO HIS I 5  ? UNP P00441 ? ? 'expression tag'        -22 213 
9  5YTO HIS I 6  ? UNP P00441 ? ? 'expression tag'        -21 214 
9  5YTO HIS I 7  ? UNP P00441 ? ? 'expression tag'        -20 215 
9  5YTO HIS I 8  ? UNP P00441 ? ? 'expression tag'        -19 216 
9  5YTO PRO I 9  ? UNP P00441 ? ? 'expression tag'        -18 217 
9  5YTO MET I 10 ? UNP P00441 ? ? 'expression tag'        -17 218 
9  5YTO SER I 11 ? UNP P00441 ? ? 'expression tag'        -16 219 
9  5YTO ASP I 12 ? UNP P00441 ? ? 'expression tag'        -15 220 
9  5YTO TYR I 13 ? UNP P00441 ? ? 'expression tag'        -14 221 
9  5YTO ASP I 14 ? UNP P00441 ? ? 'expression tag'        -13 222 
9  5YTO ILE I 15 ? UNP P00441 ? ? 'expression tag'        -12 223 
9  5YTO PRO I 16 ? UNP P00441 ? ? 'expression tag'        -11 224 
9  5YTO THR I 17 ? UNP P00441 ? ? 'expression tag'        -10 225 
9  5YTO THR I 18 ? UNP P00441 ? ? 'expression tag'        -9  226 
9  5YTO GLU I 19 ? UNP P00441 ? ? 'expression tag'        -8  227 
9  5YTO ASN I 20 ? UNP P00441 ? ? 'expression tag'        -7  228 
9  5YTO LEU I 21 ? UNP P00441 ? ? 'expression tag'        -6  229 
9  5YTO TYR I 22 ? UNP P00441 ? ? 'expression tag'        -5  230 
9  5YTO PHE I 23 ? UNP P00441 ? ? 'expression tag'        -4  231 
9  5YTO GLN I 24 ? UNP P00441 ? ? 'expression tag'        -3  232 
9  5YTO GLY I 25 ? UNP P00441 ? ? 'expression tag'        -2  233 
9  5YTO ALA I 26 ? UNP P00441 ? ? 'expression tag'        -1  234 
10 5YTO MET J 1  ? UNP P00441 ? ? 'initiating methionine' -26 235 
10 5YTO LYS J 2  ? UNP P00441 ? ? 'expression tag'        -25 236 
10 5YTO HIS J 3  ? UNP P00441 ? ? 'expression tag'        -24 237 
10 5YTO HIS J 4  ? UNP P00441 ? ? 'expression tag'        -23 238 
10 5YTO HIS J 5  ? UNP P00441 ? ? 'expression tag'        -22 239 
10 5YTO HIS J 6  ? UNP P00441 ? ? 'expression tag'        -21 240 
10 5YTO HIS J 7  ? UNP P00441 ? ? 'expression tag'        -20 241 
10 5YTO HIS J 8  ? UNP P00441 ? ? 'expression tag'        -19 242 
10 5YTO PRO J 9  ? UNP P00441 ? ? 'expression tag'        -18 243 
10 5YTO MET J 10 ? UNP P00441 ? ? 'expression tag'        -17 244 
10 5YTO SER J 11 ? UNP P00441 ? ? 'expression tag'        -16 245 
10 5YTO ASP J 12 ? UNP P00441 ? ? 'expression tag'        -15 246 
10 5YTO TYR J 13 ? UNP P00441 ? ? 'expression tag'        -14 247 
10 5YTO ASP J 14 ? UNP P00441 ? ? 'expression tag'        -13 248 
10 5YTO ILE J 15 ? UNP P00441 ? ? 'expression tag'        -12 249 
10 5YTO PRO J 16 ? UNP P00441 ? ? 'expression tag'        -11 250 
10 5YTO THR J 17 ? UNP P00441 ? ? 'expression tag'        -10 251 
10 5YTO THR J 18 ? UNP P00441 ? ? 'expression tag'        -9  252 
10 5YTO GLU J 19 ? UNP P00441 ? ? 'expression tag'        -8  253 
10 5YTO ASN J 20 ? UNP P00441 ? ? 'expression tag'        -7  254 
10 5YTO LEU J 21 ? UNP P00441 ? ? 'expression tag'        -6  255 
10 5YTO TYR J 22 ? UNP P00441 ? ? 'expression tag'        -5  256 
10 5YTO PHE J 23 ? UNP P00441 ? ? 'expression tag'        -4  257 
10 5YTO GLN J 24 ? UNP P00441 ? ? 'expression tag'        -3  258 
10 5YTO GLY J 25 ? UNP P00441 ? ? 'expression tag'        -2  259 
10 5YTO ALA J 26 ? UNP P00441 ? ? 'expression tag'        -1  260 
# 
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 
946 non-polymer         . '4-[(1~{R})-2-(naphthalen-2-ylmethylamino)-1-oxidanyl-ethyl]benzene-1,2-diol' 
'(1-(3,4-dihydroxyphenyl)-2-((naphthalen-1-ylmethyl)amino)ethan-1-one' 'C19 H19 N O3'   309.359 
ALA 'L-peptide linking' y ALANINE                                                                       ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                                      ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                    ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                               ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                      ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                     ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                               ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                                       ? 'C2 H5 N O2'     75.067  
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 
PS5 non-polymer         . PENTASULFIDE-SULFUR                                                           ? 'S5 -2'          160.325 
SER 'L-peptide linking' y SERINE                                                                        ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                                     ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                    ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                                      ? 'C9 H11 N O3'    181.189 
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                   5YTO 
_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            3.26 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         62.23 
_exptl_crystal.description                 ? 
_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    '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_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-07-22 
# 
_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   0.95372 
_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                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE BM14' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95372 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BM14 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate            23.43 
_reflns.entry_id                         5YTO 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.9 
_reflns.d_resolution_low                 50.0 
_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                       186105 
_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             99.4 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  13.5 
_reflns.pdbx_Rmerge_I_obs                0.086 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            29.5 
_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                  1.90 
_reflns_shell.d_res_low                   1.93 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.9 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           9333 
_reflns_shell.percent_possible_all        95.7 
_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                0.69 
_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             5.5 
_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]                            0.41 
_refine.aniso_B[1][2]                            0.41 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.41 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.34 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               31.585 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_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                                 5YTO 
_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                            1.90 
_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                     186105 
_refine.ls_number_reflns_R_free                  9697 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.37 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18085 
_refine.ls_R_factor_R_free                       0.21492 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17908 
_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                    ? 
_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                      1HL5 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.106 
_refine.pdbx_overall_ESU_R_Free                  0.108 
_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                             2.378 
_refine.overall_SU_ML                            0.070 
_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        10954 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         99 
_refine_hist.number_atoms_solvent             1489 
_refine_hist.number_atoms_total               12542 
_refine_hist.d_res_high                       1.90 
_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' ? 0.017  0.019  11323 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.721  1.951  15309 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.654  5.000  1536  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 40.010 25.558 466   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.508 15.000 1822  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.963 15.000 39    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.133  0.200  1693  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.021  8650  ? 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' ? ?      ?      ?     ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.900 
_refine_ls_shell.d_res_low                        1.949 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             682 
_refine_ls_shell.number_reflns_R_work             13038 
_refine_ls_shell.percent_reflns_obs               96.14 
_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                  0.288 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.250 
_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                     5YTO 
_struct.title                        
'Crystal Structure of human Superoxide Dismutase I (hSOD1) in complex with a napthalene-catechol linked compound.' 
_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        5YTO 
_struct_keywords.text            'dismutase, ligand complex, dimer, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 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 2 ? 
N  N N 3 ? 
O  N N 4 ? 
P  N N 5 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 5 ? 
T  N N 2 ? 
U  N N 4 ? 
V  N N 2 ? 
W  N N 5 ? 
X  N N 2 ? 
Y  N N 2 ? 
Z  N N 2 ? 
AA N N 4 ? 
BA N N 2 ? 
CA N N 6 ? 
DA N N 6 ? 
EA N N 6 ? 
FA N N 6 ? 
GA N N 6 ? 
HA N N 6 ? 
IA N N 6 ? 
JA N N 6 ? 
KA N N 6 ? 
LA N N 6 ? 
# 
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 82  ? GLY A 88  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  AA2 ALA B 82  ? GLY B 88  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P3  AA3 SER B 134 ? CYS B 138 ? SER B 107 CYS B 111 5 ? 5 
HELX_P HELX_P4  AA4 GLU B 160 ? GLY B 165 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P5  AA5 ALA C 82  ? GLY C 88  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6  AA6 SER C 134 ? CYS C 138 ? SER C 107 CYS C 111 5 ? 5 
HELX_P HELX_P7  AA7 GLU C 160 ? GLY C 165 ? GLU C 133 GLY C 138 1 ? 6 
HELX_P HELX_P8  AA8 ALA D 82  ? GLY D 88  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P9  AA9 ASN D 158 ? THR D 162 ? ASN D 131 THR D 135 5 ? 5 
HELX_P HELX_P10 AB1 ALA E 82  ? GLY E 88  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P11 AB2 SER E 134 ? CYS E 138 ? SER E 107 CYS E 111 5 ? 5 
HELX_P HELX_P12 AB3 GLU E 160 ? GLY E 165 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P13 AB4 ALA F 82  ? GLY F 88  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P14 AB5 ASN F 158 ? GLY F 165 ? ASN F 131 GLY F 138 1 ? 8 
HELX_P HELX_P15 AB6 ALA G 82  ? GLY G 88  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P16 AB7 GLU G 160 ? GLY G 165 ? GLU G 133 GLY G 138 1 ? 6 
HELX_P HELX_P17 AB8 ALA H 82  ? GLY H 88  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P18 AB9 SER H 134 ? CYS H 138 ? SER H 107 CYS H 111 5 ? 5 
HELX_P HELX_P19 AC1 GLU H 160 ? GLY H 165 ? GLU H 133 GLY H 138 1 ? 6 
HELX_P HELX_P20 AC2 ALA I 82  ? GLY I 88  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P21 AC3 ASN I 158 ? GLY I 165 ? ASN I 131 GLY I 138 1 ? 8 
HELX_P HELX_P22 AC4 ALA J 82  ? GLY J 88  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P23 AC5 SER J 134 ? CYS J 138 ? SER J 107 CYS J 111 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 84  SG  ? ? ? 1_555 A  CYS 173 SG ? ? A CYS 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.295 ? 
disulf2  disulf ? ? B CYS 84  SG  ? ? ? 1_555 B  CYS 173 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.252 ? 
disulf3  disulf ? ? C CYS 84  SG  ? ? ? 1_555 C  CYS 173 SG ? ? C CYS 57 C CYS 146 1_555 ? ? ? ? ? ? ? 2.219 ? 
disulf4  disulf ? ? D CYS 84  SG  ? ? ? 1_555 D  CYS 173 SG ? ? D CYS 57 D CYS 146 1_555 ? ? ? ? ? ? ? 2.249 ? 
disulf5  disulf ? ? E CYS 84  SG  ? ? ? 1_555 E  CYS 173 SG ? ? E CYS 57 E CYS 146 1_555 ? ? ? ? ? ? ? 2.233 ? 
disulf6  disulf ? ? F CYS 84  SG  ? ? ? 1_555 F  CYS 173 SG ? ? F CYS 57 F CYS 146 1_555 ? ? ? ? ? ? ? 2.207 ? 
disulf7  disulf ? ? G CYS 84  SG  ? ? ? 1_555 G  CYS 173 SG ? ? G CYS 57 G CYS 146 1_555 ? ? ? ? ? ? ? 2.136 ? 
disulf8  disulf ? ? H CYS 84  SG  ? ? ? 1_555 H  CYS 173 SG ? ? H CYS 57 H CYS 146 1_555 ? ? ? ? ? ? ? 2.157 ? 
disulf9  disulf ? ? I CYS 84  SG  ? ? ? 1_555 I  CYS 173 SG ? ? I CYS 57 I CYS 146 1_555 ? ? ? ? ? ? ? 2.189 ? 
disulf10 disulf ? ? J CYS 84  SG  ? ? ? 1_555 J  CYS 173 SG ? ? J CYS 57 J CYS 146 1_555 ? ? ? ? ? ? ? 2.218 ? 
metalc1  metalc ? ? A HIS 90  ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 63 A ZN  201 1_555 ? ? ? ? ? ? ? 2.015 ? 
metalc2  metalc ? ? A HIS 98  ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 71 A ZN  201 1_555 ? ? ? ? ? ? ? 2.289 ? 
metalc3  metalc ? ? A HIS 107 ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 80 A ZN  201 1_555 ? ? ? ? ? ? ? 2.054 ? 
metalc4  metalc ? ? A ASP 110 OD1 ? ? ? 1_555 K  ZN  .   ZN ? ? A ASP 83 A ZN  201 1_555 ? ? ? ? ? ? ? 2.005 ? 
metalc5  metalc ? ? B HIS 90  ND1 ? ? ? 1_555 M  ZN  .   ZN ? ? B HIS 63 B ZN  201 1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc6  metalc ? ? B HIS 98  ND1 ? ? ? 1_555 M  ZN  .   ZN ? ? B HIS 71 B ZN  201 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc7  metalc ? ? B HIS 107 ND1 ? ? ? 1_555 M  ZN  .   ZN ? ? B HIS 80 B ZN  201 1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc8  metalc ? ? B ASP 110 OD1 ? ? ? 1_555 M  ZN  .   ZN ? ? B ASP 83 B ZN  201 1_555 ? ? ? ? ? ? ? 1.942 ? 
metalc9  metalc ? ? C HIS 90  ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? C HIS 63 C ZN  201 1_555 ? ? ? ? ? ? ? 1.991 ? 
metalc10 metalc ? ? C HIS 98  ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? C HIS 71 C ZN  201 1_555 ? ? ? ? ? ? ? 2.162 ? 
metalc11 metalc ? ? C HIS 107 ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? C HIS 80 C ZN  201 1_555 ? ? ? ? ? ? ? 2.067 ? 
metalc12 metalc ? ? C ASP 110 OD1 ? ? ? 1_555 Q  ZN  .   ZN ? ? C ASP 83 C ZN  201 1_555 ? ? ? ? ? ? ? 1.962 ? 
metalc13 metalc ? ? D HIS 90  ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 63 D ZN  201 1_555 ? ? ? ? ? ? ? 2.286 ? 
metalc14 metalc ? ? D HIS 98  ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 71 D ZN  201 1_555 ? ? ? ? ? ? ? 2.192 ? 
metalc15 metalc ? ? D HIS 107 ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 80 D ZN  201 1_555 ? ? ? ? ? ? ? 2.020 ? 
metalc16 metalc ? ? D ASP 110 OD1 ? ? ? 1_555 T  ZN  .   ZN ? ? D ASP 83 D ZN  201 1_555 ? ? ? ? ? ? ? 1.814 ? 
metalc17 metalc ? ? E HIS 90  ND1 ? ? ? 1_555 V  ZN  .   ZN ? ? E HIS 63 E ZN  201 1_555 ? ? ? ? ? ? ? 2.044 ? 
metalc18 metalc ? ? E HIS 98  ND1 ? ? ? 1_555 V  ZN  .   ZN ? ? E HIS 71 E ZN  201 1_555 ? ? ? ? ? ? ? 2.181 ? 
metalc19 metalc ? ? E HIS 107 ND1 ? ? ? 1_555 V  ZN  .   ZN ? ? E HIS 80 E ZN  201 1_555 ? ? ? ? ? ? ? 2.010 ? 
metalc20 metalc ? ? E ASP 110 OD1 ? ? ? 1_555 V  ZN  .   ZN ? ? E ASP 83 E ZN  201 1_555 ? ? ? ? ? ? ? 1.931 ? 
metalc21 metalc ? ? F HIS 90  ND1 ? ? ? 1_555 X  ZN  .   ZN ? ? F HIS 63 F ZN  201 1_555 ? ? ? ? ? ? ? 2.168 ? 
metalc22 metalc ? ? F HIS 98  ND1 ? ? ? 1_555 X  ZN  .   ZN ? ? F HIS 71 F ZN  201 1_555 ? ? ? ? ? ? ? 2.286 ? 
metalc23 metalc ? ? F HIS 107 ND1 ? ? ? 1_555 X  ZN  .   ZN ? ? F HIS 80 F ZN  201 1_555 ? ? ? ? ? ? ? 1.886 ? 
metalc24 metalc ? ? F ASP 110 OD1 ? ? ? 1_555 X  ZN  .   ZN ? ? F ASP 83 F ZN  201 1_555 ? ? ? ? ? ? ? 1.887 ? 
metalc25 metalc ? ? G HIS 90  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? G HIS 63 G ZN  201 1_555 ? ? ? ? ? ? ? 2.119 ? 
metalc26 metalc ? ? G HIS 98  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? G HIS 71 G ZN  201 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc27 metalc ? ? G HIS 107 ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? G HIS 80 G ZN  201 1_555 ? ? ? ? ? ? ? 2.011 ? 
metalc28 metalc ? ? G ASP 110 OD1 ? ? ? 1_555 Y  ZN  .   ZN ? ? G ASP 83 G ZN  201 1_555 ? ? ? ? ? ? ? 1.984 ? 
metalc29 metalc ? ? H HIS 90  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? H HIS 63 H ZN  201 1_555 ? ? ? ? ? ? ? 1.909 ? 
metalc30 metalc ? ? H HIS 98  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? H HIS 71 H ZN  201 1_555 ? ? ? ? ? ? ? 2.211 ? 
metalc31 metalc ? ? H HIS 107 ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? H HIS 80 H ZN  201 1_555 ? ? ? ? ? ? ? 2.059 ? 
metalc32 metalc ? ? H ASP 110 OD1 ? ? ? 1_555 Z  ZN  .   ZN ? ? H ASP 83 H ZN  201 1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc33 metalc ? ? I HIS 90  ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 63 I ZN  201 1_555 ? ? ? ? ? ? ? 2.104 ? 
metalc34 metalc ? ? I HIS 98  ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 71 I ZN  201 1_555 ? ? ? ? ? ? ? 2.112 ? 
metalc35 metalc ? ? I HIS 107 ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 80 I ZN  201 1_555 ? ? ? ? ? ? ? 2.103 ? 
metalc36 metalc ? ? I ASP 110 OD1 ? ? ? 1_555 BA ZN  .   ZN ? ? I ASP 83 I ZN  201 1_555 ? ? ? ? ? ? ? 1.970 ? 
# 
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 ? 5 ? 
AB5 ? 4 ? 
AB6 ? 5 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
AB9 ? 4 ? 
AC1 ? 5 ? 
AC2 ? 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 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 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 122 ? ASP A 128 ? ALA A 95  ASP A 101 
AA1 2 VAL A 56  ? LYS A 63  ? VAL A 29  LYS A 36  
AA1 3 GLN A 42  ? GLU A 48  ? GLN A 15  GLU A 21  
AA1 4 LYS A 30  ? LEU A 35  ? LYS A 3   LEU A 8   
AA1 5 GLY A 177 ? ILE A 178 ? GLY A 150 ILE A 151 
AA2 1 ASP A 110 ? ALA A 116 ? ASP A 83  ALA A 89  
AA2 2 GLY A 68  ? HIS A 75  ? GLY A 41  HIS A 48  
AA2 3 THR A 143 ? HIS A 147 ? THR A 116 HIS A 120 
AA2 4 ARG A 170 ? VAL A 175 ? ARG A 143 VAL A 148 
AA3 1 ALA B 122 ? ASP B 128 ? ALA B 95  ASP B 101 
AA3 2 VAL B 56  ? LYS B 63  ? VAL B 29  LYS B 36  
AA3 3 GLN B 42  ? GLU B 48  ? GLN B 15  GLU B 21  
AA3 4 LYS B 30  ? LEU B 35  ? LYS B 3   LEU B 8   
AA3 5 GLY B 177 ? ILE B 178 ? GLY B 150 ILE B 151 
AA4 1 ASP B 110 ? ALA B 116 ? ASP B 83  ALA B 89  
AA4 2 GLY B 68  ? HIS B 75  ? GLY B 41  HIS B 48  
AA4 3 THR B 143 ? HIS B 147 ? THR B 116 HIS B 120 
AA4 4 ARG B 170 ? VAL B 175 ? ARG B 143 VAL B 148 
AA5 1 ALA C 122 ? ASP C 128 ? ALA C 95  ASP C 101 
AA5 2 VAL C 56  ? LYS C 63  ? VAL C 29  LYS C 36  
AA5 3 GLN C 42  ? GLU C 48  ? GLN C 15  GLU C 21  
AA5 4 LYS C 30  ? LEU C 35  ? LYS C 3   LEU C 8   
AA5 5 GLY C 177 ? ILE C 178 ? GLY C 150 ILE C 151 
AA6 1 ASP C 110 ? ALA C 116 ? ASP C 83  ALA C 89  
AA6 2 GLY C 68  ? HIS C 75  ? GLY C 41  HIS C 48  
AA6 3 THR C 143 ? HIS C 147 ? THR C 116 HIS C 120 
AA6 4 ARG C 170 ? VAL C 175 ? ARG C 143 VAL C 148 
AA7 1 ALA D 122 ? ASP D 128 ? ALA D 95  ASP D 101 
AA7 2 VAL D 56  ? LYS D 63  ? VAL D 29  LYS D 36  
AA7 3 GLN D 42  ? GLU D 48  ? GLN D 15  GLU D 21  
AA7 4 LYS D 30  ? LEU D 35  ? LYS D 3   LEU D 8   
AA7 5 GLY D 177 ? ILE D 178 ? GLY D 150 ILE D 151 
AA8 1 ASP D 110 ? ALA D 116 ? ASP D 83  ALA D 89  
AA8 2 GLY D 68  ? HIS D 75  ? GLY D 41  HIS D 48  
AA8 3 THR D 143 ? HIS D 147 ? THR D 116 HIS D 120 
AA8 4 ARG D 170 ? VAL D 175 ? ARG D 143 VAL D 148 
AA9 1 ALA E 122 ? ASP E 128 ? ALA E 95  ASP E 101 
AA9 2 VAL E 56  ? LYS E 63  ? VAL E 29  LYS E 36  
AA9 3 GLN E 42  ? GLU E 48  ? GLN E 15  GLU E 21  
AA9 4 LYS E 30  ? LEU E 35  ? LYS E 3   LEU E 8   
AA9 5 GLY E 177 ? ILE E 178 ? GLY E 150 ILE E 151 
AB1 1 ASP E 110 ? ALA E 116 ? ASP E 83  ALA E 89  
AB1 2 GLY E 68  ? HIS E 75  ? GLY E 41  HIS E 48  
AB1 3 THR E 143 ? HIS E 147 ? THR E 116 HIS E 120 
AB1 4 ARG E 170 ? VAL E 175 ? ARG E 143 VAL E 148 
AB2 1 ALA F 122 ? ASP F 128 ? ALA F 95  ASP F 101 
AB2 2 VAL F 56  ? LYS F 63  ? VAL F 29  LYS F 36  
AB2 3 GLN F 42  ? GLU F 48  ? GLN F 15  GLU F 21  
AB2 4 LYS F 30  ? LEU F 35  ? LYS F 3   LEU F 8   
AB2 5 GLY F 177 ? ILE F 178 ? GLY F 150 ILE F 151 
AB3 1 ASP F 110 ? ALA F 116 ? ASP F 83  ALA F 89  
AB3 2 GLY F 68  ? HIS F 75  ? GLY F 41  HIS F 48  
AB3 3 THR F 143 ? HIS F 147 ? THR F 116 HIS F 120 
AB3 4 ARG F 170 ? VAL F 175 ? ARG F 143 VAL F 148 
AB4 1 ALA G 122 ? ASP G 128 ? ALA G 95  ASP G 101 
AB4 2 VAL G 56  ? LYS G 63  ? VAL G 29  LYS G 36  
AB4 3 GLN G 42  ? GLU G 48  ? GLN G 15  GLU G 21  
AB4 4 LYS G 30  ? LYS G 36  ? LYS G 3   LYS G 9   
AB4 5 GLY G 177 ? ILE G 178 ? GLY G 150 ILE G 151 
AB5 1 ASP G 110 ? ALA G 116 ? ASP G 83  ALA G 89  
AB5 2 GLY G 68  ? HIS G 75  ? GLY G 41  HIS G 48  
AB5 3 THR G 143 ? HIS G 147 ? THR G 116 HIS G 120 
AB5 4 ARG G 170 ? VAL G 175 ? ARG G 143 VAL G 148 
AB6 1 ALA H 122 ? ASP H 128 ? ALA H 95  ASP H 101 
AB6 2 VAL H 56  ? LYS H 63  ? VAL H 29  LYS H 36  
AB6 3 GLN H 42  ? GLU H 48  ? GLN H 15  GLU H 21  
AB6 4 LYS H 30  ? LEU H 35  ? LYS H 3   LEU H 8   
AB6 5 GLY H 177 ? ILE H 178 ? GLY H 150 ILE H 151 
AB7 1 ASP H 110 ? ALA H 116 ? ASP H 83  ALA H 89  
AB7 2 GLY H 68  ? HIS H 75  ? GLY H 41  HIS H 48  
AB7 3 THR H 143 ? HIS H 147 ? THR H 116 HIS H 120 
AB7 4 ARG H 170 ? VAL H 175 ? ARG H 143 VAL H 148 
AB8 1 ALA I 122 ? ASP I 128 ? ALA I 95  ASP I 101 
AB8 2 VAL I 56  ? LYS I 63  ? VAL I 29  LYS I 36  
AB8 3 GLN I 42  ? GLN I 49  ? GLN I 15  GLN I 22  
AB8 4 THR I 29  ? LYS I 36  ? THR I 2   LYS I 9   
AB8 5 GLY I 177 ? ILE I 178 ? GLY I 150 ILE I 151 
AB9 1 ASP I 110 ? ALA I 116 ? ASP I 83  ALA I 89  
AB9 2 GLY I 68  ? HIS I 75  ? GLY I 41  HIS I 48  
AB9 3 THR I 143 ? HIS I 147 ? THR I 116 HIS I 120 
AB9 4 ARG I 170 ? VAL I 175 ? ARG I 143 VAL I 148 
AC1 1 ALA J 122 ? ASP J 128 ? ALA J 95  ASP J 101 
AC1 2 VAL J 56  ? LYS J 63  ? VAL J 29  LYS J 36  
AC1 3 GLN J 42  ? GLU J 48  ? GLN J 15  GLU J 21  
AC1 4 LYS J 30  ? LEU J 35  ? LYS J 3   LEU J 8   
AC1 5 GLY J 177 ? ILE J 178 ? GLY J 150 ILE J 151 
AC2 1 ASP J 110 ? ALA J 116 ? ASP J 83  ALA J 89  
AC2 2 GLY J 68  ? HIS J 75  ? GLY J 41  HIS J 48  
AC2 3 THR J 143 ? HIS J 147 ? THR J 116 HIS J 120 
AC2 4 ARG J 170 ? VAL J 175 ? 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 ILE A 126 ? O ILE A 99  N VAL A 58  ? N VAL A 31  
AA1 2 3 O TRP A 59  ? O TRP A 32  N ASN A 46  ? N ASN A 19  
AA1 3 4 O ILE A 45  ? O ILE A 18  N CYS A 33  ? N CYS A 6   
AA1 4 5 N VAL A 32  ? N VAL A 5   O GLY A 177 ? O GLY A 150 
AA2 1 2 O ALA A 116 ? O ALA A 89  N GLY A 68  ? N GLY A 41  
AA2 2 3 N HIS A 75  ? N HIS A 48  O THR A 143 ? O THR A 116 
AA2 3 4 N VAL A 146 ? N VAL A 119 O ALA A 172 ? O ALA A 145 
AA3 1 2 O ILE B 126 ? O ILE B 99  N VAL B 58  ? N VAL B 31  
AA3 2 3 O TRP B 59  ? O TRP B 32  N ASN B 46  ? N ASN B 19  
AA3 3 4 O PHE B 47  ? O PHE B 20  N ALA B 31  ? N ALA B 4   
AA3 4 5 N VAL B 32  ? N VAL B 5   O GLY B 177 ? O GLY B 150 
AA4 1 2 O ALA B 116 ? O ALA B 89  N GLY B 68  ? N GLY B 41  
AA4 2 3 N HIS B 75  ? N HIS B 48  O THR B 143 ? O THR B 116 
AA4 3 4 N VAL B 146 ? N VAL B 119 O LEU B 171 ? O LEU B 144 
AA5 1 2 O ALA C 122 ? O ALA C 95  N ILE C 62  ? N ILE C 35  
AA5 2 3 O TRP C 59  ? O TRP C 32  N ASN C 46  ? N ASN C 19  
AA5 3 4 O ILE C 45  ? O ILE C 18  N CYS C 33  ? N CYS C 6   
AA5 4 5 N VAL C 32  ? N VAL C 5   O GLY C 177 ? O GLY C 150 
AA6 1 2 O ALA C 116 ? O ALA C 89  N GLY C 68  ? N GLY C 41  
AA6 2 3 N HIS C 75  ? N HIS C 48  O THR C 143 ? O THR C 116 
AA6 3 4 N LEU C 144 ? N LEU C 117 O GLY C 174 ? O GLY C 147 
AA7 1 2 O ASP D 128 ? O ASP D 101 N VAL D 56  ? N VAL D 29  
AA7 2 3 O TRP D 59  ? O TRP D 32  N ASN D 46  ? N ASN D 19  
AA7 3 4 O GLY D 43  ? O GLY D 16  N LEU D 35  ? N LEU D 8   
AA7 4 5 N VAL D 32  ? N VAL D 5   O GLY D 177 ? O GLY D 150 
AA8 1 2 O ALA D 116 ? O ALA D 89  N GLY D 68  ? N GLY D 41  
AA8 2 3 N HIS D 75  ? N HIS D 48  O THR D 143 ? O THR D 116 
AA8 3 4 N LEU D 144 ? N LEU D 117 O GLY D 174 ? O GLY D 147 
AA9 1 2 O ASP E 128 ? O ASP E 101 N VAL E 56  ? N VAL E 29  
AA9 2 3 O TRP E 59  ? O TRP E 32  N ASN E 46  ? N ASN E 19  
AA9 3 4 O ILE E 45  ? O ILE E 18  N CYS E 33  ? N CYS E 6   
AA9 4 5 N VAL E 32  ? N VAL E 5   O GLY E 177 ? O GLY E 150 
AB1 1 2 O ALA E 116 ? O ALA E 89  N GLY E 68  ? N GLY E 41  
AB1 2 3 N HIS E 75  ? N HIS E 48  O THR E 143 ? O THR E 116 
AB1 3 4 N LEU E 144 ? N LEU E 117 O GLY E 174 ? O GLY E 147 
AB2 1 2 O ALA F 122 ? O ALA F 95  N ILE F 62  ? N ILE F 35  
AB2 2 3 O TRP F 59  ? O TRP F 32  N ASN F 46  ? N ASN F 19  
AB2 3 4 O GLY F 43  ? O GLY F 16  N LEU F 35  ? N LEU F 8   
AB2 4 5 N VAL F 32  ? N VAL F 5   O GLY F 177 ? O GLY F 150 
AB3 1 2 O ALA F 116 ? O ALA F 89  N GLY F 68  ? N GLY F 41  
AB3 2 3 N HIS F 75  ? N HIS F 48  O THR F 143 ? O THR F 116 
AB3 3 4 N LEU F 144 ? N LEU F 117 O GLY F 174 ? O GLY F 147 
AB4 1 2 O ASP G 128 ? O ASP G 101 N VAL G 56  ? N VAL G 29  
AB4 2 3 O TRP G 59  ? O TRP G 32  N ASN G 46  ? N ASN G 19  
AB4 3 4 O GLY G 43  ? O GLY G 16  N LEU G 35  ? N LEU G 8   
AB4 4 5 N VAL G 32  ? N VAL G 5   O GLY G 177 ? O GLY G 150 
AB5 1 2 O ALA G 116 ? O ALA G 89  N GLY G 68  ? N GLY G 41  
AB5 2 3 N HIS G 75  ? N HIS G 48  O THR G 143 ? O THR G 116 
AB5 3 4 N LEU G 144 ? N LEU G 117 O GLY G 174 ? O GLY G 147 
AB6 1 2 O ASP H 128 ? O ASP H 101 N VAL H 56  ? N VAL H 29  
AB6 2 3 O TRP H 59  ? O TRP H 32  N ASN H 46  ? N ASN H 19  
AB6 3 4 O GLY H 43  ? O GLY H 16  N LEU H 35  ? N LEU H 8   
AB6 4 5 N VAL H 32  ? N VAL H 5   O GLY H 177 ? O GLY H 150 
AB7 1 2 O ALA H 116 ? O ALA H 89  N GLY H 68  ? N GLY H 41  
AB7 2 3 N HIS H 75  ? N HIS H 48  O THR H 143 ? O THR H 116 
AB7 3 4 N LEU H 144 ? N LEU H 117 O GLY H 174 ? O GLY H 147 
AB8 1 2 O ASP I 128 ? O ASP I 101 N VAL I 56  ? N VAL I 29  
AB8 2 3 O TRP I 59  ? O TRP I 32  N ASN I 46  ? N ASN I 19  
AB8 3 4 O PHE I 47  ? O PHE I 20  N ALA I 31  ? N ALA I 4   
AB8 4 5 N VAL I 32  ? N VAL I 5   O GLY I 177 ? O GLY I 150 
AB9 1 2 O ALA I 116 ? O ALA I 89  N GLY I 68  ? N GLY I 41  
AB9 2 3 N HIS I 75  ? N HIS I 48  O THR I 143 ? O THR I 116 
AB9 3 4 N VAL I 146 ? N VAL I 119 O ALA I 172 ? O ALA I 145 
AC1 1 2 O ASP J 128 ? O ASP J 101 N VAL J 56  ? N VAL J 29  
AC1 2 3 O TRP J 59  ? O TRP J 32  N ASN J 46  ? N ASN J 19  
AC1 3 4 O GLY J 43  ? O GLY J 16  N LEU J 35  ? N LEU J 8   
AC1 4 5 N VAL J 32  ? N VAL J 5   O GLY J 177 ? O GLY J 150 
AC2 1 2 O ALA J 116 ? O ALA J 89  N GLY J 68  ? N GLY J 41  
AC2 2 3 N HIS J 75  ? N HIS J 48  O THR J 143 ? O THR J 116 
AC2 3 4 N LEU J 144 ? N LEU J 117 O GLY J 174 ? 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 GOL 202 ? 8  'binding site for residue GOL A 202' 
AC3 Software B ZN  201 ? 4  'binding site for residue ZN B 201'  
AC4 Software B GOL 202 ? 9  'binding site for residue GOL B 202' 
AC5 Software B 946 203 ? 9  'binding site for residue 946 B 203' 
AC6 Software B PS5 204 ? 5  'binding site for residue PS5 B 204' 
AC7 Software C ZN  201 ? 4  'binding site for residue ZN C 201'  
AC8 Software C GOL 202 ? 11 'binding site for residue GOL C 202' 
AC9 Software C PS5 203 ? 2  'binding site for residue PS5 C 203' 
AD1 Software D ZN  201 ? 4  'binding site for residue ZN D 201'  
AD2 Software D 946 202 ? 6  'binding site for residue 946 D 202' 
AD3 Software E ZN  201 ? 4  'binding site for residue ZN E 201'  
AD4 Software E PS5 202 ? 3  'binding site for residue PS5 E 202' 
AD5 Software F ZN  201 ? 4  'binding site for residue ZN F 201'  
AD6 Software G ZN  201 ? 4  'binding site for residue ZN G 201'  
AD7 Software H ZN  201 ? 4  'binding site for residue ZN H 201'  
AD8 Software H 946 202 ? 10 'binding site for residue 946 H 202' 
AD9 Software I ZN  201 ? 4  'binding site for residue ZN I 201'  
# 
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  90  ? HIS A 63  . ? 1_555  ? 
2  AC1 4  HIS A  98  ? HIS A 71  . ? 1_555  ? 
3  AC1 4  HIS A  107 ? HIS A 80  . ? 1_555  ? 
4  AC1 4  ASP A  110 ? ASP A 83  . ? 1_555  ? 
5  AC2 8  HIS A  75  ? HIS A 48  . ? 1_555  ? 
6  AC2 8  HIS A  147 ? HIS A 120 . ? 1_555  ? 
7  AC2 8  THR A  164 ? THR A 137 . ? 1_555  ? 
8  AC2 8  GLY A  168 ? GLY A 141 . ? 1_555  ? 
9  AC2 8  ARG A  170 ? ARG A 143 . ? 1_555  ? 
10 AC2 8  HOH CA .   ? HOH A 302 . ? 1_555  ? 
11 AC2 8  HOH CA .   ? HOH A 363 . ? 1_555  ? 
12 AC2 8  HOH CA .   ? HOH A 378 . ? 1_555  ? 
13 AC3 4  HIS B  90  ? HIS B 63  . ? 1_555  ? 
14 AC3 4  HIS B  98  ? HIS B 71  . ? 1_555  ? 
15 AC3 4  HIS B  107 ? HIS B 80  . ? 1_555  ? 
16 AC3 4  ASP B  110 ? ASP B 83  . ? 1_555  ? 
17 AC4 9  HIS B  75  ? HIS B 48  . ? 1_555  ? 
18 AC4 9  HIS B  90  ? HIS B 63  . ? 1_555  ? 
19 AC4 9  HIS B  147 ? HIS B 120 . ? 1_555  ? 
20 AC4 9  THR B  164 ? THR B 137 . ? 1_555  ? 
21 AC4 9  GLY B  168 ? GLY B 141 . ? 1_555  ? 
22 AC4 9  ARG B  170 ? ARG B 143 . ? 1_555  ? 
23 AC4 9  HOH DA .   ? HOH B 315 . ? 1_555  ? 
24 AC4 9  HOH DA .   ? HOH B 363 . ? 1_555  ? 
25 AC4 9  HOH DA .   ? HOH B 368 . ? 1_555  ? 
26 AC5 9  GLU B  48  ? GLU B 21  . ? 1_555  ? 
27 AC5 9  GLN B  49  ? GLN B 22  . ? 1_555  ? 
28 AC5 9  LYS B  50  ? LYS B 23  . ? 1_555  ? 
29 AC5 9  PRO B  55  ? PRO B 28  . ? 1_555  ? 
30 AC5 9  LYS B  57  ? LYS B 30  . ? 1_555  ? 
31 AC5 9  TRP B  59  ? TRP B 32  . ? 1_555  ? 
32 AC5 9  GLU B  127 ? GLU B 100 . ? 1_555  ? 
33 AC5 9  SER H  125 ? SER H 98  . ? 1_555  ? 
34 AC5 9  946 AA .   ? 946 H 202 . ? 1_555  ? 
35 AC6 5  CYS A  138 ? CYS A 111 . ? 1_555  ? 
36 AC6 5  ILE A  140 ? ILE A 113 . ? 1_555  ? 
37 AC6 5  LEU B  133 ? LEU B 106 . ? 1_555  ? 
38 AC6 5  CYS B  138 ? CYS B 111 . ? 1_555  ? 
39 AC6 5  ILE B  140 ? ILE B 113 . ? 1_555  ? 
40 AC7 4  HIS C  90  ? HIS C 63  . ? 1_555  ? 
41 AC7 4  HIS C  98  ? HIS C 71  . ? 1_555  ? 
42 AC7 4  HIS C  107 ? HIS C 80  . ? 1_555  ? 
43 AC7 4  ASP C  110 ? ASP C 83  . ? 1_555  ? 
44 AC8 11 HIS C  75  ? HIS C 48  . ? 1_555  ? 
45 AC8 11 HIS C  90  ? HIS C 63  . ? 1_555  ? 
46 AC8 11 HIS C  147 ? HIS C 120 . ? 1_555  ? 
47 AC8 11 THR C  164 ? THR C 137 . ? 1_555  ? 
48 AC8 11 GLY C  168 ? GLY C 141 . ? 1_555  ? 
49 AC8 11 ARG C  170 ? ARG C 143 . ? 1_555  ? 
50 AC8 11 HOH EA .   ? HOH C 308 . ? 1_555  ? 
51 AC8 11 HOH EA .   ? HOH C 311 . ? 1_555  ? 
52 AC8 11 HOH EA .   ? HOH C 312 . ? 1_555  ? 
53 AC8 11 HOH EA .   ? HOH C 345 . ? 1_555  ? 
54 AC8 11 HOH EA .   ? HOH C 413 . ? 1_555  ? 
55 AC9 2  CYS C  138 ? CYS C 111 . ? 1_555  ? 
56 AC9 2  ILE C  140 ? ILE C 113 . ? 1_555  ? 
57 AD1 4  HIS D  90  ? HIS D 63  . ? 1_555  ? 
58 AD1 4  HIS D  98  ? HIS D 71  . ? 1_555  ? 
59 AD1 4  HIS D  107 ? HIS D 80  . ? 1_555  ? 
60 AD1 4  ASP D  110 ? ASP D 83  . ? 1_555  ? 
61 AD2 6  GLY C  39  ? GLY C 12  . ? 10_664 ? 
62 AD2 6  PRO C  40  ? PRO C 13  . ? 10_664 ? 
63 AD2 6  LYS D  36  ? LYS D 9   . ? 1_555  ? 
64 AD2 6  GLY D  37  ? GLY D 10  . ? 1_555  ? 
65 AD2 6  GLN D  42  ? GLN D 15  . ? 1_555  ? 
66 AD2 6  HOH FA .   ? HOH D 307 . ? 1_555  ? 
67 AD3 4  HIS E  90  ? HIS E 63  . ? 1_555  ? 
68 AD3 4  HIS E  98  ? HIS E 71  . ? 1_555  ? 
69 AD3 4  HIS E  107 ? HIS E 80  . ? 1_555  ? 
70 AD3 4  ASP E  110 ? ASP E 83  . ? 1_555  ? 
71 AD4 3  CYS E  138 ? CYS E 111 . ? 1_555  ? 
72 AD4 3  ILE E  140 ? ILE E 113 . ? 1_555  ? 
73 AD4 3  ILE F  178 ? ILE F 151 . ? 1_555  ? 
74 AD5 4  HIS F  90  ? HIS F 63  . ? 1_555  ? 
75 AD5 4  HIS F  98  ? HIS F 71  . ? 1_555  ? 
76 AD5 4  HIS F  107 ? HIS F 80  . ? 1_555  ? 
77 AD5 4  ASP F  110 ? ASP F 83  . ? 1_555  ? 
78 AD6 4  HIS G  90  ? HIS G 63  . ? 1_555  ? 
79 AD6 4  HIS G  98  ? HIS G 71  . ? 1_555  ? 
80 AD6 4  HIS G  107 ? HIS G 80  . ? 1_555  ? 
81 AD6 4  ASP G  110 ? ASP G 83  . ? 1_555  ? 
82 AD7 4  HIS H  90  ? HIS H 63  . ? 1_555  ? 
83 AD7 4  HIS H  98  ? HIS H 71  . ? 1_555  ? 
84 AD7 4  HIS H  107 ? HIS H 80  . ? 1_555  ? 
85 AD7 4  ASP H  110 ? ASP H 83  . ? 1_555  ? 
86 AD8 10 THR B  29  ? THR B 2   . ? 1_555  ? 
87 AD8 10 LYS B  30  ? LYS B 3   . ? 1_555  ? 
88 AD8 10 GLU B  48  ? GLU B 21  . ? 1_555  ? 
89 AD8 10 LYS B  50  ? LYS B 23  . ? 1_555  ? 
90 AD8 10 946 O  .   ? 946 B 203 . ? 1_555  ? 
91 AD8 10 LYS H  57  ? LYS H 30  . ? 1_555  ? 
92 AD8 10 VAL H  58  ? VAL H 31  . ? 1_555  ? 
93 AD8 10 TRP H  59  ? TRP H 32  . ? 1_555  ? 
94 AD8 10 SER H  125 ? SER H 98  . ? 1_555  ? 
95 AD8 10 ILE H  126 ? ILE H 99  . ? 1_555  ? 
96 AD9 4  HIS I  90  ? HIS I 63  . ? 1_555  ? 
97 AD9 4  HIS I  98  ? HIS I 71  . ? 1_555  ? 
98 AD9 4  HIS I  107 ? HIS I 80  . ? 1_555  ? 
99 AD9 4  ASP I  110 ? ASP I 83  . ? 1_555  ? 
# 
_atom_sites.entry_id                    5YTO 
_atom_sites.fract_transf_matrix[1][1]   0.004099 
_atom_sites.fract_transf_matrix[1][2]   0.002367 
_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]   0.004734 
_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]   0.006907 
_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   . ALA A  1 26  ? 63.654  50.973  -1.407  1.00 61.53 ? -1  ALA A N   1 
ATOM   2     C  CA  . ALA A  1 26  ? 63.450  49.501  -1.441  1.00 59.10 ? -1  ALA A CA  1 
ATOM   3     C  C   . ALA A  1 26  ? 62.339  49.082  -2.417  1.00 59.17 ? -1  ALA A C   1 
ATOM   4     O  O   . ALA A  1 26  ? 61.991  47.900  -2.463  1.00 61.04 ? -1  ALA A O   1 
ATOM   5     C  CB  . ALA A  1 26  ? 63.158  48.999  -0.050  1.00 51.23 ? -1  ALA A CB  1 
ATOM   6     N  N   . MET A  1 27  ? 61.866  50.046  -3.231  1.00 58.36 ? 0   MET A N   1 
ATOM   7     C  CA  . MET A  1 27  ? 60.596  50.007  -3.998  1.00 58.58 ? 0   MET A CA  1 
ATOM   8     C  C   . MET A  1 27  ? 60.649  49.524  -5.483  1.00 50.40 ? 0   MET A C   1 
ATOM   9     O  O   . MET A  1 27  ? 59.706  48.854  -5.955  1.00 50.38 ? 0   MET A O   1 
ATOM   10    C  CB  . MET A  1 27  ? 59.878  51.377  -3.895  1.00 57.94 ? 0   MET A CB  1 
ATOM   11    C  CG  . MET A  1 27  ? 58.479  51.435  -4.505  1.00 64.75 ? 0   MET A CG  1 
ATOM   12    S  SD  . MET A  1 27  ? 57.204  50.440  -3.661  1.00 83.61 ? 0   MET A SD  1 
ATOM   13    C  CE  . MET A  1 27  ? 56.846  51.479  -2.224  1.00 69.54 ? 0   MET A CE  1 
ATOM   14    N  N   . ALA A  1 28  ? 61.697  49.876  -6.234  1.00 43.66 ? 1   ALA A N   1 
ATOM   15    C  CA  . ALA A  1 28  ? 61.794  49.345  -7.607  1.00 37.78 ? 1   ALA A CA  1 
ATOM   16    C  C   . ALA A  1 28  ? 62.085  47.843  -7.563  1.00 29.74 ? 1   ALA A C   1 
ATOM   17    O  O   . ALA A  1 28  ? 63.018  47.388  -6.881  1.00 32.49 ? 1   ALA A O   1 
ATOM   18    C  CB  . ALA A  1 28  ? 62.839  50.089  -8.426  1.00 36.51 ? 1   ALA A CB  1 
ATOM   19    N  N   . THR A  1 29  ? 61.258  47.060  -8.235  1.00 26.85 ? 2   THR A N   1 
ATOM   20    C  CA  . THR A  1 29  ? 61.570  45.633  -8.401  1.00 23.87 ? 2   THR A CA  1 
ATOM   21    C  C   . THR A  1 29  ? 61.955  45.299  -9.842  1.00 22.87 ? 2   THR A C   1 
ATOM   22    O  O   . THR A  1 29  ? 62.422  44.180  -10.099 1.00 20.11 ? 2   THR A O   1 
ATOM   23    C  CB  . THR A  1 29  ? 60.370  44.715  -8.049  1.00 27.09 ? 2   THR A CB  1 
ATOM   24    O  OG1 . THR A  1 29  ? 59.265  45.055  -8.894  1.00 28.78 ? 2   THR A OG1 1 
ATOM   25    C  CG2 . THR A  1 29  ? 59.999  44.857  -6.572  1.00 31.05 ? 2   THR A CG2 1 
ATOM   26    N  N   . LYS A  1 30  ? 61.689  46.217  -10.791 1.00 18.57 ? 3   LYS A N   1 
ATOM   27    C  CA  . LYS A  1 30  ? 62.049  45.923  -12.208 1.00 19.06 ? 3   LYS A CA  1 
ATOM   28    C  C   . LYS A  1 30  ? 62.708  47.157  -12.818 1.00 18.54 ? 3   LYS A C   1 
ATOM   29    O  O   . LYS A  1 30  ? 62.317  48.298  -12.502 1.00 18.01 ? 3   LYS A O   1 
ATOM   30    C  CB  . LYS A  1 30  ? 60.842  45.562  -13.073 1.00 21.61 ? 3   LYS A CB  1 
ATOM   31    C  CG  . LYS A  1 30  ? 59.923  44.462  -12.581 1.00 30.77 ? 3   LYS A CG  1 
ATOM   32    C  CD  . LYS A  1 30  ? 59.052  43.955  -13.743 1.00 36.67 ? 3   LYS A CD  1 
ATOM   33    C  CE  . LYS A  1 30  ? 58.028  42.914  -13.285 1.00 44.93 ? 3   LYS A CE  1 
ATOM   34    N  NZ  . LYS A  1 30  ? 58.676  41.604  -12.960 1.00 50.11 ? 3   LYS A NZ  1 
ATOM   35    N  N   . ALA A  1 31  ? 63.660  46.934  -13.713 1.00 16.07 ? 4   ALA A N   1 
ATOM   36    C  CA  . ALA A  1 31  ? 64.313  47.987  -14.450 1.00 16.57 ? 4   ALA A CA  1 
ATOM   37    C  C   . ALA A  1 31  ? 64.594  47.469  -15.874 1.00 17.08 ? 4   ALA A C   1 
ATOM   38    O  O   . ALA A  1 31  ? 64.457  46.248  -16.164 1.00 16.93 ? 4   ALA A O   1 
ATOM   39    C  CB  . ALA A  1 31  ? 65.613  48.400  -13.751 1.00 16.92 ? 4   ALA A CB  1 
ATOM   40    N  N   . VAL A  1 32  ? 64.951  48.392  -16.772 1.00 16.78 ? 5   VAL A N   1 
ATOM   41    C  CA  . VAL A  1 32  ? 65.162  48.056  -18.192 1.00 16.81 ? 5   VAL A CA  1 
ATOM   42    C  C   . VAL A  1 32  ? 66.204  48.989  -18.786 1.00 16.61 ? 5   VAL A C   1 
ATOM   43    O  O   . VAL A  1 32  ? 66.357  50.145  -18.336 1.00 17.76 ? 5   VAL A O   1 
ATOM   44    C  CB  . VAL A  1 32  ? 63.848  48.021  -19.000 1.00 17.02 ? 5   VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 32  ? 63.320  49.460  -19.206 1.00 16.83 ? 5   VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 32  ? 64.066  47.372  -20.373 1.00 18.46 ? 5   VAL A CG2 1 
ATOM   47    N  N   . CYS A  1 33  ? 66.948  48.525  -19.793 1.00 15.72 ? 6   CYS A N   1 
ATOM   48    C  CA  . CYS A  1 33  ? 67.919  49.399  -20.370 1.00 15.83 ? 6   CYS A CA  1 
ATOM   49    C  C   . CYS A  1 33  ? 67.948  49.120  -21.884 1.00 17.52 ? 6   CYS A C   1 
ATOM   50    O  O   . CYS A  1 33  ? 67.987  47.933  -22.283 1.00 15.70 ? 6   CYS A O   1 
ATOM   51    C  CB  . CYS A  1 33  ? 69.296  49.072  -19.727 1.00 18.35 ? 6   CYS A CB  1 
ATOM   52    S  SG  . CYS A  1 33  ? 70.607  50.002  -20.531 1.00 20.40 ? 6   CYS A SG  1 
ATOM   53    N  N   . VAL A  1 34  ? 67.843  50.169  -22.705 1.00 15.33 ? 7   VAL A N   1 
ATOM   54    C  CA  . VAL A  1 34  ? 67.912  50.033  -24.171 1.00 17.93 ? 7   VAL A CA  1 
ATOM   55    C  C   . VAL A  1 34  ? 69.330  50.438  -24.527 1.00 18.82 ? 7   VAL A C   1 
ATOM   56    O  O   . VAL A  1 34  ? 69.756  51.596  -24.278 1.00 16.53 ? 7   VAL A O   1 
ATOM   57    C  CB  . VAL A  1 34  ? 66.867  50.934  -24.901 1.00 18.56 ? 7   VAL A CB  1 
ATOM   58    C  CG1 . VAL A  1 34  ? 67.036  50.864  -26.446 1.00 23.24 ? 7   VAL A CG1 1 
ATOM   59    C  CG2 . VAL A  1 34  ? 65.440  50.565  -24.452 1.00 20.05 ? 7   VAL A CG2 1 
ATOM   60    N  N   . LEU A  1 35  ? 70.094  49.485  -25.064 1.00 17.33 ? 8   LEU A N   1 
ATOM   61    C  CA  . LEU A  1 35  ? 71.486  49.766  -25.452 1.00 17.53 ? 8   LEU A CA  1 
ATOM   62    C  C   . LEU A  1 35  ? 71.548  50.214  -26.903 1.00 19.08 ? 8   LEU A C   1 
ATOM   63    O  O   . LEU A  1 35  ? 70.972  49.556  -27.789 1.00 19.79 ? 8   LEU A O   1 
ATOM   64    C  CB  . LEU A  1 35  ? 72.343  48.487  -25.293 1.00 18.97 ? 8   LEU A CB  1 
ATOM   65    C  CG  . LEU A  1 35  ? 72.439  47.905  -23.863 1.00 21.88 ? 8   LEU A CG  1 
ATOM   66    C  CD1 . LEU A  1 35  ? 73.207  46.566  -23.900 1.00 28.95 ? 8   LEU A CD1 1 
ATOM   67    C  CD2 . LEU A  1 35  ? 73.306  48.830  -23.082 1.00 23.15 ? 8   LEU A CD2 1 
ATOM   68    N  N   . LYS A  1 36  ? 72.273  51.302  -27.161 1.00 18.70 ? 9   LYS A N   1 
ATOM   69    C  CA  . LYS A  1 36  ? 72.502  51.766  -28.543 1.00 21.59 ? 9   LYS A CA  1 
ATOM   70    C  C   . LYS A  1 36  ? 73.885  52.357  -28.632 1.00 20.71 ? 9   LYS A C   1 
ATOM   71    O  O   . LYS A  1 36  ? 74.449  52.799  -27.623 1.00 18.85 ? 9   LYS A O   1 
ATOM   72    C  CB  . LYS A  1 36  ? 71.554  52.938  -28.896 1.00 26.11 ? 9   LYS A CB  1 
ATOM   73    C  CG  . LYS A  1 36  ? 70.104  52.590  -29.059 1.00 39.80 ? 9   LYS A CG  1 
ATOM   74    C  CD  . LYS A  1 36  ? 69.348  53.870  -29.452 1.00 48.98 ? 9   LYS A CD  1 
ATOM   75    C  CE  . LYS A  1 36  ? 68.135  53.554  -30.338 1.00 55.81 ? 9   LYS A CE  1 
ATOM   76    N  NZ  . LYS A  1 36  ? 67.108  52.735  -29.618 1.00 48.50 ? 9   LYS A NZ  1 
ATOM   77    N  N   . GLY A  1 37  ? 74.434  52.472  -29.855 1.00 19.79 ? 10  GLY A N   1 
ATOM   78    C  CA  . GLY A  1 37  ? 75.770  53.043  -29.981 1.00 22.42 ? 10  GLY A CA  1 
ATOM   79    C  C   . GLY A  1 37  ? 75.979  53.584  -31.397 1.00 24.52 ? 10  GLY A C   1 
ATOM   80    O  O   . GLY A  1 37  ? 75.039  53.757  -32.113 1.00 25.23 ? 10  GLY A O   1 
ATOM   81    N  N   . ASP A  1 38  ? 77.219  53.836  -31.775 1.00 29.05 ? 11  ASP A N   1 
ATOM   82    C  CA  . ASP A  1 38  ? 77.533  54.389  -33.103 1.00 34.18 ? 11  ASP A CA  1 
ATOM   83    C  C   . ASP A  1 38  ? 77.552  53.318  -34.195 1.00 36.72 ? 11  ASP A C   1 
ATOM   84    O  O   . ASP A  1 38  ? 77.306  53.638  -35.360 1.00 37.05 ? 11  ASP A O   1 
ATOM   85    C  CB  . ASP A  1 38  ? 78.878  55.115  -33.055 1.00 34.64 ? 11  ASP A CB  1 
ATOM   86    C  CG  . ASP A  1 38  ? 78.779  56.432  -32.317 1.00 44.53 ? 11  ASP A CG  1 
ATOM   87    O  OD1 . ASP A  1 38  ? 77.660  57.019  -32.316 1.00 39.62 ? 11  ASP A OD1 1 
ATOM   88    O  OD2 . ASP A  1 38  ? 79.808  56.867  -31.729 1.00 47.13 ? 11  ASP A OD2 1 
ATOM   89    N  N   . GLY A  1 39  ? 77.791  52.060  -33.807 1.00 34.20 ? 12  GLY A N   1 
ATOM   90    C  CA  . GLY A  1 39  ? 77.803  50.908  -34.747 1.00 28.57 ? 12  GLY A CA  1 
ATOM   91    C  C   . GLY A  1 39  ? 76.500  50.159  -34.728 1.00 25.92 ? 12  GLY A C   1 
ATOM   92    O  O   . GLY A  1 39  ? 75.453  50.732  -34.424 1.00 28.02 ? 12  GLY A O   1 
ATOM   93    N  N   . PRO A  1 40  ? 76.526  48.848  -35.063 1.00 24.73 ? 13  PRO A N   1 
ATOM   94    C  CA  . PRO A  1 40  ? 75.311  48.030  -35.189 1.00 22.15 ? 13  PRO A CA  1 
ATOM   95    C  C   . PRO A  1 40  ? 74.861  47.427  -33.849 1.00 21.44 ? 13  PRO A C   1 
ATOM   96    O  O   . PRO A  1 40  ? 73.879  46.742  -33.813 1.00 22.99 ? 13  PRO A O   1 
ATOM   97    C  CB  . PRO A  1 40  ? 75.776  46.869  -36.128 1.00 25.25 ? 13  PRO A CB  1 
ATOM   98    C  CG  . PRO A  1 40  ? 77.234  46.746  -35.814 1.00 25.95 ? 13  PRO A CG  1 
ATOM   99    C  CD  . PRO A  1 40  ? 77.741  48.131  -35.499 1.00 27.07 ? 13  PRO A CD  1 
ATOM   100   N  N   . VAL A  1 41  ? 75.585  47.660  -32.765 1.00 21.00 ? 14  VAL A N   1 
ATOM   101   C  CA  . VAL A  1 41  ? 75.277  46.918  -31.535 1.00 22.04 ? 14  VAL A CA  1 
ATOM   102   C  C   . VAL A  1 41  ? 74.030  47.535  -30.864 1.00 23.59 ? 14  VAL A C   1 
ATOM   103   O  O   . VAL A  1 41  ? 73.971  48.758  -30.652 1.00 23.32 ? 14  VAL A O   1 
ATOM   104   C  CB  . VAL A  1 41  ? 76.421  46.906  -30.525 1.00 21.27 ? 14  VAL A CB  1 
ATOM   105   C  CG1 . VAL A  1 41  ? 75.968  46.144  -29.267 1.00 20.40 ? 14  VAL A CG1 1 
ATOM   106   C  CG2 . VAL A  1 41  ? 77.640  46.214  -31.152 1.00 24.30 ? 14  VAL A CG2 1 
ATOM   107   N  N   . GLN A  1 42  ? 73.051  46.705  -30.593 1.00 22.90 ? 15  GLN A N   1 
ATOM   108   C  CA  . GLN A  1 42  ? 71.864  47.184  -29.892 1.00 24.16 ? 15  GLN A CA  1 
ATOM   109   C  C   . GLN A  1 42  ? 71.201  46.088  -29.124 1.00 23.54 ? 15  GLN A C   1 
ATOM   110   O  O   . GLN A  1 42  ? 71.296  44.882  -29.483 1.00 23.06 ? 15  GLN A O   1 
ATOM   111   C  CB  . GLN A  1 42  ? 70.895  47.834  -30.862 1.00 29.40 ? 15  GLN A CB  1 
ATOM   112   C  CG  . GLN A  1 42  ? 70.543  47.012  -32.048 1.00 35.33 ? 15  GLN A CG  1 
ATOM   113   C  CD  . GLN A  1 42  ? 69.752  47.821  -33.062 1.00 43.34 ? 15  GLN A CD  1 
ATOM   114   O  OE1 . GLN A  1 42  ? 68.638  48.183  -32.804 1.00 45.44 ? 15  GLN A OE1 1 
ATOM   115   N  NE2 . GLN A  1 42  ? 70.327  48.081  -34.208 1.00 41.59 ? 15  GLN A NE2 1 
ATOM   116   N  N   . GLY A  1 43  ? 70.537  46.451  -28.041 1.00 21.80 ? 16  GLY A N   1 
ATOM   117   C  CA  . GLY A  1 43  ? 69.867  45.409  -27.284 1.00 21.49 ? 16  GLY A CA  1 
ATOM   118   C  C   . GLY A  1 43  ? 68.935  45.956  -26.246 1.00 21.82 ? 16  GLY A C   1 
ATOM   119   O  O   . GLY A  1 43  ? 68.870  47.163  -26.079 1.00 19.36 ? 16  GLY A O   1 
ATOM   120   N  N   . ILE A  1 44  ? 68.196  45.060  -25.628 1.00 19.40 ? 17  ILE A N   1 
ATOM   121   C  CA  . ILE A  1 44  ? 67.328  45.399  -24.515 1.00 18.59 ? 17  ILE A CA  1 
ATOM   122   C  C   . ILE A  1 44  ? 67.744  44.485  -23.381 1.00 18.01 ? 17  ILE A C   1 
ATOM   123   O  O   . ILE A  1 44  ? 67.744  43.244  -23.544 1.00 19.91 ? 17  ILE A O   1 
ATOM   124   C  CB  . ILE A  1 44  ? 65.834  45.203  -24.874 1.00 18.03 ? 17  ILE A CB  1 
ATOM   125   C  CG1 . ILE A  1 44  ? 65.424  46.178  -26.014 1.00 21.51 ? 17  ILE A CG1 1 
ATOM   126   C  CG2 . ILE A  1 44  ? 64.968  45.363  -23.617 1.00 21.01 ? 17  ILE A CG2 1 
ATOM   127   C  CD1 . ILE A  1 44  ? 64.042  45.922  -26.639 1.00 25.08 ? 17  ILE A CD1 1 
ATOM   128   N  N   . ILE A  1 45  ? 68.072  45.059  -22.220 1.00 16.25 ? 18  ILE A N   1 
ATOM   129   C  CA  . ILE A  1 45  ? 68.399  44.267  -21.027 1.00 15.71 ? 18  ILE A CA  1 
ATOM   130   C  C   . ILE A  1 45  ? 67.363  44.569  -19.911 1.00 18.57 ? 18  ILE A C   1 
ATOM   131   O  O   . ILE A  1 45  ? 67.121  45.735  -19.598 1.00 16.20 ? 18  ILE A O   1 
ATOM   132   C  CB  . ILE A  1 45  ? 69.838  44.567  -20.532 1.00 16.56 ? 18  ILE A CB  1 
ATOM   133   C  CG1 . ILE A  1 45  ? 70.892  44.135  -21.613 1.00 15.41 ? 18  ILE A CG1 1 
ATOM   134   C  CG2 . ILE A  1 45  ? 70.115  43.928  -19.173 1.00 14.50 ? 18  ILE A CG2 1 
ATOM   135   C  CD1 . ILE A  1 45  ? 70.900  42.604  -21.890 1.00 16.71 ? 18  ILE A CD1 1 
ATOM   136   N  N   . ASN A  1 46  ? 66.819  43.506  -19.316 1.00 16.74 ? 19  ASN A N   1 
ATOM   137   C  CA  . ASN A  1 46  ? 65.872  43.579  -18.192 1.00 19.45 ? 19  ASN A CA  1 
ATOM   138   C  C   . ASN A  1 46  ? 66.527  43.257  -16.887 1.00 19.97 ? 19  ASN A C   1 
ATOM   139   O  O   . ASN A  1 46  ? 67.540  42.468  -16.845 1.00 17.55 ? 19  ASN A O   1 
ATOM   140   C  CB  . ASN A  1 46  ? 64.773  42.546  -18.439 1.00 20.77 ? 19  ASN A CB  1 
ATOM   141   C  CG  . ASN A  1 46  ? 64.156  42.704  -19.795 1.00 24.54 ? 19  ASN A CG  1 
ATOM   142   O  OD1 . ASN A  1 46  ? 64.433  41.931  -20.739 1.00 29.56 ? 19  ASN A OD1 1 
ATOM   143   N  ND2 . ASN A  1 46  ? 63.376  43.728  -19.935 1.00 20.49 ? 19  ASN A ND2 1 
ATOM   144   N  N   . PHE A  1 47  ? 66.005  43.855  -15.790 1.00 18.67 ? 20  PHE A N   1 
ATOM   145   C  CA  . PHE A  1 47  ? 66.571  43.602  -14.482 1.00 17.89 ? 20  PHE A CA  1 
ATOM   146   C  C   . PHE A  1 47  ? 65.378  43.307  -13.605 1.00 19.74 ? 20  PHE A C   1 
ATOM   147   O  O   . PHE A  1 47  ? 64.325  43.968  -13.744 1.00 18.23 ? 20  PHE A O   1 
ATOM   148   C  CB  . PHE A  1 47  ? 67.258  44.822  -13.878 1.00 17.70 ? 20  PHE A CB  1 
ATOM   149   C  CG  . PHE A  1 47  ? 68.436  45.312  -14.654 1.00 19.64 ? 20  PHE A CG  1 
ATOM   150   C  CD1 . PHE A  1 47  ? 68.246  46.123  -15.787 1.00 20.20 ? 20  PHE A CD1 1 
ATOM   151   C  CD2 . PHE A  1 47  ? 69.711  44.958  -14.278 1.00 18.58 ? 20  PHE A CD2 1 
ATOM   152   C  CE1 . PHE A  1 47  ? 69.343  46.594  -16.524 1.00 21.91 ? 20  PHE A CE1 1 
ATOM   153   C  CE2 . PHE A  1 47  ? 70.820  45.426  -15.010 1.00 20.33 ? 20  PHE A CE2 1 
ATOM   154   C  CZ  . PHE A  1 47  ? 70.622  46.278  -16.114 1.00 19.13 ? 20  PHE A CZ  1 
ATOM   155   N  N   . GLU A  1 48  ? 65.509  42.308  -12.735 1.00 19.20 ? 21  GLU A N   1 
ATOM   156   C  CA  . GLU A  1 48  ? 64.379  42.029  -11.811 1.00 21.77 ? 21  GLU A CA  1 
ATOM   157   C  C   . GLU A  1 48  ? 64.928  41.695  -10.447 1.00 22.86 ? 21  GLU A C   1 
ATOM   158   O  O   . GLU A  1 48  ? 65.872  40.875  -10.319 1.00 22.36 ? 21  GLU A O   1 
ATOM   159   C  CB  . GLU A  1 48  ? 63.430  40.927  -12.345 1.00 24.20 ? 21  GLU A CB  1 
ATOM   160   C  CG  . GLU A  1 48  ? 62.348  40.569  -11.315 1.00 30.85 ? 21  GLU A CG  1 
ATOM   161   C  CD  . GLU A  1 48  ? 61.199  39.739  -11.872 1.00 44.10 ? 21  GLU A CD  1 
ATOM   162   O  OE1 . GLU A  1 48  ? 61.470  38.742  -12.570 1.00 47.62 ? 21  GLU A OE1 1 
ATOM   163   O  OE2 . GLU A  1 48  ? 60.014  40.080  -11.607 1.00 49.57 ? 21  GLU A OE2 1 
ATOM   164   N  N   . GLN A  1 49  ? 64.369  42.333  -9.408  1.00 19.69 ? 22  GLN A N   1 
ATOM   165   C  CA  . GLN A  1 49  ? 64.838  42.063  -8.052  1.00 19.53 ? 22  GLN A CA  1 
ATOM   166   C  C   . GLN A  1 49  ? 63.601  41.930  -7.175  1.00 24.56 ? 22  GLN A C   1 
ATOM   167   O  O   . GLN A  1 49  ? 63.036  42.963  -6.744  1.00 25.88 ? 22  GLN A O   1 
ATOM   168   C  CB  . GLN A  1 49  ? 65.769  43.157  -7.548  1.00 17.92 ? 22  GLN A CB  1 
ATOM   169   C  CG  . GLN A  1 49  ? 66.347  42.867  -6.184  1.00 17.75 ? 22  GLN A CG  1 
ATOM   170   C  CD  . GLN A  1 49  ? 67.190  44.003  -5.708  1.00 19.59 ? 22  GLN A CD  1 
ATOM   171   O  OE1 . GLN A  1 49  ? 66.950  45.152  -6.105  1.00 19.81 ? 22  GLN A OE1 1 
ATOM   172   N  NE2 . GLN A  1 49  ? 68.186  43.720  -4.880  1.00 20.02 ? 22  GLN A NE2 1 
ATOM   173   N  N   . LYS A  1 50  ? 63.134  40.695  -6.997  1.00 26.29 ? 23  LYS A N   1 
ATOM   174   C  CA  . LYS A  1 50  ? 61.904  40.448  -6.234  1.00 31.72 ? 23  LYS A CA  1 
ATOM   175   C  C   . LYS A  1 50  ? 62.000  40.817  -4.747  1.00 31.35 ? 23  LYS A C   1 
ATOM   176   O  O   . LYS A  1 50  ? 61.023  41.303  -4.184  1.00 33.86 ? 23  LYS A O   1 
ATOM   177   C  CB  . LYS A  1 50  ? 61.413  39.017  -6.461  1.00 40.65 ? 23  LYS A CB  1 
ATOM   178   C  CG  . LYS A  1 50  ? 60.851  38.884  -7.867  1.00 48.30 ? 23  LYS A CG  1 
ATOM   179   C  CD  . LYS A  1 50  ? 59.756  37.837  -7.980  1.00 59.80 ? 23  LYS A CD  1 
ATOM   180   C  CE  . LYS A  1 50  ? 59.381  37.648  -9.443  1.00 62.64 ? 23  LYS A CE  1 
ATOM   181   N  NZ  . LYS A  1 50  ? 58.587  36.408  -9.690  1.00 66.54 ? 23  LYS A NZ  1 
ATOM   182   N  N   . GLU A  1 51  ? 63.188  40.705  -4.146  1.00 30.11 ? 24  GLU A N   1 
ATOM   183   C  CA  . GLU A  1 51  ? 63.382  41.085  -2.751  1.00 29.13 ? 24  GLU A CA  1 
ATOM   184   C  C   . GLU A  1 51  ? 64.476  42.099  -2.668  1.00 29.37 ? 24  GLU A C   1 
ATOM   185   O  O   . GLU A  1 51  ? 65.544  41.878  -3.236  1.00 23.90 ? 24  GLU A O   1 
ATOM   186   C  CB  . GLU A  1 51  ? 63.769  39.855  -1.896  1.00 33.05 ? 24  GLU A CB  1 
ATOM   187   C  CG  . GLU A  1 51  ? 62.763  38.725  -1.944  1.00 38.16 ? 24  GLU A CG  1 
ATOM   188   C  CD  . GLU A  1 51  ? 61.557  38.991  -1.051  1.00 56.55 ? 24  GLU A CD  1 
ATOM   189   O  OE1 . GLU A  1 51  ? 61.569  40.005  -0.281  1.00 58.10 ? 24  GLU A OE1 1 
ATOM   190   O  OE2 . GLU A  1 51  ? 60.588  38.186  -1.116  1.00 59.86 ? 24  GLU A OE2 1 
ATOM   191   N  N   . SER A  1 52  ? 64.248  43.203  -1.938  1.00 24.62 ? 25  SER A N   1 
ATOM   192   C  CA  . SER A  1 52  ? 65.258  44.240  -1.830  1.00 25.17 ? 25  SER A CA  1 
ATOM   193   C  C   . SER A  1 52  ? 66.595  43.764  -1.291  1.00 23.08 ? 25  SER A C   1 
ATOM   194   O  O   . SER A  1 52  ? 67.632  44.372  -1.566  1.00 22.55 ? 25  SER A O   1 
ATOM   195   C  CB  . SER A  1 52  ? 64.753  45.415  -0.974  1.00 31.31 ? 25  SER A CB  1 
ATOM   196   O  OG  . SER A  1 52  ? 64.426  44.962  0.327   1.00 31.14 ? 25  SER A OG  1 
ATOM   197   N  N   . ASN A  1 53  ? 66.596  42.699  -0.495  1.00 25.56 ? 26  ASN A N   1 
ATOM   198   C  CA  . ASN A  1 53  ? 67.875  42.149  -0.010  1.00 27.84 ? 26  ASN A CA  1 
ATOM   199   C  C   . ASN A  1 53  ? 68.277  40.837  -0.669  1.00 29.05 ? 26  ASN A C   1 
ATOM   200   O  O   . ASN A  1 53  ? 69.069  40.071  -0.086  1.00 30.63 ? 26  ASN A O   1 
ATOM   201   C  CB  . ASN A  1 53  ? 67.881  41.971  1.526   1.00 29.05 ? 26  ASN A CB  1 
ATOM   202   C  CG  . ASN A  1 53  ? 66.881  40.972  2.004   1.00 28.53 ? 26  ASN A CG  1 
ATOM   203   O  OD1 . ASN A  1 53  ? 65.829  40.789  1.402   1.00 31.01 ? 26  ASN A OD1 1 
ATOM   204   N  ND2 . ASN A  1 53  ? 67.196  40.323  3.169   1.00 28.94 ? 26  ASN A ND2 1 
ATOM   205   N  N   . GLY A  1 54  ? 67.694  40.583  -1.840  1.00 26.29 ? 27  GLY A N   1 
ATOM   206   C  CA  . GLY A  1 54  ? 68.032  39.436  -2.667  1.00 25.54 ? 27  GLY A CA  1 
ATOM   207   C  C   . GLY A  1 54  ? 68.752  39.829  -3.963  1.00 25.05 ? 27  GLY A C   1 
ATOM   208   O  O   . GLY A  1 54  ? 69.011  41.018  -4.245  1.00 21.05 ? 27  GLY A O   1 
ATOM   209   N  N   . PRO A  1 55  ? 69.081  38.811  -4.773  1.00 24.98 ? 28  PRO A N   1 
ATOM   210   C  CA  . PRO A  1 55  ? 69.844  39.055  -5.979  1.00 23.87 ? 28  PRO A CA  1 
ATOM   211   C  C   . PRO A  1 55  ? 69.033  39.744  -7.093  1.00 21.55 ? 28  PRO A C   1 
ATOM   212   O  O   . PRO A  1 55  ? 67.791  39.664  -7.116  1.00 18.71 ? 28  PRO A O   1 
ATOM   213   C  CB  . PRO A  1 55  ? 70.282  37.639  -6.430  1.00 26.70 ? 28  PRO A CB  1 
ATOM   214   C  CG  . PRO A  1 55  ? 69.431  36.649  -5.672  1.00 28.72 ? 28  PRO A CG  1 
ATOM   215   C  CD  . PRO A  1 55  ? 68.834  37.369  -4.483  1.00 27.07 ? 28  PRO A CD  1 
ATOM   216   N  N   . VAL A  1 56  ? 69.753  40.307  -8.075  1.00 20.71 ? 29  VAL A N   1 
ATOM   217   C  CA  . VAL A  1 56  ? 69.120  40.875  -9.278  1.00 19.08 ? 29  VAL A CA  1 
ATOM   218   C  C   . VAL A  1 56  ? 69.355  39.931  -10.452 1.00 20.04 ? 29  VAL A C   1 
ATOM   219   O  O   . VAL A  1 56  ? 70.520  39.570  -10.723 1.00 19.28 ? 29  VAL A O   1 
ATOM   220   C  CB  . VAL A  1 56  ? 69.773  42.221  -9.628  1.00 16.97 ? 29  VAL A CB  1 
ATOM   221   C  CG1 . VAL A  1 56  ? 69.151  42.815  -10.907 1.00 16.15 ? 29  VAL A CG1 1 
ATOM   222   C  CG2 . VAL A  1 56  ? 69.640  43.179  -8.437  1.00 18.58 ? 29  VAL A CG2 1 
ATOM   223   N  N   . LYS A  1 57  ? 68.271  39.490  -11.083 1.00 19.34 ? 30  LYS A N   1 
ATOM   224   C  CA  . LYS A  1 57  ? 68.351  38.793  -12.359 1.00 20.32 ? 30  LYS A CA  1 
ATOM   225   C  C   . LYS A  1 57  ? 68.475  39.780  -13.497 1.00 20.19 ? 30  LYS A C   1 
ATOM   226   O  O   . LYS A  1 57  ? 67.721  40.768  -13.566 1.00 18.90 ? 30  LYS A O   1 
ATOM   227   C  CB  . LYS A  1 57  ? 67.124  37.929  -12.572 1.00 24.40 ? 30  LYS A CB  1 
ATOM   228   C  CG  . LYS A  1 57  ? 66.927  36.987  -11.407 1.00 29.78 ? 30  LYS A CG  1 
ATOM   229   C  CD  . LYS A  1 57  ? 65.800  35.990  -11.673 1.00 37.96 ? 30  LYS A CD  1 
ATOM   230   C  CE  . LYS A  1 57  ? 65.812  34.926  -10.570 1.00 41.49 ? 30  LYS A CE  1 
ATOM   231   N  NZ  . LYS A  1 57  ? 65.058  33.739  -11.048 1.00 48.02 ? 30  LYS A NZ  1 
ATOM   232   N  N   . VAL A  1 58  ? 69.402  39.513  -14.434 1.00 16.54 ? 31  VAL A N   1 
ATOM   233   C  CA  . VAL A  1 58  ? 69.649  40.439  -15.532 1.00 17.50 ? 31  VAL A CA  1 
ATOM   234   C  C   . VAL A  1 58  ? 69.529  39.606  -16.808 1.00 20.84 ? 31  VAL A C   1 
ATOM   235   O  O   . VAL A  1 58  ? 70.233  38.550  -16.908 1.00 22.79 ? 31  VAL A O   1 
ATOM   236   C  CB  . VAL A  1 58  ? 71.073  41.016  -15.440 1.00 17.19 ? 31  VAL A CB  1 
ATOM   237   C  CG1 . VAL A  1 58  ? 71.358  41.970  -16.616 1.00 15.99 ? 31  VAL A CG1 1 
ATOM   238   C  CG2 . VAL A  1 58  ? 71.335  41.713  -14.099 1.00 18.43 ? 31  VAL A CG2 1 
ATOM   239   N  N   . TRP A  1 59  ? 68.661  39.978  -17.744 1.00 18.78 ? 32  TRP A N   1 
ATOM   240   C  CA  . TRP A  1 59  ? 68.565  39.123  -18.957 1.00 21.38 ? 32  TRP A CA  1 
ATOM   241   C  C   . TRP A  1 59  ? 68.071  39.922  -20.155 1.00 21.94 ? 32  TRP A C   1 
ATOM   242   O  O   . TRP A  1 59  ? 67.389  40.943  -19.991 1.00 19.61 ? 32  TRP A O   1 
ATOM   243   C  CB  . TRP A  1 59  ? 67.645  37.911  -18.728 1.00 22.01 ? 32  TRP A CB  1 
ATOM   244   C  CG  . TRP A  1 59  ? 66.159  38.270  -18.757 1.00 23.19 ? 32  TRP A CG  1 
ATOM   245   C  CD1 . TRP A  1 59  ? 65.294  38.159  -19.819 1.00 24.92 ? 32  TRP A CD1 1 
ATOM   246   C  CD2 . TRP A  1 59  ? 65.418  38.857  -17.689 1.00 24.90 ? 32  TRP A CD2 1 
ATOM   247   N  NE1 . TRP A  1 59  ? 64.059  38.653  -19.463 1.00 24.99 ? 32  TRP A NE1 1 
ATOM   248   C  CE2 . TRP A  1 59  ? 64.104  39.054  -18.150 1.00 24.17 ? 32  TRP A CE2 1 
ATOM   249   C  CE3 . TRP A  1 59  ? 65.758  39.261  -16.391 1.00 23.73 ? 32  TRP A CE3 1 
ATOM   250   C  CZ2 . TRP A  1 59  ? 63.110  39.648  -17.370 1.00 28.27 ? 32  TRP A CZ2 1 
ATOM   251   C  CZ3 . TRP A  1 59  ? 64.747  39.838  -15.578 1.00 29.58 ? 32  TRP A CZ3 1 
ATOM   252   C  CH2 . TRP A  1 59  ? 63.435  40.012  -16.080 1.00 31.48 ? 32  TRP A CH2 1 
ATOM   253   N  N   . GLY A  1 60  ? 68.327  39.410  -21.360 1.00 17.75 ? 33  GLY A N   1 
ATOM   254   C  CA  . GLY A  1 60  ? 67.860  40.114  -22.537 1.00 19.07 ? 33  GLY A CA  1 
ATOM   255   C  C   . GLY A  1 60  ? 68.707  39.681  -23.711 1.00 22.96 ? 33  GLY A C   1 
ATOM   256   O  O   . GLY A  1 60  ? 69.347  38.655  -23.653 1.00 23.95 ? 33  GLY A O   1 
ATOM   257   N  N   . SER A  1 61  ? 68.680  40.442  -24.772 1.00 22.85 ? 34  SER A N   1 
ATOM   258   C  CA  . SER A  1 61  ? 69.375  40.053  -25.974 1.00 24.32 ? 34  SER A CA  1 
ATOM   259   C  C   . SER A  1 61  ? 70.086  41.253  -26.534 1.00 24.24 ? 34  SER A C   1 
ATOM   260   O  O   . SER A  1 61  ? 69.535  42.348  -26.476 1.00 25.19 ? 34  SER A O   1 
ATOM   261   C  CB  . SER A  1 61  ? 68.326  39.564  -26.967 1.00 28.77 ? 34  SER A CB  1 
ATOM   262   O  OG  . SER A  1 61  ? 69.015  39.147  -28.108 1.00 34.03 ? 34  SER A OG  1 
ATOM   263   N  N   . ILE A  1 62  ? 71.319  41.084  -27.021 1.00 18.63 ? 35  ILE A N   1 
ATOM   264   C  CA  . ILE A  1 62  ? 72.109  42.200  -27.557 1.00 19.72 ? 35  ILE A CA  1 
ATOM   265   C  C   . ILE A  1 62  ? 72.552  41.628  -28.922 1.00 21.92 ? 35  ILE A C   1 
ATOM   266   O  O   . ILE A  1 62  ? 73.060  40.510  -28.971 1.00 21.72 ? 35  ILE A O   1 
ATOM   267   C  CB  . ILE A  1 62  ? 73.362  42.496  -26.725 1.00 18.80 ? 35  ILE A CB  1 
ATOM   268   C  CG1 . ILE A  1 62  ? 72.998  42.947  -25.286 1.00 20.13 ? 35  ILE A CG1 1 
ATOM   269   C  CG2 . ILE A  1 62  ? 74.170  43.640  -27.356 1.00 19.60 ? 35  ILE A CG2 1 
ATOM   270   C  CD1 . ILE A  1 62  ? 74.212  43.217  -24.417 1.00 20.11 ? 35  ILE A CD1 1 
ATOM   271   N  N   . LYS A  1 63  ? 72.261  42.325  -30.004 1.00 21.19 ? 36  LYS A N   1 
ATOM   272   C  CA  . LYS A  1 63  ? 72.656  41.835  -31.346 1.00 22.85 ? 36  LYS A CA  1 
ATOM   273   C  C   . LYS A  1 63  ? 73.733  42.743  -31.965 1.00 23.91 ? 36  LYS A C   1 
ATOM   274   O  O   . LYS A  1 63  ? 74.115  43.801  -31.377 1.00 19.57 ? 36  LYS A O   1 
ATOM   275   C  CB  . LYS A  1 63  ? 71.384  41.689  -32.179 1.00 26.55 ? 36  LYS A CB  1 
ATOM   276   C  CG  . LYS A  1 63  ? 70.824  43.034  -32.604 1.00 29.77 ? 36  LYS A CG  1 
ATOM   277   C  CD  . LYS A  1 63  ? 69.447  42.800  -33.196 1.00 34.47 ? 36  LYS A CD  1 
ATOM   278   C  CE  . LYS A  1 63  ? 68.791  44.126  -33.543 1.00 38.25 ? 36  LYS A CE  1 
ATOM   279   N  NZ  . LYS A  1 63  ? 67.376  43.877  -33.960 1.00 42.63 ? 36  LYS A NZ  1 
ATOM   280   N  N   . GLY A  1 64  ? 74.312  42.320  -33.117 1.00 20.14 ? 37  GLY A N   1 
ATOM   281   C  CA  . GLY A  1 64  ? 75.365  43.100  -33.745 1.00 20.30 ? 37  GLY A CA  1 
ATOM   282   C  C   . GLY A  1 64  ? 76.768  42.998  -33.180 1.00 20.09 ? 37  GLY A C   1 
ATOM   283   O  O   . GLY A  1 64  ? 77.641  43.836  -33.495 1.00 23.11 ? 37  GLY A O   1 
ATOM   284   N  N   . LEU A  1 65  ? 77.020  41.998  -32.340 1.00 20.69 ? 38  LEU A N   1 
ATOM   285   C  CA  . LEU A  1 65  ? 78.314  41.822  -31.705 1.00 20.81 ? 38  LEU A CA  1 
ATOM   286   C  C   . LEU A  1 65  ? 79.192  40.810  -32.507 1.00 23.61 ? 38  LEU A C   1 
ATOM   287   O  O   . LEU A  1 65  ? 78.647  39.899  -33.126 1.00 25.51 ? 38  LEU A O   1 
ATOM   288   C  CB  . LEU A  1 65  ? 78.137  41.226  -30.312 1.00 21.40 ? 38  LEU A CB  1 
ATOM   289   C  CG  . LEU A  1 65  ? 77.517  42.200  -29.254 1.00 21.25 ? 38  LEU A CG  1 
ATOM   290   C  CD1 . LEU A  1 65  ? 76.966  41.357  -28.094 1.00 20.97 ? 38  LEU A CD1 1 
ATOM   291   C  CD2 . LEU A  1 65  ? 78.579  43.204  -28.801 1.00 20.17 ? 38  LEU A CD2 1 
ATOM   292   N  N   . THR A  1 66  ? 80.491  40.978  -32.453 1.00 24.39 ? 39  THR A N   1 
ATOM   293   C  CA  . THR A  1 66  ? 81.420  39.928  -32.945 1.00 29.18 ? 39  THR A CA  1 
ATOM   294   C  C   . THR A  1 66  ? 81.310  38.698  -32.015 1.00 31.81 ? 39  THR A C   1 
ATOM   295   O  O   . THR A  1 66  ? 81.094  38.811  -30.788 1.00 25.80 ? 39  THR A O   1 
ATOM   296   C  CB  . THR A  1 66  ? 82.866  40.441  -33.020 1.00 30.96 ? 39  THR A CB  1 
ATOM   297   O  OG1 . THR A  1 66  ? 83.309  40.844  -31.709 1.00 33.15 ? 39  THR A OG1 1 
ATOM   298   C  CG2 . THR A  1 66  ? 82.953  41.651  -33.951 1.00 28.25 ? 39  THR A CG2 1 
ATOM   299   N  N   . GLU A  1 67  ? 81.435  37.509  -32.596 1.00 27.35 ? 40  GLU A N   1 
ATOM   300   C  CA  . GLU A  1 67  ? 81.289  36.283  -31.840 1.00 27.06 ? 40  GLU A CA  1 
ATOM   301   C  C   . GLU A  1 67  ? 82.331  36.253  -30.738 1.00 27.12 ? 40  GLU A C   1 
ATOM   302   O  O   . GLU A  1 67  ? 83.477  36.648  -30.973 1.00 29.97 ? 40  GLU A O   1 
ATOM   303   C  CB  . GLU A  1 67  ? 81.497  35.092  -32.809 1.00 28.56 ? 40  GLU A CB  1 
ATOM   304   C  CG  . GLU A  1 67  ? 81.325  33.764  -32.123 1.00 32.00 ? 40  GLU A CG  1 
ATOM   305   C  CD  . GLU A  1 67  ? 81.583  32.582  -33.066 1.00 40.51 ? 40  GLU A CD  1 
ATOM   306   O  OE1 . GLU A  1 67  ? 82.054  32.778  -34.210 1.00 36.95 ? 40  GLU A OE1 1 
ATOM   307   O  OE2 . GLU A  1 67  ? 81.272  31.464  -32.649 1.00 41.57 ? 40  GLU A OE2 1 
ATOM   308   N  N   . GLY A  1 68  ? 81.964  35.804  -29.530 1.00 25.61 ? 41  GLY A N   1 
ATOM   309   C  CA  . GLY A  1 68  ? 82.934  35.707  -28.403 1.00 26.04 ? 41  GLY A CA  1 
ATOM   310   C  C   . GLY A  1 68  ? 82.567  36.624  -27.218 1.00 24.95 ? 41  GLY A C   1 
ATOM   311   O  O   . GLY A  1 68  ? 81.433  37.124  -27.152 1.00 24.58 ? 41  GLY A O   1 
ATOM   312   N  N   . LEU A  1 69  ? 83.523  36.846  -26.329 1.00 23.29 ? 42  LEU A N   1 
ATOM   313   C  CA  . LEU A  1 69  ? 83.293  37.524  -25.045 1.00 24.61 ? 42  LEU A CA  1 
ATOM   314   C  C   . LEU A  1 69  ? 83.343  39.060  -25.173 1.00 22.92 ? 42  LEU A C   1 
ATOM   315   O  O   . LEU A  1 69  ? 84.186  39.605  -25.890 1.00 21.41 ? 42  LEU A O   1 
ATOM   316   C  CB  . LEU A  1 69  ? 84.325  37.079  -23.978 1.00 24.47 ? 42  LEU A CB  1 
ATOM   317   C  CG  . LEU A  1 69  ? 84.441  35.613  -23.503 1.00 31.42 ? 42  LEU A CG  1 
ATOM   318   C  CD1 . LEU A  1 69  ? 85.747  35.469  -22.744 1.00 30.08 ? 42  LEU A CD1 1 
ATOM   319   C  CD2 . LEU A  1 69  ? 83.275  35.210  -22.601 1.00 32.40 ? 42  LEU A CD2 1 
ATOM   320   N  N   . HIS A  1 70  ? 82.450  39.753  -24.436 1.00 20.10 ? 43  HIS A N   1 
ATOM   321   C  CA  . HIS A  1 70  ? 82.380  41.212  -24.428 1.00 19.54 ? 43  HIS A CA  1 
ATOM   322   C  C   . HIS A  1 70  ? 82.145  41.665  -22.991 1.00 19.47 ? 43  HIS A C   1 
ATOM   323   O  O   . HIS A  1 70  ? 81.258  41.138  -22.349 1.00 19.78 ? 43  HIS A O   1 
ATOM   324   C  CB  . HIS A  1 70  ? 81.212  41.674  -25.305 1.00 18.36 ? 43  HIS A CB  1 
ATOM   325   C  CG  . HIS A  1 70  ? 81.431  41.390  -26.766 1.00 19.56 ? 43  HIS A CG  1 
ATOM   326   N  ND1 . HIS A  1 70  ? 82.186  42.217  -27.572 1.00 21.93 ? 43  HIS A ND1 1 
ATOM   327   C  CD2 . HIS A  1 70  ? 81.068  40.334  -27.531 1.00 19.64 ? 43  HIS A CD2 1 
ATOM   328   C  CE1 . HIS A  1 70  ? 82.231  41.702  -28.797 1.00 23.33 ? 43  HIS A CE1 1 
ATOM   329   N  NE2 . HIS A  1 70  ? 81.552  40.566  -28.795 1.00 22.99 ? 43  HIS A NE2 1 
ATOM   330   N  N   . GLY A  1 71  ? 82.968  42.605  -22.520 1.00 17.77 ? 44  GLY A N   1 
ATOM   331   C  CA  . GLY A  1 71  ? 82.857  43.130  -21.159 1.00 18.99 ? 44  GLY A CA  1 
ATOM   332   C  C   . GLY A  1 71  ? 81.460  43.753  -20.980 1.00 18.91 ? 44  GLY A C   1 
ATOM   333   O  O   . GLY A  1 71  ? 80.896  44.281  -21.928 1.00 17.55 ? 44  GLY A O   1 
ATOM   334   N  N   . PHE A  1 72  ? 80.895  43.670  -19.775 1.00 18.71 ? 45  PHE A N   1 
ATOM   335   C  CA  . PHE A  1 72  ? 79.471  44.047  -19.599 1.00 18.86 ? 45  PHE A CA  1 
ATOM   336   C  C   . PHE A  1 72  ? 79.448  44.678  -18.227 1.00 19.19 ? 45  PHE A C   1 
ATOM   337   O  O   . PHE A  1 72  ? 79.613  43.971  -17.240 1.00 19.22 ? 45  PHE A O   1 
ATOM   338   C  CB  . PHE A  1 72  ? 78.617  42.743  -19.660 1.00 18.94 ? 45  PHE A CB  1 
ATOM   339   C  CG  . PHE A  1 72  ? 77.108  42.943  -19.612 1.00 19.02 ? 45  PHE A CG  1 
ATOM   340   C  CD1 . PHE A  1 72  ? 76.420  43.595  -20.624 1.00 21.24 ? 45  PHE A CD1 1 
ATOM   341   C  CD2 . PHE A  1 72  ? 76.396  42.473  -18.512 1.00 18.98 ? 45  PHE A CD2 1 
ATOM   342   C  CE1 . PHE A  1 72  ? 75.024  43.695  -20.591 1.00 18.75 ? 45  PHE A CE1 1 
ATOM   343   C  CE2 . PHE A  1 72  ? 75.004  42.588  -18.472 1.00 20.94 ? 45  PHE A CE2 1 
ATOM   344   C  CZ  . PHE A  1 72  ? 74.335  43.202  -19.506 1.00 19.12 ? 45  PHE A CZ  1 
ATOM   345   N  N   . HIS A  1 73  ? 79.340  46.003  -18.154 1.00 18.33 ? 46  HIS A N   1 
ATOM   346   C  CA  . HIS A  1 73  ? 79.577  46.701  -16.883 1.00 19.18 ? 46  HIS A CA  1 
ATOM   347   C  C   . HIS A  1 73  ? 78.567  47.813  -16.636 1.00 18.32 ? 46  HIS A C   1 
ATOM   348   O  O   . HIS A  1 73  ? 78.103  48.414  -17.579 1.00 16.82 ? 46  HIS A O   1 
ATOM   349   C  CB  . HIS A  1 73  ? 80.922  47.389  -16.904 1.00 21.80 ? 46  HIS A CB  1 
ATOM   350   C  CG  . HIS A  1 73  ? 82.049  46.472  -17.236 1.00 25.69 ? 46  HIS A CG  1 
ATOM   351   N  ND1 . HIS A  1 73  ? 82.945  46.747  -18.241 1.00 28.69 ? 46  HIS A ND1 1 
ATOM   352   C  CD2 . HIS A  1 73  ? 82.428  45.290  -16.704 1.00 25.34 ? 46  HIS A CD2 1 
ATOM   353   C  CE1 . HIS A  1 73  ? 83.842  45.779  -18.307 1.00 28.09 ? 46  HIS A CE1 1 
ATOM   354   N  NE2 . HIS A  1 73  ? 83.531  44.863  -17.413 1.00 26.13 ? 46  HIS A NE2 1 
ATOM   355   N  N   . VAL A  1 74  ? 78.314  48.099  -15.374 1.00 16.08 ? 47  VAL A N   1 
ATOM   356   C  CA  . VAL A  1 74  ? 77.545  49.330  -15.062 1.00 16.65 ? 47  VAL A CA  1 
ATOM   357   C  C   . VAL A  1 74  ? 78.560  50.399  -14.743 1.00 16.40 ? 47  VAL A C   1 
ATOM   358   O  O   . VAL A  1 74  ? 79.393  50.231  -13.827 1.00 18.06 ? 47  VAL A O   1 
ATOM   359   C  CB  . VAL A  1 74  ? 76.637  49.124  -13.845 1.00 15.88 ? 47  VAL A CB  1 
ATOM   360   C  CG1 . VAL A  1 74  ? 75.872  50.430  -13.523 1.00 15.56 ? 47  VAL A CG1 1 
ATOM   361   C  CG2 . VAL A  1 74  ? 75.676  47.988  -14.113 1.00 16.98 ? 47  VAL A CG2 1 
ATOM   362   N  N   . HIS A  1 75  ? 78.528  51.487  -15.517 1.00 15.60 ? 48  HIS A N   1 
ATOM   363   C  CA  . HIS A  1 75  ? 79.340  52.665  -15.316 1.00 16.22 ? 48  HIS A CA  1 
ATOM   364   C  C   . HIS A  1 75  ? 78.616  53.689  -14.431 1.00 17.90 ? 48  HIS A C   1 
ATOM   365   O  O   . HIS A  1 75  ? 77.395  53.626  -14.274 1.00 19.26 ? 48  HIS A O   1 
ATOM   366   C  CB  . HIS A  1 75  ? 79.707  53.258  -16.677 1.00 16.31 ? 48  HIS A CB  1 
ATOM   367   C  CG  . HIS A  1 75  ? 80.683  52.391  -17.430 1.00 17.76 ? 48  HIS A CG  1 
ATOM   368   N  ND1 . HIS A  1 75  ? 81.972  52.785  -17.745 1.00 19.20 ? 48  HIS A ND1 1 
ATOM   369   C  CD2 . HIS A  1 75  ? 80.547  51.125  -17.898 1.00 17.65 ? 48  HIS A CD2 1 
ATOM   370   C  CE1 . HIS A  1 75  ? 82.576  51.799  -18.415 1.00 19.97 ? 48  HIS A CE1 1 
ATOM   371   N  NE2 . HIS A  1 75  ? 81.728  50.787  -18.527 1.00 18.67 ? 48  HIS A NE2 1 
ATOM   372   N  N   . GLU A  1 76  ? 79.384  54.583  -13.818 1.00 17.77 ? 49  GLU A N   1 
ATOM   373   C  CA  . GLU A  1 76  ? 78.881  55.371  -12.693 1.00 18.47 ? 49  GLU A CA  1 
ATOM   374   C  C   . GLU A  1 76  ? 77.733  56.346  -13.083 1.00 17.51 ? 49  GLU A C   1 
ATOM   375   O  O   . GLU A  1 76  ? 76.736  56.455  -12.338 1.00 18.00 ? 49  GLU A O   1 
ATOM   376   C  CB  . GLU A  1 76  ? 80.011  56.183  -12.063 1.00 20.74 ? 49  GLU A CB  1 
ATOM   377   C  CG  . GLU A  1 76  ? 79.482  56.921  -10.834 1.00 23.69 ? 49  GLU A CG  1 
ATOM   378   C  CD  . GLU A  1 76  ? 80.591  57.512  -9.999  1.00 27.73 ? 49  GLU A CD  1 
ATOM   379   O  OE1 . GLU A  1 76  ? 81.757  57.296  -10.357 1.00 29.02 ? 49  GLU A OE1 1 
ATOM   380   O  OE2 . GLU A  1 76  ? 80.280  58.215  -9.017  1.00 30.00 ? 49  GLU A OE2 1 
ATOM   381   N  N   . PHE A  1 77  ? 77.862  57.043  -14.206 1.00 16.67 ? 50  PHE A N   1 
ATOM   382   C  CA  . PHE A  1 77  ? 76.898  58.146  -14.523 1.00 17.91 ? 50  PHE A CA  1 
ATOM   383   C  C   . PHE A  1 77  ? 75.922  57.765  -15.585 1.00 18.20 ? 50  PHE A C   1 
ATOM   384   O  O   . PHE A  1 77  ? 76.306  57.134  -16.578 1.00 18.96 ? 50  PHE A O   1 
ATOM   385   C  CB  . PHE A  1 77  ? 77.667  59.422  -14.915 1.00 19.37 ? 50  PHE A CB  1 
ATOM   386   C  CG  . PHE A  1 77  ? 78.692  59.806  -13.878 1.00 20.61 ? 50  PHE A CG  1 
ATOM   387   C  CD1 . PHE A  1 77  ? 78.268  60.213  -12.604 1.00 21.37 ? 50  PHE A CD1 1 
ATOM   388   C  CD2 . PHE A  1 77  ? 80.061  59.669  -14.137 1.00 23.51 ? 50  PHE A CD2 1 
ATOM   389   C  CE1 . PHE A  1 77  ? 79.194  60.504  -11.608 1.00 23.12 ? 50  PHE A CE1 1 
ATOM   390   C  CE2 . PHE A  1 77  ? 80.995  59.978  -13.144 1.00 24.68 ? 50  PHE A CE2 1 
ATOM   391   C  CZ  . PHE A  1 77  ? 80.549  60.383  -11.889 1.00 22.34 ? 50  PHE A CZ  1 
ATOM   392   N  N   . GLY A  1 78  ? 74.662  58.181  -15.430 1.00 18.34 ? 51  GLY A N   1 
ATOM   393   C  CA  . GLY A  1 78  ? 73.654  57.952  -16.461 1.00 17.50 ? 51  GLY A CA  1 
ATOM   394   C  C   . GLY A  1 78  ? 73.677  59.146  -17.390 1.00 19.13 ? 51  GLY A C   1 
ATOM   395   O  O   . GLY A  1 78  ? 72.649  59.748  -17.659 1.00 18.66 ? 51  GLY A O   1 
ATOM   396   N  N   . ASP A  1 79  ? 74.853  59.520  -17.877 1.00 18.98 ? 52  ASP A N   1 
ATOM   397   C  CA  . ASP A  1 79  ? 75.000  60.762  -18.657 1.00 16.25 ? 52  ASP A CA  1 
ATOM   398   C  C   . ASP A  1 79  ? 75.428  60.287  -20.047 1.00 19.59 ? 52  ASP A C   1 
ATOM   399   O  O   . ASP A  1 79  ? 76.572  59.782  -20.222 1.00 18.34 ? 52  ASP A O   1 
ATOM   400   C  CB  . ASP A  1 79  ? 76.122  61.608  -18.027 1.00 19.36 ? 52  ASP A CB  1 
ATOM   401   C  CG  . ASP A  1 79  ? 76.423  62.902  -18.799 1.00 21.37 ? 52  ASP A CG  1 
ATOM   402   O  OD1 . ASP A  1 79  ? 76.219  62.964  -20.015 1.00 22.27 ? 52  ASP A OD1 1 
ATOM   403   O  OD2 . ASP A  1 79  ? 76.926  63.858  -18.170 1.00 22.15 ? 52  ASP A OD2 1 
ATOM   404   N  N   . ASN A  1 80  ? 74.547  60.459  -21.021 1.00 19.86 ? 53  ASN A N   1 
ATOM   405   C  CA  . ASN A  1 80  ? 74.799  60.061  -22.405 1.00 20.50 ? 53  ASN A CA  1 
ATOM   406   C  C   . ASN A  1 80  ? 75.034  61.279  -23.300 1.00 17.36 ? 53  ASN A C   1 
ATOM   407   O  O   . ASN A  1 80  ? 74.931  61.186  -24.512 1.00 18.89 ? 53  ASN A O   1 
ATOM   408   C  CB  . ASN A  1 80  ? 73.536  59.306  -22.864 1.00 27.09 ? 53  ASN A CB  1 
ATOM   409   C  CG  . ASN A  1 80  ? 73.725  58.528  -24.166 1.00 37.34 ? 53  ASN A CG  1 
ATOM   410   O  OD1 . ASN A  1 80  ? 74.611  57.666  -24.273 1.00 38.27 ? 53  ASN A OD1 1 
ATOM   411   N  ND2 . ASN A  1 80  ? 72.859  58.796  -25.148 1.00 36.31 ? 53  ASN A ND2 1 
ATOM   412   N  N   . THR A  1 81  ? 75.406  62.409  -22.739 1.00 16.03 ? 54  THR A N   1 
ATOM   413   C  CA  . THR A  1 81  ? 75.560  63.639  -23.567 1.00 16.40 ? 54  THR A CA  1 
ATOM   414   C  C   . THR A  1 81  ? 76.738  63.536  -24.516 1.00 18.51 ? 54  THR A C   1 
ATOM   415   O  O   . THR A  1 81  ? 76.811  64.260  -25.525 1.00 18.90 ? 54  THR A O   1 
ATOM   416   C  CB  . THR A  1 81  ? 75.797  64.903  -22.702 1.00 17.47 ? 54  THR A CB  1 
ATOM   417   O  OG1 . THR A  1 81  ? 76.973  64.752  -21.867 1.00 19.91 ? 54  THR A OG1 1 
ATOM   418   C  CG2 . THR A  1 81  ? 74.585  65.112  -21.786 1.00 15.62 ? 54  THR A CG2 1 
ATOM   419   N  N   . ALA A  1 82  ? 77.691  62.676  -24.166 1.00 18.19 ? 55  ALA A N   1 
ATOM   420   C  CA  . ALA A  1 82  ? 78.820  62.399  -25.099 1.00 19.38 ? 55  ALA A CA  1 
ATOM   421   C  C   . ALA A  1 82  ? 78.739  60.917  -25.485 1.00 22.50 ? 55  ALA A C   1 
ATOM   422   O  O   . ALA A  1 82  ? 79.763  60.231  -25.497 1.00 21.06 ? 55  ALA A O   1 
ATOM   423   C  CB  . ALA A  1 82  ? 80.150  62.657  -24.412 1.00 20.29 ? 55  ALA A CB  1 
ATOM   424   N  N   . GLY A  1 83  ? 77.538  60.406  -25.709 1.00 20.29 ? 56  GLY A N   1 
ATOM   425   C  CA  . GLY A  1 83  ? 77.357  58.956  -25.928 1.00 20.75 ? 56  GLY A CA  1 
ATOM   426   C  C   . GLY A  1 83  ? 77.891  58.162  -24.734 1.00 20.41 ? 56  GLY A C   1 
ATOM   427   O  O   . GLY A  1 83  ? 77.749  58.569  -23.571 1.00 20.22 ? 56  GLY A O   1 
ATOM   428   N  N   . CYS A  1 84  ? 78.499  56.991  -24.993 1.00 19.56 ? 57  CYS A N   1 
ATOM   429   C  CA  . CYS A  1 84  ? 78.922  56.128  -23.877 1.00 20.59 ? 57  CYS A CA  1 
ATOM   430   C  C   . CYS A  1 84  ? 80.088  56.713  -23.058 1.00 19.96 ? 57  CYS A C   1 
ATOM   431   O  O   . CYS A  1 84  ? 80.318  56.342  -21.904 1.00 19.82 ? 57  CYS A O   1 
ATOM   432   C  CB  . CYS A  1 84  ? 79.342  54.748  -24.433 1.00 26.02 ? 57  CYS A CB  1 
ATOM   433   S  SG  . CYS A  1 84  ? 77.934  53.950  -25.261 1.00 30.98 ? 57  CYS A SG  1 
ATOM   434   N  N   . THR A  1 85  ? 80.866  57.583  -23.683 1.00 20.18 ? 58  THR A N   1 
ATOM   435   C  CA  . THR A  1 85  ? 82.040  58.193  -23.007 1.00 21.72 ? 58  THR A CA  1 
ATOM   436   C  C   . THR A  1 85  ? 81.724  58.997  -21.731 1.00 20.63 ? 58  THR A C   1 
ATOM   437   O  O   . THR A  1 85  ? 82.468  58.929  -20.729 1.00 20.43 ? 58  THR A O   1 
ATOM   438   C  CB  . THR A  1 85  ? 82.754  59.107  -24.009 1.00 24.32 ? 58  THR A CB  1 
ATOM   439   O  OG1 . THR A  1 85  ? 82.966  58.372  -25.213 1.00 27.06 ? 58  THR A OG1 1 
ATOM   440   C  CG2 . THR A  1 85  ? 84.127  59.573  -23.453 1.00 26.18 ? 58  THR A CG2 1 
ATOM   441   N  N   . SER A  1 86  ? 80.611  59.744  -21.746 1.00 18.72 ? 59  SER A N   1 
ATOM   442   C  CA  . SER A  1 86  ? 80.224  60.534  -20.554 1.00 18.07 ? 59  SER A CA  1 
ATOM   443   C  C   . SER A  1 86  ? 79.716  59.728  -19.383 1.00 18.51 ? 59  SER A C   1 
ATOM   444   O  O   . SER A  1 86  ? 79.509  60.268  -18.311 1.00 16.53 ? 59  SER A O   1 
ATOM   445   C  CB  . SER A  1 86  ? 79.183  61.613  -20.941 1.00 18.03 ? 59  SER A CB  1 
ATOM   446   O  OG  . SER A  1 86  ? 78.237  61.105  -21.871 1.00 19.06 ? 59  SER A OG  1 
ATOM   447   N  N   . ALA A  1 87  ? 79.528  58.408  -19.554 1.00 17.84 ? 60  ALA A N   1 
ATOM   448   C  CA  . ALA A  1 87  ? 79.172  57.540  -18.410 1.00 16.66 ? 60  ALA A CA  1 
ATOM   449   C  C   . ALA A  1 87  ? 80.282  57.384  -17.372 1.00 18.82 ? 60  ALA A C   1 
ATOM   450   O  O   . ALA A  1 87  ? 79.999  57.021  -16.248 1.00 18.98 ? 60  ALA A O   1 
ATOM   451   C  CB  . ALA A  1 87  ? 78.673  56.167  -18.900 1.00 16.06 ? 60  ALA A CB  1 
ATOM   452   N  N   . GLY A  1 88  ? 81.524  57.767  -17.714 1.00 18.26 ? 61  GLY A N   1 
ATOM   453   C  CA  . GLY A  1 88  ? 82.626  57.779  -16.709 1.00 17.69 ? 61  GLY A CA  1 
ATOM   454   C  C   . GLY A  1 88  ? 83.094  56.333  -16.453 1.00 19.64 ? 61  GLY A C   1 
ATOM   455   O  O   . GLY A  1 88  ? 82.813  55.480  -17.266 1.00 20.28 ? 61  GLY A O   1 
ATOM   456   N  N   . PRO A  1 89  ? 83.712  56.063  -15.309 1.00 21.01 ? 62  PRO A N   1 
ATOM   457   C  CA  . PRO A  1 89  ? 84.283  54.734  -15.018 1.00 22.39 ? 62  PRO A CA  1 
ATOM   458   C  C   . PRO A  1 89  ? 83.267  53.754  -14.455 1.00 23.18 ? 62  PRO A C   1 
ATOM   459   O  O   . PRO A  1 89  ? 82.063  54.101  -14.326 1.00 21.14 ? 62  PRO A O   1 
ATOM   460   C  CB  . PRO A  1 89  ? 85.322  55.067  -13.957 1.00 22.43 ? 62  PRO A CB  1 
ATOM   461   C  CG  . PRO A  1 89  ? 84.679  56.207  -13.164 1.00 23.31 ? 62  PRO A CG  1 
ATOM   462   C  CD  . PRO A  1 89  ? 83.979  57.025  -14.210 1.00 22.89 ? 62  PRO A CD  1 
ATOM   463   N  N   . HIS A  1 90  ? 83.728  52.531  -14.152 1.00 20.75 ? 63  HIS A N   1 
ATOM   464   C  CA  . HIS A  1 90  ? 82.827  51.470  -13.614 1.00 19.72 ? 63  HIS A CA  1 
ATOM   465   C  C   . HIS A  1 90  ? 82.286  52.002  -12.307 1.00 20.98 ? 63  HIS A C   1 
ATOM   466   O  O   . HIS A  1 90  ? 82.985  52.743  -11.602 1.00 20.11 ? 63  HIS A O   1 
ATOM   467   C  CB  . HIS A  1 90  ? 83.616  50.148  -13.371 1.00 22.06 ? 63  HIS A CB  1 
ATOM   468   C  CG  . HIS A  1 90  ? 84.052  49.481  -14.643 1.00 20.56 ? 63  HIS A CG  1 
ATOM   469   N  ND1 . HIS A  1 90  ? 84.737  48.276  -14.679 1.00 22.72 ? 63  HIS A ND1 1 
ATOM   470   C  CD2 . HIS A  1 90  ? 83.929  49.871  -15.929 1.00 20.51 ? 63  HIS A CD2 1 
ATOM   471   C  CE1 . HIS A  1 90  ? 84.992  47.951  -15.936 1.00 21.86 ? 63  HIS A CE1 1 
ATOM   472   N  NE2 . HIS A  1 90  ? 84.509  48.896  -16.719 1.00 21.59 ? 63  HIS A NE2 1 
ATOM   473   N  N   . PHE A  1 91  ? 81.022  51.711  -12.018 1.00 17.99 ? 64  PHE A N   1 
ATOM   474   C  CA  . PHE A  1 91  ? 80.409  52.157  -10.777 1.00 19.78 ? 64  PHE A CA  1 
ATOM   475   C  C   . PHE A  1 91  ? 81.119  51.417  -9.642  1.00 21.21 ? 64  PHE A C   1 
ATOM   476   O  O   . PHE A  1 91  ? 81.098  50.192  -9.562  1.00 18.58 ? 64  PHE A O   1 
ATOM   477   C  CB  . PHE A  1 91  ? 78.915  51.794  -10.815 1.00 18.82 ? 64  PHE A CB  1 
ATOM   478   C  CG  . PHE A  1 91  ? 78.155  52.100  -9.548  1.00 21.16 ? 64  PHE A CG  1 
ATOM   479   C  CD1 . PHE A  1 91  ? 78.302  53.327  -8.881  1.00 23.11 ? 64  PHE A CD1 1 
ATOM   480   C  CD2 . PHE A  1 91  ? 77.211  51.183  -9.080  1.00 20.84 ? 64  PHE A CD2 1 
ATOM   481   C  CE1 . PHE A  1 91  ? 77.532  53.580  -7.719  1.00 22.53 ? 64  PHE A CE1 1 
ATOM   482   C  CE2 . PHE A  1 91  ? 76.442  51.428  -7.939  1.00 22.67 ? 64  PHE A CE2 1 
ATOM   483   C  CZ  . PHE A  1 91  ? 76.615  52.638  -7.270  1.00 21.26 ? 64  PHE A CZ  1 
ATOM   484   N  N   . ASN A  1 92  ? 81.690  52.175  -8.719  1.00 21.94 ? 65  ASN A N   1 
ATOM   485   C  CA  . ASN A  1 92  ? 82.618  51.590  -7.739  1.00 23.31 ? 65  ASN A CA  1 
ATOM   486   C  C   . ASN A  1 92  ? 82.521  52.381  -6.429  1.00 24.43 ? 65  ASN A C   1 
ATOM   487   O  O   . ASN A  1 92  ? 83.483  52.993  -6.021  1.00 27.24 ? 65  ASN A O   1 
ATOM   488   C  CB  . ASN A  1 92  ? 84.038  51.660  -8.364  1.00 25.61 ? 65  ASN A CB  1 
ATOM   489   C  CG  . ASN A  1 92  ? 85.134  51.092  -7.455  1.00 26.23 ? 65  ASN A CG  1 
ATOM   490   O  OD1 . ASN A  1 92  ? 84.879  50.273  -6.615  1.00 26.37 ? 65  ASN A OD1 1 
ATOM   491   N  ND2 . ASN A  1 92  ? 86.357  51.536  -7.673  1.00 27.60 ? 65  ASN A ND2 1 
ATOM   492   N  N   . PRO A  1 93  ? 81.346  52.381  -5.774  1.00 24.85 ? 66  PRO A N   1 
ATOM   493   C  CA  . PRO A  1 93  ? 81.177  53.192  -4.563  1.00 28.02 ? 66  PRO A CA  1 
ATOM   494   C  C   . PRO A  1 93  ? 82.050  52.708  -3.406  1.00 35.74 ? 66  PRO A C   1 
ATOM   495   O  O   . PRO A  1 93  ? 82.308  53.500  -2.517  1.00 35.68 ? 66  PRO A O   1 
ATOM   496   C  CB  . PRO A  1 93  ? 79.733  52.958  -4.198  1.00 27.07 ? 66  PRO A CB  1 
ATOM   497   C  CG  . PRO A  1 93  ? 79.447  51.582  -4.707  1.00 25.95 ? 66  PRO A CG  1 
ATOM   498   C  CD  . PRO A  1 93  ? 80.153  51.572  -6.028  1.00 23.91 ? 66  PRO A CD  1 
ATOM   499   N  N   . LEU A  1 94  ? 82.519  51.455  -3.430  1.00 35.32 ? 67  LEU A N   1 
ATOM   500   C  CA  . LEU A  1 94  ? 83.397  50.939  -2.334  1.00 34.32 ? 67  LEU A CA  1 
ATOM   501   C  C   . LEU A  1 94  ? 84.881  51.118  -2.616  1.00 36.17 ? 67  LEU A C   1 
ATOM   502   O  O   . LEU A  1 94  ? 85.723  50.726  -1.812  1.00 35.10 ? 67  LEU A O   1 
ATOM   503   C  CB  . LEU A  1 94  ? 83.056  49.486  -1.975  1.00 36.19 ? 67  LEU A CB  1 
ATOM   504   C  CG  . LEU A  1 94  ? 81.582  49.222  -1.589  1.00 38.00 ? 67  LEU A CG  1 
ATOM   505   C  CD1 . LEU A  1 94  ? 81.260  47.753  -1.356  1.00 36.64 ? 67  LEU A CD1 1 
ATOM   506   C  CD2 . LEU A  1 94  ? 81.095  50.064  -0.406  1.00 41.55 ? 67  LEU A CD2 1 
ATOM   507   N  N   . SER A  1 95  ? 85.208  51.714  -3.760  1.00 32.83 ? 68  SER A N   1 
ATOM   508   C  CA  . SER A  1 95  ? 86.586  52.058  -4.107  1.00 34.79 ? 68  SER A CA  1 
ATOM   509   C  C   . SER A  1 95  ? 87.477  50.827  -4.119  1.00 39.67 ? 68  SER A C   1 
ATOM   510   O  O   . SER A  1 95  ? 88.570  50.827  -3.547  1.00 36.25 ? 68  SER A O   1 
ATOM   511   C  CB  . SER A  1 95  ? 87.161  53.084  -3.115  1.00 40.08 ? 68  SER A CB  1 
ATOM   512   O  OG  . SER A  1 95  ? 86.548  54.344  -3.283  1.00 46.56 ? 68  SER A OG  1 
ATOM   513   N  N   . ARG A  1 96  ? 86.998  49.771  -4.752  1.00 37.30 ? 69  ARG A N   1 
ATOM   514   C  CA  . ARG A  1 96  ? 87.780  48.562  -4.897  1.00 36.33 ? 69  ARG A CA  1 
ATOM   515   C  C   . ARG A  1 96  ? 88.494  48.515  -6.239  1.00 33.88 ? 69  ARG A C   1 
ATOM   516   O  O   . ARG A  1 96  ? 88.341  49.409  -7.078  1.00 32.59 ? 69  ARG A O   1 
ATOM   517   C  CB  . ARG A  1 96  ? 86.902  47.347  -4.676  1.00 35.16 ? 69  ARG A CB  1 
ATOM   518   C  CG  . ARG A  1 96  ? 86.264  47.387  -3.306  1.00 42.08 ? 69  ARG A CG  1 
ATOM   519   C  CD  . ARG A  1 96  ? 85.916  46.000  -2.821  1.00 51.85 ? 69  ARG A CD  1 
ATOM   520   N  NE  . ARG A  1 96  ? 85.494  46.040  -1.417  1.00 56.04 ? 69  ARG A NE  1 
ATOM   521   C  CZ  . ARG A  1 96  ? 84.714  45.130  -0.827  1.00 57.25 ? 69  ARG A CZ  1 
ATOM   522   N  NH1 . ARG A  1 96  ? 84.255  44.078  -1.503  1.00 55.69 ? 69  ARG A NH1 1 
ATOM   523   N  NH2 . ARG A  1 96  ? 84.394  45.269  0.456   1.00 58.68 ? 69  ARG A NH2 1 
ATOM   524   N  N   . LYS A  1 97  ? 89.295  47.473  -6.443  1.00 34.04 ? 70  LYS A N   1 
ATOM   525   C  CA  . LYS A  1 97  ? 89.902  47.268  -7.749  1.00 32.96 ? 70  LYS A CA  1 
ATOM   526   C  C   . LYS A  1 97  ? 88.944  46.419  -8.602  1.00 28.91 ? 70  LYS A C   1 
ATOM   527   O  O   . LYS A  1 97  ? 88.071  45.743  -8.068  1.00 26.55 ? 70  LYS A O   1 
ATOM   528   C  CB  . LYS A  1 97  ? 91.260  46.566  -7.595  1.00 39.02 ? 70  LYS A CB  1 
ATOM   529   C  CG  . LYS A  1 97  ? 92.421  47.523  -7.296  1.00 44.63 ? 70  LYS A CG  1 
ATOM   530   C  CD  . LYS A  1 97  ? 93.703  46.734  -7.060  1.00 52.78 ? 70  LYS A CD  1 
ATOM   531   C  CE  . LYS A  1 97  ? 93.443  45.615  -6.064  1.00 53.59 ? 70  LYS A CE  1 
ATOM   532   N  NZ  . LYS A  1 97  ? 94.634  45.401  -5.194  1.00 65.40 ? 70  LYS A NZ  1 
ATOM   533   N  N   . HIS A  1 98  ? 89.122  46.489  -9.912  1.00 27.46 ? 71  HIS A N   1 
ATOM   534   C  CA  . HIS A  1 98  ? 88.317  45.736  -10.857 1.00 28.58 ? 71  HIS A CA  1 
ATOM   535   C  C   . HIS A  1 98  ? 88.506  44.235  -10.662 1.00 32.83 ? 71  HIS A C   1 
ATOM   536   O  O   . HIS A  1 98  ? 89.630  43.789  -10.427 1.00 28.55 ? 71  HIS A O   1 
ATOM   537   C  CB  . HIS A  1 98  ? 88.677  46.151  -12.294 1.00 27.49 ? 71  HIS A CB  1 
ATOM   538   C  CG  . HIS A  1 98  ? 87.950  45.361  -13.347 1.00 28.70 ? 71  HIS A CG  1 
ATOM   539   N  ND1 . HIS A  1 98  ? 86.623  45.577  -13.653 1.00 25.24 ? 71  HIS A ND1 1 
ATOM   540   C  CD2 . HIS A  1 98  ? 88.350  44.332  -14.138 1.00 24.19 ? 71  HIS A CD2 1 
ATOM   541   C  CE1 . HIS A  1 98  ? 86.228  44.727  -14.579 1.00 28.50 ? 71  HIS A CE1 1 
ATOM   542   N  NE2 . HIS A  1 98  ? 87.264  43.963  -14.902 1.00 29.04 ? 71  HIS A NE2 1 
ATOM   543   N  N   . GLY A  1 99  ? 87.413  43.481  -10.775 1.00 26.21 ? 72  GLY A N   1 
ATOM   544   C  CA  . GLY A  1 99  ? 87.406  42.022  -10.672 1.00 27.73 ? 72  GLY A CA  1 
ATOM   545   C  C   . GLY A  1 99  ? 86.307  41.432  -11.535 1.00 27.53 ? 72  GLY A C   1 
ATOM   546   O  O   . GLY A  1 99  ? 85.666  42.166  -12.317 1.00 25.63 ? 72  GLY A O   1 
ATOM   547   N  N   . GLY A  1 100 ? 86.109  40.109  -11.424 1.00 24.08 ? 73  GLY A N   1 
ATOM   548   C  CA  . GLY A  1 100 ? 84.979  39.451  -12.059 1.00 24.84 ? 73  GLY A CA  1 
ATOM   549   C  C   . GLY A  1 100 ? 83.868  39.433  -11.032 1.00 25.10 ? 73  GLY A C   1 
ATOM   550   O  O   . GLY A  1 100 ? 84.135  39.703  -9.863  1.00 26.17 ? 73  GLY A O   1 
ATOM   551   N  N   . PRO A  1 101 ? 82.641  39.098  -11.448 1.00 27.81 ? 74  PRO A N   1 
ATOM   552   C  CA  . PRO A  1 101 ? 81.488  39.236  -10.535 1.00 27.31 ? 74  PRO A CA  1 
ATOM   553   C  C   . PRO A  1 101 ? 81.598  38.288  -9.377  1.00 31.26 ? 74  PRO A C   1 
ATOM   554   O  O   . PRO A  1 101 ? 81.039  38.566  -8.323  1.00 30.04 ? 74  PRO A O   1 
ATOM   555   C  CB  . PRO A  1 101 ? 80.273  38.861  -11.388 1.00 28.17 ? 74  PRO A CB  1 
ATOM   556   C  CG  . PRO A  1 101 ? 80.818  38.300  -12.678 1.00 27.65 ? 74  PRO A CG  1 
ATOM   557   C  CD  . PRO A  1 101 ? 82.221  38.830  -12.832 1.00 27.29 ? 74  PRO A CD  1 
ATOM   558   N  N   . LYS A  1 102 ? 82.300  37.168  -9.558  1.00 30.49 ? 75  LYS A N   1 
ATOM   559   C  CA  . LYS A  1 102 ? 82.412  36.214  -8.454  1.00 33.08 ? 75  LYS A CA  1 
ATOM   560   C  C   . LYS A  1 102 ? 83.503  36.571  -7.459  1.00 32.63 ? 75  LYS A C   1 
ATOM   561   O  O   . LYS A  1 102 ? 83.581  35.958  -6.430  1.00 37.66 ? 75  LYS A O   1 
ATOM   562   C  CB  . LYS A  1 102 ? 82.570  34.790  -8.988  1.00 37.31 ? 75  LYS A CB  1 
ATOM   563   C  CG  . LYS A  1 102 ? 81.288  34.252  -9.605  1.00 42.77 ? 75  LYS A CG  1 
ATOM   564   C  CD  . LYS A  1 102 ? 81.409  32.767  -9.942  1.00 55.86 ? 75  LYS A CD  1 
ATOM   565   C  CE  . LYS A  1 102 ? 81.477  32.491  -11.450 1.00 55.62 ? 75  LYS A CE  1 
ATOM   566   N  NZ  . LYS A  1 102 ? 80.110  32.331  -12.062 1.00 56.57 ? 75  LYS A NZ  1 
ATOM   567   N  N   . ASP A  1 103 ? 84.339  37.564  -7.743  1.00 32.50 ? 76  ASP A N   1 
ATOM   568   C  CA  . ASP A  1 103 ? 85.393  38.003  -6.817  1.00 33.74 ? 76  ASP A CA  1 
ATOM   569   C  C   . ASP A  1 103 ? 84.876  38.831  -5.663  1.00 40.22 ? 76  ASP A C   1 
ATOM   570   O  O   . ASP A  1 103 ? 83.969  39.633  -5.833  1.00 40.36 ? 76  ASP A O   1 
ATOM   571   C  CB  . ASP A  1 103 ? 86.447  38.841  -7.546  1.00 34.35 ? 76  ASP A CB  1 
ATOM   572   C  CG  . ASP A  1 103 ? 87.243  38.029  -8.509  1.00 36.84 ? 76  ASP A CG  1 
ATOM   573   O  OD1 . ASP A  1 103 ? 87.336  36.834  -8.227  1.00 40.15 ? 76  ASP A OD1 1 
ATOM   574   O  OD2 . ASP A  1 103 ? 87.738  38.544  -9.538  1.00 35.23 ? 76  ASP A OD2 1 
ATOM   575   N  N   . GLU A  1 104 ? 85.477  38.673  -4.487  1.00 40.83 ? 77  GLU A N   1 
ATOM   576   C  CA  . GLU A  1 104 ? 85.247  39.615  -3.400  1.00 40.67 ? 77  GLU A CA  1 
ATOM   577   C  C   . GLU A  1 104 ? 85.778  40.976  -3.782  1.00 37.61 ? 77  GLU A C   1 
ATOM   578   O  O   . GLU A  1 104 ? 85.107  41.982  -3.586  1.00 37.89 ? 77  GLU A O   1 
ATOM   579   C  CB  . GLU A  1 104 ? 85.878  39.139  -2.069  1.00 51.30 ? 77  GLU A CB  1 
ATOM   580   C  CG  . GLU A  1 104 ? 85.596  40.053  -0.867  1.00 58.30 ? 77  GLU A CG  1 
ATOM   581   C  CD  . GLU A  1 104 ? 84.101  40.112  -0.476  1.00 71.35 ? 77  GLU A CD  1 
ATOM   582   O  OE1 . GLU A  1 104 ? 83.351  39.115  -0.704  1.00 69.45 ? 77  GLU A OE1 1 
ATOM   583   O  OE2 . GLU A  1 104 ? 83.660  41.160  0.070   1.00 71.38 ? 77  GLU A OE2 1 
ATOM   584   N  N   . GLU A  1 105 ? 86.964  41.029  -4.370  1.00 34.58 ? 78  GLU A N   1 
ATOM   585   C  CA  . GLU A  1 105 ? 87.520  42.305  -4.778  1.00 33.60 ? 78  GLU A CA  1 
ATOM   586   C  C   . GLU A  1 105 ? 86.988  42.662  -6.193  1.00 32.18 ? 78  GLU A C   1 
ATOM   587   O  O   . GLU A  1 105 ? 87.501  42.181  -7.212  1.00 29.55 ? 78  GLU A O   1 
ATOM   588   C  CB  . GLU A  1 105 ? 89.064  42.260  -4.777  1.00 36.75 ? 78  GLU A CB  1 
ATOM   589   C  CG  . GLU A  1 105 ? 89.749  43.570  -5.169  1.00 37.51 ? 78  GLU A CG  1 
ATOM   590   C  CD  . GLU A  1 105 ? 89.714  44.590  -4.031  1.00 42.97 ? 78  GLU A CD  1 
ATOM   591   O  OE1 . GLU A  1 105 ? 89.318  44.212  -2.894  1.00 45.75 ? 78  GLU A OE1 1 
ATOM   592   O  OE2 . GLU A  1 105 ? 90.103  45.767  -4.249  1.00 38.44 ? 78  GLU A OE2 1 
ATOM   593   N  N   . ARG A  1 106 ? 85.955  43.508  -6.257  1.00 29.05 ? 79  ARG A N   1 
ATOM   594   C  CA  . ARG A  1 106 ? 85.369  43.883  -7.568  1.00 26.70 ? 79  ARG A CA  1 
ATOM   595   C  C   . ARG A  1 106 ? 84.702  45.255  -7.425  1.00 26.78 ? 79  ARG A C   1 
ATOM   596   O  O   . ARG A  1 106 ? 84.439  45.703  -6.314  1.00 28.84 ? 79  ARG A O   1 
ATOM   597   C  CB  . ARG A  1 106 ? 84.318  42.849  -8.031  1.00 23.73 ? 79  ARG A CB  1 
ATOM   598   C  CG  . ARG A  1 106 ? 83.236  42.545  -7.002  1.00 24.82 ? 79  ARG A CG  1 
ATOM   599   C  CD  . ARG A  1 106 ? 82.079  41.827  -7.623  1.00 26.50 ? 79  ARG A CD  1 
ATOM   600   N  NE  . ARG A  1 106 ? 81.093  42.708  -8.267  1.00 24.64 ? 79  ARG A NE  1 
ATOM   601   C  CZ  . ARG A  1 106 ? 79.882  42.291  -8.617  1.00 23.57 ? 79  ARG A CZ  1 
ATOM   602   N  NH1 . ARG A  1 106 ? 79.533  41.018  -8.404  1.00 22.15 ? 79  ARG A NH1 1 
ATOM   603   N  NH2 . ARG A  1 106 ? 79.007  43.132  -9.186  1.00 22.58 ? 79  ARG A NH2 1 
ATOM   604   N  N   . HIS A  1 107 ? 84.438  45.896  -8.547  1.00 24.53 ? 80  HIS A N   1 
ATOM   605   C  CA  . HIS A  1 107 ? 83.526  47.066  -8.538  1.00 25.83 ? 80  HIS A CA  1 
ATOM   606   C  C   . HIS A  1 107 ? 82.078  46.588  -8.405  1.00 22.09 ? 80  HIS A C   1 
ATOM   607   O  O   . HIS A  1 107 ? 81.724  45.445  -8.801  1.00 21.78 ? 80  HIS A O   1 
ATOM   608   C  CB  . HIS A  1 107 ? 83.703  47.827  -9.836  1.00 23.81 ? 80  HIS A CB  1 
ATOM   609   C  CG  . HIS A  1 107 ? 85.101  48.299  -10.076 1.00 24.35 ? 80  HIS A CG  1 
ATOM   610   N  ND1 . HIS A  1 107 ? 85.623  48.440  -11.337 1.00 22.91 ? 80  HIS A ND1 1 
ATOM   611   C  CD2 . HIS A  1 107 ? 86.089  48.686  -9.224  1.00 24.85 ? 80  HIS A CD2 1 
ATOM   612   C  CE1 . HIS A  1 107 ? 86.845  48.940  -11.270 1.00 23.74 ? 80  HIS A CE1 1 
ATOM   613   N  NE2 . HIS A  1 107 ? 87.151  49.089  -9.996  1.00 24.66 ? 80  HIS A NE2 1 
ATOM   614   N  N   . VAL A  1 108 ? 81.179  47.438  -7.888  1.00 22.21 ? 81  VAL A N   1 
ATOM   615   C  CA  . VAL A  1 108 ? 79.776  47.006  -7.840  1.00 19.00 ? 81  VAL A CA  1 
ATOM   616   C  C   . VAL A  1 108 ? 79.308  46.790  -9.300  1.00 18.00 ? 81  VAL A C   1 
ATOM   617   O  O   . VAL A  1 108 ? 78.542  45.877  -9.603  1.00 21.36 ? 81  VAL A O   1 
ATOM   618   C  CB  . VAL A  1 108 ? 78.878  48.076  -7.104  1.00 21.24 ? 81  VAL A CB  1 
ATOM   619   C  CG1 . VAL A  1 108 ? 77.386  47.808  -7.417  1.00 19.13 ? 81  VAL A CG1 1 
ATOM   620   C  CG2 . VAL A  1 108 ? 79.166  48.022  -5.612  1.00 22.28 ? 81  VAL A CG2 1 
ATOM   621   N  N   . GLY A  1 109 ? 79.801  47.614  -10.209 1.00 19.32 ? 82  GLY A N   1 
ATOM   622   C  CA  . GLY A  1 109 ? 79.394  47.538  -11.634 1.00 19.78 ? 82  GLY A CA  1 
ATOM   623   C  C   . GLY A  1 109 ? 80.065  46.410  -12.438 1.00 21.68 ? 82  GLY A C   1 
ATOM   624   O  O   . GLY A  1 109 ? 79.781  46.250  -13.613 1.00 20.10 ? 82  GLY A O   1 
ATOM   625   N  N   . ASP A  1 110 ? 80.873  45.565  -11.785 1.00 20.76 ? 83  ASP A N   1 
ATOM   626   C  CA  . ASP A  1 110 ? 81.563  44.431  -12.489 1.00 21.84 ? 83  ASP A CA  1 
ATOM   627   C  C   . ASP A  1 110 ? 80.672  43.235  -12.772 1.00 20.28 ? 83  ASP A C   1 
ATOM   628   O  O   . ASP A  1 110 ? 80.665  42.284  -12.018 1.00 25.01 ? 83  ASP A O   1 
ATOM   629   C  CB  . ASP A  1 110 ? 82.844  44.024  -11.717 1.00 21.01 ? 83  ASP A CB  1 
ATOM   630   C  CG  . ASP A  1 110 ? 83.930  45.070  -11.796 1.00 21.08 ? 83  ASP A CG  1 
ATOM   631   O  OD1 . ASP A  1 110 ? 83.848  45.886  -12.733 1.00 20.09 ? 83  ASP A OD1 1 
ATOM   632   O  OD2 . ASP A  1 110 ? 84.918  45.062  -10.972 1.00 24.89 ? 83  ASP A OD2 1 
ATOM   633   N  N   . LEU A  1 111 ? 79.946  43.254  -13.894 1.00 19.28 ? 84  LEU A N   1 
ATOM   634   C  CA  . LEU A  1 111 ? 79.109  42.138  -14.243 1.00 19.77 ? 84  LEU A CA  1 
ATOM   635   C  C   . LEU A  1 111 ? 79.814  41.109  -15.166 1.00 23.07 ? 84  LEU A C   1 
ATOM   636   O  O   . LEU A  1 111 ? 79.135  40.212  -15.702 1.00 25.02 ? 84  LEU A O   1 
ATOM   637   C  CB  . LEU A  1 111 ? 77.788  42.586  -14.918 1.00 19.43 ? 84  LEU A CB  1 
ATOM   638   C  CG  . LEU A  1 111 ? 76.990  43.481  -13.939 1.00 21.56 ? 84  LEU A CG  1 
ATOM   639   C  CD1 . LEU A  1 111 ? 75.732  43.926  -14.657 1.00 20.31 ? 84  LEU A CD1 1 
ATOM   640   C  CD2 . LEU A  1 111 ? 76.654  42.642  -12.722 1.00 23.09 ? 84  LEU A CD2 1 
ATOM   641   N  N   . GLY A  1 112 ? 81.131  41.251  -15.403 1.00 23.84 ? 85  GLY A N   1 
ATOM   642   C  CA  . GLY A  1 112 ? 81.858  40.149  -16.139 1.00 22.00 ? 85  GLY A CA  1 
ATOM   643   C  C   . GLY A  1 112 ? 81.687  40.316  -17.637 1.00 22.98 ? 85  GLY A C   1 
ATOM   644   O  O   . GLY A  1 112 ? 81.725  41.422  -18.155 1.00 21.60 ? 85  GLY A O   1 
ATOM   645   N  N   . ASN A  1 113 ? 81.558  39.200  -18.334 1.00 19.21 ? 86  ASN A N   1 
ATOM   646   C  CA  . ASN A  1 113 ? 81.384  39.195  -19.749 1.00 20.43 ? 86  ASN A CA  1 
ATOM   647   C  C   . ASN A  1 113 ? 80.036  38.624  -20.148 1.00 18.96 ? 86  ASN A C   1 
ATOM   648   O  O   . ASN A  1 113 ? 79.425  37.856  -19.396 1.00 21.48 ? 86  ASN A O   1 
ATOM   649   C  CB  . ASN A  1 113 ? 82.421  38.218  -20.354 1.00 20.57 ? 86  ASN A CB  1 
ATOM   650   C  CG  . ASN A  1 113 ? 83.833  38.774  -20.297 1.00 24.85 ? 86  ASN A CG  1 
ATOM   651   O  OD1 . ASN A  1 113 ? 84.126  39.781  -20.948 1.00 23.74 ? 86  ASN A OD1 1 
ATOM   652   N  ND2 . ASN A  1 113 ? 84.708  38.147  -19.485 1.00 22.93 ? 86  ASN A ND2 1 
ATOM   653   N  N   . VAL A  1 114 ? 79.621  38.978  -21.360 1.00 19.41 ? 87  VAL A N   1 
ATOM   654   C  CA  . VAL A  1 114 ? 78.554  38.277  -22.048 1.00 18.46 ? 87  VAL A CA  1 
ATOM   655   C  C   . VAL A  1 114 ? 79.137  37.668  -23.337 1.00 22.01 ? 87  VAL A C   1 
ATOM   656   O  O   . VAL A  1 114 ? 80.123  38.184  -23.889 1.00 24.47 ? 87  VAL A O   1 
ATOM   657   C  CB  . VAL A  1 114 ? 77.335  39.182  -22.403 1.00 18.86 ? 87  VAL A CB  1 
ATOM   658   C  CG1 . VAL A  1 114 ? 76.658  39.610  -21.086 1.00 18.76 ? 87  VAL A CG1 1 
ATOM   659   C  CG2 . VAL A  1 114 ? 77.745  40.400  -23.270 1.00 17.41 ? 87  VAL A CG2 1 
ATOM   660   N  N   . THR A  1 115 ? 78.499  36.615  -23.812 1.00 20.96 ? 88  THR A N   1 
ATOM   661   C  CA  . THR A  1 115 ? 79.043  35.835  -24.950 1.00 22.93 ? 88  THR A CA  1 
ATOM   662   C  C   . THR A  1 115 ? 78.112  35.929  -26.132 1.00 21.40 ? 88  THR A C   1 
ATOM   663   O  O   . THR A  1 115 ? 76.932  35.639  -26.021 1.00 23.42 ? 88  THR A O   1 
ATOM   664   C  CB  . THR A  1 115 ? 79.174  34.327  -24.563 1.00 24.23 ? 88  THR A CB  1 
ATOM   665   O  OG1 . THR A  1 115 ? 80.087  34.222  -23.470 1.00 25.42 ? 88  THR A OG1 1 
ATOM   666   C  CG2 . THR A  1 115 ? 79.673  33.487  -25.781 1.00 24.05 ? 88  THR A CG2 1 
ATOM   667   N  N   . ALA A  1 116 ? 78.623  36.402  -27.254 1.00 21.44 ? 89  ALA A N   1 
ATOM   668   C  CA  . ALA A  1 116 ? 77.820  36.478  -28.452 1.00 22.12 ? 89  ALA A CA  1 
ATOM   669   C  C   . ALA A  1 116 ? 78.098  35.181  -29.252 1.00 25.25 ? 89  ALA A C   1 
ATOM   670   O  O   . ALA A  1 116 ? 79.256  34.764  -29.335 1.00 24.36 ? 89  ALA A O   1 
ATOM   671   C  CB  . ALA A  1 116 ? 78.274  37.668  -29.268 1.00 20.91 ? 89  ALA A CB  1 
ATOM   672   N  N   . ASP A  1 117 ? 77.039  34.622  -29.816 1.00 25.59 ? 90  ASP A N   1 
ATOM   673   C  CA  . ASP A  1 117 ? 77.092  33.386  -30.612 1.00 29.97 ? 90  ASP A CA  1 
ATOM   674   C  C   . ASP A  1 117 ? 77.517  33.699  -32.053 1.00 30.65 ? 90  ASP A C   1 
ATOM   675   O  O   . ASP A  1 117 ? 77.912  34.834  -32.375 1.00 24.45 ? 90  ASP A O   1 
ATOM   676   C  CB  . ASP A  1 117 ? 75.755  32.646  -30.543 1.00 29.02 ? 90  ASP A CB  1 
ATOM   677   C  CG  . ASP A  1 117 ? 74.599  33.391  -31.247 1.00 30.31 ? 90  ASP A CG  1 
ATOM   678   O  OD1 . ASP A  1 117 ? 74.818  34.301  -32.092 1.00 29.29 ? 90  ASP A OD1 1 
ATOM   679   O  OD2 . ASP A  1 117 ? 73.433  33.050  -30.952 1.00 31.43 ? 90  ASP A OD2 1 
ATOM   680   N  N   . LYS A  1 118 ? 77.477  32.698  -32.933 1.00 30.06 ? 91  LYS A N   1 
ATOM   681   C  CA  . LYS A  1 118 ? 78.040  32.922  -34.270 1.00 33.02 ? 91  LYS A CA  1 
ATOM   682   C  C   . LYS A  1 118 ? 77.194  33.853  -35.127 1.00 27.92 ? 91  LYS A C   1 
ATOM   683   O  O   . LYS A  1 118 ? 77.669  34.331  -36.144 1.00 31.72 ? 91  LYS A O   1 
ATOM   684   C  CB  . LYS A  1 118 ? 78.271  31.568  -35.009 1.00 36.20 ? 91  LYS A CB  1 
ATOM   685   C  CG  . LYS A  1 118 ? 76.982  30.796  -35.252 1.00 44.95 ? 91  LYS A CG  1 
ATOM   686   C  CD  . LYS A  1 118 ? 77.250  29.554  -36.126 1.00 55.31 ? 91  LYS A CD  1 
ATOM   687   C  CE  . LYS A  1 118 ? 76.355  28.377  -35.745 1.00 53.92 ? 91  LYS A CE  1 
ATOM   688   N  NZ  . LYS A  1 118 ? 74.895  28.640  -35.908 1.00 61.85 ? 91  LYS A NZ  1 
ATOM   689   N  N   . ASP A  1 119 ? 75.929  34.057  -34.748 1.00 27.99 ? 92  ASP A N   1 
ATOM   690   C  CA  . ASP A  1 119 ? 75.040  35.011  -35.395 1.00 27.95 ? 92  ASP A CA  1 
ATOM   691   C  C   . ASP A  1 119 ? 75.076  36.449  -34.812 1.00 28.40 ? 92  ASP A C   1 
ATOM   692   O  O   . ASP A  1 119 ? 74.257  37.299  -35.198 1.00 27.86 ? 92  ASP A O   1 
ATOM   693   C  CB  . ASP A  1 119 ? 73.626  34.495  -35.349 1.00 32.23 ? 92  ASP A CB  1 
ATOM   694   C  CG  . ASP A  1 119 ? 73.463  33.249  -36.223 1.00 43.78 ? 92  ASP A CG  1 
ATOM   695   O  OD1 . ASP A  1 119 ? 74.067  33.234  -37.312 1.00 46.80 ? 92  ASP A OD1 1 
ATOM   696   O  OD2 . ASP A  1 119 ? 72.800  32.291  -35.794 1.00 45.80 ? 92  ASP A OD2 1 
ATOM   697   N  N   . GLY A  1 120 ? 75.988  36.689  -33.895 1.00 24.07 ? 93  GLY A N   1 
ATOM   698   C  CA  . GLY A  1 120 ? 76.220  38.048  -33.423 1.00 26.51 ? 93  GLY A CA  1 
ATOM   699   C  C   . GLY A  1 120 ? 75.385  38.396  -32.201 1.00 25.26 ? 93  GLY A C   1 
ATOM   700   O  O   . GLY A  1 120 ? 75.335  39.575  -31.832 1.00 27.20 ? 93  GLY A O   1 
ATOM   701   N  N   . VAL A  1 121 ? 74.717  37.400  -31.619 1.00 23.86 ? 94  VAL A N   1 
ATOM   702   C  CA  . VAL A  1 121 ? 73.711  37.607  -30.549 1.00 25.26 ? 94  VAL A CA  1 
ATOM   703   C  C   . VAL A  1 121 ? 74.232  37.116  -29.200 1.00 26.47 ? 94  VAL A C   1 
ATOM   704   O  O   . VAL A  1 121 ? 74.686  35.950  -29.069 1.00 22.99 ? 94  VAL A O   1 
ATOM   705   C  CB  . VAL A  1 121 ? 72.362  36.937  -30.884 1.00 27.82 ? 94  VAL A CB  1 
ATOM   706   C  CG1 . VAL A  1 121 ? 71.349  37.068  -29.725 1.00 26.28 ? 94  VAL A CG1 1 
ATOM   707   C  CG2 . VAL A  1 121 ? 71.789  37.522  -32.174 1.00 30.39 ? 94  VAL A CG2 1 
ATOM   708   N  N   . ALA A  1 122 ? 74.173  37.992  -28.189 1.00 23.00 ? 95  ALA A N   1 
ATOM   709   C  CA  . ALA A  1 122 ? 74.412  37.568  -26.816 1.00 22.91 ? 95  ALA A CA  1 
ATOM   710   C  C   . ALA A  1 122 ? 73.052  37.457  -26.132 1.00 24.60 ? 95  ALA A C   1 
ATOM   711   O  O   . ALA A  1 122 ? 72.345  38.487  -25.981 1.00 22.59 ? 95  ALA A O   1 
ATOM   712   C  CB  . ALA A  1 122 ? 75.333  38.591  -26.062 1.00 21.84 ? 95  ALA A CB  1 
ATOM   713   N  N   . ASP A  1 123 ? 72.658  36.238  -25.755 1.00 22.27 ? 96  ASP A N   1 
ATOM   714   C  CA  . ASP A  1 123 ? 71.424  36.021  -24.964 1.00 24.38 ? 96  ASP A CA  1 
ATOM   715   C  C   . ASP A  1 123 ? 71.787  36.035  -23.501 1.00 23.58 ? 96  ASP A C   1 
ATOM   716   O  O   . ASP A  1 123 ? 72.138  35.012  -22.861 1.00 21.85 ? 96  ASP A O   1 
ATOM   717   C  CB  . ASP A  1 123 ? 70.732  34.741  -25.339 1.00 28.67 ? 96  ASP A CB  1 
ATOM   718   C  CG  . ASP A  1 123 ? 70.082  34.823  -26.727 1.00 36.53 ? 96  ASP A CG  1 
ATOM   719   O  OD1 . ASP A  1 123 ? 69.347  35.818  -27.043 1.00 37.13 ? 96  ASP A OD1 1 
ATOM   720   O  OD2 . ASP A  1 123 ? 70.328  33.879  -27.519 1.00 37.69 ? 96  ASP A OD2 1 
ATOM   721   N  N   . VAL A  1 124 ? 71.721  37.232  -22.948 1.00 19.33 ? 97  VAL A N   1 
ATOM   722   C  CA  . VAL A  1 124 ? 72.322  37.499  -21.656 1.00 18.33 ? 97  VAL A CA  1 
ATOM   723   C  C   . VAL A  1 124 ? 71.478  36.830  -20.597 1.00 17.86 ? 97  VAL A C   1 
ATOM   724   O  O   . VAL A  1 124 ? 70.267  36.943  -20.612 1.00 19.04 ? 97  VAL A O   1 
ATOM   725   C  CB  . VAL A  1 124 ? 72.339  39.039  -21.381 1.00 17.47 ? 97  VAL A CB  1 
ATOM   726   C  CG1 . VAL A  1 124 ? 72.932  39.335  -20.007 1.00 18.59 ? 97  VAL A CG1 1 
ATOM   727   C  CG2 . VAL A  1 124 ? 73.144  39.731  -22.459 1.00 18.37 ? 97  VAL A CG2 1 
ATOM   728   N  N   . SER A  1 125 ? 72.143  36.211  -19.624 1.00 20.32 ? 98  SER A N   1 
ATOM   729   C  CA  . SER A  1 125 ? 71.489  35.691  -18.462 1.00 22.16 ? 98  SER A CA  1 
ATOM   730   C  C   . SER A  1 125 ? 72.461  35.677  -17.287 1.00 25.51 ? 98  SER A C   1 
ATOM   731   O  O   . SER A  1 125 ? 73.433  34.901  -17.247 1.00 26.24 ? 98  SER A O   1 
ATOM   732   C  CB  . SER A  1 125 ? 70.973  34.278  -18.786 1.00 29.97 ? 98  SER A CB  1 
ATOM   733   O  OG  . SER A  1 125 ? 70.322  33.773  -17.659 1.00 29.95 ? 98  SER A OG  1 
ATOM   734   N  N   . ILE A  1 126 ? 72.264  36.588  -16.333 1.00 21.89 ? 99  ILE A N   1 
ATOM   735   C  CA  . ILE A  1 126 ? 73.203  36.805  -15.252 1.00 23.82 ? 99  ILE A CA  1 
ATOM   736   C  C   . ILE A  1 126 ? 72.343  36.949  -13.974 1.00 24.09 ? 99  ILE A C   1 
ATOM   737   O  O   . ILE A  1 126 ? 71.191  37.432  -14.058 1.00 21.96 ? 99  ILE A O   1 
ATOM   738   C  CB  . ILE A  1 126 ? 74.017  38.099  -15.526 1.00 24.76 ? 99  ILE A CB  1 
ATOM   739   C  CG1 . ILE A  1 126 ? 75.129  37.809  -16.543 1.00 26.09 ? 99  ILE A CG1 1 
ATOM   740   C  CG2 . ILE A  1 126 ? 74.729  38.671  -14.265 1.00 24.77 ? 99  ILE A CG2 1 
ATOM   741   C  CD1 . ILE A  1 126 ? 75.766  39.061  -17.105 1.00 25.88 ? 99  ILE A CD1 1 
ATOM   742   N  N   . GLU A  1 127 ? 72.853  36.456  -12.845 1.00 22.10 ? 100 GLU A N   1 
ATOM   743   C  CA  . GLU A  1 127 ? 72.267  36.787  -11.540 1.00 25.50 ? 100 GLU A CA  1 
ATOM   744   C  C   . GLU A  1 127 ? 73.358  37.325  -10.653 1.00 26.65 ? 100 GLU A C   1 
ATOM   745   O  O   . GLU A  1 127 ? 74.461  36.759  -10.586 1.00 24.39 ? 100 GLU A O   1 
ATOM   746   C  CB  . GLU A  1 127 ? 71.552  35.569  -10.981 1.00 29.03 ? 100 GLU A CB  1 
ATOM   747   C  CG  . GLU A  1 127 ? 70.982  35.761  -9.610  1.00 34.64 ? 100 GLU A CG  1 
ATOM   748   C  CD  . GLU A  1 127 ? 70.296  34.483  -9.138  1.00 43.35 ? 100 GLU A CD  1 
ATOM   749   O  OE1 . GLU A  1 127 ? 69.568  33.857  -9.951  1.00 46.86 ? 100 GLU A OE1 1 
ATOM   750   O  OE2 . GLU A  1 127 ? 70.529  34.107  -7.975  1.00 48.87 ? 100 GLU A OE2 1 
ATOM   751   N  N   . ASP A  1 128 ? 73.132  38.484  -10.033 1.00 21.94 ? 101 ASP A N   1 
ATOM   752   C  CA  . ASP A  1 128 ? 74.213  39.118  -9.334  1.00 22.99 ? 101 ASP A CA  1 
ATOM   753   C  C   . ASP A  1 128 ? 73.694  39.582  -7.965  1.00 27.94 ? 101 ASP A C   1 
ATOM   754   O  O   . ASP A  1 128 ? 72.584  40.128  -7.906  1.00 25.13 ? 101 ASP A O   1 
ATOM   755   C  CB  . ASP A  1 128 ? 74.752  40.315  -10.074 1.00 24.46 ? 101 ASP A CB  1 
ATOM   756   C  CG  . ASP A  1 128 ? 76.057  40.782  -9.470  1.00 28.37 ? 101 ASP A CG  1 
ATOM   757   O  OD1 . ASP A  1 128 ? 77.078  40.071  -9.683  1.00 29.00 ? 101 ASP A OD1 1 
ATOM   758   O  OD2 . ASP A  1 128 ? 76.103  41.800  -8.724  1.00 25.81 ? 101 ASP A OD2 1 
ATOM   759   N  N   . SER A  1 129 ? 74.488  39.435  -6.899  1.00 27.15 ? 102 SER A N   1 
ATOM   760   C  CA  A SER A  1 129 ? 74.043  39.797  -5.547  0.50 26.45 ? 102 SER A CA  1 
ATOM   761   C  CA  B SER A  1 129 ? 74.006  39.821  -5.567  0.50 26.64 ? 102 SER A CA  1 
ATOM   762   C  C   . SER A  1 129 ? 74.727  41.039  -5.044  1.00 25.93 ? 102 SER A C   1 
ATOM   763   O  O   . SER A  1 129 ? 74.555  41.439  -3.887  1.00 27.48 ? 102 SER A O   1 
ATOM   764   C  CB  A SER A  1 129 ? 74.293  38.638  -4.573  0.50 30.17 ? 102 SER A CB  1 
ATOM   765   C  CB  B SER A  1 129 ? 74.140  38.649  -4.594  0.50 30.67 ? 102 SER A CB  1 
ATOM   766   O  OG  A SER A  1 129 ? 73.321  37.630  -4.735  0.50 27.54 ? 102 SER A OG  1 
ATOM   767   O  OG  B SER A  1 129 ? 75.476  38.196  -4.582  0.50 28.63 ? 102 SER A OG  1 
ATOM   768   N  N   . VAL A  1 130 ? 75.532  41.662  -5.884  1.00 22.06 ? 103 VAL A N   1 
ATOM   769   C  CA  . VAL A  1 130 ? 76.240  42.812  -5.423  1.00 21.08 ? 103 VAL A CA  1 
ATOM   770   C  C   . VAL A  1 130 ? 75.523  44.091  -5.935  1.00 24.03 ? 103 VAL A C   1 
ATOM   771   O  O   . VAL A  1 130 ? 75.317  45.038  -5.168  1.00 22.58 ? 103 VAL A O   1 
ATOM   772   C  CB  . VAL A  1 130 ? 77.721  42.813  -5.824  1.00 23.87 ? 103 VAL A CB  1 
ATOM   773   C  CG1 . VAL A  1 130 ? 78.317  44.181  -5.554  1.00 22.02 ? 103 VAL A CG1 1 
ATOM   774   C  CG2 . VAL A  1 130 ? 78.497  41.758  -5.003  1.00 27.56 ? 103 VAL A CG2 1 
ATOM   775   N  N   . ILE A  1 131 ? 75.130  44.101  -7.211  1.00 19.59 ? 104 ILE A N   1 
ATOM   776   C  CA  . ILE A  1 131 ? 74.251  45.234  -7.703  1.00 18.44 ? 104 ILE A CA  1 
ATOM   777   C  C   . ILE A  1 131 ? 72.881  45.191  -6.996  1.00 19.04 ? 104 ILE A C   1 
ATOM   778   O  O   . ILE A  1 131 ? 72.409  44.119  -6.538  1.00 19.30 ? 104 ILE A O   1 
ATOM   779   C  CB  . ILE A  1 131 ? 74.029  45.176  -9.232  1.00 18.63 ? 104 ILE A CB  1 
ATOM   780   C  CG1 . ILE A  1 131 ? 73.505  43.794  -9.687  1.00 18.34 ? 104 ILE A CG1 1 
ATOM   781   C  CG2 . ILE A  1 131 ? 75.324  45.486  -9.976  1.00 19.02 ? 104 ILE A CG2 1 
ATOM   782   C  CD1 . ILE A  1 131 ? 72.860  43.811  -11.093 1.00 18.28 ? 104 ILE A CD1 1 
ATOM   783   N  N   . SER A  1 132 ? 72.168  46.325  -6.983  1.00 18.12 ? 105 SER A N   1 
ATOM   784   C  CA  . SER A  1 132 ? 70.801  46.291  -6.452  1.00 17.62 ? 105 SER A CA  1 
ATOM   785   C  C   . SER A  1 132 ? 69.975  47.304  -7.260  1.00 17.69 ? 105 SER A C   1 
ATOM   786   O  O   . SER A  1 132 ? 70.547  48.129  -7.960  1.00 17.71 ? 105 SER A O   1 
ATOM   787   C  CB  . SER A  1 132 ? 70.809  46.746  -4.966  1.00 18.93 ? 105 SER A CB  1 
ATOM   788   O  OG  . SER A  1 132 ? 69.549  46.417  -4.388  1.00 18.07 ? 105 SER A OG  1 
ATOM   789   N  N   . LEU A  1 133 ? 68.669  47.192  -7.181  1.00 17.76 ? 106 LEU A N   1 
ATOM   790   C  CA  . LEU A  1 133 ? 67.781  48.216  -7.753  1.00 19.20 ? 106 LEU A CA  1 
ATOM   791   C  C   . LEU A  1 133 ? 67.249  49.205  -6.694  1.00 21.84 ? 106 LEU A C   1 
ATOM   792   O  O   . LEU A  1 133 ? 66.320  49.978  -6.999  1.00 21.72 ? 106 LEU A O   1 
ATOM   793   C  CB  . LEU A  1 133 ? 66.594  47.570  -8.445  1.00 17.45 ? 106 LEU A CB  1 
ATOM   794   C  CG  . LEU A  1 133 ? 66.950  46.536  -9.535  1.00 18.13 ? 106 LEU A CG  1 
ATOM   795   C  CD1 . LEU A  1 133 ? 65.715  45.963  -10.220 1.00 17.78 ? 106 LEU A CD1 1 
ATOM   796   C  CD2 . LEU A  1 133 ? 67.885  47.151  -10.589 1.00 18.38 ? 106 LEU A CD2 1 
ATOM   797   N  N   . SER A  1 134 ? 67.791  49.142  -5.496  1.00 22.59 ? 107 SER A N   1 
ATOM   798   C  CA  . SER A  1 134 ? 67.522  50.137  -4.427  1.00 25.83 ? 107 SER A CA  1 
ATOM   799   C  C   . SER A  1 134 ? 68.693  50.260  -3.466  1.00 26.09 ? 107 SER A C   1 
ATOM   800   O  O   . SER A  1 134 ? 69.628  49.441  -3.511  1.00 21.53 ? 107 SER A O   1 
ATOM   801   C  CB  . SER A  1 134 ? 66.225  49.756  -3.700  1.00 26.58 ? 107 SER A CB  1 
ATOM   802   O  OG  . SER A  1 134 ? 66.309  48.439  -3.172  1.00 29.78 ? 107 SER A OG  1 
ATOM   803   N  N   . GLY A  1 135 ? 68.672  51.288  -2.593  1.00 24.88 ? 108 GLY A N   1 
ATOM   804   C  CA  . GLY A  1 135 ? 69.784  51.623  -1.663  1.00 28.91 ? 108 GLY A CA  1 
ATOM   805   C  C   . GLY A  1 135 ? 71.107  52.050  -2.318  1.00 33.43 ? 108 GLY A C   1 
ATOM   806   O  O   . GLY A  1 135 ? 71.127  52.525  -3.439  1.00 33.34 ? 108 GLY A O   1 
ATOM   807   N  N   . ASP A  1 136 ? 72.229  51.841  -1.641  1.00 34.42 ? 109 ASP A N   1 
ATOM   808   C  CA  . ASP A  1 136 ? 73.492  52.475  -2.053  1.00 35.34 ? 109 ASP A CA  1 
ATOM   809   C  C   . ASP A  1 136 ? 74.146  51.799  -3.258  1.00 32.04 ? 109 ASP A C   1 
ATOM   810   O  O   . ASP A  1 136 ? 74.886  52.432  -3.984  1.00 31.77 ? 109 ASP A O   1 
ATOM   811   C  CB  . ASP A  1 136 ? 74.514  52.518  -0.886  1.00 39.05 ? 109 ASP A CB  1 
ATOM   812   C  CG  . ASP A  1 136 ? 74.110  53.534  0.243   1.00 47.61 ? 109 ASP A CG  1 
ATOM   813   O  OD1 . ASP A  1 136 ? 73.066  54.263  0.130   1.00 48.11 ? 109 ASP A OD1 1 
ATOM   814   O  OD2 . ASP A  1 136 ? 74.849  53.587  1.257   1.00 49.03 ? 109 ASP A OD2 1 
ATOM   815   N  N   . HIS A  1 137 ? 73.901  50.513  -3.459  1.00 29.21 ? 110 HIS A N   1 
ATOM   816   C  CA  . HIS A  1 137 ? 74.417  49.882  -4.692  1.00 32.10 ? 110 HIS A CA  1 
ATOM   817   C  C   . HIS A  1 137 ? 73.402  49.973  -5.833  1.00 29.17 ? 110 HIS A C   1 
ATOM   818   O  O   . HIS A  1 137 ? 73.478  49.128  -6.749  1.00 26.60 ? 110 HIS A O   1 
ATOM   819   C  CB  . HIS A  1 137 ? 74.811  48.403  -4.444  1.00 32.84 ? 110 HIS A CB  1 
ATOM   820   C  CG  . HIS A  1 137 ? 75.988  48.252  -3.533  1.00 36.74 ? 110 HIS A CG  1 
ATOM   821   N  ND1 . HIS A  1 137 ? 76.538  47.024  -3.220  1.00 39.68 ? 110 HIS A ND1 1 
ATOM   822   C  CD2 . HIS A  1 137 ? 76.719  49.180  -2.859  1.00 38.48 ? 110 HIS A CD2 1 
ATOM   823   C  CE1 . HIS A  1 137 ? 77.556  47.200  -2.389  1.00 39.45 ? 110 HIS A CE1 1 
ATOM   824   N  NE2 . HIS A  1 137 ? 77.693  48.499  -2.162  1.00 37.95 ? 110 HIS A NE2 1 
ATOM   825   N  N   . CYS A  1 138 ? 72.450  50.925  -5.731  1.00 25.74 ? 111 CYS A N   1 
ATOM   826   C  CA  . CYS A  1 138 ? 71.340  51.021  -6.691  1.00 22.47 ? 111 CYS A CA  1 
ATOM   827   C  C   . CYS A  1 138 ? 71.948  51.436  -8.010  1.00 19.37 ? 111 CYS A C   1 
ATOM   828   O  O   . CYS A  1 138 ? 72.781  52.369  -8.057  1.00 20.12 ? 111 CYS A O   1 
ATOM   829   C  CB  . CYS A  1 138 ? 70.368  52.106  -6.226  1.00 26.94 ? 111 CYS A CB  1 
ATOM   830   S  SG  . CYS A  1 138 ? 69.059  52.390  -7.403  1.00 30.02 ? 111 CYS A SG  1 
ATOM   831   N  N   . ILE A  1 139 ? 71.577  50.740  -9.079  1.00 17.56 ? 112 ILE A N   1 
ATOM   832   C  CA  . ILE A  1 139 ? 72.126  51.041  -10.402 1.00 16.67 ? 112 ILE A CA  1 
ATOM   833   C  C   . ILE A  1 139 ? 71.121  51.755  -11.307 1.00 17.19 ? 112 ILE A C   1 
ATOM   834   O  O   . ILE A  1 139 ? 71.430  52.048  -12.429 1.00 15.83 ? 112 ILE A O   1 
ATOM   835   C  CB  . ILE A  1 139 ? 72.605  49.734  -11.117 1.00 17.78 ? 112 ILE A CB  1 
ATOM   836   C  CG1 . ILE A  1 139 ? 71.458  48.728  -11.214 1.00 18.92 ? 112 ILE A CG1 1 
ATOM   837   C  CG2 . ILE A  1 139 ? 73.844  49.158  -10.356 1.00 18.31 ? 112 ILE A CG2 1 
ATOM   838   C  CD1 . ILE A  1 139 ? 71.733  47.510  -12.074 1.00 20.56 ? 112 ILE A CD1 1 
ATOM   839   N  N   A ILE A  1 140 ? 69.916  52.012  -10.783 0.50 16.94 ? 113 ILE A N   1 
ATOM   840   N  N   B ILE A  1 140 ? 69.895  51.963  -10.836 0.50 16.62 ? 113 ILE A N   1 
ATOM   841   C  CA  A ILE A  1 140 ? 68.899  52.838  -11.483 0.50 16.85 ? 113 ILE A CA  1 
ATOM   842   C  CA  B ILE A  1 140 ? 68.916  52.706  -11.655 0.50 16.10 ? 113 ILE A CA  1 
ATOM   843   C  C   A ILE A  1 140 ? 69.481  54.210  -11.790 0.50 15.73 ? 113 ILE A C   1 
ATOM   844   C  C   B ILE A  1 140 ? 69.433  54.143  -11.813 0.50 15.35 ? 113 ILE A C   1 
ATOM   845   O  O   A ILE A  1 140 ? 70.067  54.847  -10.918 0.50 15.91 ? 113 ILE A O   1 
ATOM   846   O  O   B ILE A  1 140 ? 69.968  54.730  -10.877 0.50 15.84 ? 113 ILE A O   1 
ATOM   847   C  CB  A ILE A  1 140 ? 67.654  53.042  -10.586 0.50 17.02 ? 113 ILE A CB  1 
ATOM   848   C  CB  B ILE A  1 140 ? 67.512  52.621  -11.020 0.50 15.57 ? 113 ILE A CB  1 
ATOM   849   C  CG1 A ILE A  1 140 ? 67.003  51.711  -10.264 0.50 17.62 ? 113 ILE A CG1 1 
ATOM   850   C  CG1 B ILE A  1 140 ? 66.934  51.232  -11.261 0.50 16.38 ? 113 ILE A CG1 1 
ATOM   851   C  CG2 A ILE A  1 140 ? 66.645  54.004  -11.245 0.50 17.16 ? 113 ILE A CG2 1 
ATOM   852   C  CG2 B ILE A  1 140 ? 66.568  53.679  -11.607 0.50 16.31 ? 113 ILE A CG2 1 
ATOM   853   C  CD1 A ILE A  1 140 ? 66.679  50.881  -11.487 0.50 18.72 ? 113 ILE A CD1 1 
ATOM   854   C  CD1 B ILE A  1 140 ? 65.665  50.948  -10.480 0.50 14.80 ? 113 ILE A CD1 1 
ATOM   855   N  N   . GLY A  1 141 ? 69.353  54.675  -13.031 1.00 14.47 ? 114 GLY A N   1 
ATOM   856   C  CA  . GLY A  1 141 ? 69.900  56.001  -13.350 1.00 13.90 ? 114 GLY A CA  1 
ATOM   857   C  C   . GLY A  1 141 ? 71.356  55.982  -13.760 1.00 15.00 ? 114 GLY A C   1 
ATOM   858   O  O   . GLY A  1 141 ? 71.935  57.036  -14.009 1.00 14.40 ? 114 GLY A O   1 
ATOM   859   N  N   . ARG A  1 142 ? 71.980  54.803  -13.709 1.00 15.00 ? 115 ARG A N   1 
ATOM   860   C  CA  . ARG A  1 142 ? 73.429  54.712  -14.124 1.00 14.85 ? 115 ARG A CA  1 
ATOM   861   C  C   . ARG A  1 142 ? 73.444  54.065  -15.511 1.00 17.28 ? 115 ARG A C   1 
ATOM   862   O  O   . ARG A  1 142 ? 72.400  53.915  -16.124 1.00 17.99 ? 115 ARG A O   1 
ATOM   863   C  CB  . ARG A  1 142 ? 74.212  53.843  -13.117 1.00 16.61 ? 115 ARG A CB  1 
ATOM   864   C  CG  . ARG A  1 142 ? 74.035  54.433  -11.717 1.00 16.38 ? 115 ARG A CG  1 
ATOM   865   C  CD  . ARG A  1 142 ? 75.024  53.926  -10.687 1.00 17.76 ? 115 ARG A CD  1 
ATOM   866   N  NE  . ARG A  1 142 ? 74.749  54.534  -9.340  1.00 18.46 ? 115 ARG A NE  1 
ATOM   867   C  CZ  . ARG A  1 142 ? 75.222  55.705  -8.926  1.00 18.95 ? 115 ARG A CZ  1 
ATOM   868   N  NH1 . ARG A  1 142 ? 76.048  56.443  -9.661  1.00 18.53 ? 115 ARG A NH1 1 
ATOM   869   N  NH2 . ARG A  1 142 ? 74.939  56.096  -7.690  1.00 20.31 ? 115 ARG A NH2 1 
ATOM   870   N  N   . THR A  1 143 ? 74.618  53.783  -16.046 1.00 15.99 ? 116 THR A N   1 
ATOM   871   C  CA  . THR A  1 143 ? 74.680  53.424  -17.468 1.00 16.35 ? 116 THR A CA  1 
ATOM   872   C  C   . THR A  1 143 ? 75.235  52.017  -17.609 1.00 17.37 ? 116 THR A C   1 
ATOM   873   O  O   . THR A  1 143 ? 76.327  51.772  -17.083 1.00 17.34 ? 116 THR A O   1 
ATOM   874   C  CB  . THR A  1 143 ? 75.607  54.367  -18.243 1.00 16.15 ? 116 THR A CB  1 
ATOM   875   O  OG1 . THR A  1 143 ? 75.018  55.678  -18.338 1.00 17.51 ? 116 THR A OG1 1 
ATOM   876   C  CG2 . THR A  1 143 ? 75.832  53.859  -19.760 1.00 15.80 ? 116 THR A CG2 1 
ATOM   877   N  N   . LEU A  1 144 ? 74.537  51.157  -18.355 1.00 16.84 ? 117 LEU A N   1 
ATOM   878   C  CA  . LEU A  1 144 ? 75.033  49.823  -18.695 1.00 16.61 ? 117 LEU A CA  1 
ATOM   879   C  C   . LEU A  1 144 ? 75.752  49.895  -20.031 1.00 15.16 ? 117 LEU A C   1 
ATOM   880   O  O   . LEU A  1 144 ? 75.219  50.481  -20.970 1.00 15.44 ? 117 LEU A O   1 
ATOM   881   C  CB  . LEU A  1 144 ? 73.849  48.875  -18.857 1.00 15.30 ? 117 LEU A CB  1 
ATOM   882   C  CG  . LEU A  1 144 ? 74.216  47.417  -19.120 1.00 15.41 ? 117 LEU A CG  1 
ATOM   883   C  CD1 . LEU A  1 144 ? 74.904  46.768  -17.903 1.00 16.33 ? 117 LEU A CD1 1 
ATOM   884   C  CD2 . LEU A  1 144 ? 72.955  46.631  -19.482 1.00 14.38 ? 117 LEU A CD2 1 
ATOM   885   N  N   . VAL A  1 145 ? 76.962  49.329  -20.108 1.00 15.81 ? 118 VAL A N   1 
ATOM   886   C  CA  . VAL A  1 145 ? 77.769  49.410  -21.367 1.00 14.65 ? 118 VAL A CA  1 
ATOM   887   C  C   . VAL A  1 145 ? 78.223  47.988  -21.765 1.00 15.72 ? 118 VAL A C   1 
ATOM   888   O  O   . VAL A  1 145 ? 78.628  47.193  -20.896 1.00 16.33 ? 118 VAL A O   1 
ATOM   889   C  CB  . VAL A  1 145 ? 79.049  50.217  -21.088 1.00 16.31 ? 118 VAL A CB  1 
ATOM   890   C  CG1 . VAL A  1 145 ? 79.949  50.292  -22.332 1.00 16.45 ? 118 VAL A CG1 1 
ATOM   891   C  CG2 . VAL A  1 145 ? 78.708  51.642  -20.614 1.00 16.41 ? 118 VAL A CG2 1 
ATOM   892   N  N   . VAL A  1 146 ? 78.129  47.671  -23.058 1.00 16.29 ? 119 VAL A N   1 
ATOM   893   C  CA  . VAL A  1 146 ? 78.724  46.437  -23.556 1.00 17.77 ? 119 VAL A CA  1 
ATOM   894   C  C   . VAL A  1 146 ? 79.973  46.873  -24.343 1.00 18.94 ? 119 VAL A C   1 
ATOM   895   O  O   . VAL A  1 146 ? 79.972  47.878  -25.086 1.00 18.21 ? 119 VAL A O   1 
ATOM   896   C  CB  . VAL A  1 146 ? 77.732  45.587  -24.373 1.00 19.51 ? 119 VAL A CB  1 
ATOM   897   C  CG1 . VAL A  1 146 ? 77.171  46.379  -25.558 1.00 18.46 ? 119 VAL A CG1 1 
ATOM   898   C  CG2 . VAL A  1 146 ? 78.397  44.276  -24.823 1.00 20.25 ? 119 VAL A CG2 1 
ATOM   899   N  N   . HIS A  1 147 ? 81.065  46.164  -24.078 1.00 19.37 ? 120 HIS A N   1 
ATOM   900   C  CA  . HIS A  1 147 ? 82.406  46.559  -24.541 1.00 19.71 ? 120 HIS A CA  1 
ATOM   901   C  C   . HIS A  1 147 ? 82.886  45.729  -25.754 1.00 22.09 ? 120 HIS A C   1 
ATOM   902   O  O   . HIS A  1 147 ? 82.316  44.692  -26.093 1.00 22.49 ? 120 HIS A O   1 
ATOM   903   C  CB  . HIS A  1 147 ? 83.396  46.467  -23.394 1.00 18.87 ? 120 HIS A CB  1 
ATOM   904   C  CG  . HIS A  1 147 ? 83.250  47.544  -22.351 1.00 21.41 ? 120 HIS A CG  1 
ATOM   905   N  ND1 . HIS A  1 147 ? 84.035  48.682  -22.345 1.00 21.95 ? 120 HIS A ND1 1 
ATOM   906   C  CD2 . HIS A  1 147 ? 82.455  47.636  -21.251 1.00 20.31 ? 120 HIS A CD2 1 
ATOM   907   C  CE1 . HIS A  1 147 ? 83.714  49.438  -21.304 1.00 23.73 ? 120 HIS A CE1 1 
ATOM   908   N  NE2 . HIS A  1 147 ? 82.780  48.815  -20.608 1.00 21.49 ? 120 HIS A NE2 1 
ATOM   909   N  N   . GLU A  1 148 ? 83.930  46.243  -26.385 1.00 22.20 ? 121 GLU A N   1 
ATOM   910   C  CA  . GLU A  1 148 ? 84.502  45.723  -27.622 1.00 24.13 ? 121 GLU A CA  1 
ATOM   911   C  C   . GLU A  1 148 ? 85.128  44.336  -27.424 1.00 22.07 ? 121 GLU A C   1 
ATOM   912   O  O   . GLU A  1 148 ? 84.967  43.478  -28.285 1.00 23.81 ? 121 GLU A O   1 
ATOM   913   C  CB  . GLU A  1 148 ? 85.647  46.692  -27.952 1.00 28.50 ? 121 GLU A CB  1 
ATOM   914   C  CG  . GLU A  1 148 ? 86.469  46.383  -29.182 1.00 35.75 ? 121 GLU A CG  1 
ATOM   915   C  CD  . GLU A  1 148 ? 87.801  47.182  -29.194 1.00 41.78 ? 121 GLU A CD  1 
ATOM   916   O  OE1 . GLU A  1 148 ? 88.534  46.988  -30.184 1.00 48.55 ? 121 GLU A OE1 1 
ATOM   917   O  OE2 . GLU A  1 148 ? 88.156  47.957  -28.244 1.00 36.09 ? 121 GLU A OE2 1 
ATOM   918   N  N   . LYS A  1 149 ? 85.813  44.127  -26.307 1.00 26.41 ? 122 LYS A N   1 
ATOM   919   C  CA  . LYS A  1 149 ? 86.593  42.887  -26.111 1.00 28.62 ? 122 LYS A CA  1 
ATOM   920   C  C   . LYS A  1 149 ? 86.247  42.218  -24.803 1.00 27.45 ? 122 LYS A C   1 
ATOM   921   O  O   . LYS A  1 149 ? 85.440  42.740  -24.014 1.00 25.69 ? 122 LYS A O   1 
ATOM   922   C  CB  . LYS A  1 149 ? 88.092  43.233  -26.056 1.00 31.17 ? 122 LYS A CB  1 
ATOM   923   C  CG  . LYS A  1 149 ? 88.674  43.723  -27.347 1.00 40.15 ? 122 LYS A CG  1 
ATOM   924   C  CD  . LYS A  1 149 ? 90.190  43.782  -27.217 1.00 43.61 ? 122 LYS A CD  1 
ATOM   925   C  CE  . LYS A  1 149 ? 90.657  45.078  -26.585 1.00 40.91 ? 122 LYS A CE  1 
ATOM   926   N  NZ  . LYS A  1 149 ? 91.708  44.804  -25.555 1.00 47.53 ? 122 LYS A NZ  1 
ATOM   927   N  N   . ALA A  1 150 ? 86.887  41.066  -24.520 1.00 26.36 ? 123 ALA A N   1 
ATOM   928   C  CA  . ALA A  1 150 ? 86.662  40.362  -23.238 1.00 24.67 ? 123 ALA A CA  1 
ATOM   929   C  C   . ALA A  1 150 ? 87.191  41.202  -22.081 1.00 24.12 ? 123 ALA A C   1 
ATOM   930   O  O   . ALA A  1 150 ? 88.218  41.872  -22.192 1.00 24.78 ? 123 ALA A O   1 
ATOM   931   C  CB  . ALA A  1 150 ? 87.365  38.984  -23.229 1.00 27.55 ? 123 ALA A CB  1 
ATOM   932   N  N   . ASP A  1 151 ? 86.469  41.167  -20.969 1.00 21.26 ? 124 ASP A N   1 
ATOM   933   C  CA  . ASP A  1 151 ? 86.918  41.630  -19.684 1.00 23.05 ? 124 ASP A CA  1 
ATOM   934   C  C   . ASP A  1 151 ? 87.837  40.490  -19.134 1.00 23.46 ? 124 ASP A C   1 
ATOM   935   O  O   . ASP A  1 151 ? 87.406  39.315  -19.026 1.00 22.55 ? 124 ASP A O   1 
ATOM   936   C  CB  . ASP A  1 151 ? 85.650  41.809  -18.782 1.00 21.85 ? 124 ASP A CB  1 
ATOM   937   C  CG  . ASP A  1 151 ? 85.956  42.258  -17.374 1.00 28.02 ? 124 ASP A CG  1 
ATOM   938   O  OD1 . ASP A  1 151 ? 87.157  42.282  -16.950 1.00 25.63 ? 124 ASP A OD1 1 
ATOM   939   O  OD2 . ASP A  1 151 ? 84.968  42.577  -16.630 1.00 28.11 ? 124 ASP A OD2 1 
ATOM   940   N  N   . ASP A  1 152 ? 89.086  40.832  -18.784 1.00 23.94 ? 125 ASP A N   1 
ATOM   941   C  CA  . ASP A  1 152 ? 90.061  39.827  -18.277 1.00 26.64 ? 125 ASP A CA  1 
ATOM   942   C  C   . ASP A  1 152 ? 89.904  39.625  -16.771 1.00 27.47 ? 125 ASP A C   1 
ATOM   943   O  O   . ASP A  1 152 ? 90.630  38.845  -16.128 1.00 25.18 ? 125 ASP A O   1 
ATOM   944   C  CB  . ASP A  1 152 ? 91.502  40.189  -18.685 1.00 28.51 ? 125 ASP A CB  1 
ATOM   945   C  CG  . ASP A  1 152 ? 92.045  41.444  -17.964 1.00 29.80 ? 125 ASP A CG  1 
ATOM   946   O  OD1 . ASP A  1 152 ? 91.549  41.862  -16.874 1.00 27.36 ? 125 ASP A OD1 1 
ATOM   947   O  OD2 . ASP A  1 152 ? 93.012  42.016  -18.498 1.00 31.94 ? 125 ASP A OD2 1 
ATOM   948   N  N   . LEU A  1 153 ? 88.890  40.288  -16.188 1.00 24.40 ? 126 LEU A N   1 
ATOM   949   C  CA  . LEU A  1 153 ? 88.505  40.036  -14.793 1.00 23.33 ? 126 LEU A CA  1 
ATOM   950   C  C   . LEU A  1 153 ? 89.576  40.342  -13.781 1.00 22.39 ? 126 LEU A C   1 
ATOM   951   O  O   . LEU A  1 153 ? 89.567  39.830  -12.667 1.00 22.29 ? 126 LEU A O   1 
ATOM   952   C  CB  . LEU A  1 153 ? 87.932  38.617  -14.579 1.00 24.29 ? 126 LEU A CB  1 
ATOM   953   C  CG  . LEU A  1 153 ? 86.930  38.135  -15.640 1.00 28.24 ? 126 LEU A CG  1 
ATOM   954   C  CD1 . LEU A  1 153 ? 86.546  36.694  -15.336 1.00 28.81 ? 126 LEU A CD1 1 
ATOM   955   C  CD2 . LEU A  1 153 ? 85.677  39.021  -15.727 1.00 25.71 ? 126 LEU A CD2 1 
ATOM   956   N  N   . GLY A  1 154 ? 90.469  41.236  -14.143 1.00 23.19 ? 127 GLY A N   1 
ATOM   957   C  CA  . GLY A  1 154 ? 91.455  41.663  -13.179 1.00 25.70 ? 127 GLY A CA  1 
ATOM   958   C  C   . GLY A  1 154 ? 92.745  40.837  -13.250 1.00 30.26 ? 127 GLY A C   1 
ATOM   959   O  O   . GLY A  1 154 ? 93.643  41.048  -12.439 1.00 30.05 ? 127 GLY A O   1 
ATOM   960   N  N   . LYS A  1 155 ? 92.849  39.945  -14.229 1.00 26.08 ? 128 LYS A N   1 
ATOM   961   C  CA  . LYS A  1 155 ? 93.915  38.936  -14.212 1.00 30.39 ? 128 LYS A CA  1 
ATOM   962   C  C   . LYS A  1 155 ? 94.889  39.113  -15.367 1.00 31.81 ? 128 LYS A C   1 
ATOM   963   O  O   . LYS A  1 155 ? 95.589  38.161  -15.763 1.00 30.29 ? 128 LYS A O   1 
ATOM   964   C  CB  . LYS A  1 155 ? 93.273  37.532  -14.229 1.00 28.68 ? 128 LYS A CB  1 
ATOM   965   C  CG  . LYS A  1 155 ? 92.666  37.221  -12.869 1.00 34.17 ? 128 LYS A CG  1 
ATOM   966   C  CD  . LYS A  1 155 ? 91.809  35.977  -12.973 1.00 46.74 ? 128 LYS A CD  1 
ATOM   967   C  CE  . LYS A  1 155 ? 91.893  35.175  -11.682 1.00 53.15 ? 128 LYS A CE  1 
ATOM   968   N  NZ  . LYS A  1 155 ? 91.999  33.736  -12.071 1.00 55.07 ? 128 LYS A NZ  1 
ATOM   969   N  N   . GLY A  1 156 ? 94.965  40.332  -15.900 1.00 25.52 ? 129 GLY A N   1 
ATOM   970   C  CA  . GLY A  1 156 ? 95.729  40.551  -17.095 1.00 27.26 ? 129 GLY A CA  1 
ATOM   971   C  C   . GLY A  1 156 ? 97.170  41.050  -16.812 1.00 27.07 ? 129 GLY A C   1 
ATOM   972   O  O   . GLY A  1 156 ? 97.921  41.246  -17.734 1.00 30.88 ? 129 GLY A O   1 
ATOM   973   N  N   . GLY A  1 157 ? 97.514  41.269  -15.562 1.00 25.98 ? 130 GLY A N   1 
ATOM   974   C  CA  . GLY A  1 157 ? 98.893  41.633  -15.180 1.00 27.68 ? 130 GLY A CA  1 
ATOM   975   C  C   . GLY A  1 157 ? 99.365  43.035  -15.589 1.00 33.36 ? 130 GLY A C   1 
ATOM   976   O  O   . GLY A  1 157 ? 100.568 43.282  -15.677 1.00 33.54 ? 130 GLY A O   1 
ATOM   977   N  N   . ASN A  1 158 ? 98.434  43.956  -15.872 1.00 31.21 ? 131 ASN A N   1 
ATOM   978   C  CA  . ASN A  1 158 ? 98.760  45.382  -16.085 1.00 32.97 ? 131 ASN A CA  1 
ATOM   979   C  C   . ASN A  1 158 ? 97.781  46.290  -15.279 1.00 36.19 ? 131 ASN A C   1 
ATOM   980   O  O   . ASN A  1 158 ? 96.797  45.802  -14.675 1.00 34.33 ? 131 ASN A O   1 
ATOM   981   C  CB  . ASN A  1 158 ? 98.828  45.733  -17.583 1.00 36.04 ? 131 ASN A CB  1 
ATOM   982   C  CG  . ASN A  1 158 ? 97.534  45.480  -18.312 1.00 41.24 ? 131 ASN A CG  1 
ATOM   983   O  OD1 . ASN A  1 158 ? 96.476  45.418  -17.704 1.00 34.47 ? 131 ASN A OD1 1 
ATOM   984   N  ND2 . ASN A  1 158 ? 97.615  45.323  -19.625 1.00 46.70 ? 131 ASN A ND2 1 
ATOM   985   N  N   . GLU A  1 159 ? 98.031  47.590  -15.203 1.00 34.78 ? 132 GLU A N   1 
ATOM   986   C  CA  . GLU A  1 159 ? 97.140  48.343  -14.314 1.00 38.67 ? 132 GLU A CA  1 
ATOM   987   C  C   . GLU A  1 159 ? 95.764  48.549  -14.945 1.00 31.17 ? 132 GLU A C   1 
ATOM   988   O  O   . GLU A  1 159 ? 94.790  48.709  -14.245 1.00 35.60 ? 132 GLU A O   1 
ATOM   989   C  CB  . GLU A  1 159 ? 97.754  49.650  -13.798 1.00 48.97 ? 132 GLU A CB  1 
ATOM   990   C  CG  . GLU A  1 159 ? 98.164  50.661  -14.848 1.00 55.19 ? 132 GLU A CG  1 
ATOM   991   C  CD  . GLU A  1 159 ? 99.114  51.718  -14.279 1.00 62.13 ? 132 GLU A CD  1 
ATOM   992   O  OE1 . GLU A  1 159 ? 99.449  51.667  -13.068 1.00 64.70 ? 132 GLU A OE1 1 
ATOM   993   O  OE2 . GLU A  1 159 ? 99.529  52.608  -15.050 1.00 67.42 ? 132 GLU A OE2 1 
ATOM   994   N  N   . GLU A  1 160 ? 95.692  48.541  -16.265 1.00 30.11 ? 133 GLU A N   1 
ATOM   995   C  CA  . GLU A  1 160 ? 94.412  48.673  -16.964 1.00 33.06 ? 133 GLU A CA  1 
ATOM   996   C  C   . GLU A  1 160 ? 93.519  47.484  -16.607 1.00 32.69 ? 133 GLU A C   1 
ATOM   997   O  O   . GLU A  1 160 ? 92.268  47.598  -16.509 1.00 25.14 ? 133 GLU A O   1 
ATOM   998   C  CB  . GLU A  1 160 ? 94.665  48.712  -18.466 1.00 35.35 ? 133 GLU A CB  1 
ATOM   999   C  CG  . GLU A  1 160 ? 93.496  49.154  -19.317 1.00 39.79 ? 133 GLU A CG  1 
ATOM   1000  C  CD  . GLU A  1 160 ? 93.033  50.575  -18.971 1.00 50.23 ? 133 GLU A CD  1 
ATOM   1001  O  OE1 . GLU A  1 160 ? 93.774  51.556  -19.247 1.00 51.31 ? 133 GLU A OE1 1 
ATOM   1002  O  OE2 . GLU A  1 160 ? 91.924  50.701  -18.398 1.00 47.02 ? 133 GLU A OE2 1 
ATOM   1003  N  N   . SER A  1 161 ? 94.149  46.322  -16.407 1.00 26.11 ? 134 SER A N   1 
ATOM   1004  C  CA  . SER A  1 161 ? 93.420  45.174  -15.933 1.00 25.60 ? 134 SER A CA  1 
ATOM   1005  C  C   . SER A  1 161 ? 92.701  45.383  -14.591 1.00 24.83 ? 134 SER A C   1 
ATOM   1006  O  O   . SER A  1 161 ? 91.588  44.892  -14.418 1.00 26.19 ? 134 SER A O   1 
ATOM   1007  C  CB  . SER A  1 161 ? 94.358  43.965  -15.808 1.00 27.25 ? 134 SER A CB  1 
ATOM   1008  O  OG  . SER A  1 161 ? 93.611  42.875  -15.356 1.00 26.22 ? 134 SER A OG  1 
ATOM   1009  N  N   . THR A  1 162 ? 93.326  46.038  -13.614 1.00 27.13 ? 135 THR A N   1 
ATOM   1010  C  CA  . THR A  1 162 ? 92.622  46.240  -12.344 1.00 29.99 ? 135 THR A CA  1 
ATOM   1011  C  C   . THR A  1 162 ? 91.751  47.545  -12.299 1.00 30.96 ? 135 THR A C   1 
ATOM   1012  O  O   . THR A  1 162 ? 91.266  47.940  -11.244 1.00 30.87 ? 135 THR A O   1 
ATOM   1013  C  CB  . THR A  1 162 ? 93.569  46.134  -11.143 1.00 34.96 ? 135 THR A CB  1 
ATOM   1014  O  OG1 . THR A  1 162 ? 94.726  46.902  -11.418 1.00 37.85 ? 135 THR A OG1 1 
ATOM   1015  C  CG2 . THR A  1 162 ? 94.003  44.640  -10.911 1.00 38.04 ? 135 THR A CG2 1 
ATOM   1016  N  N   . LYS A  1 163 ? 91.570  48.165  -13.449 1.00 29.34 ? 136 LYS A N   1 
ATOM   1017  C  CA  . LYS A  1 163 ? 90.707  49.355  -13.622 1.00 34.65 ? 136 LYS A CA  1 
ATOM   1018  C  C   . LYS A  1 163 ? 89.480  49.007  -14.483 1.00 33.47 ? 136 LYS A C   1 
ATOM   1019  O  O   . LYS A  1 163 ? 88.341  49.190  -14.047 1.00 32.38 ? 136 LYS A O   1 
ATOM   1020  C  CB  . LYS A  1 163 ? 91.523  50.490  -14.239 1.00 35.68 ? 136 LYS A CB  1 
ATOM   1021  C  CG  . LYS A  1 163 ? 90.762  51.807  -14.397 1.00 40.82 ? 136 LYS A CG  1 
ATOM   1022  C  CD  . LYS A  1 163 ? 91.467  52.816  -15.305 1.00 43.09 ? 136 LYS A CD  1 
ATOM   1023  C  CE  . LYS A  1 163 ? 90.552  53.982  -15.653 1.00 44.60 ? 136 LYS A CE  1 
ATOM   1024  N  NZ  . LYS A  1 163 ? 91.155  54.869  -16.689 1.00 52.00 ? 136 LYS A NZ  1 
ATOM   1025  N  N   . THR A  1 164 ? 89.700  48.466  -15.686 1.00 29.29 ? 137 THR A N   1 
ATOM   1026  C  CA  . THR A  1 164 ? 88.625  48.237  -16.656 1.00 30.05 ? 137 THR A CA  1 
ATOM   1027  C  C   . THR A  1 164 ? 88.599  46.793  -17.171 1.00 30.74 ? 137 THR A C   1 
ATOM   1028  O  O   . THR A  1 164 ? 87.732  46.429  -17.963 1.00 28.73 ? 137 THR A O   1 
ATOM   1029  C  CB  . THR A  1 164 ? 88.834  49.113  -17.919 1.00 33.16 ? 137 THR A CB  1 
ATOM   1030  O  OG1 . THR A  1 164 ? 90.028  48.676  -18.595 1.00 31.44 ? 137 THR A OG1 1 
ATOM   1031  C  CG2 . THR A  1 164 ? 88.989  50.640  -17.584 1.00 29.26 ? 137 THR A CG2 1 
ATOM   1032  N  N   . GLY A  1 165 ? 89.610  45.989  -16.827 1.00 27.99 ? 138 GLY A N   1 
ATOM   1033  C  CA  . GLY A  1 165 ? 89.636  44.611  -17.307 1.00 21.84 ? 138 GLY A CA  1 
ATOM   1034  C  C   . GLY A  1 165 ? 90.102  44.493  -18.738 1.00 22.62 ? 138 GLY A C   1 
ATOM   1035  O  O   . GLY A  1 165 ? 89.945  43.412  -19.377 1.00 24.75 ? 138 GLY A O   1 
ATOM   1036  N  N   . ASN A  1 166 ? 90.621  45.586  -19.284 1.00 26.99 ? 139 ASN A N   1 
ATOM   1037  C  CA  . ASN A  1 166 ? 91.067  45.609  -20.690 1.00 29.41 ? 139 ASN A CA  1 
ATOM   1038  C  C   . ASN A  1 166 ? 89.961  45.292  -21.711 1.00 28.48 ? 139 ASN A C   1 
ATOM   1039  O  O   . ASN A  1 166 ? 90.239  44.777  -22.780 1.00 23.15 ? 139 ASN A O   1 
ATOM   1040  C  CB  . ASN A  1 166 ? 92.251  44.634  -20.889 1.00 29.76 ? 139 ASN A CB  1 
ATOM   1041  C  CG  . ASN A  1 166 ? 93.524  45.121  -20.207 1.00 29.96 ? 139 ASN A CG  1 
ATOM   1042  O  OD1 . ASN A  1 166 ? 94.050  46.149  -20.579 1.00 33.56 ? 139 ASN A OD1 1 
ATOM   1043  N  ND2 . ASN A  1 166 ? 93.989  44.412  -19.188 1.00 27.96 ? 139 ASN A ND2 1 
ATOM   1044  N  N   . ALA A  1 167 ? 88.700  45.618  -21.396 1.00 24.91 ? 140 ALA A N   1 
ATOM   1045  C  CA  . ALA A  1 167 ? 87.592  45.255  -22.296 1.00 21.91 ? 140 ALA A CA  1 
ATOM   1046  C  C   . ALA A  1 167 ? 87.469  46.188  -23.502 1.00 21.37 ? 140 ALA A C   1 
ATOM   1047  O  O   . ALA A  1 167 ? 86.603  46.019  -24.382 1.00 22.61 ? 140 ALA A O   1 
ATOM   1048  C  CB  . ALA A  1 167 ? 86.287  45.204  -21.470 1.00 23.12 ? 140 ALA A CB  1 
ATOM   1049  N  N   . GLY A  1 168 ? 88.319  47.212  -23.529 1.00 23.42 ? 141 GLY A N   1 
ATOM   1050  C  CA  . GLY A  1 168 ? 88.408  48.142  -24.651 1.00 23.19 ? 141 GLY A CA  1 
ATOM   1051  C  C   . GLY A  1 168 ? 87.191  49.061  -24.794 1.00 26.02 ? 141 GLY A C   1 
ATOM   1052  O  O   . GLY A  1 168 ? 86.546  49.444  -23.782 1.00 25.18 ? 141 GLY A O   1 
ATOM   1053  N  N   . SER A  1 169 ? 86.867  49.382  -26.026 1.00 22.04 ? 142 SER A N   1 
ATOM   1054  C  CA  . SER A  1 169 ? 86.004  50.520  -26.302 1.00 27.34 ? 142 SER A CA  1 
ATOM   1055  C  C   . SER A  1 169 ? 84.507  50.222  -25.966 1.00 23.91 ? 142 SER A C   1 
ATOM   1056  O  O   . SER A  1 169 ? 84.085  49.048  -25.803 1.00 20.48 ? 142 SER A O   1 
ATOM   1057  C  CB  . SER A  1 169 ? 86.209  50.971  -27.740 1.00 30.27 ? 142 SER A CB  1 
ATOM   1058  O  OG  . SER A  1 169 ? 85.426  50.165  -28.566 1.00 33.87 ? 142 SER A OG  1 
ATOM   1059  N  N   . ARG A  1 170 ? 83.711  51.289  -25.840 1.00 22.52 ? 143 ARG A N   1 
ATOM   1060  C  CA  . ARG A  1 170 ? 82.319  51.120  -25.463 1.00 22.33 ? 143 ARG A CA  1 
ATOM   1061  C  C   . ARG A  1 170 ? 81.481  50.993  -26.728 1.00 21.04 ? 143 ARG A C   1 
ATOM   1062  O  O   . ARG A  1 170 ? 81.304  51.974  -27.474 1.00 22.73 ? 143 ARG A O   1 
ATOM   1063  C  CB  . ARG A  1 170 ? 81.923  52.360  -24.606 1.00 20.81 ? 143 ARG A CB  1 
ATOM   1064  C  CG  . ARG A  1 170 ? 82.817  52.465  -23.362 1.00 20.78 ? 143 ARG A CG  1 
ATOM   1065  C  CD  . ARG A  1 170 ? 82.578  53.744  -22.539 1.00 20.23 ? 143 ARG A CD  1 
ATOM   1066  N  NE  . ARG A  1 170 ? 83.587  53.803  -21.511 1.00 20.07 ? 143 ARG A NE  1 
ATOM   1067  C  CZ  . ARG A  1 170 ? 83.536  54.549  -20.421 1.00 23.29 ? 143 ARG A CZ  1 
ATOM   1068  N  NH1 . ARG A  1 170 ? 82.477  55.337  -20.210 1.00 19.07 ? 143 ARG A NH1 1 
ATOM   1069  N  NH2 . ARG A  1 170 ? 84.511  54.464  -19.512 1.00 19.98 ? 143 ARG A NH2 1 
ATOM   1070  N  N   . LEU A  1 171 ? 80.913  49.832  -27.002 1.00 19.80 ? 144 LEU A N   1 
ATOM   1071  C  CA  . LEU A  1 171 ? 80.189  49.649  -28.266 1.00 19.83 ? 144 LEU A CA  1 
ATOM   1072  C  C   . LEU A  1 171 ? 78.769  50.178  -28.222 1.00 18.98 ? 144 LEU A C   1 
ATOM   1073  O  O   . LEU A  1 171 ? 78.249  50.697  -29.226 1.00 18.72 ? 144 LEU A O   1 
ATOM   1074  C  CB  . LEU A  1 171 ? 80.144  48.160  -28.643 1.00 22.75 ? 144 LEU A CB  1 
ATOM   1075  C  CG  . LEU A  1 171 ? 81.527  47.470  -28.851 1.00 23.71 ? 144 LEU A CG  1 
ATOM   1076  C  CD1 . LEU A  1 171 ? 81.206  46.106  -29.414 1.00 26.78 ? 144 LEU A CD1 1 
ATOM   1077  C  CD2 . LEU A  1 171 ? 82.362  48.278  -29.828 1.00 27.19 ? 144 LEU A CD2 1 
ATOM   1078  N  N   . ALA A  1 172 ? 78.099  50.016  -27.072 1.00 18.80 ? 145 ALA A N   1 
ATOM   1079  C  CA  . ALA A  1 172 ? 76.695  50.500  -26.954 1.00 17.45 ? 145 ALA A CA  1 
ATOM   1080  C  C   . ALA A  1 172 ? 76.395  50.681  -25.469 1.00 18.66 ? 145 ALA A C   1 
ATOM   1081  O  O   . ALA A  1 172 ? 77.048  50.049  -24.622 1.00 16.39 ? 145 ALA A O   1 
ATOM   1082  C  CB  . ALA A  1 172 ? 75.675  49.499  -27.515 1.00 17.41 ? 145 ALA A CB  1 
ATOM   1083  N  N   . CYS A  1 173 ? 75.402  51.512  -25.170 1.00 17.37 ? 146 CYS A N   1 
ATOM   1084  C  CA  . CYS A  1 173 ? 75.083  51.728  -23.756 1.00 18.18 ? 146 CYS A CA  1 
ATOM   1085  C  C   . CYS A  1 173 ? 73.697  52.314  -23.654 1.00 16.22 ? 146 CYS A C   1 
ATOM   1086  O  O   . CYS A  1 173 ? 73.068  52.692  -24.691 1.00 15.41 ? 146 CYS A O   1 
ATOM   1087  C  CB  . CYS A  1 173 ? 76.067  52.727  -23.098 1.00 19.07 ? 146 CYS A CB  1 
ATOM   1088  S  SG  . CYS A  1 173 ? 76.100  54.365  -23.946 1.00 25.07 ? 146 CYS A SG  1 
ATOM   1089  N  N   . GLY A  1 174 ? 73.205  52.357  -22.416 1.00 15.72 ? 147 GLY A N   1 
ATOM   1090  C  CA  . GLY A  1 174 ? 71.903  53.030  -22.174 1.00 14.73 ? 147 GLY A CA  1 
ATOM   1091  C  C   . GLY A  1 174 ? 71.807  53.341  -20.705 1.00 15.00 ? 147 GLY A C   1 
ATOM   1092  O  O   . GLY A  1 174 ? 72.524  52.733  -19.866 1.00 14.68 ? 147 GLY A O   1 
ATOM   1093  N  N   . VAL A  1 175 ? 70.878  54.240  -20.375 1.00 15.87 ? 148 VAL A N   1 
ATOM   1094  C  CA  . VAL A  1 175 ? 70.634  54.555  -18.955 1.00 16.08 ? 148 VAL A CA  1 
ATOM   1095  C  C   . VAL A  1 175 ? 69.659  53.504  -18.425 1.00 14.71 ? 148 VAL A C   1 
ATOM   1096  O  O   . VAL A  1 175 ? 68.671  53.169  -19.052 1.00 17.14 ? 148 VAL A O   1 
ATOM   1097  C  CB  . VAL A  1 175 ? 70.042  55.990  -18.795 1.00 17.00 ? 148 VAL A CB  1 
ATOM   1098  C  CG1 . VAL A  1 175 ? 69.829  56.312  -17.311 1.00 16.53 ? 148 VAL A CG1 1 
ATOM   1099  C  CG2 . VAL A  1 175 ? 70.961  57.019  -19.459 1.00 16.30 ? 148 VAL A CG2 1 
ATOM   1100  N  N   . ILE A  1 176 ? 69.889  53.020  -17.233 1.00 15.42 ? 149 ILE A N   1 
ATOM   1101  C  CA  . ILE A  1 176 ? 69.029  52.010  -16.651 1.00 15.82 ? 149 ILE A CA  1 
ATOM   1102  C  C   . ILE A  1 176 ? 67.799  52.694  -16.029 1.00 17.27 ? 149 ILE A C   1 
ATOM   1103  O  O   . ILE A  1 176 ? 67.947  53.571  -15.164 1.00 18.98 ? 149 ILE A O   1 
ATOM   1104  C  CB  . ILE A  1 176 ? 69.809  51.213  -15.563 1.00 16.26 ? 149 ILE A CB  1 
ATOM   1105  C  CG1 . ILE A  1 176 ? 71.000  50.487  -16.247 1.00 17.20 ? 149 ILE A CG1 1 
ATOM   1106  C  CG2 . ILE A  1 176 ? 68.873  50.197  -14.880 1.00 15.45 ? 149 ILE A CG2 1 
ATOM   1107  C  CD1 . ILE A  1 176 ? 72.033  49.940  -15.235 1.00 16.52 ? 149 ILE A CD1 1 
ATOM   1108  N  N   . GLY A  1 177 ? 66.611  52.304  -16.470 1.00 15.98 ? 150 GLY A N   1 
ATOM   1109  C  CA  . GLY A  1 177 ? 65.362  53.052  -16.115 1.00 15.97 ? 150 GLY A CA  1 
ATOM   1110  C  C   . GLY A  1 177 ? 64.441  52.143  -15.322 1.00 16.57 ? 150 GLY A C   1 
ATOM   1111  O  O   . GLY A  1 177 ? 64.507  50.903  -15.455 1.00 15.16 ? 150 GLY A O   1 
ATOM   1112  N  N   . ILE A  1 178 ? 63.568  52.754  -14.495 1.00 15.21 ? 151 ILE A N   1 
ATOM   1113  C  CA  . ILE A  1 178 ? 62.536  52.029  -13.771 1.00 17.20 ? 151 ILE A CA  1 
ATOM   1114  C  C   . ILE A  1 178 ? 61.523  51.451  -14.729 1.00 17.32 ? 151 ILE A C   1 
ATOM   1115  O  O   . ILE A  1 178 ? 61.082  52.141  -15.657 1.00 17.70 ? 151 ILE A O   1 
ATOM   1116  C  CB  . ILE A  1 178 ? 61.794  52.946  -12.714 1.00 19.01 ? 151 ILE A CB  1 
ATOM   1117  C  CG1 . ILE A  1 178 ? 62.830  53.359  -11.693 1.00 22.50 ? 151 ILE A CG1 1 
ATOM   1118  C  CG2 . ILE A  1 178 ? 60.766  52.088  -11.926 1.00 24.25 ? 151 ILE A CG2 1 
ATOM   1119  C  CD1 . ILE A  1 178 ? 62.495  54.639  -10.899 1.00 28.81 ? 151 ILE A CD1 1 
ATOM   1120  N  N   . ALA A  1 179 ? 61.162  50.168  -14.546 1.00 16.62 ? 152 ALA A N   1 
ATOM   1121  C  CA  . ALA A  1 179 ? 60.215  49.535  -15.469 1.00 19.83 ? 152 ALA A CA  1 
ATOM   1122  C  C   . ALA A  1 179 ? 58.960  49.087  -14.739 1.00 22.77 ? 152 ALA A C   1 
ATOM   1123  O  O   . ALA A  1 179 ? 58.967  48.936  -13.501 1.00 21.77 ? 152 ALA A O   1 
ATOM   1124  C  CB  . ALA A  1 179 ? 60.852  48.303  -16.146 1.00 17.80 ? 152 ALA A CB  1 
ATOM   1125  N  N   . GLN A  1 180 ? 57.897  48.857  -15.508 1.00 25.31 ? 153 GLN A N   1 
ATOM   1126  C  CA  . GLN A  1 180 ? 56.601  48.455  -14.938 1.00 33.10 ? 153 GLN A CA  1 
ATOM   1127  C  C   . GLN A  1 180 ? 56.599  46.990  -14.527 1.00 38.84 ? 153 GLN A C   1 
ATOM   1128  O  O   . GLN A  1 180 ? 57.034  46.140  -15.338 1.00 41.00 ? 153 GLN A O   1 
ATOM   1129  C  CB  . GLN A  1 180 ? 55.481  48.615  -15.955 1.00 33.26 ? 153 GLN A CB  1 
ATOM   1130  C  CG  . GLN A  1 180 ? 54.118  48.416  -15.314 1.00 37.61 ? 153 GLN A CG  1 
ATOM   1131  C  CD  . GLN A  1 180 ? 53.036  48.757  -16.292 1.00 41.61 ? 153 GLN A CD  1 
ATOM   1132  O  OE1 . GLN A  1 180 ? 53.091  48.324  -17.445 1.00 44.98 ? 153 GLN A OE1 1 
ATOM   1133  N  NE2 . GLN A  1 180 ? 52.068  49.555  -15.866 1.00 46.04 ? 153 GLN A NE2 1 
ATOM   1134  O  OXT . GLN A  1 180 ? 56.173  46.649  -13.405 1.00 46.87 ? 153 GLN A OXT 1 
ATOM   1135  N  N   . MET B  1 27  ? 73.827  60.879  -1.864  1.00 53.92 ? 0   MET B N   1 
ATOM   1136  C  CA  . MET B  1 27  ? 72.563  61.322  -2.533  1.00 56.21 ? 0   MET B CA  1 
ATOM   1137  C  C   . MET B  1 27  ? 72.922  62.191  -3.756  1.00 54.55 ? 0   MET B C   1 
ATOM   1138  O  O   . MET B  1 27  ? 73.841  63.031  -3.697  1.00 53.02 ? 0   MET B O   1 
ATOM   1139  C  CB  . MET B  1 27  ? 71.669  62.099  -1.561  1.00 52.85 ? 0   MET B CB  1 
ATOM   1140  N  N   . ALA B  1 28  ? 72.213  61.958  -4.865  1.00 48.56 ? 1   ALA B N   1 
ATOM   1141  C  CA  . ALA B  1 28  ? 72.436  62.692  -6.131  1.00 38.47 ? 1   ALA B CA  1 
ATOM   1142  C  C   . ALA B  1 28  ? 72.072  64.162  -6.012  1.00 32.61 ? 1   ALA B C   1 
ATOM   1143  O  O   . ALA B  1 28  ? 71.025  64.505  -5.466  1.00 30.75 ? 1   ALA B O   1 
ATOM   1144  C  CB  . ALA B  1 28  ? 71.640  62.047  -7.268  1.00 38.71 ? 1   ALA B CB  1 
ATOM   1145  N  N   . THR B  1 29  ? 72.952  65.044  -6.487  1.00 28.18 ? 2   THR B N   1 
ATOM   1146  C  CA  . THR B  1 29  ? 72.567  66.438  -6.507  1.00 24.38 ? 2   THR B CA  1 
ATOM   1147  C  C   . THR B  1 29  ? 72.416  66.910  -7.950  1.00 20.22 ? 2   THR B C   1 
ATOM   1148  O  O   . THR B  1 29  ? 71.979  68.036  -8.178  1.00 19.25 ? 2   THR B O   1 
ATOM   1149  C  CB  . THR B  1 29  ? 73.556  67.338  -5.751  1.00 27.32 ? 2   THR B CB  1 
ATOM   1150  O  OG1 . THR B  1 29  ? 74.794  67.334  -6.474  1.00 28.30 ? 2   THR B OG1 1 
ATOM   1151  C  CG2 . THR B  1 29  ? 73.789  66.833  -4.328  1.00 29.02 ? 2   THR B CG2 1 
ATOM   1152  N  N   . LYS B  1 30  ? 72.818  66.086  -8.916  1.00 18.59 ? 3   LYS B N   1 
ATOM   1153  C  CA  . LYS B  1 30  ? 72.709  66.464  -10.331 1.00 18.06 ? 3   LYS B CA  1 
ATOM   1154  C  C   . LYS B  1 30  ? 72.253  65.303  -11.167 1.00 15.51 ? 3   LYS B C   1 
ATOM   1155  O  O   . LYS B  1 30  ? 72.677  64.158  -10.955 1.00 16.20 ? 3   LYS B O   1 
ATOM   1156  C  CB  . LYS B  1 30  ? 74.066  66.938  -10.907 1.00 19.85 ? 3   LYS B CB  1 
ATOM   1157  C  CG  . LYS B  1 30  ? 74.613  68.242  -10.301 1.00 27.18 ? 3   LYS B CG  1 
ATOM   1158  C  CD  . LYS B  1 30  ? 76.012  68.506  -10.891 1.00 32.72 ? 3   LYS B CD  1 
ATOM   1159  C  CE  . LYS B  1 30  ? 75.961  69.049  -12.315 1.00 32.39 ? 3   LYS B CE  1 
ATOM   1160  N  NZ  . LYS B  1 30  ? 77.358  69.478  -12.760 1.00 35.38 ? 3   LYS B NZ  1 
ATOM   1161  N  N   . ALA B  1 31  ? 71.468  65.611  -12.190 1.00 15.04 ? 4   ALA B N   1 
ATOM   1162  C  CA  . ALA B  1 31  ? 71.007  64.574  -13.117 1.00 14.59 ? 4   ALA B CA  1 
ATOM   1163  C  C   . ALA B  1 31  ? 70.974  65.201  -14.507 1.00 13.79 ? 4   ALA B C   1 
ATOM   1164  O  O   . ALA B  1 31  ? 71.071  66.440  -14.670 1.00 14.39 ? 4   ALA B O   1 
ATOM   1165  C  CB  . ALA B  1 31  ? 69.598  64.015  -12.714 1.00 14.32 ? 4   ALA B CB  1 
ATOM   1166  N  N   . VAL B  1 32  ? 70.836  64.346  -15.521 1.00 13.02 ? 5   VAL B N   1 
ATOM   1167  C  CA  . VAL B  1 32  ? 70.855  64.833  -16.910 1.00 13.75 ? 5   VAL B CA  1 
ATOM   1168  C  C   . VAL B  1 32  ? 69.980  63.871  -17.776 1.00 14.15 ? 5   VAL B C   1 
ATOM   1169  O  O   . VAL B  1 32  ? 69.796  62.690  -17.446 1.00 15.21 ? 5   VAL B O   1 
ATOM   1170  C  CB  . VAL B  1 32  ? 72.310  64.932  -17.429 1.00 14.56 ? 5   VAL B CB  1 
ATOM   1171  C  CG1 . VAL B  1 32  ? 72.965  63.541  -17.573 1.00 14.56 ? 5   VAL B CG1 1 
ATOM   1172  C  CG2 . VAL B  1 32  ? 72.398  65.709  -18.729 1.00 16.48 ? 5   VAL B CG2 1 
ATOM   1173  N  N   . CYS B  1 33  ? 69.459  64.404  -18.863 1.00 15.17 ? 6   CYS B N   1 
ATOM   1174  C  CA  . CYS B  1 33  ? 68.603  63.636  -19.736 1.00 15.80 ? 6   CYS B CA  1 
ATOM   1175  C  C   . CYS B  1 33  ? 68.880  64.057  -21.161 1.00 15.08 ? 6   CYS B C   1 
ATOM   1176  O  O   . CYS B  1 33  ? 68.856  65.231  -21.474 1.00 14.41 ? 6   CYS B O   1 
ATOM   1177  C  CB  . CYS B  1 33  ? 67.144  63.990  -19.394 1.00 18.10 ? 6   CYS B CB  1 
ATOM   1178  S  SG  . CYS B  1 33  ? 66.001  63.047  -20.409 1.00 19.73 ? 6   CYS B SG  1 
ATOM   1179  N  N   . VAL B  1 34  ? 69.132  63.085  -22.030 1.00 14.38 ? 7   VAL B N   1 
ATOM   1180  C  CA  . VAL B  1 34  ? 69.298  63.382  -23.441 1.00 15.41 ? 7   VAL B CA  1 
ATOM   1181  C  C   . VAL B  1 34  ? 68.000  63.023  -24.149 1.00 15.73 ? 7   VAL B C   1 
ATOM   1182  O  O   . VAL B  1 34  ? 67.575  61.872  -24.101 1.00 15.26 ? 7   VAL B O   1 
ATOM   1183  C  CB  . VAL B  1 34  ? 70.465  62.561  -24.041 1.00 16.70 ? 7   VAL B CB  1 
ATOM   1184  C  CG1 . VAL B  1 34  ? 70.507  62.781  -25.562 1.00 18.63 ? 7   VAL B CG1 1 
ATOM   1185  C  CG2 . VAL B  1 34  ? 71.751  62.960  -23.313 1.00 16.68 ? 7   VAL B CG2 1 
ATOM   1186  N  N   . LEU B  1 35  ? 67.350  64.021  -24.774 1.00 15.59 ? 8   LEU B N   1 
ATOM   1187  C  CA  . LEU B  1 35  ? 66.031  63.775  -25.387 1.00 16.35 ? 8   LEU B CA  1 
ATOM   1188  C  C   . LEU B  1 35  ? 66.268  63.490  -26.883 1.00 17.13 ? 8   LEU B C   1 
ATOM   1189  O  O   . LEU B  1 35  ? 67.034  64.217  -27.540 1.00 17.09 ? 8   LEU B O   1 
ATOM   1190  C  CB  . LEU B  1 35  ? 65.186  65.059  -25.292 1.00 18.26 ? 8   LEU B CB  1 
ATOM   1191  C  CG  . LEU B  1 35  ? 64.816  65.547  -23.868 1.00 20.21 ? 8   LEU B CG  1 
ATOM   1192  C  CD1 . LEU B  1 35  ? 63.989  66.837  -23.963 1.00 24.92 ? 8   LEU B CD1 1 
ATOM   1193  C  CD2 . LEU B  1 35  ? 63.896  64.549  -23.259 1.00 19.36 ? 8   LEU B CD2 1 
ATOM   1194  N  N   A LYS B  1 36  ? 65.648  62.426  -27.370 0.50 16.63 ? 9   LYS B N   1 
ATOM   1195  N  N   B LYS B  1 36  ? 65.651  62.436  -27.384 0.50 17.02 ? 9   LYS B N   1 
ATOM   1196  C  CA  A LYS B  1 36  ? 65.738  62.002  -28.770 0.50 18.91 ? 9   LYS B CA  1 
ATOM   1197  C  CA  B LYS B  1 36  ? 65.677  62.132  -28.812 0.50 19.59 ? 9   LYS B CA  1 
ATOM   1198  C  C   A LYS B  1 36  ? 64.373  61.442  -29.160 0.50 17.78 ? 9   LYS B C   1 
ATOM   1199  C  C   B LYS B  1 36  ? 64.354  61.491  -29.163 0.50 18.13 ? 9   LYS B C   1 
ATOM   1200  O  O   A LYS B  1 36  ? 63.649  60.936  -28.306 0.50 17.70 ? 9   LYS B O   1 
ATOM   1201  O  O   B LYS B  1 36  ? 63.658  60.961  -28.299 0.50 17.99 ? 9   LYS B O   1 
ATOM   1202  C  CB  A LYS B  1 36  ? 66.794  60.878  -28.920 0.50 20.44 ? 9   LYS B CB  1 
ATOM   1203  C  CB  B LYS B  1 36  ? 66.796  61.136  -29.145 0.50 22.09 ? 9   LYS B CB  1 
ATOM   1204  C  CG  A LYS B  1 36  ? 68.227  61.297  -28.584 0.50 23.66 ? 9   LYS B CG  1 
ATOM   1205  C  CG  B LYS B  1 36  ? 68.199  61.614  -28.813 0.50 26.14 ? 9   LYS B CG  1 
ATOM   1206  C  CD  A LYS B  1 36  ? 69.312  60.443  -29.257 0.50 23.20 ? 9   LYS B CD  1 
ATOM   1207  C  CD  B LYS B  1 36  ? 68.765  62.547  -29.876 0.50 27.38 ? 9   LYS B CD  1 
ATOM   1208  C  CE  A LYS B  1 36  ? 70.727  61.018  -28.990 0.50 22.02 ? 9   LYS B CE  1 
ATOM   1209  C  CE  B LYS B  1 36  ? 70.002  63.273  -29.356 0.50 25.32 ? 9   LYS B CE  1 
ATOM   1210  N  NZ  A LYS B  1 36  ? 71.439  60.030  -28.114 0.50 23.15 ? 9   LYS B NZ  1 
ATOM   1211  N  NZ  B LYS B  1 36  ? 69.657  64.460  -28.539 0.50 22.83 ? 9   LYS B NZ  1 
ATOM   1212  N  N   . GLY B  1 37  ? 64.006  61.502  -30.442 1.00 19.97 ? 10  GLY B N   1 
ATOM   1213  C  CA  . GLY B  1 37  ? 62.740  60.872  -30.863 1.00 22.46 ? 10  GLY B CA  1 
ATOM   1214  C  C   . GLY B  1 37  ? 62.835  60.431  -32.332 1.00 28.96 ? 10  GLY B C   1 
ATOM   1215  O  O   . GLY B  1 37  ? 63.912  60.307  -32.866 1.00 27.86 ? 10  GLY B O   1 
ATOM   1216  N  N   . ASP B  1 38  ? 61.695  60.267  -32.983 1.00 31.05 ? 11  ASP B N   1 
ATOM   1217  C  CA  . ASP B  1 38  ? 61.679  59.828  -34.383 1.00 37.45 ? 11  ASP B CA  1 
ATOM   1218  C  C   . ASP B  1 38  ? 61.892  60.935  -35.377 1.00 36.81 ? 11  ASP B C   1 
ATOM   1219  O  O   . ASP B  1 38  ? 62.225  60.689  -36.538 1.00 38.59 ? 11  ASP B O   1 
ATOM   1220  C  CB  . ASP B  1 38  ? 60.348  59.189  -34.677 1.00 39.66 ? 11  ASP B CB  1 
ATOM   1221  C  CG  . ASP B  1 38  ? 60.206  57.901  -33.991 1.00 43.79 ? 11  ASP B CG  1 
ATOM   1222  O  OD1 . ASP B  1 38  ? 61.246  57.227  -33.803 1.00 44.90 ? 11  ASP B OD1 1 
ATOM   1223  O  OD2 . ASP B  1 38  ? 59.076  57.578  -33.586 1.00 50.24 ? 11  ASP B OD2 1 
ATOM   1224  N  N   . GLY B  1 39  ? 61.714  62.153  -34.919 1.00 32.04 ? 12  GLY B N   1 
ATOM   1225  C  CA  . GLY B  1 39  ? 61.801  63.291  -35.767 1.00 30.17 ? 12  GLY B CA  1 
ATOM   1226  C  C   . GLY B  1 39  ? 63.007  64.110  -35.410 1.00 27.98 ? 12  GLY B C   1 
ATOM   1227  O  O   . GLY B  1 39  ? 63.999  63.603  -34.889 1.00 30.88 ? 12  GLY B O   1 
ATOM   1228  N  N   . PRO B  1 40  ? 62.915  65.403  -35.665 1.00 24.59 ? 13  PRO B N   1 
ATOM   1229  C  CA  . PRO B  1 40  ? 64.070  66.246  -35.527 1.00 24.87 ? 13  PRO B CA  1 
ATOM   1230  C  C   . PRO B  1 40  ? 64.279  66.768  -34.077 1.00 21.78 ? 13  PRO B C   1 
ATOM   1231  O  O   . PRO B  1 40  ? 65.240  67.475  -33.813 1.00 22.39 ? 13  PRO B O   1 
ATOM   1232  C  CB  . PRO B  1 40  ? 63.715  67.407  -36.435 1.00 24.14 ? 13  PRO B CB  1 
ATOM   1233  C  CG  . PRO B  1 40  ? 62.239  67.536  -36.245 1.00 26.05 ? 13  PRO B CG  1 
ATOM   1234  C  CD  . PRO B  1 40  ? 61.757  66.128  -36.247 1.00 25.45 ? 13  PRO B CD  1 
ATOM   1235  N  N   . VAL B  1 41  ? 63.379  66.426  -33.156 1.00 19.64 ? 14  VAL B N   1 
ATOM   1236  C  CA  . VAL B  1 41  ? 63.441  67.093  -31.823 1.00 18.61 ? 14  VAL B CA  1 
ATOM   1237  C  C   . VAL B  1 41  ? 64.516  66.424  -30.981 1.00 18.44 ? 14  VAL B C   1 
ATOM   1238  O  O   . VAL B  1 41  ? 64.519  65.195  -30.838 1.00 19.84 ? 14  VAL B O   1 
ATOM   1239  C  CB  . VAL B  1 41  ? 62.068  67.063  -31.114 1.00 17.64 ? 14  VAL B CB  1 
ATOM   1240  C  CG1 . VAL B  1 41  ? 62.198  67.676  -29.693 1.00 17.31 ? 14  VAL B CG1 1 
ATOM   1241  C  CG2 . VAL B  1 41  ? 61.080  67.912  -31.921 1.00 19.10 ? 14  VAL B CG2 1 
ATOM   1242  N  N   . GLN B  1 42  ? 65.441  67.222  -30.444 1.00 20.85 ? 15  GLN B N   1 
ATOM   1243  C  CA  . GLN B  1 42  ? 66.483  66.681  -29.591 1.00 19.49 ? 15  GLN B CA  1 
ATOM   1244  C  C   . GLN B  1 42  ? 67.052  67.717  -28.658 1.00 17.57 ? 15  GLN B C   1 
ATOM   1245  O  O   . GLN B  1 42  ? 67.010  68.922  -28.925 1.00 19.98 ? 15  GLN B O   1 
ATOM   1246  C  CB  . GLN B  1 42  ? 67.642  66.104  -30.420 1.00 23.78 ? 15  GLN B CB  1 
ATOM   1247  C  CG  . GLN B  1 42  ? 68.292  67.117  -31.299 1.00 29.57 ? 15  GLN B CG  1 
ATOM   1248  C  CD  . GLN B  1 42  ? 69.418  66.464  -32.116 1.00 41.67 ? 15  GLN B CD  1 
ATOM   1249  O  OE1 . GLN B  1 42  ? 69.300  66.303  -33.307 1.00 43.74 ? 15  GLN B OE1 1 
ATOM   1250  N  NE2 . GLN B  1 42  ? 70.493  66.062  -31.448 1.00 45.10 ? 15  GLN B NE2 1 
ATOM   1251  N  N   . GLY B  1 43  ? 67.610  67.255  -27.557 1.00 16.93 ? 16  GLY B N   1 
ATOM   1252  C  CA  . GLY B  1 43  ? 68.178  68.207  -26.604 1.00 17.26 ? 16  GLY B CA  1 
ATOM   1253  C  C   . GLY B  1 43  ? 68.762  67.564  -25.389 1.00 15.24 ? 16  GLY B C   1 
ATOM   1254  O  O   . GLY B  1 43  ? 68.824  66.368  -25.328 1.00 16.10 ? 16  GLY B O   1 
ATOM   1255  N  N   . ILE B  1 44  ? 69.281  68.397  -24.493 1.00 14.81 ? 17  ILE B N   1 
ATOM   1256  C  CA  . ILE B  1 44  ? 69.885  67.938  -23.296 1.00 14.60 ? 17  ILE B CA  1 
ATOM   1257  C  C   . ILE B  1 44  ? 69.285  68.790  -22.204 1.00 13.62 ? 17  ILE B C   1 
ATOM   1258  O  O   . ILE B  1 44  ? 69.374  70.022  -22.258 1.00 15.81 ? 17  ILE B O   1 
ATOM   1259  C  CB  . ILE B  1 44  ? 71.402  68.164  -23.344 1.00 16.47 ? 17  ILE B CB  1 
ATOM   1260  C  CG1 . ILE B  1 44  ? 72.049  67.126  -24.332 1.00 19.43 ? 17  ILE B CG1 1 
ATOM   1261  C  CG2 . ILE B  1 44  ? 72.004  67.949  -21.953 1.00 19.77 ? 17  ILE B CG2 1 
ATOM   1262  C  CD1 . ILE B  1 44  ? 73.518  67.505  -24.664 1.00 20.72 ? 17  ILE B CD1 1 
ATOM   1263  N  N   . ILE B  1 45  ? 68.760  68.129  -21.180 1.00 13.35 ? 18  ILE B N   1 
ATOM   1264  C  CA  . ILE B  1 45  ? 68.182  68.871  -20.035 1.00 13.58 ? 18  ILE B CA  1 
ATOM   1265  C  C   . ILE B  1 45  ? 68.943  68.447  -18.759 1.00 15.59 ? 18  ILE B C   1 
ATOM   1266  O  O   . ILE B  1 45  ? 69.145  67.234  -18.464 1.00 15.32 ? 18  ILE B O   1 
ATOM   1267  C  CB  . ILE B  1 45  ? 66.667  68.520  -19.876 1.00 14.13 ? 18  ILE B CB  1 
ATOM   1268  C  CG1 . ILE B  1 45  ? 65.864  69.014  -21.120 1.00 11.56 ? 18  ILE B CG1 1 
ATOM   1269  C  CG2 . ILE B  1 45  ? 66.088  69.125  -18.568 1.00 13.16 ? 18  ILE B CG2 1 
ATOM   1270  C  CD1 . ILE B  1 45  ? 65.975  70.565  -21.284 1.00 13.90 ? 18  ILE B CD1 1 
ATOM   1271  N  N   . ASN B  1 46  ? 69.347  69.459  -17.998 1.00 15.50 ? 19  ASN B N   1 
ATOM   1272  C  CA  . ASN B  1 46  ? 70.076  69.257  -16.734 1.00 15.15 ? 19  ASN B CA  1 
ATOM   1273  C  C   . ASN B  1 46  ? 69.150  69.452  -15.550 1.00 14.44 ? 19  ASN B C   1 
ATOM   1274  O  O   . ASN B  1 46  ? 68.208  70.268  -15.662 1.00 14.34 ? 19  ASN B O   1 
ATOM   1275  C  CB  . ASN B  1 46  ? 71.200  70.304  -16.656 1.00 17.50 ? 19  ASN B CB  1 
ATOM   1276  C  CG  . ASN B  1 46  ? 72.121  70.239  -17.871 1.00 19.25 ? 19  ASN B CG  1 
ATOM   1277  O  OD1 . ASN B  1 46  ? 72.089  71.114  -18.790 1.00 23.30 ? 19  ASN B OD1 1 
ATOM   1278  N  ND2 . ASN B  1 46  ? 72.891  69.215  -17.911 1.00 16.34 ? 19  ASN B ND2 1 
ATOM   1279  N  N   . PHE B  1 47  ? 69.414  68.747  -14.439 1.00 14.77 ? 20  PHE B N   1 
ATOM   1280  C  CA  . PHE B  1 47  ? 68.604  68.900  -13.199 1.00 13.55 ? 20  PHE B CA  1 
ATOM   1281  C  C   . PHE B  1 47  ? 69.626  69.097  -12.086 1.00 15.57 ? 20  PHE B C   1 
ATOM   1282  O  O   . PHE B  1 47  ? 70.663  68.354  -12.058 1.00 16.40 ? 20  PHE B O   1 
ATOM   1283  C  CB  . PHE B  1 47  ? 67.857  67.620  -12.864 1.00 14.23 ? 20  PHE B CB  1 
ATOM   1284  C  CG  . PHE B  1 47  ? 66.813  67.241  -13.896 1.00 16.39 ? 20  PHE B CG  1 
ATOM   1285  C  CD1 . PHE B  1 47  ? 67.185  66.503  -15.024 1.00 16.26 ? 20  PHE B CD1 1 
ATOM   1286  C  CD2 . PHE B  1 47  ? 65.496  67.686  -13.762 1.00 15.14 ? 20  PHE B CD2 1 
ATOM   1287  C  CE1 . PHE B  1 47  ? 66.232  66.187  -15.988 1.00 17.12 ? 20  PHE B CE1 1 
ATOM   1288  C  CE2 . PHE B  1 47  ? 64.521  67.344  -14.704 1.00 15.68 ? 20  PHE B CE2 1 
ATOM   1289  C  CZ  . PHE B  1 47  ? 64.921  66.585  -15.822 1.00 16.33 ? 20  PHE B CZ  1 
ATOM   1290  N  N   . GLU B  1 48  ? 69.385  70.057  -11.189 1.00 15.18 ? 21  GLU B N   1 
ATOM   1291  C  CA  . GLU B  1 48  ? 70.340  70.263  -10.067 1.00 18.43 ? 21  GLU B CA  1 
ATOM   1292  C  C   . GLU B  1 48  ? 69.509  70.459  -8.835  1.00 18.09 ? 21  GLU B C   1 
ATOM   1293  O  O   . GLU B  1 48  ? 68.522  71.198  -8.884  1.00 17.41 ? 21  GLU B O   1 
ATOM   1294  C  CB  . GLU B  1 48  ? 71.090  71.597  -10.260 1.00 20.70 ? 21  GLU B CB  1 
ATOM   1295  C  CG  . GLU B  1 48  ? 71.894  71.649  -11.496 1.00 30.02 ? 21  GLU B CG  1 
ATOM   1296  C  CD  . GLU B  1 48  ? 72.492  73.003  -11.803 1.00 31.17 ? 21  GLU B CD  1 
ATOM   1297  O  OE1 . GLU B  1 48  ? 72.519  73.952  -10.941 1.00 32.79 ? 21  GLU B OE1 1 
ATOM   1298  O  OE2 . GLU B  1 48  ? 72.945  73.088  -12.950 1.00 33.48 ? 21  GLU B OE2 1 
ATOM   1299  N  N   . GLN B  1 49  ? 69.941  69.906  -7.714  1.00 16.90 ? 22  GLN B N   1 
ATOM   1300  C  CA  . GLN B  1 49  ? 69.158  70.091  -6.491  1.00 18.39 ? 22  GLN B CA  1 
ATOM   1301  C  C   . GLN B  1 49  ? 70.180  70.288  -5.347  1.00 21.72 ? 22  GLN B C   1 
ATOM   1302  O  O   . GLN B  1 49  ? 70.901  69.348  -5.000  1.00 22.89 ? 22  GLN B O   1 
ATOM   1303  C  CB  . GLN B  1 49  ? 68.217  68.894  -6.269  1.00 17.05 ? 22  GLN B CB  1 
ATOM   1304  C  CG  . GLN B  1 49  ? 67.301  69.045  -5.034  1.00 17.26 ? 22  GLN B CG  1 
ATOM   1305  C  CD  . GLN B  1 49  ? 66.440  67.810  -4.816  1.00 18.94 ? 22  GLN B CD  1 
ATOM   1306  O  OE1 . GLN B  1 49  ? 66.843  66.723  -5.130  1.00 18.93 ? 22  GLN B OE1 1 
ATOM   1307  N  NE2 . GLN B  1 49  ? 65.266  67.986  -4.234  1.00 19.77 ? 22  GLN B NE2 1 
ATOM   1308  N  N   . LYS B  1 50  ? 70.216  71.505  -4.824  1.00 27.97 ? 23  LYS B N   1 
ATOM   1309  C  CA  . LYS B  1 50  ? 71.161  71.930  -3.752  1.00 33.96 ? 23  LYS B CA  1 
ATOM   1310  C  C   . LYS B  1 50  ? 70.952  71.090  -2.491  1.00 33.29 ? 23  LYS B C   1 
ATOM   1311  O  O   . LYS B  1 50  ? 71.902  70.532  -1.925  1.00 34.69 ? 23  LYS B O   1 
ATOM   1312  C  CB  . LYS B  1 50  ? 70.975  73.430  -3.473  1.00 36.79 ? 23  LYS B CB  1 
ATOM   1313  C  CG  . LYS B  1 50  ? 71.909  74.036  -2.414  1.00 41.18 ? 23  LYS B CG  1 
ATOM   1314  C  CD  . LYS B  1 50  ? 71.316  75.341  -1.876  1.00 47.27 ? 23  LYS B CD  1 
ATOM   1315  C  CE  . LYS B  1 50  ? 72.355  76.268  -1.235  1.00 55.02 ? 23  LYS B CE  1 
ATOM   1316  N  NZ  . LYS B  1 50  ? 73.601  75.575  -0.769  1.00 57.42 ? 23  LYS B NZ  1 
ATOM   1317  N  N   . GLU B  1 51  ? 69.698  70.937  -2.101  1.00 29.98 ? 24  GLU B N   1 
ATOM   1318  C  CA  . GLU B  1 51  ? 69.355  70.283  -0.842  1.00 30.73 ? 24  GLU B CA  1 
ATOM   1319  C  C   . GLU B  1 51  ? 68.255  69.303  -1.106  1.00 28.74 ? 24  GLU B C   1 
ATOM   1320  O  O   . GLU B  1 51  ? 67.380  69.598  -1.902  1.00 29.90 ? 24  GLU B O   1 
ATOM   1321  C  CB  . GLU B  1 51  ? 68.807  71.340  0.150   1.00 34.64 ? 24  GLU B CB  1 
ATOM   1322  C  CG  . GLU B  1 51  ? 69.747  72.490  0.468   1.00 43.65 ? 24  GLU B CG  1 
ATOM   1323  C  CD  . GLU B  1 51  ? 70.981  72.035  1.243   1.00 55.55 ? 24  GLU B CD  1 
ATOM   1324  O  OE1 . GLU B  1 51  ? 70.999  70.879  1.754   1.00 59.24 ? 24  GLU B OE1 1 
ATOM   1325  O  OE2 . GLU B  1 51  ? 71.951  72.818  1.322   1.00 56.77 ? 24  GLU B OE2 1 
ATOM   1326  N  N   . SER B  1 52  ? 68.230  68.169  -0.420  1.00 30.89 ? 25  SER B N   1 
ATOM   1327  C  CA  . SER B  1 52  ? 67.189  67.207  -0.707  1.00 37.13 ? 25  SER B CA  1 
ATOM   1328  C  C   . SER B  1 52  ? 65.830  67.765  -0.255  1.00 35.16 ? 25  SER B C   1 
ATOM   1329  O  O   . SER B  1 52  ? 64.800  67.375  -0.764  1.00 35.92 ? 25  SER B O   1 
ATOM   1330  C  CB  . SER B  1 52  ? 67.496  65.873  -0.059  1.00 39.09 ? 25  SER B CB  1 
ATOM   1331  O  OG  . SER B  1 52  ? 67.495  66.030  1.339   1.00 41.87 ? 25  SER B OG  1 
ATOM   1332  N  N   . ASN B  1 53  ? 65.831  68.753  0.627   1.00 35.05 ? 26  ASN B N   1 
ATOM   1333  C  CA  . ASN B  1 53  ? 64.550  69.384  0.938   1.00 42.86 ? 26  ASN B CA  1 
ATOM   1334  C  C   . ASN B  1 53  ? 64.050  70.291  -0.196  1.00 45.57 ? 26  ASN B C   1 
ATOM   1335  O  O   . ASN B  1 53  ? 62.857  70.349  -0.449  1.00 59.09 ? 26  ASN B O   1 
ATOM   1336  C  CB  . ASN B  1 53  ? 64.491  70.020  2.360   1.00 39.65 ? 26  ASN B CB  1 
ATOM   1337  C  CG  . ASN B  1 53  ? 65.464  71.196  2.583   1.00 43.93 ? 26  ASN B CG  1 
ATOM   1338  O  OD1 . ASN B  1 53  ? 66.414  71.436  1.832   1.00 42.63 ? 26  ASN B OD1 1 
ATOM   1339  N  ND2 . ASN B  1 53  ? 65.223  71.927  3.663   1.00 42.71 ? 26  ASN B ND2 1 
ATOM   1340  N  N   . GLY B  1 54  ? 64.971  70.866  -0.964  1.00 34.65 ? 27  GLY B N   1 
ATOM   1341  C  CA  . GLY B  1 54  ? 64.669  72.008  -1.770  1.00 32.77 ? 27  GLY B CA  1 
ATOM   1342  C  C   . GLY B  1 54  ? 64.292  71.774  -3.227  1.00 25.12 ? 27  GLY B C   1 
ATOM   1343  O  O   . GLY B  1 54  ? 64.171  70.654  -3.698  1.00 22.46 ? 27  GLY B O   1 
ATOM   1344  N  N   . PRO B  1 55  ? 64.077  72.876  -3.924  1.00 25.78 ? 28  PRO B N   1 
ATOM   1345  C  CA  . PRO B  1 55  ? 63.656  72.853  -5.295  1.00 24.14 ? 28  PRO B CA  1 
ATOM   1346  C  C   . PRO B  1 55  ? 64.756  72.271  -6.225  1.00 19.74 ? 28  PRO B C   1 
ATOM   1347  O  O   . PRO B  1 55  ? 65.950  72.281  -5.895  1.00 17.67 ? 28  PRO B O   1 
ATOM   1348  C  CB  . PRO B  1 55  ? 63.401  74.328  -5.597  1.00 24.63 ? 28  PRO B CB  1 
ATOM   1349  C  CG  . PRO B  1 55  ? 64.134  75.080  -4.545  1.00 28.69 ? 28  PRO B CG  1 
ATOM   1350  C  CD  . PRO B  1 55  ? 64.137  74.240  -3.362  1.00 27.61 ? 28  PRO B CD  1 
ATOM   1351  N  N   . VAL B  1 56  ? 64.303  71.795  -7.370  1.00 18.20 ? 29  VAL B N   1 
ATOM   1352  C  CA  . VAL B  1 56  ? 65.164  71.311  -8.424  1.00 15.29 ? 29  VAL B CA  1 
ATOM   1353  C  C   . VAL B  1 56  ? 65.173  72.361  -9.542  1.00 16.43 ? 29  VAL B C   1 
ATOM   1354  O  O   . VAL B  1 56  ? 64.099  72.840  -9.983  1.00 15.28 ? 29  VAL B O   1 
ATOM   1355  C  CB  . VAL B  1 56  ? 64.610  69.981  -8.966  1.00 15.19 ? 29  VAL B CB  1 
ATOM   1356  C  CG1 . VAL B  1 56  ? 65.508  69.460  -10.110 1.00 14.86 ? 29  VAL B CG1 1 
ATOM   1357  C  CG2 . VAL B  1 56  ? 64.556  68.927  -7.866  1.00 14.24 ? 29  VAL B CG2 1 
ATOM   1358  N  N   . LYS B  1 57  ? 66.374  72.757  -9.966  1.00 15.36 ? 30  LYS B N   1 
ATOM   1359  C  CA  . LYS B  1 57  ? 66.508  73.628  -11.114 1.00 17.46 ? 30  LYS B CA  1 
ATOM   1360  C  C   . LYS B  1 57  ? 66.626  72.745  -12.367 1.00 17.66 ? 30  LYS B C   1 
ATOM   1361  O  O   . LYS B  1 57  ? 67.403  71.755  -12.371 1.00 17.92 ? 30  LYS B O   1 
ATOM   1362  C  CB  . LYS B  1 57  ? 67.764  74.495  -10.902 1.00 19.73 ? 30  LYS B CB  1 
ATOM   1363  C  CG  . LYS B  1 57  ? 67.952  75.576  -11.969 1.00 29.79 ? 30  LYS B CG  1 
ATOM   1364  C  CD  . LYS B  1 57  ? 66.923  76.716  -11.768 1.00 40.38 ? 30  LYS B CD  1 
ATOM   1365  C  CE  . LYS B  1 57  ? 66.992  77.774  -12.865 1.00 47.34 ? 30  LYS B CE  1 
ATOM   1366  N  NZ  . LYS B  1 57  ? 66.611  77.104  -14.143 1.00 43.23 ? 30  LYS B NZ  1 
ATOM   1367  N  N   . VAL B  1 58  ? 65.922  73.107  -13.440 1.00 16.52 ? 31  VAL B N   1 
ATOM   1368  C  CA  . VAL B  1 58  ? 65.830  72.264  -14.638 1.00 15.12 ? 31  VAL B CA  1 
ATOM   1369  C  C   . VAL B  1 58  ? 66.191  73.207  -15.792 1.00 17.36 ? 31  VAL B C   1 
ATOM   1370  O  O   . VAL B  1 58  ? 65.554  74.283  -15.971 1.00 16.29 ? 31  VAL B O   1 
ATOM   1371  C  CB  . VAL B  1 58  ? 64.379  71.764  -14.848 1.00 16.02 ? 31  VAL B CB  1 
ATOM   1372  C  CG1 . VAL B  1 58  ? 64.347  70.853  -16.091 1.00 14.02 ? 31  VAL B CG1 1 
ATOM   1373  C  CG2 . VAL B  1 58  ? 63.847  70.999  -13.607 1.00 14.64 ? 31  VAL B CG2 1 
ATOM   1374  N  N   . TRP B  1 59  ? 67.241  72.919  -16.558 1.00 16.13 ? 32  TRP B N   1 
ATOM   1375  C  CA  . TRP B  1 59  ? 67.607  73.890  -17.587 1.00 17.06 ? 32  TRP B CA  1 
ATOM   1376  C  C   . TRP B  1 59  ? 68.342  73.175  -18.708 1.00 16.72 ? 32  TRP B C   1 
ATOM   1377  O  O   . TRP B  1 59  ? 68.955  72.123  -18.490 1.00 15.68 ? 32  TRP B O   1 
ATOM   1378  C  CB  . TRP B  1 59  ? 68.486  75.004  -17.024 1.00 18.49 ? 32  TRP B CB  1 
ATOM   1379  C  CG  . TRP B  1 59  ? 69.812  74.480  -16.438 1.00 21.50 ? 32  TRP B CG  1 
ATOM   1380  C  CD1 . TRP B  1 59  ? 70.027  73.957  -15.183 1.00 22.47 ? 32  TRP B CD1 1 
ATOM   1381  C  CD2 . TRP B  1 59  ? 71.046  74.400  -17.113 1.00 25.44 ? 32  TRP B CD2 1 
ATOM   1382  N  NE1 . TRP B  1 59  ? 71.311  73.563  -15.054 1.00 25.87 ? 32  TRP B NE1 1 
ATOM   1383  C  CE2 . TRP B  1 59  ? 71.966  73.820  -16.228 1.00 26.03 ? 32  TRP B CE2 1 
ATOM   1384  C  CE3 . TRP B  1 59  ? 71.459  74.739  -18.414 1.00 28.70 ? 32  TRP B CE3 1 
ATOM   1385  C  CZ2 . TRP B  1 59  ? 73.308  73.576  -16.577 1.00 31.18 ? 32  TRP B CZ2 1 
ATOM   1386  C  CZ3 . TRP B  1 59  ? 72.818  74.514  -18.762 1.00 33.40 ? 32  TRP B CZ3 1 
ATOM   1387  C  CH2 . TRP B  1 59  ? 73.714  73.948  -17.832 1.00 28.15 ? 32  TRP B CH2 1 
ATOM   1388  N  N   . GLY B  1 60  ? 68.328  73.750  -19.897 1.00 15.92 ? 33  GLY B N   1 
ATOM   1389  C  CA  . GLY B  1 60  ? 69.047  73.089  -21.012 1.00 17.01 ? 33  GLY B CA  1 
ATOM   1390  C  C   . GLY B  1 60  ? 68.379  73.590  -22.270 1.00 19.21 ? 33  GLY B C   1 
ATOM   1391  O  O   . GLY B  1 60  ? 67.622  74.538  -22.246 1.00 21.72 ? 33  GLY B O   1 
ATOM   1392  N  N   . SER B  1 61  ? 68.668  72.975  -23.392 1.00 18.48 ? 34  SER B N   1 
ATOM   1393  C  CA  . SER B  1 61  ? 68.138  73.502  -24.628 1.00 19.33 ? 34  SER B CA  1 
ATOM   1394  C  C   . SER B  1 61  ? 67.570  72.339  -25.444 1.00 19.76 ? 34  SER B C   1 
ATOM   1395  O  O   . SER B  1 61  ? 68.161  71.225  -25.476 1.00 20.45 ? 34  SER B O   1 
ATOM   1396  C  CB  . SER B  1 61  ? 69.309  74.193  -25.325 1.00 23.63 ? 34  SER B CB  1 
ATOM   1397  O  OG  . SER B  1 61  ? 68.901  74.506  -26.607 1.00 32.66 ? 34  SER B OG  1 
ATOM   1398  N  N   . ILE B  1 62  ? 66.428  72.552  -26.095 1.00 15.68 ? 35  ILE B N   1 
ATOM   1399  C  CA  . ILE B  1 62  ? 65.838  71.527  -26.945 1.00 16.65 ? 35  ILE B CA  1 
ATOM   1400  C  C   . ILE B  1 62  ? 65.668  72.214  -28.308 1.00 20.07 ? 35  ILE B C   1 
ATOM   1401  O  O   . ILE B  1 62  ? 65.221  73.368  -28.352 1.00 19.12 ? 35  ILE B O   1 
ATOM   1402  C  CB  . ILE B  1 62  ? 64.433  71.109  -26.445 1.00 16.43 ? 35  ILE B CB  1 
ATOM   1403  C  CG1 . ILE B  1 62  ? 64.498  70.602  -25.004 1.00 16.12 ? 35  ILE B CG1 1 
ATOM   1404  C  CG2 . ILE B  1 62  ? 63.822  70.048  -27.378 1.00 17.62 ? 35  ILE B CG2 1 
ATOM   1405  C  CD1 . ILE B  1 62  ? 63.115  70.290  -24.386 1.00 19.03 ? 35  ILE B CD1 1 
ATOM   1406  N  N   . LYS B  1 63  ? 66.027  71.526  -29.399 1.00 19.14 ? 36  LYS B N   1 
ATOM   1407  C  CA  . LYS B  1 63  ? 65.873  72.161  -30.691 1.00 21.26 ? 36  LYS B CA  1 
ATOM   1408  C  C   . LYS B  1 63  ? 65.013  71.320  -31.600 1.00 19.81 ? 36  LYS B C   1 
ATOM   1409  O  O   . LYS B  1 63  ? 64.643  70.204  -31.261 1.00 18.76 ? 36  LYS B O   1 
ATOM   1410  C  CB  . LYS B  1 63  ? 67.259  72.428  -31.285 1.00 25.36 ? 36  LYS B CB  1 
ATOM   1411  C  CG  . LYS B  1 63  ? 67.955  71.190  -31.759 1.00 30.82 ? 36  LYS B CG  1 
ATOM   1412  C  CD  . LYS B  1 63  ? 69.279  71.558  -32.434 1.00 40.76 ? 36  LYS B CD  1 
ATOM   1413  C  CE  . LYS B  1 63  ? 70.248  70.388  -32.413 1.00 44.78 ? 36  LYS B CE  1 
ATOM   1414  N  NZ  . LYS B  1 63  ? 69.726  69.337  -33.323 1.00 49.44 ? 36  LYS B NZ  1 
ATOM   1415  N  N   . GLY B  1 64  ? 64.652  71.867  -32.763 1.00 19.25 ? 37  GLY B N   1 
ATOM   1416  C  CA  . GLY B  1 64  ? 63.801  71.135  -33.681 1.00 19.19 ? 37  GLY B CA  1 
ATOM   1417  C  C   . GLY B  1 64  ? 62.314  71.223  -33.421 1.00 19.58 ? 37  GLY B C   1 
ATOM   1418  O  O   . GLY B  1 64  ? 61.513  70.482  -34.022 1.00 20.60 ? 37  GLY B O   1 
ATOM   1419  N  N   . LEU B  1 65  ? 61.896  72.124  -32.533 1.00 18.45 ? 38  LEU B N   1 
ATOM   1420  C  CA  . LEU B  1 65  ? 60.488  72.166  -32.142 1.00 16.51 ? 38  LEU B CA  1 
ATOM   1421  C  C   . LEU B  1 65  ? 59.764  73.195  -33.009 1.00 18.94 ? 38  LEU B C   1 
ATOM   1422  O  O   . LEU B  1 65  ? 60.417  74.138  -33.430 1.00 20.79 ? 38  LEU B O   1 
ATOM   1423  C  CB  . LEU B  1 65  ? 60.380  72.685  -30.685 1.00 16.65 ? 38  LEU B CB  1 
ATOM   1424  C  CG  . LEU B  1 65  ? 60.811  71.614  -29.612 1.00 15.47 ? 38  LEU B CG  1 
ATOM   1425  C  CD1 . LEU B  1 65  ? 61.130  72.369  -28.324 1.00 16.89 ? 38  LEU B CD1 1 
ATOM   1426  C  CD2 . LEU B  1 65  ? 59.741  70.542  -29.383 1.00 15.85 ? 38  LEU B CD2 1 
ATOM   1427  N  N   . THR B  1 66  ? 58.445  73.049  -33.185 1.00 20.39 ? 39  THR B N   1 
ATOM   1428  C  CA  . THR B  1 66  ? 57.601  74.147  -33.693 1.00 21.33 ? 39  THR B CA  1 
ATOM   1429  C  C   . THR B  1 66  ? 57.589  75.331  -32.694 1.00 23.78 ? 39  THR B C   1 
ATOM   1430  O  O   . THR B  1 66  ? 57.511  75.116  -31.473 1.00 19.93 ? 39  THR B O   1 
ATOM   1431  C  CB  . THR B  1 66  ? 56.139  73.687  -33.950 1.00 22.21 ? 39  THR B CB  1 
ATOM   1432  O  OG1 . THR B  1 66  ? 55.536  73.215  -32.730 1.00 22.69 ? 39  THR B OG1 1 
ATOM   1433  C  CG2 . THR B  1 66  ? 56.076  72.527  -35.028 1.00 21.58 ? 39  THR B CG2 1 
ATOM   1434  N  N   . GLU B  1 67  ? 57.585  76.569  -33.204 1.00 20.62 ? 40  GLU B N   1 
ATOM   1435  C  CA  . GLU B  1 67  ? 57.543  77.751  -32.345 1.00 22.60 ? 40  GLU B CA  1 
ATOM   1436  C  C   . GLU B  1 67  ? 56.307  77.659  -31.455 1.00 23.64 ? 40  GLU B C   1 
ATOM   1437  O  O   . GLU B  1 67  ? 55.245  77.255  -31.918 1.00 22.59 ? 40  GLU B O   1 
ATOM   1438  C  CB  . GLU B  1 67  ? 57.456  79.019  -33.242 1.00 24.00 ? 40  GLU B CB  1 
ATOM   1439  C  CG  . GLU B  1 67  ? 57.391  80.308  -32.468 1.00 25.22 ? 40  GLU B CG  1 
ATOM   1440  C  CD  . GLU B  1 67  ? 57.360  81.537  -33.400 1.00 33.91 ? 40  GLU B CD  1 
ATOM   1441  O  OE1 . GLU B  1 67  ? 57.337  81.349  -34.636 1.00 31.74 ? 40  GLU B OE1 1 
ATOM   1442  O  OE2 . GLU B  1 67  ? 57.435  82.672  -32.877 1.00 34.33 ? 40  GLU B OE2 1 
ATOM   1443  N  N   . GLY B  1 68  ? 56.447  77.993  -30.182 1.00 20.59 ? 41  GLY B N   1 
ATOM   1444  C  CA  . GLY B  1 68  ? 55.299  78.071  -29.276 1.00 22.33 ? 41  GLY B CA  1 
ATOM   1445  C  C   . GLY B  1 68  ? 55.428  77.072  -28.122 1.00 20.45 ? 41  GLY B C   1 
ATOM   1446  O  O   . GLY B  1 68  ? 56.550  76.601  -27.821 1.00 18.53 ? 41  GLY B O   1 
ATOM   1447  N  N   . LEU B  1 69  ? 54.292  76.767  -27.488 1.00 18.21 ? 42  LEU B N   1 
ATOM   1448  C  CA  . LEU B  1 69  ? 54.287  75.997  -26.235 1.00 18.99 ? 42  LEU B CA  1 
ATOM   1449  C  C   . LEU B  1 69  ? 54.270  74.506  -26.486 1.00 17.47 ? 42  LEU B C   1 
ATOM   1450  O  O   . LEU B  1 69  ? 53.552  74.050  -27.375 1.00 16.15 ? 42  LEU B O   1 
ATOM   1451  C  CB  . LEU B  1 69  ? 53.019  76.349  -25.382 1.00 19.54 ? 42  LEU B CB  1 
ATOM   1452  C  CG  . LEU B  1 69  ? 52.934  77.783  -24.824 1.00 23.50 ? 42  LEU B CG  1 
ATOM   1453  C  CD1 . LEU B  1 69  ? 51.495  78.006  -24.307 1.00 23.36 ? 42  LEU B CD1 1 
ATOM   1454  C  CD2 . LEU B  1 69  ? 53.861  77.980  -23.672 1.00 23.11 ? 42  LEU B CD2 1 
ATOM   1455  N  N   . HIS B  1 70  ? 55.014  73.740  -25.669 1.00 13.94 ? 43  HIS B N   1 
ATOM   1456  C  CA  . HIS B  1 70  ? 55.014  72.263  -25.691 1.00 13.58 ? 43  HIS B CA  1 
ATOM   1457  C  C   . HIS B  1 70  ? 54.961  71.717  -24.283 1.00 12.13 ? 43  HIS B C   1 
ATOM   1458  O  O   . HIS B  1 70  ? 55.795  72.117  -23.457 1.00 13.52 ? 43  HIS B O   1 
ATOM   1459  C  CB  . HIS B  1 70  ? 56.363  71.839  -26.338 1.00 13.33 ? 43  HIS B CB  1 
ATOM   1460  C  CG  . HIS B  1 70  ? 56.422  72.232  -27.787 1.00 15.42 ? 43  HIS B CG  1 
ATOM   1461  N  ND1 . HIS B  1 70  ? 55.965  71.411  -28.790 1.00 17.06 ? 43  HIS B ND1 1 
