data_7XX3
# 
_entry.id   7XX3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.380 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7XX3         pdb_00007xx3 10.2210/pdb7xx3/pdb 
WWPDB D_1300029832 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7XX3 
_pdbx_database_status.recvd_initial_deposition_date   2022-05-28 
_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.status_code_nmr_data            ? 
_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 ?                   
'Unni, S.'        2 0000-0001-9905-9464 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Phialomustin-B a fungal metabolite isolated from Phialophora mustea modulates Superoxide Dismutase 1 (SOD1) aggregation: Therapeutic potential in Amyotrophic lateral sclerosis (ALS)
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Unni, S.'        1 0000-0001-9905-9464 
primary 'Padmanabhan, B.' 2 ?                   
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7XX3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     242.445 
_cell.length_a_esd                 ? 
_cell.length_b                     242.445 
_cell.length_b_esd                 ? 
_cell.length_c                     144.491 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         7XX3 
_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    5    ?        ? ? ? 
4 non-polymer syn '(2~{E},4~{E},6~{S})-4,6-dimethyldeca-2,4-dienoic acid' 196.286   4    ?        ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                    78.133    1    ?        ? ? ? 
6 water       nat water                                                   18.015    1208 ?        ? ? ? 
# 
_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,D,C,H,E,F,G,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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 7XX3 A 27 ? 180 ? P00441 1 ? 154 ? 0 153 
2  1 7XX3 B 27 ? 180 ? P00441 1 ? 154 ? 0 153 
3  1 7XX3 D 27 ? 180 ? P00441 1 ? 154 ? 0 153 
4  1 7XX3 C 27 ? 180 ? P00441 1 ? 154 ? 0 153 
5  1 7XX3 H 27 ? 180 ? P00441 1 ? 154 ? 0 153 
6  1 7XX3 E 27 ? 180 ? P00441 1 ? 154 ? 0 153 
7  1 7XX3 F 27 ? 180 ? P00441 1 ? 154 ? 0 153 
8  1 7XX3 G 27 ? 180 ? P00441 1 ? 154 ? 0 153 
9  1 7XX3 I 27 ? 180 ? P00441 1 ? 154 ? 0 153 
10 1 7XX3 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  7XX3 MET A 1  ? UNP P00441 ? ? 'initiating methionine' -26 1   
1  7XX3 LYS A 2  ? UNP P00441 ? ? 'expression tag'        -25 2   
1  7XX3 HIS A 3  ? UNP P00441 ? ? 'expression tag'        -24 3   
1  7XX3 HIS A 4  ? UNP P00441 ? ? 'expression tag'        -23 4   
1  7XX3 HIS A 5  ? UNP P00441 ? ? 'expression tag'        -22 5   
1  7XX3 HIS A 6  ? UNP P00441 ? ? 'expression tag'        -21 6   
1  7XX3 HIS A 7  ? UNP P00441 ? ? 'expression tag'        -20 7   
1  7XX3 HIS A 8  ? UNP P00441 ? ? 'expression tag'        -19 8   
1  7XX3 PRO A 9  ? UNP P00441 ? ? 'expression tag'        -18 9   
1  7XX3 MET A 10 ? UNP P00441 ? ? 'expression tag'        -17 10  
1  7XX3 SER A 11 ? UNP P00441 ? ? 'expression tag'        -16 11  
1  7XX3 ASP A 12 ? UNP P00441 ? ? 'expression tag'        -15 12  
1  7XX3 TYR A 13 ? UNP P00441 ? ? 'expression tag'        -14 13  
1  7XX3 ASP A 14 ? UNP P00441 ? ? 'expression tag'        -13 14  
1  7XX3 ILE A 15 ? UNP P00441 ? ? 'expression tag'        -12 15  
1  7XX3 PRO A 16 ? UNP P00441 ? ? 'expression tag'        -11 16  
1  7XX3 THR A 17 ? UNP P00441 ? ? 'expression tag'        -10 17  
1  7XX3 THR A 18 ? UNP P00441 ? ? 'expression tag'        -9  18  
1  7XX3 GLU A 19 ? UNP P00441 ? ? 'expression tag'        -8  19  
1  7XX3 ASN A 20 ? UNP P00441 ? ? 'expression tag'        -7  20  
1  7XX3 LEU A 21 ? UNP P00441 ? ? 'expression tag'        -6  21  
1  7XX3 TYR A 22 ? UNP P00441 ? ? 'expression tag'        -5  22  
1  7XX3 PHE A 23 ? UNP P00441 ? ? 'expression tag'        -4  23  
1  7XX3 GLN A 24 ? UNP P00441 ? ? 'expression tag'        -3  24  
1  7XX3 GLY A 25 ? UNP P00441 ? ? 'expression tag'        -2  25  
1  7XX3 ALA A 26 ? UNP P00441 ? ? 'expression tag'        -1  26  
2  7XX3 MET B 1  ? UNP P00441 ? ? 'initiating methionine' -26 27  
2  7XX3 LYS B 2  ? UNP P00441 ? ? 'expression tag'        -25 28  
2  7XX3 HIS B 3  ? UNP P00441 ? ? 'expression tag'        -24 29  
2  7XX3 HIS B 4  ? UNP P00441 ? ? 'expression tag'        -23 30  
2  7XX3 HIS B 5  ? UNP P00441 ? ? 'expression tag'        -22 31  
2  7XX3 HIS B 6  ? UNP P00441 ? ? 'expression tag'        -21 32  
2  7XX3 HIS B 7  ? UNP P00441 ? ? 'expression tag'        -20 33  
2  7XX3 HIS B 8  ? UNP P00441 ? ? 'expression tag'        -19 34  
2  7XX3 PRO B 9  ? UNP P00441 ? ? 'expression tag'        -18 35  
2  7XX3 MET B 10 ? UNP P00441 ? ? 'expression tag'        -17 36  
2  7XX3 SER B 11 ? UNP P00441 ? ? 'expression tag'        -16 37  
2  7XX3 ASP B 12 ? UNP P00441 ? ? 'expression tag'        -15 38  
2  7XX3 TYR B 13 ? UNP P00441 ? ? 'expression tag'        -14 39  
2  7XX3 ASP B 14 ? UNP P00441 ? ? 'expression tag'        -13 40  
2  7XX3 ILE B 15 ? UNP P00441 ? ? 'expression tag'        -12 41  
2  7XX3 PRO B 16 ? UNP P00441 ? ? 'expression tag'        -11 42  
2  7XX3 THR B 17 ? UNP P00441 ? ? 'expression tag'        -10 43  
2  7XX3 THR B 18 ? UNP P00441 ? ? 'expression tag'        -9  44  
2  7XX3 GLU B 19 ? UNP P00441 ? ? 'expression tag'        -8  45  
2  7XX3 ASN B 20 ? UNP P00441 ? ? 'expression tag'        -7  46  
2  7XX3 LEU B 21 ? UNP P00441 ? ? 'expression tag'        -6  47  
2  7XX3 TYR B 22 ? UNP P00441 ? ? 'expression tag'        -5  48  
2  7XX3 PHE B 23 ? UNP P00441 ? ? 'expression tag'        -4  49  
2  7XX3 GLN B 24 ? UNP P00441 ? ? 'expression tag'        -3  50  
2  7XX3 GLY B 25 ? UNP P00441 ? ? 'expression tag'        -2  51  
2  7XX3 ALA B 26 ? UNP P00441 ? ? 'expression tag'        -1  52  
3  7XX3 MET D 1  ? UNP P00441 ? ? 'initiating methionine' -26 53  
3  7XX3 LYS D 2  ? UNP P00441 ? ? 'expression tag'        -25 54  
3  7XX3 HIS D 3  ? UNP P00441 ? ? 'expression tag'        -24 55  
3  7XX3 HIS D 4  ? UNP P00441 ? ? 'expression tag'        -23 56  
3  7XX3 HIS D 5  ? UNP P00441 ? ? 'expression tag'        -22 57  
3  7XX3 HIS D 6  ? UNP P00441 ? ? 'expression tag'        -21 58  
3  7XX3 HIS D 7  ? UNP P00441 ? ? 'expression tag'        -20 59  
3  7XX3 HIS D 8  ? UNP P00441 ? ? 'expression tag'        -19 60  
3  7XX3 PRO D 9  ? UNP P00441 ? ? 'expression tag'        -18 61  
3  7XX3 MET D 10 ? UNP P00441 ? ? 'expression tag'        -17 62  
3  7XX3 SER D 11 ? UNP P00441 ? ? 'expression tag'        -16 63  
3  7XX3 ASP D 12 ? UNP P00441 ? ? 'expression tag'        -15 64  
3  7XX3 TYR D 13 ? UNP P00441 ? ? 'expression tag'        -14 65  
3  7XX3 ASP D 14 ? UNP P00441 ? ? 'expression tag'        -13 66  
3  7XX3 ILE D 15 ? UNP P00441 ? ? 'expression tag'        -12 67  
3  7XX3 PRO D 16 ? UNP P00441 ? ? 'expression tag'        -11 68  
3  7XX3 THR D 17 ? UNP P00441 ? ? 'expression tag'        -10 69  
3  7XX3 THR D 18 ? UNP P00441 ? ? 'expression tag'        -9  70  
3  7XX3 GLU D 19 ? UNP P00441 ? ? 'expression tag'        -8  71  
3  7XX3 ASN D 20 ? UNP P00441 ? ? 'expression tag'        -7  72  
3  7XX3 LEU D 21 ? UNP P00441 ? ? 'expression tag'        -6  73  
3  7XX3 TYR D 22 ? UNP P00441 ? ? 'expression tag'        -5  74  
3  7XX3 PHE D 23 ? UNP P00441 ? ? 'expression tag'        -4  75  
3  7XX3 GLN D 24 ? UNP P00441 ? ? 'expression tag'        -3  76  
3  7XX3 GLY D 25 ? UNP P00441 ? ? 'expression tag'        -2  77  
3  7XX3 ALA D 26 ? UNP P00441 ? ? 'expression tag'        -1  78  
4  7XX3 MET C 1  ? UNP P00441 ? ? 'initiating methionine' -26 79  
4  7XX3 LYS C 2  ? UNP P00441 ? ? 'expression tag'        -25 80  
4  7XX3 HIS C 3  ? UNP P00441 ? ? 'expression tag'        -24 81  
4  7XX3 HIS C 4  ? UNP P00441 ? ? 'expression tag'        -23 82  
4  7XX3 HIS C 5  ? UNP P00441 ? ? 'expression tag'        -22 83  
4  7XX3 HIS C 6  ? UNP P00441 ? ? 'expression tag'        -21 84  
4  7XX3 HIS C 7  ? UNP P00441 ? ? 'expression tag'        -20 85  
4  7XX3 HIS C 8  ? UNP P00441 ? ? 'expression tag'        -19 86  
4  7XX3 PRO C 9  ? UNP P00441 ? ? 'expression tag'        -18 87  
4  7XX3 MET C 10 ? UNP P00441 ? ? 'expression tag'        -17 88  
4  7XX3 SER C 11 ? UNP P00441 ? ? 'expression tag'        -16 89  
4  7XX3 ASP C 12 ? UNP P00441 ? ? 'expression tag'        -15 90  
4  7XX3 TYR C 13 ? UNP P00441 ? ? 'expression tag'        -14 91  
4  7XX3 ASP C 14 ? UNP P00441 ? ? 'expression tag'        -13 92  
4  7XX3 ILE C 15 ? UNP P00441 ? ? 'expression tag'        -12 93  
4  7XX3 PRO C 16 ? UNP P00441 ? ? 'expression tag'        -11 94  
4  7XX3 THR C 17 ? UNP P00441 ? ? 'expression tag'        -10 95  
4  7XX3 THR C 18 ? UNP P00441 ? ? 'expression tag'        -9  96  
4  7XX3 GLU C 19 ? UNP P00441 ? ? 'expression tag'        -8  97  
4  7XX3 ASN C 20 ? UNP P00441 ? ? 'expression tag'        -7  98  
4  7XX3 LEU C 21 ? UNP P00441 ? ? 'expression tag'        -6  99  
4  7XX3 TYR C 22 ? UNP P00441 ? ? 'expression tag'        -5  100 
4  7XX3 PHE C 23 ? UNP P00441 ? ? 'expression tag'        -4  101 
4  7XX3 GLN C 24 ? UNP P00441 ? ? 'expression tag'        -3  102 
4  7XX3 GLY C 25 ? UNP P00441 ? ? 'expression tag'        -2  103 
4  7XX3 ALA C 26 ? UNP P00441 ? ? 'expression tag'        -1  104 
5  7XX3 MET H 1  ? UNP P00441 ? ? 'initiating methionine' -26 105 
5  7XX3 LYS H 2  ? UNP P00441 ? ? 'expression tag'        -25 106 
5  7XX3 HIS H 3  ? UNP P00441 ? ? 'expression tag'        -24 107 
5  7XX3 HIS H 4  ? UNP P00441 ? ? 'expression tag'        -23 108 
5  7XX3 HIS H 5  ? UNP P00441 ? ? 'expression tag'        -22 109 
5  7XX3 HIS H 6  ? UNP P00441 ? ? 'expression tag'        -21 110 
5  7XX3 HIS H 7  ? UNP P00441 ? ? 'expression tag'        -20 111 
5  7XX3 HIS H 8  ? UNP P00441 ? ? 'expression tag'        -19 112 
5  7XX3 PRO H 9  ? UNP P00441 ? ? 'expression tag'        -18 113 
5  7XX3 MET H 10 ? UNP P00441 ? ? 'expression tag'        -17 114 
5  7XX3 SER H 11 ? UNP P00441 ? ? 'expression tag'        -16 115 
5  7XX3 ASP H 12 ? UNP P00441 ? ? 'expression tag'        -15 116 
5  7XX3 TYR H 13 ? UNP P00441 ? ? 'expression tag'        -14 117 
5  7XX3 ASP H 14 ? UNP P00441 ? ? 'expression tag'        -13 118 
5  7XX3 ILE H 15 ? UNP P00441 ? ? 'expression tag'        -12 119 
5  7XX3 PRO H 16 ? UNP P00441 ? ? 'expression tag'        -11 120 
5  7XX3 THR H 17 ? UNP P00441 ? ? 'expression tag'        -10 121 
5  7XX3 THR H 18 ? UNP P00441 ? ? 'expression tag'        -9  122 
5  7XX3 GLU H 19 ? UNP P00441 ? ? 'expression tag'        -8  123 
5  7XX3 ASN H 20 ? UNP P00441 ? ? 'expression tag'        -7  124 
5  7XX3 LEU H 21 ? UNP P00441 ? ? 'expression tag'        -6  125 
5  7XX3 TYR H 22 ? UNP P00441 ? ? 'expression tag'        -5  126 
5  7XX3 PHE H 23 ? UNP P00441 ? ? 'expression tag'        -4  127 
5  7XX3 GLN H 24 ? UNP P00441 ? ? 'expression tag'        -3  128 
5  7XX3 GLY H 25 ? UNP P00441 ? ? 'expression tag'        -2  129 
5  7XX3 ALA H 26 ? UNP P00441 ? ? 'expression tag'        -1  130 
6  7XX3 MET E 1  ? UNP P00441 ? ? 'initiating methionine' -26 131 
6  7XX3 LYS E 2  ? UNP P00441 ? ? 'expression tag'        -25 132 
6  7XX3 HIS E 3  ? UNP P00441 ? ? 'expression tag'        -24 133 
6  7XX3 HIS E 4  ? UNP P00441 ? ? 'expression tag'        -23 134 
6  7XX3 HIS E 5  ? UNP P00441 ? ? 'expression tag'        -22 135 
6  7XX3 HIS E 6  ? UNP P00441 ? ? 'expression tag'        -21 136 
6  7XX3 HIS E 7  ? UNP P00441 ? ? 'expression tag'        -20 137 
6  7XX3 HIS E 8  ? UNP P00441 ? ? 'expression tag'        -19 138 
6  7XX3 PRO E 9  ? UNP P00441 ? ? 'expression tag'        -18 139 
6  7XX3 MET E 10 ? UNP P00441 ? ? 'expression tag'        -17 140 
6  7XX3 SER E 11 ? UNP P00441 ? ? 'expression tag'        -16 141 
6  7XX3 ASP E 12 ? UNP P00441 ? ? 'expression tag'        -15 142 
6  7XX3 TYR E 13 ? UNP P00441 ? ? 'expression tag'        -14 143 
6  7XX3 ASP E 14 ? UNP P00441 ? ? 'expression tag'        -13 144 
6  7XX3 ILE E 15 ? UNP P00441 ? ? 'expression tag'        -12 145 
6  7XX3 PRO E 16 ? UNP P00441 ? ? 'expression tag'        -11 146 
6  7XX3 THR E 17 ? UNP P00441 ? ? 'expression tag'        -10 147 
6  7XX3 THR E 18 ? UNP P00441 ? ? 'expression tag'        -9  148 
6  7XX3 GLU E 19 ? UNP P00441 ? ? 'expression tag'        -8  149 
6  7XX3 ASN E 20 ? UNP P00441 ? ? 'expression tag'        -7  150 
6  7XX3 LEU E 21 ? UNP P00441 ? ? 'expression tag'        -6  151 
6  7XX3 TYR E 22 ? UNP P00441 ? ? 'expression tag'        -5  152 
6  7XX3 PHE E 23 ? UNP P00441 ? ? 'expression tag'        -4  153 
6  7XX3 GLN E 24 ? UNP P00441 ? ? 'expression tag'        -3  154 
6  7XX3 GLY E 25 ? UNP P00441 ? ? 'expression tag'        -2  155 
6  7XX3 ALA E 26 ? UNP P00441 ? ? 'expression tag'        -1  156 
7  7XX3 MET F 1  ? UNP P00441 ? ? 'initiating methionine' -26 157 
7  7XX3 LYS F 2  ? UNP P00441 ? ? 'expression tag'        -25 158 
7  7XX3 HIS F 3  ? UNP P00441 ? ? 'expression tag'        -24 159 
7  7XX3 HIS F 4  ? UNP P00441 ? ? 'expression tag'        -23 160 
7  7XX3 HIS F 5  ? UNP P00441 ? ? 'expression tag'        -22 161 
7  7XX3 HIS F 6  ? UNP P00441 ? ? 'expression tag'        -21 162 
7  7XX3 HIS F 7  ? UNP P00441 ? ? 'expression tag'        -20 163 
7  7XX3 HIS F 8  ? UNP P00441 ? ? 'expression tag'        -19 164 
7  7XX3 PRO F 9  ? UNP P00441 ? ? 'expression tag'        -18 165 
7  7XX3 MET F 10 ? UNP P00441 ? ? 'expression tag'        -17 166 
7  7XX3 SER F 11 ? UNP P00441 ? ? 'expression tag'        -16 167 
7  7XX3 ASP F 12 ? UNP P00441 ? ? 'expression tag'        -15 168 
7  7XX3 TYR F 13 ? UNP P00441 ? ? 'expression tag'        -14 169 
7  7XX3 ASP F 14 ? UNP P00441 ? ? 'expression tag'        -13 170 
7  7XX3 ILE F 15 ? UNP P00441 ? ? 'expression tag'        -12 171 
7  7XX3 PRO F 16 ? UNP P00441 ? ? 'expression tag'        -11 172 
7  7XX3 THR F 17 ? UNP P00441 ? ? 'expression tag'        -10 173 
7  7XX3 THR F 18 ? UNP P00441 ? ? 'expression tag'        -9  174 
7  7XX3 GLU F 19 ? UNP P00441 ? ? 'expression tag'        -8  175 
7  7XX3 ASN F 20 ? UNP P00441 ? ? 'expression tag'        -7  176 
7  7XX3 LEU F 21 ? UNP P00441 ? ? 'expression tag'        -6  177 
7  7XX3 TYR F 22 ? UNP P00441 ? ? 'expression tag'        -5  178 
7  7XX3 PHE F 23 ? UNP P00441 ? ? 'expression tag'        -4  179 
7  7XX3 GLN F 24 ? UNP P00441 ? ? 'expression tag'        -3  180 
7  7XX3 GLY F 25 ? UNP P00441 ? ? 'expression tag'        -2  181 
7  7XX3 ALA F 26 ? UNP P00441 ? ? 'expression tag'        -1  182 
8  7XX3 MET G 1  ? UNP P00441 ? ? 'initiating methionine' -26 183 
8  7XX3 LYS G 2  ? UNP P00441 ? ? 'expression tag'        -25 184 
8  7XX3 HIS G 3  ? UNP P00441 ? ? 'expression tag'        -24 185 
8  7XX3 HIS G 4  ? UNP P00441 ? ? 'expression tag'        -23 186 
8  7XX3 HIS G 5  ? UNP P00441 ? ? 'expression tag'        -22 187 
8  7XX3 HIS G 6  ? UNP P00441 ? ? 'expression tag'        -21 188 
8  7XX3 HIS G 7  ? UNP P00441 ? ? 'expression tag'        -20 189 
8  7XX3 HIS G 8  ? UNP P00441 ? ? 'expression tag'        -19 190 
8  7XX3 PRO G 9  ? UNP P00441 ? ? 'expression tag'        -18 191 
8  7XX3 MET G 10 ? UNP P00441 ? ? 'expression tag'        -17 192 
8  7XX3 SER G 11 ? UNP P00441 ? ? 'expression tag'        -16 193 
8  7XX3 ASP G 12 ? UNP P00441 ? ? 'expression tag'        -15 194 
8  7XX3 TYR G 13 ? UNP P00441 ? ? 'expression tag'        -14 195 
8  7XX3 ASP G 14 ? UNP P00441 ? ? 'expression tag'        -13 196 
8  7XX3 ILE G 15 ? UNP P00441 ? ? 'expression tag'        -12 197 
8  7XX3 PRO G 16 ? UNP P00441 ? ? 'expression tag'        -11 198 
8  7XX3 THR G 17 ? UNP P00441 ? ? 'expression tag'        -10 199 
8  7XX3 THR G 18 ? UNP P00441 ? ? 'expression tag'        -9  200 
8  7XX3 GLU G 19 ? UNP P00441 ? ? 'expression tag'        -8  201 
8  7XX3 ASN G 20 ? UNP P00441 ? ? 'expression tag'        -7  202 
8  7XX3 LEU G 21 ? UNP P00441 ? ? 'expression tag'        -6  203 
8  7XX3 TYR G 22 ? UNP P00441 ? ? 'expression tag'        -5  204 
8  7XX3 PHE G 23 ? UNP P00441 ? ? 'expression tag'        -4  205 
8  7XX3 GLN G 24 ? UNP P00441 ? ? 'expression tag'        -3  206 
8  7XX3 GLY G 25 ? UNP P00441 ? ? 'expression tag'        -2  207 
8  7XX3 ALA G 26 ? UNP P00441 ? ? 'expression tag'        -1  208 
9  7XX3 MET I 1  ? UNP P00441 ? ? 'initiating methionine' -26 209 
9  7XX3 LYS I 2  ? UNP P00441 ? ? 'expression tag'        -25 210 
9  7XX3 HIS I 3  ? UNP P00441 ? ? 'expression tag'        -24 211 
9  7XX3 HIS I 4  ? UNP P00441 ? ? 'expression tag'        -23 212 
9  7XX3 HIS I 5  ? UNP P00441 ? ? 'expression tag'        -22 213 
9  7XX3 HIS I 6  ? UNP P00441 ? ? 'expression tag'        -21 214 
9  7XX3 HIS I 7  ? UNP P00441 ? ? 'expression tag'        -20 215 
9  7XX3 HIS I 8  ? UNP P00441 ? ? 'expression tag'        -19 216 
9  7XX3 PRO I 9  ? UNP P00441 ? ? 'expression tag'        -18 217 
9  7XX3 MET I 10 ? UNP P00441 ? ? 'expression tag'        -17 218 
9  7XX3 SER I 11 ? UNP P00441 ? ? 'expression tag'        -16 219 
9  7XX3 ASP I 12 ? UNP P00441 ? ? 'expression tag'        -15 220 
9  7XX3 TYR I 13 ? UNP P00441 ? ? 'expression tag'        -14 221 
9  7XX3 ASP I 14 ? UNP P00441 ? ? 'expression tag'        -13 222 
9  7XX3 ILE I 15 ? UNP P00441 ? ? 'expression tag'        -12 223 
9  7XX3 PRO I 16 ? UNP P00441 ? ? 'expression tag'        -11 224 
9  7XX3 THR I 17 ? UNP P00441 ? ? 'expression tag'        -10 225 
9  7XX3 THR I 18 ? UNP P00441 ? ? 'expression tag'        -9  226 
9  7XX3 GLU I 19 ? UNP P00441 ? ? 'expression tag'        -8  227 
9  7XX3 ASN I 20 ? UNP P00441 ? ? 'expression tag'        -7  228 
9  7XX3 LEU I 21 ? UNP P00441 ? ? 'expression tag'        -6  229 
9  7XX3 TYR I 22 ? UNP P00441 ? ? 'expression tag'        -5  230 
9  7XX3 PHE I 23 ? UNP P00441 ? ? 'expression tag'        -4  231 
9  7XX3 GLN I 24 ? UNP P00441 ? ? 'expression tag'        -3  232 
9  7XX3 GLY I 25 ? UNP P00441 ? ? 'expression tag'        -2  233 
9  7XX3 ALA I 26 ? UNP P00441 ? ? 'expression tag'        -1  234 
10 7XX3 MET J 1  ? UNP P00441 ? ? 'initiating methionine' -26 235 
10 7XX3 LYS J 2  ? UNP P00441 ? ? 'expression tag'        -25 236 
10 7XX3 HIS J 3  ? UNP P00441 ? ? 'expression tag'        -24 237 
10 7XX3 HIS J 4  ? UNP P00441 ? ? 'expression tag'        -23 238 
10 7XX3 HIS J 5  ? UNP P00441 ? ? 'expression tag'        -22 239 
10 7XX3 HIS J 6  ? UNP P00441 ? ? 'expression tag'        -21 240 
10 7XX3 HIS J 7  ? UNP P00441 ? ? 'expression tag'        -20 241 
10 7XX3 HIS J 8  ? UNP P00441 ? ? 'expression tag'        -19 242 
10 7XX3 PRO J 9  ? UNP P00441 ? ? 'expression tag'        -18 243 
10 7XX3 MET J 10 ? UNP P00441 ? ? 'expression tag'        -17 244 
10 7XX3 SER J 11 ? UNP P00441 ? ? 'expression tag'        -16 245 
10 7XX3 ASP J 12 ? UNP P00441 ? ? 'expression tag'        -15 246 
10 7XX3 TYR J 13 ? UNP P00441 ? ? 'expression tag'        -14 247 
10 7XX3 ASP J 14 ? UNP P00441 ? ? 'expression tag'        -13 248 
10 7XX3 ILE J 15 ? UNP P00441 ? ? 'expression tag'        -12 249 
10 7XX3 PRO J 16 ? UNP P00441 ? ? 'expression tag'        -11 250 
10 7XX3 THR J 17 ? UNP P00441 ? ? 'expression tag'        -10 251 
10 7XX3 THR J 18 ? UNP P00441 ? ? 'expression tag'        -9  252 
10 7XX3 GLU J 19 ? UNP P00441 ? ? 'expression tag'        -8  253 
10 7XX3 ASN J 20 ? UNP P00441 ? ? 'expression tag'        -7  254 
10 7XX3 LEU J 21 ? UNP P00441 ? ? 'expression tag'        -6  255 
10 7XX3 TYR J 22 ? UNP P00441 ? ? 'expression tag'        -5  256 
10 7XX3 PHE J 23 ? UNP P00441 ? ? 'expression tag'        -4  257 
10 7XX3 GLN J 24 ? UNP P00441 ? ? 'expression tag'        -3  258 
10 7XX3 GLY J 25 ? UNP P00441 ? ? 'expression tag'        -2  259 
10 7XX3 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 
ALA 'L-peptide linking' y ALANINE                                                 ?                               'C3 H7 N O2'     
89.093  
ARG 'L-peptide linking' y ARGININE                                                ?                               'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                              ?                               'C4 H8 N2 O3'    
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                         ?                               'C4 H7 N O4'     
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                ?                               'C3 H7 N O2 S'   
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                    ?                               'C2 H6 O S'      
78.133  
GLN 'L-peptide linking' y GLUTAMINE                                               ?                               'C5 H10 N2 O3'   
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                         ?                               'C5 H9 N O4'     
147.129 
GLY 'peptide linking'   y GLYCINE                                                 ?                               'C2 H5 N O2'     
75.067  
GOL non-polymer         . GLYCEROL                                                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       
92.094  
HIS 'L-peptide linking' y HISTIDINE                                               ?                               'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                   ?                               'H2 O'           
18.015  
I2G non-polymer         . '(2~{E},4~{E},6~{S})-4,6-dimethyldeca-2,4-dienoic acid' ?                               'C12 H20 O2'     
196.286 
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 
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                   7XX3 
_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             3.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.69 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.3 M Sodium citrate (pH = 6.5)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     81 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-06-16 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.987 
_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 ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          27.660 
_reflns.entry_id                                       7XX3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.900 
_reflns.d_resolution_low                               50.000 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     195483 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.000 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.600 
_reflns.pdbx_Rmerge_I_obs                              0.112 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.000 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.048 
_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                                0.117 
_reflns.pdbx_Rpim_I_all                                0.036 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1880644 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
_reflns.pdbx_CC_split_method                           ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_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 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.900 1.930  ? ? ? ? ? ? 9652  100.000 ? ? ? ? 1.640 ? ? ? ? ? ? ? ? 8.200  ? 0.575 ? ? 1.747 0.592 ? 1  1 0.719 ? ? ? ? ? ? ? ? ? 
? 
1.930 1.970  ? ? ? ? ? ? 9672  100.000 ? ? ? ? 1.367 ? ? ? ? ? ? ? ? 8.200  ? 0.586 ? ? 1.455 0.493 ? 2  1 0.820 ? ? ? ? ? ? ? ? ? 
? 
1.970 2.010  ? ? ? ? ? ? 9676  100.000 ? ? ? ? 1.053 ? ? ? ? ? ? ? ? 8.200  ? 0.585 ? ? 1.121 0.380 ? 3  1 0.858 ? ? ? ? ? ? ? ? ? 
? 
2.010 2.050  ? ? ? ? ? ? 9658  100.000 ? ? ? ? 0.873 ? ? ? ? ? ? ? ? 8.200  ? 0.612 ? ? 0.930 0.315 ? 4  1 0.894 ? ? ? ? ? ? ? ? ? 
? 
2.050 2.090  ? ? ? ? ? ? 9676  100.000 ? ? ? ? 0.692 ? ? ? ? ? ? ? ? 8.200  ? 0.628 ? ? 0.736 0.250 ? 5  1 0.923 ? ? ? ? ? ? ? ? ? 
? 
2.090 2.140  ? ? ? ? ? ? 9678  100.000 ? ? ? ? 0.584 ? ? ? ? ? ? ? ? 8.200  ? 0.638 ? ? 0.622 0.211 ? 6  1 0.941 ? ? ? ? ? ? ? ? ? 
? 
2.140 2.190  ? ? ? ? ? ? 9723  100.000 ? ? ? ? 0.504 ? ? ? ? ? ? ? ? 8.200  ? 0.639 ? ? 0.537 0.182 ? 7  1 0.953 ? ? ? ? ? ? ? ? ? 
? 
2.190 2.250  ? ? ? ? ? ? 9658  100.000 ? ? ? ? 0.435 ? ? ? ? ? ? ? ? 8.200  ? 0.655 ? ? 0.463 0.157 ? 8  1 0.961 ? ? ? ? ? ? ? ? ? 
? 
2.250 2.320  ? ? ? ? ? ? 9732  100.000 ? ? ? ? 0.363 ? ? ? ? ? ? ? ? 8.200  ? 0.662 ? ? 0.387 0.131 ? 9  1 0.974 ? ? ? ? ? ? ? ? ? 
? 
2.320 2.390  ? ? ? ? ? ? 9690  100.000 ? ? ? ? 0.293 ? ? ? ? ? ? ? ? 8.300  ? 0.688 ? ? 0.312 0.106 ? 10 1 0.982 ? ? ? ? ? ? ? ? ? 
? 
2.390 2.480  ? ? ? ? ? ? 9726  99.900  ? ? ? ? 0.274 ? ? ? ? ? ? ? ? 8.400  ? 0.693 ? ? 0.292 0.099 ? 11 1 0.982 ? ? ? ? ? ? ? ? ? 
? 
2.480 2.580  ? ? ? ? ? ? 9719  100.000 ? ? ? ? 0.230 ? ? ? ? ? ? ? ? 8.600  ? 0.711 ? ? 0.244 0.082 ? 12 1 0.988 ? ? ? ? ? ? ? ? ? 
? 
2.580 2.700  ? ? ? ? ? ? 9757  100.000 ? ? ? ? 0.190 ? ? ? ? ? ? ? ? 8.900  ? 0.738 ? ? 0.202 0.067 ? 13 1 0.990 ? ? ? ? ? ? ? ? ? 
? 
2.700 2.840  ? ? ? ? ? ? 9779  100.000 ? ? ? ? 0.154 ? ? ? ? ? ? ? ? 9.400  ? 0.834 ? ? 0.163 0.052 ? 14 1 0.994 ? ? ? ? ? ? ? ? ? 
? 
2.840 3.020  ? ? ? ? ? ? 9774  100.000 ? ? ? ? 0.128 ? ? ? ? ? ? ? ? 10.200 ? 1.034 ? ? 0.135 0.041 ? 15 1 0.996 ? ? ? ? ? ? ? ? ? 
? 
3.020 3.250  ? ? ? ? ? ? 9819  100.000 ? ? ? ? 0.114 ? ? ? ? ? ? ? ? 11.400 ? 1.528 ? ? 0.119 0.035 ? 16 1 0.996 ? ? ? ? ? ? ? ? ? 
? 
3.250 3.580  ? ? ? ? ? ? 9845  100.000 ? ? ? ? 0.108 ? ? ? ? ? ? ? ? 12.700 ? 2.211 ? ? 0.112 0.031 ? 17 1 0.996 ? ? ? ? ? ? ? ? ? 
? 
3.580 4.090  ? ? ? ? ? ? 9889  100.000 ? ? ? ? 0.085 ? ? ? ? ? ? ? ? 13.500 ? 2.285 ? ? 0.088 0.024 ? 18 1 0.998 ? ? ? ? ? ? ? ? ? 
? 
4.090 5.160  ? ? ? ? ? ? 9994  100.000 ? ? ? ? 0.051 ? ? ? ? ? ? ? ? 13.600 ? 1.331 ? ? 0.053 0.015 ? 19 1 0.999 ? ? ? ? ? ? ? ? ? 
? 
5.160 50.000 ? ? ? ? ? ? 10366 99.700  ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 13.000 ? 1.175 ? ? 0.043 0.012 ? 20 1 0.999 ? ? ? ? ? ? ? ? ? 
? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                75.160 
_refine.B_iso_mean                               33.4739 
_refine.B_iso_min                                13.420 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_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                                 7XX3 
_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                            1.9000 
_refine.ls_d_res_low                             38.6900 
_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                     194865 
_refine.ls_number_reflns_R_free                  9830 
_refine.ls_number_reflns_R_work                  185035 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.6000 
_refine.ls_percent_reflns_R_free                 5.0400 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2001 
_refine.ls_R_factor_R_free                       0.2304 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1985 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_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                          1.340 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5YTO 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 23.9200 
_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                             ? 
_refine.overall_SU_ML                            0.2300 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.9000 
_refine_hist.d_res_low                        38.6900 
_refine_hist.number_atoms_solvent             1216 
_refine_hist.number_atoms_total               12221 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       1506 
_refine_hist.pdbx_B_iso_mean_ligand           49.00 
_refine_hist.pdbx_B_iso_mean_solvent          42.68 
_refine_hist.pdbx_number_atoms_protein        10906 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         99 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_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_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 1.9000 1.9200  6262 . 327 5935 97.0000  . . . 0.3676 0.0000 0.3250 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 1.9200 1.9400  6410 . 345 6065 99.0000  . . . 0.3580 0.0000 0.3128 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 1.9400 1.9600  6400 . 320 6080 99.0000  . . . 0.3105 0.0000 0.2795 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 1.9600 1.9900  6427 . 330 6097 99.0000  . . . 0.2983 0.0000 0.2672 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 1.9900 2.0100  6405 . 303 6102 99.0000  . . . 0.2666 0.0000 0.2415 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.0100 2.0400  6424 . 331 6093 100.0000 . . . 0.2729 0.0000 0.2308 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.0400 2.0700  6420 . 325 6095 100.0000 . . . 0.2351 0.0000 0.2204 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.0700 2.1000  6429 . 297 6132 100.0000 . . . 0.2535 0.0000 0.2252 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.1000 2.1300  6464 . 332 6132 100.0000 . . . 0.2440 0.0000 0.2203 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.1300 2.1700  6466 . 306 6160 100.0000 . . . 0.2729 0.0000 0.2206 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.1700 2.2100  6444 . 332 6112 100.0000 . . . 0.2546 0.0000 0.2263 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.2100 2.2500  6450 . 317 6133 100.0000 . . . 0.2639 0.0000 0.2297 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.2500 2.2900  6472 . 316 6156 100.0000 . . . 0.2504 0.0000 0.2244 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.2900 2.3400  6421 . 353 6068 100.0000 . . . 0.2423 0.0000 0.2234 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.3400 2.3900  6469 . 333 6136 100.0000 . . . 0.2639 0.0000 0.2205 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.3900 2.4400  6485 . 323 6162 100.0000 . . . 0.3004 0.0000 0.2279 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.4400 2.5000  6452 . 328 6124 100.0000 . . . 0.2726 0.0000 0.2298 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.5000 2.5700  6488 . 338 6150 100.0000 . . . 0.2596 0.0000 0.2224 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.5700 2.6500  6468 . 338 6130 100.0000 . . . 0.2583 0.0000 0.2227 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.6500 2.7300  6535 . 329 6206 100.0000 . . . 0.2497 0.0000 0.2173 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.7300 2.8300  6503 . 336 6167 100.0000 . . . 0.2535 0.0000 0.2214 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.8300 2.9400  6549 . 322 6227 100.0000 . . . 0.2663 0.0000 0.2130 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 2.9400 3.0800  6493 . 296 6197 100.0000 . . . 0.2455 0.0000 0.2029 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 3.0800 3.2400  6552 . 324 6228 100.0000 . . . 0.2055 0.0000 0.1874 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 3.2400 3.4400  6552 . 315 6237 100.0000 . . . 0.2154 0.0000 0.1850 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 3.4400 3.7100  6542 . 353 6189 100.0000 . . . 0.2225 0.0000 0.1724 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 3.7100 4.0800  6582 . 331 6251 100.0000 . . . 0.2022 0.0000 0.1568 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 4.0800 4.6700  6614 . 324 6290 99.0000  . . . 0.1692 0.0000 0.1507 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 4.6700 5.8800  6702 . 341 6361 100.0000 . . . 0.1789 0.0000 0.1605 . . . . . . . 30 . . . 
'X-RAY DIFFRACTION' 5.8800 38.6900 6985 . 365 6620 100.0000 . . . 0.2084 0.0000 0.1962 . . . . . . . 30 . . . 
# 
_struct.entry_id                     7XX3 
_struct.title                        
'Crystal structure of human Superoxide Dismutase (SOD1) in complex with a fungal metabolite molecule, Phialomustin B (PB)' 
_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        7XX3 
_struct_keywords.text            'Superoxide dismutase, protein aggregation, modulator, toxic trimer, 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 4 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 2 ? 
S  N N 4 ? 
T  N N 3 ? 
U  N N 2 ? 
V  N N 4 ? 
W  N N 2 ? 
X  N N 5 ? 
Y  N N 2 ? 
Z  N N 2 ? 
AA N N 2 ? 
BA N N 2 ? 
CA N N 4 ? 
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 ? 
MA 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 GLU A 159 ? LYS A 163 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P3  AA3 ALA B 82  ? GLY B 88  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4  AA4 SER B 134 ? CYS B 138 ? SER B 107 CYS B 111 5 ? 5 
HELX_P HELX_P5  AA5 GLU B 160 ? GLY B 165 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P6  AA6 ALA C 82  ? GLY C 88  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P7  AA7 GLU C 160 ? GLY C 165 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P8  AA8 ALA D 82  ? GLY D 88  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P9  AA9 GLU D 160 ? GLY D 165 ? GLU C 133 GLY C 138 1 ? 6 
HELX_P HELX_P10 AB1 ALA E 82  ? GLY E 88  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P11 AB2 ASN E 158 ? THR E 164 ? ASN H 131 THR H 137 1 ? 7 
HELX_P HELX_P12 AB3 ALA F 82  ? GLY F 88  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P13 AB4 SER F 134 ? CYS F 138 ? SER E 107 CYS E 111 5 ? 5 
HELX_P HELX_P14 AB5 GLU F 160 ? GLY F 165 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P15 AB6 ALA G 82  ? GLY G 88  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P16 AB7 SER G 134 ? CYS G 138 ? SER F 107 CYS F 111 5 ? 5 
HELX_P HELX_P17 AB8 ASN G 158 ? THR G 164 ? ASN F 131 THR F 137 1 ? 7 
HELX_P HELX_P18 AB9 ALA H 82  ? GLY H 88  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P19 AC1 SER H 134 ? CYS H 138 ? SER G 107 CYS G 111 5 ? 5 
HELX_P HELX_P20 AC2 GLU H 160 ? GLY H 165 ? GLU G 133 GLY G 138 1 ? 6 
HELX_P HELX_P21 AC3 ALA I 82  ? GLY I 88  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P22 AC4 ASN I 158 ? GLY I 165 ? ASN I 131 GLY I 138 1 ? 8 
HELX_P HELX_P23 AC5 ALA J 82  ? GLY J 88  ? ALA J 55  GLY J 61  5 ? 7 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 84  SG  ? ? ? 1_555 A  CYS 173 SG ? ? A CYS 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.128 ? ? 
disulf2  disulf ? ? B CYS 84  SG  ? ? ? 1_555 B  CYS 173 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
disulf3  disulf ? ? C CYS 84  SG  ? ? ? 1_555 C  CYS 173 SG ? ? D CYS 57 D CYS 146 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
disulf4  disulf ? ? D CYS 84  SG  ? ? ? 1_555 D  CYS 173 SG ? ? C CYS 57 C CYS 146 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
disulf5  disulf ? ? E CYS 84  SG  ? ? ? 1_555 E  CYS 173 SG ? ? H CYS 57 H CYS 146 1_555 ? ? ? ? ? ? ? 2.071 ? ? 
disulf6  disulf ? ? F CYS 84  SG  ? ? ? 1_555 F  CYS 173 SG ? ? E CYS 57 E CYS 146 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
disulf7  disulf ? ? G CYS 84  SG  ? ? ? 1_555 G  CYS 173 SG ? ? F CYS 57 F CYS 146 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
disulf8  disulf ? ? H CYS 84  SG  ? ? ? 1_555 H  CYS 173 SG ? ? G CYS 57 G CYS 146 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
disulf9  disulf ? ? I CYS 84  SG  ? ? ? 1_555 I  CYS 173 SG ? ? I CYS 57 I CYS 146 1_555 ? ? ? ? ? ? ? 2.093 ? ? 
disulf10 disulf ? ? J CYS 84  SG  ? ? ? 1_555 J  CYS 173 SG ? ? J CYS 57 J CYS 146 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc1  metalc ? ? A HIS 90  ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 63 A ZN  201 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc2  metalc ? ? A HIS 98  ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 71 A ZN  201 1_555 ? ? ? ? ? ? ? 2.217 ? ? 
metalc3  metalc ? ? A HIS 107 ND1 ? ? ? 1_555 K  ZN  .   ZN ? ? A HIS 80 A ZN  201 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc4  metalc ? ? A ASP 110 OD1 ? ? ? 1_555 K  ZN  .   ZN ? ? A ASP 83 A ZN  201 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc5  metalc ? ? B HIS 90  ND1 ? ? ? 1_555 M  ZN  .   ZN ? ? B HIS 63 B ZN  201 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc6  metalc ? ? B HIS 98  ND1 ? ? ? 1_555 M  ZN  .   ZN ? ? B HIS 71 B ZN  201 1_555 ? ? ? ? ? ? ? 2.162 ? ? 
metalc7  metalc ? ? B HIS 107 ND1 ? ? ? 1_555 M  ZN  .   ZN ? ? B HIS 80 B ZN  201 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc8  metalc ? ? B ASP 110 OD1 ? ? ? 1_555 M  ZN  .   ZN ? ? B ASP 83 B ZN  201 1_555 ? ? ? ? ? ? ? 1.964 ? ? 
metalc9  metalc ? ? C HIS 90  ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? D HIS 63 D ZN  201 1_555 ? ? ? ? ? ? ? 2.143 ? ? 
metalc10 metalc ? ? C HIS 98  ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? D HIS 71 D ZN  201 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc11 metalc ? ? C HIS 107 ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? D HIS 80 D ZN  201 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc12 metalc ? ? C ASP 110 OD1 ? ? ? 1_555 R  ZN  .   ZN ? ? D ASP 83 D ZN  201 1_555 ? ? ? ? ? ? ? 1.977 ? ? 
metalc13 metalc ? ? D HIS 90  ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? C HIS 63 C ZN  201 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc14 metalc ? ? D HIS 98  ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? C HIS 71 C ZN  201 1_555 ? ? ? ? ? ? ? 2.189 ? ? 
metalc15 metalc ? ? D HIS 107 ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? C HIS 80 C ZN  201 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc16 metalc ? ? D ASP 110 OD1 ? ? ? 1_555 U  ZN  .   ZN ? ? C ASP 83 C ZN  201 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc17 metalc ? ? E HIS 90  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? H HIS 63 H ZN  201 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc18 metalc ? ? E HIS 98  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? H HIS 71 H ZN  201 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc19 metalc ? ? E HIS 107 ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? H HIS 80 H ZN  201 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc20 metalc ? ? E ASP 110 OD1 ? ? ? 1_555 W  ZN  .   ZN ? ? H ASP 83 H ZN  201 1_555 ? ? ? ? ? ? ? 1.985 ? ? 
metalc21 metalc ? ? E ASP 110 OD2 ? ? ? 1_555 W  ZN  .   ZN ? ? H ASP 83 H ZN  201 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc22 metalc ? ? F HIS 90  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? E HIS 63 E ZN  202 1_555 ? ? ? ? ? ? ? 2.076 ? ? 
metalc23 metalc ? ? F HIS 98  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? E HIS 71 E ZN  202 1_555 ? ? ? ? ? ? ? 2.140 ? ? 
metalc24 metalc ? ? F HIS 107 ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? E HIS 80 E ZN  202 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc25 metalc ? ? F ASP 110 OD1 ? ? ? 1_555 Y  ZN  .   ZN ? ? E ASP 83 E ZN  202 1_555 ? ? ? ? ? ? ? 1.946 ? ? 
metalc26 metalc ? ? F ASP 110 OD2 ? ? ? 1_555 Y  ZN  .   ZN ? ? E ASP 83 E ZN  202 1_555 ? ? ? ? ? ? ? 2.587 ? ? 
metalc27 metalc ? ? G HIS 90  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 63 F ZN  201 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc28 metalc ? ? G HIS 98  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 71 F ZN  201 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc29 metalc ? ? G HIS 107 ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 80 F ZN  201 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc30 metalc ? ? G ASP 110 OD1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F ASP 83 F ZN  201 1_555 ? ? ? ? ? ? ? 1.968 ? ? 
metalc31 metalc ? ? H HIS 90  ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? G HIS 63 G ZN  201 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
metalc32 metalc ? ? H HIS 98  ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? G HIS 71 G ZN  201 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc33 metalc ? ? H HIS 107 ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? G HIS 80 G ZN  201 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc34 metalc ? ? H ASP 110 OD1 ? ? ? 1_555 AA ZN  .   ZN ? ? G ASP 83 G ZN  201 1_555 ? ? ? ? ? ? ? 1.964 ? ? 
metalc35 metalc ? ? H ASP 110 OD2 ? ? ? 1_555 AA ZN  .   ZN ? ? G ASP 83 G ZN  201 1_555 ? ? ? ? ? ? ? 2.438 ? ? 
metalc36 metalc ? ? I HIS 90  ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 63 I ZN  201 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc37 metalc ? ? I HIS 98  ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 71 I ZN  201 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc38 metalc ? ? I HIS 107 ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? I HIS 80 I ZN  201 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc39 metalc ? ? I ASP 110 OD1 ? ? ? 1_555 BA ZN  .   ZN ? ? I ASP 83 I ZN  201 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
# 
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 D 95  ASP D 101 
AA5 2 VAL C 56  ? LYS C 63  ? VAL D 29  LYS D 36  
AA5 3 GLN C 42  ? GLU C 48  ? GLN D 15  GLU D 21  
AA5 4 LYS C 30  ? LEU C 35  ? LYS D 3   LEU D 8   
AA5 5 GLY C 177 ? ILE C 178 ? GLY D 150 ILE D 151 
AA6 1 ASP C 110 ? ALA C 116 ? ASP D 83  ALA D 89  
AA6 2 GLY C 68  ? HIS C 75  ? GLY D 41  HIS D 48  
AA6 3 THR C 143 ? HIS C 147 ? THR D 116 HIS D 120 
AA6 4 ARG C 170 ? VAL C 175 ? ARG D 143 VAL D 148 
AA7 1 ALA D 122 ? ASP D 128 ? ALA C 95  ASP C 101 
AA7 2 VAL D 56  ? LYS D 63  ? VAL C 29  LYS C 36  
AA7 3 GLN D 42  ? GLU D 48  ? GLN C 15  GLU C 21  
AA7 4 LYS D 30  ? LEU D 35  ? LYS C 3   LEU C 8   
AA7 5 GLY D 177 ? ILE D 178 ? GLY C 150 ILE C 151 
AA8 1 ASP D 110 ? ALA D 116 ? ASP C 83  ALA C 89  
AA8 2 GLY D 68  ? HIS D 75  ? GLY C 41  HIS C 48  
AA8 3 THR D 143 ? HIS D 147 ? THR C 116 HIS C 120 
AA8 4 ARG D 170 ? VAL D 175 ? ARG C 143 VAL C 148 
AA9 1 ALA E 122 ? ASP E 128 ? ALA H 95  ASP H 101 
AA9 2 VAL E 56  ? LYS E 63  ? VAL H 29  LYS H 36  
AA9 3 GLN E 42  ? GLU E 48  ? GLN H 15  GLU H 21  
AA9 4 LYS E 30  ? LEU E 35  ? LYS H 3   LEU H 8   
AA9 5 GLY E 177 ? ILE E 178 ? GLY H 150 ILE H 151 
AB1 1 ASP E 110 ? ALA E 116 ? ASP H 83  ALA H 89  
AB1 2 GLY E 68  ? HIS E 75  ? GLY H 41  HIS H 48  
AB1 3 THR E 143 ? HIS E 147 ? THR H 116 HIS H 120 
AB1 4 ARG E 170 ? VAL E 175 ? ARG H 143 VAL H 148 
AB2 1 ALA F 122 ? ASP F 128 ? ALA E 95  ASP E 101 
AB2 2 VAL F 56  ? LYS F 63  ? VAL E 29  LYS E 36  
AB2 3 GLN F 42  ? GLU F 48  ? GLN E 15  GLU E 21  
AB2 4 LYS F 30  ? LEU F 35  ? LYS E 3   LEU E 8   
AB2 5 GLY F 177 ? ILE F 178 ? GLY E 150 ILE E 151 
AB3 1 ASP F 110 ? ALA F 116 ? ASP E 83  ALA E 89  
AB3 2 GLY F 68  ? HIS F 75  ? GLY E 41  HIS E 48  
AB3 3 THR F 143 ? HIS F 147 ? THR E 116 HIS E 120 
AB3 4 ARG F 170 ? VAL F 175 ? ARG E 143 VAL E 148 
AB4 1 ALA G 122 ? ASP G 128 ? ALA F 95  ASP F 101 
AB4 2 VAL G 56  ? LYS G 63  ? VAL F 29  LYS F 36  
AB4 3 GLN G 42  ? GLU G 48  ? GLN F 15  GLU F 21  
AB4 4 LYS G 30  ? LYS G 36  ? LYS F 3   LYS F 9   
AB4 5 GLY G 177 ? ILE G 178 ? GLY F 150 ILE F 151 
AB5 1 ASP G 110 ? ALA G 116 ? ASP F 83  ALA F 89  
AB5 2 GLY G 68  ? HIS G 75  ? GLY F 41  HIS F 48  
AB5 3 THR G 143 ? HIS G 147 ? THR F 116 HIS F 120 
AB5 4 ARG G 170 ? VAL G 175 ? ARG F 143 VAL F 148 
AB6 1 ALA H 122 ? ASP H 128 ? ALA G 95  ASP G 101 
AB6 2 VAL H 56  ? LYS H 63  ? VAL G 29  LYS G 36  
AB6 3 GLN H 42  ? GLU H 48  ? GLN G 15  GLU G 21  
AB6 4 LYS H 30  ? LYS H 36  ? LYS G 3   LYS G 9   
AB6 5 GLY H 177 ? ALA H 179 ? GLY G 150 ALA G 152 
AB7 1 ASP H 110 ? ALA H 116 ? ASP G 83  ALA G 89  
AB7 2 GLY H 68  ? HIS H 75  ? GLY G 41  HIS G 48  
AB7 3 THR H 143 ? HIS H 147 ? THR G 116 HIS G 120 
AB7 4 ARG H 170 ? VAL H 175 ? ARG G 143 VAL G 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  ? GLU I 48  ? GLN I 15  GLU I 21  
AB8 4 LYS I 30  ? LEU I 35  ? LYS I 3   LEU I 8   
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 PHE A 47  ? O PHE A 20  N ALA A 31  ? N ALA A 4   
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 GLY B 43  ? O GLY B 16  N LEU B 35  ? N LEU B 8   
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 ALA B 172 ? O ALA B 145 
AA5 1 2 O ASP C 128 ? O ASP D 101 N VAL C 56  ? N VAL D 29  
AA5 2 3 O LYS C 63  ? O LYS D 36  N GLN C 42  ? N GLN D 15  
AA5 3 4 O ILE C 45  ? O ILE D 18  N CYS C 33  ? N CYS D 6   
AA5 4 5 N VAL C 32  ? N VAL D 5   O GLY C 177 ? O GLY D 150 
AA6 1 2 O ALA C 116 ? O ALA D 89  N GLY C 68  ? N GLY D 41  
AA6 2 3 N HIS C 75  ? N HIS D 48  O THR C 143 ? O THR D 116 
AA6 3 4 N LEU C 144 ? N LEU D 117 O GLY C 174 ? O GLY D 147 
AA7 1 2 O ILE D 126 ? O ILE C 99  N VAL D 58  ? N VAL C 31  
AA7 2 3 O TRP D 59  ? O TRP C 32  N ASN D 46  ? N ASN C 19  
AA7 3 4 O PHE D 47  ? O PHE C 20  N ALA D 31  ? N ALA C 4   
AA7 4 5 N VAL D 32  ? N VAL C 5   O GLY D 177 ? O GLY C 150 
AA8 1 2 O ALA D 116 ? O ALA C 89  N GLY D 68  ? N GLY C 41  
AA8 2 3 N HIS D 75  ? N HIS C 48  O THR D 143 ? O THR C 116 
AA8 3 4 N VAL D 146 ? N VAL C 119 O ALA D 172 ? O ALA C 145 
AA9 1 2 O ILE E 126 ? O ILE H 99  N VAL E 58  ? N VAL H 31  
AA9 2 3 O LYS E 63  ? O LYS H 36  N GLN E 42  ? N GLN H 15  
AA9 3 4 O ILE E 45  ? O ILE H 18  N CYS E 33  ? N CYS H 6   
AA9 4 5 N VAL E 32  ? N VAL H 5   O GLY E 177 ? O GLY H 150 
AB1 1 2 O ALA E 116 ? O ALA H 89  N GLY E 68  ? N GLY H 41  
AB1 2 3 N HIS E 75  ? N HIS H 48  O THR E 143 ? O THR H 116 
AB1 3 4 N LEU E 144 ? N LEU H 117 O GLY E 174 ? O GLY H 147 
AB2 1 2 O ASP F 128 ? O ASP E 101 N VAL F 56  ? N VAL E 29  
AB2 2 3 O TRP F 59  ? O TRP E 32  N ASN F 46  ? N ASN E 19  
AB2 3 4 O PHE F 47  ? O PHE E 20  N ALA F 31  ? N ALA E 4   
AB2 4 5 N VAL F 32  ? N VAL E 5   O GLY F 177 ? O GLY E 150 
AB3 1 2 O ALA F 116 ? O ALA E 89  N GLY F 68  ? N GLY E 41  
AB3 2 3 N HIS F 75  ? N HIS E 48  O THR F 143 ? O THR E 116 
AB3 3 4 N LEU F 144 ? N LEU E 117 O GLY F 174 ? O GLY E 147 
AB4 1 2 O ASP G 128 ? O ASP F 101 N VAL G 56  ? N VAL F 29  
AB4 2 3 O TRP G 59  ? O TRP F 32  N ASN G 46  ? N ASN F 19  
AB4 3 4 O PHE G 47  ? O PHE F 20  N ALA G 31  ? N ALA F 4   
AB4 4 5 N VAL G 32  ? N VAL F 5   O GLY G 177 ? O GLY F 150 
AB5 1 2 O ALA G 116 ? O ALA F 89  N GLY G 68  ? N GLY F 41  
AB5 2 3 N HIS G 75  ? N HIS F 48  O THR G 143 ? O THR F 116 
AB5 3 4 N LEU G 144 ? N LEU F 117 O GLY G 174 ? O GLY F 147 
AB6 1 2 O ASP H 128 ? O ASP G 101 N VAL H 56  ? N VAL G 29  
AB6 2 3 O TRP H 59  ? O TRP G 32  N ASN H 46  ? N ASN G 19  
AB6 3 4 O GLY H 43  ? O GLY G 16  N LEU H 35  ? N LEU G 8   
AB6 4 5 N VAL H 32  ? N VAL G 5   O GLY H 177 ? O GLY G 150 
AB7 1 2 O ALA H 116 ? O ALA G 89  N GLY H 68  ? N GLY G 41  
AB7 2 3 N HIS H 75  ? N HIS G 48  O THR H 143 ? O THR G 116 
AB7 3 4 N LEU H 144 ? N LEU G 117 O GLY H 174 ? O GLY G 147 
AB8 1 2 O ALA I 122 ? O ALA I 95  N ILE I 62  ? N ILE I 35  
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 ALA J 122 ? O ALA J 95  N ILE J 62  ? N ILE J 35  
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 
# 
_atom_sites.entry_id                    7XX3 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.004125 
_atom_sites.fract_transf_matrix[1][2]   0.002381 
_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]   0.004763 
_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]   0.006921 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . MET A  1 27  ? 61.458  49.052  -2.964  1.00 42.95 ? 0   MET A N   1 
ATOM   2     C  CA  . MET A  1 27  ? 60.907  49.992  -3.948  1.00 48.63 ? 0   MET A CA  1 
ATOM   3     C  C   . MET A  1 27  ? 60.674  49.317  -5.300  1.00 47.82 ? 0   MET A C   1 
ATOM   4     O  O   . MET A  1 27  ? 59.747  48.513  -5.449  1.00 48.44 ? 0   MET A O   1 
ATOM   5     C  CB  . MET A  1 27  ? 61.833  51.201  -4.119  1.00 48.46 ? 0   MET A CB  1 
ATOM   6     N  N   . ALA A  1 28  ? 61.513  49.651  -6.284  1.00 41.41 ? 1   ALA A N   1 
ATOM   7     C  CA  . ALA A  1 28  ? 61.386  49.054  -7.607  1.00 36.42 ? 1   ALA A CA  1 
ATOM   8     C  C   . ALA A  1 28  ? 61.661  47.558  -7.551  1.00 27.35 ? 1   ALA A C   1 
ATOM   9     O  O   . ALA A  1 28  ? 62.604  47.109  -6.894  1.00 28.95 ? 1   ALA A O   1 
ATOM   10    C  CB  . ALA A  1 28  ? 62.350  49.716  -8.589  1.00 31.74 ? 1   ALA A CB  1 
ATOM   11    N  N   . THR A  1 29  ? 60.829  46.783  -8.248  1.00 25.36 ? 2   THR A N   1 
ATOM   12    C  CA  . THR A  1 29  ? 61.059  45.352  -8.409  1.00 27.68 ? 2   THR A CA  1 
ATOM   13    C  C   . THR A  1 29  ? 61.463  44.971  -9.821  1.00 22.08 ? 2   THR A C   1 
ATOM   14    O  O   . THR A  1 29  ? 61.926  43.847  -10.031 1.00 22.86 ? 2   THR A O   1 
ATOM   15    C  CB  . THR A  1 29  ? 59.800  44.549  -8.046  1.00 28.58 ? 2   THR A CB  1 
ATOM   16    O  OG1 . THR A  1 29  ? 58.723  44.958  -8.896  1.00 33.26 ? 2   THR A OG1 1 
ATOM   17    C  CG2 . THR A  1 29  ? 59.422  44.747  -6.588  1.00 33.45 ? 2   THR A CG2 1 
ATOM   18    N  N   . LYS A  1 30  ? 61.243  45.856  -10.789 1.00 21.37 ? 3   LYS A N   1 
ATOM   19    C  CA  . LYS A  1 30  ? 61.485  45.604  -12.207 1.00 20.62 ? 3   LYS A CA  1 
ATOM   20    C  C   . LYS A  1 30  ? 62.168  46.811  -12.820 1.00 20.42 ? 3   LYS A C   1 
ATOM   21    O  O   . LYS A  1 30  ? 61.816  47.955  -12.520 1.00 19.98 ? 3   LYS A O   1 
ATOM   22    C  CB  . LYS A  1 30  ? 60.202  45.331  -13.000 1.00 24.65 ? 3   LYS A CB  1 
ATOM   23    C  CG  . LYS A  1 30  ? 59.215  44.373  -12.408 1.00 36.31 ? 3   LYS A CG  1 
ATOM   24    C  CD  . LYS A  1 30  ? 58.553  43.655  -13.582 1.00 38.97 ? 3   LYS A CD  1 
ATOM   25    C  CE  . LYS A  1 30  ? 57.941  42.326  -13.213 1.00 48.22 ? 3   LYS A CE  1 
ATOM   26    N  NZ  . LYS A  1 30  ? 58.983  41.284  -13.380 1.00 56.89 ? 3   LYS A NZ  1 
ATOM   27    N  N   . ALA A  1 31  ? 63.134  46.548  -13.697 1.00 18.12 ? 4   ALA A N   1 
ATOM   28    C  CA  . ALA A  1 31  ? 63.795  47.591  -14.460 1.00 18.98 ? 4   ALA A CA  1 
ATOM   29    C  C   . ALA A  1 31  ? 64.047  47.065  -15.865 1.00 18.71 ? 4   ALA A C   1 
ATOM   30    O  O   . ALA A  1 31  ? 63.922  45.862  -16.133 1.00 19.35 ? 4   ALA A O   1 
ATOM   31    C  CB  . ALA A  1 31  ? 65.105  48.045  -13.797 1.00 18.36 ? 4   ALA A CB  1 
ATOM   32    N  N   . VAL A  1 32  ? 64.373  47.982  -16.778 1.00 19.98 ? 5   VAL A N   1 
ATOM   33    C  CA  . VAL A  1 32  ? 64.594  47.617  -18.172 1.00 16.68 ? 5   VAL A CA  1 
ATOM   34    C  C   . VAL A  1 32  ? 65.611  48.571  -18.770 1.00 20.36 ? 5   VAL A C   1 
ATOM   35    O  O   . VAL A  1 32  ? 65.757  49.719  -18.335 1.00 21.27 ? 5   VAL A O   1 
ATOM   36    C  CB  . VAL A  1 32  ? 63.269  47.612  -18.967 1.00 16.21 ? 5   VAL A CB  1 
ATOM   37    C  CG1 . VAL A  1 32  ? 62.737  49.020  -19.124 1.00 18.45 ? 5   VAL A CG1 1 
ATOM   38    C  CG2 . VAL A  1 32  ? 63.462  46.952  -20.352 1.00 21.39 ? 5   VAL A CG2 1 
ATOM   39    N  N   . CYS A  1 33  ? 66.329  48.094  -19.782 1.00 16.74 ? 6   CYS A N   1 
ATOM   40    C  CA  . CYS A  1 33  ? 67.359  48.905  -20.401 1.00 16.08 ? 6   CYS A CA  1 
ATOM   41    C  C   . CYS A  1 33  ? 67.353  48.626  -21.898 1.00 18.80 ? 6   CYS A C   1 
ATOM   42    O  O   . CYS A  1 33  ? 67.407  47.462  -22.296 1.00 15.28 ? 6   CYS A O   1 
ATOM   43    C  CB  . CYS A  1 33  ? 68.738  48.576  -19.815 1.00 16.97 ? 6   CYS A CB  1 
ATOM   44    S  SG  . CYS A  1 33  ? 70.069  49.572  -20.546 1.00 21.25 ? 6   CYS A SG  1 
ATOM   45    N  N   . VAL A  1 34  ? 67.262  49.677  -22.703 1.00 15.42 ? 7   VAL A N   1 
ATOM   46    C  CA  . VAL A  1 34  ? 67.372  49.579  -24.161 1.00 16.63 ? 7   VAL A CA  1 
ATOM   47    C  C   . VAL A  1 34  ? 68.790  49.986  -24.544 1.00 20.18 ? 7   VAL A C   1 
ATOM   48    O  O   . VAL A  1 34  ? 69.211  51.122  -24.288 1.00 20.10 ? 7   VAL A O   1 
ATOM   49    C  CB  . VAL A  1 34  ? 66.334  50.458  -24.875 1.00 20.13 ? 7   VAL A CB  1 
ATOM   50    C  CG1 . VAL A  1 34  ? 66.543  50.398  -26.430 1.00 24.69 ? 7   VAL A CG1 1 
ATOM   51    C  CG2 . VAL A  1 34  ? 64.924  50.039  -24.510 1.00 21.57 ? 7   VAL A CG2 1 
ATOM   52    N  N   . LEU A  1 35  ? 69.535  49.059  -25.142 1.00 16.50 ? 8   LEU A N   1 
ATOM   53    C  CA  . LEU A  1 35  ? 70.927  49.298  -25.504 1.00 17.44 ? 8   LEU A CA  1 
ATOM   54    C  C   . LEU A  1 35  ? 71.016  49.738  -26.959 1.00 17.97 ? 8   LEU A C   1 
ATOM   55    O  O   . LEU A  1 35  ? 70.463  49.076  -27.841 1.00 22.85 ? 8   LEU A O   1 
ATOM   56    C  CB  . LEU A  1 35  ? 71.748  48.024  -25.289 1.00 17.36 ? 8   LEU A CB  1 
ATOM   57    C  CG  . LEU A  1 35  ? 71.829  47.504  -23.844 1.00 21.16 ? 8   LEU A CG  1 
ATOM   58    C  CD1 . LEU A  1 35  ? 72.346  46.078  -23.868 1.00 31.78 ? 8   LEU A CD1 1 
ATOM   59    C  CD2 . LEU A  1 35  ? 72.755  48.348  -23.018 1.00 29.48 ? 8   LEU A CD2 1 
ATOM   60    N  N   . LYS A  1 36  ? 71.710  50.854  -27.205 1.00 20.36 ? 9   LYS A N   1 
ATOM   61    C  CA  . LYS A  1 36  ? 71.969  51.362  -28.554 1.00 23.82 ? 9   LYS A CA  1 
ATOM   62    C  C   . LYS A  1 36  ? 73.388  51.902  -28.620 1.00 23.22 ? 9   LYS A C   1 
ATOM   63    O  O   . LYS A  1 36  ? 73.965  52.295  -27.606 1.00 20.61 ? 9   LYS A O   1 
ATOM   64    C  CB  . LYS A  1 36  ? 71.005  52.497  -28.950 1.00 28.45 ? 9   LYS A CB  1 
ATOM   65    C  CG  . LYS A  1 36  ? 69.529  52.147  -28.908 1.00 37.47 ? 9   LYS A CG  1 
ATOM   66    C  CD  . LYS A  1 36  ? 69.192  51.097  -29.968 1.00 49.84 ? 9   LYS A CD  1 
ATOM   67    C  CE  . LYS A  1 36  ? 67.761  50.574  -29.838 1.00 46.88 ? 9   LYS A CE  1 
ATOM   68    N  NZ  . LYS A  1 36  ? 67.732  49.182  -29.297 1.00 39.41 ? 9   LYS A NZ  1 
ATOM   69    N  N   . GLY A  1 37  ? 73.932  51.980  -29.831 1.00 18.88 ? 10  GLY A N   1 
ATOM   70    C  CA  . GLY A  1 37  ? 75.269  52.506  -29.975 1.00 19.85 ? 10  GLY A CA  1 
ATOM   71    C  C   . GLY A  1 37  ? 75.485  53.086  -31.360 1.00 22.30 ? 10  GLY A C   1 
ATOM   72    O  O   . GLY A  1 37  ? 74.546  53.263  -32.131 1.00 28.49 ? 10  GLY A O   1 
ATOM   73    N  N   . ASP A  1 38  ? 76.751  53.394  -31.655 1.00 28.42 ? 11  ASP A N   1 
ATOM   74    C  CA  . ASP A  1 38  ? 77.130  53.900  -32.975 1.00 34.97 ? 11  ASP A CA  1 
ATOM   75    C  C   . ASP A  1 38  ? 77.091  52.828  -34.054 1.00 32.74 ? 11  ASP A C   1 
ATOM   76    O  O   . ASP A  1 38  ? 76.938  53.167  -35.236 1.00 37.84 ? 11  ASP A O   1 
ATOM   77    C  CB  . ASP A  1 38  ? 78.535  54.506  -32.928 1.00 30.82 ? 11  ASP A CB  1 
ATOM   78    C  CG  . ASP A  1 38  ? 78.579  55.819  -32.179 1.00 49.62 ? 11  ASP A CG  1 
ATOM   79    O  OD1 . ASP A  1 38  ? 77.530  56.501  -32.126 1.00 47.08 ? 11  ASP A OD1 1 
ATOM   80    O  OD2 . ASP A  1 38  ? 79.644  56.145  -31.605 1.00 52.30 ? 11  ASP A OD2 1 
ATOM   81    N  N   . GLY A  1 39  ? 77.239  51.556  -33.686 1.00 33.29 ? 12  GLY A N   1 
ATOM   82    C  CA  . GLY A  1 39  ? 77.228  50.478  -34.649 1.00 27.71 ? 12  GLY A CA  1 
ATOM   83    C  C   . GLY A  1 39  ? 75.913  49.736  -34.650 1.00 24.53 ? 12  GLY A C   1 
ATOM   84    O  O   . GLY A  1 39  ? 74.860  50.293  -34.337 1.00 25.80 ? 12  GLY A O   1 
ATOM   85    N  N   . PRO A  1 40  ? 75.955  48.451  -35.017 1.00 24.54 ? 13  PRO A N   1 
ATOM   86    C  CA  . PRO A  1 40  ? 74.736  47.636  -35.101 1.00 21.80 ? 13  PRO A CA  1 
ATOM   87    C  C   . PRO A  1 40  ? 74.298  46.981  -33.795 1.00 22.59 ? 13  PRO A C   1 
ATOM   88    O  O   . PRO A  1 40  ? 73.282  46.276  -33.791 1.00 23.73 ? 13  PRO A O   1 
ATOM   89    C  CB  . PRO A  1 40  ? 75.142  46.555  -36.115 1.00 24.63 ? 13  PRO A CB  1 
ATOM   90    C  CG  . PRO A  1 40  ? 76.594  46.358  -35.847 1.00 26.60 ? 13  PRO A CG  1 
ATOM   91    C  CD  . PRO A  1 40  ? 77.149  47.712  -35.472 1.00 28.82 ? 13  PRO A CD  1 
ATOM   92    N  N   . VAL A  1 41  ? 75.018  47.157  -32.692 1.00 21.54 ? 14  VAL A N   1 
ATOM   93    C  CA  . VAL A  1 41  ? 74.656  46.434  -31.479 1.00 20.76 ? 14  VAL A CA  1 
ATOM   94    C  C   . VAL A  1 41  ? 73.414  47.059  -30.859 1.00 26.13 ? 14  VAL A C   1 
ATOM   95    O  O   . VAL A  1 41  ? 73.366  48.270  -30.616 1.00 25.10 ? 14  VAL A O   1 
ATOM   96    C  CB  . VAL A  1 41  ? 75.820  46.418  -30.481 1.00 19.13 ? 14  VAL A CB  1 
ATOM   97    C  CG1 . VAL A  1 41  ? 75.395  45.663  -29.222 1.00 18.13 ? 14  VAL A CG1 1 
ATOM   98    C  CG2 . VAL A  1 41  ? 77.025  45.725  -31.099 1.00 24.59 ? 14  VAL A CG2 1 
ATOM   99    N  N   . GLN A  1 42  ? 72.404  46.237  -30.596 1.00 23.86 ? 15  GLN A N   1 
ATOM   100   C  CA  . GLN A  1 42  ? 71.232  46.731  -29.889 1.00 20.66 ? 15  GLN A CA  1 
ATOM   101   C  C   . GLN A  1 42  ? 70.559  45.587  -29.155 1.00 27.58 ? 15  GLN A C   1 
ATOM   102   O  O   . GLN A  1 42  ? 70.676  44.415  -29.537 1.00 24.52 ? 15  GLN A O   1 
ATOM   103   C  CB  . GLN A  1 42  ? 70.245  47.417  -30.831 1.00 34.74 ? 15  GLN A CB  1 
ATOM   104   C  CG  . GLN A  1 42  ? 70.109  46.763  -32.173 1.00 36.45 ? 15  GLN A CG  1 
ATOM   105   C  CD  . GLN A  1 42  ? 69.184  47.553  -33.094 1.00 47.78 ? 15  GLN A CD  1 
ATOM   106   O  OE1 . GLN A  1 42  ? 69.609  48.083  -34.116 1.00 47.49 ? 15  GLN A OE1 1 
ATOM   107   N  NE2 . GLN A  1 42  ? 67.915  47.645  -32.717 1.00 46.96 ? 15  GLN A NE2 1 
ATOM   108   N  N   . GLY A  1 43  ? 69.865  45.933  -28.080 1.00 25.07 ? 16  GLY A N   1 
ATOM   109   C  CA  . GLY A  1 43  ? 69.131  44.895  -27.386 1.00 25.75 ? 16  GLY A CA  1 
ATOM   110   C  C   . GLY A  1 43  ? 68.267  45.480  -26.299 1.00 27.05 ? 16  GLY A C   1 
ATOM   111   O  O   . GLY A  1 43  ? 68.213  46.694  -26.101 1.00 21.31 ? 16  GLY A O   1 
ATOM   112   N  N   . ILE A  1 44  ? 67.581  44.585  -25.608 1.00 22.10 ? 17  ILE A N   1 
ATOM   113   C  CA  . ILE A  1 44  ? 66.729  44.927  -24.477 1.00 23.55 ? 17  ILE A CA  1 
ATOM   114   C  C   . ILE A  1 44  ? 67.139  44.024  -23.327 1.00 20.64 ? 17  ILE A C   1 
ATOM   115   O  O   . ILE A  1 44  ? 67.199  42.800  -23.493 1.00 21.66 ? 17  ILE A O   1 
ATOM   116   C  CB  . ILE A  1 44  ? 65.235  44.746  -24.822 1.00 21.66 ? 17  ILE A CB  1 
ATOM   117   C  CG1 . ILE A  1 44  ? 64.823  45.702  -25.944 1.00 26.99 ? 17  ILE A CG1 1 
ATOM   118   C  CG2 . ILE A  1 44  ? 64.371  44.934  -23.575 1.00 21.69 ? 17  ILE A CG2 1 
ATOM   119   C  CD1 . ILE A  1 44  ? 63.440  45.405  -26.534 1.00 33.61 ? 17  ILE A CD1 1 
ATOM   120   N  N   . ILE A  1 45  ? 67.449  44.617  -22.170 1.00 18.94 ? 18  ILE A N   1 
ATOM   121   C  CA  . ILE A  1 45  ? 67.803  43.854  -20.977 1.00 13.42 ? 18  ILE A CA  1 
ATOM   122   C  C   . ILE A  1 45  ? 66.786  44.160  -19.880 1.00 19.95 ? 18  ILE A C   1 
ATOM   123   O  O   . ILE A  1 45  ? 66.542  45.330  -19.560 1.00 19.15 ? 18  ILE A O   1 
ATOM   124   C  CB  . ILE A  1 45  ? 69.232  44.174  -20.500 1.00 17.98 ? 18  ILE A CB  1 
ATOM   125   C  CG1 . ILE A  1 45  ? 70.274  43.798  -21.584 1.00 18.07 ? 18  ILE A CG1 1 
ATOM   126   C  CG2 . ILE A  1 45  ? 69.519  43.441  -19.201 1.00 13.91 ? 18  ILE A CG2 1 
ATOM   127   C  CD1 . ILE A  1 45  ? 70.328  42.290  -21.875 1.00 20.80 ? 18  ILE A CD1 1 
ATOM   128   N  N   . ASN A  1 46  ? 66.210  43.110  -19.303 1.00 19.87 ? 19  ASN A N   1 
ATOM   129   C  CA  . ASN A  1 46  ? 65.268  43.192  -18.195 1.00 23.27 ? 19  ASN A CA  1 
ATOM   130   C  C   . ASN A  1 46  ? 65.964  42.904  -16.876 1.00 20.29 ? 19  ASN A C   1 
ATOM   131   O  O   . ASN A  1 46  ? 66.916  42.117  -16.817 1.00 19.26 ? 19  ASN A O   1 
ATOM   132   C  CB  . ASN A  1 46  ? 64.133  42.187  -18.384 1.00 21.17 ? 19  ASN A CB  1 
ATOM   133   C  CG  . ASN A  1 46  ? 63.499  42.287  -19.752 1.00 25.09 ? 19  ASN A CG  1 
ATOM   134   O  OD1 . ASN A  1 46  ? 63.799  41.503  -20.665 1.00 28.90 ? 19  ASN A OD1 1 
ATOM   135   N  ND2 . ASN A  1 46  ? 62.634  43.271  -19.909 1.00 23.02 ? 19  ASN A ND2 1 
ATOM   136   N  N   . PHE A  1 47  ? 65.466  43.535  -15.796 1.00 18.25 ? 20  PHE A N   1 
ATOM   137   C  CA  . PHE A  1 47  ? 65.936  43.265  -14.445 1.00 16.83 ? 20  PHE A CA  1 
ATOM   138   C  C   . PHE A  1 47  ? 64.739  42.979  -13.556 1.00 22.54 ? 20  PHE A C   1 
ATOM   139   O  O   . PHE A  1 47  ? 63.710  43.654  -13.671 1.00 21.74 ? 20  PHE A O   1 
ATOM   140   C  CB  . PHE A  1 47  ? 66.700  44.463  -13.835 1.00 18.41 ? 20  PHE A CB  1 
ATOM   141   C  CG  . PHE A  1 47  ? 67.865  44.941  -14.651 1.00 19.77 ? 20  PHE A CG  1 
ATOM   142   C  CD1 . PHE A  1 47  ? 67.663  45.682  -15.808 1.00 23.11 ? 20  PHE A CD1 1 
ATOM   143   C  CD2 . PHE A  1 47  ? 69.161  44.693  -14.238 1.00 20.67 ? 20  PHE A CD2 1 
ATOM   144   C  CE1 . PHE A  1 47  ? 68.741  46.141  -16.559 1.00 21.46 ? 20  PHE A CE1 1 
ATOM   145   C  CE2 . PHE A  1 47  ? 70.242  45.151  -14.976 1.00 23.72 ? 20  PHE A CE2 1 
ATOM   146   C  CZ  . PHE A  1 47  ? 70.032  45.876  -16.139 1.00 17.24 ? 20  PHE A CZ  1 
ATOM   147   N  N   . GLU A  1 48  ? 64.884  42.007  -12.645 1.00 22.07 ? 21  GLU A N   1 
ATOM   148   C  CA  . GLU A  1 48  ? 63.828  41.646  -11.697 1.00 22.29 ? 21  GLU A CA  1 
ATOM   149   C  C   . GLU A  1 48  ? 64.419  41.371  -10.326 1.00 24.16 ? 21  GLU A C   1 
ATOM   150   O  O   . GLU A  1 48  ? 65.374  40.600  -10.190 1.00 21.77 ? 21  GLU A O   1 
ATOM   151   C  CB  . GLU A  1 48  ? 63.016  40.423  -12.144 1.00 28.50 ? 21  GLU A CB  1 
ATOM   152   C  CG  . GLU A  1 48  ? 61.790  40.187  -11.240 1.00 34.87 ? 21  GLU A CG  1 
ATOM   153   C  CD  . GLU A  1 48  ? 60.754  39.234  -11.812 1.00 54.18 ? 21  GLU A CD  1 
ATOM   154   O  OE1 . GLU A  1 48  ? 61.041  38.027  -11.913 1.00 56.74 ? 21  GLU A OE1 1 
ATOM   155   O  OE2 . GLU A  1 48  ? 59.619  39.666  -12.067 1.00 59.46 ? 21  GLU A OE2 1 
ATOM   156   N  N   . GLN A  1 49  ? 63.841  41.997  -9.307  1.00 20.47 ? 22  GLN A N   1 
ATOM   157   C  CA  . GLN A  1 49  ? 64.286  41.775  -7.927  1.00 20.49 ? 22  GLN A CA  1 
ATOM   158   C  C   . GLN A  1 49  ? 63.026  41.676  -7.066  1.00 23.42 ? 22  GLN A C   1 
ATOM   159   O  O   . GLN A  1 49  ? 62.476  42.691  -6.627  1.00 29.76 ? 22  GLN A O   1 
ATOM   160   C  CB  . GLN A  1 49  ? 65.218  42.881  -7.460  1.00 19.09 ? 22  GLN A CB  1 
ATOM   161   C  CG  . GLN A  1 49  ? 65.839  42.626  -6.105  1.00 20.77 ? 22  GLN A CG  1 
ATOM   162   C  CD  . GLN A  1 49  ? 66.673  43.792  -5.680  1.00 19.40 ? 22  GLN A CD  1 
ATOM   163   O  OE1 . GLN A  1 49  ? 66.438  44.908  -6.130  1.00 22.45 ? 22  GLN A OE1 1 
ATOM   164   N  NE2 . GLN A  1 49  ? 67.696  43.543  -4.871  1.00 20.37 ? 22  GLN A NE2 1 
ATOM   165   N  N   . LYS A  1 50  ? 62.561  40.445  -6.855  1.00 25.15 ? 23  LYS A N   1 
ATOM   166   C  CA  . LYS A  1 50  ? 61.300  40.268  -6.146  1.00 32.38 ? 23  LYS A CA  1 
ATOM   167   C  C   . LYS A  1 50  ? 61.414  40.648  -4.672  1.00 29.27 ? 23  LYS A C   1 
ATOM   168   O  O   . LYS A  1 50  ? 60.442  41.141  -4.093  1.00 32.69 ? 23  LYS A O   1 
ATOM   169   C  CB  . LYS A  1 50  ? 60.806  38.833  -6.301  1.00 36.78 ? 23  LYS A CB  1 
ATOM   170   C  CG  . LYS A  1 50  ? 60.680  38.380  -7.747  1.00 46.87 ? 23  LYS A CG  1 
ATOM   171   C  CD  . LYS A  1 50  ? 60.609  36.855  -7.854  1.00 55.93 ? 23  LYS A CD  1 
ATOM   172   C  CE  . LYS A  1 50  ? 59.549  36.412  -8.857  1.00 51.81 ? 23  LYS A CE  1 
ATOM   173   N  NZ  . LYS A  1 50  ? 59.467  34.923  -8.943  1.00 48.68 ? 23  LYS A NZ  1 
ATOM   174   N  N   . GLU A  1 51  ? 62.581  40.449  -4.053  1.00 28.10 ? 24  GLU A N   1 
ATOM   175   C  CA  . GLU A  1 51  ? 62.814  40.895  -2.685  1.00 29.69 ? 24  GLU A CA  1 
ATOM   176   C  C   . GLU A  1 51  ? 63.949  41.900  -2.657  1.00 28.00 ? 24  GLU A C   1 
ATOM   177   O  O   . GLU A  1 51  ? 64.980  41.698  -3.298  1.00 24.99 ? 24  GLU A O   1 
ATOM   178   C  CB  . GLU A  1 51  ? 63.140  39.732  -1.745  1.00 32.96 ? 24  GLU A CB  1 
ATOM   179   C  CG  . GLU A  1 51  ? 62.043  38.681  -1.690  1.00 38.07 ? 24  GLU A CG  1 
ATOM   180   C  CD  . GLU A  1 51  ? 62.594  37.276  -1.729  1.00 62.14 ? 24  GLU A CD  1 
ATOM   181   O  OE1 . GLU A  1 51  ? 63.393  36.931  -0.831  1.00 72.91 ? 24  GLU A OE1 1 
ATOM   182   O  OE2 . GLU A  1 51  ? 62.233  36.516  -2.655  1.00 70.77 ? 24  GLU A OE2 1 
ATOM   183   N  N   . SER A  1 52  ? 63.768  42.967  -1.872  1.00 25.84 ? 25  SER A N   1 
ATOM   184   C  CA  . SER A  1 52  ? 64.743  44.051  -1.853  1.00 20.10 ? 25  SER A CA  1 
ATOM   185   C  C   . SER A  1 52  ? 66.095  43.602  -1.315  1.00 22.60 ? 25  SER A C   1 
ATOM   186   O  O   . SER A  1 52  ? 67.109  44.246  -1.599  1.00 25.77 ? 25  SER A O   1 
ATOM   187   C  CB  . SER A  1 52  ? 64.215  45.216  -1.016  1.00 30.77 ? 25  SER A CB  1 
ATOM   188   O  OG  . SER A  1 52  ? 63.909  44.775  0.296   1.00 30.11 ? 25  SER A OG  1 
ATOM   189   N  N   . ASN A  1 53  ? 66.135  42.544  -0.505  1.00 25.04 ? 26  ASN A N   1 
ATOM   190   C  CA  . ASN A  1 53  ? 67.396  42.036  0.023   1.00 25.44 ? 26  ASN A CA  1 
ATOM   191   C  C   . ASN A  1 53  ? 67.821  40.733  -0.638  1.00 31.32 ? 26  ASN A C   1 
ATOM   192   O  O   . ASN A  1 53  ? 68.700  40.043  -0.110  1.00 28.26 ? 26  ASN A O   1 
ATOM   193   C  CB  . ASN A  1 53  ? 67.314  41.842  1.541   1.00 26.20 ? 26  ASN A CB  1 
ATOM   194   C  CG  . ASN A  1 53  ? 66.294  40.809  1.930   1.00 26.73 ? 26  ASN A CG  1 
ATOM   195   O  OD1 . ASN A  1 53  ? 65.289  40.633  1.239   1.00 28.94 ? 26  ASN A OD1 1 
ATOM   196   N  ND2 . ASN A  1 53  ? 66.543  40.105  3.046   1.00 30.35 ? 26  ASN A ND2 1 
ATOM   197   N  N   . GLY A  1 54  ? 67.230  40.396  -1.788  1.00 27.08 ? 27  GLY A N   1 
ATOM   198   C  CA  . GLY A  1 54  ? 67.610  39.224  -2.543  1.00 28.68 ? 27  GLY A CA  1 
ATOM   199   C  C   . GLY A  1 54  ? 68.264  39.575  -3.872  1.00 28.32 ? 27  GLY A C   1 
ATOM   200   O  O   . GLY A  1 54  ? 68.496  40.745  -4.205  1.00 23.15 ? 27  GLY A O   1 
ATOM   201   N  N   . PRO A  1 55  ? 68.581  38.561  -4.661  1.00 29.08 ? 28  PRO A N   1 
ATOM   202   C  CA  . PRO A  1 55  ? 69.345  38.806  -5.889  1.00 27.13 ? 28  PRO A CA  1 
ATOM   203   C  C   . PRO A  1 55  ? 68.502  39.456  -6.976  1.00 23.53 ? 28  PRO A C   1 
ATOM   204   O  O   . PRO A  1 55  ? 67.269  39.454  -6.934  1.00 23.41 ? 28  PRO A O   1 
ATOM   205   C  CB  . PRO A  1 55  ? 69.802  37.403  -6.305  1.00 29.47 ? 28  PRO A CB  1 
ATOM   206   C  CG  . PRO A  1 55  ? 68.780  36.489  -5.725  1.00 32.96 ? 28  PRO A CG  1 
ATOM   207   C  CD  . PRO A  1 55  ? 68.348  37.125  -4.422  1.00 28.06 ? 28  PRO A CD  1 
ATOM   208   N  N   . VAL A  1 56  ? 69.204  39.998  -7.979  1.00 21.56 ? 29  VAL A N   1 
ATOM   209   C  CA  . VAL A  1 56  ? 68.605  40.596  -9.168  1.00 20.63 ? 29  VAL A CA  1 
ATOM   210   C  C   . VAL A  1 56  ? 68.798  39.641  -10.338 1.00 24.76 ? 29  VAL A C   1 
ATOM   211   O  O   . VAL A  1 56  ? 69.933  39.262  -10.646 1.00 23.17 ? 29  VAL A O   1 
ATOM   212   C  CB  . VAL A  1 56  ? 69.251  41.953  -9.510  1.00 18.47 ? 29  VAL A CB  1 
ATOM   213   C  CG1 . VAL A  1 56  ? 68.601  42.547  -10.783 1.00 18.90 ? 29  VAL A CG1 1 
ATOM   214   C  CG2 . VAL A  1 56  ? 69.162  42.913  -8.326  1.00 18.88 ? 29  VAL A CG2 1 
ATOM   215   N  N   . LYS A  1 57  ? 67.704  39.286  -11.007 1.00 21.33 ? 30  LYS A N   1 
ATOM   216   C  CA  . LYS A  1 57  ? 67.757  38.535  -12.254 1.00 21.74 ? 30  LYS A CA  1 
ATOM   217   C  C   . LYS A  1 57  ? 67.877  39.482  -13.440 1.00 23.37 ? 30  LYS A C   1 
ATOM   218   O  O   . LYS A  1 57  ? 67.132  40.465  -13.540 1.00 21.51 ? 30  LYS A O   1 
ATOM   219   C  CB  . LYS A  1 57  ? 66.520  37.656  -12.411 1.00 21.49 ? 30  LYS A CB  1 
ATOM   220   C  CG  . LYS A  1 57  ? 66.404  36.562  -11.367 1.00 40.32 ? 30  LYS A CG  1 
ATOM   221   C  CD  . LYS A  1 57  ? 65.441  35.455  -11.811 1.00 47.49 ? 30  LYS A CD  1 
ATOM   222   C  CE  . LYS A  1 57  ? 64.612  34.892  -10.651 1.00 48.91 ? 30  LYS A CE  1 
ATOM   223   N  NZ  . LYS A  1 57  ? 63.138  35.209  -10.765 1.00 56.57 ? 30  LYS A NZ  1 
ATOM   224   N  N   . VAL A  1 58  ? 68.801  39.174  -14.356 1.00 20.48 ? 31  VAL A N   1 
ATOM   225   C  CA  . VAL A  1 58  ? 69.110  40.032  -15.499 1.00 17.79 ? 31  VAL A CA  1 
ATOM   226   C  C   . VAL A  1 58  ? 68.999  39.168  -16.746 1.00 20.93 ? 31  VAL A C   1 
ATOM   227   O  O   . VAL A  1 58  ? 69.726  38.177  -16.872 1.00 22.64 ? 31  VAL A O   1 
ATOM   228   C  CB  . VAL A  1 58  ? 70.525  40.634  -15.401 1.00 19.91 ? 31  VAL A CB  1 
ATOM   229   C  CG1 . VAL A  1 58  ? 70.782  41.623  -16.535 1.00 15.94 ? 31  VAL A CG1 1 
ATOM   230   C  CG2 . VAL A  1 58  ? 70.753  41.292  -14.041 1.00 21.13 ? 31  VAL A CG2 1 
ATOM   231   N  N   . TRP A  1 59  ? 68.092  39.514  -17.652 1.00 18.47 ? 32  TRP A N   1 
ATOM   232   C  CA  . TRP A  1 59  ? 67.946  38.671  -18.838 1.00 22.11 ? 32  TRP A CA  1 
ATOM   233   C  C   . TRP A  1 59  ? 67.477  39.486  -20.029 1.00 23.25 ? 32  TRP A C   1 
ATOM   234   O  O   . TRP A  1 59  ? 66.829  40.528  -19.893 1.00 20.63 ? 32  TRP A O   1 
ATOM   235   C  CB  . TRP A  1 59  ? 66.980  37.498  -18.587 1.00 22.02 ? 32  TRP A CB  1 
ATOM   236   C  CG  . TRP A  1 59  ? 65.541  37.879  -18.632 1.00 25.52 ? 32  TRP A CG  1 
ATOM   237   C  CD1 . TRP A  1 59  ? 64.670  37.726  -19.684 1.00 27.58 ? 32  TRP A CD1 1 
ATOM   238   C  CD2 . TRP A  1 59  ? 64.800  38.490  -17.577 1.00 25.46 ? 32  TRP A CD2 1 
ATOM   239   N  NE1 . TRP A  1 59  ? 63.432  38.220  -19.338 1.00 28.05 ? 32  TRP A NE1 1 
ATOM   240   C  CE2 . TRP A  1 59  ? 63.487  38.683  -18.044 1.00 26.14 ? 32  TRP A CE2 1 
ATOM   241   C  CE3 . TRP A  1 59  ? 65.127  38.901  -16.283 1.00 24.01 ? 32  TRP A CE3 1 
ATOM   242   C  CZ2 . TRP A  1 59  ? 62.496  39.264  -17.259 1.00 30.56 ? 32  TRP A CZ2 1 
ATOM   243   C  CZ3 . TRP A  1 59  ? 64.143  39.482  -15.500 1.00 28.93 ? 32  TRP A CZ3 1 
ATOM   244   C  CH2 . TRP A  1 59  ? 62.841  39.654  -15.989 1.00 34.58 ? 32  TRP A CH2 1 
ATOM   245   N  N   . GLY A  1 60  ? 67.793  38.982  -21.213 1.00 22.20 ? 33  GLY A N   1 
ATOM   246   C  CA  . GLY A  1 60  ? 67.311  39.614  -22.420 1.00 21.17 ? 33  GLY A CA  1 
ATOM   247   C  C   . GLY A  1 60  ? 68.166  39.186  -23.599 1.00 23.68 ? 33  GLY A C   1 
ATOM   248   O  O   . GLY A  1 60  ? 68.860  38.184  -23.547 1.00 25.43 ? 33  GLY A O   1 
ATOM   249   N  N   . SER A  1 61  ? 68.114  39.984  -24.639 1.00 23.44 ? 34  SER A N   1 
ATOM   250   C  CA  . SER A  1 61  ? 68.782  39.608  -25.868 1.00 25.99 ? 34  SER A CA  1 
ATOM   251   C  C   . SER A  1 61  ? 69.502  40.820  -26.426 1.00 24.90 ? 34  SER A C   1 
ATOM   252   O  O   . SER A  1 61  ? 68.942  41.915  -26.446 1.00 24.14 ? 34  SER A O   1 
ATOM   253   C  CB  . SER A  1 61  ? 67.775  39.062  -26.878 1.00 30.33 ? 34  SER A CB  1 
ATOM   254   O  OG  . SER A  1 61  ? 68.472  38.582  -28.002 1.00 40.90 ? 34  SER A OG  1 
ATOM   255   N  N   . ILE A  1 62  ? 70.750  40.630  -26.840 1.00 20.09 ? 35  ILE A N   1 
ATOM   256   C  CA  . ILE A  1 62  ? 71.531  41.660  -27.512 1.00 20.72 ? 35  ILE A CA  1 
ATOM   257   C  C   . ILE A  1 62  ? 71.947  41.100  -28.864 1.00 24.99 ? 35  ILE A C   1 
ATOM   258   O  O   . ILE A  1 62  ? 72.514  40.007  -28.928 1.00 24.51 ? 35  ILE A O   1 
ATOM   259   C  CB  . ILE A  1 62  ? 72.776  42.056  -26.706 1.00 19.78 ? 35  ILE A CB  1 
ATOM   260   C  CG1 . ILE A  1 62  ? 72.429  42.354  -25.240 1.00 22.64 ? 35  ILE A CG1 1 
ATOM   261   C  CG2 . ILE A  1 62  ? 73.492  43.223  -27.355 1.00 20.60 ? 35  ILE A CG2 1 
ATOM   262   C  CD1 . ILE A  1 62  ? 73.693  42.606  -24.399 1.00 20.78 ? 35  ILE A CD1 1 
ATOM   263   N  N   . LYS A  1 63  ? 71.698  41.847  -29.928 1.00 22.57 ? 36  LYS A N   1 
ATOM   264   C  CA  . LYS A  1 63  ? 72.072  41.369  -31.259 1.00 24.94 ? 36  LYS A CA  1 
ATOM   265   C  C   . LYS A  1 63  ? 73.128  42.289  -31.875 1.00 27.15 ? 36  LYS A C   1 
ATOM   266   O  O   . LYS A  1 63  ? 73.449  43.366  -31.349 1.00 22.46 ? 36  LYS A O   1 
ATOM   267   C  CB  . LYS A  1 63  ? 70.835  41.248  -32.165 1.00 27.11 ? 36  LYS A CB  1 
ATOM   268   C  CG  . LYS A  1 63  ? 70.204  42.567  -32.547 1.00 32.22 ? 36  LYS A CG  1 
ATOM   269   C  CD  . LYS A  1 63  ? 68.777  42.377  -33.039 1.00 41.17 ? 36  LYS A CD  1 
ATOM   270   C  CE  . LYS A  1 63  ? 68.305  43.584  -33.847 1.00 43.67 ? 36  LYS A CE  1 
ATOM   271   N  NZ  . LYS A  1 63  ? 67.640  43.187  -35.136 1.00 49.52 ? 36  LYS A NZ  1 
ATOM   272   N  N   . GLY A  1 64  ? 73.714  41.834  -32.987 1.00 23.11 ? 37  GLY A N   1 
ATOM   273   C  CA  . GLY A  1 64  ? 74.720  42.624  -33.663 1.00 21.06 ? 37  GLY A CA  1 
ATOM   274   C  C   . GLY A  1 64  ? 76.117  42.503  -33.109 1.00 20.02 ? 37  GLY A C   1 
ATOM   275   O  O   . GLY A  1 64  ? 76.974  43.348  -33.419 1.00 23.28 ? 37  GLY A O   1 
ATOM   276   N  N   . LEU A  1 65  ? 76.390  41.478  -32.300 1.00 20.09 ? 38  LEU A N   1 
ATOM   277   C  CA  . LEU A  1 65  ? 77.695  41.303  -31.673 1.00 21.09 ? 38  LEU A CA  1 
ATOM   278   C  C   . LEU A  1 65  ? 78.552  40.305  -32.446 1.00 25.96 ? 38  LEU A C   1 
ATOM   279   O  O   . LEU A  1 65  ? 78.036  39.360  -33.040 1.00 24.71 ? 38  LEU A O   1 
ATOM   280   C  CB  . LEU A  1 65  ? 77.536  40.782  -30.245 1.00 21.87 ? 38  LEU A CB  1 
ATOM   281   C  CG  . LEU A  1 65  ? 76.867  41.726  -29.240 1.00 25.43 ? 38  LEU A CG  1 
ATOM   282   C  CD1 . LEU A  1 65  ? 76.443  40.943  -28.005 1.00 23.02 ? 38  LEU A CD1 1 
ATOM   283   C  CD2 . LEU A  1 65  ? 77.857  42.807  -28.888 1.00 24.00 ? 38  LEU A CD2 1 
ATOM   284   N  N   . THR A  1 66  ? 79.867  40.484  -32.382 1.00 24.75 ? 39  THR A N   1 
ATOM   285   C  CA  . THR A  1 66  ? 80.760  39.426  -32.838 1.00 31.81 ? 39  THR A CA  1 
ATOM   286   C  C   . THR A  1 66  ? 80.691  38.229  -31.893 1.00 33.05 ? 39  THR A C   1 
ATOM   287   O  O   . THR A  1 66  ? 80.529  38.375  -30.674 1.00 26.72 ? 39  THR A O   1 
ATOM   288   C  CB  . THR A  1 66  ? 82.200  39.926  -32.944 1.00 32.88 ? 39  THR A CB  1 
ATOM   289   O  OG1 . THR A  1 66  ? 82.669  40.307  -31.646 1.00 34.81 ? 39  THR A OG1 1 
ATOM   290   C  CG2 . THR A  1 66  ? 82.285  41.114  -33.896 1.00 28.37 ? 39  THR A CG2 1 
ATOM   291   N  N   . GLU A  1 67  ? 80.811  37.035  -32.472 1.00 27.26 ? 40  GLU A N   1 
ATOM   292   C  CA  . GLU A  1 67  ? 80.707  35.795  -31.712 1.00 28.98 ? 40  GLU A CA  1 
ATOM   293   C  C   . GLU A  1 67  ? 81.769  35.742  -30.622 1.00 27.73 ? 40  GLU A C   1 
ATOM   294   O  O   . GLU A  1 67  ? 82.926  36.102  -30.847 1.00 32.83 ? 40  GLU A O   1 
ATOM   295   C  CB  . GLU A  1 67  ? 80.868  34.600  -32.664 1.00 31.18 ? 40  GLU A CB  1 
ATOM   296   C  CG  . GLU A  1 67  ? 80.768  33.242  -32.011 1.00 33.07 ? 40  GLU A CG  1 
ATOM   297   C  CD  . GLU A  1 67  ? 81.012  32.099  -33.001 1.00 47.95 ? 40  GLU A CD  1 
ATOM   298   O  OE1 . GLU A  1 67  ? 80.847  30.925  -32.610 1.00 52.50 ? 40  GLU A OE1 1 
ATOM   299   O  OE2 . GLU A  1 67  ? 81.396  32.378  -34.160 1.00 42.24 ? 40  GLU A OE2 1 
ATOM   300   N  N   . GLY A  1 68  ? 81.374  35.293  -29.431 1.00 26.31 ? 41  GLY A N   1 
ATOM   301   C  CA  . GLY A  1 68  ? 82.303  35.227  -28.318 1.00 29.17 ? 41  GLY A CA  1 
ATOM   302   C  C   . GLY A  1 68  ? 81.920  36.104  -27.137 1.00 28.09 ? 41  GLY A C   1 
ATOM   303   O  O   . GLY A  1 68  ? 80.771  36.547  -27.031 1.00 26.65 ? 41  GLY A O   1 
ATOM   304   N  N   . LEU A  1 69  ? 82.880  36.366  -26.257 1.00 27.91 ? 42  LEU A N   1 
ATOM   305   C  CA  . LEU A  1 69  ? 82.630  37.038  -24.986 1.00 26.53 ? 42  LEU A CA  1 
ATOM   306   C  C   . LEU A  1 69  ? 82.699  38.557  -25.122 1.00 26.52 ? 42  LEU A C   1 
ATOM   307   O  O   . LEU A  1 69  ? 83.542  39.095  -25.838 1.00 26.65 ? 42  LEU A O   1 
ATOM   308   C  CB  . LEU A  1 69  ? 83.644  36.579  -23.935 1.00 26.18 ? 42  LEU A CB  1 
ATOM   309   C  CG  . LEU A  1 69  ? 83.799  35.087  -23.646 1.00 36.53 ? 42  LEU A CG  1 
ATOM   310   C  CD1 . LEU A  1 69  ? 84.985  34.876  -22.729 1.00 35.67 ? 42  LEU A CD1 1 
ATOM   311   C  CD2 . LEU A  1 69  ? 82.562  34.580  -22.969 1.00 34.25 ? 42  LEU A CD2 1 
ATOM   312   N  N   . HIS A  1 70  ? 81.827  39.250  -24.393 1.00 24.26 ? 43  HIS A N   1 
ATOM   313   C  CA  . HIS A  1 70  ? 81.799  40.708  -24.370 1.00 20.60 ? 43  HIS A CA  1 
ATOM   314   C  C   . HIS A  1 70  ? 81.584  41.152  -22.927 1.00 21.20 ? 43  HIS A C   1 
ATOM   315   O  O   . HIS A  1 70  ? 80.725  40.598  -22.239 1.00 22.50 ? 43  HIS A O   1 
ATOM   316   C  CB  . HIS A  1 70  ? 80.686  41.256  -25.284 1.00 21.07 ? 43  HIS A CB  1 
ATOM   317   C  CG  . HIS A  1 70  ? 80.895  40.942  -26.734 1.00 22.46 ? 43  HIS A CG  1 
ATOM   318   N  ND1 . HIS A  1 70  ? 81.563  41.796  -27.585 1.00 24.31 ? 43  HIS A ND1 1 
ATOM   319   C  CD2 . HIS A  1 70  ? 80.549  39.862  -27.477 1.00 23.06 ? 43  HIS A CD2 1 
ATOM   320   C  CE1 . HIS A  1 70  ? 81.614  41.260  -28.794 1.00 26.87 ? 43  HIS A CE1 1 
ATOM   321   N  NE2 . HIS A  1 70  ? 81.007  40.086  -28.754 1.00 24.50 ? 43  HIS A NE2 1 
ATOM   322   N  N   . GLY A  1 71  ? 82.397  42.101  -22.466 1.00 21.37 ? 44  GLY A N   1 
ATOM   323   C  CA  . GLY A  1 71  ? 82.215  42.634  -21.127 1.00 21.49 ? 44  GLY A CA  1 
ATOM   324   C  C   . GLY A  1 71  ? 80.851  43.281  -20.983 1.00 19.24 ? 44  GLY A C   1 
ATOM   325   O  O   . GLY A  1 71  ? 80.297  43.825  -21.934 1.00 20.18 ? 44  GLY A O   1 
ATOM   326   N  N   . PHE A  1 72  ? 80.294  43.190  -19.778 1.00 19.83 ? 45  PHE A N   1 
ATOM   327   C  CA  . PHE A  1 72  ? 78.890  43.545  -19.540 1.00 17.24 ? 45  PHE A CA  1 
ATOM   328   C  C   . PHE A  1 72  ? 78.862  44.219  -18.176 1.00 19.08 ? 45  PHE A C   1 
ATOM   329   O  O   . PHE A  1 72  ? 78.984  43.530  -17.162 1.00 23.26 ? 45  PHE A O   1 
ATOM   330   C  CB  . PHE A  1 72  ? 78.032  42.278  -19.568 1.00 21.01 ? 45  PHE A CB  1 
ATOM   331   C  CG  . PHE A  1 72  ? 76.540  42.503  -19.569 1.00 19.85 ? 45  PHE A CG  1 
ATOM   332   C  CD1 . PHE A  1 72  ? 75.893  43.121  -20.634 1.00 23.96 ? 45  PHE A CD1 1 
ATOM   333   C  CD2 . PHE A  1 72  ? 75.777  42.040  -18.499 1.00 19.89 ? 45  PHE A CD2 1 
ATOM   334   C  CE1 . PHE A  1 72  ? 74.516  43.276  -20.632 1.00 21.14 ? 45  PHE A CE1 1 
ATOM   335   C  CE2 . PHE A  1 72  ? 74.398  42.188  -18.490 1.00 23.62 ? 45  PHE A CE2 1 
ATOM   336   C  CZ  . PHE A  1 72  ? 73.769  42.804  -19.545 1.00 19.96 ? 45  PHE A CZ  1 
ATOM   337   N  N   . HIS A  1 73  ? 78.764  45.554  -18.141 1.00 20.03 ? 46  HIS A N   1 
ATOM   338   C  CA  . HIS A  1 73  ? 79.002  46.262  -16.884 1.00 22.35 ? 46  HIS A CA  1 
ATOM   339   C  C   . HIS A  1 73  ? 78.007  47.396  -16.670 1.00 20.23 ? 46  HIS A C   1 
ATOM   340   O  O   . HIS A  1 73  ? 77.566  48.049  -17.621 1.00 17.94 ? 46  HIS A O   1 
ATOM   341   C  CB  . HIS A  1 73  ? 80.408  46.870  -16.819 1.00 28.24 ? 46  HIS A CB  1 
ATOM   342   C  CG  . HIS A  1 73  ? 81.504  45.915  -17.180 1.00 24.08 ? 46  HIS A CG  1 
ATOM   343   N  ND1 . HIS A  1 73  ? 82.405  46.179  -18.186 1.00 28.96 ? 46  HIS A ND1 1 
ATOM   344   C  CD2 . HIS A  1 73  ? 81.847  44.710  -16.673 1.00 26.08 ? 46  HIS A CD2 1 
ATOM   345   C  CE1 . HIS A  1 73  ? 83.261  45.181  -18.281 1.00 26.54 ? 46  HIS A CE1 1 
ATOM   346   N  NE2 . HIS A  1 73  ? 82.943  44.273  -17.379 1.00 25.94 ? 46  HIS A NE2 1 
ATOM   347   N  N   . VAL A  1 74  ? 77.714  47.678  -15.405 1.00 17.92 ? 47  VAL A N   1 
ATOM   348   C  CA  . VAL A  1 74  ? 76.974  48.887  -15.061 1.00 16.21 ? 47  VAL A CA  1 
ATOM   349   C  C   . VAL A  1 74  ? 78.000  49.968  -14.777 1.00 18.55 ? 47  VAL A C   1 
ATOM   350   O  O   . VAL A  1 74  ? 78.811  49.835  -13.854 1.00 20.32 ? 47  VAL A O   1 
ATOM   351   C  CB  . VAL A  1 74  ? 76.060  48.679  -13.843 1.00 18.28 ? 47  VAL A CB  1 
ATOM   352   C  CG1 . VAL A  1 74  ? 75.255  49.964  -13.563 1.00 13.53 ? 47  VAL A CG1 1 
ATOM   353   C  CG2 . VAL A  1 74  ? 75.126  47.509  -14.057 1.00 20.00 ? 47  VAL A CG2 1 
ATOM   354   N  N   . HIS A  1 75  ? 77.952  51.038  -15.547 1.00 15.99 ? 48  HIS A N   1 
ATOM   355   C  CA  . HIS A  1 75  ? 78.793  52.200  -15.334 1.00 14.47 ? 48  HIS A CA  1 
ATOM   356   C  C   . HIS A  1 75  ? 78.063  53.229  -14.471 1.00 21.94 ? 48  HIS A C   1 
ATOM   357   O  O   . HIS A  1 75  ? 76.838  53.217  -14.357 1.00 22.39 ? 48  HIS A O   1 
ATOM   358   C  CB  . HIS A  1 75  ? 79.189  52.800  -16.677 1.00 17.27 ? 48  HIS A CB  1 
ATOM   359   C  CG  . HIS A  1 75  ? 80.134  51.935  -17.455 1.00 21.85 ? 48  HIS A CG  1 
ATOM   360   N  ND1 . HIS A  1 75  ? 81.396  52.351  -17.818 1.00 23.61 ? 48  HIS A ND1 1 
ATOM   361   C  CD2 . HIS A  1 75  ? 80.008  50.668  -17.919 1.00 20.74 ? 48  HIS A CD2 1 
ATOM   362   C  CE1 . HIS A  1 75  ? 81.999  51.389  -18.500 1.00 26.23 ? 48  HIS A CE1 1 
ATOM   363   N  NE2 . HIS A  1 75  ? 81.181  50.355  -18.573 1.00 22.98 ? 48  HIS A NE2 1 
ATOM   364   N  N   . GLU A  1 76  ? 78.838  54.146  -13.891 1.00 20.47 ? 49  GLU A N   1 
ATOM   365   C  CA  . GLU A  1 76  ? 78.349  54.937  -12.759 1.00 19.59 ? 49  GLU A CA  1 
ATOM   366   C  C   . GLU A  1 76  ? 77.223  55.897  -13.148 1.00 17.49 ? 49  GLU A C   1 
ATOM   367   O  O   . GLU A  1 76  ? 76.250  56.036  -12.400 1.00 21.18 ? 49  GLU A O   1 
ATOM   368   C  CB  . GLU A  1 76  ? 79.497  55.718  -12.126 1.00 21.79 ? 49  GLU A CB  1 
ATOM   369   C  CG  . GLU A  1 76  ? 79.034  56.556  -10.937 1.00 25.55 ? 49  GLU A CG  1 
ATOM   370   C  CD  . GLU A  1 76  ? 80.174  57.119  -10.110 1.00 32.62 ? 49  GLU A CD  1 
ATOM   371   O  OE1 . GLU A  1 76  ? 81.347  56.933  -10.500 1.00 35.39 ? 49  GLU A OE1 1 
ATOM   372   O  OE2 . GLU A  1 76  ? 79.886  57.779  -9.087  1.00 32.87 ? 49  GLU A OE2 1 
ATOM   373   N  N   . PHE A  1 77  ? 77.328  56.576  -14.291 1.00 18.28 ? 50  PHE A N   1 
ATOM   374   C  CA  . PHE A  1 77  ? 76.408  57.667  -14.608 1.00 21.14 ? 50  PHE A CA  1 
ATOM   375   C  C   . PHE A  1 77  ? 75.427  57.279  -15.697 1.00 20.57 ? 50  PHE A C   1 
ATOM   376   O  O   . PHE A  1 77  ? 75.800  56.630  -16.677 1.00 21.06 ? 50  PHE A O   1 
ATOM   377   C  CB  . PHE A  1 77  ? 77.175  58.919  -15.028 1.00 20.42 ? 50  PHE A CB  1 
ATOM   378   C  CG  . PHE A  1 77  ? 78.178  59.342  -14.001 1.00 21.94 ? 50  PHE A CG  1 
ATOM   379   C  CD1 . PHE A  1 77  ? 77.756  59.725  -12.744 1.00 22.89 ? 50  PHE A CD1 1 
ATOM   380   C  CD2 . PHE A  1 77  ? 79.532  59.268  -14.262 1.00 25.20 ? 50  PHE A CD2 1 
ATOM   381   C  CE1 . PHE A  1 77  ? 78.667  60.076  -11.768 1.00 29.97 ? 50  PHE A CE1 1 
ATOM   382   C  CE2 . PHE A  1 77  ? 80.448  59.624  -13.296 1.00 30.64 ? 50  PHE A CE2 1 
ATOM   383   C  CZ  . PHE A  1 77  ? 80.015  60.021  -12.047 1.00 29.60 ? 50  PHE A CZ  1 
ATOM   384   N  N   . GLY A  1 78  ? 74.171  57.702  -15.528 1.00 17.34 ? 51  GLY A N   1 
ATOM   385   C  CA  . GLY A  1 78  ? 73.164  57.480  -16.553 1.00 17.62 ? 51  GLY A CA  1 
ATOM   386   C  C   . GLY A  1 78  ? 73.155  58.652  -17.500 1.00 22.80 ? 51  GLY A C   1 
ATOM   387   O  O   . GLY A  1 78  ? 72.107  59.218  -17.814 1.00 23.13 ? 51  GLY A O   1 
ATOM   388   N  N   . ASP A  1 79  ? 74.341  59.039  -17.945 1.00 23.20 ? 52  ASP A N   1 
ATOM   389   C  CA  . ASP A  1 79  ? 74.548  60.240  -18.746 1.00 18.75 ? 52  ASP A CA  1 
ATOM   390   C  C   . ASP A  1 79  ? 74.960  59.768  -20.133 1.00 23.13 ? 52  ASP A C   1 
ATOM   391   O  O   . ASP A  1 79  ? 76.076  59.264  -20.318 1.00 23.82 ? 52  ASP A O   1 
ATOM   392   C  CB  . ASP A  1 79  ? 75.617  61.124  -18.104 1.00 22.84 ? 52  ASP A CB  1 
ATOM   393   C  CG  . ASP A  1 79  ? 75.910  62.398  -18.900 1.00 22.99 ? 52  ASP A CG  1 
ATOM   394   O  OD1 . ASP A  1 79  ? 75.659  62.441  -20.119 1.00 23.34 ? 52  ASP A OD1 1 
ATOM   395   O  OD2 . ASP A  1 79  ? 76.444  63.360  -18.300 1.00 25.90 ? 52  ASP A OD2 1 
ATOM   396   N  N   A ASN A  1 80  ? 74.043  59.931  -21.095 0.54 21.54 ? 53  ASN A N   1 
ATOM   397   N  N   B ASN A  1 80  ? 74.076  59.911  -21.104 0.46 21.60 ? 53  ASN A N   1 
ATOM   398   C  CA  A ASN A  1 80  ? 74.204  59.555  -22.495 0.54 22.65 ? 53  ASN A CA  1 
ATOM   399   C  CA  B ASN A  1 80  ? 74.426  59.527  -22.459 0.46 22.60 ? 53  ASN A CA  1 
ATOM   400   C  C   A ASN A  1 80  ? 74.505  60.747  -23.401 0.54 20.57 ? 53  ASN A C   1 
ATOM   401   C  C   B ASN A  1 80  ? 74.485  60.740  -23.388 0.46 20.65 ? 53  ASN A C   1 
ATOM   402   O  O   A ASN A  1 80  ? 74.467  60.601  -24.627 0.54 22.74 ? 53  ASN A O   1 
ATOM   403   O  O   B ASN A  1 80  ? 74.276  60.614  -24.597 0.46 22.86 ? 53  ASN A O   1 
ATOM   404   C  CB  A ASN A  1 80  ? 72.933  58.832  -22.988 0.54 25.04 ? 53  ASN A CB  1 
ATOM   405   C  CB  B ASN A  1 80  ? 73.464  58.449  -22.965 0.46 26.89 ? 53  ASN A CB  1 
ATOM   406   C  CG  A ASN A  1 80  ? 73.159  58.022  -24.275 0.54 26.47 ? 53  ASN A CG  1 
ATOM   407   C  CG  B ASN A  1 80  ? 73.599  57.123  -22.189 0.46 24.73 ? 53  ASN A CG  1 
ATOM   408   O  OD1 A ASN A  1 80  ? 72.499  58.249  -25.290 0.54 30.87 ? 53  ASN A OD1 1 
ATOM   409   O  OD1 B ASN A  1 80  ? 74.525  56.937  -21.382 0.46 25.77 ? 53  ASN A OD1 1 
ATOM   410   N  ND2 A ASN A  1 80  ? 74.084  57.077  -24.227 0.54 24.61 ? 53  ASN A ND2 1 
ATOM   411   N  ND2 B ASN A  1 80  ? 72.689  56.189  -22.456 0.46 28.14 ? 53  ASN A ND2 1 
ATOM   412   N  N   . THR A  1 81  ? 74.809  61.918  -22.834 1.00 18.58 ? 54  THR A N   1 
ATOM   413   C  CA  . THR A  1 81  ? 74.982  63.119  -23.660 1.00 19.85 ? 54  THR A CA  1 
ATOM   414   C  C   . THR A  1 81  ? 76.147  63.002  -24.633 1.00 24.15 ? 54  THR A C   1 
ATOM   415   O  O   . THR A  1 81  ? 76.184  63.728  -25.636 1.00 21.76 ? 54  THR A O   1 
ATOM   416   C  CB  . THR A  1 81  ? 75.207  64.367  -22.797 1.00 21.02 ? 54  THR A CB  1 
ATOM   417   O  OG1 . THR A  1 81  ? 76.419  64.231  -22.038 1.00 22.03 ? 54  THR A OG1 1 
ATOM   418   C  CG2 . THR A  1 81  ? 74.027  64.577  -21.836 1.00 21.04 ? 54  THR A CG2 1 
ATOM   419   N  N   . ALA A  1 82  ? 77.103  62.128  -24.346 1.00 24.38 ? 55  ALA A N   1 