ATOM   1462  C  CD2 . HIS B  1 70  ? 56.868  73.362  -28.388 1.00 15.26 ? 43  HIS B CD2 1 
ATOM   1463  C  CE1 . HIS B  1 70  ? 56.127  72.027  -29.956 1.00 16.17 ? 43  HIS B CE1 1 
ATOM   1464  N  NE2 . HIS B  1 70  ? 56.658  73.211  -29.729 1.00 17.63 ? 43  HIS B NE2 1 
ATOM   1465  N  N   . GLY B  1 71  ? 54.086  70.747  -24.050 1.00 13.42 ? 44  GLY B N   1 
ATOM   1466  C  CA  . GLY B  1 71  ? 53.934  70.066  -22.765 1.00 12.67 ? 44  GLY B CA  1 
ATOM   1467  C  C   . GLY B  1 71  ? 55.306  69.428  -22.400 1.00 13.49 ? 44  GLY B C   1 
ATOM   1468  O  O   . GLY B  1 71  ? 56.005  68.952  -23.292 1.00 12.40 ? 44  GLY B O   1 
ATOM   1469  N  N   . PHE B  1 72  ? 55.638  69.410  -21.129 1.00 12.90 ? 45  PHE B N   1 
ATOM   1470  C  CA  . PHE B  1 72  ? 57.002  69.028  -20.699 1.00 15.12 ? 45  PHE B CA  1 
ATOM   1471  C  C   . PHE B  1 72  ? 56.758  68.274  -19.415 1.00 14.64 ? 45  PHE B C   1 
ATOM   1472  O  O   . PHE B  1 72  ? 56.427  68.882  -18.400 1.00 14.49 ? 45  PHE B O   1 
ATOM   1473  C  CB  . PHE B  1 72  ? 57.834  70.307  -20.486 1.00 14.78 ? 45  PHE B CB  1 
ATOM   1474  C  CG  . PHE B  1 72  ? 59.307  70.072  -20.210 1.00 14.93 ? 45  PHE B CG  1 
ATOM   1475  C  CD1 . PHE B  1 72  ? 60.160  69.505  -21.204 1.00 17.20 ? 45  PHE B CD1 1 
ATOM   1476  C  CD2 . PHE B  1 72  ? 59.846  70.483  -18.985 1.00 14.51 ? 45  PHE B CD2 1 
ATOM   1477  C  CE1 . PHE B  1 72  ? 61.572  69.408  -20.946 1.00 15.82 ? 45  PHE B CE1 1 
ATOM   1478  C  CE2 . PHE B  1 72  ? 61.219  70.312  -18.716 1.00 14.63 ? 45  PHE B CE2 1 
ATOM   1479  C  CZ  . PHE B  1 72  ? 62.048  69.803  -19.706 1.00 14.85 ? 45  PHE B CZ  1 
ATOM   1480  N  N   . HIS B  1 73  ? 56.902  66.939  -19.454 1.00 13.21 ? 46  HIS B N   1 
ATOM   1481  C  CA  . HIS B  1 73  ? 56.485  66.118  -18.318 1.00 14.33 ? 46  HIS B CA  1 
ATOM   1482  C  C   . HIS B  1 73  ? 57.472  65.030  -17.984 1.00 14.43 ? 46  HIS B C   1 
ATOM   1483  O  O   . HIS B  1 73  ? 58.093  64.464  -18.869 1.00 14.80 ? 46  HIS B O   1 
ATOM   1484  C  CB  . HIS B  1 73  ? 55.141  65.424  -18.610 1.00 16.44 ? 46  HIS B CB  1 
ATOM   1485  C  CG  . HIS B  1 73  ? 54.081  66.380  -19.072 1.00 17.70 ? 46  HIS B CG  1 
ATOM   1486  N  ND1 . HIS B  1 73  ? 53.443  66.246  -20.284 1.00 19.37 ? 46  HIS B ND1 1 
ATOM   1487  C  CD2 . HIS B  1 73  ? 53.590  67.508  -18.506 1.00 17.93 ? 46  HIS B CD2 1 
ATOM   1488  C  CE1 . HIS B  1 73  ? 52.567  67.233  -20.433 1.00 20.38 ? 46  HIS B CE1 1 
ATOM   1489  N  NE2 . HIS B  1 73  ? 52.662  68.035  -19.386 1.00 20.40 ? 46  HIS B NE2 1 
ATOM   1490  N  N   . VAL B  1 74  ? 57.536  64.689  -16.711 1.00 13.80 ? 47  VAL B N   1 
ATOM   1491  C  CA  . VAL B  1 74  ? 58.199  63.435  -16.317 1.00 13.99 ? 47  VAL B CA  1 
ATOM   1492  C  C   . VAL B  1 74  ? 57.173  62.316  -16.289 1.00 14.59 ? 47  VAL B C   1 
ATOM   1493  O  O   . VAL B  1 74  ? 56.129  62.399  -15.604 1.00 15.55 ? 47  VAL B O   1 
ATOM   1494  C  CB  . VAL B  1 74  ? 58.835  63.538  -14.932 1.00 13.85 ? 47  VAL B CB  1 
ATOM   1495  C  CG1 . VAL B  1 74  ? 59.577  62.222  -14.593 1.00 13.59 ? 47  VAL B CG1 1 
ATOM   1496  C  CG2 . VAL B  1 74  ? 59.816  64.700  -14.900 1.00 15.07 ? 47  VAL B CG2 1 
ATOM   1497  N  N   . HIS B  1 75  ? 57.439  61.253  -17.047 1.00 12.57 ? 48  HIS B N   1 
ATOM   1498  C  CA  . HIS B  1 75  ? 56.524  60.115  -17.120 1.00 12.69 ? 48  HIS B CA  1 
ATOM   1499  C  C   . HIS B  1 75  ? 57.088  58.983  -16.229 1.00 14.94 ? 48  HIS B C   1 
ATOM   1500  O  O   . HIS B  1 75  ? 58.299  58.989  -15.881 1.00 15.70 ? 48  HIS B O   1 
ATOM   1501  C  CB  . HIS B  1 75  ? 56.437  59.666  -18.614 1.00 13.09 ? 48  HIS B CB  1 
ATOM   1502  C  CG  . HIS B  1 75  ? 55.622  60.595  -19.458 1.00 13.52 ? 48  HIS B CG  1 
ATOM   1503  N  ND1 . HIS B  1 75  ? 54.429  60.218  -20.022 1.00 14.29 ? 48  HIS B ND1 1 
ATOM   1504  C  CD2 . HIS B  1 75  ? 55.820  61.894  -19.814 1.00 13.74 ? 48  HIS B CD2 1 
ATOM   1505  C  CE1 . HIS B  1 75  ? 53.957  61.215  -20.759 1.00 15.04 ? 48  HIS B CE1 1 
ATOM   1506  N  NE2 . HIS B  1 75  ? 54.771  62.257  -20.624 1.00 15.71 ? 48  HIS B NE2 1 
ATOM   1507  N  N   . GLU B  1 76  ? 56.249  58.022  -15.873 1.00 14.04 ? 49  GLU B N   1 
ATOM   1508  C  CA  . GLU B  1 76  ? 56.514  57.139  -14.778 1.00 15.86 ? 49  GLU B CA  1 
ATOM   1509  C  C   . GLU B  1 76  ? 57.703  56.168  -15.008 1.00 17.08 ? 49  GLU B C   1 
ATOM   1510  O  O   . GLU B  1 76  ? 58.524  55.975  -14.120 1.00 17.80 ? 49  GLU B O   1 
ATOM   1511  C  CB  . GLU B  1 76  ? 55.231  56.328  -14.507 1.00 16.98 ? 49  GLU B CB  1 
ATOM   1512  C  CG  . GLU B  1 76  ? 55.399  55.439  -13.269 1.00 20.32 ? 49  GLU B CG  1 
ATOM   1513  C  CD  . GLU B  1 76  ? 54.118  54.676  -12.935 1.00 25.04 ? 49  GLU B CD  1 
ATOM   1514  O  OE1 . GLU B  1 76  ? 53.126  54.814  -13.672 1.00 24.71 ? 49  GLU B OE1 1 
ATOM   1515  O  OE2 . GLU B  1 76  ? 54.159  53.904  -11.963 1.00 27.26 ? 49  GLU B OE2 1 
ATOM   1516  N  N   . PHE B  1 77  ? 57.794  55.579  -16.196 1.00 16.57 ? 50  PHE B N   1 
ATOM   1517  C  CA  . PHE B  1 77  ? 58.800  54.516  -16.419 1.00 16.14 ? 50  PHE B CA  1 
ATOM   1518  C  C   . PHE B  1 77  ? 59.971  55.008  -17.279 1.00 16.60 ? 50  PHE B C   1 
ATOM   1519  O  O   . PHE B  1 77  ? 59.778  55.709  -18.266 1.00 16.93 ? 50  PHE B O   1 
ATOM   1520  C  CB  . PHE B  1 77  ? 58.160  53.306  -17.070 1.00 16.17 ? 50  PHE B CB  1 
ATOM   1521  C  CG  . PHE B  1 77  ? 56.963  52.816  -16.332 1.00 19.83 ? 50  PHE B CG  1 
ATOM   1522  C  CD1 . PHE B  1 77  ? 57.079  52.330  -15.058 1.00 20.67 ? 50  PHE B CD1 1 
ATOM   1523  C  CD2 . PHE B  1 77  ? 55.681  52.865  -16.940 1.00 24.05 ? 50  PHE B CD2 1 
ATOM   1524  C  CE1 . PHE B  1 77  ? 55.941  51.908  -14.346 1.00 23.33 ? 50  PHE B CE1 1 
ATOM   1525  C  CE2 . PHE B  1 77  ? 54.547  52.397  -16.245 1.00 23.77 ? 50  PHE B CE2 1 
ATOM   1526  C  CZ  . PHE B  1 77  ? 54.695  51.948  -14.944 1.00 23.35 ? 50  PHE B CZ  1 
ATOM   1527  N  N   . GLY B  1 78  ? 61.176  54.575  -16.937 1.00 17.31 ? 51  GLY B N   1 
ATOM   1528  C  CA  . GLY B  1 78  ? 62.398  54.907  -17.695 1.00 15.15 ? 51  GLY B CA  1 
ATOM   1529  C  C   . GLY B  1 78  ? 62.574  53.764  -18.713 1.00 19.52 ? 51  GLY B C   1 
ATOM   1530  O  O   . GLY B  1 78  ? 63.634  53.142  -18.796 1.00 17.45 ? 51  GLY B O   1 
ATOM   1531  N  N   . ASP B  1 79  ? 61.529  53.484  -19.470 1.00 19.42 ? 52  ASP B N   1 
ATOM   1532  C  CA  . ASP B  1 79  ? 61.460  52.293  -20.400 1.00 18.10 ? 52  ASP B CA  1 
ATOM   1533  C  C   . ASP B  1 79  ? 61.261  52.875  -21.800 1.00 19.08 ? 52  ASP B C   1 
ATOM   1534  O  O   . ASP B  1 79  ? 60.180  53.411  -22.136 1.00 20.62 ? 52  ASP B O   1 
ATOM   1535  C  CB  . ASP B  1 79  ? 60.261  51.416  -20.010 1.00 19.62 ? 52  ASP B CB  1 
ATOM   1536  C  CG  . ASP B  1 79  ? 60.097  50.191  -20.918 1.00 20.90 ? 52  ASP B CG  1 
ATOM   1537  O  OD1 . ASP B  1 79  ? 60.574  50.201  -22.068 1.00 20.91 ? 52  ASP B OD1 1 
ATOM   1538  O  OD2 . ASP B  1 79  ? 59.496  49.237  -20.444 1.00 22.87 ? 52  ASP B OD2 1 
ATOM   1539  N  N   . ASN B  1 80  ? 62.301  52.790  -22.606 1.00 18.27 ? 53  ASN B N   1 
ATOM   1540  C  CA  . ASN B  1 80  ? 62.296  53.261  -23.992 1.00 22.22 ? 53  ASN B CA  1 
ATOM   1541  C  C   . ASN B  1 80  ? 62.210  52.100  -24.994 1.00 22.21 ? 53  ASN B C   1 
ATOM   1542  O  O   . ASN B  1 80  ? 62.525  52.300  -26.170 1.00 22.73 ? 53  ASN B O   1 
ATOM   1543  C  CB  . ASN B  1 80  ? 63.608  54.033  -24.298 1.00 26.60 ? 53  ASN B CB  1 
ATOM   1544  C  CG  . ASN B  1 80  ? 63.499  54.888  -25.558 1.00 35.13 ? 53  ASN B CG  1 
ATOM   1545  O  OD1 . ASN B  1 80  ? 62.462  55.528  -25.782 1.00 41.20 ? 53  ASN B OD1 1 
ATOM   1546  N  ND2 . ASN B  1 80  ? 64.557  54.881  -26.414 1.00 36.47 ? 53  ASN B ND2 1 
ATOM   1547  N  N   . THR B  1 81  ? 61.801  50.928  -24.535 1.00 20.49 ? 54  THR B N   1 
ATOM   1548  C  CA  . THR B  1 81  ? 61.828  49.737  -25.413 1.00 23.28 ? 54  THR B CA  1 
ATOM   1549  C  C   . THR B  1 81  ? 60.898  49.918  -26.616 1.00 28.48 ? 54  THR B C   1 
ATOM   1550  O  O   . THR B  1 81  ? 61.224  49.486  -27.700 1.00 26.92 ? 54  THR B O   1 
ATOM   1551  C  CB  . THR B  1 81  ? 61.475  48.450  -24.720 1.00 23.33 ? 54  THR B CB  1 
ATOM   1552  O  OG1 . THR B  1 81  ? 60.236  48.604  -24.041 1.00 23.14 ? 54  THR B OG1 1 
ATOM   1553  C  CG2 . THR B  1 81  ? 62.537  48.074  -23.696 1.00 22.34 ? 54  THR B CG2 1 
ATOM   1554  N  N   . ALA B  1 82  ? 59.775  50.596  -26.464 1.00 24.59 ? 55  ALA B N   1 
ATOM   1555  C  CA  . ALA B  1 82  ? 59.006  50.923  -27.665 1.00 27.93 ? 55  ALA B CA  1 
ATOM   1556  C  C   . ALA B  1 82  ? 58.994  52.423  -27.893 1.00 28.21 ? 55  ALA B C   1 
ATOM   1557  O  O   . ALA B  1 82  ? 57.973  53.003  -28.179 1.00 33.84 ? 55  ALA B O   1 
ATOM   1558  C  CB  . ALA B  1 82  ? 57.594  50.355  -27.536 1.00 30.37 ? 55  ALA B CB  1 
ATOM   1559  N  N   . GLY B  1 83  ? 60.128  53.072  -27.707 1.00 24.85 ? 56  GLY B N   1 
ATOM   1560  C  CA  . GLY B  1 83  ? 60.202  54.523  -27.925 1.00 25.35 ? 56  GLY B CA  1 
ATOM   1561  C  C   . GLY B  1 83  ? 59.504  55.225  -26.765 1.00 23.34 ? 56  GLY B C   1 
ATOM   1562  O  O   . GLY B  1 83  ? 59.361  54.659  -25.657 1.00 23.00 ? 56  GLY B O   1 
ATOM   1563  N  N   . CYS B  1 84  ? 58.994  56.425  -27.026 1.00 22.89 ? 57  CYS B N   1 
ATOM   1564  C  CA  . CYS B  1 84  ? 58.416  57.249  -25.918 1.00 22.58 ? 57  CYS B CA  1 
ATOM   1565  C  C   . CYS B  1 84  ? 57.149  56.642  -25.328 1.00 21.93 ? 57  CYS B C   1 
ATOM   1566  O  O   . CYS B  1 84  ? 56.788  56.918  -24.168 1.00 18.24 ? 57  CYS B O   1 
ATOM   1567  C  CB  . CYS B  1 84  ? 58.196  58.685  -26.444 1.00 25.82 ? 57  CYS B CB  1 
ATOM   1568  S  SG  . CYS B  1 84  ? 59.802  59.478  -26.889 1.00 31.01 ? 57  CYS B SG  1 
ATOM   1569  N  N   . THR B  1 85  ? 56.425  55.850  -26.132 1.00 19.33 ? 58  THR B N   1 
ATOM   1570  C  CA  . THR B  1 85  ? 55.194  55.212  -25.665 1.00 22.50 ? 58  THR B CA  1 
ATOM   1571  C  C   . THR B  1 85  ? 55.349  54.346  -24.448 1.00 19.64 ? 58  THR B C   1 
ATOM   1572  O  O   . THR B  1 85  ? 54.466  54.319  -23.569 1.00 20.45 ? 58  THR B O   1 
ATOM   1573  C  CB  . THR B  1 85  ? 54.572  54.338  -26.771 1.00 25.86 ? 58  THR B CB  1 
ATOM   1574  O  OG1 . THR B  1 85  ? 54.431  55.161  -27.893 1.00 29.14 ? 58  THR B OG1 1 
ATOM   1575  C  CG2 . THR B  1 85  ? 53.181  53.853  -26.328 1.00 28.58 ? 58  THR B CG2 1 
ATOM   1576  N  N   . SER B  1 86  ? 56.480  53.634  -24.340 1.00 19.24 ? 59  SER B N   1 
ATOM   1577  C  CA  A SER B  1 86  ? 56.667  52.731  -23.203 0.50 17.48 ? 59  SER B CA  1 
ATOM   1578  C  CA  B SER B  1 86  ? 56.742  52.732  -23.212 0.50 18.55 ? 59  SER B CA  1 
ATOM   1579  C  C   . SER B  1 86  ? 56.977  53.460  -21.894 1.00 17.20 ? 59  SER B C   1 
ATOM   1580  O  O   . SER B  1 86  ? 57.020  52.837  -20.833 1.00 17.49 ? 59  SER B O   1 
ATOM   1581  C  CB  A SER B  1 86  ? 57.756  51.676  -23.495 0.50 17.29 ? 59  SER B CB  1 
ATOM   1582  C  CB  B SER B  1 86  ? 57.986  51.871  -23.492 0.50 19.26 ? 59  SER B CB  1 
ATOM   1583  O  OG  A SER B  1 86  ? 58.813  52.239  -24.255 0.50 15.27 ? 59  SER B OG  1 
ATOM   1584  O  OG  B SER B  1 86  ? 57.849  51.170  -24.703 0.50 20.72 ? 59  SER B OG  1 
ATOM   1585  N  N   . ALA B  1 87  ? 57.206  54.772  -21.953 1.00 16.88 ? 60  ALA B N   1 
ATOM   1586  C  CA  . ALA B  1 87  ? 57.388  55.522  -20.672 1.00 17.58 ? 60  ALA B CA  1 
ATOM   1587  C  C   . ALA B  1 87  ? 56.109  55.582  -19.809 1.00 17.90 ? 60  ALA B C   1 
ATOM   1588  O  O   . ALA B  1 87  ? 56.155  55.996  -18.657 1.00 15.91 ? 60  ALA B O   1 
ATOM   1589  C  CB  . ALA B  1 87  ? 57.860  56.955  -20.967 1.00 15.79 ? 60  ALA B CB  1 
ATOM   1590  N  N   . GLY B  1 88  ? 54.955  55.196  -20.349 1.00 19.70 ? 61  GLY B N   1 
ATOM   1591  C  CA  . GLY B  1 88  ? 53.757  55.157  -19.477 1.00 18.00 ? 61  GLY B CA  1 
ATOM   1592  C  C   . GLY B  1 88  ? 53.162  56.582  -19.268 1.00 17.56 ? 61  GLY B C   1 
ATOM   1593  O  O   . GLY B  1 88  ? 53.468  57.490  -20.023 1.00 16.98 ? 61  GLY B O   1 
ATOM   1594  N  N   . PRO B  1 89  ? 52.335  56.759  -18.228 1.00 18.60 ? 62  PRO B N   1 
ATOM   1595  C  CA  . PRO B  1 89  ? 51.610  58.036  -18.060 1.00 18.61 ? 62  PRO B CA  1 
ATOM   1596  C  C   . PRO B  1 89  ? 52.494  59.029  -17.297 1.00 16.97 ? 62  PRO B C   1 
ATOM   1597  O  O   . PRO B  1 89  ? 53.645  58.690  -16.957 1.00 16.25 ? 62  PRO B O   1 
ATOM   1598  C  CB  . PRO B  1 89  ? 50.406  57.622  -17.202 1.00 19.12 ? 62  PRO B CB  1 
ATOM   1599  C  CG  . PRO B  1 89  ? 50.953  56.533  -16.339 1.00 20.24 ? 62  PRO B CG  1 
ATOM   1600  C  CD  . PRO B  1 89  ? 51.949  55.766  -17.208 1.00 19.34 ? 62  PRO B CD  1 
ATOM   1601  N  N   . HIS B  1 90  ? 51.972  60.212  -16.999 1.00 17.46 ? 63  HIS B N   1 
ATOM   1602  C  CA  . HIS B  1 90  ? 52.718  61.167  -16.153 1.00 18.41 ? 63  HIS B CA  1 
ATOM   1603  C  C   . HIS B  1 90  ? 53.036  60.511  -14.826 1.00 19.10 ? 63  HIS B C   1 
ATOM   1604  O  O   . HIS B  1 90  ? 52.223  59.752  -14.289 1.00 17.18 ? 63  HIS B O   1 
ATOM   1605  C  CB  . HIS B  1 90  ? 51.928  62.456  -15.891 1.00 18.27 ? 63  HIS B CB  1 
ATOM   1606  C  CG  . HIS B  1 90  ? 51.681  63.221  -17.142 1.00 19.04 ? 63  HIS B CG  1 
ATOM   1607  N  ND1 . HIS B  1 90  ? 50.898  64.346  -17.193 1.00 17.88 ? 63  HIS B ND1 1 
ATOM   1608  C  CD2 . HIS B  1 90  ? 52.113  63.006  -18.414 1.00 19.84 ? 63  HIS B CD2 1 
ATOM   1609  C  CE1 . HIS B  1 90  ? 50.861  64.812  -18.430 1.00 18.69 ? 63  HIS B CE1 1 
ATOM   1610  N  NE2 . HIS B  1 90  ? 51.565  63.997  -19.201 1.00 20.13 ? 63  HIS B NE2 1 
ATOM   1611  N  N   . PHE B  1 91  ? 54.225  60.791  -14.319 1.00 15.58 ? 64  PHE B N   1 
ATOM   1612  C  CA  . PHE B  1 91  ? 54.612  60.237  -13.018 1.00 16.54 ? 64  PHE B CA  1 
ATOM   1613  C  C   . PHE B  1 91  ? 53.673  60.807  -11.937 1.00 16.14 ? 64  PHE B C   1 
ATOM   1614  O  O   . PHE B  1 91  ? 53.593  61.987  -11.773 1.00 14.98 ? 64  PHE B O   1 
ATOM   1615  C  CB  . PHE B  1 91  ? 56.064  60.627  -12.750 1.00 15.09 ? 64  PHE B CB  1 
ATOM   1616  C  CG  . PHE B  1 91  ? 56.586  60.154  -11.421 1.00 16.37 ? 64  PHE B CG  1 
ATOM   1617  C  CD1 . PHE B  1 91  ? 56.275  58.902  -10.935 1.00 16.80 ? 64  PHE B CD1 1 
ATOM   1618  C  CD2 . PHE B  1 91  ? 57.376  60.995  -10.668 1.00 17.27 ? 64  PHE B CD2 1 
ATOM   1619  C  CE1 . PHE B  1 91  ? 56.786  58.464  -9.683  1.00 17.78 ? 64  PHE B CE1 1 
ATOM   1620  C  CE2 . PHE B  1 91  ? 57.897  60.586  -9.424  1.00 21.15 ? 64  PHE B CE2 1 
ATOM   1621  C  CZ  . PHE B  1 91  ? 57.595  59.307  -8.948  1.00 18.04 ? 64  PHE B CZ  1 
ATOM   1622  N  N   . ASN B  1 92  ? 52.941  59.954  -11.227 1.00 16.22 ? 65  ASN B N   1 
ATOM   1623  C  CA  . ASN B  1 92  ? 51.804  60.438  -10.404 1.00 17.88 ? 65  ASN B CA  1 
ATOM   1624  C  C   . ASN B  1 92  ? 51.645  59.549  -9.156  1.00 18.70 ? 65  ASN B C   1 
ATOM   1625  O  O   . ASN B  1 92  ? 50.621  58.883  -8.994  1.00 20.19 ? 65  ASN B O   1 
ATOM   1626  C  CB  . ASN B  1 92  ? 50.549  60.456  -11.271 1.00 19.34 ? 65  ASN B CB  1 
ATOM   1627  C  CG  . ASN B  1 92  ? 49.289  60.957  -10.531 1.00 20.18 ? 65  ASN B CG  1 
ATOM   1628  O  OD1 . ASN B  1 92  ? 49.349  61.705  -9.541  1.00 19.78 ? 65  ASN B OD1 1 
ATOM   1629  N  ND2 . ASN B  1 92  ? 48.132  60.518  -11.029 1.00 21.84 ? 65  ASN B ND2 1 
ATOM   1630  N  N   . PRO B  1 93  ? 52.671  59.506  -8.310  1.00 20.01 ? 66  PRO B N   1 
ATOM   1631  C  CA  . PRO B  1 93  ? 52.598  58.516  -7.246  1.00 23.98 ? 66  PRO B CA  1 
ATOM   1632  C  C   . PRO B  1 93  ? 51.538  58.875  -6.167  1.00 27.28 ? 66  PRO B C   1 
ATOM   1633  O  O   . PRO B  1 93  ? 51.196  58.045  -5.345  1.00 25.59 ? 66  PRO B O   1 
ATOM   1634  C  CB  . PRO B  1 93  ? 53.985  58.586  -6.622  1.00 21.76 ? 66  PRO B CB  1 
ATOM   1635  C  CG  . PRO B  1 93  ? 54.459  59.996  -6.890  1.00 22.62 ? 66  PRO B CG  1 
ATOM   1636  C  CD  . PRO B  1 93  ? 53.938  60.260  -8.274  1.00 20.27 ? 66  PRO B CD  1 
ATOM   1637  N  N   . LEU B  1 94  ? 51.008  60.087  -6.213  1.00 28.34 ? 67  LEU B N   1 
ATOM   1638  C  CA  . LEU B  1 94  ? 49.960  60.483  -5.268  1.00 26.34 ? 67  LEU B CA  1 
ATOM   1639  C  C   . LEU B  1 94  ? 48.581  60.391  -5.878  1.00 26.81 ? 67  LEU B C   1 
ATOM   1640  O  O   . LEU B  1 94  ? 47.608  60.832  -5.255  1.00 28.35 ? 67  LEU B O   1 
ATOM   1641  C  CB  . LEU B  1 94  ? 50.236  61.883  -4.751  1.00 27.26 ? 67  LEU B CB  1 
ATOM   1642  C  CG  . LEU B  1 94  ? 51.488  61.917  -3.874  1.00 32.43 ? 67  LEU B CG  1 
ATOM   1643  C  CD1 . LEU B  1 94  ? 51.850  63.392  -3.641  1.00 33.99 ? 67  LEU B CD1 1 
ATOM   1644  C  CD2 . LEU B  1 94  ? 51.243  61.138  -2.573  1.00 36.39 ? 67  LEU B CD2 1 
ATOM   1645  N  N   . SER B  1 95  ? 48.480  59.841  -7.093  1.00 23.31 ? 68  SER B N   1 
ATOM   1646  C  CA  . SER B  1 95  ? 47.201  59.638  -7.793  1.00 25.35 ? 68  SER B CA  1 
ATOM   1647  C  C   . SER B  1 95  ? 46.325  60.880  -7.753  1.00 27.90 ? 68  SER B C   1 
ATOM   1648  O  O   . SER B  1 95  ? 45.144  60.813  -7.372  1.00 27.36 ? 68  SER B O   1 
ATOM   1649  C  CB  . SER B  1 95  ? 46.401  58.418  -7.235  1.00 27.32 ? 68  SER B CB  1 
ATOM   1650  O  OG  . SER B  1 95  ? 47.218  57.251  -7.345  1.00 33.62 ? 68  SER B OG  1 
ATOM   1651  N  N   . ARG B  1 96  ? 46.904  62.005  -8.147  1.00 22.81 ? 69  ARG B N   1 
ATOM   1652  C  CA  . ARG B  1 96  ? 46.176  63.242  -8.308  1.00 22.91 ? 69  ARG B CA  1 
ATOM   1653  C  C   . ARG B  1 96  ? 45.731  63.445  -9.739  1.00 22.13 ? 69  ARG B C   1 
ATOM   1654  O  O   . ARG B  1 96  ? 46.063  62.651  -10.626 1.00 24.30 ? 69  ARG B O   1 
ATOM   1655  C  CB  . ARG B  1 96  ? 47.068  64.404  -7.864  1.00 23.01 ? 69  ARG B CB  1 
ATOM   1656  C  CG  . ARG B  1 96  ? 47.576  64.217  -6.455  1.00 26.37 ? 69  ARG B CG  1 
ATOM   1657  C  CD  . ARG B  1 96  ? 46.569  64.588  -5.376  1.00 32.12 ? 69  ARG B CD  1 
ATOM   1658  N  NE  . ARG B  1 96  ? 47.260  64.528  -4.078  1.00 39.24 ? 69  ARG B NE  1 
ATOM   1659  C  CZ  . ARG B  1 96  ? 46.995  63.630  -3.110  1.00 40.52 ? 69  ARG B CZ  1 
ATOM   1660  N  NH1 . ARG B  1 96  ? 46.017  62.744  -3.271  1.00 37.59 ? 69  ARG B NH1 1 
ATOM   1661  N  NH2 . ARG B  1 96  ? 47.723  63.599  -1.978  1.00 36.69 ? 69  ARG B NH2 1 
ATOM   1662  N  N   . LYS B  1 97  ? 44.964  64.507  -9.974  1.00 20.53 ? 70  LYS B N   1 
ATOM   1663  C  CA  . LYS B  1 97  ? 44.609  64.914  -11.317 1.00 21.24 ? 70  LYS B CA  1 
ATOM   1664  C  C   . LYS B  1 97  ? 45.730  65.759  -11.892 1.00 18.88 ? 70  LYS B C   1 
ATOM   1665  O  O   . LYS B  1 97  ? 46.498  66.372  -11.115 1.00 17.57 ? 70  LYS B O   1 
ATOM   1666  C  CB  . LYS B  1 97  ? 43.344  65.812  -11.286 1.00 25.16 ? 70  LYS B CB  1 
ATOM   1667  C  CG  . LYS B  1 97  ? 42.102  65.108  -10.780 1.00 34.51 ? 70  LYS B CG  1 
ATOM   1668  C  CD  . LYS B  1 97  ? 41.372  64.459  -11.919 1.00 41.64 ? 70  LYS B CD  1 
ATOM   1669  C  CE  . LYS B  1 97  ? 41.371  62.934  -11.812 1.00 51.97 ? 70  LYS B CE  1 
ATOM   1670  N  NZ  . LYS B  1 97  ? 40.072  62.485  -11.210 1.00 55.71 ? 70  LYS B NZ  1 
ATOM   1671  N  N   . HIS B  1 98  ? 45.795  65.809  -13.233 1.00 18.24 ? 71  HIS B N   1 
ATOM   1672  C  CA  . HIS B  1 98  ? 46.763  66.631  -13.962 1.00 20.15 ? 71  HIS B CA  1 
ATOM   1673  C  C   . HIS B  1 98  ? 46.566  68.133  -13.663 1.00 20.40 ? 71  HIS B C   1 
ATOM   1674  O  O   . HIS B  1 98  ? 45.416  68.615  -13.596 1.00 18.61 ? 71  HIS B O   1 
ATOM   1675  C  CB  . HIS B  1 98  ? 46.634  66.376  -15.484 1.00 19.42 ? 71  HIS B CB  1 
ATOM   1676  C  CG  . HIS B  1 98  ? 47.586  67.206  -16.310 1.00 18.31 ? 71  HIS B CG  1 
ATOM   1677  N  ND1 . HIS B  1 98  ? 48.932  66.934  -16.393 1.00 18.68 ? 71  HIS B ND1 1 
ATOM   1678  C  CD2 . HIS B  1 98  ? 47.396  68.344  -17.019 1.00 16.39 ? 71  HIS B CD2 1 
ATOM   1679  C  CE1 . HIS B  1 98  ? 49.528  67.854  -17.132 1.00 15.71 ? 71  HIS B CE1 1 
ATOM   1680  N  NE2 . HIS B  1 98  ? 48.605  68.699  -17.549 1.00 16.84 ? 71  HIS B NE2 1 
ATOM   1681  N  N   . GLY B  1 99  ? 47.654  68.869  -13.454 1.00 16.83 ? 72  GLY B N   1 
ATOM   1682  C  CA  . GLY B  1 99  ? 47.564  70.325  -13.322 1.00 17.07 ? 72  GLY B CA  1 
ATOM   1683  C  C   . GLY B  1 99  ? 48.797  70.993  -13.846 1.00 18.99 ? 72  GLY B C   1 
ATOM   1684  O  O   . GLY B  1 99  ? 49.620  70.337  -14.530 1.00 16.24 ? 72  GLY B O   1 
ATOM   1685  N  N   . GLY B  1 100 ? 48.928  72.296  -13.599 1.00 16.82 ? 73  GLY B N   1 
ATOM   1686  C  CA  . GLY B  1 100 ? 50.150  72.956  -14.002 1.00 16.23 ? 73  GLY B CA  1 
ATOM   1687  C  C   . GLY B  1 100 ? 51.060  72.930  -12.794 1.00 17.10 ? 73  GLY B C   1 
ATOM   1688  O  O   . GLY B  1 100 ? 50.608  72.607  -11.684 1.00 17.32 ? 73  GLY B O   1 
ATOM   1689  N  N   . PRO B  1 101 ? 52.339  73.296  -12.987 1.00 16.99 ? 74  PRO B N   1 
ATOM   1690  C  CA  . PRO B  1 101 ? 53.314  73.118  -11.911 1.00 18.16 ? 74  PRO B CA  1 
ATOM   1691  C  C   . PRO B  1 101 ? 53.015  73.990  -10.678 1.00 20.53 ? 74  PRO B C   1 
ATOM   1692  O  O   . PRO B  1 101 ? 53.411  73.634  -9.579  1.00 18.78 ? 74  PRO B O   1 
ATOM   1693  C  CB  . PRO B  1 101 ? 54.649  73.560  -12.558 1.00 17.39 ? 74  PRO B CB  1 
ATOM   1694  C  CG  . PRO B  1 101 ? 54.277  74.347  -13.793 1.00 17.60 ? 74  PRO B CG  1 
ATOM   1695  C  CD  . PRO B  1 101 ? 52.953  73.770  -14.238 1.00 17.04 ? 74  PRO B CD  1 
ATOM   1696  N  N   . LYS B  1 102 ? 52.327  75.114  -10.870 1.00 19.07 ? 75  LYS B N   1 
ATOM   1697  C  CA  . LYS B  1 102 ? 51.951  75.983  -9.727  1.00 20.32 ? 75  LYS B CA  1 
ATOM   1698  C  C   . LYS B  1 102 ? 50.750  75.455  -8.921  1.00 21.28 ? 75  LYS B C   1 
ATOM   1699  O  O   . LYS B  1 102 ? 50.399  76.003  -7.857  1.00 22.42 ? 75  LYS B O   1 
ATOM   1700  C  CB  . LYS B  1 102 ? 51.627  77.391  -10.250 1.00 24.66 ? 75  LYS B CB  1 
ATOM   1701  C  CG  . LYS B  1 102 ? 52.822  78.064  -10.901 1.00 30.87 ? 75  LYS B CG  1 
ATOM   1702  C  CD  . LYS B  1 102 ? 52.345  79.168  -11.881 1.00 35.63 ? 75  LYS B CD  1 
ATOM   1703  C  CE  . LYS B  1 102 ? 51.751  80.370  -11.136 1.00 37.41 ? 75  LYS B CE  1 
ATOM   1704  N  NZ  . LYS B  1 102 ? 51.806  81.657  -11.916 1.00 36.04 ? 75  LYS B NZ  1 
ATOM   1705  N  N   . ASP B  1 103 ? 50.063  74.458  -9.427  1.00 18.67 ? 76  ASP B N   1 
ATOM   1706  C  CA  . ASP B  1 103 ? 48.872  73.910  -8.738  1.00 21.67 ? 76  ASP B CA  1 
ATOM   1707  C  C   . ASP B  1 103 ? 49.167  72.982  -7.596  1.00 23.62 ? 76  ASP B C   1 
ATOM   1708  O  O   . ASP B  1 103 ? 50.056  72.152  -7.681  1.00 22.91 ? 76  ASP B O   1 
ATOM   1709  C  CB  . ASP B  1 103 ? 48.028  73.138  -9.740  1.00 22.13 ? 76  ASP B CB  1 
ATOM   1710  C  CG  . ASP B  1 103 ? 47.372  74.039  -10.742 1.00 25.97 ? 76  ASP B CG  1 
ATOM   1711  O  OD1 . ASP B  1 103 ? 47.051  75.210  -10.362 1.00 27.14 ? 76  ASP B OD1 1 
ATOM   1712  O  OD2 . ASP B  1 103 ? 47.138  73.601  -11.901 1.00 25.46 ? 76  ASP B OD2 1 
ATOM   1713  N  N   . GLU B  1 104 ? 48.362  73.051  -6.546  1.00 26.33 ? 77  GLU B N   1 
ATOM   1714  C  CA  . GLU B  1 104 ? 48.431  72.029  -5.512  1.00 25.86 ? 77  GLU B CA  1 
ATOM   1715  C  C   . GLU B  1 104 ? 47.962  70.686  -6.043  1.00 25.58 ? 77  GLU B C   1 
ATOM   1716  O  O   . GLU B  1 104 ? 48.624  69.651  -5.774  1.00 25.11 ? 77  GLU B O   1 
ATOM   1717  C  CB  . GLU B  1 104 ? 47.642  72.417  -4.242  1.00 33.98 ? 77  GLU B CB  1 
ATOM   1718  C  CG  . GLU B  1 104 ? 47.754  71.338  -3.152  1.00 41.98 ? 77  GLU B CG  1 
ATOM   1719  C  CD  . GLU B  1 104 ? 46.853  71.586  -1.932  1.00 57.18 ? 77  GLU B CD  1 
ATOM   1720  O  OE1 . GLU B  1 104 ? 46.209  72.659  -1.852  1.00 59.60 ? 77  GLU B OE1 1 
ATOM   1721  O  OE2 . GLU B  1 104 ? 46.778  70.694  -1.045  1.00 62.27 ? 77  GLU B OE2 1 
ATOM   1722  N  N   . GLU B  1 105 ? 46.916  70.682  -6.870  1.00 21.07 ? 78  GLU B N   1 
ATOM   1723  C  CA  . GLU B  1 105 ? 46.470  69.418  -7.487  1.00 22.20 ? 78  GLU B CA  1 
ATOM   1724  C  C   . GLU B  1 105 ? 47.202  69.234  -8.815  1.00 17.77 ? 78  GLU B C   1 
ATOM   1725  O  O   . GLU B  1 105 ? 46.909  69.921  -9.777  1.00 16.83 ? 78  GLU B O   1 
ATOM   1726  C  CB  . GLU B  1 105 ? 44.954  69.431  -7.749  1.00 21.08 ? 78  GLU B CB  1 
ATOM   1727  C  CG  . GLU B  1 105 ? 44.415  68.136  -8.339  1.00 26.18 ? 78  GLU B CG  1 
ATOM   1728  C  CD  . GLU B  1 105 ? 44.204  67.023  -7.334  1.00 28.95 ? 78  GLU B CD  1 
ATOM   1729  O  OE1 . GLU B  1 105 ? 44.271  67.297  -6.107  1.00 35.63 ? 78  GLU B OE1 1 
ATOM   1730  O  OE2 . GLU B  1 105 ? 43.899  65.879  -7.749  1.00 29.01 ? 78  GLU B OE2 1 
ATOM   1731  N  N   . ARG B  1 106 ? 48.185  68.355  -8.836  1.00 17.55 ? 79  ARG B N   1 
ATOM   1732  C  CA  . ARG B  1 106 ? 49.006  68.145  -10.043 1.00 15.51 ? 79  ARG B CA  1 
ATOM   1733  C  C   . ARG B  1 106 ? 49.665  66.781  -9.874  1.00 17.32 ? 79  ARG B C   1 
ATOM   1734  O  O   . ARG B  1 106 ? 49.775  66.226  -8.755  1.00 18.62 ? 79  ARG B O   1 
ATOM   1735  C  CB  . ARG B  1 106 ? 50.136  69.214  -10.217 1.00 16.77 ? 79  ARG B CB  1 
ATOM   1736  C  CG  . ARG B  1 106 ? 51.071  69.328  -8.993  1.00 16.70 ? 79  ARG B CG  1 
ATOM   1737  C  CD  . ARG B  1 106 ? 52.260  70.229  -9.261  1.00 17.45 ? 79  ARG B CD  1 
ATOM   1738  N  NE  . ARG B  1 106 ? 53.369  69.454  -9.891  1.00 16.34 ? 79  ARG B NE  1 
ATOM   1739  C  CZ  . ARG B  1 106 ? 54.621  69.901  -9.999  1.00 17.03 ? 79  ARG B CZ  1 
ATOM   1740  N  NH1 . ARG B  1 106 ? 54.912  71.159  -9.642  1.00 15.64 ? 79  ARG B NH1 1 
ATOM   1741  N  NH2 . ARG B  1 106 ? 55.600  69.104  -10.508 1.00 14.84 ? 79  ARG B NH2 1 
ATOM   1742  N  N   . HIS B  1 107 ? 50.126  66.258  -10.975 1.00 14.57 ? 80  HIS B N   1 
ATOM   1743  C  CA  . HIS B  1 107 ? 51.018  65.089  -10.897 1.00 15.35 ? 80  HIS B CA  1 
ATOM   1744  C  C   . HIS B  1 107 ? 52.395  65.564  -10.465 1.00 14.07 ? 80  HIS B C   1 
ATOM   1745  O  O   . HIS B  1 107 ? 52.800  66.682  -10.790 1.00 13.71 ? 80  HIS B O   1 
ATOM   1746  C  CB  . HIS B  1 107 ? 51.103  64.424  -12.278 1.00 14.29 ? 80  HIS B CB  1 
ATOM   1747  C  CG  . HIS B  1 107 ? 49.766  63.976  -12.843 1.00 16.22 ? 80  HIS B CG  1 
ATOM   1748  N  ND1 . HIS B  1 107 ? 49.500  63.971  -14.187 1.00 15.97 ? 80  HIS B ND1 1 
ATOM   1749  C  CD2 . HIS B  1 107 ? 48.640  63.502  -12.242 1.00 17.47 ? 80  HIS B CD2 1 
ATOM   1750  C  CE1 . HIS B  1 107 ? 48.285  63.479  -14.411 1.00 18.29 ? 80  HIS B CE1 1 
ATOM   1751  N  NE2 . HIS B  1 107 ? 47.750  63.173  -13.241 1.00 16.69 ? 80  HIS B NE2 1 
ATOM   1752  N  N   . VAL B  1 108 ? 53.163  64.703  -9.792  1.00 14.83 ? 81  VAL B N   1 
ATOM   1753  C  CA  . VAL B  1 108 ? 54.597  65.042  -9.545  1.00 14.19 ? 81  VAL B CA  1 
ATOM   1754  C  C   . VAL B  1 108 ? 55.306  65.411  -10.872 1.00 13.77 ? 81  VAL B C   1 
ATOM   1755  O  O   . VAL B  1 108 ? 56.068  66.384  -10.921 1.00 16.12 ? 81  VAL B O   1 
ATOM   1756  C  CB  . VAL B  1 108 ? 55.347  63.855  -8.873  1.00 15.96 ? 81  VAL B CB  1 
ATOM   1757  C  CG1 . VAL B  1 108 ? 56.853  64.194  -8.835  1.00 15.45 ? 81  VAL B CG1 1 
ATOM   1758  C  CG2 . VAL B  1 108 ? 54.846  63.701  -7.410  1.00 15.42 ? 81  VAL B CG2 1 
ATOM   1759  N  N   . GLY B  1 109 ? 54.988  64.703  -11.943 1.00 14.44 ? 82  GLY B N   1 
ATOM   1760  C  CA  . GLY B  1 109 ? 55.651  64.920  -13.269 1.00 14.68 ? 82  GLY B CA  1 
ATOM   1761  C  C   . GLY B  1 109 ? 55.177  66.128  -14.062 1.00 15.37 ? 82  GLY B C   1 
ATOM   1762  O  O   . GLY B  1 109 ? 55.626  66.344  -15.187 1.00 14.67 ? 82  GLY B O   1 
ATOM   1763  N  N   . ASP B  1 110 ? 54.276  66.945  -13.485 1.00 15.27 ? 83  ASP B N   1 
ATOM   1764  C  CA  . ASP B  1 110 ? 53.660  68.053  -14.245 1.00 14.06 ? 83  ASP B CA  1 
ATOM   1765  C  C   . ASP B  1 110 ? 54.546  69.296  -14.229 1.00 16.12 ? 83  ASP B C   1 
ATOM   1766  O  O   . ASP B  1 110 ? 54.374  70.192  -13.385 1.00 17.18 ? 83  ASP B O   1 
ATOM   1767  C  CB  . ASP B  1 110 ? 52.256  68.386  -13.665 1.00 15.46 ? 83  ASP B CB  1 
ATOM   1768  C  CG  . ASP B  1 110 ? 51.237  67.355  -14.058 1.00 15.99 ? 83  ASP B CG  1 
ATOM   1769  O  OD1 . ASP B  1 110 ? 51.542  66.505  -14.958 1.00 16.91 ? 83  ASP B OD1 1 
ATOM   1770  O  OD2 . ASP B  1 110 ? 50.134  67.338  -13.479 1.00 16.18 ? 83  ASP B OD2 1 
ATOM   1771  N  N   . LEU B  1 111 ? 55.472  69.406  -15.197 1.00 14.59 ? 84  LEU B N   1 
ATOM   1772  C  CA  . LEU B  1 111 ? 56.309  70.548  -15.202 1.00 15.35 ? 84  LEU B CA  1 
ATOM   1773  C  C   . LEU B  1 111 ? 55.752  71.654  -16.141 1.00 15.74 ? 84  LEU B C   1 
ATOM   1774  O  O   . LEU B  1 111 ? 56.461  72.623  -16.398 1.00 18.47 ? 84  LEU B O   1 
ATOM   1775  C  CB  . LEU B  1 111 ? 57.757  70.172  -15.642 1.00 14.82 ? 84  LEU B CB  1 
ATOM   1776  C  CG  . LEU B  1 111 ? 58.400  69.122  -14.714 1.00 17.46 ? 84  LEU B CG  1 
ATOM   1777  C  CD1 . LEU B  1 111 ? 59.796  68.808  -15.214 1.00 17.52 ? 84  LEU B CD1 1 
ATOM   1778  C  CD2 . LEU B  1 111 ? 58.483  69.752  -13.326 1.00 20.13 ? 84  LEU B CD2 1 
ATOM   1779  N  N   . GLY B  1 112 ? 54.556  71.502  -16.717 1.00 15.24 ? 85  GLY B N   1 
ATOM   1780  C  CA  . GLY B  1 112 ? 53.938  72.619  -17.448 1.00 14.45 ? 85  GLY B CA  1 
ATOM   1781  C  C   . GLY B  1 112 ? 54.406  72.627  -18.897 1.00 15.50 ? 85  GLY B C   1 
ATOM   1782  O  O   . GLY B  1 112 ? 54.555  71.561  -19.504 1.00 15.40 ? 85  GLY B O   1 
ATOM   1783  N  N   . ASN B  1 113 ? 54.657  73.813  -19.441 1.00 14.15 ? 86  ASN B N   1 
ATOM   1784  C  CA  . ASN B  1 113 ? 55.114  73.934  -20.798 1.00 15.42 ? 86  ASN B CA  1 
ATOM   1785  C  C   . ASN B  1 113 ? 56.516  74.503  -20.869 1.00 14.86 ? 86  ASN B C   1 
ATOM   1786  O  O   . ASN B  1 113 ? 56.988  75.146  -19.900 1.00 15.41 ? 86  ASN B O   1 
ATOM   1787  C  CB  . ASN B  1 113 ? 54.219  74.945  -21.543 1.00 15.41 ? 86  ASN B CB  1 
ATOM   1788  C  CG  . ASN B  1 113 ? 52.831  74.362  -21.804 1.00 17.38 ? 86  ASN B CG  1 
ATOM   1789  O  OD1 . ASN B  1 113 ? 52.731  73.339  -22.482 1.00 16.66 ? 86  ASN B OD1 1 
ATOM   1790  N  ND2 . ASN B  1 113 ? 51.768  74.979  -21.219 1.00 15.64 ? 86  ASN B ND2 1 
ATOM   1791  N  N   . VAL B  1 114 ? 57.139  74.284  -22.023 1.00 14.53 ? 87  VAL B N   1 
ATOM   1792  C  CA  . VAL B  1 114 ? 58.359  75.016  -22.393 1.00 15.82 ? 87  VAL B CA  1 
ATOM   1793  C  C   . VAL B  1 114 ? 58.065  75.710  -23.707 1.00 16.27 ? 87  VAL B C   1 
ATOM   1794  O  O   . VAL B  1 114 ? 57.279  75.215  -24.505 1.00 16.67 ? 87  VAL B O   1 
ATOM   1795  C  CB  . VAL B  1 114 ? 59.600  74.099  -22.515 1.00 15.78 ? 87  VAL B CB  1 
ATOM   1796  C  CG1 . VAL B  1 114 ? 59.923  73.476  -21.122 1.00 16.16 ? 87  VAL B CG1 1 
ATOM   1797  C  CG2 . VAL B  1 114 ? 59.358  72.923  -23.486 1.00 15.63 ? 87  VAL B CG2 1 
ATOM   1798  N  N   . THR B  1 115 ? 58.779  76.795  -23.971 1.00 15.55 ? 88  THR B N   1 
ATOM   1799  C  CA  . THR B  1 115 ? 58.447  77.618  -25.139 1.00 17.20 ? 88  THR B CA  1 
ATOM   1800  C  C   . THR B  1 115 ? 59.630  77.561  -26.104 1.00 18.00 ? 88  THR B C   1 
ATOM   1801  O  O   . THR B  1 115 ? 60.744  77.883  -25.712 1.00 16.47 ? 88  THR B O   1 
ATOM   1802  C  CB  . THR B  1 115 ? 58.238  79.101  -24.710 1.00 17.06 ? 88  THR B CB  1 
ATOM   1803  O  OG1 . THR B  1 115 ? 57.072  79.151  -23.877 1.00 16.38 ? 88  THR B OG1 1 
ATOM   1804  C  CG2 . THR B  1 115 ? 58.019  80.080  -25.933 1.00 19.97 ? 88  THR B CG2 1 
ATOM   1805  N  N   . ALA B  1 116 ? 59.351  77.195  -27.359 1.00 16.65 ? 89  ALA B N   1 
ATOM   1806  C  CA  . ALA B  1 116 ? 60.333  77.269  -28.422 1.00 17.93 ? 89  ALA B CA  1 
ATOM   1807  C  C   . ALA B  1 116 ? 60.189  78.624  -29.144 1.00 19.04 ? 89  ALA B C   1 
ATOM   1808  O  O   . ALA B  1 116 ? 59.094  79.096  -29.383 1.00 18.73 ? 89  ALA B O   1 
ATOM   1809  C  CB  . ALA B  1 116 ? 60.128  76.128  -29.432 1.00 17.43 ? 89  ALA B CB  1 
ATOM   1810  N  N   . ASP B  1 117 ? 61.320  79.211  -29.457 1.00 20.47 ? 90  ASP B N   1 
ATOM   1811  C  CA  . ASP B  1 117 ? 61.401  80.493  -30.176 1.00 23.33 ? 90  ASP B CA  1 
ATOM   1812  C  C   . ASP B  1 117 ? 61.223  80.255  -31.694 1.00 23.47 ? 90  ASP B C   1 
ATOM   1813  O  O   . ASP B  1 117 ? 60.953  79.129  -32.164 1.00 18.88 ? 90  ASP B O   1 
ATOM   1814  C  CB  . ASP B  1 117 ? 62.735  81.186  -29.827 1.00 24.12 ? 90  ASP B CB  1 
ATOM   1815  C  CG  . ASP B  1 117 ? 63.981  80.478  -30.425 1.00 27.71 ? 90  ASP B CG  1 
ATOM   1816  O  OD1 . ASP B  1 117 ? 63.866  79.615  -31.335 1.00 24.56 ? 90  ASP B OD1 1 
ATOM   1817  O  OD2 . ASP B  1 117 ? 65.094  80.797  -29.934 1.00 25.81 ? 90  ASP B OD2 1 
ATOM   1818  N  N   . LYS B  1 118 ? 61.346  81.321  -32.482 1.00 24.15 ? 91  LYS B N   1 
ATOM   1819  C  CA  . LYS B  1 118 ? 61.000  81.223  -33.902 1.00 28.99 ? 91  LYS B CA  1 
ATOM   1820  C  C   . LYS B  1 118 ? 61.991  80.346  -34.633 1.00 26.31 ? 91  LYS B C   1 
ATOM   1821  O  O   . LYS B  1 118 ? 61.668  79.847  -35.703 1.00 28.80 ? 91  LYS B O   1 
ATOM   1822  C  CB  . LYS B  1 118 ? 60.919  82.635  -34.560 1.00 29.34 ? 91  LYS B CB  1 
ATOM   1823  C  CG  . LYS B  1 118 ? 62.284  83.302  -34.653 1.00 38.40 ? 91  LYS B CG  1 
ATOM   1824  C  CD  . LYS B  1 118 ? 62.152  84.823  -34.462 1.00 49.76 ? 91  LYS B CD  1 
ATOM   1825  C  CE  . LYS B  1 118 ? 63.517  85.473  -34.564 1.00 52.07 ? 91  LYS B CE  1 
ATOM   1826  N  NZ  . LYS B  1 118 ? 64.012  85.165  -35.939 1.00 57.45 ? 91  LYS B NZ  1 
ATOM   1827  N  N   . ASP B  1 119 ? 63.173  80.103  -34.049 1.00 23.99 ? 92  ASP B N   1 
ATOM   1828  C  CA  . ASP B  1 119 ? 64.123  79.123  -34.637 1.00 25.50 ? 92  ASP B CA  1 
ATOM   1829  C  C   . ASP B  1 119 ? 63.928  77.691  -34.155 1.00 27.07 ? 92  ASP B C   1 
ATOM   1830  O  O   . ASP B  1 119 ? 64.736  76.812  -34.490 1.00 25.46 ? 92  ASP B O   1 
ATOM   1831  C  CB  . ASP B  1 119 ? 65.580  79.527  -34.323 1.00 29.12 ? 92  ASP B CB  1 
ATOM   1832  C  CG  . ASP B  1 119 ? 65.904  80.941  -34.867 1.00 34.84 ? 92  ASP B CG  1 
ATOM   1833  O  OD1 . ASP B  1 119 ? 65.389  81.297  -35.942 1.00 35.83 ? 92  ASP B OD1 1 
ATOM   1834  O  OD2 . ASP B  1 119 ? 66.555  81.710  -34.167 1.00 37.25 ? 92  ASP B OD2 1 
ATOM   1835  N  N   . GLY B  1 120 ? 62.872  77.441  -33.366 1.00 23.77 ? 93  GLY B N   1 
ATOM   1836  C  CA  . GLY B  1 120 ? 62.565  76.050  -33.007 1.00 19.00 ? 93  GLY B CA  1 
ATOM   1837  C  C   . GLY B  1 120 ? 63.324  75.604  -31.733 1.00 18.39 ? 93  GLY B C   1 
ATOM   1838  O  O   . GLY B  1 120 ? 63.331  74.400  -31.399 1.00 17.91 ? 93  GLY B O   1 
ATOM   1839  N  N   . VAL B  1 121 ? 63.891  76.577  -31.002 1.00 17.75 ? 94  VAL B N   1 
ATOM   1840  C  CA  . VAL B  1 121 ? 64.743  76.326  -29.831 1.00 18.58 ? 94  VAL B CA  1 
ATOM   1841  C  C   . VAL B  1 121 ? 64.039  76.686  -28.515 1.00 17.99 ? 94  VAL B C   1 
ATOM   1842  O  O   . VAL B  1 121 ? 63.585  77.818  -28.358 1.00 19.85 ? 94  VAL B O   1 
ATOM   1843  C  CB  . VAL B  1 121 ? 66.070  77.092  -29.899 1.00 19.64 ? 94  VAL B CB  1 
ATOM   1844  C  CG1 . VAL B  1 121 ? 66.883  76.873  -28.620 1.00 19.86 ? 94  VAL B CG1 1 
ATOM   1845  C  CG2 . VAL B  1 121 ? 66.875  76.581  -31.090 1.00 21.65 ? 94  VAL B CG2 1 
ATOM   1846  N  N   . ALA B  1 122 ? 63.961  75.714  -27.586 1.00 16.70 ? 95  ALA B N   1 
ATOM   1847  C  CA  . ALA B  1 122 ? 63.452  75.975  -26.225 1.00 17.06 ? 95  ALA B CA  1 
ATOM   1848  C  C   . ALA B  1 122 ? 64.659  76.043  -25.302 1.00 17.30 ? 95  ALA B C   1 
ATOM   1849  O  O   . ALA B  1 122 ? 65.317  75.014  -25.076 1.00 18.58 ? 95  ALA B O   1 
ATOM   1850  C  CB  . ALA B  1 122 ? 62.473  74.867  -25.769 1.00 17.96 ? 95  ALA B CB  1 
ATOM   1851  N  N   . ASP B  1 123 ? 64.950  77.237  -24.763 1.00 18.04 ? 96  ASP B N   1 
ATOM   1852  C  CA  . ASP B  1 123 ? 65.996  77.399  -23.731 1.00 19.55 ? 96  ASP B CA  1 
ATOM   1853  C  C   . ASP B  1 123 ? 65.307  77.245  -22.383 1.00 17.98 ? 96  ASP B C   1 
ATOM   1854  O  O   . ASP B  1 123 ? 64.865  78.218  -21.762 1.00 18.19 ? 96  ASP B O   1 
ATOM   1855  C  CB  . ASP B  1 123 ? 66.686  78.758  -23.873 1.00 21.36 ? 96  ASP B CB  1 
ATOM   1856  C  CG  . ASP B  1 123 ? 67.614  78.806  -25.132 1.00 26.71 ? 96  ASP B CG  1 
ATOM   1857  O  OD1 . ASP B  1 123 ? 67.459  79.743  -25.928 1.00 30.39 ? 96  ASP B OD1 1 
ATOM   1858  O  OD2 . ASP B  1 123 ? 68.419  77.850  -25.343 1.00 29.41 ? 96  ASP B OD2 1 
ATOM   1859  N  N   . VAL B  1 124 ? 65.182  75.998  -21.964 1.00 15.82 ? 97  VAL B N   1 
ATOM   1860  C  CA  . VAL B  1 124 ? 64.365  75.647  -20.814 1.00 15.27 ? 97  VAL B CA  1 
ATOM   1861  C  C   . VAL B  1 124 ? 64.986  76.222  -19.534 1.00 16.19 ? 97  VAL B C   1 
ATOM   1862  O  O   . VAL B  1 124 ? 66.214  76.150  -19.297 1.00 15.59 ? 97  VAL B O   1 
ATOM   1863  C  CB  . VAL B  1 124 ? 64.277  74.104  -20.697 1.00 15.55 ? 97  VAL B CB  1 
ATOM   1864  C  CG1 . VAL B  1 124 ? 63.600  73.672  -19.392 1.00 15.35 ? 97  VAL B CG1 1 
ATOM   1865  C  CG2 . VAL B  1 124 ? 63.588  73.538  -21.942 1.00 16.23 ? 97  VAL B CG2 1 
ATOM   1866  N  N   . SER B  1 125 ? 64.142  76.762  -18.674 1.00 15.61 ? 98  SER B N   1 
ATOM   1867  C  CA  . SER B  1 125 ? 64.633  77.199  -17.371 1.00 18.06 ? 98  SER B CA  1 
ATOM   1868  C  C   . SER B  1 125 ? 63.441  77.115  -16.442 1.00 19.87 ? 98  SER B C   1 
ATOM   1869  O  O   . SER B  1 125 ? 62.533  77.967  -16.530 1.00 22.39 ? 98  SER B O   1 
ATOM   1870  C  CB  . SER B  1 125 ? 65.143  78.671  -17.461 1.00 21.34 ? 98  SER B CB  1 
ATOM   1871  O  OG  . SER B  1 125 ? 65.606  79.056  -16.173 1.00 25.59 ? 98  SER B OG  1 
ATOM   1872  N  N   . ILE B  1 126 ? 63.376  76.071  -15.619 1.00 18.12 ? 99  ILE B N   1 
ATOM   1873  C  CA  . ILE B  1 126 ? 62.264  75.862  -14.701 1.00 17.92 ? 99  ILE B CA  1 
ATOM   1874  C  C   . ILE B  1 126 ? 62.881  75.616  -13.309 1.00 19.85 ? 99  ILE B C   1 
ATOM   1875  O  O   . ILE B  1 126 ? 64.022  75.095  -13.218 1.00 17.69 ? 99  ILE B O   1 
ATOM   1876  C  CB  . ILE B  1 126 ? 61.484  74.598  -15.210 1.00 17.33 ? 99  ILE B CB  1 
ATOM   1877  C  CG1 . ILE B  1 126 ? 60.676  74.988  -16.453 1.00 18.48 ? 99  ILE B CG1 1 
ATOM   1878  C  CG2 . ILE B  1 126 ? 60.562  74.028  -14.168 1.00 19.75 ? 99  ILE B CG2 1 
ATOM   1879  C  CD1 . ILE B  1 126 ? 60.066  73.749  -17.149 1.00 16.31 ? 99  ILE B CD1 1 
ATOM   1880  N  N   . GLU B  1 127 ? 62.187  76.026  -12.246 1.00 17.28 ? 100 GLU B N   1 
ATOM   1881  C  CA  . GLU B  1 127 ? 62.496  75.600  -10.908 1.00 16.84 ? 100 GLU B CA  1 
ATOM   1882  C  C   . GLU B  1 127 ? 61.250  75.009  -10.318 1.00 19.81 ? 100 GLU B C   1 
ATOM   1883  O  O   . GLU B  1 127 ? 60.151  75.608  -10.425 1.00 17.53 ? 100 GLU B O   1 
ATOM   1884  C  CB  . GLU B  1 127 ? 62.949  76.793  -10.077 1.00 21.98 ? 100 GLU B CB  1 
ATOM   1885  C  CG  . GLU B  1 127 ? 63.294  76.392  -8.655  1.00 27.64 ? 100 GLU B CG  1 
ATOM   1886  C  CD  . GLU B  1 127 ? 63.953  77.538  -7.864  1.00 36.65 ? 100 GLU B CD  1 
ATOM   1887  O  OE1 . GLU B  1 127 ? 63.902  78.700  -8.282  1.00 41.01 ? 100 GLU B OE1 1 
ATOM   1888  O  OE2 . GLU B  1 127 ? 64.540  77.265  -6.815  1.00 39.61 ? 100 GLU B OE2 1 
ATOM   1889  N  N   . ASP B  1 128 ? 61.370  73.819  -9.742  1.00 17.79 ? 101 ASP B N   1 
ATOM   1890  C  CA  . ASP B  1 128 ? 60.187  73.082  -9.287  1.00 20.11 ? 101 ASP B CA  1 
ATOM   1891  C  C   . ASP B  1 128 ? 60.422  72.446  -7.905  1.00 21.25 ? 101 ASP B C   1 
ATOM   1892  O  O   . ASP B  1 128 ? 61.471  71.831  -7.666  1.00 20.67 ? 101 ASP B O   1 
ATOM   1893  C  CB  . ASP B  1 128 ? 59.782  72.002  -10.310 1.00 20.83 ? 101 ASP B CB  1 
ATOM   1894  C  CG  . ASP B  1 128 ? 58.369  71.439  -10.007 1.00 22.83 ? 101 ASP B CG  1 
ATOM   1895  O  OD1 . ASP B  1 128 ? 57.361  72.153  -10.301 1.00 23.32 ? 101 ASP B OD1 1 
ATOM   1896  O  OD2 . ASP B  1 128 ? 58.255  70.334  -9.429  1.00 19.92 ? 101 ASP B OD2 1 
ATOM   1897  N  N   A SER B  1 129 ? 59.429  72.541  -7.014  0.50 21.38 ? 102 SER B N   1 
ATOM   1898  N  N   B SER B  1 129 ? 59.440  72.529  -7.007  0.50 21.09 ? 102 SER B N   1 
ATOM   1899  C  CA  A SER B  1 129 ? 59.600  72.026  -5.667  0.50 21.76 ? 102 SER B CA  1 
ATOM   1900  C  CA  B SER B  1 129 ? 59.653  72.005  -5.673  0.50 21.22 ? 102 SER B CA  1 
ATOM   1901  C  C   A SER B  1 129 ? 58.905  70.723  -5.429  0.50 20.95 ? 102 SER B C   1 
ATOM   1902  C  C   B SER B  1 129 ? 58.889  70.736  -5.421  0.50 20.70 ? 102 SER B C   1 
ATOM   1903  O  O   A SER B  1 129 ? 58.932  70.218  -4.328  0.50 21.93 ? 102 SER B O   1 
ATOM   1904  O  O   B SER B  1 129 ? 58.846  70.272  -4.301  0.50 21.69 ? 102 SER B O   1 
ATOM   1905  C  CB  A SER B  1 129 ? 59.093  73.034  -4.630  0.50 26.18 ? 102 SER B CB  1 
ATOM   1906  C  CB  B SER B  1 129 ? 59.231  73.041  -4.634  0.50 25.40 ? 102 SER B CB  1 
ATOM   1907  O  OG  A SER B  1 129 ? 59.970  74.130  -4.551  0.50 27.25 ? 102 SER B OG  1 
ATOM   1908  O  OG  B SER B  1 129 ? 57.887  73.404  -4.873  0.50 24.91 ? 102 SER B OG  1 
ATOM   1909  N  N   . VAL B  1 130 ? 58.261  70.170  -6.439  1.00 17.78 ? 103 VAL B N   1 
ATOM   1910  C  CA  . VAL B  1 130 ? 57.559  68.918  -6.237  1.00 17.11 ? 103 VAL B CA  1 
ATOM   1911  C  C   . VAL B  1 130 ? 58.397  67.708  -6.748  1.00 17.84 ? 103 VAL B C   1 
ATOM   1912  O  O   . VAL B  1 130 ? 58.464  66.651  -6.120  1.00 16.67 ? 103 VAL B O   1 
ATOM   1913  C  CB  . VAL B  1 130 ? 56.161  69.007  -6.927  1.00 16.39 ? 103 VAL B CB  1 
ATOM   1914  C  CG1 . VAL B  1 130 ? 55.456  67.679  -6.864  1.00 18.58 ? 103 VAL B CG1 1 
ATOM   1915  C  CG2 . VAL B  1 130 ? 55.250  70.066  -6.212  1.00 18.28 ? 103 VAL B CG2 1 
ATOM   1916  N  N   . ILE B  1 131 ? 58.990  67.834  -7.929  1.00 16.80 ? 104 ILE B N   1 
ATOM   1917  C  CA  . ILE B  1 131 ? 59.956  66.793  -8.338  1.00 14.97 ? 104 ILE B CA  1 
ATOM   1918  C  C   . ILE B  1 131 ? 61.151  66.830  -7.359  1.00 15.47 ? 104 ILE B C   1 
ATOM   1919  O  O   . ILE B  1 131 ? 61.438  67.859  -6.707  1.00 15.75 ? 104 ILE B O   1 
ATOM   1920  C  CB  . ILE B  1 131 ? 60.438  67.003  -9.808  1.00 15.10 ? 104 ILE B CB  1 
ATOM   1921  C  CG1 . ILE B  1 131 ? 61.104  68.373  -9.992  1.00 13.89 ? 104 ILE B CG1 1 
ATOM   1922  C  CG2 . ILE B  1 131 ? 59.283  66.793  -10.789 1.00 15.87 ? 104 ILE B CG2 1 
ATOM   1923  C  CD1 . ILE B  1 131 ? 61.998  68.456  -11.260 1.00 14.04 ? 104 ILE B CD1 1 
ATOM   1924  N  N   . SER B  1 132 ? 61.937  65.749  -7.336  1.00 14.89 ? 105 SER B N   1 
ATOM   1925  C  CA  . SER B  1 132 ? 63.116  65.685  -6.475  1.00 15.07 ? 105 SER B CA  1 
ATOM   1926  C  C   . SER B  1 132 ? 64.115  64.738  -7.161  1.00 15.46 ? 105 SER B C   1 
ATOM   1927  O  O   . SER B  1 132 ? 63.750  63.947  -8.037  1.00 14.90 ? 105 SER B O   1 
ATOM   1928  C  CB  . SER B  1 132 ? 62.742  65.024  -5.115  1.00 16.77 ? 105 SER B CB  1 
ATOM   1929  O  OG  . SER B  1 132 ? 63.860  65.204  -4.172  1.00 16.57 ? 105 SER B OG  1 
ATOM   1930  N  N   . LEU B  1 133 ? 65.359  64.842  -6.741  1.00 15.94 ? 106 LEU B N   1 
ATOM   1931  C  CA  . LEU B  1 133 ? 66.372  63.827  -7.136  1.00 17.99 ? 106 LEU B CA  1 
ATOM   1932  C  C   . LEU B  1 133 ? 66.595  62.807  -6.045  1.00 21.70 ? 106 LEU B C   1 
ATOM   1933  O  O   . LEU B  1 133 ? 67.540  62.009  -6.134  1.00 21.83 ? 106 LEU B O   1 
ATOM   1934  C  CB  . LEU B  1 133 ? 67.701  64.564  -7.479  1.00 17.61 ? 106 LEU B CB  1 
ATOM   1935  C  CG  . LEU B  1 133 ? 67.572  65.595  -8.600  1.00 17.73 ? 106 LEU B CG  1 
ATOM   1936  C  CD1 . LEU B  1 133 ? 68.932  66.311  -8.976  1.00 17.98 ? 106 LEU B CD1 1 
ATOM   1937  C  CD2 . LEU B  1 133 ? 66.929  64.977  -9.845  1.00 17.86 ? 106 LEU B CD2 1 
ATOM   1938  N  N   . SER B  1 134 ? 65.757  62.798  -5.018  1.00 20.72 ? 107 SER B N   1 
ATOM   1939  C  CA  . SER B  1 134 ? 65.750  61.677  -4.058  1.00 25.35 ? 107 SER B CA  1 
ATOM   1940  C  C   . SER B  1 134 ? 64.393  61.502  -3.429  1.00 24.93 ? 107 SER B C   1 
ATOM   1941  O  O   . SER B  1 134 ? 63.487  62.330  -3.615  1.00 21.97 ? 107 SER B O   1 
ATOM   1942  C  CB  . SER B  1 134 ? 66.757  61.909  -2.915  1.00 27.18 ? 107 SER B CB  1 
ATOM   1943  O  OG  . SER B  1 134 ? 66.535  63.170  -2.351  1.00 33.99 ? 107 SER B OG  1 
ATOM   1944  N  N   . GLY B  1 135 ? 64.247  60.418  -2.690  1.00 23.25 ? 108 GLY B N   1 
ATOM   1945  C  CA  . GLY B  1 135 ? 62.991  60.132  -2.007  1.00 26.44 ? 108 GLY B CA  1 
ATOM   1946  C  C   . GLY B  1 135 ? 61.853  59.662  -2.893  1.00 24.97 ? 108 GLY B C   1 
ATOM   1947  O  O   . GLY B  1 135 ? 62.054  59.216  -4.027  1.00 24.65 ? 108 GLY B O   1 
ATOM   1948  N  N   . ASP B  1 136 ? 60.633  59.824  -2.392  1.00 23.86 ? 109 ASP B N   1 
ATOM   1949  C  CA  . ASP B  1 136 ? 59.441  59.283  -3.069  1.00 25.63 ? 109 ASP B CA  1 
ATOM   1950  C  C   . ASP B  1 136 ? 59.168  59.962  -4.395  1.00 20.09 ? 109 ASP B C   1 
ATOM   1951  O  O   . ASP B  1 136 ? 58.514  59.365  -5.262  1.00 21.79 ? 109 ASP B O   1 
ATOM   1952  C  CB  . ASP B  1 136 ? 58.183  59.594  -2.237  1.00 29.38 ? 109 ASP B CB  1 
ATOM   1953  C  CG  . ASP B  1 136 ? 58.039  58.668  -1.043  1.00 36.24 ? 109 ASP B CG  1 
ATOM   1954  O  OD1 . ASP B  1 136 ? 57.262  59.022  -0.144  1.00 38.28 ? 109 ASP B OD1 1 
ATOM   1955  O  OD2 . ASP B  1 136 ? 58.686  57.600  -1.044  1.00 40.96 ? 109 ASP B OD2 1 
ATOM   1956  N  N   . HIS B  1 137 ? 59.509  61.240  -4.466  1.00 17.89 ? 110 HIS B N   1 
ATOM   1957  C  CA  . HIS B  1 137 ? 59.281  61.992  -5.690  1.00 20.18 ? 110 HIS B CA  1 
ATOM   1958  C  C   . HIS B  1 137 ? 60.510  62.014  -6.624  1.00 18.47 ? 110 HIS B C   1 
ATOM   1959  O  O   . HIS B  1 137 ? 60.563  62.812  -7.547  1.00 17.21 ? 110 HIS B O   1 
ATOM   1960  C  CB  . HIS B  1 137 ? 58.855  63.414  -5.341  1.00 21.36 ? 110 HIS B CB  1 
ATOM   1961  C  CG  . HIS B  1 137 ? 57.523  63.459  -4.644  1.00 26.86 ? 110 HIS B CG  1 
ATOM   1962  N  ND1 . HIS B  1 137 ? 56.948  64.635  -4.199  1.00 32.24 ? 110 HIS B ND1 1 
ATOM   1963  C  CD2 . HIS B  1 137 ? 56.656  62.461  -4.321  1.00 27.79 ? 110 HIS B CD2 1 
ATOM   1964  C  CE1 . HIS B  1 137 ? 55.800  64.351  -3.595  1.00 31.35 ? 110 HIS B CE1 1 
ATOM   1965  N  NE2 . HIS B  1 137 ? 55.586  63.049  -3.683  1.00 33.53 ? 110 HIS B NE2 1 
ATOM   1966  N  N   . CYS B  1 138 ? 61.448  61.121  -6.374  1.00 17.17 ? 111 CYS B N   1 
ATOM   1967  C  CA  . CYS B  1 138 ? 62.691  61.018  -7.173  1.00 17.73 ? 111 CYS B CA  1 
ATOM   1968  C  C   . CYS B  1 138 ? 62.336  60.743  -8.630  1.00 16.62 ? 111 CYS B C   1 
ATOM   1969  O  O   . CYS B  1 138 ? 61.549  59.864  -8.934  1.00 17.74 ? 111 CYS B O   1 
ATOM   1970  C  CB  . CYS B  1 138 ? 63.533  59.850  -6.645  1.00 20.08 ? 111 CYS B CB  1 
ATOM   1971  S  SG  . CYS B  1 138 ? 65.114  59.842  -7.489  1.00 24.23 ? 111 CYS B SG  1 
ATOM   1972  N  N   . ILE B  1 139 ? 62.946  61.483  -9.544  1.00 15.60 ? 112 ILE B N   1 
ATOM   1973  C  CA  . ILE B  1 139 ? 62.654  61.326  -10.975 1.00 15.01 ? 112 ILE B CA  1 
ATOM   1974  C  C   . ILE B  1 139 ? 63.820  60.620  -11.736 1.00 14.76 ? 112 ILE B C   1 
ATOM   1975  O  O   . ILE B  1 139 ? 63.710  60.330  -12.911 1.00 13.47 ? 112 ILE B O   1 
ATOM   1976  C  CB  . ILE B  1 139 ? 62.330  62.690  -11.636 1.00 16.21 ? 112 ILE B CB  1 
ATOM   1977  C  CG1 . ILE B  1 139 ? 63.543  63.663  -11.572 1.00 16.81 ? 112 ILE B CG1 1 
ATOM   1978  C  CG2 . ILE B  1 139 ? 60.966  63.211  -11.061 1.00 15.87 ? 112 ILE B CG2 1 
ATOM   1979  C  CD1 . ILE B  1 139 ? 63.263  64.989  -12.293 1.00 19.34 ? 112 ILE B CD1 1 
ATOM   1980  N  N   A ILE B  1 140 ? 64.909  60.348  -11.011 0.50 14.99 ? 113 ILE B N   1 
ATOM   1981  N  N   B ILE B  1 140 ? 64.924  60.377  -11.042 0.50 14.35 ? 113 ILE B N   1 
ATOM   1982  C  CA  A ILE B  1 140 ? 66.055  59.542  -11.579 0.50 15.75 ? 113 ILE B CA  1 
ATOM   1983  C  CA  B ILE B  1 140 ? 66.055  59.635  -11.697 0.50 14.33 ? 113 ILE B CA  1 
ATOM   1984  C  C   A ILE B  1 140 ? 65.539  58.194  -12.045 0.50 14.47 ? 113 ILE B C   1 
ATOM   1985  C  C   B ILE B  1 140 ? 65.575  58.232  -12.050 0.50 13.75 ? 113 ILE B C   1 
ATOM   1986  O  O   A ILE B  1 140 ? 64.821  57.526  -11.320 0.50 15.37 ? 113 ILE B O   1 
ATOM   1987  O  O   B ILE B  1 140 ? 64.891  57.587  -11.270 0.50 14.83 ? 113 ILE B O   1 
ATOM   1988  C  CB  A ILE B  1 140 ? 67.136  59.245  -10.523 0.50 15.75 ? 113 ILE B CB  1 
ATOM   1989  C  CB  B ILE B  1 140 ? 67.291  59.584  -10.790 0.50 13.45 ? 113 ILE B CB  1 
ATOM   1990  C  CG1 A ILE B  1 140 ? 67.700  60.542  -9.992  0.50 17.90 ? 113 ILE B CG1 1 
ATOM   1991  C  CG1 B ILE B  1 140 ? 67.846  60.991  -10.644 0.50 14.39 ? 113 ILE B CG1 1 
ATOM   1992  C  CG2 A ILE B  1 140 ? 68.275  58.389  -11.135 0.50 15.36 ? 113 ILE B CG2 1 
ATOM   1993  C  CG2 B ILE B  1 140 ? 68.361  58.618  -11.355 0.50 13.33 ? 113 ILE B CG2 1 
ATOM   1994  C  CD1 A ILE B  1 140 ? 68.108  61.458  -11.109 0.50 19.63 ? 113 ILE B CD1 1 
ATOM   1995  C  CD1 B ILE B  1 140 ? 68.916  61.145  -9.580  0.50 13.51 ? 113 ILE B CD1 1 
ATOM   1996  N  N   . GLY B  1 141 ? 65.875  57.782  -13.257 1.00 14.13 ? 114 GLY B N   1 
ATOM   1997  C  CA  . GLY B  1 141 ? 65.402  56.469  -13.709 1.00 12.94 ? 114 GLY B CA  1 
ATOM   1998  C  C   . GLY B  1 141 ? 64.023  56.551  -14.368 1.00 13.82 ? 114 GLY B C   1 
ATOM   1999  O  O   . GLY B  1 141 ? 63.534  55.542  -14.821 1.00 13.81 ? 114 GLY B O   1 
ATOM   2000  N  N   . ARG B  1 142 ? 63.422  57.753  -14.421 1.00 12.74 ? 115 ARG B N   1 
ATOM   2001  C  CA  . ARG B  1 142 ? 62.089  57.926  -15.114 1.00 13.88 ? 115 ARG B CA  1 
ATOM   2002  C  C   . ARG B  1 142 ? 62.379  58.639  -16.435 1.00 14.92 ? 115 ARG B C   1 
ATOM   2003  O  O   . ARG B  1 142 ? 63.548  58.852  -16.776 1.00 16.23 ? 115 ARG B O   1 
ATOM   2004  C  CB  . ARG B  1 142 ? 61.130  58.727  -14.208 1.00 13.38 ? 115 ARG B CB  1 
ATOM   2005  C  CG  . ARG B  1 142 ? 61.015  57.974  -12.862 1.00 15.60 ? 115 ARG B CG  1 
ATOM   2006  C  CD  . ARG B  1 142 ? 59.861  58.374  -11.962 1.00 18.51 ? 115 ARG B CD  1 
ATOM   2007  N  NE  . ARG B  1 142 ? 59.909  57.651  -10.647 1.00 17.08 ? 115 ARG B NE  1 
ATOM   2008  C  CZ  . ARG B  1 142 ? 59.314  56.475  -10.385 1.00 18.94 ? 115 ARG B CZ  1 
ATOM   2009  N  NH1 . ARG B  1 142 ? 58.600  55.777  -11.305 1.00 17.33 ? 115 ARG B NH1 1 
ATOM   2010  N  NH2 . ARG B  1 142 ? 59.393  56.028  -9.142  1.00 19.48 ? 115 ARG B NH2 1 
ATOM   2011  N  N   . THR B  1 143 ? 61.335  58.934  -17.195 1.00 14.86 ? 116 THR B N   1 
ATOM   2012  C  CA  . THR B  1 143 ? 61.514  59.476  -18.542 1.00 14.74 ? 116 THR B CA  1 
ATOM   2013  C  C   . THR B  1 143 ? 61.007  60.914  -18.610 1.00 15.56 ? 116 THR B C   1 
ATOM   2014  O  O   . THR B  1 143 ? 59.844  61.181  -18.223 1.00 16.28 ? 116 THR B O   1 
ATOM   2015  C  CB  . THR B  1 143 ? 60.776  58.633  -19.570 1.00 15.73 ? 116 THR B CB  1 
ATOM   2016  O  OG1 . THR B  1 143 ? 61.380  57.325  -19.647 1.00 17.20 ? 116 THR B OG1 1 
ATOM   2017  C  CG2 . THR B  1 143 ? 60.862  59.264  -21.013 1.00 14.31 ? 116 THR B CG2 1 
ATOM   2018  N  N   . LEU B  1 144 ? 61.833  61.806  -19.138 1.00 13.77 ? 117 LEU B N   1 
ATOM   2019  C  CA  . LEU B  1 144 ? 61.375  63.164  -19.508 1.00 13.34 ? 117 LEU B CA  1 
ATOM   2020  C  C   . LEU B  1 144 ? 60.880  63.132  -20.926 1.00 14.54 ? 117 LEU B C   1 
ATOM   2021  O  O   . LEU B  1 144 ? 61.562  62.564  -21.801 1.00 12.88 ? 117 LEU B O   1 
ATOM   2022  C  CB  . LEU B  1 144 ? 62.488  64.197  -19.437 1.00 14.09 ? 117 LEU B CB  1 
ATOM   2023  C  CG  . LEU B  1 144 ? 62.186  65.686  -19.642 1.00 13.38 ? 117 LEU B CG  1 
ATOM   2024  C  CD1 . LEU B  1 144 ? 61.279  66.212  -18.497 1.00 14.34 ? 117 LEU B CD1 1 
ATOM   2025  C  CD2 . LEU B  1 144 ? 63.550  66.416  -19.628 1.00 12.06 ? 117 LEU B CD2 1 
ATOM   2026  N  N   . VAL B  1 145 ? 59.711  63.759  -21.163 1.00 12.75 ? 118 VAL B N   1 
ATOM   2027  C  CA  . VAL B  1 145 ? 59.100  63.795  -22.483 1.00 13.75 ? 118 VAL B CA  1 
ATOM   2028  C  C   . VAL B  1 145 ? 58.726  65.216  -22.886 1.00 14.80 ? 118 VAL B C   1 
ATOM   2029  O  O   . VAL B  1 145 ? 58.108  65.937  -22.088 1.00 14.02 ? 118 VAL B O   1 
ATOM   2030  C  CB  . VAL B  1 145 ? 57.793  62.943  -22.511 1.00 14.10 ? 118 VAL B CB  1 
ATOM   2031  C  CG1 . VAL B  1 145 ? 57.119  63.063  -23.913 1.00 14.26 ? 118 VAL B CG1 1 
ATOM   2032  C  CG2 . VAL B  1 145 ? 58.118  61.459  -22.180 1.00 15.77 ? 118 VAL B CG2 1 
ATOM   2033  N  N   . VAL B  1 146 ? 59.045  65.615  -24.126 1.00 14.07 ? 119 VAL B N   1 
ATOM   2034  C  CA  . VAL B  1 146 ? 58.524  66.885  -24.626 1.00 13.70 ? 119 VAL B CA  1 
ATOM   2035  C  C   . VAL B  1 146 ? 57.425  66.543  -25.681 1.00 14.82 ? 119 VAL B C   1 
ATOM   2036  O  O   . VAL B  1 146 ? 57.607  65.658  -26.562 1.00 14.29 ? 119 VAL B O   1 
ATOM   2037  C  CB  . VAL B  1 146 ? 59.634  67.820  -25.178 1.00 14.25 ? 119 VAL B CB  1 
ATOM   2038  C  CG1 . VAL B  1 146 ? 60.414  67.186  -26.363 1.00 15.44 ? 119 VAL B CG1 1 
ATOM   2039  C  CG2 . VAL B  1 146 ? 59.020  69.141  -25.614 1.00 15.70 ? 119 VAL B CG2 1 
ATOM   2040  N  N   . HIS B  1 147 ? 56.279  67.209  -25.546 1.00 13.45 ? 120 HIS B N   1 
ATOM   2041  C  CA  . HIS B  1 147 ? 55.075  66.843  -26.327 1.00 14.19 ? 120 HIS B CA  1 
ATOM   2042  C  C   . HIS B  1 147 ? 54.826  67.741  -27.516 1.00 15.33 ? 120 HIS B C   1 
ATOM   2043  O  O   . HIS B  1 147 ? 55.384  68.828  -27.622 1.00 15.25 ? 120 HIS B O   1 
ATOM   2044  C  CB  . HIS B  1 147 ? 53.845  66.870  -25.413 1.00 14.03 ? 120 HIS B CB  1 
ATOM   2045  C  CG  . HIS B  1 147 ? 53.837  65.749  -24.429 1.00 15.35 ? 120 HIS B CG  1 
ATOM   2046  N  ND1 . HIS B  1 147 ? 53.136  64.588  -24.659 1.00 16.37 ? 120 HIS B ND1 1 
ATOM   2047  C  CD2 . HIS B  1 147 ? 54.477  65.574  -23.244 1.00 15.30 ? 120 HIS B CD2 1 
ATOM   2048  C  CE1 . HIS B  1 147 ? 53.269  63.768  -23.629 1.00 16.70 ? 120 HIS B CE1 1 
ATOM   2049  N  NE2 . HIS B  1 147 ? 54.102  64.333  -22.763 1.00 16.67 ? 120 HIS B NE2 1 
ATOM   2050  N  N   . GLU B  1 148 ? 53.887  67.300  -28.352 1.00 15.58 ? 121 GLU B N   1 
ATOM   2051  C  CA  . GLU B  1 148 ? 53.604  67.974  -29.606 1.00 17.62 ? 121 GLU B CA  1 
ATOM   2052  C  C   . GLU B  1 148 ? 52.914  69.352  -29.468 1.00 16.80 ? 121 GLU B C   1 
ATOM   2053  O  O   . GLU B  1 148 ? 53.205  70.258  -30.225 1.00 18.16 ? 121 GLU B O   1 
ATOM   2054  C  CB  . GLU B  1 148 ? 52.687  67.003  -30.371 1.00 18.62 ? 121 GLU B CB  1 
ATOM   2055  C  CG  . GLU B  1 148 ? 52.064  67.507  -31.657 1.00 25.15 ? 121 GLU B CG  1 
ATOM   2056  C  CD  . GLU B  1 148 ? 50.758  66.736  -32.036 1.00 34.69 ? 121 GLU B CD  1 
ATOM   2057  O  OE1 . GLU B  1 148 ? 50.224  65.814  -31.296 1.00 30.27 ? 121 GLU B OE1 1 
ATOM   2058  O  OE2 . GLU B  1 148 ? 50.222  67.112  -33.101 1.00 39.71 ? 121 GLU B OE2 1 
ATOM   2059  N  N   . LYS B  1 149 ? 52.065  69.514  -28.460 1.00 19.06 ? 122 LYS B N   1 
ATOM   2060  C  CA  . LYS B  1 149 ? 51.160  70.687  -28.333 1.00 20.93 ? 122 LYS B CA  1 
ATOM   2061  C  C   . LYS B  1 149 ? 51.296  71.259  -26.919 1.00 19.35 ? 122 LYS B C   1 
ATOM   2062  O  O   . LYS B  1 149 ? 51.942  70.646  -26.023 1.00 18.63 ? 122 LYS B O   1 
ATOM   2063  C  CB  . LYS B  1 149 ? 49.672  70.226  -28.485 1.00 23.39 ? 122 LYS B CB  1 
ATOM   2064  C  CG  . LYS B  1 149 ? 49.343  69.412  -29.711 1.00 31.04 ? 122 LYS B CG  1 
ATOM   2065  C  CD  . LYS B  1 149 ? 47.904  68.898  -29.695 1.00 37.42 ? 122 LYS B CD  1 
ATOM   2066  C  CE  . LYS B  1 149 ? 46.893  70.020  -29.549 1.00 45.18 ? 122 LYS B CE  1 
ATOM   2067  N  NZ  . LYS B  1 149 ? 45.484  69.658  -29.978 1.00 51.17 ? 122 LYS B NZ  1 
ATOM   2068  N  N   . ALA B  1 150 ? 50.668  72.417  -26.715 1.00 17.25 ? 123 ALA B N   1 
ATOM   2069  C  CA  . ALA B  1 150 ? 50.632  73.018  -25.382 1.00 16.96 ? 123 ALA B CA  1 
ATOM   2070  C  C   . ALA B  1 150 ? 49.895  72.120  -24.370 1.00 17.98 ? 123 ALA B C   1 
ATOM   2071  O  O   . ALA B  1 150 ? 48.873  71.453  -24.686 1.00 17.49 ? 123 ALA B O   1 
ATOM   2072  C  CB  . ALA B  1 150 ? 50.012  74.429  -25.458 1.00 19.74 ? 123 ALA B CB  1 
ATOM   2073  N  N   . ASP B  1 151 ? 50.421  72.081  -23.152 1.00 15.85 ? 124 ASP B N   1 
ATOM   2074  C  CA  . ASP B  1 151 ? 49.712  71.489  -22.026 1.00 16.71 ? 124 ASP B CA  1 
ATOM   2075  C  C   . ASP B  1 151 ? 48.681  72.522  -21.586 1.00 15.54 ? 124 ASP B C   1 
ATOM   2076  O  O   . ASP B  1 151 ? 49.072  73.671  -21.286 1.00 14.98 ? 124 ASP B O   1 
ATOM   2077  C  CB  . ASP B  1 151 ? 50.751  71.300  -20.907 1.00 17.11 ? 124 ASP B CB  1 
ATOM   2078  C  CG  . ASP B  1 151 ? 50.195  70.613  -19.656 1.00 19.94 ? 124 ASP B CG  1 
ATOM   2079  O  OD1 . ASP B  1 151 ? 48.975  70.537  -19.460 1.00 16.81 ? 124 ASP B OD1 1 
ATOM   2080  O  OD2 . ASP B  1 151 ? 51.041  70.092  -18.851 1.00 20.43 ? 124 ASP B OD2 1 
ATOM   2081  N  N   . ASP B  1 152 ? 47.397  72.124  -21.495 1.00 15.75 ? 125 ASP B N   1 
ATOM   2082  C  CA  . ASP B  1 152 ? 46.356  73.101  -21.045 1.00 17.54 ? 125 ASP B CA  1 
ATOM   2083  C  C   . ASP B  1 152 ? 46.260  73.257  -19.504 1.00 17.55 ? 125 ASP B C   1 
ATOM   2084  O  O   . ASP B  1 152 ? 45.368  73.936  -18.959 1.00 16.91 ? 125 ASP B O   1 
ATOM   2085  C  CB  . ASP B  1 152 ? 44.996  72.738  -21.689 1.00 18.80 ? 125 ASP B CB  1 
ATOM   2086  C  CG  . ASP B  1 152 ? 44.347  71.468  -21.113 1.00 18.70 ? 125 ASP B CG  1 
ATOM   2087  O  OD1 . ASP B  1 152 ? 44.701  70.935  -20.044 1.00 17.28 ? 125 ASP B OD1 1 
ATOM   2088  O  OD2 . ASP B  1 152 ? 43.393  70.959  -21.772 1.00 19.18 ? 125 ASP B OD2 1 
ATOM   2089  N  N   . LEU B  1 153 ? 47.113  72.505  -18.804 1.00 15.54 ? 126 LEU B N   1 
ATOM   2090  C  CA  . LEU B  1 153 ? 47.334  72.670  -17.357 1.00 15.55 ? 126 LEU B CA  1 
ATOM   2091  C  C   . LEU B  1 153 ? 46.102  72.244  -16.570 1.00 15.83 ? 126 LEU B C   1 
ATOM   2092  O  O   . LEU B  1 153 ? 45.892  72.700  -15.431 1.00 15.76 ? 126 LEU B O   1 
ATOM   2093  C  CB  . LEU B  1 153 ? 47.829  74.086  -17.007 1.00 16.99 ? 126 LEU B CB  1 
ATOM   2094  C  CG  . LEU B  1 153 ? 48.981  74.634  -17.834 1.00 18.61 ? 126 LEU B CG  1 
ATOM   2095  C  CD1 . LEU B  1 153 ? 49.296  76.040  -17.423 1.00 21.10 ? 126 LEU B CD1 1 
ATOM   2096  C  CD2 . LEU B  1 153 ? 50.245  73.765  -17.793 1.00 18.90 ? 126 LEU B CD2 1 
ATOM   2097  N  N   . GLY B  1 154 ? 45.343  71.325  -17.166 1.00 15.09 ? 127 GLY B N   1 
ATOM   2098  C  CA  . GLY B  1 154 ? 44.173  70.758  -16.494 1.00 16.34 ? 127 GLY B CA  1 
ATOM   2099  C  C   . GLY B  1 154 ? 42.941  71.698  -16.640 1.00 19.23 ? 127 GLY B C   1 
ATOM   2100  O  O   . GLY B  1 154 ? 41.934  71.474  -15.995 1.00 16.19 ? 127 GLY B O   1 
ATOM   2101  N  N   . LYS B  1 155 ? 43.017  72.703  -17.490 1.00 17.13 ? 128 LYS B N   1 
ATOM   2102  C  CA  . LYS B  1 155 ? 41.898  73.715  -17.560 1.00 18.32 ? 128 LYS B CA  1 
ATOM   2103  C  C   . LYS B  1 155 ? 41.039  73.591  -18.802 1.00 17.84 ? 128 LYS B C   1 
ATOM   2104  O  O   . LYS B  1 155 ? 40.361  74.563  -19.202 1.00 20.40 ? 128 LYS B O   1 
ATOM   2105  C  CB  . LYS B  1 155 ? 42.477  75.124  -17.482 1.00 18.73 ? 128 LYS B CB  1 
ATOM   2106  C  CG  . LYS B  1 155 ? 43.230  75.373  -16.203 1.00 22.88 ? 128 LYS B CG  1 
ATOM   2107  C  CD  . LYS B  1 155 ? 44.003  76.638  -16.524 1.00 32.91 ? 128 LYS B CD  1 
ATOM   2108  C  CE  . LYS B  1 155 ? 44.192  77.508  -15.320 1.00 40.91 ? 128 LYS B CE  1 
ATOM   2109  N  NZ  . LYS B  1 155 ? 43.979  78.867  -15.891 1.00 41.05 ? 128 LYS B NZ  1 
ATOM   2110  N  N   . GLY B  1 156 ? 41.111  72.443  -19.472 1.00 14.74 ? 129 GLY B N   1 
ATOM   2111  C  CA  . GLY B  1 156 ? 40.430  72.279  -20.771 1.00 16.58 ? 129 GLY B CA  1 
ATOM   2112  C  C   . GLY B  1 156 ? 38.952  71.820  -20.677 1.00 16.28 ? 129 GLY B C   1 
ATOM   2113  O  O   . GLY B  1 156 ? 38.275  71.707  -21.711 1.00 16.23 ? 129 GLY B O   1 
ATOM   2114  N  N   . GLY B  1 157 ? 38.503  71.454  -19.469 1.00 17.44 ? 130 GLY B N   1 
ATOM   2115  C  CA  . GLY B  1 157 ? 37.059  71.095  -19.231 1.00 18.05 ? 130 GLY B CA  1 
ATOM   2116  C  C   . GLY B  1 157 ? 36.668  69.746  -19.827 1.00 19.77 ? 130 GLY B C   1 
ATOM   2117  O  O   . GLY B  1 157 ? 35.482  69.467  -20.087 1.00 19.61 ? 130 GLY B O   1 
ATOM   2118  N  N   . ASN B  1 158 ? 37.657  68.876  -20.089 1.00 21.83 ? 131 ASN B N   1 
ATOM   2119  C  CA  . ASN B  1 158 ? 37.354  67.512  -20.504 1.00 21.32 ? 131 ASN B CA  1 
ATOM   2120  C  C   . ASN B  1 158 ? 38.182  66.504  -19.717 1.00 22.22 ? 131 ASN B C   1 
ATOM   2121  O  O   . ASN B  1 158 ? 39.108  66.875  -18.978 1.00 20.19 ? 131 ASN B O   1 
ATOM   2122  C  CB  . ASN B  1 158 ? 37.403  67.335  -22.055 1.00 23.34 ? 131 ASN B CB  1 
ATOM   2123  C  CG  . ASN B  1 158 ? 38.811  67.524  -22.664 1.00 26.29 ? 131 ASN B CG  1 
ATOM   2124  O  OD1 . ASN B  1 158 ? 39.805  67.572  -21.959 1.00 21.29 ? 131 ASN B OD1 1 
ATOM   2125  N  ND2 . ASN B  1 158 ? 38.874  67.593  -23.991 1.00 24.84 ? 131 ASN B ND2 1 
ATOM   2126  N  N   . GLU B  1 159 ? 37.837  65.229  -19.829 1.00 22.61 ? 132 GLU B N   1 
ATOM   2127  C  CA  . GLU B  1 159 ? 38.538  64.204  -19.069 1.00 27.33 ? 132 GLU B CA  1 
ATOM   2128  C  C   . GLU B  1 159 ? 40.020  64.155  -19.419 1.00 23.68 ? 132 GLU B C   1 
ATOM   2129  O  O   . GLU B  1 159 ? 40.862  63.959  -18.553 1.00 24.09 ? 132 GLU B O   1 
ATOM   2130  C  CB  . GLU B  1 159 ? 37.970  62.812  -19.348 1.00 29.68 ? 132 GLU B CB  1 
ATOM   2131  C  CG  . GLU B  1 159 ? 36.871  62.431  -18.374 1.00 40.77 ? 132 GLU B CG  1 
ATOM   2132  C  CD  . GLU B  1 159 ? 36.629  60.919  -18.284 1.00 55.44 ? 132 GLU B CD  1 
ATOM   2133  O  OE1 . GLU B  1 159 ? 37.492  60.108  -18.742 1.00 54.25 ? 132 GLU B OE1 1 
ATOM   2134  O  OE2 . GLU B  1 159 ? 35.564  60.541  -17.733 1.00 59.49 ? 132 GLU B OE2 1 
ATOM   2135  N  N   . GLU B  1 160 ? 40.305  64.300  -20.691 1.00 22.44 ? 133 GLU B N   1 
ATOM   2136  C  CA  . GLU B  1 160 ? 41.685  64.204  -21.163 1.00 24.01 ? 133 GLU B CA  1 
ATOM   2137  C  C   . GLU B  1 160 ? 42.526  65.353  -20.526 1.00 23.28 ? 133 GLU B C   1 
ATOM   2138  O  O   . GLU B  1 160 ? 43.703  65.179  -20.219 1.00 21.12 ? 133 GLU B O   1 
ATOM   2139  C  CB  . GLU B  1 160 ? 41.717  64.323  -22.666 1.00 26.12 ? 133 GLU B CB  1 
ATOM   2140  C  CG  . GLU B  1 160 ? 43.091  64.066  -23.272 1.00 33.55 ? 133 GLU B CG  1 
ATOM   2141  C  CD  . GLU B  1 160 ? 43.509  62.625  -23.094 1.00 40.12 ? 133 GLU B CD  1 
ATOM   2142  O  OE1 . GLU B  1 160 ? 42.688  61.752  -23.426 1.00 40.49 ? 133 GLU B OE1 1 
ATOM   2143  O  OE2 . GLU B  1 160 ? 44.632  62.350  -22.585 1.00 36.33 ? 133 GLU B OE2 1 
ATOM   2144  N  N   . SER B  1 161 ? 41.910  66.496  -20.269 1.00 19.38 ? 134 SER B N   1 
ATOM   2145  C  CA  . SER B  1 161 ? 42.681  67.593  -19.683 1.00 16.85 ? 134 SER B CA  1 
ATOM   2146  C  C   . SER B  1 161 ? 43.177  67.236  -18.319 1.00 17.65 ? 134 SER B C   1 
ATOM   2147  O  O   . SER B  1 161 ? 44.304  67.628  -17.958 1.00 16.06 ? 134 SER B O   1 
ATOM   2148  C  CB  . SER B  1 161 ? 41.822  68.867  -19.671 1.00 18.14 ? 134 SER B CB  1 
ATOM   2149  O  OG  . SER B  1 161 ? 42.419  69.909  -18.974 1.00 18.43 ? 134 SER B OG  1 
ATOM   2150  N  N   . THR B  1 162 ? 42.358  66.500  -17.544 1.00 17.54 ? 135 THR B N   1 
ATOM   2151  C  CA  . THR B  1 162 ? 42.691  66.110  -16.164 1.00 21.10 ? 135 THR B CA  1 
ATOM   2152  C  C   . THR B  1 162 ? 43.649  64.902  -16.121 1.00 20.51 ? 135 THR B C   1 
ATOM   2153  O  O   . THR B  1 162 ? 44.024  64.435  -15.013 1.00 19.58 ? 135 THR B O   1 
ATOM   2154  C  CB  . THR B  1 162 ? 41.396  65.625  -15.380 1.00 24.27 ? 135 THR B CB  1 
ATOM   2155  O  OG1 . THR B  1 162 ? 41.005  64.306  -15.865 1.00 35.40 ? 135 THR B OG1 1 
ATOM   2156  C  CG2 . THR B  1 162 ? 40.279  66.472  -15.595 1.00 27.11 ? 135 THR B CG2 1 
ATOM   2157  N  N   . LYS B  1 163 ? 44.003  64.392  -17.294 1.00 21.03 ? 136 LYS B N   1 
ATOM   2158  C  CA  . LYS B  1 163 ? 44.941  63.231  -17.432 1.00 23.92 ? 136 LYS B CA  1 
ATOM   2159  C  C   . LYS B  1 163 ? 46.267  63.637  -18.047 1.00 20.87 ? 136 LYS B C   1 
ATOM   2160  O  O   . LYS B  1 163 ? 47.324  63.357  -17.473 1.00 23.14 ? 136 LYS B O   1 
ATOM   2161  C  CB  . LYS B  1 163 ? 44.315  62.049  -18.214 1.00 25.13 ? 136 LYS B CB  1 
ATOM   2162  C  CG  . LYS B  1 163 ? 43.089  61.514  -17.493 1.00 34.09 ? 136 LYS B CG  1 
ATOM   2163  C  CD  . LYS B  1 163 ? 42.746  60.063  -17.860 1.00 40.90 ? 136 LYS B CD  1 
ATOM   2164  C  CE  . LYS B  1 163 ? 42.469  59.828  -19.332 1.00 47.55 ? 136 LYS B CE  1 
ATOM   2165  N  NZ  . LYS B  1 163 ? 41.880  58.459  -19.589 1.00 52.27 ? 136 LYS B NZ  1 
ATOM   2166  N  N   . THR B  1 164 ? 46.232  64.282  -19.206 1.00 20.49 ? 137 THR B N   1 
ATOM   2167  C  CA  . THR B  1 164 ? 47.465  64.582  -19.977 1.00 21.22 ? 137 THR B CA  1 
ATOM   2168  C  C   . THR B  1 164 ? 47.608  66.061  -20.300 1.00 20.57 ? 137 THR B C   1 
ATOM   2169  O  O   . THR B  1 164 ? 48.565  66.481  -20.990 1.00 20.32 ? 137 THR B O   1 
ATOM   2170  C  CB  . THR B  1 164 ? 47.431  63.846  -21.322 1.00 23.59 ? 137 THR B CB  1 
ATOM   2171  O  OG1 . THR B  1 164 ? 46.342  64.338  -22.095 1.00 22.61 ? 137 THR B OG1 1 
ATOM   2172  C  CG2 . THR B  1 164 ? 47.255  62.299  -21.114 1.00 24.93 ? 137 THR B CG2 1 
ATOM   2173  N  N   . GLY B  1 165 ? 46.567  66.849  -19.967 1.00 18.58 ? 138 GLY B N   1 
ATOM   2174  C  CA  . GLY B  1 165 ? 46.617  68.258  -20.355 1.00 16.86 ? 138 GLY B CA  1 
ATOM   2175  C  C   . GLY B  1 165 ? 46.408  68.465  -21.860 1.00 15.61 ? 138 GLY B C   1 
ATOM   2176  O  O   . GLY B  1 165 ? 46.609  69.568  -22.338 1.00 16.64 ? 138 GLY B O   1 
ATOM   2177  N  N   . ASN B  1 166 ? 45.979  67.423  -22.599 1.00 17.11 ? 139 ASN B N   1 
ATOM   2178  C  CA  . ASN B  1 166 ? 45.745  67.549  -24.040 1.00 17.26 ? 139 ASN B CA  1 
ATOM   2179  C  C   . ASN B  1 166 ? 47.035  67.917  -24.818 1.00 16.76 ? 139 ASN B C   1 
ATOM   2180  O  O   . ASN B  1 166 ? 46.982  68.576  -25.846 1.00 15.75 ? 139 ASN B O   1 
ATOM   2181  C  CB  . ASN B  1 166 ? 44.629  68.598  -24.314 1.00 20.80 ? 139 ASN B CB  1 
ATOM   2182  C  CG  . ASN B  1 166 ? 43.242  68.025  -23.981 1.00 21.88 ? 139 ASN B CG  1 
ATOM   2183  O  OD1 . ASN B  1 166 ? 42.882  66.988  -24.528 1.00 23.70 ? 139 ASN B OD1 1 
ATOM   2184  N  ND2 . ASN B  1 166 ? 42.550  68.605  -23.016 1.00 20.77 ? 139 ASN B ND2 1 
ATOM   2185  N  N   . ALA B  1 167 ? 48.214  67.513  -24.297 1.00 15.37 ? 140 ALA B N   1 
ATOM   2186  C  CA  . ALA B  1 167 ? 49.479  68.006  -24.895 1.00 15.46 ? 140 ALA B CA  1 
ATOM   2187  C  C   . ALA B  1 167 ? 49.872  67.171  -26.144 1.00 15.81 ? 140 ALA B C   1 
ATOM   2188  O  O   . ALA B  1 167 ? 50.902  67.414  -26.805 1.00 16.16 ? 140 ALA B O   1 
ATOM   2189  C  CB  . ALA B  1 167 ? 50.626  67.991  -23.829 1.00 12.56 ? 140 ALA B CB  1 
ATOM   2190  N  N   . GLY B  1 168 ? 49.071  66.174  -26.474 1.00 18.04 ? 141 GLY B N   1 
ATOM   2191  C  CA  . GLY B  1 168 ? 49.304  65.368  -27.717 1.00 19.21 ? 141 GLY B CA  1 
ATOM   2192  C  C   . GLY B  1 168 ? 50.523  64.430  -27.701 1.00 19.29 ? 141 GLY B C   1 
ATOM   2193  O  O   . GLY B  1 168 ? 50.945  63.964  -26.627 1.00 17.56 ? 141 GLY B O   1 
ATOM   2194  N  N   A SER B  1 169 ? 51.101  64.192  -28.888 0.50 19.50 ? 142 SER B N   1 
ATOM   2195  N  N   B SER B  1 169 ? 51.088  64.161  -28.882 0.50 18.79 ? 142 SER B N   1 
ATOM   2196  C  CA  A SER B  1 169 ? 52.085  63.121  -29.101 0.50 19.35 ? 142 SER B CA  1 
ATOM   2197  C  CA  B SER B  1 169 ? 52.034  63.060  -29.040 0.50 18.06 ? 142 SER B CA  1 
ATOM   2198  C  C   A SER B  1 169 ? 53.381  63.393  -28.372 0.50 18.72 ? 142 SER B C   1 
ATOM   2199  C  C   B SER B  1 169 ? 53.371  63.380  -28.388 0.50 18.04 ? 142 SER B C   1 
ATOM   2200  O  O   A SER B  1 169 ? 53.681  64.542  -28.045 0.50 18.94 ? 142 SER B O   1 
ATOM   2201  O  O   B SER B  1 169 ? 53.672  64.542  -28.105 0.50 18.34 ? 142 SER B O   1 
ATOM   2202  C  CB  A SER B  1 169 ? 52.459  62.992  -30.583 0.50 20.59 ? 142 SER B CB  1 
ATOM   2203  C  CB  B SER B  1 169 ? 52.269  62.733  -30.522 0.50 18.44 ? 142 SER B CB  1 
ATOM   2204  O  OG  A SER B  1 169 ? 51.323  63.048  -31.411 0.50 22.44 ? 142 SER B OG  1 
ATOM   2205  O  OG  B SER B  1 169 ? 52.935  63.793  -31.207 0.50 17.70 ? 142 SER B OG  1 
ATOM   2206  N  N   . ARG B  1 170 ? 54.173  62.344  -28.194 1.00 17.27 ? 143 ARG B N   1 
ATOM   2207  C  CA  . ARG B  1 170 ? 55.494  62.475  -27.560 1.00 17.93 ? 143 ARG B CA  1 
ATOM   2208  C  C   . ARG B  1 170 ? 56.514  62.698  -28.656 1.00 18.12 ? 143 ARG B C   1 
ATOM   2209  O  O   . ARG B  1 170 ? 56.760  61.793  -29.508 1.00 22.12 ? 143 ARG B O   1 
ATOM   2210  C  CB  . ARG B  1 170 ? 55.763  61.177  -26.811 1.00 17.95 ? 143 ARG B CB  1 
ATOM   2211  C  CG  . ARG B  1 170 ? 54.598  60.959  -25.828 1.00 19.71 ? 143 ARG B CG  1 
ATOM   2212  C  CD  . ARG B  1 170 ? 54.648  59.615  -25.119 1.00 18.27 ? 143 ARG B CD  1 
ATOM   2213  N  NE  . ARG B  1 170 ? 53.487  59.469  -24.232 1.00 17.92 ? 143 ARG B NE  1 
ATOM   2214  C  CZ  . ARG B  1 170 ? 53.382  58.640  -23.189 1.00 19.99 ? 143 ARG B CZ  1 
ATOM   2215  N  NH1 . ARG B  1 170 ? 54.407  57.883  -22.786 1.00 17.84 ? 143 ARG B NH1 1 
ATOM   2216  N  NH2 . ARG B  1 170 ? 52.255  58.637  -22.459 1.00 18.61 ? 143 ARG B NH2 1 
ATOM   2217  N  N   . LEU B  1 171 ? 57.126  63.859  -28.686 1.00 16.86 ? 144 LEU B N   1 
ATOM   2218  C  CA  . LEU B  1 171 ? 58.074  64.142  -29.778 1.00 17.98 ? 144 LEU B CA  1 
ATOM   2219  C  C   . LEU B  1 171 ? 59.446  63.614  -29.497 1.00 18.20 ? 144 LEU B C   1 
ATOM   2220  O  O   . LEU B  1 171 ? 60.150  63.234  -30.435 1.00 15.66 ? 144 LEU B O   1 
ATOM   2221  C  CB  . LEU B  1 171 ? 58.224  65.657  -30.026 1.00 18.36 ? 144 LEU B CB  1 
ATOM   2222  C  CG  . LEU B  1 171 ? 56.895  66.349  -30.335 1.00 22.09 ? 144 LEU B CG  1 
ATOM   2223  C  CD1 . LEU B  1 171 ? 57.181  67.822  -30.576 1.00 23.05 ? 144 LEU B CD1 1 
ATOM   2224  C  CD2 . LEU B  1 171 ? 56.217  65.717  -31.536 1.00 24.07 ? 144 LEU B CD2 1 
ATOM   2225  N  N   . ALA B  1 172 ? 59.893  63.688  -28.228 1.00 17.05 ? 145 ALA B N   1 
ATOM   2226  C  CA  . ALA B  1 172 ? 61.249  63.198  -27.913 1.00 16.39 ? 145 ALA B CA  1 
ATOM   2227  C  C   . ALA B  1 172 ? 61.254  62.863  -26.435 1.00 16.53 ? 145 ALA B C   1 
ATOM   2228  O  O   . ALA B  1 172 ? 60.467  63.438  -25.663 1.00 15.50 ? 145 ALA B O   1 
ATOM   2229  C  CB  . ALA B  1 172 ? 62.304  64.266  -28.225 1.00 16.07 ? 145 ALA B CB  1 
ATOM   2230  N  N   . CYS B  1 173 ? 62.139  61.971  -26.017 1.00 15.85 ? 146 CYS B N   1 
ATOM   2231  C  CA  . CYS B  1 173 ? 62.166  61.588  -24.591 1.00 16.22 ? 146 CYS B CA  1 
ATOM   2232  C  C   . CYS B  1 173 ? 63.544  61.020  -24.244 1.00 17.00 ? 146 CYS B C   1 
ATOM   2233  O  O   . CYS B  1 173 ? 64.323  60.758  -25.145 1.00 16.25 ? 146 CYS B O   1 
ATOM   2234  C  CB  . CYS B  1 173 ? 61.102  60.526  -24.268 1.00 17.85 ? 146 CYS B CB  1 
ATOM   2235  S  SG  . CYS B  1 173 ? 61.289  59.008  -25.264 1.00 23.42 ? 146 CYS B SG  1 
ATOM   2236  N  N   . GLY B  1 174 ? 63.822  60.828  -22.943 1.00 16.15 ? 147 GLY B N   1 
ATOM   2237  C  CA  . GLY B  1 174 ? 65.075  60.147  -22.554 1.00 17.36 ? 147 GLY B CA  1 
ATOM   2238  C  C   . GLY B  1 174 ? 64.907  59.746  -21.121 1.00 16.62 ? 147 GLY B C   1 
ATOM   2239  O  O   . GLY B  1 174 ? 64.068  60.340  -20.384 1.00 14.73 ? 147 GLY B O   1 
ATOM   2240  N  N   . VAL B  1 175 ? 65.778  58.834  -20.691 1.00 15.86 ? 148 VAL B N   1 
ATOM   2241  C  CA  . VAL B  1 175 ? 65.769  58.420  -19.287 1.00 15.00 ? 148 VAL B CA  1 
ATOM   2242  C  C   . VAL B  1 175 ? 66.597  59.430  -18.529 1.00 15.48 ? 148 VAL B C   1 
ATOM   2243  O  O   . VAL B  1 175 ? 67.688  59.798  -18.993 1.00 16.09 ? 148 VAL B O   1 
ATOM   2244  C  CB  . VAL B  1 175 ? 66.369  56.985  -19.151 1.00 15.61 ? 148 VAL B CB  1 
ATOM   2245  C  CG1 . VAL B  1 175 ? 66.305  56.531  -17.684 1.00 14.93 ? 148 VAL B CG1 1 
ATOM   2246  C  CG2 . VAL B  1 175 ? 65.545  56.013  -20.032 1.00 17.81 ? 148 VAL B CG2 1 
ATOM   2247  N  N   . ILE B  1 176 ? 66.137  59.815  -17.341 1.00 13.87 ? 149 ILE B N   1 
ATOM   2248  C  CA  . ILE B  1 176 ? 66.880  60.759  -16.511 1.00 14.53 ? 149 ILE B CA  1 
ATOM   2249  C  C   . ILE B  1 176 ? 67.962  59.958  -15.731 1.00 13.93 ? 149 ILE B C   1 
ATOM   2250  O  O   . ILE B  1 176 ? 67.642  59.051  -14.962 1.00 15.04 ? 149 ILE B O   1 
ATOM   2251  C  CB  . ILE B  1 176 ? 65.904  61.461  -15.530 1.00 14.06 ? 149 ILE B CB  1 
ATOM   2252  C  CG1 . ILE B  1 176 ? 64.857  62.280  -16.385 1.00 15.95 ? 149 ILE B CG1 1 
ATOM   2253  C  CG2 . ILE B  1 176 ? 66.643  62.435  -14.588 1.00 13.76 ? 149 ILE B CG2 1 
ATOM   2254  C  CD1 . ILE B  1 176 ? 63.567  62.599  -15.586 1.00 15.97 ? 149 ILE B CD1 1 
ATOM   2255  N  N   . GLY B  1 177 ? 69.197  60.391  -15.862 1.00 14.39 ? 150 GLY B N   1 
ATOM   2256  C  CA  . GLY B  1 177 ? 70.318  59.646  -15.285 1.00 15.08 ? 150 GLY B CA  1 
ATOM   2257  C  C   . GLY B  1 177 ? 71.071  60.493  -14.280 1.00 16.60 ? 150 GLY B C   1 
ATOM   2258  O  O   . GLY B  1 177 ? 71.066  61.710  -14.341 1.00 15.41 ? 150 GLY B O   1 
ATOM   2259  N  N   . ILE B  1 178 ? 71.807  59.818  -13.397 1.00 16.16 ? 151 ILE B N   1 
ATOM   2260  C  CA  . ILE B  1 178 ? 72.687  60.506  -12.417 1.00 17.99 ? 151 ILE B CA  1 
ATOM   2261  C  C   . ILE B  1 178 ? 73.865  61.147  -13.113 1.00 19.00 ? 151 ILE B C   1 
ATOM   2262  O  O   . ILE B  1 178 ? 74.483  60.515  -13.976 1.00 18.46 ? 151 ILE B O   1 
ATOM   2263  C  CB  . ILE B  1 178 ? 73.235  59.492  -11.353 1.00 20.77 ? 151 ILE B CB  1 
ATOM   2264  C  CG1 . ILE B  1 178 ? 72.083  58.976  -10.552 1.00 26.28 ? 151 ILE B CG1 1 
ATOM   2265  C  CG2 . ILE B  1 178 ? 74.100  60.206  -10.294 1.00 24.28 ? 151 ILE B CG2 1 
ATOM   2266  C  CD1 . ILE B  1 178 ? 72.336  57.626  -9.913  1.00 31.08 ? 151 ILE B CD1 1 
ATOM   2267  N  N   . ALA B  1 179 ? 74.180  62.394  -12.764 1.00 17.05 ? 152 ALA B N   1 
ATOM   2268  C  CA  . ALA B  1 179 ? 75.225  63.154  -13.457 1.00 18.66 ? 152 ALA B CA  1 
ATOM   2269  C  C   . ALA B  1 179 ? 76.331  63.531  -12.457 1.00 22.77 ? 152 ALA B C   1 
ATOM   2270  O  O   . ALA B  1 179 ? 76.143  63.391  -11.264 1.00 21.16 ? 152 ALA B O   1 
ATOM   2271  C  CB  . ALA B  1 179 ? 74.683  64.403  -14.113 1.00 19.09 ? 152 ALA B CB  1 
ATOM   2272  N  N   . GLN B  1 180 ? 77.493  63.901  -12.973 1.00 26.83 ? 153 GLN B N   1 
ATOM   2273  C  CA  . GLN B  1 180 ? 78.729  64.155  -12.149 1.00 36.87 ? 153 GLN B CA  1 
ATOM   2274  C  C   . GLN B  1 180 ? 78.667  65.607  -11.681 1.00 46.03 ? 153 GLN B C   1 
ATOM   2275  O  O   . GLN B  1 180 ? 78.619  66.550  -12.502 1.00 51.13 ? 153 GLN B O   1 
ATOM   2276  C  CB  . GLN B  1 180 ? 80.004  63.920  -12.998 1.00 35.21 ? 153 GLN B CB  1 
ATOM   2277  C  CG  . GLN B  1 180 ? 81.385  63.933  -12.255 1.00 44.83 ? 153 GLN B CG  1 
ATOM   2278  C  CD  . GLN B  1 180 ? 82.444  63.140  -13.012 1.00 45.62 ? 153 GLN B CD  1 
ATOM   2279  O  OE1 . GLN B  1 180 ? 82.258  62.895  -14.219 1.00 37.17 ? 153 GLN B OE1 1 
ATOM   2280  N  NE2 . GLN B  1 180 ? 83.562  62.695  -12.317 1.00 44.64 ? 153 GLN B NE2 1 
ATOM   2281  O  OXT . GLN B  1 180 ? 78.677  65.888  -10.466 1.00 61.65 ? 153 GLN B OXT 1 
ATOM   2282  N  N   . MET C  1 27  ? 50.455  112.701 -1.536  1.00 53.79 ? 0   MET C N   1 
ATOM   2283  C  CA  . MET C  1 27  ? 50.610  113.730 -2.593  1.00 54.28 ? 0   MET C CA  1 
ATOM   2284  C  C   . MET C  1 27  ? 49.924  113.260 -3.916  1.00 52.33 ? 0   MET C C   1 
ATOM   2285  O  O   . MET C  1 27  ? 48.717  113.519 -4.082  1.00 52.22 ? 0   MET C O   1 
ATOM   2286  C  CB  . MET C  1 27  ? 52.082  114.080 -2.775  1.00 53.64 ? 0   MET C CB  1 
ATOM   2287  N  N   . ALA C  1 28  ? 50.631  112.552 -4.824  1.00 46.47 ? 1   ALA C N   1 
ATOM   2288  C  CA  . ALA C  1 28  ? 50.018  112.141 -6.138  1.00 44.36 ? 1   ALA C CA  1 
ATOM   2289  C  C   . ALA C  1 28  ? 48.817  111.132 -6.083  1.00 35.21 ? 1   ALA C C   1 
ATOM   2290  O  O   . ALA C  1 28  ? 48.917  110.023 -5.574  1.00 39.05 ? 1   ALA C O   1 
ATOM   2291  C  CB  . ALA C  1 28  ? 51.088  111.724 -7.173  1.00 43.09 ? 1   ALA C CB  1 
ATOM   2292  N  N   . THR C  1 29  ? 47.647  111.540 -6.563  1.00 32.14 ? 2   THR C N   1 
ATOM   2293  C  CA  . THR C  1 29  ? 46.583  110.580 -6.665  1.00 26.27 ? 2   THR C CA  1 
ATOM   2294  C  C   . THR C  1 29  ? 46.187  110.275 -8.129  1.00 23.13 ? 2   THR C C   1 
ATOM   2295  O  O   . THR C  1 29  ? 45.399  109.368 -8.345  1.00 20.78 ? 2   THR C O   1 
ATOM   2296  C  CB  . THR C  1 29  ? 45.334  111.002 -5.873  1.00 29.95 ? 2   THR C CB  1 
ATOM   2297  O  OG1 . THR C  1 29  ? 44.796  112.175 -6.480  1.00 34.86 ? 2   THR C OG1 1 
ATOM   2298  C  CG2 . THR C  1 29  ? 45.720  111.328 -4.421  1.00 35.87 ? 2   THR C CG2 1 
ATOM   2299  N  N   . LYS C  1 30  ? 46.720  111.026 -9.086  1.00 21.15 ? 3   LYS C N   1 
ATOM   2300  C  CA  . LYS C  1 30  ? 46.432  110.782 -10.523 1.00 20.46 ? 3   LYS C CA  1 
ATOM   2301  C  C   . LYS C  1 30  ? 47.675  110.870 -11.365 1.00 17.48 ? 3   LYS C C   1 
ATOM   2302  O  O   . LYS C  1 30  ? 48.537  111.720 -11.134 1.00 18.95 ? 3   LYS C O   1 
ATOM   2303  C  CB  . LYS C  1 30  ? 45.422  111.798 -11.048 1.00 23.70 ? 3   LYS C CB  1 
ATOM   2304  C  CG  . LYS C  1 30  ? 44.103  111.649 -10.317 1.00 30.30 ? 3   LYS C CG  1 
ATOM   2305  C  CD  . LYS C  1 30  ? 42.957  111.632 -11.284 1.00 39.49 ? 3   LYS C CD  1 
ATOM   2306  C  CE  . LYS C  1 30  ? 42.480  113.044 -11.511 1.00 40.61 ? 3   LYS C CE  1 
ATOM   2307  N  NZ  . LYS C  1 30  ? 41.696  113.478 -10.320 1.00 52.31 ? 3   LYS C NZ  1 
ATOM   2308  N  N   . ALA C  1 31  ? 47.776  109.997 -12.362 1.00 16.35 ? 4   ALA C N   1 
ATOM   2309  C  CA  . ALA C  1 31  ? 48.896  110.080 -13.273 1.00 17.40 ? 4   ALA C CA  1 
ATOM   2310  C  C   . ALA C  1 31  ? 48.358  109.787 -14.684 1.00 16.02 ? 4   ALA C C   1 
ATOM   2311  O  O   . ALA C  1 31  ? 47.223  109.315 -14.850 1.00 15.89 ? 4   ALA C O   1 
ATOM   2312  C  CB  . ALA C  1 31  ? 50.028  109.095 -12.892 1.00 15.80 ? 4   ALA C CB  1 
ATOM   2313  N  N   . VAL C  1 32  ? 49.171  110.131 -15.692 1.00 15.61 ? 5   VAL C N   1 
ATOM   2314  C  CA  . VAL C  1 32  ? 48.744  109.872 -17.074 1.00 16.61 ? 5   VAL C CA  1 
ATOM   2315  C  C   . VAL C  1 32  ? 49.948  109.530 -17.948 1.00 15.61 ? 5   VAL C C   1 
ATOM   2316  O  O   . VAL C  1 32  ? 51.097  109.880 -17.618 1.00 16.61 ? 5   VAL C O   1 
ATOM   2317  C  CB  . VAL C  1 32  ? 47.959  111.099 -17.626 1.00 17.99 ? 5   VAL C CB  1 
ATOM   2318  C  CG1 . VAL C  1 32  ? 48.863  112.324 -17.762 1.00 20.41 ? 5   VAL C CG1 1 
ATOM   2319  C  CG2 . VAL C  1 32  ? 47.249  110.745 -18.932 1.00 19.78 ? 5   VAL C CG2 1 
ATOM   2320  N  N   . CYS C  1 33  ? 49.707  108.783 -19.022 1.00 15.66 ? 6   CYS C N   1 
ATOM   2321  C  CA  . CYS C  1 33  ? 50.772  108.396 -19.903 1.00 15.10 ? 6   CYS C CA  1 
ATOM   2322  C  C   . CYS C  1 33  ? 50.272  108.439 -21.343 1.00 15.17 ? 6   CYS C C   1 
ATOM   2323  O  O   . CYS C  1 33  ? 49.242  107.863 -21.639 1.00 16.11 ? 6   CYS C O   1 
ATOM   2324  C  CB  . CYS C  1 33  ? 51.231  106.952 -19.573 1.00 15.41 ? 6   CYS C CB  1 
ATOM   2325  S  SG  . CYS C  1 33  ? 52.599  106.412 -20.613 1.00 20.11 ? 6   CYS C SG  1 
ATOM   2326  N  N   . VAL C  1 34  ? 51.034  109.088 -22.226 1.00 14.44 ? 7   VAL C N   1 
ATOM   2327  C  CA  . VAL C  1 34  ? 50.704  109.130 -23.667 1.00 15.96 ? 7   VAL C CA  1 
ATOM   2328  C  C   . VAL C  1 34  ? 51.634  108.135 -24.363 1.00 16.95 ? 7   VAL C C   1 
ATOM   2329  O  O   . VAL C  1 34  ? 52.836  108.318 -24.325 1.00 16.88 ? 7   VAL C O   1 
ATOM   2330  C  CB  . VAL C  1 34  ? 50.924  110.538 -24.281 1.00 16.22 ? 7   VAL C CB  1 
ATOM   2331  C  CG1 . VAL C  1 34  ? 50.621  110.481 -25.797 1.00 19.08 ? 7   VAL C CG1 1 
ATOM   2332  C  CG2 . VAL C  1 34  ? 50.055  111.557 -23.554 1.00 17.45 ? 7   VAL C CG2 1 
ATOM   2333  N  N   . LEU C  1 35  ? 51.080  107.056 -24.920 1.00 16.19 ? 8   LEU C N   1 
ATOM   2334  C  CA  . LEU C  1 35  ? 51.909  106.026 -25.552 1.00 16.92 ? 8   LEU C CA  1 
ATOM   2335  C  C   . LEU C  1 35  ? 52.029  106.369 -27.050 1.00 17.87 ? 8   LEU C C   1 
ATOM   2336  O  O   . LEU C  1 35  ? 51.007  106.611 -27.704 1.00 16.43 ? 8   LEU C O   1 
ATOM   2337  C  CB  . LEU C  1 35  ? 51.155  104.694 -25.407 1.00 17.98 ? 8   LEU C CB  1 
ATOM   2338  C  CG  . LEU C  1 35  ? 50.922  104.181 -23.966 1.00 18.90 ? 8   LEU C CG  1 
ATOM   2339  C  CD1 . LEU C  1 35  ? 50.031  102.930 -23.998 1.00 23.85 ? 8   LEU C CD1 1 
ATOM   2340  C  CD2 . LEU C  1 35  ? 52.253  103.762 -23.413 1.00 22.00 ? 8   LEU C CD2 1 
ATOM   2341  N  N   . LYS C  1 36  ? 53.258  106.419 -27.549 1.00 17.91 ? 9   LYS C N   1 
ATOM   2342  C  CA  . LYS C  1 36  ? 53.512  106.635 -28.966 1.00 21.43 ? 9   LYS C CA  1 
ATOM   2343  C  C   . LYS C  1 36  ? 54.590  105.699 -29.383 1.00 20.45 ? 9   LYS C C   1 
ATOM   2344  O  O   . LYS C  1 36  ? 55.389  105.238 -28.575 1.00 17.53 ? 9   LYS C O   1 
ATOM   2345  C  CB  . LYS C  1 36  ? 54.045  108.050 -29.190 1.00 26.25 ? 9   LYS C CB  1 
ATOM   2346  C  CG  . LYS C  1 36  ? 52.966  109.084 -28.925 1.00 36.25 ? 9   LYS C CG  1 
ATOM   2347  C  CD  . LYS C  1 36  ? 53.463  110.496 -29.238 1.00 45.74 ? 9   LYS C CD  1 
ATOM   2348  C  CE  . LYS C  1 36  ? 52.307  111.511 -29.160 1.00 50.85 ? 9   LYS C CE  1 
ATOM   2349  N  NZ  . LYS C  1 36  ? 52.740  112.674 -28.313 1.00 50.91 ? 9   LYS C NZ  1 
ATOM   2350  N  N   . GLY C  1 37  ? 54.668  105.444 -30.672 1.00 21.41 ? 10  GLY C N   1 
ATOM   2351  C  CA  . GLY C  1 37  ? 55.775  104.612 -31.156 1.00 26.92 ? 10  GLY C CA  1 
ATOM   2352  C  C   . GLY C  1 37  ? 56.023  104.907 -32.635 1.00 27.36 ? 10  GLY C C   1 
ATOM   2353  O  O   . GLY C  1 37  ? 55.519  105.884 -33.168 1.00 26.87 ? 10  GLY C O   1 
ATOM   2354  N  N   . ASP C  1 38  ? 56.729  104.006 -33.286 1.00 28.31 ? 11  ASP C N   1 
ATOM   2355  C  CA  . ASP C  1 38  ? 57.122  104.231 -34.680 1.00 32.18 ? 11  ASP C CA  1 
ATOM   2356  C  C   . ASP C  1 38  ? 56.079  103.727 -35.654 1.00 29.49 ? 11  ASP C C   1 
ATOM   2357  O  O   . ASP C  1 38  ? 56.151  104.050 -36.835 1.00 32.47 ? 11  ASP C O   1 
ATOM   2358  C  CB  . ASP C  1 38  ? 58.444  103.529 -34.952 1.00 36.84 ? 11  ASP C CB  1 
ATOM   2359  C  CG  . ASP C  1 38  ? 59.609  104.221 -34.268 1.00 40.96 ? 11  ASP C CG  1 
ATOM   2360  O  OD1 . ASP C  1 38  ? 59.605  105.473 -34.161 1.00 44.00 ? 11  ASP C OD1 1 
ATOM   2361  O  OD2 . ASP C  1 38  ? 60.520  103.496 -33.829 1.00 52.63 ? 11  ASP C OD2 1 
ATOM   2362  N  N   . GLY C  1 39  ? 55.114  102.947 -35.179 1.00 24.79 ? 12  GLY C N   1 
ATOM   2363  C  CA  . GLY C  1 39  ? 54.073  102.426 -36.073 1.00 24.59 ? 12  GLY C CA  1 
ATOM   2364  C  C   . GLY C  1 39  ? 52.704  103.010 -35.734 1.00 24.65 ? 12  GLY C C   1 
ATOM   2365  O  O   . GLY C  1 39  ? 52.591  104.174 -35.315 1.00 24.38 ? 12  GLY C O   1 
ATOM   2366  N  N   . PRO C  1 40  ? 51.645  102.207 -35.923 1.00 20.04 ? 13  PRO C N   1 
ATOM   2367  C  CA  . PRO C  1 40  ? 50.275  102.712 -35.783 1.00 20.94 ? 13  PRO C CA  1 
ATOM   2368  C  C   . PRO C  1 40  ? 49.784  102.660 -34.327 1.00 18.44 ? 13  PRO C C   1 
ATOM   2369  O  O   . PRO C  1 40  ? 48.655  103.093 -34.054 1.00 18.95 ? 13  PRO C O   1 
ATOM   2370  C  CB  . PRO C  1 40  ? 49.466  101.724 -36.633 1.00 22.59 ? 13  PRO C CB  1 
ATOM   2371  C  CG  . PRO C  1 40  ? 50.201  100.434 -36.501 1.00 18.98 ? 13  PRO C CG  1 
ATOM   2372  C  CD  . PRO C  1 40  ? 51.678  100.848 -36.501 1.00 21.56 ? 13  PRO C CD  1 
ATOM   2373  N  N   . VAL C  1 41  ? 50.604  102.125 -33.408 1.00 17.80 ? 14  VAL C N   1 
ATOM   2374  C  CA  . VAL C  1 41  ? 50.111  101.958 -32.004 1.00 17.30 ? 14  VAL C CA  1 
ATOM   2375  C  C   . VAL C  1 41  ? 50.224  103.291 -31.236 1.00 17.78 ? 14  VAL C C   1 
ATOM   2376  O  O   . VAL C  1 41  ? 51.303  103.864 -31.188 1.00 17.90 ? 14  VAL C O   1 
ATOM   2377  C  CB  . VAL C  1 41  ? 50.867  100.843 -31.260 1.00 16.56 ? 14  VAL C CB  1 
ATOM   2378  C  CG1 . VAL C  1 41  ? 50.312  100.737 -29.802 1.00 16.62 ? 14  VAL C CG1 1 
ATOM   2379  C  CG2 . VAL C  1 41  ? 50.688  99.498  -32.015 1.00 17.44 ? 14  VAL C CG2 1 
ATOM   2380  N  N   . GLN C  1 42  ? 49.122  103.770 -30.658 1.00 18.67 ? 15  GLN C N   1 
ATOM   2381  C  CA  . GLN C  1 42  ? 49.173  104.934 -29.780 1.00 20.78 ? 15  GLN C CA  1 
ATOM   2382  C  C   . GLN C  1 42  ? 47.980  104.955 -28.865 1.00 19.50 ? 15  GLN C C   1 
ATOM   2383  O  O   . GLN C  1 42  ? 46.952  104.389 -29.167 1.00 19.38 ? 15  GLN C O   1 
ATOM   2384  C  CB  . GLN C  1 42  ? 49.236  106.260 -30.561 1.00 25.40 ? 15  GLN C CB  1 
ATOM   2385  C  CG  . GLN C  1 42  ? 48.224  106.373 -31.649 1.00 32.11 ? 15  GLN C CG  1 
ATOM   2386  C  CD  . GLN C  1 42  ? 48.320  107.706 -32.397 1.00 41.75 ? 15  GLN C CD  1 
ATOM   2387  O  OE1 . GLN C  1 42  ? 47.312  108.315 -32.676 1.00 43.05 ? 15  GLN C OE1 1 
ATOM   2388  N  NE2 . GLN C  1 42  ? 49.536  108.172 -32.677 1.00 49.35 ? 15  GLN C NE2 1 
ATOM   2389  N  N   . GLY C  1 43  ? 48.104  105.641 -27.736 1.00 19.69 ? 16  GLY C N   1 
ATOM   2390  C  CA  . GLY C  1 43  ? 46.993  105.673 -26.828 1.00 17.05 ? 16  GLY C CA  1 
ATOM   2391  C  C   . GLY C  1 43  ? 47.310  106.545 -25.628 1.00 17.09 ? 16  GLY C C   1 
ATOM   2392  O  O   . GLY C  1 43  ? 48.351  107.185 -25.583 1.00 16.21 ? 16  GLY C O   1 
ATOM   2393  N  N   . ILE C  1 44  ? 46.328  106.610 -24.739 1.00 15.96 ? 17  ILE C N   1 
ATOM   2394  C  CA  . ILE C  1 44  ? 46.433  107.400 -23.517 1.00 17.42 ? 17  ILE C CA  1 
ATOM   2395  C  C   . ILE C  1 44  ? 45.967  106.521 -22.389 1.00 15.32 ? 17  ILE C C   1 
ATOM   2396  O  O   . ILE C  1 44  ? 44.875  105.908 -22.453 1.00 15.27 ? 17  ILE C O   1 
ATOM   2397  C  CB  . ILE C  1 44  ? 45.579  108.707 -23.593 1.00 18.62 ? 17  ILE C CB  1 
ATOM   2398  C  CG1 . ILE C  1 44  ? 46.182  109.695 -24.619 1.00 21.17 ? 17  ILE C CG1 1 
ATOM   2399  C  CG2 . ILE C  1 44  ? 45.500  109.350 -22.186 1.00 18.79 ? 17  ILE C CG2 1 
ATOM   2400  C  CD1 . ILE C  1 44  ? 45.281  110.937 -24.871 1.00 25.08 ? 17  ILE C CD1 1 
ATOM   2401  N  N   . ILE C  1 45  ? 46.773  106.459 -21.316 1.00 15.99 ? 18  ILE C N   1 
ATOM   2402  C  CA  . ILE C  1 45  ? 46.424  105.594 -20.213 1.00 15.32 ? 18  ILE C CA  1 
ATOM   2403  C  C   . ILE C  1 45  ? 46.410  106.471 -18.942 1.00 16.00 ? 18  ILE C C   1 
ATOM   2404  O  O   . ILE C  1 45  ? 47.320  107.250 -18.721 1.00 15.92 ? 18  ILE C O   1 
ATOM   2405  C  CB  . ILE C  1 45  ? 47.436  104.413 -20.048 1.00 15.26 ? 18  ILE C CB  1 
ATOM   2406  C  CG1 . ILE C  1 45  ? 47.363  103.417 -21.273 1.00 13.62 ? 18  ILE C CG1 1 
ATOM   2407  C  CG2 . ILE C  1 45  ? 47.212  103.672 -18.727 1.00 12.94 ? 18  ILE C CG2 1 
ATOM   2408  C  CD1 . ILE C  1 45  ? 45.991  102.675 -21.409 1.00 15.91 ? 18  ILE C CD1 1 
ATOM   2409  N  N   . ASN C  1 46  ? 45.328  106.329 -18.164 1.00 15.91 ? 19  ASN C N   1 
ATOM   2410  C  CA  . ASN C  1 46  ? 45.169  107.093 -16.880 1.00 16.05 ? 19  ASN C CA  1 
ATOM   2411  C  C   . ASN C  1 46  ? 45.399  106.173 -15.708 1.00 16.12 ? 19  ASN C C   1 
ATOM   2412  O  O   . ASN C  1 46  ? 45.220  104.956 -15.840 1.00 15.14 ? 19  ASN C O   1 
ATOM   2413  C  CB  . ASN C  1 46  ? 43.727  107.663 -16.807 1.00 18.45 ? 19  ASN C CB  1 
ATOM   2414  C  CG  . ASN C  1 46  ? 43.371  108.437 -18.040 1.00 20.48 ? 19  ASN C CG  1 
ATOM   2415  O  OD1 . ASN C  1 46  ? 42.662  107.949 -18.952 1.00 24.22 ? 19  ASN C OD1 1 
ATOM   2416  N  ND2 . ASN C  1 46  ? 43.892  109.604 -18.115 1.00 18.71 ? 19  ASN C ND2 1 
ATOM   2417  N  N   . PHE C  1 47  ? 45.854  106.737 -14.568 1.00 16.33 ? 20  PHE C N   1 
ATOM   2418  C  CA  . PHE C  1 47  ? 46.068  105.977 -13.363 1.00 15.74 ? 20  PHE C CA  1 
ATOM   2419  C  C   . PHE C  1 47  ? 45.404  106.808 -12.274 1.00 17.29 ? 20  PHE C C   1 
ATOM   2420  O  O   . PHE C  1 47  ? 45.509  108.082 -12.285 1.00 18.00 ? 20  PHE C O   1 
ATOM   2421  C  CB  . PHE C  1 47  ? 47.556  105.922 -13.001 1.00 15.43 ? 20  PHE C CB  1 
ATOM   2422  C  CG  . PHE C  1 47  ? 48.415  105.232 -14.033 1.00 17.40 ? 20  PHE C CG  1 
ATOM   2423  C  CD1 . PHE C  1 47  ? 48.813  105.914 -15.202 1.00 17.16 ? 20  PHE C CD1 1 
ATOM   2424  C  CD2 . PHE C  1 47  ? 48.747  103.894 -13.876 1.00 17.29 ? 20  PHE C CD2 1 
ATOM   2425  C  CE1 . PHE C  1 47  ? 49.608  105.262 -16.170 1.00 18.60 ? 20  PHE C CE1 1 
ATOM   2426  C  CE2 . PHE C  1 47  ? 49.529  103.218 -14.855 1.00 17.38 ? 20  PHE C CE2 1 
ATOM   2427  C  CZ  . PHE C  1 47  ? 49.988  103.939 -15.977 1.00 17.40 ? 20  PHE C CZ  1 
ATOM   2428  N  N   . GLU C  1 48  ? 44.754  106.108 -11.353 1.00 16.58 ? 21  GLU C N   1 
ATOM   2429  C  CA  . GLU C  1 48  ? 44.184  106.831 -10.196 1.00 19.76 ? 21  GLU C CA  1 
ATOM   2430  C  C   . GLU C  1 48  ? 44.365  106.002 -8.956  1.00 18.44 ? 21  GLU C C   1 
ATOM   2431  O  O   . GLU C  1 48  ? 44.015  104.813 -8.959  1.00 18.43 ? 21  GLU C O   1 
ATOM   2432  C  CB  . GLU C  1 48  ? 42.679  107.129 -10.419 1.00 21.17 ? 21  GLU C CB  1 
ATOM   2433  C  CG  . GLU C  1 48  ? 42.075  107.869 -9.203  1.00 27.86 ? 21  GLU C CG  1 
ATOM   2434  C  CD  . GLU C  1 48  ? 40.775  108.594 -9.550  1.00 40.55 ? 21  GLU C CD  1 
ATOM   2435  O  OE1 . GLU C  1 48  ? 39.903  107.977 -10.191 1.00 39.28 ? 21  GLU C OE1 1 
ATOM   2436  O  OE2 . GLU C  1 48  ? 40.611  109.784 -9.165  1.00 46.76 ? 21  GLU C OE2 1 
ATOM   2437  N  N   . GLN C  1 49  ? 44.815  106.653 -7.869  1.00 17.80 ? 22  GLN C N   1 
ATOM   2438  C  CA  . GLN C  1 49  ? 44.970  105.964 -6.611  1.00 19.17 ? 22  GLN C CA  1 
ATOM   2439  C  C   . GLN C  1 49  ? 44.435  106.888 -5.521  1.00 22.81 ? 22  GLN C C   1 
ATOM   2440  O  O   . GLN C  1 49  ? 45.141  107.795 -5.096  1.00 24.94 ? 22  GLN C O   1 
ATOM   2441  C  CB  . GLN C  1 49  ? 46.438  105.593 -6.364  1.00 18.75 ? 22  GLN C CB  1 
ATOM   2442  C  CG  . GLN C  1 49  ? 46.663  104.698 -5.145  1.00 18.12 ? 22  GLN C CG  1 
ATOM   2443  C  CD  . GLN C  1 49  ? 48.137  104.510 -4.904  1.00 18.99 ? 22  GLN C CD  1 
ATOM   2444  O  OE1 . GLN C  1 49  ? 48.954  105.381 -5.261  1.00 20.52 ? 22  GLN C OE1 1 
ATOM   2445  N  NE2 . GLN C  1 49  ? 48.506  103.370 -4.338  1.00 20.16 ? 22  GLN C NE2 1 
ATOM   2446  N  N   . LYS C  1 50  ? 43.210  106.608 -5.115  1.00 26.30 ? 23  LYS C N   1 
ATOM   2447  C  CA  . LYS C  1 50  ? 42.476  107.413 -4.110  1.00 35.54 ? 23  LYS C CA  1 
ATOM   2448  C  C   . LYS C  1 50  ? 43.218  107.399 -2.763  1.00 31.80 ? 23  LYS C C   1 
ATOM   2449  O  O   . LYS C  1 50  ? 43.284  108.409 -2.075  1.00 34.62 ? 23  LYS C O   1 
ATOM   2450  C  CB  . LYS C  1 50  ? 41.069  106.840 -3.884  1.00 37.30 ? 23  LYS C CB  1 
ATOM   2451  C  CG  . LYS C  1 50  ? 40.341  106.245 -5.097  1.00 50.09 ? 23  LYS C CG  1 
ATOM   2452  C  CD  . LYS C  1 50  ? 39.204  107.148 -5.576  1.00 57.13 ? 23  LYS C CD  1 
ATOM   2453  C  CE  . LYS C  1 50  ? 39.625  108.624 -5.600  1.00 62.32 ? 23  LYS C CE  1 
ATOM   2454  N  NZ  . LYS C  1 50  ? 38.559  109.551 -6.093  1.00 71.74 ? 23  LYS C NZ  1 
ATOM   2455  N  N   . GLU C  1 51  ? 43.762  106.247 -2.388  1.00 26.67 ? 24  GLU C N   1 
ATOM   2456  C  CA  . GLU C  1 51  ? 44.409  106.081 -1.081  1.00 28.65 ? 24  GLU C CA  1 
ATOM   2457  C  C   . GLU C  1 51  ? 45.763  105.512 -1.299  1.00 28.34 ? 24  GLU C C   1 
ATOM   2458  O  O   . GLU C  1 51  ? 45.880  104.535 -2.049  1.00 25.29 ? 24  GLU C O   1 
ATOM   2459  C  CB  . GLU C  1 51  ? 43.610  105.041 -0.264  1.00 35.79 ? 24  GLU C CB  1 
ATOM   2460  C  CG  . GLU C  1 51  ? 42.094  105.186 -0.335  1.00 45.49 ? 24  GLU C CG  1 
ATOM   2461  C  CD  . GLU C  1 51  ? 41.593  106.470 0.327   1.00 60.01 ? 24  GLU C CD  1 
ATOM   2462  O  OE1 . GLU C  1 51  ? 42.311  106.996 1.220   1.00 66.18 ? 24  GLU C OE1 1 
ATOM   2463  O  OE2 . GLU C  1 51  ? 40.478  106.961 -0.027  1.00 66.38 ? 24  GLU C OE2 1 
ATOM   2464  N  N   . SER C  1 52  ? 46.773  106.001 -0.566  1.00 29.77 ? 25  SER C N   1 
ATOM   2465  C  CA  . SER C  1 52  ? 48.119  105.508 -0.777  1.00 32.77 ? 25  SER C CA  1 
ATOM   2466  C  C   . SER C  1 52  ? 48.281  104.042 -0.400  1.00 30.52 ? 25  SER C C   1 
ATOM   2467  O  O   . SER C  1 52  ? 49.132  103.362 -0.946  1.00 30.57 ? 25  SER C O   1 
ATOM   2468  C  CB  . SER C  1 52  ? 49.142  106.409 -0.088  1.00 37.06 ? 25  SER C CB  1 
ATOM   2469  O  OG  . SER C  1 52  ? 49.049  106.217 1.312   1.00 38.06 ? 25  SER C OG  1 
ATOM   2470  N  N   . ASN C  1 53  ? 47.435  103.530 0.484   1.00 29.61 ? 26  ASN C N   1 
ATOM   2471  C  CA  . ASN C  1 53  ? 47.468  102.070 0.818   1.00 33.07 ? 26  ASN C CA  1 
ATOM   2472  C  C   . ASN C  1 53  ? 46.499  101.205 -0.019  1.00 33.49 ? 26  ASN C C   1 
ATOM   2473  O  O   . ASN C  1 53  ? 46.085  100.087 0.404   1.00 34.99 ? 26  ASN C O   1 
ATOM   2474  C  CB  . ASN C  1 53  ? 47.175  101.834 2.306   1.00 35.52 ? 26  ASN C CB  1 
ATOM   2475  C  CG  . ASN C  1 53  ? 45.740  102.228 2.698   1.00 39.48 ? 26  ASN C CG  1 
ATOM   2476  O  OD1 . ASN C  1 53  ? 45.063  102.986 1.981   1.00 40.13 ? 26  ASN C OD1 1 
ATOM   2477  N  ND2 . ASN C  1 53  ? 45.270  101.708 3.831   1.00 38.07 ? 26  ASN C ND2 1 
ATOM   2478  N  N   . GLY C  1 54  ? 46.053  101.751 -1.146  1.00 29.88 ? 27  GLY C N   1 
ATOM   2479  C  CA  . GLY C  1 54  ? 45.009  101.076 -1.905  1.00 28.28 ? 27  GLY C CA  1 
ATOM   2480  C  C   . GLY C  1 54  ? 45.440  100.888 -3.380  1.00 22.99 ? 27  GLY C C   1 
ATOM   2481  O  O   . GLY C  1 54  ? 46.510  101.336 -3.791  1.00 23.16 ? 27  GLY C O   1 
ATOM   2482  N  N   . PRO C  1 55  ? 44.561  100.255 -4.166  1.00 23.14 ? 28  PRO C N   1 
ATOM   2483  C  CA  . PRO C  1 55  ? 44.879  99.877  -5.526  1.00 23.11 ? 28  PRO C CA  1 
ATOM   2484  C  C   . PRO C  1 55  ? 44.942  101.077 -6.444  1.00 21.67 ? 28  PRO C C   1 
ATOM   2485  O  O   . PRO C  1 55  ? 44.376  102.144 -6.164  1.00 20.22 ? 28  PRO C O   1 
ATOM   2486  C  CB  . PRO C  1 55  ? 43.689  98.971  -5.958  1.00 24.95 ? 28  PRO C CB  1 
ATOM   2487  C  CG  . PRO C  1 55  ? 42.823  98.771  -4.766  1.00 26.23 ? 28  PRO C CG  1 
ATOM   2488  C  CD  . PRO C  1 55  ? 43.243  99.770  -3.704  1.00 27.10 ? 28  PRO C CD  1 
ATOM   2489  N  N   . VAL C  1 56  ? 45.633  100.874 -7.559  1.00 19.00 ? 29  VAL C N   1 
ATOM   2490  C  CA  . VAL C  1 56  ? 45.714  101.867 -8.605  1.00 17.04 ? 29  VAL C CA  1 
ATOM   2491  C  C   . VAL C  1 56  ? 44.800  101.362 -9.710  1.00 18.07 ? 29  VAL C C   1 
ATOM   2492  O  O   . VAL C  1 56  ? 44.917  100.201 -10.134 1.00 18.26 ? 29  VAL C O   1 
ATOM   2493  C  CB  . VAL C  1 56  ? 47.157  101.982 -9.147  1.00 15.75 ? 29  VAL C CB  1 
ATOM   2494  C  CG1 . VAL C  1 56  ? 47.236  103.108 -10.226 1.00 15.26 ? 29  VAL C CG1 1 
ATOM   2495  C  CG2 . VAL C  1 56  ? 48.074  102.348 -7.968  1.00 17.19 ? 29  VAL C CG2 1 
ATOM   2496  N  N   . LYS C  1 57  ? 43.862  102.194 -10.127 1.00 17.42 ? 30  LYS C N   1 
ATOM   2497  C  CA  . LYS C  1 57  ? 43.042  101.878 -11.275 1.00 19.57 ? 30  LYS C CA  1 
ATOM   2498  C  C   . LYS C  1 57  ? 43.751  102.414 -12.520 1.00 17.47 ? 30  LYS C C   1 
ATOM   2499  O  O   . LYS C  1 57  ? 44.278  103.530 -12.536 1.00 18.24 ? 30  LYS C O   1 
ATOM   2500  C  CB  . LYS C  1 57  ? 41.668  102.556 -11.153 1.00 23.02 ? 30  LYS C CB  1 
ATOM   2501  C  CG  . LYS C  1 57  ? 40.894  102.069 -9.946  1.00 29.49 ? 30  LYS C CG  1 
ATOM   2502  C  CD  . LYS C  1 57  ? 39.413  102.428 -9.989  1.00 43.78 ? 30  LYS C CD  1 
ATOM   2503  C  CE  . LYS C  1 57  ? 38.714  101.854 -8.749  1.00 50.78 ? 30  LYS C CE  1 
ATOM   2504  N  NZ  . LYS C  1 57  ? 37.397  102.518 -8.501  1.00 58.95 ? 30  LYS C NZ  1 
ATOM   2505  N  N   . VAL C  1 58  ? 43.775  101.591 -13.553 1.00 16.46 ? 31  VAL C N   1 
ATOM   2506  C  CA  . VAL C  1 58  ? 44.503  101.899 -14.781 1.00 15.57 ? 31  VAL C CA  1 
ATOM   2507  C  C   . VAL C  1 58  ? 43.506  101.745 -15.928 1.00 16.43 ? 31  VAL C C   1 
ATOM   2508  O  O   . VAL C  1 58  ? 42.955  100.662 -16.096 1.00 17.90 ? 31  VAL C O   1 
ATOM   2509  C  CB  . VAL C  1 58  ? 45.660  100.884 -14.963 1.00 14.49 ? 31  VAL C CB  1 
ATOM   2510  C  CG1 . VAL C  1 58  ? 46.494  101.282 -16.194 1.00 14.22 ? 31  VAL C CG1 1 
ATOM   2511  C  CG2 . VAL C  1 58  ? 46.536  100.898 -13.711 1.00 13.41 ? 31  VAL C CG2 1 
ATOM   2512  N  N   . TRP C  1 59  ? 43.293  102.806 -16.717 1.00 16.84 ? 32  TRP C N   1 
ATOM   2513  C  CA  . TRP C  1 59  ? 42.281  102.711 -17.794 1.00 17.72 ? 32  TRP C CA  1 
ATOM   2514  C  C   . TRP C  1 59  ? 42.601  103.662 -18.928 1.00 16.43 ? 32  TRP C C   1 
ATOM   2515  O  O   . TRP C  1 59  ? 43.281  104.674 -18.746 1.00 17.92 ? 32  TRP C O   1 
ATOM   2516  C  CB  . TRP C  1 59  ? 40.830  102.938 -17.252 1.00 19.78 ? 32  TRP C CB  1 
ATOM   2517  C  CG  . TRP C  1 59  ? 40.532  104.417 -17.036 1.00 23.37 ? 32  TRP C CG  1 
ATOM   2518  C  CD1 . TRP C  1 59  ? 39.890  105.275 -17.901 1.00 25.74 ? 32  TRP C CD1 1 
ATOM   2519  C  CD2 . TRP C  1 59  ? 40.919  105.195 -15.917 1.00 25.72 ? 32  TRP C CD2 1 
ATOM   2520  N  NE1 . TRP C  1 59  ? 39.844  106.527 -17.364 1.00 25.64 ? 32  TRP C NE1 1 
ATOM   2521  C  CE2 . TRP C  1 59  ? 40.442  106.506 -16.130 1.00 25.49 ? 32  TRP C CE2 1 
ATOM   2522  C  CE3 . TRP C  1 59  ? 41.616  104.911 -14.746 1.00 26.87 ? 32  TRP C CE3 1 
ATOM   2523  C  CZ2 . TRP C  1 59  ? 40.658  107.544 -15.223 1.00 29.68 ? 32  TRP C CZ2 1 
ATOM   2524  C  CZ3 . TRP C  1 59  ? 41.841  105.967 -13.824 1.00 31.36 ? 32  TRP C CZ3 1 
ATOM   2525  C  CH2 . TRP C  1 59  ? 41.345  107.261 -14.072 1.00 33.11 ? 32  TRP C CH2 1 
ATOM   2526  N  N   . GLY C  1 60  ? 42.076  103.368 -20.106 1.00 18.20 ? 33  GLY C N   1 
ATOM   2527  C  CA  . GLY C  1 60  ? 42.306  104.279 -21.240 1.00 17.74 ? 33  GLY C CA  1 
ATOM   2528  C  C   . GLY C  1 60  ? 42.154  103.452 -22.507 1.00 18.54 ? 33  GLY C C   1 
ATOM   2529  O  O   . GLY C  1 60  ? 41.626  102.358 -22.484 1.00 22.39 ? 33  GLY C O   1 
ATOM   2530  N  N   . SER C  1 61  ? 42.605  103.991 -23.621 1.00 19.69 ? 34  SER C N   1 
ATOM   2531  C  CA  . SER C  1 61  ? 42.378  103.311 -24.896 1.00 20.48 ? 34  SER C CA  1 
ATOM   2532  C  C   . SER C  1 61  ? 43.676  103.324 -25.696 1.00 19.38 ? 34  SER C C   1 
ATOM   2533  O  O   . SER C  1 61  ? 44.359  104.332 -25.717 1.00 19.61 ? 34  SER C O   1 
ATOM   2534  C  CB  . SER C  1 61  ? 41.299  104.087 -25.644 1.00 24.28 ? 34  SER C CB  1 
ATOM   2535  O  OG  . SER C  1 61  ? 40.998  103.315 -26.774 1.00 34.07 ? 34  SER C OG  1 
ATOM   2536  N  N   . ILE C  1 62  ? 44.044  102.193 -26.315 1.00 17.28 ? 35  ILE C N   1 
ATOM   2537  C  CA  . ILE C  1 62  ? 45.214  102.161 -27.186 1.00 16.31 ? 35  ILE C CA  1 
ATOM   2538  C  C   . ILE C  1 62  ? 44.696  101.592 -28.530 1.00 17.75 ? 35  ILE C C   1 
ATOM   2539  O  O   . ILE C  1 62  ? 43.964  100.587 -28.532 1.00 17.61 ? 35  ILE C O   1 
ATOM   2540  C  CB  . ILE C  1 62  ? 46.277  101.186 -26.649 1.00 18.02 ? 35  ILE C CB  1 
ATOM   2541  C  CG1 . ILE C  1 62  ? 46.626  101.489 -25.168 1.00 18.58 ? 35  ILE C CG1 1 
ATOM   2542  C  CG2 . ILE C  1 62  ? 47.495  101.195 -27.563 1.00 16.25 ? 35  ILE C CG2 1 
ATOM   2543  C  CD1 . ILE C  1 62  ? 47.492  100.424 -24.479 1.00 21.07 ? 35  ILE C CD1 1 
ATOM   2544  N  N   . LYS C  1 63  ? 45.073  102.233 -29.636 1.00 17.45 ? 36  LYS C N   1 
ATOM   2545  C  CA  . LYS C  1 63  ? 44.651  101.769 -30.952 1.00 19.65 ? 36  LYS C CA  1 
ATOM   2546  C  C   . LYS C  1 63  ? 45.823  101.293 -31.774 1.00 17.93 ? 36  LYS C C   1 
ATOM   2547  O  O   . LYS C  1 63  ? 46.969  101.497 -31.412 1.00 17.54 ? 36  LYS C O   1 
ATOM   2548  C  CB  . LYS C  1 63  ? 43.891  102.877 -31.671 1.00 22.93 ? 36  LYS C CB  1 
ATOM   2549  C  CG  . LYS C  1 63  ? 44.792  104.026 -32.028 1.00 28.37 ? 36  LYS C CG  1 
ATOM   2550  C  CD  . LYS C  1 63  ? 43.951  104.991 -32.837 1.00 39.24 ? 36  LYS C CD  1 
ATOM   2551  C  CE  . LYS C  1 63  ? 44.794  105.958 -33.635 1.00 45.54 ? 36  LYS C CE  1 
ATOM   2552  N  NZ  . LYS C  1 63  ? 43.846  107.076 -33.960 1.00 52.65 ? 36  LYS C NZ  1 
ATOM   2553  N  N   . GLY C  1 64  ? 45.539  100.603 -32.890 1.00 17.05 ? 37  GLY C N   1 
ATOM   2554  C  CA  . GLY C  1 64  ? 46.608  100.181 -33.778 1.00 17.20 ? 37  GLY C CA  1 
ATOM   2555  C  C   . GLY C  1 64  ? 47.185  98.824  -33.472 1.00 18.51 ? 37  GLY C C   1 
ATOM   2556  O  O   . GLY C  1 64  ? 48.190  98.430  -34.072 1.00 18.86 ? 37  GLY C O   1 
ATOM   2557  N  N   . LEU C  1 65  ? 46.566  98.094  -32.524 1.00 16.18 ? 38  LEU C N   1 
ATOM   2558  C  CA  . LEU C  1 65  ? 47.127  96.852  -32.071 1.00 15.92 ? 38  LEU C CA  1 
ATOM   2559  C  C   . LEU C  1 65  ? 46.518  95.652  -32.811 1.00 16.72 ? 38  LEU C C   1 
ATOM   2560  O  O   . LEU C  1 65  ? 45.331  95.661  -33.093 1.00 17.58 ? 38  LEU C O   1 
ATOM   2561  C  CB  . LEU C  1 65  ? 46.791  96.656  -30.553 1.00 14.93 ? 38  LEU C CB  1 
ATOM   2562  C  CG  . LEU C  1 65  ? 47.591  97.617  -29.615 1.00 15.90 ? 38  LEU C CG  1 
ATOM   2563  C  CD1 . LEU C  1 65  ? 46.854  97.588  -28.262 1.00 16.74 ? 38  LEU C CD1 1 
ATOM   2564  C  CD2 . LEU C  1 65  ? 49.022  97.113  -29.423 1.00 15.32 ? 38  LEU C CD2 1 
ATOM   2565  N  N   . THR C  1 66  ? 47.315  94.616  -33.066 1.00 18.57 ? 39  THR C N   1 
ATOM   2566  C  CA  . THR C  1 66  ? 46.746  93.381  -33.582 1.00 17.63 ? 39  THR C CA  1 
ATOM   2567  C  C   . THR C  1 66  ? 45.799  92.763  -32.563 1.00 19.51 ? 39  THR C C   1 
ATOM   2568  O  O   . THR C  1 66  ? 46.056  92.809  -31.342 1.00 18.84 ? 39  THR C O   1 
ATOM   2569  C  CB  . THR C  1 66  ? 47.818  92.349  -33.945 1.00 19.51 ? 39  THR C CB  1 
ATOM   2570  O  OG1 . THR C  1 66  ? 48.608  92.100  -32.795 1.00 21.11 ? 39  THR C OG1 1 
ATOM   2571  C  CG2 . THR C  1 66  ? 48.718  92.909  -35.014 1.00 20.85 ? 39  THR C CG2 1 
ATOM   2572  N  N   . GLU C  1 67  ? 44.668  92.235  -33.054 1.00 19.08 ? 40  GLU C N   1 
ATOM   2573  C  CA  . GLU C  1 67  ? 43.617  91.634  -32.189 1.00 18.36 ? 40  GLU C CA  1 
ATOM   2574  C  C   . GLU C  1 67  ? 44.227  90.604  -31.274 1.00 20.58 ? 40  GLU C C   1 
ATOM   2575  O  O   . GLU C  1 67  ? 45.138  89.819  -31.681 1.00 21.46 ? 40  GLU C O   1 
ATOM   2576  C  CB  . GLU C  1 67  ? 42.560  90.940  -33.085 1.00 24.12 ? 40  GLU C CB  1 
ATOM   2577  C  CG  . GLU C  1 67  ? 41.423  90.332  -32.286 1.00 27.65 ? 40  GLU C CG  1 
ATOM   2578  C  CD  . GLU C  1 67  ? 40.210  89.865  -33.130 1.00 37.57 ? 40  GLU C CD  1 
ATOM   2579  O  OE1 . GLU C  1 67  ? 40.284  89.877  -34.390 1.00 38.95 ? 40  GLU C OE1 1 
ATOM   2580  O  OE2 . GLU C  1 67  ? 39.172  89.536  -32.486 1.00 42.33 ? 40  GLU C OE2 1 
ATOM   2581  N  N   . GLY C  1 68  ? 43.839  90.649  -30.006 1.00 19.36 ? 41  GLY C N   1 
ATOM   2582  C  CA  . GLY C  1 68  ? 44.325  89.626  -29.062 1.00 22.07 ? 41  GLY C CA  1 
ATOM   2583  C  C   . GLY C  1 68  ? 45.160  90.262  -27.945 1.00 20.55 ? 41  GLY C C   1 
ATOM   2584  O  O   . GLY C  1 68  ? 45.113  91.489  -27.744 1.00 19.08 ? 41  GLY C O   1 
ATOM   2585  N  N   . LEU C  1 69  ? 45.980  89.435  -27.292 1.00 18.28 ? 42  LEU C N   1 
ATOM   2586  C  CA  . LEU C  1 69  ? 46.702  89.838  -26.069 1.00 17.69 ? 42  LEU C CA  1 
ATOM   2587  C  C   . LEU C  1 69  ? 48.024  90.537  -26.364 1.00 17.08 ? 42  LEU C C   1 
ATOM   2588  O  O   . LEU C  1 69  ? 48.791  90.080  -27.226 1.00 15.13 ? 42  LEU C O   1 
ATOM   2589  C  CB  . LEU C  1 69  ? 47.013  88.555  -25.273 1.00 18.77 ? 42  LEU C CB  1 
ATOM   2590  C  CG  . LEU C  1 69  ? 45.841  87.752  -24.657 1.00 21.27 ? 42  LEU C CG  1 
ATOM   2591  C  CD1 . LEU C  1 69  ? 46.399  86.423  -24.128 1.00 23.19 ? 42  LEU C CD1 1 
ATOM   2592  C  CD2 . LEU C  1 69  ? 45.172  88.513  -23.518 1.00 19.52 ? 42  LEU C CD2 1 
ATOM   2593  N  N   . HIS C  1 70  ? 48.354  91.553  -25.560 1.00 14.57 ? 43  HIS C N   1 
ATOM   2594  C  CA  . HIS C  1 70  ? 49.623  92.278  -25.672 1.00 13.95 ? 43  HIS C CA  1 
ATOM   2595  C  C   . HIS C  1 70  ? 50.151  92.555  -24.280 1.00 13.43 ? 43  HIS C C   1 
ATOM   2596  O  O   . HIS C  1 70  ? 49.419  93.083  -23.432 1.00 12.96 ? 43  HIS C O   1 
ATOM   2597  C  CB  . HIS C  1 70  ? 49.410  93.615  -26.408 1.00 14.23 ? 43  HIS C CB  1 
ATOM   2598  C  CG  . HIS C  1 70  ? 49.059  93.422  -27.854 1.00 16.05 ? 43  HIS C CG  1 
ATOM   2599  N  ND1 . HIS C  1 70  ? 50.018  93.343  -28.838 1.00 16.32 ? 43  HIS C ND1 1 
ATOM   2600  C  CD2 . HIS C  1 70  ? 47.858  93.257  -28.467 1.00 14.97 ? 43  HIS C CD2 1 
ATOM   2601  C  CE1 . HIS C  1 70  ? 49.416  93.170  -30.013 1.00 17.17 ? 43  HIS C CE1 1 
ATOM   2602  N  NE2 . HIS C  1 70  ? 48.103  93.117  -29.811 1.00 16.92 ? 43  HIS C NE2 1 
ATOM   2603  N  N   . GLY C  1 71  ? 51.414  92.217  -24.052 1.00 12.86 ? 44  GLY C N   1 
ATOM   2604  C  CA  . GLY C  1 71  ? 52.045  92.484  -22.746 1.00 13.93 ? 44  GLY C CA  1 
ATOM   2605  C  C   . GLY C  1 71  ? 52.022  94.010  -22.453 1.00 14.05 ? 44  GLY C C   1 
ATOM   2606  O  O   . GLY C  1 71  ? 52.133  94.828  -23.349 1.00 13.58 ? 44  GLY C O   1 
ATOM   2607  N  N   . PHE C  1 72  ? 51.869  94.351  -21.187 1.00 12.28 ? 45  PHE C N   1 
ATOM   2608  C  CA  . PHE C  1 72  ? 51.575  95.728  -20.774 1.00 13.92 ? 45  PHE C CA  1 
ATOM   2609  C  C   . PHE C  1 72  ? 52.336  95.917  -19.468 1.00 13.57 ? 45  PHE C C   1 
ATOM   2610  O  O   . PHE C  1 72  ? 51.914  95.376  -18.430 1.00 13.96 ? 45  PHE C O   1 
ATOM   2611  C  CB  . PHE C  1 72  ? 50.029  95.889  -20.591 1.00 14.10 ? 45  PHE C CB  1 
ATOM   2612  C  CG  . PHE C  1 72  ? 49.573  97.271  -20.300 1.00 13.92 ? 45  PHE C CG  1 
ATOM   2613  C  CD1 . PHE C  1 72  ? 49.587  98.272  -21.286 1.00 15.47 ? 45  PHE C CD1 1 
ATOM   2614  C  CD2 . PHE C  1 72  ? 48.983  97.555  -19.076 1.00 15.39 ? 45  PHE C CD2 1 
ATOM   2615  C  CE1 . PHE C  1 72  ? 49.044  99.542  -21.002 1.00 15.50 ? 45  PHE C CE1 1 
ATOM   2616  C  CE2 . PHE C  1 72  ? 48.485  98.826  -18.795 1.00 17.18 ? 45  PHE C CE2 1 
ATOM   2617  C  CZ  . PHE C  1 72  ? 48.468  99.812  -19.784 1.00 16.11 ? 45  PHE C CZ  1 
ATOM   2618  N  N   . HIS C  1 73  ? 53.465  96.632  -19.520 1.00 12.76 ? 46  HIS C N   1 
ATOM   2619  C  CA  . HIS C  1 73  ? 54.381  96.673  -18.353 1.00 14.44 ? 46  HIS C CA  1 
ATOM   2620  C  C   . HIS C  1 73  ? 54.938  98.016  -18.068 1.00 14.81 ? 46  HIS C C   1 
ATOM   2621  O  O   . HIS C  1 73  ? 55.081  98.822  -18.970 1.00 15.78 ? 46  HIS C O   1 
ATOM   2622  C  CB  . HIS C  1 73  ? 55.607  95.816  -18.624 1.00 15.64 ? 46  HIS C CB  1 
ATOM   2623  C  CG  . HIS C  1 73  ? 55.254  94.441  -19.092 1.00 16.84 ? 46  HIS C CG  1 
ATOM   2624  N  ND1 . HIS C  1 73  ? 55.646  93.944  -20.303 1.00 20.25 ? 46  HIS C ND1 1 
ATOM   2625  C  CD2 . HIS C  1 73  ? 54.507  93.478  -18.510 1.00 16.53 ? 46  HIS C CD2 1 
ATOM   2626  C  CE1 . HIS C  1 73  ? 55.192  92.704  -20.441 1.00 18.75 ? 46  HIS C CE1 1 
ATOM   2627  N  NE2 . HIS C  1 73  ? 54.453  92.417  -19.381 1.00 19.33 ? 46  HIS C NE2 1 
ATOM   2628  N  N   . VAL C  1 74  ? 55.289  98.221  -16.798 1.00 14.75 ? 47  VAL C N   1 
ATOM   2629  C  CA  . VAL C  1 74  ? 55.963  99.436  -16.404 1.00 14.43 ? 47  VAL C CA  1 
ATOM   2630  C  C   . VAL C  1 74  ? 57.436  99.029  -16.380 1.00 15.00 ? 47  VAL C C   1 
ATOM   2631  O  O   . VAL C  1 74  ? 57.812  98.048  -15.708 1.00 16.21 ? 47  VAL C O   1 
ATOM   2632  C  CB  . VAL C  1 74  ? 55.562  99.926  -15.011 1.00 14.24 ? 47  VAL C CB  1 
ATOM   2633  C  CG1 . VAL C  1 74  ? 56.333  101.248 -14.720 1.00 15.36 ? 47  VAL C CG1 1 
ATOM   2634  C  CG2 . VAL C  1 74  ? 54.061  100.233 -14.983 1.00 15.04 ? 47  VAL C CG2 1 
ATOM   2635  N  N   . HIS C  1 75  ? 58.245  99.758  -17.144 1.00 14.74 ? 48  HIS C N   1 
ATOM   2636  C  CA  . HIS C  1 75  ? 59.684  99.533  -17.255 1.00 14.41 ? 48  HIS C CA  1 
ATOM   2637  C  C   . HIS C  1 75  ? 60.402  100.562 -16.370 1.00 16.12 ? 48  HIS C C   1 
ATOM   2638  O  O   . HIS C  1 75  ? 59.841  101.577 -16.023 1.00 17.12 ? 48  HIS C O   1 
ATOM   2639  C  CB  . HIS C  1 75  ? 60.153  99.673  -18.727 1.00 15.31 ? 48  HIS C CB  1 
ATOM   2640  C  CG  . HIS C  1 75  ? 59.710  98.534  -19.620 1.00 15.72 ? 48  HIS C CG  1 
ATOM   2641  N  ND1 . HIS C  1 75  ? 60.600  97.655  -20.193 1.00 15.62 ? 48  HIS C ND1 1 
ATOM   2642  C  CD2 . HIS C  1 75  ? 58.465  98.080  -19.947 1.00 15.96 ? 48  HIS C CD2 1 
ATOM   2643  C  CE1 . HIS C  1 75  ? 59.926  96.746  -20.906 1.00 17.20 ? 48  HIS C CE1 1 
ATOM   2644  N  NE2 . HIS C  1 75  ? 58.628  96.992  -20.775 1.00 15.04 ? 48  HIS C NE2 1 
ATOM   2645  N  N   . GLU C  1 76  ? 61.652  100.249 -16.003 1.00 16.38 ? 49  GLU C N   1 
ATOM   2646  C  CA  . GLU C  1 76  ? 62.343  100.892 -14.914 1.00 17.07 ? 49  GLU C CA  1 
ATOM   2647  C  C   . GLU C  1 76  ? 62.610  102.410 -15.168 1.00 17.68 ? 49  GLU C C   1 
ATOM   2648  O  O   . GLU C  1 76  ? 62.372  103.223 -14.291 1.00 18.21 ? 49  GLU C O   1 
ATOM   2649  C  CB  . GLU C  1 76  ? 63.681  100.158 -14.678 1.00 19.10 ? 49  GLU C CB  1 
ATOM   2650  C  CG  . GLU C  1 76  ? 64.424  100.787 -13.484 1.00 22.44 ? 49  GLU C CG  1 
ATOM   2651  C  CD  . GLU C  1 76  ? 65.658  99.966  -13.119 1.00 26.97 ? 49  GLU C CD  1 
ATOM   2652  O  OE1 . GLU C  1 76  ? 65.990  99.023  -13.854 1.00 26.45 ? 49  GLU C OE1 1 
ATOM   2653  O  OE2 . GLU C  1 76  ? 66.316  100.313 -12.138 1.00 28.97 ? 49  GLU C OE2 1 
ATOM   2654  N  N   . PHE C  1 77  ? 63.055  102.765 -16.356 1.00 16.86 ? 50  PHE C N   1 
ATOM   2655  C  CA  . PHE C  1 77  ? 63.458  104.174 -16.612 1.00 18.13 ? 50  PHE C CA  1 
ATOM   2656  C  C   . PHE C  1 77  ? 62.480  104.993 -17.442 1.00 18.30 ? 50  PHE C C   1 
ATOM   2657  O  O   . PHE C  1 77  ? 61.963  104.497 -18.419 1.00 19.59 ? 50  PHE C O   1 
ATOM   2658  C  CB  . PHE C  1 77  ? 64.812  104.186 -17.297 1.00 19.13 ? 50  PHE C CB  1 
ATOM   2659  C  CG  . PHE C  1 77  ? 65.838  103.371 -16.561 1.00 20.94 ? 50  PHE C CG  1 
ATOM   2660  C  CD1 . PHE C  1 77  ? 66.171  103.690 -15.247 1.00 22.78 ? 50  PHE C CD1 1 
ATOM   2661  C  CD2 . PHE C  1 77  ? 66.398  102.255 -17.169 1.00 22.51 ? 50  PHE C CD2 1 
ATOM   2662  C  CE1 . PHE C  1 77  ? 67.118  102.917 -14.547 1.00 24.80 ? 50  PHE C CE1 1 
ATOM   2663  C  CE2 . PHE C  1 77  ? 67.349  101.476 -16.477 1.00 26.56 ? 50  PHE C CE2 1 
ATOM   2664  C  CZ  . PHE C  1 77  ? 67.684  101.800 -15.168 1.00 23.39 ? 50  PHE C CZ  1 
ATOM   2665  N  N   . GLY C  1 78  ? 62.301  106.255 -17.082 1.00 17.08 ? 51  GLY C N   1 
ATOM   2666  C  CA  . GLY C  1 78  ? 61.464  107.196 -17.834 1.00 18.42 ? 51  GLY C CA  1 
ATOM   2667  C  C   . GLY C  1 78  ? 62.330  107.882 -18.870 1.00 21.56 ? 51  GLY C C   1 
ATOM   2668  O  O   . GLY C  1 78  ? 62.341  109.099 -18.961 1.00 20.99 ? 51  GLY C O   1 
ATOM   2669  N  N   . ASP C  1 79  ? 63.146  107.095 -19.562 1.00 22.98 ? 52  ASP C N   1 
ATOM   2670  C  CA  . ASP C  1 79  ? 64.163  107.609 -20.509 1.00 22.14 ? 52  ASP C CA  1 
ATOM   2671  C  C   . ASP C  1 79  ? 63.749  107.178 -21.927 1.00 21.55 ? 52  ASP C C   1 
ATOM   2672  O  O   . ASP C  1 79  ? 63.801  105.988 -22.295 1.00 22.54 ? 52  ASP C O   1 
ATOM   2673  C  CB  . ASP C  1 79  ? 65.513  106.975 -20.146 1.00 22.08 ? 52  ASP C CB  1 
ATOM   2674  C  CG  . ASP C  1 79  ? 66.672  107.485 -21.034 1.00 26.04 ? 52  ASP C CG  1 
ATOM   2675  O  OD1 . ASP C  1 79  ? 66.457  107.929 -22.158 1.00 24.34 ? 52  ASP C OD1 1 
ATOM   2676  O  OD2 . ASP C  1 79  ? 67.815  107.389 -20.596 1.00 25.34 ? 52  ASP C OD2 1 
ATOM   2677  N  N   . ASN C  1 80  ? 63.333  108.138 -22.715 1.00 20.23 ? 53  ASN C N   1 
ATOM   2678  C  CA  . ASN C  1 80  ? 62.900  107.900 -24.097 1.00 23.43 ? 53  ASN C CA  1 
ATOM   2679  C  C   . ASN C  1 80  ? 63.965  108.429 -25.092 1.00 24.48 ? 53  ASN C C   1 
ATOM   2680  O  O   . ASN C  1 80  ? 63.669  108.659 -26.257 1.00 25.12 ? 53  ASN C O   1 
ATOM   2681  C  CB  . ASN C  1 80  ? 61.572  108.669 -24.299 1.00 31.03 ? 53  ASN C CB  1 
ATOM   2682  C  CG  . ASN C  1 80  ? 60.993  108.550 -25.720 1.00 39.43 ? 53  ASN C CG  1 
ATOM   2683  O  OD1 . ASN C  1 80  ? 60.685  109.569 -26.388 1.00 46.95 ? 53  ASN C OD1 1 
ATOM   2684  N  ND2 . ASN C  1 80  ? 60.787  107.332 -26.165 1.00 39.01 ? 53  ASN C ND2 1 
ATOM   2685  N  N   . THR C  1 81  ? 65.201  108.576 -24.648 1.00 24.29 ? 54  THR C N   1 
ATOM   2686  C  CA  . THR C  1 81  ? 66.215  109.111 -25.574 1.00 24.19 ? 54  THR C CA  1 
ATOM   2687  C  C   . THR C  1 81  ? 66.486  108.212 -26.763 1.00 29.29 ? 54  THR C C   1 
ATOM   2688  O  O   . THR C  1 81  ? 66.822  108.709 -27.830 1.00 26.65 ? 54  THR C O   1 
ATOM   2689  C  CB  . THR C  1 81  ? 67.538  109.449 -24.909 1.00 26.01 ? 54  THR C CB  1 
ATOM   2690  O  OG1 . THR C  1 81  ? 68.054  108.296 -24.232 1.00 22.93 ? 54  THR C OG1 1 
ATOM   2691  C  CG2 . THR C  1 81  ? 67.339  110.581 -23.925 1.00 23.94 ? 54  THR C CG2 1 
ATOM   2692  N  N   . ALA C  1 82  ? 66.349  106.897 -26.611 1.00 24.84 ? 55  ALA C N   1 
ATOM   2693  C  CA  . ALA C  1 82  ? 66.488  106.030 -27.769 1.00 27.36 ? 55  ALA C CA  1 
ATOM   2694  C  C   . ALA C  1 82  ? 65.147  105.308 -27.965 1.00 30.78 ? 55  ALA C C   1 
ATOM   2695  O  O   . ALA C  1 82  ? 65.108  104.098 -28.095 1.00 32.23 ? 55  ALA C O   1 
ATOM   2696  C  CB  . ALA C  1 82  ? 67.628  105.021 -27.536 1.00 30.07 ? 55  ALA C CB  1 
ATOM   2697  N  N   . GLY C  1 83  ? 64.050  106.053 -27.928 1.00 27.58 ? 56  GLY C N   1 
ATOM   2698  C  CA  . GLY C  1 83  ? 62.723  105.456 -28.080 1.00 24.11 ? 56  GLY C CA  1 
ATOM   2699  C  C   . GLY C  1 83  ? 62.477  104.526 -26.883 1.00 23.46 ? 56  GLY C C   1 
ATOM   2700  O  O   . GLY C  1 83  ? 63.007  104.730 -25.762 1.00 22.66 ? 56  GLY C O   1 
ATOM   2701  N  N   . CYS C  1 84  ? 61.796  103.422 -27.147 1.00 22.03 ? 57  CYS C N   1 
ATOM   2702  C  CA  . CYS C  1 84  ? 61.308  102.553 -26.038 1.00 22.99 ? 57  CYS C CA  1 
ATOM   2703  C  C   . CYS C  1 84  ? 62.428  101.702 -25.457 1.00 22.36 ? 57  CYS C C   1 
ATOM   2704  O  O   . CYS C  1 84  ? 62.341  101.222 -24.316 1.00 19.61 ? 57  CYS C O   1 
ATOM   2705  C  CB  . CYS C  1 84  ? 60.136  101.679 -26.548 1.00 25.12 ? 57  CYS C CB  1 
ATOM   2706  S  SG  . CYS C  1 84  ? 58.648  102.665 -27.048 1.00 29.40 ? 57  CYS C SG  1 
ATOM   2707  N  N   . THR C  1 85  ? 63.484  101.493 -26.237 1.00 19.72 ? 58  THR C N   1 
ATOM   2708  C  CA  . THR C  1 85  ? 64.634  100.692 -25.786 1.00 22.04 ? 58  THR C CA  1 
ATOM   2709  C  C   . THR C  1 85  ? 65.298  101.238 -24.544 1.00 21.68 ? 58  THR C C   1 
ATOM   2710  O  O   . THR C  1 85  ? 65.682  100.458 -23.650 1.00 21.38 ? 58  THR C O   1 
ATOM   2711  C  CB  . THR C  1 85  ? 65.685  100.661 -26.929 1.00 26.81 ? 58  THR C CB  1 
ATOM   2712  O  OG1 . THR C  1 85  ? 65.020  100.159 -28.069 1.00 30.40 ? 58  THR C OG1 1 
ATOM   2713  C  CG2 . THR C  1 85  ? 66.843  99.703  -26.611 1.00 29.06 ? 58  THR C CG2 1 
ATOM   2714  N  N   . SER C  1 86  ? 65.407  102.573 -24.443 1.00 19.39 ? 59  SER C N   1 
ATOM   2715  C  CA  . SER C  1 86  ? 66.091  103.171 -23.293 1.00 20.87 ? 59  SER C CA  1 
ATOM   2716  C  C   . SER C  1 86  ? 65.257  103.147 -22.011 1.00 18.92 ? 59  SER C C   1 
ATOM   2717  O  O   . SER C  1 86  ? 65.737  103.556 -20.968 1.00 18.87 ? 59  SER C O   1 
ATOM   2718  C  CB  . SER C  1 86  ? 66.591  104.595 -23.641 1.00 23.00 ? 59  SER C CB  1 
ATOM   2719  O  OG  . SER C  1 86  ? 65.586  105.302 -24.307 1.00 24.91 ? 59  SER C OG  1 
ATOM   2720  N  N   . ALA C  1 87  ? 64.015  102.624 -22.078 1.00 18.01 ? 60  ALA C N   1 
ATOM   2721  C  CA  . ALA C  1 87  ? 63.234  102.430 -20.832 1.00 18.32 ? 60  ALA C CA  1 
ATOM   2722  C  C   . ALA C  1 87  ? 63.801  101.312 -19.923 1.00 17.20 ? 60  ALA C C   1 
ATOM   2723  O  O   . ALA C  1 87  ? 63.430  101.200 -18.743 1.00 17.62 ? 60  ALA C O   1 
ATOM   2724  C  CB  . ALA C  1 87  ? 61.767  102.160 -21.173 1.00 16.58 ? 60  ALA C CB  1 
ATOM   2725  N  N   . GLY C  1 88  ? 64.712  100.484 -20.440 1.00 18.01 ? 61  GLY C N   1 
ATOM   2726  C  CA  . GLY C  1 88  ? 65.352  99.479  -19.593 1.00 17.34 ? 61  GLY C CA  1 
ATOM   2727  C  C   . GLY C  1 88  ? 64.387  98.275  -19.397 1.00 18.29 ? 61  GLY C C   1 
ATOM   2728  O  O   . GLY C  1 88  ? 63.468  98.097  -20.174 1.00 19.28 ? 61  GLY C O   1 
ATOM   2729  N  N   . PRO C  1 89  ? 64.610  97.448  -18.361 1.00 20.23 ? 62  PRO C N   1 
ATOM   2730  C  CA  . PRO C  1 89  ? 63.843  96.194  -18.220 1.00 19.96 ? 62  PRO C CA  1 
ATOM   2731  C  C   . PRO C  1 89  ? 62.566  96.496  -17.423 1.00 18.32 ? 62  PRO C C   1 
ATOM   2732  O  O   . PRO C  1 89  ? 62.299  97.648  -17.092 1.00 17.07 ? 62  PRO C O   1 
ATOM   2733  C  CB  . PRO C  1 89  ? 64.775  95.313  -17.374 1.00 20.48 ? 62  PRO C CB  1 
ATOM   2734  C  CG  . PRO C  1 89  ? 65.453  96.326  -16.462 1.00 21.68 ? 62  PRO C CG  1 
ATOM   2735  C  CD  . PRO C  1 89  ? 65.675  97.568  -17.341 1.00 22.14 ? 62  PRO C CD  1 
ATOM   2736  N  N   . HIS C  1 90  ? 61.807  95.465  -17.083 1.00 18.00 ? 63  HIS C N   1 
ATOM   2737  C  CA  . HIS C  1 90  ? 60.586  95.710  -16.248 1.00 18.17 ? 63  HIS C CA  1 
ATOM   2738  C  C   . HIS C  1 90  ? 61.002  96.312  -14.913 1.00 18.36 ? 63  HIS C C   1 
ATOM   2739  O  O   . HIS C  1 90  ? 62.059  95.934  -14.373 1.00 18.12 ? 63  HIS C O   1 
ATOM   2740  C  CB  . HIS C  1 90  ? 59.843  94.394  -15.998 1.00 19.23 ? 63  HIS C CB  1 
ATOM   2741  C  CG  . HIS C  1 90  ? 59.255  93.802  -17.236 1.00 18.91 ? 63  HIS C CG  1 
ATOM   2742  N  ND1 . HIS C  1 90  ? 58.532  92.636  -17.222 1.00 18.96 ? 63  HIS C ND1 1 
ATOM   2743  C  CD2 . HIS C  1 90  ? 59.296  94.195  -18.536 1.00 20.07 ? 63  HIS C CD2 1 
ATOM   2744  C  CE1 . HIS C  1 90  ? 58.162  92.317  -18.447 1.00 18.01 ? 63  HIS C CE1 1 
ATOM   2745  N  NE2 . HIS C  1 90  ? 58.613  93.247  -19.264 1.00 20.03 ? 63  HIS C NE2 1 
ATOM   2746  N  N   . PHE C  1 91  ? 60.186  97.229  -14.378 1.00 16.14 ? 64  PHE C N   1 
ATOM   2747  C  CA  . PHE C  1 91  ? 60.473  97.853  -13.094 1.00 17.03 ? 64  PHE C CA  1 
ATOM   2748  C  C   . PHE C  1 91  ? 60.427  96.758  -12.030 1.00 17.31 ? 64  PHE C C   1 
ATOM   2749  O  O   . PHE C  1 91  ? 59.419  96.087  -11.869 1.00 15.36 ? 64  PHE C O   1 
ATOM   2750  C  CB  . PHE C  1 91  ? 59.442  98.980  -12.808 1.00 16.35 ? 64  PHE C CB  1 
ATOM   2751  C  CG  . PHE C  1 91  ? 59.577  99.624  -11.453 1.00 18.31 ? 64  PHE C CG  1 
ATOM   2752  C  CD1 . PHE C  1 91  ? 60.850  99.986  -10.936 1.00 18.92 ? 64  PHE C CD1 1 
ATOM   2753  C  CD2 . PHE C  1 91  ? 58.422  99.927  -10.717 1.00 18.11 ? 64  PHE C CD2 1 
ATOM   2754  C  CE1 . PHE C  1 91  ? 60.924  100.593 -9.663  1.00 19.54 ? 64  PHE C CE1 1 
ATOM   2755  C  CE2 . PHE C  1 91  ? 58.487  100.546 -9.449  1.00 19.68 ? 64  PHE C CE2 1 
ATOM   2756  C  CZ  . PHE C  1 91  ? 59.755  100.886 -8.925  1.00 17.81 ? 64  PHE C CZ  1 
ATOM   2757  N  N   . ASN C  1 92  ? 61.558  96.508  -11.350 1.00 17.13 ? 65  ASN C N   1 
ATOM   2758  C  CA  . ASN C  1 92  ? 61.670  95.308  -10.507 1.00 17.33 ? 65  ASN C CA  1 
ATOM   2759  C  C   . ASN C  1 92  ? 62.538  95.623  -9.247  1.00 18.41 ? 65  ASN C C   1 
ATOM   2760  O  O   . ASN C  1 92  ? 63.591  95.019  -9.094  1.00 19.95 ? 65  ASN C O   1 
ATOM   2761  C  CB  . ASN C  1 92  ? 62.290  94.182  -11.350 1.00 20.93 ? 65  ASN C CB  1 
ATOM   2762  C  CG  . ASN C  1 92  ? 62.365  92.814  -10.611 1.00 21.38 ? 65  ASN C CG  1 
ATOM   2763  O  OD1 . ASN C  1 92  ? 61.632  92.552  -9.661  1.00 19.61 ? 65  ASN C OD1 1 
ATOM   2764  N  ND2 . ASN C  1 92  ? 63.275  91.949  -11.074 1.00 22.95 ? 65  ASN C ND2 1 
ATOM   2765  N  N   . PRO C  1 93  ? 62.070  96.510  -8.366  1.00 19.27 ? 66  PRO C N   1 
ATOM   2766  C  CA  . PRO C  1 93  ? 62.934  96.921  -7.280  1.00 22.54 ? 66  PRO C CA  1 
ATOM   2767  C  C   . PRO C  1 93  ? 63.185  95.781  -6.286  1.00 26.97 ? 66  PRO C C   1 
ATOM   2768  O  O   . PRO C  1 93  ? 64.172  95.840  -5.525  1.00 26.78 ? 66  PRO C O   1 
ATOM   2769  C  CB  . PRO C  1 93  ? 62.167  98.070  -6.624  1.00 20.94 ? 66  PRO C CB  1 
ATOM   2770  C  CG  . PRO C  1 93  ? 60.730  97.807  -6.961  1.00 20.94 ? 66  PRO C CG  1 
ATOM   2771  C  CD  . PRO C  1 93  ? 60.768  97.207  -8.330  1.00 16.88 ? 66  PRO C CD  1 
ATOM   2772  N  N   . LEU C  1 94  ? 62.340  94.752  -6.296  1.00 25.91 ? 67  LEU C N   1 
ATOM   2773  C  CA  . LEU C  1 94  ? 62.538  93.615  -5.383  1.00 25.00 ? 67  LEU C CA  1 
ATOM   2774  C  C   . LEU C  1 94  ? 63.276  92.428  -5.986  1.00 27.02 ? 67  LEU C C   1 
ATOM   2775  O  O   . LEU C  1 94  ? 63.365  91.358  -5.360  1.00 25.96 ? 67  LEU C O   1 
ATOM   2776  C  CB  . LEU C  1 94  ? 61.202  93.186  -4.800  1.00 25.78 ? 67  LEU C CB  1 
ATOM   2777  C  CG  . LEU C  1 94  ? 60.678  94.239  -3.823  1.00 28.58 ? 67  LEU C CG  1 
ATOM   2778  C  CD1 . LEU C  1 94  ? 59.212  93.947  -3.526  1.00 31.09 ? 67  LEU C CD1 1 
ATOM   2779  C  CD2 . LEU C  1 94  ? 61.532  94.160  -2.532  1.00 30.39 ? 67  LEU C CD2 1 
ATOM   2780  N  N   . SER C  1 95  ? 63.811  92.618  -7.194  1.00 23.12 ? 68  SER C N   1 
ATOM   2781  C  CA  . SER C  1 95  ? 64.563  91.607  -7.940  1.00 24.42 ? 68  SER C CA  1 
ATOM   2782  C  C   . SER C  1 95  ? 63.846  90.249  -7.940  1.00 26.70 ? 68  SER C C   1 
ATOM   2783  O  O   . SER C  1 95  ? 64.449  89.247  -7.552  1.00 25.35 ? 68  SER C O   1 
ATOM   2784  C  CB  . SER C  1 95  ? 66.004  91.425  -7.376  1.00 29.83 ? 68  SER C CB  1 
ATOM   2785  O  OG  . SER C  1 95  ? 66.696  92.651  -7.345  1.00 32.15 ? 68  SER C OG  1 
ATOM   2786  N  N   . ARG C  1 96  ? 62.565  90.215  -8.316  1.00 22.27 ? 69  ARG C N   1 
ATOM   2787  C  CA  . ARG C  1 96  ? 61.858  88.951  -8.454  1.00 21.46 ? 69  ARG C CA  1 
ATOM   2788  C  C   . ARG C  1 96  ? 61.914  88.510  -9.886  1.00 22.69 ? 69  ARG C C   1 
ATOM   2789  O  O   . ARG C  1 96  ? 62.390  89.240  -10.765 1.00 22.40 ? 69  ARG C O   1 
ATOM   2790  C  CB  . ARG C  1 96  ? 60.406  89.081  -8.052  1.00 22.81 ? 69  ARG C CB  1 
ATOM   2791  C  CG  . ARG C  1 96  ? 60.179  89.685  -6.679  1.00 26.23 ? 69  ARG C CG  1 
ATOM   2792  C  CD  . ARG C  1 96  ? 60.608  88.762  -5.530  1.00 30.33 ? 69  ARG C CD  1 
ATOM   2793  N  NE  . ARG C  1 96  ? 60.328  89.399  -4.227  1.00 36.02 ? 69  ARG C NE  1 
ATOM   2794  C  CZ  . ARG C  1 96  ? 61.210  89.525  -3.211  1.00 37.90 ? 69  ARG C CZ  1 
ATOM   2795  N  NH1 . ARG C  1 96  ? 62.454  89.028  -3.291  1.00 35.61 ? 69  ARG C NH1 1 
ATOM   2796  N  NH2 . ARG C  1 96  ? 60.833  90.154  -2.091  1.00 39.18 ? 69  ARG C NH2 1 
ATOM   2797  N  N   . LYS C  1 97  ? 61.440  87.291  -10.127 1.00 21.43 ? 70  LYS C N   1 
ATOM   2798  C  CA  . LYS C  1 97  ? 61.245  86.841  -11.478 1.00 23.33 ? 70  LYS C CA  1 
ATOM   2799  C  C   . LYS C  1 97  ? 59.911  87.422  -12.009 1.00 19.70 ? 70  LYS C C   1 
ATOM   2800  O  O   . LYS C  1 97  ? 59.035  87.821  -11.226 1.00 18.54 ? 70  LYS C O   1 
ATOM   2801  C  CB  . LYS C  1 97  ? 61.182  85.328  -11.453 1.00 28.08 ? 70  LYS C CB  1 
ATOM   2802  C  CG  . LYS C  1 97  ? 62.566  84.714  -11.166 1.00 36.21 ? 70  LYS C CG  1 
ATOM   2803  C  CD  . LYS C  1 97  ? 62.579  83.205  -11.388 1.00 44.17 ? 70  LYS C CD  1 
ATOM   2804  C  CE  . LYS C  1 97  ? 61.708  82.494  -10.373 1.00 46.54 ? 70  LYS C CE  1 
ATOM   2805  N  NZ  . LYS C  1 97  ? 62.184  81.075  -10.274 1.00 57.66 ? 70  LYS C NZ  1 
ATOM   2806  N  N   . HIS C  1 98  ? 59.763  87.401  -13.325 1.00 19.60 ? 71  HIS C N   1 
ATOM   2807  C  CA  . HIS C  1 98  ? 58.531  87.875  -14.002 1.00 19.75 ? 71  HIS C CA  1 
ATOM   2808  C  C   . HIS C  1 98  ? 57.305  86.994  -13.652 1.00 19.80 ? 71  HIS C C   1 
ATOM   2809  O  O   . HIS C  1 98  ? 57.448  85.749  -13.553 1.00 20.27 ? 71  HIS C O   1 
ATOM   2810  C  CB  . HIS C  1 98  ? 58.810  87.937  -15.536 1.00 17.96 ? 71  HIS C CB  1 
ATOM   2811  C  CG  . HIS C  1 98  ? 57.625  88.354  -16.340 1.00 17.64 ? 71  HIS C CG  1 
ATOM   2812  N  ND1 . HIS C  1 98  ? 57.248  89.668  -16.460 1.00 16.63 ? 71  HIS C ND1 1 
ATOM   2813  C  CD2 . HIS C  1 98  ? 56.708  87.627  -17.028 1.00 17.87 ? 71  HIS C CD2 1 
ATOM   2814  C  CE1 . HIS C  1 98  ? 56.135  89.745  -17.166 1.00 17.48 ? 71  HIS C CE1 1 
ATOM   2815  N  NE2 . HIS C  1 98  ? 55.804  88.521  -17.552 1.00 16.79 ? 71  HIS C NE2 1 
ATOM   2816  N  N   . GLY C  1 99  ? 56.120  87.598  -13.456 1.00 17.02 ? 72  GLY C N   1 
ATOM   2817  C  CA  . GLY C  1 99  ? 54.887  86.824  -13.238 1.00 17.28 ? 72  GLY C CA  1 
ATOM   2818  C  C   . GLY C  1 99  ? 53.727  87.583  -13.817 1.00 19.00 ? 72  GLY C C   1 
ATOM   2819  O  O   . GLY C  1 99  ? 53.939  88.569  -14.543 1.00 17.31 ? 72  GLY C O   1 
ATOM   2820  N  N   . GLY C  1 100 ? 52.512  87.133  -13.515 1.00 19.32 ? 73  GLY C N   1 
ATOM   2821  C  CA  . GLY C  1 100 ? 51.341  87.894  -13.924 1.00 16.65 ? 73  GLY C CA  1 
ATOM   2822  C  C   . GLY C  1 100 ? 50.962  88.719  -12.723 1.00 17.59 ? 73  GLY C C   1 
ATOM   2823  O  O   . GLY C  1 100 ? 51.530  88.479  -11.610 1.00 17.88 ? 73  GLY C O   1 
ATOM   2824  N  N   . PRO C  1 101 ? 50.022  89.667  -12.907 1.00 17.26 ? 74  PRO C N   1 
ATOM   2825  C  CA  . PRO C  1 101 ? 49.727  90.634  -11.837 1.00 17.96 ? 74  PRO C CA  1 
ATOM   2826  C  C   . PRO C  1 101 ? 49.131  89.921  -10.612 1.00 22.19 ? 74  PRO C C   1 
ATOM   2827  O  O   . PRO C  1 101 ? 49.277  90.414  -9.498  1.00 20.24 ? 74  PRO C O   1 
ATOM   2828  C  CB  . PRO C  1 101 ? 48.725  91.600  -12.485 1.00 19.02 ? 74  PRO C CB  1 
ATOM   2829  C  CG  . PRO C  1 101 ? 48.231  90.953  -13.752 1.00 18.63 ? 74  PRO C CG  1 
ATOM   2830  C  CD  . PRO C  1 101 ? 49.337  89.998  -14.165 1.00 17.18 ? 74  PRO C CD  1 
ATOM   2831  N  N   . LYS C  1 102 ? 48.473  88.768  -10.802 1.00 21.40 ? 75  LYS C N   1 
ATOM   2832  C  CA  . LYS C  1 102 ? 47.918  88.030  -9.624  1.00 23.19 ? 75  LYS C CA  1 
ATOM   2833  C  C   . LYS C  1 102 ? 48.945  87.203  -8.855  1.00 23.80 ? 75  LYS C C   1 
ATOM   2834  O  O   . LYS C  1 102 ? 48.633  86.702  -7.763  1.00 24.40 ? 75  LYS C O   1 
ATOM   2835  C  CB  . LYS C  1 102 ? 46.728  87.132  -10.024 1.00 26.52 ? 75  LYS C CB  1 
ATOM   2836  C  CG  . LYS C  1 102 ? 45.536  87.880  -10.634 1.00 31.89 ? 75  LYS C CG  1 
ATOM   2837  C  CD  . LYS C  1 102 ? 44.827  86.999  -11.674 1.00 39.59 ? 75  LYS C CD  1 
ATOM   2838  C  CE  . LYS C  1 102 ? 44.185  85.770  -11.000 1.00 37.43 ? 75  LYS C CE  1 
ATOM   2839  N  NZ  . LYS C  1 102 ? 43.198  85.022  -11.844 1.00 40.99 ? 75  LYS C NZ  1 
ATOM   2840  N  N   . ASP C  1 103 ? 50.171  87.071  -9.359  1.00 20.15 ? 76  ASP C N   1 
ATOM   2841  C  CA  . ASP C  1 103 ? 51.201  86.239  -8.690  1.00 22.89 ? 76  ASP C CA  1 
ATOM   2842  C  C   . ASP C  1 103 ? 51.875  86.991  -7.562  1.00 25.42 ? 76  ASP C C   1 
ATOM   2843  O  O   . ASP C  1 103 ? 52.129  88.188  -7.674  1.00 22.23 ? 76  ASP C O   1 
ATOM   2844  C  CB  . ASP C  1 103 ? 52.278  85.834  -9.707  1.00 24.33 ? 76  ASP C CB  1 
ATOM   2845  C  CG  . ASP C  1 103 ? 51.757  84.865  -10.704 1.00 29.30 ? 76  ASP C CG  1 
ATOM   2846  O  OD1 . ASP C  1 103 ? 50.964  83.989  -10.268 1.00 29.97 ? 76  ASP C OD1 1 
ATOM   2847  O  OD2 . ASP C  1 103 ? 52.075  84.967  -11.904 1.00 28.30 ? 76  ASP C OD2 1 
ATOM   2848  N  N   . GLU C  1 104 ? 52.183  86.296  -6.472  1.00 25.16 ? 77  GLU C N   1 
ATOM   2849  C  CA  . GLU C  1 104 ? 53.062  86.880  -5.450  1.00 25.81 ? 77  GLU C CA  1 
ATOM   2850  C  C   . GLU C  1 104 ? 54.468  87.098  -6.015  1.00 23.99 ? 77  GLU C C   1 
ATOM   2851  O  O   . GLU C  1 104 ? 55.086  88.140  -5.781  1.00 25.28 ? 77  GLU C O   1 
ATOM   2852  C  CB  . GLU C  1 104 ? 53.095  85.986  -4.189  1.00 33.85 ? 77  GLU C CB  1 
ATOM   2853  C  CG  . GLU C  1 104 ? 53.818  86.644  -3.007  1.00 49.28 ? 77  GLU C CG  1 
ATOM   2854  C  CD  . GLU C  1 104 ? 54.254  85.658  -1.908  1.00 63.49 ? 77  GLU C CD  1 
ATOM   2855  O  OE1 . GLU C  1 104 ? 53.566  84.627  -1.639  1.00 61.18 ? 77  GLU C OE1 1 
ATOM   2856  O  OE2 . GLU C  1 104 ? 55.309  85.923  -1.293  1.00 65.59 ? 77  GLU C OE2 1 
ATOM   2857  N  N   . GLU C  1 105 ? 54.956  86.165  -6.824  1.00 20.92 ? 78  GLU C N   1 
ATOM   2858  C  CA  . GLU C  1 105 ? 56.269  86.347  -7.449  1.00 21.20 ? 78  GLU C CA  1 
ATOM   2859  C  C   . GLU C  1 105 ? 56.084  87.087  -8.782  1.00 18.55 ? 78  GLU C C   1 
ATOM   2860  O  O   . GLU C  1 105 ? 55.670  86.511  -9.777  1.00 20.33 ? 78  GLU C O   1 
ATOM   2861  C  CB  . GLU C  1 105 ? 56.943  85.013  -7.702  1.00 24.12 ? 78  GLU C CB  1 
ATOM   2862  C  CG  . GLU C  1 105 ? 58.337  85.096  -8.335  1.00 27.67 ? 78  GLU C CG  1 
ATOM   2863  C  CD  . GLU C  1 105 ? 59.461  85.413  -7.340  1.00 32.95 ? 78  GLU C CD  1 
ATOM   2864  O  OE1 . GLU C  1 105 ? 59.206  85.524  -6.094  1.00 35.35 ? 78  GLU C OE1 1 
ATOM   2865  O  OE2 . GLU C  1 105 ? 60.618  85.571  -7.812  1.00 30.10 ? 78  GLU C OE2 1 
ATOM   2866  N  N   . ARG C  1 106 ? 56.390  88.372  -8.801  1.00 18.85 ? 79  ARG C N   1 
ATOM   2867  C  CA  . ARG C  1 106 ? 56.248  89.176  -10.032 1.00 17.04 ? 79  ARG C CA  1 
ATOM   2868  C  C   . ARG C  1 106 ? 57.126  90.415  -9.840  1.00 18.90 ? 79  ARG C C   1 
ATOM   2869  O  O   . ARG C  1 106 ? 57.510  90.753  -8.712  1.00 19.79 ? 79  ARG C O   1 
ATOM   2870  C  CB  . ARG C  1 106 ? 54.781  89.623  -10.213 1.00 17.87 ? 79  ARG C CB  1 
ATOM   2871  C  CG  . ARG C  1 106 ? 54.235  90.359  -8.992  1.00 17.97 ? 79  ARG C CG  1 
ATOM   2872  C  CD  . ARG C  1 106 ? 52.882  91.020  -9.322  1.00 18.85 ? 79  ARG C CD  1 
ATOM   2873  N  NE  . ARG C  1 106 ? 53.055  92.391  -9.845  1.00 18.50 ? 79  ARG C NE  1 
ATOM   2874  C  CZ  . ARG C  1 106 ? 52.038  93.260  -9.968  1.00 17.66 ? 79  ARG C CZ  1 
ATOM   2875  N  NH1 . ARG C  1 106 ? 50.798  92.892  -9.628  1.00 15.40 ? 79  ARG C NH1 1 
ATOM   2876  N  NH2 . ARG C  1 106 ? 52.253  94.504  -10.419 1.00 15.69 ? 79  ARG C NH2 1 
ATOM   2877  N  N   . HIS C  1 107 ? 57.422  91.085  -10.942 1.00 16.85 ? 80  HIS C N   1 
ATOM   2878  C  CA  . HIS C  1 107 ? 58.035  92.389  -10.913 1.00 16.66 ? 80  HIS C CA  1 
ATOM   2879  C  C   . HIS C  1 107 ? 56.959  93.391  -10.511 1.00 16.37 ? 80  HIS C C   1 
ATOM   2880  O  O   . HIS C  1 107 ? 55.762  93.206  -10.821 1.00 15.45 ? 80  HIS C O   1 
ATOM   2881  C  CB  . HIS C  1 107 ? 58.495  92.722  -12.343 1.00 15.65 ? 80  HIS C CB  1 
ATOM   2882  C  CG  . HIS C  1 107 ? 59.498  91.778  -12.897 1.00 16.87 ? 80  HIS C CG  1 
ATOM   2883  N  ND1 . HIS C  1 107 ? 59.604  91.499  -14.238 1.00 16.13 ? 80  HIS C ND1 1 
ATOM   2884  C  CD2 . HIS C  1 107 ? 60.455  91.030  -12.285 1.00 16.30 ? 80  HIS C CD2 1 
ATOM   2885  C  CE1 . HIS C  1 107 ? 60.631  90.693  -14.454 1.00 17.53 ? 80  HIS C CE1 1 
ATOM   2886  N  NE2 . HIS C  1 107 ? 61.146  90.371  -13.282 1.00 16.91 ? 80  HIS C NE2 1 
ATOM   2887  N  N   . VAL C  1 108 ? 57.355  94.488  -9.879  1.00 15.47 ? 81  VAL C N   1 
ATOM   2888  C  CA  . VAL C  1 108 ? 56.326  95.518  -9.606  1.00 14.87 ? 81  VAL C CA  1 
ATOM   2889  C  C   . VAL C  1 108 ? 55.610  95.985  -10.939 1.00 13.99 ? 81  VAL C C   1 
ATOM   2890  O  O   . VAL C  1 108 ? 54.385  96.223  -10.963 1.00 14.93 ? 81  VAL C O   1 
ATOM   2891  C  CB  . VAL C  1 108 ? 56.965  96.726  -8.903  1.00 16.17 ? 81  VAL C CB  1 
ATOM   2892  C  CG1 . VAL C  1 108 ? 55.957  97.869  -8.862  1.00 15.35 ? 81  VAL C CG1 1 
ATOM   2893  C  CG2 . VAL C  1 108 ? 57.341  96.292  -7.461  1.00 17.41 ? 81  VAL C CG2 1 
ATOM   2894  N  N   . GLY C  1 109 ? 56.384  96.083  -12.007 1.00 14.70 ? 82  GLY C N   1 
ATOM   2895  C  CA  . GLY C  1 109 ? 55.885  96.541  -13.324 1.00 15.72 ? 82  GLY C CA  1 
ATOM   2896  C  C   . GLY C  1 109 ? 55.024  95.515  -14.078 1.00 16.98 ? 82  GLY C C   1 
ATOM   2897  O  O   . GLY C  1 109 ? 54.584  95.820  -15.200 1.00 16.44 ? 82  GLY C O   1 
ATOM   2898  N  N   . ASP C  1 110 ? 54.733  94.351  -13.479 1.00 14.28 ? 83  ASP C N   1 
ATOM   2899  C  CA  . ASP C  1 110 ? 54.038  93.261  -14.246 1.00 15.74 ? 83  ASP C CA  1 
ATOM   2900  C  C   . ASP C  1 110 ? 52.532  93.427  -14.199 1.00 15.46 ? 83  ASP C C   1 
ATOM   2901  O  O   . ASP C  1 110 ? 51.870  92.829  -13.345 1.00 17.15 ? 83  ASP C O   1 
ATOM   2902  C  CB  . ASP C  1 110 ? 54.433  91.889  -13.685 1.00 15.34 ? 83  ASP C CB  1 
ATOM   2903  C  CG  . ASP C  1 110 ? 55.824  91.497  -14.075 1.00 15.69 ? 83  ASP C CG  1 
ATOM   2904  O  OD1 . ASP C  1 110 ? 56.398  92.177  -14.968 1.00 16.56 ? 83  ASP C OD1 1 
ATOM   2905  O  OD2 . ASP C  1 110 ? 56.384  90.539  -13.489 1.00 16.00 ? 83  ASP C OD2 1 
ATOM   2906  N  N   . LEU C  1 111 ? 51.984  94.233  -15.121 1.00 16.23 ? 84  LEU C N   1 
ATOM   2907  C  CA  . LEU C  1 111 ? 50.540  94.460  -15.222 1.00 16.03 ? 84  LEU C CA  1 
ATOM   2908  C  C   . LEU C  1 111 ? 49.823  93.451  -16.158 1.00 16.28 ? 84  LEU C C   1 
ATOM   2909  O  O   . LEU C  1 111 ? 48.624  93.588  -16.422 1.00 21.22 ? 84  LEU C O   1 
ATOM   2910  C  CB  . LEU C  1 111 ? 50.203  95.892  -15.677 1.00 14.35 ? 84  LEU C CB  1 
ATOM   2911  C  CG  . LEU C  1 111 ? 50.766  96.964  -14.733 1.00 17.19 ? 84  LEU C CG  1 
ATOM   2912  C  CD1 . LEU C  1 111 ? 50.454  98.363  -15.262 1.00 17.85 ? 84  LEU C CD1 1 
ATOM   2913  C  CD2 . LEU C  1 111 ? 50.173  96.753  -13.339 1.00 18.58 ? 84  LEU C CD2 1 
ATOM   2914  N  N   . GLY C  1 112 ? 50.544  92.468  -16.668 1.00 16.03 ? 85  GLY C N   1 
ATOM   2915  C  CA  . GLY C  1 112 ? 49.878  91.361  -17.388 1.00 14.88 ? 85  GLY C CA  1 
ATOM   2916  C  C   . GLY C  1 112 ? 49.632  91.768  -18.847 1.00 16.02 ? 85  GLY C C   1 
ATOM   2917  O  O   . GLY C  1 112 ? 50.513  92.354  -19.509 1.00 15.57 ? 85  GLY C O   1 
ATOM   2918  N  N   . ASN C  1 113 ? 48.463  91.399  -19.364 1.00 14.64 ? 86  ASN C N   1 
ATOM   2919  C  CA  . ASN C  1 113 ? 48.166  91.693  -20.761 1.00 15.87 ? 86  ASN C CA  1 
ATOM   2920  C  C   . ASN C  1 113 ? 47.026  92.723  -20.864 1.00 15.98 ? 86  ASN C C   1 
ATOM   2921  O  O   . ASN C  1 113 ? 46.222  92.843  -19.906 1.00 15.40 ? 86  ASN C O   1 
ATOM   2922  C  CB  . ASN C  1 113 ? 47.689  90.417  -21.473 1.00 16.35 ? 86  ASN C CB  1 
ATOM   2923  C  CG  . ASN C  1 113 ? 48.824  89.481  -21.738 1.00 16.54 ? 86  ASN C CG  1 
ATOM   2924  O  OD1 . ASN C  1 113 ? 49.738  89.836  -22.496 1.00 14.59 ? 86  ASN C OD1 1 
ATOM   2925  N  ND2 . ASN C  1 113 ? 48.798  88.302  -21.106 1.00 15.15 ? 86  ASN C ND2 1 
ATOM   2926  N  N   . VAL C  1 114 ? 46.944  93.378  -22.026 1.00 14.27 ? 87  VAL C N   1 
ATOM   2927  C  CA  . VAL C  1 114 ? 45.725  94.070  -22.410 1.00 14.65 ? 87  VAL C CA  1 
ATOM   2928  C  C   . VAL C  1 114 ? 45.255  93.432  -23.709 1.00 15.68 ? 87  VAL C C   1 
ATOM   2929  O  O   . VAL C  1 114 ? 46.044  92.860  -24.443 1.00 17.94 ? 87  VAL C O   1 
ATOM   2930  C  CB  . VAL C  1 114 ? 45.922  95.605  -22.558 1.00 15.64 ? 87  VAL C CB  1 
ATOM   2931  C  CG1 . VAL C  1 114 ? 46.334  96.192  -21.186 1.00 14.94 ? 87  VAL C CG1 1 
ATOM   2932  C  CG2 . VAL C  1 114 ? 46.978  95.932  -23.631 1.00 14.66 ? 87  VAL C CG2 1 
ATOM   2933  N  N   . THR C  1 115 ? 43.977  93.566  -24.008 1.00 16.07 ? 88  THR C N   1 
ATOM   2934  C  CA  . THR C  1 115 ? 43.388  92.814  -25.130 1.00 15.62 ? 88  THR C CA  1 
ATOM   2935  C  C   . THR C  1 115 ? 42.848  93.833  -26.124 1.00 15.38 ? 88  THR C C   1 
ATOM   2936  O  O   . THR C  1 115 ? 41.970  94.677  -25.777 1.00 15.80 ? 88  THR C O   1 
ATOM   2937  C  CB  . THR C  1 115 ? 42.202  91.892  -24.638 1.00 18.08 ? 88  THR C CB  1 
ATOM   2938  O  OG1 . THR C  1 115 ? 42.723  90.832  -23.827 1.00 19.37 ? 88  THR C OG1 1 
ATOM   2939  C  CG2 . THR C  1 115 ? 41.432  91.240  -25.881 1.00 18.84 ? 88  THR C CG2 1 
ATOM   2940  N  N   . ALA C  1 116 ? 43.268  93.695  -27.382 1.00 14.42 ? 89  ALA C N   1 
ATOM   2941  C  CA  . ALA C  1 116 ? 42.718  94.526  -28.431 1.00 16.35 ? 89  ALA C CA  1 
ATOM   2942  C  C   . ALA C  1 116 ? 41.595  93.763  -29.144 1.00 17.77 ? 89  ALA C C   1 
ATOM   2943  O  O   . ALA C  1 116 ? 41.677  92.546  -29.372 1.00 17.30 ? 89  ALA C O   1 
ATOM   2944  C  CB  . ALA C  1 116 ? 43.805  94.921  -29.446 1.00 15.96 ? 89  ALA C CB  1 
ATOM   2945  N  N   . ASP C  1 117 ? 40.570  94.502  -29.509 1.00 18.25 ? 90  ASP C N   1 
ATOM   2946  C  CA  . ASP C  1 117 ? 39.380  93.917  -30.161 1.00 22.45 ? 90  ASP C CA  1 
ATOM   2947  C  C   . ASP C  1 117 ? 39.634  93.768  -31.663 1.00 24.10 ? 90  ASP C C   1 
ATOM   2948  O  O   . ASP C  1 117 ? 40.767  94.023  -32.129 1.00 20.45 ? 90  ASP C O   1 
ATOM   2949  C  CB  . ASP C  1 117 ? 38.110  94.759  -29.853 1.00 22.53 ? 90  ASP C CB  1 
ATOM   2950  C  CG  . ASP C  1 117 ? 38.168  96.217  -30.408 1.00 26.07 ? 90  ASP C CG  1 
ATOM   2951  O  OD1 . ASP C  1 117 ? 38.893  96.556  -31.362 1.00 23.13 ? 90  ASP C OD1 1 
ATOM   2952  O  OD2 . ASP C  1 117 ? 37.419  97.057  -29.879 1.00 26.21 ? 90  ASP C OD2 1 
ATOM   2953  N  N   . LYS C  1 118 ? 38.598  93.395  -32.445 1.00 24.86 ? 91  LYS C N   1 
ATOM   2954  C  CA  . LYS C  1 118 ? 38.842  93.141  -33.869 1.00 26.77 ? 91  LYS C CA  1 
ATOM   2955  C  C   . LYS C  1 118 ? 39.156  94.405  -34.663 1.00 25.92 ? 91  LYS C C   1 
ATOM   2956  O  O   . LYS C  1 118 ? 39.642  94.299  -35.779 1.00 30.78 ? 91  LYS C O   1 
ATOM   2957  C  CB  . LYS C  1 118 ? 37.648  92.428  -34.512 1.00 31.08 ? 91  LYS C CB  1 
ATOM   2958  C  CG  . LYS C  1 118 ? 36.402  93.254  -34.518 1.00 38.18 ? 91  LYS C CG  1 
ATOM   2959  C  CD  . LYS C  1 118 ? 35.260  92.454  -35.154 1.00 48.82 ? 91  LYS C CD  1 
ATOM   2960  C  CE  . LYS C  1 118 ? 34.160  93.401  -35.609 1.00 55.53 ? 91  LYS C CE  1 
ATOM   2961  N  NZ  . LYS C  1 118 ? 33.451  94.016  -34.440 1.00 58.49 ? 91  LYS C NZ  1 
ATOM   2962  N  N   . ASP C  1 119 ? 38.889  95.582  -34.100 1.00 24.25 ? 92  ASP C N   1 
ATOM   2963  C  CA  . ASP C  1 119 ? 39.281  96.851  -34.755 1.00 27.41 ? 92  ASP C CA  1 
ATOM   2964  C  C   . ASP C  1 119 ? 40.669  97.320  -34.347 1.00 25.11 ? 92  ASP C C   1 
ATOM   2965  O  O   . ASP C  1 119 ? 41.097  98.397  -34.754 1.00 23.33 ? 92  ASP C O   1 
ATOM   2966  C  CB  . ASP C  1 119 ? 38.290  97.949  -34.413 1.00 28.74 ? 92  ASP C CB  1 
ATOM   2967  C  CG  . ASP C  1 119 ? 36.875  97.607  -34.909 1.00 36.01 ? 92  ASP C CG  1 
ATOM   2968  O  OD1 . ASP C  1 119 ? 36.760  97.114  -36.056 1.00 35.00 ? 92  ASP C OD1 1 
ATOM   2969  O  OD2 . ASP C  1 119 ? 35.915  97.790  -34.162 1.00 37.81 ? 92  ASP C OD2 1 
ATOM   2970  N  N   . GLY C  1 120 ? 41.347  96.539  -33.514 1.00 23.03 ? 93  GLY C N   1 
ATOM   2971  C  CA  . GLY C  1 120 ? 42.714  96.942  -33.109 1.00 20.24 ? 93  GLY C CA  1 
ATOM   2972  C  C   . GLY C  1 120 ? 42.745  97.809  -31.844 1.00 18.75 ? 93  GLY C C   1 
ATOM   2973  O  O   . GLY C  1 120 ? 43.792  98.389  -31.506 1.00 19.23 ? 93  GLY C O   1 
ATOM   2974  N  N   . VAL C  1 121 ? 41.614  97.888  -31.121 1.00 17.89 ? 94  VAL C N   1 
ATOM   2975  C  CA  . VAL C  1 121 ? 41.503  98.820  -29.977 1.00 18.14 ? 94  VAL C CA  1 
ATOM   2976  C  C   . VAL C  1 121 ? 41.504  98.067  -28.663 1.00 17.62 ? 94  VAL C C   1 
ATOM   2977  O  O   . VAL C  1 121 ? 40.718  97.110  -28.479 1.00 19.07 ? 94  VAL C O   1 
ATOM   2978  C  CB  . VAL C  1 121 ? 40.203  99.683  -30.079 1.00 19.82 ? 94  VAL C CB  1 
ATOM   2979  C  CG1 . VAL C  1 121 ? 40.015  100.541 -28.832 1.00 18.87 ? 94  VAL C CG1 1 
ATOM   2980  C  CG2 . VAL C  1 121 ? 40.233  100.531 -31.353 1.00 20.77 ? 94  VAL C CG2 1 
ATOM   2981  N  N   . ALA C  1 122 ? 42.405  98.459  -27.744 1.00 16.28 ? 95  ALA C N   1 
ATOM   2982  C  CA  . ALA C  1 122 ? 42.389  97.840  -26.426 1.00 15.70 ? 95  ALA C CA  1 
ATOM   2983  C  C   . ALA C  1 122 ? 41.766  98.884  -25.504 1.00 16.38 ? 95  ALA C C   1 
ATOM   2984  O  O   . ALA C  1 122 ? 42.335  99.974  -25.315 1.00 17.78 ? 95  ALA C O   1 
ATOM   2985  C  CB  . ALA C  1 122 ? 43.838  97.520  -25.980 1.00 17.06 ? 95  ALA C CB  1 
ATOM   2986  N  N   . ASP C  1 123 ? 40.591  98.576  -24.961 1.00 16.83 ? 96  ASP C N   1 
ATOM   2987  C  CA  . ASP C  1 123 ? 39.968  99.442  -23.910 1.00 18.55 ? 96  ASP C CA  1 
ATOM   2988  C  C   . ASP C  1 123 ? 40.432  98.935  -22.551 1.00 17.13 ? 96  ASP C C   1 
ATOM   2989  O  O   . ASP C  1 123 ? 39.819  98.093  -21.943 1.00 17.74 ? 96  ASP C O   1 
ATOM   2990  C  CB  . ASP C  1 123 ? 38.439  99.484  -24.046 1.00 21.82 ? 96  ASP C CB  1 
ATOM   2991  C  CG  . ASP C  1 123 ? 37.998  100.303 -25.307 1.00 28.20 ? 96  ASP C CG  1 
ATOM   2992  O  OD1 . ASP C  1 123 ? 37.273  99.742  -26.131 1.00 28.51 ? 96  ASP C OD1 1 
ATOM   2993  O  OD2 . ASP C  1 123 ? 38.452  101.464 -25.508 1.00 26.90 ? 96  ASP C OD2 1 
ATOM   2994  N  N   . VAL C  1 124 ? 41.557  99.483  -22.087 1.00 16.58 ? 97  VAL C N   1 
ATOM   2995  C  CA  . VAL C  1 124 ? 42.269  98.925  -20.941 1.00 15.02 ? 97  VAL C CA  1 
ATOM   2996  C  C   . VAL C  1 124 ? 41.472  99.185  -19.667 1.00 17.55 ? 97  VAL C C   1 
ATOM   2997  O  O   . VAL C  1 124 ? 40.955  100.311 -19.462 1.00 17.12 ? 97  VAL C O   1 
ATOM   2998  C  CB  . VAL C  1 124 ? 43.635  99.634  -20.832 1.00 15.02 ? 97  VAL C CB  1 
ATOM   2999  C  CG1 . VAL C  1 124 ? 44.436  99.117  -19.611 1.00 15.42 ? 97  VAL C CG1 1 
ATOM   3000  C  CG2 . VAL C  1 124 ? 44.461  99.398  -22.112 1.00 15.72 ? 97  VAL C CG2 1 
ATOM   3001  N  N   . SER C  1 125 ? 41.401  98.176  -18.798 1.00 18.50 ? 98  SER C N   1 
ATOM   3002  C  CA  . SER C  1 125 ? 40.737  98.351  -17.511 1.00 20.09 ? 98  SER C CA  1 
ATOM   3003  C  C   . SER C  1 125 ? 41.366  97.378  -16.545 1.00 19.76 ? 98  SER C C   1 
ATOM   3004  O  O   . SER C  1 125 ? 41.077  96.210  -16.605 1.00 21.26 ? 98  SER C O   1 
ATOM   3005  C  CB  . SER C  1 125 ? 39.217  98.068  -17.648 1.00 26.18 ? 98  SER C CB  1 
ATOM   3006  O  OG  . SER C  1 125 ? 38.569  98.345  -16.431 1.00 31.89 ? 98  SER C OG  1 
ATOM   3007  N  N   . ILE C  1 126 ? 42.266  97.858  -15.682 1.00 16.79 ? 99  ILE C N   1 
ATOM   3008  C  CA  . ILE C  1 126 ? 43.092  97.010  -14.807 1.00 19.22 ? 99  ILE C CA  1 
ATOM   3009  C  C   . ILE C  1 126 ? 43.044  97.674  -13.419 1.00 19.87 ? 99  ILE C C   1 
ATOM   3010  O  O   . ILE C  1 126 ? 42.894  98.910  -13.294 1.00 19.16 ? 99  ILE C O   1 
ATOM   3011  C  CB  . ILE C  1 126 ? 44.578  97.027  -15.344 1.00 19.81 ? 99  ILE C CB  1 
ATOM   3012  C  CG1 . ILE C  1 126 ? 44.729  95.978  -16.491 1.00 20.58 ? 99  ILE C CG1 1 
ATOM   3013  C  CG2 . ILE C  1 126 ? 45.621  96.706  -14.265 1.00 23.35 ? 99  ILE C CG2 1 
ATOM   3014  C  CD1 . ILE C  1 126 ? 46.018  96.142  -17.294 1.00 18.82 ? 99  ILE C CD1 1 
ATOM   3015  N  N   . GLU C  1 127 ? 43.089  96.857  -12.388 1.00 19.68 ? 100 GLU C N   1 
ATOM   3016  C  CA  . GLU C  1 127 ? 43.232  97.399  -11.062 1.00 21.27 ? 100 GLU C CA  1 
ATOM   3017  C  C   . GLU C  1 127 ? 44.353  96.632  -10.418 1.00 21.16 ? 100 GLU C C   1 
ATOM   3018  O  O   . GLU C  1 127 ? 44.351  95.405  -10.450 1.00 21.98 ? 100 GLU C O   1 
ATOM   3019  C  CB  . GLU C  1 127 ? 41.929  97.241  -10.289 1.00 26.46 ? 100 GLU C CB  1 
ATOM   3020  C  CG  . GLU C  1 127 ? 42.107  97.473  -8.816  1.00 32.01 ? 100 GLU C CG  1 
ATOM   3021  C  CD  . GLU C  1 127 ? 40.785  97.384  -8.058  1.00 43.90 ? 100 GLU C CD  1 
ATOM   3022  O  OE1 . GLU C  1 127 ? 39.777  97.912  -8.578  1.00 45.29 ? 100 GLU C OE1 1 
ATOM   3023  O  OE2 . GLU C  1 127 ? 40.779  96.770  -6.957  1.00 45.61 ? 100 GLU C OE2 1 
ATOM   3024  N  N   . ASP C  1 128 ? 45.327  97.338  -9.844  1.00 20.55 ? 101 ASP C N   1 
ATOM   3025  C  CA  . ASP C  1 128 ? 46.501  96.637  -9.335  1.00 21.21 ? 101 ASP C CA  1 
ATOM   3026  C  C   . ASP C  1 128 ? 46.932  97.217  -8.003  1.00 21.14 ? 101 ASP C C   1 
ATOM   3027  O  O   . ASP C  1 128 ? 46.966  98.448  -7.854  1.00 21.27 ? 101 ASP C O   1 
ATOM   3028  C  CB  . ASP C  1 128 ? 47.674  96.768  -10.318 1.00 20.60 ? 101 ASP C CB  1 
ATOM   3029  C  CG  . ASP C  1 128 ? 48.820  95.799  -9.975  1.00 24.55 ? 101 ASP C CG  1 
ATOM   3030  O  OD1 . ASP C  1 128 ? 48.672  94.564  -10.190 1.00 27.22 ? 101 ASP C OD1 1 
ATOM   3031  O  OD2 . ASP C  1 128 ? 49.866  96.250  -9.463  1.00 22.35 ? 101 ASP C OD2 1 
ATOM   3032  N  N   . SER C  1 129 ? 47.348  96.349  -7.087  1.00 21.61 ? 102 SER C N   1 
ATOM   3033  C  CA  A SER C  1 129 ? 47.725  96.829  -5.757  0.50 24.53 ? 102 SER C CA  1 
ATOM   3034  C  CA  B SER C  1 129 ? 47.700  96.788  -5.738  0.50 25.59 ? 102 SER C CA  1 
ATOM   3035  C  C   . SER C  1 129 ? 49.203  96.740  -5.484  1.00 24.78 ? 102 SER C C   1 
ATOM   3036  O  O   . SER C  1 129 ? 49.640  96.995  -4.386  1.00 28.50 ? 102 SER C O   1 
ATOM   3037  C  CB  A SER C  1 129 ? 46.922  96.102  -4.691  0.50 26.87 ? 102 SER C CB  1 
ATOM   3038  C  CB  B SER C  1 129 ? 46.935  95.946  -4.711  0.50 29.50 ? 102 SER C CB  1 
ATOM   3039  O  OG  A SER C  1 129 ? 45.581  96.476  -4.819  0.50 25.94 ? 102 SER C OG  1 
ATOM   3040  O  OG  B SER C  1 129 ? 47.310  94.584  -4.812  0.50 32.81 ? 102 SER C OG  1 
ATOM   3041  N  N   . VAL C  1 130 ? 49.997  96.397  -6.500  1.00 19.88 ? 103 VAL C N   1 
ATOM   3042  C  CA  . VAL C  1 130 ? 51.450  96.312  -6.298  1.00 19.32 ? 103 VAL C CA  1 
ATOM   3043  C  C   . VAL C  1 130 ? 52.105  97.582  -6.816  1.00 20.98 ? 103 VAL C C   1 
ATOM   3044  O  O   . VAL C  1 130 ? 52.972  98.172  -6.126  1.00 20.29 ? 103 VAL C O   1 
ATOM   3045  C  CB  . VAL C  1 130 ? 52.061  95.024  -6.925  1.00 19.13 ? 103 VAL C CB  1 
ATOM   3046  C  CG1 . VAL C  1 130 ? 53.598  95.042  -6.877  1.00 20.15 ? 103 VAL C CG1 1 
ATOM   3047  C  CG2 . VAL C  1 130 ? 51.548  93.799  -6.153  1.00 19.93 ? 103 VAL C CG2 1 
ATOM   3048  N  N   . ILE C  1 131 ? 51.690  98.056  -8.007  1.00 18.57 ? 104 ILE C N   1 
ATOM   3049  C  CA  . ILE C  1 131 ? 52.178  99.410  -8.419  1.00 17.17 ? 104 ILE C CA  1 
ATOM   3050  C  C   . ILE C  1 131 ? 51.549  100.450 -7.452  1.00 17.46 ? 104 ILE C C   1 
ATOM   3051  O  O   . ILE C  1 131 ? 50.545  100.175 -6.790  1.00 18.17 ? 104 ILE C O   1 
ATOM   3052  C  CB  . ILE C  1 131 ? 51.791  99.754  -9.880  1.00 16.50 ? 104 ILE C CB  1 
ATOM   3053  C  CG1 . ILE C  1 131 ? 50.270  99.615  -10.053 1.00 15.69 ? 104 ILE C CG1 1 
ATOM   3054  C  CG2 . ILE C  1 131 ? 52.493  98.790  -10.847 1.00 17.28 ? 104 ILE C CG2 1 
ATOM   3055  C  CD1 . ILE C  1 131 ? 49.715  100.353 -11.294 1.00 16.11 ? 104 ILE C CD1 1 
ATOM   3056  N  N   . SER C  1 132 ? 52.137  101.633 -7.386  1.00 17.05 ? 105 SER C N   1 
ATOM   3057  C  CA  . SER C  1 132 ? 51.625  102.697 -6.546  1.00 18.54 ? 105 SER C CA  1 
ATOM   3058  C  C   . SER C  1 132 ? 51.963  104.008 -7.236  1.00 17.45 ? 105 SER C C   1 
ATOM   3059  O  O   . SER C  1 132 ? 52.861  104.076 -8.093  1.00 17.93 ? 105 SER C O   1 
ATOM   3060  C  CB  . SER C  1 132 ? 52.340  102.670 -5.166  1.00 19.04 ? 105 SER C CB  1 
ATOM   3061  O  OG  . SER C  1 132 ? 51.622  103.516 -4.281  1.00 17.38 ? 105 SER C OG  1 
ATOM   3062  N  N   . LEU C  1 133 ? 51.293  105.063 -6.827  1.00 17.53 ? 106 LEU C N   1 
ATOM   3063  C  CA  . LEU C  1 133 ? 51.687  106.403 -7.217  1.00 18.48 ? 106 LEU C CA  1 
ATOM   3064  C  C   . LEU C  1 133 ? 52.510  107.122 -6.129  1.00 22.47 ? 106 LEU C C   1 
ATOM   3065  O  O   . LEU C  1 133 ? 52.807  108.300 -6.262  1.00 22.31 ? 106 LEU C O   1 
ATOM   3066  C  CB  . LEU C  1 133 ? 50.451  107.230 -7.612  1.00 17.97 ? 106 LEU C CB  1 
ATOM   3067  C  CG  . LEU C  1 133 ? 49.596  106.609 -8.753  1.00 17.60 ? 106 LEU C CG  1 
ATOM   3068  C  CD1 . LEU C  1 133 ? 48.425  107.513 -9.153  1.00 20.05 ? 106 LEU C CD1 1 
ATOM   3069  C  CD2 . LEU C  1 133 ? 50.428  106.260 -10.016 1.00 18.17 ? 106 LEU C CD2 1 
ATOM   3070  N  N   . SER C  1 134 ? 52.964  106.388 -5.118  1.00 21.67 ? 107 SER C N   1 
ATOM   3071  C  CA  . SER C  1 134 ? 53.859  106.985 -4.111  1.00 25.72 ? 107 SER C CA  1 
ATOM   3072  C  C   . SER C  1 134 ? 54.677  105.904 -3.504  1.00 23.83 ? 107 SER C C   1 
ATOM   3073  O  O   . SER C  1 134 ? 54.414  104.694 -3.704  1.00 23.44 ? 107 SER C O   1 
ATOM   3074  C  CB  . SER C  1 134 ? 53.085  107.746 -3.017  1.00 25.73 ? 107 SER C CB  1 
ATOM   3075  O  OG  . SER C  1 134 ? 52.213  106.875 -2.344  1.00 28.83 ? 107 SER C OG  1 
ATOM   3076  N  N   . GLY C  1 135 ? 55.701  106.308 -2.760  1.00 24.66 ? 108 GLY C N   1 
ATOM   3077  C  CA  . GLY C  1 135 ? 56.513  105.316 -2.082  1.00 22.75 ? 108 GLY C CA  1 
ATOM   3078  C  C   . GLY C  1 135 ? 57.488  104.538 -2.941  1.00 22.32 ? 108 GLY C C   1 
ATOM   3079  O  O   . GLY C  1 135 ? 57.814  104.905 -4.073  1.00 23.83 ? 108 GLY C O   1 
ATOM   3080  N  N   . ASP C  1 136 ? 57.908  103.398 -2.441  1.00 21.81 ? 109 ASP C N   1 
ATOM   3081  C  CA  . ASP C  1 136 ? 58.976  102.633 -3.112  1.00 25.98 ? 109 ASP C CA  1 
ATOM   3082  C  C   . ASP C  1 136 ? 58.510  102.000 -4.432  1.00 23.57 ? 109 ASP C C   1 
ATOM   3083  O  O   . ASP C  1 136 ? 59.321  101.732 -5.315  1.00 24.56 ? 109 ASP C O   1 
ATOM   3084  C  CB  . ASP C  1 136 ? 59.358  101.455 -2.229  1.00 31.22 ? 109 ASP C CB  1 
ATOM   3085  C  CG  . ASP C  1 136 ? 60.335  101.845 -1.120  1.00 35.54 ? 109 ASP C CG  1 
ATOM   3086  O  OD1 . ASP C  1 136 ? 60.433  101.059 -0.168  1.00 36.32 ? 109 ASP C OD1 1 
ATOM   3087  O  OD2 . ASP C  1 136 ? 60.989  102.909 -1.230  1.00 38.82 ? 109 ASP C OD2 1 
ATOM   3088  N  N   . HIS C  1 137 ? 57.225  101.692 -4.507  1.00 21.27 ? 110 HIS C N   1 
ATOM   3089  C  CA  . HIS C  1 137 ? 56.704  101.093 -5.739  1.00 22.35 ? 110 HIS C CA  1 
ATOM   3090  C  C   . HIS C  1 137 ? 56.131  102.129 -6.688  1.00 20.78 ? 110 HIS C C   1 
ATOM   3091  O  O   . HIS C  1 137 ? 55.379  101.776 -7.593  1.00 17.78 ? 110 HIS C O   1 
ATOM   3092  C  CB  . HIS C  1 137 ? 55.696  100.022 -5.416  1.00 23.73 ? 110 HIS C CB  1 
ATOM   3093  C  CG  . HIS C  1 137 ? 56.327  98.848  -4.724  1.00 29.35 ? 110 HIS C CG  1 
ATOM   3094  N  ND1 . HIS C  1 137 ? 55.601  97.814  -4.183  1.00 36.52 ? 110 HIS C ND1 1 
ATOM   3095  C  CD2 . HIS C  1 137 ? 57.631  98.572  -4.463  1.00 33.10 ? 110 HIS C CD2 1 
ATOM   3096  C  CE1 . HIS C  1 137 ? 56.429  96.949  -3.619  1.00 33.72 ? 110 HIS C CE1 1 
ATOM   3097  N  NE2 . HIS C  1 137 ? 57.663  97.377  -3.791  1.00 36.78 ? 110 HIS C NE2 1 
ATOM   3098  N  N   . CYS C  1 138 ? 56.492  103.386 -6.475  1.00 18.14 ? 111 CYS C N   1 
ATOM   3099  C  CA  . CYS C  1 138 ? 55.936  104.487 -7.246  1.00 18.79 ? 111 CYS C CA  1 
ATOM   3100  C  C   . CYS C  1 138 ? 56.369  104.347 -8.740  1.00 16.88 ? 111 CYS C C   1 
ATOM   3101  O  O   . CYS C  1 138 ? 57.540  104.056 -9.025  1.00 17.71 ? 111 CYS C O   1 
ATOM   3102  C  CB  . CYS C  1 138 ? 56.444  105.820 -6.685  1.00 21.48 ? 111 CYS C CB  1 
ATOM   3103  S  SG  . CYS C  1 138 ? 55.820  107.221 -7.645  1.00 26.48 ? 111 CYS C SG  1 
ATOM   3104  N  N   . ILE C  1 139 ? 55.403  104.466 -9.654  1.00 16.62 ? 112 ILE C N   1 
ATOM   3105  C  CA  . ILE C  1 139 ? 55.657  104.324 -11.108 1.00 16.61 ? 112 ILE C CA  1 
ATOM   3106  C  C   . ILE C  1 139 ? 55.713  105.673 -11.844 1.00 16.37 ? 112 ILE C C   1 
ATOM   3107  O  O   . ILE C  1 139 ? 56.029  105.698 -13.035 1.00 15.12 ? 112 ILE C O   1 
ATOM   3108  C  CB  . ILE C  1 139 ? 54.615  103.402 -11.805 1.00 15.88 ? 112 ILE C CB  1 
ATOM   3109  C  CG1 . ILE C  1 139 ? 53.197  103.960 -11.671 1.00 17.21 ? 112 ILE C CG1 1 
ATOM   3110  C  CG2 . ILE C  1 139 ? 54.773  101.975 -11.251 1.00 16.01 ? 112 ILE C CG2 1 
ATOM   3111  C  CD1 . ILE C  1 139 ? 52.158  103.139 -12.451 1.00 19.30 ? 112 ILE C CD1 1 
ATOM   3112  N  N   . ILE C  1 140 ? 55.432  106.784 -11.137 1.00 17.02 ? 113 ILE C N   1 
ATOM   3113  C  CA  A ILE C  1 140 ? 55.578  108.149 -11.729 0.50 17.54 ? 113 ILE C CA  1 
ATOM   3114  C  CA  B ILE C  1 140 ? 55.553  108.123 -11.770 0.50 16.20 ? 113 ILE C CA  1 
ATOM   3115  C  C   . ILE C  1 140 ? 57.021  108.343 -12.161 1.00 16.55 ? 113 ILE C C   1 
ATOM   3116  O  O   . ILE C  1 140 ? 57.945  108.026 -11.396 1.00 16.59 ? 113 ILE C O   1 
ATOM   3117  C  CB  A ILE C  1 140 ? 55.259  109.248 -10.689 0.50 20.11 ? 113 ILE C CB  1 
ATOM   3118  C  CB  B ILE C  1 140 ? 55.001  109.222 -10.827 0.50 16.74 ? 113 ILE C CB  1 
ATOM   3119  C  CG1 A ILE C  1 140 ? 53.860  109.075 -10.175 0.50 21.14 ? 113 ILE C CG1 1 
ATOM   3120  C  CG1 B ILE C  1 140 ? 53.493  109.142 -10.806 0.50 16.26 ? 113 ILE C CG1 1 
ATOM   3121  C  CG2 A ILE C  1 140 ? 55.402  110.656 -11.292 0.50 19.89 ? 113 ILE C CG2 1 
ATOM   3122  C  CG2 B ILE C  1 140 ? 55.455  110.637 -11.247 0.50 16.83 ? 113 ILE C CG2 1 
ATOM   3123  C  CD1 A ILE C  1 140 ? 52.891  108.886 -11.302 0.50 23.25 ? 113 ILE C CD1 1 
ATOM   3124  C  CD1 B ILE C  1 140 ? 52.827  109.697 -9.549  0.50 15.19 ? 113 ILE C CD1 1 
ATOM   3125  N  N   . GLY C  1 141 ? 57.239  108.829 -13.382 1.00 16.02 ? 114 GLY C N   1 
ATOM   3126  C  CA  . GLY C  1 141 ? 58.593  109.054 -13.928 1.00 14.93 ? 114 GLY C CA  1 
ATOM   3127  C  C   . GLY C  1 141 ? 59.216  107.815 -14.519 1.00 15.22 ? 114 GLY C C   1 
ATOM   3128  O  O   . GLY C  1 141 ? 60.360  107.872 -14.969 1.00 15.14 ? 114 GLY C O   1 
ATOM   3129  N  N   . ARG C  1 142 ? 58.461  106.707 -14.601 1.00 14.20 ? 115 ARG C N   1 
ATOM   3130  C  CA  . ARG C  1 142 ? 58.940  105.477 -15.264 1.00 16.27 ? 115 ARG C CA  1 
ATOM   3131  C  C   . ARG C  1 142 ? 58.166  105.366 -16.575 1.00 16.68 ? 115 ARG C C   1 
ATOM   3132  O  O   . ARG C  1 142 ? 57.461  106.320 -16.934 1.00 17.14 ? 115 ARG C O   1 
ATOM   3133  C  CB  . ARG C  1 142 ? 58.700  104.257 -14.336 1.00 16.66 ? 115 ARG C CB  1 
ATOM   3134  C  CG  . ARG C  1 142 ? 59.456  104.566 -13.006 1.00 19.25 ? 115 ARG C CG  1 
ATOM   3135  C  CD  . ARG C  1 142 ? 59.633  103.341 -12.161 1.00 19.08 ? 115 ARG C CD  1 
ATOM   3136  N  NE  . ARG C  1 142 ? 60.204  103.683 -10.834 1.00 18.68 ? 115 ARG C NE  1 
ATOM   3137  C  CZ  . ARG C  1 142 ? 61.497  103.700 -10.527 1.00 21.67 ? 115 ARG C CZ  1 
ATOM   3138  N  NH1 . ARG C  1 142 ? 62.451  103.447 -11.427 1.00 19.99 ? 115 ARG C NH1 1 
ATOM   3139  N  NH2 . ARG C  1 142 ? 61.851  103.980 -9.253  1.00 20.50 ? 115 ARG C NH2 1 
ATOM   3140  N  N   . THR C  1 143 ? 58.390  104.292 -17.327 1.00 15.93 ? 116 THR C N   1 
ATOM   3141  C  CA  . THR C  1 143 ? 57.853  104.218 -18.687 1.00 15.65 ? 116 THR C CA  1 
ATOM   3142  C  C   . THR C  1 143 ? 56.828  103.076 -18.733 1.00 15.59 ? 116 THR C C   1 
ATOM   3143  O  O   . THR C  1 143 ? 57.131  101.958 -18.335 1.00 18.83 ? 116 THR C O   1 
ATOM   3144  C  CB  . THR C  1 143 ? 58.968  103.939 -19.729 1.00 15.94 ? 116 THR C CB  1 
ATOM   3145  O  OG1 . THR C  1 143 ? 59.832  105.083 -19.813 1.00 16.03 ? 116 THR C OG1 1 
ATOM   3146  C  CG2 . THR C  1 143 ? 58.383  103.687 -21.126 1.00 13.48 ? 116 THR C CG2 1 
ATOM   3147  N  N   . LEU C  1 144 ? 55.665  103.357 -19.287 1.00 14.05 ? 117 LEU C N   1 
ATOM   3148  C  CA  . LEU C  1 144 ? 54.695  102.305 -19.616 1.00 13.51 ? 117 LEU C CA  1 
ATOM   3149  C  C   . LEU C  1 144 ? 54.926  101.874 -21.054 1.00 12.86 ? 117 LEU C C   1 
ATOM   3150  O  O   . LEU C  1 144 ? 55.097  102.732 -21.947 1.00 13.88 ? 117 LEU C O   1 
ATOM   3151  C  CB  . LEU C  1 144 ? 53.272  102.863 -19.445 1.00 13.90 ? 117 LEU C CB  1 
ATOM   3152  C  CG  . LEU C  1 144 ? 52.100  101.898 -19.735 1.00 14.67 ? 117 LEU C CG  1 
ATOM   3153  C  CD1 . LEU C  1 144 ? 52.035  100.802 -18.625 1.00 16.75 ? 117 LEU C CD1 1 
ATOM   3154  C  CD2 . LEU C  1 144 ? 50.778  102.720 -19.713 1.00 14.59 ? 117 LEU C CD2 1 
ATOM   3155  N  N   . VAL C  1 145 ? 54.889  100.566 -21.301 1.00 13.13 ? 118 VAL C N   1 
ATOM   3156  C  CA  . VAL C  1 145 ? 55.162  100.015 -22.638 1.00 13.31 ? 118 VAL C CA  1 
ATOM   3157  C  C   . VAL C  1 145 ? 54.103  98.980  -22.993 1.00 13.49 ? 118 VAL C C   1 
ATOM   3158  O  O   . VAL C  1 145 ? 53.771  98.137  -22.184 1.00 14.57 ? 118 VAL C O   1 
ATOM   3159  C  CB  . VAL C  1 145 ? 56.528  99.273  -22.653 1.00 13.77 ? 118 VAL C CB  1 
ATOM   3160  C  CG1 . VAL C  1 145 ? 56.826  98.714  -24.056 1.00 13.76 ? 118 VAL C CG1 1 
ATOM   3161  C  CG2 . VAL C  1 145 ? 57.679  100.227 -22.266 1.00 14.28 ? 118 VAL C CG2 1 
ATOM   3162  N  N   . VAL C  1 146 ? 53.569  99.056  -24.213 1.00 13.77 ? 119 VAL C N   1 
ATOM   3163  C  CA  . VAL C  1 146 ? 52.751  98.006  -24.727 1.00 13.47 ? 119 VAL C CA  1 
ATOM   3164  C  C   . VAL C  1 146 ? 53.577  97.212  -25.780 1.00 13.82 ? 119 VAL C C   1 
ATOM   3165  O  O   . VAL C  1 146 ? 54.251  97.777  -26.645 1.00 13.84 ? 119 VAL C O   1 
ATOM   3166  C  CB  . VAL C  1 146 ? 51.387  98.539  -25.239 1.00 15.77 ? 119 VAL C CB  1 
ATOM   3167  C  CG1 . VAL C  1 146 ? 51.589  99.544  -26.425 1.00 15.98 ? 119 VAL C CG1 1 
ATOM   3168  C  CG2 . VAL C  1 146 ? 50.473  97.404  -25.629 1.00 17.09 ? 119 VAL C CG2 1 
ATOM   3169  N  N   . HIS C  1 147 ? 53.544  95.899  -25.616 1.00 13.89 ? 120 HIS C N   1 
ATOM   3170  C  CA  . HIS C  1 147 ? 54.374  94.964  -26.372 1.00 14.78 ? 120 HIS C CA  1 
ATOM   3171  C  C   . HIS C  1 147 ? 53.685  94.293  -27.560 1.00 14.50 ? 120 HIS C C   1 
ATOM   3172  O  O   . HIS C  1 147 ? 52.467  94.237  -27.669 1.00 15.03 ? 120 HIS C O   1 
ATOM   3173  C  CB  . HIS C  1 147 ? 54.947  93.906  -25.403 1.00 14.38 ? 120 HIS C CB  1 
ATOM   3174  C  CG  . HIS C  1 147 ? 55.947  94.491  -24.455 1.00 15.75 ? 120 HIS C CG  1 
ATOM   3175  N  ND1 . HIS C  1 147 ? 57.309  94.428  -24.692 1.00 15.54 ? 120 HIS C ND1 1 
ATOM   3176  C  CD2 . HIS C  1 147 ? 55.795  95.171  -23.281 1.00 15.47 ? 120 HIS C CD2 1 
ATOM   3177  C  CE1 . HIS C  1 147 ? 57.962  95.004  -23.684 1.00 15.64 ? 120 HIS C CE1 1 
ATOM   3178  N  NE2 . HIS C  1 147 ? 57.068  95.473  -22.819 1.00 15.61 ? 120 HIS C NE2 1 
ATOM   3179  N  N   . GLU C  1 148 ? 54.526  93.722  -28.410 1.00 17.17 ? 121 GLU C N   1 
ATOM   3180  C  CA  . GLU C  1 148 ? 54.149  93.065  -29.659 1.00 18.03 ? 121 GLU C CA  1 
ATOM   3181  C  C   . GLU C  1 148 ? 53.296  91.807  -29.469 1.00 17.77 ? 121 GLU C C   1 
ATOM   3182  O  O   . GLU C  1 148 ? 52.327  91.598  -30.214 1.00 18.02 ? 121 GLU C O   1 
ATOM   3183  C  CB  . GLU C  1 148 ? 55.487  92.641  -30.292 1.00 20.78 ? 121 GLU C CB  1 
ATOM   3184  C  CG  . GLU C  1 148 ? 55.399  91.947  -31.630 1.00 24.82 ? 121 GLU C CG  1 
ATOM   3185  C  CD  . GLU C  1 148 ? 56.722  91.236  -31.978 1.00 31.65 ? 121 GLU C CD  1 
ATOM   3186  O  OE1 . GLU C  1 148 ? 57.715  91.125  -31.157 1.00 30.10 ? 121 GLU C OE1 1 
ATOM   3187  O  OE2 . GLU C  1 148 ? 56.723  90.688  -33.081 1.00 38.13 ? 121 GLU C OE2 1 
ATOM   3188  N  N   . LYS C  1 149 ? 53.619  91.011  -28.444 1.00 18.53 ? 122 LYS C N   1 
ATOM   3189  C  CA  . LYS C  1 149 ? 53.002  89.683  -28.235 1.00 19.72 ? 122 LYS C CA  1 
ATOM   3190  C  C   . LYS C  1 149 ? 52.379  89.538  -26.862 1.00 17.97 ? 122 LYS C C   1 
ATOM   3191  O  O   . LYS C  1 149 ? 52.588  90.405  -26.006 1.00 16.35 ? 122 LYS C O   1 
ATOM   3192  C  CB  . LYS C  1 149 ? 54.115  88.619  -28.394 1.00 22.44 ? 122 LYS C CB  1 
ATOM   3193  C  CG  . LYS C  1 149 ? 54.766  88.708  -29.774 1.00 27.70 ? 122 LYS C CG  1 
ATOM   3194  C  CD  . LYS C  1 149 ? 56.095  87.975  -29.874 1.00 37.61 ? 122 LYS C CD  1 
ATOM   3195  C  CE  . LYS C  1 149 ? 56.023  86.562  -29.379 1.00 42.30 ? 122 LYS C CE  1 
ATOM   3196  N  NZ  . LYS C  1 149 ? 57.349  85.917  -29.659 1.00 53.22 ? 122 LYS C NZ  1 
ATOM   3197  N  N   . ALA C  1 150 ? 51.641  88.433  -26.655 1.00 16.86 ? 123 ALA C N   1 
ATOM   3198  C  CA  . ALA C  1 150 ? 51.110  88.104  -25.325 1.00 19.00 ? 123 ALA C CA  1 
ATOM   3199  C  C   . ALA C  1 150 ? 52.228  87.920  -24.302 1.00 19.74 ? 123 ALA C C   1 
ATOM   3200  O  O   . ALA C  1 150 ? 53.275  87.350  -24.591 1.00 18.65 ? 123 ALA C O   1 
ATOM   3201  C  CB  . ALA C  1 150 ? 50.217  86.855  -25.395 1.00 19.66 ? 123 ALA C CB  1 
ATOM   3202  N  N   . ASP C  1 151 ? 52.029  88.454  -23.110 1.00 16.53 ? 124 ASP C N   1 
ATOM   3203  C  CA  . ASP C  1 151 ? 52.856  88.083  -21.977 1.00 16.55 ? 124 ASP C CA  1 
ATOM   3204  C  C   . ASP C  1 151 ? 52.392  86.712  -21.483 1.00 15.60 ? 124 ASP C C   1 
ATOM   3205  O  O   . ASP C  1 151 ? 51.178  86.519  -21.221 1.00 15.32 ? 124 ASP C O   1 
ATOM   3206  C  CB  . ASP C  1 151 ? 52.609  89.160  -20.904 1.00 17.04 ? 124 ASP C CB  1 
ATOM   3207  C  CG  . ASP C  1 151 ? 53.389  88.943  -19.614 1.00 20.62 ? 124 ASP C CG  1 
ATOM   3208  O  OD1 . ASP C  1 151 ? 53.985  87.847  -19.383 1.00 18.80 ? 124 ASP C OD1 1 
ATOM   3209  O  OD2 . ASP C  1 151 ? 53.416  89.916  -18.791 1.00 21.61 ? 124 ASP C OD2 1 
ATOM   3210  N  N   . ASP C  1 152 ? 53.308  85.747  -21.352 1.00 15.50 ? 125 ASP C N   1 
ATOM   3211  C  CA  . ASP C  1 152 ? 52.909  84.412  -20.886 1.00 15.33 ? 125 ASP C CA  1 
ATOM   3212  C  C   . ASP C  1 152 ? 52.831  84.290  -19.357 1.00 15.15 ? 125 ASP C C   1 
ATOM   3213  O  O   . ASP C  1 152 ? 52.656  83.192  -18.792 1.00 15.64 ? 125 ASP C O   1 
ATOM   3214  C  CB  . ASP C  1 152 ? 53.825  83.322  -21.533 1.00 16.29 ? 125 ASP C CB  1 
ATOM   3215  C  CG  . ASP C  1 152 ? 55.289  83.375  -21.014 1.00 16.05 ? 125 ASP C CG  1 
ATOM   3216  O  OD1 . ASP C  1 152 ? 55.570  83.949  -19.949 1.00 16.43 ? 125 ASP C OD1 1 
ATOM   3217  O  OD2 . ASP C  1 152 ? 56.184  82.810  -21.681 1.00 18.48 ? 125 ASP C OD2 1 
ATOM   3218  N  N   . LEU C  1 153 ? 53.007  85.417  -18.686 1.00 15.14 ? 126 LEU C N   1 
ATOM   3219  C  CA  . LEU C  1 153 ? 52.805  85.595  -17.236 1.00 15.82 ? 126 LEU C CA  1 
ATOM   3220  C  C   . LEU C  1 153 ? 53.802  84.739  -16.453 1.00 16.34 ? 126 LEU C C   1 
ATOM   3221  O  O   . LEU C  1 153 ? 53.549  84.337  -15.304 1.00 15.42 ? 126 LEU C O   1 
ATOM   3222  C  CB  . LEU C  1 153 ? 51.346  85.352  -16.807 1.00 17.07 ? 126 LEU C CB  1 
ATOM   3223  C  CG  . LEU C  1 153 ? 50.283  86.038  -17.689 1.00 19.01 ? 126 LEU C CG  1 
ATOM   3224  C  CD1 . LEU C  1 153 ? 48.905  85.664  -17.169 1.00 21.35 ? 126 LEU C CD1 1 
ATOM   3225  C  CD2 . LEU C  1 153 ? 50.458  87.562  -17.696 1.00 18.59 ? 126 LEU C CD2 1 
ATOM   3226  N  N   . GLY C  1 154 ? 54.953  84.489  -17.081 1.00 16.77 ? 127 GLY C N   1 
ATOM   3227  C  CA  . GLY C  1 154 ? 56.040  83.789  -16.417 1.00 15.73 ? 127 GLY C CA  1 
ATOM   3228  C  C   . GLY C  1 154 ? 55.827  82.265  -16.446 1.00 17.84 ? 127 GLY C C   1 
ATOM   3229  O  O   . GLY C  1 154 ? 56.529  81.543  -15.758 1.00 17.64 ? 127 GLY C O   1 
ATOM   3230  N  N   . LYS C  1 155 ? 54.913  81.776  -17.269 1.00 15.90 ? 128 LYS C N   1 
ATOM   3231  C  CA  . LYS C  1 155 ? 54.581  80.338  -17.280 1.00 16.85 ? 128 LYS C CA  1 
ATOM   3232  C  C   . LYS C  1 155 ? 55.113  79.645  -18.531 1.00 15.95 ? 128 LYS C C   1 
ATOM   3233  O  O   . LYS C  1 155 ? 54.645  78.550  -18.877 1.00 16.15 ? 128 LYS C O   1 
ATOM   3234  C  CB  . LYS C  1 155 ? 53.031  80.195  -17.242 1.00 18.10 ? 128 LYS C CB  1 
ATOM   3235  C  CG  . LYS C  1 155 ? 52.437  80.723  -15.920 1.00 22.16 ? 128 LYS C CG  1 
ATOM   3236  C  CD  . LYS C  1 155 ? 50.907  80.730  -15.957 1.00 25.63 ? 128 LYS C CD  1 
ATOM   3237  C  CE  . LYS C  1 155 ? 50.318  79.339  -15.690 1.00 31.55 ? 128 LYS C CE  1 
ATOM   3238  N  NZ  . LYS C  1 155 ? 48.807  79.351  -15.645 1.00 43.27 ? 128 LYS C NZ  1 
ATOM   3239  N  N   . GLY C  1 156 ? 56.039  80.282  -19.249 1.00 15.34 ? 129 GLY C N   1 
ATOM   3240  C  CA  . GLY C  1 156 ? 56.444  79.766  -20.578 1.00 14.40 ? 129 GLY C CA  1 
ATOM   3241  C  C   . GLY C  1 156 ? 57.577  78.715  -20.505 1.00 15.39 ? 129 GLY C C   1 
ATOM   3242  O  O   . GLY C  1 156 ? 57.901  78.081  -21.509 1.00 16.04 ? 129 GLY C O   1 
ATOM   3243  N  N   . GLY C  1 157 ? 58.178  78.570  -19.334 1.00 13.23 ? 130 GLY C N   1 
ATOM   3244  C  CA  . GLY C  1 157 ? 59.222  77.506  -19.045 1.00 14.84 ? 130 GLY C CA  1 
ATOM   3245  C  C   . GLY C  1 157 ? 60.572  77.721  -19.762 1.00 16.30 ? 130 GLY C C   1 
ATOM   3246  O  O   . GLY C  1 157 ? 61.444  76.842  -19.728 1.00 18.11 ? 130 GLY C O   1 
ATOM   3247  N  N   . ASN C  1 158 ? 60.772  78.875  -20.401 1.00 15.78 ? 131 ASN C N   1 
ATOM   3248  C  CA  . ASN C  1 158 ? 62.075  79.186  -20.941 1.00 15.52 ? 131 ASN C CA  1 
ATOM   3249  C  C   . ASN C  1 158 ? 62.707  80.350  -20.178 1.00 18.30 ? 131 ASN C C   1 
ATOM   3250  O  O   . ASN C  1 158 ? 62.044  80.995  -19.360 1.00 17.96 ? 131 ASN C O   1 
ATOM   3251  C  CB  . ASN C  1 158 ? 62.049  79.446  -22.455 1.00 16.60 ? 131 ASN C CB  1 
ATOM   3252  C  CG  . ASN C  1 158 ? 61.253  80.714  -22.859 1.00 18.53 ? 131 ASN C CG  1 
ATOM   3253  O  OD1 . ASN C  1 158 ? 60.511  81.286  -22.060 1.00 19.23 ? 131 ASN C OD1 1 
ATOM   3254  N  ND2 . ASN C  1 158 ? 61.303  81.052  -24.134 1.00 20.99 ? 131 ASN C ND2 1 
ATOM   3255  N  N   . GLU C  1 159 ? 63.978  80.667  -20.452 1.00 16.71 ? 132 GLU C N   1 
ATOM   3256  C  CA  . GLU C  1 159 ? 64.615  81.722  -19.677 1.00 18.66 ? 132 GLU C CA  1 
ATOM   3257  C  C   . GLU C  1 159 ? 63.904  83.058  -19.919 1.00 18.92 ? 132 GLU C C   1 
ATOM   3258  O  O   . GLU C  1 159 ? 63.733  83.849  -18.997 1.00 20.08 ? 132 GLU C O   1 
ATOM   3259  C  CB  . GLU C  1 159 ? 66.081  81.923  -20.096 1.00 23.22 ? 132 GLU C CB  1 
ATOM   3260  C  CG  . GLU C  1 159 ? 66.938  80.686  -19.984 1.00 31.09 ? 132 GLU C CG  1 
ATOM   3261  C  CD  . GLU C  1 159 ? 68.320  80.850  -20.665 1.00 41.25 ? 132 GLU C CD  1 
ATOM   3262  O  OE1 . GLU C  1 159 ? 69.073  79.857  -20.727 1.00 41.45 ? 132 GLU C OE1 1 
ATOM   3263  O  OE2 . GLU C  1 159 ? 68.641  81.964  -21.153 1.00 42.71 ? 132 GLU C OE2 1 
ATOM   3264  N  N   . GLU C  1 160 ? 63.503  83.308  -21.150 1.00 19.06 ? 133 GLU C N   1 
ATOM   3265  C  CA  . GLU C  1 160 ? 62.878  84.610  -21.484 1.00 20.89 ? 133 GLU C CA  1 
ATOM   3266  C  C   . GLU C  1 160 ? 61.525  84.790  -20.723 1.00 19.81 ? 133 GLU C C   1 
ATOM   3267  O  O   . GLU C  1 160 ? 61.201  85.896  -20.311 1.00 19.96 ? 133 GLU C O   1 
ATOM   3268  C  CB  . GLU C  1 160 ? 62.640  84.703  -22.984 1.00 23.74 ? 133 GLU C CB  1 
ATOM   3269  C  CG  . GLU C  1 160 ? 62.290  86.092  -23.473 1.00 28.17 ? 133 GLU C CG  1 
ATOM   3270  C  CD  . GLU C  1 160 ? 63.463  87.052  -23.210 1.00 35.98 ? 133 GLU C CD  1 
ATOM   3271  O  OE1 . GLU C  1 160 ? 64.570  86.756  -23.685 1.00 31.37 ? 133 GLU C OE1 1 
ATOM   3272  O  OE2 . GLU C  1 160 ? 63.302  88.064  -22.490 1.00 34.19 ? 133 GLU C OE2 1 
ATOM   3273  N  N   . SER C  1 161 ? 60.807  83.692  -20.443 1.00 18.25 ? 134 SER C N   1 
ATOM   3274  C  CA  . SER C  1 161 ? 59.520  83.831  -19.719 1.00 17.13 ? 134 SER C CA  1 
ATOM   3275  C  C   . SER C  1 161 ? 59.737  84.467  -18.343 1.00 18.80 ? 134 SER C C   1 
ATOM   3276  O  O   . SER C  1 161 ? 58.911  85.291  -17.924 1.00 18.66 ? 134 SER C O   1 
ATOM   3277  C  CB  . SER C  1 161 ? 58.835  82.473  -19.573 1.00 18.08 ? 134 SER C CB  1 
ATOM   3278  O  OG  . SER C  1 161 ? 57.642  82.588  -18.836 1.00 19.38 ? 134 SER C OG  1 
ATOM   3279  N  N   . THR C  1 162 ? 60.836  84.109  -17.646 1.00 17.20 ? 135 THR C N   1 
ATOM   3280  C  CA  . THR C  1 162 ? 61.121  84.584  -16.305 1.00 18.00 ? 135 THR C CA  1 
ATOM   3281  C  C   . THR C  1 162 ? 61.646  86.025  -16.307 1.00 19.46 ? 135 THR C C   1 
ATOM   3282  O  O   . THR C  1 162 ? 61.810  86.598  -15.230 1.00 19.58 ? 135 THR C O   1 
ATOM   3283  C  CB  . THR C  1 162 ? 62.253  83.706  -15.611 1.00 21.58 ? 135 THR C CB  1 
ATOM   3284  O  OG1 . THR C  1 162 ? 63.502  84.035  -16.238 1.00 26.64 ? 135 THR C OG1 1 