ATOM   420   C  CA  . ALA A  1 82  ? 78.230  61.838  -25.227 1.00 25.97 ? 55  ALA A CA  1 
ATOM   421   C  C   . ALA A  1 82  ? 78.181  60.382  -25.676 1.00 29.60 ? 55  ALA A C   1 
ATOM   422   O  O   . ALA A  1 82  ? 79.213  59.723  -25.806 1.00 25.51 ? 55  ALA A O   1 
ATOM   423   C  CB  . ALA A  1 82  ? 79.558  62.127  -24.524 1.00 22.26 ? 55  ALA A CB  1 
ATOM   424   N  N   . GLY A  1 83  ? 76.977  59.854  -25.891 1.00 24.53 ? 56  GLY A N   1 
ATOM   425   C  CA  . GLY A  1 83  ? 76.874  58.417  -26.105 1.00 24.28 ? 56  GLY A CA  1 
ATOM   426   C  C   . GLY A  1 83  ? 77.351  57.659  -24.880 1.00 25.69 ? 56  GLY A C   1 
ATOM   427   O  O   . GLY A  1 83  ? 77.223  58.119  -23.744 1.00 22.54 ? 56  GLY A O   1 
ATOM   428   N  N   . CYS A  1 84  ? 77.947  56.485  -25.107 1.00 24.12 ? 57  CYS A N   1 
ATOM   429   C  CA  . CYS A  1 84  ? 78.354  55.659  -23.970 1.00 22.78 ? 57  CYS A CA  1 
ATOM   430   C  C   . CYS A  1 84  ? 79.542  56.244  -23.209 1.00 22.37 ? 57  CYS A C   1 
ATOM   431   O  O   . CYS A  1 84  ? 79.780  55.867  -22.058 1.00 22.71 ? 57  CYS A O   1 
ATOM   432   C  CB  . CYS A  1 84  ? 78.665  54.245  -24.457 1.00 33.14 ? 57  CYS A CB  1 
ATOM   433   S  SG  . CYS A  1 84  ? 77.236  53.506  -25.310 1.00 34.34 ? 57  CYS A SG  1 
ATOM   434   N  N   . THR A  1 85  ? 80.265  57.177  -23.817 1.00 22.18 ? 58  THR A N   1 
ATOM   435   C  CA  . THR A  1 85  ? 81.472  57.717  -23.197 1.00 25.55 ? 58  THR A CA  1 
ATOM   436   C  C   . THR A  1 85  ? 81.157  58.455  -21.902 1.00 23.68 ? 58  THR A C   1 
ATOM   437   O  O   . THR A  1 85  ? 81.907  58.366  -20.923 1.00 25.21 ? 58  THR A O   1 
ATOM   438   C  CB  . THR A  1 85  ? 82.160  58.658  -24.187 1.00 30.73 ? 58  THR A CB  1 
ATOM   439   O  OG1 . THR A  1 85  ? 82.340  57.974  -25.437 1.00 37.33 ? 58  THR A OG1 1 
ATOM   440   C  CG2 . THR A  1 85  ? 83.497  59.132  -23.645 1.00 34.26 ? 58  THR A CG2 1 
ATOM   441   N  N   . SER A  1 86  ? 80.048  59.205  -21.879 1.00 22.21 ? 59  SER A N   1 
ATOM   442   C  CA  . SER A  1 86  ? 79.745  60.030  -20.718 1.00 21.67 ? 59  SER A CA  1 
ATOM   443   C  C   . SER A  1 86  ? 79.236  59.237  -19.528 1.00 20.24 ? 59  SER A C   1 
ATOM   444   O  O   . SER A  1 86  ? 79.021  59.834  -18.469 1.00 21.76 ? 59  SER A O   1 
ATOM   445   C  CB  . SER A  1 86  ? 78.735  61.110  -21.116 1.00 22.16 ? 59  SER A CB  1 
ATOM   446   O  OG  . SER A  1 86  ? 77.761  60.622  -22.024 1.00 22.56 ? 59  SER A OG  1 
ATOM   447   N  N   . ALA A  1 87  ? 79.040  57.917  -19.650 1.00 20.57 ? 60  ALA A N   1 
ATOM   448   C  CA  . ALA A  1 87  ? 78.638  57.103  -18.509 1.00 13.42 ? 60  ALA A CA  1 
ATOM   449   C  C   . ALA A  1 87  ? 79.731  56.955  -17.466 1.00 22.23 ? 60  ALA A C   1 
ATOM   450   O  O   . ALA A  1 87  ? 79.434  56.535  -16.351 1.00 21.50 ? 60  ALA A O   1 
ATOM   451   C  CB  . ALA A  1 87  ? 78.191  55.709  -18.969 1.00 19.33 ? 60  ALA A CB  1 
ATOM   452   N  N   . GLY A  1 88  ? 80.978  57.300  -17.777 1.00 22.93 ? 61  GLY A N   1 
ATOM   453   C  CA  . GLY A  1 88  ? 82.042  57.239  -16.801 1.00 22.24 ? 61  GLY A CA  1 
ATOM   454   C  C   . GLY A  1 88  ? 82.521  55.821  -16.547 1.00 18.66 ? 61  GLY A C   1 
ATOM   455   O  O   . GLY A  1 88  ? 82.303  54.918  -17.360 1.00 23.44 ? 61  GLY A O   1 
ATOM   456   N  N   . PRO A  1 89  ? 83.159  55.592  -15.408 1.00 21.21 ? 62  PRO A N   1 
ATOM   457   C  CA  . PRO A  1 89  ? 83.760  54.284  -15.125 1.00 23.75 ? 62  PRO A CA  1 
ATOM   458   C  C   . PRO A  1 89  ? 82.708  53.317  -14.601 1.00 27.06 ? 62  PRO A C   1 
ATOM   459   O  O   . PRO A  1 89  ? 81.538  53.663  -14.448 1.00 23.60 ? 62  PRO A O   1 
ATOM   460   C  CB  . PRO A  1 89  ? 84.793  54.613  -14.049 1.00 26.03 ? 62  PRO A CB  1 
ATOM   461   C  CG  . PRO A  1 89  ? 84.154  55.755  -13.291 1.00 27.57 ? 62  PRO A CG  1 
ATOM   462   C  CD  . PRO A  1 89  ? 83.402  56.559  -14.317 1.00 24.69 ? 62  PRO A CD  1 
ATOM   463   N  N   . HIS A  1 90  ? 83.146  52.091  -14.331 1.00 22.63 ? 63  HIS A N   1 
ATOM   464   C  CA  . HIS A  1 90  ? 82.273  51.112  -13.698 1.00 24.07 ? 63  HIS A CA  1 
ATOM   465   C  C   . HIS A  1 90  ? 81.737  51.671  -12.382 1.00 25.68 ? 63  HIS A C   1 
ATOM   466   O  O   . HIS A  1 90  ? 82.434  52.392  -11.668 1.00 23.47 ? 63  HIS A O   1 
ATOM   467   C  CB  . HIS A  1 90  ? 83.030  49.800  -13.447 1.00 24.77 ? 63  HIS A CB  1 
ATOM   468   C  CG  . HIS A  1 90  ? 83.468  49.112  -14.703 1.00 23.62 ? 63  HIS A CG  1 
ATOM   469   N  ND1 . HIS A  1 90  ? 84.125  47.902  -14.702 1.00 32.44 ? 63  HIS A ND1 1 
ATOM   470   C  CD2 . HIS A  1 90  ? 83.324  49.460  -16.003 1.00 24.80 ? 63  HIS A CD2 1 
ATOM   471   C  CE1 . HIS A  1 90  ? 84.372  47.536  -15.946 1.00 26.75 ? 63  HIS A CE1 1 
ATOM   472   N  NE2 . HIS A  1 90  ? 83.895  48.463  -16.756 1.00 28.69 ? 63  HIS A NE2 1 
ATOM   473   N  N   . PHE A  1 91  ? 80.472  51.369  -12.088 1.00 22.07 ? 64  PHE A N   1 
ATOM   474   C  CA  . PHE A  1 91  ? 79.860  51.768  -10.823 1.00 19.96 ? 64  PHE A CA  1 
ATOM   475   C  C   . PHE A  1 91  ? 80.590  51.077  -9.679  1.00 24.25 ? 64  PHE A C   1 
ATOM   476   O  O   . PHE A  1 91  ? 80.589  49.844  -9.584  1.00 22.83 ? 64  PHE A O   1 
ATOM   477   C  CB  . PHE A  1 91  ? 78.368  51.391  -10.854 1.00 20.21 ? 64  PHE A CB  1 
ATOM   478   C  CG  . PHE A  1 91  ? 77.592  51.728  -9.595  1.00 22.17 ? 64  PHE A CG  1 
ATOM   479   C  CD1 . PHE A  1 91  ? 77.786  52.915  -8.902  1.00 23.39 ? 64  PHE A CD1 1 
ATOM   480   C  CD2 . PHE A  1 91  ? 76.655  50.826  -9.116  1.00 21.63 ? 64  PHE A CD2 1 
ATOM   481   C  CE1 . PHE A  1 91  ? 77.038  53.191  -7.746  1.00 21.95 ? 64  PHE A CE1 1 
ATOM   482   C  CE2 . PHE A  1 91  ? 75.912  51.088  -7.961  1.00 24.99 ? 64  PHE A CE2 1 
ATOM   483   C  CZ  . PHE A  1 91  ? 76.108  52.265  -7.286  1.00 22.90 ? 64  PHE A CZ  1 
ATOM   484   N  N   . ASN A  1 92  ? 81.205  51.867  -8.797  1.00 23.26 ? 65  ASN A N   1 
ATOM   485   C  CA  . ASN A  1 92  ? 82.162  51.354  -7.814  1.00 24.54 ? 65  ASN A CA  1 
ATOM   486   C  C   . ASN A  1 92  ? 82.060  52.161  -6.519  1.00 26.74 ? 65  ASN A C   1 
ATOM   487   O  O   . ASN A  1 92  ? 83.013  52.823  -6.099  1.00 33.77 ? 65  ASN A O   1 
ATOM   488   C  CB  . ASN A  1 92  ? 83.577  51.398  -8.393  1.00 23.28 ? 65  ASN A CB  1 
ATOM   489   C  CG  . ASN A  1 92  ? 84.624  50.738  -7.482  1.00 25.55 ? 65  ASN A CG  1 
ATOM   490   O  OD1 . ASN A  1 92  ? 84.318  49.856  -6.681  1.00 25.62 ? 65  ASN A OD1 1 
ATOM   491   N  ND2 . ASN A  1 92  ? 85.868  51.155  -7.638  1.00 28.36 ? 65  ASN A ND2 1 
ATOM   492   N  N   . PRO A  1 93  ? 80.903  52.122  -5.854  1.00 26.44 ? 66  PRO A N   1 
ATOM   493   C  CA  . PRO A  1 93  ? 80.741  52.933  -4.637  1.00 27.78 ? 66  PRO A CA  1 
ATOM   494   C  C   . PRO A  1 93  ? 81.637  52.484  -3.499  1.00 37.14 ? 66  PRO A C   1 
ATOM   495   O  O   . PRO A  1 93  ? 81.966  53.308  -2.640  1.00 38.91 ? 66  PRO A O   1 
ATOM   496   C  CB  . PRO A  1 93  ? 79.265  52.743  -4.285  1.00 25.55 ? 66  PRO A CB  1 
ATOM   497   C  CG  . PRO A  1 93  ? 78.952  51.365  -4.796  1.00 27.49 ? 66  PRO A CG  1 
ATOM   498   C  CD  . PRO A  1 93  ? 79.747  51.236  -6.076  1.00 24.79 ? 66  PRO A CD  1 
ATOM   499   N  N   . LEU A  1 94  ? 82.047  51.215  -3.464  1.00 31.57 ? 67  LEU A N   1 
ATOM   500   C  CA  . LEU A  1 94  ? 82.916  50.730  -2.395  1.00 36.28 ? 67  LEU A CA  1 
ATOM   501   C  C   . LEU A  1 94  ? 84.397  50.879  -2.717  1.00 35.71 ? 67  LEU A C   1 
ATOM   502   O  O   . LEU A  1 94  ? 85.232  50.430  -1.924  1.00 38.79 ? 67  LEU A O   1 
ATOM   503   C  CB  . LEU A  1 94  ? 82.597  49.272  -2.067  1.00 31.93 ? 67  LEU A CB  1 
ATOM   504   C  CG  . LEU A  1 94  ? 81.141  48.955  -1.711  1.00 34.25 ? 67  LEU A CG  1 
ATOM   505   C  CD1 . LEU A  1 94  ? 80.984  47.502  -1.285  1.00 36.74 ? 67  LEU A CD1 1 
ATOM   506   C  CD2 . LEU A  1 94  ? 80.647  49.886  -0.613  1.00 39.12 ? 67  LEU A CD2 1 
ATOM   507   N  N   . SER A  1 95  ? 84.735  51.497  -3.849  1.00 33.96 ? 68  SER A N   1 
ATOM   508   C  CA  . SER A  1 95  ? 86.116  51.814  -4.213  1.00 35.18 ? 68  SER A CA  1 
ATOM   509   C  C   . SER A  1 95  ? 87.002  50.570  -4.188  1.00 41.37 ? 68  SER A C   1 
ATOM   510   O  O   . SER A  1 95  ? 88.073  50.552  -3.581  1.00 37.03 ? 68  SER A O   1 
ATOM   511   C  CB  . SER A  1 95  ? 86.681  52.905  -3.294  1.00 34.73 ? 68  SER A CB  1 
ATOM   512   O  OG  . SER A  1 95  ? 86.138  54.169  -3.629  1.00 44.33 ? 68  SER A OG  1 
ATOM   513   N  N   . ARG A  1 96  ? 86.547  49.516  -4.860  1.00 36.54 ? 69  ARG A N   1 
ATOM   514   C  CA  . ARG A  1 96  ? 87.307  48.278  -4.945  1.00 33.36 ? 69  ARG A CA  1 
ATOM   515   C  C   . ARG A  1 96  ? 87.965  48.148  -6.315  1.00 34.80 ? 69  ARG A C   1 
ATOM   516   O  O   . ARG A  1 96  ? 87.777  48.971  -7.216  1.00 33.77 ? 69  ARG A O   1 
ATOM   517   C  CB  . ARG A  1 96  ? 86.406  47.081  -4.645  1.00 30.74 ? 69  ARG A CB  1 
ATOM   518   C  CG  . ARG A  1 96  ? 85.969  47.036  -3.194  1.00 38.87 ? 69  ARG A CG  1 
ATOM   519   C  CD  . ARG A  1 96  ? 85.180  45.782  -2.877  1.00 40.32 ? 69  ARG A CD  1 
ATOM   520   N  NE  . ARG A  1 96  ? 84.922  45.685  -1.444  1.00 45.57 ? 69  ARG A NE  1 
ATOM   521   C  CZ  . ARG A  1 96  ? 84.107  44.801  -0.884  1.00 50.15 ? 69  ARG A CZ  1 
ATOM   522   N  NH1 . ARG A  1 96  ? 83.471  43.890  -1.605  1.00 52.06 ? 69  ARG A NH1 1 
ATOM   523   N  NH2 . ARG A  1 96  ? 83.917  44.837  0.433   1.00 52.18 ? 69  ARG A NH2 1 
ATOM   524   N  N   . LYS A  1 97  ? 88.763  47.102  -6.472  1.00 35.25 ? 70  LYS A N   1 
ATOM   525   C  CA  . LYS A  1 97  ? 89.341  46.828  -7.776  1.00 34.27 ? 70  LYS A CA  1 
ATOM   526   C  C   . LYS A  1 97  ? 88.368  45.994  -8.605  1.00 27.00 ? 70  LYS A C   1 
ATOM   527   O  O   . LYS A  1 97  ? 87.453  45.359  -8.074  1.00 29.12 ? 70  LYS A O   1 
ATOM   528   C  CB  . LYS A  1 97  ? 90.691  46.126  -7.626  1.00 38.48 ? 70  LYS A CB  1 
ATOM   529   C  CG  . LYS A  1 97  ? 91.846  47.117  -7.638  1.00 43.03 ? 70  LYS A CG  1 
ATOM   530   C  CD  . LYS A  1 97  ? 93.215  46.443  -7.621  1.00 51.89 ? 70  LYS A CD  1 
ATOM   531   C  CE  . LYS A  1 97  ? 94.289  47.445  -7.162  1.00 54.71 ? 70  LYS A CE  1 
ATOM   532   N  NZ  . LYS A  1 97  ? 94.418  48.625  -8.097  1.00 58.10 ? 70  LYS A NZ  1 
ATOM   533   N  N   . HIS A  1 98  ? 88.568  46.023  -9.921  1.00 30.09 ? 71  HIS A N   1 
ATOM   534   C  CA  . HIS A  1 98  ? 87.709  45.287  -10.834 1.00 30.92 ? 71  HIS A CA  1 
ATOM   535   C  C   . HIS A  1 98  ? 87.917  43.789  -10.650 1.00 34.80 ? 71  HIS A C   1 
ATOM   536   O  O   . HIS A  1 98  ? 89.024  43.319  -10.379 1.00 31.19 ? 71  HIS A O   1 
ATOM   537   C  CB  . HIS A  1 98  ? 87.998  45.695  -12.288 1.00 31.00 ? 71  HIS A CB  1 
ATOM   538   C  CG  . HIS A  1 98  ? 87.271  44.873  -13.312 1.00 34.68 ? 71  HIS A CG  1 
ATOM   539   N  ND1 . HIS A  1 98  ? 85.935  45.054  -13.594 1.00 30.01 ? 71  HIS A ND1 1 
ATOM   540   C  CD2 . HIS A  1 98  ? 87.692  43.863  -14.118 1.00 29.21 ? 71  HIS A CD2 1 
ATOM   541   C  CE1 . HIS A  1 98  ? 85.562  44.191  -14.522 1.00 31.45 ? 71  HIS A CE1 1 
ATOM   542   N  NE2 . HIS A  1 98  ? 86.609  43.458  -14.859 1.00 29.79 ? 71  HIS A NE2 1 
ATOM   543   N  N   . GLY A  1 99  ? 86.836  43.037  -10.799 1.00 30.07 ? 72  GLY A N   1 
ATOM   544   C  CA  . GLY A  1 99  ? 86.899  41.594  -10.715 1.00 27.32 ? 72  GLY A CA  1 
ATOM   545   C  C   . GLY A  1 99  ? 85.755  40.994  -11.494 1.00 29.19 ? 72  GLY A C   1 
ATOM   546   O  O   . GLY A  1 99  ? 85.056  41.710  -12.223 1.00 26.02 ? 72  GLY A O   1 
ATOM   547   N  N   . GLY A  1 100 ? 85.555  39.686  -11.358 1.00 26.80 ? 73  GLY A N   1 
ATOM   548   C  CA  . GLY A  1 100 ? 84.411  39.032  -11.949 1.00 27.83 ? 73  GLY A CA  1 
ATOM   549   C  C   . GLY A  1 100 ? 83.273  39.009  -10.952 1.00 25.69 ? 73  GLY A C   1 
ATOM   550   O  O   . GLY A  1 100 ? 83.470  39.295  -9.769  1.00 28.30 ? 73  GLY A O   1 
ATOM   551   N  N   . PRO A  1 101 ? 82.064  38.658  -11.399 1.00 29.27 ? 74  PRO A N   1 
ATOM   552   C  CA  . PRO A  1 101 ? 80.904  38.742  -10.487 1.00 25.71 ? 74  PRO A CA  1 
ATOM   553   C  C   . PRO A  1 101 ? 81.040  37.883  -9.247  1.00 34.40 ? 74  PRO A C   1 
ATOM   554   O  O   . PRO A  1 101 ? 80.456  38.223  -8.210  1.00 30.27 ? 74  PRO A O   1 
ATOM   555   C  CB  . PRO A  1 101 ? 79.718  38.286  -11.357 1.00 31.14 ? 74  PRO A CB  1 
ATOM   556   C  CG  . PRO A  1 101 ? 80.309  37.763  -12.648 1.00 25.44 ? 74  PRO A CG  1 
ATOM   557   C  CD  . PRO A  1 101 ? 81.666  38.392  -12.792 1.00 24.75 ? 74  PRO A CD  1 
ATOM   558   N  N   . LYS A  1 102 ? 81.782  36.779  -9.302  1.00 34.45 ? 75  LYS A N   1 
ATOM   559   C  CA  . LYS A  1 102 ? 81.874  35.933  -8.119  1.00 31.00 ? 75  LYS A CA  1 
ATOM   560   C  C   . LYS A  1 102 ? 83.019  36.314  -7.190  1.00 32.11 ? 75  LYS A C   1 
ATOM   561   O  O   . LYS A  1 102 ? 83.117  35.747  -6.099  1.00 42.70 ? 75  LYS A O   1 
ATOM   562   C  CB  . LYS A  1 102 ? 81.982  34.466  -8.524  1.00 38.42 ? 75  LYS A CB  1 
ATOM   563   C  CG  . LYS A  1 102 ? 80.903  34.063  -9.511  1.00 41.80 ? 75  LYS A CG  1 
ATOM   564   C  CD  . LYS A  1 102 ? 81.093  32.651  -10.006 1.00 50.81 ? 75  LYS A CD  1 
ATOM   565   C  CE  . LYS A  1 102 ? 81.165  31.691  -8.830  1.00 52.02 ? 75  LYS A CE  1 
ATOM   566   N  NZ  . LYS A  1 102 ? 80.481  30.402  -9.162  1.00 57.56 ? 75  LYS A NZ  1 
ATOM   567   N  N   . ASP A  1 103 ? 83.872  37.261  -7.574  1.00 33.32 ? 76  ASP A N   1 
ATOM   568   C  CA  . ASP A  1 103 ? 84.899  37.732  -6.654  1.00 30.90 ? 76  ASP A CA  1 
ATOM   569   C  C   . ASP A  1 103 ? 84.297  38.582  -5.548  1.00 38.19 ? 76  ASP A C   1 
ATOM   570   O  O   . ASP A  1 103 ? 83.310  39.297  -5.743  1.00 36.79 ? 76  ASP A O   1 
ATOM   571   C  CB  . ASP A  1 103 ? 85.965  38.542  -7.387  1.00 31.66 ? 76  ASP A CB  1 
ATOM   572   C  CG  . ASP A  1 103 ? 86.725  37.718  -8.400  1.00 41.08 ? 76  ASP A CG  1 
ATOM   573   O  OD1 . ASP A  1 103 ? 86.917  36.509  -8.142  1.00 52.87 ? 76  ASP A OD1 1 
ATOM   574   O  OD2 . ASP A  1 103 ? 87.122  38.273  -9.455  1.00 37.01 ? 76  ASP A OD2 1 
ATOM   575   N  N   . GLU A  1 104 ? 84.904  38.497  -4.367  1.00 37.08 ? 77  GLU A N   1 
ATOM   576   C  CA  . GLU A  1 104 ? 84.562  39.450  -3.324  1.00 33.94 ? 77  GLU A CA  1 
ATOM   577   C  C   . GLU A  1 104 ? 85.146  40.817  -3.652  1.00 33.80 ? 77  GLU A C   1 
ATOM   578   O  O   . GLU A  1 104 ? 84.483  41.843  -3.465  1.00 37.83 ? 77  GLU A O   1 
ATOM   579   C  CB  . GLU A  1 104 ? 85.049  38.948  -1.957  1.00 38.77 ? 77  GLU A CB  1 
ATOM   580   C  CG  . GLU A  1 104 ? 85.306  40.058  -0.944  1.00 45.87 ? 77  GLU A CG  1 
ATOM   581   C  CD  . GLU A  1 104 ? 86.784  40.402  -0.818  1.00 67.03 ? 77  GLU A CD  1 
ATOM   582   O  OE1 . GLU A  1 104 ? 87.603  39.473  -0.599  1.00 64.55 ? 77  GLU A OE1 1 
ATOM   583   O  OE2 . GLU A  1 104 ? 87.121  41.608  -0.944  1.00 64.37 ? 77  GLU A OE2 1 
ATOM   584   N  N   . GLU A  1 105 ? 86.363  40.851  -4.192  1.00 36.43 ? 78  GLU A N   1 
ATOM   585   C  CA  . GLU A  1 105 ? 86.951  42.099  -4.667  1.00 32.49 ? 78  GLU A CA  1 
ATOM   586   C  C   . GLU A  1 105 ? 86.439  42.389  -6.075  1.00 34.31 ? 78  GLU A C   1 
ATOM   587   O  O   . GLU A  1 105 ? 86.997  41.909  -7.068  1.00 32.69 ? 78  GLU A O   1 
ATOM   588   C  CB  . GLU A  1 105 ? 88.472  42.032  -4.652  1.00 35.68 ? 78  GLU A CB  1 
ATOM   589   C  CG  . GLU A  1 105 ? 89.124  43.352  -5.052  1.00 37.85 ? 78  GLU A CG  1 
ATOM   590   C  CD  . GLU A  1 105 ? 89.084  44.400  -3.928  1.00 44.82 ? 78  GLU A CD  1 
ATOM   591   O  OE1 . GLU A  1 105 ? 88.529  44.104  -2.843  1.00 50.82 ? 78  GLU A OE1 1 
ATOM   592   O  OE2 . GLU A  1 105 ? 89.585  45.529  -4.148  1.00 45.19 ? 78  GLU A OE2 1 
ATOM   593   N  N   . ARG A  1 106 ? 85.394  43.210  -6.167  1.00 31.69 ? 79  ARG A N   1 
ATOM   594   C  CA  . ARG A  1 106 ? 84.813  43.566  -7.457  1.00 26.91 ? 79  ARG A CA  1 
ATOM   595   C  C   . ARG A  1 106 ? 84.154  44.930  -7.334  1.00 28.73 ? 79  ARG A C   1 
ATOM   596   O  O   . ARG A  1 106 ? 83.909  45.421  -6.231  1.00 26.63 ? 79  ARG A O   1 
ATOM   597   C  CB  . ARG A  1 106 ? 83.774  42.526  -7.916  1.00 25.65 ? 79  ARG A CB  1 
ATOM   598   C  CG  . ARG A  1 106 ? 82.647  42.317  -6.904  1.00 26.45 ? 79  ARG A CG  1 
ATOM   599   C  CD  . ARG A  1 106 ? 81.507  41.524  -7.496  1.00 28.58 ? 79  ARG A CD  1 
ATOM   600   N  NE  . ARG A  1 106 ? 80.531  42.371  -8.174  1.00 24.24 ? 79  ARG A NE  1 
ATOM   601   C  CZ  . ARG A  1 106 ? 79.357  41.935  -8.603  1.00 26.36 ? 79  ARG A CZ  1 
ATOM   602   N  NH1 . ARG A  1 106 ? 78.999  40.667  -8.461  1.00 24.22 ? 79  ARG A NH1 1 
ATOM   603   N  NH2 . ARG A  1 106 ? 78.523  42.789  -9.193  1.00 22.23 ? 79  ARG A NH2 1 
ATOM   604   N  N   . HIS A  1 107 ? 83.874  45.534  -8.485  1.00 24.25 ? 80  HIS A N   1 
ATOM   605   C  CA  . HIS A  1 107 ? 82.975  46.680  -8.560  1.00 28.46 ? 80  HIS A CA  1 
ATOM   606   C  C   . HIS A  1 107 ? 81.536  46.211  -8.407  1.00 26.98 ? 80  HIS A C   1 
ATOM   607   O  O   . HIS A  1 107 ? 81.197  45.075  -8.757  1.00 25.07 ? 80  HIS A O   1 
ATOM   608   C  CB  . HIS A  1 107 ? 83.151  47.399  -9.901  1.00 23.24 ? 80  HIS A CB  1 
ATOM   609   C  CG  . HIS A  1 107 ? 84.544  47.890  -10.127 1.00 24.71 ? 80  HIS A CG  1 
ATOM   610   N  ND1 . HIS A  1 107 ? 85.075  48.105  -11.378 1.00 29.66 ? 80  HIS A ND1 1 
ATOM   611   C  CD2 . HIS A  1 107 ? 85.510  48.239  -9.243  1.00 28.33 ? 80  HIS A CD2 1 
ATOM   612   C  CE1 . HIS A  1 107 ? 86.310  48.556  -11.257 1.00 24.97 ? 80  HIS A CE1 1 
ATOM   613   N  NE2 . HIS A  1 107 ? 86.597  48.646  -9.971  1.00 24.73 ? 80  HIS A NE2 1 
ATOM   614   N  N   . VAL A  1 108 ? 80.671  47.087  -7.879  1.00 22.81 ? 81  VAL A N   1 
ATOM   615   C  CA  . VAL A  1 108 ? 79.256  46.714  -7.863  1.00 19.70 ? 81  VAL A CA  1 
ATOM   616   C  C   . VAL A  1 108 ? 78.765  46.459  -9.289  1.00 16.19 ? 81  VAL A C   1 
ATOM   617   O  O   . VAL A  1 108 ? 78.026  45.504  -9.539  1.00 23.50 ? 81  VAL A O   1 
ATOM   618   C  CB  . VAL A  1 108 ? 78.395  47.770  -7.140  1.00 21.83 ? 81  VAL A CB  1 
ATOM   619   C  CG1 . VAL A  1 108 ? 76.919  47.497  -7.409  1.00 21.60 ? 81  VAL A CG1 1 
ATOM   620   C  CG2 . VAL A  1 108 ? 78.648  47.726  -5.628  1.00 21.29 ? 81  VAL A CG2 1 
ATOM   621   N  N   . GLY A  1 109 ? 79.218  47.260  -10.249 1.00 22.19 ? 82  GLY A N   1 
ATOM   622   C  CA  . GLY A  1 109 ? 78.814  47.093  -11.641 1.00 21.71 ? 82  GLY A CA  1 
ATOM   623   C  C   . GLY A  1 109 ? 79.458  45.962  -12.427 1.00 23.07 ? 82  GLY A C   1 
ATOM   624   O  O   . GLY A  1 109 ? 79.216  45.857  -13.632 1.00 23.13 ? 82  GLY A O   1 
ATOM   625   N  N   . ASP A  1 110 ? 80.231  45.083  -11.787 1.00 23.24 ? 83  ASP A N   1 
ATOM   626   C  CA  . ASP A  1 110 ? 80.993  44.025  -12.476 1.00 24.24 ? 83  ASP A CA  1 
ATOM   627   C  C   . ASP A  1 110 ? 80.112  42.803  -12.704 1.00 21.06 ? 83  ASP A C   1 
ATOM   628   O  O   . ASP A  1 110 ? 80.094  41.868  -11.907 1.00 24.95 ? 83  ASP A O   1 
ATOM   629   C  CB  . ASP A  1 110 ? 82.230  43.637  -11.669 1.00 28.01 ? 83  ASP A CB  1 
ATOM   630   C  CG  . ASP A  1 110 ? 83.353  44.642  -11.806 1.00 25.44 ? 83  ASP A CG  1 
ATOM   631   O  OD1 . ASP A  1 110 ? 83.260  45.469  -12.731 1.00 22.73 ? 83  ASP A OD1 1 
ATOM   632   O  OD2 . ASP A  1 110 ? 84.319  44.620  -10.983 1.00 25.18 ? 83  ASP A OD2 1 
ATOM   633   N  N   . LEU A  1 111 ? 79.403  42.778  -13.831 1.00 23.40 ? 84  LEU A N   1 
ATOM   634   C  CA  . LEU A  1 111 ? 78.548  41.649  -14.146 1.00 21.47 ? 84  LEU A CA  1 
ATOM   635   C  C   . LEU A  1 111 ? 79.229  40.619  -15.053 1.00 23.42 ? 84  LEU A C   1 
ATOM   636   O  O   . LEU A  1 111 ? 78.563  39.694  -15.514 1.00 24.80 ? 84  LEU A O   1 
ATOM   637   C  CB  . LEU A  1 111 ? 77.245  42.135  -14.790 1.00 19.73 ? 84  LEU A CB  1 
ATOM   638   C  CG  . LEU A  1 111 ? 76.382  43.010  -13.859 1.00 24.54 ? 84  LEU A CG  1 
ATOM   639   C  CD1 . LEU A  1 111 ? 75.073  43.403  -14.552 1.00 21.29 ? 84  LEU A CD1 1 
ATOM   640   C  CD2 . LEU A  1 111 ? 76.098  42.297  -12.538 1.00 21.54 ? 84  LEU A CD2 1 
ATOM   641   N  N   . GLY A  1 112 ? 80.524  40.764  -15.326 1.00 26.14 ? 85  GLY A N   1 
ATOM   642   C  CA  . GLY A  1 112 ? 81.244  39.744  -16.065 1.00 21.63 ? 85  GLY A CA  1 
ATOM   643   C  C   . GLY A  1 112 ? 81.072  39.866  -17.559 1.00 22.34 ? 85  GLY A C   1 
ATOM   644   O  O   . GLY A  1 112 ? 81.064  40.973  -18.089 1.00 21.20 ? 85  GLY A O   1 
ATOM   645   N  N   . ASN A  1 113 ? 80.954  38.733  -18.243 1.00 21.74 ? 86  ASN A N   1 
ATOM   646   C  CA  . ASN A  1 113 ? 80.798  38.651  -19.685 1.00 24.34 ? 86  ASN A CA  1 
ATOM   647   C  C   . ASN A  1 113 ? 79.425  38.117  -20.061 1.00 18.48 ? 86  ASN A C   1 
ATOM   648   O  O   . ASN A  1 113 ? 78.782  37.392  -19.299 1.00 21.81 ? 86  ASN A O   1 
ATOM   649   C  CB  . ASN A  1 113 ? 81.861  37.721  -20.306 1.00 23.93 ? 86  ASN A CB  1 
ATOM   650   C  CG  . ASN A  1 113 ? 83.263  38.287  -20.195 1.00 26.87 ? 86  ASN A CG  1 
ATOM   651   O  OD1 . ASN A  1 113 ? 83.577  39.299  -20.800 1.00 25.71 ? 86  ASN A OD1 1 
ATOM   652   N  ND2 . ASN A  1 113 ? 84.110  37.634  -19.414 1.00 21.93 ? 86  ASN A ND2 1 
ATOM   653   N  N   . VAL A  1 114 ? 79.007  38.467  -21.280 1.00 20.15 ? 87  VAL A N   1 
ATOM   654   C  CA  . VAL A  1 114 ? 77.912  37.798  -21.964 1.00 20.27 ? 87  VAL A CA  1 
ATOM   655   C  C   . VAL A  1 114 ? 78.469  37.184  -23.244 1.00 23.42 ? 87  VAL A C   1 
ATOM   656   O  O   . VAL A  1 114 ? 79.431  37.689  -23.832 1.00 25.51 ? 87  VAL A O   1 
ATOM   657   C  CB  . VAL A  1 114 ? 76.740  38.757  -22.272 1.00 20.51 ? 87  VAL A CB  1 
ATOM   658   C  CG1 . VAL A  1 114 ? 76.148  39.247  -20.942 1.00 17.46 ? 87  VAL A CG1 1 
ATOM   659   C  CG2 . VAL A  1 114 ? 77.209  39.931  -23.129 1.00 20.79 ? 87  VAL A CG2 1 
ATOM   660   N  N   . THR A  1 115 ? 77.849  36.096  -23.673 1.00 24.44 ? 88  THR A N   1 
ATOM   661   C  CA  . THR A  1 115 ? 78.356  35.274  -24.771 1.00 28.35 ? 88  THR A CA  1 
ATOM   662   C  C   . THR A  1 115 ? 77.440  35.412  -25.974 1.00 24.43 ? 88  THR A C   1 
ATOM   663   O  O   . THR A  1 115 ? 76.259  35.053  -25.909 1.00 26.54 ? 88  THR A O   1 
ATOM   664   C  CB  . THR A  1 115 ? 78.454  33.800  -24.367 1.00 31.02 ? 88  THR A CB  1 
ATOM   665   O  OG1 . THR A  1 115 ? 79.358  33.663  -23.265 1.00 26.19 ? 88  THR A OG1 1 
ATOM   666   C  CG2 . THR A  1 115 ? 78.987  32.971  -25.550 1.00 29.62 ? 88  THR A CG2 1 
ATOM   667   N  N   . ALA A  1 116 ? 77.991  35.905  -27.076 1.00 22.51 ? 89  ALA A N   1 
ATOM   668   C  CA  . ALA A  1 116 ? 77.249  36.015  -28.317 1.00 21.08 ? 89  ALA A CA  1 
ATOM   669   C  C   . ALA A  1 116 ? 77.503  34.771  -29.171 1.00 30.12 ? 89  ALA A C   1 
ATOM   670   O  O   . ALA A  1 116 ? 78.641  34.308  -29.278 1.00 25.07 ? 89  ALA A O   1 
ATOM   671   C  CB  . ALA A  1 116 ? 77.661  37.274  -29.077 1.00 24.49 ? 89  ALA A CB  1 
ATOM   672   N  N   . ASP A  1 117 ? 76.437  34.229  -29.763 1.00 26.37 ? 90  ASP A N   1 
ATOM   673   C  CA  . ASP A  1 117 ? 76.520  33.014  -30.567 1.00 32.62 ? 90  ASP A CA  1 
ATOM   674   C  C   . ASP A  1 117 ? 76.951  33.334  -32.002 1.00 34.43 ? 90  ASP A C   1 
ATOM   675   O  O   . ASP A  1 117 ? 77.303  34.470  -32.336 1.00 28.15 ? 90  ASP A O   1 
ATOM   676   C  CB  . ASP A  1 117 ? 75.193  32.250  -30.503 1.00 32.24 ? 90  ASP A CB  1 
ATOM   677   C  CG  . ASP A  1 117 ? 74.027  32.984  -31.184 1.00 33.55 ? 90  ASP A CG  1 
ATOM   678   O  OD1 . ASP A  1 117 ? 74.242  33.827  -32.084 1.00 34.23 ? 90  ASP A OD1 1 
ATOM   679   O  OD2 . ASP A  1 117 ? 72.864  32.690  -30.825 1.00 34.91 ? 90  ASP A OD2 1 
ATOM   680   N  N   . LYS A  1 118 ? 76.923  32.317  -32.879 1.00 31.75 ? 91  LYS A N   1 
ATOM   681   C  CA  . LYS A  1 118 ? 77.409  32.493  -34.241 1.00 35.64 ? 91  LYS A CA  1 
ATOM   682   C  C   . LYS A  1 118 ? 76.520  33.421  -35.057 1.00 30.79 ? 91  LYS A C   1 
ATOM   683   O  O   . LYS A  1 118 ? 76.982  33.955  -36.070 1.00 36.45 ? 91  LYS A O   1 
ATOM   684   C  CB  . LYS A  1 118 ? 77.522  31.137  -34.960 1.00 34.01 ? 91  LYS A CB  1 
ATOM   685   C  CG  . LYS A  1 118 ? 76.242  30.302  -34.963 1.00 42.04 ? 91  LYS A CG  1 
ATOM   686   C  CD  . LYS A  1 118 ? 76.460  28.942  -35.649 1.00 46.80 ? 91  LYS A CD  1 
ATOM   687   C  CE  . LYS A  1 118 ? 75.488  27.896  -35.138 1.00 52.98 ? 91  LYS A CE  1 
ATOM   688   N  NZ  . LYS A  1 118 ? 74.081  28.394  -35.241 1.00 57.55 ? 91  LYS A NZ  1 
ATOM   689   N  N   . ASP A  1 119 ? 75.258  33.604  -34.658 1.00 32.62 ? 92  ASP A N   1 
ATOM   690   C  CA  . ASP A  1 119 ? 74.354  34.553  -35.298 1.00 29.29 ? 92  ASP A CA  1 
ATOM   691   C  C   . ASP A  1 119 ? 74.456  35.963  -34.729 1.00 32.81 ? 92  ASP A C   1 
ATOM   692   O  O   . ASP A  1 119 ? 73.657  36.826  -35.108 1.00 31.35 ? 92  ASP A O   1 
ATOM   693   C  CB  . ASP A  1 119 ? 72.910  34.078  -35.191 1.00 31.98 ? 92  ASP A CB  1 
ATOM   694   C  CG  . ASP A  1 119 ? 72.618  32.949  -36.145 1.00 56.59 ? 92  ASP A CG  1 
ATOM   695   O  OD1 . ASP A  1 119 ? 72.616  33.214  -37.373 1.00 62.05 ? 92  ASP A OD1 1 
ATOM   696   O  OD2 . ASP A  1 119 ? 72.445  31.802  -35.675 1.00 56.73 ? 92  ASP A OD2 1 
ATOM   697   N  N   . GLY A  1 120 ? 75.406  36.211  -33.841 1.00 26.29 ? 93  GLY A N   1 
ATOM   698   C  CA  . GLY A  1 120 ? 75.598  37.542  -33.297 1.00 32.05 ? 93  GLY A CA  1 
ATOM   699   C  C   . GLY A  1 120 ? 74.697  37.899  -32.136 1.00 26.97 ? 93  GLY A C   1 
ATOM   700   O  O   . GLY A  1 120 ? 74.596  39.084  -31.796 1.00 30.27 ? 93  GLY A O   1 
ATOM   701   N  N   . VAL A  1 121 ? 74.031  36.918  -31.527 1.00 25.63 ? 94  VAL A N   1 
ATOM   702   C  CA  . VAL A  1 121 ? 73.016  37.149  -30.498 1.00 24.94 ? 94  VAL A CA  1 
ATOM   703   C  C   . VAL A  1 121 ? 73.529  36.642  -29.160 1.00 30.32 ? 94  VAL A C   1 
ATOM   704   O  O   . VAL A  1 121 ? 73.956  35.483  -29.047 1.00 27.57 ? 94  VAL A O   1 
ATOM   705   C  CB  . VAL A  1 121 ? 71.688  36.456  -30.847 1.00 29.29 ? 94  VAL A CB  1 
ATOM   706   C  CG1 . VAL A  1 121 ? 70.674  36.656  -29.692 1.00 28.42 ? 94  VAL A CG1 1 
ATOM   707   C  CG2 . VAL A  1 121 ? 71.124  36.997  -32.149 1.00 28.00 ? 94  VAL A CG2 1 
ATOM   708   N  N   . ALA A  1 122 ? 73.465  37.496  -28.143 1.00 25.88 ? 95  ALA A N   1 
ATOM   709   C  CA  . ALA A  1 122 ? 73.735  37.093  -26.770 1.00 24.70 ? 95  ALA A CA  1 
ATOM   710   C  C   . ALA A  1 122 ? 72.399  36.980  -26.044 1.00 26.95 ? 95  ALA A C   1 
ATOM   711   O  O   . ALA A  1 122 ? 71.699  37.984  -25.874 1.00 24.36 ? 95  ALA A O   1 
ATOM   712   C  CB  . ALA A  1 122 ? 74.666  38.090  -26.070 1.00 26.30 ? 95  ALA A CB  1 
ATOM   713   N  N   . ASP A  1 123 ? 72.029  35.755  -25.654 1.00 25.19 ? 96  ASP A N   1 
ATOM   714   C  CA  . ASP A  1 123 ? 70.811  35.524  -24.877 1.00 23.08 ? 96  ASP A CA  1 
ATOM   715   C  C   . ASP A  1 123 ? 71.213  35.613  -23.415 1.00 23.86 ? 96  ASP A C   1 
ATOM   716   O  O   . ASP A  1 123 ? 71.537  34.615  -22.774 1.00 23.94 ? 96  ASP A O   1 
ATOM   717   C  CB  . ASP A  1 123 ? 70.168  34.183  -25.212 1.00 28.49 ? 96  ASP A CB  1 
ATOM   718   C  CG  . ASP A  1 123 ? 69.531  34.169  -26.599 1.00 51.72 ? 96  ASP A CG  1 
ATOM   719   O  OD1 . ASP A  1 123 ? 68.766  35.120  -26.917 1.00 42.57 ? 96  ASP A OD1 1 
ATOM   720   O  OD2 . ASP A  1 123 ? 69.811  33.223  -27.379 1.00 44.39 ? 96  ASP A OD2 1 
ATOM   721   N  N   . VAL A  1 124 ? 71.165  36.833  -22.881 1.00 22.99 ? 97  VAL A N   1 
ATOM   722   C  CA  . VAL A  1 124 ? 71.689  37.108  -21.546 1.00 18.42 ? 97  VAL A CA  1 
ATOM   723   C  C   . VAL A  1 124 ? 70.832  36.430  -20.483 1.00 20.36 ? 97  VAL A C   1 
ATOM   724   O  O   . VAL A  1 124 ? 69.594  36.480  -20.521 1.00 22.29 ? 97  VAL A O   1 
ATOM   725   C  CB  . VAL A  1 124 ? 71.749  38.628  -21.313 1.00 19.87 ? 97  VAL A CB  1 
ATOM   726   C  CG1 . VAL A  1 124 ? 72.303  38.952  -19.900 1.00 17.27 ? 97  VAL A CG1 1 
ATOM   727   C  CG2 . VAL A  1 124 ? 72.586  39.303  -22.367 1.00 21.35 ? 97  VAL A CG2 1 
ATOM   728   N  N   . SER A  1 125 ? 71.491  35.828  -19.496 1.00 23.57 ? 98  SER A N   1 
ATOM   729   C  CA  . SER A  1 125 ? 70.797  35.297  -18.329 1.00 26.79 ? 98  SER A CA  1 
ATOM   730   C  C   . SER A  1 125 ? 71.790  35.297  -17.179 1.00 31.66 ? 98  SER A C   1 
ATOM   731   O  O   . SER A  1 125 ? 72.714  34.480  -17.153 1.00 24.98 ? 98  SER A O   1 
ATOM   732   C  CB  . SER A  1 125 ? 70.242  33.897  -18.590 1.00 33.24 ? 98  SER A CB  1 
ATOM   733   O  OG  . SER A  1 125 ? 69.706  33.363  -17.390 1.00 32.13 ? 98  SER A OG  1 
ATOM   734   N  N   . ILE A  1 126 ? 71.595  36.213  -16.233 1.00 22.98 ? 99  ILE A N   1 
ATOM   735   C  CA  . ILE A  1 126 ? 72.533  36.455  -15.148 1.00 22.54 ? 99  ILE A CA  1 
ATOM   736   C  C   . ILE A  1 126 ? 71.716  36.599  -13.864 1.00 26.00 ? 99  ILE A C   1 
ATOM   737   O  O   . ILE A  1 126 ? 70.568  37.057  -13.893 1.00 23.75 ? 99  ILE A O   1 
ATOM   738   C  CB  . ILE A  1 126 ? 73.382  37.714  -15.448 1.00 24.23 ? 99  ILE A CB  1 
ATOM   739   C  CG1 . ILE A  1 126 ? 74.494  37.369  -16.444 1.00 28.03 ? 99  ILE A CG1 1 
ATOM   740   C  CG2 . ILE A  1 126 ? 74.022  38.304  -14.186 1.00 27.93 ? 99  ILE A CG2 1 
ATOM   741   C  CD1 . ILE A  1 126 ? 75.242  38.588  -16.974 1.00 27.91 ? 99  ILE A CD1 1 
ATOM   742   N  N   . GLU A  1 127 ? 72.273  36.139  -12.754 1.00 23.31 ? 100 GLU A N   1 
ATOM   743   C  CA  . GLU A  1 127 ? 71.711  36.424  -11.441 1.00 23.29 ? 100 GLU A CA  1 
ATOM   744   C  C   . GLU A  1 127 ? 72.824  36.988  -10.586 1.00 28.37 ? 100 GLU A C   1 
ATOM   745   O  O   . GLU A  1 127 ? 73.914  36.418  -10.542 1.00 28.88 ? 100 GLU A O   1 
ATOM   746   C  CB  . GLU A  1 127 ? 71.119  35.168  -10.800 1.00 31.18 ? 100 GLU A CB  1 
ATOM   747   C  CG  . GLU A  1 127 ? 70.309  35.443  -9.561  1.00 35.20 ? 100 GLU A CG  1 
ATOM   748   C  CD  . GLU A  1 127 ? 69.647  34.188  -9.013  1.00 52.40 ? 100 GLU A CD  1 
ATOM   749   O  OE1 . GLU A  1 127 ? 70.074  33.714  -7.936  1.00 56.88 ? 100 GLU A OE1 1 
ATOM   750   O  OE2 . GLU A  1 127 ? 68.716  33.674  -9.675  1.00 59.60 ? 100 GLU A OE2 1 
ATOM   751   N  N   . ASP A  1 128 ? 72.570  38.119  -9.931  1.00 21.95 ? 101 ASP A N   1 
ATOM   752   C  CA  . ASP A  1 128 ? 73.628  38.783  -9.189  1.00 21.36 ? 101 ASP A CA  1 
ATOM   753   C  C   . ASP A  1 128 ? 73.090  39.296  -7.859  1.00 26.21 ? 101 ASP A C   1 
ATOM   754   O  O   . ASP A  1 128 ? 71.997  39.865  -7.808  1.00 23.20 ? 101 ASP A O   1 
ATOM   755   C  CB  . ASP A  1 128 ? 74.226  39.937  -9.986  1.00 25.56 ? 101 ASP A CB  1 
ATOM   756   C  CG  . ASP A  1 128 ? 75.537  40.419  -9.401  1.00 32.02 ? 101 ASP A CG  1 
ATOM   757   O  OD1 . ASP A  1 128 ? 76.582  39.756  -9.606  1.00 34.06 ? 101 ASP A OD1 1 
ATOM   758   O  OD2 . ASP A  1 128 ? 75.528  41.460  -8.722  1.00 25.87 ? 101 ASP A OD2 1 
ATOM   759   N  N   . SER A  1 129 ? 73.872  39.112  -6.791  1.00 27.41 ? 102 SER A N   1 
ATOM   760   C  CA  . SER A  1 129 ? 73.470  39.522  -5.450  1.00 26.21 ? 102 SER A CA  1 
ATOM   761   C  C   . SER A  1 129 ? 74.178  40.776  -4.961  1.00 27.78 ? 102 SER A C   1 
ATOM   762   O  O   . SER A  1 129 ? 74.030  41.147  -3.793  1.00 28.78 ? 102 SER A O   1 
ATOM   763   C  CB  . SER A  1 129 ? 73.706  38.386  -4.453  1.00 32.60 ? 102 SER A CB  1 
ATOM   764   O  OG  . SER A  1 129 ? 72.934  37.256  -4.801  1.00 39.31 ? 102 SER A OG  1 
ATOM   765   N  N   . VAL A  1 130 ? 74.954  41.436  -5.804  1.00 21.55 ? 103 VAL A N   1 
ATOM   766   C  CA  . VAL A  1 130 ? 75.657  42.635  -5.393  1.00 22.03 ? 103 VAL A CA  1 
ATOM   767   C  C   . VAL A  1 130 ? 74.963  43.885  -5.917  1.00 28.19 ? 103 VAL A C   1 
ATOM   768   O  O   . VAL A  1 130 ? 74.783  44.856  -5.184  1.00 23.34 ? 103 VAL A O   1 
ATOM   769   C  CB  . VAL A  1 130 ? 77.135  42.573  -5.832  1.00 22.77 ? 103 VAL A CB  1 
ATOM   770   C  CG1 . VAL A  1 130 ? 77.826  43.902  -5.559  1.00 27.90 ? 103 VAL A CG1 1 
ATOM   771   C  CG2 . VAL A  1 130 ? 77.849  41.432  -5.095  1.00 28.53 ? 103 VAL A CG2 1 
ATOM   772   N  N   . ILE A  1 131 ? 74.563  43.880  -7.188  1.00 21.62 ? 104 ILE A N   1 
ATOM   773   C  CA  . ILE A  1 131 ? 73.703  44.969  -7.678  1.00 18.44 ? 104 ILE A CA  1 
ATOM   774   C  C   . ILE A  1 131 ? 72.330  44.880  -7.008  1.00 20.14 ? 104 ILE A C   1 
ATOM   775   O  O   . ILE A  1 131 ? 71.907  43.826  -6.514  1.00 20.92 ? 104 ILE A O   1 
ATOM   776   C  CB  . ILE A  1 131 ? 73.545  44.934  -9.208  1.00 18.30 ? 104 ILE A CB  1 
ATOM   777   C  CG1 . ILE A  1 131 ? 72.961  43.581  -9.652  1.00 20.21 ? 104 ILE A CG1 1 
ATOM   778   C  CG2 . ILE A  1 131 ? 74.858  45.231  -9.905  1.00 20.14 ? 104 ILE A CG2 1 
ATOM   779   C  CD1 . ILE A  1 131 ? 72.265  43.604  -11.051 1.00 20.79 ? 104 ILE A CD1 1 
ATOM   780   N  N   . SER A  1 132 ? 71.603  45.995  -7.048  1.00 20.72 ? 105 SER A N   1 
ATOM   781   C  CA  . SER A  1 132 ? 70.259  46.046  -6.492  1.00 18.19 ? 105 SER A CA  1 
ATOM   782   C  C   . SER A  1 132 ? 69.451  47.055  -7.288  1.00 17.74 ? 105 SER A C   1 
ATOM   783   O  O   . SER A  1 132 ? 70.013  47.930  -7.951  1.00 21.45 ? 105 SER A O   1 
ATOM   784   C  CB  . SER A  1 132 ? 70.271  46.440  -5.010  1.00 21.46 ? 105 SER A CB  1 
ATOM   785   O  OG  . SER A  1 132 ? 68.971  46.267  -4.466  1.00 22.82 ? 105 SER A OG  1 
ATOM   786   N  N   . LEU A  1 133 ? 68.125  46.924  -7.228  1.00 18.68 ? 106 LEU A N   1 
ATOM   787   C  CA  . LEU A  1 133 ? 67.231  47.915  -7.820  1.00 20.31 ? 106 LEU A CA  1 
ATOM   788   C  C   . LEU A  1 133 ? 66.722  48.933  -6.803  1.00 21.75 ? 106 LEU A C   1 
ATOM   789   O  O   . LEU A  1 133 ? 65.818  49.712  -7.120  1.00 23.69 ? 106 LEU A O   1 
ATOM   790   C  CB  . LEU A  1 133 ? 66.051  47.221  -8.501  1.00 19.55 ? 106 LEU A CB  1 
ATOM   791   C  CG  . LEU A  1 133 ? 66.428  46.216  -9.598  1.00 21.97 ? 106 LEU A CG  1 
ATOM   792   C  CD1 . LEU A  1 133 ? 65.176  45.571  -10.261 1.00 19.47 ? 106 LEU A CD1 1 
ATOM   793   C  CD2 . LEU A  1 133 ? 67.341  46.861  -10.656 1.00 19.54 ? 106 LEU A CD2 1 
ATOM   794   N  N   . SER A  1 134 ? 67.283  48.946  -5.598  1.00 23.31 ? 107 SER A N   1 
ATOM   795   C  CA  . SER A  1 134 ? 66.950  49.926  -4.564  1.00 31.28 ? 107 SER A CA  1 
ATOM   796   C  C   . SER A  1 134 ? 68.141  50.039  -3.621  1.00 26.24 ? 107 SER A C   1 
ATOM   797   O  O   . SER A  1 134 ? 69.036  49.187  -3.625  1.00 24.81 ? 107 SER A O   1 
ATOM   798   C  CB  . SER A  1 134 ? 65.684  49.531  -3.791  1.00 28.33 ? 107 SER A CB  1 
ATOM   799   O  OG  . SER A  1 134 ? 65.814  48.241  -3.212  1.00 27.37 ? 107 SER A OG  1 
ATOM   800   N  N   . GLY A  1 135 ? 68.162  51.116  -2.829  1.00 27.70 ? 108 GLY A N   1 
ATOM   801   C  CA  . GLY A  1 135 ? 69.225  51.312  -1.858  1.00 28.75 ? 108 GLY A CA  1 
ATOM   802   C  C   . GLY A  1 135 ? 70.534  51.806  -2.460  1.00 33.68 ? 108 GLY A C   1 
ATOM   803   O  O   . GLY A  1 135 ? 70.592  52.343  -3.562  1.00 31.58 ? 108 GLY A O   1 
ATOM   804   N  N   . ASP A  1 136 ? 71.615  51.602  -1.706  1.00 28.86 ? 109 ASP A N   1 
ATOM   805   C  CA  . ASP A  1 136 ? 72.888  52.239  -2.048  1.00 33.75 ? 109 ASP A CA  1 
ATOM   806   C  C   . ASP A  1 136 ? 73.547  51.586  -3.256  1.00 32.85 ? 109 ASP A C   1 
ATOM   807   O  O   . ASP A  1 136 ? 74.297  52.241  -3.983  1.00 30.14 ? 109 ASP A O   1 
ATOM   808   C  CB  . ASP A  1 136 ? 73.848  52.181  -0.855  1.00 39.60 ? 109 ASP A CB  1 
ATOM   809   C  CG  . ASP A  1 136 ? 73.559  53.265  0.195   1.00 58.81 ? 109 ASP A CG  1 
ATOM   810   O  OD1 . ASP A  1 136 ? 72.586  54.041  0.014   1.00 58.20 ? 109 ASP A OD1 1 
ATOM   811   O  OD2 . ASP A  1 136 ? 74.296  53.324  1.211   1.00 54.71 ? 109 ASP A OD2 1 
ATOM   812   N  N   . HIS A  1 137 ? 73.332  50.296  -3.463  1.00 28.06 ? 110 HIS A N   1 
ATOM   813   C  CA  . HIS A  1 137 ? 73.834  49.662  -4.672  1.00 34.35 ? 110 HIS A CA  1 
ATOM   814   C  C   . HIS A  1 137 ? 72.839  49.744  -5.814  1.00 27.98 ? 110 HIS A C   1 
ATOM   815   O  O   . HIS A  1 137 ? 72.940  48.948  -6.760  1.00 28.29 ? 110 HIS A O   1 
ATOM   816   C  CB  . HIS A  1 137 ? 74.211  48.201  -4.397  1.00 30.35 ? 110 HIS A CB  1 
ATOM   817   C  CG  . HIS A  1 137 ? 75.415  48.050  -3.523  1.00 34.92 ? 110 HIS A CG  1 
ATOM   818   N  ND1 . HIS A  1 137 ? 75.938  46.822  -3.176  1.00 36.75 ? 110 HIS A ND1 1 
ATOM   819   C  CD2 . HIS A  1 137 ? 76.209  48.977  -2.936  1.00 34.16 ? 110 HIS A CD2 1 
ATOM   820   C  CE1 . HIS A  1 137 ? 76.998  46.998  -2.409  1.00 35.30 ? 110 HIS A CE1 1 
ATOM   821   N  NE2 . HIS A  1 137 ? 77.186  48.296  -2.249  1.00 36.57 ? 110 HIS A NE2 1 
ATOM   822   N  N   . CYS A  1 138 ? 71.875  50.671  -5.737  1.00 23.40 ? 111 CYS A N   1 
ATOM   823   C  CA  . CYS A  1 138 ? 70.846  50.778  -6.764  1.00 22.61 ? 111 CYS A CA  1 
ATOM   824   C  C   . CYS A  1 138 ? 71.465  51.160  -8.102  1.00 19.40 ? 111 CYS A C   1 
ATOM   825   O  O   . CYS A  1 138 ? 72.256  52.109  -8.195  1.00 20.69 ? 111 CYS A O   1 
ATOM   826   C  CB  . CYS A  1 138 ? 69.793  51.804  -6.350  1.00 28.07 ? 111 CYS A CB  1 
ATOM   827   S  SG  . CYS A  1 138 ? 68.467  52.023  -7.548  1.00 28.69 ? 111 CYS A SG  1 
ATOM   828   N  N   . ILE A  1 139 ? 71.093  50.417  -9.149  1.00 20.19 ? 112 ILE A N   1 
ATOM   829   C  CA  . ILE A  1 139 ? 71.588  50.675  -10.494 1.00 19.86 ? 112 ILE A CA  1 
ATOM   830   C  C   . ILE A  1 139 ? 70.556  51.364  -11.371 1.00 18.34 ? 112 ILE A C   1 
ATOM   831   O  O   . ILE A  1 139 ? 70.851  51.664  -12.527 1.00 17.38 ? 112 ILE A O   1 
ATOM   832   C  CB  . ILE A  1 139 ? 72.066  49.377  -11.174 1.00 19.54 ? 112 ILE A CB  1 
ATOM   833   C  CG1 . ILE A  1 139 ? 70.906  48.388  -11.356 1.00 17.89 ? 112 ILE A CG1 1 
ATOM   834   C  CG2 . ILE A  1 139 ? 73.254  48.766  -10.404 1.00 22.09 ? 112 ILE A CG2 1 
ATOM   835   C  CD1 . ILE A  1 139 ? 71.278  47.155  -12.167 1.00 21.31 ? 112 ILE A CD1 1 
ATOM   836   N  N   A ILE A  1 140 ? 69.350  51.618  -10.848 0.46 20.66 ? 113 ILE A N   1 
ATOM   837   N  N   B ILE A  1 140 ? 69.349  51.611  -10.867 0.54 20.63 ? 113 ILE A N   1 
ATOM   838   C  CA  A ILE A  1 140 ? 68.385  52.450  -11.560 0.46 20.93 ? 113 ILE A CA  1 
ATOM   839   C  CA  B ILE A  1 140 ? 68.385  52.365  -11.660 0.54 20.84 ? 113 ILE A CA  1 
ATOM   840   C  C   A ILE A  1 140 ? 69.015  53.798  -11.845 0.46 18.17 ? 113 ILE A C   1 
ATOM   841   C  C   B ILE A  1 140 ? 68.906  53.780  -11.838 0.54 18.13 ? 113 ILE A C   1 
ATOM   842   O  O   A ILE A  1 140 ? 69.641  54.406  -10.969 0.46 19.59 ? 113 ILE A O   1 
ATOM   843   O  O   B ILE A  1 140 ? 69.371  54.411  -10.882 0.54 19.80 ? 113 ILE A O   1 
ATOM   844   C  CB  A ILE A  1 140 ? 67.096  52.620  -10.739 0.46 20.72 ? 113 ILE A CB  1 
ATOM   845   C  CB  B ILE A  1 140 ? 67.005  52.338  -10.990 0.54 21.57 ? 113 ILE A CB  1 
ATOM   846   C  CG1 A ILE A  1 140 ? 66.524  51.262  -10.336 0.46 21.88 ? 113 ILE A CG1 1 
ATOM   847   C  CG1 B ILE A  1 140 ? 66.400  50.941  -11.134 0.54 23.11 ? 113 ILE A CG1 1 
ATOM   848   C  CG2 A ILE A  1 140 ? 66.065  53.470  -11.514 0.46 20.78 ? 113 ILE A CG2 1 
ATOM   849   C  CG2 B ILE A  1 140 ? 66.077  53.416  -11.597 0.54 20.81 ? 113 ILE A CG2 1 
ATOM   850   C  CD1 A ILE A  1 140 ? 65.690  50.613  -11.406 0.46 22.04 ? 113 ILE A CD1 1 
ATOM   851   C  CD1 B ILE A  1 140 ? 65.010  50.820  -10.581 0.54 20.43 ? 113 ILE A CD1 1 
ATOM   852   N  N   . GLY A  1 141 ? 68.851  54.280  -13.069 1.00 13.42 ? 114 GLY A N   1 
ATOM   853   C  CA  . GLY A  1 141 ? 69.409  55.576  -13.403 1.00 15.64 ? 114 GLY A CA  1 
ATOM   854   C  C   . GLY A  1 141 ? 70.870  55.563  -13.808 1.00 16.92 ? 114 GLY A C   1 
ATOM   855   O  O   . GLY A  1 141 ? 71.413  56.621  -14.130 1.00 14.75 ? 114 GLY A O   1 
ATOM   856   N  N   . ARG A  1 142 ? 71.528  54.405  -13.768 1.00 18.29 ? 115 ARG A N   1 
ATOM   857   C  CA  . ARG A  1 142 ? 72.911  54.274  -14.213 1.00 15.15 ? 115 ARG A CA  1 
ATOM   858   C  C   . ARG A  1 142 ? 72.898  53.621  -15.589 1.00 16.14 ? 115 ARG A C   1 
ATOM   859   O  O   . ARG A  1 142 ? 71.844  53.384  -16.160 1.00 19.84 ? 115 ARG A O   1 
ATOM   860   C  CB  . ARG A  1 142 ? 73.719  53.483  -13.183 1.00 15.79 ? 115 ARG A CB  1 
ATOM   861   C  CG  . ARG A  1 142 ? 73.455  53.958  -11.747 1.00 14.91 ? 115 ARG A CG  1 
ATOM   862   C  CD  . ARG A  1 142 ? 74.554  53.594  -10.771 1.00 15.77 ? 115 ARG A CD  1 
ATOM   863   N  NE  . ARG A  1 142 ? 74.263  54.109  -9.428  1.00 19.36 ? 115 ARG A NE  1 
ATOM   864   C  CZ  . ARG A  1 142 ? 74.740  55.242  -8.932  1.00 21.43 ? 115 ARG A CZ  1 
ATOM   865   N  NH1 . ARG A  1 142 ? 75.537  56.024  -9.638  1.00 20.39 ? 115 ARG A NH1 1 
ATOM   866   N  NH2 . ARG A  1 142 ? 74.427  55.586  -7.680  1.00 21.56 ? 115 ARG A NH2 1 
ATOM   867   N  N   . THR A  1 143 ? 74.066  53.374  -16.157 1.00 17.33 ? 116 THR A N   1 
ATOM   868   C  CA  . THR A  1 143 ? 74.155  52.975  -17.565 1.00 15.79 ? 116 THR A CA  1 
ATOM   869   C  C   . THR A  1 143 ? 74.687  51.554  -17.685 1.00 21.17 ? 116 THR A C   1 
ATOM   870   O  O   . THR A  1 143 ? 75.757  51.251  -17.153 1.00 19.88 ? 116 THR A O   1 
ATOM   871   C  CB  . THR A  1 143 ? 75.067  53.917  -18.360 1.00 19.69 ? 116 THR A CB  1 
ATOM   872   O  OG1 . THR A  1 143 ? 74.477  55.222  -18.439 1.00 21.86 ? 116 THR A OG1 1 
ATOM   873   C  CG2 . THR A  1 143 ? 75.262  53.404  -19.823 1.00 15.90 ? 116 THR A CG2 1 
ATOM   874   N  N   . LEU A  1 144 ? 73.961  50.694  -18.404 1.00 17.80 ? 117 LEU A N   1 
ATOM   875   C  CA  . LEU A  1 144 ? 74.448  49.360  -18.745 1.00 17.38 ? 117 LEU A CA  1 
ATOM   876   C  C   . LEU A  1 144 ? 75.176  49.444  -20.079 1.00 14.50 ? 117 LEU A C   1 
ATOM   877   O  O   . LEU A  1 144 ? 74.665  50.053  -21.019 1.00 17.31 ? 117 LEU A O   1 
ATOM   878   C  CB  . LEU A  1 144 ? 73.292  48.365  -18.842 1.00 15.55 ? 117 LEU A CB  1 
ATOM   879   C  CG  . LEU A  1 144 ? 73.649  46.912  -19.126 1.00 19.41 ? 117 LEU A CG  1 
ATOM   880   C  CD1 . LEU A  1 144 ? 74.329  46.317  -17.910 1.00 16.34 ? 117 LEU A CD1 1 
ATOM   881   C  CD2 . LEU A  1 144 ? 72.389  46.119  -19.512 1.00 15.85 ? 117 LEU A CD2 1 
ATOM   882   N  N   . VAL A  1 145 ? 76.379  48.873  -20.147 1.00 18.70 ? 118 VAL A N   1 
ATOM   883   C  CA  . VAL A  1 145 ? 77.222  48.939  -21.343 1.00 17.80 ? 118 VAL A CA  1 
ATOM   884   C  C   . VAL A  1 145 ? 77.650  47.526  -21.731 1.00 15.99 ? 118 VAL A C   1 
ATOM   885   O  O   . VAL A  1 145 ? 78.068  46.739  -20.877 1.00 15.88 ? 118 VAL A O   1 
ATOM   886   C  CB  . VAL A  1 145 ? 78.482  49.805  -21.107 1.00 21.51 ? 118 VAL A CB  1 
ATOM   887   C  CG1 . VAL A  1 145 ? 79.363  49.829  -22.357 1.00 21.99 ? 118 VAL A CG1 1 
ATOM   888   C  CG2 . VAL A  1 145 ? 78.116  51.221  -20.664 1.00 20.02 ? 118 VAL A CG2 1 
ATOM   889   N  N   . VAL A  1 146 ? 77.597  47.213  -23.021 1.00 19.51 ? 119 VAL A N   1 
ATOM   890   C  CA  . VAL A  1 146 ? 78.199  45.989  -23.530 1.00 24.02 ? 119 VAL A CA  1 
ATOM   891   C  C   . VAL A  1 146 ? 79.441  46.386  -24.324 1.00 21.12 ? 119 VAL A C   1 
ATOM   892   O  O   . VAL A  1 146 ? 79.420  47.356  -25.097 1.00 19.90 ? 119 VAL A O   1 
ATOM   893   C  CB  . VAL A  1 146 ? 77.205  45.158  -24.362 1.00 21.93 ? 119 VAL A CB  1 
ATOM   894   C  CG1 . VAL A  1 146 ? 76.689  45.934  -25.540 1.00 20.19 ? 119 VAL A CG1 1 
ATOM   895   C  CG2 . VAL A  1 146 ? 77.849  43.828  -24.799 1.00 21.23 ? 119 VAL A CG2 1 
ATOM   896   N  N   . HIS A  1 147 ? 80.534  45.671  -24.086 1.00 22.33 ? 120 HIS A N   1 
ATOM   897   C  CA  . HIS A  1 147 ? 81.853  46.092  -24.527 1.00 20.50 ? 120 HIS A CA  1 
ATOM   898   C  C   . HIS A  1 147 ? 82.315  45.247  -25.711 1.00 25.11 ? 120 HIS A C   1 
ATOM   899   O  O   . HIS A  1 147 ? 81.763  44.185  -26.021 1.00 23.20 ? 120 HIS A O   1 
ATOM   900   C  CB  . HIS A  1 147 ? 82.867  46.004  -23.382 1.00 20.55 ? 120 HIS A CB  1 
ATOM   901   C  CG  . HIS A  1 147 ? 82.725  47.082  -22.346 1.00 23.09 ? 120 HIS A CG  1 
ATOM   902   N  ND1 . HIS A  1 147 ? 83.475  48.240  -22.366 1.00 27.65 ? 120 HIS A ND1 1 
ATOM   903   C  CD2 . HIS A  1 147 ? 81.913  47.182  -21.266 1.00 23.05 ? 120 HIS A CD2 1 
ATOM   904   C  CE1 . HIS A  1 147 ? 83.142  49.000  -21.336 1.00 27.79 ? 120 HIS A CE1 1 
ATOM   905   N  NE2 . HIS A  1 147 ? 82.208  48.373  -20.643 1.00 23.80 ? 120 HIS A NE2 1 
ATOM   906   N  N   . GLU A  1 148 ? 83.383  45.739  -26.333 1.00 24.82 ? 121 GLU A N   1 
ATOM   907   C  CA  . GLU A  1 148 ? 83.904  45.178  -27.578 1.00 25.93 ? 121 GLU A CA  1 
ATOM   908   C  C   . GLU A  1 148 ? 84.567  43.823  -27.371 1.00 23.43 ? 121 GLU A C   1 
ATOM   909   O  O   . GLU A  1 148 ? 84.436  42.939  -28.224 1.00 28.25 ? 121 GLU A O   1 
ATOM   910   C  CB  . GLU A  1 148 ? 84.880  46.185  -28.184 1.00 28.89 ? 121 GLU A CB  1 
ATOM   911   C  CG  . GLU A  1 148 ? 85.777  45.679  -29.290 1.00 38.70 ? 121 GLU A CG  1 
ATOM   912   C  CD  . GLU A  1 148 ? 86.992  46.590  -29.476 1.00 51.55 ? 121 GLU A CD  1 
ATOM   913   O  OE1 . GLU A  1 148 ? 87.435  46.738  -30.638 1.00 51.01 ? 121 GLU A OE1 1 
ATOM   914   O  OE2 . GLU A  1 148 ? 87.448  47.221  -28.477 1.00 46.04 ? 121 GLU A OE2 1 
ATOM   915   N  N   . LYS A  1 149 ? 85.266  43.636  -26.256 1.00 24.36 ? 122 LYS A N   1 
ATOM   916   C  CA  . LYS A  1 149 ? 86.098  42.463  -26.006 1.00 33.52 ? 122 LYS A CA  1 
ATOM   917   C  C   . LYS A  1 149 ? 85.690  41.780  -24.707 1.00 31.36 ? 122 LYS A C   1 
ATOM   918   O  O   . LYS A  1 149 ? 84.868  42.281  -23.937 1.00 25.89 ? 122 LYS A O   1 
ATOM   919   C  CB  . LYS A  1 149 ? 87.580  42.844  -25.930 1.00 30.54 ? 122 LYS A CB  1 
ATOM   920   C  CG  . LYS A  1 149 ? 88.126  43.386  -27.220 1.00 36.66 ? 122 LYS A CG  1 
ATOM   921   C  CD  . LYS A  1 149 ? 89.603  43.680  -27.082 1.00 38.88 ? 122 LYS A CD  1 
ATOM   922   C  CE  . LYS A  1 149 ? 89.864  44.920  -26.245 1.00 44.92 ? 122 LYS A CE  1 
ATOM   923   N  NZ  . LYS A  1 149 ? 91.054  44.744  -25.336 1.00 46.56 ? 122 LYS A NZ  1 
ATOM   924   N  N   . ALA A  1 150 ? 86.296  40.620  -24.461 1.00 29.26 ? 123 ALA A N   1 
ATOM   925   C  CA  . ALA A  1 150 ? 86.050  39.905  -23.218 1.00 24.70 ? 123 ALA A CA  1 
ATOM   926   C  C   . ALA A  1 150 ? 86.590  40.685  -22.030 1.00 28.89 ? 123 ALA A C   1 
ATOM   927   O  O   . ALA A  1 150 ? 87.615  41.367  -22.112 1.00 28.81 ? 123 ALA A O   1 
ATOM   928   C  CB  . ALA A  1 150 ? 86.694  38.515  -23.260 1.00 31.98 ? 123 ALA A CB  1 
ATOM   929   N  N   . ASP A  1 151 ? 85.878  40.580  -20.920 1.00 24.63 ? 124 ASP A N   1 
ATOM   930   C  CA  . ASP A  1 151 ? 86.349  41.057  -19.631 1.00 24.61 ? 124 ASP A CA  1 
ATOM   931   C  C   . ASP A  1 151 ? 87.271  39.985  -19.049 1.00 27.45 ? 124 ASP A C   1 
ATOM   932   O  O   . ASP A  1 151 ? 86.878  38.815  -18.942 1.00 26.83 ? 124 ASP A O   1 
ATOM   933   C  CB  . ASP A  1 151 ? 85.125  41.325  -18.746 1.00 23.30 ? 124 ASP A CB  1 
ATOM   934   C  CG  . ASP A  1 151 ? 85.470  41.768  -17.334 1.00 31.99 ? 124 ASP A CG  1 
ATOM   935   O  OD1 . ASP A  1 151 ? 86.661  41.831  -16.966 1.00 30.02 ? 124 ASP A OD1 1 
ATOM   936   O  OD2 . ASP A  1 151 ? 84.512  42.070  -16.583 1.00 30.55 ? 124 ASP A OD2 1 
ATOM   937   N  N   . ASP A  1 152 ? 88.508  40.363  -18.712 1.00 26.92 ? 125 ASP A N   1 
ATOM   938   C  CA  . ASP A  1 152 ? 89.445  39.380  -18.173 1.00 32.28 ? 125 ASP A CA  1 
ATOM   939   C  C   . ASP A  1 152 ? 89.297  39.195  -16.670 1.00 32.76 ? 125 ASP A C   1 
ATOM   940   O  O   . ASP A  1 152 ? 90.110  38.485  -16.065 1.00 28.45 ? 125 ASP A O   1 
ATOM   941   C  CB  . ASP A  1 152 ? 90.900  39.743  -18.535 1.00 29.64 ? 125 ASP A CB  1 
ATOM   942   C  CG  . ASP A  1 152 ? 91.408  41.022  -17.848 1.00 31.97 ? 125 ASP A CG  1 
ATOM   943   O  OD1 . ASP A  1 152 ? 90.864  41.452  -16.812 1.00 29.73 ? 125 ASP A OD1 1 
ATOM   944   O  OD2 . ASP A  1 152 ? 92.383  41.606  -18.362 1.00 34.76 ? 125 ASP A OD2 1 
ATOM   945   N  N   . LEU A  1 153 ? 88.283  39.817  -16.063 1.00 27.99 ? 126 LEU A N   1 
ATOM   946   C  CA  . LEU A  1 153 ? 87.886  39.560  -14.679 1.00 26.29 ? 126 LEU A CA  1 
ATOM   947   C  C   . LEU A  1 153 ? 88.983  39.924  -13.690 1.00 22.24 ? 126 LEU A C   1 
ATOM   948   O  O   . LEU A  1 153 ? 89.028  39.402  -12.574 1.00 27.14 ? 126 LEU A O   1 
ATOM   949   C  CB  . LEU A  1 153 ? 87.442  38.105  -14.471 1.00 26.10 ? 126 LEU A CB  1 
ATOM   950   C  CG  . LEU A  1 153 ? 86.438  37.515  -15.478 1.00 31.10 ? 126 LEU A CG  1 
ATOM   951   C  CD1 . LEU A  1 153 ? 86.011  36.113  -15.042 1.00 33.52 ? 126 LEU A CD1 1 
ATOM   952   C  CD2 . LEU A  1 153 ? 85.210  38.416  -15.699 1.00 24.60 ? 126 LEU A CD2 1 
ATOM   953   N  N   . GLY A  1 154 ? 89.843  40.858  -14.059 1.00 24.57 ? 127 GLY A N   1 
ATOM   954   C  CA  . GLY A  1 154 ? 90.871  41.302  -13.141 1.00 29.25 ? 127 GLY A CA  1 
ATOM   955   C  C   . GLY A  1 154 ? 92.140  40.477  -13.153 1.00 32.67 ? 127 GLY A C   1 
ATOM   956   O  O   . GLY A  1 154 ? 93.036  40.736  -12.339 1.00 31.59 ? 127 GLY A O   1 
ATOM   957   N  N   . LYS A  1 155 ? 92.256  39.514  -14.067 1.00 30.63 ? 128 LYS A N   1 
ATOM   958   C  CA  . LYS A  1 155 ? 93.361  38.562  -14.088 1.00 36.67 ? 128 LYS A CA  1 
ATOM   959   C  C   . LYS A  1 155 ? 94.298  38.772  -15.271 1.00 36.69 ? 128 LYS A C   1 
ATOM   960   O  O   . LYS A  1 155 ? 95.016  37.842  -15.659 1.00 35.44 ? 128 LYS A O   1 
ATOM   961   C  CB  . LYS A  1 155 ? 92.814  37.132  -14.109 1.00 30.35 ? 128 LYS A CB  1 
ATOM   962   C  CG  . LYS A  1 155 ? 92.073  36.725  -12.853 1.00 33.43 ? 128 LYS A CG  1 
ATOM   963   C  CD  . LYS A  1 155 ? 91.412  35.357  -13.055 1.00 40.15 ? 128 LYS A CD  1 
ATOM   964   C  CE  . LYS A  1 155 ? 91.303  34.576  -11.747 1.00 43.90 ? 128 LYS A CE  1 
ATOM   965   N  NZ  . LYS A  1 155 ? 90.471  35.259  -10.702 1.00 44.50 ? 128 LYS A NZ  1 
ATOM   966   N  N   . GLY A  1 156 ? 94.299  39.966  -15.861 1.00 31.91 ? 129 GLY A N   1 
ATOM   967   C  CA  . GLY A  1 156 ? 95.082  40.222  -17.055 1.00 31.33 ? 129 GLY A CA  1 
ATOM   968   C  C   . GLY A  1 156 ? 96.508  40.694  -16.816 1.00 33.99 ? 129 GLY A C   1 
ATOM   969   O  O   . GLY A  1 156 ? 97.281  40.805  -17.767 1.00 39.03 ? 129 GLY A O   1 
ATOM   970   N  N   . GLY A  1 157 ? 96.874  40.994  -15.575 1.00 35.37 ? 130 GLY A N   1 
ATOM   971   C  CA  . GLY A  1 157 ? 98.243  41.383  -15.279 1.00 32.95 ? 130 GLY A CA  1 
ATOM   972   C  C   . GLY A  1 157 ? 98.663  42.766  -15.742 1.00 43.45 ? 130 GLY A C   1 
ATOM   973   O  O   . GLY A  1 157 ? 99.855  42.988  -15.991 1.00 41.74 ? 130 GLY A O   1 
ATOM   974   N  N   . ASN A  1 158 ? 97.728  43.711  -15.866 1.00 40.95 ? 131 ASN A N   1 
ATOM   975   C  CA  . ASN A  1 158 ? 98.099  45.108  -16.077 1.00 34.07 ? 131 ASN A CA  1 
ATOM   976   C  C   . ASN A  1 158 ? 97.135  46.022  -15.327 1.00 45.40 ? 131 ASN A C   1 
ATOM   977   O  O   . ASN A  1 158 ? 96.137  45.581  -14.743 1.00 43.18 ? 131 ASN A O   1 
ATOM   978   C  CB  . ASN A  1 158 ? 98.147  45.490  -17.563 1.00 37.03 ? 131 ASN A CB  1 
ATOM   979   C  CG  . ASN A  1 158 ? 96.910  45.090  -18.317 1.00 39.66 ? 131 ASN A CG  1 
ATOM   980   O  OD1 . ASN A  1 158 ? 95.867  44.824  -17.723 1.00 42.90 ? 131 ASN A OD1 1 
ATOM   981   N  ND2 . ASN A  1 158 ? 97.010  45.060  -19.644 1.00 46.57 ? 131 ASN A ND2 1 
ATOM   982   N  N   . GLU A  1 159 ? 97.475  47.314  -15.326 1.00 46.44 ? 132 GLU A N   1 
ATOM   983   C  CA  . GLU A  1 159 ? 96.643  48.319  -14.672 1.00 46.13 ? 132 GLU A CA  1 
ATOM   984   C  C   . GLU A  1 159 ? 95.215  48.283  -15.204 1.00 37.80 ? 132 GLU A C   1 
ATOM   985   O  O   . GLU A  1 159 ? 94.249  48.326  -14.432 1.00 39.09 ? 132 GLU A O   1 
ATOM   986   C  CB  . GLU A  1 159 ? 97.261  49.707  -14.875 1.00 51.86 ? 132 GLU A CB  1 
ATOM   987   C  CG  . GLU A  1 159 ? 96.912  50.717  -13.793 1.00 57.84 ? 132 GLU A CG  1 
ATOM   988   C  CD  . GLU A  1 159 ? 97.532  50.388  -12.442 1.00 66.57 ? 132 GLU A CD  1 
ATOM   989   O  OE1 . GLU A  1 159 ? 98.737  50.033  -12.391 1.00 63.76 ? 132 GLU A OE1 1 
ATOM   990   O  OE2 . GLU A  1 159 ? 96.798  50.463  -11.432 1.00 67.88 ? 132 GLU A OE2 1 
ATOM   991   N  N   . GLU A  1 160 ? 95.068  48.209  -16.529 1.00 39.14 ? 133 GLU A N   1 
ATOM   992   C  CA  . GLU A  1 160 ? 93.745  48.184  -17.140 1.00 41.50 ? 133 GLU A CA  1 
ATOM   993   C  C   . GLU A  1 160 ? 92.901  47.024  -16.623 1.00 44.53 ? 133 GLU A C   1 
ATOM   994   O  O   . GLU A  1 160 ? 91.682  47.171  -16.459 1.00 34.08 ? 133 GLU A O   1 
ATOM   995   C  CB  . GLU A  1 160 ? 93.887  48.113  -18.655 1.00 37.43 ? 133 GLU A CB  1 
ATOM   996   C  CG  . GLU A  1 160 ? 92.679  48.601  -19.430 1.00 43.70 ? 133 GLU A CG  1 
ATOM   997   C  CD  . GLU A  1 160 ? 92.445  50.099  -19.284 1.00 57.26 ? 133 GLU A CD  1 
ATOM   998   O  OE1 . GLU A  1 160 ? 93.094  50.889  -20.008 1.00 58.14 ? 133 GLU A OE1 1 
ATOM   999   O  OE2 . GLU A  1 160 ? 91.590  50.485  -18.452 1.00 55.70 ? 133 GLU A OE2 1 
ATOM   1000  N  N   . SER A  1 161 ? 93.526  45.873  -16.351 1.00 32.35 ? 134 SER A N   1 
ATOM   1001  C  CA  . SER A  1 161 ? 92.770  44.707  -15.903 1.00 33.68 ? 134 SER A CA  1 
ATOM   1002  C  C   . SER A  1 161 ? 92.002  44.982  -14.619 1.00 35.11 ? 134 SER A C   1 
ATOM   1003  O  O   . SER A  1 161 ? 90.865  44.529  -14.463 1.00 32.20 ? 134 SER A O   1 
ATOM   1004  C  CB  . SER A  1 161 ? 93.697  43.515  -15.696 1.00 33.79 ? 134 SER A CB  1 
ATOM   1005  O  OG  . SER A  1 161 ? 92.929  42.379  -15.360 1.00 37.13 ? 134 SER A OG  1 
ATOM   1006  N  N   . THR A  1 162 ? 92.615  45.682  -13.675 1.00 32.42 ? 135 THR A N   1 
ATOM   1007  C  CA  . THR A  1 162 ? 91.992  45.933  -12.386 1.00 33.37 ? 135 THR A CA  1 
ATOM   1008  C  C   . THR A  1 162 ? 91.073  47.153  -12.390 1.00 34.62 ? 135 THR A C   1 
ATOM   1009  O  O   . THR A  1 162 ? 90.527  47.506  -11.337 1.00 34.45 ? 135 THR A O   1 
ATOM   1010  C  CB  . THR A  1 162 ? 93.083  46.071  -11.325 1.00 39.07 ? 135 THR A CB  1 
ATOM   1011  O  OG1 . THR A  1 162 ? 93.918  47.183  -11.662 1.00 47.75 ? 135 THR A OG1 1 
ATOM   1012  C  CG2 . THR A  1 162 ? 93.929  44.799  -11.286 1.00 44.06 ? 135 THR A CG2 1 
ATOM   1013  N  N   . LYS A  1 163 ? 90.881  47.793  -13.542 1.00 32.98 ? 136 LYS A N   1 
ATOM   1014  C  CA  . LYS A  1 163 ? 89.978  48.930  -13.691 1.00 37.62 ? 136 LYS A CA  1 
ATOM   1015  C  C   . LYS A  1 163 ? 88.787  48.587  -14.571 1.00 36.20 ? 136 LYS A C   1 
ATOM   1016  O  O   . LYS A  1 163 ? 87.638  48.820  -14.188 1.00 38.75 ? 136 LYS A O   1 
ATOM   1017  C  CB  . LYS A  1 163 ? 90.720  50.137  -14.300 1.00 36.51 ? 136 LYS A CB  1 
ATOM   1018  C  CG  . LYS A  1 163 ? 91.731  50.820  -13.362 1.00 41.73 ? 136 LYS A CG  1 
ATOM   1019  C  CD  . LYS A  1 163 ? 91.500  50.415  -11.915 1.00 48.43 ? 136 LYS A CD  1 
ATOM   1020  C  CE  . LYS A  1 163 ? 92.281  51.243  -10.925 1.00 55.89 ? 136 LYS A CE  1 
ATOM   1021  N  NZ  . LYS A  1 163 ? 91.979  50.798  -9.531  1.00 52.75 ? 136 LYS A NZ  1 
ATOM   1022  N  N   . THR A  1 164 ? 89.040  48.024  -15.754 1.00 33.50 ? 137 THR A N   1 
ATOM   1023  C  CA  . THR A  1 164 ? 88.005  47.727  -16.727 1.00 32.23 ? 137 THR A CA  1 
ATOM   1024  C  C   . THR A  1 164 ? 87.992  46.283  -17.197 1.00 32.07 ? 137 THR A C   1 
ATOM   1025  O  O   . THR A  1 164 ? 87.110  45.919  -17.978 1.00 29.66 ? 137 THR A O   1 
ATOM   1026  C  CB  . THR A  1 164 ? 88.176  48.600  -17.974 1.00 37.38 ? 137 THR A CB  1 
ATOM   1027  O  OG1 . THR A  1 164 ? 89.329  48.139  -18.690 1.00 35.98 ? 137 THR A OG1 1 
ATOM   1028  C  CG2 . THR A  1 164 ? 88.366  50.073  -17.595 1.00 38.31 ? 137 THR A CG2 1 
ATOM   1029  N  N   . GLY A  1 165 ? 88.965  45.468  -16.808 1.00 31.51 ? 138 GLY A N   1 
ATOM   1030  C  CA  . GLY A  1 165 ? 88.998  44.114  -17.315 1.00 25.71 ? 138 GLY A CA  1 
ATOM   1031  C  C   . GLY A  1 165 ? 89.489  43.975  -18.735 1.00 29.22 ? 138 GLY A C   1 
ATOM   1032  O  O   . GLY A  1 165 ? 89.355  42.887  -19.313 1.00 27.70 ? 138 GLY A O   1 
ATOM   1033  N  N   . ASN A  1 166 ? 90.038  45.042  -19.320 1.00 33.30 ? 139 ASN A N   1 
ATOM   1034  C  CA  . ASN A  1 166 ? 90.487  45.042  -20.712 1.00 36.80 ? 139 ASN A CA  1 
ATOM   1035  C  C   . ASN A  1 166 ? 89.360  44.723  -21.687 1.00 32.81 ? 139 ASN A C   1 
ATOM   1036  O  O   . ASN A  1 166 ? 89.600  44.153  -22.753 1.00 28.81 ? 139 ASN A O   1 
ATOM   1037  C  CB  . ASN A  1 166 ? 91.652  44.070  -20.922 1.00 34.22 ? 139 ASN A CB  1 
ATOM   1038  C  CG  . ASN A  1 166 ? 92.933  44.586  -20.335 1.00 36.95 ? 139 ASN A CG  1 
ATOM   1039  O  OD1 . ASN A  1 166 ? 93.526  45.515  -20.871 1.00 42.16 ? 139 ASN A OD1 1 
ATOM   1040  N  ND2 . ASN A  1 166 ? 93.361  44.009  -19.212 1.00 35.38 ? 139 ASN A ND2 1 
ATOM   1041  N  N   . ALA A  1 167 ? 88.121  45.086  -21.344 1.00 29.82 ? 140 ALA A N   1 
ATOM   1042  C  CA  . ALA A  1 167 ? 87.001  44.773  -22.222 1.00 25.49 ? 140 ALA A CA  1 
ATOM   1043  C  C   . ALA A  1 167 ? 86.912  45.709  -23.412 1.00 23.41 ? 140 ALA A C   1 
ATOM   1044  O  O   . ALA A  1 167 ? 86.069  45.495  -24.292 1.00 25.84 ? 140 ALA A O   1 
ATOM   1045  C  CB  . ALA A  1 167 ? 85.680  44.804  -21.440 1.00 26.19 ? 140 ALA A CB  1 
ATOM   1046  N  N   . GLY A  1 168 ? 87.722  46.763  -23.447 1.00 25.81 ? 141 GLY A N   1 
ATOM   1047  C  CA  . GLY A  1 168 ? 87.777  47.598  -24.629 1.00 27.80 ? 141 GLY A CA  1 
ATOM   1048  C  C   . GLY A  1 168 ? 86.601  48.555  -24.745 1.00 31.89 ? 141 GLY A C   1 
ATOM   1049  O  O   . GLY A  1 168 ? 85.967  48.941  -23.756 1.00 31.89 ? 141 GLY A O   1 
ATOM   1050  N  N   . SER A  1 169 ? 86.298  48.918  -25.986 1.00 23.48 ? 142 SER A N   1 
ATOM   1051  C  CA  . SER A  1 169 ? 85.432  50.052  -26.254 1.00 31.36 ? 142 SER A CA  1 
ATOM   1052  C  C   . SER A  1 169 ? 83.968  49.705  -25.973 1.00 28.60 ? 142 SER A C   1 
ATOM   1053  O  O   . SER A  1 169 ? 83.581  48.542  -25.827 1.00 24.57 ? 142 SER A O   1 
ATOM   1054  C  CB  . SER A  1 169 ? 85.603  50.508  -27.695 1.00 34.58 ? 142 SER A CB  1 
ATOM   1055  O  OG  . SER A  1 169 ? 85.005  49.556  -28.533 1.00 40.36 ? 142 SER A OG  1 
ATOM   1056  N  N   . ARG A  1 170 ? 83.143  50.742  -25.915 1.00 27.24 ? 143 ARG A N   1 
ATOM   1057  C  CA  . ARG A  1 170 ? 81.738  50.618  -25.544 1.00 26.10 ? 143 ARG A CA  1 
ATOM   1058  C  C   . ARG A  1 170 ? 80.910  50.524  -26.814 1.00 24.44 ? 143 ARG A C   1 
ATOM   1059  O  O   . ARG A  1 170 ? 80.784  51.503  -27.557 1.00 30.06 ? 143 ARG A O   1 
ATOM   1060  C  CB  . ARG A  1 170 ? 81.318  51.809  -24.682 1.00 23.76 ? 143 ARG A CB  1 
ATOM   1061  C  CG  . ARG A  1 170 ? 82.295  52.037  -23.539 1.00 24.06 ? 143 ARG A CG  1 
ATOM   1062  C  CD  . ARG A  1 170 ? 81.982  53.238  -22.645 1.00 23.31 ? 143 ARG A CD  1 
ATOM   1063  N  NE  . ARG A  1 170 ? 82.991  53.291  -21.590 1.00 23.70 ? 143 ARG A NE  1 
ATOM   1064  C  CZ  . ARG A  1 170 ? 82.963  54.083  -20.526 1.00 31.49 ? 143 ARG A CZ  1 
ATOM   1065  N  NH1 . ARG A  1 170 ? 81.987  54.956  -20.336 1.00 24.87 ? 143 ARG A NH1 1 
ATOM   1066  N  NH2 . ARG A  1 170 ? 83.940  53.995  -19.625 1.00 24.52 ? 143 ARG A NH2 1 
ATOM   1067  N  N   . LEU A  1 171 ? 80.314  49.355  -27.042 1.00 22.75 ? 144 LEU A N   1 
ATOM   1068  C  CA  . LEU A  1 171 ? 79.595  49.104  -28.281 1.00 19.21 ? 144 LEU A CA  1 
ATOM   1069  C  C   . LEU A  1 171 ? 78.177  49.639  -28.234 1.00 20.44 ? 144 LEU A C   1 
ATOM   1070  O  O   . LEU A  1 171 ? 77.676  50.154  -29.238 1.00 19.17 ? 144 LEU A O   1 
ATOM   1071  C  CB  . LEU A  1 171 ? 79.562  47.602  -28.566 1.00 24.83 ? 144 LEU A CB  1 
ATOM   1072  C  CG  . LEU A  1 171 ? 80.926  46.944  -28.792 1.00 21.96 ? 144 LEU A CG  1 
ATOM   1073  C  CD1 . LEU A  1 171 ? 80.697  45.573  -29.410 1.00 26.58 ? 144 LEU A CD1 1 
ATOM   1074  C  CD2 . LEU A  1 171 ? 81.771  47.804  -29.712 1.00 28.17 ? 144 LEU A CD2 1 
ATOM   1075  N  N   . ALA A  1 172 ? 77.495  49.476  -27.098 1.00 22.69 ? 145 ALA A N   1 
ATOM   1076  C  CA  . ALA A  1 172 ? 76.132  49.969  -26.951 1.00 16.63 ? 145 ALA A CA  1 
ATOM   1077  C  C   . ALA A  1 172 ? 75.851  50.148  -25.465 1.00 16.11 ? 145 ALA A C   1 
ATOM   1078  O  O   . ALA A  1 172 ? 76.475  49.503  -24.614 1.00 17.67 ? 145 ALA A O   1 
ATOM   1079  C  CB  . ALA A  1 172 ? 75.092  49.028  -27.582 1.00 17.64 ? 145 ALA A CB  1 
ATOM   1080  N  N   . CYS A  1 173 ? 74.887  51.012  -25.174 1.00 17.78 ? 146 CYS A N   1 
ATOM   1081  C  CA  . CYS A  1 173 ? 74.534  51.273  -23.782 1.00 16.09 ? 146 CYS A CA  1 
ATOM   1082  C  C   . CYS A  1 173 ? 73.127  51.847  -23.711 1.00 17.81 ? 146 CYS A C   1 
ATOM   1083  O  O   . CYS A  1 173 ? 72.524  52.223  -24.725 1.00 15.26 ? 146 CYS A O   1 
ATOM   1084  C  CB  . CYS A  1 173 ? 75.528  52.239  -23.137 1.00 15.79 ? 146 CYS A CB  1 
ATOM   1085  S  SG  . CYS A  1 173 ? 75.591  53.823  -23.998 1.00 27.49 ? 146 CYS A SG  1 
ATOM   1086  N  N   . GLY A  1 174 ? 72.628  51.948  -22.479 1.00 13.42 ? 147 GLY A N   1 
ATOM   1087  C  CA  . GLY A  1 174 ? 71.368  52.627  -22.233 1.00 18.15 ? 147 GLY A CA  1 
ATOM   1088  C  C   . GLY A  1 174 ? 71.215  52.881  -20.752 1.00 15.46 ? 147 GLY A C   1 
ATOM   1089  O  O   . GLY A  1 174 ? 71.861  52.230  -19.926 1.00 17.56 ? 147 GLY A O   1 
ATOM   1090  N  N   . VAL A  1 175 ? 70.358  53.840  -20.425 1.00 15.76 ? 148 VAL A N   1 
ATOM   1091  C  CA  . VAL A  1 175 ? 70.065  54.113  -19.016 1.00 16.64 ? 148 VAL A CA  1 
ATOM   1092  C  C   . VAL A  1 175 ? 69.094  53.071  -18.488 1.00 14.88 ? 148 VAL A C   1 
ATOM   1093  O  O   . VAL A  1 175 ? 68.110  52.729  -19.149 1.00 18.22 ? 148 VAL A O   1 
ATOM   1094  C  CB  . VAL A  1 175 ? 69.502  55.535  -18.851 1.00 16.81 ? 148 VAL A CB  1 
ATOM   1095  C  CG1 . VAL A  1 175 ? 69.326  55.863  -17.364 1.00 18.67 ? 148 VAL A CG1 1 
ATOM   1096  C  CG2 . VAL A  1 175 ? 70.435  56.531  -19.518 1.00 19.28 ? 148 VAL A CG2 1 
ATOM   1097  N  N   . ILE A  1 176 ? 69.339  52.589  -17.272 1.00 15.44 ? 149 ILE A N   1 
ATOM   1098  C  CA  . ILE A  1 176 ? 68.472  51.586  -16.662 1.00 17.54 ? 149 ILE A CA  1 
ATOM   1099  C  C   . ILE A  1 176 ? 67.266  52.290  -16.054 1.00 17.56 ? 149 ILE A C   1 
ATOM   1100  O  O   . ILE A  1 176 ? 67.413  53.155  -15.181 1.00 20.36 ? 149 ILE A O   1 
ATOM   1101  C  CB  . ILE A  1 176 ? 69.239  50.779  -15.605 1.00 20.02 ? 149 ILE A CB  1 
ATOM   1102  C  CG1 . ILE A  1 176 ? 70.464  50.106  -16.246 1.00 17.76 ? 149 ILE A CG1 1 
ATOM   1103  C  CG2 . ILE A  1 176 ? 68.345  49.751  -14.907 1.00 18.27 ? 149 ILE A CG2 1 
ATOM   1104  C  CD1 . ILE A  1 176 ? 71.406  49.517  -15.198 1.00 15.29 ? 149 ILE A CD1 1 
ATOM   1105  N  N   . GLY A  1 177 ? 66.077  51.925  -16.508 1.00 16.87 ? 150 GLY A N   1 
ATOM   1106  C  CA  . GLY A  1 177 ? 64.871  52.635  -16.101 1.00 16.62 ? 150 GLY A CA  1 
ATOM   1107  C  C   . GLY A  1 177 ? 63.907  51.765  -15.325 1.00 19.62 ? 150 GLY A C   1 
ATOM   1108  O  O   . GLY A  1 177 ? 63.930  50.541  -15.467 1.00 16.38 ? 150 GLY A O   1 
ATOM   1109  N  N   A ILE A  1 178 ? 63.042  52.391  -14.519 0.53 17.36 ? 151 ILE A N   1 
ATOM   1110  N  N   B ILE A  1 178 ? 63.060  52.371  -14.489 0.47 17.37 ? 151 ILE A N   1 
ATOM   1111  C  CA  A ILE A  1 178 ? 62.023  51.657  -13.780 0.53 19.09 ? 151 ILE A CA  1 
ATOM   1112  C  CA  B ILE A  1 178 ? 62.089  51.584  -13.742 0.47 19.10 ? 151 ILE A CA  1 
ATOM   1113  C  C   A ILE A  1 178 ? 61.003  51.076  -14.747 0.53 21.49 ? 151 ILE A C   1 
ATOM   1114  C  C   B ILE A  1 178 ? 61.013  51.081  -14.695 0.47 21.45 ? 151 ILE A C   1 
ATOM   1115  O  O   A ILE A  1 178 ? 60.584  51.732  -15.714 0.53 18.94 ? 151 ILE A O   1 
ATOM   1116  O  O   B ILE A  1 178 ? 60.585  51.789  -15.620 0.47 19.03 ? 151 ILE A O   1 
ATOM   1117  C  CB  A ILE A  1 178 ? 61.355  52.575  -12.738 0.53 18.04 ? 151 ILE A CB  1 
ATOM   1118  C  CB  B ILE A  1 178 ? 61.499  52.402  -12.574 0.47 18.16 ? 151 ILE A CB  1 
ATOM   1119  C  CG1 A ILE A  1 178 ? 62.426  53.193  -11.841 0.53 17.69 ? 151 ILE A CG1 1 
ATOM   1120  C  CG1 B ILE A  1 178 ? 60.606  51.524  -11.693 0.47 23.56 ? 151 ILE A CG1 1 
ATOM   1121  C  CG2 A ILE A  1 178 ? 60.317  51.802  -11.927 0.53 24.47 ? 151 ILE A CG2 1 
ATOM   1122  C  CG2 B ILE A  1 178 ? 60.717  53.592  -13.073 0.47 18.22 ? 151 ILE A CG2 1 
ATOM   1123  C  CD1 A ILE A  1 178 ? 61.887  54.187  -10.808 0.53 24.79 ? 151 ILE A CD1 1 
ATOM   1124  C  CD1 B ILE A  1 178 ? 60.217  52.195  -10.391 0.47 26.60 ? 151 ILE A CD1 1 
ATOM   1125  N  N   . ALA A  1 179 ? 60.604  49.831  -14.505 1.00 19.53 ? 152 ALA A N   1 
ATOM   1126  C  CA  . ALA A  1 179 ? 59.705  49.144  -15.421 1.00 21.28 ? 152 ALA A CA  1 
ATOM   1127  C  C   . ALA A  1 179 ? 58.452  48.694  -14.686 1.00 25.94 ? 152 ALA A C   1 
ATOM   1128  O  O   . ALA A  1 179 ? 58.446  48.535  -13.462 1.00 22.52 ? 152 ALA A O   1 
ATOM   1129  C  CB  . ALA A  1 179 ? 60.381  47.939  -16.083 1.00 23.18 ? 152 ALA A CB  1 
ATOM   1130  N  N   . GLN A  1 180 ? 57.380  48.509  -15.454 1.00 27.66 ? 153 GLN A N   1 
ATOM   1131  C  CA  . GLN A  1 180 ? 56.098  48.096  -14.889 1.00 34.84 ? 153 GLN A CA  1 
ATOM   1132  C  C   . GLN A  1 180 ? 56.122  46.646  -14.419 1.00 49.36 ? 153 GLN A C   1 
ATOM   1133  O  O   . GLN A  1 180 ? 56.613  45.760  -15.130 1.00 49.91 ? 153 GLN A O   1 
ATOM   1134  C  CB  . GLN A  1 180 ? 54.977  48.274  -15.909 1.00 31.34 ? 153 GLN A CB  1 
ATOM   1135  C  CG  . GLN A  1 180 ? 53.595  47.928  -15.363 1.00 40.93 ? 153 GLN A CG  1 
ATOM   1136  C  CD  . GLN A  1 180 ? 52.492  48.525  -16.218 1.00 47.32 ? 153 GLN A CD  1 
ATOM   1137  O  OE1 . GLN A  1 180 ? 51.571  49.171  -15.714 1.00 55.46 ? 153 GLN A OE1 1 
ATOM   1138  N  NE2 . GLN A  1 180 ? 52.603  48.338  -17.526 1.00 48.13 ? 153 GLN A NE2 1 
ATOM   1139  O  OXT . GLN A  1 180 ? 55.633  46.336  -13.329 1.00 56.53 ? 153 GLN A OXT 1 
ATOM   1140  N  N   . MET B  1 27  ? 71.185  60.294  -2.696  1.00 56.36 ? 0   MET B N   1 
ATOM   1141  C  CA  . MET B  1 27  ? 72.337  61.181  -2.574  1.00 51.19 ? 0   MET B CA  1 
ATOM   1142  C  C   . MET B  1 27  ? 72.572  61.953  -3.877  1.00 48.85 ? 0   MET B C   1 
ATOM   1143  O  O   . MET B  1 27  ? 73.427  62.842  -3.922  1.00 47.51 ? 0   MET B O   1 
ATOM   1144  C  CB  . MET B  1 27  ? 73.602  60.379  -2.182  1.00 42.16 ? 0   MET B CB  1 
ATOM   1145  N  N   . ALA B  1 28  ? 71.816  61.613  -4.927  1.00 48.27 ? 1   ALA B N   1 
ATOM   1146  C  CA  . ALA B  1 28  ? 71.981  62.261  -6.228  1.00 35.35 ? 1   ALA B CA  1 
ATOM   1147  C  C   . ALA B  1 28  ? 71.615  63.739  -6.153  1.00 29.56 ? 1   ALA B C   1 
ATOM   1148  O  O   . ALA B  1 28  ? 70.532  64.096  -5.682  1.00 37.29 ? 1   ALA B O   1 
ATOM   1149  C  CB  . ALA B  1 28  ? 71.120  61.569  -7.286  1.00 37.63 ? 1   ALA B CB  1 
ATOM   1150  N  N   . THR B  1 29  ? 72.517  64.606  -6.609  1.00 27.52 ? 2   THR B N   1 
ATOM   1151  C  CA  . THR B  1 29  ? 72.185  66.016  -6.713  1.00 27.23 ? 2   THR B CA  1 
ATOM   1152  C  C   . THR B  1 29  ? 72.018  66.468  -8.150  1.00 22.66 ? 2   THR B C   1 
ATOM   1153  O  O   . THR B  1 29  ? 71.604  67.611  -8.374  1.00 20.64 ? 2   THR B O   1 
ATOM   1154  C  CB  . THR B  1 29  ? 73.261  66.894  -6.069  1.00 31.16 ? 2   THR B CB  1 
ATOM   1155  O  OG1 . THR B  1 29  ? 74.547  66.385  -6.414  1.00 35.19 ? 2   THR B OG1 1 
ATOM   1156  C  CG2 . THR B  1 29  ? 73.116  66.847  -4.549  1.00 35.02 ? 2   THR B CG2 1 
ATOM   1157  N  N   . LYS B  1 30  ? 72.395  65.636  -9.118  1.00 23.11 ? 3   LYS B N   1 
ATOM   1158  C  CA  . LYS B  1 30  ? 72.317  65.994  -10.531 1.00 20.03 ? 3   LYS B CA  1 
ATOM   1159  C  C   . LYS B  1 30  ? 71.831  64.804  -11.335 1.00 14.39 ? 3   LYS B C   1 
ATOM   1160  O  O   . LYS B  1 30  ? 72.186  63.655  -11.055 1.00 16.92 ? 3   LYS B O   1 
ATOM   1161  C  CB  . LYS B  1 30  ? 73.665  66.469  -11.108 1.00 20.97 ? 3   LYS B CB  1 
ATOM   1162  C  CG  . LYS B  1 30  ? 74.267  67.685  -10.387 1.00 34.74 ? 3   LYS B CG  1 
ATOM   1163  C  CD  . LYS B  1 30  ? 75.573  68.130  -11.048 1.00 37.25 ? 3   LYS B CD  1 
ATOM   1164  C  CE  . LYS B  1 30  ? 75.346  68.813  -12.376 1.00 36.34 ? 3   LYS B CE  1 
ATOM   1165  N  NZ  . LYS B  1 30  ? 76.633  68.957  -13.144 1.00 45.49 ? 3   LYS B NZ  1 
ATOM   1166  N  N   . ALA B  1 31  ? 71.051  65.106  -12.359 1.00 17.30 ? 4   ALA B N   1 
ATOM   1167  C  CA  . ALA B  1 31  ? 70.535  64.111  -13.274 1.00 18.12 ? 4   ALA B CA  1 
ATOM   1168  C  C   . ALA B  1 31  ? 70.539  64.723  -14.660 1.00 13.42 ? 4   ALA B C   1 
ATOM   1169  O  O   . ALA B  1 31  ? 70.670  65.938  -14.823 1.00 15.01 ? 4   ALA B O   1 
ATOM   1170  C  CB  . ALA B  1 31  ? 69.123  63.655  -12.901 1.00 17.54 ? 4   ALA B CB  1 
ATOM   1171  N  N   . VAL B  1 32  ? 70.374  63.875  -15.671 1.00 14.05 ? 5   VAL B N   1 
ATOM   1172  C  CA  . VAL B  1 32  ? 70.389  64.346  -17.056 1.00 15.66 ? 5   VAL B CA  1 
ATOM   1173  C  C   . VAL B  1 32  ? 69.555  63.400  -17.910 1.00 13.66 ? 5   VAL B C   1 
ATOM   1174  O  O   . VAL B  1 32  ? 69.357  62.231  -17.576 1.00 15.28 ? 5   VAL B O   1 
ATOM   1175  C  CB  . VAL B  1 32  ? 71.843  64.472  -17.577 1.00 16.86 ? 5   VAL B CB  1 
ATOM   1176  C  CG1 . VAL B  1 32  ? 72.468  63.103  -17.725 1.00 20.07 ? 5   VAL B CG1 1 
ATOM   1177  C  CG2 . VAL B  1 32  ? 71.913  65.249  -18.902 1.00 18.62 ? 5   VAL B CG2 1 
ATOM   1178  N  N   . CYS B  1 33  ? 69.049  63.927  -19.020 1.00 16.69 ? 6   CYS B N   1 
ATOM   1179  C  CA  . CYS B  1 33  ? 68.145  63.179  -19.869 1.00 16.84 ? 6   CYS B CA  1 
ATOM   1180  C  C   . CYS B  1 33  ? 68.423  63.577  -21.307 1.00 16.72 ? 6   CYS B C   1 
ATOM   1181  O  O   . CYS B  1 33  ? 68.441  64.767  -21.609 1.00 15.73 ? 6   CYS B O   1 
ATOM   1182  C  CB  . CYS B  1 33  ? 66.688  63.490  -19.506 1.00 17.48 ? 6   CYS B CB  1 
ATOM   1183  S  SG  . CYS B  1 33  ? 65.505  62.571  -20.484 1.00 22.38 ? 6   CYS B SG  1 
ATOM   1184  N  N   . VAL B  1 34  ? 68.632  62.601  -22.182 1.00 15.21 ? 7   VAL B N   1 
ATOM   1185  C  CA  . VAL B  1 34  ? 68.769  62.871  -23.614 1.00 14.31 ? 7   VAL B CA  1 
ATOM   1186  C  C   . VAL B  1 34  ? 67.449  62.525  -24.278 1.00 15.24 ? 7   VAL B C   1 
ATOM   1187  O  O   . VAL B  1 34  ? 67.014  61.372  -24.228 1.00 15.87 ? 7   VAL B O   1 
ATOM   1188  C  CB  . VAL B  1 34  ? 69.922  62.071  -24.236 1.00 19.30 ? 7   VAL B CB  1 
ATOM   1189  C  CG1 . VAL B  1 34  ? 69.987  62.343  -25.753 1.00 20.11 ? 7   VAL B CG1 1 
ATOM   1190  C  CG2 . VAL B  1 34  ? 71.236  62.440  -23.553 1.00 21.51 ? 7   VAL B CG2 1 
ATOM   1191  N  N   . LEU B  1 35  ? 66.811  63.521  -24.891 1.00 15.34 ? 8   LEU B N   1 
ATOM   1192  C  CA  . LEU B  1 35  ? 65.505  63.340  -25.503 1.00 16.19 ? 8   LEU B CA  1 
ATOM   1193  C  C   . LEU B  1 35  ? 65.719  62.971  -26.968 1.00 14.07 ? 8   LEU B C   1 
ATOM   1194  O  O   . LEU B  1 35  ? 66.450  63.663  -27.672 1.00 16.50 ? 8   LEU B O   1 
ATOM   1195  C  CB  . LEU B  1 35  ? 64.696  64.633  -25.412 1.00 16.50 ? 8   LEU B CB  1 
ATOM   1196  C  CG  . LEU B  1 35  ? 64.256  65.083  -24.008 1.00 23.62 ? 8   LEU B CG  1 
ATOM   1197  C  CD1 . LEU B  1 35  ? 63.511  66.411  -24.118 1.00 30.90 ? 8   LEU B CD1 1 
ATOM   1198  C  CD2 . LEU B  1 35  ? 63.338  64.071  -23.418 1.00 21.64 ? 8   LEU B CD2 1 
ATOM   1199  N  N   . LYS B  1 36  ? 65.079  61.898  -27.406 1.00 13.42 ? 9   LYS B N   1 
ATOM   1200  C  CA  . LYS B  1 36  ? 65.112  61.455  -28.795 1.00 22.52 ? 9   LYS B CA  1 
ATOM   1201  C  C   . LYS B  1 36  ? 63.745  60.910  -29.161 1.00 20.10 ? 9   LYS B C   1 
ATOM   1202  O  O   . LYS B  1 36  ? 63.016  60.392  -28.315 1.00 21.95 ? 9   LYS B O   1 
ATOM   1203  C  CB  . LYS B  1 36  ? 66.147  60.339  -29.025 1.00 26.18 ? 9   LYS B CB  1 
ATOM   1204  C  CG  . LYS B  1 36  ? 67.594  60.743  -28.804 1.00 40.70 ? 9   LYS B CG  1 
ATOM   1205  C  CD  . LYS B  1 36  ? 68.518  59.530  -28.924 1.00 51.65 ? 9   LYS B CD  1 
ATOM   1206  C  CE  . LYS B  1 36  ? 69.983  59.904  -28.678 1.00 48.80 ? 9   LYS B CE  1 
ATOM   1207  N  NZ  . LYS B  1 36  ? 70.587  59.105  -27.562 1.00 50.63 ? 9   LYS B NZ  1 
ATOM   1208  N  N   . GLY B  1 37  ? 63.433  60.940  -30.446 1.00 23.14 ? 10  GLY B N   1 
ATOM   1209  C  CA  . GLY B  1 37  ? 62.215  60.307  -30.893 1.00 21.97 ? 10  GLY B CA  1 
ATOM   1210  C  C   . GLY B  1 37  ? 62.280  59.992  -32.381 1.00 30.70 ? 10  GLY B C   1 
ATOM   1211  O  O   . GLY B  1 37  ? 63.358  59.953  -32.971 1.00 25.72 ? 10  GLY B O   1 
ATOM   1212  N  N   . ASP B  1 38  ? 61.103  59.784  -32.971 1.00 31.90 ? 11  ASP B N   1 
ATOM   1213  C  CA  . ASP B  1 38  ? 61.015  59.388  -34.381 1.00 42.76 ? 11  ASP B CA  1 
ATOM   1214  C  C   . ASP B  1 38  ? 61.349  60.534  -35.326 1.00 39.29 ? 11  ASP B C   1 
ATOM   1215  O  O   . ASP B  1 38  ? 61.943  60.322  -36.390 1.00 49.37 ? 11  ASP B O   1 
ATOM   1216  C  CB  . ASP B  1 38  ? 59.610  58.881  -34.678 1.00 40.74 ? 11  ASP B CB  1 
ATOM   1217  C  CG  . ASP B  1 38  ? 59.290  57.620  -33.933 1.00 52.17 ? 11  ASP B CG  1 
ATOM   1218  O  OD1 . ASP B  1 38  ? 60.209  56.788  -33.769 1.00 57.37 ? 11  ASP B OD1 1 
ATOM   1219  O  OD2 . ASP B  1 38  ? 58.132  57.480  -33.483 1.00 67.85 ? 11  ASP B OD2 1 
ATOM   1220  N  N   . GLY B  1 39  ? 60.944  61.742  -34.983 1.00 32.24 ? 12  GLY B N   1 
ATOM   1221  C  CA  . GLY B  1 39  ? 61.105  62.872  -35.859 1.00 30.71 ? 12  GLY B CA  1 
ATOM   1222  C  C   . GLY B  1 39  ? 62.357  63.648  -35.541 1.00 28.20 ? 12  GLY B C   1 
ATOM   1223  O  O   . GLY B  1 39  ? 63.348  63.099  -35.059 1.00 33.14 ? 12  GLY B O   1 
ATOM   1224  N  N   . PRO B  1 40  ? 62.330  64.955  -35.815 1.00 24.99 ? 13  PRO B N   1 
ATOM   1225  C  CA  . PRO B  1 40  ? 63.519  65.793  -35.609 1.00 25.79 ? 13  PRO B CA  1 
ATOM   1226  C  C   . PRO B  1 40  ? 63.732  66.268  -34.179 1.00 23.27 ? 13  PRO B C   1 
ATOM   1227  O  O   . PRO B  1 40  ? 64.730  66.958  -33.919 1.00 24.91 ? 13  PRO B O   1 
ATOM   1228  C  CB  . PRO B  1 40  ? 63.245  66.998  -36.508 1.00 27.11 ? 13  PRO B CB  1 
ATOM   1229  C  CG  . PRO B  1 40  ? 61.741  67.115  -36.506 1.00 29.09 ? 13  PRO B CG  1 
ATOM   1230  C  CD  . PRO B  1 40  ? 61.189  65.715  -36.361 1.00 28.80 ? 13  PRO B CD  1 
ATOM   1231  N  N   . VAL B  1 41  ? 62.825  65.983  -33.263 1.00 23.62 ? 14  VAL B N   1 
ATOM   1232  C  CA  . VAL B  1 41  ? 62.913  66.593  -31.934 1.00 22.48 ? 14  VAL B CA  1 
ATOM   1233  C  C   . VAL B  1 41  ? 64.011  65.907  -31.129 1.00 20.57 ? 14  VAL B C   1 
ATOM   1234  O  O   . VAL B  1 41  ? 64.014  64.679  -30.990 1.00 22.59 ? 14  VAL B O   1 
ATOM   1235  C  CB  . VAL B  1 41  ? 61.561  66.523  -31.217 1.00 20.36 ? 14  VAL B CB  1 
ATOM   1236  C  CG1 . VAL B  1 41  ? 61.655  67.206  -29.827 1.00 19.95 ? 14  VAL B CG1 1 
ATOM   1237  C  CG2 . VAL B  1 41  ? 60.525  67.237  -32.049 1.00 22.44 ? 14  VAL B CG2 1 
ATOM   1238  N  N   . GLN B  1 42  ? 64.949  66.696  -30.598 1.00 23.76 ? 15  GLN B N   1 
ATOM   1239  C  CA  . GLN B  1 42  ? 65.984  66.131  -29.737 1.00 21.94 ? 15  GLN B CA  1 
ATOM   1240  C  C   . GLN B  1 42  ? 66.496  67.194  -28.785 1.00 17.02 ? 15  GLN B C   1 
ATOM   1241  O  O   . GLN B  1 42  ? 66.459  68.389  -29.079 1.00 23.12 ? 15  GLN B O   1 
ATOM   1242  C  CB  . GLN B  1 42  ? 67.181  65.595  -30.523 1.00 26.70 ? 15  GLN B CB  1 
ATOM   1243  C  CG  . GLN B  1 42  ? 67.691  66.557  -31.549 1.00 32.52 ? 15  GLN B CG  1 
ATOM   1244  C  CD  . GLN B  1 42  ? 68.931  66.033  -32.266 1.00 51.19 ? 15  GLN B CD  1 
ATOM   1245  O  OE1 . GLN B  1 42  ? 68.830  65.272  -33.227 1.00 52.22 ? 15  GLN B OE1 1 
ATOM   1246  N  NE2 . GLN B  1 42  ? 70.109  66.416  -31.773 1.00 48.71 ? 15  GLN B NE2 1 
ATOM   1247  N  N   . GLY B  1 43  ? 67.017  66.749  -27.651 1.00 20.49 ? 16  GLY B N   1 
ATOM   1248  C  CA  . GLY B  1 43  ? 67.550  67.718  -26.717 1.00 20.95 ? 16  GLY B CA  1 
ATOM   1249  C  C   . GLY B  1 43  ? 68.224  67.044  -25.548 1.00 19.14 ? 16  GLY B C   1 
ATOM   1250  O  O   . GLY B  1 43  ? 68.277  65.814  -25.441 1.00 16.03 ? 16  GLY B O   1 
ATOM   1251  N  N   . ILE B  1 44  ? 68.757  67.888  -24.677 1.00 16.49 ? 17  ILE B N   1 
ATOM   1252  C  CA  . ILE B  1 44  ? 69.401  67.465  -23.449 1.00 13.42 ? 17  ILE B CA  1 
ATOM   1253  C  C   . ILE B  1 44  ? 68.828  68.321  -22.341 1.00 16.26 ? 17  ILE B C   1 
ATOM   1254  O  O   . ILE B  1 44  ? 68.837  69.552  -22.449 1.00 15.91 ? 17  ILE B O   1 
ATOM   1255  C  CB  . ILE B  1 44  ? 70.933  67.635  -23.520 1.00 16.77 ? 17  ILE B CB  1 
ATOM   1256  C  CG1 . ILE B  1 44  ? 71.534  66.731  -24.609 1.00 23.14 ? 17  ILE B CG1 1 
ATOM   1257  C  CG2 . ILE B  1 44  ? 71.551  67.382  -22.167 1.00 21.36 ? 17  ILE B CG2 1 
ATOM   1258  C  CD1 . ILE B  1 44  ? 73.061  66.929  -24.804 1.00 23.52 ? 17  ILE B CD1 1 
ATOM   1259  N  N   . ILE B  1 45  ? 68.341  67.679  -21.282 1.00 15.37 ? 18  ILE B N   1 
ATOM   1260  C  CA  . ILE B  1 45  ? 67.747  68.384  -20.156 1.00 13.42 ? 18  ILE B CA  1 
ATOM   1261  C  C   . ILE B  1 45  ? 68.513  67.982  -18.905 1.00 16.28 ? 18  ILE B C   1 
ATOM   1262  O  O   . ILE B  1 45  ? 68.705  66.787  -18.648 1.00 16.39 ? 18  ILE B O   1 
ATOM   1263  C  CB  . ILE B  1 45  ? 66.248  68.067  -20.003 1.00 19.31 ? 18  ILE B CB  1 
ATOM   1264  C  CG1 . ILE B  1 45  ? 65.445  68.562  -21.219 1.00 13.52 ? 18  ILE B CG1 1 
ATOM   1265  C  CG2 . ILE B  1 45  ? 65.711  68.695  -18.714 1.00 15.58 ? 18  ILE B CG2 1 
ATOM   1266  C  CD1 . ILE B  1 45  ? 65.483  70.083  -21.410 1.00 15.60 ? 18  ILE B CD1 1 
ATOM   1267  N  N   . ASN B  1 46  ? 68.933  68.978  -18.132 1.00 15.43 ? 19  ASN B N   1 
ATOM   1268  C  CA  . ASN B  1 46  ? 69.667  68.787  -16.890 1.00 16.78 ? 19  ASN B CA  1 
ATOM   1269  C  C   . ASN B  1 46  ? 68.734  69.010  -15.710 1.00 15.10 ? 19  ASN B C   1 
ATOM   1270  O  O   . ASN B  1 46  ? 67.782  69.786  -15.803 1.00 16.27 ? 19  ASN B O   1 
ATOM   1271  C  CB  . ASN B  1 46  ? 70.851  69.754  -16.803 1.00 19.79 ? 19  ASN B CB  1 
ATOM   1272  C  CG  . ASN B  1 46  ? 71.785  69.632  -17.990 1.00 23.43 ? 19  ASN B CG  1 
ATOM   1273  O  OD1 . ASN B  1 46  ? 72.528  68.669  -18.076 1.00 23.11 ? 19  ASN B OD1 1 
ATOM   1274  N  ND2 . ASN B  1 46  ? 71.734  70.592  -18.916 1.00 23.55 ? 19  ASN B ND2 1 
ATOM   1275  N  N   . PHE B  1 47  ? 69.009  68.303  -14.605 1.00 15.98 ? 20  PHE B N   1 
ATOM   1276  C  CA  . PHE B  1 47  ? 68.290  68.446  -13.344 1.00 13.88 ? 20  PHE B CA  1 
ATOM   1277  C  C   . PHE B  1 47  ? 69.308  68.640  -12.239 1.00 21.37 ? 20  PHE B C   1 
ATOM   1278  O  O   . PHE B  1 47  ? 70.320  67.933  -12.193 1.00 20.24 ? 20  PHE B O   1 
ATOM   1279  C  CB  . PHE B  1 47  ? 67.450  67.212  -12.991 1.00 16.47 ? 20  PHE B CB  1 
ATOM   1280  C  CG  . PHE B  1 47  ? 66.430  66.846  -14.029 1.00 18.40 ? 20  PHE B CG  1 
ATOM   1281  C  CD1 . PHE B  1 47  ? 66.802  66.139  -15.164 1.00 19.94 ? 20  PHE B CD1 1 
ATOM   1282  C  CD2 . PHE B  1 47  ? 65.101  67.193  -13.855 1.00 16.58 ? 20  PHE B CD2 1 
ATOM   1283  C  CE1 . PHE B  1 47  ? 65.858  65.793  -16.117 1.00 19.77 ? 20  PHE B CE1 1 
ATOM   1284  C  CE2 . PHE B  1 47  ? 64.141  66.838  -14.791 1.00 17.04 ? 20  PHE B CE2 1 
ATOM   1285  C  CZ  . PHE B  1 47  ? 64.523  66.146  -15.925 1.00 18.14 ? 20  PHE B CZ  1 
ATOM   1286  N  N   . GLU B  1 48  ? 69.034  69.575  -11.336 1.00 14.77 ? 21  GLU B N   1 
ATOM   1287  C  CA  . GLU B  1 48  ? 69.968  69.816  -10.243 1.00 17.35 ? 21  GLU B CA  1 
ATOM   1288  C  C   . GLU B  1 48  ? 69.174  70.067  -8.975  1.00 20.25 ? 21  GLU B C   1 
ATOM   1289  O  O   . GLU B  1 48  ? 68.214  70.841  -8.985  1.00 18.00 ? 21  GLU B O   1 
ATOM   1290  C  CB  . GLU B  1 48  ? 70.881  71.000  -10.561 1.00 22.60 ? 21  GLU B CB  1 
ATOM   1291  C  CG  . GLU B  1 48  ? 71.870  71.340  -9.445  1.00 33.86 ? 21  GLU B CG  1 
ATOM   1292  C  CD  . GLU B  1 48  ? 72.723  72.543  -9.795  1.00 49.88 ? 21  GLU B CD  1 
ATOM   1293  O  OE1 . GLU B  1 48  ? 72.785  73.488  -8.979  1.00 58.66 ? 21  GLU B OE1 1 
ATOM   1294  O  OE2 . GLU B  1 48  ? 73.304  72.549  -10.903 1.00 55.06 ? 21  GLU B OE2 1 
ATOM   1295  N  N   . GLN B  1 49  ? 69.574  69.418  -7.885  1.00 18.42 ? 22  GLN B N   1 
ATOM   1296  C  CA  . GLN B  1 49  ? 68.865  69.561  -6.617  1.00 23.86 ? 22  GLN B CA  1 
ATOM   1297  C  C   . GLN B  1 49  ? 69.925  69.592  -5.523  1.00 25.49 ? 22  GLN B C   1 
ATOM   1298  O  O   . GLN B  1 49  ? 70.399  68.537  -5.098  1.00 23.19 ? 22  GLN B O   1 
ATOM   1299  C  CB  . GLN B  1 49  ? 67.892  68.417  -6.412  1.00 17.65 ? 22  GLN B CB  1 
ATOM   1300  C  CG  . GLN B  1 49  ? 67.002  68.615  -5.200  1.00 19.74 ? 22  GLN B CG  1 
ATOM   1301  C  CD  . GLN B  1 49  ? 66.099  67.454  -4.944  1.00 24.41 ? 22  GLN B CD  1 
ATOM   1302  O  OE1 . GLN B  1 49  ? 66.416  66.317  -5.289  1.00 20.84 ? 22  GLN B OE1 1 
ATOM   1303  N  NE2 . GLN B  1 49  ? 64.966  67.720  -4.299  1.00 21.21 ? 22  GLN B NE2 1 
ATOM   1304  N  N   . LYS B  1 50  ? 70.314  70.789  -5.095  1.00 31.73 ? 23  LYS B N   1 
ATOM   1305  C  CA  . LYS B  1 50  ? 71.379  70.883  -4.094  1.00 38.27 ? 23  LYS B CA  1 
ATOM   1306  C  C   . LYS B  1 50  ? 70.940  70.342  -2.734  1.00 36.78 ? 23  LYS B C   1 
ATOM   1307  O  O   . LYS B  1 50  ? 71.754  69.752  -2.018  1.00 36.46 ? 23  LYS B O   1 
ATOM   1308  C  CB  . LYS B  1 50  ? 71.861  72.325  -3.963  1.00 38.75 ? 23  LYS B CB  1 
ATOM   1309  C  CG  . LYS B  1 50  ? 70.762  73.362  -4.058  1.00 47.07 ? 23  LYS B CG  1 
ATOM   1310  C  CD  . LYS B  1 50  ? 71.249  74.742  -3.591  1.00 51.58 ? 23  LYS B CD  1 
ATOM   1311  C  CE  . LYS B  1 50  ? 70.722  75.075  -2.193  1.00 49.63 ? 23  LYS B CE  1 
ATOM   1312  N  NZ  . LYS B  1 50  ? 70.564  76.552  -1.996  1.00 55.04 ? 23  LYS B NZ  1 
ATOM   1313  N  N   . GLU B  1 51  ? 69.671  70.503  -2.367  1.00 30.72 ? 24  GLU B N   1 
ATOM   1314  C  CA  . GLU B  1 51  ? 69.159  70.007  -1.096  1.00 36.33 ? 24  GLU B CA  1 
ATOM   1315  C  C   . GLU B  1 51  ? 68.006  69.046  -1.335  1.00 33.54 ? 24  GLU B C   1 
ATOM   1316  O  O   . GLU B  1 51  ? 67.110  69.339  -2.124  1.00 32.18 ? 24  GLU B O   1 
ATOM   1317  C  CB  . GLU B  1 51  ? 68.673  71.169  -0.213  1.00 37.66 ? 24  GLU B CB  1 
ATOM   1318  C  CG  . GLU B  1 51  ? 69.725  72.226  0.030   1.00 42.93 ? 24  GLU B CG  1 
ATOM   1319  C  CD  . GLU B  1 51  ? 70.851  71.753  0.941   1.00 58.28 ? 24  GLU B CD  1 
ATOM   1320  O  OE1 . GLU B  1 51  ? 71.726  72.583  1.274   1.00 64.56 ? 24  GLU B OE1 1 
ATOM   1321  O  OE2 . GLU B  1 51  ? 70.862  70.562  1.339   1.00 64.03 ? 24  GLU B OE2 1 
ATOM   1322  N  N   . SER B  1 52  ? 67.987  67.923  -0.608  1.00 34.17 ? 25  SER B N   1 
ATOM   1323  C  CA  . SER B  1 52  ? 66.930  66.942  -0.828  1.00 34.36 ? 25  SER B CA  1 
ATOM   1324  C  C   . SER B  1 52  ? 65.551  67.470  -0.440  1.00 39.29 ? 25  SER B C   1 
ATOM   1325  O  O   . SER B  1 52  ? 64.540  66.904  -0.873  1.00 39.29 ? 25  SER B O   1 
ATOM   1326  C  CB  . SER B  1 52  ? 67.224  65.659  -0.057  1.00 38.51 ? 25  SER B CB  1 
ATOM   1327  O  OG  . SER B  1 52  ? 67.295  65.920  1.327   1.00 46.72 ? 25  SER B OG  1 
ATOM   1328  N  N   . ASN B  1 53  ? 65.485  68.535  0.359   1.00 32.06 ? 26  ASN B N   1 
ATOM   1329  C  CA  . ASN B  1 53  ? 64.223  69.188  0.676   1.00 42.43 ? 26  ASN B CA  1 
ATOM   1330  C  C   . ASN B  1 53  ? 63.998  70.454  -0.147  1.00 47.36 ? 26  ASN B C   1 
ATOM   1331  O  O   . ASN B  1 53  ? 63.131  71.263  0.204   1.00 51.09 ? 26  ASN B O   1 
ATOM   1332  C  CB  . ASN B  1 53  ? 64.146  69.526  2.172   1.00 37.28 ? 26  ASN B CB  1 
ATOM   1333  C  CG  . ASN B  1 53  ? 65.164  70.597  2.598   1.00 45.49 ? 26  ASN B CG  1 
ATOM   1334  O  OD1 . ASN B  1 53  ? 66.074  70.950  1.847   1.00 43.33 ? 26  ASN B OD1 1 
ATOM   1335  N  ND2 . ASN B  1 53  ? 64.977  71.147  3.795   1.00 47.38 ? 26  ASN B ND2 1 
ATOM   1336  N  N   . GLY B  1 54  ? 64.768  70.655  -1.218  1.00 35.07 ? 27  GLY B N   1 
ATOM   1337  C  CA  . GLY B  1 54  ? 64.677  71.868  -1.994  1.00 32.96 ? 27  GLY B CA  1 
ATOM   1338  C  C   . GLY B  1 54  ? 64.168  71.617  -3.402  1.00 20.88 ? 27  GLY B C   1 
ATOM   1339  O  O   . GLY B  1 54  ? 63.951  70.475  -3.813  1.00 27.56 ? 27  GLY B O   1 
ATOM   1340  N  N   . PRO B  1 55  ? 63.974  72.684  -4.164  1.00 27.02 ? 28  PRO B N   1 
ATOM   1341  C  CA  . PRO B  1 55  ? 63.439  72.527  -5.511  1.00 26.21 ? 28  PRO B CA  1 
ATOM   1342  C  C   . PRO B  1 55  ? 64.483  71.920  -6.430  1.00 23.80 ? 28  PRO B C   1 
ATOM   1343  O  O   . PRO B  1 55  ? 65.687  71.938  -6.157  1.00 19.56 ? 28  PRO B O   1 
ATOM   1344  C  CB  . PRO B  1 55  ? 63.112  73.961  -5.930  1.00 25.92 ? 28  PRO B CB  1 
ATOM   1345  C  CG  . PRO B  1 55  ? 64.112  74.775  -5.189  1.00 37.09 ? 28  PRO B CG  1 
ATOM   1346  C  CD  . PRO B  1 55  ? 64.276  74.093  -3.857  1.00 29.64 ? 28  PRO B CD  1 
ATOM   1347  N  N   . VAL B  1 56  ? 63.989  71.377  -7.531  1.00 17.95 ? 29  VAL B N   1 
ATOM   1348  C  CA  . VAL B  1 56  ? 64.825  70.864  -8.609  1.00 17.95 ? 29  VAL B CA  1 
ATOM   1349  C  C   . VAL B  1 56  ? 64.842  71.908  -9.708  1.00 18.99 ? 29  VAL B C   1 
ATOM   1350  O  O   . VAL B  1 56  ? 63.777  72.359  -10.152 1.00 17.16 ? 29  VAL B O   1 
ATOM   1351  C  CB  . VAL B  1 56  ? 64.280  69.528  -9.138  1.00 15.26 ? 29  VAL B CB  1 
ATOM   1352  C  CG1 . VAL B  1 56  ? 65.196  69.009  -10.257 1.00 18.00 ? 29  VAL B CG1 1 
ATOM   1353  C  CG2 . VAL B  1 56  ? 64.180  68.534  -8.001  1.00 15.98 ? 29  VAL B CG2 1 
ATOM   1354  N  N   . LYS B  1 57  ? 66.042  72.327  -10.110 1.00 16.76 ? 30  LYS B N   1 
ATOM   1355  C  CA  . LYS B  1 57  ? 66.216  73.195  -11.258 1.00 17.66 ? 30  LYS B CA  1 
ATOM   1356  C  C   . LYS B  1 57  ? 66.318  72.321  -12.503 1.00 19.82 ? 30  LYS B C   1 
ATOM   1357  O  O   . LYS B  1 57  ? 67.073  71.345  -12.512 1.00 19.82 ? 30  LYS B O   1 
ATOM   1358  C  CB  . LYS B  1 57  ? 67.474  74.051  -11.099 1.00 19.82 ? 30  LYS B CB  1 
ATOM   1359  C  CG  . LYS B  1 57  ? 67.721  75.071  -12.222 1.00 34.52 ? 30  LYS B CG  1 
ATOM   1360  C  CD  . LYS B  1 57  ? 66.437  75.854  -12.564 1.00 43.65 ? 30  LYS B CD  1 
ATOM   1361  C  CE  . LYS B  1 57  ? 66.387  76.320  -14.028 1.00 28.86 ? 30  LYS B CE  1 
ATOM   1362  N  NZ  . LYS B  1 57  ? 67.588  77.130  -14.408 1.00 45.35 ? 30  LYS B NZ  1 
ATOM   1363  N  N   . VAL B  1 58  ? 65.568  72.677  -13.542 1.00 20.15 ? 31  VAL B N   1 
ATOM   1364  C  CA  . VAL B  1 58  ? 65.461  71.904  -14.783 1.00 15.00 ? 31  VAL B CA  1 
ATOM   1365  C  C   . VAL B  1 58  ? 65.828  72.846  -15.921 1.00 20.59 ? 31  VAL B C   1 
ATOM   1366  O  O   . VAL B  1 58  ? 65.177  73.880  -16.100 1.00 21.83 ? 31  VAL B O   1 
ATOM   1367  C  CB  . VAL B  1 58  ? 64.044  71.335  -14.979 1.00 20.02 ? 31  VAL B CB  1 
ATOM   1368  C  CG1 . VAL B  1 58  ? 63.961  70.468  -16.242 1.00 17.39 ? 31  VAL B CG1 1 
ATOM   1369  C  CG2 . VAL B  1 58  ? 63.584  70.522  -13.762 1.00 15.85 ? 31  VAL B CG2 1 
ATOM   1370  N  N   . TRP B  1 59  ? 66.868  72.510  -16.687 1.00 21.34 ? 32  TRP B N   1 
ATOM   1371  C  CA  . TRP B  1 59  ? 67.283  73.423  -17.746 1.00 19.14 ? 32  TRP B CA  1 
ATOM   1372  C  C   . TRP B  1 59  ? 67.969  72.670  -18.876 1.00 18.83 ? 32  TRP B C   1 
ATOM   1373  O  O   . TRP B  1 59  ? 68.554  71.605  -18.679 1.00 15.86 ? 32  TRP B O   1 
ATOM   1374  C  CB  . TRP B  1 59  ? 68.206  74.528  -17.207 1.00 20.69 ? 32  TRP B CB  1 
ATOM   1375  C  CG  . TRP B  1 59  ? 69.683  74.146  -17.148 1.00 23.51 ? 32  TRP B CG  1 
ATOM   1376  C  CD1 . TRP B  1 59  ? 70.626  74.374  -18.111 1.00 31.46 ? 32  TRP B CD1 1 
ATOM   1377  C  CD2 . TRP B  1 59  ? 70.353  73.459  -16.091 1.00 24.38 ? 32  TRP B CD2 1 
ATOM   1378  N  NE1 . TRP B  1 59  ? 71.848  73.878  -17.708 1.00 31.55 ? 32  TRP B NE1 1 
ATOM   1379  C  CE2 . TRP B  1 59  ? 71.703  73.308  -16.475 1.00 30.59 ? 32  TRP B CE2 1 
ATOM   1380  C  CE3 . TRP B  1 59  ? 69.948  72.958  -14.861 1.00 27.86 ? 32  TRP B CE3 1 
ATOM   1381  C  CZ2 . TRP B  1 59  ? 72.646  72.675  -15.664 1.00 37.02 ? 32  TRP B CZ2 1 
ATOM   1382  C  CZ3 . TRP B  1 59  ? 70.890  72.331  -14.054 1.00 38.60 ? 32  TRP B CZ3 1 
ATOM   1383  C  CH2 . TRP B  1 59  ? 72.220  72.198  -14.460 1.00 35.56 ? 32  TRP B CH2 1 
ATOM   1384  N  N   . GLY B  1 60  ? 67.900  73.251  -20.063 1.00 21.01 ? 33  GLY B N   1 
ATOM   1385  C  CA  . GLY B  1 60  ? 68.559  72.671  -21.217 1.00 20.19 ? 33  GLY B CA  1 
ATOM   1386  C  C   . GLY B  1 60  ? 67.911  73.194  -22.483 1.00 22.06 ? 33  GLY B C   1 
ATOM   1387  O  O   . GLY B  1 60  ? 67.224  74.210  -22.473 1.00 21.35 ? 33  GLY B O   1 
ATOM   1388  N  N   . SER B  1 61  ? 68.156  72.483  -23.569 1.00 22.18 ? 34  SER B N   1 
ATOM   1389  C  CA  . SER B  1 61  ? 67.693  72.933  -24.866 1.00 20.47 ? 34  SER B CA  1 
ATOM   1390  C  C   . SER B  1 61  ? 67.068  71.759  -25.593 1.00 22.37 ? 34  SER B C   1 
ATOM   1391  O  O   . SER B  1 61  ? 67.596  70.646  -25.549 1.00 23.25 ? 34  SER B O   1 
ATOM   1392  C  CB  . SER B  1 61  ? 68.862  73.518  -25.679 1.00 31.37 ? 34  SER B CB  1 
ATOM   1393  O  OG  . SER B  1 61  ? 68.389  74.438  -26.638 1.00 39.17 ? 34  SER B OG  1 
ATOM   1394  N  N   . ILE B  1 62  ? 65.931  72.002  -26.234 1.00 16.09 ? 35  ILE B N   1 
ATOM   1395  C  CA  . ILE B  1 62  ? 65.283  71.030  -27.102 1.00 19.45 ? 35  ILE B CA  1 
ATOM   1396  C  C   . ILE B  1 62  ? 65.097  71.705  -28.451 1.00 22.99 ? 35  ILE B C   1 
ATOM   1397  O  O   . ILE B  1 62  ? 64.567  72.819  -28.513 1.00 23.19 ? 35  ILE B O   1 
ATOM   1398  C  CB  . ILE B  1 62  ? 63.924  70.567  -26.551 1.00 21.29 ? 35  ILE B CB  1 
ATOM   1399  C  CG1 . ILE B  1 62  ? 64.029  70.094  -25.101 1.00 19.70 ? 35  ILE B CG1 1 
ATOM   1400  C  CG2 . ILE B  1 62  ? 63.331  69.469  -27.399 1.00 19.12 ? 35  ILE B CG2 1 
ATOM   1401  C  CD1 . ILE B  1 62  ? 62.657  69.921  -24.472 1.00 19.50 ? 35  ILE B CD1 1 
ATOM   1402  N  N   . LYS B  1 63  ? 65.514  71.041  -29.525 1.00 22.43 ? 36  LYS B N   1 
ATOM   1403  C  CA  . LYS B  1 63  ? 65.373  71.624  -30.856 1.00 22.97 ? 36  LYS B CA  1 
ATOM   1404  C  C   . LYS B  1 63  ? 64.441  70.777  -31.710 1.00 23.97 ? 36  LYS B C   1 
ATOM   1405  O  O   . LYS B  1 63  ? 64.067  69.662  -31.343 1.00 21.92 ? 36  LYS B O   1 
ATOM   1406  C  CB  . LYS B  1 63  ? 66.729  71.782  -31.554 1.00 31.33 ? 36  LYS B CB  1 
ATOM   1407  C  CG  . LYS B  1 63  ? 67.313  70.487  -32.063 1.00 32.19 ? 36  LYS B CG  1 
ATOM   1408  C  CD  . LYS B  1 63  ? 68.761  70.670  -32.532 1.00 37.70 ? 36  LYS B CD  1 
ATOM   1409  C  CE  . LYS B  1 63  ? 69.194  69.527  -33.449 1.00 41.70 ? 36  LYS B CE  1 
ATOM   1410  N  NZ  . LYS B  1 63  ? 70.683  69.369  -33.469 1.00 55.81 ? 36  LYS B NZ  1 
ATOM   1411  N  N   . GLY B  1 64  ? 64.048  71.327  -32.862 1.00 22.20 ? 37  GLY B N   1 
ATOM   1412  C  CA  . GLY B  1 64  ? 63.183  70.624  -33.789 1.00 19.86 ? 37  GLY B CA  1 
ATOM   1413  C  C   . GLY B  1 64  ? 61.695  70.702  -33.504 1.00 23.97 ? 37  GLY B C   1 
ATOM   1414  O  O   . GLY B  1 64  ? 60.923  69.942  -34.101 1.00 22.75 ? 37  GLY B O   1 
ATOM   1415  N  N   . LEU B  1 65  ? 61.264  71.588  -32.611 1.00 21.22 ? 38  LEU B N   1 
ATOM   1416  C  CA  . LEU B  1 65  ? 59.863  71.702  -32.224 1.00 19.75 ? 38  LEU B CA  1 
ATOM   1417  C  C   . LEU B  1 65  ? 59.148  72.728  -33.092 1.00 22.40 ? 38  LEU B C   1 
ATOM   1418  O  O   . LEU B  1 65  ? 59.762  73.679  -33.569 1.00 28.04 ? 38  LEU B O   1 
ATOM   1419  C  CB  . LEU B  1 65  ? 59.751  72.152  -30.762 1.00 16.45 ? 38  LEU B CB  1 
ATOM   1420  C  CG  . LEU B  1 65  ? 60.323  71.170  -29.739 1.00 20.60 ? 38  LEU B CG  1 
ATOM   1421  C  CD1 . LEU B  1 65  ? 60.674  71.875  -28.418 1.00 18.22 ? 38  LEU B CD1 1 
ATOM   1422  C  CD2 . LEU B  1 65  ? 59.313  70.074  -29.515 1.00 22.53 ? 38  LEU B CD2 1 
ATOM   1423  N  N   . THR B  1 66  ? 57.832  72.576  -33.231 1.00 24.04 ? 39  THR B N   1 
ATOM   1424  C  CA  . THR B  1 66  ? 57.039  73.685  -33.749 1.00 25.24 ? 39  THR B CA  1 
ATOM   1425  C  C   . THR B  1 66  ? 57.055  74.845  -32.753 1.00 30.02 ? 39  THR B C   1 
ATOM   1426  O  O   . THR B  1 66  ? 57.096  74.651  -31.534 1.00 22.39 ? 39  THR B O   1 
ATOM   1427  C  CB  . THR B  1 66  ? 55.589  73.251  -34.022 1.00 24.55 ? 39  THR B CB  1 
ATOM   1428  O  OG1 . THR B  1 66  ? 54.980  72.796  -32.799 1.00 26.04 ? 39  THR B OG1 1 
ATOM   1429  C  CG2 . THR B  1 66  ? 55.526  72.124  -35.062 1.00 22.00 ? 39  THR B CG2 1 
ATOM   1430  N  N   . GLU B  1 67  ? 57.037  76.065  -33.282 1.00 22.47 ? 40  GLU B N   1 
ATOM   1431  C  CA  . GLU B  1 67  ? 56.981  77.257  -32.442 1.00 25.54 ? 40  GLU B CA  1 
ATOM   1432  C  C   . GLU B  1 67  ? 55.774  77.187  -31.519 1.00 25.02 ? 40  GLU B C   1 
ATOM   1433  O  O   . GLU B  1 67  ? 54.694  76.774  -31.927 1.00 25.65 ? 40  GLU B O   1 
ATOM   1434  C  CB  . GLU B  1 67  ? 56.911  78.521  -33.312 1.00 24.07 ? 40  GLU B CB  1 
ATOM   1435  C  CG  . GLU B  1 67  ? 56.660  79.810  -32.522 1.00 26.24 ? 40  GLU B CG  1 
ATOM   1436  C  CD  . GLU B  1 67  ? 56.860  81.103  -33.344 1.00 48.28 ? 40  GLU B CD  1 
ATOM   1437  O  OE1 . GLU B  1 67  ? 57.120  82.171  -32.729 1.00 41.08 ? 40  GLU B OE1 1 
ATOM   1438  O  OE2 . GLU B  1 67  ? 56.789  81.043  -34.596 1.00 40.39 ? 40  GLU B OE2 1 
ATOM   1439  N  N   . GLY B  1 68  ? 55.973  77.546  -30.259 1.00 22.43 ? 41  GLY B N   1 
ATOM   1440  C  CA  . GLY B  1 68  ? 54.860  77.580  -29.329 1.00 30.29 ? 41  GLY B CA  1 
ATOM   1441  C  C   . GLY B  1 68  ? 54.980  76.634  -28.148 1.00 23.64 ? 41  GLY B C   1 
ATOM   1442  O  O   . GLY B  1 68  ? 56.073  76.166  -27.822 1.00 20.28 ? 41  GLY B O   1 
ATOM   1443  N  N   . LEU B  1 69  ? 53.852  76.327  -27.516 1.00 21.89 ? 42  LEU B N   1 
ATOM   1444  C  CA  . LEU B  1 69  ? 53.840  75.602  -26.249 1.00 21.46 ? 42  LEU B CA  1 
ATOM   1445  C  C   . LEU B  1 69  ? 53.781  74.099  -26.483 1.00 21.76 ? 42  LEU B C   1 
ATOM   1446  O  O   . LEU B  1 69  ? 53.047  73.620  -27.350 1.00 21.57 ? 42  LEU B O   1 
ATOM   1447  C  CB  . LEU B  1 69  ? 52.643  76.032  -25.395 1.00 22.67 ? 42  LEU B CB  1 
ATOM   1448  C  CG  . LEU B  1 69  ? 52.565  77.497  -24.958 1.00 27.81 ? 42  LEU B CG  1 
ATOM   1449  C  CD1 . LEU B  1 69  ? 51.179  77.731  -24.372 1.00 33.62 ? 42  LEU B CD1 1 
ATOM   1450  C  CD2 . LEU B  1 69  ? 53.588  77.787  -23.901 1.00 26.42 ? 42  LEU B CD2 1 
ATOM   1451  N  N   . HIS B  1 70  ? 54.554  73.355  -25.691 1.00 15.32 ? 43  HIS B N   1 
ATOM   1452  C  CA  . HIS B  1 70  ? 54.568  71.899  -25.728 1.00 13.54 ? 43  HIS B CA  1 
ATOM   1453  C  C   . HIS B  1 70  ? 54.535  71.352  -24.312 1.00 13.42 ? 43  HIS B C   1 
ATOM   1454  O  O   . HIS B  1 70  ? 55.359  71.747  -23.488 1.00 13.95 ? 43  HIS B O   1 
ATOM   1455  C  CB  . HIS B  1 70  ? 55.825  71.388  -26.429 1.00 15.46 ? 43  HIS B CB  1 
ATOM   1456  C  CG  . HIS B  1 70  ? 55.870  71.743  -27.883 1.00 20.69 ? 43  HIS B CG  1 
ATOM   1457  N  ND1 . HIS B  1 70  ? 55.401  70.897  -28.859 1.00 20.00 ? 43  HIS B ND1 1 
ATOM   1458  C  CD2 . HIS B  1 70  ? 56.319  72.848  -28.522 1.00 16.98 ? 43  HIS B CD2 1 
ATOM   1459  C  CE1 . HIS B  1 70  ? 55.565  71.461  -30.047 1.00 23.31 ? 43  HIS B CE1 1 
ATOM   1460  N  NE2 . HIS B  1 70  ? 56.107  72.652  -29.868 1.00 20.07 ? 43  HIS B NE2 1 
ATOM   1461  N  N   . GLY B  1 71  ? 53.621  70.417  -24.054 1.00 15.87 ? 44  GLY B N   1 
ATOM   1462  C  CA  . GLY B  1 71  ? 53.596  69.747  -22.764 1.00 14.08 ? 44  GLY B CA  1 
ATOM   1463  C  C   . GLY B  1 71  ? 54.907  69.034  -22.472 1.00 14.69 ? 44  GLY B C   1 
ATOM   1464  O  O   . GLY B  1 71  ? 55.572  68.508  -23.361 1.00 13.42 ? 44  GLY B O   1 
ATOM   1465  N  N   . PHE B  1 72  ? 55.248  68.987  -21.192 1.00 14.23 ? 45  PHE B N   1 
ATOM   1466  C  CA  . PHE B  1 72  ? 56.590  68.616  -20.749 1.00 16.78 ? 45  PHE B CA  1 
ATOM   1467  C  C   . PHE B  1 72  ? 56.371  67.881  -19.430 1.00 18.03 ? 45  PHE B C   1 
ATOM   1468  O  O   . PHE B  1 72  ? 56.063  68.521  -18.422 1.00 15.91 ? 45  PHE B O   1 
ATOM   1469  C  CB  . PHE B  1 72  ? 57.434  69.880  -20.595 1.00 14.42 ? 45  PHE B CB  1 
ATOM   1470  C  CG  . PHE B  1 72  ? 58.908  69.656  -20.337 1.00 14.33 ? 45  PHE B CG  1 
ATOM   1471  C  CD1 . PHE B  1 72  ? 59.750  69.100  -21.307 1.00 19.58 ? 45  PHE B CD1 1 
ATOM   1472  C  CD2 . PHE B  1 72  ? 59.464  70.075  -19.128 1.00 18.99 ? 45  PHE B CD2 1 
ATOM   1473  C  CE1 . PHE B  1 72  ? 61.134  68.955  -21.056 1.00 16.05 ? 45  PHE B CE1 1 
ATOM   1474  C  CE2 . PHE B  1 72  ? 60.827  69.934  -18.865 1.00 20.39 ? 45  PHE B CE2 1 
ATOM   1475  C  CZ  . PHE B  1 72  ? 61.665  69.373  -19.826 1.00 17.81 ? 45  PHE B CZ  1 
ATOM   1476  N  N   . HIS B  1 73  ? 56.456  66.546  -19.455 1.00 13.42 ? 46  HIS B N   1 
ATOM   1477  C  CA  . HIS B  1 73  ? 56.014  65.740  -18.322 1.00 18.55 ? 46  HIS B CA  1 
ATOM   1478  C  C   . HIS B  1 73  ? 57.006  64.628  -18.007 1.00 16.81 ? 46  HIS B C   1 
ATOM   1479  O  O   . HIS B  1 73  ? 57.630  64.068  -18.906 1.00 15.25 ? 46  HIS B O   1 
ATOM   1480  C  CB  . HIS B  1 73  ? 54.667  65.085  -18.595 1.00 20.13 ? 46  HIS B CB  1 
ATOM   1481  C  CG  . HIS B  1 73  ? 53.629  66.044  -19.066 1.00 21.43 ? 46  HIS B CG  1 
ATOM   1482  N  ND1 . HIS B  1 73  ? 52.969  65.893  -20.262 1.00 22.05 ? 46  HIS B ND1 1 
ATOM   1483  C  CD2 . HIS B  1 73  ? 53.169  67.194  -18.522 1.00 22.17 ? 46  HIS B CD2 1 
ATOM   1484  C  CE1 . HIS B  1 73  ? 52.120  66.893  -20.422 1.00 22.31 ? 46  HIS B CE1 1 
ATOM   1485  N  NE2 . HIS B  1 73  ? 52.233  67.706  -19.388 1.00 21.58 ? 46  HIS B NE2 1 
ATOM   1486  N  N   . VAL B  1 74  ? 57.096  64.272  -16.734 1.00 13.42 ? 47  VAL B N   1 
ATOM   1487  C  CA  . VAL B  1 74  ? 57.767  63.041  -16.343 1.00 15.75 ? 47  VAL B CA  1 
ATOM   1488  C  C   . VAL B  1 74  ? 56.714  61.945  -16.336 1.00 18.51 ? 47  VAL B C   1 
ATOM   1489  O  O   . VAL B  1 74  ? 55.700  62.051  -15.633 1.00 20.39 ? 47  VAL B O   1 
ATOM   1490  C  CB  . VAL B  1 74  ? 58.437  63.168  -14.965 1.00 13.42 ? 47  VAL B CB  1 
ATOM   1491  C  CG1 . VAL B  1 74  ? 59.116  61.859  -14.586 1.00 14.49 ? 47  VAL B CG1 1 
ATOM   1492  C  CG2 . VAL B  1 74  ? 59.448  64.328  -14.949 1.00 18.37 ? 47  VAL B CG2 1 
ATOM   1493  N  N   . HIS B  1 75  ? 56.945  60.897  -17.107 1.00 13.42 ? 48  HIS B N   1 
ATOM   1494  C  CA  . HIS B  1 75  ? 56.053  59.752  -17.152 1.00 13.90 ? 48  HIS B CA  1 
ATOM   1495  C  C   . HIS B  1 75  ? 56.610  58.641  -16.264 1.00 16.88 ? 48  HIS B C   1 
ATOM   1496  O  O   . HIS B  1 75  ? 57.791  58.636  -15.906 1.00 15.87 ? 48  HIS B O   1 
ATOM   1497  C  CB  . HIS B  1 75  ? 55.884  59.262  -18.604 1.00 14.36 ? 48  HIS B CB  1 
ATOM   1498  C  CG  . HIS B  1 75  ? 55.091  60.197  -19.464 1.00 13.42 ? 48  HIS B CG  1 
ATOM   1499  N  ND1 . HIS B  1 75  ? 53.935  59.814  -20.110 1.00 14.48 ? 48  HIS B ND1 1 
ATOM   1500  C  CD2 . HIS B  1 75  ? 55.288  61.500  -19.784 1.00 13.75 ? 48  HIS B CD2 1 
ATOM   1501  C  CE1 . HIS B  1 75  ? 53.462  60.839  -20.805 1.00 20.68 ? 48  HIS B CE1 1 
ATOM   1502  N  NE2 . HIS B  1 75  ? 54.261  61.877  -20.622 1.00 14.53 ? 48  HIS B NE2 1 
ATOM   1503  N  N   . GLU B  1 76  ? 55.750  57.670  -15.951 1.00 13.42 ? 49  GLU B N   1 
ATOM   1504  C  CA  . GLU B  1 76  ? 55.989  56.777  -14.822 1.00 17.40 ? 49  GLU B CA  1 
ATOM   1505  C  C   . GLU B  1 76  ? 57.196  55.859  -15.025 1.00 20.39 ? 49  GLU B C   1 
ATOM   1506  O  O   . GLU B  1 76  ? 58.003  55.686  -14.109 1.00 19.22 ? 49  GLU B O   1 
ATOM   1507  C  CB  . GLU B  1 76  ? 54.744  55.944  -14.554 1.00 16.53 ? 49  GLU B CB  1 
ATOM   1508  C  CG  . GLU B  1 76  ? 54.932  55.012  -13.360 1.00 22.30 ? 49  GLU B CG  1 
ATOM   1509  C  CD  . GLU B  1 76  ? 53.655  54.300  -12.951 1.00 29.18 ? 49  GLU B CD  1 
ATOM   1510  O  OE1 . GLU B  1 76  ? 52.634  54.399  -13.673 1.00 31.99 ? 49  GLU B OE1 1 
ATOM   1511  O  OE2 . GLU B  1 76  ? 53.704  53.587  -11.935 1.00 28.72 ? 49  GLU B OE2 1 
ATOM   1512  N  N   . PHE B  1 77  ? 57.321  55.230  -16.191 1.00 18.65 ? 50  PHE B N   1 
ATOM   1513  C  CA  . PHE B  1 77  ? 58.313  54.173  -16.398 1.00 17.21 ? 50  PHE B CA  1 
ATOM   1514  C  C   . PHE B  1 77  ? 59.456  54.657  -17.274 1.00 17.35 ? 50  PHE B C   1 
ATOM   1515  O  O   . PHE B  1 77  ? 59.233  55.365  -18.258 1.00 21.15 ? 50  PHE B O   1 
ATOM   1516  C  CB  . PHE B  1 77  ? 57.684  52.943  -17.049 1.00 18.93 ? 50  PHE B CB  1 
ATOM   1517  C  CG  . PHE B  1 77  ? 56.483  52.447  -16.314 1.00 21.76 ? 50  PHE B CG  1 
ATOM   1518  C  CD1 . PHE B  1 77  ? 56.595  51.993  -15.017 1.00 23.37 ? 50  PHE B CD1 1 
ATOM   1519  C  CD2 . PHE B  1 77  ? 55.227  52.481  -16.913 1.00 30.28 ? 50  PHE B CD2 1 
ATOM   1520  C  CE1 . PHE B  1 77  ? 55.468  51.557  -14.326 1.00 29.51 ? 50  PHE B CE1 1 
ATOM   1521  C  CE2 . PHE B  1 77  ? 54.108  52.047  -16.226 1.00 26.09 ? 50  PHE B CE2 1 
ATOM   1522  C  CZ  . PHE B  1 77  ? 54.229  51.591  -14.937 1.00 28.14 ? 50  PHE B CZ  1 
ATOM   1523  N  N   . GLY B  1 78  ? 60.670  54.222  -16.934 1.00 15.86 ? 51  GLY B N   1 
ATOM   1524  C  CA  . GLY B  1 78  ? 61.853  54.481  -17.728 1.00 16.00 ? 51  GLY B CA  1 
ATOM   1525  C  C   . GLY B  1 78  ? 62.019  53.364  -18.743 1.00 24.40 ? 51  GLY B C   1 
ATOM   1526  O  O   . GLY B  1 78  ? 63.084  52.747  -18.852 1.00 21.03 ? 51  GLY B O   1 
ATOM   1527  N  N   . ASP B  1 79  ? 60.948  53.089  -19.478 1.00 21.00 ? 52  ASP B N   1 
ATOM   1528  C  CA  . ASP B  1 79  ? 60.838  51.944  -20.385 1.00 20.35 ? 52  ASP B CA  1 
ATOM   1529  C  C   . ASP B  1 79  ? 60.658  52.486  -21.799 1.00 22.49 ? 52  ASP B C   1 
ATOM   1530  O  O   . ASP B  1 79  ? 59.576  52.958  -22.156 1.00 22.16 ? 52  ASP B O   1 
ATOM   1531  C  CB  . ASP B  1 79  ? 59.660  51.058  -19.969 1.00 21.48 ? 52  ASP B CB  1 
ATOM   1532  C  CG  . ASP B  1 79  ? 59.488  49.827  -20.868 1.00 25.20 ? 52  ASP B CG  1 
ATOM   1533  O  OD1 . ASP B  1 79  ? 60.051  49.792  -21.980 1.00 24.41 ? 52  ASP B OD1 1 
ATOM   1534  O  OD2 . ASP B  1 79  ? 58.795  48.884  -20.445 1.00 26.29 ? 52  ASP B OD2 1 
ATOM   1535  N  N   A ASN B  1 80  ? 61.730  52.406  -22.593 0.49 21.70 ? 53  ASN B N   1 
ATOM   1536  N  N   B ASN B  1 80  ? 61.701  52.449  -22.609 0.51 21.66 ? 53  ASN B N   1 
ATOM   1537  C  CA  A ASN B  1 80  ? 61.786  52.877  -23.974 0.49 22.35 ? 53  ASN B CA  1 
ATOM   1538  C  CA  B ASN B  1 80  ? 61.577  52.919  -23.978 0.51 22.24 ? 53  ASN B CA  1 
ATOM   1539  C  C   A ASN B  1 80  ? 61.646  51.748  -24.993 0.49 23.59 ? 53  ASN B C   1 
ATOM   1540  C  C   B ASN B  1 80  ? 61.682  51.757  -24.975 0.51 23.59 ? 53  ASN B C   1 
ATOM   1541  O  O   A ASN B  1 80  ? 61.872  51.968  -26.190 0.49 22.71 ? 53  ASN B O   1 
ATOM   1542  O  O   B ASN B  1 80  ? 62.088  51.946  -26.127 0.51 22.66 ? 53  ASN B O   1 
ATOM   1543  C  CB  A ASN B  1 80  ? 63.104  53.631  -24.219 0.49 24.29 ? 53  ASN B CB  1 
ATOM   1544  C  CB  B ASN B  1 80  ? 62.596  54.040  -24.237 0.51 26.84 ? 53  ASN B CB  1 
ATOM   1545  C  CG  A ASN B  1 80  ? 63.037  54.538  -25.434 0.49 26.79 ? 53  ASN B CG  1 
ATOM   1546  C  CG  B ASN B  1 80  ? 62.389  55.278  -23.293 0.51 29.36 ? 53  ASN B CG  1 
ATOM   1547  O  OD1 A ASN B  1 80  ? 62.033  55.211  -25.654 0.49 30.49 ? 53  ASN B OD1 1 
ATOM   1548  O  OD1 B ASN B  1 80  ? 61.330  55.443  -22.666 0.51 27.59 ? 53  ASN B OD1 1 
ATOM   1549  N  ND2 A ASN B  1 80  ? 64.107  54.558  -26.232 0.49 28.26 ? 53  ASN B ND2 1 
ATOM   1550  N  ND2 B ASN B  1 80  ? 63.397  56.146  -23.218 0.51 25.65 ? 53  ASN B ND2 1 
ATOM   1551  N  N   . THR B  1 81  ? 61.269  50.551  -24.549 1.00 21.61 ? 54  THR B N   1 
ATOM   1552  C  CA  . THR B  1 81  ? 61.292  49.383  -25.436 1.00 26.10 ? 54  THR B CA  1 
ATOM   1553  C  C   . THR B  1 81  ? 60.349  49.541  -26.616 1.00 31.33 ? 54  THR B C   1 
ATOM   1554  O  O   . THR B  1 81  ? 60.642  49.051  -27.706 1.00 29.62 ? 54  THR B O   1 
ATOM   1555  C  CB  . THR B  1 81  ? 60.932  48.100  -24.686 1.00 26.27 ? 54  THR B CB  1 
ATOM   1556  O  OG1 . THR B  1 81  ? 59.630  48.225  -24.095 1.00 24.72 ? 54  THR B OG1 1 
ATOM   1557  C  CG2 . THR B  1 81  ? 61.958  47.807  -23.613 1.00 24.25 ? 54  THR B CG2 1 
ATOM   1558  N  N   . ALA B  1 82  ? 59.220  50.208  -26.437 1.00 24.58 ? 55  ALA B N   1 
ATOM   1559  C  CA  . ALA B  1 82  ? 58.340  50.517  -27.556 1.00 33.70 ? 55  ALA B CA  1 
ATOM   1560  C  C   . ALA B  1 82  ? 58.375  52.011  -27.858 1.00 32.20 ? 55  ALA B C   1 
ATOM   1561  O  O   . ALA B  1 82  ? 57.357  52.625  -28.168 1.00 33.49 ? 55  ALA B O   1 
ATOM   1562  C  CB  . ALA B  1 82  ? 56.915  50.043  -27.271 1.00 33.35 ? 55  ALA B CB  1 
ATOM   1563  N  N   . GLY B  1 83  ? 59.556  52.615  -27.749 1.00 29.03 ? 56  GLY B N   1 
ATOM   1564  C  CA  . GLY B  1 83  ? 59.617  54.057  -27.890 1.00 30.38 ? 56  GLY B CA  1 
ATOM   1565  C  C   . GLY B  1 83  ? 58.944  54.749  -26.712 1.00 25.13 ? 56  GLY B C   1 
ATOM   1566  O  O   . GLY B  1 83  ? 58.816  54.193  -25.609 1.00 24.33 ? 56  GLY B O   1 
ATOM   1567  N  N   . CYS B  1 84  ? 58.467  55.968  -26.962 1.00 24.48 ? 57  CYS B N   1 
ATOM   1568  C  CA  . CYS B  1 84  ? 57.929  56.777  -25.865 1.00 23.70 ? 57  CYS B CA  1 
ATOM   1569  C  C   . CYS B  1 84  ? 56.616  56.221  -25.320 1.00 24.06 ? 57  CYS B C   1 
ATOM   1570  O  O   . CYS B  1 84  ? 56.264  56.491  -24.162 1.00 22.39 ? 57  CYS B O   1 
ATOM   1571  C  CB  . CYS B  1 84  ? 57.760  58.222  -26.344 1.00 30.52 ? 57  CYS B CB  1 
ATOM   1572  S  SG  . CYS B  1 84  ? 59.346  59.025  -26.861 1.00 34.80 ? 57  CYS B SG  1 
ATOM   1573  N  N   . THR B  1 85  ? 55.900  55.429  -26.120 1.00 22.16 ? 58  THR B N   1 
ATOM   1574  C  CA  . THR B  1 85  ? 54.639  54.834  -25.686 1.00 23.31 ? 58  THR B CA  1 
ATOM   1575  C  C   . THR B  1 85  ? 54.809  53.979  -24.440 1.00 21.85 ? 58  THR B C   1 
ATOM   1576  O  O   . THR B  1 85  ? 53.918  53.936  -23.583 1.00 23.78 ? 58  THR B O   1 
ATOM   1577  C  CB  . THR B  1 85  ? 54.061  53.989  -26.825 1.00 29.46 ? 58  THR B CB  1 
ATOM   1578  O  OG1 . THR B  1 85  ? 53.849  54.826  -27.963 1.00 35.04 ? 58  THR B OG1 1 
ATOM   1579  C  CG2 . THR B  1 85  ? 52.759  53.331  -26.403 1.00 35.69 ? 58  THR B CG2 1 
ATOM   1580  N  N   . SER B  1 86  ? 55.933  53.274  -24.313 1.00 21.08 ? 59  SER B N   1 
ATOM   1581  C  CA  . SER B  1 86  ? 56.062  52.367  -23.181 1.00 23.11 ? 59  SER B CA  1 
ATOM   1582  C  C   . SER B  1 86  ? 56.421  53.082  -21.884 1.00 19.38 ? 59  SER B C   1 
ATOM   1583  O  O   . SER B  1 86  ? 56.504  52.431  -20.842 1.00 19.90 ? 59  SER B O   1 
ATOM   1584  C  CB  . SER B  1 86  ? 57.088  51.258  -23.483 1.00 26.15 ? 59  SER B CB  1 
ATOM   1585  O  OG  . SER B  1 86  ? 58.185  51.725  -24.236 1.00 28.55 ? 59  SER B OG  1 
ATOM   1586  N  N   . ALA B  1 87  ? 56.627  54.399  -21.907 1.00 21.81 ? 60  ALA B N   1 
ATOM   1587  C  CA  . ALA B  1 87  ? 56.837  55.130  -20.655 1.00 20.59 ? 60  ALA B CA  1 
ATOM   1588  C  C   . ALA B  1 87  ? 55.582  55.207  -19.796 1.00 24.16 ? 60  ALA B C   1 
ATOM   1589  O  O   . ALA B  1 87  ? 55.675  55.613  -18.633 1.00 17.63 ? 60  ALA B O   1 
ATOM   1590  C  CB  . ALA B  1 87  ? 57.343  56.553  -20.944 1.00 18.79 ? 60  ALA B CB  1 
ATOM   1591  N  N   . GLY B  1 88  ? 54.416  54.849  -20.328 1.00 23.12 ? 61  GLY B N   1 
ATOM   1592  C  CA  . GLY B  1 88  ? 53.212  54.813  -19.521 1.00 22.33 ? 61  GLY B CA  1 
ATOM   1593  C  C   . GLY B  1 88  ? 52.661  56.205  -19.274 1.00 18.24 ? 61  GLY B C   1 
ATOM   1594  O  O   . GLY B  1 88  ? 52.968  57.149  -20.014 1.00 20.91 ? 61  GLY B O   1 
ATOM   1595  N  N   . PRO B  1 89  ? 51.845  56.371  -18.236 1.00 20.80 ? 62  PRO B N   1 
ATOM   1596  C  CA  . PRO B  1 89  ? 51.167  57.658  -18.018 1.00 21.12 ? 62  PRO B CA  1 
ATOM   1597  C  C   . PRO B  1 89  ? 52.060  58.616  -17.240 1.00 19.13 ? 62  PRO B C   1 
ATOM   1598  O  O   . PRO B  1 89  ? 53.210  58.321  -16.924 1.00 16.76 ? 62  PRO B O   1 
ATOM   1599  C  CB  . PRO B  1 89  ? 49.931  57.261  -17.205 1.00 22.37 ? 62  PRO B CB  1 
ATOM   1600  C  CG  . PRO B  1 89  ? 50.433  56.111  -16.335 1.00 23.18 ? 62  PRO B CG  1 
ATOM   1601  C  CD  . PRO B  1 89  ? 51.449  55.362  -17.226 1.00 19.24 ? 62  PRO B CD  1 
ATOM   1602  N  N   . HIS B  1 90  ? 51.511  59.789  -16.943 1.00 20.92 ? 63  HIS B N   1 
ATOM   1603  C  CA  . HIS B  1 90  ? 52.236  60.749  -16.123 1.00 19.20 ? 63  HIS B CA  1 
ATOM   1604  C  C   . HIS B  1 90  ? 52.563  60.118  -14.775 1.00 19.72 ? 63  HIS B C   1 
ATOM   1605  O  O   . HIS B  1 90  ? 51.761  59.356  -14.226 1.00 20.81 ? 63  HIS B O   1 
ATOM   1606  C  CB  . HIS B  1 90  ? 51.406  62.021  -15.918 1.00 22.04 ? 63  HIS B CB  1 
ATOM   1607  C  CG  . HIS B  1 90  ? 51.192  62.801  -17.171 1.00 22.81 ? 63  HIS B CG  1 
ATOM   1608  N  ND1 . HIS B  1 90  ? 50.554  64.020  -17.192 1.00 21.15 ? 63  HIS B ND1 1 
ATOM   1609  C  CD2 . HIS B  1 90  ? 51.562  62.547  -18.452 1.00 22.62 ? 63  HIS B CD2 1 
ATOM   1610  C  CE1 . HIS B  1 90  ? 50.512  64.474  -18.431 1.00 22.44 ? 63  HIS B CE1 1 
ATOM   1611  N  NE2 . HIS B  1 90  ? 51.121  63.600  -19.216 1.00 23.44 ? 63  HIS B NE2 1 
ATOM   1612  N  N   . PHE B  1 91  ? 53.765  60.405  -14.269 1.00 13.42 ? 64  PHE B N   1 
ATOM   1613  C  CA  . PHE B  1 91  ? 54.187  59.904  -12.968 1.00 19.01 ? 64  PHE B CA  1 
ATOM   1614  C  C   . PHE B  1 91  ? 53.254  60.479  -11.904 1.00 19.07 ? 64  PHE B C   1 
ATOM   1615  O  O   . PHE B  1 91  ? 53.197  61.696  -11.727 1.00 18.84 ? 64  PHE B O   1 
ATOM   1616  C  CB  . PHE B  1 91  ? 55.652  60.277  -12.715 1.00 14.22 ? 64  PHE B CB  1 
ATOM   1617  C  CG  . PHE B  1 91  ? 56.174  59.823  -11.388 1.00 16.50 ? 64  PHE B CG  1 
ATOM   1618  C  CD1 . PHE B  1 91  ? 55.848  58.576  -10.901 1.00 17.63 ? 64  PHE B CD1 1 
ATOM   1619  C  CD2 . PHE B  1 91  ? 56.979  60.648  -10.635 1.00 17.21 ? 64  PHE B CD2 1 
ATOM   1620  C  CE1 . PHE B  1 91  ? 56.320  58.158  -9.652  1.00 22.53 ? 64  PHE B CE1 1 
ATOM   1621  C  CE2 . PHE B  1 91  ? 57.460  60.247  -9.392  1.00 21.65 ? 64  PHE B CE2 1 
ATOM   1622  C  CZ  . PHE B  1 91  ? 57.117  58.993  -8.907  1.00 19.64 ? 64  PHE B CZ  1 
ATOM   1623  N  N   . ASN B  1 92  ? 52.487  59.631  -11.217 1.00 18.93 ? 65  ASN B N   1 
ATOM   1624  C  CA  . ASN B  1 92  ? 51.369  60.094  -10.386 1.00 19.27 ? 65  ASN B CA  1 
ATOM   1625  C  C   . ASN B  1 92  ? 51.238  59.223  -9.132  1.00 20.99 ? 65  ASN B C   1 
ATOM   1626  O  O   . ASN B  1 92  ? 50.202  58.600  -8.894  1.00 23.17 ? 65  ASN B O   1 
ATOM   1627  C  CB  . ASN B  1 92  ? 50.088  60.102  -11.218 1.00 20.58 ? 65  ASN B CB  1 
ATOM   1628  C  CG  . ASN B  1 92  ? 48.868  60.670  -10.474 1.00 23.74 ? 65  ASN B CG  1 
ATOM   1629  O  OD1 . ASN B  1 92  ? 48.988  61.489  -9.575  1.00 23.59 ? 65  ASN B OD1 1 
ATOM   1630  N  ND2 . ASN B  1 92  ? 47.683  60.250  -10.906 1.00 24.63 ? 65  ASN B ND2 1 
ATOM   1631  N  N   . PRO B  1 93  ? 52.273  59.179  -8.295  1.00 19.07 ? 66  PRO B N   1 
ATOM   1632  C  CA  . PRO B  1 93  ? 52.233  58.250  -7.158  1.00 27.03 ? 66  PRO B CA  1 
ATOM   1633  C  C   . PRO B  1 93  ? 51.159  58.583  -6.140  1.00 31.32 ? 66  PRO B C   1 
ATOM   1634  O  O   . PRO B  1 93  ? 50.818  57.713  -5.331  1.00 31.24 ? 66  PRO B O   1 
ATOM   1635  C  CB  . PRO B  1 93  ? 53.629  58.386  -6.546  1.00 25.91 ? 66  PRO B CB  1 
ATOM   1636  C  CG  . PRO B  1 93  ? 54.036  59.775  -6.878  1.00 26.63 ? 66  PRO B CG  1 
ATOM   1637  C  CD  . PRO B  1 93  ? 53.476  60.024  -8.256  1.00 22.51 ? 66  PRO B CD  1 
ATOM   1638  N  N   . LEU B  1 94  ? 50.626  59.805  -6.146  1.00 30.39 ? 67  LEU B N   1 
ATOM   1639  C  CA  . LEU B  1 94  ? 49.563  60.197  -5.227  1.00 29.54 ? 67  LEU B CA  1 
ATOM   1640  C  C   . LEU B  1 94  ? 48.176  60.125  -5.855  1.00 30.88 ? 67  LEU B C   1 
ATOM   1641  O  O   . LEU B  1 94  ? 47.199  60.543  -5.221  1.00 32.55 ? 67  LEU B O   1 
ATOM   1642  C  CB  . LEU B  1 94  ? 49.830  61.597  -4.696  1.00 26.11 ? 67  LEU B CB  1 
ATOM   1643  C  CG  . LEU B  1 94  ? 51.118  61.651  -3.874  1.00 30.65 ? 67  LEU B CG  1 
ATOM   1644  C  CD1 . LEU B  1 94  ? 51.555  63.100  -3.687  1.00 34.48 ? 67  LEU B CD1 1 
ATOM   1645  C  CD2 . LEU B  1 94  ? 50.913  60.962  -2.520  1.00 38.75 ? 67  LEU B CD2 1 
ATOM   1646  N  N   . SER B  1 95  ? 48.070  59.605  -7.079  1.00 24.70 ? 68  SER B N   1 
ATOM   1647  C  CA  . SER B  1 95  ? 46.790  59.377  -7.751  1.00 29.06 ? 68  SER B CA  1 
ATOM   1648  C  C   . SER B  1 95  ? 45.938  60.646  -7.761  1.00 34.37 ? 68  SER B C   1 
ATOM   1649  O  O   . SER B  1 95  ? 44.751  60.632  -7.430  1.00 35.80 ? 68  SER B O   1 
ATOM   1650  C  CB  . SER B  1 95  ? 46.022  58.222  -7.093  1.00 37.30 ? 68  SER B CB  1 
ATOM   1651  O  OG  . SER B  1 95  ? 46.716  56.996  -7.228  1.00 45.77 ? 68  SER B OG  1 
ATOM   1652  N  N   A ARG B  1 96  ? 46.551  61.756  -8.142  0.54 26.38 ? 69  ARG B N   1 
ATOM   1653  N  N   B ARG B  1 96  ? 46.567  61.762  -8.118  0.46 26.70 ? 69  ARG B N   1 
ATOM   1654  C  CA  A ARG B  1 96  ? 45.819  63.004  -8.256  0.54 24.33 ? 69  ARG B CA  1 
ATOM   1655  C  CA  B ARG B  1 96  ? 45.868  63.031  -8.247  0.46 24.36 ? 69  ARG B CA  1 
ATOM   1656  C  C   A ARG B  1 96  ? 45.375  63.217  -9.695  0.54 26.54 ? 69  ARG B C   1 
ATOM   1657  C  C   B ARG B  1 96  ? 45.379  63.217  -9.683  0.46 26.51 ? 69  ARG B C   1 
ATOM   1658  O  O   A ARG B  1 96  ? 45.695  62.438  -10.596 0.54 26.97 ? 69  ARG B O   1 
ATOM   1659  O  O   B ARG B  1 96  ? 45.676  62.421  -10.576 0.46 26.96 ? 69  ARG B O   1 
ATOM   1660  C  CB  A ARG B  1 96  ? 46.673  64.170  -7.768  0.54 24.31 ? 69  ARG B CB  1 
ATOM   1661  C  CB  B ARG B  1 96  ? 46.783  64.184  -7.828  0.46 24.31 ? 69  ARG B CB  1 
ATOM   1662  C  CG  A ARG B  1 96  ? 47.181  63.969  -6.358  0.54 26.00 ? 69  ARG B CG  1 
ATOM   1663  C  CG  B ARG B  1 96  ? 47.367  64.051  -6.421  0.46 26.27 ? 69  ARG B CG  1 
ATOM   1664  C  CD  A ARG B  1 96  ? 46.037  63.844  -5.369  0.54 24.10 ? 69  ARG B CD  1 
ATOM   1665  C  CD  B ARG B  1 96  ? 46.627  64.928  -5.414  0.46 28.54 ? 69  ARG B CD  1 
ATOM   1666  N  NE  A ARG B  1 96  ? 46.542  63.886  -4.001  0.54 34.08 ? 69  ARG B NE  1 
ATOM   1667  N  NE  B ARG B  1 96  ? 47.115  64.735  -4.049  0.46 31.27 ? 69  ARG B NE  1 
ATOM   1668  C  CZ  A ARG B  1 96  ? 46.308  62.966  -3.075  0.54 26.76 ? 69  ARG B CZ  1 
ATOM   1669  C  CZ  B ARG B  1 96  ? 47.944  65.548  -3.406  0.46 28.51 ? 69  ARG B CZ  1 
ATOM   1670  N  NH1 A ARG B  1 96  ? 45.522  61.929  -3.312  0.54 29.42 ? 69  ARG B NH1 1 
ATOM   1671  N  NH1 B ARG B  1 96  ? 48.400  66.656  -3.963  0.46 29.88 ? 69  ARG B NH1 1 
ATOM   1672  N  NH2 A ARG B  1 96  ? 46.890  63.084  -1.886  0.54 33.80 ? 69  ARG B NH2 1 
ATOM   1673  N  NH2 B ARG B  1 96  ? 48.318  65.245  -2.163  0.46 33.70 ? 69  ARG B NH2 1 
ATOM   1674  N  N   . LYS B  1 97  ? 44.600  64.277  -9.897  1.00 25.70 ? 70  LYS B N   1 
ATOM   1675  C  CA  . LYS B  1 97  ? 44.208  64.674  -11.237 1.00 24.98 ? 70  LYS B CA  1 
ATOM   1676  C  C   . LYS B  1 97  ? 45.321  65.526  -11.833 1.00 21.70 ? 70  LYS B C   1 
ATOM   1677  O  O   . LYS B  1 97  ? 46.114  66.124  -11.103 1.00 22.86 ? 70  LYS B O   1 
ATOM   1678  C  CB  . LYS B  1 97  ? 42.890  65.454  -11.207 1.00 29.83 ? 70  LYS B CB  1 
ATOM   1679  C  CG  . LYS B  1 97  ? 41.667  64.543  -11.302 1.00 35.45 ? 70  LYS B CG  1 
ATOM   1680  C  CD  . LYS B  1 97  ? 40.378  65.233  -10.875 1.00 40.86 ? 70  LYS B CD  1 
ATOM   1681  C  CE  . LYS B  1 97  ? 39.220  64.217  -10.878 1.00 54.73 ? 70  LYS B CE  1 
ATOM   1682  N  NZ  . LYS B  1 97  ? 37.936  64.734  -11.473 1.00 55.32 ? 70  LYS B NZ  1 
ATOM   1683  N  N   . HIS B  1 98  ? 45.368  65.582  -13.168 1.00 22.15 ? 71  HIS B N   1 
ATOM   1684  C  CA  . HIS B  1 98  ? 46.389  66.359  -13.860 1.00 19.69 ? 71  HIS B CA  1 
ATOM   1685  C  C   . HIS B  1 98  ? 46.189  67.850  -13.596 1.00 23.90 ? 71  HIS B C   1 
ATOM   1686  O  O   . HIS B  1 98  ? 45.060  68.339  -13.533 1.00 23.27 ? 71  HIS B O   1 
ATOM   1687  C  CB  . HIS B  1 98  ? 46.332  66.073  -15.372 1.00 20.66 ? 71  HIS B CB  1 
ATOM   1688  C  CG  . HIS B  1 98  ? 47.260  66.925  -16.188 1.00 22.10 ? 71  HIS B CG  1 
ATOM   1689  N  ND1 . HIS B  1 98  ? 48.600  66.640  -16.326 1.00 22.38 ? 71  HIS B ND1 1 
ATOM   1690  C  CD2 . HIS B  1 98  ? 47.041  68.050  -16.911 1.00 16.11 ? 71  HIS B CD2 1 
ATOM   1691  C  CE1 . HIS B  1 98  ? 49.168  67.544  -17.104 1.00 17.59 ? 71  HIS B CE1 1 
ATOM   1692  N  NE2 . HIS B  1 98  ? 48.244  68.412  -17.471 1.00 21.31 ? 71  HIS B NE2 1 
ATOM   1693  N  N   . GLY B  1 99  ? 47.296  68.574  -13.447 1.00 17.43 ? 72  GLY B N   1 
ATOM   1694  C  CA  . GLY B  1 99  ? 47.239  70.010  -13.274 1.00 19.65 ? 72  GLY B CA  1 
ATOM   1695  C  C   . GLY B  1 99  ? 48.477  70.683  -13.827 1.00 24.09 ? 72  GLY B C   1 
ATOM   1696  O  O   . GLY B  1 99  ? 49.297  70.018  -14.464 1.00 21.87 ? 72  GLY B O   1 
ATOM   1697  N  N   . GLY B  1 100 ? 48.611  71.991  -13.637 1.00 18.60 ? 73  GLY B N   1 
ATOM   1698  C  CA  . GLY B  1 100 ? 49.841  72.676  -13.964 1.00 15.47 ? 73  GLY B CA  1 
ATOM   1699  C  C   . GLY B  1 100 ? 50.789  72.615  -12.783 1.00 23.34 ? 73  GLY B C   1 
ATOM   1700  O  O   . GLY B  1 100 ? 50.387  72.257  -11.674 1.00 23.48 ? 73  GLY B O   1 
ATOM   1701  N  N   . PRO B  1 101 ? 52.062  72.956  -12.989 1.00 22.28 ? 74  PRO B N   1 
ATOM   1702  C  CA  . PRO B  1 101 ? 53.035  72.787  -11.903 1.00 23.34 ? 74  PRO B CA  1 
ATOM   1703  C  C   . PRO B  1 101 ? 52.723  73.622  -10.672 1.00 29.27 ? 74  PRO B C   1 
ATOM   1704  O  O   . PRO B  1 101 ? 53.145  73.252  -9.575  1.00 23.60 ? 74  PRO B O   1 
ATOM   1705  C  CB  . PRO B  1 101 ? 54.368  73.206  -12.544 1.00 20.88 ? 74  PRO B CB  1 
ATOM   1706  C  CG  . PRO B  1 101 ? 54.006  73.943  -13.788 1.00 25.69 ? 74  PRO B CG  1 
ATOM   1707  C  CD  . PRO B  1 101 ? 52.701  73.387  -14.249 1.00 20.07 ? 74  PRO B CD  1 
ATOM   1708  N  N   . LYS B  1 102 ? 52.010  74.737  -10.809 1.00 25.67 ? 75  LYS B N   1 
ATOM   1709  C  CA  . LYS B  1 102 ? 51.673  75.552  -9.649  1.00 25.34 ? 75  LYS B CA  1 
ATOM   1710  C  C   . LYS B  1 102 ? 50.404  75.093  -8.932  1.00 28.34 ? 75  LYS B C   1 
ATOM   1711  O  O   . LYS B  1 102 ? 50.055  75.663  -7.894  1.00 31.79 ? 75  LYS B O   1 
ATOM   1712  C  CB  . LYS B  1 102 ? 51.551  77.026  -10.056 1.00 28.31 ? 75  LYS B CB  1 
ATOM   1713  C  CG  . LYS B  1 102 ? 52.902  77.653  -10.375 1.00 35.24 ? 75  LYS B CG  1 
ATOM   1714  C  CD  . LYS B  1 102 ? 52.768  78.891  -11.249 1.00 52.35 ? 75  LYS B CD  1 
ATOM   1715  C  CE  . LYS B  1 102 ? 52.877  80.158  -10.389 1.00 54.10 ? 75  LYS B CE  1 
ATOM   1716  N  NZ  . LYS B  1 102 ? 51.727  80.332  -9.442  1.00 57.96 ? 75  LYS B NZ  1 
ATOM   1717  N  N   . ASP B  1 103 ? 49.716  74.082  -9.441  1.00 22.22 ? 76  ASP B N   1 
ATOM   1718  C  CA  . ASP B  1 103 ? 48.511  73.571  -8.795  1.00 25.17 ? 76  ASP B CA  1 
ATOM   1719  C  C   . ASP B  1 103 ? 48.836  72.634  -7.646  1.00 28.80 ? 76  ASP B C   1 
ATOM   1720  O  O   . ASP B  1 103 ? 49.784  71.844  -7.710  1.00 27.78 ? 76  ASP B O   1 
ATOM   1721  C  CB  . ASP B  1 103 ? 47.634  72.827  -9.799  1.00 30.00 ? 76  ASP B CB  1 
ATOM   1722  C  CG  . ASP B  1 103 ? 46.998  73.751  -10.790 1.00 32.53 ? 76  ASP B CG  1 
ATOM   1723  O  OD1 . ASP B  1 103 ? 46.654  74.881  -10.382 1.00 39.23 ? 76  ASP B OD1 1 
ATOM   1724  O  OD2 . ASP B  1 103 ? 46.855  73.366  -11.966 1.00 33.56 ? 76  ASP B OD2 1 
ATOM   1725  N  N   . GLU B  1 104 ? 48.014  72.706  -6.599  1.00 30.44 ? 77  GLU B N   1 
ATOM   1726  C  CA  . GLU B  1 104 ? 48.081  71.707  -5.544  1.00 27.50 ? 77  GLU B CA  1 
ATOM   1727  C  C   . GLU B  1 104 ? 47.634  70.343  -6.052  1.00 28.35 ? 77  GLU B C   1 
ATOM   1728  O  O   . GLU B  1 104 ? 48.278  69.325  -5.765  1.00 30.73 ? 77  GLU B O   1 
ATOM   1729  C  CB  . GLU B  1 104 ? 47.225  72.140  -4.351  1.00 35.53 ? 77  GLU B CB  1 
ATOM   1730  C  CG  . GLU B  1 104 ? 47.393  71.227  -3.154  1.00 41.89 ? 77  GLU B CG  1 
ATOM   1731  C  CD  . GLU B  1 104 ? 46.881  71.845  -1.869  1.00 59.02 ? 77  GLU B CD  1 
ATOM   1732  O  OE1 . GLU B  1 104 ? 46.362  72.985  -1.923  1.00 59.49 ? 77  GLU B OE1 1 
ATOM   1733  O  OE2 . GLU B  1 104 ? 46.996  71.185  -0.810  1.00 63.86 ? 77  GLU B OE2 1 
ATOM   1734  N  N   . GLU B  1 105 ? 46.546  70.300  -6.818  1.00 25.94 ? 78  GLU B N   1 
ATOM   1735  C  CA  . GLU B  1 105 ? 46.091  69.068  -7.457  1.00 29.16 ? 78  GLU B CA  1 
ATOM   1736  C  C   . GLU B  1 105 ? 46.848  68.918  -8.773  1.00 23.62 ? 78  GLU B C   1 
ATOM   1737  O  O   . GLU B  1 105 ? 46.529  69.572  -9.770  1.00 22.90 ? 78  GLU B O   1 
ATOM   1738  C  CB  . GLU B  1 105 ? 44.585  69.084  -7.687  1.00 24.55 ? 78  GLU B CB  1 
ATOM   1739  C  CG  . GLU B  1 105 ? 44.069  67.820  -8.323  1.00 30.61 ? 78  GLU B CG  1 
ATOM   1740  C  CD  . GLU B  1 105 ? 43.806  66.726  -7.308  1.00 35.86 ? 78  GLU B CD  1 
ATOM   1741  O  OE1 . GLU B  1 105 ? 43.871  67.021  -6.091  1.00 39.75 ? 78  GLU B OE1 1 
ATOM   1742  O  OE2 . GLU B  1 105 ? 43.529  65.572  -7.723  1.00 33.24 ? 78  GLU B OE2 1 
ATOM   1743  N  N   . ARG B  1 106 ? 47.861  68.060  -8.774  1.00 22.93 ? 79  ARG B N   1 
ATOM   1744  C  CA  . ARG B  1 106 ? 48.629  67.812  -9.992  1.00 17.04 ? 79  ARG B CA  1 
ATOM   1745  C  C   . ARG B  1 106 ? 49.327  66.473  -9.822  1.00 19.89 ? 79  ARG B C   1 
ATOM   1746  O  O   . ARG B  1 106 ? 49.433  65.947  -8.708  1.00 22.52 ? 79  ARG B O   1 
ATOM   1747  C  CB  . ARG B  1 106 ? 49.655  68.928  -10.245 1.00 14.36 ? 79  ARG B CB  1 
ATOM   1748  C  CG  . ARG B  1 106 ? 50.711  69.015  -9.094  1.00 20.83 ? 79  ARG B CG  1 
ATOM   1749  C  CD  . ARG B  1 106 ? 51.910  69.886  -9.456  1.00 24.63 ? 79  ARG B CD  1 
ATOM   1750  N  NE  . ARG B  1 106 ? 53.037  69.078  -9.934  1.00 21.06 ? 79  ARG B NE  1 
ATOM   1751  C  CZ  . ARG B  1 106 ? 54.289  69.509  -9.993  1.00 22.92 ? 79  ARG B CZ  1 
ATOM   1752  N  NH1 . ARG B  1 106 ? 54.608  70.746  -9.631  1.00 21.03 ? 79  ARG B NH1 1 
ATOM   1753  N  NH2 . ARG B  1 106 ? 55.246  68.683  -10.434 1.00 18.97 ? 79  ARG B NH2 1 
ATOM   1754  N  N   . HIS B  1 107 ? 49.768  65.916  -10.942 1.00 16.39 ? 80  HIS B N   1 
ATOM   1755  C  CA  . HIS B  1 107 ? 50.664  64.765  -10.914 1.00 17.65 ? 80  HIS B CA  1 
ATOM   1756  C  C   . HIS B  1 107 ? 52.052  65.243  -10.502 1.00 13.89 ? 80  HIS B C   1 
ATOM   1757  O  O   . HIS B  1 107 ? 52.460  66.359  -10.831 1.00 16.41 ? 80  HIS B O   1 
ATOM   1758  C  CB  . HIS B  1 107 ? 50.733  64.120  -12.313 1.00 16.98 ? 80  HIS B CB  1 
ATOM   1759  C  CG  . HIS B  1 107 ? 49.403  63.664  -12.846 1.00 19.44 ? 80  HIS B CG  1 
ATOM   1760  N  ND1 . HIS B  1 107 ? 49.146  63.540  -14.188 1.00 17.69 ? 80  HIS B ND1 1 
ATOM   1761  C  CD2 . HIS B  1 107 ? 48.276  63.253  -12.214 1.00 21.90 ? 80  HIS B CD2 1 
ATOM   1762  C  CE1 . HIS B  1 107 ? 47.915  63.092  -14.369 1.00 21.62 ? 80  HIS B CE1 1 
ATOM   1763  N  NE2 . HIS B  1 107 ? 47.368  62.906  -13.182 1.00 20.83 ? 80  HIS B NE2 1 
ATOM   1764  N  N   . VAL B  1 108 ? 52.803  64.385  -9.802  1.00 17.11 ? 81  VAL B N   1 
ATOM   1765  C  CA  . VAL B  1 108 ? 54.206  64.710  -9.541  1.00 15.60 ? 81  VAL B CA  1 
ATOM   1766  C  C   . VAL B  1 108 ? 54.918  65.056  -10.854 1.00 13.42 ? 81  VAL B C   1 
ATOM   1767  O  O   . VAL B  1 108 ? 55.688  66.017  -10.929 1.00 17.86 ? 81  VAL B O   1 
ATOM   1768  C  CB  . VAL B  1 108 ? 54.906  63.548  -8.805  1.00 20.85 ? 81  VAL B CB  1 
ATOM   1769  C  CG1 . VAL B  1 108 ? 56.414  63.764  -8.791  1.00 19.89 ? 81  VAL B CG1 1 
ATOM   1770  C  CG2 . VAL B  1 108 ? 54.398  63.450  -7.329  1.00 17.34 ? 81  VAL B CG2 1 
ATOM   1771  N  N   . GLY B  1 109 ? 54.649  64.305  -11.906 1.00 14.58 ? 82  GLY B N   1 
ATOM   1772  C  CA  . GLY B  1 109 ? 55.312  64.542  -13.198 1.00 16.71 ? 82  GLY B CA  1 
ATOM   1773  C  C   . GLY B  1 109 ? 54.831  65.746  -13.997 1.00 19.50 ? 82  GLY B C   1 
ATOM   1774  O  O   . GLY B  1 109 ? 55.296  65.935  -15.128 1.00 16.31 ? 82  GLY B O   1 
ATOM   1775  N  N   . ASP B  1 110 ? 53.916  66.563  -13.470 1.00 18.14 ? 83  ASP B N   1 
ATOM   1776  C  CA  . ASP B  1 110 ? 53.320  67.662  -14.254 1.00 15.93 ? 83  ASP B CA  1 
ATOM   1777  C  C   . ASP B  1 110 ? 54.216  68.898  -14.242 1.00 19.80 ? 83  ASP B C   1 
ATOM   1778  O  O   . ASP B  1 110 ? 54.083  69.787  -13.392 1.00 21.54 ? 83  ASP B O   1 
ATOM   1779  C  CB  . ASP B  1 110 ? 51.943  68.009  -13.702 1.00 18.50 ? 83  ASP B CB  1 
ATOM   1780  C  CG  . ASP B  1 110 ? 50.911  67.020  -14.089 1.00 17.90 ? 83  ASP B CG  1 
ATOM   1781  O  OD1 . ASP B  1 110 ? 51.181  66.200  -15.001 1.00 20.19 ? 83  ASP B OD1 1 
ATOM   1782  O  OD2 . ASP B  1 110 ? 49.832  67.038  -13.468 1.00 22.06 ? 83  ASP B OD2 1 
ATOM   1783  N  N   . LEU B  1 111 ? 55.101  69.015  -15.228 1.00 14.91 ? 84  LEU B N   1 
ATOM   1784  C  CA  . LEU B  1 111 ? 55.967  70.179  -15.288 1.00 17.54 ? 84  LEU B CA  1 
ATOM   1785  C  C   . LEU B  1 111 ? 55.439  71.272  -16.222 1.00 18.68 ? 84  LEU B C   1 
ATOM   1786  O  O   . LEU B  1 111 ? 56.164  72.234  -16.506 1.00 20.22 ? 84  LEU B O   1 
ATOM   1787  C  CB  . LEU B  1 111 ? 57.386  69.755  -15.695 1.00 17.28 ? 84  LEU B CB  1 
ATOM   1788  C  CG  . LEU B  1 111 ? 58.085  68.814  -14.712 1.00 18.28 ? 84  LEU B CG  1 
ATOM   1789  C  CD1 . LEU B  1 111 ? 59.461  68.466  -15.238 1.00 18.22 ? 84  LEU B CD1 1 
ATOM   1790  C  CD2 . LEU B  1 111 ? 58.208  69.493  -13.330 1.00 21.38 ? 84  LEU B CD2 1 
ATOM   1791  N  N   . GLY B  1 112 ? 54.210  71.147  -16.709 1.00 17.97 ? 85  GLY B N   1 
ATOM   1792  C  CA  . GLY B  1 112 ? 53.601  72.215  -17.476 1.00 18.76 ? 85  GLY B CA  1 
ATOM   1793  C  C   . GLY B  1 112 ? 54.037  72.212  -18.931 1.00 16.58 ? 85  GLY B C   1 
ATOM   1794  O  O   . GLY B  1 112 ? 54.150  71.149  -19.550 1.00 14.41 ? 85  GLY B O   1 
ATOM   1795  N  N   . ASN B  1 113 ? 54.280  73.397  -19.479 1.00 13.42 ? 86  ASN B N   1 
ATOM   1796  C  CA  . ASN B  1 113 ? 54.689  73.551  -20.866 1.00 15.78 ? 86  ASN B CA  1 
ATOM   1797  C  C   . ASN B  1 113 ? 56.109  74.080  -20.956 1.00 18.28 ? 86  ASN B C   1 
ATOM   1798  O  O   . ASN B  1 113 ? 56.610  74.727  -20.032 1.00 20.52 ? 86  ASN B O   1 
ATOM   1799  C  CB  . ASN B  1 113 ? 53.771  74.533  -21.605 1.00 18.67 ? 86  ASN B CB  1 
ATOM   1800  C  CG  . ASN B  1 113 ? 52.413  73.977  -21.825 1.00 22.09 ? 86  ASN B CG  1 
ATOM   1801  O  OD1 . ASN B  1 113 ? 52.257  72.975  -22.524 1.00 20.57 ? 86  ASN B OD1 1 
ATOM   1802  N  ND2 . ASN B  1 113 ? 51.407  74.611  -21.231 1.00 16.49 ? 86  ASN B ND2 1 
ATOM   1803  N  N   . VAL B  1 114 ? 56.739  73.839  -22.102 1.00 15.78 ? 87  VAL B N   1 
ATOM   1804  C  CA  . VAL B  1 114 ? 57.930  74.583  -22.489 1.00 16.44 ? 87  VAL B CA  1 
ATOM   1805  C  C   . VAL B  1 114 ? 57.633  75.262  -23.816 1.00 18.57 ? 87  VAL B C   1 
ATOM   1806  O  O   . VAL B  1 114 ? 56.802  74.794  -24.600 1.00 22.51 ? 87  VAL B O   1 
ATOM   1807  C  CB  . VAL B  1 114 ? 59.184  73.675  -22.569 1.00 17.20 ? 87  VAL B CB  1 
ATOM   1808  C  CG1 . VAL B  1 114 ? 59.508  73.094  -21.164 1.00 13.42 ? 87  VAL B CG1 1 
ATOM   1809  C  CG2 . VAL B  1 114 ? 58.960  72.549  -23.541 1.00 19.97 ? 87  VAL B CG2 1 
ATOM   1810  N  N   . THR B  1 115 ? 58.322  76.364  -24.073 1.00 18.72 ? 88  THR B N   1 
ATOM   1811  C  CA  . THR B  1 115 ? 58.029  77.216  -25.226 1.00 18.50 ? 88  THR B CA  1 
ATOM   1812  C  C   . THR B  1 115 ? 59.190  77.139  -26.203 1.00 17.41 ? 88  THR B C   1 
ATOM   1813  O  O   . THR B  1 115 ? 60.332  77.416  -25.825 1.00 21.62 ? 88  THR B O   1 
ATOM   1814  C  CB  . THR B  1 115 ? 57.822  78.669  -24.801 1.00 17.53 ? 88  THR B CB  1 
ATOM   1815  O  OG1 . THR B  1 115 ? 56.677  78.758  -23.943 1.00 21.09 ? 88  THR B OG1 1 
ATOM   1816  C  CG2 . THR B  1 115 ? 57.577  79.556  -26.039 1.00 20.91 ? 88  THR B CG2 1 
ATOM   1817  N  N   . ALA B  1 116 ? 58.889  76.783  -27.450 1.00 18.27 ? 89  ALA B N   1 
ATOM   1818  C  CA  . ALA B  1 116 ? 59.857  76.813  -28.536 1.00 20.56 ? 89  ALA B CA  1 
ATOM   1819  C  C   . ALA B  1 116 ? 59.744  78.135  -29.288 1.00 24.56 ? 89  ALA B C   1 
ATOM   1820  O  O   . ALA B  1 116 ? 58.640  78.639  -29.509 1.00 23.43 ? 89  ALA B O   1 
ATOM   1821  C  CB  . ALA B  1 116 ? 59.622  75.639  -29.493 1.00 19.89 ? 89  ALA B CB  1 
ATOM   1822  N  N   . ASP B  1 117 ? 60.892  78.712  -29.642 1.00 21.73 ? 90  ASP B N   1 
ATOM   1823  C  CA  . ASP B  1 117 ? 60.936  80.004  -30.320 1.00 29.48 ? 90  ASP B CA  1 
ATOM   1824  C  C   . ASP B  1 117 ? 60.698  79.801  -31.820 1.00 28.31 ? 90  ASP B C   1 
ATOM   1825  O  O   . ASP B  1 117 ? 60.360  78.704  -32.271 1.00 21.78 ? 90  ASP B O   1 
ATOM   1826  C  CB  . ASP B  1 117 ? 62.251  80.723  -30.002 1.00 34.36 ? 90  ASP B CB  1 
ATOM   1827  C  CG  . ASP B  1 117 ? 63.493  79.994  -30.548 1.00 34.71 ? 90  ASP B CG  1 
ATOM   1828  O  OD1 . ASP B  1 117 ? 63.370  79.169  -31.480 1.00 24.25 ? 90  ASP B OD1 1 
ATOM   1829  O  OD2 . ASP B  1 117 ? 64.604  80.255  -30.021 1.00 31.83 ? 90  ASP B OD2 1 
ATOM   1830  N  N   . LYS B  1 118 ? 60.875  80.862  -32.623 1.00 30.94 ? 91  LYS B N   1 
ATOM   1831  C  CA  . LYS B  1 118 ? 60.573  80.752  -34.046 1.00 32.12 ? 91  LYS B CA  1 
ATOM   1832  C  C   . LYS B  1 118 ? 61.541  79.823  -34.764 1.00 30.44 ? 91  LYS B C   1 
ATOM   1833  O  O   . LYS B  1 118 ? 61.227  79.355  -35.865 1.00 33.16 ? 91  LYS B O   1 
ATOM   1834  C  CB  . LYS B  1 118 ? 60.605  82.125  -34.748 1.00 31.93 ? 91  LYS B CB  1 
ATOM   1835  C  CG  . LYS B  1 118 ? 61.968  82.832  -34.742 1.00 39.17 ? 91  LYS B CG  1 
ATOM   1836  C  CD  . LYS B  1 118 ? 61.886  84.315  -34.357 1.00 48.96 ? 91  LYS B CD  1 
ATOM   1837  C  CE  . LYS B  1 118 ? 63.265  84.872  -33.967 1.00 49.51 ? 91  LYS B CE  1 
ATOM   1838  N  NZ  . LYS B  1 118 ? 63.783  84.313  -32.673 1.00 57.45 ? 91  LYS B NZ  1 
ATOM   1839  N  N   . ASP B  1 119 ? 62.710  79.540  -34.185 1.00 27.26 ? 92  ASP B N   1 
ATOM   1840  C  CA  . ASP B  1 119 ? 63.629  78.581  -34.796 1.00 30.04 ? 92  ASP B CA  1 
ATOM   1841  C  C   . ASP B  1 119 ? 63.391  77.148  -34.340 1.00 31.39 ? 92  ASP B C   1 
ATOM   1842  O  O   . ASP B  1 119 ? 64.158  76.257  -34.721 1.00 27.54 ? 92  ASP B O   1 
ATOM   1843  C  CB  . ASP B  1 119 ? 65.078  78.980  -34.518 1.00 32.50 ? 92  ASP B CB  1 
ATOM   1844  C  CG  . ASP B  1 119 ? 65.424  80.345  -35.106 1.00 44.41 ? 92  ASP B CG  1 
ATOM   1845  O  OD1 . ASP B  1 119 ? 64.880  80.681  -36.181 1.00 43.41 ? 92  ASP B OD1 1 
ATOM   1846  O  OD2 . ASP B  1 119 ? 66.233  81.072  -34.497 1.00 51.26 ? 92  ASP B OD2 1 
ATOM   1847  N  N   . GLY B  1 120 ? 62.362  76.907  -33.526 1.00 29.10 ? 93  GLY B N   1 
ATOM   1848  C  CA  . GLY B  1 120 ? 62.076  75.562  -33.068 1.00 24.29 ? 93  GLY B CA  1 
ATOM   1849  C  C   . GLY B  1 120 ? 62.832  75.127  -31.834 1.00 23.19 ? 93  GLY B C   1 
ATOM   1850  O  O   . GLY B  1 120 ? 62.840  73.932  -31.516 1.00 23.34 ? 93  GLY B O   1 
ATOM   1851  N  N   . VAL B  1 121 ? 63.426  76.067  -31.105 1.00 23.36 ? 94  VAL B N   1 
ATOM   1852  C  CA  . VAL B  1 121 ? 64.290  75.789  -29.964 1.00 22.31 ? 94  VAL B CA  1 
ATOM   1853  C  C   . VAL B  1 121 ? 63.583  76.185  -28.673 1.00 21.81 ? 94  VAL B C   1 
ATOM   1854  O  O   . VAL B  1 121 ? 63.160  77.337  -28.510 1.00 23.74 ? 94  VAL B O   1 
ATOM   1855  C  CB  . VAL B  1 121 ? 65.631  76.530  -30.086 1.00 26.46 ? 94  VAL B CB  1 
ATOM   1856  C  CG1 . VAL B  1 121 ? 66.421  76.377  -28.793 1.00 25.48 ? 94  VAL B CG1 1 
ATOM   1857  C  CG2 . VAL B  1 121 ? 66.422  75.979  -31.258 1.00 27.87 ? 94  VAL B CG2 1 
ATOM   1858  N  N   . ALA B  1 122 ? 63.489  75.234  -27.744 1.00 21.88 ? 95  ALA B N   1 
ATOM   1859  C  CA  . ALA B  1 122 ? 62.969  75.479  -26.402 1.00 19.83 ? 95  ALA B CA  1 
ATOM   1860  C  C   . ALA B  1 122 ? 64.154  75.527  -25.450 1.00 22.36 ? 95  ALA B C   1 
ATOM   1861  O  O   . ALA B  1 122 ? 64.800  74.498  -25.199 1.00 24.07 ? 95  ALA B O   1 
ATOM   1862  C  CB  . ALA B  1 122 ? 61.973  74.390  -25.999 1.00 22.22 ? 95  ALA B CB  1 
ATOM   1863  N  N   . ASP B  1 123 ? 64.446  76.717  -24.925 1.00 23.44 ? 96  ASP B N   1 
ATOM   1864  C  CA  . ASP B  1 123 ? 65.508  76.895  -23.936 1.00 22.03 ? 96  ASP B CA  1 
ATOM   1865  C  C   . ASP B  1 123 ? 64.885  76.752  -22.556 1.00 23.50 ? 96  ASP B C   1 
ATOM   1866  O  O   . ASP B  1 123 ? 64.474  77.728  -21.926 1.00 22.97 ? 96  ASP B O   1 
ATOM   1867  C  CB  . ASP B  1 123 ? 66.199  78.237  -24.122 1.00 24.31 ? 96  ASP B CB  1 
ATOM   1868  C  CG  . ASP B  1 123 ? 67.089  78.259  -25.359 1.00 34.43 ? 96  ASP B CG  1 
ATOM   1869  O  OD1 . ASP B  1 123 ? 67.950  77.358  -25.486 1.00 36.79 ? 96  ASP B OD1 1 
ATOM   1870  O  OD2 . ASP B  1 123 ? 66.932  79.164  -26.203 1.00 36.79 ? 96  ASP B OD2 1 
ATOM   1871  N  N   . VAL B  1 124 ? 64.828  75.508  -22.085 1.00 20.67 ? 97  VAL B N   1 
ATOM   1872  C  CA  . VAL B  1 124 ? 64.042  75.154  -20.912 1.00 17.10 ? 97  VAL B CA  1 
ATOM   1873  C  C   . VAL B  1 124 ? 64.673  75.754  -19.662 1.00 19.32 ? 97  VAL B C   1 
ATOM   1874  O  O   . VAL B  1 124 ? 65.898  75.685  -19.460 1.00 21.71 ? 97  VAL B O   1 
ATOM   1875  C  CB  . VAL B  1 124 ? 63.935  73.621  -20.815 1.00 16.70 ? 97  VAL B CB  1 
ATOM   1876  C  CG1 . VAL B  1 124 ? 63.194  73.188  -19.555 1.00 20.96 ? 97  VAL B CG1 1 
ATOM   1877  C  CG2 . VAL B  1 124 ? 63.250  73.059  -22.065 1.00 15.89 ? 97  VAL B CG2 1 
ATOM   1878  N  N   . SER B  1 125 ? 63.838  76.341  -18.809 1.00 18.51 ? 98  SER B N   1 
ATOM   1879  C  CA  . SER B  1 125 ? 64.289  76.840  -17.504 1.00 20.64 ? 98  SER B CA  1 
ATOM   1880  C  C   . SER B  1 125 ? 63.102  76.734  -16.555 1.00 19.74 ? 98  SER B C   1 
ATOM   1881  O  O   . SER B  1 125 ? 62.200  77.578  -16.590 1.00 27.35 ? 98  SER B O   1 
ATOM   1882  C  CB  . SER B  1 125 ? 64.796  78.277  -17.594 1.00 26.22 ? 98  SER B CB  1 
ATOM   1883  O  OG  . SER B  1 125 ? 65.306  78.698  -16.344 1.00 30.38 ? 98  SER B OG  1 
ATOM   1884  N  N   . ILE B  1 126 ? 63.103  75.700  -15.729 1.00 21.69 ? 99  ILE B N   1 
ATOM   1885  C  CA  . ILE B  1 126 ? 62.009  75.409  -14.814 1.00 21.53 ? 99  ILE B CA  1 
ATOM   1886  C  C   . ILE B  1 126 ? 62.599  75.150  -13.436 1.00 24.33 ? 99  ILE B C   1 
ATOM   1887  O  O   . ILE B  1 126 ? 63.696  74.597  -13.313 1.00 20.55 ? 99  ILE B O   1 
ATOM   1888  C  CB  . ILE B  1 126 ? 61.200  74.192  -15.315 1.00 21.24 ? 99  ILE B CB  1 
ATOM   1889  C  CG1 . ILE B  1 126 ? 60.373  74.569  -16.538 1.00 24.61 ? 99  ILE B CG1 1 
ATOM   1890  C  CG2 . ILE B  1 126 ? 60.295  73.647  -14.264 1.00 22.42 ? 99  ILE B CG2 1 
ATOM   1891  C  CD1 . ILE B  1 126 ? 59.671  73.345  -17.174 1.00 22.69 ? 99  ILE B CD1 1 
ATOM   1892  N  N   . GLU B  1 127 ? 61.894  75.573  -12.402 1.00 20.63 ? 100 GLU B N   1 
ATOM   1893  C  CA  . GLU B  1 127 ? 62.244  75.197  -11.048 1.00 17.44 ? 100 GLU B CA  1 
ATOM   1894  C  C   . GLU B  1 127 ? 61.003  74.574  -10.438 1.00 26.80 ? 100 GLU B C   1 
ATOM   1895  O  O   . GLU B  1 127 ? 59.916  75.153  -10.526 1.00 22.99 ? 100 GLU B O   1 
ATOM   1896  C  CB  . GLU B  1 127 ? 62.706  76.410  -10.257 1.00 27.73 ? 100 GLU B CB  1 
ATOM   1897  C  CG  . GLU B  1 127 ? 63.055  76.112  -8.836  1.00 35.97 ? 100 GLU B CG  1 
ATOM   1898  C  CD  . GLU B  1 127 ? 63.537  77.358  -8.127  1.00 55.57 ? 100 GLU B CD  1 
ATOM   1899  O  OE1 . GLU B  1 127 ? 62.898  77.777  -7.134  1.00 56.88 ? 100 GLU B OE1 1 
ATOM   1900  O  OE2 . GLU B  1 127 ? 64.507  77.962  -8.629  1.00 51.62 ? 100 GLU B OE2 1 
ATOM   1901  N  N   . ASP B  1 128 ? 61.131  73.372  -9.887  1.00 19.61 ? 101 ASP B N   1 
ATOM   1902  C  CA  . ASP B  1 128 ? 59.955  72.675  -9.386  1.00 24.13 ? 101 ASP B CA  1 
ATOM   1903  C  C   . ASP B  1 128 ? 60.250  72.040  -8.035  1.00 23.14 ? 101 ASP B C   1 
ATOM   1904  O  O   . ASP B  1 128 ? 61.314  71.445  -7.836  1.00 25.34 ? 101 ASP B O   1 
ATOM   1905  C  CB  . ASP B  1 128 ? 59.475  71.598  -10.375 1.00 23.20 ? 101 ASP B CB  1 
ATOM   1906  C  CG  . ASP B  1 128 ? 58.092  71.067  -10.014 1.00 26.51 ? 101 ASP B CG  1 
ATOM   1907  O  OD1 . ASP B  1 128 ? 57.100  71.783  -10.278 1.00 29.88 ? 101 ASP B OD1 1 
ATOM   1908  O  OD2 . ASP B  1 128 ? 57.985  69.964  -9.439  1.00 22.21 ? 101 ASP B OD2 1 
ATOM   1909  N  N   . SER B  1 129 ? 59.286  72.106  -7.119  1.00 26.01 ? 102 SER B N   1 
ATOM   1910  C  CA  . SER B  1 129 ? 59.513  71.588  -5.779  1.00 23.71 ? 102 SER B CA  1 
ATOM   1911  C  C   . SER B  1 129 ? 58.695  70.346  -5.483  1.00 23.24 ? 102 SER B C   1 
ATOM   1912  O  O   . SER B  1 129 ? 58.704  69.859  -4.353  1.00 28.28 ? 102 SER B O   1 
ATOM   1913  C  CB  . SER B  1 129 ? 59.243  72.684  -4.745  1.00 36.53 ? 102 SER B CB  1 
ATOM   1914  O  OG  . SER B  1 129 ? 58.004  73.304  -5.008  1.00 48.70 ? 102 SER B OG  1 
ATOM   1915  N  N   . VAL B  1 130 ? 58.005  69.795  -6.472  1.00 22.19 ? 103 VAL B N   1 
ATOM   1916  C  CA  . VAL B  1 130 ? 57.273  68.560  -6.267  1.00 17.19 ? 103 VAL B CA  1 
ATOM   1917  C  C   . VAL B  1 130 ? 58.051  67.353  -6.790  1.00 20.08 ? 103 VAL B C   1 
ATOM   1918  O  O   . VAL B  1 130 ? 58.098  66.315  -6.132  1.00 19.54 ? 103 VAL B O   1 
ATOM   1919  C  CB  . VAL B  1 130 ? 55.876  68.678  -6.915  1.00 20.02 ? 103 VAL B CB  1 
ATOM   1920  C  CG1 . VAL B  1 130 ? 55.177  67.343  -6.932  1.00 22.28 ? 103 VAL B CG1 1 
ATOM   1921  C  CG2 . VAL B  1 130 ? 55.038  69.721  -6.131  1.00 24.17 ? 103 VAL B CG2 1 
ATOM   1922  N  N   . ILE B  1 131 ? 58.674  67.463  -7.968  1.00 21.07 ? 104 ILE B N   1 
ATOM   1923  C  CA  . ILE B  1 131 ? 59.628  66.412  -8.368  1.00 17.70 ? 104 ILE B CA  1 
ATOM   1924  C  C   . ILE B  1 131 ? 60.834  66.447  -7.437  1.00 15.92 ? 104 ILE B C   1 
ATOM   1925  O  O   . ILE B  1 131 ? 61.134  67.453  -6.799  1.00 18.15 ? 104 ILE B O   1 
ATOM   1926  C  CB  . ILE B  1 131 ? 60.069  66.579  -9.833  1.00 13.42 ? 104 ILE B CB  1 
ATOM   1927  C  CG1 . ILE B  1 131 ? 60.691  67.961  -10.048 1.00 17.17 ? 104 ILE B CG1 1 
ATOM   1928  C  CG2 . ILE B  1 131 ? 58.896  66.383  -10.788 1.00 17.89 ? 104 ILE B CG2 1 
ATOM   1929  C  CD1 . ILE B  1 131 ? 61.581  68.048  -11.336 1.00 18.34 ? 104 ILE B CD1 1 
ATOM   1930  N  N   . SER B  1 132 ? 61.574  65.349  -7.408  1.00 13.48 ? 105 SER B N   1 
ATOM   1931  C  CA  . SER B  1 132 ? 62.769  65.277  -6.580  1.00 15.93 ? 105 SER B CA  1 
ATOM   1932  C  C   . SER B  1 132 ? 63.754  64.342  -7.256  1.00 18.71 ? 105 SER B C   1 
ATOM   1933  O  O   . SER B  1 132 ? 63.379  63.540  -8.107  1.00 16.85 ? 105 SER B O   1 
ATOM   1934  C  CB  . SER B  1 132 ? 62.437  64.755  -5.182  1.00 21.03 ? 105 SER B CB  1 
ATOM   1935  O  OG  . SER B  1 132 ? 63.566  64.854  -4.301  1.00 21.33 ? 105 SER B OG  1 
ATOM   1936  N  N   . LEU B  1 133 ? 65.010  64.421  -6.848  1.00 19.88 ? 106 LEU B N   1 
ATOM   1937  C  CA  . LEU B  1 133 ? 65.988  63.433  -7.291  1.00 21.86 ? 106 LEU B CA  1 
ATOM   1938  C  C   . LEU B  1 133 ? 66.227  62.351  -6.245  1.00 25.32 ? 106 LEU B C   1 
ATOM   1939  O  O   . LEU B  1 133 ? 67.188  61.584  -6.365  1.00 25.83 ? 106 LEU B O   1 
ATOM   1940  C  CB  . LEU B  1 133 ? 67.296  64.126  -7.676  1.00 20.73 ? 106 LEU B CB  1 
ATOM   1941  C  CG  . LEU B  1 133 ? 67.132  65.191  -8.760  1.00 23.23 ? 106 LEU B CG  1 
ATOM   1942  C  CD1 . LEU B  1 133 ? 68.496  65.838  -9.149  1.00 20.92 ? 106 LEU B CD1 1 
ATOM   1943  C  CD2 . LEU B  1 133 ? 66.412  64.606  -9.963  1.00 20.08 ? 106 LEU B CD2 1 
ATOM   1944  N  N   . SER B  1 134 ? 65.367  62.258  -5.237  1.00 22.37 ? 107 SER B N   1 
ATOM   1945  C  CA  . SER B  1 134 ? 65.462  61.207  -4.230  1.00 27.36 ? 107 SER B CA  1 
ATOM   1946  C  C   . SER B  1 134 ? 64.094  61.018  -3.587  1.00 28.54 ? 107 SER B C   1 
ATOM   1947  O  O   . SER B  1 134 ? 63.202  61.861  -3.725  1.00 22.97 ? 107 SER B O   1 
ATOM   1948  C  CB  . SER B  1 134 ? 66.528  61.545  -3.174  1.00 31.80 ? 107 SER B CB  1 
ATOM   1949  O  OG  . SER B  1 134 ? 66.142  62.674  -2.409  1.00 30.26 ? 107 SER B OG  1 
ATOM   1950  N  N   . GLY B  1 135 ? 63.933  59.889  -2.897  1.00 25.21 ? 108 GLY B N   1 
ATOM   1951  C  CA  . GLY B  1 135 ? 62.720  59.635  -2.145  1.00 28.47 ? 108 GLY B CA  1 
ATOM   1952  C  C   . GLY B  1 135 ? 61.542  59.180  -2.997  1.00 23.15 ? 108 GLY B C   1 
ATOM   1953  O  O   . GLY B  1 135 ? 61.679  58.670  -4.122  1.00 26.02 ? 108 GLY B O   1 
ATOM   1954  N  N   . ASP B  1 136 ? 60.347  59.399  -2.433  1.00 23.67 ? 109 ASP B N   1 
ATOM   1955  C  CA  . ASP B  1 136 ? 59.101  58.913  -3.033  1.00 22.74 ? 109 ASP B CA  1 
ATOM   1956  C  C   . ASP B  1 136 ? 58.841  59.543  -4.385  1.00 21.17 ? 109 ASP B C   1 
ATOM   1957  O  O   . ASP B  1 136 ? 58.211  58.929  -5.256  1.00 22.24 ? 109 ASP B O   1 
ATOM   1958  C  CB  . ASP B  1 136 ? 57.911  59.251  -2.133  1.00 31.46 ? 109 ASP B CB  1 
ATOM   1959  C  CG  . ASP B  1 136 ? 57.723  58.264  -1.009  1.00 32.14 ? 109 ASP B CG  1 
ATOM   1960  O  OD1 . ASP B  1 136 ? 58.379  57.193  -1.026  1.00 43.13 ? 109 ASP B OD1 1 
ATOM   1961  O  OD2 . ASP B  1 136 ? 56.882  58.559  -0.135  1.00 29.25 ? 109 ASP B OD2 1 
ATOM   1962  N  N   . HIS B  1 137 ? 59.208  60.810  -4.532  1.00 20.78 ? 110 HIS B N   1 
ATOM   1963  C  CA  . HIS B  1 137 ? 58.945  61.544  -5.754  1.00 25.98 ? 110 HIS B CA  1 
ATOM   1964  C  C   . HIS B  1 137 ? 60.146  61.568  -6.674  1.00 19.51 ? 110 HIS B C   1 
ATOM   1965  O  O   . HIS B  1 137 ? 60.210  62.422  -7.561  1.00 20.13 ? 110 HIS B O   1 
ATOM   1966  C  CB  . HIS B  1 137 ? 58.503  62.963  -5.424  1.00 21.89 ? 110 HIS B CB  1 
ATOM   1967  C  CG  . HIS B  1 137 ? 57.198  63.021  -4.693  1.00 28.63 ? 110 HIS B CG  1 
ATOM   1968  N  ND1 . HIS B  1 137 ? 56.664  64.199  -4.215  1.00 33.57 ? 110 HIS B ND1 1 
ATOM   1969  C  CD2 . HIS B  1 137 ? 56.318  62.042  -4.364  1.00 27.47 ? 110 HIS B CD2 1 
ATOM   1970  C  CE1 . HIS B  1 137 ? 55.519  63.939  -3.606  1.00 30.16 ? 110 HIS B CE1 1 
ATOM   1971  N  NE2 . HIS B  1 137 ? 55.284  62.640  -3.687  1.00 35.62 ? 110 HIS B NE2 1 
ATOM   1972  N  N   . CYS B  1 138 ? 61.088  60.646  -6.475  1.00 15.52 ? 111 CYS B N   1 
ATOM   1973  C  CA  . CYS B  1 138 ? 62.293  60.598  -7.281  1.00 17.49 ? 111 CYS B CA  1 
ATOM   1974  C  C   . CYS B  1 138 ? 61.935  60.335  -8.744  1.00 14.23 ? 111 CYS B C   1 
ATOM   1975  O  O   . CYS B  1 138 ? 61.119  59.469  -9.047  1.00 15.89 ? 111 CYS B O   1 
ATOM   1976  C  CB  . CYS B  1 138 ? 63.222  59.505  -6.740  1.00 19.38 ? 111 CYS B CB  1 
ATOM   1977  S  SG  . CYS B  1 138 ? 64.735  59.347  -7.648  1.00 23.96 ? 111 CYS B SG  1 
ATOM   1978  N  N   . ILE B  1 139 ? 62.538  61.095  -9.650  1.00 13.42 ? 112 ILE B N   1 
ATOM   1979  C  CA  . ILE B  1 139 ? 62.271  60.934  -11.080 1.00 15.20 ? 112 ILE B CA  1 
ATOM   1980  C  C   . ILE B  1 139 ? 63.412  60.240  -11.809 1.00 14.90 ? 112 ILE B C   1 
ATOM   1981  O  O   . ILE B  1 139 ? 63.286  59.967  -13.012 1.00 14.48 ? 112 ILE B O   1 
ATOM   1982  C  CB  . ILE B  1 139 ? 61.961  62.286  -11.751 1.00 14.96 ? 112 ILE B CB  1 
ATOM   1983  C  CG1 . ILE B  1 139 ? 63.127  63.257  -11.615 1.00 13.42 ? 112 ILE B CG1 1 
ATOM   1984  C  CG2 . ILE B  1 139 ? 60.650  62.885  -11.203 1.00 18.15 ? 112 ILE B CG2 1 
ATOM   1985  C  CD1 . ILE B  1 139 ? 62.894  64.547  -12.359 1.00 20.27 ? 112 ILE B CD1 1 
ATOM   1986  N  N   . ILE B  1 140 ? 64.532  59.968  -11.124 1.00 21.39 ? 113 ILE B N   1 
ATOM   1987  C  CA  . ILE B  1 140 ? 65.615  59.169  -11.711 1.00 17.54 ? 113 ILE B CA  1 
ATOM   1988  C  C   . ILE B  1 140 ? 65.067  57.820  -12.142 1.00 17.26 ? 113 ILE B C   1 
ATOM   1989  O  O   . ILE B  1 140 ? 64.358  57.155  -11.378 1.00 15.82 ? 113 ILE B O   1 
ATOM   1990  C  CB  . ILE B  1 140 ? 66.754  58.936  -10.708 1.00 21.16 ? 113 ILE B CB  1 
ATOM   1991  C  CG1 . ILE B  1 140 ? 67.241  60.225  -10.063 1.00 33.06 ? 113 ILE B CG1 1 
ATOM   1992  C  CG2 . ILE B  1 140 ? 67.904  58.151  -11.368 1.00 16.94 ? 113 ILE B CG2 1 
ATOM   1993  C  CD1 . ILE B  1 140 ? 67.820  61.127  -10.996 1.00 30.75 ? 113 ILE B CD1 1 
ATOM   1994  N  N   . GLY B  1 141 ? 65.414  57.395  -13.353 1.00 13.60 ? 114 GLY B N   1 
ATOM   1995  C  CA  . GLY B  1 141 ? 64.932  56.128  -13.857 1.00 13.69 ? 114 GLY B CA  1 
ATOM   1996  C  C   . GLY B  1 141 ? 63.545  56.174  -14.461 1.00 19.08 ? 114 GLY B C   1 
ATOM   1997  O  O   . GLY B  1 141 ? 63.038  55.126  -14.880 1.00 13.79 ? 114 GLY B O   1 
ATOM   1998  N  N   . ARG B  1 142 ? 62.912  57.344  -14.497 1.00 13.42 ? 115 ARG B N   1 
ATOM   1999  C  CA  . ARG B  1 142 ? 61.648  57.524  -15.187 1.00 14.73 ? 115 ARG B CA  1 
ATOM   2000  C  C   . ARG B  1 142 ? 61.917  58.245  -16.507 1.00 16.32 ? 115 ARG B C   1 
ATOM   2001  O  O   . ARG B  1 142 ? 63.063  58.509  -16.864 1.00 16.23 ? 115 ARG B O   1 
ATOM   2002  C  CB  . ARG B  1 142 ? 60.657  58.257  -14.273 1.00 13.42 ? 115 ARG B CB  1 
ATOM   2003  C  CG  . ARG B  1 142 ? 60.602  57.589  -12.868 1.00 15.98 ? 115 ARG B CG  1 
ATOM   2004  C  CD  . ARG B  1 142 ? 59.402  57.987  -12.028 1.00 21.71 ? 115 ARG B CD  1 
ATOM   2005  N  NE  . ARG B  1 142 ? 59.436  57.352  -10.708 1.00 18.66 ? 115 ARG B NE  1 
ATOM   2006  C  CZ  . ARG B  1 142 ? 58.832  56.208  -10.410 1.00 20.74 ? 115 ARG B CZ  1 
ATOM   2007  N  NH1 . ARG B  1 142 ? 58.109  55.550  -11.309 1.00 21.10 ? 115 ARG B NH1 1 
ATOM   2008  N  NH2 . ARG B  1 142 ? 58.891  55.751  -9.159  1.00 21.65 ? 115 ARG B NH2 1 
ATOM   2009  N  N   . THR B  1 143 ? 60.858  58.576  -17.239 1.00 15.26 ? 116 THR B N   1 
ATOM   2010  C  CA  . THR B  1 143 ? 61.018  59.090  -18.601 1.00 13.45 ? 116 THR B CA  1 
ATOM   2011  C  C   . THR B  1 143 ? 60.514  60.521  -18.685 1.00 15.68 ? 116 THR B C   1 
ATOM   2012  O  O   . THR B  1 143 ? 59.384  60.796  -18.286 1.00 17.13 ? 116 THR B O   1 
ATOM   2013  C  CB  . THR B  1 143 ? 60.258  58.233  -19.615 1.00 16.19 ? 116 THR B CB  1 
ATOM   2014  O  OG1 . THR B  1 143 ? 60.790  56.901  -19.630 1.00 18.80 ? 116 THR B OG1 1 
ATOM   2015  C  CG2 . THR B  1 143 ? 60.411  58.828  -21.025 1.00 16.01 ? 116 THR B CG2 1 
ATOM   2016  N  N   . LEU B  1 144 ? 61.342  61.415  -19.211 1.00 13.42 ? 117 LEU B N   1 
ATOM   2017  C  CA  . LEU B  1 144 ? 60.916  62.761  -19.554 1.00 13.42 ? 117 LEU B CA  1 
ATOM   2018  C  C   . LEU B  1 144 ? 60.391  62.734  -20.981 1.00 17.70 ? 117 LEU B C   1 
ATOM   2019  O  O   . LEU B  1 144 ? 61.020  62.129  -21.845 1.00 13.42 ? 117 LEU B O   1 
ATOM   2020  C  CB  . LEU B  1 144 ? 62.078  63.737  -19.466 1.00 13.42 ? 117 LEU B CB  1 
ATOM   2021  C  CG  . LEU B  1 144 ? 61.804  65.219  -19.705 1.00 15.32 ? 117 LEU B CG  1 
ATOM   2022  C  CD1 . LEU B  1 144 ? 60.821  65.750  -18.655 1.00 20.39 ? 117 LEU B CD1 1 
ATOM   2023  C  CD2 . LEU B  1 144 ? 63.108  66.007  -19.660 1.00 13.42 ? 117 LEU B CD2 1 
ATOM   2024  N  N   . VAL B  1 145 ? 59.251  63.386  -21.217 1.00 13.42 ? 118 VAL B N   1 
ATOM   2025  C  CA  . VAL B  1 145 ? 58.605  63.391  -22.532 1.00 15.36 ? 118 VAL B CA  1 
ATOM   2026  C  C   . VAL B  1 145 ? 58.249  64.822  -22.910 1.00 15.94 ? 118 VAL B C   1 
ATOM   2027  O  O   . VAL B  1 145 ? 57.686  65.560  -22.096 1.00 15.19 ? 118 VAL B O   1 
ATOM   2028  C  CB  . VAL B  1 145 ? 57.318  62.534  -22.552 1.00 14.35 ? 118 VAL B CB  1 
ATOM   2029  C  CG1 . VAL B  1 145 ? 56.646  62.616  -23.964 1.00 14.39 ? 118 VAL B CG1 1 
ATOM   2030  C  CG2 . VAL B  1 145 ? 57.592  61.098  -22.140 1.00 17.17 ? 118 VAL B CG2 1 
ATOM   2031  N  N   . VAL B  1 146 ? 58.524  65.208  -24.155 1.00 14.57 ? 119 VAL B N   1 
ATOM   2032  C  CA  . VAL B  1 146 ? 58.024  66.469  -24.678 1.00 16.45 ? 119 VAL B CA  1 
ATOM   2033  C  C   . VAL B  1 146 ? 56.949  66.148  -25.712 1.00 16.74 ? 119 VAL B C   1 
ATOM   2034  O  O   . VAL B  1 146 ? 57.112  65.233  -26.536 1.00 13.51 ? 119 VAL B O   1 
ATOM   2035  C  CB  . VAL B  1 146 ? 59.145  67.367  -25.232 1.00 18.19 ? 119 VAL B CB  1 
ATOM   2036  C  CG1 . VAL B  1 146 ? 59.900  66.705  -26.397 1.00 15.59 ? 119 VAL B CG1 1 
ATOM   2037  C  CG2 . VAL B  1 146 ? 58.569  68.717  -25.669 1.00 19.16 ? 119 VAL B CG2 1 
ATOM   2038  N  N   . HIS B  1 147 ? 55.821  66.847  -25.605 1.00 13.42 ? 120 HIS B N   1 
ATOM   2039  C  CA  . HIS B  1 147 ? 54.596  66.475  -26.293 1.00 14.79 ? 120 HIS B CA  1 
ATOM   2040  C  C   . HIS B  1 147 ? 54.330  67.364  -27.502 1.00 19.20 ? 120 HIS B C   1 
ATOM   2041  O  O   . HIS B  1 147 ? 54.914  68.431  -27.672 1.00 16.27 ? 120 HIS B O   1 
ATOM   2042  C  CB  . HIS B  1 147 ? 53.400  66.524  -25.338 1.00 13.42 ? 120 HIS B CB  1 
ATOM   2043  C  CG  . HIS B  1 147 ? 53.357  65.377  -24.383 1.00 17.44 ? 120 HIS B CG  1 
ATOM   2044  N  ND1 . HIS B  1 147 ? 52.610  64.241  -24.611 1.00 20.29 ? 120 HIS B ND1 1 
ATOM   2045  C  CD2 . HIS B  1 147 ? 53.981  65.186  -23.195 1.00 17.47 ? 120 HIS B CD2 1 
ATOM   2046  C  CE1 . HIS B  1 147 ? 52.757  63.406  -23.596 1.00 18.11 ? 120 HIS B CE1 1 
ATOM   2047  N  NE2 . HIS B  1 147 ? 53.586  63.955  -22.722 1.00 21.05 ? 120 HIS B NE2 1 
ATOM   2048  N  N   . GLU B  1 148 ? 53.382  66.885  -28.314 1.00 17.11 ? 121 GLU B N   1 
ATOM   2049  C  CA  . GLU B  1 148 ? 53.057  67.495  -29.603 1.00 20.58 ? 121 GLU B CA  1 
ATOM   2050  C  C   . GLU B  1 148 ? 52.419  68.871  -29.454 1.00 20.49 ? 121 GLU B C   1 
ATOM   2051  O  O   . GLU B  1 148 ? 52.740  69.786  -30.213 1.00 19.76 ? 121 GLU B O   1 
ATOM   2052  C  CB  . GLU B  1 148 ? 52.149  66.528  -30.376 1.00 21.85 ? 121 GLU B CB  1 
ATOM   2053  C  CG  . GLU B  1 148 ? 51.416  67.099  -31.572 1.00 36.75 ? 121 GLU B CG  1 
ATOM   2054  C  CD  . GLU B  1 148 ? 50.247  66.203  -32.038 1.00 45.36 ? 121 GLU B CD  1 
ATOM   2055  O  OE1 . GLU B  1 148 ? 49.995  66.194  -33.263 1.00 56.69 ? 121 GLU B OE1 1 
ATOM   2056  O  OE2 . GLU B  1 148 ? 49.632  65.470  -31.208 1.00 31.05 ? 121 GLU B OE2 1 
ATOM   2057  N  N   . LYS B  1 149 ? 51.531  69.053  -28.481 1.00 23.01 ? 122 LYS B N   1 
ATOM   2058  C  CA  . LYS B  1 149 ? 50.913  70.368  -28.341 1.00 23.09 ? 122 LYS B CA  1 
ATOM   2059  C  C   . LYS B  1 149 ? 50.888  70.860  -26.907 1.00 20.98 ? 122 LYS B C   1 
ATOM   2060  O  O   . LYS B  1 149 ? 51.517  70.269  -26.017 1.00 19.68 ? 122 LYS B O   1 
ATOM   2061  C  CB  . LYS B  1 149 ? 49.485  70.361  -28.873 1.00 29.30 ? 122 LYS B CB  1 
ATOM   2062  C  CG  . LYS B  1 149 ? 48.798  69.040  -28.863 1.00 26.43 ? 122 LYS B CG  1 
ATOM   2063  C  CD  . LYS B  1 149 ? 47.545  69.160  -29.757 1.00 37.65 ? 122 LYS B CD  1 
ATOM   2064  C  CE  . LYS B  1 149 ? 46.675  67.929  -29.715 1.00 45.16 ? 122 LYS B CE  1 
ATOM   2065  N  NZ  . LYS B  1 149 ? 46.062  67.715  -28.373 1.00 44.64 ? 122 LYS B NZ  1 
ATOM   2066  N  N   . ALA B  1 150 ? 50.156  71.944  -26.678 1.00 17.55 ? 123 ALA B N   1 
ATOM   2067  C  CA  . ALA B  1 150 ? 50.179  72.591  -25.374 1.00 20.74 ? 123 ALA B CA  1 
ATOM   2068  C  C   . ALA B  1 150 ? 49.449  71.757  -24.329 1.00 21.05 ? 123 ALA B C   1 
ATOM   2069  O  O   . ALA B  1 150 ? 48.413  71.148  -24.605 1.00 19.07 ? 123 ALA B O   1 
ATOM   2070  C  CB  . ALA B  1 150 ? 49.547  73.979  -25.461 1.00 24.85 ? 123 ALA B CB  1 
ATOM   2071  N  N   . ASP B  1 151 ? 50.016  71.727  -23.124 1.00 14.37 ? 124 ASP B N   1 
ATOM   2072  C  CA  . ASP B  1 151 ? 49.338  71.212  -21.942 1.00 18.12 ? 124 ASP B CA  1 
ATOM   2073  C  C   . ASP B  1 151 ? 48.264  72.205  -21.515 1.00 16.32 ? 124 ASP B C   1 
ATOM   2074  O  O   . ASP B  1 151 ? 48.586  73.369  -21.272 1.00 18.97 ? 124 ASP B O   1 
ATOM   2075  C  CB  . ASP B  1 151 ? 50.366  71.045  -20.826 1.00 15.75 ? 124 ASP B CB  1 
ATOM   2076  C  CG  . ASP B  1 151 ? 49.834  70.324  -19.614 1.00 21.22 ? 124 ASP B CG  1 
ATOM   2077  O  OD1 . ASP B  1 151 ? 48.615  70.194  -19.424 1.00 15.66 ? 124 ASP B OD1 1 
ATOM   2078  O  OD2 . ASP B  1 151 ? 50.683  69.919  -18.787 1.00 23.41 ? 124 ASP B OD2 1 
ATOM   2079  N  N   . ASP B  1 152 ? 47.005  71.764  -21.398 1.00 16.77 ? 125 ASP B N   1 
ATOM   2080  C  CA  . ASP B  1 152 ? 45.978  72.728  -20.977 1.00 22.13 ? 125 ASP B CA  1 
ATOM   2081  C  C   . ASP B  1 152 ? 45.908  72.870  -19.458 1.00 23.64 ? 125 ASP B C   1 
ATOM   2082  O  O   . ASP B  1 152 ? 45.041  73.594  -18.929 1.00 20.15 ? 125 ASP B O   1 
ATOM   2083  C  CB  . ASP B  1 152 ? 44.599  72.384  -21.582 1.00 23.85 ? 125 ASP B CB  1 
ATOM   2084  C  CG  . ASP B  1 152 ? 43.970  71.082  -21.044 1.00 20.28 ? 125 ASP B CG  1 
ATOM   2085  O  OD1 . ASP B  1 152 ? 44.360  70.565  -19.983 1.00 21.54 ? 125 ASP B OD1 1 
ATOM   2086  O  OD2 . ASP B  1 152 ? 43.036  70.566  -21.711 1.00 20.18 ? 125 ASP B OD2 1 
ATOM   2087  N  N   . LEU B  1 153 ? 46.807  72.187  -18.752 1.00 17.06 ? 126 LEU B N   1 
ATOM   2088  C  CA  . LEU B  1 153 ? 47.004  72.338  -17.307 1.00 19.86 ? 126 LEU B CA  1 
ATOM   2089  C  C   . LEU B  1 153 ? 45.786  71.882  -16.523 1.00 14.53 ? 126 LEU B C   1 
ATOM   2090  O  O   . LEU B  1 153 ? 45.564  72.312  -15.388 1.00 20.20 ? 126 LEU B O   1 
ATOM   2091  C  CB  . LEU B  1 153 ? 47.380  73.775  -16.943 1.00 23.22 ? 126 LEU B CB  1 
ATOM   2092  C  CG  . LEU B  1 153 ? 48.543  74.313  -17.774 1.00 25.51 ? 126 LEU B CG  1 
ATOM   2093  C  CD1 . LEU B  1 153 ? 48.822  75.756  -17.437 1.00 27.36 ? 126 LEU B CD1 1 
ATOM   2094  C  CD2 . LEU B  1 153 ? 49.803  73.455  -17.618 1.00 20.88 ? 126 LEU B CD2 1 
ATOM   2095  N  N   . GLY B  1 154 ? 45.018  70.967  -17.097 1.00 19.36 ? 127 GLY B N   1 
ATOM   2096  C  CA  . GLY B  1 154 ? 43.851  70.454  -16.416 1.00 22.66 ? 127 GLY B CA  1 
ATOM   2097  C  C   . GLY B  1 154 ? 42.615  71.322  -16.520 1.00 21.99 ? 127 GLY B C   1 
ATOM   2098  O  O   . GLY B  1 154 ? 41.610  71.010  -15.878 1.00 20.24 ? 127 GLY B O   1 
ATOM   2099  N  N   . LYS B  1 155 ? 42.647  72.381  -17.326 1.00 22.02 ? 128 LYS B N   1 
ATOM   2100  C  CA  . LYS B  1 155 ? 41.548  73.334  -17.424 1.00 22.91 ? 128 LYS B CA  1 
ATOM   2101  C  C   . LYS B  1 155 ? 40.723  73.161  -18.697 1.00 23.76 ? 128 LYS B C   1 
ATOM   2102  O  O   . LYS B  1 155 ? 40.023  74.095  -19.090 1.00 24.34 ? 128 LYS B O   1 
ATOM   2103  C  CB  . LYS B  1 155 ? 42.090  74.764  -17.363 1.00 20.53 ? 128 LYS B CB  1 
ATOM   2104  C  CG  . LYS B  1 155 ? 42.825  75.113  -16.085 1.00 27.39 ? 128 LYS B CG  1 
ATOM   2105  C  CD  . LYS B  1 155 ? 43.468  76.493  -16.244 1.00 37.56 ? 128 LYS B CD  1 
ATOM   2106  C  CE  . LYS B  1 155 ? 44.179  76.923  -14.981 1.00 40.85 ? 128 LYS B CE  1 
ATOM   2107  N  NZ  . LYS B  1 155 ? 43.555  76.279  -13.795 1.00 44.72 ? 128 LYS B NZ  1 
ATOM   2108  N  N   . GLY B  1 156 ? 40.803  71.997  -19.360 1.00 18.03 ? 129 GLY B N   1 
ATOM   2109  C  CA  . GLY B  1 156 ? 40.120  71.807  -20.635 1.00 21.30 ? 129 GLY B CA  1 
ATOM   2110  C  C   . GLY B  1 156 ? 38.675  71.339  -20.566 1.00 24.26 ? 129 GLY B C   1 
ATOM   2111  O  O   . GLY B  1 156 ? 38.004  71.276  -21.604 1.00 20.52 ? 129 GLY B O   1 
ATOM   2112  N  N   . GLY B  1 157 ? 38.195  70.976  -19.376 1.00 22.03 ? 130 GLY B N   1 
ATOM   2113  C  CA  . GLY B  1 157 ? 36.797  70.631  -19.179 1.00 18.75 ? 130 GLY B CA  1 
ATOM   2114  C  C   . GLY B  1 157 ? 36.374  69.278  -19.692 1.00 24.77 ? 130 GLY B C   1 
ATOM   2115  O  O   . GLY B  1 157 ? 35.171  69.023  -19.819 1.00 27.01 ? 130 GLY B O   1 
ATOM   2116  N  N   . ASN B  1 158 ? 37.339  68.409  -19.952 1.00 26.10 ? 131 ASN B N   1 
ATOM   2117  C  CA  . ASN B  1 158 ? 37.042  67.035  -20.407 1.00 25.58 ? 131 ASN B CA  1 
ATOM   2118  C  C   . ASN B  1 158 ? 37.896  66.049  -19.607 1.00 28.07 ? 131 ASN B C   1 
ATOM   2119  O  O   . ASN B  1 158 ? 38.812  66.474  -18.948 1.00 25.06 ? 131 ASN B O   1 
ATOM   2120  C  CB  . ASN B  1 158 ? 37.099  66.929  -21.925 1.00 26.18 ? 131 ASN B CB  1 
ATOM   2121  C  CG  . ASN B  1 158 ? 38.491  67.084  -22.481 1.00 30.27 ? 131 ASN B CG  1 
ATOM   2122  O  OD1 . ASN B  1 158 ? 39.449  67.211  -21.746 1.00 24.27 ? 131 ASN B OD1 1 
ATOM   2123  N  ND2 . ASN B  1 158 ? 38.590  67.072  -23.790 1.00 27.67 ? 131 ASN B ND2 1 
ATOM   2124  N  N   . GLU B  1 159 ? 37.559  64.767  -19.681 1.00 25.21 ? 132 GLU B N   1 
ATOM   2125  C  CA  . GLU B  1 159 ? 38.277  63.697  -18.948 1.00 31.78 ? 132 GLU B CA  1 
ATOM   2126  C  C   . GLU B  1 159 ? 39.756  63.654  -19.366 1.00 25.53 ? 132 GLU B C   1 
ATOM   2127  O  O   . GLU B  1 159 ? 40.601  63.502  -18.527 1.00 24.28 ? 132 GLU B O   1 
ATOM   2128  C  CB  . GLU B  1 159 ? 37.574  62.356  -19.150 1.00 34.59 ? 132 GLU B CB  1 
ATOM   2129  C  CG  . GLU B  1 159 ? 38.198  61.214  -18.378 1.00 49.29 ? 132 GLU B CG  1 
ATOM   2130  C  CD  . GLU B  1 159 ? 37.591  59.817  -18.432 1.00 64.28 ? 132 GLU B CD  1 
ATOM   2131  O  OE1 . GLU B  1 159 ? 36.567  59.646  -19.181 1.00 37.83 ? 132 GLU B OE1 1 
ATOM   2132  O  OE2 . GLU B  1 159 ? 38.153  58.907  -17.732 1.00 36.95 ? 132 GLU B OE2 1 
ATOM   2133  N  N   . GLU B  1 160 ? 40.037  63.850  -20.640 1.00 26.81 ? 133 GLU B N   1 
ATOM   2134  C  CA  . GLU B  1 160 ? 41.435  63.844  -21.123 1.00 29.79 ? 133 GLU B CA  1 
ATOM   2135  C  C   . GLU B  1 160 ? 42.235  64.949  -20.411 1.00 28.26 ? 133 GLU B C   1 
ATOM   2136  O  O   . GLU B  1 160 ? 43.357  64.720  -20.050 1.00 23.64 ? 133 GLU B O   1 
ATOM   2137  C  CB  . GLU B  1 160 ? 41.424  64.016  -22.633 1.00 27.39 ? 133 GLU B CB  1 
ATOM   2138  C  CG  . GLU B  1 160 ? 42.726  63.671  -23.289 1.00 36.76 ? 133 GLU B CG  1 
ATOM   2139  C  CD  . GLU B  1 160 ? 43.136  62.232  -23.107 1.00 45.35 ? 133 GLU B CD  1 
ATOM   2140  O  OE1 . GLU B  1 160 ? 42.368  61.351  -23.484 1.00 54.52 ? 133 GLU B OE1 1 
ATOM   2141  O  OE2 . GLU B  1 160 ? 44.194  62.012  -22.573 1.00 43.15 ? 133 GLU B OE2 1 
ATOM   2142  N  N   . SER B  1 161 ? 41.648  66.122  -20.239 1.00 23.22 ? 134 SER B N   1 
ATOM   2143  C  CA  . SER B  1 161 ? 42.357  67.234  -19.569 1.00 20.68 ? 134 SER B CA  1 
ATOM   2144  C  C   . SER B  1 161 ? 42.855  66.811  -18.184 1.00 21.29 ? 134 SER B C   1 
ATOM   2145  O  O   . SER B  1 161 ? 43.949  67.211  -17.841 1.00 15.59 ? 134 SER B O   1 
ATOM   2146  C  CB  . SER B  1 161 ? 41.508  68.466  -19.507 1.00 23.92 ? 134 SER B CB  1 
ATOM   2147  O  OG  . SER B  1 161 ? 42.188  69.544  -18.931 1.00 22.00 ? 134 SER B OG  1 
ATOM   2148  N  N   . THR B  1 162 ? 42.057  66.013  -17.466 1.00 17.13 ? 135 THR B N   1 
ATOM   2149  C  CA  . THR B  1 162 ? 42.404  65.603  -16.116 1.00 20.71 ? 135 THR B CA  1 
ATOM   2150  C  C   . THR B  1 162 ? 43.393  64.455  -16.097 1.00 21.63 ? 135 THR B C   1 
ATOM   2151  O  O   . THR B  1 162 ? 43.796  64.031  -15.008 1.00 22.34 ? 135 THR B O   1 
ATOM   2152  C  CB  . THR B  1 162 ? 41.146  65.171  -15.337 1.00 26.97 ? 135 THR B CB  1 
ATOM   2153  O  OG1 . THR B  1 162 ? 40.662  63.926  -15.864 1.00 34.54 ? 135 THR B OG1 1 
ATOM   2154  C  CG2 . THR B  1 162 ? 40.059  66.188  -15.460 1.00 26.78 ? 135 THR B CG2 1 
ATOM   2155  N  N   . LYS B  1 163 ? 43.742  63.914  -17.266 1.00 23.19 ? 136 LYS B N   1 
ATOM   2156  C  CA  . LYS B  1 163 ? 44.705  62.823  -17.376 1.00 26.76 ? 136 LYS B CA  1 
ATOM   2157  C  C   . LYS B  1 163 ? 46.011  63.259  -18.019 1.00 23.39 ? 136 LYS B C   1 
ATOM   2158  O  O   . LYS B  1 163 ? 47.087  62.986  -17.480 1.00 24.16 ? 136 LYS B O   1 
ATOM   2159  C  CB  . LYS B  1 163 ? 44.111  61.654  -18.181 1.00 28.44 ? 136 LYS B CB  1 
ATOM   2160  C  CG  . LYS B  1 163 ? 42.829  61.095  -17.605 1.00 37.17 ? 136 LYS B CG  1 
ATOM   2161  C  CD  . LYS B  1 163 ? 42.655  59.635  -18.003 1.00 38.77 ? 136 LYS B CD  1 
ATOM   2162  C  CE  . LYS B  1 163 ? 42.333  59.485  -19.480 1.00 46.19 ? 136 LYS B CE  1 
ATOM   2163  N  NZ  . LYS B  1 163 ? 41.103  60.236  -19.915 1.00 47.53 ? 136 LYS B NZ  1 
ATOM   2164  N  N   . THR B  1 164 ? 45.939  63.931  -19.172 1.00 21.68 ? 137 THR B N   1 
ATOM   2165  C  CA  . THR B  1 164 ? 47.108  64.257  -19.980 1.00 25.25 ? 137 THR B CA  1 
ATOM   2166  C  C   . THR B  1 164 ? 47.228  65.733  -20.302 1.00 23.26 ? 137 THR B C   1 
ATOM   2167  O  O   . THR B  1 164 ? 48.188  66.124  -20.979 1.00 21.58 ? 137 THR B O   1 
ATOM   2168  C  CB  . THR B  1 164 ? 47.073  63.495  -21.312 1.00 27.37 ? 137 THR B CB  1 
ATOM   2169  O  OG1 . THR B  1 164 ? 45.962  63.972  -22.092 1.00 26.04 ? 137 THR B OG1 1 
ATOM   2170  C  CG2 . THR B  1 164 ? 46.915  62.005  -21.061 1.00 32.44 ? 137 THR B CG2 1 
ATOM   2171  N  N   . GLY B  1 165 ? 46.255  66.554  -19.906 1.00 21.60 ? 138 GLY B N   1 
ATOM   2172  C  CA  . GLY B  1 165 ? 46.265  67.934  -20.337 1.00 18.80 ? 138 GLY B CA  1 
ATOM   2173  C  C   . GLY B  1 165 ? 45.988  68.138  -21.810 1.00 17.39 ? 138 GLY B C   1 
ATOM   2174  O  O   . GLY B  1 165 ? 46.192  69.247  -22.313 1.00 16.63 ? 138 GLY B O   1 
ATOM   2175  N  N   . ASN B  1 166 ? 45.522  67.104  -22.517 1.00 18.63 ? 139 ASN B N   1 
ATOM   2176  C  CA  . ASN B  1 166 ? 45.302  67.181  -23.967 1.00 19.70 ? 139 ASN B CA  1 
ATOM   2177  C  C   . ASN B  1 166 ? 46.573  67.558  -24.733 1.00 20.35 ? 139 ASN B C   1 
ATOM   2178  O  O   . ASN B  1 166 ? 46.499  68.210  -25.779 1.00 20.90 ? 139 ASN B O   1 
ATOM   2179  C  CB  . ASN B  1 166 ? 44.165  68.162  -24.301 1.00 22.89 ? 139 ASN B CB  1 
ATOM   2180  C  CG  . ASN B  1 166 ? 42.809  67.620  -23.892 1.00 22.90 ? 139 ASN B CG  1 
ATOM   2181  O  OD1 . ASN B  1 166 ? 42.364  66.611  -24.430 1.00 29.23 ? 139 ASN B OD1 1 
ATOM   2182  N  ND2 . ASN B  1 166 ? 42.172  68.255  -22.893 1.00 22.01 ? 139 ASN B ND2 1 
ATOM   2183  N  N   . ALA B  1 167 ? 47.753  67.145  -24.249 1.00 20.41 ? 140 ALA B N   1 
ATOM   2184  C  CA  . ALA B  1 167 ? 49.006  67.574  -24.876 1.00 18.62 ? 140 ALA B CA  1 
ATOM   2185  C  C   . ALA B  1 167 ? 49.374  66.746  -26.107 1.00 20.08 ? 140 ALA B C   1 
ATOM   2186  O  O   . ALA B  1 167 ? 50.384  67.041  -26.761 1.00 19.11 ? 140 ALA B O   1 
ATOM   2187  C  CB  . ALA B  1 167 ? 50.153  67.544  -23.848 1.00 15.60 ? 140 ALA B CB  1 
ATOM   2188  N  N   . GLY B  1 168 ? 48.608  65.702  -26.421 1.00 22.47 ? 141 GLY B N   1 
ATOM   2189  C  CA  . GLY B  1 168 ? 48.796  64.992  -27.663 1.00 26.71 ? 141 GLY B CA  1 
ATOM   2190  C  C   . GLY B  1 168 ? 49.997  64.063  -27.643 1.00 26.83 ? 141 GLY B C   1 
ATOM   2191  O  O   . GLY B  1 168 ? 50.464  63.600  -26.602 1.00 21.79 ? 141 GLY B O   1 
ATOM   2192  N  N   . SER B  1 169 ? 50.522  63.804  -28.832 1.00 21.64 ? 142 SER B N   1 
ATOM   2193  C  CA  . SER B  1 169 ? 51.433  62.687  -28.988 1.00 18.38 ? 142 SER B CA  1 
ATOM   2194  C  C   . SER B  1 169 ? 52.801  63.007  -28.379 1.00 18.60 ? 142 SER B C   1 
ATOM   2195  O  O   . SER B  1 169 ? 53.121  64.143  -28.040 1.00 17.42 ? 142 SER B O   1 
ATOM   2196  C  CB  . SER B  1 169 ? 51.555  62.319  -30.477 1.00 25.55 ? 142 SER B CB  1 
ATOM   2197  O  OG  . SER B  1 169 ? 52.384  63.256  -31.120 1.00 31.13 ? 142 SER B OG  1 
ATOM   2198  N  N   . ARG B  1 170 ? 53.619  61.969  -28.252 1.00 19.21 ? 143 ARG B N   1 
ATOM   2199  C  CA  . ARG B  1 170 ? 54.929  62.069  -27.620 1.00 21.15 ? 143 ARG B CA  1 
ATOM   2200  C  C   . ARG B  1 170 ? 55.993  62.292  -28.692 1.00 22.71 ? 143 ARG B C   1 
ATOM   2201  O  O   . ARG B  1 170 ? 56.261  61.405  -29.503 1.00 25.45 ? 143 ARG B O   1 
ATOM   2202  C  CB  . ARG B  1 170 ? 55.172  60.806  -26.802 1.00 18.42 ? 143 ARG B CB  1 
ATOM   2203  C  CG  . ARG B  1 170 ? 54.014  60.548  -25.833 1.00 21.43 ? 143 ARG B CG  1 
ATOM   2204  C  CD  . ARG B  1 170 ? 54.076  59.191  -25.140 1.00 20.91 ? 143 ARG B CD  1 
ATOM   2205  N  NE  . ARG B  1 170 ? 52.936  59.029  -24.246 1.00 21.29 ? 143 ARG B NE  1 
ATOM   2206  C  CZ  . ARG B  1 170 ? 52.908  58.257  -23.166 1.00 23.37 ? 143 ARG B CZ  1 
ATOM   2207  N  NH1 . ARG B  1 170 ? 53.951  57.513  -22.807 1.00 22.91 ? 143 ARG B NH1 1 
ATOM   2208  N  NH2 . ARG B  1 170 ? 51.813  58.246  -22.408 1.00 21.57 ? 143 ARG B NH2 1 
ATOM   2209  N  N   . LEU B  1 171 ? 56.599  63.477  -28.706 1.00 17.62 ? 144 LEU B N   1 
ATOM   2210  C  CA  . LEU B  1 171 ? 57.518  63.806  -29.791 1.00 16.88 ? 144 LEU B CA  1 
ATOM   2211  C  C   . LEU B  1 171 ? 58.912  63.253  -29.542 1.00 20.04 ? 144 LEU B C   1 
ATOM   2212  O  O   . LEU B  1 171 ? 59.600  62.843  -30.482 1.00 16.74 ? 144 LEU B O   1 
ATOM   2213  C  CB  . LEU B  1 171 ? 57.587  65.315  -29.969 1.00 17.39 ? 144 LEU B CB  1 
ATOM   2214  C  CG  . LEU B  1 171 ? 56.283  65.998  -30.385 1.00 22.59 ? 144 LEU B CG  1 
ATOM   2215  C  CD1 . LEU B  1 171 ? 56.589  67.445  -30.738 1.00 25.20 ? 144 LEU B CD1 1 
ATOM   2216  C  CD2 . LEU B  1 171 ? 55.620  65.272  -31.560 1.00 31.16 ? 144 LEU B CD2 1 
ATOM   2217  N  N   . ALA B  1 172 ? 59.359  63.255  -28.286 1.00 20.16 ? 145 ALA B N   1 
ATOM   2218  C  CA  . ALA B  1 172 ? 60.691  62.765  -27.956 1.00 16.54 ? 145 ALA B CA  1 
ATOM   2219  C  C   . ALA B  1 172 ? 60.711  62.455  -26.470 1.00 17.53 ? 145 ALA B C   1 
ATOM   2220  O  O   . ALA B  1 172 ? 59.961  63.068  -25.703 1.00 15.75 ? 145 ALA B O   1 
ATOM   2221  C  CB  . ALA B  1 172 ? 61.770  63.793  -28.285 1.00 20.44 ? 145 ALA B CB  1 
ATOM   2222  N  N   . CYS B  1 173 ? 61.582  61.531  -26.074 1.00 14.00 ? 146 CYS B N   1 
ATOM   2223  C  CA  . CYS B  1 173 ? 61.659  61.154  -24.666 1.00 15.25 ? 146 CYS B CA  1 
ATOM   2224  C  C   . CYS B  1 173 ? 63.037  60.588  -24.349 1.00 19.86 ? 146 CYS B C   1 
ATOM   2225  O  O   . CYS B  1 173 ? 63.853  60.352  -25.229 1.00 17.94 ? 146 CYS B O   1 
ATOM   2226  C  CB  . CYS B  1 173 ? 60.586  60.133  -24.309 1.00 20.68 ? 146 CYS B CB  1 
ATOM   2227  S  SG  . CYS B  1 173 ? 60.708  58.619  -25.290 1.00 24.51 ? 146 CYS B SG  1 
ATOM   2228  N  N   . GLY B  1 174 ? 63.284  60.366  -23.066 1.00 19.77 ? 147 GLY B N   1 
ATOM   2229  C  CA  . GLY B  1 174 ? 64.486  59.674  -22.647 1.00 18.05 ? 147 GLY B CA  1 
ATOM   2230  C  C   . GLY B  1 174 ? 64.390  59.339  -21.179 1.00 16.72 ? 147 GLY B C   1 
ATOM   2231  O  O   . GLY B  1 174 ? 63.597  59.938  -20.440 1.00 15.55 ? 147 GLY B O   1 
ATOM   2232  N  N   . VAL B  1 175 ? 65.198  58.365  -20.769 1.00 13.42 ? 148 VAL B N   1 
ATOM   2233  C  CA  . VAL B  1 175 ? 65.265  57.983  -19.361 1.00 13.42 ? 148 VAL B CA  1 
ATOM   2234  C  C   . VAL B  1 175 ? 66.139  58.979  -18.613 1.00 15.82 ? 148 VAL B C   1 
ATOM   2235  O  O   . VAL B  1 175 ? 67.212  59.365  -19.088 1.00 17.13 ? 148 VAL B O   1 
ATOM   2236  C  CB  . VAL B  1 175 ? 65.800  56.544  -19.221 1.00 18.60 ? 148 VAL B CB  1 
ATOM   2237  C  CG1 . VAL B  1 175 ? 65.778  56.085  -17.763 1.00 14.36 ? 148 VAL B CG1 1 
ATOM   2238  C  CG2 . VAL B  1 175 ? 64.980  55.596  -20.121 1.00 20.47 ? 148 VAL B CG2 1 
ATOM   2239  N  N   . ILE B  1 176 ? 65.678  59.404  -17.438 1.00 13.42 ? 149 ILE B N   1 
ATOM   2240  C  CA  . ILE B  1 176 ? 66.413  60.352  -16.605 1.00 16.48 ? 149 ILE B CA  1 
ATOM   2241  C  C   . ILE B  1 176 ? 67.485  59.585  -15.836 1.00 13.42 ? 149 ILE B C   1 
ATOM   2242  O  O   . ILE B  1 176 ? 67.173  58.664  -15.080 1.00 17.65 ? 149 ILE B O   1 
ATOM   2243  C  CB  . ILE B  1 176 ? 65.455  61.081  -15.646 1.00 15.48 ? 149 ILE B CB  1 
ATOM   2244  C  CG1 . ILE B  1 176 ? 64.384  61.838  -16.469 1.00 17.19 ? 149 ILE B CG1 1 
ATOM   2245  C  CG2 . ILE B  1 176 ? 66.231  62.042  -14.744 1.00 14.61 ? 149 ILE B CG2 1 
ATOM   2246  C  CD1 . ILE B  1 176 ? 63.101  62.255  -15.657 1.00 14.63 ? 149 ILE B CD1 1 
ATOM   2247  N  N   . GLY B  1 177 ? 68.744  59.967  -16.015 1.00 16.22 ? 150 GLY B N   1 
ATOM   2248  C  CA  . GLY B  1 177 ? 69.822  59.234  -15.373 1.00 18.59 ? 150 GLY B CA  1 
ATOM   2249  C  C   . GLY B  1 177 ? 70.627  60.053  -14.375 1.00 20.93 ? 150 GLY B C   1 
ATOM   2250  O  O   . GLY B  1 177 ? 70.601  61.288  -14.418 1.00 15.01 ? 150 GLY B O   1 
ATOM   2251  N  N   . ILE B  1 178 ? 71.355  59.373  -13.484 1.00 16.56 ? 151 ILE B N   1 
ATOM   2252  C  CA  . ILE B  1 178 ? 72.225  60.055  -12.521 1.00 15.68 ? 151 ILE B CA  1 
ATOM   2253  C  C   . ILE B  1 178 ? 73.397  60.680  -13.255 1.00 20.55 ? 151 ILE B C   1 
ATOM   2254  O  O   . ILE B  1 178 ? 74.013  60.046  -14.124 1.00 22.28 ? 151 ILE B O   1 
ATOM   2255  C  CB  . ILE B  1 178 ? 72.735  59.066  -11.457 1.00 20.37 ? 151 ILE B CB  1 
ATOM   2256  C  CG1 . ILE B  1 178 ? 71.576  58.277  -10.869 1.00 29.76 ? 151 ILE B CG1 1 
ATOM   2257  C  CG2 . ILE B  1 178 ? 73.496  59.803  -10.352 1.00 25.58 ? 151 ILE B CG2 1 
ATOM   2258  C  CD1 . ILE B  1 178 ? 71.966  57.395  -9.723  1.00 34.11 ? 151 ILE B CD1 1 
ATOM   2259  N  N   . ALA B  1 179 ? 73.740  61.912  -12.891 1.00 14.75 ? 152 ALA B N   1 
ATOM   2260  C  CA  . ALA B  1 179 ? 74.781  62.672  -13.568 1.00 20.10 ? 152 ALA B CA  1 
ATOM   2261  C  C   . ALA B  1 179 ? 75.880  63.079  -12.590 1.00 24.20 ? 152 ALA B C   1 
ATOM   2262  O  O   . ALA B  1 179 ? 75.690  63.081  -11.371 1.00 26.20 ? 152 ALA B O   1 
ATOM   2263  C  CB  . ALA B  1 179 ? 74.207  63.924  -14.250 1.00 22.16 ? 152 ALA B CB  1 
ATOM   2264  N  N   . GLN B  1 180 ? 77.045  63.403  -13.146 1.00 30.14 ? 153 GLN B N   1 
ATOM   2265  C  CA  . GLN B  1 180 ? 78.209  63.785  -12.337 1.00 39.79 ? 153 GLN B CA  1 
ATOM   2266  C  C   . GLN B  1 180 ? 78.020  65.195  -11.803 1.00 49.10 ? 153 GLN B C   1 
ATOM   2267  O  O   . GLN B  1 180 ? 78.143  66.191  -12.534 1.00 49.15 ? 153 GLN B O   1 
ATOM   2268  C  CB  . GLN B  1 180 ? 79.520  63.677  -13.150 1.00 38.16 ? 153 GLN B CB  1 
ATOM   2269  C  CG  . GLN B  1 180 ? 80.761  63.346  -12.286 1.00 46.25 ? 153 GLN B CG  1 
ATOM   2270  C  CD  . GLN B  1 180 ? 81.945  62.806  -13.084 1.00 50.43 ? 153 GLN B CD  1 
ATOM   2271  O  OE1 . GLN B  1 180 ? 83.012  62.504  -12.516 1.00 47.37 ? 153 GLN B OE1 1 
ATOM   2272  N  NE2 . GLN B  1 180 ? 81.755  62.641  -14.397 1.00 40.93 ? 153 GLN B NE2 1 
ATOM   2273  O  OXT . GLN B  1 180 ? 77.726  65.350  -10.613 1.00 62.35 ? 153 GLN B OXT 1 
ATOM   2274  N  N   . MET C  1 27  ? 65.648  108.525 -3.347  1.00 51.80 ? 0   MET D N   1 
ATOM   2275  C  CA  . MET C  1 27  ? 65.973  107.346 -4.154  1.00 52.42 ? 0   MET D CA  1 
ATOM   2276  C  C   . MET C  1 27  ? 66.519  107.718 -5.551  1.00 48.70 ? 0   MET D C   1 
ATOM   2277  O  O   . MET C  1 27  ? 67.678  107.408 -5.854  1.00 46.71 ? 0   MET D O   1 
ATOM   2278  C  CB  . MET C  1 27  ? 64.741  106.422 -4.279  1.00 41.75 ? 0   MET D CB  1 
ATOM   2279  N  N   . ALA C  1 28  ? 65.713  108.386 -6.392  1.00 45.31 ? 1   ALA D N   1 
ATOM   2280  C  CA  . ALA C  1 28  ? 66.138  108.673 -7.765  1.00 36.36 ? 1   ALA D CA  1 
ATOM   2281  C  C   . ALA C  1 28  ? 67.314  109.646 -7.782  1.00 27.48 ? 1   ALA D C   1 
ATOM   2282  O  O   . ALA C  1 28  ? 67.225  110.750 -7.238  1.00 35.08 ? 1   ALA D O   1 
ATOM   2283  C  CB  . ALA C  1 28  ? 64.980  109.239 -8.590  1.00 36.77 ? 1   ALA D CB  1 
ATOM   2284  N  N   . THR C  1 29  ? 68.413  109.234 -8.413  1.00 30.22 ? 2   THR D N   1 
ATOM   2285  C  CA  . THR C  1 29  ? 69.571  110.094 -8.612  1.00 31.92 ? 2   THR D CA  1 
ATOM   2286  C  C   . THR C  1 29  ? 69.743  110.596 -10.047 1.00 32.92 ? 2   THR D C   1 
ATOM   2287  O  O   . THR C  1 29  ? 70.561  111.497 -10.273 1.00 26.59 ? 2   THR D O   1 