ATOM   3285  C  CG2 . THR C  1 162 ? 62.037  82.302  -15.849 1.00 25.23 ? 135 THR C CG2 1 
ATOM   3286  N  N   . LYS C  1 163 ? 61.895  86.601  -17.490 1.00 18.23 ? 136 LYS C N   1 
ATOM   3287  C  CA  . LYS C  1 163 ? 62.379  87.990  -17.592 1.00 20.77 ? 136 LYS C CA  1 
ATOM   3288  C  C   . LYS C  1 163 ? 61.342  88.911  -18.189 1.00 18.27 ? 136 LYS C C   1 
ATOM   3289  O  O   . LYS C  1 163 ? 61.047  89.992  -17.621 1.00 20.97 ? 136 LYS C O   1 
ATOM   3290  C  CB  . LYS C  1 163 ? 63.651  88.042  -18.458 1.00 20.86 ? 136 LYS C CB  1 
ATOM   3291  C  CG  . LYS C  1 163 ? 64.807  87.297  -17.768 1.00 29.47 ? 136 LYS C CG  1 
ATOM   3292  C  CD  . LYS C  1 163 ? 66.138  87.554  -18.451 1.00 33.31 ? 136 LYS C CD  1 
ATOM   3293  C  CE  . LYS C  1 163 ? 66.122  86.977  -19.840 1.00 37.26 ? 136 LYS C CE  1 
ATOM   3294  N  NZ  . LYS C  1 163 ? 67.526  86.574  -20.180 1.00 48.95 ? 136 LYS C NZ  1 
ATOM   3295  N  N   . THR C  1 164 ? 60.797  88.547  -19.350 1.00 18.64 ? 137 THR C N   1 
ATOM   3296  C  CA  . THR C  1 164 ? 59.869  89.454  -20.066 1.00 19.93 ? 137 THR C CA  1 
ATOM   3297  C  C   . THR C  1 164 ? 58.526  88.843  -20.387 1.00 19.48 ? 137 THR C C   1 
ATOM   3298  O  O   . THR C  1 164 ? 57.688  89.502  -21.036 1.00 18.00 ? 137 THR C O   1 
ATOM   3299  C  CB  . THR C  1 164 ? 60.441  89.870  -21.415 1.00 22.87 ? 137 THR C CB  1 
ATOM   3300  O  OG1 . THR C  1 164 ? 60.593  88.689  -22.207 1.00 21.90 ? 137 THR C OG1 1 
ATOM   3301  C  CG2 . THR C  1 164 ? 61.847  90.528  -21.240 1.00 26.33 ? 137 THR C CG2 1 
ATOM   3302  N  N   . GLY C  1 165 ? 58.319  87.581  -20.017 1.00 15.82 ? 138 GLY C N   1 
ATOM   3303  C  CA  . GLY C  1 165 ? 57.068  86.922  -20.378 1.00 16.29 ? 138 GLY C CA  1 
ATOM   3304  C  C   . GLY C  1 165 ? 56.975  86.595  -21.856 1.00 15.84 ? 138 GLY C C   1 
ATOM   3305  O  O   . GLY C  1 165 ? 55.886  86.247  -22.348 1.00 16.70 ? 138 GLY C O   1 
ATOM   3306  N  N   . ASN C  1 166 ? 58.106  86.675  -22.576 1.00 17.76 ? 139 ASN C N   1 
ATOM   3307  C  CA  . ASN C  1 166 ? 58.096  86.425  -24.029 1.00 16.29 ? 139 ASN C CA  1 
ATOM   3308  C  C   . ASN C  1 166 ? 57.210  87.433  -24.795 1.00 17.02 ? 139 ASN C C   1 
ATOM   3309  O  O   . ASN C  1 166 ? 56.732  87.098  -25.884 1.00 15.27 ? 139 ASN C O   1 
ATOM   3310  C  CB  . ASN C  1 166 ? 57.692  84.958  -24.393 1.00 18.05 ? 139 ASN C CB  1 
ATOM   3311  C  CG  . ASN C  1 166 ? 58.766  83.957  -24.012 1.00 20.53 ? 139 ASN C CG  1 
ATOM   3312  O  OD1 . ASN C  1 166 ? 59.837  83.988  -24.582 1.00 21.07 ? 139 ASN C OD1 1 
ATOM   3313  N  ND2 . ASN C  1 166 ? 58.508  83.108  -23.026 1.00 17.39 ? 139 ASN C ND2 1 
ATOM   3314  N  N   . ALA C  1 167 ? 57.020  88.668  -24.270 1.00 16.03 ? 140 ALA C N   1 
ATOM   3315  C  CA  . ALA C  1 167 ? 56.059  89.590  -24.900 1.00 15.94 ? 140 ALA C CA  1 
ATOM   3316  C  C   . ALA C  1 167 ? 56.661  90.352  -26.098 1.00 17.81 ? 140 ALA C C   1 
ATOM   3317  O  O   . ALA C  1 167 ? 55.956  91.113  -26.785 1.00 15.34 ? 140 ALA C O   1 
ATOM   3318  C  CB  . ALA C  1 167 ? 55.476  90.587  -23.855 1.00 15.44 ? 140 ALA C CB  1 
ATOM   3319  N  N   . GLY C  1 168 ? 57.935  90.108  -26.367 1.00 18.89 ? 141 GLY C N   1 
ATOM   3320  C  CA  . GLY C  1 168 ? 58.541  90.569  -27.640 1.00 20.11 ? 141 GLY C CA  1 
ATOM   3321  C  C   . GLY C  1 168 ? 58.759  92.102  -27.670 1.00 19.07 ? 141 GLY C C   1 
ATOM   3322  O  O   . GLY C  1 168 ? 58.970  92.741  -26.615 1.00 17.77 ? 141 GLY C O   1 
ATOM   3323  N  N   . SER C  1 169 ? 58.655  92.683  -28.867 1.00 19.60 ? 142 SER C N   1 
ATOM   3324  C  CA  B SER C  1 169 ? 59.080  94.065  -29.145 0.38 19.94 ? 142 SER C CA  1 
ATOM   3325  C  CA  C SER C  1 169 ? 59.161  94.054  -29.059 0.62 20.20 ? 142 SER C CA  1 
ATOM   3326  C  C   . SER C  1 169 ? 58.233  95.116  -28.448 1.00 19.10 ? 142 SER C C   1 
ATOM   3327  O  O   . SER C  1 169 ? 57.075  94.838  -28.080 1.00 17.75 ? 142 SER C O   1 
ATOM   3328  C  CB  B SER C  1 169 ? 59.043  94.318  -30.654 0.38 20.84 ? 142 SER C CB  1 
ATOM   3329  C  CB  C SER C  1 169 ? 59.430  94.353  -30.543 0.62 21.50 ? 142 SER C CB  1 
ATOM   3330  O  OG  B SER C  1 169 ? 59.938  93.437  -31.288 0.38 21.55 ? 142 SER C OG  1 
ATOM   3331  O  OG  C SER C  1 169 ? 58.206  94.393  -31.225 0.62 20.84 ? 142 SER C OG  1 
ATOM   3332  N  N   . ARG C  1 170 ? 58.764  96.317  -28.325 1.00 17.51 ? 143 ARG C N   1 
ATOM   3333  C  CA  . ARG C  1 170 ? 58.062  97.432  -27.673 1.00 16.45 ? 143 ARG C CA  1 
ATOM   3334  C  C   . ARG C  1 170 ? 57.355  98.258  -28.739 1.00 16.54 ? 143 ARG C C   1 
ATOM   3335  O  O   . ARG C  1 170 ? 58.018  98.917  -29.556 1.00 18.45 ? 143 ARG C O   1 
ATOM   3336  C  CB  . ARG C  1 170 ? 59.096  98.273  -26.929 1.00 16.96 ? 143 ARG C CB  1 
ATOM   3337  C  CG  . ARG C  1 170 ? 59.862  97.403  -25.917 1.00 16.93 ? 143 ARG C CG  1 
ATOM   3338  C  CD  . ARG C  1 170 ? 61.025  98.125  -25.232 1.00 18.29 ? 143 ARG C CD  1 
ATOM   3339  N  NE  . ARG C  1 170 ? 61.766  97.165  -24.398 1.00 18.13 ? 143 ARG C NE  1 
ATOM   3340  C  CZ  . ARG C  1 170 ? 62.489  97.445  -23.318 1.00 18.41 ? 143 ARG C CZ  1 
ATOM   3341  N  NH1 . ARG C  1 170 ? 62.668  98.713  -22.892 1.00 16.15 ? 143 ARG C NH1 1 
ATOM   3342  N  NH2 . ARG C  1 170 ? 63.053  96.423  -22.642 1.00 19.08 ? 143 ARG C NH2 1 
ATOM   3343  N  N   . LEU C  1 171 ? 56.035  98.202  -28.796 1.00 15.65 ? 144 LEU C N   1 
ATOM   3344  C  CA  . LEU C  1 171 ? 55.318  98.863  -29.903 1.00 15.71 ? 144 LEU C CA  1 
ATOM   3345  C  C   . LEU C  1 171 ? 55.085  100.345 -29.615 1.00 15.68 ? 144 LEU C C   1 
ATOM   3346  O  O   . LEU C  1 171 ? 55.023  101.151 -30.537 1.00 15.94 ? 144 LEU C O   1 
ATOM   3347  C  CB  . LEU C  1 171 ? 53.924  98.230  -30.119 1.00 16.06 ? 144 LEU C CB  1 
ATOM   3348  C  CG  . LEU C  1 171 ? 54.088  96.713  -30.462 1.00 18.91 ? 144 LEU C CG  1 
ATOM   3349  C  CD1 . LEU C  1 171 ? 52.697  96.161  -30.790 1.00 20.50 ? 144 LEU C CD1 1 
ATOM   3350  C  CD2 . LEU C  1 171 ? 55.062  96.463  -31.606 1.00 21.10 ? 144 LEU C CD2 1 
ATOM   3351  N  N   . ALA C  1 172 ? 54.868  100.712 -28.353 1.00 14.89 ? 145 ALA C N   1 
ATOM   3352  C  CA  . ALA C  1 172 ? 54.633  102.157 -28.079 1.00 14.00 ? 145 ALA C CA  1 
ATOM   3353  C  C   . ALA C  1 172 ? 54.900  102.347 -26.602 1.00 15.91 ? 145 ALA C C   1 
ATOM   3354  O  O   . ALA C  1 172 ? 54.768  101.384 -25.833 1.00 15.06 ? 145 ALA C O   1 
ATOM   3355  C  CB  . ALA C  1 172 ? 53.195  102.575 -28.406 1.00 14.27 ? 145 ALA C CB  1 
ATOM   3356  N  N   . CYS C  1 173 ? 55.280  103.561 -26.195 1.00 14.56 ? 146 CYS C N   1 
ATOM   3357  C  CA  . CYS C  1 173 ? 55.604  103.769 -24.762 1.00 16.31 ? 146 CYS C CA  1 
ATOM   3358  C  C   . CYS C  1 173 ? 55.492  105.240 -24.458 1.00 15.32 ? 146 CYS C C   1 
ATOM   3359  O  O   . CYS C  1 173 ? 55.389  106.077 -25.386 1.00 15.23 ? 146 CYS C O   1 
ATOM   3360  C  CB  . CYS C  1 173 ? 57.040  103.294 -24.443 1.00 18.24 ? 146 CYS C CB  1 
ATOM   3361  S  SG  . CYS C  1 173 ? 58.312  104.153 -25.436 1.00 23.71 ? 146 CYS C SG  1 
ATOM   3362  N  N   . GLY C  1 174 ? 55.516  105.565 -23.176 1.00 16.07 ? 147 GLY C N   1 
ATOM   3363  C  CA  . GLY C  1 174 ? 55.539  106.956 -22.765 1.00 17.00 ? 147 GLY C CA  1 
ATOM   3364  C  C   . GLY C  1 174 ? 55.980  107.017 -21.309 1.00 16.44 ? 147 GLY C C   1 
ATOM   3365  O  O   . GLY C  1 174 ? 55.904  106.006 -20.557 1.00 13.57 ? 147 GLY C O   1 
ATOM   3366  N  N   . VAL C  1 175 ? 56.393  108.211 -20.901 1.00 15.57 ? 148 VAL C N   1 
ATOM   3367  C  CA  . VAL C  1 175 ? 56.724  108.425 -19.496 1.00 17.00 ? 148 VAL C CA  1 
ATOM   3368  C  C   . VAL C  1 175 ? 55.450  108.731 -18.728 1.00 16.52 ? 148 VAL C C   1 
ATOM   3369  O  O   . VAL C  1 175 ? 54.593  109.477 -19.200 1.00 17.01 ? 148 VAL C O   1 
ATOM   3370  C  CB  . VAL C  1 175 ? 57.774  109.583 -19.349 1.00 17.27 ? 148 VAL C CB  1 
ATOM   3371  C  CG1 . VAL C  1 175 ? 58.170  109.728 -17.887 1.00 17.25 ? 148 VAL C CG1 1 
ATOM   3372  C  CG2 . VAL C  1 175 ? 58.990  109.242 -20.213 1.00 17.17 ? 148 VAL C CG2 1 
ATOM   3373  N  N   . ILE C  1 176 ? 55.317  108.112 -17.550 1.00 15.31 ? 149 ILE C N   1 
ATOM   3374  C  CA  . ILE C  1 176 ? 54.172  108.294 -16.658 1.00 15.37 ? 149 ILE C CA  1 
ATOM   3375  C  C   . ILE C  1 176 ? 54.348  109.617 -15.888 1.00 16.98 ? 149 ILE C C   1 
ATOM   3376  O  O   . ILE C  1 176 ? 55.348  109.775 -15.137 1.00 18.53 ? 149 ILE C O   1 
ATOM   3377  C  CB  . ILE C  1 176 ? 54.058  107.096 -15.673 1.00 15.18 ? 149 ILE C CB  1 
ATOM   3378  C  CG1 . ILE C  1 176 ? 53.830  105.797 -16.490 1.00 14.46 ? 149 ILE C CG1 1 
ATOM   3379  C  CG2 . ILE C  1 176 ? 52.832  107.269 -14.742 1.00 16.38 ? 149 ILE C CG2 1 
ATOM   3380  C  CD1 . ILE C  1 176 ? 54.083  104.464 -15.738 1.00 15.09 ? 149 ILE C CD1 1 
ATOM   3381  N  N   . GLY C  1 177 ? 53.401  110.546 -16.071 1.00 16.04 ? 150 GLY C N   1 
ATOM   3382  C  CA  . GLY C  1 177 ? 53.525  111.908 -15.537 1.00 16.90 ? 150 GLY C CA  1 
ATOM   3383  C  C   . GLY C  1 177 ? 52.456  112.155 -14.490 1.00 19.00 ? 150 GLY C C   1 
ATOM   3384  O  O   . GLY C  1 177 ? 51.388  111.555 -14.529 1.00 18.30 ? 150 GLY C O   1 
ATOM   3385  N  N   . ILE C  1 178 ? 52.715  113.110 -13.591 1.00 19.14 ? 151 ILE C N   1 
ATOM   3386  C  CA  . ILE C  1 178 ? 51.666  113.529 -12.623 1.00 19.93 ? 151 ILE C CA  1 
ATOM   3387  C  C   . ILE C  1 178 ? 50.549  114.251 -13.339 1.00 20.80 ? 151 ILE C C   1 
ATOM   3388  O  O   . ILE C  1 178 ? 50.809  115.098 -14.229 1.00 19.57 ? 151 ILE C O   1 
ATOM   3389  C  CB  . ILE C  1 178 ? 52.229  114.469 -11.506 1.00 22.86 ? 151 ILE C CB  1 
ATOM   3390  C  CG1 . ILE C  1 178 ? 53.290  113.724 -10.770 1.00 26.14 ? 151 ILE C CG1 1 
ATOM   3391  C  CG2 . ILE C  1 178 ? 51.121  114.780 -10.483 1.00 26.42 ? 151 ILE C CG2 1 
ATOM   3392  C  CD1 . ILE C  1 178 ? 54.346  114.652 -10.169 1.00 36.46 ? 151 ILE C CD1 1 
ATOM   3393  N  N   . ALA C  1 179 ? 49.304  113.913 -12.989 1.00 19.88 ? 152 ALA C N   1 
ATOM   3394  C  CA  . ALA C  1 179 ? 48.146  114.519 -13.675 1.00 23.00 ? 152 ALA C CA  1 
ATOM   3395  C  C   . ALA C  1 179 ? 47.384  115.326 -12.633 1.00 27.37 ? 152 ALA C C   1 
ATOM   3396  O  O   . ALA C  1 179 ? 47.594  115.129 -11.439 1.00 27.17 ? 152 ALA C O   1 
ATOM   3397  C  CB  . ALA C  1 179 ? 47.232  113.475 -14.306 1.00 20.72 ? 152 ALA C CB  1 
ATOM   3398  N  N   . GLN C  1 180 ? 46.538  116.239 -13.096 1.00 32.07 ? 153 GLN C N   1 
ATOM   3399  C  CA  . GLN C  1 180 ? 45.795  117.159 -12.194 1.00 41.37 ? 153 GLN C CA  1 
ATOM   3400  C  C   . GLN C  1 180 ? 44.694  116.367 -11.521 1.00 45.97 ? 153 GLN C C   1 
ATOM   3401  O  O   . GLN C  1 180 ? 44.030  115.610 -12.236 1.00 45.61 ? 153 GLN C O   1 
ATOM   3402  C  CB  . GLN C  1 180 ? 45.188  118.335 -12.981 1.00 38.12 ? 153 GLN C CB  1 
ATOM   3403  C  CG  . GLN C  1 180 ? 44.473  119.363 -12.103 1.00 44.21 ? 153 GLN C CG  1 
ATOM   3404  C  CD  . GLN C  1 180 ? 44.157  120.635 -12.879 1.00 49.04 ? 153 GLN C CD  1 
ATOM   3405  O  OE1 . GLN C  1 180 ? 43.566  120.589 -13.961 1.00 47.92 ? 153 GLN C OE1 1 
ATOM   3406  N  NE2 . GLN C  1 180 ? 44.567  121.775 -12.340 1.00 51.49 ? 153 GLN C NE2 1 
ATOM   3407  O  OXT . GLN C  1 180 ? 44.471  116.444 -10.298 1.00 53.14 ? 153 GLN C OXT 1 
ATOM   3408  N  N   . ALA D  1 26  ? 64.462  110.152 -1.156  1.00 62.26 ? -1  ALA D N   1 
ATOM   3409  C  CA  . ALA D  1 26  ? 65.786  110.682 -1.571  1.00 61.98 ? -1  ALA D CA  1 
ATOM   3410  C  C   . ALA D  1 26  ? 66.590  109.710 -2.464  1.00 63.79 ? -1  ALA D C   1 
ATOM   3411  O  O   . ALA D  1 26  ? 67.819  109.640 -2.351  1.00 72.29 ? -1  ALA D O   1 
ATOM   3412  C  CB  . ALA D  1 26  ? 66.560  111.088 -0.342  1.00 55.84 ? -1  ALA D CB  1 
ATOM   3413  N  N   . MET D  1 27  ? 65.887  109.016 -3.379  1.00 61.51 ? 0   MET D N   1 
ATOM   3414  C  CA  . MET D  1 27  ? 66.429  107.878 -4.161  1.00 54.95 ? 0   MET D CA  1 
ATOM   3415  C  C   . MET D  1 27  ? 66.930  108.180 -5.601  1.00 48.74 ? 0   MET D C   1 
ATOM   3416  O  O   . MET D  1 27  ? 68.032  107.734 -5.963  1.00 48.26 ? 0   MET D O   1 
ATOM   3417  C  CB  . MET D  1 27  ? 65.446  106.710 -4.172  1.00 48.67 ? 0   MET D CB  1 
ATOM   3418  N  N   . ALA D  1 28  ? 66.150  108.900 -6.426  1.00 47.91 ? 1   ALA D N   1 
ATOM   3419  C  CA  . ALA D  1 28  ? 66.618  109.252 -7.803  1.00 39.34 ? 1   ALA D CA  1 
ATOM   3420  C  C   . ALA D  1 28  ? 67.863  110.188 -7.785  1.00 34.15 ? 1   ALA D C   1 
ATOM   3421  O  O   . ALA D  1 28  ? 67.842  111.237 -7.176  1.00 36.11 ? 1   ALA D O   1 
ATOM   3422  C  CB  . ALA D  1 28  ? 65.491  109.861 -8.653  1.00 36.29 ? 1   ALA D CB  1 
ATOM   3423  N  N   . THR D  1 29  ? 68.946  109.789 -8.437  1.00 32.46 ? 2   THR D N   1 
ATOM   3424  C  CA  . THR D  1 29  ? 70.061  110.721 -8.604  1.00 31.27 ? 2   THR D CA  1 
ATOM   3425  C  C   . THR D  1 29  ? 70.198  111.268 -10.052 1.00 30.21 ? 2   THR D C   1 
ATOM   3426  O  O   . THR D  1 29  ? 70.964  112.211 -10.281 1.00 25.58 ? 2   THR D O   1 
ATOM   3427  C  CB  . THR D  1 29  ? 71.396  110.086 -8.175  1.00 32.17 ? 2   THR D CB  1 
ATOM   3428  O  OG1 . THR D  1 29  ? 71.653  108.956 -9.007  1.00 34.30 ? 2   THR D OG1 1 
ATOM   3429  C  CG2 . THR D  1 29  ? 71.331  109.635 -6.713  1.00 35.64 ? 2   THR D CG2 1 
ATOM   3430  N  N   . LYS D  1 30  ? 69.489  110.663 -11.021 1.00 25.18 ? 3   LYS D N   1 
ATOM   3431  C  CA  . LYS D  1 30  ? 69.546  111.125 -12.413 1.00 22.45 ? 3   LYS D CA  1 
ATOM   3432  C  C   . LYS D  1 30  ? 68.141  111.119 -13.012 1.00 23.27 ? 3   LYS D C   1 
ATOM   3433  O  O   . LYS D  1 30  ? 67.323  110.246 -12.692 1.00 20.22 ? 3   LYS D O   1 
ATOM   3434  C  CB  . LYS D  1 30  ? 70.447  110.241 -13.264 1.00 25.99 ? 3   LYS D CB  1 
ATOM   3435  C  CG  . LYS D  1 30  ? 71.807  110.003 -12.686 1.00 34.90 ? 3   LYS D CG  1 
ATOM   3436  C  CD  . LYS D  1 30  ? 72.760  109.468 -13.735 1.00 45.01 ? 3   LYS D CD  1 
ATOM   3437  C  CE  . LYS D  1 30  ? 74.026  108.964 -13.039 1.00 54.85 ? 3   LYS D CE  1 
ATOM   3438  N  NZ  . LYS D  1 30  ? 75.228  109.545 -13.718 1.00 54.40 ? 3   LYS D NZ  1 
ATOM   3439  N  N   . ALA D  1 31  ? 67.871  112.082 -13.892 1.00 20.40 ? 4   ALA D N   1 
ATOM   3440  C  CA  . ALA D  1 31  ? 66.585  112.172 -14.597 1.00 18.80 ? 4   ALA D CA  1 
ATOM   3441  C  C   . ALA D  1 31  ? 66.926  112.661 -16.017 1.00 19.61 ? 4   ALA D C   1 
ATOM   3442  O  O   . ALA D  1 31  ? 68.071  113.130 -16.298 1.00 19.13 ? 4   ALA D O   1 
ATOM   3443  C  CB  . ALA D  1 31  ? 65.630  113.121 -13.860 1.00 19.69 ? 4   ALA D CB  1 
ATOM   3444  N  N   . VAL D  1 32  ? 65.999  112.463 -16.945 1.00 17.97 ? 5   VAL D N   1 
ATOM   3445  C  CA  . VAL D  1 32  ? 66.221  112.907 -18.326 1.00 18.28 ? 5   VAL D CA  1 
ATOM   3446  C  C   . VAL D  1 32  ? 64.884  113.386 -18.899 1.00 19.98 ? 5   VAL D C   1 
ATOM   3447  O  O   . VAL D  1 32  ? 63.787  112.982 -18.412 1.00 20.13 ? 5   VAL D O   1 
ATOM   3448  C  CB  . VAL D  1 32  ? 66.877  111.793 -19.150 1.00 20.05 ? 5   VAL D CB  1 
ATOM   3449  C  CG1 . VAL D  1 32  ? 65.891  110.608 -19.304 1.00 18.48 ? 5   VAL D CG1 1 
ATOM   3450  C  CG2 . VAL D  1 32  ? 67.331  112.284 -20.531 1.00 20.54 ? 5   VAL D CG2 1 
ATOM   3451  N  N   . CYS D  1 33  ? 64.928  114.280 -19.892 1.00 18.82 ? 6   CYS D N   1 
ATOM   3452  C  CA  . CYS D  1 33  ? 63.710  114.745 -20.489 1.00 18.70 ? 6   CYS D CA  1 
ATOM   3453  C  C   . CYS D  1 33  ? 63.939  114.871 -21.989 1.00 19.48 ? 6   CYS D C   1 
ATOM   3454  O  O   . CYS D  1 33  ? 64.961  115.432 -22.411 1.00 19.67 ? 6   CYS D O   1 
ATOM   3455  C  CB  . CYS D  1 33  ? 63.317  116.106 -19.903 1.00 19.00 ? 6   CYS D CB  1 
ATOM   3456  S  SG  . CYS D  1 33  ? 61.785  116.778 -20.617 1.00 22.67 ? 6   CYS D SG  1 
ATOM   3457  N  N   . VAL D  1 34  ? 63.054  114.286 -22.786 1.00 17.74 ? 7   VAL D N   1 
ATOM   3458  C  CA  . VAL D  1 34  ? 63.084  114.487 -24.254 1.00 17.43 ? 7   VAL D CA  1 
ATOM   3459  C  C   . VAL D  1 34  ? 62.038  115.517 -24.620 1.00 18.56 ? 7   VAL D C   1 
ATOM   3460  O  O   . VAL D  1 34  ? 60.834  115.301 -24.426 1.00 17.42 ? 7   VAL D O   1 
ATOM   3461  C  CB  . VAL D  1 34  ? 62.822  113.155 -25.021 1.00 19.65 ? 7   VAL D CB  1 
ATOM   3462  C  CG1 . VAL D  1 34  ? 62.867  113.392 -26.546 1.00 19.53 ? 7   VAL D CG1 1 
ATOM   3463  C  CG2 . VAL D  1 34  ? 63.891  112.108 -24.631 1.00 18.80 ? 7   VAL D CG2 1 
ATOM   3464  N  N   . LEU D  1 35  ? 62.480  116.647 -25.180 1.00 19.10 ? 8   LEU D N   1 
ATOM   3465  C  CA  . LEU D  1 35  ? 61.559  117.711 -25.568 1.00 17.79 ? 8   LEU D CA  1 
ATOM   3466  C  C   . LEU D  1 35  ? 61.143  117.542 -27.024 1.00 17.21 ? 8   LEU D C   1 
ATOM   3467  O  O   . LEU D  1 35  ? 62.002  117.412 -27.882 1.00 17.00 ? 8   LEU D O   1 
ATOM   3468  C  CB  . LEU D  1 35  ? 62.262  119.083 -25.447 1.00 19.43 ? 8   LEU D CB  1 
ATOM   3469  C  CG  . LEU D  1 35  ? 62.753  119.362 -24.018 1.00 26.05 ? 8   LEU D CG  1 
ATOM   3470  C  CD1 . LEU D  1 35  ? 63.968  120.263 -24.050 1.00 35.26 ? 8   LEU D CD1 1 
ATOM   3471  C  CD2 . LEU D  1 35  ? 61.641  120.067 -23.335 1.00 26.79 ? 8   LEU D CD2 1 
ATOM   3472  N  N   . LYS D  1 36  ? 59.845  117.650 -27.274 1.00 18.86 ? 9   LYS D N   1 
ATOM   3473  C  CA  . LYS D  1 36  ? 59.294  117.634 -28.659 1.00 20.81 ? 9   LYS D CA  1 
ATOM   3474  C  C   . LYS D  1 36  ? 58.139  118.543 -28.698 1.00 19.80 ? 9   LYS D C   1 
ATOM   3475  O  O   . LYS D  1 36  ? 57.504  118.796 -27.662 1.00 18.43 ? 9   LYS D O   1 
ATOM   3476  C  CB  . LYS D  1 36  ? 58.733  116.227 -28.983 1.00 23.34 ? 9   LYS D CB  1 
ATOM   3477  C  CG  . LYS D  1 36  ? 59.744  115.128 -29.007 1.00 31.18 ? 9   LYS D CG  1 
ATOM   3478  C  CD  . LYS D  1 36  ? 58.976  113.780 -28.924 1.00 36.13 ? 9   LYS D CD  1 
ATOM   3479  C  CE  . LYS D  1 36  ? 59.696  112.604 -29.589 1.00 45.25 ? 9   LYS D CE  1 
ATOM   3480  N  NZ  . LYS D  1 36  ? 61.192  112.659 -29.594 1.00 44.78 ? 9   LYS D NZ  1 
ATOM   3481  N  N   . GLY D  1 37  ? 57.774  119.032 -29.901 1.00 21.47 ? 10  GLY D N   1 
ATOM   3482  C  CA  . GLY D  1 37  ? 56.542  119.799 -29.996 1.00 21.27 ? 10  GLY D CA  1 
ATOM   3483  C  C   . GLY D  1 37  ? 55.973  119.687 -31.417 1.00 24.87 ? 10  GLY D C   1 
ATOM   3484  O  O   . GLY D  1 37  ? 56.337  118.784 -32.148 1.00 23.36 ? 10  GLY D O   1 
ATOM   3485  N  N   . ASP D  1 38  ? 55.112  120.613 -31.790 1.00 28.10 ? 11  ASP D N   1 
ATOM   3486  C  CA  . ASP D  1 38  ? 54.503  120.555 -33.134 1.00 32.37 ? 11  ASP D CA  1 
ATOM   3487  C  C   . ASP D  1 38  ? 55.428  121.066 -34.256 1.00 31.97 ? 11  ASP D C   1 
ATOM   3488  O  O   . ASP D  1 38  ? 55.181  120.817 -35.446 1.00 34.85 ? 11  ASP D O   1 
ATOM   3489  C  CB  . ASP D  1 38  ? 53.237  121.337 -33.128 1.00 37.40 ? 11  ASP D CB  1 
ATOM   3490  C  CG  . ASP D  1 38  ? 52.186  120.711 -32.277 1.00 46.53 ? 11  ASP D CG  1 
ATOM   3491  O  OD1 . ASP D  1 38  ? 52.137  119.451 -32.202 1.00 45.66 ? 11  ASP D OD1 1 
ATOM   3492  O  OD2 . ASP D  1 38  ? 51.389  121.485 -31.688 1.00 52.92 ? 11  ASP D OD2 1 
ATOM   3493  N  N   . GLY D  1 39  ? 56.496  121.747 -33.876 1.00 26.38 ? 12  GLY D N   1 
ATOM   3494  C  CA  . GLY D  1 39  ? 57.434  122.345 -34.806 1.00 22.18 ? 12  GLY D CA  1 
ATOM   3495  C  C   . GLY D  1 39  ? 58.760  121.695 -34.703 1.00 20.90 ? 12  GLY D C   1 
ATOM   3496  O  O   . GLY D  1 39  ? 58.858  120.533 -34.312 1.00 21.07 ? 12  GLY D O   1 
ATOM   3497  N  N   . PRO D  1 40  ? 59.830  122.436 -35.040 1.00 19.40 ? 13  PRO D N   1 
ATOM   3498  C  CA  . PRO D  1 40  ? 61.123  121.850 -35.186 1.00 18.60 ? 13  PRO D CA  1 
ATOM   3499  C  C   . PRO D  1 40  ? 61.916  121.834 -33.881 1.00 18.98 ? 13  PRO D C   1 
ATOM   3500  O  O   . PRO D  1 40  ? 63.041  121.397 -33.898 1.00 20.90 ? 13  PRO D O   1 
ATOM   3501  C  CB  . PRO D  1 40  ? 61.848  122.831 -36.155 1.00 20.13 ? 13  PRO D CB  1 
ATOM   3502  C  CG  . PRO D  1 40  ? 61.197  124.146 -35.862 1.00 19.55 ? 13  PRO D CG  1 
ATOM   3503  C  CD  . PRO D  1 40  ? 59.769  123.821 -35.562 1.00 22.16 ? 13  PRO D CD  1 
ATOM   3504  N  N   . VAL D  1 41  ? 61.340  122.309 -32.791 1.00 20.08 ? 14  VAL D N   1 
ATOM   3505  C  CA  . VAL D  1 41  ? 62.144  122.406 -31.532 1.00 22.29 ? 14  VAL D CA  1 
ATOM   3506  C  C   . VAL D  1 41  ? 62.249  121.010 -30.934 1.00 19.97 ? 14  VAL D C   1 
ATOM   3507  O  O   . VAL D  1 41  ? 61.207  120.372 -30.697 1.00 21.21 ? 14  VAL D O   1 
ATOM   3508  C  CB  . VAL D  1 41  ? 61.571  123.425 -30.501 1.00 22.01 ? 14  VAL D CB  1 
ATOM   3509  C  CG1 . VAL D  1 41  ? 62.406  123.380 -29.183 1.00 22.64 ? 14  VAL D CG1 1 
ATOM   3510  C  CG2 . VAL D  1 41  ? 61.573  124.855 -31.094 1.00 23.09 ? 14  VAL D CG2 1 
ATOM   3511  N  N   . GLN D  1 42  ? 63.478  120.550 -30.708 1.00 24.04 ? 15  GLN D N   1 
ATOM   3512  C  CA  . GLN D  1 42  ? 63.725  119.218 -30.163 1.00 24.92 ? 15  GLN D CA  1 
ATOM   3513  C  C   . GLN D  1 42  ? 64.959  119.270 -29.279 1.00 25.28 ? 15  GLN D C   1 
ATOM   3514  O  O   . GLN D  1 42  ? 65.936  119.948 -29.606 1.00 23.41 ? 15  GLN D O   1 
ATOM   3515  C  CB  . GLN D  1 42  ? 64.078  118.225 -31.267 1.00 28.68 ? 15  GLN D CB  1 
ATOM   3516  C  CG  . GLN D  1 42  ? 63.094  118.116 -32.404 1.00 31.87 ? 15  GLN D CG  1 
ATOM   3517  C  CD  . GLN D  1 42  ? 63.467  116.957 -33.323 1.00 33.49 ? 15  GLN D CD  1 
ATOM   3518  O  OE1 . GLN D  1 42  ? 63.146  115.830 -33.036 1.00 40.33 ? 15  GLN D OE1 1 
ATOM   3519  N  NE2 . GLN D  1 42  ? 64.187  117.232 -34.364 1.00 31.25 ? 15  GLN D NE2 1 
ATOM   3520  N  N   . GLY D  1 43  ? 64.961  118.501 -28.188 1.00 22.82 ? 16  GLY D N   1 
ATOM   3521  C  CA  . GLY D  1 43  ? 66.153  118.429 -27.368 1.00 23.84 ? 16  GLY D CA  1 
ATOM   3522  C  C   . GLY D  1 43  ? 66.139  117.329 -26.323 1.00 22.87 ? 16  GLY D C   1 
ATOM   3523  O  O   . GLY D  1 43  ? 65.124  116.672 -26.114 1.00 19.12 ? 16  GLY D O   1 
ATOM   3524  N  N   . ILE D  1 44  ? 67.289  117.132 -25.708 1.00 21.62 ? 17  ILE D N   1 
ATOM   3525  C  CA  . ILE D  1 44  ? 67.439  116.208 -24.590 1.00 21.02 ? 17  ILE D CA  1 
ATOM   3526  C  C   . ILE D  1 44  ? 68.087  116.979 -23.428 1.00 22.88 ? 17  ILE D C   1 
ATOM   3527  O  O   . ILE D  1 44  ? 69.157  117.600 -23.593 1.00 24.24 ? 17  ILE D O   1 
ATOM   3528  C  CB  . ILE D  1 44  ? 68.301  114.999 -24.955 1.00 23.85 ? 17  ILE D CB  1 
ATOM   3529  C  CG1 . ILE D  1 44  ? 67.578  114.144 -26.035 1.00 25.47 ? 17  ILE D CG1 1 
ATOM   3530  C  CG2 . ILE D  1 44  ? 68.605  114.165 -23.676 1.00 23.51 ? 17  ILE D CG2 1 
ATOM   3531  C  CD1 . ILE D  1 44  ? 68.421  113.030 -26.684 1.00 26.71 ? 17  ILE D CD1 1 
ATOM   3532  N  N   . ILE D  1 45  ? 67.449  116.948 -22.271 1.00 18.72 ? 18  ILE D N   1 
ATOM   3533  C  CA  . ILE D  1 45  ? 67.988  117.659 -21.093 1.00 19.85 ? 18  ILE D CA  1 
ATOM   3534  C  C   . ILE D  1 45  ? 68.195  116.585 -19.991 1.00 21.06 ? 18  ILE D C   1 
ATOM   3535  O  O   . ILE D  1 45  ? 67.273  115.739 -19.759 1.00 19.08 ? 18  ILE D O   1 
ATOM   3536  C  CB  . ILE D  1 45  ? 67.010  118.720 -20.622 1.00 18.48 ? 18  ILE D CB  1 
ATOM   3537  C  CG1 . ILE D  1 45  ? 66.883  119.897 -21.648 1.00 19.94 ? 18  ILE D CG1 1 
ATOM   3538  C  CG2 . ILE D  1 45  ? 67.429  119.279 -19.258 1.00 18.37 ? 18  ILE D CG2 1 
ATOM   3539  C  CD1 . ILE D  1 45  ? 68.251  120.602 -21.984 1.00 20.67 ? 18  ILE D CD1 1 
ATOM   3540  N  N   . ASN D  1 46  ? 69.384  116.578 -19.383 1.00 19.39 ? 19  ASN D N   1 
ATOM   3541  C  CA  . ASN D  1 46  ? 69.771  115.619 -18.334 1.00 20.78 ? 19  ASN D CA  1 
ATOM   3542  C  C   . ASN D  1 46  ? 69.796  116.333 -17.004 1.00 23.42 ? 19  ASN D C   1 
ATOM   3543  O  O   . ASN D  1 46  ? 70.010  117.595 -16.936 1.00 20.47 ? 19  ASN D O   1 
ATOM   3544  C  CB  . ASN D  1 46  ? 71.150  115.085 -18.595 1.00 23.13 ? 19  ASN D CB  1 
ATOM   3545  C  CG  . ASN D  1 46  ? 71.286  114.487 -19.951 1.00 26.49 ? 19  ASN D CG  1 
ATOM   3546  O  OD1 . ASN D  1 46  ? 71.928  115.054 -20.864 1.00 29.89 ? 19  ASN D OD1 1 
ATOM   3547  N  ND2 . ASN D  1 46  ? 70.679  113.349 -20.113 1.00 23.37 ? 19  ASN D ND2 1 
ATOM   3548  N  N   . PHE D  1 47  ? 69.483  115.584 -15.935 1.00 22.67 ? 20  PHE D N   1 
ATOM   3549  C  CA  . PHE D  1 47  ? 69.496  116.176 -14.584 1.00 22.14 ? 20  PHE D CA  1 
ATOM   3550  C  C   . PHE D  1 47  ? 70.344  115.244 -13.726 1.00 25.19 ? 20  PHE D C   1 
ATOM   3551  O  O   . PHE D  1 47  ? 70.246  114.028 -13.861 1.00 21.26 ? 20  PHE D O   1 
ATOM   3552  C  CB  . PHE D  1 47  ? 68.121  116.195 -13.964 1.00 21.15 ? 20  PHE D CB  1 
ATOM   3553  C  CG  . PHE D  1 47  ? 67.104  117.032 -14.720 1.00 22.15 ? 20  PHE D CG  1 
ATOM   3554  C  CD1 . PHE D  1 47  ? 66.538  116.565 -15.922 1.00 21.15 ? 20  PHE D CD1 1 
ATOM   3555  C  CD2 . PHE D  1 47  ? 66.766  118.300 -14.261 1.00 21.55 ? 20  PHE D CD2 1 
ATOM   3556  C  CE1 . PHE D  1 47  ? 65.599  117.336 -16.611 1.00 20.57 ? 20  PHE D CE1 1 
ATOM   3557  C  CE2 . PHE D  1 47  ? 65.857  119.104 -14.947 1.00 23.47 ? 20  PHE D CE2 1 
ATOM   3558  C  CZ  . PHE D  1 47  ? 65.245  118.608 -16.118 1.00 22.81 ? 20  PHE D CZ  1 
ATOM   3559  N  N   . GLU D  1 48  ? 71.132  115.797 -12.802 1.00 23.44 ? 21  GLU D N   1 
ATOM   3560  C  CA  . GLU D  1 48  ? 71.918  114.918 -11.926 1.00 25.62 ? 21  GLU D CA  1 
ATOM   3561  C  C   . GLU D  1 48  ? 72.031  115.535 -10.550 1.00 28.18 ? 21  GLU D C   1 
ATOM   3562  O  O   . GLU D  1 48  ? 72.258  116.748 -10.432 1.00 26.36 ? 21  GLU D O   1 
ATOM   3563  C  CB  . GLU D  1 48  ? 73.271  114.564 -12.525 1.00 31.49 ? 21  GLU D CB  1 
ATOM   3564  C  CG  . GLU D  1 48  ? 74.102  113.606 -11.655 1.00 38.54 ? 21  GLU D CG  1 
ATOM   3565  C  CD  . GLU D  1 48  ? 75.540  113.467 -12.164 1.00 50.89 ? 21  GLU D CD  1 
ATOM   3566  O  OE1 . GLU D  1 48  ? 75.760  112.754 -13.183 1.00 54.67 ? 21  GLU D OE1 1 
ATOM   3567  O  OE2 . GLU D  1 48  ? 76.458  114.086 -11.563 1.00 57.45 ? 21  GLU D OE2 1 
ATOM   3568  N  N   . GLN D  1 49  ? 71.805  114.731 -9.501  1.00 25.09 ? 22  GLN D N   1 
ATOM   3569  C  CA  . GLN D  1 49  ? 71.798  115.286 -8.171  1.00 27.67 ? 22  GLN D CA  1 
ATOM   3570  C  C   . GLN D  1 49  ? 72.405  114.257 -7.241  1.00 32.70 ? 22  GLN D C   1 
ATOM   3571  O  O   . GLN D  1 49  ? 71.705  113.331 -6.789  1.00 30.64 ? 22  GLN D O   1 
ATOM   3572  C  CB  . GLN D  1 49  ? 70.412  115.635 -7.714  1.00 23.07 ? 22  GLN D CB  1 
ATOM   3573  C  CG  . GLN D  1 49  ? 70.402  116.271 -6.326  1.00 24.76 ? 22  GLN D CG  1 
ATOM   3574  C  CD  . GLN D  1 49  ? 69.012  116.475 -5.814  1.00 27.07 ? 22  GLN D CD  1 
ATOM   3575  O  OE1 . GLN D  1 49  ? 68.102  115.728 -6.198  1.00 24.70 ? 22  GLN D OE1 1 
ATOM   3576  N  NE2 . GLN D  1 49  ? 68.811  117.488 -4.942  1.00 24.96 ? 22  GLN D NE2 1 
ATOM   3577  N  N   . LYS D  1 50  ? 73.691  114.406 -6.999  1.00 33.44 ? 23  LYS D N   1 
ATOM   3578  C  CA  . LYS D  1 50  ? 74.430  113.361 -6.292  1.00 40.01 ? 23  LYS D CA  1 
ATOM   3579  C  C   . LYS D  1 50  ? 74.141  113.273 -4.805  1.00 36.29 ? 23  LYS D C   1 
ATOM   3580  O  O   . LYS D  1 50  ? 74.285  112.197 -4.239  1.00 41.46 ? 23  LYS D O   1 
ATOM   3581  C  CB  . LYS D  1 50  ? 75.923  113.405 -6.587  1.00 47.89 ? 23  LYS D CB  1 
ATOM   3582  C  CG  . LYS D  1 50  ? 76.247  112.710 -7.906  1.00 54.79 ? 23  LYS D CG  1 
ATOM   3583  C  CD  . LYS D  1 50  ? 77.696  112.264 -8.029  1.00 63.99 ? 23  LYS D CD  1 
ATOM   3584  C  CE  . LYS D  1 50  ? 77.834  111.236 -9.149  1.00 69.91 ? 23  LYS D CE  1 
ATOM   3585  N  NZ  . LYS D  1 50  ? 79.183  111.262 -9.777  1.00 71.24 ? 23  LYS D NZ  1 
ATOM   3586  N  N   . GLU D  1 51  ? 73.699  114.368 -4.202  1.00 35.95 ? 24  GLU D N   1 
ATOM   3587  C  CA  . GLU D  1 51  ? 73.284  114.409 -2.792  1.00 35.54 ? 24  GLU D CA  1 
ATOM   3588  C  C   . GLU D  1 51  ? 71.889  114.948 -2.737  1.00 33.38 ? 24  GLU D C   1 
ATOM   3589  O  O   . GLU D  1 51  ? 71.591  115.988 -3.350  1.00 31.45 ? 24  GLU D O   1 
ATOM   3590  C  CB  . GLU D  1 51  ? 74.182  115.371 -1.949  1.00 37.79 ? 24  GLU D CB  1 
ATOM   3591  C  CG  . GLU D  1 51  ? 75.661  115.002 -1.899  1.00 50.52 ? 24  GLU D CG  1 
ATOM   3592  C  CD  . GLU D  1 51  ? 75.933  113.780 -1.005  1.00 65.74 ? 24  GLU D CD  1 
ATOM   3593  O  OE1 . GLU D  1 51  ? 74.971  113.227 -0.382  1.00 65.69 ? 24  GLU D OE1 1 
ATOM   3594  O  OE2 . GLU D  1 51  ? 77.118  113.364 -0.911  1.00 66.34 ? 24  GLU D OE2 1 
ATOM   3595  N  N   . SER D  1 52  ? 71.037  114.310 -1.942  1.00 27.64 ? 25  SER D N   1 
ATOM   3596  C  CA  . SER D  1 52  ? 69.629  114.741 -1.827  1.00 27.43 ? 25  SER D CA  1 
ATOM   3597  C  C   . SER D  1 52  ? 69.385  116.110 -1.281  1.00 30.24 ? 25  SER D C   1 
ATOM   3598  O  O   . SER D  1 52  ? 68.344  116.727 -1.542  1.00 26.96 ? 25  SER D O   1 
ATOM   3599  C  CB  . SER D  1 52  ? 68.799  113.707 -1.044  1.00 34.69 ? 25  SER D CB  1 
ATOM   3600  O  OG  . SER D  1 52  ? 69.251  113.610 0.310   1.00 37.25 ? 25  SER D OG  1 
ATOM   3601  N  N   . ASN D  1 53  ? 70.299  116.593 -0.448  1.00 31.08 ? 26  ASN D N   1 
ATOM   3602  C  CA  . ASN D  1 53  ? 70.151  117.943 0.031   1.00 31.91 ? 26  ASN D CA  1 
ATOM   3603  C  C   . ASN D  1 53  ? 71.112  118.879 -0.693  1.00 35.88 ? 26  ASN D C   1 
ATOM   3604  O  O   . ASN D  1 53  ? 71.385  119.964 -0.186  1.00 39.38 ? 26  ASN D O   1 
ATOM   3605  C  CB  . ASN D  1 53  ? 70.343  118.018 1.584   1.00 35.33 ? 26  ASN D CB  1 
ATOM   3606  C  CG  . ASN D  1 53  ? 71.749  117.641 2.031   1.00 31.49 ? 26  ASN D CG  1 
ATOM   3607  O  OD1 . ASN D  1 53  ? 72.474  116.881 1.372   1.00 32.09 ? 26  ASN D OD1 1 
ATOM   3608  N  ND2 . ASN D  1 53  ? 72.156  118.204 3.188   1.00 35.31 ? 26  ASN D ND2 1 
ATOM   3609  N  N   . GLY D  1 54  ? 71.648  118.461 -1.842  1.00 33.88 ? 27  GLY D N   1 
ATOM   3610  C  CA  . GLY D  1 54  ? 72.524  119.316 -2.666  1.00 32.65 ? 27  GLY D CA  1 
ATOM   3611  C  C   . GLY D  1 54  ? 71.878  119.808 -3.970  1.00 34.67 ? 27  GLY D C   1 
ATOM   3612  O  O   . GLY D  1 54  ? 70.703  119.501 -4.217  1.00 28.66 ? 27  GLY D O   1 
ATOM   3613  N  N   . PRO D  1 55  ? 72.654  120.563 -4.808  1.00 33.11 ? 28  PRO D N   1 
ATOM   3614  C  CA  . PRO D  1 55  ? 72.121  121.137 -6.041  1.00 32.35 ? 28  PRO D CA  1 
ATOM   3615  C  C   . PRO D  1 55  ? 71.915  120.068 -7.125  1.00 28.77 ? 28  PRO D C   1 
ATOM   3616  O  O   . PRO D  1 55  ? 72.479  118.975 -7.050  1.00 26.91 ? 28  PRO D O   1 
ATOM   3617  C  CB  . PRO D  1 55  ? 73.230  122.116 -6.491  1.00 30.91 ? 28  PRO D CB  1 
ATOM   3618  C  CG  . PRO D  1 55  ? 74.497  121.665 -5.809  1.00 36.72 ? 28  PRO D CG  1 
ATOM   3619  C  CD  . PRO D  1 55  ? 74.136  120.581 -4.803  1.00 33.84 ? 28  PRO D CD  1 
ATOM   3620  N  N   . VAL D  1 56  ? 71.163  120.441 -8.167  1.00 28.36 ? 29  VAL D N   1 
ATOM   3621  C  CA  . VAL D  1 56  ? 70.967  119.632 -9.375  1.00 24.37 ? 29  VAL D CA  1 
ATOM   3622  C  C   . VAL D  1 56  ? 71.657  120.262 -10.580 1.00 22.79 ? 29  VAL D C   1 
ATOM   3623  O  O   . VAL D  1 56  ? 71.406  121.416 -10.830 1.00 27.19 ? 29  VAL D O   1 
ATOM   3624  C  CB  . VAL D  1 56  ? 69.458  119.608 -9.706  1.00 24.46 ? 29  VAL D CB  1 
ATOM   3625  C  CG1 . VAL D  1 56  ? 69.163  118.606 -10.852 1.00 21.21 ? 29  VAL D CG1 1 
ATOM   3626  C  CG2 . VAL D  1 56  ? 68.663  119.214 -8.472  1.00 24.50 ? 29  VAL D CG2 1 
ATOM   3627  N  N   . LYS D  1 57  ? 72.508  119.505 -11.275 1.00 24.86 ? 30  LYS D N   1 
ATOM   3628  C  CA  . LYS D  1 57  ? 73.129  119.897 -12.528 1.00 26.65 ? 30  LYS D CA  1 
ATOM   3629  C  C   . LYS D  1 57  ? 72.092  119.597 -13.616 1.00 29.47 ? 30  LYS D C   1 
ATOM   3630  O  O   . LYS D  1 57  ? 71.445  118.546 -13.577 1.00 23.37 ? 30  LYS D O   1 
ATOM   3631  C  CB  . LYS D  1 57  ? 74.367  119.063 -12.843 1.00 30.86 ? 30  LYS D CB  1 
ATOM   3632  C  CG  . LYS D  1 57  ? 75.563  119.191 -11.907 1.00 42.36 ? 30  LYS D CG  1 
ATOM   3633  C  CD  . LYS D  1 57  ? 76.857  118.773 -12.648 1.00 48.23 ? 30  LYS D CD  1 
ATOM   3634  C  CE  . LYS D  1 57  ? 77.682  117.713 -11.905 1.00 56.70 ? 30  LYS D CE  1 
ATOM   3635  N  NZ  . LYS D  1 57  ? 78.520  118.266 -10.798 1.00 53.29 ? 30  LYS D NZ  1 
ATOM   3636  N  N   . VAL D  1 58  ? 71.932  120.511 -14.572 1.00 26.02 ? 31  VAL D N   1 
ATOM   3637  C  CA  . VAL D  1 58  ? 70.901  120.388 -15.638 1.00 25.55 ? 31  VAL D CA  1 
ATOM   3638  C  C   . VAL D  1 58  ? 71.693  120.723 -16.883 1.00 27.78 ? 31  VAL D C   1 
ATOM   3639  O  O   . VAL D  1 58  ? 72.421  121.766 -16.913 1.00 26.61 ? 31  VAL D O   1 
ATOM   3640  C  CB  . VAL D  1 58  ? 69.782  121.415 -15.475 1.00 24.18 ? 31  VAL D CB  1 
ATOM   3641  C  CG1 . VAL D  1 58  ? 68.766  121.324 -16.622 1.00 23.30 ? 31  VAL D CG1 1 
ATOM   3642  C  CG2 . VAL D  1 58  ? 69.034  121.297 -14.156 1.00 23.65 ? 31  VAL D CG2 1 
ATOM   3643  N  N   . TRP D  1 59  ? 71.725  119.824 -17.851 1.00 25.32 ? 32  TRP D N   1 
ATOM   3644  C  CA  . TRP D  1 59  ? 72.543  120.104 -19.039 1.00 24.75 ? 32  TRP D CA  1 
ATOM   3645  C  C   . TRP D  1 59  ? 72.026  119.330 -20.226 1.00 28.43 ? 32  TRP D C   1 
ATOM   3646  O  O   . TRP D  1 59  ? 71.444  118.235 -20.057 1.00 22.98 ? 32  TRP D O   1 
ATOM   3647  C  CB  . TRP D  1 59  ? 74.029  119.729 -18.850 1.00 25.45 ? 32  TRP D CB  1 
ATOM   3648  C  CG  . TRP D  1 59  ? 74.361  118.267 -18.902 1.00 25.92 ? 32  TRP D CG  1 
ATOM   3649  C  CD1 . TRP D  1 59  ? 74.840  117.545 -19.962 1.00 29.02 ? 32  TRP D CD1 1 
ATOM   3650  C  CD2 . TRP D  1 59  ? 74.189  117.351 -17.839 1.00 28.11 ? 32  TRP D CD2 1 
ATOM   3651  N  NE1 . TRP D  1 59  ? 74.992  116.222 -19.610 1.00 29.57 ? 32  TRP D NE1 1 
ATOM   3652  C  CE2 . TRP D  1 59  ? 74.600  116.082 -18.300 1.00 31.17 ? 32  TRP D CE2 1 
ATOM   3653  C  CE3 . TRP D  1 59  ? 73.681  117.473 -16.543 1.00 29.71 ? 32  TRP D CE3 1 
ATOM   3654  C  CZ2 . TRP D  1 59  ? 74.542  114.939 -17.502 1.00 33.62 ? 32  TRP D CZ2 1 
ATOM   3655  C  CZ3 . TRP D  1 59  ? 73.626  116.316 -15.740 1.00 34.32 ? 32  TRP D CZ3 1 
ATOM   3656  C  CH2 . TRP D  1 59  ? 74.050  115.081 -16.226 1.00 36.02 ? 32  TRP D CH2 1 
ATOM   3657  N  N   . GLY D  1 60  ? 72.277  119.869 -21.412 1.00 24.43 ? 33  GLY D N   1 
ATOM   3658  C  CA  . GLY D  1 60  ? 71.985  119.127 -22.646 1.00 23.68 ? 33  GLY D CA  1 
ATOM   3659  C  C   . GLY D  1 60  ? 71.886  120.152 -23.761 1.00 27.94 ? 33  GLY D C   1 
ATOM   3660  O  O   . GLY D  1 60  ? 72.499  121.215 -23.698 1.00 25.16 ? 33  GLY D O   1 
ATOM   3661  N  N   . SER D  1 61  ? 71.118  119.840 -24.786 1.00 25.94 ? 34  SER D N   1 
ATOM   3662  C  CA  . SER D  1 61  ? 71.077  120.673 -25.991 1.00 26.47 ? 34  SER D CA  1 
ATOM   3663  C  C   . SER D  1 61  ? 69.635  120.688 -26.508 1.00 28.77 ? 34  SER D C   1 
ATOM   3664  O  O   . SER D  1 61  ? 68.908  119.662 -26.406 1.00 24.61 ? 34  SER D O   1 
ATOM   3665  C  CB  . SER D  1 61  ? 72.002  120.039 -27.018 1.00 33.05 ? 34  SER D CB  1 
ATOM   3666  O  OG  . SER D  1 61  ? 72.166  120.906 -28.116 1.00 43.09 ? 34  SER D OG  1 
ATOM   3667  N  N   . ILE D  1 62  ? 69.217  121.841 -27.032 1.00 23.80 ? 35  ILE D N   1 
ATOM   3668  C  CA  . ILE D  1 62  ? 67.907  122.007 -27.661 1.00 22.65 ? 35  ILE D CA  1 
ATOM   3669  C  C   . ILE D  1 62  ? 68.211  122.635 -29.019 1.00 27.26 ? 35  ILE D C   1 
ATOM   3670  O  O   . ILE D  1 62  ? 68.994  123.614 -29.101 1.00 24.69 ? 35  ILE D O   1 
ATOM   3671  C  CB  . ILE D  1 62  ? 67.022  122.954 -26.865 1.00 22.99 ? 35  ILE D CB  1 
ATOM   3672  C  CG1 . ILE D  1 62  ? 66.926  122.500 -25.370 1.00 22.24 ? 35  ILE D CG1 1 
ATOM   3673  C  CG2 . ILE D  1 62  ? 65.617  123.058 -27.472 1.00 23.07 ? 35  ILE D CG2 1 
ATOM   3674  C  CD1 . ILE D  1 62  ? 65.965  123.351 -24.555 1.00 24.42 ? 35  ILE D CD1 1 
ATOM   3675  N  N   . LYS D  1 63  ? 67.646  122.066 -30.082 1.00 25.36 ? 36  LYS D N   1 
ATOM   3676  C  CA  . LYS D  1 63  ? 67.829  122.621 -31.436 1.00 23.49 ? 36  LYS D CA  1 
ATOM   3677  C  C   . LYS D  1 63  ? 66.488  123.088 -32.021 1.00 24.26 ? 36  LYS D C   1 
ATOM   3678  O  O   . LYS D  1 63  ? 65.407  122.867 -31.446 1.00 21.81 ? 36  LYS D O   1 
ATOM   3679  C  CB  . LYS D  1 63  ? 68.554  121.613 -32.306 1.00 28.77 ? 36  LYS D CB  1 
ATOM   3680  C  CG  . LYS D  1 63  ? 67.756  120.352 -32.500 1.00 34.50 ? 36  LYS D CG  1 
ATOM   3681  C  CD  . LYS D  1 63  ? 68.629  119.229 -33.040 1.00 41.71 ? 36  LYS D CD  1 
ATOM   3682  C  CE  . LYS D  1 63  ? 67.797  117.954 -33.253 1.00 42.02 ? 36  LYS D CE  1 
ATOM   3683  N  NZ  . LYS D  1 63  ? 68.677  116.930 -33.862 1.00 52.21 ? 36  LYS D NZ  1 
ATOM   3684  N  N   . GLY D  1 64  ? 66.562  123.794 -33.154 1.00 22.97 ? 37  GLY D N   1 
ATOM   3685  C  CA  . GLY D  1 64  ? 65.370  124.333 -33.806 1.00 22.15 ? 37  GLY D CA  1 
ATOM   3686  C  C   . GLY D  1 64  ? 64.797  125.592 -33.268 1.00 22.98 ? 37  GLY D C   1 
ATOM   3687  O  O   . GLY D  1 64  ? 63.666  125.953 -33.614 1.00 23.15 ? 37  GLY D O   1 
ATOM   3688  N  N   . LEU D  1 65  ? 65.543  126.293 -32.409 1.00 20.35 ? 38  LEU D N   1 
ATOM   3689  C  CA  . LEU D  1 65  ? 65.012  127.502 -31.753 1.00 20.93 ? 38  LEU D CA  1 
ATOM   3690  C  C   . LEU D  1 65  ? 65.410  128.756 -32.568 1.00 21.96 ? 38  LEU D C   1 
ATOM   3691  O  O   . LEU D  1 65  ? 66.449  128.736 -33.206 1.00 24.68 ? 38  LEU D O   1 
ATOM   3692  C  CB  . LEU D  1 65  ? 65.719  127.696 -30.381 1.00 23.31 ? 38  LEU D CB  1 
ATOM   3693  C  CG  . LEU D  1 65  ? 65.271  126.662 -29.305 1.00 23.39 ? 38  LEU D CG  1 
ATOM   3694  C  CD1 . LEU D  1 65  ? 66.251  126.551 -28.135 1.00 22.85 ? 38  LEU D CD1 1 
ATOM   3695  C  CD2 . LEU D  1 65  ? 63.857  127.003 -28.853 1.00 19.96 ? 38  LEU D CD2 1 
ATOM   3696  N  N   . THR D  1 66  ? 64.638  129.832 -32.454 1.00 23.68 ? 39  THR D N   1 
ATOM   3697  C  CA  . THR D  1 66  ? 65.097  131.116 -32.997 1.00 29.87 ? 39  THR D CA  1 
ATOM   3698  C  C   . THR D  1 66  ? 66.300  131.617 -32.184 1.00 31.27 ? 39  THR D C   1 
ATOM   3699  O  O   . THR D  1 66  ? 66.392  131.373 -30.969 1.00 28.00 ? 39  THR D O   1 
ATOM   3700  C  CB  . THR D  1 66  ? 63.949  132.141 -33.004 1.00 30.07 ? 39  THR D CB  1 
ATOM   3701  O  OG1 . THR D  1 66  ? 63.378  132.275 -31.693 1.00 30.39 ? 39  THR D OG1 1 
ATOM   3702  C  CG2 . THR D  1 66  ? 62.829  131.656 -33.930 1.00 28.86 ? 39  THR D CG2 1 
ATOM   3703  N  N   . GLU D  1 67  ? 67.226  132.303 -32.841 1.00 27.67 ? 40  GLU D N   1 
ATOM   3704  C  CA  . GLU D  1 67  ? 68.394  132.874 -32.147 1.00 30.49 ? 40  GLU D CA  1 
ATOM   3705  C  C   . GLU D  1 67  ? 67.912  133.725 -31.029 1.00 27.56 ? 40  GLU D C   1 
ATOM   3706  O  O   . GLU D  1 67  ? 66.885  134.428 -31.156 1.00 28.03 ? 40  GLU D O   1 
ATOM   3707  C  CB  . GLU D  1 67  ? 69.266  133.700 -33.112 1.00 33.51 ? 40  GLU D CB  1 
ATOM   3708  C  CG  . GLU D  1 67  ? 70.578  134.179 -32.507 1.00 36.26 ? 40  GLU D CG  1 
ATOM   3709  C  CD  . GLU D  1 67  ? 71.484  134.824 -33.561 1.00 46.89 ? 40  GLU D CD  1 
ATOM   3710  O  OE1 . GLU D  1 67  ? 70.970  135.135 -34.646 1.00 45.18 ? 40  GLU D OE1 1 
ATOM   3711  O  OE2 . GLU D  1 67  ? 72.711  134.971 -33.331 1.00 47.65 ? 40  GLU D OE2 1 
ATOM   3712  N  N   . GLY D  1 68  ? 68.577  133.634 -29.873 1.00 29.54 ? 41  GLY D N   1 
ATOM   3713  C  CA  . GLY D  1 68  ? 68.118  134.457 -28.753 1.00 27.95 ? 41  GLY D CA  1 
ATOM   3714  C  C   . GLY D  1 68  ? 67.671  133.684 -27.527 1.00 26.70 ? 41  GLY D C   1 
ATOM   3715  O  O   . GLY D  1 68  ? 67.882  132.463 -27.441 1.00 26.93 ? 41  GLY D O   1 
ATOM   3716  N  N   . LEU D  1 69  ? 67.020  134.385 -26.620 1.00 26.24 ? 42  LEU D N   1 
ATOM   3717  C  CA  . LEU D  1 69  ? 66.661  133.839 -25.312 1.00 30.18 ? 42  LEU D CA  1 
ATOM   3718  C  C   . LEU D  1 69  ? 65.308  133.175 -25.343 1.00 29.80 ? 42  LEU D C   1 
ATOM   3719  O  O   . LEU D  1 69  ? 64.355  133.675 -25.967 1.00 26.15 ? 42  LEU D O   1 
ATOM   3720  C  CB  . LEU D  1 69  ? 66.627  134.946 -24.255 1.00 29.81 ? 42  LEU D CB  1 
ATOM   3721  C  CG  . LEU D  1 69  ? 67.954  135.291 -23.569 1.00 33.79 ? 42  LEU D CG  1 
ATOM   3722  C  CD1 . LEU D  1 69  ? 69.078  135.531 -24.563 1.00 34.76 ? 42  LEU D CD1 1 
ATOM   3723  C  CD2 . LEU D  1 69  ? 67.736  136.535 -22.745 1.00 35.19 ? 42  LEU D CD2 1 
ATOM   3724  N  N   . HIS D  1 70  ? 65.205  132.062 -24.611 1.00 25.38 ? 43  HIS D N   1 
ATOM   3725  C  CA  . HIS D  1 70  ? 63.938  131.364 -24.486 1.00 22.06 ? 43  HIS D CA  1 
ATOM   3726  C  C   . HIS D  1 70  ? 63.730  130.903 -23.061 1.00 22.51 ? 43  HIS D C   1 
ATOM   3727  O  O   . HIS D  1 70  ? 64.631  130.260 -22.519 1.00 23.94 ? 43  HIS D O   1 
ATOM   3728  C  CB  . HIS D  1 70  ? 63.984  130.120 -25.391 1.00 22.27 ? 43  HIS D CB  1 
ATOM   3729  C  CG  . HIS D  1 70  ? 64.030  130.468 -26.854 1.00 22.45 ? 43  HIS D CG  1 
ATOM   3730  N  ND1 . HIS D  1 70  ? 62.889  130.750 -27.567 1.00 24.35 ? 43  HIS D ND1 1 
ATOM   3731  C  CD2 . HIS D  1 70  ? 65.063  130.642 -27.700 1.00 22.91 ? 43  HIS D CD2 1 
ATOM   3732  C  CE1 . HIS D  1 70  ? 63.224  131.070 -28.811 1.00 24.41 ? 43  HIS D CE1 1 
ATOM   3733  N  NE2 . HIS D  1 70  ? 64.535  131.004 -28.918 1.00 24.18 ? 43  HIS D NE2 1 
ATOM   3734  N  N   . GLY D  1 71  ? 62.542  131.204 -22.550 1.00 20.78 ? 44  GLY D N   1 
ATOM   3735  C  CA  . GLY D  1 71  ? 62.056  130.847 -21.215 1.00 23.43 ? 44  GLY D CA  1 
ATOM   3736  C  C   . GLY D  1 71  ? 62.097  129.325 -21.047 1.00 24.81 ? 44  GLY D C   1 
ATOM   3737  O  O   . GLY D  1 71  ? 61.787  128.589 -22.005 1.00 21.25 ? 44  GLY D O   1 
ATOM   3738  N  N   . PHE D  1 72  ? 62.506  128.857 -19.851 1.00 22.21 ? 45  PHE D N   1 
ATOM   3739  C  CA  . PHE D  1 72  ? 62.804  127.438 -19.645 1.00 21.08 ? 45  PHE D CA  1 
ATOM   3740  C  C   . PHE D  1 72  ? 62.319  127.065 -18.252 1.00 24.10 ? 45  PHE D C   1 
ATOM   3741  O  O   . PHE D  1 72  ? 62.910  127.517 -17.262 1.00 25.19 ? 45  PHE D O   1 
ATOM   3742  C  CB  . PHE D  1 72  ? 64.298  127.285 -19.764 1.00 21.34 ? 45  PHE D CB  1 
ATOM   3743  C  CG  . PHE D  1 72  ? 64.819  125.870 -19.733 1.00 23.79 ? 45  PHE D CG  1 
ATOM   3744  C  CD1 . PHE D  1 72  ? 64.473  124.928 -20.710 1.00 24.46 ? 45  PHE D CD1 1 
ATOM   3745  C  CD2 . PHE D  1 72  ? 65.734  125.491 -18.742 1.00 23.63 ? 45  PHE D CD2 1 
ATOM   3746  C  CE1 . PHE D  1 72  ? 65.046  123.654 -20.698 1.00 25.30 ? 45  PHE D CE1 1 
ATOM   3747  C  CE2 . PHE D  1 72  ? 66.287  124.212 -18.720 1.00 27.74 ? 45  PHE D CE2 1 
ATOM   3748  C  CZ  . PHE D  1 72  ? 65.955  123.291 -19.714 1.00 27.06 ? 45  PHE D CZ  1 
ATOM   3749  N  N   . HIS D  1 73  ? 61.228  126.299 -18.171 1.00 21.45 ? 46  HIS D N   1 
ATOM   3750  C  CA  . HIS D  1 73  ? 60.549  126.095 -16.895 1.00 21.47 ? 46  HIS D CA  1 
ATOM   3751  C  C   . HIS D  1 73  ? 60.122  124.670 -16.699 1.00 23.15 ? 46  HIS D C   1 
ATOM   3752  O  O   . HIS D  1 73  ? 59.772  123.978 -17.677 1.00 18.67 ? 46  HIS D O   1 
ATOM   3753  C  CB  . HIS D  1 73  ? 59.316  126.958 -16.804 1.00 24.37 ? 46  HIS D CB  1 
ATOM   3754  C  CG  . HIS D  1 73  ? 59.552  128.375 -17.224 1.00 30.56 ? 46  HIS D CG  1 
ATOM   3755  N  ND1 . HIS D  1 73  ? 58.844  128.968 -18.246 1.00 34.41 ? 46  HIS D ND1 1 
ATOM   3756  C  CD2 . HIS D  1 73  ? 60.443  129.304 -16.787 1.00 33.50 ? 46  HIS D CD2 1 
ATOM   3757  C  CE1 . HIS D  1 73  ? 59.265  130.217 -18.399 1.00 37.73 ? 46  HIS D CE1 1 
ATOM   3758  N  NE2 . HIS D  1 73  ? 60.252  130.439 -17.548 1.00 31.50 ? 46  HIS D NE2 1 
ATOM   3759  N  N   . VAL D  1 74  ? 60.062  124.277 -15.442 1.00 22.18 ? 47  VAL D N   1 
ATOM   3760  C  CA  . VAL D  1 74  ? 59.307  123.054 -15.090 1.00 22.24 ? 47  VAL D CA  1 
ATOM   3761  C  C   . VAL D  1 74  ? 57.896  123.457 -14.805 1.00 21.84 ? 47  VAL D C   1 
ATOM   3762  O  O   . VAL D  1 74  ? 57.616  124.362 -13.981 1.00 23.45 ? 47  VAL D O   1 
ATOM   3763  C  CB  . VAL D  1 74  ? 59.912  122.370 -13.833 1.00 21.38 ? 47  VAL D CB  1 
ATOM   3764  C  CG1 . VAL D  1 74  ? 59.129  121.067 -13.507 1.00 19.73 ? 47  VAL D CG1 1 
ATOM   3765  C  CG2 . VAL D  1 74  ? 61.375  122.083 -14.092 1.00 21.14 ? 47  VAL D CG2 1 
ATOM   3766  N  N   . HIS D  1 75  ? 56.961  122.826 -15.510 1.00 20.07 ? 48  HIS D N   1 
ATOM   3767  C  CA  . HIS D  1 75  ? 55.546  123.042 -15.311 1.00 18.54 ? 48  HIS D CA  1 
ATOM   3768  C  C   . HIS D  1 75  ? 54.950  121.935 -14.447 1.00 18.83 ? 48  HIS D C   1 
ATOM   3769  O  O   . HIS D  1 75  ? 55.585  120.916 -14.256 1.00 21.04 ? 48  HIS D O   1 
ATOM   3770  C  CB  . HIS D  1 75  ? 54.818  123.130 -16.664 1.00 19.39 ? 48  HIS D CB  1 
ATOM   3771  C  CG  . HIS D  1 75  ? 55.130  124.385 -17.419 1.00 18.09 ? 48  HIS D CG  1 
ATOM   3772  N  ND1 . HIS D  1 75  ? 54.162  125.296 -17.750 1.00 21.37 ? 48  HIS D ND1 1 
ATOM   3773  C  CD2 . HIS D  1 75  ? 56.292  124.881 -17.888 1.00 20.65 ? 48  HIS D CD2 1 
ATOM   3774  C  CE1 . HIS D  1 75  ? 54.704  126.280 -18.447 1.00 19.39 ? 48  HIS D CE1 1 
ATOM   3775  N  NE2 . HIS D  1 75  ? 55.999  126.064 -18.531 1.00 23.24 ? 48  HIS D NE2 1 
ATOM   3776  N  N   . GLU D  1 76  ? 53.775  122.174 -13.873 1.00 21.21 ? 49  GLU D N   1 
ATOM   3777  C  CA  . GLU D  1 76  ? 53.273  121.367 -12.761 1.00 23.76 ? 49  GLU D CA  1 
ATOM   3778  C  C   . GLU D  1 76  ? 52.895  119.903 -13.124 1.00 23.78 ? 49  GLU D C   1 
ATOM   3779  O  O   . GLU D  1 76  ? 53.163  118.999 -12.333 1.00 22.68 ? 49  GLU D O   1 
ATOM   3780  C  CB  . GLU D  1 76  ? 52.027  121.994 -12.162 1.00 25.55 ? 49  GLU D CB  1 
ATOM   3781  C  CG  . GLU D  1 76  ? 51.591  121.305 -10.871 1.00 29.32 ? 49  GLU D CG  1 
ATOM   3782  C  CD  . GLU D  1 76  ? 50.390  121.960 -10.184 1.00 35.34 ? 49  GLU D CD  1 
ATOM   3783  O  OE1 . GLU D  1 76  ? 49.928  123.020 -10.642 1.00 34.34 ? 49  GLU D OE1 1 
ATOM   3784  O  OE2 . GLU D  1 76  ? 49.883  121.371 -9.207  1.00 35.21 ? 49  GLU D OE2 1 
ATOM   3785  N  N   . PHE D  1 77  ? 52.241  119.685 -14.271 1.00 22.24 ? 50  PHE D N   1 
ATOM   3786  C  CA  . PHE D  1 77  ? 51.785  118.315 -14.613 1.00 24.06 ? 50  PHE D CA  1 
ATOM   3787  C  C   . PHE D  1 77  ? 52.604  117.661 -15.712 1.00 22.81 ? 50  PHE D C   1 
ATOM   3788  O  O   . PHE D  1 77  ? 52.974  118.317 -16.689 1.00 21.69 ? 50  PHE D O   1 
ATOM   3789  C  CB  . PHE D  1 77  ? 50.338  118.335 -15.017 1.00 21.49 ? 50  PHE D CB  1 
ATOM   3790  C  CG  . PHE D  1 77  ? 49.469  119.054 -14.011 1.00 27.24 ? 50  PHE D CG  1 
ATOM   3791  C  CD1 . PHE D  1 77  ? 49.319  118.543 -12.744 1.00 27.71 ? 50  PHE D CD1 1 
ATOM   3792  C  CD2 . PHE D  1 77  ? 48.823  120.251 -14.345 1.00 28.79 ? 50  PHE D CD2 1 
ATOM   3793  C  CE1 . PHE D  1 77  ? 48.536  119.217 -11.785 1.00 34.55 ? 50  PHE D CE1 1 
ATOM   3794  C  CE2 . PHE D  1 77  ? 48.007  120.920 -13.408 1.00 31.23 ? 50  PHE D CE2 1 
ATOM   3795  C  CZ  . PHE D  1 77  ? 47.877  120.397 -12.125 1.00 28.86 ? 50  PHE D CZ  1 
ATOM   3796  N  N   . GLY D  1 78  ? 52.831  116.355 -15.577 1.00 20.86 ? 51  GLY D N   1 
ATOM   3797  C  CA  . GLY D  1 78  ? 53.551  115.600 -16.618 1.00 20.79 ? 51  GLY D CA  1 
ATOM   3798  C  C   . GLY D  1 78  ? 52.466  115.011 -17.542 1.00 21.36 ? 51  GLY D C   1 
ATOM   3799  O  O   . GLY D  1 78  ? 52.451  113.835 -17.834 1.00 22.01 ? 51  GLY D O   1 
ATOM   3800  N  N   . ASP D  1 79  ? 51.556  115.865 -17.983 1.00 21.73 ? 52  ASP D N   1 
ATOM   3801  C  CA  . ASP D  1 79  ? 50.368  115.451 -18.744 1.00 21.42 ? 52  ASP D CA  1 
ATOM   3802  C  C   . ASP D  1 79  ? 50.546  116.053 -20.126 1.00 23.56 ? 52  ASP D C   1 
ATOM   3803  O  O   . ASP D  1 79  ? 50.512  117.300 -20.297 1.00 22.13 ? 52  ASP D O   1 
ATOM   3804  C  CB  . ASP D  1 79  ? 49.125  115.999 -18.040 1.00 21.87 ? 52  ASP D CB  1 
ATOM   3805  C  CG  . ASP D  1 79  ? 47.803  115.687 -18.807 1.00 24.12 ? 52  ASP D CG  1 
ATOM   3806  O  OD1 . ASP D  1 79  ? 47.846  115.410 -20.017 1.00 23.59 ? 52  ASP D OD1 1 
ATOM   3807  O  OD2 . ASP D  1 79  ? 46.714  115.673 -18.191 1.00 26.97 ? 52  ASP D OD2 1 
ATOM   3808  N  N   . ASN D  1 80  ? 50.786  115.190 -21.110 1.00 22.77 ? 53  ASN D N   1 
ATOM   3809  C  CA  . ASN D  1 80  ? 50.970  115.649 -22.463 1.00 24.53 ? 53  ASN D CA  1 
ATOM   3810  C  C   . ASN D  1 80  ? 49.778  115.296 -23.388 1.00 21.32 ? 53  ASN D C   1 
ATOM   3811  O  O   . ASN D  1 80  ? 49.929  115.248 -24.589 1.00 23.50 ? 53  ASN D O   1 
ATOM   3812  C  CB  . ASN D  1 80  ? 52.232  115.001 -23.021 1.00 29.50 ? 53  ASN D CB  1 
ATOM   3813  C  CG  . ASN D  1 80  ? 52.721  115.687 -24.268 1.00 40.26 ? 53  ASN D CG  1 
ATOM   3814  O  OD1 . ASN D  1 80  ? 52.827  116.916 -24.297 1.00 43.85 ? 53  ASN D OD1 1 
ATOM   3815  N  ND2 . ASN D  1 80  ? 53.017  114.903 -25.318 1.00 42.31 ? 53  ASN D ND2 1 
ATOM   3816  N  N   . THR D  1 81  ? 48.622  115.034 -22.829 1.00 20.78 ? 54  THR D N   1 
ATOM   3817  C  CA  . THR D  1 81  ? 47.467  114.565 -23.590 1.00 21.68 ? 54  THR D CA  1 
ATOM   3818  C  C   . THR D  1 81  ? 46.930  115.652 -24.550 1.00 25.48 ? 54  THR D C   1 
ATOM   3819  O  O   . THR D  1 81  ? 46.439  115.317 -25.599 1.00 26.48 ? 54  THR D O   1 
ATOM   3820  C  CB  . THR D  1 81  ? 46.310  114.128 -22.696 1.00 24.09 ? 54  THR D CB  1 
ATOM   3821  O  OG1 . THR D  1 81  ? 45.924  115.211 -21.835 1.00 23.41 ? 54  THR D OG1 1 
ATOM   3822  C  CG2 . THR D  1 81  ? 46.726  112.901 -21.855 1.00 20.85 ? 54  THR D CG2 1 
ATOM   3823  N  N   . ALA D  1 82  ? 47.113  116.926 -24.227 1.00 25.70 ? 55  ALA D N   1 
ATOM   3824  C  CA  . ALA D  1 82  ? 46.783  118.030 -25.184 1.00 32.47 ? 55  ALA D CA  1 
ATOM   3825  C  C   . ALA D  1 82  ? 48.055  118.784 -25.531 1.00 32.06 ? 55  ALA D C   1 
ATOM   3826  O  O   . ALA D  1 82  ? 48.092  120.000 -25.516 1.00 37.38 ? 55  ALA D O   1 
ATOM   3827  C  CB  . ALA D  1 82  ? 45.742  118.982 -24.597 1.00 32.68 ? 55  ALA D CB  1 
ATOM   3828  N  N   . GLY D  1 83  ? 49.131  118.048 -25.779 1.00 27.92 ? 56  GLY D N   1 
ATOM   3829  C  CA  . GLY D  1 83  ? 50.449  118.648 -26.067 1.00 28.22 ? 56  GLY D CA  1 
ATOM   3830  C  C   . GLY D  1 83  ? 50.930  119.379 -24.818 1.00 28.79 ? 56  GLY D C   1 
ATOM   3831  O  O   . GLY D  1 83  ? 50.545  119.021 -23.714 1.00 29.08 ? 56  GLY D O   1 
ATOM   3832  N  N   . CYS D  1 84  ? 51.692  120.458 -25.013 1.00 26.11 ? 57  CYS D N   1 
ATOM   3833  C  CA  . CYS D  1 84  ? 52.364  121.182 -23.913 1.00 25.55 ? 57  CYS D CA  1 
ATOM   3834  C  C   . CYS D  1 84  ? 51.391  121.997 -23.075 1.00 25.71 ? 57  CYS D C   1 
ATOM   3835  O  O   . CYS D  1 84  ? 51.698  122.366 -21.930 1.00 23.43 ? 57  CYS D O   1 
ATOM   3836  C  CB  . CYS D  1 84  ? 53.438  122.101 -24.493 1.00 29.61 ? 57  CYS D CB  1 
ATOM   3837  S  SG  . CYS D  1 84  ? 54.772  121.215 -25.344 1.00 32.92 ? 57  CYS D SG  1 
ATOM   3838  N  N   . THR D  1 85  ? 50.189  122.221 -23.623 1.00 25.45 ? 58  THR D N   1 
ATOM   3839  C  CA  . THR D  1 85  ? 49.087  122.935 -22.939 1.00 28.53 ? 58  THR D CA  1 
ATOM   3840  C  C   . THR D  1 85  ? 48.600  122.263 -21.662 1.00 28.79 ? 58  THR D C   1 
ATOM   3841  O  O   . THR D  1 85  ? 48.313  122.949 -20.643 1.00 25.12 ? 58  THR D O   1 
ATOM   3842  C  CB  . THR D  1 85  ? 47.903  123.119 -23.940 1.00 30.67 ? 58  THR D CB  1 
ATOM   3843  O  OG1 . THR D  1 85  ? 48.425  123.878 -25.038 1.00 34.78 ? 58  THR D OG1 1 
ATOM   3844  C  CG2 . THR D  1 85  ? 46.720  123.865 -23.342 1.00 33.36 ? 58  THR D CG2 1 
ATOM   3845  N  N   . SER D  1 86  ? 48.504  120.928 -21.694 1.00 24.30 ? 59  SER D N   1 
ATOM   3846  C  CA  . SER D  1 86  ? 48.033  120.212 -20.516 1.00 24.45 ? 59  SER D CA  1 
ATOM   3847  C  C   . SER D  1 86  ? 49.094  120.122 -19.411 1.00 21.41 ? 59  SER D C   1 
ATOM   3848  O  O   . SER D  1 86  ? 48.804  119.578 -18.376 1.00 22.04 ? 59  SER D O   1 
ATOM   3849  C  CB  . SER D  1 86  ? 47.459  118.836 -20.874 1.00 25.58 ? 59  SER D CB  1 
ATOM   3850  O  OG  . SER D  1 86  ? 48.239  118.244 -21.899 1.00 28.21 ? 59  SER D OG  1 
ATOM   3851  N  N   . ALA D  1 87  ? 50.284  120.677 -19.600 1.00 20.38 ? 60  ALA D N   1 
ATOM   3852  C  CA  . ALA D  1 87  ? 51.263  120.679 -18.490 1.00 20.82 ? 60  ALA D CA  1 
ATOM   3853  C  C   . ALA D  1 87  ? 50.921  121.699 -17.376 1.00 25.62 ? 60  ALA D C   1 
ATOM   3854  O  O   . ALA D  1 87  ? 51.529  121.638 -16.296 1.00 24.29 ? 60  ALA D O   1 
ATOM   3855  C  CB  . ALA D  1 87  ? 52.675  120.908 -18.974 1.00 21.61 ? 60  ALA D CB  1 
ATOM   3856  N  N   . GLY D  1 88  ? 49.944  122.580 -17.647 1.00 24.43 ? 61  GLY D N   1 
ATOM   3857  C  CA  . GLY D  1 88  ? 49.463  123.549 -16.647 1.00 27.46 ? 61  GLY D CA  1 
ATOM   3858  C  C   . GLY D  1 88  ? 50.511  124.598 -16.371 1.00 25.08 ? 61  GLY D C   1 
ATOM   3859  O  O   . GLY D  1 88  ? 51.404  124.831 -17.184 1.00 24.52 ? 61  GLY D O   1 
ATOM   3860  N  N   . PRO D  1 89  ? 50.424  125.267 -15.198 1.00 29.03 ? 62  PRO D N   1 
ATOM   3861  C  CA  . PRO D  1 89  ? 51.320  126.421 -14.937 1.00 27.75 ? 62  PRO D CA  1 
ATOM   3862  C  C   . PRO D  1 89  ? 52.741  126.041 -14.454 1.00 30.00 ? 62  PRO D C   1 
ATOM   3863  O  O   . PRO D  1 89  ? 53.046  124.833 -14.279 1.00 26.60 ? 62  PRO D O   1 
ATOM   3864  C  CB  . PRO D  1 89  ? 50.544  127.191 -13.833 1.00 29.40 ? 62  PRO D CB  1 
ATOM   3865  C  CG  . PRO D  1 89  ? 49.895  126.119 -13.049 1.00 30.52 ? 62  PRO D CG  1 
ATOM   3866  C  CD  . PRO D  1 89  ? 49.546  124.987 -14.050 1.00 29.06 ? 62  PRO D CD  1 
ATOM   3867  N  N   . HIS D  1 90  ? 53.606  127.040 -14.211 1.00 26.55 ? 63  HIS D N   1 
ATOM   3868  C  CA  . HIS D  1 90  ? 54.921  126.777 -13.617 1.00 26.72 ? 63  HIS D CA  1 
ATOM   3869  C  C   . HIS D  1 90  ? 54.726  126.041 -12.308 1.00 25.58 ? 63  HIS D C   1 
ATOM   3870  O  O   . HIS D  1 90  ? 53.772  126.266 -11.621 1.00 28.69 ? 63  HIS D O   1 
ATOM   3871  C  CB  . HIS D  1 90  ? 55.797  128.047 -13.452 1.00 27.86 ? 63  HIS D CB  1 
ATOM   3872  C  CG  . HIS D  1 90  ? 56.099  128.735 -14.750 1.00 30.57 ? 63  HIS D CG  1 
ATOM   3873  N  ND1 . HIS D  1 90  ? 56.834  129.901 -14.842 1.00 28.64 ? 63  HIS D ND1 1 
ATOM   3874  C  CD2 . HIS D  1 90  ? 55.717  128.440 -16.020 1.00 27.74 ? 63  HIS D CD2 1 
ATOM   3875  C  CE1 . HIS D  1 90  ? 56.910  130.291 -16.095 1.00 31.40 ? 63  HIS D CE1 1 
ATOM   3876  N  NE2 . HIS D  1 90  ? 56.251  129.415 -16.836 1.00 30.83 ? 63  HIS D NE2 1 
ATOM   3877  N  N   . PHE D  1 91  ? 55.582  125.079 -12.049 1.00 24.17 ? 64  PHE D N   1 
ATOM   3878  C  CA  . PHE D  1 91  ? 55.554  124.289 -10.837 1.00 24.40 ? 64  PHE D CA  1 
ATOM   3879  C  C   . PHE D  1 91  ? 55.908  125.264 -9.681  1.00 24.33 ? 64  PHE D C   1 
ATOM   3880  O  O   . PHE D  1 91  ? 56.987  125.837 -9.659  1.00 23.94 ? 64  PHE D O   1 
ATOM   3881  C  CB  . PHE D  1 91  ? 56.580  123.144 -10.915 1.00 25.38 ? 64  PHE D CB  1 
ATOM   3882  C  CG  . PHE D  1 91  ? 56.652  122.286 -9.642  1.00 26.16 ? 64  PHE D CG  1 
ATOM   3883  C  CD1 . PHE D  1 91  ? 55.491  121.821 -9.045  1.00 25.09 ? 64  PHE D CD1 1 
ATOM   3884  C  CD2 . PHE D  1 91  ? 57.886  121.923 -9.115  1.00 26.02 ? 64  PHE D CD2 1 
ATOM   3885  C  CE1 . PHE D  1 91  ? 55.566  121.034 -7.882  1.00 27.84 ? 64  PHE D CE1 1 
ATOM   3886  C  CE2 . PHE D  1 91  ? 57.981  121.130 -7.958  1.00 28.22 ? 64  PHE D CE2 1 
ATOM   3887  C  CZ  . PHE D  1 91  ? 56.800  120.701 -7.346  1.00 25.90 ? 64  PHE D CZ  1 
ATOM   3888  N  N   . ASN D  1 92  ? 54.950  125.406 -8.773  1.00 28.18 ? 65  ASN D N   1 
ATOM   3889  C  CA  . ASN D  1 92  ? 54.955  126.433 -7.693  1.00 32.51 ? 65  ASN D CA  1 
ATOM   3890  C  C   . ASN D  1 92  ? 54.332  125.839 -6.410  1.00 29.73 ? 65  ASN D C   1 
ATOM   3891  O  O   . ASN D  1 92  ? 53.273  126.294 -5.999  1.00 34.00 ? 65  ASN D O   1 
ATOM   3892  C  CB  . ASN D  1 92  ? 54.074  127.588 -8.153  1.00 33.84 ? 65  ASN D CB  1 
ATOM   3893  C  CG  . ASN D  1 92  ? 54.188  128.817 -7.264  1.00 35.61 ? 65  ASN D CG  1 
ATOM   3894  O  OD1 . ASN D  1 92  ? 55.219  129.065 -6.628  1.00 34.62 ? 65  ASN D OD1 1 
ATOM   3895  N  ND2 . ASN D  1 92  ? 53.163  129.615 -7.295  1.00 33.17 ? 65  ASN D ND2 1 
ATOM   3896  N  N   . PRO D  1 93  ? 54.958  124.816 -5.789  1.00 28.78 ? 66  PRO D N   1 
ATOM   3897  C  CA  . PRO D  1 93  ? 54.285  124.274 -4.587  1.00 32.63 ? 66  PRO D CA  1 
ATOM   3898  C  C   . PRO D  1 93  ? 54.255  125.255 -3.373  1.00 39.27 ? 66  PRO D C   1 
ATOM   3899  O  O   . PRO D  1 93  ? 53.429  125.085 -2.475  1.00 40.25 ? 66  PRO D O   1 
ATOM   3900  C  CB  . PRO D  1 93  ? 55.133  123.068 -4.232  1.00 29.92 ? 66  PRO D CB  1 
ATOM   3901  C  CG  . PRO D  1 93  ? 56.491  123.355 -4.761  1.00 30.88 ? 66  PRO D CG  1 
ATOM   3902  C  CD  . PRO D  1 93  ? 56.285  124.210 -5.999  1.00 31.82 ? 66  PRO D CD  1 
ATOM   3903  N  N   . LEU D  1 94  ? 55.154  126.241 -3.367  1.00 40.71 ? 67  LEU D N   1 
ATOM   3904  C  CA  . LEU D  1 94  ? 55.295  127.202 -2.246  1.00 43.32 ? 67  LEU D CA  1 
ATOM   3905  C  C   . LEU D  1 94  ? 54.592  128.505 -2.528  1.00 45.66 ? 67  LEU D C   1 
ATOM   3906  O  O   . LEU D  1 94  ? 54.843  129.479 -1.834  1.00 48.70 ? 67  LEU D O   1 
ATOM   3907  C  CB  . LEU D  1 94  ? 56.769  127.515 -1.980  1.00 42.36 ? 67  LEU D CB  1 
ATOM   3908  C  CG  . LEU D  1 94  ? 57.707  126.356 -1.664  1.00 44.14 ? 67  LEU D CG  1 
ATOM   3909  C  CD1 . LEU D  1 94  ? 59.138  126.881 -1.527  1.00 43.57 ? 67  LEU D CD1 1 
ATOM   3910  C  CD2 . LEU D  1 94  ? 57.265  125.537 -0.449  1.00 44.87 ? 67  LEU D CD2 1 
ATOM   3911  N  N   . SER D  1 95  ? 53.783  128.540 -3.591  1.00 42.71 ? 68  SER D N   1 
ATOM   3912  C  CA  . SER D  1 95  ? 52.906  129.669 -3.935  1.00 46.24 ? 68  SER D CA  1 
ATOM   3913  C  C   . SER D  1 95  ? 53.581  131.036 -4.029  1.00 44.82 ? 68  SER D C   1 
ATOM   3914  O  O   . SER D  1 95  ? 52.986  132.048 -3.695  1.00 50.43 ? 68  SER D O   1 
ATOM   3915  C  CB  . SER D  1 95  ? 51.720  129.716 -2.963  1.00 46.23 ? 68  SER D CB  1 
ATOM   3916  O  OG  . SER D  1 95  ? 50.927  128.564 -3.152  1.00 49.82 ? 68  SER D OG  1 
ATOM   3917  N  N   . ARG D  1 96  ? 54.817  131.078 -4.502  1.00 44.45 ? 69  ARG D N   1 
ATOM   3918  C  CA  . ARG D  1 96  ? 55.472  132.364 -4.696  1.00 42.09 ? 69  ARG D CA  1 
ATOM   3919  C  C   . ARG D  1 96  ? 55.148  132.981 -6.068  1.00 47.19 ? 69  ARG D C   1 
ATOM   3920  O  O   . ARG D  1 96  ? 54.367  132.424 -6.843  1.00 42.61 ? 69  ARG D O   1 
ATOM   3921  C  CB  . ARG D  1 96  ? 56.970  132.222 -4.499  1.00 42.80 ? 69  ARG D CB  1 
ATOM   3922  C  CG  . ARG D  1 96  ? 57.331  131.579 -3.177  1.00 47.80 ? 69  ARG D CG  1 
ATOM   3923  C  CD  . ARG D  1 96  ? 58.707  132.031 -2.746  1.00 53.94 ? 69  ARG D CD  1 
ATOM   3924  N  NE  . ARG D  1 96  ? 58.986  131.559 -1.396  1.00 64.41 ? 69  ARG D NE  1 
ATOM   3925  C  CZ  . ARG D  1 96  ? 60.093  130.914 -1.039  1.00 64.97 ? 69  ARG D CZ  1 
ATOM   3926  N  NH1 . ARG D  1 96  ? 61.050  130.680 -1.924  1.00 70.48 ? 69  ARG D NH1 1 
ATOM   3927  N  NH2 . ARG D  1 96  ? 60.248  130.522 0.217   1.00 67.05 ? 69  ARG D NH2 1 
ATOM   3928  N  N   . LYS D  1 97  ? 55.732  134.144 -6.341  1.00 43.80 ? 70  LYS D N   1 
ATOM   3929  C  CA  . LYS D  1 97  ? 55.619  134.779 -7.640  1.00 42.42 ? 70  LYS D CA  1 
ATOM   3930  C  C   . LYS D  1 97  ? 56.789  134.361 -8.535  1.00 39.35 ? 70  LYS D C   1 
ATOM   3931  O  O   . LYS D  1 97  ? 57.808  133.818 -8.061  1.00 37.24 ? 70  LYS D O   1 
ATOM   3932  C  CB  . LYS D  1 97  ? 55.533  136.319 -7.475  1.00 47.07 ? 70  LYS D CB  1 
ATOM   3933  C  CG  . LYS D  1 97  ? 54.277  136.763 -6.716  1.00 50.24 ? 70  LYS D CG  1 
ATOM   3934  C  CD  . LYS D  1 97  ? 53.948  138.247 -6.855  1.00 58.14 ? 70  LYS D CD  1 
ATOM   3935  C  CE  . LYS D  1 97  ? 52.571  138.559 -6.274  1.00 62.24 ? 70  LYS D CE  1 
ATOM   3936  N  NZ  . LYS D  1 97  ? 51.522  137.683 -6.873  1.00 63.52 ? 70  LYS D NZ  1 
ATOM   3937  N  N   . HIS D  1 98  ? 56.635  134.611 -9.838  1.00 38.13 ? 71  HIS D N   1 
ATOM   3938  C  CA  . HIS D  1 98  ? 57.632  134.264 -10.810 1.00 33.38 ? 71  HIS D CA  1 
ATOM   3939  C  C   . HIS D  1 98  ? 58.961  135.047 -10.647 1.00 35.44 ? 71  HIS D C   1 
ATOM   3940  O  O   . HIS D  1 98  ? 58.948  136.246 -10.387 1.00 39.12 ? 71  HIS D O   1 
ATOM   3941  C  CB  . HIS D  1 98  ? 57.008  134.409 -12.221 1.00 37.00 ? 71  HIS D CB  1 
ATOM   3942  C  CG  . HIS D  1 98  ? 57.968  134.080 -13.310 1.00 36.92 ? 71  HIS D CG  1 
ATOM   3943  N  ND1 . HIS D  1 98  ? 58.301  132.782 -13.636 1.00 33.56 ? 71  HIS D ND1 1 
ATOM   3944  C  CD2 . HIS D  1 98  ? 58.755  134.874 -14.073 1.00 36.08 ? 71  HIS D CD2 1 
ATOM   3945  C  CE1 . HIS D  1 98  ? 59.240  132.787 -14.563 1.00 34.33 ? 71  HIS D CE1 1 
ATOM   3946  N  NE2 . HIS D  1 98  ? 59.532  134.045 -14.850 1.00 35.77 ? 71  HIS D NE2 1 
ATOM   3947  N  N   . GLY D  1 99  ? 60.104  134.400 -10.806 1.00 31.67 ? 72  GLY D N   1 
ATOM   3948  C  CA  . GLY D  1 99  ? 61.410  135.097 -10.836 1.00 33.66 ? 72  GLY D CA  1 
ATOM   3949  C  C   . GLY D  1 99  ? 62.418  134.375 -11.703 1.00 38.99 ? 72  GLY D C   1 
ATOM   3950  O  O   . GLY D  1 99  ? 62.087  133.419 -12.429 1.00 40.87 ? 72  GLY D O   1 
ATOM   3951  N  N   . GLY D  1 100 ? 63.657  134.821 -11.650 1.00 32.17 ? 73  GLY D N   1 
ATOM   3952  C  CA  . GLY D  1 100 ? 64.739  134.134 -12.317 1.00 37.23 ? 73  GLY D CA  1 
ATOM   3953  C  C   . GLY D  1 100 ? 65.224  133.050 -11.376 1.00 33.40 ? 73  GLY D C   1 
ATOM   3954  O  O   . GLY D  1 100 ? 64.836  133.042 -10.207 1.00 35.96 ? 73  GLY D O   1 
ATOM   3955  N  N   . PRO D  1 101 ? 66.089  132.154 -11.868 1.00 33.95 ? 74  PRO D N   1 
ATOM   3956  C  CA  . PRO D  1 101 ? 66.517  131.073 -10.989 1.00 34.34 ? 74  PRO D CA  1 
ATOM   3957  C  C   . PRO D  1 101 ? 67.449  131.556 -9.836  1.00 40.19 ? 74  PRO D C   1 
ATOM   3958  O  O   . PRO D  1 101 ? 67.538  130.869 -8.796  1.00 34.43 ? 74  PRO D O   1 
ATOM   3959  C  CB  . PRO D  1 101 ? 67.298  130.164 -11.921 1.00 37.49 ? 74  PRO D CB  1 
ATOM   3960  C  CG  . PRO D  1 101 ? 67.819  131.065 -12.999 1.00 35.71 ? 74  PRO D CG  1 
ATOM   3961  C  CD  . PRO D  1 101 ? 66.723  132.071 -13.195 1.00 33.50 ? 74  PRO D CD  1 
ATOM   3962  N  N   . LYS D  1 102 ? 68.143  132.689 -10.017 1.00 38.49 ? 75  LYS D N   1 
ATOM   3963  C  CA  . LYS D  1 102 ? 69.057  133.177 -8.960  1.00 42.40 ? 75  LYS D CA  1 
ATOM   3964  C  C   . LYS D  1 102 ? 68.358  134.098 -7.972  1.00 43.20 ? 75  LYS D C   1 
ATOM   3965  O  O   . LYS D  1 102 ? 68.992  134.557 -7.024  1.00 47.57 ? 75  LYS D O   1 
ATOM   3966  C  CB  . LYS D  1 102 ? 70.330  133.841 -9.513  1.00 44.67 ? 75  LYS D CB  1 
ATOM   3967  C  CG  . LYS D  1 102 ? 71.219  132.989 -10.429 1.00 51.41 ? 75  LYS D CG  1 
ATOM   3968  C  CD  . LYS D  1 102 ? 71.536  131.587 -9.895  1.00 58.68 ? 75  LYS D CD  1 
ATOM   3969  C  CE  . LYS D  1 102 ? 72.340  130.785 -10.922 1.00 62.21 ? 75  LYS D CE  1 
ATOM   3970  N  NZ  . LYS D  1 102 ? 72.727  129.422 -10.442 1.00 59.42 ? 75  LYS D NZ  1 
ATOM   3971  N  N   . ASP D  1 103 ? 67.062  134.338 -8.157  1.00 39.00 ? 76  ASP D N   1 
ATOM   3972  C  CA  . ASP D  1 103 ? 66.245  135.106 -7.220  1.00 41.30 ? 76  ASP D CA  1 
ATOM   3973  C  C   . ASP D  1 103 ? 65.640  134.310 -6.058  1.00 46.67 ? 76  ASP D C   1 
ATOM   3974  O  O   . ASP D  1 103 ? 65.238  133.158 -6.245  1.00 40.81 ? 76  ASP D O   1 
ATOM   3975  C  CB  . ASP D  1 103 ? 65.060  135.680 -7.962  1.00 45.38 ? 76  ASP D CB  1 
ATOM   3976  C  CG  . ASP D  1 103 ? 65.281  137.112 -8.428  1.00 53.58 ? 76  ASP D CG  1 
ATOM   3977  O  OD1 . ASP D  1 103 ? 66.433  137.527 -8.786  1.00 46.08 ? 76  ASP D OD1 1 
ATOM   3978  O  OD2 . ASP D  1 103 ? 64.250  137.827 -8.436  1.00 60.26 ? 76  ASP D OD2 1 
ATOM   3979  N  N   . GLU D  1 104 ? 65.504  134.955 -4.883  1.00 47.60 ? 77  GLU D N   1 
ATOM   3980  C  CA  . GLU D  1 104 ? 64.856  134.359 -3.680  1.00 45.12 ? 77  GLU D CA  1 
ATOM   3981  C  C   . GLU D  1 104 ? 63.378  134.133 -3.949  1.00 43.58 ? 77  GLU D C   1 
ATOM   3982  O  O   . GLU D  1 104 ? 62.769  133.126 -3.542  1.00 40.19 ? 77  GLU D O   1 
ATOM   3983  C  CB  . GLU D  1 104 ? 64.931  135.328 -2.461  1.00 51.92 ? 77  GLU D CB  1 
ATOM   3984  C  CG  . GLU D  1 104 ? 65.985  135.082 -1.374  1.00 59.12 ? 77  GLU D CG  1 
ATOM   3985  C  CD  . GLU D  1 104 ? 66.106  136.258 -0.345  1.00 57.60 ? 77  GLU D CD  1 
ATOM   3986  O  OE1 . GLU D  1 104 ? 65.894  136.016 0.890   1.00 52.74 ? 77  GLU D OE1 1 
ATOM   3987  O  OE2 . GLU D  1 104 ? 66.424  137.430 -0.761  1.00 46.73 ? 77  GLU D OE2 1 
ATOM   3988  N  N   . GLU D  1 105 ? 62.751  135.112 -4.584  1.00 37.57 ? 78  GLU D N   1 
ATOM   3989  C  CA  . GLU D  1 105 ? 61.345  134.950 -4.855  1.00 39.49 ? 78  GLU D CA  1 
ATOM   3990  C  C   . GLU D  1 105 ? 61.233  134.347 -6.297  1.00 38.62 ? 78  GLU D C   1 
ATOM   3991  O  O   . GLU D  1 105 ? 61.440  135.056 -7.285  1.00 37.31 ? 78  GLU D O   1 
ATOM   3992  C  CB  . GLU D  1 105 ? 60.620  136.277 -4.741  1.00 40.62 ? 78  GLU D CB  1 
ATOM   3993  C  CG  . GLU D  1 105 ? 59.134  136.248 -5.078  1.00 41.59 ? 78  GLU D CG  1 
ATOM   3994  C  CD  . GLU D  1 105 ? 58.276  135.749 -3.936  1.00 48.83 ? 78  GLU D CD  1 
ATOM   3995  O  OE1 . GLU D  1 105 ? 58.852  135.349 -2.892  1.00 54.87 ? 78  GLU D OE1 1 
ATOM   3996  O  OE2 . GLU D  1 105 ? 57.027  135.739 -4.077  1.00 46.44 ? 78  GLU D OE2 1 
ATOM   3997  N  N   . ARG D  1 106 ? 60.923  133.050 -6.395  1.00 38.33 ? 79  ARG D N   1 
ATOM   3998  C  CA  . ARG D  1 106 ? 60.809  132.376 -7.724  1.00 32.12 ? 79  ARG D CA  1 
ATOM   3999  C  C   . ARG D  1 106 ? 59.937  131.152 -7.583  1.00 35.15 ? 79  ARG D C   1 
ATOM   4000  O  O   . ARG D  1 106 ? 59.724  130.692 -6.461  1.00 35.11 ? 79  ARG D O   1 
ATOM   4001  C  CB  . ARG D  1 106 ? 62.175  131.936 -8.181  1.00 35.91 ? 79  ARG D CB  1 
ATOM   4002  C  CG  . ARG D  1 106 ? 62.796  130.948 -7.224  1.00 33.19 ? 79  ARG D CG  1 
ATOM   4003  C  CD  . ARG D  1 106 ? 64.038  130.382 -7.825  1.00 34.64 ? 79  ARG D CD  1 
ATOM   4004  N  NE  . ARG D  1 106 ? 63.738  129.104 -8.465  1.00 28.96 ? 79  ARG D NE  1 
ATOM   4005  C  CZ  . ARG D  1 106 ? 64.668  128.269 -8.929  1.00 29.60 ? 79  ARG D CZ  1 
ATOM   4006  N  NH1 . ARG D  1 106 ? 65.953  128.566 -8.825  1.00 30.21 ? 79  ARG D NH1 1 
ATOM   4007  N  NH2 . ARG D  1 106 ? 64.324  127.073 -9.448  1.00 28.39 ? 79  ARG D NH2 1 
ATOM   4008  N  N   . HIS D  1 107 ? 59.392  130.619 -8.683  1.00 31.58 ? 80  HIS D N   1 
ATOM   4009  C  CA  . HIS D  1 107 ? 58.648  129.328 -8.601  1.00 28.34 ? 80  HIS D CA  1 
ATOM   4010  C  C   . HIS D  1 107 ? 59.733  128.279 -8.501  1.00 25.77 ? 80  HIS D C   1 
ATOM   4011  O  O   . HIS D  1 107 ? 60.868  128.513 -8.977  1.00 27.03 ? 80  HIS D O   1 
ATOM   4012  C  CB  . HIS D  1 107 ? 57.762  129.072 -9.857  1.00 30.79 ? 80  HIS D CB  1 
ATOM   4013  C  CG  . HIS D  1 107 ? 56.665  130.093 -10.101 1.00 31.64 ? 80  HIS D CG  1 
ATOM   4014  N  ND1 . HIS D  1 107 ? 56.361  130.604 -11.360 1.00 36.27 ? 80  HIS D ND1 1 
ATOM   4015  C  CD2 . HIS D  1 107 ? 55.794  130.682 -9.248  1.00 35.14 ? 80  HIS D CD2 1 
ATOM   4016  C  CE1 . HIS D  1 107 ? 55.337  131.435 -11.264 1.00 34.95 ? 80  HIS D CE1 1 
ATOM   4017  N  NE2 . HIS D  1 107 ? 54.979  131.502 -9.995  1.00 33.05 ? 80  HIS D NE2 1 
ATOM   4018  N  N   . VAL D  1 108 ? 59.418  127.109 -7.925  1.00 26.19 ? 81  VAL D N   1 
ATOM   4019  C  CA  . VAL D  1 108 ? 60.401  126.047 -7.940  1.00 25.73 ? 81  VAL D CA  1 
ATOM   4020  C  C   . VAL D  1 108 ? 60.802  125.749 -9.392  1.00 22.05 ? 81  VAL D C   1 
ATOM   4021  O  O   . VAL D  1 108 ? 61.960  125.508 -9.703  1.00 26.75 ? 81  VAL D O   1 
ATOM   4022  C  CB  . VAL D  1 108 ? 59.885  124.778 -7.223  1.00 26.38 ? 81  VAL D CB  1 
ATOM   4023  C  CG1 . VAL D  1 108 ? 60.819  123.582 -7.543  1.00 26.42 ? 81  VAL D CG1 1 
ATOM   4024  C  CG2 . VAL D  1 108 ? 59.851  125.057 -5.718  1.00 27.41 ? 81  VAL D CG2 1 
ATOM   4025  N  N   . GLY D  1 109 ? 59.839  125.818 -10.297 1.00 26.86 ? 82  GLY D N   1 
ATOM   4026  C  CA  . GLY D  1 109 ? 60.160  125.451 -11.688 1.00 26.78 ? 82  GLY D CA  1 
ATOM   4027  C  C   . GLY D  1 109 ? 60.827  126.527 -12.550 1.00 27.50 ? 82  GLY D C   1 
ATOM   4028  O  O   . GLY D  1 109 ? 61.016  126.324 -13.755 1.00 24.78 ? 82  GLY D O   1 
ATOM   4029  N  N   . ASP D  1 110 ? 61.247  127.644 -11.954 1.00 29.05 ? 83  ASP D N   1 
ATOM   4030  C  CA  . ASP D  1 110 ? 61.825  128.756 -12.770 1.00 26.74 ? 83  ASP D CA  1 
ATOM   4031  C  C   . ASP D  1 110 ? 63.284  128.623 -13.071 1.00 30.41 ? 83  ASP D C   1 
ATOM   4032  O  O   . ASP D  1 110 ? 64.138  128.970 -12.239 1.00 33.99 ? 83  ASP D O   1 
ATOM   4033  C  CB  . ASP D  1 110 ? 61.585  130.085 -12.075 1.00 30.47 ? 83  ASP D CB  1 
ATOM   4034  C  CG  . ASP D  1 110 ? 60.132  130.500 -12.049 1.00 29.86 ? 83  ASP D CG  1 
ATOM   4035  O  OD1 . ASP D  1 110 ? 59.282  130.059 -12.874 1.00 30.37 ? 83  ASP D OD1 1 
ATOM   4036  O  OD2 . ASP D  1 110 ? 59.782  131.383 -11.222 1.00 31.30 ? 83  ASP D OD2 1 
ATOM   4037  N  N   . LEU D  1 111 ? 63.615  128.141 -14.265 1.00 23.38 ? 84  LEU D N   1 
ATOM   4038  C  CA  . LEU D  1 111 ? 64.980  127.866 -14.585 1.00 24.10 ? 84  LEU D CA  1 
ATOM   4039  C  C   . LEU D  1 111 ? 65.550  128.918 -15.560 1.00 22.35 ? 84  LEU D C   1 
ATOM   4040  O  O   . LEU D  1 111 ? 66.600  128.716 -16.169 1.00 27.32 ? 84  LEU D O   1 
ATOM   4041  C  CB  . LEU D  1 111 ? 65.120  126.471 -15.171 1.00 25.43 ? 84  LEU D CB  1 
ATOM   4042  C  CG  . LEU D  1 111 ? 64.673  125.369 -14.187 1.00 27.12 ? 84  LEU D CG  1 
ATOM   4043  C  CD1 . LEU D  1 111 ? 65.040  124.031 -14.794 1.00 27.28 ? 84  LEU D CD1 1 
ATOM   4044  C  CD2 . LEU D  1 111 ? 65.388  125.593 -12.846 1.00 26.99 ? 84  LEU D CD2 1 
ATOM   4045  N  N   . GLY D  1 112 ? 64.847  130.027 -15.672 1.00 24.12 ? 85  GLY D N   1 
ATOM   4046  C  CA  . GLY D  1 112 ? 65.439  131.243 -16.362 1.00 26.14 ? 85  GLY D CA  1 
ATOM   4047  C  C   . GLY D  1 112 ? 65.330  131.134 -17.879 1.00 28.20 ? 85  GLY D C   1 
ATOM   4048  O  O   . GLY D  1 112 ? 64.280  130.719 -18.387 1.00 30.48 ? 85  GLY D O   1 
ATOM   4049  N  N   . ASN D  1 113 ? 66.395  131.475 -18.585 1.00 27.54 ? 86  ASN D N   1 
ATOM   4050  C  CA  . ASN D  1 113 ? 66.401  131.416 -20.050 1.00 29.46 ? 86  ASN D CA  1 
ATOM   4051  C  C   . ASN D  1 113 ? 67.478  130.553 -20.531 1.00 28.96 ? 86  ASN D C   1 
ATOM   4052  O  O   . ASN D  1 113 ? 68.522  130.507 -19.900 1.00 31.52 ? 86  ASN D O   1 
ATOM   4053  C  CB  . ASN D  1 113 ? 66.691  132.821 -20.604 1.00 29.03 ? 86  ASN D CB  1 
ATOM   4054  C  CG  . ASN D  1 113 ? 65.503  133.707 -20.514 1.00 29.04 ? 86  ASN D CG  1 
ATOM   4055  O  OD1 . ASN D  1 113 ? 64.469  133.426 -21.092 1.00 31.72 ? 86  ASN D OD1 1 
ATOM   4056  N  ND2 . ASN D  1 113 ? 65.616  134.765 -19.743 1.00 31.62 ? 86  ASN D ND2 1 
ATOM   4057  N  N   . VAL D  1 114 ? 67.269  129.877 -21.676 1.00 25.15 ? 87  VAL D N   1 
ATOM   4058  C  CA  . VAL D  1 114 ? 68.349  129.301 -22.368 1.00 24.82 ? 87  VAL D CA  1 
ATOM   4059  C  C   . VAL D  1 114 ? 68.635  130.186 -23.582 1.00 25.89 ? 87  VAL D C   1 
ATOM   4060  O  O   . VAL D  1 114 ? 67.789  130.946 -23.975 1.00 25.79 ? 87  VAL D O   1 
ATOM   4061  C  CB  . VAL D  1 114 ? 68.065  127.842 -22.780 1.00 27.79 ? 87  VAL D CB  1 
ATOM   4062  C  CG1 . VAL D  1 114 ? 67.897  127.006 -21.505 1.00 24.46 ? 87  VAL D CG1 1 
ATOM   4063  C  CG2 . VAL D  1 114 ? 66.804  127.745 -23.672 1.00 24.72 ? 87  VAL D CG2 1 
ATOM   4064  N  N   . THR D  1 115 ? 69.815  130.052 -24.140 1.00 28.96 ? 88  THR D N   1 
ATOM   4065  C  CA  . THR D  1 115 ? 70.259  130.926 -25.236 1.00 31.96 ? 88  THR D CA  1 
ATOM   4066  C  C   . THR D  1 115 ? 70.531  130.097 -26.461 1.00 28.46 ? 88  THR D C   1 
ATOM   4067  O  O   . THR D  1 115 ? 71.430  129.235 -26.463 1.00 28.69 ? 88  THR D O   1 
ATOM   4068  C  CB  . THR D  1 115 ? 71.588  131.664 -24.879 1.00 34.33 ? 88  THR D CB  1 
ATOM   4069  O  OG1 . THR D  1 115 ? 71.339  132.555 -23.792 1.00 34.80 ? 88  THR D OG1 1 
ATOM   4070  C  CG2 . THR D  1 115 ? 72.134  132.457 -26.086 1.00 35.32 ? 88  THR D CG2 1 
ATOM   4071  N  N   . ALA D  1 116 ? 69.786  130.382 -27.524 1.00 28.04 ? 89  ALA D N   1 
ATOM   4072  C  CA  . ALA D  1 116 ? 70.072  129.754 -28.793 1.00 26.15 ? 89  ALA D CA  1 
ATOM   4073  C  C   . ALA D  1 116 ? 71.024  130.630 -29.633 1.00 28.02 ? 89  ALA D C   1 
ATOM   4074  O  O   . ALA D  1 116 ? 70.806  131.836 -29.740 1.00 26.67 ? 89  ALA D O   1 
ATOM   4075  C  CB  . ALA D  1 116 ? 68.780  129.492 -29.543 1.00 25.30 ? 89  ALA D CB  1 
ATOM   4076  N  N   . ASP D  1 117 ? 72.053  129.998 -30.189 1.00 29.81 ? 90  ASP D N   1 
ATOM   4077  C  CA  . ASP D  1 117 ? 72.980  130.615 -31.125 1.00 34.71 ? 90  ASP D CA  1 
ATOM   4078  C  C   . ASP D  1 117 ? 72.355  130.899 -32.502 1.00 36.63 ? 90  ASP D C   1 
ATOM   4079  O  O   . ASP D  1 117 ? 71.126  130.724 -32.687 1.00 32.73 ? 90  ASP D O   1 
ATOM   4080  C  CB  . ASP D  1 117 ? 74.315  129.821 -31.218 1.00 34.15 ? 90  ASP D CB  1 
ATOM   4081  C  CG  . ASP D  1 117 ? 74.187  128.454 -31.917 1.00 36.97 ? 90  ASP D CG  1 
ATOM   4082  O  OD1 . ASP D  1 117 ? 73.207  128.178 -32.634 1.00 36.61 ? 90  ASP D OD1 1 
ATOM   4083  O  OD2 . ASP D  1 117 ? 75.112  127.632 -31.767 1.00 39.83 ? 90  ASP D OD2 1 
ATOM   4084  N  N   . LYS D  1 118 ? 73.189  131.387 -33.435 1.00 36.00 ? 91  LYS D N   1 
ATOM   4085  C  CA  . LYS D  1 118 ? 72.757  131.699 -34.798 1.00 40.16 ? 91  LYS D CA  1 
ATOM   4086  C  C   . LYS D  1 118 ? 72.277  130.462 -35.547 1.00 35.12 ? 91  LYS D C   1 
ATOM   4087  O  O   . LYS D  1 118 ? 71.440  130.562 -36.433 1.00 37.09 ? 91  LYS D O   1 
ATOM   4088  C  CB  . LYS D  1 118 ? 73.868  132.439 -35.593 1.00 41.85 ? 91  LYS D CB  1 
ATOM   4089  C  CG  . LYS D  1 118 ? 75.094  131.598 -35.971 1.00 46.91 ? 91  LYS D CG  1 
ATOM   4090  C  CD  . LYS D  1 118 ? 76.164  132.415 -36.729 1.00 54.26 ? 91  LYS D CD  1 
ATOM   4091  C  CE  . LYS D  1 118 ? 77.312  131.535 -37.226 1.00 57.40 ? 91  LYS D CE  1 
ATOM   4092  N  NZ  . LYS D  1 118 ? 76.842  130.497 -38.203 1.00 58.98 ? 91  LYS D NZ  1 
ATOM   4093  N  N   . ASP D  1 119 ? 72.788  129.294 -35.187 1.00 36.81 ? 92  ASP D N   1 
ATOM   4094  C  CA  . ASP D  1 119 ? 72.319  128.033 -35.771 1.00 32.20 ? 92  ASP D CA  1 
ATOM   4095  C  C   . ASP D  1 119 ? 71.059  127.440 -35.092 1.00 34.34 ? 92  ASP D C   1 
ATOM   4096  O  O   . ASP D  1 119 ? 70.668  126.332 -35.404 1.00 33.52 ? 92  ASP D O   1 
ATOM   4097  C  CB  . ASP D  1 119 ? 73.423  127.001 -35.682 1.00 39.42 ? 92  ASP D CB  1 
ATOM   4098  C  CG  . ASP D  1 119 ? 74.615  127.349 -36.572 1.00 45.64 ? 92  ASP D CG  1 
ATOM   4099  O  OD1 . ASP D  1 119 ? 74.424  128.038 -37.597 1.00 47.35 ? 92  ASP D OD1 1 
ATOM   4100  O  OD2 . ASP D  1 119 ? 75.727  126.913 -36.249 1.00 44.63 ? 92  ASP D OD2 1 
ATOM   4101  N  N   . GLY D  1 120 ? 70.444  128.156 -34.173 1.00 29.28 ? 93  GLY D N   1 
ATOM   4102  C  CA  . GLY D  1 120 ? 69.214  127.667 -33.523 1.00 32.33 ? 93  GLY D CA  1 
ATOM   4103  C  C   . GLY D  1 120 ? 69.442  126.663 -32.382 1.00 27.54 ? 93  GLY D C   1 
ATOM   4104  O  O   . GLY D  1 120 ? 68.472  126.027 -31.915 1.00 25.62 ? 93  GLY D O   1 
ATOM   4105  N  N   . VAL D  1 121 ? 70.695  126.512 -31.955 1.00 27.13 ? 94  VAL D N   1 
ATOM   4106  C  CA  . VAL D  1 121 ? 71.076  125.556 -30.871 1.00 29.64 ? 94  VAL D CA  1 
ATOM   4107  C  C   . VAL D  1 121 ? 71.343  126.241 -29.511 1.00 31.69 ? 94  VAL D C   1 
ATOM   4108  O  O   . VAL D  1 121 ? 72.136  127.198 -29.429 1.00 29.17 ? 94  VAL D O   1 
ATOM   4109  C  CB  . VAL D  1 121 ? 72.323  124.693 -31.220 1.00 31.23 ? 94  VAL D CB  1 
ATOM   4110  C  CG1 . VAL D  1 121 ? 72.625  123.714 -30.080 1.00 33.32 ? 94  VAL D CG1 1 
ATOM   4111  C  CG2 . VAL D  1 121 ? 72.171  123.937 -32.542 1.00 31.37 ? 94  VAL D CG2 1 
ATOM   4112  N  N   . ALA D  1 122 ? 70.685  125.754 -28.453 1.00 27.52 ? 95  ALA D N   1 
ATOM   4113  C  CA  . ALA D  1 122 ? 70.938  126.203 -27.090 1.00 29.51 ? 95  ALA D CA  1 
ATOM   4114  C  C   . ALA D  1 122 ? 71.712  125.082 -26.408 1.00 33.10 ? 95  ALA D C   1 
ATOM   4115  O  O   . ALA D  1 122 ? 71.219  123.943 -26.294 1.00 29.61 ? 95  ALA D O   1 
ATOM   4116  C  CB  . ALA D  1 122 ? 69.625  126.475 -26.364 1.00 29.64 ? 95  ALA D CB  1 
ATOM   4117  N  N   . ASP D  1 123 ? 72.947  125.362 -26.013 1.00 29.64 ? 96  ASP D N   1 
ATOM   4118  C  CA  . ASP D  1 123 ? 73.653  124.451 -25.134 1.00 32.01 ? 96  ASP D CA  1 
ATOM   4119  C  C   . ASP D  1 123 ? 73.329  124.799 -23.680 1.00 33.51 ? 96  ASP D C   1 
ATOM   4120  O  O   . ASP D  1 123 ? 73.619  125.895 -23.226 1.00 33.80 ? 96  ASP D O   1 
ATOM   4121  C  CB  . ASP D  1 123 ? 75.126  124.465 -25.441 1.00 36.55 ? 96  ASP D CB  1 
ATOM   4122  C  CG  . ASP D  1 123 ? 75.436  123.707 -26.717 1.00 43.87 ? 96  ASP D CG  1 
ATOM   4123  O  OD1 . ASP D  1 123 ? 74.664  122.770 -27.119 1.00 49.87 ? 96  ASP D OD1 1 
ATOM   4124  O  OD2 . ASP D  1 123 ? 76.452  124.042 -27.339 1.00 52.20 ? 96  ASP D OD2 1 
ATOM   4125  N  N   . VAL D  1 124 ? 72.685  123.880 -22.952 1.00 26.76 ? 97  VAL D N   1 
ATOM   4126  C  CA  . VAL D  1 124 ? 72.134  124.190 -21.629 1.00 25.34 ? 97  VAL D CA  1 
ATOM   4127  C  C   . VAL D  1 124 ? 73.110  123.645 -20.592 1.00 25.13 ? 97  VAL D C   1 
ATOM   4128  O  O   . VAL D  1 124 ? 73.596  122.499 -20.687 1.00 25.05 ? 97  VAL D O   1 
ATOM   4129  C  CB  . VAL D  1 124 ? 70.707  123.567 -21.401 1.00 25.68 ? 97  VAL D CB  1 
ATOM   4130  C  CG1 . VAL D  1 124 ? 70.144  123.927 -20.038 1.00 24.26 ? 97  VAL D CG1 1 
ATOM   4131  C  CG2 . VAL D  1 124 ? 69.726  124.036 -22.476 1.00 25.22 ? 97  VAL D CG2 1 
ATOM   4132  N  N   . SER D  1 125 ? 73.440  124.492 -19.634 1.00 29.74 ? 98  SER D N   1 
ATOM   4133  C  CA  . SER D  1 125 ? 74.331  124.087 -18.547 1.00 31.74 ? 98  SER D CA  1 
ATOM   4134  C  C   . SER D  1 125 ? 74.013  124.947 -17.350 1.00 35.20 ? 98  SER D C   1 
ATOM   4135  O  O   . SER D  1 125 ? 74.355  126.119 -17.301 1.00 37.97 ? 98  SER D O   1 
ATOM   4136  C  CB  . SER D  1 125 ? 75.781  124.233 -18.953 1.00 37.80 ? 98  SER D CB  1 
ATOM   4137  O  OG  . SER D  1 125 ? 76.606  123.633 -17.983 1.00 43.07 ? 98  SER D OG  1 
ATOM   4138  N  N   . ILE D  1 126 ? 73.327  124.356 -16.379 1.00 30.27 ? 99  ILE D N   1 
ATOM   4139  C  CA  . ILE D  1 126 ? 72.704  125.053 -15.299 1.00 30.78 ? 99  ILE D CA  1 
ATOM   4140  C  C   . ILE D  1 126 ? 73.054  124.226 -14.021 1.00 32.58 ? 99  ILE D C   1 
ATOM   4141  O  O   . ILE D  1 126 ? 73.180  122.978 -14.059 1.00 29.72 ? 99  ILE D O   1 
ATOM   4142  C  CB  . ILE D  1 126 ? 71.172  125.066 -15.549 1.00 31.87 ? 99  ILE D CB  1 
ATOM   4143  C  CG1 . ILE D  1 126 ? 70.782  126.099 -16.615 1.00 38.11 ? 99  ILE D CG1 1 
ATOM   4144  C  CG2 . ILE D  1 126 ? 70.369  125.372 -14.303 1.00 36.62 ? 99  ILE D CG2 1 
ATOM   4145  C  CD1 . ILE D  1 126 ? 69.291  126.078 -16.934 1.00 37.85 ? 99  ILE D CD1 1 
ATOM   4146  N  N   . GLU D  1 127 ? 73.249  124.922 -12.915 1.00 32.17 ? 100 GLU D N   1 
ATOM   4147  C  CA  . GLU D  1 127 ? 73.226  124.266 -11.627 1.00 35.55 ? 100 GLU D CA  1 
ATOM   4148  C  C   . GLU D  1 127 ? 72.190  124.987 -10.832 1.00 33.16 ? 100 GLU D C   1 
ATOM   4149  O  O   . GLU D  1 127 ? 72.155  126.202 -10.797 1.00 37.30 ? 100 GLU D O   1 
ATOM   4150  C  CB  . GLU D  1 127 ? 74.595  124.293 -10.943 1.00 39.29 ? 100 GLU D CB  1 
ATOM   4151  C  CG  . GLU D  1 127 ? 74.575  123.530 -9.629  1.00 45.20 ? 100 GLU D CG  1 
ATOM   4152  C  CD  . GLU D  1 127 ? 75.703  123.954 -8.702  1.00 53.32 ? 100 GLU D CD  1 
ATOM   4153  O  OE1 . GLU D  1 127 ? 75.429  124.635 -7.674  1.00 50.18 ? 100 GLU D OE1 1 
ATOM   4154  O  OE2 . GLU D  1 127 ? 76.857  123.596 -9.020  1.00 56.49 ? 100 GLU D OE2 1 
ATOM   4155  N  N   . ASP D  1 128 ? 71.306  124.233 -10.214 1.00 29.34 ? 101 ASP D N   1 
ATOM   4156  C  CA  . ASP D  1 128 ? 70.229  124.810 -9.475  1.00 29.55 ? 101 ASP D CA  1 
ATOM   4157  C  C   . ASP D  1 128 ? 70.040  124.143 -8.100  1.00 34.78 ? 101 ASP D C   1 
ATOM   4158  O  O   . ASP D  1 128 ? 70.116  122.897 -7.984  1.00 30.78 ? 101 ASP D O   1 
ATOM   4159  C  CB  . ASP D  1 128 ? 68.938  124.721 -10.265 1.00 29.37 ? 101 ASP D CB  1 
ATOM   4160  C  CG  . ASP D  1 128 ? 67.879  125.639 -9.719  1.00 32.69 ? 101 ASP D CG  1 
ATOM   4161  O  OD1 . ASP D  1 128 ? 67.976  126.870 -9.943  1.00 43.69 ? 101 ASP D OD1 1 
ATOM   4162  O  OD2 . ASP D  1 128 ? 66.939  125.174 -9.039  1.00 32.65 ? 101 ASP D OD2 1 
ATOM   4163  N  N   . SER D  1 129 ? 69.718  124.970 -7.089  1.00 34.79 ? 102 SER D N   1 
ATOM   4164  C  CA  . SER D  1 129 ? 69.645  124.526 -5.685  1.00 34.04 ? 102 SER D CA  1 
ATOM   4165  C  C   . SER D  1 129 ? 68.262  124.535 -5.187  1.00 28.35 ? 102 SER D C   1 
ATOM   4166  O  O   . SER D  1 129 ? 68.018  124.264 -4.030  1.00 31.96 ? 102 SER D O   1 
ATOM   4167  C  CB  . SER D  1 129 ? 70.465  125.479 -4.794  1.00 35.90 ? 102 SER D CB  1 
ATOM   4168  O  OG  . SER D  1 129 ? 71.829  125.131 -4.948  1.00 43.58 ? 102 SER D OG  1 
ATOM   4169  N  N   . VAL D  1 130 ? 67.324  124.908 -6.024  1.00 28.82 ? 103 VAL D N   1 
ATOM   4170  C  CA  . VAL D  1 130 ? 65.961  124.946 -5.575  1.00 24.88 ? 103 VAL D CA  1 
ATOM   4171  C  C   . VAL D  1 130 ? 65.186  123.706 -6.051  1.00 29.42 ? 103 VAL D C   1 
ATOM   4172  O  O   . VAL D  1 130 ? 64.423  123.089 -5.269  1.00 27.35 ? 103 VAL D O   1 
ATOM   4173  C  CB  . VAL D  1 130 ? 65.262  126.214 -6.024  1.00 28.66 ? 103 VAL D CB  1 
ATOM   4174  C  CG1 . VAL D  1 130 ? 63.774  126.179 -5.660  1.00 25.24 ? 103 VAL D CG1 1 
ATOM   4175  C  CG2 . VAL D  1 130 ? 65.986  127.456 -5.429  1.00 32.14 ? 103 VAL D CG2 1 
ATOM   4176  N  N   . ILE D  1 131 ? 65.328  123.366 -7.328  1.00 26.66 ? 104 ILE D N   1 
ATOM   4177  C  CA  . ILE D  1 131 ? 64.671  122.128 -7.817  1.00 27.45 ? 104 ILE D CA  1 
ATOM   4178  C  C   . ILE D  1 131 ? 65.326  120.917 -7.135  1.00 26.75 ? 104 ILE D C   1 
ATOM   4179  O  O   . ILE D  1 131 ? 66.509  120.977 -6.750  1.00 23.17 ? 104 ILE D O   1 
ATOM   4180  C  CB  . ILE D  1 131 ? 64.789  121.983 -9.367  1.00 24.03 ? 104 ILE D CB  1 
ATOM   4181  C  CG1 . ILE D  1 131 ? 66.261  122.028 -9.846  1.00 24.51 ? 104 ILE D CG1 1 
ATOM   4182  C  CG2 . ILE D  1 131 ? 63.845  122.977 -10.017 1.00 26.00 ? 104 ILE D CG2 1 
ATOM   4183  C  CD1 . ILE D  1 131 ? 66.518  121.568 -11.297 1.00 18.89 ? 104 ILE D CD1 1 
ATOM   4184  N  N   . SER D  1 132 ? 64.599  119.792 -7.069  1.00 24.46 ? 105 SER D N   1 
ATOM   4185  C  CA  . SER D  1 132 ? 65.186  118.573 -6.524  1.00 24.05 ? 105 SER D CA  1 
ATOM   4186  C  C   . SER D  1 132 ? 64.656  117.358 -7.315  1.00 23.82 ? 105 SER D C   1 
ATOM   4187  O  O   . SER D  1 132 ? 63.617  117.469 -7.942  1.00 23.15 ? 105 SER D O   1 
ATOM   4188  C  CB  . SER D  1 132 ? 64.772  118.398 -5.056  1.00 23.03 ? 105 SER D CB  1 
ATOM   4189  O  OG  . SER D  1 132 ? 65.613  117.412 -4.466  1.00 22.56 ? 105 SER D OG  1 
ATOM   4190  N  N   . LEU D  1 133 ? 65.401  116.268 -7.290  1.00 23.20 ? 106 LEU D N   1 
ATOM   4191  C  CA  . LEU D  1 133 ? 64.888  114.989 -7.814  1.00 24.12 ? 106 LEU D CA  1 
ATOM   4192  C  C   . LEU D  1 133 ? 64.323  114.034 -6.745  1.00 28.21 ? 106 LEU D C   1 
ATOM   4193  O  O   . LEU D  1 133 ? 64.101  112.852 -7.035  1.00 27.57 ? 106 LEU D O   1 
ATOM   4194  C  CB  . LEU D  1 133 ? 65.999  114.296 -8.557  1.00 21.09 ? 106 LEU D CB  1 
ATOM   4195  C  CG  . LEU D  1 133 ? 66.732  115.102 -9.619  1.00 20.61 ? 106 LEU D CG  1 
ATOM   4196  C  CD1 . LEU D  1 133 ? 67.794  114.205 -10.294 1.00 20.68 ? 106 LEU D CD1 1 
ATOM   4197  C  CD2 . LEU D  1 133 ? 65.685  115.631 -10.608 1.00 21.33 ? 106 LEU D CD2 1 
ATOM   4198  N  N   . SER D  1 134 ? 64.099  114.553 -5.541  1.00 26.45 ? 107 SER D N   1 
ATOM   4199  C  CA  . SER D  1 134 ? 63.390  113.824 -4.469  1.00 32.75 ? 107 SER D CA  1 
ATOM   4200  C  C   . SER D  1 134 ? 62.741  114.826 -3.512  1.00 31.97 ? 107 SER D C   1 
ATOM   4201  O  O   . SER D  1 134 ? 63.048  116.030 -3.583  1.00 30.24 ? 107 SER D O   1 
ATOM   4202  C  CB  . SER D  1 134 ? 64.355  112.893 -3.734  1.00 29.50 ? 107 SER D CB  1 
ATOM   4203  O  OG  . SER D  1 134 ? 65.486  113.622 -3.252  1.00 34.59 ? 107 SER D OG  1 
ATOM   4204  N  N   . GLY D  1 135 ? 61.818  114.337 -2.665  1.00 28.76 ? 108 GLY D N   1 
ATOM   4205  C  CA  . GLY D  1 135 ? 61.007  115.133 -1.728  1.00 32.80 ? 108 GLY D CA  1 
ATOM   4206  C  C   . GLY D  1 135 ? 59.987  116.086 -2.321  1.00 42.09 ? 108 GLY D C   1 
ATOM   4207  O  O   . GLY D  1 135 ? 59.504  115.883 -3.424  1.00 38.15 ? 108 GLY D O   1 
ATOM   4208  N  N   . ASP D  1 136 ? 59.693  117.185 -1.634  1.00 42.06 ? 109 ASP D N   1 
ATOM   4209  C  CA  . ASP D  1 136 ? 58.564  118.046 -2.057  1.00 43.48 ? 109 ASP D CA  1 
ATOM   4210  C  C   . ASP D  1 136 ? 58.813  119.003 -3.249  1.00 36.42 ? 109 ASP D C   1 
ATOM   4211  O  O   . ASP D  1 136 ? 57.877  119.371 -3.926  1.00 41.87 ? 109 ASP D O   1 
ATOM   4212  C  CB  . ASP D  1 136 ? 57.943  118.827 -0.863  1.00 49.22 ? 109 ASP D CB  1 
ATOM   4213  C  CG  . ASP D  1 136 ? 57.107  117.917 0.115   1.00 57.03 ? 109 ASP D CG  1 
ATOM   4214  O  OD1 . ASP D  1 136 ? 57.008  116.669 -0.074  1.00 57.52 ? 109 ASP D OD1 1 
ATOM   4215  O  OD2 . ASP D  1 136 ? 56.563  118.464 1.111   1.00 58.29 ? 109 ASP D OD2 1 
ATOM   4216  N  N   . HIS D  1 137 ? 60.047  119.431 -3.461  1.00 37.01 ? 110 HIS D N   1 
ATOM   4217  C  CA  . HIS D  1 137 ? 60.389  120.200 -4.674  1.00 40.03 ? 110 HIS D CA  1 
ATOM   4218  C  C   . HIS D  1 137 ? 60.685  119.259 -5.868  1.00 34.94 ? 110 HIS D C   1 
ATOM   4219  O  O   . HIS D  1 137 ? 61.435  119.654 -6.809  1.00 34.48 ? 110 HIS D O   1 
ATOM   4220  C  CB  . HIS D  1 137 ? 61.615  121.101 -4.390  1.00 38.49 ? 110 HIS D CB  1 
ATOM   4221  C  CG  . HIS D  1 137 ? 61.302  122.288 -3.525  1.00 45.64 ? 110 HIS D CG  1 
ATOM   4222  N  ND1 . HIS D  1 137 ? 62.243  123.248 -3.198  1.00 46.03 ? 110 HIS D ND1 1 
ATOM   4223  C  CD2 . HIS D  1 137 ? 60.144  122.683 -2.943  1.00 45.61 ? 110 HIS D CD2 1 
ATOM   4224  C  CE1 . HIS D  1 137 ? 61.684  124.165 -2.430  1.00 45.77 ? 110 HIS D CE1 1 
ATOM   4225  N  NE2 . HIS D  1 137 ? 60.408  123.856 -2.273  1.00 45.78 ? 110 HIS D NE2 1 
ATOM   4226  N  N   . CYS D  1 138 ? 60.212  118.004 -5.770  1.00 29.06 ? 111 CYS D N   1 
ATOM   4227  C  CA  . CYS D  1 138 ? 60.758  116.923 -6.630  1.00 27.77 ? 111 CYS D CA  1 
ATOM   4228  C  C   . CYS D  1 138 ? 60.135  117.174 -8.021  1.00 21.50 ? 111 CYS D C   1 
ATOM   4229  O  O   . CYS D  1 138 ? 58.952  117.483 -8.078  1.00 22.51 ? 111 CYS D O   1 
ATOM   4230  C  CB  . CYS D  1 138 ? 60.317  115.570 -6.126  1.00 29.93 ? 111 CYS D CB  1 
ATOM   4231  S  SG  . CYS D  1 138 ? 60.517  114.224 -7.312  1.00 32.68 ? 111 CYS D SG  1 
ATOM   4232  N  N   . ILE D  1 139 ? 60.935  117.107 -9.087  1.00 21.20 ? 112 ILE D N   1 
ATOM   4233  C  CA  . ILE D  1 139 ? 60.377  117.480 -10.416 1.00 21.60 ? 112 ILE D CA  1 
ATOM   4234  C  C   . ILE D  1 139 ? 60.190  116.257 -11.335 1.00 22.44 ? 112 ILE D C   1 
ATOM   4235  O  O   . ILE D  1 139 ? 59.730  116.391 -12.455 1.00 20.58 ? 112 ILE D O   1 
ATOM   4236  C  CB  . ILE D  1 139 ? 61.263  118.539 -11.145 1.00 21.11 ? 112 ILE D CB  1 
ATOM   4237  C  CG1 . ILE D  1 139 ? 62.676  118.032 -11.304 1.00 21.12 ? 112 ILE D CG1 1 
ATOM   4238  C  CG2 . ILE D  1 139 ? 61.195  119.867 -10.352 1.00 22.00 ? 112 ILE D CG2 1 
ATOM   4239  C  CD1 . ILE D  1 139 ? 63.561  118.833 -12.228 1.00 22.23 ? 112 ILE D CD1 1 
ATOM   4240  N  N   . ILE D  1 140 ? 60.564  115.076 -10.863 1.00 20.49 ? 113 ILE D N   1 
ATOM   4241  C  CA  . ILE D  1 140 ? 60.282  113.822 -11.635 1.00 21.65 ? 113 ILE D CA  1 
ATOM   4242  C  C   . ILE D  1 140 ? 58.780  113.715 -11.884 1.00 19.28 ? 113 ILE D C   1 
ATOM   4243  O  O   . ILE D  1 140 ? 57.998  113.962 -11.009 1.00 17.37 ? 113 ILE D O   1 
ATOM   4244  C  CB  . ILE D  1 140 ? 60.722  112.594 -10.788 1.00 23.67 ? 113 ILE D CB  1 
ATOM   4245  C  CG1 . ILE D  1 140 ? 62.158  112.782 -10.349 1.00 27.42 ? 113 ILE D CG1 1 
ATOM   4246  C  CG2 . ILE D  1 140 ? 60.535  111.260 -11.556 1.00 22.40 ? 113 ILE D CG2 1 
ATOM   4247  C  CD1 . ILE D  1 140 ? 63.150  112.518 -11.413 1.00 28.14 ? 113 ILE D CD1 1 
ATOM   4248  N  N   . GLY D  1 141 ? 58.369  113.394 -13.108 1.00 18.34 ? 114 GLY D N   1 
ATOM   4249  C  CA  . GLY D  1 141 ? 56.941  113.260 -13.393 1.00 16.45 ? 114 GLY D CA  1 
ATOM   4250  C  C   . GLY D  1 141 ? 56.257  114.537 -13.812 1.00 16.48 ? 114 GLY D C   1 
ATOM   4251  O  O   . GLY D  1 141 ? 55.058  114.540 -14.103 1.00 16.99 ? 114 GLY D O   1 
ATOM   4252  N  N   . ARG D  1 142 ? 57.000  115.632 -13.797 1.00 18.29 ? 115 ARG D N   1 
ATOM   4253  C  CA  . ARG D  1 142 ? 56.441  116.932 -14.200 1.00 18.42 ? 115 ARG D CA  1 
ATOM   4254  C  C   . ARG D  1 142 ? 56.973  117.196 -15.603 1.00 18.47 ? 115 ARG D C   1 
ATOM   4255  O  O   . ARG D  1 142 ? 57.681  116.361 -16.149 1.00 18.88 ? 115 ARG D O   1 
ATOM   4256  C  CB  . ARG D  1 142 ? 56.894  118.004 -13.167 1.00 18.72 ? 115 ARG D CB  1 
ATOM   4257  C  CG  . ARG D  1 142 ? 56.491  117.521 -11.757 1.00 19.68 ? 115 ARG D CG  1 
ATOM   4258  C  CD  . ARG D  1 142 ? 56.389  118.633 -10.729 1.00 23.15 ? 115 ARG D CD  1 
ATOM   4259  N  NE  . ARG D  1 142 ? 55.955  118.094 -9.406  1.00 23.88 ? 115 ARG D NE  1 
ATOM   4260  C  CZ  . ARG D  1 142 ? 54.701  118.002 -8.964  1.00 24.21 ? 115 ARG D CZ  1 
ATOM   4261  N  NH1 . ARG D  1 142 ? 53.660  118.378 -9.674  1.00 22.56 ? 115 ARG D NH1 1 
ATOM   4262  N  NH2 . ARG D  1 142 ? 54.491  117.526 -7.735  1.00 25.20 ? 115 ARG D NH2 1 
ATOM   4263  N  N   . THR D  1 143 ? 56.627  118.335 -16.175 1.00 18.83 ? 116 THR D N   1 
ATOM   4264  C  CA  . THR D  1 143 ? 56.958  118.613 -17.575 1.00 19.23 ? 116 THR D CA  1 
ATOM   4265  C  C   . THR D  1 143 ? 57.950  119.770 -17.720 1.00 18.40 ? 116 THR D C   1 
ATOM   4266  O  O   . THR D  1 143 ? 57.764  120.779 -17.050 1.00 22.25 ? 116 THR D O   1 
ATOM   4267  C  CB  . THR D  1 143 ? 55.699  118.978 -18.344 1.00 19.41 ? 116 THR D CB  1 
ATOM   4268  O  OG1 . THR D  1 143 ? 54.838  117.842 -18.434 1.00 20.99 ? 116 THR D OG1 1 
ATOM   4269  C  CG2 . THR D  1 143 ? 56.050  119.432 -19.794 1.00 19.01 ? 116 THR D CG2 1 
ATOM   4270  N  N   . LEU D  1 144 ? 59.033  119.573 -18.503 1.00 17.67 ? 117 LEU D N   1 
ATOM   4271  C  CA  . LEU D  1 144 ? 59.981  120.665 -18.777 1.00 18.33 ? 117 LEU D CA  1 
ATOM   4272  C  C   . LEU D  1 144 ? 59.503  121.288 -20.088 1.00 19.77 ? 117 LEU D C   1 
ATOM   4273  O  O   . LEU D  1 144 ? 59.135  120.531 -21.007 1.00 16.51 ? 117 LEU D O   1 
ATOM   4274  C  CB  . LEU D  1 144 ? 61.377  120.112 -18.943 1.00 18.08 ? 117 LEU D CB  1 
ATOM   4275  C  CG  . LEU D  1 144 ? 62.486  121.096 -19.249 1.00 17.13 ? 117 LEU D CG  1 
ATOM   4276  C  CD1 . LEU D  1 144 ? 62.632  122.025 -18.014 1.00 19.95 ? 117 LEU D CD1 1 
ATOM   4277  C  CD2 . LEU D  1 144 ? 63.767  120.304 -19.494 1.00 17.78 ? 117 LEU D CD2 1 
ATOM   4278  N  N   . VAL D  1 145 ? 59.454  122.625 -20.151 1.00 18.82 ? 118 VAL D N   1 
ATOM   4279  C  CA  . VAL D  1 145 ? 58.894  123.341 -21.355 1.00 19.58 ? 118 VAL D CA  1 
ATOM   4280  C  C   . VAL D  1 145 ? 59.909  124.406 -21.773 1.00 22.97 ? 118 VAL D C   1 
ATOM   4281  O  O   . VAL D  1 145 ? 60.438  125.151 -20.911 1.00 21.04 ? 118 VAL D O   1 
ATOM   4282  C  CB  . VAL D  1 145 ? 57.578  124.040 -21.004 1.00 18.28 ? 118 VAL D CB  1 
ATOM   4283  C  CG1 . VAL D  1 145 ? 56.998  124.843 -22.207 1.00 18.98 ? 118 VAL D CG1 1 
ATOM   4284  C  CG2 . VAL D  1 145 ? 56.553  123.033 -20.498 1.00 18.02 ? 118 VAL D CG2 1 
ATOM   4285  N  N   . VAL D  1 146 ? 60.221  124.464 -23.069 1.00 21.65 ? 119 VAL D N   1 
ATOM   4286  C  CA  . VAL D  1 146 ? 60.984  125.602 -23.600 1.00 20.99 ? 119 VAL D CA  1 
ATOM   4287  C  C   . VAL D  1 146 ? 59.991  126.514 -24.340 1.00 22.83 ? 119 VAL D C   1 
ATOM   4288  O  O   . VAL D  1 146 ? 59.101  126.035 -25.057 1.00 19.53 ? 119 VAL D O   1 
ATOM   4289  C  CB  . VAL D  1 146 ? 62.183  125.151 -24.412 1.00 21.56 ? 119 VAL D CB  1 
ATOM   4290  C  CG1 . VAL D  1 146 ? 61.745  124.274 -25.585 1.00 22.26 ? 119 VAL D CG1 1 
ATOM   4291  C  CG2 . VAL D  1 146 ? 63.044  126.338 -24.904 1.00 22.38 ? 119 VAL D CG2 1 
ATOM   4292  N  N   . HIS D  1 147 ? 60.094  127.825 -24.114 1.00 19.82 ? 120 HIS D N   1 
ATOM   4293  C  CA  . HIS D  1 147 ? 59.055  128.755 -24.522 1.00 21.05 ? 120 HIS D CA  1 
ATOM   4294  C  C   . HIS D  1 147 ? 59.483  129.608 -25.709 1.00 20.45 ? 120 HIS D C   1 
ATOM   4295  O  O   . HIS D  1 147 ? 60.651  129.651 -26.058 1.00 22.29 ? 120 HIS D O   1 
ATOM   4296  C  CB  . HIS D  1 147 ? 58.691  129.713 -23.394 1.00 21.12 ? 120 HIS D CB  1 
ATOM   4297  C  CG  . HIS D  1 147 ? 57.878  129.082 -22.334 1.00 22.89 ? 120 HIS D CG  1 
ATOM   4298  N  ND1 . HIS D  1 147 ? 56.523  129.256 -22.249 1.00 23.90 ? 120 HIS D ND1 1 
ATOM   4299  C  CD2 . HIS D  1 147 ? 58.222  128.228 -21.338 1.00 22.05 ? 120 HIS D CD2 1 
ATOM   4300  C  CE1 . HIS D  1 147 ? 56.059  128.562 -21.224 1.00 23.36 ? 120 HIS D CE1 1 
ATOM   4301  N  NE2 . HIS D  1 147 ? 57.074  127.941 -20.652 1.00 21.63 ? 120 HIS D NE2 1 
ATOM   4302  N  N   . GLU D  1 148 ? 58.505  130.317 -26.262 1.00 25.05 ? 121 GLU D N   1 
ATOM   4303  C  CA  . GLU D  1 148 ? 58.689  131.055 -27.534 1.00 27.08 ? 121 GLU D CA  1 
ATOM   4304  C  C   . GLU D  1 148 ? 59.601  132.297 -27.365 1.00 25.96 ? 121 GLU D C   1 
ATOM   4305  O  O   . GLU D  1 148 ? 60.488  132.561 -28.194 1.00 28.71 ? 121 GLU D O   1 
ATOM   4306  C  CB  . GLU D  1 148 ? 57.287  131.448 -28.016 1.00 31.76 ? 121 GLU D CB  1 
ATOM   4307  C  CG  . GLU D  1 148 ? 57.223  132.526 -29.101 1.00 38.25 ? 121 GLU D CG  1 
ATOM   4308  C  CD  . GLU D  1 148 ? 55.836  133.193 -29.180 1.00 44.41 ? 121 GLU D CD  1 
ATOM   4309  O  OE1 . GLU D  1 148 ? 55.514  133.665 -30.288 1.00 52.95 ? 121 GLU D OE1 1 
ATOM   4310  O  OE2 . GLU D  1 148 ? 55.073  133.280 -28.158 1.00 37.83 ? 121 GLU D OE2 1 
ATOM   4311  N  N   . LYS D  1 149 ? 59.431  132.988 -26.241 1.00 26.87 ? 122 LYS D N   1 
ATOM   4312  C  CA  . LYS D  1 149 ? 60.123  134.266 -25.991 1.00 32.14 ? 122 LYS D CA  1 
ATOM   4313  C  C   . LYS D  1 149 ? 61.011  134.208 -24.736 1.00 32.62 ? 122 LYS D C   1 
ATOM   4314  O  O   . LYS D  1 149 ? 60.994  133.209 -23.977 1.00 27.02 ? 122 LYS D O   1 
ATOM   4315  C  CB  . LYS D  1 149 ? 59.067  135.339 -25.760 1.00 31.54 ? 122 LYS D CB  1 
ATOM   4316  C  CG  . LYS D  1 149 ? 58.159  135.562 -26.937 1.00 39.02 ? 122 LYS D CG  1 
ATOM   4317  C  CD  . LYS D  1 149 ? 57.137  136.604 -26.565 1.00 45.17 ? 122 LYS D CD  1 
ATOM   4318  C  CE  . LYS D  1 149 ? 56.272  136.916 -27.768 1.00 54.96 ? 122 LYS D CE  1 
ATOM   4319  N  NZ  . LYS D  1 149 ? 54.986  137.494 -27.285 1.00 66.25 ? 122 LYS D NZ  1 
ATOM   4320  N  N   . ALA D  1 150 ? 61.753  135.294 -24.515 1.00 29.13 ? 123 ALA D N   1 
ATOM   4321  C  CA  . ALA D  1 150 ? 62.565  135.469 -23.306 1.00 30.56 ? 123 ALA D CA  1 
ATOM   4322  C  C   . ALA D  1 150 ? 61.682  135.564 -22.077 1.00 31.13 ? 123 ALA D C   1 
ATOM   4323  O  O   . ALA D  1 150 ? 60.569  136.098 -22.109 1.00 28.53 ? 123 ALA D O   1 
ATOM   4324  C  CB  . ALA D  1 150 ? 63.476  136.716 -23.446 1.00 32.08 ? 123 ALA D CB  1 
ATOM   4325  N  N   . ASP D  1 151 ? 62.181  135.015 -20.968 1.00 30.81 ? 124 ASP D N   1 
ATOM   4326  C  CA  . ASP D  1 151 ? 61.489  135.097 -19.719 1.00 30.87 ? 124 ASP D CA  1 
ATOM   4327  C  C   . ASP D  1 151 ? 61.977  136.461 -19.170 1.00 31.04 ? 124 ASP D C   1 
ATOM   4328  O  O   . ASP D  1 151 ? 63.161  136.688 -19.157 1.00 30.10 ? 124 ASP D O   1 
ATOM   4329  C  CB  . ASP D  1 151 ? 62.014  133.981 -18.831 1.00 33.27 ? 124 ASP D CB  1 
ATOM   4330  C  CG  . ASP D  1 151 ? 61.326  133.889 -17.479 1.00 39.62 ? 124 ASP D CG  1 
ATOM   4331  O  OD1 . ASP D  1 151 ? 60.634  134.847 -17.018 1.00 36.72 ? 124 ASP D OD1 1 
ATOM   4332  O  OD2 . ASP D  1 151 ? 61.480  132.777 -16.870 1.00 34.02 ? 124 ASP D OD2 1 
ATOM   4333  N  N   . ASP D  1 152 ? 61.088  137.331 -18.732 1.00 31.54 ? 125 ASP D N   1 
ATOM   4334  C  CA  . ASP D  1 152 ? 61.591  138.647 -18.242 1.00 38.46 ? 125 ASP D CA  1 
ATOM   4335  C  C   . ASP D  1 152 ? 62.056  138.574 -16.758 1.00 44.02 ? 125 ASP D C   1 
ATOM   4336  O  O   . ASP D  1 152 ? 62.380  139.596 -16.122 1.00 38.40 ? 125 ASP D O   1 
ATOM   4337  C  CB  . ASP D  1 152 ? 60.576  139.767 -18.505 1.00 37.98 ? 125 ASP D CB  1 
ATOM   4338  C  CG  . ASP D  1 152 ? 59.268  139.566 -17.797 1.00 40.69 ? 125 ASP D CG  1 
ATOM   4339  O  OD1 . ASP D  1 152 ? 59.211  138.902 -16.733 1.00 40.58 ? 125 ASP D OD1 1 
ATOM   4340  O  OD2 . ASP D  1 152 ? 58.262  140.086 -18.311 1.00 41.99 ? 125 ASP D OD2 1 
ATOM   4341  N  N   . LEU D  1 153 ? 62.063  137.336 -16.236 1.00 38.18 ? 126 LEU D N   1 
ATOM   4342  C  CA  . LEU D  1 153 ? 62.530  136.983 -14.904 1.00 37.34 ? 126 LEU D CA  1 
ATOM   4343  C  C   . LEU D  1 153 ? 61.686  137.610 -13.814 1.00 37.92 ? 126 LEU D C   1 
ATOM   4344  O  O   . LEU D  1 153 ? 62.160  137.812 -12.696 1.00 41.45 ? 126 LEU D O   1 
ATOM   4345  C  CB  . LEU D  1 153 ? 64.035  137.245 -14.739 1.00 35.69 ? 126 LEU D CB  1 
ATOM   4346  C  CG  . LEU D  1 153 ? 64.925  136.611 -15.822 1.00 38.85 ? 126 LEU D CG  1 
ATOM   4347  C  CD1 . LEU D  1 153 ? 66.384  136.978 -15.587 1.00 41.23 ? 126 LEU D CD1 1 
ATOM   4348  C  CD2 . LEU D  1 153 ? 64.758  135.104 -15.897 1.00 36.78 ? 126 LEU D CD2 1 
ATOM   4349  N  N   . GLY D  1 154 ? 60.426  137.908 -14.140 1.00 34.12 ? 127 GLY D N   1 
ATOM   4350  C  CA  . GLY D  1 154 ? 59.467  138.405 -13.173 1.00 35.41 ? 127 GLY D CA  1 
ATOM   4351  C  C   . GLY D  1 154 ? 59.493  139.931 -12.952 1.00 41.80 ? 127 GLY D C   1 
ATOM   4352  O  O   . GLY D  1 154 ? 58.650  140.458 -12.226 1.00 43.01 ? 127 GLY D O   1 
ATOM   4353  N  N   . LYS D  1 155 ? 60.438  140.619 -13.599 1.00 44.17 ? 128 LYS D N   1 
ATOM   4354  C  CA  . LYS D  1 155 ? 60.653  142.083 -13.447 1.00 45.78 ? 128 LYS D CA  1 
ATOM   4355  C  C   . LYS D  1 155 ? 60.119  142.885 -14.625 1.00 48.95 ? 128 LYS D C   1 
ATOM   4356  O  O   . LYS D  1 155 ? 60.690  143.914 -14.969 1.00 55.55 ? 128 LYS D O   1 
ATOM   4357  C  CB  . LYS D  1 155 ? 62.142  142.388 -13.387 1.00 49.13 ? 128 LYS D CB  1 
ATOM   4358  C  CG  . LYS D  1 155 ? 62.997  141.559 -12.447 1.00 52.76 ? 128 LYS D CG  1 
ATOM   4359  C  CD  . LYS D  1 155 ? 64.394  141.565 -13.056 1.00 65.75 ? 128 LYS D CD  1 
ATOM   4360  C  CE  . LYS D  1 155 ? 65.536  141.588 -12.037 1.00 79.03 ? 128 LYS D CE  1 
ATOM   4361  N  NZ  . LYS D  1 155 ? 65.769  142.924 -11.407 1.00 79.24 ? 128 LYS D NZ  1 
ATOM   4362  N  N   . GLY D  1 156 ? 59.047  142.434 -15.260 1.00 49.31 ? 129 GLY D N   1 
ATOM   4363  C  CA  . GLY D  1 156 ? 58.534  143.124 -16.442 1.00 52.62 ? 129 GLY D CA  1 
ATOM   4364  C  C   . GLY D  1 156 ? 57.448  144.142 -16.148 1.00 57.14 ? 129 GLY D C   1 
ATOM   4365  O  O   . GLY D  1 156 ? 56.847  144.697 -17.064 1.00 62.52 ? 129 GLY D O   1 
ATOM   4366  N  N   . GLY D  1 157 ? 57.172  144.378 -14.873 1.00 57.89 ? 130 GLY D N   1 
ATOM   4367  C  CA  . GLY D  1 157 ? 56.249  145.442 -14.488 1.00 57.11 ? 130 GLY D CA  1 
ATOM   4368  C  C   . GLY D  1 157 ? 54.785  145.320 -14.892 1.00 60.10 ? 130 GLY D C   1 
ATOM   4369  O  O   . GLY D  1 157 ? 54.061  146.317 -14.904 1.00 60.75 ? 130 GLY D O   1 
ATOM   4370  N  N   . ASN D  1 158 ? 54.331  144.121 -15.236 1.00 55.11 ? 131 ASN D N   1 
ATOM   4371  C  CA  . ASN D  1 158 ? 52.886  143.881 -15.356 1.00 52.96 ? 131 ASN D CA  1 
ATOM   4372  C  C   . ASN D  1 158 ? 52.537  142.544 -14.689 1.00 53.91 ? 131 ASN D C   1 
ATOM   4373  O  O   . ASN D  1 158 ? 53.443  141.791 -14.288 1.00 54.90 ? 131 ASN D O   1 
ATOM   4374  C  CB  . ASN D  1 158 ? 52.480  143.832 -16.821 1.00 52.68 ? 131 ASN D CB  1 
ATOM   4375  C  CG  . ASN D  1 158 ? 52.719  142.461 -17.422 1.00 58.18 ? 131 ASN D CG  1 
ATOM   4376  O  OD1 . ASN D  1 158 ? 53.853  141.944 -17.399 1.00 43.97 ? 131 ASN D OD1 1 
ATOM   4377  N  ND2 . ASN D  1 158 ? 51.633  141.824 -17.896 1.00 59.85 ? 131 ASN D ND2 1 
ATOM   4378  N  N   . GLU D  1 159 ? 51.245  142.229 -14.631 1.00 48.05 ? 132 GLU D N   1 
ATOM   4379  C  CA  . GLU D  1 159 ? 50.767  141.070 -13.912 1.00 52.25 ? 132 GLU D CA  1 
ATOM   4380  C  C   . GLU D  1 159 ? 51.245  139.732 -14.522 1.00 52.65 ? 132 GLU D C   1 
ATOM   4381  O  O   . GLU D  1 159 ? 51.622  138.791 -13.795 1.00 51.57 ? 132 GLU D O   1 
ATOM   4382  C  CB  . GLU D  1 159 ? 49.251  141.117 -13.837 1.00 56.92 ? 132 GLU D CB  1 
ATOM   4383  C  CG  . GLU D  1 159 ? 48.696  140.313 -12.669 1.00 68.74 ? 132 GLU D CG  1 
ATOM   4384  C  CD  . GLU D  1 159 ? 47.232  139.914 -12.850 1.00 79.63 ? 132 GLU D CD  1 
ATOM   4385  O  OE1 . GLU D  1 159 ? 46.456  140.671 -13.495 1.00 80.22 ? 132 GLU D OE1 1 
ATOM   4386  O  OE2 . GLU D  1 159 ? 46.851  138.830 -12.341 1.00 80.26 ? 132 GLU D OE2 1 
ATOM   4387  N  N   . GLU D  1 160 ? 51.259  139.672 -15.849 1.00 47.31 ? 133 GLU D N   1 
ATOM   4388  C  CA  . GLU D  1 160 ? 51.706  138.485 -16.564 1.00 46.07 ? 133 GLU D CA  1 
ATOM   4389  C  C   . GLU D  1 160 ? 53.168  138.182 -16.281 1.00 46.09 ? 133 GLU D C   1 
ATOM   4390  O  O   . GLU D  1 160 ? 53.588  137.013 -16.340 1.00 45.61 ? 133 GLU D O   1 
ATOM   4391  C  CB  . GLU D  1 160 ? 51.441  138.627 -18.072 1.00 51.68 ? 133 GLU D CB  1 
ATOM   4392  C  CG  . GLU D  1 160 ? 51.382  137.312 -18.854 1.00 54.25 ? 133 GLU D CG  1 
ATOM   4393  C  CD  . GLU D  1 160 ? 50.386  136.313 -18.268 1.00 61.59 ? 133 GLU D CD  1 
ATOM   4394  O  OE1 . GLU D  1 160 ? 49.179  136.639 -18.163 1.00 61.20 ? 133 GLU D OE1 1 
ATOM   4395  O  OE2 . GLU D  1 160 ? 50.811  135.193 -17.900 1.00 60.28 ? 133 GLU D OE2 1 
ATOM   4396  N  N   . SER D  1 161 ? 53.948  139.214 -15.961 1.00 37.05 ? 134 SER D N   1 
ATOM   4397  C  CA  . SER D  1 161 ? 55.371  139.036 -15.719 1.00 41.00 ? 134 SER D CA  1 
ATOM   4398  C  C   . SER D  1 161 ? 55.572  138.189 -14.464 1.00 42.96 ? 134 SER D C   1 
ATOM   4399  O  O   . SER D  1 161 ? 56.530  137.391 -14.371 1.00 39.33 ? 134 SER D O   1 
ATOM   4400  C  CB  . SER D  1 161 ? 56.077  140.370 -15.543 1.00 38.06 ? 134 SER D CB  1 
ATOM   4401  O  OG  . SER D  1 161 ? 57.433  140.153 -15.156 1.00 43.82 ? 134 SER D OG  1 
ATOM   4402  N  N   . THR D  1 162 ? 54.659  138.368 -13.520 1.00 41.50 ? 135 THR D N   1 
ATOM   4403  C  CA  . THR D  1 162 ? 54.792  137.755 -12.202 1.00 43.40 ? 135 THR D CA  1 
ATOM   4404  C  C   . THR D  1 162 ? 54.119  136.371 -12.182 1.00 46.39 ? 135 THR D C   1 
ATOM   4405  O  O   . THR D  1 162 ? 54.138  135.690 -11.140 1.00 48.52 ? 135 THR D O   1 
ATOM   4406  C  CB  . THR D  1 162 ? 54.091  138.599 -11.119 1.00 44.93 ? 135 THR D CB  1 
ATOM   4407  O  OG1 . THR D  1 162 ? 52.680  138.580 -11.388 1.00 44.56 ? 135 THR D OG1 1 
ATOM   4408  C  CG2 . THR D  1 162 ? 54.630  140.070 -11.079 1.00 41.53 ? 135 THR D CG2 1 
ATOM   4409  N  N   . LYS D  1 163 ? 53.481  135.978 -13.294 1.00 43.16 ? 136 LYS D N   1 
ATOM   4410  C  CA  . LYS D  1 163 ? 52.951  134.615 -13.412 1.00 45.20 ? 136 LYS D CA  1 
ATOM   4411  C  C   . LYS D  1 163 ? 53.806  133.744 -14.340 1.00 42.62 ? 136 LYS D C   1 
ATOM   4412  O  O   . LYS D  1 163 ? 54.150  132.609 -13.975 1.00 38.19 ? 136 LYS D O   1 
ATOM   4413  C  CB  . LYS D  1 163 ? 51.471  134.601 -13.802 1.00 45.26 ? 136 LYS D CB  1 
ATOM   4414  C  CG  . LYS D  1 163 ? 50.592  135.128 -12.676 1.00 53.23 ? 136 LYS D CG  1 
ATOM   4415  C  CD  . LYS D  1 163 ? 49.121  134.756 -12.830 1.00 55.16 ? 136 LYS D CD  1 
ATOM   4416  C  CE  . LYS D  1 163 ? 48.543  135.246 -14.144 1.00 58.87 ? 136 LYS D CE  1 
ATOM   4417  N  NZ  . LYS D  1 163 ? 48.631  136.724 -14.343 1.00 66.38 ? 136 LYS D NZ  1 
ATOM   4418  N  N   . THR D  1 164 ? 54.169  134.284 -15.503 1.00 38.16 ? 137 THR D N   1 
ATOM   4419  C  CA  . THR D  1 164 ? 54.830  133.509 -16.541 1.00 35.38 ? 137 THR D CA  1 
ATOM   4420  C  C   . THR D  1 164 ? 56.105  134.131 -17.020 1.00 36.80 ? 137 THR D C   1 
ATOM   4421  O  O   . THR D  1 164 ? 56.844  133.531 -17.835 1.00 35.44 ? 137 THR D O   1 
ATOM   4422  C  CB  . THR D  1 164 ? 53.936  133.354 -17.792 1.00 40.90 ? 137 THR D CB  1 
ATOM   4423  O  OG1 . THR D  1 164 ? 53.734  134.646 -18.409 1.00 40.43 ? 137 THR D OG1 1 
ATOM   4424  C  CG2 . THR D  1 164 ? 52.601  132.707 -17.445 1.00 40.24 ? 137 THR D CG2 1 
ATOM   4425  N  N   . GLY D  1 165 ? 56.392  135.349 -16.566 1.00 31.64 ? 138 GLY D N   1 
ATOM   4426  C  CA  . GLY D  1 165 ? 57.552  136.029 -17.121 1.00 27.87 ? 138 GLY D CA  1 
ATOM   4427  C  C   . GLY D  1 165 ? 57.362  136.501 -18.573 1.00 29.05 ? 138 GLY D C   1 
ATOM   4428  O  O   . GLY D  1 165 ? 58.338  136.907 -19.240 1.00 30.78 ? 138 GLY D O   1 
ATOM   4429  N  N   . ASN D  1 166 ? 56.121  136.471 -19.054 1.00 30.47 ? 139 ASN D N   1 
ATOM   4430  C  CA  . ASN D  1 166 ? 55.802  136.834 -20.449 1.00 35.14 ? 139 ASN D CA  1 
ATOM   4431  C  C   . ASN D  1 166 ? 56.628  136.025 -21.474 1.00 33.67 ? 139 ASN D C   1 
ATOM   4432  O  O   . ASN D  1 166 ? 57.010  136.554 -22.505 1.00 29.77 ? 139 ASN D O   1 
ATOM   4433  C  CB  . ASN D  1 166 ? 56.010  138.353 -20.712 1.00 37.49 ? 139 ASN D CB  1 
ATOM   4434  C  CG  . ASN D  1 166 ? 55.060  139.210 -19.902 1.00 40.55 ? 139 ASN D CG  1 
ATOM   4435  O  OD1 . ASN D  1 166 ? 53.847  139.158 -20.097 1.00 41.46 ? 139 ASN D OD1 1 
ATOM   4436  N  ND2 . ASN D  1 166 ? 55.610  139.976 -18.952 1.00 37.70 ? 139 ASN D ND2 1 
ATOM   4437  N  N   . ALA D  1 167 ? 56.913  134.743 -21.200 1.00 29.59 ? 140 ALA D N   1 
ATOM   4438  C  CA  . ALA D  1 167 ? 57.778  133.977 -22.113 1.00 30.31 ? 140 ALA D CA  1 
ATOM   4439  C  C   . ALA D  1 167 ? 56.973  133.380 -23.282 1.00 27.66 ? 140 ALA D C   1 
ATOM   4440  O  O   . ALA D  1 167 ? 57.554  132.722 -24.167 1.00 29.59 ? 140 ALA D O   1 
ATOM   4441  C  CB  . ALA D  1 167 ? 58.575  132.889 -21.373 1.00 27.34 ? 140 ALA D CB  1 
ATOM   4442  N  N   . GLY D  1 168 ? 55.657  133.582 -23.266 1.00 31.31 ? 141 GLY D N   1 
ATOM   4443  C  CA  . GLY D  1 168 ? 54.800  133.251 -24.437 1.00 33.70 ? 141 GLY D CA  1 
ATOM   4444  C  C   . GLY D  1 168 ? 54.515  131.751 -24.625 1.00 37.05 ? 141 GLY D C   1 
ATOM   4445  O  O   . GLY D  1 168 ? 54.495  130.995 -23.626 1.00 33.53 ? 141 GLY D O   1 
ATOM   4446  N  N   . SER D  1 169 ? 54.295  131.320 -25.883 1.00 30.81 ? 142 SER D N   1 
ATOM   4447  C  CA  . SER D  1 169 ? 53.756  129.981 -26.158 1.00 29.08 ? 142 SER D CA  1 
ATOM   4448  C  C   . SER D  1 169 ? 54.795  128.894 -25.873 1.00 26.17 ? 142 SER D C   1 
ATOM   4449  O  O   . SER D  1 169 ? 56.000  129.171 -25.737 1.00 26.14 ? 142 SER D O   1 
ATOM   4450  C  CB  . SER D  1 169 ? 53.284  129.866 -27.601 1.00 31.68 ? 142 SER D CB  1 
ATOM   4451  O  OG  . SER D  1 169 ? 54.412  129.890 -28.437 1.00 36.16 ? 142 SER D OG  1 
ATOM   4452  N  N   . ARG D  1 170 ? 54.306  127.653 -25.792 1.00 24.35 ? 143 ARG D N   1 
ATOM   4453  C  CA  . ARG D  1 170 ? 55.159  126.517 -25.451 1.00 23.83 ? 143 ARG D CA  1 
ATOM   4454  C  C   . ARG D  1 170 ? 55.629  125.870 -26.742 1.00 21.17 ? 143 ARG D C   1 
ATOM   4455  O  O   . ARG D  1 170 ? 54.821  125.335 -27.482 1.00 25.69 ? 143 ARG D O   1 
ATOM   4456  C  CB  . ARG D  1 170 ? 54.321  125.587 -24.601 1.00 23.55 ? 143 ARG D CB  1 
ATOM   4457  C  CG  . ARG D  1 170 ? 53.819  126.355 -23.362 1.00 25.19 ? 143 ARG D CG  1 
ATOM   4458  C  CD  . ARG D  1 170 ? 52.816  125.574 -22.531 1.00 27.60 ? 143 ARG D CD  1 
ATOM   4459  N  NE  . ARG D  1 170 ? 52.309  126.383 -21.421 1.00 26.80 ? 143 ARG D NE  1 
ATOM   4460  C  CZ  . ARG D  1 170 ? 51.711  125.917 -20.321 1.00 28.92 ? 143 ARG D CZ  1 
ATOM   4461  N  NH1 . ARG D  1 170 ? 51.499  124.595 -20.118 1.00 23.07 ? 143 ARG D NH1 1 
ATOM   4462  N  NH2 . ARG D  1 170 ? 51.288  126.791 -19.403 1.00 25.30 ? 143 ARG D NH2 1 
ATOM   4463  N  N   . LEU D  1 171 ? 56.912  125.910 -27.017 1.00 21.52 ? 144 LEU D N   1 
ATOM   4464  C  CA  . LEU D  1 171 ? 57.432  125.354 -28.251 1.00 22.37 ? 144 LEU D CA  1 
ATOM   4465  C  C   . LEU D  1 171 ? 57.676  123.845 -28.197 1.00 23.23 ? 144 LEU D C   1 
ATOM   4466  O  O   . LEU D  1 171 ? 57.490  123.164 -29.201 1.00 22.35 ? 144 LEU D O   1 
ATOM   4467  C  CB  . LEU D  1 171 ? 58.738  126.010 -28.626 1.00 24.11 ? 144 LEU D CB  1 
ATOM   4468  C  CG  . LEU D  1 171 ? 58.691  127.557 -28.821 1.00 26.45 ? 144 LEU D CG  1 
ATOM   4469  C  CD1 . LEU D  1 171 ? 60.054  127.950 -29.349 1.00 28.36 ? 144 LEU D CD1 1 
ATOM   4470  C  CD2 . LEU D  1 171 ? 57.574  128.001 -29.749 1.00 26.69 ? 144 LEU D CD2 1 
ATOM   4471  N  N   . ALA D  1 172 ? 58.208  123.341 -27.070 1.00 20.17 ? 145 ALA D N   1 
ATOM   4472  C  CA  . ALA D  1 172 ? 58.421  121.903 -26.968 1.00 17.70 ? 145 ALA D CA  1 
ATOM   4473  C  C   . ALA D  1 172 ? 58.435  121.520 -25.500 1.00 19.08 ? 145 ALA D C   1 
ATOM   4474  O  O   . ALA D  1 172 ? 58.640  122.399 -24.632 1.00 17.81 ? 145 ALA D O   1 
ATOM   4475  C  CB  . ALA D  1 172 ? 59.734  121.484 -27.605 1.00 16.85 ? 145 ALA D CB  1 
ATOM   4476  N  N   . CYS D  1 173 ? 58.180  120.239 -25.222 1.00 17.47 ? 146 CYS D N   1 
ATOM   4477  C  CA  . CYS D  1 173 ? 58.110  119.837 -23.780 1.00 18.29 ? 146 CYS D CA  1 
ATOM   4478  C  C   . CYS D  1 173 ? 58.293  118.351 -23.694 1.00 18.70 ? 146 CYS D C   1 
ATOM   4479  O  O   . CYS D  1 173 ? 58.217  117.656 -24.731 1.00 15.57 ? 146 CYS D O   1 
ATOM   4480  C  CB  . CYS D  1 173 ? 56.752  120.192 -23.175 1.00 21.71 ? 146 CYS D CB  1 
ATOM   4481  S  SG  . CYS D  1 173 ? 55.323  119.495 -24.004 1.00 26.42 ? 146 CYS D SG  1 
ATOM   4482  N  N   . GLY D  1 174 ? 58.470  117.854 -22.469 1.00 15.69 ? 147 GLY D N   1 
ATOM   4483  C  CA  . GLY D  1 174 ? 58.475  116.396 -22.281 1.00 18.69 ? 147 GLY D CA  1 
ATOM   4484  C  C   . GLY D  1 174 ? 58.334  116.159 -20.799 1.00 17.66 ? 147 GLY D C   1 
ATOM   4485  O  O   . GLY D  1 174 ? 58.584  117.085 -19.979 1.00 17.19 ? 147 GLY D O   1 
ATOM   4486  N  N   . VAL D  1 175 ? 58.023  114.908 -20.441 1.00 16.76 ? 148 VAL D N   1 
ATOM   4487  C  CA  . VAL D  1 175 ? 57.888  114.571 -19.003 1.00 17.02 ? 148 VAL D CA  1 
ATOM   4488  C  C   . VAL D  1 175 ? 59.279  114.254 -18.496 1.00 16.50 ? 148 VAL D C   1 
ATOM   4489  O  O   . VAL D  1 175 ? 60.043  113.554 -19.174 1.00 17.60 ? 148 VAL D O   1 
ATOM   4490  C  CB  . VAL D  1 175 ? 56.961  113.321 -18.847 1.00 18.41 ? 148 VAL D CB  1 
ATOM   4491  C  CG1 . VAL D  1 175 ? 56.726  112.947 -17.353 1.00 15.67 ? 148 VAL D CG1 1 
ATOM   4492  C  CG2 . VAL D  1 175 ? 55.624  113.585 -19.526 1.00 17.31 ? 148 VAL D CG2 1 
ATOM   4493  N  N   . ILE D  1 176 ? 59.607  114.675 -17.269 1.00 16.59 ? 149 ILE D N   1 
ATOM   4494  C  CA  . ILE D  1 176 ? 60.918  114.415 -16.687 1.00 16.40 ? 149 ILE D CA  1 
ATOM   4495  C  C   . ILE D  1 176 ? 60.889  112.976 -16.068 1.00 16.56 ? 149 ILE D C   1 
ATOM   4496  O  O   . ILE D  1 176 ? 60.048  112.682 -15.220 1.00 21.41 ? 149 ILE D O   1 
ATOM   4497  C  CB  . ILE D  1 176 ? 61.249  115.474 -15.584 1.00 17.76 ? 149 ILE D CB  1 
ATOM   4498  C  CG1 . ILE D  1 176 ? 61.308  116.876 -16.251 1.00 19.98 ? 149 ILE D CG1 1 
ATOM   4499  C  CG2 . ILE D  1 176 ? 62.616  115.147 -14.966 1.00 16.84 ? 149 ILE D CG2 1 
ATOM   4500  C  CD1 . ILE D  1 176 ? 61.187  118.055 -15.261 1.00 19.74 ? 149 ILE D CD1 1 
ATOM   4501  N  N   . GLY D  1 177 ? 61.735  112.095 -16.562 1.00 17.83 ? 150 GLY D N   1 
ATOM   4502  C  CA  . GLY D  1 177 ? 61.707  110.659 -16.190 1.00 19.17 ? 150 GLY D CA  1 
ATOM   4503  C  C   . GLY D  1 177 ? 62.950  110.268 -15.438 1.00 20.22 ? 150 GLY D C   1 
ATOM   4504  O  O   . GLY D  1 177 ? 63.998  110.896 -15.571 1.00 18.63 ? 150 GLY D O   1 
ATOM   4505  N  N   . ILE D  1 178 ? 62.830  109.227 -14.617 1.00 20.62 ? 151 ILE D N   1 
ATOM   4506  C  CA  . ILE D  1 178 ? 64.000  108.651 -13.920 1.00 18.74 ? 151 ILE D CA  1 
ATOM   4507  C  C   . ILE D  1 178 ? 64.945  108.018 -14.920 1.00 20.91 ? 151 ILE D C   1 
ATOM   4508  O  O   . ILE D  1 178 ? 64.516  107.284 -15.858 1.00 18.70 ? 151 ILE D O   1 
ATOM   4509  C  CB  . ILE D  1 178 ? 63.528  107.579 -12.865 1.00 21.88 ? 151 ILE D CB  1 
ATOM   4510  C  CG1 . ILE D  1 178 ? 62.567  108.261 -11.918 1.00 24.49 ? 151 ILE D CG1 1 
ATOM   4511  C  CG2 . ILE D  1 178 ? 64.742  107.113 -12.014 1.00 25.36 ? 151 ILE D CG2 1 
ATOM   4512  C  CD1 . ILE D  1 178 ? 61.695  107.322 -11.061 1.00 30.92 ? 151 ILE D CD1 1 
ATOM   4513  N  N   . ALA D  1 179 ? 66.237  108.311 -14.752 1.00 17.95 ? 152 ALA D N   1 
ATOM   4514  C  CA  . ALA D  1 179 ? 67.237  107.833 -15.672 1.00 23.21 ? 152 ALA D CA  1 
ATOM   4515  C  C   . ALA D  1 179 ? 68.218  106.890 -14.958 1.00 25.41 ? 152 ALA D C   1 
ATOM   4516  O  O   . ALA D  1 179 ? 68.342  106.926 -13.731 1.00 26.37 ? 152 ALA D O   1 
ATOM   4517  C  CB  . ALA D  1 179 ? 68.018  109.000 -16.297 1.00 22.29 ? 152 ALA D CB  1 
ATOM   4518  N  N   . GLN D  1 180 ? 68.905  106.072 -15.733 1.00 29.95 ? 153 GLN D N   1 
ATOM   4519  C  CA  . GLN D  1 180 ? 69.848  105.109 -15.175 1.00 37.42 ? 153 GLN D CA  1 
ATOM   4520  C  C   . GLN D  1 180 ? 71.099  105.822 -14.652 1.00 48.25 ? 153 GLN D C   1 
ATOM   4521  O  O   . GLN D  1 180 ? 71.597  106.761 -15.309 1.00 48.24 ? 153 GLN D O   1 
ATOM   4522  C  CB  . GLN D  1 180 ? 70.224  104.061 -16.217 1.00 36.59 ? 153 GLN D CB  1 
ATOM   4523  C  CG  . GLN D  1 180 ? 70.970  102.886 -15.596 1.00 44.66 ? 153 GLN D CG  1 
ATOM   4524  C  CD  . GLN D  1 180 ? 71.374  101.887 -16.639 1.00 43.30 ? 153 GLN D CD  1 
ATOM   4525  O  OE1 . GLN D  1 180 ? 71.983  102.242 -17.650 1.00 49.01 ? 153 GLN D OE1 1 
ATOM   4526  N  NE2 . GLN D  1 180 ? 71.021  100.632 -16.418 1.00 45.85 ? 153 GLN D NE2 1 
ATOM   4527  O  OXT . GLN D  1 180 ? 71.618  105.474 -13.572 1.00 53.63 ? 153 GLN D OXT 1 
ATOM   4528  N  N   . MET E  1 27  ? 51.164  49.557  1.795   1.00 48.23 ? 0   MET E N   1 
ATOM   4529  C  CA  . MET E  1 27  ? 51.117  48.235  2.491   1.00 55.37 ? 0   MET E CA  1 
ATOM   4530  C  C   . MET E  1 27  ? 50.439  48.378  3.883   1.00 52.12 ? 0   MET E C   1 
ATOM   4531  O  O   . MET E  1 27  ? 49.304  47.928  4.042   1.00 49.83 ? 0   MET E O   1 
ATOM   4532  C  CB  . MET E  1 27  ? 52.508  47.588  2.576   1.00 52.11 ? 0   MET E CB  1 
ATOM   4533  N  N   . ALA E  1 28  ? 51.098  49.011  4.868   1.00 46.59 ? 1   ALA E N   1 
ATOM   4534  C  CA  . ALA E  1 28  ? 50.429  49.301  6.157   1.00 41.16 ? 1   ALA E CA  1 
ATOM   4535  C  C   . ALA E  1 28  ? 49.221  50.271  6.057   1.00 35.95 ? 1   ALA E C   1 
ATOM   4536  O  O   . ALA E  1 28  ? 49.315  51.345  5.505   1.00 36.89 ? 1   ALA E O   1 
ATOM   4537  C  CB  . ALA E  1 28  ? 51.438  49.821  7.170   1.00 42.57 ? 1   ALA E CB  1 
ATOM   4538  N  N   . THR E  1 29  ? 48.068  49.889  6.566   1.00 31.09 ? 2   THR E N   1 
ATOM   4539  C  CA  . THR E  1 29  ? 47.005  50.859  6.628   1.00 29.67 ? 2   THR E CA  1 
ATOM   4540  C  C   . THR E  1 29  ? 46.600  51.104  8.096   1.00 25.72 ? 2   THR E C   1 
ATOM   4541  O  O   . THR E  1 29  ? 45.764  51.954  8.341   1.00 23.70 ? 2   THR E O   1 
ATOM   4542  C  CB  . THR E  1 29  ? 45.778  50.432  5.792   1.00 29.51 ? 2   THR E CB  1 
ATOM   4543  O  OG1 . THR E  1 29  ? 45.317  49.204  6.304   1.00 33.79 ? 2   THR E OG1 1 
ATOM   4544  C  CG2 . THR E  1 29  ? 46.160  50.185  4.313   1.00 35.66 ? 2   THR E CG2 1 
ATOM   4545  N  N   . LYS E  1 30  ? 47.168  50.336  9.037   1.00 23.84 ? 3   LYS E N   1 
ATOM   4546  C  CA  . LYS E  1 30  ? 46.861  50.510  10.492  1.00 23.82 ? 3   LYS E CA  1 
ATOM   4547  C  C   . LYS E  1 30  ? 48.136  50.452  11.318  1.00 21.45 ? 3   LYS E C   1 
ATOM   4548  O  O   . LYS E  1 30  ? 49.061  49.643  11.025  1.00 20.90 ? 3   LYS E O   1 
ATOM   4549  C  CB  . LYS E  1 30  ? 45.909  49.414  10.978  1.00 28.81 ? 3   LYS E CB  1 
ATOM   4550  C  CG  . LYS E  1 30  ? 44.475  49.594  10.514  1.00 34.41 ? 3   LYS E CG  1 
ATOM   4551  C  CD  . LYS E  1 30  ? 43.637  48.376  10.896  1.00 42.66 ? 3   LYS E CD  1 
ATOM   4552  C  CE  . LYS E  1 30  ? 42.284  48.412  10.189  1.00 48.71 ? 3   LYS E CE  1 
ATOM   4553  N  NZ  . LYS E  1 30  ? 41.423  47.225  10.464  1.00 52.60 ? 3   LYS E NZ  1 
ATOM   4554  N  N   . ALA E  1 31  ? 48.232  51.305  12.341  1.00 18.00 ? 4   ALA E N   1 
ATOM   4555  C  CA  . ALA E  1 31  ? 49.404  51.289  13.228  1.00 17.43 ? 4   ALA E CA  1 
ATOM   4556  C  C   . ALA E  1 31  ? 48.851  51.597  14.636  1.00 17.78 ? 4   ALA E C   1 
ATOM   4557  O  O   . ALA E  1 31  ? 47.668  52.029  14.808  1.00 18.70 ? 4   ALA E O   1 
ATOM   4558  C  CB  . ALA E  1 31  ? 50.516  52.306  12.804  1.00 17.23 ? 4   ALA E CB  1 
ATOM   4559  N  N   . VAL E  1 32  ? 49.677  51.334  15.634  1.00 18.13 ? 5   VAL E N   1 
ATOM   4560  C  CA  . VAL E  1 32  ? 49.245  51.535  17.016  1.00 19.39 ? 5   VAL E CA  1 
ATOM   4561  C  C   . VAL E  1 32  ? 50.464  51.891  17.851  1.00 19.19 ? 5   VAL E C   1 
ATOM   4562  O  O   . VAL E  1 32  ? 51.613  51.562  17.507  1.00 21.05 ? 5   VAL E O   1 
ATOM   4563  C  CB  . VAL E  1 32  ? 48.485  50.298  17.567  1.00 19.31 ? 5   VAL E CB  1 
ATOM   4564  C  CG1 . VAL E  1 32  ? 49.450  49.132  17.744  1.00 20.32 ? 5   VAL E CG1 1 
ATOM   4565  C  CG2 . VAL E  1 32  ? 47.782  50.641  18.882  1.00 20.92 ? 5   VAL E CG2 1 
ATOM   4566  N  N   . CYS E  1 33  ? 50.232  52.607  18.946  1.00 19.28 ? 6   CYS E N   1 
ATOM   4567  C  CA  . CYS E  1 33  ? 51.322  53.032  19.803  1.00 17.94 ? 6   CYS E CA  1 
ATOM   4568  C  C   . CYS E  1 33  ? 50.834  52.940  21.252  1.00 18.83 ? 6   CYS E C   1 
ATOM   4569  O  O   . CYS E  1 33  ? 49.784  53.482  21.567  1.00 17.18 ? 6   CYS E O   1 
ATOM   4570  C  CB  . CYS E  1 33  ? 51.657  54.519  19.513  1.00 19.01 ? 6   CYS E CB  1 
ATOM   4571  S  SG  . CYS E  1 33  ? 53.041  55.079  20.476  1.00 22.08 ? 6   CYS E SG  1 
ATOM   4572  N  N   . VAL E  1 34  ? 51.625  52.280  22.110  1.00 17.67 ? 7   VAL E N   1 
ATOM   4573  C  CA  . VAL E  1 34  ? 51.413  52.234  23.571  1.00 18.63 ? 7   VAL E CA  1 
ATOM   4574  C  C   . VAL E  1 34  ? 52.322  53.211  24.263  1.00 18.87 ? 7   VAL E C   1 
ATOM   4575  O  O   . VAL E  1 34  ? 53.571  53.092  24.199  1.00 18.42 ? 7   VAL E O   1 
ATOM   4576  C  CB  . VAL E  1 34  ? 51.587  50.806  24.148  1.00 20.63 ? 7   VAL E CB  1 
ATOM   4577  C  CG1 . VAL E  1 34  ? 51.350  50.802  25.678  1.00 21.53 ? 7   VAL E CG1 1 
ATOM   4578  C  CG2 . VAL E  1 34  ? 50.654  49.841  23.436  1.00 20.64 ? 7   VAL E CG2 1 
ATOM   4579  N  N   . LEU E  1 35  ? 51.722  54.250  24.880  1.00 18.19 ? 8   LEU E N   1 
ATOM   4580  C  CA  . LEU E  1 35  ? 52.522  55.289  25.547  1.00 17.53 ? 8   LEU E CA  1 
ATOM   4581  C  C   . LEU E  1 35  ? 52.700  54.924  27.005  1.00 17.55 ? 8   LEU E C   1 
ATOM   4582  O  O   . LEU E  1 35  ? 51.714  54.559  27.641  1.00 19.55 ? 8   LEU E O   1 
ATOM   4583  C  CB  . LEU E  1 35  ? 51.845  56.665  25.473  1.00 18.95 ? 8   LEU E CB  1 
ATOM   4584  C  CG  . LEU E  1 35  ? 51.494  57.081  24.019  1.00 21.97 ? 8   LEU E CG  1 
ATOM   4585  C  CD1 . LEU E  1 35  ? 50.398  58.137  24.044  1.00 28.25 ? 8   LEU E CD1 1 
ATOM   4586  C  CD2 . LEU E  1 35  ? 52.702  57.672  23.379  1.00 22.95 ? 8   LEU E CD2 1 
ATOM   4587  N  N   . LYS E  1 36  ? 53.939  54.996  27.478  1.00 18.80 ? 9   LYS E N   1 
ATOM   4588  C  CA  . LYS E  1 36  ? 54.258  54.816  28.919  1.00 22.17 ? 9   LYS E CA  1 
ATOM   4589  C  C   . LYS E  1 36  ? 55.370  55.776  29.212  1.00 18.99 ? 9   LYS E C   1 
ATOM   4590  O  O   . LYS E  1 36  ? 56.120  56.187  28.326  1.00 18.19 ? 9   LYS E O   1 
ATOM   4591  C  CB  . LYS E  1 36  ? 54.850  53.398  29.195  1.00 26.75 ? 9   LYS E CB  1 
ATOM   4592  C  CG  . LYS E  1 36  ? 53.960  52.245  28.793  1.00 38.76 ? 9   LYS E CG  1 
ATOM   4593  C  CD  . LYS E  1 36  ? 54.500  50.914  29.348  1.00 43.65 ? 9   LYS E CD  1 
ATOM   4594  C  CE  . LYS E  1 36  ? 53.583  49.724  29.034  1.00 48.34 ? 9   LYS E CE  1 
ATOM   4595  N  NZ  . LYS E  1 36  ? 52.175  50.013  29.418  1.00 47.16 ? 9   LYS E NZ  1 
ATOM   4596  N  N   . GLY E  1 37  ? 55.565  56.104  30.482  1.00 22.25 ? 10  GLY E N   1 
ATOM   4597  C  CA  . GLY E  1 37  ? 56.729  56.887  30.838  1.00 23.89 ? 10  GLY E CA  1 
ATOM   4598  C  C   . GLY E  1 37  ? 57.073  56.627  32.288  1.00 27.55 ? 10  GLY E C   1 
ATOM   4599  O  O   . GLY E  1 37  ? 56.735  55.587  32.821  1.00 26.32 ? 10  GLY E O   1 
ATOM   4600  N  N   . ASP E  1 38  ? 57.762  57.576  32.890  1.00 28.43 ? 11  ASP E N   1 
ATOM   4601  C  CA  . ASP E  1 38  ? 58.293  57.382  34.242  1.00 34.27 ? 11  ASP E CA  1 
ATOM   4602  C  C   . ASP E  1 38  ? 57.249  57.750  35.279  1.00 35.17 ? 11  ASP E C   1 
ATOM   4603  O  O   . ASP E  1 38  ? 57.336  57.307  36.433  1.00 36.64 ? 11  ASP E O   1 
ATOM   4604  C  CB  . ASP E  1 38  ? 59.503  58.242  34.434  1.00 34.85 ? 11  ASP E CB  1 
ATOM   4605  C  CG  . ASP E  1 38  ? 60.722  57.599  33.910  1.00 47.01 ? 11  ASP E CG  1 
ATOM   4606  O  OD1 . ASP E  1 38  ? 60.827  56.345  33.989  1.00 45.88 ? 11  ASP E OD1 1 
ATOM   4607  O  OD2 . ASP E  1 38  ? 61.563  58.352  33.388  1.00 52.79 ? 11  ASP E OD2 1 
ATOM   4608  N  N   . GLY E  1 39  ? 56.237  58.515  34.861  1.00 29.07 ? 12  GLY E N   1 
ATOM   4609  C  CA  . GLY E  1 39  ? 55.170  58.902  35.777  1.00 28.52 ? 12  GLY E CA  1 
ATOM   4610  C  C   . GLY E  1 39  ? 53.906  58.162  35.446  1.00 24.62 ? 12  GLY E C   1 
ATOM   4611  O  O   . GLY E  1 39  ? 53.960  57.072  34.892  1.00 26.37 ? 12  GLY E O   1 
ATOM   4612  N  N   . PRO E  1 40  ? 52.737  58.779  35.717  1.00 22.03 ? 13  PRO E N   1 
ATOM   4613  C  CA  . PRO E  1 40  ? 51.502  58.034  35.556  1.00 22.45 ? 13  PRO E CA  1 
ATOM   4614  C  C   . PRO E  1 40  ? 50.869  58.092  34.178  1.00 21.43 ? 13  PRO E C   1 
ATOM   4615  O  O   . PRO E  1 40  ? 49.771  57.561  33.996  1.00 23.69 ? 13  PRO E O   1 
ATOM   4616  C  CB  . PRO E  1 40  ? 50.553  58.767  36.499  1.00 24.23 ? 13  PRO E CB  1 
ATOM   4617  C  CG  . PRO E  1 40  ? 51.027  60.195  36.424  1.00 24.10 ? 13  PRO E CG  1 
ATOM   4618  C  CD  . PRO E  1 40  ? 52.517  60.081  36.398  1.00 22.27 ? 13  PRO E CD  1 
ATOM   4619  N  N   . VAL E  1 41  ? 51.471  58.814  33.243  1.00 21.14 ? 14  VAL E N   1 
ATOM   4620  C  CA  . VAL E  1 41  ? 50.822  59.020  31.920  1.00 20.42 ? 14  VAL E CA  1 
ATOM   4621  C  C   . VAL E  1 41  ? 50.881  57.759  31.085  1.00 20.73 ? 14  VAL E C   1 
ATOM   4622  O  O   . VAL E  1 41  ? 51.953  57.190  30.890  1.00 22.32 ? 14  VAL E O   1 
ATOM   4623  C  CB  . VAL E  1 41  ? 51.430  60.217  31.163  1.00 20.77 ? 14  VAL E CB  1 
ATOM   4624  C  CG1 . VAL E  1 41  ? 50.794  60.355  29.769  1.00 18.26 ? 14  VAL E CG1 1 
ATOM   4625  C  CG2 . VAL E  1 41  ? 51.212  61.508  31.970  1.00 22.82 ? 14  VAL E CG2 1 
ATOM   4626  N  N   . GLN E  1 42  ? 49.740  57.307  30.617  1.00 21.53 ? 15  GLN E N   1 
ATOM   4627  C  CA  . GLN E  1 42  ? 49.715  56.157  29.716  1.00 23.67 ? 15  GLN E CA  1 
ATOM   4628  C  C   . GLN E  1 42  ? 48.586  56.243  28.752  1.00 21.94 ? 15  GLN E C   1 
ATOM   4629  O  O   . GLN E  1 42  ? 47.574  56.873  29.025  1.00 20.28 ? 15  GLN E O   1 
ATOM   4630  C  CB  . GLN E  1 42  ? 49.701  54.801  30.468  1.00 27.45 ? 15  GLN E CB  1 
ATOM   4631  C  CG  . GLN E  1 42  ? 48.568  54.565  31.422  1.00 35.59 ? 15  GLN E CG  1 
ATOM   4632  C  CD  . GLN E  1 42  ? 48.889  53.392  32.354  1.00 45.83 ? 15  GLN E CD  1 
ATOM   4633  O  OE1 . GLN E  1 42  ? 49.704  52.511  32.028  1.00 50.82 ? 15  GLN E OE1 1 
ATOM   4634  N  NE2 . GLN E  1 42  ? 48.303  53.399  33.516  1.00 44.28 ? 15  GLN E NE2 1 
ATOM   4635  N  N   . GLY E  1 43  ? 48.715  55.576  27.610  1.00 21.47 ? 16  GLY E N   1 
ATOM   4636  C  CA  . GLY E  1 43  ? 47.615  55.567  26.717  1.00 19.74 ? 16  GLY E CA  1 
ATOM   4637  C  C   . GLY E  1 43  ? 47.862  54.694  25.525  1.00 18.46 ? 16  GLY E C   1 
ATOM   4638  O  O   . GLY E  1 43  ? 48.936  54.109  25.418  1.00 18.37 ? 16  GLY E O   1 
ATOM   4639  N  N   . ILE E  1 44  ? 46.841  54.581  24.686  1.00 17.63 ? 17  ILE E N   1 
ATOM   4640  C  CA  . ILE E  1 44  ? 46.931  53.830  23.448  1.00 18.38 ? 17  ILE E CA  1 
ATOM   4641  C  C   . ILE E  1 44  ? 46.451  54.731  22.341  1.00 17.20 ? 17  ILE E C   1 
ATOM   4642  O  O   . ILE E  1 44  ? 45.305  55.281  22.382  1.00 18.28 ? 17  ILE E O   1 
ATOM   4643  C  CB  . ILE E  1 44  ? 46.053  52.554  23.485  1.00 19.66 ? 17  ILE E CB  1 
ATOM   4644  C  CG1 . ILE E  1 44  ? 46.673  51.554  24.491  1.00 24.39 ? 17  ILE E CG1 1 
ATOM   4645  C  CG2 . ILE E  1 44  ? 46.075  51.873  22.108  1.00 20.05 ? 17  ILE E CG2 1 
ATOM   4646  C  CD1 . ILE E  1 44  ? 45.753  50.394  24.821  1.00 27.95 ? 17  ILE E CD1 1 
ATOM   4647  N  N   . ILE E  1 45  ? 47.297  54.897  21.343  1.00 15.92 ? 18  ILE E N   1 
ATOM   4648  C  CA  . ILE E  1 45  ? 46.899  55.667  20.161  1.00 15.89 ? 18  ILE E CA  1 
ATOM   4649  C  C   . ILE E  1 45  ? 46.877  54.818  18.877  1.00 18.48 ? 18  ILE E C   1 
ATOM   4650  O  O   . ILE E  1 45  ? 47.845  54.100  18.568  1.00 17.94 ? 18  ILE E O   1 
ATOM   4651  C  CB  . ILE E  1 45  ? 47.827  56.895  20.025  1.00 15.05 ? 18  ILE E CB  1 
ATOM   4652  C  CG1 . ILE E  1 45  ? 47.688  57.853  21.276  1.00 14.10 ? 18  ILE E CG1 1 
ATOM   4653  C  CG2 . ILE E  1 45  ? 47.518  57.645  18.726  1.00 14.29 ? 18  ILE E CG2 1 
ATOM   4654  C  CD1 . ILE E  1 45  ? 46.262  58.528  21.414  1.00 15.49 ? 18  ILE E CD1 1 
ATOM   4655  N  N   . ASN E  1 46  ? 45.796  54.928  18.103  1.00 17.57 ? 19  ASN E N   1 
ATOM   4656  C  CA  . ASN E  1 46  ? 45.653  54.144  16.864  1.00 19.18 ? 19  ASN E CA  1 
ATOM   4657  C  C   . ASN E  1 46  ? 45.806  55.090  15.690  1.00 20.17 ? 19  ASN E C   1 
ATOM   4658  O  O   . ASN E  1 46  ? 45.483  56.298  15.817  1.00 16.87 ? 19  ASN E O   1 
ATOM   4659  C  CB  . ASN E  1 46  ? 44.216  53.612  16.813  1.00 18.80 ? 19  ASN E CB  1 
ATOM   4660  C  CG  . ASN E  1 46  ? 43.847  52.853  18.051  1.00 23.42 ? 19  ASN E CG  1 
ATOM   4661  O  OD1 . ASN E  1 46  ? 43.104  53.337  18.931  1.00 27.18 ? 19  ASN E OD1 1 
ATOM   4662  N  ND2 . ASN E  1 46  ? 44.383  51.675  18.160  1.00 19.83 ? 19  ASN E ND2 1 
ATOM   4663  N  N   . PHE E  1 47  ? 46.323  54.556  14.568  1.00 18.72 ? 20  PHE E N   1 
ATOM   4664  C  CA  . PHE E  1 47  ? 46.466  55.316  13.337  1.00 17.38 ? 20  PHE E CA  1 
ATOM   4665  C  C   . PHE E  1 47  ? 45.809  54.483  12.230  1.00 19.09 ? 20  PHE E C   1 
ATOM   4666  O  O   . PHE E  1 47  ? 45.942  53.220  12.215  1.00 19.16 ? 20  PHE E O   1 
ATOM   4667  C  CB  . PHE E  1 47  ? 47.962  55.441  13.001  1.00 16.89 ? 20  PHE E CB  1 
ATOM   4668  C  CG  . PHE E  1 47  ? 48.776  56.167  14.058  1.00 19.00 ? 20  PHE E CG  1 
ATOM   4669  C  CD1 . PHE E  1 47  ? 49.245  55.504  15.199  1.00 18.93 ? 20  PHE E CD1 1 
ATOM   4670  C  CD2 . PHE E  1 47  ? 49.067  57.508  13.902  1.00 19.10 ? 20  PHE E CD2 1 
ATOM   4671  C  CE1 . PHE E  1 47  ? 50.005  56.187  16.153  1.00 19.80 ? 20  PHE E CE1 1 
ATOM   4672  C  CE2 . PHE E  1 47  ? 49.830  58.203  14.864  1.00 21.00 ? 20  PHE E CE2 1 
ATOM   4673  C  CZ  . PHE E  1 47  ? 50.295  57.535  15.989  1.00 18.52 ? 20  PHE E CZ  1 
ATOM   4674  N  N   . GLU E  1 48  ? 45.055  55.127  11.352  1.00 18.41 ? 21  GLU E N   1 
ATOM   4675  C  CA  . GLU E  1 48  ? 44.490  54.382  10.210  1.00 21.07 ? 21  GLU E CA  1 
ATOM   4676  C  C   . GLU E  1 48  ? 44.645  55.236  8.956   1.00 21.69 ? 21  GLU E C   1 
ATOM   4677  O  O   . GLU E  1 48  ? 44.322  56.432  8.978   1.00 21.18 ? 21  GLU E O   1 
ATOM   4678  C  CB  . GLU E  1 48  ? 43.004  54.084  10.441  1.00 23.80 ? 21  GLU E CB  1 
ATOM   4679  C  CG  . GLU E  1 48  ? 42.387  53.409  9.216   1.00 29.84 ? 21  GLU E CG  1 
ATOM   4680  C  CD  . GLU E  1 48  ? 41.182  52.590  9.592   1.00 43.19 ? 21  GLU E CD  1 
ATOM   4681  O  OE1 . GLU E  1 48  ? 40.271  53.172  10.214  1.00 39.80 ? 21  GLU E OE1 1 
ATOM   4682  O  OE2 . GLU E  1 48  ? 41.158  51.368  9.273   1.00 51.62 ? 21  GLU E OE2 1 
ATOM   4683  N  N   . GLN E  1 49  ? 45.113  54.632  7.860   1.00 21.45 ? 22  GLN E N   1 
ATOM   4684  C  CA  . GLN E  1 49  ? 45.248  55.343  6.622   1.00 20.63 ? 22  GLN E CA  1 
ATOM   4685  C  C   . GLN E  1 49  ? 44.744  54.405  5.530   1.00 26.44 ? 22  GLN E C   1 
ATOM   4686  O  O   . GLN E  1 49  ? 45.421  53.442  5.119   1.00 26.78 ? 22  GLN E O   1 
ATOM   4687  C  CB  . GLN E  1 49  ? 46.674  55.801  6.399   1.00 20.24 ? 22  GLN E CB  1 
ATOM   4688  C  CG  . GLN E  1 49  ? 46.896  56.680  5.141   1.00 18.88 ? 22  GLN E CG  1 
ATOM   4689  C  CD  . GLN E  1 49  ? 48.392  56.909  4.908   1.00 20.36 ? 22  GLN E CD  1 
ATOM   4690  O  OE1 . GLN E  1 49  ? 49.242  56.044  5.280   1.00 20.17 ? 22  GLN E OE1 1 
ATOM   4691  N  NE2 . GLN E  1 49  ? 48.752  58.076  4.340   1.00 20.30 ? 22  GLN E NE2 1 
ATOM   4692  N  N   . LYS E  1 50  ? 43.536  54.663  5.118   1.00 29.40 ? 23  LYS E N   1 
ATOM   4693  C  CA  . LYS E  1 50  ? 42.886  53.764  4.158   1.00 37.31 ? 23  LYS E CA  1 
ATOM   4694  C  C   . LYS E  1 50  ? 43.520  53.841  2.768   1.00 36.52 ? 23  LYS E C   1 
ATOM   4695  O  O   . LYS E  1 50  ? 43.651  52.827  2.094   1.00 36.95 ? 23  LYS E O   1 
ATOM   4696  C  CB  . LYS E  1 50  ? 41.385  53.970  4.184   1.00 41.64 ? 23  LYS E CB  1 
ATOM   4697  C  CG  . LYS E  1 50  ? 40.773  52.880  5.057   1.00 52.42 ? 23  LYS E CG  1 
ATOM   4698  C  CD  . LYS E  1 50  ? 39.539  53.313  5.838   1.00 54.33 ? 23  LYS E CD  1 
ATOM   4699  C  CE  . LYS E  1 50  ? 39.098  52.150  6.721   1.00 57.12 ? 23  LYS E CE  1 
ATOM   4700  N  NZ  . LYS E  1 50  ? 37.816  52.456  7.415   1.00 63.81 ? 23  LYS E NZ  1 
ATOM   4701  N  N   . GLU E  1 51  ? 44.032  55.012  2.395   1.00 31.10 ? 24  GLU E N   1 
ATOM   4702  C  CA  . GLU E  1 51  ? 44.666  55.197  1.073   1.00 32.98 ? 24  GLU E CA  1 
ATOM   4703  C  C   . GLU E  1 51  ? 45.990  55.856  1.279   1.00 31.34 ? 24  GLU E C   1 
ATOM   4704  O  O   . GLU E  1 51  ? 46.085  56.793  2.070   1.00 28.95 ? 24  GLU E O   1 
ATOM   4705  C  CB  . GLU E  1 51  ? 43.816  56.158  0.232   1.00 38.92 ? 24  GLU E CB  1 
ATOM   4706  C  CG  . GLU E  1 51  ? 42.343  55.816  0.161   1.00 44.62 ? 24  GLU E CG  1 
ATOM   4707  C  CD  . GLU E  1 51  ? 42.026  54.773  -0.912  1.00 59.14 ? 24  GLU E CD  1 
ATOM   4708  O  OE1 . GLU E  1 51  ? 42.962  54.071  -1.411  1.00 54.05 ? 24  GLU E OE1 1 
ATOM   4709  O  OE2 . GLU E  1 51  ? 40.824  54.648  -1.264  1.00 62.16 ? 24  GLU E OE2 1 
ATOM   4710  N  N   . SER E  1 52  ? 47.024  55.409  0.565   1.00 31.64 ? 25  SER E N   1 
ATOM   4711  C  CA  . SER E  1 52  ? 48.356  55.957  0.814   1.00 35.49 ? 25  SER E CA  1 
ATOM   4712  C  C   . SER E  1 52  ? 48.464  57.403  0.412   1.00 32.09 ? 25  SER E C   1 
ATOM   4713  O  O   . SER E  1 52  ? 49.367  58.104  0.850   1.00 36.14 ? 25  SER E O   1 
ATOM   4714  C  CB  . SER E  1 52  ? 49.444  55.145  0.088   1.00 38.11 ? 25  SER E CB  1 
ATOM   4715  O  OG  . SER E  1 52  ? 49.264  55.225  -1.308  1.00 36.85 ? 25  SER E OG  1 
ATOM   4716  N  N   . ASN E  1 53  ? 47.553  57.881  -0.423  1.00 29.85 ? 26  ASN E N   1 
ATOM   4717  C  CA  . ASN E  1 53  ? 47.604  59.324  -0.778  1.00 33.02 ? 26  ASN E CA  1 
ATOM   4718  C  C   . ASN E  1 53  ? 46.603  60.148  0.057   1.00 33.23 ? 26  ASN E C   1 
ATOM   4719  O  O   . ASN E  1 53  ? 46.210  61.229  -0.349  1.00 34.62 ? 26  ASN E O   1 
ATOM   4720  C  CB  . ASN E  1 53  ? 47.290  59.505  -2.275  1.00 34.08 ? 26  ASN E CB  1 
ATOM   4721  C  CG  . ASN E  1 53  ? 45.869  59.014  -2.642  1.00 41.92 ? 26  ASN E CG  1 
ATOM   4722  O  OD1 . ASN E  1 53  ? 45.192  58.352  -1.832  1.00 38.01 ? 26  ASN E OD1 1 
ATOM   4723  N  ND2 . ASN E  1 53  ? 45.414  59.341  -3.855  1.00 34.32 ? 26  ASN E ND2 1 
ATOM   4724  N  N   . GLY E  1 54  ? 46.134  59.605  1.183   1.00 29.28 ? 27  GLY E N   1 
ATOM   4725  C  CA  . GLY E  1 54  ? 45.047  60.269  1.916   1.00 28.56 ? 27  GLY E CA  1 
ATOM   4726  C  C   . GLY E  1 54  ? 45.457  60.503  3.358   1.00 23.61 ? 27  GLY E C   1 
ATOM   4727  O  O   . GLY E  1 54  ? 46.534  60.105  3.767   1.00 22.48 ? 27  GLY E O   1 
ATOM   4728  N  N   . PRO E  1 55  ? 44.577  61.118  4.142   1.00 24.22 ? 28  PRO E N   1 
ATOM   4729  C  CA  . PRO E  1 55  ? 44.942  61.493  5.507   1.00 23.69 ? 28  PRO E CA  1 
ATOM   4730  C  C   . PRO E  1 55  ? 45.044  60.282  6.448   1.00 22.93 ? 28  PRO E C   1 
ATOM   4731  O  O   . PRO E  1 55  ? 44.444  59.232  6.185   1.00 20.96 ? 28  PRO E O   1 
ATOM   4732  C  CB  . PRO E  1 55  ? 43.761  62.374  5.976   1.00 26.20 ? 28  PRO E CB  1 
ATOM   4733  C  CG  . PRO E  1 55  ? 42.803  62.435  4.838   1.00 29.80 ? 28  PRO E CG  1 
ATOM   4734  C  CD  . PRO E  1 55  ? 43.165  61.406  3.822   1.00 27.60 ? 28  PRO E CD  1 
ATOM   4735  N  N   . VAL E  1 56  ? 45.756  60.478  7.556   1.00 20.29 ? 29  VAL E N   1 
ATOM   4736  C  CA  . VAL E  1 56  ? 45.821  59.460  8.580   1.00 17.69 ? 29  VAL E CA  1 
ATOM   4737  C  C   . VAL E  1 56  ? 44.895  59.919  9.725   1.00 20.01 ? 29  VAL E C   1 
ATOM   4738  O  O   . VAL E  1 56  ? 45.001  61.061  10.196  1.00 20.67 ? 29  VAL E O   1 
ATOM   4739  C  CB  . VAL E  1 56  ? 47.256  59.418  9.156   1.00 17.23 ? 29  VAL E CB  1 
ATOM   4740  C  CG1 . VAL E  1 56  ? 47.363  58.324  10.250  1.00 16.22 ? 29  VAL E CG1 1 
ATOM   4741  C  CG2 . VAL E  1 56  ? 48.274  59.124  8.043   1.00 16.89 ? 29  VAL E CG2 1 
ATOM   4742  N  N   . LYS E  1 57  ? 44.015  59.031  10.162  1.00 19.06 ? 30  LYS E N   1 
ATOM   4743  C  CA  . LYS E  1 57  ? 43.208  59.301  11.356  1.00 21.18 ? 30  LYS E CA  1 
ATOM   4744  C  C   . LYS E  1 57  ? 44.009  58.797  12.535  1.00 19.25 ? 30  LYS E C   1 
ATOM   4745  O  O   . LYS E  1 57  ? 44.546  57.667  12.510  1.00 18.87 ? 30  LYS E O   1 
ATOM   4746  C  CB  . LYS E  1 57  ? 41.915  58.524  11.278  1.00 25.58 ? 30  LYS E CB  1 
ATOM   4747  C  CG  . LYS E  1 57  ? 41.091  58.930  10.068  1.00 33.81 ? 30  LYS E CG  1 
ATOM   4748  C  CD  . LYS E  1 57  ? 39.706  58.275  10.086  1.00 43.65 ? 30  LYS E CD  1 
ATOM   4749  C  CE  . LYS E  1 57  ? 38.820  58.884  8.995   1.00 43.39 ? 30  LYS E CE  1 
ATOM   4750  N  NZ  . LYS E  1 57  ? 37.412  58.396  9.067   1.00 51.78 ? 30  LYS E NZ  1 
ATOM   4751  N  N   . VAL E  1 58  ? 44.048  59.610  13.574  1.00 18.94 ? 31  VAL E N   1 
ATOM   4752  C  CA  . VAL E  1 58  ? 44.780  59.365  14.804  1.00 17.95 ? 31  VAL E CA  1 
ATOM   4753  C  C   . VAL E  1 58  ? 43.782  59.490  15.962  1.00 20.61 ? 31  VAL E C   1 
ATOM   4754  O  O   . VAL E  1 58  ? 43.124  60.556  16.139  1.00 18.77 ? 31  VAL E O   1 
ATOM   4755  C  CB  . VAL E  1 58  ? 45.911  60.423  14.973  1.00 16.62 ? 31  VAL E CB  1 
ATOM   4756  C  CG1 . VAL E  1 58  ? 46.772  60.039  16.201  1.00 14.73 ? 31  VAL E CG1 1 
ATOM   4757  C  CG2 . VAL E  1 58  ? 46.782  60.488  13.682  1.00 16.79 ? 31  VAL E CG2 1 
ATOM   4758  N  N   . TRP E  1 59  ? 43.631  58.424  16.755  1.00 20.36 ? 32  TRP E N   1 
ATOM   4759  C  CA  . TRP E  1 59  ? 42.665  58.509  17.843  1.00 20.12 ? 32  TRP E CA  1 
ATOM   4760  C  C   . TRP E  1 59  ? 42.980  57.526  18.971  1.00 19.87 ? 32  TRP E C   1 
ATOM   4761  O  O   . TRP E  1 59  ? 43.607  56.524  18.756  1.00 18.92 ? 32  TRP E O   1 
ATOM   4762  C  CB  . TRP E  1 59  ? 41.237  58.303  17.324  1.00 21.24 ? 32  TRP E CB  1 
ATOM   4763  C  CG  . TRP E  1 59  ? 40.887  56.841  17.127  1.00 23.87 ? 32  TRP E CG  1 
ATOM   4764  C  CD1 . TRP E  1 59  ? 40.248  56.009  18.013  1.00 25.12 ? 32  TRP E CD1 1 
ATOM   4765  C  CD2 . TRP E  1 59  ? 41.243  56.038  16.010  1.00 26.40 ? 32  TRP E CD2 1 
ATOM   4766  N  NE1 . TRP E  1 59  ? 40.176  54.754  17.509  1.00 26.48 ? 32  TRP E NE1 1 
ATOM   4767  C  CE2 . TRP E  1 59  ? 40.763  54.727  16.273  1.00 26.78 ? 32  TRP E CE2 1 
ATOM   4768  C  CE3 . TRP E  1 59  ? 41.934  56.291  14.824  1.00 25.53 ? 32  TRP E CE3 1 
ATOM   4769  C  CZ2 . TRP E  1 59  ? 40.903  53.669  15.367  1.00 29.10 ? 32  TRP E CZ2 1 
ATOM   4770  C  CZ3 . TRP E  1 59  ? 42.076  55.213  13.881  1.00 29.35 ? 32  TRP E CZ3 1 
ATOM   4771  C  CH2 . TRP E  1 59  ? 41.574  53.920  14.176  1.00 29.97 ? 32  TRP E CH2 1 
ATOM   4772  N  N   . GLY E  1 60  ? 42.553  57.846  20.175  1.00 18.48 ? 33  GLY E N   1 
ATOM   4773  C  CA  . GLY E  1 60  ? 42.644  56.885  21.303  1.00 19.64 ? 33  GLY E CA  1 
ATOM   4774  C  C   . GLY E  1 60  ? 42.603  57.748  22.529  1.00 22.99 ? 33  GLY E C   1 
ATOM   4775  O  O   . GLY E  1 60  ? 42.083  58.842  22.491  1.00 24.37 ? 33  GLY E O   1 
ATOM   4776  N  N   . SER E  1 61  ? 43.112  57.239  23.626  1.00 25.58 ? 34  SER E N   1 
ATOM   4777  C  CA  . SER E  1 61  ? 42.876  57.890  24.890  1.00 24.92 ? 34  SER E CA  1 
ATOM   4778  C  C   . SER E  1 61  ? 44.160  57.907  25.658  1.00 22.70 ? 34  SER E C   1 
ATOM   4779  O  O   . SER E  1 61  ? 44.882  56.890  25.698  1.00 22.40 ? 34  SER E O   1 
ATOM   4780  C  CB  . SER E  1 61  ? 41.846  57.069  25.656  1.00 29.19 ? 34  SER E CB  1 
ATOM   4781  O  OG  . SER E  1 61  ? 41.502  57.824  26.784  1.00 38.88 ? 34  SER E OG  1 
ATOM   4782  N  N   . ILE E  1 62  ? 44.506  59.054  26.247  1.00 18.75 ? 35  ILE E N   1 
ATOM   4783  C  CA  . ILE E  1 62  ? 45.698  59.131  27.067  1.00 18.02 ? 35  ILE E CA  1 
ATOM   4784  C  C   . ILE E  1 62  ? 45.245  59.583  28.464  1.00 23.00 ? 35  ILE E C   1 
ATOM   4785  O  O   . ILE E  1 62  ? 44.466  60.541  28.555  1.00 21.97 ? 35  ILE E O   1 
ATOM   4786  C  CB  . ILE E  1 62  ? 46.677  60.180  26.517  1.00 17.55 ? 35  ILE E CB  1 
ATOM   4787  C  CG1 . ILE E  1 62  ? 46.937  59.911  25.024  1.00 17.49 ? 35  ILE E CG1 1 
ATOM   4788  C  CG2 . ILE E  1 62  ? 47.961  60.238  27.382  1.00 17.62 ? 35  ILE E CG2 1 
ATOM   4789  C  CD1 . ILE E  1 62  ? 47.898  60.904  24.366  1.00 21.52 ? 35  ILE E CD1 1 
ATOM   4790  N  N   . LYS E  1 63  ? 45.679  58.877  29.513  1.00 22.61 ? 36  LYS E N   1 
ATOM   4791  C  CA  . LYS E  1 63  ? 45.243  59.225  30.892  1.00 24.79 ? 36  LYS E CA  1 
ATOM   4792  C  C   . LYS E  1 63  ? 46.403  59.587  31.752  1.00 23.32 ? 36  LYS E C   1 
ATOM   4793  O  O   . LYS E  1 63  ? 47.565  59.482  31.315  1.00 19.58 ? 36  LYS E O   1 
ATOM   4794  C  CB  . LYS E  1 63  ? 44.368  58.118  31.488  1.00 27.24 ? 36  LYS E CB  1 
ATOM   4795  C  CG  . LYS E  1 63  ? 44.998  56.779  31.779  1.00 35.60 ? 36  LYS E CG  1 
ATOM   4796  C  CD  . LYS E  1 63  ? 43.860  55.781  32.167  1.00 43.25 ? 36  LYS E CD  1 
ATOM   4797  C  CE  . LYS E  1 63  ? 44.211  54.305  31.987  1.00 47.81 ? 36  LYS E CE  1 
ATOM   4798  N  NZ  . LYS E  1 63  ? 45.615  54.081  32.447  1.00 47.07 ? 36  LYS E NZ  1 
ATOM   4799  N  N   . GLY E  1 64  ? 46.140  60.018  32.996  1.00 22.95 ? 37  GLY E N   1 
ATOM   4800  C  CA  . GLY E  1 64  ? 47.218  60.444  33.832  1.00 19.86 ? 37  GLY E CA  1 
ATOM   4801  C  C   . GLY E  1 64  ? 47.773  61.828  33.563  1.00 20.64 ? 37  GLY E C   1 
ATOM   4802  O  O   . GLY E  1 64  ? 48.819  62.151  34.101  1.00 19.63 ? 37  GLY E O   1 
ATOM   4803  N  N   . LEU E  1 65  ? 47.054  62.670  32.798  1.00 20.87 ? 38  LEU E N   1 
ATOM   4804  C  CA  . LEU E  1 65  ? 47.569  63.991  32.417  1.00 19.09 ? 38  LEU E CA  1 
ATOM   4805  C  C   . LEU E  1 65  ? 46.984  65.109  33.308  1.00 22.13 ? 38  LEU E C   1 
ATOM   4806  O  O   . LEU E  1 65  ? 45.816  65.000  33.678  1.00 24.15 ? 38  LEU E O   1 
ATOM   4807  C  CB  . LEU E  1 65  ? 47.148  64.323  30.953  1.00 19.22 ? 38  LEU E CB  1 
ATOM   4808  C  CG  . LEU E  1 65  ? 47.809  63.451  29.841  1.00 19.56 ? 38  LEU E CG  1 
ATOM   4809  C  CD1 . LEU E  1 65  ? 47.045  63.578  28.511  1.00 19.23 ? 38  LEU E CD1 1 
ATOM   4810  C  CD2 . LEU E  1 65  ? 49.257  63.908  29.700  1.00 18.84 ? 38  LEU E CD2 1 
ATOM   4811  N  N   . THR E  1 66  ? 47.735  66.185  33.540  1.00 20.71 ? 39  THR E N   1 
ATOM   4812  C  CA  . THR E  1 66  ? 47.113  67.426  34.078  1.00 24.49 ? 39  THR E CA  1 
ATOM   4813  C  C   . THR E  1 66  ? 46.157  68.061  33.064  1.00 24.83 ? 39  THR E C   1 
ATOM   4814  O  O   . THR E  1 66  ? 46.405  68.066  31.837  1.00 21.16 ? 39  THR E O   1 
ATOM   4815  C  CB  . THR E  1 66  ? 48.182  68.452  34.451  1.00 26.35 ? 39  THR E CB  1 
ATOM   4816  O  OG1 . THR E  1 66  ? 48.922  68.773  33.278  1.00 28.34 ? 39  THR E OG1 1 
ATOM   4817  C  CG2 . THR E  1 66  ? 49.179  67.875  35.455  1.00 27.11 ? 39  THR E CG2 1 
ATOM   4818  N  N   . GLU E  1 67  ? 45.041  68.607  33.567  1.00 24.05 ? 40  GLU E N   1 
ATOM   4819  C  CA  . GLU E  1 67  ? 44.018  69.244  32.753  1.00 23.95 ? 40  GLU E CA  1 
ATOM   4820  C  C   . GLU E  1 67  ? 44.639  70.301  31.861  1.00 23.34 ? 40  GLU E C   1 
ATOM   4821  O  O   . GLU E  1 67  ? 45.528  71.036  32.287  1.00 24.49 ? 40  GLU E O   1 
ATOM   4822  C  CB  . GLU E  1 67  ? 42.910  69.875  33.674  1.00 27.54 ? 40  GLU E CB  1 
ATOM   4823  C  CG  . GLU E  1 67  ? 41.893  70.739  32.907  1.00 31.62 ? 40  GLU E CG  1 
ATOM   4824  C  CD  . GLU E  1 67  ? 40.709  71.195  33.782  1.00 39.06 ? 40  GLU E CD  1 
ATOM   4825  O  OE1 . GLU E  1 67  ? 40.875  71.201  35.027  1.00 38.12 ? 40  GLU E OE1 1 
ATOM   4826  O  OE2 . GLU E  1 67  ? 39.618  71.504  33.224  1.00 43.28 ? 40  GLU E OE2 1 
ATOM   4827  N  N   . GLY E  1 68  ? 44.217  70.356  30.606  1.00 21.39 ? 41  GLY E N   1 
ATOM   4828  C  CA  . GLY E  1 68  ? 44.713  71.414  29.706  1.00 21.62 ? 41  GLY E CA  1 
ATOM   4829  C  C   . GLY E  1 68  ? 45.467  70.864  28.489  1.00 21.24 ? 41  GLY E C   1 
ATOM   4830  O  O   . GLY E  1 68  ? 45.396  69.688  28.242  1.00 18.21 ? 41  GLY E O   1 
ATOM   4831  N  N   . LEU E  1 69  ? 46.222  71.724  27.793  1.00 19.14 ? 42  LEU E N   1 
ATOM   4832  C  CA  . LEU E  1 69  ? 46.862  71.382  26.508  1.00 19.01 ? 42  LEU E CA  1 
ATOM   4833  C  C   . LEU E  1 69  ? 48.205  70.688  26.750  1.00 17.77 ? 42  LEU E C   1 
ATOM   4834  O  O   . LEU E  1 69  ? 49.002  71.121  27.585  1.00 16.89 ? 42  LEU E O   1 
ATOM   4835  C  CB  . LEU E  1 69  ? 47.138  72.665  25.694  1.00 19.98 ? 42  LEU E CB  1 
ATOM   4836  C  CG  . LEU E  1 69  ? 45.905  73.417  25.125  1.00 23.47 ? 42  LEU E CG  1 
ATOM   4837  C  CD1 . LEU E  1 69  ? 46.352  74.797  24.638  1.00 25.84 ? 42  LEU E CD1 1 
ATOM   4838  C  CD2 . LEU E  1 69  ? 45.173  72.680  24.000  1.00 22.82 ? 42  LEU E CD2 1 
ATOM   4839  N  N   . HIS E  1 70  ? 48.494  69.698  25.901  1.00 15.72 ? 43  HIS E N   1 
ATOM   4840  C  CA  . HIS E  1 70  ? 49.792  68.985  25.925  1.00 15.66 ? 43  HIS E CA  1 
ATOM   4841  C  C   . HIS E  1 70  ? 50.295  68.779  24.489  1.00 14.58 ? 43  HIS E C   1 
ATOM   4842  O  O   . HIS E  1 70  ? 49.534  68.251  23.661  1.00 14.79 ? 43  HIS E O   1 
ATOM   4843  C  CB  . HIS E  1 70  ? 49.556  67.600  26.606  1.00 16.60 ? 43  HIS E CB  1 
ATOM   4844  C  CG  . HIS E  1 70  ? 49.269  67.711  28.084  1.00 16.77 ? 43  HIS E CG  1 
ATOM   4845  N  ND1 . HIS E  1 70  ? 50.280  67.839  29.023  1.00 19.96 ? 43  HIS E ND1 1 
ATOM   4846  C  CD2 . HIS E  1 70  ? 48.104  67.806  28.765  1.00 19.24 ? 43  HIS E CD2 1 
ATOM   4847  C  CE1 . HIS E  1 70  ? 49.742  67.924  30.233  1.00 20.35 ? 43  HIS E CE1 1 
ATOM   4848  N  NE2 . HIS E  1 70  ? 48.426  67.934  30.100  1.00 19.12 ? 43  HIS E NE2 1 
ATOM   4849  N  N   . GLY E  1 71  ? 51.566  69.124  24.250  1.00 14.17 ? 44  GLY E N   1 
ATOM   4850  C  CA  . GLY E  1 71  ? 52.176  68.966  22.891  1.00 14.55 ? 44  GLY E CA  1 
ATOM   4851  C  C   . GLY E  1 71  ? 52.143  67.451  22.565  1.00 15.51 ? 44  GLY E C   1 
ATOM   4852  O  O   . GLY E  1 71  ? 52.258  66.598  23.458  1.00 13.70 ? 44  GLY E O   1 
ATOM   4853  N  N   . PHE E  1 72  ? 51.961  67.123  21.297  1.00 15.36 ? 45  PHE E N   1 
ATOM   4854  C  CA  . PHE E  1 72  ? 51.748  65.719  20.861  1.00 15.45 ? 45  PHE E CA  1 
ATOM   4855  C  C   . PHE E  1 72  ? 52.471  65.617  19.534  1.00 15.51 ? 45  PHE E C   1 
ATOM   4856  O  O   . PHE E  1 72  ? 52.009  66.178  18.512  1.00 14.88 ? 45  PHE E O   1 
ATOM   4857  C  CB  . PHE E  1 72  ? 50.250  65.541  20.712  1.00 15.77 ? 45  PHE E CB  1 
ATOM   4858  C  CG  . PHE E  1 72  ? 49.767  64.138  20.370  1.00 16.04 ? 45  PHE E CG  1 
ATOM   4859  C  CD1 . PHE E  1 72  ? 49.857  63.091  21.283  1.00 16.41 ? 45  PHE E CD1 1 
ATOM   4860  C  CD2 . PHE E  1 72  ? 49.145  63.919  19.158  1.00 16.45 ? 45  PHE E CD2 1 
ATOM   4861  C  CE1 . PHE E  1 72  ? 49.269  61.848  20.969  1.00 16.01 ? 45  PHE E CE1 1 
ATOM   4862  C  CE2 . PHE E  1 72  ? 48.576  62.687  18.826  1.00 17.07 ? 45  PHE E CE2 1 
ATOM   4863  C  CZ  . PHE E  1 72  ? 48.636  61.659  19.738  1.00 17.55 ? 45  PHE E CZ  1 
ATOM   4864  N  N   . HIS E  1 73  ? 53.612  64.909  19.533  1.00 15.27 ? 46  HIS E N   1 
ATOM   4865  C  CA  . HIS E  1 73  ? 54.531  64.973  18.383  1.00 14.86 ? 46  HIS E CA  1 
ATOM   4866  C  C   . HIS E  1 73  ? 55.077  63.578  18.055  1.00 17.10 ? 46  HIS E C   1 
ATOM   4867  O  O   . HIS E  1 73  ? 55.285  62.743  18.964  1.00 15.69 ? 46  HIS E O   1 
ATOM   4868  C  CB  . HIS E  1 73  ? 55.748  65.864  18.735  1.00 16.41 ? 46  HIS E CB  1 
ATOM   4869  C  CG  . HIS E  1 73  ? 55.362  67.241  19.194  1.00 18.25 ? 46  HIS E CG  1 
ATOM   4870  N  ND1 . HIS E  1 73  ? 55.754  67.762  20.404  1.00 20.31 ? 46  HIS E ND1 1 
ATOM   4871  C  CD2 . HIS E  1 73  ? 54.542  68.166  18.634  1.00 18.61 ? 46  HIS E CD2 1 
ATOM   4872  C  CE1 . HIS E  1 73  ? 55.248  68.974  20.549  1.00 19.33 ? 46  HIS E CE1 1 
ATOM   4873  N  NE2 . HIS E  1 73  ? 54.487  69.236  19.502  1.00 20.20 ? 46  HIS E NE2 1 
ATOM   4874  N  N   . VAL E  1 74  ? 55.364  63.379  16.771  1.00 14.97 ? 47  VAL E N   1 
ATOM   4875  C  CA  . VAL E  1 74  ? 56.159  62.203  16.370  1.00 14.96 ? 47  VAL E CA  1 
ATOM   4876  C  C   . VAL E  1 74  ? 57.596  62.636  16.364  1.00 15.56 ? 47  VAL E C   1 
ATOM   4877  O  O   . VAL E  1 74  ? 57.983  63.629  15.701  1.00 17.29 ? 47  VAL E O   1 
ATOM   4878  C  CB  . VAL E  1 74  ? 55.734  61.680  14.998  1.00 14.66 ? 47  VAL E CB  1 
ATOM   4879  C  CG1 . VAL E  1 74  ? 56.594  60.399  14.635  1.00 14.88 ? 47  VAL E CG1 1 
ATOM   4880  C  CG2 . VAL E  1 74  ? 54.240  61.330  15.070  1.00 15.89 ? 47  VAL E CG2 1 
ATOM   4881  N  N   . HIS E  1 75  ? 58.427  61.891  17.101  1.00 14.97 ? 48  HIS E N   1 
ATOM   4882  C  CA  . HIS E  1 75  ? 59.857  62.177  17.151  1.00 15.14 ? 48  HIS E CA  1 
ATOM   4883  C  C   . HIS E  1 75  ? 60.624  61.165  16.254  1.00 17.32 ? 48  HIS E C   1 
ATOM   4884  O  O   . HIS E  1 75  ? 60.083  60.139  15.868  1.00 16.46 ? 48  HIS E O   1 
ATOM   4885  C  CB  . HIS E  1 75  ? 60.407  62.086  18.607  1.00 15.40 ? 48  HIS E CB  1 
ATOM   4886  C  CG  . HIS E  1 75  ? 59.931  63.206  19.490  1.00 16.80 ? 48  HIS E CG  1 
ATOM   4887  N  ND1 . HIS E  1 75  ? 60.791  64.079  20.127  1.00 15.74 ? 48  HIS E ND1 1 
ATOM   4888  C  CD2 . HIS E  1 75  ? 58.667  63.606  19.814  1.00 16.93 ? 48  HIS E CD2 1 
ATOM   4889  C  CE1 . HIS E  1 75  ? 60.074  64.931  20.871  1.00 17.65 ? 48  HIS E CE1 1 
ATOM   4890  N  NE2 . HIS E  1 75  ? 58.788  64.682  20.659  1.00 16.91 ? 48  HIS E NE2 1 
ATOM   4891  N  N   . GLU E  1 76  ? 61.881  61.516  15.941  1.00 16.98 ? 49  GLU E N   1 
ATOM   4892  C  CA  . GLU E  1 76  ? 62.565  60.921  14.807  1.00 17.60 ? 49  GLU E CA  1 
ATOM   4893  C  C   . GLU E  1 76  ? 62.879  59.433  15.014  1.00 18.80 ? 49  GLU E C   1 
ATOM   4894  O  O   . GLU E  1 76  ? 62.673  58.645  14.097  1.00 20.70 ? 49  GLU E O   1 
ATOM   4895  C  CB  . GLU E  1 76  ? 63.826  61.692  14.523  1.00 19.39 ? 49  GLU E CB  1 
ATOM   4896  C  CG  . GLU E  1 76  ? 64.503  61.154  13.258  1.00 24.53 ? 49  GLU E CG  1 
ATOM   4897  C  CD  . GLU E  1 76  ? 65.748  61.919  12.913  1.00 27.86 ? 49  GLU E CD  1 
ATOM   4898  O  OE1 . GLU E  1 76  ? 66.118  62.868  13.635  1.00 28.24 ? 49  GLU E OE1 1 
ATOM   4899  O  OE2 . GLU E  1 76  ? 66.377  61.495  11.935  1.00 30.76 ? 49  GLU E OE2 1 
ATOM   4900  N  N   . PHE E  1 77  ? 63.353  59.062  16.201  1.00 18.29 ? 50  PHE E N   1 
ATOM   4901  C  CA  . PHE E  1 77  ? 63.862  57.677  16.419  1.00 20.13 ? 50  PHE E CA  1 
ATOM   4902  C  C   . PHE E  1 77  ? 62.928  56.871  17.282  1.00 19.24 ? 50  PHE E C   1 
ATOM   4903  O  O   . PHE E  1 77  ? 62.402  57.388  18.266  1.00 19.66 ? 50  PHE E O   1 
ATOM   4904  C  CB  . PHE E  1 77  ? 65.245  57.735  17.091  1.00 19.45 ? 50  PHE E CB  1 
ATOM   4905  C  CG  . PHE E  1 77  ? 66.210  58.571  16.340  1.00 22.54 ? 50  PHE E CG  1 
ATOM   4906  C  CD1 . PHE E  1 77  ? 66.516  58.245  15.020  1.00 24.47 ? 50  PHE E CD1 1 
ATOM   4907  C  CD2 . PHE E  1 77  ? 66.807  59.683  16.937  1.00 24.87 ? 50  PHE E CD2 1 
ATOM   4908  C  CE1 . PHE E  1 77  ? 67.418  59.034  14.262  1.00 27.25 ? 50  PHE E CE1 1 
ATOM   4909  C  CE2 . PHE E  1 77  ? 67.683  60.495  16.184  1.00 27.35 ? 50  PHE E CE2 1 
ATOM   4910  C  CZ  . PHE E  1 77  ? 67.985  60.165  14.853  1.00 26.60 ? 50  PHE E CZ  1 
ATOM   4911  N  N   . GLY E  1 78  ? 62.702  55.620  16.900  1.00 18.38 ? 51  GLY E N   1 
ATOM   4912  C  CA  . GLY E  1 78  ? 61.946  54.634  17.688  1.00 18.04 ? 51  GLY E CA  1 
ATOM   4913  C  C   . GLY E  1 78  ? 62.897  53.993  18.714  1.00 21.27 ? 51  GLY E C   1 
ATOM   4914  O  O   . GLY E  1 78  ? 62.988  52.763  18.808  1.00 22.24 ? 51  GLY E O   1 
ATOM   4915  N  N   . ASP E  1 79  ? 63.656  54.826  19.406  1.00 22.22 ? 52  ASP E N   1 
ATOM   4916  C  CA  . ASP E  1 79  ? 64.734  54.387  20.322  1.00 22.45 ? 52  ASP E CA  1 
ATOM   4917  C  C   . ASP E  1 79  ? 64.337  54.760  21.767  1.00 22.38 ? 52  ASP E C   1 
ATOM   4918  O  O   . ASP E  1 79  ? 64.287  55.936  22.128  1.00 22.52 ? 52  ASP E O   1 
ATOM   4919  C  CB  . ASP E  1 79  ? 66.037  55.079  19.943  1.00 22.50 ? 52  ASP E CB  1 
ATOM   4920  C  CG  . ASP E  1 79  ? 67.248  54.577  20.765  1.00 28.05 ? 52  ASP E CG  1 
ATOM   4921  O  OD1 . ASP E  1 79  ? 67.053  54.050  21.868  1.00 26.00 ? 52  ASP E OD1 1 
ATOM   4922  O  OD2 . ASP E  1 79  ? 68.391  54.727  20.287  1.00 30.87 ? 52  ASP E OD2 1 
ATOM   4923  N  N   . ASN E  1 80  ? 63.989  53.770  22.577  1.00 22.95 ? 53  ASN E N   1 
ATOM   4924  C  CA  . ASN E  1 80  ? 63.575  54.035  23.959  1.00 25.43 ? 53  ASN E CA  1 
ATOM   4925  C  C   . ASN E  1 80  ? 64.649  53.545  24.957  1.00 26.60 ? 53  ASN E C   1 
ATOM   4926  O  O   . ASN E  1 80  ? 64.375  53.308  26.133  1.00 25.84 ? 53  ASN E O   1 
ATOM   4927  C  CB  . ASN E  1 80  ? 62.294  53.266  24.271  1.00 28.21 ? 53  ASN E CB  1 
ATOM   4928  C  CG  . ASN E  1 80  ? 61.601  53.782  25.536  1.00 38.12 ? 53  ASN E CG  1 
ATOM   4929  O  OD1 . ASN E  1 80  ? 61.484  54.995  25.739  1.00 42.11 ? 53  ASN E OD1 1 
ATOM   4930  N  ND2 . ASN E  1 80  ? 61.122  52.863  26.383  1.00 40.97 ? 53  ASN E ND2 1 
ATOM   4931  N  N   . THR E  1 81  ? 65.872  53.407  24.503  1.00 26.24 ? 54  THR E N   1 
ATOM   4932  C  CA  . THR E  1 81  ? 66.925  52.861  25.379  1.00 26.10 ? 54  THR E CA  1 
ATOM   4933  C  C   . THR E  1 81  ? 67.244  53.759  26.572  1.00 31.93 ? 54  THR E C   1 
ATOM   4934  O  O   . THR E  1 81  ? 67.532  53.262  27.662  1.00 31.38 ? 54  THR E O   1 
ATOM   4935  C  CB  . THR E  1 81  ? 68.205  52.610  24.606  1.00 25.03 ? 54  THR E CB  1 
ATOM   4936  O  OG1 . THR E  1 81  ? 68.657  53.831  24.028  1.00 26.74 ? 54  THR E OG1 1 
ATOM   4937  C  CG2 . THR E  1 81  ? 67.974  51.650  23.523  1.00 25.32 ? 54  THR E CG2 1 
ATOM   4938  N  N   . ALA E  1 82  ? 67.183  55.069  26.412  1.00 26.77 ? 55  ALA E N   1 
ATOM   4939  C  CA  . ALA E  1 82  ? 67.298  55.937  27.575  1.00 28.69 ? 55  ALA E CA  1 
ATOM   4940  C  C   . ALA E  1 82  ? 65.940  56.524  27.950  1.00 29.82 ? 55  ALA E C   1 
ATOM   4941  O  O   . ALA E  1 82  ? 65.885  57.648  28.393  1.00 37.00 ? 55  ALA E O   1 
ATOM   4942  C  CB  . ALA E  1 82  ? 68.285  57.047  27.309  1.00 29.85 ? 55  ALA E CB  1 
ATOM   4943  N  N   . GLY E  1 83  ? 64.863  55.800  27.734  1.00 24.90 ? 56  GLY E N   1 
ATOM   4944  C  CA  . GLY E  1 83  ? 63.544  56.385  27.974  1.00 27.70 ? 56  GLY E CA  1 
ATOM   4945  C  C   . GLY E  1 83  ? 63.174  57.313  26.790  1.00 27.35 ? 56  GLY E C   1 
ATOM   4946  O  O   . GLY E  1 83  ? 63.773  57.231  25.684  1.00 25.88 ? 56  GLY E O   1 
ATOM   4947  N  N   . CYS E  1 84  ? 62.234  58.224  27.023  1.00 23.22 ? 57  CYS E N   1 
ATOM   4948  C  CA  . CYS E  1 84  ? 61.762  59.080  25.940  1.00 23.47 ? 57  CYS E CA  1 
ATOM   4949  C  C   . CYS E  1 84  ? 62.841  59.981  25.344  1.00 22.45 ? 57  CYS E C   1 
ATOM   4950  O  O   . CYS E  1 84  ? 62.686  60.455  24.203  1.00 21.84 ? 57  CYS E O   1 
ATOM   4951  C  CB  . CYS E  1 84  ? 60.546  59.946  26.456  1.00 24.80 ? 57  CYS E CB  1 
ATOM   4952  S  SG  . CYS E  1 84  ? 59.122  58.909  26.958  1.00 32.09 ? 57  CYS E SG  1 
ATOM   4953  N  N   . THR E  1 85  ? 63.869  60.313  26.115  1.00 20.63 ? 58  THR E N   1 
ATOM   4954  C  CA  . THR E  1 85  ? 64.935  61.191  25.658  1.00 25.34 ? 58  THR E CA  1 
ATOM   4955  C  C   . THR E  1 85  ? 65.635  60.658  24.409  1.00 25.97 ? 58  THR E C   1 
ATOM   4956  O  O   . THR E  1 85  ? 66.079  61.434  23.571  1.00 25.40 ? 58  THR E O   1 
ATOM   4957  C  CB  . THR E  1 85  ? 66.028  61.345  26.747  1.00 30.97 ? 58  THR E CB  1 
ATOM   4958  O  OG1 . THR E  1 85  ? 65.427  61.878  27.916  1.00 38.99 ? 58  THR E OG1 1 
ATOM   4959  C  CG2 . THR E  1 85  ? 67.106  62.329  26.327  1.00 33.86 ? 58  THR E CG2 1 
ATOM   4960  N  N   . SER E  1 86  ? 65.757  59.339  24.298  1.00 22.72 ? 59  SER E N   1 
ATOM   4961  C  CA  . SER E  1 86  ? 66.488  58.770  23.155  1.00 24.38 ? 59  SER E CA  1 
ATOM   4962  C  C   . SER E  1 86  ? 65.664  58.807  21.851  1.00 22.69 ? 59  SER E C   1 
ATOM   4963  O  O   . SER E  1 86  ? 66.164  58.446  20.784  1.00 21.32 ? 59  SER E O   1 
ATOM   4964  C  CB  . SER E  1 86  ? 67.067  57.379  23.498  1.00 26.80 ? 59  SER E CB  1 
ATOM   4965  O  OG  . SER E  1 86  ? 66.084  56.624  24.101  1.00 31.28 ? 59  SER E OG  1 
ATOM   4966  N  N   . ALA E  1 87  ? 64.418  59.312  21.902  1.00 20.07 ? 60  ALA E N   1 
ATOM   4967  C  CA  . ALA E  1 87  ? 63.639  59.395  20.635  1.00 19.76 ? 60  ALA E CA  1 
ATOM   4968  C  C   . ALA E  1 87  ? 64.147  60.565  19.788  1.00 19.22 ? 60  ALA E C   1 
ATOM   4969  O  O   . ALA E  1 87  ? 63.753  60.713  18.619  1.00 18.79 ? 60  ALA E O   1 
ATOM   4970  C  CB  . ALA E  1 87  ? 62.126  59.506  20.910  1.00 20.19 ? 60  ALA E CB  1 
ATOM   4971  N  N   . GLY E  1 88  ? 64.999  61.413  20.363  1.00 19.24 ? 61  GLY E N   1 
ATOM   4972  C  CA  . GLY E  1 88  ? 65.649  62.440  19.562  1.00 20.36 ? 61  GLY E CA  1 
ATOM   4973  C  C   . GLY E  1 88  ? 64.634  63.609  19.325  1.00 22.32 ? 61  GLY E C   1 
ATOM   4974  O  O   . GLY E  1 88  ? 63.671  63.745  20.094  1.00 21.28 ? 61  GLY E O   1 
ATOM   4975  N  N   . PRO E  1 89  ? 64.868  64.445  18.293  1.00 22.38 ? 62  PRO E N   1 
ATOM   4976  C  CA  . PRO E  1 89  ? 64.039  65.644  18.059  1.00 20.20 ? 62  PRO E CA  1 
ATOM   4977  C  C   . PRO E  1 89  ? 62.726  65.283  17.294  1.00 19.87 ? 62  PRO E C   1 
ATOM   4978  O  O   . PRO E  1 89  ? 62.492  64.125  16.982  1.00 16.85 ? 62  PRO E O   1 
ATOM   4979  C  CB  . PRO E  1 89  ? 64.961  66.505  17.189  1.00 22.34 ? 62  PRO E CB  1 
ATOM   4980  C  CG  . PRO E  1 89  ? 65.641  65.473  16.309  1.00 24.64 ? 62  PRO E CG  1 
ATOM   4981  C  CD  . PRO E  1 89  ? 65.935  64.309  17.264  1.00 22.83 ? 62  PRO E CD  1 
ATOM   4982  N  N   . HIS E  1 90  ? 61.893  66.267  16.965  1.00 18.55 ? 63  HIS E N   1 
ATOM   4983  C  CA  . HIS E  1 90  ? 60.715  65.972  16.136  1.00 17.50 ? 63  HIS E CA  1 
ATOM   4984  C  C   . HIS E  1 90  ? 61.126  65.378  14.821  1.00 18.07 ? 63  HIS E C   1 
ATOM   4985  O  O   . HIS E  1 90  ? 62.146  65.748  14.256  1.00 20.15 ? 63  HIS E O   1 
ATOM   4986  C  CB  . HIS E  1 90  ? 59.847  67.250  15.905  1.00 17.89 ? 63  HIS E CB  1 
ATOM   4987  C  CG  . HIS E  1 90  ? 59.292  67.818  17.176  1.00 18.42 ? 63  HIS E CG  1 
ATOM   4988  N  ND1 . HIS E  1 90  ? 58.567  68.978  17.238  1.00 19.43 ? 63  HIS E ND1 1 
ATOM   4989  C  CD2 . HIS E  1 90  ? 59.367  67.368  18.464  1.00 20.19 ? 63  HIS E CD2 1 
ATOM   4990  C  CE1 . HIS E  1 90  ? 58.195  69.225  18.479  1.00 17.47 ? 63  HIS E CE1 1 
ATOM   4991  N  NE2 . HIS E  1 90  ? 58.680  68.269  19.251  1.00 19.72 ? 63  HIS E NE2 1 
ATOM   4992  N  N   . PHE E  1 91  ? 60.321  64.471  14.299  1.00 16.41 ? 64  PHE E N   1 
ATOM   4993  C  CA  . PHE E  1 91  ? 60.589  63.892  12.992  1.00 18.09 ? 64  PHE E CA  1 
ATOM   4994  C  C   . PHE E  1 91  ? 60.430  64.995  11.950  1.00 19.04 ? 64  PHE E C   1 
ATOM   4995  O  O   . PHE E  1 91  ? 59.380  65.611  11.850  1.00 17.15 ? 64  PHE E O   1 
ATOM   4996  C  CB  . PHE E  1 91  ? 59.607  62.782  12.767  1.00 17.04 ? 64  PHE E CB  1 
ATOM   4997  C  CG  . PHE E  1 91  ? 59.684  62.133  11.403  1.00 19.27 ? 64  PHE E CG  1 
ATOM   4998  C  CD1 . PHE E  1 91  ? 60.923  61.754  10.847  1.00 19.10 ? 64  PHE E CD1 1 
ATOM   4999  C  CD2 . PHE E  1 91  ? 58.517  61.820  10.744  1.00 17.35 ? 64  PHE E CD2 1 
ATOM   5000  C  CE1 . PHE E  1 91  ? 60.954  61.124  9.574   1.00 20.20 ? 64  PHE E CE1 1 
ATOM   5001  C  CE2 . PHE E  1 91  ? 58.521  61.153  9.496   1.00 20.21 ? 64  PHE E CE2 1 
ATOM   5002  C  CZ  . PHE E  1 91  ? 59.756  60.808  8.910   1.00 19.01 ? 64  PHE E CZ  1 
ATOM   5003  N  N   . ASN E  1 92  ? 61.514  65.274  11.213  1.00 19.46 ? 65  ASN E N   1 
ATOM   5004  C  CA  . ASN E  1 92  ? 61.587  66.490  10.411  1.00 20.03 ? 65  ASN E CA  1 
ATOM   5005  C  C   . ASN E  1 92  ? 62.399  66.158  9.152   1.00 21.29 ? 65  ASN E C   1 
ATOM   5006  O  O   . ASN E  1 92  ? 63.447  66.720  8.974   1.00 23.08 ? 65  ASN E O   1 
ATOM   5007  C  CB  . ASN E  1 92  ? 62.243  67.596  11.228  1.00 18.97 ? 65  ASN E CB  1 
ATOM   5008  C  CG  . ASN E  1 92  ? 62.288  68.962  10.502  1.00 22.36 ? 65  ASN E CG  1 
ATOM   5009  O  OD1 . ASN E  1 92  ? 61.520  69.269  9.577   1.00 22.51 ? 65  ASN E OD1 1 
ATOM   5010  N  ND2 . ASN E  1 92  ? 63.177  69.779  10.960  1.00 21.28 ? 65  ASN E ND2 1 
ATOM   5011  N  N   . PRO E  1 93  ? 61.876  65.281  8.265   1.00 22.91 ? 66  PRO E N   1 
ATOM   5012  C  CA  . PRO E  1 93  ? 62.768  64.921  7.140   1.00 24.83 ? 66  PRO E CA  1 
ATOM   5013  C  C   . PRO E  1 93  ? 62.983  66.065  6.136   1.00 29.02 ? 66  PRO E C   1 
ATOM   5014  O  O   . PRO E  1 93  ? 63.954  66.034  5.393   1.00 29.43 ? 66  PRO E O   1 
ATOM   5015  C  CB  . PRO E  1 93  ? 62.061  63.738  6.496   1.00 21.93 ? 66  PRO E CB  1 
ATOM   5016  C  CG  . PRO E  1 93  ? 60.593  63.924  6.859   1.00 22.45 ? 66  PRO E CG  1 
ATOM   5017  C  CD  . PRO E  1 93  ? 60.661  64.468  8.273   1.00 20.48 ? 66  PRO E CD  1 
ATOM   5018  N  N   . LEU E  1 94  ? 62.123  67.083  6.140   1.00 29.24 ? 67  LEU E N   1 
ATOM   5019  C  CA  . LEU E  1 94  ? 62.347  68.245  5.259   1.00 31.11 ? 67  LEU E CA  1 
ATOM   5020  C  C   . LEU E  1 94  ? 63.043  69.426  5.874   1.00 28.40 ? 67  LEU E C   1 
ATOM   5021  O  O   . LEU E  1 94  ? 63.123  70.495  5.256   1.00 29.71 ? 67  LEU E O   1 
ATOM   5022  C  CB  . LEU E  1 94  ? 61.026  68.681  4.654   1.00 31.21 ? 67  LEU E CB  1 
ATOM   5023  C  CG  . LEU E  1 94  ? 60.390  67.519  3.908   1.00 34.74 ? 67  LEU E CG  1 
ATOM   5024  C  CD1 . LEU E  1 94  ? 58.934  67.793  3.590   1.00 32.29 ? 67  LEU E CD1 1 
ATOM   5025  C  CD2 . LEU E  1 94  ? 61.217  67.259  2.640   1.00 40.31 ? 67  LEU E CD2 1 
ATOM   5026  N  N   . SER E  1 95  ? 63.535  69.271  7.096   1.00 27.18 ? 68  SER E N   1 
ATOM   5027  C  CA  . SER E  1 95  ? 64.332  70.302  7.741   1.00 29.21 ? 68  SER E CA  1 
ATOM   5028  C  C   . SER E  1 95  ? 63.615  71.648  7.771   1.00 30.10 ? 68  SER E C   1 
ATOM   5029  O  O   . SER E  1 95  ? 64.202  72.664  7.424   1.00 29.28 ? 68  SER E O   1 
ATOM   5030  C  CB  . SER E  1 95  ? 65.730  70.464  7.089   1.00 35.32 ? 68  SER E CB  1 
ATOM   5031  O  OG  . SER E  1 95  ? 66.440  69.244  7.221   1.00 36.77 ? 68  SER E OG  1 
ATOM   5032  N  N   . ARG E  1 96  ? 62.366  71.650  8.228   1.00 25.28 ? 69  ARG E N   1 
ATOM   5033  C  CA  . ARG E  1 96  ? 61.620  72.877  8.395   1.00 24.44 ? 69  ARG E CA  1 
ATOM   5034  C  C   . ARG E  1 96  ? 61.701  73.311  9.829   1.00 23.81 ? 69  ARG E C   1 
ATOM   5035  O  O   . ARG E  1 96  ? 62.271  72.627  10.656  1.00 21.91 ? 69  ARG E O   1 
ATOM   5036  C  CB  . ARG E  1 96  ? 60.143  72.648  8.001   1.00 24.13 ? 69  ARG E CB  1 
ATOM   5037  C  CG  . ARG E  1 96  ? 59.949  72.095  6.599   1.00 29.76 ? 69  ARG E CG  1 
ATOM   5038  C  CD  . ARG E  1 96  ? 60.417  73.041  5.502   1.00 35.19 ? 69  ARG E CD  1 
ATOM   5039  N  NE  . ARG E  1 96  ? 60.222  72.410  4.181   1.00 43.72 ? 69  ARG E NE  1 
ATOM   5040  C  CZ  . ARG E  1 96  ? 61.176  72.296  3.229   1.00 47.08 ? 69  ARG E CZ  1 
ATOM   5041  N  NH1 . ARG E  1 96  ? 62.405  72.801  3.408   1.00 39.92 ? 69  ARG E NH1 1 
ATOM   5042  N  NH2 . ARG E  1 96  ? 60.908  71.666  2.080   1.00 44.43 ? 69  ARG E NH2 1 
ATOM   5043  N  N   . LYS E  1 97  ? 61.155  74.485  10.120  1.00 22.12 ? 70  LYS E N   1 
ATOM   5044  C  CA  . LYS E  1 97  ? 61.012  74.931  11.499  1.00 23.12 ? 70  LYS E CA  1 
ATOM   5045  C  C   . LYS E  1 97  ? 59.721  74.330  12.058  1.00 21.70 ? 70  LYS E C   1 
ATOM   5046  O  O   . LYS E  1 97  ? 58.813  73.967  11.289  1.00 21.01 ? 70  LYS E O   1 
ATOM   5047  C  CB  . LYS E  1 97  ? 60.896  76.447  11.540  1.00 26.86 ? 70  LYS E CB  1 
ATOM   5048  C  CG  . LYS E  1 97  ? 62.229  77.127  11.181  1.00 33.24 ? 70  LYS E CG  1 
ATOM   5049  C  CD  . LYS E  1 97  ? 62.032  78.632  11.078  1.00 42.65 ? 70  LYS E CD  1 
ATOM   5050  C  CE  . LYS E  1 97  ? 63.396  79.340  10.956  1.00 51.60 ? 70  LYS E CE  1 
ATOM   5051  N  NZ  . LYS E  1 97  ? 63.247  80.828  10.809  1.00 59.21 ? 70  LYS E NZ  1 
ATOM   5052  N  N   . HIS E  1 98  ? 59.637  74.295  13.385  1.00 20.61 ? 71  HIS E N   1 
ATOM   5053  C  CA  . HIS E  1 98  ? 58.443  73.777  14.071  1.00 20.46 ? 71  HIS E CA  1 
ATOM   5054  C  C   . HIS E  1 98  ? 57.169  74.628  13.781  1.00 19.62 ? 71  HIS E C   1 
ATOM   5055  O  O   . HIS E  1 98  ? 57.238  75.873  13.740  1.00 21.00 ? 71  HIS E O   1 
ATOM   5056  C  CB  . HIS E  1 98  ? 58.734  73.732  15.589  1.00 17.80 ? 71  HIS E CB  1 
ATOM   5057  C  CG  . HIS E  1 98  ? 57.564  73.262  16.392  1.00 19.11 ? 71  HIS E CG  1 
ATOM   5058  N  ND1 . HIS E  1 98  ? 57.215  71.939  16.501  1.00 19.71 ? 71  HIS E ND1 1 
ATOM   5059  C  CD2 . HIS E  1 98  ? 56.642  73.946  17.105  1.00 18.02 ? 71  HIS E CD2 1 
ATOM   5060  C  CE1 . HIS E  1 98  ? 56.123  71.818  17.228  1.00 18.59 ? 71  HIS E CE1 1 
ATOM   5061  N  NE2 . HIS E  1 98  ? 55.782  73.023  17.647  1.00 19.13 ? 71  HIS E NE2 1 
ATOM   5062  N  N   . GLY E  1 99  ? 56.028  73.973  13.551  1.00 15.99 ? 72  GLY E N   1 
ATOM   5063  C  CA  . GLY E  1 99  ? 54.761  74.694  13.361  1.00 18.74 ? 72  GLY E CA  1 
ATOM   5064  C  C   . GLY E  1 99  ? 53.630  73.915  13.952  1.00 19.24 ? 72  GLY E C   1 
ATOM   5065  O  O   . GLY E  1 99  ? 53.868  72.907  14.643  1.00 18.40 ? 72  GLY E O   1 
ATOM   5066  N  N   . GLY E  1 100 ? 52.399  74.394  13.752  1.00 17.43 ? 73  GLY E N   1 
ATOM   5067  C  CA  . GLY E  1 100 ? 51.217  73.622  14.117  1.00 17.71 ? 73  GLY E CA  1 
ATOM   5068  C  C   . GLY E  1 100 ? 50.877  72.738  12.924  1.00 17.85 ? 73  GLY E C   1 
ATOM   5069  O  O   . GLY E  1 100 ? 51.418  72.960  11.829  1.00 20.88 ? 73  GLY E O   1 
ATOM   5070  N  N   . PRO E  1 101 ? 49.942  71.805  13.110  1.00 18.44 ? 74  PRO E N   1 
ATOM   5071  C  CA  . PRO E  1 101 ? 49.601  70.884  12.032  1.00 18.66 ? 74  PRO E CA  1 
ATOM   5072  C  C   . PRO E  1 101 ? 49.000  71.575  10.811  1.00 20.63 ? 74  PRO E C   1 
ATOM   5073  O  O   . PRO E  1 101 ? 49.131  71.065  9.721   1.00 19.44 ? 74  PRO E O   1 
ATOM   5074  C  CB  . PRO E  1 101 ? 48.587  69.905  12.692  1.00 19.10 ? 74  PRO E CB  1 
ATOM   5075  C  CG  . PRO E  1 101 ? 48.236  70.473  14.016  1.00 17.94 ? 74  PRO E CG  1 
ATOM   5076  C  CD  . PRO E  1 101 ? 49.387  71.369  14.410  1.00 16.32 ? 74  PRO E CD  1 
ATOM   5077  N  N   . LYS E  1 102 ? 48.367  72.737  11.000  1.00 22.83 ? 75  LYS E N   1 
ATOM   5078  C  CA  . LYS E  1 102 ? 47.802  73.459  9.884   1.00 24.81 ? 75  LYS E CA  1 
ATOM   5079  C  C   . LYS E  1 102 ? 48.790  74.324  9.133   1.00 25.50 ? 75  LYS E C   1 
ATOM   5080  O  O   . LYS E  1 102 ? 48.411  74.892  8.085   1.00 27.32 ? 75  LYS E O   1 
ATOM   5081  C  CB  . LYS E  1 102 ? 46.615  74.330  10.358  1.00 28.88 ? 75  LYS E CB  1 
ATOM   5082  C  CG  . LYS E  1 102 ? 45.498  73.537  11.061  1.00 30.77 ? 75  LYS E CG  1 
ATOM   5083  C  CD  . LYS E  1 102 ? 44.623  74.504  11.873  1.00 39.64 ? 75  LYS E CD  1 
ATOM   5084  C  CE  . LYS E  1 102 ? 43.968  75.587  10.982  1.00 37.18 ? 75  LYS E CE  1 
ATOM   5085  N  NZ  . LYS E  1 102 ? 43.602  76.804  11.788  1.00 40.72 ? 75  LYS E NZ  1 
ATOM   5086  N  N   . ASP E  1 103 ? 50.024  74.467  9.618   1.00 24.42 ? 76  ASP E N   1 
ATOM   5087  C  CA  . ASP E  1 103 ? 51.033  75.296  8.925   1.00 27.21 ? 76  ASP E CA  1 
ATOM   5088  C  C   . ASP E  1 103 ? 51.741  74.620  7.778   1.00 28.32 ? 76  ASP E C   1 
ATOM   5089  O  O   . ASP E  1 103 ? 52.057  73.427  7.869   1.00 24.75 ? 76  ASP E O   1 
ATOM   5090  C  CB  . ASP E  1 103 ? 52.113  75.747  9.904   1.00 31.11 ? 76  ASP E CB  1 
ATOM   5091  C  CG  . ASP E  1 103 ? 51.576  76.655  10.930  1.00 34.82 ? 76  ASP E CG  1 
ATOM   5092  O  OD1 . ASP E  1 103 ? 50.741  77.490  10.542  1.00 37.13 ? 76  ASP E OD1 1 
ATOM   5093  O  OD2 . ASP E  1 103 ? 51.922  76.504  12.120  1.00 34.91 ? 76  ASP E OD2 1 
ATOM   5094  N  N   . GLU E  1 104 ? 52.044  75.378  6.714   1.00 29.24 ? 77  GLU E N   1 
ATOM   5095  C  CA  . GLU E  1 104 ? 52.875  74.852  5.619   1.00 33.08 ? 77  GLU E CA  1 
ATOM   5096  C  C   . GLU E  1 104 ? 54.273  74.576  6.136   1.00 31.95 ? 77  GLU E C   1 
ATOM   5097  O  O   . GLU E  1 104 ? 54.851  73.467  5.904   1.00 31.33 ? 77  GLU E O   1 
ATOM   5098  C  CB  . GLU E  1 104 ? 52.948  75.829  4.428   1.00 41.48 ? 77  GLU E CB  1 
ATOM   5099  C  CG  . GLU E  1 104 ? 53.740  75.268  3.241   1.00 53.70 ? 77  GLU E CG  1 
ATOM   5100  C  CD  . GLU E  1 104 ? 53.171  73.954  2.691   1.00 64.57 ? 77  GLU E CD  1 
ATOM   5101  O  OE1 . GLU E  1 104 ? 51.938  73.715  2.816   1.00 67.47 ? 77  GLU E OE1 1 
ATOM   5102  O  OE2 . GLU E  1 104 ? 53.952  73.150  2.112   1.00 72.45 ? 77  GLU E OE2 1 
ATOM   5103  N  N   . GLU E  1 105 ? 54.776  75.527  6.933   1.00 26.79 ? 78  GLU E N   1 
ATOM   5104  C  CA  . GLU E  1 105 ? 56.077  75.366  7.590   1.00 25.74 ? 78  GLU E CA  1 
ATOM   5105  C  C   . GLU E  1 105 ? 55.853  74.597  8.910   1.00 21.34 ? 78  GLU E C   1 
ATOM   5106  O  O   . GLU E  1 105 ? 55.458  75.175  9.939   1.00 20.35 ? 78  GLU E O   1 