ATOM   2288  C  CB  . THR C  1 29  ? 70.847  109.358 -8.181  1.00 34.08 ? 2   THR D CB  1 
ATOM   2289  O  OG1 . THR C  1 29  ? 71.067  108.236 -9.044  1.00 36.77 ? 2   THR D OG1 1 
ATOM   2290  C  CG2 . THR C  1 29  ? 70.734  108.888 -6.717  1.00 33.43 ? 2   THR D CG2 1 
ATOM   2291  N  N   . LYS C  1 30  ? 69.011  110.041 -11.014 1.00 28.83 ? 3   LYS D N   1 
ATOM   2292  C  CA  . LYS C  1 30  ? 69.106  110.458 -12.414 1.00 22.02 ? 3   LYS D CA  1 
ATOM   2293  C  C   . LYS C  1 30  ? 67.715  110.486 -13.029 1.00 28.83 ? 3   LYS D C   1 
ATOM   2294  O  O   . LYS C  1 30  ? 66.875  109.632 -12.728 1.00 23.19 ? 3   LYS D O   1 
ATOM   2295  C  CB  . LYS C  1 30  ? 70.004  109.512 -13.214 1.00 26.18 ? 3   LYS D CB  1 
ATOM   2296  C  CG  . LYS C  1 30  ? 71.461  109.511 -12.775 1.00 38.82 ? 3   LYS D CG  1 
ATOM   2297  C  CD  . LYS C  1 30  ? 72.393  108.924 -13.838 1.00 49.06 ? 3   LYS D CD  1 
ATOM   2298  C  CE  . LYS C  1 30  ? 72.423  109.749 -15.114 1.00 50.95 ? 3   LYS D CE  1 
ATOM   2299  N  NZ  . LYS C  1 30  ? 73.807  110.216 -15.487 1.00 58.57 ? 3   LYS D NZ  1 
ATOM   2300  N  N   . ALA C  1 31  ? 67.473  111.475 -13.889 1.00 24.23 ? 4   ALA D N   1 
ATOM   2301  C  CA  . ALA C  1 31  ? 66.226  111.568 -14.635 1.00 20.32 ? 4   ALA D CA  1 
ATOM   2302  C  C   . ALA C  1 31  ? 66.556  112.062 -16.043 1.00 22.60 ? 4   ALA D C   1 
ATOM   2303  O  O   . ALA C  1 31  ? 67.675  112.503 -16.322 1.00 21.59 ? 4   ALA D O   1 
ATOM   2304  C  CB  . ALA C  1 31  ? 65.210  112.482 -13.933 1.00 20.20 ? 4   ALA D CB  1 
ATOM   2305  N  N   . VAL C  1 32  ? 65.597  111.937 -16.961 1.00 20.81 ? 5   VAL D N   1 
ATOM   2306  C  CA  . VAL C  1 32  ? 65.806  112.377 -18.340 1.00 16.30 ? 5   VAL D CA  1 
ATOM   2307  C  C   . VAL C  1 32  ? 64.460  112.808 -18.902 1.00 21.74 ? 5   VAL D C   1 
ATOM   2308  O  O   . VAL C  1 32  ? 63.399  112.402 -18.420 1.00 19.25 ? 5   VAL D O   1 
ATOM   2309  C  CB  . VAL C  1 32  ? 66.470  111.265 -19.202 1.00 20.41 ? 5   VAL D CB  1 
ATOM   2310  C  CG1 . VAL C  1 32  ? 65.550  110.050 -19.321 1.00 20.43 ? 5   VAL D CG1 1 
ATOM   2311  C  CG2 . VAL C  1 32  ? 66.903  111.784 -20.598 1.00 24.08 ? 5   VAL D CG2 1 
ATOM   2312  N  N   . CYS C  1 33  ? 64.498  113.663 -19.924 1.00 19.86 ? 6   CYS D N   1 
ATOM   2313  C  CA  . CYS C  1 33  ? 63.262  114.170 -20.501 1.00 16.00 ? 6   CYS D CA  1 
ATOM   2314  C  C   . CYS C  1 33  ? 63.488  114.315 -21.995 1.00 21.49 ? 6   CYS D C   1 
ATOM   2315  O  O   . CYS C  1 33  ? 64.510  114.882 -22.393 1.00 20.58 ? 6   CYS D O   1 
ATOM   2316  C  CB  . CYS C  1 33  ? 62.891  115.524 -19.894 1.00 18.42 ? 6   CYS D CB  1 
ATOM   2317  S  SG  . CYS C  1 33  ? 61.371  116.240 -20.541 1.00 23.15 ? 6   CYS D SG  1 
ATOM   2318  N  N   . VAL C  1 34  ? 62.590  113.759 -22.802 1.00 15.61 ? 7   VAL D N   1 
ATOM   2319  C  CA  . VAL C  1 34  ? 62.628  113.936 -24.258 1.00 19.77 ? 7   VAL D CA  1 
ATOM   2320  C  C   . VAL C  1 34  ? 61.562  114.957 -24.621 1.00 18.96 ? 7   VAL D C   1 
ATOM   2321  O  O   . VAL C  1 34  ? 60.368  114.710 -24.416 1.00 19.17 ? 7   VAL D O   1 
ATOM   2322  C  CB  . VAL C  1 34  ? 62.394  112.611 -24.993 1.00 21.11 ? 7   VAL D CB  1 
ATOM   2323  C  CG1 . VAL C  1 34  ? 62.338  112.856 -26.528 1.00 23.58 ? 7   VAL D CG1 1 
ATOM   2324  C  CG2 . VAL C  1 34  ? 63.501  111.607 -24.633 1.00 24.02 ? 7   VAL D CG2 1 
ATOM   2325  N  N   . LEU C  1 35  ? 61.992  116.105 -25.152 1.00 21.31 ? 8   LEU D N   1 
ATOM   2326  C  CA  . LEU C  1 35  ? 61.089  117.192 -25.503 1.00 20.06 ? 8   LEU D CA  1 
ATOM   2327  C  C   . LEU C  1 35  ? 60.645  117.026 -26.953 1.00 14.70 ? 8   LEU D C   1 
ATOM   2328  O  O   . LEU C  1 35  ? 61.484  116.875 -27.839 1.00 17.71 ? 8   LEU D O   1 
ATOM   2329  C  CB  . LEU C  1 35  ? 61.787  118.541 -25.358 1.00 19.68 ? 8   LEU D CB  1 
ATOM   2330  C  CG  . LEU C  1 35  ? 62.315  118.903 -23.973 1.00 28.54 ? 8   LEU D CG  1 
ATOM   2331  C  CD1 . LEU C  1 35  ? 63.124  120.186 -24.051 1.00 33.21 ? 8   LEU D CD1 1 
ATOM   2332  C  CD2 . LEU C  1 35  ? 61.182  119.038 -23.024 1.00 26.41 ? 8   LEU D CD2 1 
ATOM   2333  N  N   . LYS C  1 36  ? 59.338  117.086 -27.183 1.00 18.01 ? 9   LYS D N   1 
ATOM   2334  C  CA  . LYS C  1 36  ? 58.761  116.986 -28.519 1.00 23.43 ? 9   LYS D CA  1 
ATOM   2335  C  C   . LYS C  1 36  ? 57.598  117.956 -28.577 1.00 22.65 ? 9   LYS D C   1 
ATOM   2336  O  O   . LYS C  1 36  ? 56.976  118.245 -27.560 1.00 21.40 ? 9   LYS D O   1 
ATOM   2337  C  CB  . LYS C  1 36  ? 58.232  115.570 -28.816 1.00 23.86 ? 9   LYS D CB  1 
ATOM   2338  C  CG  . LYS C  1 36  ? 59.283  114.480 -28.858 1.00 32.77 ? 9   LYS D CG  1 
ATOM   2339  C  CD  . LYS C  1 36  ? 58.604  113.109 -28.845 1.00 38.26 ? 9   LYS D CD  1 
ATOM   2340  C  CE  . LYS C  1 36  ? 59.621  111.965 -28.806 1.00 40.41 ? 9   LYS D CE  1 
ATOM   2341  N  NZ  . LYS C  1 36  ? 59.086  110.634 -29.231 1.00 48.51 ? 9   LYS D NZ  1 
ATOM   2342  N  N   . GLY C  1 37  ? 57.264  118.431 -29.768 1.00 20.99 ? 10  GLY D N   1 
ATOM   2343  C  CA  . GLY C  1 37  ? 56.084  119.271 -29.865 1.00 20.80 ? 10  GLY D CA  1 
ATOM   2344  C  C   . GLY C  1 37  ? 55.490  119.189 -31.259 1.00 27.70 ? 10  GLY D C   1 
ATOM   2345  O  O   . GLY C  1 37  ? 55.811  118.259 -31.996 1.00 23.51 ? 10  GLY D O   1 
ATOM   2346  N  N   . ASP C  1 38  ? 54.617  120.122 -31.626 1.00 28.02 ? 11  ASP D N   1 
ATOM   2347  C  CA  . ASP C  1 38  ? 54.027  120.067 -32.963 1.00 33.78 ? 11  ASP D CA  1 
ATOM   2348  C  C   . ASP C  1 38  ? 54.978  120.527 -34.059 1.00 33.87 ? 11  ASP D C   1 
ATOM   2349  O  O   . ASP C  1 38  ? 54.769  120.184 -35.231 1.00 40.85 ? 11  ASP D O   1 
ATOM   2350  C  CB  . ASP C  1 38  ? 52.771  120.922 -33.023 1.00 39.60 ? 11  ASP D CB  1 
ATOM   2351  C  CG  . ASP C  1 38  ? 51.707  120.433 -32.085 1.00 59.27 ? 11  ASP D CG  1 
ATOM   2352  O  OD1 . ASP C  1 38  ? 51.537  119.193 -31.994 1.00 68.89 ? 11  ASP D OD1 1 
ATOM   2353  O  OD2 . ASP C  1 38  ? 51.050  121.282 -31.437 1.00 69.27 ? 11  ASP D OD2 1 
ATOM   2354  N  N   . GLY C  1 39  ? 55.986  121.311 -33.719 1.00 27.42 ? 12  GLY D N   1 
ATOM   2355  C  CA  . GLY C  1 39  ? 56.881  121.867 -34.695 1.00 22.12 ? 12  GLY D CA  1 
ATOM   2356  C  C   . GLY C  1 39  ? 58.217  121.177 -34.633 1.00 20.07 ? 12  GLY D C   1 
ATOM   2357  O  O   . GLY C  1 39  ? 58.318  120.016 -34.229 1.00 21.32 ? 12  GLY D O   1 
ATOM   2358  N  N   . PRO C  1 40  ? 59.274  121.877 -35.051 1.00 19.73 ? 13  PRO D N   1 
ATOM   2359  C  CA  . PRO C  1 40  ? 60.604  121.270 -35.101 1.00 20.85 ? 13  PRO D CA  1 
ATOM   2360  C  C   . PRO C  1 40  ? 61.362  121.258 -33.783 1.00 19.29 ? 13  PRO D C   1 
ATOM   2361  O  O   . PRO C  1 40  ? 62.498  120.776 -33.775 1.00 21.70 ? 13  PRO D O   1 
ATOM   2362  C  CB  . PRO C  1 40  ? 61.329  122.167 -36.107 1.00 21.43 ? 13  PRO D CB  1 
ATOM   2363  C  CG  . PRO C  1 40  ? 60.716  123.507 -35.876 1.00 21.73 ? 13  PRO D CG  1 
ATOM   2364  C  CD  . PRO C  1 40  ? 59.292  123.286 -35.489 1.00 21.55 ? 13  PRO D CD  1 
ATOM   2365  N  N   . VAL C  1 41  ? 60.821  121.767 -32.683 1.00 21.32 ? 14  VAL D N   1 
ATOM   2366  C  CA  . VAL C  1 41  ? 61.618  121.838 -31.457 1.00 21.07 ? 14  VAL D CA  1 
ATOM   2367  C  C   . VAL C  1 41  ? 61.713  120.437 -30.870 1.00 17.57 ? 14  VAL D C   1 
ATOM   2368  O  O   . VAL C  1 41  ? 60.687  119.804 -30.601 1.00 22.14 ? 14  VAL D O   1 
ATOM   2369  C  CB  . VAL C  1 41  ? 61.027  122.834 -30.449 1.00 20.78 ? 14  VAL D CB  1 
ATOM   2370  C  CG1 . VAL C  1 41  ? 61.854  122.823 -29.147 1.00 20.50 ? 14  VAL D CG1 1 
ATOM   2371  C  CG2 . VAL C  1 41  ? 61.043  124.241 -31.055 1.00 23.32 ? 14  VAL D CG2 1 
ATOM   2372  N  N   . GLN C  1 42  ? 62.944  119.956 -30.690 1.00 24.30 ? 15  GLN D N   1 
ATOM   2373  C  CA  . GLN C  1 42  ? 63.251  118.636 -30.150 1.00 23.16 ? 15  GLN D CA  1 
ATOM   2374  C  C   . GLN C  1 42  ? 64.468  118.747 -29.245 1.00 27.14 ? 15  GLN D C   1 
ATOM   2375  O  O   . GLN C  1 42  ? 65.393  119.508 -29.539 1.00 22.12 ? 15  GLN D O   1 
ATOM   2376  C  CB  . GLN C  1 42  ? 63.601  117.629 -31.249 1.00 29.10 ? 15  GLN D CB  1 
ATOM   2377  C  CG  . GLN C  1 42  ? 62.676  117.574 -32.414 1.00 33.94 ? 15  GLN D CG  1 
ATOM   2378  C  CD  . GLN C  1 42  ? 63.026  116.411 -33.314 1.00 37.19 ? 15  GLN D CD  1 
ATOM   2379  O  OE1 . GLN C  1 42  ? 62.609  115.284 -33.073 1.00 44.47 ? 15  GLN D OE1 1 
ATOM   2380  N  NE2 . GLN C  1 42  ? 63.827  116.673 -34.329 1.00 38.42 ? 15  GLN D NE2 1 
ATOM   2381  N  N   . GLY C  1 43  ? 64.494  117.956 -28.166 1.00 23.17 ? 16  GLY D N   1 
ATOM   2382  C  CA  . GLY C  1 43  ? 65.671  117.967 -27.312 1.00 25.99 ? 16  GLY D CA  1 
ATOM   2383  C  C   . GLY C  1 43  ? 65.666  116.822 -26.319 1.00 30.20 ? 16  GLY D C   1 
ATOM   2384  O  O   . GLY C  1 43  ? 64.663  116.132 -26.137 1.00 21.81 ? 16  GLY D O   1 
ATOM   2385  N  N   . ILE C  1 44  ? 66.823  116.611 -25.701 1.00 25.11 ? 17  ILE D N   1 
ATOM   2386  C  CA  . ILE C  1 44  ? 66.978  115.682 -24.586 1.00 22.88 ? 17  ILE D CA  1 
ATOM   2387  C  C   . ILE C  1 44  ? 67.636  116.440 -23.444 1.00 26.27 ? 17  ILE D C   1 
ATOM   2388  O  O   . ILE C  1 44  ? 68.701  117.036 -23.627 1.00 23.16 ? 17  ILE D O   1 
ATOM   2389  C  CB  . ILE C  1 44  ? 67.824  114.453 -24.977 1.00 25.82 ? 17  ILE D CB  1 
ATOM   2390  C  CG1 . ILE C  1 44  ? 67.121  113.633 -26.067 1.00 23.51 ? 17  ILE D CG1 1 
ATOM   2391  C  CG2 . ILE C  1 44  ? 68.093  113.588 -23.753 1.00 27.39 ? 17  ILE D CG2 1 
ATOM   2392  C  CD1 . ILE C  1 44  ? 67.981  112.499 -26.606 1.00 30.53 ? 17  ILE D CD1 1 
ATOM   2393  N  N   . ILE C  1 45  ? 67.011  116.408 -22.274 1.00 22.77 ? 18  ILE D N   1 
ATOM   2394  C  CA  . ILE C  1 45  ? 67.512  117.089 -21.085 1.00 22.46 ? 18  ILE D CA  1 
ATOM   2395  C  C   . ILE C  1 45  ? 67.731  116.035 -20.006 1.00 26.93 ? 18  ILE D C   1 
ATOM   2396  O  O   . ILE C  1 45  ? 66.837  115.223 -19.737 1.00 20.71 ? 18  ILE D O   1 
ATOM   2397  C  CB  . ILE C  1 45  ? 66.540  118.178 -20.589 1.00 18.21 ? 18  ILE D CB  1 
ATOM   2398  C  CG1 . ILE C  1 45  ? 66.395  119.324 -21.612 1.00 22.25 ? 18  ILE D CG1 1 
ATOM   2399  C  CG2 . ILE C  1 45  ? 67.031  118.755 -19.251 1.00 20.99 ? 18  ILE D CG2 1 
ATOM   2400  C  CD1 . ILE C  1 45  ? 67.739  120.056 -21.890 1.00 22.21 ? 18  ILE D CD1 1 
ATOM   2401  N  N   . ASN C  1 46  ? 68.914  116.050 -19.402 1.00 22.59 ? 19  ASN D N   1 
ATOM   2402  C  CA  . ASN C  1 46  ? 69.313  115.126 -18.350 1.00 24.51 ? 19  ASN D CA  1 
ATOM   2403  C  C   . ASN C  1 46  ? 69.291  115.823 -16.999 1.00 29.65 ? 19  ASN D C   1 
ATOM   2404  O  O   . ASN C  1 46  ? 69.482  117.039 -16.909 1.00 22.77 ? 19  ASN D O   1 
ATOM   2405  C  CB  . ASN C  1 46  ? 70.715  114.581 -18.598 1.00 22.01 ? 19  ASN D CB  1 
ATOM   2406  C  CG  . ASN C  1 46  ? 70.865  113.934 -19.944 1.00 25.31 ? 19  ASN D CG  1 
ATOM   2407  O  OD1 . ASN C  1 46  ? 71.538  114.467 -20.839 1.00 33.67 ? 19  ASN D OD1 1 
ATOM   2408  N  ND2 . ASN C  1 46  ? 70.263  112.763 -20.098 1.00 26.40 ? 19  ASN D ND2 1 
ATOM   2409  N  N   . PHE C  1 47  ? 69.053  115.036 -15.942 1.00 27.06 ? 20  PHE D N   1 
ATOM   2410  C  CA  . PHE C  1 47  ? 69.071  115.511 -14.565 1.00 21.86 ? 20  PHE D CA  1 
ATOM   2411  C  C   . PHE C  1 47  ? 69.915  114.552 -13.735 1.00 30.89 ? 20  PHE D C   1 
ATOM   2412  O  O   . PHE C  1 47  ? 69.842  113.334 -13.924 1.00 24.57 ? 20  PHE D O   1 
ATOM   2413  C  CB  . PHE C  1 47  ? 67.684  115.584 -13.942 1.00 23.00 ? 20  PHE D CB  1 
ATOM   2414  C  CG  . PHE C  1 47  ? 66.697  116.401 -14.710 1.00 26.86 ? 20  PHE D CG  1 
ATOM   2415  C  CD1 . PHE C  1 47  ? 66.115  115.906 -15.872 1.00 25.11 ? 20  PHE D CD1 1 
ATOM   2416  C  CD2 . PHE C  1 47  ? 66.325  117.649 -14.255 1.00 23.38 ? 20  PHE D CD2 1 
ATOM   2417  C  CE1 . PHE C  1 47  ? 65.197  116.659 -16.570 1.00 21.28 ? 20  PHE D CE1 1 
ATOM   2418  C  CE2 . PHE C  1 47  ? 65.410  118.413 -14.944 1.00 32.66 ? 20  PHE D CE2 1 
ATOM   2419  C  CZ  . PHE C  1 47  ? 64.835  117.918 -16.104 1.00 25.77 ? 20  PHE D CZ  1 
ATOM   2420  N  N   . GLU C  1 48  ? 70.716  115.096 -12.817 1.00 28.30 ? 21  GLU D N   1 
ATOM   2421  C  CA  . GLU C  1 48  ? 71.532  114.261 -11.944 1.00 29.17 ? 21  GLU D CA  1 
ATOM   2422  C  C   . GLU C  1 48  ? 71.617  114.897 -10.564 1.00 31.10 ? 21  GLU D C   1 
ATOM   2423  O  O   . GLU C  1 48  ? 71.921  116.086 -10.439 1.00 29.62 ? 21  GLU D O   1 
ATOM   2424  C  CB  . GLU C  1 48  ? 72.932  114.049 -12.517 1.00 32.61 ? 21  GLU D CB  1 
ATOM   2425  C  CG  . GLU C  1 48  ? 73.728  112.991 -11.770 1.00 37.84 ? 21  GLU D CG  1 
ATOM   2426  C  CD  . GLU C  1 48  ? 75.151  112.868 -12.278 1.00 56.93 ? 21  GLU D CD  1 
ATOM   2427  O  OE1 . GLU C  1 48  ? 76.035  113.596 -11.765 1.00 55.39 ? 21  GLU D OE1 1 
ATOM   2428  O  OE2 . GLU C  1 48  ? 75.375  112.051 -13.205 1.00 59.62 ? 21  GLU D OE2 1 
ATOM   2429  N  N   . GLN C  1 49  ? 71.311  114.111 -9.529  1.00 31.91 ? 22  GLN D N   1 
ATOM   2430  C  CA  . GLN C  1 49  ? 71.321  114.604 -8.151  1.00 30.45 ? 22  GLN D CA  1 
ATOM   2431  C  C   . GLN C  1 49  ? 72.001  113.530 -7.306  1.00 35.94 ? 22  GLN D C   1 
ATOM   2432  O  O   . GLN C  1 49  ? 71.354  112.579 -6.868  1.00 31.90 ? 22  GLN D O   1 
ATOM   2433  C  CB  . GLN C  1 49  ? 69.923  114.903 -7.655  1.00 24.76 ? 22  GLN D CB  1 
ATOM   2434  C  CG  . GLN C  1 49  ? 69.905  115.586 -6.315  1.00 28.60 ? 22  GLN D CG  1 
ATOM   2435  C  CD  . GLN C  1 49  ? 68.507  115.764 -5.803  1.00 28.82 ? 22  GLN D CD  1 
ATOM   2436  O  OE1 . GLN C  1 49  ? 67.600  115.029 -6.194  1.00 31.08 ? 22  GLN D OE1 1 
ATOM   2437  N  NE2 . GLN C  1 49  ? 68.311  116.754 -4.943  1.00 28.30 ? 22  GLN D NE2 1 
ATOM   2438  N  N   . LYS C  1 50  ? 73.310  113.672 -7.099  1.00 36.41 ? 23  LYS D N   1 
ATOM   2439  C  CA  . LYS C  1 50  ? 74.030  112.603 -6.420  1.00 35.76 ? 23  LYS D CA  1 
ATOM   2440  C  C   . LYS C  1 50  ? 73.752  112.554 -4.924  1.00 32.44 ? 23  LYS D C   1 
ATOM   2441  O  O   . LYS C  1 50  ? 73.969  111.502 -4.314  1.00 47.72 ? 23  LYS D O   1 
ATOM   2442  C  CB  . LYS C  1 50  ? 75.528  112.709 -6.702  1.00 38.82 ? 23  LYS D CB  1 
ATOM   2443  C  CG  . LYS C  1 50  ? 75.909  111.996 -8.004  1.00 45.90 ? 23  LYS D CG  1 
ATOM   2444  C  CD  . LYS C  1 50  ? 76.982  112.717 -8.804  1.00 50.93 ? 23  LYS D CD  1 
ATOM   2445  C  CE  . LYS C  1 50  ? 77.756  111.729 -9.686  1.00 54.52 ? 23  LYS D CE  1 
ATOM   2446  N  NZ  . LYS C  1 50  ? 79.195  112.106 -9.872  1.00 55.64 ? 23  LYS D NZ  1 
ATOM   2447  N  N   . GLU C  1 51  ? 73.243  113.634 -4.329  1.00 36.73 ? 24  GLU D N   1 
ATOM   2448  C  CA  . GLU C  1 51  ? 72.841  113.645 -2.925  1.00 38.04 ? 24  GLU D CA  1 
ATOM   2449  C  C   . GLU C  1 51  ? 71.447  114.235 -2.798  1.00 37.53 ? 24  GLU D C   1 
ATOM   2450  O  O   . GLU C  1 51  ? 71.139  115.263 -3.407  1.00 35.05 ? 24  GLU D O   1 
ATOM   2451  C  CB  . GLU C  1 51  ? 73.818  114.457 -2.038  1.00 38.50 ? 24  GLU D CB  1 
ATOM   2452  C  CG  . GLU C  1 51  ? 75.296  114.205 -2.325  1.00 46.53 ? 24  GLU D CG  1 
ATOM   2453  C  CD  . GLU C  1 51  ? 75.878  113.041 -1.520  1.00 65.86 ? 24  GLU D CD  1 
ATOM   2454  O  OE1 . GLU C  1 51  ? 75.272  111.942 -1.503  1.00 66.37 ? 24  GLU D OE1 1 
ATOM   2455  O  OE2 . GLU C  1 51  ? 76.956  113.228 -0.911  1.00 64.81 ? 24  GLU D OE2 1 
ATOM   2456  N  N   . SER C  1 52  ? 70.626  113.607 -1.954  1.00 29.31 ? 25  SER D N   1 
ATOM   2457  C  CA  . SER C  1 52  ? 69.214  113.959 -1.865  1.00 23.15 ? 25  SER D CA  1 
ATOM   2458  C  C   . SER C  1 52  ? 68.970  115.324 -1.271  1.00 30.00 ? 25  SER D C   1 
ATOM   2459  O  O   . SER C  1 52  ? 67.897  115.896 -1.489  1.00 32.03 ? 25  SER D O   1 
ATOM   2460  C  CB  . SER C  1 52  ? 68.459  112.901 -1.065  1.00 31.95 ? 25  SER D CB  1 
ATOM   2461  O  OG  . SER C  1 52  ? 68.996  112.768 0.239   1.00 37.17 ? 25  SER D OG  1 
ATOM   2462  N  N   . ASN C  1 53  ? 69.915  115.863 -0.506  1.00 33.51 ? 26  ASN D N   1 
ATOM   2463  C  CA  . ASN C  1 53  ? 69.751  117.200 0.028   1.00 30.08 ? 26  ASN D CA  1 
ATOM   2464  C  C   . ASN C  1 53  ? 70.655  118.205 -0.675  1.00 40.88 ? 26  ASN D C   1 
ATOM   2465  O  O   . ASN C  1 53  ? 70.744  119.354 -0.230  1.00 50.29 ? 26  ASN D O   1 
ATOM   2466  C  CB  . ASN C  1 53  ? 69.976  117.204 1.553   1.00 38.17 ? 26  ASN D CB  1 
ATOM   2467  C  CG  . ASN C  1 53  ? 71.384  116.813 1.948   1.00 34.65 ? 26  ASN D CG  1 
ATOM   2468  O  OD1 . ASN C  1 53  ? 72.068  116.047 1.248   1.00 34.67 ? 26  ASN D OD1 1 
ATOM   2469  N  ND2 . ASN C  1 53  ? 71.834  117.336 3.096   1.00 37.42 ? 26  ASN D ND2 1 
ATOM   2470  N  N   . GLY C  1 54  ? 71.293  117.807 -1.782  1.00 38.04 ? 27  GLY D N   1 
ATOM   2471  C  CA  . GLY C  1 54  ? 72.116  118.691 -2.582  1.00 33.63 ? 27  GLY D CA  1 
ATOM   2472  C  C   . GLY C  1 54  ? 71.463  119.114 -3.893  1.00 42.93 ? 27  GLY D C   1 
ATOM   2473  O  O   . GLY C  1 54  ? 70.280  118.845 -4.138  1.00 34.41 ? 27  GLY D O   1 
ATOM   2474  N  N   . PRO C  1 55  ? 72.224  119.784 -4.760  1.00 40.75 ? 28  PRO D N   1 
ATOM   2475  C  CA  . PRO C  1 55  ? 71.647  120.366 -5.976  1.00 41.06 ? 28  PRO D CA  1 
ATOM   2476  C  C   . PRO C  1 55  ? 71.526  119.367 -7.125  1.00 36.13 ? 28  PRO D C   1 
ATOM   2477  O  O   . PRO C  1 55  ? 72.096  118.270 -7.104  1.00 28.78 ? 28  PRO D O   1 
ATOM   2478  C  CB  . PRO C  1 55  ? 72.647  121.481 -6.326  1.00 34.65 ? 28  PRO D CB  1 
ATOM   2479  C  CG  . PRO C  1 55  ? 73.966  120.938 -5.871  1.00 43.60 ? 28  PRO D CG  1 
ATOM   2480  C  CD  . PRO C  1 55  ? 73.678  120.024 -4.670  1.00 38.43 ? 28  PRO D CD  1 
ATOM   2481  N  N   . VAL C  1 56  ? 70.783  119.790 -8.155  1.00 36.02 ? 29  VAL D N   1 
ATOM   2482  C  CA  . VAL C  1 56  ? 70.526  118.996 -9.359  1.00 30.00 ? 29  VAL D CA  1 
ATOM   2483  C  C   . VAL C  1 56  ? 71.262  119.633 -10.525 1.00 24.22 ? 29  VAL D C   1 
ATOM   2484  O  O   . VAL C  1 56  ? 71.063  120.819 -10.808 1.00 30.34 ? 29  VAL D O   1 
ATOM   2485  C  CB  . VAL C  1 56  ? 69.025  118.920 -9.685  1.00 32.07 ? 29  VAL D CB  1 
ATOM   2486  C  CG1 . VAL C  1 56  ? 68.784  117.997 -10.903 1.00 23.90 ? 29  VAL D CG1 1 
ATOM   2487  C  CG2 . VAL C  1 56  ? 68.232  118.463 -8.486  1.00 27.00 ? 29  VAL D CG2 1 
ATOM   2488  N  N   . LYS C  1 57  ? 72.102  118.852 -11.201 1.00 26.58 ? 30  LYS D N   1 
ATOM   2489  C  CA  . LYS C  1 57  ? 72.639  119.262 -12.490 1.00 33.83 ? 30  LYS D CA  1 
ATOM   2490  C  C   . LYS C  1 57  ? 71.634  118.955 -13.596 1.00 37.08 ? 30  LYS D C   1 
ATOM   2491  O  O   . LYS C  1 57  ? 71.038  117.875 -13.631 1.00 28.38 ? 30  LYS D O   1 
ATOM   2492  C  CB  . LYS C  1 57  ? 73.966  118.561 -12.782 1.00 32.40 ? 30  LYS D CB  1 
ATOM   2493  C  CG  . LYS C  1 57  ? 75.063  118.887 -11.779 1.00 46.61 ? 30  LYS D CG  1 
ATOM   2494  C  CD  . LYS C  1 57  ? 76.343  118.084 -12.033 1.00 50.01 ? 30  LYS D CD  1 
ATOM   2495  C  CE  . LYS C  1 57  ? 77.255  118.104 -10.802 1.00 44.69 ? 30  LYS D CE  1 
ATOM   2496  N  NZ  . LYS C  1 57  ? 78.632  117.673 -11.133 1.00 49.29 ? 30  LYS D NZ  1 
ATOM   2497  N  N   . VAL C  1 58  ? 71.451  119.922 -14.495 1.00 34.18 ? 31  VAL D N   1 
ATOM   2498  C  CA  . VAL C  1 58  ? 70.524  119.843 -15.622 1.00 31.35 ? 31  VAL D CA  1 
ATOM   2499  C  C   . VAL C  1 58  ? 71.334  120.174 -16.865 1.00 33.05 ? 31  VAL D C   1 
ATOM   2500  O  O   . VAL C  1 58  ? 71.973  121.231 -16.917 1.00 29.28 ? 31  VAL D O   1 
ATOM   2501  C  CB  . VAL C  1 58  ? 69.351  120.826 -15.464 1.00 28.68 ? 31  VAL D CB  1 
ATOM   2502  C  CG1 . VAL C  1 58  ? 68.328  120.645 -16.571 1.00 28.29 ? 31  VAL D CG1 1 
ATOM   2503  C  CG2 . VAL C  1 58  ? 68.682  120.668 -14.101 1.00 21.87 ? 31  VAL D CG2 1 
ATOM   2504  N  N   . TRP C  1 59  ? 71.368  119.260 -17.836 1.00 27.70 ? 32  TRP D N   1 
ATOM   2505  C  CA  . TRP C  1 59  ? 72.148  119.538 -19.037 1.00 27.78 ? 32  TRP D CA  1 
ATOM   2506  C  C   . TRP C  1 59  ? 71.583  118.762 -20.214 1.00 28.12 ? 32  TRP D C   1 
ATOM   2507  O  O   . TRP C  1 59  ? 70.970  117.709 -20.053 1.00 22.75 ? 32  TRP D O   1 
ATOM   2508  C  CB  . TRP C  1 59  ? 73.629  119.195 -18.866 1.00 27.20 ? 32  TRP D CB  1 
ATOM   2509  C  CG  . TRP C  1 59  ? 73.922  117.741 -18.884 1.00 25.81 ? 32  TRP D CG  1 
ATOM   2510  C  CD1 . TRP C  1 59  ? 74.434  117.008 -19.920 1.00 29.55 ? 32  TRP D CD1 1 
ATOM   2511  C  CD2 . TRP C  1 59  ? 73.712  116.830 -17.808 1.00 24.64 ? 32  TRP D CD2 1 
ATOM   2512  N  NE1 . TRP C  1 59  ? 74.554  115.692 -19.549 1.00 30.19 ? 32  TRP D NE1 1 
ATOM   2513  C  CE2 . TRP C  1 59  ? 74.120  115.559 -18.251 1.00 32.71 ? 32  TRP D CE2 1 
ATOM   2514  C  CE3 . TRP C  1 59  ? 73.206  116.967 -16.512 1.00 28.29 ? 32  TRP D CE3 1 
ATOM   2515  C  CZ2 . TRP C  1 59  ? 74.043  114.426 -17.441 1.00 31.44 ? 32  TRP D CZ2 1 
ATOM   2516  C  CZ3 . TRP C  1 59  ? 73.134  115.837 -15.701 1.00 33.61 ? 32  TRP D CZ3 1 
ATOM   2517  C  CH2 . TRP C  1 59  ? 73.549  114.584 -16.172 1.00 33.54 ? 32  TRP D CH2 1 
ATOM   2518  N  N   . GLY C  1 60  ? 71.843  119.283 -21.403 1.00 23.46 ? 33  GLY D N   1 
ATOM   2519  C  CA  . GLY C  1 60  ? 71.417  118.636 -22.626 1.00 27.28 ? 33  GLY D CA  1 
ATOM   2520  C  C   . GLY C  1 60  ? 71.383  119.669 -23.736 1.00 30.77 ? 33  GLY D C   1 
ATOM   2521  O  O   . GLY C  1 60  ? 71.961  120.746 -23.621 1.00 24.44 ? 33  GLY D O   1 
ATOM   2522  N  N   . SER C  1 61  ? 70.695  119.312 -24.810 1.00 29.78 ? 34  SER D N   1 
ATOM   2523  C  CA  . SER C  1 61  ? 70.596  120.168 -25.984 1.00 28.04 ? 34  SER D CA  1 
ATOM   2524  C  C   . SER C  1 61  ? 69.160  120.177 -26.476 1.00 29.91 ? 34  SER D C   1 
ATOM   2525  O  O   . SER C  1 61  ? 68.457  119.165 -26.396 1.00 26.80 ? 34  SER D O   1 
ATOM   2526  C  CB  . SER C  1 61  ? 71.516  119.705 -27.133 1.00 36.70 ? 34  SER D CB  1 
ATOM   2527  O  OG  . SER C  1 61  ? 72.881  119.750 -26.756 1.00 51.24 ? 34  SER D OG  1 
ATOM   2528  N  N   . ILE C  1 62  ? 68.736  121.334 -26.979 1.00 22.96 ? 35  ILE D N   1 
ATOM   2529  C  CA  . ILE C  1 62  ? 67.428  121.508 -27.604 1.00 21.03 ? 35  ILE D CA  1 
ATOM   2530  C  C   . ILE C  1 62  ? 67.681  122.147 -28.956 1.00 28.48 ? 35  ILE D C   1 
ATOM   2531  O  O   . ILE C  1 62  ? 68.469  123.093 -29.055 1.00 27.29 ? 35  ILE D O   1 
ATOM   2532  C  CB  . ILE C  1 62  ? 66.474  122.392 -26.778 1.00 18.43 ? 35  ILE D CB  1 
ATOM   2533  C  CG1 . ILE C  1 62  ? 66.363  121.920 -25.316 1.00 23.84 ? 35  ILE D CG1 1 
ATOM   2534  C  CG2 . ILE C  1 62  ? 65.080  122.426 -27.397 1.00 22.30 ? 35  ILE D CG2 1 
ATOM   2535  C  CD1 . ILE C  1 62  ? 65.533  122.852 -24.489 1.00 24.43 ? 35  ILE D CD1 1 
ATOM   2536  N  N   . LYS C  1 63  ? 67.035  121.636 -29.997 1.00 27.85 ? 36  LYS D N   1 
ATOM   2537  C  CA  . LYS C  1 63  ? 67.266  122.167 -31.335 1.00 21.13 ? 36  LYS D CA  1 
ATOM   2538  C  C   . LYS C  1 63  ? 65.937  122.602 -31.939 1.00 26.64 ? 36  LYS D C   1 
ATOM   2539  O  O   . LYS C  1 63  ? 64.862  122.351 -31.384 1.00 21.08 ? 36  LYS D O   1 
ATOM   2540  C  CB  . LYS C  1 63  ? 67.992  121.138 -32.207 1.00 26.84 ? 36  LYS D CB  1 
ATOM   2541  C  CG  . LYS C  1 63  ? 67.148  119.912 -32.549 1.00 31.94 ? 36  LYS D CG  1 
ATOM   2542  C  CD  . LYS C  1 63  ? 68.027  118.751 -33.008 1.00 39.32 ? 36  LYS D CD  1 
ATOM   2543  C  CE  . LYS C  1 63  ? 67.372  117.934 -34.134 1.00 45.77 ? 36  LYS D CE  1 
ATOM   2544  N  NZ  . LYS C  1 63  ? 66.917  118.758 -35.314 1.00 46.78 ? 36  LYS D NZ  1 
ATOM   2545  N  N   . GLY C  1 64  ? 66.019  123.290 -33.082 1.00 26.66 ? 37  GLY D N   1 
ATOM   2546  C  CA  . GLY C  1 64  ? 64.835  123.802 -33.746 1.00 23.27 ? 37  GLY D CA  1 
ATOM   2547  C  C   . GLY C  1 64  ? 64.267  125.084 -33.189 1.00 26.93 ? 37  GLY D C   1 
ATOM   2548  O  O   . GLY C  1 64  ? 63.129  125.438 -33.523 1.00 23.29 ? 37  GLY D O   1 
ATOM   2549  N  N   . LEU C  1 65  ? 65.009  125.789 -32.341 1.00 21.46 ? 38  LEU D N   1 
ATOM   2550  C  CA  . LEU C  1 65  ? 64.515  127.000 -31.701 1.00 21.71 ? 38  LEU D CA  1 
ATOM   2551  C  C   . LEU C  1 65  ? 64.891  128.236 -32.515 1.00 20.23 ? 38  LEU D C   1 
ATOM   2552  O  O   . LEU C  1 65  ? 65.906  128.251 -33.205 1.00 26.53 ? 38  LEU D O   1 
ATOM   2553  C  CB  . LEU C  1 65  ? 65.117  127.143 -30.298 1.00 25.31 ? 38  LEU D CB  1 
ATOM   2554  C  CG  . LEU C  1 65  ? 64.746  126.060 -29.275 1.00 22.74 ? 38  LEU D CG  1 
ATOM   2555  C  CD1 . LEU C  1 65  ? 65.782  126.031 -28.153 1.00 25.29 ? 38  LEU D CD1 1 
ATOM   2556  C  CD2 . LEU C  1 65  ? 63.356  126.308 -28.714 1.00 20.77 ? 38  LEU D CD2 1 
ATOM   2557  N  N   . THR C  1 66  ? 64.094  129.292 -32.379 1.00 24.30 ? 39  THR D N   1 
ATOM   2558  C  CA  . THR C  1 66  ? 64.525  130.587 -32.894 1.00 32.10 ? 39  THR D CA  1 
ATOM   2559  C  C   . THR C  1 66  ? 65.706  131.104 -32.081 1.00 31.90 ? 39  THR D C   1 
ATOM   2560  O  O   . THR C  1 66  ? 65.803  130.869 -30.874 1.00 29.23 ? 39  THR D O   1 
ATOM   2561  C  CB  . THR C  1 66  ? 63.399  131.615 -32.838 1.00 31.95 ? 39  THR D CB  1 
ATOM   2562  O  OG1 . THR C  1 66  ? 62.826  131.634 -31.529 1.00 34.01 ? 39  THR D OG1 1 
ATOM   2563  C  CG2 . THR C  1 66  ? 62.310  131.281 -33.849 1.00 31.98 ? 39  THR D CG2 1 
ATOM   2564  N  N   . GLU C  1 67  ? 66.619  131.800 -32.760 1.00 29.65 ? 40  GLU D N   1 
ATOM   2565  C  CA  . GLU C  1 67  ? 67.776  132.374 -32.084 1.00 33.39 ? 40  GLU D CA  1 
ATOM   2566  C  C   . GLU C  1 67  ? 67.320  133.271 -30.947 1.00 29.73 ? 40  GLU D C   1 
ATOM   2567  O  O   . GLU C  1 67  ? 66.382  134.055 -31.101 1.00 34.51 ? 40  GLU D O   1 
ATOM   2568  C  CB  . GLU C  1 67  ? 68.625  133.173 -33.079 1.00 34.52 ? 40  GLU D CB  1 
ATOM   2569  C  CG  . GLU C  1 67  ? 69.653  134.070 -32.419 1.00 40.05 ? 40  GLU D CG  1 
ATOM   2570  C  CD  . GLU C  1 67  ? 70.724  134.543 -33.388 1.00 50.40 ? 40  GLU D CD  1 
ATOM   2571  O  OE1 . GLU C  1 67  ? 70.468  134.550 -34.611 1.00 54.02 ? 40  GLU D OE1 1 
ATOM   2572  O  OE2 . GLU C  1 67  ? 71.814  134.931 -32.927 1.00 61.92 ? 40  GLU D OE2 1 
ATOM   2573  N  N   . GLY C  1 68  ? 67.952  133.122 -29.780 1.00 32.62 ? 41  GLY D N   1 
ATOM   2574  C  CA  . GLY C  1 68  ? 67.557  133.947 -28.658 1.00 30.36 ? 41  GLY D CA  1 
ATOM   2575  C  C   . GLY C  1 68  ? 67.112  133.179 -27.431 1.00 28.73 ? 41  GLY D C   1 
ATOM   2576  O  O   . GLY C  1 68  ? 67.356  131.973 -27.325 1.00 28.42 ? 41  GLY D O   1 
ATOM   2577  N  N   . LEU C  1 69  ? 66.412  133.866 -26.531 1.00 30.42 ? 42  LEU D N   1 
ATOM   2578  C  CA  . LEU C  1 69  ? 66.057  133.354 -25.214 1.00 33.52 ? 42  LEU D CA  1 
ATOM   2579  C  C   . LEU C  1 69  ? 64.712  132.646 -25.223 1.00 34.90 ? 42  LEU D C   1 
ATOM   2580  O  O   . LEU C  1 69  ? 63.753  133.115 -25.843 1.00 30.31 ? 42  LEU D O   1 
ATOM   2581  C  CB  . LEU C  1 69  ? 66.001  134.505 -24.214 1.00 30.50 ? 42  LEU D CB  1 
ATOM   2582  C  CG  . LEU C  1 69  ? 67.257  134.799 -23.414 1.00 35.73 ? 42  LEU D CG  1 
ATOM   2583  C  CD1 . LEU C  1 69  ? 68.462  134.930 -24.314 1.00 33.53 ? 42  LEU D CD1 1 
ATOM   2584  C  CD2 . LEU C  1 69  ? 67.012  136.081 -22.643 1.00 35.07 ? 42  LEU D CD2 1 
ATOM   2585  N  N   . HIS C  1 70  ? 64.629  131.538 -24.486 1.00 25.53 ? 43  HIS D N   1 
ATOM   2586  C  CA  . HIS C  1 70  ? 63.385  130.793 -24.368 1.00 22.77 ? 43  HIS D CA  1 
ATOM   2587  C  C   . HIS C  1 70  ? 63.183  130.386 -22.923 1.00 24.47 ? 43  HIS D C   1 
ATOM   2588  O  O   . HIS C  1 70  ? 64.089  129.806 -22.328 1.00 24.57 ? 43  HIS D O   1 
ATOM   2589  C  CB  . HIS C  1 70  ? 63.422  129.552 -25.259 1.00 27.40 ? 43  HIS D CB  1 
ATOM   2590  C  CG  . HIS C  1 70  ? 63.485  129.887 -26.716 1.00 22.85 ? 43  HIS D CG  1 
ATOM   2591  N  ND1 . HIS C  1 70  ? 62.363  130.200 -27.444 1.00 26.20 ? 43  HIS D ND1 1 
ATOM   2592  C  CD2 . HIS C  1 70  ? 64.536  130.015 -27.561 1.00 26.98 ? 43  HIS D CD2 1 
ATOM   2593  C  CE1 . HIS C  1 70  ? 62.714  130.473 -28.692 1.00 25.10 ? 43  HIS D CE1 1 
ATOM   2594  N  NE2 . HIS C  1 70  ? 64.028  130.373 -28.789 1.00 27.52 ? 43  HIS D NE2 1 
ATOM   2595  N  N   . GLY C  1 71  ? 61.986  130.646 -22.399 1.00 23.61 ? 44  GLY D N   1 
ATOM   2596  C  CA  . GLY C  1 71  ? 61.662  130.224 -21.048 1.00 29.49 ? 44  GLY D CA  1 
ATOM   2597  C  C   . GLY C  1 71  ? 61.652  128.713 -20.911 1.00 35.11 ? 44  GLY D C   1 
ATOM   2598  O  O   . GLY C  1 71  ? 61.280  127.977 -21.831 1.00 23.40 ? 44  GLY D O   1 
ATOM   2599  N  N   . PHE C  1 72  ? 62.056  128.251 -19.726 1.00 25.58 ? 45  PHE D N   1 
ATOM   2600  C  CA  . PHE C  1 72  ? 62.416  126.851 -19.505 1.00 21.91 ? 45  PHE D CA  1 
ATOM   2601  C  C   . PHE C  1 72  ? 61.919  126.491 -18.110 1.00 29.61 ? 45  PHE D C   1 
ATOM   2602  O  O   . PHE C  1 72  ? 62.490  126.954 -17.119 1.00 28.99 ? 45  PHE D O   1 
ATOM   2603  C  CB  . PHE C  1 72  ? 63.922  126.696 -19.638 1.00 25.35 ? 45  PHE D CB  1 
ATOM   2604  C  CG  . PHE C  1 72  ? 64.415  125.289 -19.674 1.00 27.19 ? 45  PHE D CG  1 
ATOM   2605  C  CD1 . PHE C  1 72  ? 64.022  124.408 -20.675 1.00 25.74 ? 45  PHE D CD1 1 
ATOM   2606  C  CD2 . PHE C  1 72  ? 65.342  124.860 -18.730 1.00 27.27 ? 45  PHE D CD2 1 
ATOM   2607  C  CE1 . PHE C  1 72  ? 64.530  123.119 -20.719 1.00 26.94 ? 45  PHE D CE1 1 
ATOM   2608  C  CE2 . PHE C  1 72  ? 65.844  123.573 -18.769 1.00 34.81 ? 45  PHE D CE2 1 
ATOM   2609  C  CZ  . PHE C  1 72  ? 65.442  122.704 -19.767 1.00 30.58 ? 45  PHE D CZ  1 
ATOM   2610  N  N   . HIS C  1 73  ? 60.833  125.721 -18.039 1.00 24.48 ? 46  HIS D N   1 
ATOM   2611  C  CA  . HIS C  1 73  ? 60.106  125.538 -16.786 1.00 26.28 ? 46  HIS D CA  1 
ATOM   2612  C  C   . HIS C  1 73  ? 59.662  124.095 -16.624 1.00 30.55 ? 46  HIS D C   1 
ATOM   2613  O  O   . HIS C  1 73  ? 59.319  123.417 -17.598 1.00 23.16 ? 46  HIS D O   1 
ATOM   2614  C  CB  . HIS C  1 73  ? 58.851  126.413 -16.715 1.00 28.07 ? 46  HIS D CB  1 
ATOM   2615  C  CG  . HIS C  1 73  ? 59.084  127.845 -17.080 1.00 34.92 ? 46  HIS D CG  1 
ATOM   2616  N  ND1 . HIS C  1 73  ? 58.180  128.578 -17.820 1.00 44.26 ? 46  HIS D ND1 1 
ATOM   2617  C  CD2 . HIS C  1 73  ? 60.097  128.692 -16.779 1.00 42.14 ? 46  HIS D CD2 1 
ATOM   2618  C  CE1 . HIS C  1 73  ? 58.639  129.808 -17.980 1.00 44.47 ? 46  HIS D CE1 1 
ATOM   2619  N  NE2 . HIS C  1 73  ? 59.803  129.903 -17.362 1.00 39.29 ? 46  HIS D NE2 1 
ATOM   2620  N  N   . VAL C  1 74  ? 59.638  123.648 -15.375 1.00 23.09 ? 47  VAL D N   1 
ATOM   2621  C  CA  . VAL C  1 74  ? 58.908  122.449 -14.989 1.00 23.49 ? 47  VAL D CA  1 
ATOM   2622  C  C   . VAL C  1 74  ? 57.476  122.853 -14.703 1.00 22.83 ? 47  VAL D C   1 
ATOM   2623  O  O   . VAL C  1 74  ? 57.225  123.740 -13.877 1.00 26.54 ? 47  VAL D O   1 
ATOM   2624  C  CB  . VAL C  1 74  ? 59.544  121.792 -13.750 1.00 22.23 ? 47  VAL D CB  1 
ATOM   2625  C  CG1 . VAL C  1 74  ? 58.816  120.488 -13.409 1.00 20.30 ? 47  VAL D CG1 1 
ATOM   2626  C  CG2 . VAL C  1 74  ? 61.017  121.568 -13.985 1.00 22.10 ? 47  VAL D CG2 1 
ATOM   2627  N  N   . HIS C  1 75  ? 56.531  122.211 -15.379 1.00 19.87 ? 48  HIS D N   1 
ATOM   2628  C  CA  . HIS C  1 75  ? 55.106  122.404 -15.165 1.00 17.15 ? 48  HIS D CA  1 
ATOM   2629  C  C   . HIS C  1 75  ? 54.564  121.267 -14.310 1.00 22.28 ? 48  HIS D C   1 
ATOM   2630  O  O   . HIS C  1 75  ? 55.200  120.220 -14.167 1.00 23.81 ? 48  HIS D O   1 
ATOM   2631  C  CB  . HIS C  1 75  ? 54.350  122.492 -16.506 1.00 21.80 ? 48  HIS D CB  1 
ATOM   2632  C  CG  . HIS C  1 75  ? 54.640  123.753 -17.268 1.00 20.61 ? 48  HIS D CG  1 
ATOM   2633  N  ND1 . HIS C  1 75  ? 53.660  124.648 -17.636 1.00 25.17 ? 48  HIS D ND1 1 
ATOM   2634  C  CD2 . HIS C  1 75  ? 55.812  124.287 -17.682 1.00 22.29 ? 48  HIS D CD2 1 
ATOM   2635  C  CE1 . HIS C  1 75  ? 54.215  125.669 -18.270 1.00 21.80 ? 48  HIS D CE1 1 
ATOM   2636  N  NE2 . HIS C  1 75  ? 55.520  125.471 -18.317 1.00 26.02 ? 48  HIS D NE2 1 
ATOM   2637  N  N   . GLU C  1 76  ? 53.352  121.479 -13.774 1.00 24.51 ? 49  GLU D N   1 
ATOM   2638  C  CA  . GLU C  1 76  ? 52.867  120.680 -12.642 1.00 29.49 ? 49  GLU D CA  1 
ATOM   2639  C  C   . GLU C  1 76  ? 52.536  119.233 -13.013 1.00 28.84 ? 49  GLU D C   1 
ATOM   2640  O  O   . GLU C  1 76  ? 52.826  118.319 -12.233 1.00 23.38 ? 49  GLU D O   1 
ATOM   2641  C  CB  . GLU C  1 76  ? 51.640  121.330 -12.014 1.00 28.73 ? 49  GLU D CB  1 
ATOM   2642  C  CG  . GLU C  1 76  ? 51.235  120.659 -10.706 1.00 28.72 ? 49  GLU D CG  1 
ATOM   2643  C  CD  . GLU C  1 76  ? 49.975  121.252 -10.079 1.00 42.26 ? 49  GLU D CD  1 
ATOM   2644  O  OE1 . GLU C  1 76  ? 49.498  122.316 -10.547 1.00 41.14 ? 49  GLU D OE1 1 
ATOM   2645  O  OE2 . GLU C  1 76  ? 49.479  120.655 -9.093  1.00 40.90 ? 49  GLU D OE2 1 
ATOM   2646  N  N   . PHE C  1 77  ? 51.889  118.993 -14.156 1.00 24.99 ? 50  PHE D N   1 
ATOM   2647  C  CA  . PHE C  1 77  ? 51.423  117.653 -14.490 1.00 25.49 ? 50  PHE D CA  1 
ATOM   2648  C  C   . PHE C  1 77  ? 52.230  117.043 -15.630 1.00 26.28 ? 50  PHE D C   1 
ATOM   2649  O  O   . PHE C  1 77  ? 52.581  117.730 -16.596 1.00 30.04 ? 50  PHE D O   1 
ATOM   2650  C  CB  . PHE C  1 77  ? 49.949  117.673 -14.875 1.00 24.29 ? 50  PHE D CB  1 
ATOM   2651  C  CG  . PHE C  1 77  ? 49.095  118.385 -13.889 1.00 31.30 ? 50  PHE D CG  1 
ATOM   2652  C  CD1 . PHE C  1 77  ? 48.955  117.890 -12.612 1.00 29.08 ? 50  PHE D CD1 1 
ATOM   2653  C  CD2 . PHE C  1 77  ? 48.435  119.554 -14.241 1.00 33.41 ? 50  PHE D CD2 1 
ATOM   2654  C  CE1 . PHE C  1 77  ? 48.180  118.558 -11.677 1.00 42.24 ? 50  PHE D CE1 1 
ATOM   2655  C  CE2 . PHE C  1 77  ? 47.654  120.218 -13.324 1.00 38.40 ? 50  PHE D CE2 1 
ATOM   2656  C  CZ  . PHE C  1 77  ? 47.534  119.721 -12.041 1.00 30.58 ? 50  PHE D CZ  1 
ATOM   2657  N  N   . GLY C  1 78  ? 52.500  115.743 -15.513 1.00 24.45 ? 51  GLY D N   1 
ATOM   2658  C  CA  . GLY C  1 78  ? 53.122  114.967 -16.572 1.00 21.18 ? 51  GLY D CA  1 
ATOM   2659  C  C   . GLY C  1 78  ? 52.047  114.389 -17.470 1.00 22.95 ? 51  GLY D C   1 
ATOM   2660  O  O   . GLY C  1 78  ? 52.016  113.191 -17.769 1.00 23.68 ? 51  GLY D O   1 
ATOM   2661  N  N   . ASP C  1 79  ? 51.135  115.259 -17.881 1.00 26.05 ? 52  ASP D N   1 
ATOM   2662  C  CA  . ASP C  1 79  ? 49.954  114.908 -18.651 1.00 24.11 ? 52  ASP D CA  1 
ATOM   2663  C  C   . ASP C  1 79  ? 50.143  115.520 -20.035 1.00 29.69 ? 52  ASP D C   1 
ATOM   2664  O  O   . ASP C  1 79  ? 50.062  116.744 -20.190 1.00 24.12 ? 52  ASP D O   1 
ATOM   2665  C  CB  . ASP C  1 79  ? 48.700  115.446 -17.962 1.00 24.46 ? 52  ASP D CB  1 
ATOM   2666  C  CG  . ASP C  1 79  ? 47.410  115.083 -18.690 1.00 27.12 ? 52  ASP D CG  1 
ATOM   2667  O  OD1 . ASP C  1 79  ? 47.460  114.799 -19.904 1.00 25.47 ? 52  ASP D OD1 1 
ATOM   2668  O  OD2 . ASP C  1 79  ? 46.333  115.087 -18.058 1.00 29.91 ? 52  ASP D OD2 1 
ATOM   2669  N  N   A ASN C  1 80  ? 50.391  114.662 -21.030 0.50 25.53 ? 53  ASN D N   1 
ATOM   2670  N  N   B ASN C  1 80  ? 50.420  114.692 -21.036 0.50 25.53 ? 53  ASN D N   1 
ATOM   2671  C  CA  A ASN C  1 80  ? 50.584  115.065 -22.421 0.50 24.78 ? 53  ASN D CA  1 
ATOM   2672  C  CA  B ASN C  1 80  ? 50.535  115.200 -22.397 0.50 24.74 ? 53  ASN D CA  1 
ATOM   2673  C  C   A ASN C  1 80  ? 49.385  114.710 -23.301 0.50 25.65 ? 53  ASN D C   1 
ATOM   2674  C  C   B ASN C  1 80  ? 49.398  114.698 -23.288 0.50 25.63 ? 53  ASN D C   1 
ATOM   2675  O  O   A ASN C  1 80  ? 49.512  114.649 -24.529 0.50 27.23 ? 53  ASN D O   1 
ATOM   2676  O  O   B ASN C  1 80  ? 49.569  114.539 -24.500 0.50 27.39 ? 53  ASN D O   1 
ATOM   2677  C  CB  A ASN C  1 80  ? 51.858  114.423 -22.976 0.50 26.89 ? 53  ASN D CB  1 
ATOM   2678  C  CB  B ASN C  1 80  ? 51.905  114.861 -22.987 0.50 26.79 ? 53  ASN D CB  1 
ATOM   2679  C  CG  A ASN C  1 80  ? 52.334  115.072 -24.270 0.50 30.55 ? 53  ASN D CG  1 
ATOM   2680  C  CG  B ASN C  1 80  ? 53.073  115.472 -22.193 0.50 30.56 ? 53  ASN D CG  1 
ATOM   2681  O  OD1 A ASN C  1 80  ? 52.423  116.293 -24.370 0.50 31.39 ? 53  ASN D OD1 1 
ATOM   2682  O  OD1 B ASN C  1 80  ? 52.892  116.364 -21.344 0.50 35.30 ? 53  ASN D OD1 1 
ATOM   2683  N  ND2 A ASN C  1 80  ? 52.609  114.249 -25.276 0.50 28.63 ? 53  ASN D ND2 1 
ATOM   2684  N  ND2 B ASN C  1 80  ? 54.286  115.018 -22.501 0.50 30.33 ? 53  ASN D ND2 1 
ATOM   2685  N  N   . THR C  1 81  ? 48.216  114.475 -22.705 1.00 22.53 ? 54  THR D N   1 
ATOM   2686  C  CA  . THR C  1 81  ? 47.084  113.996 -23.503 1.00 24.56 ? 54  THR D CA  1 
ATOM   2687  C  C   . THR C  1 81  ? 46.576  115.047 -24.479 1.00 29.52 ? 54  THR D C   1 
ATOM   2688  O  O   . THR C  1 81  ? 46.024  114.696 -25.524 1.00 30.85 ? 54  THR D O   1 
ATOM   2689  C  CB  . THR C  1 81  ? 45.939  113.549 -22.602 1.00 29.66 ? 54  THR D CB  1 
ATOM   2690  O  OG1 . THR C  1 81  ? 45.501  114.653 -21.800 1.00 27.66 ? 54  THR D OG1 1 
ATOM   2691  C  CG2 . THR C  1 81  ? 46.376  112.394 -21.718 1.00 24.71 ? 54  THR D CG2 1 
ATOM   2692  N  N   . ALA C  1 82  ? 46.745  116.327 -24.164 1.00 27.56 ? 55  ALA D N   1 
ATOM   2693  C  CA  . ALA C  1 82  ? 46.434  117.418 -25.085 1.00 35.11 ? 55  ALA D CA  1 
ATOM   2694  C  C   . ALA C  1 82  ? 47.707  118.164 -25.459 1.00 31.59 ? 55  ALA D C   1 
ATOM   2695  O  O   . ALA C  1 82  ? 47.748  119.393 -25.472 1.00 38.76 ? 55  ALA D O   1 
ATOM   2696  C  CB  . ALA C  1 82  ? 45.407  118.372 -24.480 1.00 32.87 ? 55  ALA D CB  1 
ATOM   2697  N  N   . GLY C  1 83  ? 48.772  117.417 -25.737 1.00 26.50 ? 56  GLY D N   1 
ATOM   2698  C  CA  . GLY C  1 83  ? 50.069  118.029 -25.960 1.00 29.56 ? 56  GLY D CA  1 
ATOM   2699  C  C   . GLY C  1 83  ? 50.536  118.779 -24.724 1.00 30.87 ? 56  GLY D C   1 
ATOM   2700  O  O   . GLY C  1 83  ? 50.157  118.467 -23.590 1.00 27.37 ? 56  GLY D O   1 
ATOM   2701  N  N   . CYS C  1 84  ? 51.347  119.815 -24.954 1.00 25.65 ? 57  CYS D N   1 
ATOM   2702  C  CA  . CYS C  1 84  ? 51.951  120.562 -23.854 1.00 27.07 ? 57  CYS D CA  1 
ATOM   2703  C  C   . CYS C  1 84  ? 50.928  121.346 -23.041 1.00 34.12 ? 57  CYS D C   1 
ATOM   2704  O  O   . CYS C  1 84  ? 51.214  121.726 -21.896 1.00 24.95 ? 57  CYS D O   1 
ATOM   2705  C  CB  . CYS C  1 84  ? 53.031  121.486 -24.414 1.00 31.40 ? 57  CYS D CB  1 
ATOM   2706  S  SG  . CYS C  1 84  ? 54.331  120.561 -25.286 1.00 33.72 ? 57  CYS D SG  1 
ATOM   2707  N  N   . THR C  1 85  ? 49.731  121.550 -23.586 1.00 27.89 ? 58  THR D N   1 
ATOM   2708  C  CA  . THR C  1 85  ? 48.707  122.331 -22.899 1.00 30.85 ? 58  THR D CA  1 
ATOM   2709  C  C   . THR C  1 85  ? 48.253  121.656 -21.614 1.00 34.36 ? 58  THR D C   1 
ATOM   2710  O  O   . THR C  1 85  ? 48.056  122.320 -20.586 1.00 29.99 ? 58  THR D O   1 
ATOM   2711  C  CB  . THR C  1 85  ? 47.521  122.536 -23.843 1.00 31.68 ? 58  THR D CB  1 
ATOM   2712  O  OG1 . THR C  1 85  ? 47.910  123.457 -24.862 1.00 48.17 ? 58  THR D OG1 1 
ATOM   2713  C  CG2 . THR C  1 85  ? 46.323  123.089 -23.101 1.00 40.72 ? 58  THR D CG2 1 
ATOM   2714  N  N   . SER C  1 86  ? 48.082  120.339 -21.646 1.00 29.22 ? 59  SER D N   1 
ATOM   2715  C  CA  . SER C  1 86  ? 47.624  119.659 -20.447 1.00 31.15 ? 59  SER D CA  1 
ATOM   2716  C  C   . SER C  1 86  ? 48.702  119.556 -19.356 1.00 25.65 ? 59  SER D C   1 
ATOM   2717  O  O   . SER C  1 86  ? 48.416  119.001 -18.298 1.00 24.09 ? 59  SER D O   1 
ATOM   2718  C  CB  . SER C  1 86  ? 47.065  118.277 -20.826 1.00 29.74 ? 59  SER D CB  1 
ATOM   2719  O  OG  . SER C  1 86  ? 47.763  117.699 -21.921 1.00 30.03 ? 59  SER D OG  1 
ATOM   2720  N  N   . ALA C  1 87  ? 49.907  120.100 -19.547 1.00 26.25 ? 60  ALA D N   1 
ATOM   2721  C  CA  . ALA C  1 87  ? 50.875  120.070 -18.452 1.00 21.96 ? 60  ALA D CA  1 
ATOM   2722  C  C   . ALA C  1 87  ? 50.519  121.022 -17.315 1.00 30.45 ? 60  ALA D C   1 
ATOM   2723  O  O   . ALA C  1 87  ? 51.178  120.976 -16.270 1.00 25.64 ? 60  ALA D O   1 
ATOM   2724  C  CB  . ALA C  1 87  ? 52.278  120.404 -18.952 1.00 23.04 ? 60  ALA D CB  1 
ATOM   2725  N  N   . GLY C  1 88  ? 49.513  121.879 -17.488 1.00 32.46 ? 61  GLY D N   1 
ATOM   2726  C  CA  . GLY C  1 88  ? 49.109  122.793 -16.437 1.00 29.42 ? 61  GLY D CA  1 
ATOM   2727  C  C   . GLY C  1 88  ? 50.087  123.936 -16.243 1.00 25.54 ? 61  GLY D C   1 
ATOM   2728  O  O   . GLY C  1 88  ? 50.921  124.235 -17.110 1.00 25.01 ? 61  GLY D O   1 
ATOM   2729  N  N   . PRO C  1 89  ? 50.002  124.601 -15.087 1.00 31.40 ? 62  PRO D N   1 
ATOM   2730  C  CA  . PRO C  1 89  ? 50.838  125.776 -14.818 1.00 28.50 ? 62  PRO D CA  1 
ATOM   2731  C  C   . PRO C  1 89  ? 52.218  125.355 -14.333 1.00 32.40 ? 62  PRO D C   1 
ATOM   2732  O  O   . PRO C  1 89  ? 52.514  124.171 -14.178 1.00 27.97 ? 62  PRO D O   1 
ATOM   2733  C  CB  . PRO C  1 89  ? 50.055  126.512 -13.723 1.00 33.01 ? 62  PRO D CB  1 
ATOM   2734  C  CG  . PRO C  1 89  ? 49.400  125.418 -12.949 1.00 31.30 ? 62  PRO D CG  1 
ATOM   2735  C  CD  . PRO C  1 89  ? 49.078  124.314 -13.973 1.00 34.38 ? 62  PRO D CD  1 
ATOM   2736  N  N   . HIS C  1 90  ? 53.068  126.352 -14.089 1.00 29.23 ? 63  HIS D N   1 
ATOM   2737  C  CA  . HIS C  1 90  ? 54.381  126.070 -13.523 1.00 27.09 ? 63  HIS D CA  1 
ATOM   2738  C  C   . HIS C  1 90  ? 54.226  125.315 -12.208 1.00 26.92 ? 63  HIS D C   1 
ATOM   2739  O  O   . HIS C  1 90  ? 53.253  125.509 -11.475 1.00 33.60 ? 63  HIS D O   1 
ATOM   2740  C  CB  . HIS C  1 90  ? 55.169  127.357 -13.284 1.00 35.69 ? 63  HIS D CB  1 
ATOM   2741  C  CG  . HIS C  1 90  ? 55.454  128.131 -14.528 1.00 42.49 ? 63  HIS D CG  1 
ATOM   2742  N  ND1 . HIS C  1 90  ? 56.142  129.325 -14.515 1.00 48.53 ? 63  HIS D ND1 1 
ATOM   2743  C  CD2 . HIS C  1 90  ? 55.148  127.882 -15.825 1.00 37.71 ? 63  HIS D CD2 1 
ATOM   2744  C  CE1 . HIS C  1 90  ? 56.242  129.782 -15.751 1.00 45.27 ? 63  HIS D CE1 1 
ATOM   2745  N  NE2 . HIS C  1 90  ? 55.646  128.927 -16.564 1.00 35.11 ? 63  HIS D NE2 1 
ATOM   2746  N  N   . PHE C  1 91  ? 55.164  124.410 -11.952 1.00 28.26 ? 64  PHE D N   1 
ATOM   2747  C  CA  . PHE C  1 91  ? 55.159  123.619 -10.731 1.00 29.52 ? 64  PHE D CA  1 
ATOM   2748  C  C   . PHE C  1 91  ? 55.438  124.549 -9.545  1.00 28.75 ? 64  PHE D C   1 
ATOM   2749  O  O   . PHE C  1 91  ? 56.511  125.162 -9.474  1.00 25.29 ? 64  PHE D O   1 
ATOM   2750  C  CB  . PHE C  1 91  ? 56.202  122.504 -10.830 1.00 25.42 ? 64  PHE D CB  1 
ATOM   2751  C  CG  . PHE C  1 91  ? 56.319  121.644 -9.585  1.00 23.48 ? 64  PHE D CG  1 
ATOM   2752  C  CD1 . PHE C  1 91  ? 55.192  121.180 -8.934  1.00 28.37 ? 64  PHE D CD1 1 
ATOM   2753  C  CD2 . PHE C  1 91  ? 57.564  121.302 -9.087  1.00 27.60 ? 64  PHE D CD2 1 
ATOM   2754  C  CE1 . PHE C  1 91  ? 55.306  120.394 -7.777  1.00 28.43 ? 64  PHE D CE1 1 
ATOM   2755  C  CE2 . PHE C  1 91  ? 57.683  120.508 -7.952  1.00 31.70 ? 64  PHE D CE2 1 
ATOM   2756  C  CZ  . PHE C  1 91  ? 56.547  120.061 -7.302  1.00 26.53 ? 64  PHE D CZ  1 
ATOM   2757  N  N   . ASN C  1 92  ? 54.462  124.636 -8.630  1.00 35.18 ? 65  ASN D N   1 
ATOM   2758  C  CA  . ASN C  1 92  ? 54.434  125.659 -7.574  1.00 42.05 ? 65  ASN D CA  1 
ATOM   2759  C  C   . ASN C  1 92  ? 53.817  125.076 -6.304  1.00 40.04 ? 65  ASN D C   1 
ATOM   2760  O  O   . ASN C  1 92  ? 52.699  125.436 -5.913  1.00 48.78 ? 65  ASN D O   1 
ATOM   2761  C  CB  . ASN C  1 92  ? 53.628  126.871 -8.047  1.00 39.29 ? 65  ASN D CB  1 
ATOM   2762  C  CG  . ASN C  1 92  ? 53.789  128.085 -7.156  1.00 40.65 ? 65  ASN D CG  1 
ATOM   2763  O  OD1 . ASN C  1 92  ? 54.821  128.284 -6.511  1.00 39.09 ? 65  ASN D OD1 1 
ATOM   2764  N  ND2 . ASN C  1 92  ? 52.749  128.907 -7.117  1.00 32.16 ? 65  ASN D ND2 1 
ATOM   2765  N  N   . PRO C  1 93  ? 54.516  124.149 -5.636  1.00 34.25 ? 66  PRO D N   1 
ATOM   2766  C  CA  . PRO C  1 93  ? 53.947  123.613 -4.384  1.00 39.04 ? 66  PRO D CA  1 
ATOM   2767  C  C   . PRO C  1 93  ? 53.867  124.657 -3.279  1.00 46.56 ? 66  PRO D C   1 
ATOM   2768  O  O   . PRO C  1 93  ? 52.901  124.664 -2.504  1.00 52.77 ? 66  PRO D O   1 
ATOM   2769  C  CB  . PRO C  1 93  ? 54.902  122.469 -4.012  1.00 32.76 ? 66  PRO D CB  1 
ATOM   2770  C  CG  . PRO C  1 93  ? 56.175  122.738 -4.744  1.00 38.28 ? 66  PRO D CG  1 
ATOM   2771  C  CD  . PRO C  1 93  ? 55.821  123.550 -5.972  1.00 35.67 ? 66  PRO D CD  1 
ATOM   2772  N  N   . LEU C  1 94  ? 54.852  125.550 -3.195  1.00 50.01 ? 67  LEU D N   1 
ATOM   2773  C  CA  . LEU C  1 94  ? 54.948  126.537 -2.122  1.00 42.94 ? 67  LEU D CA  1 
ATOM   2774  C  C   . LEU C  1 94  ? 54.098  127.775 -2.372  1.00 53.05 ? 67  LEU D C   1 
ATOM   2775  O  O   . LEU C  1 94  ? 54.170  128.717 -1.576  1.00 58.64 ? 67  LEU D O   1 
ATOM   2776  C  CB  . LEU C  1 94  ? 56.408  126.948 -1.932  1.00 43.92 ? 67  LEU D CB  1 
ATOM   2777  C  CG  . LEU C  1 94  ? 57.359  125.840 -1.482  1.00 41.06 ? 67  LEU D CG  1 
ATOM   2778  C  CD1 . LEU C  1 94  ? 58.707  126.414 -1.032  1.00 43.65 ? 67  LEU D CD1 1 
ATOM   2779  C  CD2 . LEU C  1 94  ? 56.724  124.972 -0.397  1.00 51.64 ? 67  LEU D CD2 1 
ATOM   2780  N  N   . SER C  1 95  ? 53.353  127.770 -3.474  1.00 51.44 ? 68  SER D N   1 
ATOM   2781  C  CA  . SER C  1 95  ? 52.403  128.856 -3.821  1.00 47.47 ? 68  SER D CA  1 
ATOM   2782  C  C   . SER C  1 95  ? 53.080  130.219 -3.790  1.00 52.31 ? 68  SER D C   1 
ATOM   2783  O  O   . SER C  1 95  ? 52.468  131.159 -3.302  1.00 56.95 ? 68  SER D O   1 
ATOM   2784  C  CB  . SER C  1 95  ? 51.240  128.840 -2.901  1.00 45.80 ? 68  SER D CB  1 
ATOM   2785  O  OG  . SER C  1 95  ? 50.880  127.512 -2.625  1.00 60.08 ? 68  SER D OG  1 
ATOM   2786  N  N   . ARG C  1 96  ? 54.266  130.335 -4.373  1.00 47.78 ? 69  ARG D N   1 
ATOM   2787  C  CA  . ARG C  1 96  ? 54.968  131.634 -4.400  1.00 46.77 ? 69  ARG D CA  1 
ATOM   2788  C  C   . ARG C  1 96  ? 54.594  132.416 -5.663  1.00 53.53 ? 69  ARG D C   1 
ATOM   2789  O  O   . ARG C  1 96  ? 53.436  132.360 -6.113  1.00 54.68 ? 69  ARG D O   1 
ATOM   2790  C  CB  . ARG C  1 96  ? 56.479  131.419 -4.308  1.00 45.44 ? 69  ARG D CB  1 
ATOM   2791  C  CG  . ARG C  1 96  ? 56.972  130.912 -2.960  1.00 45.59 ? 69  ARG D CG  1 
ATOM   2792  C  CD  . ARG C  1 96  ? 58.343  131.482 -2.687  1.00 50.41 ? 69  ARG D CD  1 
ATOM   2793  N  NE  . ARG C  1 96  ? 59.297  130.651 -1.976  1.00 61.85 ? 69  ARG D NE  1 
ATOM   2794  C  CZ  . ARG C  1 96  ? 59.146  130.213 -0.736  1.00 65.07 ? 69  ARG D CZ  1 
ATOM   2795  N  NH1 . ARG C  1 96  ? 58.052  130.509 -0.057  1.00 60.21 ? 69  ARG D NH1 1 
ATOM   2796  N  NH2 . ARG C  1 96  ? 60.086  129.477 -0.180  1.00 57.59 ? 69  ARG D NH2 1 
ATOM   2797  N  N   . LYS C  1 97  ? 55.553  133.175 -6.177  1.00 51.60 ? 70  LYS D N   1 
ATOM   2798  C  CA  . LYS C  1 97  ? 55.336  133.987 -7.393  1.00 46.82 ? 70  LYS D CA  1 
ATOM   2799  C  C   . LYS C  1 97  ? 56.461  133.671 -8.361  1.00 44.83 ? 70  LYS D C   1 
ATOM   2800  O  O   . LYS C  1 97  ? 57.540  133.307 -7.906  1.00 46.76 ? 70  LYS D O   1 
ATOM   2801  C  CB  . LYS C  1 97  ? 55.291  135.484 -7.072  1.00 52.38 ? 70  LYS D CB  1 
ATOM   2802  C  CG  . LYS C  1 97  ? 53.923  136.126 -7.244  1.00 48.23 ? 70  LYS D CG  1 
ATOM   2803  C  CD  . LYS C  1 97  ? 53.582  137.130 -6.191  1.00 46.81 ? 70  LYS D CD  1 
ATOM   2804  C  CE  . LYS C  1 97  ? 52.172  137.658 -6.322  1.00 48.23 ? 70  LYS D CE  1 
ATOM   2805  N  NZ  . LYS C  1 97  ? 51.311  136.717 -7.073  1.00 53.39 ? 70  LYS D NZ  1 
ATOM   2806  N  N   . HIS C  1 98  ? 56.196  133.852 -9.648  1.00 48.10 ? 71  HIS D N   1 
ATOM   2807  C  CA  . HIS C  1 98  ? 57.186  133.520 -10.688 1.00 38.60 ? 71  HIS D CA  1 
ATOM   2808  C  C   . HIS C  1 98  ? 58.441  134.374 -10.539 1.00 41.04 ? 71  HIS D C   1 
ATOM   2809  O  O   . HIS C  1 98  ? 58.337  135.525 -10.199 1.00 52.26 ? 71  HIS D O   1 
ATOM   2810  C  CB  . HIS C  1 98  ? 56.546  133.622 -12.079 1.00 44.10 ? 71  HIS D CB  1 
ATOM   2811  C  CG  . HIS C  1 98  ? 57.508  133.306 -13.163 1.00 47.19 ? 71  HIS D CG  1 
ATOM   2812  N  ND1 . HIS C  1 98  ? 57.915  132.025 -13.442 1.00 46.95 ? 71  HIS D ND1 1 
ATOM   2813  C  CD2 . HIS C  1 98  ? 58.200  134.109 -13.987 1.00 44.03 ? 71  HIS D CD2 1 
ATOM   2814  C  CE1 . HIS C  1 98  ? 58.813  132.065 -14.388 1.00 45.13 ? 71  HIS D CE1 1 
ATOM   2815  N  NE2 . HIS C  1 98  ? 58.999  133.311 -14.739 1.00 49.45 ? 71  HIS D NE2 1 
ATOM   2816  N  N   . GLY C  1 99  ? 59.595  133.772 -10.739 1.00 36.81 ? 72  GLY D N   1 
ATOM   2817  C  CA  . GLY C  1 99  ? 60.836  134.509 -10.779 1.00 34.52 ? 72  GLY D CA  1 
ATOM   2818  C  C   . GLY C  1 99  ? 61.890  133.759 -11.555 1.00 43.80 ? 72  GLY D C   1 
ATOM   2819  O  O   . GLY C  1 99  ? 61.602  132.785 -12.255 1.00 48.07 ? 72  GLY D O   1 
ATOM   2820  N  N   . GLY C  1 100 ? 63.114  134.236 -11.432 1.00 37.21 ? 73  GLY D N   1 
ATOM   2821  C  CA  . GLY C  1 100 ? 64.249  133.554 -11.998 1.00 41.82 ? 73  GLY D CA  1 
ATOM   2822  C  C   . GLY C  1 100 ? 64.742  132.447 -11.095 1.00 45.55 ? 73  GLY D C   1 
ATOM   2823  O  O   . GLY C  1 100 ? 64.381  132.343 -9.912  1.00 46.10 ? 73  GLY D O   1 
ATOM   2824  N  N   . PRO C  1 101 ? 65.600  131.588 -11.652 1.00 45.67 ? 74  PRO D N   1 
ATOM   2825  C  CA  . PRO C  1 101 ? 66.180  130.506 -10.838 1.00 43.85 ? 74  PRO D CA  1 
ATOM   2826  C  C   . PRO C  1 101 ? 67.050  131.006 -9.688  1.00 51.09 ? 74  PRO D C   1 
ATOM   2827  O  O   . PRO C  1 101 ? 67.207  130.284 -8.693  1.00 47.37 ? 74  PRO D O   1 
ATOM   2828  C  CB  . PRO C  1 101 ? 66.998  129.698 -11.855 1.00 41.47 ? 74  PRO D CB  1 
ATOM   2829  C  CG  . PRO C  1 101 ? 67.286  130.669 -12.978 1.00 38.51 ? 74  PRO D CG  1 
ATOM   2830  C  CD  . PRO C  1 101 ? 66.102  131.587 -13.037 1.00 37.05 ? 74  PRO D CD  1 
ATOM   2831  N  N   . LYS C  1 102 ? 67.613  132.213 -9.781  1.00 48.60 ? 75  LYS D N   1 
ATOM   2832  C  CA  . LYS C  1 102 ? 68.431  132.766 -8.709  1.00 42.64 ? 75  LYS D CA  1 
ATOM   2833  C  C   . LYS C  1 102 ? 67.644  133.654 -7.753  1.00 48.46 ? 75  LYS D C   1 
ATOM   2834  O  O   . LYS C  1 102 ? 68.208  134.119 -6.756  1.00 59.33 ? 75  LYS D O   1 
ATOM   2835  C  CB  . LYS C  1 102 ? 69.610  133.550 -9.291  1.00 40.13 ? 75  LYS D CB  1 
ATOM   2836  N  N   . ASP C  1 103 ? 66.367  133.907 -8.032  1.00 44.73 ? 76  ASP D N   1 
ATOM   2837  C  CA  . ASP C  1 103 ? 65.505  134.594 -7.083  1.00 39.38 ? 76  ASP D CA  1 
ATOM   2838  C  C   . ASP C  1 103 ? 65.153  133.669 -5.930  1.00 53.58 ? 76  ASP D C   1 
ATOM   2839  O  O   . ASP C  1 103 ? 65.028  132.451 -6.097  1.00 47.64 ? 76  ASP D O   1 
ATOM   2840  C  CB  . ASP C  1 103 ? 64.198  135.046 -7.741  1.00 48.47 ? 76  ASP D CB  1 
ATOM   2841  C  CG  . ASP C  1 103 ? 64.352  136.304 -8.581  1.00 62.82 ? 76  ASP D CG  1 
ATOM   2842  O  OD1 . ASP C  1 103 ? 65.448  136.533 -9.146  1.00 67.54 ? 76  ASP D OD1 1 
ATOM   2843  O  OD2 . ASP C  1 103 ? 63.359  137.069 -8.664  1.00 64.67 ? 76  ASP D OD2 1 
ATOM   2844  N  N   . GLU C  1 104 ? 64.948  134.260 -4.752  1.00 53.37 ? 77  GLU D N   1 
ATOM   2845  C  CA  . GLU C  1 104 ? 64.419  133.448 -3.666  1.00 50.91 ? 77  GLU D CA  1 
ATOM   2846  C  C   . GLU C  1 104 ? 62.903  133.306 -3.773  1.00 50.16 ? 77  GLU D C   1 
ATOM   2847  O  O   . GLU C  1 104 ? 62.346  132.273 -3.373  1.00 52.00 ? 77  GLU D O   1 
ATOM   2848  C  CB  . GLU C  1 104 ? 64.828  134.022 -2.307  1.00 52.64 ? 77  GLU D CB  1 
ATOM   2849  C  CG  . GLU C  1 104 ? 64.668  132.999 -1.193  1.00 51.01 ? 77  GLU D CG  1 
ATOM   2850  C  CD  . GLU C  1 104 ? 65.136  133.488 0.166   1.00 71.07 ? 77  GLU D CD  1 
ATOM   2851  O  OE1 . GLU C  1 104 ? 65.865  134.509 0.232   1.00 67.93 ? 77  GLU D OE1 1 
ATOM   2852  O  OE2 . GLU C  1 104 ? 64.767  132.835 1.172   1.00 64.15 ? 77  GLU D OE2 1 
ATOM   2853  N  N   . GLU C  1 105 ? 62.222  134.309 -4.321  1.00 44.01 ? 78  GLU D N   1 
ATOM   2854  C  CA  . GLU C  1 105 ? 60.809  134.176 -4.659  1.00 48.81 ? 78  GLU D CA  1 
ATOM   2855  C  C   . GLU C  1 105 ? 60.718  133.647 -6.091  1.00 52.84 ? 78  GLU D C   1 
ATOM   2856  O  O   . GLU C  1 105 ? 60.994  134.377 -7.049  1.00 46.59 ? 78  GLU D O   1 
ATOM   2857  C  CB  . GLU C  1 105 ? 60.079  135.506 -4.508  1.00 37.49 ? 78  GLU D CB  1 
ATOM   2858  C  CG  . GLU C  1 105 ? 58.612  135.467 -4.955  1.00 47.31 ? 78  GLU D CG  1 
ATOM   2859  C  CD  . GLU C  1 105 ? 57.670  134.994 -3.865  1.00 51.24 ? 78  GLU D CD  1 
ATOM   2860  O  OE1 . GLU C  1 105 ? 58.161  134.618 -2.783  1.00 61.32 ? 78  GLU D OE1 1 
ATOM   2861  O  OE2 . GLU C  1 105 ? 56.434  134.998 -4.079  1.00 54.12 ? 78  GLU D OE2 1 
ATOM   2862  N  N   . ARG C  1 106 ? 60.350  132.373 -6.229  1.00 53.14 ? 79  ARG D N   1 
ATOM   2863  C  CA  . ARG C  1 106 ? 60.248  131.716 -7.527  1.00 40.56 ? 79  ARG D CA  1 
ATOM   2864  C  C   . ARG C  1 106 ? 59.339  130.509 -7.364  1.00 45.71 ? 79  ARG D C   1 
ATOM   2865  O  O   . ARG C  1 106 ? 59.152  130.004 -6.256  1.00 40.25 ? 79  ARG D O   1 
ATOM   2866  C  CB  . ARG C  1 106 ? 61.627  131.287 -8.047  1.00 45.51 ? 79  ARG D CB  1 
ATOM   2867  C  CG  . ARG C  1 106 ? 62.374  130.358 -7.096  1.00 34.68 ? 79  ARG D CG  1 
ATOM   2868  C  CD  . ARG C  1 106 ? 63.596  129.722 -7.732  1.00 40.38 ? 79  ARG D CD  1 
ATOM   2869  N  NE  . ARG C  1 106 ? 63.287  128.426 -8.333  1.00 32.43 ? 79  ARG D NE  1 
ATOM   2870  C  CZ  . ARG C  1 106 ? 64.199  127.564 -8.768  1.00 41.04 ? 79  ARG D CZ  1 
ATOM   2871  N  NH1 . ARG C  1 106 ? 65.495  127.820 -8.679  1.00 38.76 ? 79  ARG D NH1 1 
ATOM   2872  N  NH2 . ARG C  1 106 ? 63.802  126.405 -9.292  1.00 38.84 ? 79  ARG D NH2 1 
ATOM   2873  N  N   . HIS C  1 107 ? 58.748  130.067 -8.472  1.00 39.78 ? 80  HIS D N   1 
ATOM   2874  C  CA  . HIS C  1 107 ? 58.158  128.736 -8.494  1.00 33.35 ? 80  HIS D CA  1 
ATOM   2875  C  C   . HIS C  1 107 ? 59.281  127.705 -8.424  1.00 31.17 ? 80  HIS D C   1 
ATOM   2876  O  O   . HIS C  1 107 ? 60.414  127.965 -8.850  1.00 33.33 ? 80  HIS D O   1 
ATOM   2877  C  CB  . HIS C  1 107 ? 57.316  128.531 -9.766  1.00 39.05 ? 80  HIS D CB  1 
ATOM   2878  C  CG  . HIS C  1 107 ? 56.187  129.513 -9.928  1.00 41.36 ? 80  HIS D CG  1 
ATOM   2879  N  ND1 . HIS C  1 107 ? 55.734  129.934 -11.162 1.00 52.15 ? 80  HIS D ND1 1 
ATOM   2880  C  CD2 . HIS C  1 107 ? 55.406  130.135 -9.012  1.00 47.68 ? 80  HIS D CD2 1 
ATOM   2881  C  CE1 . HIS C  1 107 ? 54.726  130.772 -10.998 1.00 43.18 ? 80  HIS D CE1 1 
ATOM   2882  N  NE2 . HIS C  1 107 ? 54.506  130.910 -9.702  1.00 43.78 ? 80  HIS D NE2 1 
ATOM   2883  N  N   . VAL C  1 108 ? 58.983  126.533 -7.844  1.00 32.98 ? 81  VAL D N   1 
ATOM   2884  C  CA  . VAL C  1 108 ? 59.975  125.458 -7.887  1.00 28.78 ? 81  VAL D CA  1 
ATOM   2885  C  C   . VAL C  1 108 ? 60.349  125.142 -9.334  1.00 27.09 ? 81  VAL D C   1 
ATOM   2886  O  O   . VAL C  1 108 ? 61.525  124.922 -9.648  1.00 29.55 ? 81  VAL D O   1 
ATOM   2887  C  CB  . VAL C  1 108 ? 59.462  124.212 -7.136  1.00 31.27 ? 81  VAL D CB  1 
ATOM   2888  C  CG1 . VAL C  1 108 ? 60.329  122.994 -7.456  1.00 26.84 ? 81  VAL D CG1 1 
ATOM   2889  C  CG2 . VAL C  1 108 ? 59.486  124.463 -5.620  1.00 30.34 ? 81  VAL D CG2 1 
ATOM   2890  N  N   . GLY C  1 109 ? 59.388  125.191 -10.242 1.00 31.12 ? 82  GLY D N   1 
ATOM   2891  C  CA  . GLY C  1 109 ? 59.710  124.878 -11.630 1.00 31.22 ? 82  GLY D CA  1 
ATOM   2892  C  C   . GLY C  1 109 ? 60.403  125.949 -12.463 1.00 36.62 ? 82  GLY D C   1 
ATOM   2893  O  O   . GLY C  1 109 ? 60.629  125.718 -13.657 1.00 29.40 ? 82  GLY D O   1 
ATOM   2894  N  N   . ASP C  1 110 ? 60.775  127.098 -11.895 1.00 39.43 ? 83  ASP D N   1 
ATOM   2895  C  CA  . ASP C  1 110 ? 61.326  128.216 -12.674 1.00 29.14 ? 83  ASP D CA  1 
ATOM   2896  C  C   . ASP C  1 110 ? 62.815  128.023 -12.920 1.00 37.86 ? 83  ASP D C   1 
ATOM   2897  O  O   . ASP C  1 110 ? 63.645  128.373 -12.078 1.00 38.87 ? 83  ASP D O   1 
ATOM   2898  C  CB  . ASP C  1 110 ? 61.087  129.535 -11.956 1.00 34.79 ? 83  ASP D CB  1 
ATOM   2899  C  CG  . ASP C  1 110 ? 59.630  129.916 -11.893 1.00 35.43 ? 83  ASP D CG  1 
ATOM   2900  O  OD1 . ASP C  1 110 ? 58.821  129.389 -12.699 1.00 32.53 ? 83  ASP D OD1 1 
ATOM   2901  O  OD2 . ASP C  1 110 ? 59.283  130.749 -11.028 1.00 41.54 ? 83  ASP D OD2 1 
ATOM   2902  N  N   . LEU C  1 111 ? 63.170  127.527 -14.111 1.00 24.41 ? 84  LEU D N   1 
ATOM   2903  C  CA  . LEU C  1 111 ? 64.559  127.305 -14.458 1.00 24.63 ? 84  LEU D CA  1 
ATOM   2904  C  C   . LEU C  1 111 ? 65.098  128.351 -15.436 1.00 28.66 ? 84  LEU D C   1 
ATOM   2905  O  O   . LEU C  1 111 ? 66.143  128.129 -16.057 1.00 36.32 ? 84  LEU D O   1 
ATOM   2906  C  CB  . LEU C  1 111 ? 64.733  125.894 -15.012 1.00 25.82 ? 84  LEU D CB  1 
ATOM   2907  C  CG  . LEU C  1 111 ? 64.163  124.815 -14.089 1.00 32.44 ? 84  LEU D CG  1 
ATOM   2908  C  CD1 . LEU C  1 111 ? 64.561  123.459 -14.595 1.00 33.23 ? 84  LEU D CD1 1 
ATOM   2909  C  CD2 . LEU C  1 111 ? 64.681  125.016 -12.658 1.00 32.48 ? 84  LEU D CD2 1 
ATOM   2910  N  N   . GLY C  1 112 ? 64.425  129.492 -15.565 1.00 28.78 ? 85  GLY D N   1 
ATOM   2911  C  CA  . GLY C  1 112 ? 65.018  130.620 -16.267 1.00 26.29 ? 85  GLY D CA  1 
ATOM   2912  C  C   . GLY C  1 112 ? 64.883  130.535 -17.776 1.00 27.15 ? 85  GLY D C   1 
ATOM   2913  O  O   . GLY C  1 112 ? 63.847  130.099 -18.278 1.00 30.32 ? 85  GLY D O   1 
ATOM   2914  N  N   . ASN C  1 113 ? 65.914  130.957 -18.498 1.00 28.22 ? 86  ASN D N   1 
ATOM   2915  C  CA  . ASN C  1 113 ? 65.924  130.923 -19.950 1.00 32.57 ? 86  ASN D CA  1 
ATOM   2916  C  C   . ASN C  1 113 ? 67.069  130.060 -20.424 1.00 32.11 ? 86  ASN D C   1 
ATOM   2917  O  O   . ASN C  1 113 ? 68.144  130.039 -19.817 1.00 36.53 ? 86  ASN D O   1 
ATOM   2918  C  CB  . ASN C  1 113 ? 66.081  132.319 -20.565 1.00 32.10 ? 86  ASN D CB  1 
ATOM   2919  C  CG  . ASN C  1 113 ? 64.898  133.211 -20.300 1.00 31.85 ? 86  ASN D CG  1 
ATOM   2920  O  OD1 . ASN C  1 113 ? 63.795  132.958 -20.791 1.00 40.31 ? 86  ASN D OD1 1 
ATOM   2921  N  ND2 . ASN C  1 113 ? 65.111  134.268 -19.512 1.00 40.44 ? 86  ASN D ND2 1 
ATOM   2922  N  N   . VAL C  1 114 ? 66.840  129.360 -21.523 1.00 30.84 ? 87  VAL D N   1 
ATOM   2923  C  CA  . VAL C  1 114 ? 67.926  128.778 -22.262 1.00 24.74 ? 87  VAL D CA  1 
ATOM   2924  C  C   . VAL C  1 114 ? 68.164  129.665 -23.475 1.00 27.44 ? 87  VAL D C   1 
ATOM   2925  O  O   . VAL C  1 114 ? 67.316  130.472 -23.858 1.00 27.14 ? 87  VAL D O   1 
ATOM   2926  C  CB  . VAL C  1 114 ? 67.645  127.312 -22.651 1.00 28.58 ? 87  VAL D CB  1 
ATOM   2927  C  CG1 . VAL C  1 114 ? 67.542  126.466 -21.375 1.00 29.13 ? 87  VAL D CG1 1 
ATOM   2928  C  CG2 . VAL C  1 114 ? 66.355  127.208 -23.442 1.00 26.88 ? 87  VAL D CG2 1 
ATOM   2929  N  N   . THR C  1 115 ? 69.344  129.530 -24.067 1.00 27.91 ? 88  THR D N   1 
ATOM   2930  C  CA  . THR C  1 115 ? 69.800  130.414 -25.129 1.00 30.52 ? 88  THR D CA  1 
ATOM   2931  C  C   . THR C  1 115 ? 70.020  129.599 -26.390 1.00 29.84 ? 88  THR D C   1 
ATOM   2932  O  O   . THR C  1 115 ? 70.905  128.737 -26.432 1.00 33.39 ? 88  THR D O   1 
ATOM   2933  C  CB  . THR C  1 115 ? 71.092  131.134 -24.720 1.00 37.24 ? 88  THR D CB  1 
ATOM   2934  O  OG1 . THR C  1 115 ? 70.792  132.096 -23.703 1.00 37.13 ? 88  THR D OG1 1 
ATOM   2935  C  CG2 . THR C  1 115 ? 71.724  131.852 -25.915 1.00 38.36 ? 88  THR D CG2 1 
ATOM   2936  N  N   . ALA C  1 116 ? 69.230  129.878 -27.421 1.00 28.00 ? 89  ALA D N   1 
ATOM   2937  C  CA  . ALA C  1 116 ? 69.437  129.267 -28.724 1.00 28.75 ? 89  ALA D CA  1 
ATOM   2938  C  C   . ALA C  1 116 ? 70.421  130.106 -29.537 1.00 31.01 ? 89  ALA D C   1 
ATOM   2939  O  O   . ALA C  1 116 ? 70.261  131.326 -29.652 1.00 30.95 ? 89  ALA D O   1 
ATOM   2940  C  CB  . ALA C  1 116 ? 68.109  129.121 -29.472 1.00 26.04 ? 89  ALA D CB  1 
ATOM   2941  N  N   . ASP C  1 117 ? 71.379  129.446 -30.154 1.00 32.69 ? 90  ASP D N   1 
ATOM   2942  C  CA  . ASP C  1 117 ? 72.378  130.127 -31.003 1.00 35.12 ? 90  ASP D CA  1 
ATOM   2943  C  C   . ASP C  1 117 ? 71.811  130.406 -32.402 1.00 38.75 ? 90  ASP D C   1 
ATOM   2944  O  O   . ASP C  1 117 ? 70.651  130.109 -32.682 1.00 30.68 ? 90  ASP D O   1 
ATOM   2945  C  CB  . ASP C  1 117 ? 73.666  129.312 -31.057 1.00 34.44 ? 90  ASP D CB  1 
ATOM   2946  C  CG  . ASP C  1 117 ? 73.573  127.989 -31.786 1.00 39.85 ? 90  ASP D CG  1 
ATOM   2947  O  OD1 . ASP C  1 117 ? 72.626  127.794 -32.529 1.00 39.02 ? 90  ASP D OD1 1 
ATOM   2948  O  OD2 . ASP C  1 117 ? 74.475  127.193 -31.616 1.00 43.08 ? 90  ASP D OD2 1 
ATOM   2949  N  N   . LYS C  1 118 ? 72.681  130.832 -33.317 1.00 36.15 ? 91  LYS D N   1 
ATOM   2950  C  CA  . LYS C  1 118 ? 72.261  131.154 -34.705 1.00 41.55 ? 91  LYS D CA  1 
ATOM   2951  C  C   . LYS C  1 118 ? 71.742  129.910 -35.435 1.00 36.61 ? 91  LYS D C   1 
ATOM   2952  O  O   . LYS C  1 118 ? 70.914  130.069 -36.289 1.00 41.57 ? 91  LYS D O   1 
ATOM   2953  C  CB  . LYS C  1 118 ? 73.384  131.861 -35.469 1.00 38.33 ? 91  LYS D CB  1 
ATOM   2954  C  CG  . LYS C  1 118 ? 74.657  131.052 -35.647 1.00 43.30 ? 91  LYS D CG  1 
ATOM   2955  C  CD  . LYS C  1 118 ? 75.744  131.786 -36.407 1.00 53.33 ? 91  LYS D CD  1 
ATOM   2956  C  CE  . LYS C  1 118 ? 76.308  132.958 -35.636 1.00 55.36 ? 91  LYS D CE  1 
ATOM   2957  N  NZ  . LYS C  1 118 ? 77.365  133.652 -36.406 1.00 55.58 ? 91  LYS D NZ  1 
ATOM   2958  N  N   . ASP C  1 119 ? 72.221  128.723 -35.087 1.00 37.20 ? 92  ASP D N   1 
ATOM   2959  C  CA  . ASP C  1 119 ? 71.770  127.446 -35.679 1.00 33.06 ? 92  ASP D CA  1 
ATOM   2960  C  C   . ASP C  1 119 ? 70.503  126.909 -34.987 1.00 33.83 ? 92  ASP D C   1 
ATOM   2961  O  O   . ASP C  1 119 ? 70.076  125.850 -35.357 1.00 35.78 ? 92  ASP D O   1 
ATOM   2962  C  CB  . ASP C  1 119 ? 72.929  126.462 -35.646 1.00 38.92 ? 92  ASP D CB  1 
ATOM   2963  C  CG  . ASP C  1 119 ? 74.116  126.976 -36.429 1.00 54.80 ? 92  ASP D CG  1 
ATOM   2964  O  OD1 . ASP C  1 119 ? 73.891  127.615 -37.459 1.00 65.74 ? 92  ASP D OD1 1 
ATOM   2965  O  OD2 . ASP C  1 119 ? 75.231  126.736 -36.006 1.00 60.60 ? 92  ASP D OD2 1 
ATOM   2966  N  N   . GLY C  1 120 ? 69.938  127.626 -34.024 1.00 27.44 ? 93  GLY D N   1 
ATOM   2967  C  CA  . GLY C  1 120 ? 68.698  127.218 -33.345 1.00 32.28 ? 93  GLY D CA  1 
ATOM   2968  C  C   . GLY C  1 120 ? 68.911  126.152 -32.280 1.00 30.09 ? 93  GLY D C   1 
ATOM   2969  O  O   . GLY C  1 120 ? 67.936  125.541 -31.894 1.00 26.04 ? 93  GLY D O   1 
ATOM   2970  N  N   . VAL C  1 121 ? 70.144  125.992 -31.814 1.00 23.61 ? 94  VAL D N   1 
ATOM   2971  C  CA  . VAL C  1 121 ? 70.521  124.990 -30.817 1.00 28.44 ? 94  VAL D CA  1 
ATOM   2972  C  C   . VAL C  1 121 ? 70.791  125.681 -29.488 1.00 34.23 ? 94  VAL D C   1 
ATOM   2973  O  O   . VAL C  1 121 ? 71.585  126.629 -29.424 1.00 27.09 ? 94  VAL D O   1 
ATOM   2974  C  CB  . VAL C  1 121 ? 71.757  124.188 -31.258 1.00 26.24 ? 94  VAL D CB  1 
ATOM   2975  C  CG1 . VAL C  1 121 ? 72.056  123.087 -30.240 1.00 34.14 ? 94  VAL D CG1 1 
ATOM   2976  C  CG2 . VAL C  1 121 ? 71.534  123.577 -32.644 1.00 28.64 ? 94  VAL D CG2 1 
ATOM   2977  N  N   . ALA C  1 122 ? 70.149  125.193 -28.425 1.00 27.28 ? 95  ALA D N   1 
ATOM   2978  C  CA  . ALA C  1 122 ? 70.369  125.679 -27.066 1.00 28.38 ? 95  ALA D CA  1 
ATOM   2979  C  C   . ALA C  1 122 ? 71.086  124.593 -26.276 1.00 32.81 ? 95  ALA D C   1 
ATOM   2980  O  O   . ALA C  1 122 ? 70.532  123.510 -26.064 1.00 34.22 ? 95  ALA D O   1 
ATOM   2981  C  CB  . ALA C  1 122 ? 69.052  126.036 -26.378 1.00 27.07 ? 95  ALA D CB  1 
ATOM   2982  N  N   . ASP C  1 123 ? 72.307  124.871 -25.848 1.00 33.37 ? 96  ASP D N   1 
ATOM   2983  C  CA  . ASP C  1 123 ? 73.044  123.947 -24.997 1.00 33.19 ? 96  ASP D CA  1 
ATOM   2984  C  C   . ASP C  1 123 ? 72.733  124.320 -23.552 1.00 34.46 ? 96  ASP D C   1 
ATOM   2985  O  O   . ASP C  1 123 ? 72.957  125.461 -23.138 1.00 32.18 ? 96  ASP D O   1 
ATOM   2986  C  CB  . ASP C  1 123 ? 74.536  124.008 -25.295 1.00 31.14 ? 96  ASP D CB  1 
ATOM   2987  C  CG  . ASP C  1 123 ? 74.868  123.434 -26.668 1.00 48.49 ? 96  ASP D CG  1 
ATOM   2988  O  OD1 . ASP C  1 123 ? 74.271  122.401 -27.057 1.00 49.13 ? 96  ASP D OD1 1 
ATOM   2989  O  OD2 . ASP C  1 123 ? 75.697  124.037 -27.383 1.00 60.98 ? 96  ASP D OD2 1 
ATOM   2990  N  N   . VAL C  1 124 ? 72.164  123.377 -22.813 1.00 28.20 ? 97  VAL D N   1 
ATOM   2991  C  CA  . VAL C  1 124 ? 71.671  123.615 -21.464 1.00 28.50 ? 97  VAL D CA  1 
ATOM   2992  C  C   . VAL C  1 124 ? 72.702  123.081 -20.478 1.00 27.78 ? 97  VAL D C   1 
ATOM   2993  O  O   . VAL C  1 124 ? 73.220  121.968 -20.643 1.00 25.42 ? 97  VAL D O   1 
ATOM   2994  C  CB  . VAL C  1 124 ? 70.301  122.944 -21.249 1.00 28.98 ? 97  VAL D CB  1 
ATOM   2995  C  CG1 . VAL C  1 124 ? 69.764  123.228 -19.862 1.00 28.24 ? 97  VAL D CG1 1 
ATOM   2996  C  CG2 . VAL C  1 124 ? 69.302  123.420 -22.304 1.00 28.75 ? 97  VAL D CG2 1 
ATOM   2997  N  N   . SER C  1 125 ? 73.022  123.888 -19.466 1.00 32.83 ? 98  SER D N   1 
ATOM   2998  C  CA  . SER C  1 125 ? 73.937  123.454 -18.411 1.00 30.90 ? 98  SER D CA  1 
ATOM   2999  C  C   . SER C  1 125 ? 73.630  124.324 -17.198 1.00 39.51 ? 98  SER D C   1 
ATOM   3000  O  O   . SER C  1 125 ? 74.104  125.460 -17.109 1.00 40.51 ? 98  SER D O   1 
ATOM   3001  C  CB  . SER C  1 125 ? 75.390  123.567 -18.834 1.00 40.91 ? 98  SER D CB  1 
ATOM   3002  O  OG  . SER C  1 125 ? 76.209  122.695 -18.067 1.00 44.64 ? 98  SER D OG  1 
ATOM   3003  N  N   . ILE C  1 126 ? 72.817  123.787 -16.299 1.00 32.69 ? 99  ILE D N   1 
ATOM   3004  C  CA  . ILE C  1 126 ? 72.315  124.486 -15.136 1.00 30.94 ? 99  ILE D CA  1 
ATOM   3005  C  C   . ILE C  1 126 ? 72.653  123.634 -13.918 1.00 31.82 ? 99  ILE D C   1 
ATOM   3006  O  O   . ILE C  1 126 ? 72.733  122.404 -14.000 1.00 32.46 ? 99  ILE D O   1 
ATOM   3007  C  CB  . ILE C  1 126 ? 70.794  124.721 -15.247 1.00 31.95 ? 99  ILE D CB  1 
ATOM   3008  C  CG1 . ILE C  1 126 ? 70.477  125.640 -16.422 1.00 42.88 ? 99  ILE D CG1 1 
ATOM   3009  C  CG2 . ILE C  1 126 ? 70.225  125.355 -13.992 1.00 40.62 ? 99  ILE D CG2 1 
ATOM   3010  C  CD1 . ILE C  1 126 ? 69.040  125.513 -16.885 1.00 42.35 ? 99  ILE D CD1 1 
ATOM   3011  N  N   . GLU C  1 127 ? 72.906  124.295 -12.799 1.00 33.80 ? 100 GLU D N   1 
ATOM   3012  C  CA  . GLU C  1 127 ? 72.887  123.654 -11.492 1.00 34.00 ? 100 GLU D CA  1 
ATOM   3013  C  C   . GLU C  1 127 ? 71.823  124.364 -10.678 1.00 32.08 ? 100 GLU D C   1 
ATOM   3014  O  O   . GLU C  1 127 ? 71.841  125.593 -10.572 1.00 40.79 ? 100 GLU D O   1 
ATOM   3015  C  CB  . GLU C  1 127 ? 74.255  123.731 -10.799 1.00 37.45 ? 100 GLU D CB  1 
ATOM   3016  C  CG  . GLU C  1 127 ? 74.320  122.981 -9.467  1.00 46.40 ? 100 GLU D CG  1 
ATOM   3017  C  CD  . GLU C  1 127 ? 75.479  123.437 -8.570  1.00 58.12 ? 100 GLU D CD  1 
ATOM   3018  O  OE1 . GLU C  1 127 ? 75.244  124.269 -7.662  1.00 57.47 ? 100 GLU D OE1 1 
ATOM   3019  O  OE2 . GLU C  1 127 ? 76.621  122.958 -8.777  1.00 59.77 ? 100 GLU D OE2 1 
ATOM   3020  N  N   . ASP C  1 128 ? 70.881  123.613 -10.132 1.00 27.20 ? 101 ASP D N   1 
ATOM   3021  C  CA  . ASP C  1 128 ? 69.802  124.252 -9.404  1.00 28.71 ? 101 ASP D CA  1 
ATOM   3022  C  C   . ASP C  1 128 ? 69.632  123.561 -8.052  1.00 39.03 ? 101 ASP D C   1 
ATOM   3023  O  O   . ASP C  1 128 ? 69.812  122.342 -7.939  1.00 30.88 ? 101 ASP D O   1 
ATOM   3024  C  CB  . ASP C  1 128 ? 68.504  124.213 -10.202 1.00 30.25 ? 101 ASP D CB  1 
ATOM   3025  C  CG  . ASP C  1 128 ? 67.386  124.962 -9.521  1.00 33.89 ? 101 ASP D CG  1 
ATOM   3026  O  OD1 . ASP C  1 128 ? 67.411  126.213 -9.550  1.00 49.75 ? 101 ASP D OD1 1 
ATOM   3027  O  OD2 . ASP C  1 128 ? 66.457  124.325 -9.007  1.00 34.74 ? 101 ASP D OD2 1 
ATOM   3028  N  N   . SER C  1 129 ? 69.284  124.338 -7.023  1.00 35.97 ? 102 SER D N   1 
ATOM   3029  C  CA  . SER C  1 129 ? 69.184  123.822 -5.659  1.00 38.34 ? 102 SER D CA  1 
ATOM   3030  C  C   . SER C  1 129 ? 67.769  123.859 -5.110  1.00 27.23 ? 102 SER D C   1 
ATOM   3031  O  O   . SER C  1 129 ? 67.570  123.575 -3.927  1.00 35.43 ? 102 SER D O   1 
ATOM   3032  C  CB  . SER C  1 129 ? 70.113  124.598 -4.719  1.00 36.50 ? 102 SER D CB  1 
ATOM   3033  O  OG  . SER C  1 129 ? 71.469  124.278 -4.990  1.00 49.10 ? 102 SER D OG  1 
ATOM   3034  N  N   . VAL C  1 130 ? 66.790  124.238 -5.917  1.00 29.89 ? 103 VAL D N   1 
ATOM   3035  C  CA  . VAL C  1 130 ? 65.400  124.246 -5.494  1.00 28.26 ? 103 VAL D CA  1 
ATOM   3036  C  C   . VAL C  1 130 ? 64.664  123.004 -5.982  1.00 37.01 ? 103 VAL D C   1 
ATOM   3037  O  O   . VAL C  1 130 ? 63.967  122.346 -5.209  1.00 32.52 ? 103 VAL D O   1 
ATOM   3038  C  CB  . VAL C  1 130 ? 64.709  125.542 -5.967  1.00 31.83 ? 103 VAL D CB  1 
ATOM   3039  C  CG1 . VAL C  1 130 ? 63.236  125.529 -5.596  1.00 28.24 ? 103 VAL D CG1 1 
ATOM   3040  C  CG2 . VAL C  1 130 ? 65.417  126.753 -5.352  1.00 40.33 ? 103 VAL D CG2 1 
ATOM   3041  N  N   . ILE C  1 131 ? 64.812  122.656 -7.265  1.00 29.08 ? 104 ILE D N   1 
ATOM   3042  C  CA  . ILE C  1 131 ? 64.221  121.409 -7.745  1.00 35.51 ? 104 ILE D CA  1 
ATOM   3043  C  C   . ILE C  1 131 ? 64.924  120.230 -7.079  1.00 30.59 ? 104 ILE D C   1 
ATOM   3044  O  O   . ILE C  1 131 ? 66.081  120.325 -6.650  1.00 23.74 ? 104 ILE D O   1 
ATOM   3045  C  CB  . ILE C  1 131 ? 64.309  121.293 -9.279  1.00 27.08 ? 104 ILE D CB  1 
ATOM   3046  C  CG1 . ILE C  1 131 ? 65.781  121.366 -9.739  1.00 27.16 ? 104 ILE D CG1 1 
ATOM   3047  C  CG2 . ILE C  1 131 ? 63.428  122.358 -9.896  1.00 27.68 ? 104 ILE D CG2 1 
ATOM   3048  C  CD1 . ILE C  1 131 ? 66.104  120.878 -11.206 1.00 20.72 ? 104 ILE D CD1 1 
ATOM   3049  N  N   . SER C  1 132 ? 64.231  119.096 -7.026  1.00 30.16 ? 105 SER D N   1 
ATOM   3050  C  CA  . SER C  1 132 ? 64.825  117.870 -6.522  1.00 28.43 ? 105 SER D CA  1 
ATOM   3051  C  C   . SER C  1 132 ? 64.303  116.689 -7.329  1.00 28.21 ? 105 SER D C   1 
ATOM   3052  O  O   . SER C  1 132 ? 63.258  116.776 -7.970  1.00 26.15 ? 105 SER D O   1 
ATOM   3053  C  CB  . SER C  1 132 ? 64.517  117.665 -5.030  1.00 24.63 ? 105 SER D CB  1 
ATOM   3054  O  OG  . SER C  1 132 ? 65.303  116.597 -4.540  1.00 29.00 ? 105 SER D OG  1 
ATOM   3055  N  N   . LEU C  1 133 ? 65.030  115.576 -7.273  1.00 25.82 ? 106 LEU D N   1 
ATOM   3056  C  CA  . LEU C  1 133 ? 64.558  114.327 -7.853  1.00 26.41 ? 106 LEU D CA  1 
ATOM   3057  C  C   . LEU C  1 133 ? 63.927  113.391 -6.825  1.00 35.11 ? 106 LEU D C   1 
ATOM   3058  O  O   . LEU C  1 133 ? 63.689  112.221 -7.142  1.00 29.06 ? 106 LEU D O   1 
ATOM   3059  C  CB  . LEU C  1 133 ? 65.699  113.618 -8.572  1.00 24.40 ? 106 LEU D CB  1 
ATOM   3060  C  CG  . LEU C  1 133 ? 66.391  114.422 -9.672  1.00 27.78 ? 106 LEU D CG  1 
ATOM   3061  C  CD1 . LEU C  1 133 ? 67.397  113.559 -10.424 1.00 24.54 ? 106 LEU D CD1 1 
ATOM   3062  C  CD2 . LEU C  1 133 ? 65.347  115.011 -10.624 1.00 23.30 ? 106 LEU D CD2 1 
ATOM   3063  N  N   . SER C  1 134 ? 63.661  113.875 -5.608  1.00 29.09 ? 107 SER D N   1 
ATOM   3064  C  CA  . SER C  1 134 ? 62.942  113.129 -4.576  1.00 35.82 ? 107 SER D CA  1 
ATOM   3065  C  C   . SER C  1 134 ? 62.322  114.133 -3.608  1.00 30.79 ? 107 SER D C   1 
ATOM   3066  O  O   . SER C  1 134 ? 62.691  115.311 -3.598  1.00 32.77 ? 107 SER D O   1 
ATOM   3067  C  CB  . SER C  1 134 ? 63.862  112.161 -3.816  1.00 33.25 ? 107 SER D CB  1 
ATOM   3068  O  OG  . SER C  1 134 ? 65.138  112.733 -3.560  1.00 33.78 ? 107 SER D OG  1 
ATOM   3069  N  N   . GLY C  1 135 ? 61.358  113.658 -2.802  1.00 30.58 ? 108 GLY D N   1 
ATOM   3070  C  CA  . GLY C  1 135 ? 60.743  114.494 -1.778  1.00 33.20 ? 108 GLY D CA  1 
ATOM   3071  C  C   . GLY C  1 135 ? 59.636  115.396 -2.306  1.00 45.53 ? 108 GLY D C   1 
ATOM   3072  O  O   . GLY C  1 135 ? 59.049  115.155 -3.361  1.00 40.08 ? 108 GLY D O   1 
ATOM   3073  N  N   . ASP C  1 136 ? 59.359  116.472 -1.561  1.00 39.38 ? 109 ASP D N   1 
ATOM   3074  C  CA  . ASP C  1 136 ? 58.205  117.312 -1.900  1.00 47.63 ? 109 ASP D CA  1 
ATOM   3075  C  C   . ASP C  1 136 ? 58.450  118.187 -3.127  1.00 31.11 ? 109 ASP D C   1 
ATOM   3076  O  O   . ASP C  1 136 ? 57.491  118.595 -3.784  1.00 37.44 ? 109 ASP D O   1 
ATOM   3077  C  CB  . ASP C  1 136 ? 57.807  118.194 -0.707  1.00 46.41 ? 109 ASP D CB  1 
ATOM   3078  C  CG  . ASP C  1 136 ? 56.847  117.486 0.265   1.00 60.45 ? 109 ASP D CG  1 
ATOM   3079  O  OD1 . ASP C  1 136 ? 56.458  116.328 -0.009  1.00 61.37 ? 109 ASP D OD1 1 
ATOM   3080  O  OD2 . ASP C  1 136 ? 56.494  118.081 1.315   1.00 57.77 ? 109 ASP D OD2 1 
ATOM   3081  N  N   . HIS C  1 137 ? 59.700  118.535 -3.415  1.00 33.87 ? 110 HIS D N   1 
ATOM   3082  C  CA  . HIS C  1 137 ? 60.027  119.311 -4.601  1.00 41.91 ? 110 HIS D CA  1 
ATOM   3083  C  C   . HIS C  1 137 ? 60.396  118.415 -5.773  1.00 38.34 ? 110 HIS D C   1 
ATOM   3084  O  O   . HIS C  1 137 ? 61.076  118.874 -6.709  1.00 33.34 ? 110 HIS D O   1 
ATOM   3085  C  CB  . HIS C  1 137 ? 61.162  120.293 -4.301  1.00 36.35 ? 110 HIS D CB  1 
ATOM   3086  C  CG  . HIS C  1 137 ? 60.738  121.455 -3.455  1.00 50.79 ? 110 HIS D CG  1 
ATOM   3087  N  ND1 . HIS C  1 137 ? 61.611  122.440 -3.045  1.00 48.46 ? 110 HIS D ND1 1 
ATOM   3088  C  CD2 . HIS C  1 137 ? 59.527  121.790 -2.949  1.00 43.78 ? 110 HIS D CD2 1 
ATOM   3089  C  CE1 . HIS C  1 137 ? 60.957  123.330 -2.320  1.00 49.42 ? 110 HIS D CE1 1 
ATOM   3090  N  NE2 . HIS C  1 137 ? 59.689  122.961 -2.251  1.00 52.32 ? 110 HIS D NE2 1 
ATOM   3091  N  N   . CYS C  1 138 ? 59.985  117.144 -5.715  1.00 28.64 ? 111 CYS D N   1 
ATOM   3092  C  CA  . CYS C  1 138 ? 60.351  116.167 -6.728  1.00 32.70 ? 111 CYS D CA  1 
ATOM   3093  C  C   . CYS C  1 138 ? 59.713  116.545 -8.058  1.00 19.41 ? 111 CYS D C   1 
ATOM   3094  O  O   . CYS C  1 138 ? 58.523  116.867 -8.105  1.00 22.72 ? 111 CYS D O   1 
ATOM   3095  C  CB  . CYS C  1 138 ? 59.883  114.783 -6.304  1.00 33.82 ? 111 CYS D CB  1 
ATOM   3096  S  SG  . CYS C  1 138 ? 60.255  113.501 -7.472  1.00 33.27 ? 111 CYS D SG  1 
ATOM   3097  N  N   . ILE C  1 139 ? 60.497  116.484 -9.131  1.00 25.18 ? 112 ILE D N   1 
ATOM   3098  C  CA  . ILE C  1 139 ? 60.005  116.838 -10.462 1.00 26.81 ? 112 ILE D CA  1 
ATOM   3099  C  C   . ILE C  1 139 ? 59.839  115.628 -11.366 1.00 26.50 ? 112 ILE D C   1 
ATOM   3100  O  O   . ILE C  1 139 ? 59.393  115.782 -12.521 1.00 22.89 ? 112 ILE D O   1 
ATOM   3101  C  CB  . ILE C  1 139 ? 60.911  117.892 -11.118 1.00 20.83 ? 112 ILE D CB  1 
ATOM   3102  C  CG1 . ILE C  1 139 ? 62.334  117.369 -11.282 1.00 23.74 ? 112 ILE D CG1 1 
ATOM   3103  C  CG2 . ILE C  1 139 ? 60.859  119.162 -10.278 1.00 24.12 ? 112 ILE D CG2 1 
ATOM   3104  C  CD1 . ILE C  1 139 ? 63.200  118.222 -12.190 1.00 26.14 ? 112 ILE D CD1 1 
ATOM   3105  N  N   . ILE C  1 140 ? 60.164  114.427 -10.878 1.00 25.96 ? 113 ILE D N   1 
ATOM   3106  C  CA  . ILE C  1 140 ? 59.895  113.207 -11.631 1.00 25.45 ? 113 ILE D CA  1 
ATOM   3107  C  C   . ILE C  1 140 ? 58.404  113.090 -11.876 1.00 20.59 ? 113 ILE D C   1 
ATOM   3108  O  O   . ILE C  1 140 ? 57.591  113.316 -10.982 1.00 18.51 ? 113 ILE D O   1 
ATOM   3109  C  CB  . ILE C  1 140 ? 60.420  111.986 -10.857 1.00 26.02 ? 113 ILE D CB  1 
ATOM   3110  C  CG1 . ILE C  1 140 ? 61.884  112.181 -10.486 1.00 32.53 ? 113 ILE D CG1 1 
ATOM   3111  C  CG2 . ILE C  1 140 ? 60.176  110.670 -11.638 1.00 24.48 ? 113 ILE D CG2 1 
ATOM   3112  C  CD1 . ILE C  1 140 ? 62.825  111.753 -11.522 1.00 27.25 ? 113 ILE D CD1 1 
ATOM   3113  N  N   . GLY C  1 141 ? 58.023  112.762 -13.105 1.00 20.00 ? 114 GLY D N   1 
ATOM   3114  C  CA  . GLY C  1 141 ? 56.614  112.620 -13.396 1.00 17.27 ? 114 GLY D CA  1 
ATOM   3115  C  C   . GLY C  1 141 ? 55.920  113.908 -13.760 1.00 19.09 ? 114 GLY D C   1 
ATOM   3116  O  O   . GLY C  1 141 ? 54.717  113.890 -14.047 1.00 19.02 ? 114 GLY D O   1 
ATOM   3117  N  N   . ARG C  1 142 ? 56.626  115.021 -13.736 1.00 20.00 ? 115 ARG D N   1 
ATOM   3118  C  CA  . ARG C  1 142 ? 56.075  116.294 -14.153 1.00 20.47 ? 115 ARG D CA  1 
ATOM   3119  C  C   . ARG C  1 142 ? 56.601  116.568 -15.553 1.00 20.00 ? 115 ARG D C   1 
ATOM   3120  O  O   . ARG C  1 142 ? 57.308  115.746 -16.136 1.00 22.08 ? 115 ARG D O   1 
ATOM   3121  C  CB  . ARG C  1 142 ? 56.454  117.376 -13.146 1.00 19.64 ? 115 ARG D CB  1 
ATOM   3122  C  CG  . ARG C  1 142 ? 56.129  116.909 -11.702 1.00 21.92 ? 115 ARG D CG  1 
ATOM   3123  C  CD  . ARG C  1 142 ? 55.984  118.051 -10.731 1.00 29.00 ? 115 ARG D CD  1 
ATOM   3124  N  NE  . ARG C  1 142 ? 55.661  117.568 -9.387  1.00 27.27 ? 115 ARG D NE  1 
ATOM   3125  C  CZ  . ARG C  1 142 ? 54.440  117.467 -8.882  1.00 27.64 ? 115 ARG D CZ  1 
ATOM   3126  N  NH1 . ARG C  1 142 ? 53.365  117.806 -9.579  1.00 24.24 ? 115 ARG D NH1 1 
ATOM   3127  N  NH2 . ARG C  1 142 ? 54.293  117.017 -7.637  1.00 31.99 ? 115 ARG D NH2 1 
ATOM   3128  N  N   . THR C  1 143 ? 56.270  117.726 -16.095 1.00 21.52 ? 116 THR D N   1 
ATOM   3129  C  CA  . THR C  1 143 ? 56.584  118.037 -17.495 1.00 16.26 ? 116 THR D CA  1 
ATOM   3130  C  C   . THR C  1 143 ? 57.530  119.213 -17.608 1.00 19.93 ? 116 THR D C   1 
ATOM   3131  O  O   . THR C  1 143 ? 57.278  120.278 -17.035 1.00 29.65 ? 116 THR D O   1 
ATOM   3132  C  CB  . THR C  1 143 ? 55.326  118.347 -18.304 1.00 22.20 ? 116 THR D CB  1 
ATOM   3133  O  OG1 . THR C  1 143 ? 54.432  117.225 -18.303 1.00 24.62 ? 116 THR D OG1 1 
ATOM   3134  C  CG2 . THR C  1 143 ? 55.671  118.749 -19.723 1.00 19.89 ? 116 THR D CG2 1 
ATOM   3135  N  N   . LEU C  1 144 ? 58.608  119.013 -18.358 1.00 19.23 ? 117 LEU D N   1 
ATOM   3136  C  CA  . LEU C  1 144 ? 59.531  120.079 -18.700 1.00 17.53 ? 117 LEU D CA  1 
ATOM   3137  C  C   . LEU C  1 144 ? 59.051  120.706 -19.996 1.00 27.11 ? 117 LEU D C   1 
ATOM   3138  O  O   . LEU C  1 144 ? 58.710  119.982 -20.928 1.00 21.35 ? 117 LEU D O   1 
ATOM   3139  C  CB  . LEU C  1 144 ? 60.936  119.526 -18.860 1.00 15.54 ? 117 LEU D CB  1 
ATOM   3140  C  CG  . LEU C  1 144 ? 62.058  120.501 -19.160 1.00 19.65 ? 117 LEU D CG  1 
ATOM   3141  C  CD1 . LEU C  1 144 ? 62.203  121.492 -18.019 1.00 25.36 ? 117 LEU D CD1 1 
ATOM   3142  C  CD2 . LEU C  1 144 ? 63.332  119.690 -19.346 1.00 21.78 ? 117 LEU D CD2 1 
ATOM   3143  N  N   . VAL C  1 145 ? 59.011  122.039 -20.048 1.00 22.17 ? 118 VAL D N   1 
ATOM   3144  C  CA  . VAL C  1 145 ? 58.485  122.766 -21.207 1.00 23.20 ? 118 VAL D CA  1 
ATOM   3145  C  C   . VAL C  1 145 ? 59.479  123.841 -21.627 1.00 27.17 ? 118 VAL D C   1 
ATOM   3146  O  O   . VAL C  1 145 ? 60.001  124.586 -20.790 1.00 23.81 ? 118 VAL D O   1 
ATOM   3147  C  CB  . VAL C  1 145 ? 57.118  123.416 -20.914 1.00 20.55 ? 118 VAL D CB  1 
ATOM   3148  C  CG1 . VAL C  1 145 ? 56.579  124.160 -22.171 1.00 24.07 ? 118 VAL D CG1 1 
ATOM   3149  C  CG2 . VAL C  1 145 ? 56.117  122.385 -20.433 1.00 24.51 ? 118 VAL D CG2 1 
ATOM   3150  N  N   . VAL C  1 146 ? 59.727  123.948 -22.928 1.00 23.88 ? 119 VAL D N   1 
ATOM   3151  C  CA  . VAL C  1 146 ? 60.487  125.065 -23.474 1.00 21.36 ? 119 VAL D CA  1 
ATOM   3152  C  C   . VAL C  1 146 ? 59.498  125.965 -24.203 1.00 23.80 ? 119 VAL D C   1 
ATOM   3153  O  O   . VAL C  1 146 ? 58.621  125.477 -24.930 1.00 24.17 ? 119 VAL D O   1 
ATOM   3154  C  CB  . VAL C  1 146 ? 61.642  124.590 -24.369 1.00 21.23 ? 119 VAL D CB  1 
ATOM   3155  C  CG1 . VAL C  1 146 ? 61.119  123.823 -25.594 1.00 21.12 ? 119 VAL D CG1 1 
ATOM   3156  C  CG2 . VAL C  1 146 ? 62.519  125.771 -24.786 1.00 24.92 ? 119 VAL D CG2 1 
ATOM   3157  N  N   . HIS C  1 147 ? 59.588  127.264 -23.952 1.00 23.16 ? 120 HIS D N   1 
ATOM   3158  C  CA  . HIS C  1 147 ? 58.555  128.209 -24.344 1.00 23.99 ? 120 HIS D CA  1 
ATOM   3159  C  C   . HIS C  1 147 ? 58.988  129.044 -25.551 1.00 23.84 ? 120 HIS D C   1 
ATOM   3160  O  O   . HIS C  1 147 ? 60.159  129.099 -25.934 1.00 22.15 ? 120 HIS D O   1 
ATOM   3161  C  CB  . HIS C  1 147 ? 58.195  129.138 -23.175 1.00 26.27 ? 120 HIS D CB  1 
ATOM   3162  C  CG  . HIS C  1 147 ? 57.376  128.483 -22.105 1.00 27.41 ? 120 HIS D CG  1 
ATOM   3163  N  ND1 . HIS C  1 147 ? 56.006  128.605 -22.038 1.00 32.90 ? 120 HIS D ND1 1 
ATOM   3164  C  CD2 . HIS C  1 147 ? 57.735  127.698 -21.062 1.00 24.87 ? 120 HIS D CD2 1 
ATOM   3165  C  CE1 . HIS C  1 147 ? 55.554  127.928 -20.996 1.00 27.89 ? 120 HIS D CE1 1 
ATOM   3166  N  NE2 . HIS C  1 147 ? 56.583  127.365 -20.391 1.00 27.79 ? 120 HIS D NE2 1 
ATOM   3167  N  N   . GLU C  1 148 ? 58.000  129.734 -26.119 1.00 26.37 ? 121 GLU D N   1 
ATOM   3168  C  CA  . GLU C  1 148 ? 58.194  130.481 -27.361 1.00 30.14 ? 121 GLU D CA  1 
ATOM   3169  C  C   . GLU C  1 148 ? 59.061  131.720 -27.159 1.00 28.48 ? 121 GLU D C   1 
ATOM   3170  O  O   . GLU C  1 148 ? 59.904  132.040 -28.008 1.00 33.12 ? 121 GLU D O   1 
ATOM   3171  C  CB  . GLU C  1 148 ? 56.829  130.869 -27.910 1.00 31.75 ? 121 GLU D CB  1 
ATOM   3172  C  CG  . GLU C  1 148 ? 56.818  132.058 -28.849 1.00 41.82 ? 121 GLU D CG  1 
ATOM   3173  C  CD  . GLU C  1 148 ? 55.396  132.521 -29.130 1.00 49.69 ? 121 GLU D CD  1 
ATOM   3174  O  OE1 . GLU C  1 148 ? 54.632  132.704 -28.149 1.00 47.86 ? 121 GLU D OE1 1 
ATOM   3175  O  OE2 . GLU C  1 148 ? 55.044  132.694 -30.324 1.00 48.74 ? 121 GLU D OE2 1 
ATOM   3176  N  N   . LYS C  1 149 ? 58.873  132.425 -26.045 1.00 29.58 ? 122 LYS D N   1 
ATOM   3177  C  CA  . LYS C  1 149 ? 59.507  133.716 -25.804 1.00 36.96 ? 122 LYS D CA  1 
ATOM   3178  C  C   . LYS C  1 149 ? 60.377  133.658 -24.553 1.00 39.01 ? 122 LYS D C   1 
ATOM   3179  O  O   . LYS C  1 149 ? 60.326  132.705 -23.770 1.00 29.03 ? 122 LYS D O   1 
ATOM   3180  C  CB  . LYS C  1 149 ? 58.459  134.824 -25.631 1.00 34.48 ? 122 LYS D CB  1 
ATOM   3181  C  CG  . LYS C  1 149 ? 57.834  135.359 -26.911 1.00 40.17 ? 122 LYS D CG  1 
ATOM   3182  C  CD  . LYS C  1 149 ? 56.598  136.192 -26.565 1.00 42.68 ? 122 LYS D CD  1 
ATOM   3183  C  CE  . LYS C  1 149 ? 55.396  135.858 -27.448 1.00 49.17 ? 122 LYS D CE  1 
ATOM   3184  N  NZ  . LYS C  1 149 ? 55.487  136.461 -28.821 1.00 54.10 ? 122 LYS D NZ  1 
ATOM   3185  N  N   . ALA C  1 150 ? 61.164  134.713 -24.359 1.00 36.18 ? 123 ALA D N   1 
ATOM   3186  C  CA  . ALA C  1 150 ? 61.969  134.836 -23.152 1.00 30.54 ? 123 ALA D CA  1 
ATOM   3187  C  C   . ALA C  1 150 ? 61.082  134.959 -21.922 1.00 35.88 ? 123 ALA D C   1 
ATOM   3188  O  O   . ALA C  1 150 ? 59.944  135.438 -21.982 1.00 33.22 ? 123 ALA D O   1 
ATOM   3189  C  CB  . ALA C  1 150 ? 62.906  136.044 -23.248 1.00 35.27 ? 123 ALA D CB  1 
ATOM   3190  N  N   . ASP C  1 151 ? 61.603  134.464 -20.806 1.00 32.70 ? 124 ASP D N   1 
ATOM   3191  C  CA  . ASP C  1 151 ? 60.994  134.633 -19.501 1.00 38.49 ? 124 ASP D CA  1 
ATOM   3192  C  C   . ASP C  1 151 ? 61.510  135.947 -18.928 1.00 30.18 ? 124 ASP D C   1 
ATOM   3193  O  O   . ASP C  1 151 ? 62.724  136.166 -18.889 1.00 38.12 ? 124 ASP D O   1 
ATOM   3194  C  CB  . ASP C  1 151 ? 61.381  133.445 -18.619 1.00 38.46 ? 124 ASP D CB  1 
ATOM   3195  C  CG  . ASP C  1 151 ? 60.667  133.418 -17.281 1.00 47.53 ? 124 ASP D CG  1 
ATOM   3196  O  OD1 . ASP C  1 151 ? 60.014  134.409 -16.880 1.00 44.30 ? 124 ASP D OD1 1 
ATOM   3197  O  OD2 . ASP C  1 151 ? 60.783  132.364 -16.619 1.00 41.40 ? 124 ASP D OD2 1 
ATOM   3198  N  N   . ASP C  1 152 ? 60.602  136.839 -18.547 1.00 36.56 ? 125 ASP D N   1 
ATOM   3199  C  CA  . ASP C  1 152 ? 61.062  138.116 -17.999 1.00 44.04 ? 125 ASP D CA  1 
ATOM   3200  C  C   . ASP C  1 152 ? 61.529  137.991 -16.550 1.00 48.48 ? 125 ASP D C   1 
ATOM   3201  O  O   . ASP C  1 152 ? 61.903  139.003 -15.943 1.00 45.69 ? 125 ASP D O   1 
ATOM   3202  C  CB  . ASP C  1 152 ? 59.970  139.193 -18.125 1.00 35.40 ? 125 ASP D CB  1 
ATOM   3203  C  CG  . ASP C  1 152 ? 58.677  138.828 -17.417 1.00 44.84 ? 125 ASP D CG  1 
ATOM   3204  O  OD1 . ASP C  1 152 ? 58.732  138.209 -16.331 1.00 52.10 ? 125 ASP D OD1 1 
ATOM   3205  O  OD2 . ASP C  1 152 ? 57.595  139.193 -17.937 1.00 45.99 ? 125 ASP D OD2 1 
ATOM   3206  N  N   . LEU C  1 153 ? 61.508  136.771 -16.000 1.00 47.22 ? 126 LEU D N   1 
ATOM   3207  C  CA  . LEU C  1 153 ? 61.978  136.453 -14.653 1.00 44.05 ? 126 LEU D CA  1 
ATOM   3208  C  C   . LEU C  1 153 ? 61.090  137.072 -13.578 1.00 46.10 ? 126 LEU D C   1 
ATOM   3209  O  O   . LEU C  1 153 ? 61.546  137.347 -12.466 1.00 53.58 ? 126 LEU D O   1 
ATOM   3210  C  CB  . LEU C  1 153 ? 63.446  136.862 -14.463 1.00 41.06 ? 126 LEU D CB  1 
ATOM   3211  C  CG  . LEU C  1 153 ? 64.361  136.283 -15.550 1.00 45.98 ? 126 LEU D CG  1 
ATOM   3212  C  CD1 . LEU C  1 153 ? 65.833  136.684 -15.369 1.00 41.78 ? 126 LEU D CD1 1 
ATOM   3213  C  CD2 . LEU C  1 153 ? 64.195  134.760 -15.653 1.00 39.70 ? 126 LEU D CD2 1 
ATOM   3214  N  N   . GLY C  1 154 ? 59.806  137.273 -13.887 1.00 44.39 ? 127 GLY D N   1 
ATOM   3215  C  CA  . GLY C  1 154 ? 58.868  137.848 -12.947 1.00 42.07 ? 127 GLY D CA  1 
ATOM   3216  C  C   . GLY C  1 154 ? 58.910  139.360 -12.831 1.00 50.14 ? 127 GLY D C   1 
ATOM   3217  O  O   . GLY C  1 154 ? 57.991  139.948 -12.246 1.00 51.87 ? 127 GLY D O   1 
ATOM   3218  N  N   . LYS C  1 155 ? 59.933  140.008 -13.384 1.00 51.52 ? 128 LYS D N   1 
ATOM   3219  C  CA  . LYS C  1 155 ? 60.107  141.460 -13.303 1.00 49.75 ? 128 LYS D CA  1 
ATOM   3220  C  C   . LYS C  1 155 ? 59.572  142.165 -14.548 1.00 48.00 ? 128 LYS D C   1 
ATOM   3221  O  O   . LYS C  1 155 ? 60.280  142.938 -15.192 1.00 54.77 ? 128 LYS D O   1 
ATOM   3222  C  CB  . LYS C  1 155 ? 61.580  141.778 -13.092 1.00 45.84 ? 128 LYS D CB  1 
ATOM   3223  C  CG  . LYS C  1 155 ? 62.182  141.060 -11.906 1.00 44.00 ? 128 LYS D CG  1 
ATOM   3224  C  CD  . LYS C  1 155 ? 63.591  140.594 -12.219 1.00 49.32 ? 128 LYS D CD  1 
ATOM   3225  C  CE  . LYS C  1 155 ? 63.918  139.310 -11.449 1.00 53.40 ? 128 LYS D CE  1 
ATOM   3226  N  NZ  . LYS C  1 155 ? 63.537  139.428 -10.007 1.00 53.41 ? 128 LYS D NZ  1 
ATOM   3227  N  N   . GLY C  1 156 ? 58.309  141.907 -14.890 1.00 50.25 ? 129 GLY D N   1 
ATOM   3228  C  CA  . GLY C  1 156 ? 57.734  142.422 -16.120 1.00 49.44 ? 129 GLY D CA  1 
ATOM   3229  C  C   . GLY C  1 156 ? 56.689  143.507 -15.934 1.00 55.30 ? 129 GLY D C   1 
ATOM   3230  O  O   . GLY C  1 156 ? 56.151  144.040 -16.912 1.00 59.11 ? 129 GLY D O   1 
ATOM   3231  N  N   . GLY C  1 157 ? 56.381  143.836 -14.684 1.00 55.11 ? 130 GLY D N   1 
ATOM   3232  C  CA  . GLY C  1 157 ? 55.482  144.942 -14.422 1.00 55.54 ? 130 GLY D CA  1 
ATOM   3233  C  C   . GLY C  1 157 ? 54.037  144.722 -14.811 1.00 58.74 ? 130 GLY D C   1 
ATOM   3234  O  O   . GLY C  1 157 ? 53.320  145.697 -15.057 1.00 61.43 ? 130 GLY D O   1 
ATOM   3235  N  N   . ASN C  1 158 ? 53.578  143.474 -14.876 1.00 54.93 ? 131 ASN D N   1 
ATOM   3236  C  CA  . ASN C  1 158 ? 52.163  143.223 -15.113 1.00 47.54 ? 131 ASN D CA  1 
ATOM   3237  C  C   . ASN C  1 158 ? 51.790  141.897 -14.466 1.00 57.43 ? 131 ASN D C   1 
ATOM   3238  O  O   . ASN C  1 158 ? 52.648  141.146 -13.990 1.00 59.45 ? 131 ASN D O   1 
ATOM   3239  C  CB  . ASN C  1 158 ? 51.835  143.230 -16.611 1.00 50.03 ? 131 ASN D CB  1 
ATOM   3240  C  CG  . ASN C  1 158 ? 52.102  141.894 -17.277 1.00 56.81 ? 131 ASN D CG  1 
ATOM   3241  O  OD1 . ASN C  1 158 ? 53.247  141.558 -17.594 1.00 53.13 ? 131 ASN D OD1 1 
ATOM   3242  N  ND2 . ASN C  1 158 ? 51.033  141.148 -17.548 1.00 53.95 ? 131 ASN D ND2 1 
ATOM   3243  N  N   . GLU C  1 159 ? 50.486  141.621 -14.455 1.00 52.49 ? 132 GLU D N   1 
ATOM   3244  C  CA  . GLU C  1 159 ? 49.970  140.443 -13.765 1.00 53.33 ? 132 GLU D CA  1 
ATOM   3245  C  C   . GLU C  1 159 ? 50.541  139.159 -14.361 1.00 56.51 ? 132 GLU D C   1 
ATOM   3246  O  O   . GLU C  1 159 ? 51.017  138.276 -13.633 1.00 56.85 ? 132 GLU D O   1 
ATOM   3247  C  CB  . GLU C  1 159 ? 48.444  140.454 -13.836 1.00 50.83 ? 132 GLU D CB  1 
ATOM   3248  C  CG  . GLU C  1 159 ? 47.731  139.523 -12.875 1.00 52.63 ? 132 GLU D CG  1 
ATOM   3249  C  CD  . GLU C  1 159 ? 46.332  139.165 -13.368 1.00 69.12 ? 132 GLU D CD  1 
ATOM   3250  O  OE1 . GLU C  1 159 ? 45.753  139.968 -14.143 1.00 64.29 ? 132 GLU D OE1 1 
ATOM   3251  O  OE2 . GLU C  1 159 ? 45.813  138.085 -12.988 1.00 63.90 ? 132 GLU D OE2 1 
ATOM   3252  N  N   . GLU C  1 160 ? 50.523  139.049 -15.693 1.00 50.76 ? 133 GLU D N   1 
ATOM   3253  C  CA  . GLU C  1 160 ? 50.974  137.831 -16.354 1.00 48.59 ? 133 GLU D CA  1 
ATOM   3254  C  C   . GLU C  1 160 ? 52.455  137.566 -16.116 1.00 51.91 ? 133 GLU D C   1 
ATOM   3255  O  O   . GLU C  1 160 ? 52.901  136.416 -16.235 1.00 53.62 ? 133 GLU D O   1 
ATOM   3256  C  CB  . GLU C  1 160 ? 50.679  137.921 -17.857 1.00 51.33 ? 133 GLU D CB  1 
ATOM   3257  C  CG  . GLU C  1 160 ? 50.823  136.603 -18.615 1.00 44.71 ? 133 GLU D CG  1 
ATOM   3258  C  CD  . GLU C  1 160 ? 49.817  135.562 -18.134 1.00 62.82 ? 133 GLU D CD  1 
ATOM   3259  O  OE1 . GLU C  1 160 ? 48.614  135.895 -18.042 1.00 71.04 ? 133 GLU D OE1 1 
ATOM   3260  O  OE2 . GLU C  1 160 ? 50.223  134.418 -17.844 1.00 55.10 ? 133 GLU D OE2 1 
ATOM   3261  N  N   . SER C  1 161 ? 53.224  138.596 -15.764 1.00 45.70 ? 134 SER D N   1 
ATOM   3262  C  CA  . SER C  1 161 ? 54.633  138.390 -15.461 1.00 45.75 ? 134 SER D CA  1 
ATOM   3263  C  C   . SER C  1 161 ? 54.819  137.561 -14.195 1.00 48.59 ? 134 SER D C   1 
ATOM   3264  O  O   . SER C  1 161 ? 55.773  136.780 -14.099 1.00 48.48 ? 134 SER D O   1 
ATOM   3265  C  CB  . SER C  1 161 ? 55.336  139.738 -15.319 1.00 41.38 ? 134 SER D CB  1 
ATOM   3266  O  OG  . SER C  1 161 ? 56.699  139.562 -14.976 1.00 55.72 ? 134 SER D OG  1 
ATOM   3267  N  N   . THR C  1 162 ? 53.923  137.726 -13.218 1.00 54.37 ? 135 THR D N   1 
ATOM   3268  C  CA  . THR C  1 162 ? 54.005  137.039 -11.934 1.00 50.02 ? 135 THR D CA  1 
ATOM   3269  C  C   . THR C  1 162 ? 53.510  135.600 -11.995 1.00 51.44 ? 135 THR D C   1 
ATOM   3270  O  O   . THR C  1 162 ? 53.668  134.868 -11.010 1.00 53.71 ? 135 THR D O   1 
ATOM   3271  C  CB  . THR C  1 162 ? 53.199  137.809 -10.879 1.00 50.42 ? 135 THR D CB  1 
ATOM   3272  O  OG1 . THR C  1 162 ? 51.799  137.536 -11.046 1.00 55.49 ? 135 THR D OG1 1 
ATOM   3273  C  CG2 . THR C  1 162 ? 53.442  139.312 -11.005 1.00 44.79 ? 135 THR D CG2 1 
ATOM   3274  N  N   . LYS C  1 163 ? 52.900  135.192 -13.110 1.00 55.25 ? 136 LYS D N   1 
ATOM   3275  C  CA  . LYS C  1 163 ? 52.437  133.826 -13.326 1.00 51.01 ? 136 LYS D CA  1 
ATOM   3276  C  C   . LYS C  1 163 ? 53.382  133.035 -14.222 1.00 52.60 ? 136 LYS D C   1 
ATOM   3277  O  O   . LYS C  1 163 ? 53.799  131.928 -13.875 1.00 50.50 ? 136 LYS D O   1 
ATOM   3278  C  CB  . LYS C  1 163 ? 51.039  133.835 -13.956 1.00 47.05 ? 136 LYS D CB  1 
ATOM   3279  C  CG  . LYS C  1 163 ? 49.876  133.935 -12.985 1.00 47.47 ? 136 LYS D CG  1 
ATOM   3280  C  CD  . LYS C  1 163 ? 48.767  134.812 -13.569 1.00 49.63 ? 136 LYS D CD  1 
ATOM   3281  C  CE  . LYS C  1 163 ? 47.510  134.771 -12.704 1.00 50.90 ? 136 LYS D CE  1 
ATOM   3282  N  NZ  . LYS C  1 163 ? 47.052  136.117 -12.219 1.00 51.46 ? 136 LYS D NZ  1 
ATOM   3283  N  N   . THR C  1 164 ? 53.715  133.586 -15.387 1.00 47.82 ? 137 THR D N   1 
ATOM   3284  C  CA  . THR C  1 164 ? 54.449  132.866 -16.413 1.00 42.89 ? 137 THR D CA  1 
ATOM   3285  C  C   . THR C  1 164 ? 55.705  133.571 -16.893 1.00 44.27 ? 137 THR D C   1 
ATOM   3286  O  O   . THR C  1 164 ? 56.452  132.987 -17.689 1.00 44.86 ? 137 THR D O   1 
ATOM   3287  C  CB  . THR C  1 164 ? 53.538  132.590 -17.624 1.00 47.45 ? 137 THR D CB  1 
ATOM   3288  O  OG1 . THR C  1 164 ? 53.538  133.727 -18.503 1.00 50.31 ? 137 THR D OG1 1 
ATOM   3289  C  CG2 . THR C  1 164 ? 52.119  132.219 -17.197 1.00 47.77 ? 137 THR D CG2 1 
ATOM   3290  N  N   . GLY C  1 165 ? 55.965  134.797 -16.445 1.00 37.31 ? 138 GLY D N   1 
ATOM   3291  C  CA  . GLY C  1 165 ? 57.074  135.537 -17.003 1.00 36.98 ? 138 GLY D CA  1 
ATOM   3292  C  C   . GLY C  1 165 ? 56.870  135.984 -18.437 1.00 33.24 ? 138 GLY D C   1 
ATOM   3293  O  O   . GLY C  1 165 ? 57.840  136.372 -19.095 1.00 38.29 ? 138 GLY D O   1 
ATOM   3294  N  N   . ASN C  1 166 ? 55.628  135.936 -18.930 1.00 33.18 ? 139 ASN D N   1 
ATOM   3295  C  CA  . ASN C  1 166 ? 55.285  136.265 -20.317 1.00 41.33 ? 139 ASN D CA  1 
ATOM   3296  C  C   . ASN C  1 166 ? 56.112  135.460 -21.320 1.00 43.98 ? 139 ASN D C   1 
ATOM   3297  O  O   . ASN C  1 166 ? 56.543  135.975 -22.355 1.00 38.99 ? 139 ASN D O   1 
ATOM   3298  C  CB  . ASN C  1 166 ? 55.433  137.767 -20.579 1.00 44.16 ? 139 ASN D CB  1 
ATOM   3299  C  CG  . ASN C  1 166 ? 54.464  138.598 -19.757 1.00 49.83 ? 139 ASN D CG  1 
ATOM   3300  O  OD1 . ASN C  1 166 ? 54.863  139.267 -18.798 1.00 50.82 ? 139 ASN D OD1 1 
ATOM   3301  N  ND2 . ASN C  1 166 ? 53.182  138.556 -20.124 1.00 45.72 ? 139 ASN D ND2 1 
ATOM   3302  N  N   . ALA C  1 167 ? 56.325  134.173 -21.028 1.00 37.73 ? 140 ALA D N   1 
ATOM   3303  C  CA  . ALA C  1 167 ? 57.140  133.357 -21.924 1.00 34.00 ? 140 ALA D CA  1 
ATOM   3304  C  C   . ALA C  1 167 ? 56.354  132.791 -23.106 1.00 35.69 ? 140 ALA D C   1 
ATOM   3305  O  O   . ALA C  1 167 ? 56.967  132.231 -24.024 1.00 36.98 ? 140 ALA D O   1 
ATOM   3306  C  CB  . ALA C  1 167 ? 57.817  132.218 -21.148 1.00 38.42 ? 140 ALA D CB  1 
ATOM   3307  N  N   . GLY C  1 168 ? 55.030  132.920 -23.115 1.00 37.24 ? 141 GLY D N   1 
ATOM   3308  C  CA  . GLY C  1 168 ? 54.258  132.598 -24.302 1.00 46.59 ? 141 GLY D CA  1 
ATOM   3309  C  C   . GLY C  1 168 ? 53.925  131.127 -24.494 1.00 50.51 ? 141 GLY D C   1 
ATOM   3310  O  O   . GLY C  1 168 ? 53.846  130.361 -23.523 1.00 43.52 ? 141 GLY D O   1 
ATOM   3311  N  N   . SER C  1 169 ? 53.730  130.716 -25.750 1.00 35.67 ? 142 SER D N   1 
ATOM   3312  C  CA  . SER C  1 169 ? 53.217  129.380 -26.007 1.00 32.39 ? 142 SER D CA  1 
ATOM   3313  C  C   . SER C  1 169 ? 54.279  128.326 -25.695 1.00 27.87 ? 142 SER D C   1 
ATOM   3314  O  O   . SER C  1 169 ? 55.462  128.619 -25.495 1.00 31.60 ? 142 SER D O   1 
ATOM   3315  C  CB  . SER C  1 169 ? 52.759  129.248 -27.453 1.00 35.75 ? 142 SER D CB  1 
ATOM   3316  O  OG  . SER C  1 169 ? 53.874  129.367 -28.307 1.00 39.67 ? 142 SER D OG  1 
ATOM   3317  N  N   . ARG C  1 170 ? 53.835  127.075 -25.677 1.00 29.65 ? 143 ARG D N   1 
ATOM   3318  C  CA  . ARG C  1 170 ? 54.685  125.944 -25.349 1.00 26.90 ? 143 ARG D CA  1 
ATOM   3319  C  C   . ARG C  1 170 ? 55.142  125.280 -26.644 1.00 21.76 ? 143 ARG D C   1 
ATOM   3320  O  O   . ARG C  1 170 ? 54.327  124.705 -27.373 1.00 31.44 ? 143 ARG D O   1 
ATOM   3321  C  CB  . ARG C  1 170 ? 53.920  124.995 -24.436 1.00 26.20 ? 143 ARG D CB  1 
ATOM   3322  C  CG  . ARG C  1 170 ? 53.269  125.764 -23.254 1.00 27.97 ? 143 ARG D CG  1 
ATOM   3323  C  CD  . ARG C  1 170 ? 52.408  124.922 -22.341 1.00 33.60 ? 143 ARG D CD  1 
ATOM   3324  N  NE  . ARG C  1 170 ? 51.835  125.754 -21.289 1.00 31.83 ? 143 ARG D NE  1 
ATOM   3325  C  CZ  . ARG C  1 170 ? 51.225  125.294 -20.206 1.00 34.97 ? 143 ARG D CZ  1 
ATOM   3326  N  NH1 . ARG C  1 170 ? 51.113  123.993 -19.971 1.00 27.64 ? 143 ARG D NH1 1 
ATOM   3327  N  NH2 . ARG C  1 170 ? 50.717  126.161 -19.331 1.00 31.56 ? 143 ARG D NH2 1 
ATOM   3328  N  N   . LEU C  1 171 ? 56.449  125.343 -26.914 1.00 20.82 ? 144 LEU D N   1 
ATOM   3329  C  CA  . LEU C  1 171 ? 56.965  124.826 -28.184 1.00 22.76 ? 144 LEU D CA  1 
ATOM   3330  C  C   . LEU C  1 171 ? 57.207  123.322 -28.140 1.00 27.24 ? 144 LEU D C   1 
ATOM   3331  O  O   . LEU C  1 171 ? 56.978  122.624 -29.139 1.00 22.20 ? 144 LEU D O   1 
ATOM   3332  C  CB  . LEU C  1 171 ? 58.260  125.536 -28.558 1.00 24.85 ? 144 LEU D CB  1 
ATOM   3333  C  CG  . LEU C  1 171 ? 58.184  127.064 -28.661 1.00 29.03 ? 144 LEU D CG  1 
ATOM   3334  C  CD1 . LEU C  1 171 ? 59.493  127.562 -29.159 1.00 27.78 ? 144 LEU D CD1 1 
ATOM   3335  C  CD2 . LEU C  1 171 ? 57.043  127.504 -29.559 1.00 30.21 ? 144 LEU D CD2 1 
ATOM   3336  N  N   . ALA C  1 172 ? 57.680  122.805 -27.006 1.00 22.22 ? 145 ALA D N   1 
ATOM   3337  C  CA  . ALA C  1 172 ? 57.932  121.372 -26.874 1.00 13.88 ? 145 ALA D CA  1 
ATOM   3338  C  C   . ALA C  1 172 ? 57.908  120.998 -25.400 1.00 23.24 ? 145 ALA D C   1 
ATOM   3339  O  O   . ALA C  1 172 ? 58.150  121.838 -24.526 1.00 22.84 ? 145 ALA D O   1 
ATOM   3340  C  CB  . ALA C  1 172 ? 59.278  120.975 -27.471 1.00 15.96 ? 145 ALA D CB  1 
ATOM   3341  N  N   . CYS C  1 173 ? 57.664  119.720 -25.135 1.00 15.25 ? 146 CYS D N   1 
ATOM   3342  C  CA  . CYS C  1 173 ? 57.608  119.289 -23.740 1.00 22.65 ? 146 CYS D CA  1 
ATOM   3343  C  C   . CYS C  1 173 ? 57.816  117.784 -23.665 1.00 26.23 ? 146 CYS D C   1 
ATOM   3344  O  O   . CYS C  1 173 ? 57.804  117.079 -24.677 1.00 16.27 ? 146 CYS D O   1 
ATOM   3345  C  CB  . CYS C  1 173 ? 56.274  119.682 -23.111 1.00 20.18 ? 146 CYS D CB  1 
ATOM   3346  S  SG  . CYS C  1 173 ? 54.832  119.017 -23.946 1.00 34.31 ? 146 CYS D SG  1 
ATOM   3347  N  N   . GLY C  1 174 ? 58.012  117.299 -22.443 1.00 14.58 ? 147 GLY D N   1 
ATOM   3348  C  CA  . GLY C  1 174 ? 58.062  115.873 -22.206 1.00 18.77 ? 147 GLY D CA  1 
ATOM   3349  C  C   . GLY C  1 174 ? 57.925  115.610 -20.723 1.00 20.94 ? 147 GLY D C   1 
ATOM   3350  O  O   . GLY C  1 174 ? 58.123  116.513 -19.897 1.00 19.44 ? 147 GLY D O   1 
ATOM   3351  N  N   . VAL C  1 175 ? 57.579  114.360 -20.396 1.00 16.44 ? 148 VAL D N   1 
ATOM   3352  C  CA  . VAL C  1 175 ? 57.508  113.952 -18.992 1.00 17.83 ? 148 VAL D CA  1 
ATOM   3353  C  C   . VAL C  1 175 ? 58.905  113.615 -18.505 1.00 18.51 ? 148 VAL D C   1 
ATOM   3354  O  O   . VAL C  1 175 ? 59.660  112.921 -19.189 1.00 17.52 ? 148 VAL D O   1 
ATOM   3355  C  CB  . VAL C  1 175 ? 56.560  112.751 -18.817 1.00 21.80 ? 148 VAL D CB  1 
ATOM   3356  C  CG1 . VAL C  1 175 ? 56.414  112.392 -17.313 1.00 13.42 ? 148 VAL D CG1 1 
ATOM   3357  C  CG2 . VAL C  1 175 ? 55.214  113.056 -19.402 1.00 21.99 ? 148 VAL D CG2 1 
ATOM   3358  N  N   . ILE C  1 176 ? 59.246  114.082 -17.302 1.00 21.30 ? 149 ILE D N   1 
ATOM   3359  C  CA  . ILE C  1 176 ? 60.540  113.796 -16.696 1.00 17.57 ? 149 ILE D CA  1 
ATOM   3360  C  C   . ILE C  1 176 ? 60.480  112.403 -16.077 1.00 19.01 ? 149 ILE D C   1 
ATOM   3361  O  O   . ILE C  1 176 ? 59.652  112.135 -15.201 1.00 22.87 ? 149 ILE D O   1 
ATOM   3362  C  CB  . ILE C  1 176 ? 60.902  114.853 -15.640 1.00 22.46 ? 149 ILE D CB  1 
ATOM   3363  C  CG1 . ILE C  1 176 ? 60.989  116.243 -16.293 1.00 20.84 ? 149 ILE D CG1 1 
ATOM   3364  C  CG2 . ILE C  1 176 ? 62.198  114.478 -14.935 1.00 18.72 ? 149 ILE D CG2 1 
ATOM   3365  C  CD1 . ILE C  1 176 ? 61.001  117.444 -15.265 1.00 21.93 ? 149 ILE D CD1 1 
ATOM   3366  N  N   . GLY C  1 177 ? 61.345  111.520 -16.537 1.00 19.55 ? 150 GLY D N   1 
ATOM   3367  C  CA  . GLY C  1 177 ? 61.277  110.135 -16.134 1.00 21.66 ? 150 GLY D CA  1 
ATOM   3368  C  C   . GLY C  1 177 ? 62.533  109.686 -15.427 1.00 21.81 ? 150 GLY D C   1 
ATOM   3369  O  O   . GLY C  1 177 ? 63.604  110.276 -15.596 1.00 22.19 ? 150 GLY D O   1 
ATOM   3370  N  N   . ILE C  1 178 ? 62.415  108.618 -14.641 1.00 21.00 ? 151 ILE D N   1 
ATOM   3371  C  CA  . ILE C  1 178 ? 63.558  108.076 -13.923 1.00 21.21 ? 151 ILE D CA  1 
ATOM   3372  C  C   . ILE C  1 178 ? 64.534  107.476 -14.926 1.00 24.58 ? 151 ILE D C   1 
ATOM   3373  O  O   . ILE C  1 178 ? 64.135  106.752 -15.849 1.00 23.47 ? 151 ILE D O   1 
ATOM   3374  C  CB  . ILE C  1 178 ? 63.078  107.017 -12.922 1.00 22.70 ? 151 ILE D CB  1 
ATOM   3375  C  CG1 . ILE C  1 178 ? 62.311  107.718 -11.812 1.00 30.92 ? 151 ILE D CG1 1 
ATOM   3376  C  CG2 . ILE C  1 178 ? 64.280  106.372 -12.269 1.00 29.53 ? 151 ILE D CG2 1 
ATOM   3377  C  CD1 . ILE C  1 178 ? 61.452  106.780 -10.991 1.00 32.93 ? 151 ILE D CD1 1 
ATOM   3378  N  N   . ALA C  1 179 ? 65.817  107.784 -14.773 1.00 22.57 ? 152 ALA D N   1 
ATOM   3379  C  CA  . ALA C  1 179 ? 66.817  107.290 -15.704 1.00 23.94 ? 152 ALA D CA  1 
ATOM   3380  C  C   . ALA C  1 179 ? 67.819  106.401 -14.979 1.00 34.08 ? 152 ALA D C   1 
ATOM   3381  O  O   . ALA C  1 179 ? 67.966  106.457 -13.756 1.00 32.03 ? 152 ALA D O   1 
ATOM   3382  C  CB  . ALA C  1 179 ? 67.558  108.432 -16.411 1.00 22.88 ? 152 ALA D CB  1 
ATOM   3383  N  N   . GLN C  1 180 ? 68.504  105.577 -15.757 1.00 32.65 ? 153 GLN D N   1 
ATOM   3384  C  CA  . GLN C  1 180 ? 69.468  104.638 -15.202 1.00 40.31 ? 153 GLN D CA  1 
ATOM   3385  C  C   . GLN C  1 180 ? 70.708  105.364 -14.696 1.00 53.24 ? 153 GLN D C   1 
ATOM   3386  O  O   . GLN C  1 180 ? 71.242  106.224 -15.405 1.00 48.92 ? 153 GLN D O   1 
ATOM   3387  C  CB  . GLN C  1 180 ? 69.875  103.602 -16.246 1.00 35.42 ? 153 GLN D CB  1 
ATOM   3388  C  CG  . GLN C  1 180 ? 70.647  102.438 -15.652 1.00 43.34 ? 153 GLN D CG  1 
ATOM   3389  C  CD  . GLN C  1 180 ? 70.788  101.299 -16.634 1.00 49.76 ? 153 GLN D CD  1 
ATOM   3390  O  OE1 . GLN C  1 180 ? 70.910  101.521 -17.844 1.00 59.58 ? 153 GLN D OE1 1 
ATOM   3391  N  NE2 . GLN C  1 180 ? 70.764  100.071 -16.128 1.00 51.58 ? 153 GLN D NE2 1 
ATOM   3392  O  OXT . GLN C  1 180 ? 71.201  105.100 -13.593 1.00 59.40 ? 153 GLN D OXT 1 
ATOM   3393  N  N   . ALA D  1 28  ? 50.340  111.873 -4.920  1.00 41.67 ? 1   ALA C N   1 
ATOM   3394  C  CA  . ALA D  1 28  ? 49.742  111.589 -6.229  1.00 33.36 ? 1   ALA C CA  1 
ATOM   3395  C  C   . ALA D  1 28  ? 48.613  110.569 -6.140  1.00 27.69 ? 1   ALA C C   1 
ATOM   3396  O  O   . ALA D  1 28  ? 48.819  109.450 -5.696  1.00 37.76 ? 1   ALA C O   1 
ATOM   3397  C  CB  . ALA D  1 28  ? 50.810  111.099 -7.198  1.00 36.02 ? 1   ALA C CB  1 
ATOM   3398  N  N   . THR D  1 29  ? 47.406  110.956 -6.554  1.00 24.79 ? 2   THR C N   1 
ATOM   3399  C  CA  . THR D  1 29  ? 46.308  110.011 -6.640  1.00 25.42 ? 2   THR C CA  1 
ATOM   3400  C  C   . THR D  1 29  ? 45.892  109.700 -8.073  1.00 21.37 ? 2   THR C C   1 
ATOM   3401  O  O   . THR D  1 29  ? 45.064  108.810 -8.268  1.00 21.38 ? 2   THR C O   1 
ATOM   3402  C  CB  . THR D  1 29  ? 45.076  110.536 -5.892  1.00 26.63 ? 2   THR C CB  1 
ATOM   3403  O  OG1 . THR D  1 29  ? 44.734  111.827 -6.405  1.00 37.01 ? 2   THR C OG1 1 
ATOM   3404  C  CG2 . THR D  1 29  ? 45.385  110.658 -4.412  1.00 34.04 ? 2   THR C CG2 1 
ATOM   3405  N  N   . LYS D  1 30  ? 46.389  110.438 -9.052  1.00 21.92 ? 3   LYS C N   1 
ATOM   3406  C  CA  . LYS D  1 30  ? 46.052  110.178 -10.445 1.00 22.58 ? 3   LYS C CA  1 
ATOM   3407  C  C   . LYS D  1 30  ? 47.303  110.261 -11.293 1.00 15.26 ? 3   LYS C C   1 
ATOM   3408  O  O   . LYS D  1 30  ? 48.189  111.083 -11.048 1.00 21.75 ? 3   LYS C O   1 
ATOM   3409  C  CB  . LYS D  1 30  ? 45.012  111.169 -10.980 1.00 23.89 ? 3   LYS C CB  1 
ATOM   3410  C  CG  . LYS D  1 30  ? 43.579  110.777 -10.703 1.00 31.71 ? 3   LYS C CG  1 
ATOM   3411  C  CD  . LYS D  1 30  ? 42.644  111.957 -10.964 1.00 44.12 ? 3   LYS C CD  1 
ATOM   3412  C  CE  . LYS D  1 30  ? 41.509  111.997 -9.953  1.00 52.63 ? 3   LYS C CE  1 
ATOM   3413  N  NZ  . LYS D  1 30  ? 41.139  113.388 -9.554  1.00 53.86 ? 3   LYS C NZ  1 
ATOM   3414  N  N   . ALA D  1 31  ? 47.350  109.430 -12.334 1.00 22.12 ? 4   ALA C N   1 
ATOM   3415  C  CA  . ALA D  1 31  ? 48.461  109.464 -13.265 1.00 21.94 ? 4   ALA C CA  1 
ATOM   3416  C  C   . ALA D  1 31  ? 47.918  109.195 -14.658 1.00 13.43 ? 4   ALA C C   1 
ATOM   3417  O  O   . ALA D  1 31  ? 46.793  108.719 -14.827 1.00 15.63 ? 4   ALA C O   1 
ATOM   3418  C  CB  . ALA D  1 31  ? 49.548  108.446 -12.897 1.00 16.40 ? 4   ALA C CB  1 
ATOM   3419  N  N   . VAL D  1 32  ? 48.743  109.488 -15.662 1.00 16.31 ? 5   VAL C N   1 
ATOM   3420  C  CA  . VAL D  1 32  ? 48.331  109.287 -17.045 1.00 15.29 ? 5   VAL C CA  1 
ATOM   3421  C  C   . VAL D  1 32  ? 49.544  108.933 -17.888 1.00 17.42 ? 5   VAL C C   1 
ATOM   3422  O  O   . VAL D  1 32  ? 50.684  109.284 -17.573 1.00 16.97 ? 5   VAL C O   1 
ATOM   3423  C  CB  . VAL D  1 32  ? 47.578  110.531 -17.578 1.00 17.96 ? 5   VAL C CB  1 
ATOM   3424  C  CG1 . VAL D  1 32  ? 48.509  111.733 -17.654 1.00 21.91 ? 5   VAL C CG1 1 
ATOM   3425  C  CG2 . VAL D  1 32  ? 46.856  110.230 -18.909 1.00 26.00 ? 5   VAL C CG2 1 
ATOM   3426  N  N   . CYS D  1 33  ? 49.288  108.224 -18.983 1.00 21.01 ? 6   CYS C N   1 
ATOM   3427  C  CA  . CYS D  1 33  ? 50.352  107.806 -19.869 1.00 13.80 ? 6   CYS C CA  1 
ATOM   3428  C  C   . CYS D  1 33  ? 49.848  107.890 -21.296 1.00 19.84 ? 6   CYS C C   1 
ATOM   3429  O  O   . CYS D  1 33  ? 48.786  107.347 -21.598 1.00 14.55 ? 6   CYS C O   1 
ATOM   3430  C  CB  . CYS D  1 33  ? 50.790  106.373 -19.560 1.00 13.42 ? 6   CYS C CB  1 
ATOM   3431  S  SG  . CYS D  1 33  ? 52.190  105.856 -20.551 1.00 23.17 ? 6   CYS C SG  1 
ATOM   3432  N  N   . VAL D  1 34  ? 50.609  108.540 -22.165 1.00 14.63 ? 7   VAL C N   1 
ATOM   3433  C  CA  . VAL D  1 34  ? 50.283  108.585 -23.591 1.00 17.33 ? 7   VAL C CA  1 
ATOM   3434  C  C   . VAL D  1 34  ? 51.203  107.596 -24.295 1.00 15.01 ? 7   VAL C C   1 
ATOM   3435  O  O   . VAL D  1 34  ? 52.422  107.772 -24.305 1.00 19.24 ? 7   VAL C O   1 
ATOM   3436  C  CB  . VAL D  1 34  ? 50.421  109.996 -24.165 1.00 18.37 ? 7   VAL C CB  1 
ATOM   3437  C  CG1 . VAL D  1 34  ? 50.075  109.966 -25.681 1.00 23.27 ? 7   VAL C CG1 1 
ATOM   3438  C  CG2 . VAL D  1 34  ? 49.479  110.948 -23.405 1.00 21.57 ? 7   VAL C CG2 1 
ATOM   3439  N  N   . LEU D  1 35  ? 50.622  106.536 -24.845 1.00 18.09 ? 8   LEU C N   1 
ATOM   3440  C  CA  . LEU D  1 35  ? 51.378  105.468 -25.492 1.00 16.15 ? 8   LEU C CA  1 
ATOM   3441  C  C   . LEU D  1 35  ? 51.560  105.808 -26.969 1.00 19.05 ? 8   LEU C C   1 
ATOM   3442  O  O   . LEU D  1 35  ? 50.579  106.015 -27.691 1.00 17.46 ? 8   LEU C O   1 
ATOM   3443  C  CB  . LEU D  1 35  ? 50.657  104.128 -25.362 1.00 16.14 ? 8   LEU C CB  1 
ATOM   3444  C  CG  . LEU D  1 35  ? 50.519  103.510 -23.959 1.00 22.15 ? 8   LEU C CG  1 
ATOM   3445  C  CD1 . LEU D  1 35  ? 49.594  102.303 -24.044 1.00 24.97 ? 8   LEU C CD1 1 
ATOM   3446  C  CD2 . LEU D  1 35  ? 51.862  103.080 -23.433 1.00 26.06 ? 8   LEU C CD2 1 
ATOM   3447  N  N   . LYS D  1 36  ? 52.800  105.823 -27.422 1.00 16.57 ? 9   LYS C N   1 
ATOM   3448  C  CA  . LYS D  1 36  ? 53.081  106.107 -28.820 1.00 21.16 ? 9   LYS C CA  1 
ATOM   3449  C  C   . LYS D  1 36  ? 54.142  105.146 -29.305 1.00 20.52 ? 9   LYS C C   1 
ATOM   3450  O  O   . LYS D  1 36  ? 54.979  104.681 -28.540 1.00 15.36 ? 9   LYS C O   1 
ATOM   3451  C  CB  . LYS D  1 36  ? 53.580  107.540 -29.009 1.00 25.77 ? 9   LYS C CB  1 
ATOM   3452  C  CG  . LYS D  1 36  ? 52.470  108.561 -28.857 1.00 41.13 ? 9   LYS C CG  1 
ATOM   3453  C  CD  . LYS D  1 36  ? 53.000  109.988 -28.863 1.00 46.65 ? 9   LYS C CD  1 
ATOM   3454  C  CE  . LYS D  1 36  ? 51.841  110.985 -28.878 1.00 53.49 ? 9   LYS C CE  1 
ATOM   3455  N  NZ  . LYS D  1 36  ? 50.626  110.401 -29.540 1.00 54.30 ? 9   LYS C NZ  1 
ATOM   3456  N  N   . GLY D  1 37  ? 54.148  104.896 -30.610 1.00 20.69 ? 10  GLY C N   1 
ATOM   3457  C  CA  . GLY D  1 37  ? 55.204  104.077 -31.157 1.00 23.35 ? 10  GLY C CA  1 
ATOM   3458  C  C   . GLY D  1 37  ? 55.418  104.425 -32.619 1.00 26.40 ? 10  GLY C C   1 
ATOM   3459  O  O   . GLY D  1 37  ? 54.850  105.388 -33.135 1.00 23.93 ? 10  GLY C O   1 
ATOM   3460  N  N   . ASP D  1 38  ? 56.238  103.625 -33.283 1.00 29.38 ? 11  ASP C N   1 
ATOM   3461  C  CA  . ASP D  1 38  ? 56.525  103.873 -34.690 1.00 31.28 ? 11  ASP C CA  1 
ATOM   3462  C  C   . ASP D  1 38  ? 55.538  103.206 -35.634 1.00 34.23 ? 11  ASP C C   1 
ATOM   3463  O  O   . ASP D  1 38  ? 55.632  103.424 -36.841 1.00 34.80 ? 11  ASP C O   1 
ATOM   3464  C  CB  . ASP D  1 38  ? 57.956  103.435 -35.018 1.00 35.56 ? 11  ASP C CB  1 
ATOM   3465  C  CG  . ASP D  1 38  ? 58.995  104.286 -34.304 1.00 45.58 ? 11  ASP C CG  1 
ATOM   3466  O  OD1 . ASP D  1 38  ? 58.834  105.530 -34.276 1.00 49.13 ? 11  ASP C OD1 1 
ATOM   3467  O  OD2 . ASP D  1 38  ? 59.970  103.716 -33.781 1.00 55.83 ? 11  ASP C OD2 1 
ATOM   3468  N  N   . GLY D  1 39  ? 54.586  102.432 -35.127 1.00 27.45 ? 12  GLY C N   1 
ATOM   3469  C  CA  . GLY D  1 39  ? 53.562  101.846 -35.957 1.00 24.17 ? 12  GLY C CA  1 
ATOM   3470  C  C   . GLY D  1 39  ? 52.189  102.426 -35.680 1.00 22.29 ? 12  GLY C C   1 
ATOM   3471  O  O   . GLY D  1 39  ? 52.044  103.586 -35.289 1.00 22.69 ? 12  GLY C O   1 
ATOM   3472  N  N   . PRO D  1 40  ? 51.141  101.630 -35.889 1.00 15.54 ? 13  PRO C N   1 
ATOM   3473  C  CA  . PRO D  1 40  ? 49.783  102.147 -35.713 1.00 20.48 ? 13  PRO C CA  1 
ATOM   3474  C  C   . PRO D  1 40  ? 49.302  102.143 -34.273 1.00 19.03 ? 13  PRO C C   1 
ATOM   3475  O  O   . PRO D  1 40  ? 48.168  102.561 -34.022 1.00 19.52 ? 13  PRO C O   1 
ATOM   3476  C  CB  . PRO D  1 40  ? 48.951  101.184 -36.559 1.00 23.73 ? 13  PRO C CB  1 
ATOM   3477  C  CG  . PRO D  1 40  ? 49.662  99.883  -36.397 1.00 21.49 ? 13  PRO C CG  1 
ATOM   3478  C  CD  . PRO D  1 40  ? 51.145  100.211 -36.285 1.00 24.83 ? 13  PRO C CD  1 
ATOM   3479  N  N   . VAL D  1 41  ? 50.101  101.669 -33.330 1.00 17.59 ? 14  VAL C N   1 
ATOM   3480  C  CA  . VAL D  1 41  ? 49.615  101.494 -31.957 1.00 16.64 ? 14  VAL C CA  1 
ATOM   3481  C  C   . VAL D  1 41  ? 49.743  102.808 -31.195 1.00 15.06 ? 14  VAL C C   1 
ATOM   3482  O  O   . VAL D  1 41  ? 50.825  103.397 -31.133 1.00 18.52 ? 14  VAL C O   1 
ATOM   3483  C  CB  . VAL D  1 41  ? 50.371  100.369 -31.234 1.00 13.42 ? 14  VAL C CB  1 
ATOM   3484  C  CG1 . VAL D  1 41  ? 49.877  100.272 -29.758 1.00 16.38 ? 14  VAL C CG1 1 
ATOM   3485  C  CG2 . VAL D  1 41  ? 50.123  99.030  -31.928 1.00 17.65 ? 14  VAL C CG2 1 
ATOM   3486  N  N   . GLN D  1 42  ? 48.646  103.248 -30.583 1.00 20.34 ? 15  GLN C N   1 
ATOM   3487  C  CA  . GLN D  1 42  ? 48.685  104.431 -29.733 1.00 22.15 ? 15  GLN C CA  1 
ATOM   3488  C  C   . GLN D  1 42  ? 47.499  104.398 -28.787 1.00 19.26 ? 15  GLN C C   1 
ATOM   3489  O  O   . GLN D  1 42  ? 46.466  103.784 -29.069 1.00 19.10 ? 15  GLN C O   1 
ATOM   3490  C  CB  . GLN D  1 42  ? 48.677  105.731 -30.540 1.00 27.42 ? 15  GLN C CB  1 
ATOM   3491  C  CG  . GLN D  1 42  ? 47.368  105.992 -31.242 1.00 31.02 ? 15  GLN C CG  1 
ATOM   3492  C  CD  . GLN D  1 42  ? 47.457  107.120 -32.255 1.00 44.86 ? 15  GLN C CD  1 
ATOM   3493  O  OE1 . GLN D  1 42  ? 48.231  107.058 -33.201 1.00 51.14 ? 15  GLN C OE1 1 
ATOM   3494  N  NE2 . GLN D  1 42  ? 46.650  108.159 -32.059 1.00 49.58 ? 15  GLN C NE2 1 
ATOM   3495  N  N   . GLY D  1 43  ? 47.664  105.057 -27.648 1.00 21.29 ? 16  GLY C N   1 
ATOM   3496  C  CA  . GLY D  1 43  ? 46.578  105.019 -26.693 1.00 18.37 ? 16  GLY C CA  1 
ATOM   3497  C  C   . GLY D  1 43  ? 46.833  105.973 -25.547 1.00 16.41 ? 16  GLY C C   1 
ATOM   3498  O  O   . GLY D  1 43  ? 47.868  106.639 -25.477 1.00 16.34 ? 16  GLY C O   1 
ATOM   3499  N  N   . ILE D  1 44  ? 45.840  106.057 -24.671 1.00 15.75 ? 17  ILE C N   1 
ATOM   3500  C  CA  . ILE D  1 44  ? 45.957  106.819 -23.431 1.00 20.30 ? 17  ILE C CA  1 
ATOM   3501  C  C   . ILE D  1 44  ? 45.520  105.925 -22.288 1.00 18.28 ? 17  ILE C C   1 
ATOM   3502  O  O   . ILE D  1 44  ? 44.473  105.279 -22.367 1.00 20.28 ? 17  ILE C O   1 
ATOM   3503  C  CB  . ILE D  1 44  ? 45.131  108.120 -23.470 1.00 18.40 ? 17  ILE C CB  1 
ATOM   3504  C  CG1 . ILE D  1 44  ? 45.760  109.076 -24.486 1.00 25.01 ? 17  ILE C CG1 1 
ATOM   3505  C  CG2 . ILE D  1 44  ? 45.089  108.775 -22.064 1.00 22.16 ? 17  ILE C CG2 1 
ATOM   3506  C  CD1 . ILE D  1 44  ? 44.930  110.327 -24.759 1.00 30.14 ? 17  ILE C CD1 1 
ATOM   3507  N  N   . ILE D  1 45  ? 46.326  105.874 -21.228 1.00 18.12 ? 18  ILE C N   1 
ATOM   3508  C  CA  . ILE D  1 45  ? 46.033  105.003 -20.101 1.00 17.39 ? 18  ILE C CA  1 
ATOM   3509  C  C   . ILE D  1 45  ? 46.035  105.865 -18.851 1.00 18.12 ? 18  ILE C C   1 
ATOM   3510  O  O   . ILE D  1 45  ? 46.975  106.634 -18.631 1.00 16.91 ? 18  ILE C O   1 
ATOM   3511  C  CB  . ILE D  1 45  ? 47.052  103.852 -19.964 1.00 16.49 ? 18  ILE C CB  1 
ATOM   3512  C  CG1 . ILE D  1 45  ? 46.994  102.889 -21.168 1.00 13.42 ? 18  ILE C CG1 1 
ATOM   3513  C  CG2 . ILE D  1 45  ? 46.801  103.089 -18.677 1.00 13.42 ? 18  ILE C CG2 1 
ATOM   3514  C  CD1 . ILE D  1 45  ? 45.678  102.101 -21.272 1.00 18.51 ? 18  ILE C CD1 1 
ATOM   3515  N  N   . ASN D  1 46  ? 44.971  105.750 -18.061 1.00 21.14 ? 19  ASN C N   1 
ATOM   3516  C  CA  . ASN D  1 46  ? 44.794  106.493 -16.816 1.00 21.03 ? 19  ASN C CA  1 
ATOM   3517  C  C   . ASN D  1 46  ? 45.088  105.592 -15.626 1.00 17.61 ? 19  ASN C C   1 
ATOM   3518  O  O   . ASN D  1 46  ? 44.893  104.375 -15.690 1.00 16.50 ? 19  ASN C O   1 
ATOM   3519  C  CB  . ASN D  1 46  ? 43.367  107.036 -16.708 1.00 18.86 ? 19  ASN C CB  1 
ATOM   3520  C  CG  . ASN D  1 46  ? 42.964  107.847 -17.924 1.00 23.96 ? 19  ASN C CG  1 
ATOM   3521  O  OD1 . ASN D  1 46  ? 42.217  107.380 -18.787 1.00 26.36 ? 19  ASN C OD1 1 
ATOM   3522  N  ND2 . ASN D  1 46  ? 43.491  109.053 -18.013 1.00 21.70 ? 19  ASN C ND2 1 
ATOM   3523  N  N   . PHE D  1 47  ? 45.548  106.207 -14.526 1.00 19.60 ? 20  PHE C N   1 
ATOM   3524  C  CA  . PHE D  1 47  ? 45.758  105.497 -13.275 1.00 16.40 ? 20  PHE C CA  1 
ATOM   3525  C  C   . PHE D  1 47  ? 45.095  106.287 -12.162 1.00 21.55 ? 20  PHE C C   1 
ATOM   3526  O  O   . PHE D  1 47  ? 45.135  107.518 -12.167 1.00 18.21 ? 20  PHE C O   1 
ATOM   3527  C  CB  . PHE D  1 47  ? 47.243  105.340 -12.931 1.00 17.76 ? 20  PHE C CB  1 
ATOM   3528  C  CG  . PHE D  1 47  ? 48.056  104.634 -13.982 1.00 18.28 ? 20  PHE C CG  1 
ATOM   3529  C  CD1 . PHE D  1 47  ? 48.505  105.327 -15.108 1.00 19.97 ? 20  PHE C CD1 1 
ATOM   3530  C  CD2 . PHE D  1 47  ? 48.397  103.293 -13.831 1.00 18.40 ? 20  PHE C CD2 1 
ATOM   3531  C  CE1 . PHE D  1 47  ? 49.285  104.689 -16.071 1.00 20.98 ? 20  PHE C CE1 1 
ATOM   3532  C  CE2 . PHE D  1 47  ? 49.165  102.637 -14.792 1.00 19.03 ? 20  PHE C CE2 1 
ATOM   3533  C  CZ  . PHE D  1 47  ? 49.608  103.339 -15.910 1.00 16.82 ? 20  PHE C CZ  1 
ATOM   3534  N  N   . GLU D  1 48  ? 44.487  105.584 -11.215 1.00 17.50 ? 21  GLU C N   1 
ATOM   3535  C  CA  . GLU D  1 48  ? 43.856  106.257 -10.086 1.00 21.36 ? 21  GLU C CA  1 
ATOM   3536  C  C   . GLU D  1 48  ? 44.052  105.423 -8.839  1.00 19.76 ? 21  GLU C C   1 
ATOM   3537  O  O   . GLU D  1 48  ? 43.752  104.229 -8.846  1.00 22.20 ? 21  GLU C O   1 
ATOM   3538  C  CB  . GLU D  1 48  ? 42.356  106.492 -10.320 1.00 20.70 ? 21  GLU C CB  1 
ATOM   3539  C  CG  . GLU D  1 48  ? 41.700  107.216 -9.125  1.00 28.29 ? 21  GLU C CG  1 
ATOM   3540  C  CD  . GLU D  1 48  ? 40.448  107.996 -9.513  1.00 51.55 ? 21  GLU C CD  1 
ATOM   3541  O  OE1 . GLU D  1 48  ? 40.461  109.236 -9.396  1.00 57.50 ? 21  GLU C OE1 1 
ATOM   3542  O  OE2 . GLU D  1 48  ? 39.456  107.371 -9.943  1.00 49.80 ? 21  GLU C OE2 1 
ATOM   3543  N  N   . GLN D  1 49  ? 44.515  106.061 -7.762  1.00 20.29 ? 22  GLN C N   1 
ATOM   3544  C  CA  . GLN D  1 49  ? 44.681  105.399 -6.469  1.00 18.44 ? 22  GLN C CA  1 
ATOM   3545  C  C   . GLN D  1 49  ? 44.107  106.335 -5.407  1.00 20.86 ? 22  GLN C C   1 
ATOM   3546  O  O   . GLN D  1 49  ? 44.785  107.270 -4.975  1.00 23.12 ? 22  GLN C O   1 
ATOM   3547  C  CB  . GLN D  1 49  ? 46.147  105.092 -6.208  1.00 21.95 ? 22  GLN C CB  1 
ATOM   3548  C  CG  . GLN D  1 49  ? 46.390  104.113 -5.093  1.00 24.52 ? 22  GLN C CG  1 
ATOM   3549  C  CD  . GLN D  1 49  ? 47.856  103.925 -4.837  1.00 21.65 ? 22  GLN C CD  1 
ATOM   3550  O  OE1 . GLN D  1 49  ? 48.671  104.788 -5.181  1.00 22.80 ? 22  GLN C OE1 1 
ATOM   3551  N  NE2 . GLN D  1 49  ? 48.217  102.778 -4.277  1.00 24.70 ? 22  GLN C NE2 1 
ATOM   3552  N  N   . LYS D  1 50  ? 42.857  106.096 -5.021  1.00 25.35 ? 23  LYS C N   1 
ATOM   3553  C  CA  . LYS D  1 50  ? 42.218  106.958 -4.031  1.00 37.85 ? 23  LYS C CA  1 
ATOM   3554  C  C   . LYS D  1 50  ? 42.927  106.880 -2.682  1.00 31.29 ? 23  LYS C C   1 
ATOM   3555  O  O   . LYS D  1 50  ? 43.113  107.900 -2.009  1.00 35.85 ? 23  LYS C O   1 
ATOM   3556  C  CB  . LYS D  1 50  ? 40.742  106.589 -3.899  1.00 39.86 ? 23  LYS C CB  1 
ATOM   3557  C  CG  . LYS D  1 50  ? 40.046  106.355 -5.234  1.00 46.09 ? 23  LYS C CG  1 
ATOM   3558  C  CD  . LYS D  1 50  ? 38.989  107.431 -5.483  1.00 48.79 ? 23  LYS C CD  1 
ATOM   3559  C  CE  . LYS D  1 50  ? 37.750  106.865 -6.175  1.00 50.39 ? 23  LYS C CE  1 
ATOM   3560  N  NZ  . LYS D  1 50  ? 37.936  106.628 -7.636  1.00 60.21 ? 23  LYS C NZ  1 
ATOM   3561  N  N   . GLU D  1 51  ? 43.367  105.692 -2.286  1.00 30.48 ? 24  GLU C N   1 
ATOM   3562  C  CA  . GLU D  1 51  ? 44.064  105.513 -1.018  1.00 33.27 ? 24  GLU C CA  1 
ATOM   3563  C  C   . GLU D  1 51  ? 45.453  104.950 -1.250  1.00 29.64 ? 24  GLU C C   1 
ATOM   3564  O  O   . GLU D  1 51  ? 45.629  104.015 -2.037  1.00 30.35 ? 24  GLU C O   1 
ATOM   3565  C  CB  . GLU D  1 51  ? 43.276  104.584 -0.096  1.00 36.25 ? 24  GLU C CB  1 
ATOM   3566  C  CG  . GLU D  1 51  ? 41.802  104.930 -0.025  1.00 46.17 ? 24  GLU C CG  1 
ATOM   3567  C  CD  . GLU D  1 51  ? 41.516  106.106 0.904   1.00 62.43 ? 24  GLU C CD  1 
ATOM   3568  O  OE1 . GLU D  1 51  ? 42.482  106.748 1.386   1.00 62.51 ? 24  GLU C OE1 1 
ATOM   3569  O  OE2 . GLU D  1 51  ? 40.319  106.398 1.141   1.00 70.09 ? 24  GLU C OE2 1 
ATOM   3570  N  N   . SER D  1 52  ? 46.436  105.481 -0.518  1.00 32.91 ? 25  SER C N   1 
ATOM   3571  C  CA  . SER D  1 52  ? 47.803  105.032 -0.742  1.00 34.92 ? 25  SER C CA  1 
ATOM   3572  C  C   . SER D  1 52  ? 48.031  103.587 -0.314  1.00 35.36 ? 25  SER C C   1 
ATOM   3573  O  O   . SER D  1 52  ? 49.030  102.994 -0.727  1.00 38.80 ? 25  SER C O   1 
ATOM   3574  C  CB  . SER D  1 52  ? 48.791  105.961 -0.036  1.00 40.13 ? 25  SER C CB  1 
ATOM   3575  O  OG  . SER D  1 52  ? 48.759  105.770 1.365   1.00 40.19 ? 25  SER C OG  1 
ATOM   3576  N  N   . ASN D  1 53  ? 47.122  102.997 0.467   1.00 33.74 ? 26  ASN C N   1 
ATOM   3577  C  CA  . ASN D  1 53  ? 47.192  101.587 0.838   1.00 39.42 ? 26  ASN C CA  1 
ATOM   3578  C  C   . ASN D  1 53  ? 46.242  100.716 0.018   1.00 42.11 ? 26  ASN C C   1 
ATOM   3579  O  O   . ASN D  1 53  ? 45.989  99.563  0.390   1.00 38.04 ? 26  ASN C O   1 
ATOM   3580  C  CB  . ASN D  1 53  ? 46.891  101.415 2.333   1.00 39.75 ? 26  ASN C CB  1 
ATOM   3581  C  CG  . ASN D  1 53  ? 45.426  101.685 2.674   1.00 41.79 ? 26  ASN C CG  1 
ATOM   3582  O  OD1 . ASN D  1 53  ? 44.720  102.367 1.933   1.00 43.57 ? 26  ASN C OD1 1 
ATOM   3583  N  ND2 . ASN D  1 53  ? 44.970  101.160 3.810   1.00 37.19 ? 26  ASN C ND2 1 
ATOM   3584  N  N   . GLY D  1 54  ? 45.701  101.241 -1.077  1.00 29.75 ? 27  GLY C N   1 
ATOM   3585  C  CA  . GLY D  1 54  ? 44.692  100.536 -1.820  1.00 28.47 ? 27  GLY C CA  1 
ATOM   3586  C  C   . GLY D  1 54  ? 45.124  100.303 -3.256  1.00 21.98 ? 27  GLY C C   1 
ATOM   3587  O  O   . GLY D  1 54  ? 46.208  100.711 -3.689  1.00 25.54 ? 27  GLY C O   1 
ATOM   3588  N  N   . PRO D  1 55  ? 44.246  99.655  -4.012  1.00 23.65 ? 28  PRO C N   1 
ATOM   3589  C  CA  . PRO D  1 55  ? 44.560  99.279  -5.389  1.00 26.43 ? 28  PRO C CA  1 
ATOM   3590  C  C   . PRO D  1 55  ? 44.657  100.496 -6.283  1.00 27.41 ? 28  PRO C C   1 
ATOM   3591  O  O   . PRO D  1 55  ? 44.104  101.561 -5.996  1.00 21.88 ? 28  PRO C O   1 
ATOM   3592  C  CB  . PRO D  1 55  ? 43.362  98.409  -5.796  1.00 28.34 ? 28  PRO C CB  1 
ATOM   3593  C  CG  . PRO D  1 55  ? 42.676  98.041  -4.529  1.00 32.64 ? 28  PRO C CG  1 
ATOM   3594  C  CD  . PRO D  1 55  ? 42.913  99.187  -3.603  1.00 29.33 ? 28  PRO C CD  1 
ATOM   3595  N  N   . VAL D  1 56  ? 45.354  100.312 -7.405  1.00 24.16 ? 29  VAL C N   1 
ATOM   3596  C  CA  . VAL D  1 56  ? 45.415  101.302 -8.472  1.00 18.13 ? 29  VAL C CA  1 
ATOM   3597  C  C   . VAL D  1 56  ? 44.488  100.814 -9.575  1.00 24.17 ? 29  VAL C C   1 
ATOM   3598  O  O   . VAL D  1 56  ? 44.576  99.654  -9.998  1.00 19.67 ? 29  VAL C O   1 
ATOM   3599  C  CB  . VAL D  1 56  ? 46.851  101.475 -8.998  1.00 20.32 ? 29  VAL C CB  1 
ATOM   3600  C  CG1 . VAL D  1 56  ? 46.912  102.532 -10.146 1.00 18.62 ? 29  VAL C CG1 1 
ATOM   3601  C  CG2 . VAL D  1 56  ? 47.786  101.845 -7.853  1.00 18.68 ? 29  VAL C CG2 1 
ATOM   3602  N  N   . LYS D  1 57  ? 43.570  101.673 -10.003 1.00 21.56 ? 30  LYS C N   1 
ATOM   3603  C  CA  . LYS D  1 57  ? 42.726  101.377 -11.148 1.00 21.01 ? 30  LYS C CA  1 
ATOM   3604  C  C   . LYS D  1 57  ? 43.450  101.855 -12.397 1.00 18.02 ? 30  LYS C C   1 
ATOM   3605  O  O   . LYS D  1 57  ? 43.996  102.959 -12.415 1.00 22.52 ? 30  LYS C O   1 
ATOM   3606  C  CB  . LYS D  1 57  ? 41.366  102.074 -11.042 1.00 26.55 ? 30  LYS C CB  1 
ATOM   3607  C  CG  . LYS D  1 57  ? 40.287  101.324 -10.247 1.00 39.10 ? 30  LYS C CG  1 
ATOM   3608  C  CD  . LYS D  1 57  ? 39.419  102.290 -9.426  1.00 53.53 ? 30  LYS C CD  1 
ATOM   3609  C  CE  . LYS D  1 57  ? 38.348  101.556 -8.608  1.00 46.55 ? 30  LYS C CE  1 
ATOM   3610  N  NZ  . LYS D  1 57  ? 38.848  101.017 -7.314  1.00 53.37 ? 30  LYS C NZ  1 
ATOM   3611  N  N   . VAL D  1 58  ? 43.451  101.022 -13.439 1.00 19.26 ? 31  VAL C N   1 
ATOM   3612  C  CA  . VAL D  1 58  ? 44.168  101.305 -14.682 1.00 16.89 ? 31  VAL C CA  1 
ATOM   3613  C  C   . VAL D  1 58  ? 43.162  101.161 -15.812 1.00 15.22 ? 31  VAL C C   1 
ATOM   3614  O  O   . VAL D  1 58  ? 42.560  100.095 -15.962 1.00 21.63 ? 31  VAL C O   1 
ATOM   3615  C  CB  . VAL D  1 58  ? 45.351  100.340 -14.900 1.00 17.62 ? 31  VAL C CB  1 
ATOM   3616  C  CG1 . VAL D  1 58  ? 46.203  100.811 -16.090 1.00 13.59 ? 31  VAL C CG1 1 
ATOM   3617  C  CG2 . VAL D  1 58  ? 46.222  100.279 -13.656 1.00 14.86 ? 31  VAL C CG2 1 
ATOM   3618  N  N   . TRP D  1 59  ? 42.952  102.223 -16.585 1.00 20.05 ? 32  TRP C N   1 
ATOM   3619  C  CA  . TRP D  1 59  ? 41.952  102.110 -17.638 1.00 16.15 ? 32  TRP C CA  1 
ATOM   3620  C  C   . TRP D  1 59  ? 42.237  103.096 -18.761 1.00 19.05 ? 32  TRP C C   1 
ATOM   3621  O  O   . TRP D  1 59  ? 42.901  104.117 -18.580 1.00 20.72 ? 32  TRP C O   1 
ATOM   3622  C  CB  . TRP D  1 59  ? 40.529  102.320 -17.083 1.00 21.69 ? 32  TRP C CB  1 
ATOM   3623  C  CG  . TRP D  1 59  ? 40.218  103.770 -16.867 1.00 21.39 ? 32  TRP C CG  1 
ATOM   3624  C  CD1 . TRP D  1 59  ? 39.512  104.593 -17.703 1.00 30.50 ? 32  TRP C CD1 1 
ATOM   3625  C  CD2 . TRP D  1 59  ? 40.614  104.572 -15.756 1.00 27.09 ? 32  TRP C CD2 1 
ATOM   3626  N  NE1 . TRP D  1 59  ? 39.462  105.861 -17.184 1.00 26.10 ? 32  TRP C NE1 1 
ATOM   3627  C  CE2 . TRP D  1 59  ? 40.110  105.871 -15.978 1.00 28.58 ? 32  TRP C CE2 1 
ATOM   3628  C  CE3 . TRP D  1 59  ? 41.340  104.320 -14.590 1.00 29.59 ? 32  TRP C CE3 1 
ATOM   3629  C  CZ2 . TRP D  1 59  ? 40.312  106.915 -15.079 1.00 30.00 ? 32  TRP C CZ2 1 
ATOM   3630  C  CZ3 . TRP D  1 59  ? 41.544  105.372 -13.694 1.00 34.41 ? 32  TRP C CZ3 1 
ATOM   3631  C  CH2 . TRP D  1 59  ? 41.032  106.648 -13.950 1.00 32.53 ? 32  TRP C CH2 1 
ATOM   3632  N  N   . GLY D  1 60  ? 41.696  102.784 -19.923 1.00 21.35 ? 33  GLY C N   1 
ATOM   3633  C  CA  . GLY D  1 60  ? 41.887  103.634 -21.077 1.00 20.39 ? 33  GLY C CA  1 
ATOM   3634  C  C   . GLY D  1 60  ? 41.695  102.807 -22.329 1.00 21.47 ? 33  GLY C C   1 
ATOM   3635  O  O   . GLY D  1 60  ? 41.171  101.702 -22.291 1.00 23.24 ? 33  GLY C O   1 
ATOM   3636  N  N   A SER D  1 61  ? 42.142  103.373 -23.439 0.53 23.43 ? 34  SER C N   1 
ATOM   3637  N  N   B SER D  1 61  ? 42.143  103.371 -23.443 0.47 23.42 ? 34  SER C N   1 
ATOM   3638  C  CA  A SER D  1 61  ? 41.960  102.738 -24.733 0.53 22.22 ? 34  SER C CA  1 
ATOM   3639  C  CA  B SER D  1 61  ? 41.950  102.751 -24.744 0.47 22.42 ? 34  SER C CA  1 
ATOM   3640  C  C   A SER D  1 61  ? 43.270  102.756 -25.499 0.53 20.67 ? 34  SER C C   1 
ATOM   3641  C  C   B SER D  1 61  ? 43.256  102.767 -25.519 0.47 20.66 ? 34  SER C C   1 
ATOM   3642  O  O   A SER D  1 61  ? 43.998  103.750 -25.465 0.53 22.92 ? 34  SER C O   1 
ATOM   3643  O  O   B SER D  1 61  ? 43.968  103.772 -25.512 0.47 22.96 ? 34  SER C O   1 
ATOM   3644  C  CB  A SER D  1 61  ? 40.874  103.447 -25.543 0.53 25.31 ? 34  SER C CB  1 
ATOM   3645  C  CB  B SER D  1 61  ? 40.860  103.481 -25.542 0.47 25.62 ? 34  SER C CB  1 
ATOM   3646  O  OG  A SER D  1 61  ? 40.596  102.717 -26.721 0.53 24.33 ? 34  SER C OG  1 
ATOM   3647  O  OG  B SER D  1 61  ? 39.581  103.262 -24.974 0.47 29.78 ? 34  SER C OG  1 
ATOM   3648  N  N   . ILE D  1 62  ? 43.609  101.787 -26.131 1.00 19.84 ? 35  ILE C N   1 
ATOM   3649  C  CA  . ILE D  1 62  ? 44.722  101.542 -27.097 1.00 13.42 ? 35  ILE C CA  1 
ATOM   3650  C  C   . ILE D  1 62  ? 44.194  101.005 -28.435 1.00 19.07 ? 35  ILE C C   1 
ATOM   3651  O  O   . ILE D  1 62  ? 43.519  100.006 -28.437 1.00 22.10 ? 35  ILE C O   1 
ATOM   3652  C  CB  . ILE D  1 62  ? 45.799  100.604 -26.531 1.00 20.29 ? 35  ILE C CB  1 
ATOM   3653  C  CG1 . ILE D  1 62  ? 46.150  100.905 -25.078 1.00 20.13 ? 35  ILE C CG1 1 
ATOM   3654  C  CG2 . ILE D  1 62  ? 47.024  100.614 -27.418 1.00 15.88 ? 35  ILE C CG2 1 
ATOM   3655  C  CD1 . ILE D  1 62  ? 46.961  99.835  -24.431 1.00 20.82 ? 35  ILE C CD1 1 
ATOM   3656  N  N   . LYS D  1 63  ? 44.587  101.641 -29.526 1.00 20.61 ? 36  LYS C N   1 
ATOM   3657  C  CA  . LYS D  1 63  ? 44.142  101.241 -30.877 1.00 19.05 ? 36  LYS C CA  1 
ATOM   3658  C  C   . LYS D  1 63  ? 45.342  100.752 -31.684 1.00 20.81 ? 36  LYS C C   1 
ATOM   3659  O  O   . LYS D  1 63  ? 46.456  100.994 -31.282 1.00 17.63 ? 36  LYS C O   1 
ATOM   3660  C  CB  . LYS D  1 63  ? 43.512  102.436 -31.594 1.00 20.83 ? 36  LYS C CB  1 
ATOM   3661  C  CG  . LYS D  1 63  ? 44.480  103.544 -31.957 1.00 28.66 ? 36  LYS C CG  1 
ATOM   3662  C  CD  . LYS D  1 63  ? 44.376  104.063 -33.381 1.00 44.79 ? 36  LYS C CD  1 
ATOM   3663  C  CE  . LYS D  1 63  ? 45.680  104.611 -33.931 1.00 43.13 ? 36  LYS C CE  1 
ATOM   3664  N  NZ  . LYS D  1 63  ? 46.130  103.972 -35.186 1.00 29.61 ? 36  LYS C NZ  1 
ATOM   3665  N  N   . GLY D  1 64  ? 45.066  100.115 -32.815 1.00 20.39 ? 37  GLY C N   1 
ATOM   3666  C  CA  . GLY D  1 64  ? 46.131  99.666  -33.716 1.00 16.55 ? 37  GLY C CA  1 
ATOM   3667  C  C   . GLY D  1 64  ? 46.735  98.325  -33.355 1.00 21.69 ? 37  GLY C C   1 
ATOM   3668  O  O   . GLY D  1 64  ? 47.705  97.974  -33.973 1.00 20.95 ? 37  GLY C O   1 
ATOM   3669  N  N   . LEU D  1 65  ? 46.121  97.599  -32.432 1.00 13.69 ? 38  LEU C N   1 
ATOM   3670  C  CA  . LEU D  1 65  ? 46.680  96.307  -31.981 1.00 16.46 ? 38  LEU C CA  1 
ATOM   3671  C  C   . LEU D  1 65  ? 46.041  95.131  -32.723 1.00 16.28 ? 38  LEU C C   1 
ATOM   3672  O  O   . LEU D  1 65  ? 44.860  95.153  -32.932 1.00 18.53 ? 38  LEU C O   1 
ATOM   3673  C  CB  . LEU D  1 65  ? 46.394  96.145  -30.485 1.00 13.42 ? 38  LEU C CB  1 
ATOM   3674  C  CG  . LEU D  1 65  ? 47.131  97.093  -29.545 1.00 16.99 ? 38  LEU C CG  1 
ATOM   3675  C  CD1 . LEU D  1 65  ? 46.468  97.137  -28.188 1.00 16.24 ? 38  LEU C CD1 1 
ATOM   3676  C  CD2 . LEU D  1 65  ? 48.579  96.695  -29.400 1.00 18.34 ? 38  LEU C CD2 1 
ATOM   3677  N  N   . THR D  1 66  ? 46.832  94.110  -33.039 1.00 17.89 ? 39  THR C N   1 
ATOM   3678  C  CA  . THR D  1 66  ? 46.243  92.884  -33.563 1.00 16.09 ? 39  THR C CA  1 
ATOM   3679  C  C   . THR D  1 66  ? 45.297  92.277  -32.535 1.00 25.49 ? 39  THR C C   1 
ATOM   3680  O  O   . THR D  1 66  ? 45.569  92.290  -31.331 1.00 21.83 ? 39  THR C O   1 
ATOM   3681  C  CB  . THR D  1 66  ? 47.327  91.858  -33.928 1.00 21.15 ? 39  THR C CB  1 
ATOM   3682  O  OG1 . THR D  1 66  ? 48.101  91.546  -32.763 1.00 22.30 ? 39  THR C OG1 1 
ATOM   3683  C  CG2 . THR D  1 66  ? 48.236  92.406  -34.994 1.00 23.63 ? 39  THR C CG2 1 
ATOM   3684  N  N   . GLU D  1 67  ? 44.171  91.760  -33.019 1.00 21.80 ? 40  GLU C N   1 
ATOM   3685  C  CA  . GLU D  1 67  ? 43.153  91.167  -32.161 1.00 17.80 ? 40  GLU C CA  1 
ATOM   3686  C  C   . GLU D  1 67  ? 43.770  90.111  -31.260 1.00 21.71 ? 40  GLU C C   1 
ATOM   3687  O  O   . GLU D  1 67  ? 44.599  89.310  -31.697 1.00 22.23 ? 40  GLU C O   1 
ATOM   3688  C  CB  . GLU D  1 67  ? 42.060  90.535  -33.033 1.00 29.33 ? 40  GLU C CB  1 
ATOM   3689  C  CG  . GLU D  1 67  ? 40.998  89.791  -32.269 1.00 29.90 ? 40  GLU C CG  1 
ATOM   3690  C  CD  . GLU D  1 67  ? 39.833  89.326  -33.160 1.00 43.07 ? 40  GLU C CD  1 
ATOM   3691  O  OE1 . GLU D  1 67  ? 39.961  89.348  -34.415 1.00 40.04 ? 40  GLU C OE1 1 
ATOM   3692  O  OE2 . GLU D  1 67  ? 38.781  88.956  -32.593 1.00 47.19 ? 40  GLU C OE2 1 
ATOM   3693  N  N   . GLY D  1 68  ? 43.389  90.132  -29.982 1.00 22.37 ? 41  GLY C N   1 
ATOM   3694  C  CA  . GLY D  1 68  ? 43.896  89.142  -29.057 1.00 24.30 ? 41  GLY C CA  1 
ATOM   3695  C  C   . GLY D  1 68  ? 44.711  89.756  -27.934 1.00 21.80 ? 41  GLY C C   1 
ATOM   3696  O  O   . GLY D  1 68  ? 44.614  90.961  -27.699 1.00 18.55 ? 41  GLY C O   1 
ATOM   3697  N  N   . LEU D  1 69  ? 45.562  88.949  -27.298 1.00 18.88 ? 42  LEU C N   1 
ATOM   3698  C  CA  . LEU D  1 69  ? 46.262  89.311  -26.065 1.00 19.51 ? 42  LEU C CA  1 
ATOM   3699  C  C   . LEU D  1 69  ? 47.598  89.989  -26.339 1.00 18.41 ? 42  LEU C C   1 
ATOM   3700  O  O   . LEU D  1 69  ? 48.361  89.557  -27.204 1.00 17.59 ? 42  LEU C O   1 
ATOM   3701  C  CB  . LEU D  1 69  ? 46.497  88.053  -25.227 1.00 22.13 ? 42  LEU C CB  1 
ATOM   3702  C  CG  . LEU D  1 69  ? 45.248  87.348  -24.696 1.00 22.79 ? 42  LEU C CG  1 
ATOM   3703  C  CD1 . LEU D  1 69  ? 45.613  85.917  -24.418 1.00 32.71 ? 42  LEU C CD1 1 
ATOM   3704  C  CD2 . LEU D  1 69  ? 44.793  88.005  -23.393 1.00 24.43 ? 42  LEU C CD2 1 
ATOM   3705  N  N   . HIS D  1 70  ? 47.899  91.024  -25.558 1.00 15.98 ? 43  HIS C N   1 
ATOM   3706  C  CA  . HIS D  1 70  ? 49.169  91.738  -25.633 1.00 15.47 ? 43  HIS C CA  1 
ATOM   3707  C  C   . HIS D  1 70  ? 49.715  91.992  -24.236 1.00 17.01 ? 43  HIS C C   1 
ATOM   3708  O  O   . HIS D  1 70  ? 48.997  92.527  -23.386 1.00 13.42 ? 43  HIS C O   1 
ATOM   3709  C  CB  . HIS D  1 70  ? 48.989  93.066  -26.366 1.00 13.42 ? 43  HIS C CB  1 
ATOM   3710  C  CG  . HIS D  1 70  ? 48.643  92.885  -27.809 1.00 18.62 ? 43  HIS C CG  1 
ATOM   3711  N  ND1 . HIS D  1 70  ? 49.603  92.869  -28.791 1.00 18.73 ? 43  HIS C ND1 1 
ATOM   3712  C  CD2 . HIS D  1 70  ? 47.458  92.686  -28.430 1.00 18.58 ? 43  HIS C CD2 1 
ATOM   3713  C  CE1 . HIS D  1 70  ? 49.023  92.683  -29.969 1.00 20.97 ? 43  HIS C CE1 1 
ATOM   3714  N  NE2 . HIS D  1 70  ? 47.720  92.561  -29.775 1.00 21.15 ? 43  HIS C NE2 1 
ATOM   3715  N  N   . GLY D  1 71  ? 50.986  91.638  -24.017 1.00 13.96 ? 44  GLY C N   1 
ATOM   3716  C  CA  . GLY D  1 71  ? 51.632  91.959  -22.749 1.00 19.10 ? 44  GLY C CA  1 
ATOM   3717  C  C   . GLY D  1 71  ? 51.606  93.452  -22.461 1.00 17.49 ? 44  GLY C C   1 
ATOM   3718  O  O   . GLY D  1 71  ? 51.690  94.289  -23.359 1.00 16.24 ? 44  GLY C O   1 
ATOM   3719  N  N   . PHE D  1 72  ? 51.505  93.791  -21.179 1.00 13.42 ? 45  PHE C N   1 
ATOM   3720  C  CA  . PHE D  1 72  ? 51.190  95.164  -20.760 1.00 17.41 ? 45  PHE C CA  1 
ATOM   3721  C  C   . PHE D  1 72  ? 51.947  95.372  -19.449 1.00 15.39 ? 45  PHE C C   1 
ATOM   3722  O  O   . PHE D  1 72  ? 51.530  94.842  -18.418 1.00 14.98 ? 45  PHE C O   1 
ATOM   3723  C  CB  . PHE D  1 72  ? 49.679  95.320  -20.596 1.00 15.62 ? 45  PHE C CB  1 
ATOM   3724  C  CG  . PHE D  1 72  ? 49.189  96.721  -20.277 1.00 13.79 ? 45  PHE C CG  1 
ATOM   3725  C  CD1 . PHE D  1 72  ? 49.244  97.748  -21.202 1.00 15.06 ? 45  PHE C CD1 1 
ATOM   3726  C  CD2 . PHE D  1 72  ? 48.590  96.977  -19.050 1.00 18.55 ? 45  PHE C CD2 1 
ATOM   3727  C  CE1 . PHE D  1 72  ? 48.730  99.016  -20.906 1.00 17.21 ? 45  PHE C CE1 1 
ATOM   3728  C  CE2 . PHE D  1 72  ? 48.088  98.246  -18.741 1.00 19.88 ? 45  PHE C CE2 1 
ATOM   3729  C  CZ  . PHE D  1 72  ? 48.161  99.264  -19.673 1.00 19.30 ? 45  PHE C CZ  1 
ATOM   3730  N  N   . HIS D  1 73  ? 53.092  96.057  -19.513 1.00 13.42 ? 46  HIS C N   1 
ATOM   3731  C  CA  . HIS D  1 73  ? 54.032  96.062  -18.397 1.00 17.11 ? 46  HIS C CA  1 
ATOM   3732  C  C   . HIS D  1 73  ? 54.565  97.453  -18.095 1.00 17.63 ? 46  HIS C C   1 
ATOM   3733  O  O   . HIS D  1 73  ? 54.735  98.287  -18.990 1.00 14.94 ? 46  HIS C O   1 
ATOM   3734  C  CB  . HIS D  1 73  ? 55.236  95.166  -18.662 1.00 15.36 ? 46  HIS C CB  1 
ATOM   3735  C  CG  . HIS D  1 73  ? 54.870  93.793  -19.094 1.00 17.66 ? 46  HIS C CG  1 
ATOM   3736  N  ND1 . HIS D  1 73  ? 55.274  93.263  -20.297 1.00 24.12 ? 46  HIS C ND1 1 
ATOM   3737  C  CD2 . HIS D  1 73  ? 54.109  92.847  -18.497 1.00 17.56 ? 46  HIS C CD2 1 
ATOM   3738  C  CE1 . HIS D  1 73  ? 54.798  92.037  -20.413 1.00 23.97 ? 46  HIS C CE1 1 
ATOM   3739  N  NE2 . HIS D  1 73  ? 54.090  91.760  -19.332 1.00 20.87 ? 46  HIS C NE2 1 
ATOM   3740  N  N   . VAL D  1 74  ? 54.846  97.686  -16.815 1.00 14.97 ? 47  VAL C N   1 
ATOM   3741  C  CA  . VAL D  1 74  ? 55.607  98.855  -16.405 1.00 16.87 ? 47  VAL C CA  1 
ATOM   3742  C  C   . VAL D  1 74  ? 57.075  98.469  -16.425 1.00 18.36 ? 47  VAL C C   1 
ATOM   3743  O  O   . VAL D  1 74  ? 57.474  97.506  -15.755 1.00 14.90 ? 47  VAL C O   1 
ATOM   3744  C  CB  . VAL D  1 74  ? 55.208  99.346  -15.008 1.00 15.15 ? 47  VAL C CB  1 
ATOM   3745  C  CG1 . VAL D  1 74  ? 56.009  100.599 -14.701 1.00 15.48 ? 47  VAL C CG1 1 
ATOM   3746  C  CG2 . VAL D  1 74  ? 53.718  99.629  -14.952 1.00 19.09 ? 47  VAL C CG2 1 
ATOM   3747  N  N   . HIS D  1 75  ? 57.875  99.226  -17.175 1.00 13.70 ? 48  HIS C N   1 
ATOM   3748  C  CA  . HIS D  1 75  ? 59.307  98.994  -17.306 1.00 14.43 ? 48  HIS C CA  1 
ATOM   3749  C  C   . HIS D  1 75  ? 60.055  99.974  -16.408 1.00 19.18 ? 48  HIS C C   1 
ATOM   3750  O  O   . HIS D  1 75  ? 59.515  100.993 -15.989 1.00 18.23 ? 48  HIS C O   1 
ATOM   3751  C  CB  . HIS D  1 75  ? 59.768  99.122  -18.774 1.00 19.27 ? 48  HIS C CB  1 
ATOM   3752  C  CG  . HIS D  1 75  ? 59.342  97.974  -19.640 1.00 18.09 ? 48  HIS C CG  1 
ATOM   3753  N  ND1 . HIS D  1 75  ? 60.240  97.123  -20.253 1.00 16.83 ? 48  HIS C ND1 1 
ATOM   3754  C  CD2 . HIS D  1 75  ? 58.108  97.514  -19.967 1.00 17.16 ? 48  HIS C CD2 1 
ATOM   3755  C  CE1 . HIS D  1 75  ? 59.576  96.208  -20.943 1.00 21.43 ? 48  HIS C CE1 1 
ATOM   3756  N  NE2 . HIS D  1 75  ? 58.282  96.425  -20.789 1.00 15.86 ? 48  HIS C NE2 1 
ATOM   3757  N  N   . GLU D  1 76  ? 61.304  99.631  -16.090 1.00 17.36 ? 49  GLU C N   1 
ATOM   3758  C  CA  . GLU D  1 76  ? 61.994  100.294 -14.982 1.00 19.81 ? 49  GLU C CA  1 
ATOM   3759  C  C   . GLU D  1 76  ? 62.190  101.799 -15.208 1.00 20.68 ? 49  GLU C C   1 
ATOM   3760  O  O   . GLU D  1 76  ? 61.970  102.594 -14.288 1.00 21.89 ? 49  GLU C O   1 
ATOM   3761  C  CB  . GLU D  1 76  ? 63.337  99.622  -14.736 1.00 23.87 ? 49  GLU C CB  1 
ATOM   3762  C  CG  . GLU D  1 76  ? 64.063  100.240 -13.551 1.00 27.12 ? 49  GLU C CG  1 
ATOM   3763  C  CD  . GLU D  1 76  ? 65.254  99.421  -13.153 1.00 32.01 ? 49  GLU C CD  1 
ATOM   3764  O  OE1 . GLU D  1 76  ? 65.572  98.476  -13.900 1.00 28.73 ? 49  GLU C OE1 1 
ATOM   3765  O  OE2 . GLU D  1 76  ? 65.869  99.728  -12.110 1.00 35.57 ? 49  GLU C OE2 1 
ATOM   3766  N  N   . PHE D  1 77  ? 62.589  102.217 -16.413 1.00 20.19 ? 50  PHE C N   1 
ATOM   3767  C  CA  . PHE D  1 77  ? 63.029  103.594 -16.636 1.00 18.04 ? 50  PHE C CA  1 
ATOM   3768  C  C   . PHE D  1 77  ? 62.038  104.398 -17.475 1.00 20.67 ? 50  PHE C C   1 
ATOM   3769  O  O   . PHE D  1 77  ? 61.486  103.895 -18.451 1.00 21.13 ? 50  PHE C O   1 
ATOM   3770  C  CB  . PHE D  1 77  ? 64.398  103.618 -17.317 1.00 21.15 ? 50  PHE C CB  1 
ATOM   3771  C  CG  . PHE D  1 77  ? 65.425  102.804 -16.604 1.00 25.16 ? 50  PHE C CG  1 
ATOM   3772  C  CD1 . PHE D  1 77  ? 65.791  103.123 -15.308 1.00 24.52 ? 50  PHE C CD1 1 
ATOM   3773  C  CD2 . PHE D  1 77  ? 66.004  101.705 -17.218 1.00 27.96 ? 50  PHE C CD2 1 
ATOM   3774  C  CE1 . PHE D  1 77  ? 66.730  102.356 -14.628 1.00 34.56 ? 50  PHE C CE1 1 
ATOM   3775  C  CE2 . PHE D  1 77  ? 66.939  100.928 -16.545 1.00 32.77 ? 50  PHE C CE2 1 
ATOM   3776  C  CZ  . PHE D  1 77  ? 67.302  101.253 -15.258 1.00 25.54 ? 50  PHE C CZ  1 
ATOM   3777  N  N   . GLY D  1 78  ? 61.865  105.670 -17.113 1.00 18.89 ? 51  GLY C N   1 
ATOM   3778  C  CA  . GLY D  1 78  ? 61.067  106.616 -17.879 1.00 19.77 ? 51  GLY C CA  1 
ATOM   3779  C  C   . GLY D  1 78  ? 61.928  107.343 -18.896 1.00 22.40 ? 51  GLY C C   1 
ATOM   3780  O  O   . GLY D  1 78  ? 61.889  108.575 -19.012 1.00 22.20 ? 51  GLY C O   1 
ATOM   3781  N  N   . ASP D  1 79  ? 62.713  106.562 -19.632 1.00 22.75 ? 52  ASP C N   1 
ATOM   3782  C  CA  . ASP D  1 79  ? 63.750  107.040 -20.542 1.00 21.62 ? 52  ASP C CA  1 
ATOM   3783  C  C   . ASP D  1 79  ? 63.334  106.633 -21.947 1.00 23.35 ? 52  ASP C C   1 
ATOM   3784  O  O   . ASP D  1 79  ? 63.409  105.453 -22.306 1.00 23.56 ? 52  ASP C O   1 
ATOM   3785  C  CB  . ASP D  1 79  ? 65.101  106.431 -20.178 1.00 22.41 ? 52  ASP C CB  1 
ATOM   3786  C  CG  . ASP D  1 79  ? 66.240  106.886 -21.102 1.00 28.86 ? 52  ASP C CG  1 
ATOM   3787  O  OD1 . ASP D  1 79  ? 65.995  107.402 -22.213 1.00 26.94 ? 52  ASP C OD1 1 
ATOM   3788  O  OD2 . ASP D  1 79  ? 67.407  106.700 -20.700 1.00 30.91 ? 52  ASP C OD2 1 
ATOM   3789  N  N   A ASN D  1 80  ? 62.914  107.620 -22.736 0.50 23.48 ? 53  ASN C N   1 
ATOM   3790  N  N   B ASN D  1 80  ? 62.871  107.584 -22.741 0.50 23.50 ? 53  ASN C N   1 
ATOM   3791  C  CA  A ASN D  1 80  ? 62.454  107.416 -24.105 0.50 25.06 ? 53  ASN C CA  1 
ATOM   3792  C  CA  B ASN D  1 80  ? 62.494  107.281 -24.116 0.50 24.91 ? 53  ASN C CA  1 
ATOM   3793  C  C   A ASN D  1 80  ? 63.470  107.912 -25.133 0.50 26.97 ? 53  ASN C C   1 
ATOM   3794  C  C   B ASN D  1 80  ? 63.458  107.922 -25.119 0.50 26.64 ? 53  ASN C C   1 
ATOM   3795  O  O   A ASN D  1 80  ? 63.120  108.124 -26.301 0.50 25.23 ? 53  ASN C O   1 
ATOM   3796  O  O   B ASN D  1 80  ? 63.066  108.248 -26.245 0.50 26.38 ? 53  ASN C O   1 
ATOM   3797  C  CB  A ASN D  1 80  ? 61.098  108.102 -24.293 0.50 25.02 ? 53  ASN C CB  1 
ATOM   3798  C  CB  B ASN D  1 80  ? 61.043  107.700 -24.376 0.50 25.40 ? 53  ASN C CB  1 
ATOM   3799  C  CG  A ASN D  1 80  ? 60.435  107.742 -25.607 0.50 28.57 ? 53  ASN C CG  1 
ATOM   3800  C  CG  B ASN D  1 80  ? 60.018  106.869 -23.567 0.50 30.71 ? 53  ASN C CG  1 
ATOM   3801  O  OD1 A ASN D  1 80  ? 60.263  106.567 -25.922 0.50 33.44 ? 53  ASN C OD1 1 
ATOM   3802  O  OD1 B ASN D  1 80  ? 60.347  105.832 -22.957 0.50 29.09 ? 53  ASN C OD1 1 
ATOM   3803  N  ND2 A ASN D  1 80  ? 60.029  108.752 -26.363 0.50 27.12 ? 53  ASN C ND2 1 
ATOM   3804  N  ND2 B ASN D  1 80  ? 58.768  107.342 -23.551 0.50 30.81 ? 53  ASN C ND2 1 
ATOM   3805  N  N   . THR D  1 81  ? 64.731  108.087 -24.727 1.00 24.90 ? 54  THR C N   1 
ATOM   3806  C  CA  . THR D  1 81  ? 65.724  108.642 -25.646 1.00 25.89 ? 54  THR C CA  1 
ATOM   3807  C  C   . THR D  1 81  ? 65.960  107.730 -26.839 1.00 29.88 ? 54  THR C C   1 
ATOM   3808  O  O   . THR D  1 81  ? 66.306  108.209 -27.919 1.00 30.70 ? 54  THR C O   1 
ATOM   3809  C  CB  . THR D  1 81  ? 67.066  108.905 -24.952 1.00 24.96 ? 54  THR C CB  1 
ATOM   3810  O  OG1 . THR D  1 81  ? 67.546  107.717 -24.310 1.00 26.53 ? 54  THR C OG1 1 
ATOM   3811  C  CG2 . THR D  1 81  ? 66.935  110.016 -23.929 1.00 23.06 ? 54  THR C CG2 1 
ATOM   3812  N  N   . ALA D  1 82  ? 65.783  106.426 -26.667 1.00 25.70 ? 55  ALA C N   1 
ATOM   3813  C  CA  . ALA D  1 82  ? 65.929  105.459 -27.743 1.00 30.18 ? 55  ALA C CA  1 
ATOM   3814  C  C   . ALA D  1 82  ? 64.594  104.788 -28.035 1.00 29.60 ? 55  ALA C C   1 
ATOM   3815  O  O   . ALA D  1 82  ? 64.524  103.589 -28.291 1.00 35.14 ? 55  ALA C O   1 
ATOM   3816  C  CB  . ALA D  1 82  ? 66.995  104.419 -27.397 1.00 32.56 ? 55  ALA C CB  1 
ATOM   3817  N  N   . GLY D  1 83  ? 63.513  105.558 -27.973 1.00 28.33 ? 56  GLY C N   1 
ATOM   3818  C  CA  . GLY D  1 83  ? 62.215  104.925 -28.068 1.00 29.27 ? 56  GLY C CA  1 
ATOM   3819  C  C   . GLY D  1 83  ? 61.979  104.011 -26.875 1.00 27.93 ? 56  GLY C C   1 
ATOM   3820  O  O   . GLY D  1 83  ? 62.505  104.220 -25.772 1.00 25.31 ? 56  GLY C O   1 
ATOM   3821  N  N   . CYS D  1 84  ? 61.212  102.950 -27.111 1.00 27.90 ? 57  CYS C N   1 
ATOM   3822  C  CA  . CYS D  1 84  ? 60.804  102.084 -26.007 1.00 26.85 ? 57  CYS C CA  1 
ATOM   3823  C  C   . CYS D  1 84  ? 61.950  101.221 -25.512 1.00 24.11 ? 57  CYS C C   1 
ATOM   3824  O  O   . CYS D  1 84  ? 61.890  100.715 -24.383 1.00 22.10 ? 57  CYS C O   1 
ATOM   3825  C  CB  . CYS D  1 84  ? 59.628  101.218 -26.449 1.00 29.60 ? 57  CYS C CB  1 
ATOM   3826  S  SG  . CYS D  1 84  ? 58.167  102.217 -26.967 1.00 30.39 ? 57  CYS C SG  1 
ATOM   3827  N  N   . THR D  1 85  ? 62.996  101.065 -26.329 1.00 23.45 ? 58  THR C N   1 
ATOM   3828  C  CA  . THR D  1 85  ? 64.153  100.261 -25.944 1.00 26.02 ? 58  THR C CA  1 
ATOM   3829  C  C   . THR D  1 85  ? 64.816  100.788 -24.684 1.00 25.28 ? 58  THR C C   1 
ATOM   3830  O  O   . THR D  1 85  ? 65.276  100.006 -23.844 1.00 26.00 ? 58  THR C O   1 
ATOM   3831  C  CB  . THR D  1 85  ? 65.172  100.252 -27.083 1.00 28.99 ? 58  THR C CB  1 
ATOM   3832  O  OG1 . THR D  1 85  ? 64.505  99.910  -28.291 1.00 33.14 ? 58  THR C OG1 1 
ATOM   3833  C  CG2 . THR D  1 85  ? 66.286  99.247  -26.801 1.00 33.79 ? 58  THR C CG2 1 
ATOM   3834  N  N   . SER D  1 86  ? 64.909  102.110 -24.538 1.00 21.96 ? 59  SER C N   1 
ATOM   3835  C  CA  . SER D  1 86  ? 65.625  102.626 -23.376 1.00 24.39 ? 59  SER C CA  1 
ATOM   3836  C  C   . SER D  1 86  ? 64.806  102.567 -22.089 1.00 23.43 ? 59  SER C C   1 
ATOM   3837  O  O   . SER D  1 86  ? 65.295  103.007 -21.047 1.00 23.67 ? 59  SER C O   1 
ATOM   3838  C  CB  . SER D  1 86  ? 66.098  104.059 -23.637 1.00 27.24 ? 59  SER C CB  1 
ATOM   3839  O  OG  . SER D  1 86  ? 65.137  104.789 -24.370 1.00 27.06 ? 59  SER C OG  1 
ATOM   3840  N  N   . ALA D  1 87  ? 63.582  102.033 -22.121 1.00 21.91 ? 60  ALA C N   1 
ATOM   3841  C  CA  . ALA D  1 87  ? 62.843  101.878 -20.865 1.00 20.78 ? 60  ALA C CA  1 
ATOM   3842  C  C   . ALA D  1 87  ? 63.412  100.779 -19.971 1.00 21.99 ? 60  ALA C C   1 
ATOM   3843  O  O   . ALA D  1 87  ? 63.020  100.681 -18.796 1.00 22.80 ? 60  ALA C O   1 
ATOM   3844  C  CB  . ALA D  1 87  ? 61.371  101.595 -21.163 1.00 20.02 ? 60  ALA C CB  1 
ATOM   3845  N  N   . GLY D  1 88  ? 64.298  99.934  -20.489 1.00 22.41 ? 61  GLY C N   1 
ATOM   3846  C  CA  . GLY D  1 88  ? 64.899  98.889  -19.693 1.00 22.78 ? 61  GLY C CA  1 
ATOM   3847  C  C   . GLY D  1 88  ? 63.958  97.717  -19.483 1.00 21.71 ? 61  GLY C C   1 
ATOM   3848  O  O   . GLY D  1 88  ? 62.995  97.519  -20.236 1.00 22.21 ? 61  GLY C O   1 
ATOM   3849  N  N   . PRO D  1 89  ? 64.233  96.901  -18.453 1.00 22.71 ? 62  PRO C N   1 
ATOM   3850  C  CA  . PRO D  1 89  ? 63.439  95.685  -18.239 1.00 24.55 ? 62  PRO C CA  1 
ATOM   3851  C  C   . PRO D  1 89  ? 62.177  95.990  -17.453 1.00 20.98 ? 62  PRO C C   1 
ATOM   3852  O  O   . PRO D  1 89  ? 61.911  97.149  -17.131 1.00 20.65 ? 62  PRO C O   1 
ATOM   3853  C  CB  . PRO D  1 89  ? 64.388  94.798  -17.425 1.00 26.13 ? 62  PRO C CB  1 
ATOM   3854  C  CG  . PRO D  1 89  ? 65.135  95.810  -16.559 1.00 24.22 ? 62  PRO C CG  1 
ATOM   3855  C  CD  . PRO D  1 89  ? 65.278  97.064  -17.422 1.00 25.03 ? 62  PRO C CD  1 
ATOM   3856  N  N   . HIS D  1 90  ? 61.412  94.964  -17.097 1.00 20.86 ? 63  HIS C N   1 
ATOM   3857  C  CA  . HIS D  1 90  ? 60.232  95.195  -16.267 1.00 20.28 ? 63  HIS C CA  1 
ATOM   3858  C  C   . HIS D  1 90  ? 60.668  95.763  -14.917 1.00 20.51 ? 63  HIS C C   1 
ATOM   3859  O  O   . HIS D  1 90  ? 61.724  95.405  -14.385 1.00 23.83 ? 63  HIS C O   1 
ATOM   3860  C  CB  . HIS D  1 90  ? 59.442  93.890  -16.066 1.00 21.45 ? 63  HIS C CB  1 
ATOM   3861  C  CG  . HIS D  1 90  ? 58.883  93.318  -17.334 1.00 18.87 ? 63  HIS C CG  1 
ATOM   3862  N  ND1 . HIS D  1 90  ? 58.083  92.203  -17.351 1.00 24.46 ? 63  HIS C ND1 1 
ATOM   3863  C  CD2 . HIS D  1 90  ? 59.009  93.706  -18.633 1.00 21.52 ? 63  HIS C CD2 1 
ATOM   3864  C  CE1 . HIS D  1 90  ? 57.754  91.906  -18.593 1.00 20.24 ? 63  HIS C CE1 1 
ATOM   3865  N  NE2 . HIS D  1 90  ? 58.285  92.817  -19.391 1.00 23.74 ? 63  HIS C NE2 1 
ATOM   3866  N  N   . PHE D  1 91  ? 59.880  96.705  -14.393 1.00 16.40 ? 64  PHE C N   1 
ATOM   3867  C  CA  . PHE D  1 91  ? 60.133  97.275  -13.075 1.00 14.81 ? 64  PHE C CA  1 
ATOM   3868  C  C   . PHE D  1 91  ? 60.078  96.165  -12.033 1.00 21.39 ? 64  PHE C C   1 
ATOM   3869  O  O   . PHE D  1 91  ? 59.044  95.525  -11.848 1.00 19.16 ? 64  PHE C O   1 
ATOM   3870  C  CB  . PHE D  1 91  ? 59.089  98.360  -12.784 1.00 17.06 ? 64  PHE C CB  1 
ATOM   3871  C  CG  . PHE D  1 91  ? 59.228  99.030  -11.425 1.00 18.83 ? 64  PHE C CG  1 
ATOM   3872  C  CD1 . PHE D  1 91  ? 60.476  99.380  -10.903 1.00 20.58 ? 64  PHE C CD1 1 
ATOM   3873  C  CD2 . PHE D  1 91  ? 58.092  99.336  -10.693 1.00 15.30 ? 64  PHE C CD2 1 
ATOM   3874  C  CE1 . PHE D  1 91  ? 60.577  100.003 -9.633  1.00 22.60 ? 64  PHE C CE1 1 
ATOM   3875  C  CE2 . PHE D  1 91  ? 58.180  99.932  -9.431  1.00 21.87 ? 64  PHE C CE2 1 
ATOM   3876  C  CZ  . PHE D  1 91  ? 59.430  100.289 -8.910  1.00 18.79 ? 64  PHE C CZ  1 
ATOM   3877  N  N   . ASN D  1 92  ? 61.200  95.907  -11.365 1.00 18.00 ? 65  ASN C N   1 
ATOM   3878  C  CA  . ASN D  1 92  ? 61.358  94.688  -10.572 1.00 19.33 ? 65  ASN C CA  1 
ATOM   3879  C  C   . ASN D  1 92  ? 62.209  94.984  -9.335  1.00 20.07 ? 65  ASN C C   1 
ATOM   3880  O  O   . ASN D  1 92  ? 63.281  94.405  -9.147  1.00 23.61 ? 65  ASN C O   1 
ATOM   3881  C  CB  . ASN D  1 92  ? 61.981  93.594  -11.435 1.00 20.07 ? 65  ASN C CB  1 
ATOM   3882  C  CG  . ASN D  1 92  ? 62.054  92.244  -10.729 1.00 23.73 ? 65  ASN C CG  1 
ATOM   3883  O  OD1 . ASN D  1 92  ? 61.336  91.993  -9.767  1.00 21.61 ? 65  ASN C OD1 1 
ATOM   3884  N  ND2 . ASN D  1 92  ? 62.888  91.353  -11.254 1.00 21.60 ? 65  ASN C ND2 1 
ATOM   3885  N  N   . PRO D  1 93  ? 61.754  95.893  -8.470  1.00 22.97 ? 66  PRO C N   1 
ATOM   3886  C  CA  . PRO D  1 93  ? 62.602  96.301  -7.337  1.00 27.66 ? 66  PRO C CA  1 
ATOM   3887  C  C   . PRO D  1 93  ? 62.820  95.200  -6.309  1.00 28.30 ? 66  PRO C C   1 
ATOM   3888  O  O   . PRO D  1 93  ? 63.744  95.320  -5.500  1.00 31.66 ? 66  PRO C O   1 
ATOM   3889  C  CB  . PRO D  1 93  ? 61.834  97.473  -6.724  1.00 24.95 ? 66  PRO C CB  1 
ATOM   3890  C  CG  . PRO D  1 93  ? 60.419  97.210  -7.074  1.00 23.77 ? 66  PRO C CG  1 
ATOM   3891  C  CD  . PRO D  1 93  ? 60.443  96.559  -8.432  1.00 20.84 ? 66  PRO C CD  1 
ATOM   3892  N  N   . LEU D  1 94  ? 62.002  94.151  -6.287  1.00 26.39 ? 67  LEU C N   1 
ATOM   3893  C  CA  . LEU D  1 94  ? 62.227  93.030  -5.379  1.00 28.86 ? 67  LEU C CA  1 
ATOM   3894  C  C   . LEU D  1 94  ? 62.934  91.855  -6.047  1.00 30.75 ? 67  LEU C C   1 
ATOM   3895  O  O   . LEU D  1 94  ? 63.031  90.780  -5.445  1.00 28.24 ? 67  LEU C O   1 
ATOM   3896  C  CB  . LEU D  1 94  ? 60.907  92.581  -4.762  1.00 28.72 ? 67  LEU C CB  1 
ATOM   3897  C  CG  . LEU D  1 94  ? 60.235  93.667  -3.923  1.00 29.77 ? 67  LEU C CG  1 
ATOM   3898  C  CD1 . LEU D  1 94  ? 58.810  93.269  -3.557  1.00 36.89 ? 67  LEU C CD1 1 
ATOM   3899  C  CD2 . LEU D  1 94  ? 61.067  93.864  -2.653  1.00 36.34 ? 67  LEU C CD2 1 
ATOM   3900  N  N   . SER D  1 95  ? 63.449  92.055  -7.263  1.00 25.81 ? 68  SER C N   1 
ATOM   3901  C  CA  . SER D  1 95  ? 64.211  91.054  -8.028  1.00 26.32 ? 68  SER C CA  1 
ATOM   3902  C  C   . SER D  1 95  ? 63.530  89.684  -8.017  1.00 32.80 ? 68  SER C C   1 
ATOM   3903  O  O   . SER D  1 95  ? 64.133  88.664  -7.683  1.00 30.45 ? 68  SER C O   1 
ATOM   3904  C  CB  . SER D  1 95  ? 65.662  90.948  -7.527  1.00 37.76 ? 68  SER C CB  1 
ATOM   3905  O  OG  . SER D  1 95  ? 66.224  92.218  -7.219  1.00 37.37 ? 68  SER C OG  1 
ATOM   3906  N  N   . ARG D  1 96  ? 62.257  89.659  -8.388  1.00 25.95 ? 69  ARG C N   1 
ATOM   3907  C  CA  . ARG D  1 96  ? 61.532  88.407  -8.520  1.00 20.67 ? 69  ARG C CA  1 
ATOM   3908  C  C   . ARG D  1 96  ? 61.555  87.930  -9.967  1.00 25.21 ? 69  ARG C C   1 
ATOM   3909  O  O   . ARG D  1 96  ? 62.008  88.632  -10.877 1.00 23.69 ? 69  ARG C O   1 
ATOM   3910  C  CB  . ARG D  1 96  ? 60.095  88.575  -8.043  1.00 26.58 ? 69  ARG C CB  1 
ATOM   3911  C  CG  . ARG D  1 96  ? 59.987  89.215  -6.661  1.00 31.52 ? 69  ARG C CG  1 
ATOM   3912  C  CD  . ARG D  1 96  ? 60.039  88.189  -5.534  1.00 33.17 ? 69  ARG C CD  1 
ATOM   3913  N  NE  . ARG D  1 96  ? 59.861  88.805  -4.217  1.00 38.36 ? 69  ARG C NE  1 
ATOM   3914  C  CZ  . ARG D  1 96  ? 60.810  88.934  -3.291  1.00 49.31 ? 69  ARG C CZ  1 
ATOM   3915  N  NH1 . ARG D  1 96  ? 62.035  88.456  -3.471  1.00 38.58 ? 69  ARG C NH1 1 
ATOM   3916  N  NH2 . ARG D  1 96  ? 60.526  89.564  -2.154  1.00 47.68 ? 69  ARG C NH2 1 
ATOM   3917  N  N   . LYS D  1 97  ? 61.059  86.714  -10.174 1.00 24.49 ? 70  LYS C N   1 
ATOM   3918  C  CA  . LYS D  1 97  ? 60.834  86.241  -11.528 1.00 22.43 ? 70  LYS C CA  1 
ATOM   3919  C  C   . LYS D  1 97  ? 59.514  86.800  -12.065 1.00 22.29 ? 70  LYS C C   1 
ATOM   3920  O  O   . LYS D  1 97  ? 58.623  87.196  -11.305 1.00 22.60 ? 70  LYS C O   1 
ATOM   3921  C  CB  . LYS D  1 97  ? 60.837  84.711  -11.575 1.00 26.51 ? 70  LYS C CB  1 
ATOM   3922  C  CG  . LYS D  1 97  ? 62.247  84.124  -11.380 1.00 33.78 ? 70  LYS C CG  1 
ATOM   3923  C  CD  . LYS D  1 97  ? 62.284  82.593  -11.486 1.00 43.03 ? 70  LYS C CD  1 
ATOM   3924  C  CE  . LYS D  1 97  ? 61.436  81.934  -10.411 1.00 45.59 ? 70  LYS C CE  1 
ATOM   3925  N  NZ  . LYS D  1 97  ? 62.011  80.623  -9.967  1.00 56.85 ? 70  LYS C NZ  1 
ATOM   3926  N  N   . HIS D  1 98  ? 59.410  86.834  -13.393 1.00 22.02 ? 71  HIS C N   1 
ATOM   3927  C  CA  . HIS D  1 98  ? 58.202  87.318  -14.048 1.00 23.62 ? 71  HIS C CA  1 
ATOM   3928  C  C   . HIS D  1 98  ? 57.004  86.440  -13.700 1.00 21.33 ? 71  HIS C C   1 
ATOM   3929  O  O   . HIS D  1 98  ? 57.115  85.212  -13.586 1.00 22.89 ? 71  HIS C O   1 
ATOM   3930  C  CB  . HIS D  1 98  ? 58.420  87.351  -15.566 1.00 19.71 ? 71  HIS C CB  1 
ATOM   3931  C  CG  . HIS D  1 98  ? 57.211  87.771  -16.343 1.00 20.22 ? 71  HIS C CG  1 
ATOM   3932  N  ND1 . HIS D  1 98  ? 56.834  89.085  -16.479 1.00 23.96 ? 71  HIS C ND1 1 
ATOM   3933  C  CD2 . HIS D  1 98  ? 56.299  87.041  -17.034 1.00 19.20 ? 71  HIS C CD2 1 
ATOM   3934  C  CE1 . HIS D  1 98  ? 55.745  89.156  -17.221 1.00 17.48 ? 71  HIS C CE1 1 
ATOM   3935  N  NE2 . HIS D  1 98  ? 55.397  87.929  -17.568 1.00 19.86 ? 71  HIS C NE2 1 
ATOM   3936  N  N   . GLY D  1 99  ? 55.854  87.078  -13.509 1.00 17.04 ? 72  GLY C N   1 
ATOM   3937  C  CA  . GLY D  1 99  ? 54.627  86.346  -13.274 1.00 20.51 ? 72  GLY C CA  1 
ATOM   3938  C  C   . GLY D  1 99  ? 53.427  87.088  -13.813 1.00 23.80 ? 72  GLY C C   1 
ATOM   3939  O  O   . GLY D  1 99  ? 53.574  88.093  -14.519 1.00 19.94 ? 72  GLY C O   1 
ATOM   3940  N  N   . GLY D  1 100 ? 52.237  86.591  -13.518 1.00 20.05 ? 73  GLY C N   1 
ATOM   3941  C  CA  . GLY D  1 100 ? 51.022  87.289  -13.863 1.00 20.46 ? 73  GLY C CA  1 
ATOM   3942  C  C   . GLY D  1 100 ? 50.625  88.151  -12.688 1.00 21.60 ? 73  GLY C C   1 
ATOM   3943  O  O   . GLY D  1 100 ? 51.146  87.984  -11.582 1.00 24.91 ? 73  GLY C O   1 
ATOM   3944  N  N   . PRO D  1 101 ? 49.708  89.093  -12.902 1.00 21.49 ? 74  PRO C N   1 
ATOM   3945  C  CA  . PRO D  1 101 ? 49.378  90.032  -11.816 1.00 20.41 ? 74  PRO C CA  1 
ATOM   3946  C  C   . PRO D  1 101 ? 48.851  89.346  -10.575 1.00 24.82 ? 74  PRO C C   1 
ATOM   3947  O  O   . PRO D  1 101 ? 49.028  89.876  -9.476  1.00 23.95 ? 74  PRO C O   1 
ATOM   3948  C  CB  . PRO D  1 101 ? 48.325  90.967  -12.442 1.00 22.39 ? 74  PRO C CB  1 
ATOM   3949  C  CG  . PRO D  1 101 ? 47.966  90.356  -13.810 1.00 23.49 ? 74  PRO C CG  1 
ATOM   3950  C  CD  . PRO D  1 101 ? 49.114  89.478  -14.196 1.00 18.70 ? 74  PRO C CD  1 
ATOM   3951  N  N   . LYS D  1 102 ? 48.229  88.176  -10.697 1.00 25.28 ? 75  LYS C N   1 
ATOM   3952  C  CA  . LYS D  1 102 ? 47.683  87.534  -9.510  1.00 25.85 ? 75  LYS C CA  1 
ATOM   3953  C  C   . LYS D  1 102 ? 48.681  86.627  -8.801  1.00 30.64 ? 75  LYS C C   1 
ATOM   3954  O  O   . LYS D  1 102 ? 48.338  86.066  -7.752  1.00 32.99 ? 75  LYS C O   1 
ATOM   3955  C  CB  . LYS D  1 102 ? 46.427  86.740  -9.857  1.00 27.96 ? 75  LYS C CB  1 
ATOM   3956  C  CG  . LYS D  1 102 ? 45.286  87.618  -10.343 1.00 33.31 ? 75  LYS C CG  1 
ATOM   3957  C  CD  . LYS D  1 102 ? 44.413  86.834  -11.298 1.00 44.19 ? 75  LYS C CD  1 
ATOM   3958  C  CE  . LYS D  1 102 ? 43.445  85.992  -10.464 1.00 47.99 ? 75  LYS C CE  1 
ATOM   3959  N  NZ  . LYS D  1 102 ? 43.259  84.599  -10.935 1.00 53.84 ? 75  LYS C NZ  1 
ATOM   3960  N  N   . ASP D  1 103 ? 49.903  86.491  -9.320  1.00 22.43 ? 76  ASP C N   1 
ATOM   3961  C  CA  . ASP D  1 103 ? 50.921  85.662  -8.684  1.00 28.41 ? 76  ASP C CA  1 
ATOM   3962  C  C   . ASP D  1 103 ? 51.633  86.425  -7.581  1.00 29.63 ? 76  ASP C C   1 
ATOM   3963  O  O   . ASP D  1 103 ? 51.889  87.627  -7.693  1.00 22.39 ? 76  ASP C O   1 
ATOM   3964  C  CB  . ASP D  1 103 ? 51.978  85.185  -9.688  1.00 28.53 ? 76  ASP C CB  1 
ATOM   3965  C  CG  . ASP D  1 103 ? 51.422  84.251  -10.741 1.00 38.42 ? 76  ASP C CG  1 
ATOM   3966  O  OD1 . ASP D  1 103 ? 50.732  83.285  -10.352 1.00 46.00 ? 76  ASP C OD1 1 
ATOM   3967  O  OD2 . ASP D  1 103 ? 51.659  84.494  -11.946 1.00 44.40 ? 76  ASP C OD2 1 
ATOM   3968  N  N   . GLU D  1 104 ? 51.995  85.712  -6.515  1.00 31.60 ? 77  GLU C N   1 
ATOM   3969  C  CA  . GLU D  1 104 ? 52.823  86.367  -5.510  1.00 28.50 ? 77  GLU C CA  1 
ATOM   3970  C  C   . GLU D  1 104 ? 54.245  86.546  -6.025  1.00 27.29 ? 77  GLU C C   1 
ATOM   3971  O  O   . GLU D  1 104 ? 54.883  87.566  -5.747  1.00 33.48 ? 77  GLU C O   1 
ATOM   3972  C  CB  . GLU D  1 104 ? 52.782  85.574  -4.196  1.00 39.99 ? 77  GLU C CB  1 
ATOM   3973  C  CG  . GLU D  1 104 ? 51.354  85.460  -3.572  1.00 46.59 ? 77  GLU C CG  1 
ATOM   3974  C  CD  . GLU D  1 104 ? 50.612  86.806  -3.391  1.00 62.05 ? 77  GLU C CD  1 
ATOM   3975  O  OE1 . GLU D  1 104 ? 50.603  87.332  -2.252  1.00 72.25 ? 77  GLU C OE1 1 
ATOM   3976  O  OE2 . GLU D  1 104 ? 49.995  87.316  -4.366  1.00 54.70 ? 77  GLU C OE2 1 
ATOM   3977  N  N   . GLU D  1 105 ? 54.738  85.601  -6.822  1.00 24.18 ? 78  GLU C N   1 
ATOM   3978  C  CA  . GLU D  1 105 ? 56.029  85.743  -7.491  1.00 23.07 ? 78  GLU C CA  1 
ATOM   3979  C  C   . GLU D  1 105 ? 55.813  86.491  -8.803  1.00 21.02 ? 78  GLU C C   1 
ATOM   3980  O  O   . GLU D  1 105 ? 55.434  85.893  -9.810  1.00 22.54 ? 78  GLU C O   1 
ATOM   3981  C  CB  . GLU D  1 105 ? 56.651  84.377  -7.744  1.00 26.44 ? 78  GLU C CB  1 
ATOM   3982  C  CG  . GLU D  1 105 ? 58.004  84.401  -8.415  1.00 30.66 ? 78  GLU C CG  1 
ATOM   3983  C  CD  . GLU D  1 105 ? 59.143  84.703  -7.439  1.00 37.11 ? 78  GLU C CD  1 
ATOM   3984  O  OE1 . GLU D  1 105 ? 58.891  84.729  -6.213  1.00 40.67 ? 78  GLU C OE1 1 
ATOM   3985  O  OE2 . GLU D  1 105 ? 60.284  84.925  -7.900  1.00 35.47 ? 78  GLU C OE2 1 
ATOM   3986  N  N   . ARG D  1 106 ? 56.077  87.795  -8.799  1.00 22.98 ? 79  ARG C N   1 
ATOM   3987  C  CA  . ARG D  1 106 ? 55.929  88.597  -10.009 1.00 18.56 ? 79  ARG C CA  1 
ATOM   3988  C  C   . ARG D  1 106 ? 56.817  89.826  -9.886  1.00 21.07 ? 79  ARG C C   1 
ATOM   3989  O  O   . ARG D  1 106 ? 57.283  90.167  -8.796  1.00 21.30 ? 79  ARG C O   1 
ATOM   3990  C  CB  . ARG D  1 106 ? 54.464  89.010  -10.224 1.00 17.16 ? 79  ARG C CB  1 
ATOM   3991  C  CG  . ARG D  1 106 ? 53.923  89.828  -9.035  1.00 23.09 ? 79  ARG C CG  1 
ATOM   3992  C  CD  . ARG D  1 106 ? 52.547  90.450  -9.328  1.00 23.90 ? 79  ARG C CD  1 
ATOM   3993  N  NE  . ARG D  1 106 ? 52.679  91.815  -9.837  1.00 22.89 ? 79  ARG C NE  1 
ATOM   3994  C  CZ  . ARG D  1 106 ? 51.685  92.689  -9.907  1.00 19.62 ? 79  ARG C CZ  1 
ATOM   3995  N  NH1 . ARG D  1 106 ? 50.456  92.369  -9.521  1.00 18.58 ? 79  ARG C NH1 1 
ATOM   3996  N  NH2 . ARG D  1 106 ? 51.928  93.913  -10.383 1.00 18.79 ? 79  ARG C NH2 1 
ATOM   3997  N  N   . HIS D  1 107 ? 57.066  90.471  -11.023 1.00 15.83 ? 80  HIS C N   1 
ATOM   3998  C  CA  . HIS D  1 107 ? 57.639  91.809  -11.030 1.00 13.42 ? 80  HIS C CA  1 
ATOM   3999  C  C   . HIS D  1 107 ? 56.571  92.808  -10.604 1.00 21.11 ? 80  HIS C C   1 
ATOM   4000  O  O   . HIS D  1 107 ? 55.383  92.612  -10.871 1.00 19.79 ? 80  HIS C O   1 
ATOM   4001  C  CB  . HIS D  1 107 ? 58.180  92.183  -12.434 1.00 20.07 ? 80  HIS C CB  1 
ATOM   4002  C  CG  . HIS D  1 107 ? 59.195  91.219  -12.965 1.00 20.73 ? 80  HIS C CG  1 
ATOM   4003  N  ND1 . HIS D  1 107 ? 59.391  90.974  -14.301 1.00 25.43 ? 80  HIS C ND1 1 
ATOM   4004  C  CD2 . HIS D  1 107 ? 60.110  90.461  -12.307 1.00 23.31 ? 80  HIS C CD2 1 
ATOM   4005  C  CE1 . HIS D  1 107 ? 60.372  90.103  -14.454 1.00 20.03 ? 80  HIS C CE1 1 
ATOM   4006  N  NE2 . HIS D  1 107 ? 60.827  89.776  -13.256 1.00 19.66 ? 80  HIS C NE2 1 
ATOM   4007  N  N   . VAL D  1 108 ? 56.990  93.888  -9.931  1.00 13.42 ? 81  VAL C N   1 
ATOM   4008  C  CA  . VAL D  1 108 ? 56.024  94.951  -9.651  1.00 15.48 ? 81  VAL C CA  1 
ATOM   4009  C  C   . VAL D  1 108 ? 55.349  95.415  -10.953 1.00 14.15 ? 81  VAL C C   1 
ATOM   4010  O  O   . VAL D  1 108 ? 54.133  95.619  -10.995 1.00 18.59 ? 81  VAL C O   1 
ATOM   4011  C  CB  . VAL D  1 108 ? 56.688  96.123  -8.905  1.00 19.52 ? 81  VAL C CB  1 
ATOM   4012  C  CG1 . VAL D  1 108 ? 55.754  97.337  -8.860  1.00 18.36 ? 81  VAL C CG1 1 
ATOM   4013  C  CG2 . VAL D  1 108 ? 57.052  95.690  -7.464  1.00 21.06 ? 81  VAL C CG2 1 
ATOM   4014  N  N   . GLY D  1 109 ? 56.108  95.539  -12.030 1.00 16.53 ? 82  GLY C N   1 
ATOM   4015  C  CA  . GLY D  1 109 ? 55.501  96.000  -13.281 1.00 13.42 ? 82  GLY C CA  1 
ATOM   4016  C  C   . GLY D  1 109 ? 54.648  95.000  -14.051 1.00 22.16 ? 82  GLY C C   1 
ATOM   4017  O  O   . GLY D  1 109 ? 54.203  95.319  -15.165 1.00 18.63 ? 82  GLY C O   1 
ATOM   4018  N  N   . ASP D  1 110 ? 54.380  93.810  -13.508 1.00 16.54 ? 83  ASP C N   1 
ATOM   4019  C  CA  . ASP D  1 110 ? 53.686  92.746  -14.250 1.00 17.04 ? 83  ASP C CA  1 
ATOM   4020  C  C   . ASP D  1 110 ? 52.173  92.920  -14.196 1.00 18.12 ? 83  ASP C C   1 
ATOM   4021  O  O   . ASP D  1 110 ? 51.495  92.319  -13.366 1.00 20.49 ? 83  ASP C O   1 
ATOM   4022  C  CB  . ASP D  1 110 ? 54.070  91.378  -13.699 1.00 17.99 ? 83  ASP C CB  1 
ATOM   4023  C  CG  . ASP D  1 110 ? 55.464  90.979  -14.096 1.00 15.92 ? 83  ASP C CG  1 
ATOM   4024  O  OD1 . ASP D  1 110 ? 55.999  91.644  -15.000 1.00 26.98 ? 83  ASP C OD1 1 
ATOM   4025  O  OD2 . ASP D  1 110 ? 56.043  90.021  -13.533 1.00 14.61 ? 83  ASP C OD2 1 
ATOM   4026  N  N   . LEU D  1 111 ? 51.622  93.698  -15.136 1.00 16.42 ? 84  LEU C N   1 
ATOM   4027  C  CA  . LEU D  1 111 ? 50.179  93.889  -15.204 1.00 18.72 ? 84  LEU C CA  1 
ATOM   4028  C  C   . LEU D  1 111 ? 49.482  92.903  -16.150 1.00 18.75 ? 84  LEU C C   1 
ATOM   4029  O  O   . LEU D  1 111 ? 48.270  93.033  -16.374 1.00 23.00 ? 84  LEU C O   1 
ATOM   4030  C  CB  . LEU D  1 111 ? 49.855  95.334  -15.595 1.00 16.82 ? 84  LEU C CB  1 
ATOM   4031  C  CG  . LEU D  1 111 ? 50.342  96.378  -14.582 1.00 24.54 ? 84  LEU C CG  1 
ATOM   4032  C  CD1 . LEU D  1 111 ? 50.061  97.806  -15.073 1.00 21.97 ? 84  LEU C CD1 1 
ATOM   4033  C  CD2 . LEU D  1 111 ? 49.691  96.158  -13.209 1.00 21.62 ? 84  LEU C CD2 1 
ATOM   4034  N  N   . GLY D  1 112 ? 50.200  91.915  -16.685 1.00 13.42 ? 85  GLY C N   1 
ATOM   4035  C  CA  . GLY D  1 112 ? 49.557  90.839  -17.409 1.00 15.09 ? 85  GLY C CA  1 
ATOM   4036  C  C   . GLY D  1 112 ? 49.273  91.188  -18.860 1.00 18.10 ? 85  GLY C C   1 
ATOM   4037  O  O   . GLY D  1 112 ? 50.111  91.795  -19.530 1.00 15.33 ? 85  GLY C O   1 
ATOM   4038  N  N   . ASN D  1 113 ? 48.091  90.828  -19.345 1.00 13.42 ? 86  ASN C N   1 
ATOM   4039  C  CA  . ASN D  1 113 ? 47.722  91.087  -20.731 1.00 17.79 ? 86  ASN C CA  1 
ATOM   4040  C  C   . ASN D  1 113 ? 46.596  92.107  -20.805 1.00 19.62 ? 86  ASN C C   1 
ATOM   4041  O  O   . ASN D  1 113 ? 45.792  92.239  -19.871 1.00 18.51 ? 86  ASN C O   1 
ATOM   4042  C  CB  . ASN D  1 113 ? 47.265  89.801  -21.431 1.00 16.64 ? 86  ASN C CB  1 
ATOM   4043  C  CG  . ASN D  1 113 ? 48.411  88.879  -21.724 1.00 23.34 ? 86  ASN C CG  1 
ATOM   4044  O  OD1 . ASN D  1 113 ? 49.301  89.238  -22.491 1.00 14.78 ? 86  ASN C OD1 1 
ATOM   4045  N  ND2 . ASN D  1 113 ? 48.412  87.686  -21.109 1.00 18.26 ? 86  ASN C ND2 1 
ATOM   4046  N  N   . VAL D  1 114 ? 46.529  92.801  -21.941 1.00 18.00 ? 87  VAL C N   1 
ATOM   4047  C  CA  . VAL D  1 114 ? 45.328  93.507  -22.362 1.00 13.82 ? 87  VAL C CA  1 
ATOM   4048  C  C   . VAL D  1 114 ? 44.872  92.869  -23.670 1.00 19.88 ? 87  VAL C C   1 
ATOM   4049  O  O   . VAL D  1 114 ? 45.669  92.269  -24.397 1.00 22.02 ? 87  VAL C O   1 
ATOM   4050  C  CB  . VAL D  1 114 ? 45.559  95.032  -22.508 1.00 18.58 ? 87  VAL C CB  1 
ATOM   4051  C  CG1 . VAL D  1 114 ? 45.971  95.642  -21.145 1.00 13.93 ? 87  VAL C CG1 1 
ATOM   4052  C  CG2 . VAL D  1 114 ? 46.619  95.338  -23.561 1.00 18.52 ? 87  VAL C CG2 1 
ATOM   4053  N  N   . THR D  1 115 ? 43.580  92.978  -23.966 1.00 19.02 ? 88  THR C N   1 
ATOM   4054  C  CA  . THR D  1 115 ? 42.977  92.238  -25.073 1.00 17.15 ? 88  THR C CA  1 
ATOM   4055  C  C   . THR D  1 115 ? 42.390  93.243  -26.046 1.00 16.62 ? 88  THR C C   1 
ATOM   4056  O  O   . THR D  1 115 ? 41.556  94.069  -25.649 1.00 19.04 ? 88  THR C O   1 
ATOM   4057  C  CB  . THR D  1 115 ? 41.873  91.290  -24.575 1.00 19.92 ? 88  THR C CB  1 
ATOM   4058  O  OG1 . THR D  1 115 ? 42.444  90.263  -23.752 1.00 21.84 ? 88  THR C OG1 1 
ATOM   4059  C  CG2 . THR D  1 115 ? 41.176  90.620  -25.774 1.00 23.27 ? 88  THR C CG2 1 
ATOM   4060  N  N   . ALA D  1 116 ? 42.824  93.176  -27.311 1.00 16.40 ? 89  ALA C N   1 
ATOM   4061  C  CA  . ALA D  1 116 ? 42.278  94.024  -28.357 1.00 19.12 ? 89  ALA C CA  1 
ATOM   4062  C  C   . ALA D  1 116 ? 41.156  93.285  -29.073 1.00 19.80 ? 89  ALA C C   1 
ATOM   4063  O  O   . ALA D  1 116 ? 41.250  92.081  -29.307 1.00 21.46 ? 89  ALA C O   1 
ATOM   4064  C  CB  . ALA D  1 116 ? 43.357  94.428  -29.362 1.00 18.52 ? 89  ALA C CB  1 
ATOM   4065  N  N   . ASP D  1 117 ? 40.095  94.013  -29.410 1.00 22.13 ? 90  ASP C N   1 
ATOM   4066  C  CA  . ASP D  1 117 ? 38.930  93.430  -30.069 1.00 25.00 ? 90  ASP C CA  1 
ATOM   4067  C  C   . ASP D  1 117 ? 39.222  93.275  -31.567 1.00 28.22 ? 90  ASP C C   1 
ATOM   4068  O  O   . ASP D  1 117 ? 40.361  93.447  -32.020 1.00 24.38 ? 90  ASP C O   1 
ATOM   4069  C  CB  . ASP D  1 117 ? 37.671  94.253  -29.767 1.00 23.96 ? 90  ASP C CB  1 
ATOM   4070  C  CG  . ASP D  1 117 ? 37.727  95.691  -30.307 1.00 31.62 ? 90  ASP C CG  1 
ATOM   4071  O  OD1 . ASP D  1 117 ? 38.471  95.987  -31.265 1.00 24.50 ? 90  ASP C OD1 1 
ATOM   4072  O  OD2 . ASP D  1 117 ? 36.996  96.546  -29.764 1.00 30.27 ? 90  ASP C OD2 1 
ATOM   4073  N  N   . LYS D  1 118 ? 38.203  92.911  -32.358 1.00 26.58 ? 91  LYS C N   1 
ATOM   4074  C  CA  . LYS D  1 118 ? 38.449  92.672  -33.777 1.00 25.76 ? 91  LYS C CA  1 
ATOM   4075  C  C   . LYS D  1 118 ? 38.734  93.958  -34.547 1.00 30.29 ? 91  LYS C C   1 
ATOM   4076  O  O   . LYS D  1 118 ? 39.237  93.886  -35.672 1.00 30.92 ? 91  LYS C O   1 
ATOM   4077  C  CB  . LYS D  1 118 ? 37.262  91.954  -34.430 1.00 33.46 ? 91  LYS C CB  1 
ATOM   4078  C  CG  . LYS D  1 118 ? 35.934  92.691  -34.352 1.00 37.19 ? 91  LYS C CG  1 
ATOM   4079  C  CD  . LYS D  1 118 ? 34.885  91.987  -35.244 1.00 45.85 ? 91  LYS C CD  1 
ATOM   4080  C  CE  . LYS D  1 118 ? 33.491  92.616  -35.129 1.00 53.72 ? 91  LYS C CE  1 
ATOM   4081  N  NZ  . LYS D  1 118 ? 33.052  92.897  -33.728 1.00 54.43 ? 91  LYS C NZ  1 
ATOM   4082  N  N   . ASP D  1 119 ? 38.400  95.122  -33.989 1.00 28.18 ? 92  ASP C N   1 
ATOM   4083  C  CA  . ASP D  1 119 ? 38.766  96.398  -34.591 1.00 30.92 ? 92  ASP C CA  1 
ATOM   4084  C  C   . ASP D  1 119 ? 40.175  96.839  -34.217 1.00 28.06 ? 92  ASP C C   1 
ATOM   4085  O  O   . ASP D  1 119 ? 40.610  97.910  -34.650 1.00 23.76 ? 92  ASP C O   1 
ATOM   4086  C  CB  . ASP D  1 119 ? 37.772  97.489  -34.177 1.00 35.42 ? 92  ASP C CB  1 
ATOM   4087  C  CG  . ASP D  1 119 ? 36.332  97.172  -34.591 1.00 46.06 ? 92  ASP C CG  1 
ATOM   4088  O  OD1 . ASP D  1 119 ? 36.140  96.548  -35.659 1.00 39.94 ? 92  ASP C OD1 1 
ATOM   4089  O  OD2 . ASP D  1 119 ? 35.396  97.570  -33.862 1.00 49.34 ? 92  ASP C OD2 1 
ATOM   4090  N  N   . GLY D  1 120 ? 40.888  96.059  -33.410 1.00 24.03 ? 93  GLY C N   1 
ATOM   4091  C  CA  . GLY D  1 120 ? 42.209  96.458  -32.963 1.00 20.10 ? 93  GLY C CA  1 
ATOM   4092  C  C   . GLY D  1 120 ? 42.250  97.299  -31.702 1.00 22.29 ? 93  GLY C C   1 
ATOM   4093  O  O   . GLY D  1 120 ? 43.304  97.878  -31.397 1.00 22.46 ? 93  GLY C O   1 
ATOM   4094  N  N   . VAL D  1 121 ? 41.162  97.363  -30.943 1.00 19.92 ? 94  VAL C N   1 
ATOM   4095  C  CA  . VAL D  1 121 ? 41.038  98.291  -29.823 1.00 21.98 ? 94  VAL C CA  1 
ATOM   4096  C  C   . VAL D  1 121 ? 41.041  97.512  -28.518 1.00 20.97 ? 94  VAL C C   1 
ATOM   4097  O  O   . VAL D  1 121 ? 40.238  96.585  -28.330 1.00 23.82 ? 94  VAL C O   1 
ATOM   4098  C  CB  . VAL D  1 121 ? 39.769  99.152  -29.938 1.00 25.44 ? 94  VAL C CB  1 
ATOM   4099  C  CG1 . VAL D  1 121 ? 39.597  99.977  -28.679 1.00 22.65 ? 94  VAL C CG1 1 
ATOM   4100  C  CG2 . VAL D  1 121 ? 39.860  100.060 -31.161 1.00 25.14 ? 94  VAL C CG2 1 
ATOM   4101  N  N   . ALA D  1 122 ? 41.933  97.904  -27.610 1.00 21.12 ? 95  ALA C N   1 
ATOM   4102  C  CA  . ALA D  1 122 ? 42.000  97.340  -26.262 1.00 18.32 ? 95  ALA C CA  1 
ATOM   4103  C  C   . ALA D  1 122 ? 41.378  98.363  -25.325 1.00 19.75 ? 95  ALA C C   1 
ATOM   4104  O  O   . ALA D  1 122 ? 41.924  99.461  -25.148 1.00 23.07 ? 95  ALA C O   1 
ATOM   4105  C  CB  . ALA D  1 122 ? 43.447  97.030  -25.860 1.00 20.30 ? 95  ALA C CB  1 
ATOM   4106  N  N   . ASP D  1 123 ? 40.223  98.018  -24.754 1.00 20.57 ? 96  ASP C N   1 
ATOM   4107  C  CA  . ASP D  1 123 ? 39.568  98.868  -23.757 1.00 20.74 ? 96  ASP C CA  1 
ATOM   4108  C  C   . ASP D  1 123 ? 40.030  98.366  -22.397 1.00 20.45 ? 96  ASP C C   1 
ATOM   4109  O  O   . ASP D  1 123 ? 39.387  97.532  -21.771 1.00 22.07 ? 96  ASP C O   1 
ATOM   4110  C  CB  . ASP D  1 123 ? 38.051  98.832  -23.908 1.00 21.64 ? 96  ASP C CB  1 
ATOM   4111  C  CG  . ASP D  1 123 ? 37.572  99.561  -25.170 1.00 38.12 ? 96  ASP C CG  1 
ATOM   4112  O  OD1 . ASP D  1 123 ? 37.997  100.717 -25.387 1.00 31.46 ? 96  ASP C OD1 1 
ATOM   4113  O  OD2 . ASP D  1 123 ? 36.798  98.976  -25.959 1.00 40.63 ? 96  ASP C OD2 1 
ATOM   4114  N  N   . VAL D  1 124 ? 41.169  98.905  -21.948 1.00 21.24 ? 97  VAL C N   1 
ATOM   4115  C  CA  . VAL D  1 124 ? 41.888  98.370  -20.799 1.00 19.60 ? 97  VAL C CA  1 
ATOM   4116  C  C   . VAL D  1 124 ? 41.087  98.614  -19.531 1.00 19.05 ? 97  VAL C C   1 
ATOM   4117  O  O   . VAL D  1 124 ? 40.575  99.718  -19.307 1.00 21.62 ? 97  VAL C O   1 
ATOM   4118  C  CB  . VAL D  1 124 ? 43.277  99.020  -20.697 1.00 18.51 ? 97  VAL C CB  1 
ATOM   4119  C  CG1 . VAL D  1 124 ? 44.037  98.497  -19.464 1.00 18.66 ? 97  VAL C CG1 1 
ATOM   4120  C  CG2 . VAL D  1 124 ? 44.085  98.770  -21.969 1.00 17.12 ? 97  VAL C CG2 1 
ATOM   4121  N  N   . SER D  1 125 ? 40.989  97.590  -18.688 1.00 20.57 ? 98  SER C N   1 
ATOM   4122  C  CA  . SER D  1 125 ? 40.350  97.752  -17.379 1.00 18.71 ? 98  SER C CA  1 
ATOM   4123  C  C   . SER D  1 125 ? 41.029  96.777  -16.428 1.00 19.61 ? 98  SER C C   1 
ATOM   4124  O  O   . SER D  1 125 ? 40.748  95.576  -16.474 1.00 24.34 ? 98  SER C O   1 
ATOM   4125  C  CB  . SER D  1 125 ? 38.850  97.499  -17.463 1.00 25.85 ? 98  SER C CB  1 
ATOM   4126  O  OG  . SER D  1 125 ? 38.241  97.647  -16.193 1.00 34.58 ? 98  SER C OG  1 
ATOM   4127  N  N   . ILE D  1 126 ? 41.909  97.307  -15.566 1.00 22.33 ? 99  ILE C N   1 
ATOM   4128  C  CA  . ILE D  1 126 ? 42.752  96.529  -14.663 1.00 20.60 ? 99  ILE C CA  1 
ATOM   4129  C  C   . ILE D  1 126 ? 42.704  97.165  -13.277 1.00 20.77 ? 99  ILE C C   1 
ATOM   4130  O  O   . ILE D  1 126 ? 42.662  98.393  -13.144 1.00 20.49 ? 99  ILE C O   1 
ATOM   4131  C  CB  . ILE D  1 126 ? 44.203  96.464  -15.201 1.00 22.24 ? 99  ILE C CB  1 
ATOM   4132  C  CG1 . ILE D  1 126 ? 44.295  95.477  -16.366 1.00 21.85 ? 99  ILE C CG1 1 
ATOM   4133  C  CG2 . ILE D  1 126 ? 45.221  96.086  -14.118 1.00 24.81 ? 99  ILE C CG2 1 
ATOM   4134  C  CD1 . ILE D  1 126 ? 45.616  95.560  -17.122 1.00 20.61 ? 99  ILE C CD1 1 
ATOM   4135  N  N   . GLU D  1 127 ? 42.683  96.331  -12.247 1.00 20.75 ? 100 GLU C N   1 
ATOM   4136  C  CA  . GLU D  1 127 ? 42.889  96.779  -10.878 1.00 22.43 ? 100 GLU C CA  1 
ATOM   4137  C  C   . GLU D  1 127 ? 44.056  96.000  -10.298 1.00 21.05 ? 100 GLU C C   1 
ATOM   4138  O  O   . GLU D  1 127 ? 44.078  94.767  -10.365 1.00 24.39 ? 100 GLU C O   1 
ATOM   4139  C  CB  . GLU D  1 127 ? 41.628  96.571  -10.045 1.00 25.58 ? 100 GLU C CB  1 
ATOM   4140  C  CG  . GLU D  1 127 ? 41.689  97.163  -8.660  1.00 32.70 ? 100 GLU C CG  1 
ATOM   4141  C  CD  . GLU D  1 127 ? 40.410  96.878  -7.889  1.00 52.44 ? 100 GLU C CD  1 
ATOM   4142  O  OE1 . GLU D  1 127 ? 40.493  96.358  -6.753  1.00 53.61 ? 100 GLU C OE1 1 
ATOM   4143  O  OE2 . GLU D  1 127 ? 39.322  97.153  -8.442  1.00 54.98 ? 100 GLU C OE2 1 
ATOM   4144  N  N   . ASP D  1 128 ? 45.043  96.710  -9.770  1.00 22.11 ? 101 ASP C N   1 
ATOM   4145  C  CA  . ASP D  1 128 ? 46.239  96.052  -9.272  1.00 23.17 ? 101 ASP C CA  1 
ATOM   4146  C  C   . ASP D  1 128 ? 46.656  96.632  -7.930  1.00 23.11 ? 101 ASP C C   1 
ATOM   4147  O  O   . ASP D  1 128 ? 46.644  97.847  -7.740  1.00 23.13 ? 101 ASP C O   1 
ATOM   4148  C  CB  . ASP D  1 128 ? 47.397  96.181  -10.261 1.00 20.49 ? 101 ASP C CB  1 
ATOM   4149  C  CG  . ASP D  1 128 ? 48.548  95.263  -9.911  1.00 24.41 ? 101 ASP C CG  1 
ATOM   4150  O  OD1 . ASP D  1 128 ? 48.444  94.038  -10.167 1.00 30.12 ? 101 ASP C OD1 1 
ATOM   4151  O  OD2 . ASP D  1 128 ? 49.560  95.766  -9.394  1.00 24.42 ? 101 ASP C OD2 1 
ATOM   4152  N  N   A SER D  1 129 ? 47.057  95.766  -7.009  0.51 24.45 ? 102 SER C N   1 
ATOM   4153  N  N   B SER D  1 129 ? 47.059  95.752  -7.013  0.49 24.46 ? 102 SER C N   1 
ATOM   4154  C  CA  A SER D  1 129 ? 47.436  96.223  -5.682  0.51 27.64 ? 102 SER C CA  1 