ATOM   5107  C  CB  . GLU E  1 105 ? 56.753  76.710  7.833   1.00 26.99 ? 78  GLU E CB  1 
ATOM   5108  C  CG  . GLU E  1 105 ? 58.147  76.630  8.449   1.00 30.62 ? 78  GLU E CG  1 
ATOM   5109  C  CD  . GLU E  1 105 ? 59.288  76.270  7.471   1.00 35.64 ? 78  GLU E CD  1 
ATOM   5110  O  OE1 . GLU E  1 105 ? 59.074  76.212  6.223   1.00 41.67 ? 78  GLU E OE1 1 
ATOM   5111  O  OE2 . GLU E  1 105 ? 60.433  76.041  7.947   1.00 35.09 ? 78  GLU E OE2 1 
ATOM   5112  N  N   . ARG E  1 106 ? 56.143  73.303  8.876   1.00 20.69 ? 79  ARG E N   1 
ATOM   5113  C  CA  . ARG E  1 106 ? 56.015  72.457  10.089  1.00 18.38 ? 79  ARG E CA  1 
ATOM   5114  C  C   . ARG E  1 106 ? 56.932  71.266  9.915   1.00 20.08 ? 79  ARG E C   1 
ATOM   5115  O  O   . ARG E  1 106 ? 57.333  70.945  8.792   1.00 22.26 ? 79  ARG E O   1 
ATOM   5116  C  CB  . ARG E  1 106 ? 54.575  71.978  10.304  1.00 17.70 ? 79  ARG E CB  1 
ATOM   5117  C  CG  . ARG E  1 106 ? 53.998  71.208  9.099   1.00 18.16 ? 79  ARG E CG  1 
ATOM   5118  C  CD  . ARG E  1 106 ? 52.686  70.537  9.429   1.00 18.72 ? 79  ARG E CD  1 
ATOM   5119  N  NE  . ARG E  1 106 ? 52.888  69.176  10.009  1.00 19.11 ? 79  ARG E NE  1 
ATOM   5120  C  CZ  . ARG E  1 106 ? 51.922  68.270  10.073  1.00 18.51 ? 79  ARG E CZ  1 
ATOM   5121  N  NH1 . ARG E  1 106 ? 50.695  68.625  9.712   1.00 16.98 ? 79  ARG E NH1 1 
ATOM   5122  N  NH2 . ARG E  1 106 ? 52.170  67.012  10.526  1.00 17.80 ? 79  ARG E NH2 1 
ATOM   5123  N  N   . HIS E  1 107 ? 57.298  70.631  11.020  1.00 18.51 ? 80  HIS E N   1 
ATOM   5124  C  CA  . HIS E  1 107 ? 57.904  69.289  10.952  1.00 17.28 ? 80  HIS E CA  1 
ATOM   5125  C  C   . HIS E  1 107 ? 56.828  68.291  10.562  1.00 17.10 ? 80  HIS E C   1 
ATOM   5126  O  O   . HIS E  1 107 ? 55.624  68.468  10.859  1.00 16.64 ? 80  HIS E O   1 
ATOM   5127  C  CB  . HIS E  1 107 ? 58.440  68.908  12.325  1.00 15.85 ? 80  HIS E CB  1 
ATOM   5128  C  CG  . HIS E  1 107 ? 59.413  69.887  12.886  1.00 16.63 ? 80  HIS E CG  1 
ATOM   5129  N  ND1 . HIS E  1 107 ? 59.522  70.130  14.228  1.00 16.13 ? 80  HIS E ND1 1 
ATOM   5130  C  CD2 . HIS E  1 107 ? 60.341  70.681  12.283  1.00 16.72 ? 80  HIS E CD2 1 
ATOM   5131  C  CE1 . HIS E  1 107 ? 60.510  70.978  14.449  1.00 17.70 ? 80  HIS E CE1 1 
ATOM   5132  N  NE2 . HIS E  1 107 ? 61.014  71.329  13.276  1.00 18.18 ? 80  HIS E NE2 1 
ATOM   5133  N  N   . VAL E  1 108 ? 57.232  67.204  9.890   1.00 16.76 ? 81  VAL E N   1 
ATOM   5134  C  CA  . VAL E  1 108 ? 56.246  66.149  9.609   1.00 16.51 ? 81  VAL E CA  1 
ATOM   5135  C  C   . VAL E  1 108 ? 55.612  65.646  10.938  1.00 14.82 ? 81  VAL E C   1 
ATOM   5136  O  O   . VAL E  1 108 ? 54.420  65.359  10.992  1.00 15.20 ? 81  VAL E O   1 
ATOM   5137  C  CB  . VAL E  1 108 ? 56.901  64.962  8.859   1.00 16.86 ? 81  VAL E CB  1 
ATOM   5138  C  CG1 . VAL E  1 108 ? 55.945  63.748  8.860   1.00 16.54 ? 81  VAL E CG1 1 
ATOM   5139  C  CG2 . VAL E  1 108 ? 57.236  65.436  7.417   1.00 16.80 ? 81  VAL E CG2 1 
ATOM   5140  N  N   . GLY E  1 109 ? 56.415  65.582  11.991  1.00 15.90 ? 82  GLY E N   1 
ATOM   5141  C  CA  . GLY E  1 109 ? 55.953  65.126  13.330  1.00 16.36 ? 82  GLY E CA  1 
ATOM   5142  C  C   . GLY E  1 109 ? 55.031  66.080  14.138  1.00 18.15 ? 82  GLY E C   1 
ATOM   5143  O  O   . GLY E  1 109 ? 54.606  65.739  15.220  1.00 15.99 ? 82  GLY E O   1 
ATOM   5144  N  N   . ASP E  1 110 ? 54.665  67.241  13.580  1.00 17.01 ? 83  ASP E N   1 
ATOM   5145  C  CA  . ASP E  1 110 ? 53.993  68.318  14.372  1.00 15.99 ? 83  ASP E CA  1 
ATOM   5146  C  C   . ASP E  1 110 ? 52.490  68.084  14.356  1.00 16.65 ? 83  ASP E C   1 
ATOM   5147  O  O   . ASP E  1 110 ? 51.773  68.604  13.491  1.00 18.55 ? 83  ASP E O   1 
ATOM   5148  C  CB  . ASP E  1 110 ? 54.375  69.687  13.748  1.00 16.13 ? 83  ASP E CB  1 
ATOM   5149  C  CG  . ASP E  1 110 ? 55.767  70.099  14.125  1.00 16.50 ? 83  ASP E CG  1 
ATOM   5150  O  OD1 . ASP E  1 110 ? 56.383  69.429  15.035  1.00 15.41 ? 83  ASP E OD1 1 
ATOM   5151  O  OD2 . ASP E  1 110 ? 56.317  71.067  13.567  1.00 16.57 ? 83  ASP E OD2 1 
ATOM   5152  N  N   . LEU E  1 111 ? 51.982  67.332  15.338  1.00 15.09 ? 84  LEU E N   1 
ATOM   5153  C  CA  . LEU E  1 111 ? 50.556  67.063  15.369  1.00 15.96 ? 84  LEU E CA  1 
ATOM   5154  C  C   . LEU E  1 111 ? 49.834  68.025  16.340  1.00 16.21 ? 84  LEU E C   1 
ATOM   5155  O  O   . LEU E  1 111 ? 48.650  67.797  16.652  1.00 19.60 ? 84  LEU E O   1 
ATOM   5156  C  CB  . LEU E  1 111 ? 50.251  65.598  15.766  1.00 16.28 ? 84  LEU E CB  1 
ATOM   5157  C  CG  . LEU E  1 111 ? 50.883  64.608  14.764  1.00 17.82 ? 84  LEU E CG  1 
ATOM   5158  C  CD1 . LEU E  1 111 ? 50.652  63.162  15.229  1.00 18.54 ? 84  LEU E CD1 1 
ATOM   5159  C  CD2 . LEU E  1 111 ? 50.256  64.737  13.395  1.00 19.15 ? 84  LEU E CD2 1 
ATOM   5160  N  N   . GLY E  1 112 ? 50.538  69.026  16.845  1.00 15.31 ? 85  GLY E N   1 
ATOM   5161  C  CA  . GLY E  1 112 ? 49.837  70.065  17.634  1.00 17.11 ? 85  GLY E CA  1 
ATOM   5162  C  C   . GLY E  1 112 ? 49.623  69.635  19.073  1.00 18.67 ? 85  GLY E C   1 
ATOM   5163  O  O   . GLY E  1 112 ? 50.526  69.029  19.694  1.00 16.47 ? 85  GLY E O   1 
ATOM   5164  N  N   . ASN E  1 113 ? 48.483  70.039  19.639  1.00 15.61 ? 86  ASN E N   1 
ATOM   5165  C  CA  . ASN E  1 113 ? 48.176  69.758  21.039  1.00 15.61 ? 86  ASN E CA  1 
ATOM   5166  C  C   . ASN E  1 113 ? 47.048  68.747  21.139  1.00 14.30 ? 86  ASN E C   1 
ATOM   5167  O  O   . ASN E  1 113 ? 46.213  68.667  20.235  1.00 14.73 ? 86  ASN E O   1 
ATOM   5168  C  CB  . ASN E  1 113 ? 47.714  71.070  21.732  1.00 16.41 ? 86  ASN E CB  1 
ATOM   5169  C  CG  . ASN E  1 113 ? 48.871  71.984  22.003  1.00 16.51 ? 86  ASN E CG  1 
ATOM   5170  O  OD1 . ASN E  1 113 ? 49.816  71.580  22.661  1.00 17.64 ? 86  ASN E OD1 1 
ATOM   5171  N  ND2 . ASN E  1 113 ? 48.833  73.219  21.471  1.00 15.56 ? 86  ASN E ND2 1 
ATOM   5172  N  N   . VAL E  1 114 ? 47.014  68.031  22.256  1.00 14.22 ? 87  VAL E N   1 
ATOM   5173  C  CA  . VAL E  1 114 ? 45.818  67.308  22.661  1.00 15.36 ? 87  VAL E CA  1 
ATOM   5174  C  C   . VAL E  1 114 ? 45.362  67.962  23.974  1.00 16.49 ? 87  VAL E C   1 
ATOM   5175  O  O   . VAL E  1 114 ? 46.158  68.585  24.641  1.00 18.00 ? 87  VAL E O   1 
ATOM   5176  C  CB  . VAL E  1 114 ? 46.059  65.770  22.806  1.00 16.99 ? 87  VAL E CB  1 
ATOM   5177  C  CG1 . VAL E  1 114 ? 46.488  65.161  21.455  1.00 15.94 ? 87  VAL E CG1 1 
ATOM   5178  C  CG2 . VAL E  1 114 ? 47.092  65.461  23.899  1.00 15.13 ? 87  VAL E CG2 1 
ATOM   5179  N  N   . THR E  1 115 ? 44.094  67.776  24.332  1.00 16.61 ? 88  THR E N   1 
ATOM   5180  C  CA  . THR E  1 115 ? 43.474  68.459  25.486  1.00 18.25 ? 88  THR E CA  1 
ATOM   5181  C  C   . THR E  1 115 ? 43.044  67.436  26.471  1.00 17.07 ? 88  THR E C   1 
ATOM   5182  O  O   . THR E  1 115 ? 42.221  66.579  26.131  1.00 19.24 ? 88  THR E O   1 
ATOM   5183  C  CB  . THR E  1 115 ? 42.219  69.277  25.029  1.00 20.88 ? 88  THR E CB  1 
ATOM   5184  O  OG1 . THR E  1 115 ? 42.661  70.245  24.066  1.00 18.69 ? 88  THR E OG1 1 
ATOM   5185  C  CG2 . THR E  1 115 ? 41.538  70.042  26.240  1.00 21.35 ? 88  THR E CG2 1 
ATOM   5186  N  N   . ALA E  1 116 ? 43.607  67.502  27.676  1.00 17.91 ? 89  ALA E N   1 
ATOM   5187  C  CA  . ALA E  1 116 ? 43.143  66.612  28.742  1.00 18.36 ? 89  ALA E CA  1 
ATOM   5188  C  C   . ALA E  1 116 ? 42.003  67.348  29.536  1.00 21.75 ? 89  ALA E C   1 
ATOM   5189  O  O   . ALA E  1 116 ? 42.137  68.536  29.834  1.00 21.01 ? 89  ALA E O   1 
ATOM   5190  C  CB  . ALA E  1 116 ? 44.295  66.296  29.697  1.00 18.84 ? 89  ALA E CB  1 
ATOM   5191  N  N   . ASP E  1 117 ? 40.955  66.607  29.855  1.00 22.62 ? 90  ASP E N   1 
ATOM   5192  C  CA  . ASP E  1 117 ? 39.845  67.119  30.653  1.00 28.40 ? 90  ASP E CA  1 
ATOM   5193  C  C   . ASP E  1 117 ? 40.164  67.165  32.138  1.00 28.63 ? 90  ASP E C   1 
ATOM   5194  O  O   . ASP E  1 117 ? 41.273  66.823  32.581  1.00 24.13 ? 90  ASP E O   1 
ATOM   5195  C  CB  . ASP E  1 117 ? 38.574  66.319  30.358  1.00 28.76 ? 90  ASP E CB  1 
ATOM   5196  C  CG  . ASP E  1 117 ? 38.629  64.833  30.834  1.00 29.33 ? 90  ASP E CG  1 
ATOM   5197  O  OD1 . ASP E  1 117 ? 39.355  64.430  31.752  1.00 30.09 ? 90  ASP E OD1 1 
ATOM   5198  O  OD2 . ASP E  1 117 ? 37.886  64.048  30.274  1.00 33.68 ? 90  ASP E OD2 1 
ATOM   5199  N  N   . LYS E  1 118 ? 39.191  67.589  32.944  1.00 29.90 ? 91  LYS E N   1 
ATOM   5200  C  CA  . LYS E  1 118 ? 39.433  67.714  34.391  1.00 31.24 ? 91  LYS E CA  1 
ATOM   5201  C  C   . LYS E  1 118 ? 39.665  66.353  35.084  1.00 30.33 ? 91  LYS E C   1 
ATOM   5202  O  O   . LYS E  1 118 ? 40.189  66.330  36.188  1.00 33.29 ? 91  LYS E O   1 
ATOM   5203  C  CB  . LYS E  1 118 ? 38.233  68.410  35.065  1.00 37.87 ? 91  LYS E CB  1 
ATOM   5204  C  CG  . LYS E  1 118 ? 36.962  67.599  34.829  1.00 41.88 ? 91  LYS E CG  1 
ATOM   5205  C  CD  . LYS E  1 118 ? 35.711  68.439  34.581  1.00 53.16 ? 91  LYS E CD  1 
ATOM   5206  C  CE  . LYS E  1 118 ? 35.008  68.712  35.895  1.00 51.73 ? 91  LYS E CE  1 
ATOM   5207  N  NZ  . LYS E  1 118 ? 34.754  67.413  36.583  1.00 55.03 ? 91  LYS E NZ  1 
ATOM   5208  N  N   . ASP E  1 119 ? 39.295  65.230  34.453  1.00 27.57 ? 92  ASP E N   1 
ATOM   5209  C  CA  . ASP E  1 119 ? 39.614  63.912  35.021  1.00 33.38 ? 92  ASP E CA  1 
ATOM   5210  C  C   . ASP E  1 119 ? 40.964  63.296  34.562  1.00 32.53 ? 92  ASP E C   1 
ATOM   5211  O  O   . ASP E  1 119 ? 41.246  62.128  34.824  1.00 32.39 ? 92  ASP E O   1 
ATOM   5212  C  CB  . ASP E  1 119 ? 38.473  62.971  34.716  1.00 34.03 ? 92  ASP E CB  1 
ATOM   5213  C  CG  . ASP E  1 119 ? 37.193  63.392  35.454  1.00 41.86 ? 92  ASP E CG  1 
ATOM   5214  O  OD1 . ASP E  1 119 ? 37.314  63.782  36.635  1.00 42.91 ? 92  ASP E OD1 1 
ATOM   5215  O  OD2 . ASP E  1 119 ? 36.108  63.391  34.850  1.00 41.80 ? 92  ASP E OD2 1 
ATOM   5216  N  N   . GLY E  1 120 ? 41.744  64.096  33.858  1.00 27.26 ? 93  GLY E N   1 
ATOM   5217  C  CA  . GLY E  1 120 ? 43.085  63.753  33.439  1.00 26.12 ? 93  GLY E CA  1 
ATOM   5218  C  C   . GLY E  1 120 ? 43.145  62.964  32.128  1.00 25.10 ? 93  GLY E C   1 
ATOM   5219  O  O   . GLY E  1 120 ? 44.206  62.443  31.791  1.00 24.44 ? 93  GLY E O   1 
ATOM   5220  N  N   . VAL E  1 121 ? 42.046  62.919  31.381  1.00 22.31 ? 94  VAL E N   1 
ATOM   5221  C  CA  . VAL E  1 121 ? 41.978  62.112  30.163  1.00 22.83 ? 94  VAL E CA  1 
ATOM   5222  C  C   . VAL E  1 121 ? 41.935  62.976  28.908  1.00 23.28 ? 94  VAL E C   1 
ATOM   5223  O  O   . VAL E  1 121 ? 41.134  63.916  28.842  1.00 20.81 ? 94  VAL E O   1 
ATOM   5224  C  CB  . VAL E  1 121 ? 40.751  61.176  30.183  1.00 26.24 ? 94  VAL E CB  1 
ATOM   5225  C  CG1 . VAL E  1 121 ? 40.655  60.371  28.902  1.00 23.54 ? 94  VAL E CG1 1 
ATOM   5226  C  CG2 . VAL E  1 121 ? 40.814  60.264  31.406  1.00 26.27 ? 94  VAL E CG2 1 
ATOM   5227  N  N   . ALA E  1 122 ? 42.831  62.690  27.951  1.00 18.78 ? 95  ALA E N   1 
ATOM   5228  C  CA  . ALA E  1 122 ? 42.788  63.321  26.646  1.00 18.24 ? 95  ALA E CA  1 
ATOM   5229  C  C   . ALA E  1 122 ? 42.204  62.265  25.684  1.00 21.48 ? 95  ALA E C   1 
ATOM   5230  O  O   . ALA E  1 122 ? 42.851  61.214  25.448  1.00 21.67 ? 95  ALA E O   1 
ATOM   5231  C  CB  . ALA E  1 122 ? 44.220  63.729  26.221  1.00 17.18 ? 95  ALA E CB  1 
ATOM   5232  N  N   . ASP E  1 123 ? 40.995  62.505  25.161  1.00 21.02 ? 96  ASP E N   1 
ATOM   5233  C  CA  . ASP E  1 123 ? 40.434  61.652  24.128  1.00 23.58 ? 96  ASP E CA  1 
ATOM   5234  C  C   . ASP E  1 123 ? 40.830  62.209  22.773  1.00 22.54 ? 96  ASP E C   1 
ATOM   5235  O  O   . ASP E  1 123 ? 40.219  63.143  22.236  1.00 25.68 ? 96  ASP E O   1 
ATOM   5236  C  CB  . ASP E  1 123 ? 38.924  61.514  24.229  1.00 24.43 ? 96  ASP E CB  1 
ATOM   5237  C  CG  . ASP E  1 123 ? 38.489  60.740  25.497  1.00 32.81 ? 96  ASP E CG  1 
ATOM   5238  O  OD1 . ASP E  1 123 ? 37.677  61.325  26.263  1.00 33.84 ? 96  ASP E OD1 1 
ATOM   5239  O  OD2 . ASP E  1 123 ? 38.965  59.583  25.736  1.00 33.26 ? 96  ASP E OD2 1 
ATOM   5240  N  N   . VAL E  1 124 ? 41.845  61.599  22.195  1.00 20.27 ? 97  VAL E N   1 
ATOM   5241  C  CA  . VAL E  1 124 ? 42.521  62.172  21.051  1.00 17.54 ? 97  VAL E CA  1 
ATOM   5242  C  C   . VAL E  1 124 ? 41.732  61.868  19.814  1.00 20.31 ? 97  VAL E C   1 
ATOM   5243  O  O   . VAL E  1 124 ? 41.292  60.730  19.621  1.00 20.31 ? 97  VAL E O   1 
ATOM   5244  C  CB  . VAL E  1 124 ? 43.950  61.607  20.940  1.00 17.46 ? 97  VAL E CB  1 
ATOM   5245  C  CG1 . VAL E  1 124 ? 44.618  62.094  19.641  1.00 16.05 ? 97  VAL E CG1 1 
ATOM   5246  C  CG2 . VAL E  1 124 ? 44.811  61.983  22.152  1.00 16.42 ? 97  VAL E CG2 1 
ATOM   5247  N  N   . SER E  1 125 ? 41.542  62.880  18.975  1.00 19.00 ? 98  SER E N   1 
ATOM   5248  C  CA  . SER E  1 125 ? 40.960  62.652  17.693  1.00 20.10 ? 98  SER E CA  1 
ATOM   5249  C  C   . SER E  1 125 ? 41.499  63.691  16.716  1.00 21.80 ? 98  SER E C   1 
ATOM   5250  O  O   . SER E  1 125 ? 41.127  64.851  16.768  1.00 20.04 ? 98  SER E O   1 
ATOM   5251  C  CB  . SER E  1 125 ? 39.435  62.751  17.817  1.00 26.76 ? 98  SER E CB  1 
ATOM   5252  O  OG  . SER E  1 125 ? 38.850  62.119  16.715  1.00 31.38 ? 98  SER E OG  1 
ATOM   5253  N  N   . ILE E  1 126 ? 42.339  63.269  15.774  1.00 19.49 ? 99  ILE E N   1 
ATOM   5254  C  CA  . ILE E  1 126 ? 43.075  64.177  14.898  1.00 21.92 ? 99  ILE E CA  1 
ATOM   5255  C  C   . ILE E  1 126 ? 43.021  63.545  13.517  1.00 21.59 ? 99  ILE E C   1 
ATOM   5256  O  O   . ILE E  1 126 ? 42.952  62.322  13.417  1.00 22.97 ? 99  ILE E O   1 
ATOM   5257  C  CB  . ILE E  1 126 ? 44.527  64.253  15.452  1.00 21.53 ? 99  ILE E CB  1 
ATOM   5258  C  CG1 . ILE E  1 126 ? 44.550  65.192  16.681  1.00 25.46 ? 99  ILE E CG1 1 
ATOM   5259  C  CG2 . ILE E  1 126 ? 45.572  64.655  14.403  1.00 24.26 ? 99  ILE E CG2 1 
ATOM   5260  C  CD1 . ILE E  1 126 ? 45.882  65.110  17.465  1.00 24.86 ? 99  ILE E CD1 1 
ATOM   5261  N  N   . GLU E  1 127 ? 42.992  64.358  12.459  1.00 18.86 ? 100 GLU E N   1 
ATOM   5262  C  CA  . GLU E  1 127 ? 43.200  63.826  11.135  1.00 22.66 ? 100 GLU E CA  1 
ATOM   5263  C  C   . GLU E  1 127 ? 44.332  64.654  10.527  1.00 22.70 ? 100 GLU E C   1 
ATOM   5264  O  O   . GLU E  1 127 ? 44.365  65.894  10.654  1.00 23.52 ? 100 GLU E O   1 
ATOM   5265  C  CB  . GLU E  1 127 ? 41.899  63.926  10.337  1.00 28.77 ? 100 GLU E CB  1 
ATOM   5266  C  CG  . GLU E  1 127 ? 42.126  63.574  8.885   1.00 37.04 ? 100 GLU E CG  1 
ATOM   5267  C  CD  . GLU E  1 127 ? 40.870  63.644  8.044   1.00 47.08 ? 100 GLU E CD  1 
ATOM   5268  O  OE1 . GLU E  1 127 ? 39.925  62.883  8.350   1.00 45.06 ? 100 GLU E OE1 1 
ATOM   5269  O  OE2 . GLU E  1 127 ? 40.866  64.460  7.074   1.00 52.43 ? 100 GLU E OE2 1 
ATOM   5270  N  N   . ASP E  1 128 ? 45.301  63.978  9.934   1.00 19.79 ? 101 ASP E N   1 
ATOM   5271  C  CA  . ASP E  1 128 ? 46.472  64.657  9.441   1.00 20.80 ? 101 ASP E CA  1 
ATOM   5272  C  C   . ASP E  1 128 ? 46.910  64.122  8.079   1.00 22.88 ? 101 ASP E C   1 
ATOM   5273  O  O   . ASP E  1 128 ? 46.993  62.902  7.879   1.00 21.73 ? 101 ASP E O   1 
ATOM   5274  C  CB  . ASP E  1 128 ? 47.642  64.581  10.439  1.00 21.12 ? 101 ASP E CB  1 
ATOM   5275  C  CG  . ASP E  1 128 ? 48.756  65.589  10.076  1.00 23.55 ? 101 ASP E CG  1 
ATOM   5276  O  OD1 . ASP E  1 128 ? 48.574  66.815  10.346  1.00 26.20 ? 101 ASP E OD1 1 
ATOM   5277  O  OD2 . ASP E  1 128 ? 49.805  65.205  9.479   1.00 22.60 ? 101 ASP E OD2 1 
ATOM   5278  N  N   A SER E  1 129 ? 47.217  65.022  7.155   0.50 21.81 ? 102 SER E N   1 
ATOM   5279  N  N   B SER E  1 129 ? 47.227  65.036  7.176   0.50 22.77 ? 102 SER E N   1 
ATOM   5280  C  CA  A SER E  1 129 ? 47.622  64.591  5.821   0.50 22.69 ? 102 SER E CA  1 
ATOM   5281  C  CA  B SER E  1 129 ? 47.583  64.659  5.824   0.50 24.44 ? 102 SER E CA  1 
ATOM   5282  C  C   A SER E  1 129 ? 49.107  64.741  5.563   0.50 22.83 ? 102 SER E C   1 
ATOM   5283  C  C   B SER E  1 129 ? 49.078  64.798  5.557   0.50 23.83 ? 102 SER E C   1 
ATOM   5284  O  O   A SER E  1 129 ? 49.546  64.518  4.446   0.50 25.11 ? 102 SER E O   1 
ATOM   5285  O  O   B SER E  1 129 ? 49.493  64.621  4.423   0.50 26.06 ? 102 SER E O   1 
ATOM   5286  C  CB  A SER E  1 129 ? 46.820  65.324  4.745   0.50 24.69 ? 102 SER E CB  1 
ATOM   5287  C  CB  B SER E  1 129 ? 46.793  65.516  4.829   0.50 27.71 ? 102 SER E CB  1 
ATOM   5288  O  OG  A SER E  1 129 ? 45.482  64.892  4.783   0.50 21.70 ? 102 SER E OG  1 
ATOM   5289  O  OG  B SER E  1 129 ? 47.206  66.867  4.925   0.50 28.77 ? 102 SER E OG  1 
ATOM   5290  N  N   . VAL E  1 130 ? 49.884  65.133  6.573   1.00 19.86 ? 103 VAL E N   1 
ATOM   5291  C  CA  . VAL E  1 130 ? 51.329  65.276  6.375   1.00 20.43 ? 103 VAL E CA  1 
ATOM   5292  C  C   . VAL E  1 130 ? 52.086  64.003  6.875   1.00 19.90 ? 103 VAL E C   1 
ATOM   5293  O  O   . VAL E  1 130 ? 52.993  63.498  6.186   1.00 19.97 ? 103 VAL E O   1 
ATOM   5294  C  CB  . VAL E  1 130 ? 51.926  66.554  7.000   1.00 19.79 ? 103 VAL E CB  1 
ATOM   5295  C  CG1 . VAL E  1 130 ? 53.475  66.505  6.930   1.00 20.02 ? 103 VAL E CG1 1 
ATOM   5296  C  CG2 . VAL E  1 130 ? 51.416  67.795  6.214   1.00 21.38 ? 103 VAL E CG2 1 
ATOM   5297  N  N   . ILE E  1 131 ? 51.692  63.460  8.022   1.00 18.82 ? 104 ILE E N   1 
ATOM   5298  C  CA  . ILE E  1 131 ? 52.248  62.142  8.427   1.00 17.75 ? 104 ILE E CA  1 
ATOM   5299  C  C   . ILE E  1 131 ? 51.697  61.096  7.465   1.00 17.11 ? 104 ILE E C   1 
ATOM   5300  O  O   . ILE E  1 131 ? 50.689  61.328  6.779   1.00 17.82 ? 104 ILE E O   1 
ATOM   5301  C  CB  . ILE E  1 131 ? 51.877  61.734  9.880   1.00 17.96 ? 104 ILE E CB  1 
ATOM   5302  C  CG1 . ILE E  1 131 ? 50.344  61.807  10.092  1.00 16.51 ? 104 ILE E CG1 1 
ATOM   5303  C  CG2 . ILE E  1 131 ? 52.615  62.644  10.862  1.00 18.15 ? 104 ILE E CG2 1 
ATOM   5304  C  CD1 . ILE E  1 131 ? 49.793  61.086  11.331  1.00 16.58 ? 104 ILE E CD1 1 
ATOM   5305  N  N   . SER E  1 132 ? 52.355  59.947  7.394   1.00 17.72 ? 105 SER E N   1 
ATOM   5306  C  CA  . SER E  1 132 ? 51.828  58.851  6.554   1.00 18.29 ? 105 SER E CA  1 
ATOM   5307  C  C   . SER E  1 132 ? 52.214  57.527  7.216   1.00 17.79 ? 105 SER E C   1 
ATOM   5308  O  O   . SER E  1 132 ? 53.080  57.509  8.088   1.00 17.76 ? 105 SER E O   1 
ATOM   5309  C  CB  . SER E  1 132 ? 52.444  58.927  5.132   1.00 19.55 ? 105 SER E CB  1 
ATOM   5310  O  OG  . SER E  1 132 ? 51.737  58.041  4.251   1.00 17.78 ? 105 SER E OG  1 
ATOM   5311  N  N   . LEU E  1 133 ? 51.567  56.440  6.810   1.00 18.79 ? 106 LEU E N   1 
ATOM   5312  C  CA  . LEU E  1 133 ? 52.031  55.102  7.212   1.00 18.14 ? 106 LEU E CA  1 
ATOM   5313  C  C   . LEU E  1 133 ? 52.839  54.419  6.105   1.00 24.55 ? 106 LEU E C   1 
ATOM   5314  O  O   . LEU E  1 133 ? 53.112  53.190  6.192   1.00 24.21 ? 106 LEU E O   1 
ATOM   5315  C  CB  . LEU E  1 133 ? 50.819  54.220  7.597   1.00 19.54 ? 106 LEU E CB  1 
ATOM   5316  C  CG  . LEU E  1 133 ? 49.920  54.838  8.662   1.00 20.28 ? 106 LEU E CG  1 
ATOM   5317  C  CD1 . LEU E  1 133 ? 48.787  53.864  9.002   1.00 23.09 ? 106 LEU E CD1 1 
ATOM   5318  C  CD2 . LEU E  1 133 ? 50.715  55.267  9.886   1.00 19.47 ? 106 LEU E CD2 1 
ATOM   5319  N  N   . SER E  1 134 ? 53.219  55.189  5.089   1.00 22.36 ? 107 SER E N   1 
ATOM   5320  C  CA  . SER E  1 134 ? 54.160  54.722  4.052   1.00 24.98 ? 107 SER E CA  1 
ATOM   5321  C  C   . SER E  1 134 ? 54.948  55.839  3.456   1.00 27.51 ? 107 SER E C   1 
ATOM   5322  O  O   . SER E  1 134 ? 54.620  57.020  3.660   1.00 24.31 ? 107 SER E O   1 
ATOM   5323  C  CB  . SER E  1 134 ? 53.435  53.896  2.951   1.00 28.90 ? 107 SER E CB  1 
ATOM   5324  O  OG  . SER E  1 134 ? 52.479  54.672  2.265   1.00 30.41 ? 107 SER E OG  1 
ATOM   5325  N  N   . GLY E  1 135 ? 56.040  55.485  2.753   1.00 27.32 ? 108 GLY E N   1 
ATOM   5326  C  CA  . GLY E  1 135 ? 56.836  56.460  2.034   1.00 26.83 ? 108 GLY E CA  1 
ATOM   5327  C  C   . GLY E  1 135 ? 57.725  57.321  2.898   1.00 27.36 ? 108 GLY E C   1 
ATOM   5328  O  O   . GLY E  1 135 ? 57.978  57.007  4.055   1.00 26.38 ? 108 GLY E O   1 
ATOM   5329  N  N   . ASP E  1 136 ? 58.211  58.423  2.338   1.00 24.59 ? 109 ASP E N   1 
ATOM   5330  C  CA  . ASP E  1 136 ? 59.166  59.298  3.030   1.00 25.86 ? 109 ASP E CA  1 
ATOM   5331  C  C   . ASP E  1 136 ? 58.671  59.823  4.392   1.00 23.81 ? 109 ASP E C   1 
ATOM   5332  O  O   . ASP E  1 136 ? 59.480  60.183  5.263   1.00 24.89 ? 109 ASP E O   1 
ATOM   5333  C  CB  . ASP E  1 136 ? 59.379  60.575  2.182   1.00 32.50 ? 109 ASP E CB  1 
ATOM   5334  C  CG  . ASP E  1 136 ? 60.326  60.361  1.013   1.00 39.03 ? 109 ASP E CG  1 
ATOM   5335  O  OD1 . ASP E  1 136 ? 60.416  61.287  0.176   1.00 40.96 ? 109 ASP E OD1 1 
ATOM   5336  O  OD2 . ASP E  1 136 ? 60.943  59.273  0.947   1.00 42.25 ? 109 ASP E OD2 1 
ATOM   5337  N  N   . HIS E  1 137 ? 57.363  59.998  4.518   1.00 21.58 ? 110 HIS E N   1 
ATOM   5338  C  CA  . HIS E  1 137 ? 56.812  60.642  5.721   1.00 22.28 ? 110 HIS E CA  1 
ATOM   5339  C  C   . HIS E  1 137 ? 56.271  59.566  6.692   1.00 21.57 ? 110 HIS E C   1 
ATOM   5340  O  O   . HIS E  1 137 ? 55.509  59.885  7.624   1.00 18.45 ? 110 HIS E O   1 
ATOM   5341  C  CB  . HIS E  1 137 ? 55.706  61.627  5.342   1.00 25.57 ? 110 HIS E CB  1 
ATOM   5342  C  CG  . HIS E  1 137 ? 56.191  62.851  4.605   1.00 31.84 ? 110 HIS E CG  1 
ATOM   5343  N  ND1 . HIS E  1 137 ? 55.350  63.901  4.292   1.00 37.08 ? 110 HIS E ND1 1 
ATOM   5344  C  CD2 . HIS E  1 137 ? 57.425  63.218  4.174   1.00 37.07 ? 110 HIS E CD2 1 
ATOM   5345  C  CE1 . HIS E  1 137 ? 56.035  64.835  3.655   1.00 37.57 ? 110 HIS E CE1 1 
ATOM   5346  N  NE2 . HIS E  1 137 ? 57.293  64.445  3.568   1.00 38.01 ? 110 HIS E NE2 1 
ATOM   5347  N  N   . CYS E  1 138 ? 56.692  58.306  6.479   1.00 18.92 ? 111 CYS E N   1 
ATOM   5348  C  CA  . CYS E  1 138 ? 56.181  57.167  7.235   1.00 18.97 ? 111 CYS E CA  1 
ATOM   5349  C  C   . CYS E  1 138 ? 56.578  57.332  8.676   1.00 16.72 ? 111 CYS E C   1 
ATOM   5350  O  O   . CYS E  1 138 ? 57.750  57.625  8.953   1.00 19.13 ? 111 CYS E O   1 
ATOM   5351  C  CB  . CYS E  1 138 ? 56.859  55.866  6.710   1.00 20.61 ? 111 CYS E CB  1 
ATOM   5352  S  SG  . CYS E  1 138 ? 56.157  54.419  7.505   1.00 26.52 ? 111 CYS E SG  1 
ATOM   5353  N  N   . ILE E  1 139 ? 55.639  57.154  9.597   1.00 16.64 ? 112 ILE E N   1 
ATOM   5354  C  CA  . ILE E  1 139 ? 55.960  57.296  11.018  1.00 17.35 ? 112 ILE E CA  1 
ATOM   5355  C  C   . ILE E  1 139 ? 56.062  55.944  11.758  1.00 15.87 ? 112 ILE E C   1 
ATOM   5356  O  O   . ILE E  1 139 ? 56.346  55.915  12.936  1.00 15.49 ? 112 ILE E O   1 
ATOM   5357  C  CB  . ILE E  1 139 ? 54.923  58.200  11.728  1.00 17.98 ? 112 ILE E CB  1 
ATOM   5358  C  CG1 . ILE E  1 139 ? 53.520  57.546  11.675  1.00 19.39 ? 112 ILE E CG1 1 
ATOM   5359  C  CG2 . ILE E  1 139 ? 55.017  59.646  11.136  1.00 17.25 ? 112 ILE E CG2 1 
ATOM   5360  C  CD1 . ILE E  1 139 ? 52.403  58.319  12.388  1.00 21.33 ? 112 ILE E CD1 1 
ATOM   5361  N  N   . ILE E  1 140 ? 55.808  54.834  11.064  1.00 18.08 ? 113 ILE E N   1 
ATOM   5362  C  CA  . ILE E  1 140 ? 56.007  53.501  11.671  1.00 19.09 ? 113 ILE E CA  1 
ATOM   5363  C  C   . ILE E  1 140 ? 57.463  53.348  12.026  1.00 18.16 ? 113 ILE E C   1 
ATOM   5364  O  O   . ILE E  1 140 ? 58.357  53.756  11.277  1.00 17.07 ? 113 ILE E O   1 
ATOM   5365  C  CB  . ILE E  1 140 ? 55.520  52.419  10.700  1.00 22.73 ? 113 ILE E CB  1 
ATOM   5366  C  CG1 . ILE E  1 140 ? 54.000  52.580  10.600  1.00 23.36 ? 113 ILE E CG1 1 
ATOM   5367  C  CG2 . ILE E  1 140 ? 56.002  50.994  11.146  1.00 22.78 ? 113 ILE E CG2 1 
ATOM   5368  C  CD1 . ILE E  1 140 ? 53.335  51.709  9.567   1.00 26.59 ? 113 ILE E CD1 1 
ATOM   5369  N  N   . GLY E  1 141 ? 57.713  52.853  13.225  1.00 17.85 ? 114 GLY E N   1 
ATOM   5370  C  CA  . GLY E  1 141 ? 59.072  52.698  13.724  1.00 16.12 ? 114 GLY E CA  1 
ATOM   5371  C  C   . GLY E  1 141 ? 59.624  53.939  14.357  1.00 17.05 ? 114 GLY E C   1 
ATOM   5372  O  O   . GLY E  1 141 ? 60.782  53.947  14.758  1.00 17.39 ? 114 GLY E O   1 
ATOM   5373  N  N   . ARG E  1 142 ? 58.817  55.034  14.438  1.00 16.40 ? 115 ARG E N   1 
ATOM   5374  C  CA  . ARG E  1 142 ? 59.291  56.242  15.126  1.00 15.91 ? 115 ARG E CA  1 
ATOM   5375  C  C   . ARG E  1 142 ? 58.589  56.351  16.451  1.00 16.34 ? 115 ARG E C   1 
ATOM   5376  O  O   . ARG E  1 142 ? 57.879  55.432  16.814  1.00 17.36 ? 115 ARG E O   1 
ATOM   5377  C  CB  . ARG E  1 142 ? 59.091  57.507  14.230  1.00 16.17 ? 115 ARG E CB  1 
ATOM   5378  C  CG  . ARG E  1 142 ? 59.831  57.194  12.920  1.00 20.12 ? 115 ARG E CG  1 
ATOM   5379  C  CD  . ARG E  1 142 ? 59.973  58.376  12.021  1.00 21.21 ? 115 ARG E CD  1 
ATOM   5380  N  NE  . ARG E  1 142 ? 60.554  58.003  10.700  1.00 20.12 ? 115 ARG E NE  1 
ATOM   5381  C  CZ  . ARG E  1 142 ? 61.848  58.036  10.412  1.00 21.27 ? 115 ARG E CZ  1 
ATOM   5382  N  NH1 . ARG E  1 142 ? 62.769  58.405  11.303  1.00 19.71 ? 115 ARG E NH1 1 
ATOM   5383  N  NH2 . ARG E  1 142 ? 62.225  57.802  9.140   1.00 22.57 ? 115 ARG E NH2 1 
ATOM   5384  N  N   . THR E  1 143 ? 58.826  57.436  17.208  1.00 16.64 ? 116 THR E N   1 
ATOM   5385  C  CA  . THR E  1 143 ? 58.235  57.491  18.536  1.00 16.05 ? 116 THR E CA  1 
ATOM   5386  C  C   . THR E  1 143 ? 57.142  58.596  18.638  1.00 16.54 ? 116 THR E C   1 
ATOM   5387  O  O   . THR E  1 143 ? 57.427  59.716  18.241  1.00 17.36 ? 116 THR E O   1 
ATOM   5388  C  CB  . THR E  1 143 ? 59.326  57.759  19.564  1.00 18.26 ? 116 THR E CB  1 
ATOM   5389  O  OG1 . THR E  1 143 ? 60.177  56.583  19.647  1.00 19.37 ? 116 THR E OG1 1 
ATOM   5390  C  CG2 . THR E  1 143 ? 58.733  58.000  21.006  1.00 15.39 ? 116 THR E CG2 1 
ATOM   5391  N  N   . LEU E  1 144 ? 55.984  58.269  19.218  1.00 15.38 ? 117 LEU E N   1 
ATOM   5392  C  CA  . LEU E  1 144 ? 54.948  59.317  19.555  1.00 14.47 ? 117 LEU E CA  1 
ATOM   5393  C  C   . LEU E  1 144 ? 55.203  59.733  20.995  1.00 14.71 ? 117 LEU E C   1 
ATOM   5394  O  O   . LEU E  1 144 ? 55.472  58.862  21.839  1.00 13.22 ? 117 LEU E O   1 
ATOM   5395  C  CB  . LEU E  1 144 ? 53.556  58.704  19.419  1.00 14.50 ? 117 LEU E CB  1 
ATOM   5396  C  CG  . LEU E  1 144 ? 52.396  59.680  19.735  1.00 14.38 ? 117 LEU E CG  1 
ATOM   5397  C  CD1 . LEU E  1 144 ? 52.340  60.788  18.618  1.00 15.36 ? 117 LEU E CD1 1 
ATOM   5398  C  CD2 . LEU E  1 144 ? 51.106  58.855  19.701  1.00 14.13 ? 117 LEU E CD2 1 
ATOM   5399  N  N   . VAL E  1 145 ? 55.206  61.044  21.276  1.00 12.83 ? 118 VAL E N   1 
ATOM   5400  C  CA  . VAL E  1 145 ? 55.501  61.550  22.609  1.00 14.51 ? 118 VAL E CA  1 
ATOM   5401  C  C   . VAL E  1 145 ? 54.381  62.532  23.012  1.00 15.34 ? 118 VAL E C   1 
ATOM   5402  O  O   . VAL E  1 145 ? 54.024  63.386  22.196  1.00 14.22 ? 118 VAL E O   1 
ATOM   5403  C  CB  . VAL E  1 145 ? 56.838  62.342  22.596  1.00 15.22 ? 118 VAL E CB  1 
ATOM   5404  C  CG1 . VAL E  1 145 ? 57.134  62.913  24.024  1.00 16.13 ? 118 VAL E CG1 1 
ATOM   5405  C  CG2 . VAL E  1 145 ? 58.040  61.459  22.201  1.00 15.69 ? 118 VAL E CG2 1 
ATOM   5406  N  N   . VAL E  1 146 ? 53.899  62.448  24.271  1.00 14.11 ? 119 VAL E N   1 
ATOM   5407  C  CA  . VAL E  1 146 ? 53.013  63.468  24.794  1.00 15.05 ? 119 VAL E CA  1 
ATOM   5408  C  C   . VAL E  1 146 ? 53.853  64.236  25.811  1.00 16.94 ? 119 VAL E C   1 
ATOM   5409  O  O   . VAL E  1 146 ? 54.606  63.645  26.636  1.00 15.86 ? 119 VAL E O   1 
ATOM   5410  C  CB  . VAL E  1 146 ? 51.676  62.904  25.323  1.00 15.99 ? 119 VAL E CB  1 
ATOM   5411  C  CG1 . VAL E  1 146 ? 51.923  61.908  26.476  1.00 17.13 ? 119 VAL E CG1 1 
ATOM   5412  C  CG2 . VAL E  1 146 ? 50.792  64.036  25.813  1.00 15.19 ? 119 VAL E CG2 1 
ATOM   5413  N  N   . HIS E  1 147 ? 53.755  65.560  25.695  1.00 15.21 ? 120 HIS E N   1 
ATOM   5414  C  CA  . HIS E  1 147 ? 54.620  66.473  26.418  1.00 14.78 ? 120 HIS E CA  1 
ATOM   5415  C  C   . HIS E  1 147 ? 53.916  67.106  27.632  1.00 15.25 ? 120 HIS E C   1 
ATOM   5416  O  O   . HIS E  1 147 ? 52.678  67.088  27.757  1.00 17.32 ? 120 HIS E O   1 
ATOM   5417  C  CB  . HIS E  1 147 ? 55.126  67.561  25.458  1.00 14.94 ? 120 HIS E CB  1 
ATOM   5418  C  CG  . HIS E  1 147 ? 56.163  67.047  24.484  1.00 17.01 ? 120 HIS E CG  1 
ATOM   5419  N  ND1 . HIS E  1 147 ? 57.506  67.193  24.704  1.00 17.97 ? 120 HIS E ND1 1 
ATOM   5420  C  CD2 . HIS E  1 147 ? 56.044  66.430  23.285  1.00 17.55 ? 120 HIS E CD2 1 
ATOM   5421  C  CE1 . HIS E  1 147 ? 58.191  66.678  23.687  1.00 18.45 ? 120 HIS E CE1 1 
ATOM   5422  N  NE2 . HIS E  1 147 ? 57.324  66.198  22.811  1.00 18.93 ? 120 HIS E NE2 1 
ATOM   5423  N  N   . GLU E  1 148 ? 54.754  67.690  28.470  1.00 17.09 ? 121 GLU E N   1 
ATOM   5424  C  CA  . GLU E  1 148 ? 54.374  68.326  29.725  1.00 19.97 ? 121 GLU E CA  1 
ATOM   5425  C  C   . GLU E  1 148 ? 53.504  69.557  29.567  1.00 19.27 ? 121 GLU E C   1 
ATOM   5426  O  O   . GLU E  1 148 ? 52.599  69.764  30.373  1.00 18.34 ? 121 GLU E O   1 
ATOM   5427  C  CB  . GLU E  1 148 ? 55.684  68.718  30.396  1.00 22.54 ? 121 GLU E CB  1 
ATOM   5428  C  CG  . GLU E  1 148 ? 55.570  69.455  31.727  1.00 29.91 ? 121 GLU E CG  1 
ATOM   5429  C  CD  . GLU E  1 148 ? 56.881  70.205  32.047  1.00 36.77 ? 121 GLU E CD  1 
ATOM   5430  O  OE1 . GLU E  1 148 ? 57.822  70.354  31.186  1.00 32.44 ? 121 GLU E OE1 1 
ATOM   5431  O  OE2 . GLU E  1 148 ? 56.961  70.672  33.198  1.00 46.20 ? 121 GLU E OE2 1 
ATOM   5432  N  N   . LYS E  1 149 ? 53.808  70.394  28.578  1.00 20.00 ? 122 LYS E N   1 
ATOM   5433  C  CA  . LYS E  1 149 ? 53.121  71.707  28.424  1.00 22.54 ? 122 LYS E CA  1 
ATOM   5434  C  C   . LYS E  1 149 ? 52.498  71.873  27.038  1.00 20.53 ? 122 LYS E C   1 
ATOM   5435  O  O   . LYS E  1 149 ? 52.715  71.045  26.158  1.00 17.73 ? 122 LYS E O   1 
ATOM   5436  C  CB  . LYS E  1 149 ? 54.144  72.848  28.613  1.00 24.69 ? 122 LYS E CB  1 
ATOM   5437  C  CG  . LYS E  1 149 ? 55.217  72.547  29.618  1.00 31.06 ? 122 LYS E CG  1 
ATOM   5438  C  CD  . LYS E  1 149 ? 55.616  73.744  30.433  1.00 35.85 ? 122 LYS E CD  1 
ATOM   5439  C  CE  . LYS E  1 149 ? 56.005  74.888  29.542  1.00 40.81 ? 122 LYS E CE  1 
ATOM   5440  N  NZ  . LYS E  1 149 ? 57.455  74.888  29.223  1.00 48.63 ? 122 LYS E NZ  1 
ATOM   5441  N  N   . ALA E  1 150 ? 51.741  72.966  26.842  1.00 18.95 ? 123 ALA E N   1 
ATOM   5442  C  CA  . ALA E  1 150 ? 51.170  73.239  25.543  1.00 18.82 ? 123 ALA E CA  1 
ATOM   5443  C  C   . ALA E  1 150 ? 52.284  73.516  24.533  1.00 18.87 ? 123 ALA E C   1 
ATOM   5444  O  O   . ALA E  1 150 ? 53.306  74.116  24.849  1.00 19.05 ? 123 ALA E O   1 
ATOM   5445  C  CB  . ALA E  1 150 ? 50.224  74.469  25.622  1.00 20.08 ? 123 ALA E CB  1 
ATOM   5446  N  N   . ASP E  1 151 ? 52.062  73.083  23.294  1.00 17.09 ? 124 ASP E N   1 
ATOM   5447  C  CA  . ASP E  1 151 ? 52.906  73.435  22.162  1.00 17.16 ? 124 ASP E CA  1 
ATOM   5448  C  C   . ASP E  1 151 ? 52.458  74.837  21.713  1.00 16.82 ? 124 ASP E C   1 
ATOM   5449  O  O   . ASP E  1 151 ? 51.244  75.012  21.490  1.00 16.68 ? 124 ASP E O   1 
ATOM   5450  C  CB  . ASP E  1 151 ? 52.540  72.408  21.057  1.00 17.66 ? 124 ASP E CB  1 
ATOM   5451  C  CG  . ASP E  1 151 ? 53.355  72.566  19.775  1.00 20.01 ? 124 ASP E CG  1 
ATOM   5452  O  OD1 . ASP E  1 151 ? 53.999  73.640  19.511  1.00 18.68 ? 124 ASP E OD1 1 
ATOM   5453  O  OD2 . ASP E  1 151 ? 53.334  71.583  18.978  1.00 21.70 ? 124 ASP E OD2 1 
ATOM   5454  N  N   . ASP E  1 152 ? 53.391  75.801  21.567  1.00 16.51 ? 125 ASP E N   1 
ATOM   5455  C  CA  . ASP E  1 152 ? 53.016  77.170  21.124  1.00 18.56 ? 125 ASP E CA  1 
ATOM   5456  C  C   . ASP E  1 152 ? 52.907  77.304  19.567  1.00 17.23 ? 125 ASP E C   1 
ATOM   5457  O  O   . ASP E  1 152 ? 52.804  78.395  18.967  1.00 15.98 ? 125 ASP E O   1 
ATOM   5458  C  CB  . ASP E  1 152 ? 53.996  78.192  21.751  1.00 19.72 ? 125 ASP E CB  1 
ATOM   5459  C  CG  . ASP E  1 152 ? 55.427  78.131  21.171  1.00 18.89 ? 125 ASP E CG  1 
ATOM   5460  O  OD1 . ASP E  1 152 ? 55.697  77.559  20.105  1.00 18.59 ? 125 ASP E OD1 1 
ATOM   5461  O  OD2 . ASP E  1 152 ? 56.322  78.721  21.792  1.00 19.46 ? 125 ASP E OD2 1 
ATOM   5462  N  N   . LEU E  1 153 ? 53.034  76.157  18.910  1.00 16.67 ? 126 LEU E N   1 
ATOM   5463  C  CA  . LEU E  1 153 ? 52.860  76.016  17.473  1.00 17.94 ? 126 LEU E CA  1 
ATOM   5464  C  C   . LEU E  1 153 ? 53.864  76.839  16.672  1.00 15.82 ? 126 LEU E C   1 
ATOM   5465  O  O   . LEU E  1 153 ? 53.593  77.242  15.512  1.00 16.78 ? 126 LEU E O   1 
ATOM   5466  C  CB  . LEU E  1 153 ? 51.399  76.282  17.065  1.00 18.20 ? 126 LEU E CB  1 
ATOM   5467  C  CG  . LEU E  1 153 ? 50.320  75.541  17.921  1.00 20.05 ? 126 LEU E CG  1 
ATOM   5468  C  CD1 . LEU E  1 153 ? 48.910  75.906  17.509  1.00 21.40 ? 126 LEU E CD1 1 
ATOM   5469  C  CD2 . LEU E  1 153 ? 50.475  74.014  17.912  1.00 19.18 ? 126 LEU E CD2 1 
ATOM   5470  N  N   . GLY E  1 154 ? 55.022  77.047  17.267  1.00 15.45 ? 127 GLY E N   1 
ATOM   5471  C  CA  . GLY E  1 154 ? 56.112  77.652  16.562  1.00 15.97 ? 127 GLY E CA  1 
ATOM   5472  C  C   . GLY E  1 154 ? 55.986  79.179  16.576  1.00 17.94 ? 127 GLY E C   1 
ATOM   5473  O  O   . GLY E  1 154 ? 56.718  79.858  15.896  1.00 16.01 ? 127 GLY E O   1 
ATOM   5474  N  N   . LYS E  1 155 ? 55.056  79.704  17.359  1.00 15.11 ? 128 LYS E N   1 
ATOM   5475  C  CA  . LYS E  1 155 ? 54.775  81.187  17.325  1.00 17.08 ? 128 LYS E CA  1 
ATOM   5476  C  C   . LYS E  1 155 ? 55.312  81.906  18.574  1.00 16.81 ? 128 LYS E C   1 
ATOM   5477  O  O   . LYS E  1 155 ? 54.867  82.997  18.914  1.00 17.53 ? 128 LYS E O   1 
ATOM   5478  C  CB  . LYS E  1 155 ? 53.257  81.380  17.235  1.00 18.65 ? 128 LYS E CB  1 
ATOM   5479  C  CG  . LYS E  1 155 ? 52.777  80.866  15.859  1.00 22.17 ? 128 LYS E CG  1 
ATOM   5480  C  CD  . LYS E  1 155 ? 51.286  80.723  15.875  1.00 29.51 ? 128 LYS E CD  1 
ATOM   5481  C  CE  . LYS E  1 155 ? 50.670  82.059  15.633  1.00 34.73 ? 128 LYS E CE  1 
ATOM   5482  N  NZ  . LYS E  1 155 ? 49.194  81.859  15.733  1.00 44.49 ? 128 LYS E NZ  1 
ATOM   5483  N  N   . GLY E  1 156 ? 56.231  81.275  19.287  1.00 17.12 ? 129 GLY E N   1 
ATOM   5484  C  CA  . GLY E  1 156 ? 56.649  81.835  20.587  1.00 16.39 ? 129 GLY E CA  1 
ATOM   5485  C  C   . GLY E  1 156 ? 57.798  82.838  20.500  1.00 15.99 ? 129 GLY E C   1 
ATOM   5486  O  O   . GLY E  1 156 ? 58.117  83.498  21.531  1.00 17.08 ? 129 GLY E O   1 
ATOM   5487  N  N   . GLY E  1 157 ? 58.416  82.976  19.316  1.00 14.29 ? 130 GLY E N   1 
ATOM   5488  C  CA  . GLY E  1 157 ? 59.448  84.048  19.108  1.00 16.12 ? 130 GLY E CA  1 
ATOM   5489  C  C   . GLY E  1 157 ? 60.793  83.818  19.787  1.00 18.68 ? 130 GLY E C   1 
ATOM   5490  O  O   . GLY E  1 157 ? 61.689  84.691  19.778  1.00 19.80 ? 130 GLY E O   1 
ATOM   5491  N  N   . ASN E  1 158 ? 60.964  82.656  20.405  1.00 20.11 ? 131 ASN E N   1 
ATOM   5492  C  CA  . ASN E  1 158 ? 62.299  82.270  20.886  1.00 20.58 ? 131 ASN E CA  1 
ATOM   5493  C  C   . ASN E  1 158 ? 62.840  81.101  20.132  1.00 22.45 ? 131 ASN E C   1 
ATOM   5494  O  O   . ASN E  1 158 ? 62.141  80.442  19.295  1.00 22.55 ? 131 ASN E O   1 
ATOM   5495  C  CB  . ASN E  1 158 ? 62.326  82.039  22.426  1.00 21.70 ? 131 ASN E CB  1 
ATOM   5496  C  CG  . ASN E  1 158 ? 61.510  80.826  22.880  1.00 23.10 ? 131 ASN E CG  1 
ATOM   5497  O  OD1 . ASN E  1 158 ? 60.793  80.210  22.087  1.00 22.79 ? 131 ASN E OD1 1 
ATOM   5498  N  ND2 . ASN E  1 158 ? 61.573  80.509  24.198  1.00 23.49 ? 131 ASN E ND2 1 
ATOM   5499  N  N   . GLU E  1 159 ? 64.103  80.757  20.403  1.00 23.11 ? 132 GLU E N   1 
ATOM   5500  C  CA  . GLU E  1 159 ? 64.732  79.704  19.575  1.00 22.56 ? 132 GLU E CA  1 
ATOM   5501  C  C   . GLU E  1 159 ? 64.038  78.357  19.812  1.00 22.62 ? 132 GLU E C   1 
ATOM   5502  O  O   . GLU E  1 159 ? 63.870  77.523  18.887  1.00 23.57 ? 132 GLU E O   1 
ATOM   5503  C  CB  . GLU E  1 159 ? 66.236  79.551  19.965  1.00 29.62 ? 132 GLU E CB  1 
ATOM   5504  C  CG  . GLU E  1 159 ? 66.932  80.914  20.121  1.00 36.35 ? 132 GLU E CG  1 
ATOM   5505  C  CD  . GLU E  1 159 ? 68.405  80.860  20.622  1.00 46.52 ? 132 GLU E CD  1 
ATOM   5506  O  OE1 . GLU E  1 159 ? 68.766  79.952  21.411  1.00 50.96 ? 132 GLU E OE1 1 
ATOM   5507  O  OE2 . GLU E  1 159 ? 69.198  81.772  20.281  1.00 45.56 ? 132 GLU E OE2 1 
ATOM   5508  N  N   . GLU E  1 160 ? 63.659  78.133  21.062  1.00 20.97 ? 133 GLU E N   1 
ATOM   5509  C  CA  . GLU E  1 160 ? 63.042  76.850  21.444  1.00 21.46 ? 133 GLU E CA  1 
ATOM   5510  C  C   . GLU E  1 160 ? 61.683  76.658  20.697  1.00 23.37 ? 133 GLU E C   1 
ATOM   5511  O  O   . GLU E  1 160 ? 61.360  75.553  20.244  1.00 21.50 ? 133 GLU E O   1 
ATOM   5512  C  CB  . GLU E  1 160 ? 62.836  76.816  22.958  1.00 23.65 ? 133 GLU E CB  1 
ATOM   5513  C  CG  . GLU E  1 160 ? 62.541  75.442  23.528  1.00 26.84 ? 133 GLU E CG  1 
ATOM   5514  C  CD  . GLU E  1 160 ? 63.656  74.430  23.193  1.00 34.89 ? 133 GLU E CD  1 
ATOM   5515  O  OE1 . GLU E  1 160 ? 64.850  74.655  23.515  1.00 32.73 ? 133 GLU E OE1 1 
ATOM   5516  O  OE2 . GLU E  1 160 ? 63.327  73.428  22.550  1.00 36.23 ? 133 GLU E OE2 1 
ATOM   5517  N  N   . SER E  1 161 ? 60.945  77.746  20.486  1.00 21.30 ? 134 SER E N   1 
ATOM   5518  C  CA  . SER E  1 161 ? 59.663  77.609  19.774  1.00 19.69 ? 134 SER E CA  1 
ATOM   5519  C  C   . SER E  1 161 ? 59.852  77.018  18.390  1.00 18.38 ? 134 SER E C   1 
ATOM   5520  O  O   . SER E  1 161 ? 58.995  76.242  17.931  1.00 17.66 ? 134 SER E O   1 
ATOM   5521  C  CB  . SER E  1 161 ? 58.994  78.995  19.639  1.00 19.29 ? 134 SER E CB  1 
ATOM   5522  O  OG  . SER E  1 161 ? 57.730  78.840  19.034  1.00 19.17 ? 134 SER E OG  1 
ATOM   5523  N  N   . THR E  1 162 ? 60.906  77.435  17.671  1.00 17.28 ? 135 THR E N   1 
ATOM   5524  C  CA  . THR E  1 162 ? 61.156  76.943  16.318  1.00 19.19 ? 135 THR E CA  1 
ATOM   5525  C  C   . THR E  1 162 ? 61.629  75.444  16.303  1.00 21.12 ? 135 THR E C   1 
ATOM   5526  O  O   . THR E  1 162 ? 61.790  74.871  15.223  1.00 20.85 ? 135 THR E O   1 
ATOM   5527  C  CB  . THR E  1 162 ? 62.237  77.784  15.550  1.00 23.54 ? 135 THR E CB  1 
ATOM   5528  O  OG1 . THR E  1 162 ? 63.530  77.553  16.140  1.00 29.84 ? 135 THR E OG1 1 
ATOM   5529  C  CG2 . THR E  1 162 ? 61.948  79.275  15.641  1.00 26.94 ? 135 THR E CG2 1 
ATOM   5530  N  N   . LYS E  1 163 ? 61.901  74.864  17.484  1.00 21.48 ? 136 LYS E N   1 
ATOM   5531  C  CA  . LYS E  1 163 ? 62.416  73.460  17.580  1.00 22.31 ? 136 LYS E CA  1 
ATOM   5532  C  C   . LYS E  1 163 ? 61.369  72.562  18.197  1.00 20.60 ? 136 LYS E C   1 
ATOM   5533  O  O   . LYS E  1 163 ? 61.018  71.488  17.664  1.00 21.72 ? 136 LYS E O   1 
ATOM   5534  C  CB  . LYS E  1 163 ? 63.747  73.418  18.394  1.00 22.80 ? 136 LYS E CB  1 
ATOM   5535  C  CG  . LYS E  1 163 ? 64.858  74.235  17.731  1.00 26.79 ? 136 LYS E CG  1 
ATOM   5536  C  CD  . LYS E  1 163 ? 66.242  74.102  18.355  1.00 34.86 ? 136 LYS E CD  1 
ATOM   5537  C  CE  . LYS E  1 163 ? 66.332  74.797  19.702  1.00 40.08 ? 136 LYS E CE  1 
ATOM   5538  N  NZ  . LYS E  1 163 ? 67.725  74.796  20.274  1.00 48.11 ? 136 LYS E NZ  1 
ATOM   5539  N  N   . THR E  1 164 ? 60.824  72.985  19.332  1.00 20.49 ? 137 THR E N   1 
ATOM   5540  C  CA  . THR E  1 164 ? 59.931  72.102  20.079  1.00 21.59 ? 137 THR E CA  1 
ATOM   5541  C  C   . THR E  1 164 ? 58.587  72.683  20.424  1.00 20.49 ? 137 THR E C   1 
ATOM   5542  O  O   . THR E  1 164 ? 57.770  72.012  21.083  1.00 19.50 ? 137 THR E O   1 
ATOM   5543  C  CB  . THR E  1 164 ? 60.548  71.702  21.445  1.00 22.93 ? 137 THR E CB  1 
ATOM   5544  O  OG1 . THR E  1 164 ? 60.739  72.879  22.206  1.00 21.70 ? 137 THR E OG1 1 
ATOM   5545  C  CG2 . THR E  1 164 ? 61.922  71.006  21.273  1.00 26.28 ? 137 THR E CG2 1 
ATOM   5546  N  N   . GLY E  1 165 ? 58.345  73.943  20.038  1.00 18.42 ? 138 GLY E N   1 
ATOM   5547  C  CA  . GLY E  1 165 ? 57.114  74.610  20.438  1.00 18.06 ? 138 GLY E CA  1 
ATOM   5548  C  C   . GLY E  1 165 ? 57.067  74.913  21.933  1.00 18.28 ? 138 GLY E C   1 
ATOM   5549  O  O   . GLY E  1 165 ? 55.998  75.255  22.473  1.00 18.97 ? 138 GLY E O   1 
ATOM   5550  N  N   . ASN E  1 166 ? 58.199  74.797  22.625  1.00 19.46 ? 139 ASN E N   1 
ATOM   5551  C  CA  . ASN E  1 166 ? 58.204  75.064  24.090  1.00 18.62 ? 139 ASN E CA  1 
ATOM   5552  C  C   . ASN E  1 166 ? 57.316  74.082  24.883  1.00 18.20 ? 139 ASN E C   1 
ATOM   5553  O  O   . ASN E  1 166 ? 56.844  74.421  26.000  1.00 16.53 ? 139 ASN E O   1 
ATOM   5554  C  CB  . ASN E  1 166 ? 57.797  76.561  24.395  1.00 19.48 ? 139 ASN E CB  1 
ATOM   5555  C  CG  . ASN E  1 166 ? 58.944  77.542  24.064  1.00 21.58 ? 139 ASN E CG  1 
ATOM   5556  O  OD1 . ASN E  1 166 ? 59.990  77.439  24.648  1.00 23.23 ? 139 ASN E OD1 1 
ATOM   5557  N  ND2 . ASN E  1 166 ? 58.783  78.375  23.058  1.00 18.83 ? 139 ASN E ND2 1 
ATOM   5558  N  N   . ALA E  1 167 ? 57.112  72.869  24.357  1.00 16.41 ? 140 ALA E N   1 
ATOM   5559  C  CA  . ALA E  1 167 ? 56.170  71.941  24.995  1.00 17.49 ? 140 ALA E CA  1 
ATOM   5560  C  C   . ALA E  1 167 ? 56.781  71.219  26.226  1.00 17.39 ? 140 ALA E C   1 
ATOM   5561  O  O   . ALA E  1 167 ? 56.114  70.410  26.861  1.00 17.82 ? 140 ALA E O   1 
ATOM   5562  C  CB  . ALA E  1 167 ? 55.672  70.913  23.986  1.00 18.38 ? 140 ALA E CB  1 
ATOM   5563  N  N   . GLY E  1 168 ? 58.052  71.476  26.520  1.00 18.94 ? 141 GLY E N   1 
ATOM   5564  C  CA  . GLY E  1 168 ? 58.633  70.981  27.782  1.00 20.54 ? 141 GLY E CA  1 
ATOM   5565  C  C   . GLY E  1 168 ? 58.909  69.477  27.774  1.00 20.28 ? 141 GLY E C   1 
ATOM   5566  O  O   . GLY E  1 168 ? 59.136  68.859  26.695  1.00 19.26 ? 141 GLY E O   1 
ATOM   5567  N  N   A SER E  1 169 ? 58.808  68.868  28.957  0.50 21.87 ? 142 SER E N   1 
ATOM   5568  N  N   B SER E  1 169 ? 58.975  68.873  28.961  0.50 20.69 ? 142 SER E N   1 
ATOM   5569  C  CA  A SER E  1 169 ? 59.279  67.494  29.161  0.50 21.14 ? 142 SER E CA  1 
ATOM   5570  C  CA  B SER E  1 169 ? 59.508  67.506  29.073  0.50 18.88 ? 142 SER E CA  1 
ATOM   5571  C  C   A SER E  1 169 ? 58.468  66.425  28.454  0.50 18.79 ? 142 SER E C   1 
ATOM   5572  C  C   B SER E  1 169 ? 58.569  66.471  28.432  0.50 17.58 ? 142 SER E C   1 
ATOM   5573  O  O   A SER E  1 169 ? 57.304  66.633  28.079  0.50 17.92 ? 142 SER E O   1 
ATOM   5574  O  O   B SER E  1 169 ? 57.413  66.751  28.092  0.50 17.20 ? 142 SER E O   1 
ATOM   5575  C  CB  A SER E  1 169 ? 59.347  67.173  30.654  0.50 22.44 ? 142 SER E CB  1 
ATOM   5576  C  CB  B SER E  1 169 ? 59.762  67.126  30.540  0.50 18.55 ? 142 SER E CB  1 
ATOM   5577  O  OG  A SER E  1 169 ? 60.196  68.120  31.239  0.50 25.14 ? 142 SER E OG  1 
ATOM   5578  O  OG  B SER E  1 169 ? 58.525  67.105  31.225  0.50 16.10 ? 142 SER E OG  1 
ATOM   5579  N  N   . ARG E  1 170 ? 59.074  65.251  28.320  1.00 17.44 ? 143 ARG E N   1 
ATOM   5580  C  CA  . ARG E  1 170 ? 58.402  64.147  27.627  1.00 17.62 ? 143 ARG E CA  1 
ATOM   5581  C  C   . ARG E  1 170 ? 57.756  63.298  28.704  1.00 19.23 ? 143 ARG E C   1 
ATOM   5582  O  O   . ARG E  1 170 ? 58.468  62.628  29.471  1.00 21.59 ? 143 ARG E O   1 
ATOM   5583  C  CB  . ARG E  1 170 ? 59.474  63.357  26.859  1.00 18.91 ? 143 ARG E CB  1 
ATOM   5584  C  CG  . ARG E  1 170 ? 60.216  64.230  25.881  1.00 18.50 ? 143 ARG E CG  1 
ATOM   5585  C  CD  . ARG E  1 170 ? 61.321  63.486  25.108  1.00 19.76 ? 143 ARG E CD  1 
ATOM   5586  N  NE  . ARG E  1 170 ? 62.015  64.482  24.303  1.00 20.15 ? 143 ARG E NE  1 
ATOM   5587  C  CZ  . ARG E  1 170 ? 62.732  64.236  23.218  1.00 20.17 ? 143 ARG E CZ  1 
ATOM   5588  N  NH1 . ARG E  1 170 ? 62.888  62.994  22.763  1.00 17.91 ? 143 ARG E NH1 1 
ATOM   5589  N  NH2 . ARG E  1 170 ? 63.250  65.256  22.558  1.00 19.76 ? 143 ARG E NH2 1 
ATOM   5590  N  N   . LEU E  1 171 ? 56.440  63.288  28.776  1.00 17.38 ? 144 LEU E N   1 
ATOM   5591  C  CA  . LEU E  1 171 ? 55.738  62.606  29.870  1.00 17.84 ? 144 LEU E CA  1 
ATOM   5592  C  C   . LEU E  1 171 ? 55.587  61.130  29.603  1.00 16.98 ? 144 LEU E C   1 
ATOM   5593  O  O   . LEU E  1 171 ? 55.686  60.286  30.511  1.00 16.62 ? 144 LEU E O   1 
ATOM   5594  C  CB  . LEU E  1 171 ? 54.338  63.212  30.072  1.00 18.78 ? 144 LEU E CB  1 
ATOM   5595  C  CG  . LEU E  1 171 ? 54.275  64.689  30.484  1.00 20.18 ? 144 LEU E CG  1 
ATOM   5596  C  CD1 . LEU E  1 171 ? 52.801  65.062  30.739  1.00 21.86 ? 144 LEU E CD1 1 
ATOM   5597  C  CD2 . LEU E  1 171 ? 55.122  64.967  31.729  1.00 22.55 ? 144 LEU E CD2 1 
ATOM   5598  N  N   . ALA E  1 172 ? 55.381  60.778  28.343  1.00 16.01 ? 145 ALA E N   1 
ATOM   5599  C  CA  . ALA E  1 172 ? 55.187  59.367  27.973  1.00 17.36 ? 145 ALA E CA  1 
ATOM   5600  C  C   . ALA E  1 172 ? 55.417  59.205  26.489  1.00 18.39 ? 145 ALA E C   1 
ATOM   5601  O  O   . ALA E  1 172 ? 55.239  60.186  25.711  1.00 16.25 ? 145 ALA E O   1 
ATOM   5602  C  CB  . ALA E  1 172 ? 53.778  58.874  28.322  1.00 15.87 ? 145 ALA E CB  1 
ATOM   5603  N  N   . CYS E  1 173 ? 55.816  57.993  26.095  1.00 17.39 ? 146 CYS E N   1 
ATOM   5604  C  CA  . CYS E  1 173 ? 56.127  57.762  24.679  1.00 17.37 ? 146 CYS E CA  1 
ATOM   5605  C  C   . CYS E  1 173 ? 55.997  56.283  24.347  1.00 18.13 ? 146 CYS E C   1 
ATOM   5606  O  O   . CYS E  1 173 ? 55.904  55.416  25.254  1.00 16.68 ? 146 CYS E O   1 
ATOM   5607  C  CB  . CYS E  1 173 ? 57.516  58.265  24.335  1.00 20.22 ? 146 CYS E CB  1 
ATOM   5608  S  SG  . CYS E  1 173 ? 58.858  57.452  25.287  1.00 25.73 ? 146 CYS E SG  1 
ATOM   5609  N  N   . GLY E  1 174 ? 56.013  55.997  23.043  1.00 15.82 ? 147 GLY E N   1 
ATOM   5610  C  CA  . GLY E  1 174 ? 55.957  54.613  22.581  1.00 18.51 ? 147 GLY E CA  1 
ATOM   5611  C  C   . GLY E  1 174 ? 56.448  54.610  21.140  1.00 21.08 ? 147 GLY E C   1 
ATOM   5612  O  O   . GLY E  1 174 ? 56.292  55.634  20.389  1.00 15.62 ? 147 GLY E O   1 
ATOM   5613  N  N   . VAL E  1 175 ? 56.940  53.451  20.731  1.00 18.41 ? 148 VAL E N   1 
ATOM   5614  C  CA  . VAL E  1 175 ? 57.279  53.229  19.312  1.00 17.75 ? 148 VAL E CA  1 
ATOM   5615  C  C   . VAL E  1 175 ? 56.026  52.884  18.547  1.00 16.01 ? 148 VAL E C   1 
ATOM   5616  O  O   . VAL E  1 175 ? 55.156  52.155  19.008  1.00 18.63 ? 148 VAL E O   1 
ATOM   5617  C  CB  . VAL E  1 175 ? 58.378  52.081  19.141  1.00 17.84 ? 148 VAL E CB  1 
ATOM   5618  C  CG1 . VAL E  1 175 ? 58.843  52.012  17.684  1.00 15.87 ? 148 VAL E CG1 1 
ATOM   5619  C  CG2 . VAL E  1 175 ? 59.593  52.394  19.991  1.00 15.96 ? 148 VAL E CG2 1 
ATOM   5620  N  N   . ILE E  1 176 ? 55.887  53.459  17.362  1.00 16.07 ? 149 ILE E N   1 
ATOM   5621  C  CA  . ILE E  1 176 ? 54.673  53.267  16.576  1.00 16.98 ? 149 ILE E CA  1 
ATOM   5622  C  C   . ILE E  1 176 ? 54.845  51.975  15.786  1.00 18.47 ? 149 ILE E C   1 
ATOM   5623  O  O   . ILE E  1 176 ? 55.779  51.894  15.013  1.00 19.66 ? 149 ILE E O   1 
ATOM   5624  C  CB  . ILE E  1 176 ? 54.463  54.457  15.593  1.00 17.24 ? 149 ILE E CB  1 
ATOM   5625  C  CG1 . ILE E  1 176 ? 54.234  55.743  16.420  1.00 17.71 ? 149 ILE E CG1 1 
ATOM   5626  C  CG2 . ILE E  1 176 ? 53.256  54.182  14.683  1.00 16.18 ? 149 ILE E CG2 1 
ATOM   5627  C  CD1 . ILE E  1 176 ? 54.401  57.057  15.671  1.00 17.76 ? 149 ILE E CD1 1 
ATOM   5628  N  N   . GLY E  1 177 ? 53.961  50.998  15.993  1.00 18.84 ? 150 GLY E N   1 
ATOM   5629  C  CA  . GLY E  1 177 ? 54.125  49.681  15.415  1.00 21.67 ? 150 GLY E CA  1 
ATOM   5630  C  C   . GLY E  1 177 ? 53.048  49.367  14.407  1.00 22.91 ? 150 GLY E C   1 
ATOM   5631  O  O   . GLY E  1 177 ? 51.931  49.923  14.437  1.00 21.00 ? 150 GLY E O   1 
ATOM   5632  N  N   . ILE E  1 178 ? 53.365  48.453  13.478  1.00 21.65 ? 151 ILE E N   1 
ATOM   5633  C  CA  . ILE E  1 178 ? 52.336  47.966  12.525  1.00 22.64 ? 151 ILE E CA  1 
ATOM   5634  C  C   . ILE E  1 178 ? 51.251  47.213  13.240  1.00 23.08 ? 151 ILE E C   1 
ATOM   5635  O  O   . ILE E  1 178 ? 51.561  46.376  14.089  1.00 24.53 ? 151 ILE E O   1 
ATOM   5636  C  CB  . ILE E  1 178 ? 52.967  47.004  11.457  1.00 25.43 ? 151 ILE E CB  1 
ATOM   5637  C  CG1 . ILE E  1 178 ? 54.020  47.760  10.711  1.00 29.41 ? 151 ILE E CG1 1 
ATOM   5638  C  CG2 . ILE E  1 178 ? 51.875  46.473  10.528  1.00 29.64 ? 151 ILE E CG2 1 
ATOM   5639  C  CD1 . ILE E  1 178 ? 55.111  46.881  10.105  1.00 34.67 ? 151 ILE E CD1 1 
ATOM   5640  N  N   . ALA E  1 179 ? 49.976  47.484  12.926  1.00 21.46 ? 152 ALA E N   1 
ATOM   5641  C  CA  . ALA E  1 179 ? 48.867  46.829  13.605  1.00 24.32 ? 152 ALA E CA  1 
ATOM   5642  C  C   . ALA E  1 179 ? 48.110  45.963  12.606  1.00 27.13 ? 152 ALA E C   1 
ATOM   5643  O  O   . ALA E  1 179 ? 48.238  46.141  11.397  1.00 31.46 ? 152 ALA E O   1 
ATOM   5644  C  CB  . ALA E  1 179 ? 47.885  47.831  14.243  1.00 22.59 ? 152 ALA E CB  1 
ATOM   5645  N  N   . GLN E  1 180 ? 47.303  45.056  13.116  1.00 32.24 ? 153 GLN E N   1 
ATOM   5646  C  CA  . GLN E  1 180 ? 46.485  44.164  12.278  1.00 40.22 ? 153 GLN E CA  1 
ATOM   5647  C  C   . GLN E  1 180 ? 45.251  44.857  11.737  1.00 47.25 ? 153 GLN E C   1 
ATOM   5648  O  O   . GLN E  1 180 ? 44.550  45.615  12.445  1.00 48.75 ? 153 GLN E O   1 
ATOM   5649  C  CB  . GLN E  1 180 ? 46.041  42.926  13.061  1.00 41.79 ? 153 GLN E CB  1 
ATOM   5650  C  CG  . GLN E  1 180 ? 45.336  41.902  12.168  1.00 47.82 ? 153 GLN E CG  1 
ATOM   5651  C  CD  . GLN E  1 180 ? 45.027  40.620  12.913  1.00 52.73 ? 153 GLN E CD  1 
ATOM   5652  O  OE1 . GLN E  1 180 ? 44.367  40.649  13.949  1.00 49.44 ? 153 GLN E OE1 1 
ATOM   5653  N  NE2 . GLN E  1 180 ? 45.508  39.482  12.389  1.00 50.78 ? 153 GLN E NE2 1 
ATOM   5654  O  OXT . GLN E  1 180 ? 44.921  44.641  10.560  1.00 54.25 ? 153 GLN E OXT 1 
ATOM   5655  N  N   . ALA F  1 26  ? 66.116  58.820  3.568   1.00 69.55 ? -1  ALA F N   1 
ATOM   5656  C  CA  . ALA F  1 26  ? 66.925  57.739  4.187   1.00 69.43 ? -1  ALA F CA  1 
ATOM   5657  C  C   . ALA F  1 26  ? 66.175  56.401  4.050   1.00 72.26 ? -1  ALA F C   1 
ATOM   5658  O  O   . ALA F  1 26  ? 64.927  56.347  4.104   1.00 69.41 ? -1  ALA F O   1 
ATOM   5659  C  CB  . ALA F  1 26  ? 67.212  58.064  5.653   1.00 66.02 ? -1  ALA F CB  1 
ATOM   5660  N  N   . MET F  1 27  ? 66.930  55.334  3.803   1.00 65.18 ? 0   MET F N   1 
ATOM   5661  C  CA  . MET F  1 27  ? 66.456  53.983  4.121   1.00 59.37 ? 0   MET F CA  1 
ATOM   5662  C  C   . MET F  1 27  ? 67.146  53.647  5.437   1.00 50.18 ? 0   MET F C   1 
ATOM   5663  O  O   . MET F  1 27  ? 68.249  54.158  5.722   1.00 52.45 ? 0   MET F O   1 
ATOM   5664  C  CB  . MET F  1 27  ? 66.825  52.993  3.042   1.00 52.77 ? 0   MET F CB  1 
ATOM   5665  N  N   . ALA F  1 28  ? 66.493  52.841  6.260   1.00 42.56 ? 1   ALA F N   1 
ATOM   5666  C  CA  . ALA F  1 28  ? 67.002  52.609  7.613   1.00 39.52 ? 1   ALA F CA  1 
ATOM   5667  C  C   . ALA F  1 28  ? 68.288  51.763  7.584   1.00 33.63 ? 1   ALA F C   1 
ATOM   5668  O  O   . ALA F  1 28  ? 68.274  50.678  7.021   1.00 36.11 ? 1   ALA F O   1 
ATOM   5669  C  CB  . ALA F  1 28  ? 65.925  51.933  8.464   1.00 37.94 ? 1   ALA F CB  1 
ATOM   5670  N  N   A THR F  1 29  ? 69.359  52.286  8.192   0.50 32.28 ? 2   THR F N   1 
ATOM   5671  N  N   B THR F  1 29  ? 69.384  52.257  8.164   0.50 30.28 ? 2   THR F N   1 
ATOM   5672  C  CA  A THR F  1 29  ? 70.634  51.572  8.370   0.50 30.53 ? 2   THR F CA  1 
ATOM   5673  C  CA  B THR F  1 29  ? 70.584  51.420  8.344   0.50 27.32 ? 2   THR F CA  1 
ATOM   5674  C  C   A THR F  1 29  ? 70.785  50.945  9.773   0.50 31.32 ? 2   THR F C   1 
ATOM   5675  C  C   B THR F  1 29  ? 70.717  50.850  9.773   0.50 29.31 ? 2   THR F C   1 
ATOM   5676  O  O   A THR F  1 29  ? 71.582  50.018  9.951   0.50 28.60 ? 2   THR F O   1 
ATOM   5677  O  O   B THR F  1 29  ? 71.440  49.873  9.970   0.50 26.76 ? 2   THR F O   1 
ATOM   5678  C  CB  A THR F  1 29  ? 71.852  52.477  8.037   0.50 33.72 ? 2   THR F CB  1 
ATOM   5679  C  CB  B THR F  1 29  ? 71.892  52.104  7.866   0.50 27.99 ? 2   THR F CB  1 
ATOM   5680  O  OG1 A THR F  1 29  ? 73.011  51.669  7.839   0.50 38.58 ? 2   THR F OG1 1 
ATOM   5681  O  OG1 B THR F  1 29  ? 72.209  53.247  8.677   0.50 28.53 ? 2   THR F OG1 1 
ATOM   5682  C  CG2 A THR F  1 29  ? 72.142  53.512  9.133   0.50 34.07 ? 2   THR F CG2 1 
ATOM   5683  C  CG2 B THR F  1 29  ? 71.765  52.542  6.395   0.50 27.46 ? 2   THR F CG2 1 
ATOM   5684  N  N   . LYS F  1 30  ? 70.014  51.444  10.753  1.00 24.82 ? 3   LYS F N   1 
ATOM   5685  C  CA  . LYS F  1 30  ? 70.106  51.007  12.161  1.00 23.67 ? 3   LYS F CA  1 
ATOM   5686  C  C   . LYS F  1 30  ? 68.729  50.969  12.804  1.00 24.23 ? 3   LYS F C   1 
ATOM   5687  O  O   . LYS F  1 30  ? 67.854  51.776  12.449  1.00 23.25 ? 3   LYS F O   1 
ATOM   5688  C  CB  . LYS F  1 30  ? 70.992  51.977  12.948  1.00 28.94 ? 3   LYS F CB  1 
ATOM   5689  C  CG  . LYS F  1 30  ? 72.384  52.167  12.345  1.00 35.18 ? 3   LYS F CG  1 
ATOM   5690  C  CD  . LYS F  1 30  ? 73.446  52.198  13.425  1.00 46.99 ? 3   LYS F CD  1 
ATOM   5691  C  CE  . LYS F  1 30  ? 73.871  53.618  13.737  1.00 50.47 ? 3   LYS F CE  1 
ATOM   5692  N  NZ  . LYS F  1 30  ? 74.122  53.764  15.204  1.00 53.44 ? 3   LYS F NZ  1 
ATOM   5693  N  N   . ALA F  1 31  ? 68.490  49.999  13.679  1.00 21.42 ? 4   ALA F N   1 
ATOM   5694  C  CA  . ALA F  1 31  ? 67.244  49.901  14.419  1.00 19.86 ? 4   ALA F CA  1 
ATOM   5695  C  C   . ALA F  1 31  ? 67.608  49.426  15.839  1.00 23.46 ? 4   ALA F C   1 
ATOM   5696  O  O   . ALA F  1 31  ? 68.764  48.999  16.103  1.00 23.67 ? 4   ALA F O   1 
ATOM   5697  C  CB  . ALA F  1 31  ? 66.259  48.967  13.775  1.00 18.70 ? 4   ALA F CB  1 
ATOM   5698  N  N   . VAL F  1 32  ? 66.649  49.534  16.757  1.00 22.02 ? 5   VAL F N   1 
ATOM   5699  C  CA  . VAL F  1 32  ? 66.942  49.180  18.171  1.00 21.51 ? 5   VAL F CA  1 
ATOM   5700  C  C   . VAL F  1 32  ? 65.642  48.661  18.705  1.00 22.50 ? 5   VAL F C   1 
ATOM   5701  O  O   . VAL F  1 32  ? 64.555  48.975  18.180  1.00 23.48 ? 5   VAL F O   1 
ATOM   5702  C  CB  . VAL F  1 32  ? 67.524  50.345  18.985  1.00 24.81 ? 5   VAL F CB  1 
ATOM   5703  C  CG1 . VAL F  1 32  ? 66.469  51.441  19.184  1.00 23.59 ? 5   VAL F CG1 1 
ATOM   5704  C  CG2 . VAL F  1 32  ? 67.991  49.807  20.331  1.00 26.49 ? 5   VAL F CG2 1 
ATOM   5705  N  N   . CYS F  1 33  ? 65.711  47.769  19.696  1.00 22.14 ? 6   CYS F N   1 
ATOM   5706  C  CA  . CYS F  1 33  ? 64.520  47.281  20.277  1.00 21.78 ? 6   CYS F CA  1 
ATOM   5707  C  C   . CYS F  1 33  ? 64.770  47.163  21.806  1.00 24.75 ? 6   CYS F C   1 
ATOM   5708  O  O   . CYS F  1 33  ? 65.825  46.640  22.194  1.00 20.64 ? 6   CYS F O   1 
ATOM   5709  C  CB  . CYS F  1 33  ? 64.181  45.924  19.698  1.00 23.22 ? 6   CYS F CB  1 
ATOM   5710  S  SG  . CYS F  1 33  ? 62.719  45.182  20.433  1.00 26.29 ? 6   CYS F SG  1 
ATOM   5711  N  N   . VAL F  1 34  ? 63.837  47.677  22.627  1.00 21.27 ? 7   VAL F N   1 
ATOM   5712  C  CA  . VAL F  1 34  ? 63.925  47.534  24.089  1.00 22.33 ? 7   VAL F CA  1 
ATOM   5713  C  C   . VAL F  1 34  ? 62.940  46.446  24.495  1.00 22.83 ? 7   VAL F C   1 
ATOM   5714  O  O   . VAL F  1 34  ? 61.767  46.590  24.274  1.00 20.83 ? 7   VAL F O   1 
ATOM   5715  C  CB  . VAL F  1 34  ? 63.662  48.875  24.821  1.00 23.84 ? 7   VAL F CB  1 
ATOM   5716  C  CG1 . VAL F  1 34  ? 63.625  48.657  26.354  1.00 25.08 ? 7   VAL F CG1 1 
ATOM   5717  C  CG2 . VAL F  1 34  ? 64.732  49.890  24.429  1.00 24.32 ? 7   VAL F CG2 1 
ATOM   5718  N  N   . LEU F  1 35  ? 63.429  45.318  25.046  1.00 22.24 ? 8   LEU F N   1 
ATOM   5719  C  CA  . LEU F  1 35  ? 62.542  44.231  25.411  1.00 22.13 ? 8   LEU F CA  1 
ATOM   5720  C  C   . LEU F  1 35  ? 62.105  44.370  26.878  1.00 22.34 ? 8   LEU F C   1 
ATOM   5721  O  O   . LEU F  1 35  ? 62.951  44.630  27.747  1.00 23.27 ? 8   LEU F O   1 
ATOM   5722  C  CB  . LEU F  1 35  ? 63.290  42.893  25.264  1.00 25.00 ? 8   LEU F CB  1 
ATOM   5723  C  CG  . LEU F  1 35  ? 63.754  42.623  23.823  1.00 26.74 ? 8   LEU F CG  1 
ATOM   5724  C  CD1 . LEU F  1 35  ? 64.879  41.593  23.879  1.00 34.72 ? 8   LEU F CD1 1 
ATOM   5725  C  CD2 . LEU F  1 35  ? 62.586  41.957  23.170  1.00 27.02 ? 8   LEU F CD2 1 
ATOM   5726  N  N   . LYS F  1 36  ? 60.815  44.193  27.119  1.00 23.40 ? 9   LYS F N   1 
ATOM   5727  C  CA  . LYS F  1 36  ? 60.253  44.314  28.474  1.00 27.19 ? 9   LYS F CA  1 
ATOM   5728  C  C   . LYS F  1 36  ? 59.150  43.352  28.545  1.00 23.42 ? 9   LYS F C   1 
ATOM   5729  O  O   . LYS F  1 36  ? 58.511  43.094  27.568  1.00 24.96 ? 9   LYS F O   1 
ATOM   5730  C  CB  . LYS F  1 36  ? 59.682  45.729  28.709  1.00 28.98 ? 9   LYS F CB  1 
ATOM   5731  C  CG  . LYS F  1 36  ? 60.723  46.695  29.221  1.00 42.66 ? 9   LYS F CG  1 
ATOM   5732  C  CD  . LYS F  1 36  ? 60.052  47.997  29.696  1.00 50.18 ? 9   LYS F CD  1 
ATOM   5733  C  CE  . LYS F  1 36  ? 60.766  49.236  29.153  1.00 51.42 ? 9   LYS F CE  1 
ATOM   5734  N  NZ  . LYS F  1 36  ? 62.132  49.362  29.727  1.00 55.92 ? 9   LYS F NZ  1 
ATOM   5735  N  N   . GLY F  1 37  ? 58.863  42.822  29.734  1.00 24.10 ? 10  GLY F N   1 
ATOM   5736  C  CA  . GLY F  1 37  ? 57.663  42.040  29.870  1.00 23.34 ? 10  GLY F CA  1 
ATOM   5737  C  C   . GLY F  1 37  ? 57.065  42.116  31.276  1.00 29.63 ? 10  GLY F C   1 
ATOM   5738  O  O   . GLY F  1 37  ? 57.290  43.084  32.006  1.00 29.36 ? 10  GLY F O   1 
ATOM   5739  N  N   . ASP F  1 38  ? 56.306  41.099  31.655  1.00 32.30 ? 11  ASP F N   1 
ATOM   5740  C  CA  . ASP F  1 38  ? 55.624  41.122  32.969  1.00 38.02 ? 11  ASP F CA  1 
ATOM   5741  C  C   . ASP F  1 38  ? 56.465  40.602  34.122  1.00 37.64 ? 11  ASP F C   1 
ATOM   5742  O  O   . ASP F  1 38  ? 56.109  40.789  35.292  1.00 42.26 ? 11  ASP F O   1 
ATOM   5743  C  CB  . ASP F  1 38  ? 54.314  40.368  32.914  1.00 38.64 ? 11  ASP F CB  1 
ATOM   5744  C  CG  . ASP F  1 38  ? 53.264  41.154  32.205  1.00 49.45 ? 11  ASP F CG  1 
ATOM   5745  O  OD1 . ASP F  1 38  ? 53.302  42.414  32.296  1.00 49.32 ? 11  ASP F OD1 1 
ATOM   5746  O  OD2 . ASP F  1 38  ? 52.434  40.527  31.526  1.00 54.66 ? 11  ASP F OD2 1 
ATOM   5747  N  N   . GLY F  1 39  ? 57.559  39.942  33.765  1.00 34.75 ? 12  GLY F N   1 
ATOM   5748  C  CA  . GLY F  1 39  ? 58.523  39.421  34.707  1.00 35.09 ? 12  GLY F CA  1 
ATOM   5749  C  C   . GLY F  1 39  ? 59.791  40.237  34.612  1.00 31.55 ? 12  GLY F C   1 
ATOM   5750  O  O   . GLY F  1 39  ? 59.788  41.407  34.231  1.00 32.34 ? 12  GLY F O   1 
ATOM   5751  N  N   . PRO F  1 40  ? 60.915  39.626  34.963  1.00 28.99 ? 13  PRO F N   1 
ATOM   5752  C  CA  . PRO F  1 40  ? 62.183  40.348  35.116  1.00 26.96 ? 13  PRO F CA  1 
ATOM   5753  C  C   . PRO F  1 40  ? 63.000  40.385  33.809  1.00 27.01 ? 13  PRO F C   1 
ATOM   5754  O  O   . PRO F  1 40  ? 64.128  40.895  33.797  1.00 30.07 ? 13  PRO F O   1 
ATOM   5755  C  CB  . PRO F  1 40  ? 62.933  39.467  36.151  1.00 27.46 ? 13  PRO F CB  1 
ATOM   5756  C  CG  . PRO F  1 40  ? 62.415  38.103  35.852  1.00 27.26 ? 13  PRO F CG  1 
ATOM   5757  C  CD  . PRO F  1 40  ? 61.002  38.215  35.395  1.00 30.05 ? 13  PRO F CD  1 
ATOM   5758  N  N   . VAL F  1 41  ? 62.480  39.801  32.741  1.00 29.38 ? 14  VAL F N   1 
ATOM   5759  C  CA  . VAL F  1 41  ? 63.310  39.700  31.515  1.00 29.64 ? 14  VAL F CA  1 
ATOM   5760  C  C   . VAL F  1 41  ? 63.474  41.073  30.857  1.00 30.74 ? 14  VAL F C   1 
ATOM   5761  O  O   . VAL F  1 41  ? 62.490  41.733  30.588  1.00 29.92 ? 14  VAL F O   1 
ATOM   5762  C  CB  . VAL F  1 41  ? 62.764  38.676  30.524  1.00 29.96 ? 14  VAL F CB  1 
ATOM   5763  C  CG1 . VAL F  1 41  ? 63.601  38.697  29.231  1.00 32.20 ? 14  VAL F CG1 1 
ATOM   5764  C  CG2 . VAL F  1 41  ? 62.816  37.277  31.162  1.00 30.64 ? 14  VAL F CG2 1 
ATOM   5765  N  N   . GLN F  1 42  ? 64.694  41.512  30.609  1.00 30.09 ? 15  GLN F N   1 
ATOM   5766  C  CA  . GLN F  1 42  ? 64.830  42.746  29.842  1.00 34.96 ? 15  GLN F CA  1 
ATOM   5767  C  C   . GLN F  1 42  ? 66.129  42.888  29.073  1.00 32.01 ? 15  GLN F C   1 
ATOM   5768  O  O   . GLN F  1 42  ? 67.161  42.303  29.434  1.00 32.06 ? 15  GLN F O   1 
ATOM   5769  C  CB  . GLN F  1 42  ? 64.636  43.953  30.741  1.00 38.51 ? 15  GLN F CB  1 
ATOM   5770  C  CG  . GLN F  1 42  ? 65.734  44.179  31.742  1.00 39.59 ? 15  GLN F CG  1 
ATOM   5771  C  CD  . GLN F  1 42  ? 65.215  45.011  32.916  1.00 50.52 ? 15  GLN F CD  1 
ATOM   5772  O  OE1 . GLN F  1 42  ? 64.017  45.053  33.156  1.00 55.81 ? 15  GLN F OE1 1 
ATOM   5773  N  NE2 . GLN F  1 42  ? 66.107  45.676  33.630  1.00 50.34 ? 15  GLN F NE2 1 
ATOM   5774  N  N   . GLY F  1 43  ? 66.111  43.710  28.023  1.00 27.20 ? 16  GLY F N   1 
ATOM   5775  C  CA  . GLY F  1 43  ? 67.293  43.811  27.194  1.00 27.60 ? 16  GLY F CA  1 
ATOM   5776  C  C   . GLY F  1 43  ? 67.141  44.851  26.120  1.00 28.12 ? 16  GLY F C   1 
ATOM   5777  O  O   . GLY F  1 43  ? 66.067  45.395  25.962  1.00 24.30 ? 16  GLY F O   1 
ATOM   5778  N  N   . ILE F  1 44  ? 68.266  45.149  25.485  1.00 26.32 ? 17  ILE F N   1 
ATOM   5779  C  CA  . ILE F  1 44  ? 68.399  46.126  24.425  1.00 24.56 ? 17  ILE F CA  1 
ATOM   5780  C  C   . ILE F  1 44  ? 69.103  45.350  23.300  1.00 28.74 ? 17  ILE F C   1 
ATOM   5781  O  O   . ILE F  1 44  ? 70.251  44.788  23.489  1.00 24.56 ? 17  ILE F O   1 
ATOM   5782  C  CB  . ILE F  1 44  ? 69.261  47.326  24.855  1.00 27.19 ? 17  ILE F CB  1 
ATOM   5783  C  CG1 . ILE F  1 44  ? 68.559  48.141  25.998  1.00 27.19 ? 17  ILE F CG1 1 
ATOM   5784  C  CG2 . ILE F  1 44  ? 69.622  48.208  23.644  1.00 26.28 ? 17  ILE F CG2 1 
ATOM   5785  C  CD1 . ILE F  1 44  ? 69.420  49.273  26.539  1.00 30.77 ? 17  ILE F CD1 1 
ATOM   5786  N  N   . ILE F  1 45  ? 68.429  45.305  22.151  1.00 24.90 ? 18  ILE F N   1 
ATOM   5787  C  CA  . ILE F  1 45  ? 68.965  44.651  20.950  1.00 23.87 ? 18  ILE F CA  1 
ATOM   5788  C  C   . ILE F  1 45  ? 69.109  45.680  19.856  1.00 28.60 ? 18  ILE F C   1 
ATOM   5789  O  O   . ILE F  1 45  ? 68.124  46.447  19.583  1.00 26.06 ? 18  ILE F O   1 
ATOM   5790  C  CB  . ILE F  1 45  ? 68.017  43.529  20.516  1.00 23.02 ? 18  ILE F CB  1 
ATOM   5791  C  CG1 . ILE F  1 45  ? 67.926  42.419  21.590  1.00 27.49 ? 18  ILE F CG1 1 
ATOM   5792  C  CG2 . ILE F  1 45  ? 68.443  42.961  19.173  1.00 23.78 ? 18  ILE F CG2 1 
ATOM   5793  C  CD1 . ILE F  1 45  ? 69.269  41.734  21.890  1.00 28.57 ? 18  ILE F CD1 1 
ATOM   5794  N  N   . ASN F  1 46  ? 70.310  45.741  19.277  1.00 23.40 ? 19  ASN F N   1 
ATOM   5795  C  CA  . ASN F  1 46  ? 70.634  46.618  18.174  1.00 24.54 ? 19  ASN F CA  1 
ATOM   5796  C  C   . ASN F  1 46  ? 70.645  45.894  16.814  1.00 28.24 ? 19  ASN F C   1 
ATOM   5797  O  O   . ASN F  1 46  ? 70.867  44.653  16.721  1.00 25.10 ? 19  ASN F O   1 
ATOM   5798  C  CB  . ASN F  1 46  ? 72.009  47.204  18.412  1.00 28.96 ? 19  ASN F CB  1 
ATOM   5799  C  CG  . ASN F  1 46  ? 72.125  47.867  19.757  1.00 34.71 ? 19  ASN F CG  1 
ATOM   5800  O  OD1 . ASN F  1 46  ? 72.759  47.342  20.694  1.00 35.19 ? 19  ASN F OD1 1 
ATOM   5801  N  ND2 . ASN F  1 46  ? 71.511  49.029  19.869  1.00 27.63 ? 19  ASN F ND2 1 
ATOM   5802  N  N   . PHE F  1 47  ? 70.374  46.657  15.746  1.00 24.79 ? 20  PHE F N   1 
ATOM   5803  C  CA  . PHE F  1 47  ? 70.345  46.096  14.415  1.00 25.60 ? 20  PHE F CA  1 
ATOM   5804  C  C   . PHE F  1 47  ? 71.094  47.058  13.545  1.00 26.24 ? 20  PHE F C   1 
ATOM   5805  O  O   . PHE F  1 47  ? 70.934  48.299  13.675  1.00 23.47 ? 20  PHE F O   1 
ATOM   5806  C  CB  . PHE F  1 47  ? 68.947  45.988  13.827  1.00 25.27 ? 20  PHE F CB  1 
ATOM   5807  C  CG  . PHE F  1 47  ? 68.015  45.133  14.590  1.00 29.15 ? 20  PHE F CG  1 
ATOM   5808  C  CD1 . PHE F  1 47  ? 67.340  45.627  15.748  1.00 26.42 ? 20  PHE F CD1 1 
ATOM   5809  C  CD2 . PHE F  1 47  ? 67.702  43.882  14.133  1.00 26.73 ? 20  PHE F CD2 1 
ATOM   5810  C  CE1 . PHE F  1 47  ? 66.426  44.832  16.404  1.00 25.99 ? 20  PHE F CE1 1 
ATOM   5811  C  CE2 . PHE F  1 47  ? 66.791  43.066  14.812  1.00 28.79 ? 20  PHE F CE2 1 
ATOM   5812  C  CZ  . PHE F  1 47  ? 66.145  43.556  15.948  1.00 27.32 ? 20  PHE F CZ  1 
ATOM   5813  N  N   . GLU F  1 48  ? 71.943  46.505  12.666  1.00 25.55 ? 21  GLU F N   1 
ATOM   5814  C  CA  . GLU F  1 48  ? 72.686  47.332  11.721  1.00 27.90 ? 21  GLU F CA  1 
ATOM   5815  C  C   . GLU F  1 48  ? 72.763  46.678  10.341  1.00 29.08 ? 21  GLU F C   1 
ATOM   5816  O  O   . GLU F  1 48  ? 73.035  45.462  10.231  1.00 28.06 ? 21  GLU F O   1 
ATOM   5817  C  CB  . GLU F  1 48  ? 74.072  47.704  12.242  1.00 33.27 ? 21  GLU F CB  1 
ATOM   5818  C  CG  . GLU F  1 48  ? 74.786  48.680  11.311  1.00 40.51 ? 21  GLU F CG  1 
ATOM   5819  C  CD  . GLU F  1 48  ? 76.065  49.287  11.901  1.00 55.63 ? 21  GLU F CD  1 
ATOM   5820  O  OE1 . GLU F  1 48  ? 76.990  48.532  12.293  1.00 55.36 ? 21  GLU F OE1 1 
ATOM   5821  O  OE2 . GLU F  1 48  ? 76.158  50.535  11.958  1.00 57.74 ? 21  GLU F OE2 1 
ATOM   5822  N  N   . GLN F  1 49  ? 72.506  47.468  9.287   1.00 24.48 ? 22  GLN F N   1 
ATOM   5823  C  CA  . GLN F  1 49  ? 72.492  46.909  7.933   1.00 27.85 ? 22  GLN F CA  1 
ATOM   5824  C  C   . GLN F  1 49  ? 73.097  47.962  7.055   1.00 31.99 ? 22  GLN F C   1 
ATOM   5825  O  O   . GLN F  1 49  ? 72.406  48.891  6.641   1.00 29.15 ? 22  GLN F O   1 
ATOM   5826  C  CB  . GLN F  1 49  ? 71.098  46.520  7.481   1.00 25.97 ? 22  GLN F CB  1 
ATOM   5827  C  CG  . GLN F  1 49  ? 71.036  45.716  6.179   1.00 24.99 ? 22  GLN F CG  1 
ATOM   5828  C  CD  . GLN F  1 49  ? 69.626  45.571  5.687   1.00 26.21 ? 22  GLN F CD  1 
ATOM   5829  O  OE1 . GLN F  1 49  ? 68.731  46.323  6.106   1.00 23.02 ? 22  GLN F OE1 1 
ATOM   5830  N  NE2 . GLN F  1 49  ? 69.391  44.603  4.807   1.00 22.92 ? 22  GLN F NE2 1 
ATOM   5831  N  N   . LYS F  1 50  ? 74.409  47.841  6.855   1.00 30.25 ? 23  LYS F N   1 
ATOM   5832  C  CA  . LYS F  1 50  ? 75.210  48.810  6.119   1.00 34.77 ? 23  LYS F CA  1 
ATOM   5833  C  C   . LYS F  1 50  ? 74.774  48.880  4.678   1.00 33.80 ? 23  LYS F C   1 
ATOM   5834  O  O   . LYS F  1 50  ? 74.793  49.949  4.104   1.00 34.30 ? 23  LYS F O   1 
ATOM   5835  C  CB  . LYS F  1 50  ? 76.695  48.412  6.141   1.00 40.33 ? 23  LYS F CB  1 
ATOM   5836  C  CG  . LYS F  1 50  ? 77.327  48.394  7.514   1.00 50.90 ? 23  LYS F CG  1 
ATOM   5837  C  CD  . LYS F  1 50  ? 77.368  49.785  8.149   1.00 51.02 ? 23  LYS F CD  1 
ATOM   5838  C  CE  . LYS F  1 50  ? 78.709  49.960  8.859   1.00 62.14 ? 23  LYS F CE  1 
ATOM   5839  N  NZ  . LYS F  1 50  ? 78.817  51.205  9.678   1.00 65.24 ? 23  LYS F NZ  1 
ATOM   5840  N  N   . GLU F  1 51  ? 74.370  47.747  4.106   1.00 30.79 ? 24  GLU F N   1 
ATOM   5841  C  CA  . GLU F  1 51  ? 73.936  47.703  2.703   1.00 33.68 ? 24  GLU F CA  1 
ATOM   5842  C  C   . GLU F  1 51  ? 72.553  47.117  2.644   1.00 27.62 ? 24  GLU F C   1 
ATOM   5843  O  O   . GLU F  1 51  ? 72.297  46.083  3.227   1.00 25.09 ? 24  GLU F O   1 
ATOM   5844  C  CB  . GLU F  1 51  ? 74.891  46.800  1.863   1.00 38.25 ? 24  GLU F CB  1 
ATOM   5845  C  CG  . GLU F  1 51  ? 76.329  47.305  1.853   1.00 49.78 ? 24  GLU F CG  1 
ATOM   5846  C  CD  . GLU F  1 51  ? 76.485  48.598  1.042   1.00 65.19 ? 24  GLU F CD  1 
ATOM   5847  O  OE1 . GLU F  1 51  ? 75.538  48.960  0.286   1.00 64.73 ? 24  GLU F OE1 1 
ATOM   5848  O  OE2 . GLU F  1 51  ? 77.555  49.263  1.141   1.00 68.64 ? 24  GLU F OE2 1 
ATOM   5849  N  N   . SER F  1 52  ? 71.659  47.748  1.882   1.00 24.60 ? 25  SER F N   1 
ATOM   5850  C  CA  . SER F  1 52  ? 70.284  47.308  1.842   1.00 23.26 ? 25  SER F CA  1 
ATOM   5851  C  C   . SER F  1 52  ? 70.107  45.929  1.256   1.00 24.42 ? 25  SER F C   1 
ATOM   5852  O  O   . SER F  1 52  ? 69.095  45.239  1.467   1.00 21.33 ? 25  SER F O   1 
ATOM   5853  C  CB  . SER F  1 52  ? 69.447  48.335  1.051   1.00 28.21 ? 25  SER F CB  1 
ATOM   5854  O  OG  . SER F  1 52  ? 69.960  48.499  -0.265  1.00 29.01 ? 25  SER F OG  1 
ATOM   5855  N  N   . ASN F  1 53  ? 71.085  45.498  0.462   1.00 25.73 ? 26  ASN F N   1 
ATOM   5856  C  CA  . ASN F  1 53  ? 70.968  44.164  -0.077  1.00 28.16 ? 26  ASN F CA  1 
ATOM   5857  C  C   . ASN F  1 53  ? 71.928  43.211  0.625   1.00 31.87 ? 26  ASN F C   1 
ATOM   5858  O  O   . ASN F  1 53  ? 72.206  42.151  0.100   1.00 34.94 ? 26  ASN F O   1 
ATOM   5859  C  CB  . ASN F  1 53  ? 71.177  44.159  -1.629  1.00 29.17 ? 26  ASN F CB  1 
ATOM   5860  C  CG  . ASN F  1 53  ? 72.564  44.612  -2.043  1.00 27.83 ? 26  ASN F CG  1 
ATOM   5861  O  OD1 . ASN F  1 53  ? 73.179  45.436  -1.396  1.00 28.75 ? 26  ASN F OD1 1 
ATOM   5862  N  ND2 . ASN F  1 53  ? 73.075  44.050  -3.164  1.00 29.16 ? 26  ASN F ND2 1 
ATOM   5863  N  N   . GLY F  1 54  ? 72.456  43.630  1.774   1.00 30.70 ? 27  GLY F N   1 
ATOM   5864  C  CA  . GLY F  1 54  ? 73.360  42.840  2.577   1.00 28.78 ? 27  GLY F CA  1 
ATOM   5865  C  C   . GLY F  1 54  ? 72.707  42.350  3.891   1.00 28.76 ? 27  GLY F C   1 
ATOM   5866  O  O   . GLY F  1 54  ? 71.511  42.572  4.146   1.00 25.48 ? 27  GLY F O   1 
ATOM   5867  N  N   . PRO F  1 55  ? 73.494  41.651  4.722   1.00 29.78 ? 28  PRO F N   1 
ATOM   5868  C  CA  . PRO F  1 55  ? 72.878  41.065  5.917   1.00 29.06 ? 28  PRO F CA  1 
ATOM   5869  C  C   . PRO F  1 55  ? 72.735  42.084  7.043   1.00 24.90 ? 28  PRO F C   1 
ATOM   5870  O  O   . PRO F  1 55  ? 73.413  43.129  7.061   1.00 26.87 ? 28  PRO F O   1 
ATOM   5871  C  CB  . PRO F  1 55  ? 73.845  39.924  6.314   1.00 30.17 ? 28  PRO F CB  1 
ATOM   5872  C  CG  . PRO F  1 55  ? 75.173  40.326  5.711   1.00 33.23 ? 28  PRO F CG  1 
ATOM   5873  C  CD  . PRO F  1 55  ? 74.856  41.130  4.457   1.00 31.66 ? 28  PRO F CD  1 
ATOM   5874  N  N   . VAL F  1 56  ? 71.859  41.745  7.971   1.00 27.94 ? 29  VAL F N   1 
ATOM   5875  C  CA  . VAL F  1 56  ? 71.643  42.535  9.177   1.00 26.10 ? 29  VAL F CA  1 
ATOM   5876  C  C   . VAL F  1 56  ? 72.427  41.953  10.371  1.00 24.84 ? 29  VAL F C   1 
ATOM   5877  O  O   . VAL F  1 56  ? 72.236  40.803  10.700  1.00 27.14 ? 29  VAL F O   1 
ATOM   5878  C  CB  . VAL F  1 56  ? 70.139  42.517  9.528   1.00 23.16 ? 29  VAL F CB  1 
ATOM   5879  C  CG1 . VAL F  1 56  ? 69.860  43.403  10.744  1.00 23.06 ? 29  VAL F CG1 1 
ATOM   5880  C  CG2 . VAL F  1 56  ? 69.316  43.015  8.323   1.00 21.71 ? 29  VAL F CG2 1 
ATOM   5881  N  N   . LYS F  1 57  ? 73.233  42.768  11.029  1.00 25.03 ? 30  LYS F N   1 
ATOM   5882  C  CA  . LYS F  1 57  ? 73.884  42.363  12.262  1.00 26.49 ? 30  LYS F CA  1 
ATOM   5883  C  C   . LYS F  1 57  ? 72.961  42.681  13.427  1.00 29.65 ? 30  LYS F C   1 
ATOM   5884  O  O   . LYS F  1 57  ? 72.403  43.797  13.499  1.00 28.31 ? 30  LYS F O   1 
ATOM   5885  C  CB  . LYS F  1 57  ? 75.192  43.098  12.439  1.00 32.57 ? 30  LYS F CB  1 
ATOM   5886  C  CG  . LYS F  1 57  ? 76.057  43.048  11.186  1.00 41.15 ? 30  LYS F CG  1 
ATOM   5887  C  CD  . LYS F  1 57  ? 77.559  42.922  11.439  1.00 44.35 ? 30  LYS F CD  1 
ATOM   5888  C  CE  . LYS F  1 57  ? 78.172  44.173  12.032  1.00 52.35 ? 30  LYS F CE  1 
ATOM   5889  N  NZ  . LYS F  1 57  ? 78.062  44.115  13.519  1.00 61.99 ? 30  LYS F NZ  1 
ATOM   5890  N  N   . VAL F  1 58  ? 72.776  41.700  14.319  1.00 28.78 ? 31  VAL F N   1 
ATOM   5891  C  CA  . VAL F  1 58  ? 71.851  41.811  15.461  1.00 28.00 ? 31  VAL F CA  1 
ATOM   5892  C  C   . VAL F  1 58  ? 72.704  41.581  16.718  1.00 32.14 ? 31  VAL F C   1 
ATOM   5893  O  O   . VAL F  1 58  ? 73.363  40.516  16.823  1.00 30.59 ? 31  VAL F O   1 
ATOM   5894  C  CB  . VAL F  1 58  ? 70.713  40.772  15.378  1.00 26.40 ? 31  VAL F CB  1 
ATOM   5895  C  CG1 . VAL F  1 58  ? 69.685  41.002  16.488  1.00 27.98 ? 31  VAL F CG1 1 
ATOM   5896  C  CG2 . VAL F  1 58  ? 69.997  40.809  14.033  1.00 28.38 ? 31  VAL F CG2 1 
ATOM   5897  N  N   . TRP F  1 59  ? 72.796  42.555  17.621  1.00 27.97 ? 32  TRP F N   1 
ATOM   5898  C  CA  . TRP F  1 59  ? 73.598  42.329  18.832  1.00 27.69 ? 32  TRP F CA  1 
ATOM   5899  C  C   . TRP F  1 59  ? 73.078  43.084  20.024  1.00 32.99 ? 32  TRP F C   1 
ATOM   5900  O  O   . TRP F  1 59  ? 72.457  44.165  19.882  1.00 27.42 ? 32  TRP F O   1 
ATOM   5901  C  CB  . TRP F  1 59  ? 75.051  42.738  18.633  1.00 28.84 ? 32  TRP F CB  1 
ATOM   5902  C  CG  . TRP F  1 59  ? 75.327  44.210  18.698  1.00 31.61 ? 32  TRP F CG  1 
ATOM   5903  C  CD1 . TRP F  1 59  ? 75.830  44.902  19.763  1.00 33.64 ? 32  TRP F CD1 1 
ATOM   5904  C  CD2 . TRP F  1 59  ? 75.099  45.163  17.672  1.00 32.68 ? 32  TRP F CD2 1 
ATOM   5905  N  NE1 . TRP F  1 59  ? 75.946  46.229  19.458  1.00 36.87 ? 32  TRP F NE1 1 
ATOM   5906  C  CE2 . TRP F  1 59  ? 75.509  46.423  18.175  1.00 35.99 ? 32  TRP F CE2 1 
ATOM   5907  C  CE3 . TRP F  1 59  ? 74.594  45.080  16.365  1.00 35.84 ? 32  TRP F CE3 1 
ATOM   5908  C  CZ2 . TRP F  1 59  ? 75.442  47.598  17.418  1.00 37.03 ? 32  TRP F CZ2 1 
ATOM   5909  C  CZ3 . TRP F  1 59  ? 74.509  46.267  15.598  1.00 36.49 ? 32  TRP F CZ3 1 
ATOM   5910  C  CH2 . TRP F  1 59  ? 74.947  47.499  16.126  1.00 37.99 ? 32  TRP F CH2 1 
ATOM   5911  N  N   . GLY F  1 60  ? 73.339  42.535  21.210  1.00 28.04 ? 33  GLY F N   1 
ATOM   5912  C  CA  . GLY F  1 60  ? 73.085  43.333  22.427  1.00 29.13 ? 33  GLY F CA  1 
ATOM   5913  C  C   . GLY F  1 60  ? 73.043  42.361  23.585  1.00 32.35 ? 33  GLY F C   1 
ATOM   5914  O  O   . GLY F  1 60  ? 73.739  41.338  23.553  1.00 27.44 ? 33  GLY F O   1 
ATOM   5915  N  N   . SER F  1 61  ? 72.244  42.671  24.600  1.00 30.48 ? 34  SER F N   1 
ATOM   5916  C  CA  . SER F  1 61  ? 72.222  41.828  25.800  1.00 32.64 ? 34  SER F CA  1 
ATOM   5917  C  C   . SER F  1 61  ? 70.814  41.728  26.370  1.00 30.84 ? 34  SER F C   1 
ATOM   5918  O  O   . SER F  1 61  ? 70.027  42.702  26.300  1.00 28.44 ? 34  SER F O   1 
ATOM   5919  C  CB  . SER F  1 61  ? 73.229  42.402  26.794  1.00 34.70 ? 34  SER F CB  1 
ATOM   5920  O  OG  . SER F  1 61  ? 73.347  41.529  27.895  1.00 44.87 ? 34  SER F OG  1 
ATOM   5921  N  N   . ILE F  1 62  ? 70.458  40.530  26.829  1.00 28.90 ? 35  ILE F N   1 
ATOM   5922  C  CA  . ILE F  1 62  ? 69.212  40.280  27.507  1.00 24.69 ? 35  ILE F CA  1 
ATOM   5923  C  C   . ILE F  1 62  ? 69.552  39.725  28.926  1.00 34.98 ? 35  ILE F C   1 
ATOM   5924  O  O   . ILE F  1 62  ? 70.373  38.790  29.051  1.00 32.45 ? 35  ILE F O   1 
ATOM   5925  C  CB  . ILE F  1 62  ? 68.346  39.288  26.767  1.00 24.34 ? 35  ILE F CB  1 
ATOM   5926  C  CG1 . ILE F  1 62  ? 68.123  39.674  25.284  1.00 26.57 ? 35  ILE F CG1 1 
ATOM   5927  C  CG2 . ILE F  1 62  ? 66.942  39.172  27.387  1.00 24.72 ? 35  ILE F CG2 1 
ATOM   5928  C  CD1 . ILE F  1 62  ? 67.054  38.811  24.613  1.00 24.11 ? 35  ILE F CD1 1 
ATOM   5929  N  N   . LYS F  1 63  ? 68.924  40.290  29.973  1.00 31.35 ? 36  LYS F N   1 
ATOM   5930  C  CA  . LYS F  1 63  ? 69.023  39.749  31.348  1.00 29.80 ? 36  LYS F CA  1 
ATOM   5931  C  C   . LYS F  1 63  ? 67.701  39.274  31.936  1.00 28.96 ? 36  LYS F C   1 
ATOM   5932  O  O   . LYS F  1 63  ? 66.589  39.451  31.371  1.00 28.60 ? 36  LYS F O   1 
ATOM   5933  C  CB  . LYS F  1 63  ? 69.725  40.770  32.235  1.00 33.01 ? 36  LYS F CB  1 
ATOM   5934  C  CG  . LYS F  1 63  ? 68.893  41.994  32.574  1.00 35.12 ? 36  LYS F CG  1 
ATOM   5935  C  CD  . LYS F  1 63  ? 69.813  43.062  33.166  1.00 39.88 ? 36  LYS F CD  1 
ATOM   5936  C  CE  . LYS F  1 63  ? 69.048  44.321  33.523  1.00 42.60 ? 36  LYS F CE  1 
ATOM   5937  N  NZ  . LYS F  1 63  ? 70.031  45.369  33.895  1.00 45.41 ? 36  LYS F NZ  1 
ATOM   5938  N  N   . GLY F  1 64  ? 67.797  38.609  33.086  1.00 31.42 ? 37  GLY F N   1 
ATOM   5939  C  CA  . GLY F  1 64  ? 66.626  38.076  33.746  1.00 26.37 ? 37  GLY F CA  1 
ATOM   5940  C  C   . GLY F  1 64  ? 66.154  36.753  33.229  1.00 27.82 ? 37  GLY F C   1 
ATOM   5941  O  O   . GLY F  1 64  ? 65.020  36.353  33.495  1.00 29.34 ? 37  GLY F O   1 
ATOM   5942  N  N   . LEU F  1 65  ? 67.028  36.047  32.489  1.00 27.50 ? 38  LEU F N   1 
ATOM   5943  C  CA  . LEU F  1 65  ? 66.649  34.798  31.860  1.00 30.06 ? 38  LEU F CA  1 
ATOM   5944  C  C   . LEU F  1 65  ? 67.170  33.610  32.697  1.00 29.53 ? 38  LEU F C   1 
ATOM   5945  O  O   . LEU F  1 65  ? 68.233  33.715  33.312  1.00 30.93 ? 38  LEU F O   1 
ATOM   5946  C  CB  . LEU F  1 65  ? 67.265  34.705  30.443  1.00 30.72 ? 38  LEU F CB  1 
ATOM   5947  C  CG  . LEU F  1 65  ? 66.653  35.632  29.341  1.00 31.15 ? 38  LEU F CG  1 
ATOM   5948  C  CD1 . LEU F  1 65  ? 67.573  35.758  28.128  1.00 31.65 ? 38  LEU F CD1 1 
ATOM   5949  C  CD2 . LEU F  1 65  ? 65.279  35.154  28.950  1.00 25.81 ? 38  LEU F CD2 1 
ATOM   5950  N  N   . THR F  1 66  ? 66.429  32.517  32.690  1.00 31.66 ? 39  THR F N   1 
ATOM   5951  C  CA  . THR F  1 66  ? 66.962  31.229  33.194  1.00 37.93 ? 39  THR F CA  1 
ATOM   5952  C  C   . THR F  1 66  ? 68.102  30.763  32.254  1.00 42.39 ? 39  THR F C   1 
ATOM   5953  O  O   . THR F  1 66  ? 67.997  30.879  31.009  1.00 38.58 ? 39  THR F O   1 
ATOM   5954  C  CB  . THR F  1 66  ? 65.850  30.167  33.298  1.00 36.19 ? 39  THR F CB  1 
ATOM   5955  O  OG1 . THR F  1 66  ? 65.261  29.952  32.003  1.00 40.86 ? 39  THR F OG1 1 
ATOM   5956  C  CG2 . THR F  1 66  ? 64.751  30.643  34.264  1.00 37.43 ? 39  THR F CG2 1 
ATOM   5957  N  N   . GLU F  1 67  ? 69.200  30.282  32.845  1.00 36.85 ? 40  GLU F N   1 
ATOM   5958  C  CA  . GLU F  1 67  ? 70.350  29.729  32.110  1.00 35.23 ? 40  GLU F CA  1 
ATOM   5959  C  C   . GLU F  1 67  ? 69.881  28.771  31.008  1.00 37.85 ? 40  GLU F C   1 
ATOM   5960  O  O   . GLU F  1 67  ? 68.923  28.019  31.208  1.00 35.09 ? 40  GLU F O   1 
ATOM   5961  C  CB  . GLU F  1 67  ? 71.248  28.969  33.122  1.00 38.05 ? 40  GLU F CB  1 
ATOM   5962  C  CG  . GLU F  1 67  ? 72.411  28.203  32.510  1.00 41.16 ? 40  GLU F CG  1 
ATOM   5963  C  CD  . GLU F  1 67  ? 73.355  27.660  33.583  1.00 48.01 ? 40  GLU F CD  1 
ATOM   5964  O  OE1 . GLU F  1 67  ? 72.921  27.554  34.752  1.00 48.09 ? 40  GLU F OE1 1 
ATOM   5965  O  OE2 . GLU F  1 67  ? 74.529  27.373  33.277  1.00 45.36 ? 40  GLU F OE2 1 
ATOM   5966  N  N   . GLY F  1 68  ? 70.509  28.826  29.828  1.00 37.26 ? 41  GLY F N   1 
ATOM   5967  C  CA  . GLY F  1 68  ? 70.062  27.964  28.732  1.00 37.00 ? 41  GLY F CA  1 
ATOM   5968  C  C   . GLY F  1 68  ? 69.572  28.698  27.485  1.00 40.75 ? 41  GLY F C   1 
ATOM   5969  O  O   . GLY F  1 68  ? 69.752  29.921  27.350  1.00 37.60 ? 41  GLY F O   1 
ATOM   5970  N  N   . LEU F  1 69  ? 68.946  27.936  26.585  1.00 38.82 ? 42  LEU F N   1 
ATOM   5971  C  CA  . LEU F  1 69  ? 68.535  28.423  25.254  1.00 40.98 ? 42  LEU F CA  1 
ATOM   5972  C  C   . LEU F  1 69  ? 67.131  28.977  25.256  1.00 38.55 ? 42  LEU F C   1 
ATOM   5973  O  O   . LEU F  1 69  ? 66.241  28.379  25.865  1.00 38.40 ? 42  LEU F O   1 
ATOM   5974  C  CB  . LEU F  1 69  ? 68.585  27.283  24.217  1.00 41.36 ? 42  LEU F CB  1 
ATOM   5975  C  CG  . LEU F  1 69  ? 69.805  27.188  23.320  1.00 44.67 ? 42  LEU F CG  1 
ATOM   5976  C  CD1 . LEU F  1 69  ? 71.085  26.955  24.106  1.00 45.31 ? 42  LEU F CD1 1 
ATOM   5977  C  CD2 . LEU F  1 69  ? 69.559  26.046  22.326  1.00 50.21 ? 42  LEU F CD2 1 
ATOM   5978  N  N   . HIS F  1 70  ? 66.920  30.079  24.509  1.00 34.39 ? 43  HIS F N   1 
ATOM   5979  C  CA  . HIS F  1 70  ? 65.635  30.774  24.490  1.00 29.42 ? 43  HIS F CA  1 
ATOM   5980  C  C   . HIS F  1 70  ? 65.308  31.232  23.037  1.00 26.87 ? 43  HIS F C   1 
ATOM   5981  O  O   . HIS F  1 70  ? 66.177  31.817  22.359  1.00 26.65 ? 43  HIS F O   1 
ATOM   5982  C  CB  . HIS F  1 70  ? 65.718  31.997  25.428  1.00 33.02 ? 43  HIS F CB  1 
ATOM   5983  C  CG  . HIS F  1 70  ? 65.723  31.644  26.894  1.00 31.89 ? 43  HIS F CG  1 
ATOM   5984  N  ND1 . HIS F  1 70  ? 64.568  31.322  27.580  1.00 33.59 ? 43  HIS F ND1 1 
ATOM   5985  C  CD2 . HIS F  1 70  ? 66.738  31.547  27.789  1.00 34.64 ? 43  HIS F CD2 1 
ATOM   5986  C  CE1 . HIS F  1 70  ? 64.869  31.071  28.845  1.00 36.05 ? 43  HIS F CE1 1 
ATOM   5987  N  NE2 . HIS F  1 70  ? 66.177  31.203  28.999  1.00 32.14 ? 43  HIS F NE2 1 
ATOM   5988  N  N   . GLY F  1 71  ? 64.094  30.917  22.607  1.00 23.10 ? 44  GLY F N   1 
ATOM   5989  C  CA  . GLY F  1 71  ? 63.633  31.195  21.242  1.00 31.50 ? 44  GLY F CA  1 
ATOM   5990  C  C   . GLY F  1 71  ? 63.654  32.725  21.046  1.00 28.50 ? 44  GLY F C   1 
ATOM   5991  O  O   . GLY F  1 71  ? 63.443  33.466  22.023  1.00 25.02 ? 44  GLY F O   1 
ATOM   5992  N  N   . PHE F  1 72  ? 63.974  33.195  19.834  1.00 26.30 ? 45  PHE F N   1 
ATOM   5993  C  CA  . PHE F  1 72  ? 64.200  34.624  19.622  1.00 26.71 ? 45  PHE F CA  1 
ATOM   5994  C  C   . PHE F  1 72  ? 63.671  34.930  18.236  1.00 30.20 ? 45  PHE F C   1 
ATOM   5995  O  O   . PHE F  1 72  ? 64.338  34.581  17.257  1.00 28.01 ? 45  PHE F O   1 
ATOM   5996  C  CB  . PHE F  1 72  ? 65.705  34.828  19.698  1.00 27.68 ? 45  PHE F CB  1 
ATOM   5997  C  CG  . PHE F  1 72  ? 66.172  36.253  19.666  1.00 31.09 ? 45  PHE F CG  1 
ATOM   5998  C  CD1 . PHE F  1 72  ? 65.753  37.176  20.629  1.00 32.03 ? 45  PHE F CD1 1 
ATOM   5999  C  CD2 . PHE F  1 72  ? 67.097  36.661  18.708  1.00 34.05 ? 45  PHE F CD2 1 
ATOM   6000  C  CE1 . PHE F  1 72  ? 66.248  38.463  20.627  1.00 33.34 ? 45  PHE F CE1 1 
ATOM   6001  C  CE2 . PHE F  1 72  ? 67.593  37.980  18.694  1.00 33.06 ? 45  PHE F CE2 1 
ATOM   6002  C  CZ  . PHE F  1 72  ? 67.172  38.876  19.664  1.00 33.70 ? 45  PHE F CZ  1 
ATOM   6003  N  N   . HIS F  1 73  ? 62.497  35.589  18.164  1.00 27.12 ? 46  HIS F N   1 
ATOM   6004  C  CA  . HIS F  1 73  ? 61.724  35.745  16.922  1.00 28.06 ? 46  HIS F CA  1 
ATOM   6005  C  C   . HIS F  1 73  ? 61.255  37.172  16.696  1.00 29.62 ? 46  HIS F C   1 
ATOM   6006  O  O   . HIS F  1 73  ? 60.938  37.891  17.680  1.00 25.71 ? 46  HIS F O   1 
ATOM   6007  C  CB  . HIS F  1 73  ? 60.494  34.835  16.950  1.00 29.41 ? 46  HIS F CB  1 
ATOM   6008  C  CG  . HIS F  1 73  ? 60.844  33.410  17.216  1.00 36.84 ? 46  HIS F CG  1 
ATOM   6009  N  ND1 . HIS F  1 73  ? 60.403  32.726  18.328  1.00 40.84 ? 46  HIS F ND1 1 
ATOM   6010  C  CD2 . HIS F  1 73  ? 61.660  32.562  16.548  1.00 37.49 ? 46  HIS F CD2 1 
ATOM   6011  C  CE1 . HIS F  1 73  ? 60.909  31.504  18.319  1.00 38.54 ? 46  HIS F CE1 1 
ATOM   6012  N  NE2 . HIS F  1 73  ? 61.696  31.387  17.264  1.00 37.43 ? 46  HIS F NE2 1 
ATOM   6013  N  N   . VAL F  1 74  ? 61.234  37.575  15.425  1.00 26.01 ? 47  VAL F N   1 
ATOM   6014  C  CA  . VAL F  1 74  ? 60.435  38.767  15.027  1.00 24.49 ? 47  VAL F CA  1 
ATOM   6015  C  C   . VAL F  1 74  ? 59.015  38.315  14.745  1.00 23.97 ? 47  VAL F C   1 
ATOM   6016  O  O   . VAL F  1 74  ? 58.781  37.371  13.972  1.00 26.43 ? 47  VAL F O   1 
ATOM   6017  C  CB  . VAL F  1 74  ? 60.999  39.433  13.767  1.00 22.66 ? 47  VAL F CB  1 
ATOM   6018  C  CG1 . VAL F  1 74  ? 60.181  40.714  13.453  1.00 21.83 ? 47  VAL F CG1 1 
ATOM   6019  C  CG2 . VAL F  1 74  ? 62.441  39.789  13.993  1.00 22.59 ? 47  VAL F CG2 1 
ATOM   6020  N  N   . HIS F  1 75  ? 58.054  38.894  15.457  1.00 20.74 ? 48  HIS F N   1 
ATOM   6021  C  CA  . HIS F  1 75  ? 56.648  38.608  15.282  1.00 20.93 ? 48  HIS F CA  1 
ATOM   6022  C  C   . HIS F  1 75  ? 55.985  39.702  14.424  1.00 22.58 ? 48  HIS F C   1 
ATOM   6023  O  O   . HIS F  1 75  ? 56.568  40.768  14.246  1.00 22.92 ? 48  HIS F O   1 
ATOM   6024  C  CB  . HIS F  1 75  ? 55.965  38.521  16.623  1.00 23.66 ? 48  HIS F CB  1 
ATOM   6025  C  CG  . HIS F  1 75  ? 56.341  37.287  17.417  1.00 22.59 ? 48  HIS F CG  1 
ATOM   6026  N  ND1 . HIS F  1 75  ? 55.430  36.317  17.727  1.00 25.32 ? 48  HIS F ND1 1 
ATOM   6027  C  CD2 . HIS F  1 75  ? 57.521  36.880  17.935  1.00 25.36 ? 48  HIS F CD2 1 
ATOM   6028  C  CE1 . HIS F  1 75  ? 56.013  35.375  18.457  1.00 23.81 ? 48  HIS F CE1 1 
ATOM   6029  N  NE2 . HIS F  1 75  ? 57.289  35.690  18.591  1.00 29.13 ? 48  HIS F NE2 1 
ATOM   6030  N  N   . GLU F  1 76  ? 54.783  39.435  13.924  1.00 23.52 ? 49  GLU F N   1 
ATOM   6031  C  CA  . GLU F  1 76  ? 54.231  40.174  12.808  1.00 27.36 ? 49  GLU F CA  1 
ATOM   6032  C  C   . GLU F  1 76  ? 53.861  41.636  13.139  1.00 28.09 ? 49  GLU F C   1 
ATOM   6033  O  O   . GLU F  1 76  ? 54.166  42.536  12.347  1.00 27.28 ? 49  GLU F O   1 
ATOM   6034  C  CB  . GLU F  1 76  ? 52.995  39.480  12.274  1.00 27.43 ? 49  GLU F CB  1 
ATOM   6035  C  CG  . GLU F  1 76  ? 52.499  40.087  10.979  1.00 32.39 ? 49  GLU F CG  1 
ATOM   6036  C  CD  . GLU F  1 76  ? 51.315  39.360  10.391  1.00 37.41 ? 49  GLU F CD  1 
ATOM   6037  O  OE1 . GLU F  1 76  ? 50.936  38.300  10.934  1.00 36.85 ? 49  GLU F OE1 1 
ATOM   6038  O  OE2 . GLU F  1 76  ? 50.767  39.858  9.380   1.00 39.78 ? 49  GLU F OE2 1 
ATOM   6039  N  N   . PHE F  1 77  ? 53.180  41.849  14.273  1.00 26.97 ? 50  PHE F N   1 
ATOM   6040  C  CA  . PHE F  1 77  ? 52.621  43.189  14.604  1.00 24.70 ? 50  PHE F CA  1 
ATOM   6041  C  C   . PHE F  1 77  ? 53.395  43.884  15.685  1.00 26.97 ? 50  PHE F C   1 
ATOM   6042  O  O   . PHE F  1 77  ? 53.789  43.242  16.681  1.00 25.00 ? 50  PHE F O   1 
ATOM   6043  C  CB  . PHE F  1 77  ? 51.170  43.058  15.030  1.00 25.50 ? 50  PHE F CB  1 
ATOM   6044  C  CG  . PHE F  1 77  ? 50.342  42.309  14.050  1.00 29.54 ? 50  PHE F CG  1 
ATOM   6045  C  CD1 . PHE F  1 77  ? 50.203  42.776  12.758  1.00 32.10 ? 50  PHE F CD1 1 
ATOM   6046  C  CD2 . PHE F  1 77  ? 49.716  41.126  14.418  1.00 32.28 ? 50  PHE F CD2 1 
ATOM   6047  C  CE1 . PHE F  1 77  ? 49.466  42.070  11.821  1.00 35.99 ? 50  PHE F CE1 1 
ATOM   6048  C  CE2 . PHE F  1 77  ? 48.968  40.408  13.479  1.00 35.81 ? 50  PHE F CE2 1 
ATOM   6049  C  CZ  . PHE F  1 77  ? 48.842  40.898  12.183  1.00 34.03 ? 50  PHE F CZ  1 
ATOM   6050  N  N   . GLY F  1 78  ? 53.574  45.210  15.523  1.00 23.42 ? 51  GLY F N   1 
ATOM   6051  C  CA  . GLY F  1 78  ? 54.237  46.026  16.537  1.00 22.97 ? 51  GLY F CA  1 
ATOM   6052  C  C   . GLY F  1 78  ? 53.120  46.533  17.458  1.00 25.07 ? 51  GLY F C   1 
ATOM   6053  O  O   . GLY F  1 78  ? 53.016  47.728  17.718  1.00 24.71 ? 51  GLY F O   1 
ATOM   6054  N  N   . ASP F  1 79  ? 52.268  45.620  17.922  1.00 24.54 ? 52  ASP F N   1 
ATOM   6055  C  CA  . ASP F  1 79  ? 51.094  45.956  18.739  1.00 22.91 ? 52  ASP F CA  1 
ATOM   6056  C  C   . ASP F  1 79  ? 51.339  45.339  20.122  1.00 26.14 ? 52  ASP F C   1 
ATOM   6057  O  O   . ASP F  1 79  ? 51.428  44.097  20.273  1.00 26.35 ? 52  ASP F O   1 
ATOM   6058  C  CB  . ASP F  1 79  ? 49.858  45.406  18.051  1.00 24.72 ? 52  ASP F CB  1 
ATOM   6059  C  CG  . ASP F  1 79  ? 48.561  45.690  18.811  1.00 26.12 ? 52  ASP F CG  1 
ATOM   6060  O  OD1 . ASP F  1 79  ? 48.567  45.984  20.028  1.00 27.03 ? 52  ASP F OD1 1 
ATOM   6061  O  OD2 . ASP F  1 79  ? 47.528  45.566  18.169  1.00 25.87 ? 52  ASP F OD2 1 
ATOM   6062  N  N   . ASN F  1 80  ? 51.542  46.203  21.116  1.00 24.00 ? 53  ASN F N   1 
ATOM   6063  C  CA  . ASN F  1 80  ? 51.793  45.774  22.477  1.00 24.91 ? 53  ASN F CA  1 
ATOM   6064  C  C   . ASN F  1 80  ? 50.585  46.124  23.378  1.00 25.67 ? 53  ASN F C   1 
ATOM   6065  O  O   . ASN F  1 80  ? 50.721  46.178  24.593  1.00 27.98 ? 53  ASN F O   1 
ATOM   6066  C  CB  . ASN F  1 80  ? 53.050  46.451  23.014  1.00 33.81 ? 53  ASN F CB  1 
ATOM   6067  C  CG  . ASN F  1 80  ? 53.459  45.947  24.401  1.00 46.09 ? 53  ASN F CG  1 
ATOM   6068  O  OD1 . ASN F  1 80  ? 53.492  44.724  24.665  1.00 47.92 ? 53  ASN F OD1 1 
ATOM   6069  N  ND2 . ASN F  1 80  ? 53.803  46.882  25.289  1.00 43.98 ? 53  ASN F ND2 1 
ATOM   6070  N  N   . THR F  1 81  ? 49.432  46.345  22.783  1.00 24.80 ? 54  THR F N   1 
ATOM   6071  C  CA  . THR F  1 81  ? 48.268  46.749  23.573  1.00 28.25 ? 54  THR F CA  1 
ATOM   6072  C  C   . THR F  1 81  ? 47.807  45.673  24.569  1.00 35.20 ? 54  THR F C   1 
ATOM   6073  O  O   . THR F  1 81  ? 47.269  46.033  25.585  1.00 35.30 ? 54  THR F O   1 
ATOM   6074  C  CB  . THR F  1 81  ? 47.081  47.172  22.737  1.00 27.42 ? 54  THR F CB  1 
ATOM   6075  O  OG1 . THR F  1 81  ? 46.724  46.118  21.829  1.00 29.34 ? 54  THR F OG1 1 
ATOM   6076  C  CG2 . THR F  1 81  ? 47.426  48.434  21.898  1.00 25.82 ? 54  THR F CG2 1 
ATOM   6077  N  N   . ALA F  1 82  ? 47.990  44.382  24.270  1.00 32.08 ? 55  ALA F N   1 
ATOM   6078  C  CA  . ALA F  1 82  ? 47.752  43.313  25.293  1.00 35.23 ? 55  ALA F CA  1 
ATOM   6079  C  C   . ALA F  1 82  ? 49.050  42.622  25.652  1.00 33.97 ? 55  ALA F C   1 
ATOM   6080  O  O   . ALA F  1 82  ? 49.118  41.395  25.712  1.00 42.72 ? 55  ALA F O   1 
ATOM   6081  C  CB  . ALA F  1 82  ? 46.739  42.304  24.783  1.00 34.88 ? 55  ALA F CB  1 
ATOM   6082  N  N   . GLY F  1 83  ? 50.104  43.410  25.832  1.00 33.12 ? 56  GLY F N   1 
ATOM   6083  C  CA  . GLY F  1 83  ? 51.430  42.887  26.096  1.00 31.24 ? 56  GLY F CA  1 
ATOM   6084  C  C   . GLY F  1 83  ? 51.896  42.100  24.877  1.00 33.62 ? 56  GLY F C   1 
ATOM   6085  O  O   . GLY F  1 83  ? 51.439  42.344  23.737  1.00 31.53 ? 56  GLY F O   1 
ATOM   6086  N  N   . CYS F  1 84  ? 52.762  41.121  25.124  1.00 31.83 ? 57  CYS F N   1 
ATOM   6087  C  CA  . CYS F  1 84  ? 53.410  40.362  24.056  1.00 33.70 ? 57  CYS F CA  1 
ATOM   6088  C  C   . CYS F  1 84  ? 52.458  39.539  23.187  1.00 31.58 ? 57  CYS F C   1 
ATOM   6089  O  O   . CYS F  1 84  ? 52.765  39.262  22.022  1.00 33.30 ? 57  CYS F O   1 
ATOM   6090  C  CB  . CYS F  1 84  ? 54.557  39.520  24.596  1.00 32.52 ? 57  CYS F CB  1 
ATOM   6091  S  SG  . CYS F  1 84  ? 55.888  40.501  25.365  1.00 40.37 ? 57  CYS F SG  1 
ATOM   6092  N  N   . THR F  1 85  ? 51.282  39.212  23.697  1.00 29.40 ? 58  THR F N   1 
ATOM   6093  C  CA  . THR F  1 85  ? 50.298  38.441  22.934  1.00 30.72 ? 58  THR F CA  1 
ATOM   6094  C  C   . THR F  1 85  ? 49.851  39.151  21.676  1.00 34.36 ? 58  THR F C   1 
ATOM   6095  O  O   . THR F  1 85  ? 49.621  38.512  20.634  1.00 31.11 ? 58  THR F O   1 
ATOM   6096  C  CB  . THR F  1 85  ? 49.028  38.213  23.778  1.00 37.50 ? 58  THR F CB  1 
ATOM   6097  O  OG1 . THR F  1 85  ? 49.444  37.717  25.049  1.00 41.69 ? 58  THR F OG1 1 
ATOM   6098  C  CG2 . THR F  1 85  ? 48.061  37.203  23.123  1.00 38.62 ? 58  THR F CG2 1 
ATOM   6099  N  N   . SER F  1 86  ? 49.709  40.480  21.750  1.00 29.13 ? 59  SER F N   1 
ATOM   6100  C  CA  . SER F  1 86  ? 49.124  41.171  20.620  1.00 28.29 ? 59  SER F CA  1 
ATOM   6101  C  C   . SER F  1 86  ? 50.098  41.301  19.423  1.00 25.72 ? 59  SER F C   1 
ATOM   6102  O  O   . SER F  1 86  ? 49.695  41.778  18.366  1.00 26.13 ? 59  SER F O   1 
ATOM   6103  C  CB  . SER F  1 86  ? 48.474  42.502  21.083  1.00 30.84 ? 59  SER F CB  1 
ATOM   6104  O  OG  . SER F  1 86  ? 49.336  43.136  22.001  1.00 34.82 ? 59  SER F OG  1 
ATOM   6105  N  N   . ALA F  1 87  ? 51.354  40.883  19.601  1.00 26.85 ? 60  ALA F N   1 
ATOM   6106  C  CA  . ALA F  1 87  ? 52.343  40.793  18.506  1.00 26.77 ? 60  ALA F CA  1 
ATOM   6107  C  C   . ALA F  1 87  ? 51.988  39.757  17.435  1.00 29.20 ? 60  ALA F C   1 
ATOM   6108  O  O   . ALA F  1 87  ? 52.504  39.845  16.320  1.00 27.19 ? 60  ALA F O   1 
ATOM   6109  C  CB  . ALA F  1 87  ? 53.762  40.614  19.026  1.00 25.53 ? 60  ALA F CB  1 
ATOM   6110  N  N   . GLY F  1 88  ? 51.048  38.854  17.742  1.00 29.48 ? 61  GLY F N   1 
ATOM   6111  C  CA  . GLY F  1 88  ? 50.583  37.864  16.775  1.00 29.73 ? 61  GLY F CA  1 
ATOM   6112  C  C   . GLY F  1 88  ? 51.663  36.823  16.506  1.00 28.99 ? 61  GLY F C   1 
ATOM   6113  O  O   . GLY F  1 88  ? 52.576  36.644  17.341  1.00 26.71 ? 61  GLY F O   1 
ATOM   6114  N  N   . PRO F  1 89  ? 51.596  36.158  15.320  1.00 30.24 ? 62  PRO F N   1 
ATOM   6115  C  CA  . PRO F  1 89  ? 52.473  35.032  15.016  1.00 31.11 ? 62  PRO F CA  1 
ATOM   6116  C  C   . PRO F  1 89  ? 53.875  35.461  14.526  1.00 30.71 ? 62  PRO F C   1 
ATOM   6117  O  O   . PRO F  1 89  ? 54.157  36.685  14.431  1.00 30.43 ? 62  PRO F O   1 
ATOM   6118  C  CB  . PRO F  1 89  ? 51.678  34.282  13.909  1.00 30.73 ? 62  PRO F CB  1 
ATOM   6119  C  CG  . PRO F  1 89  ? 51.049  35.411  13.154  1.00 32.99 ? 62  PRO F CG  1 
ATOM   6120  C  CD  . PRO F  1 89  ? 50.636  36.417  14.226  1.00 31.98 ? 62  PRO F CD  1 
ATOM   6121  N  N   . HIS F  1 90  ? 54.755  34.486  14.203  1.00 30.02 ? 63  HIS F N   1 
ATOM   6122  C  CA  . HIS F  1 90  ? 56.129  34.820  13.699  1.00 29.39 ? 63  HIS F CA  1 
ATOM   6123  C  C   . HIS F  1 90  ? 55.913  35.593  12.387  1.00 28.58 ? 63  HIS F C   1 
ATOM   6124  O  O   . HIS F  1 90  ? 54.893  35.367  11.704  1.00 27.68 ? 63  HIS F O   1 
ATOM   6125  C  CB  . HIS F  1 90  ? 57.043  33.567  13.500  1.00 30.85 ? 63  HIS F CB  1 
ATOM   6126  C  CG  . HIS F  1 90  ? 57.393  32.862  14.781  1.00 33.66 ? 63  HIS F CG  1 
ATOM   6127  N  ND1 . HIS F  1 90  ? 58.180  31.734  14.831  1.00 34.05 ? 63  HIS F ND1 1 
ATOM   6128  C  CD2 . HIS F  1 90  ? 57.030  33.108  16.067  1.00 37.90 ? 63  HIS F CD2 1 
ATOM   6129  C  CE1 . HIS F  1 90  ? 58.321  31.335  16.083  1.00 36.17 ? 63  HIS F CE1 1 
ATOM   6130  N  NE2 . HIS F  1 90  ? 57.638  32.158  16.857  1.00 35.16 ? 63  HIS F NE2 1 
ATOM   6131  N  N   . PHE F  1 91  ? 56.808  36.547  12.092  1.00 28.42 ? 64  PHE F N   1 
ATOM   6132  C  CA  . PHE F  1 91  ? 56.663  37.386  10.887  1.00 27.96 ? 64  PHE F CA  1 
ATOM   6133  C  C   . PHE F  1 91  ? 56.881  36.446  9.672   1.00 27.58 ? 64  PHE F C   1 
ATOM   6134  O  O   . PHE F  1 91  ? 57.910  35.811  9.586   1.00 24.82 ? 64  PHE F O   1 
ATOM   6135  C  CB  . PHE F  1 91  ? 57.683  38.524  10.893  1.00 25.49 ? 64  PHE F CB  1 
ATOM   6136  C  CG  . PHE F  1 91  ? 57.665  39.381  9.623   1.00 24.93 ? 64  PHE F CG  1 
ATOM   6137  C  CD1 . PHE F  1 91  ? 56.470  39.736  9.012   1.00 26.37 ? 64  PHE F CD1 1 
ATOM   6138  C  CD2 . PHE F  1 91  ? 58.859  39.866  9.092   1.00 25.54 ? 64  PHE F CD2 1 
ATOM   6139  C  CE1 . PHE F  1 91  ? 56.477  40.508  7.846   1.00 25.94 ? 64  PHE F CE1 1 
ATOM   6140  C  CE2 . PHE F  1 91  ? 58.874  40.675  7.935   1.00 27.77 ? 64  PHE F CE2 1 
ATOM   6141  C  CZ  . PHE F  1 91  ? 57.677  40.971  7.317   1.00 24.15 ? 64  PHE F CZ  1 
ATOM   6142  N  N   . ASN F  1 92  ? 55.884  36.341  8.801   1.00 28.08 ? 65  ASN F N   1 
ATOM   6143  C  CA  . ASN F  1 92  ? 55.943  35.304  7.754   1.00 35.11 ? 65  ASN F CA  1 
ATOM   6144  C  C   . ASN F  1 92  ? 55.356  35.811  6.426   1.00 34.52 ? 65  ASN F C   1 
ATOM   6145  O  O   . ASN F  1 92  ? 54.318  35.309  5.993   1.00 38.26 ? 65  ASN F O   1 
ATOM   6146  C  CB  . ASN F  1 92  ? 55.172  34.065  8.248   1.00 33.52 ? 65  ASN F CB  1 
ATOM   6147  C  CG  . ASN F  1 92  ? 55.456  32.806  7.413   1.00 41.48 ? 65  ASN F CG  1 
ATOM   6148  O  OD1 . ASN F  1 92  ? 56.517  32.655  6.769   1.00 36.66 ? 65  ASN F OD1 1 
ATOM   6149  N  ND2 . ASN F  1 92  ? 54.504  31.891  7.437   1.00 38.73 ? 65  ASN F ND2 1 
ATOM   6150  N  N   . PRO F  1 93  ? 55.993  36.825  5.796   1.00 32.51 ? 66  PRO F N   1 
ATOM   6151  C  CA  . PRO F  1 93  ? 55.325  37.365  4.624   1.00 33.75 ? 66  PRO F CA  1 
ATOM   6152  C  C   . PRO F  1 93  ? 55.298  36.353  3.440   1.00 39.94 ? 66  PRO F C   1 
ATOM   6153  O  O   . PRO F  1 93  ? 54.434  36.462  2.575   1.00 43.11 ? 66  PRO F O   1 
ATOM   6154  C  CB  . PRO F  1 93  ? 56.147  38.596  4.287   1.00 31.93 ? 66  PRO F CB  1 
ATOM   6155  C  CG  . PRO F  1 93  ? 57.529  38.309  4.815   1.00 34.25 ? 66  PRO F CG  1 
ATOM   6156  C  CD  . PRO F  1 93  ? 57.335  37.414  6.011   1.00 31.70 ? 66  PRO F CD  1 
ATOM   6157  N  N   . LEU F  1 94  ? 56.212  35.382  3.429   1.00 43.93 ? 67  LEU F N   1 
ATOM   6158  C  CA  . LEU F  1 94  ? 56.253  34.321  2.367   1.00 45.92 ? 67  LEU F CA  1 
ATOM   6159  C  C   . LEU F  1 94  ? 55.439  33.037  2.645   1.00 50.23 ? 67  LEU F C   1 
ATOM   6160  O  O   . LEU F  1 94  ? 55.562  32.059  1.899   1.00 49.91 ? 67  LEU F O   1 
ATOM   6161  C  CB  . LEU F  1 94  ? 57.700  33.976  2.031   1.00 46.40 ? 67  LEU F CB  1 
ATOM   6162  C  CG  . LEU F  1 94  ? 58.547  35.169  1.555   1.00 50.82 ? 67  LEU F CG  1 
ATOM   6163  C  CD1 . LEU F  1 94  ? 59.960  34.751  1.149   1.00 49.68 ? 67  LEU F CD1 1 
ATOM   6164  C  CD2 . LEU F  1 94  ? 57.852  35.924  0.421   1.00 49.96 ? 67  LEU F CD2 1 
ATOM   6165  N  N   . SER F  1 95  ? 54.625  33.040  3.713   1.00 46.42 ? 68  SER F N   1 
ATOM   6166  C  CA  . SER F  1 95  ? 53.799  31.892  4.154   1.00 45.96 ? 68  SER F CA  1 
ATOM   6167  C  C   . SER F  1 95  ? 54.519  30.531  4.092   1.00 47.76 ? 68  SER F C   1 
ATOM   6168  O  O   . SER F  1 95  ? 53.998  29.564  3.519   1.00 49.41 ? 68  SER F O   1 
ATOM   6169  C  CB  . SER F  1 95  ? 52.471  31.817  3.379   1.00 46.21 ? 68  SER F CB  1 
ATOM   6170  O  OG  . SER F  1 95  ? 52.200  33.046  2.763   1.00 45.92 ? 68  SER F OG  1 
ATOM   6171  N  N   . ARG F  1 96  ? 55.718  30.484  4.672   1.00 46.63 ? 69  ARG F N   1 
ATOM   6172  C  CA  . ARG F  1 96  ? 56.492  29.264  4.832   1.00 46.04 ? 69  ARG F CA  1 
ATOM   6173  C  C   . ARG F  1 96  ? 56.274  28.631  6.232   1.00 48.98 ? 69  ARG F C   1 
ATOM   6174  O  O   . ARG F  1 96  ? 55.629  29.229  7.111   1.00 41.68 ? 69  ARG F O   1 
ATOM   6175  C  CB  . ARG F  1 96  ? 57.969  29.576  4.546   1.00 45.88 ? 69  ARG F CB  1 
ATOM   6176  C  CG  . ARG F  1 96  ? 58.158  29.980  3.089   1.00 47.26 ? 69  ARG F CG  1 
ATOM   6177  C  CD  . ARG F  1 96  ? 59.620  30.015  2.677   1.00 55.53 ? 69  ARG F CD  1 
ATOM   6178  N  NE  . ARG F  1 96  ? 59.774  30.515  1.296   1.00 62.88 ? 69  ARG F NE  1 
ATOM   6179  C  CZ  . ARG F  1 96  ? 60.933  30.874  0.726   1.00 65.23 ? 69  ARG F CZ  1 
ATOM   6180  N  NH1 . ARG F  1 96  ? 62.077  30.782  1.396   1.00 63.54 ? 69  ARG F NH1 1 
ATOM   6181  N  NH2 . ARG F  1 96  ? 60.953  31.322  -0.529  1.00 59.42 ? 69  ARG F NH2 1 
ATOM   6182  N  N   . LYS F  1 97  ? 56.776  27.415  6.425   1.00 44.25 ? 70  LYS F N   1 
ATOM   6183  C  CA  . LYS F  1 97  ? 56.765  26.778  7.740   1.00 45.31 ? 70  LYS F CA  1 
ATOM   6184  C  C   . LYS F  1 97  ? 57.927  27.342  8.583   1.00 40.55 ? 70  LYS F C   1 
ATOM   6185  O  O   . LYS F  1 97  ? 58.885  27.895  8.038   1.00 40.55 ? 70  LYS F O   1 
ATOM   6186  C  CB  . LYS F  1 97  ? 56.856  25.236  7.594   1.00 46.71 ? 70  LYS F CB  1 
ATOM   6187  N  N   . HIS F  1 98  ? 57.821  27.192  9.911   1.00 42.46 ? 71  HIS F N   1 
ATOM   6188  C  CA  . HIS F  1 98  ? 58.826  27.641  10.874  1.00 44.01 ? 71  HIS F CA  1 
ATOM   6189  C  C   . HIS F  1 98  ? 60.109  26.815  10.748  1.00 44.46 ? 71  HIS F C   1 
ATOM   6190  O  O   . HIS F  1 98  ? 60.020  25.606  10.564  1.00 48.65 ? 71  HIS F O   1 
ATOM   6191  C  CB  . HIS F  1 98  ? 58.241  27.517  12.300  1.00 44.21 ? 71  HIS F CB  1 
ATOM   6192  C  CG  . HIS F  1 98  ? 59.251  27.714  13.390  1.00 43.42 ? 71  HIS F CG  1 
ATOM   6193  N  ND1 . HIS F  1 98  ? 59.704  28.954  13.773  1.00 39.17 ? 71  HIS F ND1 1 
ATOM   6194  C  CD2 . HIS F  1 98  ? 59.920  26.822  14.159  1.00 43.09 ? 71  HIS F CD2 1 
ATOM   6195  C  CE1 . HIS F  1 98  ? 60.613  28.826  14.724  1.00 43.45 ? 71  HIS F CE1 1 
ATOM   6196  N  NE2 . HIS F  1 98  ? 60.756  27.540  14.983  1.00 45.45 ? 71  HIS F NE2 1 
ATOM   6197  N  N   . GLY F  1 99  ? 61.275  27.457  10.848  1.00 41.33 ? 72  GLY F N   1 
ATOM   6198  C  CA  . GLY F  1 99  ? 62.566  26.772  10.820  1.00 45.58 ? 72  GLY F CA  1 
ATOM   6199  C  C   . GLY F  1 99  ? 63.636  27.496  11.615  1.00 45.77 ? 72  GLY F C   1 
ATOM   6200  O  O   . GLY F  1 99  ? 63.355  28.473  12.332  1.00 44.96 ? 72  GLY F O   1 
ATOM   6201  N  N   . GLY F  1 100 ? 64.870  27.027  11.489  1.00 42.58 ? 73  GLY F N   1 
ATOM   6202  C  CA  . GLY F  1 100 ? 66.004  27.664  12.140  1.00 39.93 ? 73  GLY F CA  1 
ATOM   6203  C  C   . GLY F  1 100 ? 66.500  28.743  11.202  1.00 41.24 ? 73  GLY F C   1 
ATOM   6204  O  O   . GLY F  1 100 ? 66.124  28.742  10.020  1.00 38.08 ? 73  GLY F O   1 
ATOM   6205  N  N   . PRO F  1 101 ? 67.339  29.671  11.716  1.00 40.71 ? 74  PRO F N   1 
ATOM   6206  C  CA  . PRO F  1 101 ? 67.860  30.768  10.902  1.00 39.00 ? 74  PRO F CA  1 
ATOM   6207  C  C   . PRO F  1 101 ? 68.598  30.284  9.653   1.00 45.17 ? 74  PRO F C   1 
ATOM   6208  O  O   . PRO F  1 101 ? 68.468  30.919  8.595   1.00 35.97 ? 74  PRO F O   1 
ATOM   6209  C  CB  . PRO F  1 101 ? 68.806  31.534  11.843  1.00 40.62 ? 74  PRO F CB  1 
ATOM   6210  C  CG  . PRO F  1 101 ? 68.806  30.808  13.147  1.00 44.29 ? 74  PRO F CG  1 
ATOM   6211  C  CD  . PRO F  1 101 ? 67.648  29.840  13.144  1.00 40.59 ? 74  PRO F CD  1 
ATOM   6212  N  N   . LYS F  1 102 ? 69.327  29.164  9.755   1.00 44.03 ? 75  LYS F N   1 
ATOM   6213  C  CA  . LYS F  1 102 ? 70.095  28.631  8.597   1.00 46.50 ? 75  LYS F CA  1 
ATOM   6214  C  C   . LYS F  1 102 ? 69.302  27.737  7.630   1.00 43.48 ? 75  LYS F C   1 
ATOM   6215  O  O   . LYS F  1 102 ? 69.858  27.262  6.638   1.00 46.59 ? 75  LYS F O   1 
ATOM   6216  C  CB  . LYS F  1 102 ? 71.346  27.896  9.074   1.00 46.73 ? 75  LYS F CB  1 
ATOM   6217  C  CG  . LYS F  1 102 ? 72.347  28.771  9.798   1.00 51.26 ? 75  LYS F CG  1 
ATOM   6218  C  CD  . LYS F  1 102 ? 73.676  28.839  9.055   1.00 55.59 ? 75  LYS F CD  1 
ATOM   6219  C  CE  . LYS F  1 102 ? 74.832  28.826  10.051  1.00 61.12 ? 75  LYS F CE  1 
ATOM   6220  N  NZ  . LYS F  1 102 ? 76.031  29.537  9.523   1.00 60.59 ? 75  LYS F NZ  1 
ATOM   6221  N  N   . ASP F  1 103 ? 68.024  27.495  7.897   1.00 43.10 ? 76  ASP F N   1 
ATOM   6222  C  CA  . ASP F  1 103 ? 67.175  26.735  6.970   1.00 45.31 ? 76  ASP F CA  1 
ATOM   6223  C  C   . ASP F  1 103 ? 66.632  27.607  5.841   1.00 52.38 ? 76  ASP F C   1 
ATOM   6224  O  O   . ASP F  1 103 ? 66.368  28.810  6.048   1.00 48.95 ? 76  ASP F O   1 
ATOM   6225  C  CB  . ASP F  1 103 ? 66.010  26.094  7.714   1.00 43.53 ? 76  ASP F CB  1 
ATOM   6226  C  CG  . ASP F  1 103 ? 66.481  25.139  8.841   1.00 52.53 ? 76  ASP F CG  1 
ATOM   6227  O  OD1 . ASP F  1 103 ? 67.619  24.607  8.744   1.00 53.20 ? 76  ASP F OD1 1 
ATOM   6228  O  OD2 . ASP F  1 103 ? 65.733  24.932  9.830   1.00 47.50 ? 76  ASP F OD2 1 
ATOM   6229  N  N   . GLU F  1 104 ? 66.457  26.995  4.662   1.00 52.01 ? 77  GLU F N   1 
ATOM   6230  C  CA  . GLU F  1 104 ? 65.777  27.627  3.508   1.00 50.19 ? 77  GLU F CA  1 
ATOM   6231  C  C   . GLU F  1 104 ? 64.274  27.767  3.794   1.00 50.56 ? 77  GLU F C   1 
ATOM   6232  O  O   . GLU F  1 104 ? 63.655  28.790  3.471   1.00 50.50 ? 77  GLU F O   1 
ATOM   6233  C  CB  . GLU F  1 104 ? 66.029  26.836  2.196   1.00 50.98 ? 77  GLU F CB  1 
ATOM   6234  N  N   . GLU F  1 105 ? 63.689  26.753  4.427   1.00 46.98 ? 78  GLU F N   1 
ATOM   6235  C  CA  . GLU F  1 105 ? 62.298  26.823  4.829   1.00 46.55 ? 78  GLU F CA  1 
ATOM   6236  C  C   . GLU F  1 105 ? 62.230  27.420  6.245   1.00 42.64 ? 78  GLU F C   1 
ATOM   6237  O  O   . GLU F  1 105 ? 62.502  26.731  7.224   1.00 43.14 ? 78  GLU F O   1 
ATOM   6238  C  CB  . GLU F  1 105 ? 61.676  25.426  4.821   1.00 44.34 ? 78  GLU F CB  1 
ATOM   6239  C  CG  . GLU F  1 105 ? 60.196  25.387  5.170   1.00 48.25 ? 78  GLU F CG  1 
ATOM   6240  C  CD  . GLU F  1 105 ? 59.301  26.006  4.099   1.00 54.93 ? 78  GLU F CD  1 
ATOM   6241  O  OE1 . GLU F  1 105 ? 59.814  26.394  3.026   1.00 63.10 ? 78  GLU F OE1 1 
ATOM   6242  O  OE2 . GLU F  1 105 ? 58.068  26.091  4.307   1.00 49.58 ? 78  GLU F OE2 1 
ATOM   6243  N  N   . ARG F  1 106 ? 61.878  28.698  6.358   1.00 39.73 ? 79  ARG F N   1 
ATOM   6244  C  CA  . ARG F  1 106 ? 61.822  29.352  7.685   1.00 38.60 ? 79  ARG F CA  1 
ATOM   6245  C  C   . ARG F  1 106 ? 60.907  30.553  7.539   1.00 42.14 ? 79  ARG F C   1 
ATOM   6246  O  O   . ARG F  1 106 ? 60.606  30.961  6.410   1.00 40.96 ? 79  ARG F O   1 
ATOM   6247  C  CB  . ARG F  1 106 ? 63.212  29.810  8.176   1.00 38.16 ? 79  ARG F CB  1 
ATOM   6248  C  CG  . ARG F  1 106 ? 63.918  30.779  7.227   1.00 37.87 ? 79  ARG F CG  1 
ATOM   6249  C  CD  . ARG F  1 106 ? 65.129  31.452  7.849   1.00 39.38 ? 79  ARG F CD  1 
ATOM   6250  N  NE  . ARG F  1 106 ? 64.835  32.762  8.463   1.00 31.37 ? 79  ARG F NE  1 
ATOM   6251  C  CZ  . ARG F  1 106 ? 65.775  33.604  8.861   1.00 31.62 ? 79  ARG F CZ  1 
ATOM   6252  N  NH1 . ARG F  1 106 ? 67.052  33.292  8.691   1.00 31.83 ? 79  ARG F NH1 1 
ATOM   6253  N  NH2 . ARG F  1 106 ? 65.470  34.788  9.406   1.00 28.61 ? 79  ARG F NH2 1 
ATOM   6254  N  N   . HIS F  1 107 ? 60.417  31.072  8.668   1.00 35.12 ? 80  HIS F N   1 
ATOM   6255  C  CA  . HIS F  1 107 ? 59.739  32.381  8.675   1.00 33.43 ? 80  HIS F CA  1 
ATOM   6256  C  C   . HIS F  1 107 ? 60.842  33.440  8.530   1.00 27.95 ? 80  HIS F C   1 
ATOM   6257  O  O   . HIS F  1 107 ? 62.006  33.204  8.909   1.00 31.23 ? 80  HIS F O   1 
ATOM   6258  C  CB  . HIS F  1 107 ? 58.974  32.571  9.992   1.00 31.68 ? 80  HIS F CB  1 
ATOM   6259  C  CG  . HIS F  1 107 ? 57.897  31.537  10.268  1.00 37.79 ? 80  HIS F CG  1 
ATOM   6260  N  ND1 . HIS F  1 107 ? 57.685  30.971  11.526  1.00 32.87 ? 80  HIS F ND1 1 
ATOM   6261  C  CD2 . HIS F  1 107 ? 56.927  31.024  9.470   1.00 37.97 ? 80  HIS F CD2 1 
ATOM   6262  C  CE1 . HIS F  1 107 ? 56.622  30.188  11.486  1.00 36.31 ? 80  HIS F CE1 1 
ATOM   6263  N  NE2 . HIS F  1 107 ? 56.150  30.188  10.247  1.00 32.92 ? 80  HIS F NE2 1 
ATOM   6264  N  N   . VAL F  1 108 ? 60.484  34.626  8.018   1.00 29.50 ? 81  VAL F N   1 
ATOM   6265  C  CA  . VAL F  1 108 ? 61.429  35.724  7.971   1.00 27.74 ? 81  VAL F CA  1 
ATOM   6266  C  C   . VAL F  1 108 ? 61.855  36.056  9.413   1.00 27.33 ? 81  VAL F C   1 
ATOM   6267  O  O   . VAL F  1 108 ? 63.042  36.343  9.697   1.00 29.13 ? 81  VAL F O   1 
ATOM   6268  C  CB  . VAL F  1 108 ? 60.830  36.963  7.219   1.00 28.89 ? 81  VAL F CB  1 
ATOM   6269  C  CG1 . VAL F  1 108 ? 61.702  38.210  7.409   1.00 26.13 ? 81  VAL F CG1 1 
ATOM   6270  C  CG2 . VAL F  1 108 ? 60.645  36.604  5.733   1.00 27.50 ? 81  VAL F CG2 1 
ATOM   6271  N  N   . GLY F  1 109 ? 60.903  36.011  10.325  1.00 28.32 ? 82  GLY F N   1 
ATOM   6272  C  CA  . GLY F  1 109 ? 61.232  36.359  11.723  1.00 32.13 ? 82  GLY F CA  1 
ATOM   6273  C  C   . GLY F  1 109 ? 62.048  35.323  12.523  1.00 36.93 ? 82  GLY F C   1 
ATOM   6274  O  O   . GLY F  1 109 ? 62.356  35.565  13.710  1.00 30.25 ? 82  GLY F O   1 
ATOM   6275  N  N   . ASP F  1 110 ? 62.401  34.168  11.912  1.00 32.69 ? 83  ASP F N   1 
ATOM   6276  C  CA  . ASP F  1 110 ? 62.963  33.028  12.724  1.00 32.04 ? 83  ASP F CA  1 
ATOM   6277  C  C   . ASP F  1 110 ? 64.399  33.283  13.017  1.00 30.03 ? 83  ASP F C   1 
ATOM   6278  O  O   . ASP F  1 110 ? 65.261  33.018  12.189  1.00 35.19 ? 83  ASP F O   1 
ATOM   6279  C  CB  . ASP F  1 110 ? 62.829  31.690  11.972  1.00 33.17 ? 83  ASP F CB  1 
ATOM   6280  C  CG  . ASP F  1 110 ? 61.424  31.185  11.973  1.00 34.83 ? 83  ASP F CG  1 
ATOM   6281  O  OD1 . ASP F  1 110 ? 60.637  31.702  12.813  1.00 33.02 ? 83  ASP F OD1 1 
ATOM   6282  O  OD2 . ASP F  1 110 ? 61.059  30.280  11.155  1.00 39.32 ? 83  ASP F OD2 1 
ATOM   6283  N  N   . LEU F  1 111 ? 64.707  33.839  14.179  1.00 27.88 ? 84  LEU F N   1 
ATOM   6284  C  CA  . LEU F  1 111 ? 66.106  34.151  14.450  1.00 28.30 ? 84  LEU F CA  1 
ATOM   6285  C  C   . LEU F  1 111 ? 66.798  33.105  15.371  1.00 30.23 ? 84  LEU F C   1 
ATOM   6286  O  O   . LEU F  1 111 ? 67.904  33.334  15.868  1.00 35.36 ? 84  LEU F O   1 
ATOM   6287  C  CB  . LEU F  1 111 ? 66.247  35.544  15.050  1.00 31.73 ? 84  LEU F CB  1 
ATOM   6288  C  CG  . LEU F  1 111 ? 65.897  36.656  14.044  1.00 32.43 ? 84  LEU F CG  1 
ATOM   6289  C  CD1 . LEU F  1 111 ? 65.974  38.006  14.752  1.00 34.57 ? 84  LEU F CD1 1 
ATOM   6290  C  CD2 . LEU F  1 111 ? 66.867  36.605  12.856  1.00 31.81 ? 84  LEU F CD2 1 
ATOM   6291  N  N   . GLY F  1 112 ? 66.154  31.976  15.583  1.00 30.08 ? 85  GLY F N   1 
ATOM   6292  C  CA  . GLY F  1 112 ? 66.877  30.873  16.315  1.00 33.57 ? 85  GLY F CA  1 
ATOM   6293  C  C   . GLY F  1 112 ? 66.760  30.966  17.825  1.00 31.75 ? 85  GLY F C   1 
ATOM   6294  O  O   . GLY F  1 112 ? 65.683  31.216  18.340  1.00 32.78 ? 85  GLY F O   1 
ATOM   6295  N  N   . ASN F  1 113 ? 67.869  30.753  18.532  1.00 33.13 ? 86  ASN F N   1 
ATOM   6296  C  CA  . ASN F  1 113 ? 67.846  30.788  19.983  1.00 32.80 ? 86  ASN F CA  1 
ATOM   6297  C  C   . ASN F  1 113 ? 68.933  31.700  20.431  1.00 33.04 ? 86  ASN F C   1 
ATOM   6298  O  O   . ASN F  1 113 ? 69.968  31.820  19.781  1.00 35.31 ? 86  ASN F O   1 
ATOM   6299  C  CB  . ASN F  1 113 ? 68.140  29.399  20.558  1.00 34.39 ? 86  ASN F CB  1 
ATOM   6300  C  CG  . ASN F  1 113 ? 66.998  28.459  20.356  1.00 34.28 ? 86  ASN F CG  1 
ATOM   6301  O  OD1 . ASN F  1 113 ? 65.914  28.620  20.953  1.00 32.73 ? 86  ASN F OD1 1 
ATOM   6302  N  ND2 . ASN F  1 113 ? 67.211  27.462  19.489  1.00 36.28 ? 86  ASN F ND2 1 
ATOM   6303  N  N   . VAL F  1 114 ? 68.712  32.352  21.562  1.00 32.39 ? 87  VAL F N   1 
ATOM   6304  C  CA  . VAL F  1 114 ? 69.828  32.980  22.224  1.00 31.37 ? 87  VAL F CA  1 
ATOM   6305  C  C   . VAL F  1 114 ? 70.138  32.109  23.462  1.00 27.49 ? 87  VAL F C   1 
ATOM   6306  O  O   . VAL F  1 114 ? 69.274  31.334  23.930  1.00 29.11 ? 87  VAL F O   1 
ATOM   6307  C  CB  . VAL F  1 114 ? 69.521  34.450  22.635  1.00 31.71 ? 87  VAL F CB  1 
ATOM   6308  C  CG1 . VAL F  1 114 ? 69.285  35.291  21.378  1.00 31.36 ? 87  VAL F CG1 1 
ATOM   6309  C  CG2 . VAL F  1 114 ? 68.317  34.481  23.580  1.00 30.16 ? 87  VAL F CG2 1 
ATOM   6310  N  N   . THR F  1 115 ? 71.328  32.320  23.993  1.00 30.54 ? 88  THR F N   1 
ATOM   6311  C  CA  . THR F  1 115 ? 71.844  31.556  25.138  1.00 33.59 ? 88  THR F CA  1 
ATOM   6312  C  C   . THR F  1 115 ? 72.140  32.376  26.394  1.00 29.99 ? 88  THR F C   1 
ATOM   6313  O  O   . THR F  1 115 ? 73.068  33.201  26.423  1.00 33.13 ? 88  THR F O   1 
ATOM   6314  C  CB  . THR F  1 115 ? 73.117  30.760  24.718  1.00 36.69 ? 88  THR F CB  1 
ATOM   6315  O  OG1 . THR F  1 115 ? 72.779  29.938  23.598  1.00 38.45 ? 88  THR F OG1 1 
ATOM   6316  C  CG2 . THR F  1 115 ? 73.635  29.832  25.886  1.00 38.73 ? 88  THR F CG2 1 
ATOM   6317  N  N   . ALA F  1 116 ? 71.393  32.092  27.449  1.00 34.84 ? 89  ALA F N   1 
ATOM   6318  C  CA  . ALA F  1 116 ? 71.617  32.755  28.735  1.00 35.50 ? 89  ALA F CA  1 
ATOM   6319  C  C   . ALA F  1 116 ? 72.630  31.929  29.569  1.00 35.19 ? 89  ALA F C   1 
ATOM   6320  O  O   . ALA F  1 116 ? 72.459  30.719  29.736  1.00 37.13 ? 89  ALA F O   1 
ATOM   6321  C  CB  . ALA F  1 116 ? 70.288  32.920  29.485  1.00 30.43 ? 89  ALA F CB  1 
ATOM   6322  N  N   . ASP F  1 117 ? 73.671  32.614  30.040  1.00 35.49 ? 90  ASP F N   1 
ATOM   6323  C  CA  . ASP F  1 117 ? 74.678  32.066  30.928  1.00 37.66 ? 90  ASP F CA  1 
ATOM   6324  C  C   . ASP F  1 117 ? 74.133  31.785  32.315  1.00 38.38 ? 90  ASP F C   1 
ATOM   6325  O  O   . ASP F  1 117 ? 72.919  31.892  32.560  1.00 37.77 ? 90  ASP F O   1 
ATOM   6326  C  CB  . ASP F  1 117 ? 75.938  32.949  30.956  1.00 34.17 ? 90  ASP F CB  1 
ATOM   6327  C  CG  . ASP F  1 117 ? 75.761  34.279  31.696  1.00 39.67 ? 90  ASP F CG  1 
ATOM   6328  O  OD1 . ASP F  1 117 ? 74.795  34.480  32.457  1.00 42.17 ? 90  ASP F OD1 1 
ATOM   6329  O  OD2 . ASP F  1 117 ? 76.658  35.131  31.555  1.00 35.87 ? 90  ASP F OD2 1 
ATOM   6330  N  N   . LYS F  1 118 ? 75.025  31.401  33.230  1.00 38.89 ? 91  LYS F N   1 
ATOM   6331  C  CA  . LYS F  1 118 ? 74.556  31.006  34.552  1.00 40.33 ? 91  LYS F CA  1 
ATOM   6332  C  C   . LYS F  1 118 ? 74.098  32.219  35.357  1.00 40.01 ? 91  LYS F C   1 
ATOM   6333  O  O   . LYS F  1 118 ? 73.308  32.070  36.292  1.00 41.50 ? 91  LYS F O   1 
ATOM   6334  C  CB  . LYS F  1 118 ? 75.605  30.183  35.309  1.00 41.93 ? 91  LYS F CB  1 
ATOM   6335  C  CG  . LYS F  1 118 ? 76.808  30.979  35.750  1.00 48.30 ? 91  LYS F CG  1 
ATOM   6336  C  CD  . LYS F  1 118 ? 77.538  30.231  36.868  1.00 56.16 ? 91  LYS F CD  1 
ATOM   6337  C  CE  . LYS F  1 118 ? 79.028  30.346  36.655  1.00 53.67 ? 91  LYS F CE  1 
ATOM   6338  N  NZ  . LYS F  1 118 ? 79.425  31.778  36.532  1.00 65.65 ? 91  LYS F NZ  1 
ATOM   6339  N  N   . ASP F  1 119 ? 74.570  33.413  34.976  1.00 38.35 ? 92  ASP F N   1 
ATOM   6340  C  CA  . ASP F  1 119 ? 74.098  34.666  35.600  1.00 39.47 ? 92  ASP F CA  1 
ATOM   6341  C  C   . ASP F  1 119 ? 72.821  35.240  34.981  1.00 39.16 ? 92  ASP F C   1 
ATOM   6342  O  O   . ASP F  1 119 ? 72.438  36.377  35.302  1.00 36.51 ? 92  ASP F O   1 
ATOM   6343  C  CB  . ASP F  1 119 ? 75.205  35.709  35.588  1.00 41.19 ? 92  ASP F CB  1 
ATOM   6344  C  CG  . ASP F  1 119 ? 76.415  35.257  36.392  1.00 52.26 ? 92  ASP F CG  1 
ATOM   6345  O  OD1 . ASP F  1 119 ? 76.220  34.807  37.545  1.00 51.35 ? 92  ASP F OD1 1 
ATOM   6346  O  OD2 . ASP F  1 119 ? 77.546  35.350  35.877  1.00 53.85 ? 92  ASP F OD2 1 
ATOM   6347  N  N   . GLY F  1 120 ? 72.183  34.457  34.112  1.00 32.41 ? 93  GLY F N   1 
ATOM   6348  C  CA  . GLY F  1 120 ? 70.922  34.819  33.479  1.00 34.82 ? 93  GLY F CA  1 
ATOM   6349  C  C   . GLY F  1 120 ? 71.055  35.844  32.335  1.00 32.59 ? 93  GLY F C   1 
ATOM   6350  O  O   . GLY F  1 120 ? 70.061  36.394  31.898  1.00 36.70 ? 93  GLY F O   1 
ATOM   6351  N  N   . VAL F  1 121 ? 72.276  36.083  31.868  1.00 32.03 ? 94  VAL F N   1 
ATOM   6352  C  CA  . VAL F  1 121 ? 72.556  37.068  30.833  1.00 33.28 ? 94  VAL F CA  1 
ATOM   6353  C  C   . VAL F  1 121 ? 72.834  36.388  29.482  1.00 37.99 ? 94  VAL F C   1 
ATOM   6354  O  O   . VAL F  1 121 ? 73.684  35.477  29.391  1.00 33.12 ? 94  VAL F O   1 
ATOM   6355  C  CB  . VAL F  1 121 ? 73.754  37.958  31.255  1.00 33.92 ? 94  VAL F CB  1 
ATOM   6356  C  CG1 . VAL F  1 121 ? 74.173  38.903  30.128  1.00 35.68 ? 94  VAL F CG1 1 
ATOM   6357  C  CG2 . VAL F  1 121 ? 73.416  38.728  32.534  1.00 33.66 ? 94  VAL F CG2 1 
ATOM   6358  N  N   . ALA F  1 122 ? 72.123  36.804  28.434  1.00 32.02 ? 95  ALA F N   1 
ATOM   6359  C  CA  . ALA F  1 122 ? 72.346  36.254  27.092  1.00 33.56 ? 95  ALA F CA  1 
ATOM   6360  C  C   . ALA F  1 122 ? 72.993  37.343  26.267  1.00 37.91 ? 95  ALA F C   1 
ATOM   6361  O  O   . ALA F  1 122 ? 72.371  38.392  26.072  1.00 36.75 ? 95  ALA F O   1 
ATOM   6362  C  CB  . ALA F  1 122 ? 71.025  35.802  26.459  1.00 32.68 ? 95  ALA F CB  1 
ATOM   6363  N  N   . ASP F  1 123 ? 74.244  37.131  25.837  1.00 31.74 ? 96  ASP F N   1 
ATOM   6364  C  CA  . ASP F  1 123 ? 74.910  38.027  24.906  1.00 36.84 ? 96  ASP F CA  1 
ATOM   6365  C  C   . ASP F  1 123 ? 74.558  37.586  23.509  1.00 39.14 ? 96  ASP F C   1 
ATOM   6366  O  O   . ASP F  1 123 ? 74.724  36.407  23.156  1.00 38.56 ? 96  ASP F O   1 
ATOM   6367  C  CB  . ASP F  1 123 ? 76.415  38.051  25.116  1.00 46.25 ? 96  ASP F CB  1 
ATOM   6368  C  CG  . ASP F  1 123 ? 76.796  38.764  26.393  1.00 60.51 ? 96  ASP F CG  1 
ATOM   6369  O  OD1 . ASP F  1 123 ? 75.913  39.453  26.994  1.00 65.82 ? 96  ASP F OD1 1 
ATOM   6370  O  OD2 . ASP F  1 123 ? 77.976  38.647  26.795  1.00 64.37 ? 96  ASP F OD2 1 
ATOM   6371  N  N   . VAL F  1 124 ? 73.965  38.514  22.754  1.00 33.58 ? 97  VAL F N   1 
ATOM   6372  C  CA  . VAL F  1 124 ? 73.395  38.222  21.422  1.00 34.70 ? 97  VAL F CA  1 
ATOM   6373  C  C   . VAL F  1 124 ? 74.328  38.805  20.394  1.00 31.59 ? 97  VAL F C   1 
ATOM   6374  O  O   . VAL F  1 124 ? 74.743  39.968  20.503  1.00 27.23 ? 97  VAL F O   1 
ATOM   6375  C  CB  . VAL F  1 124 ? 72.001  38.846  21.193  1.00 36.30 ? 97  VAL F CB  1 
ATOM   6376  C  CG1 . VAL F  1 124 ? 71.433  38.409  19.839  1.00 34.48 ? 97  VAL F CG1 1 
ATOM   6377  C  CG2 . VAL F  1 124 ? 71.032  38.502  22.313  1.00 36.72 ? 97  VAL F CG2 1 
ATOM   6378  N  N   . SER F  1 125 ? 74.721  37.949  19.444  1.00 32.95 ? 98  SER F N   1 
ATOM   6379  C  CA  . SER F  1 125 ? 75.530  38.310  18.303  1.00 34.45 ? 98  SER F CA  1 
ATOM   6380  C  C   . SER F  1 125 ? 75.110  37.413  17.139  1.00 38.09 ? 98  SER F C   1 
ATOM   6381  O  O   . SER F  1 125 ? 75.281  36.188  17.168  1.00 35.53 ? 98  SER F O   1 
ATOM   6382  C  CB  . SER F  1 125 ? 77.004  38.120  18.602  1.00 37.26 ? 98  SER F CB  1 
ATOM   6383  O  OG  . SER F  1 125 ? 77.740  38.999  17.780  1.00 38.97 ? 98  SER F OG  1 
ATOM   6384  N  N   . ILE F  1 126 ? 74.529  38.024  16.119  1.00 33.47 ? 99  ILE F N   1 
ATOM   6385  C  CA  . ILE F  1 126 ? 73.829  37.286  15.072  1.00 35.67 ? 99  ILE F CA  1 
ATOM   6386  C  C   . ILE F  1 126 ? 74.101  38.106  13.809  1.00 34.60 ? 99  ILE F C   1 
ATOM   6387  O  O   . ILE F  1 126 ? 74.206  39.343  13.859  1.00 30.18 ? 99  ILE F O   1 
ATOM   6388  C  CB  . ILE F  1 126 ? 72.289  37.283  15.339  1.00 36.52 ? 99  ILE F CB  1 
ATOM   6389  C  CG1 . ILE F  1 126 ? 71.900  36.200  16.333  1.00 42.00 ? 99  ILE F CG1 1 
ATOM   6390  C  CG2 . ILE F  1 126 ? 71.474  37.031  14.078  1.00 38.79 ? 99  ILE F CG2 1 
ATOM   6391  C  CD1 . ILE F  1 126 ? 70.396  36.107  16.577  1.00 40.86 ? 99  ILE F CD1 1 
ATOM   6392  N  N   . GLU F  1 127 ? 74.243  37.420  12.686  1.00 33.83 ? 100 GLU F N   1 
ATOM   6393  C  CA  . GLU F  1 127 ? 74.258  38.100  11.404  1.00 34.66 ? 100 GLU F CA  1 
ATOM   6394  C  C   . GLU F  1 127 ? 73.249  37.342  10.562  1.00 33.61 ? 100 GLU F C   1 
ATOM   6395  O  O   . GLU F  1 127 ? 73.290  36.116  10.505  1.00 35.27 ? 100 GLU F O   1 
ATOM   6396  C  CB  . GLU F  1 127 ? 75.678  38.151  10.841  1.00 39.30 ? 100 GLU F CB  1 
ATOM   6397  C  CG  . GLU F  1 127 ? 75.760  38.761  9.457   1.00 48.97 ? 100 GLU F CG  1 
ATOM   6398  C  CD  . GLU F  1 127 ? 77.201  39.011  9.000   1.00 58.07 ? 100 GLU F CD  1 
ATOM   6399  O  OE1 . GLU F  1 127 ? 77.942  39.766  9.678   1.00 60.81 ? 100 GLU F OE1 1 
ATOM   6400  O  OE2 . GLU F  1 127 ? 77.588  38.448  7.953   1.00 64.66 ? 100 GLU F OE2 1 
ATOM   6401  N  N   . ASP F  1 128 ? 72.256  38.026  9.992   1.00 30.62 ? 101 ASP F N   1 
ATOM   6402  C  CA  . ASP F  1 128 ? 71.190  37.272  9.319   1.00 27.15 ? 101 ASP F CA  1 
ATOM   6403  C  C   . ASP F  1 128 ? 70.895  37.913  7.964   1.00 31.00 ? 101 ASP F C   1 
ATOM   6404  O  O   . ASP F  1 128 ? 70.790  39.157  7.890   1.00 28.51 ? 101 ASP F O   1 
ATOM   6405  C  CB  . ASP F  1 128 ? 69.916  37.220  10.164  1.00 29.80 ? 101 ASP F CB  1 
ATOM   6406  C  CG  . ASP F  1 128 ? 68.853  36.292  9.573   1.00 33.22 ? 101 ASP F CG  1 
ATOM   6407  O  OD1 . ASP F  1 128 ? 68.897  35.060  9.849   1.00 36.28 ? 101 ASP F OD1 1 
ATOM   6408  O  OD2 . ASP F  1 128 ? 67.963  36.763  8.820   1.00 32.01 ? 101 ASP F OD2 1 
ATOM   6409  N  N   A SER F  1 129 ? 70.740  37.079  6.926   0.50 29.76 ? 102 SER F N   1 
ATOM   6410  N  N   B SER F  1 129 ? 70.730  37.102  6.913   0.50 29.11 ? 102 SER F N   1 
ATOM   6411  C  CA  A SER F  1 129 ? 70.581  37.575  5.547   0.50 31.63 ? 102 SER F CA  1 
ATOM   6412  C  CA  B SER F  1 129 ? 70.553  37.657  5.555   0.50 30.27 ? 102 SER F CA  1 
ATOM   6413  C  C   A SER F  1 129 ? 69.136  37.478  5.054   0.50 28.60 ? 102 SER F C   1 
ATOM   6414  C  C   B SER F  1 129 ? 69.119  37.526  5.062   0.50 27.89 ? 102 SER F C   1 
ATOM   6415  O  O   A SER F  1 129 ? 68.854  37.729  3.889   0.50 31.18 ? 102 SER F O   1 
ATOM   6416  O  O   B SER F  1 129 ? 68.830  37.783  3.900   0.50 30.53 ? 102 SER F O   1 
ATOM   6417  C  CB  A SER F  1 129 ? 71.534  36.841  4.573   0.50 32.60 ? 102 SER F CB  1 
ATOM   6418  C  CB  B SER F  1 129 ? 71.490  36.969  4.557   0.50 30.66 ? 102 SER F CB  1 
ATOM   6419  O  OG  A SER F  1 129 ? 72.875  37.302  4.715   0.50 33.17 ? 102 SER F OG  1 
ATOM   6420  O  OG  B SER F  1 129 ? 71.303  35.579  4.636   0.50 28.34 ? 102 SER F OG  1 
ATOM   6421  N  N   . VAL F  1 130 ? 68.214  37.117  5.926   1.00 25.96 ? 103 VAL F N   1 
ATOM   6422  C  CA  . VAL F  1 130 ? 66.823  36.989  5.499   1.00 28.19 ? 103 VAL F CA  1 
ATOM   6423  C  C   . VAL F  1 130 ? 65.950  38.207  5.966   1.00 31.46 ? 103 VAL F C   1 
ATOM   6424  O  O   . VAL F  1 130 ? 65.182  38.778  5.163   1.00 27.58 ? 103 VAL F O   1 
ATOM   6425  C  CB  . VAL F  1 130 ? 66.229  35.653  5.926   1.00 28.69 ? 103 VAL F CB  1 
ATOM   6426  C  CG1 . VAL F  1 130 ? 64.732  35.588  5.639   1.00 28.19 ? 103 VAL F CG1 1 
ATOM   6427  C  CG2 . VAL F  1 130 ? 66.971  34.501  5.198   1.00 31.46 ? 103 VAL F CG2 1 
ATOM   6428  N  N   . ILE F  1 131 ? 66.066  38.576  7.244   1.00 29.80 ? 104 ILE F N   1 
ATOM   6429  C  CA  . ILE F  1 131 ? 65.456  39.847  7.723   1.00 26.79 ? 104 ILE F CA  1 
ATOM   6430  C  C   . ILE F  1 131 ? 66.110  41.051  7.032   1.00 26.00 ? 104 ILE F C   1 
ATOM   6431  O  O   . ILE F  1 131 ? 67.319  41.032  6.617   1.00 25.14 ? 104 ILE F O   1 
ATOM   6432  C  CB  . ILE F  1 131 ? 65.620  40.006  9.253   1.00 26.36 ? 104 ILE F CB  1 
ATOM   6433  C  CG1 . ILE F  1 131 ? 67.111  40.088  9.648   1.00 24.10 ? 104 ILE F CG1 1 
ATOM   6434  C  CG2 . ILE F  1 131 ? 64.867  38.903  9.953   1.00 26.17 ? 104 ILE F CG2 1 
ATOM   6435  C  CD1 . ILE F  1 131 ? 67.402  40.491  11.091  1.00 25.58 ? 104 ILE F CD1 1 
ATOM   6436  N  N   . SER F  1 132 ? 65.349  42.146  6.930   1.00 22.75 ? 105 SER F N   1 
ATOM   6437  C  CA  . SER F  1 132 ? 65.929  43.357  6.371   1.00 20.48 ? 105 SER F CA  1 
ATOM   6438  C  C   . SER F  1 132 ? 65.404  44.560  7.174   1.00 19.89 ? 105 SER F C   1 
ATOM   6439  O  O   . SER F  1 132 ? 64.387  44.426  7.855   1.00 21.79 ? 105 SER F O   1 
ATOM   6440  C  CB  . SER F  1 132 ? 65.504  43.510  4.878   1.00 18.91 ? 105 SER F CB  1 
ATOM   6441  O  OG  . SER F  1 132 ? 66.363  44.523  4.302   1.00 21.92 ? 105 SER F OG  1 
ATOM   6442  N  N   . LEU F  1 133 ? 66.121  45.670  7.134   1.00 21.89 ? 106 LEU F N   1 
ATOM   6443  C  CA  . LEU F  1 133 ? 65.573  46.931  7.683   1.00 21.45 ? 106 LEU F CA  1 
ATOM   6444  C  C   . LEU F  1 133 ? 64.889  47.814  6.608   1.00 25.22 ? 106 LEU F C   1 
ATOM   6445  O  O   . LEU F  1 133 ? 64.589  48.994  6.884   1.00 22.83 ? 106 LEU F O   1 
ATOM   6446  C  CB  . LEU F  1 133 ? 66.657  47.710  8.395   1.00 19.81 ? 106 LEU F CB  1 
ATOM   6447  C  CG  . LEU F  1 133 ? 67.435  46.915  9.485   1.00 19.76 ? 106 LEU F CG  1 
ATOM   6448  C  CD1 . LEU F  1 133 ? 68.483  47.776  10.159  1.00 22.70 ? 106 LEU F CD1 1 
ATOM   6449  C  CD2 . LEU F  1 133 ? 66.488  46.265  10.481  1.00 19.33 ? 106 LEU F CD2 1 
ATOM   6450  N  N   . SER F  1 134 ? 64.652  47.248  5.435   1.00 25.80 ? 107 SER F N   1 
ATOM   6451  C  CA  . SER F  1 134 ? 63.952  47.937  4.328   1.00 27.65 ? 107 SER F CA  1 
ATOM   6452  C  C   . SER F  1 134 ? 63.325  46.917  3.389   1.00 30.82 ? 107 SER F C   1 
ATOM   6453  O  O   . SER F  1 134 ? 63.644  45.719  3.479   1.00 26.36 ? 107 SER F O   1 
ATOM   6454  C  CB  . SER F  1 134 ? 64.882  48.933  3.618   1.00 32.00 ? 107 SER F CB  1 
ATOM   6455  O  OG  . SER F  1 134 ? 66.068  48.326  3.105   1.00 33.18 ? 107 SER F OG  1 
ATOM   6456  N  N   . GLY F  1 135 ? 62.385  47.362  2.531   1.00 30.22 ? 108 GLY F N   1 
ATOM   6457  C  CA  . GLY F  1 135 ? 61.568  46.491  1.650   1.00 31.69 ? 108 GLY F CA  1 
ATOM   6458  C  C   . GLY F  1 135 ? 60.599  45.469  2.242   1.00 41.58 ? 108 GLY F C   1 
ATOM   6459  O  O   . GLY F  1 135 ? 60.056  45.634  3.318   1.00 40.00 ? 108 GLY F O   1 
ATOM   6460  N  N   . ASP F  1 136 ? 60.402  44.358  1.553   1.00 39.33 ? 109 ASP F N   1 
ATOM   6461  C  CA  . ASP F  1 136 ? 59.327  43.438  1.937   1.00 45.80 ? 109 ASP F CA  1 
ATOM   6462  C  C   . ASP F  1 136 ? 59.635  42.534  3.152   1.00 38.59 ? 109 ASP F C   1 
ATOM   6463  O  O   . ASP F  1 136 ? 58.739  42.064  3.827   1.00 40.09 ? 109 ASP F O   1 
ATOM   6464  C  CB  . ASP F  1 136 ? 58.901  42.615  0.711   1.00 49.16 ? 109 ASP F CB  1 
ATOM   6465  C  CG  . ASP F  1 136 ? 57.917  43.393  -0.236  1.00 54.74 ? 109 ASP F CG  1 
ATOM   6466  O  OD1 . ASP F  1 136 ? 57.777  44.643  -0.113  1.00 54.89 ? 109 ASP F OD1 1 
ATOM   6467  O  OD2 . ASP F  1 136 ? 57.289  42.740  -1.110  1.00 54.36 ? 109 ASP F OD2 1 
ATOM   6468  N  N   . HIS F  1 137 ? 60.911  42.266  3.387   1.00 38.25 ? 110 HIS F N   1 
ATOM   6469  C  CA  . HIS F  1 137 ? 61.330  41.513  4.581   1.00 38.60 ? 110 HIS F CA  1 
ATOM   6470  C  C   . HIS F  1 137 ? 61.585  42.475  5.763   1.00 34.57 ? 110 HIS F C   1 
ATOM   6471  O  O   . HIS F  1 137 ? 62.299  42.068  6.703   1.00 34.36 ? 110 HIS F O   1 
ATOM   6472  C  CB  . HIS F  1 137 ? 62.614  40.677  4.283   1.00 37.61 ? 110 HIS F CB  1 
ATOM   6473  C  CG  . HIS F  1 137 ? 62.365  39.448  3.459   1.00 42.24 ? 110 HIS F CG  1 
ATOM   6474  N  ND1 . HIS F  1 137 ? 63.323  38.469  3.262   1.00 45.71 ? 110 HIS F ND1 1 
ATOM   6475  C  CD2 . HIS F  1 137 ? 61.256  39.024  2.800   1.00 43.39 ? 110 HIS F CD2 1 
ATOM   6476  C  CE1 . HIS F  1 137 ? 62.819  37.506  2.508   1.00 45.38 ? 110 HIS F CE1 1 
ATOM   6477  N  NE2 . HIS F  1 137 ? 61.562  37.812  2.225   1.00 42.24 ? 110 HIS F NE2 1 
ATOM   6478  N  N   . CYS F  1 138 ? 61.065  43.722  5.672   1.00 28.51 ? 111 CYS F N   1 
ATOM   6479  C  CA  . CYS F  1 138 ? 61.479  44.820  6.587   1.00 26.76 ? 111 CYS F CA  1 
ATOM   6480  C  C   . CYS F  1 138 ? 60.846  44.549  7.958   1.00 21.66 ? 111 CYS F C   1 
ATOM   6481  O  O   . CYS F  1 138 ? 59.676  44.200  8.007   1.00 22.44 ? 111 CYS F O   1 
ATOM   6482  C  CB  . CYS F  1 138 ? 61.029  46.165  6.053   1.00 29.65 ? 111 CYS F CB  1 
ATOM   6483  S  SG  . CYS F  1 138 ? 61.130  47.502  7.248   1.00 31.99 ? 111 CYS F SG  1 
ATOM   6484  N  N   . ILE F  1 139 ? 61.638  44.671  9.024   1.00 20.88 ? 112 ILE F N   1 
ATOM   6485  C  CA  . ILE F  1 139 ? 61.151  44.265  10.359  1.00 21.55 ? 112 ILE F CA  1 
ATOM   6486  C  C   . ILE F  1 139 ? 60.896  45.505  11.245  1.00 21.02 ? 112 ILE F C   1 
ATOM   6487  O  O   . ILE F  1 139 ? 60.468  45.366  12.391  1.00 19.09 ? 112 ILE F O   1 
ATOM   6488  C  CB  . ILE F  1 139 ? 62.125  43.285  11.055  1.00 19.97 ? 112 ILE F CB  1 
ATOM   6489  C  CG1 . ILE F  1 139 ? 63.475  43.959  11.284  1.00 22.69 ? 112 ILE F CG1 1 
ATOM   6490  C  CG2 . ILE F  1 139 ? 62.174  41.979  10.190  1.00 20.93 ? 112 ILE F CG2 1 
ATOM   6491  C  CD1 . ILE F  1 139 ? 64.510  43.157  12.085  1.00 25.00 ? 112 ILE F CD1 1 
ATOM   6492  N  N   . ILE F  1 140 ? 61.143  46.687  10.680  1.00 22.43 ? 113 ILE F N   1 
ATOM   6493  C  CA  . ILE F  1 140 ? 60.895  47.945  11.449  1.00 24.63 ? 113 ILE F CA  1 
ATOM   6494  C  C   . ILE F  1 140 ? 59.395  48.045  11.724  1.00 20.57 ? 113 ILE F C   1 
ATOM   6495  O  O   . ILE F  1 140 ? 58.565  47.753  10.853  1.00 21.83 ? 113 ILE F O   1 
ATOM   6496  C  CB  . ILE F  1 140 ? 61.329  49.188  10.669  1.00 25.99 ? 113 ILE F CB  1 
ATOM   6497  C  CG1 . ILE F  1 140 ? 62.759  49.052  10.235  1.00 28.92 ? 113 ILE F CG1 1 
ATOM   6498  C  CG2 . ILE F  1 140 ? 61.031  50.492  11.476  1.00 23.46 ? 113 ILE F CG2 1 
ATOM   6499  C  CD1 . ILE F  1 140 ? 63.748  49.345  11.281  1.00 27.70 ? 113 ILE F CD1 1 
ATOM   6500  N  N   . GLY F  1 141 ? 59.002  48.420  12.947  1.00 20.40 ? 114 GLY F N   1 
ATOM   6501  C  CA  . GLY F  1 141 ? 57.555  48.451  13.250  1.00 16.42 ? 114 GLY F CA  1 
ATOM   6502  C  C   . GLY F  1 141 ? 56.952  47.121  13.693  1.00 18.25 ? 114 GLY F C   1 
ATOM   6503  O  O   . GLY F  1 141 ? 55.782  47.041  14.020  1.00 17.37 ? 114 GLY F O   1 
ATOM   6504  N  N   . ARG F  1 142 ? 57.740  46.035  13.674  1.00 19.34 ? 115 ARG F N   1 
ATOM   6505  C  CA  . ARG F  1 142 ? 57.205  44.733  14.125  1.00 21.41 ? 115 ARG F CA  1 
ATOM   6506  C  C   . ARG F  1 142 ? 57.809  44.504  15.515  1.00 21.37 ? 115 ARG F C   1 
ATOM   6507  O  O   . ARG F  1 142 ? 58.502  45.368  16.035  1.00 20.41 ? 115 ARG F O   1 
ATOM   6508  C  CB  . ARG F  1 142 ? 57.580  43.614  13.131  1.00 20.92 ? 115 ARG F CB  1 
ATOM   6509  C  CG  . ARG F  1 142 ? 57.104  44.084  11.733  1.00 22.39 ? 115 ARG F CG  1 
ATOM   6510  C  CD  . ARG F  1 142 ? 57.115  42.997  10.686  1.00 25.04 ? 115 ARG F CD  1 
ATOM   6511  N  NE  . ARG F  1 142 ? 56.699  43.542  9.366   1.00 27.24 ? 115 ARG F NE  1 
ATOM   6512  C  CZ  . ARG F  1 142 ? 55.443  43.566  8.913   1.00 25.34 ? 115 ARG F CZ  1 
ATOM   6513  N  NH1 . ARG F  1 142 ? 54.440  43.049  9.609   1.00 23.76 ? 115 ARG F NH1 1 
ATOM   6514  N  NH2 . ARG F  1 142 ? 55.192  44.055  7.696   1.00 24.83 ? 115 ARG F NH2 1 
ATOM   6515  N  N   . THR F  1 143 ? 57.569  43.334  16.091  1.00 23.05 ? 116 THR F N   1 
ATOM   6516  C  CA  . THR F  1 143 ? 57.913  43.131  17.517  1.00 22.57 ? 116 THR F CA  1 
ATOM   6517  C  C   . THR F  1 143 ? 58.973  42.009  17.654  1.00 24.77 ? 116 THR F C   1 
ATOM   6518  O  O   . THR F  1 143 ? 58.821  40.971  17.004  1.00 26.67 ? 116 THR F O   1 
ATOM   6519  C  CB  . THR F  1 143 ? 56.662  42.688  18.262  1.00 24.66 ? 116 THR F CB  1 
ATOM   6520  O  OG1 . THR F  1 143 ? 55.738  43.774  18.318  1.00 25.62 ? 116 THR F OG1 1 
ATOM   6521  C  CG2 . THR F  1 143 ? 56.970  42.232  19.744  1.00 22.62 ? 116 THR F CG2 1 
ATOM   6522  N  N   . LEU F  1 144 ? 60.029  42.235  18.437  1.00 20.99 ? 117 LEU F N   1 
ATOM   6523  C  CA  . LEU F  1 144 ? 61.030  41.171  18.728  1.00 21.09 ? 117 LEU F CA  1 
ATOM   6524  C  C   . LEU F  1 144 ? 60.593  40.568  20.029  1.00 25.08 ? 117 LEU F C   1 
ATOM   6525  O  O   . LEU F  1 144 ? 60.195  41.308  20.921  1.00 21.99 ? 117 LEU F O   1 
ATOM   6526  C  CB  . LEU F  1 144 ? 62.396  41.772  18.849  1.00 22.57 ? 117 LEU F CB  1 
ATOM   6527  C  CG  . LEU F  1 144 ? 63.526  40.815  19.111  1.00 23.04 ? 117 LEU F CG  1 
ATOM   6528  C  CD1 . LEU F  1 144 ? 63.721  39.961  17.848  1.00 23.90 ? 117 LEU F CD1 1 
ATOM   6529  C  CD2 . LEU F  1 144 ? 64.724  41.681  19.360  1.00 22.55 ? 117 LEU F CD2 1 
ATOM   6530  N  N   . VAL F  1 145 ? 60.596  39.233  20.114  1.00 25.05 ? 118 VAL F N   1 
ATOM   6531  C  CA  . VAL F  1 145 ? 60.122  38.515  21.310  1.00 26.25 ? 118 VAL F CA  1 
ATOM   6532  C  C   . VAL F  1 145 ? 61.220  37.506  21.745  1.00 28.20 ? 118 VAL F C   1 
ATOM   6533  O  O   . VAL F  1 145 ? 61.828  36.809  20.891  1.00 26.44 ? 118 VAL F O   1 
ATOM   6534  C  CB  . VAL F  1 145 ? 58.815  37.769  21.001  1.00 24.84 ? 118 VAL F CB  1 
ATOM   6535  C  CG1 . VAL F  1 145 ? 58.328  36.972  22.225  1.00 28.51 ? 118 VAL F CG1 1 
ATOM   6536  C  CG2 . VAL F  1 145 ? 57.725  38.698  20.516  1.00 27.00 ? 118 VAL F CG2 1 
ATOM   6537  N  N   . VAL F  1 146 ? 61.527  37.490  23.044  1.00 25.52 ? 119 VAL F N   1 
ATOM   6538  C  CA  . VAL F  1 146 ? 62.316  36.428  23.621  1.00 27.26 ? 119 VAL F CA  1 
ATOM   6539  C  C   . VAL F  1 146 ? 61.373  35.455  24.349  1.00 30.55 ? 119 VAL F C   1 
ATOM   6540  O  O   . VAL F  1 146 ? 60.440  35.855  25.081  1.00 27.36 ? 119 VAL F O   1 
ATOM   6541  C  CB  . VAL F  1 146 ? 63.548  36.962  24.418  1.00 27.95 ? 119 VAL F CB  1 
ATOM   6542  C  CG1 . VAL F  1 146 ? 63.145  37.767  25.638  1.00 26.39 ? 119 VAL F CG1 1 
ATOM   6543  C  CG2 . VAL F  1 146 ? 64.486  35.818  24.821  1.00 30.47 ? 119 VAL F CG2 1 
ATOM   6544  N  N   . HIS F  1 147 ? 61.578  34.159  24.087  1.00 31.00 ? 120 HIS F N   1 
ATOM   6545  C  CA  . HIS F  1 147 ? 60.590  33.140  24.486  1.00 31.60 ? 120 HIS F CA  1 
ATOM   6546  C  C   . HIS F  1 147 ? 61.051  32.319  25.730  1.00 29.43 ? 120 HIS F C   1 
ATOM   6547  O  O   . HIS F  1 147 ? 62.238  32.338  26.106  1.00 30.45 ? 120 HIS F O   1 
ATOM   6548  C  CB  . HIS F  1 147 ? 60.253  32.190  23.315  1.00 31.54 ? 120 HIS F CB  1 
ATOM   6549  C  CG  . HIS F  1 147 ? 59.306  32.767  22.311  1.00 31.18 ? 120 HIS F CG  1 
ATOM   6550  N  ND1 . HIS F  1 147 ? 57.959  32.508  22.342  1.00 29.12 ? 120 HIS F ND1 1 
ATOM   6551  C  CD2 . HIS F  1 147 ? 59.512  33.579  21.244  1.00 30.86 ? 120 HIS F CD2 1 
ATOM   6552  C  CE1 . HIS F  1 147 ? 57.364  33.139  21.339  1.00 31.24 ? 120 HIS F CE1 1 
ATOM   6553  N  NE2 . HIS F  1 147 ? 58.283  33.811  20.671  1.00 27.57 ? 120 HIS F NE2 1 
ATOM   6554  N  N   . GLU F  1 148 ? 60.095  31.600  26.313  1.00 33.13 ? 121 GLU F N   1 
ATOM   6555  C  CA  . GLU F  1 148 ? 60.306  30.871  27.596  1.00 38.13 ? 121 GLU F CA  1 
ATOM   6556  C  C   . GLU F  1 148 ? 61.324  29.708  27.491  1.00 38.67 ? 121 GLU F C   1 
ATOM   6557  O  O   . GLU F  1 148 ? 62.221  29.571  28.344  1.00 38.88 ? 121 GLU F O   1 
ATOM   6558  C  CB  . GLU F  1 148 ? 58.950  30.393  28.071  1.00 42.52 ? 121 GLU F CB  1 
ATOM   6559  C  CG  . GLU F  1 148 ? 58.935  29.295  29.116  1.00 52.06 ? 121 GLU F CG  1 
ATOM   6560  C  CD  . GLU F  1 148 ? 57.522  28.763  29.336  1.00 52.98 ? 121 GLU F CD  1 
ATOM   6561  O  OE1 . GLU F  1 148 ? 56.709  28.656  28.372  1.00 50.07 ? 121 GLU F OE1 1 
ATOM   6562  O  OE2 . GLU F  1 148 ? 57.211  28.453  30.501  1.00 65.91 ? 121 GLU F OE2 1 
ATOM   6563  N  N   . LYS F  1 149 ? 61.226  28.944  26.398  1.00 36.94 ? 122 LYS F N   1 
ATOM   6564  C  CA  . LYS F  1 149 ? 62.024  27.723  26.167  1.00 43.04 ? 122 LYS F CA  1 
ATOM   6565  C  C   . LYS F  1 149 ? 62.802  27.812  24.869  1.00 45.25 ? 122 LYS F C   1 
ATOM   6566  O  O   . LYS F  1 149 ? 62.561  28.715  24.030  1.00 36.98 ? 122 LYS F O   1 
ATOM   6567  C  CB  . LYS F  1 149 ? 61.105  26.528  26.003  1.00 44.08 ? 122 LYS F CB  1 
ATOM   6568  C  CG  . LYS F  1 149 ? 60.058  26.352  27.083  1.00 49.99 ? 122 LYS F CG  1 
ATOM   6569  C  CD  . LYS F  1 149 ? 58.930  25.488  26.546  1.00 53.89 ? 122 LYS F CD  1 
ATOM   6570  C  CE  . LYS F  1 149 ? 57.760  25.521  27.511  1.00 57.35 ? 122 LYS F CE  1 
ATOM   6571  N  NZ  . LYS F  1 149 ? 56.543  25.032  26.805  1.00 64.67 ? 122 LYS F NZ  1 
ATOM   6572  N  N   . ALA F  1 150 ? 63.709  26.854  24.691  1.00 38.77 ? 123 ALA F N   1 
ATOM   6573  C  CA  . ALA F  1 150 ? 64.395  26.647  23.403  1.00 36.32 ? 123 ALA F CA  1 
ATOM   6574  C  C   . ALA F  1 150 ? 63.437  26.528  22.200  1.00 37.59 ? 123 ALA F C   1 
ATOM   6575  O  O   . ALA F  1 150 ? 62.330  25.973  22.288  1.00 34.51 ? 123 ALA F O   1 
ATOM   6576  C  CB  . ALA F  1 150 ? 65.317  25.434  23.489  1.00 39.31 ? 123 ALA F CB  1 
ATOM   6577  N  N   . ASP F  1 151 ? 63.864  27.124  21.083  1.00 40.21 ? 124 ASP F N   1 
ATOM   6578  C  CA  . ASP F  1 151 ? 63.209  26.948  19.796  1.00 39.32 ? 124 ASP F CA  1 
ATOM   6579  C  C   . ASP F  1 151 ? 63.789  25.649  19.214  1.00 39.26 ? 124 ASP F C   1 
ATOM   6580  O  O   . ASP F  1 151 ? 65.017  25.571  19.022  1.00 38.84 ? 124 ASP F O   1 
ATOM   6581  C  CB  . ASP F  1 151 ? 63.619  28.109  18.887  1.00 40.47 ? 124 ASP F CB  1 
ATOM   6582  C  CG  . ASP F  1 151 ? 63.000  28.044  17.489  1.00 46.01 ? 124 ASP F CG  1 
ATOM   6583  O  OD1 . ASP F  1 151 ? 62.259  27.069  17.156  1.00 43.78 ? 124 ASP F OD1 1 
ATOM   6584  O  OD2 . ASP F  1 151 ? 63.253  29.012  16.718  1.00 49.86 ? 124 ASP F OD2 1 
ATOM   6585  N  N   . ASP F  1 152 ? 62.923  24.685  18.876  1.00 37.92 ? 125 ASP F N   1 
ATOM   6586  C  CA  . ASP F  1 152 ? 63.384  23.363  18.326  1.00 44.62 ? 125 ASP F CA  1 
ATOM   6587  C  C   . ASP F  1 152 ? 63.699  23.395  16.810  1.00 49.54 ? 125 ASP F C   1 
ATOM   6588  O  O   . ASP F  1 152 ? 63.848  22.340  16.130  1.00 42.22 ? 125 ASP F O   1 
ATOM   6589  C  CB  . ASP F  1 152 ? 62.376  22.255  18.659  1.00 41.72 ? 125 ASP F CB  1 
ATOM   6590  C  CG  . ASP F  1 152 ? 61.052  22.413  17.925  1.00 46.73 ? 125 ASP F CG  1 
ATOM   6591  O  OD1 . ASP F  1 152 ? 60.973  23.128  16.887  1.00 46.21 ? 125 ASP F OD1 1 
ATOM   6592  O  OD2 . ASP F  1 152 ? 60.069  21.795  18.389  1.00 47.96 ? 125 ASP F OD2 1 
ATOM   6593  N  N   . LEU F  1 153 ? 63.756  24.624  16.289  1.00 46.14 ? 126 LEU F N   1 
ATOM   6594  C  CA  . LEU F  1 153 ? 64.119  24.914  14.897  1.00 43.00 ? 126 LEU F CA  1 
ATOM   6595  C  C   . LEU F  1 153 ? 63.217  24.243  13.852  1.00 44.93 ? 126 LEU F C   1 
ATOM   6596  O  O   . LEU F  1 153 ? 63.645  24.003  12.711  1.00 48.33 ? 126 LEU F O   1 
ATOM   6597  C  CB  . LEU F  1 153 ? 65.629  24.712  14.641  1.00 42.49 ? 126 LEU F CB  1 
ATOM   6598  C  CG  . LEU F  1 153 ? 66.614  25.369  15.644  1.00 45.84 ? 126 LEU F CG  1 
ATOM   6599  C  CD1 . LEU F  1 153 ? 68.084  25.089  15.314  1.00 46.10 ? 126 LEU F CD1 1 
ATOM   6600  C  CD2 . LEU F  1 153 ? 66.386  26.872  15.847  1.00 42.37 ? 126 LEU F CD2 1 
ATOM   6601  N  N   . GLY F  1 154 ? 61.970  23.971  14.255  1.00 44.14 ? 127 GLY F N   1 
ATOM   6602  C  CA  . GLY F  1 154 ? 60.922  23.407  13.388  1.00 46.25 ? 127 GLY F CA  1 
ATOM   6603  C  C   . GLY F  1 154 ? 61.085  21.911  13.133  1.00 55.16 ? 127 GLY F C   1 
ATOM   6604  O  O   . GLY F  1 154 ? 60.437  21.357  12.232  1.00 57.24 ? 127 GLY F O   1 
ATOM   6605  N  N   . LYS F  1 155 ? 61.954  21.273  13.923  1.00 54.67 ? 128 LYS F N   1 
ATOM   6606  C  CA  . LYS F  1 155 ? 62.313  19.863  13.764  1.00 58.58 ? 128 LYS F CA  1 
ATOM   6607  C  C   . LYS F  1 155 ? 61.853  19.049  14.973  1.00 57.32 ? 128 LYS F C   1 
ATOM   6608  O  O   . LYS F  1 155 ? 62.468  18.040  15.293  1.00 61.39 ? 128 LYS F O   1 
ATOM   6609  C  CB  . LYS F  1 155 ? 63.833  19.689  13.638  1.00 59.99 ? 128 LYS F CB  1 
ATOM   6610  C  CG  . LYS F  1 155 ? 64.555  20.608  12.668  1.00 64.40 ? 128 LYS F CG  1 
ATOM   6611  C  CD  . LYS F  1 155 ? 64.711  20.052  11.254  1.00 63.37 ? 128 LYS F CD  1 
ATOM   6612  C  CE  . LYS F  1 155 ? 66.096  20.418  10.725  1.00 66.42 ? 128 LYS F CE  1 
ATOM   6613  N  NZ  . LYS F  1 155 ? 66.059  21.128  9.413   1.00 70.02 ? 128 LYS F NZ  1 
ATOM   6614  N  N   . GLY F  1 156 ? 60.795  19.488  15.655  1.00 52.97 ? 129 GLY F N   1 
ATOM   6615  C  CA  . GLY F  1 156 ? 60.265  18.751  16.810  1.00 53.93 ? 129 GLY F CA  1 
ATOM   6616  C  C   . GLY F  1 156 ? 59.223  17.694  16.452  1.00 52.13 ? 129 GLY F C   1 
ATOM   6617  O  O   . GLY F  1 156 ? 58.690  17.011  17.341  1.00 52.61 ? 129 GLY F O   1 
ATOM   6618  N  N   . GLY F  1 157 ? 58.900  17.588  15.163  1.00 54.57 ? 130 GLY F N   1 
ATOM   6619  C  CA  . GLY F  1 157 ? 58.000  16.550  14.641  1.00 57.04 ? 130 GLY F CA  1 
ATOM   6620  C  C   . GLY F  1 157 ? 56.526  16.562  15.036  1.00 60.07 ? 130 GLY F C   1 
ATOM   6621  O  O   . GLY F  1 157 ? 55.840  15.543  14.908  1.00 59.93 ? 130 GLY F O   1 
ATOM   6622  N  N   . ASN F  1 158 ? 56.027  17.694  15.527  1.00 57.20 ? 131 ASN F N   1 
ATOM   6623  C  CA  . ASN F  1 158 ? 54.573  17.892  15.696  1.00 55.91 ? 131 ASN F CA  1 
ATOM   6624  C  C   . ASN F  1 158 ? 54.150  19.183  14.968  1.00 62.84 ? 131 ASN F C   1 
ATOM   6625  O  O   . ASN F  1 158 ? 55.007  19.920  14.424  1.00 60.23 ? 131 ASN F O   1 
ATOM   6626  C  CB  . ASN F  1 158 ? 54.187  17.943  17.179  1.00 55.49 ? 131 ASN F CB  1 
ATOM   6627  C  CG  . ASN F  1 158 ? 55.132  18.829  17.995  1.00 61.15 ? 131 ASN F CG  1 
ATOM   6628  O  OD1 . ASN F  1 158 ? 55.263  20.042  17.739  1.00 56.81 ? 131 ASN F OD1 1 
ATOM   6629  N  ND2 . ASN F  1 158 ? 55.820  18.221  18.966  1.00 56.79 ? 131 ASN F ND2 1 
ATOM   6630  N  N   . GLU F  1 159 ? 52.848  19.468  14.962  1.00 58.27 ? 132 GLU F N   1 
ATOM   6631  C  CA  . GLU F  1 159 ? 52.336  20.633  14.240  1.00 63.81 ? 132 GLU F CA  1 
ATOM   6632  C  C   . GLU F  1 159 ? 52.849  21.966  14.838  1.00 60.75 ? 132 GLU F C   1 
ATOM   6633  O  O   . GLU F  1 159 ? 53.371  22.831  14.106  1.00 55.65 ? 132 GLU F O   1 
ATOM   6634  C  CB  . GLU F  1 159 ? 50.820  20.594  14.199  1.00 65.84 ? 132 GLU F CB  1 
ATOM   6635  C  CG  . GLU F  1 159 ? 50.273  21.184  12.925  1.00 77.99 ? 132 GLU F CG  1 
ATOM   6636  C  CD  . GLU F  1 159 ? 49.209  22.212  13.214  1.00 93.18 ? 132 GLU F CD  1 
ATOM   6637  O  OE1 . GLU F  1 159 ? 48.080  21.807  13.588  1.00 89.82 ? 132 GLU F OE1 1 
ATOM   6638  O  OE2 . GLU F  1 159 ? 49.513  23.425  13.083  1.00 95.67 ? 132 GLU F OE2 1 
ATOM   6639  N  N   . GLU F  1 160 ? 52.720  22.093  16.164  1.00 58.68 ? 133 GLU F N   1 
ATOM   6640  C  CA  . GLU F  1 160 ? 53.261  23.206  16.953  1.00 59.03 ? 133 GLU F CA  1 
ATOM   6641  C  C   . GLU F  1 160 ? 54.743  23.524  16.612  1.00 56.71 ? 133 GLU F C   1 
ATOM   6642  O  O   . GLU F  1 160 ? 55.166  24.719  16.579  1.00 47.98 ? 133 GLU F O   1 
ATOM   6643  C  CB  . GLU F  1 160 ? 53.090  22.905  18.461  1.00 62.01 ? 133 GLU F CB  1 
ATOM   6644  C  CG  . GLU F  1 160 ? 53.329  24.100  19.385  1.00 64.82 ? 133 GLU F CG  1 
ATOM   6645  C  CD  . GLU F  1 160 ? 52.394  25.270  19.096  1.00 67.46 ? 133 GLU F CD  1 
ATOM   6646  O  OE1 . GLU F  1 160 ? 51.152  25.081  19.146  1.00 65.56 ? 133 GLU F OE1 1 
ATOM   6647  O  OE2 . GLU F  1 160 ? 52.901  26.384  18.818  1.00 63.75 ? 133 GLU F OE2 1 
ATOM   6648  N  N   . SER F  1 161 ? 55.526  22.478  16.334  1.00 46.09 ? 134 SER F N   1 
ATOM   6649  C  CA  . SER F  1 161 ? 56.916  22.704  15.914  1.00 46.95 ? 134 SER F CA  1 
ATOM   6650  C  C   . SER F  1 161 ? 57.012  23.525  14.603  1.00 48.61 ? 134 SER F C   1 
ATOM   6651  O  O   . SER F  1 161 ? 57.934  24.348  14.471  1.00 43.96 ? 134 SER F O   1 
ATOM   6652  C  CB  . SER F  1 161 ? 57.717  21.400  15.792  1.00 48.28 ? 134 SER F CB  1 
ATOM   6653  O  OG  . SER F  1 161 ? 59.091  21.714  15.569  1.00 49.82 ? 134 SER F OG  1 
ATOM   6654  N  N   . THR F  1 162 ? 56.049  23.303  13.680  1.00 46.63 ? 135 THR F N   1 
ATOM   6655  C  CA  . THR F  1 162 ? 56.013  23.907  12.326  1.00 52.44 ? 135 THR F CA  1 
ATOM   6656  C  C   . THR F  1 162 ? 55.488  25.357  12.337  1.00 51.16 ? 135 THR F C   1 
ATOM   6657  O  O   . THR F  1 162 ? 55.561  26.051  11.321  1.00 45.45 ? 135 THR F O   1 
ATOM   6658  C  CB  . THR F  1 162 ? 55.160  23.080  11.302  1.00 48.70 ? 135 THR F CB  1 
ATOM   6659  O  OG1 . THR F  1 162 ? 53.757  23.203  11.606  1.00 50.11 ? 135 THR F OG1 1 
ATOM   6660  C  CG2 . THR F  1 162 ? 55.562  21.587  11.277  1.00 49.04 ? 135 THR F CG2 1 
ATOM   6661  N  N   . LYS F  1 163 ? 54.959  25.787  13.486  1.00 48.30 ? 136 LYS F N   1 
ATOM   6662  C  CA  . LYS F  1 163 ? 54.400  27.146  13.658  1.00 50.49 ? 136 LYS F CA  1 
ATOM   6663  C  C   . LYS F  1 163 ? 55.295  28.001  14.550  1.00 48.70 ? 136 LYS F C   1 
ATOM   6664  O  O   . LYS F  1 163 ? 55.633  29.127  14.189  1.00 45.75 ? 136 LYS F O   1 
ATOM   6665  C  CB  . LYS F  1 163 ? 52.986  27.094  14.249  1.00 48.35 ? 136 LYS F CB  1 
ATOM   6666  C  CG  . LYS F  1 163 ? 52.122  25.994  13.650  1.00 51.62 ? 136 LYS F CG  1 
ATOM   6667  C  CD  . LYS F  1 163 ? 50.713  26.479  13.379  1.00 58.98 ? 136 LYS F CD  1 
ATOM   6668  C  CE  . LYS F  1 163 ? 50.738  27.403  12.171  1.00 63.31 ? 136 LYS F CE  1 
ATOM   6669  N  NZ  . LYS F  1 163 ? 49.403  27.970  11.834  1.00 67.91 ? 136 LYS F NZ  1 
ATOM   6670  N  N   . THR F  1 164 ? 55.706  27.440  15.692  1.00 45.61 ? 137 THR F N   1 
ATOM   6671  C  CA  . THR F  1 164 ? 56.376  28.195  16.745  1.00 46.73 ? 137 THR F CA  1 
ATOM   6672  C  C   . THR F  1 164 ? 57.739  27.641  17.198  1.00 47.78 ? 137 THR F C   1 
ATOM   6673  O  O   . THR F  1 164 ? 58.435  28.284  18.016  1.00 40.84 ? 137 THR F O   1 
ATOM   6674  C  CB  . THR F  1 164 ? 55.464  28.296  17.991  1.00 52.04 ? 137 THR F CB  1 
ATOM   6675  O  OG1 . THR F  1 164 ? 55.349  26.998  18.598  1.00 55.40 ? 137 THR F OG1 1 
ATOM   6676  C  CG2 . THR F  1 164 ? 54.046  28.862  17.627  1.00 46.39 ? 137 THR F CG2 1 
ATOM   6677  N  N   . GLY F  1 165 ? 58.118  26.450  16.703  1.00 44.81 ? 138 GLY F N   1 
ATOM   6678  C  CA  . GLY F  1 165 ? 59.346  25.779  17.176  1.00 44.02 ? 138 GLY F CA  1 
ATOM   6679  C  C   . GLY F  1 165 ? 59.276  25.341  18.641  1.00 43.21 ? 138 GLY F C   1 
ATOM   6680  O  O   . GLY F  1 165 ? 60.319  25.105  19.277  1.00 43.47 ? 138 GLY F O   1 
ATOM   6681  N  N   . ASN F  1 166 ? 58.035  25.219  19.136  1.00 39.41 ? 139 ASN F N   1 
ATOM   6682  C  CA  . ASN F  1 166 ? 57.726  24.903  20.545  1.00 44.43 ? 139 ASN F CA  1 
ATOM   6683  C  C   . ASN F  1 166 ? 58.353  25.790  21.636  1.00 44.83 ? 139 ASN F C   1 
ATOM   6684  O  O   . ASN F  1 166 ? 58.503  25.343  22.782  1.00 42.76 ? 139 ASN F O   1 
ATOM   6685  C  CB  . ASN F  1 166 ? 58.056  23.427  20.827  1.00 43.40 ? 139 ASN F CB  1 
ATOM   6686  C  CG  . ASN F  1 166 ? 57.013  22.508  20.280  1.00 45.73 ? 139 ASN F CG  1 
ATOM   6687  O  OD1 . ASN F  1 166 ? 55.851  22.603  20.654  1.00 43.39 ? 139 ASN F OD1 1 
ATOM   6688  N  ND2 . ASN F  1 166 ? 57.413  21.620  19.375  1.00 50.28 ? 139 ASN F ND2 1 
ATOM   6689  N  N   . ALA F  1 167 ? 58.705  27.040  21.307  1.00 41.05 ? 140 ALA F N   1 
ATOM   6690  C  CA  . ALA F  1 167 ? 59.440  27.899  22.261  1.00 37.46 ? 140 ALA F CA  1 
ATOM   6691  C  C   . ALA F  1 167 ? 58.577  28.422  23.442  1.00 37.04 ? 140 ALA F C   1 
ATOM   6692  O  O   . ALA F  1 167 ? 59.103  29.041  24.361  1.00 39.13 ? 140 ALA F O   1 
ATOM   6693  C  CB  . ALA F  1 167 ? 60.147  29.041  21.518  1.00 40.83 ? 140 ALA F CB  1 
ATOM   6694  N  N   . GLY F  1 168 ? 57.260  28.201  23.411  1.00 33.92 ? 141 GLY F N   1 
ATOM   6695  C  CA  . GLY F  1 168 ? 56.437  28.538  24.574  1.00 38.07 ? 141 GLY F CA  1 
ATOM   6696  C  C   . GLY F  1 168 ? 56.169  30.029  24.784  1.00 42.97 ? 141 GLY F C   1 
ATOM   6697  O  O   . GLY F  1 168 ? 56.239  30.827  23.822  1.00 41.35 ? 141 GLY F O   1 
ATOM   6698  N  N   A SER F  1 169 ? 55.864  30.404  26.026  0.50 39.09 ? 142 SER F N   1 
ATOM   6699  N  N   B SER F  1 169 ? 55.924  30.405  26.039  0.50 40.08 ? 142 SER F N   1 
ATOM   6700  C  CA  A SER F  1 169 ? 55.358  31.742  26.342  0.50 37.63 ? 142 SER F CA  1 
ATOM   6701  C  CA  B SER F  1 169 ? 55.407  31.730  26.379  0.50 39.48 ? 142 SER F CA  1 
ATOM   6702  C  C   A SER F  1 169 ? 56.332  32.882  26.019  0.50 33.58 ? 142 SER F C   1 
ATOM   6703  C  C   B SER F  1 169 ? 56.358  32.893  26.065  0.50 34.52 ? 142 SER F C   1 
ATOM   6704  O  O   A SER F  1 169 ? 57.541  32.690  25.846  0.50 35.13 ? 142 SER F O   1 
ATOM   6705  O  O   B SER F  1 169 ? 57.577  32.723  25.926  0.50 35.38 ? 142 SER F O   1 
ATOM   6706  C  CB  A SER F  1 169 ? 54.956  31.813  27.818  0.50 37.67 ? 142 SER F CB  1 
ATOM   6707  C  CB  B SER F  1 169 ? 54.994  31.760  27.855  0.50 40.81 ? 142 SER F CB  1 
ATOM   6708  O  OG  A SER F  1 169 ? 56.098  32.005  28.621  0.50 33.71 ? 142 SER F OG  1 
ATOM   6709  O  OG  B SER F  1 169 ? 53.692  32.301  27.976  0.50 41.33 ? 142 SER F OG  1 
ATOM   6710  N  N   . ARG F  1 170 ? 55.793  34.090  25.969  1.00 37.24 ? 143 ARG F N   1 
ATOM   6711  C  CA  . ARG F  1 170 ? 56.591  35.254  25.611  1.00 31.11 ? 143 ARG F CA  1 
ATOM   6712  C  C   . ARG F  1 170 ? 57.049  35.961  26.861  1.00 29.57 ? 143 ARG F C   1 
ATOM   6713  O  O   . ARG F  1 170 ? 56.234  36.519  27.587  1.00 33.08 ? 143 ARG F O   1 
ATOM   6714  C  CB  . ARG F  1 170 ? 55.748  36.134  24.662  1.00 32.29 ? 143 ARG F CB  1 
ATOM   6715  C  CG  . ARG F  1 170 ? 55.033  35.259  23.628  1.00 33.94 ? 143 ARG F CG  1 
ATOM   6716  C  CD  . ARG F  1 170 ? 54.073  36.039  22.738  1.00 34.66 ? 143 ARG F CD  1 
ATOM   6717  N  NE  . ARG F  1 170 ? 53.632  35.177  21.639  1.00 35.57 ? 143 ARG F NE  1 
ATOM   6718  C  CZ  . ARG F  1 170 ? 53.041  35.588  20.518  1.00 37.33 ? 143 ARG F CZ  1 
ATOM   6719  N  NH1 . ARG F  1 170 ? 52.815  36.888  20.297  1.00 32.96 ? 143 ARG F NH1 1 
ATOM   6720  N  NH2 . ARG F  1 170 ? 52.682  34.680  19.603  1.00 33.28 ? 143 ARG F NH2 1 
ATOM   6721  N  N   . LEU F  1 171 ? 58.350  35.950  27.120  1.00 27.99 ? 144 LEU F N   1 
ATOM   6722  C  CA  . LEU F  1 171 ? 58.875  36.534  28.361  1.00 31.09 ? 144 LEU F CA  1 
ATOM   6723  C  C   . LEU F  1 171 ? 59.014  38.056  28.280  1.00 31.39 ? 144 LEU F C   1 
ATOM   6724  O  O   . LEU F  1 171 ? 58.759  38.765  29.258  1.00 25.37 ? 144 LEU F O   1 
ATOM   6725  C  CB  . LEU F  1 171 ? 60.249  35.958  28.711  1.00 31.96 ? 144 LEU F CB  1 
ATOM   6726  C  CG  . LEU F  1 171 ? 60.329  34.428  28.854  1.00 36.38 ? 144 LEU F CG  1 
ATOM   6727  C  CD1 . LEU F  1 171 ? 61.766  34.110  29.228  1.00 35.50 ? 144 LEU F CD1 1 
ATOM   6728  C  CD2 . LEU F  1 171 ? 59.288  33.931  29.847  1.00 36.46 ? 144 LEU F CD2 1 
ATOM   6729  N  N   . ALA F  1 172 ? 59.457  38.555  27.122  1.00 28.31 ? 145 ALA F N   1 
ATOM   6730  C  CA  . ALA F  1 172 ? 59.599  39.985  26.967  1.00 24.87 ? 145 ALA F CA  1 
ATOM   6731  C  C   . ALA F  1 172 ? 59.506  40.286  25.469  1.00 28.95 ? 145 ALA F C   1 
ATOM   6732  O  O   . ALA F  1 172 ? 59.608  39.359  24.614  1.00 26.24 ? 145 ALA F O   1 
ATOM   6733  C  CB  . ALA F  1 172 ? 60.924  40.469  27.514  1.00 24.16 ? 145 ALA F CB  1 
ATOM   6734  N  N   . CYS F  1 173 ? 59.267  41.559  25.157  1.00 23.16 ? 146 CYS F N   1 
ATOM   6735  C  CA  . CYS F  1 173 ? 59.139  41.956  23.734  1.00 22.66 ? 146 CYS F CA  1 
ATOM   6736  C  C   . CYS F  1 173 ? 59.273  43.471  23.612  1.00 24.58 ? 146 CYS F C   1 
ATOM   6737  O  O   . CYS F  1 173 ? 59.270  44.199  24.632  1.00 20.60 ? 146 CYS F O   1 
ATOM   6738  C  CB  . CYS F  1 173 ? 57.776  41.531  23.173  1.00 27.24 ? 146 CYS F CB  1 
ATOM   6739  S  SG  . CYS F  1 173 ? 56.334  42.196  24.024  1.00 34.40 ? 146 CYS F SG  1 
ATOM   6740  N  N   . GLY F  1 174 ? 59.407  43.960  22.373  1.00 20.65 ? 147 GLY F N   1 
ATOM   6741  C  CA  . GLY F  1 174 ? 59.457  45.422  22.184  1.00 21.97 ? 147 GLY F CA  1 
ATOM   6742  C  C   . GLY F  1 174 ? 59.245  45.645  20.693  1.00 24.91 ? 147 GLY F C   1 
ATOM   6743  O  O   . GLY F  1 174 ? 59.456  44.709  19.869  1.00 20.43 ? 147 GLY F O   1 
ATOM   6744  N  N   . VAL F  1 175 ? 58.809  46.864  20.337  1.00 20.37 ? 148 VAL F N   1 
ATOM   6745  C  CA  . VAL F  1 175 ? 58.654  47.185  18.933  1.00 18.29 ? 148 VAL F CA  1 
ATOM   6746  C  C   . VAL F  1 175 ? 60.033  47.584  18.411  1.00 18.48 ? 148 VAL F C   1 
ATOM   6747  O  O   . VAL F  1 175 ? 60.846  48.291  19.096  1.00 21.20 ? 148 VAL F O   1 
ATOM   6748  C  CB  . VAL F  1 175 ? 57.626  48.353  18.785  1.00 20.09 ? 148 VAL F CB  1 
ATOM   6749  C  CG1 . VAL F  1 175 ? 57.420  48.651  17.295  1.00 17.12 ? 148 VAL F CG1 1 
ATOM   6750  C  CG2 . VAL F  1 175 ? 56.299  47.926  19.404  1.00 17.97 ? 148 VAL F CG2 1 
ATOM   6751  N  N   . ILE F  1 176 ? 60.339  47.147  17.191  1.00 17.80 ? 149 ILE F N   1 
ATOM   6752  C  CA  . ILE F  1 176 ? 61.597  47.483  16.580  1.00 18.28 ? 149 ILE F CA  1 
ATOM   6753  C  C   . ILE F  1 176 ? 61.494  48.882  15.955  1.00 17.93 ? 149 ILE F C   1 
ATOM   6754  O  O   . ILE F  1 176 ? 60.698  49.080  15.060  1.00 21.43 ? 149 ILE F O   1 
ATOM   6755  C  CB  . ILE F  1 176 ? 62.010  46.409  15.483  1.00 19.47 ? 149 ILE F CB  1 
ATOM   6756  C  CG1 . ILE F  1 176 ? 62.117  44.985  16.137  1.00 20.18 ? 149 ILE F CG1 1 
ATOM   6757  C  CG2 . ILE F  1 176 ? 63.344  46.833  14.832  1.00 18.94 ? 149 ILE F CG2 1 
ATOM   6758  C  CD1 . ILE F  1 176 ? 61.935  43.801  15.169  1.00 21.58 ? 149 ILE F CD1 1 
ATOM   6759  N  N   . GLY F  1 177 ? 62.388  49.763  16.368  1.00 21.02 ? 150 GLY F N   1 
ATOM   6760  C  CA  . GLY F  1 177 ? 62.326  51.168  16.029  1.00 23.46 ? 150 GLY F CA  1 
ATOM   6761  C  C   . GLY F  1 177 ? 63.524  51.587  15.248  1.00 24.22 ? 150 GLY F C   1 
ATOM   6762  O  O   . GLY F  1 177 ? 64.629  50.989  15.368  1.00 19.25 ? 150 GLY F O   1 
ATOM   6763  N  N   . ILE F  1 178 ? 63.337  52.641  14.434  1.00 20.61 ? 151 ILE F N   1 
ATOM   6764  C  CA  . ILE F  1 178 ? 64.467  53.266  13.761  1.00 20.39 ? 151 ILE F CA  1 
ATOM   6765  C  C   . ILE F  1 178 ? 65.428  53.932  14.702  1.00 23.11 ? 151 ILE F C   1 
ATOM   6766  O  O   . ILE F  1 178 ? 65.019  54.656  15.637  1.00 22.48 ? 151 ILE F O   1 
ATOM   6767  C  CB  . ILE F  1 178 ? 63.952  54.287  12.699  1.00 25.08 ? 151 ILE F CB  1 
ATOM   6768  C  CG1 . ILE F  1 178 ? 62.979  53.562  11.744  1.00 27.46 ? 151 ILE F CG1 1 
ATOM   6769  C  CG2 . ILE F  1 178 ? 65.123  54.876  11.902  1.00 30.18 ? 151 ILE F CG2 1 
ATOM   6770  C  CD1 . ILE F  1 178 ? 62.181  54.462  10.783  1.00 30.89 ? 151 ILE F CD1 1 
ATOM   6771  N  N   . ALA F  1 179 ? 66.738  53.710  14.497  1.00 20.51 ? 152 ALA F N   1 
ATOM   6772  C  CA  . ALA F  1 179 ? 67.728  54.240  15.428  1.00 23.01 ? 152 ALA F CA  1 
ATOM   6773  C  C   . ALA F  1 179 ? 68.660  55.180  14.702  1.00 25.77 ? 152 ALA F C   1 
ATOM   6774  O  O   . ALA F  1 179 ? 68.732  55.161  13.476  1.00 26.26 ? 152 ALA F O   1 
ATOM   6775  C  CB  . ALA F  1 179 ? 68.554  53.094  16.070  1.00 24.29 ? 152 ALA F CB  1 
ATOM   6776  N  N   . GLN F  1 180 ? 69.375  55.993  15.463  1.00 28.91 ? 153 GLN F N   1 
ATOM   6777  C  CA  . GLN F  1 180 ? 70.310  56.961  14.898  1.00 36.26 ? 153 GLN F CA  1 
ATOM   6778  C  C   . GLN F  1 180 ? 71.610  56.259  14.517  1.00 47.61 ? 153 GLN F C   1 
ATOM   6779  O  O   . GLN F  1 180 ? 72.051  55.325  15.209  1.00 49.44 ? 153 GLN F O   1 
ATOM   6780  C  CB  . GLN F  1 180 ? 70.648  58.046  15.902  1.00 36.93 ? 153 GLN F CB  1 
ATOM   6781  C  CG  . GLN F  1 180 ? 71.456  59.180  15.290  1.00 41.39 ? 153 GLN F CG  1 
ATOM   6782  C  CD  . GLN F  1 180 ? 71.706  60.285  16.275  1.00 46.34 ? 153 GLN F CD  1 
ATOM   6783  O  OE1 . GLN F  1 180 ? 71.954  60.030  17.462  1.00 49.56 ? 153 GLN F OE1 1 
ATOM   6784  N  NE2 . GLN F  1 180 ? 71.654  61.521  15.800  1.00 48.55 ? 153 GLN F NE2 1 
ATOM   6785  O  OXT . GLN F  1 180 ? 72.254  56.631  13.532  1.00 52.70 ? 153 GLN F OXT 1 
ATOM   6786  N  N   . ALA G  1 28  ? 101.755 86.335  0.054   1.00 62.30 ? 1   ALA G N   1 
ATOM   6787  C  CA  . ALA G  1 28  ? 102.099 86.955  -1.269  1.00 61.61 ? 1   ALA G CA  1 
ATOM   6788  C  C   . ALA G  1 28  ? 103.227 87.985  -1.113  1.00 53.37 ? 1   ALA G C   1 
ATOM   6789  O  O   . ALA G  1 28  ? 103.048 89.048  -0.542  1.00 54.41 ? 1   ALA G O   1 
ATOM   6790  C  CB  . ALA G  1 28  ? 100.863 87.586  -1.922  1.00 58.47 ? 1   ALA G CB  1 
ATOM   6791  N  N   . THR G  1 29  ? 104.407 87.634  -1.584  1.00 47.62 ? 2   THR G N   1 
ATOM   6792  C  CA  . THR G  1 29  ? 105.496 88.584  -1.664  1.00 45.33 ? 2   THR G CA  1 
ATOM   6793  C  C   . THR G  1 29  ? 105.825 88.778  -3.145  1.00 41.20 ? 2   THR G C   1 
ATOM   6794  O  O   . THR G  1 29  ? 106.490 89.748  -3.500  1.00 37.18 ? 2   THR G O   1 
ATOM   6795  C  CB  . THR G  1 29  ? 106.754 88.086  -0.909  1.00 45.47 ? 2   THR G CB  1 
ATOM   6796  O  OG1 . THR G  1 29  ? 107.225 86.889  -1.533  1.00 47.52 ? 2   THR G OG1 1 
ATOM   6797  C  CG2 . THR G  1 29  ? 106.457 87.808  0.570   1.00 44.07 ? 2   THR G CG2 1 
ATOM   6798  N  N   . LYS G  1 30  ? 105.364 87.857  -4.009  1.00 35.40 ? 3   LYS G N   1 
ATOM   6799  C  CA  . LYS G  1 30  ? 105.531 87.991  -5.462  1.00 30.85 ? 3   LYS G CA  1 
ATOM   6800  C  C   . LYS G  1 30  ? 104.207 87.861  -6.234  1.00 34.33 ? 3   LYS G C   1 
ATOM   6801  O  O   . LYS G  1 30  ? 103.322 87.081  -5.828  1.00 32.00 ? 3   LYS G O   1 
ATOM   6802  C  CB  . LYS G  1 30  ? 106.529 86.993  -6.021  1.00 36.36 ? 3   LYS G CB  1 
ATOM   6803  C  CG  . LYS G  1 30  ? 107.977 87.183  -5.505  1.00 46.49 ? 3   LYS G CG  1 
ATOM   6804  C  CD  . LYS G  1 30  ? 109.027 86.382  -6.289  1.00 48.98 ? 3   LYS G CD  1 
ATOM   6805  C  CE  . LYS G  1 30  ? 109.077 86.719  -7.787  1.00 57.72 ? 3   LYS G CE  1 
ATOM   6806  N  NZ  . LYS G  1 30  ? 109.051 88.176  -8.171  1.00 65.66 ? 3   LYS G NZ  1 
ATOM   6807  N  N   . ALA G  1 31  ? 104.094 88.611  -7.340  1.00 32.27 ? 4   ALA G N   1 
ATOM   6808  C  CA  . ALA G  1 31  ? 102.949 88.494  -8.283  1.00 28.72 ? 4   ALA G CA  1 
ATOM   6809  C  C   . ALA G  1 31  ? 103.419 88.771  -9.668  1.00 31.08 ? 4   ALA G C   1 
ATOM   6810  O  O   . ALA G  1 31  ? 104.568 89.253  -9.886  1.00 31.28 ? 4   ALA G O   1 
ATOM   6811  C  CB  . ALA G  1 31  ? 101.818 89.431  -7.860  1.00 30.39 ? 4   ALA G CB  1 
ATOM   6812  N  N   . VAL G  1 32  ? 102.598 88.423  -10.650 1.00 26.76 ? 5   VAL G N   1 
ATOM   6813  C  CA  . VAL G  1 32  ? 102.973 88.557  -12.030 1.00 25.92 ? 5   VAL G CA  1 
ATOM   6814  C  C   . VAL G  1 32  ? 101.730 88.828  -12.894 1.00 30.28 ? 5   VAL G C   1 
ATOM   6815  O  O   . VAL G  1 32  ? 100.604 88.452  -12.514 1.00 30.67 ? 5   VAL G O   1 
ATOM   6816  C  CB  . VAL G  1 32  ? 103.728 87.305  -12.540 1.00 29.61 ? 5   VAL G CB  1 
ATOM   6817  C  CG1 . VAL G  1 32  ? 102.798 86.096  -12.661 1.00 30.84 ? 5   VAL G CG1 1 
ATOM   6818  C  CG2 . VAL G  1 32  ? 104.419 87.591  -13.864 1.00 27.41 ? 5   VAL G CG2 1 
ATOM   6819  N  N   . CYS G  1 33  ? 101.930 89.442  -14.044 1.00 28.16 ? 6   CYS G N   1 
ATOM   6820  C  CA  . CYS G  1 33  ? 100.826 89.799  -14.923 1.00 29.64 ? 6   CYS G CA  1 
ATOM   6821  C  C   . CYS G  1 33  ? 101.290 89.710  -16.339 1.00 30.61 ? 6   CYS G C   1 
ATOM   6822  O  O   . CYS G  1 33  ? 102.332 90.268  -16.688 1.00 31.32 ? 6   CYS G O   1 
ATOM   6823  C  CB  . CYS G  1 33  ? 100.326 91.229  -14.600 1.00 31.98 ? 6   CYS G CB  1 
ATOM   6824  S  SG  . CYS G  1 33  ? 98.989  91.782  -15.676 1.00 33.45 ? 6   CYS G SG  1 
ATOM   6825  N  N   . VAL G  1 34  ? 100.520 88.998  -17.163 1.00 27.53 ? 7   VAL G N   1 
ATOM   6826  C  CA  . VAL G  1 34  ? 100.763 88.895  -18.577 1.00 27.95 ? 7   VAL G CA  1 
ATOM   6827  C  C   . VAL G  1 34  ? 99.783  89.802  -19.289 1.00 33.07 ? 7   VAL G C   1 
ATOM   6828  O  O   . VAL G  1 34  ? 98.563  89.610  -19.181 1.00 30.13 ? 7   VAL G O   1 
ATOM   6829  C  CB  . VAL G  1 34  ? 100.594 87.414  -19.062 1.00 30.23 ? 7   VAL G CB  1 
ATOM   6830  C  CG1 . VAL G  1 34  ? 100.692 87.322  -20.572 1.00 29.58 ? 7   VAL G CG1 1 
ATOM   6831  C  CG2 . VAL G  1 34  ? 101.653 86.509  -18.436 1.00 29.71 ? 7   VAL G CG2 1 
ATOM   6832  N  N   . LEU G  1 35  ? 100.293 90.813  -19.991 1.00 30.55 ? 8   LEU G N   1 
ATOM   6833  C  CA  . LEU G  1 35  ? 99.426  91.794  -20.642 1.00 33.09 ? 8   LEU G CA  1 
ATOM   6834  C  C   . LEU G  1 35  ? 99.222  91.397  -22.089 1.00 32.91 ? 8   LEU G C   1 
ATOM   6835  O  O   . LEU G  1 35  ? 100.179 91.131  -22.780 1.00 34.42 ? 8   LEU G O   1 
ATOM   6836  C  CB  . LEU G  1 35  ? 100.034 93.217  -20.565 1.00 30.38 ? 8   LEU G CB  1 
ATOM   6837  C  CG  . LEU G  1 35  ? 100.224 93.746  -19.145 1.00 33.74 ? 8   LEU G CG  1 
ATOM   6838  C  CD1 . LEU G  1 35  ? 101.492 94.570  -19.118 1.00 43.53 ? 8   LEU G CD1 1 
ATOM   6839  C  CD2 . LEU G  1 35  ? 99.096  94.659  -18.767 1.00 35.62 ? 8   LEU G CD2 1 
ATOM   6840  N  N   . LYS G  1 36  ? 97.960  91.323  -22.534 1.00 32.64 ? 9   LYS G N   1 
ATOM   6841  C  CA  . LYS G  1 36  ? 97.639  91.133  -23.950 1.00 33.35 ? 9   LYS G CA  1 
ATOM   6842  C  C   . LYS G  1 36  ? 96.435  91.980  -24.280 1.00 32.57 ? 9   LYS G C   1 
ATOM   6843  O  O   . LYS G  1 36  ? 95.654  92.319  -23.405 1.00 30.10 ? 9   LYS G O   1 
ATOM   6844  C  CB  . LYS G  1 36  ? 97.218  89.688  -24.262 1.00 39.24 ? 9   LYS G CB  1 
ATOM   6845  C  CG  . LYS G  1 36  ? 97.954  88.601  -23.520 1.00 48.00 ? 9   LYS G CG  1 
ATOM   6846  C  CD  . LYS G  1 36  ? 97.232  87.260  -23.715 1.00 53.05 ? 9   LYS G CD  1 
ATOM   6847  C  CE  . LYS G  1 36  ? 98.057  86.086  -23.180 1.00 53.44 ? 9   LYS G CE  1 
ATOM   6848  N  NZ  . LYS G  1 36  ? 99.471  86.143  -23.679 1.00 54.66 ? 9   LYS G NZ  1 
ATOM   6849  N  N   . GLY G  1 37  ? 96.264  92.308  -25.550 1.00 34.14 ? 10  GLY G N   1 
ATOM   6850  C  CA  . GLY G  1 37  ? 95.067  93.040  -25.983 1.00 39.77 ? 10  GLY G CA  1 
ATOM   6851  C  C   . GLY G  1 37  ? 94.643  92.590  -27.379 1.00 43.90 ? 10  GLY G C   1 
ATOM   6852  O  O   . GLY G  1 37  ? 95.091  91.530  -27.863 1.00 40.90 ? 10  GLY G O   1 
ATOM   6853  N  N   . ASP G  1 38  ? 93.808  93.392  -28.036 1.00 42.59 ? 11  ASP G N   1 
ATOM   6854  C  CA  . ASP G  1 38  ? 93.438  93.135  -29.440 1.00 50.01 ? 11  ASP G CA  1 
ATOM   6855  C  C   . ASP G  1 38  ? 94.518  93.415  -30.464 1.00 52.56 ? 11  ASP G C   1 
ATOM   6856  O  O   . ASP G  1 38  ? 94.485  92.871  -31.565 1.00 59.99 ? 11  ASP G O   1 
ATOM   6857  C  CB  . ASP G  1 38  ? 92.219  93.949  -29.802 1.00 51.60 ? 11  ASP G CB  1 
ATOM   6858  C  CG  . ASP G  1 38  ? 91.069  93.624  -28.925 1.00 60.99 ? 11  ASP G CG  1 
ATOM   6859  O  OD1 . ASP G  1 38  ? 91.056  92.489  -28.372 1.00 60.97 ? 11  ASP G OD1 1 
ATOM   6860  O  OD2 . ASP G  1 38  ? 90.196  94.500  -28.771 1.00 69.13 ? 11  ASP G OD2 1 
ATOM   6861  N  N   . GLY G  1 39  ? 95.458  94.281  -30.125 1.00 46.27 ? 12  GLY G N   1 
ATOM   6862  C  CA  . GLY G  1 39  ? 96.455  94.714  -31.084 1.00 41.73 ? 12  GLY G CA  1 
ATOM   6863  C  C   . GLY G  1 39  ? 97.779  94.070  -30.802 1.00 43.30 ? 12  GLY G C   1 
ATOM   6864  O  O   . GLY G  1 39  ? 97.835  92.994  -30.188 1.00 44.47 ? 12  GLY G O   1 
ATOM   6865  N  N   . PRO G  1 40  ? 98.863  94.743  -31.214 1.00 42.37 ? 13  PRO G N   1 
ATOM   6866  C  CA  . PRO G  1 40  ? 100.208 94.199  -31.029 1.00 44.67 ? 13  PRO G CA  1 
ATOM   6867  C  C   . PRO G  1 40  ? 100.824 94.426  -29.636 1.00 43.83 ? 13  PRO G C   1 
ATOM   6868  O  O   . PRO G  1 40  ? 101.901 93.909  -29.373 1.00 46.11 ? 13  PRO G O   1 
ATOM   6869  C  CB  . PRO G  1 40  ? 101.016 94.935  -32.111 1.00 44.01 ? 13  PRO G CB  1 
ATOM   6870  C  CG  . PRO G  1 40  ? 100.357 96.282  -32.194 1.00 45.40 ? 13  PRO G CG  1 
ATOM   6871  C  CD  . PRO G  1 40  ? 98.879  96.036  -31.944 1.00 41.37 ? 13  PRO G CD  1 
ATOM   6872  N  N   . VAL G  1 41  ? 100.174 95.173  -28.743 1.00 39.49 ? 14  VAL G N   1 
ATOM   6873  C  CA  . VAL G  1 41  ? 100.754 95.353  -27.399 1.00 36.54 ? 14  VAL G CA  1 
ATOM   6874  C  C   . VAL G  1 41  ? 100.709 94.091  -26.501 1.00 38.56 ? 14  VAL G C   1 
ATOM   6875  O  O   . VAL G  1 41  ? 99.643  93.485  -26.297 1.00 36.03 ? 14  VAL G O   1 
ATOM   6876  C  CB  . VAL G  1 41  ? 100.105 96.518  -26.641 1.00 34.73 ? 14  VAL G CB  1 
ATOM   6877  C  CG1 . VAL G  1 41  ? 100.883 96.799  -25.350 1.00 32.92 ? 14  VAL G CG1 1 
ATOM   6878  C  CG2 . VAL G  1 41  ? 100.016 97.757  -27.514 1.00 37.76 ? 14  VAL G CG2 1 
ATOM   6879  N  N   . GLN G  1 42  ? 101.852 93.708  -25.943 1.00 32.35 ? 15  GLN G N   1 
ATOM   6880  C  CA  . GLN G  1 42  ? 101.906 92.609  -24.975 1.00 35.25 ? 15  GLN G CA  1 
ATOM   6881  C  C   . GLN G  1 42  ? 103.103 92.750  -24.091 1.00 38.36 ? 15  GLN G C   1 
ATOM   6882  O  O   . GLN G  1 42  ? 104.076 93.396  -24.460 1.00 40.33 ? 15  GLN G O   1 
ATOM   6883  C  CB  . GLN G  1 42  ? 101.977 91.272  -25.684 1.00 40.21 ? 15  GLN G CB  1 
ATOM   6884  C  CG  . GLN G  1 42  ? 102.855 91.299  -26.914 1.00 45.28 ? 15  GLN G CG  1 
ATOM   6885  C  CD  . GLN G  1 42  ? 103.066 89.915  -27.489 1.00 54.67 ? 15  GLN G CD  1 
ATOM   6886  O  OE1 . GLN G  1 42  ? 103.736 89.073  -26.895 1.00 60.14 ? 15  GLN G OE1 1 
ATOM   6887  N  NE2 . GLN G  1 42  ? 102.500 89.678  -28.651 1.00 54.41 ? 15  GLN G NE2 1 
ATOM   6888  N  N   . GLY G  1 43  ? 103.046 92.162  -22.913 1.00 34.94 ? 16  GLY G N   1 
ATOM   6889  C  CA  . GLY G  1 43  ? 104.186 92.211  -22.026 1.00 34.15 ? 16  GLY G CA  1 
ATOM   6890  C  C   . GLY G  1 43  ? 103.981 91.367  -20.806 1.00 37.36 ? 16  GLY G C   1 
ATOM   6891  O  O   . GLY G  1 43  ? 102.930 90.720  -20.652 1.00 33.05 ? 16  GLY G O   1 
ATOM   6892  N  N   . ILE G  1 44  ? 104.975 91.408  -19.916 1.00 31.70 ? 17  ILE G N   1 
ATOM   6893  C  CA  . ILE G  1 44  ? 104.960 90.689  -18.670 1.00 32.62 ? 17  ILE G CA  1 
ATOM   6894  C  C   . ILE G  1 44  ? 105.484 91.651  -17.624 1.00 33.64 ? 17  ILE G C   1 
ATOM   6895  O  O   . ILE G  1 44  ? 106.546 92.298  -17.822 1.00 34.54 ? 17  ILE G O   1 
ATOM   6896  C  CB  . ILE G  1 44  ? 105.866 89.416  -18.741 1.00 33.47 ? 17  ILE G CB  1 
ATOM   6897  C  CG1 . ILE G  1 44  ? 105.253 88.363  -19.657 1.00 35.41 ? 17  ILE G CG1 1 
ATOM   6898  C  CG2 . ILE G  1 44  ? 106.077 88.827  -17.373 1.00 32.85 ? 17  ILE G CG2 1 
ATOM   6899  C  CD1 . ILE G  1 44  ? 106.208 87.263  -20.115 1.00 39.18 ? 17  ILE G CD1 1 
ATOM   6900  N  N   . ILE G  1 45  ? 104.766 91.760  -16.523 1.00 27.83 ? 18  ILE G N   1 
ATOM   6901  C  CA  . ILE G  1 45  ? 105.146 92.665  -15.471 1.00 29.52 ? 18  ILE G CA  1 
ATOM   6902  C  C   . ILE G  1 45  ? 105.186 91.886  -14.174 1.00 30.13 ? 18  ILE G C   1 
ATOM   6903  O  O   . ILE G  1 45  ? 104.218 91.174  -13.791 1.00 31.25 ? 18  ILE G O   1 
ATOM   6904  C  CB  . ILE G  1 45  ? 104.168 93.884  -15.369 1.00 27.68 ? 18  ILE G CB  1 
ATOM   6905  C  CG1 . ILE G  1 45  ? 104.226 94.767  -16.636 1.00 31.90 ? 18  ILE G CG1 1 
ATOM   6906  C  CG2 . ILE G  1 45  ? 104.335 94.642  -14.054 1.00 28.39 ? 18  ILE G CG2 1 
ATOM   6907  C  CD1 . ILE G  1 45  ? 105.478 95.625  -16.803 1.00 33.31 ? 18  ILE G CD1 1 
ATOM   6908  N  N   . ASN G  1 46  ? 106.316 92.000  -13.473 1.00 27.85 ? 19  ASN G N   1 
ATOM   6909  C  CA  . ASN G  1 46  ? 106.463 91.448  -12.120 1.00 27.08 ? 19  ASN G CA  1 
ATOM   6910  C  C   . ASN G  1 46  ? 106.230 92.389  -10.982 1.00 28.62 ? 19  ASN G C   1 
ATOM   6911  O  O   . ASN G  1 46  ? 106.440 93.588  -11.137 1.00 30.61 ? 19  ASN G O   1 
ATOM   6912  C  CB  . ASN G  1 46  ? 107.861 90.812  -11.998 1.00 32.59 ? 19  ASN G CB  1 
ATOM   6913  C  CG  . ASN G  1 46  ? 108.255 90.082  -13.264 1.00 34.72 ? 19  ASN G CG  1 
ATOM   6914  O  OD1 . ASN G  1 46  ? 108.955 90.634  -14.144 1.00 39.20 ? 19  ASN G OD1 1 
ATOM   6915  N  ND2 . ASN G  1 46  ? 107.735 88.853  -13.420 1.00 32.39 ? 19  ASN G ND2 1 
ATOM   6916  N  N   . PHE G  1 47  ? 105.777 91.853  -9.843  1.00 27.09 ? 20  PHE G N   1 
ATOM   6917  C  CA  . PHE G  1 47  ? 105.623 92.567  -8.607  1.00 29.98 ? 20  PHE G CA  1 
ATOM   6918  C  C   . PHE G  1 47  ? 106.344 91.820  -7.499  1.00 35.57 ? 20  PHE G C   1 
ATOM   6919  O  O   . PHE G  1 47  ? 106.311 90.570  -7.422  1.00 36.31 ? 20  PHE G O   1 
ATOM   6920  C  CB  . PHE G  1 47  ? 104.151 92.707  -8.198  1.00 30.95 ? 20  PHE G CB  1 
ATOM   6921  C  CG  . PHE G  1 47  ? 103.287 93.321  -9.267  1.00 31.92 ? 20  PHE G CG  1 
ATOM   6922  C  CD1 . PHE G  1 47  ? 102.914 92.572  -10.390 1.00 33.21 ? 20  PHE G CD1 1 
ATOM   6923  C  CD2 . PHE G  1 47  ? 102.867 94.646  -9.159  1.00 31.91 ? 20  PHE G CD2 1 
ATOM   6924  C  CE1 . PHE G  1 47  ? 102.120 93.134  -11.388 1.00 34.81 ? 20  PHE G CE1 1 
ATOM   6925  C  CE2 . PHE G  1 47  ? 102.071 95.216  -10.159 1.00 32.11 ? 20  PHE G CE2 1 
ATOM   6926  C  CZ  . PHE G  1 47  ? 101.724 94.466  -11.274 1.00 31.02 ? 20  PHE G CZ  1 
ATOM   6927  N  N   . GLU G  1 48  ? 106.972 92.583  -6.620  1.00 32.96 ? 21  GLU G N   1 
ATOM   6928  C  CA  . GLU G  1 48  ? 107.606 91.988  -5.434  1.00 32.84 ? 21  GLU G CA  1 
ATOM   6929  C  C   . GLU G  1 48  ? 107.549 92.897  -4.251  1.00 35.35 ? 21  GLU G C   1 