ATOM   4155  C  CA  B SER D  1 129 ? 47.429  96.148  -5.660  0.49 28.17 ? 102 SER C CA  1 
ATOM   4156  C  C   A SER D  1 129 ? 48.934  96.180  -5.438  0.51 26.80 ? 102 SER C C   1 
ATOM   4157  C  C   B SER D  1 129 ? 48.928  96.066  -5.407  0.49 26.87 ? 102 SER C C   1 
ATOM   4158  O  O   A SER D  1 129 ? 49.375  96.510  -4.334  0.51 30.82 ? 102 SER C O   1 
ATOM   4159  O  O   B SER D  1 129 ? 49.360  96.229  -4.261  0.49 30.73 ? 102 SER C O   1 
ATOM   4160  C  CB  A SER D  1 129 ? 46.699  95.403  -4.621  0.51 30.14 ? 102 SER C CB  1 
ATOM   4161  C  CB  B SER D  1 129 ? 46.687  95.289  -4.631  0.49 30.08 ? 102 SER C CB  1 
ATOM   4162  O  OG  A SER D  1 129 ? 45.303  95.549  -4.803  0.51 32.02 ? 102 SER C OG  1 
ATOM   4163  O  OG  B SER D  1 129 ? 46.643  93.929  -5.028  0.49 32.19 ? 102 SER C OG  1 
ATOM   4164  N  N   . VAL D  1 130 ? 49.732  95.791  -6.430  1.00 23.40 ? 103 VAL C N   1 
ATOM   4165  C  CA  . VAL D  1 130 ? 51.178  95.739  -6.266  1.00 19.95 ? 103 VAL C CA  1 
ATOM   4166  C  C   . VAL D  1 130 ? 51.851  96.995  -6.805  1.00 22.66 ? 103 VAL C C   1 
ATOM   4167  O  O   . VAL D  1 130 ? 52.753  97.537  -6.163  1.00 22.08 ? 103 VAL C O   1 
ATOM   4168  C  CB  . VAL D  1 130 ? 51.755  94.452  -6.895  1.00 21.82 ? 103 VAL C CB  1 
ATOM   4169  C  CG1 . VAL D  1 130 ? 53.284  94.518  -6.963  1.00 23.58 ? 103 VAL C CG1 1 
ATOM   4170  C  CG2 . VAL D  1 130 ? 51.340  93.274  -6.050  1.00 23.03 ? 103 VAL C CG2 1 
ATOM   4171  N  N   . ILE D  1 131 ? 51.410  97.512  -7.962  1.00 23.62 ? 104 ILE C N   1 
ATOM   4172  C  CA  . ILE D  1 131 ? 51.865  98.851  -8.344  1.00 17.58 ? 104 ILE C CA  1 
ATOM   4173  C  C   . ILE D  1 131 ? 51.258  99.885  -7.393  1.00 16.27 ? 104 ILE C C   1 
ATOM   4174  O  O   . ILE D  1 131 ? 50.242  99.649  -6.742  1.00 22.83 ? 104 ILE C O   1 
ATOM   4175  C  CB  . ILE D  1 131 ? 51.502  99.164  -9.805  1.00 16.14 ? 104 ILE C CB  1 
ATOM   4176  C  CG1 . ILE D  1 131 ? 49.985  99.065  -10.003 1.00 20.17 ? 104 ILE C CG1 1 
ATOM   4177  C  CG2 . ILE D  1 131 ? 52.223  98.210  -10.748 1.00 18.27 ? 104 ILE C CG2 1 
ATOM   4178  C  CD1 . ILE D  1 131 ? 49.449  99.843  -11.267 1.00 17.05 ? 104 ILE C CD1 1 
ATOM   4179  N  N   . SER D  1 132 ? 51.890  101.055 -7.328  1.00 20.76 ? 105 SER C N   1 
ATOM   4180  C  CA  . SER D  1 132 ? 51.387  102.137 -6.495  1.00 20.68 ? 105 SER C CA  1 
ATOM   4181  C  C   . SER D  1 132 ? 51.731  103.437 -7.195  1.00 21.44 ? 105 SER C C   1 
ATOM   4182  O  O   . SER D  1 132 ? 52.626  103.489 -8.040  1.00 22.57 ? 105 SER C O   1 
ATOM   4183  C  CB  . SER D  1 132 ? 51.999  102.099 -5.083  1.00 18.61 ? 105 SER C CB  1 
ATOM   4184  O  OG  . SER D  1 132 ? 51.362  103.042 -4.224  1.00 22.39 ? 105 SER C OG  1 
ATOM   4185  N  N   . LEU D  1 133 ? 51.012  104.490 -6.847  1.00 20.38 ? 106 LEU C N   1 
ATOM   4186  C  CA  . LEU D  1 133 ? 51.382  105.830 -7.281  1.00 19.10 ? 106 LEU C CA  1 
ATOM   4187  C  C   . LEU D  1 133 ? 52.225  106.560 -6.234  1.00 27.35 ? 106 LEU C C   1 
ATOM   4188  O  O   . LEU D  1 133 ? 52.500  107.754 -6.388  1.00 26.29 ? 106 LEU C O   1 
ATOM   4189  C  CB  . LEU D  1 133 ? 50.115  106.625 -7.626  1.00 23.37 ? 106 LEU C CB  1 
ATOM   4190  C  CG  . LEU D  1 133 ? 49.227  106.017 -8.733  1.00 21.39 ? 106 LEU C CG  1 
ATOM   4191  C  CD1 . LEU D  1 133 ? 48.113  106.970 -9.169  1.00 24.76 ? 106 LEU C CD1 1 
ATOM   4192  C  CD2 . LEU D  1 133 ? 50.062  105.589 -9.946  1.00 19.28 ? 106 LEU C CD2 1 
ATOM   4193  N  N   . SER D  1 134 ? 52.662  105.871 -5.184  1.00 25.39 ? 107 SER C N   1 
ATOM   4194  C  CA  . SER D  1 134 ? 53.593  106.464 -4.230  1.00 31.10 ? 107 SER C CA  1 
ATOM   4195  C  C   . SER D  1 134 ? 54.438  105.363 -3.602  1.00 27.68 ? 107 SER C C   1 
ATOM   4196  O  O   . SER D  1 134 ? 54.161  104.168 -3.759  1.00 25.51 ? 107 SER C O   1 
ATOM   4197  C  CB  . SER D  1 134 ? 52.860  107.267 -3.143  1.00 28.50 ? 107 SER C CB  1 
ATOM   4198  O  OG  . SER D  1 134 ? 51.941  106.454 -2.425  1.00 33.42 ? 107 SER C OG  1 
ATOM   4199  N  N   . GLY D  1 135 ? 55.488  105.784 -2.892  1.00 27.49 ? 108 GLY C N   1 
ATOM   4200  C  CA  . GLY D  1 135 ? 56.295  104.831 -2.149  1.00 25.11 ? 108 GLY C CA  1 
ATOM   4201  C  C   . GLY D  1 135 ? 57.248  104.018 -3.011  1.00 26.11 ? 108 GLY C C   1 
ATOM   4202  O  O   . GLY D  1 135 ? 57.587  104.376 -4.148  1.00 27.06 ? 108 GLY C O   1 
ATOM   4203  N  N   . ASP D  1 136 ? 57.685  102.888 -2.440  1.00 23.62 ? 109 ASP C N   1 
ATOM   4204  C  CA  . ASP D  1 136 ? 58.728  102.064 -3.059  1.00 27.50 ? 109 ASP C CA  1 
ATOM   4205  C  C   . ASP D  1 136 ? 58.297  101.532 -4.414  1.00 23.05 ? 109 ASP C C   1 
ATOM   4206  O  O   . ASP D  1 136 ? 59.121  101.354 -5.322  1.00 23.80 ? 109 ASP C O   1 
ATOM   4207  C  CB  . ASP D  1 136 ? 59.044  100.870 -2.165  1.00 31.79 ? 109 ASP C CB  1 
ATOM   4208  C  CG  . ASP D  1 136 ? 60.034  101.195 -1.077  1.00 40.27 ? 109 ASP C CG  1 
ATOM   4209  O  OD1 . ASP D  1 136 ? 60.636  102.293 -1.120  1.00 37.87 ? 109 ASP C OD1 1 
ATOM   4210  O  OD2 . ASP D  1 136 ? 60.169  100.346 -0.167  1.00 35.38 ? 109 ASP C OD2 1 
ATOM   4211  N  N   . HIS D  1 137 ? 57.026  101.178 -4.533  1.00 20.55 ? 110 HIS C N   1 
ATOM   4212  C  CA  . HIS D  1 137 ? 56.510  100.580 -5.748  1.00 23.80 ? 110 HIS C CA  1 
ATOM   4213  C  C   . HIS D  1 137 ? 55.897  101.618 -6.668  1.00 22.47 ? 110 HIS C C   1 
ATOM   4214  O  O   . HIS D  1 137 ? 55.091  101.266 -7.536  1.00 21.82 ? 110 HIS C O   1 
ATOM   4215  C  CB  . HIS D  1 137 ? 55.501  99.495  -5.395  1.00 22.98 ? 110 HIS C CB  1 
ATOM   4216  C  CG  . HIS D  1 137 ? 56.122  98.314  -4.730  1.00 27.25 ? 110 HIS C CG  1 
ATOM   4217  N  ND1 . HIS D  1 137 ? 55.388  97.248  -4.259  1.00 38.83 ? 110 HIS C ND1 1 
ATOM   4218  C  CD2 . HIS D  1 137 ? 57.420  98.030  -4.464  1.00 32.49 ? 110 HIS C CD2 1 
ATOM   4219  C  CE1 . HIS D  1 137 ? 56.209  96.357  -3.729  1.00 34.72 ? 110 HIS C CE1 1 
ATOM   4220  N  NE2 . HIS D  1 137 ? 57.447  96.808  -3.843  1.00 33.72 ? 110 HIS C NE2 1 
ATOM   4221  N  N   . CYS D  1 138 ? 56.292  102.880 -6.509  1.00 16.75 ? 111 CYS C N   1 
ATOM   4222  C  CA  . CYS D  1 138 ? 55.689  103.962 -7.272  1.00 19.28 ? 111 CYS C CA  1 
ATOM   4223  C  C   . CYS D  1 138 ? 56.055  103.794 -8.747  1.00 15.08 ? 111 CYS C C   1 
ATOM   4224  O  O   . CYS D  1 138 ? 57.209  103.498 -9.079  1.00 21.29 ? 111 CYS C O   1 
ATOM   4225  C  CB  . CYS D  1 138 ? 56.172  105.307 -6.739  1.00 20.84 ? 111 CYS C CB  1 
ATOM   4226  S  SG  . CYS D  1 138 ? 55.592  106.719 -7.667  1.00 27.02 ? 111 CYS C SG  1 
ATOM   4227  N  N   . ILE D  1 139 ? 55.063  103.923 -9.630  1.00 17.39 ? 112 ILE C N   1 
ATOM   4228  C  CA  . ILE D  1 139 ? 55.326  103.760 -11.068 1.00 18.96 ? 112 ILE C CA  1 
ATOM   4229  C  C   . ILE D  1 139 ? 55.375  105.090 -11.797 1.00 20.22 ? 112 ILE C C   1 
ATOM   4230  O  O   . ILE D  1 139 ? 55.646  105.113 -13.014 1.00 16.01 ? 112 ILE C O   1 
ATOM   4231  C  CB  . ILE D  1 139 ? 54.294  102.830 -11.733 1.00 13.71 ? 112 ILE C CB  1 
ATOM   4232  C  CG1 . ILE D  1 139 ? 52.889  103.390 -11.591 1.00 18.06 ? 112 ILE C CG1 1 
ATOM   4233  C  CG2 . ILE D  1 139 ? 54.359  101.418 -11.153 1.00 16.98 ? 112 ILE C CG2 1 
ATOM   4234  C  CD1 . ILE D  1 139 ? 51.862  102.630 -12.375 1.00 23.16 ? 112 ILE C CD1 1 
ATOM   4235  N  N   A ILE D  1 140 ? 55.148  106.202 -11.083 0.39 20.92 ? 113 ILE C N   1 
ATOM   4236  N  N   B ILE D  1 140 ? 55.121  106.204 -11.104 0.61 20.91 ? 113 ILE C N   1 
ATOM   4237  C  CA  A ILE D  1 140 ? 55.309  107.538 -11.654 0.39 19.45 ? 113 ILE C CA  1 
ATOM   4238  C  CA  B ILE D  1 140 ? 55.222  107.515 -11.743 0.61 19.35 ? 113 ILE C CA  1 
ATOM   4239  C  C   A ILE D  1 140 ? 56.733  107.714 -12.145 0.39 21.09 ? 113 ILE C C   1 
ATOM   4240  C  C   B ILE D  1 140 ? 56.669  107.784 -12.121 0.61 21.16 ? 113 ILE C C   1 
ATOM   4241  O  O   A ILE D  1 140 ? 57.697  107.387 -11.442 0.39 18.52 ? 113 ILE C O   1 
ATOM   4242  O  O   B ILE D  1 140 ? 57.591  107.553 -11.330 0.61 18.25 ? 113 ILE C O   1 
ATOM   4243  C  CB  A ILE D  1 140 ? 54.966  108.612 -10.611 0.39 24.08 ? 113 ILE C CB  1 
ATOM   4244  C  CB  B ILE D  1 140 ? 54.658  108.601 -10.817 0.61 23.17 ? 113 ILE C CB  1 
ATOM   4245  C  CG1 A ILE D  1 140 ? 53.576  108.373 -10.045 0.39 23.88 ? 113 ILE C CG1 1 
ATOM   4246  C  CG1 B ILE D  1 140 ? 53.141  108.508 -10.786 0.61 22.11 ? 113 ILE C CG1 1 
ATOM   4247  C  CG2 A ILE D  1 140 ? 55.070  110.012 -11.211 0.39 20.48 ? 113 ILE C CG2 1 
ATOM   4248  C  CG2 B ILE D  1 140 ? 55.116  109.999 -11.245 0.61 20.42 ? 113 ILE C CG2 1 
ATOM   4249  C  CD1 A ILE D  1 140 ? 52.509  108.469 -11.078 0.39 23.44 ? 113 ILE C CD1 1 
ATOM   4250  C  CD1 B ILE D  1 140 ? 52.513  109.362 -9.706  0.61 24.17 ? 113 ILE C CD1 1 
ATOM   4251  N  N   . GLY D  1 141 ? 56.877  108.255 -13.350 1.00 18.44 ? 114 GLY C N   1 
ATOM   4252  C  CA  . GLY D  1 141 ? 58.197  108.458 -13.899 1.00 18.14 ? 114 GLY C CA  1 
ATOM   4253  C  C   . GLY D  1 141 ? 58.797  107.236 -14.563 1.00 15.41 ? 114 GLY C C   1 
ATOM   4254  O  O   . GLY D  1 141 ? 59.954  107.289 -15.000 1.00 18.32 ? 114 GLY C O   1 
ATOM   4255  N  N   . ARG D  1 142 ? 58.072  106.136 -14.620 1.00 15.42 ? 115 ARG C N   1 
ATOM   4256  C  CA  . ARG D  1 142 ? 58.523  104.949 -15.308 1.00 14.23 ? 115 ARG C CA  1 
ATOM   4257  C  C   . ARG D  1 142 ? 57.755  104.850 -16.622 1.00 16.25 ? 115 ARG C C   1 
ATOM   4258  O  O   . ARG D  1 142 ? 56.983  105.741 -16.969 1.00 17.56 ? 115 ARG C O   1 
ATOM   4259  C  CB  . ARG D  1 142 ? 58.372  103.728 -14.395 1.00 15.74 ? 115 ARG C CB  1 
ATOM   4260  C  CG  . ARG D  1 142 ? 58.992  104.001 -12.980 1.00 19.94 ? 115 ARG C CG  1 
ATOM   4261  C  CD  . ARG D  1 142 ? 59.301  102.738 -12.215 1.00 21.03 ? 115 ARG C CD  1 
ATOM   4262  N  NE  . ARG D  1 142 ? 59.830  103.041 -10.883 1.00 22.38 ? 115 ARG C NE  1 
ATOM   4263  C  CZ  . ARG D  1 142 ? 61.123  103.060 -10.580 1.00 23.15 ? 115 ARG C CZ  1 
ATOM   4264  N  NH1 . ARG D  1 142 ? 62.051  102.799 -11.491 1.00 21.53 ? 115 ARG C NH1 1 
ATOM   4265  N  NH2 . ARG D  1 142 ? 61.496  103.345 -9.330  1.00 24.56 ? 115 ARG C NH2 1 
ATOM   4266  N  N   . THR D  1 143 ? 57.972  103.774 -17.358 1.00 16.35 ? 116 THR C N   1 
ATOM   4267  C  CA  . THR D  1 143 ? 57.451  103.641 -18.724 1.00 13.42 ? 116 THR C CA  1 
ATOM   4268  C  C   . THR D  1 143 ? 56.457  102.494 -18.788 1.00 18.40 ? 116 THR C C   1 
ATOM   4269  O  O   . THR D  1 143 ? 56.798  101.354 -18.451 1.00 21.65 ? 116 THR C O   1 
ATOM   4270  C  CB  . THR D  1 143 ? 58.576  103.391 -19.725 1.00 18.73 ? 116 THR C CB  1 
ATOM   4271  O  OG1 . THR D  1 143 ? 59.467  104.520 -19.759 1.00 21.13 ? 116 THR C OG1 1 
ATOM   4272  C  CG2 . THR D  1 143 ? 57.990  103.171 -21.147 1.00 13.42 ? 116 THR C CG2 1 
ATOM   4273  N  N   . LEU D  1 144 ? 55.253  102.776 -19.261 1.00 15.22 ? 117 LEU C N   1 
ATOM   4274  C  CA  . LEU D  1 144 ? 54.294  101.731 -19.581 1.00 13.62 ? 117 LEU C CA  1 
ATOM   4275  C  C   . LEU D  1 144 ? 54.506  101.305 -21.033 1.00 13.84 ? 117 LEU C C   1 
ATOM   4276  O  O   . LEU D  1 144 ? 54.679  102.158 -21.899 1.00 13.42 ? 117 LEU C O   1 
ATOM   4277  C  CB  . LEU D  1 144 ? 52.871  102.247 -19.399 1.00 13.42 ? 117 LEU C CB  1 
ATOM   4278  C  CG  . LEU D  1 144 ? 51.704  101.291 -19.645 1.00 15.10 ? 117 LEU C CG  1 
ATOM   4279  C  CD1 . LEU D  1 144 ? 51.655  100.201 -18.569 1.00 19.45 ? 117 LEU C CD1 1 
ATOM   4280  C  CD2 . LEU D  1 144 ? 50.382  102.099 -19.691 1.00 13.42 ? 117 LEU C CD2 1 
ATOM   4281  N  N   . VAL D  1 145 ? 54.496  99.996  -21.287 1.00 14.85 ? 118 VAL C N   1 
ATOM   4282  C  CA  . VAL D  1 145 ? 54.760  99.448  -22.626 1.00 13.42 ? 118 VAL C CA  1 
ATOM   4283  C  C   . VAL D  1 145 ? 53.681  98.430  -22.972 1.00 17.17 ? 118 VAL C C   1 
ATOM   4284  O  O   . VAL D  1 145 ? 53.357  97.562  -22.157 1.00 17.01 ? 118 VAL C O   1 
ATOM   4285  C  CB  . VAL D  1 145 ? 56.144  98.761  -22.693 1.00 19.98 ? 118 VAL C CB  1 
ATOM   4286  C  CG1 . VAL D  1 145 ? 56.408  98.202  -24.107 1.00 15.95 ? 118 VAL C CG1 1 
ATOM   4287  C  CG2 . VAL D  1 145 ? 57.250  99.721  -22.254 1.00 19.71 ? 118 VAL C CG2 1 
ATOM   4288  N  N   . VAL D  1 146 ? 53.155  98.491  -24.193 1.00 14.17 ? 119 VAL C N   1 
ATOM   4289  C  CA  . VAL D  1 146 ? 52.288  97.438  -24.693 1.00 13.42 ? 119 VAL C CA  1 
ATOM   4290  C  C   . VAL D  1 146 ? 53.086  96.644  -25.719 1.00 17.77 ? 119 VAL C C   1 
ATOM   4291  O  O   . VAL D  1 146 ? 53.800  97.225  -26.556 1.00 14.95 ? 119 VAL C O   1 
ATOM   4292  C  CB  . VAL D  1 146 ? 50.963  97.988  -25.260 1.00 17.32 ? 119 VAL C CB  1 
ATOM   4293  C  CG1 . VAL D  1 146 ? 51.182  98.967  -26.438 1.00 13.51 ? 119 VAL C CG1 1 
ATOM   4294  C  CG2 . VAL D  1 146 ? 50.040  96.847  -25.653 1.00 20.86 ? 119 VAL C CG2 1 
ATOM   4295  N  N   . HIS D  1 147 ? 53.007  95.323  -25.617 1.00 15.76 ? 120 HIS C N   1 
ATOM   4296  C  CA  . HIS D  1 147 ? 53.900  94.431  -26.345 1.00 20.38 ? 120 HIS C CA  1 
ATOM   4297  C  C   . HIS D  1 147 ? 53.210  93.748  -27.521 1.00 13.42 ? 120 HIS C C   1 
ATOM   4298  O  O   . HIS D  1 147 ? 51.989  93.742  -27.671 1.00 16.17 ? 120 HIS C O   1 
ATOM   4299  C  CB  . HIS D  1 147 ? 54.494  93.378  -25.405 1.00 13.42 ? 120 HIS C CB  1 
ATOM   4300  C  CG  . HIS D  1 147 ? 55.541  93.926  -24.484 1.00 18.62 ? 120 HIS C CG  1 
ATOM   4301  N  ND1 . HIS D  1 147 ? 56.892  93.824  -24.749 1.00 20.48 ? 120 HIS C ND1 1 
ATOM   4302  C  CD2 . HIS D  1 147 ? 55.437  94.568  -23.293 1.00 14.82 ? 120 HIS C CD2 1 
ATOM   4303  C  CE1 . HIS D  1 147 ? 57.577  94.381  -23.762 1.00 19.59 ? 120 HIS C CE1 1 
ATOM   4304  N  NE2 . HIS D  1 147 ? 56.719  94.854  -22.874 1.00 16.27 ? 120 HIS C NE2 1 
ATOM   4305  N  N   . GLU D  1 148 ? 54.052  93.121  -28.339 1.00 18.06 ? 121 GLU C N   1 
ATOM   4306  C  CA  . GLU D  1 148 ? 53.641  92.537  -29.613 1.00 16.76 ? 121 GLU C CA  1 
ATOM   4307  C  C   . GLU D  1 148 ? 52.834  91.253  -29.451 1.00 20.65 ? 121 GLU C C   1 
ATOM   4308  O  O   . GLU D  1 148 ? 51.896  91.014  -30.230 1.00 18.78 ? 121 GLU C O   1 
ATOM   4309  C  CB  . GLU D  1 148 ? 54.910  92.315  -30.439 1.00 23.14 ? 121 GLU C CB  1 
ATOM   4310  C  CG  . GLU D  1 148 ? 54.813  91.426  -31.640 1.00 30.17 ? 121 GLU C CG  1 
ATOM   4311  C  CD  . GLU D  1 148 ? 56.200  91.047  -32.171 1.00 42.87 ? 121 GLU C CD  1 
ATOM   4312  O  OE1 . GLU D  1 148 ? 57.107  90.653  -31.370 1.00 32.99 ? 121 GLU C OE1 1 
ATOM   4313  O  OE2 . GLU D  1 148 ? 56.378  91.162  -33.402 1.00 53.71 ? 121 GLU C OE2 1 
ATOM   4314  N  N   . LYS D  1 149 ? 53.160  90.427  -28.449 1.00 19.02 ? 122 LYS C N   1 
ATOM   4315  C  CA  . LYS D  1 149 ? 52.523  89.130  -28.255 1.00 20.56 ? 122 LYS C CA  1 
ATOM   4316  C  C   . LYS D  1 149 ? 51.927  88.999  -26.858 1.00 21.66 ? 122 LYS C C   1 
ATOM   4317  O  O   . LYS D  1 149 ? 52.123  89.848  -25.985 1.00 18.66 ? 122 LYS C O   1 
ATOM   4318  C  CB  . LYS D  1 149 ? 53.516  87.978  -28.482 1.00 27.93 ? 122 LYS C CB  1 
ATOM   4319  C  CG  . LYS D  1 149 ? 54.532  88.168  -29.581 1.00 33.03 ? 122 LYS C CG  1 
ATOM   4320  C  CD  . LYS D  1 149 ? 55.385  86.904  -29.694 1.00 36.46 ? 122 LYS C CD  1 
ATOM   4321  C  CE  . LYS D  1 149 ? 56.453  87.043  -30.772 1.00 43.98 ? 122 LYS C CE  1 
ATOM   4322  N  NZ  . LYS D  1 149 ? 57.797  86.593  -30.282 1.00 51.71 ? 122 LYS C NZ  1 
ATOM   4323  N  N   . ALA D  1 150 ? 51.223  87.886  -26.646 1.00 18.18 ? 123 ALA C N   1 
ATOM   4324  C  CA  . ALA D  1 150 ? 50.683  87.590  -25.323 1.00 23.85 ? 123 ALA C CA  1 
ATOM   4325  C  C   . ALA D  1 150 ? 51.799  87.357  -24.311 1.00 22.39 ? 123 ALA C C   1 
ATOM   4326  O  O   . ALA D  1 150 ? 52.839  86.764  -24.608 1.00 22.08 ? 123 ALA C O   1 
ATOM   4327  C  CB  . ALA D  1 150 ? 49.761  86.362  -25.373 1.00 24.01 ? 123 ALA C CB  1 
ATOM   4328  N  N   . ASP D  1 151 ? 51.585  87.867  -23.112 1.00 18.07 ? 124 ASP C N   1 
ATOM   4329  C  CA  . ASP D  1 151 ? 52.427  87.549  -21.969 1.00 17.25 ? 124 ASP C CA  1 
ATOM   4330  C  C   . ASP D  1 151 ? 52.011  86.173  -21.459 1.00 19.86 ? 124 ASP C C   1 
ATOM   4331  O  O   . ASP D  1 151 ? 50.822  85.952  -21.197 1.00 19.08 ? 124 ASP C O   1 
ATOM   4332  C  CB  . ASP D  1 151 ? 52.222  88.651  -20.924 1.00 15.20 ? 124 ASP C CB  1 
ATOM   4333  C  CG  . ASP D  1 151 ? 53.008  88.442  -19.637 1.00 21.44 ? 124 ASP C CG  1 
ATOM   4334  O  OD1 . ASP D  1 151 ? 53.614  87.372  -19.421 1.00 16.91 ? 124 ASP C OD1 1 
ATOM   4335  O  OD2 . ASP D  1 151 ? 53.030  89.404  -18.828 1.00 23.99 ? 124 ASP C OD2 1 
ATOM   4336  N  N   . ASP D  1 152 ? 52.954  85.232  -21.345 1.00 15.98 ? 125 ASP C N   1 
ATOM   4337  C  CA  . ASP D  1 152 ? 52.562  83.904  -20.876 1.00 18.27 ? 125 ASP C CA  1 
ATOM   4338  C  C   . ASP D  1 152 ? 52.493  83.811  -19.356 1.00 17.61 ? 125 ASP C C   1 
ATOM   4339  O  O   . ASP D  1 152 ? 52.312  82.710  -18.809 1.00 18.79 ? 125 ASP C O   1 
ATOM   4340  C  CB  . ASP D  1 152 ? 53.475  82.812  -21.480 1.00 20.53 ? 125 ASP C CB  1 
ATOM   4341  C  CG  . ASP D  1 152 ? 54.925  82.880  -21.001 1.00 18.12 ? 125 ASP C CG  1 
ATOM   4342  O  OD1 . ASP D  1 152 ? 55.202  83.453  -19.928 1.00 19.43 ? 125 ASP C OD1 1 
ATOM   4343  O  OD2 . ASP D  1 152 ? 55.803  82.324  -21.715 1.00 22.98 ? 125 ASP C OD2 1 
ATOM   4344  N  N   . LEU D  1 153 ? 52.588  84.950  -18.677 1.00 19.72 ? 126 LEU C N   1 
ATOM   4345  C  CA  . LEU D  1 153 ? 52.417  85.068  -17.220 1.00 16.17 ? 126 LEU C CA  1 
ATOM   4346  C  C   . LEU D  1 153 ? 53.432  84.216  -16.460 1.00 21.98 ? 126 LEU C C   1 
ATOM   4347  O  O   . LEU D  1 153 ? 53.194  83.798  -15.320 1.00 15.06 ? 126 LEU C O   1 
ATOM   4348  C  CB  . LEU D  1 153 ? 50.989  84.717  -16.789 1.00 21.57 ? 126 LEU C CB  1 
ATOM   4349  C  CG  . LEU D  1 153 ? 49.882  85.365  -17.637 1.00 21.15 ? 126 LEU C CG  1 
ATOM   4350  C  CD1 . LEU D  1 153 ? 48.516  85.036  -17.082 1.00 26.51 ? 126 LEU C CD1 1 
ATOM   4351  C  CD2 . LEU D  1 153 ? 50.090  86.871  -17.761 1.00 20.19 ? 126 LEU C CD2 1 
ATOM   4352  N  N   . GLY D  1 154 ? 54.583  83.980  -17.079 1.00 21.13 ? 127 GLY C N   1 
ATOM   4353  C  CA  . GLY D  1 154 ? 55.653  83.244  -16.437 1.00 21.50 ? 127 GLY C CA  1 
ATOM   4354  C  C   . GLY D  1 154 ? 55.508  81.743  -16.507 1.00 20.80 ? 127 GLY C C   1 
ATOM   4355  O  O   . GLY D  1 154 ? 56.271  81.036  -15.843 1.00 22.02 ? 127 GLY C O   1 
ATOM   4356  N  N   . LYS D  1 155 ? 54.556  81.234  -17.286 1.00 17.79 ? 128 LYS C N   1 
ATOM   4357  C  CA  . LYS D  1 155 ? 54.237  79.811  -17.305 1.00 19.30 ? 128 LYS C CA  1 
ATOM   4358  C  C   . LYS D  1 155 ? 54.762  79.126  -18.557 1.00 18.91 ? 128 LYS C C   1 
ATOM   4359  O  O   . LYS D  1 155 ? 54.342  78.005  -18.870 1.00 23.30 ? 128 LYS C O   1 
ATOM   4360  C  CB  . LYS D  1 155 ? 52.722  79.617  -17.164 1.00 17.38 ? 128 LYS C CB  1 
ATOM   4361  C  CG  . LYS D  1 155 ? 52.202  80.266  -15.878 1.00 26.98 ? 128 LYS C CG  1 
ATOM   4362  C  CD  . LYS D  1 155 ? 50.679  80.237  -15.717 1.00 36.44 ? 128 LYS C CD  1 
ATOM   4363  C  CE  . LYS D  1 155 ? 50.128  78.830  -15.816 1.00 39.62 ? 128 LYS C CE  1 
ATOM   4364  N  NZ  . LYS D  1 155 ? 48.631  78.804  -15.728 1.00 53.53 ? 128 LYS C NZ  1 
ATOM   4365  N  N   . GLY D  1 156 ? 55.679  79.781  -19.272 1.00 19.68 ? 129 GLY C N   1 
ATOM   4366  C  CA  . GLY D  1 156 ? 56.133  79.308  -20.573 1.00 17.52 ? 129 GLY C CA  1 
ATOM   4367  C  C   . GLY D  1 156 ? 57.226  78.261  -20.525 1.00 21.00 ? 129 GLY C C   1 
ATOM   4368  O  O   . GLY D  1 156 ? 57.476  77.612  -21.544 1.00 20.32 ? 129 GLY C O   1 
ATOM   4369  N  N   . GLY D  1 157 ? 57.868  78.075  -19.372 1.00 15.57 ? 130 GLY C N   1 
ATOM   4370  C  CA  . GLY D  1 157 ? 58.875  77.032  -19.188 1.00 13.42 ? 130 GLY C CA  1 
ATOM   4371  C  C   . GLY D  1 157 ? 60.218  77.285  -19.851 1.00 22.26 ? 130 GLY C C   1 
ATOM   4372  O  O   . GLY D  1 157 ? 61.116  76.426  -19.768 1.00 20.98 ? 130 GLY C O   1 
ATOM   4373  N  N   . ASN D  1 158 ? 60.411  78.424  -20.495 1.00 21.97 ? 131 ASN C N   1 
ATOM   4374  C  CA  . ASN D  1 158 ? 61.715  78.732  -21.052 1.00 17.78 ? 131 ASN C CA  1 
ATOM   4375  C  C   . ASN D  1 158 ? 62.292  79.926  -20.305 1.00 25.06 ? 131 ASN C C   1 
ATOM   4376  O  O   . ASN D  1 158 ? 61.621  80.560  -19.491 1.00 22.93 ? 131 ASN C O   1 
ATOM   4377  C  CB  . ASN D  1 158 ? 61.646  78.972  -22.573 1.00 20.03 ? 131 ASN C CB  1 
ATOM   4378  C  CG  . ASN D  1 158 ? 60.829  80.201  -22.959 1.00 23.58 ? 131 ASN C CG  1 
ATOM   4379  O  OD1 . ASN D  1 158 ? 60.146  80.782  -22.135 1.00 24.55 ? 131 ASN C OD1 1 
ATOM   4380  N  ND2 . ASN D  1 158 ? 60.892  80.581  -24.238 1.00 22.59 ? 131 ASN C ND2 1 
ATOM   4381  N  N   . GLU D  1 159 ? 63.563  80.215  -20.575 1.00 22.83 ? 132 GLU C N   1 
ATOM   4382  C  CA  . GLU D  1 159 ? 64.231  81.313  -19.885 1.00 22.54 ? 132 GLU C CA  1 
ATOM   4383  C  C   . GLU D  1 159 ? 63.496  82.627  -20.096 1.00 24.81 ? 132 GLU C C   1 
ATOM   4384  O  O   . GLU D  1 159 ? 63.353  83.426  -19.165 1.00 24.71 ? 132 GLU C O   1 
ATOM   4385  C  CB  . GLU D  1 159 ? 65.672  81.457  -20.375 1.00 29.78 ? 132 GLU C CB  1 
ATOM   4386  C  CG  . GLU D  1 159 ? 66.475  80.169  -20.386 1.00 46.23 ? 132 GLU C CG  1 
ATOM   4387  C  CD  . GLU D  1 159 ? 67.949  80.411  -20.708 1.00 61.23 ? 132 GLU C CD  1 
ATOM   4388  O  OE1 . GLU D  1 159 ? 68.592  79.496  -21.272 1.00 57.02 ? 132 GLU C OE1 1 
ATOM   4389  O  OE2 . GLU D  1 159 ? 68.447  81.531  -20.435 1.00 54.52 ? 132 GLU C OE2 1 
ATOM   4390  N  N   . GLU D  1 160 ? 63.035  82.870  -21.318 1.00 24.04 ? 133 GLU C N   1 
ATOM   4391  C  CA  . GLU D  1 160 ? 62.411  84.151  -21.629 1.00 23.48 ? 133 GLU C CA  1 
ATOM   4392  C  C   . GLU D  1 160 ? 61.129  84.338  -20.834 1.00 26.46 ? 133 GLU C C   1 
ATOM   4393  O  O   . GLU D  1 160 ? 60.772  85.470  -20.490 1.00 23.99 ? 133 GLU C O   1 
ATOM   4394  C  CB  . GLU D  1 160 ? 62.142  84.246  -23.129 1.00 24.86 ? 133 GLU C CB  1 
ATOM   4395  C  CG  . GLU D  1 160 ? 61.997  85.669  -23.663 1.00 28.86 ? 133 GLU C CG  1 
ATOM   4396  C  CD  . GLU D  1 160 ? 63.207  86.534  -23.337 1.00 41.06 ? 133 GLU C CD  1 
ATOM   4397  O  OE1 . GLU D  1 160 ? 64.320  86.197  -23.784 1.00 42.51 ? 133 GLU C OE1 1 
ATOM   4398  O  OE2 . GLU D  1 160 ? 63.049  87.530  -22.591 1.00 42.57 ? 133 GLU C OE2 1 
ATOM   4399  N  N   . SER D  1 161 ? 60.444  83.242  -20.506 1.00 22.56 ? 134 SER C N   1 
ATOM   4400  C  CA  . SER D  1 161 ? 59.185  83.365  -19.791 1.00 18.34 ? 134 SER C CA  1 
ATOM   4401  C  C   . SER D  1 161 ? 59.405  83.994  -18.425 1.00 23.60 ? 134 SER C C   1 
ATOM   4402  O  O   . SER D  1 161 ? 58.599  84.822  -17.978 1.00 22.04 ? 134 SER C O   1 
ATOM   4403  C  CB  . SER D  1 161 ? 58.516  81.996  -19.664 1.00 19.92 ? 134 SER C CB  1 
ATOM   4404  O  OG  . SER D  1 161 ? 57.322  82.120  -18.930 1.00 22.23 ? 134 SER C OG  1 
ATOM   4405  N  N   . THR D  1 162 ? 60.515  83.639  -17.758 1.00 21.93 ? 135 THR C N   1 
ATOM   4406  C  CA  . THR D  1 162 ? 60.818  84.138  -16.424 1.00 20.16 ? 135 THR C CA  1 
ATOM   4407  C  C   . THR D  1 162 ? 61.301  85.574  -16.425 1.00 26.74 ? 135 THR C C   1 
ATOM   4408  O  O   . THR D  1 162 ? 61.494  86.132  -15.344 1.00 23.88 ? 135 THR C O   1 
ATOM   4409  C  CB  . THR D  1 162 ? 61.909  83.277  -15.754 1.00 27.79 ? 135 THR C CB  1 
ATOM   4410  O  OG1 . THR D  1 162 ? 63.180  83.578  -16.355 1.00 29.91 ? 135 THR C OG1 1 
ATOM   4411  C  CG2 . THR D  1 162 ? 61.646  81.816  -15.964 1.00 29.26 ? 135 THR C CG2 1 
ATOM   4412  N  N   . LYS D  1 163 ? 61.542  86.165  -17.592 1.00 24.12 ? 136 LYS C N   1 
ATOM   4413  C  CA  . LYS D  1 163 ? 61.985  87.550  -17.711 1.00 24.50 ? 136 LYS C CA  1 
ATOM   4414  C  C   . LYS D  1 163 ? 60.928  88.477  -18.299 1.00 18.98 ? 136 LYS C C   1 
ATOM   4415  O  O   . LYS D  1 163 ? 60.607  89.523  -17.712 1.00 24.71 ? 136 LYS C O   1 
ATOM   4416  C  CB  . LYS D  1 163 ? 63.250  87.588  -18.575 1.00 23.35 ? 136 LYS C CB  1 
ATOM   4417  C  CG  . LYS D  1 163 ? 64.403  86.839  -17.890 1.00 33.09 ? 136 LYS C CG  1 
ATOM   4418  C  CD  . LYS D  1 163 ? 65.743  87.454  -18.160 1.00 39.42 ? 136 LYS C CD  1 
ATOM   4419  C  CE  . LYS D  1 163 ? 66.359  86.881  -19.409 1.00 43.13 ? 136 LYS C CE  1 
ATOM   4420  N  NZ  . LYS D  1 163 ? 67.466  87.767  -19.890 1.00 57.51 ? 136 LYS C NZ  1 
ATOM   4421  N  N   . THR D  1 164 ? 60.364  88.121  -19.447 1.00 22.15 ? 137 THR C N   1 
ATOM   4422  C  CA  . THR D  1 164 ? 59.458  88.985  -20.188 1.00 22.48 ? 137 THR C CA  1 
ATOM   4423  C  C   . THR D  1 164 ? 58.100  88.366  -20.449 1.00 22.84 ? 137 THR C C   1 
ATOM   4424  O  O   . THR D  1 164 ? 57.265  89.009  -21.096 1.00 24.43 ? 137 THR C O   1 
ATOM   4425  C  CB  . THR D  1 164 ? 60.053  89.340  -21.558 1.00 23.00 ? 137 THR C CB  1 
ATOM   4426  O  OG1 . THR D  1 164 ? 60.142  88.144  -22.348 1.00 23.16 ? 137 THR C OG1 1 
ATOM   4427  C  CG2 . THR D  1 164 ? 61.430  89.979  -21.419 1.00 30.71 ? 137 THR C CG2 1 
ATOM   4428  N  N   . GLY D  1 165 ? 57.885  87.109  -20.067 1.00 22.97 ? 138 GLY C N   1 
ATOM   4429  C  CA  . GLY D  1 165 ? 56.661  86.447  -20.453 1.00 17.55 ? 138 GLY C CA  1 
ATOM   4430  C  C   . GLY D  1 165 ? 56.564  86.104  -21.922 1.00 15.91 ? 138 GLY C C   1 
ATOM   4431  O  O   . GLY D  1 165 ? 55.472  85.760  -22.388 1.00 17.23 ? 138 GLY C O   1 
ATOM   4432  N  N   . ASN D  1 166 ? 57.677  86.167  -22.668 1.00 20.77 ? 139 ASN C N   1 
ATOM   4433  C  CA  . ASN D  1 166 ? 57.677  85.935  -24.124 1.00 19.01 ? 139 ASN C CA  1 
ATOM   4434  C  C   . ASN D  1 166 ? 56.765  86.922  -24.855 1.00 18.43 ? 139 ASN C C   1 
ATOM   4435  O  O   . ASN D  1 166 ? 56.235  86.613  -25.927 1.00 20.64 ? 139 ASN C O   1 
ATOM   4436  C  CB  . ASN D  1 166 ? 57.284  84.487  -24.476 1.00 22.13 ? 139 ASN C CB  1 
ATOM   4437  C  CG  . ASN D  1 166 ? 58.353  83.479  -24.099 1.00 24.95 ? 139 ASN C CG  1 
ATOM   4438  O  OD1 . ASN D  1 166 ? 59.399  83.426  -24.722 1.00 24.93 ? 139 ASN C OD1 1 
ATOM   4439  N  ND2 . ASN D  1 166 ? 58.097  82.682  -23.057 1.00 21.76 ? 139 ASN C ND2 1 
ATOM   4440  N  N   . ALA D  1 167 ? 56.585  88.130  -24.303 1.00 17.97 ? 140 ALA C N   1 
ATOM   4441  C  CA  . ALA D  1 167 ? 55.661  89.094  -24.902 1.00 20.72 ? 140 ALA C CA  1 
ATOM   4442  C  C   . ALA D  1 167 ? 56.250  89.836  -26.103 1.00 21.52 ? 140 ALA C C   1 
ATOM   4443  O  O   . ALA D  1 167 ? 55.530  90.599  -26.753 1.00 15.79 ? 140 ALA C O   1 
ATOM   4444  C  CB  . ALA D  1 167 ? 55.181  90.110  -23.848 1.00 15.81 ? 140 ALA C CB  1 
ATOM   4445  N  N   . GLY D  1 168 ? 57.526  89.647  -26.421 1.00 23.31 ? 141 GLY C N   1 
ATOM   4446  C  CA  . GLY D  1 168 ? 58.005  90.110  -27.719 1.00 22.72 ? 141 GLY C CA  1 
ATOM   4447  C  C   . GLY D  1 168 ? 58.227  91.614  -27.757 1.00 23.80 ? 141 GLY C C   1 
ATOM   4448  O  O   . GLY D  1 168 ? 58.446  92.255  -26.728 1.00 20.41 ? 141 GLY C O   1 
ATOM   4449  N  N   . SER D  1 169 ? 58.144  92.185  -28.966 1.00 22.12 ? 142 SER C N   1 
ATOM   4450  C  CA  . SER D  1 169 ? 58.586  93.558  -29.205 1.00 22.55 ? 142 SER C CA  1 
ATOM   4451  C  C   . SER D  1 169 ? 57.720  94.591  -28.488 1.00 19.06 ? 142 SER C C   1 
ATOM   4452  O  O   . SER D  1 169 ? 56.562  94.349  -28.146 1.00 20.22 ? 142 SER C O   1 
ATOM   4453  C  CB  . SER D  1 169 ? 58.575  93.882  -30.706 1.00 27.50 ? 142 SER C CB  1 
ATOM   4454  O  OG  . SER D  1 169 ? 59.461  93.022  -31.382 1.00 37.66 ? 142 SER C OG  1 
ATOM   4455  N  N   . ARG D  1 170 ? 58.287  95.780  -28.331 1.00 16.44 ? 143 ARG C N   1 
ATOM   4456  C  CA  . ARG D  1 170 ? 57.608  96.915  -27.711 1.00 20.53 ? 143 ARG C CA  1 
ATOM   4457  C  C   . ARG D  1 170 ? 56.915  97.738  -28.791 1.00 20.34 ? 143 ARG C C   1 
ATOM   4458  O  O   . ARG D  1 170 ? 57.579  98.403  -29.590 1.00 22.07 ? 143 ARG C O   1 
ATOM   4459  C  CB  . ARG D  1 170 ? 58.630  97.737  -26.935 1.00 20.33 ? 143 ARG C CB  1 
ATOM   4460  C  CG  . ARG D  1 170 ? 59.453  96.832  -25.990 1.00 19.96 ? 143 ARG C CG  1 
ATOM   4461  C  CD  . ARG D  1 170 ? 60.570  97.563  -25.237 1.00 22.40 ? 143 ARG C CD  1 
ATOM   4462  N  NE  . ARG D  1 170 ? 61.324  96.615  -24.417 1.00 22.52 ? 143 ARG C NE  1 
ATOM   4463  C  CZ  . ARG D  1 170 ? 62.065  96.934  -23.359 1.00 26.89 ? 143 ARG C CZ  1 
ATOM   4464  N  NH1 . ARG D  1 170 ? 62.191  98.190  -22.944 1.00 21.55 ? 143 ARG C NH1 1 
ATOM   4465  N  NH2 . ARG D  1 170 ? 62.672  95.967  -22.678 1.00 22.30 ? 143 ARG C NH2 1 
ATOM   4466  N  N   . LEU D  1 171 ? 55.582  97.691  -28.823 1.00 16.41 ? 144 LEU C N   1 
ATOM   4467  C  CA  . LEU D  1 171 ? 54.835  98.370  -29.882 1.00 14.65 ? 144 LEU C CA  1 
ATOM   4468  C  C   . LEU D  1 171 ? 54.611  99.849  -29.584 1.00 18.68 ? 144 LEU C C   1 
ATOM   4469  O  O   . LEU D  1 171 ? 54.587  100.672 -30.502 1.00 17.82 ? 144 LEU C O   1 
ATOM   4470  C  CB  . LEU D  1 171 ? 53.488  97.679  -30.097 1.00 15.66 ? 144 LEU C CB  1 
ATOM   4471  C  CG  . LEU D  1 171 ? 53.606  96.201  -30.476 1.00 25.00 ? 144 LEU C CG  1 
ATOM   4472  C  CD1 . LEU D  1 171 ? 52.237  95.629  -30.795 1.00 22.18 ? 144 LEU C CD1 1 
ATOM   4473  C  CD2 . LEU D  1 171 ? 54.608  95.993  -31.635 1.00 24.93 ? 144 LEU C CD2 1 
ATOM   4474  N  N   . ALA D  1 172 ? 54.387  100.210 -28.324 1.00 14.84 ? 145 ALA C N   1 
ATOM   4475  C  CA  . ALA D  1 172 ? 54.163  101.611 -28.010 1.00 13.42 ? 145 ALA C CA  1 
ATOM   4476  C  C   . ALA D  1 172 ? 54.455  101.783 -26.531 1.00 17.15 ? 145 ALA C C   1 
ATOM   4477  O  O   . ALA D  1 172 ? 54.339  100.827 -25.768 1.00 14.84 ? 145 ALA C O   1 
ATOM   4478  C  CB  . ALA D  1 172 ? 52.731  102.057 -28.313 1.00 13.42 ? 145 ALA C CB  1 
ATOM   4479  N  N   . CYS D  1 173 ? 54.811  103.001 -26.137 1.00 13.42 ? 146 CYS C N   1 
ATOM   4480  C  CA  . CYS D  1 173 ? 55.158  103.231 -24.734 1.00 13.42 ? 146 CYS C CA  1 
ATOM   4481  C  C   . CYS D  1 173 ? 55.043  104.715 -24.429 1.00 17.84 ? 146 CYS C C   1 
ATOM   4482  O  O   . CYS D  1 173 ? 54.944  105.555 -25.324 1.00 16.86 ? 146 CYS C O   1 
ATOM   4483  C  CB  . CYS D  1 173 ? 56.577  102.764 -24.417 1.00 17.75 ? 146 CYS C CB  1 
ATOM   4484  S  SG  . CYS D  1 173 ? 57.853  103.596 -25.392 1.00 25.97 ? 146 CYS C SG  1 
ATOM   4485  N  N   . GLY D  1 174 ? 55.106  105.032 -23.145 1.00 19.29 ? 147 GLY C N   1 
ATOM   4486  C  CA  . GLY D  1 174 ? 55.085  106.416 -22.731 1.00 16.71 ? 147 GLY C CA  1 
ATOM   4487  C  C   . GLY D  1 174 ? 55.511  106.472 -21.284 1.00 15.16 ? 147 GLY C C   1 
ATOM   4488  O  O   . GLY D  1 174 ? 55.406  105.479 -20.555 1.00 16.55 ? 147 GLY C O   1 
ATOM   4489  N  N   . VAL D  1 175 ? 55.984  107.634 -20.880 1.00 16.92 ? 148 VAL C N   1 
ATOM   4490  C  CA  . VAL D  1 175 ? 56.333  107.837 -19.475 1.00 19.34 ? 148 VAL C CA  1 
ATOM   4491  C  C   . VAL D  1 175 ? 55.071  108.125 -18.680 1.00 18.22 ? 148 VAL C C   1 
ATOM   4492  O  O   . VAL D  1 175 ? 54.194  108.875 -19.122 1.00 16.10 ? 148 VAL C O   1 
ATOM   4493  C  CB  . VAL D  1 175 ? 57.363  108.976 -19.327 1.00 19.16 ? 148 VAL C CB  1 
ATOM   4494  C  CG1 . VAL D  1 175 ? 57.781  109.128 -17.860 1.00 17.30 ? 148 VAL C CG1 1 
ATOM   4495  C  CG2 . VAL D  1 175 ? 58.561  108.703 -20.199 1.00 23.30 ? 148 VAL C CG2 1 
ATOM   4496  N  N   . ILE D  1 176 ? 54.985  107.543 -17.484 1.00 19.09 ? 149 ILE C N   1 
ATOM   4497  C  CA  . ILE D  1 176 ? 53.827  107.718 -16.616 1.00 18.13 ? 149 ILE C CA  1 
ATOM   4498  C  C   . ILE D  1 176 ? 53.995  109.032 -15.857 1.00 18.81 ? 149 ILE C C   1 
ATOM   4499  O  O   . ILE D  1 176 ? 54.970  109.215 -15.119 1.00 21.29 ? 149 ILE C O   1 
ATOM   4500  C  CB  . ILE D  1 176 ? 53.678  106.525 -15.655 1.00 15.34 ? 149 ILE C CB  1 
ATOM   4501  C  CG1 . ILE D  1 176 ? 53.489  105.221 -16.452 1.00 13.52 ? 149 ILE C CG1 1 
ATOM   4502  C  CG2 . ILE D  1 176 ? 52.470  106.717 -14.715 1.00 20.04 ? 149 ILE C CG2 1 
ATOM   4503  C  CD1 . ILE D  1 176 ? 53.678  103.919 -15.629 1.00 17.22 ? 149 ILE C CD1 1 
ATOM   4504  N  N   . GLY D  1 177 ? 53.043  109.947 -16.035 1.00 17.33 ? 150 GLY C N   1 
ATOM   4505  C  CA  . GLY D  1 177 ? 53.156  111.267 -15.447 1.00 19.77 ? 150 GLY C CA  1 
ATOM   4506  C  C   . GLY D  1 177 ? 52.069  111.579 -14.433 1.00 22.00 ? 150 GLY C C   1 
ATOM   4507  O  O   . GLY D  1 177 ? 50.983  111.001 -14.484 1.00 18.94 ? 150 GLY C O   1 
ATOM   4508  N  N   A ILE D  1 178 ? 52.351  112.498 -13.508 0.62 20.49 ? 151 ILE C N   1 
ATOM   4509  N  N   B ILE D  1 178 ? 52.351  112.501 -13.508 0.38 20.56 ? 151 ILE C N   1 
ATOM   4510  C  CA  A ILE D  1 178 ? 51.340  112.918 -12.547 0.62 21.49 ? 151 ILE C CA  1 
ATOM   4511  C  CA  B ILE D  1 178 ? 51.343  112.912 -12.539 0.38 21.51 ? 151 ILE C CA  1 
ATOM   4512  C  C   A ILE D  1 178 ? 50.211  113.643 -13.267 0.62 24.07 ? 151 ILE C C   1 
ATOM   4513  C  C   B ILE D  1 178 ? 50.216  113.651 -13.252 0.38 24.08 ? 151 ILE C C   1 
ATOM   4514  O  O   A ILE D  1 178 ? 50.445  114.521 -14.108 0.62 24.02 ? 151 ILE C O   1 
ATOM   4515  O  O   B ILE D  1 178 ? 50.454  114.529 -14.093 0.38 24.03 ? 151 ILE C O   1 
ATOM   4516  C  CB  A ILE D  1 178 ? 51.973  113.814 -11.470 0.62 21.58 ? 151 ILE C CB  1 
ATOM   4517  C  CB  B ILE D  1 178 ? 51.977  113.772 -11.427 0.38 21.74 ? 151 ILE C CB  1 
ATOM   4518  C  CG1 A ILE D  1 178 ? 53.083  113.053 -10.757 0.62 20.78 ? 151 ILE C CG1 1 
ATOM   4519  C  CG1 B ILE D  1 178 ? 50.898  114.310 -10.498 0.38 28.09 ? 151 ILE C CG1 1 
ATOM   4520  C  CG2 A ILE D  1 178 ? 50.904  114.284 -10.479 0.62 28.19 ? 151 ILE C CG2 1 
ATOM   4521  C  CG2 B ILE D  1 178 ? 52.736  114.946 -11.983 0.38 22.90 ? 151 ILE C CG2 1 
ATOM   4522  C  CD1 A ILE D  1 178 ? 53.923  113.917 -9.819  0.62 29.37 ? 151 ILE C CD1 1 
ATOM   4523  C  CD1 B ILE D  1 178 ? 50.185  113.242 -9.801  0.38 28.35 ? 151 ILE C CD1 1 
ATOM   4524  N  N   . ALA D  1 179 ? 48.975  113.292 -12.926 1.00 20.97 ? 152 ALA C N   1 
ATOM   4525  C  CA  . ALA D  1 179 ? 47.801  113.878 -13.546 1.00 24.28 ? 152 ALA C CA  1 
ATOM   4526  C  C   . ALA D  1 179 ? 47.001  114.660 -12.510 1.00 33.18 ? 152 ALA C C   1 
ATOM   4527  O  O   . ALA D  1 179 ? 47.119  114.431 -11.300 1.00 28.82 ? 152 ALA C O   1 
ATOM   4528  C  CB  . ALA D  1 179 ? 46.917  112.797 -14.191 1.00 22.60 ? 152 ALA C CB  1 
ATOM   4529  N  N   . GLN D  1 180 ? 46.179  115.588 -12.992 1.00 32.17 ? 153 GLN C N   1 
ATOM   4530  C  CA  . GLN D  1 180 ? 45.401  116.439 -12.086 1.00 42.67 ? 153 GLN C CA  1 
ATOM   4531  C  C   . GLN D  1 180 ? 44.254  115.659 -11.458 1.00 54.25 ? 153 GLN C C   1 
ATOM   4532  O  O   . GLN D  1 180 ? 43.591  114.874 -12.137 1.00 58.20 ? 153 GLN C O   1 
ATOM   4533  C  CB  . GLN D  1 180 ? 44.855  117.673 -12.812 1.00 37.61 ? 153 GLN C CB  1 
ATOM   4534  C  CG  . GLN D  1 180 ? 44.225  118.707 -11.865 1.00 46.77 ? 153 GLN C CG  1 
ATOM   4535  C  CD  . GLN D  1 180 ? 43.629  119.905 -12.597 1.00 48.50 ? 153 GLN C CD  1 
ATOM   4536  O  OE1 . GLN D  1 180 ? 42.933  119.753 -13.603 1.00 47.70 ? 153 GLN C OE1 1 
ATOM   4537  N  NE2 . GLN D  1 180 ? 43.906  121.106 -12.091 1.00 49.55 ? 153 GLN C NE2 1 
ATOM   4538  O  OXT . GLN D  1 180 ? 43.961  115.800 -10.267 1.00 61.49 ? 153 GLN C OXT 1 
ATOM   4539  N  N   . MET E  1 27  ? 65.999  52.376  3.153   1.00 48.52 ? 0   MET H N   1 
ATOM   4540  C  CA  . MET E  1 27  ? 66.486  53.620  3.743   1.00 55.66 ? 0   MET H CA  1 
ATOM   4541  C  C   . MET E  1 27  ? 67.056  53.416  5.154   1.00 50.48 ? 0   MET H C   1 
ATOM   4542  O  O   . MET E  1 27  ? 68.157  53.893  5.453   1.00 54.34 ? 0   MET H O   1 
ATOM   4543  C  CB  . MET E  1 27  ? 65.367  54.676  3.768   1.00 44.01 ? 0   MET H CB  1 
ATOM   4544  N  N   . ALA E  1 28  ? 66.316  52.717  6.019   1.00 41.96 ? 1   ALA H N   1 
ATOM   4545  C  CA  . ALA E  1 28  ? 66.764  52.523  7.398   1.00 39.13 ? 1   ALA H CA  1 
ATOM   4546  C  C   . ALA E  1 28  ? 67.968  51.591  7.453   1.00 33.23 ? 1   ALA H C   1 
ATOM   4547  O  O   . ALA E  1 28  ? 67.912  50.471  6.943   1.00 34.52 ? 1   ALA H O   1 
ATOM   4548  C  CB  . ALA E  1 28  ? 65.633  51.948  8.245   1.00 37.02 ? 1   ALA H CB  1 
ATOM   4549  N  N   . THR E  1 29  ? 69.058  52.046  8.085   1.00 32.32 ? 2   THR H N   1 
ATOM   4550  C  CA  . THR E  1 29  ? 70.242  51.205  8.245   1.00 29.12 ? 2   THR H CA  1 
ATOM   4551  C  C   . THR E  1 29  ? 70.428  50.705  9.664   1.00 33.40 ? 2   THR H C   1 
ATOM   4552  O  O   . THR E  1 29  ? 71.227  49.790  9.877   1.00 28.39 ? 2   THR H O   1 
ATOM   4553  C  CB  . THR E  1 29  ? 71.526  51.944  7.826   1.00 30.04 ? 2   THR H CB  1 
ATOM   4554  O  OG1 . THR E  1 29  ? 71.697  53.115  8.627   1.00 35.40 ? 2   THR H OG1 1 
ATOM   4555  C  CG2 . THR E  1 29  ? 71.456  52.349  6.345   1.00 35.12 ? 2   THR H CG2 1 
ATOM   4556  N  N   . LYS E  1 30  ? 69.733  51.288  10.636  1.00 22.68 ? 3   LYS H N   1 
ATOM   4557  C  CA  . LYS E  1 30  ? 69.854  50.867  12.027  1.00 19.49 ? 3   LYS H CA  1 
ATOM   4558  C  C   . LYS E  1 30  ? 68.473  50.792  12.658  1.00 25.59 ? 3   LYS H C   1 
ATOM   4559  O  O   . LYS E  1 30  ? 67.591  51.598  12.340  1.00 24.15 ? 3   LYS H O   1 
ATOM   4560  C  CB  . LYS E  1 30  ? 70.759  51.814  12.818  1.00 27.59 ? 3   LYS H CB  1 
ATOM   4561  C  CG  . LYS E  1 30  ? 72.194  51.782  12.309  1.00 37.52 ? 3   LYS H CG  1 
ATOM   4562  C  CD  . LYS E  1 30  ? 73.256  51.958  13.382  1.00 40.56 ? 3   LYS H CD  1 
ATOM   4563  C  CE  . LYS E  1 30  ? 73.623  53.414  13.631  1.00 46.13 ? 3   LYS H CE  1 
ATOM   4564  N  NZ  . LYS E  1 30  ? 73.654  53.736  15.097  1.00 51.70 ? 3   LYS H NZ  1 
ATOM   4565  N  N   . ALA E  1 31  ? 68.281  49.797  13.524  1.00 21.64 ? 4   ALA H N   1 
ATOM   4566  C  CA  . ALA E  1 31  ? 67.059  49.654  14.295  1.00 20.59 ? 4   ALA H CA  1 
ATOM   4567  C  C   . ALA E  1 31  ? 67.446  49.252  15.707  1.00 23.60 ? 4   ALA H C   1 
ATOM   4568  O  O   . ALA E  1 31  ? 68.598  48.909  15.980  1.00 23.30 ? 4   ALA H O   1 
ATOM   4569  C  CB  . ALA E  1 31  ? 66.095  48.631  13.681  1.00 19.22 ? 4   ALA H CB  1 
ATOM   4570  N  N   . VAL E  1 32  ? 66.480  49.320  16.622  1.00 21.60 ? 5   VAL H N   1 
ATOM   4571  C  CA  . VAL E  1 32  ? 66.740  48.955  18.012  1.00 20.40 ? 5   VAL H CA  1 
ATOM   4572  C  C   . VAL E  1 32  ? 65.436  48.452  18.585  1.00 25.28 ? 5   VAL H C   1 
ATOM   4573  O  O   . VAL E  1 32  ? 64.354  48.802  18.106  1.00 22.19 ? 5   VAL H O   1 
ATOM   4574  C  CB  . VAL E  1 32  ? 67.317  50.136  18.835  1.00 25.75 ? 5   VAL H CB  1 
ATOM   4575  C  CG1 . VAL E  1 32  ? 66.255  51.199  19.066  1.00 22.44 ? 5   VAL H CG1 1 
ATOM   4576  C  CG2 . VAL E  1 32  ? 67.877  49.648  20.174  1.00 26.99 ? 5   VAL H CG2 1 
ATOM   4577  N  N   . CYS E  1 33  ? 65.536  47.610  19.604  1.00 21.75 ? 6   CYS H N   1 
ATOM   4578  C  CA  . CYS E  1 33  ? 64.348  47.070  20.229  1.00 18.80 ? 6   CYS H CA  1 
ATOM   4579  C  C   . CYS E  1 33  ? 64.598  46.951  21.725  1.00 26.56 ? 6   CYS H C   1 
ATOM   4580  O  O   . CYS E  1 33  ? 65.632  46.417  22.131  1.00 21.68 ? 6   CYS H O   1 
ATOM   4581  C  CB  . CYS E  1 33  ? 64.000  45.708  19.631  1.00 20.08 ? 6   CYS H CB  1 
ATOM   4582  S  SG  . CYS E  1 33  ? 62.554  44.927  20.352  1.00 25.16 ? 6   CYS H SG  1 
ATOM   4583  N  N   . VAL E  1 34  ? 63.667  47.451  22.538  1.00 20.13 ? 7   VAL H N   1 
ATOM   4584  C  CA  . VAL E  1 34  ? 63.742  47.327  23.996  1.00 18.59 ? 7   VAL H CA  1 
ATOM   4585  C  C   . VAL E  1 34  ? 62.752  46.249  24.399  1.00 25.28 ? 7   VAL H C   1 
ATOM   4586  O  O   . VAL E  1 34  ? 61.544  46.407  24.212  1.00 21.60 ? 7   VAL H O   1 
ATOM   4587  C  CB  . VAL E  1 34  ? 63.435  48.646  24.717  1.00 23.91 ? 7   VAL H CB  1 
ATOM   4588  C  CG1 . VAL E  1 34  ? 63.399  48.426  26.268  1.00 21.20 ? 7   VAL H CG1 1 
ATOM   4589  C  CG2 . VAL E  1 34  ? 64.464  49.695  24.362  1.00 23.37 ? 7   VAL H CG2 1 
ATOM   4590  N  N   . LEU E  1 35  ? 63.263  45.149  24.945  1.00 21.88 ? 8   LEU H N   1 
ATOM   4591  C  CA  . LEU E  1 35  ? 62.438  44.030  25.380  1.00 20.24 ? 8   LEU H CA  1 
ATOM   4592  C  C   . LEU E  1 35  ? 62.020  44.194  26.839  1.00 22.86 ? 8   LEU H C   1 
ATOM   4593  O  O   . LEU E  1 35  ? 62.867  44.385  27.716  1.00 23.19 ? 8   LEU H O   1 
ATOM   4594  C  CB  . LEU E  1 35  ? 63.212  42.724  25.223  1.00 25.46 ? 8   LEU H CB  1 
ATOM   4595  C  CG  . LEU E  1 35  ? 63.625  42.416  23.787  1.00 31.00 ? 8   LEU H CG  1 
ATOM   4596  C  CD1 . LEU E  1 35  ? 64.838  41.492  23.779  1.00 34.45 ? 8   LEU H CD1 1 
ATOM   4597  C  CD2 . LEU E  1 35  ? 62.456  41.791  23.095  1.00 25.05 ? 8   LEU H CD2 1 
ATOM   4598  N  N   . LYS E  1 36  ? 60.715  44.082  27.088  1.00 23.48 ? 9   LYS H N   1 
ATOM   4599  C  CA  . LYS E  1 36  ? 60.131  44.145  28.419  1.00 30.53 ? 9   LYS H CA  1 
ATOM   4600  C  C   . LYS E  1 36  ? 58.979  43.160  28.468  1.00 25.97 ? 9   LYS H C   1 
ATOM   4601  O  O   . LYS E  1 36  ? 58.347  42.880  27.451  1.00 25.21 ? 9   LYS H O   1 
ATOM   4602  C  CB  . LYS E  1 36  ? 59.599  45.546  28.776  1.00 26.23 ? 9   LYS H CB  1 
ATOM   4603  C  CG  . LYS E  1 36  ? 60.634  46.665  28.709  1.00 35.48 ? 9   LYS H CG  1 
ATOM   4604  C  CD  . LYS E  1 36  ? 61.606  46.600  29.877  1.00 46.01 ? 9   LYS H CD  1 
ATOM   4605  C  CE  . LYS E  1 36  ? 62.625  47.734  29.826  1.00 47.83 ? 9   LYS H CE  1 
ATOM   4606  N  NZ  . LYS E  1 36  ? 63.979  47.216  29.427  1.00 44.83 ? 9   LYS H NZ  1 
ATOM   4607  N  N   . GLY E  1 37  ? 58.701  42.641  29.662  1.00 24.25 ? 10  GLY H N   1 
ATOM   4608  C  CA  . GLY E  1 37  ? 57.566  41.742  29.800  1.00 23.44 ? 10  GLY H CA  1 
ATOM   4609  C  C   . GLY E  1 37  ? 56.925  41.828  31.176  1.00 28.15 ? 10  GLY H C   1 
ATOM   4610  O  O   . GLY E  1 37  ? 57.193  42.769  31.926  1.00 30.05 ? 10  GLY H O   1 
ATOM   4611  N  N   . ASP E  1 38  ? 56.073  40.862  31.515  1.00 31.18 ? 11  ASP H N   1 
ATOM   4612  C  CA  . ASP E  1 38  ? 55.435  40.879  32.824  1.00 35.94 ? 11  ASP H CA  1 
ATOM   4613  C  C   . ASP E  1 38  ? 56.345  40.369  33.929  1.00 33.61 ? 11  ASP H C   1 
ATOM   4614  O  O   . ASP E  1 38  ? 56.094  40.664  35.102  1.00 44.68 ? 11  ASP H O   1 
ATOM   4615  C  CB  . ASP E  1 38  ? 54.143  40.058  32.795  1.00 41.18 ? 11  ASP H CB  1 
ATOM   4616  C  CG  . ASP E  1 38  ? 53.018  40.781  32.082  1.00 57.26 ? 11  ASP H CG  1 
ATOM   4617  O  OD1 . ASP E  1 38  ? 53.043  42.037  32.053  1.00 60.23 ? 11  ASP H OD1 1 
ATOM   4618  O  OD2 . ASP E  1 38  ? 52.112  40.103  31.553  1.00 61.73 ? 11  ASP H OD2 1 
ATOM   4619  N  N   . GLY E  1 39  ? 57.387  39.619  33.588  1.00 36.97 ? 12  GLY H N   1 
ATOM   4620  C  CA  . GLY E  1 39  ? 58.350  39.165  34.560  1.00 30.49 ? 12  GLY H CA  1 
ATOM   4621  C  C   . GLY E  1 39  ? 59.594  40.026  34.532  1.00 32.79 ? 12  GLY H C   1 
ATOM   4622  O  O   . GLY E  1 39  ? 59.544  41.219  34.215  1.00 31.74 ? 12  GLY H O   1 
ATOM   4623  N  N   . PRO E  1 40  ? 60.743  39.437  34.861  1.00 28.65 ? 13  PRO H N   1 
ATOM   4624  C  CA  . PRO E  1 40  ? 61.984  40.214  34.980  1.00 27.19 ? 13  PRO H CA  1 
ATOM   4625  C  C   . PRO E  1 40  ? 62.839  40.290  33.722  1.00 26.18 ? 13  PRO H C   1 
ATOM   4626  O  O   . PRO E  1 40  ? 63.944  40.847  33.789  1.00 31.40 ? 13  PRO H O   1 
ATOM   4627  C  CB  . PRO E  1 40  ? 62.732  39.445  36.080  1.00 29.13 ? 13  PRO H CB  1 
ATOM   4628  C  CG  . PRO E  1 40  ? 62.328  38.026  35.837  1.00 28.50 ? 13  PRO H CG  1 
ATOM   4629  C  CD  . PRO E  1 40  ? 60.914  38.044  35.324  1.00 30.94 ? 13  PRO H CD  1 
ATOM   4630  N  N   . VAL E  1 41  ? 62.392  39.750  32.596  1.00 27.38 ? 14  VAL H N   1 
ATOM   4631  C  CA  . VAL E  1 41  ? 63.248  39.700  31.412  1.00 25.87 ? 14  VAL H CA  1 
ATOM   4632  C  C   . VAL E  1 41  ? 63.308  41.082  30.773  1.00 28.35 ? 14  VAL H C   1 
ATOM   4633  O  O   . VAL E  1 41  ? 62.274  41.688  30.468  1.00 28.12 ? 14  VAL H O   1 
ATOM   4634  C  CB  . VAL E  1 41  ? 62.753  38.639  30.418  1.00 27.15 ? 14  VAL H CB  1 
ATOM   4635  C  CG1 . VAL E  1 41  ? 63.583  38.686  29.142  1.00 25.66 ? 14  VAL H CG1 1 
ATOM   4636  C  CG2 . VAL E  1 41  ? 62.812  37.245  31.056  1.00 29.66 ? 14  VAL H CG2 1 
ATOM   4637  N  N   . GLN E  1 42  ? 64.527  41.579  30.578  1.00 27.31 ? 15  GLN H N   1 
ATOM   4638  C  CA  . GLN E  1 42  ? 64.816  42.902  30.040  1.00 32.13 ? 15  GLN H CA  1 
ATOM   4639  C  C   . GLN E  1 42  ? 65.977  42.793  29.071  1.00 29.90 ? 15  GLN H C   1 
ATOM   4640  O  O   . GLN E  1 42  ? 66.937  42.072  29.344  1.00 31.58 ? 15  GLN H O   1 
ATOM   4641  C  CB  . GLN E  1 42  ? 65.238  43.899  31.127  1.00 31.23 ? 15  GLN H CB  1 
ATOM   4642  C  CG  . GLN E  1 42  ? 64.207  44.274  32.134  1.00 39.40 ? 15  GLN H CG  1 
ATOM   4643  C  CD  . GLN E  1 42  ? 64.798  45.198  33.170  1.00 45.13 ? 15  GLN H CD  1 
ATOM   4644  O  OE1 . GLN E  1 42  ? 65.762  45.919  32.892  1.00 51.56 ? 15  GLN H OE1 1 
ATOM   4645  N  NE2 . GLN E  1 42  ? 64.232  45.188  34.368  1.00 47.67 ? 15  GLN H NE2 1 
ATOM   4646  N  N   . GLY E  1 43  ? 65.926  43.538  27.972  1.00 26.31 ? 16  GLY H N   1 
ATOM   4647  C  CA  . GLY E  1 43  ? 67.040  43.526  27.043  1.00 27.50 ? 16  GLY H CA  1 
ATOM   4648  C  C   . GLY E  1 43  ? 66.971  44.678  26.070  1.00 28.41 ? 16  GLY H C   1 
ATOM   4649  O  O   . GLY E  1 43  ? 65.917  45.291  25.880  1.00 23.83 ? 16  GLY H O   1 
ATOM   4650  N  N   . ILE E  1 44  ? 68.125  44.981  25.477  1.00 22.12 ? 17  ILE H N   1 
ATOM   4651  C  CA  . ILE E  1 44  ? 68.239  45.922  24.369  1.00 22.42 ? 17  ILE H CA  1 
ATOM   4652  C  C   . ILE E  1 44  ? 68.892  45.181  23.215  1.00 28.26 ? 17  ILE H C   1 
ATOM   4653  O  O   . ILE E  1 44  ? 69.977  44.606  23.380  1.00 23.78 ? 17  ILE H O   1 
ATOM   4654  C  CB  . ILE E  1 44  ? 69.065  47.165  24.747  1.00 25.49 ? 17  ILE H CB  1 
ATOM   4655  C  CG1 . ILE E  1 44  ? 68.333  47.981  25.826  1.00 26.62 ? 17  ILE H CG1 1 
ATOM   4656  C  CG2 . ILE E  1 44  ? 69.335  48.009  23.513  1.00 24.93 ? 17  ILE H CG2 1 
ATOM   4657  C  CD1 . ILE E  1 44  ? 69.174  49.083  26.417  1.00 32.97 ? 17  ILE H CD1 1 
ATOM   4658  N  N   . ILE E  1 45  ? 68.233  45.181  22.058  1.00 23.63 ? 18  ILE H N   1 
ATOM   4659  C  CA  . ILE E  1 45  ? 68.731  44.510  20.862  1.00 25.21 ? 18  ILE H CA  1 
ATOM   4660  C  C   . ILE E  1 45  ? 68.882  45.543  19.750  1.00 28.45 ? 18  ILE H C   1 
ATOM   4661  O  O   . ILE E  1 45  ? 67.939  46.291  19.459  1.00 23.23 ? 18  ILE H O   1 
ATOM   4662  C  CB  . ILE E  1 45  ? 67.805  43.358  20.431  1.00 23.85 ? 18  ILE H CB  1 
ATOM   4663  C  CG1 . ILE E  1 45  ? 67.753  42.268  21.509  1.00 28.28 ? 18  ILE H CG1 1 
ATOM   4664  C  CG2 . ILE E  1 45  ? 68.298  42.754  19.141  1.00 21.75 ? 18  ILE H CG2 1 
ATOM   4665  C  CD1 . ILE E  1 45  ? 69.115  41.570  21.772  1.00 25.68 ? 18  ILE H CD1 1 
ATOM   4666  N  N   . ASN E  1 46  ? 70.072  45.590  19.148  1.00 21.54 ? 19  ASN H N   1 
ATOM   4667  C  CA  . ASN E  1 46  ? 70.425  46.483  18.053  1.00 24.22 ? 19  ASN H CA  1 
ATOM   4668  C  C   . ASN E  1 46  ? 70.442  45.745  16.720  1.00 31.42 ? 19  ASN H C   1 
ATOM   4669  O  O   . ASN E  1 46  ? 70.750  44.553  16.647  1.00 24.25 ? 19  ASN H O   1 
ATOM   4670  C  CB  . ASN E  1 46  ? 71.800  47.114  18.281  1.00 27.27 ? 19  ASN H CB  1 
ATOM   4671  C  CG  . ASN E  1 46  ? 71.951  47.675  19.678  1.00 32.58 ? 19  ASN H CG  1 
ATOM   4672  O  OD1 . ASN E  1 46  ? 72.460  47.010  20.588  1.00 36.28 ? 19  ASN H OD1 1 
ATOM   4673  N  ND2 . ASN E  1 46  ? 71.481  48.904  19.863  1.00 28.13 ? 19  ASN H ND2 1 
ATOM   4674  N  N   . PHE E  1 47  ? 70.110  46.476  15.657  1.00 26.32 ? 20  PHE H N   1 
ATOM   4675  C  CA  . PHE E  1 47  ? 70.117  45.949  14.299  1.00 23.54 ? 20  PHE H CA  1 
ATOM   4676  C  C   . PHE E  1 47  ? 70.881  46.912  13.416  1.00 27.71 ? 20  PHE H C   1 
ATOM   4677  O  O   . PHE E  1 47  ? 70.705  48.130  13.526  1.00 23.45 ? 20  PHE H O   1 
ATOM   4678  C  CB  . PHE E  1 47  ? 68.698  45.777  13.721  1.00 22.17 ? 20  PHE H CB  1 
ATOM   4679  C  CG  . PHE E  1 47  ? 67.787  44.919  14.547  1.00 24.79 ? 20  PHE H CG  1 
ATOM   4680  C  CD1 . PHE E  1 47  ? 67.170  45.422  15.688  1.00 26.90 ? 20  PHE H CD1 1 
ATOM   4681  C  CD2 . PHE E  1 47  ? 67.487  43.633  14.148  1.00 26.81 ? 20  PHE H CD2 1 
ATOM   4682  C  CE1 . PHE E  1 47  ? 66.297  44.633  16.437  1.00 23.95 ? 20  PHE H CE1 1 
ATOM   4683  C  CE2 . PHE E  1 47  ? 66.624  42.840  14.884  1.00 25.77 ? 20  PHE H CE2 1 
ATOM   4684  C  CZ  . PHE E  1 47  ? 66.026  43.339  16.038  1.00 23.54 ? 20  PHE H CZ  1 
ATOM   4685  N  N   . GLU E  1 48  ? 71.710  46.369  12.521  1.00 23.55 ? 21  GLU H N   1 
ATOM   4686  C  CA  . GLU E  1 48  ? 72.432  47.208  11.581  1.00 25.64 ? 21  GLU H CA  1 
ATOM   4687  C  C   . GLU E  1 48  ? 72.483  46.525  10.226  1.00 26.79 ? 21  GLU H C   1 
ATOM   4688  O  O   . GLU E  1 48  ? 72.723  45.316  10.140  1.00 24.81 ? 21  GLU H O   1 
ATOM   4689  C  CB  . GLU E  1 48  ? 73.837  47.515  12.079  1.00 29.98 ? 21  GLU H CB  1 
ATOM   4690  C  CG  . GLU E  1 48  ? 74.612  48.413  11.144  1.00 37.18 ? 21  GLU H CG  1 
ATOM   4691  C  CD  . GLU E  1 48  ? 75.898  48.903  11.774  1.00 54.30 ? 21  GLU H CD  1 
ATOM   4692  O  OE1 . GLU E  1 48  ? 76.886  48.133  11.790  1.00 57.90 ? 21  GLU H OE1 1 
ATOM   4693  O  OE2 . GLU E  1 48  ? 75.906  50.044  12.285  1.00 63.01 ? 21  GLU H OE2 1 
ATOM   4694  N  N   . GLN E  1 49  ? 72.222  47.300  9.174   1.00 23.72 ? 22  GLN H N   1 
ATOM   4695  C  CA  . GLN E  1 49  ? 72.209  46.784  7.803   1.00 22.89 ? 22  GLN H CA  1 
ATOM   4696  C  C   . GLN E  1 49  ? 72.839  47.872  6.945   1.00 31.95 ? 22  GLN H C   1 
ATOM   4697  O  O   . GLN E  1 49  ? 72.172  48.841  6.569   1.00 31.52 ? 22  GLN H O   1 
ATOM   4698  C  CB  . GLN E  1 49  ? 70.802  46.444  7.342   1.00 24.51 ? 22  GLN H CB  1 
ATOM   4699  C  CG  . GLN E  1 49  ? 70.728  45.601  6.080   1.00 25.87 ? 22  GLN H CG  1 
ATOM   4700  C  CD  . GLN E  1 49  ? 69.314  45.484  5.579   1.00 28.60 ? 22  GLN H CD  1 
ATOM   4701  O  OE1 . GLN E  1 49  ? 68.433  46.229  6.019   1.00 21.26 ? 22  GLN H OE1 1 
ATOM   4702  N  NE2 . GLN E  1 49  ? 69.070  44.529  4.675   1.00 22.98 ? 22  GLN H NE2 1 
ATOM   4703  N  N   . LYS E  1 50  ? 74.127  47.735  6.664   1.00 29.39 ? 23  LYS H N   1 
ATOM   4704  C  CA  . LYS E  1 50  ? 74.787  48.819  5.959   1.00 34.52 ? 23  LYS H CA  1 
ATOM   4705  C  C   . LYS E  1 50  ? 74.477  48.825  4.472   1.00 32.52 ? 23  LYS H C   1 
ATOM   4706  O  O   . LYS E  1 50  ? 74.592  49.879  3.847   1.00 40.02 ? 23  LYS H O   1 
ATOM   4707  C  CB  . LYS E  1 50  ? 76.290  48.783  6.233   1.00 38.67 ? 23  LYS H CB  1 
ATOM   4708  C  CG  . LYS E  1 50  ? 76.607  49.625  7.470   1.00 42.75 ? 23  LYS H CG  1 
ATOM   4709  C  CD  . LYS E  1 50  ? 78.062  49.618  7.883   1.00 52.26 ? 23  LYS H CD  1 
ATOM   4710  C  CE  . LYS E  1 50  ? 78.180  50.048  9.345   1.00 50.76 ? 23  LYS H CE  1 
ATOM   4711  N  NZ  . LYS E  1 50  ? 79.571  50.454  9.708   1.00 55.53 ? 23  LYS H NZ  1 
ATOM   4712  N  N   . GLU E  1 51  ? 74.031  47.703  3.908   1.00 32.50 ? 24  GLU H N   1 
ATOM   4713  C  CA  . GLU E  1 51  ? 73.543  47.673  2.536   1.00 34.13 ? 24  GLU H CA  1 
ATOM   4714  C  C   . GLU E  1 51  ? 72.147  47.082  2.519   1.00 26.76 ? 24  GLU H C   1 
ATOM   4715  O  O   . GLU E  1 51  ? 71.910  46.030  3.116   1.00 23.11 ? 24  GLU H O   1 
ATOM   4716  C  CB  . GLU E  1 51  ? 74.470  46.857  1.614   1.00 33.30 ? 24  GLU H CB  1 
ATOM   4717  C  CG  . GLU E  1 51  ? 75.943  47.292  1.679   1.00 42.73 ? 24  GLU H CG  1 
ATOM   4718  C  CD  . GLU E  1 51  ? 76.187  48.724  1.173   1.00 52.70 ? 24  GLU H CD  1 
ATOM   4719  O  OE1 . GLU E  1 51  ? 75.218  49.491  0.949   1.00 58.77 ? 24  GLU H OE1 1 
ATOM   4720  O  OE2 . GLU E  1 51  ? 77.372  49.094  1.005   1.00 56.47 ? 24  GLU H OE2 1 
ATOM   4721  N  N   . SER E  1 52  ? 71.238  47.733  1.794   1.00 27.04 ? 25  SER H N   1 
ATOM   4722  C  CA  . SER E  1 52  ? 69.855  47.275  1.767   1.00 22.55 ? 25  SER H CA  1 
ATOM   4723  C  C   . SER E  1 52  ? 69.699  45.886  1.176   1.00 26.18 ? 25  SER H C   1 
ATOM   4724  O  O   . SER E  1 52  ? 68.679  45.231  1.417   1.00 24.83 ? 25  SER H O   1 
ATOM   4725  C  CB  . SER E  1 52  ? 68.998  48.284  0.999   1.00 30.47 ? 25  SER H CB  1 
ATOM   4726  O  OG  . SER E  1 52  ? 69.302  48.244  -0.383  1.00 28.29 ? 25  SER H OG  1 
ATOM   4727  N  N   . ASN E  1 53  ? 70.666  45.412  0.400   1.00 25.37 ? 26  ASN H N   1 
ATOM   4728  C  CA  . ASN E  1 53  ? 70.586  44.062  -0.134  1.00 27.39 ? 26  ASN H CA  1 
ATOM   4729  C  C   . ASN E  1 53  ? 71.576  43.127  0.548   1.00 31.95 ? 26  ASN H C   1 
ATOM   4730  O  O   . ASN E  1 53  ? 71.884  42.057  0.016   1.00 35.46 ? 26  ASN H O   1 
ATOM   4731  C  CB  . ASN E  1 53  ? 70.795  44.059  -1.658  1.00 29.11 ? 26  ASN H CB  1 
ATOM   4732  C  CG  . ASN E  1 53  ? 72.158  44.571  -2.082  1.00 26.27 ? 26  ASN H CG  1 
ATOM   4733  O  OD1 . ASN E  1 53  ? 72.791  45.355  -1.378  1.00 29.23 ? 26  ASN H OD1 1 
ATOM   4734  N  ND2 . ASN E  1 53  ? 72.629  44.108  -3.252  1.00 26.43 ? 26  ASN H ND2 1 
ATOM   4735  N  N   . GLY E  1 54  ? 72.078  43.516  1.721   1.00 31.37 ? 27  GLY H N   1 
ATOM   4736  C  CA  . GLY E  1 54  ? 72.996  42.705  2.479   1.00 28.95 ? 27  GLY H CA  1 
ATOM   4737  C  C   . GLY E  1 54  ? 72.410  42.240  3.806   1.00 29.67 ? 27  GLY H C   1 
ATOM   4738  O  O   . GLY E  1 54  ? 71.245  42.500  4.131   1.00 25.63 ? 27  GLY H O   1 
ATOM   4739  N  N   . PRO E  1 55  ? 73.207  41.520  4.587   1.00 31.03 ? 28  PRO H N   1 
ATOM   4740  C  CA  . PRO E  1 55  ? 72.687  40.928  5.822   1.00 27.54 ? 28  PRO H CA  1 
ATOM   4741  C  C   . PRO E  1 55  ? 72.485  41.972  6.911   1.00 22.11 ? 28  PRO H C   1 
ATOM   4742  O  O   . PRO E  1 55  ? 73.079  43.055  6.904   1.00 24.42 ? 28  PRO H O   1 
ATOM   4743  C  CB  . PRO E  1 55  ? 73.776  39.921  6.220   1.00 33.12 ? 28  PRO H CB  1 
ATOM   4744  C  CG  . PRO E  1 55  ? 75.047  40.538  5.689   1.00 36.02 ? 28  PRO H CG  1 
ATOM   4745  C  CD  . PRO E  1 55  ? 74.624  41.173  4.355   1.00 33.83 ? 28  PRO H CD  1 
ATOM   4746  N  N   . VAL E  1 56  ? 71.639  41.607  7.871   1.00 29.22 ? 29  VAL H N   1 
ATOM   4747  C  CA  . VAL E  1 56  ? 71.388  42.414  9.061   1.00 27.16 ? 29  VAL H CA  1 
ATOM   4748  C  C   . VAL E  1 56  ? 72.187  41.833  10.217  1.00 26.67 ? 29  VAL H C   1 
ATOM   4749  O  O   . VAL E  1 56  ? 72.050  40.645  10.532  1.00 25.99 ? 29  VAL H O   1 
ATOM   4750  C  CB  . VAL E  1 56  ? 69.895  42.437  9.417   1.00 22.74 ? 29  VAL H CB  1 
ATOM   4751  C  CG1 . VAL E  1 56  ? 69.659  43.344  10.627  1.00 22.43 ? 29  VAL H CG1 1 
ATOM   4752  C  CG2 . VAL E  1 56  ? 69.072  42.888  8.213   1.00 22.59 ? 29  VAL H CG2 1 
ATOM   4753  N  N   . LYS E  1 57  ? 73.000  42.666  10.855  1.00 25.87 ? 30  LYS H N   1 
ATOM   4754  C  CA  . LYS E  1 57  ? 73.686  42.299  12.083  1.00 26.73 ? 30  LYS H CA  1 
ATOM   4755  C  C   . LYS E  1 57  ? 72.777  42.604  13.271  1.00 29.73 ? 30  LYS H C   1 
ATOM   4756  O  O   . LYS E  1 57  ? 72.240  43.712  13.376  1.00 26.30 ? 30  LYS H O   1 
ATOM   4757  C  CB  . LYS E  1 57  ? 74.999  43.072  12.225  1.00 27.64 ? 30  LYS H CB  1 
ATOM   4758  C  CG  . LYS E  1 57  ? 75.975  42.887  11.085  1.00 41.17 ? 30  LYS H CG  1 
ATOM   4759  C  CD  . LYS E  1 57  ? 77.277  43.646  11.339  1.00 48.89 ? 30  LYS H CD  1 
ATOM   4760  C  CE  . LYS E  1 57  ? 77.197  45.087  10.804  1.00 52.91 ? 30  LYS H CE  1 
ATOM   4761  N  NZ  . LYS E  1 57  ? 78.425  45.536  10.087  1.00 55.42 ? 30  LYS H NZ  1 
ATOM   4762  N  N   . VAL E  1 58  ? 72.614  41.621  14.158  1.00 28.50 ? 31  VAL H N   1 
ATOM   4763  C  CA  . VAL E  1 58  ? 71.753  41.708  15.338  1.00 26.68 ? 31  VAL H CA  1 
ATOM   4764  C  C   . VAL E  1 58  ? 72.627  41.459  16.555  1.00 32.46 ? 31  VAL H C   1 
ATOM   4765  O  O   . VAL E  1 58  ? 73.300  40.422  16.625  1.00 30.09 ? 31  VAL H O   1 
ATOM   4766  C  CB  . VAL E  1 58  ? 70.613  40.675  15.290  1.00 23.49 ? 31  VAL H CB  1 
ATOM   4767  C  CG1 . VAL E  1 58  ? 69.613  40.919  16.414  1.00 26.13 ? 31  VAL H CG1 1 
ATOM   4768  C  CG2 . VAL E  1 58  ? 69.929  40.665  13.950  1.00 27.15 ? 31  VAL H CG2 1 
ATOM   4769  N  N   . TRP E  1 59  ? 72.629  42.392  17.514  1.00 25.64 ? 32  TRP H N   1 
ATOM   4770  C  CA  . TRP E  1 59  ? 73.474  42.204  18.689  1.00 22.02 ? 32  TRP H CA  1 
ATOM   4771  C  C   . TRP E  1 59  ? 72.909  42.964  19.880  1.00 29.99 ? 32  TRP H C   1 
ATOM   4772  O  O   . TRP E  1 59  ? 72.218  43.975  19.728  1.00 25.59 ? 32  TRP H O   1 
ATOM   4773  C  CB  . TRP E  1 59  ? 74.915  42.652  18.433  1.00 25.13 ? 32  TRP H CB  1 
ATOM   4774  C  CG  . TRP E  1 59  ? 75.134  44.146  18.483  1.00 24.39 ? 32  TRP H CG  1 
ATOM   4775  C  CD1 . TRP E  1 59  ? 75.597  44.877  19.542  1.00 30.59 ? 32  TRP H CD1 1 
ATOM   4776  C  CD2 . TRP E  1 59  ? 74.936  45.075  17.413  1.00 26.08 ? 32  TRP H CD2 1 
ATOM   4777  N  NE1 . TRP E  1 59  ? 75.685  46.206  19.201  1.00 32.26 ? 32  TRP H NE1 1 
ATOM   4778  C  CE2 . TRP E  1 59  ? 75.283  46.355  17.900  1.00 30.98 ? 32  TRP H CE2 1 
ATOM   4779  C  CE3 . TRP E  1 59  ? 74.483  44.954  16.098  1.00 32.32 ? 32  TRP H CE3 1 
ATOM   4780  C  CZ2 . TRP E  1 59  ? 75.197  47.504  17.115  1.00 33.96 ? 32  TRP H CZ2 1 
ATOM   4781  C  CZ3 . TRP E  1 59  ? 74.395  46.111  15.312  1.00 34.97 ? 32  TRP H CZ3 1 
ATOM   4782  C  CH2 . TRP E  1 59  ? 74.754  47.360  15.826  1.00 34.34 ? 32  TRP H CH2 1 
ATOM   4783  N  N   . GLY E  1 60  ? 73.232  42.473  21.066  1.00 26.23 ? 33  GLY H N   1 
ATOM   4784  C  CA  . GLY E  1 60  ? 72.814  43.123  22.294  1.00 27.45 ? 33  GLY H CA  1 
ATOM   4785  C  C   . GLY E  1 60  ? 72.843  42.129  23.447  1.00 30.54 ? 33  GLY H C   1 
ATOM   4786  O  O   . GLY E  1 60  ? 73.556  41.128  23.401  1.00 29.41 ? 33  GLY H O   1 
ATOM   4787  N  N   . SER E  1 61  ? 72.050  42.426  24.466  1.00 24.54 ? 34  SER H N   1 
ATOM   4788  C  CA  . SER E  1 61  ? 72.073  41.628  25.681  1.00 30.69 ? 34  SER H CA  1 
ATOM   4789  C  C   . SER E  1 61  ? 70.663  41.545  26.247  1.00 29.49 ? 34  SER H C   1 
ATOM   4790  O  O   . SER E  1 61  ? 69.902  42.519  26.196  1.00 26.73 ? 34  SER H O   1 
ATOM   4791  C  CB  . SER E  1 61  ? 73.048  42.230  26.697  1.00 33.62 ? 34  SER H CB  1 
ATOM   4792  O  OG  . SER E  1 61  ? 73.189  41.390  27.825  1.00 45.75 ? 34  SER H OG  1 
ATOM   4793  N  N   . ILE E  1 62  ? 70.303  40.359  26.725  1.00 24.90 ? 35  ILE H N   1 
ATOM   4794  C  CA  . ILE E  1 62  ? 69.055  40.121  27.436  1.00 20.42 ? 35  ILE H CA  1 
ATOM   4795  C  C   . ILE E  1 62  ? 69.398  39.569  28.818  1.00 33.38 ? 35  ILE H C   1 
ATOM   4796  O  O   . ILE E  1 62  ? 70.253  38.682  28.941  1.00 31.80 ? 35  ILE H O   1 
ATOM   4797  C  CB  . ILE E  1 62  ? 68.144  39.145  26.667  1.00 21.12 ? 35  ILE H CB  1 
ATOM   4798  C  CG1 . ILE E  1 62  ? 68.004  39.595  25.204  1.00 25.31 ? 35  ILE H CG1 1 
ATOM   4799  C  CG2 . ILE E  1 62  ? 66.788  39.057  27.324  1.00 22.36 ? 35  ILE H CG2 1 
ATOM   4800  C  CD1 . ILE E  1 62  ? 67.149  38.669  24.380  1.00 28.33 ? 35  ILE H CD1 1 
ATOM   4801  N  N   . LYS E  1 63  ? 68.743  40.093  29.857  1.00 26.71 ? 36  LYS H N   1 
ATOM   4802  C  CA  . LYS E  1 63  ? 68.961  39.591  31.212  1.00 27.76 ? 36  LYS H CA  1 
ATOM   4803  C  C   . LYS E  1 63  ? 67.641  39.154  31.837  1.00 31.29 ? 36  LYS H C   1 
ATOM   4804  O  O   . LYS E  1 63  ? 66.554  39.369  31.287  1.00 26.52 ? 36  LYS H O   1 
ATOM   4805  C  CB  . LYS E  1 63  ? 69.661  40.633  32.089  1.00 29.56 ? 36  LYS H CB  1 
ATOM   4806  C  CG  . LYS E  1 63  ? 68.796  41.823  32.476  1.00 32.85 ? 36  LYS H CG  1 
ATOM   4807  C  CD  . LYS E  1 63  ? 69.543  42.727  33.464  1.00 40.78 ? 36  LYS H CD  1 
ATOM   4808  C  CE  . LYS E  1 63  ? 69.073  44.171  33.424  1.00 41.99 ? 36  LYS H CE  1 
ATOM   4809  N  NZ  . LYS E  1 63  ? 70.127  45.105  33.946  1.00 49.19 ? 36  LYS H NZ  1 
ATOM   4810  N  N   . GLY E  1 64  ? 67.747  38.507  33.002  1.00 25.38 ? 37  GLY H N   1 
ATOM   4811  C  CA  . GLY E  1 64  ? 66.568  37.996  33.667  1.00 22.14 ? 37  GLY H CA  1 
ATOM   4812  C  C   . GLY E  1 64  ? 66.085  36.663  33.167  1.00 26.89 ? 37  GLY H C   1 
ATOM   4813  O  O   . GLY E  1 64  ? 64.948  36.274  33.463  1.00 28.73 ? 37  GLY H O   1 
ATOM   4814  N  N   . LEU E  1 65  ? 66.912  35.945  32.407  1.00 26.47 ? 38  LEU H N   1 
ATOM   4815  C  CA  . LEU E  1 65  ? 66.530  34.677  31.807  1.00 29.95 ? 38  LEU H CA  1 
ATOM   4816  C  C   . LEU E  1 65  ? 67.026  33.528  32.676  1.00 31.08 ? 38  LEU H C   1 
ATOM   4817  O  O   . LEU E  1 65  ? 68.000  33.669  33.416  1.00 32.11 ? 38  LEU H O   1 
ATOM   4818  C  CB  . LEU E  1 65  ? 67.116  34.535  30.397  1.00 26.19 ? 38  LEU H CB  1 
ATOM   4819  C  CG  . LEU E  1 65  ? 66.575  35.514  29.346  1.00 31.10 ? 38  LEU H CG  1 
ATOM   4820  C  CD1 . LEU E  1 65  ? 67.522  35.625  28.151  1.00 31.04 ? 38  LEU H CD1 1 
ATOM   4821  C  CD2 . LEU E  1 65  ? 65.182  35.099  28.923  1.00 27.08 ? 38  LEU H CD2 1 
ATOM   4822  N  N   . THR E  1 66  ? 66.335  32.397  32.593  1.00 30.63 ? 39  THR H N   1 
ATOM   4823  C  CA  . THR E  1 66  ? 66.898  31.168  33.134  1.00 35.57 ? 39  THR H CA  1 
ATOM   4824  C  C   . THR E  1 66  ? 67.999  30.674  32.206  1.00 37.49 ? 39  THR H C   1 
ATOM   4825  O  O   . THR E  1 66  ? 67.890  30.785  30.978  1.00 34.55 ? 39  THR H O   1 
ATOM   4826  C  CB  . THR E  1 66  ? 65.828  30.098  33.278  1.00 33.33 ? 39  THR H CB  1 
ATOM   4827  O  OG1 . THR E  1 66  ? 65.244  29.843  31.994  1.00 37.86 ? 39  THR H OG1 1 
ATOM   4828  C  CG2 . THR E  1 66  ? 64.741  30.547  34.260  1.00 34.42 ? 39  THR H CG2 1 
ATOM   4829  N  N   . GLU E  1 67  ? 69.069  30.145  32.802  1.00 33.20 ? 40  GLU H N   1 
ATOM   4830  C  CA  . GLU E  1 67  ? 70.188  29.600  32.038  1.00 32.54 ? 40  GLU H CA  1 
ATOM   4831  C  C   . GLU E  1 67  ? 69.693  28.628  30.971  1.00 33.69 ? 40  GLU H C   1 
ATOM   4832  O  O   . GLU E  1 67  ? 68.766  27.849  31.210  1.00 39.28 ? 40  GLU H O   1 
ATOM   4833  C  CB  . GLU E  1 67  ? 71.161  28.896  33.004  1.00 39.87 ? 40  GLU H CB  1 
ATOM   4834  C  CG  . GLU E  1 67  ? 72.112  27.892  32.355  1.00 45.28 ? 40  GLU H CG  1 
ATOM   4835  C  CD  . GLU E  1 67  ? 73.334  27.582  33.222  1.00 51.92 ? 40  GLU H CD  1 
ATOM   4836  O  OE1 . GLU E  1 67  ? 74.455  27.474  32.669  1.00 50.27 ? 40  GLU H OE1 1 
ATOM   4837  O  OE2 . GLU E  1 67  ? 73.172  27.447  34.456  1.00 53.02 ? 40  GLU H OE2 1 
ATOM   4838  N  N   . GLY E  1 68  ? 70.289  28.704  29.771  1.00 36.36 ? 41  GLY H N   1 
ATOM   4839  C  CA  . GLY E  1 68  ? 69.933  27.831  28.667  1.00 33.10 ? 41  GLY H CA  1 
ATOM   4840  C  C   . GLY E  1 68  ? 69.423  28.583  27.446  1.00 38.33 ? 41  GLY H C   1 
ATOM   4841  O  O   . GLY E  1 68  ? 69.612  29.797  27.290  1.00 35.31 ? 41  GLY H O   1 
ATOM   4842  N  N   . LEU E  1 69  ? 68.769  27.826  26.560  1.00 33.33 ? 42  LEU H N   1 
ATOM   4843  C  CA  . LEU E  1 69  ? 68.368  28.283  25.232  1.00 35.66 ? 42  LEU H CA  1 
ATOM   4844  C  C   . LEU E  1 69  ? 66.951  28.835  25.242  1.00 32.69 ? 42  LEU H C   1 
ATOM   4845  O  O   . LEU E  1 69  ? 66.049  28.254  25.857  1.00 34.59 ? 42  LEU H O   1 
ATOM   4846  C  CB  . LEU E  1 69  ? 68.435  27.137  24.215  1.00 37.63 ? 42  LEU H CB  1 
ATOM   4847  C  CG  . LEU E  1 69  ? 69.716  26.888  23.427  1.00 38.89 ? 42  LEU H CG  1 
ATOM   4848  C  CD1 . LEU E  1 69  ? 70.908  26.703  24.360  1.00 38.08 ? 42  LEU H CD1 1 
ATOM   4849  C  CD2 . LEU E  1 69  ? 69.535  25.671  22.518  1.00 43.25 ? 42  LEU H CD2 1 
ATOM   4850  N  N   . HIS E  1 70  ? 66.751  29.927  24.498  1.00 32.75 ? 43  HIS H N   1 
ATOM   4851  C  CA  . HIS E  1 70  ? 65.461  30.602  24.446  1.00 31.39 ? 43  HIS H CA  1 
ATOM   4852  C  C   . HIS E  1 70  ? 65.140  31.008  23.015  1.00 24.07 ? 43  HIS H C   1 
ATOM   4853  O  O   . HIS E  1 70  ? 65.973  31.625  22.341  1.00 25.02 ? 43  HIS H O   1 
ATOM   4854  C  CB  . HIS E  1 70  ? 65.456  31.839  25.350  1.00 33.06 ? 43  HIS H CB  1 
ATOM   4855  C  CG  . HIS E  1 70  ? 65.579  31.520  26.806  1.00 33.26 ? 43  HIS H CG  1 
ATOM   4856  N  ND1 . HIS E  1 70  ? 64.498  31.151  27.581  1.00 31.98 ? 43  HIS H ND1 1 
ATOM   4857  C  CD2 . HIS E  1 70  ? 66.658  31.495  27.625  1.00 32.85 ? 43  HIS H CD2 1 
ATOM   4858  C  CE1 . HIS E  1 70  ? 64.905  30.932  28.821  1.00 36.78 ? 43  HIS H CE1 1 
ATOM   4859  N  NE2 . HIS E  1 70  ? 66.211  31.136  28.874  1.00 31.00 ? 43  HIS H NE2 1 
ATOM   4860  N  N   . GLY E  1 71  ? 63.937  30.661  22.564  1.00 23.16 ? 44  GLY H N   1 
ATOM   4861  C  CA  . GLY E  1 71  ? 63.526  31.036  21.223  1.00 30.46 ? 44  GLY H CA  1 
ATOM   4862  C  C   . GLY E  1 71  ? 63.491  32.544  21.058  1.00 30.28 ? 44  GLY H C   1 
ATOM   4863  O  O   . GLY E  1 71  ? 63.215  33.289  22.000  1.00 24.21 ? 44  GLY H O   1 
ATOM   4864  N  N   . PHE E  1 72  ? 63.783  32.996  19.837  1.00 27.75 ? 45  PHE H N   1 
ATOM   4865  C  CA  . PHE E  1 72  ? 64.063  34.406  19.560  1.00 24.75 ? 45  PHE H CA  1 
ATOM   4866  C  C   . PHE E  1 72  ? 63.479  34.706  18.183  1.00 33.63 ? 45  PHE H C   1 
ATOM   4867  O  O   . PHE E  1 72  ? 64.090  34.366  17.167  1.00 28.84 ? 45  PHE H O   1 
ATOM   4868  C  CB  . PHE E  1 72  ? 65.565  34.642  19.608  1.00 22.48 ? 45  PHE H CB  1 
ATOM   4869  C  CG  . PHE E  1 72  ? 65.987  36.080  19.671  1.00 27.06 ? 45  PHE H CG  1 
ATOM   4870  C  CD1 . PHE E  1 72  ? 65.504  36.932  20.650  1.00 24.34 ? 45  PHE H CD1 1 
ATOM   4871  C  CD2 . PHE E  1 72  ? 66.934  36.563  18.774  1.00 28.54 ? 45  PHE H CD2 1 
ATOM   4872  C  CE1 . PHE E  1 72  ? 65.941  38.242  20.716  1.00 29.36 ? 45  PHE H CE1 1 
ATOM   4873  C  CE2 . PHE E  1 72  ? 67.371  37.873  18.832  1.00 31.95 ? 45  PHE H CE2 1 
ATOM   4874  C  CZ  . PHE E  1 72  ? 66.876  38.713  19.803  1.00 26.20 ? 45  PHE H CZ  1 
ATOM   4875  N  N   . HIS E  1 73  ? 62.295  35.325  18.149  1.00 27.10 ? 46  HIS H N   1 
ATOM   4876  C  CA  . HIS E  1 73  ? 61.520  35.433  16.916  1.00 28.94 ? 46  HIS H CA  1 
ATOM   4877  C  C   . HIS E  1 73  ? 61.027  36.860  16.710  1.00 33.61 ? 46  HIS H C   1 
ATOM   4878  O  O   . HIS E  1 73  ? 60.669  37.547  17.676  1.00 24.63 ? 46  HIS H O   1 
ATOM   4879  C  CB  . HIS E  1 73  ? 60.308  34.486  16.941  1.00 29.61 ? 46  HIS H CB  1 
ATOM   4880  C  CG  . HIS E  1 73  ? 60.663  33.058  17.219  1.00 33.98 ? 46  HIS H CG  1 
ATOM   4881  N  ND1 . HIS E  1 73  ? 60.146  32.359  18.290  1.00 47.07 ? 46  HIS H ND1 1 
ATOM   4882  C  CD2 . HIS E  1 73  ? 61.499  32.204  16.585  1.00 44.68 ? 46  HIS H CD2 1 
ATOM   4883  C  CE1 . HIS E  1 73  ? 60.643  31.135  18.299  1.00 39.49 ? 46  HIS H CE1 1 
ATOM   4884  N  NE2 . HIS E  1 73  ? 61.465  31.014  17.274  1.00 39.45 ? 46  HIS H NE2 1 
ATOM   4885  N  N   . VAL E  1 74  ? 61.010  37.298  15.452  1.00 26.13 ? 47  VAL H N   1 
ATOM   4886  C  CA  . VAL E  1 74  ? 60.228  38.465  15.047  1.00 24.46 ? 47  VAL H CA  1 
ATOM   4887  C  C   . VAL E  1 74  ? 58.800  37.992  14.802  1.00 27.56 ? 47  VAL H C   1 
ATOM   4888  O  O   . VAL E  1 74  ? 58.572  37.066  14.018  1.00 26.32 ? 47  VAL H O   1 
ATOM   4889  C  CB  . VAL E  1 74  ? 60.806  39.124  13.784  1.00 26.32 ? 47  VAL H CB  1 
ATOM   4890  C  CG1 . VAL E  1 74  ? 59.940  40.305  13.347  1.00 23.90 ? 47  VAL H CG1 1 
ATOM   4891  C  CG2 . VAL E  1 74  ? 62.234  39.580  14.020  1.00 24.33 ? 47  VAL H CG2 1 
ATOM   4892  N  N   . HIS E  1 75  ? 57.839  38.620  15.464  1.00 22.59 ? 48  HIS H N   1 
ATOM   4893  C  CA  . HIS E  1 75  ? 56.430  38.321  15.253  1.00 21.74 ? 48  HIS H CA  1 
ATOM   4894  C  C   . HIS E  1 75  ? 55.785  39.409  14.393  1.00 23.25 ? 48  HIS H C   1 
ATOM   4895  O  O   . HIS E  1 75  ? 56.328  40.500  14.226  1.00 22.53 ? 48  HIS H O   1 
ATOM   4896  C  CB  . HIS E  1 75  ? 55.703  38.172  16.588  1.00 25.96 ? 48  HIS H CB  1 
ATOM   4897  C  CG  . HIS E  1 75  ? 56.084  36.935  17.351  1.00 22.31 ? 48  HIS H CG  1 
ATOM   4898  N  ND1 . HIS E  1 75  ? 55.168  35.962  17.692  1.00 25.81 ? 48  HIS H ND1 1 
ATOM   4899  C  CD2 . HIS E  1 75  ? 57.281  36.504  17.816  1.00 26.66 ? 48  HIS H CD2 1 
ATOM   4900  C  CE1 . HIS E  1 75  ? 55.778  34.999  18.363  1.00 25.41 ? 48  HIS H CE1 1 
ATOM   4901  N  NE2 . HIS E  1 75  ? 57.063  35.299  18.445  1.00 29.95 ? 48  HIS H NE2 1 
ATOM   4902  N  N   . GLU E  1 76  ? 54.604  39.096  13.853  1.00 24.98 ? 49  GLU H N   1 
ATOM   4903  C  CA  . GLU E  1 76  ? 54.076  39.852  12.715  1.00 26.30 ? 49  GLU H CA  1 
ATOM   4904  C  C   . GLU E  1 76  ? 53.697  41.289  13.076  1.00 26.93 ? 49  GLU H C   1 
ATOM   4905  O  O   . GLU E  1 76  ? 53.954  42.213  12.292  1.00 25.34 ? 49  GLU H O   1 
ATOM   4906  C  CB  . GLU E  1 76  ? 52.866  39.135  12.127  1.00 23.60 ? 49  GLU H CB  1 
ATOM   4907  C  CG  . GLU E  1 76  ? 52.365  39.766  10.831  1.00 29.46 ? 49  GLU H CG  1 
ATOM   4908  C  CD  . GLU E  1 76  ? 51.162  39.050  10.260  1.00 37.23 ? 49  GLU H CD  1 
ATOM   4909  O  OE1 . GLU E  1 76  ? 50.749  38.024  10.847  1.00 40.27 ? 49  GLU H OE1 1 
ATOM   4910  O  OE2 . GLU E  1 76  ? 50.624  39.516  9.227   1.00 44.00 ? 49  GLU H OE2 1 
ATOM   4911  N  N   . PHE E  1 77  ? 53.064  41.508  14.227  1.00 27.70 ? 50  PHE H N   1 
ATOM   4912  C  CA  . PHE E  1 77  ? 52.492  42.814  14.539  1.00 22.24 ? 50  PHE H CA  1 
ATOM   4913  C  C   . PHE E  1 77  ? 53.266  43.526  15.638  1.00 24.16 ? 50  PHE H C   1 
ATOM   4914  O  O   . PHE E  1 77  ? 53.695  42.906  16.616  1.00 23.45 ? 50  PHE H O   1 
ATOM   4915  C  CB  . PHE E  1 77  ? 51.021  42.683  14.937  1.00 25.82 ? 50  PHE H CB  1 
ATOM   4916  C  CG  . PHE E  1 77  ? 50.194  41.955  13.918  1.00 27.31 ? 50  PHE H CG  1 
ATOM   4917  C  CD1 . PHE E  1 77  ? 50.022  42.480  12.650  1.00 34.52 ? 50  PHE H CD1 1 
ATOM   4918  C  CD2 . PHE E  1 77  ? 49.616  40.734  14.215  1.00 35.75 ? 50  PHE H CD2 1 
ATOM   4919  C  CE1 . PHE E  1 77  ? 49.275  41.808  11.694  1.00 33.53 ? 50  PHE H CE1 1 
ATOM   4920  C  CE2 . PHE E  1 77  ? 48.857  40.057  13.263  1.00 34.19 ? 50  PHE H CE2 1 
ATOM   4921  C  CZ  . PHE E  1 77  ? 48.695  40.599  12.003  1.00 34.00 ? 50  PHE H CZ  1 
ATOM   4922  N  N   . GLY E  1 78  ? 53.420  44.840  15.474  1.00 23.39 ? 51  GLY H N   1 
ATOM   4923  C  CA  . GLY E  1 78  ? 54.000  45.699  16.489  1.00 24.50 ? 51  GLY H CA  1 
ATOM   4924  C  C   . GLY E  1 78  ? 52.922  46.211  17.420  1.00 25.98 ? 51  GLY H C   1 
ATOM   4925  O  O   . GLY E  1 78  ? 52.801  47.413  17.674  1.00 25.99 ? 51  GLY H O   1 
ATOM   4926  N  N   . ASP E  1 79  ? 52.133  45.276  17.939  1.00 23.15 ? 52  ASP H N   1 
ATOM   4927  C  CA  . ASP E  1 79  ? 50.962  45.566  18.750  1.00 22.39 ? 52  ASP H CA  1 
ATOM   4928  C  C   . ASP E  1 79  ? 51.215  44.962  20.128  1.00 25.30 ? 52  ASP H C   1 
ATOM   4929  O  O   . ASP E  1 79  ? 51.221  43.737  20.283  1.00 28.82 ? 52  ASP H O   1 
ATOM   4930  C  CB  . ASP E  1 79  ? 49.706  45.005  18.079  1.00 24.38 ? 52  ASP H CB  1 
ATOM   4931  C  CG  . ASP E  1 79  ? 48.423  45.293  18.860  1.00 27.83 ? 52  ASP H CG  1 
ATOM   4932  O  OD1 . ASP E  1 79  ? 48.490  45.586  20.071  1.00 29.28 ? 52  ASP H OD1 1 
ATOM   4933  O  OD2 . ASP E  1 79  ? 47.336  45.212  18.244  1.00 27.92 ? 52  ASP H OD2 1 
ATOM   4934  N  N   A ASN E  1 80  ? 51.415  45.837  21.117  0.52 26.57 ? 53  ASN H N   1 
ATOM   4935  N  N   B ASN E  1 80  ? 51.483  45.815  21.116  0.48 26.57 ? 53  ASN H N   1 
ATOM   4936  C  CA  A ASN E  1 80  ? 51.664  45.479  22.509  0.52 26.07 ? 53  ASN H CA  1 
ATOM   4937  C  CA  B ASN E  1 80  ? 51.637  45.369  22.494  0.48 26.04 ? 53  ASN H CA  1 
ATOM   4938  C  C   A ASN E  1 80  ? 50.455  45.759  23.397  0.52 28.52 ? 53  ASN H C   1 
ATOM   4939  C  C   B ASN E  1 80  ? 50.483  45.845  23.381  0.48 28.91 ? 53  ASN H C   1 
ATOM   4940  O  O   A ASN E  1 80  ? 50.574  45.734  24.628  0.52 29.60 ? 53  ASN H O   1 
ATOM   4941  O  O   B ASN E  1 80  ? 50.664  46.044  24.586  0.48 29.67 ? 53  ASN H O   1 
ATOM   4942  C  CB  A ASN E  1 80  ? 52.901  46.237  23.016  0.52 28.57 ? 53  ASN H CB  1 
ATOM   4943  C  CB  B ASN E  1 80  ? 52.985  45.805  23.082  0.48 29.81 ? 53  ASN H CB  1 
ATOM   4944  C  CG  A ASN E  1 80  ? 53.357  45.792  24.408  0.52 31.74 ? 53  ASN H CG  1 
ATOM   4945  C  CG  B ASN E  1 80  ? 54.185  45.527  22.153  0.48 31.76 ? 53  ASN H CG  1 
ATOM   4946  O  OD1 A ASN E  1 80  ? 53.542  46.619  25.301  0.52 31.71 ? 53  ASN H OD1 1 
ATOM   4947  O  OD1 B ASN E  1 80  ? 54.156  44.622  21.313  0.48 29.08 ? 53  ASN H OD1 1 
ATOM   4948  N  ND2 A ASN E  1 80  ? 53.532  44.487  24.592  0.52 30.46 ? 53  ASN H ND2 1 
ATOM   4949  N  ND2 B ASN E  1 80  ? 55.279  46.253  22.376  0.48 29.32 ? 53  ASN H ND2 1 
ATOM   4950  N  N   . THR E  1 81  ? 49.285  46.008  22.802  1.00 27.04 ? 54  THR H N   1 
ATOM   4951  C  CA  . THR E  1 81  ? 48.128  46.421  23.593  1.00 31.72 ? 54  THR H CA  1 
ATOM   4952  C  C   . THR E  1 81  ? 47.695  45.361  24.600  1.00 35.82 ? 54  THR H C   1 
ATOM   4953  O  O   . THR E  1 81  ? 47.187  45.710  25.666  1.00 35.36 ? 54  THR H O   1 
ATOM   4954  C  CB  . THR E  1 81  ? 46.939  46.787  22.700  1.00 25.62 ? 54  THR H CB  1 
ATOM   4955  O  OG1 . THR E  1 81  ? 46.563  45.673  21.889  1.00 28.82 ? 54  THR H OG1 1 
ATOM   4956  C  CG2 . THR E  1 81  ? 47.275  47.979  21.810  1.00 27.82 ? 54  THR H CG2 1 
ATOM   4957  N  N   . ALA E  1 82  ? 47.864  44.078  24.296  1.00 31.13 ? 55  ALA H N   1 
ATOM   4958  C  CA  . ALA E  1 82  ? 47.602  43.017  25.273  1.00 32.74 ? 55  ALA H CA  1 
ATOM   4959  C  C   . ALA E  1 82  ? 48.895  42.316  25.674  1.00 32.11 ? 55  ALA H C   1 
ATOM   4960  O  O   . ALA E  1 82  ? 48.947  41.091  25.794  1.00 45.44 ? 55  ALA H O   1 
ATOM   4961  C  CB  . ALA E  1 82  ? 46.589  42.009  24.734  1.00 34.12 ? 55  ALA H CB  1 
ATOM   4962  N  N   . GLY E  1 83  ? 49.964  43.093  25.864  1.00 30.57 ? 56  GLY H N   1 
ATOM   4963  C  CA  . GLY E  1 83  ? 51.249  42.501  26.146  1.00 30.65 ? 56  GLY H CA  1 
ATOM   4964  C  C   . GLY E  1 83  ? 51.754  41.783  24.904  1.00 35.25 ? 56  GLY H C   1 
ATOM   4965  O  O   . GLY E  1 83  ? 51.302  42.020  23.779  1.00 32.16 ? 56  GLY H O   1 
ATOM   4966  N  N   . CYS E  1 84  ? 52.686  40.855  25.131  1.00 31.22 ? 57  CYS H N   1 
ATOM   4967  C  CA  . CYS E  1 84  ? 53.319  40.179  24.009  1.00 31.49 ? 57  CYS H CA  1 
ATOM   4968  C  C   . CYS E  1 84  ? 52.358  39.277  23.245  1.00 29.89 ? 57  CYS H C   1 
ATOM   4969  O  O   . CYS E  1 84  ? 52.658  38.910  22.104  1.00 30.32 ? 57  CYS H O   1 
ATOM   4970  C  CB  . CYS E  1 84  ? 54.544  39.404  24.511  1.00 38.16 ? 57  CYS H CB  1 
ATOM   4971  S  SG  . CYS E  1 84  ? 55.808  40.495  25.288  1.00 62.64 ? 57  CYS H SG  1 
ATOM   4972  N  N   . THR E  1 85  ? 51.192  38.964  23.806  1.00 29.06 ? 58  THR H N   1 
ATOM   4973  C  CA  . THR E  1 85  ? 50.217  38.138  23.089  1.00 32.37 ? 58  THR H CA  1 
ATOM   4974  C  C   . THR E  1 85  ? 49.740  38.806  21.799  1.00 34.62 ? 58  THR H C   1 
ATOM   4975  O  O   . THR E  1 85  ? 49.533  38.132  20.782  1.00 33.76 ? 58  THR H O   1 
ATOM   4976  C  CB  . THR E  1 85  ? 49.027  37.829  24.004  1.00 34.83 ? 58  THR H CB  1 
ATOM   4977  O  OG1 . THR E  1 85  ? 49.500  37.251  25.228  1.00 44.31 ? 58  THR H OG1 1 
ATOM   4978  C  CG2 . THR E  1 85  ? 48.080  36.848  23.340  1.00 39.81 ? 58  THR H CG2 1 
ATOM   4979  N  N   . SER E  1 86  ? 49.564  40.128  21.803  1.00 26.33 ? 59  SER H N   1 
ATOM   4980  C  CA  . SER E  1 86  ? 48.994  40.757  20.615  1.00 27.16 ? 59  SER H CA  1 
ATOM   4981  C  C   . SER E  1 86  ? 49.985  40.892  19.461  1.00 25.42 ? 59  SER H C   1 
ATOM   4982  O  O   . SER E  1 86  ? 49.595  41.388  18.399  1.00 25.76 ? 59  SER H O   1 
ATOM   4983  C  CB  . SER E  1 86  ? 48.423  42.133  20.963  1.00 29.80 ? 59  SER H CB  1 
ATOM   4984  O  OG  . SER E  1 86  ? 49.191  42.750  21.968  1.00 34.95 ? 59  SER H OG  1 
ATOM   4985  N  N   . ALA E  1 87  ? 51.241  40.469  19.630  1.00 25.19 ? 60  ALA H N   1 
ATOM   4986  C  CA  . ALA E  1 87  ? 52.173  40.481  18.506  1.00 28.32 ? 60  ALA H CA  1 
ATOM   4987  C  C   . ALA E  1 87  ? 51.823  39.456  17.433  1.00 27.07 ? 60  ALA H C   1 
ATOM   4988  O  O   . ALA E  1 87  ? 52.385  39.525  16.334  1.00 28.45 ? 60  ALA H O   1 
ATOM   4989  C  CB  . ALA E  1 87  ? 53.600  40.247  18.995  1.00 23.66 ? 60  ALA H CB  1 
ATOM   4990  N  N   . GLY E  1 88  ? 50.902  38.536  17.702  1.00 29.85 ? 61  GLY H N   1 
ATOM   4991  C  CA  . GLY E  1 88  ? 50.480  37.578  16.710  1.00 28.76 ? 61  GLY H CA  1 
ATOM   4992  C  C   . GLY E  1 88  ? 51.523  36.503  16.473  1.00 26.60 ? 61  GLY H C   1 
ATOM   4993  O  O   . GLY E  1 88  ? 52.406  36.266  17.302  1.00 24.07 ? 61  GLY H O   1 
ATOM   4994  N  N   . PRO E  1 89  ? 51.447  35.849  15.320  1.00 31.63 ? 62  PRO H N   1 
ATOM   4995  C  CA  . PRO E  1 89  ? 52.313  34.704  15.025  1.00 28.51 ? 62  PRO H CA  1 
ATOM   4996  C  C   . PRO E  1 89  ? 53.672  35.179  14.523  1.00 30.77 ? 62  PRO H C   1 
ATOM   4997  O  O   . PRO E  1 89  ? 53.916  36.382  14.380  1.00 26.87 ? 62  PRO H O   1 
ATOM   4998  C  CB  . PRO E  1 89  ? 51.526  33.971  13.936  1.00 31.15 ? 62  PRO H CB  1 
ATOM   4999  C  CG  . PRO E  1 89  ? 50.882  35.101  13.161  1.00 34.04 ? 62  PRO H CG  1 
ATOM   5000  C  CD  . PRO E  1 89  ? 50.551  36.175  14.194  1.00 28.92 ? 62  PRO H CD  1 
ATOM   5001  N  N   . HIS E  1 90  ? 54.562  34.212  14.251  1.00 27.59 ? 63  HIS H N   1 
ATOM   5002  C  CA  . HIS E  1 90  ? 55.868  34.540  13.683  1.00 29.07 ? 63  HIS H CA  1 
ATOM   5003  C  C   . HIS E  1 90  ? 55.679  35.277  12.363  1.00 30.52 ? 63  HIS H C   1 
ATOM   5004  O  O   . HIS E  1 90  ? 54.743  34.999  11.614  1.00 28.56 ? 63  HIS H O   1 
ATOM   5005  C  CB  . HIS E  1 90  ? 56.712  33.279  13.435  1.00 35.91 ? 63  HIS H CB  1 
ATOM   5006  C  CG  . HIS E  1 90  ? 57.131  32.557  14.679  1.00 38.65 ? 63  HIS H CG  1 
ATOM   5007  N  ND1 . HIS E  1 90  ? 57.726  31.313  14.645  1.00 53.69 ? 63  HIS H ND1 1 
ATOM   5008  C  CD2 . HIS E  1 90  ? 57.014  32.884  15.988  1.00 43.30 ? 63  HIS H CD2 1 
ATOM   5009  C  CE1 . HIS E  1 90  ? 57.972  30.914  15.881  1.00 39.79 ? 63  HIS H CE1 1 
ATOM   5010  N  NE2 . HIS E  1 90  ? 57.549  31.848  16.715  1.00 42.61 ? 63  HIS H NE2 1 
ATOM   5011  N  N   . PHE E  1 91  ? 56.566  36.242  12.092  1.00 28.38 ? 64  PHE H N   1 
ATOM   5012  C  CA  . PHE E  1 91  ? 56.469  37.047  10.875  1.00 31.38 ? 64  PHE H CA  1 
ATOM   5013  C  C   . PHE E  1 91  ? 56.725  36.154  9.658   1.00 31.94 ? 64  PHE H C   1 
ATOM   5014  O  O   . PHE E  1 91  ? 57.782  35.521  9.562   1.00 29.26 ? 64  PHE H O   1 
ATOM   5015  C  CB  . PHE E  1 91  ? 57.460  38.218  10.911  1.00 26.25 ? 64  PHE H CB  1 
ATOM   5016  C  CG  . PHE E  1 91  ? 57.473  39.065  9.637   1.00 24.35 ? 64  PHE H CG  1 
ATOM   5017  C  CD1 . PHE E  1 91  ? 56.299  39.407  8.991   1.00 25.35 ? 64  PHE H CD1 1 
ATOM   5018  C  CD2 . PHE E  1 91  ? 58.670  39.529  9.113   1.00 25.93 ? 64  PHE H CD2 1 
ATOM   5019  C  CE1 . PHE E  1 91  ? 56.325  40.190  7.823   1.00 27.37 ? 64  PHE H CE1 1 
ATOM   5020  C  CE2 . PHE E  1 91  ? 58.710  40.310  7.951   1.00 30.35 ? 64  PHE H CE2 1 
ATOM   5021  C  CZ  . PHE E  1 91  ? 57.540  40.636  7.305   1.00 23.26 ? 64  PHE H CZ  1 
ATOM   5022  N  N   . ASN E  1 92  ? 55.761  36.114  8.729   1.00 34.07 ? 65  ASN H N   1 
ATOM   5023  C  CA  . ASN E  1 92  ? 55.752  35.123  7.648   1.00 42.88 ? 65  ASN H CA  1 
ATOM   5024  C  C   . ASN E  1 92  ? 55.056  35.682  6.416   1.00 44.43 ? 65  ASN H C   1 
ATOM   5025  O  O   . ASN E  1 92  ? 53.946  35.266  6.061   1.00 45.04 ? 65  ASN H O   1 
ATOM   5026  C  CB  . ASN E  1 92  ? 55.076  33.835  8.111   1.00 40.77 ? 65  ASN H CB  1 
ATOM   5027  C  CG  . ASN E  1 92  ? 55.441  32.646  7.248   1.00 52.79 ? 65  ASN H CG  1 
ATOM   5028  O  OD1 . ASN E  1 92  ? 56.521  32.596  6.643   1.00 48.51 ? 65  ASN H OD1 1 
ATOM   5029  N  ND2 . ASN E  1 92  ? 54.551  31.656  7.217   1.00 50.89 ? 65  ASN H ND2 1 
ATOM   5030  N  N   . PRO E  1 93  ? 55.700  36.612  5.710   1.00 39.60 ? 66  PRO H N   1 
ATOM   5031  C  CA  . PRO E  1 93  ? 55.099  37.114  4.464   1.00 37.83 ? 66  PRO H CA  1 
ATOM   5032  C  C   . PRO E  1 93  ? 55.040  36.063  3.363   1.00 45.84 ? 66  PRO H C   1 
ATOM   5033  O  O   . PRO E  1 93  ? 54.179  36.162  2.481   1.00 52.93 ? 66  PRO H O   1 
ATOM   5034  C  CB  . PRO E  1 93  ? 56.015  38.282  4.080   1.00 37.26 ? 66  PRO H CB  1 
ATOM   5035  C  CG  . PRO E  1 93  ? 57.353  37.890  4.642   1.00 36.31 ? 66  PRO H CG  1 
ATOM   5036  C  CD  . PRO E  1 93  ? 57.059  37.135  5.929   1.00 33.83 ? 66  PRO H CD  1 
ATOM   5037  N  N   . LEU E  1 94  ? 55.908  35.048  3.407   1.00 47.23 ? 67  LEU H N   1 
ATOM   5038  C  CA  . LEU E  1 94  ? 56.036  34.045  2.353   1.00 47.80 ? 67  LEU H CA  1 
ATOM   5039  C  C   . LEU E  1 94  ? 55.230  32.773  2.631   1.00 51.75 ? 67  LEU H C   1 
ATOM   5040  O  O   . LEU E  1 94  ? 55.359  31.799  1.881   1.00 53.79 ? 67  LEU H O   1 
ATOM   5041  C  CB  . LEU E  1 94  ? 57.516  33.697  2.155   1.00 45.30 ? 67  LEU H CB  1 
ATOM   5042  C  CG  . LEU E  1 94  ? 58.414  34.808  1.599   1.00 44.92 ? 67  LEU H CG  1 
ATOM   5043  C  CD1 . LEU E  1 94  ? 59.595  34.239  0.832   1.00 48.61 ? 67  LEU H CD1 1 
ATOM   5044  C  CD2 . LEU E  1 94  ? 57.614  35.741  0.699   1.00 42.44 ? 67  LEU H CD2 1 
ATOM   5045  N  N   . SER E  1 95  ? 54.429  32.754  3.703   1.00 51.08 ? 68  SER H N   1 
ATOM   5046  C  CA  . SER E  1 95  ? 53.499  31.655  4.010   1.00 54.17 ? 68  SER H CA  1 
ATOM   5047  C  C   . SER E  1 95  ? 54.190  30.288  4.033   1.00 53.58 ? 68  SER H C   1 
ATOM   5048  O  O   . SER E  1 95  ? 53.651  29.287  3.550   1.00 55.82 ? 68  SER H O   1 
ATOM   5049  C  CB  . SER E  1 95  ? 52.321  31.650  3.030   1.00 50.26 ? 68  SER H CB  1 
ATOM   5050  O  OG  . SER E  1 95  ? 51.944  32.976  2.703   1.00 57.33 ? 68  SER H OG  1 
ATOM   5051  N  N   . ARG E  1 96  ? 55.392  30.242  4.613   1.00 54.05 ? 69  ARG H N   1 
ATOM   5052  C  CA  . ARG E  1 96  ? 56.148  29.006  4.770   1.00 53.64 ? 69  ARG H CA  1 
ATOM   5053  C  C   . ARG E  1 96  ? 56.005  28.461  6.195   1.00 59.61 ? 69  ARG H C   1 
ATOM   5054  O  O   . ARG E  1 96  ? 55.375  29.068  7.072   1.00 48.83 ? 69  ARG H O   1 
ATOM   5055  C  CB  . ARG E  1 96  ? 57.625  29.222  4.407   1.00 50.40 ? 69  ARG H CB  1 
ATOM   5056  C  CG  . ARG E  1 96  ? 57.833  29.960  3.088   1.00 47.44 ? 69  ARG H CG  1 
ATOM   5057  C  CD  . ARG E  1 96  ? 58.973  29.351  2.274   1.00 54.71 ? 69  ARG H CD  1 
ATOM   5058  N  NE  . ARG E  1 96  ? 59.279  30.149  1.088   1.00 58.13 ? 69  ARG H NE  1 
ATOM   5059  C  CZ  . ARG E  1 96  ? 60.498  30.528  0.719   1.00 64.38 ? 69  ARG H CZ  1 
ATOM   5060  N  NH1 . ARG E  1 96  ? 61.573  30.164  1.402   1.00 56.28 ? 69  ARG H NH1 1 
ATOM   5061  N  NH2 . ARG E  1 96  ? 60.643  31.287  -0.368  1.00 57.82 ? 69  ARG H NH2 1 
ATOM   5062  N  N   . LYS E  1 97  ? 56.594  27.288  6.421   1.00 55.40 ? 70  LYS H N   1 
ATOM   5063  C  CA  . LYS E  1 97  ? 56.545  26.636  7.719   1.00 50.02 ? 70  LYS H CA  1 
ATOM   5064  C  C   . LYS E  1 97  ? 57.688  27.125  8.607   1.00 54.16 ? 70  LYS H C   1 
ATOM   5065  O  O   . LYS E  1 97  ? 58.639  27.762  8.147   1.00 52.90 ? 70  LYS H O   1 
ATOM   5066  C  CB  . LYS E  1 97  ? 56.598  25.113  7.558   1.00 53.75 ? 70  LYS H CB  1 
ATOM   5067  N  N   . HIS E  1 98  ? 57.581  26.816  9.901   1.00 54.08 ? 71  HIS H N   1 
ATOM   5068  C  CA  . HIS E  1 98  ? 58.573  27.266  10.870  1.00 53.81 ? 71  HIS H CA  1 
ATOM   5069  C  C   . HIS E  1 98  ? 59.863  26.465  10.738  1.00 53.94 ? 71  HIS H C   1 
ATOM   5070  O  O   . HIS E  1 98  ? 59.842  25.240  10.583  1.00 59.79 ? 71  HIS H O   1 
ATOM   5071  C  CB  . HIS E  1 98  ? 58.030  27.137  12.299  1.00 54.51 ? 71  HIS H CB  1 
ATOM   5072  C  CG  . HIS E  1 98  ? 59.039  27.462  13.358  1.00 56.48 ? 71  HIS H CG  1 
ATOM   5073  N  ND1 . HIS E  1 98  ? 59.322  28.756  13.743  1.00 59.23 ? 71  HIS H ND1 1 
ATOM   5074  C  CD2 . HIS E  1 98  ? 59.850  26.664  14.093  1.00 49.53 ? 71  HIS H CD2 1 
ATOM   5075  C  CE1 . HIS E  1 98  ? 60.258  28.738  14.675  1.00 53.53 ? 71  HIS H CE1 1 
ATOM   5076  N  NE2 . HIS E  1 98  ? 60.597  27.483  14.905  1.00 52.83 ? 71  HIS H NE2 1 
ATOM   5077  N  N   . GLY E  1 99  ? 60.991  27.165  10.812  1.00 55.30 ? 72  GLY H N   1 
ATOM   5078  C  CA  . GLY E  1 99  ? 62.284  26.510  10.797  1.00 53.61 ? 72  GLY H CA  1 
ATOM   5079  C  C   . GLY E  1 99  ? 63.332  27.241  11.611  1.00 53.53 ? 72  GLY H C   1 
ATOM   5080  O  O   . GLY E  1 99  ? 63.017  28.179  12.354  1.00 52.53 ? 72  GLY H O   1 
ATOM   5081  N  N   . GLY E  1 100 ? 64.582  26.803  11.490  1.00 54.09 ? 73  GLY H N   1 
ATOM   5082  C  CA  . GLY E  1 100 ? 65.699  27.492  12.090  1.00 47.68 ? 73  GLY H CA  1 
ATOM   5083  C  C   . GLY E  1 100 ? 66.199  28.571  11.153  1.00 51.96 ? 73  GLY H C   1 
ATOM   5084  O  O   . GLY E  1 100 ? 65.782  28.653  9.992   1.00 50.32 ? 73  GLY H O   1 
ATOM   5085  N  N   . PRO E  1 101 ? 67.100  29.428  11.640  1.00 47.87 ? 74  PRO H N   1 
ATOM   5086  C  CA  . PRO E  1 101 ? 67.565  30.546  10.805  1.00 43.10 ? 74  PRO H CA  1 
ATOM   5087  C  C   . PRO E  1 101 ? 68.188  30.119  9.481   1.00 54.71 ? 74  PRO H C   1 
ATOM   5088  O  O   . PRO E  1 101 ? 68.141  30.890  8.512   1.00 52.82 ? 74  PRO H O   1 
ATOM   5089  C  CB  . PRO E  1 101 ? 68.583  31.271  11.704  1.00 49.75 ? 74  PRO H CB  1 
ATOM   5090  C  CG  . PRO E  1 101 ? 68.819  30.365  12.893  1.00 47.74 ? 74  PRO H CG  1 
ATOM   5091  C  CD  . PRO E  1 101 ? 67.595  29.509  13.023  1.00 43.14 ? 74  PRO H CD  1 
ATOM   5092  N  N   . LYS E  1 102 ? 68.754  28.914  9.390   1.00 53.86 ? 75  LYS H N   1 
ATOM   5093  C  CA  . LYS E  1 102 ? 69.459  28.510  8.179   1.00 51.07 ? 75  LYS H CA  1 
ATOM   5094  C  C   . LYS E  1 102 ? 68.672  27.519  7.323   1.00 52.69 ? 75  LYS H C   1 
ATOM   5095  O  O   . LYS E  1 102 ? 69.228  26.971  6.364   1.00 57.06 ? 75  LYS H O   1 
ATOM   5096  C  CB  . LYS E  1 102 ? 70.836  27.951  8.543   1.00 46.36 ? 75  LYS H CB  1 
ATOM   5097  C  CG  . LYS E  1 102 ? 71.969  28.918  8.183   1.00 49.40 ? 75  LYS H CG  1 
ATOM   5098  C  CD  . LYS E  1 102 ? 73.335  28.338  8.492   1.00 48.00 ? 75  LYS H CD  1 
ATOM   5099  C  CE  . LYS E  1 102 ? 73.567  28.266  9.995   1.00 53.14 ? 75  LYS H CE  1 
ATOM   5100  N  NZ  . LYS E  1 102 ? 74.942  28.707  10.376  1.00 64.48 ? 75  LYS H NZ  1 
ATOM   5101  N  N   . ASP E  1 103 ? 67.392  27.293  7.627   1.00 52.15 ? 76  ASP H N   1 
ATOM   5102  C  CA  . ASP E  1 103 ? 66.519  26.535  6.737   1.00 53.15 ? 76  ASP H CA  1 
ATOM   5103  C  C   . ASP E  1 103 ? 65.982  27.435  5.632   1.00 59.34 ? 76  ASP H C   1 
ATOM   5104  O  O   . ASP E  1 103 ? 65.649  28.602  5.870   1.00 62.29 ? 76  ASP H O   1 
ATOM   5105  C  CB  . ASP E  1 103 ? 65.340  25.927  7.504   1.00 50.64 ? 76  ASP H CB  1 
ATOM   5106  C  CG  . ASP E  1 103 ? 65.771  24.887  8.521   1.00 63.86 ? 76  ASP H CG  1 
ATOM   5107  O  OD1 . ASP E  1 103 ? 66.392  23.871  8.126   1.00 64.57 ? 76  ASP H OD1 1 
ATOM   5108  O  OD2 . ASP E  1 103 ? 65.490  25.091  9.723   1.00 64.61 ? 76  ASP H OD2 1 
ATOM   5109  N  N   . GLU E  1 104 ? 65.894  26.889  4.415   1.00 53.52 ? 77  GLU H N   1 
ATOM   5110  C  CA  . GLU E  1 104 ? 65.149  27.580  3.367   1.00 55.42 ? 77  GLU H CA  1 
ATOM   5111  C  C   . GLU E  1 104 ? 63.657  27.585  3.676   1.00 60.90 ? 77  GLU H C   1 
ATOM   5112  O  O   . GLU E  1 104 ? 62.932  28.489  3.240   1.00 61.10 ? 77  GLU H O   1 
ATOM   5113  C  CB  . GLU E  1 104 ? 65.412  26.933  2.003   1.00 54.46 ? 77  GLU H CB  1 
ATOM   5114  N  N   . GLU E  1 105 ? 63.188  26.592  4.436   1.00 53.68 ? 78  GLU H N   1 
ATOM   5115  C  CA  . GLU E  1 105 ? 61.796  26.522  4.877   1.00 53.86 ? 78  GLU H CA  1 
ATOM   5116  C  C   . GLU E  1 105 ? 61.738  27.081  6.297   1.00 54.31 ? 78  GLU H C   1 
ATOM   5117  O  O   . GLU E  1 105 ? 61.809  26.356  7.291   1.00 58.20 ? 78  GLU H O   1 
ATOM   5118  C  CB  . GLU E  1 105 ? 61.278  25.087  4.808   1.00 49.35 ? 78  GLU H CB  1 
ATOM   5119  C  CG  . GLU E  1 105 ? 59.830  24.901  5.253   1.00 46.18 ? 78  GLU H CG  1 
ATOM   5120  C  CD  . GLU E  1 105 ? 58.828  25.455  4.248   1.00 58.12 ? 78  GLU H CD  1 
ATOM   5121  O  OE1 . GLU E  1 105 ? 59.248  25.922  3.163   1.00 58.83 ? 78  GLU H OE1 1 
ATOM   5122  O  OE2 . GLU E  1 105 ? 57.614  25.409  4.539   1.00 62.27 ? 78  GLU H OE2 1 
ATOM   5123  N  N   . ARG E  1 106 ? 61.618  28.404  6.380   1.00 49.84 ? 79  ARG H N   1 
ATOM   5124  C  CA  . ARG E  1 106 ? 61.527  29.098  7.654   1.00 51.98 ? 79  ARG H CA  1 
ATOM   5125  C  C   . ARG E  1 106 ? 60.583  30.277  7.491   1.00 50.86 ? 79  ARG H C   1 
ATOM   5126  O  O   . ARG E  1 106 ? 60.249  30.679  6.375   1.00 54.18 ? 79  ARG H O   1 
ATOM   5127  C  CB  . ARG E  1 106 ? 62.900  29.596  8.138   1.00 46.15 ? 79  ARG H CB  1 
ATOM   5128  C  CG  . ARG E  1 106 ? 63.546  30.597  7.175   1.00 44.37 ? 79  ARG H CG  1 
ATOM   5129  C  CD  . ARG E  1 106 ? 64.796  31.251  7.763   1.00 45.04 ? 79  ARG H CD  1 
ATOM   5130  N  NE  . ARG E  1 106 ? 64.541  32.556  8.370   1.00 42.60 ? 79  ARG H NE  1 
ATOM   5131  C  CZ  . ARG E  1 106 ? 65.491  33.341  8.864   1.00 42.14 ? 79  ARG H CZ  1 
ATOM   5132  N  NH1 . ARG E  1 106 ? 66.762  32.982  8.841   1.00 45.28 ? 79  ARG H NH1 1 
ATOM   5133  N  NH2 . ARG E  1 106 ? 65.161  34.525  9.378   1.00 31.81 ? 79  ARG H NH2 1 
ATOM   5134  N  N   . HIS E  1 107 ? 60.142  30.817  8.623   1.00 48.68 ? 80  HIS H N   1 
ATOM   5135  C  CA  . HIS E  1 107 ? 59.532  32.136  8.628   1.00 42.28 ? 80  HIS H CA  1 
ATOM   5136  C  C   . HIS E  1 107 ? 60.637  33.183  8.521   1.00 35.43 ? 80  HIS H C   1 
ATOM   5137  O  O   . HIS E  1 107 ? 61.773  32.957  8.953   1.00 37.32 ? 80  HIS H O   1 
ATOM   5138  C  CB  . HIS E  1 107 ? 58.716  32.356  9.909   1.00 39.66 ? 80  HIS H CB  1 
ATOM   5139  C  CG  . HIS E  1 107 ? 57.643  31.331  10.150  1.00 49.59 ? 80  HIS H CG  1 
ATOM   5140  N  ND1 . HIS E  1 107 ? 57.471  30.704  11.370  1.00 59.04 ? 80  HIS H ND1 1 
ATOM   5141  C  CD2 . HIS E  1 107 ? 56.675  30.839  9.338   1.00 48.72 ? 80  HIS H CD2 1 
ATOM   5142  C  CE1 . HIS E  1 107 ? 56.443  29.875  11.296  1.00 46.74 ? 80  HIS H CE1 1 
ATOM   5143  N  NE2 . HIS E  1 107 ? 55.943  29.937  10.074  1.00 47.97 ? 80  HIS H NE2 1 
ATOM   5144  N  N   . VAL E  1 108 ? 60.306  34.334  7.928   1.00 28.80 ? 81  VAL H N   1 
ATOM   5145  C  CA  . VAL E  1 108 ? 61.260  35.443  7.935   1.00 29.80 ? 81  VAL H CA  1 
ATOM   5146  C  C   . VAL E  1 108 ? 61.658  35.799  9.369   1.00 31.22 ? 81  VAL H C   1 
ATOM   5147  O  O   . VAL E  1 108 ? 62.825  36.093  9.653   1.00 30.49 ? 81  VAL H O   1 
ATOM   5148  C  CB  . VAL E  1 108 ? 60.686  36.662  7.184   1.00 31.87 ? 81  VAL H CB  1 
ATOM   5149  C  CG1 . VAL E  1 108 ? 61.589  37.891  7.368   1.00 29.17 ? 81  VAL H CG1 1 
ATOM   5150  C  CG2 . VAL E  1 108 ? 60.517  36.342  5.682   1.00 34.04 ? 81  VAL H CG2 1 
ATOM   5151  N  N   . GLY E  1 109 ? 60.710  35.752  10.295  1.00 31.22 ? 82  GLY H N   1 
ATOM   5152  C  CA  . GLY E  1 109 ? 61.032  36.113  11.664  1.00 36.34 ? 82  GLY H CA  1 
ATOM   5153  C  C   . GLY E  1 109 ? 61.783  35.103  12.514  1.00 39.06 ? 82  GLY H C   1 
ATOM   5154  O  O   . GLY E  1 109 ? 62.009  35.362  13.701  1.00 36.59 ? 82  GLY H O   1 
ATOM   5155  N  N   . ASP E  1 110 ? 62.207  33.964  11.972  1.00 37.95 ? 83  ASP H N   1 
ATOM   5156  C  CA  . ASP E  1 110 ? 62.775  32.903  12.806  1.00 34.38 ? 83  ASP H CA  1 
ATOM   5157  C  C   . ASP E  1 110 ? 64.276  33.131  12.952  1.00 34.24 ? 83  ASP H C   1 
ATOM   5158  O  O   . ASP E  1 110 ? 65.061  32.789  12.065  1.00 39.86 ? 83  ASP H O   1 
ATOM   5159  C  CB  . ASP E  1 110 ? 62.436  31.534  12.222  1.00 43.27 ? 83  ASP H CB  1 
ATOM   5160  C  CG  . ASP E  1 110 ? 60.941  31.212  12.333  1.00 53.17 ? 83  ASP H CG  1 
ATOM   5161  O  OD1 . ASP E  1 110 ? 60.226  31.934  13.053  1.00 52.43 ? 83  ASP H OD1 1 
ATOM   5162  O  OD2 . ASP E  1 110 ? 60.464  30.235  11.722  1.00 58.71 ? 83  ASP H OD2 1 
ATOM   5163  N  N   . LEU E  1 111 ? 64.683  33.712  14.084  1.00 30.43 ? 84  LEU H N   1 
ATOM   5164  C  CA  . LEU E  1 111 ? 66.084  33.985  14.363  1.00 33.35 ? 84  LEU H CA  1 
ATOM   5165  C  C   . LEU E  1 111 ? 66.719  32.935  15.267  1.00 35.39 ? 84  LEU H C   1 
ATOM   5166  O  O   . LEU E  1 111 ? 67.844  33.131  15.740  1.00 42.28 ? 84  LEU H O   1 
ATOM   5167  C  CB  . LEU E  1 111 ? 66.242  35.376  14.979  1.00 36.40 ? 84  LEU H CB  1 
ATOM   5168  C  CG  . LEU E  1 111 ? 65.782  36.525  14.075  1.00 41.48 ? 84  LEU H CG  1 
ATOM   5169  C  CD1 . LEU E  1 111 ? 65.975  37.873  14.763  1.00 36.54 ? 84  LEU H CD1 1 
ATOM   5170  C  CD2 . LEU E  1 111 ? 66.564  36.482  12.776  1.00 34.85 ? 84  LEU H CD2 1 
ATOM   5171  N  N   . GLY E  1 112 ? 66.031  31.835  15.518  1.00 34.93 ? 85  GLY H N   1 
ATOM   5172  C  CA  . GLY E  1 112 ? 66.644  30.709  16.208  1.00 40.51 ? 85  GLY H CA  1 
ATOM   5173  C  C   . GLY E  1 112 ? 66.558  30.848  17.713  1.00 38.80 ? 85  GLY H C   1 
ATOM   5174  O  O   . GLY E  1 112 ? 65.491  31.131  18.256  1.00 31.90 ? 85  GLY H O   1 
ATOM   5175  N  N   . ASN E  1 113 ? 67.683  30.620  18.389  1.00 32.73 ? 86  ASN H N   1 
ATOM   5176  C  CA  . ASN E  1 113 ? 67.734  30.640  19.841  1.00 34.25 ? 86  ASN H CA  1 
ATOM   5177  C  C   . ASN E  1 113 ? 68.821  31.587  20.299  1.00 31.32 ? 86  ASN H C   1 
ATOM   5178  O  O   . ASN E  1 113 ? 69.803  31.822  19.589  1.00 38.92 ? 86  ASN H O   1 
ATOM   5179  C  CB  . ASN E  1 113 ? 68.021  29.256  20.437  1.00 34.25 ? 86  ASN H CB  1 
ATOM   5180  C  CG  . ASN E  1 113 ? 66.895  28.288  20.216  1.00 36.26 ? 86  ASN H CG  1 
ATOM   5181  O  OD1 . ASN E  1 113 ? 65.810  28.439  20.789  1.00 36.15 ? 86  ASN H OD1 1 
ATOM   5182  N  ND2 . ASN E  1 113 ? 67.136  27.279  19.387  1.00 36.60 ? 86  ASN H ND2 1 
ATOM   5183  N  N   . VAL E  1 114 ? 68.631  32.131  21.493  1.00 33.75 ? 87  VAL H N   1 
ATOM   5184  C  CA  . VAL E  1 114 ? 69.698  32.805  22.203  1.00 29.50 ? 87  VAL H CA  1 
ATOM   5185  C  C   . VAL E  1 114 ? 70.003  31.972  23.443  1.00 26.68 ? 87  VAL H C   1 
ATOM   5186  O  O   . VAL E  1 114 ? 69.179  31.177  23.904  1.00 34.48 ? 87  VAL H O   1 
ATOM   5187  C  CB  . VAL E  1 114 ? 69.341  34.261  22.575  1.00 32.98 ? 87  VAL H CB  1 
ATOM   5188  C  CG1 . VAL E  1 114 ? 69.121  35.089  21.303  1.00 32.88 ? 87  VAL H CG1 1 
ATOM   5189  C  CG2 . VAL E  1 114 ? 68.115  34.304  23.483  1.00 30.69 ? 87  VAL H CG2 1 
ATOM   5190  N  N   . THR E  1 115 ? 71.200  32.169  23.987  1.00 30.47 ? 88  THR H N   1 
ATOM   5191  C  CA  . THR E  1 115 ? 71.709  31.353  25.086  1.00 35.76 ? 88  THR H CA  1 
ATOM   5192  C  C   . THR E  1 115 ? 72.044  32.233  26.283  1.00 27.58 ? 88  THR H C   1 
ATOM   5193  O  O   . THR E  1 115 ? 72.936  33.085  26.208  1.00 33.77 ? 88  THR H O   1 
ATOM   5194  C  CB  . THR E  1 115 ? 72.952  30.568  24.656  1.00 36.60 ? 88  THR H CB  1 
ATOM   5195  O  OG1 . THR E  1 115 ? 72.578  29.571  23.699  1.00 47.52 ? 88  THR H OG1 1 
ATOM   5196  C  CG2 . THR E  1 115 ? 73.570  29.865  25.884  1.00 38.56 ? 88  THR H CG2 1 
ATOM   5197  N  N   . ALA E  1 116 ? 71.354  32.010  27.390  1.00 31.49 ? 89  ALA H N   1 
ATOM   5198  C  CA  . ALA E  1 116 ? 71.640  32.740  28.612  1.00 31.01 ? 89  ALA H CA  1 
ATOM   5199  C  C   . ALA E  1 116 ? 72.623  31.928  29.444  1.00 35.94 ? 89  ALA H C   1 
ATOM   5200  O  O   . ALA E  1 116 ? 72.480  30.707  29.565  1.00 34.23 ? 89  ALA H O   1 
ATOM   5201  C  CB  . ALA E  1 116 ? 70.360  32.999  29.413  1.00 34.60 ? 89  ALA H CB  1 
ATOM   5202  N  N   . ASP E  1 117 ? 73.621  32.613  30.001  1.00 37.23 ? 90  ASP H N   1 
ATOM   5203  C  CA  . ASP E  1 117 ? 74.620  31.983  30.853  1.00 36.61 ? 90  ASP H CA  1 
ATOM   5204  C  C   . ASP E  1 117 ? 74.036  31.716  32.238  1.00 38.59 ? 90  ASP H C   1 
ATOM   5205  O  O   . ASP E  1 117 ? 72.840  31.888  32.490  1.00 35.77 ? 90  ASP H O   1 
ATOM   5206  C  CB  . ASP E  1 117 ? 75.894  32.831  30.921  1.00 33.50 ? 90  ASP H CB  1 
ATOM   5207  C  CG  . ASP E  1 117 ? 75.668  34.252  31.461  1.00 36.83 ? 90  ASP H CG  1 
ATOM   5208  O  OD1 . ASP E  1 117 ? 74.755  34.495  32.288  1.00 39.68 ? 90  ASP H OD1 1 
ATOM   5209  O  OD2 . ASP E  1 117 ? 76.474  35.134  31.097  1.00 40.60 ? 90  ASP H OD2 1 
ATOM   5210  N  N   . LYS E  1 118 ? 74.898  31.287  33.162  1.00 42.46 ? 91  LYS H N   1 
ATOM   5211  C  CA  . LYS E  1 118 ? 74.444  30.944  34.502  1.00 35.93 ? 91  LYS H CA  1 
ATOM   5212  C  C   . LYS E  1 118 ? 73.994  32.166  35.286  1.00 39.27 ? 91  LYS H C   1 
ATOM   5213  O  O   . LYS E  1 118 ? 73.324  32.017  36.312  1.00 40.59 ? 91  LYS H O   1 
ATOM   5214  C  CB  . LYS E  1 118 ? 75.562  30.239  35.275  1.00 41.45 ? 91  LYS H CB  1 
ATOM   5215  C  CG  . LYS E  1 118 ? 76.698  31.175  35.665  1.00 41.13 ? 91  LYS H CG  1 
ATOM   5216  C  CD  . LYS E  1 118 ? 77.618  30.544  36.703  1.00 52.47 ? 91  LYS H CD  1 
ATOM   5217  C  CE  . LYS E  1 118 ? 79.019  31.137  36.629  1.00 50.30 ? 91  LYS H CE  1 
ATOM   5218  N  NZ  . LYS E  1 118 ? 79.524  31.200  35.227  1.00 53.78 ? 91  LYS H NZ  1 
ATOM   5219  N  N   . ASP E  1 119 ? 74.365  33.364  34.842  1.00 35.12 ? 92  ASP H N   1 
ATOM   5220  C  CA  . ASP E  1 119 ? 73.946  34.593  35.499  1.00 39.49 ? 92  ASP H CA  1 
ATOM   5221  C  C   . ASP E  1 119 ? 72.665  35.156  34.904  1.00 36.87 ? 92  ASP H C   1 
ATOM   5222  O  O   . ASP E  1 119 ? 72.293  36.289  35.228  1.00 36.30 ? 92  ASP H O   1 
ATOM   5223  C  CB  . ASP E  1 119 ? 75.057  35.632  35.416  1.00 39.58 ? 92  ASP H CB  1 
ATOM   5224  C  CG  . ASP E  1 119 ? 76.139  35.403  36.459  1.00 51.94 ? 92  ASP H CG  1 
ATOM   5225  O  OD1 . ASP E  1 119 ? 75.806  35.277  37.661  1.00 54.94 ? 92  ASP H OD1 1 
ATOM   5226  O  OD2 . ASP E  1 119 ? 77.324  35.334  36.067  1.00 57.97 ? 92  ASP H OD2 1 
ATOM   5227  N  N   . GLY E  1 120 ? 71.989  34.392  34.049  1.00 32.43 ? 93  GLY H N   1 
ATOM   5228  C  CA  . GLY E  1 120 ? 70.761  34.824  33.415  1.00 36.95 ? 93  GLY H CA  1 
ATOM   5229  C  C   . GLY E  1 120 ? 70.913  35.804  32.268  1.00 32.42 ? 93  GLY H C   1 
ATOM   5230  O  O   . GLY E  1 120 ? 69.918  36.414  31.866  1.00 28.94 ? 93  GLY H O   1 
ATOM   5231  N  N   . VAL E  1 121 ? 72.116  35.982  31.732  1.00 26.57 ? 94  VAL H N   1 
ATOM   5232  C  CA  . VAL E  1 121 ? 72.376  36.958  30.682  1.00 29.49 ? 94  VAL H CA  1 
ATOM   5233  C  C   . VAL E  1 121 ? 72.647  36.234  29.369  1.00 33.23 ? 94  VAL H C   1 
ATOM   5234  O  O   . VAL E  1 121 ? 73.543  35.386  29.287  1.00 31.19 ? 94  VAL H O   1 
ATOM   5235  C  CB  . VAL E  1 121 ? 73.558  37.869  31.047  1.00 28.97 ? 94  VAL H CB  1 
ATOM   5236  C  CG1 . VAL E  1 121 ? 73.816  38.876  29.926  1.00 32.24 ? 94  VAL H CG1 1 
ATOM   5237  C  CG2 . VAL E  1 121 ? 73.307  38.552  32.391  1.00 30.60 ? 94  VAL H CG2 1 
ATOM   5238  N  N   . ALA E  1 122 ? 71.898  36.592  28.335  1.00 31.81 ? 95  ALA H N   1 
ATOM   5239  C  CA  . ALA E  1 122 ? 72.158  36.122  26.982  1.00 29.44 ? 95  ALA H CA  1 
ATOM   5240  C  C   . ALA E  1 122 ? 72.806  37.254  26.202  1.00 40.22 ? 95  ALA H C   1 
ATOM   5241  O  O   . ALA E  1 122 ? 72.199  38.316  26.031  1.00 33.88 ? 95  ALA H O   1 
ATOM   5242  C  CB  . ALA E  1 122 ? 70.870  35.667  26.294  1.00 30.26 ? 95  ALA H CB  1 
ATOM   5243  N  N   . ASP E  1 123 ? 74.035  37.037  25.745  1.00 30.01 ? 96  ASP H N   1 
ATOM   5244  C  CA  . ASP E  1 123 ? 74.690  37.978  24.851  1.00 34.05 ? 96  ASP H CA  1 
ATOM   5245  C  C   . ASP E  1 123 ? 74.394  37.554  23.421  1.00 35.97 ? 96  ASP H C   1 
ATOM   5246  O  O   . ASP E  1 123 ? 74.654  36.408  23.040  1.00 37.51 ? 96  ASP H O   1 
ATOM   5247  C  CB  . ASP E  1 123 ? 76.191  38.051  25.117  1.00 39.20 ? 96  ASP H CB  1 
ATOM   5248  C  CG  . ASP E  1 123 ? 76.509  38.770  26.417  1.00 58.59 ? 96  ASP H CG  1 
ATOM   5249  O  OD1 . ASP E  1 123 ? 75.935  39.860  26.652  1.00 61.32 ? 96  ASP H OD1 1 
ATOM   5250  O  OD2 . ASP E  1 123 ? 77.328  38.252  27.206  1.00 60.42 ? 96  ASP H OD2 1 
ATOM   5251  N  N   . VAL E  1 124 ? 73.805  38.458  22.650  1.00 34.39 ? 97  VAL H N   1 
ATOM   5252  C  CA  . VAL E  1 124 ? 73.294  38.136  21.323  1.00 31.85 ? 97  VAL H CA  1 
ATOM   5253  C  C   . VAL E  1 124 ? 74.244  38.695  20.286  1.00 29.60 ? 97  VAL H C   1 
ATOM   5254  O  O   . VAL E  1 124 ? 74.696  39.841  20.397  1.00 28.48 ? 97  VAL H O   1 
ATOM   5255  C  CB  . VAL E  1 124 ? 71.876  38.686  21.117  1.00 30.98 ? 97  VAL H CB  1 
ATOM   5256  C  CG1 . VAL E  1 124 ? 71.362  38.302  19.723  1.00 29.96 ? 97  VAL H CG1 1 
ATOM   5257  C  CG2 . VAL E  1 124 ? 70.965  38.174  22.217  1.00 33.63 ? 97  VAL H CG2 1 
ATOM   5258  N  N   . SER E  1 125 ? 74.572  37.869  19.295  1.00 32.88 ? 98  SER H N   1 
ATOM   5259  C  CA  . SER E  1 125 ? 75.393  38.270  18.162  1.00 31.38 ? 98  SER H CA  1 
ATOM   5260  C  C   . SER E  1 125 ? 74.976  37.363  17.016  1.00 34.91 ? 98  SER H C   1 
ATOM   5261  O  O   . SER E  1 125 ? 75.286  36.168  17.023  1.00 41.50 ? 98  SER H O   1 
ATOM   5262  C  CB  . SER E  1 125 ? 76.881  38.149  18.461  1.00 34.31 ? 98  SER H CB  1 
ATOM   5263  O  OG  . SER E  1 125 ? 77.629  38.961  17.569  1.00 40.51 ? 98  SER H OG  1 
ATOM   5264  N  N   . ILE E  1 126 ? 74.246  37.931  16.060  1.00 32.94 ? 99  ILE H N   1 
ATOM   5265  C  CA  . ILE E  1 126 ? 73.595  37.200  14.981  1.00 31.59 ? 99  ILE H CA  1 
ATOM   5266  C  C   . ILE E  1 126 ? 73.815  38.012  13.715  1.00 35.25 ? 99  ILE H C   1 
ATOM   5267  O  O   . ILE E  1 126 ? 73.897  39.243  13.754  1.00 29.73 ? 99  ILE H O   1 
ATOM   5268  C  CB  . ILE E  1 126 ? 72.076  37.014  15.248  1.00 34.49 ? 99  ILE H CB  1 
ATOM   5269  C  CG1 . ILE E  1 126 ? 71.826  36.111  16.452  1.00 44.55 ? 99  ILE H CG1 1 
ATOM   5270  C  CG2 . ILE E  1 126 ? 71.348  36.455  14.041  1.00 41.45 ? 99  ILE H CG2 1 
ATOM   5271  C  CD1 . ILE E  1 126 ? 70.362  35.708  16.591  1.00 43.57 ? 99  ILE H CD1 1 
ATOM   5272  N  N   . GLU E  1 127 ? 73.954  37.311  12.593  1.00 34.02 ? 100 GLU H N   1 
ATOM   5273  C  CA  . GLU E  1 127 ? 73.922  37.916  11.272  1.00 33.90 ? 100 GLU H CA  1 
ATOM   5274  C  C   . GLU E  1 127 ? 72.891  37.151  10.463  1.00 35.81 ? 100 GLU H C   1 
ATOM   5275  O  O   . GLU E  1 127 ? 72.970  35.923  10.371  1.00 37.58 ? 100 GLU H O   1 
ATOM   5276  C  CB  . GLU E  1 127 ? 75.294  37.863  10.601  1.00 37.61 ? 100 GLU H CB  1 
ATOM   5277  C  CG  . GLU E  1 127 ? 75.483  38.844  9.453   1.00 43.17 ? 100 GLU H CG  1 
ATOM   5278  C  CD  . GLU E  1 127 ? 76.955  39.037  9.086   1.00 56.39 ? 100 GLU H CD  1 
ATOM   5279  O  OE1 . GLU E  1 127 ? 77.290  40.058  8.444   1.00 68.20 ? 100 GLU H OE1 1 
ATOM   5280  O  OE2 . GLU E  1 127 ? 77.777  38.161  9.437   1.00 60.22 ? 100 GLU H OE2 1 
ATOM   5281  N  N   . ASP E  1 128 ? 71.900  37.849  9.913   1.00 29.19 ? 101 ASP H N   1 
ATOM   5282  C  CA  . ASP E  1 128 ? 70.830  37.151  9.211   1.00 31.08 ? 101 ASP H CA  1 
ATOM   5283  C  C   . ASP E  1 128 ? 70.585  37.814  7.864   1.00 31.46 ? 101 ASP H C   1 
ATOM   5284  O  O   . ASP E  1 128 ? 70.452  39.042  7.789   1.00 33.54 ? 101 ASP H O   1 
ATOM   5285  C  CB  . ASP E  1 128 ? 69.551  37.112  10.054  1.00 27.76 ? 101 ASP H CB  1 
ATOM   5286  C  CG  . ASP E  1 128 ? 68.497  36.183  9.473   1.00 38.15 ? 101 ASP H CG  1 
ATOM   5287  O  OD1 . ASP E  1 128 ? 67.734  36.606  8.573   1.00 33.30 ? 101 ASP H OD1 1 
ATOM   5288  O  OD2 . ASP E  1 128 ? 68.405  35.025  9.940   1.00 46.10 ? 101 ASP H OD2 1 
ATOM   5289  N  N   A SER E  1 129 ? 70.529  37.003  6.803   0.52 31.74 ? 102 SER H N   1 
ATOM   5290  N  N   B SER E  1 129 ? 70.519  37.005  6.806   0.48 31.58 ? 102 SER H N   1 
ATOM   5291  C  CA  A SER E  1 129 ? 70.350  37.499  5.444   0.52 29.53 ? 102 SER H CA  1 
ATOM   5292  C  CA  B SER E  1 129 ? 70.345  37.512  5.451   0.48 29.77 ? 102 SER H CA  1 
ATOM   5293  C  C   A SER E  1 129 ? 68.913  37.392  4.947   0.52 29.82 ? 102 SER H C   1 
ATOM   5294  C  C   B SER E  1 129 ? 68.910  37.408  4.951   0.48 29.84 ? 102 SER H C   1 
ATOM   5295  O  O   A SER E  1 129 ? 68.658  37.661  3.770   0.52 31.88 ? 102 SER H O   1 
ATOM   5296  O  O   B SER E  1 129 ? 68.655  37.692  3.778   0.48 31.90 ? 102 SER H O   1 
ATOM   5297  C  CB  A SER E  1 129 ? 71.281  36.757  4.476   0.52 32.09 ? 102 SER H CB  1 
ATOM   5298  C  CB  B SER E  1 129 ? 71.282  36.779  4.486   0.48 32.52 ? 102 SER H CB  1 
ATOM   5299  O  OG  A SER E  1 129 ? 72.637  37.128  4.669   0.52 31.85 ? 102 SER H OG  1 
ATOM   5300  O  OG  B SER E  1 129 ? 70.873  35.435  4.313   0.48 29.37 ? 102 SER H OG  1 
ATOM   5301  N  N   . VAL E  1 130 ? 67.966  37.010  5.797   1.00 27.30 ? 103 VAL H N   1 
ATOM   5302  C  CA  . VAL E  1 130 ? 66.573  36.899  5.379   1.00 25.59 ? 103 VAL H CA  1 
ATOM   5303  C  C   . VAL E  1 130 ? 65.739  38.075  5.883   1.00 33.03 ? 103 VAL H C   1 
ATOM   5304  O  O   . VAL E  1 130 ? 64.926  38.626  5.135   1.00 28.03 ? 103 VAL H O   1 
ATOM   5305  C  CB  . VAL E  1 130 ? 65.964  35.554  5.824   1.00 32.50 ? 103 VAL H CB  1 
ATOM   5306  C  CG1 . VAL E  1 130 ? 64.511  35.462  5.381   1.00 32.40 ? 103 VAL H CG1 1 
ATOM   5307  C  CG2 . VAL E  1 130 ? 66.766  34.385  5.240   1.00 37.15 ? 103 VAL H CG2 1 
ATOM   5308  N  N   . ILE E  1 131 ? 65.917  38.459  7.153   1.00 29.48 ? 104 ILE H N   1 
ATOM   5309  C  CA  . ILE E  1 131 ? 65.303  39.691  7.647   1.00 27.86 ? 104 ILE H CA  1 
ATOM   5310  C  C   . ILE E  1 131 ? 65.926  40.890  6.943   1.00 25.40 ? 104 ILE H C   1 
ATOM   5311  O  O   . ILE E  1 131 ? 67.060  40.850  6.449   1.00 22.81 ? 104 ILE H O   1 
ATOM   5312  C  CB  . ILE E  1 131 ? 65.449  39.813  9.178   1.00 22.96 ? 104 ILE H CB  1 
ATOM   5313  C  CG1 . ILE E  1 131 ? 66.929  39.847  9.562   1.00 22.43 ? 104 ILE H CG1 1 
ATOM   5314  C  CG2 . ILE E  1 131 ? 64.765  38.661  9.852   1.00 25.99 ? 104 ILE H CG2 1 
ATOM   5315  C  CD1 . ILE E  1 131 ? 67.226  40.308  11.011  1.00 23.48 ? 104 ILE H CD1 1 
ATOM   5316  N  N   . SER E  1 132 ? 65.179  41.986  6.916   1.00 24.03 ? 105 SER H N   1 
ATOM   5317  C  CA  . SER E  1 132 ? 65.676  43.229  6.351   1.00 20.80 ? 105 SER H CA  1 
ATOM   5318  C  C   . SER E  1 132 ? 65.164  44.387  7.188   1.00 20.76 ? 105 SER H C   1 
ATOM   5319  O  O   . SER E  1 132 ? 64.174  44.247  7.901   1.00 24.00 ? 105 SER H O   1 
ATOM   5320  C  CB  . SER E  1 132 ? 65.232  43.410  4.883   1.00 21.72 ? 105 SER H CB  1 
ATOM   5321  O  OG  . SER E  1 132 ? 66.122  44.335  4.277   1.00 22.42 ? 105 SER H OG  1 
ATOM   5322  N  N   . LEU E  1 133 ? 65.843  45.533  7.094   1.00 21.27 ? 106 LEU H N   1 
ATOM   5323  C  CA  . LEU E  1 133 ? 65.316  46.772  7.662   1.00 22.65 ? 106 LEU H CA  1 
ATOM   5324  C  C   . LEU E  1 133 ? 64.566  47.617  6.632   1.00 28.15 ? 106 LEU H C   1 
ATOM   5325  O  O   . LEU E  1 133 ? 64.155  48.739  6.947   1.00 24.66 ? 106 LEU H O   1 
ATOM   5326  C  CB  . LEU E  1 133 ? 66.437  47.589  8.300   1.00 20.41 ? 106 LEU H CB  1 
ATOM   5327  C  CG  . LEU E  1 133 ? 67.265  46.860  9.379   1.00 22.24 ? 106 LEU H CG  1 
ATOM   5328  C  CD1 . LEU E  1 133 ? 68.234  47.814  10.049  1.00 24.20 ? 106 LEU H CD1 1 
ATOM   5329  C  CD2 . LEU E  1 133 ? 66.369  46.178  10.393  1.00 21.35 ? 106 LEU H CD2 1 
ATOM   5330  N  N   . SER E  1 134 ? 64.379  47.101  5.418   1.00 25.56 ? 107 SER H N   1 
ATOM   5331  C  CA  . SER E  1 134 ? 63.611  47.777  4.375   1.00 29.37 ? 107 SER H CA  1 
ATOM   5332  C  C   . SER E  1 134 ? 62.963  46.722  3.490   1.00 30.82 ? 107 SER H C   1 
ATOM   5333  O  O   . SER E  1 134 ? 63.312  45.541  3.545   1.00 25.44 ? 107 SER H O   1 
ATOM   5334  C  CB  . SER E  1 134 ? 64.486  48.725  3.541   1.00 32.42 ? 107 SER H CB  1 
ATOM   5335  O  OG  . SER E  1 134 ? 65.763  48.168  3.252   1.00 32.49 ? 107 SER H OG  1 
ATOM   5336  N  N   . GLY E  1 135 ? 61.985  47.155  2.685   1.00 26.66 ? 108 GLY H N   1 
ATOM   5337  C  CA  . GLY E  1 135 ? 61.379  46.267  1.714   1.00 27.31 ? 108 GLY H CA  1 
ATOM   5338  C  C   . GLY E  1 135 ? 60.371  45.285  2.298   1.00 37.36 ? 108 GLY H C   1 
ATOM   5339  O  O   . GLY E  1 135 ? 59.802  45.488  3.368   1.00 33.81 ? 108 GLY H O   1 
ATOM   5340  N  N   . ASP E  1 136 ? 60.162  44.185  1.567   1.00 33.79 ? 109 ASP H N   1 
ATOM   5341  C  CA  . ASP E  1 136 ? 59.076  43.259  1.888   1.00 38.06 ? 109 ASP H CA  1 
ATOM   5342  C  C   . ASP E  1 136 ? 59.369  42.433  3.137   1.00 35.36 ? 109 ASP H C   1 
ATOM   5343  O  O   . ASP E  1 136 ? 58.438  42.028  3.840   1.00 34.74 ? 109 ASP H O   1 
ATOM   5344  C  CB  . ASP E  1 136 ? 58.813  42.332  0.697   1.00 46.66 ? 109 ASP H CB  1 
ATOM   5345  C  CG  . ASP E  1 136 ? 57.700  42.848  -0.226  1.00 59.79 ? 109 ASP H CG  1 
ATOM   5346  O  OD1 . ASP E  1 136 ? 57.363  44.055  -0.154  1.00 59.25 ? 109 ASP H OD1 1 
ATOM   5347  O  OD2 . ASP E  1 136 ? 57.180  42.053  -1.043  1.00 62.30 ? 109 ASP H OD2 1 
ATOM   5348  N  N   . HIS E  1 137 ? 60.638  42.124  3.396   1.00 31.83 ? 110 HIS H N   1 
ATOM   5349  C  CA  . HIS E  1 137 ? 61.048  41.414  4.602   1.00 38.25 ? 110 HIS H CA  1 
ATOM   5350  C  C   . HIS E  1 137 ? 61.363  42.363  5.746   1.00 33.18 ? 110 HIS H C   1 
ATOM   5351  O  O   . HIS E  1 137 ? 62.075  41.965  6.686   1.00 31.66 ? 110 HIS H O   1 
ATOM   5352  C  CB  . HIS E  1 137 ? 62.272  40.529  4.323   1.00 30.94 ? 110 HIS H CB  1 
ATOM   5353  C  CG  . HIS E  1 137 ? 61.971  39.315  3.501   1.00 39.54 ? 110 HIS H CG  1 
ATOM   5354  N  ND1 . HIS E  1 137 ? 62.914  38.342  3.239   1.00 43.59 ? 110 HIS H ND1 1 
ATOM   5355  C  CD2 . HIS E  1 137 ? 60.834  38.914  2.885   1.00 38.30 ? 110 HIS H CD2 1 
ATOM   5356  C  CE1 . HIS E  1 137 ? 62.367  37.393  2.500   1.00 42.95 ? 110 HIS H CE1 1 
ATOM   5357  N  NE2 . HIS E  1 137 ? 61.108  37.718  2.269   1.00 38.55 ? 110 HIS H NE2 1 
ATOM   5358  N  N   . CYS E  1 138 ? 60.871  43.609  5.670   1.00 23.20 ? 111 CYS H N   1 
ATOM   5359  C  CA  . CYS E  1 138 ? 61.224  44.632  6.646   1.00 25.92 ? 111 CYS H CA  1 
ATOM   5360  C  C   . CYS E  1 138 ? 60.615  44.288  8.002   1.00 22.19 ? 111 CYS H C   1 
ATOM   5361  O  O   . CYS E  1 138 ? 59.425  43.956  8.093   1.00 23.39 ? 111 CYS H O   1 
ATOM   5362  C  CB  . CYS E  1 138 ? 60.734  46.001  6.181   1.00 28.24 ? 111 CYS H CB  1 
ATOM   5363  S  SG  . CYS E  1 138 ? 60.933  47.341  7.386   1.00 38.16 ? 111 CYS H SG  1 
ATOM   5364  N  N   . ILE E  1 139 ? 61.425  44.383  9.057   1.00 19.78 ? 112 ILE H N   1 
ATOM   5365  C  CA  . ILE E  1 139 ? 60.950  44.040  10.396  1.00 20.17 ? 112 ILE H CA  1 
ATOM   5366  C  C   . ILE E  1 139 ? 60.713  45.276  11.258  1.00 22.28 ? 112 ILE H C   1 
ATOM   5367  O  O   . ILE E  1 139 ? 60.313  45.142  12.421  1.00 21.08 ? 112 ILE H O   1 
ATOM   5368  C  CB  . ILE E  1 139 ? 61.925  43.068  11.089  1.00 19.67 ? 112 ILE H CB  1 
ATOM   5369  C  CG1 . ILE E  1 139 ? 63.292  43.730  11.246  1.00 22.45 ? 112 ILE H CG1 1 
ATOM   5370  C  CG2 . ILE E  1 139 ? 62.013  41.763  10.267  1.00 26.93 ? 112 ILE H CG2 1 
ATOM   5371  C  CD1 . ILE E  1 139 ? 64.313  42.934  12.098  1.00 20.58 ? 112 ILE H CD1 1 
ATOM   5372  N  N   A ILE E  1 140 ? 60.943  46.472  10.709  0.50 23.85 ? 113 ILE H N   1 
ATOM   5373  N  N   B ILE E  1 140 ? 60.958  46.474  10.735  0.50 23.88 ? 113 ILE H N   1 
ATOM   5374  C  CA  A ILE E  1 140 ? 60.617  47.703  11.419  0.50 23.79 ? 113 ILE H CA  1 
ATOM   5375  C  CA  B ILE E  1 140 ? 60.699  47.677  11.521  0.50 23.79 ? 113 ILE H CA  1 
ATOM   5376  C  C   A ILE E  1 140 ? 59.129  47.723  11.720  0.50 22.40 ? 113 ILE H C   1 
ATOM   5377  C  C   B ILE E  1 140 ? 59.197  47.838  11.702  0.50 22.42 ? 113 ILE H C   1 
ATOM   5378  O  O   A ILE E  1 140 ? 58.298  47.346  10.885  0.50 19.42 ? 113 ILE H O   1 
ATOM   5379  O  O   B ILE E  1 140 ? 58.417  47.655  10.760  0.50 19.23 ? 113 ILE H O   1 
ATOM   5380  C  CB  A ILE E  1 140 ? 61.042  48.919  10.582  0.50 23.21 ? 113 ILE H CB  1 
ATOM   5381  C  CB  B ILE E  1 140 ? 61.349  48.899  10.858  0.50 23.69 ? 113 ILE H CB  1 
ATOM   5382  C  CG1 A ILE E  1 140 ? 62.511  48.784  10.208  0.50 24.57 ? 113 ILE H CG1 1 
ATOM   5383  C  CG1 B ILE E  1 140 ? 62.862  48.823  11.058  0.50 24.02 ? 113 ILE H CG1 1 
ATOM   5384  C  CG2 A ILE E  1 140 ? 60.810  50.233  11.343  0.50 21.49 ? 113 ILE H CG2 1 
ATOM   5385  C  CG2 B ILE E  1 140 ? 60.780  50.212  11.419  0.50 21.52 ? 113 ILE H CG2 1 
ATOM   5386  C  CD1 A ILE E  1 140 ? 63.411  48.844  11.405  0.50 23.30 ? 113 ILE H CD1 1 
ATOM   5387  C  CD1 B ILE E  1 140 ? 63.645  49.820  10.233  0.50 24.20 ? 113 ILE H CD1 1 
ATOM   5388  N  N   . GLY E  1 141 ? 58.779  48.141  12.928  1.00 18.59 ? 114 GLY H N   1 
ATOM   5389  C  CA  . GLY E  1 141 ? 57.381  48.172  13.273  1.00 20.08 ? 114 GLY H CA  1 
ATOM   5390  C  C   . GLY E  1 141 ? 56.792  46.831  13.642  1.00 18.27 ? 114 GLY H C   1 
ATOM   5391  O  O   . GLY E  1 141 ? 55.600  46.760  13.930  1.00 17.85 ? 114 GLY H O   1 
ATOM   5392  N  N   . ARG E  1 142 ? 57.578  45.759  13.624  1.00 21.62 ? 115 ARG H N   1 
ATOM   5393  C  CA  . ARG E  1 142 ? 57.107  44.466  14.089  1.00 18.86 ? 115 ARG H CA  1 
ATOM   5394  C  C   . ARG E  1 142 ? 57.694  44.226  15.473  1.00 19.79 ? 115 ARG H C   1 
ATOM   5395  O  O   . ARG E  1 142 ? 58.375  45.085  16.021  1.00 21.59 ? 115 ARG H O   1 
ATOM   5396  C  CB  . ARG E  1 142 ? 57.454  43.374  13.077  1.00 17.56 ? 115 ARG H CB  1 
ATOM   5397  C  CG  . ARG E  1 142 ? 56.946  43.789  11.668  1.00 17.34 ? 115 ARG H CG  1 
ATOM   5398  C  CD  . ARG E  1 142 ? 56.865  42.632  10.697  1.00 26.01 ? 115 ARG H CD  1 
ATOM   5399  N  NE  . ARG E  1 142 ? 56.539  43.124  9.360   1.00 25.18 ? 115 ARG H NE  1 
ATOM   5400  C  CZ  . ARG E  1 142 ? 55.308  43.203  8.872   1.00 27.58 ? 115 ARG H CZ  1 
ATOM   5401  N  NH1 . ARG E  1 142 ? 54.260  42.814  9.577   1.00 22.71 ? 115 ARG H NH1 1 
ATOM   5402  N  NH2 . ARG E  1 142 ? 55.126  43.665  7.634   1.00 24.86 ? 115 ARG H NH2 1 
ATOM   5403  N  N   . THR E  1 143 ? 57.425  43.058  16.042  1.00 21.18 ? 116 THR H N   1 
ATOM   5404  C  CA  . THR E  1 143 ? 57.732  42.805  17.453  1.00 19.12 ? 116 THR H CA  1 
ATOM   5405  C  C   . THR E  1 143 ? 58.763  41.690  17.587  1.00 23.50 ? 116 THR H C   1 
ATOM   5406  O  O   . THR E  1 143 ? 58.584  40.604  17.028  1.00 26.18 ? 116 THR H O   1 
ATOM   5407  C  CB  . THR E  1 143 ? 56.469  42.430  18.228  1.00 23.11 ? 116 THR H CB  1 
ATOM   5408  O  OG1 . THR E  1 143 ? 55.575  43.546  18.245  1.00 22.94 ? 116 THR H OG1 1 
ATOM   5409  C  CG2 . THR E  1 143 ? 56.804  42.034  19.691  1.00 17.89 ? 116 THR H CG2 1 
ATOM   5410  N  N   . LEU E  1 144 ? 59.827  41.958  18.341  1.00 21.57 ? 117 LEU H N   1 
ATOM   5411  C  CA  . LEU E  1 144 ? 60.818  40.944  18.672  1.00 16.83 ? 117 LEU H CA  1 
ATOM   5412  C  C   . LEU E  1 144 ? 60.416  40.312  19.994  1.00 26.84 ? 117 LEU H C   1 
ATOM   5413  O  O   . LEU E  1 144 ? 60.048  41.027  20.919  1.00 22.31 ? 117 LEU H O   1 
ATOM   5414  C  CB  . LEU E  1 144 ? 62.201  41.573  18.754  1.00 18.54 ? 117 LEU H CB  1 
ATOM   5415  C  CG  . LEU E  1 144 ? 63.351  40.630  19.062  1.00 23.66 ? 117 LEU H CG  1 
ATOM   5416  C  CD1 . LEU E  1 144 ? 63.542  39.661  17.890  1.00 27.80 ? 117 LEU H CD1 1 
ATOM   5417  C  CD2 . LEU E  1 144 ? 64.613  41.420  19.331  1.00 21.99 ? 117 LEU H CD2 1 
ATOM   5418  N  N   . VAL E  1 145 ? 60.424  38.980  20.065  1.00 23.96 ? 118 VAL H N   1 
ATOM   5419  C  CA  . VAL E  1 145 ? 59.957  38.259  21.244  1.00 25.07 ? 118 VAL H CA  1 
ATOM   5420  C  C   . VAL E  1 145 ? 61.032  37.265  21.661  1.00 27.07 ? 118 VAL H C   1 
ATOM   5421  O  O   . VAL E  1 145 ? 61.547  36.516  20.820  1.00 24.46 ? 118 VAL H O   1 
ATOM   5422  C  CB  . VAL E  1 145 ? 58.632  37.514  20.972  1.00 22.85 ? 118 VAL H CB  1 
ATOM   5423  C  CG1 . VAL E  1 145 ? 58.224  36.683  22.194  1.00 24.76 ? 118 VAL H CG1 1 
ATOM   5424  C  CG2 . VAL E  1 145 ? 57.506  38.476  20.558  1.00 22.39 ? 118 VAL H CG2 1 
ATOM   5425  N  N   . VAL E  1 146 ? 61.370  37.243  22.949  1.00 23.67 ? 119 VAL H N   1 
ATOM   5426  C  CA  . VAL E  1 146 ? 62.192  36.170  23.499  1.00 23.38 ? 119 VAL H CA  1 
ATOM   5427  C  C   . VAL E  1 146 ? 61.266  35.224  24.258  1.00 28.87 ? 119 VAL H C   1 
ATOM   5428  O  O   . VAL E  1 146 ? 60.407  35.668  25.034  1.00 27.14 ? 119 VAL H O   1 
ATOM   5429  C  CB  . VAL E  1 146 ? 63.336  36.717  24.377  1.00 27.38 ? 119 VAL H CB  1 
ATOM   5430  C  CG1 . VAL E  1 146 ? 62.816  37.537  25.547  1.00 28.19 ? 119 VAL H CG1 1 
ATOM   5431  C  CG2 . VAL E  1 146 ? 64.231  35.577  24.859  1.00 30.88 ? 119 VAL H CG2 1 
ATOM   5432  N  N   . HIS E  1 147 ? 61.411  33.922  24.005  1.00 23.39 ? 120 HIS H N   1 
ATOM   5433  C  CA  . HIS E  1 147 ? 60.447  32.920  24.436  1.00 28.65 ? 120 HIS H CA  1 
ATOM   5434  C  C   . HIS E  1 147 ? 60.951  32.124  25.642  1.00 33.05 ? 120 HIS H C   1 
ATOM   5435  O  O   . HIS E  1 147 ? 62.125  32.164  26.013  1.00 30.57 ? 120 HIS H O   1 
ATOM   5436  C  CB  . HIS E  1 147 ? 60.121  31.958  23.293  1.00 30.46 ? 120 HIS H CB  1 
ATOM   5437  C  CG  . HIS E  1 147 ? 59.213  32.540  22.258  1.00 33.80 ? 120 HIS H CG  1 
ATOM   5438  N  ND1 . HIS E  1 147 ? 57.847  32.359  22.274  1.00 32.66 ? 120 HIS H ND1 1 
ATOM   5439  C  CD2 . HIS E  1 147 ? 59.478  33.309  21.175  1.00 30.59 ? 120 HIS H CD2 1 
ATOM   5440  C  CE1 . HIS E  1 147 ? 57.309  32.991  21.245  1.00 29.03 ? 120 HIS H CE1 1 
ATOM   5441  N  NE2 . HIS E  1 147 ? 58.277  33.572  20.559  1.00 27.81 ? 120 HIS H NE2 1 
ATOM   5442  N  N   . GLU E  1 148 ? 60.027  31.345  26.210  1.00 29.04 ? 121 GLU H N   1 
ATOM   5443  C  CA  . GLU E  1 148 ? 60.253  30.665  27.485  1.00 37.90 ? 121 GLU H CA  1 
ATOM   5444  C  C   . GLU E  1 148 ? 61.223  29.495  27.331  1.00 41.44 ? 121 GLU H C   1 
ATOM   5445  O  O   . GLU E  1 148 ? 62.193  29.376  28.088  1.00 42.67 ? 121 GLU H O   1 
ATOM   5446  C  CB  . GLU E  1 148 ? 58.907  30.181  28.029  1.00 34.90 ? 121 GLU H CB  1 
ATOM   5447  C  CG  . GLU E  1 148 ? 58.931  29.541  29.401  1.00 44.74 ? 121 GLU H CG  1 
ATOM   5448  C  CD  . GLU E  1 148 ? 57.732  28.630  29.608  1.00 52.26 ? 121 GLU H CD  1 
ATOM   5449  O  OE1 . GLU E  1 148 ? 57.715  27.888  30.613  1.00 52.70 ? 121 GLU H OE1 1 
ATOM   5450  O  OE2 . GLU E  1 148 ? 56.831  28.614  28.732  1.00 53.60 ? 121 GLU H OE2 1 
ATOM   5451  N  N   . LYS E  1 149 ? 60.980  28.622  26.354  1.00 35.56 ? 122 LYS H N   1 
ATOM   5452  C  CA  . LYS E  1 149 ? 61.818  27.453  26.112  1.00 40.44 ? 122 LYS H CA  1 
ATOM   5453  C  C   . LYS E  1 149 ? 62.564  27.589  24.794  1.00 41.77 ? 122 LYS H C   1 
ATOM   5454  O  O   . LYS E  1 149 ? 62.379  28.542  24.028  1.00 36.61 ? 122 LYS H O   1 
ATOM   5455  C  CB  . LYS E  1 149 ? 60.996  26.160  26.102  1.00 40.12 ? 122 LYS H CB  1 
ATOM   5456  C  CG  . LYS E  1 149 ? 59.954  26.027  27.205  1.00 45.35 ? 122 LYS H CG  1 
ATOM   5457  C  CD  . LYS E  1 149 ? 58.631  25.529  26.632  1.00 48.21 ? 122 LYS H CD  1 
ATOM   5458  C  CE  . LYS E  1 149 ? 58.856  24.355  25.686  1.00 51.12 ? 122 LYS H CE  1 
ATOM   5459  N  NZ  . LYS E  1 149 ? 57.575  23.730  25.234  1.00 56.16 ? 122 LYS H NZ  1 
ATOM   5460  N  N   . ALA E  1 150 ? 63.405  26.591  24.535  1.00 41.34 ? 123 ALA H N   1 
ATOM   5461  C  CA  . ALA E  1 150 ? 64.174  26.523  23.302  1.00 33.85 ? 123 ALA H CA  1 
ATOM   5462  C  C   . ALA E  1 150 ? 63.265  26.336  22.096  1.00 39.55 ? 123 ALA H C   1 
ATOM   5463  O  O   . ALA E  1 150 ? 62.216  25.686  22.165  1.00 39.19 ? 123 ALA H O   1 
ATOM   5464  C  CB  . ALA E  1 150 ? 65.181  25.372  23.366  1.00 40.23 ? 123 ALA H CB  1 
ATOM   5465  N  N   . ASP E  1 151 ? 63.688  26.921  20.979  1.00 32.18 ? 124 ASP H N   1 
ATOM   5466  C  CA  . ASP E  1 151 ? 63.040  26.701  19.697  1.00 38.75 ? 124 ASP H CA  1 
ATOM   5467  C  C   . ASP E  1 151 ? 63.586  25.399  19.122  1.00 41.93 ? 124 ASP H C   1 
ATOM   5468  O  O   . ASP E  1 151 ? 64.802  25.266  18.948  1.00 42.44 ? 124 ASP H O   1 
ATOM   5469  C  CB  . ASP E  1 151 ? 63.338  27.878  18.772  1.00 41.09 ? 124 ASP H CB  1 
ATOM   5470  C  CG  . ASP E  1 151 ? 62.588  27.813  17.457  1.00 51.08 ? 124 ASP H CG  1 
ATOM   5471  O  OD1 . ASP E  1 151 ? 61.932  26.785  17.157  1.00 50.88 ? 124 ASP H OD1 1 
ATOM   5472  O  OD2 . ASP E  1 151 ? 62.687  28.806  16.704  1.00 50.13 ? 124 ASP H OD2 1 
ATOM   5473  N  N   . ASP E  1 152 ? 62.708  24.429  18.848  1.00 39.88 ? 125 ASP H N   1 
ATOM   5474  C  CA  . ASP E  1 152 ? 63.177  23.176  18.255  1.00 45.57 ? 125 ASP H CA  1 
ATOM   5475  C  C   . ASP E  1 152 ? 63.418  23.299  16.750  1.00 51.76 ? 125 ASP H C   1 
ATOM   5476  O  O   . ASP E  1 152 ? 63.717  22.294  16.090  1.00 49.96 ? 125 ASP H O   1 
ATOM   5477  C  CB  . ASP E  1 152 ? 62.202  22.028  18.571  1.00 43.91 ? 125 ASP H CB  1 
ATOM   5478  C  CG  . ASP E  1 152 ? 60.820  22.207  17.938  1.00 53.07 ? 125 ASP H CG  1 
ATOM   5479  O  OD1 . ASP E  1 152 ? 60.687  22.900  16.907  1.00 50.92 ? 125 ASP H OD1 1 
ATOM   5480  O  OD2 . ASP E  1 152 ? 59.849  21.642  18.493  1.00 54.43 ? 125 ASP H OD2 1 
ATOM   5481  N  N   . LEU E  1 153 ? 63.385  24.526  16.241  1.00 50.50 ? 126 LEU H N   1 
ATOM   5482  C  CA  . LEU E  1 153 ? 63.691  24.857  14.825  1.00 49.34 ? 126 LEU H CA  1 
ATOM   5483  C  C   . LEU E  1 153 ? 62.797  24.117  13.822  1.00 56.75 ? 126 LEU H C   1 
ATOM   5484  O  O   . LEU E  1 153 ? 63.274  23.795  12.734  1.00 56.82 ? 126 LEU H O   1 
ATOM   5485  C  CB  . LEU E  1 153 ? 65.192  24.694  14.570  1.00 45.02 ? 126 LEU H CB  1 
ATOM   5486  C  CG  . LEU E  1 153 ? 66.064  25.216  15.710  1.00 48.88 ? 126 LEU H CG  1 
ATOM   5487  C  CD1 . LEU E  1 153 ? 67.535  24.955  15.467  1.00 42.70 ? 126 LEU H CD1 1 
ATOM   5488  C  CD2 . LEU E  1 153 ? 65.816  26.693  15.959  1.00 41.83 ? 126 LEU H CD2 1 
ATOM   5489  N  N   . GLY E  1 154 ? 61.541  23.866  14.199  1.00 55.71 ? 127 GLY H N   1 
ATOM   5490  C  CA  . GLY E  1 154 ? 60.502  23.281  13.328  1.00 53.91 ? 127 GLY H CA  1 
ATOM   5491  C  C   . GLY E  1 154 ? 60.674  21.805  13.038  1.00 60.92 ? 127 GLY H C   1 
ATOM   5492  O  O   . GLY E  1 154 ? 59.997  21.316  12.130  1.00 63.94 ? 127 GLY H O   1 
ATOM   5493  N  N   . LYS E  1 155 ? 61.556  21.139  13.779  1.00 57.53 ? 128 LYS H N   1 
ATOM   5494  C  CA  . LYS E  1 155 ? 61.810  19.700  13.604  1.00 59.03 ? 128 LYS H CA  1 
ATOM   5495  C  C   . LYS E  1 155 ? 61.468  19.020  14.924  1.00 57.44 ? 128 LYS H C   1 
ATOM   5496  O  O   . LYS E  1 155 ? 62.262  18.210  15.387  1.00 60.51 ? 128 LYS H O   1 
ATOM   5497  C  CB  . LYS E  1 155 ? 63.249  19.486  13.227  1.00 48.39 ? 128 LYS H CB  1 
ATOM   5498  N  N   . GLY E  1 156 ? 60.346  19.416  15.520  1.00 60.40 ? 129 GLY H N   1 
ATOM   5499  C  CA  . GLY E  1 156 ? 59.882  18.810  16.779  1.00 58.44 ? 129 GLY H CA  1 
ATOM   5500  C  C   . GLY E  1 156 ? 58.906  17.687  16.494  1.00 58.30 ? 129 GLY H C   1 
ATOM   5501  O  O   . GLY E  1 156 ? 58.382  17.121  17.448  1.00 62.93 ? 129 GLY H O   1 
ATOM   5502  N  N   . GLY E  1 157 ? 58.595  17.467  15.216  1.00 57.43 ? 130 GLY H N   1 
ATOM   5503  C  CA  . GLY E  1 157 ? 57.728  16.359  14.774  1.00 56.08 ? 130 GLY H CA  1 
ATOM   5504  C  C   . GLY E  1 157 ? 56.236  16.557  14.983  1.00 61.10 ? 130 GLY H C   1 
ATOM   5505  O  O   . GLY E  1 157 ? 55.486  15.672  14.571  1.00 61.82 ? 130 GLY H O   1 
ATOM   5506  N  N   . ASN E  1 158 ? 55.798  17.656  15.594  1.00 55.86 ? 131 ASN H N   1 
ATOM   5507  C  CA  . ASN E  1 158 ? 54.338  17.837  15.771  1.00 57.15 ? 131 ASN H CA  1 
ATOM   5508  C  C   . ASN E  1 158 ? 53.879  19.071  14.991  1.00 61.52 ? 131 ASN H C   1 
ATOM   5509  O  O   . ASN E  1 158 ? 54.711  19.810  14.469  1.00 56.67 ? 131 ASN H O   1 
ATOM   5510  C  CB  . ASN E  1 158 ? 53.928  17.862  17.238  1.00 52.64 ? 131 ASN H CB  1 
ATOM   5511  C  CG  . ASN E  1 158 ? 54.973  18.528  18.100  1.00 66.14 ? 131 ASN H CG  1 
ATOM   5512  O  OD1 . ASN E  1 158 ? 55.227  19.718  17.954  1.00 66.50 ? 131 ASN H OD1 1 
ATOM   5513  N  ND2 . ASN E  1 158 ? 55.595  17.764  18.981  1.00 62.16 ? 131 ASN H ND2 1 
ATOM   5514  N  N   . GLU E  1 159 ? 52.573  19.270  14.942  1.00 60.96 ? 132 GLU H N   1 
ATOM   5515  C  CA  . GLU E  1 159 ? 52.000  20.419  14.202  1.00 56.68 ? 132 GLU H CA  1 
ATOM   5516  C  C   . GLU E  1 159 ? 52.517  21.717  14.824  1.00 62.02 ? 132 GLU H C   1 
ATOM   5517  O  O   . GLU E  1 159 ? 53.028  22.543  14.075  1.00 63.26 ? 132 GLU H O   1 
ATOM   5518  C  CB  . GLU E  1 159 ? 50.477  20.372  14.240  1.00 50.29 ? 132 GLU H CB  1 
ATOM   5519  C  CG  . GLU E  1 159 ? 49.834  21.408  13.357  1.00 51.95 ? 132 GLU H CG  1 
ATOM   5520  C  CD  . GLU E  1 159 ? 48.334  21.554  13.541  0.00 68.97 ? 132 GLU H CD  1 
ATOM   5521  O  OE1 . GLU E  1 159 ? 47.662  20.523  13.744  0.00 71.12 ? 132 GLU H OE1 1 
ATOM   5522  O  OE2 . GLU E  1 159 ? 47.841  22.697  13.482  0.00 74.10 ? 132 GLU H OE2 1 
ATOM   5523  N  N   . GLU E  1 160 ? 52.455  21.825  16.157  1.00 61.43 ? 133 GLU H N   1 
ATOM   5524  C  CA  . GLU E  1 160 ? 52.898  23.010  16.942  1.00 57.63 ? 133 GLU H CA  1 
ATOM   5525  C  C   . GLU E  1 160 ? 54.344  23.407  16.594  1.00 62.43 ? 133 GLU H C   1 
ATOM   5526  O  O   . GLU E  1 160 ? 54.601  24.612  16.527  1.00 60.51 ? 133 GLU H O   1 
ATOM   5527  C  CB  . GLU E  1 160 ? 52.687  22.766  18.435  1.00 56.24 ? 133 GLU H CB  1 
ATOM   5528  C  CG  . GLU E  1 160 ? 52.854  24.013  19.274  1.00 57.59 ? 133 GLU H CG  1 
ATOM   5529  C  CD  . GLU E  1 160 ? 51.793  25.069  19.053  1.00 62.75 ? 133 GLU H CD  1 
ATOM   5530  O  OE1 . GLU E  1 160 ? 50.619  24.808  19.352  1.00 62.14 ? 133 GLU H OE1 1 
ATOM   5531  O  OE2 . GLU E  1 160 ? 52.154  26.148  18.582  1.00 64.57 ? 133 GLU H OE2 1 
ATOM   5532  N  N   . SER E  1 161 ? 55.250  22.449  16.353  1.00 51.76 ? 134 SER H N   1 
ATOM   5533  C  CA  . SER E  1 161 ? 56.642  22.778  15.938  1.00 57.94 ? 134 SER H CA  1 
ATOM   5534  C  C   . SER E  1 161 ? 56.675  23.416  14.539  1.00 59.56 ? 134 SER H C   1 
ATOM   5535  O  O   . SER E  1 161 ? 57.610  24.165  14.276  1.00 60.35 ? 134 SER H O   1 
ATOM   5536  C  CB  . SER E  1 161 ? 57.557  21.589  16.013  1.00 56.48 ? 134 SER H CB  1 
ATOM   5537  O  OG  . SER E  1 161 ? 58.766  21.850  15.326  1.00 55.13 ? 134 SER H OG  1 
ATOM   5538  N  N   . THR E  1 162 ? 55.683  23.159  13.674  1.00 57.26 ? 135 THR H N   1 
ATOM   5539  C  CA  . THR E  1 162 ? 55.654  23.795  12.326  1.00 58.37 ? 135 THR H CA  1 
ATOM   5540  C  C   . THR E  1 162 ? 55.116  25.229  12.415  1.00 57.86 ? 135 THR H C   1 
ATOM   5541  O  O   . THR E  1 162 ? 55.275  25.965  11.446  1.00 52.40 ? 135 THR H O   1 
ATOM   5542  C  CB  . THR E  1 162 ? 54.850  22.972  11.311  1.00 55.53 ? 135 THR H CB  1 
ATOM   5543  O  OG1 . THR E  1 162 ? 53.473  23.308  11.465  1.00 65.91 ? 135 THR H OG1 1 
ATOM   5544  C  CG2 . THR E  1 162 ? 55.053  21.482  11.475  1.00 46.57 ? 135 THR H CG2 1 
ATOM   5545  N  N   . LYS E  1 163 ? 54.546  25.592  13.561  1.00 56.02 ? 136 LYS H N   1 
ATOM   5546  C  CA  . LYS E  1 163 ? 53.970  26.946  13.724  1.00 56.36 ? 136 LYS H CA  1 
ATOM   5547  C  C   . LYS E  1 163 ? 54.861  27.814  14.619  1.00 55.43 ? 136 LYS H C   1 
ATOM   5548  O  O   . LYS E  1 163 ? 55.159  28.929  14.217  1.00 58.20 ? 136 LYS H O   1 
ATOM   5549  C  CB  . LYS E  1 163 ? 52.533  26.839  14.242  1.00 51.11 ? 136 LYS H CB  1 
ATOM   5550  C  CG  . LYS E  1 163 ? 51.532  26.362  13.201  1.00 57.17 ? 136 LYS H CG  1 
ATOM   5551  C  CD  . LYS E  1 163 ? 50.090  26.444  13.636  1.00 60.50 ? 136 LYS H CD  1 
ATOM   5552  C  CE  . LYS E  1 163 ? 49.320  27.569  12.976  1.00 58.03 ? 136 LYS H CE  1 
ATOM   5553  N  NZ  . LYS E  1 163 ? 47.862  27.462  13.225  1.00 57.21 ? 136 LYS H NZ  1 
ATOM   5554  N  N   . THR E  1 164 ? 55.321  27.291  15.756  1.00 53.67 ? 137 THR H N   1 
ATOM   5555  C  CA  . THR E  1 164 ? 56.087  28.134  16.702  1.00 55.78 ? 137 THR H CA  1 
ATOM   5556  C  C   . THR E  1 164 ? 57.396  27.481  17.140  1.00 58.57 ? 137 THR H C   1 
ATOM   5557  O  O   . THR E  1 164 ? 58.129  28.122  17.883  1.00 53.05 ? 137 THR H O   1 
ATOM   5558  C  CB  . THR E  1 164 ? 55.257  28.355  17.968  1.00 58.25 ? 137 THR H CB  1 
ATOM   5559  O  OG1 . THR E  1 164 ? 55.148  27.084  18.600  1.00 59.70 ? 137 THR H OG1 1 
ATOM   5560  C  CG2 . THR E  1 164 ? 53.876  28.897  17.680  1.00 51.21 ? 137 THR H CG2 1 
ATOM   5561  N  N   . GLY E  1 165 ? 57.620  26.214  16.788  1.00 54.26 ? 138 GLY H N   1 
ATOM   5562  C  CA  . GLY E  1 165 ? 58.851  25.513  17.204  1.00 51.10 ? 138 GLY H CA  1 
ATOM   5563  C  C   . GLY E  1 165 ? 58.825  25.114  18.671  1.00 51.28 ? 138 GLY H C   1 
ATOM   5564  O  O   . GLY E  1 165 ? 59.889  24.857  19.204  1.00 46.81 ? 138 GLY H O   1 
ATOM   5565  N  N   . ASN E  1 166 ? 57.635  25.079  19.279  1.00 51.44 ? 139 ASN H N   1 
ATOM   5566  C  CA  . ASN E  1 166 ? 57.401  24.718  20.701  1.00 48.61 ? 139 ASN H CA  1 
ATOM   5567  C  C   . ASN E  1 166 ? 58.200  25.617  21.649  1.00 51.82 ? 139 ASN H C   1 
ATOM   5568  O  O   . ASN E  1 166 ? 58.480  25.175  22.744  1.00 50.26 ? 139 ASN H O   1 
ATOM   5569  C  CB  . ASN E  1 166 ? 57.710  23.245  20.941  1.00 47.45 ? 139 ASN H CB  1 
ATOM   5570  C  CG  . ASN E  1 166 ? 56.651  22.348  20.345  1.00 52.02 ? 139 ASN H CG  1 
ATOM   5571  O  OD1 . ASN E  1 166 ? 56.931  21.562  19.455  1.00 55.71 ? 139 ASN H OD1 1 
ATOM   5572  N  ND2 . ASN E  1 166 ? 55.432  22.473  20.827  1.00 51.89 ? 139 ASN H ND2 1 
ATOM   5573  N  N   . ALA E  1 167 ? 58.492  26.855  21.263  1.00 49.44 ? 140 ALA H N   1 
ATOM   5574  C  CA  . ALA E  1 167 ? 59.339  27.697  22.105  1.00 43.25 ? 140 ALA H CA  1 
ATOM   5575  C  C   . ALA E  1 167 ? 58.616  28.252  23.332  1.00 48.32 ? 140 ALA H C   1 
ATOM   5576  O  O   . ALA E  1 167 ? 59.260  28.893  24.171  1.00 52.39 ? 140 ALA H O   1 
ATOM   5577  C  CB  . ALA E  1 167 ? 59.926  28.848  21.278  1.00 45.02 ? 140 ALA H CB  1 
ATOM   5578  N  N   . GLY E  1 168 ? 57.307  28.034  23.458  1.00 46.61 ? 141 GLY H N   1 
ATOM   5579  C  CA  . GLY E  1 168 ? 56.613  28.359  24.690  1.00 53.44 ? 141 GLY H CA  1 
ATOM   5580  C  C   . GLY E  1 168 ? 56.137  29.797  24.786  1.00 50.74 ? 141 GLY H C   1 
ATOM   5581  O  O   . GLY E  1 168 ? 56.095  30.561  23.811  1.00 44.05 ? 141 GLY H O   1 
ATOM   5582  N  N   . SER E  1 169 ? 55.782  30.168  26.018  1.00 42.85 ? 142 SER H N   1 
ATOM   5583  C  CA  . SER E  1 169 ? 55.180  31.467  26.271  1.00 41.23 ? 142 SER H CA  1 
ATOM   5584  C  C   . SER E  1 169 ? 56.195  32.590  26.046  1.00 35.72 ? 142 SER H C   1 
ATOM   5585  O  O   . SER E  1 169 ? 57.402  32.371  25.882  1.00 40.39 ? 142 SER H O   1 
ATOM   5586  C  CB  . SER E  1 169 ? 54.608  31.525  27.686  1.00 39.58 ? 142 SER H CB  1 
ATOM   5587  O  OG  . SER E  1 169 ? 55.583  31.973  28.606  1.00 48.13 ? 142 SER H OG  1 
ATOM   5588  N  N   . ARG E  1 170 ? 55.685  33.813  26.018  1.00 34.94 ? 143 ARG H N   1 
ATOM   5589  C  CA  . ARG E  1 170 ? 56.471  34.966  25.609  1.00 27.06 ? 143 ARG H CA  1 
ATOM   5590  C  C   . ARG E  1 170 ? 56.946  35.697  26.862  1.00 33.14 ? 143 ARG H C   1 
ATOM   5591  O  O   . ARG E  1 170 ? 56.136  36.249  27.613  1.00 32.79 ? 143 ARG H O   1 
ATOM   5592  C  CB  . ARG E  1 170 ? 55.633  35.841  24.675  1.00 30.31 ? 143 ARG H CB  1 
ATOM   5593  C  CG  . ARG E  1 170 ? 54.823  34.977  23.695  1.00 29.69 ? 143 ARG H CG  1 
ATOM   5594  C  CD  . ARG E  1 170 ? 53.994  35.769  22.664  1.00 31.92 ? 143 ARG H CD  1 
ATOM   5595  N  NE  . ARG E  1 170 ? 53.499  34.890  21.610  1.00 33.20 ? 143 ARG H NE  1 
ATOM   5596  C  CZ  . ARG E  1 170 ? 52.890  35.292  20.501  1.00 34.52 ? 143 ARG H CZ  1 
ATOM   5597  N  NH1 . ARG E  1 170 ? 52.686  36.576  20.248  1.00 30.74 ? 143 ARG H NH1 1 
ATOM   5598  N  NH2 . ARG E  1 170 ? 52.489  34.382  19.613  1.00 31.44 ? 143 ARG H NH2 1 
ATOM   5599  N  N   . LEU E  1 171 ? 58.266  35.687  27.093  1.00 28.24 ? 144 LEU H N   1 
ATOM   5600  C  CA  . LEU E  1 171 ? 58.824  36.285  28.306  1.00 26.53 ? 144 LEU H CA  1 
ATOM   5601  C  C   . LEU E  1 171 ? 58.918  37.804  28.212  1.00 29.53 ? 144 LEU H C   1 
ATOM   5602  O  O   . LEU E  1 171 ? 58.624  38.511  29.184  1.00 24.59 ? 144 LEU H O   1 
ATOM   5603  C  CB  . LEU E  1 171 ? 60.204  35.699  28.581  1.00 27.84 ? 144 LEU H CB  1 
ATOM   5604  C  CG  . LEU E  1 171 ? 60.183  34.178  28.777  1.00 35.54 ? 144 LEU H CG  1 
ATOM   5605  C  CD1 . LEU E  1 171 ? 61.532  33.724  29.286  1.00 36.11 ? 144 LEU H CD1 1 
ATOM   5606  C  CD2 . LEU E  1 171 ? 59.042  33.761  29.722  1.00 30.27 ? 144 LEU H CD2 1 
ATOM   5607  N  N   . ALA E  1 172 ? 59.361  38.319  27.069  1.00 24.66 ? 145 ALA H N   1 
ATOM   5608  C  CA  . ALA E  1 172 ? 59.506  39.752  26.878  1.00 21.40 ? 145 ALA H CA  1 
ATOM   5609  C  C   . ALA E  1 172 ? 59.403  40.044  25.389  1.00 25.42 ? 145 ALA H C   1 
ATOM   5610  O  O   . ALA E  1 172 ? 59.607  39.163  24.552  1.00 23.76 ? 145 ALA H O   1 
ATOM   5611  C  CB  . ALA E  1 172 ? 60.837  40.281  27.410  1.00 17.84 ? 145 ALA H CB  1 
ATOM   5612  N  N   . CYS E  1 173 ? 59.119  41.300  25.070  1.00 18.01 ? 146 CYS H N   1 
ATOM   5613  C  CA  . CYS E  1 173 ? 58.996  41.693  23.672  1.00 20.24 ? 146 CYS H CA  1 
ATOM   5614  C  C   . CYS E  1 173 ? 59.127  43.203  23.578  1.00 23.83 ? 146 CYS H C   1 
ATOM   5615  O  O   . CYS E  1 173 ? 59.131  43.914  24.586  1.00 22.01 ? 146 CYS H O   1 
ATOM   5616  C  CB  . CYS E  1 173 ? 57.676  41.209  23.087  1.00 22.45 ? 146 CYS H CB  1 
ATOM   5617  S  SG  . CYS E  1 173 ? 56.263  41.953  23.890  1.00 31.72 ? 146 CYS H SG  1 
ATOM   5618  N  N   . GLY E  1 174 ? 59.236  43.686  22.345  1.00 20.35 ? 147 GLY H N   1 
ATOM   5619  C  CA  . GLY E  1 174 ? 59.268  45.112  22.103  1.00 20.88 ? 147 GLY H CA  1 
ATOM   5620  C  C   . GLY E  1 174 ? 59.090  45.371  20.624  1.00 23.94 ? 147 GLY H C   1 
ATOM   5621  O  O   . GLY E  1 174 ? 59.388  44.493  19.800  1.00 19.86 ? 147 GLY H O   1 
ATOM   5622  N  N   . VAL E  1 175 ? 58.614  46.559  20.272  1.00 17.98 ? 148 VAL H N   1 
ATOM   5623  C  CA  . VAL E  1 175 ? 58.471  46.915  18.860  1.00 15.50 ? 148 VAL H CA  1 
ATOM   5624  C  C   . VAL E  1 175 ? 59.831  47.338  18.333  1.00 19.69 ? 148 VAL H C   1 
ATOM   5625  O  O   . VAL E  1 175 ? 60.587  48.053  19.006  1.00 20.76 ? 148 VAL H O   1 
ATOM   5626  C  CB  . VAL E  1 175 ? 57.428  48.035  18.683  1.00 19.71 ? 148 VAL H CB  1 
ATOM   5627  C  CG1 . VAL E  1 175 ? 57.181  48.297  17.190  1.00 17.94 ? 148 VAL H CG1 1 
ATOM   5628  C  CG2 . VAL E  1 175 ? 56.153  47.664  19.380  1.00 21.88 ? 148 VAL H CG2 1 
ATOM   5629  N  N   . ILE E  1 176 ? 60.152  46.902  17.122  1.00 17.05 ? 149 ILE H N   1 
ATOM   5630  C  CA  . ILE E  1 176 ? 61.438  47.230  16.512  1.00 20.67 ? 149 ILE H CA  1 
ATOM   5631  C  C   . ILE E  1 176 ? 61.336  48.615  15.894  1.00 20.54 ? 149 ILE H C   1 
ATOM   5632  O  O   . ILE E  1 176 ? 60.499  48.852  15.017  1.00 24.87 ? 149 ILE H O   1 
ATOM   5633  C  CB  . ILE E  1 176 ? 61.833  46.176  15.461  1.00 21.84 ? 149 ILE H CB  1 
ATOM   5634  C  CG1 . ILE E  1 176 ? 61.894  44.794  16.126  1.00 23.39 ? 149 ILE H CG1 1 
ATOM   5635  C  CG2 . ILE E  1 176 ? 63.142  46.560  14.766  1.00 20.40 ? 149 ILE H CG2 1 
ATOM   5636  C  CD1 . ILE E  1 176 ? 61.987  43.627  15.148  1.00 21.47 ? 149 ILE H CD1 1 
ATOM   5637  N  N   . GLY E  1 177 ? 62.204  49.517  16.325  1.00 22.69 ? 150 GLY H N   1 
ATOM   5638  C  CA  . GLY E  1 177 ? 62.092  50.895  15.892  1.00 22.54 ? 150 GLY H CA  1 
ATOM   5639  C  C   . GLY E  1 177 ? 63.303  51.393  15.145  1.00 26.57 ? 150 GLY H C   1 
ATOM   5640  O  O   . GLY E  1 177 ? 64.407  50.868  15.313  1.00 22.23 ? 150 GLY H O   1 
ATOM   5641  N  N   . ILE E  1 178 ? 63.110  52.412  14.306  1.00 21.71 ? 151 ILE H N   1 
ATOM   5642  C  CA  . ILE E  1 178 ? 64.234  53.018  13.607  1.00 18.25 ? 151 ILE H CA  1 
ATOM   5643  C  C   . ILE E  1 178 ? 65.151  53.700  14.600  1.00 22.76 ? 151 ILE H C   1 
ATOM   5644  O  O   . ILE E  1 178 ? 64.698  54.410  15.511  1.00 23.83 ? 151 ILE H O   1 
ATOM   5645  C  CB  . ILE E  1 178 ? 63.738  54.012  12.538  1.00 23.28 ? 151 ILE H CB  1 
ATOM   5646  C  CG1 . ILE E  1 178 ? 62.694  53.345  11.646  1.00 32.65 ? 151 ILE H CG1 1 
ATOM   5647  C  CG2 . ILE E  1 178 ? 64.903  54.522  11.690  1.00 31.89 ? 151 ILE H CG2 1 
ATOM   5648  C  CD1 . ILE E  1 178 ? 62.136  54.269  10.568  1.00 35.71 ? 151 ILE H CD1 1 
ATOM   5649  N  N   . ALA E  1 179 ? 66.458  53.520  14.410  1.00 22.62 ? 152 ALA H N   1 
ATOM   5650  C  CA  . ALA E  1 179 ? 67.450  54.052  15.330  1.00 22.75 ? 152 ALA H CA  1 
ATOM   5651  C  C   . ALA E  1 179 ? 68.428  54.940  14.576  1.00 27.50 ? 152 ALA H C   1 
ATOM   5652  O  O   . ALA E  1 179 ? 68.507  54.912  13.346  1.00 29.34 ? 152 ALA H O   1 
ATOM   5653  C  CB  . ALA E  1 179 ? 68.215  52.935  16.047  1.00 28.03 ? 152 ALA H CB  1 
ATOM   5654  N  N   . GLN E  1 180 ? 69.159  55.744  15.338  1.00 28.86 ? 153 GLN H N   1 
ATOM   5655  C  CA  . GLN E  1 180 ? 70.079  56.722  14.775  1.00 31.44 ? 153 GLN H CA  1 
ATOM   5656  C  C   . GLN E  1 180 ? 71.423  56.090  14.449  1.00 51.37 ? 153 GLN H C   1 
ATOM   5657  O  O   . GLN E  1 180 ? 72.022  55.445  15.319  1.00 54.48 ? 153 GLN H O   1 
ATOM   5658  C  CB  . GLN E  1 180 ? 70.300  57.868  15.750  1.00 39.88 ? 153 GLN H CB  1 
ATOM   5659  C  CG  . GLN E  1 180 ? 71.397  58.822  15.341  1.00 37.67 ? 153 GLN H CG  1 
ATOM   5660  C  CD  . GLN E  1 180 ? 71.255  60.173  16.022  1.00 48.75 ? 153 GLN H CD  1 
ATOM   5661  O  OE1 . GLN E  1 180 ? 71.112  61.205  15.365  1.00 54.34 ? 153 GLN H OE1 1 
ATOM   5662  N  NE2 . GLN E  1 180 ? 71.318  60.171  17.351  1.00 50.49 ? 153 GLN H NE2 1 
ATOM   5663  O  OXT . GLN E  1 180 ? 71.947  56.233  13.342  1.00 53.95 ? 153 GLN H OXT 1 
ATOM   5664  N  N   . ALA F  1 28  ? 51.074  49.016  4.886   1.00 38.16 ? 1   ALA E N   1 
ATOM   5665  C  CA  . ALA F  1 28  ? 50.284  48.982  6.118   1.00 29.54 ? 1   ALA E CA  1 
ATOM   5666  C  C   . ALA F  1 28  ? 49.047  49.883  6.047   1.00 24.40 ? 1   ALA E C   1 
ATOM   5667  O  O   . ALA F  1 28  ? 49.111  51.004  5.564   1.00 39.05 ? 1   ALA E O   1 
ATOM   5668  C  CB  . ALA F  1 28  ? 51.151  49.382  7.299   1.00 37.53 ? 1   ALA E CB  1 
ATOM   5669  N  N   . THR F  1 29  ? 47.913  49.356  6.511   1.00 25.62 ? 2   THR E N   1 
ATOM   5670  C  CA  . THR F  1 29  ? 46.673  50.107  6.640   1.00 29.13 ? 2   THR E CA  1 
ATOM   5671  C  C   . THR F  1 29  ? 46.393  50.530  8.071   1.00 24.08 ? 2   THR E C   1 
ATOM   5672  O  O   . THR F  1 29  ? 45.608  51.458  8.281   1.00 23.43 ? 2   THR E O   1 
ATOM   5673  C  CB  . THR F  1 29  ? 45.477  49.267  6.155   1.00 25.77 ? 2   THR E CB  1 
ATOM   5674  N  N   . LYS F  1 30  ? 46.973  49.834  9.043   1.00 24.84 ? 3   LYS E N   1 
ATOM   5675  C  CA  . LYS F  1 30  ? 46.696  50.056  10.453  1.00 24.15 ? 3   LYS E CA  1 
ATOM   5676  C  C   . LYS F  1 30  ? 47.983  50.009  11.250  1.00 21.46 ? 3   LYS E C   1 
ATOM   5677  O  O   . LYS F  1 30  ? 48.883  49.209  10.967  1.00 19.32 ? 3   LYS E O   1 
ATOM   5678  C  CB  . LYS F  1 30  ? 45.714  49.025  11.021  1.00 28.72 ? 3   LYS E CB  1 
ATOM   5679  C  CG  . LYS F  1 30  ? 44.283  49.208  10.540  1.00 34.66 ? 3   LYS E CG  1 
ATOM   5680  C  CD  . LYS F  1 30  ? 43.425  47.989  10.857  1.00 45.31 ? 3   LYS E CD  1 
ATOM   5681  C  CE  . LYS F  1 30  ? 42.584  47.576  9.649   1.00 51.53 ? 3   LYS E CE  1 
ATOM   5682  N  NZ  . LYS F  1 30  ? 41.120  47.698  9.944   1.00 57.31 ? 3   LYS E NZ  1 
ATOM   5683  N  N   . ALA F  1 31  ? 48.065  50.892  12.240  1.00 20.98 ? 4   ALA E N   1 
ATOM   5684  C  CA  . ALA F  1 31  ? 49.185  50.921  13.167  1.00 18.42 ? 4   ALA E CA  1 
ATOM   5685  C  C   . ALA F  1 31  ? 48.632  51.186  14.560  1.00 20.83 ? 4   ALA E C   1 
ATOM   5686  O  O   . ALA F  1 31  ? 47.467  51.574  14.732  1.00 18.94 ? 4   ALA E O   1 
ATOM   5687  C  CB  . ALA F  1 31  ? 50.238  51.974  12.772  1.00 20.23 ? 4   ALA E CB  1 
ATOM   5688  N  N   . VAL F  1 32  ? 49.473  50.953  15.567  1.00 19.86 ? 5   VAL E N   1 
ATOM   5689  C  CA  . VAL F  1 32  ? 49.051  51.133  16.950  1.00 20.19 ? 5   VAL E CA  1 
ATOM   5690  C  C   . VAL F  1 32  ? 50.269  51.486  17.784  1.00 21.87 ? 5   VAL E C   1 
ATOM   5691  O  O   . VAL F  1 32  ? 51.399  51.144  17.443  1.00 20.55 ? 5   VAL E O   1 
ATOM   5692  C  CB  . VAL F  1 32  ? 48.330  49.879  17.495  1.00 22.12 ? 5   VAL E CB  1 
ATOM   5693  C  CG1 . VAL F  1 32  ? 49.317  48.728  17.627  1.00 22.42 ? 5   VAL E CG1 1 
ATOM   5694  C  CG2 . VAL F  1 32  ? 47.664  50.187  18.831  1.00 24.64 ? 5   VAL E CG2 1 
ATOM   5695  N  N   . CYS F  1 33  ? 50.033  52.185  18.890  1.00 18.66 ? 6   CYS E N   1 
ATOM   5696  C  CA  . CYS F  1 33  ? 51.119  52.655  19.726  1.00 16.40 ? 6   CYS E CA  1 
ATOM   5697  C  C   . CYS F  1 33  ? 50.666  52.546  21.172  1.00 21.81 ? 6   CYS E C   1 
ATOM   5698  O  O   . CYS F  1 33  ? 49.579  53.022  21.495  1.00 18.75 ? 6   CYS E O   1 
ATOM   5699  C  CB  . CYS F  1 33  ? 51.468  54.105  19.405  1.00 15.78 ? 6   CYS E CB  1 
ATOM   5700  S  SG  . CYS F  1 33  ? 52.799  54.763  20.412  1.00 23.42 ? 6   CYS E SG  1 
ATOM   5701  N  N   . VAL F  1 34  ? 51.474  51.916  22.021  1.00 18.91 ? 7   VAL E N   1 
ATOM   5702  C  CA  . VAL F  1 34  ? 51.219  51.846  23.463  1.00 16.34 ? 7   VAL E CA  1 
ATOM   5703  C  C   . VAL F  1 34  ? 52.123  52.861  24.142  1.00 19.74 ? 7   VAL E C   1 
ATOM   5704  O  O   . VAL F  1 34  ? 53.349  52.714  24.140  1.00 18.25 ? 7   VAL E O   1 
ATOM   5705  C  CB  . VAL F  1 34  ? 51.447  50.435  24.023  1.00 21.40 ? 7   VAL E CB  1 
ATOM   5706  C  CG1 . VAL F  1 34  ? 51.130  50.407  25.537  1.00 22.59 ? 7   VAL E CG1 1 
ATOM   5707  C  CG2 . VAL F  1 34  ? 50.581  49.414  23.296  1.00 24.59 ? 7   VAL E CG2 1 
ATOM   5708  N  N   A LEU F  1 35  ? 51.519  53.893  24.737  0.59 20.29 ? 8   LEU E N   1 
ATOM   5709  N  N   B LEU F  1 35  ? 51.527  53.887  24.751  0.41 20.26 ? 8   LEU E N   1 
ATOM   5710  C  CA  A LEU F  1 35  ? 52.256  54.947  25.418  0.59 18.20 ? 8   LEU E CA  1 
ATOM   5711  C  CA  B LEU F  1 35  ? 52.288  54.946  25.399  0.41 18.29 ? 8   LEU E CA  1 
ATOM   5712  C  C   A LEU F  1 35  ? 52.510  54.555  26.870  0.59 18.04 ? 8   LEU E C   1 
ATOM   5713  C  C   B LEU F  1 35  ? 52.513  54.587  26.864  0.41 18.11 ? 8   LEU E C   1 
ATOM   5714  O  O   A LEU F  1 35  ? 51.573  54.207  27.590  0.59 21.50 ? 8   LEU E O   1 
ATOM   5715  O  O   B LEU F  1 35  ? 51.561  54.277  27.583  0.41 21.67 ? 8   LEU E O   1 
ATOM   5716  C  CB  A LEU F  1 35  ? 51.476  56.262  25.373  0.59 20.20 ? 8   LEU E CB  1 
ATOM   5717  C  CB  B LEU F  1 35  ? 51.565  56.293  25.294  0.41 20.37 ? 8   LEU E CB  1 
ATOM   5718  C  CG  A LEU F  1 35  ? 51.155  56.766  23.963  0.59 21.95 ? 8   LEU E CG  1 
ATOM   5719  C  CG  B LEU F  1 35  ? 51.540  56.945  23.900  0.41 21.60 ? 8   LEU E CG  1 
ATOM   5720  C  CD1 A LEU F  1 35  ? 50.081  57.838  24.027  0.59 18.98 ? 8   LEU E CD1 1 
ATOM   5721  C  CD1 B LEU F  1 35  ? 50.503  56.268  23.016  0.41 19.72 ? 8   LEU E CD1 1 
ATOM   5722  C  CD2 A LEU F  1 35  ? 52.417  57.290  23.307  0.59 18.89 ? 8   LEU E CD2 1 
ATOM   5723  C  CD2 B LEU F  1 35  ? 51.306  58.455  23.955  0.41 19.36 ? 8   LEU E CD2 1 
ATOM   5724  N  N   . LYS F  1 36  ? 53.774  54.620  27.289  1.00 23.27 ? 9   LYS E N   1 
ATOM   5725  C  CA  . LYS F  1 36  ? 54.159  54.411  28.683  1.00 26.34 ? 9   LYS E CA  1 
ATOM   5726  C  C   . LYS F  1 36  ? 55.248  55.407  29.031  1.00 19.64 ? 9   LYS E C   1 
ATOM   5727  O  O   . LYS F  1 36  ? 55.954  55.911  28.159  1.00 23.24 ? 9   LYS E O   1 
ATOM   5728  C  CB  . LYS F  1 36  ? 54.703  52.999  28.960  1.00 28.55 ? 9   LYS E CB  1 
ATOM   5729  C  CG  . LYS F  1 36  ? 53.676  51.906  28.932  1.00 36.84 ? 9   LYS E CG  1 
ATOM   5730  C  CD  . LYS F  1 36  ? 54.282  50.580  28.500  1.00 42.46 ? 9   LYS E CD  1 
ATOM   5731  C  CE  . LYS F  1 36  ? 53.175  49.554  28.237  1.00 41.42 ? 9   LYS E CE  1 
ATOM   5732  N  NZ  . LYS F  1 36  ? 52.459  49.181  29.473  1.00 46.10 ? 9   LYS E NZ  1 
ATOM   5733  N  N   . GLY F  1 37  ? 55.422  55.660  30.325  1.00 19.88 ? 10  GLY E N   1 
ATOM   5734  C  CA  . GLY F  1 37  ? 56.453  56.584  30.735  1.00 18.35 ? 10  GLY E CA  1 
ATOM   5735  C  C   . GLY F  1 37  ? 56.881  56.321  32.165  1.00 28.37 ? 10  GLY E C   1 
ATOM   5736  O  O   . GLY F  1 37  ? 56.529  55.304  32.757  1.00 26.67 ? 10  GLY E O   1 
ATOM   5737  N  N   . ASP F  1 38  ? 57.638  57.271  32.710  1.00 29.14 ? 11  ASP E N   1 
ATOM   5738  C  CA  . ASP F  1 38  ? 58.140  57.163  34.085  1.00 38.21 ? 11  ASP E CA  1 
ATOM   5739  C  C   . ASP F  1 38  ? 57.054  57.442  35.122  1.00 37.69 ? 11  ASP E C   1 
ATOM   5740  O  O   . ASP F  1 38  ? 57.149  56.982  36.272  1.00 34.82 ? 11  ASP E O   1 
ATOM   5741  C  CB  . ASP F  1 38  ? 59.294  58.140  34.267  1.00 34.61 ? 11  ASP E CB  1 
ATOM   5742  C  CG  . ASP F  1 38  ? 60.601  57.584  33.776  1.00 59.48 ? 11  ASP E CG  1 
ATOM   5743  O  OD1 . ASP F  1 38  ? 60.766  56.341  33.815  1.00 67.27 ? 11  ASP E OD1 1 
ATOM   5744  O  OD2 . ASP F  1 38  ? 61.445  58.387  33.318  1.00 60.30 ? 11  ASP E OD2 1 
ATOM   5745  N  N   . GLY F  1 39  ? 56.037  58.206  34.752  1.00 26.41 ? 12  GLY E N   1 
ATOM   5746  C  CA  . GLY F  1 39  ? 54.957  58.523  35.649  1.00 25.84 ? 12  GLY E CA  1 
ATOM   5747  C  C   . GLY F  1 39  ? 53.712  57.749  35.285  1.00 22.28 ? 12  GLY E C   1 
ATOM   5748  O  O   . GLY F  1 39  ? 53.774  56.645  34.745  1.00 25.15 ? 12  GLY E O   1 
ATOM   5749  N  N   . PRO F  1 40  ? 52.548  58.328  35.578  1.00 21.70 ? 13  PRO E N   1 
ATOM   5750  C  CA  . PRO F  1 40  ? 51.275  57.621  35.392  1.00 24.25 ? 13  PRO E CA  1 
ATOM   5751  C  C   . PRO F  1 40  ? 50.661  57.723  34.006  1.00 20.33 ? 13  PRO E C   1 
ATOM   5752  O  O   . PRO F  1 40  ? 49.575  57.172  33.807  1.00 25.82 ? 13  PRO E O   1 
ATOM   5753  C  CB  . PRO F  1 40  ? 50.368  58.325  36.402  1.00 25.50 ? 13  PRO E CB  1 
ATOM   5754  C  CG  . PRO F  1 40  ? 50.874  59.728  36.401  1.00 25.67 ? 13  PRO E CG  1 
ATOM   5755  C  CD  . PRO F  1 40  ? 52.370  59.625  36.260  1.00 23.19 ? 13  PRO E CD  1 
ATOM   5756  N  N   . VAL F  1 41  ? 51.276  58.433  33.066  1.00 21.33 ? 14  VAL E N   1 
ATOM   5757  C  CA  . VAL F  1 41  ? 50.627  58.624  31.774  1.00 21.27 ? 14  VAL E CA  1 
ATOM   5758  C  C   . VAL F  1 41  ? 50.730  57.340  30.967  1.00 20.02 ? 14  VAL E C   1 
ATOM   5759  O  O   . VAL F  1 41  ? 51.821  56.793  30.778  1.00 23.60 ? 14  VAL E O   1 
ATOM   5760  C  CB  . VAL F  1 41  ? 51.249  59.804  31.023  1.00 20.70 ? 14  VAL E CB  1 
ATOM   5761  C  CG1 . VAL F  1 41  ? 50.622  59.913  29.632  1.00 15.80 ? 14  VAL E CG1 1 
ATOM   5762  C  CG2 . VAL F  1 41  ? 51.041  61.087  31.810  1.00 24.73 ? 14  VAL E CG2 1 
ATOM   5763  N  N   . GLN F  1 42  ? 49.591  56.854  30.488  1.00 22.95 ? 15  GLN E N   1 
ATOM   5764  C  CA  . GLN F  1 42  ? 49.580  55.677  29.632  1.00 25.41 ? 15  GLN E CA  1 
ATOM   5765  C  C   . GLN F  1 42  ? 48.405  55.773  28.686  1.00 23.27 ? 15  GLN E C   1 
ATOM   5766  O  O   . GLN F  1 42  ? 47.405  56.439  28.966  1.00 23.55 ? 15  GLN E O   1 
ATOM   5767  C  CB  . GLN F  1 42  ? 49.484  54.369  30.425  1.00 29.08 ? 15  GLN E CB  1 
ATOM   5768  C  CG  . GLN F  1 42  ? 48.176  54.205  31.153  1.00 31.96 ? 15  GLN E CG  1 
ATOM   5769  C  CD  . GLN F  1 42  ? 48.104  52.899  31.922  1.00 48.84 ? 15  GLN E CD  1 
ATOM   5770  O  OE1 . GLN F  1 42  ? 48.386  52.844  33.126  1.00 47.57 ? 15  GLN E OE1 1 
ATOM   5771  N  NE2 . GLN F  1 42  ? 47.733  51.826  31.218  1.00 54.27 ? 15  GLN E NE2 1 
ATOM   5772  N  N   . GLY F  1 43  ? 48.513  55.090  27.561  1.00 22.37 ? 16  GLY E N   1 
ATOM   5773  C  CA  . GLY F  1 43  ? 47.424  55.163  26.619  1.00 22.11 ? 16  GLY E CA  1 
ATOM   5774  C  C   . GLY F  1 43  ? 47.684  54.255  25.449  1.00 20.00 ? 16  GLY E C   1 
ATOM   5775  O  O   . GLY F  1 43  ? 48.762  53.663  25.317  1.00 17.65 ? 16  GLY E O   1 
ATOM   5776  N  N   . ILE F  1 44  ? 46.658  54.153  24.611  1.00 20.62 ? 17  ILE E N   1 
ATOM   5777  C  CA  . ILE F  1 44  ? 46.689  53.386  23.381  1.00 21.52 ? 17  ILE E CA  1 
ATOM   5778  C  C   . ILE F  1 44  ? 46.220  54.305  22.266  1.00 20.58 ? 17  ILE E C   1 
ATOM   5779  O  O   . ILE F  1 44  ? 45.125  54.879  22.346  1.00 22.55 ? 17  ILE E O   1 
ATOM   5780  C  CB  . ILE F  1 44  ? 45.796  52.143  23.479  1.00 20.35 ? 17  ILE E CB  1 
ATOM   5781  C  CG1 . ILE F  1 44  ? 46.360  51.195  24.554  1.00 27.62 ? 17  ILE E CG1 1 
ATOM   5782  C  CG2 . ILE F  1 44  ? 45.655  51.485  22.097  1.00 22.98 ? 17  ILE E CG2 1 
ATOM   5783  C  CD1 . ILE F  1 44  ? 45.609  49.881  24.655  1.00 31.95 ? 17  ILE E CD1 1 
ATOM   5784  N  N   . ILE F  1 45  ? 47.038  54.458  21.231  1.00 19.27 ? 18  ILE E N   1 
ATOM   5785  C  CA  . ILE F  1 45  ? 46.676  55.282  20.083  1.00 16.18 ? 18  ILE E CA  1 
ATOM   5786  C  C   . ILE F  1 45  ? 46.685  54.416  18.833  1.00 21.52 ? 18  ILE E C   1 
ATOM   5787  O  O   . ILE F  1 45  ? 47.679  53.733  18.554  1.00 20.74 ? 18  ILE E O   1 
ATOM   5788  C  CB  . ILE F  1 45  ? 47.625  56.485  19.924  1.00 18.24 ? 18  ILE E CB  1 
ATOM   5789  C  CG1 . ILE F  1 45  ? 47.521  57.434  21.146  1.00 17.64 ? 18  ILE E CG1 1 
ATOM   5790  C  CG2 . ILE F  1 45  ? 47.343  57.200  18.605  1.00 17.71 ? 18  ILE E CG2 1 
ATOM   5791  C  CD1 . ILE F  1 45  ? 46.129  58.118  21.322  1.00 20.22 ? 18  ILE E CD1 1 
ATOM   5792  N  N   . ASN F  1 46  ? 45.588  54.470  18.071  1.00 22.18 ? 19  ASN E N   1 
ATOM   5793  C  CA  . ASN F  1 46  ? 45.414  53.734  16.824  1.00 20.62 ? 19  ASN E CA  1 
ATOM   5794  C  C   . ASN F  1 46  ? 45.621  54.666  15.637  1.00 20.82 ? 19  ASN E C   1 
ATOM   5795  O  O   . ASN F  1 46  ? 45.325  55.863  15.712  1.00 20.37 ? 19  ASN E O   1 
ATOM   5796  C  CB  . ASN F  1 46  ? 44.008  53.126  16.732  1.00 17.63 ? 19  ASN E CB  1 
ATOM   5797  C  CG  . ASN F  1 46  ? 43.621  52.366  17.964  1.00 28.94 ? 19  ASN E CG  1 
ATOM   5798  O  OD1 . ASN F  1 46  ? 42.874  52.854  18.820  1.00 30.44 ? 19  ASN E OD1 1 
ATOM   5799  N  ND2 . ASN F  1 46  ? 44.139  51.171  18.079  1.00 21.92 ? 19  ASN E ND2 1 
ATOM   5800  N  N   . PHE F  1 47  ? 46.112  54.097  14.527  1.00 19.34 ? 20  PHE E N   1 
ATOM   5801  C  CA  . PHE F  1 47  ? 46.301  54.809  13.275  1.00 19.51 ? 20  PHE E CA  1 
ATOM   5802  C  C   . PHE F  1 47  ? 45.649  53.985  12.177  1.00 20.69 ? 20  PHE E C   1 
ATOM   5803  O  O   . PHE F  1 47  ? 45.793  52.757  12.152  1.00 21.76 ? 20  PHE E O   1 
ATOM   5804  C  CB  . PHE F  1 47  ? 47.778  55.000  12.930  1.00 19.72 ? 20  PHE E CB  1 
ATOM   5805  C  CG  . PHE F  1 47  ? 48.559  55.751  13.965  1.00 22.77 ? 20  PHE E CG  1 
ATOM   5806  C  CD1 . PHE F  1 47  ? 49.000  55.112  15.133  1.00 21.63 ? 20  PHE E CD1 1 
ATOM   5807  C  CD2 . PHE F  1 47  ? 48.869  57.084  13.768  1.00 19.73 ? 20  PHE E CD2 1 
ATOM   5808  C  CE1 . PHE F  1 47  ? 49.731  55.807  16.084  1.00 21.06 ? 20  PHE E CE1 1 
ATOM   5809  C  CE2 . PHE F  1 47  ? 49.603  57.791  14.718  1.00 24.02 ? 20  PHE E CE2 1 
ATOM   5810  C  CZ  . PHE F  1 47  ? 50.029  57.147  15.875  1.00 19.87 ? 20  PHE E CZ  1 
ATOM   5811  N  N   . GLU F  1 48  ? 44.920  54.648  11.293  1.00 18.10 ? 21  GLU E N   1 
ATOM   5812  C  CA  . GLU F  1 48  ? 44.325  53.954  10.152  1.00 20.28 ? 21  GLU E CA  1 
ATOM   5813  C  C   . GLU F  1 48  ? 44.429  54.814  8.909   1.00 21.75 ? 21  GLU E C   1 
ATOM   5814  O  O   . GLU F  1 48  ? 44.112  56.006  8.934   1.00 22.91 ? 21  GLU E O   1 
ATOM   5815  C  CB  . GLU F  1 48  ? 42.862  53.609  10.432  1.00 25.32 ? 21  GLU E CB  1 
ATOM   5816  C  CG  . GLU F  1 48  ? 42.167  52.889  9.313   1.00 34.53 ? 21  GLU E CG  1 
ATOM   5817  C  CD  . GLU F  1 48  ? 40.771  52.499  9.729   1.00 53.93 ? 21  GLU E CD  1 
ATOM   5818  O  OE1 . GLU F  1 48  ? 40.630  51.486  10.447  1.00 63.83 ? 21  GLU E OE1 1 
ATOM   5819  O  OE2 . GLU F  1 48  ? 39.828  53.258  9.417   1.00 61.20 ? 21  GLU E OE2 1 
ATOM   5820  N  N   . GLN F  1 49  ? 44.862  54.195  7.810   1.00 24.12 ? 22  GLN E N   1 
ATOM   5821  C  CA  . GLN F  1 49  ? 45.027  54.891  6.541   1.00 20.50 ? 22  GLN E CA  1 
ATOM   5822  C  C   . GLN F  1 49  ? 44.492  53.934  5.476   1.00 27.09 ? 22  GLN E C   1 
ATOM   5823  O  O   . GLN F  1 49  ? 45.203  53.028  5.037   1.00 27.94 ? 22  GLN E O   1 
ATOM   5824  C  CB  . GLN F  1 49  ? 46.477  55.269  6.289   1.00 24.88 ? 22  GLN E CB  1 
ATOM   5825  C  CG  . GLN F  1 49  ? 46.695  56.147  5.055   1.00 24.37 ? 22  GLN E CG  1 
ATOM   5826  C  CD  . GLN F  1 49  ? 48.156  56.441  4.841   1.00 24.95 ? 22  GLN E CD  1 
ATOM   5827  O  OE1 . GLN F  1 49  ? 49.015  55.619  5.182   1.00 23.08 ? 22  GLN E OE1 1 
ATOM   5828  N  NE2 . GLN F  1 49  ? 48.459  57.601  4.276   1.00 26.00 ? 22  GLN E NE2 1 
ATOM   5829  N  N   . LYS F  1 50  ? 43.227  54.118  5.107   1.00 29.94 ? 23  LYS E N   1 
ATOM   5830  C  CA  . LYS F  1 50  ? 42.601  53.211  4.149   1.00 38.12 ? 23  LYS E CA  1 
ATOM   5831  C  C   . LYS F  1 50  ? 43.267  53.279  2.784   1.00 34.66 ? 23  LYS E C   1 
ATOM   5832  O  O   . LYS F  1 50  ? 43.373  52.259  2.094   1.00 40.42 ? 23  LYS E O   1 
ATOM   5833  C  CB  . LYS F  1 50  ? 41.110  53.518  4.029   1.00 38.08 ? 23  LYS E CB  1 
ATOM   5834  C  CG  . LYS F  1 50  ? 40.258  52.678  4.971   1.00 49.41 ? 23  LYS E CG  1 
ATOM   5835  C  CD  . LYS F  1 50  ? 38.983  53.380  5.405   1.00 45.04 ? 23  LYS E CD  1 
ATOM   5836  C  CE  . LYS F  1 50  ? 38.549  52.883  6.776   1.00 52.16 ? 23  LYS E CE  1 
ATOM   5837  N  NZ  . LYS F  1 50  ? 37.689  51.655  6.703   1.00 55.81 ? 23  LYS E NZ  1 
ATOM   5838  N  N   . GLU F  1 51  ? 43.744  54.454  2.389   1.00 33.63 ? 24  GLU E N   1 
ATOM   5839  C  CA  . GLU F  1 51  ? 44.352  54.648  1.080   1.00 33.48 ? 24  GLU E CA  1 
ATOM   5840  C  C   . GLU F  1 51  ? 45.689  55.345  1.253   1.00 33.74 ? 24  GLU E C   1 
ATOM   5841  O  O   . GLU F  1 51  ? 45.798  56.305  2.021   1.00 31.99 ? 24  GLU E O   1 
ATOM   5842  C  CB  . GLU F  1 51  ? 43.437  55.466  0.168   1.00 37.96 ? 24  GLU E CB  1 
ATOM   5843  C  CG  . GLU F  1 51  ? 42.074  54.806  -0.027  1.00 49.16 ? 24  GLU E CG  1 
ATOM   5844  C  CD  . GLU F  1 51  ? 42.150  53.578  -0.937  1.00 69.19 ? 24  GLU E CD  1 
ATOM   5845  O  OE1 . GLU F  1 51  ? 41.313  52.653  -0.782  1.00 68.23 ? 24  GLU E OE1 1 
ATOM   5846  O  OE2 . GLU F  1 51  ? 43.075  53.526  -1.782  1.00 62.85 ? 24  GLU E OE2 1 
ATOM   5847  N  N   . SER F  1 52  ? 46.705  54.864  0.534   1.00 32.60 ? 25  SER E N   1 
ATOM   5848  C  CA  . SER F  1 52  ? 48.055  55.380  0.732   1.00 38.01 ? 25  SER E CA  1 
ATOM   5849  C  C   . SER F  1 52  ? 48.190  56.850  0.360   1.00 33.78 ? 25  SER E C   1 
ATOM   5850  O  O   . SER F  1 52  ? 49.154  57.494  0.786   1.00 36.84 ? 25  SER E O   1 
ATOM   5851  C  CB  . SER F  1 52  ? 49.065  54.550  -0.066  1.00 42.52 ? 25  SER E CB  1 
ATOM   5852  O  OG  . SER F  1 52  ? 48.859  54.688  -1.460  1.00 39.94 ? 25  SER E OG  1 
ATOM   5853  N  N   . ASN F  1 53  ? 47.255  57.401  -0.413  1.00 34.31 ? 26  ASN E N   1 
ATOM   5854  C  CA  . ASN F  1 53  ? 47.271  58.824  -0.744  1.00 45.62 ? 26  ASN E CA  1 
ATOM   5855  C  C   . ASN F  1 53  ? 46.253  59.622  0.068   1.00 43.70 ? 26  ASN E C   1 
ATOM   5856  O  O   . ASN F  1 53  ? 45.927  60.758  -0.301  1.00 39.50 ? 26  ASN E O   1 
ATOM   5857  C  CB  . ASN F  1 53  ? 47.019  59.022  -2.242  1.00 37.40 ? 26  ASN E CB  1 
ATOM   5858  C  CG  . ASN F  1 53  ? 45.618  58.571  -2.671  1.00 47.40 ? 26  ASN E CG  1 
ATOM   5859  O  OD1 . ASN F  1 53  ? 44.955  57.803  -1.971  1.00 44.04 ? 26  ASN E OD1 1 
ATOM   5860  N  ND2 . ASN F  1 53  ? 45.177  59.034  -3.840  1.00 50.17 ? 26  ASN E ND2 1 
ATOM   5861  N  N   . GLY F  1 54  ? 45.727  59.050  1.151   1.00 31.97 ? 27  GLY E N   1 
ATOM   5862  C  CA  . GLY F  1 54  ? 44.678  59.696  1.903   1.00 31.44 ? 27  GLY E CA  1 
ATOM   5863  C  C   . GLY F  1 54  ? 45.137  59.987  3.315   1.00 26.57 ? 27  GLY E C   1 
ATOM   5864  O  O   . GLY F  1 54  ? 46.255  59.640  3.708   1.00 25.96 ? 27  GLY E O   1 
ATOM   5865  N  N   . PRO F  1 55  ? 44.284  60.636  4.103   1.00 27.72 ? 28  PRO E N   1 
ATOM   5866  C  CA  . PRO F  1 55  ? 44.682  61.016  5.457   1.00 26.11 ? 28  PRO E CA  1 
ATOM   5867  C  C   . PRO F  1 55  ? 44.781  59.813  6.382   1.00 29.14 ? 28  PRO E C   1 
ATOM   5868  O  O   . PRO F  1 55  ? 44.213  58.742  6.139   1.00 23.46 ? 28  PRO E O   1 
ATOM   5869  C  CB  . PRO F  1 55  ? 43.558  61.964  5.899   1.00 27.17 ? 28  PRO E CB  1 
ATOM   5870  C  CG  . PRO F  1 55  ? 42.382  61.484  5.156   1.00 34.21 ? 28  PRO E CG  1 
ATOM   5871  C  CD  . PRO F  1 55  ? 42.905  61.053  3.806   1.00 26.48 ? 28  PRO E CD  1 
ATOM   5872  N  N   . VAL F  1 56  ? 45.531  60.013  7.469   1.00 21.83 ? 29  VAL E N   1 
ATOM   5873  C  CA  . VAL F  1 56  ? 45.647  59.030  8.533   1.00 20.81 ? 29  VAL E CA  1 
ATOM   5874  C  C   . VAL F  1 56  ? 44.700  59.440  9.649   1.00 24.03 ? 29  VAL E C   1 
ATOM   5875  O  O   . VAL F  1 56  ? 44.774  60.565  10.149  1.00 23.50 ? 29  VAL E O   1 
ATOM   5876  C  CB  . VAL F  1 56  ? 47.088  58.935  9.058   1.00 19.59 ? 29  VAL E CB  1 
ATOM   5877  C  CG1 . VAL F  1 56  ? 47.171  57.840  10.133  1.00 19.98 ? 29  VAL E CG1 1 
ATOM   5878  C  CG2 . VAL F  1 56  ? 48.030  58.626  7.918   1.00 19.35 ? 29  VAL E CG2 1 
ATOM   5879  N  N   . LYS F  1 57  ? 43.791  58.553  10.020  1.00 19.14 ? 30  LYS E N   1 
ATOM   5880  C  CA  . LYS F  1 57  ? 42.983  58.769  11.209  1.00 19.29 ? 30  LYS E CA  1 
ATOM   5881  C  C   . LYS F  1 57  ? 43.765  58.318  12.438  1.00 21.71 ? 30  LYS E C   1 
ATOM   5882  O  O   . LYS F  1 57  ? 44.341  57.231  12.446  1.00 22.14 ? 30  LYS E O   1 
ATOM   5883  C  CB  . LYS F  1 57  ? 41.664  58.000  11.100  1.00 26.35 ? 30  LYS E CB  1 
ATOM   5884  C  CG  . LYS F  1 57  ? 40.637  58.418  12.142  1.00 39.45 ? 30  LYS E CG  1 
ATOM   5885  C  CD  . LYS F  1 57  ? 40.443  59.949  12.158  1.00 50.12 ? 30  LYS E CD  1 
ATOM   5886  C  CE  . LYS F  1 57  ? 39.866  60.454  13.499  1.00 43.81 ? 30  LYS E CE  1 
ATOM   5887  N  NZ  . LYS F  1 57  ? 39.167  61.787  13.371  1.00 53.58 ? 30  LYS E NZ  1 
ATOM   5888  N  N   . VAL F  1 58  ? 43.783  59.162  13.470  1.00 21.44 ? 31  VAL E N   1 
ATOM   5889  C  CA  . VAL F  1 58  ? 44.518  58.926  14.709  1.00 18.39 ? 31  VAL E CA  1 
ATOM   5890  C  C   . VAL F  1 58  ? 43.518  59.033  15.852  1.00 22.63 ? 31  VAL E C   1 
ATOM   5891  O  O   . VAL F  1 58  ? 42.876  60.078  16.016  1.00 22.62 ? 31  VAL E O   1 
ATOM   5892  C  CB  . VAL F  1 58  ? 45.654  59.950  14.889  1.00 17.58 ? 31  VAL E CB  1 
ATOM   5893  C  CG1 . VAL F  1 58  ? 46.482  59.639  16.135  1.00 18.34 ? 31  VAL E CG1 1 
ATOM   5894  C  CG2 . VAL F  1 58  ? 46.540  60.013  13.623  1.00 19.36 ? 31  VAL E CG2 1 
ATOM   5895  N  N   . TRP F  1 59  ? 43.374  57.967  16.641  1.00 22.58 ? 32  TRP E N   1 
ATOM   5896  C  CA  . TRP F  1 59  ? 42.383  58.038  17.707  1.00 23.26 ? 32  TRP E CA  1 
ATOM   5897  C  C   . TRP F  1 59  ? 42.741  57.068  18.826  1.00 22.20 ? 32  TRP E C   1 
ATOM   5898  O  O   . TRP F  1 59  ? 43.452  56.082  18.631  1.00 23.25 ? 32  TRP E O   1 
ATOM   5899  C  CB  . TRP F  1 59  ? 40.966  57.757  17.182  1.00 23.70 ? 32  TRP E CB  1 
ATOM   5900  C  CG  . TRP F  1 59  ? 40.680  56.283  16.998  1.00 25.58 ? 32  TRP E CG  1 
ATOM   5901  C  CD1 . TRP F  1 59  ? 40.034  55.454  17.870  1.00 26.62 ? 32  TRP E CD1 1 
ATOM   5902  C  CD2 . TRP F  1 59  ? 41.036  55.484  15.873  1.00 26.19 ? 32  TRP E CD2 1 
ATOM   5903  N  NE1 . TRP F  1 59  ? 39.983  54.182  17.363  1.00 31.80 ? 32  TRP E NE1 1 
ATOM   5904  C  CE2 . TRP F  1 59  ? 40.591  54.172  16.135  1.00 28.30 ? 32  TRP E CE2 1 
ATOM   5905  C  CE3 . TRP F  1 59  ? 41.706  55.747  14.673  1.00 26.39 ? 32  TRP E CE3 1 
ATOM   5906  C  CZ2 . TRP F  1 59  ? 40.775  53.127  15.232  1.00 25.06 ? 32  TRP E CZ2 1 
ATOM   5907  C  CZ3 . TRP F  1 59  ? 41.901  54.705  13.775  1.00 28.07 ? 32  TRP E CZ3 1 
ATOM   5908  C  CH2 . TRP F  1 59  ? 41.433  53.408  14.060  1.00 30.52 ? 32  TRP E CH2 1 
ATOM   5909  N  N   . GLY F  1 60  ? 42.227  57.360  20.006  1.00 21.96 ? 33  GLY E N   1 
ATOM   5910  C  CA  . GLY F  1 60  ? 42.481  56.499  21.139  1.00 17.47 ? 33  GLY E CA  1 
ATOM   5911  C  C   . GLY F  1 60  ? 42.338  57.304  22.413  1.00 23.60 ? 33  GLY E C   1 
ATOM   5912  O  O   . GLY F  1 60  ? 41.751  58.380  22.419  1.00 23.80 ? 33  GLY E O   1 
ATOM   5913  N  N   . SER F  1 61  ? 42.896  56.771  23.482  1.00 24.48 ? 34  SER E N   1 
ATOM   5914  C  CA  . SER F  1 61  ? 42.687  57.417  24.766  1.00 23.50 ? 34  SER E CA  1 
ATOM   5915  C  C   . SER F  1 61  ? 43.992  57.423  25.537  1.00 23.99 ? 34  SER E C   1 
ATOM   5916  O  O   . SER F  1 61  ? 44.694  56.407  25.570  1.00 22.75 ? 34  SER E O   1 
ATOM   5917  C  CB  . SER F  1 61  ? 41.583  56.696  25.546  1.00 30.25 ? 34  SER E CB  1 
ATOM   5918  O  OG  . SER F  1 61  ? 41.162  57.495  26.627  1.00 43.71 ? 34  SER E OG  1 
ATOM   5919  N  N   . ILE F  1 62  ? 44.335  58.574  26.119  1.00 21.23 ? 35  ILE E N   1 
ATOM   5920  C  CA  . ILE F  1 62  ? 45.482  58.709  27.009  1.00 20.31 ? 35  ILE E CA  1 
ATOM   5921  C  C   . ILE F  1 62  ? 44.975  59.161  28.367  1.00 28.60 ? 35  ILE E C   1 
ATOM   5922  O  O   . ILE F  1 62  ? 44.246  60.155  28.449  1.00 23.63 ? 35  ILE E O   1 
ATOM   5923  C  CB  . ILE F  1 62  ? 46.502  59.732  26.486  1.00 19.79 ? 35  ILE E CB  1 
ATOM   5924  C  CG1 . ILE F  1 62  ? 46.821  59.487  25.007  1.00 20.48 ? 35  ILE E CG1 1 
ATOM   5925  C  CG2 . ILE F  1 62  ? 47.767  59.704  27.342  1.00 17.22 ? 35  ILE E CG2 1 
ATOM   5926  C  CD1 . ILE F  1 62  ? 47.718  60.553  24.443  1.00 23.43 ? 35  ILE E CD1 1 
ATOM   5927  N  N   . LYS F  1 63  ? 45.388  58.468  29.427  1.00 28.69 ? 36  LYS E N   1 
ATOM   5928  C  CA  . LYS F  1 63  ? 44.987  58.843  30.781  1.00 29.70 ? 36  LYS E CA  1 
ATOM   5929  C  C   . LYS F  1 63  ? 46.205  59.162  31.640  1.00 25.98 ? 36  LYS E C   1 
ATOM   5930  O  O   . LYS F  1 63  ? 47.356  59.040  31.212  1.00 23.36 ? 36  LYS E O   1 
ATOM   5931  C  CB  . LYS F  1 63  ? 44.143  57.751  31.447  1.00 31.74 ? 36  LYS E CB  1 
ATOM   5932  C  CG  . LYS F  1 63  ? 44.555  56.327  31.226  1.00 36.55 ? 36  LYS E CG  1 
ATOM   5933  C  CD  . LYS F  1 63  ? 43.362  55.409  31.564  1.00 45.33 ? 36  LYS E CD  1 
ATOM   5934  C  CE  . LYS F  1 63  ? 43.723  53.926  31.617  1.00 41.50 ? 36  LYS E CE  1 
ATOM   5935  N  NZ  . LYS F  1 63  ? 45.102  53.696  32.106  1.00 46.03 ? 36  LYS E NZ  1 
ATOM   5936  N  N   . GLY F  1 64  ? 45.943  59.605  32.872  1.00 23.41 ? 37  GLY E N   1 
ATOM   5937  C  CA  . GLY F  1 64  ? 47.018  60.037  33.742  1.00 19.89 ? 37  GLY E CA  1 
ATOM   5938  C  C   . GLY F  1 64  ? 47.564  61.420  33.467  1.00 21.50 ? 37  GLY E C   1 
ATOM   5939  O  O   . GLY F  1 64  ? 48.644  61.754  33.977  1.00 22.30 ? 37  GLY E O   1 
ATOM   5940  N  N   . LEU F  1 65  ? 46.857  62.236  32.679  1.00 23.40 ? 38  LEU E N   1 
ATOM   5941  C  CA  . LEU F  1 65  ? 47.300  63.572  32.299  1.00 22.46 ? 38  LEU E CA  1 
ATOM   5942  C  C   . LEU F  1 65  ? 46.673  64.636  33.193  1.00 24.59 ? 38  LEU E C   1 
ATOM   5943  O  O   . LEU F  1 65  ? 45.533  64.500  33.629  1.00 27.39 ? 38  LEU E O   1 
ATOM   5944  C  CB  . LEU F  1 65  ? 46.907  63.884  30.848  1.00 19.59 ? 38  LEU E CB  1 
ATOM   5945  C  CG  . LEU F  1 65  ? 47.561  62.984  29.799  1.00 21.26 ? 38  LEU E CG  1 
ATOM   5946  C  CD1 . LEU F  1 65  ? 46.821  63.157  28.446  1.00 22.35 ? 38  LEU E CD1 1 
ATOM   5947  C  CD2 . LEU F  1 65  ? 48.999  63.390  29.671  1.00 20.35 ? 38  LEU E CD2 1 
ATOM   5948  N  N   . THR F  1 66  ? 47.411  65.724  33.403  1.00 22.56 ? 39  THR E N   1 
ATOM   5949  C  CA  . THR F  1 66  ? 46.826  66.940  33.954  1.00 28.18 ? 39  THR E CA  1 
ATOM   5950  C  C   . THR F  1 66  ? 45.879  67.580  32.949  1.00 30.94 ? 39  THR E C   1 
ATOM   5951  O  O   . THR F  1 66  ? 46.110  67.556  31.732  1.00 25.18 ? 39  THR E O   1 
ATOM   5952  C  CB  . THR F  1 66  ? 47.915  67.940  34.346  1.00 28.80 ? 39  THR E CB  1 
ATOM   5953  O  OG1 . THR F  1 66  ? 48.679  68.297  33.186  1.00 33.35 ? 39  THR E OG1 1 
ATOM   5954  C  CG2 . THR F  1 66  ? 48.841  67.331  35.376  1.00 30.37 ? 39  THR E CG2 1 
ATOM   5955  N  N   . GLU F  1 67  ? 44.798  68.158  33.472  1.00 27.25 ? 40  GLU E N   1 
ATOM   5956  C  CA  . GLU F  1 67  ? 43.774  68.744  32.617  1.00 26.96 ? 40  GLU E CA  1 
ATOM   5957  C  C   . GLU F  1 67  ? 44.364  69.865  31.775  1.00 28.79 ? 40  GLU E C   1 
ATOM   5958  O  O   . GLU F  1 67  ? 45.213  70.629  32.238  1.00 29.06 ? 40  GLU E O   1 
ATOM   5959  C  CB  . GLU F  1 67  ? 42.609  69.269  33.473  1.00 35.43 ? 40  GLU E CB  1 
ATOM   5960  C  CG  . GLU F  1 67  ? 41.729  70.302  32.758  1.00 35.04 ? 40  GLU E CG  1 
ATOM   5961  C  CD  . GLU F  1 67  ? 40.523  70.722  33.596  1.00 48.26 ? 40  GLU E CD  1 
ATOM   5962  O  OE1 . GLU F  1 67  ? 40.689  70.900  34.824  1.00 49.84 ? 40  GLU E OE1 1 
ATOM   5963  O  OE2 . GLU F  1 67  ? 39.421  70.898  33.016  1.00 48.73 ? 40  GLU E OE2 1 
ATOM   5964  N  N   . GLY F  1 68  ? 43.949  69.924  30.508  1.00 25.30 ? 41  GLY E N   1 
ATOM   5965  C  CA  . GLY F  1 68  ? 44.448  70.949  29.613  1.00 28.17 ? 41  GLY E CA  1 
ATOM   5966  C  C   . GLY F  1 68  ? 45.168  70.398  28.393  1.00 26.65 ? 41  GLY E C   1 
ATOM   5967  O  O   . GLY F  1 68  ? 45.053  69.208  28.087  1.00 20.98 ? 41  GLY E O   1 
ATOM   5968  N  N   . LEU F  1 69  ? 45.935  71.253  27.722  1.00 22.72 ? 42  LEU E N   1 
ATOM   5969  C  CA  . LEU F  1 69  ? 46.554  70.937  26.436  1.00 23.05 ? 42  LEU E CA  1 
ATOM   5970  C  C   . LEU F  1 69  ? 47.911  70.276  26.646  1.00 20.25 ? 42  LEU E C   1 
ATOM   5971  O  O   . LEU F  1 69  ? 48.660  70.655  27.547  1.00 22.10 ? 42  LEU E O   1 
ATOM   5972  C  CB  . LEU F  1 69  ? 46.736  72.202  25.599  1.00 21.54 ? 42  LEU E CB  1 
ATOM   5973  C  CG  . LEU F  1 69  ? 45.517  72.916  24.989  1.00 27.41 ? 42  LEU E CG  1 
ATOM   5974  C  CD1 . LEU F  1 69  ? 45.971  74.241  24.384  1.00 33.83 ? 42  LEU E CD1 1 
ATOM   5975  C  CD2 . LEU F  1 69  ? 44.821  72.089  23.929  1.00 26.24 ? 42  LEU E CD2 1 
ATOM   5976  N  N   . HIS F  1 70  ? 48.223  69.297  25.790  1.00 20.83 ? 43  HIS E N   1 
ATOM   5977  C  CA  . HIS F  1 70  ? 49.484  68.562  25.808  1.00 15.13 ? 43  HIS E CA  1 
ATOM   5978  C  C   . HIS F  1 70  ? 49.966  68.368  24.376  1.00 13.42 ? 43  HIS E C   1 
ATOM   5979  O  O   . HIS F  1 70  ? 49.207  67.873  23.545  1.00 15.78 ? 43  HIS E O   1 
ATOM   5980  C  CB  . HIS F  1 70  ? 49.305  67.195  26.489  1.00 15.93 ? 43  HIS E CB  1 
ATOM   5981  C  CG  . HIS F  1 70  ? 49.017  67.303  27.957  1.00 18.26 ? 43  HIS E CG  1 
ATOM   5982  N  ND1 . HIS F  1 70  ? 50.020  67.414  28.898  1.00 22.17 ? 43  HIS E ND1 1 
ATOM   5983  C  CD2 . HIS F  1 70  ? 47.851  67.352  28.640  1.00 23.42 ? 43  HIS E CD2 1 
ATOM   5984  C  CE1 . HIS F  1 70  ? 49.481  67.509  30.104  1.00 23.84 ? 43  HIS E CE1 1 
ATOM   5985  N  NE2 . HIS F  1 70  ? 48.166  67.473  29.973  1.00 23.70 ? 43  HIS E NE2 1 
ATOM   5986  N  N   . GLY F  1 71  ? 51.214  68.744  24.103  1.00 13.42 ? 44  GLY E N   1 
ATOM   5987  C  CA  . GLY F  1 71  ? 51.776  68.505  22.780  1.00 17.34 ? 44  GLY E CA  1 
ATOM   5988  C  C   . GLY F  1 71  ? 51.806  67.021  22.465  1.00 20.38 ? 44  GLY E C   1 
ATOM   5989  O  O   . GLY F  1 71  ? 51.961  66.182  23.347  1.00 15.92 ? 44  GLY E O   1 
ATOM   5990  N  N   . PHE F  1 72  ? 51.656  66.698  21.185  1.00 18.52 ? 45  PHE E N   1 
ATOM   5991  C  CA  . PHE F  1 72  ? 51.398  65.326  20.730  1.00 13.42 ? 45  PHE E CA  1 
ATOM   5992  C  C   . PHE F  1 72  ? 52.156  65.206  19.413  1.00 21.29 ? 45  PHE E C   1 
ATOM   5993  O  O   . PHE F  1 72  ? 51.719  65.781  18.419  1.00 13.42 ? 45  PHE E O   1 
ATOM   5994  C  CB  . PHE F  1 72  ? 49.901  65.145  20.562  1.00 13.42 ? 45  PHE E CB  1 
ATOM   5995  C  CG  . PHE F  1 72  ? 49.432  63.739  20.254  1.00 16.85 ? 45  PHE E CG  1 
ATOM   5996  C  CD1 . PHE F  1 72  ? 49.566  62.704  21.181  1.00 19.67 ? 45  PHE E CD1 1 
ATOM   5997  C  CD2 . PHE F  1 72  ? 48.798  63.472  19.048  1.00 19.15 ? 45  PHE E CD2 1 
ATOM   5998  C  CE1 . PHE F  1 72  ? 49.074  61.421  20.903  1.00 17.10 ? 45  PHE E CE1 1 
ATOM   5999  C  CE2 . PHE F  1 72  ? 48.297  62.194  18.757  1.00 17.28 ? 45  PHE E CE2 1 
ATOM   6000  C  CZ  . PHE F  1 72  ? 48.442  61.168  19.678  1.00 18.45 ? 45  PHE E CZ  1 
ATOM   6001  N  N   . HIS F  1 73  ? 53.305  64.517  19.421  1.00 17.20 ? 46  HIS E N   1 
ATOM   6002  C  CA  . HIS F  1 73  ? 54.248  64.594  18.309  1.00 15.23 ? 46  HIS E CA  1 
ATOM   6003  C  C   . HIS F  1 73  ? 54.839  63.226  17.988  1.00 18.58 ? 46  HIS E C   1 
ATOM   6004  O  O   . HIS F  1 73  ? 55.078  62.400  18.881  1.00 15.32 ? 46  HIS E O   1 
ATOM   6005  C  CB  . HIS F  1 73  ? 55.406  65.558  18.621  1.00 19.68 ? 46  HIS E CB  1 
ATOM   6006  C  CG  . HIS F  1 73  ? 54.970  66.913  19.081  1.00 19.97 ? 46  HIS E CG  1 
ATOM   6007  N  ND1 . HIS F  1 73  ? 55.414  67.481  20.257  1.00 23.49 ? 46  HIS E ND1 1 
ATOM   6008  C  CD2 . HIS F  1 73  ? 54.139  67.823  18.515  1.00 20.60 ? 46  HIS E CD2 1 
ATOM   6009  C  CE1 . HIS F  1 73  ? 54.872  68.678  20.400  1.00 20.79 ? 46  HIS E CE1 1 
ATOM   6010  N  NE2 . HIS F  1 73  ? 54.098  68.913  19.355  1.00 22.74 ? 46  HIS E NE2 1 
ATOM   6011  N  N   . VAL F  1 74  ? 55.125  63.014  16.707  1.00 13.42 ? 47  VAL E N   1 
ATOM   6012  C  CA  . VAL F  1 74  ? 55.922  61.869  16.284  1.00 17.09 ? 47  VAL E CA  1 
ATOM   6013  C  C   . VAL F  1 74  ? 57.376  62.314  16.272  1.00 19.37 ? 47  VAL E C   1 
ATOM   6014  O  O   . VAL F  1 74  ? 57.737  63.283  15.588  1.00 17.42 ? 47  VAL E O   1 
ATOM   6015  C  CB  . VAL F  1 74  ? 55.490  61.349  14.902  1.00 17.60 ? 47  VAL E CB  1 
ATOM   6016  C  CG1 . VAL F  1 74  ? 56.339  60.124  14.506  1.00 15.42 ? 47  VAL E CG1 1 
ATOM   6017  C  CG2 . VAL F  1 74  ? 54.010  61.017  14.897  1.00 19.75 ? 47  VAL E CG2 1 
ATOM   6018  N  N   . HIS F  1 75  ? 58.215  61.614  17.030  1.00 13.87 ? 48  HIS E N   1 
ATOM   6019  C  CA  . HIS F  1 75  ? 59.643  61.883  17.053  1.00 13.42 ? 48  HIS E CA  1 
ATOM   6020  C  C   . HIS F  1 75  ? 60.375  60.891  16.150  1.00 19.51 ? 48  HIS E C   1 
ATOM   6021  O  O   . HIS F  1 75  ? 59.841  59.839  15.792  1.00 19.18 ? 48  HIS E O   1 