ATOM   6930  O  O   . GLU G  1 48  ? 107.824 94.102  -4.369  1.00 38.33 ? 21  GLU G O   1 
ATOM   6931  C  CB  . GLU G  1 48  ? 109.037 91.586  -5.747  1.00 34.20 ? 21  GLU G CB  1 
ATOM   6932  C  CG  . GLU G  1 48  ? 109.699 90.940  -4.542  1.00 45.22 ? 21  GLU G CG  1 
ATOM   6933  C  CD  . GLU G  1 48  ? 111.154 90.639  -4.803  1.00 56.17 ? 21  GLU G CD  1 
ATOM   6934  O  OE1 . GLU G  1 48  ? 112.016 91.369  -4.254  1.00 61.97 ? 21  GLU G OE1 1 
ATOM   6935  O  OE2 . GLU G  1 48  ? 111.428 89.707  -5.590  1.00 60.05 ? 21  GLU G OE2 1 
ATOM   6936  N  N   . GLN G  1 49  ? 107.167 92.342  -3.113  1.00 34.18 ? 22  GLN G N   1 
ATOM   6937  C  CA  . GLN G  1 49  ? 106.997 93.094  -1.901  1.00 35.62 ? 22  GLN G CA  1 
ATOM   6938  C  C   . GLN G  1 49  ? 107.660 92.323  -0.762  1.00 44.98 ? 22  GLN G C   1 
ATOM   6939  O  O   . GLN G  1 49  ? 107.127 91.305  -0.306  1.00 41.27 ? 22  GLN G O   1 
ATOM   6940  C  CB  . GLN G  1 49  ? 105.522 93.312  -1.587  1.00 37.58 ? 22  GLN G CB  1 
ATOM   6941  C  CG  . GLN G  1 49  ? 105.270 94.389  -0.557  1.00 35.44 ? 22  GLN G CG  1 
ATOM   6942  C  CD  . GLN G  1 49  ? 103.815 94.495  -0.214  1.00 42.30 ? 22  GLN G CD  1 
ATOM   6943  O  OE1 . GLN G  1 49  ? 103.026 93.630  -0.597  1.00 42.94 ? 22  GLN G OE1 1 
ATOM   6944  N  NE2 . GLN G  1 49  ? 103.427 95.573  0.472   1.00 36.18 ? 22  GLN G NE2 1 
ATOM   6945  N  N   . LYS G  1 50  ? 108.811 92.829  -0.308  1.00 47.17 ? 23  LYS G N   1 
ATOM   6946  C  CA  . LYS G  1 50  ? 109.633 92.154  0.712   1.00 50.81 ? 23  LYS G CA  1 
ATOM   6947  C  C   . LYS G  1 50  ? 109.047 92.184  2.107   1.00 49.41 ? 23  LYS G C   1 
ATOM   6948  O  O   . LYS G  1 50  ? 109.087 91.182  2.802   1.00 51.06 ? 23  LYS G O   1 
ATOM   6949  C  CB  . LYS G  1 50  ? 111.061 92.726  0.735   1.00 57.86 ? 23  LYS G CB  1 
ATOM   6950  C  CG  . LYS G  1 50  ? 111.800 92.720  -0.602  1.00 59.05 ? 23  LYS G CG  1 
ATOM   6951  C  CD  . LYS G  1 50  ? 111.580 91.433  -1.411  1.00 64.93 ? 23  LYS G CD  1 
ATOM   6952  C  CE  . LYS G  1 50  ? 112.349 90.223  -0.890  1.00 67.51 ? 23  LYS G CE  1 
ATOM   6953  N  NZ  . LYS G  1 50  ? 113.803 90.510  -0.730  1.00 69.98 ? 23  LYS G NZ  1 
ATOM   6954  N  N   . GLU G  1 51  ? 108.525 93.325  2.540   1.00 48.72 ? 24  GLU G N   1 
ATOM   6955  C  CA  . GLU G  1 51  ? 107.885 93.405  3.845   1.00 52.39 ? 24  GLU G CA  1 
ATOM   6956  C  C   . GLU G  1 51  ? 106.427 93.776  3.621   1.00 56.71 ? 24  GLU G C   1 
ATOM   6957  O  O   . GLU G  1 51  ? 106.104 94.439  2.632   1.00 56.78 ? 24  GLU G O   1 
ATOM   6958  C  CB  . GLU G  1 51  ? 108.603 94.419  4.758   1.00 53.32 ? 24  GLU G CB  1 
ATOM   6959  N  N   . SER G  1 52  ? 105.537 93.340  4.510   1.00 55.92 ? 25  SER G N   1 
ATOM   6960  C  CA  . SER G  1 52  ? 104.112 93.559  4.299   1.00 56.37 ? 25  SER G CA  1 
ATOM   6961  C  C   . SER G  1 52  ? 103.714 95.050  4.406   1.00 61.15 ? 25  SER G C   1 
ATOM   6962  O  O   . SER G  1 52  ? 102.797 95.518  3.713   1.00 60.10 ? 25  SER G O   1 
ATOM   6963  C  CB  . SER G  1 52  ? 103.283 92.660  5.231   1.00 59.93 ? 25  SER G CB  1 
ATOM   6964  O  OG  . SER G  1 52  ? 102.903 93.319  6.431   1.00 59.14 ? 25  SER G OG  1 
ATOM   6965  N  N   . ASN G  1 53  ? 104.405 95.800  5.262   1.00 62.31 ? 26  ASN G N   1 
ATOM   6966  C  CA  . ASN G  1 53  ? 104.226 97.253  5.286   1.00 66.25 ? 26  ASN G CA  1 
ATOM   6967  C  C   . ASN G  1 53  ? 104.624 97.887  3.933   1.00 64.82 ? 26  ASN G C   1 
ATOM   6968  O  O   . ASN G  1 53  ? 103.973 98.819  3.452   1.00 65.20 ? 26  ASN G O   1 
ATOM   6969  C  CB  . ASN G  1 53  ? 105.046 97.879  6.434   1.00 65.83 ? 26  ASN G CB  1 
ATOM   6970  N  N   . GLY G  1 54  ? 105.642 97.306  3.297   1.00 58.65 ? 27  GLY G N   1 
ATOM   6971  C  CA  . GLY G  1 54  ? 106.565 98.055  2.448   1.00 52.17 ? 27  GLY G CA  1 
ATOM   6972  C  C   . GLY G  1 54  ? 106.249 98.293  0.994   1.00 48.74 ? 27  GLY G C   1 
ATOM   6973  O  O   . GLY G  1 54  ? 105.153 97.957  0.520   1.00 47.97 ? 27  GLY G O   1 
ATOM   6974  N  N   . PRO G  1 55  ? 107.223 98.890  0.277   1.00 43.79 ? 28  PRO G N   1 
ATOM   6975  C  CA  . PRO G  1 55  ? 107.125 99.258  -1.115  1.00 40.75 ? 28  PRO G CA  1 
ATOM   6976  C  C   . PRO G  1 55  ? 107.050 98.017  -2.000  1.00 39.20 ? 28  PRO G C   1 
ATOM   6977  O  O   . PRO G  1 55  ? 107.633 96.975  -1.683  1.00 37.71 ? 28  PRO G O   1 
ATOM   6978  C  CB  . PRO G  1 55  ? 108.454 100.007 -1.377  1.00 41.24 ? 28  PRO G CB  1 
ATOM   6979  C  CG  . PRO G  1 55  ? 108.998 100.330 -0.031  1.00 43.67 ? 28  PRO G CG  1 
ATOM   6980  C  CD  . PRO G  1 55  ? 108.570 99.175  0.808   1.00 43.39 ? 28  PRO G CD  1 
ATOM   6981  N  N   . VAL G  1 56  ? 106.345 98.143  -3.111  1.00 33.82 ? 29  VAL G N   1 
ATOM   6982  C  CA  . VAL G  1 56  ? 106.287 97.084  -4.093  1.00 30.10 ? 29  VAL G CA  1 
ATOM   6983  C  C   . VAL G  1 56  ? 107.135 97.491  -5.266  1.00 30.64 ? 29  VAL G C   1 
ATOM   6984  O  O   . VAL G  1 56  ? 106.965 98.587  -5.803  1.00 33.07 ? 29  VAL G O   1 
ATOM   6985  C  CB  . VAL G  1 56  ? 104.807 96.882  -4.543  1.00 32.60 ? 29  VAL G CB  1 
ATOM   6986  C  CG1 . VAL G  1 56  ? 104.694 95.802  -5.608  1.00 31.17 ? 29  VAL G CG1 1 
ATOM   6987  C  CG2 . VAL G  1 56  ? 103.926 96.591  -3.339  1.00 31.55 ? 29  VAL G CG2 1 
ATOM   6988  N  N   . LYS G  1 57  ? 108.063 96.640  -5.677  1.00 29.52 ? 30  LYS G N   1 
ATOM   6989  C  CA  . LYS G  1 57  ? 108.748 96.834  -6.931  1.00 31.14 ? 30  LYS G CA  1 
ATOM   6990  C  C   . LYS G  1 57  ? 107.957 96.266  -8.088  1.00 33.08 ? 30  LYS G C   1 
ATOM   6991  O  O   . LYS G  1 57  ? 107.478 95.125  -8.028  1.00 33.80 ? 30  LYS G O   1 
ATOM   6992  C  CB  . LYS G  1 57  ? 110.122 96.158  -6.918  1.00 37.09 ? 30  LYS G CB  1 
ATOM   6993  C  CG  . LYS G  1 57  ? 111.152 96.760  -5.951  1.00 45.46 ? 30  LYS G CG  1 
ATOM   6994  C  CD  . LYS G  1 57  ? 112.538 96.144  -6.224  1.00 56.09 ? 30  LYS G CD  1 
ATOM   6995  C  CE  . LYS G  1 57  ? 113.634 96.626  -5.271  1.00 58.66 ? 30  LYS G CE  1 
ATOM   6996  N  NZ  . LYS G  1 57  ? 113.199 96.626  -3.836  1.00 59.05 ? 30  LYS G NZ  1 
ATOM   6997  N  N   . VAL G  1 58  ? 107.874 97.032  -9.166  1.00 30.25 ? 31  VAL G N   1 
ATOM   6998  C  CA  . VAL G  1 58  ? 107.131 96.635  -10.364 1.00 31.31 ? 31  VAL G CA  1 
ATOM   6999  C  C   . VAL G  1 58  ? 108.042 96.752  -11.557 1.00 31.59 ? 31  VAL G C   1 
ATOM   7000  O  O   . VAL G  1 58  ? 108.520 97.848  -11.873 1.00 34.75 ? 31  VAL G O   1 
ATOM   7001  C  CB  . VAL G  1 58  ? 105.945 97.614  -10.601 1.00 29.88 ? 31  VAL G CB  1 
ATOM   7002  C  CG1 . VAL G  1 58  ? 105.158 97.199  -11.847 1.00 29.92 ? 31  VAL G CG1 1 
ATOM   7003  C  CG2 . VAL G  1 58  ? 105.093 97.767  -9.337  1.00 28.66 ? 31  VAL G CG2 1 
ATOM   7004  N  N   . TRP G  1 59  ? 108.292 95.658  -12.248 1.00 29.78 ? 32  TRP G N   1 
ATOM   7005  C  CA  . TRP G  1 59  ? 109.247 95.720  -13.358 1.00 31.13 ? 32  TRP G CA  1 
ATOM   7006  C  C   . TRP G  1 59  ? 108.929 94.703  -14.373 1.00 29.25 ? 32  TRP G C   1 
ATOM   7007  O  O   . TRP G  1 59  ? 108.383 93.643  -14.052 1.00 32.72 ? 32  TRP G O   1 
ATOM   7008  C  CB  . TRP G  1 59  ? 110.710 95.497  -12.875 1.00 32.93 ? 32  TRP G CB  1 
ATOM   7009  C  CG  . TRP G  1 59  ? 111.058 94.012  -12.626 1.00 34.54 ? 32  TRP G CG  1 
ATOM   7010  C  CD1 . TRP G  1 59  ? 111.675 93.122  -13.502 1.00 32.30 ? 32  TRP G CD1 1 
ATOM   7011  C  CD2 . TRP G  1 59  ? 110.801 93.286  -11.428 1.00 34.05 ? 32  TRP G CD2 1 
ATOM   7012  N  NE1 . TRP G  1 59  ? 111.811 91.896  -12.893 1.00 34.47 ? 32  TRP G NE1 1 
ATOM   7013  C  CE2 . TRP G  1 59  ? 111.289 91.964  -11.623 1.00 34.16 ? 32  TRP G CE2 1 
ATOM   7014  C  CE3 . TRP G  1 59  ? 110.208 93.621  -10.201 1.00 35.33 ? 32  TRP G CE3 1 
ATOM   7015  C  CZ2 . TRP G  1 59  ? 111.166 90.968  -10.646 1.00 36.79 ? 32  TRP G CZ2 1 
ATOM   7016  C  CZ3 . TRP G  1 59  ? 110.098 92.620  -9.204  1.00 40.82 ? 32  TRP G CZ3 1 
ATOM   7017  C  CH2 . TRP G  1 59  ? 110.588 91.309  -9.439  1.00 38.11 ? 32  TRP G CH2 1 
ATOM   7018  N  N   . GLY G  1 60  ? 109.309 94.979  -15.593 1.00 30.19 ? 33  GLY G N   1 
ATOM   7019  C  CA  . GLY G  1 60  ? 109.203 94.022  -16.628 1.00 31.22 ? 33  GLY G CA  1 
ATOM   7020  C  C   . GLY G  1 60  ? 109.312 94.780  -17.896 1.00 35.73 ? 33  GLY G C   1 
ATOM   7021  O  O   . GLY G  1 60  ? 109.909 95.853  -17.923 1.00 33.21 ? 33  GLY G O   1 
ATOM   7022  N  N   . SER G  1 61  ? 108.719 94.234  -18.947 1.00 35.29 ? 34  SER G N   1 
ATOM   7023  C  CA  . SER G  1 61  ? 108.796 94.787  -20.274 1.00 35.06 ? 34  SER G CA  1 
ATOM   7024  C  C   . SER G  1 61  ? 107.464 94.683  -21.076 1.00 40.56 ? 34  SER G C   1 
ATOM   7025  O  O   . SER G  1 61  ? 106.744 93.690  -20.961 1.00 42.29 ? 34  SER G O   1 
ATOM   7026  C  CB  . SER G  1 61  ? 109.910 94.039  -21.008 1.00 38.96 ? 34  SER G CB  1 
ATOM   7027  O  OG  . SER G  1 61  ? 110.073 94.596  -22.290 1.00 45.93 ? 34  SER G OG  1 
ATOM   7028  N  N   . ILE G  1 62  ? 107.162 95.687  -21.906 1.00 32.82 ? 35  ILE G N   1 
ATOM   7029  C  CA  . ILE G  1 62  ? 105.985 95.703  -22.758 1.00 33.42 ? 35  ILE G CA  1 
ATOM   7030  C  C   . ILE G  1 62  ? 106.400 96.089  -24.176 1.00 37.82 ? 35  ILE G C   1 
ATOM   7031  O  O   . ILE G  1 62  ? 107.137 97.066  -24.372 1.00 39.84 ? 35  ILE G O   1 
ATOM   7032  C  CB  . ILE G  1 62  ? 104.933 96.731  -22.237 1.00 32.45 ? 35  ILE G CB  1 
ATOM   7033  C  CG1 . ILE G  1 62  ? 104.616 96.479  -20.750 1.00 31.78 ? 35  ILE G CG1 1 
ATOM   7034  C  CG2 . ILE G  1 62  ? 103.669 96.697  -23.089 1.00 33.21 ? 35  ILE G CG2 1 
ATOM   7035  C  CD1 . ILE G  1 62  ? 103.819 97.575  -20.039 1.00 37.72 ? 35  ILE G CD1 1 
ATOM   7036  N  N   . LYS G  1 63  ? 105.946 95.346  -25.182 1.00 36.63 ? 36  LYS G N   1 
ATOM   7037  C  CA  . LYS G  1 63  ? 106.257 95.719  -26.570 1.00 35.99 ? 36  LYS G CA  1 
ATOM   7038  C  C   . LYS G  1 63  ? 105.051 96.043  -27.400 1.00 35.83 ? 36  LYS G C   1 
ATOM   7039  O  O   . LYS G  1 63  ? 103.906 95.878  -26.946 1.00 34.76 ? 36  LYS G O   1 
ATOM   7040  C  CB  . LYS G  1 63  ? 107.155 94.685  -27.275 1.00 44.24 ? 36  LYS G CB  1 
ATOM   7041  C  CG  . LYS G  1 63  ? 106.647 93.248  -27.356 1.00 51.23 ? 36  LYS G CG  1 
ATOM   7042  C  CD  . LYS G  1 63  ? 107.794 92.388  -27.899 1.00 57.54 ? 36  LYS G CD  1 
ATOM   7043  C  CE  . LYS G  1 63  ? 107.667 90.909  -27.561 1.00 63.93 ? 36  LYS G CE  1 
ATOM   7044  N  NZ  . LYS G  1 63  ? 106.741 90.234  -28.514 1.00 64.21 ? 36  LYS G NZ  1 
ATOM   7045  N  N   . GLY G  1 64  ? 105.310 96.530  -28.610 1.00 32.53 ? 37  GLY G N   1 
ATOM   7046  C  CA  . GLY G  1 64  ? 104.269 96.878  -29.552 1.00 35.79 ? 37  GLY G CA  1 
ATOM   7047  C  C   . GLY G  1 64  ? 103.691 98.280  -29.330 1.00 37.52 ? 37  GLY G C   1 
ATOM   7048  O  O   . GLY G  1 64  ? 102.712 98.637  -29.963 1.00 37.34 ? 37  GLY G O   1 
ATOM   7049  N  N   . LEU G  1 65  ? 104.296 99.066  -28.437 1.00 37.54 ? 38  LEU G N   1 
ATOM   7050  C  CA  . LEU G  1 65  ? 103.758 100.390 -28.080 1.00 39.63 ? 38  LEU G CA  1 
ATOM   7051  C  C   . LEU G  1 65  ? 104.253 101.495 -29.026 1.00 42.64 ? 38  LEU G C   1 
ATOM   7052  O  O   . LEU G  1 65  ? 105.359 101.393 -29.517 1.00 43.67 ? 38  LEU G O   1 
ATOM   7053  C  CB  . LEU G  1 65  ? 104.194 100.717 -26.649 1.00 35.61 ? 38  LEU G CB  1 
ATOM   7054  C  CG  . LEU G  1 65  ? 103.505 99.962  -25.511 1.00 33.08 ? 38  LEU G CG  1 
ATOM   7055  C  CD1 . LEU G  1 65  ? 104.331 100.144 -24.264 1.00 31.33 ? 38  LEU G CD1 1 
ATOM   7056  C  CD2 . LEU G  1 65  ? 102.059 100.445 -25.329 1.00 34.00 ? 38  LEU G CD2 1 
ATOM   7057  N  N   . THR G  1 66  ? 103.446 102.534 -29.272 1.00 43.48 ? 39  THR G N   1 
ATOM   7058  C  CA  . THR G  1 66  ? 103.958 103.787 -29.881 1.00 43.18 ? 39  THR G CA  1 
ATOM   7059  C  C   . THR G  1 66  ? 105.000 104.461 -28.955 1.00 45.29 ? 39  THR G C   1 
ATOM   7060  O  O   . THR G  1 66  ? 104.873 104.423 -27.715 1.00 44.23 ? 39  THR G O   1 
ATOM   7061  C  CB  . THR G  1 66  ? 102.824 104.797 -30.213 1.00 42.85 ? 39  THR G CB  1 
ATOM   7062  O  OG1 . THR G  1 66  ? 102.070 105.089 -29.035 1.00 42.60 ? 39  THR G OG1 1 
ATOM   7063  C  CG2 . THR G  1 66  ? 101.854 104.265 -31.255 1.00 40.91 ? 39  THR G CG2 1 
ATOM   7064  N  N   . GLU G  1 67  ? 106.044 105.065 -29.528 1.00 41.92 ? 40  GLU G N   1 
ATOM   7065  C  CA  . GLU G  1 67  ? 107.113 105.627 -28.695 1.00 39.62 ? 40  GLU G CA  1 
ATOM   7066  C  C   . GLU G  1 67  ? 106.547 106.763 -27.835 1.00 40.09 ? 40  GLU G C   1 
ATOM   7067  O  O   . GLU G  1 67  ? 105.686 107.512 -28.272 1.00 42.27 ? 40  GLU G O   1 
ATOM   7068  C  CB  . GLU G  1 67  ? 108.300 106.092 -29.560 1.00 47.29 ? 40  GLU G CB  1 
ATOM   7069  C  CG  . GLU G  1 67  ? 109.248 107.100 -28.910 1.00 47.74 ? 40  GLU G CG  1 
ATOM   7070  C  CD  . GLU G  1 67  ? 110.333 107.615 -29.864 1.00 56.71 ? 40  GLU G CD  1 
ATOM   7071  O  OE1 . GLU G  1 67  ? 110.041 107.867 -31.066 1.00 48.93 ? 40  GLU G OE1 1 
ATOM   7072  O  OE2 . GLU G  1 67  ? 111.486 107.776 -29.393 1.00 54.20 ? 40  GLU G OE2 1 
ATOM   7073  N  N   . GLY G  1 68  ? 107.000 106.866 -26.596 1.00 38.15 ? 41  GLY G N   1 
ATOM   7074  C  CA  . GLY G  1 68  ? 106.482 107.914 -25.730 1.00 38.78 ? 41  GLY G CA  1 
ATOM   7075  C  C   . GLY G  1 68  ? 105.814 107.387 -24.477 1.00 36.47 ? 41  GLY G C   1 
ATOM   7076  O  O   . GLY G  1 68  ? 106.057 106.232 -24.086 1.00 35.90 ? 41  GLY G O   1 
ATOM   7077  N  N   . LEU G  1 69  ? 105.009 108.240 -23.834 1.00 35.06 ? 42  LEU G N   1 
ATOM   7078  C  CA  . LEU G  1 69  ? 104.476 107.951 -22.496 1.00 35.00 ? 42  LEU G CA  1 
ATOM   7079  C  C   . LEU G  1 69  ? 103.125 107.225 -22.612 1.00 33.04 ? 42  LEU G C   1 
ATOM   7080  O  O   . LEU G  1 69  ? 102.316 107.573 -23.477 1.00 34.22 ? 42  LEU G O   1 
ATOM   7081  C  CB  . LEU G  1 69  ? 104.350 109.239 -21.660 1.00 34.53 ? 42  LEU G CB  1 
ATOM   7082  C  CG  . LEU G  1 69  ? 105.617 109.925 -21.102 1.00 39.25 ? 42  LEU G CG  1 
ATOM   7083  C  CD1 . LEU G  1 69  ? 105.264 111.245 -20.399 1.00 38.73 ? 42  LEU G CD1 1 
ATOM   7084  C  CD2 . LEU G  1 69  ? 106.366 109.015 -20.136 1.00 36.50 ? 42  LEU G CD2 1 
ATOM   7085  N  N   . HIS G  1 70  ? 102.890 106.239 -21.737 1.00 32.69 ? 43  HIS G N   1 
ATOM   7086  C  CA  . HIS G  1 70  ? 101.575 105.504 -21.691 1.00 28.91 ? 43  HIS G CA  1 
ATOM   7087  C  C   . HIS G  1 70  ? 101.111 105.347 -20.259 1.00 24.91 ? 43  HIS G C   1 
ATOM   7088  O  O   . HIS G  1 70  ? 101.860 104.882 -19.392 1.00 26.08 ? 43  HIS G O   1 
ATOM   7089  C  CB  . HIS G  1 70  ? 101.742 104.143 -22.377 1.00 29.31 ? 43  HIS G CB  1 
ATOM   7090  C  CG  . HIS G  1 70  ? 101.989 104.240 -23.856 1.00 31.44 ? 43  HIS G CG  1 
ATOM   7091  N  ND1 . HIS G  1 70  ? 100.966 104.291 -24.779 1.00 35.92 ? 43  HIS G ND1 1 
ATOM   7092  C  CD2 . HIS G  1 70  ? 103.140 104.279 -24.574 1.00 33.15 ? 43  HIS G CD2 1 
ATOM   7093  C  CE1 . HIS G  1 70  ? 101.470 104.375 -25.999 1.00 34.11 ? 43  HIS G CE1 1 
ATOM   7094  N  NE2 . HIS G  1 70  ? 102.787 104.378 -25.901 1.00 29.94 ? 43  HIS G NE2 1 
ATOM   7095  N  N   . GLY G  1 71  ? 99.867  105.754 -19.980 1.00 25.58 ? 44  GLY G N   1 
ATOM   7096  C  CA  . GLY G  1 71  ? 99.304  105.548 -18.661 1.00 24.29 ? 44  GLY G CA  1 
ATOM   7097  C  C   . GLY G  1 71  ? 99.393  104.073 -18.231 1.00 23.34 ? 44  GLY G C   1 
ATOM   7098  O  O   . GLY G  1 71  ? 99.313  103.179 -19.053 1.00 26.62 ? 44  GLY G O   1 
ATOM   7099  N  N   . PHE G  1 72  ? 99.510  103.830 -16.944 1.00 24.58 ? 45  PHE G N   1 
ATOM   7100  C  CA  . PHE G  1 72  ? 99.790  102.498 -16.462 1.00 26.26 ? 45  PHE G CA  1 
ATOM   7101  C  C   . PHE G  1 72  ? 99.126  102.416 -15.142 1.00 25.97 ? 45  PHE G C   1 
ATOM   7102  O  O   . PHE G  1 72  ? 99.563  103.072 -14.182 1.00 23.63 ? 45  PHE G O   1 
ATOM   7103  C  CB  . PHE G  1 72  ? 101.319 102.388 -16.377 1.00 27.79 ? 45  PHE G CB  1 
ATOM   7104  C  CG  . PHE G  1 72  ? 101.848 101.032 -16.015 1.00 28.81 ? 45  PHE G CG  1 
ATOM   7105  C  CD1 . PHE G  1 72  ? 101.734 99.945  -16.900 1.00 30.99 ? 45  PHE G CD1 1 
ATOM   7106  C  CD2 . PHE G  1 72  ? 102.570 100.874 -14.834 1.00 28.12 ? 45  PHE G CD2 1 
ATOM   7107  C  CE1 . PHE G  1 72  ? 102.294 98.702  -16.569 1.00 29.50 ? 45  PHE G CE1 1 
ATOM   7108  C  CE2 . PHE G  1 72  ? 103.120 99.645  -14.494 1.00 29.88 ? 45  PHE G CE2 1 
ATOM   7109  C  CZ  . PHE G  1 72  ? 102.971 98.556  -15.362 1.00 33.13 ? 45  PHE G CZ  1 
ATOM   7110  N  N   . HIS G  1 73  ? 98.019  101.641 -15.068 1.00 24.24 ? 46  HIS G N   1 
ATOM   7111  C  CA  . HIS G  1 73  ? 97.186  101.673 -13.884 1.00 24.72 ? 46  HIS G CA  1 
ATOM   7112  C  C   . HIS G  1 73  ? 96.719  100.283 -13.438 1.00 24.19 ? 46  HIS G C   1 
ATOM   7113  O  O   . HIS G  1 73  ? 96.484  99.408  -14.266 1.00 24.77 ? 46  HIS G O   1 
ATOM   7114  C  CB  . HIS G  1 73  ? 95.934  102.512 -14.125 1.00 26.21 ? 46  HIS G CB  1 
ATOM   7115  C  CG  . HIS G  1 73  ? 96.217  103.842 -14.743 1.00 26.96 ? 46  HIS G CG  1 
ATOM   7116  N  ND1 . HIS G  1 73  ? 95.833  104.146 -16.022 1.00 26.63 ? 46  HIS G ND1 1 
ATOM   7117  C  CD2 . HIS G  1 73  ? 96.906  104.922 -14.285 1.00 25.81 ? 46  HIS G CD2 1 
ATOM   7118  C  CE1 . HIS G  1 73  ? 96.217  105.376 -16.320 1.00 28.09 ? 46  HIS G CE1 1 
ATOM   7119  N  NE2 . HIS G  1 73  ? 96.898  105.860 -15.293 1.00 25.61 ? 46  HIS G NE2 1 
ATOM   7120  N  N   . VAL G  1 74  ? 96.522  100.133 -12.145 1.00 22.72 ? 47  VAL G N   1 
ATOM   7121  C  CA  . VAL G  1 74  ? 95.737  98.994  -11.682 1.00 24.47 ? 47  VAL G CA  1 
ATOM   7122  C  C   . VAL G  1 74  ? 94.246  99.386  -11.649 1.00 23.36 ? 47  VAL G C   1 
ATOM   7123  O  O   . VAL G  1 74  ? 93.869  100.399 -11.057 1.00 25.07 ? 47  VAL G O   1 
ATOM   7124  C  CB  . VAL G  1 74  ? 96.195  98.497  -10.307 1.00 25.31 ? 47  VAL G CB  1 
ATOM   7125  C  CG1 . VAL G  1 74  ? 95.351  97.275  -9.855  1.00 23.13 ? 47  VAL G CG1 1 
ATOM   7126  C  CG2 . VAL G  1 74  ? 97.694  98.214  -10.358 1.00 24.48 ? 47  VAL G CG2 1 
ATOM   7127  N  N   . HIS G  1 75  ? 93.425  98.591  -12.334 1.00 24.39 ? 48  HIS G N   1 
ATOM   7128  C  CA  . HIS G  1 75  ? 91.974  98.797  -12.371 1.00 24.35 ? 48  HIS G CA  1 
ATOM   7129  C  C   . HIS G  1 75  ? 91.282  97.814  -11.422 1.00 26.19 ? 48  HIS G C   1 
ATOM   7130  O  O   . HIS G  1 75  ? 91.860  96.819  -11.009 1.00 27.01 ? 48  HIS G O   1 
ATOM   7131  C  CB  . HIS G  1 75  ? 91.457  98.619  -13.796 1.00 23.23 ? 48  HIS G CB  1 
ATOM   7132  C  CG  . HIS G  1 75  ? 91.842  99.727  -14.731 1.00 24.53 ? 48  HIS G CG  1 
ATOM   7133  N  ND1 . HIS G  1 75  ? 90.909  100.567 -15.317 1.00 25.04 ? 48  HIS G ND1 1 
ATOM   7134  C  CD2 . HIS G  1 75  ? 93.046  100.078 -15.256 1.00 23.60 ? 48  HIS G CD2 1 
ATOM   7135  C  CE1 . HIS G  1 75  ? 91.527  101.412 -16.131 1.00 25.52 ? 48  HIS G CE1 1 
ATOM   7136  N  NE2 . HIS G  1 75  ? 92.826  101.134 -16.114 1.00 23.20 ? 48  HIS G NE2 1 
ATOM   7137  N  N   . GLU G  1 76  ? 90.039  98.102  -11.089 1.00 26.16 ? 49  GLU G N   1 
ATOM   7138  C  CA  . GLU G  1 76  ? 89.404  97.476  -9.971  1.00 25.55 ? 49  GLU G CA  1 
ATOM   7139  C  C   . GLU G  1 76  ? 89.137  95.966  -10.147 1.00 25.66 ? 49  GLU G C   1 
ATOM   7140  O  O   . GLU G  1 76  ? 89.397  95.188  -9.241  1.00 25.87 ? 49  GLU G O   1 
ATOM   7141  C  CB  . GLU G  1 76  ? 88.118  98.218  -9.676  1.00 27.17 ? 49  GLU G CB  1 
ATOM   7142  C  CG  . GLU G  1 76  ? 87.457  97.675  -8.433  1.00 32.76 ? 49  GLU G CG  1 
ATOM   7143  C  CD  . GLU G  1 76  ? 86.215  98.449  -8.047  1.00 36.95 ? 49  GLU G CD  1 
ATOM   7144  O  OE1 . GLU G  1 76  ? 85.843  99.415  -8.765  1.00 36.11 ? 49  GLU G OE1 1 
ATOM   7145  O  OE2 . GLU G  1 76  ? 85.622  98.073  -7.019  1.00 37.19 ? 49  GLU G OE2 1 
ATOM   7146  N  N   . PHE G  1 77  ? 88.680  95.548  -11.319 1.00 26.82 ? 50  PHE G N   1 
ATOM   7147  C  CA  . PHE G  1 77  ? 88.241  94.147  -11.437 1.00 26.70 ? 50  PHE G CA  1 
ATOM   7148  C  C   . PHE G  1 77  ? 89.203  93.306  -12.235 1.00 24.81 ? 50  PHE G C   1 
ATOM   7149  O  O   . PHE G  1 77  ? 89.706  93.728  -13.293 1.00 25.74 ? 50  PHE G O   1 
ATOM   7150  C  CB  . PHE G  1 77  ? 86.819  94.083  -12.034 1.00 26.95 ? 50  PHE G CB  1 
ATOM   7151  C  CG  . PHE G  1 77  ? 85.832  94.929  -11.290 1.00 28.59 ? 50  PHE G CG  1 
ATOM   7152  C  CD1 . PHE G  1 77  ? 85.534  94.660  -9.966  1.00 30.97 ? 50  PHE G CD1 1 
ATOM   7153  C  CD2 . PHE G  1 77  ? 85.263  96.064  -11.906 1.00 30.95 ? 50  PHE G CD2 1 
ATOM   7154  C  CE1 . PHE G  1 77  ? 84.637  95.495  -9.257  1.00 33.69 ? 50  PHE G CE1 1 
ATOM   7155  C  CE2 . PHE G  1 77  ? 84.369  96.883  -11.220 1.00 31.99 ? 50  PHE G CE2 1 
ATOM   7156  C  CZ  . PHE G  1 77  ? 84.062  96.597  -9.886  1.00 32.86 ? 50  PHE G CZ  1 
ATOM   7157  N  N   . GLY G  1 78  ? 89.414  92.077  -11.767 1.00 24.30 ? 51  GLY G N   1 
ATOM   7158  C  CA  . GLY G  1 78  ? 90.178  91.105  -12.561 1.00 26.56 ? 51  GLY G CA  1 
ATOM   7159  C  C   . GLY G  1 78  ? 89.266  90.360  -13.543 1.00 30.85 ? 51  GLY G C   1 
ATOM   7160  O  O   . GLY G  1 78  ? 89.290  89.123  -13.590 1.00 32.39 ? 51  GLY G O   1 
ATOM   7161  N  N   . ASP G  1 79  ? 88.456  91.115  -14.293 1.00 31.51 ? 52  ASP G N   1 
ATOM   7162  C  CA  . ASP G  1 79  ? 87.415  90.575  -15.192 1.00 25.14 ? 52  ASP G CA  1 
ATOM   7163  C  C   . ASP G  1 79  ? 87.771  90.927  -16.628 1.00 25.78 ? 52  ASP G C   1 
ATOM   7164  O  O   . ASP G  1 79  ? 87.736  92.093  -17.054 1.00 29.91 ? 52  ASP G O   1 
ATOM   7165  C  CB  . ASP G  1 79  ? 86.046  91.123  -14.767 1.00 26.70 ? 52  ASP G CB  1 
ATOM   7166  C  CG  . ASP G  1 79  ? 84.880  90.610  -15.652 1.00 26.58 ? 52  ASP G CG  1 
ATOM   7167  O  OD1 . ASP G  1 79  ? 85.105  90.143  -16.790 1.00 24.47 ? 52  ASP G OD1 1 
ATOM   7168  O  OD2 . ASP G  1 79  ? 83.744  90.693  -15.145 1.00 29.54 ? 52  ASP G OD2 1 
ATOM   7169  N  N   . ASN G  1 80  ? 88.204  89.920  -17.370 1.00 27.29 ? 53  ASN G N   1 
ATOM   7170  C  CA  . ASN G  1 80  ? 88.556  90.100  -18.758 1.00 28.48 ? 53  ASN G CA  1 
ATOM   7171  C  C   . ASN G  1 80  ? 87.511  89.516  -19.734 1.00 27.80 ? 53  ASN G C   1 
ATOM   7172  O  O   . ASN G  1 80  ? 87.821  89.311  -20.918 1.00 27.81 ? 53  ASN G O   1 
ATOM   7173  C  CB  . ASN G  1 80  ? 89.914  89.446  -19.023 1.00 34.51 ? 53  ASN G CB  1 
ATOM   7174  C  CG  . ASN G  1 80  ? 90.506  89.869  -20.348 1.00 44.77 ? 53  ASN G CG  1 
ATOM   7175  O  OD1 . ASN G  1 80  ? 90.589  91.062  -20.645 1.00 52.75 ? 53  ASN G OD1 1 
ATOM   7176  N  ND2 . ASN G  1 80  ? 90.881  88.891  -21.178 1.00 47.76 ? 53  ASN G ND2 1 
ATOM   7177  N  N   . THR G  1 81  ? 86.284  89.301  -19.263 1.00 29.18 ? 54  THR G N   1 
ATOM   7178  C  CA  . THR G  1 81  ? 85.236  88.709  -20.137 1.00 31.95 ? 54  THR G CA  1 
ATOM   7179  C  C   . THR G  1 81  ? 84.879  89.600  -21.327 1.00 34.80 ? 54  THR G C   1 
ATOM   7180  O  O   . THR G  1 81  ? 84.516  89.099  -22.387 1.00 34.32 ? 54  THR G O   1 
ATOM   7181  C  CB  . THR G  1 81  ? 83.952  88.396  -19.370 1.00 30.62 ? 54  THR G CB  1 
ATOM   7182  O  OG1 . THR G  1 81  ? 83.500  89.589  -18.770 1.00 30.84 ? 54  THR G OG1 1 
ATOM   7183  C  CG2 . THR G  1 81  ? 84.204  87.322  -18.255 1.00 30.74 ? 54  THR G CG2 1 
ATOM   7184  N  N   . ALA G  1 82  ? 84.988  90.917  -21.192 1.00 34.25 ? 55  ALA G N   1 
ATOM   7185  C  CA  . ALA G  1 82  ? 84.822  91.746  -22.397 1.00 36.01 ? 55  ALA G CA  1 
ATOM   7186  C  C   . ALA G  1 82  ? 86.103  92.492  -22.672 1.00 40.29 ? 55  ALA G C   1 
ATOM   7187  O  O   . ALA G  1 82  ? 86.090  93.707  -22.885 1.00 39.15 ? 55  ALA G O   1 
ATOM   7188  C  CB  . ALA G  1 82  ? 83.651  92.713  -22.244 1.00 37.94 ? 55  ALA G CB  1 
ATOM   7189  N  N   . GLY G  1 83  ? 87.219  91.767  -22.620 1.00 36.99 ? 56  GLY G N   1 
ATOM   7190  C  CA  . GLY G  1 83  ? 88.518  92.390  -22.797 1.00 36.25 ? 56  GLY G CA  1 
ATOM   7191  C  C   . GLY G  1 83  ? 88.775  93.389  -21.679 1.00 34.02 ? 56  GLY G C   1 
ATOM   7192  O  O   . GLY G  1 83  ? 88.225  93.275  -20.565 1.00 30.37 ? 56  GLY G O   1 
ATOM   7193  N  N   . CYS G  1 84  ? 89.600  94.386  -21.977 1.00 32.13 ? 57  CYS G N   1 
ATOM   7194  C  CA  . CYS G  1 84  ? 90.031  95.313  -20.934 1.00 34.49 ? 57  CYS G CA  1 
ATOM   7195  C  C   . CYS G  1 84  ? 88.908  96.213  -20.381 1.00 32.38 ? 57  CYS G C   1 
ATOM   7196  O  O   . CYS G  1 84  ? 89.020  96.723  -19.259 1.00 28.55 ? 57  CYS G O   1 
ATOM   7197  C  CB  . CYS G  1 84  ? 91.221  96.144  -21.441 1.00 34.76 ? 57  CYS G CB  1 
ATOM   7198  S  SG  . CYS G  1 84  ? 92.629  95.122  -21.965 1.00 40.56 ? 57  CYS G SG  1 
ATOM   7199  N  N   . THR G  1 85  ? 87.808  96.376  -21.136 1.00 31.45 ? 58  THR G N   1 
ATOM   7200  C  CA  . THR G  1 85  ? 86.675  97.203  -20.674 1.00 32.44 ? 58  THR G CA  1 
ATOM   7201  C  C   . THR G  1 85  ? 86.077  96.676  -19.408 1.00 30.67 ? 58  THR G C   1 
ATOM   7202  O  O   . THR G  1 85  ? 85.701  97.464  -18.532 1.00 30.37 ? 58  THR G O   1 
ATOM   7203  C  CB  . THR G  1 85  ? 85.545  97.245  -21.710 1.00 37.37 ? 58  THR G CB  1 
ATOM   7204  O  OG1 . THR G  1 85  ? 86.101  97.574  -22.982 1.00 44.17 ? 58  THR G OG1 1 
ATOM   7205  C  CG2 . THR G  1 85  ? 84.503  98.276  -21.324 1.00 40.62 ? 58  THR G CG2 1 
ATOM   7206  N  N   . SER G  1 86  ? 85.991  95.340  -19.266 1.00 26.76 ? 59  SER G N   1 
ATOM   7207  C  CA  . SER G  1 86  ? 85.353  94.811  -18.080 1.00 28.88 ? 59  SER G CA  1 
ATOM   7208  C  C   . SER G  1 86  ? 86.205  94.921  -16.799 1.00 27.03 ? 59  SER G C   1 
ATOM   7209  O  O   . SER G  1 86  ? 85.702  94.636  -15.707 1.00 27.25 ? 59  SER G O   1 
ATOM   7210  C  CB  . SER G  1 86  ? 84.842  93.369  -18.343 1.00 31.58 ? 59  SER G CB  1 
ATOM   7211  O  OG  . SER G  1 86  ? 85.832  92.623  -19.007 1.00 34.07 ? 59  SER G OG  1 
ATOM   7212  N  N   . ALA G  1 87  ? 87.473  95.374  -16.898 1.00 27.14 ? 60  ALA G N   1 
ATOM   7213  C  CA  . ALA G  1 87  ? 88.285  95.656  -15.677 1.00 24.90 ? 60  ALA G CA  1 
ATOM   7214  C  C   . ALA G  1 87  ? 87.760  96.840  -14.835 1.00 27.20 ? 60  ALA G C   1 
ATOM   7215  O  O   . ALA G  1 87  ? 88.176  97.021  -13.700 1.00 26.73 ? 60  ALA G O   1 
ATOM   7216  C  CB  . ALA G  1 87  ? 89.769  95.893  -16.042 1.00 23.25 ? 60  ALA G CB  1 
ATOM   7217  N  N   . GLY G  1 88  ? 86.820  97.633  -15.349 1.00 27.01 ? 61  GLY G N   1 
ATOM   7218  C  CA  . GLY G  1 88  ? 86.258  98.706  -14.503 1.00 26.84 ? 61  GLY G CA  1 
ATOM   7219  C  C   . GLY G  1 88  ? 87.231  99.895  -14.405 1.00 24.29 ? 61  GLY G C   1 
ATOM   7220  O  O   . GLY G  1 88  ? 88.129  100.009 -15.232 1.00 26.37 ? 61  GLY G O   1 
ATOM   7221  N  N   . PRO G  1 89  ? 87.027  100.783 -13.428 1.00 29.77 ? 62  PRO G N   1 
ATOM   7222  C  CA  . PRO G  1 89  ? 87.811  102.031 -13.326 1.00 29.42 ? 62  PRO G CA  1 
ATOM   7223  C  C   . PRO G  1 89  ? 89.122  101.798 -12.569 1.00 29.32 ? 62  PRO G C   1 
ATOM   7224  O  O   . PRO G  1 89  ? 89.362  100.680 -12.093 1.00 25.13 ? 62  PRO G O   1 
ATOM   7225  C  CB  . PRO G  1 89  ? 86.890  102.930 -12.508 1.00 30.39 ? 62  PRO G CB  1 
ATOM   7226  C  CG  . PRO G  1 89  ? 86.173  101.980 -11.597 1.00 32.84 ? 62  PRO G CG  1 
ATOM   7227  C  CD  . PRO G  1 89  ? 85.939  100.744 -12.420 1.00 31.30 ? 62  PRO G CD  1 
ATOM   7228  N  N   . HIS G  1 90  ? 89.948  102.840 -12.434 1.00 27.68 ? 63  HIS G N   1 
ATOM   7229  C  CA  . HIS G  1 90  ? 91.179  102.736 -11.614 1.00 26.77 ? 63  HIS G CA  1 
ATOM   7230  C  C   . HIS G  1 90  ? 90.809  102.217 -10.233 1.00 25.91 ? 63  HIS G C   1 
ATOM   7231  O  O   . HIS G  1 90  ? 89.790  102.620 -9.690  1.00 27.42 ? 63  HIS G O   1 
ATOM   7232  C  CB  . HIS G  1 90  ? 91.898  104.128 -11.528 1.00 27.23 ? 63  HIS G CB  1 
ATOM   7233  C  CG  . HIS G  1 90  ? 92.378  104.628 -12.857 1.00 25.34 ? 63  HIS G CG  1 
ATOM   7234  N  ND1 . HIS G  1 90  ? 93.051  105.825 -13.033 1.00 25.37 ? 63  HIS G ND1 1 
ATOM   7235  C  CD2 . HIS G  1 90  ? 92.333  104.043 -14.082 1.00 27.26 ? 63  HIS G CD2 1 
ATOM   7236  C  CE1 . HIS G  1 90  ? 93.352  105.974 -14.314 1.00 24.70 ? 63  HIS G CE1 1 
ATOM   7237  N  NE2 . HIS G  1 90  ? 92.931  104.905 -14.970 1.00 28.56 ? 63  HIS G NE2 1 
ATOM   7238  N  N   . PHE G  1 91  ? 91.613  101.312 -9.677  1.00 23.88 ? 64  PHE G N   1 
ATOM   7239  C  CA  . PHE G  1 91  ? 91.350  100.766 -8.377  1.00 26.71 ? 64  PHE G CA  1 
ATOM   7240  C  C   . PHE G  1 91  ? 91.428  101.907 -7.353  1.00 29.90 ? 64  PHE G C   1 
ATOM   7241  O  O   . PHE G  1 91  ? 92.460  102.566 -7.249  1.00 28.31 ? 64  PHE G O   1 
ATOM   7242  C  CB  . PHE G  1 91  ? 92.366  99.674  -8.071  1.00 25.93 ? 64  PHE G CB  1 
ATOM   7243  C  CG  . PHE G  1 91  ? 92.224  99.068  -6.687  1.00 29.48 ? 64  PHE G CG  1 
ATOM   7244  C  CD1 . PHE G  1 91  ? 90.961  98.717  -6.164  1.00 30.37 ? 64  PHE G CD1 1 
ATOM   7245  C  CD2 . PHE G  1 91  ? 93.342  98.804  -5.937  1.00 28.28 ? 64  PHE G CD2 1 
ATOM   7246  C  CE1 . PHE G  1 91  ? 90.854  98.155  -4.909  1.00 29.38 ? 64  PHE G CE1 1 
ATOM   7247  C  CE2 . PHE G  1 91  ? 93.240  98.237  -4.685  1.00 31.99 ? 64  PHE G CE2 1 
ATOM   7248  C  CZ  . PHE G  1 91  ? 91.994  97.912  -4.167  1.00 31.35 ? 64  PHE G CZ  1 
ATOM   7249  N  N   . ASN G  1 92  ? 90.339  102.146 -6.616  1.00 30.40 ? 65  ASN G N   1 
ATOM   7250  C  CA  . ASN G  1 92  ? 90.195  103.372 -5.808  1.00 29.58 ? 65  ASN G CA  1 
ATOM   7251  C  C   . ASN G  1 92  ? 89.413  103.145 -4.502  1.00 31.42 ? 65  ASN G C   1 
ATOM   7252  O  O   . ASN G  1 92  ? 88.387  103.778 -4.285  1.00 33.10 ? 65  ASN G O   1 
ATOM   7253  C  CB  . ASN G  1 92  ? 89.537  104.478 -6.659  1.00 30.04 ? 65  ASN G CB  1 
ATOM   7254  C  CG  . ASN G  1 92  ? 89.459  105.851 -5.943  1.00 33.22 ? 65  ASN G CG  1 
ATOM   7255  O  OD1 . ASN G  1 92  ? 90.274  106.182 -5.077  1.00 31.33 ? 65  ASN G OD1 1 
ATOM   7256  N  ND2 . ASN G  1 92  ? 88.493  106.670 -6.360  1.00 29.25 ? 65  ASN G ND2 1 
ATOM   7257  N  N   . PRO G  1 93  ? 89.924  102.287 -3.602  1.00 32.65 ? 66  PRO G N   1 
ATOM   7258  C  CA  . PRO G  1 93  ? 89.139  101.948 -2.407  1.00 37.02 ? 66  PRO G CA  1 
ATOM   7259  C  C   . PRO G  1 93  ? 88.969  103.131 -1.423  1.00 40.66 ? 66  PRO G C   1 
ATOM   7260  O  O   . PRO G  1 93  ? 88.037  103.137 -0.620  1.00 40.27 ? 66  PRO G O   1 
ATOM   7261  C  CB  . PRO G  1 93  ? 89.963  100.853 -1.753  1.00 33.49 ? 66  PRO G CB  1 
ATOM   7262  C  CG  . PRO G  1 93  ? 91.361  101.149 -2.170  1.00 33.60 ? 66  PRO G CG  1 
ATOM   7263  C  CD  . PRO G  1 93  ? 91.265  101.678 -3.573  1.00 31.98 ? 66  PRO G CD  1 
ATOM   7264  N  N   . LEU G  1 94  ? 89.862  104.119 -1.480  1.00 39.84 ? 67  LEU G N   1 
ATOM   7265  C  CA  . LEU G  1 94  ? 89.720  105.284 -0.603  1.00 38.56 ? 67  LEU G CA  1 
ATOM   7266  C  C   . LEU G  1 94  ? 88.914  106.422 -1.217  1.00 39.91 ? 67  LEU G C   1 
ATOM   7267  O  O   . LEU G  1 94  ? 88.825  107.481 -0.606  1.00 38.34 ? 67  LEU G O   1 
ATOM   7268  C  CB  . LEU G  1 94  ? 91.091  105.770 -0.123  1.00 42.29 ? 67  LEU G CB  1 
ATOM   7269  C  CG  . LEU G  1 94  ? 91.926  104.694 0.585   1.00 43.88 ? 67  LEU G CG  1 
ATOM   7270  C  CD1 . LEU G  1 94  ? 93.338  105.190 0.861   1.00 43.96 ? 67  LEU G CD1 1 
ATOM   7271  C  CD2 . LEU G  1 94  ? 91.252  104.197 1.873   1.00 47.16 ? 67  LEU G CD2 1 
ATOM   7272  N  N   . SER G  1 95  ? 88.322  106.211 -2.408  1.00 40.09 ? 68  SER G N   1 
ATOM   7273  C  CA  . SER G  1 95  ? 87.454  107.219 -3.060  1.00 40.06 ? 68  SER G CA  1 
ATOM   7274  C  C   . SER G  1 95  ? 88.128  108.572 -3.320  1.00 41.83 ? 68  SER G C   1 
ATOM   7275  O  O   . SER G  1 95  ? 87.527  109.633 -3.120  1.00 43.02 ? 68  SER G O   1 
ATOM   7276  C  CB  . SER G  1 95  ? 86.197  107.470 -2.229  1.00 44.30 ? 68  SER G CB  1 
ATOM   7277  O  OG  . SER G  1 95  ? 85.393  106.322 -2.237  1.00 46.55 ? 68  SER G OG  1 
ATOM   7278  N  N   . ARG G  1 96  ? 89.366  108.538 -3.768  1.00 36.25 ? 69  ARG G N   1 
ATOM   7279  C  CA  . ARG G  1 96  ? 90.102  109.765 -4.016  1.00 36.70 ? 69  ARG G CA  1 
ATOM   7280  C  C   . ARG G  1 96  ? 90.011  110.174 -5.462  1.00 37.05 ? 69  ARG G C   1 
ATOM   7281  O  O   . ARG G  1 96  ? 89.424  109.459 -6.275  1.00 37.79 ? 69  ARG G O   1 
ATOM   7282  C  CB  . ARG G  1 96  ? 91.535  109.591 -3.563  1.00 33.57 ? 69  ARG G CB  1 
ATOM   7283  C  CG  . ARG G  1 96  ? 91.541  109.321 -2.092  1.00 40.89 ? 69  ARG G CG  1 
ATOM   7284  C  CD  . ARG G  1 96  ? 92.904  109.562 -1.523  1.00 47.26 ? 69  ARG G CD  1 
ATOM   7285  N  NE  . ARG G  1 96  ? 92.763  109.619 -0.078  1.00 56.70 ? 69  ARG G NE  1 
ATOM   7286  C  CZ  . ARG G  1 96  ? 93.717  109.282 0.787   1.00 61.06 ? 69  ARG G CZ  1 
ATOM   7287  N  NH1 . ARG G  1 96  ? 94.892  108.838 0.349   1.00 57.62 ? 69  ARG G NH1 1 
ATOM   7288  N  NH2 . ARG G  1 96  ? 93.480  109.368 2.097   1.00 60.69 ? 69  ARG G NH2 1 
ATOM   7289  N  N   . LYS G  1 97  ? 90.541  111.345 -5.793  1.00 35.62 ? 70  LYS G N   1 
ATOM   7290  C  CA  . LYS G  1 97  ? 90.598  111.755 -7.194  1.00 33.98 ? 70  LYS G CA  1 
ATOM   7291  C  C   . LYS G  1 97  ? 91.870  111.205 -7.824  1.00 30.76 ? 70  LYS G C   1 
ATOM   7292  O  O   . LYS G  1 97  ? 92.789  110.842 -7.114  1.00 28.33 ? 70  LYS G O   1 
ATOM   7293  C  CB  . LYS G  1 97  ? 90.516  113.283 -7.310  1.00 37.51 ? 70  LYS G CB  1 
ATOM   7294  C  CG  . LYS G  1 97  ? 89.197  113.822 -6.753  1.00 41.94 ? 70  LYS G CG  1 
ATOM   7295  C  CD  . LYS G  1 97  ? 88.837  115.185 -7.325  1.00 51.40 ? 70  LYS G CD  1 
ATOM   7296  C  CE  . LYS G  1 97  ? 89.766  116.295 -6.831  1.00 54.94 ? 70  LYS G CE  1 
ATOM   7297  N  NZ  . LYS G  1 97  ? 89.425  117.591 -7.498  1.00 66.20 ? 70  LYS G NZ  1 
ATOM   7298  N  N   . HIS G  1 98  ? 91.930  111.170 -9.157  1.00 27.89 ? 71  HIS G N   1 
ATOM   7299  C  CA  . HIS G  1 98  ? 93.079  110.654 -9.883  1.00 27.56 ? 71  HIS G CA  1 
ATOM   7300  C  C   . HIS G  1 98  ? 94.320  111.569 -9.699  1.00 29.08 ? 71  HIS G C   1 
ATOM   7301  O  O   . HIS G  1 98  ? 94.198  112.780 -9.739  1.00 28.40 ? 71  HIS G O   1 
ATOM   7302  C  CB  . HIS G  1 98  ? 92.743  110.483 -11.399 1.00 25.58 ? 71  HIS G CB  1 
ATOM   7303  C  CG  . HIS G  1 98  ? 93.912  110.063 -12.239 1.00 26.38 ? 71  HIS G CG  1 
ATOM   7304  N  ND1 . HIS G  1 98  ? 94.320  108.752 -12.359 1.00 25.42 ? 71  HIS G ND1 1 
ATOM   7305  C  CD2 . HIS G  1 98  ? 94.754  110.786 -13.019 1.00 25.64 ? 71  HIS G CD2 1 
ATOM   7306  C  CE1 . HIS G  1 98  ? 95.377  108.680 -13.152 1.00 24.90 ? 71  HIS G CE1 1 
ATOM   7307  N  NE2 . HIS G  1 98  ? 95.648  109.900 -13.581 1.00 26.32 ? 71  HIS G NE2 1 
ATOM   7308  N  N   . GLY G  1 99  ? 95.497  110.987 -9.535  1.00 27.73 ? 72  GLY G N   1 
ATOM   7309  C  CA  . GLY G  1 99  ? 96.732  111.777 -9.450  1.00 29.01 ? 72  GLY G CA  1 
ATOM   7310  C  C   . GLY G  1 99  ? 97.896  111.006 -10.017 1.00 31.74 ? 72  GLY G C   1 
ATOM   7311  O  O   . GLY G  1 99  ? 97.713  109.929 -10.584 1.00 27.87 ? 72  GLY G O   1 
ATOM   7312  N  N   . GLY G  1 100 ? 99.109  111.553 -9.893  1.00 29.01 ? 73  GLY G N   1 
ATOM   7313  C  CA  . GLY G  1 100 ? 100.315 110.785 -10.217 1.00 27.54 ? 73  GLY G CA  1 
ATOM   7314  C  C   . GLY G  1 100 ? 100.782 109.937 -9.032  1.00 24.93 ? 73  GLY G C   1 
ATOM   7315  O  O   . GLY G  1 100 ? 100.348 110.169 -7.898  1.00 27.56 ? 73  GLY G O   1 
ATOM   7316  N  N   . PRO G  1 101 ? 101.719 109.005 -9.253  1.00 25.33 ? 74  PRO G N   1 
ATOM   7317  C  CA  . PRO G  1 101 ? 102.049 108.120 -8.096  1.00 29.73 ? 74  PRO G CA  1 
ATOM   7318  C  C   . PRO G  1 101 ? 102.671 108.845 -6.912  1.00 33.49 ? 74  PRO G C   1 
ATOM   7319  O  O   . PRO G  1 101 ? 102.486 108.422 -5.783  1.00 32.28 ? 74  PRO G O   1 
ATOM   7320  C  CB  . PRO G  1 101 ? 103.042 107.127 -8.670  1.00 26.77 ? 74  PRO G CB  1 
ATOM   7321  C  CG  . PRO G  1 101 ? 103.497 107.731 -9.953  1.00 30.50 ? 74  PRO G CG  1 
ATOM   7322  C  CD  . PRO G  1 101 ? 102.367 108.556 -10.475 1.00 27.06 ? 74  PRO G CD  1 
ATOM   7323  N  N   . LYS G  1 102 ? 103.344 109.968 -7.171  1.00 35.34 ? 75  LYS G N   1 
ATOM   7324  C  CA  . LYS G  1 102 ? 103.896 110.774 -6.064  1.00 38.95 ? 75  LYS G CA  1 
ATOM   7325  C  C   . LYS G  1 102 ? 102.922 111.717 -5.338  1.00 39.57 ? 75  LYS G C   1 
ATOM   7326  O  O   . LYS G  1 102 ? 103.267 112.307 -4.314  1.00 37.63 ? 75  LYS G O   1 
ATOM   7327  C  CB  . LYS G  1 102 ? 105.188 111.461 -6.508  1.00 40.05 ? 75  LYS G CB  1 
ATOM   7328  C  CG  . LYS G  1 102 ? 106.262 110.443 -6.883  1.00 46.45 ? 75  LYS G CG  1 
ATOM   7329  C  CD  . LYS G  1 102 ? 107.610 110.678 -6.183  1.00 60.46 ? 75  LYS G CD  1 
ATOM   7330  C  CE  . LYS G  1 102 ? 108.191 112.079 -6.433  1.00 61.99 ? 75  LYS G CE  1 
ATOM   7331  N  NZ  . LYS G  1 102 ? 108.335 112.396 -7.900  1.00 61.45 ? 75  LYS G NZ  1 
ATOM   7332  N  N   . ASP G  1 103 ? 101.683 111.821 -5.814  1.00 37.10 ? 76  ASP G N   1 
ATOM   7333  C  CA  . ASP G  1 103 ? 100.690 112.662 -5.151  1.00 37.21 ? 76  ASP G CA  1 
ATOM   7334  C  C   . ASP G  1 103 ? 100.040 111.974 -3.959  1.00 43.80 ? 76  ASP G C   1 
ATOM   7335  O  O   . ASP G  1 103 ? 99.774  110.773 -3.995  1.00 40.19 ? 76  ASP G O   1 
ATOM   7336  C  CB  . ASP G  1 103 ? 99.594  113.069 -6.141  1.00 36.74 ? 76  ASP G CB  1 
ATOM   7337  C  CG  . ASP G  1 103 ? 100.143 113.860 -7.278  1.00 43.01 ? 76  ASP G CG  1 
ATOM   7338  O  OD1 . ASP G  1 103 ? 101.160 114.531 -7.021  1.00 44.48 ? 76  ASP G OD1 1 
ATOM   7339  O  OD2 . ASP G  1 103 ? 99.608  113.820 -8.413  1.00 40.23 ? 76  ASP G OD2 1 
ATOM   7340  N  N   . GLU G  1 104 ? 99.767  112.754 -2.917  1.00 42.48 ? 77  GLU G N   1 
ATOM   7341  C  CA  . GLU G  1 104 ? 98.944  112.327 -1.791  1.00 46.39 ? 77  GLU G CA  1 
ATOM   7342  C  C   . GLU G  1 104 ? 97.538  112.000 -2.307  1.00 44.04 ? 77  GLU G C   1 
ATOM   7343  O  O   . GLU G  1 104 ? 96.948  110.972 -1.933  1.00 41.61 ? 77  GLU G O   1 
ATOM   7344  C  CB  . GLU G  1 104 ? 98.846  113.462 -0.750  1.00 52.88 ? 77  GLU G CB  1 
ATOM   7345  C  CG  . GLU G  1 104 ? 100.169 114.145 -0.344  1.00 64.83 ? 77  GLU G CG  1 
ATOM   7346  C  CD  . GLU G  1 104 ? 101.056 114.667 -1.506  1.00 71.95 ? 77  GLU G CD  1 
ATOM   7347  O  OE1 . GLU G  1 104 ? 100.565 115.350 -2.452  1.00 63.49 ? 77  GLU G OE1 1 
ATOM   7348  O  OE2 . GLU G  1 104 ? 102.286 114.396 -1.473  1.00 76.12 ? 77  GLU G OE2 1 
ATOM   7349  N  N   . GLU G  1 105 ? 97.012  112.865 -3.183  1.00 39.33 ? 78  GLU G N   1 
ATOM   7350  C  CA  . GLU G  1 105 ? 95.673  112.663 -3.744  1.00 37.29 ? 78  GLU G CA  1 
ATOM   7351  C  C   . GLU G  1 105 ? 95.824  111.848 -5.027  1.00 34.12 ? 78  GLU G C   1 
ATOM   7352  O  O   . GLU G  1 105 ? 96.188  112.368 -6.071  1.00 30.39 ? 78  GLU G O   1 
ATOM   7353  C  CB  . GLU G  1 105 ? 94.970  114.001 -4.009  1.00 35.22 ? 78  GLU G CB  1 
ATOM   7354  C  CG  . GLU G  1 105 ? 93.523  113.895 -4.510  1.00 41.16 ? 78  GLU G CG  1 
ATOM   7355  C  CD  . GLU G  1 105 ? 92.523  113.426 -3.449  1.00 48.90 ? 78  GLU G CD  1 
ATOM   7356  O  OE1 . GLU G  1 105 ? 92.860  113.393 -2.232  1.00 57.74 ? 78  GLU G OE1 1 
ATOM   7357  O  OE2 . GLU G  1 105 ? 91.373  113.095 -3.810  1.00 46.18 ? 78  GLU G OE2 1 
ATOM   7358  N  N   . ARG G  1 106 ? 95.586  110.548 -4.921  1.00 31.84 ? 79  ARG G N   1 
ATOM   7359  C  CA  . ARG G  1 106 ? 95.662  109.664 -6.083  1.00 28.35 ? 79  ARG G CA  1 
ATOM   7360  C  C   . ARG G  1 106 ? 94.746  108.449 -5.800  1.00 27.98 ? 79  ARG G C   1 
ATOM   7361  O  O   . ARG G  1 106 ? 94.368  108.200 -4.655  1.00 29.31 ? 79  ARG G O   1 
ATOM   7362  C  CB  . ARG G  1 106 ? 97.104  109.152 -6.274  1.00 27.41 ? 79  ARG G CB  1 
ATOM   7363  C  CG  . ARG G  1 106 ? 97.670  108.475 -5.033  1.00 27.06 ? 79  ARG G CG  1 
ATOM   7364  C  CD  . ARG G  1 106 ? 99.016  107.814 -5.331  1.00 30.23 ? 79  ARG G CD  1 
ATOM   7365  N  NE  . ARG G  1 106 ? 98.857  106.394 -5.712  1.00 26.48 ? 79  ARG G NE  1 
ATOM   7366  C  CZ  . ARG G  1 106 ? 99.864  105.535 -5.885  1.00 29.34 ? 79  ARG G CZ  1 
ATOM   7367  N  NH1 . ARG G  1 106 ? 101.114 105.925 -5.720  1.00 29.97 ? 79  ARG G NH1 1 
ATOM   7368  N  NH2 . ARG G  1 106 ? 99.637  104.247 -6.226  1.00 27.06 ? 79  ARG G NH2 1 
ATOM   7369  N  N   . HIS G  1 107 ? 94.410  107.705 -6.845  1.00 28.13 ? 80  HIS G N   1 
ATOM   7370  C  CA  . HIS G  1 107 ? 93.839  106.365 -6.670  1.00 26.62 ? 80  HIS G CA  1 
ATOM   7371  C  C   . HIS G  1 107 ? 94.931  105.397 -6.233  1.00 27.48 ? 80  HIS G C   1 
ATOM   7372  O  O   . HIS G  1 107 ? 96.115  105.550 -6.618  1.00 26.39 ? 80  HIS G O   1 
ATOM   7373  C  CB  . HIS G  1 107 ? 93.256  105.877 -8.001  1.00 24.56 ? 80  HIS G CB  1 
ATOM   7374  C  CG  . HIS G  1 107 ? 92.214  106.791 -8.568  1.00 23.31 ? 80  HIS G CG  1 
ATOM   7375  N  ND1 . HIS G  1 107 ? 92.121  107.071 -9.919  1.00 23.06 ? 80  HIS G ND1 1 
ATOM   7376  C  CD2 . HIS G  1 107 ? 91.238  107.510 -7.968  1.00 24.70 ? 80  HIS G CD2 1 
ATOM   7377  C  CE1 . HIS G  1 107 ? 91.078  107.863 -10.131 1.00 24.50 ? 80  HIS G CE1 1 
ATOM   7378  N  NE2 . HIS G  1 107 ? 90.536  108.156 -8.960  1.00 24.59 ? 80  HIS G NE2 1 
ATOM   7379  N  N   . VAL G  1 108 ? 94.548  104.346 -5.499  1.00 27.25 ? 81  VAL G N   1 
ATOM   7380  C  CA  . VAL G  1 108 ? 95.512  103.301 -5.216  1.00 24.73 ? 81  VAL G CA  1 
ATOM   7381  C  C   . VAL G  1 108 ? 96.158  102.769 -6.494  1.00 26.33 ? 81  VAL G C   1 
ATOM   7382  O  O   . VAL G  1 108 ? 97.368  102.560 -6.533  1.00 26.24 ? 81  VAL G O   1 
ATOM   7383  C  CB  . VAL G  1 108 ? 94.923  102.149 -4.350  1.00 26.90 ? 81  VAL G CB  1 
ATOM   7384  C  CG1 . VAL G  1 108 ? 95.896  100.955 -4.323  1.00 26.44 ? 81  VAL G CG1 1 
ATOM   7385  C  CG2 . VAL G  1 108 ? 94.700  102.670 -2.945  1.00 27.15 ? 81  VAL G CG2 1 
ATOM   7386  N  N   . GLY G  1 109 ? 95.373  102.612 -7.572  1.00 26.65 ? 82  GLY G N   1 
ATOM   7387  C  CA  . GLY G  1 109 ? 95.896  102.086 -8.831  1.00 25.50 ? 82  GLY G CA  1 
ATOM   7388  C  C   . GLY G  1 109 ? 96.728  103.026 -9.720  1.00 27.89 ? 82  GLY G C   1 
ATOM   7389  O  O   . GLY G  1 109 ? 97.147  102.651 -10.814 1.00 26.27 ? 82  GLY G O   1 
ATOM   7390  N  N   . ASP G  1 110 ? 97.008  104.236 -9.246  1.00 26.91 ? 83  ASP G N   1 
ATOM   7391  C  CA  . ASP G  1 110 ? 97.709  105.219 -10.095 1.00 27.79 ? 83  ASP G CA  1 
ATOM   7392  C  C   . ASP G  1 110 ? 99.213  105.041 -10.086 1.00 27.30 ? 83  ASP G C   1 
ATOM   7393  O  O   . ASP G  1 110 ? 99.892  105.580 -9.211  1.00 28.98 ? 83  ASP G O   1 
ATOM   7394  C  CB  . ASP G  1 110 ? 97.353  106.627 -9.640  1.00 24.35 ? 83  ASP G CB  1 
ATOM   7395  C  CG  . ASP G  1 110 ? 95.921  106.984 -9.998  1.00 25.61 ? 83  ASP G CG  1 
ATOM   7396  O  OD1 . ASP G  1 110 ? 95.287  106.229 -10.798 1.00 26.39 ? 83  ASP G OD1 1 
ATOM   7397  O  OD2 . ASP G  1 110 ? 95.432  107.994 -9.477  1.00 26.30 ? 83  ASP G OD2 1 
ATOM   7398  N  N   . LEU G  1 111 ? 99.716  104.297 -11.054 1.00 25.05 ? 84  LEU G N   1 
ATOM   7399  C  CA  . LEU G  1 111 ? 101.146 104.053 -11.160 1.00 26.58 ? 84  LEU G CA  1 
ATOM   7400  C  C   . LEU G  1 111 ? 101.808 105.010 -12.157 1.00 27.49 ? 84  LEU G C   1 
ATOM   7401  O  O   . LEU G  1 111 ? 102.969 104.819 -12.511 1.00 29.45 ? 84  LEU G O   1 
ATOM   7402  C  CB  . LEU G  1 111 ? 101.465 102.590 -11.520 1.00 25.05 ? 84  LEU G CB  1 
ATOM   7403  C  CG  . LEU G  1 111 ? 101.017 101.588 -10.452 1.00 27.17 ? 84  LEU G CG  1 
ATOM   7404  C  CD1 . LEU G  1 111 ? 101.375 100.148 -10.846 1.00 27.50 ? 84  LEU G CD1 1 
ATOM   7405  C  CD2 . LEU G  1 111 ? 101.678 101.968 -9.131  1.00 28.16 ? 84  LEU G CD2 1 
ATOM   7406  N  N   . GLY G  1 112 ? 101.075 106.026 -12.617 1.00 26.84 ? 85  GLY G N   1 
ATOM   7407  C  CA  . GLY G  1 112 ? 101.624 107.004 -13.597 1.00 26.16 ? 85  GLY G CA  1 
ATOM   7408  C  C   . GLY G  1 112 ? 101.821 106.515 -15.016 1.00 29.37 ? 85  GLY G C   1 
ATOM   7409  O  O   . GLY G  1 112 ? 100.925 105.869 -15.610 1.00 28.20 ? 85  GLY G O   1 
ATOM   7410  N  N   . ASN G  1 113 ? 102.991 106.831 -15.582 1.00 23.53 ? 86  ASN G N   1 
ATOM   7411  C  CA  . ASN G  1 113 ? 103.328 106.446 -16.937 1.00 25.25 ? 86  ASN G CA  1 
ATOM   7412  C  C   . ASN G  1 113 ? 104.500 105.444 -17.107 1.00 26.89 ? 86  ASN G C   1 
ATOM   7413  O  O   . ASN G  1 113 ? 105.375 105.350 -16.272 1.00 29.02 ? 86  ASN G O   1 
ATOM   7414  C  CB  . ASN G  1 113 ? 103.699 107.700 -17.731 1.00 25.63 ? 86  ASN G CB  1 
ATOM   7415  C  CG  . ASN G  1 113 ? 102.497 108.574 -18.016 1.00 29.67 ? 86  ASN G CG  1 
ATOM   7416  O  OD1 . ASN G  1 113 ? 101.577 108.164 -18.748 1.00 27.86 ? 86  ASN G OD1 1 
ATOM   7417  N  ND2 . ASN G  1 113 ? 102.478 109.779 -17.429 1.00 27.66 ? 86  ASN G ND2 1 
ATOM   7418  N  N   . VAL G  1 114 ? 104.516 104.743 -18.229 1.00 27.85 ? 87  VAL G N   1 
ATOM   7419  C  CA  . VAL G  1 114 ? 105.714 104.021 -18.653 1.00 29.98 ? 87  VAL G CA  1 
ATOM   7420  C  C   . VAL G  1 114 ? 106.145 104.600 -19.980 1.00 31.14 ? 87  VAL G C   1 
ATOM   7421  O  O   . VAL G  1 114 ? 105.336 105.252 -20.663 1.00 31.63 ? 87  VAL G O   1 
ATOM   7422  C  CB  . VAL G  1 114 ? 105.499 102.489 -18.717 1.00 30.09 ? 87  VAL G CB  1 
ATOM   7423  C  CG1 . VAL G  1 114 ? 105.146 101.997 -17.345 1.00 29.80 ? 87  VAL G CG1 1 
ATOM   7424  C  CG2 . VAL G  1 114 ? 104.425 102.122 -19.744 1.00 29.88 ? 87  VAL G CG2 1 
ATOM   7425  N  N   . THR G  1 115 ? 107.416 104.380 -20.353 1.00 31.44 ? 88  THR G N   1 
ATOM   7426  C  CA  . THR G  1 115 ? 107.967 104.996 -21.548 1.00 32.28 ? 88  THR G CA  1 
ATOM   7427  C  C   . THR G  1 115 ? 108.388 103.944 -22.568 1.00 31.41 ? 88  THR G C   1 
ATOM   7428  O  O   . THR G  1 115 ? 109.166 103.064 -22.259 1.00 40.54 ? 88  THR G O   1 
ATOM   7429  C  CB  . THR G  1 115 ? 109.223 105.898 -21.225 1.00 34.61 ? 88  THR G CB  1 
ATOM   7430  O  OG1 . THR G  1 115 ? 108.944 106.735 -20.105 1.00 36.26 ? 88  THR G OG1 1 
ATOM   7431  C  CG2 . THR G  1 115 ? 109.615 106.791 -22.427 1.00 37.06 ? 88  THR G CG2 1 
ATOM   7432  N  N   . ALA G  1 116 ? 107.879 104.075 -23.770 1.00 36.68 ? 89  ALA G N   1 
ATOM   7433  C  CA  . ALA G  1 116 ? 108.209 103.203 -24.873 1.00 41.01 ? 89  ALA G CA  1 
ATOM   7434  C  C   . ALA G  1 116 ? 109.334 103.900 -25.664 1.00 41.94 ? 89  ALA G C   1 
ATOM   7435  O  O   . ALA G  1 116 ? 109.167 105.055 -26.068 1.00 40.27 ? 89  ALA G O   1 
ATOM   7436  C  CB  . ALA G  1 116 ? 106.989 103.005 -25.751 1.00 36.24 ? 89  ALA G CB  1 
ATOM   7437  N  N   . ASP G  1 117 ? 110.453 103.189 -25.867 1.00 45.26 ? 90  ASP G N   1 
ATOM   7438  C  CA  . ASP G  1 117 ? 111.558 103.638 -26.760 1.00 45.49 ? 90  ASP G CA  1 
ATOM   7439  C  C   . ASP G  1 117 ? 111.094 103.637 -28.223 1.00 47.63 ? 90  ASP G C   1 
ATOM   7440  O  O   . ASP G  1 117 ? 109.949 103.233 -28.525 1.00 44.43 ? 90  ASP G O   1 
ATOM   7441  C  CB  . ASP G  1 117 ? 112.832 102.780 -26.540 1.00 45.42 ? 90  ASP G CB  1 
ATOM   7442  C  CG  . ASP G  1 117 ? 112.715 101.354 -27.127 1.00 47.45 ? 90  ASP G CG  1 
ATOM   7443  O  OD1 . ASP G  1 117 ? 111.933 101.114 -28.071 1.00 50.63 ? 90  ASP G OD1 1 
ATOM   7444  O  OD2 . ASP G  1 117 ? 113.436 100.456 -26.660 1.00 48.14 ? 90  ASP G OD2 1 
ATOM   7445  N  N   . LYS G  1 118 ? 111.955 104.083 -29.145 1.00 50.37 ? 91  LYS G N   1 
ATOM   7446  C  CA  . LYS G  1 118 ? 111.555 104.199 -30.573 1.00 48.17 ? 91  LYS G CA  1 
ATOM   7447  C  C   . LYS G  1 118 ? 111.240 102.852 -31.242 1.00 44.94 ? 91  LYS G C   1 
ATOM   7448  O  O   . LYS G  1 118 ? 110.517 102.799 -32.233 1.00 50.37 ? 91  LYS G O   1 
ATOM   7449  C  CB  . LYS G  1 118 ? 112.597 104.991 -31.396 1.00 53.06 ? 91  LYS G CB  1 
ATOM   7450  C  CG  . LYS G  1 118 ? 113.993 104.370 -31.458 1.00 56.70 ? 91  LYS G CG  1 
ATOM   7451  C  CD  . LYS G  1 118 ? 115.047 105.452 -31.733 1.00 61.68 ? 91  LYS G CD  1 
ATOM   7452  C  CE  . LYS G  1 118 ? 116.081 105.017 -32.762 1.00 63.01 ? 91  LYS G CE  1 
ATOM   7453  N  NZ  . LYS G  1 118 ? 116.794 103.761 -32.384 1.00 60.24 ? 91  LYS G NZ  1 
ATOM   7454  N  N   . ASP G  1 119 ? 111.785 101.770 -30.689 1.00 47.74 ? 92  ASP G N   1 
ATOM   7455  C  CA  . ASP G  1 119 ? 111.409 100.394 -31.085 1.00 52.99 ? 92  ASP G CA  1 
ATOM   7456  C  C   . ASP G  1 119 ? 110.127 99.856  -30.417 1.00 54.38 ? 92  ASP G C   1 
ATOM   7457  O  O   . ASP G  1 119 ? 109.849 98.652  -30.503 1.00 50.99 ? 92  ASP G O   1 
ATOM   7458  C  CB  . ASP G  1 119 ? 112.545 99.422  -30.755 1.00 52.16 ? 92  ASP G CB  1 
ATOM   7459  C  CG  . ASP G  1 119 ? 113.852 99.823  -31.396 1.00 57.13 ? 92  ASP G CG  1 
ATOM   7460  O  OD1 . ASP G  1 119 ? 113.863 99.995  -32.633 1.00 58.58 ? 92  ASP G OD1 1 
ATOM   7461  O  OD2 . ASP G  1 119 ? 114.854 99.976  -30.663 1.00 55.19 ? 92  ASP G OD2 1 
ATOM   7462  N  N   . GLY G  1 120 ? 109.361 100.728 -29.749 1.00 55.27 ? 93  GLY G N   1 
ATOM   7463  C  CA  . GLY G  1 120 ? 108.075 100.357 -29.149 1.00 44.17 ? 93  GLY G CA  1 
ATOM   7464  C  C   . GLY G  1 120 ? 108.161 99.539  -27.875 1.00 45.37 ? 93  GLY G C   1 
ATOM   7465  O  O   . GLY G  1 120 ? 107.162 99.006  -27.404 1.00 43.53 ? 93  GLY G O   1 
ATOM   7466  N  N   . VAL G  1 121 ? 109.348 99.436  -27.300 1.00 41.62 ? 94  VAL G N   1 
ATOM   7467  C  CA  . VAL G  1 121 ? 109.541 98.661  -26.082 1.00 40.20 ? 94  VAL G CA  1 
ATOM   7468  C  C   . VAL G  1 121 ? 109.574 99.594  -24.891 1.00 42.16 ? 94  VAL G C   1 
ATOM   7469  O  O   . VAL G  1 121 ? 110.330 100.570 -24.901 1.00 42.56 ? 94  VAL G O   1 
ATOM   7470  C  CB  . VAL G  1 121 ? 110.873 97.864  -26.121 1.00 41.70 ? 94  VAL G CB  1 
ATOM   7471  C  CG1 . VAL G  1 121 ? 111.078 97.082  -24.828 1.00 40.44 ? 94  VAL G CG1 1 
ATOM   7472  C  CG2 . VAL G  1 121 ? 110.885 96.931  -27.313 1.00 39.80 ? 94  VAL G CG2 1 
ATOM   7473  N  N   . ALA G  1 122 ? 108.755 99.310  -23.874 1.00 36.87 ? 95  ALA G N   1 
ATOM   7474  C  CA  . ALA G  1 122 ? 108.882 99.968  -22.578 1.00 36.56 ? 95  ALA G CA  1 
ATOM   7475  C  C   . ALA G  1 122 ? 109.474 98.984  -21.597 1.00 40.71 ? 95  ALA G C   1 
ATOM   7476  O  O   . ALA G  1 122 ? 108.891 97.917  -21.344 1.00 39.03 ? 95  ALA G O   1 
ATOM   7477  C  CB  . ALA G  1 122 ? 107.508 100.441 -22.063 1.00 36.76 ? 95  ALA G CB  1 
ATOM   7478  N  N   . ASP G  1 123 ? 110.634 99.331  -21.043 1.00 38.22 ? 96  ASP G N   1 
ATOM   7479  C  CA  . ASP G  1 123 ? 111.200 98.602  -19.908 1.00 42.24 ? 96  ASP G CA  1 
ATOM   7480  C  C   . ASP G  1 123 ? 110.681 99.320  -18.707 1.00 41.93 ? 96  ASP G C   1 
ATOM   7481  O  O   . ASP G  1 123 ? 110.858 100.526 -18.576 1.00 48.57 ? 96  ASP G O   1 
ATOM   7482  C  CB  . ASP G  1 123 ? 112.748 98.595  -19.940 1.00 47.76 ? 96  ASP G CB  1 
ATOM   7483  C  CG  . ASP G  1 123 ? 113.297 97.658  -21.015 1.00 53.43 ? 96  ASP G CG  1 
ATOM   7484  O  OD1 . ASP G  1 123 ? 114.037 98.132  -21.904 1.00 61.55 ? 96  ASP G OD1 1 
ATOM   7485  O  OD2 . ASP G  1 123 ? 112.966 96.445  -20.985 1.00 60.80 ? 96  ASP G OD2 1 
ATOM   7486  N  N   . VAL G  1 124 ? 109.975 98.605  -17.852 1.00 33.83 ? 97  VAL G N   1 
ATOM   7487  C  CA  . VAL G  1 124 ? 109.275 99.252  -16.822 1.00 30.70 ? 97  VAL G CA  1 
ATOM   7488  C  C   . VAL G  1 124 ? 110.016 98.953  -15.568 1.00 30.98 ? 97  VAL G C   1 
ATOM   7489  O  O   . VAL G  1 124 ? 110.418 97.812  -15.367 1.00 31.98 ? 97  VAL G O   1 
ATOM   7490  C  CB  . VAL G  1 124 ? 107.832 98.680  -16.739 1.00 32.23 ? 97  VAL G CB  1 
ATOM   7491  C  CG1 . VAL G  1 124 ? 107.151 99.088  -15.433 1.00 34.49 ? 97  VAL G CG1 1 
ATOM   7492  C  CG2 . VAL G  1 124 ? 107.049 99.060  -17.987 1.00 29.10 ? 97  VAL G CG2 1 
ATOM   7493  N  N   . SER G  1 125 ? 110.162 99.961  -14.709 1.00 28.27 ? 98  SER G N   1 
ATOM   7494  C  CA  . SER G  1 125 ? 110.752 99.784  -13.416 1.00 30.53 ? 98  SER G CA  1 
ATOM   7495  C  C   . SER G  1 125 ? 110.279 100.890 -12.497 1.00 34.28 ? 98  SER G C   1 
ATOM   7496  O  O   . SER G  1 125 ? 110.659 102.059 -12.621 1.00 33.30 ? 98  SER G O   1 
ATOM   7497  C  CB  . SER G  1 125 ? 112.304 99.749  -13.509 1.00 33.91 ? 98  SER G CB  1 
ATOM   7498  O  OG  . SER G  1 125 ? 112.826 99.511  -12.214 1.00 35.76 ? 98  SER G OG  1 
ATOM   7499  N  N   . ILE G  1 126 ? 109.462 100.506 -11.530 1.00 34.75 ? 99  ILE G N   1 
ATOM   7500  C  CA  . ILE G  1 126 ? 108.752 101.445 -10.729 1.00 32.91 ? 99  ILE G CA  1 
ATOM   7501  C  C   . ILE G  1 126 ? 108.791 100.902 -9.309  1.00 34.30 ? 99  ILE G C   1 
ATOM   7502  O  O   . ILE G  1 126 ? 108.812 99.682  -9.073  1.00 35.60 ? 99  ILE G O   1 
ATOM   7503  C  CB  . ILE G  1 126 ? 107.271 101.533 -11.254 1.00 36.31 ? 99  ILE G CB  1 
ATOM   7504  C  CG1 . ILE G  1 126 ? 107.177 102.464 -12.467 1.00 36.95 ? 99  ILE G CG1 1 
ATOM   7505  C  CG2 . ILE G  1 126 ? 106.318 101.972 -10.157 1.00 37.52 ? 99  ILE G CG2 1 
ATOM   7506  C  CD1 . ILE G  1 126 ? 105.804 102.446 -13.165 1.00 39.02 ? 99  ILE G CD1 1 
ATOM   7507  N  N   . GLU G  1 127 ? 108.775 101.795 -8.342  1.00 30.60 ? 100 GLU G N   1 
ATOM   7508  C  CA  . GLU G  1 127 ? 108.649 101.374 -6.988  1.00 36.13 ? 100 GLU G CA  1 
ATOM   7509  C  C   . GLU G  1 127 ? 107.513 102.163 -6.348  1.00 35.72 ? 100 GLU G C   1 
ATOM   7510  O  O   . GLU G  1 127 ? 107.460 103.374 -6.481  1.00 36.71 ? 100 GLU G O   1 
ATOM   7511  C  CB  . GLU G  1 127 ? 109.990 101.611 -6.272  1.00 39.67 ? 100 GLU G CB  1 
ATOM   7512  C  CG  . GLU G  1 127 ? 109.869 101.491 -4.782  1.00 46.10 ? 100 GLU G CG  1 
ATOM   7513  C  CD  . GLU G  1 127 ? 111.149 101.017 -4.111  1.00 54.66 ? 100 GLU G CD  1 
ATOM   7514  O  OE1 . GLU G  1 127 ? 111.982 100.327 -4.761  1.00 57.76 ? 100 GLU G OE1 1 
ATOM   7515  O  OE2 . GLU G  1 127 ? 111.284 101.325 -2.909  1.00 50.51 ? 100 GLU G OE2 1 
ATOM   7516  N  N   . ASP G  1 128 ? 106.606 101.488 -5.647  1.00 33.78 ? 101 ASP G N   1 
ATOM   7517  C  CA  . ASP G  1 128 ? 105.429 102.146 -5.156  1.00 33.89 ? 101 ASP G CA  1 
ATOM   7518  C  C   . ASP G  1 128 ? 105.048 101.685 -3.782  1.00 37.14 ? 101 ASP G C   1 
ATOM   7519  O  O   . ASP G  1 128 ? 105.045 100.491 -3.495  1.00 38.87 ? 101 ASP G O   1 
ATOM   7520  C  CB  . ASP G  1 128 ? 104.237 101.935 -6.119  1.00 39.20 ? 101 ASP G CB  1 
ATOM   7521  C  CG  . ASP G  1 128 ? 103.086 102.915 -5.838  1.00 38.77 ? 101 ASP G CG  1 
ATOM   7522  O  OD1 . ASP G  1 128 ? 103.199 104.081 -6.275  1.00 43.86 ? 101 ASP G OD1 1 
ATOM   7523  O  OD2 . ASP G  1 128 ? 102.083 102.548 -5.184  1.00 34.95 ? 101 ASP G OD2 1 
ATOM   7524  N  N   . SER G  1 129 ? 104.631 102.619 -2.941  1.00 35.83 ? 102 SER G N   1 
ATOM   7525  C  CA  . SER G  1 129 ? 104.334 102.259 -1.575  1.00 37.46 ? 102 SER G CA  1 
ATOM   7526  C  C   . SER G  1 129 ? 102.880 102.368 -1.231  1.00 36.13 ? 102 SER G C   1 
ATOM   7527  O  O   . SER G  1 129 ? 102.501 102.167 -0.075  1.00 40.06 ? 102 SER G O   1 
ATOM   7528  C  CB  . SER G  1 129 ? 105.169 103.097 -0.614  1.00 42.90 ? 102 SER G CB  1 
ATOM   7529  O  OG  . SER G  1 129 ? 106.415 102.445 -0.432  1.00 54.03 ? 102 SER G OG  1 
ATOM   7530  N  N   . VAL G  1 130 ? 102.060 102.665 -2.236  1.00 35.38 ? 103 VAL G N   1 
ATOM   7531  C  CA  . VAL G  1 130 ? 100.617 102.734 -2.030  1.00 31.20 ? 103 VAL G CA  1 
ATOM   7532  C  C   . VAL G  1 130 ? 99.885  101.427 -2.420  1.00 32.41 ? 103 VAL G C   1 
ATOM   7533  O  O   . VAL G  1 130 ? 98.997  100.970 -1.677  1.00 31.59 ? 103 VAL G O   1 
ATOM   7534  C  CB  . VAL G  1 130 ? 100.010 103.955 -2.756  1.00 34.00 ? 103 VAL G CB  1 
ATOM   7535  C  CG1 . VAL G  1 130 ? 98.496  103.923 -2.674  1.00 32.65 ? 103 VAL G CG1 1 
ATOM   7536  C  CG2 . VAL G  1 130 ? 100.523 105.262 -2.123  1.00 36.26 ? 103 VAL G CG2 1 
ATOM   7537  N  N   . ILE G  1 131 ? 100.227 100.855 -3.572  1.00 30.99 ? 104 ILE G N   1 
ATOM   7538  C  CA  . ILE G  1 131 ? 99.760  99.501  -3.880  1.00 31.35 ? 104 ILE G CA  1 
ATOM   7539  C  C   . ILE G  1 131 ? 100.364 98.518  -2.874  1.00 38.59 ? 104 ILE G C   1 
ATOM   7540  O  O   . ILE G  1 131 ? 101.397 98.819  -2.256  1.00 36.94 ? 104 ILE G O   1 
ATOM   7541  C  CB  . ILE G  1 131 ? 100.102 99.065  -5.301  1.00 30.77 ? 104 ILE G CB  1 
ATOM   7542  C  CG1 . ILE G  1 131 ? 101.633 99.046  -5.529  1.00 28.33 ? 104 ILE G CG1 1 
ATOM   7543  C  CG2 . ILE G  1 131 ? 99.284  99.898  -6.298  1.00 28.72 ? 104 ILE G CG2 1 
ATOM   7544  C  CD1 . ILE G  1 131 ? 102.125 98.440  -6.842  1.00 28.17 ? 104 ILE G CD1 1 
ATOM   7545  N  N   . SER G  1 132 ? 99.691  97.373  -2.677  1.00 33.22 ? 105 SER G N   1 
ATOM   7546  C  CA  . SER G  1 132 ? 100.209 96.303  -1.844  1.00 36.23 ? 105 SER G CA  1 
ATOM   7547  C  C   . SER G  1 132 ? 99.877  94.916  -2.434  1.00 38.40 ? 105 SER G C   1 
ATOM   7548  O  O   . SER G  1 132 ? 99.002  94.781  -3.316  1.00 33.76 ? 105 SER G O   1 
ATOM   7549  C  CB  . SER G  1 132 ? 99.669  96.422  -0.429  1.00 37.32 ? 105 SER G CB  1 
ATOM   7550  O  OG  . SER G  1 132 ? 100.390 95.545  0.395   1.00 38.28 ? 105 SER G OG  1 
ATOM   7551  N  N   . LEU G  1 133 ? 100.609 93.903  -1.977  1.00 38.12 ? 106 LEU G N   1 
ATOM   7552  C  CA  . LEU G  1 133 ? 100.276 92.515  -2.314  1.00 36.56 ? 106 LEU G CA  1 
ATOM   7553  C  C   . LEU G  1 133 ? 99.466  91.808  -1.226  1.00 38.18 ? 106 LEU G C   1 
ATOM   7554  O  O   . LEU G  1 133 ? 99.138  90.642  -1.375  1.00 39.62 ? 106 LEU G O   1 
ATOM   7555  C  CB  . LEU G  1 133 ? 101.520 91.709  -2.728  1.00 34.77 ? 106 LEU G CB  1 
ATOM   7556  C  CG  . LEU G  1 133 ? 102.321 92.227  -3.933  1.00 32.72 ? 106 LEU G CG  1 
ATOM   7557  C  CD1 . LEU G  1 133 ? 103.388 91.216  -4.338  1.00 33.15 ? 106 LEU G CD1 1 
ATOM   7558  C  CD2 . LEU G  1 133 ? 101.464 92.591  -5.157  1.00 35.61 ? 106 LEU G CD2 1 
ATOM   7559  N  N   . SER G  1 134 ? 99.141  92.522  -0.149  1.00 39.41 ? 107 SER G N   1 
ATOM   7560  C  CA  . SER G  1 134 ? 98.218  92.048  0.896   1.00 41.83 ? 107 SER G CA  1 
ATOM   7561  C  C   . SER G  1 134 ? 97.418  93.214  1.484   1.00 43.16 ? 107 SER G C   1 
ATOM   7562  O  O   . SER G  1 134 ? 97.665  94.377  1.128   1.00 43.18 ? 107 SER G O   1 
ATOM   7563  C  CB  . SER G  1 134 ? 98.981  91.310  1.996   1.00 45.80 ? 107 SER G CB  1 
ATOM   7564  O  OG  . SER G  1 134 ? 100.019 92.116  2.551   1.00 50.06 ? 107 SER G OG  1 
ATOM   7565  N  N   . GLY G  1 135 ? 96.424  92.910  2.323   1.00 40.33 ? 108 GLY G N   1 
ATOM   7566  C  CA  . GLY G  1 135 ? 95.594  93.928  2.963   1.00 41.19 ? 108 GLY G CA  1 
ATOM   7567  C  C   . GLY G  1 135 ? 94.640  94.676  2.038   1.00 48.35 ? 108 GLY G C   1 
ATOM   7568  O  O   . GLY G  1 135 ? 94.364  94.240  0.902   1.00 44.52 ? 108 GLY G O   1 
ATOM   7569  N  N   . ASP G  1 136 ? 94.169  95.825  2.529   1.00 46.86 ? 109 ASP G N   1 
ATOM   7570  C  CA  . ASP G  1 136 ? 93.085  96.633  1.918   1.00 53.75 ? 109 ASP G CA  1 
ATOM   7571  C  C   . ASP G  1 136 ? 93.411  97.212  0.542   1.00 48.77 ? 109 ASP G C   1 
ATOM   7572  O  O   . ASP G  1 136 ? 92.509  97.482  -0.258  1.00 49.97 ? 109 ASP G O   1 
ATOM   7573  C  CB  . ASP G  1 136 ? 92.695  97.788  2.862   1.00 60.21 ? 109 ASP G CB  1 
ATOM   7574  C  CG  . ASP G  1 136 ? 92.029  97.302  4.164   1.00 71.97 ? 109 ASP G CG  1 
ATOM   7575  O  OD1 . ASP G  1 136 ? 92.114  96.089  4.484   1.00 74.23 ? 109 ASP G OD1 1 
ATOM   7576  O  OD2 . ASP G  1 136 ? 91.406  98.138  4.868   1.00 69.81 ? 109 ASP G OD2 1 
ATOM   7577  N  N   . HIS G  1 137 ? 94.700  97.418  0.294   1.00 40.58 ? 110 HIS G N   1 
ATOM   7578  C  CA  . HIS G  1 137 ? 95.190  97.933  -0.988  1.00 40.16 ? 110 HIS G CA  1 
ATOM   7579  C  C   . HIS G  1 137 ? 95.766  96.796  -1.829  1.00 37.57 ? 110 HIS G C   1 
ATOM   7580  O  O   . HIS G  1 137 ? 96.524  97.029  -2.765  1.00 36.54 ? 110 HIS G O   1 
ATOM   7581  C  CB  . HIS G  1 137 ? 96.275  99.024  -0.786  1.00 41.90 ? 110 HIS G CB  1 
ATOM   7582  C  CG  . HIS G  1 137 ? 95.784  100.263 -0.096  1.00 43.41 ? 110 HIS G CG  1 
ATOM   7583  N  ND1 . HIS G  1 137 ? 96.620  101.325 0.210   1.00 47.23 ? 110 HIS G ND1 1 
ATOM   7584  C  CD2 . HIS G  1 137 ? 94.548  100.613 0.345   1.00 42.63 ? 110 HIS G CD2 1 
ATOM   7585  C  CE1 . HIS G  1 137 ? 95.916  102.273 0.807   1.00 48.55 ? 110 HIS G CE1 1 
ATOM   7586  N  NE2 . HIS G  1 137 ? 94.658  101.867 0.900   1.00 45.78 ? 110 HIS G NE2 1 
ATOM   7587  N  N   . CYS G  1 138 ? 95.417  95.565  -1.483  1.00 33.93 ? 111 CYS G N   1 
ATOM   7588  C  CA  . CYS G  1 138 ? 95.912  94.408  -2.218  1.00 33.63 ? 111 CYS G CA  1 
ATOM   7589  C  C   . CYS G  1 138 ? 95.482  94.447  -3.701  1.00 28.35 ? 111 CYS G C   1 
ATOM   7590  O  O   . CYS G  1 138 ? 94.342  94.692  -3.987  1.00 32.18 ? 111 CYS G O   1 
ATOM   7591  C  CB  . CYS G  1 138 ? 95.402  93.131  -1.532  1.00 32.91 ? 111 CYS G CB  1 
ATOM   7592  S  SG  . CYS G  1 138 ? 95.976  91.699  -2.406  1.00 41.22 ? 111 CYS G SG  1 
ATOM   7593  N  N   . ILE G  1 139 ? 96.376  94.194  -4.645  1.00 28.38 ? 112 ILE G N   1 
ATOM   7594  C  CA  . ILE G  1 139 ? 95.992  94.294  -6.063  1.00 28.26 ? 112 ILE G CA  1 
ATOM   7595  C  C   . ILE G  1 139 ? 95.946  92.922  -6.735  1.00 25.92 ? 112 ILE G C   1 
ATOM   7596  O  O   . ILE G  1 139 ? 95.780  92.813  -7.952  1.00 25.46 ? 112 ILE G O   1 
ATOM   7597  C  CB  . ILE G  1 139 ? 96.978  95.196  -6.862  1.00 31.01 ? 112 ILE G CB  1 
ATOM   7598  C  CG1 . ILE G  1 139 ? 98.404  94.639  -6.748  1.00 31.04 ? 112 ILE G CG1 1 
ATOM   7599  C  CG2 . ILE G  1 139 ? 96.874  96.658  -6.362  1.00 31.25 ? 112 ILE G CG2 1 
ATOM   7600  C  CD1 . ILE G  1 139 ? 99.461  95.377  -7.548  1.00 29.60 ? 112 ILE G CD1 1 
ATOM   7601  N  N   . ILE G  1 140 ? 96.199  91.879  -5.951  1.00 27.81 ? 113 ILE G N   1 
ATOM   7602  C  CA  . ILE G  1 140 ? 96.205  90.519  -6.496  1.00 28.26 ? 113 ILE G CA  1 
ATOM   7603  C  C   . ILE G  1 140 ? 94.778  90.259  -6.948  1.00 26.47 ? 113 ILE G C   1 
ATOM   7604  O  O   . ILE G  1 140 ? 93.846  90.528  -6.203  1.00 25.36 ? 113 ILE G O   1 
ATOM   7605  C  CB  . ILE G  1 140 ? 96.595  89.492  -5.419  1.00 32.18 ? 113 ILE G CB  1 
ATOM   7606  C  CG1 . ILE G  1 140 ? 98.042  89.740  -4.984  1.00 34.06 ? 113 ILE G CG1 1 
ATOM   7607  C  CG2 . ILE G  1 140 ? 96.444  88.062  -5.945  1.00 32.98 ? 113 ILE G CG2 1 
ATOM   7608  C  CD1 . ILE G  1 140 ? 99.015  89.130  -5.938  1.00 34.27 ? 113 ILE G CD1 1 
ATOM   7609  N  N   . GLY G  1 141 ? 94.598  89.769  -8.167  1.00 27.33 ? 114 GLY G N   1 
ATOM   7610  C  CA  . GLY G  1 141 ? 93.231  89.424  -8.587  1.00 26.57 ? 114 GLY G CA  1 
ATOM   7611  C  C   . GLY G  1 141 ? 92.568  90.618  -9.258  1.00 30.09 ? 114 GLY G C   1 
ATOM   7612  O  O   . GLY G  1 141 ? 91.430  90.522  -9.693  1.00 26.91 ? 114 GLY G O   1 
ATOM   7613  N  N   . ARG G  1 142 ? 93.284  91.750  -9.345  1.00 27.59 ? 115 ARG G N   1 
ATOM   7614  C  CA  . ARG G  1 142 ? 92.792  92.911  -10.096 1.00 25.94 ? 115 ARG G CA  1 
ATOM   7615  C  C   . ARG G  1 142 ? 93.497  92.935  -11.447 1.00 27.43 ? 115 ARG G C   1 
ATOM   7616  O  O   . ARG G  1 142 ? 94.145  91.979  -11.805 1.00 27.08 ? 115 ARG G O   1 
ATOM   7617  C  CB  . ARG G  1 142 ? 92.948  94.200  -9.262  1.00 24.74 ? 115 ARG G CB  1 
ATOM   7618  C  CG  . ARG G  1 142 ? 92.459  93.995  -7.838  1.00 26.65 ? 115 ARG G CG  1 
ATOM   7619  C  CD  . ARG G  1 142 ? 92.167  95.265  -7.074  1.00 27.40 ? 115 ARG G CD  1 
ATOM   7620  N  NE  . ARG G  1 142 ? 91.635  95.028  -5.727  1.00 29.00 ? 115 ARG G NE  1 
ATOM   7621  C  CZ  . ARG G  1 142 ? 90.343  94.963  -5.413  1.00 30.01 ? 115 ARG G CZ  1 
ATOM   7622  N  NH1 . ARG G  1 142 ? 89.396  95.117  -6.335  1.00 29.56 ? 115 ARG G NH1 1 
ATOM   7623  N  NH2 . ARG G  1 142 ? 90.002  94.788  -4.156  1.00 31.82 ? 115 ARG G NH2 1 
ATOM   7624  N  N   . THR G  1 143 ? 93.364  94.019  -12.213 1.00 26.52 ? 116 THR G N   1 
ATOM   7625  C  CA  . THR G  1 143 ? 93.828  94.040  -13.579 1.00 25.44 ? 116 THR G CA  1 
ATOM   7626  C  C   . THR G  1 143 ? 94.807  95.187  -13.786 1.00 28.02 ? 116 THR G C   1 
ATOM   7627  O  O   . THR G  1 143 ? 94.541  96.350  -13.387 1.00 28.58 ? 116 THR G O   1 
ATOM   7628  C  CB  . THR G  1 143 ? 92.640  94.218  -14.567 1.00 27.36 ? 116 THR G CB  1 
ATOM   7629  O  OG1 . THR G  1 143 ? 91.818  93.023  -14.561 1.00 24.53 ? 116 THR G OG1 1 
ATOM   7630  C  CG2 . THR G  1 143 ? 93.125  94.501  -16.003 1.00 25.23 ? 116 THR G CG2 1 
ATOM   7631  N  N   . LEU G  1 144 ? 95.930  94.870  -14.407 1.00 27.11 ? 117 LEU G N   1 
ATOM   7632  C  CA  . LEU G  1 144 ? 96.885  95.926  -14.774 1.00 26.55 ? 117 LEU G CA  1 
ATOM   7633  C  C   . LEU G  1 144 ? 96.613  96.303  -16.201 1.00 23.53 ? 117 LEU G C   1 
ATOM   7634  O  O   . LEU G  1 144 ? 96.441  95.425  -17.061 1.00 25.46 ? 117 LEU G O   1 
ATOM   7635  C  CB  . LEU G  1 144 ? 98.308  95.379  -14.617 1.00 26.05 ? 117 LEU G CB  1 
ATOM   7636  C  CG  . LEU G  1 144 ? 99.405  96.336  -15.062 1.00 28.10 ? 117 LEU G CG  1 
ATOM   7637  C  CD1 . LEU G  1 144 ? 99.462  97.502  -14.086 1.00 26.65 ? 117 LEU G CD1 1 
ATOM   7638  C  CD2 . LEU G  1 144 ? 100.694 95.532  -15.042 1.00 25.55 ? 117 LEU G CD2 1 
ATOM   7639  N  N   . VAL G  1 145 ? 96.550  97.609  -16.501 1.00 22.99 ? 118 VAL G N   1 
ATOM   7640  C  CA  . VAL G  1 145 ? 96.254  98.034  -17.853 1.00 22.57 ? 118 VAL G CA  1 
ATOM   7641  C  C   . VAL G  1 145 ? 97.276  99.050  -18.362 1.00 25.70 ? 118 VAL G C   1 
ATOM   7642  O  O   . VAL G  1 145 ? 97.616  99.981  -17.643 1.00 26.95 ? 118 VAL G O   1 
ATOM   7643  C  CB  . VAL G  1 145 ? 94.859  98.745  -17.920 1.00 24.01 ? 118 VAL G CB  1 
ATOM   7644  C  CG1 . VAL G  1 145 ? 94.553  99.261  -19.327 1.00 23.44 ? 118 VAL G CG1 1 
ATOM   7645  C  CG2 . VAL G  1 145 ? 93.750  97.786  -17.469 1.00 24.46 ? 118 VAL G CG2 1 
ATOM   7646  N  N   . VAL G  1 146 ? 97.707  98.900  -19.607 1.00 23.83 ? 119 VAL G N   1 
ATOM   7647  C  CA  . VAL G  1 146 ? 98.537  99.938  -20.240 1.00 27.89 ? 119 VAL G CA  1 
ATOM   7648  C  C   . VAL G  1 146 ? 97.689  100.688 -21.262 1.00 28.58 ? 119 VAL G C   1 
ATOM   7649  O  O   . VAL G  1 146 ? 96.951  100.075 -22.054 1.00 28.36 ? 119 VAL G O   1 
ATOM   7650  C  CB  . VAL G  1 146 ? 99.837  99.381  -20.865 1.00 28.91 ? 119 VAL G CB  1 
ATOM   7651  C  CG1 . VAL G  1 146 ? 99.565  98.270  -21.884 1.00 30.08 ? 119 VAL G CG1 1 
ATOM   7652  C  CG2 . VAL G  1 146 ? 100.647 100.487 -21.525 1.00 31.80 ? 119 VAL G CG2 1 
ATOM   7653  N  N   . HIS G  1 147 ? 97.756  102.018 -21.213 1.00 25.05 ? 120 HIS G N   1 
ATOM   7654  C  CA  . HIS G  1 147 ? 96.833  102.860 -22.004 1.00 24.87 ? 120 HIS G CA  1 
ATOM   7655  C  C   . HIS G  1 147 ? 97.466  103.466 -23.267 1.00 26.62 ? 120 HIS G C   1 
ATOM   7656  O  O   . HIS G  1 147 ? 98.705  103.502 -23.427 1.00 31.49 ? 120 HIS G O   1 
ATOM   7657  C  CB  . HIS G  1 147 ? 96.228  103.961 -21.142 1.00 26.33 ? 120 HIS G CB  1 
ATOM   7658  C  CG  . HIS G  1 147 ? 95.258  103.467 -20.107 1.00 24.30 ? 120 HIS G CG  1 
ATOM   7659  N  ND1 . HIS G  1 147 ? 93.896  103.686 -20.201 1.00 27.04 ? 120 HIS G ND1 1 
ATOM   7660  C  CD2 . HIS G  1 147 ? 95.453  102.780 -18.960 1.00 27.14 ? 120 HIS G CD2 1 
ATOM   7661  C  CE1 . HIS G  1 147 ? 93.290  103.145 -19.153 1.00 26.92 ? 120 HIS G CE1 1 
ATOM   7662  N  NE2 . HIS G  1 147 ? 94.221  102.588 -18.380 1.00 28.85 ? 120 HIS G NE2 1 
ATOM   7663  N  N   . GLU G  1 148 ? 96.586  103.958 -24.138 1.00 25.42 ? 121 GLU G N   1 
ATOM   7664  C  CA  . GLU G  1 148 ? 96.905  104.502 -25.450 1.00 32.05 ? 121 GLU G CA  1 
ATOM   7665  C  C   . GLU G  1 148 ? 97.772  105.761 -25.393 1.00 32.40 ? 121 GLU G C   1 
ATOM   7666  O  O   . GLU G  1 148 ? 98.729  105.886 -26.164 1.00 31.62 ? 121 GLU G O   1 
ATOM   7667  C  CB  . GLU G  1 148 ? 95.558  104.812 -26.121 1.00 35.31 ? 121 GLU G CB  1 
ATOM   7668  C  CG  . GLU G  1 148 ? 95.555  105.439 -27.501 1.00 40.22 ? 121 GLU G CG  1 
ATOM   7669  C  CD  . GLU G  1 148 ? 94.239  106.200 -27.767 1.00 44.80 ? 121 GLU G CD  1 
ATOM   7670  O  OE1 . GLU G  1 148 ? 93.316  106.259 -26.911 1.00 40.43 ? 121 GLU G OE1 1 
ATOM   7671  O  OE2 . GLU G  1 148 ? 94.131  106.804 -28.841 1.00 49.37 ? 121 GLU G OE2 1 
ATOM   7672  N  N   . LYS G  1 149 ? 97.440  106.678 -24.481 1.00 34.22 ? 122 LYS G N   1 
ATOM   7673  C  CA  . LYS G  1 149 ? 98.141  107.991 -24.352 1.00 36.71 ? 122 LYS G CA  1 
ATOM   7674  C  C   . LYS G  1 149 ? 98.769  108.199 -22.970 1.00 32.48 ? 122 LYS G C   1 
ATOM   7675  O  O   . LYS G  1 149 ? 98.580  107.377 -22.069 1.00 29.05 ? 122 LYS G O   1 
ATOM   7676  C  CB  . LYS G  1 149 ? 97.193  109.169 -24.575 1.00 37.02 ? 122 LYS G CB  1 
ATOM   7677  C  CG  . LYS G  1 149 ? 96.143  109.029 -25.649 1.00 43.76 ? 122 LYS G CG  1 
ATOM   7678  C  CD  . LYS G  1 149 ? 95.758  110.423 -26.107 1.00 46.64 ? 122 LYS G CD  1 
ATOM   7679  C  CE  . LYS G  1 149 ? 94.355  110.444 -26.674 1.00 52.59 ? 122 LYS G CE  1 
ATOM   7680  N  NZ  . LYS G  1 149 ? 93.374  110.435 -25.558 1.00 55.65 ? 122 LYS G NZ  1 
ATOM   7681  N  N   . ALA G  1 150 ? 99.492  109.320 -22.820 1.00 28.90 ? 123 ALA G N   1 
ATOM   7682  C  CA  . ALA G  1 150 ? 100.104 109.714 -21.536 1.00 28.05 ? 123 ALA G CA  1 
ATOM   7683  C  C   . ALA G  1 150 ? 99.037  109.944 -20.499 1.00 27.31 ? 123 ALA G C   1 
ATOM   7684  O  O   . ALA G  1 150 ? 97.946  110.480 -20.812 1.00 29.34 ? 123 ALA G O   1 
ATOM   7685  C  CB  . ALA G  1 150 ? 100.930 111.004 -21.723 1.00 27.31 ? 123 ALA G CB  1 
ATOM   7686  N  N   . ASP G  1 151 ? 99.297  109.520 -19.266 1.00 25.58 ? 124 ASP G N   1 
ATOM   7687  C  CA  . ASP G  1 151 ? 98.484  109.950 -18.134 1.00 25.72 ? 124 ASP G CA  1 
ATOM   7688  C  C   . ASP G  1 151 ? 98.936  111.390 -17.795 1.00 29.61 ? 124 ASP G C   1 
ATOM   7689  O  O   . ASP G  1 151 ? 100.149 111.598 -17.605 1.00 25.52 ? 124 ASP G O   1 
ATOM   7690  C  CB  . ASP G  1 151 ? 98.775  109.006 -16.992 1.00 26.55 ? 124 ASP G CB  1 
ATOM   7691  C  CG  . ASP G  1 151 ? 97.980  109.281 -15.733 1.00 27.81 ? 124 ASP G CG  1 
ATOM   7692  O  OD1 . ASP G  1 151 ? 97.449  110.381 -15.510 1.00 26.48 ? 124 ASP G OD1 1 
ATOM   7693  O  OD2 . ASP G  1 151 ? 97.970  108.366 -14.870 1.00 29.35 ? 124 ASP G OD2 1 
ATOM   7694  N  N   . ASP G  1 152 ? 97.998  112.345 -17.691 1.00 26.04 ? 125 ASP G N   1 
ATOM   7695  C  CA  . ASP G  1 152 ? 98.346  113.756 -17.354 1.00 25.68 ? 125 ASP G CA  1 
ATOM   7696  C  C   . ASP G  1 152 ? 98.496  113.998 -15.843 1.00 26.52 ? 125 ASP G C   1 
ATOM   7697  O  O   . ASP G  1 152 ? 98.723  115.118 -15.368 1.00 24.22 ? 125 ASP G O   1 
ATOM   7698  C  CB  . ASP G  1 152 ? 97.385  114.761 -18.045 1.00 25.48 ? 125 ASP G CB  1 
ATOM   7699  C  CG  . ASP G  1 152 ? 95.968  114.745 -17.477 1.00 25.53 ? 125 ASP G CG  1 
ATOM   7700  O  OD1 . ASP G  1 152 ? 95.692  114.290 -16.331 1.00 25.45 ? 125 ASP G OD1 1 
ATOM   7701  O  OD2 . ASP G  1 152 ? 95.101  115.242 -18.233 1.00 27.15 ? 125 ASP G OD2 1 
ATOM   7702  N  N   . LEU G  1 153 ? 98.374  112.908 -15.081 1.00 23.63 ? 126 LEU G N   1 
ATOM   7703  C  CA  . LEU G  1 153 ? 98.627  112.889 -13.634 1.00 25.47 ? 126 LEU G CA  1 
ATOM   7704  C  C   . LEU G  1 153 ? 97.690  113.794 -12.884 1.00 26.44 ? 126 LEU G C   1 
ATOM   7705  O  O   . LEU G  1 153 ? 98.008  114.244 -11.783 1.00 25.92 ? 126 LEU G O   1 
ATOM   7706  C  CB  . LEU G  1 153 ? 100.109 113.178 -13.280 1.00 26.16 ? 126 LEU G CB  1 
ATOM   7707  C  CG  . LEU G  1 153 ? 101.139 112.431 -14.124 1.00 28.90 ? 126 LEU G CG  1 
ATOM   7708  C  CD1 . LEU G  1 153 ? 102.572 112.878 -13.794 1.00 31.01 ? 126 LEU G CD1 1 
ATOM   7709  C  CD2 . LEU G  1 153 ? 100.983 110.898 -13.940 1.00 28.17 ? 126 LEU G CD2 1 
ATOM   7710  N  N   . GLY G  1 154 ? 96.491  114.022 -13.444 1.00 25.37 ? 127 GLY G N   1 
ATOM   7711  C  CA  . GLY G  1 154 ? 95.528  114.833 -12.732 1.00 23.98 ? 127 GLY G CA  1 
ATOM   7712  C  C   . GLY G  1 154 ? 95.747  116.304 -12.976 1.00 21.78 ? 127 GLY G C   1 
ATOM   7713  O  O   . GLY G  1 154 ? 95.099  117.134 -12.345 1.00 23.21 ? 127 GLY G O   1 
ATOM   7714  N  N   . LYS G  1 155 ? 96.588  116.653 -13.946 1.00 23.73 ? 128 LYS G N   1 
ATOM   7715  C  CA  . LYS G  1 155 ? 96.902  118.079 -14.151 1.00 24.25 ? 128 LYS G CA  1 
ATOM   7716  C  C   . LYS G  1 155 ? 96.352  118.659 -15.458 1.00 25.05 ? 128 LYS G C   1 
ATOM   7717  O  O   . LYS G  1 155 ? 96.822  119.698 -15.924 1.00 26.37 ? 128 LYS G O   1 
ATOM   7718  C  CB  . LYS G  1 155 ? 98.428  118.297 -14.104 1.00 29.11 ? 128 LYS G CB  1 
ATOM   7719  C  CG  . LYS G  1 155 ? 99.039  117.868 -12.750 1.00 30.76 ? 128 LYS G CG  1 
ATOM   7720  C  CD  . LYS G  1 155 ? 100.420 118.472 -12.521 1.00 44.09 ? 128 LYS G CD  1 
ATOM   7721  C  CE  . LYS G  1 155 ? 101.338 118.259 -13.711 1.00 46.31 ? 128 LYS G CE  1 
ATOM   7722  N  NZ  . LYS G  1 155 ? 102.664 118.945 -13.555 1.00 52.21 ? 128 LYS G NZ  1 
ATOM   7723  N  N   . GLY G  1 156 ? 95.355  118.001 -16.020 1.00 23.93 ? 129 GLY G N   1 
ATOM   7724  C  CA  . GLY G  1 156 ? 94.818  118.391 -17.314 1.00 20.67 ? 129 GLY G CA  1 
ATOM   7725  C  C   . GLY G  1 156 ? 93.756  119.482 -17.279 1.00 22.21 ? 129 GLY G C   1 
ATOM   7726  O  O   . GLY G  1 156 ? 93.450  120.044 -18.335 1.00 24.50 ? 129 GLY G O   1 
ATOM   7727  N  N   . GLY G  1 157 ? 93.212  119.790 -16.093 1.00 20.36 ? 130 GLY G N   1 
ATOM   7728  C  CA  . GLY G  1 157 ? 92.245  120.874 -15.891 1.00 23.70 ? 130 GLY G CA  1 
ATOM   7729  C  C   . GLY G  1 157 ? 90.830  120.633 -16.420 1.00 25.18 ? 130 GLY G C   1 
ATOM   7730  O  O   . GLY G  1 157 ? 90.011  121.561 -16.440 1.00 24.71 ? 130 GLY G O   1 
ATOM   7731  N  N   . ASN G  1 158 ? 90.570  119.430 -16.924 1.00 25.75 ? 131 ASN G N   1 
ATOM   7732  C  CA  . ASN G  1 158 ? 89.187  119.039 -17.237 1.00 26.87 ? 131 ASN G CA  1 
ATOM   7733  C  C   . ASN G  1 158 ? 88.691  117.968 -16.245 1.00 29.62 ? 131 ASN G C   1 
ATOM   7734  O  O   . ASN G  1 158 ? 89.475  117.402 -15.479 1.00 28.54 ? 131 ASN G O   1 
ATOM   7735  C  CB  . ASN G  1 158 ? 89.034  118.587 -18.714 1.00 26.83 ? 131 ASN G CB  1 
ATOM   7736  C  CG  . ASN G  1 158 ? 89.808  117.320 -19.040 1.00 28.42 ? 131 ASN G CG  1 
ATOM   7737  O  OD1 . ASN G  1 158 ? 90.572  116.813 -18.226 1.00 31.19 ? 131 ASN G OD1 1 
ATOM   7738  N  ND2 . ASN G  1 158 ? 89.610  116.802 -20.242 1.00 29.54 ? 131 ASN G ND2 1 
ATOM   7739  N  N   . GLU G  1 159 ? 87.397  117.664 -16.263 1.00 29.01 ? 132 GLU G N   1 
ATOM   7740  C  CA  . GLU G  1 159 ? 86.843  116.659 -15.339 1.00 32.89 ? 132 GLU G CA  1 
ATOM   7741  C  C   . GLU G  1 159 ? 87.501  115.301 -15.516 1.00 29.11 ? 132 GLU G C   1 
ATOM   7742  O  O   . GLU G  1 159 ? 87.792  114.624 -14.548 1.00 31.73 ? 132 GLU G O   1 
ATOM   7743  C  CB  . GLU G  1 159 ? 85.327  116.521 -15.544 1.00 35.76 ? 132 GLU G CB  1 
ATOM   7744  C  CG  . GLU G  1 159 ? 84.605  117.849 -15.406 1.00 45.77 ? 132 GLU G CG  1 
ATOM   7745  C  CD  . GLU G  1 159 ? 83.088  117.714 -15.369 1.00 56.47 ? 132 GLU G CD  1 
ATOM   7746  O  OE1 . GLU G  1 159 ? 82.559  117.094 -14.401 1.00 56.34 ? 132 GLU G OE1 1 
ATOM   7747  O  OE2 . GLU G  1 159 ? 82.434  118.253 -16.297 1.00 56.59 ? 132 GLU G OE2 1 
ATOM   7748  N  N   . GLU G  1 160 ? 87.729  114.927 -16.762 1.00 27.22 ? 133 GLU G N   1 
ATOM   7749  C  CA  . GLU G  1 160 ? 88.304  113.625 -17.101 1.00 30.83 ? 133 GLU G CA  1 
ATOM   7750  C  C   . GLU G  1 160 ? 89.719  113.451 -16.480 1.00 31.05 ? 133 GLU G C   1 
ATOM   7751  O  O   . GLU G  1 160 ? 90.087  112.357 -16.082 1.00 27.22 ? 133 GLU G O   1 
ATOM   7752  C  CB  . GLU G  1 160 ? 88.373  113.474 -18.621 1.00 34.46 ? 133 GLU G CB  1 
ATOM   7753  C  CG  . GLU G  1 160 ? 88.588  112.062 -19.148 1.00 38.37 ? 133 GLU G CG  1 
ATOM   7754  C  CD  . GLU G  1 160 ? 87.540  111.098 -18.603 1.00 45.83 ? 133 GLU G CD  1 
ATOM   7755  O  OE1 . GLU G  1 160 ? 86.325  111.386 -18.681 1.00 43.37 ? 133 GLU G OE1 1 
ATOM   7756  O  OE2 . GLU G  1 160 ? 87.933  110.055 -18.055 1.00 44.42 ? 133 GLU G OE2 1 
ATOM   7757  N  N   . SER G  1 161 ? 90.470  114.539 -16.336 1.00 27.55 ? 134 SER G N   1 
ATOM   7758  C  CA  . SER G  1 161 ? 91.812  114.431 -15.753 1.00 26.40 ? 134 SER G CA  1 
ATOM   7759  C  C   . SER G  1 161 ? 91.796  113.849 -14.339 1.00 26.54 ? 134 SER G C   1 
ATOM   7760  O  O   . SER G  1 161 ? 92.668  113.055 -14.004 1.00 25.09 ? 134 SER G O   1 
ATOM   7761  C  CB  . SER G  1 161 ? 92.502  115.811 -15.748 1.00 25.61 ? 134 SER G CB  1 
ATOM   7762  O  OG  . SER G  1 161 ? 93.810  115.661 -15.228 1.00 25.94 ? 134 SER G OG  1 
ATOM   7763  N  N   . THR G  1 162 ? 90.805  114.262 -13.540 1.00 24.93 ? 135 THR G N   1 
ATOM   7764  C  CA  . THR G  1 162 ? 90.617  113.897 -12.156 1.00 28.11 ? 135 THR G CA  1 
ATOM   7765  C  C   . THR G  1 162 ? 90.025  112.474 -12.012 1.00 27.17 ? 135 THR G C   1 
ATOM   7766  O  O   . THR G  1 162 ? 89.894  111.958 -10.890 1.00 27.33 ? 135 THR G O   1 
ATOM   7767  C  CB  . THR G  1 162 ? 89.645  114.899 -11.435 1.00 34.07 ? 135 THR G CB  1 
ATOM   7768  O  OG1 . THR G  1 162 ? 88.278  114.589 -11.805 1.00 44.53 ? 135 THR G OG1 1 
ATOM   7769  C  CG2 . THR G  1 162 ? 89.897  116.301 -11.853 1.00 36.24 ? 135 THR G CG2 1 
ATOM   7770  N  N   . LYS G  1 163 ? 89.697  111.848 -13.134 1.00 29.73 ? 136 LYS G N   1 
ATOM   7771  C  CA  . LYS G  1 163 ? 89.140  110.487 -13.149 1.00 32.81 ? 136 LYS G CA  1 
ATOM   7772  C  C   . LYS G  1 163 ? 90.115  109.488 -13.784 1.00 28.49 ? 136 LYS G C   1 
ATOM   7773  O  O   . LYS G  1 163 ? 90.459  108.467 -13.181 1.00 31.81 ? 136 LYS G O   1 
ATOM   7774  C  CB  . LYS G  1 163 ? 87.812  110.495 -13.926 1.00 34.96 ? 136 LYS G CB  1 
ATOM   7775  C  CG  . LYS G  1 163 ? 86.697  111.160 -13.129 1.00 41.67 ? 136 LYS G CG  1 
ATOM   7776  C  CD  . LYS G  1 163 ? 85.394  111.238 -13.903 1.00 52.06 ? 136 LYS G CD  1 
ATOM   7777  C  CE  . LYS G  1 163 ? 84.369  112.070 -13.131 1.00 60.38 ? 136 LYS G CE  1 
ATOM   7778  N  NZ  . LYS G  1 163 ? 83.245  112.537 -13.998 1.00 65.53 ? 136 LYS G NZ  1 
ATOM   7779  N  N   . THR G  1 164 ? 90.580  109.783 -14.995 1.00 26.94 ? 137 THR G N   1 
ATOM   7780  C  CA  . THR G  1 164 ? 91.431  108.826 -15.722 1.00 28.54 ? 137 THR G CA  1 
ATOM   7781  C  C   . THR G  1 164 ? 92.805  109.386 -16.169 1.00 27.78 ? 137 THR G C   1 
ATOM   7782  O  O   . THR G  1 164 ? 93.606  108.674 -16.793 1.00 27.57 ? 137 THR G O   1 
ATOM   7783  C  CB  . THR G  1 164 ? 90.714  108.350 -16.994 1.00 29.37 ? 137 THR G CB  1 
ATOM   7784  O  OG1 . THR G  1 164 ? 90.589  109.447 -17.917 1.00 29.56 ? 137 THR G OG1 1 
ATOM   7785  C  CG2 . THR G  1 164 ? 89.325  107.761 -16.661 1.00 30.92 ? 137 THR G CG2 1 
ATOM   7786  N  N   . GLY G  1 165 ? 93.048  110.660 -15.904 1.00 25.87 ? 138 GLY G N   1 
ATOM   7787  C  CA  . GLY G  1 165 ? 94.281  111.310 -16.395 1.00 25.38 ? 138 GLY G CA  1 
ATOM   7788  C  C   . GLY G  1 165 ? 94.271  111.469 -17.901 1.00 25.17 ? 138 GLY G C   1 
ATOM   7789  O  O   . GLY G  1 165 ? 95.315  111.672 -18.505 1.00 23.85 ? 138 GLY G O   1 
ATOM   7790  N  N   . ASN G  1 166 ? 93.105  111.307 -18.544 1.00 26.81 ? 139 ASN G N   1 
ATOM   7791  C  CA  . ASN G  1 166 ? 93.019  111.410 -20.006 1.00 25.21 ? 139 ASN G CA  1 
ATOM   7792  C  C   . ASN G  1 166 ? 93.946  110.440 -20.751 1.00 26.66 ? 139 ASN G C   1 
ATOM   7793  O  O   . ASN G  1 166 ? 94.401  110.748 -21.877 1.00 26.09 ? 139 ASN G O   1 
ATOM   7794  C  CB  . ASN G  1 166 ? 93.337  112.874 -20.468 1.00 26.54 ? 139 ASN G CB  1 
ATOM   7795  C  CG  . ASN G  1 166 ? 92.273  113.876 -20.011 1.00 32.71 ? 139 ASN G CG  1 
ATOM   7796  O  OD1 . ASN G  1 166 ? 91.158  113.847 -20.490 1.00 32.63 ? 139 ASN G OD1 1 
ATOM   7797  N  ND2 . ASN G  1 166 ? 92.611  114.745 -19.086 1.00 28.57 ? 139 ASN G ND2 1 
ATOM   7798  N  N   . ALA G  1 167 ? 94.238  109.281 -20.154 1.00 23.95 ? 140 ALA G N   1 
ATOM   7799  C  CA  . ALA G  1 167 ? 95.156  108.308 -20.766 1.00 25.30 ? 140 ALA G CA  1 
ATOM   7800  C  C   . ALA G  1 167 ? 94.528  107.518 -21.970 1.00 27.59 ? 140 ALA G C   1 
ATOM   7801  O  O   . ALA G  1 167 ? 95.214  106.731 -22.614 1.00 27.58 ? 140 ALA G O   1 
ATOM   7802  C  CB  . ALA G  1 167 ? 95.747  107.349 -19.697 1.00 24.65 ? 140 ALA G CB  1 
ATOM   7803  N  N   . GLY G  1 168 ? 93.266  107.812 -22.311 1.00 31.64 ? 141 GLY G N   1 
ATOM   7804  C  CA  . GLY G  1 168 ? 92.635  107.208 -23.498 1.00 31.80 ? 141 GLY G CA  1 
ATOM   7805  C  C   . GLY G  1 168 ? 92.406  105.696 -23.369 1.00 31.13 ? 141 GLY G C   1 
ATOM   7806  O  O   . GLY G  1 168 ? 92.250  105.148 -22.238 1.00 28.94 ? 141 GLY G O   1 
ATOM   7807  N  N   A SER G  1 169 ? 92.444  105.015 -24.511 0.50 32.33 ? 142 SER G N   1 
ATOM   7808  N  N   B SER G  1 169 ? 92.383  105.016 -24.516 0.50 31.47 ? 142 SER G N   1 
ATOM   7809  C  CA  A SER G  1 169 ? 92.009  103.611 -24.598 0.50 32.99 ? 142 SER G CA  1 
ATOM   7810  C  CA  B SER G  1 169 ? 91.911  103.617 -24.586 0.50 31.36 ? 142 SER G CA  1 
ATOM   7811  C  C   A SER G  1 169 ? 92.887  102.602 -23.875 0.50 32.05 ? 142 SER G C   1 
ATOM   7812  C  C   B SER G  1 169 ? 92.865  102.598 -23.952 0.50 31.09 ? 142 SER G C   1 
ATOM   7813  O  O   A SER G  1 169 ? 94.042  102.886 -23.538 0.50 31.69 ? 142 SER G O   1 
ATOM   7814  O  O   B SER G  1 169 ? 94.054  102.877 -23.750 0.50 31.13 ? 142 SER G O   1 
ATOM   7815  C  CB  A SER G  1 169 ? 91.851  103.207 -26.056 0.50 32.51 ? 142 SER G CB  1 
ATOM   7816  C  CB  B SER G  1 169 ? 91.599  103.216 -26.032 0.50 29.72 ? 142 SER G CB  1 
ATOM   7817  O  OG  A SER G  1 169 ? 90.818  103.980 -26.613 0.50 33.62 ? 142 SER G OG  1 
ATOM   7818  O  OG  B SER G  1 169 ? 92.783  102.991 -26.771 0.50 27.86 ? 142 SER G OG  1 
ATOM   7819  N  N   . ARG G  1 170 ? 92.320  101.418 -23.639 1.00 30.25 ? 143 ARG G N   1 
ATOM   7820  C  CA  . ARG G  1 170 ? 93.041  100.345 -22.990 1.00 28.37 ? 143 ARG G CA  1 
ATOM   7821  C  C   . ARG G  1 170 ? 93.692  99.455  -24.018 1.00 31.76 ? 143 ARG G C   1 
ATOM   7822  O  O   . ARG G  1 170 ? 93.006  98.753  -24.771 1.00 34.34 ? 143 ARG G O   1 
ATOM   7823  C  CB  . ARG G  1 170 ? 92.073  99.568  -22.107 1.00 29.50 ? 143 ARG G CB  1 
ATOM   7824  C  CG  . ARG G  1 170 ? 91.313  100.504 -21.170 1.00 26.85 ? 143 ARG G CG  1 
ATOM   7825  C  CD  . ARG G  1 170 ? 90.262  99.774  -20.324 1.00 28.61 ? 143 ARG G CD  1 
ATOM   7826  N  NE  . ARG G  1 170 ? 89.578  100.767 -19.487 1.00 27.75 ? 143 ARG G NE  1 
ATOM   7827  C  CZ  . ARG G  1 170 ? 88.869  100.524 -18.385 1.00 30.01 ? 143 ARG G CZ  1 
ATOM   7828  N  NH1 . ARG G  1 170 ? 88.705  99.294  -17.918 1.00 28.60 ? 143 ARG G NH1 1 
ATOM   7829  N  NH2 . ARG G  1 170 ? 88.346  101.549 -17.714 1.00 29.09 ? 143 ARG G NH2 1 
ATOM   7830  N  N   . LEU G  1 171 ? 95.019  99.445  -24.075 1.00 29.12 ? 144 LEU G N   1 
ATOM   7831  C  CA  . LEU G  1 171 ? 95.693  98.722  -25.169 1.00 30.11 ? 144 LEU G CA  1 
ATOM   7832  C  C   . LEU G  1 171 ? 95.905  97.252  -24.876 1.00 30.16 ? 144 LEU G C   1 
ATOM   7833  O  O   . LEU G  1 171 ? 95.825  96.442  -25.778 1.00 33.26 ? 144 LEU G O   1 
ATOM   7834  C  CB  . LEU G  1 171 ? 97.052  99.331  -25.501 1.00 32.00 ? 144 LEU G CB  1 
ATOM   7835  C  CG  . LEU G  1 171 ? 97.043  100.804 -25.914 1.00 32.54 ? 144 LEU G CG  1 
ATOM   7836  C  CD1 . LEU G  1 171 ? 98.484  101.219 -26.198 1.00 33.49 ? 144 LEU G CD1 1 
ATOM   7837  C  CD2 . LEU G  1 171 ? 96.159  101.076 -27.123 1.00 35.80 ? 144 LEU G CD2 1 
ATOM   7838  N  N   . ALA G  1 172 ? 96.261  96.928  -23.642 1.00 29.64 ? 145 ALA G N   1 
ATOM   7839  C  CA  . ALA G  1 172 ? 96.479  95.559  -23.221 1.00 30.58 ? 145 ALA G CA  1 
ATOM   7840  C  C   . ALA G  1 172 ? 96.302  95.516  -21.713 1.00 30.06 ? 145 ALA G C   1 
ATOM   7841  O  O   . ALA G  1 172 ? 96.408  96.554  -21.024 1.00 26.23 ? 145 ALA G O   1 
ATOM   7842  C  CB  . ALA G  1 172 ? 97.867  95.058  -23.662 1.00 29.68 ? 145 ALA G CB  1 
ATOM   7843  N  N   . CYS G  1 173 ? 96.005  94.327  -21.180 1.00 27.15 ? 146 CYS G N   1 
ATOM   7844  C  CA  . CYS G  1 173 ? 95.727  94.167  -19.770 1.00 25.16 ? 146 CYS G CA  1 
ATOM   7845  C  C   . CYS G  1 173 ? 95.904  92.707  -19.372 1.00 25.97 ? 146 CYS G C   1 
ATOM   7846  O  O   . CYS G  1 173 ? 95.975  91.848  -20.236 1.00 26.10 ? 146 CYS G O   1 
ATOM   7847  C  CB  . CYS G  1 173 ? 94.316  94.646  -19.445 1.00 31.92 ? 146 CYS G CB  1 
ATOM   7848  S  SG  . CYS G  1 173 ? 93.033  93.751  -20.377 1.00 35.18 ? 146 CYS G SG  1 
ATOM   7849  N  N   . GLY G  1 174 ? 95.988  92.441  -18.078 1.00 24.68 ? 147 GLY G N   1 
ATOM   7850  C  CA  . GLY G  1 174 ? 96.033  91.080  -17.602 1.00 25.94 ? 147 GLY G CA  1 
ATOM   7851  C  C   . GLY G  1 174 ? 95.641  91.086  -16.165 1.00 24.58 ? 147 GLY G C   1 
ATOM   7852  O  O   . GLY G  1 174 ? 95.706  92.137  -15.526 1.00 25.22 ? 147 GLY G O   1 
ATOM   7853  N  N   . VAL G  1 175 ? 95.213  89.931  -15.640 1.00 21.60 ? 148 VAL G N   1 
ATOM   7854  C  CA  . VAL G  1 175 ? 94.912  89.791  -14.215 1.00 24.81 ? 148 VAL G CA  1 
ATOM   7855  C  C   . VAL G  1 175 ? 96.255  89.575  -13.477 1.00 28.29 ? 148 VAL G C   1 
ATOM   7856  O  O   . VAL G  1 175 ? 97.154  88.847  -13.969 1.00 31.00 ? 148 VAL G O   1 
ATOM   7857  C  CB  . VAL G  1 175 ? 93.879  88.611  -13.931 1.00 23.60 ? 148 VAL G CB  1 
ATOM   7858  C  CG1 . VAL G  1 175 ? 93.500  88.495  -12.473 1.00 23.39 ? 148 VAL G CG1 1 
ATOM   7859  C  CG2 . VAL G  1 175 ? 92.583  88.818  -14.724 1.00 26.41 ? 148 VAL G CG2 1 
ATOM   7860  N  N   . ILE G  1 176 ? 96.352  90.172  -12.295 1.00 26.44 ? 149 ILE G N   1 
ATOM   7861  C  CA  . ILE G  1 176 ? 97.526  90.094  -11.456 1.00 28.56 ? 149 ILE G CA  1 
ATOM   7862  C  C   . ILE G  1 176 ? 97.403  88.821  -10.603 1.00 28.07 ? 149 ILE G C   1 
ATOM   7863  O  O   . ILE G  1 176 ? 96.470  88.713  -9.779  1.00 28.03 ? 149 ILE G O   1 
ATOM   7864  C  CB  . ILE G  1 176 ? 97.655  91.377  -10.589 1.00 26.26 ? 149 ILE G CB  1 
ATOM   7865  C  CG1 . ILE G  1 176 ? 97.778  92.611  -11.517 1.00 27.20 ? 149 ILE G CG1 1 
ATOM   7866  C  CG2 . ILE G  1 176 ? 98.848  91.284  -9.636  1.00 27.82 ? 149 ILE G CG2 1 
ATOM   7867  C  CD1 . ILE G  1 176 ? 97.602  93.963  -10.802 1.00 24.76 ? 149 ILE G CD1 1 
ATOM   7868  N  N   . GLY G  1 177 ? 98.292  87.858  -10.858 1.00 28.42 ? 150 GLY G N   1 
ATOM   7869  C  CA  . GLY G  1 177 ? 98.233  86.547  -10.191 1.00 30.53 ? 150 GLY G CA  1 
ATOM   7870  C  C   . GLY G  1 177 ? 99.357  86.336  -9.211  1.00 34.22 ? 150 GLY G C   1 
ATOM   7871  O  O   . GLY G  1 177 ? 100.388 87.026  -9.314  1.00 30.95 ? 150 GLY G O   1 
ATOM   7872  N  N   . ILE G  1 178 ? 99.154  85.418  -8.253  1.00 32.07 ? 151 ILE G N   1 
ATOM   7873  C  CA  . ILE G  1 178 ? 100.162 85.025  -7.227  1.00 34.13 ? 151 ILE G CA  1 
ATOM   7874  C  C   . ILE G  1 178 ? 101.292 84.310  -7.932  1.00 34.20 ? 151 ILE G C   1 
ATOM   7875  O  O   . ILE G  1 178 ? 101.062 83.466  -8.811  1.00 32.73 ? 151 ILE G O   1 
ATOM   7876  C  CB  . ILE G  1 178 ? 99.578  84.151  -6.096  1.00 39.06 ? 151 ILE G CB  1 
ATOM   7877  C  CG1 . ILE G  1 178 ? 98.583  84.965  -5.287  1.00 43.31 ? 151 ILE G CG1 1 
ATOM   7878  C  CG2 . ILE G  1 178 ? 100.658 83.703  -5.112  1.00 41.20 ? 151 ILE G CG2 1 
ATOM   7879  C  CD1 . ILE G  1 178 ? 97.656  84.138  -4.406  1.00 44.15 ? 151 ILE G CD1 1 
ATOM   7880  N  N   . ALA G  1 179 ? 102.534 84.696  -7.618  1.00 32.88 ? 152 ALA G N   1 
ATOM   7881  C  CA  . ALA G  1 179 ? 103.673 84.083  -8.293  1.00 30.81 ? 152 ALA G CA  1 
ATOM   7882  C  C   . ALA G  1 179 ? 104.524 83.324  -7.289  1.00 30.65 ? 152 ALA G C   1 
ATOM   7883  O  O   . ALA G  1 179 ? 104.411 83.514  -6.069  1.00 28.26 ? 152 ALA G O   1 
ATOM   7884  C  CB  . ALA G  1 179 ? 104.510 85.097  -9.070  1.00 33.82 ? 152 ALA G CB  1 
ATOM   7885  N  N   . GLN G  1 180 ? 105.360 82.447  -7.810  1.00 36.10 ? 153 GLN G N   1 
ATOM   7886  C  CA  . GLN G  1 180 ? 106.234 81.676  -6.927  1.00 47.21 ? 153 GLN G CA  1 
ATOM   7887  C  C   . GLN G  1 180 ? 107.425 82.532  -6.505  1.00 50.50 ? 153 GLN G C   1 
ATOM   7888  O  O   . GLN G  1 180 ? 108.058 83.183  -7.356  1.00 48.50 ? 153 GLN G O   1 
ATOM   7889  C  CB  . GLN G  1 180 ? 106.730 80.425  -7.614  1.00 48.04 ? 153 GLN G CB  1 
ATOM   7890  C  CG  . GLN G  1 180 ? 107.408 79.479  -6.647  1.00 51.58 ? 153 GLN G CG  1 
ATOM   7891  C  CD  . GLN G  1 180 ? 107.852 78.231  -7.350  1.00 54.12 ? 153 GLN G CD  1 
ATOM   7892  O  OE1 . GLN G  1 180 ? 108.191 78.267  -8.532  1.00 54.45 ? 153 GLN G OE1 1 
ATOM   7893  N  NE2 . GLN G  1 180 ? 107.829 77.110  -6.640  1.00 53.81 ? 153 GLN G NE2 1 
ATOM   7894  O  OXT . GLN G  1 180 ? 107.753 82.584  -5.309  1.00 53.81 ? 153 GLN G OXT 1 
ATOM   7895  N  N   . MET H  1 27  ? 86.156  90.153  1.942   1.00 55.58 ? 0   MET H N   1 
ATOM   7896  C  CA  . MET H  1 27  ? 85.275  91.123  1.221   1.00 59.18 ? 0   MET H CA  1 
ATOM   7897  C  C   . MET H  1 27  ? 84.824  90.627  -0.182  1.00 59.02 ? 0   MET H C   1 
ATOM   7898  O  O   . MET H  1 27  ? 83.685  90.907  -0.583  1.00 58.76 ? 0   MET H O   1 
ATOM   7899  C  CB  . MET H  1 27  ? 85.907  92.523  1.152   1.00 51.00 ? 0   MET H CB  1 
ATOM   7900  N  N   . ALA H  1 28  ? 85.680  89.890  -0.909  1.00 56.20 ? 1   ALA H N   1 
ATOM   7901  C  CA  . ALA H  1 28  ? 85.323  89.406  -2.266  1.00 52.55 ? 1   ALA H CA  1 
ATOM   7902  C  C   . ALA H  1 28  ? 84.186  88.363  -2.237  1.00 45.48 ? 1   ALA H C   1 
ATOM   7903  O  O   . ALA H  1 28  ? 84.224  87.442  -1.442  1.00 45.60 ? 1   ALA H O   1 
ATOM   7904  C  CB  . ALA H  1 28  ? 86.539  88.851  -2.998  1.00 51.71 ? 1   ALA H CB  1 
ATOM   7905  N  N   . THR H  1 29  ? 83.170  88.536  -3.081  1.00 38.98 ? 2   THR H N   1 
ATOM   7906  C  CA  . THR H  1 29  ? 82.084  87.570  -3.129  1.00 36.00 ? 2   THR H CA  1 
ATOM   7907  C  C   . THR H  1 29  ? 81.815  87.049  -4.556  1.00 34.00 ? 2   THR H C   1 
ATOM   7908  O  O   . THR H  1 29  ? 80.995  86.155  -4.714  1.00 32.18 ? 2   THR H O   1 
ATOM   7909  C  CB  . THR H  1 29  ? 80.753  88.123  -2.578  1.00 36.64 ? 2   THR H CB  1 
ATOM   7910  O  OG1 . THR H  1 29  ? 80.314  89.160  -3.444  1.00 36.73 ? 2   THR H OG1 1 
ATOM   7911  C  CG2 . THR H  1 29  ? 80.863  88.617  -1.120  1.00 37.93 ? 2   THR H CG2 1 
ATOM   7912  N  N   . LYS H  1 30  ? 82.440  87.637  -5.576  1.00 26.80 ? 3   LYS H N   1 
ATOM   7913  C  CA  . LYS H  1 30  ? 82.332  87.132  -6.937  1.00 29.05 ? 3   LYS H CA  1 
ATOM   7914  C  C   . LYS H  1 30  ? 83.694  87.177  -7.565  1.00 30.05 ? 3   LYS H C   1 
ATOM   7915  O  O   . LYS H  1 30  ? 84.498  88.102  -7.309  1.00 29.59 ? 3   LYS H O   1 
ATOM   7916  C  CB  . LYS H  1 30  ? 81.367  87.946  -7.803  1.00 32.74 ? 3   LYS H CB  1 
ATOM   7917  C  CG  . LYS H  1 30  ? 79.907  87.869  -7.331  1.00 39.05 ? 3   LYS H CG  1 
ATOM   7918  C  CD  . LYS H  1 30  ? 79.147  89.142  -7.644  1.00 45.20 ? 3   LYS H CD  1 
ATOM   7919  C  CE  . LYS H  1 30  ? 78.737  89.211  -9.112  1.00 50.41 ? 3   LYS H CE  1 
ATOM   7920  N  NZ  . LYS H  1 30  ? 77.318  88.782  -9.305  1.00 52.19 ? 3   LYS H NZ  1 
ATOM   7921  N  N   . ALA H  1 31  ? 83.953  86.197  -8.404  1.00 26.39 ? 4   ALA H N   1 
ATOM   7922  C  CA  . ALA H  1 31  ? 85.214  86.137  -9.143  1.00 24.59 ? 4   ALA H CA  1 
ATOM   7923  C  C   . ALA H  1 31  ? 84.903  85.543  -10.511 1.00 25.73 ? 4   ALA H C   1 
ATOM   7924  O  O   . ALA H  1 31  ? 83.785  85.006  -10.745 1.00 25.79 ? 4   ALA H O   1 
ATOM   7925  C  CB  . ALA H  1 31  ? 86.226  85.305  -8.390  1.00 23.14 ? 4   ALA H CB  1 
ATOM   7926  N  N   . VAL H  1 32  ? 85.826  85.710  -11.446 1.00 24.42 ? 5   VAL H N   1 
ATOM   7927  C  CA  . VAL H  1 32  ? 85.607  85.244  -12.801 1.00 24.89 ? 5   VAL H CA  1 
ATOM   7928  C  C   . VAL H  1 32  ? 86.915  84.758  -13.395 1.00 25.85 ? 5   VAL H C   1 
ATOM   7929  O  O   . VAL H  1 32  ? 87.984  85.184  -12.958 1.00 26.29 ? 5   VAL H O   1 
ATOM   7930  C  CB  . VAL H  1 32  ? 84.897  86.324  -13.671 1.00 28.21 ? 5   VAL H CB  1 
ATOM   7931  C  CG1 . VAL H  1 32  ? 85.830  87.472  -14.013 1.00 29.32 ? 5   VAL H CG1 1 
ATOM   7932  C  CG2 . VAL H  1 32  ? 84.297  85.716  -14.928 1.00 26.68 ? 5   VAL H CG2 1 
ATOM   7933  N  N   . CYS H  1 33  ? 86.841  83.886  -14.400 1.00 24.11 ? 6   CYS H N   1 
ATOM   7934  C  CA  . CYS H  1 33  ? 88.046  83.380  -15.036 1.00 23.85 ? 6   CYS H CA  1 
ATOM   7935  C  C   . CYS H  1 33  ? 87.802  83.148  -16.502 1.00 24.58 ? 6   CYS H C   1 
ATOM   7936  O  O   . CYS H  1 33  ? 86.823  82.471  -16.882 1.00 25.11 ? 6   CYS H O   1 
ATOM   7937  C  CB  . CYS H  1 33  ? 88.515  82.099  -14.319 1.00 24.97 ? 6   CYS H CB  1 
ATOM   7938  S  SG  . CYS H  1 33  ? 89.996  81.404  -15.085 1.00 30.62 ? 6   CYS H SG  1 
ATOM   7939  N  N   . VAL H  1 34  ? 88.682  83.692  -17.339 1.00 20.89 ? 7   VAL H N   1 
ATOM   7940  C  CA  . VAL H  1 34  ? 88.601  83.511  -18.778 1.00 23.84 ? 7   VAL H CA  1 
ATOM   7941  C  C   . VAL H  1 34  ? 89.649  82.473  -19.175 1.00 29.19 ? 7   VAL H C   1 
ATOM   7942  O  O   . VAL H  1 34  ? 90.869  82.695  -18.977 1.00 24.89 ? 7   VAL H O   1 
ATOM   7943  C  CB  . VAL H  1 34  ? 88.871  84.823  -19.538 1.00 27.28 ? 7   VAL H CB  1 
ATOM   7944  C  CG1 . VAL H  1 34  ? 88.874  84.582  -21.047 1.00 30.38 ? 7   VAL H CG1 1 
ATOM   7945  C  CG2 . VAL H  1 34  ? 87.844  85.907  -19.136 1.00 28.34 ? 7   VAL H CG2 1 
ATOM   7946  N  N   . LEU H  1 35  ? 89.199  81.341  -19.719 1.00 25.27 ? 8   LEU H N   1 
ATOM   7947  C  CA  . LEU H  1 35  ? 90.130  80.245  -20.019 1.00 26.99 ? 8   LEU H CA  1 
ATOM   7948  C  C   . LEU H  1 35  ? 90.529  80.321  -21.470 1.00 27.29 ? 8   LEU H C   1 
ATOM   7949  O  O   . LEU H  1 35  ? 89.664  80.455  -22.378 1.00 27.15 ? 8   LEU H O   1 
ATOM   7950  C  CB  . LEU H  1 35  ? 89.507  78.845  -19.651 1.00 28.00 ? 8   LEU H CB  1 
ATOM   7951  C  CG  . LEU H  1 35  ? 89.445  78.737  -18.119 1.00 30.86 ? 8   LEU H CG  1 
ATOM   7952  C  CD1 . LEU H  1 35  ? 88.019  78.914  -17.643 1.00 37.22 ? 8   LEU H CD1 1 
ATOM   7953  C  CD2 . LEU H  1 35  ? 90.020  77.472  -17.552 1.00 33.46 ? 8   LEU H CD2 1 
ATOM   7954  N  N   . LYS H  1 36  ? 91.845  80.256  -21.705 1.00 26.71 ? 9   LYS H N   1 
ATOM   7955  C  CA  . LYS H  1 36  ? 92.383  80.245  -23.065 1.00 28.45 ? 9   LYS H CA  1 
ATOM   7956  C  C   . LYS H  1 36  ? 93.597  79.339  -23.087 1.00 26.86 ? 9   LYS H C   1 
ATOM   7957  O  O   . LYS H  1 36  ? 94.232  79.134  -22.061 1.00 26.41 ? 9   LYS H O   1 
ATOM   7958  C  CB  . LYS H  1 36  ? 92.805  81.671  -23.482 1.00 34.84 ? 9   LYS H CB  1 
ATOM   7959  C  CG  . LYS H  1 36  ? 91.634  82.603  -23.794 1.00 43.45 ? 9   LYS H CG  1 
ATOM   7960  C  CD  . LYS H  1 36  ? 91.978  83.614  -24.891 1.00 53.76 ? 9   LYS H CD  1 
ATOM   7961  C  CE  . LYS H  1 36  ? 90.784  84.501  -25.219 1.00 57.57 ? 9   LYS H CE  1 
ATOM   7962  N  NZ  . LYS H  1 36  ? 90.545  85.388  -24.046 1.00 59.46 ? 9   LYS H NZ  1 
ATOM   7963  N  N   . GLY H  1 37  ? 93.883  78.760  -24.244 1.00 32.56 ? 10  GLY H N   1 
ATOM   7964  C  CA  . GLY H  1 37  ? 95.122  78.002  -24.400 1.00 36.15 ? 10  GLY H CA  1 
ATOM   7965  C  C   . GLY H  1 37  ? 95.665  78.123  -25.812 1.00 39.77 ? 10  GLY H C   1 
ATOM   7966  O  O   . GLY H  1 37  ? 95.285  79.034  -26.560 1.00 37.38 ? 10  GLY H O   1 
ATOM   7967  N  N   . ASP H  1 38  ? 96.540  77.190  -26.183 1.00 40.39 ? 11  ASP H N   1 
ATOM   7968  C  CA  . ASP H  1 38  ? 97.139  77.177  -27.530 1.00 46.00 ? 11  ASP H CA  1 
ATOM   7969  C  C   . ASP H  1 38  ? 96.192  76.699  -28.607 1.00 49.77 ? 11  ASP H C   1 
ATOM   7970  O  O   . ASP H  1 38  ? 96.385  77.027  -29.788 1.00 49.18 ? 11  ASP H O   1 
ATOM   7971  C  CB  . ASP H  1 38  ? 98.337  76.234  -27.575 1.00 52.48 ? 11  ASP H CB  1 
ATOM   7972  C  CG  . ASP H  1 38  ? 99.480  76.692  -26.701 1.00 56.82 ? 11  ASP H CG  1 
ATOM   7973  O  OD1 . ASP H  1 38  ? 99.649  77.922  -26.512 1.00 57.76 ? 11  ASP H OD1 1 
ATOM   7974  O  OD2 . ASP H  1 38  ? 100.226 75.805  -26.226 1.00 65.19 ? 11  ASP H OD2 1 
ATOM   7975  N  N   . GLY H  1 39  ? 95.220  75.866  -28.214 1.00 45.31 ? 12  GLY H N   1 
ATOM   7976  C  CA  . GLY H  1 39  ? 94.323  75.217  -29.165 1.00 39.20 ? 12  GLY H CA  1 
ATOM   7977  C  C   . GLY H  1 39  ? 92.957  75.867  -29.140 1.00 39.28 ? 12  GLY H C   1 
ATOM   7978  O  O   . GLY H  1 39  ? 92.832  77.040  -28.758 1.00 39.07 ? 12  GLY H O   1 
ATOM   7979  N  N   . PRO H  1 40  ? 91.916  75.114  -29.509 1.00 37.68 ? 13  PRO H N   1 
ATOM   7980  C  CA  . PRO H  1 40  ? 90.598  75.753  -29.651 1.00 37.37 ? 13  PRO H CA  1 
ATOM   7981  C  C   . PRO H  1 40  ? 89.777  75.810  -28.333 1.00 34.57 ? 13  PRO H C   1 
ATOM   7982  O  O   . PRO H  1 40  ? 88.651  76.296  -28.347 1.00 33.56 ? 13  PRO H O   1 
ATOM   7983  C  CB  . PRO H  1 40  ? 89.895  74.852  -30.667 1.00 35.67 ? 13  PRO H CB  1 
ATOM   7984  C  CG  . PRO H  1 40  ? 90.481  73.477  -30.415 1.00 40.78 ? 13  PRO H CG  1 
ATOM   7985  C  CD  . PRO H  1 40  ? 91.861  73.659  -29.771 1.00 39.04 ? 13  PRO H CD  1 
ATOM   7986  N  N   . VAL H  1 41  ? 90.322  75.308  -27.227 1.00 34.13 ? 14  VAL H N   1 
ATOM   7987  C  CA  . VAL H  1 41  ? 89.562  75.245  -25.964 1.00 31.93 ? 14  VAL H CA  1 
ATOM   7988  C  C   . VAL H  1 41  ? 89.442  76.652  -25.333 1.00 32.78 ? 14  VAL H C   1 
ATOM   7989  O  O   . VAL H  1 41  ? 90.444  77.348  -25.106 1.00 30.71 ? 14  VAL H O   1 
ATOM   7990  C  CB  . VAL H  1 41  ? 90.209  74.245  -24.973 1.00 32.59 ? 14  VAL H CB  1 
ATOM   7991  C  CG1 . VAL H  1 41  ? 89.489  74.252  -23.613 1.00 30.39 ? 14  VAL H CG1 1 
ATOM   7992  C  CG2 . VAL H  1 41  ? 90.187  72.823  -25.566 1.00 32.41 ? 14  VAL H CG2 1 
ATOM   7993  N  N   . GLN H  1 42  ? 88.225  77.069  -25.001 1.00 28.70 ? 15  GLN H N   1 
ATOM   7994  C  CA  . GLN H  1 42  ? 88.092  78.346  -24.330 1.00 29.50 ? 15  GLN H CA  1 
ATOM   7995  C  C   . GLN H  1 42  ? 86.790  78.377  -23.574 1.00 32.69 ? 15  GLN H C   1 
ATOM   7996  O  O   . GLN H  1 42  ? 85.824  77.712  -23.965 1.00 28.22 ? 15  GLN H O   1 
ATOM   7997  C  CB  . GLN H  1 42  ? 88.133  79.485  -25.356 1.00 32.92 ? 15  GLN H CB  1 
ATOM   7998  C  CG  . GLN H  1 42  ? 87.029  79.454  -26.396 1.00 40.31 ? 15  GLN H CG  1 
ATOM   7999  C  CD  . GLN H  1 42  ? 87.309  80.373  -27.578 1.00 47.52 ? 15  GLN H CD  1 
ATOM   8000  O  OE1 . GLN H  1 42  ? 86.567  80.381  -28.556 1.00 53.54 ? 15  GLN H OE1 1 
ATOM   8001  N  NE2 . GLN H  1 42  ? 88.392  81.123  -27.506 1.00 55.10 ? 15  GLN H NE2 1 
ATOM   8002  N  N   . GLY H  1 43  ? 86.756  79.179  -22.522 1.00 30.53 ? 16  GLY H N   1 
ATOM   8003  C  CA  . GLY H  1 43  ? 85.515  79.397  -21.809 1.00 31.46 ? 16  GLY H CA  1 
ATOM   8004  C  C   . GLY H  1 43  ? 85.592  80.482  -20.757 1.00 31.74 ? 16  GLY H C   1 
ATOM   8005  O  O   . GLY H  1 43  ? 86.636  81.141  -20.591 1.00 28.98 ? 16  GLY H O   1 
ATOM   8006  N  N   . ILE H  1 44  ? 84.473  80.663  -20.071 1.00 26.24 ? 17  ILE H N   1 
ATOM   8007  C  CA  . ILE H  1 44  ? 84.348  81.645  -19.011 1.00 25.92 ? 17  ILE H CA  1 
ATOM   8008  C  C   . ILE H  1 44  ? 83.731  80.929  -17.834 1.00 25.25 ? 17  ILE H C   1 
ATOM   8009  O  O   . ILE H  1 44  ? 82.674  80.264  -17.976 1.00 25.45 ? 17  ILE H O   1 
ATOM   8010  C  CB  . ILE H  1 44  ? 83.467  82.835  -19.429 1.00 25.94 ? 17  ILE H CB  1 
ATOM   8011  C  CG1 . ILE H  1 44  ? 84.127  83.609  -20.582 1.00 30.02 ? 17  ILE H CG1 1 
ATOM   8012  C  CG2 . ILE H  1 44  ? 83.199  83.760  -18.218 1.00 24.73 ? 17  ILE H CG2 1 
ATOM   8013  C  CD1 . ILE H  1 44  ? 83.210  84.665  -21.206 1.00 34.48 ? 17  ILE H CD1 1 
ATOM   8014  N  N   . ILE H  1 45  ? 84.410  80.984  -16.696 1.00 20.91 ? 18  ILE H N   1 
ATOM   8015  C  CA  . ILE H  1 45  ? 83.903  80.414  -15.462 1.00 21.40 ? 18  ILE H CA  1 
ATOM   8016  C  C   . ILE H  1 45  ? 83.673  81.499  -14.427 1.00 25.02 ? 18  ILE H C   1 
ATOM   8017  O  O   . ILE H  1 45  ? 84.586  82.343  -14.164 1.00 23.04 ? 18  ILE H O   1 
ATOM   8018  C  CB  . ILE H  1 45  ? 84.870  79.332  -14.937 1.00 21.59 ? 18  ILE H CB  1 
ATOM   8019  C  CG1 . ILE H  1 45  ? 85.004  78.225  -16.001 1.00 24.65 ? 18  ILE H CG1 1 
ATOM   8020  C  CG2 . ILE H  1 45  ? 84.468  78.805  -13.570 1.00 21.68 ? 18  ILE H CG2 1 
ATOM   8021  C  CD1 . ILE H  1 45  ? 83.717  77.421  -16.236 1.00 26.00 ? 18  ILE H CD1 1 
ATOM   8022  N  N   . ASN H  1 46  ? 82.475  81.490  -13.843 1.00 20.98 ? 19  ASN H N   1 
ATOM   8023  C  CA  . ASN H  1 46  ? 82.111  82.408  -12.733 1.00 22.27 ? 19  ASN H CA  1 
ATOM   8024  C  C   . ASN H  1 46  ? 82.154  81.767  -11.402 1.00 24.62 ? 19  ASN H C   1 
ATOM   8025  O  O   . ASN H  1 46  ? 81.945  80.532  -11.290 1.00 24.31 ? 19  ASN H O   1 
ATOM   8026  C  CB  . ASN H  1 46  ? 80.694  82.933  -12.973 1.00 24.82 ? 19  ASN H CB  1 
ATOM   8027  C  CG  . ASN H  1 46  ? 80.512  83.451  -14.357 1.00 30.24 ? 19  ASN H CG  1 
ATOM   8028  O  OD1 . ASN H  1 46  ? 80.031  82.728  -15.277 1.00 34.98 ? 19  ASN H OD1 1 
ATOM   8029  N  ND2 . ASN H  1 46  ? 80.908  84.698  -14.554 1.00 25.92 ? 19  ASN H ND2 1 
ATOM   8030  N  N   . PHE H  1 47  ? 82.414  82.564  -10.361 1.00 21.92 ? 20  PHE H N   1 
ATOM   8031  C  CA  . PHE H  1 47  ? 82.436  82.101  -8.995  1.00 24.19 ? 20  PHE H CA  1 
ATOM   8032  C  C   . PHE H  1 47  ? 81.602  83.034  -8.138  1.00 26.73 ? 20  PHE H C   1 
ATOM   8033  O  O   . PHE H  1 47  ? 81.675  84.271  -8.310  1.00 26.51 ? 20  PHE H O   1 
ATOM   8034  C  CB  . PHE H  1 47  ? 83.863  82.097  -8.399  1.00 24.96 ? 20  PHE H CB  1 
ATOM   8035  C  CG  . PHE H  1 47  ? 84.846  81.242  -9.144  1.00 25.22 ? 20  PHE H CG  1 
ATOM   8036  C  CD1 . PHE H  1 47  ? 85.434  81.688  -10.333 1.00 25.71 ? 20  PHE H CD1 1 
ATOM   8037  C  CD2 . PHE H  1 47  ? 85.210  79.995  -8.631  1.00 24.86 ? 20  PHE H CD2 1 
ATOM   8038  C  CE1 . PHE H  1 47  ? 86.361  80.893  -11.007 1.00 23.54 ? 20  PHE H CE1 1 
ATOM   8039  C  CE2 . PHE H  1 47  ? 86.107  79.177  -9.321  1.00 25.24 ? 20  PHE H CE2 1 
ATOM   8040  C  CZ  . PHE H  1 47  ? 86.693  79.648  -10.501 1.00 24.94 ? 20  PHE H CZ  1 
ATOM   8041  N  N   . GLU H  1 48  ? 80.840  82.463  -7.193  1.00 26.21 ? 21  GLU H N   1 
ATOM   8042  C  CA  . GLU H  1 48  ? 80.058  83.297  -6.284  1.00 29.29 ? 21  GLU H CA  1 
ATOM   8043  C  C   . GLU H  1 48  ? 80.078  82.749  -4.895  1.00 28.71 ? 21  GLU H C   1 
ATOM   8044  O  O   . GLU H  1 48  ? 79.822  81.550  -4.669  1.00 29.49 ? 21  GLU H O   1 
ATOM   8045  C  CB  . GLU H  1 48  ? 78.606  83.488  -6.769  1.00 31.15 ? 21  GLU H CB  1 
ATOM   8046  C  CG  . GLU H  1 48  ? 77.817  84.477  -5.898  1.00 41.57 ? 21  GLU H CG  1 
ATOM   8047  C  CD  . GLU H  1 48  ? 76.319  84.422  -6.136  1.00 53.74 ? 21  GLU H CD  1 
ATOM   8048  O  OE1 . GLU H  1 48  ? 75.896  84.836  -7.238  1.00 52.07 ? 21  GLU H OE1 1 
ATOM   8049  O  OE2 . GLU H  1 48  ? 75.569  83.949  -5.229  1.00 60.31 ? 21  GLU H OE2 1 
ATOM   8050  N  N   . GLN H  1 49  ? 80.367  83.600  -3.921  1.00 29.45 ? 22  GLN H N   1 
ATOM   8051  C  CA  . GLN H  1 49  ? 80.346  83.122  -2.546  1.00 31.91 ? 22  GLN H CA  1 
ATOM   8052  C  C   . GLN H  1 49  ? 79.793  84.206  -1.632  1.00 37.31 ? 22  GLN H C   1 
ATOM   8053  O  O   . GLN H  1 49  ? 80.517  85.101  -1.225  1.00 40.22 ? 22  GLN H O   1 
ATOM   8054  C  CB  . GLN H  1 49  ? 81.727  82.702  -2.120  1.00 30.75 ? 22  GLN H CB  1 
ATOM   8055  C  CG  . GLN H  1 49  ? 81.755  82.127  -0.710  1.00 33.30 ? 22  GLN H CG  1 
ATOM   8056  C  CD  . GLN H  1 49  ? 83.173  82.043  -0.155  1.00 35.09 ? 22  GLN H CD  1 
ATOM   8057  O  OE1 . GLN H  1 49  ? 84.061  82.800  -0.559  1.00 34.33 ? 22  GLN H OE1 1 
ATOM   8058  N  NE2 . GLN H  1 49  ? 83.393  81.106  0.757   1.00 36.09 ? 22  GLN H NE2 1 
ATOM   8059  N  N   . LYS H  1 50  ? 78.507  84.122  -1.329  1.00 40.04 ? 23  LYS H N   1 
ATOM   8060  C  CA  . LYS H  1 50  ? 77.813  85.161  -0.553  1.00 45.57 ? 23  LYS H CA  1 
ATOM   8061  C  C   . LYS H  1 50  ? 78.190  85.183  0.942   1.00 47.48 ? 23  LYS H C   1 
ATOM   8062  O  O   . LYS H  1 50  ? 78.327  86.250  1.525   1.00 52.59 ? 23  LYS H O   1 
ATOM   8063  C  CB  . LYS H  1 50  ? 76.294  85.068  -0.773  1.00 48.19 ? 23  LYS H CB  1 
ATOM   8064  C  CG  . LYS H  1 50  ? 75.920  85.524  -2.174  1.00 52.94 ? 23  LYS H CG  1 
ATOM   8065  C  CD  . LYS H  1 50  ? 74.431  85.630  -2.447  1.00 56.85 ? 23  LYS H CD  1 
ATOM   8066  C  CE  . LYS H  1 50  ? 74.220  86.619  -3.585  1.00 59.23 ? 23  LYS H CE  1 
ATOM   8067  N  NZ  . LYS H  1 50  ? 72.792  87.003  -3.754  1.00 61.22 ? 23  LYS H NZ  1 
ATOM   8068  N  N   . GLU H  1 51  ? 78.382  84.019  1.552   1.00 47.48 ? 24  GLU H N   1 
ATOM   8069  C  CA  . GLU H  1 51  ? 78.782  83.931  2.973   1.00 47.99 ? 24  GLU H CA  1 
ATOM   8070  C  C   . GLU H  1 51  ? 80.216  83.471  3.017   1.00 46.58 ? 24  GLU H C   1 
ATOM   8071  O  O   . GLU H  1 51  ? 80.548  82.522  2.334   1.00 43.87 ? 24  GLU H O   1 
ATOM   8072  C  CB  . GLU H  1 51  ? 77.906  82.896  3.716   1.00 47.79 ? 24  GLU H CB  1 
ATOM   8073  C  CG  . GLU H  1 51  ? 76.459  83.326  3.979   1.00 58.17 ? 24  GLU H CG  1 
ATOM   8074  C  CD  . GLU H  1 51  ? 76.360  84.543  4.908   1.00 66.63 ? 24  GLU H CD  1 
ATOM   8075  O  OE1 . GLU H  1 51  ? 77.120  84.611  5.908   1.00 68.40 ? 24  GLU H OE1 1 
ATOM   8076  O  OE2 . GLU H  1 51  ? 75.534  85.449  4.644   1.00 65.90 ? 24  GLU H OE2 1 
ATOM   8077  N  N   . SER H  1 52  ? 81.077  84.078  3.834   1.00 46.56 ? 25  SER H N   1 
ATOM   8078  C  CA  . SER H  1 52  ? 82.511  83.714  3.747   1.00 48.60 ? 25  SER H CA  1 
ATOM   8079  C  C   . SER H  1 52  ? 82.871  82.333  4.330   1.00 49.41 ? 25  SER H C   1 
ATOM   8080  O  O   . SER H  1 52  ? 83.859  81.714  3.934   1.00 49.59 ? 25  SER H O   1 
ATOM   8081  C  CB  . SER H  1 52  ? 83.417  84.820  4.304   1.00 55.11 ? 25  SER H CB  1 
ATOM   8082  O  OG  . SER H  1 52  ? 83.177  85.040  5.680   1.00 59.81 ? 25  SER H OG  1 
ATOM   8083  N  N   . ASN H  1 53  ? 82.062  81.840  5.257   1.00 48.20 ? 26  ASN H N   1 
ATOM   8084  C  CA  . ASN H  1 53  ? 82.206  80.467  5.711   1.00 56.27 ? 26  ASN H CA  1 
ATOM   8085  C  C   . ASN H  1 53  ? 81.486  79.493  4.739   1.00 56.29 ? 26  ASN H C   1 
ATOM   8086  O  O   . ASN H  1 53  ? 81.436  78.284  4.977   1.00 60.96 ? 26  ASN H O   1 
ATOM   8087  C  CB  . ASN H  1 53  ? 81.638  80.329  7.141   1.00 55.35 ? 26  ASN H CB  1 
ATOM   8088  N  N   . GLY H  1 54  ? 80.923  80.026  3.655   1.00 49.39 ? 27  GLY H N   1 
ATOM   8089  C  CA  . GLY H  1 54  ? 79.940  79.288  2.866   1.00 41.77 ? 27  GLY H CA  1 
ATOM   8090  C  C   . GLY H  1 54  ? 80.472  78.625  1.610   1.00 37.50 ? 27  GLY H C   1 
ATOM   8091  O  O   . GLY H  1 54  ? 81.632  78.815  1.218   1.00 34.08 ? 27  GLY H O   1 
ATOM   8092  N  N   . PRO H  1 55  ? 79.623  77.822  0.956   1.00 37.16 ? 28  PRO H N   1 
ATOM   8093  C  CA  . PRO H  1 55  ? 80.080  77.231  -0.308  1.00 35.86 ? 28  PRO H CA  1 
ATOM   8094  C  C   . PRO H  1 55  ? 80.241  78.263  -1.454  1.00 32.86 ? 28  PRO H C   1 
ATOM   8095  O  O   . PRO H  1 55  ? 79.675  79.384  -1.403  1.00 33.31 ? 28  PRO H O   1 
ATOM   8096  C  CB  . PRO H  1 55  ? 78.977  76.212  -0.634  1.00 38.93 ? 28  PRO H CB  1 
ATOM   8097  C  CG  . PRO H  1 55  ? 77.770  76.703  0.105   1.00 41.75 ? 28  PRO H CG  1 
ATOM   8098  C  CD  . PRO H  1 55  ? 78.323  77.271  1.387   1.00 39.31 ? 28  PRO H CD  1 
ATOM   8099  N  N   . VAL H  1 56  ? 81.028  77.872  -2.449  1.00 30.44 ? 29  VAL H N   1 
ATOM   8100  C  CA  . VAL H  1 56  ? 81.256  78.658  -3.662  1.00 28.78 ? 29  VAL H CA  1 
ATOM   8101  C  C   . VAL H  1 56  ? 80.522  77.997  -4.831  1.00 29.08 ? 29  VAL H C   1 
ATOM   8102  O  O   . VAL H  1 56  ? 80.743  76.819  -5.097  1.00 30.72 ? 29  VAL H O   1 
ATOM   8103  C  CB  . VAL H  1 56  ? 82.772  78.748  -3.987  1.00 28.23 ? 29  VAL H CB  1 
ATOM   8104  C  CG1 . VAL H  1 56  ? 83.046  79.634  -5.231  1.00 26.52 ? 29  VAL H CG1 1 
ATOM   8105  C  CG2 . VAL H  1 56  ? 83.539  79.224  -2.747  1.00 29.25 ? 29  VAL H CG2 1 
ATOM   8106  N  N   . LYS H  1 57  ? 79.684  78.765  -5.525  1.00 28.10 ? 30  LYS H N   1 
ATOM   8107  C  CA  . LYS H  1 57  ? 79.067  78.305  -6.794  1.00 29.95 ? 30  LYS H CA  1 
ATOM   8108  C  C   . LYS H  1 57  ? 80.051  78.559  -7.910  1.00 27.67 ? 30  LYS H C   1 
ATOM   8109  O  O   . LYS H  1 57  ? 80.611  79.666  -7.993  1.00 24.92 ? 30  LYS H O   1 
ATOM   8110  C  CB  . LYS H  1 57  ? 77.824  79.146  -7.120  1.00 27.59 ? 30  LYS H CB  1 
ATOM   8111  C  CG  . LYS H  1 57  ? 76.760  79.091  -6.030  1.00 36.32 ? 30  LYS H CG  1 
ATOM   8112  C  CD  . LYS H  1 57  ? 75.510  79.824  -6.515  1.00 40.07 ? 30  LYS H CD  1 
ATOM   8113  C  CE  . LYS H  1 57  ? 74.654  80.353  -5.374  1.00 48.92 ? 30  LYS H CE  1 
ATOM   8114  N  NZ  . LYS H  1 57  ? 73.658  81.291  -5.993  1.00 54.64 ? 30  LYS H NZ  1 
ATOM   8115  N  N   . VAL H  1 58  ? 80.254  77.571  -8.776  1.00 25.81 ? 31  VAL H N   1 
ATOM   8116  C  CA  . VAL H  1 58  ? 81.162  77.699  -9.907  1.00 24.27 ? 31  VAL H CA  1 
ATOM   8117  C  C   . VAL H  1 58  ? 80.377  77.320  -11.157 1.00 25.43 ? 31  VAL H C   1 
ATOM   8118  O  O   . VAL H  1 58  ? 79.801  76.216  -11.238 1.00 25.61 ? 31  VAL H O   1 
ATOM   8119  C  CB  . VAL H  1 58  ? 82.347  76.719  -9.738  1.00 25.43 ? 31  VAL H CB  1 
ATOM   8120  C  CG1 . VAL H  1 58  ? 83.380  76.915  -10.833 1.00 23.02 ? 31  VAL H CG1 1 
ATOM   8121  C  CG2 . VAL H  1 58  ? 83.003  76.872  -8.352  1.00 26.25 ? 31  VAL H CG2 1 
ATOM   8122  N  N   . TRP H  1 59  ? 80.329  78.193  -12.142 1.00 23.47 ? 32  TRP H N   1 
ATOM   8123  C  CA  . TRP H  1 59  ? 79.513  77.870  -13.310 1.00 23.34 ? 32  TRP H CA  1 
ATOM   8124  C  C   . TRP H  1 59  ? 79.953  78.632  -14.508 1.00 22.72 ? 32  TRP H C   1 
ATOM   8125  O  O   . TRP H  1 59  ? 80.532  79.740  -14.400 1.00 24.66 ? 32  TRP H O   1 
ATOM   8126  C  CB  . TRP H  1 59  ? 78.003  78.147  -13.055 1.00 25.19 ? 32  TRP H CB  1 
ATOM   8127  C  CG  . TRP H  1 59  ? 77.621  79.629  -13.139 1.00 24.38 ? 32  TRP H CG  1 
ATOM   8128  C  CD1 . TRP H  1 59  ? 77.093  80.303  -14.193 1.00 25.96 ? 32  TRP H CD1 1 
ATOM   8129  C  CD2 . TRP H  1 59  ? 77.778  80.565  -12.090 1.00 25.03 ? 32  TRP H CD2 1 
ATOM   8130  N  NE1 . TRP H  1 59  ? 76.898  81.633  -13.851 1.00 27.20 ? 32  TRP H NE1 1 
ATOM   8131  C  CE2 . TRP H  1 59  ? 77.306  81.807  -12.556 1.00 26.93 ? 32  TRP H CE2 1 
ATOM   8132  C  CE3 . TRP H  1 59  ? 78.266  80.465  -10.776 1.00 28.42 ? 32  TRP H CE3 1 
ATOM   8133  C  CZ2 . TRP H  1 59  ? 77.306  82.959  -11.763 1.00 32.44 ? 32  TRP H CZ2 1 
ATOM   8134  C  CZ3 . TRP H  1 59  ? 78.269  81.630  -9.969  1.00 35.69 ? 32  TRP H CZ3 1 
ATOM   8135  C  CH2 . TRP H  1 59  ? 77.793  82.863  -10.483 1.00 33.82 ? 32  TRP H CH2 1 
ATOM   8136  N  N   . GLY H  1 60  ? 79.671  78.078  -15.669 1.00 22.95 ? 33  GLY H N   1 
ATOM   8137  C  CA  . GLY H  1 60  ? 80.049  78.707  -16.916 1.00 22.53 ? 33  GLY H CA  1 
ATOM   8138  C  C   . GLY H  1 60  ? 80.032  77.656  -17.987 1.00 25.89 ? 33  GLY H C   1 
ATOM   8139  O  O   . GLY H  1 60  ? 79.326  76.640  -17.867 1.00 26.00 ? 33  GLY H O   1 
ATOM   8140  N  N   . SER H  1 61  ? 80.795  77.884  -19.032 1.00 24.27 ? 34  SER H N   1 
ATOM   8141  C  CA  . SER H  1 61  ? 80.830  76.973  -20.144 1.00 25.28 ? 34  SER H CA  1 
ATOM   8142  C  C   . SER H  1 61  ? 82.218  76.985  -20.776 1.00 25.83 ? 34  SER H C   1 
ATOM   8143  O  O   . SER H  1 61  ? 82.900  78.023  -20.816 1.00 23.89 ? 34  SER H O   1 
ATOM   8144  C  CB  . SER H  1 61  ? 79.796  77.400  -21.170 1.00 28.59 ? 34  SER H CB  1 
ATOM   8145  O  OG  . SER H  1 61  ? 79.729  76.439  -22.225 1.00 34.13 ? 34  SER H OG  1 
ATOM   8146  N  N   . ILE H  1 62  ? 82.660  75.821  -21.235 1.00 23.34 ? 35  ILE H N   1 
ATOM   8147  C  CA  . ILE H  1 62  ? 83.943  75.699  -21.902 1.00 21.95 ? 35  ILE H CA  1 
ATOM   8148  C  C   . ILE H  1 62  ? 83.632  75.041  -23.230 1.00 26.26 ? 35  ILE H C   1 
ATOM   8149  O  O   . ILE H  1 62  ? 82.881  74.036  -23.240 1.00 27.84 ? 35  ILE H O   1 
ATOM   8150  C  CB  . ILE H  1 62  ? 84.929  74.804  -21.115 1.00 21.92 ? 35  ILE H CB  1 
ATOM   8151  C  CG1 . ILE H  1 62  ? 85.048  75.291  -19.662 1.00 22.98 ? 35  ILE H CG1 1 
ATOM   8152  C  CG2 . ILE H  1 62  ? 86.239  74.641  -21.948 1.00 22.67 ? 35  ILE H CG2 1 
ATOM   8153  C  CD1 . ILE H  1 62  ? 86.043  74.564  -18.752 1.00 23.85 ? 35  ILE H CD1 1 
ATOM   8154  N  N   . LYS H  1 63  ? 84.128  75.588  -24.346 1.00 25.34 ? 36  LYS H N   1 
ATOM   8155  C  CA  . LYS H  1 63  ? 83.900  74.938  -25.643 1.00 26.89 ? 36  LYS H CA  1 
ATOM   8156  C  C   . LYS H  1 63  ? 85.231  74.498  -26.287 1.00 29.16 ? 36  LYS H C   1 
ATOM   8157  O  O   . LYS H  1 63  ? 86.295  74.802  -25.756 1.00 28.22 ? 36  LYS H O   1 
ATOM   8158  C  CB  . LYS H  1 63  ? 83.172  75.856  -26.599 1.00 32.41 ? 36  LYS H CB  1 
ATOM   8159  C  CG  . LYS H  1 63  ? 84.005  77.057  -26.989 1.00 39.10 ? 36  LYS H CG  1 
ATOM   8160  C  CD  . LYS H  1 63  ? 83.134  78.104  -27.654 1.00 47.44 ? 36  LYS H CD  1 
ATOM   8161  C  CE  . LYS H  1 63  ? 83.978  78.971  -28.566 1.00 54.65 ? 36  LYS H CE  1 
ATOM   8162  N  NZ  . LYS H  1 63  ? 83.070  79.694  -29.493 1.00 61.26 ? 36  LYS H NZ  1 
ATOM   8163  N  N   . GLY H  1 64  ? 85.158  73.780  -27.407 1.00 27.27 ? 37  GLY H N   1 
ATOM   8164  C  CA  . GLY H  1 64  ? 86.366  73.303  -28.078 1.00 29.98 ? 37  GLY H CA  1 
ATOM   8165  C  C   . GLY H  1 64  ? 86.975  72.024  -27.530 1.00 31.44 ? 37  GLY H C   1 
ATOM   8166  O  O   . GLY H  1 64  ? 88.050  71.577  -28.001 1.00 30.93 ? 37  GLY H O   1 
ATOM   8167  N  N   . LEU H  1 65  ? 86.278  71.382  -26.591 1.00 26.48 ? 38  LEU H N   1 
ATOM   8168  C  CA  . LEU H  1 65  ? 86.803  70.197  -25.925 1.00 24.89 ? 38  LEU H CA  1 
ATOM   8169  C  C   . LEU H  1 65  ? 86.494  68.938  -26.727 1.00 26.81 ? 38  LEU H C   1 
ATOM   8170  O  O   . LEU H  1 65  ? 85.499  68.923  -27.433 1.00 29.81 ? 38  LEU H O   1 
ATOM   8171  C  CB  . LEU H  1 65  ? 86.104  70.030  -24.558 1.00 25.27 ? 38  LEU H CB  1 
ATOM   8172  C  CG  . LEU H  1 65  ? 86.541  71.061  -23.532 1.00 26.52 ? 38  LEU H CG  1 
ATOM   8173  C  CD1 . LEU H  1 65  ? 85.559  71.098  -22.371 1.00 26.00 ? 38  LEU H CD1 1 
ATOM   8174  C  CD2 . LEU H  1 65  ? 87.965  70.791  -23.025 1.00 27.00 ? 38  LEU H CD2 1 
ATOM   8175  N  N   . THR H  1 66  ? 87.309  67.889  -26.543 1.00 28.54 ? 39  THR H N   1 
ATOM   8176  C  CA  . THR H  1 66  ? 86.998  66.523  -26.991 1.00 29.37 ? 39  THR H CA  1 
ATOM   8177  C  C   . THR H  1 66  ? 85.848  66.042  -26.086 1.00 28.85 ? 39  THR H C   1 
ATOM   8178  O  O   . THR H  1 66  ? 85.851  66.321  -24.878 1.00 25.91 ? 39  THR H O   1 
ATOM   8179  C  CB  . THR H  1 66  ? 88.192  65.546  -26.826 1.00 30.00 ? 39  THR H CB  1 
ATOM   8180  O  OG1 . THR H  1 66  ? 88.676  65.583  -25.489 1.00 33.75 ? 39  THR H OG1 1 
ATOM   8181  C  CG2 . THR H  1 66  ? 89.387  65.869  -27.775 1.00 33.38 ? 39  THR H CG2 1 
ATOM   8182  N  N   . GLU H  1 67  ? 84.885  65.323  -26.664 1.00 28.98 ? 40  GLU H N   1 
ATOM   8183  C  CA  . GLU H  1 67  ? 83.729  64.844  -25.861 1.00 29.65 ? 40  GLU H CA  1 
ATOM   8184  C  C   . GLU H  1 67  ? 84.164  63.940  -24.692 1.00 28.47 ? 40  GLU H C   1 
ATOM   8185  O  O   . GLU H  1 67  ? 85.147  63.190  -24.809 1.00 29.01 ? 40  GLU H O   1 
ATOM   8186  C  CB  . GLU H  1 67  ? 82.722  64.172  -26.794 1.00 31.71 ? 40  GLU H CB  1 
ATOM   8187  C  CG  . GLU H  1 67  ? 83.238  62.871  -27.374 1.00 37.57 ? 40  GLU H CG  1 
ATOM   8188  C  CD  . GLU H  1 67  ? 82.170  62.069  -28.099 1.00 43.74 ? 40  GLU H CD  1 
ATOM   8189  O  OE1 . GLU H  1 67  ? 81.134  62.628  -28.545 1.00 44.27 ? 40  GLU H OE1 1 
ATOM   8190  O  OE2 . GLU H  1 67  ? 82.392  60.853  -28.220 1.00 46.85 ? 40  GLU H OE2 1 
ATOM   8191  N  N   . GLY H  1 68  ? 83.478  64.014  -23.546 1.00 24.24 ? 41  GLY H N   1 
ATOM   8192  C  CA  . GLY H  1 68  ? 83.801  63.191  -22.370 1.00 21.48 ? 41  GLY H CA  1 
ATOM   8193  C  C   . GLY H  1 68  ? 84.364  63.996  -21.217 1.00 21.59 ? 41  GLY H C   1 
ATOM   8194  O  O   . GLY H  1 68  ? 84.189  65.220  -21.168 1.00 22.82 ? 41  GLY H O   1 
ATOM   8195  N  N   . LEU H  1 69  ? 85.063  63.319  -20.309 1.00 21.88 ? 42  LEU H N   1 
ATOM   8196  C  CA  . LEU H  1 69  ? 85.414  63.864  -19.009 1.00 22.10 ? 42  LEU H CA  1 
ATOM   8197  C  C   . LEU H  1 69  ? 86.741  64.645  -19.053 1.00 26.00 ? 42  LEU H C   1 
ATOM   8198  O  O   . LEU H  1 69  ? 87.685  64.223  -19.720 1.00 24.86 ? 42  LEU H O   1 
ATOM   8199  C  CB  . LEU H  1 69  ? 85.498  62.778  -17.936 1.00 22.18 ? 42  LEU H CB  1 
ATOM   8200  C  CG  . LEU H  1 69  ? 84.189  62.317  -17.245 1.00 23.30 ? 42  LEU H CG  1 
ATOM   8201  C  CD1 . LEU H  1 69  ? 83.271  61.704  -18.296 1.00 25.60 ? 42  LEU H CD1 1 
ATOM   8202  C  CD2 . LEU H  1 69  ? 84.505  61.290  -16.159 1.00 22.27 ? 42  LEU H CD2 1 
ATOM   8203  N  N   . HIS H  1 70  ? 86.822  65.761  -18.336 1.00 23.40 ? 43  HIS H N   1 
ATOM   8204  C  CA  . HIS H  1 70  ? 88.088  66.560  -18.348 1.00 24.04 ? 43  HIS H CA  1 
ATOM   8205  C  C   . HIS H  1 70  ? 88.386  67.039  -16.950 1.00 26.18 ? 43  HIS H C   1 
ATOM   8206  O  O   . HIS H  1 70  ? 87.526  67.658  -16.292 1.00 24.43 ? 43  HIS H O   1 
ATOM   8207  C  CB  . HIS H  1 70  ? 87.980  67.746  -19.308 1.00 25.29 ? 43  HIS H CB  1 
ATOM   8208  C  CG  . HIS H  1 70  ? 87.928  67.361  -20.746 1.00 25.27 ? 43  HIS H CG  1 
ATOM   8209  N  ND1 . HIS H  1 70  ? 89.057  67.211  -21.521 1.00 26.11 ? 43  HIS H ND1 1 
ATOM   8210  C  CD2 . HIS H  1 70  ? 86.879  67.126  -21.567 1.00 24.92 ? 43  HIS H CD2 1 
ATOM   8211  C  CE1 . HIS H  1 70  ? 88.709  66.881  -22.751 1.00 27.45 ? 43  HIS H CE1 1 
ATOM   8212  N  NE2 . HIS H  1 70  ? 87.390  66.811  -22.805 1.00 28.42 ? 43  HIS H NE2 1 
ATOM   8213  N  N   . GLY H  1 71  ? 89.603  66.752  -16.466 1.00 24.11 ? 44  GLY H N   1 
ATOM   8214  C  CA  . GLY H  1 71  ? 90.015  67.203  -15.153 1.00 22.07 ? 44  GLY H CA  1 
ATOM   8215  C  C   . GLY H  1 71  ? 89.885  68.753  -15.057 1.00 21.24 ? 44  GLY H C   1 
ATOM   8216  O  O   . GLY H  1 71  ? 90.092  69.444  -16.033 1.00 22.58 ? 44  GLY H O   1 
ATOM   8217  N  N   . PHE H  1 72  ? 89.552  69.240  -13.885 1.00 22.20 ? 45  PHE H N   1 
ATOM   8218  C  CA  . PHE H  1 72  ? 89.165  70.669  -13.695 1.00 23.44 ? 45  PHE H CA  1 
ATOM   8219  C  C   . PHE H  1 72  ? 89.682  71.099  -12.342 1.00 23.48 ? 45  PHE H C   1 
ATOM   8220  O  O   . PHE H  1 72  ? 89.121  70.697  -11.287 1.00 23.20 ? 45  PHE H O   1 
ATOM   8221  C  CB  . PHE H  1 72  ? 87.627  70.783  -13.752 1.00 23.25 ? 45  PHE H CB  1 
ATOM   8222  C  CG  . PHE H  1 72  ? 87.102  72.217  -13.801 1.00 23.54 ? 45  PHE H CG  1 
ATOM   8223  C  CD1 . PHE H  1 72  ? 87.404  73.058  -14.894 1.00 23.65 ? 45  PHE H CD1 1 
ATOM   8224  C  CD2 . PHE H  1 72  ? 86.236  72.662  -12.829 1.00 23.91 ? 45  PHE H CD2 1 
ATOM   8225  C  CE1 . PHE H  1 72  ? 86.842  74.348  -14.968 1.00 23.43 ? 45  PHE H CE1 1 
ATOM   8226  C  CE2 . PHE H  1 72  ? 85.679  73.938  -12.893 1.00 25.78 ? 45  PHE H CE2 1 
ATOM   8227  C  CZ  . PHE H  1 72  ? 86.003  74.785  -13.956 1.00 23.52 ? 45  PHE H CZ  1 
ATOM   8228  N  N   . HIS H  1 73  ? 90.765  71.912  -12.320 1.00 24.51 ? 46  HIS H N   1 
ATOM   8229  C  CA  . HIS H  1 73  ? 91.450  72.154  -11.037 1.00 23.95 ? 46  HIS H CA  1 
ATOM   8230  C  C   . HIS H  1 73  ? 91.885  73.604  -10.838 1.00 22.89 ? 46  HIS H C   1 
ATOM   8231  O  O   . HIS H  1 73  ? 92.156  74.261  -11.806 1.00 24.07 ? 46  HIS H O   1 
ATOM   8232  C  CB  . HIS H  1 73  ? 92.709  71.300  -10.914 1.00 27.43 ? 46  HIS H CB  1 
ATOM   8233  C  CG  . HIS H  1 73  ? 92.480  69.842  -11.180 1.00 30.81 ? 46  HIS H CG  1 
ATOM   8234  N  ND1 . HIS H  1 73  ? 92.944  69.217  -12.315 1.00 29.61 ? 46  HIS H ND1 1 
ATOM   8235  C  CD2 . HIS H  1 73  ? 91.771  68.910  -10.495 1.00 30.25 ? 46  HIS H CD2 1 
ATOM   8236  C  CE1 . HIS H  1 73  ? 92.563  67.950  -12.305 1.00 30.64 ? 46  HIS H CE1 1 
ATOM   8237  N  NE2 . HIS H  1 73  ? 91.851  67.739  -11.208 1.00 30.61 ? 46  HIS H NE2 1 
ATOM   8238  N  N   . VAL H  1 74  ? 91.960  74.038  -9.590  1.00 23.56 ? 47  VAL H N   1 
ATOM   8239  C  CA  . VAL H  1 74  ? 92.644  75.308  -9.274  1.00 27.92 ? 47  VAL H CA  1 
ATOM   8240  C  C   . VAL H  1 74  ? 94.119  74.952  -8.952  1.00 27.09 ? 47  VAL H C   1 
ATOM   8241  O  O   . VAL H  1 74  ? 94.370  74.138  -8.061  1.00 29.51 ? 47  VAL H O   1 
ATOM   8242  C  CB  . VAL H  1 74  ? 92.034  76.033  -8.078  1.00 25.49 ? 47  VAL H CB  1 
ATOM   8243  C  CG1 . VAL H  1 74  ? 92.803  77.347  -7.827  1.00 26.52 ? 47  VAL H CG1 1 
ATOM   8244  C  CG2 . VAL H  1 74  ? 90.554  76.325  -8.323  1.00 26.30 ? 47  VAL H CG2 1 
ATOM   8245  N  N   . HIS H  1 75  ? 95.033  75.517  -9.725  1.00 29.69 ? 48  HIS H N   1 
ATOM   8246  C  CA  . HIS H  1 75  ? 96.481  75.326  -9.571  1.00 27.61 ? 48  HIS H CA  1 
ATOM   8247  C  C   . HIS H  1 75  ? 97.065  76.488  -8.749  1.00 32.56 ? 48  HIS H C   1 
ATOM   8248  O  O   . HIS H  1 75  ? 96.447  77.547  -8.625  1.00 31.60 ? 48  HIS H O   1 
ATOM   8249  C  CB  . HIS H  1 75  ? 97.133  75.227  -10.944 1.00 28.81 ? 48  HIS H CB  1 
ATOM   8250  C  CG  . HIS H  1 75  ? 96.849  73.933  -11.673 1.00 30.67 ? 48  HIS H CG  1 
ATOM   8251  N  ND1 . HIS H  1 75  ? 97.841  73.050  -12.040 1.00 31.87 ? 48  HIS H ND1 1 
ATOM   8252  C  CD2 . HIS H  1 75  ? 95.688  73.398  -12.134 1.00 30.27 ? 48  HIS H CD2 1 
ATOM   8253  C  CE1 . HIS H  1 75  ? 97.314  72.025  -12.690 1.00 31.64 ? 48  HIS H CE1 1 
ATOM   8254  N  NE2 . HIS H  1 75  ? 96.003  72.210  -12.757 1.00 32.19 ? 48  HIS H NE2 1 
ATOM   8255  N  N   . GLU H  1 76  ? 98.265  76.291  -8.205  1.00 31.69 ? 49  GLU H N   1 
ATOM   8256  C  CA  . GLU H  1 76  ? 98.759  77.138  -7.149  1.00 28.49 ? 49  GLU H CA  1 
ATOM   8257  C  C   . GLU H  1 76  ? 99.014  78.611  -7.572  1.00 27.38 ? 49  GLU H C   1 
ATOM   8258  O  O   . GLU H  1 76  ? 98.605  79.534  -6.844  1.00 31.38 ? 49  GLU H O   1 
ATOM   8259  C  CB  . GLU H  1 76  ? 100.004 76.530  -6.516  1.00 31.78 ? 49  GLU H CB  1 
ATOM   8260  C  CG  . GLU H  1 76  ? 100.288 77.129  -5.150  1.00 34.69 ? 49  GLU H CG  1 
ATOM   8261  C  CD  . GLU H  1 76  ? 101.566 76.581  -4.540  1.00 40.64 ? 49  GLU H CD  1 
ATOM   8262  O  OE1 . GLU H  1 76  ? 102.198 75.687  -5.147  1.00 37.55 ? 49  GLU H OE1 1 
ATOM   8263  O  OE2 . GLU H  1 76  ? 101.926 77.075  -3.461  1.00 42.44 ? 49  GLU H OE2 1 
ATOM   8264  N  N   . PHE H  1 77  ? 99.599  78.822  -8.750  1.00 28.64 ? 50  PHE H N   1 
ATOM   8265  C  CA  . PHE H  1 77  ? 100.075 80.165  -9.117  1.00 33.65 ? 50  PHE H CA  1 
ATOM   8266  C  C   . PHE H  1 77  ? 99.265  80.775  -10.242 1.00 31.94 ? 50  PHE H C   1 
ATOM   8267  O  O   . PHE H  1 77  ? 98.946  80.098  -11.225 1.00 33.12 ? 50  PHE H O   1 
ATOM   8268  C  CB  . PHE H  1 77  ? 101.576 80.134  -9.508  1.00 31.80 ? 50  PHE H CB  1 
ATOM   8269  C  CG  . PHE H  1 77  ? 102.444 79.437  -8.483  1.00 34.06 ? 50  PHE H CG  1 
ATOM   8270  C  CD1 . PHE H  1 77  ? 102.591 79.962  -7.196  1.00 38.83 ? 50  PHE H CD1 1 
ATOM   8271  C  CD2 . PHE H  1 77  ? 103.094 78.242  -8.800  1.00 39.64 ? 50  PHE H CD2 1 
ATOM   8272  C  CE1 . PHE H  1 77  ? 103.358 79.313  -6.239  1.00 41.21 ? 50  PHE H CE1 1 
ATOM   8273  C  CE2 . PHE H  1 77  ? 103.871 77.582  -7.849  1.00 38.77 ? 50  PHE H CE2 1 
ATOM   8274  C  CZ  . PHE H  1 77  ? 104.003 78.115  -6.576  1.00 40.27 ? 50  PHE H CZ  1 
ATOM   8275  N  N   . GLY H  1 78  ? 99.013  82.080  -10.128 1.00 30.36 ? 51  GLY H N   1 
ATOM   8276  C  CA  . GLY H  1 78  ? 98.394  82.826  -11.212 1.00 30.12 ? 51  GLY H CA  1 
ATOM   8277  C  C   . GLY H  1 78  ? 99.389  83.380  -12.188 1.00 33.96 ? 51  GLY H C   1 
ATOM   8278  O  O   . GLY H  1 78  ? 99.326  84.562  -12.560 1.00 33.70 ? 51  GLY H O   1 
ATOM   8279  N  N   . ASP H  1 79  ? 100.307 82.507  -12.600 1.00 34.14 ? 52  ASP H N   1 
ATOM   8280  C  CA  . ASP H  1 79  ? 101.402 82.836  -13.495 1.00 33.53 ? 52  ASP H CA  1 
ATOM   8281  C  C   . ASP H  1 79  ? 101.202 82.147  -14.826 1.00 32.55 ? 52  ASP H C   1 
ATOM   8282  O  O   . ASP H  1 79  ? 101.214 80.907  -14.918 1.00 32.42 ? 52  ASP H O   1 
ATOM   8283  C  CB  . ASP H  1 79  ? 102.697 82.360  -12.840 1.00 35.21 ? 52  ASP H CB  1 
ATOM   8284  C  CG  . ASP H  1 79  ? 103.944 82.754  -13.619 1.00 33.09 ? 52  ASP H CG  1 
ATOM   8285  O  OD1 . ASP H  1 79  ? 103.892 82.960  -14.868 1.00 36.71 ? 52  ASP H OD1 1 
ATOM   8286  O  OD2 . ASP H  1 79  ? 104.978 82.827  -12.927 1.00 38.24 ? 52  ASP H OD2 1 
ATOM   8287  N  N   . ASN H  1 80  ? 100.986 82.940  -15.855 1.00 30.86 ? 53  ASN H N   1 
ATOM   8288  C  CA  . ASN H  1 80  ? 100.768 82.406  -17.180 1.00 33.19 ? 53  ASN H CA  1 
ATOM   8289  C  C   . ASN H  1 80  ? 101.876 82.791  -18.149 1.00 33.92 ? 53  ASN H C   1 
ATOM   8290  O  O   . ASN H  1 80  ? 101.684 82.787  -19.364 1.00 35.45 ? 53  ASN H O   1 
ATOM   8291  C  CB  . ASN H  1 80  ? 99.426  82.922  -17.704 1.00 40.37 ? 53  ASN H CB  1 
ATOM   8292  C  CG  . ASN H  1 80  ? 99.050  82.307  -19.016 1.00 48.42 ? 53  ASN H CG  1 
ATOM   8293  O  OD1 . ASN H  1 80  ? 98.936  81.083  -19.119 1.00 55.80 ? 53  ASN H OD1 1 
ATOM   8294  N  ND2 . ASN H  1 80  ? 98.879  83.146  -20.050 1.00 51.48 ? 53  ASN H ND2 1 
ATOM   8295  N  N   . THR H  1 81  ? 103.054 83.094  -17.612 1.00 35.77 ? 54  THR H N   1 
ATOM   8296  C  CA  . THR H  1 81  ? 104.152 83.601  -18.459 1.00 39.71 ? 54  THR H CA  1 
ATOM   8297  C  C   . THR H  1 81  ? 104.674 82.553  -19.416 1.00 39.86 ? 54  THR H C   1 
ATOM   8298  O  O   . THR H  1 81  ? 105.143 82.885  -20.497 1.00 42.45 ? 54  THR H O   1 
ATOM   8299  C  CB  . THR H  1 81  ? 105.320 84.125  -17.616 1.00 36.17 ? 54  THR H CB  1 
ATOM   8300  O  OG1 . THR H  1 81  ? 105.706 83.112  -16.711 1.00 35.99 ? 54  THR H OG1 1 
ATOM   8301  C  CG2 . THR H  1 81  ? 104.886 85.308  -16.792 1.00 37.95 ? 54  THR H CG2 1 
ATOM   8302  N  N   . ALA H  1 82  ? 104.572 81.284  -19.044 1.00 40.43 ? 55  ALA H N   1 
ATOM   8303  C  CA  . ALA H  1 82  ? 104.915 80.225  -19.979 1.00 41.07 ? 55  ALA H CA  1 
ATOM   8304  C  C   . ALA H  1 82  ? 103.674 79.352  -20.237 1.00 46.03 ? 55  ALA H C   1 
ATOM   8305  O  O   . ALA H  1 82  ? 103.729 78.121  -20.114 1.00 45.70 ? 55  ALA H O   1 
ATOM   8306  C  CB  . ALA H  1 82  ? 106.070 79.389  -19.420 1.00 40.56 ? 55  ALA H CB  1 
ATOM   8307  N  N   . GLY H  1 83  ? 102.545 79.997  -20.545 1.00 41.22 ? 56  GLY H N   1 
ATOM   8308  C  CA  . GLY H  1 83  ? 101.273 79.277  -20.700 1.00 36.98 ? 56  GLY H CA  1 
ATOM   8309  C  C   . GLY H  1 83  ? 100.843 78.592  -19.410 1.00 36.64 ? 56  GLY H C   1 
ATOM   8310  O  O   . GLY H  1 83  ? 101.211 79.011  -18.302 1.00 35.45 ? 56  GLY H O   1 
ATOM   8311  N  N   . CYS H  1 84  ? 100.069 77.514  -19.538 1.00 35.55 ? 57  CYS H N   1 
ATOM   8312  C  CA  . CYS H  1 84  ? 99.507  76.882  -18.352 1.00 34.88 ? 57  CYS H CA  1 
ATOM   8313  C  C   . CYS H  1 84  ? 100.547 76.158  -17.489 1.00 32.71 ? 57  CYS H C   1 
ATOM   8314  O  O   . CYS H  1 84  ? 100.326 75.932  -16.296 1.00 32.90 ? 57  CYS H O   1 
ATOM   8315  C  CB  . CYS H  1 84  ? 98.310  75.978  -18.736 1.00 40.23 ? 57  CYS H CB  1 
ATOM   8316  S  SG  . CYS H  1 84  ? 97.051  76.866  -19.704 1.00 45.68 ? 57  CYS H SG  1 
ATOM   8317  N  N   . THR H  1 85  ? 101.709 75.841  -18.060 1.00 36.55 ? 58  THR H N   1 
ATOM   8318  C  CA  . THR H  1 85  ? 102.794 75.217  -17.255 1.00 36.79 ? 58  THR H CA  1 
ATOM   8319  C  C   . THR H  1 85  ? 103.229 76.044  -16.055 1.00 38.24 ? 58  THR H C   1 
ATOM   8320  O  O   . THR H  1 85  ? 103.494 75.482  -14.979 1.00 37.46 ? 58  THR H O   1 
ATOM   8321  C  CB  . THR H  1 85  ? 104.034 74.963  -18.118 1.00 41.13 ? 58  THR H CB  1 
ATOM   8322  O  OG1 . THR H  1 85  ? 103.599 74.715  -19.453 1.00 42.34 ? 58  THR H OG1 1 
ATOM   8323  C  CG2 . THR H  1 85  ? 104.823 73.771  -17.583 1.00 40.01 ? 58  THR H CG2 1 
ATOM   8324  N  N   . SER H  1 86  ? 103.284 77.379  -16.198 1.00 36.09 ? 59  SER H N   1 
ATOM   8325  C  CA  . SER H  1 86  ? 103.730 78.210  -15.065 1.00 33.57 ? 59  SER H CA  1 
ATOM   8326  C  C   . SER H  1 86  ? 102.751 78.232  -13.922 1.00 33.42 ? 59  SER H C   1 
ATOM   8327  O  O   . SER H  1 86  ? 103.076 78.714  -12.825 1.00 31.87 ? 59  SER H O   1 
ATOM   8328  C  CB  . SER H  1 86  ? 104.044 79.659  -15.479 1.00 34.56 ? 59  SER H CB  1 
ATOM   8329  O  OG  . SER H  1 86  ? 103.980 79.809  -16.855 1.00 41.95 ? 59  SER H OG  1 
ATOM   8330  N  N   . ALA H  1 87  ? 101.544 77.670  -14.117 1.00 32.82 ? 60  ALA H N   1 
ATOM   8331  C  CA  . ALA H  1 87  ? 100.610 77.652  -12.993 1.00 29.54 ? 60  ALA H CA  1 
ATOM   8332  C  C   . ALA H  1 87  ? 101.027 76.759  -11.832 1.00 31.37 ? 60  ALA H C   1 
ATOM   8333  O  O   . ALA H  1 87  ? 100.514 76.923  -10.699 1.00 30.44 ? 60  ALA H O   1 
ATOM   8334  C  CB  . ALA H  1 87  ? 99.186  77.333  -13.474 1.00 29.87 ? 60  ALA H CB  1 
ATOM   8335  N  N   . GLY H  1 88  ? 102.000 75.863  -12.062 1.00 30.11 ? 61  GLY H N   1 
ATOM   8336  C  CA  . GLY H  1 88  ? 102.462 74.996  -10.974 1.00 33.47 ? 61  GLY H CA  1 
ATOM   8337  C  C   . GLY H  1 88  ? 101.447 73.845  -10.760 1.00 33.50 ? 61  GLY H C   1 
ATOM   8338  O  O   . GLY H  1 88  ? 100.632 73.570  -11.672 1.00 35.37 ? 61  GLY H O   1 
ATOM   8339  N  N   . PRO H  1 89  ? 101.465 73.216  -9.563  1.00 34.56 ? 62  PRO H N   1 
ATOM   8340  C  CA  . PRO H  1 89  ? 100.639 72.046  -9.226  1.00 35.43 ? 62  PRO H CA  1 
ATOM   8341  C  C   . PRO H  1 89  ? 99.244  72.437  -8.690  1.00 38.31 ? 62  PRO H C   1 
ATOM   8342  O  O   . PRO H  1 89  ? 98.966  73.641  -8.536  1.00 35.08 ? 62  PRO H O   1 
ATOM   8343  C  CB  . PRO H  1 89  ? 101.463 71.372  -8.126  1.00 35.34 ? 62  PRO H CB  1 
ATOM   8344  C  CG  . PRO H  1 89  ? 102.073 72.532  -7.375  1.00 37.50 ? 62  PRO H CG  1 
ATOM   8345  C  CD  . PRO H  1 89  ? 102.325 73.605  -8.415  1.00 36.17 ? 62  PRO H CD  1 
ATOM   8346  N  N   . HIS H  1 90  ? 98.387  71.447  -8.405  1.00 33.57 ? 63  HIS H N   1 
ATOM   8347  C  CA  . HIS H  1 90  ? 97.055  71.714  -7.821  1.00 36.35 ? 63  HIS H CA  1 
ATOM   8348  C  C   . HIS H  1 90  ? 97.289  72.510  -6.539  1.00 38.66 ? 63  HIS H C   1 
ATOM   8349  O  O   . HIS H  1 90  ? 98.210  72.199  -5.758  1.00 33.02 ? 63  HIS H O   1 
ATOM   8350  C  CB  . HIS H  1 90  ? 96.255  70.407  -7.496  1.00 33.50 ? 63  HIS H CB  1 
ATOM   8351  C  CG  . HIS H  1 90  ? 96.009  69.529  -8.689  1.00 32.60 ? 63  HIS H CG  1 
ATOM   8352  N  ND1 . HIS H  1 90  ? 95.423  68.263  -8.609  1.00 30.57 ? 63  HIS H ND1 1 
ATOM   8353  C  CD2 . HIS H  1 90  ? 96.259  69.747  -9.999  1.00 30.15 ? 63  HIS H CD2 1 
ATOM   8354  C  CE1 . HIS H  1 90  ? 95.341  67.763  -9.833  1.00 31.08 ? 63  HIS H CE1 1 
ATOM   8355  N  NE2 . HIS H  1 90  ? 95.834  68.640  -10.690 1.00 32.26 ? 63  HIS H NE2 1 
ATOM   8356  N  N   . PHE H  1 91  ? 96.468  73.530  -6.326  1.00 32.24 ? 64  PHE H N   1 
ATOM   8357  C  CA  . PHE H  1 91  ? 96.534  74.308  -5.118  1.00 34.76 ? 64  PHE H CA  1 
ATOM   8358  C  C   . PHE H  1 91  ? 96.294  73.384  -3.933  1.00 36.17 ? 64  PHE H C   1 
ATOM   8359  O  O   . PHE H  1 91  ? 95.243  72.722  -3.822  1.00 32.87 ? 64  PHE H O   1 
ATOM   8360  C  CB  . PHE H  1 91  ? 95.514  75.475  -5.183  1.00 31.14 ? 64  PHE H CB  1 
ATOM   8361  C  CG  . PHE H  1 91  ? 95.441  76.299  -3.936  1.00 31.16 ? 64  PHE H CG  1 
ATOM   8362  C  CD1 . PHE H  1 91  ? 96.612  76.826  -3.336  1.00 32.07 ? 64  PHE H CD1 1 
ATOM   8363  C  CD2 . PHE H  1 91  ? 94.197  76.640  -3.395  1.00 31.89 ? 64  PHE H CD2 1 
ATOM   8364  C  CE1 . PHE H  1 91  ? 96.514  77.641  -2.200  1.00 28.61 ? 64  PHE H CE1 1 
ATOM   8365  C  CE2 . PHE H  1 91  ? 94.094  77.417  -2.248  1.00 34.04 ? 64  PHE H CE2 1 
ATOM   8366  C  CZ  . PHE H  1 91  ? 95.261  77.924  -1.649  1.00 33.64 ? 64  PHE H CZ  1 
ATOM   8367  N  N   . ASN H  1 92  ? 97.256  73.360  -3.006  1.00 35.44 ? 65  ASN H N   1 
ATOM   8368  C  CA  . ASN H  1 92  ? 97.258  72.344  -1.972  1.00 35.66 ? 65  ASN H CA  1 
ATOM   8369  C  C   . ASN H  1 92  ? 97.867  72.877  -0.686  1.00 39.05 ? 65  ASN H C   1 
ATOM   8370  O  O   . ASN H  1 92  ? 98.874  72.345  -0.246  1.00 39.91 ? 65  ASN H O   1 
ATOM   8371  C  CB  . ASN H  1 92  ? 98.030  71.102  -2.512  1.00 34.37 ? 65  ASN H CB  1 
ATOM   8372  C  CG  . ASN H  1 92  ? 98.079  69.938  -1.522  1.00 33.40 ? 65  ASN H CG  1 
ATOM   8373  O  OD1 . ASN H  1 92  ? 97.254  69.821  -0.594  1.00 34.08 ? 65  ASN H OD1 1 
ATOM   8374  N  ND2 . ASN H  1 92  ? 99.055  69.062  -1.727  1.00 31.50 ? 65  ASN H ND2 1 
ATOM   8375  N  N   . PRO H  1 93  ? 97.254  73.913  -0.073  1.00 38.70 ? 66  PRO H N   1 
ATOM   8376  C  CA  . PRO H  1 93  ? 97.862  74.505  1.121   1.00 40.81 ? 66  PRO H CA  1 
ATOM   8377  C  C   . PRO H  1 93  ? 97.855  73.576  2.356   1.00 46.50 ? 66  PRO H C   1 
ATOM   8378  O  O   . PRO H  1 93  ? 98.611  73.813  3.294   1.00 46.74 ? 66  PRO H O   1 
ATOM   8379  C  CB  . PRO H  1 93  ? 96.970  75.718  1.400   1.00 39.00 ? 66  PRO H CB  1 
ATOM   8380  C  CG  . PRO H  1 93  ? 95.620  75.309  0.876   1.00 39.96 ? 66  PRO H CG  1 
ATOM   8381  C  CD  . PRO H  1 93  ? 95.922  74.489  -0.349  1.00 38.03 ? 66  PRO H CD  1 
ATOM   8382  N  N   . LEU H  1 94  ? 96.994  72.561  2.395   1.00 43.40 ? 67  LEU H N   1 
ATOM   8383  C  CA  . LEU H  1 94  ? 96.996  71.669  3.553   1.00 41.37 ? 67  LEU H CA  1 
ATOM   8384  C  C   . LEU H  1 94  ? 97.881  70.437  3.320   1.00 40.98 ? 67  LEU H C   1 
ATOM   8385  O  O   . LEU H  1 94  ? 97.878  69.516  4.127   1.00 42.32 ? 67  LEU H O   1 
ATOM   8386  C  CB  . LEU H  1 94  ? 95.563  71.305  3.971   1.00 45.45 ? 67  LEU H CB  1 
ATOM   8387  C  CG  . LEU H  1 94  ? 94.753  72.432  4.634   1.00 50.37 ? 67  LEU H CG  1 
ATOM   8388  C  CD1 . LEU H  1 94  ? 93.274  72.079  4.720   1.00 53.65 ? 67  LEU H CD1 1 
ATOM   8389  C  CD2 . LEU H  1 94  ? 95.285  72.791  6.018   1.00 52.66 ? 67  LEU H CD2 1 
ATOM   8390  N  N   . SER H  1 95  ? 98.643  70.427  2.223   1.00 40.57 ? 68  SER H N   1 
ATOM   8391  C  CA  . SER H  1 95  ? 99.561  69.314  1.907   1.00 45.14 ? 68  SER H CA  1 
ATOM   8392  C  C   . SER H  1 95  ? 98.901  67.925  1.932   1.00 49.02 ? 68  SER H C   1 
ATOM   8393  O  O   . SER H  1 95  ? 99.485  66.972  2.481   1.00 43.06 ? 68  SER H O   1 
ATOM   8394  C  CB  . SER H  1 95  ? 100.770 69.314  2.870   1.00 45.68 ? 68  SER H CB  1 
ATOM   8395  O  OG  . SER H  1 95  ? 101.610 70.412  2.574   1.00 48.42 ? 68  SER H OG  1 
ATOM   8396  N  N   . ARG H  1 96  ? 97.694  67.809  1.352   1.00 45.20 ? 69  ARG H N   1 
ATOM   8397  C  CA  . ARG H  1 96  ? 96.966  66.522  1.285   1.00 40.00 ? 69  ARG H CA  1 
ATOM   8398  C  C   . ARG H  1 96  ? 97.307  65.829  -0.014  1.00 39.25 ? 69  ARG H C   1 
ATOM   8399  O  O   . ARG H  1 96  ? 97.980  66.401  -0.872  1.00 39.71 ? 69  ARG H O   1 
ATOM   8400  C  CB  . ARG H  1 96  ? 95.466  66.745  1.339   1.00 39.48 ? 69  ARG H CB  1 
ATOM   8401  C  CG  . ARG H  1 96  ? 94.992  67.569  2.517   1.00 45.12 ? 69  ARG H CG  1 
ATOM   8402  C  CD  . ARG H  1 96  ? 94.743  66.721  3.744   1.00 50.89 ? 69  ARG H CD  1 
ATOM   8403  N  NE  . ARG H  1 96  ? 94.157  67.536  4.807   1.00 62.02 ? 69  ARG H NE  1 
ATOM   8404  C  CZ  . ARG H  1 96  ? 92.849  67.681  5.039   1.00 62.13 ? 69  ARG H CZ  1 
ATOM   8405  N  NH1 . ARG H  1 96  ? 91.944  67.060  4.293   1.00 64.25 ? 69  ARG H NH1 1 
ATOM   8406  N  NH2 . ARG H  1 96  ? 92.440  68.448  6.039   1.00 66.94 ? 69  ARG H NH2 1 
ATOM   8407  N  N   . LYS H  1 97  ? 96.843  64.589  -0.165  1.00 39.26 ? 70  LYS H N   1 
ATOM   8408  C  CA  . LYS H  1 97  ? 96.909  63.873  -1.452  1.00 38.53 ? 70  LYS H CA  1 
ATOM   8409  C  C   . LYS H  1 97  ? 95.729  64.288  -2.374  1.00 34.67 ? 70  LYS H C   1 
ATOM   8410  O  O   . LYS H  1 97  ? 94.709  64.757  -1.890  1.00 32.33 ? 70  LYS H O   1 
ATOM   8411  C  CB  . LYS H  1 97  ? 96.796  62.346  -1.224  1.00 43.52 ? 70  LYS H CB  1 
ATOM   8412  C  CG  . LYS H  1 97  ? 97.766  61.780  -0.192  1.00 47.66 ? 70  LYS H CG  1 
ATOM   8413  C  CD  . LYS H  1 97  ? 99.164  62.109  -0.655  1.00 49.05 ? 70  LYS H CD  1 
ATOM   8414  C  CE  . LYS H  1 97  ? 99.844  60.880  -1.229  1.00 56.09 ? 70  LYS H CE  1 
ATOM   8415  N  NZ  . LYS H  1 97  ? 100.841 60.437  -0.216  1.00 51.10 ? 70  LYS H NZ  1 
ATOM   8416  N  N   . HIS H  1 98  ? 95.890  64.066  -3.670  1.00 35.17 ? 71  HIS H N   1 
ATOM   8417  C  CA  . HIS H  1 98  ? 94.858  64.373  -4.663  1.00 38.07 ? 71  HIS H CA  1 
ATOM   8418  C  C   . HIS H  1 98  ? 93.612  63.506  -4.479  1.00 38.72 ? 71  HIS H C   1 
ATOM   8419  O  O   . HIS H  1 98  ? 93.712  62.315  -4.189  1.00 37.25 ? 71  HIS H O   1 
ATOM   8420  C  CB  . HIS H  1 98  ? 95.414  64.162  -6.063  1.00 35.93 ? 71  HIS H CB  1 
ATOM   8421  C  CG  . HIS H  1 98  ? 94.406  64.366  -7.154  1.00 36.69 ? 71  HIS H CG  1 
ATOM   8422  N  ND1 . HIS H  1 98  ? 94.009  65.613  -7.576  1.00 33.49 ? 71  HIS H ND1 1 
ATOM   8423  C  CD2 . HIS H  1 98  ? 93.708  63.477  -7.908  1.00 35.67 ? 71  HIS H CD2 1 
ATOM   8424  C  CE1 . HIS H  1 98  ? 93.120  65.498  -8.549  1.00 32.88 ? 71  HIS H CE1 1 
ATOM   8425  N  NE2 . HIS H  1 98  ? 92.931  64.210  -8.779  1.00 34.70 ? 71  HIS H NE2 1 
ATOM   8426  N  N   . GLY H  1 99  ? 92.440  64.111  -4.624  1.00 36.84 ? 72  GLY H N   1 
ATOM   8427  C  CA  . GLY H  1 99  ? 91.214  63.329  -4.618  1.00 35.18 ? 72  GLY H CA  1 
ATOM   8428  C  C   . GLY H  1 99  ? 90.159  63.978  -5.480  1.00 35.60 ? 72  GLY H C   1 
ATOM   8429  O  O   . GLY H  1 99  ? 90.461  64.922  -6.241  1.00 28.75 ? 72  GLY H O   1 
ATOM   8430  N  N   . GLY H  1 100 ? 88.931  63.467  -5.342  1.00 30.70 ? 73  GLY H N   1 
ATOM   8431  C  CA  . GLY H  1 100 ? 87.747  64.085  -5.917  1.00 30.64 ? 73  GLY H CA  1 
ATOM   8432  C  C   . GLY H  1 100 ? 87.197  65.124  -4.976  1.00 31.42 ? 73  GLY H C   1 
ATOM   8433  O  O   . GLY H  1 100 ? 87.545  65.153  -3.785  1.00 31.34 ? 73  GLY H O   1 
ATOM   8434  N  N   . PRO H  1 101 ? 86.339  66.013  -5.502  1.00 31.80 ? 74  PRO H N   1 
ATOM   8435  C  CA  . PRO H  1 101 ? 85.802  67.046  -4.655  1.00 30.99 ? 74  PRO H CA  1 
ATOM   8436  C  C   . PRO H  1 101 ? 84.967  66.524  -3.488  1.00 34.36 ? 74  PRO H C   1 
ATOM   8437  O  O   . PRO H  1 101 ? 84.822  67.241  -2.500  1.00 34.30 ? 74  PRO H O   1 
ATOM   8438  C  CB  . PRO H  1 101 ? 84.938  67.881  -5.611  1.00 34.25 ? 74  PRO H CB  1 
ATOM   8439  C  CG  . PRO H  1 101 ? 84.650  66.978  -6.787  1.00 32.68 ? 74  PRO H CG  1 
ATOM   8440  C  CD  . PRO H  1 101 ? 85.927  66.171  -6.907  1.00 30.80 ? 74  PRO H CD  1 
ATOM   8441  N  N   . LYS H  1 102 ? 84.397  65.319  -3.602  1.00 33.64 ? 75  LYS H N   1 
ATOM   8442  C  CA  . LYS H  1 102 ? 83.601  64.746  -2.500  1.00 38.91 ? 75  LYS H CA  1 
ATOM   8443  C  C   . LYS H  1 102 ? 84.462  64.075  -1.423  1.00 38.75 ? 75  LYS H C   1 
ATOM   8444  O  O   . LYS H  1 102 ? 83.940  63.706  -0.388  1.00 38.97 ? 75  LYS H O   1 
ATOM   8445  C  CB  . LYS H  1 102 ? 82.588  63.719  -3.024  1.00 36.69 ? 75  LYS H CB  1 
ATOM   8446  C  CG  . LYS H  1 102 ? 81.576  64.285  -4.003  1.00 45.44 ? 75  LYS H CG  1 
ATOM   8447  C  CD  . LYS H  1 102 ? 80.465  63.257  -4.148  1.00 50.92 ? 75  LYS H CD  1 
ATOM   8448  C  CE  . LYS H  1 102 ? 79.635  63.474  -5.395  1.00 58.23 ? 75  LYS H CE  1 
ATOM   8449  N  NZ  . LYS H  1 102 ? 79.369  62.106  -5.943  1.00 62.59 ? 75  LYS H NZ  1 
ATOM   8450  N  N   . ASP H  1 103 ? 85.756  63.895  -1.693  1.00 39.03 ? 76  ASP H N   1 
ATOM   8451  C  CA  . ASP H  1 103 ? 86.688  63.257  -0.761  1.00 40.43 ? 76  ASP H CA  1 
ATOM   8452  C  C   . ASP H  1 103 ? 87.149  64.195  0.346   1.00 45.91 ? 76  ASP H C   1 
ATOM   8453  O  O   . ASP H  1 103 ? 87.417  65.395  0.117   1.00 38.52 ? 76  ASP H O   1 
ATOM   8454  C  CB  . ASP H  1 103 ? 87.899  62.722  -1.512  1.00 42.12 ? 76  ASP H CB  1 
ATOM   8455  C  CG  . ASP H  1 103 ? 87.524  61.610  -2.463  1.00 46.88 ? 76  ASP H CG  1 
ATOM   8456  O  OD1 . ASP H  1 103 ? 86.622  60.834  -2.089  1.00 46.69 ? 76  ASP H OD1 1 
ATOM   8457  O  OD2 . ASP H  1 103 ? 88.094  61.512  -3.574  1.00 44.70 ? 76  ASP H OD2 1 
ATOM   8458  N  N   . GLU H  1 104 ? 87.249  63.652  1.554   1.00 46.91 ? 77  GLU H N   1 
ATOM   8459  C  CA  . GLU H  1 104 ? 87.803  64.444  2.652   1.00 52.87 ? 77  GLU H CA  1 
ATOM   8460  C  C   . GLU H  1 104 ? 89.286  64.649  2.386   1.00 48.70 ? 77  GLU H C   1 
ATOM   8461  O  O   . GLU H  1 104 ? 89.841  65.706  2.694   1.00 55.65 ? 77  GLU H O   1 
ATOM   8462  C  CB  . GLU H  1 104 ? 87.606  63.769  4.000   1.00 60.40 ? 77  GLU H CB  1 
ATOM   8463  C  CG  . GLU H  1 104 ? 87.950  64.699  5.152   1.00 70.70 ? 77  GLU H CG  1 
ATOM   8464  C  CD  . GLU H  1 104 ? 87.688  64.067  6.501   1.00 82.55 ? 77  GLU H CD  1 
ATOM   8465  O  OE1 . GLU H  1 104 ? 88.433  63.127  6.870   1.00 86.05 ? 77  GLU H OE1 1 
ATOM   8466  O  OE2 . GLU H  1 104 ? 86.738  64.514  7.193   1.00 85.88 ? 77  GLU H OE2 1 
ATOM   8467  N  N   . GLU H  1 105 ? 89.918  63.655  1.788   1.00 39.61 ? 78  GLU H N   1 
ATOM   8468  C  CA  . GLU H  1 105 ? 91.306  63.791  1.412   1.00 38.55 ? 78  GLU H CA  1 
ATOM   8469  C  C   . GLU H  1 105 ? 91.391  64.239  -0.036  1.00 36.22 ? 78  GLU H C   1 
ATOM   8470  O  O   . GLU H  1 105 ? 91.243  63.424  -0.959  1.00 35.80 ? 78  GLU H O   1 
ATOM   8471  C  CB  . GLU H  1 105 ? 92.086  62.475  1.630   1.00 39.93 ? 78  GLU H CB  1 
ATOM   8472  C  CG  . GLU H  1 105 ? 93.575  62.551  1.244   1.00 42.73 ? 78  GLU H CG  1 
ATOM   8473  C  CD  . GLU H  1 105 ? 94.463  63.163  2.348   1.00 50.32 ? 78  GLU H CD  1 
ATOM   8474  O  OE1 . GLU H  1 105 ? 93.951  63.422  3.467   1.00 50.68 ? 78  GLU H OE1 1 
ATOM   8475  O  OE2 . GLU H  1 105 ? 95.679  63.399  2.103   1.00 45.35 ? 78  GLU H OE2 1 
ATOM   8476  N  N   . ARG H  1 106 ? 91.624  65.540  -0.234  1.00 32.15 ? 79  ARG H N   1 
ATOM   8477  C  CA  . ARG H  1 106 ? 91.783  66.130  -1.585  1.00 32.65 ? 79  ARG H CA  1 
ATOM   8478  C  C   . ARG H  1 106 ? 92.667  67.392  -1.476  1.00 32.62 ? 79  ARG H C   1 
ATOM   8479  O  O   . ARG H  1 106 ? 92.863  67.934  -0.391  1.00 34.51 ? 79  ARG H O   1 
ATOM   8480  C  CB  . ARG H  1 106 ? 90.408  66.533  -2.150  1.00 32.62 ? 79  ARG H CB  1 
ATOM   8481  C  CG  . ARG H  1 106 ? 89.618  67.402  -1.179  1.00 33.04 ? 79  ARG H CG  1 
ATOM   8482  C  CD  . ARG H  1 106 ? 88.348  68.031  -1.748  1.00 35.38 ? 79  ARG H CD  1 
ATOM   8483  N  NE  . ARG H  1 106 ? 88.607  69.299  -2.471  1.00 31.82 ? 79  ARG H NE  1 
ATOM   8484  C  CZ  . ARG H  1 106 ? 87.641  70.134  -2.862  1.00 33.43 ? 79  ARG H CZ  1 
ATOM   8485  N  NH1 . ARG H  1 106 ? 86.359  69.847  -2.601  1.00 29.44 ? 79  ARG H NH1 1 
ATOM   8486  N  NH2 . ARG H  1 106 ? 87.936  71.270  -3.490  1.00 31.43 ? 79  ARG H NH2 1 
ATOM   8487  N  N   . HIS H  1 107 ? 93.211  67.842  -2.590  1.00 34.46 ? 80  HIS H N   1 
ATOM   8488  C  CA  . HIS H  1 107 ? 93.721  69.210  -2.623  1.00 35.61 ? 80  HIS H CA  1 
ATOM   8489  C  C   . HIS H  1 107 ? 92.584  70.210  -2.583  1.00 36.66 ? 80  HIS H C   1 
ATOM   8490  O  O   . HIS H  1 107 ? 91.471  69.915  -3.072  1.00 33.40 ? 80  HIS H O   1 
ATOM   8491  C  CB  . HIS H  1 107 ? 94.480  69.407  -3.887  1.00 31.24 ? 80  HIS H CB  1 
ATOM   8492  C  CG  . HIS H  1 107 ? 95.565  68.408  -4.078  1.00 34.92 ? 80  HIS H CG  1 
ATOM   8493  N  ND1 . HIS H  1 107 ? 95.909  67.926  -5.317  1.00 32.93 ? 80  HIS H ND1 1 
ATOM   8494  C  CD2 . HIS H  1 107 ? 96.402  67.814  -3.197  1.00 32.35 ? 80  HIS H CD2 1 
ATOM   8495  C  CE1 . HIS H  1 107 ? 96.928  67.099  -5.206  1.00 31.28 ? 80  HIS H CE1 1 
ATOM   8496  N  NE2 . HIS H  1 107 ? 97.228  66.995  -3.925  1.00 29.40 ? 80  HIS H NE2 1 
ATOM   8497  N  N   . VAL H  1 108 ? 92.836  71.399  -2.023  1.00 34.81 ? 81  VAL H N   1 
ATOM   8498  C  CA  . VAL H  1 108 ? 91.837  72.469  -2.109  1.00 34.36 ? 81  VAL H CA  1 
ATOM   8499  C  C   . VAL H  1 108 ? 91.361  72.700  -3.557  1.00 30.10 ? 81  VAL H C   1 
ATOM   8500  O  O   . VAL H  1 108 ? 90.161  72.922  -3.795  1.00 31.60 ? 81  VAL H O   1 
ATOM   8501  C  CB  . VAL H  1 108 ? 92.330  73.794  -1.472  1.00 35.53 ? 81  VAL H CB  1 
ATOM   8502  C  CG1 . VAL H  1 108 ? 91.415  74.951  -1.861  1.00 29.82 ? 81  VAL H CG1 1 
ATOM   8503  C  CG2 . VAL H  1 108 ? 92.369  73.637  0.048   1.00 33.24 ? 81  VAL H CG2 1 
ATOM   8504  N  N   . GLY H  1 109 ? 92.292  72.651  -4.501  1.00 26.25 ? 82  GLY H N   1 
ATOM   8505  C  CA  . GLY H  1 109 ? 91.985  72.916  -5.899  1.00 27.19 ? 82  GLY H CA  1 
ATOM   8506  C  C   . GLY H  1 109 ? 91.283  71.788  -6.676  1.00 26.45 ? 82  GLY H C   1 
ATOM   8507  O  O   . GLY H  1 109 ? 91.069  71.915  -7.893  1.00 28.09 ? 82  GLY H O   1 
ATOM   8508  N  N   . ASP H  1 110 ? 90.907  70.693  -5.995  1.00 27.99 ? 83  ASP H N   1 
ATOM   8509  C  CA  . ASP H  1 110 ? 90.430  69.489  -6.728  1.00 27.60 ? 83  ASP H CA  1 
ATOM   8510  C  C   . ASP H  1 110 ? 88.955  69.640  -7.051  1.00 27.18 ? 83  ASP H C   1 
ATOM   8511  O  O   . ASP H  1 110 ? 88.097  69.320  -6.215  1.00 27.47 ? 83  ASP H O   1 
ATOM   8512  C  CB  . ASP H  1 110 ? 90.650  68.222  -5.869  1.00 29.54 ? 83  ASP H CB  1 
ATOM   8513  C  CG  . ASP H  1 110 ? 92.093  67.789  -5.839  1.00 33.54 ? 83  ASP H CG  1 
ATOM   8514  O  OD1 . ASP H  1 110 ? 92.848  68.367  -6.659  1.00 34.51 ? 83  ASP H OD1 1 
ATOM   8515  O  OD2 . ASP H  1 110 ? 92.471  66.868  -5.034  1.00 31.58 ? 83  ASP H OD2 1 
ATOM   8516  N  N   . LEU H  1 111 ? 88.639  70.131  -8.238  1.00 24.88 ? 84  LEU H N   1 
ATOM   8517  C  CA  . LEU H  1 111 ? 87.208  70.288  -8.519  1.00 26.85 ? 84  LEU H CA  1 
ATOM   8518  C  C   . LEU H  1 111 ? 86.648  69.143  -9.378  1.00 26.75 ? 84  LEU H C   1 
ATOM   8519  O  O   . LEU H  1 111 ? 85.559  69.267  -9.921  1.00 28.86 ? 84  LEU H O   1 
ATOM   8520  C  CB  . LEU H  1 111 ? 86.904  71.668  -9.107  1.00 25.95 ? 84  LEU H CB  1 
ATOM   8521  C  CG  . LEU H  1 111 ? 87.305  72.825  -8.168  1.00 27.08 ? 84  LEU H CG  1 
ATOM   8522  C  CD1 . LEU H  1 111 ? 87.057  74.140  -8.879  1.00 26.46 ? 84  LEU H CD1 1 
ATOM   8523  C  CD2 . LEU H  1 111 ? 86.515  72.789  -6.858  1.00 25.05 ? 84  LEU H CD2 1 
ATOM   8524  N  N   . GLY H  1 112 ? 87.396  68.053  -9.517  1.00 26.88 ? 85  GLY H N   1 
ATOM   8525  C  CA  . GLY H  1 112 ? 86.850  66.846  -10.186 1.00 25.97 ? 85  GLY H CA  1 
ATOM   8526  C  C   . GLY H  1 112 ? 86.885  66.931  -11.699 1.00 28.43 ? 85  GLY H C   1 
ATOM   8527  O  O   . GLY H  1 112 ? 87.885  67.348  -12.285 1.00 27.40 ? 85  GLY H O   1 
ATOM   8528  N  N   . ASN H  1 113 ? 85.784  66.526  -12.342 1.00 24.67 ? 86  ASN H N   1 
ATOM   8529  C  CA  . ASN H  1 113 ? 85.715  66.501  -13.796 1.00 23.84 ? 86  ASN H CA  1 
ATOM   8530  C  C   . ASN H  1 113 ? 84.530  67.324  -14.282 1.00 23.41 ? 86  ASN H C   1 
ATOM   8531  O  O   . ASN H  1 113 ? 83.495  67.316  -13.632 1.00 23.68 ? 86  ASN H O   1 
ATOM   8532  C  CB  . ASN H  1 113 ? 85.471  65.074  -14.289 1.00 25.26 ? 86  ASN H CB  1 
ATOM   8533  C  CG  . ASN H  1 113 ? 86.718  64.188  -14.182 1.00 25.20 ? 86  ASN H CG  1 
ATOM   8534  O  OD1 . ASN H  1 113 ? 87.698  64.409  -14.902 1.00 26.38 ? 86  ASN H OD1 1 
ATOM   8535  N  ND2 . ASN H  1 113 ? 86.669  63.183  -13.315 1.00 23.01 ? 86  ASN H ND2 1 
ATOM   8536  N  N   . VAL H  1 114 ? 84.681  67.944  -15.446 1.00 21.38 ? 87  VAL H N   1 
ATOM   8537  C  CA  . VAL H  1 114 ? 83.583  68.542  -16.179 1.00 23.36 ? 87  VAL H CA  1 
ATOM   8538  C  C   . VAL H  1 114 ? 83.402  67.668  -17.422 1.00 25.18 ? 87  VAL H C   1 
ATOM   8539  O  O   . VAL H  1 114 ? 84.354  67.028  -17.893 1.00 25.99 ? 87  VAL H O   1 
ATOM   8540  C  CB  . VAL H  1 114 ? 83.850  70.040  -16.554 1.00 23.26 ? 87  VAL H CB  1 
ATOM   8541  C  CG1 . VAL H  1 114 ? 84.127  70.838  -15.274 1.00 22.61 ? 87  VAL H CG1 1 
ATOM   8542  C  CG2 . VAL H  1 114 ? 85.010  70.170  -17.551 1.00 23.53 ? 87  VAL H CG2 1 
ATOM   8543  N  N   . THR H  1 115 ? 82.184  67.636  -17.943 1.00 22.25 ? 88  THR H N   1 
ATOM   8544  C  CA  . THR H  1 115 ? 81.852  66.705  -19.042 1.00 21.77 ? 88  THR H CA  1 
ATOM   8545  C  C   . THR H  1 115 ? 81.485  67.451  -20.283 1.00 20.95 ? 88  THR H C   1 
ATOM   8546  O  O   . THR H  1 115 ? 80.515  68.239  -20.291 1.00 21.69 ? 88  THR H O   1 
ATOM   8547  C  CB  . THR H  1 115 ? 80.664  65.774  -18.604 1.00 21.86 ? 88  THR H CB  1 
ATOM   8548  O  OG1 . THR H  1 115 ? 81.032  65.067  -17.427 1.00 24.37 ? 88  THR H OG1 1 
ATOM   8549  C  CG2 . THR H  1 115 ? 80.358  64.757  -19.676 1.00 20.69 ? 88  THR H CG2 1 
ATOM   8550  N  N   . ALA H  1 116 ? 82.254  67.233  -21.355 1.00 19.36 ? 89  ALA H N   1 
ATOM   8551  C  CA  . ALA H  1 116 ? 81.920  67.867  -22.605 1.00 19.28 ? 89  ALA H CA  1 
ATOM   8552  C  C   . ALA H  1 116 ? 80.978  66.955  -23.394 1.00 23.21 ? 89  ALA H C   1 
ATOM   8553  O  O   . ALA H  1 116 ? 81.219  65.736  -23.464 1.00 22.65 ? 89  ALA H O   1 
ATOM   8554  C  CB  . ALA H  1 116 ? 83.214  68.107  -23.413 1.00 22.72 ? 89  ALA H CB  1 
ATOM   8555  N  N   . ASP H  1 117 ? 79.954  67.545  -24.013 1.00 23.54 ? 90  ASP H N   1 
ATOM   8556  C  CA  . ASP H  1 117 ? 78.993  66.801  -24.820 1.00 25.25 ? 90  ASP H CA  1 
ATOM   8557  C  C   . ASP H  1 117 ? 79.581  66.493  -26.218 1.00 25.00 ? 90  ASP H C   1 
ATOM   8558  O  O   . ASP H  1 117 ? 80.736  66.822  -26.468 1.00 23.53 ? 90  ASP H O   1 
ATOM   8559  C  CB  . ASP H  1 117 ? 77.645  67.544  -24.921 1.00 25.18 ? 90  ASP H CB  1 
ATOM   8560  C  CG  . ASP H  1 117 ? 77.723  68.879  -25.697 1.00 31.44 ? 90  ASP H CG  1 
ATOM   8561  O  OD1 . ASP H  1 117 ? 78.716  69.186  -26.400 1.00 30.09 ? 90  ASP H OD1 1 
ATOM   8562  O  OD2 . ASP H  1 117 ? 76.729  69.631  -25.594 1.00 30.96 ? 90  ASP H OD2 1 
ATOM   8563  N  N   . LYS H  1 118 ? 78.757  65.920  -27.109 1.00 26.13 ? 91  LYS H N   1 
ATOM   8564  C  CA  . LYS H  1 118 ? 79.177  65.522  -28.463 1.00 30.82 ? 91  LYS H CA  1 
ATOM   8565  C  C   . LYS H  1 118 ? 79.676  66.687  -29.281 1.00 34.53 ? 91  LYS H C   1 
ATOM   8566  O  O   . LYS H  1 118 ? 80.457  66.447  -30.177 1.00 34.08 ? 91  LYS H O   1 
ATOM   8567  C  CB  . LYS H  1 118 ? 78.033  64.868  -29.260 1.00 33.54 ? 91  LYS H CB  1 
ATOM   8568  C  CG  . LYS H  1 118 ? 77.663  63.532  -28.695 1.00 39.41 ? 91  LYS H CG  1 
ATOM   8569  C  CD  . LYS H  1 118 ? 76.836  62.655  -29.623 1.00 43.47 ? 91  LYS H CD  1 
ATOM   8570  C  CE  . LYS H  1 118 ? 76.598  61.325  -28.909 1.00 47.24 ? 91  LYS H CE  1 
ATOM   8571  N  NZ  . LYS H  1 118 ? 75.648  60.442  -29.632 1.00 48.34 ? 91  LYS H NZ  1 
ATOM   8572  N  N   . ASP H  1 119 ? 79.186  67.910  -29.011 1.00 32.63 ? 92  ASP H N   1 
ATOM   8573  C  CA  . ASP H  1 119 ? 79.626  69.108  -29.732 1.00 33.83 ? 92  ASP H CA  1 
ATOM   8574  C  C   . ASP H  1 119 ? 80.842  69.763  -29.074 1.00 33.61 ? 92  ASP H C   1 
ATOM   8575  O  O   . ASP H  1 119 ? 81.228  70.852  -29.474 1.00 30.36 ? 92  ASP H O   1 
ATOM   8576  C  CB  . ASP H  1 119 ? 78.516  70.159  -29.821 1.00 37.38 ? 92  ASP H CB  1 
ATOM   8577  C  CG  . ASP H  1 119 ? 77.329  69.680  -30.619 1.00 44.20 ? 92  ASP H CG  1 
ATOM   8578  O  OD1 . ASP H  1 119 ? 77.518  68.933  -31.611 1.00 44.25 ? 92  ASP H OD1 1 
ATOM   8579  O  OD2 . ASP H  1 119 ? 76.200  70.020  -30.226 1.00 44.81 ? 92  ASP H OD2 1 
ATOM   8580  N  N   . GLY H  1 120 ? 81.408  69.135  -28.053 1.00 29.09 ? 93  GLY H N   1 
ATOM   8581  C  CA  . GLY H  1 120 ? 82.618  69.652  -27.405 1.00 28.63 ? 93  GLY H CA  1 
ATOM   8582  C  C   . GLY H  1 120 ? 82.376  70.741  -26.377 1.00 25.96 ? 93  GLY H C   1 
ATOM   8583  O  O   . GLY H  1 120 ? 83.327  71.440  -25.960 1.00 25.49 ? 93  GLY H O   1 
ATOM   8584  N  N   . VAL H  1 121 ? 81.127  70.854  -25.903 1.00 23.58 ? 94  VAL H N   1 
ATOM   8585  C  CA  . VAL H  1 121 ? 80.758  71.919  -24.956 1.00 24.14 ? 94  VAL H CA  1 
ATOM   8586  C  C   . VAL H  1 121 ? 80.521  71.336  -23.559 1.00 23.91 ? 94  VAL H C   1 
ATOM   8587  O  O   . VAL H  1 121 ? 79.764  70.336  -23.389 1.00 23.39 ? 94  VAL H O   1 
ATOM   8588  C  CB  . VAL H  1 121 ? 79.507  72.703  -25.409 1.00 24.77 ? 94  VAL H CB  1 
ATOM   8589  C  CG1 . VAL H  1 121 ? 79.092  73.723  -24.336 1.00 23.17 ? 94  VAL H CG1 1 
ATOM   8590  C  CG2 . VAL H  1 121 ? 79.767  73.378  -26.747 1.00 27.06 ? 94  VAL H CG2 1 
ATOM   8591  N  N   . ALA H  1 122 ? 81.251  71.865  -22.578 1.00 23.48 ? 95  ALA H N   1 
ATOM   8592  C  CA  . ALA H  1 122 ? 81.050  71.456  -21.203 1.00 24.48 ? 95  ALA H CA  1 
ATOM   8593  C  C   . ALA H  1 122 ? 80.401  72.617  -20.444 1.00 27.41 ? 95  ALA H C   1 
ATOM   8594  O  O   . ALA H  1 122 ? 81.049  73.622  -20.148 1.00 26.29 ? 95  ALA H O   1 
ATOM   8595  C  CB  . ALA H  1 122 ? 82.370  71.020  -20.545 1.00 24.85 ? 95  ALA H CB  1 
ATOM   8596  N  N   . ASP H  1 123 ? 79.116  72.478  -20.148 1.00 24.84 ? 96  ASP H N   1 
ATOM   8597  C  CA  . ASP H  1 123 ? 78.434  73.381  -19.210 1.00 25.22 ? 96  ASP H CA  1 
ATOM   8598  C  C   . ASP H  1 123 ? 78.806  73.011  -17.781 1.00 25.95 ? 96  ASP H C   1 
ATOM   8599  O  O   . ASP H  1 123 ? 78.582  71.902  -17.314 1.00 30.78 ? 96  ASP H O   1 
ATOM   8600  C  CB  . ASP H  1 123 ? 76.914  73.373  -19.458 1.00 27.97 ? 96  ASP H CB  1 
ATOM   8601  C  CG  . ASP H  1 123 ? 76.547  74.020  -20.783 1.00 34.40 ? 96  ASP H CG  1 
ATOM   8602  O  OD1 . ASP H  1 123 ? 77.247  74.989  -21.218 1.00 32.09 ? 96  ASP H OD1 1 
ATOM   8603  O  OD2 . ASP H  1 123 ? 75.561  73.579  -21.420 1.00 36.09 ? 96  ASP H OD2 1 
ATOM   8604  N  N   . VAL H  1 124 ? 79.418  73.951  -17.073 1.00 21.20 ? 97  VAL H N   1 
ATOM   8605  C  CA  . VAL H  1 124 ? 79.946  73.658  -15.766 1.00 21.02 ? 97  VAL H CA  1 
ATOM   8606  C  C   . VAL H  1 124 ? 78.938  74.149  -14.732 1.00 22.18 ? 97  VAL H C   1 
ATOM   8607  O  O   . VAL H  1 124 ? 78.468  75.316  -14.762 1.00 21.79 ? 97  VAL H O   1 
ATOM   8608  C  CB  . VAL H  1 124 ? 81.313  74.382  -15.577 1.00 21.61 ? 97  VAL H CB  1 
ATOM   8609  C  CG1 . VAL H  1 124 ? 81.851  74.155  -14.155 1.00 22.66 ? 97  VAL H CG1 1 
ATOM   8610  C  CG2 . VAL H  1 124 ? 82.294  73.833  -16.607 1.00 22.30 ? 97  VAL H CG2 1 
ATOM   8611  N  N   . SER H  1 125 ? 78.652  73.289  -13.781 1.00 24.01 ? 98  SER H N   1 
ATOM   8612  C  CA  . SER H  1 125 ? 77.806  73.684  -12.677 1.00 24.74 ? 98  SER H CA  1 
ATOM   8613  C  C   . SER H  1 125 ? 78.237  72.890  -11.472 1.00 26.76 ? 98  SER H C   1 
ATOM   8614  O  O   . SER H  1 125 ? 78.004  71.650  -11.374 1.00 28.20 ? 98  SER H O   1 
ATOM   8615  C  CB  . SER H  1 125 ? 76.329  73.391  -13.039 1.00 28.44 ? 98  SER H CB  1 
ATOM   8616  O  OG  . SER H  1 125 ? 75.507  73.816  -11.974 1.00 28.83 ? 98  SER H OG  1 
ATOM   8617  N  N   . ILE H  1 126 ? 78.842  73.595  -10.526 1.00 26.45 ? 99  ILE H N   1 
ATOM   8618  C  CA  . ILE H  1 126 ? 79.507  72.978  -9.374  1.00 26.71 ? 99  ILE H CA  1 
ATOM   8619  C  C   . ILE H  1 126 ? 79.181  73.821  -8.144  1.00 28.67 ? 99  ILE H C   1 
ATOM   8620  O  O   . ILE H  1 126 ? 79.099  75.055  -8.242  1.00 26.29 ? 99  ILE H O   1 
ATOM   8621  C  CB  . ILE H  1 126 ? 81.047  72.948  -9.603  1.00 27.76 ? 99  ILE H CB  1 
ATOM   8622  C  CG1 . ILE H  1 126 ? 81.402  71.924  -10.687 1.00 28.04 ? 99  ILE H CG1 1 
ATOM   8623  C  CG2 . ILE H  1 126 ? 81.778  72.605  -8.315  1.00 26.87 ? 99  ILE H CG2 1 
ATOM   8624  C  CD1 . ILE H  1 126 ? 82.870  71.913  -11.106 1.00 25.65 ? 99  ILE H CD1 1 
ATOM   8625  N  N   . GLU H  1 127 ? 78.963  73.166  -6.999  1.00 27.09 ? 100 GLU H N   1 
ATOM   8626  C  CA  . GLU H  1 127 ? 78.976  73.849  -5.720  1.00 31.01 ? 100 GLU H CA  1 
ATOM   8627  C  C   . GLU H  1 127 ? 80.088  73.214  -4.898  1.00 31.55 ? 100 GLU H C   1 
ATOM   8628  O  O   . GLU H  1 127 ? 80.174  71.970  -4.800  1.00 30.24 ? 100 GLU H O   1 
ATOM   8629  C  CB  . GLU H  1 127 ? 77.643  73.761  -4.992  1.00 32.91 ? 100 GLU H CB  1 
ATOM   8630  C  CG  . GLU H  1 127 ? 77.726  74.542  -3.696  1.00 40.69 ? 100 GLU H CG  1 
ATOM   8631  C  CD  . GLU H  1 127 ? 76.409  75.164  -3.292  1.00 49.12 ? 100 GLU H CD  1 
ATOM   8632  O  OE1 . GLU H  1 127 ? 75.771  74.673  -2.328  1.00 44.15 ? 100 GLU H OE1 1 
ATOM   8633  O  OE2 . GLU H  1 127 ? 76.023  76.160  -3.942  1.00 54.64 ? 100 GLU H OE2 1 
ATOM   8634  N  N   . ASP H  1 128 ? 80.984  74.034  -4.346  1.00 28.15 ? 101 ASP H N   1 
ATOM   8635  C  CA  . ASP H  1 128 ? 82.135  73.469  -3.617  1.00 29.25 ? 101 ASP H CA  1 
ATOM   8636  C  C   . ASP H  1 128 ? 82.355  74.188  -2.296  1.00 33.02 ? 101 ASP H C   1 
ATOM   8637  O  O   . ASP H  1 128 ? 82.322  75.436  -2.252  1.00 33.41 ? 101 ASP H O   1 
ATOM   8638  C  CB  . ASP H  1 128 ? 83.398  73.444  -4.475  1.00 31.03 ? 101 ASP H CB  1 
ATOM   8639  C  CG  . ASP H  1 128 ? 84.532  72.600  -3.827  1.00 34.98 ? 101 ASP H CG  1 
ATOM   8640  O  OD1 . ASP H  1 128 ? 84.522  71.350  -3.953  1.00 34.45 ? 101 ASP H OD1 1 
ATOM   8641  O  OD2 . ASP H  1 128 ? 85.399  73.191  -3.130  1.00 31.71 ? 101 ASP H OD2 1 
ATOM   8642  N  N   A SER H  1 129 ? 82.560  73.419  -1.228  0.50 34.24 ? 102 SER H N   1 
ATOM   8643  N  N   B SER H  1 129 ? 82.566  73.429  -1.224  0.50 34.01 ? 102 SER H N   1 
ATOM   8644  C  CA  A SER H  1 129 ? 82.716  73.999  0.114   0.50 37.47 ? 102 SER H CA  1 
ATOM   8645  C  CA  B SER H  1 129 ? 82.713  74.031  0.111   0.50 37.06 ? 102 SER H CA  1 
ATOM   8646  C  C   A SER H  1 129 ? 84.123  73.940  0.687   0.50 37.05 ? 102 SER H C   1 
ATOM   8647  C  C   B SER H  1 129 ? 84.155  74.191  0.580   0.50 36.94 ? 102 SER H C   1 
ATOM   8648  O  O   A SER H  1 129 ? 84.312  74.201  1.874   0.50 38.90 ? 102 SER H O   1 
ATOM   8649  O  O   B SER H  1 129 ? 84.402  74.845  1.596   0.50 39.17 ? 102 SER H O   1 
ATOM   8650  C  CB  A SER H  1 129 ? 81.742  73.376  1.114   0.50 39.33 ? 102 SER H CB  1 
ATOM   8651  C  CB  B SER H  1 129 ? 81.930  73.247  1.166   0.50 38.36 ? 102 SER H CB  1 
ATOM   8652  O  OG  A SER H  1 129 ? 80.468  73.975  0.994   0.50 40.99 ? 102 SER H OG  1 
ATOM   8653  O  OG  B SER H  1 129 ? 82.337  71.894  1.182   0.50 39.40 ? 102 SER H OG  1 
ATOM   8654  N  N   . VAL H  1 130 ? 85.093  73.601  -0.150  1.00 34.28 ? 103 VAL H N   1 
ATOM   8655  C  CA  . VAL H  1 130 ? 86.495  73.617  0.247   1.00 34.36 ? 103 VAL H CA  1 
ATOM   8656  C  C   . VAL H  1 130 ? 87.228  74.848  -0.318  1.00 35.32 ? 103 VAL H C   1 
ATOM   8657  O  O   . VAL H  1 130 ? 87.915  75.550  0.429   1.00 34.24 ? 103 VAL H O   1 
ATOM   8658  C  CB  . VAL H  1 130 ? 87.193  72.294  -0.113  1.00 35.28 ? 103 VAL H CB  1 
ATOM   8659  C  CG1 . VAL H  1 130 ? 88.699  72.345  0.141   1.00 36.30 ? 103 VAL H CG1 1 
ATOM   8660  C  CG2 . VAL H  1 130 ? 86.559  71.161  0.690   1.00 35.57 ? 103 VAL H CG2 1 
ATOM   8661  N  N   . ILE H  1 131 ? 87.078  75.136  -1.613  1.00 32.28 ? 104 ILE H N   1 
ATOM   8662  C  CA  . ILE H  1 131 ? 87.623  76.401  -2.163  1.00 29.72 ? 104 ILE H CA  1 
ATOM   8663  C  C   . ILE H  1 131 ? 86.949  77.590  -1.492  1.00 31.80 ? 104 ILE H C   1 
ATOM   8664  O  O   . ILE H  1 131 ? 85.845  77.468  -0.929  1.00 33.25 ? 104 ILE H O   1 
ATOM   8665  C  CB  . ILE H  1 131 ? 87.472  76.523  -3.683  1.00 30.12 ? 104 ILE H CB  1 
ATOM   8666  C  CG1 . ILE H  1 131 ? 85.967  76.561  -4.064  1.00 27.04 ? 104 ILE H CG1 1 
ATOM   8667  C  CG2 . ILE H  1 131 ? 88.311  75.466  -4.386  1.00 30.67 ? 104 ILE H CG2 1 
ATOM   8668  C  CD1 . ILE H  1 131 ? 85.699  76.842  -5.531  1.00 24.91 ? 104 ILE H CD1 1 
ATOM   8669  N  N   . SER H  1 132 ? 87.609  78.751  -1.528  1.00 28.89 ? 105 SER H N   1 
ATOM   8670  C  CA  . SER H  1 132 ? 87.000  79.929  -0.979  1.00 29.43 ? 105 SER H CA  1 
ATOM   8671  C  C   . SER H  1 132 ? 87.423  81.160  -1.773  1.00 28.03 ? 105 SER H C   1 
ATOM   8672  O  O   . SER H  1 132 ? 88.426  81.135  -2.515  1.00 27.79 ? 105 SER H O   1 
ATOM   8673  C  CB  . SER H  1 132 ? 87.406  80.089  0.496   1.00 30.75 ? 105 SER H CB  1 
ATOM   8674  O  OG  . SER H  1 132 ? 86.632  81.139  1.038   1.00 30.67 ? 105 SER H OG  1 
ATOM   8675  N  N   . LEU H  1 133 ? 86.655  82.234  -1.634  1.00 30.36 ? 106 LEU H N   1 
ATOM   8676  C  CA  . LEU H  1 133 ? 87.079  83.519  -2.214  1.00 32.98 ? 106 LEU H CA  1 
ATOM   8677  C  C   . LEU H  1 133 ? 87.767  84.456  -1.198  1.00 35.71 ? 106 LEU H C   1 
ATOM   8678  O  O   . LEU H  1 133 ? 88.079  85.609  -1.531  1.00 34.01 ? 106 LEU H O   1 
ATOM   8679  C  CB  . LEU H  1 133 ? 85.918  84.217  -2.947  1.00 30.72 ? 106 LEU H CB  1 
ATOM   8680  C  CG  . LEU H  1 133 ? 85.285  83.408  -4.076  1.00 27.90 ? 106 LEU H CG  1 
ATOM   8681  C  CD1 . LEU H  1 133 ? 84.256  84.233  -4.833  1.00 27.61 ? 106 LEU H CD1 1 
ATOM   8682  C  CD2 . LEU H  1 133 ? 86.353  82.914  -5.038  1.00 25.41 ? 106 LEU H CD2 1 
ATOM   8683  N  N   . SER H  1 134 ? 88.013  83.946  0.009   1.00 36.90 ? 107 SER H N   1 
ATOM   8684  C  CA  . SER H  1 134 ? 88.768  84.684  1.048   1.00 43.18 ? 107 SER H CA  1 
ATOM   8685  C  C   . SER H  1 134 ? 89.438  83.699  2.031   1.00 44.21 ? 107 SER H C   1 
ATOM   8686  O  O   . SER H  1 134 ? 89.123  82.523  2.024   1.00 40.63 ? 107 SER H O   1 
ATOM   8687  C  CB  . SER H  1 134 ? 87.847  85.677  1.776   1.00 42.26 ? 107 SER H CB  1 
ATOM   8688  O  OG  . SER H  1 134 ? 86.968  85.008  2.684   1.00 49.15 ? 107 SER H OG  1 
ATOM   8689  N  N   . GLY H  1 135 ? 90.378  84.168  2.859   1.00 44.03 ? 108 GLY H N   1 
ATOM   8690  C  CA  . GLY H  1 135 ? 91.047  83.287  3.827   1.00 41.31 ? 108 GLY H CA  1 
ATOM   8691  C  C   . GLY H  1 135 ? 92.142  82.404  3.253   1.00 43.54 ? 108 GLY H C   1 
ATOM   8692  O  O   . GLY H  1 135 ? 92.637  82.639  2.160   1.00 47.03 ? 108 GLY H O   1 
ATOM   8693  N  N   . ASP H  1 136 ? 92.514  81.367  4.000   1.00 46.97 ? 109 ASP H N   1 
ATOM   8694  C  CA  . ASP H  1 136 ? 93.588  80.420  3.620   1.00 48.18 ? 109 ASP H CA  1 
ATOM   8695  C  C   . ASP H  1 136 ? 93.310  79.569  2.384   1.00 47.43 ? 109 ASP H C   1 
ATOM   8696  O  O   . ASP H  1 136 ? 94.243  79.077  1.734   1.00 43.17 ? 109 ASP H O   1 
ATOM   8697  C  CB  . ASP H  1 136 ? 93.845  79.429  4.773   1.00 58.72 ? 109 ASP H CB  1 
ATOM   8698  C  CG  . ASP H  1 136 ? 94.419  80.098  6.016   1.00 68.98 ? 109 ASP H CG  1 
ATOM   8699  O  OD1 . ASP H  1 136 ? 94.844  81.277  5.931   1.00 68.61 ? 109 ASP H OD1 1 
ATOM   8700  O  OD2 . ASP H  1 136 ? 94.445  79.433  7.082   1.00 74.14 ? 109 ASP H OD2 1 
ATOM   8701  N  N   . HIS H  1 137 ? 92.027  79.338  2.101   1.00 45.19 ? 110 HIS H N   1 
ATOM   8702  C  CA  . HIS H  1 137 ? 91.644  78.512  0.951   1.00 44.07 ? 110 HIS H CA  1 
ATOM   8703  C  C   . HIS H  1 137 ? 91.357  79.397  -0.268  1.00 42.48 ? 110 HIS H C   1 
ATOM   8704  O  O   . HIS H  1 137 ? 90.902  78.907  -1.322  1.00 37.98 ? 110 HIS H O   1 
ATOM   8705  C  CB  . HIS H  1 137 ? 90.448  77.595  1.329   1.00 44.40 ? 110 HIS H CB  1 
ATOM   8706  C  CG  . HIS H  1 137 ? 90.793  76.515  2.318   1.00 50.00 ? 110 HIS H CG  1 
ATOM   8707  N  ND1 . HIS H  1 137 ? 89.929  75.476  2.627   1.00 53.40 ? 110 HIS H ND1 1 
ATOM   8708  C  CD2 . HIS H  1 137 ? 91.915  76.300  3.057   1.00 49.27 ? 110 HIS H CD2 1 
ATOM   8709  C  CE1 . HIS H  1 137 ? 90.500  74.680  3.519   1.00 49.78 ? 110 HIS H CE1 1 
ATOM   8710  N  NE2 . HIS H  1 137 ? 91.705  75.154  3.791   1.00 49.17 ? 110 HIS H NE2 1 
ATOM   8711  N  N   . CYS H  1 138 ? 91.647  80.698  -0.128  1.00 37.65 ? 111 CYS H N   1 
ATOM   8712  C  CA  . CYS H  1 138 ? 91.328  81.701  -1.156  1.00 34.76 ? 111 CYS H CA  1 
ATOM   8713  C  C   . CYS H  1 138 ? 91.963  81.353  -2.497  1.00 33.80 ? 111 CYS H C   1 
ATOM   8714  O  O   . CYS H  1 138 ? 93.168  81.090  -2.584  1.00 32.36 ? 111 CYS H O   1 
ATOM   8715  C  CB  . CYS H  1 138 ? 91.734  83.120  -0.698  1.00 37.69 ? 111 CYS H CB  1 
ATOM   8716  S  SG  . CYS H  1 138 ? 91.424  84.367  -1.970  1.00 40.74 ? 111 CYS H SG  1 
ATOM   8717  N  N   . ILE H  1 139 ? 91.147  81.341  -3.555  1.00 30.82 ? 112 ILE H N   1 
ATOM   8718  C  CA  . ILE H  1 139 ? 91.629  80.983  -4.901  1.00 28.46 ? 112 ILE H CA  1 
ATOM   8719  C  C   . ILE H  1 139 ? 91.801  82.205  -5.838  1.00 25.20 ? 112 ILE H C   1 
ATOM   8720  O  O   . ILE H  1 139 ? 92.195  82.047  -6.995  1.00 25.28 ? 112 ILE H O   1 
ATOM   8721  C  CB  . ILE H  1 139 ? 90.722  79.892  -5.576  1.00 29.05 ? 112 ILE H CB  1 
ATOM   8722  C  CG1 . ILE H  1 139 ? 89.300  80.445  -5.822  1.00 30.44 ? 112 ILE H CG1 1 
ATOM   8723  C  CG2 . ILE H  1 139 ? 90.755  78.599  -4.741  1.00 29.21 ? 112 ILE H CG2 1 
ATOM   8724  C  CD1 . ILE H  1 139 ? 88.326  79.481  -6.531  1.00 29.09 ? 112 ILE H CD1 1 
ATOM   8725  N  N   . ILE H  1 140 ? 91.428  83.401  -5.383  1.00 28.63 ? 113 ILE H N   1 
ATOM   8726  C  CA  . ILE H  1 140 ? 91.602  84.629  -6.203  1.00 27.80 ? 113 ILE H CA  1 
ATOM   8727  C  C   . ILE H  1 140 ? 93.087  84.810  -6.455  1.00 29.35 ? 113 ILE H C   1 
ATOM   8728  O  O   . ILE H  1 140 ? 93.843  84.748  -5.519  1.00 29.52 ? 113 ILE H O   1 
ATOM   8729  C  CB  . ILE H  1 140 ? 91.121  85.929  -5.480  1.00 32.04 ? 113 ILE H CB  1 
ATOM   8730  C  CG1 . ILE H  1 140 ? 89.653  85.877  -5.066  1.00 35.13 ? 113 ILE H CG1 1 
ATOM   8731  C  CG2 . ILE H  1 140 ? 91.439  87.174  -6.334  1.00 30.05 ? 113 ILE H CG2 1 
ATOM   8732  C  CD1 . ILE H  1 140 ? 88.721  85.550  -6.168  1.00 37.49 ? 113 ILE H CD1 1 
ATOM   8733  N  N   . GLY H  1 141 ? 93.495  84.996  -7.704  1.00 29.69 ? 114 GLY H N   1 
ATOM   8734  C  CA  . GLY H  1 141 ? 94.892  85.229  -8.021  1.00 31.41 ? 114 GLY H CA  1 
ATOM   8735  C  C   . GLY H  1 141 ? 95.621  83.953  -8.379  1.00 30.24 ? 114 GLY H C   1 
ATOM   8736  O  O   . GLY H  1 141 ? 96.812  83.992  -8.718  1.00 29.46 ? 114 GLY H O   1 
ATOM   8737  N  N   . ARG H  1 142 ? 94.917  82.818  -8.316  1.00 27.80 ? 115 ARG H N   1 
ATOM   8738  C  CA  . ARG H  1 142 ? 95.487  81.534  -8.749  1.00 28.01 ? 115 ARG H CA  1 
ATOM   8739  C  C   . ARG H  1 142 ? 94.926  81.183  -10.123 1.00 29.83 ? 115 ARG H C   1 
ATOM   8740  O  O   . ARG H  1 142 ? 94.247  82.015  -10.702 1.00 30.20 ? 115 ARG H O   1 
ATOM   8741  C  CB  . ARG H  1 142 ? 95.163  80.494  -7.690  1.00 30.58 ? 115 ARG H CB  1 
ATOM   8742  C  CG  . ARG H  1 142 ? 95.617  80.997  -6.337  1.00 32.11 ? 115 ARG H CG  1 
ATOM   8743  C  CD  . ARG H  1 142 ? 95.644  79.918  -5.278  1.00 35.96 ? 115 ARG H CD  1 
ATOM   8744  N  NE  . ARG H  1 142 ? 95.983  80.449  -3.960  1.00 34.50 ? 115 ARG H NE  1 
ATOM   8745  C  CZ  . ARG H  1 142 ? 97.220  80.634  -3.492  1.00 33.28 ? 115 ARG H CZ  1 
ATOM   8746  N  NH1 . ARG H  1 142 ? 98.293  80.334  -4.201  1.00 33.12 ? 115 ARG H NH1 1 
ATOM   8747  N  NH2 . ARG H  1 142 ? 97.357  81.123  -2.277  1.00 35.17 ? 115 ARG H NH2 1 
ATOM   8748  N  N   . THR H  1 143 ? 95.207  79.978  -10.662 1.00 26.94 ? 116 THR H N   1 
ATOM   8749  C  CA  . THR H  1 143 ? 94.895  79.677  -12.037 1.00 29.15 ? 116 THR H CA  1 
ATOM   8750  C  C   . THR H  1 143 ? 93.901  78.505  -12.077 1.00 28.31 ? 116 THR H C   1 
ATOM   8751  O  O   . THR H  1 143 ? 94.087  77.515  -11.381 1.00 28.05 ? 116 THR H O   1 
ATOM   8752  C  CB  . THR H  1 143 ? 96.147  79.301  -12.864 1.00 30.69 ? 116 THR H CB  1 
ATOM   8753  O  OG1 . THR H  1 143 ? 96.991  80.455  -13.039 1.00 32.89 ? 116 THR H OG1 1 
ATOM   8754  C  CG2 . THR H  1 143 ? 95.763  78.833  -14.276 1.00 29.06 ? 116 THR H CG2 1 
ATOM   8755  N  N   . LEU H  1 144 ? 92.885  78.634  -12.920 1.00 26.11 ? 117 LEU H N   1 
ATOM   8756  C  CA  . LEU H  1 144 ? 91.936  77.522  -13.177 1.00 24.32 ? 117 LEU H CA  1 
ATOM   8757  C  C   . LEU H  1 144 ? 92.385  76.900  -14.442 1.00 23.39 ? 117 LEU H C   1 
ATOM   8758  O  O   . LEU H  1 144 ? 92.637  77.600  -15.435 1.00 23.70 ? 117 LEU H O   1 
ATOM   8759  C  CB  . LEU H  1 144 ? 90.499  78.066  -13.330 1.00 23.52 ? 117 LEU H CB  1 
ATOM   8760  C  CG  . LEU H  1 144 ? 89.367  77.035  -13.462 1.00 24.65 ? 117 LEU H CG  1 
ATOM   8761  C  CD1 . LEU H  1 144 ? 89.167  76.232  -12.183 1.00 24.58 ? 117 LEU H CD1 1 
ATOM   8762  C  CD2 . LEU H  1 144 ? 88.101  77.816  -13.789 1.00 23.82 ? 117 LEU H CD2 1 
ATOM   8763  N  N   . VAL H  1 145 ? 92.476  75.561  -14.432 1.00 21.53 ? 118 VAL H N   1 
ATOM   8764  C  CA  . VAL H  1 145 ? 92.937  74.806  -15.577 1.00 23.01 ? 118 VAL H CA  1 
ATOM   8765  C  C   . VAL H  1 145 ? 91.956  73.671  -15.931 1.00 21.58 ? 118 VAL H C   1 
ATOM   8766  O  O   . VAL H  1 145 ? 91.486  72.970  -15.042 1.00 24.12 ? 118 VAL H O   1 
ATOM   8767  C  CB  . VAL H  1 145 ? 94.303  74.125  -15.282 1.00 25.09 ? 118 VAL H CB  1 
ATOM   8768  C  CG1 . VAL H  1 145 ? 94.836  73.421  -16.537 1.00 23.97 ? 118 VAL H CG1 1 
ATOM   8769  C  CG2 . VAL H  1 145 ? 95.312  75.181  -14.845 1.00 24.75 ? 118 VAL H CG2 1 
ATOM   8770  N  N   . VAL H  1 146 ? 91.683  73.539  -17.209 1.00 22.20 ? 119 VAL H N   1 
ATOM   8771  C  CA  . VAL H  1 146 ? 90.939  72.363  -17.704 1.00 25.98 ? 119 VAL H CA  1 
ATOM   8772  C  C   . VAL H  1 146 ? 91.911  71.445  -18.464 1.00 27.88 ? 119 VAL H C   1 
ATOM   8773  O  O   . VAL H  1 146 ? 92.679  71.907  -19.322 1.00 26.18 ? 119 VAL H O   1 
ATOM   8774  C  CB  . VAL H  1 146 ? 89.729  72.730  -18.565 1.00 24.50 ? 119 VAL H CB  1 
ATOM   8775  C  CG1 . VAL H  1 146 ? 90.098  73.575  -19.759 1.00 24.80 ? 119 VAL H CG1 1 
ATOM   8776  C  CG2 . VAL H  1 146 ? 88.964  71.459  -19.024 1.00 23.32 ? 119 VAL H CG2 1 
ATOM   8777  N  N   . HIS H  1 147 ? 91.872  70.167  -18.104 1.00 27.30 ? 120 HIS H N   1 
ATOM   8778  C  CA  . HIS H  1 147 ? 92.865  69.184  -18.570 1.00 26.99 ? 120 HIS H CA  1 
ATOM   8779  C  C   . HIS H  1 147 ? 92.397  68.293  -19.711 1.00 30.65 ? 120 HIS H C   1 
ATOM   8780  O  O   . HIS H  1 147 ? 91.194  68.182  -20.028 1.00 31.05 ? 120 HIS H O   1 
ATOM   8781  C  CB  . HIS H  1 147 ? 93.299  68.305  -17.412 1.00 25.74 ? 120 HIS H CB  1 
ATOM   8782  C  CG  . HIS H  1 147 ? 94.112  69.014  -16.386 1.00 29.02 ? 120 HIS H CG  1 
ATOM   8783  N  ND1 . HIS H  1 147 ? 95.492  69.000  -16.402 1.00 31.93 ? 120 HIS H ND1 1 
ATOM   8784  C  CD2 . HIS H  1 147 ? 93.754  69.762  -15.317 1.00 30.89 ? 120 HIS H CD2 1 
ATOM   8785  C  CE1 . HIS H  1 147 ? 95.951  69.718  -15.388 1.00 31.98 ? 120 HIS H CE1 1 
ATOM   8786  N  NE2 . HIS H  1 147 ? 94.920  70.180  -14.706 1.00 33.83 ? 120 HIS H NE2 1 
ATOM   8787  N  N   . GLU H  1 148 ? 93.377  67.652  -20.331 1.00 27.21 ? 121 GLU H N   1 
ATOM   8788  C  CA  . GLU H  1 148 ? 93.214  66.844  -21.525 1.00 28.67 ? 121 GLU H CA  1 
ATOM   8789  C  C   . GLU H  1 148 ? 92.263  65.636  -21.319 1.00 25.49 ? 121 GLU H C   1 
ATOM   8790  O  O   . GLU H  1 148 ? 91.518  65.276  -22.238 1.00 30.84 ? 121 GLU H O   1 
ATOM   8791  C  CB  . GLU H  1 148 ? 94.603  66.258  -21.853 1.00 32.73 ? 121 GLU H CB  1 
ATOM   8792  C  CG  . GLU H  1 148 ? 94.718  65.498  -23.156 1.00 38.14 ? 121 GLU H CG  1 
ATOM   8793  C  CD  . GLU H  1 148 ? 96.119  64.866  -23.294 1.00 45.99 ? 121 GLU H CD  1 
ATOM   8794  O  OE1 . GLU H  1 148 ? 96.468  64.458  -24.425 1.00 45.81 ? 121 GLU H OE1 1 
ATOM   8795  O  OE2 . GLU H  1 148 ? 96.852  64.779  -22.260 1.00 41.01 ? 121 GLU H OE2 1 
ATOM   8796  N  N   . LYS H  1 149 ? 92.323  65.037  -20.142 1.00 30.20 ? 122 LYS H N   1 
ATOM   8797  C  CA  . LYS H  1 149 ? 91.768  63.705  -19.900 1.00 32.09 ? 122 LYS H CA  1 
ATOM   8798  C  C   . LYS H  1 149 ? 91.006  63.715  -18.614 1.00 30.48 ? 122 LYS H C   1 
ATOM   8799  O  O   . LYS H  1 149 ? 91.112  64.663  -17.843 1.00 30.58 ? 122 LYS H O   1 
ATOM   8800  C  CB  . LYS H  1 149 ? 92.911  62.665  -19.722 1.00 32.93 ? 122 LYS H CB  1 
ATOM   8801  C  CG  . LYS H  1 149 ? 93.973  62.660  -20.819 1.00 38.91 ? 122 LYS H CG  1 
ATOM   8802  C  CD  . LYS H  1 149 ? 94.616  61.287  -21.047 1.00 44.20 ? 122 LYS H CD  1 
ATOM   8803  C  CE  . LYS H  1 149 ? 95.215  60.672  -19.784 1.00 49.57 ? 122 LYS H CE  1 
ATOM   8804  N  NZ  . LYS H  1 149 ? 96.114  61.616  -19.060 1.00 55.87 ? 122 LYS H NZ  1 
ATOM   8805  N  N   . ALA H  1 150 ? 90.317  62.598  -18.323 1.00 26.74 ? 123 ALA H N   1 
ATOM   8806  C  CA  . ALA H  1 150 ? 89.601  62.496  -17.068 1.00 29.68 ? 123 ALA H CA  1 
ATOM   8807  C  C   . ALA H  1 150 ? 90.514  62.457  -15.857 1.00 29.70 ? 123 ALA H C   1 
ATOM   8808  O  O   . ALA H  1 150 ? 91.572  61.850  -15.889 1.00 32.78 ? 123 ALA H O   1 
ATOM   8809  C  CB  . ALA H  1 150 ? 88.678  61.284  -17.071 1.00 30.88 ? 123 ALA H CB  1 
ATOM   8810  N  N   . ASP H  1 151 ? 90.092  63.113  -14.786 1.00 25.95 ? 124 ASP H N   1 
ATOM   8811  C  CA  . ASP H  1 151 ? 90.699  62.984  -13.490 1.00 31.71 ? 124 ASP H CA  1 
ATOM   8812  C  C   . ASP H  1 151 ? 90.170  61.674  -12.855 1.00 32.81 ? 124 ASP H C   1 
ATOM   8813  O  O   . ASP H  1 151 ? 88.943  61.496  -12.776 1.00 28.66 ? 124 ASP H O   1 
ATOM   8814  C  CB  . ASP H  1 151 ? 90.271  64.204  -12.676 1.00 31.25 ? 124 ASP H CB  1 
ATOM   8815  C  CG  . ASP H  1 151 ? 90.883  64.271  -11.313 1.00 34.36 ? 124 ASP H CG  1 
ATOM   8816  O  OD1 . ASP H  1 151 ? 91.358  63.243  -10.792 1.00 30.49 ? 124 ASP H OD1 1 
ATOM   8817  O  OD2 . ASP H  1 151 ? 90.852  65.383  -10.718 1.00 37.99 ? 124 ASP H OD2 1 
ATOM   8818  N  N   . ASP H  1 152 ? 91.070  60.817  -12.328 1.00 30.84 ? 125 ASP H N   1 
ATOM   8819  C  CA  . ASP H  1 152 ? 90.669  59.520  -11.759 1.00 29.74 ? 125 ASP H CA  1 
ATOM   8820  C  C   . ASP H  1 152 ? 90.340  59.673  -10.299 1.00 33.92 ? 125 ASP H C   1 
ATOM   8821  O  O   . ASP H  1 152 ? 90.084  58.687  -9.546  1.00 31.39 ? 125 ASP H O   1 
ATOM   8822  C  CB  . ASP H  1 152 ? 91.741  58.457  -11.989 1.00 36.18 ? 125 ASP H CB  1 
ATOM   8823  C  CG  . ASP H  1 152 ? 93.079  58.772  -11.267 1.00 34.48 ? 125 ASP H CG  1 
ATOM   8824  O  OD1 . ASP H  1 152 ? 93.095  59.415  -10.172 1.00 36.44 ? 125 ASP H OD1 1 
ATOM   8825  O  OD2 . ASP H  1 152 ? 94.095  58.325  -11.818 1.00 38.82 ? 125 ASP H OD2 1 
ATOM   8826  N  N   . LEU H  1 153 ? 90.366  60.932  -9.885  1.00 29.87 ? 126 LEU H N   1 
ATOM   8827  C  CA  . LEU H  1 153 ? 89.953  61.330  -8.554  1.00 29.14 ? 126 LEU H CA  1 
ATOM   8828  C  C   . LEU H  1 153 ? 90.823  60.689  -7.450  1.00 31.55 ? 126 LEU H C   1 
ATOM   8829  O  O   . LEU H  1 153 ? 90.354  60.498  -6.333  1.00 31.70 ? 126 LEU H O   1 
ATOM   8830  C  CB  . LEU H  1 153 ? 88.475  61.051  -8.325  1.00 28.45 ? 126 LEU H CB  1 
ATOM   8831  C  CG  . LEU H  1 153 ? 87.555  61.614  -9.427  1.00 30.58 ? 126 LEU H CG  1 
ATOM   8832  C  CD1 . LEU H  1 153 ? 86.102  61.272  -9.097  1.00 33.63 ? 126 LEU H CD1 1 
ATOM   8833  C  CD2 . LEU H  1 153 ? 87.702  63.125  -9.631  1.00 29.10 ? 126 LEU H CD2 1 
ATOM   8834  N  N   . GLY H  1 154 ? 92.076  60.396  -7.772  1.00 33.68 ? 127 GLY H N   1 
ATOM   8835  C  CA  . GLY H  1 154 ? 93.001  59.848  -6.759  1.00 40.87 ? 127 GLY H CA  1 
ATOM   8836  C  C   . GLY H  1 154 ? 92.756  58.364  -6.467  1.00 45.00 ? 127 GLY H C   1 
ATOM   8837  O  O   . GLY H  1 154 ? 93.104  57.856  -5.393  1.00 46.17 ? 127 GLY H O   1 
ATOM   8838  N  N   . LYS H  1 155 ? 92.157  57.663  -7.427  1.00 43.63 ? 128 LYS H N   1 
ATOM   8839  C  CA  . LYS H  1 155 ? 91.800  56.257  -7.223  1.00 46.80 ? 128 LYS H CA  1 
ATOM   8840  C  C   . LYS H  1 155 ? 92.352  55.450  -8.358  1.00 43.23 ? 128 LYS H C   1 
ATOM   8841  O  O   . LYS H  1 155 ? 91.824  54.391  -8.656  1.00 43.83 ? 128 LYS H O   1 
ATOM   8842  C  CB  . LYS H  1 155 ? 90.277  56.089  -7.158  1.00 47.36 ? 128 LYS H CB  1 
ATOM   8843  C  CG  . LYS H  1 155 ? 89.675  56.627  -5.873  1.00 49.42 ? 128 LYS H CG  1 
ATOM   8844  C  CD  . LYS H  1 155 ? 88.190  56.832  -6.053  1.00 54.66 ? 128 LYS H CD  1 
ATOM   8845  C  CE  . LYS H  1 155 ? 87.498  56.859  -4.705  1.00 59.09 ? 128 LYS H CE  1 
ATOM   8846  N  NZ  . LYS H  1 155 ? 87.880  58.010  -3.838  1.00 57.45 ? 128 LYS H NZ  1 
ATOM   8847  N  N   . GLY H  1 156 ? 93.390  55.972  -9.022  1.00 36.79 ? 129 GLY H N   1 
ATOM   8848  C  CA  . GLY H  1 156 ? 94.003  55.287  -10.159 1.00 37.82 ? 129 GLY H CA  1 
ATOM   8849  C  C   . GLY H  1 156 ? 94.980  54.195  -9.693  1.00 41.81 ? 129 GLY H C   1 
ATOM   8850  O  O   . GLY H  1 156 ? 95.579  53.532  -10.516 1.00 40.43 ? 129 GLY H O   1 
ATOM   8851  N  N   . GLY H  1 157 ? 95.154  54.063  -8.375  1.00 44.00 ? 130 GLY H N   1 
ATOM   8852  C  CA  . GLY H  1 157 ? 96.050  53.077  -7.773  1.00 52.71 ? 130 GLY H CA  1 
ATOM   8853  C  C   . GLY H  1 157 ? 97.554  53.255  -7.983  1.00 55.54 ? 130 GLY H C   1 
ATOM   8854  O  O   . GLY H  1 157 ? 98.324  52.376  -7.589  1.00 55.57 ? 130 GLY H O   1 
ATOM   8855  N  N   . ASN H  1 158 ? 97.979  54.358  -8.607  1.00 51.12 ? 131 ASN H N   1 
ATOM   8856  C  CA  . ASN H  1 158 ? 99.422  54.645  -8.826  1.00 49.06 ? 131 ASN H CA  1 
ATOM   8857  C  C   . ASN H  1 158 ? 99.864  55.970  -8.196  1.00 50.49 ? 131 ASN H C   1 
ATOM   8858  O  O   . ASN H  1 158 ? 99.040  56.695  -7.600  1.00 49.92 ? 131 ASN H O   1 
ATOM   8859  C  CB  . ASN H  1 158 ? 99.834  54.551  -10.320 1.00 45.11 ? 131 ASN H CB  1 
ATOM   8860  C  CG  . ASN H  1 158 ? 98.993  55.434  -11.245 1.00 52.59 ? 131 ASN H CG  1 
ATOM   8861  O  OD1 . ASN H  1 158 ? 98.676  56.600  -10.938 1.00 46.24 ? 131 ASN H OD1 1 
ATOM   8862  N  ND2 . ASN H  1 158 ? 98.666  54.892  -12.416 1.00 48.26 ? 131 ASN H ND2 1 
ATOM   8863  N  N   . GLU H  1 159 ? 101.160 56.283  -8.307  1.00 50.01 ? 132 GLU H N   1 
ATOM   8864  C  CA  . GLU H  1 159 ? 101.713 57.479  -7.656  1.00 48.97 ? 132 GLU H CA  1 
ATOM   8865  C  C   . GLU H  1 159 ? 101.142 58.791  -8.205  1.00 40.18 ? 132 GLU H C   1 
ATOM   8866  O  O   . GLU H  1 159 ? 100.756 59.681  -7.438  1.00 44.66 ? 132 GLU H O   1 
ATOM   8867  C  CB  . GLU H  1 159 ? 103.249 57.505  -7.741  1.00 49.91 ? 132 GLU H CB  1 
ATOM   8868  C  CG  . GLU H  1 159 ? 103.855 57.876  -6.398  1.00 60.17 ? 132 GLU H CG  1 
ATOM   8869  C  CD  . GLU H  1 159 ? 105.083 58.776  -6.487  1.00 64.38 ? 132 GLU H CD  1 
ATOM   8870  O  OE1 . GLU H  1 159 ? 105.746 58.851  -7.565  1.00 61.92 ? 132 GLU H OE1 1 
ATOM   8871  O  OE2 . GLU H  1 159 ? 105.379 59.417  -5.452  1.00 56.98 ? 132 GLU H OE2 1 
ATOM   8872  N  N   . GLU H  1 160 ? 101.131 58.876  -9.526  1.00 36.06 ? 133 GLU H N   1 
ATOM   8873  C  CA  . GLU H  1 160 ? 100.626 59.990  -10.320 1.00 41.76 ? 133 GLU H CA  1 
ATOM   8874  C  C   . GLU H  1 160 ? 99.163  60.337  -9.963  1.00 43.52 ? 133 GLU H C   1 
ATOM   8875  O  O   . GLU H  1 160 ? 98.803  61.505  -9.794  1.00 41.27 ? 133 GLU H O   1 
ATOM   8876  C  CB  . GLU H  1 160 ? 100.741 59.573  -11.799 1.00 44.03 ? 133 GLU H CB  1 
ATOM   8877  C  CG  . GLU H  1 160 ? 100.750 60.690  -12.835 1.00 49.47 ? 133 GLU H CG  1 
ATOM   8878  C  CD  . GLU H  1 160 ? 101.611 61.896  -12.440 1.00 58.76 ? 133 GLU H CD  1 
ATOM   8879  O  OE1 . GLU H  1 160 ? 102.728 61.726  -11.864 1.00 59.68 ? 133 GLU H OE1 1 
ATOM   8880  O  OE2 . GLU H  1 160 ? 101.153 63.034  -12.701 1.00 52.05 ? 133 GLU H OE2 1 
ATOM   8881  N  N   . SER H  1 161 ? 98.339  59.305  -9.815  1.00 38.06 ? 134 SER H N   1 
ATOM   8882  C  CA  . SER H  1 161 ? 96.959  59.486  -9.369  1.00 40.63 ? 134 SER H CA  1 
ATOM   8883  C  C   . SER H  1 161 ? 96.887  60.259  -8.062  1.00 38.90 ? 134 SER H C   1 
ATOM   8884  O  O   . SER H  1 161 ? 95.970  61.102  -7.900  1.00 32.72 ? 134 SER H O   1 
ATOM   8885  C  CB  . SER H  1 161 ? 96.202  58.140  -9.274  1.00 38.79 ? 134 SER H CB  1 
ATOM   8886  O  OG  . SER H  1 161 ? 94.978  58.250  -8.527  1.00 35.91 ? 134 SER H OG  1 
ATOM   8887  N  N   . THR H  1 162 ? 97.842  60.040  -7.137  1.00 35.29 ? 135 THR H N   1 
ATOM   8888  C  CA  . THR H  1 162 ? 97.783  60.765  -5.863  1.00 35.88 ? 135 THR H CA  1 
ATOM   8889  C  C   . THR H  1 162 ? 98.308  62.220  -6.025  1.00 33.30 ? 135 THR H C   1 
ATOM   8890  O  O   . THR H  1 162 ? 98.218  63.013  -5.085  1.00 34.34 ? 135 THR H O   1 
ATOM   8891  C  CB  . THR H  1 162 ? 98.583  60.082  -4.699  1.00 40.78 ? 135 THR H CB  1 
ATOM   8892  O  OG1 . THR H  1 162 ? 99.990  60.176  -4.993  1.00 45.05 ? 135 THR H OG1 1 
ATOM   8893  C  CG2 . THR H  1 162 ? 98.175  58.625  -4.493  1.00 38.30 ? 135 THR H CG2 1 
ATOM   8894  N  N   . LYS H  1 163 ? 98.846  62.528  -7.203  1.00 35.77 ? 136 LYS H N   1 
ATOM   8895  C  CA  . LYS H  1 163 ? 99.395  63.853  -7.522  1.00 38.98 ? 136 LYS H CA  1 
ATOM   8896  C  C   . LYS H  1 163 ? 98.450  64.687  -8.386  1.00 36.52 ? 136 LYS H C   1 
ATOM   8897  O  O   . LYS H  1 163 ? 97.926  65.707  -7.933  1.00 37.99 ? 136 LYS H O   1 
ATOM   8898  C  CB  . LYS H  1 163 ? 100.765 63.727  -8.214  1.00 41.49 ? 136 LYS H CB  1 
ATOM   8899  C  CG  . LYS H  1 163 ? 101.857 63.272  -7.243  1.00 48.96 ? 136 LYS H CG  1 
ATOM   8900  C  CD  . LYS H  1 163 ? 103.231 63.196  -7.881  1.00 53.52 ? 136 LYS H CD  1 
ATOM   8901  C  CE  . LYS H  1 163 ? 104.291 63.306  -6.791  1.00 60.06 ? 136 LYS H CE  1 
ATOM   8902  N  NZ  . LYS H  1 163 ? 105.672 63.450  -7.338  1.00 62.67 ? 136 LYS H NZ  1 
ATOM   8903  N  N   . THR H  1 164 ? 98.239  64.232  -9.615  1.00 35.09 ? 137 THR H N   1 
ATOM   8904  C  CA  . THR H  1 164 ? 97.460  64.943  -10.598 1.00 36.18 ? 137 THR H CA  1 
ATOM   8905  C  C   . THR H  1 164 ? 96.094  64.292  -10.964 1.00 38.70 ? 137 THR H C   1 
ATOM   8906  O  O   . THR H  1 164 ? 95.344  64.822  -11.818 1.00 35.63 ? 137 THR H O   1 
ATOM   8907  C  CB  . THR H  1 164 ? 98.293  65.075  -11.877 1.00 40.94 ? 137 THR H CB  1 
ATOM   8908  O  OG1 . THR H  1 164 ? 98.533  63.774  -12.426 1.00 38.92 ? 137 THR H OG1 1 
ATOM   8909  C  CG2 . THR H  1 164 ? 99.669  65.742  -11.575 1.00 39.81 ? 137 THR H CG2 1 
ATOM   8910  N  N   . GLY H  1 165 ? 95.799  63.122  -10.387 1.00 34.22 ? 138 GLY H N   1 
ATOM   8911  C  CA  . GLY H  1 165 ? 94.635  62.309  -10.846 1.00 33.95 ? 138 GLY H CA  1 
ATOM   8912  C  C   . GLY H  1 165 ? 94.736  61.790  -12.265 1.00 34.71 ? 138 GLY H C   1 
ATOM   8913  O  O   . GLY H  1 165 ? 93.725  61.352  -12.855 1.00 32.03 ? 138 GLY H O   1 
ATOM   8914  N  N   . ASN H  1 166 ? 95.952  61.833  -12.830 1.00 33.91 ? 139 ASN H N   1 
ATOM   8915  C  CA  . ASN H  1 166 ? 96.218  61.397  -14.209 1.00 32.49 ? 139 ASN H CA  1 
ATOM   8916  C  C   . ASN H  1 166 ? 95.487  62.151  -15.329 1.00 36.26 ? 139 ASN H C   1 
ATOM   8917  O  O   . ASN H  1 166 ? 95.269  61.600  -16.430 1.00 31.71 ? 139 ASN H O   1 
ATOM   8918  C  CB  . ASN H  1 166 ? 95.985  59.865  -14.353 1.00 34.99 ? 139 ASN H CB  1 
ATOM   8919  C  CG  . ASN H  1 166 ? 97.112  59.050  -13.748 1.00 36.44 ? 139 ASN H CG  1 
ATOM   8920  O  OD1 . ASN H  1 166 ? 98.183  58.963  -14.349 1.00 40.31 ? 139 ASN H OD1 1 
ATOM   8921  N  ND2 . ASN H  1 166 ? 96.881  58.441  -12.578 1.00 36.90 ? 139 ASN H ND2 1 
ATOM   8922  N  N   . ALA H  1 167 ? 95.136  63.412  -15.071 1.00 34.16 ? 140 ALA H N   1 
ATOM   8923  C  CA  . ALA H  1 167 ? 94.303  64.188  -15.998 1.00 32.82 ? 140 ALA H CA  1 
ATOM   8924  C  C   . ALA H  1 167 ? 95.080  64.719  -17.227 1.00 34.79 ? 140 ALA H C   1 
ATOM   8925  O  O   . ALA H  1 167 ? 94.504  65.299  -18.137 1.00 33.24 ? 140 ALA H O   1 
ATOM   8926  C  CB  . ALA H  1 167 ? 93.581  65.295  -15.224 1.00 34.71 ? 140 ALA H CB  1 
ATOM   8927  N  N   . GLY H  1 168 ? 96.402  64.492  -17.297 1.00 34.76 ? 141 GLY H N   1 
ATOM   8928  C  CA  . GLY H  1 168 ? 97.142  64.834  -18.527 1.00 32.96 ? 141 GLY H CA  1 
ATOM   8929  C  C   . GLY H  1 168 ? 97.427  66.325  -18.724 1.00 30.83 ? 141 GLY H C   1 
ATOM   8930  O  O   . GLY H  1 168 ? 97.476  67.082  -17.754 1.00 34.08 ? 141 GLY H O   1 
ATOM   8931  N  N   A SER H  1 169 ? 97.553  66.733  -19.985 0.50 32.69 ? 142 SER H N   1 
ATOM   8932  N  N   B SER H  1 169 ? 97.575  66.726  -19.975 0.50 33.35 ? 142 SER H N   1 
ATOM   8933  C  CA  A SER H  1 169 ? 98.027  68.069  -20.372 0.50 35.19 ? 142 SER H CA  1 
ATOM   8934  C  CA  B SER H  1 169 ? 98.032  68.061  -20.325 0.50 36.39 ? 142 SER H CA  1 
ATOM   8935  C  C   A SER H  1 169 ? 96.991  69.184  -20.177 0.50 35.55 ? 142 SER H C   1 
ATOM   8936  C  C   B SER H  1 169 ? 97.063  69.158  -19.863 0.50 36.68 ? 142 SER H C   1 
ATOM   8937  O  O   A SER H  1 169 ? 95.778  68.943  -20.174 0.50 30.93 ? 142 SER H O   1 
ATOM   8938  O  O   B SER H  1 169 ? 95.964  68.879  -19.351 0.50 31.89 ? 142 SER H O   1 
ATOM   8939  C  CB  A SER H  1 169 ? 98.512  68.082  -21.821 0.50 36.53 ? 142 SER H CB  1 
ATOM   8940  C  CB  B SER H  1 169 ? 98.273  68.147  -21.831 0.50 38.07 ? 142 SER H CB  1 
ATOM   8941  O  OG  A SER H  1 169 ? 97.443  68.315  -22.725 0.50 37.35 ? 142 SER H OG  1 
ATOM   8942  O  OG  B SER H  1 169 ? 99.176  67.131  -22.243 0.50 42.06 ? 142 SER H OG  1 
ATOM   8943  N  N   . ARG H  1 170 ? 97.503  70.403  -20.026 1.00 35.61 ? 143 ARG H N   1 
ATOM   8944  C  CA  . ARG H  1 170 ? 96.706  71.566  -19.656 1.00 34.01 ? 143 ARG H CA  1 
ATOM   8945  C  C   . ARG H  1 170 ? 96.170  72.186  -20.928 1.00 35.97 ? 143 ARG H C   1 
ATOM   8946  O  O   . ARG H  1 170 ? 96.929  72.696  -21.744 1.00 32.93 ? 143 ARG H O   1 
ATOM   8947  C  CB  . ARG H  1 170 ? 97.614  72.508  -18.869 1.00 35.27 ? 143 ARG H CB  1 
ATOM   8948  C  CG  . ARG H  1 170 ? 98.224  71.802  -17.659 1.00 33.72 ? 143 ARG H CG  1 
ATOM   8949  C  CD  . ARG H  1 170 ? 99.137  72.692  -16.817 1.00 35.37 ? 143 ARG H CD  1 
ATOM   8950  N  NE  . ARG H  1 170 ? 99.668  71.919  -15.700 1.00 33.38 ? 143 ARG H NE  1 
ATOM   8951  C  CZ  . ARG H  1 170 ? 100.232 72.410  -14.607 1.00 34.75 ? 143 ARG H CZ  1 
ATOM   8952  N  NH1 . ARG H  1 170 ? 100.398 73.736  -14.426 1.00 33.42 ? 143 ARG H NH1 1 
ATOM   8953  N  NH2 . ARG H  1 170 ? 100.634 71.553  -13.671 1.00 31.91 ? 143 ARG H NH2 1 
ATOM   8954  N  N   . LEU H  1 171 ? 94.860  72.097  -21.156 1.00 30.62 ? 144 LEU H N   1 
ATOM   8955  C  CA  . LEU H  1 171 ? 94.351  72.547  -22.432 1.00 29.23 ? 144 LEU H CA  1 
ATOM   8956  C  C   . LEU H  1 171 ? 94.105  74.078  -22.449 1.00 28.91 ? 144 LEU H C   1 
ATOM   8957  O  O   . LEU H  1 171 ? 94.251  74.725  -23.483 1.00 27.51 ? 144 LEU H O   1 
ATOM   8958  C  CB  . LEU H  1 171 ? 93.055  71.795  -22.808 1.00 31.05 ? 144 LEU H CB  1 
ATOM   8959  C  CG  . LEU H  1 171 ? 93.040  70.252  -22.932 1.00 33.29 ? 144 LEU H CG  1 
ATOM   8960  C  CD1 . LEU H  1 171 ? 91.602  69.743  -23.127 1.00 31.98 ? 144 LEU H CD1 1 
ATOM   8961  C  CD2 . LEU H  1 171 ? 93.923  69.833  -24.101 1.00 34.13 ? 144 LEU H CD2 1 
ATOM   8962  N  N   . ALA H  1 172 ? 93.660  74.615  -21.316 1.00 28.01 ? 145 ALA H N   1 
ATOM   8963  C  CA  . ALA H  1 172 ? 93.332  76.056  -21.219 1.00 27.38 ? 145 ALA H CA  1 
ATOM   8964  C  C   . ALA H  1 172 ? 93.344  76.458  -19.792 1.00 26.39 ? 145 ALA H C   1 
ATOM   8965  O  O   . ALA H  1 172 ? 93.155  75.621  -18.885 1.00 24.41 ? 145 ALA H O   1 
ATOM   8966  C  CB  . ALA H  1 172 ? 92.000  76.395  -21.876 1.00 30.10 ? 145 ALA H CB  1 
ATOM   8967  N  N   . CYS H  1 173 ? 93.631  77.741  -19.548 1.00 26.11 ? 146 CYS H N   1 
ATOM   8968  C  CA  . CYS H  1 173 ? 93.704  78.206  -18.174 1.00 26.05 ? 146 CYS H CA  1 
ATOM   8969  C  C   . CYS H  1 173 ? 93.535  79.709  -18.142 1.00 24.44 ? 146 CYS H C   1 
ATOM   8970  O  O   . CYS H  1 173 ? 93.551  80.342  -19.181 1.00 25.54 ? 146 CYS H O   1 
ATOM   8971  C  CB  . CYS H  1 173 ? 95.052  77.834  -17.547 1.00 32.11 ? 146 CYS H CB  1 
ATOM   8972  S  SG  . CYS H  1 173 ? 96.436  78.543  -18.495 1.00 36.89 ? 146 CYS H SG  1 
ATOM   8973  N  N   . GLY H  1 174 ? 93.324  80.242  -16.948 1.00 26.64 ? 147 GLY H N   1 
ATOM   8974  C  CA  . GLY H  1 174 ? 93.218  81.687  -16.782 1.00 27.37 ? 147 GLY H CA  1 
ATOM   8975  C  C   . GLY H  1 174 ? 93.399  81.989  -15.343 1.00 25.60 ? 147 GLY H C   1 
ATOM   8976  O  O   . GLY H  1 174 ? 93.196  81.116  -14.479 1.00 26.73 ? 147 GLY H O   1 
ATOM   8977  N  N   . VAL H  1 175 ? 93.757  83.238  -15.053 1.00 25.15 ? 148 VAL H N   1 
ATOM   8978  C  CA  . VAL H  1 175 ? 93.925  83.663  -13.675 1.00 24.80 ? 148 VAL H CA  1 
ATOM   8979  C  C   . VAL H  1 175 ? 92.554  84.035  -13.131 1.00 24.78 ? 148 VAL H C   1 
ATOM   8980  O  O   . VAL H  1 175 ? 91.753  84.606  -13.849 1.00 27.24 ? 148 VAL H O   1 
ATOM   8981  C  CB  . VAL H  1 175 ? 94.889  84.897  -13.587 1.00 23.10 ? 148 VAL H CB  1 
ATOM   8982  C  CG1 . VAL H  1 175 ? 95.038  85.257  -12.131 1.00 25.28 ? 148 VAL H CG1 1 
ATOM   8983  C  CG2 . VAL H  1 175 ? 96.243  84.522  -14.234 1.00 26.45 ? 148 VAL H CG2 1 
ATOM   8984  N  N   . ILE H  1 176 ? 92.278  83.675  -11.884 1.00 23.32 ? 149 ILE H N   1 
ATOM   8985  C  CA  . ILE H  1 176 ? 90.994  83.955  -11.260 1.00 25.79 ? 149 ILE H CA  1 
ATOM   8986  C  C   . ILE H  1 176 ? 90.998  85.393  -10.695 1.00 26.90 ? 149 ILE H C   1 
ATOM   8987  O  O   . ILE H  1 176 ? 91.762  85.708  -9.781  1.00 28.56 ? 149 ILE H O   1 
ATOM   8988  C  CB  . ILE H  1 176 ? 90.678  82.920  -10.166 1.00 22.66 ? 149 ILE H CB  1 
ATOM   8989  C  CG1 . ILE H  1 176 ? 90.629  81.530  -10.828 1.00 23.83 ? 149 ILE H CG1 1 
ATOM   8990  C  CG2 . ILE H  1 176 ? 89.377  83.282  -9.437  1.00 24.93 ? 149 ILE H CG2 1 
ATOM   8991  C  CD1 . ILE H  1 176 ? 90.837  80.365  -9.873  1.00 23.60 ? 149 ILE H CD1 1 
ATOM   8992  N  N   . GLY H  1 177 ? 90.149  86.246  -11.249 1.00 26.47 ? 150 GLY H N   1 
ATOM   8993  C  CA  . GLY H  1 177 ? 90.130  87.668  -10.872 1.00 26.13 ? 150 GLY H CA  1 
ATOM   8994  C  C   . GLY H  1 177 ? 88.861  88.098  -10.171 1.00 30.69 ? 150 GLY H C   1 
ATOM   8995  O  O   . GLY H  1 177 ? 87.780  87.445  -10.324 1.00 26.40 ? 150 GLY H O   1 
ATOM   8996  N  N   . ILE H  1 178 ? 88.979  89.177  -9.383  1.00 27.33 ? 151 ILE H N   1 
ATOM   8997  C  CA  . ILE H  1 178 ? 87.838  89.711  -8.639  1.00 28.97 ? 151 ILE H CA  1 
ATOM   8998  C  C   . ILE H  1 178 ? 86.845  90.302  -9.646  1.00 28.36 ? 151 ILE H C   1 
ATOM   8999  O  O   . ILE H  1 178 ? 87.227  91.053  -10.579 1.00 25.87 ? 151 ILE H O   1 
ATOM   9000  C  CB  . ILE H  1 178 ? 88.272  90.792  -7.618  1.00 31.18 ? 151 ILE H CB  1 
ATOM   9001  C  CG1 . ILE H  1 178 ? 89.213  90.139  -6.620  1.00 35.25 ? 151 ILE H CG1 1 
ATOM   9002  C  CG2 . ILE H  1 178 ? 87.051  91.367  -6.894  1.00 33.11 ? 151 ILE H CG2 1 
ATOM   9003  C  CD1 . ILE H  1 178 ? 90.038  91.121  -5.781  1.00 37.84 ? 151 ILE H CD1 1 
ATOM   9004  N  N   . ALA H  1 179 ? 85.570  89.938  -9.482  1.00 27.22 ? 152 ALA H N   1 
ATOM   9005  C  CA  . ALA H  1 179 ? 84.527  90.402  -10.401 1.00 28.76 ? 152 ALA H CA  1 
ATOM   9006  C  C   . ALA H  1 179 ? 83.598  91.388  -9.657  1.00 30.64 ? 152 ALA H C   1 
ATOM   9007  O  O   . ALA H  1 179 ? 83.582  91.435  -8.425  1.00 31.78 ? 152 ALA H O   1 
ATOM   9008  C  CB  . ALA H  1 179 ? 83.719  89.204  -10.967 1.00 28.19 ? 152 ALA H CB  1 
ATOM   9009  N  N   . GLN H  1 180 ? 82.862  92.197  -10.407 1.00 34.43 ? 153 GLN H N   1 
ATOM   9010  C  CA  . GLN H  1 180 ? 81.914  93.134  -9.791  1.00 44.47 ? 153 GLN H CA  1 
ATOM   9011  C  C   . GLN H  1 180 ? 80.646  92.391  -9.367  1.00 51.17 ? 153 GLN H C   1 
ATOM   9012  O  O   . GLN H  1 180 ? 80.104  91.590  -10.158 1.00 50.05 ? 153 GLN H O   1 
ATOM   9013  C  CB  . GLN H  1 180 ? 81.517  94.221  -10.773 1.00 40.50 ? 153 GLN H CB  1 
ATOM   9014  C  CG  . GLN H  1 180 ? 80.681  95.306  -10.118 1.00 50.63 ? 153 GLN H CG  1 
ATOM   9015  C  CD  . GLN H  1 180 ? 80.379  96.430  -11.085 1.00 50.75 ? 153 GLN H CD  1 
ATOM   9016  O  OE1 . GLN H  1 180 ? 80.026  96.184  -12.242 1.00 53.46 ? 153 GLN H OE1 1 
ATOM   9017  N  NE2 . GLN H  1 180 ? 80.543  97.668  -10.630 1.00 50.77 ? 153 GLN H NE2 1 
ATOM   9018  O  OXT . GLN H  1 180 ? 80.159  92.585  -8.241  1.00 54.22 ? 153 GLN H OXT 1 
ATOM   9019  N  N   . ALA I  1 28  ? 47.136  77.888  -71.323 1.00 58.09 ? 1   ALA I N   1 
ATOM   9020  C  CA  . ALA I  1 28  ? 47.513  76.824  -70.333 1.00 54.15 ? 1   ALA I CA  1 
ATOM   9021  C  C   . ALA I  1 28  ? 46.322  76.124  -69.607 1.00 53.55 ? 1   ALA I C   1 
ATOM   9022  O  O   . ALA I  1 28  ? 45.398  76.786  -69.130 1.00 58.19 ? 1   ALA I O   1 
ATOM   9023  C  CB  . ALA I  1 28  ? 48.489  77.402  -69.313 1.00 52.04 ? 1   ALA I CB  1 
ATOM   9024  N  N   . THR I  1 29  ? 46.346  74.788  -69.540 1.00 44.99 ? 2   THR I N   1 
ATOM   9025  C  CA  . THR I  1 29  ? 45.572  74.028  -68.536 1.00 44.03 ? 2   THR I CA  1 
ATOM   9026  C  C   . THR I  1 29  ? 46.311  74.217  -67.203 1.00 38.24 ? 2   THR I C   1 
ATOM   9027  O  O   . THR I  1 29  ? 47.547  74.314  -67.186 1.00 29.30 ? 2   THR I O   1 
ATOM   9028  C  CB  . THR I  1 29  ? 45.563  72.555  -68.876 1.00 43.82 ? 2   THR I CB  1 
ATOM   9029  O  OG1 . THR I  1 29  ? 45.532  72.468  -70.303 1.00 54.53 ? 2   THR I OG1 1 
ATOM   9030  C  CG2 . THR I  1 29  ? 44.365  71.845  -68.325 1.00 40.83 ? 2   THR I CG2 1 
ATOM   9031  N  N   . LYS I  1 30  ? 45.537  74.295  -66.112 1.00 34.75 ? 3   LYS I N   1 
ATOM   9032  C  CA  . LYS I  1 30  ? 46.064  74.619  -64.780 1.00 32.18 ? 3   LYS I CA  1 
ATOM   9033  C  C   . LYS I  1 30  ? 45.365  73.746  -63.761 1.00 29.27 ? 3   LYS I C   1 
ATOM   9034  O  O   . LYS I  1 30  ? 44.143  73.389  -63.899 1.00 29.00 ? 3   LYS I O   1 
ATOM   9035  C  CB  . LYS I  1 30  ? 45.814  76.090  -64.445 1.00 39.27 ? 3   LYS I CB  1 
ATOM   9036  C  CG  . LYS I  1 30  ? 46.722  77.056  -65.190 1.00 49.18 ? 3   LYS I CG  1 
ATOM   9037  C  CD  . LYS I  1 30  ? 46.361  78.512  -64.933 1.00 52.48 ? 3   LYS I CD  1 
ATOM   9038  C  CE  . LYS I  1 30  ? 46.896  79.386  -66.069 1.00 59.75 ? 3   LYS I CE  1 
ATOM   9039  N  NZ  . LYS I  1 30  ? 47.318  80.731  -65.586 1.00 59.02 ? 3   LYS I NZ  1 
ATOM   9040  N  N   . ALA I  1 31  ? 46.148  73.346  -62.764 1.00 25.05 ? 4   ALA I N   1 
ATOM   9041  C  CA  . ALA I  1 31  ? 45.625  72.551  -61.660 1.00 24.25 ? 4   ALA I CA  1 
ATOM   9042  C  C   . ALA I  1 31  ? 46.241  73.163  -60.392 1.00 24.41 ? 4   ALA I C   1 
ATOM   9043  O  O   . ALA I  1 31  ? 47.193  73.927  -60.473 1.00 25.26 ? 4   ALA I O   1 
ATOM   9044  C  CB  . ALA I  1 31  ? 45.997  71.084  -61.823 1.00 24.73 ? 4   ALA I CB  1 
ATOM   9045  N  N   . VAL I  1 32  ? 45.637  72.880  -59.230 1.00 24.56 ? 5   VAL I N   1 
ATOM   9046  C  CA  . VAL I  1 32  ? 46.163  73.432  -57.983 1.00 24.21 ? 5   VAL I CA  1 
ATOM   9047  C  C   . VAL I  1 32  ? 45.986  72.364  -56.887 1.00 22.45 ? 5   VAL I C   1 
ATOM   9048  O  O   . VAL I  1 32  ? 45.072  71.535  -56.964 1.00 25.21 ? 5   VAL I O   1 
ATOM   9049  C  CB  . VAL I  1 32  ? 45.491  74.790  -57.633 1.00 25.29 ? 5   VAL I CB  1 
ATOM   9050  C  CG1 . VAL I  1 32  ? 43.973  74.617  -57.351 1.00 25.42 ? 5   VAL I CG1 1 
ATOM   9051  C  CG2 . VAL I  1 32  ? 46.227  75.469  -56.484 1.00 28.32 ? 5   VAL I CG2 1 
ATOM   9052  N  N   . CYS I  1 33  ? 46.826  72.406  -55.846 1.00 22.75 ? 6   CYS I N   1 
ATOM   9053  C  CA  . CYS I  1 33  ? 46.707  71.434  -54.782 1.00 22.36 ? 6   CYS I CA  1 
ATOM   9054  C  C   . CYS I  1 33  ? 46.958  72.155  -53.469 1.00 21.50 ? 6   CYS I C   1 
ATOM   9055  O  O   . CYS I  1 33  ? 47.980  72.799  -53.326 1.00 21.14 ? 6   CYS I O   1 
ATOM   9056  C  CB  . CYS I  1 33  ? 47.805  70.369  -54.930 1.00 23.43 ? 6   CYS I CB  1 
ATOM   9057  S  SG  . CYS I  1 33  ? 47.596  69.024  -53.756 1.00 26.96 ? 6   CYS I SG  1 
ATOM   9058  N  N   . VAL I  1 34  ? 46.081  71.949  -52.489 1.00 20.04 ? 7   VAL I N   1 
ATOM   9059  C  CA  . VAL I  1 34  ? 46.343  72.535  -51.149 1.00 20.38 ? 7   VAL I CA  1 
ATOM   9060  C  C   . VAL I  1 34  ? 46.789  71.387  -50.252 1.00 19.98 ? 7   VAL I C   1 
ATOM   9061  O  O   . VAL I  1 34  ? 46.057  70.432  -50.081 1.00 21.54 ? 7   VAL I O   1 
ATOM   9062  C  CB  . VAL I  1 34  ? 45.081  73.236  -50.581 1.00 21.65 ? 7   VAL I CB  1 
ATOM   9063  C  CG1 . VAL I  1 34  ? 45.367  73.782  -49.189 1.00 21.12 ? 7   VAL I CG1 1 
ATOM   9064  C  CG2 . VAL I  1 34  ? 44.647  74.364  -51.499 1.00 24.32 ? 7   VAL I CG2 1 
ATOM   9065  N  N   . LEU I  1 35  ? 48.023  71.449  -49.762 1.00 21.58 ? 8   LEU I N   1 
ATOM   9066  C  CA  . LEU I  1 35  ? 48.560  70.377  -48.930 1.00 23.04 ? 8   LEU I CA  1 
ATOM   9067  C  C   . LEU I  1 35  ? 48.287  70.691  -47.458 1.00 21.86 ? 8   LEU I C   1 
ATOM   9068  O  O   . LEU I  1 35  ? 48.548  71.818  -47.003 1.00 20.11 ? 8   LEU I O   1 
ATOM   9069  C  CB  . LEU I  1 35  ? 50.053  70.289  -49.110 1.00 23.59 ? 8   LEU I CB  1 
ATOM   9070  C  CG  . LEU I  1 35  ? 50.518  70.017  -50.553 1.00 25.84 ? 8   LEU I CG  1 
ATOM   9071  C  CD1 . LEU I  1 35  ? 52.020  70.275  -50.630 1.00 30.09 ? 8   LEU I CD1 1 
ATOM   9072  C  CD2 . LEU I  1 35  ? 50.242  68.551  -50.838 1.00 27.89 ? 8   LEU I CD2 1 
ATOM   9073  N  N   . LYS I  1 36  ? 47.729  69.717  -46.768 1.00 21.16 ? 9   LYS I N   1 
ATOM   9074  C  CA  . LYS I  1 36  ? 47.459  69.811  -45.333 1.00 26.65 ? 9   LYS I CA  1 
ATOM   9075  C  C   . LYS I  1 36  ? 47.777  68.431  -44.739 1.00 25.53 ? 9   LYS I C   1 
ATOM   9076  O  O   . LYS I  1 36  ? 47.622  67.408  -45.437 1.00 22.96 ? 9   LYS I O   1 
ATOM   9077  C  CB  . LYS I  1 36  ? 45.964  70.065  -45.138 1.00 28.61 ? 9   LYS I CB  1 
ATOM   9078  C  CG  . LYS I  1 36  ? 45.539  71.457  -45.627 1.00 37.72 ? 9   LYS I CG  1 
ATOM   9079  C  CD  . LYS I  1 36  ? 45.859  72.535  -44.594 1.00 45.49 ? 9   LYS I CD  1 
ATOM   9080  C  CE  . LYS I  1 36  ? 45.746  73.940  -45.175 1.00 51.54 ? 9   LYS I CE  1 
ATOM   9081  N  NZ  . LYS I  1 36  ? 44.331  74.222  -45.546 1.00 48.36 ? 9   LYS I NZ  1 
ATOM   9082  N  N   . GLY I  1 37  ? 48.118  68.392  -43.459 1.00 26.52 ? 10  GLY I N   1 
ATOM   9083  C  CA  . GLY I  1 37  ? 48.252  67.096  -42.756 1.00 28.19 ? 10  GLY I CA  1 
ATOM   9084  C  C   . GLY I  1 37  ? 47.958  67.245  -41.273 1.00 37.03 ? 10  GLY I C   1 
ATOM   9085  O  O   . GLY I  1 37  ? 47.252  68.165  -40.888 1.00 31.97 ? 10  GLY I O   1 
ATOM   9086  N  N   . ASP I  1 38  ? 48.536  66.374  -40.445 1.00 37.21 ? 11  ASP I N   1 
ATOM   9087  C  CA  . ASP I  1 38  ? 48.256  66.361  -38.997 1.00 42.98 ? 11  ASP I CA  1 
ATOM   9088  C  C   . ASP I  1 38  ? 49.197  67.244  -38.252 1.00 41.82 ? 11  ASP I C   1 
ATOM   9089  O  O   . ASP I  1 38  ? 48.969  67.506  -37.091 1.00 44.48 ? 11  ASP I O   1 
ATOM   9090  C  CB  . ASP I  1 38  ? 48.399  64.961  -38.423 1.00 47.21 ? 11  ASP I CB  1 
ATOM   9091  C  CG  . ASP I  1 38  ? 47.368  64.041  -38.942 1.00 52.98 ? 11  ASP I CG  1 
ATOM   9092  O  OD1 . ASP I  1 38  ? 46.268  64.555  -39.252 1.00 53.14 ? 11  ASP I OD1 1 
ATOM   9093  O  OD2 . ASP I  1 38  ? 47.650  62.820  -39.066 1.00 57.30 ? 11  ASP I OD2 1 
ATOM   9094  N  N   . GLY I  1 39  ? 50.266  67.678  -38.902 1.00 36.65 ? 12  GLY I N   1 
ATOM   9095  C  CA  . GLY I  1 39  ? 51.253  68.533  -38.258 1.00 34.33 ? 12  GLY I CA  1 
ATOM   9096  C  C   . GLY I  1 39  ? 51.198  69.939  -38.810 1.00 31.15 ? 12  GLY I C   1 
ATOM   9097  O  O   . GLY I  1 39  ? 50.206  70.358  -39.333 1.00 34.38 ? 12  GLY I O   1 
ATOM   9098  N  N   . PRO I  1 40  ? 52.307  70.650  -38.740 1.00 33.85 ? 13  PRO I N   1 
ATOM   9099  C  CA  . PRO I  1 40  ? 52.367  72.029  -39.203 1.00 35.12 ? 13  PRO I CA  1 
ATOM   9100  C  C   . PRO I  1 40  ? 52.639  72.169  -40.715 1.00 33.88 ? 13  PRO I C   1 
ATOM   9101  O  O   . PRO I  1 40  ? 52.697  73.301  -41.230 1.00 29.80 ? 13  PRO I O   1 
ATOM   9102  C  CB  . PRO I  1 40  ? 53.562  72.584  -38.432 1.00 33.97 ? 13  PRO I CB  1 
ATOM   9103  C  CG  . PRO I  1 40  ? 54.479  71.402  -38.288 1.00 35.25 ? 13  PRO I CG  1 
ATOM   9104  C  CD  . PRO I  1 40  ? 53.594  70.176  -38.190 1.00 33.09 ? 13  PRO I CD  1 
ATOM   9105  N  N   . VAL I  1 41  ? 52.824  71.048  -41.423 1.00 26.10 ? 14  VAL I N   1 
ATOM   9106  C  CA  . VAL I  1 41  ? 53.237  71.154  -42.844 1.00 24.00 ? 14  VAL I CA  1 
ATOM   9107  C  C   . VAL I  1 41  ? 52.031  71.563  -43.694 1.00 21.56 ? 14  VAL I C   1 
ATOM   9108  O  O   . VAL I  1 41  ? 50.968  70.926  -43.644 1.00 23.94 ? 14  VAL I O   1 
ATOM   9109  C  CB  . VAL I  1 41  ? 53.838  69.831  -43.391 1.00 23.74 ? 14  VAL I CB  1 
ATOM   9110  C  CG1 . VAL I  1 41  ? 54.176  69.993  -44.874 1.00 23.21 ? 14  VAL I CG1 1 
ATOM   9111  C  CG2 . VAL I  1 41  ? 55.127  69.502  -42.627 1.00 23.18 ? 14  VAL I CG2 1 
ATOM   9112  N  N   . GLN I  1 42  ? 52.195  72.616  -44.477 1.00 22.68 ? 15  GLN I N   1 
ATOM   9113  C  CA  . GLN I  1 42  ? 51.085  73.062  -45.343 1.00 23.62 ? 15  GLN I CA  1 
ATOM   9114  C  C   . GLN I  1 42  ? 51.615  73.881  -46.488 1.00 21.54 ? 15  GLN I C   1 
ATOM   9115  O  O   . GLN I  1 42  ? 52.676  74.481  -46.389 1.00 21.65 ? 15  GLN I O   1 
ATOM   9116  C  CB  . GLN I  1 42  ? 50.039  73.880  -44.551 1.00 29.97 ? 15  GLN I CB  1 
ATOM   9117  C  CG  . GLN I  1 42  ? 50.597  75.195  -44.030 1.00 33.10 ? 15  GLN I CG  1 
ATOM   9118  C  CD  . GLN I  1 42  ? 49.599  75.953  -43.152 1.00 44.03 ? 15  GLN I CD  1 
ATOM   9119  O  OE1 . GLN I  1 42  ? 49.991  76.790  -42.366 1.00 50.60 ? 15  GLN I OE1 1 
ATOM   9120  N  NE2 . GLN I  1 42  ? 48.327  75.648  -43.276 1.00 44.31 ? 15  GLN I NE2 1 
ATOM   9121  N  N   . GLY I  1 43  ? 50.863  73.904  -47.597 1.00 24.49 ? 16  GLY I N   1 
ATOM   9122  C  CA  . GLY I  1 43  ? 51.259  74.756  -48.687 1.00 23.81 ? 16  GLY I CA  1 
ATOM   9123  C  C   . GLY I  1 43  ? 50.308  74.681  -49.836 1.00 22.21 ? 16  GLY I C   1 
ATOM   9124  O  O   . GLY I  1 43  ? 49.270  74.047  -49.750 1.00 22.71 ? 16  GLY I O   1 
ATOM   9125  N  N   . ILE I  1 44  ? 50.670  75.379  -50.901 1.00 24.08 ? 17  ILE I N   1 
ATOM   9126  C  CA  . ILE I  1 44  ? 49.839  75.440  -52.099 1.00 22.51 ? 17  ILE I CA  1 
ATOM   9127  C  C   . ILE I  1 44  ? 50.777  75.197  -53.237 1.00 20.79 ? 17  ILE I C   1 
ATOM   9128  O  O   . ILE I  1 44  ? 51.796  75.853  -53.335 1.00 21.89 ? 17  ILE I O   1 
ATOM   9129  C  CB  . ILE I  1 44  ? 49.174  76.821  -52.283 1.00 26.22 ? 17  ILE I CB  1 
ATOM   9130  C  CG1 . ILE I  1 44  ? 48.149  77.084  -51.135 1.00 28.45 ? 17  ILE I CG1 1 
ATOM   9131  C  CG2 . ILE I  1 44  ? 48.484  76.904  -53.662 1.00 25.31 ? 17  ILE I CG2 1 
ATOM   9132  C  CD1 . ILE I  1 44  ? 47.557  78.492  -51.099 1.00 32.47 ? 17  ILE I CD1 1 
ATOM   9133  N  N   . ILE I  1 45  ? 50.413  74.250  -54.101 1.00 20.40 ? 18  ILE I N   1 
ATOM   9134  C  CA  . ILE I  1 45  ? 51.271  73.940  -55.220 1.00 20.16 ? 18  ILE I CA  1 
ATOM   9135  C  C   . ILE I  1 45  ? 50.411  74.133  -56.471 1.00 21.93 ? 18  ILE I C   1 
ATOM   9136  O  O   . ILE I  1 45  ? 49.274  73.657  -56.534 1.00 21.51 ? 18  ILE I O   1 
ATOM   9137  C  CB  . ILE I  1 45  ? 51.745  72.470  -55.168 1.00 20.78 ? 18  ILE I CB  1 
ATOM   9138  C  CG1 . ILE I  1 45  ? 52.659  72.240  -53.956 1.00 18.64 ? 18  ILE I CG1 1 
ATOM   9139  C  CG2 . ILE I  1 45  ? 52.500  72.101  -56.436 1.00 20.44 ? 18  ILE I CG2 1 
ATOM   9140  C  CD1 . ILE I  1 45  ? 53.927  73.075  -54.033 1.00 19.63 ? 18  ILE I CD1 1 
ATOM   9141  N  N   . ASN I  1 46  ? 51.008  74.803  -57.460 1.00 23.42 ? 19  ASN I N   1 
ATOM   9142  C  CA  . ASN I  1 46  ? 50.333  75.134  -58.707 1.00 24.80 ? 19  ASN I CA  1 
ATOM   9143  C  C   . ASN I  1 46  ? 50.904  74.274  -59.834 1.00 25.45 ? 19  ASN I C   1 
ATOM   9144  O  O   . ASN I  1 46  ? 52.089  73.911  -59.817 1.00 24.04 ? 19  ASN I O   1 
ATOM   9145  C  CB  . ASN I  1 46  ? 50.608  76.621  -59.027 1.00 25.98 ? 19  ASN I CB  1 
ATOM   9146  C  CG  . ASN I  1 46  ? 50.121  77.536  -57.931 1.00 26.54 ? 19  ASN I CG  1 
ATOM   9147  O  OD1 . ASN I  1 46  ? 50.904  78.092  -57.125 1.00 30.96 ? 19  ASN I OD1 1 
ATOM   9148  N  ND2 . ASN I  1 46  ? 48.833  77.648  -57.841 1.00 24.11 ? 19  ASN I ND2 1 
ATOM   9149  N  N   . PHE I  1 47  ? 50.064  73.938  -60.816 1.00 24.93 ? 20  PHE I N   1 
ATOM   9150  C  CA  . PHE I  1 47  ? 50.559  73.190  -61.946 1.00 26.60 ? 20  PHE I CA  1 
ATOM   9151  C  C   . PHE I  1 47  ? 50.134  73.939  -63.203 1.00 27.28 ? 20  PHE I C   1 
ATOM   9152  O  O   . PHE I  1 47  ? 48.985  74.398  -63.300 1.00 26.31 ? 20  PHE I O   1 
ATOM   9153  C  CB  . PHE I  1 47  ? 49.939  71.797  -62.004 1.00 25.45 ? 20  PHE I CB  1 
ATOM   9154  C  CG  . PHE I  1 47  ? 50.232  70.916  -60.791 1.00 27.16 ? 20  PHE I CG  1 
ATOM   9155  C  CD1 . PHE I  1 47  ? 49.433  70.993  -59.624 1.00 25.04 ? 20  PHE I CD1 1 
ATOM   9156  C  CD2 . PHE I  1 47  ? 51.261  69.979  -60.833 1.00 23.13 ? 20  PHE I CD2 1 
ATOM   9157  C  CE1 . PHE I  1 47  ? 49.696  70.153  -58.533 1.00 24.75 ? 20  PHE I CE1 1 
ATOM   9158  C  CE2 . PHE I  1 47  ? 51.529  69.146  -59.732 1.00 26.02 ? 20  PHE I CE2 1 
ATOM   9159  C  CZ  . PHE I  1 47  ? 50.717  69.238  -58.581 1.00 23.01 ? 20  PHE I CZ  1 
ATOM   9160  N  N   . GLU I  1 48  ? 51.034  74.011  -64.170 1.00 27.07 ? 21  GLU I N   1 
ATOM   9161  C  CA  . GLU I  1 48  ? 50.651  74.644  -65.428 1.00 32.26 ? 21  GLU I CA  1 
ATOM   9162  C  C   . GLU I  1 48  ? 51.271  73.868  -66.595 1.00 32.28 ? 21  GLU I C   1 
ATOM   9163  O  O   . GLU I  1 48  ? 52.478  73.576  -66.582 1.00 30.42 ? 21  GLU I O   1 
ATOM   9164  C  CB  . GLU I  1 48  ? 51.091  76.101  -65.393 1.00 36.78 ? 21  GLU I CB  1 
ATOM   9165  C  CG  . GLU I  1 48  ? 50.807  76.899  -66.662 1.00 48.11 ? 21  GLU I CG  1 
ATOM   9166  C  CD  . GLU I  1 48  ? 51.639  78.173  -66.714 1.00 60.55 ? 21  GLU I CD  1 
ATOM   9167  O  OE1 . GLU I  1 48  ? 52.685  78.211  -67.430 1.00 65.12 ? 21  GLU I OE1 1 
ATOM   9168  O  OE2 . GLU I  1 48  ? 51.255  79.131  -66.009 1.00 62.49 ? 21  GLU I OE2 1 
ATOM   9169  N  N   . GLN I  1 49  ? 50.429  73.515  -67.570 1.00 36.77 ? 22  GLN I N   1 
ATOM   9170  C  CA  . GLN I  1 49  ? 50.865  72.844  -68.789 1.00 35.25 ? 22  GLN I CA  1 
ATOM   9171  C  C   . GLN I  1 49  ? 50.408  73.620  -70.048 1.00 38.20 ? 22  GLN I C   1 
ATOM   9172  O  O   . GLN I  1 49  ? 49.217  73.605  -70.386 1.00 38.41 ? 22  GLN I O   1 
ATOM   9173  C  CB  . GLN I  1 49  ? 50.286  71.442  -68.795 1.00 31.97 ? 22  GLN I CB  1 
ATOM   9174  C  CG  . GLN I  1 49  ? 50.900  70.557  -69.866 1.00 31.74 ? 22  GLN I CG  1 
ATOM   9175  C  CD  . GLN I  1 49  ? 50.391  69.138  -69.806 1.00 29.22 ? 22  GLN I CD  1 
ATOM   9176  O  OE1 . GLN I  1 49  ? 49.277  68.874  -69.361 1.00 35.00 ? 22  GLN I OE1 1 
ATOM   9177  N  NE2 . GLN I  1 49  ? 51.215  68.209  -70.229 1.00 35.77 ? 22  GLN I NE2 1 
ATOM   9178  N  N   . LYS I  1 50  ? 51.336  74.295  -70.721 1.00 40.01 ? 23  LYS I N   1 
ATOM   9179  C  CA  . LYS I  1 50  ? 51.006  75.148  -71.884 1.00 43.82 ? 23  LYS I CA  1 
ATOM   9180  C  C   . LYS I  1 50  ? 50.582  74.318  -73.093 1.00 45.60 ? 23  LYS I C   1 
ATOM   9181  O  O   . LYS I  1 50  ? 49.664  74.698  -73.813 1.00 51.56 ? 23  LYS I O   1 
ATOM   9182  C  CB  . LYS I  1 50  ? 52.179  76.061  -72.269 1.00 46.90 ? 23  LYS I CB  1 
ATOM   9183  C  CG  . LYS I  1 50  ? 52.584  77.091  -71.222 1.00 50.47 ? 23  LYS I CG  1 
ATOM   9184  C  CD  . LYS I  1 50  ? 53.637  78.039  -71.796 1.00 58.11 ? 23  LYS I CD  1 
ATOM   9185  C  CE  . LYS I  1 50  ? 54.272  78.951  -70.749 1.00 63.87 ? 23  LYS I CE  1 
ATOM   9186  N  NZ  . LYS I  1 50  ? 53.318  79.944  -70.157 1.00 62.57 ? 23  LYS I NZ  1 
ATOM   9187  N  N   . GLU I  1 51  ? 51.240  73.189  -73.317 1.00 46.35 ? 24  GLU I N   1 
ATOM   9188  C  CA  . GLU I  1 51  ? 50.855  72.317  -74.429 1.00 47.82 ? 24  GLU I CA  1 
ATOM   9189  C  C   . GLU I  1 51  ? 50.421  70.936  -74.026 1.00 47.25 ? 24  GLU I C   1 
ATOM   9190  O  O   . GLU I  1 51  ? 50.948  70.314  -73.079 1.00 44.12 ? 24  GLU I O   1 
ATOM   9191  C  CB  . GLU I  1 51  ? 51.872  72.278  -75.598 1.00 50.13 ? 24  GLU I CB  1 
ATOM   9192  C  CG  . GLU I  1 51  ? 53.356  72.272  -75.283 1.00 58.58 ? 24  GLU I CG  1 
ATOM   9193  C  CD  . GLU I  1 51  ? 54.190  72.936  -76.400 1.00 64.99 ? 24  GLU I CD  1 
ATOM   9194  O  OE1 . GLU I  1 51  ? 54.990  73.847  -76.090 1.00 63.22 ? 24  GLU I OE1 1 
ATOM   9195  O  OE2 . GLU I  1 51  ? 54.054  72.575  -77.597 1.00 63.78 ? 24  GLU I OE2 1 
ATOM   9196  N  N   . SER I  1 52  ? 49.444  70.453  -74.777 1.00 50.34 ? 25  SER I N   1 
ATOM   9197  C  CA  . SER I  1 52  ? 48.782  69.205  -74.473 1.00 51.50 ? 25  SER I CA  1 
ATOM   9198  C  C   . SER I  1 52  ? 49.811  68.117  -74.209 1.00 52.58 ? 25  SER I C   1 
ATOM   9199  O  O   . SER I  1 52  ? 49.661  67.295  -73.295 1.00 55.97 ? 25  SER I O   1 
ATOM   9200  C  CB  . SER I  1 52  ? 47.830  68.819  -75.605 1.00 55.25 ? 25  SER I CB  1 
ATOM   9201  O  OG  . SER I  1 52  ? 46.658  68.234  -75.059 1.00 59.45 ? 25  SER I OG  1 
ATOM   9202  N  N   . ASN I  1 53  ? 50.892  68.112  -74.960 1.00 54.41 ? 26  ASN I N   1 
ATOM   9203  C  CA  . ASN I  1 53  ? 51.829  67.045  -74.710 1.00 61.48 ? 26  ASN I CA  1 
ATOM   9204  C  C   . ASN I  1 53  ? 53.038  67.343  -73.821 1.00 57.32 ? 26  ASN I C   1 
ATOM   9205  O  O   . ASN I  1 53  ? 53.762  66.423  -73.443 1.00 57.37 ? 26  ASN I O   1 
ATOM   9206  C  CB  . ASN I  1 53  ? 52.266  66.384  -76.006 1.00 69.38 ? 26  ASN I CB  1 
ATOM   9207  C  CG  . ASN I  1 53  ? 52.365  64.894  -75.843 1.00 83.80 ? 26  ASN I CG  1 
ATOM   9208  O  OD1 . ASN I  1 53  ? 51.538  64.293  -75.142 1.00 83.76 ? 26  ASN I OD1 1 
ATOM   9209  N  ND2 . ASN I  1 53  ? 53.389  64.285  -76.439 1.00 84.76 ? 26  ASN I ND2 1 
ATOM   9210  N  N   . GLY I  1 54  ? 53.220  68.611  -73.462 1.00 45.77 ? 27  GLY I N   1 
ATOM   9211  C  CA  . GLY I  1 54  ? 54.515  69.090  -73.031 1.00 43.23 ? 27  GLY I CA  1 
ATOM   9212  C  C   . GLY I  1 54  ? 54.750  69.060  -71.540 1.00 39.76 ? 27  GLY I C   1 
ATOM   9213  O  O   . GLY I  1 54  ? 53.978  68.439  -70.807 1.00 40.19 ? 27  GLY I O   1 
ATOM   9214  N  N   . PRO I  1 55  ? 55.826  69.728  -71.098 1.00 38.82 ? 28  PRO I N   1 
ATOM   9215  C  CA  . PRO I  1 55  ? 56.262  69.798  -69.694 1.00 35.45 ? 28  PRO I CA  1 
ATOM   9216  C  C   . PRO I  1 55  ? 55.161  70.437  -68.791 1.00 34.31 ? 28  PRO I C   1 
ATOM   9217  O  O   . PRO I  1 55  ? 54.409  71.279  -69.250 1.00 32.35 ? 28  PRO I O   1 
ATOM   9218  C  CB  . PRO I  1 55  ? 57.496  70.695  -69.755 1.00 36.71 ? 28  PRO I CB  1 
ATOM   9219  C  CG  . PRO I  1 55  ? 57.864  70.803  -71.197 1.00 41.25 ? 28  PRO I CG  1 
ATOM   9220  C  CD  . PRO I  1 55  ? 56.598  70.636  -71.962 1.00 39.49 ? 28  PRO I CD  1 
ATOM   9221  N  N   . VAL I  1 56  ? 55.045  69.974  -67.543 1.00 35.18 ? 29  VAL I N   1 
ATOM   9222  C  CA  . VAL I  1 56  ? 54.205  70.626  -66.521 1.00 27.88 ? 29  VAL I CA  1 
ATOM   9223  C  C   . VAL I  1 56  ? 55.125  71.444  -65.604 1.00 27.20 ? 29  VAL I C   1 
ATOM   9224  O  O   . VAL I  1 56  ? 56.106  70.920  -65.109 1.00 27.81 ? 29  VAL I O   1 
ATOM   9225  C  CB  . VAL I  1 56  ? 53.401  69.589  -65.728 1.00 27.93 ? 29  VAL I CB  1 
ATOM   9226  C  CG1 . VAL I  1 56  ? 52.435  70.263  -64.760 1.00 24.23 ? 29  VAL I CG1 1 
ATOM   9227  C  CG2 . VAL I  1 56  ? 52.592  68.702  -66.657 1.00 26.78 ? 29  VAL I CG2 1 
ATOM   9228  N  N   . LYS I  1 57  ? 54.833  72.723  -65.406 1.00 25.91 ? 30  LYS I N   1 
ATOM   9229  C  CA  . LYS I  1 57  ? 55.564  73.526  -64.415 1.00 28.50 ? 30  LYS I CA  1 
ATOM   9230  C  C   . LYS I  1 57  ? 54.847  73.333  -63.097 1.00 25.96 ? 30  LYS I C   1 
ATOM   9231  O  O   . LYS I  1 57  ? 53.628  73.440  -63.041 1.00 27.09 ? 30  LYS I O   1 
ATOM   9232  C  CB  . LYS I  1 57  ? 55.531  75.014  -64.744 1.00 34.00 ? 30  LYS I CB  1 
ATOM   9233  C  CG  . LYS I  1 57  ? 56.116  75.338  -66.113 1.00 43.78 ? 30  LYS I CG  1 
ATOM   9234  C  CD  . LYS I  1 57  ? 56.392  76.833  -66.235 1.00 51.95 ? 30  LYS I CD  1 
ATOM   9235  C  CE  . LYS I  1 57  ? 56.491  77.266  -67.698 1.00 56.45 ? 30  LYS I CE  1 
ATOM   9236  N  NZ  . LYS I  1 57  ? 57.847  76.988  -68.259 1.00 56.63 ? 30  LYS I NZ  1 
ATOM   9237  N  N   . VAL I  1 58  ? 55.613  73.091  -62.047 1.00 27.73 ? 31  VAL I N   1 
ATOM   9238  C  CA  . VAL I  1 58  ? 55.056  72.803  -60.719 1.00 25.33 ? 31  VAL I CA  1 
ATOM   9239  C  C   . VAL I  1 58  ? 55.770  73.812  -59.825 1.00 28.53 ? 31  VAL I C   1 
ATOM   9240  O  O   . VAL I  1 58  ? 57.020  73.826  -59.779 1.00 27.98 ? 31  VAL I O   1 
ATOM   9241  C  CB  . VAL I  1 58  ? 55.366  71.351  -60.281 1.00 27.15 ? 31  VAL I CB  1 
ATOM   9242  C  CG1 . VAL I  1 58  ? 54.760  71.067  -58.895 1.00 24.53 ? 31  VAL I CG1 1 
ATOM   9243  C  CG2 . VAL I  1 58  ? 54.846  70.322  -61.315 1.00 23.25 ? 31  VAL I CG2 1 
ATOM   9244  N  N   . TRP I  1 59  ? 55.007  74.687  -59.151 1.00 26.39 ? 32  TRP I N   1 
ATOM   9245  C  CA  . TRP I  1 59  ? 55.635  75.700  -58.312 1.00 26.82 ? 32  TRP I CA  1 
ATOM   9246  C  C   . TRP I  1 59  ? 54.722  76.073  -57.148 1.00 24.34 ? 32  TRP I C   1 
ATOM   9247  O  O   . TRP I  1 59  ? 53.496  75.954  -57.227 1.00 25.09 ? 32  TRP I O   1 
ATOM   9248  C  CB  . TRP I  1 59  ? 56.032  76.954  -59.134 1.00 28.75 ? 32  TRP I CB  1 
ATOM   9249  C  CG  . TRP I  1 59  ? 54.861  77.891  -59.424 1.00 34.21 ? 32  TRP I CG  1 
ATOM   9250  C  CD1 . TRP I  1 59  ? 54.467  79.010  -58.697 1.00 33.87 ? 32  TRP I CD1 1 
ATOM   9251  C  CD2 . TRP I  1 59  ? 53.931  77.766  -60.486 1.00 37.39 ? 32  TRP I CD2 1 
ATOM   9252  N  NE1 . TRP I  1 59  ? 53.359  79.577  -59.277 1.00 35.26 ? 32  TRP I NE1 1 
ATOM   9253  C  CE2 . TRP I  1 59  ? 53.015  78.844  -60.378 1.00 38.50 ? 32  TRP I CE2 1 
ATOM   9254  C  CE3 . TRP I  1 59  ? 53.783  76.851  -61.538 1.00 44.79 ? 32  TRP I CE3 1 
ATOM   9255  C  CZ2 . TRP I  1 59  ? 51.974  79.034  -61.283 1.00 44.13 ? 32  TRP I CZ2 1 
ATOM   9256  C  CZ3 . TRP I  1 59  ? 52.735  77.040  -62.446 1.00 50.76 ? 32  TRP I CZ3 1 
ATOM   9257  C  CH2 . TRP I  1 59  ? 51.843  78.131  -62.305 1.00 48.78 ? 32  TRP I CH2 1 
ATOM   9258  N  N   . GLY I  1 60  ? 55.311  76.513  -56.059 1.00 24.92 ? 33  GLY I N   1 
ATOM   9259  C  CA  . GLY I  1 60  ? 54.476  76.992  -54.961 1.00 25.64 ? 33  GLY I CA  1 
ATOM   9260  C  C   . GLY I  1 60  ? 55.319  76.993  -53.731 1.00 26.09 ? 33  GLY I C   1 
ATOM   9261  O  O   . GLY I  1 60  ? 56.539  76.959  -53.820 1.00 28.58 ? 33  GLY I O   1 
ATOM   9262  N  N   . SER I  1 61  ? 54.671  77.048  -52.572 1.00 25.64 ? 34  SER I N   1 
ATOM   9263  C  CA  . SER I  1 61  ? 55.420  77.132  -51.339 1.00 25.95 ? 34  SER I CA  1 
ATOM   9264  C  C   . SER I  1 61  ? 54.829  76.169  -50.340 1.00 26.07 ? 34  SER I C   1 
ATOM   9265  O  O   . SER I  1 61  ? 53.616  76.095  -50.201 1.00 25.42 ? 34  SER I O   1 
ATOM   9266  C  CB  . SER I  1 61  ? 55.364  78.563  -50.813 1.00 32.76 ? 34  SER I CB  1 
ATOM   9267  O  OG  . SER I  1 61  ? 56.177  78.671  -49.675 1.00 41.72 ? 34  SER I OG  1 
ATOM   9268  N  N   . ILE I  1 62  ? 55.696  75.431  -49.646 1.00 22.44 ? 35  ILE I N   1 
ATOM   9269  C  CA  . ILE I  1 62  ? 55.281  74.537  -48.555 1.00 23.56 ? 35  ILE I CA  1 
ATOM   9270  C  C   . ILE I  1 62  ? 56.036  75.001  -47.290 1.00 24.35 ? 35  ILE I C   1 
ATOM   9271  O  O   . ILE I  1 62  ? 57.235  75.192  -47.332 1.00 25.87 ? 35  ILE I O   1 
ATOM   9272  C  CB  . ILE I  1 62  ? 55.695  73.061  -48.855 1.00 24.02 ? 35  ILE I CB  1 
ATOM   9273  C  CG1 . ILE I  1 62  ? 55.182  72.617  -50.246 1.00 22.77 ? 35  ILE I CG1 1 
ATOM   9274  C  CG2 . ILE I  1 62  ? 55.141  72.127  -47.785 1.00 20.93 ? 35  ILE I CG2 1 
ATOM   9275  C  CD1 . ILE I  1 62  ? 55.477  71.156  -50.610 1.00 22.32 ? 35  ILE I CD1 1 
ATOM   9276  N  N   . LYS I  1 63  ? 55.337  75.149  -46.178 1.00 23.94 ? 36  LYS I N   1 
ATOM   9277  C  CA  . LYS I  1 63  ? 56.010  75.624  -44.964 1.00 26.85 ? 36  LYS I CA  1 
ATOM   9278  C  C   . LYS I  1 63  ? 55.880  74.598  -43.851 1.00 22.02 ? 36  LYS I C   1 
ATOM   9279  O  O   . LYS I  1 63  ? 55.152  73.627  -44.003 1.00 24.52 ? 36  LYS I O   1 
ATOM   9280  C  CB  . LYS I  1 63  ? 55.461  76.995  -44.551 1.00 24.35 ? 36  LYS I CB  1 
ATOM   9281  C  CG  . LYS I  1 63  ? 54.041  76.963  -44.117 1.00 28.30 ? 36  LYS I CG  1 
ATOM   9282  C  CD  . LYS I  1 63  ? 53.717  78.400  -43.688 1.00 35.12 ? 36  LYS I CD  1 
ATOM   9283  C  CE  . LYS I  1 63  ? 52.333  78.507  -43.096 1.00 37.38 ? 36  LYS I CE  1 
ATOM   9284  N  NZ  . LYS I  1 63  ? 52.136  79.894  -42.561 1.00 44.45 ? 36  LYS I NZ  1 
ATOM   9285  N  N   . GLY I  1 64  ? 56.631  74.758  -42.757 1.00 21.57 ? 37  GLY I N   1 
ATOM   9286  C  CA  . GLY I  1 64  ? 56.482  73.797  -41.664 1.00 21.50 ? 37  GLY I CA  1 
ATOM   9287  C  C   . GLY I  1 64  ? 57.397  72.569  -41.789 1.00 23.35 ? 37  GLY I C   1 
ATOM   9288  O  O   . GLY I  1 64  ? 57.285  71.614  -41.017 1.00 23.33 ? 37  GLY I O   1 
ATOM   9289  N  N   . LEU I  1 65  ? 58.299  72.571  -42.778 1.00 23.05 ? 38  LEU I N   1 
ATOM   9290  C  CA  . LEU I  1 65  ? 59.169  71.383  -43.025 1.00 23.80 ? 38  LEU I CA  1 
ATOM   9291  C  C   . LEU I  1 65  ? 60.504  71.447  -42.281 1.00 24.10 ? 38  LEU I C   1 
ATOM   9292  O  O   . LEU I  1 65  ? 61.033  72.532  -42.112 1.00 24.89 ? 38  LEU I O   1 
ATOM   9293  C  CB  . LEU I  1 65  ? 59.510  71.349  -44.524 1.00 23.43 ? 38  LEU I CB  1 
ATOM   9294  C  CG  . LEU I  1 65  ? 58.325  70.943  -45.418 1.00 23.05 ? 38  LEU I CG  1 
ATOM   9295  C  CD1 . LEU I  1 65  ? 58.671  71.315  -46.862 1.00 23.02 ? 38  LEU I CD1 1 
ATOM   9296  C  CD2 . LEU I  1 65  ? 58.045  69.473  -45.296 1.00 22.46 ? 38  LEU I CD2 1 
ATOM   9297  N  N   . THR I  1 66  ? 61.115  70.302  -41.965 1.00 25.05 ? 39  THR I N   1 
ATOM   9298  C  CA  . THR I  1 66  ? 62.534  70.324  -41.553 1.00 24.15 ? 39  THR I CA  1 
ATOM   9299  C  C   . THR I  1 66  ? 63.436  70.747  -42.715 1.00 25.90 ? 39  THR I C   1 
ATOM   9300  O  O   . THR I  1 66  ? 63.208  70.373  -43.903 1.00 25.47 ? 39  THR I O   1 
ATOM   9301  C  CB  . THR I  1 66  ? 62.997  68.944  -41.035 1.00 25.09 ? 39  THR I CB  1 
ATOM   9302  O  OG1 . THR I  1 66  ? 62.775  67.974  -42.065 1.00 25.99 ? 39  THR I OG1 1 
ATOM   9303  C  CG2 . THR I  1 66  ? 62.228  68.508  -39.798 1.00 26.39 ? 39  THR I CG2 1 
ATOM   9304  N  N   . GLU I  1 67  ? 64.471  71.508  -42.390 1.00 21.42 ? 40  GLU I N   1 
ATOM   9305  C  CA  . GLU I  1 67  ? 65.503  71.895  -43.358 1.00 26.03 ? 40  GLU I CA  1 
ATOM   9306  C  C   . GLU I  1 67  ? 66.042  70.689  -44.171 1.00 27.66 ? 40  GLU I C   1 
ATOM   9307  O  O   . GLU I  1 67  ? 66.268  69.617  -43.601 1.00 27.81 ? 40  GLU I O   1 
ATOM   9308  C  CB  . GLU I  1 67  ? 66.660  72.574  -42.638 1.00 27.74 ? 40  GLU I CB  1 
ATOM   9309  C  CG  . GLU I  1 67  ? 67.731  73.076  -43.619 1.00 31.18 ? 40  GLU I CG  1 
ATOM   9310  C  CD  . GLU I  1 67  ? 68.841  73.870  -42.929 1.00 37.78 ? 40  GLU I CD  1 
ATOM   9311  O  OE1 . GLU I  1 67  ? 68.865  73.918  -41.686 1.00 41.47 ? 40  GLU I OE1 1 
ATOM   9312  O  OE2 . GLU I  1 67  ? 69.683  74.457  -43.634 1.00 38.61 ? 40  GLU I OE2 1 
ATOM   9313  N  N   . GLY I  1 68  ? 66.160  70.845  -45.496 1.00 25.54 ? 41  GLY I N   1 
ATOM   9314  C  CA  . GLY I  1 68  ? 66.729  69.789  -46.343 1.00 27.59 ? 41  GLY I CA  1 
ATOM   9315  C  C   . GLY I  1 68  ? 65.735  69.085  -47.264 1.00 27.85 ? 41  GLY I C   1 
ATOM   9316  O  O   . GLY I  1 68  ? 64.675  69.647  -47.560 1.00 23.74 ? 41  GLY I O   1 
ATOM   9317  N  N   . LEU I  1 69  ? 66.069  67.856  -47.705 1.00 24.64 ? 42  LEU I N   1 
ATOM   9318  C  CA  . LEU I  1 69  ? 65.329  67.178  -48.791 1.00 23.54 ? 42  LEU I CA  1 
ATOM   9319  C  C   . LEU I  1 69  ? 64.102  66.448  -48.316 1.00 22.09 ? 42  LEU I C   1 
ATOM   9320  O  O   . LEU I  1 69  ? 64.118  65.785  -47.272 1.00 23.01 ? 42  LEU I O   1 
ATOM   9321  C  CB  . LEU I  1 69  ? 66.207  66.150  -49.542 1.00 24.56 ? 42  LEU I CB  1 
ATOM   9322  C  CG  . LEU I  1 69  ? 67.414  66.719  -50.260 1.00 28.35 ? 42  LEU I CG  1 
ATOM   9323  C  CD1 . LEU I  1 69  ? 68.409  65.600  -50.628 1.00 31.39 ? 42  LEU I CD1 1 
ATOM   9324  C  CD2 . LEU I  1 69  ? 66.964  67.437  -51.517 1.00 27.36 ? 42  LEU I CD2 1 
ATOM   9325  N  N   . HIS I  1 70  ? 63.028  66.552  -49.079 1.00 19.63 ? 43  HIS I N   1 
ATOM   9326  C  CA  . HIS I  1 70  ? 61.804  65.818  -48.804 1.00 19.83 ? 43  HIS I CA  1 
ATOM   9327  C  C   . HIS I  1 70  ? 61.239  65.213  -50.075 1.00 20.13 ? 43  HIS I C   1 
ATOM   9328  O  O   . HIS I  1 70  ? 60.996  65.945  -51.049 1.00 19.77 ? 43  HIS I O   1 
ATOM   9329  C  CB  . HIS I  1 70  ? 60.726  66.773  -48.253 1.00 21.77 ? 43  HIS I CB  1 
ATOM   9330  C  CG  . HIS I  1 70  ? 61.062  67.261  -46.893 1.00 22.63 ? 43  HIS I CG  1 
ATOM   9331  N  ND1 . HIS I  1 70  ? 60.656  66.587  -45.757 1.00 25.39 ? 43  HIS I ND1 1 
ATOM   9332  C  CD2 . HIS I  1 70  ? 61.839  68.285  -46.480 1.00 23.87 ? 43  HIS I CD2 1 
ATOM   9333  C  CE1 . HIS I  1 70  ? 61.137  67.209  -44.691 1.00 24.49 ? 43  HIS I CE1 1 
ATOM   9334  N  NE2 . HIS I  1 70  ? 61.865  68.236  -45.100 1.00 24.92 ? 43  HIS I NE2 1 
ATOM   9335  N  N   . GLY I  1 71  ? 60.872  63.931  -50.010 1.00 19.22 ? 44  GLY I N   1 
ATOM   9336  C  CA  . GLY I  1 71  ? 60.213  63.268  -51.181 1.00 18.82 ? 44  GLY I CA  1 
ATOM   9337  C  C   . GLY I  1 71  ? 58.897  63.961  -51.556 1.00 21.38 ? 44  GLY I C   1 
ATOM   9338  O  O   . GLY I  1 71  ? 58.146  64.396  -50.701 1.00 18.65 ? 44  GLY I O   1 
ATOM   9339  N  N   . PHE I  1 72  ? 58.599  64.028  -52.849 1.00 19.41 ? 45  PHE I N   1 
ATOM   9340  C  CA  . PHE I  1 72  ? 57.469  64.825  -53.290 1.00 20.31 ? 45  PHE I CA  1 
ATOM   9341  C  C   . PHE I  1 72  ? 56.850  64.023  -54.411 1.00 20.94 ? 45  PHE I C   1 
ATOM   9342  O  O   . PHE I  1 72  ? 57.478  63.960  -55.472 1.00 20.69 ? 45  PHE I O   1 
ATOM   9343  C  CB  . PHE I  1 72  ? 58.085  66.103  -53.845 1.00 21.05 ? 45  PHE I CB  1 
ATOM   9344  C  CG  . PHE I  1 72  ? 57.076  67.175  -54.243 1.00 22.51 ? 45  PHE I CG  1 
ATOM   9345  C  CD1 . PHE I  1 72  ? 56.243  67.780  -53.290 1.00 23.71 ? 45  PHE I CD1 1 
ATOM   9346  C  CD2 . PHE I  1 72  ? 57.070  67.668  -55.540 1.00 21.93 ? 45  PHE I CD2 1 
ATOM   9347  C  CE1 . PHE I  1 72  ? 55.365  68.813  -53.649 1.00 24.22 ? 45  PHE I CE1 1 
ATOM   9348  C  CE2 . PHE I  1 72  ? 56.177  68.699  -55.916 1.00 24.19 ? 45  PHE I CE2 1 
ATOM   9349  C  CZ  . PHE I  1 72  ? 55.336  69.270  -54.965 1.00 24.90 ? 45  PHE I CZ  1 
ATOM   9350  N  N   . HIS I  1 73  ? 55.701  63.380  -54.182 1.00 20.58 ? 46  HIS I N   1 
ATOM   9351  C  CA  . HIS I  1 73  ? 55.145  62.392  -55.147 1.00 22.71 ? 46  HIS I CA  1 
ATOM   9352  C  C   . HIS I  1 73  ? 53.687  62.558  -55.410 1.00 24.31 ? 46  HIS I C   1 
ATOM   9353  O  O   . HIS I  1 73  ? 52.905  62.943  -54.517 1.00 23.85 ? 46  HIS I O   1 
ATOM   9354  C  CB  . HIS I  1 73  ? 55.357  60.956  -54.667 1.00 21.67 ? 46  HIS I CB  1 
ATOM   9355  C  CG  . HIS I  1 73  ? 56.763  60.692  -54.259 1.00 24.62 ? 46  HIS I CG  1 
ATOM   9356  N  ND1 . HIS I  1 73  ? 57.113  60.258  -53.002 1.00 27.26 ? 46  HIS I ND1 1 
ATOM   9357  C  CD2 . HIS I  1 73  ? 57.922  60.864  -54.933 1.00 23.71 ? 46  HIS I CD2 1 
ATOM   9358  C  CE1 . HIS I  1 73  ? 58.426  60.145  -52.931 1.00 23.84 ? 46  HIS I CE1 1 
ATOM   9359  N  NE2 . HIS I  1 73  ? 58.944  60.564  -54.064 1.00 25.91 ? 46  HIS I NE2 1 
ATOM   9360  N  N   . VAL I  1 74  ? 53.291  62.197  -56.630 1.00 22.35 ? 47  VAL I N   1 
ATOM   9361  C  CA  . VAL I  1 74  ? 51.874  61.995  -56.914 1.00 23.91 ? 47  VAL I CA  1 
ATOM   9362  C  C   . VAL I  1 74  ? 51.505  60.544  -56.624 1.00 25.23 ? 47  VAL I C   1 
ATOM   9363  O  O   . VAL I  1 74  ? 52.123  59.566  -57.148 1.00 22.06 ? 47  VAL I O   1 
ATOM   9364  C  CB  . VAL I  1 74  ? 51.497  62.423  -58.364 1.00 23.01 ? 47  VAL I CB  1 
ATOM   9365  C  CG1 . VAL I  1 74  ? 50.000  62.335  -58.597 1.00 22.02 ? 47  VAL I CG1 1 
ATOM   9366  C  CG2 . VAL I  1 74  ? 52.011  63.835  -58.605 1.00 22.74 ? 47  VAL I CG2 1 
ATOM   9367  N  N   . HIS I  1 75  ? 50.528  60.388  -55.728 1.00 22.25 ? 48  HIS I N   1 
ATOM   9368  C  CA  . HIS I  1 75  ? 50.027  59.079  -55.348 1.00 21.71 ? 48  HIS I CA  1 
ATOM   9369  C  C   . HIS I  1 75  ? 48.754  58.777  -56.134 1.00 23.04 ? 48  HIS I C   1 
ATOM   9370  O  O   . HIS I  1 75  ? 48.148  59.666  -56.702 1.00 26.17 ? 48  HIS I O   1 
ATOM   9371  C  CB  . HIS I  1 75  ? 49.810  58.962  -53.839 1.00 22.89 ? 48  HIS I CB  1 
ATOM   9372  C  CG  . HIS I  1 75  ? 51.088  58.975  -53.055 1.00 20.96 ? 48  HIS I CG  1 
ATOM   9373  N  ND1 . HIS I  1 75  ? 51.468  57.944  -52.229 1.00 21.59 ? 48  HIS I ND1 1 
ATOM   9374  C  CD2 . HIS I  1 75  ? 52.097  59.876  -53.022 1.00 21.10 ? 48  HIS I CD2 1 
ATOM   9375  C  CE1 . HIS I  1 75  ? 52.630  58.234  -51.668 1.00 20.44 ? 48  HIS I CE1 1 
ATOM   9376  N  NE2 . HIS I  1 75  ? 53.045  59.394  -52.159 1.00 21.24 ? 48  HIS I NE2 1 
ATOM   9377  N  N   . GLU I  1 76  ? 48.418  57.504  -56.215 1.00 24.40 ? 49  GLU I N   1 
ATOM   9378  C  CA  . GLU I  1 76  ? 47.456  57.022  -57.179 1.00 25.87 ? 49  GLU I CA  1 
ATOM   9379  C  C   . GLU I  1 76  ? 46.002  57.505  -56.920 1.00 27.51 ? 49  GLU I C   1 
ATOM   9380  O  O   . GLU I  1 76  ? 45.336  57.909  -57.850 1.00 26.41 ? 49  GLU I O   1 
ATOM   9381  C  CB  . GLU I  1 76  ? 47.515  55.497  -57.221 1.00 28.12 ? 49  GLU I CB  1 
ATOM   9382  C  CG  . GLU I  1 76  ? 46.494  54.892  -58.202 1.00 29.89 ? 49  GLU I CG  1 
ATOM   9383  C  CD  . GLU I  1 76  ? 46.527  53.369  -58.253 1.00 34.30 ? 49  GLU I CD  1 
ATOM   9384  O  OE1 . GLU I  1 76  ? 47.230  52.697  -57.451 1.00 33.11 ? 49  GLU I OE1 1 
ATOM   9385  O  OE2 . GLU I  1 76  ? 45.766  52.853  -59.092 1.00 42.18 ? 49  GLU I OE2 1 
ATOM   9386  N  N   . PHE I  1 77  ? 45.559  57.546  -55.658 1.00 26.00 ? 50  PHE I N   1 
ATOM   9387  C  CA  . PHE I  1 77  ? 44.153  57.845  -55.376 1.00 25.57 ? 50  PHE I CA  1 
ATOM   9388  C  C   . PHE I  1 77  ? 43.949  59.224  -54.770 1.00 26.34 ? 50  PHE I C   1 
ATOM   9389  O  O   . PHE I  1 77  ? 44.745  59.625  -53.948 1.00 25.43 ? 50  PHE I O   1 
ATOM   9390  C  CB  . PHE I  1 77  ? 43.582  56.792  -54.444 1.00 28.62 ? 50  PHE I CB  1 
ATOM   9391  C  CG  . PHE I  1 77  ? 43.735  55.416  -54.971 1.00 32.37 ? 50  PHE I CG  1 
ATOM   9392  C  CD1 . PHE I  1 77  ? 43.154  55.081  -56.183 1.00 36.13 ? 50  PHE I CD1 1 
ATOM   9393  C  CD2 . PHE I  1 77  ? 44.493  54.472  -54.276 1.00 35.26 ? 50  PHE I CD2 1 
ATOM   9394  C  CE1 . PHE I  1 77  ? 43.323  53.802  -56.702 1.00 40.27 ? 50  PHE I CE1 1 
ATOM   9395  C  CE2 . PHE I  1 77  ? 44.670  53.192  -54.794 1.00 36.67 ? 50  PHE I CE2 1 
ATOM   9396  C  CZ  . PHE I  1 77  ? 44.079  52.867  -56.002 1.00 36.86 ? 50  PHE I CZ  1 
ATOM   9397  N  N   . GLY I  1 78  ? 42.890  59.923  -55.183 1.00 26.30 ? 51  GLY I N   1 
ATOM   9398  C  CA  . GLY I  1 78  ? 42.505  61.222  -54.604 1.00 26.39 ? 51  GLY I CA  1 
ATOM   9399  C  C   . GLY I  1 78  ? 41.542  60.951  -53.452 1.00 28.30 ? 51  GLY I C   1 
ATOM   9400  O  O   . GLY I  1 78  ? 40.480  61.516  -53.396 1.00 30.89 ? 51  GLY I O   1 
ATOM   9401  N  N   . ASP I  1 79  ? 41.943  60.065  -52.551 1.00 29.86 ? 52  ASP I N   1 
ATOM   9402  C  CA  . ASP I  1 79  ? 41.118  59.589  -51.450 1.00 28.92 ? 52  ASP I CA  1 
ATOM   9403  C  C   . ASP I  1 79  ? 41.830  59.980  -50.153 1.00 29.81 ? 52  ASP I C   1 
ATOM   9404  O  O   . ASP I  1 79  ? 42.961  59.540  -49.851 1.00 26.91 ? 52  ASP I O   1 
ATOM   9405  C  CB  . ASP I  1 79  ? 40.950  58.072  -51.598 1.00 31.19 ? 52  ASP I CB  1 
ATOM   9406  C  CG  . ASP I  1 79  ? 40.133  57.447  -50.483 1.00 34.26 ? 52  ASP I CG  1 
ATOM   9407  O  OD1 . ASP I  1 79  ? 40.000  58.053  -49.397 1.00 33.69 ? 52  ASP I OD1 1 
ATOM   9408  O  OD2 . ASP I  1 79  ? 39.651  56.316  -50.711 1.00 38.62 ? 52  ASP I OD2 1 
ATOM   9409  N  N   . ASN I  1 80  ? 41.213  60.913  -49.436 1.00 28.59 ? 53  ASN I N   1 
ATOM   9410  C  CA  . ASN I  1 80  ? 41.774  61.427  -48.208 1.00 29.36 ? 53  ASN I CA  1 
ATOM   9411  C  C   . ASN I  1 80  ? 40.922  60.983  -46.999 1.00 30.14 ? 53  ASN I C   1 
ATOM   9412  O  O   . ASN I  1 80  ? 41.061  61.531  -45.905 1.00 30.04 ? 53  ASN I O   1 
ATOM   9413  C  CB  . ASN I  1 80  ? 41.842  62.942  -48.258 1.00 35.27 ? 53  ASN I CB  1 
ATOM   9414  C  CG  . ASN I  1 80  ? 42.675  63.529  -47.121 1.00 43.04 ? 53  ASN I CG  1 
ATOM   9415  O  OD1 . ASN I  1 80  ? 43.786  63.056  -46.839 1.00 47.50 ? 53  ASN I OD1 1 
ATOM   9416  N  ND2 . ASN I  1 80  ? 42.133  64.562  -46.450 1.00 43.06 ? 53  ASN I ND2 1 
ATOM   9417  N  N   . THR I  1 81  ? 40.077  59.993  -47.209 1.00 29.03 ? 54  THR I N   1 
ATOM   9418  C  CA  . THR I  1 81  ? 39.125  59.543  -46.183 1.00 33.08 ? 54  THR I CA  1 
ATOM   9419  C  C   . THR I  1 81  ? 39.859  59.042  -44.934 1.00 35.86 ? 54  THR I C   1 
ATOM   9420  O  O   . THR I  1 81  ? 39.344  59.208  -43.837 1.00 35.52 ? 54  THR I O   1 
ATOM   9421  C  CB  . THR I  1 81  ? 38.201  58.416  -46.664 1.00 34.95 ? 54  THR I CB  1 
ATOM   9422  O  OG1 . THR I  1 81  ? 38.997  57.289  -47.011 1.00 35.86 ? 54  THR I OG1 1 
ATOM   9423  C  CG2 . THR I  1 81  ? 37.415  58.800  -47.858 1.00 34.53 ? 54  THR I CG2 1 
ATOM   9424  N  N   . ALA I  1 82  ? 41.059  58.464  -45.070 1.00 34.26 ? 55  ALA I N   1 
ATOM   9425  C  CA  . ALA I  1 82  ? 41.850  58.077  -43.888 1.00 35.06 ? 55  ALA I CA  1 
ATOM   9426  C  C   . ALA I  1 82  ? 43.072  58.959  -43.749 1.00 35.62 ? 55  ALA I C   1 
ATOM   9427  O  O   . ALA I  1 82  ? 44.102  58.487  -43.324 1.00 39.39 ? 55  ALA I O   1 
ATOM   9428  C  CB  . ALA I  1 82  ? 42.251  56.584  -43.933 1.00 34.99 ? 55  ALA I CB  1 
ATOM   9429  N  N   . GLY I  1 83  ? 42.979  60.239  -44.108 1.00 31.69 ? 56  GLY I N   1 
ATOM   9430  C  CA  . GLY I  1 83  ? 44.183  61.067  -44.218 1.00 31.39 ? 56  GLY I CA  1 
ATOM   9431  C  C   . GLY I  1 83  ? 45.076  60.635  -45.396 1.00 29.73 ? 56  GLY I C   1 
ATOM   9432  O  O   . GLY I  1 83  ? 44.610  60.026  -46.370 1.00 32.13 ? 56  GLY I O   1 
ATOM   9433  N  N   . CYS I  1 84  ? 46.361  60.933  -45.305 1.00 30.79 ? 57  CYS I N   1 
ATOM   9434  C  CA  . CYS I  1 84  ? 47.263  60.726  -46.436 1.00 30.92 ? 57  CYS I CA  1 
ATOM   9435  C  C   . CYS I  1 84  ? 47.442  59.238  -46.779 1.00 31.55 ? 57  CYS I C   1 
ATOM   9436  O  O   . CYS I  1 84  ? 47.734  58.891  -47.915 1.00 26.60 ? 57  CYS I O   1 
ATOM   9437  C  CB  . CYS I  1 84  ? 48.584  61.422  -46.166 1.00 33.15 ? 57  CYS I CB  1 
ATOM   9438  S  SG  . CYS I  1 84  ? 48.420  63.264  -46.106 1.00 37.52 ? 57  CYS I SG  1 
ATOM   9439  N  N   . THR I  1 85  ? 47.234  58.366  -45.803 1.00 29.41 ? 58  THR I N   1 
ATOM   9440  C  CA  . THR I  1 85  ? 47.353  56.914  -46.020 1.00 32.50 ? 58  THR I CA  1 
ATOM   9441  C  C   . THR I  1 85  ? 46.455  56.412  -47.133 1.00 32.47 ? 58  THR I C   1 
ATOM   9442  O  O   . THR I  1 85  ? 46.880  55.561  -47.945 1.00 33.72 ? 58  THR I O   1 
ATOM   9443  C  CB  . THR I  1 85  ? 47.013  56.134  -44.753 1.00 32.57 ? 58  THR I CB  1 
ATOM   9444  O  OG1 . THR I  1 85  ? 47.760  56.704  -43.689 1.00 40.91 ? 58  THR I OG1 1 
ATOM   9445  C  CG2 . THR I  1 85  ? 47.429  54.669  -44.900 1.00 35.56 ? 58  THR I CG2 1 
ATOM   9446  N  N   . SER I  1 86  ? 45.233  56.941  -47.227 1.00 29.30 ? 59  SER I N   1 
ATOM   9447  C  CA  . SER I  1 86  ? 44.312  56.428  -48.222 1.00 29.71 ? 59  SER I CA  1 
ATOM   9448  C  C   . SER I  1 86  ? 44.675  56.823  -49.654 1.00 28.63 ? 59  SER I C   1 
ATOM   9449  O  O   . SER I  1 86  ? 44.008  56.381  -50.577 1.00 29.53 ? 59  SER I O   1 
ATOM   9450  C  CB  . SER I  1 86  ? 42.853  56.792  -47.900 1.00 33.70 ? 59  SER I CB  1 
ATOM   9451  O  OG  . SER I  1 86  ? 42.819  58.055  -47.316 1.00 38.80 ? 59  SER I OG  1 
ATOM   9452  N  N   . ALA I  1 87  ? 45.728  57.630  -49.833 1.00 25.99 ? 60  ALA I N   1 
ATOM   9453  C  CA  . ALA I  1 87  ? 46.169  58.012  -51.205 1.00 28.30 ? 60  ALA I CA  1 
ATOM   9454  C  C   . ALA I  1 87  ? 46.765  56.840  -51.963 1.00 27.83 ? 60  ALA I C   1 
ATOM   9455  O  O   . ALA I  1 87  ? 46.941  56.933  -53.173 1.00 32.51 ? 60  ALA I O   1 
ATOM   9456  C  CB  . ALA I  1 87  ? 47.156  59.180  -51.196 1.00 24.63 ? 60  ALA I CB  1 
ATOM   9457  N  N   . GLY I  1 88  ? 47.087  55.751  -51.259 1.00 28.20 ? 61  GLY I N   1 
ATOM   9458  C  CA  . GLY I  1 88  ? 47.621  54.537  -51.926 1.00 28.24 ? 61  GLY I CA  1 
ATOM   9459  C  C   . GLY I  1 88  ? 49.085  54.756  -52.328 1.00 27.37 ? 61  GLY I C   1 
ATOM   9460  O  O   . GLY I  1 88  ? 49.729  55.675  -51.824 1.00 26.41 ? 61  GLY I O   1 
ATOM   9461  N  N   . PRO I  1 89  ? 49.623  53.928  -53.252 1.00 27.30 ? 62  PRO I N   1 
ATOM   9462  C  CA  . PRO I  1 89  ? 51.064  54.027  -53.582 1.00 25.67 ? 62  PRO I CA  1 
ATOM   9463  C  C   . PRO I  1 89  ? 51.352  55.146  -54.582 1.00 25.34 ? 62  PRO I C   1 
ATOM   9464  O  O   . PRO I  1 89  ? 50.444  55.844  -55.013 1.00 23.56 ? 62  PRO I O   1 
ATOM   9465  C  CB  . PRO I  1 89  ? 51.346  52.655  -54.253 1.00 27.15 ? 62  PRO I CB  1 
ATOM   9466  C  CG  . PRO I  1 89  ? 50.064  52.329  -54.949 1.00 24.97 ? 62  PRO I CG  1 
ATOM   9467  C  CD  . PRO I  1 89  ? 48.932  52.915  -54.077 1.00 28.41 ? 62  PRO I CD  1 
ATOM   9468  N  N   . HIS I  1 90  ? 52.612  55.292  -55.016 1.00 26.40 ? 63  HIS I N   1 
ATOM   9469  C  CA  . HIS I  1 90  ? 52.913  56.279  -56.065 1.00 24.83 ? 63  HIS I CA  1 
ATOM   9470  C  C   . HIS I  1 90  ? 52.131  55.955  -57.305 1.00 26.62 ? 63  HIS I C   1 
ATOM   9471  O  O   . HIS I  1 90  ? 51.963  54.767  -57.625 1.00 25.77 ? 63  HIS I O   1 
ATOM   9472  C  CB  . HIS I  1 90  ? 54.403  56.263  -56.378 1.00 24.71 ? 63  HIS I CB  1 
ATOM   9473  C  CG  . HIS I  1 90  ? 55.247  56.677  -55.217 1.00 25.34 ? 63  HIS I CG  1 
ATOM   9474  N  ND1 . HIS I  1 90  ? 56.616  56.776  -55.288 1.00 26.62 ? 63  HIS I ND1 1 
ATOM   9475  C  CD2 . HIS I  1 90  ? 54.916  57.025  -53.944 1.00 23.89 ? 63  HIS I CD2 1 
ATOM   9476  C  CE1 . HIS I  1 90  ? 57.107  57.140  -54.120 1.00 25.49 ? 63  HIS I CE1 1 
ATOM   9477  N  NE2 . HIS I  1 90  ? 56.092  57.292  -53.283 1.00 26.81 ? 63  HIS I NE2 1 
ATOM   9478  N  N   . PHE I  1 91  ? 51.640  56.984  -57.993 1.00 24.47 ? 64  PHE I N   1 
ATOM   9479  C  CA  . PHE I  1 91  ? 50.924  56.813  -59.255 1.00 26.65 ? 64  PHE I CA  1 
ATOM   9480  C  C   . PHE I  1 91  ? 51.878  56.144  -60.297 1.00 29.31 ? 64  PHE I C   1 
ATOM   9481  O  O   . PHE I  1 91  ? 52.923  56.706  -60.638 1.00 26.80 ? 64  PHE I O   1 
ATOM   9482  C  CB  . PHE I  1 91  ? 50.463  58.169  -59.754 1.00 25.34 ? 64  PHE I CB  1 
ATOM   9483  C  CG  . PHE I  1 91  ? 49.680  58.114  -61.047 1.00 26.65 ? 64  PHE I CG  1 
ATOM   9484  C  CD1 . PHE I  1 91  ? 48.790  57.070  -61.311 1.00 26.35 ? 64  PHE I CD1 1 
ATOM   9485  C  CD2 . PHE I  1 91  ? 49.800  59.146  -61.973 1.00 29.20 ? 64  PHE I CD2 1 
ATOM   9486  C  CE1 . PHE I  1 91  ? 48.076  57.067  -62.524 1.00 28.18 ? 64  PHE I CE1 1 
ATOM   9487  C  CE2 . PHE I  1 91  ? 49.079  59.155  -63.166 1.00 32.21 ? 64  PHE I CE2 1 
ATOM   9488  C  CZ  . PHE I  1 91  ? 48.208  58.109  -63.443 1.00 26.32 ? 64  PHE I CZ  1 
ATOM   9489  N  N   . ASN I  1 92  ? 51.509  54.950  -60.775 1.00 29.57 ? 65  ASN I N   1 
ATOM   9490  C  CA  . ASN I  1 92  ? 52.431  54.103  -61.535 1.00 27.17 ? 65  ASN I CA  1 
ATOM   9491  C  C   . ASN I  1 92  ? 51.614  53.314  -62.586 1.00 31.77 ? 65  ASN I C   1 
ATOM   9492  O  O   . ASN I  1 92  ? 51.587  52.089  -62.526 1.00 34.10 ? 65  ASN I O   1 
ATOM   9493  C  CB  . ASN I  1 92  ? 53.076  53.127  -60.572 1.00 28.31 ? 65  ASN I CB  1 
ATOM   9494  C  CG  . ASN I  1 92  ? 54.177  52.255  -61.213 1.00 28.78 ? 65  ASN I CG  1 
ATOM   9495  O  OD1 . ASN I  1 92  ? 54.749  52.589  -62.252 1.00 28.09 ? 65  ASN I OD1 1 
ATOM   9496  N  ND2 . ASN I  1 92  ? 54.521  51.169  -60.517 1.00 27.44 ? 65  ASN I ND2 1 
ATOM   9497  N  N   . PRO I  1 93  ? 50.983  54.012  -63.550 1.00 30.14 ? 66  PRO I N   1 
ATOM   9498  C  CA  . PRO I  1 93  ? 50.119  53.271  -64.470 1.00 33.19 ? 66  PRO I CA  1 
ATOM   9499  C  C   . PRO I  1 93  ? 50.914  52.323  -65.405 1.00 38.79 ? 66  PRO I C   1 
ATOM   9500  O  O   . PRO I  1 93  ? 50.327  51.437  -66.009 1.00 39.44 ? 66  PRO I O   1 
ATOM   9501  C  CB  . PRO I  1 93  ? 49.406  54.370  -65.249 1.00 33.32 ? 66  PRO I CB  1 
ATOM   9502  C  CG  . PRO I  1 93  ? 50.324  55.570  -65.176 1.00 31.57 ? 66  PRO I CG  1 
ATOM   9503  C  CD  . PRO I  1 93  ? 51.050  55.453  -63.868 1.00 29.92 ? 66  PRO I CD  1 
ATOM   9504  N  N   . LEU I  1 94  ? 52.237  52.475  -65.484 1.00 39.68 ? 67  LEU I N   1 
ATOM   9505  C  CA  . LEU I  1 94  ? 53.042  51.622  -66.369 1.00 38.29 ? 67  LEU I CA  1 
ATOM   9506  C  C   . LEU I  1 94  ? 53.803  50.531  -65.633 1.00 42.04 ? 67  LEU I C   1 
ATOM   9507  O  O   . LEU I  1 94  ? 54.591  49.835  -66.256 1.00 40.32 ? 67  LEU I O   1 
ATOM   9508  C  CB  . LEU I  1 94  ? 53.988  52.477  -67.223 1.00 38.05 ? 67  LEU I CB  1 
ATOM   9509  C  CG  . LEU I  1 94  ? 53.404  53.603  -68.079 1.00 39.93 ? 67  LEU I CG  1 
ATOM   9510  C  CD1 . LEU I  1 94  ? 54.524  54.486  -68.630 1.00 40.95 ? 67  LEU I CD1 1 
ATOM   9511  C  CD2 . LEU I  1 94  ? 52.530  53.086  -69.221 1.00 40.15 ? 67  LEU I CD2 1 
ATOM   9512  N  N   . SER I  1 95  ? 53.537  50.356  -64.329 1.00 38.25 ? 68  SER I N   1 
ATOM   9513  C  CA  . SER I  1 95  ? 54.210  49.360  -63.441 1.00 38.61 ? 68  SER I CA  1 
ATOM   9514  C  C   . SER I  1 95  ? 55.716  49.332  -63.550 1.00 42.04 ? 68  SER I C   1 
ATOM   9515  O  O   . SER I  1 95  ? 56.293  48.300  -63.896 1.00 40.42 ? 68  SER I O   1 
ATOM   9516  C  CB  . SER I  1 95  ? 53.717  47.921  -63.664 1.00 42.73 ? 68  SER I CB  1 
ATOM   9517  O  OG  . SER I  1 95  ? 52.340  47.898  -63.951 1.00 45.75 ? 68  SER I OG  1 
ATOM   9518  N  N   . ARG I  1 96  ? 56.355  50.444  -63.233 1.00 37.56 ? 69  ARG I N   1 
ATOM   9519  C  CA  . ARG I  1 96  ? 57.804  50.508  -63.260 1.00 35.34 ? 69  ARG I CA  1 
ATOM   9520  C  C   . ARG I  1 96  ? 58.267  50.527  -61.833 1.00 33.87 ? 69  ARG I C   1 
ATOM   9521  O  O   . ARG I  1 96  ? 57.437  50.580  -60.917 1.00 31.30 ? 69  ARG I O   1 
ATOM   9522  C  CB  . ARG I  1 96  ? 58.241  51.767  -63.964 1.00 35.72 ? 69  ARG I CB  1 
ATOM   9523  C  CG  . ARG I  1 96  ? 57.545  51.979  -65.296 1.00 45.65 ? 69  ARG I CG  1 
ATOM   9524  C  CD  . ARG I  1 96  ? 58.278  51.309  -66.436 1.00 47.48 ? 69  ARG I CD  1 
ATOM   9525  N  NE  . ARG I  1 96  ? 57.871  51.885  -67.720 1.00 56.13 ? 69  ARG I NE  1 
ATOM   9526  C  CZ  . ARG I  1 96  ? 58.505  52.877  -68.354 1.00 60.42 ? 69  ARG I CZ  1 
ATOM   9527  N  NH1 . ARG I  1 96  ? 59.601  53.426  -67.829 1.00 65.77 ? 69  ARG I NH1 1 
ATOM   9528  N  NH2 . ARG I  1 96  ? 58.044  53.321  -69.520 1.00 55.21 ? 69  ARG I NH2 1 
ATOM   9529  N  N   . LYS I  1 97  ? 59.575  50.443  -61.639 1.00 32.46 ? 70  LYS I N   1 
ATOM   9530  C  CA  . LYS I  1 97  ? 60.152  50.659  -60.327 1.00 33.91 ? 70  LYS I CA  1 
ATOM   9531  C  C   . LYS I  1 97  ? 60.216  52.174  -60.068 1.00 28.63 ? 70  LYS I C   1 
ATOM   9532  O  O   . LYS I  1 97  ? 60.228  52.997  -60.997 1.00 26.11 ? 70  LYS I O   1 
ATOM   9533  C  CB  . LYS I  1 97  ? 61.583  50.099  -60.233 1.00 37.88 ? 70  LYS I CB  1 
ATOM   9534  C  CG  . LYS I  1 97  ? 61.745  48.630  -60.613 1.00 46.29 ? 70  LYS I CG  1 
ATOM   9535  C  CD  . LYS I  1 97  ? 60.797  47.713  -59.854 1.00 46.61 ? 70  LYS I CD  1 
ATOM   9536  C  CE  . LYS I  1 97  ? 61.182  46.249  -60.047 1.00 56.45 ? 70  LYS I CE  1 
ATOM   9537  N  NZ  . LYS I  1 97  ? 62.672  46.074  -59.971 1.00 62.50 ? 70  LYS I NZ  1 
ATOM   9538  N  N   . HIS I  1 98  ? 60.358  52.501  -58.797 1.00 30.77 ? 71  HIS I N   1 
ATOM   9539  C  CA  . HIS I  1 98  ? 60.532  53.896  -58.394 1.00 26.43 ? 71  HIS I CA  1 
ATOM   9540  C  C   . HIS I  1 98  ? 61.872  54.442  -58.937 1.00 29.28 ? 71  HIS I C   1 
ATOM   9541  O  O   . HIS I  1 98  ? 62.891  53.743  -58.907 1.00 27.82 ? 71  HIS I O   1 
ATOM   9542  C  CB  . HIS I  1 98  ? 60.481  53.960  -56.865 1.00 25.29 ? 71  HIS I CB  1 
ATOM   9543  C  CG  . HIS I  1 98  ? 60.742  55.330  -56.323 1.00 26.04 ? 71  HIS I CG  1 
ATOM   9544  N  ND1 . HIS I  1 98  ? 59.774  56.318  -56.322 1.00 26.15 ? 71  HIS I ND1 1 
ATOM   9545  C  CD2 . HIS I  1 98  ? 61.851  55.879  -55.779 1.00 23.91 ? 71  HIS I CD2 1 
ATOM   9546  C  CE1 . HIS I  1 98  ? 60.292  57.427  -55.814 1.00 25.76 ? 71  HIS I CE1 1 
ATOM   9547  N  NE2 . HIS I  1 98  ? 61.545  57.185  -55.465 1.00 24.28 ? 71  HIS I NE2 1 
ATOM   9548  N  N   . GLY I  1 99  ? 61.882  55.681  -59.411 1.00 25.57 ? 72  GLY I N   1 
ATOM   9549  C  CA  . GLY I  1 99  ? 63.132  56.340  -59.773 1.00 25.14 ? 72  GLY I CA  1 
ATOM   9550  C  C   . GLY I  1 99  ? 63.053  57.824  -59.471 1.00 25.92 ? 72  GLY I C   1 
ATOM   9551  O  O   . GLY I  1 99  ? 62.081  58.323  -58.859 1.00 25.01 ? 72  GLY I O   1 
ATOM   9552  N  N   . GLY I  1 100 ? 64.085  58.545  -59.889 1.00 25.82 ? 73  GLY I N   1 
ATOM   9553  C  CA  . GLY I  1 100 ? 64.073  59.993  -59.819 1.00 26.04 ? 73  GLY I CA  1 
ATOM   9554  C  C   . GLY I  1 100 ? 63.404  60.518  -61.069 1.00 27.32 ? 73  GLY I C   1 
ATOM   9555  O  O   . GLY I  1 100 ? 63.201  59.761  -62.022 1.00 30.75 ? 73  GLY I O   1 
ATOM   9556  N  N   . PRO I  1 101 ? 63.082  61.827  -61.097 1.00 28.20 ? 74  PRO I N   1 
ATOM   9557  C  CA  . PRO I  1 101 ? 62.348  62.398  -62.204 1.00 29.36 ? 74  PRO I CA  1 
ATOM   9558  C  C   . PRO I  1 101 ? 63.092  62.315  -63.549 1.00 33.76 ? 74  PRO I C   1 
ATOM   9559  O  O   . PRO I  1 101 ? 62.436  62.309  -64.591 1.00 31.73 ? 74  PRO I O   1 
ATOM   9560  C  CB  . PRO I  1 101 ? 62.145  63.877  -61.799 1.00 30.46 ? 74  PRO I CB  1 
ATOM   9561  C  CG  . PRO I  1 101 ? 63.005  64.098  -60.602 1.00 30.56 ? 74  PRO I CG  1 
ATOM   9562  C  CD  . PRO I  1 101 ? 63.144  62.751  -59.952 1.00 28.47 ? 74  PRO I CD  1 
ATOM   9563  N  N   . LYS I  1 102 ? 64.425  62.330  -63.515 1.00 33.82 ? 75  LYS I N   1 
ATOM   9564  C  CA  . LYS I  1 102 ? 65.226  62.287  -64.739 1.00 39.02 ? 75  LYS I CA  1 
ATOM   9565  C  C   . LYS I  1 102 ? 65.476  60.850  -65.213 1.00 38.78 ? 75  LYS I C   1 
ATOM   9566  O  O   . LYS I  1 102 ? 66.051  60.661  -66.280 1.00 41.32 ? 75  LYS I O   1 
ATOM   9567  C  CB  . LYS I  1 102 ? 66.572  63.003  -64.520 1.00 41.02 ? 75  LYS I CB  1 
ATOM   9568  C  CG  . LYS I  1 102 ? 66.463  64.503  -64.233 1.00 44.55 ? 75  LYS I CG  1 
ATOM   9569  C  CD  . LYS I  1 102 ? 67.642  64.943  -63.347 1.00 54.25 ? 75  LYS I CD  1 
ATOM   9570  C  CE  . LYS I  1 102 ? 68.959  65.205  -64.097 1.00 57.68 ? 75  LYS I CE  1 
ATOM   9571  N  NZ  . LYS I  1 102 ? 69.989  65.867  -63.225 1.00 54.66 ? 75  LYS I NZ  1 
ATOM   9572  N  N   . ASP I  1 103 ? 65.077  59.845  -64.434 1.00 34.79 ? 76  ASP I N   1 
ATOM   9573  C  CA  . ASP I  1 103 ? 65.248  58.422  -64.843 1.00 35.96 ? 76  ASP I CA  1 
ATOM   9574  C  C   . ASP I  1 103 ? 64.212  57.951  -65.885 1.00 39.02 ? 76  ASP I C   1 
ATOM   9575  O  O   . ASP I  1 103 ? 63.054  58.391  -65.850 1.00 38.51 ? 76  ASP I O   1 
ATOM   9576  C  CB  . ASP I  1 103 ? 65.234  57.511  -63.606 1.00 38.98 ? 76  ASP I CB  1 
ATOM   9577  C  CG  . ASP I  1 103 ? 66.415  57.757  -62.684 1.00 45.45 ? 76  ASP I CG  1 
ATOM   9578  O  OD1 . ASP I  1 103 ? 67.490  58.105  -63.238 1.00 52.31 ? 76  ASP I OD1 1 
ATOM   9579  O  OD2 . ASP I  1 103 ? 66.294  57.622  -61.421 1.00 41.03 ? 76  ASP I OD2 1 
ATOM   9580  N  N   . GLU I  1 104 ? 64.576  57.069  -66.833 1.00 42.16 ? 77  GLU I N   1 
ATOM   9581  C  CA  . GLU I  1 104 ? 63.490  56.513  -67.699 1.00 45.96 ? 77  GLU I CA  1 
ATOM   9582  C  C   . GLU I  1 104 ? 62.666  55.439  -66.976 1.00 38.49 ? 77  GLU I C   1 
ATOM   9583  O  O   . GLU I  1 104 ? 61.438  55.320  -67.193 1.00 41.04 ? 77  GLU I O   1 
ATOM   9584  C  CB  . GLU I  1 104 ? 63.927  56.092  -69.124 1.00 51.18 ? 77  GLU I CB  1 
ATOM   9585  C  CG  . GLU I  1 104 ? 64.749  54.810  -69.213 1.00 63.66 ? 77  GLU I CG  1 
ATOM   9586  C  CD  . GLU I  1 104 ? 66.218  55.031  -68.871 1.00 70.70 ? 77  GLU I CD  1 
ATOM   9587  O  OE1 . GLU I  1 104 ? 67.097  54.745  -69.739 1.00 67.43 ? 77  GLU I OE1 1 
ATOM   9588  O  OE2 . GLU I  1 104 ? 66.482  55.512  -67.738 1.00 69.89 ? 77  GLU I OE2 1 
ATOM   9589  N  N   . GLU I  1 105 ? 63.315  54.709  -66.068 1.00 32.13 ? 78  GLU I N   1 
ATOM   9590  C  CA  . GLU I  1 105 ? 62.614  53.810  -65.162 1.00 32.08 ? 78  GLU I CA  1 
ATOM   9591  C  C   . GLU I  1 105 ? 62.145  54.624  -63.897 1.00 30.57 ? 78  GLU I C   1 
ATOM   9592  O  O   . GLU I  1 105 ? 62.935  54.889  -62.974 1.00 29.28 ? 78  GLU I O   1 
ATOM   9593  C  CB  . GLU I  1 105 ? 63.517  52.656  -64.726 1.00 34.94 ? 78  GLU I CB  1 
ATOM   9594  C  CG  . GLU I  1 105 ? 62.887  51.621  -63.797 1.00 40.23 ? 78  GLU I CG  1 
ATOM   9595  C  CD  . GLU I  1 105 ? 61.889  50.704  -64.490 1.00 45.57 ? 78  GLU I CD  1 
ATOM   9596  O  OE1 . GLU I  1 105 ? 61.773  50.802  -65.732 1.00 54.76 ? 78  GLU I OE1 1 
ATOM   9597  O  OE2 . GLU I  1 105 ? 61.213  49.881  -63.818 1.00 41.11 ? 78  GLU I OE2 1 
ATOM   9598  N  N   . ARG I  1 106 ? 60.861  54.947  -63.866 1.00 28.38 ? 79  ARG I N   1 
ATOM   9599  C  CA  . ARG I  1 106 ? 60.303  55.687  -62.719 1.00 29.40 ? 79  ARG I CA  1 
ATOM   9600  C  C   . ARG I  1 106 ? 58.783  55.528  -62.741 1.00 30.89 ? 79  ARG I C   1 
ATOM   9601  O  O   . ARG I  1 106 ? 58.192  55.184  -63.787 1.00 30.56 ? 79  ARG I O   1 
ATOM   9602  C  CB  . ARG I  1 106 ? 60.669  57.174  -62.819 1.00 25.59 ? 79  ARG I CB  1 
ATOM   9603  C  CG  . ARG I  1 106 ? 60.206  57.821  -64.129 1.00 26.79 ? 79  ARG I CG  1 
ATOM   9604  C  CD  . ARG I  1 106 ? 60.304  59.341  -64.120 1.00 27.22 ? 79  ARG I CD  1 
ATOM   9605  N  NE  . ARG I  1 106 ? 59.062  59.966  -63.599 1.00 28.75 ? 79  ARG I NE  1 
ATOM   9606  C  CZ  . ARG I  1 106 ? 58.762  61.265  -63.672 1.00 28.67 ? 79  ARG I CZ  1 
ATOM   9607  N  NH1 . ARG I  1 106 ? 59.601  62.116  -64.240 1.00 27.73 ? 79  ARG I NH1 1 
ATOM   9608  N  NH2 . ARG I  1 106 ? 57.599  61.725  -63.160 1.00 27.35 ? 79  ARG I NH2 1 
ATOM   9609  N  N   . HIS I  1 107 ? 58.145  55.791  -61.596 1.00 25.74 ? 80  HIS I N   1 
ATOM   9610  C  CA  . HIS I  1 107 ? 56.699  55.940  -61.579 1.00 25.68 ? 80  HIS I CA  1 
ATOM   9611  C  C   . HIS I  1 107 ? 56.347  57.258  -62.268 1.00 24.27 ? 80  HIS I C   1 
ATOM   9612  O  O   . HIS I  1 107 ? 57.152  58.230  -62.241 1.00 23.09 ? 80  HIS I O   1 
ATOM   9613  C  CB  . HIS I  1 107 ? 56.214  55.919  -60.112 1.00 25.37 ? 80  HIS I CB  1 
ATOM   9614  C  CG  . HIS I  1 107 ? 56.598  54.689  -59.347 1.00 23.57 ? 80  HIS I CG  1 
ATOM   9615  N  ND1 . HIS I  1 107 ? 56.850  54.703  -57.997 1.00 23.98 ? 80  HIS I ND1 1 
ATOM   9616  C  CD2 . HIS I  1 107 ? 56.718  53.386  -59.731 1.00 23.70 ? 80  HIS I CD2 1 
ATOM   9617  C  CE1 . HIS I  1 107 ? 57.111  53.477  -57.571 1.00 25.06 ? 80  HIS I CE1 1 
ATOM   9618  N  NE2 . HIS I  1 107 ? 57.032  52.657  -58.612 1.00 24.68 ? 80  HIS I NE2 1 
ATOM   9619  N  N   . VAL I  1 108 ? 55.152  57.344  -62.872 1.00 22.58 ? 81  VAL I N   1 
ATOM   9620  C  CA  . VAL I  1 108 ? 54.670  58.608  -63.397 1.00 22.08 ? 81  VAL I CA  1 
ATOM   9621  C  C   . VAL I  1 108 ? 54.659  59.676  -62.268 1.00 23.05 ? 81  VAL I C   1 
ATOM   9622  O  O   . VAL I  1 108 ? 54.996  60.815  -62.512 1.00 24.76 ? 81  VAL I O   1 
ATOM   9623  C  CB  . VAL I  1 108 ? 53.251  58.500  -63.991 1.00 25.43 ? 81  VAL I CB  1 
ATOM   9624  C  CG1 . VAL I  1 108 ? 52.664  59.888  -64.239 1.00 24.41 ? 81  VAL I CG1 1 
ATOM   9625  C  CG2 . VAL I  1 108 ? 53.313  57.703  -65.322 1.00 25.74 ? 81  VAL I CG2 1 
ATOM   9626  N  N   . GLY I  1 109 ? 54.301  59.257  -61.054 1.00 24.36 ? 82  GLY I N   1 
ATOM   9627  C  CA  . GLY I  1 109 ? 54.248  60.187  -59.887 1.00 24.83 ? 82  GLY I CA  1 
ATOM   9628  C  C   . GLY I  1 109 ? 55.578  60.627  -59.276 1.00 26.06 ? 82  GLY I C   1 
ATOM   9629  O  O   . GLY I  1 109 ? 55.560  61.366  -58.276 1.00 23.97 ? 82  GLY I O   1 
ATOM   9630  N  N   . ASP I  1 110 ? 56.733  60.205  -59.835 1.00 25.35 ? 83  ASP I N   1 
ATOM   9631  C  CA  . ASP I  1 110 ? 58.031  60.424  -59.171 1.00 24.74 ? 83  ASP I CA  1 
ATOM   9632  C  C   . ASP I  1 110 ? 58.599  61.797  -59.510 1.00 26.99 ? 83  ASP I C   1 
ATOM   9633  O  O   . ASP I  1 110 ? 59.369  61.953  -60.484 1.00 25.69 ? 83  ASP I O   1 
ATOM   9634  C  CB  . ASP I  1 110 ? 59.046  59.308  -59.562 1.00 25.04 ? 83  ASP I CB  1 
ATOM   9635  C  CG  . ASP I  1 110 ? 58.712  57.991  -58.958 1.00 26.10 ? 83  ASP I CG  1 
ATOM   9636  O  OD1 . ASP I  1 110 ? 57.889  57.977  -58.012 1.00 23.94 ? 83  ASP I OD1 1 
ATOM   9637  O  OD2 . ASP I  1 110 ? 59.253  56.925  -59.394 1.00 24.24 ? 83  ASP I OD2 1 
ATOM   9638  N  N   . LEU I  1 111 ? 58.243  62.805  -58.700 1.00 23.30 ? 84  LEU I N   1 
ATOM   9639  C  CA  . LEU I  1 111 ? 58.710  64.138  -58.949 1.00 22.40 ? 84  LEU I CA  1 
ATOM   9640  C  C   . LEU I  1 111 ? 60.026  64.427  -58.223 1.00 22.52 ? 84  LEU I C   1 
ATOM   9641  O  O   . LEU I  1 111 ? 60.514  65.556  -58.272 1.00 28.78 ? 84  LEU I O   1 
ATOM   9642  C  CB  . LEU I  1 111 ? 57.625  65.195  -58.596 1.00 21.65 ? 84  LEU I CB  1 
ATOM   9643  C  CG  . LEU I  1 111 ? 56.360  65.134  -59.480 1.00 27.44 ? 84  LEU I CG  1 
ATOM   9644  C  CD1 . LEU I  1 111 ? 55.348  66.204  -59.060 1.00 24.88 ? 84  LEU I CD1 1 
ATOM   9645  C  CD2 . LEU I  1 111 ? 56.780  65.348  -60.941 1.00 28.33 ? 84  LEU I CD2 1 
ATOM   9646  N  N   . GLY I  1 112 ? 60.553  63.463  -57.499 1.00 20.80 ? 85  GLY I N   1 
ATOM   9647  C  CA  . GLY I  1 112 ? 61.868  63.633  -56.872 1.00 20.51 ? 85  GLY I CA  1 
ATOM   9648  C  C   . GLY I  1 112 ? 61.764  64.278  -55.486 1.00 22.58 ? 85  GLY I C   1 
ATOM   9649  O  O   . GLY I  1 112 ? 60.897  63.934  -54.695 1.00 22.27 ? 85  GLY I O   1 
ATOM   9650  N  N   . ASN I  1 113 ? 62.699  65.150  -55.169 1.00 21.03 ? 86  ASN I N   1 
ATOM   9651  C  CA  . ASN I  1 113 ? 62.687  65.829  -53.874 1.00 21.46 ? 86  ASN I CA  1 
ATOM   9652  C  C   . ASN I  1 113 ? 62.348  67.312  -54.030 1.00 22.47 ? 86  ASN I C   1 
ATOM   9653  O  O   . ASN I  1 113 ? 62.581  67.923  -55.097 1.00 22.14 ? 86  ASN I O   1 
ATOM   9654  C  CB  . ASN I  1 113 ? 64.058  65.758  -53.203 1.00 21.53 ? 86  ASN I CB  1 
ATOM   9655  C  CG  . ASN I  1 113 ? 64.358  64.397  -52.639 1.00 21.61 ? 86  ASN I CG  1 
ATOM   9656  O  OD1 . ASN I  1 113 ? 63.611  63.855  -51.801 1.00 22.18 ? 86  ASN I OD1 1 
ATOM   9657  N  ND2 . ASN I  1 113 ? 65.438  63.799  -53.151 1.00 23.00 ? 86  ASN I ND2 1 
ATOM   9658  N  N   . VAL I  1 114 ? 61.866  67.890  -52.940 1.00 21.21 ? 87  VAL I N   1 
ATOM   9659  C  CA  . VAL I  1 114 ? 61.882  69.362  -52.807 1.00 22.05 ? 87  VAL I CA  1 
ATOM   9660  C  C   . VAL I  1 114 ? 62.741  69.724  -51.599 1.00 24.16 ? 87  VAL I C   1 
ATOM   9661  O  O   . VAL I  1 114 ? 62.923  68.890  -50.706 1.00 25.75 ? 87  VAL I O   1 
ATOM   9662  C  CB  . VAL I  1 114 ? 60.449  69.923  -52.695 1.00 21.91 ? 87  VAL I CB  1 
ATOM   9663  C  CG1 . VAL I  1 114 ? 59.676  69.639  -53.979 1.00 20.92 ? 87  VAL I CG1 1 
ATOM   9664  C  CG2 . VAL I  1 114 ? 59.691  69.339  -51.511 1.00 21.73 ? 87  VAL I CG2 1 
ATOM   9665  N  N   . THR I  1 115 ? 63.260  70.952  -51.547 1.00 21.49 ? 88  THR I N   1 
ATOM   9666  C  CA  . THR I  1 115 ? 64.221  71.294  -50.499 1.00 23.95 ? 88  THR I CA  1 
ATOM   9667  C  C   . THR I  1 115 ? 63.675  72.462  -49.685 1.00 23.88 ? 88  THR I C   1 
ATOM   9668  O  O   . THR I  1 115 ? 63.298  73.495  -50.272 1.00 21.48 ? 88  THR I O   1 
ATOM   9669  C  CB  . THR I  1 115 ? 65.594  71.726  -51.111 1.00 25.20 ? 88  THR I CB  1 
ATOM   9670  O  OG1 . THR I  1 115 ? 66.184  70.630  -51.818 1.00 27.81 ? 88  THR I OG1 1 
ATOM   9671  C  CG2 . THR I  1 115 ? 66.588  72.196  -50.042 1.00 27.38 ? 88  THR I CG2 1 
ATOM   9672  N  N   . ALA I  1 116 ? 63.645  72.278  -48.358 1.00 24.60 ? 89  ALA I N   1 
ATOM   9673  C  CA  . ALA I  1 116 ? 63.246  73.313  -47.445 1.00 25.09 ? 89  ALA I CA  1 
ATOM   9674  C  C   . ALA I  1 116 ? 64.505  74.020  -46.951 1.00 27.17 ? 89  ALA I C   1 
ATOM   9675  O  O   . ALA I  1 116 ? 65.561  73.396  -46.632 1.00 26.35 ? 89  ALA I O   1 
ATOM   9676  C  CB  . ALA I  1 116 ? 62.456  72.740  -46.258 1.00 23.68 ? 89  ALA I CB  1 
ATOM   9677  N  N   . ASP I  1 117 ? 64.369  75.323  -46.850 1.00 26.12 ? 90  ASP I N   1 
ATOM   9678  C  CA  . ASP I  1 117 ? 65.454  76.153  -46.337 1.00 29.32 ? 90  ASP I CA  1 
ATOM   9679  C  C   . ASP I  1 117 ? 65.505  76.101  -44.811 1.00 30.37 ? 90  ASP I C   1 
ATOM   9680  O  O   . ASP I  1 117 ? 64.750  75.347  -44.178 1.00 25.78 ? 90  ASP I O   1 
ATOM   9681  C  CB  . ASP I  1 117 ? 65.316  77.570  -46.890 1.00 29.88 ? 90  ASP I CB  1 
ATOM   9682  C  CG  . ASP I  1 117 ? 64.059  78.308  -46.366 1.00 32.42 ? 90  ASP I CG  1 
ATOM   9683  O  OD1 . ASP I  1 117 ? 63.492  77.950  -45.322 1.00 27.60 ? 90  ASP I OD1 1 
ATOM   9684  O  OD2 . ASP I  1 117 ? 63.628  79.278  -47.026 1.00 31.84 ? 90  ASP I OD2 1 
ATOM   9685  N  N   . LYS I  1 118 ? 66.384  76.913  -44.206 1.00 33.71 ? 91  LYS I N   1 
ATOM   9686  C  CA  . LYS I  1 118 ? 66.580  76.876  -42.745 1.00 33.09 ? 91  LYS I CA  1 
ATOM   9687  C  C   . LYS I  1 118 ? 65.370  77.370  -41.961 1.00 34.40 ? 91  LYS I C   1 
ATOM   9688  O  O   . LYS I  1 118 ? 65.255  77.063  -40.791 1.00 32.06 ? 91  LYS I O   1 
ATOM   9689  C  CB  . LYS I  1 118 ? 67.828  77.684  -42.331 1.00 36.69 ? 91  LYS I CB  1 
ATOM   9690  C  CG  . LYS I  1 118 ? 67.636  79.174  -42.486 1.00 42.12 ? 91  LYS I CG  1 
ATOM   9691  C  CD  . LYS I  1 118 ? 68.809  79.970  -41.913 1.00 53.80 ? 91  LYS I CD  1 
ATOM   9692  C  CE  . LYS I  1 118 ? 68.429  81.442  -41.766 1.00 54.39 ? 91  LYS I CE  1 
ATOM   9693  N  NZ  . LYS I  1 118 ? 68.158  82.018  -43.115 1.00 61.35 ? 91  LYS I NZ  1 
ATOM   9694  N  N   . ASP I  1 119 ? 64.480  78.137  -42.606 1.00 32.34 ? 92  ASP I N   1 
ATOM   9695  C  CA  . ASP I  1 119 ? 63.192  78.498  -42.003 1.00 35.17 ? 92  ASP I CA  1 
ATOM   9696  C  C   . ASP I  1 119 ? 62.079  77.498  -42.237 1.00 31.97 ? 92  ASP I C   1 
ATOM   9697  O  O   . ASP I  1 119 ? 60.927  77.811  -41.931 1.00 29.84 ? 92  ASP I O   1 
ATOM   9698  C  CB  . ASP I  1 119 ? 62.721  79.845  -42.546 1.00 37.49 ? 92  ASP I CB  1 
ATOM   9699  C  CG  . ASP I  1 119 ? 63.707  80.948  -42.253 1.00 47.22 ? 92  ASP I CG  1 
ATOM   9700  O  OD1 . ASP I  1 119 ? 64.388  80.879  -41.184 1.00 42.12 ? 92  ASP I OD1 1 
ATOM   9701  O  OD2 . ASP I  1 119 ? 63.825  81.855  -43.114 1.00 50.55 ? 92  ASP I OD2 1 
ATOM   9702  N  N   . GLY I  1 120 ? 62.391  76.323  -42.801 1.00 26.99 ? 93  GLY I N   1 
ATOM   9703  C  CA  . GLY I  1 120 ? 61.365  75.308  -42.996 1.00 23.91 ? 93  GLY I CA  1 
ATOM   9704  C  C   . GLY I  1 120 ? 60.495  75.526  -44.243 1.00 23.28 ? 93  GLY I C   1 
ATOM   9705  O  O   . GLY I  1 120 ? 59.450  74.916  -44.390 1.00 23.08 ? 93  GLY I O   1 
ATOM   9706  N  N   . VAL I  1 121 ? 60.939  76.358  -45.179 1.00 23.67 ? 94  VAL I N   1 
ATOM   9707  C  CA  . VAL I  1 121 ? 60.109  76.653  -46.342 1.00 24.34 ? 94  VAL I CA  1 
ATOM   9708  C  C   . VAL I  1 121 ? 60.744  76.066  -47.595 1.00 23.72 ? 94  VAL I C   1 
ATOM   9709  O  O   . VAL I  1 121 ? 61.927  76.326  -47.876 1.00 24.74 ? 94  VAL I O   1 
ATOM   9710  C  CB  . VAL I  1 121 ? 59.972  78.197  -46.556 1.00 24.96 ? 94  VAL I CB  1 
ATOM   9711  C  CG1 . VAL I  1 121 ? 59.350  78.526  -47.920 1.00 25.16 ? 94  VAL I CG1 1 
ATOM   9712  C  CG2 . VAL I  1 121 ? 59.099  78.789  -45.447 1.00 26.23 ? 94  VAL I CG2 1 
ATOM   9713  N  N   . ALA I  1 122 ? 59.956  75.320  -48.348 1.00 24.06 ? 95  ALA I N   1 
ATOM   9714  C  CA  . ALA I  1 122 ? 60.375  74.811  -49.660 1.00 22.40 ? 95  ALA I CA  1 
ATOM   9715  C  C   . ALA I  1 122 ? 59.718  75.671  -50.685 1.00 22.09 ? 95  ALA I C   1 
ATOM   9716  O  O   . ALA I  1 122 ? 58.474  75.652  -50.813 1.00 25.11 ? 95  ALA I O   1 
ATOM   9717  C  CB  . ALA I  1 122 ? 59.885  73.379  -49.859 1.00 24.61 ? 95  ALA I CB  1 
ATOM   9718  N  N   . ASP I  1 123 ? 60.513  76.445  -51.414 1.00 24.91 ? 96  ASP I N   1 
ATOM   9719  C  CA  . ASP I  1 123 ? 59.952  77.190  -52.552 1.00 25.17 ? 96  ASP I CA  1 
ATOM   9720  C  C   . ASP I  1 123 ? 60.081  76.325  -53.780 1.00 22.28 ? 96  ASP I C   1 
ATOM   9721  O  O   . ASP I  1 123 ? 61.095  76.342  -54.473 1.00 23.66 ? 96  ASP I O   1 
ATOM   9722  C  CB  . ASP I  1 123 ? 60.620  78.544  -52.717 1.00 26.29 ? 96  ASP I CB  1 
ATOM   9723  C  CG  . ASP I  1 123 ? 60.215  79.521  -51.580 1.00 35.73 ? 96  ASP I CG  1 
ATOM   9724  O  OD1 . ASP I  1 123 ? 58.994  79.623  -51.253 1.00 32.25 ? 96  ASP I OD1 1 
ATOM   9725  O  OD2 . ASP I  1 123 ? 61.137  80.171  -51.028 1.00 38.27 ? 96  ASP I OD2 1 
ATOM   9726  N  N   . VAL I  1 124 ? 59.026  75.562  -54.037 1.00 22.54 ? 97  VAL I N   1 
ATOM   9727  C  CA  . VAL I  1 124 ? 59.096  74.491  -55.033 1.00 23.65 ? 97  VAL I CA  1 
ATOM   9728  C  C   . VAL I  1 124 ? 59.145  75.059  -56.438 1.00 26.55 ? 97  VAL I C   1 
ATOM   9729  O  O   . VAL I  1 124 ? 58.326  75.933  -56.781 1.00 24.52 ? 97  VAL I O   1 
ATOM   9730  C  CB  . VAL I  1 124 ? 57.855  73.610  -54.919 1.00 24.96 ? 97  VAL I CB  1 
ATOM   9731  C  CG1 . VAL I  1 124 ? 57.858  72.520  -55.992 1.00 23.59 ? 97  VAL I CG1 1 
ATOM   9732  C  CG2 . VAL I  1 124 ? 57.795  73.009  -53.526 1.00 21.60 ? 97  VAL I CG2 1 
ATOM   9733  N  N   . SER I  1 125 ? 60.033  74.503  -57.268 1.00 26.78 ? 98  SER I N   1 
ATOM   9734  C  CA  . SER I  1 125 ? 60.139  74.918  -58.666 1.00 29.75 ? 98  SER I CA  1 
ATOM   9735  C  C   . SER I  1 125 ? 60.646  73.738  -59.474 1.00 29.67 ? 98  SER I C   1 
ATOM   9736  O  O   . SER I  1 125 ? 61.810  73.392  -59.416 1.00 28.22 ? 98  SER I O   1 
ATOM   9737  C  CB  . SER I  1 125 ? 61.095  76.105  -58.780 1.00 35.43 ? 98  SER I CB  1 
ATOM   9738  O  OG  . SER I  1 125 ? 61.158  76.558  -60.112 1.00 42.54 ? 98  SER I OG  1 
ATOM   9739  N  N   . ILE I  1 126 ? 59.738  73.090  -60.173 1.00 28.39 ? 99  ILE I N   1 
ATOM   9740  C  CA  . ILE I  1 126 ? 60.020  71.821  -60.830 1.00 29.17 ? 99  ILE I CA  1 
ATOM   9741  C  C   . ILE I  1 126 ? 59.416  71.897  -62.216 1.00 28.61 ? 99  ILE I C   1 
ATOM   9742  O  O   . ILE I  1 126 ? 58.368  72.526  -62.413 1.00 28.98 ? 99  ILE I O   1 
ATOM   9743  C  CB  . ILE I  1 126 ? 59.385  70.673  -60.010 1.00 29.62 ? 99  ILE I CB  1 
ATOM   9744  C  CG1 . ILE I  1 126 ? 60.348  70.281  -58.889 1.00 30.79 ? 99  ILE I CG1 1 
ATOM   9745  C  CG2 . ILE I  1 126 ? 59.101  69.417  -60.830 1.00 33.18 ? 99  ILE I CG2 1 
ATOM   9746  C  CD1 . ILE I  1 126 ? 59.675  69.351  -57.890 1.00 34.19 ? 99  ILE I CD1 1 
ATOM   9747  N  N   . GLU I  1 127 ? 60.087  71.291  -63.187 1.00 25.91 ? 100 GLU I N   1 
ATOM   9748  C  CA  . GLU I  1 127 ? 59.467  71.126  -64.476 1.00 31.23 ? 100 GLU I CA  1 
ATOM   9749  C  C   . GLU I  1 127 ? 59.552  69.677  -64.824 1.00 28.90 ? 100 GLU I C   1 
ATOM   9750  O  O   . GLU I  1 127 ? 60.625  69.082  -64.750 1.00 31.79 ? 100 GLU I O   1 
ATOM   9751  C  CB  . GLU I  1 127 ? 60.177  71.947  -65.514 1.00 35.27 ? 100 GLU I CB  1 
ATOM   9752  C  CG  . GLU I  1 127 ? 59.453  71.933  -66.839 1.00 45.04 ? 100 GLU I CG  1 
ATOM   9753  C  CD  . GLU I  1 127 ? 60.240  72.719  -67.874 1.00 54.83 ? 100 GLU I CD  1 
ATOM   9754  O  OE1 . GLU I  1 127 ? 60.160  73.969  -67.828 1.00 50.29 ? 100 GLU I OE1 1 
ATOM   9755  O  OE2 . GLU I  1 127 ? 60.955  72.078  -68.687 1.00 56.96 ? 100 GLU I OE2 1 
ATOM   9756  N  N   . ASP I  1 128 ? 58.414  69.088  -65.148 1.00 28.18 ? 101 ASP I N   1 
ATOM   9757  C  CA  . ASP I  1 128 ? 58.393  67.663  -65.369 1.00 29.22 ? 101 ASP I CA  1 
ATOM   9758  C  C   . ASP I  1 128 ? 57.660  67.317  -66.634 1.00 30.90 ? 101 ASP I C   1 
ATOM   9759  O  O   . ASP I  1 128 ? 56.594  67.879  -66.925 1.00 33.11 ? 101 ASP I O   1 
ATOM   9760  C  CB  . ASP I  1 128 ? 57.749  66.893  -64.213 1.00 29.63 ? 101 ASP I CB  1 
ATOM   9761  C  CG  . ASP I  1 128 ? 58.069  65.380  -64.292 1.00 32.08 ? 101 ASP I CG  1 
ATOM   9762  O  OD1 . ASP I  1 128 ? 59.229  65.006  -64.013 1.00 35.62 ? 101 ASP I OD1 1 
ATOM   9763  O  OD2 . ASP I  1 128 ? 57.189  64.565  -64.673 1.00 32.10 ? 101 ASP I OD2 1 
ATOM   9764  N  N   . SER I  1 129 ? 58.219  66.352  -67.365 1.00 34.55 ? 102 SER I N   1 
ATOM   9765  C  CA  . SER I  1 129 ? 57.692  65.979  -68.664 1.00 38.07 ? 102 SER I CA  1 
ATOM   9766  C  C   . SER I  1 129 ? 56.922  64.687  -68.694 1.00 34.77 ? 102 SER I C   1 
ATOM   9767  O  O   . SER I  1 129 ? 56.358  64.346  -69.721 1.00 37.25 ? 102 SER I O   1 
ATOM   9768  C  CB  . SER I  1 129 ? 58.815  65.978  -69.716 1.00 44.73 ? 102 SER I CB  1 
ATOM   9769  O  OG  . SER I  1 129 ? 59.000  67.330  -70.144 1.00 50.98 ? 102 SER I OG  1 
ATOM   9770  N  N   . VAL I  1 130 ? 56.874  63.981  -67.573 1.00 29.99 ? 103 VAL I N   1 
ATOM   9771  C  CA  . VAL I  1 130 ? 56.215  62.685  -67.509 1.00 28.46 ? 103 VAL I CA  1 
ATOM   9772  C  C   . VAL I  1 130 ? 54.778  62.768  -66.953 1.00 31.28 ? 103 VAL I C   1 
ATOM   9773  O  O   . VAL I  1 130 ? 53.853  62.115  -67.459 1.00 31.47 ? 103 VAL I O   1 
ATOM   9774  C  CB  . VAL I  1 130 ? 57.085  61.681  -66.739 1.00 27.78 ? 103 VAL I CB  1 
ATOM   9775  C  CG1 . VAL I  1 130 ? 56.338  60.358  -66.526 1.00 26.13 ? 103 VAL I CG1 1 
ATOM   9776  C  CG2 . VAL I  1 130 ? 58.387  61.422  -67.513 1.00 28.99 ? 103 VAL I CG2 1 
ATOM   9777  N  N   . ILE I  1 131 ? 54.569  63.566  -65.897 1.00 25.73 ? 104 ILE I N   1 
ATOM   9778  C  CA  . ILE I  1 131 ? 53.170  63.828  -65.460 1.00 25.42 ? 104 ILE I CA  1 
ATOM   9779  C  C   . ILE I  1 131 ? 52.512  64.698  -66.534 1.00 27.73 ? 104 ILE I C   1 
ATOM   9780  O  O   . ILE I  1 131 ? 53.220  65.383  -67.319 1.00 30.16 ? 104 ILE I O   1 
ATOM   9781  C  CB  . ILE I  1 131 ? 53.116  64.601  -64.097 1.00 24.51 ? 104 ILE I CB  1 
ATOM   9782  C  CG1 . ILE I  1 131 ? 53.926  65.910  -64.157 1.00 23.97 ? 104 ILE I CG1 1 
ATOM   9783  C  CG2 . ILE I  1 131 ? 53.625  63.724  -62.999 1.00 26.48 ? 104 ILE I CG2 1 
ATOM   9784  C  CD1 . ILE I  1 131 ? 53.707  66.929  -63.016 1.00 20.94 ? 104 ILE I CD1 1 
ATOM   9785  N  N   . SER I  1 132 ? 51.184  64.680  -66.544 1.00 25.90 ? 105 SER I N   1 
ATOM   9786  C  CA  . SER I  1 132 ? 50.395  65.494  -67.420 1.00 28.45 ? 105 SER I CA  1 
ATOM   9787  C  C   . SER I  1 132 ? 49.096  65.906  -66.697 1.00 29.99 ? 105 SER I C   1 
ATOM   9788  O  O   . SER I  1 132 ? 48.679  65.241  -65.723 1.00 29.63 ? 105 SER I O   1 
ATOM   9789  C  CB  . SER I  1 132 ? 50.104  64.663  -68.697 1.00 29.63 ? 105 SER I CB  1 
ATOM   9790  O  OG  . SER I  1 132 ? 49.433  65.469  -69.645 1.00 29.42 ? 105 SER I OG  1 
ATOM   9791  N  N   . LEU I  1 133 ? 48.490  66.998  -67.167 1.00 29.95 ? 106 LEU I N   1 
ATOM   9792  C  CA  . LEU I  1 133 ? 47.155  67.481  -66.752 1.00 30.34 ? 106 LEU I CA  1 
ATOM   9793  C  C   . LEU I  1 133 ? 46.032  67.050  -67.689 1.00 38.29 ? 106 LEU I C   1 
ATOM   9794  O  O   . LEU I  1 133 ? 44.937  67.598  -67.648 1.00 40.05 ? 106 LEU I O   1 
ATOM   9795  C  CB  . LEU I  1 133 ? 47.159  68.996  -66.673 1.00 27.76 ? 106 LEU I CB  1 
ATOM   9796  C  CG  . LEU I  1 133 ? 48.252  69.586  -65.771 1.00 26.98 ? 106 LEU I CG  1 
ATOM   9797  C  CD1 . LEU I  1 133 ? 48.066  71.087  -65.575 1.00 29.63 ? 106 LEU I CD1 1 
ATOM   9798  C  CD2 . LEU I  1 133 ? 48.348  68.871  -64.410 1.00 26.08 ? 106 LEU I CD2 1 
ATOM   9799  N  N   . SER I  1 134 ? 46.328  66.117  -68.582 1.00 40.19 ? 107 SER I N   1 
ATOM   9800  C  CA  . SER I  1 134 ? 45.302  65.487  -69.418 1.00 43.38 ? 107 SER I CA  1 
ATOM   9801  C  C   . SER I  1 134 ? 45.927  64.234  -69.987 1.00 44.65 ? 107 SER I C   1 
ATOM   9802  O  O   . SER I  1 134 ? 47.131  63.972  -69.788 1.00 43.22 ? 107 SER I O   1 
ATOM   9803  C  CB  . SER I  1 134 ? 44.739  66.437  -70.505 1.00 41.77 ? 107 SER I CB  1 
ATOM   9804  O  OG  . SER I  1 134 ? 45.756  66.995  -71.343 1.00 43.36 ? 107 SER I OG  1 
ATOM   9805  N  N   . GLY I  1 135 ? 45.112  63.414  -70.633 1.00 44.76 ? 108 GLY I N   1 
ATOM   9806  C  CA  . GLY I  1 135 ? 45.631  62.198  -71.225 1.00 45.33 ? 108 GLY I CA  1 
ATOM   9807  C  C   . GLY I  1 135 ? 45.737  61.095  -70.204 1.00 49.61 ? 108 GLY I C   1 
ATOM   9808  O  O   . GLY I  1 135 ? 45.211  61.225  -69.100 1.00 46.45 ? 108 GLY I O   1 
ATOM   9809  N  N   . ASP I  1 136 ? 46.423  60.012  -70.582 1.00 46.77 ? 109 ASP I N   1 
ATOM   9810  C  CA  . ASP I  1 136 ? 46.597  58.809  -69.747 1.00 46.30 ? 109 ASP I CA  1 
ATOM   9811  C  C   . ASP I  1 136 ? 47.478  58.968  -68.515 1.00 44.18 ? 109 ASP I C   1 
ATOM   9812  O  O   . ASP I  1 136 ? 47.365  58.200  -67.550 1.00 45.14 ? 109 ASP I O   1 
ATOM   9813  C  CB  . ASP I  1 136 ? 47.163  57.670  -70.590 1.00 55.32 ? 109 ASP I CB  1 
ATOM   9814  C  CG  . ASP I  1 136 ? 46.082  56.953  -71.405 1.00 64.45 ? 109 ASP I CG  1 
ATOM   9815  O  OD1 . ASP I  1 136 ? 46.059  55.698  -71.402 1.00 68.67 ? 109 ASP I OD1 1 
ATOM   9816  O  OD2 . ASP I  1 136 ? 45.234  57.639  -72.022 1.00 66.54 ? 109 ASP I OD2 1 
ATOM   9817  N  N   . HIS I  1 137 ? 48.386  59.929  -68.550 1.00 39.66 ? 110 HIS I N   1 
ATOM   9818  C  CA  . HIS I  1 137 ? 49.211  60.189  -67.333 1.00 42.28 ? 110 HIS I CA  1 
ATOM   9819  C  C   . HIS I  1 137 ? 48.667  61.364  -66.515 1.00 36.38 ? 110 HIS I C   1 
ATOM   9820  O  O   . HIS I  1 137 ? 49.433  62.069  -65.833 1.00 37.74 ? 110 HIS I O   1 
ATOM   9821  C  CB  . HIS I  1 137 ? 50.673  60.459  -67.701 1.00 41.07 ? 110 HIS I CB  1 
ATOM   9822  C  CG  . HIS I  1 137 ? 51.341  59.303  -68.380 1.00 45.40 ? 110 HIS I CG  1 
ATOM   9823  N  ND1 . HIS I  1 137 ? 52.621  59.384  -68.893 1.00 46.79 ? 110 HIS I ND1 1 
ATOM   9824  C  CD2 . HIS I  1 137 ? 50.908  58.039  -68.625 1.00 45.46 ? 110 HIS I CD2 1 
ATOM   9825  C  CE1 . HIS I  1 137 ? 52.953  58.216  -69.416 1.00 46.75 ? 110 HIS I CE1 1 
ATOM   9826  N  NE2 . HIS I  1 137 ? 51.936  57.382  -69.259 1.00 50.77 ? 110 HIS I NE2 1 
ATOM   9827  N  N   . CYS I  1 138 ? 47.359  61.589  -66.638 1.00 34.86 ? 111 CYS I N   1 
ATOM   9828  C  CA  . CYS I  1 138 ? 46.699  62.744  -66.069 1.00 34.16 ? 111 CYS I CA  1 
ATOM   9829  C  C   . CYS I  1 138 ? 46.765  62.614  -64.529 1.00 27.49 ? 111 CYS I C   1 
ATOM   9830  O  O   . CYS I  1 138 ? 46.507  61.533  -63.969 1.00 30.52 ? 111 CYS I O   1 
ATOM   9831  C  CB  . CYS I  1 138 ? 45.251  62.730  -66.500 1.00 37.75 ? 111 CYS I CB  1 
ATOM   9832  S  SG  . CYS I  1 138 ? 44.360  64.100  -65.815 1.00 41.05 ? 111 CYS I SG  1 
ATOM   9833  N  N   . ILE I  1 139 ? 47.147  63.701  -63.860 1.00 28.55 ? 112 ILE I N   1 
ATOM   9834  C  CA  . ILE I  1 139 ? 47.245  63.665  -62.376 1.00 29.04 ? 112 ILE I CA  1 
ATOM   9835  C  C   . ILE I  1 139 ? 46.122  64.395  -61.654 1.00 30.05 ? 112 ILE I C   1 
ATOM   9836  O  O   . ILE I  1 139 ? 46.111  64.409  -60.426 1.00 27.92 ? 112 ILE I O   1 
ATOM   9837  C  CB  . ILE I  1 139 ? 48.589  64.181  -61.860 1.00 27.01 ? 112 ILE I CB  1 
ATOM   9838  C  CG1 . ILE I  1 139 ? 48.774  65.666  -62.257 1.00 24.85 ? 112 ILE I CG1 1 
ATOM   9839  C  CG2 . ILE I  1 139 ? 49.699  63.273  -62.368 1.00 25.71 ? 112 ILE I CG2 1 
ATOM   9840  C  CD1 . ILE I  1 139 ? 50.036  66.284  -61.675 1.00 25.24 ? 112 ILE I CD1 1 
ATOM   9841  N  N   . ILE I  1 140 ? 45.202  65.019  -62.402 1.00 29.35 ? 113 ILE I N   1 
ATOM   9842  C  CA  . ILE I  1 140 ? 44.013  65.654  -61.807 1.00 29.68 ? 113 ILE I CA  1 
ATOM   9843  C  C   . ILE I  1 140 ? 43.172  64.590  -61.097 1.00 32.11 ? 113 ILE I C   1 
ATOM   9844  O  O   . ILE I  1 140 ? 42.947  63.520  -61.656 1.00 29.76 ? 113 ILE I O   1 
ATOM   9845  C  CB  . ILE I  1 140 ? 43.137  66.323  -62.901 1.00 32.87 ? 113 ILE I CB  1 
ATOM   9846  C  CG1 . ILE I  1 140 ? 43.950  67.295  -63.764 1.00 32.92 ? 113 ILE I CG1 1 
ATOM   9847  C  CG2 . ILE I  1 140 ? 41.902  67.000  -62.320 1.00 27.25 ? 113 ILE I CG2 1 
ATOM   9848  C  CD1 . ILE I  1 140 ? 44.218  68.668  -63.228 1.00 38.41 ? 113 ILE I CD1 1 
ATOM   9849  N  N   . GLY I  1 141 ? 42.702  64.856  -59.868 1.00 29.66 ? 114 GLY I N   1 
ATOM   9850  C  CA  . GLY I  1 141 ? 41.925  63.840  -59.116 1.00 25.49 ? 114 GLY I CA  1 
ATOM   9851  C  C   . GLY I  1 141 ? 42.764  62.824  -58.360 1.00 25.38 ? 114 GLY I C   1 
ATOM   9852  O  O   . GLY I  1 141 ? 42.251  61.877  -57.716 1.00 27.51 ? 114 GLY I O   1 
ATOM   9853  N  N   . ARG I  1 142 ? 44.081  62.995  -58.426 1.00 26.43 ? 115 ARG I N   1 
ATOM   9854  C  CA  . ARG I  1 142 ? 44.995  62.134  -57.657 1.00 25.84 ? 115 ARG I CA  1 
ATOM   9855  C  C   . ARG I  1 142 ? 45.595  62.971  -56.503 1.00 24.43 ? 115 ARG I C   1 
ATOM   9856  O  O   . ARG I  1 142 ? 45.231  64.113  -56.355 1.00 24.09 ? 115 ARG I O   1 
ATOM   9857  C  CB  . ARG I  1 142 ? 46.079  61.555  -58.578 1.00 28.76 ? 115 ARG I CB  1 
ATOM   9858  C  CG  . ARG I  1 142 ? 45.426  60.846  -59.768 1.00 30.27 ? 115 ARG I CG  1 
ATOM   9859  C  CD  . ARG I  1 142 ? 46.354  59.841  -60.409 1.00 35.51 ? 115 ARG I CD  1 
ATOM   9860  N  NE  . ARG I  1 142 ? 45.719  59.250  -61.591 1.00 30.89 ? 115 ARG I NE  1 
ATOM   9861  C  CZ  . ARG I  1 142 ? 45.020  58.121  -61.606 1.00 31.45 ? 115 ARG I CZ  1 
ATOM   9862  N  NH1 . ARG I  1 142 ? 44.826  57.379  -60.524 1.00 29.34 ? 115 ARG I NH1 1 
ATOM   9863  N  NH2 . ARG I  1 142 ? 44.503  57.718  -62.755 1.00 34.42 ? 115 ARG I NH2 1 
ATOM   9864  N  N   . THR I  1 143 ? 46.495  62.408  -55.705 1.00 24.30 ? 116 THR I N   1 
ATOM   9865  C  CA  . THR I  1 143 ? 46.967  63.095  -54.487 1.00 22.77 ? 116 THR I CA  1 
ATOM   9866  C  C   . THR I  1 143 ? 48.439  63.475  -54.580 1.00 22.53 ? 116 THR I C   1 
ATOM   9867  O  O   . THR I  1 143 ? 49.282  62.596  -54.876 1.00 23.32 ? 116 THR I O   1 
ATOM   9868  C  CB  . THR I  1 143 ? 46.720  62.229  -53.240 1.00 23.24 ? 116 THR I CB  1 
ATOM   9869  O  OG1 . THR I  1 143 ? 45.291  62.048  -53.042 1.00 24.97 ? 116 THR I OG1 1 
ATOM   9870  C  CG2 . THR I  1 143 ? 47.308  62.895  -51.980 1.00 21.05 ? 116 THR I CG2 1 
ATOM   9871  N  N   . LEU I  1 144 ? 48.772  64.738  -54.281 1.00 20.67 ? 117 LEU I N   1 
ATOM   9872  C  CA  . LEU I  1 144 ? 50.145  65.139  -54.111 1.00 19.66 ? 117 LEU I CA  1 
ATOM   9873  C  C   . LEU I  1 144 ? 50.524  64.982  -52.632 1.00 21.25 ? 117 LEU I C   1 
ATOM   9874  O  O   . LEU I  1 144 ? 49.738  65.397  -51.760 1.00 19.82 ? 117 LEU I O   1 
ATOM   9875  C  CB  . LEU I  1 144 ? 50.310  66.618  -54.500 1.00 21.41 ? 117 LEU I CB  1 
ATOM   9876  C  CG  . LEU I  1 144 ? 51.775  67.119  -54.558 1.00 21.91 ? 117 LEU I CG  1 
ATOM   9877  C  CD1 . LEU I  1 144 ? 52.720  66.376  -55.557 1.00 20.80 ? 117 LEU I CD1 1 
ATOM   9878  C  CD2 . LEU I  1 144 ? 51.797  68.663  -54.744 1.00 22.36 ? 117 LEU I CD2 1 
ATOM   9879  N  N   . VAL I  1 145 ? 51.682  64.385  -52.355 1.00 20.31 ? 118 VAL I N   1 
ATOM   9880  C  CA  . VAL I  1 145 ? 52.170  64.156  -50.967 1.00 20.93 ? 118 VAL I CA  1 
ATOM   9881  C  C   . VAL I  1 145 ? 53.596  64.643  -50.792 1.00 20.97 ? 118 VAL I C   1 
ATOM   9882  O  O   . VAL I  1 145 ? 54.467  64.381  -51.637 1.00 21.33 ? 118 VAL I O   1 
ATOM   9883  C  CB  . VAL I  1 145 ? 52.196  62.657  -50.623 1.00 21.21 ? 118 VAL I CB  1 
ATOM   9884  C  CG1 . VAL I  1 145 ? 52.644  62.442  -49.175 1.00 22.57 ? 118 VAL I CG1 1 
ATOM   9885  C  CG2 . VAL I  1 145 ? 50.809  62.037  -50.817 1.00 21.58 ? 118 VAL I CG2 1 
ATOM   9886  N  N   . VAL I  1 146 ? 53.871  65.302  -49.667 1.00 18.57 ? 119 VAL I N   1 
ATOM   9887  C  CA  . VAL I  1 146 ? 55.205  65.678  -49.342 1.00 17.91 ? 119 VAL I CA  1 
ATOM   9888  C  C   . VAL I  1 146 ? 55.551  64.776  -48.175 1.00 19.08 ? 119 VAL I C   1 
ATOM   9889  O  O   . VAL I  1 146 ? 54.766  64.608  -47.236 1.00 18.49 ? 119 VAL I O   1 
ATOM   9890  C  CB  . VAL I  1 146 ? 55.418  67.186  -49.049 1.00 19.01 ? 119 VAL I CB  1 
ATOM   9891  C  CG1 . VAL I  1 146 ? 54.534  67.656  -47.895 1.00 17.93 ? 119 VAL I CG1 1 
ATOM   9892  C  CG2 . VAL I  1 146 ? 56.901  67.506  -48.751 1.00 18.82 ? 119 VAL I CG2 1 
ATOM   9893  N  N   . HIS I  1 147 ? 56.727  64.162  -48.285 1.00 19.45 ? 120 HIS I N   1 
ATOM   9894  C  CA  . HIS I  1 147 ? 57.146  63.134  -47.347 1.00 19.23 ? 120 HIS I CA  1 
ATOM   9895  C  C   . HIS I  1 147 ? 58.143  63.629  -46.287 1.00 18.84 ? 120 HIS I C   1 
ATOM   9896  O  O   . HIS I  1 147 ? 58.784  64.648  -46.408 1.00 20.58 ? 120 HIS I O   1 
ATOM   9897  C  CB  . HIS I  1 147 ? 57.757  61.926  -48.129 1.00 17.67 ? 120 HIS I CB  1 
ATOM   9898  C  CG  . HIS I  1 147 ? 56.739  61.124  -48.881 1.00 19.71 ? 120 HIS I CG  1 
ATOM   9899  N  ND1 . HIS I  1 147 ? 56.163  59.993  -48.362 1.00 22.53 ? 120 HIS I ND1 1 
ATOM   9900  C  CD2 . HIS I  1 147 ? 56.173  61.302  -50.095 1.00 19.78 ? 120 HIS I CD2 1 
ATOM   9901  C  CE1 . HIS I  1 147 ? 55.315  59.474  -49.235 1.00 19.76 ? 120 HIS I CE1 1 
ATOM   9902  N  NE2 . HIS I  1 147 ? 55.288  60.270  -50.284 1.00 20.83 ? 120 HIS I NE2 1 
ATOM   9903  N  N   . GLU I  1 148 ? 58.291  62.803  -45.261 1.00 21.34 ? 121 GLU I N   1 
ATOM   9904  C  CA  . GLU I  1 148 ? 59.111  63.066  -44.103 1.00 23.04 ? 121 GLU I CA  1 
ATOM   9905  C  C   . GLU I  1 148 ? 60.606  63.225  -44.425 1.00 24.58 ? 121 GLU I C   1 
ATOM   9906  O  O   . GLU I  1 148 ? 61.300  64.088  -43.824 1.00 22.77 ? 121 GLU I O   1 
ATOM   9907  C  CB  . GLU I  1 148 ? 58.836  61.881  -43.128 1.00 23.90 ? 121 GLU I CB  1 
ATOM   9908  C  CG  . GLU I  1 148 ? 59.765  61.764  -41.942 1.00 32.69 ? 121 GLU I CG  1 
ATOM   9909  C  CD  . GLU I  1 148 ? 59.819  60.341  -41.336 1.00 37.05 ? 121 GLU I CD  1 
ATOM   9910  O  OE1 . GLU I  1 148 ? 60.422  60.250  -40.255 1.00 41.06 ? 121 GLU I OE1 1 
ATOM   9911  O  OE2 . GLU I  1 148 ? 59.295  59.311  -41.904 1.00 35.32 ? 121 GLU I OE2 1 
ATOM   9912  N  N   . LYS I  1 149 ? 61.131  62.369  -45.319 1.00 24.53 ? 122 LYS I N   1 
ATOM   9913  C  CA  . LYS I  1 149 ? 62.582  62.227  -45.542 1.00 26.71 ? 122 LYS I CA  1 
ATOM   9914  C  C   . LYS I  1 149 ? 62.935  62.354  -47.016 1.00 24.20 ? 122 LYS I C   1 
ATOM   9915  O  O   . LYS I  1 149 ? 62.022  62.378  -47.861 1.00 22.70 ? 122 LYS I O   1 
ATOM   9916  C  CB  . LYS I  1 149 ? 63.037  60.802  -45.117 1.00 30.61 ? 122 LYS I CB  1 
ATOM   9917  C  CG  . LYS I  1 149 ? 62.618  60.372  -43.725 1.00 38.73 ? 122 LYS I CG  1 
ATOM   9918  C  CD  . LYS I  1 149 ? 63.519  59.257  -43.236 1.00 45.23 ? 122 LYS I CD  1 
ATOM   9919  C  CE  . LYS I  1 149 ? 62.990  57.922  -43.712 1.00 50.76 ? 122 LYS I CE  1 
ATOM   9920  N  NZ  . LYS I  1 149 ? 64.116  57.102  -44.251 1.00 59.70 ? 122 LYS I NZ  1 
ATOM   9921  N  N   . ALA I  1 150 ? 64.240  62.398  -47.321 1.00 22.34 ? 123 ALA I N   1 
ATOM   9922  C  CA  . ALA I  1 150 ? 64.718  62.467  -48.707 1.00 23.63 ? 123 ALA I CA  1 
ATOM   9923  C  C   . ALA I  1 150 ? 64.259  61.211  -49.466 1.00 23.99 ? 123 ALA I C   1 
ATOM   9924  O  O   . ALA I  1 150 ? 64.224  60.118  -48.912 1.00 23.74 ? 123 ALA I O   1 
ATOM   9925  C  CB  . ALA I  1 150 ? 66.242  62.594  -48.764 1.00 23.28 ? 123 ALA I CB  1 
ATOM   9926  N  N   . ASP I  1 151 ? 63.833  61.414  -50.702 1.00 23.29 ? 124 ASP I N   1 
ATOM   9927  C  CA  . ASP I  1 151 ? 63.647  60.337  -51.658 1.00 24.47 ? 124 ASP I CA  1 
ATOM   9928  C  C   . ASP I  1 151 ? 65.049  59.921  -52.130 1.00 20.62 ? 124 ASP I C   1 
ATOM   9929  O  O   . ASP I  1 151 ? 65.833  60.777  -52.555 1.00 21.88 ? 124 ASP I O   1 
ATOM   9930  C  CB  . ASP I  1 151 ? 62.784  60.904  -52.814 1.00 24.16 ? 124 ASP I CB  1 
ATOM   9931  C  CG  . ASP I  1 151 ? 62.499  59.892  -53.918 1.00 29.45 ? 124 ASP I CG  1 
ATOM   9932  O  OD1 . ASP I  1 151 ? 63.124  58.801  -53.983 1.00 26.95 ? 124 ASP I OD1 1 
ATOM   9933  O  OD2 . ASP I  1 151 ? 61.628  60.200  -54.747 1.00 27.07 ? 124 ASP I OD2 1 
ATOM   9934  N  N   . ASP I  1 152 ? 65.401  58.630  -52.027 1.00 23.14 ? 125 ASP I N   1 
ATOM   9935  C  CA  . ASP I  1 152 ? 66.724  58.186  -52.538 1.00 25.64 ? 125 ASP I CA  1 
ATOM   9936  C  C   . ASP I  1 152 ? 66.753  57.954  -54.055 1.00 26.48 ? 125 ASP I C   1 
ATOM   9937  O  O   . ASP I  1 152 ? 67.765  57.488  -54.627 1.00 27.21 ? 125 ASP I O   1 
ATOM   9938  C  CB  . ASP I  1 152 ? 67.244  56.978  -51.740 1.00 25.54 ? 125 ASP I CB  1 
ATOM   9939  C  CG  . ASP I  1 152 ? 66.409  55.682  -51.955 1.00 24.31 ? 125 ASP I CG  1 
ATOM   9940  O  OD1 . ASP I  1 152 ? 65.613  55.539  -52.908 1.00 24.42 ? 125 ASP I OD1 1 
ATOM   9941  O  OD2 . ASP I  1 152 ? 66.593  54.747  -51.140 1.00 26.26 ? 125 ASP I OD2 1 
ATOM   9942  N  N   . LEU I  1 153 ? 65.629  58.244  -54.695 1.00 24.44 ? 126 LEU I N   1 
ATOM   9943  C  CA  . LEU I  1 153 ? 65.519  58.291  -56.165 1.00 24.83 ? 126 LEU I CA  1 
ATOM   9944  C  C   . LEU I  1 153 ? 65.656  56.872  -56.698 1.00 24.73 ? 126 LEU I C   1 
ATOM   9945  O  O   . LEU I  1 153 ? 66.040  56.661  -57.857 1.00 23.24 ? 126 LEU I O   1 
ATOM   9946  C  CB  . LEU I  1 153 ? 66.527  59.261  -56.808 1.00 25.09 ? 126 LEU I CB  1 
ATOM   9947  C  CG  . LEU I  1 153 ? 66.503  60.690  -56.231 1.00 26.06 ? 126 LEU I CG  1 
ATOM   9948  C  CD1 . LEU I  1 153 ? 67.465  61.521  -57.029 1.00 30.36 ? 126 LEU I CD1 1 
ATOM   9949  C  CD2 . LEU I  1 153 ? 65.085  61.295  -56.351 1.00 24.64 ? 126 LEU I CD2 1 
ATOM   9950  N  N   . GLY I  1 154 ? 65.273  55.904  -55.864 1.00 23.65 ? 127 GLY I N   1 
ATOM   9951  C  CA  . GLY I  1 154 ? 65.291  54.502  -56.293 1.00 24.10 ? 127 GLY I CA  1 
ATOM   9952  C  C   . GLY I  1 154 ? 66.718  53.933  -56.298 1.00 25.22 ? 127 GLY I C   1 
ATOM   9953  O  O   . GLY I  1 154 ? 66.940  52.858  -56.853 1.00 26.58 ? 127 GLY I O   1 
ATOM   9954  N  N   . LYS I  1 155 ? 67.690  54.618  -55.677 1.00 23.53 ? 128 LYS I N   1 
ATOM   9955  C  CA  . LYS I  1 155 ? 69.112  54.174  -55.718 1.00 23.96 ? 128 LYS I CA  1 
ATOM   9956  C  C   . LYS I  1 155 ? 69.591  53.497  -54.435 1.00 22.65 ? 128 LYS I C   1 
ATOM   9957  O  O   . LYS I  1 155 ? 70.789  53.361  -54.217 1.00 24.67 ? 128 LYS I O   1 
ATOM   9958  C  CB  . LYS I  1 155 ? 70.012  55.366  -56.062 1.00 27.52 ? 128 LYS I CB  1 
ATOM   9959  C  CG  . LYS I  1 155 ? 69.637  55.939  -57.422 1.00 29.23 ? 128 LYS I CG  1 
ATOM   9960  C  CD  . LYS I  1 155 ? 70.569  57.048  -57.847 1.00 39.05 ? 128 LYS I CD  1 
ATOM   9961  C  CE  . LYS I  1 155 ? 70.248  57.408  -59.294 1.00 44.94 ? 128 LYS I CE  1 
ATOM   9962  N  NZ  . LYS I  1 155 ? 71.135  58.517  -59.773 1.00 57.93 ? 128 LYS I NZ  1 
ATOM   9963  N  N   . GLY I  1 156 ? 68.659  53.144  -53.562 1.00 20.61 ? 129 GLY I N   1 
ATOM   9964  C  CA  . GLY I  1 156 ? 69.011  52.688  -52.233 1.00 21.55 ? 129 GLY I CA  1 
ATOM   9965  C  C   . GLY I  1 156 ? 69.264  51.154  -52.138 1.00 23.69 ? 129 GLY I C   1 
ATOM   9966  O  O   . GLY I  1 156 ? 69.694  50.683  -51.086 1.00 22.25 ? 129 GLY I O   1 
ATOM   9967  N  N   . GLY I  1 157 ? 68.921  50.396  -53.191 1.00 21.24 ? 130 GLY I N   1 
ATOM   9968  C  CA  . GLY I  1 157 ? 69.294  48.951  -53.309 1.00 22.54 ? 130 GLY I CA  1 
ATOM   9969  C  C   . GLY I  1 157 ? 68.535  48.030  -52.394 1.00 26.61 ? 130 GLY I C   1 
ATOM   9970  O  O   . GLY I  1 157 ? 68.837  46.846  -52.300 1.00 26.92 ? 130 GLY I O   1 
ATOM   9971  N  N   . ASN I  1 158 ? 67.527  48.558  -51.704 1.00 25.61 ? 131 ASN I N   1 
ATOM   9972  C  CA  . ASN I  1 158 ? 66.694  47.721  -50.895 1.00 24.79 ? 131 ASN I CA  1 
ATOM   9973  C  C   . ASN I  1 158 ? 65.305  47.725  -51.468 1.00 24.04 ? 131 ASN I C   1 
ATOM   9974  O  O   . ASN I  1 158 ? 64.990  48.477  -52.378 1.00 24.79 ? 131 ASN I O   1 
ATOM   9975  C  CB  . ASN I  1 158 ? 66.785  48.044  -49.378 1.00 26.16 ? 131 ASN I CB  1 
ATOM   9976  C  CG  . ASN I  1 158 ? 66.158  49.399  -49.004 1.00 28.59 ? 131 ASN I CG  1 
ATOM   9977  O  OD1 . ASN I  1 158 ? 65.795  50.171  -49.868 1.00 26.53 ? 131 ASN I OD1 1 
ATOM   9978  N  ND2 . ASN I  1 158 ? 66.044  49.667  -47.705 1.00 31.22 ? 131 ASN I ND2 1 
ATOM   9979  N  N   . GLU I  1 159 ? 64.460  46.841  -50.990 1.00 25.42 ? 132 GLU I N   1 
ATOM   9980  C  CA  . GLU I  1 159 ? 63.128  46.751  -51.563 1.00 25.11 ? 132 GLU I CA  1 
ATOM   9981  C  C   . GLU I  1 159 ? 62.307  48.060  -51.411 1.00 25.70 ? 132 GLU I C   1 
ATOM   9982  O  O   . GLU I  1 159 ? 61.515  48.451  -52.276 1.00 24.87 ? 132 GLU I O   1 
ATOM   9983  C  CB  . GLU I  1 159 ? 62.335  45.680  -50.825 1.00 34.39 ? 132 GLU I CB  1 
ATOM   9984  C  CG  . GLU I  1 159 ? 63.089  44.377  -50.613 1.00 41.73 ? 132 GLU I CG  1 
ATOM   9985  C  CD  . GLU I  1 159 ? 62.155  43.267  -50.114 1.00 58.27 ? 132 GLU I CD  1 
ATOM   9986  O  OE1 . GLU I  1 159 ? 60.899  43.479  -50.086 1.00 59.64 ? 132 GLU I OE1 1 
ATOM   9987  O  OE2 . GLU I  1 159 ? 62.679  42.189  -49.747 1.00 54.52 ? 132 GLU I OE2 1 
ATOM   9988  N  N   . GLU I  1 160 ? 62.465  48.682  -50.268 1.00 26.52 ? 133 GLU I N   1 
ATOM   9989  C  CA  . GLU I  1 160 ? 61.710  49.930  -49.989 1.00 27.08 ? 133 GLU I CA  1 
ATOM   9990  C  C   . GLU I  1 160 ? 62.122  51.032  -51.015 1.00 27.06 ? 133 GLU I C   1 
ATOM   9991  O  O   . GLU I  1 160 ? 61.279  51.790  -51.546 1.00 28.79 ? 133 GLU I O   1 
ATOM   9992  C  CB  . GLU I  1 160 ? 62.012  50.346  -48.558 1.00 29.95 ? 133 GLU I CB  1 
ATOM   9993  C  CG  . GLU I  1 160 ? 61.071  51.430  -48.052 1.00 35.42 ? 133 GLU I CG  1 
ATOM   9994  C  CD  . GLU I  1 160 ? 59.614  51.007  -48.182 1.00 36.60 ? 133 GLU I CD  1 
ATOM   9995  O  OE1 . GLU I  1 160 ? 59.210  50.005  -47.575 1.00 38.14 ? 133 GLU I OE1 1 
ATOM   9996  O  OE2 . GLU I  1 160 ? 58.863  51.681  -48.900 1.00 41.77 ? 133 GLU I OE2 1 
ATOM   9997  N  N   . SER I  1 161 ? 63.406  51.067  -51.371 1.00 26.18 ? 134 SER I N   1 
ATOM   9998  C  CA  . SER I  1 161 ? 63.859  52.052  -52.359 1.00 25.33 ? 134 SER I CA  1 
ATOM   9999  C  C   . SER I  1 161 ? 63.108  51.976  -53.671 1.00 26.18 ? 134 SER I C   1 
ATOM   10000 O  O   . SER I  1 161 ? 62.787  53.018  -54.298 1.00 26.53 ? 134 SER I O   1 
ATOM   10001 C  CB  . SER I  1 161 ? 65.349  51.965  -52.603 1.00 21.80 ? 134 SER I CB  1 
ATOM   10002 O  OG  . SER I  1 161 ? 65.710  52.914  -53.600 1.00 22.68 ? 134 SER I OG  1 
ATOM   10003 N  N   . THR I  1 162 ? 62.868  50.746  -54.125 1.00 25.99 ? 135 THR I N   1 
ATOM   10004 C  CA  . THR I  1 162 ? 62.223  50.507  -55.391 1.00 26.11 ? 135 THR I CA  1 
ATOM   10005 C  C   . THR I  1 162 ? 60.708  50.766  -55.389 1.00 24.79 ? 135 THR I C   1 
ATOM   10006 O  O   . THR I  1 162 ? 60.115  50.781  -56.440 1.00 26.71 ? 135 THR I O   1 
ATOM   10007 C  CB  . THR I  1 162 ? 62.401  49.019  -55.853 1.00 29.26 ? 135 THR I CB  1 
ATOM   10008 O  OG1 . THR I  1 162 ? 61.596  48.178  -55.016 1.00 32.21 ? 135 THR I OG1 1 
ATOM   10009 C  CG2 . THR I  1 162 ? 63.821  48.581  -55.734 1.00 29.61 ? 135 THR I CG2 1 
ATOM   10010 N  N   . LYS I  1 163 ? 60.114  50.966  -54.211 1.00 27.63 ? 136 LYS I N   1 
ATOM   10011 C  CA  . LYS I  1 163 ? 58.660  51.301  -54.087 1.00 28.13 ? 136 LYS I CA  1 
ATOM   10012 C  C   . LYS I  1 163 ? 58.441  52.781  -53.735 1.00 27.87 ? 136 LYS I C   1 
ATOM   10013 O  O   . LYS I  1 163 ? 57.641  53.470  -54.378 1.00 30.23 ? 136 LYS I O   1 
ATOM   10014 C  CB  . LYS I  1 163 ? 57.998  50.451  -52.990 1.00 27.93 ? 136 LYS I CB  1 
ATOM   10015 C  CG  . LYS I  1 163 ? 58.015  48.938  -53.183 1.00 37.16 ? 136 LYS I CG  1 
ATOM   10016 C  CD  . LYS I  1 163 ? 57.497  48.295  -51.883 1.00 45.66 ? 136 LYS I CD  1 
ATOM   10017 C  CE  . LYS I  1 163 ? 57.880  46.831  -51.658 1.00 54.40 ? 136 LYS I CE  1 
ATOM   10018 N  NZ  . LYS I  1 163 ? 56.757  45.842  -51.882 1.00 50.01 ? 136 LYS I NZ  1 
ATOM   10019 N  N   . THR I  1 164 ? 59.186  53.273  -52.739 1.00 29.08 ? 137 THR I N   1 
ATOM   10020 C  CA  . THR I  1 164 ? 58.931  54.638  -52.213 1.00 29.21 ? 137 THR I CA  1 
ATOM   10021 C  C   . THR I  1 164 ? 60.131  55.564  -52.125 1.00 29.03 ? 137 THR I C   1 
ATOM   10022 O  O   . THR I  1 164 ? 59.973  56.728  -51.698 1.00 26.82 ? 137 THR I O   1 
ATOM   10023 C  CB  . THR I  1 164 ? 58.359  54.557  -50.784 1.00 29.44 ? 137 THR I CB  1 
ATOM   10024 O  OG1 . THR I  1 164 ? 59.373  54.014  -49.927 1.00 28.94 ? 137 THR I OG1 1 
ATOM   10025 C  CG2 . THR I  1 164 ? 57.112  53.709  -50.759 1.00 29.69 ? 137 THR I CG2 1 
ATOM   10026 N  N   . GLY I  1 165 ? 61.330  55.090  -52.490 1.00 23.27 ? 138 GLY I N   1 
ATOM   10027 C  CA  . GLY I  1 165 ? 62.524  55.933  -52.379 1.00 21.69 ? 138 GLY I CA  1 
ATOM   10028 C  C   . GLY I  1 165 ? 62.959  56.088  -50.921 1.00 19.07 ? 138 GLY I C   1 
ATOM   10029 O  O   . GLY I  1 165 ? 63.828  56.900  -50.640 1.00 24.10 ? 138 GLY I O   1 
ATOM   10030 N  N   . ASN I  1 166 ? 62.404  55.268  -50.020 1.00 21.50 ? 139 ASN I N   1 
ATOM   10031 C  CA  . ASN I  1 166 ? 62.682  55.357  -48.583 1.00 21.53 ? 139 ASN I CA  1 
ATOM   10032 C  C   . ASN I  1 166 ? 62.329  56.782  -48.023 1.00 22.31 ? 139 ASN I C   1 
ATOM   10033 O  O   . ASN I  1 166 ? 63.020  57.267  -47.126 1.00 22.40 ? 139 ASN I O   1 
ATOM   10034 C  CB  . ASN I  1 166 ? 64.152  55.071  -48.285 1.00 23.34 ? 139 ASN I CB  1 
ATOM   10035 C  CG  . ASN I  1 166 ? 64.459  53.584  -48.335 1.00 28.23 ? 139 ASN I CG  1 
ATOM   10036 O  OD1 . ASN I  1 166 ? 63.884  52.839  -47.552 1.00 30.91 ? 139 ASN I OD1 1 
ATOM   10037 N  ND2 . ASN I  1 166 ? 65.306  53.145  -49.283 1.00 23.50 ? 139 ASN I ND2 1 
ATOM   10038 N  N   . ALA I  1 167 ? 61.303  57.414  -48.576 1.00 22.11 ? 140 ALA I N   1 
ATOM   10039 C  CA  . ALA I  1 167 ? 61.034  58.841  -48.220 1.00 25.11 ? 140 ALA I CA  1 
ATOM   10040 C  C   . ALA I  1 167 ? 60.185  58.935  -46.941 1.00 25.16 ? 140 ALA I C   1 
ATOM   10041 O  O   . ALA I  1 167 ? 59.881  60.044  -46.446 1.00 24.15 ? 140 ALA I O   1 
ATOM   10042 C  CB  . ALA I  1 167 ? 60.364  59.565  -49.381 1.00 23.38 ? 140 ALA I CB  1 
ATOM   10043 N  N   . GLY I  1 168 ? 59.821  57.775  -46.378 1.00 24.71 ? 141 GLY I N   1 
ATOM   10044 C  CA  . GLY I  1 168 ? 59.150  57.750  -45.083 1.00 25.05 ? 141 GLY I CA  1 
ATOM   10045 C  C   . GLY I  1 168 ? 57.723  58.310  -45.090 1.00 25.28 ? 141 GLY I C   1 
ATOM   10046 O  O   . GLY I  1 168 ? 57.001  58.281  -46.109 1.00 23.39 ? 141 GLY I O   1 
ATOM   10047 N  N   . SER I  1 169 ? 57.285  58.792  -43.933 1.00 24.26 ? 142 SER I N   1 
ATOM   10048 C  CA  . SER I  1 169 ? 55.847  59.046  -43.736 1.00 24.80 ? 142 SER I CA  1 
ATOM   10049 C  C   . SER I  1 169 ? 55.336  60.248  -44.569 1.00 24.23 ? 142 SER I C   1 
ATOM   10050 O  O   . SER I  1 169 ? 56.116  61.035  -45.113 1.00 22.45 ? 142 SER I O   1 
ATOM   10051 C  CB  . SER I  1 169 ? 55.540  59.277  -42.245 1.00 29.30 ? 142 SER I CB  1 
ATOM   10052 O  OG  . SER I  1 169 ? 56.098  60.528  -41.852 1.00 33.13 ? 142 SER I OG  1 
ATOM   10053 N  N   . ARG I  1 170 ? 54.022  60.395  -44.592 1.00 23.41 ? 143 ARG I N   1 
ATOM   10054 C  CA  . ARG I  1 170 ? 53.351  61.389  -45.438 1.00 22.76 ? 143 ARG I CA  1 
ATOM   10055 C  C   . ARG I  1 170 ? 53.023  62.555  -44.507 1.00 23.52 ? 143 ARG I C   1 
ATOM   10056 O  O   . ARG I  1 170 ? 52.207  62.394  -43.616 1.00 26.06 ? 143 ARG I O   1 
ATOM   10057 C  CB  . ARG I  1 170 ? 52.077  60.731  -45.954 1.00 22.08 ? 143 ARG I CB  1 
ATOM   10058 C  CG  . ARG I  1 170 ? 52.411  59.441  -46.737 1.00 23.63 ? 143 ARG I CG  1 
ATOM   10059 C  CD  . ARG I  1 170 ? 51.170  58.745  -47.268 1.00 23.26 ? 143 ARG I CD  1 
ATOM   10060 N  NE  . ARG I  1 170 ? 51.605  57.504  -47.910 1.00 28.16 ? 143 ARG I NE  1 
ATOM   10061 C  CZ  . ARG I  1 170 ? 50.954  56.802  -48.830 1.00 27.78 ? 143 ARG I CZ  1 
ATOM   10062 N  NH1 . ARG I  1 170 ? 49.753  57.158  -49.282 1.00 25.44 ? 143 ARG I NH1 1 
ATOM   10063 N  NH2 . ARG I  1 170 ? 51.544  55.706  -49.307 1.00 26.80 ? 143 ARG I NH2 1 
ATOM   10064 N  N   . LEU I  1 171 ? 53.726  63.659  -44.659 1.00 22.29 ? 144 LEU I N   1 
ATOM   10065 C  CA  . LEU I  1 171 ? 53.551  64.845  -43.793 1.00 22.45 ? 144 LEU I CA  1 
ATOM   10066 C  C   . LEU I  1 171 ? 52.356  65.692  -44.164 1.00 25.18 ? 144 LEU I C   1 
ATOM   10067 O  O   . LEU I  1 171 ? 51.673  66.219  -43.262 1.00 24.63 ? 144 LEU I O   1 
ATOM   10068 C  CB  . LEU I  1 171 ? 54.780  65.733  -43.840 1.00 22.06 ? 144 LEU I CB  1 
ATOM   10069 C  CG  . LEU I  1 171 ? 56.073  64.999  -43.423 1.00 25.23 ? 144 LEU I CG  1 
ATOM   10070 C  CD1 . LEU I  1 171 ? 57.217  65.987  -43.482 1.00 27.03 ? 144 LEU I CD1 1 
ATOM   10071 C  CD2 . LEU I  1 171 ? 55.922  64.404  -42.032 1.00 27.37 ? 144 LEU I CD2 1 
ATOM   10072 N  N   . ALA I  1 172 ? 52.112  65.900  -45.467 1.00 20.35 ? 145 ALA I N   1 
ATOM   10073 C  CA  . ALA I  1 172 ? 50.905  66.614  -45.885 1.00 21.76 ? 145 ALA I CA  1 
ATOM   10074 C  C   . ALA I  1 172 ? 50.534  66.179  -47.294 1.00 20.97 ? 145 ALA I C   1 
ATOM   10075 O  O   . ALA I  1 172 ? 51.399  65.674  -48.056 1.00 19.92 ? 145 ALA I O   1 
ATOM   10076 C  CB  . ALA I  1 172 ? 51.104  68.143  -45.813 1.00 20.71 ? 145 ALA I CB  1 
ATOM   10077 N  N   . CYS I  1 173 ? 49.263  66.337  -47.621 1.00 21.28 ? 146 CYS I N   1 
ATOM   10078 C  CA  . CYS I  1 173 ? 48.769  65.916  -48.948 1.00 22.27 ? 146 CYS I CA  1 
ATOM   10079 C  C   . CYS I  1 173 ? 47.544  66.711  -49.330 1.00 23.19 ? 146 CYS I C   1 
ATOM   10080 O  O   . CYS I  1 173 ? 46.933  67.377  -48.476 1.00 21.03 ? 146 CYS I O   1 
ATOM   10081 C  CB  . CYS I  1 173 ? 48.420  64.427  -48.977 1.00 26.24 ? 146 CYS I CB  1 
ATOM   10082 S  SG  . CYS I  1 173 ? 47.162  63.919  -47.773 1.00 32.28 ? 146 CYS I SG  1 
ATOM   10083 N  N   . GLY I  1 174 ? 47.191  66.660  -50.618 1.00 21.83 ? 147 GLY I N   1 
ATOM   10084 C  CA  . GLY I  1 174 ? 45.882  67.166  -51.059 1.00 23.77 ? 147 GLY I CA  1 
ATOM   10085 C  C   . GLY I  1 174 ? 45.516  66.564  -52.394 1.00 25.51 ? 147 GLY I C   1 
ATOM   10086 O  O   . GLY I  1 174 ? 46.391  65.999  -53.086 1.00 22.63 ? 147 GLY I O   1 
ATOM   10087 N  N   . VAL I  1 175 ? 44.228  66.646  -52.748 1.00 23.54 ? 148 VAL I N   1 
ATOM   10088 C  CA  . VAL I  1 175 ? 43.782  66.193  -54.073 1.00 25.66 ? 148 VAL I CA  1 
ATOM   10089 C  C   . VAL I  1 175 ? 44.103  67.289  -55.075 1.00 25.43 ? 148 VAL I C   1 
ATOM   10090 O  O   . VAL I  1 175 ? 43.956  68.507  -54.797 1.00 25.77 ? 148 VAL I O   1 
ATOM   10091 C  CB  . VAL I  1 175 ? 42.270  65.834  -54.058 1.00 26.82 ? 148 VAL I CB  1 
ATOM   10092 C  CG1 . VAL I  1 175 ? 41.831  65.279  -55.394 1.00 26.58 ? 148 VAL I CG1 1 
ATOM   10093 C  CG2 . VAL I  1 175 ? 42.012  64.802  -52.966 1.00 25.13 ? 148 VAL I CG2 1 
ATOM   10094 N  N   . ILE I  1 176 ? 44.606  66.875  -56.244 1.00 24.36 ? 149 ILE I N   1 
ATOM   10095 C  CA  . ILE I  1 176 ? 45.002  67.836  -57.261 1.00 24.24 ? 149 ILE I CA  1 
ATOM   10096 C  C   . ILE I  1 176 ? 43.722  68.193  -58.038 1.00 24.21 ? 149 ILE I C   1 
ATOM   10097 O  O   . ILE I  1 176 ? 43.108  67.323  -58.597 1.00 25.89 ? 149 ILE I O   1 
ATOM   10098 C  CB  . ILE I  1 176 ? 46.051  67.205  -58.223 1.00 22.53 ? 149 ILE I CB  1 
ATOM   10099 C  CG1 . ILE I  1 176 ? 47.341  66.888  -57.449 1.00 23.31 ? 149 ILE I CG1 1 
ATOM   10100 C  CG2 . ILE I  1 176 ? 46.379  68.194  -59.342 1.00 22.71 ? 149 ILE I CG2 1 
ATOM   10101 C  CD1 . ILE I  1 176 ? 48.246  65.844  -58.071 1.00 26.61 ? 149 ILE I CD1 1 
ATOM   10102 N  N   . GLY I  1 177 ? 43.349  69.468  -58.087 1.00 25.92 ? 150 GLY I N   1 
ATOM   10103 C  CA  . GLY I  1 177 ? 42.055  69.837  -58.693 1.00 26.91 ? 150 GLY I CA  1 
ATOM   10104 C  C   . GLY I  1 177 ? 42.223  70.774  -59.887 1.00 28.70 ? 150 GLY I C   1 
ATOM   10105 O  O   . GLY I  1 177 ? 43.255  71.428  -60.011 1.00 25.42 ? 150 GLY I O   1 
ATOM   10106 N  N   . ILE I  1 178 ? 41.205  70.854  -60.763 1.00 28.48 ? 151 ILE I N   1 
ATOM   10107 C  CA  . ILE I  1 178 ? 41.251  71.796  -61.907 1.00 30.30 ? 151 ILE I CA  1 
ATOM   10108 C  C   . ILE I  1 178 ? 41.164  73.235  -61.425 1.00 29.91 ? 151 ILE I C   1 
ATOM   10109 O  O   . ILE I  1 178 ? 40.328  73.556  -60.584 1.00 31.40 ? 151 ILE I O   1 
ATOM   10110 C  CB  . ILE I  1 178 ? 40.101  71.499  -62.932 1.00 34.48 ? 151 ILE I CB  1 
ATOM   10111 C  CG1 . ILE I  1 178 ? 40.205  70.050  -63.414 1.00 36.34 ? 151 ILE I CG1 1 
ATOM   10112 C  CG2 . ILE I  1 178 ? 40.212  72.430  -64.157 1.00 36.96 ? 151 ILE I CG2 1 
ATOM   10113 C  CD1 . ILE I  1 178 ? 38.890  69.433  -63.889 1.00 41.06 ? 151 ILE I CD1 1 
ATOM   10114 N  N   . ALA I  1 179 ? 42.008  74.096  -61.963 1.00 27.09 ? 152 ALA I N   1 
ATOM   10115 C  CA  . ALA I  1 179 ? 42.072  75.492  -61.573 1.00 33.42 ? 152 ALA I CA  1 
ATOM   10116 C  C   . ALA I  1 179 ? 41.693  76.350  -62.769 1.00 38.78 ? 152 ALA I C   1 
ATOM   10117 O  O   . ALA I  1 179 ? 41.889  75.956  -63.927 1.00 40.19 ? 152 ALA I O   1 
ATOM   10118 C  CB  . ALA I  1 179 ? 43.471  75.882  -61.100 1.00 29.33 ? 152 ALA I CB  1 
ATOM   10119 N  N   . GLN I  1 180 ? 41.133  77.512  -62.475 1.00 41.31 ? 153 GLN I N   1 
ATOM   10120 C  CA  . GLN I  1 180 ? 40.766  78.475  -63.507 1.00 48.48 ? 153 GLN I CA  1 
ATOM   10121 C  C   . GLN I  1 180 ? 42.058  79.015  -64.144 1.00 51.42 ? 153 GLN I C   1 
ATOM   10122 O  O   . GLN I  1 180 ? 43.148  79.047  -63.546 1.00 55.24 ? 153 GLN I O   1 
ATOM   10123 C  CB  . GLN I  1 180 ? 39.924  79.621  -62.922 1.00 43.94 ? 153 GLN I CB  1 
ATOM   10124 C  CG  . GLN I  1 180 ? 39.160  80.455  -63.971 1.00 42.46 ? 153 GLN I CG  1 
ATOM   10125 C  CD  . GLN I  1 180 ? 38.258  81.498  -63.330 1.00 47.05 ? 153 GLN I CD  1 
ATOM   10126 O  OE1 . GLN I  1 180 ? 38.315  81.698  -62.117 1.00 47.13 ? 153 GLN I OE1 1 
ATOM   10127 N  NE2 . GLN I  1 180 ? 37.409  82.163  -64.137 1.00 48.48 ? 153 GLN I NE2 1 
ATOM   10128 O  OXT . GLN I  1 180 ? 42.031  79.413  -65.297 1.00 57.23 ? 153 GLN I OXT 1 
ATOM   10129 N  N   . ALA J  1 28  ? 38.093  54.724  -64.680 1.00 68.75 ? 1   ALA J N   1 
ATOM   10130 C  CA  . ALA J  1 28  ? 37.507  55.607  -63.604 1.00 67.72 ? 1   ALA J CA  1 
ATOM   10131 C  C   . ALA J  1 28  ? 36.037  55.246  -63.293 1.00 55.01 ? 1   ALA J C   1 
ATOM   10132 O  O   . ALA J  1 28  ? 35.109  55.832  -63.834 1.00 58.58 ? 1   ALA J O   1 
ATOM   10133 C  CB  . ALA J  1 28  ? 37.644  57.087  -63.979 1.00 64.98 ? 1   ALA J CB  1 
ATOM   10134 N  N   . THR J  1 29  ? 35.831  54.264  -62.429 1.00 54.00 ? 2   THR J N   1 
ATOM   10135 C  CA  . THR J  1 29  ? 34.472  53.860  -62.070 1.00 47.58 ? 2   THR J CA  1 
ATOM   10136 C  C   . THR J  1 29  ? 34.085  54.298  -60.637 1.00 44.69 ? 2   THR J C   1 
ATOM   10137 O  O   . THR J  1 29  ? 32.895  54.332  -60.326 1.00 42.69 ? 2   THR J O   1 
ATOM   10138 C  CB  . THR J  1 29  ? 34.247  52.336  -62.240 1.00 47.46 ? 2   THR J CB  1 
ATOM   10139 O  OG1 . THR J  1 29  ? 34.993  51.632  -61.251 1.00 44.94 ? 2   THR J OG1 1 
ATOM   10140 C  CG2 . THR J  1 29  ? 34.688  51.870  -63.612 1.00 46.89 ? 2   THR J CG2 1 
ATOM   10141 N  N   . LYS J  1 30  ? 35.083  54.628  -59.797 1.00 39.41 ? 3   LYS J N   1 
ATOM   10142 C  CA  . LYS J  1 30  ? 34.871  55.114  -58.406 1.00 37.00 ? 3   LYS J CA  1 
ATOM   10143 C  C   . LYS J  1 30  ? 35.582  56.439  -58.108 1.00 35.03 ? 3   LYS J C   1 
ATOM   10144 O  O   . LYS J  1 30  ? 36.703  56.668  -58.565 1.00 32.14 ? 3   LYS J O   1 
ATOM   10145 C  CB  . LYS J  1 30  ? 35.297  54.079  -57.360 1.00 38.08 ? 3   LYS J CB  1 
ATOM   10146 C  CG  . LYS J  1 30  ? 34.634  52.710  -57.466 1.00 42.64 ? 3   LYS J CG  1 
ATOM   10147 C  CD  . LYS J  1 30  ? 34.826  51.930  -56.174 1.00 55.95 ? 3   LYS J CD  1 
ATOM   10148 C  CE  . LYS J  1 30  ? 34.504  50.459  -56.360 1.00 60.52 ? 3   LYS J CE  1 
ATOM   10149 N  NZ  . LYS J  1 30  ? 34.003  49.880  -55.082 1.00 65.59 ? 3   LYS J NZ  1 
ATOM   10150 N  N   . ALA J  1 31  ? 34.931  57.294  -57.317 1.00 33.61 ? 4   ALA J N   1 
ATOM   10151 C  CA  . ALA J  1 31  ? 35.502  58.570  -56.860 1.00 31.46 ? 4   ALA J CA  1 
ATOM   10152 C  C   . ALA J  1 31  ? 35.018  58.803  -55.421 1.00 33.18 ? 4   ALA J C   1 
ATOM   10153 O  O   . ALA J  1 31  ? 34.117  58.068  -54.928 1.00 34.37 ? 4   ALA J O   1 
ATOM   10154 C  CB  . ALA J  1 31  ? 35.097  59.714  -57.784 1.00 28.24 ? 4   ALA J CB  1 
ATOM   10155 N  N   . VAL J  1 32  ? 35.627  59.774  -54.745 1.00 29.63 ? 5   VAL J N   1 
ATOM   10156 C  CA  . VAL J  1 32  ? 35.336  60.063  -53.321 1.00 28.80 ? 5   VAL J CA  1 
ATOM   10157 C  C   . VAL J  1 32  ? 35.669  61.524  -53.070 1.00 28.50 ? 5   VAL J C   1 
ATOM   10158 O  O   . VAL J  1 32  ? 36.509  62.125  -53.763 1.00 26.39 ? 5   VAL J O   1 
ATOM   10159 C  CB  . VAL J  1 32  ? 36.124  59.133  -52.365 1.00 31.07 ? 5   VAL J CB  1 
ATOM   10160 C  CG1 . VAL J  1 32  ? 37.641  59.370  -52.451 1.00 30.61 ? 5   VAL J CG1 1 
ATOM   10161 C  CG2 . VAL J  1 32  ? 35.613  59.235  -50.924 1.00 30.88 ? 5   VAL J CG2 1 
ATOM   10162 N  N   . CYS J  1 33  ? 34.975  62.109  -52.092 1.00 27.17 ? 6   CYS J N   1 
ATOM   10163 C  CA  . CYS J  1 33  ? 35.138  63.499  -51.780 1.00 25.77 ? 6   CYS J CA  1 
ATOM   10164 C  C   . CYS J  1 33  ? 35.080  63.598  -50.236 1.00 27.38 ? 6   CYS J C   1 
ATOM   10165 O  O   . CYS J  1 33  ? 34.154  63.075  -49.614 1.00 28.18 ? 6   CYS J O   1 
ATOM   10166 C  CB  . CYS J  1 33  ? 33.988  64.331  -52.350 1.00 24.54 ? 6   CYS J CB  1 
ATOM   10167 S  SG  . CYS J  1 33  ? 34.308  66.095  -52.060 1.00 30.91 ? 6   CYS J SG  1 
ATOM   10168 N  N   . VAL J  1 34  ? 36.075  64.230  -49.645 1.00 25.69 ? 7   VAL J N   1 
ATOM   10169 C  CA  . VAL J  1 34  ? 36.052  64.531  -48.206 1.00 26.95 ? 7   VAL J CA  1 
ATOM   10170 C  C   . VAL J  1 34  ? 35.668  65.991  -48.012 1.00 25.70 ? 7   VAL J C   1 
ATOM   10171 O  O   . VAL J  1 34  ? 36.361  66.886  -48.483 1.00 23.52 ? 7   VAL J O   1 
ATOM   10172 C  CB  . VAL J  1 34  ? 37.413  64.252  -47.544 1.00 28.49 ? 7   VAL J CB  1 
ATOM   10173 C  CG1 . VAL J  1 34  ? 37.343  64.613  -46.062 1.00 26.56 ? 7   VAL J CG1 1 
ATOM   10174 C  CG2 . VAL J  1 34  ? 37.775  62.796  -47.768 1.00 27.15 ? 7   VAL J CG2 1 
ATOM   10175 N  N   . LEU J  1 35  ? 34.542  66.236  -47.352 1.00 23.69 ? 8   LEU J N   1 
ATOM   10176 C  CA  . LEU J  1 35  ? 34.082  67.625  -47.246 1.00 24.21 ? 8   LEU J CA  1 
ATOM   10177 C  C   . LEU J  1 35  ? 34.581  68.214  -45.919 1.00 24.80 ? 8   LEU J C   1 
ATOM   10178 O  O   . LEU J  1 35  ? 34.449  67.545  -44.891 1.00 24.53 ? 8   LEU J O   1 
ATOM   10179 C  CB  . LEU J  1 35  ? 32.547  67.616  -47.227 1.00 26.13 ? 8   LEU J CB  1 
ATOM   10180 C  CG  . LEU J  1 35  ? 31.827  67.149  -48.493 1.00 28.50 ? 8   LEU J CG  1 
ATOM   10181 C  CD1 . LEU J  1 35  ? 30.368  66.965  -48.109 1.00 33.77 ? 8   LEU J CD1 1 
ATOM   10182 C  CD2 . LEU J  1 35  ? 31.957  68.259  -49.501 1.00 27.07 ? 8   LEU J CD2 1 
ATOM   10183 N  N   . LYS J  1 36  ? 35.123  69.430  -45.948 1.00 24.63 ? 9   LYS J N   1 
ATOM   10184 C  CA  . LYS J  1 36  ? 35.614  70.118  -44.745 1.00 29.30 ? 9   LYS J CA  1 
ATOM   10185 C  C   . LYS J  1 36  ? 35.368  71.565  -44.950 1.00 26.15 ? 9   LYS J C   1 
ATOM   10186 O  O   . LYS J  1 36  ? 35.342  72.026  -46.090 1.00 28.75 ? 9   LYS J O   1 
ATOM   10187 C  CB  . LYS J  1 36  ? 37.147  69.921  -44.562 1.00 31.03 ? 9   LYS J CB  1 
ATOM   10188 C  CG  . LYS J  1 36  ? 37.507  68.515  -44.109 1.00 41.03 ? 9   LYS J CG  1 
ATOM   10189 C  CD  . LYS J  1 36  ? 38.883  68.432  -43.422 1.00 49.40 ? 9   LYS J CD  1 
ATOM   10190 C  CE  . LYS J  1 36  ? 39.127  67.075  -42.734 1.00 51.35 ? 9   LYS J CE  1 
ATOM   10191 N  NZ  . LYS J  1 36  ? 39.525  65.996  -43.696 1.00 50.97 ? 9   LYS J NZ  1 
ATOM   10192 N  N   . GLY J  1 37  ? 35.231  72.340  -43.883 1.00 26.85 ? 10  GLY J N   1 
ATOM   10193 C  CA  . GLY J  1 37  ? 35.051  73.782  -44.063 1.00 27.01 ? 10  GLY J CA  1 
ATOM   10194 C  C   . GLY J  1 37  ? 35.565  74.599  -42.869 1.00 34.60 ? 10  GLY J C   1 
ATOM   10195 O  O   . GLY J  1 37  ? 36.393  74.126  -42.124 1.00 33.21 ? 10  GLY J O   1 
ATOM   10196 N  N   . ASP J  1 38  ? 35.081  75.818  -42.698 1.00 34.65 ? 11  ASP J N   1 
ATOM   10197 C  CA  . ASP J  1 38  ? 35.535  76.694  -41.605 1.00 39.95 ? 11  ASP J CA  1 
ATOM   10198 C  C   . ASP J  1 38  ? 34.841  76.430  -40.273 1.00 38.86 ? 11  ASP J C   1 
ATOM   10199 O  O   . ASP J  1 38  ? 35.306  76.857  -39.236 1.00 36.01 ? 11  ASP J O   1 
ATOM   10200 C  CB  . ASP J  1 38  ? 35.330  78.146  -42.001 1.00 42.61 ? 11  ASP J CB  1 
ATOM   10201 C  CG  . ASP J  1 38  ? 36.368  78.612  -42.969 1.00 50.60 ? 11  ASP J CG  1 
ATOM   10202 O  OD1 . ASP J  1 38  ? 37.475  78.015  -42.967 1.00 53.60 ? 11  ASP J OD1 1 
ATOM   10203 O  OD2 . ASP J  1 38  ? 36.095  79.559  -43.738 1.00 56.86 ? 11  ASP J OD2 1 
ATOM   10204 N  N   . GLY J  1 39  ? 33.717  75.730  -40.321 1.00 36.37 ? 12  GLY J N   1 
ATOM   10205 C  CA  . GLY J  1 39  ? 33.007  75.339  -39.130 1.00 33.63 ? 12  GLY J CA  1 
ATOM   10206 C  C   . GLY J  1 39  ? 33.047  73.862  -38.934 1.00 32.46 ? 12  GLY J C   1 
ATOM   10207 O  O   . GLY J  1 39  ? 34.019  73.168  -39.324 1.00 32.60 ? 12  GLY J O   1 
ATOM   10208 N  N   . PRO J  1 40  ? 31.969  73.323  -38.354 1.00 29.14 ? 13  PRO J N   1 
ATOM   10209 C  CA  . PRO J  1 40  ? 32.013  71.913  -38.000 1.00 27.74 ? 13  PRO J CA  1 
ATOM   10210 C  C   . PRO J  1 40  ? 31.534  70.942  -39.091 1.00 25.92 ? 13  PRO J C   1 
ATOM   10211 O  O   . PRO J  1 40  ? 31.523  69.751  -38.858 1.00 28.81 ? 13  PRO J O   1 
ATOM   10212 C  CB  . PRO J  1 40  ? 31.058  71.848  -36.805 1.00 29.51 ? 13  PRO J CB  1 
ATOM   10213 C  CG  . PRO J  1 40  ? 30.006  72.901  -37.156 1.00 28.24 ? 13  PRO J CG  1 
ATOM   10214 C  CD  . PRO J  1 40  ? 30.738  74.005  -37.872 1.00 31.65 ? 13  PRO J CD  1 
ATOM   10215 N  N   . VAL J  1 41  ? 31.105  71.450  -40.247 1.00 28.46 ? 14  VAL J N   1 
ATOM   10216 C  CA  . VAL J  1 41  ? 30.500  70.576  -41.274 1.00 26.30 ? 14  VAL J CA  1 
ATOM   10217 C  C   . VAL J  1 41  ? 31.566  69.668  -41.896 1.00 28.09 ? 14  VAL J C   1 
ATOM   10218 O  O   . VAL J  1 41  ? 32.548  70.189  -42.425 1.00 28.49 ? 14  VAL J O   1 
ATOM   10219 C  CB  . VAL J  1 41  ? 29.772  71.403  -42.362 1.00 26.46 ? 14  VAL J CB  1 
ATOM   10220 C  CG1 . VAL J  1 41  ? 29.152  70.463  -43.400 1.00 26.95 ? 14  VAL J CG1 1 
ATOM   10221 C  CG2 . VAL J  1 41  ? 28.655  72.250  -41.724 1.00 26.33 ? 14  VAL J CG2 1 
ATOM   10222 N  N   . GLN J  1 42  ? 31.382  68.348  -41.800 1.00 28.63 ? 15  GLN J N   1 
ATOM   10223 C  CA  . GLN J  1 42  ? 32.321  67.366  -42.376 1.00 33.02 ? 15  GLN J CA  1 
ATOM   10224 C  C   . GLN J  1 42  ? 31.562  66.199  -42.962 1.00 31.55 ? 15  GLN J C   1 
ATOM   10225 O  O   . GLN J  1 42  ? 30.534  65.762  -42.427 1.00 30.73 ? 15  GLN J O   1 
ATOM   10226 C  CB  . GLN J  1 42  ? 33.223  66.727  -41.313 1.00 35.94 ? 15  GLN J CB  1 
ATOM   10227 C  CG  . GLN J  1 42  ? 33.618  67.596  -40.157 1.00 43.23 ? 15  GLN J CG  1 
ATOM   10228 C  CD  . GLN J  1 42  ? 34.513  66.834  -39.191 1.00 51.91 ? 15  GLN J CD  1 
ATOM   10229 O  OE1 . GLN J  1 42  ? 34.551  65.584  -39.177 1.00 53.70 ? 15  GLN J OE1 1 
ATOM   10230 N  NE2 . GLN J  1 42  ? 35.241  67.576  -38.388 1.00 53.47 ? 15  GLN J NE2 1 
ATOM   10231 N  N   . GLY J  1 43  ? 32.077  65.645  -44.046 1.00 29.15 ? 16  GLY J N   1 
ATOM   10232 C  CA  . GLY J  1 43  ? 31.451  64.461  -44.590 1.00 30.03 ? 16  GLY J CA  1 
ATOM   10233 C  C   . GLY J  1 43  ? 32.315  63.753  -45.604 1.00 29.36 ? 16  GLY J C   1 
ATOM   10234 O  O   . GLY J  1 43  ? 33.386  64.254  -45.982 1.00 27.88 ? 16  GLY J O   1 
ATOM   10235 N  N   . ILE J  1 44  ? 31.877  62.560  -45.955 1.00 28.47 ? 17  ILE J N   1 
ATOM   10236 C  CA  . ILE J  1 44  ? 32.551  61.738  -46.957 1.00 29.77 ? 17  ILE J CA  1 
ATOM   10237 C  C   . ILE J  1 44  ? 31.447  61.274  -47.907 1.00 32.21 ? 17  ILE J C   1 
ATOM   10238 O  O   . ILE J  1 44  ? 30.442  60.650  -47.481 1.00 31.41 ? 17  ILE J O   1 
ATOM   10239 C  CB  . ILE J  1 44  ? 33.231  60.499  -46.367 1.00 30.95 ? 17  ILE J CB  1 
ATOM   10240 C  CG1 . ILE J  1 44  ? 34.362  60.874  -45.402 1.00 33.57 ? 17  ILE J CG1 1 
ATOM   10241 C  CG2 . ILE J  1 44  ? 33.780  59.614  -47.498 1.00 32.33 ? 17  ILE J CG2 1 
ATOM   10242 C  CD1 . ILE J  1 44  ? 34.828  59.704  -44.547 1.00 36.96 ? 17  ILE J CD1 1 
ATOM   10243 N  N   . ILE J  1 45  ? 31.641  61.592  -49.182 1.00 30.05 ? 18  ILE J N   1 
ATOM   10244 C  CA  . ILE J  1 45  ? 30.724  61.204  -50.235 1.00 29.74 ? 18  ILE J CA  1 
ATOM   10245 C  C   . ILE J  1 45  ? 31.431  60.322  -51.258 1.00 33.84 ? 18  ILE J C   1 
ATOM   10246 O  O   . ILE J  1 45  ? 32.542  60.674  -51.730 1.00 30.87 ? 18  ILE J O   1 
ATOM   10247 C  CB  . ILE J  1 45  ? 30.151  62.434  -50.913 1.00 28.29 ? 18  ILE J CB  1 
ATOM   10248 C  CG1 . ILE J  1 45  ? 29.386  63.308  -49.882 1.00 29.95 ? 18  ILE J CG1 1 
ATOM   10249 C  CG2 . ILE J  1 45  ? 29.203  62.018  -52.043 1.00 27.73 ? 18  ILE J CG2 1 
ATOM   10250 C  CD1 . ILE J  1 45  ? 28.100  62.646  -49.324 1.00 30.65 ? 18  ILE J CD1 1 
ATOM   10251 N  N   . ASN J  1 46  ? 30.811  59.185  -51.562 1.00 32.93 ? 19  ASN J N   1 
ATOM   10252 C  CA  . ASN J  1 46  ? 31.346  58.239  -52.518 1.00 36.09 ? 19  ASN J CA  1 
ATOM   10253 C  C   . ASN J  1 46  ? 30.592  58.343  -53.834 1.00 39.24 ? 19  ASN J C   1 
ATOM   10254 O  O   . ASN J  1 46  ? 29.423  58.719  -53.841 1.00 37.66 ? 19  ASN J O   1 
ATOM   10255 C  CB  . ASN J  1 46  ? 31.224  56.840  -51.948 1.00 36.51 ? 19  ASN J CB  1 
ATOM   10256 C  CG  . ASN J  1 46  ? 31.818  56.732  -50.548 1.00 42.50 ? 19  ASN J CG  1 
ATOM   10257 O  OD1 . ASN J  1 46  ? 31.091  56.634  -49.541 1.00 45.36 ? 19  ASN J OD1 1 
ATOM   10258 N  ND2 . ASN J  1 46  ? 33.129  56.756  -50.472 1.00 41.49 ? 19  ASN J ND2 1 
ATOM   10259 N  N   . PHE J  1 47  ? 31.262  58.018  -54.948 1.00 36.45 ? 20  PHE J N   1 
ATOM   10260 C  CA  . PHE J  1 47  ? 30.668  58.047  -56.287 1.00 35.05 ? 20  PHE J CA  1 
ATOM   10261 C  C   . PHE J  1 47  ? 31.032  56.725  -56.948 1.00 36.38 ? 20  PHE J C   1 
ATOM   10262 O  O   . PHE J  1 47  ? 32.184  56.246  -56.818 1.00 34.16 ? 20  PHE J O   1 
ATOM   10263 C  CB  . PHE J  1 47  ? 31.259  59.170  -57.127 1.00 34.62 ? 20  PHE J CB  1 
ATOM   10264 C  CG  . PHE J  1 47  ? 31.038  60.546  -56.572 1.00 33.63 ? 20  PHE J CG  1 
ATOM   10265 C  CD1 . PHE J  1 47  ? 31.869  61.064  -55.565 1.00 37.42 ? 20  PHE J CD1 1 
ATOM   10266 C  CD2 . PHE J  1 47  ? 30.018  61.326  -57.054 1.00 33.04 ? 20  PHE J CD2 1 
ATOM   10267 C  CE1 . PHE J  1 47  ? 31.654  62.338  -55.068 1.00 36.47 ? 20  PHE J CE1 1 
ATOM   10268 C  CE2 . PHE J  1 47  ? 29.798  62.609  -56.560 1.00 39.65 ? 20  PHE J CE2 1 
ATOM   10269 C  CZ  . PHE J  1 47  ? 30.636  63.118  -55.572 1.00 37.65 ? 20  PHE J CZ  1 
ATOM   10270 N  N   . GLU J  1 48  ? 30.064  56.107  -57.617 1.00 35.77 ? 21  GLU J N   1 
ATOM   10271 C  CA  . GLU J  1 48  ? 30.349  54.893  -58.379 1.00 40.67 ? 21  GLU J CA  1 
ATOM   10272 C  C   . GLU J  1 48  ? 29.574  54.877  -59.706 1.00 45.56 ? 21  GLU J C   1 
ATOM   10273 O  O   . GLU J  1 48  ? 28.384  55.232  -59.767 1.00 40.99 ? 21  GLU J O   1 
ATOM   10274 C  CB  . GLU J  1 48  ? 30.102  53.648  -57.536 1.00 41.72 ? 21  GLU J CB  1 
ATOM   10275 C  CG  . GLU J  1 48  ? 30.370  52.349  -58.286 1.00 53.02 ? 21  GLU J CG  1 
ATOM   10276 C  CD  . GLU J  1 48  ? 30.564  51.154  -57.380 1.00 61.56 ? 21  GLU J CD  1 
ATOM   10277 O  OE1 . GLU J  1 48  ? 29.640  50.811  -56.595 1.00 64.91 ? 21  GLU J OE1 1 
ATOM   10278 O  OE2 . GLU J  1 48  ? 31.651  50.534  -57.467 1.00 67.14 ? 21  GLU J OE2 1 
ATOM   10279 N  N   . GLN J  1 49  ? 30.276  54.510  -60.782 1.00 44.91 ? 22  GLN J N   1 
ATOM   10280 C  CA  . GLN J  1 49  ? 29.680  54.508  -62.114 1.00 44.38 ? 22  GLN J CA  1 
ATOM   10281 C  C   . GLN J  1 49  ? 30.134  53.264  -62.834 1.00 48.62 ? 22  GLN J C   1 
ATOM   10282 O  O   . GLN J  1 49  ? 31.108  53.315  -63.580 1.00 46.71 ? 22  GLN J O   1 
ATOM   10283 C  CB  . GLN J  1 49  ? 30.091  55.746  -62.891 1.00 40.23 ? 22  GLN J CB  1 
ATOM   10284 C  CG  . GLN J  1 49  ? 29.362  55.902  -64.221 1.00 41.39 ? 22  GLN J CG  1 
ATOM   10285 C  CD  . GLN J  1 49  ? 29.850  57.116  -64.977 1.00 41.54 ? 22  GLN J CD  1 
ATOM   10286 O  OE1 . GLN J  1 49  ? 31.012  57.496  -64.848 1.00 44.82 ? 22  GLN J OE1 1 
ATOM   10287 N  NE2 . GLN J  1 49  ? 28.957  57.769  -65.728 1.00 42.14 ? 22  GLN J NE2 1 
ATOM   10288 N  N   . LYS J  1 50  ? 29.427  52.156  -62.579 1.00 52.30 ? 23  LYS J N   1 
ATOM   10289 C  CA  . LYS J  1 50  ? 29.813  50.834  -63.084 1.00 56.94 ? 23  LYS J CA  1 
ATOM   10290 C  C   . LYS J  1 50  ? 29.806  50.755  -64.628 1.00 59.25 ? 23  LYS J C   1 
ATOM   10291 O  O   . LYS J  1 50  ? 30.633  50.037  -65.201 1.00 59.69 ? 23  LYS J O   1 
ATOM   10292 C  CB  . LYS J  1 50  ? 28.958  49.716  -62.446 1.00 53.42 ? 23  LYS J CB  1 
ATOM   10293 N  N   . GLU J  1 51  ? 28.904  51.494  -65.285 1.00 53.87 ? 24  GLU J N   1 
ATOM   10294 C  CA  . GLU J  1 51  ? 28.803  51.487  -66.752 1.00 55.17 ? 24  GLU J CA  1 
ATOM   10295 C  C   . GLU J  1 51  ? 29.251  52.824  -67.353 1.00 57.90 ? 24  GLU J C   1 
ATOM   10296 O  O   . GLU J  1 51  ? 28.846  53.897  -66.888 1.00 55.19 ? 24  GLU J O   1 
ATOM   10297 C  CB  . GLU J  1 51  ? 27.377  51.111  -67.222 1.00 55.10 ? 24  GLU J CB  1 
ATOM   10298 N  N   . SER J  1 52  ? 30.067  52.727  -68.408 1.00 58.43 ? 25  SER J N   1 
ATOM   10299 C  CA  . SER J  1 52  ? 30.754  53.858  -69.056 1.00 62.66 ? 25  SER J CA  1 
ATOM   10300 C  C   . SER J  1 52  ? 29.909  55.105  -69.139 1.00 59.39 ? 25  SER J C   1 
ATOM   10301 O  O   . SER J  1 52  ? 30.403  56.208  -68.936 1.00 64.30 ? 25  SER J O   1 
ATOM   10302 C  CB  . SER J  1 52  ? 31.208  53.502  -70.490 1.00 63.44 ? 25  SER J CB  1 
ATOM   10303 O  OG  . SER J  1 52  ? 31.940  52.287  -70.545 1.00 67.89 ? 25  SER J OG  1 
ATOM   10304 N  N   . ASN J  1 53  ? 28.639  54.958  -69.474 1.00 59.71 ? 26  ASN J N   1 
ATOM   10305 C  CA  . ASN J  1 53  ? 27.848  56.164  -69.613 1.00 61.89 ? 26  ASN J CA  1 
ATOM   10306 C  C   . ASN J  1 53  ? 26.557  56.243  -68.792 1.00 60.80 ? 26  ASN J C   1 
ATOM   10307 O  O   . ASN J  1 53  ? 25.737  57.165  -68.968 1.00 57.33 ? 26  ASN J O   1 
ATOM   10308 C  CB  . ASN J  1 53  ? 27.598  56.440  -71.079 1.00 67.09 ? 26  ASN J CB  1 
ATOM   10309 C  CG  . ASN J  1 53  ? 27.953  57.850  -71.433 1.00 71.02 ? 26  ASN J CG  1 
ATOM   10310 O  OD1 . ASN J  1 53  ? 28.576  58.546  -70.625 1.00 71.41 ? 26  ASN J OD1 1 
ATOM   10311 N  ND2 . ASN J  1 53  ? 27.558  58.295  -72.625 1.00 69.72 ? 26  ASN J ND2 1 
ATOM   10312 N  N   . GLY J  1 54  ? 26.421  55.289  -67.874 1.00 59.48 ? 27  GLY J N   1 
ATOM   10313 C  CA  . GLY J  1 54  ? 25.216  55.137  -67.072 1.00 59.98 ? 27  GLY J CA  1 
ATOM   10314 C  C   . GLY J  1 54  ? 25.191  56.040  -65.853 1.00 57.42 ? 27  GLY J C   1 
ATOM   10315 O  O   . GLY J  1 54  ? 26.038  56.922  -65.711 1.00 50.87 ? 27  GLY J O   1 
ATOM   10316 N  N   . PRO J  1 55  ? 24.196  55.829  -64.969 1.00 57.37 ? 28  PRO J N   1 
ATOM   10317 C  CA  . PRO J  1 55  ? 24.048  56.647  -63.765 1.00 54.14 ? 28  PRO J CA  1 
ATOM   10318 C  C   . PRO J  1 55  ? 25.232  56.536  -62.782 1.00 46.19 ? 28  PRO J C   1 
ATOM   10319 O  O   . PRO J  1 55  ? 25.922  55.487  -62.693 1.00 41.59 ? 28  PRO J O   1 
ATOM   10320 C  CB  . PRO J  1 55  ? 22.767  56.084  -63.125 1.00 55.61 ? 28  PRO J CB  1 
ATOM   10321 C  CG  . PRO J  1 55  ? 22.001  55.507  -64.278 1.00 58.53 ? 28  PRO J CG  1 
ATOM   10322 C  CD  . PRO J  1 55  ? 23.084  54.864  -65.102 1.00 58.72 ? 28  PRO J CD  1 
ATOM   10323 N  N   . VAL J  1 56  ? 25.435  57.611  -62.028 1.00 43.27 ? 29  VAL J N   1 
ATOM   10324 C  CA  . VAL J  1 56  ? 26.422  57.600  -60.957 1.00 39.94 ? 29  VAL J CA  1 
ATOM   10325 C  C   . VAL J  1 56  ? 25.690  57.406  -59.622 1.00 40.11 ? 29  VAL J C   1 
ATOM   10326 O  O   . VAL J  1 56  ? 24.776  58.175  -59.318 1.00 38.57 ? 29  VAL J O   1 
ATOM   10327 C  CB  . VAL J  1 56  ? 27.197  58.928  -60.936 1.00 40.44 ? 29  VAL J CB  1 
ATOM   10328 C  CG1 . VAL J  1 56  ? 28.319  58.875  -59.891 1.00 38.88 ? 29  VAL J CG1 1 
ATOM   10329 C  CG2 . VAL J  1 56  ? 27.762  59.238  -62.324 1.00 38.42 ? 29  VAL J CG2 1 
ATOM   10330 N  N   . LYS J  1 57  ? 26.041  56.379  -58.848 1.00 37.20 ? 30  LYS J N   1 
ATOM   10331 C  CA  . LYS J  1 57  ? 25.520  56.327  -57.461 1.00 40.91 ? 30  LYS J CA  1 
ATOM   10332 C  C   . LYS J  1 57  ? 26.356  57.312  -56.611 1.00 42.05 ? 30  LYS J C   1 
ATOM   10333 O  O   . LYS J  1 57  ? 27.598  57.325  -56.706 1.00 36.70 ? 30  LYS J O   1 
ATOM   10334 C  CB  . LYS J  1 57  ? 25.548  54.926  -56.857 1.00 43.21 ? 30  LYS J CB  1 
ATOM   10335 C  CG  . LYS J  1 57  ? 24.783  53.876  -57.668 1.00 54.39 ? 30  LYS J CG  1 
ATOM   10336 C  CD  . LYS J  1 57  ? 24.692  52.494  -57.007 1.00 56.86 ? 30  LYS J CD  1 
ATOM   10337 C  CE  . LYS J  1 57  ? 25.992  51.670  -57.088 1.00 63.87 ? 30  LYS J CE  1 
ATOM   10338 N  NZ  . LYS J  1 57  ? 26.691  51.617  -58.419 1.00 61.65 ? 30  LYS J NZ  1 
ATOM   10339 N  N   . VAL J  1 58  ? 25.668  58.176  -55.858 1.00 41.46 ? 31  VAL J N   1 
ATOM   10340 C  CA  . VAL J  1 58  ? 26.298  59.099  -54.893 1.00 38.30 ? 31  VAL J CA  1 
ATOM   10341 C  C   . VAL J  1 58  ? 25.797  58.726  -53.495 1.00 40.49 ? 31  VAL J C   1 
ATOM   10342 O  O   . VAL J  1 58  ? 24.585  58.780  -53.239 1.00 40.77 ? 31  VAL J O   1 
ATOM   10343 C  CB  . VAL J  1 58  ? 25.945  60.569  -55.207 1.00 37.08 ? 31  VAL J CB  1 
ATOM   10344 C  CG1 . VAL J  1 58  ? 26.706  61.546  -54.298 1.00 31.07 ? 31  VAL J CG1 1 
ATOM   10345 C  CG2 . VAL J  1 58  ? 26.245  60.895  -56.650 1.00 36.45 ? 31  VAL J CG2 1 
ATOM   10346 N  N   . TRP J  1 59  ? 26.695  58.334  -52.595 1.00 35.93 ? 32  TRP J N   1 
ATOM   10347 C  CA  . TRP J  1 59  ? 26.251  58.043  -51.246 1.00 36.10 ? 32  TRP J CA  1 
ATOM   10348 C  C   . TRP J  1 59  ? 27.294  58.415  -50.188 1.00 39.16 ? 32  TRP J C   1 
ATOM   10349 O  O   . TRP J  1 59  ? 28.520  58.441  -50.441 1.00 34.35 ? 32  TRP J O   1 
ATOM   10350 C  CB  . TRP J  1 59  ? 25.831  56.572  -51.110 1.00 35.93 ? 32  TRP J CB  1 
ATOM   10351 C  CG  . TRP J  1 59  ? 26.966  55.659  -51.013 1.00 38.36 ? 32  TRP J CG  1 
ATOM   10352 C  CD1 . TRP J  1 59  ? 27.495  55.122  -49.875 1.00 38.10 ? 32  TRP J CD1 1 
ATOM   10353 C  CD2 . TRP J  1 59  ? 27.773  55.193  -52.092 1.00 38.62 ? 32  TRP J CD2 1 
ATOM   10354 N  NE1 . TRP J  1 59  ? 28.577  54.345  -50.181 1.00 40.73 ? 32  TRP J NE1 1 
ATOM   10355 C  CE2 . TRP J  1 59  ? 28.767  54.364  -51.538 1.00 40.70 ? 32  TRP J CE2 1 
ATOM   10356 C  CE3 . TRP J  1 59  ? 27.743  55.391  -53.473 1.00 39.39 ? 32  TRP J CE3 1 
ATOM   10357 C  CZ2 . TRP J  1 59  ? 29.717  53.716  -52.313 1.00 43.19 ? 32  TRP J CZ2 1 
ATOM   10358 C  CZ3 . TRP J  1 59  ? 28.702  54.770  -54.253 1.00 42.81 ? 32  TRP J CZ3 1 
ATOM   10359 C  CH2 . TRP J  1 59  ? 29.678  53.932  -53.670 1.00 42.38 ? 32  TRP J CH2 1 
ATOM   10360 N  N   . GLY J  1 60  ? 26.803  58.728  -48.992 1.00 36.05 ? 33  GLY J N   1 
ATOM   10361 C  CA  . GLY J  1 60  ? 27.699  58.910  -47.859 1.00 34.49 ? 33  GLY J CA  1 
ATOM   10362 C  C   . GLY J  1 60  ? 26.934  59.672  -46.806 1.00 39.91 ? 33  GLY J C   1 
ATOM   10363 O  O   . GLY J  1 60  ? 25.725  59.487  -46.663 1.00 34.94 ? 33  GLY J O   1 
ATOM   10364 N  N   . SER J  1 61  ? 27.617  60.558  -46.093 1.00 37.54 ? 34  SER J N   1 
ATOM   10365 C  CA  . SER J  1 61  ? 27.015  61.159  -44.908 1.00 34.35 ? 34  SER J CA  1 
ATOM   10366 C  C   . SER J  1 61  ? 27.736  62.455  -44.600 1.00 36.01 ? 34  SER J C   1 
ATOM   10367 O  O   . SER J  1 61  ? 28.968  62.539  -44.781 1.00 35.05 ? 34  SER J O   1 
ATOM   10368 C  CB  . SER J  1 61  ? 27.140  60.168  -43.760 1.00 34.85 ? 34  SER J CB  1 
ATOM   10369 O  OG  . SER J  1 61  ? 26.496  60.687  -42.620 1.00 46.07 ? 34  SER J OG  1 
ATOM   10370 N  N   . ILE J  1 62  ? 26.975  63.476  -44.198 1.00 31.48 ? 35  ILE J N   1 
ATOM   10371 C  CA  . ILE J  1 62  ? 27.527  64.759  -43.803 1.00 29.57 ? 35  ILE J CA  1 
ATOM   10372 C  C   . ILE J  1 62  ? 27.023  65.032  -42.382 1.00 35.60 ? 35  ILE J C   1 
ATOM   10373 O  O   . ILE J  1 62  ? 25.844  64.778  -42.069 1.00 33.24 ? 35  ILE J O   1 
ATOM   10374 C  CB  . ILE J  1 62  ? 27.059  65.873  -44.743 1.00 30.28 ? 35  ILE J CB  1 
ATOM   10375 C  CG1 . ILE J  1 62  ? 27.295  65.453  -46.221 1.00 30.01 ? 35  ILE J CG1 1 
ATOM   10376 C  CG2 . ILE J  1 62  ? 27.739  67.206  -44.437 1.00 28.65 ? 35  ILE J CG2 1 
ATOM   10377 C  CD1 . ILE J  1 62  ? 26.875  66.517  -47.204 1.00 32.43 ? 35  ILE J CD1 1 
ATOM   10378 N  N   . LYS J  1 63  ? 27.903  65.517  -41.515 1.00 30.96 ? 36  LYS J N   1 
ATOM   10379 C  CA  . LYS J  1 63  ? 27.489  65.894  -40.158 1.00 30.07 ? 36  LYS J CA  1 
ATOM   10380 C  C   . LYS J  1 63  ? 27.814  67.338  -39.858 1.00 27.64 ? 36  LYS J C   1 
ATOM   10381 O  O   . LYS J  1 63  ? 28.490  67.989  -40.652 1.00 26.88 ? 36  LYS J O   1 
ATOM   10382 C  CB  . LYS J  1 63  ? 28.124  64.933  -39.149 1.00 30.48 ? 36  LYS J CB  1 
ATOM   10383 C  CG  . LYS J  1 63  ? 29.657  64.979  -39.048 1.00 33.78 ? 36  LYS J CG  1 
ATOM   10384 C  CD  . LYS J  1 63  ? 30.122  63.871  -38.096 1.00 35.13 ? 36  LYS J CD  1 
ATOM   10385 C  CE  . LYS J  1 63  ? 31.611  63.605  -38.132 1.00 41.74 ? 36  LYS J CE  1 
ATOM   10386 N  NZ  . LYS J  1 63  ? 32.309  64.745  -37.499 1.00 51.52 ? 36  LYS J NZ  1 
ATOM   10387 N  N   . GLY J  1 64  ? 27.377  67.850  -38.694 1.00 26.41 ? 37  GLY J N   1 
ATOM   10388 C  CA  . GLY J  1 64  ? 27.597  69.266  -38.361 1.00 26.47 ? 37  GLY J CA  1 
ATOM   10389 C  C   . GLY J  1 64  ? 26.652  70.280  -38.986 1.00 26.76 ? 37  GLY J C   1 
ATOM   10390 O  O   . GLY J  1 64  ? 26.882  71.499  -38.935 1.00 29.52 ? 37  GLY J O   1 
ATOM   10391 N  N   . LEU J  1 65  ? 25.570  69.792  -39.601 1.00 26.61 ? 38  LEU J N   1 
ATOM   10392 C  CA  . LEU J  1 65  ? 24.628  70.675  -40.278 1.00 27.81 ? 38  LEU J CA  1 
ATOM   10393 C  C   . LEU J  1 65  ? 23.480  71.125  -39.340 1.00 31.11 ? 38  LEU J C   1 
ATOM   10394 O  O   . LEU J  1 65  ? 23.223  70.466  -38.345 1.00 34.35 ? 38  LEU J O   1 
ATOM   10395 C  CB  . LEU J  1 65  ? 23.996  69.964  -41.499 1.00 29.52 ? 38  LEU J CB  1 
ATOM   10396 C  CG  . LEU J  1 65  ? 25.014  69.612  -42.598 1.00 30.25 ? 38  LEU J CG  1 
ATOM   10397 C  CD1 . LEU J  1 65  ? 24.504  68.462  -43.488 1.00 29.01 ? 38  LEU J CD1 1 
ATOM   10398 C  CD2 . LEU J  1 65  ? 25.370  70.864  -43.377 1.00 28.22 ? 38  LEU J CD2 1 
ATOM   10399 N  N   . THR J  1 66  ? 22.812  72.223  -39.664 1.00 32.93 ? 39  THR J N   1 
ATOM   10400 C  CA  . THR J  1 66  ? 21.539  72.544  -38.975 1.00 35.23 ? 39  THR J CA  1 
ATOM   10401 C  C   . THR J  1 66  ? 20.449  71.660  -39.592 1.00 39.43 ? 39  THR J C   1 
ATOM   10402 O  O   . THR J  1 66  ? 20.447  71.452  -40.806 1.00 36.15 ? 39  THR J O   1 
ATOM   10403 C  CB  . THR J  1 66  ? 21.148  74.012  -39.125 1.00 36.46 ? 39  THR J CB  1 
ATOM   10404 O  OG1 . THR J  1 66  ? 21.012  74.316  -40.521 1.00 37.05 ? 39  THR J OG1 1 
ATOM   10405 C  CG2 . THR J  1 66  ? 22.229  74.910  -38.553 1.00 35.02 ? 39  THR J CG2 1 
ATOM   10406 N  N   . GLU J  1 67  ? 19.575  71.094  -38.760 1.00 35.83 ? 40  GLU J N   1 
ATOM   10407 C  CA  . GLU J  1 67  ? 18.391  70.350  -39.233 1.00 35.00 ? 40  GLU J CA  1 
ATOM   10408 C  C   . GLU J  1 67  ? 17.711  71.037  -40.429 1.00 33.65 ? 40  GLU J C   1 
ATOM   10409 O  O   . GLU J  1 67  ? 17.495  72.259  -40.442 1.00 35.49 ? 40  GLU J O   1 
ATOM   10410 C  CB  . GLU J  1 67  ? 17.388  70.212  -38.077 1.00 39.90 ? 40  GLU J CB  1 
ATOM   10411 C  CG  . GLU J  1 67  ? 16.189  69.312  -38.365 1.00 42.04 ? 40  GLU J CG  1 
ATOM   10412 C  CD  . GLU J  1 67  ? 15.270  69.175  -37.154 1.00 49.41 ? 40  GLU J CD  1 
ATOM   10413 O  OE1 . GLU J  1 67  ? 15.290  70.056  -36.275 1.00 47.66 ? 40  GLU J OE1 1 
ATOM   10414 O  OE2 . GLU J  1 67  ? 14.538  68.170  -37.069 1.00 52.06 ? 40  GLU J OE2 1 
ATOM   10415 N  N   . GLY J  1 68  ? 17.436  70.256  -41.467 1.00 34.63 ? 41  GLY J N   1 
ATOM   10416 C  CA  . GLY J  1 68  ? 16.676  70.757  -42.609 1.00 34.65 ? 41  GLY J CA  1 
ATOM   10417 C  C   . GLY J  1 68  ? 17.483  70.571  -43.881 1.00 36.80 ? 41  GLY J C   1 
ATOM   10418 O  O   . GLY J  1 68  ? 18.484  69.818  -43.900 1.00 32.92 ? 41  GLY J O   1 
ATOM   10419 N  N   . LEU J  1 69  ? 17.062  71.275  -44.923 1.00 36.18 ? 42  LEU J N   1 
ATOM   10420 C  CA  . LEU J  1 69  ? 17.565  71.049  -46.274 1.00 37.77 ? 42  LEU J CA  1 
ATOM   10421 C  C   . LEU J  1 69  ? 18.747  71.943  -46.574 1.00 36.23 ? 42  LEU J C   1 
ATOM   10422 O  O   . LEU J  1 69  ? 18.769  73.135  -46.236 1.00 34.72 ? 42  LEU J O   1 
ATOM   10423 C  CB  . LEU J  1 69  ? 16.482  71.330  -47.324 1.00 40.88 ? 42  LEU J CB  1 
ATOM   10424 C  CG  . LEU J  1 69  ? 15.204  70.496  -47.271 1.00 43.45 ? 42  LEU J CG  1 
ATOM   10425 C  CD1 . LEU J  1 69  ? 14.230  70.991  -48.323 1.00 48.89 ? 42  LEU J CD1 1 
ATOM   10426 C  CD2 . LEU J  1 69  ? 15.470  69.020  -47.476 1.00 43.46 ? 42  LEU J CD2 1 
ATOM   10427 N  N   . HIS J  1 70  ? 19.747  71.362  -47.238 1.00 36.47 ? 43  HIS J N   1 
ATOM   10428 C  CA  . HIS J  1 70  ? 20.903  72.178  -47.640 1.00 32.93 ? 43  HIS J CA  1 
ATOM   10429 C  C   . HIS J  1 70  ? 21.255  71.875  -49.073 1.00 28.36 ? 43  HIS J C   1 
ATOM   10430 O  O   . HIS J  1 70  ? 21.259  70.690  -49.455 1.00 30.52 ? 43  HIS J O   1 
ATOM   10431 C  CB  . HIS J  1 70  ? 22.090  71.822  -46.744 1.00 33.72 ? 43  HIS J CB  1 
ATOM   10432 C  CG  . HIS J  1 70  ? 21.890  72.205  -45.312 1.00 33.55 ? 43  HIS J CG  1 
ATOM   10433 N  ND1 . HIS J  1 70  ? 22.144  73.479  -44.850 1.00 33.62 ? 43  HIS J ND1 1 
ATOM   10434 C  CD2 . HIS J  1 70  ? 21.442  71.493  -44.251 1.00 33.06 ? 43  HIS J CD2 1 
ATOM   10435 C  CE1 . HIS J  1 70  ? 21.852  73.535  -43.561 1.00 33.11 ? 43  HIS J CE1 1 
ATOM   10436 N  NE2 . HIS J  1 70  ? 21.423  72.346  -43.174 1.00 34.64 ? 43  HIS J NE2 1 
ATOM   10437 N  N   . GLY J  1 71  ? 21.586  72.928  -49.814 1.00 31.45 ? 44  GLY J N   1 
ATOM   10438 C  CA  . GLY J  1 71  ? 21.955  72.799  -51.225 1.00 35.37 ? 44  GLY J CA  1 
ATOM   10439 C  C   . GLY J  1 71  ? 23.250  72.003  -51.363 1.00 37.83 ? 44  GLY J C   1 
ATOM   10440 O  O   . GLY J  1 71  ? 24.120  72.077  -50.487 1.00 31.38 ? 44  GLY J O   1 
ATOM   10441 N  N   . PHE J  1 72  ? 23.363  71.225  -52.448 1.00 33.11 ? 45  PHE J N   1 
ATOM   10442 C  CA  . PHE J  1 72  ? 24.417  70.244  -52.611 1.00 32.53 ? 45  PHE J CA  1 
ATOM   10443 C  C   . PHE J  1 72  ? 24.768  70.302  -54.082 1.00 35.25 ? 45  PHE J C   1 
ATOM   10444 O  O   . PHE J  1 72  ? 23.933  69.891  -54.923 1.00 35.01 ? 45  PHE J O   1 
ATOM   10445 C  CB  . PHE J  1 72  ? 23.842  68.887  -52.273 1.00 31.38 ? 45  PHE J CB  1 
ATOM   10446 C  CG  . PHE J  1 72  ? 24.850  67.793  -52.092 1.00 33.28 ? 45  PHE J CG  1 
ATOM   10447 C  CD1 . PHE J  1 72  ? 26.010  67.985  -51.371 1.00 33.98 ? 45  PHE J CD1 1 
ATOM   10448 C  CD2 . PHE J  1 72  ? 24.574  66.509  -52.577 1.00 32.96 ? 45  PHE J CD2 1 
ATOM   10449 C  CE1 . PHE J  1 72  ? 26.903  66.943  -51.173 1.00 32.51 ? 45  PHE J CE1 1 
ATOM   10450 C  CE2 . PHE J  1 72  ? 25.451  65.463  -52.384 1.00 33.80 ? 45  PHE J CE2 1 
ATOM   10451 C  CZ  . PHE J  1 72  ? 26.631  65.680  -51.672 1.00 36.15 ? 45  PHE J CZ  1 
ATOM   10452 N  N   . HIS J  1 73  ? 25.959  70.823  -54.390 1.00 32.82 ? 46  HIS J N   1 
ATOM   10453 C  CA  . HIS J  1 73  ? 26.413  71.054  -55.786 1.00 32.81 ? 46  HIS J CA  1 
ATOM   10454 C  C   . HIS J  1 73  ? 27.841  70.693  -56.097 1.00 33.92 ? 46  HIS J C   1 
ATOM   10455 O  O   . HIS J  1 73  ? 28.739  70.872  -55.277 1.00 31.36 ? 46  HIS J O   1 
ATOM   10456 C  CB  . HIS J  1 73  ? 26.273  72.519  -56.154 1.00 33.32 ? 46  HIS J CB  1 
ATOM   10457 C  CG  . HIS J  1 73  ? 24.866  72.998  -56.077 1.00 43.52 ? 46  HIS J CG  1 
ATOM   10458 N  ND1 . HIS J  1 73  ? 24.439  73.921  -55.144 1.00 45.76 ? 46  HIS J ND1 1 
ATOM   10459 C  CD2 . HIS J  1 73  ? 23.764  72.624  -56.777 1.00 46.78 ? 46  HIS J CD2 1 
ATOM   10460 C  CE1 . HIS J  1 73  ? 23.135  74.107  -55.283 1.00 43.31 ? 46  HIS J CE1 1 
ATOM   10461 N  NE2 . HIS J  1 73  ? 22.702  73.333  -56.264 1.00 49.65 ? 46  HIS J NE2 1 
ATOM   10462 N  N   . VAL J  1 74  ? 28.053  70.227  -57.319 1.00 32.29 ? 47  VAL J N   1 
ATOM   10463 C  CA  . VAL J  1 74  ? 29.408  70.213  -57.868 1.00 32.68 ? 47  VAL J CA  1 
ATOM   10464 C  C   . VAL J  1 74  ? 29.679  71.577  -58.423 1.00 27.73 ? 47  VAL J C   1 
ATOM   10465 O  O   . VAL J  1 74  ? 28.886  72.115  -59.195 1.00 33.45 ? 47  VAL J O   1 
ATOM   10466 C  CB  . VAL J  1 74  ? 29.578  69.150  -58.973 1.00 31.96 ? 47  VAL J CB  1 
ATOM   10467 C  CG1 . VAL J  1 74  ? 31.027  69.152  -59.477 1.00 30.22 ? 47  VAL J CG1 1 
ATOM   10468 C  CG2 . VAL J  1 74  ? 29.126  67.782  -58.456 1.00 31.67 ? 47  VAL J CG2 1 
ATOM   10469 N  N   . HIS J  1 75  ? 30.803  72.166  -58.038 1.00 27.84 ? 48  HIS J N   1 
ATOM   10470 C  CA  . HIS J  1 75  ? 31.213  73.453  -58.557 1.00 27.74 ? 48  HIS J CA  1 
ATOM   10471 C  C   . HIS J  1 75  ? 32.367  73.280  -59.512 1.00 28.17 ? 48  HIS J C   1 
ATOM   10472 O  O   . HIS J  1 75  ? 32.985  72.210  -59.561 1.00 30.05 ? 48  HIS J O   1 
ATOM   10473 C  CB  . HIS J  1 75  ? 31.596  74.445  -57.455 1.00 28.00 ? 48  HIS J CB  1 
ATOM   10474 C  CG  . HIS J  1 75  ? 30.424  74.934  -56.667 1.00 27.49 ? 48  HIS J CG  1 
ATOM   10475 N  ND1 . HIS J  1 75  ? 30.098  76.266  -56.577 1.00 28.78 ? 48  HIS J ND1 1 
ATOM   10476 C  CD2 . HIS J  1 75  ? 29.485  74.264  -55.960 1.00 29.17 ? 48  HIS J CD2 1 
ATOM   10477 C  CE1 . HIS J  1 75  ? 29.047  76.410  -55.790 1.00 28.57 ? 48  HIS J CE1 1 
ATOM   10478 N  NE2 . HIS J  1 75  ? 28.645  75.206  -55.409 1.00 33.23 ? 48  HIS J NE2 1 
ATOM   10479 N  N   . GLU J  1 76  ? 32.662  74.335  -60.250 1.00 28.49 ? 49  GLU J N   1 
ATOM   10480 C  CA  . GLU J  1 76  ? 33.541  74.171  -61.430 1.00 34.48 ? 49  GLU J CA  1 
ATOM   10481 C  C   . GLU J  1 76  ? 35.010  73.851  -61.124 1.00 33.23 ? 49  GLU J C   1 
ATOM   10482 O  O   . GLU J  1 76  ? 35.566  72.968  -61.731 1.00 33.29 ? 49  GLU J O   1 
ATOM   10483 C  CB  . GLU J  1 76  ? 33.438  75.348  -62.382 1.00 34.20 ? 49  GLU J CB  1 
ATOM   10484 C  CG  . GLU J  1 76  ? 34.063  75.066  -63.735 1.00 43.74 ? 49  GLU J CG  1 
ATOM   10485 C  CD  . GLU J  1 76  ? 34.050  76.275  -64.663 1.00 47.05 ? 49  GLU J CD  1 
ATOM   10486 O  OE1 . GLU J  1 76  ? 33.459  77.311  -64.296 1.00 45.84 ? 49  GLU J OE1 1 
ATOM   10487 O  OE2 . GLU J  1 76  ? 34.653  76.188  -65.755 1.00 49.54 ? 49  GLU J OE2 1 
ATOM   10488 N  N   . PHE J  1 77  ? 35.633  74.577  -60.206 1.00 34.25 ? 50  PHE J N   1 
ATOM   10489 C  CA  . PHE J  1 77  ? 37.052  74.353  -59.949 1.00 31.91 ? 50  PHE J CA  1 
ATOM   10490 C  C   . PHE J  1 77  ? 37.346  73.537  -58.703 1.00 35.35 ? 50  PHE J C   1 
ATOM   10491 O  O   . PHE J  1 77  ? 36.676  73.705  -57.659 1.00 29.96 ? 50  PHE J O   1 
ATOM   10492 C  CB  . PHE J  1 77  ? 37.792  75.671  -59.903 1.00 29.52 ? 50  PHE J CB  1 
ATOM   10493 C  CG  . PHE J  1 77  ? 37.387  76.606  -61.013 1.00 39.10 ? 50  PHE J CG  1 
ATOM   10494 C  CD1 . PHE J  1 77  ? 37.658  76.282  -62.345 1.00 42.07 ? 50  PHE J CD1 1 
ATOM   10495 C  CD2 . PHE J  1 77  ? 36.699  77.792  -60.736 1.00 42.17 ? 50  PHE J CD2 1 
ATOM   10496 C  CE1 . PHE J  1 77  ? 37.247  77.131  -63.384 1.00 43.44 ? 50  PHE J CE1 1 
ATOM   10497 C  CE2 . PHE J  1 77  ? 36.295  78.647  -61.767 1.00 46.81 ? 50  PHE J CE2 1 
ATOM   10498 C  CZ  . PHE J  1 77  ? 36.568  78.310  -63.091 1.00 42.87 ? 50  PHE J CZ  1 
ATOM   10499 N  N   . GLY J  1 78  ? 38.366  72.685  -58.814 1.00 29.84 ? 51  GLY J N   1 
ATOM   10500 C  CA  . GLY J  1 78  ? 38.886  71.924  -57.695 1.00 28.76 ? 51  GLY J CA  1 
ATOM   10501 C  C   . GLY J  1 78  ? 39.955  72.743  -56.974 1.00 30.52 ? 51  GLY J C   1 
ATOM   10502 O  O   . GLY J  1 78  ? 40.998  72.229  -56.637 1.00 30.50 ? 51  GLY J O   1 
ATOM   10503 N  N   . ASP J  1 79  ? 39.681  74.029  -56.781 1.00 30.67 ? 52  ASP J N   1 
ATOM   10504 C  CA  . ASP J  1 79  ? 40.621  74.971  -56.227 1.00 29.55 ? 52  ASP J CA  1 
ATOM   10505 C  C   . ASP J  1 79  ? 40.122  75.307  -54.816 1.00 31.47 ? 52  ASP J C   1 
ATOM   10506 O  O   . ASP J  1 79  ? 39.036  75.905  -54.655 1.00 32.49 ? 52  ASP J O   1 
ATOM   10507 C  CB  . ASP J  1 79  ? 40.670  76.209  -57.105 1.00 33.80 ? 52  ASP J CB  1 
ATOM   10508 C  CG  . ASP J  1 79  ? 41.693  77.240  -56.622 1.00 34.49 ? 52  ASP J CG  1 
ATOM   10509 O  OD1 . ASP J  1 79  ? 42.080  77.198  -55.437 1.00 34.96 ? 52  ASP J OD1 1 
ATOM   10510 O  OD2 . ASP J  1 79  ? 42.101  78.111  -57.411 1.00 34.46 ? 52  ASP J OD2 1 
ATOM   10511 N  N   . ASN J  1 80  ? 40.896  74.912  -53.798 1.00 28.98 ? 53  ASN J N   1 
ATOM   10512 C  CA  . ASN J  1 80  ? 40.513  75.195  -52.417 1.00 30.38 ? 53  ASN J CA  1 
ATOM   10513 C  C   . ASN J  1 80  ? 41.445  76.236  -51.804 1.00 28.97 ? 53  ASN J C   1 
ATOM   10514 O  O   . ASN J  1 80  ? 41.484  76.388  -50.590 1.00 30.28 ? 53  ASN J O   1 
ATOM   10515 C  CB  . ASN J  1 80  ? 40.462  73.909  -51.573 1.00 34.44 ? 53  ASN J CB  1 
ATOM   10516 C  CG  . ASN J  1 80  ? 39.737  74.115  -50.246 1.00 43.51 ? 53  ASN J CG  1 
ATOM   10517 O  OD1 . ASN J  1 80  ? 38.599  74.601  -50.215 1.00 42.74 ? 53  ASN J OD1 1 
ATOM   10518 N  ND2 . ASN J  1 80  ? 40.408  73.789  -49.132 1.00 45.42 ? 53  ASN J ND2 1 
ATOM   10519 N  N   . THR J  1 81  ? 42.194  76.960  -52.625 1.00 27.87 ? 54  THR J N   1 
ATOM   10520 C  CA  . THR J  1 81  ? 43.194  77.886  -52.078 1.00 29.87 ? 54  THR J CA  1 
ATOM   10521 C  C   . THR J  1 81  ? 42.611  79.005  -51.188 1.00 31.45 ? 54  THR J C   1 
ATOM   10522 O  O   . THR J  1 81  ? 43.253  79.404  -50.244 1.00 35.25 ? 54  THR J O   1 
ATOM   10523 C  CB  . THR J  1 81  ? 44.087  78.542  -53.144 1.00 32.09 ? 54  THR J CB  1 
ATOM   10524 O  OG1 . THR J  1 81  ? 43.270  79.283  -54.037 1.00 34.93 ? 54  THR J OG1 1 
ATOM   10525 C  CG2 . THR J  1 81  ? 44.841  77.493  -53.931 1.00 29.63 ? 54  THR J CG2 1 
ATOM   10526 N  N   . ALA J  1 82  ? 41.421  79.510  -51.475 1.00 28.58 ? 55  ALA J N   1 
ATOM   10527 C  CA  . ALA J  1 82  ? 40.771  80.461  -50.535 1.00 32.94 ? 55  ALA J CA  1 
ATOM   10528 C  C   . ALA J  1 82  ? 39.545  79.806  -49.934 1.00 34.02 ? 55  ALA J C   1 
ATOM   10529 O  O   . ALA J  1 82  ? 38.471  80.385  -49.914 1.00 40.19 ? 55  ALA J O   1 
ATOM   10530 C  CB  . ALA J  1 82  ? 40.394  81.765  -51.236 1.00 32.96 ? 55  ALA J CB  1 
ATOM   10531 N  N   . GLY J  1 83  ? 39.676  78.559  -49.511 1.00 32.93 ? 56  GLY J N   1 
ATOM   10532 C  CA  . GLY J  1 83  ? 38.514  77.863  -48.977 1.00 30.46 ? 56  GLY J CA  1 
ATOM   10533 C  C   . GLY J  1 83  ? 37.492  77.615  -50.056 1.00 31.44 ? 56  GLY J C   1 
ATOM   10534 O  O   . GLY J  1 83  ? 37.830  77.493  -51.225 1.00 28.76 ? 56  GLY J O   1 
ATOM   10535 N  N   . CYS J  1 84  ? 36.226  77.535  -49.667 1.00 31.33 ? 57  CYS J N   1 
ATOM   10536 C  CA  . CYS J  1 84  ? 35.202  77.049  -50.591 1.00 35.12 ? 57  CYS J CA  1 
ATOM   10537 C  C   . CYS J  1 84  ? 34.901  78.066  -51.695 1.00 35.18 ? 57  CYS J C   1 
ATOM   10538 O  O   . CYS J  1 84  ? 34.366  77.710  -52.761 1.00 35.54 ? 57  CYS J O   1 
ATOM   10539 C  CB  . CYS J  1 84  ? 33.949  76.623  -49.826 1.00 33.66 ? 57  CYS J CB  1 
ATOM   10540 S  SG  . CYS J  1 84  ? 34.248  75.144  -48.801 1.00 41.31 ? 57  CYS J SG  1 
ATOM   10541 N  N   . THR J  1 85  ? 35.271  79.315  -51.425 1.00 34.78 ? 58  THR J N   1 
ATOM   10542 C  CA  . THR J  1 85  ? 35.090  80.429  -52.362 1.00 38.01 ? 58  THR J CA  1 
ATOM   10543 C  C   . THR J  1 85  ? 35.772  80.186  -53.676 1.00 37.88 ? 58  THR J C   1 
ATOM   10544 O  O   . THR J  1 85  ? 35.227  80.539  -54.704 1.00 34.49 ? 58  THR J O   1 
ATOM   10545 C  CB  . THR J  1 85  ? 35.632  81.765  -51.795 1.00 37.42 ? 58  THR J CB  1 
ATOM   10546 O  OG1 . THR J  1 85  ? 34.865  82.101  -50.652 1.00 43.31 ? 58  THR J OG1 1 
ATOM   10547 C  CG2 . THR J  1 85  ? 35.471  82.931  -52.783 1.00 43.36 ? 58  THR J CG2 1 
ATOM   10548 N  N   . SER J  1 86  ? 36.982  79.629  -53.658 1.00 33.60 ? 59  SER J N   1 
ATOM   10549 C  CA  . SER J  1 86  ? 37.684  79.460  -54.920 1.00 32.87 ? 59  SER J CA  1 
ATOM   10550 C  C   . SER J  1 86  ? 37.224  78.287  -55.786 1.00 29.54 ? 59  SER J C   1 
ATOM   10551 O  O   . SER J  1 86  ? 37.785  78.069  -56.848 1.00 34.32 ? 59  SER J O   1 
ATOM   10552 C  CB  . SER J  1 86  ? 39.219  79.494  -54.748 1.00 34.83 ? 59  SER J CB  1 
ATOM   10553 O  OG  . SER J  1 86  ? 39.571  78.998  -53.503 1.00 31.08 ? 59  SER J OG  1 
ATOM   10554 N  N   . ALA J  1 87  ? 36.213  77.534  -55.370 1.00 28.55 ? 60  ALA J N   1 
ATOM   10555 C  CA  . ALA J  1 87  ? 35.678  76.515  -56.238 1.00 27.82 ? 60  ALA J CA  1 
ATOM   10556 C  C   . ALA J  1 87  ? 34.864  77.106  -57.415 1.00 29.88 ? 60  ALA J C   1 
ATOM   10557 O  O   . ALA J  1 87  ? 34.514  76.368  -58.325 1.00 31.06 ? 60  ALA J O   1 
ATOM   10558 C  CB  . ALA J  1 87  ? 34.861  75.504  -55.469 1.00 28.05 ? 60  ALA J CB  1 
ATOM   10559 N  N   . GLY J  1 88  ? 34.621  78.417  -57.379 1.00 30.78 ? 61  GLY J N   1 
ATOM   10560 C  CA  . GLY J  1 88  ? 33.902  79.155  -58.422 1.00 33.31 ? 61  GLY J CA  1 
ATOM   10561 C  C   . GLY J  1 88  ? 32.425  78.823  -58.478 1.00 35.93 ? 61  GLY J C   1 
ATOM   10562 O  O   . GLY J  1 88  ? 31.838  78.370  -57.492 1.00 34.30 ? 61  GLY J O   1 
ATOM   10563 N  N   . PRO J  1 89  ? 31.805  78.999  -59.665 1.00 42.32 ? 62  PRO J N   1 
ATOM   10564 C  CA  . PRO J  1 89  ? 30.368  78.808  -59.780 1.00 38.99 ? 62  PRO J CA  1 
ATOM   10565 C  C   . PRO J  1 89  ? 29.964  77.340  -59.972 1.00 39.99 ? 62  PRO J C   1 
ATOM   10566 O  O   . PRO J  1 89  ? 30.828  76.465  -60.084 1.00 40.34 ? 62  PRO J O   1 
ATOM   10567 C  CB  . PRO J  1 89  ? 30.029  79.655  -60.993 1.00 40.64 ? 62  PRO J CB  1 
ATOM   10568 C  CG  . PRO J  1 89  ? 31.224  79.533  -61.866 1.00 43.66 ? 62  PRO J CG  1 
ATOM   10569 C  CD  . PRO J  1 89  ? 32.417  79.354  -60.960 1.00 42.37 ? 62  PRO J CD  1 
ATOM   10570 N  N   . HIS J  1 90  ? 28.657  77.066  -60.016 1.00 38.84 ? 63  HIS J N   1 
ATOM   10571 C  CA  . HIS J  1 90  ? 28.141  75.709  -60.263 1.00 38.79 ? 63  HIS J CA  1 
ATOM   10572 C  C   . HIS J  1 90  ? 28.752  75.149  -61.550 1.00 39.35 ? 63  HIS J C   1 
ATOM   10573 O  O   . HIS J  1 90  ? 28.988  75.889  -62.487 1.00 41.14 ? 63  HIS J O   1 
ATOM   10574 C  CB  . HIS J  1 90  ? 26.603  75.715  -60.389 1.00 44.54 ? 63  HIS J CB  1 
ATOM   10575 C  CG  . HIS J  1 90  ? 25.879  76.068  -59.120 1.00 46.86 ? 63  HIS J CG  1 
ATOM   10576 N  ND1 . HIS J  1 90  ? 24.504  76.009  -59.010 1.00 48.20 ? 63  HIS J ND1 1 
ATOM   10577 C  CD2 . HIS J  1 90  ? 26.338  76.478  -57.911 1.00 47.08 ? 63  HIS J CD2 1 
ATOM   10578 C  CE1 . HIS J  1 90  ? 24.151  76.374  -57.789 1.00 52.67 ? 63  HIS J CE1 1 
ATOM   10579 N  NE2 . HIS J  1 90  ? 25.245  76.666  -57.104 1.00 48.85 ? 63  HIS J NE2 1 
ATOM   10580 N  N   . PHE J  1 91  ? 29.017  73.849  -61.592 1.00 38.97 ? 64  PHE J N   1 
ATOM   10581 C  CA  . PHE J  1 91  ? 29.639  73.251  -62.776 1.00 39.92 ? 64  PHE J CA  1 
ATOM   10582 C  C   . PHE J  1 91  ? 28.593  73.201  -63.915 1.00 41.33 ? 64  PHE J C   1 
ATOM   10583 O  O   . PHE J  1 91  ? 27.559  72.531  -63.760 1.00 36.77 ? 64  PHE J O   1 
ATOM   10584 C  CB  . PHE J  1 91  ? 30.113  71.828  -62.449 1.00 37.57 ? 64  PHE J CB  1 
ATOM   10585 C  CG  . PHE J  1 91  ? 30.745  71.124  -63.609 1.00 36.93 ? 64  PHE J CG  1 
ATOM   10586 C  CD1 . PHE J  1 91  ? 31.599  71.809  -64.472 1.00 40.13 ? 64  PHE J CD1 1 
ATOM   10587 C  CD2 . PHE J  1 91  ? 30.479  69.791  -63.842 1.00 38.22 ? 64  PHE J CD2 1 
ATOM   10588 C  CE1 . PHE J  1 91  ? 32.179  71.162  -65.551 1.00 41.63 ? 64  PHE J CE1 1 
ATOM   10589 C  CE2 . PHE J  1 91  ? 31.059  69.134  -64.918 1.00 40.16 ? 64  PHE J CE2 1 
ATOM   10590 C  CZ  . PHE J  1 91  ? 31.917  69.820  -65.760 1.00 38.69 ? 64  PHE J CZ  1 
ATOM   10591 N  N   . ASN J  1 92  ? 28.878  73.889  -65.026 1.00 43.32 ? 65  ASN J N   1 
ATOM   10592 C  CA  . ASN J  1 92  ? 27.862  74.090  -66.096 1.00 58.29 ? 65  ASN J CA  1 
ATOM   10593 C  C   . ASN J  1 92  ? 28.360  73.992  -67.527 1.00 65.51 ? 65  ASN J C   1 
ATOM   10594 O  O   . ASN J  1 92  ? 28.289  74.989  -68.261 1.00 74.08 ? 65  ASN J O   1 
ATOM   10595 C  CB  . ASN J  1 92  ? 27.138  75.438  -65.931 1.00 49.54 ? 65  ASN J CB  1 
ATOM   10596 C  CG  . ASN J  1 92  ? 25.811  75.495  -66.671 1.00 54.92 ? 65  ASN J CG  1 
ATOM   10597 O  OD1 . ASN J  1 92  ? 25.152  76.522  -66.653 1.00 53.03 ? 65  ASN J OD1 1 
ATOM   10598 N  ND2 . ASN J  1 92  ? 25.408  74.400  -67.314 1.00 59.25 ? 65  ASN J ND2 1 
ATOM   10599 N  N   . PRO J  1 93  ? 28.813  72.795  -67.960 1.00 71.25 ? 66  PRO J N   1 
ATOM   10600 C  CA  . PRO J  1 93  ? 29.432  72.722  -69.301 1.00 74.24 ? 66  PRO J CA  1 
ATOM   10601 C  C   . PRO J  1 93  ? 28.434  73.050  -70.451 1.00 76.97 ? 66  PRO J C   1 
ATOM   10602 O  O   . PRO J  1 93  ? 28.290  72.284  -71.419 1.00 74.30 ? 66  PRO J O   1 
ATOM   10603 C  CB  . PRO J  1 93  ? 29.973  71.274  -69.360 1.00 70.82 ? 66  PRO J CB  1 
ATOM   10604 C  CG  . PRO J  1 93  ? 29.064  70.508  -68.451 1.00 64.34 ? 66  PRO J CG  1 
ATOM   10605 C  CD  . PRO J  1 93  ? 28.693  71.461  -67.332 1.00 65.15 ? 66  PRO J CD  1 
ATOM   10606 N  N   . ARG J  1 106 ? 18.672  72.970  -64.989 1.00 64.44 ? 79  ARG J N   1 
ATOM   10607 C  CA  . ARG J  1 106 ? 19.657  72.708  -63.962 1.00 57.03 ? 79  ARG J CA  1 
ATOM   10608 C  C   . ARG J  1 106 ? 21.088  73.076  -64.440 1.00 59.48 ? 79  ARG J C   1 
ATOM   10609 O  O   . ARG J  1 106 ? 21.273  73.952  -65.286 1.00 60.94 ? 79  ARG J O   1 
ATOM   10610 C  CB  . ARG J  1 106 ? 19.532  71.242  -63.466 1.00 60.31 ? 79  ARG J CB  1 
ATOM   10611 C  CG  . ARG J  1 106 ? 19.601  70.148  -64.543 1.00 61.07 ? 79  ARG J CG  1 
ATOM   10612 C  CD  . ARG J  1 106 ? 19.733  68.743  -63.936 1.00 62.14 ? 79  ARG J CD  1 
ATOM   10613 N  NE  . ARG J  1 106 ? 21.067  68.471  -63.368 1.00 62.73 ? 79  ARG J NE  1 
ATOM   10614 C  CZ  . ARG J  1 106 ? 21.399  67.390  -62.643 1.00 64.22 ? 79  ARG J CZ  1 
ATOM   10615 N  NH1 . ARG J  1 106 ? 20.491  66.446  -62.376 1.00 63.36 ? 79  ARG J NH1 1 
ATOM   10616 N  NH2 . ARG J  1 106 ? 22.652  67.236  -62.177 1.00 55.31 ? 79  ARG J NH2 1 
ATOM   10617 N  N   . HIS J  1 107 ? 22.095  72.453  -63.834 1.00 57.11 ? 80  HIS J N   1 
ATOM   10618 C  CA  . HIS J  1 107 ? 23.482  72.497  -64.295 1.00 53.46 ? 80  HIS J CA  1 
ATOM   10619 C  C   . HIS J  1 107 ? 23.930  71.080  -64.049 1.00 48.15 ? 80  HIS J C   1 
ATOM   10620 O  O   . HIS J  1 107 ? 23.183  70.296  -63.437 1.00 48.80 ? 80  HIS J O   1 
ATOM   10621 C  CB  . HIS J  1 107 ? 24.323  73.512  -63.493 1.00 58.32 ? 80  HIS J CB  1 
ATOM   10622 C  CG  . HIS J  1 107 ? 24.199  73.371  -61.998 1.00 66.01 ? 80  HIS J CG  1 
ATOM   10623 N  ND1 . HIS J  1 107 ? 25.094  72.642  -61.236 1.00 72.46 ? 80  HIS J ND1 1 
ATOM   10624 C  CD2 . HIS J  1 107 ? 23.287  73.874  -61.126 1.00 69.18 ? 80  HIS J CD2 1 
ATOM   10625 C  CE1 . HIS J  1 107 ? 24.736  72.701  -59.964 1.00 67.46 ? 80  HIS J CE1 1 
ATOM   10626 N  NE2 . HIS J  1 107 ? 23.636  73.430  -59.874 1.00 67.39 ? 80  HIS J NE2 1 
ATOM   10627 N  N   . VAL J  1 108 ? 25.123  70.725  -64.508 1.00 47.89 ? 81  VAL J N   1 
ATOM   10628 C  CA  . VAL J  1 108 ? 25.590  69.365  -64.328 1.00 44.60 ? 81  VAL J CA  1 
ATOM   10629 C  C   . VAL J  1 108 ? 25.817  69.069  -62.824 1.00 49.60 ? 81  VAL J C   1 
ATOM   10630 O  O   . VAL J  1 108 ? 25.353  68.031  -62.310 1.00 47.74 ? 81  VAL J O   1 
ATOM   10631 C  CB  . VAL J  1 108 ? 26.798  69.050  -65.245 1.00 46.45 ? 81  VAL J CB  1 
ATOM   10632 C  CG1 . VAL J  1 108 ? 27.407  67.693  -64.910 1.00 41.94 ? 81  VAL J CG1 1 
ATOM   10633 C  CG2 . VAL J  1 108 ? 26.340  69.059  -66.704 1.00 46.10 ? 81  VAL J CG2 1 
ATOM   10634 N  N   . GLY J  1 109 ? 26.455  70.000  -62.113 1.00 52.48 ? 82  GLY J N   1 
ATOM   10635 C  CA  . GLY J  1 109 ? 26.578  69.901  -60.623 1.00 61.67 ? 82  GLY J CA  1 
ATOM   10636 C  C   . GLY J  1 109 ? 25.378  69.594  -59.692 1.00 55.72 ? 82  GLY J C   1 
ATOM   10637 O  O   . GLY J  1 109 ? 25.562  69.076  -58.589 1.00 47.64 ? 82  GLY J O   1 
ATOM   10638 N  N   . ASP J  1 110 ? 24.156  69.859  -60.151 1.00 52.53 ? 83  ASP J N   1 
ATOM   10639 C  CA  . ASP J  1 110 ? 22.966  69.967  -59.289 1.00 50.26 ? 83  ASP J CA  1 
ATOM   10640 C  C   . ASP J  1 110 ? 22.467  68.660  -58.697 1.00 50.67 ? 83  ASP J C   1 
ATOM   10641 O  O   . ASP J  1 110 ? 21.789  67.880  -59.366 1.00 52.39 ? 83  ASP J O   1 
ATOM   10642 C  CB  . ASP J  1 110 ? 21.846  70.593  -60.104 1.00 58.94 ? 83  ASP J CB  1 
ATOM   10643 C  CG  . ASP J  1 110 ? 20.852  71.344  -59.253 1.00 74.03 ? 83  ASP J CG  1 
ATOM   10644 O  OD1 . ASP J  1 110 ? 20.663  70.991  -58.051 1.00 75.61 ? 83  ASP J OD1 1 
ATOM   10645 O  OD2 . ASP J  1 110 ? 20.262  72.304  -59.809 1.00 74.96 ? 83  ASP J OD2 1 
ATOM   10646 N  N   . LEU J  1 111 ? 22.761  68.424  -57.426 1.00 39.49 ? 84  LEU J N   1 
ATOM   10647 C  CA  . LEU J  1 111 ? 22.325  67.210  -56.795 1.00 42.64 ? 84  LEU J CA  1 
ATOM   10648 C  C   . LEU J  1 111 ? 21.191  67.482  -55.821 1.00 44.22 ? 84  LEU J C   1 
ATOM   10649 O  O   . LEU J  1 111 ? 20.873  66.639  -54.979 1.00 48.54 ? 84  LEU J O   1 
ATOM   10650 C  CB  . LEU J  1 111 ? 23.492  66.555  -56.073 1.00 42.71 ? 84  LEU J CB  1 
ATOM   10651 C  CG  . LEU J  1 111 ? 24.471  65.674  -56.857 1.00 52.35 ? 84  LEU J CG  1 
ATOM   10652 C  CD1 . LEU J  1 111 ? 24.315  65.742  -58.376 1.00 52.51 ? 84  LEU J CD1 1 
ATOM   10653 C  CD2 . LEU J  1 111 ? 25.880  66.030  -56.421 1.00 46.57 ? 84  LEU J CD2 1 
ATOM   10654 N  N   . GLY J  1 112 ? 20.625  68.681  -55.921 1.00 44.35 ? 85  GLY J N   1 
ATOM   10655 C  CA  . GLY J  1 112 ? 19.459  69.049  -55.153 1.00 46.65 ? 85  GLY J CA  1 
ATOM   10656 C  C   . GLY J  1 112 ? 19.813  69.423  -53.733 1.00 48.24 ? 85  GLY J C   1 
ATOM   10657 O  O   . GLY J  1 112 ? 20.665  70.279  -53.506 1.00 51.03 ? 85  GLY J O   1 
ATOM   10658 N  N   . ASN J  1 113 ? 19.143  68.765  -52.796 1.00 46.97 ? 86  ASN J N   1 
ATOM   10659 C  CA  . ASN J  1 113 ? 19.237  69.082  -51.382 1.00 43.18 ? 86  ASN J CA  1 
ATOM   10660 C  C   . ASN J  1 113 ? 19.532  67.838  -50.606 1.00 41.01 ? 86  ASN J C   1 
ATOM   10661 O  O   . ASN J  1 113 ? 18.946  66.762  -50.834 1.00 38.68 ? 86  ASN J O   1 
ATOM   10662 C  CB  . ASN J  1 113 ? 17.914  69.660  -50.868 1.00 47.23 ? 86  ASN J CB  1 
ATOM   10663 C  CG  . ASN J  1 113 ? 17.714  71.117  -51.240 1.00 48.72 ? 86  ASN J CG  1 
ATOM   10664 O  OD1 . ASN J  1 113 ? 18.646  71.913  -51.252 1.00 50.32 ? 86  ASN J OD1 1 
ATOM   10665 N  ND2 . ASN J  1 113 ? 16.469  71.478  -51.521 1.00 51.19 ? 86  ASN J ND2 1 
ATOM   10666 N  N   . VAL J  1 114 ? 20.439  67.977  -49.656 1.00 36.70 ? 87  VAL J N   1 
ATOM   10667 C  CA  . VAL J  1 114 ? 20.571  66.965  -48.677 1.00 34.76 ? 87  VAL J CA  1 
ATOM   10668 C  C   . VAL J  1 114 ? 19.691  67.416  -47.510 1.00 34.47 ? 87  VAL J C   1 
ATOM   10669 O  O   . VAL J  1 114 ? 19.383  68.597  -47.352 1.00 36.47 ? 87  VAL J O   1 
ATOM   10670 C  CB  . VAL J  1 114 ? 22.045  66.755  -48.218 1.00 38.42 ? 87  VAL J CB  1 
ATOM   10671 C  CG1 . VAL J  1 114 ? 22.912  66.306  -49.393 1.00 38.67 ? 87  VAL J CG1 1 
ATOM   10672 C  CG2 . VAL J  1 114 ? 22.608  68.035  -47.608 1.00 35.56 ? 87  VAL J CG2 1 
ATOM   10673 N  N   . THR J  1 115 ? 19.319  66.444  -46.700 1.00 36.08 ? 88  THR J N   1 
ATOM   10674 C  CA  . THR J  1 115 ? 18.405  66.674  -45.612 1.00 38.73 ? 88  THR J CA  1 
ATOM   10675 C  C   . THR J  1 115 ? 19.060  66.195  -44.347 1.00 33.90 ? 88  THR J C   1 
ATOM   10676 O  O   . THR J  1 115 ? 19.275  64.978  -44.157 1.00 30.75 ? 88  THR J O   1 
ATOM   10677 C  CB  . THR J  1 115 ? 17.062  65.933  -45.868 1.00 39.71 ? 88  THR J CB  1 
ATOM   10678 O  OG1 . THR J  1 115 ? 16.457  66.515  -47.031 1.00 42.16 ? 88  THR J OG1 1 
ATOM   10679 C  CG2 . THR J  1 115 ? 16.097  66.056  -44.661 1.00 36.97 ? 88  THR J CG2 1 
ATOM   10680 N  N   . ALA J  1 116 ? 19.380  67.161  -43.483 1.00 33.42 ? 89  ALA J N   1 
ATOM   10681 C  CA  . ALA J  1 116 ? 19.941  66.826  -42.175 1.00 33.57 ? 89  ALA J CA  1 
ATOM   10682 C  C   . ALA J  1 116 ? 18.838  66.561  -41.126 1.00 34.18 ? 89  ALA J C   1 
ATOM   10683 O  O   . ALA J  1 116 ? 17.890  67.319  -40.996 1.00 34.15 ? 89  ALA J O   1 
ATOM   10684 C  CB  . ALA J  1 116 ? 20.887  67.907  -41.700 1.00 33.11 ? 89  ALA J CB  1 
ATOM   10685 N  N   . ASP J  1 117 ? 18.997  65.473  -40.391 1.00 32.26 ? 90  ASP J N   1 
ATOM   10686 C  CA  . ASP J  1 117 ? 18.059  65.124  -39.361 1.00 35.84 ? 90  ASP J CA  1 
ATOM   10687 C  C   . ASP J  1 117 ? 18.246  66.044  -38.127 1.00 36.46 ? 90  ASP J C   1 
ATOM   10688 O  O   . ASP J  1 117 ? 18.972  67.066  -38.181 1.00 32.22 ? 90  ASP J O   1 
ATOM   10689 C  CB  . ASP J  1 117 ? 18.178  63.633  -39.036 1.00 33.11 ? 90  ASP J CB  1 
ATOM   10690 C  CG  . ASP J  1 117 ? 19.494  63.253  -38.324 1.00 38.34 ? 90  ASP J CG  1 
ATOM   10691 O  OD1 . ASP J  1 117 ? 20.271  64.134  -37.850 1.00 36.83 ? 90  ASP J OD1 1 
ATOM   10692 O  OD2 . ASP J  1 117 ? 19.752  62.047  -38.191 1.00 38.18 ? 90  ASP J OD2 1 
ATOM   10693 N  N   . LYS J  1 118 ? 17.566  65.706  -37.039 1.00 36.53 ? 91  LYS J N   1 
ATOM   10694 C  CA  . LYS J  1 118 ? 17.539  66.593  -35.876 1.00 36.91 ? 91  LYS J CA  1 
ATOM   10695 C  C   . LYS J  1 118 ? 18.891  66.577  -35.177 1.00 35.01 ? 91  LYS J C   1 
ATOM   10696 O  O   . LYS J  1 118 ? 19.173  67.474  -34.383 1.00 36.27 ? 91  LYS J O   1 
ATOM   10697 C  CB  . LYS J  1 118 ? 16.430  66.163  -34.901 1.00 38.26 ? 91  LYS J CB  1 
ATOM   10698 C  CG  . LYS J  1 118 ? 16.762  64.868  -34.211 1.00 41.17 ? 91  LYS J CG  1 
ATOM   10699 C  CD  . LYS J  1 118 ? 15.551  64.272  -33.521 1.00 52.88 ? 91  LYS J CD  1 
ATOM   10700 C  CE  . LYS J  1 118 ? 15.839  62.807  -33.211 1.00 57.58 ? 91  LYS J CE  1 
ATOM   10701 N  NZ  . LYS J  1 118 ? 16.874  62.678  -32.142 1.00 57.29 ? 91  LYS J NZ  1 
ATOM   10702 N  N   . ASP J  1 119 ? 19.711  65.551  -35.465 1.00 35.00 ? 92  ASP J N   1 
ATOM   10703 C  CA  . ASP J  1 119 ? 21.097  65.461  -34.936 1.00 35.83 ? 92  ASP J CA  1 
ATOM   10704 C  C   . ASP J  1 119 ? 22.142  66.059  -35.880 1.00 33.74 ? 92  ASP J C   1 
ATOM   10705 O  O   . ASP J  1 119 ? 23.341  65.864  -35.652 1.00 33.73 ? 92  ASP J O   1 
ATOM   10706 C  CB  . ASP J  1 119 ? 21.501  64.030  -34.648 1.00 35.23 ? 92  ASP J CB  1 
ATOM   10707 C  CG  . ASP J  1 119 ? 20.569  63.355  -33.657 1.00 48.67 ? 92  ASP J CG  1 
ATOM   10708 O  OD1 . ASP J  1 119 ? 20.321  63.920  -32.571 1.00 48.99 ? 92  ASP J OD1 1 
ATOM   10709 O  OD2 . ASP J  1 119 ? 20.085  62.250  -33.964 1.00 56.53 ? 92  ASP J OD2 1 
ATOM   10710 N  N   . GLY J  1 120 ? 21.677  66.765  -36.908 1.00 32.57 ? 93  GLY J N   1 
ATOM   10711 C  CA  . GLY J  1 120 ? 22.515  67.465  -37.880 1.00 31.23 ? 93  GLY J CA  1 
ATOM   10712 C  C   . GLY J  1 120 ? 23.271  66.569  -38.862 1.00 33.53 ? 93  GLY J C   1 
ATOM   10713 O  O   . GLY J  1 120 ? 24.263  67.024  -39.451 1.00 33.20 ? 93  GLY J O   1 
ATOM   10714 N  N   . VAL J  1 121 ? 22.824  65.314  -39.028 1.00 32.62 ? 94  VAL J N   1 
ATOM   10715 C  CA  . VAL J  1 121 ? 23.457  64.348  -39.957 1.00 31.38 ? 94  VAL J CA  1 
ATOM   10716 C  C   . VAL J  1 121 ? 22.552  64.207  -41.190 1.00 37.08 ? 94  VAL J C   1 
ATOM   10717 O  O   . VAL J  1 121 ? 21.325  63.974  -41.069 1.00 34.03 ? 94  VAL J O   1 
ATOM   10718 C  CB  . VAL J  1 121 ? 23.675  62.965  -39.300 1.00 33.44 ? 94  VAL J CB  1 
ATOM   10719 C  CG1 . VAL J  1 121 ? 24.191  61.902  -40.309 1.00 31.72 ? 94  VAL J CG1 1 
ATOM   10720 C  CG2 . VAL J  1 121 ? 24.616  63.085  -38.097 1.00 33.86 ? 94  VAL J CG2 1 
ATOM   10721 N  N   . ALA J  1 122 ? 23.138  64.402  -42.369 1.00 34.01 ? 95  ALA J N   1 
ATOM   10722 C  CA  . ALA J  1 122 ? 22.435  64.165  -43.624 1.00 36.03 ? 95  ALA J CA  1 
ATOM   10723 C  C   . ALA J  1 122 ? 22.969  62.861  -44.179 1.00 38.58 ? 95  ALA J C   1 
ATOM   10724 O  O   . ALA J  1 122 ? 24.175  62.750  -44.458 1.00 35.58 ? 95  ALA J O   1 
ATOM   10725 C  CB  . ALA J  1 122 ? 22.676  65.297  -44.584 1.00 34.67 ? 95  ALA J CB  1 
ATOM   10726 N  N   . ASP J  1 123 ? 22.107  61.858  -44.299 1.00 39.24 ? 96  ASP J N   1 
ATOM   10727 C  CA  . ASP J  1 123 ? 22.501  60.636  -45.034 1.00 44.20 ? 96  ASP J CA  1 
ATOM   10728 C  C   . ASP J  1 123 ? 22.216  60.815  -46.530 1.00 42.27 ? 96  ASP J C   1 
ATOM   10729 O  O   . ASP J  1 123 ? 21.159  61.273  -46.916 1.00 41.91 ? 96  ASP J O   1 
ATOM   10730 C  CB  . ASP J  1 123 ? 21.878  59.375  -44.457 1.00 46.37 ? 96  ASP J CB  1 
ATOM   10731 C  CG  . ASP J  1 123 ? 22.519  58.962  -43.126 1.00 58.62 ? 96  ASP J CG  1 
ATOM   10732 O  OD1 . ASP J  1 123 ? 23.741  59.245  -42.869 1.00 52.29 ? 96  ASP J OD1 1 
ATOM   10733 O  OD2 . ASP J  1 123 ? 21.788  58.335  -42.322 1.00 65.14 ? 96  ASP J OD2 1 
ATOM   10734 N  N   . VAL J  1 124 ? 23.200  60.519  -47.376 1.00 40.40 ? 97  VAL J N   1 
ATOM   10735 C  CA  . VAL J  1 124 ? 23.050  60.793  -48.815 1.00 39.81 ? 97  VAL J CA  1 
ATOM   10736 C  C   . VAL J  1 124 ? 22.992  59.455  -49.534 1.00 40.14 ? 97  VAL J C   1 
ATOM   10737 O  O   . VAL J  1 124 ? 23.829  58.585  -49.303 1.00 40.04 ? 97  VAL J O   1 
ATOM   10738 C  CB  . VAL J  1 124 ? 24.208  61.668  -49.364 1.00 39.98 ? 97  VAL J CB  1 
ATOM   10739 C  CG1 . VAL J  1 124 ? 24.098  61.859  -50.874 1.00 38.33 ? 97  VAL J CG1 1 
ATOM   10740 C  CG2 . VAL J  1 124 ? 24.220  63.015  -48.668 1.00 42.92 ? 97  VAL J CG2 1 
ATOM   10741 N  N   . SER J  1 125 ? 21.968  59.264  -50.357 1.00 41.99 ? 98  SER J N   1 
ATOM   10742 C  CA  . SER J  1 125 ? 21.902  58.092  -51.218 1.00 48.63 ? 98  SER J CA  1 
ATOM   10743 C  C   . SER J  1 125 ? 21.065  58.464  -52.421 1.00 50.15 ? 98  SER J C   1 
ATOM   10744 O  O   . SER J  1 125 ? 19.847  58.463  -52.333 1.00 52.74 ? 98  SER J O   1 
ATOM   10745 C  CB  . SER J  1 125 ? 21.297  56.901  -50.483 1.00 52.85 ? 98  SER J CB  1 
ATOM   10746 O  OG  . SER J  1 125 ? 21.333  55.745  -51.303 1.00 57.90 ? 98  SER J OG  1 
ATOM   10747 N  N   . ILE J  1 126 ? 21.720  58.861  -53.512 1.00 46.87 ? 99  ILE J N   1 
ATOM   10748 C  CA  . ILE J  1 126 ? 21.025  59.270  -54.726 1.00 46.62 ? 99  ILE J CA  1 
ATOM   10749 C  C   . ILE J  1 126 ? 21.659  58.676  -55.983 1.00 45.67 ? 99  ILE J C   1 
ATOM   10750 O  O   . ILE J  1 126 ? 22.738  58.083  -55.924 1.00 47.61 ? 99  ILE J O   1 
ATOM   10751 C  CB  . ILE J  1 126 ? 20.957  60.802  -54.905 1.00 48.21 ? 99  ILE J CB  1 
ATOM   10752 C  CG1 . ILE J  1 126 ? 22.336  61.366  -55.210 1.00 42.78 ? 99  ILE J CG1 1 
ATOM   10753 C  CG2 . ILE J  1 126 ? 20.273  61.497  -53.719 1.00 48.60 ? 99  ILE J CG2 1 
ATOM   10754 C  CD1 . ILE J  1 126 ? 22.381  62.866  -55.171 1.00 48.15 ? 99  ILE J CD1 1 
ATOM   10755 N  N   . GLU J  1 127 ? 20.967  58.860  -57.110 1.00 49.28 ? 100 GLU J N   1 
ATOM   10756 C  CA  . GLU J  1 127 ? 21.478  58.544  -58.450 1.00 51.53 ? 100 GLU J CA  1 
ATOM   10757 C  C   . GLU J  1 127 ? 21.263  59.694  -59.399 1.00 51.15 ? 100 GLU J C   1 
ATOM   10758 O  O   . GLU J  1 127 ? 20.191  60.293  -59.449 1.00 53.30 ? 100 GLU J O   1 
ATOM   10759 C  CB  . GLU J  1 127 ? 20.794  57.317  -59.026 1.00 55.01 ? 100 GLU J CB  1 
ATOM   10760 C  CG  . GLU J  1 127 ? 21.285  56.030  -58.407 1.00 60.24 ? 100 GLU J CG  1 
ATOM   10761 C  CD  . GLU J  1 127 ? 20.696  54.817  -59.089 1.00 67.84 ? 100 GLU J CD  1 
ATOM   10762 O  OE1 . GLU J  1 127 ? 20.618  53.745  -58.431 1.00 70.90 ? 100 GLU J OE1 1 
ATOM   10763 O  OE2 . GLU J  1 127 ? 20.317  54.943  -60.281 1.00 67.46 ? 100 GLU J OE2 1 
ATOM   10764 N  N   . ASP J  1 128 ? 22.291  60.008  -60.165 1.00 47.30 ? 101 ASP J N   1 
ATOM   10765 C  CA  . ASP J  1 128 ? 22.195  61.115  -61.069 1.00 49.21 ? 101 ASP J CA  1 
ATOM   10766 C  C   . ASP J  1 128 ? 22.824  60.634  -62.347 1.00 50.02 ? 101 ASP J C   1 
ATOM   10767 O  O   . ASP J  1 128 ? 23.791  59.852  -62.309 1.00 50.26 ? 101 ASP J O   1 
ATOM   10768 C  CB  . ASP J  1 128 ? 22.952  62.321  -60.524 1.00 51.96 ? 101 ASP J CB  1 
ATOM   10769 C  CG  . ASP J  1 128 ? 22.618  63.598  -61.270 1.00 58.02 ? 101 ASP J CG  1 
ATOM   10770 O  OD1 . ASP J  1 128 ? 21.602  64.238  -60.929 1.00 67.70 ? 101 ASP J OD1 1 
ATOM   10771 O  OD2 . ASP J  1 128 ? 23.366  63.971  -62.199 1.00 59.99 ? 101 ASP J OD2 1 
ATOM   10772 N  N   . SER J  1 129 ? 22.266  61.055  -63.477 1.00 52.31 ? 102 SER J N   1 
ATOM   10773 C  CA  . SER J  1 129 ? 22.860  60.672  -64.758 1.00 51.90 ? 102 SER J CA  1 
ATOM   10774 C  C   . SER J  1 129 ? 23.119  61.867  -65.619 1.00 49.68 ? 102 SER J C   1 
ATOM   10775 O  O   . SER J  1 129 ? 23.266  61.747  -66.833 1.00 54.59 ? 102 SER J O   1 
ATOM   10776 C  CB  . SER J  1 129 ? 22.048  59.598  -65.485 1.00 54.55 ? 102 SER J CB  1 
ATOM   10777 O  OG  . SER J  1 129 ? 20.688  59.659  -65.102 1.00 50.80 ? 102 SER J OG  1 
ATOM   10778 N  N   . VAL J  1 130 ? 23.190  63.027  -64.991 1.00 44.42 ? 103 VAL J N   1 
ATOM   10779 C  CA  . VAL J  1 130 ? 23.768  64.175  -65.660 1.00 44.92 ? 103 VAL J CA  1 
ATOM   10780 C  C   . VAL J  1 130 ? 25.280  64.279  -65.377 1.00 50.57 ? 103 VAL J C   1 
ATOM   10781 O  O   . VAL J  1 130 ? 26.071  64.646  -66.263 1.00 45.08 ? 103 VAL J O   1 
ATOM   10782 C  CB  . VAL J  1 130 ? 23.042  65.466  -65.271 1.00 47.30 ? 103 VAL J CB  1 
ATOM   10783 C  CG1 . VAL J  1 130 ? 23.643  66.666  -65.979 1.00 45.17 ? 103 VAL J CG1 1 
ATOM   10784 C  CG2 . VAL J  1 130 ? 21.561  65.326  -65.609 1.00 53.82 ? 103 VAL J CG2 1 
ATOM   10785 N  N   . ILE J  1 131 ? 25.680  64.004  -64.134 1.00 47.03 ? 104 ILE J N   1 
ATOM   10786 C  CA  . ILE J  1 131 ? 27.107  63.996  -63.794 1.00 41.84 ? 104 ILE J CA  1 
ATOM   10787 C  C   . ILE J  1 131 ? 27.685  62.702  -64.359 1.00 41.48 ? 104 ILE J C   1 
ATOM   10788 O  O   . ILE J  1 131 ? 26.955  61.724  -64.571 1.00 42.64 ? 104 ILE J O   1 
ATOM   10789 C  CB  . ILE J  1 131 ? 27.358  64.070  -62.251 1.00 40.13 ? 104 ILE J CB  1 
ATOM   10790 C  CG1 . ILE J  1 131 ? 26.763  62.861  -61.535 1.00 41.70 ? 104 ILE J CG1 1 
ATOM   10791 C  CG2 . ILE J  1 131 ? 26.833  65.386  -61.682 1.00 40.99 ? 104 ILE J CG2 1 
ATOM   10792 C  CD1 . ILE J  1 131 ? 27.210  62.685  -60.091 1.00 41.76 ? 104 ILE J CD1 1 
ATOM   10793 N  N   . SER J  1 132 ? 28.991  62.696  -64.595 1.00 39.87 ? 105 SER J N   1 
ATOM   10794 C  CA  . SER J  1 132 ? 29.710  61.500  -64.964 1.00 37.85 ? 105 SER J CA  1 
ATOM   10795 C  C   . SER J  1 132 ? 31.122  61.449  -64.326 1.00 37.02 ? 105 SER J C   1 
ATOM   10796 O  O   . SER J  1 132 ? 31.686  62.476  -63.959 1.00 41.22 ? 105 SER J O   1 
ATOM   10797 C  CB  . SER J  1 132 ? 29.855  61.477  -66.485 1.00 41.27 ? 105 SER J CB  1 
ATOM   10798 O  OG  . SER J  1 132 ? 30.321  60.217  -66.914 1.00 38.20 ? 105 SER J OG  1 
ATOM   10799 N  N   . LEU J  1 133 ? 31.687  60.254  -64.228 1.00 36.96 ? 106 LEU J N   1 
ATOM   10800 C  CA  . LEU J  1 133 ? 33.101  60.118  -63.873 1.00 38.19 ? 106 LEU J CA  1 
ATOM   10801 C  C   . LEU J  1 133 ? 34.049  60.111  -65.090 1.00 41.78 ? 106 LEU J C   1 
ATOM   10802 O  O   . LEU J  1 133 ? 35.226  59.775  -64.951 1.00 42.20 ? 106 LEU J O   1 
ATOM   10803 C  CB  . LEU J  1 133 ? 33.343  58.893  -63.008 1.00 35.06 ? 106 LEU J CB  1 
ATOM   10804 C  CG  . LEU J  1 133 ? 32.499  58.788  -61.746 1.00 34.57 ? 106 LEU J CG  1 
ATOM   10805 C  CD1 . LEU J  1 133 ? 32.959  57.606  -60.908 1.00 34.35 ? 106 LEU J CD1 1 
ATOM   10806 C  CD2 . LEU J  1 133 ? 32.473  60.096  -60.965 1.00 32.43 ? 106 LEU J CD2 1 
ATOM   10807 N  N   . SER J  1 134 ? 33.521  60.466  -66.264 1.00 44.72 ? 107 SER J N   1 
ATOM   10808 C  CA  . SER J  1 134 ? 34.341  60.741  -67.448 1.00 43.19 ? 107 SER J CA  1 
ATOM   10809 C  C   . SER J  1 134 ? 33.599  61.574  -68.491 1.00 46.94 ? 107 SER J C   1 
ATOM   10810 O  O   . SER J  1 134 ? 32.392  61.782  -68.395 1.00 43.39 ? 107 SER J O   1 
ATOM   10811 C  CB  . SER J  1 134 ? 34.808  59.443  -68.078 1.00 45.50 ? 107 SER J CB  1 
ATOM   10812 O  OG  . SER J  1 134 ? 33.683  58.706  -68.480 1.00 46.82 ? 107 SER J OG  1 
ATOM   10813 N  N   . GLY J  1 135 ? 34.322  62.054  -69.497 1.00 42.90 ? 108 GLY J N   1 
ATOM   10814 C  CA  . GLY J  1 135 ? 33.663  62.680  -70.616 1.00 46.35 ? 108 GLY J CA  1 
ATOM   10815 C  C   . GLY J  1 135 ? 33.493  64.138  -70.324 1.00 52.82 ? 108 GLY J C   1 
ATOM   10816 O  O   . GLY J  1 135 ? 34.202  64.713  -69.482 1.00 52.97 ? 108 GLY J O   1 
ATOM   10817 N  N   . ASP J  1 136 ? 32.539  64.742  -71.013 1.00 52.03 ? 109 ASP J N   1 
ATOM   10818 C  CA  . ASP J  1 136 ? 32.335  66.179  -70.909 1.00 56.43 ? 109 ASP J CA  1 
ATOM   10819 C  C   . ASP J  1 136 ? 31.825  66.506  -69.506 1.00 47.68 ? 109 ASP J C   1 
ATOM   10820 O  O   . ASP J  1 136 ? 32.057  67.595  -68.996 1.00 47.21 ? 109 ASP J O   1 
ATOM   10821 C  CB  . ASP J  1 136 ? 31.286  66.664  -71.937 1.00 58.22 ? 109 ASP J CB  1 
ATOM   10822 C  CG  . ASP J  1 136 ? 31.865  66.906  -73.347 1.00 64.80 ? 109 ASP J CG  1 
ATOM   10823 O  OD1 . ASP J  1 136 ? 33.045  67.348  -73.480 1.00 61.77 ? 109 ASP J OD1 1 
ATOM   10824 O  OD2 . ASP J  1 136 ? 31.091  66.690  -74.323 1.00 58.66 ? 109 ASP J OD2 1 
ATOM   10825 N  N   . HIS J  1 137 ? 31.092  65.562  -68.915 1.00 47.70 ? 110 HIS J N   1 
ATOM   10826 C  CA  . HIS J  1 137 ? 30.357  65.818  -67.688 1.00 44.34 ? 110 HIS J CA  1 
ATOM   10827 C  C   . HIS J  1 137 ? 31.116  65.288  -66.468 1.00 41.84 ? 110 HIS J C   1 
ATOM   10828 O  O   . HIS J  1 137 ? 30.547  65.201  -65.376 1.00 40.06 ? 110 HIS J O   1 
ATOM   10829 C  CB  . HIS J  1 137 ? 28.942  65.221  -67.795 1.00 47.48 ? 110 HIS J CB  1 
ATOM   10830 C  CG  . HIS J  1 137 ? 28.018  66.018  -68.669 1.00 50.09 ? 110 HIS J CG  1 
ATOM   10831 N  ND1 . HIS J  1 137 ? 26.664  65.751  -68.762 1.00 52.25 ? 110 HIS J ND1 1 
ATOM   10832 C  CD2 . HIS J  1 137 ? 28.247  67.088  -69.471 1.00 46.96 ? 110 HIS J CD2 1 
ATOM   10833 C  CE1 . HIS J  1 137 ? 26.100  66.628  -69.576 1.00 51.28 ? 110 HIS J CE1 1 
ATOM   10834 N  NE2 . HIS J  1 137 ? 27.039  67.446  -70.024 1.00 52.93 ? 110 HIS J NE2 1 
ATOM   10835 N  N   . CYS J  1 138 ? 32.379  64.921  -66.689 1.00 40.14 ? 111 CYS J N   1 
ATOM   10836 C  CA  . CYS J  1 138 ? 33.298  64.417  -65.652 1.00 40.03 ? 111 CYS J CA  1 
ATOM   10837 C  C   . CYS J  1 138 ? 33.439  65.407  -64.486 1.00 36.93 ? 111 CYS J C   1 
ATOM   10838 O  O   . CYS J  1 138 ? 33.749  66.570  -64.702 1.00 32.49 ? 111 CYS J O   1 
ATOM   10839 C  CB  . CYS J  1 138 ? 34.682  64.228  -66.230 1.00 37.63 ? 111 CYS J CB  1 
ATOM   10840 S  SG  . CYS J  1 138 ? 35.757  63.311  -65.113 1.00 41.28 ? 111 CYS J SG  1 
ATOM   10841 N  N   . ILE J  1 139 ? 33.251  64.910  -63.262 1.00 37.28 ? 112 ILE J N   1 
ATOM   10842 C  CA  . ILE J  1 139 ? 33.323  65.787  -62.066 1.00 33.35 ? 112 ILE J CA  1 
ATOM   10843 C  C   . ILE J  1 139 ? 34.583  65.573  -61.233 1.00 36.87 ? 112 ILE J C   1 
ATOM   10844 O  O   . ILE J  1 139 ? 34.814  66.320  -60.272 1.00 31.18 ? 112 ILE J O   1 
ATOM   10845 C  CB  . ILE J  1 139 ? 32.074  65.606  -61.185 1.00 33.34 ? 112 ILE J CB  1 
ATOM   10846 C  CG1 . ILE J  1 139 ? 31.978  64.154  -60.689 1.00 31.66 ? 112 ILE J CG1 1 
ATOM   10847 C  CG2 . ILE J  1 139 ? 30.836  66.046  -61.985 1.00 33.36 ? 112 ILE J CG2 1 
ATOM   10848 C  CD1 . ILE J  1 139 ? 30.901  63.925  -59.640 1.00 36.21 ? 112 ILE J CD1 1 
ATOM   10849 N  N   . ILE J  1 140 ? 35.395  64.585  -61.628 1.00 32.24 ? 113 ILE J N   1 
ATOM   10850 C  CA  . ILE J  1 140 ? 36.667  64.298  -60.968 1.00 31.77 ? 113 ILE J CA  1 
ATOM   10851 C  C   . ILE J  1 140 ? 37.569  65.510  -61.115 1.00 31.47 ? 113 ILE J C   1 
ATOM   10852 O  O   . ILE J  1 140 ? 37.639  66.111  -62.182 1.00 30.75 ? 113 ILE J O   1 
ATOM   10853 C  CB  . ILE J  1 140 ? 37.299  62.982  -61.489 1.00 32.23 ? 113 ILE J CB  1 
ATOM   10854 C  CG1 . ILE J  1 140 ? 36.504  61.834  -60.880 1.00 35.19 ? 113 ILE J CG1 1 
ATOM   10855 C  CG2 . ILE J  1 140 ? 38.775  62.893  -61.087 1.00 32.28 ? 113 ILE J CG2 1 
ATOM   10856 C  CD1 . ILE J  1 140 ? 36.739  60.437  -61.410 1.00 36.63 ? 113 ILE J CD1 1 
ATOM   10857 N  N   . GLY J  1 141 ? 38.171  65.955  -60.013 1.00 26.50 ? 114 GLY J N   1 
ATOM   10858 C  CA  . GLY J  1 141 ? 39.001  67.145  -60.067 1.00 27.02 ? 114 GLY J CA  1 
ATOM   10859 C  C   . GLY J  1 141 ? 38.228  68.434  -59.869 1.00 26.10 ? 114 GLY J C   1 
ATOM   10860 O  O   . GLY J  1 141 ? 38.803  69.506  -59.882 1.00 25.87 ? 114 GLY J O   1 
ATOM   10861 N  N   . ARG J  1 142 ? 36.916  68.335  -59.691 1.00 27.27 ? 115 ARG J N   1 
ATOM   10862 C  CA  . ARG J  1 142 ? 36.103  69.540  -59.423 1.00 28.92 ? 115 ARG J CA  1 
ATOM   10863 C  C   . ARG J  1 142 ? 35.724  69.525  -57.925 1.00 26.84 ? 115 ARG J C   1 
ATOM   10864 O  O   . ARG J  1 142 ? 36.198  68.656  -57.220 1.00 27.16 ? 115 ARG J O   1 
ATOM   10865 C  CB  . ARG J  1 142 ? 34.862  69.552  -60.345 1.00 31.36 ? 115 ARG J CB  1 
ATOM   10866 C  CG  . ARG J  1 142 ? 35.358  69.532  -61.801 1.00 32.95 ? 115 ARG J CG  1 
ATOM   10867 C  CD  . ARG J  1 142 ? 34.282  69.857  -62.806 1.00 38.83 ? 115 ARG J CD  1 
ATOM   10868 N  NE  . ARG J  1 142 ? 34.791  69.609  -64.168 1.00 37.24 ? 115 ARG J NE  1 
ATOM   10869 C  CZ  . ARG J  1 142 ? 35.426  70.496  -64.917 1.00 38.74 ? 115 ARG J CZ  1 
ATOM   10870 N  NH1 . ARG J  1 142 ? 35.655  71.744  -64.498 1.00 32.38 ? 115 ARG J NH1 1 
ATOM   10871 N  NH2 . ARG J  1 142 ? 35.822  70.119  -66.124 1.00 37.41 ? 115 ARG J NH2 1 
ATOM   10872 N  N   . THR J  1 143 ? 34.903  70.461  -57.456 1.00 28.71 ? 116 THR J N   1 
ATOM   10873 C  CA  . THR J  1 143 ? 34.626  70.556  -55.998 1.00 27.63 ? 116 THR J CA  1 
ATOM   10874 C  C   . THR J  1 143 ? 33.177  70.260  -55.651 1.00 29.46 ? 116 THR J C   1 
ATOM   10875 O  O   . THR J  1 143 ? 32.277  70.776  -56.299 1.00 33.27 ? 116 THR J O   1 
ATOM   10876 C  CB  . THR J  1 143 ? 34.985  71.949  -55.479 1.00 28.81 ? 116 THR J CB  1 
ATOM   10877 O  OG1 . THR J  1 143 ? 36.387  72.164  -55.650 1.00 29.81 ? 116 THR J OG1 1 
ATOM   10878 C  CG2 . THR J  1 143 ? 34.697  72.089  -53.970 1.00 29.21 ? 116 THR J CG2 1 
ATOM   10879 N  N   . LEU J  1 144 ? 32.937  69.438  -54.638 1.00 26.55 ? 117 LEU J N   1 
ATOM   10880 C  CA  . LEU J  1 144 ? 31.599  69.225  -54.141 1.00 27.07 ? 117 LEU J CA  1 
ATOM   10881 C  C   . LEU J  1 144 ? 31.373  70.223  -53.000 1.00 29.99 ? 117 LEU J C   1 
ATOM   10882 O  O   . LEU J  1 144 ? 32.245  70.384  -52.159 1.00 26.82 ? 117 LEU J O   1 
ATOM   10883 C  CB  . LEU J  1 144 ? 31.461  67.800  -53.654 1.00 26.91 ? 117 LEU J CB  1 
ATOM   10884 C  CG  . LEU J  1 144 ? 30.105  67.317  -53.189 1.00 27.99 ? 117 LEU J CG  1 
ATOM   10885 C  CD1 . LEU J  1 144 ? 29.115  67.405  -54.351 1.00 30.39 ? 117 LEU J CD1 1 
ATOM   10886 C  CD2 . LEU J  1 144 ? 30.230  65.883  -52.749 1.00 29.54 ? 117 LEU J CD2 1 
ATOM   10887 N  N   . VAL J  1 145 ? 30.231  70.912  -52.985 1.00 29.58 ? 118 VAL J N   1 
ATOM   10888 C  CA  . VAL J  1 145 ? 29.981  71.938  -51.960 1.00 29.18 ? 118 VAL J CA  1 
ATOM   10889 C  C   . VAL J  1 145 ? 28.635  71.665  -51.289 1.00 32.94 ? 118 VAL J C   1 
ATOM   10890 O  O   . VAL J  1 145 ? 27.653  71.347  -51.979 1.00 29.19 ? 118 VAL J O   1 
ATOM   10891 C  CB  . VAL J  1 145 ? 29.995  73.360  -52.547 1.00 28.80 ? 118 VAL J CB  1 
ATOM   10892 C  CG1 . VAL J  1 145 ? 29.670  74.426  -51.487 1.00 29.23 ? 118 VAL J CG1 1 
ATOM   10893 C  CG2 . VAL J  1 145 ? 31.317  73.673  -53.233 1.00 29.44 ? 118 VAL J CG2 1 
ATOM   10894 N  N   . VAL J  1 146 ? 28.589  71.743  -49.950 1.00 30.67 ? 119 VAL J N   1 
ATOM   10895 C  CA  . VAL J  1 146 ? 27.320  71.748  -49.239 1.00 31.25 ? 119 VAL J CA  1 
ATOM   10896 C  C   . VAL J  1 146 ? 27.065  73.175  -48.760 1.00 33.80 ? 119 VAL J C   1 
ATOM   10897 O  O   . VAL J  1 146 ? 27.968  73.842  -48.238 1.00 31.24 ? 119 VAL J O   1 
ATOM   10898 C  CB  . VAL J  1 146 ? 27.217  70.635  -48.175 1.00 33.79 ? 119 VAL J CB  1 
ATOM   10899 C  CG1 . VAL J  1 146 ? 28.390  70.701  -47.226 1.00 29.45 ? 119 VAL J CG1 1 
ATOM   10900 C  CG2 . VAL J  1 146 ? 25.879  70.707  -47.416 1.00 31.67 ? 119 VAL J CG2 1 
ATOM   10901 N  N   . HIS J  1 147 ? 25.853  73.682  -49.018 1.00 32.58 ? 120 HIS J N   1 
ATOM   10902 C  CA  . HIS J  1 147 ? 25.521  75.096  -48.777 1.00 33.03 ? 120 HIS J CA  1 
ATOM   10903 C  C   . HIS J  1 147 ? 24.669  75.306  -47.509 1.00 33.64 ? 120 HIS J C   1 
ATOM   10904 O  O   . HIS J  1 147 ? 24.050  74.390  -46.981 1.00 33.51 ? 120 HIS J O   1 
ATOM   10905 C  CB  . HIS J  1 147 ? 24.773  75.686  -49.962 1.00 35.54 ? 120 HIS J CB  1 
ATOM   10906 C  CG  . HIS J  1 147 ? 25.605  75.785  -51.197 1.00 33.81 ? 120 HIS J CG  1 
ATOM   10907 N  ND1 . HIS J  1 147 ? 26.169  76.970  -51.619 1.00 34.71 ? 120 HIS J ND1 1 
ATOM   10908 C  CD2 . HIS J  1 147 ? 26.016  74.835  -52.063 1.00 33.50 ? 120 HIS J CD2 1 
ATOM   10909 C  CE1 . HIS J  1 147 ? 26.865  76.746  -52.723 1.00 34.66 ? 120 HIS J CE1 1 
ATOM   10910 N  NE2 . HIS J  1 147 ? 26.800  75.455  -53.002 1.00 31.72 ? 120 HIS J NE2 1 
ATOM   10911 N  N   . GLU J  1 148 ? 24.679  76.543  -47.053 1.00 33.83 ? 121 GLU J N   1 
ATOM   10912 C  CA  . GLU J  1 148 ? 24.030  76.937  -45.827 1.00 36.94 ? 121 GLU J CA  1 
ATOM   10913 C  C   . GLU J  1 148 ? 22.491  76.800  -45.950 1.00 39.86 ? 121 GLU J C   1 
ATOM   10914 O  O   . GLU J  1 148 ? 21.816  76.298  -45.041 1.00 38.64 ? 121 GLU J O   1 
ATOM   10915 C  CB  . GLU J  1 148 ? 24.417  78.374  -45.608 1.00 40.63 ? 121 GLU J CB  1 
ATOM   10916 C  CG  . GLU J  1 148 ? 23.724  79.045  -44.442 1.00 51.56 ? 121 GLU J CG  1 
ATOM   10917 C  CD  . GLU J  1 148 ? 24.054  80.517  -44.439 1.00 59.04 ? 121 GLU J CD  1 
ATOM   10918 O  OE1 . GLU J  1 148 ? 23.799  81.198  -45.467 1.00 66.42 ? 121 GLU J OE1 1 
ATOM   10919 O  OE2 . GLU J  1 148 ? 24.597  80.995  -43.431 1.00 66.89 ? 121 GLU J OE2 1 
ATOM   10920 N  N   . LYS J  1 149 ? 21.972  77.204  -47.107 1.00 37.84 ? 122 LYS J N   1 
ATOM   10921 C  CA  . LYS J  1 149 ? 20.523  77.219  -47.319 1.00 48.13 ? 122 LYS J CA  1 
ATOM   10922 C  C   . LYS J  1 149 ? 19.996  76.171  -48.304 1.00 48.07 ? 122 LYS J C   1 
ATOM   10923 O  O   . LYS J  1 149 ? 20.744  75.647  -49.139 1.00 45.35 ? 122 LYS J O   1 
ATOM   10924 C  CB  . LYS J  1 149 ? 20.088  78.633  -47.706 1.00 49.41 ? 122 LYS J CB  1 
ATOM   10925 C  CG  . LYS J  1 149 ? 19.696  79.420  -46.467 1.00 57.44 ? 122 LYS J CG  1 
ATOM   10926 C  CD  . LYS J  1 149 ? 19.820  80.917  -46.675 1.00 64.62 ? 122 LYS J CD  1 
ATOM   10927 C  CE  . LYS J  1 149 ? 19.682  81.652  -45.347 1.00 66.77 ? 122 LYS J CE  1 
ATOM   10928 N  NZ  . LYS J  1 149 ? 19.306  83.075  -45.604 1.00 73.66 ? 122 LYS J NZ  1 
ATOM   10929 N  N   . ALA J  1 150 ? 18.709  75.848  -48.183 1.00 47.04 ? 123 ALA J N   1 
ATOM   10930 C  CA  . ALA J  1 150 ? 18.058  74.946  -49.133 1.00 46.45 ? 123 ALA J CA  1 
ATOM   10931 C  C   . ALA J  1 150 ? 18.200  75.504  -50.535 1.00 48.37 ? 123 ALA J C   1 
ATOM   10932 O  O   . ALA J  1 150 ? 18.216  76.724  -50.767 1.00 48.72 ? 123 ALA J O   1 
ATOM   10933 C  CB  . ALA J  1 150 ? 16.580  74.716  -48.791 1.00 45.90 ? 123 ALA J CB  1 
ATOM   10934 N  N   . ASP J  1 151 ? 18.340  74.586  -51.471 1.00 51.76 ? 124 ASP J N   1 
ATOM   10935 C  CA  . ASP J  1 151 ? 18.181  74.933  -52.845 1.00 59.55 ? 124 ASP J CA  1 
ATOM   10936 C  C   . ASP J  1 151 ? 16.668  74.817  -53.133 1.00 59.50 ? 124 ASP J C   1 
ATOM   10937 O  O   . ASP J  1 151 ? 15.988  73.913  -52.616 1.00 53.63 ? 124 ASP J O   1 
ATOM   10938 C  CB  . ASP J  1 151 ? 18.969  73.948  -53.675 1.00 62.80 ? 124 ASP J CB  1 
ATOM   10939 C  CG  . ASP J  1 151 ? 19.376  74.509  -54.991 1.00 69.91 ? 124 ASP J CG  1 
ATOM   10940 O  OD1 . ASP J  1 151 ? 19.205  75.740  -55.199 1.00 70.28 ? 124 ASP J OD1 1 
ATOM   10941 O  OD2 . ASP J  1 151 ? 19.859  73.703  -55.819 1.00 66.72 ? 124 ASP J OD2 1 
ATOM   10942 N  N   . ASP J  1 152 ? 16.136  75.755  -53.905 1.00 57.52 ? 125 ASP J N   1 
ATOM   10943 C  CA  . ASP J  1 152 ? 14.737  75.662  -54.354 1.00 65.95 ? 125 ASP J CA  1 
ATOM   10944 C  C   . ASP J  1 152 ? 14.632  75.619  -55.891 1.00 59.09 ? 125 ASP J C   1 
ATOM   10945 O  O   . ASP J  1 152 ? 14.678  74.554  -56.507 1.00 67.56 ? 125 ASP J O   1 
ATOM   10946 C  CB  . ASP J  1 152 ? 13.951  76.850  -53.809 1.00 67.72 ? 125 ASP J CB  1 
ATOM   10947 C  CG  . ASP J  1 152 ? 14.447  78.170  -54.369 1.00 73.12 ? 125 ASP J CG  1 
ATOM   10948 O  OD1 . ASP J  1 152 ? 14.850  78.207  -55.563 1.00 71.84 ? 125 ASP J OD1 1 
ATOM   10949 O  OD2 . ASP J  1 152 ? 14.435  79.170  -53.618 1.00 78.37 ? 125 ASP J OD2 1 
ATOM   10950 N  N   . SER J  1 169 ? 26.164  81.020  -48.468 1.00 44.86 ? 142 SER J N   1 
ATOM   10951 C  CA  . SER J  1 169 ? 27.325  80.593  -47.713 1.00 42.74 ? 142 SER J CA  1 
ATOM   10952 C  C   . SER J  1 169 ? 27.660  79.122  -47.975 1.00 38.60 ? 142 SER J C   1 
ATOM   10953 O  O   . SER J  1 169 ? 26.782  78.254  -47.960 1.00 37.42 ? 142 SER J O   1 
ATOM   10954 C  CB  . SER J  1 169 ? 27.046  80.791  -46.231 1.00 46.48 ? 142 SER J CB  1 
ATOM   10955 O  OG  . SER J  1 169 ? 28.234  80.891  -45.503 1.00 50.71 ? 142 SER J OG  1 
ATOM   10956 N  N   . ARG J  1 170 ? 28.946  78.850  -48.206 1.00 34.69 ? 143 ARG J N   1 
ATOM   10957 C  CA  . ARG J  1 170 ? 29.402  77.492  -48.489 1.00 32.42 ? 143 ARG J CA  1 
ATOM   10958 C  C   . ARG J  1 170 ? 29.928  76.926  -47.172 1.00 29.34 ? 143 ARG J C   1 
ATOM   10959 O  O   . ARG J  1 170 ? 30.908  77.446  -46.636 1.00 31.54 ? 143 ARG J O   1 
ATOM   10960 C  CB  . ARG J  1 170 ? 30.488  77.539  -49.596 1.00 30.78 ? 143 ARG J CB  1 
ATOM   10961 C  CG  . ARG J  1 170 ? 29.988  78.185  -50.905 1.00 34.15 ? 143 ARG J CG  1 
ATOM   10962 C  CD  . ARG J  1 170 ? 31.093  78.472  -51.923 1.00 34.96 ? 143 ARG J CD  1 
ATOM   10963 N  NE  . ARG J  1 170 ? 30.471  79.101  -53.090 1.00 34.48 ? 143 ARG J NE  1 
ATOM   10964 C  CZ  . ARG J  1 170 ? 30.940  79.053  -54.329 1.00 38.55 ? 143 ARG J CZ  1 
ATOM   10965 N  NH1 . ARG J  1 170 ? 32.076  78.399  -54.612 1.00 33.30 ? 143 ARG J NH1 1 
ATOM   10966 N  NH2 . ARG J  1 170 ? 30.251  79.645  -55.298 1.00 37.39 ? 143 ARG J NH2 1 
ATOM   10967 N  N   . LEU J  1 171 ? 29.272  75.898  -46.638 1.00 27.82 ? 144 LEU J N   1 
ATOM   10968 C  CA  . LEU J  1 171 ? 29.614  75.361  -45.340 1.00 31.54 ? 144 LEU J CA  1 
ATOM   10969 C  C   . LEU J  1 171 ? 30.820  74.429  -45.392 1.00 31.72 ? 144 LEU J C   1 
ATOM   10970 O  O   . LEU J  1 171 ? 31.658  74.461  -44.510 1.00 27.84 ? 144 LEU J O   1 
ATOM   10971 C  CB  . LEU J  1 171 ? 28.419  74.600  -44.713 1.00 32.13 ? 144 LEU J CB  1 
ATOM   10972 C  CG  . LEU J  1 171 ? 27.141  75.462  -44.578 1.00 32.51 ? 144 LEU J CG  1 
ATOM   10973 C  CD1 . LEU J  1 171 ? 26.058  74.636  -43.931 1.00 35.71 ? 144 LEU J CD1 1 
ATOM   10974 C  CD2 . LEU J  1 171 ? 27.429  76.766  -43.858 1.00 35.84 ? 144 LEU J CD2 1 
ATOM   10975 N  N   . ALA J  1 172 ? 30.876  73.548  -46.390 1.00 28.30 ? 145 ALA J N   1 
ATOM   10976 C  CA  . ALA J  1 172 ? 32.042  72.658  -46.513 1.00 25.45 ? 145 ALA J CA  1 
ATOM   10977 C  C   . ALA J  1 172 ? 32.222  72.279  -47.968 1.00 28.36 ? 145 ALA J C   1 
ATOM   10978 O  O   . ALA J  1 172 ? 31.270  72.417  -48.764 1.00 27.57 ? 145 ALA J O   1 
ATOM   10979 C  CB  . ALA J  1 172 ? 31.882  71.400  -45.664 1.00 25.25 ? 145 ALA J CB  1 
ATOM   10980 N  N   . CYS J  1 173 ? 33.405  71.772  -48.307 1.00 26.25 ? 146 CYS J N   1 
ATOM   10981 C  CA  . CYS J  1 173 ? 33.677  71.376  -49.695 1.00 25.41 ? 146 CYS J CA  1 
ATOM   10982 C  C   . CYS J  1 173 ? 34.866  70.481  -49.741 1.00 29.24 ? 146 CYS J C   1 
ATOM   10983 O  O   . CYS J  1 173 ? 35.606  70.399  -48.757 1.00 22.79 ? 146 CYS J O   1 
ATOM   10984 C  CB  . CYS J  1 173 ? 33.989  72.599  -50.539 1.00 26.48 ? 146 CYS J CB  1 
ATOM   10985 S  SG  . CYS J  1 173 ? 35.358  73.632  -49.984 1.00 32.67 ? 146 CYS J SG  1 
ATOM   10986 N  N   . GLY J  1 174 ? 35.058  69.803  -50.884 1.00 25.91 ? 147 GLY J N   1 
ATOM   10987 C  CA  . GLY J  1 174 ? 36.253  69.013  -51.070 1.00 26.37 ? 147 GLY J CA  1 
ATOM   10988 C  C   . GLY J  1 174 ? 36.430  68.763  -52.557 1.00 28.22 ? 147 GLY J C   1 
ATOM   10989 O  O   . GLY J  1 174 ? 35.479  68.881  -53.341 1.00 25.00 ? 147 GLY J O   1 
ATOM   10990 N  N   . VAL J  1 175 ? 37.658  68.442  -52.930 1.00 27.27 ? 148 VAL J N   1 
ATOM   10991 C  CA  . VAL J  1 175 ? 37.958  68.065  -54.320 1.00 25.78 ? 148 VAL J CA  1 
ATOM   10992 C  C   . VAL J  1 175 ? 37.567  66.619  -54.531 1.00 26.04 ? 148 VAL J C   1 
ATOM   10993 O  O   . VAL J  1 175 ? 37.860  65.753  -53.694 1.00 26.39 ? 148 VAL J O   1 
ATOM   10994 C  CB  . VAL J  1 175 ? 39.460  68.275  -54.651 1.00 26.70 ? 148 VAL J CB  1 
ATOM   10995 C  CG1 . VAL J  1 175 ? 39.725  68.015  -56.156 1.00 24.28 ? 148 VAL J CG1 1 
ATOM   10996 C  CG2 . VAL J  1 175 ? 39.880  69.688  -54.284 1.00 24.86 ? 148 VAL J CG2 1 
ATOM   10997 N  N   . ILE J  1 176 ? 36.883  66.352  -55.649 1.00 24.78 ? 149 ILE J N   1 
ATOM   10998 C  CA  . ILE J  1 176 ? 36.461  65.022  -55.998 1.00 25.40 ? 149 ILE J CA  1 
ATOM   10999 C  C   . ILE J  1 176 ? 37.674  64.266  -56.600 1.00 26.50 ? 149 ILE J C   1 
ATOM   11000 O  O   . ILE J  1 176 ? 38.286  64.720  -57.582 1.00 31.25 ? 149 ILE J O   1 
ATOM   11001 C  CB  . ILE J  1 176 ? 35.226  65.032  -56.931 1.00 24.64 ? 149 ILE J CB  1 
ATOM   11002 C  CG1 . ILE J  1 176 ? 34.077  65.823  -56.269 1.00 25.36 ? 149 ILE J CG1 1 
ATOM   11003 C  CG2 . ILE J  1 176 ? 34.832  63.593  -57.268 1.00 24.81 ? 149 ILE J CG2 1 
ATOM   11004 C  CD1 . ILE J  1 176 ? 32.941  66.276  -57.182 1.00 27.88 ? 149 ILE J CD1 1 
ATOM   11005 N  N   . GLY J  1 177 ? 38.023  63.153  -55.974 1.00 26.00 ? 150 GLY J N   1 
ATOM   11006 C  CA  . GLY J  1 177 ? 39.227  62.407  -56.334 1.00 28.04 ? 150 GLY J CA  1 
ATOM   11007 C  C   . GLY J  1 177 ? 38.936  60.993  -56.792 1.00 31.57 ? 150 GLY J C   1 
ATOM   11008 O  O   . GLY J  1 177 ? 37.897  60.380  -56.426 1.00 28.47 ? 150 GLY J O   1 
ATOM   11009 N  N   . ILE J  1 178 ? 39.882  60.429  -57.550 1.00 30.09 ? 151 ILE J N   1 
ATOM   11010 C  CA  . ILE J  1 178 ? 39.783  59.023  -57.992 1.00 32.36 ? 151 ILE J CA  1 
ATOM   11011 C  C   . ILE J  1 178 ? 39.945  58.097  -56.803 1.00 32.02 ? 151 ILE J C   1 
ATOM   11012 O  O   . ILE J  1 178 ? 40.866  58.272  -55.983 1.00 33.63 ? 151 ILE J O   1 
ATOM   11013 C  CB  . ILE J  1 178 ? 40.862  58.701  -59.085 1.00 32.50 ? 151 ILE J CB  1 
ATOM   11014 C  CG1 . ILE J  1 178 ? 40.761  59.721  -60.216 1.00 34.88 ? 151 ILE J CG1 1 
ATOM   11015 C  CG2 . ILE J  1 178 ? 40.628  57.330  -59.673 1.00 36.45 ? 151 ILE J CG2 1 
ATOM   11016 C  CD1 . ILE J  1 178 ? 41.907  59.695  -61.224 1.00 43.92 ? 151 ILE J CD1 1 
ATOM   11017 N  N   . ALA J  1 179 ? 39.046  57.126  -56.670 1.00 30.38 ? 152 ALA J N   1 
ATOM   11018 C  CA  . ALA J  1 179 ? 39.167  56.164  -55.584 1.00 32.71 ? 152 ALA J CA  1 
ATOM   11019 C  C   . ALA J  1 179 ? 39.461  54.760  -56.098 1.00 35.41 ? 152 ALA J C   1 
ATOM   11020 O  O   . ALA J  1 179 ? 39.260  54.463  -57.277 1.00 39.22 ? 152 ALA J O   1 
ATOM   11021 C  CB  . ALA J  1 179 ? 37.895  56.167  -54.710 1.00 31.21 ? 152 ALA J CB  1 
ATOM   11022 N  N   . GLN J  1 180 ? 39.930  53.904  -55.200 1.00 41.90 ? 153 GLN J N   1 
ATOM   11023 C  CA  . GLN J  1 180 ? 40.168  52.495  -55.504 1.00 51.22 ? 153 GLN J CA  1 
ATOM   11024 C  C   . GLN J  1 180 ? 38.821  51.796  -55.591 1.00 54.41 ? 153 GLN J C   1 
ATOM   11025 O  O   . GLN J  1 180 ? 38.164  51.511  -54.568 1.00 55.75 ? 153 GLN J O   1 
ATOM   11026 C  CB  . GLN J  1 180 ? 41.039  51.852  -54.419 1.00 51.45 ? 153 GLN J CB  1 
ATOM   11027 C  CG  . GLN J  1 180 ? 41.546  50.453  -54.764 1.00 55.25 ? 153 GLN J CG  1 
ATOM   11028 C  CD  . GLN J  1 180 ? 42.494  49.931  -53.708 1.00 61.17 ? 153 GLN J CD  1 
ATOM   11029 O  OE1 . GLN J  1 180 ? 42.266  50.122  -52.513 1.00 66.00 ? 153 GLN J OE1 1 
ATOM   11030 N  NE2 . GLN J  1 180 ? 43.562  49.270  -54.136 1.00 64.74 ? 153 GLN J NE2 1 
ATOM   11031 O  OXT . GLN J  1 180 ? 38.352  51.557  -56.711 1.00 64.35 ? 153 GLN J OXT 1 
HETATM 11032 ZN ZN  . ZN  K  2 .   ? 85.254  47.291  -12.999 1.00 34.34 ? 201 ZN  A ZN  1 
HETATM 11033 C  C1  . GOL L  3 .   ? 86.104  51.511  -20.532 1.00 46.58 ? 202 GOL A C1  1 
HETATM 11034 O  O1  . GOL L  3 .   ? 85.982  51.538  -19.108 1.00 40.98 ? 202 GOL A O1  1 
HETATM 11035 C  C2  . GOL L  3 .   ? 86.431  52.849  -21.174 1.00 50.07 ? 202 GOL A C2  1 
HETATM 11036 O  O2  . GOL L  3 .   ? 87.672  53.447  -20.733 1.00 52.29 ? 202 GOL A O2  1 
HETATM 11037 C  C3  . GOL L  3 .   ? 86.453  52.669  -22.680 1.00 52.72 ? 202 GOL A C3  1 
HETATM 11038 O  O3  . GOL L  3 .   ? 86.950  53.894  -23.238 1.00 58.64 ? 202 GOL A O3  1 
HETATM 11039 ZN ZN  . ZN  M  2 .   ? 50.136  65.321  -15.586 1.00 24.05 ? 201 ZN  B ZN  1 
HETATM 11040 C  C1  . GOL N  3 .   ? 51.116  60.944  -24.978 1.00 37.07 ? 202 GOL B C1  1 
HETATM 11041 O  O1  . GOL N  3 .   ? 50.628  60.060  -25.996 1.00 49.69 ? 202 GOL B O1  1 
HETATM 11042 C  C2  . GOL N  3 .   ? 50.163  60.899  -23.794 1.00 43.70 ? 202 GOL B C2  1 
HETATM 11043 O  O2  . GOL N  3 .   ? 49.491  59.611  -23.771 1.00 47.02 ? 202 GOL B O2  1 
HETATM 11044 C  C3  . GOL N  3 .   ? 51.004  61.028  -22.541 1.00 37.82 ? 202 GOL B C3  1 
HETATM 11045 O  O3  . GOL N  3 .   ? 50.760  62.174  -21.765 1.00 37.79 ? 202 GOL B O3  1 
HETATM 11046 C  C1  . 946 O  4 .   ? 68.686  74.530  -6.994  1.00 36.27 ? 203 946 B C1  1 
HETATM 11047 O  O1  . 946 O  4 .   ? 68.364  73.413  -6.364  1.00 32.49 ? 203 946 B O1  1 
HETATM 11048 C  C2  . 946 O  4 .   ? 67.722  75.468  -7.290  1.00 37.10 ? 203 946 B C2  1 
HETATM 11049 O  O2  . 946 O  4 .   ? 66.443  75.240  -6.962  1.00 33.96 ? 203 946 B O2  1 
HETATM 11050 C  C3  . 946 O  4 .   ? 68.109  76.630  -7.940  1.00 36.14 ? 203 946 B C3  1 
HETATM 11051 O  O3  . 946 O  4 .   ? 72.769  75.230  -7.602  1.00 51.16 ? 203 946 B O3  1 
HETATM 11052 C  C4  . 946 O  4 .   ? 69.444  76.840  -8.275  1.00 41.21 ? 203 946 B C4  1 
HETATM 11053 C  C5  . 946 O  4 .   ? 70.438  75.911  -7.967  1.00 40.88 ? 203 946 B C5  1 
HETATM 11054 C  C6  . 946 O  4 .   ? 71.892  76.092  -8.346  1.00 50.73 ? 203 946 B C6  1 
HETATM 11055 C  C7  . 946 O  4 .   ? 72.138  75.687  -9.820  1.00 66.53 ? 203 946 B C7  1 
HETATM 11056 C  C8  . 946 O  4 .   ? 71.774  76.453  -12.160 1.00 69.38 ? 203 946 B C8  1 
HETATM 11057 C  C9  . 946 O  4 .   ? 72.512  76.794  -13.445 1.00 74.82 ? 203 946 B C9  1 
HETATM 11058 C  C10 . 946 O  4 .   ? 72.371  77.537  -15.769 1.00 68.58 ? 203 946 B C10 1 
HETATM 11059 C  C11 . 946 O  4 .   ? 71.609  77.967  -16.838 1.00 58.90 ? 203 946 B C11 1 
HETATM 11060 C  C12 . 946 O  4 .   ? 72.231  78.260  -18.040 1.00 60.56 ? 203 946 B C12 1 
HETATM 11061 C  C13 . 946 O  4 .   ? 73.610  78.149  -18.186 1.00 62.00 ? 203 946 B C13 1 
HETATM 11062 C  C14 . 946 O  4 .   ? 74.377  77.730  -17.104 1.00 62.70 ? 203 946 B C14 1 
HETATM 11063 C  C15 . 946 O  4 .   ? 73.748  77.418  -15.901 1.00 65.66 ? 203 946 B C15 1 
HETATM 11064 C  C16 . 946 O  4 .   ? 74.487  77.000  -14.806 1.00 64.14 ? 203 946 B C16 1 
HETATM 11065 C  C17 . 946 O  4 .   ? 73.879  76.667  -13.600 1.00 67.75 ? 203 946 B C17 1 
HETATM 11066 C  C18 . 946 O  4 .   ? 70.019  74.761  -7.320  1.00 36.20 ? 203 946 B C18 1 
HETATM 11067 C  C19 . 946 O  4 .   ? 71.768  77.209  -14.560 1.00 73.07 ? 203 946 B C19 1 
HETATM 11068 N  N1  . 946 O  4 .   ? 72.333  76.780  -10.839 1.00 68.34 ? 203 946 B N1  1 
HETATM 11069 S  S1  . PS5 P  5 .   ? 64.980  54.979  -7.809  0.75 70.04 ? 204 PS5 B S1  1 
HETATM 11070 S  S2  . PS5 P  5 .   ? 66.057  56.559  -7.974  0.75 69.59 ? 204 PS5 B S2  1 
HETATM 11071 S  S3  . PS5 P  5 .   ? 67.946  55.804  -8.002  0.75 67.93 ? 204 PS5 B S3  1 
HETATM 11072 S  S4  . PS5 P  5 .   ? 69.218  57.229  -7.308  0.75 69.19 ? 204 PS5 B S4  1 
HETATM 11073 S  S5  . PS5 P  5 .   ? 68.109  58.669  -6.654  0.75 55.39 ? 204 PS5 B S5  1 
HETATM 11074 ZN ZN  . ZN  Q  2 .   ? 58.100  91.485  -15.656 1.00 23.47 ? 201 ZN  C ZN  1 
HETATM 11075 C  C1  . GOL R  3 .   ? 61.480  93.184  -23.101 1.00 43.99 ? 202 GOL C C1  1 
HETATM 11076 O  O1  . GOL R  3 .   ? 60.767  93.950  -22.121 1.00 37.21 ? 202 GOL C O1  1 
HETATM 11077 C  C2  . GOL R  3 .   ? 62.501  93.969  -23.897 1.00 48.77 ? 202 GOL C C2  1 
HETATM 11078 O  O2  . GOL R  3 .   ? 63.777  93.277  -24.003 1.00 48.04 ? 202 GOL C O2  1 
HETATM 11079 C  C3  . GOL R  3 .   ? 61.843  94.229  -25.243 1.00 41.69 ? 202 GOL C C3  1 
HETATM 11080 O  O3  . GOL R  3 .   ? 62.735  94.932  -26.127 1.00 49.65 ? 202 GOL C O3  1 
HETATM 11081 S  S1  . PS5 S  5 .   ? 56.464  112.412 -7.834  0.75 62.58 ? 203 PS5 C S1  1 
HETATM 11082 S  S2  . PS5 S  5 .   ? 56.551  110.533 -7.382  0.75 69.69 ? 203 PS5 C S2  1 
HETATM 11083 S  S3  . PS5 S  5 .   ? 58.352  110.379 -8.275  0.75 64.54 ? 203 PS5 C S3  1 
HETATM 11084 S  S4  . PS5 S  5 .   ? 59.119  108.520 -8.172  0.75 68.20 ? 203 PS5 C S4  1 
HETATM 11085 S  S5  . PS5 S  5 .   ? 60.883  109.246 -7.926  0.75 62.61 ? 203 PS5 C S5  1 
HETATM 11086 ZN ZN  . ZN  T  2 .   ? 57.637  130.823 -12.910 1.00 34.72 ? 201 ZN  D ZN  1 
HETATM 11087 C  C1  . 946 U  4 .   ? 59.138  115.447 -32.618 1.00 46.74 ? 202 946 D C1  1 
HETATM 11088 O  O1  . 946 U  4 .   ? 60.013  116.455 -32.240 1.00 34.97 ? 202 946 D O1  1 
HETATM 11089 C  C2  . 946 U  4 .   ? 59.550  114.092 -32.739 1.00 48.20 ? 202 946 D C2  1 
HETATM 11090 O  O2  . 946 U  4 .   ? 60.857  113.722 -32.486 1.00 54.59 ? 202 946 D O2  1 
HETATM 11091 C  C3  . 946 U  4 .   ? 58.633  113.089 -33.109 1.00 48.37 ? 202 946 D C3  1 
HETATM 11092 O  O3  . 946 U  4 .   ? 55.308  116.530 -34.118 1.00 51.93 ? 202 946 D O3  1 
HETATM 11093 C  C4  . 946 U  4 .   ? 57.306  113.451 -33.367 1.00 52.85 ? 202 946 D C4  1 
HETATM 11094 C  C5  . 946 U  4 .   ? 56.861  114.795 -33.257 1.00 52.51 ? 202 946 D C5  1 
HETATM 11095 C  C6  . 946 U  4 .   ? 55.425  115.182 -33.559 1.00 57.20 ? 202 946 D C6  1 
HETATM 11096 C  C7  . 946 U  4 .   ? 54.756  114.208 -34.566 1.00 58.72 ? 202 946 D C7  1 
HETATM 11097 C  C18 . 946 U  4 .   ? 57.794  115.781 -32.870 1.00 47.41 ? 202 946 D C18 1 
HETATM 11098 ZN ZN  . ZN  V  2 .   ? 58.079  70.137  15.627  1.00 24.14 ? 201 ZN  E ZN  1 
HETATM 11099 S  S1  . PS5 W  5 .   ? 61.230  52.748  7.804   0.75 64.38 ? 202 PS5 E S1  1 
HETATM 11100 S  S2  . PS5 W  5 .   ? 59.351  52.715  8.255   0.75 65.55 ? 202 PS5 E S2  1 
HETATM 11101 S  S3  . PS5 W  5 .   ? 58.867  50.761  8.138   0.75 65.38 ? 202 PS5 E S3  1 
HETATM 11102 S  S4  . PS5 W  5 .   ? 57.044  50.893  7.296   0.75 78.26 ? 202 PS5 E S4  1 
HETATM 11103 S  S5  . PS5 W  5 .   ? 56.449  49.071  7.281   0.75 74.08 ? 202 PS5 E S5  1 
HETATM 11104 ZN ZN  . ZN  X  2 .   ? 58.917  30.938  12.954  1.00 40.05 ? 201 ZN  F ZN  1 
HETATM 11105 ZN ZN  . ZN  Y  2 .   ? 93.542  107.002 -11.341 1.00 27.85 ? 201 ZN  G ZN  1 
HETATM 11106 ZN ZN  . ZN  Z  2 .   ? 94.708  67.618  -6.961  1.00 35.11 ? 201 ZN  H ZN  1 
HETATM 11107 C  C1  . 946 AA 4 .   ? 74.207  72.333  -7.514  1.00 54.31 ? 202 946 H C1  1 
HETATM 11108 O  O1  . 946 AA 4 .   ? 73.338  71.867  -6.630  1.00 49.44 ? 202 946 H O1  1 
HETATM 11109 C  C2  . 946 AA 4 .   ? 74.990  71.456  -8.183  1.00 47.74 ? 202 946 H C2  1 
HETATM 11110 O  O2  . 946 AA 4 .   ? 74.885  70.180  -7.931  1.00 45.85 ? 202 946 H O2  1 
HETATM 11111 C  C3  . 946 AA 4 .   ? 75.894  71.886  -9.088  1.00 48.06 ? 202 946 H C3  1 
HETATM 11112 O  O3  . 946 AA 4 .   ? 75.587  76.064  -7.642  1.00 41.23 ? 202 946 H O3  1 
HETATM 11113 C  C4  . 946 AA 4 .   ? 76.027  73.221  -9.351  1.00 55.30 ? 202 946 H C4  1 
HETATM 11114 C  C5  . 946 AA 4 .   ? 75.221  74.104  -8.712  1.00 47.29 ? 202 946 H C5  1 
HETATM 11115 C  C6  . 946 AA 4 .   ? 75.338  75.542  -8.914  1.00 44.09 ? 202 946 H C6  1 
HETATM 11116 C  C7  . 946 AA 4 .   ? 76.425  76.099  -9.811  1.00 43.36 ? 202 946 H C7  1 
HETATM 11117 C  C8  . 946 AA 4 .   ? 74.968  77.940  -9.904  1.00 50.13 ? 202 946 H C8  1 
HETATM 11118 C  C9  . 946 AA 4 .   ? 74.495  79.196  -10.602 1.00 70.97 ? 202 946 H C9  1 
HETATM 11119 C  C10 . 946 AA 4 .   ? 73.724  80.396  -12.524 1.00 78.05 ? 202 946 H C10 1 
HETATM 11120 C  C11 . 946 AA 4 .   ? 73.384  80.421  -13.869 1.00 71.23 ? 202 946 H C11 1 
HETATM 11121 C  C12 . 946 AA 4 .   ? 72.952  81.591  -14.447 1.00 77.26 ? 202 946 H C12 1 
HETATM 11122 C  C13 . 946 AA 4 .   ? 72.876  82.755  -13.693 1.00 80.20 ? 202 946 H C13 1 
HETATM 11123 C  C14 . 946 AA 4 .   ? 73.228  82.732  -12.353 1.00 81.88 ? 202 946 H C14 1 
HETATM 11124 C  C15 . 946 AA 4 .   ? 73.644  81.548  -11.774 1.00 80.66 ? 202 946 H C15 1 
HETATM 11125 C  C16 . 946 AA 4 .   ? 73.982  81.535  -10.446 1.00 77.25 ? 202 946 H C16 1 
HETATM 11126 C  C17 . 946 AA 4 .   ? 74.389  80.365  -9.859  1.00 69.80 ? 202 946 H C17 1 
HETATM 11127 C  C18 . 946 AA 4 .   ? 74.315  73.670  -7.772  1.00 47.94 ? 202 946 H C18 1 
HETATM 11128 C  C19 . 946 AA 4 .   ? 74.151  79.214  -11.946 1.00 72.49 ? 202 946 H C19 1 
HETATM 11129 N  N1  . 946 AA 4 .   ? 75.743  76.986  -10.715 1.00 49.83 ? 202 946 H N1  1 
HETATM 11130 ZN ZN  . ZN  BA 2 .   ? 57.768  56.301  -56.983 1.00 29.37 ? 201 ZN  I ZN  1 
HETATM 11131 O  O   . HOH CA 6 .   ? 79.842  30.254  -31.257 1.00 60.90 ? 301 HOH A O   1 
HETATM 11132 O  O   . HOH CA 6 .   ? 86.099  52.593  -16.904 1.00 30.77 ? 302 HOH A O   1 
HETATM 11133 O  O   . HOH CA 6 .   ? 74.881  53.149  -35.515 1.00 50.70 ? 303 HOH A O   1 
HETATM 11134 O  O   . HOH CA 6 .   ? 94.140  40.903  -20.404 1.00 35.91 ? 304 HOH A O   1 
HETATM 11135 O  O   . HOH CA 6 .   ? 89.574  41.060  -8.002  1.00 39.07 ? 305 HOH A O   1 
HETATM 11136 O  O   . HOH CA 6 .   ? 73.659  50.882  -31.962 1.00 32.31 ? 306 HOH A O   1 
HETATM 11137 O  O   . HOH CA 6 .   ? 72.122  45.803  -35.374 1.00 41.85 ? 307 HOH A O   1 
HETATM 11138 O  O   . HOH CA 6 .   ? 67.917  43.165  -36.344 1.00 41.18 ? 308 HOH A O   1 
HETATM 11139 O  O   . HOH CA 6 .   ? 69.512  54.008  -25.161 1.00 32.25 ? 309 HOH A O   1 
HETATM 11140 O  O   . HOH CA 6 .   ? 77.103  37.821  -10.954 1.00 32.82 ? 310 HOH A O   1 
HETATM 11141 O  O   . HOH CA 6 .   ? 84.903  36.590  -33.138 1.00 44.36 ? 311 HOH A O   1 
HETATM 11142 O  O   . HOH CA 6 .   ? 84.861  58.048  -20.242 1.00 32.58 ? 312 HOH A O   1 
HETATM 11143 O  O   . HOH CA 6 .   ? 76.573  54.169  -2.983  1.00 45.32 ? 313 HOH A O   1 
HETATM 11144 O  O   . HOH CA 6 .   ? 65.196  46.725  -4.812  1.00 28.80 ? 314 HOH A O   1 
HETATM 11145 O  O   . HOH CA 6 .   ? 83.679  42.341  -14.358 1.00 27.50 ? 315 HOH A O   1 
HETATM 11146 O  O   . HOH CA 6 .   ? 90.637  41.669  -23.190 1.00 30.58 ? 316 HOH A O   1 
HETATM 11147 O  O   . HOH CA 6 .   ? 76.620  66.450  -18.531 1.00 29.70 ? 317 HOH A O   1 
HETATM 11148 O  O   . HOH CA 6 .   ? 71.183  33.589  -32.226 1.00 35.89 ? 318 HOH A O   1 
HETATM 11149 O  O   . HOH CA 6 .   ? 93.813  40.670  -9.827  1.00 45.40 ? 319 HOH A O   1 
HETATM 11150 O  O   . HOH CA 6 .   ? 51.549  50.664  -13.521 1.00 51.01 ? 320 HOH A O   1 
HETATM 11151 O  O   . HOH CA 6 .   ? 92.441  31.236  -11.322 1.00 55.35 ? 321 HOH A O   1 
HETATM 11152 O  O   . HOH CA 6 .   ? 62.828  44.525  -4.608  1.00 35.77 ? 322 HOH A O   1 
HETATM 11153 O  O   . HOH CA 6 .   ? 79.124  37.699  -16.564 1.00 27.96 ? 323 HOH A O   1 
HETATM 11154 O  O   . HOH CA 6 .   ? 72.174  48.819  -2.353  1.00 36.60 ? 324 HOH A O   1 
HETATM 11155 O  O   . HOH CA 6 .   ? 78.869  38.605  -35.440 1.00 36.84 ? 325 HOH A O   1 
HETATM 11156 O  O   . HOH CA 6 .   ? 86.036  39.068  -27.737 1.00 45.56 ? 326 HOH A O   1 
HETATM 11157 O  O   . HOH CA 6 .   ? 90.289  36.285  -16.810 1.00 39.54 ? 327 HOH A O   1 
HETATM 11158 O  O   . HOH CA 6 .   ? 58.491  41.611  -4.989  1.00 50.70 ? 328 HOH A O   1 
HETATM 11159 O  O   . HOH CA 6 .   ? 68.298  46.970  -2.074  1.00 28.89 ? 329 HOH A O   1 
HETATM 11160 O  O   . HOH CA 6 .   ? 67.755  34.131  -18.375 1.00 56.04 ? 330 HOH A O   1 
HETATM 11161 O  O   . HOH CA 6 .   ? 93.306  47.855  -22.520 1.00 47.69 ? 331 HOH A O   1 
HETATM 11162 O  O   . HOH CA 6 .   ? 70.534  39.499  2.099   1.00 46.54 ? 332 HOH A O   1 
HETATM 11163 O  O   . HOH CA 6 .   ? 89.156  37.355  -11.498 1.00 46.46 ? 333 HOH A O   1 
HETATM 11164 O  O   . HOH CA 6 .   ? 69.258  33.992  -29.994 1.00 53.74 ? 334 HOH A O   1 
HETATM 11165 O  O   . HOH CA 6 .   ? 79.474  52.682  -30.590 1.00 39.84 ? 335 HOH A O   1 
HETATM 11166 O  O   . HOH CA 6 .   ? 67.852  36.397  -29.222 1.00 53.72 ? 336 HOH A O   1 
HETATM 11167 O  O   . HOH CA 6 .   ? 95.696  35.451  -15.889 1.00 34.40 ? 337 HOH A O   1 
HETATM 11168 O  O   . HOH CA 6 .   ? 72.955  32.953  -28.278 1.00 35.12 ? 338 HOH A O   1 
HETATM 11169 O  O   . HOH CA 6 .   ? 64.320  51.627  -6.167  1.00 47.73 ? 339 HOH A O   1 
HETATM 11170 O  O   . HOH CA 6 .   ? 89.706  50.044  -10.032 1.00 39.07 ? 340 HOH A O   1 
HETATM 11171 O  O   . HOH CA 6 .   ? 77.818  67.282  -21.283 1.00 30.16 ? 341 HOH A O   1 
HETATM 11172 O  O   . HOH CA 6 .   ? 83.915  58.964  -10.572 1.00 35.66 ? 342 HOH A O   1 
HETATM 11173 O  O   . HOH CA 6 .   ? 81.850  54.904  -8.582  1.00 39.71 ? 343 HOH A O   1 
HETATM 11174 O  O   . HOH CA 6 .   ? 73.344  54.058  -5.974  1.00 33.11 ? 344 HOH A O   1 
HETATM 11175 O  O   . HOH CA 6 .   ? 80.356  32.284  -28.910 1.00 34.56 ? 345 HOH A O   1 
HETATM 11176 O  O   . HOH CA 6 .   ? 66.842  53.331  -2.731  1.00 39.74 ? 346 HOH A O   1 
HETATM 11177 O  O   . HOH CA 6 .   ? 85.748  48.304  -19.099 1.00 31.99 ? 347 HOH A O   1 
HETATM 11178 O  O   . HOH CA 6 .   ? 80.084  45.078  -33.286 1.00 30.60 ? 348 HOH A O   1 
HETATM 11179 O  O   . HOH CA 6 .   ? 85.655  54.989  -5.810  1.00 53.89 ? 349 HOH A O   1 
HETATM 11180 O  O   . HOH CA 6 .   ? 87.620  36.977  -4.116  1.00 47.55 ? 350 HOH A O   1 
HETATM 11181 O  O   . HOH CA 6 .   ? 72.989  30.324  -30.920 1.00 52.33 ? 351 HOH A O   1 
HETATM 11182 O  O   . HOH CA 6 .   ? 94.645  52.288  -16.725 1.00 58.57 ? 352 HOH A O   1 
HETATM 11183 O  O   . HOH CA 6 .   ? 77.373  38.918  -2.700  1.00 55.31 ? 353 HOH A O   1 
HETATM 11184 O  O   . HOH CA 6 .   ? 85.606  53.190  -10.832 1.00 42.76 ? 354 HOH A O   1 
HETATM 11185 O  O   . HOH CA 6 .   ? 88.392  39.888  -26.525 1.00 39.99 ? 355 HOH A O   1 
HETATM 11186 O  O   . HOH CA 6 .   ? 84.691  53.858  -26.202 1.00 27.90 ? 356 HOH A O   1 
HETATM 11187 O  O   . HOH CA 6 .   ? 57.475  46.602  -18.042 1.00 45.54 ? 357 HOH A O   1 
HETATM 11188 O  O   . HOH CA 6 .   ? 72.210  55.160  -25.643 1.00 34.04 ? 358 HOH A O   1 
HETATM 11189 O  O   . HOH CA 6 .   ? 62.395  44.963  -17.519 1.00 28.01 ? 359 HOH A O   1 
HETATM 11190 O  O   . HOH CA 6 .   ? 76.408  58.046  -6.350  1.00 43.53 ? 360 HOH A O   1 
HETATM 11191 O  O   . HOH CA 6 .   ? 88.826  38.961  -4.498  1.00 42.89 ? 361 HOH A O   1 
HETATM 11192 O  O   . HOH CA 6 .   ? 57.977  47.982  -7.961  1.00 52.55 ? 362 HOH A O   1 
HETATM 11193 O  O   . HOH CA 6 .   ? 87.332  49.393  -21.104 1.00 38.92 ? 363 HOH A O   1 
HETATM 11194 O  O   . HOH CA 6 .   ? 75.581  33.889  -15.778 1.00 35.66 ? 364 HOH A O   1 
HETATM 11195 O  O   . HOH CA 6 .   ? 71.560  42.206  -4.689  1.00 26.45 ? 365 HOH A O   1 
HETATM 11196 O  O   . HOH CA 6 .   ? 81.346  29.039  -34.033 1.00 55.01 ? 366 HOH A O   1 
HETATM 11197 O  O   . HOH CA 6 .   ? 96.361  41.370  -13.019 1.00 32.01 ? 367 HOH A O   1 
HETATM 11198 O  O   . HOH CA 6 .   ? 65.787  39.377  -5.190  1.00 27.06 ? 368 HOH A O   1 
HETATM 11199 O  O   . HOH CA 6 .   ? 82.630  46.901  -4.547  1.00 31.98 ? 369 HOH A O   1 
HETATM 11200 O  O   . HOH CA 6 .   ? 67.426  52.736  -21.526 1.00 15.08 ? 370 HOH A O   1 
HETATM 11201 O  O   . HOH CA 6 .   ? 82.311  42.211  -3.646  1.00 49.84 ? 371 HOH A O   1 
HETATM 11202 O  O   . HOH CA 6 .   ? 88.163  36.620  -19.274 1.00 37.52 ? 372 HOH A O   1 
HETATM 11203 O  O   . HOH CA 6 .   ? 82.518  49.219  -5.500  1.00 24.95 ? 373 HOH A O   1 
HETATM 11204 O  O   . HOH CA 6 .   ? 77.533  58.668  -8.559  1.00 30.58 ? 374 HOH A O   1 
HETATM 11205 O  O   . HOH CA 6 .   ? 61.702  44.841  -21.920 1.00 32.17 ? 375 HOH A O   1 
HETATM 11206 O  O   . HOH CA 6 .   ? 71.899  61.023  -20.080 1.00 17.24 ? 376 HOH A O   1 
HETATM 11207 O  O   . HOH CA 6 .   ? 89.225  44.245  -30.500 1.00 57.96 ? 377 HOH A O   1 
HETATM 11208 O  O   . HOH CA 6 .   ? 86.077  56.423  -22.249 1.00 37.78 ? 378 HOH A O   1 
HETATM 11209 O  O   . HOH CA 6 .   ? 76.897  37.940  -7.225  1.00 33.04 ? 379 HOH A O   1 
HETATM 11210 O  O   . HOH CA 6 .   ? 65.787  41.603  -24.823 1.00 34.07 ? 380 HOH A O   1 
HETATM 11211 O  O   . HOH CA 6 .   ? 74.442  34.142  -26.557 1.00 31.88 ? 381 HOH A O   1 
HETATM 11212 O  O   . HOH CA 6 .   ? 69.203  55.423  -22.381 1.00 22.75 ? 382 HOH A O   1 
HETATM 11213 O  O   . HOH CA 6 .   ? 62.165  43.255  -15.492 1.00 40.07 ? 383 HOH A O   1 
HETATM 11214 O  O   . HOH CA 6 .   ? 86.074  35.666  -26.912 1.00 33.44 ? 384 HOH A O   1 
HETATM 11215 O  O   . HOH CA 6 .   ? 74.386  64.378  -27.072 1.00 42.26 ? 385 HOH A O   1 
HETATM 11216 O  O   . HOH CA 6 .   ? 84.205  55.929  -24.320 1.00 49.86 ? 386 HOH A O   1 
HETATM 11217 O  O   . HOH CA 6 .   ? 73.430  56.360  -21.989 1.00 47.04 ? 387 HOH A O   1 
HETATM 11218 O  O   . HOH CA 6 .   ? 70.600  30.504  -35.255 1.00 60.26 ? 388 HOH A O   1 
HETATM 11219 O  O   . HOH CA 6 .   ? 95.714  51.070  -21.330 1.00 53.84 ? 389 HOH A O   1 
HETATM 11220 O  O   . HOH CA 6 .   ? 84.003  43.907  -30.980 1.00 33.18 ? 390 HOH A O   1 
HETATM 11221 O  O   A HOH CA 6 .   ? 68.590  49.865  -29.405 0.50 19.66 ? 391 HOH A O   1 
HETATM 11222 O  O   B HOH CA 6 .   ? 67.621  48.469  -28.811 0.50 27.09 ? 391 HOH A O   1 
HETATM 11223 O  O   . HOH CA 6 .   ? 91.579  32.336  -14.580 1.00 55.31 ? 392 HOH A O   1 
HETATM 11224 O  O   . HOH CA 6 .   ? 77.680  49.819  -31.952 1.00 30.78 ? 393 HOH A O   1 
HETATM 11225 O  O   . HOH CA 6 .   ? 83.417  51.779  -29.934 1.00 46.26 ? 394 HOH A O   1 
HETATM 11226 O  O   . HOH CA 6 .   ? 100.318 48.675  -16.678 1.00 38.10 ? 395 HOH A O   1 
HETATM 11227 O  O   . HOH CA 6 .   ? 73.517  41.052  -35.639 1.00 44.05 ? 396 HOH A O   1 
HETATM 11228 O  O   . HOH CA 6 .   ? 77.488  29.970  -31.849 1.00 34.73 ? 397 HOH A O   1 
HETATM 11229 O  O   . HOH CA 6 .   ? 59.057  37.013  -12.535 1.00 60.59 ? 398 HOH A O   1 
HETATM 11230 O  O   A HOH CA 6 .   ? 80.751  38.443  -5.390  0.50 32.68 ? 399 HOH A O   1 
HETATM 11231 O  O   B HOH CA 6 .   ? 81.389  39.618  -4.696  0.50 32.06 ? 399 HOH A O   1 
HETATM 11232 O  O   . HOH CA 6 .   ? 75.673  57.172  -21.270 1.00 40.69 ? 400 HOH A O   1 
HETATM 11233 O  O   . HOH CA 6 .   ? 81.555  43.596  -31.592 1.00 27.97 ? 401 HOH A O   1 
HETATM 11234 O  O   . HOH CA 6 .   ? 86.665  51.616  -14.250 1.00 26.19 ? 402 HOH A O   1 
HETATM 11235 O  O   . HOH CA 6 .   ? 75.485  35.148  -13.178 1.00 33.65 ? 403 HOH A O   1 
HETATM 11236 O  O   . HOH CA 6 .   ? 67.517  36.608  -24.772 1.00 43.04 ? 404 HOH A O   1 
HETATM 11237 O  O   . HOH CA 6 .   ? 84.736  54.129  -0.929  1.00 48.46 ? 405 HOH A O   1 
HETATM 11238 O  O   . HOH CA 6 .   ? 57.604  50.584  -11.437 1.00 37.94 ? 406 HOH A O   1 
HETATM 11239 O  O   . HOH CA 6 .   ? 79.129  56.370  -27.839 1.00 45.64 ? 407 HOH A O   1 
HETATM 11240 O  O   . HOH CA 6 .   ? 73.652  36.013  -7.222  1.00 42.45 ? 408 HOH A O   1 
HETATM 11241 O  O   . HOH CA 6 .   ? 59.992  48.676  -10.535 1.00 30.91 ? 409 HOH A O   1 
HETATM 11242 O  O   . HOH CA 6 .   ? 90.288  48.817  -21.913 1.00 41.47 ? 410 HOH A O   1 
HETATM 11243 O  O   . HOH CA 6 .   ? 65.849  37.837  0.759   1.00 47.02 ? 411 HOH A O   1 
HETATM 11244 O  O   . HOH CA 6 .   ? 81.210  37.477  -35.618 1.00 35.31 ? 412 HOH A O   1 
HETATM 11245 O  O   . HOH CA 6 .   ? 74.614  56.532  1.968   1.00 48.94 ? 413 HOH A O   1 
HETATM 11246 O  O   . HOH CA 6 .   ? 81.941  55.637  -26.183 1.00 52.91 ? 414 HOH A O   1 
HETATM 11247 O  O   . HOH CA 6 .   ? 63.414  42.105  -23.639 1.00 40.99 ? 415 HOH A O   1 
HETATM 11248 O  O   . HOH CA 6 .   ? 97.885  49.059  -18.365 1.00 34.52 ? 416 HOH A O   1 
HETATM 11249 O  O   . HOH CA 6 .   ? 68.825  35.828  -15.243 1.00 38.83 ? 417 HOH A O   1 
HETATM 11250 O  O   . HOH CA 6 .   ? 64.814  38.412  -8.416  1.00 43.17 ? 418 HOH A O   1 
HETATM 11251 O  O   . HOH CA 6 .   ? 75.049  56.199  -27.054 1.00 52.00 ? 419 HOH A O   1 
HETATM 11252 O  O   . HOH CA 6 .   ? 60.997  44.897  -2.768  1.00 40.68 ? 420 HOH A O   1 
HETATM 11253 O  O   . HOH CA 6 .   ? 83.815  35.881  -12.075 1.00 28.12 ? 421 HOH A O   1 
HETATM 11254 O  O   . HOH CA 6 .   ? 50.974  52.392  -16.954 1.00 50.66 ? 422 HOH A O   1 
HETATM 11255 O  O   A HOH CA 6 .   ? 85.862  57.096  -17.560 0.50 12.30 ? 423 HOH A O   1 
HETATM 11256 O  O   B HOH CA 6 .   ? 86.072  58.306  -17.899 0.50 36.65 ? 423 HOH A O   1 
HETATM 11257 O  O   . HOH CA 6 .   ? 87.338  54.369  -17.579 1.00 42.82 ? 424 HOH A O   1 
HETATM 11258 O  O   . HOH CA 6 .   ? 71.262  38.001  -2.179  1.00 44.74 ? 425 HOH A O   1 
HETATM 11259 O  O   . HOH CA 6 .   ? 68.534  42.570  -29.629 1.00 44.94 ? 426 HOH A O   1 
HETATM 11260 O  O   . HOH CA 6 .   ? 66.467  42.804  -27.686 1.00 50.41 ? 427 HOH A O   1 
HETATM 11261 O  O   . HOH CA 6 .   ? 89.271  52.560  -6.422  1.00 47.11 ? 428 HOH A O   1 
HETATM 11262 O  O   . HOH CA 6 .   ? 80.435  55.952  -6.574  1.00 41.61 ? 429 HOH A O   1 
HETATM 11263 O  O   . HOH CA 6 .   ? 85.820  48.497  -31.546 1.00 60.97 ? 430 HOH A O   1 
HETATM 11264 O  O   . HOH CA 6 .   ? 69.105  54.944  -4.729  1.00 56.31 ? 431 HOH A O   1 
HETATM 11265 O  O   . HOH CA 6 .   ? 66.353  40.649  -34.545 1.00 46.91 ? 432 HOH A O   1 
HETATM 11266 O  O   . HOH CA 6 .   ? 70.415  31.003  -25.548 1.00 49.46 ? 433 HOH A O   1 
HETATM 11267 O  O   . HOH CA 6 .   ? 87.746  53.838  -26.637 1.00 55.34 ? 434 HOH A O   1 
HETATM 11268 O  O   . HOH CA 6 .   ? 58.467  50.521  -8.808  1.00 56.22 ? 435 HOH A O   1 
HETATM 11269 O  O   . HOH CA 6 .   ? 53.361  51.335  -19.309 1.00 44.03 ? 436 HOH A O   1 
HETATM 11270 O  O   . HOH CA 6 .   ? 81.373  45.000  -3.499  1.00 47.39 ? 437 HOH A O   1 
HETATM 11271 O  O   . HOH CA 6 .   ? 67.461  45.844  -30.035 1.00 54.77 ? 438 HOH A O   1 
HETATM 11272 O  O   . HOH CA 6 .   ? 55.061  49.471  -11.239 1.00 38.67 ? 439 HOH A O   1 
HETATM 11273 O  O   . HOH CA 6 .   ? 79.142  44.759  -1.746  1.00 54.67 ? 440 HOH A O   1 
HETATM 11274 O  O   . HOH CA 6 .   ? 69.765  58.593  -22.986 1.00 37.77 ? 441 HOH A O   1 
HETATM 11275 O  O   . HOH CA 6 .   ? 97.754  48.902  -20.860 1.00 51.54 ? 442 HOH A O   1 
HETATM 11276 O  O   . HOH CA 6 .   ? 68.855  36.379  -0.917  1.00 48.02 ? 443 HOH A O   1 
HETATM 11277 O  O   . HOH CA 6 .   ? 86.376  34.863  -18.573 1.00 42.99 ? 444 HOH A O   1 
HETATM 11278 O  O   . HOH CA 6 .   ? 65.512  38.326  -24.711 1.00 50.01 ? 445 HOH A O   1 
HETATM 11279 O  O   . HOH CA 6 .   ? 88.018  52.759  -12.603 1.00 43.77 ? 446 HOH A O   1 
HETATM 11280 O  O   . HOH CA 6 .   ? 89.562  34.358  -15.063 1.00 50.07 ? 447 HOH A O   1 
HETATM 11281 O  O   . HOH CA 6 .   ? 67.228  54.553  -23.464 1.00 46.91 ? 448 HOH A O   1 
HETATM 11282 O  O   . HOH CA 6 .   ? 95.563  35.406  -11.390 1.00 50.53 ? 449 HOH A O   1 
HETATM 11283 O  O   . HOH CA 6 .   ? 81.408  51.778  -32.107 1.00 52.52 ? 450 HOH A O   1 
HETATM 11284 O  O   . HOH CA 6 .   ? 90.379  38.253  -21.605 1.00 43.44 ? 451 HOH A O   1 
HETATM 11285 O  O   . HOH CA 6 .   ? 90.110  56.597  -21.530 1.00 55.73 ? 452 HOH A O   1 
HETATM 11286 O  O   . HOH CA 6 .   ? 97.637  39.081  -12.095 1.00 48.61 ? 453 HOH A O   1 
HETATM 11287 O  O   . HOH CA 6 .   ? 78.081  56.392  -5.054  1.00 37.57 ? 454 HOH A O   1 
HETATM 11288 O  O   . HOH CA 6 .   ? 77.881  35.967  -12.787 1.00 44.16 ? 455 HOH A O   1 
HETATM 11289 O  O   . HOH CA 6 .   ? 71.403  51.835  -32.649 1.00 45.77 ? 456 HOH A O   1 
HETATM 11290 O  O   . HOH CA 6 .   ? 78.196  54.464  -1.079  1.00 57.85 ? 457 HOH A O   1 
HETATM 11291 O  O   . HOH CA 6 .   ? 93.561  42.120  -22.652 1.00 50.39 ? 458 HOH A O   1 
HETATM 11292 O  O   . HOH CA 6 .   ? 70.146  35.170  -34.246 1.00 42.65 ? 459 HOH A O   1 
HETATM 11293 O  O   . HOH CA 6 .   ? 70.747  39.638  -35.127 1.00 28.02 ? 460 HOH A O   1 
HETATM 11294 O  O   . HOH CA 6 .   ? 80.088  48.455  -32.803 1.00 37.58 ? 461 HOH A O   1 
HETATM 11295 O  O   . HOH CA 6 .   ? 85.958  57.220  -9.712  1.00 47.79 ? 462 HOH A O   1 
HETATM 11296 O  O   . HOH CA 6 .   ? 65.171  36.943  -4.323  1.00 44.80 ? 463 HOH A O   1 
HETATM 11297 O  O   . HOH CA 6 .   ? 87.493  58.156  -15.711 1.00 45.73 ? 464 HOH A O   1 
HETATM 11298 O  O   . HOH CA 6 .   ? 83.041  32.174  -27.346 1.00 52.60 ? 465 HOH A O   1 
HETATM 11299 O  O   . HOH CA 6 .   ? 92.179  35.339  -18.306 1.00 51.99 ? 466 HOH A O   1 
HETATM 11300 O  O   . HOH CA 6 .   ? 89.020  55.346  -12.839 1.00 50.22 ? 467 HOH A O   1 
HETATM 11301 O  O   . HOH CA 6 .   ? 68.581  39.304  -33.142 1.00 40.99 ? 468 HOH A O   1 
HETATM 11302 O  O   . HOH CA 6 .   ? 88.431  36.419  -25.399 1.00 47.44 ? 469 HOH A O   1 
HETATM 11303 O  O   . HOH CA 6 .   ? 86.245  32.460  -24.879 1.00 44.31 ? 470 HOH A O   1 
HETATM 11304 O  O   . HOH CA 6 .   ? 88.757  33.036  -21.398 1.00 54.68 ? 471 HOH A O   1 
HETATM 11305 O  O   . HOH CA 6 .   ? 90.244  32.481  -19.052 1.00 45.50 ? 472 HOH A O   1 
HETATM 11306 O  O   . HOH DA 6 .   ? 57.991  66.401  -3.306  1.00 47.89 ? 301 HOH B O   1 
HETATM 11307 O  O   . HOH DA 6 .   ? 48.361  64.286  -31.123 1.00 55.72 ? 302 HOH B O   1 
HETATM 11308 O  O   . HOH DA 6 .   ? 46.549  75.008  -13.823 1.00 30.64 ? 303 HOH B O   1 
HETATM 11309 O  O   . HOH DA 6 .   ? 70.342  77.672  -26.924 1.00 35.68 ? 304 HOH B O   1 
HETATM 11310 O  O   . HOH DA 6 .   ? 51.268  53.296  -14.360 1.00 42.54 ? 305 HOH B O   1 
HETATM 11311 O  O   . HOH DA 6 .   ? 68.093  65.293  -3.448  1.00 44.23 ? 306 HOH B O   1 
HETATM 11312 O  O   . HOH DA 6 .   ? 67.414  80.386  -30.880 1.00 29.89 ? 307 HOH B O   1 
HETATM 11313 O  O   . HOH DA 6 .   ? 65.262  63.175  -32.191 1.00 24.75 ? 308 HOH B O   1 
HETATM 11314 O  O   . HOH DA 6 .   ? 58.194  47.282  -24.784 1.00 43.50 ? 309 HOH B O   1 
HETATM 11315 O  O   . HOH DA 6 .   ? 63.438  64.988  -1.664  1.00 36.15 ? 310 HOH B O   1 
HETATM 11316 O  O   . HOH DA 6 .   ? 70.386  59.057  -25.996 1.00 39.29 ? 311 HOH B O   1 
HETATM 11317 O  O   . HOH DA 6 .   ? 57.654  79.630  -36.506 1.00 48.37 ? 312 HOH B O   1 
HETATM 11318 O  O   . HOH DA 6 .   ? 42.434  63.868  -7.091  1.00 39.88 ? 313 HOH B O   1 
HETATM 11319 O  O   . HOH DA 6 .   ? 68.017  59.525  -25.064 1.00 29.07 ? 314 HOH B O   1 
HETATM 11320 O  O   . HOH DA 6 .   ? 50.217  60.430  -19.949 1.00 28.91 ? 315 HOH B O   1 
HETATM 11321 O  O   . HOH DA 6 .   ? 49.259  66.130  -3.767  1.00 47.24 ? 316 HOH B O   1 
HETATM 11322 O  O   . HOH DA 6 .   ? 57.679  83.045  -36.563 1.00 50.13 ? 317 HOH B O   1 
HETATM 11323 O  O   . HOH DA 6 .   ? 44.866  70.939  -11.011 1.00 33.26 ? 318 HOH B O   1 
HETATM 11324 O  O   . HOH DA 6 .   ? 65.283  83.378  -29.536 1.00 40.68 ? 319 HOH B O   1 
HETATM 11325 O  O   . HOH DA 6 .   ? 52.258  74.706  -29.563 1.00 39.90 ? 320 HOH B O   1 
HETATM 11326 O  O   . HOH DA 6 .   ? 40.710  66.703  -25.994 1.00 40.72 ? 321 HOH B O   1 
HETATM 11327 O  O   . HOH DA 6 .   ? 48.502  56.966  -5.060  1.00 40.62 ? 322 HOH B O   1 
HETATM 11328 O  O   . HOH DA 6 .   ? 57.790  74.663  -11.143 1.00 31.86 ? 323 HOH B O   1 
HETATM 11329 O  O   . HOH DA 6 .   ? 45.632  76.479  -19.662 1.00 31.79 ? 324 HOH B O   1 
HETATM 11330 O  O   . HOH DA 6 .   ? 57.223  74.045  -7.362  1.00 39.24 ? 325 HOH B O   1 
HETATM 11331 O  O   . HOH DA 6 .   ? 55.946  50.616  -19.850 1.00 30.65 ? 326 HOH B O   1 
HETATM 11332 O  O   . HOH DA 6 .   ? 46.624  71.909  -26.024 1.00 28.38 ? 327 HOH B O   1 
HETATM 11333 O  O   . HOH DA 6 .   ? 67.025  69.119  -34.910 1.00 47.42 ? 328 HOH B O   1 
HETATM 11334 O  O   . HOH DA 6 .   ? 57.189  57.071  -5.559  1.00 38.00 ? 329 HOH B O   1 
HETATM 11335 O  O   . HOH DA 6 .   ? 53.236  51.438  -11.497 1.00 45.37 ? 330 HOH B O   1 
HETATM 11336 O  O   . HOH DA 6 .   ? 61.997  68.821  -4.275  1.00 31.70 ? 331 HOH B O   1 
HETATM 11337 O  O   . HOH DA 6 .   ? 39.398  71.129  -16.799 1.00 19.65 ? 332 HOH B O   1 
HETATM 11338 O  O   . HOH DA 6 .   ? 51.838  70.341  -16.297 1.00 17.87 ? 333 HOH B O   1 
HETATM 11339 O  O   . HOH DA 6 .   ? 58.942  57.321  -29.566 1.00 47.09 ? 334 HOH B O   1 
HETATM 11340 O  O   . HOH DA 6 .   ? 45.483  68.232  -3.882  1.00 50.98 ? 335 HOH B O   1 
HETATM 11341 O  O   . HOH DA 6 .   ? 65.186  58.421  -26.188 1.00 36.51 ? 336 HOH B O   1 
HETATM 11342 O  O   . HOH DA 6 .   ? 67.251  54.667  -26.368 1.00 38.93 ? 337 HOH B O   1 
HETATM 11343 O  O   . HOH DA 6 .   ? 59.066  69.398  -34.402 1.00 30.25 ? 338 HOH B O   1 
HETATM 11344 O  O   . HOH DA 6 .   ? 77.869  63.641  -15.638 1.00 28.11 ? 339 HOH B O   1 
HETATM 11345 O  O   . HOH DA 6 .   ? 59.323  61.246  -32.130 1.00 41.32 ? 340 HOH B O   1 
HETATM 11346 O  O   . HOH DA 6 .   ? 78.451  66.527  -15.205 1.00 40.88 ? 341 HOH B O   1 
HETATM 11347 O  O   . HOH DA 6 .   ? 46.045  76.192  -8.045  1.00 39.79 ? 342 HOH B O   1 
HETATM 11348 O  O   . HOH DA 6 .   ? 53.780  75.009  -31.521 1.00 42.54 ? 343 HOH B O   1 
HETATM 11349 O  O   . HOH DA 6 .   ? 54.179  77.296  -34.414 1.00 36.93 ? 344 HOH B O   1 
HETATM 11350 O  O   . HOH DA 6 .   ? 60.998  63.022  -2.763  1.00 22.67 ? 345 HOH B O   1 
HETATM 11351 O  O   . HOH DA 6 .   ? 56.692  75.226  -17.162 1.00 20.60 ? 346 HOH B O   1 
HETATM 11352 O  O   . HOH DA 6 .   ? 70.439  67.596  -2.965  1.00 38.65 ? 347 HOH B O   1 
HETATM 11353 O  O   . HOH DA 6 .   ? 60.622  79.841  -17.083 1.00 32.36 ? 348 HOH B O   1 
HETATM 11354 O  O   . HOH DA 6 .   ? 69.371  60.387  -21.065 1.00 13.52 ? 349 HOH B O   1 
HETATM 11355 O  O   . HOH DA 6 .   ? 62.775  57.450  -9.355  1.00 45.58 ? 350 HOH B O   1 
HETATM 11356 O  O   . HOH DA 6 .   ? 53.122  57.219  -11.332 1.00 25.75 ? 351 HOH B O   1 
HETATM 11357 O  O   . HOH DA 6 .   ? 53.007  57.382  -27.137 1.00 51.56 ? 352 HOH B O   1 
HETATM 11358 O  O   . HOH DA 6 .   ? 57.869  49.370  -18.234 1.00 27.58 ? 353 HOH B O   1 
HETATM 11359 O  O   . HOH DA 6 .   ? 65.603  74.260  -33.946 1.00 29.82 ? 354 HOH B O   1 
HETATM 11360 O  O   . HOH DA 6 .   ? 55.366  81.311  -23.868 1.00 19.14 ? 355 HOH B O   1 
HETATM 11361 O  O   . HOH DA 6 .   ? 70.422  67.603  1.147   1.00 47.13 ? 356 HOH B O   1 
HETATM 11362 O  O   . HOH DA 6 .   ? 45.225  72.834  -7.198  1.00 31.29 ? 357 HOH B O   1 
HETATM 11363 O  O   . HOH DA 6 .   ? 74.853  68.453  -19.691 1.00 38.94 ? 358 HOH B O   1 
HETATM 11364 O  O   . HOH DA 6 .   ? 44.132  65.509  -26.496 1.00 39.90 ? 359 HOH B O   1 
HETATM 11365 O  O   . HOH DA 6 .   ? 65.139  80.715  -27.173 1.00 28.52 ? 360 HOH B O   1 
HETATM 11366 O  O   . HOH DA 6 .   ? 57.800  81.527  -29.144 1.00 38.07 ? 361 HOH B O   1 
HETATM 11367 O  O   . HOH DA 6 .   ? 51.864  55.215  -23.288 1.00 32.07 ? 362 HOH B O   1 
HETATM 11368 O  O   . HOH DA 6 .   ? 50.713  64.954  -21.831 1.00 22.83 ? 363 HOH B O   1 
HETATM 11369 O  O   . HOH DA 6 .   ? 41.056  61.075  -21.295 1.00 63.44 ? 364 HOH B O   1 
HETATM 11370 O  O   . HOH DA 6 .   ? 47.692  58.811  -13.169 1.00 38.40 ? 365 HOH B O   1 
HETATM 11371 O  O   . HOH DA 6 .   ? 69.621  60.888  -4.677  1.00 47.83 ? 366 HOH B O   1 
HETATM 11372 O  O   . HOH DA 6 .   ? 54.686  70.137  -32.572 1.00 24.37 ? 367 HOH B O   1 
HETATM 11373 O  O   . HOH DA 6 .   ? 49.769  63.756  -24.115 1.00 33.35 ? 368 HOH B O   1 
HETATM 11374 O  O   . HOH DA 6 .   ? 67.555  57.666  -22.488 1.00 23.94 ? 369 HOH B O   1 
HETATM 11375 O  O   . HOH DA 6 .   ? 42.341  72.226  -24.018 1.00 22.73 ? 370 HOH B O   1 
HETATM 11376 O  O   . HOH DA 6 .   ? 48.213  76.294  -21.678 1.00 33.42 ? 371 HOH B O   1 
HETATM 11377 O  O   . HOH DA 6 .   ? 43.862  62.358  -5.001  1.00 39.49 ? 372 HOH B O   1 
HETATM 11378 O  O   . HOH DA 6 .   ? 73.787  61.330  -27.332 1.00 41.44 ? 373 HOH B O   1 
HETATM 11379 O  O   . HOH DA 6 .   ? 58.026  84.743  -34.667 1.00 54.27 ? 374 HOH B O   1 
HETATM 11380 O  O   . HOH DA 6 .   ? 54.237  82.678  -12.875 1.00 34.24 ? 375 HOH B O   1 
HETATM 11381 O  O   . HOH DA 6 .   ? 60.561  57.915  -7.174  1.00 26.68 ? 376 HOH B O   1 
HETATM 11382 O  O   . HOH DA 6 .   ? 49.441  60.094  -14.469 1.00 32.52 ? 377 HOH B O   1 
HETATM 11383 O  O   . HOH DA 6 .   ? 51.948  78.033  -28.386 1.00 31.49 ? 378 HOH B O   1 
HETATM 11384 O  O   . HOH DA 6 .   ? 59.996  46.479  -20.695 1.00 35.03 ? 379 HOH B O   1 
HETATM 11385 O  O   . HOH DA 6 .   ? 64.049  52.053  -28.525 1.00 47.71 ? 380 HOH B O   1 
HETATM 11386 O  O   . HOH DA 6 .   ? 64.766  52.157  -21.187 1.00 19.01 ? 381 HOH B O   1 
HETATM 11387 O  O   . HOH DA 6 .   ? 45.249  62.005  -13.839 1.00 26.55 ? 382 HOH B O   1 
HETATM 11388 O  O   . HOH DA 6 .   ? 57.343  48.250  -21.992 1.00 44.37 ? 383 HOH B O   1 
HETATM 11389 O  O   . HOH DA 6 .   ? 57.822  76.801  -36.018 1.00 29.42 ? 384 HOH B O   1 
HETATM 11390 O  O   . HOH DA 6 .   ? 51.515  62.548  -7.918  1.00 18.16 ? 385 HOH B O   1 
HETATM 11391 O  O   . HOH DA 6 .   ? 38.766  76.476  -17.839 1.00 27.32 ? 386 HOH B O   1 
HETATM 11392 O  O   . HOH DA 6 .   ? 56.802  70.834  -2.402  1.00 46.45 ? 387 HOH B O   1 
HETATM 11393 O  O   . HOH DA 6 .   ? 46.584  75.229  -6.026  1.00 40.35 ? 388 HOH B O   1 
HETATM 11394 O  O   . HOH DA 6 .   ? 84.472  59.993  -12.537 1.00 27.64 ? 389 HOH B O   1 
HETATM 11395 O  O   . HOH DA 6 .   ? 67.445  72.491  -3.464  1.00 25.79 ? 390 HOH B O   1 
HETATM 11396 O  O   . HOH DA 6 .   ? 56.981  53.451  -10.890 1.00 31.39 ? 391 HOH B O   1 
HETATM 11397 O  O   . HOH DA 6 .   ? 52.568  72.956  -6.564  1.00 44.18 ? 392 HOH B O   1 
HETATM 11398 O  O   . HOH DA 6 .   ? 51.413  64.943  -6.781  1.00 23.09 ? 393 HOH B O   1 
HETATM 11399 O  O   . HOH DA 6 .   ? 57.489  70.424  -32.535 1.00 21.31 ? 394 HOH B O   1 
HETATM 11400 O  O   . HOH DA 6 .   ? 44.144  73.175  -13.207 1.00 37.03 ? 395 HOH B O   1 
HETATM 11401 O  O   . HOH DA 6 .   ? 61.197  71.325  -2.575  1.00 36.63 ? 396 HOH B O   1 
HETATM 11402 O  O   . HOH DA 6 .   ? 61.137  83.916  -31.273 1.00 36.57 ? 397 HOH B O   1 
HETATM 11403 O  O   . HOH DA 6 .   ? 66.540  76.947  -36.719 1.00 43.40 ? 398 HOH B O   1 
HETATM 11404 O  O   . HOH DA 6 .   ? 69.693  76.989  -22.912 1.00 37.63 ? 399 HOH B O   1 
HETATM 11405 O  O   . HOH DA 6 .   ? 49.434  73.896  -28.854 1.00 29.34 ? 400 HOH B O   1 
HETATM 11406 O  O   . HOH DA 6 .   ? 73.421  67.986  -15.309 1.00 30.32 ? 401 HOH B O   1 
HETATM 11407 O  O   . HOH DA 6 .   ? 49.175  56.672  -10.154 1.00 47.91 ? 402 HOH B O   1 
HETATM 11408 O  O   . HOH DA 6 .   ? 53.315  59.707  -28.998 1.00 24.55 ? 403 HOH B O   1 
HETATM 11409 O  O   . HOH DA 6 .   ? 73.042  69.325  -13.395 1.00 48.63 ? 404 HOH B O   1 
HETATM 11410 O  O   . HOH DA 6 .   ? 49.068  61.014  -17.535 1.00 23.28 ? 405 HOH B O   1 
HETATM 11411 O  O   . HOH DA 6 .   ? 74.669  63.712  -8.457  1.00 28.73 ? 406 HOH B O   1 
HETATM 11412 O  O   . HOH DA 6 .   ? 42.621  68.671  -14.489 1.00 38.66 ? 407 HOH B O   1 
HETATM 11413 O  O   . HOH DA 6 .   ? 61.876  70.852  -36.912 1.00 34.20 ? 408 HOH B O   1 
HETATM 11414 O  O   . HOH DA 6 .   ? 61.704  77.175  -36.952 1.00 48.93 ? 409 HOH B O   1 
HETATM 11415 O  O   . HOH DA 6 .   ? 60.678  56.120  -23.202 1.00 29.64 ? 410 HOH B O   1 
HETATM 11416 O  O   . HOH DA 6 .   ? 51.030  76.217  -13.293 1.00 20.53 ? 411 HOH B O   1 
HETATM 11417 O  O   . HOH DA 6 .   ? 61.159  64.377  -33.002 1.00 28.00 ? 412 HOH B O   1 
HETATM 11418 O  O   . HOH DA 6 .   ? 38.337  63.946  -22.911 1.00 24.86 ? 413 HOH B O   1 
HETATM 11419 O  O   . HOH DA 6 .   ? 59.145  78.417  -10.261 1.00 43.16 ? 414 HOH B O   1 
HETATM 11420 O  O   . HOH DA 6 .   ? 66.293  58.249  -2.491  1.00 42.58 ? 415 HOH B O   1 
HETATM 11421 O  O   . HOH DA 6 .   ? 51.578  69.327  -5.443  1.00 29.01 ? 416 HOH B O   1 
HETATM 11422 O  O   . HOH DA 6 .   ? 59.714  77.502  -13.057 1.00 25.26 ? 417 HOH B O   1 
HETATM 11423 O  O   . HOH DA 6 .   ? 77.123  61.526  -9.136  1.00 36.96 ? 418 HOH B O   1 
HETATM 11424 O  O   . HOH DA 6 .   ? 55.258  61.961  -32.117 1.00 40.23 ? 419 HOH B O   1 
HETATM 11425 O  O   . HOH DA 6 .   ? 58.758  59.737  -30.457 1.00 37.36 ? 420 HOH B O   1 
HETATM 11426 O  O   . HOH DA 6 .   ? 46.846  64.622  -25.124 1.00 38.45 ? 421 HOH B O   1 
HETATM 11427 O  O   . HOH DA 6 .   ? 71.679  71.945  -22.732 1.00 27.63 ? 422 HOH B O   1 
HETATM 11428 O  O   . HOH DA 6 .   ? 64.195  49.100  -28.234 1.00 49.76 ? 423 HOH B O   1 
HETATM 11429 O  O   . HOH DA 6 .   ? 65.000  62.823  0.254   1.00 48.34 ? 424 HOH B O   1 
HETATM 11430 O  O   . HOH DA 6 .   ? 67.131  73.494  5.515   1.00 54.54 ? 425 HOH B O   1 
HETATM 11431 O  O   . HOH DA 6 .   ? 57.871  53.442  -8.412  1.00 45.14 ? 426 HOH B O   1 
HETATM 11432 O  O   . HOH DA 6 .   ? 42.440  80.658  -13.893 1.00 37.10 ? 427 HOH B O   1 
HETATM 11433 O  O   . HOH DA 6 .   ? 54.391  82.848  -33.460 1.00 57.31 ? 428 HOH B O   1 
HETATM 11434 O  O   . HOH DA 6 .   ? 41.456  72.461  -13.085 1.00 43.79 ? 429 HOH B O   1 
HETATM 11435 O  O   . HOH DA 6 .   ? 46.356  78.989  -17.893 1.00 46.60 ? 430 HOH B O   1 
HETATM 11436 O  O   . HOH DA 6 .   ? 65.546  60.798  -35.484 1.00 52.30 ? 431 HOH B O   1 
HETATM 11437 O  O   . HOH DA 6 .   ? 71.173  70.851  -26.220 1.00 40.18 ? 432 HOH B O   1 
HETATM 11438 O  O   . HOH DA 6 .   ? 76.989  65.233  -7.918  1.00 52.57 ? 433 HOH B O   1 
HETATM 11439 O  O   . HOH DA 6 .   ? 49.060  58.337  -20.944 1.00 36.46 ? 434 HOH B O   1 
HETATM 11440 O  O   . HOH DA 6 .   ? 52.953  55.477  -4.992  1.00 49.59 ? 435 HOH B O   1 
HETATM 11441 O  O   . HOH DA 6 .   ? 60.146  76.054  -7.059  1.00 47.57 ? 436 HOH B O   1 
HETATM 11442 O  O   . HOH DA 6 .   ? 43.073  58.803  -6.066  1.00 52.16 ? 437 HOH B O   1 
HETATM 11443 O  O   . HOH DA 6 .   ? 74.925  76.238  2.053   1.00 51.53 ? 438 HOH B O   1 
HETATM 11444 O  O   A HOH DA 6 .   ? 62.799  57.491  -28.323 0.50 25.07 ? 439 HOH B O   1 
HETATM 11445 O  O   B HOH DA 6 .   ? 63.886  57.847  -29.871 0.50 33.38 ? 439 HOH B O   1 
HETATM 11446 O  O   . HOH DA 6 .   ? 54.630  73.955  -6.581  1.00 41.59 ? 440 HOH B O   1 
HETATM 11447 O  O   . HOH DA 6 .   ? 42.556  61.694  -9.140  1.00 47.56 ? 441 HOH B O   1 
HETATM 11448 O  O   . HOH DA 6 .   ? 50.591  56.196  -21.058 1.00 28.28 ? 442 HOH B O   1 
HETATM 11449 O  O   . HOH DA 6 .   ? 65.419  56.863  -23.910 1.00 38.73 ? 443 HOH B O   1 
HETATM 11450 O  O   . HOH DA 6 .   ? 76.179  64.362  -5.664  1.00 49.04 ? 444 HOH B O   1 
HETATM 11451 O  O   . HOH DA 6 .   ? 72.721  58.718  -5.522  1.00 50.25 ? 445 HOH B O   1 
HETATM 11452 O  O   . HOH DA 6 .   ? 69.663  71.115  -28.465 1.00 46.80 ? 446 HOH B O   1 
HETATM 11453 O  O   . HOH DA 6 .   ? 44.933  59.482  -10.546 1.00 45.11 ? 447 HOH B O   1 
HETATM 11454 O  O   . HOH DA 6 .   ? 54.512  50.560  -24.483 1.00 50.19 ? 448 HOH B O   1 
HETATM 11455 O  O   . HOH DA 6 .   ? 70.308  56.815  -28.072 1.00 53.73 ? 449 HOH B O   1 
HETATM 11456 O  O   . HOH DA 6 .   ? 51.398  56.792  -25.407 1.00 40.37 ? 450 HOH B O   1 
HETATM 11457 O  O   . HOH DA 6 .   ? 53.507  80.163  -32.337 1.00 50.05 ? 451 HOH B O   1 
HETATM 11458 O  O   . HOH DA 6 .   ? 56.127  55.328  -1.260  1.00 53.41 ? 452 HOH B O   1 
HETATM 11459 O  O   . HOH DA 6 .   ? 48.894  61.396  -28.653 1.00 58.76 ? 453 HOH B O   1 
HETATM 11460 O  O   . HOH DA 6 .   ? 53.917  56.000  -9.241  1.00 40.30 ? 454 HOH B O   1 
HETATM 11461 O  O   . HOH DA 6 .   ? 39.318  64.458  -25.407 1.00 50.83 ? 455 HOH B O   1 
HETATM 11462 O  O   . HOH DA 6 .   ? 63.136  56.796  -22.598 1.00 39.58 ? 456 HOH B O   1 
HETATM 11463 O  O   A HOH DA 6 .   ? 82.122  61.919  -9.211  0.50 35.27 ? 457 HOH B O   1 
HETATM 11464 O  O   B HOH DA 6 .   ? 82.906  60.413  -8.731  0.50 32.82 ? 457 HOH B O   1 
HETATM 11465 O  O   . HOH DA 6 .   ? 71.779  74.573  -23.081 1.00 48.57 ? 458 HOH B O   1 
HETATM 11466 O  O   . HOH DA 6 .   ? 63.201  79.577  -13.421 1.00 39.26 ? 459 HOH B O   1 
HETATM 11467 O  O   . HOH DA 6 .   ? 66.750  71.977  -35.644 1.00 52.05 ? 460 HOH B O   1 
HETATM 11468 O  O   . HOH DA 6 .   ? 34.429  62.049  -20.780 1.00 39.96 ? 461 HOH B O   1 
HETATM 11469 O  O   . HOH DA 6 .   ? 54.890  81.212  -30.436 1.00 50.45 ? 462 HOH B O   1 
HETATM 11470 O  O   . HOH DA 6 .   ? 52.635  73.380  -34.945 1.00 55.95 ? 463 HOH B O   1 
HETATM 11471 O  O   . HOH DA 6 .   ? 51.166  74.381  -4.617  1.00 46.96 ? 464 HOH B O   1 
HETATM 11472 O  O   . HOH DA 6 .   ? 76.067  67.562  -15.652 1.00 52.67 ? 465 HOH B O   1 
HETATM 11473 O  O   . HOH DA 6 .   ? 43.965  71.782  -4.673  1.00 49.61 ? 466 HOH B O   1 
HETATM 11474 O  O   . HOH DA 6 .   ? 59.997  46.056  -18.589 1.00 47.86 ? 467 HOH B O   1 
HETATM 11475 O  O   . HOH DA 6 .   ? 46.483  74.332  -24.560 1.00 39.84 ? 468 HOH B O   1 
HETATM 11476 O  O   . HOH DA 6 .   ? 53.773  66.529  -3.099  1.00 43.41 ? 469 HOH B O   1 
HETATM 11477 O  O   . HOH DA 6 .   ? 55.999  55.523  -7.302  1.00 36.44 ? 470 HOH B O   1 
HETATM 11478 O  O   . HOH DA 6 .   ? 59.392  70.550  -37.314 1.00 47.04 ? 471 HOH B O   1 
HETATM 11479 O  O   . HOH DA 6 .   ? 55.944  76.749  -11.084 1.00 41.35 ? 472 HOH B O   1 
HETATM 11480 O  O   . HOH DA 6 .   ? 49.380  54.514  -19.713 1.00 50.14 ? 473 HOH B O   1 
HETATM 11481 O  O   . HOH DA 6 .   ? 60.351  65.968  -2.324  1.00 46.51 ? 474 HOH B O   1 
HETATM 11482 O  O   . HOH DA 6 .   ? 71.947  66.551  -1.227  1.00 52.14 ? 475 HOH B O   1 
HETATM 11483 O  O   . HOH DA 6 .   ? 49.316  57.122  -13.304 1.00 49.92 ? 476 HOH B O   1 
HETATM 11484 O  O   . HOH DA 6 .   ? 46.904  59.336  -17.235 1.00 45.81 ? 477 HOH B O   1 
HETATM 11485 O  O   . HOH DA 6 .   ? 38.825  60.968  -22.495 1.00 47.48 ? 478 HOH B O   1 
HETATM 11486 O  O   . HOH DA 6 .   ? 61.222  64.699  -39.283 1.00 47.13 ? 479 HOH B O   1 
HETATM 11487 O  O   . HOH DA 6 .   ? 55.102  77.372  -8.945  1.00 53.10 ? 480 HOH B O   1 
HETATM 11488 O  O   . HOH DA 6 .   ? 39.798  74.363  -14.090 1.00 40.89 ? 481 HOH B O   1 
HETATM 11489 O  O   . HOH DA 6 .   ? 54.541  82.267  -8.938  1.00 38.39 ? 482 HOH B O   1 
HETATM 11490 O  O   . HOH DA 6 .   ? 43.068  57.778  -15.716 1.00 55.81 ? 483 HOH B O   1 
HETATM 11491 O  O   . HOH DA 6 .   ? 46.990  73.242  -28.460 1.00 41.71 ? 484 HOH B O   1 
HETATM 11492 O  O   . HOH DA 6 .   ? 71.910  68.814  -27.769 1.00 49.74 ? 485 HOH B O   1 
HETATM 11493 O  O   . HOH DA 6 .   ? 54.722  81.198  -28.041 1.00 48.65 ? 486 HOH B O   1 
HETATM 11494 O  O   . HOH DA 6 .   ? 43.659  73.062  -8.936  1.00 38.38 ? 487 HOH B O   1 
HETATM 11495 O  O   . HOH DA 6 .   ? 37.863  73.238  -15.647 1.00 26.09 ? 488 HOH B O   1 
HETATM 11496 O  O   . HOH DA 6 .   ? 43.721  76.703  -21.765 1.00 47.08 ? 489 HOH B O   1 
HETATM 11497 O  O   . HOH DA 6 .   ? 48.703  79.465  -9.775  1.00 48.10 ? 490 HOH B O   1 
HETATM 11498 O  O   . HOH DA 6 .   ? 57.358  62.380  -33.747 1.00 46.08 ? 491 HOH B O   1 
HETATM 11499 O  O   . HOH DA 6 .   ? 69.872  72.936  -35.729 1.00 57.46 ? 492 HOH B O   1 
HETATM 11500 O  O   . HOH DA 6 .   ? 67.414  74.771  -1.895  1.00 48.93 ? 493 HOH B O   1 
HETATM 11501 O  O   . HOH DA 6 .   ? 80.961  66.263  -6.776  1.00 42.79 ? 494 HOH B O   1 
HETATM 11502 O  O   . HOH DA 6 .   ? 83.287  64.003  -8.140  1.00 46.04 ? 495 HOH B O   1 
HETATM 11503 O  O   . HOH DA 6 .   ? 40.224  76.674  -15.301 1.00 29.88 ? 496 HOH B O   1 
HETATM 11504 O  O   . HOH DA 6 .   ? 43.717  71.499  -26.150 1.00 34.08 ? 497 HOH B O   1 
HETATM 11505 O  O   . HOH DA 6 .   ? 72.692  76.986  -26.017 1.00 55.25 ? 498 HOH B O   1 
HETATM 11506 O  O   . HOH DA 6 .   ? 45.687  59.739  -15.131 1.00 45.53 ? 499 HOH B O   1 
HETATM 11507 O  O   . HOH DA 6 .   ? 47.616  77.003  -23.836 1.00 44.45 ? 500 HOH B O   1 
HETATM 11508 O  O   . HOH DA 6 .   ? 52.321  66.763  -5.125  1.00 41.63 ? 501 HOH B O   1 
HETATM 11509 O  O   . HOH DA 6 .   ? 58.693  66.446  -34.568 1.00 38.28 ? 502 HOH B O   1 
HETATM 11510 O  O   . HOH DA 6 .   ? 53.793  75.271  -36.323 1.00 39.53 ? 503 HOH B O   1 
HETATM 11511 O  O   . HOH DA 6 .   ? 52.088  80.659  -27.045 1.00 44.73 ? 504 HOH B O   1 
HETATM 11512 O  O   . HOH DA 6 .   ? 68.736  74.870  -33.672 1.00 33.68 ? 505 HOH B O   1 
HETATM 11513 O  O   . HOH DA 6 .   ? 43.865  74.535  -24.551 1.00 36.84 ? 506 HOH B O   1 
HETATM 11514 O  O   . HOH DA 6 .   ? 41.832  69.089  -10.338 1.00 46.52 ? 507 HOH B O   1 
HETATM 11515 O  O   . HOH DA 6 .   ? 64.387  70.996  -37.673 1.00 41.29 ? 508 HOH B O   1 
HETATM 11516 O  O   . HOH DA 6 .   ? 56.652  82.556  -39.139 1.00 55.07 ? 509 HOH B O   1 
HETATM 11517 O  O   . HOH DA 6 .   ? 47.069  55.525  -23.432 1.00 55.20 ? 510 HOH B O   1 
HETATM 11518 O  O   . HOH DA 6 .   ? 61.597  43.990  -24.574 1.00 48.54 ? 511 HOH B O   1 
HETATM 11519 O  O   . HOH DA 6 .   ? 49.473  77.134  -27.759 1.00 46.12 ? 512 HOH B O   1 
HETATM 11520 O  O   . HOH DA 6 .   ? 72.647  73.148  -32.081 1.00 61.89 ? 513 HOH B O   1 
HETATM 11521 O  O   . HOH DA 6 .   ? 70.134  74.728  -31.477 1.00 45.26 ? 514 HOH B O   1 
HETATM 11522 O  O   . HOH DA 6 .   ? 70.663  77.576  -30.211 1.00 53.17 ? 515 HOH B O   1 
HETATM 11523 O  O   . HOH DA 6 .   ? 48.006  77.097  -26.012 1.00 47.24 ? 516 HOH B O   1 
HETATM 11524 O  O   . HOH DA 6 .   ? 48.795  80.317  -23.457 1.00 46.79 ? 517 HOH B O   1 
HETATM 11525 O  O   . HOH DA 6 .   ? 44.977  78.307  -24.146 1.00 49.88 ? 518 HOH B O   1 
HETATM 11526 O  O   . HOH EA 6 .   ? 52.414  105.363 -32.656 1.00 38.63 ? 301 HOH C O   1 
HETATM 11527 O  O   . HOH EA 6 .   ? 43.596  115.304 -14.586 1.00 41.86 ? 302 HOH C O   1 
HETATM 11528 O  O   . HOH EA 6 .   ? 59.251  111.549 -26.386 1.00 36.08 ? 303 HOH C O   1 
HETATM 11529 O  O   . HOH EA 6 .   ? 51.736  110.612 -1.620  1.00 58.09 ? 304 HOH C O   1 
HETATM 11530 O  O   . HOH EA 6 .   ? 49.935  107.020 -3.252  1.00 43.17 ? 305 HOH C O   1 
HETATM 11531 O  O   . HOH EA 6 .   ? 60.067  90.376  -31.167 1.00 51.53 ? 306 HOH C O   1 
HETATM 11532 O  O   . HOH EA 6 .   ? 57.865  85.996  -4.035  1.00 44.30 ? 307 HOH C O   1 
HETATM 11533 O  O   . HOH EA 6 .   ? 64.406  96.818  -26.332 1.00 39.65 ? 308 HOH C O   1 
HETATM 11534 O  O   . HOH EA 6 .   ? 51.798  103.314 -1.767  1.00 35.83 ? 309 HOH C O   1 
HETATM 11535 O  O   . HOH EA 6 .   ? 51.349  83.569  -13.893 1.00 28.08 ? 310 HOH C O   1 
HETATM 11536 O  O   . HOH EA 6 .   ? 62.107  92.715  -27.191 1.00 52.97 ? 311 HOH C O   1 
HETATM 11537 O  O   . HOH EA 6 .   ? 62.389  93.888  -20.153 1.00 31.53 ? 312 HOH C O   1 
HETATM 11538 O  O   . HOH EA 6 .   ? 54.730  109.876 -25.096 1.00 33.47 ? 313 HOH C O   1 
HETATM 11539 O  O   . HOH EA 6 .   ? 56.825  84.308  -11.511 1.00 29.23 ? 314 HOH C O   1 
HETATM 11540 O  O   . HOH EA 6 .   ? 63.023  85.504  -6.872  1.00 41.21 ? 315 HOH C O   1 
HETATM 11541 O  O   . HOH EA 6 .   ? 38.134  88.938  -35.484 1.00 41.39 ? 316 HOH C O   1 
HETATM 11542 O  O   . HOH EA 6 .   ? 47.724  89.752  -31.578 1.00 37.48 ? 317 HOH C O   1 
HETATM 11543 O  O   . HOH EA 6 .   ? 46.334  92.602  -17.125 1.00 17.34 ? 318 HOH C O   1 
HETATM 11544 O  O   . HOH EA 6 .   ? 36.512  99.115  -31.176 1.00 41.40 ? 319 HOH C O   1 
HETATM 11545 O  O   . HOH EA 6 .   ? 68.163  103.522 -20.040 1.00 30.74 ? 320 HOH C O   1 
HETATM 11546 O  O   . HOH EA 6 .   ? 68.453  77.331  -20.722 1.00 29.68 ? 321 HOH C O   1 
HETATM 11547 O  O   . HOH EA 6 .   ? 47.092  93.618  -7.228  1.00 41.86 ? 322 HOH C O   1 
HETATM 11548 O  O   . HOH EA 6 .   ? 45.826  88.885  -34.026 1.00 39.77 ? 323 HOH C O   1 
HETATM 11549 O  O   . HOH EA 6 .   ? 52.897  90.609  -16.317 1.00 20.99 ? 324 HOH C O   1 
HETATM 11550 O  O   . HOH EA 6 .   ? 50.330  96.972  -34.524 1.00 21.73 ? 325 HOH C O   1 
HETATM 11551 O  O   . HOH EA 6 .   ? 50.563  89.996  -6.568  1.00 46.18 ? 326 HOH C O   1 
HETATM 11552 O  O   . HOH EA 6 .   ? 40.495  93.648  -16.854 1.00 39.87 ? 327 HOH C O   1 
HETATM 11553 O  O   . HOH EA 6 .   ? 53.919  112.456 -25.962 1.00 47.18 ? 328 HOH C O   1 
HETATM 11554 O  O   . HOH EA 6 .   ? 69.722  109.212 -20.470 1.00 39.44 ? 329 HOH C O   1 
HETATM 11555 O  O   . HOH EA 6 .   ? 35.039  96.022  -29.355 1.00 46.16 ? 330 HOH C O   1 
HETATM 11556 O  O   . HOH EA 6 .   ? 53.329  110.663 -21.204 1.00 16.25 ? 331 HOH C O   1 
HETATM 11557 O  O   . HOH EA 6 .   ? 46.231  93.640  -11.094 1.00 32.51 ? 332 HOH C O   1 
HETATM 11558 O  O   . HOH EA 6 .   ? 41.197  86.317  -13.039 1.00 34.33 ? 333 HOH C O   1 
HETATM 11559 O  O   . HOH EA 6 .   ? 63.795  97.950  -11.512 1.00 25.92 ? 334 HOH C O   1 
HETATM 11560 O  O   . HOH EA 6 .   ? 55.225  84.067  -10.764 1.00 35.73 ? 335 HOH C O   1 
HETATM 11561 O  O   . HOH EA 6 .   ? 43.659  111.717 -19.743 1.00 37.24 ? 336 HOH C O   1 
HETATM 11562 O  O   . HOH EA 6 .   ? 46.486  116.863 -15.702 1.00 29.58 ? 337 HOH C O   1 
HETATM 11563 O  O   . HOH EA 6 .   ? 38.891  101.624 -20.562 1.00 29.26 ? 338 HOH C O   1 
HETATM 11564 O  O   . HOH EA 6 .   ? 49.031  100.739 -1.514  1.00 54.38 ? 339 HOH C O   1 
HETATM 11565 O  O   . HOH EA 6 .   ? 63.126  93.472  -14.568 1.00 35.29 ? 340 HOH C O   1 
HETATM 11566 O  O   . HOH EA 6 .   ? 66.192  93.784  -4.955  1.00 40.09 ? 341 HOH C O   1 
HETATM 11567 O  O   . HOH EA 6 .   ? 40.555  99.242  -37.257 1.00 45.52 ? 342 HOH C O   1 
HETATM 11568 O  O   . HOH EA 6 .   ? 65.465  89.588  -21.963 1.00 43.52 ? 343 HOH C O   1 
HETATM 11569 O  O   . HOH EA 6 .   ? 51.865  92.747  -32.614 1.00 24.23 ? 344 HOH C O   1 
HETATM 11570 O  O   . HOH EA 6 .   ? 59.712  91.966  -24.134 1.00 29.62 ? 345 HOH C O   1 
HETATM 11571 O  O   . HOH EA 6 .   ? 44.081  95.528  -6.864  1.00 41.15 ? 346 HOH C O   1 
HETATM 11572 O  O   . HOH EA 6 .   ? 63.926  87.628  -5.087  1.00 38.44 ? 347 HOH C O   1 
HETATM 11573 O  O   . HOH EA 6 .   ? 66.063  97.784  -23.388 1.00 35.47 ? 348 HOH C O   1 
HETATM 11574 O  O   . HOH EA 6 .   ? 59.977  93.976  -8.038  1.00 19.19 ? 349 HOH C O   1 
HETATM 11575 O  O   . HOH EA 6 .   ? 46.946  108.115 -3.085  1.00 45.09 ? 350 HOH C O   1 
HETATM 11576 O  O   . HOH EA 6 .   ? 44.731  110.677 -15.758 1.00 30.65 ? 351 HOH C O   1 
HETATM 11577 O  O   . HOH EA 6 .   ? 63.302  88.802  -13.846 1.00 27.70 ? 352 HOH C O   1 
HETATM 11578 O  O   . HOH EA 6 .   ? 57.165  101.467 -32.396 1.00 36.50 ? 353 HOH C O   1 
HETATM 11579 O  O   . HOH EA 6 .   ? 57.928  92.707  -6.853  1.00 22.21 ? 354 HOH C O   1 
HETATM 11580 O  O   . HOH EA 6 .   ? 37.453  97.191  -27.151 1.00 28.18 ? 355 HOH C O   1 
HETATM 11581 O  O   . HOH EA 6 .   ? 54.040  85.189  -26.078 1.00 28.85 ? 356 HOH C O   1 
HETATM 11582 O  O   . HOH EA 6 .   ? 48.893  92.760  -3.525  1.00 48.98 ? 357 HOH C O   1 
HETATM 11583 O  O   . HOH EA 6 .   ? 57.243  107.807 -26.428 1.00 42.95 ? 358 HOH C O   1 
HETATM 11584 O  O   . HOH EA 6 .   ? 62.052  101.524 -5.542  1.00 40.94 ? 359 HOH C O   1 
HETATM 11585 O  O   . HOH EA 6 .   ? 52.918  98.200  -3.372  1.00 49.87 ? 360 HOH C O   1 
HETATM 11586 O  O   . HOH EA 6 .   ? 68.389  98.136  -14.878 1.00 41.10 ? 361 HOH C O   1 
HETATM 11587 O  O   . HOH EA 6 .   ? 48.676  88.611  -29.558 1.00 41.12 ? 362 HOH C O   1 
HETATM 11588 O  O   . HOH EA 6 .   ? 58.045  79.414  -16.643 1.00 17.42 ? 363 HOH C O   1 
HETATM 11589 O  O   . HOH EA 6 .   ? 53.681  106.616 -36.006 1.00 47.30 ? 364 HOH C O   1 
HETATM 11590 O  O   . HOH EA 6 .   ? 40.126  90.279  -29.026 1.00 31.95 ? 365 HOH C O   1 
HETATM 11591 O  O   . HOH EA 6 .   ? 61.259  102.442 -29.680 1.00 44.69 ? 366 HOH C O   1 
HETATM 11592 O  O   . HOH EA 6 .   ? 59.695  104.310 -7.302  1.00 27.24 ? 367 HOH C O   1 
HETATM 11593 O  O   . HOH EA 6 .   ? 55.005  102.122 -2.853  1.00 22.40 ? 368 HOH C O   1 
HETATM 11594 O  O   A HOH EA 6 .   ? 50.339  82.029  -19.818 0.50 15.67 ? 369 HOH C O   1 
HETATM 11595 O  O   B HOH EA 6 .   ? 50.868  80.692  -21.421 0.50 28.08 ? 369 HOH C O   1 
HETATM 11596 O  O   . HOH EA 6 .   ? 53.732  101.517 -33.194 1.00 29.62 ? 370 HOH C O   1 
HETATM 11597 O  O   . HOH EA 6 .   ? 36.440  92.165  -31.130 1.00 33.58 ? 371 HOH C O   1 
HETATM 11598 O  O   . HOH EA 6 .   ? 43.010  100.399 -34.270 1.00 20.32 ? 372 HOH C O   1 
HETATM 11599 O  O   . HOH EA 6 .   ? 57.770  90.327  -3.502  1.00 46.25 ? 373 HOH C O   1 
HETATM 11600 O  O   . HOH EA 6 .   ? 58.085  92.216  -21.831 1.00 24.65 ? 374 HOH C O   1 
HETATM 11601 O  O   . HOH EA 6 .   ? 69.656  105.889 -22.115 1.00 47.52 ? 375 HOH C O   1 
HETATM 11602 O  O   . HOH EA 6 .   ? 61.446  96.738  -29.092 1.00 22.63 ? 376 HOH C O   1 
HETATM 11603 O  O   . HOH EA 6 .   ? 52.174  77.473  -19.754 1.00 28.26 ? 377 HOH C O   1 
HETATM 11604 O  O   . HOH EA 6 .   ? 56.612  108.993 -2.637  1.00 42.43 ? 378 HOH C O   1 
HETATM 11605 O  O   . HOH EA 6 .   ? 62.716  110.612 -21.336 1.00 20.03 ? 379 HOH C O   1 
HETATM 11606 O  O   . HOH EA 6 .   ? 51.068  86.798  -28.908 1.00 29.57 ? 380 HOH C O   1 
HETATM 11607 O  O   . HOH EA 6 .   ? 49.130  100.279 -4.325  1.00 34.17 ? 381 HOH C O   1 
HETATM 11608 O  O   . HOH EA 6 .   ? 53.783  83.587  -7.140  1.00 35.84 ? 382 HOH C O   1 
HETATM 11609 O  O   . HOH EA 6 .   ? 60.174  88.773  -25.214 1.00 37.17 ? 383 HOH C O   1 
HETATM 11610 O  O   . HOH EA 6 .   ? 62.299  99.418  -28.506 1.00 40.50 ? 384 HOH C O   1 
HETATM 11611 O  O   . HOH EA 6 .   ? 38.623  103.019 -23.118 1.00 42.33 ? 385 HOH C O   1 
HETATM 11612 O  O   . HOH EA 6 .   ? 46.316  114.575 -6.137  1.00 57.75 ? 386 HOH C O   1 
HETATM 11613 O  O   . HOH EA 6 .   ? 56.544  110.405 -22.736 1.00 22.68 ? 387 HOH C O   1 
HETATM 11614 O  O   . HOH EA 6 .   ? 39.389  96.083  -25.707 1.00 20.86 ? 388 HOH C O   1 
HETATM 11615 O  O   . HOH EA 6 .   ? 43.482  103.547 -3.823  1.00 28.88 ? 389 HOH C O   1 
HETATM 11616 O  O   . HOH EA 6 .   ? 43.593  109.764 -13.616 1.00 36.84 ? 390 HOH C O   1 
HETATM 11617 O  O   . HOH EA 6 .   ? 66.301  94.829  -10.042 1.00 48.28 ? 391 HOH C O   1 
HETATM 11618 O  O   . HOH EA 6 .   ? 49.149  84.492  -21.467 1.00 38.46 ? 392 HOH C O   1 
HETATM 11619 O  O   . HOH EA 6 .   ? 50.129  95.007  -32.568 1.00 20.38 ? 393 HOH C O   1 
HETATM 11620 O  O   . HOH EA 6 .   ? 58.908  83.428  -14.466 1.00 30.60 ? 394 HOH C O   1 
HETATM 11621 O  O   . HOH EA 6 .   ? 45.964  86.659  -28.126 1.00 28.83 ? 395 HOH C O   1 
HETATM 11622 O  O   . HOH EA 6 .   ? 62.380  92.568  -17.715 1.00 26.05 ? 396 HOH C O   1 
HETATM 11623 O  O   . HOH EA 6 .   ? 65.271  103.008 -10.875 1.00 33.57 ? 397 HOH C O   1 
HETATM 11624 O  O   . HOH EA 6 .   ? 61.165  105.158 -23.216 1.00 31.54 ? 398 HOH C O   1 
HETATM 11625 O  O   . HOH EA 6 .   ? 64.523  81.890  -23.483 1.00 17.44 ? 399 HOH C O   1 
HETATM 11626 O  O   . HOH EA 6 .   ? 48.997  80.831  -13.136 1.00 43.23 ? 400 HOH C O   1 
HETATM 11627 O  O   . HOH EA 6 .   ? 65.112  92.599  -13.256 1.00 36.64 ? 401 HOH C O   1 
HETATM 11628 O  O   . HOH EA 6 .   ? 48.244  77.071  -13.893 1.00 36.51 ? 402 HOH C O   1 
HETATM 11629 O  O   . HOH EA 6 .   ? 42.899  94.041  -13.196 1.00 24.30 ? 403 HOH C O   1 
HETATM 11630 O  O   . HOH EA 6 .   ? 63.220  79.471  -25.700 1.00 21.88 ? 404 HOH C O   1 
HETATM 11631 O  O   . HOH EA 6 .   ? 42.289  107.056 -23.245 1.00 30.88 ? 405 HOH C O   1 
HETATM 11632 O  O   . HOH EA 6 .   ? 59.253  106.606 -28.567 1.00 50.27 ? 406 HOH C O   1 
HETATM 11633 O  O   . HOH EA 6 .   ? 41.717  109.068 -21.511 1.00 41.31 ? 407 HOH C O   1 
HETATM 11634 O  O   . HOH EA 6 .   ? 48.059  87.126  -13.223 1.00 21.18 ? 408 HOH C O   1 
HETATM 11635 O  O   . HOH EA 6 .   ? 53.929  76.055  -17.465 1.00 27.04 ? 409 HOH C O   1 
HETATM 11636 O  O   . HOH EA 6 .   ? 49.931  94.667  -2.587  1.00 52.24 ? 410 HOH C O   1 
HETATM 11637 O  O   . HOH EA 6 .   ? 42.917  102.623 5.373   1.00 48.49 ? 411 HOH C O   1 
HETATM 11638 O  O   . HOH EA 6 .   ? 67.972  100.486 -21.776 1.00 48.55 ? 412 HOH C O   1 
HETATM 11639 O  O   . HOH EA 6 .   ? 64.596  93.806  -21.202 1.00 36.11 ? 413 HOH C O   1 
HETATM 11640 O  O   A HOH EA 6 .   ? 47.868  113.746 -8.715  0.50 17.22 ? 414 HOH C O   1 
HETATM 11641 O  O   B HOH EA 6 .   ? 46.117  114.606 -8.699  0.50 39.84 ? 414 HOH C O   1 
HETATM 11642 O  O   . HOH EA 6 .   ? 64.755  104.135 -8.577  1.00 40.03 ? 415 HOH C O   1 
HETATM 11643 O  O   . HOH EA 6 .   ? 53.997  90.909  -5.523  1.00 36.59 ? 416 HOH C O   1 
HETATM 11644 O  O   . HOH EA 6 .   ? 41.583  92.146  -36.531 1.00 47.64 ? 417 HOH C O   1 
HETATM 11645 O  O   . HOH EA 6 .   ? 65.111  86.906  -9.309  1.00 45.79 ? 418 HOH C O   1 
HETATM 11646 O  O   . HOH EA 6 .   ? 55.755  80.511  -13.048 1.00 30.94 ? 419 HOH C O   1 
HETATM 11647 O  O   . HOH EA 6 .   ? 61.863  104.805 0.933   1.00 51.44 ? 420 HOH C O   1 
HETATM 11648 O  O   . HOH EA 6 .   ? 47.570  98.462  -2.763  1.00 48.10 ? 421 HOH C O   1 
HETATM 11649 O  O   . HOH EA 6 .   ? 51.003  89.147  -31.426 1.00 49.66 ? 422 HOH C O   1 
HETATM 11650 O  O   . HOH EA 6 .   ? 58.857  97.519  -32.156 1.00 46.03 ? 423 HOH C O   1 
HETATM 11651 O  O   . HOH EA 6 .   ? 40.266  100.393 -13.976 1.00 37.20 ? 424 HOH C O   1 
HETATM 11652 O  O   . HOH EA 6 .   ? 61.070  82.830  -27.174 1.00 41.07 ? 425 HOH C O   1 
HETATM 11653 O  O   . HOH EA 6 .   ? 46.557  80.476  -13.833 1.00 55.24 ? 426 HOH C O   1 
HETATM 11654 O  O   . HOH EA 6 .   ? 65.233  96.189  -12.836 1.00 58.10 ? 427 HOH C O   1 
HETATM 11655 O  O   . HOH EA 6 .   ? 48.581  117.097 -9.225  1.00 49.33 ? 428 HOH C O   1 
HETATM 11656 O  O   . HOH EA 6 .   ? 67.118  82.323  -23.861 1.00 39.58 ? 429 HOH C O   1 
HETATM 11657 O  O   . HOH EA 6 .   ? 43.427  107.237 -26.491 1.00 42.09 ? 430 HOH C O   1 
HETATM 11658 O  O   . HOH EA 6 .   ? 42.513  96.186  -23.042 1.00 54.01 ? 431 HOH C O   1 
HETATM 11659 O  O   . HOH EA 6 .   ? 46.083  109.761 -1.442  1.00 45.04 ? 432 HOH C O   1 
HETATM 11660 O  O   . HOH EA 6 .   ? 65.896  96.212  -21.236 1.00 30.97 ? 433 HOH C O   1 
HETATM 11661 O  O   . HOH EA 6 .   ? 41.805  103.952 -6.835  1.00 41.40 ? 434 HOH C O   1 
HETATM 11662 O  O   . HOH EA 6 .   ? 48.099  109.160 -28.071 1.00 43.10 ? 435 HOH C O   1 
HETATM 11663 O  O   . HOH EA 6 .   ? 54.212  88.749  -33.546 1.00 42.97 ? 436 HOH C O   1 
HETATM 11664 O  O   . HOH EA 6 .   ? 58.327  108.911 -24.273 1.00 38.44 ? 437 HOH C O   1 
HETATM 11665 O  O   . HOH EA 6 .   ? 47.474  94.509  -13.233 1.00 54.20 ? 438 HOH C O   1 
HETATM 11666 O  O   . HOH EA 6 .   ? 46.173  118.607 -8.467  1.00 54.80 ? 439 HOH C O   1 
HETATM 11667 O  O   . HOH EA 6 .   ? 54.764  84.006  -30.601 1.00 59.50 ? 440 HOH C O   1 
HETATM 11668 O  O   . HOH EA 6 .   ? 43.833  105.832 -28.903 1.00 43.04 ? 441 HOH C O   1 
HETATM 11669 O  O   . HOH EA 6 .   ? 53.269  114.790 -4.934  1.00 52.62 ? 442 HOH C O   1 
HETATM 11670 O  O   . HOH EA 6 .   ? 59.464  106.763 -22.877 1.00 51.63 ? 443 HOH C O   1 
HETATM 11671 O  O   . HOH EA 6 .   ? 63.702  82.743  -26.079 1.00 27.75 ? 444 HOH C O   1 
HETATM 11672 O  O   . HOH EA 6 .   ? 64.621  99.377  -9.068  1.00 42.62 ? 445 HOH C O   1 
HETATM 11673 O  O   . HOH EA 6 .   ? 54.632  99.288  -34.724 1.00 41.42 ? 446 HOH C O   1 
HETATM 11674 O  O   . HOH EA 6 .   ? 69.097  102.329 -24.863 1.00 40.37 ? 447 HOH C O   1 
HETATM 11675 O  O   . HOH EA 6 .   ? 68.030  96.421  -19.619 1.00 49.39 ? 448 HOH C O   1 
HETATM 11676 O  O   . HOH EA 6 .   ? 59.452  111.622 -23.455 1.00 46.04 ? 449 HOH C O   1 
HETATM 11677 O  O   . HOH EA 6 .   ? 41.747  87.472  -30.213 1.00 50.02 ? 450 HOH C O   1 
HETATM 11678 O  O   . HOH EA 6 .   ? 52.639  85.121  -28.380 1.00 40.60 ? 451 HOH C O   1 
HETATM 11679 O  O   . HOH EA 6 .   ? 55.615  82.893  -4.832  1.00 45.04 ? 452 HOH C O   1 
HETATM 11680 O  O   . HOH EA 6 .   ? 55.266  94.087  -3.021  1.00 46.23 ? 453 HOH C O   1 
HETATM 11681 O  O   . HOH EA 6 .   ? 63.975  101.324 -7.265  1.00 39.10 ? 454 HOH C O   1 
HETATM 11682 O  O   A HOH EA 6 .   ? 51.436  83.871  -24.319 0.50 28.67 ? 455 HOH C O   1 
HETATM 11683 O  O   B HOH EA 6 .   ? 49.226  83.869  -23.572 0.50 24.67 ? 455 HOH C O   1 
HETATM 11684 O  O   . HOH EA 6 .   ? 64.504  90.574  -15.426 1.00 50.94 ? 456 HOH C O   1 
HETATM 11685 O  O   . HOH EA 6 .   ? 46.739  85.056  -20.022 1.00 37.96 ? 457 HOH C O   1 
HETATM 11686 O  O   . HOH EA 6 .   ? 52.832  100.222 -2.290  1.00 44.65 ? 458 HOH C O   1 
HETATM 11687 O  O   . HOH EA 6 .   ? 45.154  91.086  -11.107 1.00 37.19 ? 459 HOH C O   1 
HETATM 11688 O  O   . HOH EA 6 .   ? 41.222  102.918 -2.416  1.00 48.76 ? 460 HOH C O   1 
HETATM 11689 O  O   . HOH EA 6 .   ? 55.260  78.031  -13.828 1.00 34.25 ? 461 HOH C O   1 
HETATM 11690 O  O   . HOH EA 6 .   ? 50.086  78.948  -19.646 1.00 43.34 ? 462 HOH C O   1 
HETATM 11691 O  O   . HOH EA 6 .   ? 57.223  77.150  -15.459 1.00 25.38 ? 463 HOH C O   1 
HETATM 11692 O  O   . HOH EA 6 .   ? 52.860  77.214  -15.233 1.00 28.56 ? 464 HOH C O   1 
HETATM 11693 O  O   . HOH EA 6 .   ? 57.195  99.133  -33.811 1.00 44.10 ? 465 HOH C O   1 
HETATM 11694 O  O   . HOH EA 6 .   ? 55.402  82.889  -26.106 1.00 28.14 ? 466 HOH C O   1 
HETATM 11695 O  O   . HOH EA 6 .   ? 65.421  91.597  -20.206 1.00 47.73 ? 467 HOH C O   1 
HETATM 11696 O  O   . HOH EA 6 .   ? 44.032  85.392  -27.022 1.00 46.12 ? 468 HOH C O   1 
HETATM 11697 O  O   . HOH EA 6 .   ? 55.857  92.705  -4.960  1.00 35.93 ? 469 HOH C O   1 
HETATM 11698 O  O   . HOH EA 6 .   ? 63.109  86.828  -28.011 1.00 47.62 ? 470 HOH C O   1 
HETATM 11699 O  O   . HOH EA 6 .   ? 54.621  111.058 -2.604  1.00 51.62 ? 471 HOH C O   1 
HETATM 11700 O  O   . HOH EA 6 .   ? 64.381  104.615 -3.852  1.00 53.35 ? 472 HOH C O   1 
HETATM 11701 O  O   . HOH EA 6 .   ? 58.697  90.499  -37.295 1.00 59.41 ? 473 HOH C O   1 
HETATM 11702 O  O   . HOH EA 6 .   ? 52.608  81.318  -24.267 1.00 36.38 ? 474 HOH C O   1 
HETATM 11703 O  O   . HOH EA 6 .   ? 48.215  85.221  -27.685 1.00 49.75 ? 475 HOH C O   1 
HETATM 11704 O  O   . HOH EA 6 .   ? 42.359  111.496 -22.496 1.00 48.62 ? 476 HOH C O   1 
HETATM 11705 O  O   . HOH EA 6 .   ? 67.724  88.825  -15.478 1.00 51.53 ? 477 HOH C O   1 
HETATM 11706 O  O   . HOH EA 6 .   ? 48.938  83.645  -25.888 1.00 50.23 ? 478 HOH C O   1 
HETATM 11707 O  O   . HOH EA 6 .   ? 67.566  93.194  -16.254 1.00 49.91 ? 479 HOH C O   1 
HETATM 11708 O  O   . HOH EA 6 .   ? 57.572  87.710  -38.215 1.00 55.69 ? 480 HOH C O   1 
HETATM 11709 O  O   . HOH EA 6 .   ? 69.129  90.935  -12.927 1.00 54.49 ? 481 HOH C O   1 
HETATM 11710 O  O   . HOH EA 6 .   ? 46.600  80.597  -22.194 1.00 47.67 ? 482 HOH C O   1 
HETATM 11711 O  O   . HOH FA 6 .   ? 57.793  131.236 -6.521  1.00 53.15 ? 301 HOH D O   1 
HETATM 11712 O  O   . HOH FA 6 .   ? 65.561  136.707 -10.894 1.00 46.91 ? 302 HOH D O   1 
HETATM 11713 O  O   . HOH FA 6 .   ? 75.835  114.491 -21.084 1.00 53.39 ? 303 HOH D O   1 
HETATM 11714 O  O   . HOH FA 6 .   ? 55.430  119.503 -3.656  1.00 54.92 ? 304 HOH D O   1 
HETATM 11715 O  O   . HOH FA 6 .   ? 69.000  129.415 -16.104 1.00 36.54 ? 305 HOH D O   1 
HETATM 11716 O  O   . HOH FA 6 .   ? 64.388  119.862 -35.416 1.00 25.45 ? 306 HOH D O   1 
HETATM 11717 O  O   . HOH FA 6 .   ? 59.587  118.977 -32.184 1.00 21.02 ? 307 HOH D O   1 
HETATM 11718 O  O   . HOH FA 6 .   ? 50.216  125.659 -24.566 1.00 47.34 ? 308 HOH D O   1 
HETATM 11719 O  O   . HOH FA 6 .   ? 44.750  114.023 -18.417 1.00 38.78 ? 309 HOH D O   1 
HETATM 11720 O  O   . HOH FA 6 .   ? 58.710  114.056 -25.186 1.00 32.00 ? 310 HOH D O   1 
HETATM 11721 O  O   . HOH FA 6 .   ? 70.510  112.534 -4.645  1.00 40.00 ? 311 HOH D O   1 
HETATM 11722 O  O   . HOH FA 6 .   ? 51.977  133.407 -6.903  1.00 51.05 ? 312 HOH D O   1 
HETATM 11723 O  O   . HOH FA 6 .   ? 61.501  127.406 -33.404 1.00 35.73 ? 313 HOH D O   1 
HETATM 11724 O  O   . HOH FA 6 .   ? 73.647  128.223 -25.496 1.00 41.00 ? 314 HOH D O   1 
HETATM 11725 O  O   . HOH FA 6 .   ? 65.866  130.991 -4.884  1.00 45.42 ? 315 HOH D O   1 
HETATM 11726 O  O   . HOH FA 6 .   ? 65.799  116.174 -1.972  1.00 33.35 ? 316 HOH D O   1 
HETATM 11727 O  O   . HOH FA 6 .   ? 63.986  135.099 -28.170 1.00 44.73 ? 317 HOH D O   1 
HETATM 11728 O  O   . HOH FA 6 .   ? 63.856  110.132 -5.926  1.00 49.28 ? 318 HOH D O   1 
HETATM 11729 O  O   . HOH FA 6 .   ? 55.025  122.971 -30.575 1.00 35.18 ? 319 HOH D O   1 
HETATM 11730 O  O   . HOH FA 6 .   ? 57.075  117.267 -6.212  1.00 38.83 ? 320 HOH D O   1 
HETATM 11731 O  O   . HOH FA 6 .   ? 46.543  119.464 -16.961 1.00 34.62 ? 321 HOH D O   1 
HETATM 11732 O  O   . HOH FA 6 .   ? 56.301  130.945 -19.026 1.00 34.91 ? 322 HOH D O   1 
HETATM 11733 O  O   . HOH FA 6 .   ? 72.971  125.686 -7.602  1.00 47.78 ? 323 HOH D O   1 
HETATM 11734 O  O   . HOH FA 6 .   ? 43.751  116.757 -22.052 1.00 48.97 ? 324 HOH D O   1 
HETATM 11735 O  O   . HOH FA 6 .   ? 67.590  113.394 -4.900  1.00 35.27 ? 325 HOH D O   1 
HETATM 11736 O  O   . HOH FA 6 .   ? 53.242  133.550 -9.704  1.00 45.30 ? 326 HOH D O   1 
HETATM 11737 O  O   . HOH FA 6 .   ? 67.038  132.571 -35.523 1.00 36.16 ? 327 HOH D O   1 
HETATM 11738 O  O   . HOH FA 6 .   ? 58.694  141.693 -20.444 1.00 48.61 ? 328 HOH D O   1 
HETATM 11739 O  O   . HOH FA 6 .   ? 48.070  125.571 -20.021 1.00 37.36 ? 329 HOH D O   1 
HETATM 11740 O  O   . HOH FA 6 .   ? 68.639  121.120 -4.893  1.00 34.81 ? 330 HOH D O   1 
HETATM 11741 O  O   . HOH FA 6 .   ? 70.086  127.959 -11.264 1.00 40.85 ? 331 HOH D O   1 
HETATM 11742 O  O   . HOH FA 6 .   ? 68.496  105.839 -18.425 1.00 28.40 ? 332 HOH D O   1 
HETATM 11743 O  O   . HOH FA 6 .   ? 63.786  130.613 -3.889  1.00 48.28 ? 333 HOH D O   1 
HETATM 11744 O  O   . HOH FA 6 .   ? 68.063  134.506 -12.072 1.00 37.27 ? 334 HOH D O   1 
HETATM 11745 O  O   . HOH FA 6 .   ? 59.001  138.247 -23.361 1.00 47.17 ? 335 HOH D O   1 
HETATM 11746 O  O   . HOH FA 6 .   ? 62.762  131.520 -14.671 1.00 33.11 ? 336 HOH D O   1 
HETATM 11747 O  O   . HOH FA 6 .   ? 57.053  115.412 -8.868  1.00 48.21 ? 337 HOH D O   1 
HETATM 11748 O  O   . HOH FA 6 .   ? 56.382  115.781 -25.569 1.00 34.03 ? 338 HOH D O   1 
HETATM 11749 O  O   . HOH FA 6 .   ? 60.878  111.747 -2.722  1.00 44.89 ? 339 HOH D O   1 
HETATM 11750 O  O   . HOH FA 6 .   ? 64.247  134.496 -30.294 1.00 40.95 ? 340 HOH D O   1 
HETATM 11751 O  O   . HOH FA 6 .   ? 69.854  106.771 -7.812  1.00 51.81 ? 341 HOH D O   1 
HETATM 11752 O  O   . HOH FA 6 .   ? 51.690  112.682 -20.235 1.00 20.14 ? 342 HOH D O   1 
HETATM 11753 O  O   . HOH FA 6 .   ? 75.740  121.846 -22.315 1.00 44.33 ? 343 HOH D O   1 
HETATM 11754 O  O   . HOH FA 6 .   ? 52.116  127.133 -1.099  1.00 53.26 ? 344 HOH D O   1 
HETATM 11755 O  O   . HOH FA 6 .   ? 74.430  127.414 -27.885 1.00 39.33 ? 345 HOH D O   1 
HETATM 11756 O  O   . HOH FA 6 .   ? 73.731  117.159 -5.361  1.00 28.87 ? 346 HOH D O   1 
HETATM 11757 O  O   . HOH FA 6 .   ? 70.362  128.995 -18.468 1.00 40.69 ? 347 HOH D O   1 
HETATM 11758 O  O   . HOH FA 6 .   ? 75.549  127.369 -21.873 1.00 40.39 ? 348 HOH D O   1 
HETATM 11759 O  O   . HOH FA 6 .   ? 70.673  111.405 -22.102 1.00 36.77 ? 349 HOH D O   1 
HETATM 11760 O  O   . HOH FA 6 .   ? 68.358  138.993 0.486   1.00 35.83 ? 350 HOH D O   1 
HETATM 11761 O  O   . HOH FA 6 .   ? 52.557  123.980 -8.663  1.00 43.40 ? 351 HOH D O   1 
HETATM 11762 O  O   . HOH FA 6 .   ? 51.558  127.302 -26.199 1.00 32.94 ? 352 HOH D O   1 
HETATM 11763 O  O   . HOH FA 6 .   ? 76.318  128.990 -34.466 1.00 59.96 ? 353 HOH D O   1 
HETATM 11764 O  O   . HOH FA 6 .   ? 44.389  116.966 -19.076 1.00 49.97 ? 354 HOH D O   1 
HETATM 11765 O  O   A HOH FA 6 .   ? 52.057  129.145 -21.855 0.50 26.79 ? 355 HOH D O   1 
HETATM 11766 O  O   B HOH FA 6 .   ? 50.289  129.729 -20.948 0.50 35.71 ? 355 HOH D O   1 
HETATM 11767 O  O   . HOH FA 6 .   ? 70.248  111.883 -17.758 1.00 33.46 ? 356 HOH D O   1 
HETATM 11768 O  O   . HOH FA 6 .   ? 59.549  128.579 -4.619  1.00 39.41 ? 357 HOH D O   1 
HETATM 11769 O  O   . HOH FA 6 .   ? 62.498  118.622 -2.339  1.00 43.93 ? 358 HOH D O   1 
HETATM 11770 O  O   . HOH FA 6 .   ? 60.998  112.673 -21.678 1.00 16.45 ? 359 HOH D O   1 
HETATM 11771 O  O   . HOH FA 6 .   ? 53.015  118.023 -21.380 1.00 39.17 ? 360 HOH D O   1 
HETATM 11772 O  O   . HOH FA 6 .   ? 68.643  124.390 -34.967 1.00 30.91 ? 361 HOH D O   1 
HETATM 11773 O  O   . HOH FA 6 .   ? 60.327  131.529 -30.824 1.00 31.93 ? 362 HOH D O   1 
HETATM 11774 O  O   . HOH FA 6 .   ? 61.761  128.322 -3.321  1.00 55.13 ? 363 HOH D O   1 
HETATM 11775 O  O   . HOH FA 6 .   ? 75.820  125.849 -29.682 1.00 41.37 ? 364 HOH D O   1 
HETATM 11776 O  O   . HOH FA 6 .   ? 57.706  112.968 -22.497 1.00 25.04 ? 365 HOH D O   1 
HETATM 11777 O  O   . HOH FA 6 .   ? 52.908  137.999 -22.522 1.00 52.81 ? 366 HOH D O   1 
HETATM 11778 O  O   . HOH FA 6 .   ? 75.624  116.049 -9.670  1.00 59.04 ? 367 HOH D O   1 
HETATM 11779 O  O   . HOH FA 6 .   ? 70.607  125.601 -38.168 1.00 42.90 ? 368 HOH D O   1 
HETATM 11780 O  O   . HOH FA 6 .   ? 72.391  114.423 -23.618 1.00 38.22 ? 369 HOH D O   1 
HETATM 11781 O  O   . HOH FA 6 .   ? 53.498  134.391 -21.251 1.00 52.01 ? 370 HOH D O   1 
HETATM 11782 O  O   . HOH FA 6 .   ? 50.827  118.727 -8.567  1.00 39.92 ? 371 HOH D O   1 
HETATM 11783 O  O   . HOH FA 6 .   ? 57.223  127.302 -5.533  1.00 31.21 ? 372 HOH D O   1 
HETATM 11784 O  O   . HOH FA 6 .   ? 54.118  131.577 -20.819 1.00 35.78 ? 373 HOH D O   1 
HETATM 11785 O  O   . HOH FA 6 .   ? 54.354  123.159 -36.930 1.00 32.07 ? 374 HOH D O   1 
HETATM 11786 O  O   . HOH FA 6 .   ? 52.916  129.980 -14.204 1.00 32.63 ? 375 HOH D O   1 
HETATM 11787 O  O   . HOH FA 6 .   ? 63.850  126.742 -36.419 1.00 24.35 ? 376 HOH D O   1 
HETATM 11788 O  O   . HOH FA 6 .   ? 61.561  137.707 -26.148 1.00 49.16 ? 377 HOH D O   1 
HETATM 11789 O  O   . HOH FA 6 .   ? 60.768  118.318 0.834   1.00 39.53 ? 378 HOH D O   1 
HETATM 11790 O  O   . HOH FA 6 .   ? 58.410  122.959 -31.975 1.00 26.32 ? 379 HOH D O   1 
HETATM 11791 O  O   . HOH FA 6 .   ? 69.689  127.844 -7.676  1.00 39.35 ? 380 HOH D O   1 
HETATM 11792 O  O   . HOH FA 6 .   ? 71.387  106.609 -18.231 1.00 46.87 ? 381 HOH D O   1 
HETATM 11793 O  O   . HOH FA 6 .   ? 61.901  129.264 -31.488 1.00 30.43 ? 382 HOH D O   1 
HETATM 11794 O  O   . HOH FA 6 .   ? 51.639  121.967 -27.563 1.00 56.50 ? 383 HOH D O   1 
HETATM 11795 O  O   . HOH FA 6 .   ? 71.618  116.519 -24.857 1.00 38.20 ? 384 HOH D O   1 
HETATM 11796 O  O   . HOH FA 6 .   ? 68.595  132.121 -16.677 1.00 36.77 ? 385 HOH D O   1 
HETATM 11797 O  O   . HOH FA 6 .   ? 75.863  121.637 -15.868 1.00 40.71 ? 386 HOH D O   1 
HETATM 11798 O  O   . HOH FA 6 .   ? 63.824  137.872 -5.078  1.00 49.85 ? 387 HOH D O   1 
HETATM 11799 O  O   . HOH FA 6 .   ? 79.511  123.821 -18.751 1.00 44.97 ? 388 HOH D O   1 
HETATM 11800 O  O   . HOH FA 6 .   ? 71.682  128.148 -22.673 1.00 34.19 ? 389 HOH D O   1 
HETATM 11801 O  O   . HOH FA 6 .   ? 68.202  107.900 -10.870 1.00 32.79 ? 390 HOH D O   1 
HETATM 11802 O  O   . HOH FA 6 .   ? 49.289  133.030 -16.400 1.00 55.06 ? 391 HOH D O   1 
HETATM 11803 O  O   . HOH FA 6 .   ? 73.489  127.931 -13.367 1.00 43.58 ? 392 HOH D O   1 
HETATM 11804 O  O   . HOH FA 6 .   ? 66.412  137.321 -27.196 1.00 38.17 ? 393 HOH D O   1 
HETATM 11805 O  O   . HOH FA 6 .   ? 46.166  121.838 -27.042 1.00 50.28 ? 394 HOH D O   1 
HETATM 11806 O  O   . HOH FA 6 .   ? 63.194  115.028 -29.445 1.00 42.64 ? 395 HOH D O   1 
HETATM 11807 O  O   . HOH FA 6 .   ? 75.900  132.405 -32.335 1.00 47.22 ? 396 HOH D O   1 
HETATM 11808 O  O   . HOH FA 6 .   ? 69.118  98.269  -17.052 1.00 48.62 ? 397 HOH D O   1 
HETATM 11809 O  O   . HOH FA 6 .   ? 51.312  132.027 -25.269 1.00 54.01 ? 398 HOH D O   1 
HETATM 11810 O  O   . HOH FA 6 .   ? 72.098  127.321 -20.011 1.00 36.89 ? 399 HOH D O   1 
HETATM 11811 O  O   . HOH FA 6 .   ? 67.426  104.828 -11.542 1.00 47.47 ? 400 HOH D O   1 
HETATM 11812 O  O   . HOH FA 6 .   ? 53.838  127.022 -29.984 1.00 41.68 ? 401 HOH D O   1 
HETATM 11813 O  O   . HOH FA 6 .   ? 68.508  135.230 -18.497 1.00 37.65 ? 402 HOH D O   1 
HETATM 11814 O  O   . HOH FA 6 .   ? 48.657  126.761 -17.611 1.00 40.33 ? 403 HOH D O   1 
HETATM 11815 O  O   . HOH FA 6 .   ? 54.752  116.479 -21.794 1.00 43.59 ? 404 HOH D O   1 
HETATM 11816 O  O   . HOH FA 6 .   ? 64.903  139.031 -11.552 1.00 54.07 ? 405 HOH D O   1 
HETATM 11817 O  O   . HOH FA 6 .   ? 76.236  128.559 -18.262 1.00 49.95 ? 406 HOH D O   1 
HETATM 11818 O  O   . HOH FA 6 .   ? 55.596  114.675 -23.364 1.00 42.25 ? 407 HOH D O   1 
HETATM 11819 O  O   . HOH FA 6 .   ? 76.604  110.829 1.155   1.00 61.16 ? 408 HOH D O   1 
HETATM 11820 O  O   . HOH FA 6 .   ? 50.241  129.242 -17.475 1.00 40.73 ? 409 HOH D O   1 
HETATM 11821 O  O   . HOH FA 6 .   ? 67.784  137.640 -30.748 1.00 53.56 ? 410 HOH D O   1 
HETATM 11822 O  O   . HOH FA 6 .   ? 63.753  116.375 -37.639 1.00 33.77 ? 411 HOH D O   1 
HETATM 11823 O  O   . HOH FA 6 .   ? 69.816  133.409 -18.564 1.00 39.80 ? 412 HOH D O   1 
HETATM 11824 O  O   . HOH FA 6 .   ? 53.422  129.514 -19.365 1.00 43.73 ? 413 HOH D O   1 
HETATM 11825 O  O   . HOH FA 6 .   ? 69.838  103.221 -11.580 1.00 48.77 ? 414 HOH D O   1 
HETATM 11826 O  O   . HOH FA 6 .   ? 46.324  134.126 -14.781 1.00 63.82 ? 415 HOH D O   1 
HETATM 11827 O  O   . HOH FA 6 .   ? 65.447  115.076 -29.244 1.00 53.69 ? 416 HOH D O   1 
HETATM 11828 O  O   . HOH FA 6 .   ? 52.545  129.240 -16.769 1.00 40.62 ? 417 HOH D O   1 
HETATM 11829 O  O   . HOH FA 6 .   ? 52.064  122.290 -6.571  1.00 51.44 ? 418 HOH D O   1 
HETATM 11830 O  O   . HOH FA 6 .   ? 63.168  140.887 -9.868  1.00 64.83 ? 419 HOH D O   1 
HETATM 11831 O  O   . HOH FA 6 .   ? 67.249  119.674 -35.631 1.00 44.26 ? 420 HOH D O   1 
HETATM 11832 O  O   . HOH FA 6 .   ? 69.832  100.148 -13.084 1.00 53.69 ? 421 HOH D O   1 
HETATM 11833 O  O   . HOH FA 6 .   ? 71.224  110.526 -3.015  1.00 44.86 ? 422 HOH D O   1 
HETATM 11834 O  O   . HOH FA 6 .   ? 54.408  112.140 -23.255 1.00 38.85 ? 423 HOH D O   1 
HETATM 11835 O  O   . HOH FA 6 .   ? 44.796  121.233 -21.763 1.00 47.64 ? 424 HOH D O   1 
HETATM 11836 O  O   . HOH FA 6 .   ? 71.491  119.612 -31.583 1.00 50.01 ? 425 HOH D O   1 
HETATM 11837 O  O   . HOH FA 6 .   ? 74.548  128.638 -20.105 1.00 50.79 ? 426 HOH D O   1 
HETATM 11838 O  O   . HOH FA 6 .   ? 68.329  107.267 0.585   1.00 55.88 ? 427 HOH D O   1 
HETATM 11839 O  O   . HOH FA 6 .   ? 53.233  119.963 -5.075  1.00 46.40 ? 428 HOH D O   1 
HETATM 11840 O  O   . HOH FA 6 .   ? 67.610  116.304 -29.858 1.00 50.24 ? 429 HOH D O   1 
HETATM 11841 O  O   . HOH FA 6 .   ? 68.777  100.750 -19.518 1.00 49.30 ? 430 HOH D O   1 
HETATM 11842 O  O   . HOH FA 6 .   ? 70.543  116.366 -27.601 1.00 50.53 ? 431 HOH D O   1 
HETATM 11843 O  O   . HOH FA 6 .   ? 70.560  129.120 -13.629 1.00 35.37 ? 432 HOH D O   1 
HETATM 11844 O  O   . HOH FA 6 .   ? 46.663  126.266 -15.687 1.00 52.59 ? 433 HOH D O   1 
HETATM 11845 O  O   . HOH FA 6 .   ? 73.941  111.309 -19.249 1.00 52.07 ? 434 HOH D O   1 
HETATM 11846 O  O   . HOH FA 6 .   ? 79.440  126.560 -34.625 1.00 58.55 ? 435 HOH D O   1 
HETATM 11847 O  O   . HOH FA 6 .   ? 75.538  129.532 -23.888 1.00 46.90 ? 436 HOH D O   1 
HETATM 11848 O  O   . HOH FA 6 .   ? 53.745  124.979 -31.981 1.00 44.77 ? 437 HOH D O   1 
HETATM 11849 O  O   . HOH FA 6 .   ? 68.581  134.068 -14.818 1.00 52.87 ? 438 HOH D O   1 
HETATM 11850 O  O   . HOH FA 6 .   ? 57.734  125.737 -32.795 1.00 46.44 ? 439 HOH D O   1 
HETATM 11851 O  O   . HOH FA 6 .   ? 67.306  117.639 -37.892 1.00 42.53 ? 440 HOH D O   1 
HETATM 11852 O  O   . HOH FA 6 .   ? 69.372  121.957 -35.956 1.00 43.12 ? 441 HOH D O   1 
HETATM 11853 O  O   . HOH FA 6 .   ? 78.052  125.960 -21.623 1.00 44.91 ? 442 HOH D O   1 
HETATM 11854 O  O   . HOH FA 6 .   ? 47.716  111.743 -28.233 1.00 49.42 ? 443 HOH D O   1 
HETATM 11855 O  O   . HOH FA 6 .   ? 71.629  121.074 -34.837 1.00 48.44 ? 444 HOH D O   1 
HETATM 11856 O  O   . HOH FA 6 .   ? 74.500  133.719 -41.557 1.00 54.44 ? 445 HOH D O   1 
HETATM 11857 O  O   . HOH GA 6 .   ? 51.444  77.937  13.955  1.00 35.33 ? 301 HOH E O   1 
HETATM 11858 O  O   . HOH GA 6 .   ? 57.918  71.652  3.873   1.00 46.23 ? 302 HOH E O   1 
HETATM 11859 O  O   . HOH GA 6 .   ? 55.390  51.621  25.006  1.00 33.84 ? 303 HOH E O   1 
HETATM 11860 O  O   . HOH GA 6 .   ? 48.446  68.556  3.598   1.00 55.97 ? 304 HOH E O   1 
HETATM 11861 O  O   . HOH GA 6 .   ? 59.518  75.007  27.835  1.00 48.71 ? 305 HOH E O   1 
HETATM 11862 O  O   . HOH GA 6 .   ? 66.068  68.314  4.928   1.00 54.31 ? 306 HOH E O   1 
HETATM 11863 O  O   . HOH GA 6 .   ? 52.094  58.011  1.768   1.00 37.00 ? 307 HOH E O   1 
HETATM 11864 O  O   . HOH GA 6 .   ? 50.935  52.133  28.867  1.00 39.65 ? 308 HOH E O   1 
HETATM 11865 O  O   . HOH GA 6 .   ? 62.585  52.043  28.276  1.00 52.14 ? 309 HOH E O   1 
HETATM 11866 O  O   . HOH GA 6 .   ? 37.207  61.737  31.123  1.00 40.91 ? 310 HOH E O   1 
HETATM 11867 O  O   . HOH GA 6 .   ? 66.671  76.221  22.120  1.00 51.83 ? 311 HOH E O   1 
HETATM 11868 O  O   . HOH GA 6 .   ? 62.006  59.930  5.636   1.00 39.15 ? 312 HOH E O   1 
HETATM 11869 O  O   . HOH GA 6 .   ? 53.450  55.689  32.359  1.00 24.70 ? 313 HOH E O   1 
HETATM 11870 O  O   . HOH GA 6 .   ? 50.088  54.453  3.427   1.00 39.63 ? 314 HOH E O   1 
HETATM 11871 O  O   . HOH GA 6 .   ? 60.811  76.184  4.309   1.00 41.08 ? 315 HOH E O   1 
HETATM 11872 O  O   . HOH GA 6 .   ? 42.803  59.153  -1.253  1.00 48.24 ? 316 HOH E O   1 
HETATM 11873 O  O   . HOH GA 6 .   ? 40.562  67.345  16.336  1.00 32.72 ? 317 HOH E O   1 
HETATM 11874 O  O   . HOH GA 6 .   ? 48.975  72.620  29.702  1.00 47.42 ? 318 HOH E O   1 
HETATM 11875 O  O   . HOH GA 6 .   ? 65.351  71.966  21.824  1.00 40.49 ? 319 HOH E O   1 
HETATM 11876 O  O   . HOH GA 6 .   ? 52.904  63.492  3.474   1.00 48.97 ? 320 HOH E O   1 
HETATM 11877 O  O   . HOH GA 6 .   ? 68.547  58.555  19.708  1.00 37.26 ? 321 HOH E O   1 
HETATM 11878 O  O   . HOH GA 6 .   ? 67.351  79.419  23.554  1.00 39.68 ? 322 HOH E O   1 
HETATM 11879 O  O   . HOH GA 6 .   ? 46.310  68.687  17.442  1.00 20.10 ? 323 HOH E O   1 
HETATM 11880 O  O   . HOH GA 6 .   ? 53.964  76.250  26.231  1.00 31.81 ? 324 HOH E O   1 
HETATM 11881 O  O   . HOH GA 6 .   ? 66.347  64.030  23.256  1.00 39.50 ? 325 HOH E O   1 
HETATM 11882 O  O   . HOH GA 6 .   ? 38.379  57.784  27.562  1.00 45.67 ? 326 HOH E O   1 
HETATM 11883 O  O   . HOH GA 6 .   ? 35.187  61.893  25.602  1.00 50.58 ? 327 HOH E O   1 
HETATM 11884 O  O   . HOH GA 6 .   ? 46.249  67.614  11.336  1.00 28.07 ? 328 HOH E O   1 
HETATM 11885 O  O   . HOH GA 6 .   ? 44.309  49.516  19.685  1.00 31.21 ? 329 HOH E O   1 
HETATM 11886 O  O   . HOH GA 6 .   ? 60.374  71.041  31.359  1.00 57.00 ? 330 HOH E O   1 
HETATM 11887 O  O   . HOH GA 6 .   ? 57.597  53.612  26.207  1.00 40.28 ? 331 HOH E O   1 
HETATM 11888 O  O   . HOH GA 6 .   ? 64.065  63.999  27.086  1.00 53.18 ? 332 HOH E O   1 
HETATM 11889 O  O   . HOH GA 6 .   ? 64.244  59.887  29.218  1.00 44.27 ? 333 HOH E O   1 
HETATM 11890 O  O   . HOH GA 6 .   ? 50.909  63.752  34.551  1.00 28.00 ? 334 HOH E O   1 
HETATM 11891 O  O   . HOH GA 6 .   ? 57.895  60.145  32.130  1.00 40.85 ? 335 HOH E O   1 
HETATM 11892 O  O   . HOH GA 6 .   ? 39.266  59.469  20.856  1.00 32.10 ? 336 HOH E O   1 
HETATM 11893 O  O   . HOH GA 6 .   ? 44.720  45.392  15.118  1.00 49.72 ? 337 HOH E O   1 
HETATM 11894 O  O   . HOH GA 6 .   ? 70.498  53.058  20.192  1.00 44.65 ? 338 HOH E O   1 
HETATM 11895 O  O   . HOH GA 6 .   ? 45.457  78.559  12.640  1.00 50.76 ? 339 HOH E O   1 
HETATM 11896 O  O   . HOH GA 6 .   ? 45.992  72.118  34.730  1.00 49.56 ? 340 HOH E O   1 
HETATM 11897 O  O   . HOH GA 6 .   ? 52.877  70.877  16.397  1.00 17.79 ? 341 HOH E O   1 
HETATM 11898 O  O   . HOH GA 6 .   ? 59.900  57.450  7.298   1.00 31.14 ? 342 HOH E O   1 
HETATM 11899 O  O   . HOH GA 6 .   ? 57.695  69.023  6.903   1.00 26.32 ? 343 HOH E O   1 
HETATM 11900 O  O   . HOH GA 6 .   ? 62.998  76.566  7.186   1.00 45.00 ? 344 HOH E O   1 
HETATM 11901 O  O   . HOH GA 6 .   ? 55.158  54.677  35.445  1.00 40.57 ? 345 HOH E O   1 
HETATM 11902 O  O   . HOH GA 6 .   ? 57.900  62.297  -0.181  1.00 53.15 ? 346 HOH E O   1 
HETATM 11903 O  O   . HOH GA 6 .   ? 38.042  63.901  27.108  1.00 43.81 ? 347 HOH E O   1 
HETATM 11904 O  O   . HOH GA 6 .   ? 45.010  63.886  2.283   1.00 60.90 ? 348 HOH E O   1 
HETATM 11905 O  O   . HOH GA 6 .   ? 56.184  77.311  11.490  1.00 27.84 ? 349 HOH E O   1 
HETATM 11906 O  O   . HOH GA 6 .   ? 55.624  80.214  23.981  1.00 20.59 ? 350 HOH E O   1 
HETATM 11907 O  O   . HOH GA 6 .   ? 35.456  64.721  29.199  1.00 47.99 ? 351 HOH E O   1 
HETATM 11908 O  O   . HOH GA 6 .   ? 47.096  67.786  7.506   1.00 36.90 ? 352 HOH E O   1 
HETATM 11909 O  O   . HOH GA 6 .   ? 44.506  65.556  36.024  1.00 38.43 ? 353 HOH E O   1 
HETATM 11910 O  O   . HOH GA 6 .   ? 57.410  75.640  4.114   1.00 54.45 ? 354 HOH E O   1 
HETATM 11911 O  O   . HOH GA 6 .   ? 53.934  50.872  21.121  1.00 17.37 ? 355 HOH E O   1 
HETATM 11912 O  O   . HOH GA 6 .   ? 39.948  65.088  25.659  1.00 28.09 ? 356 HOH E O   1 
HETATM 11913 O  O   . HOH GA 6 .   ? 63.317  51.337  21.147  1.00 24.19 ? 357 HOH E O   1 
HETATM 11914 O  O   . HOH GA 6 .   ? 62.425  69.107  17.586  1.00 23.48 ? 358 HOH E O   1 
HETATM 11915 O  O   . HOH GA 6 .   ? 37.638  62.985  21.242  1.00 24.64 ? 359 HOH E O   1 
HETATM 11916 O  O   . HOH GA 6 .   ? 55.975  76.660  27.690  1.00 47.69 ? 360 HOH E O   1 
HETATM 11917 O  O   . HOH GA 6 .   ? 58.276  82.019  16.663  1.00 18.96 ? 361 HOH E O   1 
HETATM 11918 O  O   . HOH GA 6 .   ? 63.897  63.850  11.313  1.00 26.64 ? 362 HOH E O   1 
HETATM 11919 O  O   . HOH GA 6 .   ? 52.384  83.883  19.796  1.00 28.20 ? 363 HOH E O   1 
HETATM 11920 O  O   . HOH GA 6 .   ? 50.461  78.834  8.118   1.00 45.17 ? 364 HOH E O   1 
HETATM 11921 O  O   . HOH GA 6 .   ? 59.943  69.638  24.143  1.00 33.51 ? 365 HOH E O   1 
HETATM 11922 O  O   . HOH GA 6 .   ? 59.843  67.770  7.929   1.00 22.39 ? 366 HOH E O   1 
HETATM 11923 O  O   . HOH GA 6 .   ? 46.942  53.218  -1.161  1.00 51.55 ? 367 HOH E O   1 
HETATM 11924 O  O   . HOH GA 6 .   ? 37.591  72.212  35.012  1.00 47.76 ? 368 HOH E O   1 
HETATM 11925 O  O   . HOH GA 6 .   ? 47.381  53.249  3.127   1.00 44.62 ? 369 HOH E O   1 
HETATM 11926 O  O   . HOH GA 6 .   ? 55.097  59.636  2.771   1.00 22.53 ? 370 HOH E O   1 
HETATM 11927 O  O   . HOH GA 6 .   ? 68.537  64.053  14.430  1.00 40.83 ? 371 HOH E O   1 
HETATM 11928 O  O   . HOH GA 6 .   ? 48.958  61.352  4.466   1.00 36.81 ? 372 HOH E O   1 
HETATM 11929 O  O   . HOH GA 6 .   ? 42.140  69.500  36.881  1.00 44.21 ? 373 HOH E O   1 
HETATM 11930 O  O   . HOH GA 6 .   ? 42.089  57.804  6.788   1.00 41.29 ? 374 HOH E O   1 
HETATM 11931 O  O   . HOH GA 6 .   ? 51.121  74.727  28.957  1.00 29.47 ? 375 HOH E O   1 
HETATM 11932 O  O   . HOH GA 6 .   ? 58.798  78.127  14.420  1.00 23.14 ? 376 HOH E O   1 
HETATM 11933 O  O   . HOH GA 6 .   ? 57.081  51.256  22.505  1.00 26.22 ? 377 HOH E O   1 
HETATM 11934 O  O   . HOH GA 6 .   ? 54.352  59.884  32.971  1.00 25.34 ? 378 HOH E O   1 
HETATM 11935 O  O   . HOH GA 6 .   ? 63.328  72.873  13.783  1.00 27.99 ? 379 HOH E O   1 
HETATM 11936 O  O   . HOH GA 6 .   ? 40.599  70.891  29.525  1.00 31.77 ? 380 HOH E O   1 
HETATM 11937 O  O   . HOH GA 6 .   ? 58.180  69.246  21.861  1.00 27.57 ? 381 HOH E O   1 
HETATM 11938 O  O   . HOH GA 6 .   ? 42.835  54.220  23.302  1.00 30.57 ? 382 HOH E O   1 
HETATM 11939 O  O   . HOH GA 6 .   ? 45.411  50.517  15.646  1.00 31.26 ? 383 HOH E O   1 
HETATM 11940 O  O   . HOH GA 6 .   ? 50.977  77.946  6.078   1.00 49.58 ? 384 HOH E O   1 
HETATM 11941 O  O   . HOH GA 6 .   ? 61.804  64.887  29.069  1.00 25.64 ? 385 HOH E O   1 
HETATM 11942 O  O   . HOH GA 6 .   ? 37.464  59.668  17.183  1.00 54.61 ? 386 HOH E O   1 
HETATM 11943 O  O   . HOH GA 6 .   ? 49.847  60.739  1.856   1.00 54.94 ? 387 HOH E O   1 
HETATM 11944 O  O   . HOH GA 6 .   ? 50.040  71.606  6.954   1.00 45.46 ? 388 HOH E O   1 
HETATM 11945 O  O   . HOH GA 6 .   ? 60.184  50.150  26.501  1.00 40.42 ? 389 HOH E O   1 
HETATM 11946 O  O   . HOH GA 6 .   ? 46.348  74.449  28.710  1.00 27.89 ? 390 HOH E O   1 
HETATM 11947 O  O   . HOH GA 6 .   ? 52.123  68.158  32.721  1.00 27.03 ? 391 HOH E O   1 
HETATM 11948 O  O   . HOH GA 6 .   ? 42.078  42.330  14.507  1.00 56.77 ? 392 HOH E O   1 
HETATM 11949 O  O   . HOH GA 6 .   ? 63.300  68.400  14.374  1.00 34.78 ? 393 HOH E O   1 
HETATM 11950 O  O   . HOH GA 6 .   ? 44.045  51.400  13.433  1.00 46.48 ? 394 HOH E O   1 
HETATM 11951 O  O   . HOH GA 6 .   ? 43.943  65.841  7.047   1.00 46.61 ? 395 HOH E O   1 
HETATM 11952 O  O   . HOH GA 6 .   ? 43.769  57.690  3.825   1.00 27.95 ? 396 HOH E O   1 
HETATM 11953 O  O   . HOH GA 6 .   ? 42.534  67.123  13.205  1.00 25.32 ? 397 HOH E O   1 
HETATM 11954 O  O   . HOH GA 6 .   ? 65.559  58.918  10.685  1.00 36.63 ? 398 HOH E O   1 
HETATM 11955 O  O   . HOH GA 6 .   ? 36.905  68.809  31.633  1.00 40.22 ? 399 HOH E O   1 
HETATM 11956 O  O   . HOH GA 6 .   ? 66.342  66.631  8.737   1.00 51.40 ? 400 HOH E O   1 
HETATM 11957 O  O   . HOH GA 6 .   ? 64.878  74.910  9.146   1.00 47.04 ? 401 HOH E O   1 
HETATM 11958 O  O   . HOH GA 6 .   ? 50.567  66.027  32.882  1.00 25.57 ? 402 HOH E O   1 
HETATM 11959 O  O   . HOH GA 6 .   ? 54.261  85.421  17.406  1.00 24.76 ? 403 HOH E O   1 
HETATM 11960 O  O   . HOH GA 6 .   ? 53.587  78.129  7.547   1.00 36.09 ? 404 HOH E O   1 
HETATM 11961 O  O   . HOH GA 6 .   ? 46.389  74.194  20.168  1.00 27.10 ? 405 HOH E O   1 
HETATM 11962 O  O   . HOH GA 6 .   ? 43.704  59.863  34.633  1.00 42.74 ? 406 HOH E O   1 
HETATM 11963 O  O   . HOH GA 6 .   ? 64.798  79.569  23.394  1.00 25.95 ? 407 HOH E O   1 
HETATM 11964 O  O   . HOH GA 6 .   ? 42.156  52.238  21.526  1.00 39.88 ? 408 HOH E O   1 
HETATM 11965 O  O   . HOH GA 6 .   ? 42.142  56.355  29.295  1.00 52.10 ? 409 HOH E O   1 
HETATM 11966 O  O   . HOH GA 6 .   ? 48.034  62.899  2.453   1.00 44.50 ? 410 HOH E O   1 
HETATM 11967 O  O   . HOH GA 6 .   ? 65.115  58.060  8.445   1.00 39.95 ? 411 HOH E O   1 
HETATM 11968 O  O   . HOH GA 6 .   ? 49.287  44.299  9.297   1.00 46.56 ? 412 HOH E O   1 
HETATM 11969 O  O   . HOH GA 6 .   ? 53.771  70.696  5.650   1.00 35.06 ? 413 HOH E O   1 
HETATM 11970 O  O   . HOH GA 6 .   ? 42.658  65.395  23.236  1.00 25.02 ? 414 HOH E O   1 
HETATM 11971 O  O   . HOH GA 6 .   ? 65.208  69.021  13.022  1.00 47.00 ? 415 HOH E O   1 
HETATM 11972 O  O   . HOH GA 6 .   ? 60.454  72.717  25.220  1.00 36.98 ? 416 HOH E O   1 
HETATM 11973 O  O   . HOH GA 6 .   ? 61.562  56.688  23.251  1.00 30.58 ? 417 HOH E O   1 
HETATM 11974 O  O   . HOH GA 6 .   ? 38.960  58.007  23.171  1.00 41.76 ? 418 HOH E O   1 
HETATM 11975 O  O   . HOH GA 6 .   ? 40.350  60.871  13.887  1.00 34.85 ? 419 HOH E O   1 
HETATM 11976 O  O   . HOH GA 6 .   ? 65.371  76.368  25.944  1.00 41.00 ? 420 HOH E O   1 
HETATM 11977 O  O   . HOH GA 6 .   ? 48.489  47.636  8.713   1.00 32.58 ? 421 HOH E O   1 
HETATM 11978 O  O   . HOH GA 6 .   ? 58.825  64.281  32.302  1.00 56.42 ? 422 HOH E O   1 
HETATM 11979 O  O   . HOH GA 6 .   ? 56.310  52.587  32.516  1.00 55.18 ? 423 HOH E O   1 
HETATM 11980 O  O   . HOH GA 6 .   ? 60.477  55.133  22.314  1.00 38.46 ? 424 HOH E O   1 
HETATM 11981 O  O   . HOH GA 6 .   ? 47.892  74.380  13.527  1.00 24.34 ? 425 HOH E O   1 
HETATM 11982 O  O   . HOH GA 6 .   ? 37.853  64.559  15.140  1.00 53.14 ? 426 HOH E O   1 
HETATM 11983 O  O   . HOH GA 6 .   ? 48.406  84.083  13.763  1.00 41.97 ? 427 HOH E O   1 
HETATM 11984 O  O   . HOH GA 6 .   ? 44.752  68.439  36.627  1.00 39.69 ? 428 HOH E O   1 
HETATM 11985 O  O   . HOH GA 6 .   ? 63.838  82.033  13.615  1.00 40.87 ? 429 HOH E O   1 
HETATM 11986 O  O   . HOH GA 6 .   ? 56.931  52.493  2.499   1.00 49.67 ? 430 HOH E O   1 
HETATM 11987 O  O   . HOH GA 6 .   ? 55.863  81.032  13.097  1.00 30.52 ? 431 HOH E O   1 
HETATM 11988 O  O   . HOH GA 6 .   ? 59.500  55.471  28.149  1.00 44.81 ? 432 HOH E O   1 
HETATM 11989 O  O   . HOH GA 6 .   ? 66.192  65.577  21.020  1.00 32.56 ? 433 HOH E O   1 
HETATM 11990 O  O   . HOH GA 6 .   ? 44.541  68.008  8.209   1.00 48.19 ? 434 HOH E O   1 
HETATM 11991 O  O   . HOH GA 6 .   ? 62.262  61.809  28.641  1.00 43.18 ? 435 HOH E O   1 
HETATM 11992 O  O   . HOH GA 6 .   ? 63.980  60.411  1.359   1.00 55.28 ? 436 HOH E O   1 
HETATM 11993 O  O   . HOH GA 6 .   ? 48.505  51.811  27.714  1.00 40.39 ? 437 HOH E O   1 
HETATM 11994 O  O   . HOH GA 6 .   ? 46.502  51.612  0.916   1.00 43.79 ? 438 HOH E O   1 
HETATM 11995 O  O   . HOH GA 6 .   ? 65.552  72.093  10.536  1.00 48.99 ? 439 HOH E O   1 
HETATM 11996 O  O   . HOH GA 6 .   ? 59.079  53.084  23.672  1.00 40.57 ? 440 HOH E O   1 
HETATM 11997 O  O   . HOH GA 6 .   ? 46.834  53.026  28.864  1.00 44.63 ? 441 HOH E O   1 
HETATM 11998 O  O   . HOH GA 6 .   ? 51.226  80.858  20.743  1.00 42.81 ? 442 HOH E O   1 
HETATM 11999 O  O   . HOH GA 6 .   ? 45.236  57.529  35.175  1.00 44.15 ? 443 HOH E O   1 
HETATM 12000 O  O   . HOH GA 6 .   ? 62.143  70.198  28.938  1.00 57.50 ? 444 HOH E O   1 
HETATM 12001 O  O   . HOH GA 6 .   ? 64.787  68.005  21.155  1.00 38.82 ? 445 HOH E O   1 
HETATM 12002 O  O   . HOH GA 6 .   ? 49.541  77.389  23.340  1.00 42.63 ? 446 HOH E O   1 
HETATM 12003 O  O   . HOH GA 6 .   ? 62.539  67.795  20.290  1.00 34.62 ? 447 HOH E O   1 
HETATM 12004 O  O   . HOH GA 6 .   ? 64.746  62.610  9.065   1.00 41.39 ? 448 HOH E O   1 
HETATM 12005 O  O   . HOH GA 6 .   ? 48.250  69.967  6.250   1.00 50.85 ? 449 HOH E O   1 
HETATM 12006 O  O   . HOH GA 6 .   ? 44.448  68.474  13.114  1.00 37.89 ? 450 HOH E O   1 
HETATM 12007 O  O   . HOH GA 6 .   ? 64.099  78.783  26.062  1.00 34.73 ? 451 HOH E O   1 
HETATM 12008 O  O   . HOH GA 6 .   ? 47.319  42.756  8.668   1.00 48.71 ? 452 HOH E O   1 
HETATM 12009 O  O   . HOH GA 6 .   ? 55.215  67.452  3.309   1.00 48.45 ? 453 HOH E O   1 
HETATM 12010 O  O   . HOH GA 6 .   ? 51.873  77.580  24.744  1.00 43.95 ? 454 HOH E O   1 
HETATM 12011 O  O   . HOH GA 6 .   ? 65.428  65.685  25.587  1.00 52.68 ? 455 HOH E O   1 
HETATM 12012 O  O   . HOH GA 6 .   ? 41.983  73.417  31.010  1.00 54.43 ? 456 HOH E O   1 
HETATM 12013 O  O   . HOH GA 6 .   ? 58.911  54.114  29.866  1.00 52.80 ? 457 HOH E O   1 
HETATM 12014 O  O   . HOH GA 6 .   ? 64.051  60.570  7.192   1.00 40.68 ? 458 HOH E O   1 
HETATM 12015 O  O   . HOH GA 6 .   ? 64.143  70.637  15.485  1.00 45.95 ? 459 HOH E O   1 
HETATM 12016 O  O   . HOH GA 6 .   ? 53.161  61.261  2.346   1.00 37.87 ? 460 HOH E O   1 
HETATM 12017 O  O   . HOH GA 6 .   ? 44.557  47.874  15.701  1.00 47.44 ? 461 HOH E O   1 
HETATM 12018 O  O   . HOH GA 6 .   ? 68.528  65.437  19.551  1.00 50.92 ? 462 HOH E O   1 
HETATM 12019 O  O   . HOH GA 6 .   ? 53.886  62.390  34.274  1.00 40.87 ? 463 HOH E O   1 
HETATM 12020 O  O   . HOH GA 6 .   ? 41.457  58.109  2.876   1.00 45.44 ? 464 HOH E O   1 
HETATM 12021 O  O   . HOH GA 6 .   ? 57.475  62.232  33.788  1.00 50.88 ? 465 HOH E O   1 
HETATM 12022 O  O   . HOH GA 6 .   ? 37.422  59.977  33.047  1.00 37.68 ? 466 HOH E O   1 
HETATM 12023 O  O   . HOH GA 6 .   ? 46.528  76.439  20.200  1.00 49.53 ? 467 HOH E O   1 
HETATM 12024 O  O   . HOH GA 6 .   ? 57.444  84.405  15.418  1.00 23.65 ? 468 HOH E O   1 
HETATM 12025 O  O   . HOH GA 6 .   ? 53.313  84.239  15.118  1.00 28.07 ? 469 HOH E O   1 
HETATM 12026 O  O   . HOH GA 6 .   ? 55.488  69.077  5.349   1.00 40.40 ? 470 HOH E O   1 
HETATM 12027 O  O   . HOH GA 6 .   ? 64.725  69.622  18.962  1.00 47.24 ? 471 HOH E O   1 
HETATM 12028 O  O   . HOH GA 6 .   ? 55.823  78.822  26.257  1.00 38.68 ? 472 HOH E O   1 
HETATM 12029 O  O   . HOH GA 6 .   ? 41.525  57.810  33.963  1.00 29.04 ? 473 HOH E O   1 
HETATM 12030 O  O   . HOH GA 6 .   ? 72.007  51.044  24.800  1.00 57.57 ? 474 HOH E O   1 
HETATM 12031 O  O   . HOH GA 6 .   ? 55.640  83.600  13.729  1.00 27.19 ? 475 HOH E O   1 
HETATM 12032 O  O   . HOH GA 6 .   ? 53.024  79.942  24.573  1.00 37.91 ? 476 HOH E O   1 
HETATM 12033 O  O   . HOH GA 6 .   ? 58.111  79.140  10.359  1.00 43.05 ? 477 HOH E O   1 
HETATM 12034 O  O   . HOH GA 6 .   ? 69.453  64.625  24.091  1.00 56.08 ? 478 HOH E O   1 
HETATM 12035 O  O   . HOH GA 6 .   ? 54.152  67.111  34.635  1.00 45.51 ? 479 HOH E O   1 
HETATM 12036 O  O   . HOH GA 6 .   ? 47.956  76.166  27.750  1.00 53.04 ? 480 HOH E O   1 
HETATM 12037 O  O   . HOH GA 6 .   ? 43.084  49.628  22.286  1.00 51.21 ? 481 HOH E O   1 
HETATM 12038 O  O   . HOH GA 6 .   ? 50.889  79.943  23.086  1.00 49.66 ? 482 HOH E O   1 
HETATM 12039 O  O   . HOH GA 6 .   ? 43.865  75.906  27.103  1.00 47.03 ? 483 HOH E O   1 
HETATM 12040 O  O   . HOH GA 6 .   ? 63.712  62.827  32.456  1.00 57.42 ? 484 HOH E O   1 
HETATM 12041 O  O   . HOH GA 6 .   ? 40.597  56.679  31.655  1.00 43.55 ? 485 HOH E O   1 
HETATM 12042 O  O   . HOH GA 6 .   ? 67.388  69.010  16.865  1.00 53.71 ? 486 HOH E O   1 
HETATM 12043 O  O   . HOH GA 6 .   ? 38.674  57.772  -5.144  1.00 58.18 ? 487 HOH E O   1 
HETATM 12044 O  O   . HOH HA 6 .   ? 66.963  27.610  30.533  1.00 45.81 ? 301 HOH F O   1 
HETATM 12045 O  O   . HOH HA 6 .   ? 50.198  39.007  26.973  1.00 51.20 ? 302 HOH F O   1 
HETATM 12046 O  O   . HOH HA 6 .   ? 77.134  37.332  32.506  1.00 43.82 ? 303 HOH F O   1 
HETATM 12047 O  O   . HOH HA 6 .   ? 53.022  34.634  1.056   1.00 48.21 ? 304 HOH F O   1 
HETATM 12048 O  O   . HOH HA 6 .   ? 71.416  33.475  18.636  1.00 47.88 ? 305 HOH F O   1 
HETATM 12049 O  O   . HOH HA 6 .   ? 63.164  34.719  33.289  1.00 33.10 ? 306 HOH F O   1 
HETATM 12050 O  O   . HOH HA 6 .   ? 59.695  47.759  25.050  1.00 34.67 ? 307 HOH F O   1 
HETATM 12051 O  O   . HOH HA 6 .   ? 61.270  27.653  1.406   1.00 56.62 ? 308 HOH F O   1 
HETATM 12052 O  O   . HOH HA 6 .   ? 51.783  35.303  5.959   1.00 52.97 ? 309 HOH F O   1 
HETATM 12053 O  O   . HOH HA 6 .   ? 68.057  48.544  4.667   1.00 31.21 ? 310 HOH F O   1 
HETATM 12054 O  O   . HOH HA 6 .   ? 52.164  33.872  29.286  1.00 52.68 ? 311 HOH F O   1 
HETATM 12055 O  O   . HOH HA 6 .   ? 58.219  34.211  5.672   1.00 38.91 ? 312 HOH F O   1 
HETATM 12056 O  O   . HOH HA 6 .   ? 71.432  50.759  21.765  1.00 41.40 ? 313 HOH F O   1 
HETATM 12057 O  O   . HOH HA 6 .   ? 76.194  41.459  28.587  1.00 52.27 ? 314 HOH F O   1 
HETATM 12058 O  O   . HOH HA 6 .   ? 57.633  30.843  19.092  1.00 39.74 ? 315 HOH F O   1 
HETATM 12059 O  O   . HOH HA 6 .   ? 60.788  43.187  31.922  1.00 32.86 ? 316 HOH F O   1 
HETATM 12060 O  O   . HOH HA 6 .   ? 64.131  51.968  5.580   1.00 50.28 ? 317 HOH F O   1 
HETATM 12061 O  O   . HOH HA 6 .   ? 71.177  49.481  4.382   1.00 46.19 ? 318 HOH F O   1 
HETATM 12062 O  O   . HOH HA 6 .   ? 61.619  49.240  21.437  1.00 19.82 ? 319 HOH F O   1 
HETATM 12063 O  O   . HOH HA 6 .   ? 64.060  32.735  31.539  1.00 37.91 ? 320 HOH F O   1 
HETATM 12064 O  O   . HOH HA 6 .   ? 55.165  26.948  21.237  1.00 50.37 ? 321 HOH F O   1 
HETATM 12065 O  O   . HOH HA 6 .   ? 66.510  45.776  1.965   1.00 27.89 ? 322 HOH F O   1 
HETATM 12066 O  O   . HOH HA 6 .   ? 64.173  25.282  26.787  1.00 50.75 ? 323 HOH F O   1 
HETATM 12067 O  O   . HOH HA 6 .   ? 64.140  30.227  14.522  1.00 47.48 ? 324 HOH F O   1 
HETATM 12068 O  O   . HOH HA 6 .   ? 47.318  41.975  17.149  1.00 42.46 ? 325 HOH F O   1 
HETATM 12069 O  O   . HOH HA 6 .   ? 69.454  40.930  4.682   1.00 27.47 ? 326 HOH F O   1 
HETATM 12070 O  O   . HOH HA 6 .   ? 48.409  37.395  11.088  1.00 48.75 ? 327 HOH F O   1 
HETATM 12071 O  O   . HOH HA 6 .   ? 45.364  47.156  18.342  1.00 37.60 ? 328 HOH F O   1 
HETATM 12072 O  O   . HOH HA 6 .   ? 47.206  44.380  15.774  1.00 32.77 ? 329 HOH F O   1 
HETATM 12073 O  O   . HOH HA 6 .   ? 68.946  56.305  18.108  1.00 33.02 ? 330 HOH F O   1 
HETATM 12074 O  O   . HOH HA 6 .   ? 49.147  35.916  20.057  1.00 43.77 ? 331 HOH F O   1 
HETATM 12075 O  O   . HOH HA 6 .   ? 73.331  47.925  23.273  1.00 42.11 ? 332 HOH F O   1 
HETATM 12076 O  O   . HOH HA 6 .   ? 65.685  42.391  35.442  1.00 41.91 ? 333 HOH F O   1 
HETATM 12077 O  O   . HOH HA 6 .   ? 52.864  43.951  6.289   1.00 51.15 ? 334 HOH F O   1 
HETATM 12078 O  O   . HOH HA 6 .   ? 68.966  32.991  35.836  1.00 42.07 ? 335 HOH F O   1 
HETATM 12079 O  O   . HOH HA 6 .   ? 57.732  44.330  6.094   1.00 40.51 ? 336 HOH F O   1 
HETATM 12080 O  O   . HOH HA 6 .   ? 75.796  34.942  27.733  1.00 52.31 ? 337 HOH F O   1 
HETATM 12081 O  O   . HOH HA 6 .   ? 58.698  23.200  10.595  1.00 48.72 ? 338 HOH F O   1 
HETATM 12082 O  O   . HOH HA 6 .   ? 53.496  37.707  8.754   1.00 39.95 ? 339 HOH F O   1 
HETATM 12083 O  O   . HOH HA 6 .   ? 63.172  43.071  2.039   1.00 38.65 ? 340 HOH F O   1 
HETATM 12084 O  O   . HOH HA 6 .   ? 52.374  48.909  20.123  1.00 22.48 ? 341 HOH F O   1 
HETATM 12085 O  O   . HOH HA 6 .   ? 53.074  34.411  26.309  1.00 36.89 ? 342 HOH F O   1 
HETATM 12086 O  O   . HOH HA 6 .   ? 72.271  40.519  -2.130  1.00 37.22 ? 343 HOH F O   1 
HETATM 12087 O  O   . HOH HA 6 .   ? 57.983  46.468  8.472   1.00 51.61 ? 344 HOH F O   1 
HETATM 12088 O  O   . HOH HA 6 .   ? 60.077  20.286  20.709  1.00 51.71 ? 345 HOH F O   1 
HETATM 12089 O  O   . HOH HA 6 .   ? 70.899  50.378  17.530  1.00 37.63 ? 346 HOH F O   1 
HETATM 12090 O  O   . HOH HA 6 .   ? 77.211  46.497  10.421  1.00 60.01 ? 347 HOH F O   1 
HETATM 12091 O  O   . HOH HA 6 .   ? 56.162  38.570  30.507  1.00 46.29 ? 348 HOH F O   1 
HETATM 12092 O  O   . HOH HA 6 .   ? 50.969  47.157  27.186  1.00 53.72 ? 349 HOH F O   1 
HETATM 12093 O  O   . HOH HA 6 .   ? 72.908  34.215  22.689  1.00 36.11 ? 350 HOH F O   1 
HETATM 12094 O  O   . HOH HA 6 .   ? 61.131  49.862  2.555   1.00 47.42 ? 351 HOH F O   1 
HETATM 12095 O  O   . HOH HA 6 .   ? 58.351  48.729  22.377  1.00 27.69 ? 352 HOH F O   1 
HETATM 12096 O  O   . HOH HA 6 .   ? 59.738  38.986  31.878  1.00 32.01 ? 353 HOH F O   1 
HETATM 12097 O  O   . HOH HA 6 .   ? 45.531  43.690  18.840  1.00 39.54 ? 354 HOH F O   1 
HETATM 12098 O  O   . HOH HA 6 .   ? 58.311  43.506  35.419  1.00 47.20 ? 355 HOH F O   1 
HETATM 12099 O  O   . HOH HA 6 .   ? 72.604  50.217  0.872   1.00 39.42 ? 356 HOH F O   1 
HETATM 12100 O  O   . HOH HA 6 .   ? 51.783  42.697  8.696   1.00 40.13 ? 357 HOH F O   1 
HETATM 12101 O  O   . HOH HA 6 .   ? 70.968  34.279  7.290   1.00 38.56 ? 358 HOH F O   1 
HETATM 12102 O  O   . HOH HA 6 .   ? 70.487  62.188  13.305  1.00 51.66 ? 359 HOH F O   1 
HETATM 12103 O  O   . HOH HA 6 .   ? 61.606  43.507  -0.869  1.00 37.06 ? 360 HOH F O   1 
HETATM 12104 O  O   . HOH HA 6 .   ? 74.302  44.953  5.076   1.00 34.38 ? 361 HOH F O   1 
HETATM 12105 O  O   A HOH HA 6 .   ? 75.855  44.600  -0.921  0.50 42.66 ? 362 HOH F O   1 
HETATM 12106 O  O   B HOH HA 6 .   ? 76.126  42.872  -1.649  0.50 35.87 ? 362 HOH F O   1 
HETATM 12107 O  O   . HOH HA 6 .   ? 77.436  30.171  32.354  1.00 43.28 ? 363 HOH F O   1 
HETATM 12108 O  O   . HOH HA 6 .   ? 60.173  33.011  4.478   1.00 41.17 ? 364 HOH F O   1 
HETATM 12109 O  O   . HOH HA 6 .   ? 71.403  33.999  10.818  1.00 52.65 ? 365 HOH F O   1 
HETATM 12110 O  O   . HOH HA 6 .   ? 53.690  43.202  21.767  1.00 44.93 ? 366 HOH F O   1 
HETATM 12111 O  O   . HOH HA 6 .   ? 62.303  30.648  30.991  1.00 42.47 ? 367 HOH F O   1 
HETATM 12112 O  O   . HOH HA 6 .   ? 69.897  55.248  7.804   1.00 57.68 ? 368 HOH F O   1 
HETATM 12113 O  O   . HOH HA 6 .   ? 63.619  46.921  29.430  1.00 51.08 ? 369 HOH F O   1 
HETATM 12114 O  O   . HOH HA 6 .   ? 69.402  27.276  11.930  1.00 46.64 ? 370 HOH F O   1 
HETATM 12115 O  O   . HOH HA 6 .   ? 71.714  55.314  18.071  1.00 48.91 ? 371 HOH F O   1 
HETATM 12116 O  O   . HOH HA 6 .   ? 54.988  49.448  25.881  1.00 38.51 ? 372 HOH F O   1 
HETATM 12117 O  O   . HOH HA 6 .   ? 54.018  28.096  9.977   1.00 47.75 ? 373 HOH F O   1 
HETATM 12118 O  O   . HOH HA 6 .   ? 54.187  31.655  14.386  1.00 35.07 ? 374 HOH F O   1 
HETATM 12119 O  O   . HOH HA 6 .   ? 74.493  28.726  29.221  1.00 41.72 ? 375 HOH F O   1 
HETATM 12120 O  O   . HOH HA 6 .   ? 52.834  29.089  6.361   1.00 59.80 ? 376 HOH F O   1 
HETATM 12121 O  O   . HOH HA 6 .   ? 73.605  35.297  19.784  1.00 38.79 ? 377 HOH F O   1 
HETATM 12122 O  O   . HOH HA 6 .   ? 57.011  45.669  25.700  1.00 35.99 ? 378 HOH F O   1 
HETATM 12123 O  O   . HOH HA 6 .   ? 53.008  32.487  22.547  1.00 49.07 ? 379 HOH F O   1 
HETATM 12124 O  O   . HOH HA 6 .   ? 72.698  45.926  24.586  1.00 46.69 ? 380 HOH F O   1 
HETATM 12125 O  O   . HOH HA 6 .   ? 76.920  40.905  22.219  1.00 45.85 ? 381 HOH F O   1 
HETATM 12126 O  O   . HOH HA 6 .   ? 72.276  50.194  15.515  1.00 52.14 ? 382 HOH F O   1 
HETATM 12127 O  O   . HOH HA 6 .   ? 70.095  38.184  35.110  1.00 40.28 ? 383 HOH F O   1 
HETATM 12128 O  O   . HOH HA 6 .   ? 74.563  34.502  13.291  1.00 36.37 ? 384 HOH F O   1 
HETATM 12129 O  O   . HOH HA 6 .   ? 74.357  36.449  7.205   1.00 44.89 ? 385 HOH F O   1 
HETATM 12130 O  O   . HOH HA 6 .   ? 67.928  31.181  4.968   1.00 52.69 ? 386 HOH F O   1 
HETATM 12131 O  O   . HOH HA 6 .   ? 75.657  45.674  8.579   1.00 43.79 ? 387 HOH F O   1 
HETATM 12132 O  O   . HOH HA 6 .   ? 68.564  54.122  10.527  1.00 31.88 ? 388 HOH F O   1 
HETATM 12133 O  O   . HOH HA 6 .   ? 64.997  24.068  5.078   1.00 46.59 ? 389 HOH F O   1 
HETATM 12134 O  O   . HOH HA 6 .   ? 68.015  57.404  11.495  1.00 43.84 ? 390 HOH F O   1 
HETATM 12135 O  O   . HOH HA 6 .   ? 56.254  47.002  23.397  1.00 44.04 ? 391 HOH F O   1 
HETATM 12136 O  O   . HOH HA 6 .   ? 68.905  30.292  35.935  1.00 41.19 ? 392 HOH F O   1 
HETATM 12137 O  O   . HOH HA 6 .   ? 61.014  45.740  32.664  1.00 47.57 ? 393 HOH F O   1 
HETATM 12138 O  O   . HOH HA 6 .   ? 55.296  43.787  27.049  1.00 52.38 ? 394 HOH F O   1 
HETATM 12139 O  O   . HOH HA 6 .   ? 75.699  33.980  19.399  1.00 46.39 ? 395 HOH F O   1 
HETATM 12140 O  O   . HOH HA 6 .   ? 58.055  40.391  1.220   1.00 56.48 ? 396 HOH F O   1 
HETATM 12141 O  O   . HOH HA 6 .   ? 52.572  25.642  9.900   1.00 69.64 ? 397 HOH F O   1 
HETATM 12142 O  O   . HOH HA 6 .   ? 55.616  42.373  4.564   1.00 47.80 ? 398 HOH F O   1 
HETATM 12143 O  O   . HOH HA 6 .   ? 69.456  63.508  17.115  1.00 47.59 ? 399 HOH F O   1 
HETATM 12144 O  O   . HOH HA 6 .   ? 75.385  50.322  15.127  1.00 70.81 ? 400 HOH F O   1 
HETATM 12145 O  O   . HOH HA 6 .   ? 49.874  34.563  17.637  1.00 41.46 ? 401 HOH F O   1 
HETATM 12146 O  O   . HOH HA 6 .   ? 55.339  45.084  21.332  1.00 46.86 ? 402 HOH F O   1 
HETATM 12147 O  O   . HOH HA 6 .   ? 75.485  34.241  8.821   1.00 50.17 ? 403 HOH F O   1 
HETATM 12148 O  O   . HOH HA 6 .   ? 71.237  45.615  27.588  1.00 45.59 ? 404 HOH F O   1 
HETATM 12149 O  O   . HOH HA 6 .   ? 54.953  32.127  19.408  1.00 44.40 ? 405 HOH F O   1 
HETATM 12150 O  O   . HOH HA 6 .   ? 73.199  39.331  1.944   1.00 46.88 ? 406 HOH F O   1 
HETATM 12151 O  O   . HOH HA 6 .   ? 63.301  35.117  0.881   1.00 54.34 ? 407 HOH F O   1 
HETATM 12152 O  O   . HOH HA 6 .   ? 71.584  52.877  17.699  1.00 52.26 ? 408 HOH F O   1 
HETATM 12153 O  O   A HOH HA 6 .   ? 53.640  32.496  16.921  0.50 28.99 ? 409 HOH F O   1 
HETATM 12154 O  O   B HOH HA 6 .   ? 51.973  32.370  17.506  0.50 31.81 ? 409 HOH F O   1 
HETATM 12155 O  O   . HOH HA 6 .   ? 48.409  49.023  27.130  1.00 50.72 ? 410 HOH F O   1 
HETATM 12156 O  O   . HOH HA 6 .   ? 78.326  45.669  1.042   1.00 59.09 ? 411 HOH F O   1 
HETATM 12157 O  O   . HOH HA 6 .   ? 76.415  33.066  10.573  1.00 46.26 ? 412 HOH F O   1 
HETATM 12158 O  O   . HOH HA 6 .   ? 67.194  51.540  1.607   1.00 45.07 ? 413 HOH F O   1 
HETATM 12159 O  O   . HOH HA 6 .   ? 77.434  35.758  13.681  1.00 53.03 ? 414 HOH F O   1 
HETATM 12160 O  O   . HOH HA 6 .   ? 70.178  58.868  11.308  1.00 41.32 ? 415 HOH F O   1 
HETATM 12161 O  O   . HOH HA 6 .   ? 71.621  51.554  2.655   1.00 46.81 ? 416 HOH F O   1 
HETATM 12162 O  O   . HOH HA 6 .   ? 50.683  31.598  20.776  1.00 54.54 ? 417 HOH F O   1 
HETATM 12163 O  O   . HOH HA 6 .   ? 68.854  61.456  19.358  1.00 50.22 ? 418 HOH F O   1 
HETATM 12164 O  O   . HOH HA 6 .   ? 76.303  38.846  34.660  1.00 44.35 ? 419 HOH F O   1 
HETATM 12165 O  O   . HOH HA 6 .   ? 72.769  32.645  8.613   1.00 53.43 ? 420 HOH F O   1 
HETATM 12166 O  O   . HOH HA 6 .   ? 72.012  40.365  35.256  1.00 40.69 ? 421 HOH F O   1 
HETATM 12167 O  O   . HOH HA 6 .   ? 59.625  36.360  32.885  1.00 42.32 ? 422 HOH F O   1 
HETATM 12168 O  O   . HOH HA 6 .   ? 76.778  44.348  3.870   1.00 46.51 ? 423 HOH F O   1 
HETATM 12169 O  O   . HOH HA 6 .   ? 72.146  33.254  13.378  1.00 48.92 ? 424 HOH F O   1 
HETATM 12170 O  O   . HOH HA 6 .   ? 63.060  51.570  3.247   1.00 54.27 ? 425 HOH F O   1 
HETATM 12171 O  O   . HOH HA 6 .   ? 73.894  24.663  38.033  1.00 55.29 ? 426 HOH F O   1 
HETATM 12172 O  O   . HOH HA 6 .   ? 48.744  32.551  12.217  1.00 48.55 ? 427 HOH F O   1 
HETATM 12173 O  O   . HOH HA 6 .   ? 60.552  22.327  6.553   1.00 54.02 ? 428 HOH F O   1 
HETATM 12174 O  O   . HOH HA 6 .   ? 47.800  31.325  20.082  1.00 63.25 ? 429 HOH F O   1 
HETATM 12175 O  O   . HOH IA 6 .   ? 100.693 99.974  -30.143 1.00 44.62 ? 301 HOH G O   1 
HETATM 12176 O  O   . HOH IA 6 .   ? 100.131 115.272 -10.366 1.00 41.20 ? 302 HOH G O   1 
HETATM 12177 O  O   . HOH IA 6 .   ? 91.873  104.895 -3.577  1.00 30.45 ? 303 HOH G O   1 
HETATM 12178 O  O   . HOH IA 6 .   ? 96.494  114.555 -7.345  1.00 42.73 ? 304 HOH G O   1 
HETATM 12179 O  O   . HOH IA 6 .   ? 102.786 98.799  0.072   1.00 47.45 ? 305 HOH G O   1 
HETATM 12180 O  O   . HOH IA 6 .   ? 98.066  91.934  -27.609 1.00 48.82 ? 306 HOH G O   1 
HETATM 12181 O  O   . HOH IA 6 .   ? 95.548  116.425 -20.473 1.00 25.80 ? 307 HOH G O   1 
HETATM 12182 O  O   . HOH IA 6 .   ? 110.904 104.613 -12.303 1.00 40.42 ? 308 HOH G O   1 
HETATM 12183 O  O   . HOH IA 6 .   ? 90.009  97.090  -0.806  1.00 49.54 ? 309 HOH G O   1 
HETATM 12184 O  O   . HOH IA 6 .   ? 96.598  88.071  -19.938 1.00 37.08 ? 310 HOH G O   1 
HETATM 12185 O  O   . HOH IA 6 .   ? 83.324  94.606  -14.601 1.00 36.68 ? 311 HOH G O   1 
HETATM 12186 O  O   . HOH IA 6 .   ? 88.845  105.062 -9.989  1.00 41.61 ? 312 HOH G O   1 
HETATM 12187 O  O   . HOH IA 6 .   ? 83.043  92.228  -13.109 1.00 35.82 ? 313 HOH G O   1 
HETATM 12188 O  O   . HOH IA 6 .   ? 105.588 105.026 -7.360  1.00 37.51 ? 314 HOH G O   1 
HETATM 12189 O  O   . HOH IA 6 .   ? 88.085  100.746 -6.419  1.00 43.27 ? 315 HOH G O   1 
HETATM 12190 O  O   . HOH IA 6 .   ? 105.472 81.574  -10.336 1.00 45.09 ? 316 HOH G O   1 
HETATM 12191 O  O   . HOH IA 6 .   ? 101.022 115.970 -16.460 1.00 37.89 ? 317 HOH G O   1 
HETATM 12192 O  O   . HOH IA 6 .   ? 98.268  87.473  -15.999 1.00 23.12 ? 318 HOH G O   1 
HETATM 12193 O  O   . HOH IA 6 .   ? 96.991  96.997  1.653   1.00 42.02 ? 319 HOH G O   1 
HETATM 12194 O  O   . HOH IA 6 .   ? 97.051  112.350 -22.543 1.00 35.85 ? 320 HOH G O   1 
HETATM 12195 O  O   . HOH IA 6 .   ? 101.992 113.506 -18.128 1.00 40.57 ? 321 HOH G O   1 
HETATM 12196 O  O   . HOH IA 6 .   ? 93.171  95.636  -26.667 1.00 49.83 ? 322 HOH G O   1 
HETATM 12197 O  O   . HOH IA 6 .   ? 81.740  88.872  -15.179 1.00 37.80 ? 323 HOH G O   1 
HETATM 12198 O  O   . HOH IA 6 .   ? 105.352 105.809 -13.602 1.00 35.32 ? 324 HOH G O   1 
HETATM 12199 O  O   . HOH IA 6 .   ? 114.237 105.172 -28.167 1.00 54.76 ? 325 HOH G O   1 
HETATM 12200 O  O   . HOH IA 6 .   ? 93.610  119.273 -13.455 1.00 25.36 ? 326 HOH G O   1 
HETATM 12201 O  O   . HOH IA 6 .   ? 86.259  95.684  -5.891  1.00 46.20 ? 327 HOH G O   1 
HETATM 12202 O  O   . HOH IA 6 .   ? 98.807  107.966 -12.307 1.00 28.84 ? 328 HOH G O   1 
HETATM 12203 O  O   . HOH IA 6 .   ? 98.919  104.474 -28.491 1.00 34.39 ? 329 HOH G O   1 
HETATM 12204 O  O   . HOH IA 6 .   ? 92.232  94.751  -2.257  1.00 41.32 ? 330 HOH G O   1 
HETATM 12205 O  O   . HOH IA 6 .   ? 108.752 102.607 -18.762 1.00 43.14 ? 331 HOH G O   1 
HETATM 12206 O  O   . HOH IA 6 .   ? 90.806  118.680 -13.462 1.00 41.98 ? 332 HOH G O   1 
HETATM 12207 O  O   . HOH IA 6 .   ? 94.173  89.957  -21.049 1.00 44.55 ? 333 HOH G O   1 
HETATM 12208 O  O   . HOH IA 6 .   ? 86.032  108.080 -17.893 1.00 45.19 ? 334 HOH G O   1 
HETATM 12209 O  O   . HOH IA 6 .   ? 100.746 90.876  4.912   1.00 59.28 ? 335 HOH G O   1 
HETATM 12210 O  O   . HOH IA 6 .   ? 100.857 102.090 -28.405 1.00 39.62 ? 336 HOH G O   1 
HETATM 12211 O  O   . HOH IA 6 .   ? 97.532  122.244 -15.067 1.00 30.70 ? 337 HOH G O   1 
HETATM 12212 O  O   . HOH IA 6 .   ? 94.168  106.368 -2.570  1.00 36.48 ? 338 HOH G O   1 
HETATM 12213 O  O   . HOH IA 6 .   ? 90.833  108.861 -20.628 1.00 41.74 ? 339 HOH G O   1 
HETATM 12214 O  O   . HOH IA 6 .   ? 85.524  110.277 -16.250 1.00 63.13 ? 340 HOH G O   1 
HETATM 12215 O  O   . HOH IA 6 .   ? 107.805 96.804  -29.833 1.00 41.39 ? 341 HOH G O   1 
HETATM 12216 O  O   . HOH IA 6 .   ? 105.069 110.943 -24.601 1.00 41.03 ? 342 HOH G O   1 
HETATM 12217 O  O   . HOH IA 6 .   ? 99.155  120.388 -17.334 1.00 34.13 ? 343 HOH G O   1 
HETATM 12218 O  O   . HOH IA 6 .   ? 93.363  105.797 -17.614 1.00 30.95 ? 344 HOH G O   1 
HETATM 12219 O  O   . HOH IA 6 .   ? 88.371  109.825 -9.685  1.00 37.71 ? 345 HOH G O   1 
HETATM 12220 O  O   . HOH IA 6 .   ? 83.296  100.199 -9.734  1.00 44.98 ? 346 HOH G O   1 
HETATM 12221 O  O   . HOH IA 6 .   ? 89.584  100.951 -24.235 1.00 32.87 ? 347 HOH G O   1 
HETATM 12222 O  O   . HOH IA 6 .   ? 88.488  119.243 -9.608  1.00 53.81 ? 348 HOH G O   1 
HETATM 12223 O  O   . HOH IA 6 .   ? 104.836 105.410 -3.445  1.00 46.86 ? 349 HOH G O   1 
HETATM 12224 O  O   . HOH IA 6 .   ? 111.697 101.939 -21.453 1.00 38.15 ? 350 HOH G O   1 
HETATM 12225 O  O   . HOH IA 6 .   ? 105.248 104.991 -10.810 1.00 63.47 ? 351 HOH G O   1 
HETATM 12226 O  O   . HOH IA 6 .   ? 98.033  115.453 -3.819  1.00 42.33 ? 352 HOH G O   1 
HETATM 12227 O  O   . HOH IA 6 .   ? 95.343  87.587  -17.273 1.00 36.91 ? 353 HOH G O   1 
HETATM 12228 O  O   . HOH IA 6 .   ? 89.517  103.470 -20.473 1.00 46.66 ? 354 HOH G O   1 
HETATM 12229 O  O   . HOH IA 6 .   ? 108.626 95.604  0.648   1.00 41.54 ? 355 HOH G O   1 
HETATM 12230 O  O   . HOH IA 6 .   ? 89.269  105.843 -13.074 1.00 32.87 ? 356 HOH G O   1 
HETATM 12231 O  O   . HOH IA 6 .   ? 105.636 105.303 -32.374 1.00 52.57 ? 357 HOH G O   1 
HETATM 12232 O  O   . HOH IA 6 .   ? 108.523 100.796 -32.824 1.00 66.13 ? 358 HOH G O   1 
HETATM 12233 O  O   . HOH IA 6 .   ? 85.009  100.253 -18.249 1.00 46.13 ? 359 HOH G O   1 
HETATM 12234 O  O   . HOH IA 6 .   ? 97.216  95.503  -28.187 1.00 50.09 ? 360 HOH G O   1 
HETATM 12235 O  O   . HOH IA 6 .   ? 109.159 104.550 -9.156  1.00 35.24 ? 361 HOH G O   1 
HETATM 12236 O  O   . HOH IA 6 .   ? 89.566  114.608 -22.796 1.00 41.63 ? 362 HOH G O   1 
HETATM 12237 O  O   . HOH IA 6 .   ? 91.400  106.082 -19.606 1.00 38.29 ? 363 HOH G O   1 
HETATM 12238 O  O   . HOH IA 6 .   ? 90.687  112.832 -0.351  1.00 58.15 ? 364 HOH G O   1 
HETATM 12239 O  O   . HOH IA 6 .   ? 88.896  87.447  -15.960 1.00 24.85 ? 365 HOH G O   1 
HETATM 12240 O  O   . HOH IA 6 .   ? 101.419 108.824 -2.552  1.00 48.96 ? 366 HOH G O   1 
HETATM 12241 O  O   . HOH IA 6 .   ? 106.950 87.780  -10.752 1.00 40.62 ? 367 HOH G O   1 
HETATM 12242 O  O   . HOH IA 6 .   ? 89.781  109.253 1.540   1.00 48.96 ? 368 HOH G O   1 
HETATM 12243 O  O   . HOH IA 6 .   ? 100.349 110.792 -25.223 1.00 53.65 ? 369 HOH G O   1 
HETATM 12244 O  O   . HOH IA 6 .   ? 111.360 98.271  -9.552  1.00 41.72 ? 370 HOH G O   1 
HETATM 12245 O  O   . HOH IA 6 .   ? 103.827 85.054  -3.591  1.00 48.39 ? 371 HOH G O   1 
HETATM 12246 O  O   . HOH IA 6 .   ? 95.664  90.021  2.500   1.00 52.48 ? 372 HOH G O   1 
HETATM 12247 O  O   . HOH IA 6 .   ? 96.074  106.084 -31.001 1.00 52.38 ? 373 HOH G O   1 
HETATM 12248 O  O   . HOH IA 6 .   ? 86.449  116.222 -19.138 1.00 31.87 ? 374 HOH G O   1 
HETATM 12249 O  O   . HOH IA 6 .   ? 90.472  92.734  -18.093 1.00 37.65 ? 375 HOH G O   1 
HETATM 12250 O  O   . HOH IA 6 .   ? 86.726  105.602 -8.532  1.00 46.79 ? 376 HOH G O   1 
HETATM 12251 O  O   . HOH IA 6 .   ? 92.153  86.179  -21.033 1.00 42.96 ? 377 HOH G O   1 
HETATM 12252 O  O   . HOH IA 6 .   ? 96.281  106.556 -1.028  1.00 49.06 ? 378 HOH G O   1 
HETATM 12253 O  O   . HOH IA 6 .   ? 90.921  118.991 -9.721  1.00 52.49 ? 379 HOH G O   1 
HETATM 12254 O  O   . HOH IA 6 .   ? 109.244 90.971  -18.240 1.00 46.47 ? 380 HOH G O   1 
HETATM 12255 O  O   . HOH IA 6 .   ? 107.822 90.901  -21.636 1.00 51.38 ? 381 HOH G O   1 
HETATM 12256 O  O   . HOH IA 6 .   ? 103.679 111.582 -9.773  1.00 33.78 ? 382 HOH G O   1 
HETATM 12257 O  O   . HOH IA 6 .   ? 110.309 94.992  -2.707  1.00 45.70 ? 383 HOH G O   1 
HETATM 12258 O  O   . HOH IA 6 .   ? 98.667  108.333 -1.579  1.00 49.69 ? 384 HOH G O   1 
HETATM 12259 O  O   . HOH IA 6 .   ? 85.567  101.747 -16.098 1.00 39.49 ? 385 HOH G O   1 
HETATM 12260 O  O   . HOH IA 6 .   ? 112.812 92.920  -6.985  1.00 64.46 ? 386 HOH G O   1 
HETATM 12261 O  O   . HOH IA 6 .   ? 86.015  108.731 -5.947  1.00 48.67 ? 387 HOH G O   1 
HETATM 12262 O  O   . HOH IA 6 .   ? 92.430  90.664  -23.452 1.00 58.19 ? 388 HOH G O   1 
HETATM 12263 O  O   . HOH IA 6 .   ? 103.726 121.765 -12.246 1.00 49.84 ? 389 HOH G O   1 
HETATM 12264 O  O   . HOH IA 6 .   ? 104.481 109.166 -13.775 1.00 42.89 ? 390 HOH G O   1 
HETATM 12265 O  O   . HOH IA 6 .   ? 89.280  104.336 -15.329 1.00 37.25 ? 391 HOH G O   1 
HETATM 12266 O  O   . HOH IA 6 .   ? 92.918  89.586  -18.607 1.00 47.24 ? 392 HOH G O   1 
HETATM 12267 O  O   . HOH IA 6 .   ? 90.458  104.243 -17.626 1.00 39.71 ? 393 HOH G O   1 
HETATM 12268 O  O   . HOH IA 6 .   ? 87.179  99.548  -4.166  1.00 44.51 ? 394 HOH G O   1 
HETATM 12269 O  O   . HOH IA 6 .   ? 86.868  104.356 -15.953 1.00 47.57 ? 395 HOH G O   1 
HETATM 12270 O  O   . HOH IA 6 .   ? 87.023  114.722 -21.807 1.00 46.28 ? 396 HOH G O   1 
HETATM 12271 O  O   . HOH IA 6 .   ? 92.251  86.650  -18.389 1.00 44.44 ? 397 HOH G O   1 
HETATM 12272 O  O   . HOH IA 6 .   ? 96.922  105.114 1.011   1.00 56.50 ? 398 HOH G O   1 
HETATM 12273 O  O   . HOH IA 6 .   ? 88.191  97.762  -2.150  1.00 52.56 ? 399 HOH G O   1 
HETATM 12274 O  O   . HOH IA 6 .   ? 102.100 114.066 -20.131 1.00 40.30 ? 400 HOH G O   1 
HETATM 12275 O  O   . HOH IA 6 .   ? 101.395 119.194 -17.419 1.00 46.20 ? 401 HOH G O   1 
HETATM 12276 O  O   . HOH IA 6 .   ? 106.918 106.017 -9.571  1.00 46.97 ? 402 HOH G O   1 
HETATM 12277 O  O   . HOH IA 6 .   ? 104.650 113.203 -16.493 1.00 43.96 ? 403 HOH G O   1 
HETATM 12278 O  O   . HOH IA 6 .   ? 94.691  121.618 -12.635 1.00 35.42 ? 404 HOH G O   1 
HETATM 12279 O  O   . HOH IA 6 .   ? 98.975  121.491 -12.804 1.00 34.36 ? 405 HOH G O   1 
HETATM 12280 O  O   . HOH IA 6 .   ? 100.083 117.502 -18.647 1.00 48.91 ? 406 HOH G O   1 
HETATM 12281 O  O   . HOH IA 6 .   ? 98.096  115.710 -21.313 1.00 42.25 ? 407 HOH G O   1 
HETATM 12282 O  O   . HOH IA 6 .   ? 97.131  121.080 -11.188 1.00 40.81 ? 408 HOH G O   1 
HETATM 12283 O  O   . HOH IA 6 .   ? 82.805  98.029  -3.361  1.00 50.68 ? 409 HOH G O   1 
HETATM 12284 O  O   . HOH JA 6 .   ? 92.250  61.405  -1.621  1.00 40.70 ? 301 HOH H O   1 
HETATM 12285 O  O   . HOH JA 6 .   ? 98.443  63.729  -14.859 1.00 44.15 ? 302 HOH H O   1 
HETATM 12286 O  O   . HOH JA 6 .   ? 79.384  61.023  -29.359 1.00 53.90 ? 303 HOH H O   1 
HETATM 12287 O  O   . HOH JA 6 .   ? 80.293  77.408  -24.502 1.00 49.71 ? 304 HOH H O   1 
HETATM 12288 O  O   . HOH JA 6 .   ? 81.352  65.966  -15.044 1.00 43.75 ? 305 HOH H O   1 
HETATM 12289 O  O   . HOH JA 6 .   ? 100.106 57.238  -14.170 1.00 43.54 ? 306 HOH H O   1 
HETATM 12290 O  O   . HOH JA 6 .   ? 84.358  59.491  -27.200 1.00 43.46 ? 307 HOH H O   1 
HETATM 12291 O  O   . HOH JA 6 .   ? 84.020  77.785  1.197   1.00 49.01 ? 308 HOH H O   1 
HETATM 12292 O  O   . HOH JA 6 .   ? 104.572 74.699  -5.560  1.00 50.99 ? 309 HOH H O   1 
HETATM 12293 O  O   . HOH JA 6 .   ? 88.762  63.229  -21.884 1.00 50.31 ? 310 HOH H O   1 
HETATM 12294 O  O   . HOH JA 6 .   ? 87.831  63.615  -23.976 1.00 42.06 ? 311 HOH H O   1 
HETATM 12295 O  O   . HOH JA 6 .   ? 94.919  81.403  -0.638  1.00 39.92 ? 312 HOH H O   1 
HETATM 12296 O  O   . HOH JA 6 .   ? 89.723  80.252  3.224   1.00 48.04 ? 313 HOH H O   1 
HETATM 12297 O  O   . HOH JA 6 .   ? 92.262  78.688  -26.478 1.00 36.89 ? 314 HOH H O   1 
HETATM 12298 O  O   . HOH JA 6 .   ? 77.795  70.407  -21.618 1.00 31.86 ? 315 HOH H O   1 
HETATM 12299 O  O   . HOH JA 6 .   ? 76.374  71.955  -26.819 1.00 41.48 ? 316 HOH H O   1 
HETATM 12300 O  O   . HOH JA 6 .   ? 79.656  62.792  -8.497  1.00 48.26 ? 317 HOH H O   1 
HETATM 12301 O  O   . HOH JA 6 .   ? 105.407 78.788  -11.535 1.00 41.72 ? 318 HOH H O   1 
HETATM 12302 O  O   . HOH JA 6 .   ? 99.964  85.502  -14.980 1.00 30.42 ? 319 HOH H O   1 
HETATM 12303 O  O   . HOH JA 6 .   ? 93.035  83.835  -20.055 1.00 40.61 ? 320 HOH H O   1 
HETATM 12304 O  O   . HOH JA 6 .   ? 97.532  85.418  -20.491 1.00 42.80 ? 321 HOH H O   1 
HETATM 12305 O  O   . HOH JA 6 .   ? 107.099 84.485  -13.011 1.00 43.80 ? 322 HOH H O   1 
HETATM 12306 O  O   . HOH JA 6 .   ? 82.981  68.493  -10.047 1.00 33.55 ? 323 HOH H O   1 
HETATM 12307 O  O   . HOH JA 6 .   ? 95.762  67.265  -13.009 1.00 39.76 ? 324 HOH H O   1 
HETATM 12308 O  O   . HOH JA 6 .   ? 92.681  59.717  -17.116 1.00 39.13 ? 325 HOH H O   1 
HETATM 12309 O  O   . HOH JA 6 .   ? 91.498  66.215  -24.773 1.00 36.38 ? 326 HOH H O   1 
HETATM 12310 O  O   . HOH JA 6 .   ? 80.730  58.728  -27.987 1.00 45.99 ? 327 HOH H O   1 
HETATM 12311 O  O   . HOH JA 6 .   ? 95.353  82.019  -20.323 1.00 40.67 ? 328 HOH H O   1 
HETATM 12312 O  O   . HOH JA 6 .   ? 76.524  76.659  -23.238 1.00 44.20 ? 329 HOH H O   1 
HETATM 12313 O  O   . HOH JA 6 .   ? 93.807  56.350  -13.666 1.00 42.09 ? 330 HOH H O   1 
HETATM 12314 O  O   . HOH JA 6 .   ? 81.045  86.429  -16.648 1.00 40.89 ? 331 HOH H O   1 
HETATM 12315 O  O   . HOH JA 6 .   ? 82.377  70.267  -5.235  1.00 36.46 ? 332 HOH H O   1 
HETATM 12316 O  O   . HOH JA 6 .   ? 81.552  68.850  -12.495 1.00 27.57 ? 333 HOH H O   1 
HETATM 12317 O  O   . HOH JA 6 .   ? 82.844  73.019  -29.120 1.00 29.95 ? 334 HOH H O   1 
HETATM 12318 O  O   . HOH JA 6 .   ? 99.611  74.718  -2.769  1.00 41.44 ? 335 HOH H O   1 
HETATM 12319 O  O   . HOH JA 6 .   ? 85.037  64.907  -29.370 1.00 42.78 ? 336 HOH H O   1 
HETATM 12320 O  O   . HOH JA 6 .   ? 86.418  61.469  -26.542 1.00 43.05 ? 337 HOH H O   1 
HETATM 12321 O  O   . HOH JA 6 .   ? 90.601  62.283  5.389   1.00 51.95 ? 338 HOH H O   1 
HETATM 12322 O  O   . HOH JA 6 .   ? 97.598  71.245  -24.000 1.00 57.98 ? 339 HOH H O   1 
HETATM 12323 O  O   . HOH JA 6 .   ? 98.683  60.208  -16.768 1.00 50.88 ? 340 HOH H O   1 
HETATM 12324 O  O   . HOH JA 6 .   ? 99.690  65.145  -4.097  1.00 38.20 ? 341 HOH H O   1 
HETATM 12325 O  O   . HOH JA 6 .   ? 96.997  79.412  1.687   1.00 46.99 ? 342 HOH H O   1 
HETATM 12326 O  O   . HOH JA 6 .   ? 90.262  69.931  -27.680 1.00 38.66 ? 343 HOH H O   1 
HETATM 12327 O  O   . HOH JA 6 .   ? 90.699  60.141  -19.559 1.00 52.67 ? 344 HOH H O   1 
HETATM 12328 O  O   . HOH JA 6 .   ? 89.608  66.429  -8.414  1.00 30.71 ? 345 HOH H O   1 
HETATM 12329 O  O   . HOH JA 6 .   ? 73.871  71.385  -21.160 1.00 30.48 ? 346 HOH H O   1 
HETATM 12330 O  O   . HOH JA 6 .   ? 95.153  71.405  0.329   1.00 37.79 ? 347 HOH H O   1 
HETATM 12331 O  O   . HOH JA 6 .   ? 80.120  62.545  -16.635 1.00 26.07 ? 348 HOH H O   1 
HETATM 12332 O  O   . HOH JA 6 .   ? 84.492  63.505  -5.728  1.00 36.57 ? 349 HOH H O   1 
HETATM 12333 O  O   . HOH JA 6 .   ? 86.299  61.066  2.062   1.00 52.98 ? 350 HOH H O   1 
HETATM 12334 O  O   . HOH JA 6 .   ? 77.371  80.017  -2.870  1.00 46.82 ? 351 HOH H O   1 
HETATM 12335 O  O   . HOH JA 6 .   ? 93.993  85.128  -17.111 1.00 32.59 ? 352 HOH H O   1 
HETATM 12336 O  O   . HOH JA 6 .   ? 82.460  76.139  3.154   1.00 51.12 ? 353 HOH H O   1 
HETATM 12337 O  O   . HOH JA 6 .   ? 80.398  91.311  -12.942 1.00 46.12 ? 354 HOH H O   1 
HETATM 12338 O  O   . HOH JA 6 .   ? 90.711  85.521  -16.299 1.00 27.12 ? 355 HOH H O   1 
HETATM 12339 O  O   . HOH JA 6 .   ? 87.051  59.416  -12.917 1.00 29.76 ? 356 HOH H O   1 
HETATM 12340 O  O   . HOH JA 6 .   ? 97.895  66.705  -14.995 1.00 46.06 ? 357 HOH H O   1 
HETATM 12341 O  O   . HOH JA 6 .   ? 76.723  82.497  -2.789  1.00 41.12 ? 358 HOH H O   1 
HETATM 12342 O  O   . HOH JA 6 .   ? 85.960  60.724  -20.987 1.00 28.85 ? 359 HOH H O   1 
HETATM 12343 O  O   . HOH JA 6 .   ? 80.259  69.083  -16.460 1.00 31.42 ? 360 HOH H O   1 
HETATM 12344 O  O   . HOH JA 6 .   ? 96.944  74.921  -24.542 1.00 46.77 ? 361 HOH H O   1 
HETATM 12345 O  O   . HOH JA 6 .   ? 93.379  74.883  -26.303 1.00 38.05 ? 362 HOH H O   1 
HETATM 12346 O  O   . HOH JA 6 .   ? 87.991  57.379  -10.942 1.00 39.97 ? 363 HOH H O   1 
HETATM 12347 O  O   . HOH JA 6 .   ? 91.576  86.749  2.684   1.00 48.45 ? 364 HOH H O   1 
HETATM 12348 O  O   . HOH JA 6 .   ? 103.189 54.439  -9.113  1.00 45.24 ? 365 HOH H O   1 
HETATM 12349 O  O   . HOH JA 6 .   ? 103.870 72.801  -14.061 1.00 46.69 ? 366 HOH H O   1 
HETATM 12350 O  O   . HOH JA 6 .   ? 100.939 80.282  -3.117  1.00 42.09 ? 367 HOH H O   1 
HETATM 12351 O  O   . HOH JA 6 .   ? 78.290  69.420  -18.923 1.00 47.91 ? 368 HOH H O   1 
HETATM 12352 O  O   . HOH JA 6 .   ? 89.918  68.558  -25.551 1.00 32.67 ? 369 HOH H O   1 
HETATM 12353 O  O   . HOH JA 6 .   ? 79.469  83.292  -18.043 1.00 40.40 ? 370 HOH H O   1 
HETATM 12354 O  O   . HOH JA 6 .   ? 81.432  86.104  -12.004 1.00 37.38 ? 371 HOH H O   1 
HETATM 12355 O  O   . HOH JA 6 .   ? 100.291 70.837  -20.632 1.00 36.42 ? 372 HOH H O   1 
HETATM 12356 O  O   . HOH JA 6 .   ? 78.461  81.234  0.451   1.00 34.29 ? 373 HOH H O   1 
HETATM 12357 O  O   . HOH JA 6 .   ? 83.688  90.273  -5.333  1.00 41.76 ? 374 HOH H O   1 
HETATM 12358 O  O   . HOH JA 6 .   ? 84.559  85.246  1.046   1.00 60.56 ? 375 HOH H O   1 
HETATM 12359 O  O   . HOH JA 6 .   ? 92.807  70.277  1.407   1.00 40.66 ? 376 HOH H O   1 
HETATM 12360 O  O   . HOH JA 6 .   ? 100.328 69.126  -16.441 1.00 50.30 ? 377 HOH H O   1 
HETATM 12361 O  O   . HOH JA 6 .   ? 75.215  68.295  -27.766 1.00 48.09 ? 378 HOH H O   1 
HETATM 12362 O  O   . HOH JA 6 .   ? 80.266  81.127  -19.478 1.00 40.20 ? 379 HOH H O   1 
HETATM 12363 O  O   . HOH JA 6 .   ? 80.092  85.798  -10.302 1.00 40.98 ? 380 HOH H O   1 
HETATM 12364 O  O   . HOH JA 6 .   ? 79.921  70.612  -14.036 1.00 25.27 ? 381 HOH H O   1 
HETATM 12365 O  O   . HOH JA 6 .   ? 87.765  71.520  -30.965 1.00 44.79 ? 382 HOH H O   1 
HETATM 12366 O  O   . HOH JA 6 .   ? 78.558  70.244  -7.510  1.00 39.80 ? 383 HOH H O   1 
HETATM 12367 O  O   . HOH JA 6 .   ? 102.300 56.718  -11.246 1.00 47.83 ? 384 HOH H O   1 
HETATM 12368 O  O   . HOH JA 6 .   ? 83.653  65.448  -10.501 1.00 35.64 ? 385 HOH H O   1 
HETATM 12369 O  O   . HOH JA 6 .   ? 76.422  70.653  -15.597 1.00 37.47 ? 386 HOH H O   1 
HETATM 12370 O  O   . HOH JA 6 .   ? 82.702  70.404  -1.583  1.00 47.20 ? 387 HOH H O   1 
HETATM 12371 O  O   . HOH JA 6 .   ? 99.146  68.509  -8.136  1.00 39.54 ? 388 HOH H O   1 
HETATM 12372 O  O   . HOH JA 6 .   ? 84.357  93.461  -6.283  1.00 44.29 ? 389 HOH H O   1 
HETATM 12373 O  O   . HOH JA 6 .   ? 89.341  60.674  1.431   1.00 43.97 ? 390 HOH H O   1 
HETATM 12374 O  O   . HOH JA 6 .   ? 100.152 64.231  1.286   1.00 54.27 ? 391 HOH H O   1 
HETATM 12375 O  O   . HOH JA 6 .   ? 103.333 71.705  -11.731 1.00 42.74 ? 392 HOH H O   1 
HETATM 12376 O  O   . HOH JA 6 .   ? 97.761  81.549  -16.130 1.00 48.51 ? 393 HOH H O   1 
HETATM 12377 O  O   . HOH JA 6 .   ? 85.032  61.062  -4.911  1.00 44.53 ? 394 HOH H O   1 
HETATM 12378 O  O   . HOH JA 6 .   ? 79.123  72.330  -1.478  1.00 49.92 ? 395 HOH H O   1 
HETATM 12379 O  O   . HOH JA 6 .   ? 92.913  51.670  -7.113  1.00 56.24 ? 396 HOH H O   1 
HETATM 12380 O  O   . HOH JA 6 .   ? 98.624  68.910  -13.372 1.00 52.73 ? 397 HOH H O   1 
HETATM 12381 O  O   . HOH JA 6 .   ? 81.676  80.878  -22.047 1.00 48.29 ? 398 HOH H O   1 
HETATM 12382 O  O   . HOH JA 6 .   ? 82.388  79.086  -23.976 1.00 47.39 ? 399 HOH H O   1 
HETATM 12383 O  O   . HOH JA 6 .   ? 96.186  83.243  -17.989 1.00 48.39 ? 400 HOH H O   1 
HETATM 12384 O  O   . HOH JA 6 .   ? 86.607  82.675  -23.670 1.00 46.40 ? 401 HOH H O   1 
HETATM 12385 O  O   . HOH JA 6 .   ? 102.987 71.391  -16.757 1.00 54.39 ? 402 HOH H O   1 
HETATM 12386 O  O   . HOH JA 6 .   ? 99.534  69.199  -10.947 1.00 42.59 ? 403 HOH H O   1 
HETATM 12387 O  O   . HOH JA 6 .   ? 75.632  69.515  -22.151 1.00 43.91 ? 404 HOH H O   1 
HETATM 12388 O  O   . HOH JA 6 .   ? 77.725  79.714  -19.746 1.00 45.75 ? 405 HOH H O   1 
HETATM 12389 O  O   . HOH JA 6 .   ? 94.106  82.445  -27.166 1.00 52.86 ? 406 HOH H O   1 
HETATM 12390 O  O   . HOH JA 6 .   ? 81.848  95.129  -6.148  1.00 53.62 ? 407 HOH H O   1 
HETATM 12391 O  O   . HOH JA 6 .   ? 101.698 51.577  -8.909  1.00 48.60 ? 408 HOH H O   1 
HETATM 12392 O  O   . HOH JA 6 .   ? 91.595  54.917  -12.384 1.00 47.52 ? 409 HOH H O   1 
HETATM 12393 O  O   . HOH JA 6 .   ? 79.010  94.878  -5.444  1.00 55.68 ? 410 HOH H O   1 
HETATM 12394 O  O   . HOH JA 6 .   ? 90.675  70.573  3.094   1.00 46.47 ? 411 HOH H O   1 
HETATM 12395 O  O   . HOH JA 6 .   ? 93.795  72.514  -26.715 1.00 51.99 ? 412 HOH H O   1 
HETATM 12396 O  O   . HOH JA 6 .   ? 76.129  80.635  1.353   1.00 46.27 ? 413 HOH H O   1 
HETATM 12397 O  O   . HOH JA 6 .   ? 96.504  54.269  -4.238  1.00 52.87 ? 414 HOH H O   1 
HETATM 12398 O  O   . HOH JA 6 .   ? 98.960  78.519  0.791   1.00 54.89 ? 415 HOH H O   1 
HETATM 12399 O  O   . HOH JA 6 .   ? 81.775  68.885  -7.831  1.00 41.48 ? 416 HOH H O   1 
HETATM 12400 O  O   . HOH JA 6 .   ? 90.217  68.319  -30.232 1.00 50.36 ? 417 HOH H O   1 
HETATM 12401 O  O   . HOH JA 6 .   ? 80.446  75.341  -29.268 1.00 42.76 ? 418 HOH H O   1 
HETATM 12402 O  O   . HOH JA 6 .   ? 79.566  77.148  -26.942 1.00 43.40 ? 419 HOH H O   1 
HETATM 12403 O  O   . HOH JA 6 .   ? 88.728  58.162  -19.298 1.00 42.82 ? 420 HOH H O   1 
HETATM 12404 O  O   . HOH JA 6 .   ? 92.783  70.509  -27.594 1.00 47.38 ? 421 HOH H O   1 
HETATM 12405 O  O   . HOH JA 6 .   ? 77.941  93.296  0.670   1.00 55.35 ? 422 HOH H O   1 
HETATM 12406 O  O   . HOH KA 6 .   ? 61.735  51.754  -67.808 1.00 46.26 ? 301 HOH I O   1 
HETATM 12407 O  O   . HOH KA 6 .   ? 63.701  54.851  -44.176 1.00 48.17 ? 302 HOH I O   1 
HETATM 12408 O  O   . HOH KA 6 .   ? 52.260  81.332  -58.044 1.00 45.44 ? 303 HOH I O   1 
HETATM 12409 O  O   . HOH KA 6 .   ? 48.987  61.529  -70.280 1.00 47.50 ? 304 HOH I O   1 
HETATM 12410 O  O   . HOH KA 6 .   ? 65.557  67.292  -43.239 1.00 44.32 ? 305 HOH I O   1 
HETATM 12411 O  O   . HOH KA 6 .   ? 47.061  58.950  -42.859 1.00 39.75 ? 306 HOH I O   1 
HETATM 12412 O  O   . HOH KA 6 .   ? 53.016  75.655  -40.430 1.00 39.77 ? 307 HOH I O   1 
HETATM 12413 O  O   . HOH KA 6 .   ? 44.042  69.542  -48.834 1.00 39.83 ? 308 HOH I O   1 
HETATM 12414 O  O   . HOH KA 6 .   ? 38.963  55.114  -45.714 1.00 48.96 ? 309 HOH I O   1 
HETATM 12415 O  O   . HOH KA 6 .   ? 60.391  68.615  -68.417 1.00 53.85 ? 310 HOH I O   1 
HETATM 12416 O  O   . HOH KA 6 .   ? 57.869  69.269  -40.145 1.00 31.69 ? 311 HOH I O   1 
HETATM 12417 O  O   . HOH KA 6 .   ? 44.398  81.186  -64.259 1.00 62.49 ? 312 HOH I O   1 
HETATM 12418 O  O   . HOH KA 6 .   ? 49.021  70.706  -41.950 1.00 31.57 ? 313 HOH I O   1 
HETATM 12419 O  O   . HOH KA 6 .   ? 44.672  67.149  -47.200 1.00 42.16 ? 314 HOH I O   1 
HETATM 12420 O  O   . HOH KA 6 .   ? 65.734  58.426  -47.590 1.00 39.79 ? 315 HOH I O   1 
HETATM 12421 O  O   . HOH KA 6 .   ? 69.812  59.092  -54.221 1.00 36.62 ? 316 HOH I O   1 
HETATM 12422 O  O   . HOH KA 6 .   ? 62.156  81.311  -46.151 1.00 35.53 ? 317 HOH I O   1 
HETATM 12423 O  O   . HOH KA 6 .   ? 50.707  64.979  -41.088 1.00 41.38 ? 318 HOH I O   1 
HETATM 12424 O  O   . HOH KA 6 .   ? 60.652  65.367  -66.920 1.00 55.51 ? 319 HOH I O   1 
HETATM 12425 O  O   . HOH KA 6 .   ? 43.661  70.516  -53.072 1.00 23.69 ? 320 HOH I O   1 
HETATM 12426 O  O   . HOH KA 6 .   ? 42.753  54.075  -51.063 1.00 42.75 ? 321 HOH I O   1 
HETATM 12427 O  O   . HOH KA 6 .   ? 53.378  65.925  -70.127 1.00 41.85 ? 322 HOH I O   1 
HETATM 12428 O  O   . HOH KA 6 .   ? 39.389  62.390  -51.109 1.00 27.11 ? 323 HOH I O   1 
HETATM 12429 O  O   . HOH KA 6 .   ? 62.307  61.910  -39.300 1.00 46.68 ? 324 HOH I O   1 
HETATM 12430 O  O   . HOH KA 6 .   ? 62.571  67.232  -57.806 1.00 26.85 ? 325 HOH I O   1 
HETATM 12431 O  O   . HOH KA 6 .   ? 60.640  65.508  -41.627 1.00 29.88 ? 326 HOH I O   1 
HETATM 12432 O  O   . HOH KA 6 .   ? 56.273  55.172  -65.698 1.00 37.94 ? 327 HOH I O   1 
HETATM 12433 O  O   . HOH KA 6 .   ? 68.555  54.815  -49.271 1.00 28.28 ? 328 HOH I O   1 
HETATM 12434 O  O   . HOH KA 6 .   ? 40.271  63.318  -44.020 1.00 43.13 ? 329 HOH I O   1 
HETATM 12435 O  O   . HOH KA 6 .   ? 72.801  55.135  -53.793 1.00 45.40 ? 330 HOH I O   1 
HETATM 12436 O  O   . HOH KA 6 .   ? 61.012  60.552  -57.377 1.00 22.10 ? 331 HOH I O   1 
HETATM 12437 O  O   . HOH KA 6 .   ? 68.319  50.681  -55.835 1.00 29.05 ? 332 HOH I O   1 
HETATM 12438 O  O   . HOH KA 6 .   ? 65.574  65.461  -44.984 1.00 47.52 ? 333 HOH I O   1 
HETATM 12439 O  O   . HOH KA 6 .   ? 61.392  66.630  -63.628 1.00 41.19 ? 334 HOH I O   1 
HETATM 12440 O  O   . HOH KA 6 .   ? 63.308  79.063  -49.761 1.00 36.80 ? 335 HOH I O   1 
HETATM 12441 O  O   . HOH KA 6 .   ? 59.448  68.117  -42.026 1.00 25.75 ? 336 HOH I O   1 
HETATM 12442 O  O   . HOH KA 6 .   ? 62.554  70.213  -62.624 1.00 34.87 ? 337 HOH I O   1 
HETATM 12443 O  O   . HOH KA 6 .   ? 57.556  50.166  -57.570 1.00 38.19 ? 338 HOH I O   1 
HETATM 12444 O  O   . HOH KA 6 .   ? 37.030  55.505  -50.514 1.00 48.23 ? 339 HOH I O   1 
HETATM 12445 O  O   . HOH KA 6 .   ? 40.389  66.668  -46.753 1.00 43.86 ? 340 HOH I O   1 
HETATM 12446 O  O   . HOH KA 6 .   ? 65.294  41.327  -49.749 1.00 37.69 ? 341 HOH I O   1 
HETATM 12447 O  O   . HOH KA 6 .   ? 48.965  53.764  -47.873 1.00 39.83 ? 342 HOH I O   1 
HETATM 12448 O  O   . HOH KA 6 .   ? 72.939  52.684  -55.802 1.00 44.08 ? 343 HOH I O   1 
HETATM 12449 O  O   . HOH KA 6 .   ? 64.188  51.510  -57.926 1.00 29.69 ? 344 HOH I O   1 
HETATM 12450 O  O   . HOH KA 6 .   ? 67.219  69.259  -41.028 1.00 42.88 ? 345 HOH I O   1 
HETATM 12451 O  O   . HOH KA 6 .   ? 56.373  50.488  -49.078 1.00 49.52 ? 346 HOH I O   1 
HETATM 12452 O  O   . HOH KA 6 .   ? 64.596  53.423  -61.315 1.00 41.04 ? 347 HOH I O   1 
HETATM 12453 O  O   . HOH KA 6 .   ? 70.691  58.297  -62.499 1.00 52.55 ? 348 HOH I O   1 
HETATM 12454 O  O   . HOH KA 6 .   ? 47.246  79.333  -56.315 1.00 38.77 ? 349 HOH I O   1 
HETATM 12455 O  O   . HOH KA 6 .   ? 44.907  61.444  -49.306 1.00 36.39 ? 350 HOH I O   1 
HETATM 12456 O  O   . HOH KA 6 .   ? 58.319  78.619  -56.074 1.00 38.17 ? 351 HOH I O   1 
HETATM 12457 O  O   . HOH KA 6 .   ? 57.126  56.519  -48.253 1.00 33.58 ? 352 HOH I O   1 
HETATM 12458 O  O   . HOH KA 6 .   ? 45.286  59.245  -64.978 1.00 44.89 ? 353 HOH I O   1 
HETATM 12459 O  O   . HOH KA 6 .   ? 57.560  57.928  -50.963 1.00 29.85 ? 354 HOH I O   1 
HETATM 12460 O  O   . HOH KA 6 .   ? 42.809  74.704  -66.571 1.00 44.55 ? 355 HOH I O   1 
HETATM 12461 O  O   . HOH KA 6 .   ? 65.049  51.336  -45.501 1.00 38.60 ? 356 HOH I O   1 
HETATM 12462 O  O   . HOH KA 6 .   ? 58.222  77.113  -42.118 1.00 28.41 ? 357 HOH I O   1 
HETATM 12463 O  O   . HOH KA 6 .   ? 64.792  72.478  -39.775 1.00 37.73 ? 358 HOH I O   1 
HETATM 12464 O  O   . HOH KA 6 .   ? 49.004  53.775  -60.293 1.00 37.81 ? 359 HOH I O   1 
HETATM 12465 O  O   . HOH KA 6 .   ? 42.475  67.946  -50.974 1.00 33.75 ? 360 HOH I O   1 
HETATM 12466 O  O   . HOH KA 6 .   ? 51.986  68.091  -41.092 1.00 34.90 ? 361 HOH I O   1 
HETATM 12467 O  O   . HOH KA 6 .   ? 54.181  54.578  -64.172 1.00 30.92 ? 362 HOH I O   1 
HETATM 12468 O  O   . HOH KA 6 .   ? 63.220  76.448  -50.595 1.00 27.17 ? 363 HOH I O   1 
HETATM 12469 O  O   . HOH KA 6 .   ? 68.243  73.790  -47.454 1.00 38.80 ? 364 HOH I O   1 
HETATM 12470 O  O   . HOH KA 6 .   ? 46.979  50.313  -55.932 1.00 43.99 ? 365 HOH I O   1 
HETATM 12471 O  O   . HOH KA 6 .   ? 47.314  76.752  -60.148 1.00 43.93 ? 366 HOH I O   1 
HETATM 12472 O  O   . HOH KA 6 .   ? 66.267  62.624  -45.333 1.00 38.09 ? 367 HOH I O   1 
HETATM 12473 O  O   . HOH KA 6 .   ? 51.619  78.079  -49.729 1.00 42.92 ? 368 HOH I O   1 
HETATM 12474 O  O   . HOH KA 6 .   ? 59.842  58.196  -38.359 1.00 47.39 ? 369 HOH I O   1 
HETATM 12475 O  O   . HOH KA 6 .   ? 59.973  48.501  -65.992 1.00 55.06 ? 370 HOH I O   1 
HETATM 12476 O  O   . HOH KA 6 .   ? 54.775  53.493  -54.323 1.00 28.26 ? 371 HOH I O   1 
HETATM 12477 O  O   . HOH KA 6 .   ? 52.432  58.368  -43.311 1.00 34.19 ? 372 HOH I O   1 
HETATM 12478 O  O   . HOH KA 6 .   ? 43.934  54.639  -60.602 1.00 42.64 ? 373 HOH I O   1 
HETATM 12479 O  O   . HOH KA 6 .   ? 57.701  72.670  -38.355 1.00 37.89 ? 374 HOH I O   1 
HETATM 12480 O  O   . HOH KA 6 .   ? 59.645  54.901  -47.099 1.00 34.14 ? 375 HOH I O   1 
HETATM 12481 O  O   . HOH KA 6 .   ? 53.691  61.757  -40.589 1.00 48.41 ? 376 HOH I O   1 
HETATM 12482 O  O   . HOH KA 6 .   ? 49.070  77.333  -62.764 1.00 73.82 ? 377 HOH I O   1 
HETATM 12483 O  O   . HOH KA 6 .   ? 59.874  47.203  -63.759 1.00 55.49 ? 378 HOH I O   1 
HETATM 12484 O  O   . HOH KA 6 .   ? 68.689  66.809  -46.696 1.00 35.51 ? 379 HOH I O   1 
HETATM 12485 O  O   . HOH KA 6 .   ? 46.297  69.626  -38.423 1.00 52.85 ? 380 HOH I O   1 
HETATM 12486 O  O   . HOH KA 6 .   ? 44.204  63.180  -50.455 1.00 41.95 ? 381 HOH I O   1 
HETATM 12487 O  O   . HOH KA 6 .   ? 49.564  63.393  -42.522 1.00 44.58 ? 382 HOH I O   1 
HETATM 12488 O  O   . HOH KA 6 .   ? 63.662  47.487  -47.752 1.00 29.71 ? 383 HOH I O   1 
HETATM 12489 O  O   . HOH KA 6 .   ? 53.943  74.459  -69.101 1.00 47.03 ? 384 HOH I O   1 
HETATM 12490 O  O   . HOH KA 6 .   ? 66.513  54.328  -64.931 1.00 46.57 ? 385 HOH I O   1 
HETATM 12491 O  O   . HOH KA 6 .   ? 68.562  78.175  -45.933 1.00 39.36 ? 386 HOH I O   1 
HETATM 12492 O  O   . HOH KA 6 .   ? 66.379  62.299  -61.154 1.00 27.12 ? 387 HOH I O   1 
HETATM 12493 O  O   . HOH KA 6 .   ? 64.629  45.299  -57.696 1.00 41.25 ? 388 HOH I O   1 
HETATM 12494 O  O   . HOH KA 6 .   ? 63.106  80.760  -53.353 1.00 51.38 ? 389 HOH I O   1 
HETATM 12495 O  O   A HOH KA 6 .   ? 53.794  55.804  -46.489 0.50 34.33 ? 390 HOH I O   1 
HETATM 12496 O  O   B HOH KA 6 .   ? 53.414  56.068  -45.019 0.50 38.49 ? 390 HOH I O   1 
HETATM 12497 O  O   . HOH KA 6 .   ? 57.412  79.943  -54.181 1.00 52.65 ? 391 HOH I O   1 
HETATM 12498 O  O   . HOH KA 6 .   ? 50.771  80.100  -54.718 1.00 37.59 ? 392 HOH I O   1 
HETATM 12499 O  O   . HOH KA 6 .   ? 68.832  61.421  -51.876 1.00 43.13 ? 393 HOH I O   1 
HETATM 12500 O  O   . HOH KA 6 .   ? 52.265  78.996  -53.137 1.00 36.00 ? 394 HOH I O   1 
HETATM 12501 O  O   . HOH KA 6 .   ? 58.671  75.656  -62.277 1.00 45.12 ? 395 HOH I O   1 
HETATM 12502 O  O   . HOH KA 6 .   ? 61.223  59.618  -68.119 1.00 53.08 ? 396 HOH I O   1 
HETATM 12503 O  O   . HOH KA 6 .   ? 58.838  74.461  -64.906 1.00 71.41 ? 397 HOH I O   1 
HETATM 12504 O  O   . HOH KA 6 .   ? 50.291  52.776  -50.339 1.00 42.66 ? 398 HOH I O   1 
HETATM 12505 O  O   . HOH KA 6 .   ? 43.258  65.700  -49.227 1.00 44.53 ? 399 HOH I O   1 
HETATM 12506 O  O   . HOH KA 6 .   ? 49.169  71.869  -77.700 1.00 56.25 ? 400 HOH I O   1 
HETATM 12507 O  O   . HOH KA 6 .   ? 48.935  50.192  -62.000 1.00 53.55 ? 401 HOH I O   1 
HETATM 12508 O  O   . HOH KA 6 .   ? 47.925  75.969  -47.396 1.00 44.41 ? 402 HOH I O   1 
HETATM 12509 O  O   . HOH KA 6 .   ? 52.947  52.749  -49.937 1.00 44.47 ? 403 HOH I O   1 
HETATM 12510 O  O   . HOH KA 6 .   ? 74.380  59.278  -59.829 1.00 51.14 ? 404 HOH I O   1 
HETATM 12511 O  O   . HOH KA 6 .   ? 59.861  46.941  -48.762 1.00 51.64 ? 405 HOH I O   1 
HETATM 12512 O  O   . HOH KA 6 .   ? 67.592  68.137  -62.619 1.00 49.29 ? 406 HOH I O   1 
HETATM 12513 O  O   . HOH KA 6 .   ? 63.809  48.834  -45.341 1.00 35.26 ? 407 HOH I O   1 
HETATM 12514 O  O   . HOH KA 6 .   ? 39.114  75.448  -65.808 1.00 57.47 ? 408 HOH I O   1 
HETATM 12515 O  O   . HOH KA 6 .   ? 47.346  53.147  -62.101 1.00 45.57 ? 409 HOH I O   1 
HETATM 12516 O  O   . HOH KA 6 .   ? 55.176  69.362  -76.199 1.00 51.27 ? 410 HOH I O   1 
HETATM 12517 O  O   . HOH KA 6 .   ? 57.677  61.597  -71.369 1.00 53.58 ? 411 HOH I O   1 
HETATM 12518 O  O   . HOH KA 6 .   ? 55.868  77.082  -40.215 1.00 51.77 ? 412 HOH I O   1 
HETATM 12519 O  O   . HOH KA 6 .   ? 40.900  61.766  -63.942 1.00 55.80 ? 413 HOH I O   1 
HETATM 12520 O  O   . HOH KA 6 .   ? 53.997  54.706  -51.711 1.00 38.64 ? 414 HOH I O   1 
HETATM 12521 O  O   . HOH KA 6 .   ? 51.020  54.094  -46.132 1.00 54.93 ? 415 HOH I O   1 
HETATM 12522 O  O   . HOH KA 6 .   ? 44.525  65.621  -43.967 1.00 53.21 ? 416 HOH I O   1 
HETATM 12523 O  O   . HOH KA 6 .   ? 49.873  77.324  -46.970 1.00 54.95 ? 417 HOH I O   1 
HETATM 12524 O  O   . HOH KA 6 .   ? 53.782  53.665  -47.325 1.00 58.62 ? 418 HOH I O   1 
HETATM 12525 O  O   . HOH KA 6 .   ? 42.350  74.872  -69.880 1.00 55.40 ? 419 HOH I O   1 
HETATM 12526 O  O   . HOH KA 6 .   ? 68.039  59.261  -49.408 1.00 38.88 ? 420 HOH I O   1 
HETATM 12527 O  O   . HOH KA 6 .   ? 42.314  70.501  -50.850 1.00 42.97 ? 421 HOH I O   1 
HETATM 12528 O  O   . HOH KA 6 .   ? 49.247  50.521  -51.347 1.00 58.36 ? 422 HOH I O   1 
HETATM 12529 O  O   . HOH KA 6 .   ? 72.238  53.480  -57.894 1.00 37.76 ? 423 HOH I O   1 
HETATM 12530 O  O   . HOH KA 6 .   ? 41.597  54.272  -46.624 1.00 48.41 ? 424 HOH I O   1 
HETATM 12531 O  O   . HOH KA 6 .   ? 53.913  82.026  -50.062 1.00 46.13 ? 425 HOH I O   1 
HETATM 12532 O  O   . HOH KA 6 .   ? 47.727  78.297  -39.273 1.00 62.79 ? 426 HOH I O   1 
HETATM 12533 O  O   . HOH KA 6 .   ? 45.856  54.327  -64.667 1.00 55.82 ? 427 HOH I O   1 
HETATM 12534 O  O   . HOH KA 6 .   ? 67.410  55.957  -47.011 1.00 36.74 ? 428 HOH I O   1 
HETATM 12535 O  O   . HOH KA 6 .   ? 52.803  64.296  -39.323 1.00 54.68 ? 429 HOH I O   1 
HETATM 12536 O  O   . HOH KA 6 .   ? 53.592  69.516  -34.813 1.00 40.28 ? 430 HOH I O   1 
HETATM 12537 O  O   . HOH KA 6 .   ? 54.934  67.332  -39.415 1.00 39.66 ? 431 HOH I O   1 
HETATM 12538 O  O   . HOH KA 6 .   ? 65.814  68.347  -39.004 1.00 46.52 ? 432 HOH I O   1 
HETATM 12539 O  O   . HOH KA 6 .   ? 65.644  52.740  -43.555 1.00 49.28 ? 433 HOH I O   1 
HETATM 12540 O  O   . HOH KA 6 .   ? 70.397  50.200  -57.387 1.00 40.94 ? 434 HOH I O   1 
HETATM 12541 O  O   . HOH KA 6 .   ? 71.325  57.882  -52.059 1.00 47.28 ? 435 HOH I O   1 
HETATM 12542 O  O   . HOH KA 6 .   ? 56.758  57.189  -67.775 1.00 48.28 ? 436 HOH I O   1 
HETATM 12543 O  O   . HOH KA 6 .   ? 58.519  64.154  -38.753 1.00 51.67 ? 437 HOH I O   1 
HETATM 12544 O  O   . HOH KA 6 .   ? 70.024  57.327  -49.396 1.00 40.36 ? 438 HOH I O   1 
HETATM 12545 O  O   . HOH KA 6 .   ? 57.051  80.173  -42.965 1.00 38.64 ? 439 HOH I O   1 
HETATM 12546 O  O   . HOH KA 6 .   ? 56.486  75.105  -37.899 1.00 41.67 ? 440 HOH I O   1 
HETATM 12547 O  O   . HOH KA 6 .   ? 55.838  68.433  -36.211 1.00 50.99 ? 441 HOH I O   1 
HETATM 12548 O  O   . HOH KA 6 .   ? 54.064  53.125  -73.136 1.00 52.53 ? 442 HOH I O   1 
HETATM 12549 O  O   . HOH LA 6 .   ? 30.035  53.501  -48.770 1.00 59.81 ? 201 HOH J O   1 
HETATM 12550 O  O   . HOH LA 6 .   ? 19.319  62.711  -43.718 1.00 59.88 ? 202 HOH J O   1 
HETATM 12551 O  O   . HOH LA 6 .   ? 25.854  72.279  -66.373 1.00 51.16 ? 203 HOH J O   1 
HETATM 12552 O  O   . HOH LA 6 .   ? 21.418  60.858  -36.808 1.00 49.22 ? 204 HOH J O   1 
HETATM 12553 O  O   . HOH LA 6 .   ? 42.117  80.526  -56.691 1.00 44.28 ? 205 HOH J O   1 
HETATM 12554 O  O   . HOH LA 6 .   ? 38.508  68.158  -48.073 1.00 32.42 ? 206 HOH J O   1 
HETATM 12555 O  O   . HOH LA 6 .   ? 24.473  77.562  -54.862 1.00 53.14 ? 207 HOH J O   1 
HETATM 12556 O  O   . HOH LA 6 .   ? 38.280  79.913  -58.570 1.00 51.08 ? 208 HOH J O   1 
HETATM 12557 O  O   . HOH LA 6 .   ? 17.254  77.091  -46.424 1.00 48.57 ? 209 HOH J O   1 
HETATM 12558 O  O   . HOH LA 6 .   ? 34.442  67.756  -66.939 1.00 49.18 ? 210 HOH J O   1 
HETATM 12559 O  O   . HOH LA 6 .   ? 36.004  80.727  -48.725 1.00 44.03 ? 211 HOH J O   1 
HETATM 12560 O  O   . HOH LA 6 .   ? 15.305  66.855  -41.335 1.00 43.08 ? 212 HOH J O   1 
HETATM 12561 O  O   . HOH LA 6 .   ? 17.143  65.286  -49.282 1.00 45.99 ? 213 HOH J O   1 
HETATM 12562 O  O   . HOH LA 6 .   ? 34.722  71.275  -41.347 1.00 25.99 ? 214 HOH J O   1 
HETATM 12563 O  O   . HOH LA 6 .   ? 40.449  54.627  -52.686 1.00 40.93 ? 215 HOH J O   1 
HETATM 12564 O  O   . HOH LA 6 .   ? 26.391  73.936  -39.949 1.00 33.54 ? 216 HOH J O   1 
HETATM 12565 O  O   . HOH LA 6 .   ? 38.379  65.017  -51.158 1.00 23.44 ? 217 HOH J O   1 
HETATM 12566 O  O   . HOH LA 6 .   ? 30.222  63.090  -69.576 1.00 46.19 ? 218 HOH J O   1 
HETATM 12567 O  O   . HOH LA 6 .   ? 37.985  71.494  -48.061 1.00 36.77 ? 219 HOH J O   1 
HETATM 12568 O  O   . HOH LA 6 .   ? 35.086  56.283  -48.658 1.00 43.00 ? 220 HOH J O   1 
HETATM 12569 O  O   . HOH LA 6 .   ? 41.008  78.382  -59.882 1.00 37.53 ? 221 HOH J O   1 
HETATM 12570 O  O   . HOH LA 6 .   ? 22.622  76.062  -41.841 1.00 49.04 ? 222 HOH J O   1 
HETATM 12571 O  O   . HOH LA 6 .   ? 30.655  80.928  -48.587 1.00 47.40 ? 223 HOH J O   1 
HETATM 12572 O  O   . HOH LA 6 .   ? 31.213  63.389  -72.988 1.00 47.06 ? 224 HOH J O   1 
HETATM 12573 O  O   . HOH LA 6 .   ? 20.128  64.049  -47.812 1.00 42.33 ? 225 HOH J O   1 
HETATM 12574 O  O   . HOH LA 6 .   ? 25.953  66.251  -36.475 1.00 37.23 ? 226 HOH J O   1 
HETATM 12575 O  O   . HOH LA 6 .   ? 30.343  58.365  -45.911 1.00 49.36 ? 227 HOH J O   1 
HETATM 12576 O  O   . HOH LA 6 .   ? 39.659  68.133  -51.030 1.00 31.68 ? 228 HOH J O   1 
HETATM 12577 O  O   . HOH LA 6 .   ? 42.649  72.811  -54.406 1.00 28.20 ? 229 HOH J O   1 
HETATM 12578 O  O   . HOH LA 6 .   ? 19.842  71.814  -36.049 1.00 35.89 ? 230 HOH J O   1 
HETATM 12579 O  O   . HOH LA 6 .   ? 17.083  67.173  -53.889 1.00 52.26 ? 231 HOH J O   1 
HETATM 12580 O  O   . HOH LA 6 .   ? 34.321  55.926  -53.098 1.00 41.60 ? 232 HOH J O   1 
HETATM 12581 O  O   . HOH LA 6 .   ? 19.892  64.649  -52.453 1.00 48.75 ? 233 HOH J O   1 
HETATM 12582 O  O   . HOH LA 6 .   ? 22.463  70.679  -35.621 1.00 42.80 ? 234 HOH J O   1 
HETATM 12583 O  O   . HOH LA 6 .   ? 28.083  61.852  -40.575 1.00 45.46 ? 235 HOH J O   1 
HETATM 12584 O  O   . HOH LA 6 .   ? 20.256  61.401  -41.612 1.00 53.86 ? 236 HOH J O   1 
HETATM 12585 O  O   . HOH LA 6 .   ? 36.007  77.371  -46.836 1.00 49.40 ? 237 HOH J O   1 
HETATM 12586 O  O   . HOH LA 6 .   ? 26.711  52.884  -60.975 1.00 59.58 ? 238 HOH J O   1 
HETATM 12587 O  O   . HOH LA 6 .   ? 38.077  78.452  -45.740 1.00 51.01 ? 239 HOH J O   1 
HETATM 12588 O  O   . HOH LA 6 .   ? 31.806  64.046  -34.757 1.00 39.54 ? 240 HOH J O   1 
HETATM 12589 O  O   . HOH LA 6 .   ? 31.254  67.642  -36.916 1.00 43.02 ? 241 HOH J O   1 
HETATM 12590 O  O   . HOH LA 6 .   ? 15.333  63.897  -37.295 1.00 43.34 ? 242 HOH J O   1 
HETATM 12591 O  O   . HOH LA 6 .   ? 36.733  74.218  -66.116 1.00 51.86 ? 243 HOH J O   1 
HETATM 12592 O  O   . HOH LA 6 .   ? 24.230  74.092  -41.353 1.00 38.02 ? 244 HOH J O   1 
HETATM 12593 O  O   . HOH LA 6 .   ? 13.223  71.772  -35.192 1.00 55.61 ? 245 HOH J O   1 
HETATM 12594 O  O   . HOH LA 6 .   ? 27.879  80.366  -52.806 1.00 54.11 ? 246 HOH J O   1 
HETATM 12595 O  O   . HOH LA 6 .   ? 18.151  59.324  -56.592 1.00 49.10 ? 247 HOH J O   1 
HETATM 12596 O  O   . HOH LA 6 .   ? 26.680  79.178  -59.744 1.00 47.77 ? 248 HOH J O   1 
HETATM 12597 O  O   . HOH LA 6 .   ? 37.106  74.662  -52.851 1.00 41.60 ? 249 HOH J O   1 
HETATM 12598 O  O   . HOH LA 6 .   ? 26.751  53.309  -64.480 1.00 46.69 ? 250 HOH J O   1 
HETATM 12599 O  O   . HOH LA 6 .   ? 31.556  74.068  -41.606 1.00 30.84 ? 251 HOH J O   1 
HETATM 12600 O  O   . HOH LA 6 .   ? 27.107  77.932  -63.468 1.00 50.94 ? 252 HOH J O   1 
HETATM 12601 O  O   . HOH LA 6 .   ? 36.049  65.872  -42.999 1.00 51.15 ? 253 HOH J O   1 
HETATM 12602 O  O   . HOH LA 6 .   ? 38.049  54.454  -60.380 1.00 44.72 ? 254 HOH J O   1 
HETATM 12603 O  O   . HOH LA 6 .   ? 17.310  74.378  -38.245 1.00 48.94 ? 255 HOH J O   1 
HETATM 12604 O  O   . HOH LA 6 .   ? 14.686  73.154  -44.468 1.00 41.26 ? 256 HOH J O   1 
HETATM 12605 O  O   . HOH LA 6 .   ? 33.607  76.981  -45.212 1.00 49.46 ? 257 HOH J O   1 
HETATM 12606 O  O   . HOH LA 6 .   ? 37.134  60.674  -69.525 1.00 56.82 ? 258 HOH J O   1 
HETATM 12607 O  O   . HOH LA 6 .   ? 19.615  62.604  -62.791 1.00 52.58 ? 259 HOH J O   1 
HETATM 12608 O  O   . HOH LA 6 .   ? 31.004  81.524  -57.942 1.00 47.87 ? 260 HOH J O   1 
HETATM 12609 O  O   . HOH LA 6 .   ? 18.252  62.823  -59.171 1.00 50.94 ? 261 HOH J O   1 
HETATM 12610 O  O   . HOH LA 6 .   ? 37.685  74.583  -47.145 1.00 47.50 ? 262 HOH J O   1 
HETATM 12611 O  O   . HOH LA 6 .   ? 30.885  60.383  -43.377 1.00 49.68 ? 263 HOH J O   1 
HETATM 12612 O  O   . HOH LA 6 .   ? 27.066  79.257  -55.366 1.00 51.41 ? 264 HOH J O   1 
HETATM 12613 O  O   . HOH LA 6 .   ? 38.004  72.493  -52.862 1.00 46.03 ? 265 HOH J O   1 
HETATM 12614 O  O   . HOH LA 6 .   ? 31.276  82.272  -53.484 1.00 45.17 ? 266 HOH J O   1 
HETATM 12615 O  O   . HOH LA 6 .   ? 30.486  62.496  -41.711 1.00 50.83 ? 267 HOH J O   1 
HETATM 12616 O  O   . HOH LA 6 .   ? 35.224  63.725  -43.137 1.00 43.78 ? 268 HOH J O   1 
HETATM 12617 O  O   . HOH LA 6 .   ? 38.048  81.795  -41.988 1.00 51.78 ? 269 HOH J O   1 
HETATM 12618 O  O   . HOH LA 6 .   ? 39.025  70.935  -50.723 1.00 42.04 ? 270 HOH J O   1 
HETATM 12619 O  O   . HOH LA 6 .   ? 21.962  75.813  -52.490 1.00 70.93 ? 271 HOH J O   1 
HETATM 12620 O  O   . HOH LA 6 .   ? 20.457  62.687  -50.360 1.00 45.66 ? 272 HOH J O   1 
HETATM 12621 O  O   . HOH LA 6 .   ? 27.957  57.128  -44.534 1.00 52.31 ? 273 HOH J O   1 
HETATM 12622 O  O   . HOH LA 6 .   ? 23.527  61.055  -35.195 1.00 50.33 ? 274 HOH J O   1 
HETATM 12623 O  O   . HOH LA 6 .   ? 41.855  69.000  -44.943 1.00 51.68 ? 275 HOH J O   1 
HETATM 12624 O  O   . HOH LA 6 .   ? 11.951  76.040  -59.103 1.00 61.36 ? 276 HOH J O   1 
HETATM 12625 O  O   . HOH LA 6 .   ? 37.855  64.442  -65.922 1.00 61.98 ? 277 HOH J O   1 
HETATM 12626 O  O   . HOH LA 6 .   ? 27.101  64.176  -35.489 1.00 39.95 ? 278 HOH J O   1 
HETATM 12627 O  O   . HOH LA 6 .   ? 38.117  63.138  -68.208 1.00 58.01 ? 279 HOH J O   1 
HETATM 12628 O  O   . HOH LA 6 .   ? 29.088  75.813  -40.191 1.00 42.32 ? 280 HOH J O   1 
HETATM 12629 O  O   . HOH LA 6 .   ? 38.713  82.577  -56.301 1.00 51.16 ? 281 HOH J O   1 
HETATM 12630 O  O   . HOH LA 6 .   ? 34.530  56.067  -46.020 1.00 53.67 ? 282 HOH J O   1 
HETATM 12631 O  O   . HOH LA 6 .   ? 27.701  61.941  -37.180 1.00 48.27 ? 283 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   -26 ?   ?   ?   A . n 
A 1 2   LYS 2   -25 ?   ?   ?   A . n 
A 1 3   HIS 3   -24 ?   ?   ?   A . n 
A 1 4   HIS 4   -23 ?   ?   ?   A . n 
A 1 5   HIS 5   -22 ?   ?   ?   A . n 
A 1 6   HIS 6   -21 ?   ?   ?   A . n 
A 1 7   HIS 7   -20 ?   ?   ?   A . n 
A 1 8   HIS 8   -19 ?   ?   ?   A . n 
A 1 9   PRO 9   -18 ?   ?   ?   A . n 
A 1 10  MET 10  -17 ?   ?   ?   A . n 
A 1 11  SER 11  -16 ?   ?   ?   A . n 
A 1 12  ASP 12  -15 ?   ?   ?   A . n 
A 1 13  TYR 13  -14 ?   ?   ?   A . n 
A 1 14  ASP 14  -13 ?   ?   ?   A . n 
A 1 15  ILE 15  -12 ?   ?   ?   A . n 
A 1 16  PRO 16  -11 ?   ?   ?   A . n 
A 1 17  THR 17  -10 ?   ?   ?   A . n 
A 1 18  THR 18  -9  ?   ?   ?   A . n 
A 1 19  GLU 19  -8  ?   ?   ?   A . n 
A 1 20  ASN 20  -7  ?   ?   ?   A . n 
A 1 21  LEU 21  -6  ?   ?   ?   A . n 
A 1 22  TYR 22  -5  ?   ?   ?   A . n 
A 1 23  PHE 23  -4  ?   ?   ?   A . n 
A 1 24  GLN 24  -3  ?   ?   ?   A . n 
A 1 25  GLY 25  -2  ?   ?   ?   A . n 
A 1 26  ALA 26  -1  -1  ALA ALA A . n 
A 1 27  MET 27  0   0   MET MET A . n 
A 1 28  ALA 28  1   1   ALA ALA A . n 
A 1 29  THR 29  2   2   THR THR A . n 
A 1 30  LYS 30  3   3   LYS LYS A . n 
A 1 31  ALA 31  4   4   ALA ALA A . n 
A 1 32  VAL 32  5   5   VAL VAL A . n 
A 1 33  CYS 33  6   6   CYS CYS A . n 
A 1 34  VAL 34  7   7   VAL VAL A . n 
A 1 35  LEU 35  8   8   LEU LEU A . n 
A 1 36  LYS 36  9   9   LYS LYS A . n 
A 1 37  GLY 37  10  10  GLY GLY A . n 
A 1 38  ASP 38  11  11  ASP ASP A . n 
A 1 39  GLY 39  12  12  GLY GLY A . n 
A 1 40  PRO 40  13  13  PRO PRO A . n 
A 1 41  VAL 41  14  14  VAL VAL A . n 
A 1 42  GLN 42  15  15  GLN GLN A . n 
A 1 43  GLY 43  16  16  GLY GLY A . n 
A 1 44  ILE 44  17  17  ILE ILE A . n 
A 1 45  ILE 45  18  18  ILE ILE A . n 
A 1 46  ASN 46  19  19  ASN ASN A . n 
A 1 47  PHE 47  20  20  PHE PHE A . n 
A 1 48  GLU 48  21  21  GLU GLU A . n 
A 1 49  GLN 49  22  22  GLN GLN A . n 
A 1 50  LYS 50  23  23  LYS LYS A . n 
A 1 51  GLU 51  24  24  GLU GLU A . n 
A 1 52  SER 52  25  25  SER SER A . n 
A 1 53  ASN 53  26  26  ASN ASN A . n 
A 1 54  GLY 54  27  27  GLY GLY A . n 
A 1 55  PRO 55  28  28  PRO PRO A . n 
A 1 56  VAL 56  29  29  VAL VAL A . n 
A 1 57  LYS 57  30  30  LYS LYS A . n 
A 1 58  VAL 58  31  31  VAL VAL A . n 
A 1 59  TRP 59  32  32  TRP TRP A . n 
A 1 60  GLY 60  33  33  GLY GLY A . n 
A 1 61  SER 61  34  34  SER SER A . n 
A 1 62  ILE 62  35  35  ILE ILE A . n 
A 1 63  LYS 63  36  36  LYS LYS A . n 
A 1 64  GLY 64  37  37  GLY GLY A . n 
A 1 65  LEU 65  38  38  LEU LEU A . n 
A 1 66  THR 66  39  39  THR THR A . n 
A 1 67  GLU 67  40  40  GLU GLU A . n 
A 1 68  GLY 68  41  41  GLY GLY A . n 
A 1 69  LEU 69  42  42  LEU LEU A . n 
A 1 70  HIS 70  43  43  HIS HIS A . n 
A 1 71  GLY 71  44  44  GLY GLY A . n 
A 1 72  PHE 72  45  45  PHE PHE A . n 
A 1 73  HIS 73  46  46  HIS HIS A . n 
A 1 74  VAL 74  47  47  VAL VAL A . n 
A 1 75  HIS 75  48  48  HIS HIS A . n 
A 1 76  GLU 76  49  49  GLU GLU A . n 
A 1 77  PHE 77  50  50  PHE PHE A . n 
A 1 78  GLY 78  51  51  GLY GLY A . n 
A 1 79  ASP 79  52  52  ASP ASP A . n 
A 1 80  ASN 80  53  53  ASN ASN A . n 
A 1 81  THR 81  54  54  THR THR A . n 
A 1 82  ALA 82  55  55  ALA ALA A . n 
A 1 83  GLY 83  56  56  GLY GLY A . n 
A 1 84  CYS 84  57  57  CYS CYS A . n 
A 1 85  THR 85  58  58  THR THR A . n 
A 1 86  SER 86  59  59  SER SER A . n 
A 1 87  ALA 87  60  60  ALA ALA A . n 
A 1 88  GLY 88  61  61  GLY GLY A . n 
A 1 89  PRO 89  62  62  PRO PRO A . n 
A 1 90  HIS 90  63  63  HIS HIS A . n 
A 1 91  PHE 91  64  64  PHE PHE A . n 
A 1 92  ASN 92  65  65  ASN ASN A . n 
A 1 93  PRO 93  66  66  PRO PRO A . n 
A 1 94  LEU 94  67  67  LEU LEU A . n 
A 1 95  SER 95  68  68  SER SER A . n 
A 1 96  ARG 96  69  69  ARG ARG A . n 
A 1 97  LYS 97  70  70  LYS LYS A . n 
A 1 98  HIS 98  71  71  HIS HIS A . n 
A 1 99  GLY 99  72  72  GLY GLY A . n 
A 1 100 GLY 100 73  73  GLY GLY A . n 
A 1 101 PRO 101 74  74  PRO PRO A . n 
A 1 102 LYS 102 75  75  LYS LYS A . n 
A 1 103 ASP 103 76  76  ASP ASP A . n 
A 1 104 GLU 104 77  77  GLU GLU A . n 
A 1 105 GLU 105 78  78  GLU GLU A . n 
A 1 106 ARG 106 79  79  ARG ARG A . n 
A 1 107 HIS 107 80  80  HIS HIS A . n 
A 1 108 VAL 108 81  81  VAL VAL A . n 
A 1 109 GLY 109 82  82  GLY GLY A . n 
A 1 110 ASP 110 83  83  ASP ASP A . n 
A 1 111 LEU 111 84  84  LEU LEU A . n 
A 1 112 GLY 112 85  85  GLY GLY A . n 
A 1 113 ASN 113 86  86  ASN ASN A . n 
A 1 114 VAL 114 87  87  VAL VAL A . n 
A 1 115 THR 115 88  88  THR THR A . n 
A 1 116 ALA 116 89  89  ALA ALA A . n 
A 1 117 ASP 117 90  90  ASP ASP A . n 
A 1 118 LYS 118 91  91  LYS LYS A . n 
A 1 119 ASP 119 92  92  ASP ASP A . n 
A 1 120 GLY 120 93  93  GLY GLY A . n 
A 1 121 VAL 121 94  94  VAL VAL A . n 
A 1 122 ALA 122 95  95  ALA ALA A . n 
A 1 123 ASP 123 96  96  ASP ASP A . n 
A 1 124 VAL 124 97  97  VAL VAL A . n 
A 1 125 SER 125 98  98  SER SER A . n 
A 1 126 ILE 126 99  99  ILE ILE A . n 
A 1 127 GLU 127 100 100 GLU GLU A . n 
A 1 128 ASP 128 101 101 ASP ASP A . n 
A 1 129 SER 129 102 102 SER SER A . n 
A 1 130 VAL 130 103 103 VAL VAL A . n 
A 1 131 ILE 131 104 104 ILE ILE A . n 
A 1 132 SER 132 105 105 SER SER A . n 
A 1 133 LEU 133 106 106 LEU LEU A . n 
A 1 134 SER 134 107 107 SER SER A . n 
A 1 135 GLY 135 108 108 GLY GLY A . n 
A 1 136 ASP 136 109 109 ASP ASP A . n 
A 1 137 HIS 137 110 110 HIS HIS A . n 
A 1 138 CYS 138 111 111 CYS CYS A . n 
A 1 139 ILE 139 112 112 ILE ILE A . n 
A 1 140 ILE 140 113 113 ILE ILE A . n 
A 1 141 GLY 141 114 114 GLY GLY A . n 
A 1 142 ARG 142 115 115 ARG ARG A . n 
A 1 143 THR 143 116 116 THR THR A . n 
A 1 144 LEU 144 117 117 LEU LEU A . n 
A 1 145 VAL 145 118 118 VAL VAL A . n 
A 1 146 VAL 146 119 119 VAL VAL A . n 
A 1 147 HIS 147 120 120 HIS HIS A . n 
A 1 148 GLU 148 121 121 GLU GLU A . n 
A 1 149 LYS 149 122 122 LYS LYS A . n 
A 1 150 ALA 150 123 123 ALA ALA A . n 
A 1 151 ASP 151 124 124 ASP ASP A . n 
A 1 152 ASP 152 125 125 ASP ASP A . n 
A 1 153 LEU 153 126 126 LEU LEU A . n 
A 1 154 GLY 154 127 127 GLY GLY A . n 
A 1 155 LYS 155 128 128 LYS LYS A . n 
A 1 156 GLY 156 129 129 GLY GLY A . n 
A 1 157 GLY 157 130 130 GLY GLY A . n 
A 1 158 ASN 158 131 131 ASN ASN A . n 
A 1 159 GLU 159 132 132 GLU GLU A . n 
A 1 160 GLU 160 133 133 GLU GLU A . n 
A 1 161 SER 161 134 134 SER SER A . n 
A 1 162 THR 162 135 135 THR THR A . n 
A 1 163 LYS 163 136 136 LYS LYS A . n 
A 1 164 THR 164 137 137 THR THR A . n 
A 1 165 GLY 165 138 138 GLY GLY A . n 
A 1 166 ASN 166 139 139 ASN ASN A . n 
A 1 167 ALA 167 140 140 ALA ALA A . n 
A 1 168 GLY 168 141 141 GLY GLY A . n 
A 1 169 SER 169 142 142 SER SER A . n 
A 1 170 ARG 170 143 143 ARG ARG A . n 
A 1 171 LEU 171 144 144 LEU LEU A . n 
A 1 172 ALA 172 145 145 ALA ALA A . n 
A 1 173 CYS 173 146 146 CYS CYS A . n 
A 1 174 GLY 174 147 147 GLY GLY A . n 
A 1 175 VAL 175 148 148 VAL VAL A . n 
A 1 176 ILE 176 149 149 ILE ILE A . n 
A 1 177 GLY 177 150 150 GLY GLY A . n 
A 1 178 ILE 178 151 151 ILE ILE A . n 
A 1 179 ALA 179 152 152 ALA ALA A . n 
A 1 180 GLN 180 153 153 GLN GLN A . n 
B 1 1   MET 1   -26 ?   ?   ?   B . n 
B 1 2   LYS 2   -25 ?   ?   ?   B . n 
B 1 3   HIS 3   -24 ?   ?   ?   B . n 
B 1 4   HIS 4   -23 ?   ?   ?   B . n 
B 1 5   HIS 5   -22 ?   ?   ?   B . n 
B 1 6   HIS 6   -21 ?   ?   ?   B . n 
B 1 7   HIS 7   -20 ?   ?   ?   B . n 
B 1 8   HIS 8   -19 ?   ?   ?   B . n 
B 1 9   PRO 9   -18 ?   ?   ?   B . n 
B 1 10  MET 10  -17 ?   ?   ?   B . n 
B 1 11  SER 11  -16 ?   ?   ?   B . n 
B 1 12  ASP 12  -15 ?   ?   ?   B . n 
B 1 13  TYR 13  -14 ?   ?   ?   B . n 
B 1 14  ASP 14  -13 ?   ?   ?   B . n 
B 1 15  ILE 15  -12 ?   ?   ?   B . n 
B 1 16  PRO 16  -11 ?   ?   ?   B . n 
B 1 17  THR 17  -10 ?   ?   ?   B . n 
B 1 18  THR 18  -9  ?   ?   ?   B . n 
B 1 19  GLU 19  -8  ?   ?   ?   B . n 
B 1 20  ASN 20  -7  ?   ?   ?   B . n 
B 1 21  LEU 21  -6  ?   ?   ?   B . n 
B 1 22  TYR 22  -5  ?   ?   ?   B . n 
B 1 23  PHE 23  -4  ?   ?   ?   B . n 
B 1 24  GLN 24  -3  ?   ?   ?   B . n 
B 1 25  GLY 25  -2  ?   ?   ?   B . n 
B 1 26  ALA 26  -1  ?   ?   ?   B . n 
B 1 27  MET 27  0   0   MET ALA B . n 
B 1 28  ALA 28  1   1   ALA ALA B . n 
B 1 29  THR 29  2   2   THR THR B . n 
B 1 30  LYS 30  3   3   LYS LYS B . n 
B 1 31  ALA 31  4   4   ALA ALA B . n 
B 1 32  VAL 32  5   5   VAL VAL B . n 
B 1 33  CYS 33  6   6   CYS CYS B . n 
B 1 34  VAL 34  7   7   VAL VAL B . n 
B 1 35  LEU 35  8   8   LEU LEU B . n 
B 1 36  LYS 36  9   9   LYS LYS B . n 
B 1 37  GLY 37  10  10  GLY GLY B . n 
B 1 38  ASP 38  11  11  ASP ASP B . n 
B 1 39  GLY 39  12  12  GLY GLY B . n 
B 1 40  PRO 40  13  13  PRO PRO B . n 
B 1 41  VAL 41  14  14  VAL VAL B . n 
B 1 42  GLN 42  15  15  GLN GLN B . n 
B 1 43  GLY 43  16  16  GLY GLY B . n 
B 1 44  ILE 44  17  17  ILE ILE B . n 
B 1 45  ILE 45  18  18  ILE ILE B . n 
B 1 46  ASN 46  19  19  ASN ASN B . n 
B 1 47  PHE 47  20  20  PHE PHE B . n 
B 1 48  GLU 48  21  21  GLU GLU B . n 
B 1 49  GLN 49  22  22  GLN GLN B . n 
B 1 50  LYS 50  23  23  LYS LYS B . n 
B 1 51  GLU 51  24  24  GLU GLU B . n 
B 1 52  SER 52  25  25  SER SER B . n 
B 1 53  ASN 53  26  26  ASN ASN B . n 
B 1 54  GLY 54  27  27  GLY GLY B . n 
B 1 55  PRO 55  28  28  PRO PRO B . n 
B 1 56  VAL 56  29  29  VAL VAL B . n 
B 1 57  LYS 57  30  30  LYS LYS B . n 
B 1 58  VAL 58  31  31  VAL VAL B . n 
B 1 59  TRP 59  32  32  TRP TRP B . n 
B 1 60  GLY 60  33  33  GLY GLY B . n 
B 1 61  SER 61  34  34  SER SER B . n 
B 1 62  ILE 62  35  35  ILE ILE B . n 
B 1 63  LYS 63  36  36  LYS LYS B . n 
B 1 64  GLY 64  37  37  GLY GLY B . n 
B 1 65  LEU 65  38  38  LEU LEU B . n 
B 1 66  THR 66  39  39  THR THR B . n 
B 1 67  GLU 67  40  40  GLU GLU B . n 
B 1 68  GLY 68  41  41  GLY GLY B . n 
B 1 69  LEU 69  42  42  LEU LEU B . n 
B 1 70  HIS 70  43  43  HIS HIS B . n 
B 1 71  GLY 71  44  44  GLY GLY B . n 
B 1 72  PHE 72  45  45  PHE PHE B . n 
B 1 73  HIS 73  46  46  HIS HIS B . n 
B 1 74  VAL 74  47  47  VAL VAL B . n 
B 1 75  HIS 75  48  48  HIS HIS B . n 
B 1 76  GLU 76  49  49  GLU GLU B . n 
B 1 77  PHE 77  50  50  PHE PHE B . n 
B 1 78  GLY 78  51  51  GLY GLY B . n 
B 1 79  ASP 79  52  52  ASP ASP B . n 
B 1 80  ASN 80  53  53  ASN ASN B . n 
B 1 81  THR 81  54  54  THR THR B . n 
B 1 82  ALA 82  55  55  ALA ALA B . n 
B 1 83  GLY 83  56  56  GLY GLY B . n 
B 1 84  CYS 84  57  57  CYS CYS B . n 
B 1 85  THR 85  58  58  THR THR B . n 
B 1 86  SER 86  59  59  SER SER B . n 
B 1 87  ALA 87  60  60  ALA ALA B . n 
B 1 88  GLY 88  61  61  GLY GLY B . n 
B 1 89  PRO 89  62  62  PRO PRO B . n 
B 1 90  HIS 90  63  63  HIS HIS B . n 
B 1 91  PHE 91  64  64  PHE PHE B . n 
B 1 92  ASN 92  65  65  ASN ASN B . n 
B 1 93  PRO 93  66  66  PRO PRO B . n 
B 1 94  LEU 94  67  67  LEU LEU B . n 
B 1 95  SER 95  68  68  SER SER B . n 
B 1 96  ARG 96  69  69  ARG ARG B . n 
B 1 97  LYS 97  70  70  LYS LYS B . n 
B 1 98  HIS 98  71  71  HIS HIS B . n 
B 1 99  GLY 99  72  72  GLY GLY B . n 
B 1 100 GLY 100 73  73  GLY GLY B . n 
B 1 101 PRO 101 74  74  PRO PRO B . n 
B 1 102 LYS 102 75  75  LYS LYS B . n 
B 1 103 ASP 103 76  76  ASP ASP B . n 
B 1 104 GLU 104 77  77  GLU GLU B . n 
B 1 105 GLU 105 78  78  GLU GLU B . n 
B 1 106 ARG 106 79  79  ARG ARG B . n 
B 1 107 HIS 107 80  80  HIS HIS B . n 
B 1 108 VAL 108 81  81  VAL VAL B . n 
B 1 109 GLY 109 82  82  GLY GLY B . n 
B 1 110 ASP 110 83  83  ASP ASP B . n 
B 1 111 LEU 111 84  84  LEU LEU B . n 
B 1 112 GLY 112 85  85  GLY GLY B . n 
B 1 113 ASN 113 86  86  ASN ASN B . n 
B 1 114 VAL 114 87  87  VAL VAL B . n 
B 1 115 THR 115 88  88  THR THR B . n 
B 1 116 ALA 116 89  89  ALA ALA B . n 
B 1 117 ASP 117 90  90  ASP ASP B . n 
B 1 118 LYS 118 91  91  LYS LYS B . n 
B 1 119 ASP 119 92  92  ASP ASP B . n 
B 1 120 GLY 120 93  93  GLY GLY B . n 
B 1 121 VAL 121 94  94  VAL VAL B . n 
B 1 122 ALA 122 95  95  ALA ALA B . n 
B 1 123 ASP 123 96  96  ASP ASP B . n 
B 1 124 VAL 124 97  97  VAL VAL B . n 
B 1 125 SER 125 98  98  SER SER B . n 
B 1 126 ILE 126 99  99  ILE ILE B . n 
B 1 127 GLU 127 100 100 GLU GLU B . n 
B 1 128 ASP 128 101 101 ASP ASP B . n 
B 1 129 SER 129 102 102 SER SER B . n 
B 1 130 VAL 130 103 103 VAL VAL B . n 
B 1 131 ILE 131 104 104 ILE ILE B . n 
B 1 132 SER 132 105 105 SER SER B . n 
B 1 133 LEU 133 106 106 LEU LEU B . n 
B 1 134 SER 134 107 107 SER SER B . n 
B 1 135 GLY 135 108 108 GLY GLY B . n 
B 1 136 ASP 136 109 109 ASP ASP B . n 
B 1 137 HIS 137 110 110 HIS HIS B . n 
B 1 138 CYS 138 111 111 CYS CYS B . n 
B 1 139 ILE 139 112 112 ILE ILE B . n 
B 1 140 ILE 140 113 113 ILE ILE B . n 
B 1 141 GLY 141 114 114 GLY GLY B . n 
B 1 142 ARG 142 115 115 ARG ARG B . n 
B 1 143 THR 143 116 116 THR THR B . n 
B 1 144 LEU 144 117 117 LEU LEU B . n 
B 1 145 VAL 145 118 118 VAL VAL B . n 
B 1 146 VAL 146 119 119 VAL VAL B . n 
B 1 147 HIS 147 120 120 HIS HIS B . n 
B 1 148 GLU 148 121 121 GLU GLU B . n 
B 1 149 LYS 149 122 122 LYS LYS B . n 
B 1 150 ALA 150 123 123 ALA ALA B . n 
B 1 151 ASP 151 124 124 ASP ASP B . n 
B 1 152 ASP 152 125 125 ASP ASP B . n 
B 1 153 LEU 153 126 126 LEU LEU B . n 
B 1 154 GLY 154 127 127 GLY GLY B . n 
B 1 155 LYS 155 128 128 LYS LYS B . n 
B 1 156 GLY 156 129 129 GLY GLY B . n 
B 1 157 GLY 157 130 130 GLY GLY B . n 
B 1 158 ASN 158 131 131 ASN ASN B . n 
B 1 159 GLU 159 132 132 GLU GLU B . n 
B 1 160 GLU 160 133 133 GLU GLU B . n 
B 1 161 SER 161 134 134 SER SER B . n 
B 1 162 THR 162 135 135 THR THR B . n 
B 1 163 LYS 163 136 136 LYS LYS B . n 
B 1 164 THR 164 137 137 THR THR B . n 
B 1 165 GLY 165 138 138 GLY GLY B . n 
B 1 166 ASN 166 139 139 ASN ASN B . n 
B 1 167 ALA 167 140 140 ALA ALA B . n 
B 1 168 GLY 168 141 141 GLY GLY B . n 
B 1 169 SER 169 142 142 SER SER B . n 
B 1 170 ARG 170 143 143 ARG ARG B . n 
B 1 171 LEU 171 144 144 LEU LEU B . n 
B 1 172 ALA 172 145 145 ALA ALA B . n 
B 1 173 CYS 173 146 146 CYS CYS B . n 
B 1 174 GLY 174 147 147 GLY GLY B . n 
B 1 175 VAL 175 148 148 VAL VAL B . n 
B 1 176 ILE 176 149 149 ILE ILE B . n 
B 1 177 GLY 177 150 150 GLY GLY B . n 
B 1 178 ILE 178 151 151 ILE ILE B . n 
B 1 179 ALA 179 152 152 ALA ALA B . n 
B 1 180 GLN 180 153 153 GLN GLN B . n 
C 1 1   MET 1   -26 ?   ?   ?   C . n 
C 1 2   LYS 2   -25 ?   ?   ?   C . n 
C 1 3   HIS 3   -24 ?   ?   ?   C . n 
C 1 4   HIS 4   -23 ?   ?   ?   C . n 
C 1 5   HIS 5   -22 ?   ?   ?   C . n 
C 1 6   HIS 6   -21 ?   ?   ?   C . n 
C 1 7   HIS 7   -20 ?   ?   ?   C . n 
C 1 8   HIS 8   -19 ?   ?   ?   C . n 
C 1 9   PRO 9   -18 ?   ?   ?   C . n 
C 1 10  MET 10  -17 ?   ?   ?   C . n 
C 1 11  SER 11  -16 ?   ?   ?   C . n 
C 1 12  ASP 12  -15 ?   ?   ?   C . n 
C 1 13  TYR 13  -14 ?   ?   ?   C . n 
C 1 14  ASP 14  -13 ?   ?   ?   C . n 
C 1 15  ILE 15  -12 ?   ?   ?   C . n 
C 1 16  PRO 16  -11 ?   ?   ?   C . n 
C 1 17  THR 17  -10 ?   ?   ?   C . n 
C 1 18  THR 18  -9  ?   ?   ?   C . n 
C 1 19  GLU 19  -8  ?   ?   ?   C . n 
C 1 20  ASN 20  -7  ?   ?   ?   C . n 
C 1 21  LEU 21  -6  ?   ?   ?   C . n 
C 1 22  TYR 22  -5  ?   ?   ?   C . n 
C 1 23  PHE 23  -4  ?   ?   ?   C . n 
C 1 24  GLN 24  -3  ?   ?   ?   C . n 
C 1 25  GLY 25  -2  ?   ?   ?   C . n 
C 1 26  ALA 26  -1  ?   ?   ?   C . n 
C 1 27  MET 27  0   0   MET ALA C . n 
C 1 28  ALA 28  1   1   ALA ALA C . n 
C 1 29  THR 29  2   2   THR THR C . n 
C 1 30  LYS 30  3   3   LYS LYS C . n 
C 1 31  ALA 31  4   4   ALA ALA C . n 
C 1 32  VAL 32  5   5   VAL VAL C . n 
C 1 33  CYS 33  6   6   CYS CYS C . n 
C 1 34  VAL 34  7   7   VAL VAL C . n 
C 1 35  LEU 35  8   8   LEU LEU C . n 
C 1 36  LYS 36  9   9   LYS LYS C . n 
C 1 37  GLY 37  10  10  GLY GLY C . n 
C 1 38  ASP 38  11  11  ASP ASP C . n 
C 1 39  GLY 39  12  12  GLY GLY C . n 
C 1 40  PRO 40  13  13  PRO PRO C . n 
C 1 41  VAL 41  14  14  VAL VAL C . n 
C 1 42  GLN 42  15  15  GLN GLN C . n 
C 1 43  GLY 43  16  16  GLY GLY C . n 
C 1 44  ILE 44  17  17  ILE ILE C . n 
C 1 45  ILE 45  18  18  ILE ILE C . n 
C 1 46  ASN 46  19  19  ASN ASN C . n 
C 1 47  PHE 47  20  20  PHE PHE C . n 
C 1 48  GLU 48  21  21  GLU GLU C . n 
C 1 49  GLN 49  22  22  GLN GLN C . n 
C 1 50  LYS 50  23  23  LYS LYS C . n 
C 1 51  GLU 51  24  24  GLU GLU C . n 
C 1 52  SER 52  25  25  SER SER C . n 
C 1 53  ASN 53  26  26  ASN ASN C . n 
C 1 54  GLY 54  27  27  GLY GLY C . n 
C 1 55  PRO 55  28  28  PRO PRO C . n 
C 1 56  VAL 56  29  29  VAL VAL C . n 
C 1 57  LYS 57  30  30  LYS LYS C . n 
C 1 58  VAL 58  31  31  VAL VAL C . n 
C 1 59  TRP 59  32  32  TRP TRP C . n 
C 1 60  GLY 60  33  33  GLY GLY C . n 
C 1 61  SER 61  34  34  SER SER C . n 
C 1 62  ILE 62  35  35  ILE ILE C . n 
C 1 63  LYS 63  36  36  LYS LYS C . n 
C 1 64  GLY 64  37  37  GLY GLY C . n 
C 1 65  LEU 65  38  38  LEU LEU C . n 
C 1 66  THR 66  39  39  THR THR C . n 
C 1 67  GLU 67  40  40  GLU GLU C . n 
C 1 68  GLY 68  41  41  GLY GLY C . n 
C 1 69  LEU 69  42  42  LEU LEU C . n 
C 1 70  HIS 70  43  43  HIS HIS C . n 
C 1 71  GLY 71  44  44  GLY GLY C . n 
C 1 72  PHE 72  45  45  PHE PHE C . n 
C 1 73  HIS 73  46  46  HIS HIS C . n 
C 1 74  VAL 74  47  47  VAL VAL C . n 
C 1 75  HIS 75  48  48  HIS HIS C . n 
C 1 76  GLU 76  49  49  GLU GLU C . n 
C 1 77  PHE 77  50  50  PHE PHE C . n 
C 1 78  GLY 78  51  51  GLY GLY C . n 
C 1 79  ASP 79  52  52  ASP ASP C . n 
C 1 80  ASN 80  53  53  ASN ASN C . n 
C 1 81  THR 81  54  54  THR THR C . n 
C 1 82  ALA 82  55  55  ALA ALA C . n 
C 1 83  GLY 83  56  56  GLY GLY C . n 
C 1 84  CYS 84  57  57  CYS CYS C . n 
C 1 85  THR 85  58  58  THR THR C . n 
C 1 86  SER 86  59  59  SER SER C . n 
C 1 87  ALA 87  60  60  ALA ALA C . n 
C 1 88  GLY 88  61  61  GLY GLY C . n 
C 1 89  PRO 89  62  62  PRO PRO C . n 
C 1 90  HIS 90  63  63  HIS HIS C . n 
C 1 91  PHE 91  64  64  PHE PHE C . n 
C 1 92  ASN 92  65  65  ASN ASN C . n 
C 1 93  PRO 93  66  66  PRO PRO C . n 
C 1 94  LEU 94  67  67  LEU LEU C . n 
C 1 95  SER 95  68  68  SER SER C . n 
C 1 96  ARG 96  69  69  ARG ARG C . n 
C 1 97  LYS 97  70  70  LYS LYS C . n 
C 1 98  HIS 98  71  71  HIS HIS C . n 
C 1 99  GLY 99  72  72  GLY GLY C . n 
C 1 100 GLY 100 73  73  GLY GLY C . n 
C 1 101 PRO 101 74  74  PRO PRO C . n 
C 1 102 LYS 102 75  75  LYS LYS C . n 
C 1 103 ASP 103 76  76  ASP ASP C . n 
C 1 104 GLU 104 77  77  GLU GLU C . n 
C 1 105 GLU 105 78  78  GLU GLU C . n 
C 1 106 ARG 106 79  79  ARG ARG C . n 
C 1 107 HIS 107 80  80  HIS HIS C . n 
C 1 108 VAL 108 81  81  VAL VAL C . n 
C 1 109 GLY 109 82  82  GLY GLY C . n 
C 1 110 ASP 110 83  83  ASP ASP C . n 
C 1 111 LEU 111 84  84  LEU LEU C . n 
C 1 112 GLY 112 85  85  GLY GLY C . n 
C 1 113 ASN 113 86  86  ASN ASN C . n 
C 1 114 VAL 114 87  87  VAL VAL C . n 
C 1 115 THR 115 88  88  THR THR C . n 
C 1 116 ALA 116 89  89  ALA ALA C . n 
C 1 117 ASP 117 90  90  ASP ASP C . n 
C 1 118 LYS 118 91  91  LYS LYS C . n 
C 1 119 ASP 119 92  92  ASP ASP C . n 
C 1 120 GLY 120 93  93  GLY GLY C . n 
C 1 121 VAL 121 94  94  VAL VAL C . n 
C 1 122 ALA 122 95  95  ALA ALA C . n 
C 1 123 ASP 123 96  96  ASP ASP C . n 
C 1 124 VAL 124 97  97  VAL VAL C . n 
C 1 125 SER 125 98  98  SER SER C . n 
C 1 126 ILE 126 99  99  ILE ILE C . n 
C 1 127 GLU 127 100 100 GLU GLU C . n 
C 1 128 ASP 128 101 101 ASP ASP C . n 
C 1 129 SER 129 102 102 SER SER C . n 
C 1 130 VAL 130 103 103 VAL VAL C . n 
C 1 131 ILE 131 104 104 ILE ILE C . n 
C 1 132 SER 132 105 105 SER SER C . n 
C 1 133 LEU 133 106 106 LEU LEU C . n 
C 1 134 SER 134 107 107 SER SER C . n 
C 1 135 GLY 135 108 108 GLY GLY C . n 
C 1 136 ASP 136 109 109 ASP ASP C . n 
C 1 137 HIS 137 110 110 HIS HIS C . n 
C 1 138 CYS 138 111 111 CYS CYS C . n 
C 1 139 ILE 139 112 112 ILE ILE C . n 
C 1 140 ILE 140 113 113 ILE ILE C . n 
C 1 141 GLY 141 114 114 GLY GLY C . n 
C 1 142 ARG 142 115 115 ARG ARG C . n 
C 1 143 THR 143 116 116 THR THR C . n 
C 1 144 LEU 144 117 117 LEU LEU C . n 
C 1 145 VAL 145 118 118 VAL VAL C . n 
C 1 146 VAL 146 119 119 VAL VAL C . n 
C 1 147 HIS 147 120 120 HIS HIS C . n 
C 1 148 GLU 148 121 121 GLU GLU C . n 
C 1 149 LYS 149 122 122 LYS LYS C . n 
C 1 150 ALA 150 123 123 ALA ALA C . n 
C 1 151 ASP 151 124 124 ASP ASP C . n 
C 1 152 ASP 152 125 125 ASP ASP C . n 
C 1 153 LEU 153 126 126 LEU LEU C . n 
C 1 154 GLY 154 127 127 GLY GLY C . n 
C 1 155 LYS 155 128 128 LYS LYS C . n 
C 1 156 GLY 156 129 129 GLY GLY C . n 
C 1 157 GLY 157 130 130 GLY GLY C . n 
C 1 158 ASN 158 131 131 ASN ASN C . n 
C 1 159 GLU 159 132 132 GLU GLU C . n 
C 1 160 GLU 160 133 133 GLU GLU C . n 
C 1 161 SER 161 134 134 SER SER C . n 
C 1 162 THR 162 135 135 THR THR C . n 
C 1 163 LYS 163 136 136 LYS LYS C . n 
C 1 164 THR 164 137 137 THR THR C . n 
C 1 165 GLY 165 138 138 GLY GLY C . n 
C 1 166 ASN 166 139 139 ASN ASN C . n 
C 1 167 ALA 167 140 140 ALA ALA C . n 
C 1 168 GLY 168 141 141 GLY GLY C . n 
C 1 169 SER 169 142 142 SER SER C . n 
C 1 170 ARG 170 143 143 ARG ARG C . n 
C 1 171 LEU 171 144 144 LEU LEU C . n 
C 1 172 ALA 172 145 145 ALA ALA C . n 
C 1 173 CYS 173 146 146 CYS CYS C . n 
C 1 174 GLY 174 147 147 GLY GLY C . n 
C 1 175 VAL 175 148 148 VAL VAL C . n 
C 1 176 ILE 176 149 149 ILE ILE C . n 
C 1 177 GLY 177 150 150 GLY GLY C . n 
C 1 178 ILE 178 151 151 ILE ILE C . n 
C 1 179 ALA 179 152 152 ALA ALA C . n 
C 1 180 GLN 180 153 153 GLN GLN C . n 
D 1 1   MET 1   -26 ?   ?   ?   D . n 
D 1 2   LYS 2   -25 ?   ?   ?   D . n 
D 1 3   HIS 3   -24 ?   ?   ?   D . n 
D 1 4   HIS 4   -23 ?   ?   ?   D . n 
D 1 5   HIS 5   -22 ?   ?   ?   D . n 
D 1 6   HIS 6   -21 ?   ?   ?   D . n 
D 1 7   HIS 7   -20 ?   ?   ?   D . n 
D 1 8   HIS 8   -19 ?   ?   ?   D . n 
D 1 9   PRO 9   -18 ?   ?   ?   D . n 
D 1 10  MET 10  -17 ?   ?   ?   D . n 
D 1 11  SER 11  -16 ?   ?   ?   D . n 
D 1 12  ASP 12  -15 ?   ?   ?   D . n 
D 1 13  TYR 13  -14 ?   ?   ?   D . n 
D 1 14  ASP 14  -13 ?   ?   ?   D . n 
D 1 15  ILE 15  -12 ?   ?   ?   D . n 
D 1 16  PRO 16  -11 ?   ?   ?   D . n 
D 1 17  THR 17  -10 ?   ?   ?   D . n 
D 1 18  THR 18  -9  ?   ?   ?   D . n 
D 1 19  GLU 19  -8  ?   ?   ?   D . n 
D 1 20  ASN 20  -7  ?   ?   ?   D . n 
D 1 21  LEU 21  -6  ?   ?   ?   D . n 
D 1 22  TYR 22  -5  ?   ?   ?   D . n 
D 1 23  PHE 23  -4  ?   ?   ?   D . n 
D 1 24  GLN 24  -3  ?   ?   ?   D . n 
D 1 25  GLY 25  -2  ?   ?   ?   D . n 
D 1 26  ALA 26  -1  -1  ALA ALA D . n 
D 1 27  MET 27  0   0   MET ALA D . n 
D 1 28  ALA 28  1   1   ALA ALA D . n 
D 1 29  THR 29  2   2   THR THR D . n 
D 1 30  LYS 30  3   3   LYS LYS D . n 
D 1 31  ALA 31  4   4   ALA ALA D . n 
D 1 32  VAL 32  5   5   VAL VAL D . n 
D 1 33  CYS 33  6   6   CYS CYS D . n 
D 1 34  VAL 34  7   7   VAL VAL D . n 
D 1 35  LEU 35  8   8   LEU LEU D . n 
D 1 36  LYS 36  9   9   LYS LYS D . n 
D 1 37  GLY 37  10  10  GLY GLY D . n 
D 1 38  ASP 38  11  11  ASP ASP D . n 
D 1 39  GLY 39  12  12  GLY GLY D . n 
D 1 40  PRO 40  13  13  PRO PRO D . n 
D 1 41  VAL 41  14  14  VAL VAL D . n 
D 1 42  GLN 42  15  15  GLN GLN D . n 
D 1 43  GLY 43  16  16  GLY GLY D . n 
D 1 44  ILE 44  17  17  ILE ILE D . n 
D 1 45  ILE 45  18  18  ILE ILE D . n 
D 1 46  ASN 46  19  19  ASN ASN D . n 
D 1 47  PHE 47  20  20  PHE PHE D . n 
D 1 48  GLU 48  21  21  GLU GLU D . n 
D 1 49  GLN 49  22  22  GLN GLN D . n 
D 1 50  LYS 50  23  23  LYS LYS D . n 
D 1 51  GLU 51  24  24  GLU GLU D . n 
D 1 52  SER 52  25  25  SER SER D . n 
D 1 53  ASN 53  26  26  ASN ASN D . n 
D 1 54  GLY 54  27  27  GLY GLY D . n 
D 1 55  PRO 55  28  28  PRO PRO D . n 
D 1 56  VAL 56  29  29  VAL VAL D . n 
D 1 57  LYS 57  30  30  LYS LYS D . n 
D 1 58  VAL 58  31  31  VAL VAL D . n 
D 1 59  TRP 59  32  32  TRP TRP D . n 
D 1 60  GLY 60  33  33  GLY GLY D . n 
D 1 61  SER 61  34  34  SER SER D . n 
D 1 62  ILE 62  35  35  ILE ILE D . n 
D 1 63  LYS 63  36  36  LYS LYS D . n 
D 1 64  GLY 64  37  37  GLY GLY D . n 
D 1 65  LEU 65  38  38  LEU LEU D . n 
D 1 66  THR 66  39  39  THR THR D . n 
D 1 67  GLU 67  40  40  GLU GLU D . n 
D 1 68  GLY 68  41  41  GLY GLY D . n 
D 1 69  LEU 69  42  42  LEU LEU D . n 
D 1 70  HIS 70  43  43  HIS HIS D . n 
D 1 71  GLY 71  44  44  GLY GLY D . n 
D 1 72  PHE 72  45  45  PHE PHE D . n 
D 1 73  HIS 73  46  46  HIS HIS D . n 
D 1 74  VAL 74  47  47  VAL VAL D . n 
D 1 75  HIS 75  48  48  HIS HIS D . n 
D 1 76  GLU 76  49  49  GLU GLU D . n 
D 1 77  PHE 77  50  50  PHE PHE D . n 
D 1 78  GLY 78  51  51  GLY GLY D . n 
D 1 79  ASP 79  52  52  ASP ASP D . n 
D 1 80  ASN 80  53  53  ASN ASN D . n 
D 1 81  THR 81  54  54  THR THR D . n 
D 1 82  ALA 82  55  55  ALA ALA D . n 
D 1 83  GLY 83  56  56  GLY GLY D . n 
D 1 84  CYS 84  57  57  CYS CYS D . n 
D 1 85  THR 85  58  58  THR THR D . n 
D 1 86  SER 86  59  59  SER SER D . n 
D 1 87  ALA 87  60  60  ALA ALA D . n 
D 1 88  GLY 88  61  61  GLY GLY D . n 
D 1 89  PRO 89  62  62  PRO PRO D . n 
D 1 90  HIS 90  63  63  HIS HIS D . n 
D 1 91  PHE 91  64  64  PHE PHE D . n 
D 1 92  ASN 92  65  65  ASN ASN D . n 
D 1 93  PRO 93  66  66  PRO PRO D . n 
D 1 94  LEU 94  67  67  LEU LEU D . n 
D 1 95  SER 95  68  68  SER SER D . n 
D 1 96  ARG 96  69  69  ARG ARG D . n 
D 1 97  LYS 97  70  70  LYS LYS D . n 
D 1 98  HIS 98  71  71  HIS HIS D . n 
D 1 99  GLY 99  72  72  GLY GLY D . n 
D 1 100 GLY 100 73  73  GLY GLY D . n 
D 1 101 PRO 101 74  74  PRO PRO D . n 
D 1 102 LYS 102 75  75  LYS LYS D . n 
D 1 103 ASP 103 76  76  ASP ASP D . n 
D 1 104 GLU 104 77  77  GLU GLU D . n 
D 1 105 GLU 105 78  78  GLU GLU D . n 
D 1 106 ARG 106 79  79  ARG ARG D . n 
D 1 107 HIS 107 80  80  HIS HIS D . n 
D 1 108 VAL 108 81  81  VAL VAL D . n 
D 1 109 GLY 109 82  82  GLY GLY D . n 
D 1 110 ASP 110 83  83  ASP ASP D . n 
D 1 111 LEU 111 84  84  LEU LEU D . n 
D 1 112 GLY 112 85  85  GLY GLY D . n 
D 1 113 ASN 113 86  86  ASN ASN D . n 
D 1 114 VAL 114 87  87  VAL VAL D . n 
D 1 115 THR 115 88  88  THR THR D . n 
D 1 116 ALA 116 89  89  ALA ALA D . n 
D 1 117 ASP 117 90  90  ASP ASP D . n 
D 1 118 LYS 118 91  91  LYS LYS D . n 
D 1 119 ASP 119 92  92  ASP ASP D . n 
D 1 120 GLY 120 93  93  GLY GLY D . n 
D 1 121 VAL 121 94  94  VAL VAL D . n 
D 1 122 ALA 122 95  95  ALA ALA D . n 
D 1 123 ASP 123 96  96  ASP ASP D . n 
D 1 124 VAL 124 97  97  VAL VAL D . n 
D 1 125 SER 125 98  98  SER SER D . n 
D 1 126 ILE 126 99  99  ILE ILE D . n 
D 1 127 GLU 127 100 100 GLU GLU D . n 
D 1 128 ASP 128 101 101 ASP ASP D . n 
D 1 129 SER 129 102 102 SER SER D . n 
D 1 130 VAL 130 103 103 VAL VAL D . n 
D 1 131 ILE 131 104 104 ILE ILE D . n 
D 1 132 SER 132 105 105 SER SER D . n 
D 1 133 LEU 133 106 106 LEU LEU D . n 
D 1 134 SER 134 107 107 SER SER D . n 
D 1 135 GLY 135 108 108 GLY GLY D . n 
D 1 136 ASP 136 109 109 ASP ASP D . n 
D 1 137 HIS 137 110 110 HIS HIS D . n 
D 1 138 CYS 138 111 111 CYS CYS D . n 
D 1 139 ILE 139 112 112 ILE ILE D . n 
D 1 140 ILE 140 113 113 ILE ILE D . n 
D 1 141 GLY 141 114 114 GLY GLY D . n 
D 1 142 ARG 142 115 115 ARG ARG D . n 
D 1 143 THR 143 116 116 THR THR D . n 
D 1 144 LEU 144 117 117 LEU LEU D . n 
D 1 145 VAL 145 118 118 VAL VAL D . n 
D 1 146 VAL 146 119 119 VAL VAL D . n 
D 1 147 HIS 147 120 120 HIS HIS D . n 
D 1 148 GLU 148 121 121 GLU GLU D . n 
D 1 149 LYS 149 122 122 LYS LYS D . n 
D 1 150 ALA 150 123 123 ALA ALA D . n 
D 1 151 ASP 151 124 124 ASP ASP D . n 
D 1 152 ASP 152 125 125 ASP ASP D . n 
D 1 153 LEU 153 126 126 LEU LEU D . n 
D 1 154 GLY 154 127 127 GLY GLY D . n 
D 1 155 LYS 155 128 128 LYS LYS D . n 
D 1 156 GLY 156 129 129 GLY GLY D . n 
D 1 157 GLY 157 130 130 GLY GLY D . n 
D 1 158 ASN 158 131 131 ASN ASN D . n 
D 1 159 GLU 159 132 132 GLU GLU D . n 
D 1 160 GLU 160 133 133 GLU GLU D . n 
D 1 161 SER 161 134 134 SER SER D . n 
D 1 162 THR 162 135 135 THR THR D . n 
D 1 163 LYS 163 136 136 LYS LYS D . n 
D 1 164 THR 164 137 137 THR THR D . n 
D 1 165 GLY 165 138 138 GLY GLY D . n 
D 1 166 ASN 166 139 139 ASN ASN D . n 
D 1 167 ALA 167 140 140 ALA ALA D . n 
D 1 168 GLY 168 141 141 GLY GLY D . n 
D 1 169 SER 169 142 142 SER SER D . n 
D 1 170 ARG 170 143 143 ARG ARG D . n 
D 1 171 LEU 171 144 144 LEU LEU D . n 
D 1 172 ALA 172 145 145 ALA ALA D . n 
D 1 173 CYS 173 146 146 CYS CYS D . n 
D 1 174 GLY 174 147 147 GLY GLY D . n 
D 1 175 VAL 175 148 148 VAL VAL D . n 
D 1 176 ILE 176 149 149 ILE ILE D . n 
D 1 177 GLY 177 150 150 GLY GLY D . n 
D 1 178 ILE 178 151 151 ILE ILE D . n 
D 1 179 ALA 179 152 152 ALA ALA D . n 
D 1 180 GLN 180 153 153 GLN GLN D . n 
E 1 1   MET 1   -26 ?   ?   ?   E . n 
E 1 2   LYS 2   -25 ?   ?   ?   E . n 
E 1 3   HIS 3   -24 ?   ?   ?   E . n 
E 1 4   HIS 4   -23 ?   ?   ?   E . n 
E 1 5   HIS 5   -22 ?   ?   ?   E . n 
E 1 6   HIS 6   -21 ?   ?   ?   E . n 
E 1 7   HIS 7   -20 ?   ?   ?   E . n 
E 1 8   HIS 8   -19 ?   ?   ?   E . n 
E 1 9   PRO 9   -18 ?   ?   ?   E . n 
E 1 10  MET 10  -17 ?   ?   ?   E . n 
E 1 11  SER 11  -16 ?   ?   ?   E . n 
E 1 12  ASP 12  -15 ?   ?   ?   E . n 
E 1 13  TYR 13  -14 ?   ?   ?   E . n 
E 1 14  ASP 14  -13 ?   ?   ?   E . n 
E 1 15  ILE 15  -12 ?   ?   ?   E . n 
E 1 16  PRO 16  -11 ?   ?   ?   E . n 
E 1 17  THR 17  -10 ?   ?   ?   E . n 
E 1 18  THR 18  -9  ?   ?   ?   E . n 
E 1 19  GLU 19  -8  ?   ?   ?   E . n 
E 1 20  ASN 20  -7  ?   ?   ?   E . n 
E 1 21  LEU 21  -6  ?   ?   ?   E . n 
E 1 22  TYR 22  -5  ?   ?   ?   E . n 
E 1 23  PHE 23  -4  ?   ?   ?   E . n 
E 1 24  GLN 24  -3  ?   ?   ?   E . n 
E 1 25  GLY 25  -2  ?   ?   ?   E . n 
E 1 26  ALA 26  -1  ?   ?   ?   E . n 
E 1 27  MET 27  0   0   MET ALA E . n 
E 1 28  ALA 28  1   1   ALA ALA E . n 
E 1 29  THR 29  2   2   THR THR E . n 
E 1 30  LYS 30  3   3   LYS LYS E . n 
E 1 31  ALA 31  4   4   ALA ALA E . n 
E 1 32  VAL 32  5   5   VAL VAL E . n 
E 1 33  CYS 33  6   6   CYS CYS E . n 
E 1 34  VAL 34  7   7   VAL VAL E . n 
E 1 35  LEU 35  8   8   LEU LEU E . n 
E 1 36  LYS 36  9   9   LYS LYS E . n 
E 1 37  GLY 37  10  10  GLY GLY E . n 
E 1 38  ASP 38  11  11  ASP ASP E . n 
E 1 39  GLY 39  12  12  GLY GLY E . n 
E 1 40  PRO 40  13  13  PRO PRO E . n 
E 1 41  VAL 41  14  14  VAL VAL E . n 
E 1 42  GLN 42  15  15  GLN GLN E . n 
E 1 43  GLY 43  16  16  GLY GLY E . n 
E 1 44  ILE 44  17  17  ILE ILE E . n 
E 1 45  ILE 45  18  18  ILE ILE E . n 
E 1 46  ASN 46  19  19  ASN ASN E . n 
E 1 47  PHE 47  20  20  PHE PHE E . n 
E 1 48  GLU 48  21  21  GLU GLU E . n 
E 1 49  GLN 49  22  22  GLN GLN E . n 
E 1 50  LYS 50  23  23  LYS LYS E . n 
E 1 51  GLU 51  24  24  GLU GLU E . n 
E 1 52  SER 52  25  25  SER SER E . n 
E 1 53  ASN 53  26  26  ASN ASN E . n 
E 1 54  GLY 54  27  27  GLY GLY E . n 
E 1 55  PRO 55  28  28  PRO PRO E . n 
E 1 56  VAL 56  29  29  VAL VAL E . n 
E 1 57  LYS 57  30  30  LYS LYS E . n 
E 1 58  VAL 58  31  31  VAL VAL E . n 
E 1 59  TRP 59  32  32  TRP TRP E . n 
E 1 60  GLY 60  33  33  GLY GLY E . n 
E 1 61  SER 61  34  34  SER SER E . n 
E 1 62  ILE 62  35  35  ILE ILE E . n 
E 1 63  LYS 63  36  36  LYS LYS E . n 
E 1 64  GLY 64  37  37  GLY GLY E . n 
E 1 65  LEU 65  38  38  LEU LEU E . n 
E 1 66  THR 66  39  39  THR THR E . n 
E 1 67  GLU 67  40  40  GLU GLU E . n 
E 1 68  GLY 68  41  41  GLY GLY E . n 
E 1 69  LEU 69  42  42  LEU LEU E . n 
E 1 70  HIS 70  43  43  HIS HIS E . n 
E 1 71  GLY 71  44  44  GLY GLY E . n 
E 1 72  PHE 72  45  45  PHE PHE E . n 
E 1 73  HIS 73  46  46  HIS HIS E . n 
E 1 74  VAL 74  47  47  VAL VAL E . n 
E 1 75  HIS 75  48  48  HIS HIS E . n 
E 1 76  GLU 76  49  49  GLU GLU E . n 
E 1 77  PHE 77  50  50  PHE PHE E . n 
E 1 78  GLY 78  51  51  GLY GLY E . n 
E 1 79  ASP 79  52  52  ASP ASP E . n 
E 1 80  ASN 80  53  53  ASN ASN E . n 
E 1 81  THR 81  54  54  THR THR E . n 
E 1 82  ALA 82  55  55  ALA ALA E . n 
E 1 83  GLY 83  56  56  GLY GLY E . n 
E 1 84  CYS 84  57  57  CYS CYS E . n 
E 1 85  THR 85  58  58  THR THR E . n 
E 1 86  SER 86  59  59  SER SER E . n 
E 1 87  ALA 87  60  60  ALA ALA E . n 
E 1 88  GLY 88  61  61  GLY GLY E . n 
E 1 89  PRO 89  62  62  PRO PRO E . n 
E 1 90  HIS 90  63  63  HIS HIS E . n 
E 1 91  PHE 91  64  64  PHE PHE E . n 
E 1 92  ASN 92  65  65  ASN ASN E . n 
E 1 93  PRO 93  66  66  PRO PRO E . n 
E 1 94  LEU 94  67  67  LEU LEU E . n 
E 1 95  SER 95  68  68  SER SER E . n 
E 1 96  ARG 96  69  69  ARG ARG E . n 
E 1 97  LYS 97  70  70  LYS LYS E . n 
E 1 98  HIS 98  71  71  HIS HIS E . n 
E 1 99  GLY 99  72  72  GLY GLY E . n 
E 1 100 GLY 100 73  73  GLY GLY E . n 
E 1 101 PRO 101 74  74  PRO PRO E . n 
E 1 102 LYS 102 75  75  LYS LYS E . n 
E 1 103 ASP 103 76  76  ASP ASP E . n 
E 1 104 GLU 104 77  77  GLU GLU E . n 
E 1 105 GLU 105 78  78  GLU GLU E . n 
E 1 106 ARG 106 79  79  ARG ARG E . n 
E 1 107 HIS 107 80  80  HIS HIS E . n 
E 1 108 VAL 108 81  81  VAL VAL E . n 
E 1 109 GLY 109 82  82  GLY GLY E . n 
E 1 110 ASP 110 83  83  ASP ASP E . n 
E 1 111 LEU 111 84  84  LEU LEU E . n 
E 1 112 GLY 112 85  85  GLY GLY E . n 
E 1 113 ASN 113 86  86  ASN ASN E . n 
E 1 114 VAL 114 87  87  VAL VAL E . n 
E 1 115 THR 115 88  88  THR THR E . n 
E 1 116 ALA 116 89  89  ALA ALA E . n 
E 1 117 ASP 117 90  90  ASP ASP E . n 
E 1 118 LYS 118 91  91  LYS LYS E . n 
E 1 119 ASP 119 92  92  ASP ASP E . n 
E 1 120 GLY 120 93  93  GLY GLY E . n 
E 1 121 VAL 121 94  94  VAL VAL E . n 
E 1 122 ALA 122 95  95  ALA ALA E . n 
E 1 123 ASP 123 96  96  ASP ASP E . n 
E 1 124 VAL 124 97  97  VAL VAL E . n 
E 1 125 SER 125 98  98  SER SER E . n 
E 1 126 ILE 126 99  99  ILE ILE E . n 
E 1 127 GLU 127 100 100 GLU GLU E . n 
E 1 128 ASP 128 101 101 ASP ASP E . n 
E 1 129 SER 129 102 102 SER SER E . n 
E 1 130 VAL 130 103 103 VAL VAL E . n 
E 1 131 ILE 131 104 104 ILE ILE E . n 
E 1 132 SER 132 105 105 SER SER E . n 
E 1 133 LEU 133 106 106 LEU LEU E . n 
E 1 134 SER 134 107 107 SER SER E . n 
E 1 135 GLY 135 108 108 GLY GLY E . n 
E 1 136 ASP 136 109 109 ASP ASP E . n 
E 1 137 HIS 137 110 110 HIS HIS E . n 
E 1 138 CYS 138 111 111 CYS CYS E . n 
E 1 139 ILE 139 112 112 ILE ILE E . n 
E 1 140 ILE 140 113 113 ILE ILE E . n 
E 1 141 GLY 141 114 114 GLY GLY E . n 
E 1 142 ARG 142 115 115 ARG ARG E . n 
E 1 143 THR 143 116 116 THR THR E . n 
E 1 144 LEU 144 117 117 LEU LEU E . n 
E 1 145 VAL 145 118 118 VAL VAL E . n 
E 1 146 VAL 146 119 119 VAL VAL E . n 
E 1 147 HIS 147 120 120 HIS HIS E . n 
E 1 148 GLU 148 121 121 GLU GLU E . n 
E 1 149 LYS 149 122 122 LYS LYS E . n 
E 1 150 ALA 150 123 123 ALA ALA E . n 
E 1 151 ASP 151 124 124 ASP ASP E . n 
E 1 152 ASP 152 125 125 ASP ASP E . n 
E 1 153 LEU 153 126 126 LEU LEU E . n 
E 1 154 GLY 154 127 127 GLY GLY E . n 
E 1 155 LYS 155 128 128 LYS LYS E . n 
E 1 156 GLY 156 129 129 GLY GLY E . n 
E 1 157 GLY 157 130 130 GLY GLY E . n 
E 1 158 ASN 158 131 131 ASN ASN E . n 
E 1 159 GLU 159 132 132 GLU GLU E . n 
E 1 160 GLU 160 133 133 GLU GLU E . n 
E 1 161 SER 161 134 134 SER SER E . n 
E 1 162 THR 162 135 135 THR THR E . n 
E 1 163 LYS 163 136 136 LYS LYS E . n 
E 1 164 THR 164 137 137 THR THR E . n 
E 1 165 GLY 165 138 138 GLY GLY E . n 
E 1 166 ASN 166 139 139 ASN ASN E . n 
E 1 167 ALA 167 140 140 ALA ALA E . n 
E 1 168 GLY 168 141 141 GLY GLY E . n 
E 1 169 SER 169 142 142 SER SER E . n 
E 1 170 ARG 170 143 143 ARG ARG E . n 
E 1 171 LEU 171 144 144 LEU LEU E . n 
E 1 172 ALA 172 145 145 ALA ALA E . n 
E 1 173 CYS 173 146 146 CYS CYS E . n 
E 1 174 GLY 174 147 147 GLY GLY E . n 
E 1 175 VAL 175 148 148 VAL VAL E . n 
E 1 176 ILE 176 149 149 ILE ILE E . n 
E 1 177 GLY 177 150 150 GLY GLY E . n 
E 1 178 ILE 178 151 151 ILE ILE E . n 
E 1 179 ALA 179 152 152 ALA ALA E . n 
E 1 180 GLN 180 153 153 GLN GLN E . n 
F 1 1   MET 1   -26 ?   ?   ?   F . n 
F 1 2   LYS 2   -25 ?   ?   ?   F . n 
F 1 3   HIS 3   -24 ?   ?   ?   F . n 
F 1 4   HIS 4   -23 ?   ?   ?   F . n 
F 1 5   HIS 5   -22 ?   ?   ?   F . n 
F 1 6   HIS 6   -21 ?   ?   ?   F . n 
F 1 7   HIS 7   -20 ?   ?   ?   F . n 
F 1 8   HIS 8   -19 ?   ?   ?   F . n 
F 1 9   PRO 9   -18 ?   ?   ?   F . n 
F 1 10  MET 10  -17 ?   ?   ?   F . n 
F 1 11  SER 11  -16 ?   ?   ?   F . n 
F 1 12  ASP 12  -15 ?   ?   ?   F . n 
F 1 13  TYR 13  -14 ?   ?   ?   F . n 
F 1 14  ASP 14  -13 ?   ?   ?   F . n 
F 1 15  ILE 15  -12 ?   ?   ?   F . n 
F 1 16  PRO 16  -11 ?   ?   ?   F . n 
F 1 17  THR 17  -10 ?   ?   ?   F . n 
F 1 18  THR 18  -9  ?   ?   ?   F . n 
F 1 19  GLU 19  -8  ?   ?   ?   F . n 
F 1 20  ASN 20  -7  ?   ?   ?   F . n 
F 1 21  LEU 21  -6  ?   ?   ?   F . n 
F 1 22  TYR 22  -5  ?   ?   ?   F . n 
F 1 23  PHE 23  -4  ?   ?   ?   F . n 
F 1 24  GLN 24  -3  ?   ?   ?   F . n 
F 1 25  GLY 25  -2  ?   ?   ?   F . n 
F 1 26  ALA 26  -1  -1  ALA ALA F . n 
F 1 27  MET 27  0   0   MET ALA F . n 
F 1 28  ALA 28  1   1   ALA ALA F . n 
F 1 29  THR 29  2   2   THR THR F . n 
F 1 30  LYS 30  3   3   LYS LYS F . n 
F 1 31  ALA 31  4   4   ALA ALA F . n 
F 1 32  VAL 32  5   5   VAL VAL F . n 
F 1 33  CYS 33  6   6   CYS CYS F . n 
F 1 34  VAL 34  7   7   VAL VAL F . n 
F 1 35  LEU 35  8   8   LEU LEU F . n 
F 1 36  LYS 36  9   9   LYS LYS F . n 
F 1 37  GLY 37  10  10  GLY GLY F . n 
F 1 38  ASP 38  11  11  ASP ASP F . n 
F 1 39  GLY 39  12  12  GLY GLY F . n 
F 1 40  PRO 40  13  13  PRO PRO F . n 
F 1 41  VAL 41  14  14  VAL VAL F . n 
F 1 42  GLN 42  15  15  GLN GLN F . n 
F 1 43  GLY 43  16  16  GLY GLY F . n 
F 1 44  ILE 44  17  17  ILE ILE F . n 
F 1 45  ILE 45  18  18  ILE ILE F . n 
F 1 46  ASN 46  19  19  ASN ASN F . n 
F 1 47  PHE 47  20  20  PHE PHE F . n 
F 1 48  GLU 48  21  21  GLU GLU F . n 
F 1 49  GLN 49  22  22  GLN GLN F . n 
F 1 50  LYS 50  23  23  LYS LYS F . n 
F 1 51  GLU 51  24  24  GLU GLU F . n 
F 1 52  SER 52  25  25  SER SER F . n 
F 1 53  ASN 53  26  26  ASN ASN F . n 
F 1 54  GLY 54  27  27  GLY GLY F . n 
F 1 55  PRO 55  28  28  PRO PRO F . n 
F 1 56  VAL 56  29  29  VAL VAL F . n 
F 1 57  LYS 57  30  30  LYS LYS F . n 
F 1 58  VAL 58  31  31  VAL VAL F . n 
F 1 59  TRP 59  32  32  TRP TRP F . n 
F 1 60  GLY 60  33  33  GLY GLY F . n 
F 1 61  SER 61  34  34  SER SER F . n 
F 1 62  ILE 62  35  35  ILE ILE F . n 
F 1 63  LYS 63  36  36  LYS LYS F . n 
F 1 64  GLY 64  37  37  GLY GLY F . n 
F 1 65  LEU 65  38  38  LEU LEU F . n 
F 1 66  THR 66  39  39  THR THR F . n 
F 1 67  GLU 67  40  40  GLU GLU F . n 
F 1 68  GLY 68  41  41  GLY GLY F . n 
F 1 69  LEU 69  42  42  LEU LEU F . n 
F 1 70  HIS 70  43  43  HIS HIS F . n 
F 1 71  GLY 71  44  44  GLY GLY F . n 
F 1 72  PHE 72  45  45  PHE PHE F . n 
F 1 73  HIS 73  46  46  HIS HIS F . n 
F 1 74  VAL 74  47  47  VAL VAL F . n 
F 1 75  HIS 75  48  48  HIS HIS F . n 
F 1 76  GLU 76  49  49  GLU GLU F . n 
F 1 77  PHE 77  50  50  PHE PHE F . n 
F 1 78  GLY 78  51  51  GLY GLY F . n 
F 1 79  ASP 79  52  52  ASP ASP F . n 
F 1 80  ASN 80  53  53  ASN ASN F . n 
F 1 81  THR 81  54  54  THR THR F . n 
F 1 82  ALA 82  55  55  ALA ALA F . n 
F 1 83  GLY 83  56  56  GLY GLY F . n 
F 1 84  CYS 84  57  57  CYS CYS F . n 
F 1 85  THR 85  58  58  THR THR F . n 
F 1 86  SER 86  59  59  SER SER F . n 
F 1 87  ALA 87  60  60  ALA ALA F . n 
F 1 88  GLY 88  61  61  GLY GLY F . n 
F 1 89  PRO 89  62  62  PRO PRO F . n 
F 1 90  HIS 90  63  63  HIS HIS F . n 
F 1 91  PHE 91  64  64  PHE PHE F . n 
F 1 92  ASN 92  65  65  ASN ASN F . n 
F 1 93  PRO 93  66  66  PRO PRO F . n 
F 1 94  LEU 94  67  67  LEU LEU F . n 
F 1 95  SER 95  68  68  SER SER F . n 
F 1 96  ARG 96  69  69  ARG ARG F . n 
F 1 97  LYS 97  70  70  LYS LYS F . n 
F 1 98  HIS 98  71  71  HIS HIS F . n 
F 1 99  GLY 99  72  72  GLY GLY F . n 
F 1 100 GLY 100 73  73  GLY GLY F . n 
F 1 101 PRO 101 74  74  PRO PRO F . n 
F 1 102 LYS 102 75  75  LYS LYS F . n 
F 1 103 ASP 103 76  76  ASP ASP F . n 
F 1 104 GLU 104 77  77  GLU GLU F . n 
F 1 105 GLU 105 78  78  GLU GLU F . n 
F 1 106 ARG 106 79  79  ARG ARG F . n 
F 1 107 HIS 107 80  80  HIS HIS F . n 
F 1 108 VAL 108 81  81  VAL VAL F . n 
F 1 109 GLY 109 82  82  GLY GLY F . n 
F 1 110 ASP 110 83  83  ASP ASP F . n 
F 1 111 LEU 111 84  84  LEU LEU F . n 
F 1 112 GLY 112 85  85  GLY GLY F . n 
F 1 113 ASN 113 86  86  ASN ASN F . n 
F 1 114 VAL 114 87  87  VAL VAL F . n 
F 1 115 THR 115 88  88  THR THR F . n 
F 1 116 ALA 116 89  89  ALA ALA F . n 
F 1 117 ASP 117 90  90  ASP ASP F . n 
F 1 118 LYS 118 91  91  LYS LYS F . n 
F 1 119 ASP 119 92  92  ASP ASP F . n 
F 1 120 GLY 120 93  93  GLY GLY F . n 
F 1 121 VAL 121 94  94  VAL VAL F . n 
F 1 122 ALA 122 95  95  ALA ALA F . n 
F 1 123 ASP 123 96  96  ASP ASP F . n 
F 1 124 VAL 124 97  97  VAL VAL F . n 
F 1 125 SER 125 98  98  SER SER F . n 
F 1 126 ILE 126 99  99  ILE ILE F . n 
F 1 127 GLU 127 100 100 GLU GLU F . n 
F 1 128 ASP 128 101 101 ASP ASP F . n 
F 1 129 SER 129 102 102 SER SER F . n 
F 1 130 VAL 130 103 103 VAL VAL F . n 
F 1 131 ILE 131 104 104 ILE ILE F . n 
F 1 132 SER 132 105 105 SER SER F . n 
F 1 133 LEU 133 106 106 LEU LEU F . n 
F 1 134 SER 134 107 107 SER SER F . n 
F 1 135 GLY 135 108 108 GLY GLY F . n 
F 1 136 ASP 136 109 109 ASP ASP F . n 
F 1 137 HIS 137 110 110 HIS HIS F . n 
F 1 138 CYS 138 111 111 CYS CYS F . n 
F 1 139 ILE 139 112 112 ILE ILE F . n 
F 1 140 ILE 140 113 113 ILE ILE F . n 
F 1 141 GLY 141 114 114 GLY GLY F . n 
F 1 142 ARG 142 115 115 ARG ARG F . n 
F 1 143 THR 143 116 116 THR THR F . n 
F 1 144 LEU 144 117 117 LEU LEU F . n 
F 1 145 VAL 145 118 118 VAL VAL F . n 
F 1 146 VAL 146 119 119 VAL VAL F . n 
F 1 147 HIS 147 120 120 HIS HIS F . n 
F 1 148 GLU 148 121 121 GLU GLU F . n 
F 1 149 LYS 149 122 122 LYS LYS F . n 
F 1 150 ALA 150 123 123 ALA ALA F . n 
F 1 151 ASP 151 124 124 ASP ASP F . n 
F 1 152 ASP 152 125 125 ASP ASP F . n 
F 1 153 LEU 153 126 126 LEU LEU F . n 
F 1 154 GLY 154 127 127 GLY GLY F . n 
F 1 155 LYS 155 128 128 LYS LYS F . n 
F 1 156 GLY 156 129 129 GLY GLY F . n 
F 1 157 GLY 157 130 130 GLY GLY F . n 
F 1 158 ASN 158 131 131 ASN ASN F . n 
F 1 159 GLU 159 132 132 GLU GLU F . n 
F 1 160 GLU 160 133 133 GLU GLU F . n 
F 1 161 SER 161 134 134 SER SER F . n 
F 1 162 THR 162 135 135 THR THR F . n 
F 1 163 LYS 163 136 136 LYS LYS F . n 
F 1 164 THR 164 137 137 THR THR F . n 
F 1 165 GLY 165 138 138 GLY GLY F . n 
F 1 166 ASN 166 139 139 ASN ASN F . n 
F 1 167 ALA 167 140 140 ALA ALA F . n 
F 1 168 GLY 168 141 141 GLY GLY F . n 
F 1 169 SER 169 142 142 SER SER F . n 
F 1 170 ARG 170 143 143 ARG ARG F . n 
F 1 171 LEU 171 144 144 LEU LEU F . n 
F 1 172 ALA 172 145 145 ALA ALA F . n 
F 1 173 CYS 173 146 146 CYS CYS F . n 
F 1 174 GLY 174 147 147 GLY GLY F . n 
F 1 175 VAL 175 148 148 VAL VAL F . n 
F 1 176 ILE 176 149 149 ILE ILE F . n 
F 1 177 GLY 177 150 150 GLY GLY F . n 
F 1 178 ILE 178 151 151 ILE ILE F . n 
F 1 179 ALA 179 152 152 ALA ALA F . n 
F 1 180 GLN 180 153 153 GLN GLN F . n 
G 1 1   MET 1   -26 ?   ?   ?   G . n 
G 1 2   LYS 2   -25 ?   ?   ?   G . n 
G 1 3   HIS 3   -24 ?   ?   ?   G . n 
G 1 4   HIS 4   -23 ?   ?   ?   G . n 
G 1 5   HIS 5   -22 ?   ?   ?   G . n 
G 1 6   HIS 6   -21 ?   ?   ?   G . n 
G 1 7   HIS 7   -20 ?   ?   ?   G . n 
G 1 8   HIS 8   -19 ?   ?   ?   G . n 
G 1 9   PRO 9   -18 ?   ?   ?   G . n 
G 1 10  MET 10  -17 ?   ?   ?   G . n 
G 1 11  SER 11  -16 ?   ?   ?   G . n 
G 1 12  ASP 12  -15 ?   ?   ?   G . n 
G 1 13  TYR 13  -14 ?   ?   ?   G . n 
G 1 14  ASP 14  -13 ?   ?   ?   G . n 
G 1 15  ILE 15  -12 ?   ?   ?   G . n 
G 1 16  PRO 16  -11 ?   ?   ?   G . n 
G 1 17  THR 17  -10 ?   ?   ?   G . n 
G 1 18  THR 18  -9  ?   ?   ?   G . n 
G 1 19  GLU 19  -8  ?   ?   ?   G . n 
G 1 20  ASN 20  -7  ?   ?   ?   G . n 
G 1 21  LEU 21  -6  ?   ?   ?   G . n 
G 1 22  TYR 22  -5  ?   ?   ?   G . n 
G 1 23  PHE 23  -4  ?   ?   ?   G . n 
G 1 24  GLN 24  -3  ?   ?   ?   G . n 
G 1 25  GLY 25  -2  ?   ?   ?   G . n 
G 1 26  ALA 26  -1  ?   ?   ?   G . n 
G 1 27  MET 27  0   ?   ?   ?   G . n 
G 1 28  ALA 28  1   1   ALA ALA G . n 
G 1 29  THR 29  2   2   THR THR G . n 
G 1 30  LYS 30  3   3   LYS LYS G . n 
G 1 31  ALA 31  4   4   ALA ALA G . n 
G 1 32  VAL 32  5   5   VAL VAL G . n 
G 1 33  CYS 33  6   6   CYS CYS G . n 
G 1 34  VAL 34  7   7   VAL VAL G . n 
G 1 35  LEU 35  8   8   LEU LEU G . n 
G 1 36  LYS 36  9   9   LYS LYS G . n 
G 1 37  GLY 37  10  10  GLY GLY G . n 
G 1 38  ASP 38  11  11  ASP ASP G . n 
G 1 39  GLY 39  12  12  GLY GLY G . n 
G 1 40  PRO 40  13  13  PRO PRO G . n 
G 1 41  VAL 41  14  14  VAL VAL G . n 
G 1 42  GLN 42  15  15  GLN GLN G . n 
G 1 43  GLY 43  16  16  GLY GLY G . n 
G 1 44  ILE 44  17  17  ILE ILE G . n 
G 1 45  ILE 45  18  18  ILE ILE G . n 
G 1 46  ASN 46  19  19  ASN ASN G . n 
G 1 47  PHE 47  20  20  PHE PHE G . n 
G 1 48  GLU 48  21  21  GLU GLU G . n 
G 1 49  GLN 49  22  22  GLN GLN G . n 
G 1 50  LYS 50  23  23  LYS LYS G . n 
G 1 51  GLU 51  24  24  GLU GLU G . n 
G 1 52  SER 52  25  25  SER SER G . n 
G 1 53  ASN 53  26  26  ASN ASN G . n 
G 1 54  GLY 54  27  27  GLY GLY G . n 
G 1 55  PRO 55  28  28  PRO PRO G . n 
G 1 56  VAL 56  29  29  VAL VAL G . n 
G 1 57  LYS 57  30  30  LYS LYS G . n 
G 1 58  VAL 58  31  31  VAL VAL G . n 
G 1 59  TRP 59  32  32  TRP TRP G . n 
G 1 60  GLY 60  33  33  GLY GLY G . n 
G 1 61  SER 61  34  34  SER SER G . n 
G 1 62  ILE 62  35  35  ILE ILE G . n 
G 1 63  LYS 63  36  36  LYS LYS G . n 
G 1 64  GLY 64  37  37  GLY GLY G . n 
G 1 65  LEU 65  38  38  LEU LEU G . n 
G 1 66  THR 66  39  39  THR THR G . n 
G 1 67  GLU 67  40  40  GLU GLU G . n 
G 1 68  GLY 68  41  41  GLY GLY G . n 
G 1 69  LEU 69  42  42  LEU LEU G . n 
G 1 70  HIS 70  43  43  HIS HIS G . n 
G 1 71  GLY 71  44  44  GLY GLY G . n 
G 1 72  PHE 72  45  45  PHE PHE G . n 
G 1 73  HIS 73  46  46  HIS HIS G . n 
G 1 74  VAL 74  47  47  VAL VAL G . n 
G 1 75  HIS 75  48  48  HIS HIS G . n 
G 1 76  GLU 76  49  49  GLU GLU G . n 
G 1 77  PHE 77  50  50  PHE PHE G . n 
G 1 78  GLY 78  51  51  GLY GLY G . n 
G 1 79  ASP 79  52  52  ASP ASP G . n 
G 1 80  ASN 80  53  53  ASN ASN G . n 
G 1 81  THR 81  54  54  THR THR G . n 
G 1 82  ALA 82  55  55  ALA ALA G . n 
G 1 83  GLY 83  56  56  GLY GLY G . n 
G 1 84  CYS 84  57  57  CYS CYS G . n 
G 1 85  THR 85  58  58  THR THR G . n 
G 1 86  SER 86  59  59  SER SER G . n 
G 1 87  ALA 87  60  60  ALA ALA G . n 
G 1 88  GLY 88  61  61  GLY GLY G . n 
G 1 89  PRO 89  62  62  PRO PRO G . n 
G 1 90  HIS 90  63  63  HIS HIS G . n 
G 1 91  PHE 91  64  64  PHE PHE G . n 
G 1 92  ASN 92  65  65  ASN ASN G . n 
G 1 93  PRO 93  66  66  PRO PRO G . n 
G 1 94  LEU 94  67  67  LEU LEU G . n 
G 1 95  SER 95  68  68  SER SER G . n 
G 1 96  ARG 96  69  69  ARG ARG G . n 
G 1 97  LYS 97  70  70  LYS LYS G . n 
G 1 98  HIS 98  71  71  HIS HIS G . n 
G 1 99  GLY 99  72  72  GLY GLY G . n 
G 1 100 GLY 100 73  73  GLY GLY G . n 
G 1 101 PRO 101 74  74  PRO PRO G . n 
G 1 102 LYS 102 75  75  LYS LYS G . n 
G 1 103 ASP 103 76  76  ASP ASP G . n 
G 1 104 GLU 104 77  77  GLU GLU G . n 
G 1 105 GLU 105 78  78  GLU GLU G . n 
G 1 106 ARG 106 79  79  ARG ARG G . n 
G 1 107 HIS 107 80  80  HIS HIS G . n 
G 1 108 VAL 108 81  81  VAL VAL G . n 
G 1 109 GLY 109 82  82  GLY GLY G . n 
G 1 110 ASP 110 83  83  ASP ASP G . n 
G 1 111 LEU 111 84  84  LEU LEU G . n 
G 1 112 GLY 112 85  85  GLY GLY G . n 
G 1 113 ASN 113 86  86  ASN ASN G . n 
G 1 114 VAL 114 87  87  VAL VAL G . n 
G 1 115 THR 115 88  88  THR THR G . n 
G 1 116 ALA 116 89  89  ALA ALA G . n 
G 1 117 ASP 117 90  90  ASP ASP G . n 
G 1 118 LYS 118 91  91  LYS LYS G . n 
G 1 119 ASP 119 92  92  ASP ASP G . n 
G 1 120 GLY 120 93  93  GLY GLY G . n 
G 1 121 VAL 121 94  94  VAL VAL G . n 
G 1 122 ALA 122 95  95  ALA ALA G . n 
G 1 123 ASP 123 96  96  ASP ASP G . n 
G 1 124 VAL 124 97  97  VAL VAL G . n 
G 1 125 SER 125 98  98  SER SER G . n 
G 1 126 ILE 126 99  99  ILE ILE G . n 
G 1 127 GLU 127 100 100 GLU GLU G . n 
G 1 128 ASP 128 101 101 ASP ASP G . n 
G 1 129 SER 129 102 102 SER SER G . n 
G 1 130 VAL 130 103 103 VAL VAL G . n 
G 1 131 ILE 131 104 104 ILE ILE G . n 
G 1 132 SER 132 105 105 SER SER G . n 
G 1 133 LEU 133 106 106 LEU LEU G . n 
G 1 134 SER 134 107 107 SER SER G . n 
G 1 135 GLY 135 108 108 GLY GLY G . n 
G 1 136 ASP 136 109 109 ASP ASP G . n 
G 1 137 HIS 137 110 110 HIS HIS G . n 
G 1 138 CYS 138 111 111 CYS CYS G . n 
G 1 139 ILE 139 112 112 ILE ILE G . n 
G 1 140 ILE 140 113 113 ILE ILE G . n 
G 1 141 GLY 141 114 114 GLY GLY G . n 
G 1 142 ARG 142 115 115 ARG ARG G . n 
G 1 143 THR 143 116 116 THR THR G . n 
G 1 144 LEU 144 117 117 LEU LEU G . n 
G 1 145 VAL 145 118 118 VAL VAL G . n 
G 1 146 VAL 146 119 119 VAL VAL G . n 
G 1 147 HIS 147 120 120 HIS HIS G . n 
G 1 148 GLU 148 121 121 GLU GLU G . n 
G 1 149 LYS 149 122 122 LYS LYS G . n 
G 1 150 ALA 150 123 123 ALA ALA G . n 
G 1 151 ASP 151 124 124 ASP ASP G . n 
G 1 152 ASP 152 125 125 ASP ASP G . n 
G 1 153 LEU 153 126 126 LEU LEU G . n 
G 1 154 GLY 154 127 127 GLY GLY G . n 
G 1 155 LYS 155 128 128 LYS LYS G . n 
G 1 156 GLY 156 129 129 GLY GLY G . n 
G 1 157 GLY 157 130 130 GLY GLY G . n 
G 1 158 ASN 158 131 131 ASN ASN G . n 
G 1 159 GLU 159 132 132 GLU GLU G . n 
G 1 160 GLU 160 133 133 GLU GLU G . n 
G 1 161 SER 161 134 134 SER SER G . n 
G 1 162 THR 162 135 135 THR THR G . n 
G 1 163 LYS 163 136 136 LYS LYS G . n 
G 1 164 THR 164 137 137 THR THR G . n 
G 1 165 GLY 165 138 138 GLY GLY G . n 
G 1 166 ASN 166 139 139 ASN ASN G . n 
G 1 167 ALA 167 140 140 ALA ALA G . n 
G 1 168 GLY 168 141 141 GLY GLY G . n 
G 1 169 SER 169 142 142 SER SER G . n 
G 1 170 ARG 170 143 143 ARG ARG G . n 
G 1 171 LEU 171 144 144 LEU LEU G . n 
G 1 172 ALA 172 145 145 ALA ALA G . n 
G 1 173 CYS 173 146 146 CYS CYS G . n 
G 1 174 GLY 174 147 147 GLY GLY G . n 
G 1 175 VAL 175 148 148 VAL VAL G . n 
G 1 176 ILE 176 149 149 ILE ILE G . n 
G 1 177 GLY 177 150 150 GLY GLY G . n 
G 1 178 ILE 178 151 151 ILE ILE G . n 
G 1 179 ALA 179 152 152 ALA ALA G . n 
G 1 180 GLN 180 153 153 GLN GLN G . n 
H 1 1   MET 1   -26 ?   ?   ?   H . n 
H 1 2   LYS 2   -25 ?   ?   ?   H . n 
H 1 3   HIS 3   -24 ?   ?   ?   H . n 
H 1 4   HIS 4   -23 ?   ?   ?   H . n 
H 1 5   HIS 5   -22 ?   ?   ?   H . n 
H 1 6   HIS 6   -21 ?   ?   ?   H . n 
H 1 7   HIS 7   -20 ?   ?   ?   H . n 
H 1 8   HIS 8   -19 ?   ?   ?   H . n 
H 1 9   PRO 9   -18 ?   ?   ?   H . n 
H 1 10  MET 10  -17 ?   ?   ?   H . n 
H 1 11  SER 11  -16 ?   ?   ?   H . n 
H 1 12  ASP 12  -15 ?   ?   ?   H . n 
H 1 13  TYR 13  -14 ?   ?   ?   H . n 
H 1 14  ASP 14  -13 ?   ?   ?   H . n 
H 1 15  ILE 15  -12 ?   ?   ?   H . n 
H 1 16  PRO 16  -11 ?   ?   ?   H . n 
H 1 17  THR 17  -10 ?   ?   ?   H . n 
H 1 18  THR 18  -9  ?   ?   ?   H . n 
H 1 19  GLU 19  -8  ?   ?   ?   H . n 
H 1 20  ASN 20  -7  ?   ?   ?   H . n 
H 1 21  LEU 21  -6  ?   ?   ?   H . n 
H 1 22  TYR 22  -5  ?   ?   ?   H . n 
H 1 23  PHE 23  -4  ?   ?   ?   H . n 
H 1 24  GLN 24  -3  ?   ?   ?   H . n 
H 1 25  GLY 25  -2  ?   ?   ?   H . n 
H 1 26  ALA 26  -1  ?   ?   ?   H . n 
H 1 27  MET 27  0   0   MET ALA H . n 
H 1 28  ALA 28  1   1   ALA ALA H . n 
H 1 29  THR 29  2   2   THR THR H . n 
H 1 30  LYS 30  3   3   LYS LYS H . n 
H 1 31  ALA 31  4   4   ALA ALA H . n 
H 1 32  VAL 32  5   5   VAL VAL H . n 
H 1 33  CYS 33  6   6   CYS CYS H . n 
H 1 34  VAL 34  7   7   VAL VAL H . n 
H 1 35  LEU 35  8   8   LEU LEU H . n 
H 1 36  LYS 36  9   9   LYS LYS H . n 
H 1 37  GLY 37  10  10  GLY GLY H . n 
H 1 38  ASP 38  11  11  ASP ASP H . n 
H 1 39  GLY 39  12  12  GLY GLY H . n 
H 1 40  PRO 40  13  13  PRO PRO H . n 
H 1 41  VAL 41  14  14  VAL VAL H . n 
H 1 42  GLN 42  15  15  GLN GLN H . n 
H 1 43  GLY 43  16  16  GLY GLY H . n 
H 1 44  ILE 44  17  17  ILE ILE H . n 
H 1 45  ILE 45  18  18  ILE ILE H . n 
H 1 46  ASN 46  19  19  ASN ASN H . n 
H 1 47  PHE 47  20  20  PHE PHE H . n 
H 1 48  GLU 48  21  21  GLU GLU H . n 
H 1 49  GLN 49  22  22  GLN GLN H . n 
H 1 50  LYS 50  23  23  LYS LYS H . n 
H 1 51  GLU 51  24  24  GLU GLU H . n 
H 1 52  SER 52  25  25  SER SER H . n 
H 1 53  ASN 53  26  26  ASN ASN H . n 
H 1 54  GLY 54  27  27  GLY GLY H . n 
H 1 55  PRO 55  28  28  PRO PRO H . n 
H 1 56  VAL 56  29  29  VAL VAL H . n 
H 1 57  LYS 57  30  30  LYS LYS H . n 
H 1 58  VAL 58  31  31  VAL VAL H . n 
H 1 59  TRP 59  32  32  TRP TRP H . n 
H 1 60  GLY 60  33  33  GLY GLY H . n 
H 1 61  SER 61  34  34  SER SER H . n 
H 1 62  ILE 62  35  35  ILE ILE H . n 
H 1 63  LYS 63  36  36  LYS LYS H . n 
H 1 64  GLY 64  37  37  GLY GLY H . n 
H 1 65  LEU 65  38  38  LEU LEU H . n 
H 1 66  THR 66  39  39  THR THR H . n 
H 1 67  GLU 67  40  40  GLU GLU H . n 
H 1 68  GLY 68  41  41  GLY GLY H . n 
H 1 69  LEU 69  42  42  LEU LEU H . n 
H 1 70  HIS 70  43  43  HIS HIS H . n 
H 1 71  GLY 71  44  44  GLY GLY H . n 
H 1 72  PHE 72  45  45  PHE PHE H . n 
H 1 73  HIS 73  46  46  HIS HIS H . n 
H 1 74  VAL 74  47  47  VAL VAL H . n 
H 1 75  HIS 75  48  48  HIS HIS H . n 
H 1 76  GLU 76  49  49  GLU GLU H . n 
H 1 77  PHE 77  50  50  PHE PHE H . n 
H 1 78  GLY 78  51  51  GLY GLY H . n 
H 1 79  ASP 79  52  52  ASP ASP H . n 
H 1 80  ASN 80  53  53  ASN ASN H . n 
H 1 81  THR 81  54  54  THR THR H . n 
H 1 82  ALA 82  55  55  ALA ALA H . n 
H 1 83  GLY 83  56  56  GLY GLY H . n 
H 1 84  CYS 84  57  57  CYS CYS H . n 
H 1 85  THR 85  58  58  THR THR H . n 
H 1 86  SER 86  59  59  SER SER H . n 
H 1 87  ALA 87  60  60  ALA ALA H . n 
H 1 88  GLY 88  61  61  GLY GLY H . n 
H 1 89  PRO 89  62  62  PRO PRO H . n 
H 1 90  HIS 90  63  63  HIS HIS H . n 
H 1 91  PHE 91  64  64  PHE PHE H . n 
H 1 92  ASN 92  65  65  ASN ASN H . n 
H 1 93  PRO 93  66  66  PRO PRO H . n 
H 1 94  LEU 94  67  67  LEU LEU H . n 
H 1 95  SER 95  68  68  SER SER H . n 
H 1 96  ARG 96  69  69  ARG ARG H . n 
H 1 97  LYS 97  70  70  LYS LYS H . n 
H 1 98  HIS 98  71  71  HIS HIS H . n 
H 1 99  GLY 99  72  72  GLY GLY H . n 
H 1 100 GLY 100 73  73  GLY GLY H . n 
H 1 101 PRO 101 74  74  PRO PRO H . n 
H 1 102 LYS 102 75  75  LYS LYS H . n 
H 1 103 ASP 103 76  76  ASP ASP H . n 
H 1 104 GLU 104 77  77  GLU GLU H . n 
H 1 105 GLU 105 78  78  GLU GLU H . n 
H 1 106 ARG 106 79  79  ARG ARG H . n 
H 1 107 HIS 107 80  80  HIS HIS H . n 
H 1 108 VAL 108 81  81  VAL VAL H . n 
H 1 109 GLY 109 82  82  GLY GLY H . n 
H 1 110 ASP 110 83  83  ASP ASP H . n 
H 1 111 LEU 111 84  84  LEU LEU H . n 
H 1 112 GLY 112 85  85  GLY GLY H . n 
H 1 113 ASN 113 86  86  ASN ASN H . n 
H 1 114 VAL 114 87  87  VAL VAL H . n 
H 1 115 THR 115 88  88  THR THR H . n 
H 1 116 ALA 116 89  89  ALA ALA H . n 
H 1 117 ASP 117 90  90  ASP ASP H . n 
H 1 118 LYS 118 91  91  LYS LYS H . n 
H 1 119 ASP 119 92  92  ASP ASP H . n 
H 1 120 GLY 120 93  93  GLY GLY H . n 
H 1 121 VAL 121 94  94  VAL VAL H . n 
H 1 122 ALA 122 95  95  ALA ALA H . n 
H 1 123 ASP 123 96  96  ASP ASP H . n 
H 1 124 VAL 124 97  97  VAL VAL H . n 
H 1 125 SER 125 98  98  SER SER H . n 
H 1 126 ILE 126 99  99  ILE ILE H . n 
H 1 127 GLU 127 100 100 GLU GLU H . n 
H 1 128 ASP 128 101 101 ASP ASP H . n 
H 1 129 SER 129 102 102 SER SER H . n 
H 1 130 VAL 130 103 103 VAL VAL H . n 
H 1 131 ILE 131 104 104 ILE ILE H . n 
H 1 132 SER 132 105 105 SER SER H . n 
H 1 133 LEU 133 106 106 LEU LEU H . n 
H 1 134 SER 134 107 107 SER SER H . n 
H 1 135 GLY 135 108 108 GLY GLY H . n 
H 1 136 ASP 136 109 109 ASP ASP H . n 
H 1 137 HIS 137 110 110 HIS HIS H . n 
H 1 138 CYS 138 111 111 CYS CYS H . n 
H 1 139 ILE 139 112 112 ILE ILE H . n 
H 1 140 ILE 140 113 113 ILE ILE H . n 
H 1 141 GLY 141 114 114 GLY GLY H . n 
H 1 142 ARG 142 115 115 ARG ARG H . n 
H 1 143 THR 143 116 116 THR THR H . n 
H 1 144 LEU 144 117 117 LEU LEU H . n 
H 1 145 VAL 145 118 118 VAL VAL H . n 
H 1 146 VAL 146 119 119 VAL VAL H . n 
H 1 147 HIS 147 120 120 HIS HIS H . n 
H 1 148 GLU 148 121 121 GLU GLU H . n 
H 1 149 LYS 149 122 122 LYS LYS H . n 
H 1 150 ALA 150 123 123 ALA ALA H . n 
H 1 151 ASP 151 124 124 ASP ASP H . n 
H 1 152 ASP 152 125 125 ASP ASP H . n 
H 1 153 LEU 153 126 126 LEU LEU H . n 
H 1 154 GLY 154 127 127 GLY GLY H . n 
H 1 155 LYS 155 128 128 LYS LYS H . n 
H 1 156 GLY 156 129 129 GLY GLY H . n 
H 1 157 GLY 157 130 130 GLY GLY H . n 
H 1 158 ASN 158 131 131 ASN ASN H . n 
H 1 159 GLU 159 132 132 GLU GLU H . n 
H 1 160 GLU 160 133 133 GLU GLU H . n 
H 1 161 SER 161 134 134 SER SER H . n 
H 1 162 THR 162 135 135 THR THR H . n 
H 1 163 LYS 163 136 136 LYS LYS H . n 
H 1 164 THR 164 137 137 THR THR H . n 
H 1 165 GLY 165 138 138 GLY GLY H . n 
H 1 166 ASN 166 139 139 ASN ASN H . n 
H 1 167 ALA 167 140 140 ALA ALA H . n 
H 1 168 GLY 168 141 141 GLY GLY H . n 
H 1 169 SER 169 142 142 SER SER H . n 
H 1 170 ARG 170 143 143 ARG ARG H . n 
H 1 171 LEU 171 144 144 LEU LEU H . n 
H 1 172 ALA 172 145 145 ALA ALA H . n 
H 1 173 CYS 173 146 146 CYS CYS H . n 
H 1 174 GLY 174 147 147 GLY GLY H . n 
H 1 175 VAL 175 148 148 VAL VAL H . n 
H 1 176 ILE 176 149 149 ILE ILE H . n 
H 1 177 GLY 177 150 150 GLY GLY H . n 
H 1 178 ILE 178 151 151 ILE ILE H . n 
H 1 179 ALA 179 152 152 ALA ALA H . n 
H 1 180 GLN 180 153 153 GLN GLN H . n 
I 1 1   MET 1   -26 ?   ?   ?   I . n 
I 1 2   LYS 2   -25 ?   ?   ?   I . n 
I 1 3   HIS 3   -24 ?   ?   ?   I . n 
I 1 4   HIS 4   -23 ?   ?   ?   I . n 
I 1 5   HIS 5   -22 ?   ?   ?   I . n 
I 1 6   HIS 6   -21 ?   ?   ?   I . n 
I 1 7   HIS 7   -20 ?   ?   ?   I . n 
I 1 8   HIS 8   -19 ?   ?   ?   I . n 
I 1 9   PRO 9   -18 ?   ?   ?   I . n 
I 1 10  MET 10  -17 ?   ?   ?   I . n 
I 1 11  SER 11  -16 ?   ?   ?   I . n 
I 1 12  ASP 12  -15 ?   ?   ?   I . n 
I 1 13  TYR 13  -14 ?   ?   ?   I . n 
I 1 14  ASP 14  -13 ?   ?   ?   I . n 
I 1 15  ILE 15  -12 ?   ?   ?   I . n 
I 1 16  PRO 16  -11 ?   ?   ?   I . n 
I 1 17  THR 17  -10 ?   ?   ?   I . n 
I 1 18  THR 18  -9  ?   ?   ?   I . n 
I 1 19  GLU 19  -8  ?   ?   ?   I . n 
I 1 20  ASN 20  -7  ?   ?   ?   I . n 
I 1 21  LEU 21  -6  ?   ?   ?   I . n 
I 1 22  TYR 22  -5  ?   ?   ?   I . n 
I 1 23  PHE 23  -4  ?   ?   ?   I . n 
I 1 24  GLN 24  -3  ?   ?   ?   I . n 
I 1 25  GLY 25  -2  ?   ?   ?   I . n 
I 1 26  ALA 26  -1  ?   ?   ?   I . n 
I 1 27  MET 27  0   ?   ?   ?   I . n 
I 1 28  ALA 28  1   1   ALA ALA I . n 
I 1 29  THR 29  2   2   THR THR I . n 
I 1 30  LYS 30  3   3   LYS LYS I . n 
I 1 31  ALA 31  4   4   ALA ALA I . n 
I 1 32  VAL 32  5   5   VAL VAL I . n 
I 1 33  CYS 33  6   6   CYS CYS I . n 
I 1 34  VAL 34  7   7   VAL VAL I . n 
I 1 35  LEU 35  8   8   LEU LEU I . n 
I 1 36  LYS 36  9   9   LYS LYS I . n 
I 1 37  GLY 37  10  10  GLY GLY I . n 
I 1 38  ASP 38  11  11  ASP ASP I . n 
I 1 39  GLY 39  12  12  GLY GLY I . n 
I 1 40  PRO 40  13  13  PRO PRO I . n 
I 1 41  VAL 41  14  14  VAL VAL I . n 
I 1 42  GLN 42  15  15  GLN GLN I . n 
I 1 43  GLY 43  16  16  GLY GLY I . n 
I 1 44  ILE 44  17  17  ILE ILE I . n 
I 1 45  ILE 45  18  18  ILE ILE I . n 
I 1 46  ASN 46  19  19  ASN ASN I . n 
I 1 47  PHE 47  20  20  PHE PHE I . n 
I 1 48  GLU 48  21  21  GLU GLU I . n 
I 1 49  GLN 49  22  22  GLN GLN I . n 
I 1 50  LYS 50  23  23  LYS LYS I . n 
I 1 51  GLU 51  24  24  GLU GLU I . n 
I 1 52  SER 52  25  25  SER SER I . n 
I 1 53  ASN 53  26  26  ASN ASN I . n 
I 1 54  GLY 54  27  27  GLY GLY I . n 
I 1 55  PRO 55  28  28  PRO PRO I . n 
I 1 56  VAL 56  29  29  VAL VAL I . n 
I 1 57  LYS 57  30  30  LYS LYS I . n 
I 1 58  VAL 58  31  31  VAL VAL I . n 
I 1 59  TRP 59  32  32  TRP TRP I . n 
I 1 60  GLY 60  33  33  GLY GLY I . n 
I 1 61  SER 61  34  34  SER SER I . n 
I 1 62  ILE 62  35  35  ILE ILE I . n 
I 1 63  LYS 63  36  36  LYS LYS I . n 
I 1 64  GLY 64  37  37  GLY GLY I . n 
I 1 65  LEU 65  38  38  LEU LEU I . n 
I 1 66  THR 66  39  39  THR THR I . n 
I 1 67  GLU 67  40  40  GLU GLU I . n 
I 1 68  GLY 68  41  41  GLY GLY I . n 
I 1 69  LEU 69  42  42  LEU LEU I . n 
I 1 70  HIS 70  43  43  HIS HIS I . n 
I 1 71  GLY 71  44  44  GLY GLY I . n 
I 1 72  PHE 72  45  45  PHE PHE I . n 
I 1 73  HIS 73  46  46  HIS HIS I . n 
I 1 74  VAL 74  47  47  VAL VAL I . n 
I 1 75  HIS 75  48  48  HIS HIS I . n 
I 1 76  GLU 76  49  49  GLU GLU I . n 
I 1 77  PHE 77  50  50  PHE PHE I . n 
I 1 78  GLY 78  51  51  GLY GLY I . n 
I 1 79  ASP 79  52  52  ASP ASP I . n 
I 1 80  ASN 80  53  53  ASN ASN I . n 
I 1 81  THR 81  54  54  THR THR I . n 
I 1 82  ALA 82  55  55  ALA ALA I . n 
I 1 83  GLY 83  56  56  GLY GLY I . n 
I 1 84  CYS 84  57  57  CYS CYS I . n 
I 1 85  THR 85  58  58  THR THR I . n 
I 1 86  SER 86  59  59  SER SER I . n 
I 1 87  ALA 87  60  60  ALA ALA I . n 
I 1 88  GLY 88  61  61  GLY GLY I . n 
I 1 89  PRO 89  62  62  PRO PRO I . n 
I 1 90  HIS 90  63  63  HIS HIS I . n 
I 1 91  PHE 91  64  64  PHE PHE I . n 
I 1 92  ASN 92  65  65  ASN ASN I . n 
I 1 93  PRO 93  66  66  PRO PRO I . n 
I 1 94  LEU 94  67  67  LEU LEU I . n 
I 1 95  SER 95  68  68  SER SER I . n 
I 1 96  ARG 96  69  69  ARG ARG I . n 
I 1 97  LYS 97  70  70  LYS LYS I . n 
I 1 98  HIS 98  71  71  HIS HIS I . n 
I 1 99  GLY 99  72  72  GLY GLY I . n 
I 1 100 GLY 100 73  73  GLY GLY I . n 
I 1 101 PRO 101 74  74  PRO PRO I . n 
I 1 102 LYS 102 75  75  LYS LYS I . n 
I 1 103 ASP 103 76  76  ASP ASP I . n 
I 1 104 GLU 104 77  77  GLU GLU I . n 
I 1 105 GLU 105 78  78  GLU GLU I . n 
I 1 106 ARG 106 79  79  ARG ARG I . n 
I 1 107 HIS 107 80  80  HIS HIS I . n 
I 1 108 VAL 108 81  81  VAL VAL I . n 
I 1 109 GLY 109 82  82  GLY GLY I . n 
I 1 110 ASP 110 83  83  ASP ASP I . n 
I 1 111 LEU 111 84  84  LEU LEU I . n 
I 1 112 GLY 112 85  85  GLY GLY I . n 
I 1 113 ASN 113 86  86  ASN ASN I . n 
I 1 114 VAL 114 87  87  VAL VAL I . n 
I 1 115 THR 115 88  88  THR THR I . n 
I 1 116 ALA 116 89  89  ALA ALA I . n 
I 1 117 ASP 117 90  90  ASP ASP I . n 
I 1 118 LYS 118 91  91  LYS LYS I . n 
I 1 119 ASP 119 92  92  ASP ASP I . n 
I 1 120 GLY 120 93  93  GLY GLY I . n 
I 1 121 VAL 121 94  94  VAL VAL I . n 
I 1 122 ALA 122 95  95  ALA ALA I . n 
I 1 123 ASP 123 96  96  ASP ASP I . n 
I 1 124 VAL 124 97  97  VAL VAL I . n 
I 1 125 SER 125 98  98  SER SER I . n 
I 1 126 ILE 126 99  99  ILE ILE I . n 
I 1 127 GLU 127 100 100 GLU GLU I . n 
I 1 128 ASP 128 101 101 ASP ASP I . n 
I 1 129 SER 129 102 102 SER SER I . n 
I 1 130 VAL 130 103 103 VAL VAL I . n 
I 1 131 ILE 131 104 104 ILE ILE I . n 
I 1 132 SER 132 105 105 SER SER I . n 
I 1 133 LEU 133 106 106 LEU LEU I . n 
I 1 134 SER 134 107 107 SER SER I . n 
I 1 135 GLY 135 108 108 GLY GLY I . n 
I 1 136 ASP 136 109 109 ASP ASP I . n 
I 1 137 HIS 137 110 110 HIS HIS I . n 
I 1 138 CYS 138 111 111 CYS CYS I . n 
I 1 139 ILE 139 112 112 ILE ILE I . n 
I 1 140 ILE 140 113 113 ILE ILE I . n 
I 1 141 GLY 141 114 114 GLY GLY I . n 
I 1 142 ARG 142 115 115 ARG ARG I . n 
I 1 143 THR 143 116 116 THR THR I . n 
I 1 144 LEU 144 117 117 LEU LEU I . n 
I 1 145 VAL 145 118 118 VAL VAL I . n 
I 1 146 VAL 146 119 119 VAL VAL I . n 
I 1 147 HIS 147 120 120 HIS HIS I . n 
I 1 148 GLU 148 121 121 GLU GLU I . n 
I 1 149 LYS 149 122 122 LYS LYS I . n 
I 1 150 ALA 150 123 123 ALA ALA I . n 
I 1 151 ASP 151 124 124 ASP ASP I . n 
I 1 152 ASP 152 125 125 ASP ASP I . n 
I 1 153 LEU 153 126 126 LEU LEU I . n 
I 1 154 GLY 154 127 127 GLY GLY I . n 
I 1 155 LYS 155 128 128 LYS LYS I . n 
I 1 156 GLY 156 129 129 GLY GLY I . n 
I 1 157 GLY 157 130 130 GLY GLY I . n 
I 1 158 ASN 158 131 131 ASN ASN I . n 
I 1 159 GLU 159 132 132 GLU GLU I . n 
I 1 160 GLU 160 133 133 GLU GLU I . n 
I 1 161 SER 161 134 134 SER SER I . n 
I 1 162 THR 162 135 135 THR THR I . n 
I 1 163 LYS 163 136 136 LYS LYS I . n 
I 1 164 THR 164 137 137 THR THR I . n 
I 1 165 GLY 165 138 138 GLY GLY I . n 
I 1 166 ASN 166 139 139 ASN ASN I . n 
I 1 167 ALA 167 140 140 ALA ALA I . n 
I 1 168 GLY 168 141 141 GLY GLY I . n 
I 1 169 SER 169 142 142 SER SER I . n 
I 1 170 ARG 170 143 143 ARG ARG I . n 
I 1 171 LEU 171 144 144 LEU LEU I . n 
I 1 172 ALA 172 145 145 ALA ALA I . n 
I 1 173 CYS 173 146 146 CYS CYS I . n 
I 1 174 GLY 174 147 147 GLY GLY I . n 
I 1 175 VAL 175 148 148 VAL VAL I . n 
I 1 176 ILE 176 149 149 ILE ILE I . n 
I 1 177 GLY 177 150 150 GLY GLY I . n 
I 1 178 ILE 178 151 151 ILE ILE I . n 
I 1 179 ALA 179 152 152 ALA ALA I . n 
I 1 180 GLN 180 153 153 GLN GLN I . n 
J 1 1   MET 1   -26 ?   ?   ?   J . n 
J 1 2   LYS 2   -25 ?   ?   ?   J . n 
J 1 3   HIS 3   -24 ?   ?   ?   J . n 
J 1 4   HIS 4   -23 ?   ?   ?   J . n 
J 1 5   HIS 5   -22 ?   ?   ?   J . n 
J 1 6   HIS 6   -21 ?   ?   ?   J . n 
J 1 7   HIS 7   -20 ?   ?   ?   J . n 
J 1 8   HIS 8   -19 ?   ?   ?   J . n 
J 1 9   PRO 9   -18 ?   ?   ?   J . n 
J 1 10  MET 10  -17 ?   ?   ?   J . n 
J 1 11  SER 11  -16 ?   ?   ?   J . n 
J 1 12  ASP 12  -15 ?   ?   ?   J . n 
J 1 13  TYR 13  -14 ?   ?   ?   J . n 
J 1 14  ASP 14  -13 ?   ?   ?   J . n 
J 1 15  ILE 15  -12 ?   ?   ?   J . n 
J 1 16  PRO 16  -11 ?   ?   ?   J . n 
J 1 17  THR 17  -10 ?   ?   ?   J . n 
J 1 18  THR 18  -9  ?   ?   ?   J . n 
J 1 19  GLU 19  -8  ?   ?   ?   J . n 
J 1 20  ASN 20  -7  ?   ?   ?   J . n 
J 1 21  LEU 21  -6  ?   ?   ?   J . n 
J 1 22  TYR 22  -5  ?   ?   ?   J . n 
J 1 23  PHE 23  -4  ?   ?   ?   J . n 
J 1 24  GLN 24  -3  ?   ?   ?   J . n 
J 1 25  GLY 25  -2  ?   ?   ?   J . n 
J 1 26  ALA 26  -1  ?   ?   ?   J . n 
J 1 27  MET 27  0   ?   ?   ?   J . n 
J 1 28  ALA 28  1   1   ALA ALA J . n 
J 1 29  THR 29  2   2   THR THR J . n 
J 1 30  LYS 30  3   3   LYS LYS J . n 
J 1 31  ALA 31  4   4   ALA ALA J . n 
J 1 32  VAL 32  5   5   VAL VAL J . n 
J 1 33  CYS 33  6   6   CYS CYS J . n 
J 1 34  VAL 34  7   7   VAL VAL J . n 
J 1 35  LEU 35  8   8   LEU LEU J . n 
J 1 36  LYS 36  9   9   LYS LYS J . n 
J 1 37  GLY 37  10  10  GLY GLY J . n 
J 1 38  ASP 38  11  11  ASP ASP J . n 
J 1 39  GLY 39  12  12  GLY GLY J . n 
J 1 40  PRO 40  13  13  PRO PRO J . n 
J 1 41  VAL 41  14  14  VAL VAL J . n 
J 1 42  GLN 42  15  15  GLN GLN J . n 
J 1 43  GLY 43  16  16  GLY GLY J . n 
J 1 44  ILE 44  17  17  ILE ILE J . n 
J 1 45  ILE 45  18  18  ILE ILE J . n 
J 1 46  ASN 46  19  19  ASN ASN J . n 
J 1 47  PHE 47  20  20  PHE PHE J . n 
J 1 48  GLU 48  21  21  GLU GLU J . n 
J 1 49  GLN 49  22  22  GLN GLN J . n 
J 1 50  LYS 50  23  23  LYS LYS J . n 
J 1 51  GLU 51  24  24  GLU GLU J . n 
J 1 52  SER 52  25  25  SER SER J . n 
J 1 53  ASN 53  26  26  ASN ASN J . n 
J 1 54  GLY 54  27  27  GLY GLY J . n 
J 1 55  PRO 55  28  28  PRO PRO J . n 
J 1 56  VAL 56  29  29  VAL VAL J . n 
J 1 57  LYS 57  30  30  LYS LYS J . n 
J 1 58  VAL 58  31  31  VAL VAL J . n 
J 1 59  TRP 59  32  32  TRP TRP J . n 
J 1 60  GLY 60  33  33  GLY GLY J . n 
J 1 61  SER 61  34  34  SER SER J . n 
J 1 62  ILE 62  35  35  ILE ILE J . n 
J 1 63  LYS 63  36  36  LYS LYS J . n 
J 1 64  GLY 64  37  37  GLY GLY J . n 
J 1 65  LEU 65  38  38  LEU LEU J . n 
J 1 66  THR 66  39  39  THR THR J . n 
J 1 67  GLU 67  40  40  GLU GLU J . n 
J 1 68  GLY 68  41  41  GLY GLY J . n 
J 1 69  LEU 69  42  42  LEU LEU J . n 
J 1 70  HIS 70  43  43  HIS HIS J . n 
J 1 71  GLY 71  44  44  GLY GLY J . n 
J 1 72  PHE 72  45  45  PHE PHE J . n 
J 1 73  HIS 73  46  46  HIS HIS J . n 
J 1 74  VAL 74  47  47  VAL VAL J . n 
J 1 75  HIS 75  48  48  HIS HIS J . n 
J 1 76  GLU 76  49  49  GLU GLU J . n 
J 1 77  PHE 77  50  50  PHE PHE J . n 
J 1 78  GLY 78  51  51  GLY GLY J . n 
J 1 79  ASP 79  52  52  ASP ASP J . n 
J 1 80  ASN 80  53  53  ASN ASN J . n 
J 1 81  THR 81  54  54  THR THR J . n 
J 1 82  ALA 82  55  55  ALA ALA J . n 
J 1 83  GLY 83  56  56  GLY GLY J . n 
J 1 84  CYS 84  57  57  CYS CYS J . n 
J 1 85  THR 85  58  58  THR THR J . n 
J 1 86  SER 86  59  59  SER SER J . n 
J 1 87  ALA 87  60  60  ALA ALA J . n 
J 1 88  GLY 88  61  61  GLY GLY J . n 
J 1 89  PRO 89  62  62  PRO PRO J . n 
J 1 90  HIS 90  63  63  HIS HIS J . n 
J 1 91  PHE 91  64  64  PHE PHE J . n 
J 1 92  ASN 92  65  65  ASN ASN J . n 
J 1 93  PRO 93  66  66  PRO PRO J . n 
J 1 94  LEU 94  67  ?   ?   ?   J . n 
J 1 95  SER 95  68  ?   ?   ?   J . n 
J 1 96  ARG 96  69  ?   ?   ?   J . n 
J 1 97  LYS 97  70  ?   ?   ?   J . n 
J 1 98  HIS 98  71  ?   ?   ?   J . n 
J 1 99  GLY 99  72  ?   ?   ?   J . n 
J 1 100 GLY 100 73  ?   ?   ?   J . n 
J 1 101 PRO 101 74  ?   ?   ?   J . n 
J 1 102 LYS 102 75  ?   ?   ?   J . n 
J 1 103 ASP 103 76  ?   ?   ?   J . n 
J 1 104 GLU 104 77  ?   ?   ?   J . n 
J 1 105 GLU 105 78  ?   ?   ?   J . n 
J 1 106 ARG 106 79  79  ARG ARG J . n 
J 1 107 HIS 107 80  80  HIS HIS J . n 
J 1 108 VAL 108 81  81  VAL VAL J . n 
J 1 109 GLY 109 82  82  GLY GLY J . n 
J 1 110 ASP 110 83  83  ASP ASP J . n 
J 1 111 LEU 111 84  84  LEU LEU J . n 
J 1 112 GLY 112 85  85  GLY GLY J . n 
J 1 113 ASN 113 86  86  ASN ASN J . n 
J 1 114 VAL 114 87  87  VAL VAL J . n 
J 1 115 THR 115 88  88  THR THR J . n 
J 1 116 ALA 116 89  89  ALA ALA J . n 
J 1 117 ASP 117 90  90  ASP ASP J . n 
J 1 118 LYS 118 91  91  LYS LYS J . n 
J 1 119 ASP 119 92  92  ASP ASP J . n 
J 1 120 GLY 120 93  93  GLY GLY J . n 
J 1 121 VAL 121 94  94  VAL VAL J . n 
J 1 122 ALA 122 95  95  ALA ALA J . n 
J 1 123 ASP 123 96  96  ASP ASP J . n 
J 1 124 VAL 124 97  97  VAL VAL J . n 
J 1 125 SER 125 98  98  SER SER J . n 
J 1 126 ILE 126 99  99  ILE ILE J . n 
J 1 127 GLU 127 100 100 GLU GLU J . n 
J 1 128 ASP 128 101 101 ASP ASP J . n 
J 1 129 SER 129 102 102 SER SER J . n 
J 1 130 VAL 130 103 103 VAL VAL J . n 
J 1 131 ILE 131 104 104 ILE ILE J . n 
J 1 132 SER 132 105 105 SER SER J . n 
J 1 133 LEU 133 106 106 LEU LEU J . n 
J 1 134 SER 134 107 107 SER SER J . n 
J 1 135 GLY 135 108 108 GLY GLY J . n 
J 1 136 ASP 136 109 109 ASP ASP J . n 
J 1 137 HIS 137 110 110 HIS HIS J . n 
J 1 138 CYS 138 111 111 CYS CYS J . n 
J 1 139 ILE 139 112 112 ILE ILE J . n 
J 1 140 ILE 140 113 113 ILE ILE J . n 
J 1 141 GLY 141 114 114 GLY GLY J . n 
J 1 142 ARG 142 115 115 ARG ARG J . n 
J 1 143 THR 143 116 116 THR THR J . n 
J 1 144 LEU 144 117 117 LEU LEU J . n 
J 1 145 VAL 145 118 118 VAL VAL J . n 
J 1 146 VAL 146 119 119 VAL VAL J . n 
J 1 147 HIS 147 120 120 HIS HIS J . n 
J 1 148 GLU 148 121 121 GLU GLU J . n 
J 1 149 LYS 149 122 122 LYS LYS J . n 
J 1 150 ALA 150 123 123 ALA ALA J . n 
J 1 151 ASP 151 124 124 ASP ASP J . n 
J 1 152 ASP 152 125 125 ASP ASP J . n 
J 1 153 LEU 153 126 ?   ?   ?   J . n 
J 1 154 GLY 154 127 ?   ?   ?   J . n 
J 1 155 LYS 155 128 ?   ?   ?   J . n 
J 1 156 GLY 156 129 ?   ?   ?   J . n 
J 1 157 GLY 157 130 ?   ?   ?   J . n 
J 1 158 ASN 158 131 ?   ?   ?   J . n 
J 1 159 GLU 159 132 ?   ?   ?   J . n 
J 1 160 GLU 160 133 ?   ?   ?   J . n 
J 1 161 SER 161 134 ?   ?   ?   J . n 
J 1 162 THR 162 135 ?   ?   ?   J . n 
J 1 163 LYS 163 136 ?   ?   ?   J . n 
J 1 164 THR 164 137 ?   ?   ?   J . n 
J 1 165 GLY 165 138 ?   ?   ?   J . n 
J 1 166 ASN 166 139 ?   ?   ?   J . n 
J 1 167 ALA 167 140 ?   ?   ?   J . n 
J 1 168 GLY 168 141 ?   ?   ?   J . n 
J 1 169 SER 169 142 142 SER SER J . n 
J 1 170 ARG 170 143 143 ARG ARG J . n 
J 1 171 LEU 171 144 144 LEU LEU J . n 
J 1 172 ALA 172 145 145 ALA ALA J . n 
J 1 173 CYS 173 146 146 CYS CYS J . n 
J 1 174 GLY 174 147 147 GLY GLY J . n 
J 1 175 VAL 175 148 148 VAL VAL J . n 
J 1 176 ILE 176 149 149 ILE ILE J . n 
J 1 177 GLY 177 150 150 GLY GLY J . n 
J 1 178 ILE 178 151 151 ILE ILE J . n 
J 1 179 ALA 179 152 152 ALA ALA J . n 
J 1 180 GLN 180 153 153 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 2    ZN  ZN  A . 
L  3 GOL 1   202 1    GOL GOL A . 
M  2 ZN  1   201 3    ZN  ZN  B . 
N  3 GOL 1   202 1    GOL GOL B . 
O  4 946 1   203 1    946 L44 B . 
P  5 PS5 1   204 1    PS5 PS5 B . 
Q  2 ZN  1   201 4    ZN  ZN  C . 
R  3 GOL 1   202 1    GOL GOL C . 
S  5 PS5 1   203 2    PS5 PS5 C . 
T  2 ZN  1   201 1    ZN  ZN  D . 
U  4 946 1   202 1    946 L44 D . 
V  2 ZN  1   201 6    ZN  ZN  E . 
W  5 PS5 1   202 3    PS5 PS5 E . 
X  2 ZN  1   201 5    ZN  ZN  F . 
Y  2 ZN  1   201 8    ZN  ZN  G . 
Z  2 ZN  1   201 7    ZN  ZN  H . 
AA 4 946 1   202 1    946 L44 H . 
BA 2 ZN  1   201 9    ZN  ZN  I . 
CA 6 HOH 1   301 1398 HOH HOH A . 
CA 6 HOH 2   302 200  HOH HOH A . 
CA 6 HOH 3   303 848  HOH HOH A . 
CA 6 HOH 4   304 295  HOH HOH A . 
CA 6 HOH 5   305 821  HOH HOH A . 
CA 6 HOH 6   306 340  HOH HOH A . 
CA 6 HOH 7   307 1238 HOH HOH A . 
CA 6 HOH 8   308 1086 HOH HOH A . 
CA 6 HOH 9   309 394  HOH HOH A . 
CA 6 HOH 10  310 317  HOH HOH A . 
CA 6 HOH 11  311 1144 HOH HOH A . 
CA 6 HOH 12  312 360  HOH HOH A . 
CA 6 HOH 13  313 1008 HOH HOH A . 
CA 6 HOH 14  314 148  HOH HOH A . 
CA 6 HOH 15  315 8    HOH HOH A . 
CA 6 HOH 16  316 390  HOH HOH A . 
CA 6 HOH 17  317 177  HOH HOH A . 
CA 6 HOH 18  318 291  HOH HOH A . 
CA 6 HOH 19  319 1206 HOH HOH A . 
CA 6 HOH 20  320 1402 HOH HOH A . 
CA 6 HOH 21  321 1183 HOH HOH A . 
CA 6 HOH 22  322 833  HOH HOH A . 
CA 6 HOH 23  323 175  HOH HOH A . 
CA 6 HOH 24  324 193  HOH HOH A . 
CA 6 HOH 25  325 431  HOH HOH A . 
CA 6 HOH 26  326 640  HOH HOH A . 
CA 6 HOH 27  327 369  HOH HOH A . 
CA 6 HOH 28  328 1385 HOH HOH A . 
CA 6 HOH 29  329 171  HOH HOH A . 
CA 6 HOH 30  330 1009 HOH HOH A . 
CA 6 HOH 31  331 1179 HOH HOH A . 
CA 6 HOH 32  332 853  HOH HOH A . 
CA 6 HOH 33  333 937  HOH HOH A . 
CA 6 HOH 34  334 1441 HOH HOH A . 
CA 6 HOH 35  335 467  HOH HOH A . 
CA 6 HOH 36  336 1124 HOH HOH A . 
CA 6 HOH 37  337 459  HOH HOH A . 
CA 6 HOH 38  338 271  HOH HOH A . 
CA 6 HOH 39  339 695  HOH HOH A . 
CA 6 HOH 40  340 457  HOH HOH A . 
CA 6 HOH 41  341 261  HOH HOH A . 
CA 6 HOH 42  342 579  HOH HOH A . 
CA 6 HOH 43  343 453  HOH HOH A . 
CA 6 HOH 44  344 217  HOH HOH A . 
CA 6 HOH 45  345 392  HOH HOH A . 
CA 6 HOH 46  346 398  HOH HOH A . 
CA 6 HOH 47  347 153  HOH HOH A . 
CA 6 HOH 48  348 162  HOH HOH A . 
CA 6 HOH 49  349 700  HOH HOH A . 
CA 6 HOH 50  350 1120 HOH HOH A . 
CA 6 HOH 51  351 1063 HOH HOH A . 
CA 6 HOH 52  352 976  HOH HOH A . 
CA 6 HOH 53  353 1436 HOH HOH A . 
CA 6 HOH 54  354 740  HOH HOH A . 
CA 6 HOH 55  355 574  HOH HOH A . 
CA 6 HOH 56  356 132  HOH HOH A . 
CA 6 HOH 57  357 1061 HOH HOH A . 
CA 6 HOH 58  358 515  HOH HOH A . 
CA 6 HOH 59  359 93   HOH HOH A . 
CA 6 HOH 60  360 889  HOH HOH A . 
CA 6 HOH 61  361 470  HOH HOH A . 
CA 6 HOH 62  362 867  HOH HOH A . 
CA 6 HOH 63  363 869  HOH HOH A . 
CA 6 HOH 64  364 577  HOH HOH A . 
CA 6 HOH 65  365 46   HOH HOH A . 
CA 6 HOH 66  366 1421 HOH HOH A . 
CA 6 HOH 67  367 240  HOH HOH A . 
CA 6 HOH 68  368 149  HOH HOH A . 
CA 6 HOH 69  369 206  HOH HOH A . 
CA 6 HOH 70  370 9    HOH HOH A . 
CA 6 HOH 71  371 649  HOH HOH A . 
CA 6 HOH 72  372 625  HOH HOH A . 
CA 6 HOH 73  373 29   HOH HOH A . 
CA 6 HOH 74  374 245  HOH HOH A . 
CA 6 HOH 75  375 301  HOH HOH A . 
CA 6 HOH 76  376 22   HOH HOH A . 
CA 6 HOH 77  377 1482 HOH HOH A . 
CA 6 HOH 78  378 338  HOH HOH A . 
CA 6 HOH 79  379 243  HOH HOH A . 
CA 6 HOH 80  380 320  HOH HOH A . 
CA 6 HOH 81  381 124  HOH HOH A . 
CA 6 HOH 82  382 119  HOH HOH A . 
CA 6 HOH 83  383 1129 HOH HOH A . 
CA 6 HOH 84  384 314  HOH HOH A . 
CA 6 HOH 85  385 651  HOH HOH A . 
CA 6 HOH 86  386 799  HOH HOH A . 
CA 6 HOH 87  387 752  HOH HOH A . 
CA 6 HOH 88  388 1256 HOH HOH A . 
CA 6 HOH 89  389 1393 HOH HOH A . 
CA 6 HOH 90  390 224  HOH HOH A . 
CA 6 HOH 91  391 410  HOH HOH A . 
CA 6 HOH 92  392 1311 HOH HOH A . 
CA 6 HOH 93  393 235  HOH HOH A . 
CA 6 HOH 94  394 1185 HOH HOH A . 
CA 6 HOH 95  395 600  HOH HOH A . 
CA 6 HOH 96  396 666  HOH HOH A . 
CA 6 HOH 97  397 267  HOH HOH A . 
CA 6 HOH 98  398 471  HOH HOH A . 
CA 6 HOH 99  399 575  HOH HOH A . 
CA 6 HOH 100 400 353  HOH HOH A . 
CA 6 HOH 101 401 58   HOH HOH A . 
CA 6 HOH 102 402 94   HOH HOH A . 
CA 6 HOH 103 403 258  HOH HOH A . 
CA 6 HOH 104 404 924  HOH HOH A . 
CA 6 HOH 105 405 778  HOH HOH A . 
CA 6 HOH 106 406 208  HOH HOH A . 
CA 6 HOH 107 407 1162 HOH HOH A . 
CA 6 HOH 108 408 613  HOH HOH A . 
CA 6 HOH 109 409 362  HOH HOH A . 
CA 6 HOH 110 410 391  HOH HOH A . 
CA 6 HOH 111 411 919  HOH HOH A . 
CA 6 HOH 112 412 363  HOH HOH A . 
CA 6 HOH 113 413 1352 HOH HOH A . 
CA 6 HOH 114 414 1356 HOH HOH A . 
CA 6 HOH 115 415 608  HOH HOH A . 
CA 6 HOH 116 416 113  HOH HOH A . 
CA 6 HOH 117 417 794  HOH HOH A . 
CA 6 HOH 118 418 735  HOH HOH A . 
CA 6 HOH 119 419 1031 HOH HOH A . 
CA 6 HOH 120 420 698  HOH HOH A . 
CA 6 HOH 121 421 63   HOH HOH A . 
CA 6 HOH 122 422 1310 HOH HOH A . 
CA 6 HOH 123 423 52   HOH HOH A . 
CA 6 HOH 124 424 785  HOH HOH A . 
CA 6 HOH 125 425 588  HOH HOH A . 
CA 6 HOH 126 426 1347 HOH HOH A . 
CA 6 HOH 127 427 1303 HOH HOH A . 
CA 6 HOH 128 428 634  HOH HOH A . 
CA 6 HOH 129 429 822  HOH HOH A . 
CA 6 HOH 130 430 1166 HOH HOH A . 
CA 6 HOH 131 431 1140 HOH HOH A . 
CA 6 HOH 132 432 986  HOH HOH A . 
CA 6 HOH 133 433 1453 HOH HOH A . 
CA 6 HOH 134 434 209  HOH HOH A . 
CA 6 HOH 135 435 1221 HOH HOH A . 
CA 6 HOH 136 436 1293 HOH HOH A . 
CA 6 HOH 137 437 585  HOH HOH A . 
CA 6 HOH 138 438 1484 HOH HOH A . 
CA 6 HOH 139 439 781  HOH HOH A . 
CA 6 HOH 140 440 737  HOH HOH A . 
CA 6 HOH 141 441 883  HOH HOH A . 
CA 6 HOH 142 442 984  HOH HOH A . 
CA 6 HOH 143 443 1234 HOH HOH A . 
CA 6 HOH 144 444 981  HOH HOH A . 
CA 6 HOH 145 445 1260 HOH HOH A . 
CA 6 HOH 146 446 1386 HOH HOH A . 
CA 6 HOH 147 447 1156 HOH HOH A . 
CA 6 HOH 148 448 1295 HOH HOH A . 
CA 6 HOH 149 449 713  HOH HOH A . 
CA 6 HOH 150 450 1369 HOH HOH A . 
CA 6 HOH 151 451 1483 HOH HOH A . 
CA 6 HOH 152 452 414  HOH HOH A . 
CA 6 HOH 153 453 771  HOH HOH A . 
CA 6 HOH 154 454 838  HOH HOH A . 
CA 6 HOH 155 455 1194 HOH HOH A . 
CA 6 HOH 156 456 1012 HOH HOH A . 
CA 6 HOH 157 457 1099 HOH HOH A . 
CA 6 HOH 158 458 978  HOH HOH A . 
CA 6 HOH 159 459 851  HOH HOH A . 
CA 6 HOH 160 460 699  HOH HOH A . 
CA 6 HOH 161 461 671  HOH HOH A . 
CA 6 HOH 162 462 1265 HOH HOH A . 
CA 6 HOH 163 463 1383 HOH HOH A . 
CA 6 HOH 164 464 1027 HOH HOH A . 
CA 6 HOH 165 465 1372 HOH HOH A . 
CA 6 HOH 166 466 1437 HOH HOH A . 
CA 6 HOH 167 467 892  HOH HOH A . 
CA 6 HOH 168 468 839  HOH HOH A . 
CA 6 HOH 169 469 1228 HOH HOH A . 
CA 6 HOH 170 470 906  HOH HOH A . 
CA 6 HOH 171 471 1312 HOH HOH A . 
CA 6 HOH 172 472 1323 HOH HOH A . 
DA 6 HOH 1   301 1353 HOH HOH B . 
DA 6 HOH 2   302 1266 HOH HOH B . 
DA 6 HOH 3   303 122  HOH HOH B . 
DA 6 HOH 4   304 789  HOH HOH B . 
DA 6 HOH 5   305 526  HOH HOH B . 
DA 6 HOH 6   306 719  HOH HOH B . 
DA 6 HOH 7   307 259  HOH HOH B . 
DA 6 HOH 8   308 81   HOH HOH B . 
DA 6 HOH 9   309 1037 HOH HOH B . 
DA 6 HOH 10  310 492  HOH HOH B . 
DA 6 HOH 11  311 809  HOH HOH B . 
DA 6 HOH 12  312 1258 HOH HOH B . 
DA 6 HOH 13  313 225  HOH HOH B . 
DA 6 HOH 14  314 181  HOH HOH B . 
DA 6 HOH 15  315 129  HOH HOH B . 
DA 6 HOH 16  316 592  HOH HOH B . 
DA 6 HOH 17  317 1313 HOH HOH B . 
DA 6 HOH 18  318 329  HOH HOH B . 
DA 6 HOH 19  319 746  HOH HOH B . 
DA 6 HOH 20  320 934  HOH HOH B . 
DA 6 HOH 21  321 633  HOH HOH B . 
DA 6 HOH 22  322 372  HOH HOH B . 
DA 6 HOH 23  323 159  HOH HOH B . 
DA 6 HOH 24  324 164  HOH HOH B . 
DA 6 HOH 25  325 313  HOH HOH B . 
DA 6 HOH 26  326 244  HOH HOH B . 
DA 6 HOH 27  327 147  HOH HOH B . 
DA 6 HOH 28  328 1348 HOH HOH B . 
DA 6 HOH 29  329 468  HOH HOH B . 
DA 6 HOH 30  330 920  HOH HOH B . 
DA 6 HOH 31  331 264  HOH HOH B . 
DA 6 HOH 32  332 34   HOH HOH B . 
DA 6 HOH 33  333 4    HOH HOH B . 
DA 6 HOH 34  334 763  HOH HOH B . 
DA 6 HOH 35  335 1151 HOH HOH B . 
DA 6 HOH 36  336 260  HOH HOH B . 
DA 6 HOH 37  337 660  HOH HOH B . 
DA 6 HOH 38  338 154  HOH HOH B . 
DA 6 HOH 39  339 172  HOH HOH B . 
DA 6 HOH 40  340 620  HOH HOH B . 
DA 6 HOH 41  341 770  HOH HOH B . 
DA 6 HOH 42  342 581  HOH HOH B . 
DA 6 HOH 43  343 606  HOH HOH B . 
DA 6 HOH 44  344 626  HOH HOH B . 
DA 6 HOH 45  345 36   HOH HOH B . 
DA 6 HOH 46  346 35   HOH HOH B . 
DA 6 HOH 47  347 543  HOH HOH B . 
DA 6 HOH 48  348 168  HOH HOH B . 
DA 6 HOH 49  349 2    HOH HOH B . 
DA 6 HOH 50  350 1284 HOH HOH B . 
DA 6 HOH 51  351 51   HOH HOH B . 
DA 6 HOH 52  352 1394 HOH HOH B . 
DA 6 HOH 53  353 173  HOH HOH B . 
DA 6 HOH 54  354 269  HOH HOH B . 
DA 6 HOH 55  355 13   HOH HOH B . 
DA 6 HOH 56  356 1123 HOH HOH B . 
DA 6 HOH 57  357 290  HOH HOH B . 
DA 6 HOH 58  358 512  HOH HOH B . 
DA 6 HOH 59  359 683  HOH HOH B . 
DA 6 HOH 60  360 222  HOH HOH B . 
DA 6 HOH 61  361 432  HOH HOH B . 
DA 6 HOH 62  362 262  HOH HOH B . 
DA 6 HOH 63  363 41   HOH HOH B . 
DA 6 HOH 64  364 1115 HOH HOH B . 
DA 6 HOH 65  365 555  HOH HOH B . 
DA 6 HOH 66  366 886  HOH HOH B . 
DA 6 HOH 67  367 49   HOH HOH B . 
DA 6 HOH 68  368 322  HOH HOH B . 
DA 6 HOH 69  369 39   HOH HOH B . 
DA 6 HOH 70  370 27   HOH HOH B . 
DA 6 HOH 71  371 227  HOH HOH B . 
DA 6 HOH 72  372 845  HOH HOH B . 
DA 6 HOH 73  373 652  HOH HOH B . 
DA 6 HOH 74  374 1195 HOH HOH B . 
DA 6 HOH 75  375 708  HOH HOH B . 
DA 6 HOH 76  376 292  HOH HOH B . 
DA 6 HOH 77  377 728  HOH HOH B . 
DA 6 HOH 78  378 100  HOH HOH B . 
DA 6 HOH 79  379 403  HOH HOH B . 
DA 6 HOH 80  380 1420 HOH HOH B . 
DA 6 HOH 81  381 37   HOH HOH B . 
DA 6 HOH 82  382 73   HOH HOH B . 
DA 6 HOH 83  383 1434 HOH HOH B . 
DA 6 HOH 84  384 126  HOH HOH B . 
DA 6 HOH 85  385 25   HOH HOH B . 
DA 6 HOH 86  386 176  HOH HOH B . 
DA 6 HOH 87  387 1006 HOH HOH B . 
DA 6 HOH 88  388 511  HOH HOH B . 
DA 6 HOH 89  389 196  HOH HOH B . 
DA 6 HOH 90  390 59   HOH HOH B . 
DA 6 HOH 91  391 166  HOH HOH B . 
DA 6 HOH 92  392 840  HOH HOH B . 
DA 6 HOH 93  393 107  HOH HOH B . 
DA 6 HOH 94  394 16   HOH HOH B . 
DA 6 HOH 95  395 518  HOH HOH B . 
DA 6 HOH 96  396 489  HOH HOH B . 
DA 6 HOH 97  397 315  HOH HOH B . 
DA 6 HOH 98  398 1024 HOH HOH B . 
DA 6 HOH 99  399 1474 HOH HOH B . 
DA 6 HOH 100 400 77   HOH HOH B . 
DA 6 HOH 101 401 203  HOH HOH B . 
DA 6 HOH 102 402 1425 HOH HOH B . 
DA 6 HOH 103 403 80   HOH HOH B . 
DA 6 HOH 104 404 615  HOH HOH B . 
DA 6 HOH 105 405 64   HOH HOH B . 
DA 6 HOH 106 406 184  HOH HOH B . 
DA 6 HOH 107 407 604  HOH HOH B . 
DA 6 HOH 108 408 265  HOH HOH B . 
DA 6 HOH 109 409 940  HOH HOH B . 
DA 6 HOH 110 410 281  HOH HOH B . 
DA 6 HOH 111 411 6    HOH HOH B . 
DA 6 HOH 112 412 90   HOH HOH B . 
DA 6 HOH 113 413 79   HOH HOH B . 
DA 6 HOH 114 414 795  HOH HOH B . 
DA 6 HOH 115 415 748  HOH HOH B . 
DA 6 HOH 116 416 238  HOH HOH B . 
DA 6 HOH 117 417 76   HOH HOH B . 
DA 6 HOH 118 418 237  HOH HOH B . 
DA 6 HOH 119 419 1116 HOH HOH B . 
DA 6 HOH 120 420 1098 HOH HOH B . 
DA 6 HOH 121 421 231  HOH HOH B . 
DA 6 HOH 122 422 178  HOH HOH B . 
DA 6 HOH 123 423 1340 HOH HOH B . 
DA 6 HOH 124 424 1315 HOH HOH B . 
DA 6 HOH 125 425 1301 HOH HOH B . 
DA 6 HOH 126 426 528  HOH HOH B . 
DA 6 HOH 127 427 904  HOH HOH B . 
DA 6 HOH 128 428 1389 HOH HOH B . 
DA 6 HOH 129 429 539  HOH HOH B . 
DA 6 HOH 130 430 1065 HOH HOH B . 
DA 6 HOH 131 431 909  HOH HOH B . 
DA 6 HOH 132 432 1026 HOH HOH B . 
DA 6 HOH 133 433 1292 HOH HOH B . 
DA 6 HOH 134 434 418  HOH HOH B . 
DA 6 HOH 135 435 485  HOH HOH B . 
DA 6 HOH 136 436 1242 HOH HOH B . 
DA 6 HOH 137 437 1028 HOH HOH B . 
DA 6 HOH 138 438 1210 HOH HOH B . 
DA 6 HOH 139 439 628  HOH HOH B . 
DA 6 HOH 140 440 1423 HOH HOH B . 
DA 6 HOH 141 441 656  HOH HOH B . 
DA 6 HOH 142 442 109  HOH HOH B . 
DA 6 HOH 143 443 325  HOH HOH B . 
DA 6 HOH 144 444 1286 HOH HOH B . 
DA 6 HOH 145 445 1074 HOH HOH B . 
DA 6 HOH 146 446 1395 HOH HOH B . 
DA 6 HOH 147 447 790  HOH HOH B . 
DA 6 HOH 148 448 1095 HOH HOH B . 
DA 6 HOH 149 449 1481 HOH HOH B . 
DA 6 HOH 150 450 682  HOH HOH B . 
DA 6 HOH 151 451 1102 HOH HOH B . 
DA 6 HOH 152 452 1064 HOH HOH B . 
DA 6 HOH 153 453 1412 HOH HOH B . 
DA 6 HOH 154 454 475  HOH HOH B . 
DA 6 HOH 155 455 815  HOH HOH B . 
DA 6 HOH 156 456 256  HOH HOH B . 
DA 6 HOH 157 457 1287 HOH HOH B . 
DA 6 HOH 158 458 1475 HOH HOH B . 
DA 6 HOH 159 459 1130 HOH HOH B . 
DA 6 HOH 160 460 1127 HOH HOH B . 
DA 6 HOH 161 461 896  HOH HOH B . 
DA 6 HOH 162 462 1035 HOH HOH B . 
DA 6 HOH 163 463 1379 HOH HOH B . 
DA 6 HOH 164 464 1118 HOH HOH B . 
DA 6 HOH 165 465 1189 HOH HOH B . 
DA 6 HOH 166 466 1407 HOH HOH B . 
DA 6 HOH 167 467 922  HOH HOH B . 
DA 6 HOH 168 468 806  HOH HOH B . 
DA 6 HOH 169 469 570  HOH HOH B . 
DA 6 HOH 170 470 831  HOH HOH B . 
DA 6 HOH 171 471 898  HOH HOH B . 
DA 6 HOH 172 472 1142 HOH HOH B . 
DA 6 HOH 173 473 1199 HOH HOH B . 
DA 6 HOH 174 474 664  HOH HOH B . 
DA 6 HOH 175 475 931  HOH HOH B . 
DA 6 HOH 176 476 1447 HOH HOH B . 
DA 6 HOH 177 477 1381 HOH HOH B . 
DA 6 HOH 178 478 1261 HOH HOH B . 
DA 6 HOH 179 479 813  HOH HOH B . 
DA 6 HOH 180 480 1207 HOH HOH B . 
DA 6 HOH 181 481 567  HOH HOH B . 
DA 6 HOH 182 482 1069 HOH HOH B . 
DA 6 HOH 183 483 1403 HOH HOH B . 
DA 6 HOH 184 484 820  HOH HOH B . 
DA 6 HOH 185 485 1480 HOH HOH B . 
DA 6 HOH 186 486 1132 HOH HOH B . 
DA 6 HOH 187 487 882  HOH HOH B . 
DA 6 HOH 188 488 155  HOH HOH B . 
DA 6 HOH 189 489 1048 HOH HOH B . 
DA 6 HOH 190 490 1417 HOH HOH B . 
DA 6 HOH 191 491 985  HOH HOH B . 
DA 6 HOH 192 492 1247 HOH HOH B . 
DA 6 HOH 193 493 727  HOH HOH B . 
DA 6 HOH 194 494 969  HOH HOH B . 
DA 6 HOH 195 495 849  HOH HOH B . 
DA 6 HOH 196 496 151  HOH HOH B . 
DA 6 HOH 197 497 476  HOH HOH B . 
DA 6 HOH 198 498 1057 HOH HOH B . 
DA 6 HOH 199 499 722  HOH HOH B . 
DA 6 HOH 200 500 689  HOH HOH B . 
DA 6 HOH 201 501 365  HOH HOH B . 
DA 6 HOH 202 502 503  HOH HOH B . 
DA 6 HOH 203 503 780  HOH HOH B . 
DA 6 HOH 204 504 1039 HOH HOH B . 
DA 6 HOH 205 505 319  HOH HOH B . 
DA 6 HOH 206 506 434  HOH HOH B . 
DA 6 HOH 207 507 1291 HOH HOH B . 
DA 6 HOH 208 508 452  HOH HOH B . 
DA 6 HOH 209 509 1346 HOH HOH B . 
DA 6 HOH 210 510 1458 HOH HOH B . 
DA 6 HOH 211 511 1011 HOH HOH B . 
DA 6 HOH 212 512 1023 HOH HOH B . 
DA 6 HOH 213 513 451  HOH HOH B . 
DA 6 HOH 214 514 987  HOH HOH B . 
DA 6 HOH 215 515 1476 HOH HOH B . 
DA 6 HOH 216 516 1470 HOH HOH B . 
DA 6 HOH 217 517 872  HOH HOH B . 
DA 6 HOH 218 518 1469 HOH HOH B . 
EA 6 HOH 1   301 361  HOH HOH C . 
EA 6 HOH 2   302 803  HOH HOH C . 
EA 6 HOH 3   303 655  HOH HOH C . 
EA 6 HOH 4   304 1040 HOH HOH C . 
EA 6 HOH 5   305 558  HOH HOH C . 
EA 6 HOH 6   306 888  HOH HOH C . 
EA 6 HOH 7   307 694  HOH HOH C . 
EA 6 HOH 8   308 751  HOH HOH C . 
EA 6 HOH 9   309 675  HOH HOH C . 
EA 6 HOH 10  310 183  HOH HOH C . 
EA 6 HOH 11  311 1471 HOH HOH C . 
EA 6 HOH 12  312 316  HOH HOH C . 
EA 6 HOH 13  313 302  HOH HOH C . 
EA 6 HOH 14  314 248  HOH HOH C . 
EA 6 HOH 15  315 541  HOH HOH C . 
EA 6 HOH 16  316 786  HOH HOH C . 
EA 6 HOH 17  317 416  HOH HOH C . 
EA 6 HOH 18  318 5    HOH HOH C . 
EA 6 HOH 19  319 942  HOH HOH C . 
EA 6 HOH 20  320 321  HOH HOH C . 
EA 6 HOH 21  321 989  HOH HOH C . 
EA 6 HOH 22  322 382  HOH HOH C . 
EA 6 HOH 23  323 958  HOH HOH C . 
EA 6 HOH 24  324 3    HOH HOH C . 
EA 6 HOH 25  325 102  HOH HOH C . 
EA 6 HOH 26  326 524  HOH HOH C . 
EA 6 HOH 27  327 370  HOH HOH C . 
EA 6 HOH 28  328 796  HOH HOH C . 
EA 6 HOH 29  329 687  HOH HOH C . 
EA 6 HOH 30  330 895  HOH HOH C . 
EA 6 HOH 31  331 26   HOH HOH C . 
EA 6 HOH 32  332 194  HOH HOH C . 
EA 6 HOH 33  333 590  HOH HOH C . 
EA 6 HOH 34  334 98   HOH HOH C . 
EA 6 HOH 35  335 1331 HOH HOH C . 
EA 6 HOH 36  336 463  HOH HOH C . 
EA 6 HOH 37  337 110  HOH HOH C . 
EA 6 HOH 38  338 211  HOH HOH C . 
EA 6 HOH 39  339 648  HOH HOH C . 
EA 6 HOH 40  340 499  HOH HOH C . 
EA 6 HOH 41  341 401  HOH HOH C . 
EA 6 HOH 42  342 1240 HOH HOH C . 
EA 6 HOH 43  343 742  HOH HOH C . 
EA 6 HOH 44  344 111  HOH HOH C . 
EA 6 HOH 45  345 270  HOH HOH C . 
EA 6 HOH 46  346 598  HOH HOH C . 
EA 6 HOH 47  347 523  HOH HOH C . 
EA 6 HOH 48  348 272  HOH HOH C . 
EA 6 HOH 49  349 12   HOH HOH C . 
EA 6 HOH 50  350 716  HOH HOH C . 
EA 6 HOH 51  351 182  HOH HOH C . 
EA 6 HOH 52  352 192  HOH HOH C . 
EA 6 HOH 53  353 454  HOH HOH C . 
EA 6 HOH 54  354 32   HOH HOH C . 
EA 6 HOH 55  355 232  HOH HOH C . 
EA 6 HOH 56  356 127  HOH HOH C . 
EA 6 HOH 57  357 1375 HOH HOH C . 
EA 6 HOH 58  358 279  HOH HOH C . 
EA 6 HOH 59  359 669  HOH HOH C . 
EA 6 HOH 60  360 1435 HOH HOH C . 
EA 6 HOH 61  361 381  HOH HOH C . 
EA 6 HOH 62  362 890  HOH HOH C . 
EA 6 HOH 63  363 17   HOH HOH C . 
EA 6 HOH 64  364 1302 HOH HOH C . 
EA 6 HOH 65  365 174  HOH HOH C . 
EA 6 HOH 66  366 916  HOH HOH C . 
EA 6 HOH 67  367 205  HOH HOH C . 
EA 6 HOH 68  368 48   HOH HOH C . 
EA 6 HOH 69  369 167  HOH HOH C . 
EA 6 HOH 70  370 131  HOH HOH C . 
EA 6 HOH 71  371 229  HOH HOH C . 
EA 6 HOH 72  372 14   HOH HOH C . 
EA 6 HOH 73  373 521  HOH HOH C . 
EA 6 HOH 74  374 71   HOH HOH C . 
EA 6 HOH 75  375 1113 HOH HOH C . 
EA 6 HOH 76  376 11   HOH HOH C . 
EA 6 HOH 77  377 97   HOH HOH C . 
EA 6 HOH 78  378 584  HOH HOH C . 
EA 6 HOH 79  379 28   HOH HOH C . 
EA 6 HOH 80  380 137  HOH HOH C . 
EA 6 HOH 81  381 782  HOH HOH C . 
EA 6 HOH 82  382 252  HOH HOH C . 
EA 6 HOH 83  383 348  HOH HOH C . 
EA 6 HOH 84  384 1108 HOH HOH C . 
EA 6 HOH 85  385 760  HOH HOH C . 
EA 6 HOH 86  386 530  HOH HOH C . 
EA 6 HOH 87  387 57   HOH HOH C . 
EA 6 HOH 88  388 70   HOH HOH C . 
EA 6 HOH 89  389 170  HOH HOH C . 
EA 6 HOH 90  390 376  HOH HOH C . 
EA 6 HOH 91  391 1196 HOH HOH C . 
EA 6 HOH 92  392 714  HOH HOH C . 
EA 6 HOH 93  393 10   HOH HOH C . 
EA 6 HOH 94  394 354  HOH HOH C . 
EA 6 HOH 95  395 156  HOH HOH C . 
EA 6 HOH 96  396 138  HOH HOH C . 
EA 6 HOH 97  397 158  HOH HOH C . 
EA 6 HOH 98  398 250  HOH HOH C . 
EA 6 HOH 99  399 24   HOH HOH C . 
EA 6 HOH 100 400 311  HOH HOH C . 
EA 6 HOH 101 401 617  HOH HOH C . 
EA 6 HOH 102 402 571  HOH HOH C . 
EA 6 HOH 103 403 74   HOH HOH C . 
EA 6 HOH 104 404 62   HOH HOH C . 
EA 6 HOH 105 405 201  HOH HOH C . 
EA 6 HOH 106 406 542  HOH HOH C . 
EA 6 HOH 107 407 721  HOH HOH C . 
EA 6 HOH 108 408 18   HOH HOH C . 
EA 6 HOH 109 409 108  HOH HOH C . 
EA 6 HOH 110 410 1176 HOH HOH C . 
EA 6 HOH 111 411 1244 HOH HOH C . 
EA 6 HOH 112 412 169  HOH HOH C . 
EA 6 HOH 113 413 605  HOH HOH C . 
EA 6 HOH 114 414 345  HOH HOH C . 
EA 6 HOH 115 415 587  HOH HOH C . 
EA 6 HOH 116 416 297  HOH HOH C . 
EA 6 HOH 117 417 908  HOH HOH C . 
EA 6 HOH 118 418 1138 HOH HOH C . 
EA 6 HOH 119 419 397  HOH HOH C . 
EA 6 HOH 120 420 1045 HOH HOH C . 
EA 6 HOH 121 421 802  HOH HOH C . 
EA 6 HOH 122 422 1489 HOH HOH C . 
EA 6 HOH 123 423 1388 HOH HOH C . 
EA 6 HOH 124 424 443  HOH HOH C . 
EA 6 HOH 125 425 1106 HOH HOH C . 
EA 6 HOH 126 426 1468 HOH HOH C . 
EA 6 HOH 127 427 1277 HOH HOH C . 
EA 6 HOH 128 428 647  HOH HOH C . 
EA 6 HOH 129 429 665  HOH HOH C . 
EA 6 HOH 130 430 792  HOH HOH C . 
EA 6 HOH 131 431 1325 HOH HOH C . 
EA 6 HOH 132 432 877  HOH HOH C . 
EA 6 HOH 133 433 187  HOH HOH C . 
EA 6 HOH 134 434 318  HOH HOH C . 
EA 6 HOH 135 435 566  HOH HOH C . 
EA 6 HOH 136 436 1488 HOH HOH C . 
EA 6 HOH 137 437 239  HOH HOH C . 
EA 6 HOH 138 438 1252 HOH HOH C . 
EA 6 HOH 139 439 1411 HOH HOH C . 
EA 6 HOH 140 440 1485 HOH HOH C . 
EA 6 HOH 141 441 812  HOH HOH C . 
EA 6 HOH 142 442 1321 HOH HOH C . 
EA 6 HOH 143 443 1318 HOH HOH C . 
EA 6 HOH 144 444 190  HOH HOH C . 
EA 6 HOH 145 445 738  HOH HOH C . 
EA 6 HOH 146 446 929  HOH HOH C . 
EA 6 HOH 147 447 614  HOH HOH C . 
EA 6 HOH 148 448 810  HOH HOH C . 
EA 6 HOH 149 449 1282 HOH HOH C . 
EA 6 HOH 150 450 1033 HOH HOH C . 
EA 6 HOH 151 451 514  HOH HOH C . 
EA 6 HOH 152 452 1276 HOH HOH C . 
EA 6 HOH 153 453 965  HOH HOH C . 
EA 6 HOH 154 454 712  HOH HOH C . 
EA 6 HOH 155 455 1335 HOH HOH C . 
EA 6 HOH 156 456 983  HOH HOH C . 
EA 6 HOH 157 457 841  HOH HOH C . 
EA 6 HOH 158 458 811  HOH HOH C . 
EA 6 HOH 159 459 554  HOH HOH C . 
EA 6 HOH 160 460 1082 HOH HOH C . 
EA 6 HOH 161 461 303  HOH HOH C . 
EA 6 HOH 162 462 827  HOH HOH C . 
EA 6 HOH 163 463 150  HOH HOH C . 
EA 6 HOH 164 464 145  HOH HOH C . 
EA 6 HOH 165 465 653  HOH HOH C . 
EA 6 HOH 166 466 223  HOH HOH C . 
EA 6 HOH 167 467 1270 HOH HOH C . 
EA 6 HOH 168 468 1089 HOH HOH C . 
EA 6 HOH 169 469 527  HOH HOH C . 
EA 6 HOH 170 470 873  HOH HOH C . 
EA 6 HOH 171 471 1368 HOH HOH C . 
EA 6 HOH 172 472 977  HOH HOH C . 
EA 6 HOH 173 473 1486 HOH HOH C . 
EA 6 HOH 174 474 759  HOH HOH C . 
EA 6 HOH 175 475 1096 HOH HOH C . 
EA 6 HOH 176 476 563  HOH HOH C . 
EA 6 HOH 177 477 1288 HOH HOH C . 
EA 6 HOH 178 478 967  HOH HOH C . 
EA 6 HOH 179 479 513  HOH HOH C . 
EA 6 HOH 180 480 1487 HOH HOH C . 
EA 6 HOH 181 481 663  HOH HOH C . 
EA 6 HOH 182 482 1085 HOH HOH C . 
FA 6 HOH 1   301 1336 HOH HOH D . 
FA 6 HOH 2   302 1137 HOH HOH D . 
FA 6 HOH 3   303 1455 HOH HOH D . 
FA 6 HOH 4   304 1218 HOH HOH D . 
FA 6 HOH 5   305 246  HOH HOH D . 
FA 6 HOH 6   306 66   HOH HOH D . 
FA 6 HOH 7   307 1456 HOH HOH D . 
FA 6 HOH 8   308 979  HOH HOH D . 
FA 6 HOH 9   309 327  HOH HOH D . 
FA 6 HOH 10  310 298  HOH HOH D . 
FA 6 HOH 11  311 913  HOH HOH D . 
FA 6 HOH 12  312 1212 HOH HOH D . 
FA 6 HOH 13  313 505  HOH HOH D . 
FA 6 HOH 14  314 639  HOH HOH D . 
FA 6 HOH 15  315 1204 HOH HOH D . 
FA 6 HOH 16  316 228  HOH HOH D . 
FA 6 HOH 17  317 1249 HOH HOH D . 
FA 6 HOH 18  318 417  HOH HOH D . 
FA 6 HOH 19  319 326  HOH HOH D . 
FA 6 HOH 20  320 331  HOH HOH D . 
FA 6 HOH 21  321 328  HOH HOH D . 
FA 6 HOH 22  322 152  HOH HOH D . 
FA 6 HOH 23  323 580  HOH HOH D . 
FA 6 HOH 24  324 1215 HOH HOH D . 
FA 6 HOH 25  325 368  HOH HOH D . 
FA 6 HOH 26  326 1016 HOH HOH D . 
FA 6 HOH 27  327 335  HOH HOH D . 
FA 6 HOH 28  328 959  HOH HOH D . 
FA 6 HOH 29  329 657  HOH HOH D . 
FA 6 HOH 30  330 349  HOH HOH D . 
FA 6 HOH 31  331 520  HOH HOH D . 
FA 6 HOH 32  332 69   HOH HOH D . 
FA 6 HOH 33  333 776  HOH HOH D . 
FA 6 HOH 34  334 351  HOH HOH D . 
FA 6 HOH 35  335 1473 HOH HOH D . 
FA 6 HOH 36  336 20   HOH HOH D . 
FA 6 HOH 37  337 1299 HOH HOH D . 
FA 6 HOH 38  338 496  HOH HOH D . 
FA 6 HOH 39  339 670  HOH HOH D . 
FA 6 HOH 40  340 690  HOH HOH D . 
FA 6 HOH 41  341 1283 HOH HOH D . 
FA 6 HOH 42  342 53   HOH HOH D . 
FA 6 HOH 43  343 907  HOH HOH D . 
FA 6 HOH 44  344 1141 HOH HOH D . 
FA 6 HOH 45  345 572  HOH HOH D . 
FA 6 HOH 46  346 123  HOH HOH D . 
FA 6 HOH 47  347 597  HOH HOH D . 
FA 6 HOH 48  348 854  HOH HOH D . 
FA 6 HOH 49  349 334  HOH HOH D . 
FA 6 HOH 50  350 310  HOH HOH D . 
FA 6 HOH 51  351 756  HOH HOH D . 
FA 6 HOH 52  352 202  HOH HOH D . 
FA 6 HOH 53  353 1349 HOH HOH D . 
FA 6 HOH 54  354 1042 HOH HOH D . 
FA 6 HOH 55  355 726  HOH HOH D . 
FA 6 HOH 56  356 254  HOH HOH D . 
FA 6 HOH 57  357 766  HOH HOH D . 
FA 6 HOH 58  358 504  HOH HOH D . 
FA 6 HOH 59  359 19   HOH HOH D . 
FA 6 HOH 60  360 426  HOH HOH D . 
FA 6 HOH 61  361 218  HOH HOH D . 
FA 6 HOH 62  362 439  HOH HOH D . 
FA 6 HOH 63  363 1136 HOH HOH D . 
FA 6 HOH 64  364 1081 HOH HOH D . 
FA 6 HOH 65  365 125  HOH HOH D . 
FA 6 HOH 66  366 1170 HOH HOH D . 
FA 6 HOH 67  367 1443 HOH HOH D . 
FA 6 HOH 68  368 1049 HOH HOH D . 
FA 6 HOH 69  369 437  HOH HOH D . 
FA 6 HOH 70  370 1422 HOH HOH D . 
FA 6 HOH 71  371 532  HOH HOH D . 
FA 6 HOH 72  372 139  HOH HOH D . 
FA 6 HOH 73  373 407  HOH HOH D . 
FA 6 HOH 74  374 280  HOH HOH D . 
FA 6 HOH 75  375 356  HOH HOH D . 
FA 6 HOH 76  376 133  HOH HOH D . 
FA 6 HOH 77  377 1171 HOH HOH D . 
FA 6 HOH 78  378 506  HOH HOH D . 
FA 6 HOH 79  379 241  HOH HOH D . 
FA 6 HOH 80  380 490  HOH HOH D . 
FA 6 HOH 81  381 1131 HOH HOH D . 
FA 6 HOH 82  382 105  HOH HOH D . 
FA 6 HOH 83  383 1472 HOH HOH D . 
FA 6 HOH 84  384 556  HOH HOH D . 
FA 6 HOH 85  385 603  HOH HOH D . 
FA 6 HOH 86  386 479  HOH HOH D . 
FA 6 HOH 87  387 926  HOH HOH D . 
FA 6 HOH 88  388 411  HOH HOH D . 
FA 6 HOH 89  389 346  HOH HOH D . 
FA 6 HOH 90  390 273  HOH HOH D . 
FA 6 HOH 91  391 994  HOH HOH D . 
FA 6 HOH 92  392 715  HOH HOH D . 
FA 6 HOH 93  393 378  HOH HOH D . 
FA 6 HOH 94  394 1278 HOH HOH D . 
FA 6 HOH 95  395 975  HOH HOH D . 
FA 6 HOH 96  396 787  HOH HOH D . 
FA 6 HOH 97  397 927  HOH HOH D . 
FA 6 HOH 98  398 1236 HOH HOH D . 
FA 6 HOH 99  399 578  HOH HOH D . 
FA 6 HOH 100 400 1232 HOH HOH D . 
FA 6 HOH 101 401 589  HOH HOH D . 
FA 6 HOH 102 402 707  HOH HOH D . 
FA 6 HOH 103 403 380  HOH HOH D . 
FA 6 HOH 104 404 413  HOH HOH D . 
FA 6 HOH 105 405 1330 HOH HOH D . 
FA 6 HOH 106 406 1268 HOH HOH D . 
FA 6 HOH 107 407 646  HOH HOH D . 
FA 6 HOH 108 408 1326 HOH HOH D . 
FA 6 HOH 109 409 668  HOH HOH D . 
FA 6 HOH 110 410 1345 HOH HOH D . 
FA 6 HOH 111 411 484  HOH HOH D . 
FA 6 HOH 112 412 594  HOH HOH D . 
FA 6 HOH 113 413 448  HOH HOH D . 
FA 6 HOH 114 414 1333 HOH HOH D . 
FA 6 HOH 115 415 1454 HOH HOH D . 
FA 6 HOH 116 416 1097 HOH HOH D . 
FA 6 HOH 117 417 481  HOH HOH D . 
FA 6 HOH 118 418 1396 HOH HOH D . 
FA 6 HOH 119 419 1384 HOH HOH D . 
FA 6 HOH 120 420 358  HOH HOH D . 
FA 6 HOH 121 421 1371 HOH HOH D . 
FA 6 HOH 122 422 1053 HOH HOH D . 
FA 6 HOH 123 423 1025 HOH HOH D . 
FA 6 HOH 124 424 1354 HOH HOH D . 
FA 6 HOH 125 425 1332 HOH HOH D . 
FA 6 HOH 126 426 1071 HOH HOH D . 
FA 6 HOH 127 427 1439 HOH HOH D . 
FA 6 HOH 128 428 1328 HOH HOH D . 
FA 6 HOH 129 429 1438 HOH HOH D . 
FA 6 HOH 130 430 935  HOH HOH D . 
FA 6 HOH 131 431 1126 HOH HOH D . 
FA 6 HOH 132 432 406  HOH HOH D . 
FA 6 HOH 133 433 1177 HOH HOH D . 
FA 6 HOH 134 434 1440 HOH HOH D . 
FA 6 HOH 135 435 944  HOH HOH D . 
FA 6 HOH 136 436 1174 HOH HOH D . 
FA 6 HOH 137 437 995  HOH HOH D . 
FA 6 HOH 138 438 1173 HOH HOH D . 
FA 6 HOH 139 439 1019 HOH HOH D . 
FA 6 HOH 140 440 772  HOH HOH D . 
FA 6 HOH 141 441 1047 HOH HOH D . 
FA 6 HOH 142 442 923  HOH HOH D . 
FA 6 HOH 143 443 943  HOH HOH D . 
FA 6 HOH 144 444 1297 HOH HOH D . 
FA 6 HOH 145 445 1449 HOH HOH D . 
GA 6 HOH 1   301 214  HOH HOH E . 
GA 6 HOH 2   302 754  HOH HOH E . 
GA 6 HOH 3   303 436  HOH HOH E . 
GA 6 HOH 4   304 1427 HOH HOH E . 
GA 6 HOH 5   305 1201 HOH HOH E . 
GA 6 HOH 6   306 599  HOH HOH E . 
GA 6 HOH 7   307 729  HOH HOH E . 
GA 6 HOH 8   308 197  HOH HOH E . 
GA 6 HOH 9   309 1373 HOH HOH E . 
GA 6 HOH 10  310 661  HOH HOH E . 
GA 6 HOH 11  311 1231 HOH HOH E . 
GA 6 HOH 12  312 758  HOH HOH E . 
GA 6 HOH 13  313 67   HOH HOH E . 
GA 6 HOH 14  314 643  HOH HOH E . 
GA 6 HOH 15  315 866  HOH HOH E . 
GA 6 HOH 16  316 879  HOH HOH E . 
GA 6 HOH 17  317 186  HOH HOH E . 
GA 6 HOH 18  318 1229 HOH HOH E . 
GA 6 HOH 19  319 618  HOH HOH E . 
GA 6 HOH 20  320 1267 HOH HOH E . 
GA 6 HOH 21  321 420  HOH HOH E . 
GA 6 HOH 22  322 731  HOH HOH E . 
GA 6 HOH 23  323 86   HOH HOH E . 
GA 6 HOH 24  324 304  HOH HOH E . 
GA 6 HOH 25  325 788  HOH HOH E . 
GA 6 HOH 26  326 899  HOH HOH E . 
GA 6 HOH 27  327 1399 HOH HOH E . 
GA 6 HOH 28  328 189  HOH HOH E . 
GA 6 HOH 29  329 226  HOH HOH E . 
GA 6 HOH 30  330 1275 HOH HOH E . 
GA 6 HOH 31  331 611  HOH HOH E . 
GA 6 HOH 32  332 1161 HOH HOH E . 
GA 6 HOH 33  333 1227 HOH HOH E . 
GA 6 HOH 34  334 112  HOH HOH E . 
GA 6 HOH 35  335 502  HOH HOH E . 
GA 6 HOH 36  336 466  HOH HOH E . 
GA 6 HOH 37  337 1341 HOH HOH E . 
GA 6 HOH 38  338 552  HOH HOH E . 
GA 6 HOH 39  339 672  HOH HOH E . 
GA 6 HOH 40  340 1445 HOH HOH E . 
GA 6 HOH 41  341 1    HOH HOH E . 
GA 6 HOH 42  342 332  HOH HOH E . 
GA 6 HOH 43  343 185  HOH HOH E . 
GA 6 HOH 44  344 750  HOH HOH E . 
GA 6 HOH 45  345 428  HOH HOH E . 
GA 6 HOH 46  346 1290 HOH HOH E . 
GA 6 HOH 47  347 685  HOH HOH E . 
GA 6 HOH 48  348 1013 HOH HOH E . 
GA 6 HOH 49  349 212  HOH HOH E . 
GA 6 HOH 50  350 47   HOH HOH E . 
GA 6 HOH 51  351 1005 HOH HOH E . 
GA 6 HOH 52  352 415  HOH HOH E . 
GA 6 HOH 53  353 734  HOH HOH E . 
GA 6 HOH 54  354 941  HOH HOH E . 
GA 6 HOH 55  355 15   HOH HOH E . 
GA 6 HOH 56  356 99   HOH HOH E . 
GA 6 HOH 57  357 75   HOH HOH E . 
GA 6 HOH 58  358 130  HOH HOH E . 
GA 6 HOH 59  359 180  HOH HOH E . 
GA 6 HOH 60  360 1093 HOH HOH E . 
GA 6 HOH 61  361 21   HOH HOH E . 
GA 6 HOH 62  362 84   HOH HOH E . 
GA 6 HOH 63  363 179  HOH HOH E . 
GA 6 HOH 64  364 816  HOH HOH E . 
GA 6 HOH 65  365 440  HOH HOH E . 
GA 6 HOH 66  366 30   HOH HOH E . 
GA 6 HOH 67  367 1152 HOH HOH E . 
GA 6 HOH 68  368 1038 HOH HOH E . 
GA 6 HOH 69  369 917  HOH HOH E . 
GA 6 HOH 70  370 33   HOH HOH E . 
GA 6 HOH 71  371 842  HOH HOH E . 
GA 6 HOH 72  372 483  HOH HOH E . 
GA 6 HOH 73  373 1262 HOH HOH E . 
GA 6 HOH 74  374 753  HOH HOH E . 
GA 6 HOH 75  375 140  HOH HOH E . 
GA 6 HOH 76  376 85   HOH HOH E . 
GA 6 HOH 77  377 103  HOH HOH E . 
GA 6 HOH 78  378 72   HOH HOH E . 
GA 6 HOH 79  379 106  HOH HOH E . 
GA 6 HOH 80  380 433  HOH HOH E . 
GA 6 HOH 81  381 95   HOH HOH E . 
GA 6 HOH 82  382 210  HOH HOH E . 
GA 6 HOH 83  383 268  HOH HOH E . 
GA 6 HOH 84  384 1358 HOH HOH E . 
GA 6 HOH 85  385 60   HOH HOH E . 
GA 6 HOH 86  386 1271 HOH HOH E . 
GA 6 HOH 87  387 1392 HOH HOH E . 
GA 6 HOH 88  388 868  HOH HOH E . 
GA 6 HOH 89  389 565  HOH HOH E . 
GA 6 HOH 90  390 91   HOH HOH E . 
GA 6 HOH 91  391 257  HOH HOH E . 
GA 6 HOH 92  392 1463 HOH HOH E . 
GA 6 HOH 93  393 676  HOH HOH E . 
GA 6 HOH 94  394 1122 HOH HOH E . 
GA 6 HOH 95  395 631  HOH HOH E . 
GA 6 HOH 96  396 83   HOH HOH E . 
GA 6 HOH 97  397 56   HOH HOH E . 
GA 6 HOH 98  398 341  HOH HOH E . 
GA 6 HOH 99  399 447  HOH HOH E . 
GA 6 HOH 100 400 1087 HOH HOH E . 
GA 6 HOH 101 401 1160 HOH HOH E . 
GA 6 HOH 102 402 65   HOH HOH E . 
GA 6 HOH 103 403 115  HOH HOH E . 
GA 6 HOH 104 404 344  HOH HOH E . 
GA 6 HOH 105 405 141  HOH HOH E . 
GA 6 HOH 106 406 516  HOH HOH E . 
GA 6 HOH 107 407 121  HOH HOH E . 
GA 6 HOH 108 408 623  HOH HOH E . 
GA 6 HOH 109 409 1056 HOH HOH E . 
GA 6 HOH 110 410 878  HOH HOH E . 
GA 6 HOH 111 411 400  HOH HOH E . 
GA 6 HOH 112 412 1022 HOH HOH E . 
GA 6 HOH 113 413 324  HOH HOH E . 
GA 6 HOH 114 414 144  HOH HOH E . 
GA 6 HOH 115 415 1148 HOH HOH E . 
GA 6 HOH 116 416 287  HOH HOH E . 
GA 6 HOH 117 417 1317 HOH HOH E . 
GA 6 HOH 118 418 568  HOH HOH E . 
GA 6 HOH 119 419 383  HOH HOH E . 
GA 6 HOH 120 420 901  HOH HOH E . 
GA 6 HOH 121 421 352  HOH HOH E . 
GA 6 HOH 122 422 1272 HOH HOH E . 
GA 6 HOH 123 423 1361 HOH HOH E . 
GA 6 HOH 124 424 282  HOH HOH E . 
GA 6 HOH 125 425 23   HOH HOH E . 
GA 6 HOH 126 426 1165 HOH HOH E . 
GA 6 HOH 127 427 480  HOH HOH E . 
GA 6 HOH 128 428 427  HOH HOH E . 
GA 6 HOH 129 429 609  HOH HOH E . 
GA 6 HOH 130 430 622  HOH HOH E . 
GA 6 HOH 131 431 393  HOH HOH E . 
GA 6 HOH 132 432 784  HOH HOH E . 
GA 6 HOH 133 433 195  HOH HOH E . 
GA 6 HOH 134 434 902  HOH HOH E . 
GA 6 HOH 135 435 1339 HOH HOH E . 
GA 6 HOH 136 436 1367 HOH HOH E . 
GA 6 HOH 137 437 692  HOH HOH E . 
GA 6 HOH 138 438 691  HOH HOH E . 
GA 6 HOH 139 439 1192 HOH HOH E . 
GA 6 HOH 140 440 696  HOH HOH E . 
GA 6 HOH 141 441 1020 HOH HOH E . 
GA 6 HOH 142 442 966  HOH HOH E . 
GA 6 HOH 143 443 933  HOH HOH E . 
GA 6 HOH 144 444 996  HOH HOH E . 
GA 6 HOH 145 445 493  HOH HOH E . 
GA 6 HOH 146 446 775  HOH HOH E . 
GA 6 HOH 147 447 309  HOH HOH E . 
GA 6 HOH 148 448 482  HOH HOH E . 
GA 6 HOH 149 449 894  HOH HOH E . 
GA 6 HOH 150 450 871  HOH HOH E . 
GA 6 HOH 151 451 333  HOH HOH E . 
GA 6 HOH 152 452 1462 HOH HOH E . 
GA 6 HOH 153 453 736  HOH HOH E . 
GA 6 HOH 154 454 863  HOH HOH E . 
GA 6 HOH 155 455 1029 HOH HOH E . 
GA 6 HOH 156 456 1226 HOH HOH E . 
GA 6 HOH 157 457 1409 HOH HOH E . 
GA 6 HOH 158 458 533  HOH HOH E . 
GA 6 HOH 159 459 915  HOH HOH E . 
GA 6 HOH 160 460 405  HOH HOH E . 
GA 6 HOH 161 461 1233 HOH HOH E . 
GA 6 HOH 162 462 1248 HOH HOH E . 
GA 6 HOH 163 463 800  HOH HOH E . 
GA 6 HOH 164 464 1139 HOH HOH E . 
GA 6 HOH 165 465 1034 HOH HOH E . 
GA 6 HOH 166 466 711  HOH HOH E . 
GA 6 HOH 167 467 1289 HOH HOH E . 
GA 6 HOH 168 468 157  HOH HOH E . 
GA 6 HOH 169 469 146  HOH HOH E . 
GA 6 HOH 170 470 679  HOH HOH E . 
GA 6 HOH 171 471 1376 HOH HOH E . 
GA 6 HOH 172 472 1062 HOH HOH E . 
GA 6 HOH 173 473 561  HOH HOH E . 
GA 6 HOH 174 474 1400 HOH HOH E . 
GA 6 HOH 175 475 283  HOH HOH E . 
GA 6 HOH 176 476 706  HOH HOH E . 
GA 6 HOH 177 477 1157 HOH HOH E . 
GA 6 HOH 178 478 745  HOH HOH E . 
GA 6 HOH 179 479 1202 HOH HOH E . 
GA 6 HOH 180 480 1175 HOH HOH E . 
GA 6 HOH 181 481 914  HOH HOH E . 
GA 6 HOH 182 482 999  HOH HOH E . 
GA 6 HOH 183 483 1193 HOH HOH E . 
GA 6 HOH 184 484 498  HOH HOH E . 
GA 6 HOH 185 485 701  HOH HOH E . 
GA 6 HOH 186 486 1466 HOH HOH E . 
GA 6 HOH 187 487 1320 HOH HOH E . 
HA 6 HOH 1   301 1322 HOH HOH F . 
HA 6 HOH 2   302 1112 HOH HOH F . 
HA 6 HOH 3   303 1014 HOH HOH F . 
HA 6 HOH 4   304 1415 HOH HOH F . 
HA 6 HOH 5   305 732  HOH HOH F . 
HA 6 HOH 6   306 288  HOH HOH F . 
HA 6 HOH 7   307 508  HOH HOH F . 
HA 6 HOH 8   308 1269 HOH HOH F . 
HA 6 HOH 9   309 921  HOH HOH F . 
HA 6 HOH 10  310 284  HOH HOH F . 
HA 6 HOH 11  311 1450 HOH HOH F . 
HA 6 HOH 12  312 293  HOH HOH F . 
HA 6 HOH 13  313 1167 HOH HOH F . 
HA 6 HOH 14  314 1424 HOH HOH F . 
HA 6 HOH 15  315 488  HOH HOH F . 
HA 6 HOH 16  316 469  HOH HOH F . 
HA 6 HOH 17  317 573  HOH HOH F . 
HA 6 HOH 18  318 1264 HOH HOH F . 
HA 6 HOH 19  319 43   HOH HOH F . 
HA 6 HOH 20  320 373  HOH HOH F . 
HA 6 HOH 21  321 1216 HOH HOH F . 
HA 6 HOH 22  322 161  HOH HOH F . 
HA 6 HOH 23  323 1220 HOH HOH F . 
HA 6 HOH 24  324 120  HOH HOH F . 
HA 6 HOH 25  325 641  HOH HOH F . 
HA 6 HOH 26  326 163  HOH HOH F . 
HA 6 HOH 27  327 1050 HOH HOH F . 
HA 6 HOH 28  328 460  HOH HOH F . 
HA 6 HOH 29  329 136  HOH HOH F . 
HA 6 HOH 30  330 199  HOH HOH F . 
HA 6 HOH 31  331 624  HOH HOH F . 
HA 6 HOH 32  332 601  HOH HOH F . 
HA 6 HOH 33  333 1188 HOH HOH F . 
HA 6 HOH 34  334 1309 HOH HOH F . 
HA 6 HOH 35  335 1070 HOH HOH F . 
HA 6 HOH 36  336 251  HOH HOH F . 
HA 6 HOH 37  337 1109 HOH HOH F . 
HA 6 HOH 38  338 1479 HOH HOH F . 
HA 6 HOH 39  339 720  HOH HOH F . 
HA 6 HOH 40  340 491  HOH HOH F . 
HA 6 HOH 41  341 45   HOH HOH F . 
HA 6 HOH 42  342 323  HOH HOH F . 
HA 6 HOH 43  343 387  HOH HOH F . 
HA 6 HOH 44  344 1224 HOH HOH F . 
HA 6 HOH 45  345 1164 HOH HOH F . 
HA 6 HOH 46  346 299  HOH HOH F . 
HA 6 HOH 47  347 1459 HOH HOH F . 
HA 6 HOH 48  348 1159 HOH HOH F . 
HA 6 HOH 49  349 1464 HOH HOH F . 
HA 6 HOH 50  350 445  HOH HOH F . 
HA 6 HOH 51  351 723  HOH HOH F . 
HA 6 HOH 52  352 118  HOH HOH F . 
HA 6 HOH 53  353 198  HOH HOH F . 
HA 6 HOH 54  354 1181 HOH HOH F . 
HA 6 HOH 55  355 946  HOH HOH F . 
HA 6 HOH 56  356 733  HOH HOH F . 
HA 6 HOH 57  357 612  HOH HOH F . 
HA 6 HOH 58  358 296  HOH HOH F . 
HA 6 HOH 59  359 1255 HOH HOH F . 
HA 6 HOH 60  360 562  HOH HOH F . 
HA 6 HOH 61  361 114  HOH HOH F . 
HA 6 HOH 62  362 1306 HOH HOH F . 
HA 6 HOH 63  363 517  HOH HOH F . 
HA 6 HOH 64  364 953  HOH HOH F . 
HA 6 HOH 65  365 1119 HOH HOH F . 
HA 6 HOH 66  366 425  HOH HOH F . 
HA 6 HOH 67  367 429  HOH HOH F . 
HA 6 HOH 68  368 1337 HOH HOH F . 
HA 6 HOH 69  369 769  HOH HOH F . 
HA 6 HOH 70  370 997  HOH HOH F . 
HA 6 HOH 71  371 1134 HOH HOH F . 
HA 6 HOH 72  372 564  HOH HOH F . 
HA 6 HOH 73  373 1418 HOH HOH F . 
HA 6 HOH 74  374 247  HOH HOH F . 
HA 6 HOH 75  375 1307 HOH HOH F . 
HA 6 HOH 76  376 1329 HOH HOH F . 
HA 6 HOH 77  377 255  HOH HOH F . 
HA 6 HOH 78  378 709  HOH HOH F . 
HA 6 HOH 79  379 724  HOH HOH F . 
HA 6 HOH 80  380 1324 HOH HOH F . 
HA 6 HOH 81  381 1058 HOH HOH F . 
HA 6 HOH 82  382 1380 HOH HOH F . 
HA 6 HOH 83  383 602  HOH HOH F . 
HA 6 HOH 84  384 312  HOH HOH F . 
HA 6 HOH 85  385 764  HOH HOH F . 
HA 6 HOH 86  386 1190 HOH HOH F . 
HA 6 HOH 87  387 545  HOH HOH F . 
HA 6 HOH 88  388 364  HOH HOH F . 
HA 6 HOH 89  389 905  HOH HOH F . 
HA 6 HOH 90  390 1241 HOH HOH F . 
HA 6 HOH 91  391 891  HOH HOH F . 
HA 6 HOH 92  392 546  HOH HOH F . 
HA 6 HOH 93  393 823  HOH HOH F . 
HA 6 HOH 94  394 1217 HOH HOH F . 
HA 6 HOH 95  395 880  HOH HOH F . 
HA 6 HOH 96  396 852  HOH HOH F . 
HA 6 HOH 97  397 964  HOH HOH F . 
HA 6 HOH 98  398 992  HOH HOH F . 
HA 6 HOH 99  399 1015 HOH HOH F . 
HA 6 HOH 100 400 1460 HOH HOH F . 
HA 6 HOH 101 401 704  HOH HOH F . 
HA 6 HOH 102 402 366  HOH HOH F . 
HA 6 HOH 103 403 1172 HOH HOH F . 
HA 6 HOH 104 404 1378 HOH HOH F . 
HA 6 HOH 105 405 717  HOH HOH F . 
HA 6 HOH 106 406 1055 HOH HOH F . 
HA 6 HOH 107 407 939  HOH HOH F . 
HA 6 HOH 108 408 1205 HOH HOH F . 
HA 6 HOH 109 409 962  HOH HOH F . 
HA 6 HOH 110 410 1184 HOH HOH F . 
HA 6 HOH 111 411 1155 HOH HOH F . 
HA 6 HOH 112 412 1390 HOH HOH F . 
HA 6 HOH 113 413 472  HOH HOH F . 
HA 6 HOH 114 414 860  HOH HOH F . 
HA 6 HOH 115 415 1319 HOH HOH F . 
HA 6 HOH 116 416 844  HOH HOH F . 
HA 6 HOH 117 417 1405 HOH HOH F . 
HA 6 HOH 118 418 1461 HOH HOH F . 
HA 6 HOH 119 419 1094 HOH HOH F . 
HA 6 HOH 120 420 1429 HOH HOH F . 
HA 6 HOH 121 421 1051 HOH HOH F . 
HA 6 HOH 122 422 801  HOH HOH F . 
HA 6 HOH 123 423 1169 HOH HOH F . 
HA 6 HOH 124 424 586  HOH HOH F . 
HA 6 HOH 125 425 1125 HOH HOH F . 
HA 6 HOH 126 426 1465 HOH HOH F . 
HA 6 HOH 127 427 531  HOH HOH F . 
HA 6 HOH 128 428 1209 HOH HOH F . 
HA 6 HOH 129 429 1467 HOH HOH F . 
IA 6 HOH 1   301 805  HOH HOH G . 
IA 6 HOH 2   302 550  HOH HOH G . 
IA 6 HOH 3   303 92   HOH HOH G . 
IA 6 HOH 4   304 559  HOH HOH G . 
IA 6 HOH 5   305 1080 HOH HOH G . 
IA 6 HOH 6   306 870  HOH HOH G . 
IA 6 HOH 7   307 117  HOH HOH G . 
IA 6 HOH 8   308 993  HOH HOH G . 
IA 6 HOH 9   309 1197 HOH HOH G . 
IA 6 HOH 10  310 743  HOH HOH G . 
IA 6 HOH 11  311 500  HOH HOH G . 
IA 6 HOH 12  312 697  HOH HOH G . 
IA 6 HOH 13  313 404  HOH HOH G . 
IA 6 HOH 14  314 342  HOH HOH G . 
IA 6 HOH 15  315 741  HOH HOH G . 
IA 6 HOH 16  316 629  HOH HOH G . 
IA 6 HOH 17  317 230  HOH HOH G . 
IA 6 HOH 18  318 82   HOH HOH G . 
IA 6 HOH 19  319 560  HOH HOH G . 
IA 6 HOH 20  320 478  HOH HOH G . 
IA 6 HOH 21  321 673  HOH HOH G . 
IA 6 HOH 22  322 957  HOH HOH G . 
IA 6 HOH 23  323 494  HOH HOH G . 
IA 6 HOH 24  324 438  HOH HOH G . 
IA 6 HOH 25  325 951  HOH HOH G . 
IA 6 HOH 26  326 55   HOH HOH G . 
IA 6 HOH 27  327 547  HOH HOH G . 
IA 6 HOH 28  328 31   HOH HOH G . 
IA 6 HOH 29  329 474  HOH HOH G . 
IA 6 HOH 30  330 819  HOH HOH G . 
IA 6 HOH 31  331 422  HOH HOH G . 
IA 6 HOH 32  332 510  HOH HOH G . 
IA 6 HOH 33  333 1187 HOH HOH G . 
IA 6 HOH 34  334 1128 HOH HOH G . 
IA 6 HOH 35  335 1387 HOH HOH G . 
IA 6 HOH 36  336 446  HOH HOH G . 
IA 6 HOH 37  337 350  HOH HOH G . 
IA 6 HOH 38  338 441  HOH HOH G . 
IA 6 HOH 39  339 458  HOH HOH G . 
IA 6 HOH 40  340 1446 HOH HOH G . 
IA 6 HOH 41  341 610  HOH HOH G . 
IA 6 HOH 42  342 1017 HOH HOH G . 
IA 6 HOH 43  343 553  HOH HOH G . 
IA 6 HOH 44  344 42   HOH HOH G . 
IA 6 HOH 45  345 725  HOH HOH G . 
IA 6 HOH 46  346 783  HOH HOH G . 
IA 6 HOH 47  347 207  HOH HOH G . 
IA 6 HOH 48  348 1030 HOH HOH G . 
IA 6 HOH 49  349 767  HOH HOH G . 
IA 6 HOH 50  350 389  HOH HOH G . 
IA 6 HOH 51  351 1377 HOH HOH G . 
IA 6 HOH 52  352 495  HOH HOH G . 
IA 6 HOH 53  353 379  HOH HOH G . 
IA 6 HOH 54  354 855  HOH HOH G . 
IA 6 HOH 55  355 829  HOH HOH G . 
IA 6 HOH 56  356 300  HOH HOH G . 
IA 6 HOH 57  357 1351 HOH HOH G . 
IA 6 HOH 58  358 1360 HOH HOH G . 
IA 6 HOH 59  359 825  HOH HOH G . 
IA 6 HOH 60  360 884  HOH HOH G . 
IA 6 HOH 61  361 395  HOH HOH G . 
IA 6 HOH 62  362 1168 HOH HOH G . 
IA 6 HOH 63  363 658  HOH HOH G . 
IA 6 HOH 64  364 1219 HOH HOH G . 
IA 6 HOH 65  365 143  HOH HOH G . 
IA 6 HOH 66  366 858  HOH HOH G . 
IA 6 HOH 67  367 409  HOH HOH G . 
IA 6 HOH 68  368 1359 HOH HOH G . 
IA 6 HOH 69  369 1414 HOH HOH G . 
IA 6 HOH 70  370 536  HOH HOH G . 
IA 6 HOH 71  371 1002 HOH HOH G . 
IA 6 HOH 72  372 1073 HOH HOH G . 
IA 6 HOH 73  373 1428 HOH HOH G . 
IA 6 HOH 74  374 191  HOH HOH G . 
IA 6 HOH 75  375 837  HOH HOH G . 
IA 6 HOH 76  376 1235 HOH HOH G . 
IA 6 HOH 77  377 761  HOH HOH G . 
IA 6 HOH 78  378 1076 HOH HOH G . 
IA 6 HOH 79  379 1426 HOH HOH G . 
IA 6 HOH 80  380 1077 HOH HOH G . 
IA 6 HOH 81  381 1078 HOH HOH G . 
IA 6 HOH 82  382 306  HOH HOH G . 
IA 6 HOH 83  383 1046 HOH HOH G . 
IA 6 HOH 84  384 952  HOH HOH G . 
IA 6 HOH 85  385 339  HOH HOH G . 
IA 6 HOH 86  386 1413 HOH HOH G . 
IA 6 HOH 87  387 1000 HOH HOH G . 
IA 6 HOH 88  388 1143 HOH HOH G . 
IA 6 HOH 89  389 1294 HOH HOH G . 
IA 6 HOH 90  390 836  HOH HOH G . 
IA 6 HOH 91  391 703  HOH HOH G . 
IA 6 HOH 92  392 874  HOH HOH G . 
IA 6 HOH 93  393 330  HOH HOH G . 
IA 6 HOH 94  394 912  HOH HOH G . 
IA 6 HOH 95  395 1105 HOH HOH G . 
IA 6 HOH 96  396 856  HOH HOH G . 
IA 6 HOH 97  397 1430 HOH HOH G . 
IA 6 HOH 98  398 1092 HOH HOH G . 
IA 6 HOH 99  399 1075 HOH HOH G . 
IA 6 HOH 100 400 1327 HOH HOH G . 
IA 6 HOH 101 401 875  HOH HOH G . 
IA 6 HOH 102 402 1253 HOH HOH G . 
IA 6 HOH 103 403 632  HOH HOH G . 
IA 6 HOH 104 404 359  HOH HOH G . 
IA 6 HOH 105 405 509  HOH HOH G . 
IA 6 HOH 106 406 1180 HOH HOH G . 
IA 6 HOH 107 407 1451 HOH HOH G . 
IA 6 HOH 108 408 621  HOH HOH G . 
IA 6 HOH 109 409 910  HOH HOH G . 
JA 6 HOH 1   301 773  HOH HOH H . 
JA 6 HOH 2   302 674  HOH HOH H . 
JA 6 HOH 3   303 1225 HOH HOH H . 
JA 6 HOH 4   304 925  HOH HOH H . 
JA 6 HOH 5   305 824  HOH HOH H . 
JA 6 HOH 6   306 932  HOH HOH H . 
JA 6 HOH 7   307 998  HOH HOH H . 
JA 6 HOH 8   308 956  HOH HOH H . 
JA 6 HOH 9   309 818  HOH HOH H . 
JA 6 HOH 10  310 1305 HOH HOH H . 
JA 6 HOH 11  311 864  HOH HOH H . 
JA 6 HOH 12  312 501  HOH HOH H . 
JA 6 HOH 13  313 705  HOH HOH H . 
JA 6 HOH 14  314 583  HOH HOH H . 
JA 6 HOH 15  315 253  HOH HOH H . 
JA 6 HOH 16  316 990  HOH HOH H . 
JA 6 HOH 17  317 627  HOH HOH H . 
JA 6 HOH 18  318 1259 HOH HOH H . 
JA 6 HOH 19  319 234  HOH HOH H . 
JA 6 HOH 20  320 636  HOH HOH H . 
JA 6 HOH 21  321 693  HOH HOH H . 
JA 6 HOH 22  322 1018 HOH HOH H . 
JA 6 HOH 23  323 221  HOH HOH H . 
JA 6 HOH 24  324 435  HOH HOH H . 
JA 6 HOH 25  325 718  HOH HOH H . 
JA 6 HOH 26  326 371  HOH HOH H . 
JA 6 HOH 27  327 850  HOH HOH H . 
JA 6 HOH 28  328 1316 HOH HOH H . 
JA 6 HOH 29  329 1100 HOH HOH H . 
JA 6 HOH 30  330 774  HOH HOH H . 
JA 6 HOH 31  331 635  HOH HOH H . 
JA 6 HOH 32  332 337  HOH HOH H . 
JA 6 HOH 33  333 343  HOH HOH H . 
JA 6 HOH 34  334 204  HOH HOH H . 
JA 6 HOH 35  335 638  HOH HOH H . 
JA 6 HOH 36  336 525  HOH HOH H . 
JA 6 HOH 37  337 619  HOH HOH H . 
JA 6 HOH 38  338 1432 HOH HOH H . 
JA 6 HOH 39  339 1149 HOH HOH H . 
JA 6 HOH 40  340 1145 HOH HOH H . 
JA 6 HOH 41  341 835  HOH HOH H . 
JA 6 HOH 42  342 961  HOH HOH H . 
JA 6 HOH 43  343 455  HOH HOH H . 
JA 6 HOH 44  344 1036 HOH HOH H . 
JA 6 HOH 45  345 44   HOH HOH H . 
JA 6 HOH 46  346 89   HOH HOH H . 
JA 6 HOH 47  347 377  HOH HOH H . 
JA 6 HOH 48  348 38   HOH HOH H . 
JA 6 HOH 49  349 236  HOH HOH H . 
JA 6 HOH 50  350 948  HOH HOH H . 
JA 6 HOH 51  351 1419 HOH HOH H . 
JA 6 HOH 52  352 465  HOH HOH H . 
JA 6 HOH 53  353 1103 HOH HOH H . 
JA 6 HOH 54  354 1344 HOH HOH H . 
JA 6 HOH 55  355 61   HOH HOH H . 
JA 6 HOH 56  356 263  HOH HOH H . 
JA 6 HOH 57  357 662  HOH HOH H . 
JA 6 HOH 58  358 557  HOH HOH H . 
JA 6 HOH 59  359 286  HOH HOH H . 
JA 6 HOH 60  360 278  HOH HOH H . 
JA 6 HOH 61  361 885  HOH HOH H . 
JA 6 HOH 62  362 412  HOH HOH H . 
JA 6 HOH 63  363 374  HOH HOH H . 
JA 6 HOH 64  364 650  HOH HOH H . 
JA 6 HOH 65  365 540  HOH HOH H . 
JA 6 HOH 66  366 1254 HOH HOH H . 
JA 6 HOH 67  367 644  HOH HOH H . 
JA 6 HOH 68  368 928  HOH HOH H . 
JA 6 HOH 69  369 276  HOH HOH H . 
JA 6 HOH 70  370 677  HOH HOH H . 
JA 6 HOH 71  371 569  HOH HOH H . 
JA 6 HOH 72  372 355  HOH HOH H . 
JA 6 HOH 73  373 277  HOH HOH H . 
JA 6 HOH 74  374 843  HOH HOH H . 
JA 6 HOH 75  375 1060 HOH HOH H . 
JA 6 HOH 76  376 591  HOH HOH H . 
JA 6 HOH 77  377 1001 HOH HOH H . 
JA 6 HOH 78  378 918  HOH HOH H . 
JA 6 HOH 79  379 911  HOH HOH H . 
JA 6 HOH 80  380 386  HOH HOH H . 
JA 6 HOH 81  381 54   HOH HOH H . 
JA 6 HOH 82  382 777  HOH HOH H . 
JA 6 HOH 83  383 1478 HOH HOH H . 
JA 6 HOH 84  384 461  HOH HOH H . 
JA 6 HOH 85  385 375  HOH HOH H . 
JA 6 HOH 86  386 1477 HOH HOH H . 
JA 6 HOH 87  387 991  HOH HOH H . 
JA 6 HOH 88  388 347  HOH HOH H . 
JA 6 HOH 89  389 793  HOH HOH H . 
JA 6 HOH 90  390 828  HOH HOH H . 
JA 6 HOH 91  391 1021 HOH HOH H . 
JA 6 HOH 92  392 449  HOH HOH H . 
JA 6 HOH 93  393 135  HOH HOH H . 
JA 6 HOH 94  394 950  HOH HOH H . 
JA 6 HOH 95  395 945  HOH HOH H . 
JA 6 HOH 96  396 960  HOH HOH H . 
JA 6 HOH 97  397 1239 HOH HOH H . 
JA 6 HOH 98  398 980  HOH HOH H . 
JA 6 HOH 99  399 1214 HOH HOH H . 
JA 6 HOH 100 400 1147 HOH HOH H . 
JA 6 HOH 101 401 947  HOH HOH H . 
JA 6 HOH 102 402 1133 HOH HOH H . 
JA 6 HOH 103 403 762  HOH HOH H . 
JA 6 HOH 104 404 881  HOH HOH H . 
JA 6 HOH 105 405 968  HOH HOH H . 
JA 6 HOH 106 406 970  HOH HOH H . 
JA 6 HOH 107 407 1416 HOH HOH H . 
JA 6 HOH 108 408 1191 HOH HOH H . 
JA 6 HOH 109 409 847  HOH HOH H . 
JA 6 HOH 110 410 1178 HOH HOH H . 
JA 6 HOH 111 411 1338 HOH HOH H . 
JA 6 HOH 112 412 1213 HOH HOH H . 
JA 6 HOH 113 413 1135 HOH HOH H . 
JA 6 HOH 114 414 1374 HOH HOH H . 
JA 6 HOH 115 415 1300 HOH HOH H . 
JA 6 HOH 116 416 876  HOH HOH H . 
JA 6 HOH 117 417 1117 HOH HOH H . 
JA 6 HOH 118 418 1203 HOH HOH H . 
JA 6 HOH 119 419 1154 HOH HOH H . 
JA 6 HOH 120 420 1273 HOH HOH H . 
JA 6 HOH 121 421 582  HOH HOH H . 
JA 6 HOH 122 422 1448 HOH HOH H . 
KA 6 HOH 1   301 971  HOH HOH I . 
KA 6 HOH 2   302 1364 HOH HOH I . 
KA 6 HOH 3   303 1090 HOH HOH I . 
KA 6 HOH 4   304 859  HOH HOH I . 
KA 6 HOH 5   305 659  HOH HOH I . 
KA 6 HOH 6   306 834  HOH HOH I . 
KA 6 HOH 7   307 988  HOH HOH I . 
KA 6 HOH 8   308 739  HOH HOH I . 
KA 6 HOH 9   309 900  HOH HOH I . 
KA 6 HOH 10  310 1281 HOH HOH I . 
KA 6 HOH 11  311 307  HOH HOH I . 
KA 6 HOH 12  312 1391 HOH HOH I . 
KA 6 HOH 13  313 285  HOH HOH I . 
KA 6 HOH 14  314 798  HOH HOH I . 
KA 6 HOH 15  315 305  HOH HOH I . 
KA 6 HOH 16  316 357  HOH HOH I . 
KA 6 HOH 17  317 535  HOH HOH I . 
KA 6 HOH 18  318 684  HOH HOH I . 
KA 6 HOH 19  319 963  HOH HOH I . 
KA 6 HOH 20  320 40   HOH HOH I . 
KA 6 HOH 21  321 688  HOH HOH I . 
KA 6 HOH 22  322 1043 HOH HOH I . 
KA 6 HOH 23  323 213  HOH HOH I . 
KA 6 HOH 24  324 1163 HOH HOH I . 
KA 6 HOH 25  325 116  HOH HOH I . 
KA 6 HOH 26  326 289  HOH HOH I . 
KA 6 HOH 27  327 450  HOH HOH I . 
KA 6 HOH 28  328 101  HOH HOH I . 
KA 6 HOH 29  329 955  HOH HOH I . 
KA 6 HOH 30  330 1091 HOH HOH I . 
KA 6 HOH 31  331 7    HOH HOH I . 
KA 6 HOH 32  332 220  HOH HOH I . 
KA 6 HOH 33  333 1007 HOH HOH I . 
KA 6 HOH 34  334 887  HOH HOH I . 
KA 6 HOH 35  335 549  HOH HOH I . 
KA 6 HOH 36  336 50   HOH HOH I . 
KA 6 HOH 37  337 188  HOH HOH I . 
KA 6 HOH 38  338 456  HOH HOH I . 
KA 6 HOH 39  339 1067 HOH HOH I . 
KA 6 HOH 40  340 1083 HOH HOH I . 
KA 6 HOH 41  341 385  HOH HOH I . 
KA 6 HOH 42  342 399  HOH HOH I . 
KA 6 HOH 43  343 973  HOH HOH I . 
KA 6 HOH 44  344 96   HOH HOH I . 
KA 6 HOH 45  345 1365 HOH HOH I . 
KA 6 HOH 46  346 757  HOH HOH I . 
KA 6 HOH 47  347 607  HOH HOH I . 
KA 6 HOH 48  348 1237 HOH HOH I . 
KA 6 HOH 49  349 637  HOH HOH I . 
KA 6 HOH 50  350 423  HOH HOH I . 
KA 6 HOH 51  351 642  HOH HOH I . 
KA 6 HOH 52  352 593  HOH HOH I . 
KA 6 HOH 53  353 830  HOH HOH I . 
KA 6 HOH 54  354 87   HOH HOH I . 
KA 6 HOH 55  355 730  HOH HOH I . 
KA 6 HOH 56  356 846  HOH HOH I . 
KA 6 HOH 57  357 215  HOH HOH I . 
KA 6 HOH 58  358 529  HOH HOH I . 
KA 6 HOH 59  359 275  HOH HOH I . 
KA 6 HOH 60  360 336  HOH HOH I . 
KA 6 HOH 61  361 88   HOH HOH I . 
KA 6 HOH 62  362 165  HOH HOH I . 
KA 6 HOH 63  363 78   HOH HOH I . 
KA 6 HOH 64  364 865  HOH HOH I . 
KA 6 HOH 65  365 826  HOH HOH I . 
KA 6 HOH 66  366 1314 HOH HOH I . 
KA 6 HOH 67  367 308  HOH HOH I . 
KA 6 HOH 68  368 804  HOH HOH I . 
KA 6 HOH 69  369 1110 HOH HOH I . 
KA 6 HOH 70  370 1114 HOH HOH I . 
KA 6 HOH 71  371 219  HOH HOH I . 
KA 6 HOH 72  372 242  HOH HOH I . 
KA 6 HOH 73  373 755  HOH HOH I . 
KA 6 HOH 74  374 477  HOH HOH I . 
KA 6 HOH 75  375 442  HOH HOH I . 
KA 6 HOH 76  376 974  HOH HOH I . 
KA 6 HOH 77  377 1431 HOH HOH I . 
KA 6 HOH 78  378 1343 HOH HOH I . 
KA 6 HOH 79  379 367  HOH HOH I . 
KA 6 HOH 80  380 1243 HOH HOH I . 
KA 6 HOH 81  381 1366 HOH HOH I . 
KA 6 HOH 82  382 1251 HOH HOH I . 
KA 6 HOH 83  383 274  HOH HOH I . 
KA 6 HOH 84  384 710  HOH HOH I . 
KA 6 HOH 85  385 1059 HOH HOH I . 
KA 6 HOH 86  386 249  HOH HOH I . 
KA 6 HOH 87  387 104  HOH HOH I . 
KA 6 HOH 88  388 861  HOH HOH I . 
KA 6 HOH 89  389 1308 HOH HOH I . 
KA 6 HOH 90  390 1357 HOH HOH I . 
KA 6 HOH 91  391 1382 HOH HOH I . 
KA 6 HOH 92  392 486  HOH HOH I . 
KA 6 HOH 93  393 497  HOH HOH I . 
KA 6 HOH 94  394 462  HOH HOH I . 
KA 6 HOH 95  395 791  HOH HOH I . 
KA 6 HOH 96  396 897  HOH HOH I . 
KA 6 HOH 97  397 1397 HOH HOH I . 
KA 6 HOH 98  398 596  HOH HOH I . 
KA 6 HOH 99  399 388  HOH HOH I . 
KA 6 HOH 100 400 1279 HOH HOH I . 
KA 6 HOH 101 401 1223 HOH HOH I . 
KA 6 HOH 102 402 678  HOH HOH I . 
KA 6 HOH 103 403 982  HOH HOH I . 
KA 6 HOH 104 404 1211 HOH HOH I . 
KA 6 HOH 105 405 747  HOH HOH I . 
KA 6 HOH 106 406 473  HOH HOH I . 
KA 6 HOH 107 407 534  HOH HOH I . 
KA 6 HOH 108 408 1198 HOH HOH I . 
KA 6 HOH 109 409 893  HOH HOH I . 
KA 6 HOH 110 410 1146 HOH HOH I . 
KA 6 HOH 111 411 1158 HOH HOH I . 
KA 6 HOH 112 412 1088 HOH HOH I . 
KA 6 HOH 113 413 1410 HOH HOH I . 
KA 6 HOH 114 414 537  HOH HOH I . 
KA 6 HOH 115 415 1230 HOH HOH I . 
KA 6 HOH 116 416 1457 HOH HOH I . 
KA 6 HOH 117 417 1274 HOH HOH I . 
KA 6 HOH 118 418 1257 HOH HOH I . 
KA 6 HOH 119 419 1280 HOH HOH I . 
KA 6 HOH 120 420 464  HOH HOH I . 
KA 6 HOH 121 421 1032 HOH HOH I . 
KA 6 HOH 122 422 1362 HOH HOH I . 
KA 6 HOH 123 423 396  HOH HOH I . 
KA 6 HOH 124 424 1084 HOH HOH I . 
KA 6 HOH 125 425 972  HOH HOH I . 
KA 6 HOH 126 426 1186 HOH HOH I . 
KA 6 HOH 127 427 1121 HOH HOH I . 
KA 6 HOH 128 428 538  HOH HOH I . 
KA 6 HOH 129 429 294  HOH HOH I . 
KA 6 HOH 130 430 1044 HOH HOH I . 
KA 6 HOH 131 431 402  HOH HOH I . 
KA 6 HOH 132 432 954  HOH HOH I . 
KA 6 HOH 133 433 807  HOH HOH I . 
KA 6 HOH 134 434 1350 HOH HOH I . 
KA 6 HOH 135 435 616  HOH HOH I . 
KA 6 HOH 136 436 857  HOH HOH I . 
KA 6 HOH 137 437 1107 HOH HOH I . 
KA 6 HOH 138 438 384  HOH HOH I . 
KA 6 HOH 139 439 817  HOH HOH I . 
KA 6 HOH 140 440 808  HOH HOH I . 
KA 6 HOH 141 441 1401 HOH HOH I . 
KA 6 HOH 142 442 630  HOH HOH I . 
LA 6 HOH 1   201 1433 HOH HOH J . 
LA 6 HOH 2   202 1406 HOH HOH J . 
LA 6 HOH 3   203 266  HOH HOH J . 
LA 6 HOH 4   204 1250 HOH HOH J . 
LA 6 HOH 5   205 1104 HOH HOH J . 
LA 6 HOH 6   206 444  HOH HOH J . 
LA 6 HOH 7   207 1363 HOH HOH J . 
LA 6 HOH 8   208 1200 HOH HOH J . 
LA 6 HOH 9   209 1404 HOH HOH J . 
LA 6 HOH 10  210 1245 HOH HOH J . 
LA 6 HOH 11  211 576  HOH HOH J . 
LA 6 HOH 12  212 765  HOH HOH J . 
LA 6 HOH 13  213 1041 HOH HOH J . 
LA 6 HOH 14  214 160  HOH HOH J . 
LA 6 HOH 15  215 522  HOH HOH J . 
LA 6 HOH 16  216 128  HOH HOH J . 
LA 6 HOH 17  217 68   HOH HOH J . 
LA 6 HOH 18  218 654  HOH HOH J . 
LA 6 HOH 19  219 645  HOH HOH J . 
LA 6 HOH 20  220 797  HOH HOH J . 
LA 6 HOH 21  221 749  HOH HOH J . 
LA 6 HOH 22  222 1370 HOH HOH J . 
LA 6 HOH 23  223 1079 HOH HOH J . 
LA 6 HOH 24  224 680  HOH HOH J . 
LA 6 HOH 25  225 544  HOH HOH J . 
LA 6 HOH 26  226 779  HOH HOH J . 
LA 6 HOH 27  227 1153 HOH HOH J . 
LA 6 HOH 28  228 233  HOH HOH J . 
LA 6 HOH 29  229 142  HOH HOH J . 
LA 6 HOH 30  230 519  HOH HOH J . 
LA 6 HOH 31  231 1072 HOH HOH J . 
LA 6 HOH 32  232 548  HOH HOH J . 
LA 6 HOH 33  233 507  HOH HOH J . 
LA 6 HOH 34  234 814  HOH HOH J . 
LA 6 HOH 35  235 1150 HOH HOH J . 
LA 6 HOH 36  236 1052 HOH HOH J . 
LA 6 HOH 37  237 1004 HOH HOH J . 
LA 6 HOH 38  238 1296 HOH HOH J . 
LA 6 HOH 39  239 1285 HOH HOH J . 
LA 6 HOH 40  240 686  HOH HOH J . 
LA 6 HOH 41  241 938  HOH HOH J . 
LA 6 HOH 42  242 487  HOH HOH J . 
LA 6 HOH 43  243 1003 HOH HOH J . 
LA 6 HOH 44  244 216  HOH HOH J . 
LA 6 HOH 45  245 1452 HOH HOH J . 
LA 6 HOH 46  246 1355 HOH HOH J . 
LA 6 HOH 47  247 949  HOH HOH J . 
LA 6 HOH 48  248 551  HOH HOH J . 
LA 6 HOH 49  249 424  HOH HOH J . 
LA 6 HOH 50  250 1066 HOH HOH J . 
LA 6 HOH 51  251 134  HOH HOH J . 
LA 6 HOH 52  252 1298 HOH HOH J . 
LA 6 HOH 53  253 667  HOH HOH J . 
LA 6 HOH 54  254 832  HOH HOH J . 
LA 6 HOH 55  255 1111 HOH HOH J . 
LA 6 HOH 56  256 419  HOH HOH J . 
LA 6 HOH 57  257 768  HOH HOH J . 
LA 6 HOH 58  258 936  HOH HOH J . 
LA 6 HOH 59  259 1068 HOH HOH J . 
LA 6 HOH 60  260 1010 HOH HOH J . 
LA 6 HOH 61  261 1304 HOH HOH J . 
LA 6 HOH 62  262 681  HOH HOH J . 
LA 6 HOH 63  263 1408 HOH HOH J . 
LA 6 HOH 64  264 595  HOH HOH J . 
LA 6 HOH 65  265 421  HOH HOH J . 
LA 6 HOH 66  266 903  HOH HOH J . 
LA 6 HOH 67  267 1246 HOH HOH J . 
LA 6 HOH 68  268 1054 HOH HOH J . 
LA 6 HOH 69  269 930  HOH HOH J . 
LA 6 HOH 70  270 408  HOH HOH J . 
LA 6 HOH 71  271 1334 HOH HOH J . 
LA 6 HOH 72  272 1101 HOH HOH J . 
LA 6 HOH 73  273 1208 HOH HOH J . 
LA 6 HOH 74  274 1263 HOH HOH J . 
LA 6 HOH 75  275 744  HOH HOH J . 
LA 6 HOH 76  276 1342 HOH HOH J . 
LA 6 HOH 77  277 1442 HOH HOH J . 
LA 6 HOH 78  278 702  HOH HOH J . 
LA 6 HOH 79  279 1182 HOH HOH J . 
LA 6 HOH 80  280 430  HOH HOH J . 
LA 6 HOH 81  281 1444 HOH HOH J . 
LA 6 HOH 82  282 1222 HOH HOH J . 
LA 6 HOH 83  283 862  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,CA,DA 
2 1 C,D,Q,R,S,T,U,EA,FA   
3 1 E,F,V,W,X,GA,HA       
4 1 G,H,Y,Z,AA,IA,JA      
5 1 I,J,BA,KA,LA          
# 
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)' 2300  ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  14240 ? 
2 'ABSA (A^2)' 2080  ? 
2 MORE         -23   ? 
2 'SSA (A^2)'  14160 ? 
3 'ABSA (A^2)' 1840  ? 
3 MORE         -24   ? 
3 'SSA (A^2)'  14170 ? 
4 'ABSA (A^2)' 1420  ? 
4 MORE         -11   ? 
4 'SSA (A^2)'  14220 ? 
5 'ABSA (A^2)' 1410  ? 
5 MORE         -11   ? 
5 'SSA (A^2)'  12870 ? 
# 
_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 90  ? A HIS 63 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 98  ? A HIS 71 ? 1_555 106.3 ? 
2  ND1 ? A HIS 90  ? A HIS 63 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 107 ? A HIS 80 ? 1_555 116.6 ? 
3  ND1 ? A HIS 98  ? A HIS 71 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 107 ? A HIS 80 ? 1_555 122.9 ? 
4  ND1 ? A HIS 90  ? A HIS 63 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 110 ? A ASP 83 ? 1_555 105.9 ? 
5  ND1 ? A HIS 98  ? A HIS 71 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 110 ? A ASP 83 ? 1_555 86.1  ? 
6  ND1 ? A HIS 107 ? A HIS 80 ? 1_555 ZN ? K  ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 110 ? A ASP 83 ? 1_555 114.2 ? 
7  ND1 ? B HIS 90  ? B HIS 63 ? 1_555 ZN ? M  ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 98  ? B HIS 71 ? 1_555 105.7 ? 
8  ND1 ? B HIS 90  ? B HIS 63 ? 1_555 ZN ? M  ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 107 ? B HIS 80 ? 1_555 110.0 ? 
9  ND1 ? B HIS 98  ? B HIS 71 ? 1_555 ZN ? M  ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 107 ? B HIS 80 ? 1_555 124.9 ? 
10 ND1 ? B HIS 90  ? B HIS 63 ? 1_555 ZN ? M  ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 110 ? B ASP 83 ? 1_555 106.1 ? 
11 ND1 ? B HIS 98  ? B HIS 71 ? 1_555 ZN ? M  ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 110 ? B ASP 83 ? 1_555 93.9  ? 
12 ND1 ? B HIS 107 ? B HIS 80 ? 1_555 ZN ? M  ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 110 ? B ASP 83 ? 1_555 114.0 ? 
13 ND1 ? C HIS 90  ? C HIS 63 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 98  ? C HIS 71 ? 1_555 106.2 ? 
14 ND1 ? C HIS 90  ? C HIS 63 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 107 ? C HIS 80 ? 1_555 112.2 ? 
15 ND1 ? C HIS 98  ? C HIS 71 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 ND1 ? C HIS 107 ? C HIS 80 ? 1_555 123.2 ? 
16 ND1 ? C HIS 90  ? C HIS 63 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 110 ? C ASP 83 ? 1_555 105.1 ? 
17 ND1 ? C HIS 98  ? C HIS 71 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 110 ? C ASP 83 ? 1_555 94.9  ? 
18 ND1 ? C HIS 107 ? C HIS 80 ? 1_555 ZN ? Q  ZN . ? C ZN 201 ? 1_555 OD1 ? C ASP 110 ? C ASP 83 ? 1_555 112.8 ? 
19 ND1 ? D HIS 90  ? D HIS 63 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 98  ? D HIS 71 ? 1_555 100.8 ? 
20 ND1 ? D HIS 90  ? D HIS 63 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 107 ? D HIS 80 ? 1_555 112.5 ? 
21 ND1 ? D HIS 98  ? D HIS 71 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 ND1 ? D HIS 107 ? D HIS 80 ? 1_555 122.9 ? 
22 ND1 ? D HIS 90  ? D HIS 63 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 110 ? D ASP 83 ? 1_555 99.5  ? 
23 ND1 ? D HIS 98  ? D HIS 71 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 110 ? D ASP 83 ? 1_555 96.2  ? 
24 ND1 ? D HIS 107 ? D HIS 80 ? 1_555 ZN ? T  ZN . ? D ZN 201 ? 1_555 OD1 ? D ASP 110 ? D ASP 83 ? 1_555 120.8 ? 
25 ND1 ? E HIS 90  ? E HIS 63 ? 1_555 ZN ? V  ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 98  ? E HIS 71 ? 1_555 104.3 ? 
26 ND1 ? E HIS 90  ? E HIS 63 ? 1_555 ZN ? V  ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 107 ? E HIS 80 ? 1_555 112.0 ? 
27 ND1 ? E HIS 98  ? E HIS 71 ? 1_555 ZN ? V  ZN . ? E ZN 201 ? 1_555 ND1 ? E HIS 107 ? E HIS 80 ? 1_555 124.5 ? 
28 ND1 ? E HIS 90  ? E HIS 63 ? 1_555 ZN ? V  ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 110 ? E ASP 83 ? 1_555 104.1 ? 
29 ND1 ? E HIS 98  ? E HIS 71 ? 1_555 ZN ? V  ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 110 ? E ASP 83 ? 1_555 94.5  ? 
30 ND1 ? E HIS 107 ? E HIS 80 ? 1_555 ZN ? V  ZN . ? E ZN 201 ? 1_555 OD1 ? E ASP 110 ? E ASP 83 ? 1_555 114.6 ? 
31 ND1 ? F HIS 90  ? F HIS 63 ? 1_555 ZN ? X  ZN . ? F ZN 201 ? 1_555 ND1 ? F HIS 98  ? F HIS 71 ? 1_555 97.2  ? 
32 ND1 ? F HIS 90  ? F HIS 63 ? 1_555 ZN ? X  ZN . ? F ZN 201 ? 1_555 ND1 ? F HIS 107 ? F HIS 80 ? 1_555 115.3 ? 
33 ND1 ? F HIS 98  ? F HIS 71 ? 1_555 ZN ? X  ZN . ? F ZN 201 ? 1_555 ND1 ? F HIS 107 ? F HIS 80 ? 1_555 120.7 ? 
34 ND1 ? F HIS 90  ? F HIS 63 ? 1_555 ZN ? X  ZN . ? F ZN 201 ? 1_555 OD1 ? F ASP 110 ? F ASP 83 ? 1_555 103.1 ? 
35 ND1 ? F HIS 98  ? F HIS 71 ? 1_555 ZN ? X  ZN . ? F ZN 201 ? 1_555 OD1 ? F ASP 110 ? F ASP 83 ? 1_555 93.7  ? 
36 ND1 ? F HIS 107 ? F HIS 80 ? 1_555 ZN ? X  ZN . ? F ZN 201 ? 1_555 OD1 ? F ASP 110 ? F ASP 83 ? 1_555 122.1 ? 
37 ND1 ? G HIS 90  ? G HIS 63 ? 1_555 ZN ? Y  ZN . ? G ZN 201 ? 1_555 ND1 ? G HIS 98  ? G HIS 71 ? 1_555 99.0  ? 
38 ND1 ? G HIS 90  ? G HIS 63 ? 1_555 ZN ? Y  ZN . ? G ZN 201 ? 1_555 ND1 ? G HIS 107 ? G HIS 80 ? 1_555 114.8 ? 
39 ND1 ? G HIS 98  ? G HIS 71 ? 1_555 ZN ? Y  ZN . ? G ZN 201 ? 1_555 ND1 ? G HIS 107 ? G HIS 80 ? 1_555 123.9 ? 
40 ND1 ? G HIS 90  ? G HIS 63 ? 1_555 ZN ? Y  ZN . ? G ZN 201 ? 1_555 OD1 ? G ASP 110 ? G ASP 83 ? 1_555 101.9 ? 
41 ND1 ? G HIS 98  ? G HIS 71 ? 1_555 ZN ? Y  ZN . ? G ZN 201 ? 1_555 OD1 ? G ASP 110 ? G ASP 83 ? 1_555 97.3  ? 
42 ND1 ? G HIS 107 ? G HIS 80 ? 1_555 ZN ? Y  ZN . ? G ZN 201 ? 1_555 OD1 ? G ASP 110 ? G ASP 83 ? 1_555 116.2 ? 
43 ND1 ? H HIS 90  ? H HIS 63 ? 1_555 ZN ? Z  ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 98  ? H HIS 71 ? 1_555 100.6 ? 
44 ND1 ? H HIS 90  ? H HIS 63 ? 1_555 ZN ? Z  ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 107 ? H HIS 80 ? 1_555 114.9 ? 
45 ND1 ? H HIS 98  ? H HIS 71 ? 1_555 ZN ? Z  ZN . ? H ZN 201 ? 1_555 ND1 ? H HIS 107 ? H HIS 80 ? 1_555 122.8 ? 
46 ND1 ? H HIS 90  ? H HIS 63 ? 1_555 ZN ? Z  ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 110 ? H ASP 83 ? 1_555 110.3 ? 
47 ND1 ? H HIS 98  ? H HIS 71 ? 1_555 ZN ? Z  ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 110 ? H ASP 83 ? 1_555 95.0  ? 
48 ND1 ? H HIS 107 ? H HIS 80 ? 1_555 ZN ? Z  ZN . ? H ZN 201 ? 1_555 OD1 ? H ASP 110 ? H ASP 83 ? 1_555 111.2 ? 
49 ND1 ? I HIS 90  ? I HIS 63 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 98  ? I HIS 71 ? 1_555 105.4 ? 
50 ND1 ? I HIS 90  ? I HIS 63 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 107 ? I HIS 80 ? 1_555 108.7 ? 
51 ND1 ? I HIS 98  ? I HIS 71 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 ND1 ? I HIS 107 ? I HIS 80 ? 1_555 124.9 ? 
52 ND1 ? I HIS 90  ? I HIS 63 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 110 ? I ASP 83 ? 1_555 105.2 ? 
53 ND1 ? I HIS 98  ? I HIS 71 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 110 ? I ASP 83 ? 1_555 95.6  ? 
54 ND1 ? I HIS 107 ? I HIS 80 ? 1_555 ZN ? BA ZN . ? I ZN 201 ? 1_555 OD1 ? I ASP 110 ? I ASP 83 ? 1_555 114.9 ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2018-11-21 
# 
_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_
_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   ? ? ? 5.7.0029 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .        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 O   C HOH 314 ? ? O  C HOH 335 ? ? 1.78 
2 1 O   D ARG 79  ? ? O  D HOH 301 ? ? 2.01 
3 1 CB  F MET 0   ? ? O  F HOH 413 ? ? 2.08 
4 1 O   G HOH 321 ? ? O  G HOH 400 ? ? 2.08 
5 1 OE1 B GLU 21  ? ? C7 B 946 203 ? ? 2.10 
6 1 O   F GLU 40  ? ? O  F HOH 301 ? ? 2.11 
7 1 O   E HOH 417 ? ? O  E HOH 424 ? ? 2.11 
8 1 O   B HOH 379 ? ? O  B HOH 467 ? ? 2.15 
9 1 O   H HOH 371 ? ? O  H HOH 380 ? ? 2.19 
# 
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 C HOH 446 ? ? 1_555 O D HOH 411 ? ? 10_664 2.12 
2 1 O A HOH 449 ? ? 1_555 O G HOH 382 ? ? 2_655  2.15 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE B ARG 115 ? ? CZ B ARG 115 ? ? NH1 B ARG 115 ? ? 123.41 120.30 3.11  0.50 N 
2 1 NE B ARG 115 ? ? CZ B ARG 115 ? ? NH2 B ARG 115 ? ? 116.89 120.30 -3.41 0.50 N 
3 1 CB E ASP 90  ? ? CG E ASP 90  ? ? OD1 E ASP 90  ? ? 123.82 118.30 5.52  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 F 90  ? ? -69.47  -173.75 
2 1 ARG G 115 ? ? -101.04 -169.56 
3 1 LYS H 136 ? ? -102.36 -66.29  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_1   G 
_pdbx_validate_peptide_omega.auth_seq_id_1    26 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   G 
_pdbx_validate_peptide_omega.auth_seq_id_2    27 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -148.52 
# 
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 471 ? 6.80 . 
2 1 O ? A HOH 472 ? 7.01 . 
3 1 O ? B HOH 517 ? 6.51 . 
4 1 O ? B HOH 518 ? 6.79 . 
5 1 O ? C HOH 480 ? 6.00 . 
6 1 O ? C HOH 481 ? 6.22 . 
7 1 O ? C HOH 482 ? 7.02 . 
8 1 O ? F HOH 429 ? 5.94 . 
9 1 O ? H HOH 422 ? 6.30 . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B MET 0   ? CG  ? B MET 27  CG  
2  1 Y 1 B MET 0   ? SD  ? B MET 27  SD  
3  1 Y 1 B MET 0   ? CE  ? B MET 27  CE  
4  1 Y 1 C MET 0   ? CG  ? C MET 27  CG  
5  1 Y 1 C MET 0   ? SD  ? C MET 27  SD  
6  1 Y 1 C MET 0   ? CE  ? C MET 27  CE  
7  1 Y 1 D MET 0   ? CG  ? D MET 27  CG  
8  1 Y 1 D MET 0   ? SD  ? D MET 27  SD  
9  1 Y 1 D MET 0   ? CE  ? D MET 27  CE  
10 1 Y 1 E MET 0   ? CG  ? E MET 27  CG  
11 1 Y 1 E MET 0   ? SD  ? E MET 27  SD  
12 1 Y 1 E MET 0   ? CE  ? E MET 27  CE  
13 1 Y 1 F MET 0   ? CG  ? F MET 27  CG  
14 1 Y 1 F MET 0   ? SD  ? F MET 27  SD  
15 1 Y 1 F MET 0   ? CE  ? F MET 27  CE  
16 1 Y 1 F LYS 70  ? CG  ? F LYS 97  CG  
17 1 Y 1 F LYS 70  ? CD  ? F LYS 97  CD  
18 1 Y 1 F LYS 70  ? CE  ? F LYS 97  CE  
19 1 Y 1 F LYS 70  ? NZ  ? F LYS 97  NZ  
20 1 Y 1 F GLU 77  ? CG  ? F GLU 104 CG  
21 1 Y 1 F GLU 77  ? CD  ? F GLU 104 CD  
22 1 Y 1 F GLU 77  ? OE1 ? F GLU 104 OE1 
23 1 Y 1 F GLU 77  ? OE2 ? F GLU 104 OE2 
24 1 Y 1 G GLU 24  ? CG  ? G GLU 51  CG  
25 1 Y 1 G GLU 24  ? CD  ? G GLU 51  CD  
26 1 Y 1 G GLU 24  ? OE1 ? G GLU 51  OE1 
27 1 Y 1 G GLU 24  ? OE2 ? G GLU 51  OE2 
28 1 Y 1 G ASN 26  ? CG  ? G ASN 53  CG  
29 1 Y 1 G ASN 26  ? OD1 ? G ASN 53  OD1 
30 1 Y 1 G ASN 26  ? ND2 ? G ASN 53  ND2 
31 1 Y 1 H MET 0   ? CG  ? H MET 27  CG  
32 1 Y 1 H MET 0   ? SD  ? H MET 27  SD  
33 1 Y 1 H MET 0   ? CE  ? H MET 27  CE  
34 1 Y 1 H ASN 26  ? CG  ? H ASN 53  CG  
35 1 Y 1 H ASN 26  ? OD1 ? H ASN 53  OD1 
36 1 Y 1 H ASN 26  ? ND2 ? H ASN 53  ND2 
37 1 Y 1 J LYS 23  ? CG  ? J LYS 50  CG  
38 1 Y 1 J LYS 23  ? CD  ? J LYS 50  CD  
39 1 Y 1 J LYS 23  ? CE  ? J LYS 50  CE  
40 1 Y 1 J LYS 23  ? NZ  ? J LYS 50  NZ  
41 1 Y 1 J GLU 24  ? CG  ? J GLU 51  CG  
42 1 Y 1 J GLU 24  ? CD  ? J GLU 51  CD  
43 1 Y 1 J GLU 24  ? OE1 ? J GLU 51  OE1 
44 1 Y 1 J GLU 24  ? OE2 ? J GLU 51  OE2 
45 1 N 1 D 946 202 ? C8  ? U 946 1   C8  
46 1 N 1 D 946 202 ? C9  ? U 946 1   C9  
47 1 N 1 D 946 202 ? C10 ? U 946 1   C10 
48 1 N 1 D 946 202 ? C11 ? U 946 1   C11 
49 1 N 1 D 946 202 ? C12 ? U 946 1   C12 
50 1 N 1 D 946 202 ? C13 ? U 946 1   C13 
51 1 N 1 D 946 202 ? C14 ? U 946 1   C14 
52 1 N 1 D 946 202 ? C15 ? U 946 1   C15 
53 1 N 1 D 946 202 ? C16 ? U 946 1   C16 
54 1 N 1 D 946 202 ? C17 ? U 946 1   C17 
55 1 N 1 D 946 202 ? C19 ? U 946 1   C19 
56 1 N 1 D 946 202 ? N1  ? U 946 1   N1  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -26 ? A MET 1   
2   1 Y 1 A LYS -25 ? A LYS 2   
3   1 Y 1 A HIS -24 ? A HIS 3   
4   1 Y 1 A HIS -23 ? A HIS 4   
5   1 Y 1 A HIS -22 ? A HIS 5   
6   1 Y 1 A HIS -21 ? A HIS 6   
7   1 Y 1 A HIS -20 ? A HIS 7   
8   1 Y 1 A HIS -19 ? A HIS 8   
9   1 Y 1 A PRO -18 ? A PRO 9   
10  1 Y 1 A MET -17 ? A MET 10  
11  1 Y 1 A SER -16 ? A SER 11  
12  1 Y 1 A ASP -15 ? A ASP 12  
13  1 Y 1 A TYR -14 ? A TYR 13  
14  1 Y 1 A ASP -13 ? A ASP 14  
15  1 Y 1 A ILE -12 ? A ILE 15  
16  1 Y 1 A PRO -11 ? A PRO 16  
17  1 Y 1 A THR -10 ? A THR 17  
18  1 Y 1 A THR -9  ? A THR 18  
19  1 Y 1 A GLU -8  ? A GLU 19  
20  1 Y 1 A ASN -7  ? A ASN 20  
21  1 Y 1 A LEU -6  ? A LEU 21  
22  1 Y 1 A TYR -5  ? A TYR 22  
23  1 Y 1 A PHE -4  ? A PHE 23  
24  1 Y 1 A GLN -3  ? A GLN 24  
25  1 Y 1 A GLY -2  ? A GLY 25  
26  1 Y 1 B MET -26 ? B MET 1   
27  1 Y 1 B LYS -25 ? B LYS 2   
28  1 Y 1 B HIS -24 ? B HIS 3   
29  1 Y 1 B HIS -23 ? B HIS 4   
30  1 Y 1 B HIS -22 ? B HIS 5   
31  1 Y 1 B HIS -21 ? B HIS 6   
32  1 Y 1 B HIS -20 ? B HIS 7   
33  1 Y 1 B HIS -19 ? B HIS 8   
34  1 Y 1 B PRO -18 ? B PRO 9   
35  1 Y 1 B MET -17 ? B MET 10  
36  1 Y 1 B SER -16 ? B SER 11  
37  1 Y 1 B ASP -15 ? B ASP 12  
38  1 Y 1 B TYR -14 ? B TYR 13  
39  1 Y 1 B ASP -13 ? B ASP 14  
40  1 Y 1 B ILE -12 ? B ILE 15  
41  1 Y 1 B PRO -11 ? B PRO 16  
42  1 Y 1 B THR -10 ? B THR 17  
43  1 Y 1 B THR -9  ? B THR 18  
44  1 Y 1 B GLU -8  ? B GLU 19  
45  1 Y 1 B ASN -7  ? B ASN 20  
46  1 Y 1 B LEU -6  ? B LEU 21  
47  1 Y 1 B TYR -5  ? B TYR 22  
48  1 Y 1 B PHE -4  ? B PHE 23  
49  1 Y 1 B GLN -3  ? B GLN 24  
50  1 Y 1 B GLY -2  ? B GLY 25  
51  1 Y 1 B ALA -1  ? B ALA 26  
52  1 Y 1 C MET -26 ? C MET 1   
53  1 Y 1 C LYS -25 ? C LYS 2   
54  1 Y 1 C HIS -24 ? C HIS 3   
55  1 Y 1 C HIS -23 ? C HIS 4   
56  1 Y 1 C HIS -22 ? C HIS 5   
57  1 Y 1 C HIS -21 ? C HIS 6   
58  1 Y 1 C HIS -20 ? C HIS 7   
59  1 Y 1 C HIS -19 ? C HIS 8   
60  1 Y 1 C PRO -18 ? C PRO 9   
61  1 Y 1 C MET -17 ? C MET 10  
62  1 Y 1 C SER -16 ? C SER 11  
63  1 Y 1 C ASP -15 ? C ASP 12  
64  1 Y 1 C TYR -14 ? C TYR 13  
65  1 Y 1 C ASP -13 ? C ASP 14  
66  1 Y 1 C ILE -12 ? C ILE 15  
67  1 Y 1 C PRO -11 ? C PRO 16  
68  1 Y 1 C THR -10 ? C THR 17  
69  1 Y 1 C THR -9  ? C THR 18  
70  1 Y 1 C GLU -8  ? C GLU 19  
71  1 Y 1 C ASN -7  ? C ASN 20  
72  1 Y 1 C LEU -6  ? C LEU 21  
73  1 Y 1 C TYR -5  ? C TYR 22  
74  1 Y 1 C PHE -4  ? C PHE 23  
75  1 Y 1 C GLN -3  ? C GLN 24  
76  1 Y 1 C GLY -2  ? C GLY 25  
77  1 Y 1 C ALA -1  ? C ALA 26  
78  1 Y 1 D MET -26 ? D MET 1   
79  1 Y 1 D LYS -25 ? D LYS 2   
80  1 Y 1 D HIS -24 ? D HIS 3   
81  1 Y 1 D HIS -23 ? D HIS 4   
82  1 Y 1 D HIS -22 ? D HIS 5   
83  1 Y 1 D HIS -21 ? D HIS 6   
84  1 Y 1 D HIS -20 ? D HIS 7   
85  1 Y 1 D HIS -19 ? D HIS 8   
86  1 Y 1 D PRO -18 ? D PRO 9   
87  1 Y 1 D MET -17 ? D MET 10  
88  1 Y 1 D SER -16 ? D SER 11  
89  1 Y 1 D ASP -15 ? D ASP 12  
90  1 Y 1 D TYR -14 ? D TYR 13  
91  1 Y 1 D ASP -13 ? D ASP 14  
92  1 Y 1 D ILE -12 ? D ILE 15  
93  1 Y 1 D PRO -11 ? D PRO 16  
94  1 Y 1 D THR -10 ? D THR 17  
95  1 Y 1 D THR -9  ? D THR 18  
96  1 Y 1 D GLU -8  ? D GLU 19  
97  1 Y 1 D ASN -7  ? D ASN 20  
98  1 Y 1 D LEU -6  ? D LEU 21  
99  1 Y 1 D TYR -5  ? D TYR 22  
100 1 Y 1 D PHE -4  ? D PHE 23  
101 1 Y 1 D GLN -3  ? D GLN 24  
102 1 Y 1 D GLY -2  ? D GLY 25  
103 1 Y 1 E MET -26 ? E MET 1   
104 1 Y 1 E LYS -25 ? E LYS 2   
105 1 Y 1 E HIS -24 ? E HIS 3   
106 1 Y 1 E HIS -23 ? E HIS 4   
107 1 Y 1 E HIS -22 ? E HIS 5   
108 1 Y 1 E HIS -21 ? E HIS 6   
109 1 Y 1 E HIS -20 ? E HIS 7   
110 1 Y 1 E HIS -19 ? E HIS 8   
111 1 Y 1 E PRO -18 ? E PRO 9   
112 1 Y 1 E MET -17 ? E MET 10  
113 1 Y 1 E SER -16 ? E SER 11  
114 1 Y 1 E ASP -15 ? E ASP 12  
115 1 Y 1 E TYR -14 ? E TYR 13  
116 1 Y 1 E ASP -13 ? E ASP 14  
117 1 Y 1 E ILE -12 ? E ILE 15  
118 1 Y 1 E PRO -11 ? E PRO 16  
119 1 Y 1 E THR -10 ? E THR 17  
120 1 Y 1 E THR -9  ? E THR 18  
121 1 Y 1 E GLU -8  ? E GLU 19  
122 1 Y 1 E ASN -7  ? E ASN 20  
123 1 Y 1 E LEU -6  ? E LEU 21  
124 1 Y 1 E TYR -5  ? E TYR 22  
125 1 Y 1 E PHE -4  ? E PHE 23  
126 1 Y 1 E GLN -3  ? E GLN 24  
127 1 Y 1 E GLY -2  ? E GLY 25  
128 1 Y 1 E ALA -1  ? E ALA 26  
129 1 Y 1 F MET -26 ? F MET 1   
130 1 Y 1 F LYS -25 ? F LYS 2   
131 1 Y 1 F HIS -24 ? F HIS 3   
132 1 Y 1 F HIS -23 ? F HIS 4   
133 1 Y 1 F HIS -22 ? F HIS 5   
134 1 Y 1 F HIS -21 ? F HIS 6   
135 1 Y 1 F HIS -20 ? F HIS 7   
136 1 Y 1 F HIS -19 ? F HIS 8   
137 1 Y 1 F PRO -18 ? F PRO 9   
138 1 Y 1 F MET -17 ? F MET 10  
139 1 Y 1 F SER -16 ? F SER 11  
140 1 Y 1 F ASP -15 ? F ASP 12  
141 1 Y 1 F TYR -14 ? F TYR 13  
142 1 Y 1 F ASP -13 ? F ASP 14  
143 1 Y 1 F ILE -12 ? F ILE 15  
144 1 Y 1 F PRO -11 ? F PRO 16  
145 1 Y 1 F THR -10 ? F THR 17  
146 1 Y 1 F THR -9  ? F THR 18  
147 1 Y 1 F GLU -8  ? F GLU 19  
148 1 Y 1 F ASN -7  ? F ASN 20  
149 1 Y 1 F LEU -6  ? F LEU 21  
150 1 Y 1 F TYR -5  ? F TYR 22  
151 1 Y 1 F PHE -4  ? F PHE 23  
152 1 Y 1 F GLN -3  ? F GLN 24  
153 1 Y 1 F GLY -2  ? F GLY 25  
154 1 Y 1 G MET -26 ? G MET 1   
155 1 Y 1 G LYS -25 ? G LYS 2   
156 1 Y 1 G HIS -24 ? G HIS 3   
157 1 Y 1 G HIS -23 ? G HIS 4   
158 1 Y 1 G HIS -22 ? G HIS 5   
159 1 Y 1 G HIS -21 ? G HIS 6   
160 1 Y 1 G HIS -20 ? G HIS 7   
161 1 Y 1 G HIS -19 ? G HIS 8   
162 1 Y 1 G PRO -18 ? G PRO 9   
163 1 Y 1 G MET -17 ? G MET 10  
164 1 Y 1 G SER -16 ? G SER 11  
165 1 Y 1 G ASP -15 ? G ASP 12  
166 1 Y 1 G TYR -14 ? G TYR 13  
167 1 Y 1 G ASP -13 ? G ASP 14  
168 1 Y 1 G ILE -12 ? G ILE 15  
169 1 Y 1 G PRO -11 ? G PRO 16  
170 1 Y 1 G THR -10 ? G THR 17  
171 1 Y 1 G THR -9  ? G THR 18  
172 1 Y 1 G GLU -8  ? G GLU 19  
173 1 Y 1 G ASN -7  ? G ASN 20  
174 1 Y 1 G LEU -6  ? G LEU 21  
175 1 Y 1 G TYR -5  ? G TYR 22  
176 1 Y 1 G PHE -4  ? G PHE 23  
177 1 Y 1 G GLN -3  ? G GLN 24  
178 1 Y 1 G GLY -2  ? G GLY 25  
179 1 Y 1 G ALA -1  ? G ALA 26  
180 1 Y 1 G MET 0   ? G MET 27  
181 1 Y 1 H MET -26 ? H MET 1   
182 1 Y 1 H LYS -25 ? H LYS 2   
183 1 Y 1 H HIS -24 ? H HIS 3   
184 1 Y 1 H HIS -23 ? H HIS 4   
185 1 Y 1 H HIS -22 ? H HIS 5   
186 1 Y 1 H HIS -21 ? H HIS 6   
187 1 Y 1 H HIS -20 ? H HIS 7   
188 1 Y 1 H HIS -19 ? H HIS 8   
189 1 Y 1 H PRO -18 ? H PRO 9   
190 1 Y 1 H MET -17 ? H MET 10  
191 1 Y 1 H SER -16 ? H SER 11  
192 1 Y 1 H ASP -15 ? H ASP 12  
193 1 Y 1 H TYR -14 ? H TYR 13  
194 1 Y 1 H ASP -13 ? H ASP 14  
195 1 Y 1 H ILE -12 ? H ILE 15  
196 1 Y 1 H PRO -11 ? H PRO 16  
197 1 Y 1 H THR -10 ? H THR 17  
198 1 Y 1 H THR -9  ? H THR 18  
199 1 Y 1 H GLU -8  ? H GLU 19  
200 1 Y 1 H ASN -7  ? H ASN 20  
201 1 Y 1 H LEU -6  ? H LEU 21  
202 1 Y 1 H TYR -5  ? H TYR 22  
203 1 Y 1 H PHE -4  ? H PHE 23  
204 1 Y 1 H GLN -3  ? H GLN 24  
205 1 Y 1 H GLY -2  ? H GLY 25  
206 1 Y 1 H ALA -1  ? H ALA 26  
207 1 Y 1 I MET -26 ? I MET 1   
208 1 Y 1 I LYS -25 ? I LYS 2   
209 1 Y 1 I HIS -24 ? I HIS 3   
210 1 Y 1 I HIS -23 ? I HIS 4   
211 1 Y 1 I HIS -22 ? I HIS 5   
212 1 Y 1 I HIS -21 ? I HIS 6   
213 1 Y 1 I HIS -20 ? I HIS 7   
214 1 Y 1 I HIS -19 ? I HIS 8   
215 1 Y 1 I PRO -18 ? I PRO 9   
216 1 Y 1 I MET -17 ? I MET 10  
217 1 Y 1 I SER -16 ? I SER 11  
218 1 Y 1 I ASP -15 ? I ASP 12  
219 1 Y 1 I TYR -14 ? I TYR 13  
220 1 Y 1 I ASP -13 ? I ASP 14  
221 1 Y 1 I ILE -12 ? I ILE 15  
222 1 Y 1 I PRO -11 ? I PRO 16  
223 1 Y 1 I THR -10 ? I THR 17  
224 1 Y 1 I THR -9  ? I THR 18  
225 1 Y 1 I GLU -8  ? I GLU 19  
226 1 Y 1 I ASN -7  ? I ASN 20  
227 1 Y 1 I LEU -6  ? I LEU 21  
228 1 Y 1 I TYR -5  ? I TYR 22  
229 1 Y 1 I PHE -4  ? I PHE 23  
230 1 Y 1 I GLN -3  ? I GLN 24  
231 1 Y 1 I GLY -2  ? I GLY 25  
232 1 Y 1 I ALA -1  ? I ALA 26  
233 1 Y 1 I MET 0   ? I MET 27  
234 1 Y 1 J MET -26 ? J MET 1   
235 1 Y 1 J LYS -25 ? J LYS 2   
236 1 Y 1 J HIS -24 ? J HIS 3   
237 1 Y 1 J HIS -23 ? J HIS 4   
238 1 Y 1 J HIS -22 ? J HIS 5   
239 1 Y 1 J HIS -21 ? J HIS 6   
240 1 Y 1 J HIS -20 ? J HIS 7   
241 1 Y 1 J HIS -19 ? J HIS 8   
242 1 Y 1 J PRO -18 ? J PRO 9   
243 1 Y 1 J MET -17 ? J MET 10  
244 1 Y 1 J SER -16 ? J SER 11  
245 1 Y 1 J ASP -15 ? J ASP 12  
246 1 Y 1 J TYR -14 ? J TYR 13  
247 1 Y 1 J ASP -13 ? J ASP 14  
248 1 Y 1 J ILE -12 ? J ILE 15  
249 1 Y 1 J PRO -11 ? J PRO 16  
250 1 Y 1 J THR -10 ? J THR 17  
251 1 Y 1 J THR -9  ? J THR 18  
252 1 Y 1 J GLU -8  ? J GLU 19  
253 1 Y 1 J ASN -7  ? J ASN 20  
254 1 Y 1 J LEU -6  ? J LEU 21  
255 1 Y 1 J TYR -5  ? J TYR 22  
256 1 Y 1 J PHE -4  ? J PHE 23  
257 1 Y 1 J GLN -3  ? J GLN 24  
258 1 Y 1 J GLY -2  ? J GLY 25  
259 1 Y 1 J ALA -1  ? J ALA 26  
260 1 Y 1 J MET 0   ? J MET 27  
261 1 Y 1 J LEU 67  ? J LEU 94  
262 1 Y 1 J SER 68  ? J SER 95  
263 1 Y 1 J ARG 69  ? J ARG 96  
264 1 Y 1 J LYS 70  ? J LYS 97  
265 1 Y 1 J HIS 71  ? J HIS 98  
266 1 Y 1 J GLY 72  ? J GLY 99  
267 1 Y 1 J GLY 73  ? J GLY 100 
268 1 Y 1 J PRO 74  ? J PRO 101 
269 1 Y 1 J LYS 75  ? J LYS 102 
270 1 Y 1 J ASP 76  ? J ASP 103 
271 1 Y 1 J GLU 77  ? J GLU 104 
272 1 Y 1 J GLU 78  ? J GLU 105 
273 1 Y 1 J LEU 126 ? J LEU 153 
274 1 Y 1 J GLY 127 ? J GLY 154 
275 1 Y 1 J LYS 128 ? J LYS 155 
276 1 Y 1 J GLY 129 ? J GLY 156 
277 1 Y 1 J GLY 130 ? J GLY 157 
278 1 Y 1 J ASN 131 ? J ASN 158 
279 1 Y 1 J GLU 132 ? J GLU 159 
280 1 Y 1 J GLU 133 ? J GLU 160 
281 1 Y 1 J SER 134 ? J SER 161 
282 1 Y 1 J THR 135 ? J THR 162 
283 1 Y 1 J LYS 136 ? J LYS 163 
284 1 Y 1 J THR 137 ? J THR 164 
285 1 Y 1 J GLY 138 ? J GLY 165 
286 1 Y 1 J ASN 139 ? J ASN 166 
287 1 Y 1 J ALA 140 ? J ALA 167 
288 1 Y 1 J GLY 141 ? J GLY 168 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        946 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   946 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                    ZN  
3 GLYCEROL                                                                      GOL 
4 '4-[(1~{R})-2-(naphthalen-2-ylmethylamino)-1-oxidanyl-ethyl]benzene-1,2-diol' 946 
5 PENTASULFIDE-SULFUR                                                           PS5 
6 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                ? 
# 