ATOM   6022  C  CB  . HIS F  1 75  ? 60.173  61.803  18.493  1.00 19.23 ? 48  HIS E CB  1 
ATOM   6023  C  CG  . HIS F  1 75  ? 59.673  62.908  19.371  1.00 15.62 ? 48  HIS E CG  1 
ATOM   6024  N  ND1 . HIS F  1 75  ? 60.513  63.797  20.007  1.00 19.36 ? 48  HIS E ND1 1 
ATOM   6025  C  CD2 . HIS F  1 75  ? 58.411  63.276  19.704  1.00 17.14 ? 48  HIS E CD2 1 
ATOM   6026  C  CE1 . HIS F  1 75  ? 59.790  64.655  20.712  1.00 22.76 ? 48  HIS E CE1 1 
ATOM   6027  N  NE2 . HIS F  1 75  ? 58.513  64.356  20.551  1.00 17.94 ? 48  HIS E NE2 1 
ATOM   6028  N  N   . GLU F  1 76  ? 61.622  61.239  15.803  1.00 15.51 ? 49  GLU E N   1 
ATOM   6029  C  CA  . GLU F  1 76  ? 62.287  60.611  14.664  1.00 15.55 ? 49  GLU E CA  1 
ATOM   6030  C  C   . GLU F  1 76  ? 62.573  59.129  14.896  1.00 20.12 ? 49  GLU E C   1 
ATOM   6031  O  O   . GLU F  1 76  ? 62.379  58.315  13.991  1.00 22.92 ? 49  GLU E O   1 
ATOM   6032  C  CB  . GLU F  1 76  ? 63.591  61.339  14.351  1.00 20.67 ? 49  GLU E CB  1 
ATOM   6033  C  CG  . GLU F  1 76  ? 64.260  60.794  13.086  1.00 25.21 ? 49  GLU E CG  1 
ATOM   6034  C  CD  . GLU F  1 76  ? 65.491  61.578  12.697  1.00 34.60 ? 49  GLU E CD  1 
ATOM   6035  O  OE1 . GLU F  1 76  ? 65.792  62.576  13.386  1.00 31.10 ? 49  GLU E OE1 1 
ATOM   6036  O  OE2 . GLU F  1 76  ? 66.165  61.191  11.712  1.00 35.93 ? 49  GLU E OE2 1 
ATOM   6037  N  N   . PHE F  1 77  ? 63.049  58.758  16.086  1.00 18.82 ? 50  PHE E N   1 
ATOM   6038  C  CA  . PHE F  1 77  ? 63.563  57.414  16.338  1.00 19.71 ? 50  PHE E CA  1 
ATOM   6039  C  C   . PHE F  1 77  ? 62.623  56.605  17.221  1.00 19.08 ? 50  PHE E C   1 
ATOM   6040  O  O   . PHE F  1 77  ? 62.097  57.109  18.220  1.00 22.44 ? 50  PHE E O   1 
ATOM   6041  C  CB  . PHE F  1 77  ? 64.954  57.483  16.983  1.00 19.52 ? 50  PHE E CB  1 
ATOM   6042  C  CG  . PHE F  1 77  ? 65.929  58.287  16.176  1.00 23.39 ? 50  PHE E CG  1 
ATOM   6043  C  CD1 . PHE F  1 77  ? 66.230  57.914  14.871  1.00 28.81 ? 50  PHE E CD1 1 
ATOM   6044  C  CD2 . PHE F  1 77  ? 66.522  59.422  16.704  1.00 30.64 ? 50  PHE E CD2 1 
ATOM   6045  C  CE1 . PHE F  1 77  ? 67.123  58.661  14.100  1.00 33.41 ? 50  PHE E CE1 1 
ATOM   6046  C  CE2 . PHE F  1 77  ? 67.410  60.173  15.945  1.00 31.27 ? 50  PHE E CE2 1 
ATOM   6047  C  CZ  . PHE F  1 77  ? 67.712  59.796  14.643  1.00 31.94 ? 50  PHE E CZ  1 
ATOM   6048  N  N   . GLY F  1 78  ? 62.415  55.347  16.835  1.00 16.79 ? 51  GLY E N   1 
ATOM   6049  C  CA  . GLY F  1 78  ? 61.707  54.374  17.637  1.00 16.94 ? 51  GLY E CA  1 
ATOM   6050  C  C   . GLY F  1 78  ? 62.670  53.747  18.639  1.00 21.00 ? 51  GLY E C   1 
ATOM   6051  O  O   . GLY F  1 78  ? 62.775  52.521  18.740  1.00 24.35 ? 51  GLY E O   1 
ATOM   6052  N  N   . ASP F  1 79  ? 63.402  54.592  19.352  1.00 22.39 ? 52  ASP E N   1 
ATOM   6053  C  CA  . ASP F  1 79  ? 64.481  54.193  20.252  1.00 22.51 ? 52  ASP E CA  1 
ATOM   6054  C  C   . ASP F  1 79  ? 64.069  54.555  21.677  1.00 22.98 ? 52  ASP E C   1 
ATOM   6055  O  O   . ASP F  1 79  ? 64.017  55.732  22.026  1.00 24.72 ? 52  ASP E O   1 
ATOM   6056  C  CB  . ASP F  1 79  ? 65.770  54.903  19.853  1.00 20.27 ? 52  ASP E CB  1 
ATOM   6057  C  CG  . ASP F  1 79  ? 66.979  54.454  20.664  1.00 28.54 ? 52  ASP E CG  1 
ATOM   6058  O  OD1 . ASP F  1 79  ? 66.797  53.868  21.744  1.00 26.27 ? 52  ASP E OD1 1 
ATOM   6059  O  OD2 . ASP F  1 79  ? 68.117  54.697  20.221  1.00 32.70 ? 52  ASP E OD2 1 
ATOM   6060  N  N   . ASN F  1 80  ? 63.773  53.548  22.493  1.00 22.14 ? 53  ASN E N   1 
ATOM   6061  C  CA  . ASN F  1 80  ? 63.364  53.741  23.880  1.00 23.94 ? 53  ASN E CA  1 
ATOM   6062  C  C   . ASN F  1 80  ? 64.446  53.298  24.865  1.00 24.36 ? 53  ASN E C   1 
ATOM   6063  O  O   . ASN F  1 80  ? 64.144  53.021  26.033  1.00 23.37 ? 53  ASN E O   1 
ATOM   6064  C  CB  . ASN F  1 80  ? 62.064  52.983  24.156  1.00 28.04 ? 53  ASN E CB  1 
ATOM   6065  C  CG  . ASN F  1 80  ? 61.350  53.476  25.410  1.00 41.92 ? 53  ASN E CG  1 
ATOM   6066  O  OD1 . ASN F  1 80  ? 61.271  54.680  25.658  1.00 43.84 ? 53  ASN E OD1 1 
ATOM   6067  N  ND2 . ASN F  1 80  ? 60.851  52.544  26.219  1.00 43.30 ? 53  ASN E ND2 1 
ATOM   6068  N  N   . THR F  1 81  ? 65.703  53.237  24.425  1.00 24.47 ? 54  THR E N   1 
ATOM   6069  C  CA  . THR F  1 81  ? 66.755  52.675  25.276  1.00 24.74 ? 54  THR E CA  1 
ATOM   6070  C  C   . THR F  1 81  ? 67.000  53.524  26.518  1.00 31.53 ? 54  THR E C   1 
ATOM   6071  O  O   . THR F  1 81  ? 67.286  52.987  27.593  1.00 31.02 ? 54  THR E O   1 
ATOM   6072  C  CB  . THR F  1 81  ? 68.050  52.503  24.477  1.00 24.26 ? 54  THR E CB  1 
ATOM   6073  O  OG1 . THR F  1 81  ? 68.456  53.749  23.900  1.00 28.22 ? 54  THR E OG1 1 
ATOM   6074  C  CG2 . THR F  1 81  ? 67.870  51.475  23.380  1.00 26.75 ? 54  THR E CG2 1 
ATOM   6075  N  N   . ALA F  1 82  ? 66.901  54.843  26.402  1.00 25.94 ? 55  ALA E N   1 
ATOM   6076  C  CA  . ALA F  1 82  ? 67.017  55.731  27.553  1.00 35.10 ? 55  ALA E CA  1 
ATOM   6077  C  C   . ALA F  1 82  ? 65.673  56.356  27.908  1.00 34.43 ? 55  ALA E C   1 
ATOM   6078  O  O   . ALA F  1 82  ? 65.605  57.522  28.305  1.00 37.84 ? 55  ALA E O   1 
ATOM   6079  C  CB  . ALA F  1 82  ? 68.063  56.815  27.289  1.00 34.95 ? 55  ALA E CB  1 
ATOM   6080  N  N   . GLY F  1 83  ? 64.601  55.597  27.761  1.00 28.65 ? 56  GLY E N   1 
ATOM   6081  C  CA  . GLY F  1 83  ? 63.295  56.169  27.932  1.00 28.83 ? 56  GLY E CA  1 
ATOM   6082  C  C   . GLY F  1 83  ? 62.937  57.060  26.755  1.00 29.64 ? 56  GLY E C   1 
ATOM   6083  O  O   . GLY F  1 83  ? 63.494  56.952  25.646  1.00 23.03 ? 56  GLY E O   1 
ATOM   6084  N  N   . CYS F  1 84  ? 61.997  57.976  27.005  1.00 25.67 ? 57  CYS E N   1 
ATOM   6085  C  CA  . CYS F  1 84  ? 61.473  58.786  25.902  1.00 27.54 ? 57  CYS E CA  1 
ATOM   6086  C  C   . CYS F  1 84  ? 62.526  59.716  25.313  1.00 24.87 ? 57  CYS E C   1 
ATOM   6087  O  O   . CYS F  1 84  ? 62.385  60.133  24.155  1.00 22.96 ? 57  CYS E O   1 
ATOM   6088  C  CB  . CYS F  1 84  ? 60.244  59.573  26.383  1.00 29.26 ? 57  CYS E CB  1 
ATOM   6089  S  SG  . CYS F  1 84  ? 58.809  58.481  26.813  1.00 31.49 ? 57  CYS E SG  1 
ATOM   6090  N  N   . THR F  1 85  ? 63.580  60.037  26.078  1.00 22.15 ? 58  THR E N   1 
ATOM   6091  C  CA  . THR F  1 85  ? 64.651  60.908  25.590  1.00 25.30 ? 58  THR E CA  1 
ATOM   6092  C  C   . THR F  1 85  ? 65.313  60.354  24.335  1.00 25.57 ? 58  THR E C   1 
ATOM   6093  O  O   . THR F  1 85  ? 65.768  61.124  23.481  1.00 25.36 ? 58  THR E O   1 
ATOM   6094  C  CB  . THR F  1 85  ? 65.721  61.089  26.680  1.00 31.78 ? 58  THR E CB  1 
ATOM   6095  O  OG1 . THR F  1 85  ? 65.097  61.430  27.921  1.00 43.89 ? 58  THR E OG1 1 
ATOM   6096  C  CG2 . THR F  1 85  ? 66.705  62.173  26.295  1.00 35.28 ? 58  THR E CG2 1 
ATOM   6097  N  N   . SER F  1 86  ? 65.409  59.029  24.220  1.00 25.85 ? 59  SER E N   1 
ATOM   6098  C  CA  . SER F  1 86  ? 66.137  58.423  23.111  1.00 25.75 ? 59  SER E CA  1 
ATOM   6099  C  C   . SER F  1 86  ? 65.419  58.601  21.780  1.00 22.25 ? 59  SER E C   1 
ATOM   6100  O  O   . SER F  1 86  ? 66.003  58.310  20.732  1.00 23.31 ? 59  SER E O   1 
ATOM   6101  C  CB  . SER F  1 86  ? 66.325  56.923  23.348  1.00 23.73 ? 59  SER E CB  1 
ATOM   6102  O  OG  . SER F  1 86  ? 66.493  56.631  24.696  1.00 40.37 ? 59  SER E OG  1 
ATOM   6103  N  N   . ALA F  1 87  ? 64.165  59.047  21.795  1.00 20.93 ? 60  ALA E N   1 
ATOM   6104  C  CA  . ALA F  1 87  ? 63.410  59.153  20.554  1.00 20.56 ? 60  ALA E CA  1 
ATOM   6105  C  C   . ALA F  1 87  ? 63.875  60.313  19.688  1.00 22.88 ? 60  ALA E C   1 
ATOM   6106  O  O   . ALA F  1 87  ? 63.463  60.404  18.519  1.00 22.32 ? 60  ALA E O   1 
ATOM   6107  C  CB  . ALA F  1 87  ? 61.913  59.279  20.862  1.00 19.47 ? 60  ALA E CB  1 
ATOM   6108  N  N   . GLY F  1 88  ? 64.734  61.179  20.211  1.00 19.49 ? 61  GLY E N   1 
ATOM   6109  C  CA  . GLY F  1 88  ? 65.302  62.250  19.429  1.00 23.04 ? 61  GLY E CA  1 
ATOM   6110  C  C   . GLY F  1 88  ? 64.300  63.367  19.198  1.00 22.21 ? 61  GLY E C   1 
ATOM   6111  O  O   . GLY F  1 88  ? 63.301  63.491  19.914  1.00 22.96 ? 61  GLY E O   1 
ATOM   6112  N  N   . PRO F  1 89  ? 64.547  64.183  18.184  1.00 23.33 ? 62  PRO E N   1 
ATOM   6113  C  CA  . PRO F  1 89  ? 63.707  65.354  17.913  1.00 23.43 ? 62  PRO E CA  1 
ATOM   6114  C  C   . PRO F  1 89  ? 62.451  64.950  17.139  1.00 19.99 ? 62  PRO E C   1 
ATOM   6115  O  O   . PRO F  1 89  ? 62.211  63.778  16.858  1.00 21.18 ? 62  PRO E O   1 
ATOM   6116  C  CB  . PRO F  1 89  ? 64.627  66.242  17.071  1.00 24.47 ? 62  PRO E CB  1 
ATOM   6117  C  CG  . PRO F  1 89  ? 65.447  65.229  16.264  1.00 25.74 ? 62  PRO E CG  1 
ATOM   6118  C  CD  . PRO F  1 89  ? 65.640  64.031  17.198  1.00 22.12 ? 62  PRO E CD  1 
ATOM   6119  N  N   . HIS F  1 90  ? 61.635  65.945  16.798  1.00 19.06 ? 63  HIS E N   1 
ATOM   6120  C  CA  . HIS F  1 90  ? 60.445  65.651  16.005  1.00 18.76 ? 63  HIS E CA  1 
ATOM   6121  C  C   . HIS F  1 90  ? 60.862  65.069  14.657  1.00 18.67 ? 63  HIS E C   1 
ATOM   6122  O  O   . HIS F  1 90  ? 61.892  65.443  14.091  1.00 23.69 ? 63  HIS E O   1 
ATOM   6123  C  CB  . HIS F  1 90  ? 59.610  66.921  15.788  1.00 20.02 ? 63  HIS E CB  1 
ATOM   6124  C  CG  . HIS F  1 90  ? 59.020  67.481  17.046  1.00 17.69 ? 63  HIS E CG  1 
ATOM   6125  N  ND1 . HIS F  1 90  ? 58.128  68.529  17.053  1.00 22.21 ? 63  HIS E ND1 1 
ATOM   6126  C  CD2 . HIS F  1 90  ? 59.184  67.119  18.342  1.00 22.63 ? 63  HIS E CD2 1 
ATOM   6127  C  CE1 . HIS F  1 90  ? 57.773  68.798  18.300  1.00 22.04 ? 63  HIS E CE1 1 
ATOM   6128  N  NE2 . HIS F  1 90  ? 58.403  67.956  19.101  1.00 22.90 ? 63  HIS E NE2 1 
ATOM   6129  N  N   . PHE F  1 91  ? 60.067  64.122  14.166  1.00 19.35 ? 64  PHE E N   1 
ATOM   6130  C  CA  . PHE F  1 91  ? 60.252  63.574  12.829  1.00 16.19 ? 64  PHE E CA  1 
ATOM   6131  C  C   . PHE F  1 91  ? 60.096  64.689  11.808  1.00 23.72 ? 64  PHE E C   1 
ATOM   6132  O  O   . PHE F  1 91  ? 59.026  65.291  11.690  1.00 22.94 ? 64  PHE E O   1 
ATOM   6133  C  CB  . PHE F  1 91  ? 59.238  62.460  12.601  1.00 15.34 ? 64  PHE E CB  1 
ATOM   6134  C  CG  . PHE F  1 91  ? 59.339  61.794  11.246  1.00 20.67 ? 64  PHE E CG  1 
ATOM   6135  C  CD1 . PHE F  1 91  ? 60.570  61.549  10.662  1.00 23.11 ? 64  PHE E CD1 1 
ATOM   6136  C  CD2 . PHE F  1 91  ? 58.193  61.379  10.594  1.00 20.04 ? 64  PHE E CD2 1 
ATOM   6137  C  CE1 . PHE F  1 91  ? 60.659  60.916  9.407   1.00 23.50 ? 64  PHE E CE1 1 
ATOM   6138  C  CE2 . PHE F  1 91  ? 58.266  60.761  9.335   1.00 21.92 ? 64  PHE E CE2 1 
ATOM   6139  C  CZ  . PHE F  1 91  ? 59.512  60.520  8.763   1.00 18.07 ? 64  PHE E CZ  1 
ATOM   6140  N  N   . ASN F  1 92  ? 61.169  64.977  11.090  1.00 23.51 ? 65  ASN E N   1 
ATOM   6141  C  CA  . ASN F  1 92  ? 61.257  66.176  10.272  1.00 19.47 ? 65  ASN E CA  1 
ATOM   6142  C  C   . ASN F  1 92  ? 62.070  65.881  9.013   1.00 23.57 ? 65  ASN E C   1 
ATOM   6143  O  O   . ASN F  1 92  ? 63.128  66.487  8.813   1.00 23.29 ? 65  ASN E O   1 
ATOM   6144  C  CB  . ASN F  1 92  ? 61.906  67.299  11.078  1.00 19.14 ? 65  ASN E CB  1 
ATOM   6145  C  CG  . ASN F  1 92  ? 61.931  68.626  10.337  1.00 25.21 ? 65  ASN E CG  1 
ATOM   6146  O  OD1 . ASN F  1 92  ? 61.122  68.879  9.449   1.00 24.26 ? 65  ASN E OD1 1 
ATOM   6147  N  ND2 . ASN F  1 92  ? 62.866  69.479  10.714  1.00 26.22 ? 65  ASN E ND2 1 
ATOM   6148  N  N   . PRO F  1 93  ? 61.619  64.969  8.145   1.00 22.45 ? 66  PRO E N   1 
ATOM   6149  C  CA  . PRO F  1 93  ? 62.449  64.612  6.984   1.00 26.72 ? 66  PRO E CA  1 
ATOM   6150  C  C   . PRO F  1 93  ? 62.640  65.744  5.989   1.00 31.61 ? 66  PRO E C   1 
ATOM   6151  O  O   . PRO F  1 93  ? 63.596  65.688  5.211   1.00 33.79 ? 66  PRO E O   1 
ATOM   6152  C  CB  . PRO F  1 93  ? 61.687  63.442  6.355   1.00 25.25 ? 66  PRO E CB  1 
ATOM   6153  C  CG  . PRO F  1 93  ? 60.273  63.624  6.808   1.00 27.15 ? 66  PRO E CG  1 
ATOM   6154  C  CD  . PRO F  1 93  ? 60.375  64.179  8.187   1.00 23.18 ? 66  PRO E CD  1 
ATOM   6155  N  N   . LEU F  1 94  ? 61.775  66.764  5.978   1.00 26.91 ? 67  LEU E N   1 
ATOM   6156  C  CA  . LEU F  1 94  ? 61.929  67.891  5.060   1.00 29.94 ? 67  LEU E CA  1 
ATOM   6157  C  C   . LEU F  1 94  ? 62.658  69.079  5.670   1.00 31.58 ? 67  LEU E C   1 
ATOM   6158  O  O   . LEU F  1 94  ? 62.746  70.128  5.025   1.00 35.66 ? 67  LEU E O   1 
ATOM   6159  C  CB  . LEU F  1 94  ? 60.568  68.331  4.529   1.00 30.42 ? 67  LEU E CB  1 
ATOM   6160  C  CG  . LEU F  1 94  ? 59.859  67.203  3.781   1.00 32.97 ? 67  LEU E CG  1 
ATOM   6161  C  CD1 . LEU F  1 94  ? 58.395  67.505  3.543   1.00 34.69 ? 67  LEU E CD1 1 
ATOM   6162  C  CD2 . LEU F  1 94  ? 60.577  66.932  2.470   1.00 40.32 ? 67  LEU E CD2 1 
ATOM   6163  N  N   . SER F  1 95  ? 63.175  68.939  6.894   1.00 26.48 ? 68  SER E N   1 
ATOM   6164  C  CA  . SER F  1 95  ? 63.987  69.960  7.550   1.00 31.75 ? 68  SER E CA  1 
ATOM   6165  C  C   . SER F  1 95  ? 63.262  71.305  7.616   1.00 34.78 ? 68  SER E C   1 
ATOM   6166  O  O   . SER F  1 95  ? 63.816  72.350  7.279   1.00 30.57 ? 68  SER E O   1 
ATOM   6167  C  CB  . SER F  1 95  ? 65.345  70.113  6.855   1.00 37.98 ? 68  SER E CB  1 
ATOM   6168  O  OG  . SER F  1 95  ? 66.170  68.986  7.094   1.00 41.84 ? 68  SER E OG  1 
ATOM   6169  N  N   . ARG F  1 96  ? 62.009  71.275  8.063   1.00 25.06 ? 69  ARG E N   1 
ATOM   6170  C  CA  . ARG F  1 96  ? 61.234  72.491  8.253   1.00 26.22 ? 69  ARG E CA  1 
ATOM   6171  C  C   . ARG F  1 96  ? 61.301  72.942  9.709   1.00 26.60 ? 69  ARG E C   1 
ATOM   6172  O  O   . ARG F  1 96  ? 61.840  72.250  10.575  1.00 24.21 ? 69  ARG E O   1 
ATOM   6173  C  CB  . ARG F  1 96  ? 59.783  72.271  7.829   1.00 23.60 ? 69  ARG E CB  1 
ATOM   6174  C  CG  . ARG F  1 96  ? 59.625  71.688  6.428   1.00 32.16 ? 69  ARG E CG  1 
ATOM   6175  C  CD  . ARG F  1 96  ? 59.939  72.712  5.343   1.00 36.94 ? 69  ARG E CD  1 
ATOM   6176  N  NE  . ARG F  1 96  ? 59.742  72.161  4.001   1.00 49.36 ? 69  ARG E NE  1 
ATOM   6177  C  CZ  . ARG F  1 96  ? 60.698  71.995  3.089   1.00 52.44 ? 69  ARG E CZ  1 
ATOM   6178  N  NH1 . ARG F  1 96  ? 61.954  72.345  3.326   1.00 40.65 ? 69  ARG E NH1 1 
ATOM   6179  N  NH2 . ARG F  1 96  ? 60.385  71.465  1.906   1.00 41.32 ? 69  ARG E NH2 1 
ATOM   6180  N  N   . LYS F  1 97  ? 60.770  74.143  9.966   1.00 25.60 ? 70  LYS E N   1 
ATOM   6181  C  CA  . LYS F  1 97  ? 60.564  74.595  11.336  1.00 24.44 ? 70  LYS E CA  1 
ATOM   6182  C  C   . LYS F  1 97  ? 59.283  73.999  11.912  1.00 22.17 ? 70  LYS E C   1 
ATOM   6183  O  O   . LYS F  1 97  ? 58.372  73.597  11.183  1.00 22.77 ? 70  LYS E O   1 
ATOM   6184  C  CB  . LYS F  1 97  ? 60.500  76.123  11.408  1.00 26.45 ? 70  LYS E CB  1 
ATOM   6185  C  CG  . LYS F  1 97  ? 61.734  76.815  10.841  1.00 33.38 ? 70  LYS E CG  1 
ATOM   6186  C  CD  . LYS F  1 97  ? 61.816  78.268  11.285  1.00 43.37 ? 70  LYS E CD  1 
ATOM   6187  C  CE  . LYS F  1 97  ? 62.769  79.064  10.385  1.00 46.73 ? 70  LYS E CE  1 
ATOM   6188  N  NZ  . LYS F  1 97  ? 62.416  80.521  10.333  1.00 55.55 ? 70  LYS E NZ  1 
ATOM   6189  N  N   . HIS F  1 98  ? 59.213  73.976  13.245  1.00 22.68 ? 71  HIS E N   1 
ATOM   6190  C  CA  . HIS F  1 98  ? 58.053  73.425  13.932  1.00 20.57 ? 71  HIS E CA  1 
ATOM   6191  C  C   . HIS F  1 98  ? 56.814  74.273  13.647  1.00 20.89 ? 71  HIS E C   1 
ATOM   6192  O  O   . HIS F  1 98  ? 56.895  75.503  13.564  1.00 23.42 ? 71  HIS E O   1 
ATOM   6193  C  CB  . HIS F  1 98  ? 58.324  73.373  15.448  1.00 19.33 ? 71  HIS E CB  1 
ATOM   6194  C  CG  . HIS F  1 98  ? 57.157  72.889  16.249  1.00 23.56 ? 71  HIS E CG  1 
ATOM   6195  N  ND1 . HIS F  1 98  ? 56.821  71.556  16.320  1.00 22.87 ? 71  HIS E ND1 1 
ATOM   6196  C  CD2 . HIS F  1 98  ? 56.252  73.549  17.014  1.00 18.02 ? 71  HIS E CD2 1 
ATOM   6197  C  CE1 . HIS F  1 98  ? 55.757  71.412  17.091  1.00 22.84 ? 71  HIS E CE1 1 
ATOM   6198  N  NE2 . HIS F  1 98  ? 55.388  72.607  17.523  1.00 18.94 ? 71  HIS E NE2 1 
ATOM   6199  N  N   . GLY F  1 99  ? 55.669  73.610  13.474  1.00 16.95 ? 72  GLY E N   1 
ATOM   6200  C  CA  . GLY F  1 99  ? 54.409  74.305  13.272  1.00 21.94 ? 72  GLY E CA  1 
ATOM   6201  C  C   . GLY F  1 99  ? 53.238  73.521  13.828  1.00 21.82 ? 72  GLY E C   1 
ATOM   6202  O  O   . GLY F  1 99  ? 53.430  72.484  14.468  1.00 22.12 ? 72  GLY E O   1 
ATOM   6203  N  N   . GLY F  1 100 ? 52.023  74.006  13.617  1.00 18.17 ? 73  GLY E N   1 
ATOM   6204  C  CA  . GLY F  1 100 ? 50.846  73.244  13.948  1.00 18.27 ? 73  GLY E CA  1 
ATOM   6205  C  C   . GLY F  1 100 ? 50.480  72.348  12.789  1.00 20.01 ? 73  GLY E C   1 
ATOM   6206  O  O   . GLY F  1 100 ? 50.977  72.532  11.676  1.00 22.84 ? 73  GLY E O   1 
ATOM   6207  N  N   . PRO F  1 101 ? 49.591  71.381  13.013  1.00 23.00 ? 74  PRO E N   1 
ATOM   6208  C  CA  . PRO F  1 101 ? 49.255  70.441  11.927  1.00 21.70 ? 74  PRO E CA  1 
ATOM   6209  C  C   . PRO F  1 101 ? 48.661  71.116  10.701  1.00 25.16 ? 74  PRO E C   1 
ATOM   6210  O  O   . PRO F  1 101 ? 48.806  70.582  9.602   1.00 23.23 ? 74  PRO E O   1 
ATOM   6211  C  CB  . PRO F  1 101 ? 48.255  69.472  12.579  1.00 25.80 ? 74  PRO E CB  1 
ATOM   6212  C  CG  . PRO F  1 101 ? 47.907  70.071  13.918  1.00 25.74 ? 74  PRO E CG  1 
ATOM   6213  C  CD  . PRO F  1 101 ? 49.029  70.967  14.309  1.00 22.42 ? 74  PRO E CD  1 
ATOM   6214  N  N   . LYS F  1 102 ? 48.022  72.281  10.846  1.00 24.57 ? 75  LYS E N   1 
ATOM   6215  C  CA  . LYS F  1 102 ? 47.468  72.968  9.678   1.00 26.63 ? 75  LYS E CA  1 
ATOM   6216  C  C   . LYS F  1 102 ? 48.466  73.856  8.959   1.00 27.66 ? 75  LYS E C   1 
ATOM   6217  O  O   . LYS F  1 102 ? 48.131  74.383  7.892   1.00 35.25 ? 75  LYS E O   1 
ATOM   6218  C  CB  . LYS F  1 102 ? 46.259  73.830  10.052  1.00 30.73 ? 75  LYS E CB  1 
ATOM   6219  C  CG  . LYS F  1 102 ? 45.083  73.064  10.620  1.00 36.17 ? 75  LYS E CG  1 
ATOM   6220  C  CD  . LYS F  1 102 ? 43.906  74.006  10.797  1.00 46.21 ? 75  LYS E CD  1 
ATOM   6221  C  CE  . LYS F  1 102 ? 42.831  73.374  11.644  1.00 51.39 ? 75  LYS E CE  1 
ATOM   6222  N  NZ  . LYS F  1 102 ? 41.442  73.792  11.230  1.00 52.34 ? 75  LYS E NZ  1 
ATOM   6223  N  N   . ASP F  1 103 ? 49.661  74.043  9.496   1.00 25.55 ? 76  ASP E N   1 
ATOM   6224  C  CA  . ASP F  1 103 ? 50.647  74.898  8.849   1.00 30.92 ? 76  ASP E CA  1 
ATOM   6225  C  C   . ASP F  1 103 ? 51.334  74.173  7.702   1.00 31.36 ? 76  ASP E C   1 
ATOM   6226  O  O   . ASP F  1 103 ? 51.583  72.966  7.772   1.00 27.76 ? 76  ASP E O   1 
ATOM   6227  C  CB  . ASP F  1 103 ? 51.690  75.349  9.865   1.00 30.00 ? 76  ASP E CB  1 
ATOM   6228  C  CG  . ASP F  1 103 ? 51.136  76.335  10.839  1.00 36.40 ? 76  ASP E CG  1 
ATOM   6229  O  OD1 . ASP F  1 103 ? 50.556  77.334  10.372  1.00 44.98 ? 76  ASP E OD1 1 
ATOM   6230  O  OD2 . ASP F  1 103 ? 51.239  76.096  12.068  1.00 38.23 ? 76  ASP E OD2 1 
ATOM   6231  N  N   . GLU F  1 104 ? 51.655  74.919  6.638   1.00 36.69 ? 77  GLU E N   1 
ATOM   6232  C  CA  . GLU F  1 104 ? 52.475  74.333  5.580   1.00 34.63 ? 77  GLU E CA  1 
ATOM   6233  C  C   . GLU F  1 104 ? 53.905  74.146  6.061   1.00 35.45 ? 77  GLU E C   1 
ATOM   6234  O  O   . GLU F  1 104 ? 54.528  73.103  5.803   1.00 36.97 ? 77  GLU E O   1 
ATOM   6235  C  CB  . GLU F  1 104 ? 52.437  75.200  4.312   1.00 42.11 ? 77  GLU E CB  1 
ATOM   6236  C  CG  . GLU F  1 104 ? 53.250  74.626  3.131   1.00 41.56 ? 77  GLU E CG  1 
ATOM   6237  C  CD  . GLU F  1 104 ? 52.622  73.380  2.501   1.00 65.72 ? 77  GLU E CD  1 
ATOM   6238  O  OE1 . GLU F  1 104 ? 53.149  72.264  2.729   1.00 71.56 ? 77  GLU E OE1 1 
ATOM   6239  O  OE2 . GLU F  1 104 ? 51.612  73.511  1.768   1.00 70.60 ? 77  GLU E OE2 1 
ATOM   6240  N  N   . GLU F  1 105 ? 54.427  75.124  6.800   1.00 29.58 ? 78  GLU E N   1 
ATOM   6241  C  CA  . GLU F  1 105 ? 55.721  74.991  7.467   1.00 29.85 ? 78  GLU E CA  1 
ATOM   6242  C  C   . GLU F  1 105 ? 55.513  74.231  8.769   1.00 26.10 ? 78  GLU E C   1 
ATOM   6243  O  O   . GLU F  1 105 ? 55.118  74.809  9.787   1.00 24.14 ? 78  GLU E O   1 
ATOM   6244  C  CB  . GLU F  1 105 ? 56.348  76.361  7.707   1.00 26.81 ? 78  GLU E CB  1 
ATOM   6245  C  CG  . GLU F  1 105 ? 57.755  76.343  8.317   1.00 30.56 ? 78  GLU E CG  1 
ATOM   6246  C  CD  . GLU F  1 105 ? 58.855  75.980  7.323   1.00 40.75 ? 78  GLU E CD  1 
ATOM   6247  O  OE1 . GLU F  1 105 ? 58.564  75.878  6.107   1.00 48.35 ? 78  GLU E OE1 1 
ATOM   6248  O  OE2 . GLU F  1 105 ? 60.020  75.817  7.762   1.00 35.46 ? 78  GLU E OE2 1 
ATOM   6249  N  N   . ARG F  1 106 ? 55.782  72.928  8.739   1.00 23.81 ? 79  ARG E N   1 
ATOM   6250  C  CA  . ARG F  1 106 ? 55.677  72.098  9.942   1.00 21.97 ? 79  ARG E CA  1 
ATOM   6251  C  C   . ARG F  1 106 ? 56.573  70.884  9.762   1.00 23.32 ? 79  ARG E C   1 
ATOM   6252  O  O   . ARG F  1 106 ? 56.958  70.535  8.642   1.00 22.54 ? 79  ARG E O   1 
ATOM   6253  C  CB  . ARG F  1 106 ? 54.231  71.650  10.189  1.00 17.90 ? 79  ARG E CB  1 
ATOM   6254  C  CG  . ARG F  1 106 ? 53.679  70.796  9.039   1.00 21.41 ? 79  ARG E CG  1 
ATOM   6255  C  CD  . ARG F  1 106 ? 52.372  70.123  9.386   1.00 23.25 ? 79  ARG E CD  1 
ATOM   6256  N  NE  . ARG F  1 106 ? 52.552  68.753  9.862   1.00 21.48 ? 79  ARG E NE  1 
ATOM   6257  C  CZ  . ARG F  1 106 ? 51.565  67.876  9.961   1.00 22.02 ? 79  ARG E CZ  1 
ATOM   6258  N  NH1 . ARG F  1 106 ? 50.314  68.208  9.660   1.00 22.25 ? 79  ARG E NH1 1 
ATOM   6259  N  NH2 . ARG F  1 106 ? 51.833  66.633  10.381  1.00 21.77 ? 79  ARG E NH2 1 
ATOM   6260  N  N   . HIS F  1 107 ? 56.922  70.262  10.881  1.00 21.69 ? 80  HIS E N   1 
ATOM   6261  C  CA  . HIS F  1 107 ? 57.513  68.931  10.864  1.00 19.72 ? 80  HIS E CA  1 
ATOM   6262  C  C   . HIS F  1 107 ? 56.446  67.932  10.445  1.00 19.34 ? 80  HIS E C   1 
ATOM   6263  O  O   . HIS F  1 107 ? 55.261  68.113  10.735  1.00 19.61 ? 80  HIS E O   1 
ATOM   6264  C  CB  . HIS F  1 107 ? 58.039  68.564  12.264  1.00 19.05 ? 80  HIS E CB  1 
ATOM   6265  C  CG  . HIS F  1 107 ? 59.053  69.529  12.805  1.00 21.81 ? 80  HIS E CG  1 
ATOM   6266  N  ND1 . HIS F  1 107 ? 59.260  69.718  14.151  1.00 22.39 ? 80  HIS E ND1 1 
ATOM   6267  C  CD2 . HIS F  1 107 ? 59.945  70.330  12.176  1.00 19.16 ? 80  HIS E CD2 1 
ATOM   6268  C  CE1 . HIS F  1 107 ? 60.232  70.591  14.333  1.00 21.22 ? 80  HIS E CE1 1 
ATOM   6269  N  NE2 . HIS F  1 107 ? 60.656  70.987  13.145  1.00 20.81 ? 80  HIS E NE2 1 
ATOM   6270  N  N   . VAL F  1 108 ? 56.867  66.850  9.777   1.00 19.04 ? 81  VAL E N   1 
ATOM   6271  C  CA  . VAL F  1 108 ? 55.927  65.760  9.521   1.00 18.45 ? 81  VAL E CA  1 
ATOM   6272  C  C   . VAL F  1 108 ? 55.334  65.260  10.837  1.00 13.53 ? 81  VAL E C   1 
ATOM   6273  O  O   . VAL F  1 108 ? 54.146  64.944  10.916  1.00 16.00 ? 81  VAL E O   1 
ATOM   6274  C  CB  . VAL F  1 108 ? 56.607  64.618  8.742   1.00 21.54 ? 81  VAL E CB  1 
ATOM   6275  C  CG1 . VAL F  1 108 ? 55.744  63.365  8.784   1.00 22.90 ? 81  VAL E CG1 1 
ATOM   6276  C  CG2 . VAL F  1 108 ? 56.839  65.039  7.259   1.00 19.17 ? 81  VAL E CG2 1 
ATOM   6277  N  N   . GLY F  1 109 ? 56.134  65.218  11.888  1.00 14.33 ? 82  GLY E N   1 
ATOM   6278  C  CA  . GLY F  1 109 ? 55.624  64.740  13.173  1.00 13.42 ? 82  GLY E CA  1 
ATOM   6279  C  C   . GLY F  1 109 ? 54.732  65.682  13.966  1.00 22.50 ? 82  GLY E C   1 
ATOM   6280  O  O   . GLY F  1 109 ? 54.356  65.352  15.101  1.00 20.84 ? 82  GLY E O   1 
ATOM   6281  N  N   . ASP F  1 110 ? 54.335  66.831  13.412  1.00 20.79 ? 83  ASP E N   1 
ATOM   6282  C  CA  . ASP F  1 110 ? 53.672  67.884  14.196  1.00 19.75 ? 83  ASP E CA  1 
ATOM   6283  C  C   . ASP F  1 110 ? 52.160  67.675  14.214  1.00 19.44 ? 83  ASP E C   1 
ATOM   6284  O  O   . ASP F  1 110 ? 51.423  68.211  13.387  1.00 21.61 ? 83  ASP E O   1 
ATOM   6285  C  CB  . ASP F  1 110 ? 54.060  69.259  13.656  1.00 19.72 ? 83  ASP E CB  1 
ATOM   6286  C  CG  . ASP F  1 110 ? 55.456  69.651  14.089  1.00 20.52 ? 83  ASP E CG  1 
ATOM   6287  O  OD1 . ASP F  1 110 ? 55.951  68.992  15.011  1.00 17.32 ? 83  ASP E OD1 1 
ATOM   6288  O  OD2 . ASP F  1 110 ? 56.094  70.592  13.578  1.00 21.55 ? 83  ASP E OD2 1 
ATOM   6289  N  N   . LEU F  1 111 ? 51.674  66.913  15.196  1.00 16.38 ? 84  LEU E N   1 
ATOM   6290  C  CA  . LEU F  1 111 ? 50.248  66.646  15.292  1.00 14.17 ? 84  LEU E CA  1 
ATOM   6291  C  C   . LEU F  1 111 ? 49.536  67.563  16.286  1.00 20.06 ? 84  LEU E C   1 
ATOM   6292  O  O   . LEU F  1 111 ? 48.402  67.275  16.677  1.00 22.95 ? 84  LEU E O   1 
ATOM   6293  C  CB  . LEU F  1 111 ? 50.009  65.177  15.651  1.00 18.34 ? 84  LEU E CB  1 
ATOM   6294  C  CG  . LEU F  1 111 ? 50.522  64.187  14.590  1.00 19.48 ? 84  LEU E CG  1 
ATOM   6295  C  CD1 . LEU F  1 111 ? 50.313  62.763  15.088  1.00 20.07 ? 84  LEU E CD1 1 
ATOM   6296  C  CD2 . LEU F  1 111 ? 49.817  64.392  13.248  1.00 19.97 ? 84  LEU E CD2 1 
ATOM   6297  N  N   . GLY F  1 112 ? 50.179  68.641  16.720  1.00 15.41 ? 85  GLY E N   1 
ATOM   6298  C  CA  . GLY F  1 112 ? 49.482  69.640  17.511  1.00 21.47 ? 85  GLY E CA  1 
ATOM   6299  C  C   . GLY F  1 112 ? 49.333  69.277  18.971  1.00 25.05 ? 85  GLY E C   1 
ATOM   6300  O  O   . GLY F  1 112 ? 50.254  68.725  19.584  1.00 16.01 ? 85  GLY E O   1 
ATOM   6301  N  N   . ASN F  1 113 ? 48.165  69.585  19.525  1.00 15.79 ? 86  ASN E N   1 
ATOM   6302  C  CA  . ASN F  1 113 ? 47.851  69.333  20.925  1.00 21.18 ? 86  ASN E CA  1 
ATOM   6303  C  C   . ASN F  1 113 ? 46.733  68.318  21.037  1.00 19.37 ? 86  ASN E C   1 
ATOM   6304  O  O   . ASN F  1 113 ? 45.893  68.199  20.138  1.00 20.47 ? 86  ASN E O   1 
ATOM   6305  C  CB  . ASN F  1 113 ? 47.403  70.617  21.634  1.00 19.17 ? 86  ASN E CB  1 
ATOM   6306  C  CG  . ASN F  1 113 ? 48.541  71.556  21.882  1.00 20.89 ? 86  ASN E CG  1 
ATOM   6307  O  OD1 . ASN F  1 113 ? 49.494  71.210  22.583  1.00 16.57 ? 86  ASN E OD1 1 
ATOM   6308  N  ND2 . ASN F  1 113 ? 48.473  72.747  21.296  1.00 19.37 ? 86  ASN E ND2 1 
ATOM   6309  N  N   . VAL F  1 114 ? 46.703  67.621  22.172  1.00 17.26 ? 87  VAL E N   1 
ATOM   6310  C  CA  . VAL F  1 114 ? 45.527  66.879  22.590  1.00 14.64 ? 87  VAL E CA  1 
ATOM   6311  C  C   . VAL F  1 114 ? 45.055  67.502  23.900  1.00 19.43 ? 87  VAL E C   1 
ATOM   6312  O  O   . VAL F  1 114 ? 45.812  68.165  24.600  1.00 21.78 ? 87  VAL E O   1 
ATOM   6313  C  CB  . VAL F  1 114 ? 45.786  65.357  22.745  1.00 19.95 ? 87  VAL E CB  1 
ATOM   6314  C  CG1 . VAL F  1 114 ? 46.195  64.727  21.381  1.00 17.56 ? 87  VAL E CG1 1 
ATOM   6315  C  CG2 . VAL F  1 114 ? 46.833  65.068  23.835  1.00 18.73 ? 87  VAL E CG2 1 
ATOM   6316  N  N   . THR F  1 115 ? 43.787  67.287  24.222  1.00 16.94 ? 88  THR E N   1 
ATOM   6317  C  CA  . THR F  1 115 ? 43.136  67.947  25.355  1.00 22.10 ? 88  THR E CA  1 
ATOM   6318  C  C   . THR F  1 115 ? 42.708  66.893  26.362  1.00 15.40 ? 88  THR E C   1 
ATOM   6319  O  O   . THR F  1 115 ? 41.932  65.992  26.026  1.00 22.88 ? 88  THR E O   1 
ATOM   6320  C  CB  . THR F  1 115 ? 41.920  68.758  24.895  1.00 24.84 ? 88  THR E CB  1 
ATOM   6321  O  OG1 . THR F  1 115 ? 42.340  69.730  23.938  1.00 22.66 ? 88  THR E OG1 1 
ATOM   6322  C  CG2 . THR F  1 115 ? 41.260  69.480  26.080  1.00 26.21 ? 88  THR E CG2 1 
ATOM   6323  N  N   . ALA F  1 116 ? 43.221  67.003  27.581  1.00 20.71 ? 89  ALA E N   1 
ATOM   6324  C  CA  . ALA F  1 116 ? 42.829  66.138  28.683  1.00 22.74 ? 89  ALA E CA  1 
ATOM   6325  C  C   . ALA F  1 116 ? 41.704  66.805  29.478  1.00 29.66 ? 89  ALA E C   1 
ATOM   6326  O  O   . ALA F  1 116 ? 41.764  68.005  29.761  1.00 23.89 ? 89  ALA E O   1 
ATOM   6327  C  CB  . ALA F  1 116 ? 44.026  65.859  29.595  1.00 24.22 ? 89  ALA E CB  1 
ATOM   6328  N  N   . ASP F  1 117 ? 40.677  66.028  29.822  1.00 26.32 ? 90  ASP E N   1 
ATOM   6329  C  CA  . ASP F  1 117 ? 39.537  66.546  30.569  1.00 30.71 ? 90  ASP E CA  1 
ATOM   6330  C  C   . ASP F  1 117 ? 39.820  66.561  32.075  1.00 33.87 ? 90  ASP E C   1 
ATOM   6331  O  O   . ASP F  1 117 ? 40.935  66.280  32.536  1.00 27.24 ? 90  ASP E O   1 
ATOM   6332  C  CB  . ASP F  1 117 ? 38.279  65.758  30.194  1.00 31.80 ? 90  ASP E CB  1 
ATOM   6333  C  CG  . ASP F  1 117 ? 38.301  64.297  30.667  1.00 34.99 ? 90  ASP E CG  1 
ATOM   6334  O  OD1 . ASP F  1 117 ? 39.082  63.920  31.568  1.00 35.03 ? 90  ASP E OD1 1 
ATOM   6335  O  OD2 . ASP F  1 117 ? 37.514  63.508  30.102  1.00 42.93 ? 90  ASP E OD2 1 
ATOM   6336  N  N   . LYS F  1 118 ? 38.790  66.924  32.859  1.00 34.93 ? 91  LYS E N   1 
ATOM   6337  C  CA  . LYS F  1 118 ? 38.946  67.080  34.306  1.00 34.73 ? 91  LYS E CA  1 
ATOM   6338  C  C   . LYS F  1 118 ? 39.374  65.779  34.977  1.00 32.47 ? 91  LYS E C   1 
ATOM   6339  O  O   . LYS F  1 118 ? 40.050  65.807  36.012  1.00 36.96 ? 91  LYS E O   1 
ATOM   6340  C  CB  . LYS F  1 118 ? 37.624  67.561  34.933  1.00 43.26 ? 91  LYS E CB  1 
ATOM   6341  C  CG  . LYS F  1 118 ? 37.292  69.036  34.712  1.00 53.04 ? 91  LYS E CG  1 
ATOM   6342  C  CD  . LYS F  1 118 ? 37.836  69.929  35.822  1.00 58.05 ? 91  LYS E CD  1 
ATOM   6343  C  CE  . LYS F  1 118 ? 37.482  71.396  35.575  1.00 50.22 ? 91  LYS E CE  1 
ATOM   6344  N  NZ  . LYS F  1 118 ? 38.568  72.288  36.081  1.00 46.34 ? 91  LYS E NZ  1 
ATOM   6345  N  N   . ASP F  1 119 ? 38.973  64.637  34.416  1.00 29.01 ? 92  ASP E N   1 
ATOM   6346  C  CA  . ASP F  1 119 ? 39.332  63.309  34.909  1.00 35.09 ? 92  ASP E CA  1 
ATOM   6347  C  C   . ASP F  1 119 ? 40.710  62.830  34.443  1.00 36.57 ? 92  ASP E C   1 
ATOM   6348  O  O   . ASP F  1 119 ? 41.055  61.668  34.690  1.00 33.56 ? 92  ASP E O   1 
ATOM   6349  C  CB  . ASP F  1 119 ? 38.272  62.299  34.466  1.00 35.43 ? 92  ASP E CB  1 
ATOM   6350  C  CG  . ASP F  1 119 ? 36.907  62.594  35.060  1.00 52.50 ? 92  ASP E CG  1 
ATOM   6351  O  OD1 . ASP F  1 119 ? 36.856  63.129  36.189  1.00 56.02 ? 92  ASP E OD1 1 
ATOM   6352  O  OD2 . ASP F  1 119 ? 35.891  62.310  34.394  1.00 61.92 ? 92  ASP E OD2 1 
ATOM   6353  N  N   . GLY F  1 120 ? 41.486  63.678  33.771  1.00 29.59 ? 93  GLY E N   1 
ATOM   6354  C  CA  . GLY F  1 120 ? 42.816  63.316  33.330  1.00 29.67 ? 93  GLY E CA  1 
ATOM   6355  C  C   . GLY F  1 120 ? 42.897  62.520  32.040  1.00 26.53 ? 93  GLY E C   1 
ATOM   6356  O  O   . GLY F  1 120 ? 43.956  61.956  31.753  1.00 25.88 ? 93  GLY E O   1 
ATOM   6357  N  N   . VAL F  1 121 ? 41.826  62.466  31.253  1.00 23.17 ? 94  VAL E N   1 
ATOM   6358  C  CA  . VAL F  1 121 ? 41.742  61.620  30.069  1.00 26.76 ? 94  VAL E CA  1 
ATOM   6359  C  C   . VAL F  1 121 ? 41.698  62.496  28.824  1.00 29.69 ? 94  VAL E C   1 
ATOM   6360  O  O   . VAL F  1 121 ? 40.847  63.386  28.713  1.00 26.12 ? 94  VAL E O   1 
ATOM   6361  C  CB  . VAL F  1 121 ? 40.503  60.711  30.107  1.00 24.48 ? 94  VAL E CB  1 
ATOM   6362  C  CG1 . VAL F  1 121 ? 40.395  59.907  28.800  1.00 25.12 ? 94  VAL E CG1 1 
ATOM   6363  C  CG2 . VAL F  1 121 ? 40.530  59.799  31.341  1.00 27.97 ? 94  VAL E CG2 1 
ATOM   6364  N  N   . ALA F  1 122 ? 42.590  62.227  27.880  1.00 23.63 ? 95  ALA E N   1 
ATOM   6365  C  CA  . ALA F  1 122 ? 42.519  62.836  26.555  1.00 21.26 ? 95  ALA E CA  1 
ATOM   6366  C  C   . ALA F  1 122 ? 41.967  61.786  25.598  1.00 27.73 ? 95  ALA E C   1 
ATOM   6367  O  O   . ALA F  1 122 ? 42.622  60.767  25.347  1.00 24.27 ? 95  ALA E O   1 
ATOM   6368  C  CB  . ALA F  1 122 ? 43.892  63.336  26.109  1.00 21.58 ? 95  ALA E CB  1 
ATOM   6369  N  N   . ASP F  1 123 ? 40.749  62.014  25.094  1.00 23.57 ? 96  ASP E N   1 
ATOM   6370  C  CA  . ASP F  1 123 ? 40.154  61.165  24.062  1.00 27.17 ? 96  ASP E CA  1 
ATOM   6371  C  C   . ASP F  1 123 ? 40.599  61.704  22.708  1.00 27.86 ? 96  ASP E C   1 
ATOM   6372  O  O   . ASP F  1 123 ? 39.989  62.620  22.161  1.00 30.50 ? 96  ASP E O   1 
ATOM   6373  C  CB  . ASP F  1 123 ? 38.632  61.131  24.170  1.00 30.04 ? 96  ASP E CB  1 
ATOM   6374  C  CG  . ASP F  1 123 ? 38.138  60.351  25.395  1.00 45.19 ? 96  ASP E CG  1 
ATOM   6375  O  OD1 . ASP F  1 123 ? 38.671  59.246  25.664  1.00 38.08 ? 96  ASP E OD1 1 
ATOM   6376  O  OD2 . ASP F  1 123 ? 37.222  60.846  26.093  1.00 47.24 ? 96  ASP E OD2 1 
ATOM   6377  N  N   . VAL F  1 124 ? 41.641  61.118  22.153  1.00 23.87 ? 97  VAL E N   1 
ATOM   6378  C  CA  . VAL F  1 124 ? 42.284  61.677  20.967  1.00 19.60 ? 97  VAL E CA  1 
ATOM   6379  C  C   . VAL F  1 124 ? 41.460  61.346  19.735  1.00 22.95 ? 97  VAL E C   1 
ATOM   6380  O  O   . VAL F  1 124 ? 41.012  60.211  19.562  1.00 21.67 ? 97  VAL E O   1 
ATOM   6381  C  CB  . VAL F  1 124 ? 43.720  61.134  20.840  1.00 19.04 ? 97  VAL E CB  1 
ATOM   6382  C  CG1 . VAL F  1 124 ? 44.395  61.680  19.559  1.00 16.93 ? 97  VAL E CG1 1 
ATOM   6383  C  CG2 . VAL F  1 124 ? 44.532  61.490  22.069  1.00 19.24 ? 97  VAL E CG2 1 
ATOM   6384  N  N   . SER F  1 125 ? 41.279  62.336  18.860  1.00 22.26 ? 98  SER E N   1 
ATOM   6385  C  CA  . SER F  1 125 ? 40.605  62.123  17.578  1.00 22.67 ? 98  SER E CA  1 
ATOM   6386  C  C   . SER F  1 125 ? 41.152  63.161  16.602  1.00 27.09 ? 98  SER E C   1 
ATOM   6387  O  O   . SER F  1 125 ? 40.777  64.334  16.664  1.00 24.49 ? 98  SER E O   1 
ATOM   6388  C  CB  . SER F  1 125 ? 39.088  62.214  17.716  1.00 29.04 ? 98  SER E CB  1 
ATOM   6389  O  OG  . SER F  1 125 ? 38.459  61.624  16.587  1.00 34.77 ? 98  SER E OG  1 
ATOM   6390  N  N   . ILE F  1 126 ? 42.032  62.719  15.704  1.00 23.32 ? 99  ILE E N   1 
ATOM   6391  C  CA  . ILE F  1 126 ? 42.793  63.594  14.822  1.00 24.04 ? 99  ILE E CA  1 
ATOM   6392  C  C   . ILE F  1 126 ? 42.768  62.973  13.434  1.00 24.15 ? 99  ILE E C   1 
ATOM   6393  O  O   . ILE F  1 126 ? 42.731  61.749  13.287  1.00 24.46 ? 99  ILE E O   1 
ATOM   6394  C  CB  . ILE F  1 126 ? 44.243  63.764  15.360  1.00 24.79 ? 99  ILE E CB  1 
ATOM   6395  C  CG1 . ILE F  1 126 ? 44.264  64.736  16.541  1.00 25.85 ? 99  ILE E CG1 1 
ATOM   6396  C  CG2 . ILE F  1 126 ? 45.228  64.241  14.303  1.00 28.65 ? 99  ILE E CG2 1 
ATOM   6397  C  CD1 . ILE F  1 126 ? 45.610  64.748  17.270  1.00 26.83 ? 99  ILE E CD1 1 
ATOM   6398  N  N   . GLU F  1 127 ? 42.740  63.819  12.408  1.00 22.63 ? 100 GLU E N   1 
ATOM   6399  C  CA  . GLU F  1 127 ? 42.911  63.356  11.037  1.00 21.65 ? 100 GLU E CA  1 
ATOM   6400  C  C   . GLU F  1 127 ? 44.025  64.174  10.403  1.00 23.33 ? 100 GLU E C   1 
ATOM   6401  O  O   . GLU F  1 127 ? 44.005  65.407  10.462  1.00 24.72 ? 100 GLU E O   1 
ATOM   6402  C  CB  . GLU F  1 127 ? 41.591  63.473  10.271  1.00 29.19 ? 100 GLU E CB  1 
ATOM   6403  C  CG  . GLU F  1 127 ? 41.726  63.758  8.814   1.00 37.75 ? 100 GLU E CG  1 
ATOM   6404  C  CD  . GLU F  1 127 ? 40.524  63.270  8.014   1.00 51.78 ? 100 GLU E CD  1 
ATOM   6405  O  OE1 . GLU F  1 127 ? 40.488  63.530  6.794   1.00 55.71 ? 100 GLU E OE1 1 
ATOM   6406  O  OE2 . GLU F  1 127 ? 39.628  62.621  8.603   1.00 51.38 ? 100 GLU E OE2 1 
ATOM   6407  N  N   . ASP F  1 128 ? 45.027  63.494  9.840   1.00 22.56 ? 101 ASP E N   1 
ATOM   6408  C  CA  . ASP F  1 128 ? 46.189  64.205  9.335   1.00 20.54 ? 101 ASP E CA  1 
ATOM   6409  C  C   . ASP F  1 128 ? 46.619  63.642  7.989   1.00 26.32 ? 101 ASP E C   1 
ATOM   6410  O  O   . ASP F  1 128 ? 46.667  62.425  7.798   1.00 26.53 ? 101 ASP E O   1 
ATOM   6411  C  CB  . ASP F  1 128 ? 47.362  64.139  10.322  1.00 23.91 ? 101 ASP E CB  1 
ATOM   6412  C  CG  . ASP F  1 128 ? 48.469  65.134  9.975   1.00 29.59 ? 101 ASP E CG  1 
ATOM   6413  O  OD1 . ASP F  1 128 ? 48.312  66.353  10.251  1.00 31.31 ? 101 ASP E OD1 1 
ATOM   6414  O  OD2 . ASP F  1 128 ? 49.501  64.700  9.413   1.00 24.26 ? 101 ASP E OD2 1 
ATOM   6415  N  N   A SER F  1 129 ? 46.950  64.536  7.061   0.55 25.78 ? 102 SER E N   1 
ATOM   6416  N  N   B SER F  1 129 ? 46.961  64.542  7.068   0.45 25.81 ? 102 SER E N   1 
ATOM   6417  C  CA  A SER F  1 129 ? 47.320  64.139  5.711   0.55 25.69 ? 102 SER E CA  1 
ATOM   6418  C  CA  B SER F  1 129 ? 47.315  64.173  5.705   0.45 26.56 ? 102 SER E CA  1 
ATOM   6419  C  C   A SER F  1 129 ? 48.812  64.253  5.437   0.55 24.94 ? 102 SER E C   1 
ATOM   6420  C  C   B SER F  1 129 ? 48.801  64.340  5.412   0.45 24.71 ? 102 SER E C   1 
ATOM   6421  O  O   A SER F  1 129 ? 49.249  63.941  4.326   0.55 28.37 ? 102 SER E O   1 
ATOM   6422  O  O   B SER F  1 129 ? 49.215  64.174  4.262   0.45 28.32 ? 102 SER E O   1 
ATOM   6423  C  CB  A SER F  1 129 ? 46.542  64.974  4.689   0.55 29.72 ? 102 SER E CB  1 
ATOM   6424  C  CB  B SER F  1 129 ? 46.501  65.002  4.714   0.45 29.46 ? 102 SER E CB  1 
ATOM   6425  O  OG  A SER F  1 129 ? 45.156  64.722  4.812   0.55 27.50 ? 102 SER E OG  1 
ATOM   6426  O  OG  B SER F  1 129 ? 46.551  66.371  5.071   0.45 26.52 ? 102 SER E OG  1 
ATOM   6427  N  N   . VAL F  1 130 ? 49.614  64.676  6.407   1.00 22.90 ? 103 VAL E N   1 
ATOM   6428  C  CA  . VAL F  1 130 ? 51.051  64.798  6.202   1.00 19.32 ? 103 VAL E CA  1 
ATOM   6429  C  C   . VAL F  1 130 ? 51.799  63.578  6.734   1.00 24.33 ? 103 VAL E C   1 
ATOM   6430  O  O   . VAL F  1 130 ? 52.714  63.087  6.076   1.00 21.68 ? 103 VAL E O   1 
ATOM   6431  C  CB  . VAL F  1 130 ? 51.587  66.109  6.813   1.00 21.95 ? 103 VAL E CB  1 
ATOM   6432  C  CG1 . VAL F  1 130 ? 53.115  66.137  6.776   1.00 23.82 ? 103 VAL E CG1 1 
ATOM   6433  C  CG2 . VAL F  1 130 ? 51.032  67.307  6.031   1.00 26.45 ? 103 VAL E CG2 1 
ATOM   6434  N  N   . ILE F  1 131 ? 51.424  63.053  7.908   1.00 20.37 ? 104 ILE E N   1 
ATOM   6435  C  CA  . ILE F  1 131 ? 51.946  61.733  8.291   1.00 18.55 ? 104 ILE E CA  1 
ATOM   6436  C  C   . ILE F  1 131 ? 51.408  60.684  7.329   1.00 20.12 ? 104 ILE E C   1 
ATOM   6437  O  O   . ILE F  1 131 ? 50.393  60.881  6.659   1.00 20.06 ? 104 ILE E O   1 
ATOM   6438  C  CB  . ILE F  1 131 ? 51.586  61.368  9.741   1.00 17.26 ? 104 ILE E CB  1 
ATOM   6439  C  CG1 . ILE F  1 131 ? 50.067  61.445  9.971   1.00 18.03 ? 104 ILE E CG1 1 
ATOM   6440  C  CG2 . ILE F  1 131 ? 52.368  62.239  10.705  1.00 19.84 ? 104 ILE E CG2 1 
ATOM   6441  C  CD1 . ILE F  1 131 ? 49.553  60.676  11.257  1.00 18.41 ? 104 ILE E CD1 1 
ATOM   6442  N  N   . SER F  1 132 ? 52.085  59.542  7.276   1.00 17.49 ? 105 SER E N   1 
ATOM   6443  C  CA  . SER F  1 132 ? 51.589  58.434  6.476   1.00 19.12 ? 105 SER E CA  1 
ATOM   6444  C  C   . SER F  1 132 ? 51.994  57.136  7.158   1.00 21.39 ? 105 SER E C   1 
ATOM   6445  O  O   . SER F  1 132 ? 52.870  57.129  8.013   1.00 23.41 ? 105 SER E O   1 
ATOM   6446  C  CB  . SER F  1 132 ? 52.154  58.490  5.050   1.00 21.43 ? 105 SER E CB  1 
ATOM   6447  O  OG  . SER F  1 132 ? 51.527  57.519  4.255   1.00 20.74 ? 105 SER E OG  1 
ATOM   6448  N  N   . LEU F  1 133 ? 51.350  56.034  6.775   1.00 19.85 ? 106 LEU E N   1 
ATOM   6449  C  CA  . LEU F  1 133 ? 51.796  54.708  7.184   1.00 21.47 ? 106 LEU E CA  1 
ATOM   6450  C  C   . LEU F  1 133 ? 52.632  54.013  6.108   1.00 25.43 ? 106 LEU E C   1 
ATOM   6451  O  O   . LEU F  1 133 ? 52.906  52.816  6.223   1.00 23.20 ? 106 LEU E O   1 
ATOM   6452  C  CB  . LEU F  1 133 ? 50.596  53.839  7.564   1.00 22.58 ? 106 LEU E CB  1 
ATOM   6453  C  CG  . LEU F  1 133 ? 49.703  54.407  8.669   1.00 22.03 ? 106 LEU E CG  1 
ATOM   6454  C  CD1 . LEU F  1 133 ? 48.613  53.417  9.043   1.00 22.53 ? 106 LEU E CD1 1 
ATOM   6455  C  CD2 . LEU F  1 133 ? 50.543  54.789  9.878   1.00 19.64 ? 106 LEU E CD2 1 
ATOM   6456  N  N   . SER F  1 134 ? 53.055  54.738  5.076   1.00 21.71 ? 107 SER E N   1 
ATOM   6457  C  CA  . SER F  1 134 ? 53.954  54.193  4.068   1.00 29.05 ? 107 SER E CA  1 
ATOM   6458  C  C   . SER F  1 134 ? 54.737  55.335  3.437   1.00 31.47 ? 107 SER E C   1 
ATOM   6459  O  O   . SER F  1 134 ? 54.386  56.508  3.592   1.00 24.53 ? 107 SER E O   1 
ATOM   6460  C  CB  . SER F  1 134 ? 53.180  53.409  3.000   1.00 30.55 ? 107 SER E CB  1 
ATOM   6461  O  OG  . SER F  1 134 ? 52.209  54.228  2.378   1.00 33.46 ? 107 SER E OG  1 
ATOM   6462  N  N   . GLY F  1 135 ? 55.813  54.982  2.720   1.00 27.06 ? 108 GLY E N   1 
ATOM   6463  C  CA  . GLY F  1 135 ? 56.553  55.982  1.964   1.00 27.98 ? 108 GLY E CA  1 
ATOM   6464  C  C   . GLY F  1 135 ? 57.447  56.868  2.822   1.00 27.35 ? 108 GLY E C   1 
ATOM   6465  O  O   . GLY F  1 135 ? 57.750  56.571  3.981   1.00 28.14 ? 108 GLY E O   1 
ATOM   6466  N  N   . ASP F  1 136 ? 57.864  57.996  2.225   1.00 22.15 ? 109 ASP E N   1 
ATOM   6467  C  CA  . ASP F  1 136 ? 58.845  58.890  2.853   1.00 26.17 ? 109 ASP E CA  1 
ATOM   6468  C  C   . ASP F  1 136 ? 58.407  59.386  4.223   1.00 24.92 ? 109 ASP E C   1 
ATOM   6469  O  O   . ASP F  1 136 ? 59.250  59.698  5.078   1.00 23.89 ? 109 ASP E O   1 
ATOM   6470  C  CB  . ASP F  1 136 ? 59.081  60.135  1.989   1.00 28.07 ? 109 ASP E CB  1 
ATOM   6471  C  CG  . ASP F  1 136 ? 60.111  59.916  0.889   1.00 41.55 ? 109 ASP E CG  1 
ATOM   6472  O  OD1 . ASP F  1 136 ? 60.817  58.884  0.913   1.00 44.33 ? 109 ASP E OD1 1 
ATOM   6473  O  OD2 . ASP F  1 136 ? 60.203  60.788  0.003   1.00 34.93 ? 109 ASP E OD2 1 
ATOM   6474  N  N   . HIS F  1 137 ? 57.108  59.586  4.407   1.00 22.24 ? 110 HIS E N   1 
ATOM   6475  C  CA  . HIS F  1 137 ? 56.586  60.158  5.641   1.00 23.99 ? 110 HIS E CA  1 
ATOM   6476  C  C   . HIS F  1 137 ? 56.061  59.093  6.578   1.00 23.33 ? 110 HIS E C   1 
ATOM   6477  O  O   . HIS F  1 137 ? 55.282  59.404  7.487   1.00 22.00 ? 110 HIS E O   1 
ATOM   6478  C  CB  . HIS F  1 137 ? 55.490  61.175  5.331   1.00 21.38 ? 110 HIS E CB  1 
ATOM   6479  C  CG  . HIS F  1 137 ? 55.991  62.392  4.612   1.00 29.61 ? 110 HIS E CG  1 
ATOM   6480  N  ND1 . HIS F  1 137 ? 55.148  63.363  4.116   1.00 37.85 ? 110 HIS E ND1 1 
ATOM   6481  C  CD2 . HIS F  1 137 ? 57.249  62.783  4.291   1.00 32.30 ? 110 HIS E CD2 1 
ATOM   6482  C  CE1 . HIS F  1 137 ? 55.865  64.304  3.526   1.00 33.30 ? 110 HIS E CE1 1 
ATOM   6483  N  NE2 . HIS F  1 137 ? 57.142  63.979  3.624   1.00 39.23 ? 110 HIS E NE2 1 
ATOM   6484  N  N   . CYS F  1 138 ? 56.476  57.842  6.375   1.00 23.15 ? 111 CYS E N   1 
ATOM   6485  C  CA  . CYS F  1 138 ? 55.974  56.737  7.175   1.00 21.76 ? 111 CYS E CA  1 
ATOM   6486  C  C   . CYS F  1 138 ? 56.385  56.916  8.628   1.00 16.61 ? 111 CYS E C   1 
ATOM   6487  O  O   . CYS F  1 138 ? 57.549  57.205  8.921   1.00 19.08 ? 111 CYS E O   1 
ATOM   6488  C  CB  . CYS F  1 138 ? 56.529  55.423  6.634   1.00 22.26 ? 111 CYS E CB  1 
ATOM   6489  S  SG  . CYS F  1 138 ? 55.963  53.993  7.535   1.00 27.14 ? 111 CYS E SG  1 
ATOM   6490  N  N   . ILE F  1 139 ? 55.422  56.776  9.538   1.00 17.96 ? 112 ILE E N   1 
ATOM   6491  C  CA  . ILE F  1 139 ? 55.717  56.928  10.963  1.00 16.18 ? 112 ILE E CA  1 
ATOM   6492  C  C   . ILE F  1 139 ? 55.818  55.590  11.693  1.00 17.35 ? 112 ILE E C   1 
ATOM   6493  O  O   . ILE F  1 139 ? 56.152  55.572  12.885  1.00 18.98 ? 112 ILE E O   1 
ATOM   6494  C  CB  . ILE F  1 139 ? 54.677  57.843  11.642  1.00 16.51 ? 112 ILE E CB  1 
ATOM   6495  C  CG1 . ILE F  1 139 ? 53.282  57.232  11.542  1.00 18.94 ? 112 ILE E CG1 1 
ATOM   6496  C  CG2 . ILE F  1 139 ? 54.750  59.248  11.054  1.00 17.95 ? 112 ILE E CG2 1 
ATOM   6497  C  CD1 . ILE F  1 139 ? 52.214  57.999  12.341  1.00 23.27 ? 112 ILE E CD1 1 
ATOM   6498  N  N   . ILE F  1 140 ? 55.567  54.469  11.010  1.00 23.85 ? 113 ILE E N   1 
ATOM   6499  C  CA  . ILE F  1 140 ? 55.770  53.158  11.618  1.00 20.89 ? 113 ILE E CA  1 
ATOM   6500  C  C   . ILE F  1 140 ? 57.239  52.999  11.961  1.00 20.06 ? 113 ILE E C   1 
ATOM   6501  O  O   . ILE F  1 140 ? 58.122  53.368  11.172  1.00 18.83 ? 113 ILE E O   1 
ATOM   6502  C  CB  . ILE F  1 140 ? 55.278  52.063  10.657  1.00 25.31 ? 113 ILE E CB  1 
ATOM   6503  C  CG1 . ILE F  1 140 ? 53.756  52.122  10.581  1.00 25.46 ? 113 ILE E CG1 1 
ATOM   6504  C  CG2 . ILE F  1 140 ? 55.785  50.661  11.093  1.00 22.85 ? 113 ILE E CG2 1 
ATOM   6505  C  CD1 . ILE F  1 140 ? 53.162  51.193  9.560   1.00 31.23 ? 113 ILE E CD1 1 
ATOM   6506  N  N   . GLY F  1 141 ? 57.511  52.506  13.170  1.00 21.04 ? 114 GLY E N   1 
ATOM   6507  C  CA  . GLY F  1 141 ? 58.873  52.414  13.657  1.00 18.35 ? 114 GLY E CA  1 
ATOM   6508  C  C   . GLY F  1 141 ? 59.416  53.674  14.295  1.00 22.03 ? 114 GLY E C   1 
ATOM   6509  O  O   . GLY F  1 141 ? 60.581  53.685  14.721  1.00 15.53 ? 114 GLY E O   1 
ATOM   6510  N  N   . ARG F  1 142 ? 58.624  54.735  14.375  1.00 15.64 ? 115 ARG E N   1 
ATOM   6511  C  CA  . ARG F  1 142 ? 59.036  55.952  15.051  1.00 16.66 ? 115 ARG E CA  1 
ATOM   6512  C  C   . ARG F  1 142 ? 58.287  56.031  16.371  1.00 14.70 ? 115 ARG E C   1 
ATOM   6513  O  O   . ARG F  1 142 ? 57.535  55.127  16.718  1.00 19.45 ? 115 ARG E O   1 
ATOM   6514  C  CB  . ARG F  1 142 ? 58.807  57.160  14.137  1.00 16.75 ? 115 ARG E CB  1 
ATOM   6515  C  CG  . ARG F  1 142 ? 59.430  56.887  12.750  1.00 22.26 ? 115 ARG E CG  1 
ATOM   6516  C  CD  . ARG F  1 142 ? 59.674  58.136  11.937  1.00 18.25 ? 115 ARG E CD  1 
ATOM   6517  N  NE  . ARG F  1 142 ? 60.180  57.805  10.602  1.00 20.56 ? 115 ARG E NE  1 
ATOM   6518  C  CZ  . ARG F  1 142 ? 61.470  57.828  10.278  1.00 21.38 ? 115 ARG E CZ  1 
ATOM   6519  N  NH1 . ARG F  1 142 ? 62.402  58.123  11.172  1.00 20.51 ? 115 ARG E NH1 1 
ATOM   6520  N  NH2 . ARG F  1 142 ? 61.831  57.592  9.014   1.00 21.18 ? 115 ARG E NH2 1 
ATOM   6521  N  N   . THR F  1 143 ? 58.503  57.105  17.116  1.00 16.40 ? 116 THR E N   1 
ATOM   6522  C  CA  . THR F  1 143 ? 57.971  57.198  18.472  1.00 14.68 ? 116 THR E CA  1 
ATOM   6523  C  C   . THR F  1 143 ? 56.924  58.302  18.576  1.00 19.25 ? 116 THR E C   1 
ATOM   6524  O  O   . THR F  1 143 ? 57.186  59.445  18.191  1.00 21.31 ? 116 THR E O   1 
ATOM   6525  C  CB  . THR F  1 143 ? 59.083  57.449  19.473  1.00 24.43 ? 116 THR E CB  1 
ATOM   6526  O  OG1 . THR F  1 143 ? 59.981  56.338  19.465  1.00 22.37 ? 116 THR E OG1 1 
ATOM   6527  C  CG2 . THR F  1 143 ? 58.512  57.630  20.899  1.00 13.42 ? 116 THR E CG2 1 
ATOM   6528  N  N   . LEU F  1 144 ? 55.760  57.960  19.121  1.00 13.42 ? 117 LEU E N   1 
ATOM   6529  C  CA  . LEU F  1 144 ? 54.735  58.948  19.450  1.00 13.42 ? 117 LEU E CA  1 
ATOM   6530  C  C   . LEU F  1 144 ? 54.967  59.374  20.896  1.00 17.28 ? 117 LEU E C   1 
ATOM   6531  O  O   . LEU F  1 144 ? 55.163  58.514  21.749  1.00 13.56 ? 117 LEU E O   1 
ATOM   6532  C  CB  . LEU F  1 144 ? 53.342  58.350  19.311  1.00 13.42 ? 117 LEU E CB  1 
ATOM   6533  C  CG  . LEU F  1 144 ? 52.153  59.286  19.575  1.00 13.42 ? 117 LEU E CG  1 
ATOM   6534  C  CD1 . LEU F  1 144 ? 52.083  60.385  18.468  1.00 18.94 ? 117 LEU E CD1 1 
ATOM   6535  C  CD2 . LEU F  1 144 ? 50.873  58.463  19.590  1.00 13.94 ? 117 LEU E CD2 1 
ATOM   6536  N  N   . VAL F  1 145 ? 54.955  60.685  21.155  1.00 13.42 ? 118 VAL E N   1 
ATOM   6537  C  CA  . VAL F  1 145 ? 55.230  61.232  22.483  1.00 17.48 ? 118 VAL E CA  1 
ATOM   6538  C  C   . VAL F  1 145 ? 54.100  62.184  22.860  1.00 15.90 ? 118 VAL E C   1 
ATOM   6539  O  O   . VAL F  1 145 ? 53.723  63.047  22.059  1.00 13.42 ? 118 VAL E O   1 
ATOM   6540  C  CB  . VAL F  1 145 ? 56.574  61.983  22.518  1.00 16.19 ? 118 VAL E CB  1 
ATOM   6541  C  CG1 . VAL F  1 145 ? 56.803  62.609  23.934  1.00 16.85 ? 118 VAL E CG1 1 
ATOM   6542  C  CG2 . VAL F  1 145 ? 57.734  61.052  22.140  1.00 13.42 ? 118 VAL E CG2 1 
ATOM   6543  N  N   . VAL F  1 146 ? 53.598  62.068  24.090  1.00 19.67 ? 119 VAL E N   1 
ATOM   6544  C  CA  . VAL F  1 146 ? 52.711  63.076  24.654  1.00 17.00 ? 119 VAL E CA  1 
ATOM   6545  C  C   . VAL F  1 146 ? 53.519  63.884  25.661  1.00 20.39 ? 119 VAL E C   1 
ATOM   6546  O  O   . VAL F  1 146 ? 54.265  63.323  26.480  1.00 16.60 ? 119 VAL E O   1 
ATOM   6547  C  CB  . VAL F  1 146 ? 51.446  62.460  25.283  1.00 19.17 ? 119 VAL E CB  1 
ATOM   6548  C  CG1 . VAL F  1 146 ? 51.801  61.516  26.450  1.00 20.86 ? 119 VAL E CG1 1 
ATOM   6549  C  CG2 . VAL F  1 146 ? 50.498  63.567  25.756  1.00 16.37 ? 119 VAL E CG2 1 
ATOM   6550  N  N   . HIS F  1 147 ? 53.405  65.200  25.571  1.00 15.74 ? 120 HIS E N   1 
ATOM   6551  C  CA  . HIS F  1 147 ? 54.303  66.108  26.263  1.00 17.71 ? 120 HIS E CA  1 
ATOM   6552  C  C   . HIS F  1 147 ? 53.626  66.740  27.478  1.00 14.46 ? 120 HIS E C   1 
ATOM   6553  O  O   . HIS F  1 147 ? 52.414  66.671  27.666  1.00 17.59 ? 120 HIS E O   1 
ATOM   6554  C  CB  . HIS F  1 147 ? 54.815  67.195  25.306  1.00 13.75 ? 120 HIS E CB  1 
ATOM   6555  C  CG  . HIS F  1 147 ? 55.848  66.700  24.330  1.00 19.80 ? 120 HIS E CG  1 
ATOM   6556  N  ND1 . HIS F  1 147 ? 57.202  66.852  24.539  1.00 19.45 ? 120 HIS E ND1 1 
ATOM   6557  C  CD2 . HIS F  1 147 ? 55.722  66.089  23.126  1.00 18.89 ? 120 HIS E CD2 1 
ATOM   6558  C  CE1 . HIS F  1 147 ? 57.867  66.346  23.512  1.00 22.11 ? 120 HIS E CE1 1 
ATOM   6559  N  NE2 . HIS F  1 147 ? 56.990  65.869  22.642  1.00 20.63 ? 120 HIS E NE2 1 
ATOM   6560  N  N   . GLU F  1 148 ? 54.469  67.381  28.285  1.00 22.65 ? 121 GLU E N   1 
ATOM   6561  C  CA  . GLU F  1 148 ? 54.091  67.937  29.584  1.00 23.68 ? 121 GLU E CA  1 
ATOM   6562  C  C   . GLU F  1 148 ? 53.173  69.148  29.453  1.00 23.00 ? 121 GLU E C   1 
ATOM   6563  O  O   . GLU F  1 148 ? 52.224  69.294  30.231  1.00 21.17 ? 121 GLU E O   1 
ATOM   6564  C  CB  . GLU F  1 148 ? 55.380  68.297  30.327  1.00 26.29 ? 121 GLU E CB  1 
ATOM   6565  C  CG  . GLU F  1 148 ? 55.269  69.292  31.473  1.00 35.63 ? 121 GLU E CG  1 
ATOM   6566  C  CD  . GLU F  1 148 ? 56.655  69.705  31.998  1.00 42.09 ? 121 GLU E CD  1 
ATOM   6567  O  OE1 . GLU F  1 148 ? 57.553  70.081  31.183  1.00 34.63 ? 121 GLU E OE1 1 
ATOM   6568  O  OE2 . GLU F  1 148 ? 56.842  69.661  33.229  1.00 59.86 ? 121 GLU E OE2 1 
ATOM   6569  N  N   . LYS F  1 149 ? 53.443  70.027  28.490  1.00 20.11 ? 122 LYS E N   1 
ATOM   6570  C  CA  . LYS F  1 149 ? 52.779  71.318  28.319  1.00 22.10 ? 122 LYS E CA  1 
ATOM   6571  C  C   . LYS F  1 149 ? 52.170  71.436  26.926  1.00 20.75 ? 122 LYS E C   1 
ATOM   6572  O  O   . LYS F  1 149 ? 52.384  70.595  26.055  1.00 19.07 ? 122 LYS E O   1 
ATOM   6573  C  CB  . LYS F  1 149 ? 53.768  72.476  28.509  1.00 23.22 ? 122 LYS E CB  1 
ATOM   6574  C  CG  . LYS F  1 149 ? 54.793  72.230  29.582  1.00 34.19 ? 122 LYS E CG  1 
ATOM   6575  C  CD  . LYS F  1 149 ? 55.313  73.519  30.183  1.00 34.40 ? 122 LYS E CD  1 
ATOM   6576  C  CE  . LYS F  1 149 ? 56.191  74.245  29.193  1.00 36.08 ? 122 LYS E CE  1 
ATOM   6577  N  NZ  . LYS F  1 149 ? 57.613  73.790  29.273  1.00 51.10 ? 122 LYS E NZ  1 
ATOM   6578  N  N   . ALA F  1 150 ? 51.464  72.548  26.707  1.00 21.84 ? 123 ALA E N   1 
ATOM   6579  C  CA  . ALA F  1 150 ? 50.864  72.801  25.409  1.00 21.50 ? 123 ALA E CA  1 
ATOM   6580  C  C   . ALA F  1 150 ? 51.935  73.096  24.371  1.00 19.27 ? 123 ALA E C   1 
ATOM   6581  O  O   . ALA F  1 150 ? 52.942  73.751  24.655  1.00 21.09 ? 123 ALA E O   1 
ATOM   6582  C  CB  . ALA F  1 150 ? 49.880  73.972  25.487  1.00 22.96 ? 123 ALA E CB  1 
ATOM   6583  N  N   . ASP F  1 151 ? 51.694  72.612  23.155  1.00 19.66 ? 124 ASP E N   1 
ATOM   6584  C  CA  . ASP F  1 151 ? 52.474  72.987  21.987  1.00 16.61 ? 124 ASP E CA  1 
ATOM   6585  C  C   . ASP F  1 151 ? 52.044  74.387  21.539  1.00 18.79 ? 124 ASP E C   1 
ATOM   6586  O  O   . ASP F  1 151 ? 50.855  74.621  21.322  1.00 21.42 ? 124 ASP E O   1 
ATOM   6587  C  CB  . ASP F  1 151 ? 52.206  71.938  20.903  1.00 15.89 ? 124 ASP E CB  1 
ATOM   6588  C  CG  . ASP F  1 151 ? 53.012  72.132  19.638  1.00 23.40 ? 124 ASP E CG  1 
ATOM   6589  O  OD1 . ASP F  1 151 ? 53.679  73.170  19.429  1.00 21.30 ? 124 ASP E OD1 1 
ATOM   6590  O  OD2 . ASP F  1 151 ? 52.944  71.197  18.814  1.00 23.21 ? 124 ASP E OD2 1 
ATOM   6591  N  N   . ASP F  1 152 ? 52.994  75.319  21.412  1.00 16.43 ? 125 ASP E N   1 
ATOM   6592  C  CA  . ASP F  1 152 ? 52.636  76.667  20.955  1.00 22.33 ? 125 ASP E CA  1 
ATOM   6593  C  C   . ASP F  1 152 ? 52.552  76.780  19.431  1.00 18.05 ? 125 ASP E C   1 
ATOM   6594  O  O   . ASP F  1 152 ? 52.440  77.897  18.904  1.00 17.39 ? 125 ASP E O   1 
ATOM   6595  C  CB  . ASP F  1 152 ? 53.598  77.726  21.543  1.00 23.31 ? 125 ASP E CB  1 
ATOM   6596  C  CG  . ASP F  1 152 ? 55.032  77.692  20.959  1.00 23.56 ? 125 ASP E CG  1 
ATOM   6597  O  OD1 . ASP F  1 152 ? 55.307  77.105  19.873  1.00 21.25 ? 125 ASP E OD1 1 
ATOM   6598  O  OD2 . ASP F  1 152 ? 55.918  78.298  21.627  1.00 24.04 ? 125 ASP E OD2 1 
ATOM   6599  N  N   . LEU F  1 153 ? 52.622  75.647  18.732  1.00 20.27 ? 126 LEU E N   1 
ATOM   6600  C  CA  . LEU F  1 153 ? 52.438  75.561  17.277  1.00 18.38 ? 126 LEU E CA  1 
ATOM   6601  C  C   . LEU F  1 153 ? 53.472  76.391  16.526  1.00 18.26 ? 126 LEU E C   1 
ATOM   6602  O  O   . LEU F  1 153 ? 53.255  76.797  15.374  1.00 19.46 ? 126 LEU E O   1 
ATOM   6603  C  CB  . LEU F  1 153 ? 51.014  75.959  16.873  1.00 22.43 ? 126 LEU E CB  1 
ATOM   6604  C  CG  . LEU F  1 153 ? 49.897  75.304  17.698  1.00 23.42 ? 126 LEU E CG  1 
ATOM   6605  C  CD1 . LEU F  1 153 ? 48.527  75.717  17.184  1.00 33.16 ? 126 LEU E CD1 1 
ATOM   6606  C  CD2 . LEU F  1 153 ? 50.019  73.779  17.765  1.00 19.34 ? 126 LEU E CD2 1 
ATOM   6607  N  N   . GLY F  1 154 ? 54.629  76.601  17.144  1.00 18.17 ? 127 GLY E N   1 
ATOM   6608  C  CA  . GLY F  1 154 ? 55.713  77.298  16.485  1.00 17.13 ? 127 GLY E CA  1 
ATOM   6609  C  C   . GLY F  1 154 ? 55.584  78.805  16.478  1.00 21.06 ? 127 GLY E C   1 
ATOM   6610  O  O   . GLY F  1 154 ? 56.333  79.469  15.758  1.00 19.16 ? 127 GLY E O   1 
ATOM   6611  N  N   . LYS F  1 155 ? 54.641  79.361  17.230  1.00 14.22 ? 128 LYS E N   1 
ATOM   6612  C  CA  . LYS F  1 155 ? 54.384  80.795  17.248  1.00 18.69 ? 128 LYS E CA  1 
ATOM   6613  C  C   . LYS F  1 155 ? 54.907  81.464  18.522  1.00 21.18 ? 128 LYS E C   1 
ATOM   6614  O  O   . LYS F  1 155 ? 54.467  82.572  18.861  1.00 22.97 ? 128 LYS E O   1 
ATOM   6615  C  CB  . LYS F  1 155 ? 52.880  81.057  17.088  1.00 21.75 ? 128 LYS E CB  1 
ATOM   6616  C  CG  . LYS F  1 155 ? 52.217  80.398  15.858  1.00 25.22 ? 128 LYS E CG  1 
ATOM   6617  C  CD  . LYS F  1 155 ? 50.810  80.977  15.686  1.00 32.10 ? 128 LYS E CD  1 
ATOM   6618  C  CE  . LYS F  1 155 ? 50.114  80.392  14.492  1.00 43.27 ? 128 LYS E CE  1 
ATOM   6619  N  NZ  . LYS F  1 155 ? 51.062  79.655  13.625  1.00 52.46 ? 128 LYS E NZ  1 
ATOM   6620  N  N   . GLY F  1 156 ? 55.845  80.819  19.223  1.00 20.22 ? 129 GLY E N   1 
ATOM   6621  C  CA  . GLY F  1 156 ? 56.337  81.296  20.508  1.00 19.81 ? 129 GLY E CA  1 
ATOM   6622  C  C   . GLY F  1 156 ? 57.437  82.329  20.432  1.00 19.70 ? 129 GLY E C   1 
ATOM   6623  O  O   . GLY F  1 156 ? 57.697  83.007  21.430  1.00 20.66 ? 129 GLY E O   1 
ATOM   6624  N  N   . GLY F  1 157 ? 58.087  82.474  19.275  1.00 13.64 ? 130 GLY E N   1 
ATOM   6625  C  CA  . GLY F  1 157 ? 59.070  83.520  19.056  1.00 14.89 ? 130 GLY E CA  1 
ATOM   6626  C  C   . GLY F  1 157 ? 60.423  83.302  19.702  1.00 22.51 ? 130 GLY E C   1 
ATOM   6627  O  O   . GLY F  1 157 ? 61.294  84.178  19.591  1.00 22.91 ? 130 GLY E O   1 
ATOM   6628  N  N   . ASN F  1 158 ? 60.636  82.183  20.382  1.00 23.15 ? 131 ASN E N   1 
ATOM   6629  C  CA  . ASN F  1 158 ? 61.963  81.823  20.862  1.00 23.77 ? 131 ASN E CA  1 
ATOM   6630  C  C   . ASN F  1 158 ? 62.493  80.641  20.063  1.00 25.76 ? 131 ASN E C   1 
ATOM   6631  O  O   . ASN F  1 158 ? 61.782  80.042  19.250  1.00 24.46 ? 131 ASN E O   1 
ATOM   6632  C  CB  . ASN F  1 158 ? 61.947  81.527  22.373  1.00 22.48 ? 131 ASN E CB  1 
ATOM   6633  C  CG  . ASN F  1 158 ? 61.136  80.287  22.744  1.00 25.84 ? 131 ASN E CG  1 
ATOM   6634  O  OD1 . ASN F  1 158 ? 60.402  79.730  21.932  1.00 24.76 ? 131 ASN E OD1 1 
ATOM   6635  N  ND2 . ASN F  1 158 ? 61.263  79.859  24.011  1.00 24.27 ? 131 ASN E ND2 1 
ATOM   6636  N  N   . GLU F  1 159 ? 63.772  80.308  20.286  1.00 26.49 ? 132 GLU E N   1 
ATOM   6637  C  CA  . GLU F  1 159 ? 64.379  79.225  19.515  1.00 27.68 ? 132 GLU E CA  1 
ATOM   6638  C  C   . GLU F  1 159 ? 63.659  77.906  19.754  1.00 24.62 ? 132 GLU E C   1 
ATOM   6639  O  O   . GLU F  1 159 ? 63.389  77.156  18.809  1.00 26.01 ? 132 GLU E O   1 
ATOM   6640  C  CB  . GLU F  1 159 ? 65.864  79.089  19.854  1.00 30.96 ? 132 GLU E CB  1 
ATOM   6641  C  CG  . GLU F  1 159 ? 66.622  80.410  19.870  1.00 38.68 ? 132 GLU E CG  1 
ATOM   6642  C  CD  . GLU F  1 159 ? 68.064  80.279  20.384  1.00 55.75 ? 132 GLU E CD  1 
ATOM   6643  O  OE1 . GLU F  1 159 ? 68.440  79.186  20.862  1.00 60.94 ? 132 GLU E OE1 1 
ATOM   6644  O  OE2 . GLU F  1 159 ? 68.818  81.278  20.314  1.00 54.78 ? 132 GLU E OE2 1 
ATOM   6645  N  N   . GLU F  1 160 ? 63.337  77.610  21.014  1.00 22.57 ? 133 GLU E N   1 
ATOM   6646  C  CA  . GLU F  1 160 ? 62.651  76.364  21.353  1.00 26.52 ? 133 GLU E CA  1 
ATOM   6647  C  C   . GLU F  1 160 ? 61.333  76.212  20.603  1.00 28.27 ? 133 GLU E C   1 
ATOM   6648  O  O   . GLU F  1 160 ? 60.956  75.096  20.246  1.00 24.52 ? 133 GLU E O   1 
ATOM   6649  C  CB  . GLU F  1 160 ? 62.392  76.297  22.861  1.00 24.57 ? 133 GLU E CB  1 
ATOM   6650  C  CG  . GLU F  1 160 ? 62.188  74.904  23.416  1.00 33.38 ? 133 GLU E CG  1 
ATOM   6651  C  CD  . GLU F  1 160 ? 63.315  73.949  23.033  1.00 48.34 ? 133 GLU E CD  1 
ATOM   6652  O  OE1 . GLU F  1 160 ? 64.468  74.168  23.464  1.00 47.86 ? 133 GLU E OE1 1 
ATOM   6653  O  OE2 . GLU F  1 160 ? 63.042  72.981  22.293  1.00 46.91 ? 133 GLU E OE2 1 
ATOM   6654  N  N   . SER F  1 161 ? 60.626  77.314  20.336  1.00 23.02 ? 134 SER E N   1 
ATOM   6655  C  CA  . SER F  1 161 ? 59.334  77.191  19.661  1.00 18.78 ? 134 SER E CA  1 
ATOM   6656  C  C   . SER F  1 161 ? 59.499  76.611  18.267  1.00 20.84 ? 134 SER E C   1 
ATOM   6657  O  O   . SER F  1 161 ? 58.666  75.813  17.821  1.00 18.55 ? 134 SER E O   1 
ATOM   6658  C  CB  . SER F  1 161 ? 58.642  78.550  19.581  1.00 21.65 ? 134 SER E CB  1 
ATOM   6659  O  OG  . SER F  1 161 ? 57.452  78.435  18.837  1.00 21.08 ? 134 SER E OG  1 
ATOM   6660  N  N   . THR F  1 162 ? 60.560  77.011  17.557  1.00 17.57 ? 135 THR E N   1 
ATOM   6661  C  CA  . THR F  1 162 ? 60.808  76.501  16.212  1.00 17.39 ? 135 THR E CA  1 
ATOM   6662  C  C   . THR F  1 162 ? 61.241  75.041  16.194  1.00 27.74 ? 135 THR E C   1 
ATOM   6663  O  O   . THR F  1 162 ? 61.361  74.467  15.108  1.00 24.56 ? 135 THR E O   1 
ATOM   6664  C  CB  . THR F  1 162 ? 61.888  77.334  15.514  1.00 24.10 ? 135 THR E CB  1 
ATOM   6665  O  OG1 . THR F  1 162 ? 63.178  76.945  16.019  1.00 29.67 ? 135 THR E OG1 1 
ATOM   6666  C  CG2 . THR F  1 162 ? 61.680  78.833  15.758  1.00 28.09 ? 135 THR E CG2 1 
ATOM   6667  N  N   . LYS F  1 163 ? 61.514  74.443  17.355  1.00 24.00 ? 136 LYS E N   1 
ATOM   6668  C  CA  . LYS F  1 163 ? 61.961  73.055  17.442  1.00 24.76 ? 136 LYS E CA  1 
ATOM   6669  C  C   . LYS F  1 163 ? 60.935  72.134  18.076  1.00 23.14 ? 136 LYS E C   1 
ATOM   6670  O  O   . LYS F  1 163 ? 60.630  71.074  17.521  1.00 22.50 ? 136 LYS E O   1 
ATOM   6671  C  CB  . LYS F  1 163 ? 63.286  72.973  18.223  1.00 24.63 ? 136 LYS E CB  1 
ATOM   6672  C  CG  . LYS F  1 163 ? 64.383  73.817  17.572  1.00 29.48 ? 136 LYS E CG  1 
ATOM   6673  C  CD  . LYS F  1 163 ? 65.760  73.582  18.158  1.00 39.01 ? 136 LYS E CD  1 
ATOM   6674  C  CE  . LYS F  1 163 ? 65.804  73.963  19.628  1.00 40.77 ? 136 LYS E CE  1 
ATOM   6675  N  NZ  . LYS F  1 163 ? 67.192  74.279  20.104  1.00 52.51 ? 136 LYS E NZ  1 
ATOM   6676  N  N   . THR F  1 164 ? 60.398  72.507  19.250  1.00 23.63 ? 137 THR E N   1 
ATOM   6677  C  CA  . THR F  1 164 ? 59.513  71.638  20.005  1.00 22.46 ? 137 THR E CA  1 
ATOM   6678  C  C   . THR F  1 164 ? 58.161  72.250  20.330  1.00 21.35 ? 137 THR E C   1 
ATOM   6679  O  O   . THR F  1 164 ? 57.354  71.588  20.992  1.00 23.08 ? 137 THR E O   1 
ATOM   6680  C  CB  . THR F  1 164 ? 60.165  71.232  21.334  1.00 27.96 ? 137 THR E CB  1 
ATOM   6681  O  OG1 . THR F  1 164 ? 60.352  72.407  22.137  1.00 24.19 ? 137 THR E OG1 1 
ATOM   6682  C  CG2 . THR F  1 164 ? 61.522  70.549  21.078  1.00 32.97 ? 137 THR E CG2 1 
ATOM   6683  N  N   . GLY F  1 165 ? 57.894  73.491  19.917  1.00 19.03 ? 138 GLY E N   1 
ATOM   6684  C  CA  . GLY F  1 165 ? 56.699  74.174  20.348  1.00 20.21 ? 138 GLY E CA  1 
ATOM   6685  C  C   . GLY F  1 165 ? 56.673  74.525  21.826  1.00 18.90 ? 138 GLY E C   1 
ATOM   6686  O  O   . GLY F  1 165 ? 55.612  74.878  22.338  1.00 17.06 ? 138 GLY E O   1 
ATOM   6687  N  N   . ASN F  1 166 ? 57.806  74.443  22.526  1.00 23.25 ? 139 ASN E N   1 
ATOM   6688  C  CA  . ASN F  1 166 ? 57.856  74.657  23.987  1.00 21.71 ? 139 ASN E CA  1 
ATOM   6689  C  C   . ASN F  1 166 ? 56.952  73.690  24.749  1.00 21.18 ? 139 ASN E C   1 
ATOM   6690  O  O   . ASN F  1 166 ? 56.430  74.019  25.830  1.00 21.92 ? 139 ASN E O   1 
ATOM   6691  C  CB  . ASN F  1 166 ? 57.509  76.111  24.350  1.00 21.74 ? 139 ASN E CB  1 
ATOM   6692  C  CG  . ASN F  1 166 ? 58.627  77.072  23.996  1.00 21.84 ? 139 ASN E CG  1 
ATOM   6693  O  OD1 . ASN F  1 166 ? 59.673  77.058  24.622  1.00 24.35 ? 139 ASN E OD1 1 
ATOM   6694  N  ND2 . ASN F  1 166 ? 58.424  77.882  22.960  1.00 20.91 ? 139 ASN E ND2 1 
ATOM   6695  N  N   . ALA F  1 167 ? 56.749  72.485  24.221  1.00 18.51 ? 140 ALA E N   1 
ATOM   6696  C  CA  . ALA F  1 167 ? 55.837  71.543  24.867  1.00 18.89 ? 140 ALA E CA  1 
ATOM   6697  C  C   . ALA F  1 167 ? 56.461  70.844  26.075  1.00 19.65 ? 140 ALA E C   1 
ATOM   6698  O  O   . ALA F  1 167 ? 55.776  70.061  26.739  1.00 19.73 ? 140 ALA E O   1 
ATOM   6699  C  CB  . ALA F  1 167 ? 55.346  70.496  23.858  1.00 19.23 ? 140 ALA E CB  1 
ATOM   6700  N  N   . GLY F  1 168 ? 57.737  71.087  26.372  1.00 22.89 ? 141 GLY E N   1 
ATOM   6701  C  CA  . GLY F  1 168 ? 58.262  70.579  27.628  1.00 24.55 ? 141 GLY E CA  1 
ATOM   6702  C  C   . GLY F  1 168 ? 58.601  69.092  27.607  1.00 26.15 ? 141 GLY E C   1 
ATOM   6703  O  O   . GLY F  1 168 ? 58.854  68.483  26.555  1.00 23.31 ? 141 GLY E O   1 
ATOM   6704  N  N   A SER F  1 169 ? 58.570  68.496  28.796  0.43 24.71 ? 142 SER E N   1 
ATOM   6705  N  N   B SER F  1 169 ? 58.610  68.498  28.796  0.57 24.64 ? 142 SER E N   1 
ATOM   6706  C  CA  A SER F  1 169 ? 59.075  67.147  29.007  0.43 24.66 ? 142 SER E CA  1 
ATOM   6707  C  CA  B SER F  1 169 ? 59.145  67.154  28.953  0.57 24.66 ? 142 SER E CA  1 
ATOM   6708  C  C   A SER F  1 169 ? 58.202  66.100  28.323  0.43 21.56 ? 142 SER E C   1 
ATOM   6709  C  C   B SER F  1 169 ? 58.213  66.099  28.354  0.57 21.56 ? 142 SER E C   1 
ATOM   6710  O  O   A SER F  1 169 ? 57.043  66.335  27.975  0.43 21.47 ? 142 SER E O   1 
ATOM   6711  O  O   B SER F  1 169 ? 57.032  66.332  28.083  0.57 21.43 ? 142 SER E O   1 
ATOM   6712  C  CB  A SER F  1 169 ? 59.154  66.839  30.501  0.43 25.38 ? 142 SER E CB  1 
ATOM   6713  C  CB  B SER F  1 169 ? 59.399  66.848  30.431  0.57 25.23 ? 142 SER E CB  1 
ATOM   6714  O  OG  A SER F  1 169 ? 60.061  67.714  31.130  0.43 26.13 ? 142 SER E OG  1 
ATOM   6715  O  OG  B SER F  1 169 ? 58.176  66.730  31.125  0.57 22.89 ? 142 SER E OG  1 
ATOM   6716  N  N   . ARG F  1 170 ? 58.774  64.914  28.156  1.00 21.30 ? 143 ARG E N   1 
ATOM   6717  C  CA  . ARG F  1 170 ? 58.082  63.794  27.531  1.00 19.95 ? 143 ARG E CA  1 
ATOM   6718  C  C   . ARG F  1 170 ? 57.454  62.949  28.636  1.00 23.97 ? 143 ARG E C   1 
ATOM   6719  O  O   . ARG F  1 170 ? 58.166  62.328  29.430  1.00 25.46 ? 143 ARG E O   1 
ATOM   6720  C  CB  . ARG F  1 170 ? 59.080  63.011  26.683  1.00 20.96 ? 143 ARG E CB  1 
ATOM   6721  C  CG  . ARG F  1 170 ? 59.902  63.935  25.788  1.00 22.74 ? 143 ARG E CG  1 
ATOM   6722  C  CD  . ARG F  1 170 ? 60.998  63.250  24.974  1.00 20.34 ? 143 ARG E CD  1 
ATOM   6723  N  NE  . ARG F  1 170 ? 61.695  64.251  24.175  1.00 22.18 ? 143 ARG E NE  1 
ATOM   6724  C  CZ  . ARG F  1 170 ? 62.402  63.994  23.083  1.00 23.85 ? 143 ARG E CZ  1 
ATOM   6725  N  NH1 . ARG F  1 170 ? 62.564  62.759  22.638  1.00 22.03 ? 143 ARG E NH1 1 
ATOM   6726  N  NH2 . ARG F  1 170 ? 62.941  65.004  22.406  1.00 23.38 ? 143 ARG E NH2 1 
ATOM   6727  N  N   . LEU F  1 171 ? 56.120  62.948  28.706  1.00 19.87 ? 144 LEU E N   1 
ATOM   6728  C  CA  . LEU F  1 171 ? 55.428  62.235  29.778  1.00 18.12 ? 144 LEU E CA  1 
ATOM   6729  C  C   . LEU F  1 171 ? 55.300  60.754  29.475  1.00 18.58 ? 144 LEU E C   1 
ATOM   6730  O  O   . LEU F  1 171 ? 55.392  59.919  30.382  1.00 19.48 ? 144 LEU E O   1 
ATOM   6731  C  CB  . LEU F  1 171 ? 54.042  62.836  30.014  1.00 20.29 ? 144 LEU E CB  1 
ATOM   6732  C  CG  . LEU F  1 171 ? 53.988  64.313  30.411  1.00 23.01 ? 144 LEU E CG  1 
ATOM   6733  C  CD1 . LEU F  1 171 ? 52.528  64.729  30.600  1.00 24.32 ? 144 LEU E CD1 1 
ATOM   6734  C  CD2 . LEU F  1 171 ? 54.806  64.583  31.675  1.00 28.18 ? 144 LEU E CD2 1 
ATOM   6735  N  N   . ALA F  1 172 ? 55.110  60.399  28.207  1.00 22.15 ? 145 ALA E N   1 
ATOM   6736  C  CA  . ALA F  1 172 ? 54.956  59.000  27.854  1.00 15.24 ? 145 ALA E CA  1 
ATOM   6737  C  C   . ALA F  1 172 ? 55.169  58.867  26.357  1.00 22.04 ? 145 ALA E C   1 
ATOM   6738  O  O   . ALA F  1 172 ? 55.011  59.831  25.601  1.00 14.75 ? 145 ALA E O   1 
ATOM   6739  C  CB  . ALA F  1 172 ? 53.582  58.457  28.249  1.00 16.74 ? 145 ALA E CB  1 
ATOM   6740  N  N   . CYS F  1 173 ? 55.529  57.662  25.942  1.00 15.61 ? 146 CYS E N   1 
ATOM   6741  C  CA  . CYS F  1 173 ? 55.852  57.450  24.536  1.00 15.52 ? 146 CYS E CA  1 
ATOM   6742  C  C   . CYS F  1 173 ? 55.765  55.969  24.222  1.00 17.25 ? 146 CYS E C   1 
ATOM   6743  O  O   . CYS F  1 173 ? 55.664  55.124  25.114  1.00 16.43 ? 146 CYS E O   1 
ATOM   6744  C  CB  . CYS F  1 173 ? 57.240  57.978  24.199  1.00 20.89 ? 146 CYS E CB  1 
ATOM   6745  S  SG  . CYS F  1 173 ? 58.606  57.196  25.136  1.00 27.59 ? 146 CYS E SG  1 
ATOM   6746  N  N   . GLY F  1 174 ? 55.799  55.667  22.925  1.00 13.42 ? 147 GLY E N   1 
ATOM   6747  C  CA  . GLY F  1 174 ? 55.875  54.286  22.495  1.00 20.49 ? 147 GLY E CA  1 
ATOM   6748  C  C   . GLY F  1 174 ? 56.239  54.241  21.030  1.00 20.51 ? 147 GLY E C   1 
ATOM   6749  O  O   . GLY F  1 174 ? 56.058  55.222  20.296  1.00 15.01 ? 147 GLY E O   1 
ATOM   6750  N  N   . VAL F  1 175 ? 56.761  53.099  20.615  1.00 17.75 ? 148 VAL E N   1 
ATOM   6751  C  CA  . VAL F  1 175 ? 57.073  52.887  19.202  1.00 20.12 ? 148 VAL E CA  1 
ATOM   6752  C  C   . VAL F  1 175 ? 55.796  52.554  18.452  1.00 15.26 ? 148 VAL E C   1 
ATOM   6753  O  O   . VAL F  1 175 ? 54.954  51.782  18.926  1.00 21.62 ? 148 VAL E O   1 
ATOM   6754  C  CB  . VAL F  1 175 ? 58.134  51.776  19.037  1.00 20.81 ? 148 VAL E CB  1 
ATOM   6755  C  CG1 . VAL F  1 175 ? 58.569  51.660  17.587  1.00 19.83 ? 148 VAL E CG1 1 
ATOM   6756  C  CG2 . VAL F  1 175 ? 59.341  52.083  19.919  1.00 18.86 ? 148 VAL E CG2 1 
ATOM   6757  N  N   . ILE F  1 176 ? 55.643  53.148  17.274  1.00 19.59 ? 149 ILE E N   1 
ATOM   6758  C  CA  . ILE F  1 176 ? 54.451  52.942  16.460  1.00 18.48 ? 149 ILE E CA  1 
ATOM   6759  C  C   . ILE F  1 176 ? 54.631  51.650  15.678  1.00 17.78 ? 149 ILE E C   1 
ATOM   6760  O  O   . ILE F  1 176 ? 55.570  51.526  14.889  1.00 21.34 ? 149 ILE E O   1 
ATOM   6761  C  CB  . ILE F  1 176 ? 54.224  54.138  15.525  1.00 20.34 ? 149 ILE E CB  1 
ATOM   6762  C  CG1 . ILE F  1 176 ? 54.007  55.401  16.363  1.00 15.02 ? 149 ILE E CG1 1 
ATOM   6763  C  CG2 . ILE F  1 176 ? 53.044  53.903  14.619  1.00 19.30 ? 149 ILE E CG2 1 
ATOM   6764  C  CD1 . ILE F  1 176 ? 54.199  56.725  15.575  1.00 16.73 ? 149 ILE E CD1 1 
ATOM   6765  N  N   . GLY F  1 177 ? 53.753  50.676  15.916  1.00 19.66 ? 150 GLY E N   1 
ATOM   6766  C  CA  . GLY F  1 177 ? 53.907  49.367  15.298  1.00 22.33 ? 150 GLY E CA  1 
ATOM   6767  C  C   . GLY F  1 177 ? 52.832  49.022  14.282  1.00 23.50 ? 150 GLY E C   1 
ATOM   6768  O  O   . GLY F  1 177 ? 51.728  49.566  14.336  1.00 21.19 ? 150 GLY E O   1 
ATOM   6769  N  N   . ILE F  1 178 ? 53.136  48.112  13.352  1.00 20.99 ? 151 ILE E N   1 
ATOM   6770  C  CA  . ILE F  1 178 ? 52.120  47.612  12.427  1.00 16.80 ? 151 ILE E CA  1 
ATOM   6771  C  C   . ILE F  1 178 ? 51.038  46.868  13.190  1.00 19.91 ? 151 ILE E C   1 
ATOM   6772  O  O   . ILE F  1 178 ? 51.329  46.033  14.054  1.00 25.15 ? 151 ILE E O   1 
ATOM   6773  C  CB  . ILE F  1 178 ? 52.768  46.686  11.382  1.00 24.23 ? 151 ILE E CB  1 
ATOM   6774  C  CG1 . ILE F  1 178 ? 54.022  47.339  10.813  1.00 25.67 ? 151 ILE E CG1 1 
ATOM   6775  C  CG2 . ILE F  1 178 ? 51.747  46.298  10.311  1.00 29.10 ? 151 ILE E CG2 1 
ATOM   6776  C  CD1 . ILE F  1 178 ? 54.474  46.754  9.486   1.00 37.39 ? 151 ILE E CD1 1 
ATOM   6777  N  N   . ALA F  1 179 ? 49.777  47.138  12.862  1.00 20.35 ? 152 ALA E N   1 
ATOM   6778  C  CA  . ALA F  1 179 ? 48.673  46.462  13.532  1.00 22.09 ? 152 ALA E CA  1 
ATOM   6779  C  C   . ALA F  1 179 ? 47.898  45.610  12.538  1.00 27.85 ? 152 ALA E C   1 
ATOM   6780  O  O   . ALA F  1 179 ? 47.965  45.814  11.324  1.00 30.35 ? 152 ALA E O   1 
ATOM   6781  C  CB  . ALA F  1 179 ? 47.712  47.444  14.211  1.00 22.37 ? 152 ALA E CB  1 
ATOM   6782  N  N   . GLN F  1 180 ? 47.147  44.660  13.072  1.00 33.39 ? 153 GLN E N   1 
ATOM   6783  C  CA  . GLN F  1 180 ? 46.365  43.762  12.225  1.00 41.88 ? 153 GLN E CA  1 
ATOM   6784  C  C   . GLN F  1 180 ? 45.128  44.457  11.668  1.00 54.74 ? 153 GLN E C   1 
ATOM   6785  O  O   . GLN F  1 180 ? 44.515  45.291  12.344  1.00 56.24 ? 153 GLN E O   1 
ATOM   6786  C  CB  . GLN F  1 180 ? 45.944  42.511  13.002  1.00 41.31 ? 153 GLN E CB  1 
ATOM   6787  C  CG  . GLN F  1 180 ? 45.164  41.507  12.153  1.00 45.98 ? 153 GLN E CG  1 
ATOM   6788  C  CD  . GLN F  1 180 ? 45.238  40.097  12.710  1.00 57.14 ? 153 GLN E CD  1 
ATOM   6789  O  OE1 . GLN F  1 180 ? 45.084  39.887  13.918  1.00 57.96 ? 153 GLN E OE1 1 
ATOM   6790  N  NE2 . GLN F  1 180 ? 45.477  39.121  11.833  1.00 55.00 ? 153 GLN E NE2 1 
ATOM   6791  O  OXT . GLN F  1 180 ? 44.708  44.192  10.533  1.00 57.87 ? 153 GLN E OXT 1 
ATOM   6792  N  N   . ALA G  1 28  ? 85.528  89.070  -1.008  1.00 46.59 ? 1   ALA F N   1 
ATOM   6793  C  CA  . ALA G  1 28  ? 85.077  88.723  -2.351  1.00 47.42 ? 1   ALA F CA  1 
ATOM   6794  C  C   . ALA G  1 28  ? 84.010  87.637  -2.294  1.00 48.25 ? 1   ALA F C   1 
ATOM   6795  O  O   . ALA G  1 28  ? 84.183  86.620  -1.625  1.00 49.38 ? 1   ALA F O   1 
ATOM   6796  C  CB  . ALA G  1 28  ? 86.243  88.268  -3.209  1.00 46.08 ? 1   ALA F CB  1 
ATOM   6797  N  N   . THR G  1 29  ? 82.913  87.858  -3.018  1.00 43.51 ? 2   THR F N   1 
ATOM   6798  C  CA  . THR G  1 29  ? 81.793  86.893  -3.026  1.00 44.73 ? 2   THR F CA  1 
ATOM   6799  C  C   . THR G  1 29  ? 81.500  86.394  -4.441  1.00 39.93 ? 2   THR F C   1 
ATOM   6800  O  O   . THR G  1 29  ? 80.706  85.503  -4.561  1.00 40.76 ? 2   THR F O   1 
ATOM   6801  C  CB  . THR G  1 29  ? 80.545  87.491  -2.379  1.00 43.14 ? 2   THR F CB  1 
ATOM   6802  O  OG1 . THR G  1 29  ? 80.059  88.509  -3.244  1.00 44.97 ? 2   THR F OG1 1 
ATOM   6803  C  CG2 . THR G  1 29  ? 80.824  88.050  -1.005  1.00 42.69 ? 2   THR F CG2 1 
ATOM   6804  N  N   . LYS G  1 30  ? 82.103  86.991  -5.453  1.00 34.01 ? 3   LYS F N   1 
ATOM   6805  C  CA  . LYS G  1 30  ? 81.884  86.555  -6.848  1.00 35.49 ? 3   LYS F CA  1 
ATOM   6806  C  C   . LYS G  1 30  ? 83.239  86.516  -7.549  1.00 38.74 ? 3   LYS F C   1 
ATOM   6807  O  O   . LYS G  1 30  ? 84.058  87.383  -7.302  1.00 39.59 ? 3   LYS F O   1 
ATOM   6808  C  CB  . LYS G  1 30  ? 81.012  87.551  -7.611  1.00 41.18 ? 3   LYS F CB  1 
ATOM   6809  C  CG  . LYS G  1 30  ? 79.504  87.462  -7.425  1.00 43.29 ? 3   LYS F CG  1 
ATOM   6810  C  CD  . LYS G  1 30  ? 78.790  88.097  -8.600  1.00 54.26 ? 3   LYS F CD  1 
ATOM   6811  C  CE  . LYS G  1 30  ? 77.306  88.337  -8.422  1.00 58.08 ? 3   LYS F CE  1 
ATOM   6812  N  NZ  . LYS G  1 30  ? 76.958  89.778  -8.529  1.00 55.73 ? 3   LYS F NZ  1 
ATOM   6813  N  N   . ALA G  1 31  ? 83.456  85.523  -8.383  1.00 32.59 ? 4   ALA F N   1 
ATOM   6814  C  CA  . ALA G  1 31  ? 84.706  85.460  -9.160  1.00 32.48 ? 4   ALA F CA  1 
ATOM   6815  C  C   . ALA G  1 31  ? 84.383  84.927  -10.551 1.00 31.80 ? 4   ALA F C   1 
ATOM   6816  O  O   . ALA G  1 31  ? 83.304  84.392  -10.744 1.00 30.20 ? 4   ALA F O   1 
ATOM   6817  C  CB  . ALA G  1 31  ? 85.741  84.635  -8.462  1.00 30.62 ? 4   ALA F CB  1 
ATOM   6818  N  N   . VAL G  1 32  ? 85.303  85.098  -11.481 1.00 28.75 ? 5   VAL F N   1 
ATOM   6819  C  CA  . VAL G  1 32  ? 85.047  84.630  -12.865 1.00 27.81 ? 5   VAL F CA  1 
ATOM   6820  C  C   . VAL G  1 32  ? 86.374  84.201  -13.471 1.00 34.19 ? 5   VAL F C   1 
ATOM   6821  O  O   . VAL G  1 32  ? 87.398  84.655  -13.020 1.00 34.89 ? 5   VAL F O   1 
ATOM   6822  C  CB  . VAL G  1 32  ? 84.372  85.729  -13.701 1.00 31.34 ? 5   VAL F CB  1 
ATOM   6823  C  CG1 . VAL G  1 32  ? 85.349  86.826  -14.066 1.00 31.59 ? 5   VAL F CG1 1 
ATOM   6824  C  CG2 . VAL G  1 32  ? 83.687  85.183  -14.937 1.00 29.17 ? 5   VAL F CG2 1 
ATOM   6825  N  N   . CYS G  1 33  ? 86.315  83.345  -14.471 1.00 29.71 ? 6   CYS F N   1 
ATOM   6826  C  CA  . CYS G  1 33  ? 87.536  82.906  -15.118 1.00 28.62 ? 6   CYS F CA  1 
ATOM   6827  C  C   . CYS G  1 33  ? 87.250  82.614  -16.584 1.00 32.06 ? 6   CYS F C   1 
ATOM   6828  O  O   . CYS G  1 33  ? 86.262  81.950  -16.918 1.00 32.36 ? 6   CYS F O   1 
ATOM   6829  C  CB  . CYS G  1 33  ? 88.118  81.682  -14.393 1.00 33.96 ? 6   CYS F CB  1 
ATOM   6830  S  SG  . CYS G  1 33  ? 89.375  80.800  -15.313 1.00 47.27 ? 6   CYS F SG  1 
ATOM   6831  N  N   . VAL G  1 34  ? 88.111  83.127  -17.457 1.00 27.55 ? 7   VAL F N   1 
ATOM   6832  C  CA  . VAL G  1 34  ? 87.976  82.958  -18.902 1.00 26.06 ? 7   VAL F CA  1 
ATOM   6833  C  C   . VAL G  1 34  ? 89.008  81.931  -19.340 1.00 36.57 ? 7   VAL F C   1 
ATOM   6834  O  O   . VAL G  1 34  ? 90.217  82.166  -19.220 1.00 33.02 ? 7   VAL F O   1 
ATOM   6835  C  CB  . VAL G  1 34  ? 88.176  84.284  -19.651 1.00 32.19 ? 7   VAL F CB  1 
ATOM   6836  C  CG1 . VAL G  1 34  ? 88.037  84.065  -21.159 1.00 30.42 ? 7   VAL F CG1 1 
ATOM   6837  C  CG2 . VAL G  1 34  ? 87.191  85.344  -19.157 1.00 34.64 ? 7   VAL F CG2 1 
ATOM   6838  N  N   A LEU G  1 35  ? 88.540  80.791  -19.841 0.63 31.54 ? 8   LEU F N   1 
ATOM   6839  N  N   B LEU G  1 35  ? 88.536  80.799  -19.855 0.37 32.59 ? 8   LEU F N   1 
ATOM   6840  C  CA  A LEU G  1 35  ? 89.424  79.681  -20.175 0.63 31.61 ? 8   LEU F CA  1 
ATOM   6841  C  CA  B LEU G  1 35  ? 89.410  79.685  -20.193 0.37 32.10 ? 8   LEU F CA  1 
ATOM   6842  C  C   A LEU G  1 35  ? 89.837  79.785  -21.635 0.63 32.23 ? 8   LEU F C   1 
ATOM   6843  C  C   B LEU G  1 35  ? 89.838  79.797  -21.647 0.37 33.09 ? 8   LEU F C   1 
ATOM   6844  O  O   A LEU G  1 35  ? 88.984  79.906  -22.521 0.63 33.44 ? 8   LEU F O   1 
ATOM   6845  O  O   B LEU G  1 35  ? 88.995  79.933  -22.541 0.37 33.50 ? 8   LEU F O   1 
ATOM   6846  C  CB  A LEU G  1 35  ? 88.733  78.342  -19.917 0.63 31.91 ? 8   LEU F CB  1 
ATOM   6847  C  CB  B LEU G  1 35  ? 88.712  78.346  -19.952 0.37 29.34 ? 8   LEU F CB  1 
ATOM   6848  C  CG  A LEU G  1 35  ? 88.266  78.032  -18.495 0.63 31.52 ? 8   LEU F CG  1 
ATOM   6849  C  CG  B LEU G  1 35  ? 88.627  77.856  -18.505 0.37 31.32 ? 8   LEU F CG  1 
ATOM   6850  C  CD1 A LEU G  1 35  ? 87.348  76.814  -18.534 0.63 32.42 ? 8   LEU F CD1 1 
ATOM   6851  C  CD1 B LEU G  1 35  ? 87.578  78.638  -17.718 0.37 28.50 ? 8   LEU F CD1 1 
ATOM   6852  C  CD2 A LEU G  1 35  ? 89.439  77.781  -17.546 0.63 25.11 ? 8   LEU F CD2 1 
ATOM   6853  C  CD2 B LEU G  1 35  ? 88.345  76.356  -18.455 0.37 31.04 ? 8   LEU F CD2 1 
ATOM   6854  N  N   . LYS G  1 36  ? 91.148  79.745  -21.878 1.00 36.18 ? 9   LYS F N   1 
ATOM   6855  C  CA  . LYS G  1 36  ? 91.696  79.834  -23.223 1.00 33.33 ? 9   LYS F CA  1 
ATOM   6856  C  C   . LYS G  1 36  ? 92.858  78.861  -23.346 1.00 34.56 ? 9   LYS F C   1 
ATOM   6857  O  O   . LYS G  1 36  ? 93.539  78.561  -22.361 1.00 36.39 ? 9   LYS F O   1 
ATOM   6858  C  CB  . LYS G  1 36  ? 92.171  81.260  -23.545 1.00 35.68 ? 9   LYS F CB  1 
ATOM   6859  C  CG  . LYS G  1 36  ? 91.036  82.259  -23.742 1.00 43.70 ? 9   LYS F CG  1 
ATOM   6860  C  CD  . LYS G  1 36  ? 90.840  82.614  -25.198 1.00 48.25 ? 9   LYS F CD  1 
ATOM   6861  C  CE  . LYS G  1 36  ? 89.365  82.840  -25.505 1.00 52.62 ? 9   LYS F CE  1 
ATOM   6862  N  NZ  . LYS G  1 36  ? 89.078  82.646  -26.953 1.00 53.25 ? 9   LYS F NZ  1 
ATOM   6863  N  N   . GLY G  1 37  ? 93.079  78.373  -24.562 1.00 37.58 ? 10  GLY F N   1 
ATOM   6864  C  CA  . GLY G  1 37  ? 94.238  77.539  -24.824 1.00 41.36 ? 10  GLY F CA  1 
ATOM   6865  C  C   . GLY G  1 37  ? 94.831  77.770  -26.197 1.00 45.73 ? 10  GLY F C   1 
ATOM   6866  O  O   . GLY G  1 37  ? 94.427  78.701  -26.903 1.00 48.20 ? 10  GLY F O   1 
ATOM   6867  N  N   . ASP G  1 38  ? 95.804  76.939  -26.585 1.00 46.98 ? 11  ASP F N   1 
ATOM   6868  C  CA  . ASP G  1 38  ? 96.314  76.978  -27.951 1.00 48.28 ? 11  ASP F CA  1 
ATOM   6869  C  C   . ASP G  1 38  ? 95.461  76.172  -28.913 1.00 52.12 ? 11  ASP F C   1 
ATOM   6870  O  O   . ASP G  1 38  ? 95.680  76.254  -30.127 1.00 57.02 ? 11  ASP F O   1 
ATOM   6871  C  CB  . ASP G  1 38  ? 97.761  76.487  -27.995 1.00 51.93 ? 11  ASP F CB  1 
ATOM   6872  C  CG  . ASP G  1 38  ? 98.659  77.264  -27.049 1.00 67.22 ? 11  ASP F CG  1 
ATOM   6873  O  OD1 . ASP G  1 38  ? 98.829  78.489  -27.277 1.00 66.91 ? 11  ASP F OD1 1 
ATOM   6874  O  OD2 . ASP G  1 38  ? 99.171  76.664  -26.072 1.00 63.43 ? 11  ASP F OD2 1 
ATOM   6875  N  N   . GLY G  1 39  ? 94.500  75.407  -28.398 1.00 48.96 ? 12  GLY F N   1 
ATOM   6876  C  CA  . GLY G  1 39  ? 93.551  74.704  -29.219 1.00 42.94 ? 12  GLY F CA  1 
ATOM   6877  C  C   . GLY G  1 39  ? 92.214  75.410  -29.214 1.00 44.34 ? 12  GLY F C   1 
ATOM   6878  O  O   . GLY G  1 39  ? 92.107  76.579  -28.829 1.00 48.89 ? 12  GLY F O   1 
ATOM   6879  N  N   . PRO G  1 40  ? 91.157  74.703  -29.619 1.00 50.05 ? 13  PRO F N   1 
ATOM   6880  C  CA  . PRO G  1 40  ? 89.834  75.332  -29.729 1.00 41.94 ? 13  PRO F CA  1 
ATOM   6881  C  C   . PRO G  1 40  ? 89.036  75.364  -28.433 1.00 38.93 ? 13  PRO F C   1 
ATOM   6882  O  O   . PRO G  1 40  ? 87.878  75.796  -28.453 1.00 41.71 ? 13  PRO F O   1 
ATOM   6883  C  CB  . PRO G  1 40  ? 89.140  74.451  -30.771 1.00 34.36 ? 13  PRO F CB  1 
ATOM   6884  C  CG  . PRO G  1 40  ? 89.707  73.064  -30.512 1.00 39.95 ? 13  PRO F CG  1 
ATOM   6885  C  CD  . PRO G  1 40  ? 91.125  73.270  -29.980 1.00 45.02 ? 13  PRO F CD  1 
ATOM   6886  N  N   . VAL G  1 41  ? 89.601  74.922  -27.320 1.00 38.79 ? 14  VAL F N   1 
ATOM   6887  C  CA  . VAL G  1 41  ? 88.853  74.849  -26.069 1.00 35.33 ? 14  VAL F CA  1 
ATOM   6888  C  C   . VAL G  1 41  ? 88.762  76.244  -25.461 1.00 41.20 ? 14  VAL F C   1 
ATOM   6889  O  O   . VAL G  1 41  ? 89.778  76.936  -25.310 1.00 35.52 ? 14  VAL F O   1 
ATOM   6890  C  CB  . VAL G  1 41  ? 89.520  73.860  -25.102 1.00 33.26 ? 14  VAL F CB  1 
ATOM   6891  C  CG1 . VAL G  1 41  ? 88.783  73.832  -23.752 1.00 33.63 ? 14  VAL F CG1 1 
ATOM   6892  C  CG2 . VAL G  1 41  ? 89.563  72.467  -25.725 1.00 36.82 ? 14  VAL F CG2 1 
ATOM   6893  N  N   . GLN G  1 42  ? 87.547  76.667  -25.108 1.00 34.36 ? 15  GLN F N   1 
ATOM   6894  C  CA  . GLN G  1 42  ? 87.393  77.960  -24.453 1.00 35.82 ? 15  GLN F CA  1 
ATOM   6895  C  C   . GLN G  1 42  ? 86.098  77.965  -23.658 1.00 39.54 ? 15  GLN F C   1 
ATOM   6896  O  O   . GLN G  1 42  ? 85.147  77.250  -23.991 1.00 33.72 ? 15  GLN F O   1 
ATOM   6897  C  CB  . GLN G  1 42  ? 87.380  79.107  -25.459 1.00 36.40 ? 15  GLN F CB  1 
ATOM   6898  C  CG  . GLN G  1 42  ? 86.452  78.860  -26.613 1.00 42.58 ? 15  GLN F CG  1 
ATOM   6899  C  CD  . GLN G  1 42  ? 86.606  79.892  -27.705 1.00 51.33 ? 15  GLN F CD  1 
ATOM   6900  O  OE1 . GLN G  1 42  ? 87.090  79.588  -28.793 1.00 58.96 ? 15  GLN F OE1 1 
ATOM   6901  N  NE2 . GLN G  1 42  ? 86.242  81.132  -27.405 1.00 57.78 ? 15  GLN F NE2 1 
ATOM   6902  N  N   . GLY G  1 43  ? 86.062  78.792  -22.624 1.00 31.54 ? 16  GLY F N   1 
ATOM   6903  C  CA  . GLY G  1 43  ? 84.882  78.822  -21.778 1.00 33.00 ? 16  GLY F CA  1 
ATOM   6904  C  C   . GLY G  1 43  ? 84.929  79.967  -20.795 1.00 32.88 ? 16  GLY F C   1 
ATOM   6905  O  O   . GLY G  1 43  ? 85.932  80.675  -20.666 1.00 31.87 ? 16  GLY F O   1 
ATOM   6906  N  N   . ILE G  1 44  ? 83.808  80.143  -20.108 1.00 30.22 ? 17  ILE F N   1 
ATOM   6907  C  CA  . ILE G  1 44  ? 83.685  81.081  -19.003 1.00 28.40 ? 17  ILE F CA  1 
ATOM   6908  C  C   . ILE G  1 44  ? 83.095  80.341  -17.815 1.00 33.18 ? 17  ILE F C   1 
ATOM   6909  O  O   . ILE G  1 44  ? 82.032  79.718  -17.925 1.00 29.91 ? 17  ILE F O   1 
ATOM   6910  C  CB  . ILE G  1 44  ? 82.816  82.300  -19.367 1.00 31.46 ? 17  ILE F CB  1 
ATOM   6911  C  CG1 . ILE G  1 44  ? 83.449  83.076  -20.527 1.00 30.97 ? 17  ILE F CG1 1 
ATOM   6912  C  CG2 . ILE G  1 44  ? 82.559  83.168  -18.112 1.00 29.12 ? 17  ILE F CG2 1 
ATOM   6913  C  CD1 . ILE G  1 44  ? 82.478  84.005  -21.227 1.00 38.00 ? 17  ILE F CD1 1 
ATOM   6914  N  N   . ILE G  1 45  ? 83.789  80.400  -16.687 1.00 25.44 ? 18  ILE F N   1 
ATOM   6915  C  CA  . ILE G  1 45  ? 83.341  79.776  -15.451 1.00 29.10 ? 18  ILE F CA  1 
ATOM   6916  C  C   . ILE G  1 45  ? 83.144  80.866  -14.409 1.00 31.90 ? 18  ILE F C   1 
ATOM   6917  O  O   . ILE G  1 45  ? 84.061  81.656  -14.154 1.00 31.68 ? 18  ILE F O   1 
ATOM   6918  C  CB  . ILE G  1 45  ? 84.351  78.720  -14.967 1.00 24.03 ? 18  ILE F CB  1 
ATOM   6919  C  CG1 . ILE G  1 45  ? 84.551  77.637  -16.033 1.00 29.78 ? 18  ILE F CG1 1 
ATOM   6920  C  CG2 . ILE G  1 45  ? 83.931  78.145  -13.640 1.00 22.62 ? 18  ILE F CG2 1 
ATOM   6921  C  CD1 . ILE G  1 45  ? 83.302  76.813  -16.323 1.00 32.48 ? 18  ILE F CD1 1 
ATOM   6922  N  N   . ASN G  1 46  ? 81.949  80.915  -13.817 1.00 27.77 ? 19  ASN F N   1 
ATOM   6923  C  CA  . ASN G  1 46  ? 81.634  81.841  -12.735 1.00 28.72 ? 19  ASN F CA  1 
ATOM   6924  C  C   . ASN G  1 46  ? 81.700  81.149  -11.386 1.00 30.55 ? 19  ASN F C   1 
ATOM   6925  O  O   . ASN G  1 46  ? 81.457  79.944  -11.277 1.00 33.17 ? 19  ASN F O   1 
ATOM   6926  C  CB  . ASN G  1 46  ? 80.243  82.445  -12.914 1.00 30.77 ? 19  ASN F CB  1 
ATOM   6927  C  CG  . ASN G  1 46  ? 80.004  82.951  -14.306 1.00 36.10 ? 19  ASN F CG  1 
ATOM   6928  O  OD1 . ASN G  1 46  ? 80.294  84.112  -14.592 1.00 40.82 ? 19  ASN F OD1 1 
ATOM   6929  N  ND2 . ASN G  1 46  ? 79.440  82.104  -15.180 1.00 35.15 ? 19  ASN F ND2 1 
ATOM   6930  N  N   . PHE G  1 47  ? 82.024  81.929  -10.351 1.00 27.95 ? 20  PHE F N   1 
ATOM   6931  C  CA  . PHE G  1 47  ? 82.073  81.450  -8.977  1.00 30.36 ? 20  PHE F CA  1 
ATOM   6932  C  C   . PHE G  1 47  ? 81.267  82.396  -8.101  1.00 37.31 ? 20  PHE F C   1 
ATOM   6933  O  O   . PHE G  1 47  ? 81.341  83.617  -8.269  1.00 33.79 ? 20  PHE F O   1 
ATOM   6934  C  CB  . PHE G  1 47  ? 83.499  81.389  -8.397  1.00 34.51 ? 20  PHE F CB  1 
ATOM   6935  C  CG  . PHE G  1 47  ? 84.474  80.612  -9.223  1.00 31.06 ? 20  PHE F CG  1 
ATOM   6936  C  CD1 . PHE G  1 47  ? 84.998  81.149  -10.390 1.00 33.73 ? 20  PHE F CD1 1 
ATOM   6937  C  CD2 . PHE G  1 47  ? 84.903  79.363  -8.811  1.00 32.83 ? 20  PHE F CD2 1 
ATOM   6938  C  CE1 . PHE G  1 47  ? 85.901  80.447  -11.138 1.00 32.73 ? 20  PHE F CE1 1 
ATOM   6939  C  CE2 . PHE G  1 47  ? 85.816  78.655  -9.558  1.00 29.87 ? 20  PHE F CE2 1 
ATOM   6940  C  CZ  . PHE G  1 47  ? 86.313  79.199  -10.726 1.00 30.82 ? 20  PHE F CZ  1 
ATOM   6941  N  N   . GLU G  1 48  ? 80.532  81.840  -7.140  1.00 32.47 ? 21  GLU F N   1 
ATOM   6942  C  CA  . GLU G  1 48  ? 79.738  82.663  -6.237  1.00 31.42 ? 21  GLU F CA  1 
ATOM   6943  C  C   . GLU G  1 48  ? 79.742  82.040  -4.853  1.00 39.45 ? 21  GLU F C   1 
ATOM   6944  O  O   . GLU G  1 48  ? 79.552  80.827  -4.713  1.00 38.47 ? 21  GLU F O   1 
ATOM   6945  C  CB  . GLU G  1 48  ? 78.310  82.832  -6.759  1.00 35.03 ? 21  GLU F CB  1 
ATOM   6946  C  CG  . GLU G  1 48  ? 77.400  83.645  -5.853  1.00 45.34 ? 21  GLU F CG  1 
ATOM   6947  C  CD  . GLU G  1 48  ? 76.305  84.364  -6.620  1.00 59.14 ? 21  GLU F CD  1 
ATOM   6948  O  OE1 . GLU G  1 48  ? 76.575  84.846  -7.745  1.00 65.83 ? 21  GLU F OE1 1 
ATOM   6949  O  OE2 . GLU G  1 48  ? 75.164  84.414  -6.113  1.00 69.71 ? 21  GLU F OE2 1 
ATOM   6950  N  N   . GLN G  1 49  ? 79.980  82.875  -3.844  1.00 35.90 ? 22  GLN F N   1 
ATOM   6951  C  CA  . GLN G  1 49  ? 80.031  82.424  -2.431  1.00 36.93 ? 22  GLN F CA  1 
ATOM   6952  C  C   . GLN G  1 49  ? 79.422  83.498  -1.529  1.00 44.21 ? 22  GLN F C   1 
ATOM   6953  O  O   . GLN G  1 49  ? 80.122  84.427  -1.190  1.00 48.47 ? 22  GLN F O   1 
ATOM   6954  C  CB  . GLN G  1 49  ? 81.467  82.126  -2.014  1.00 36.98 ? 22  GLN F CB  1 
ATOM   6955  C  CG  . GLN G  1 49  ? 81.580  81.668  -0.577  1.00 39.55 ? 22  GLN F CG  1 
ATOM   6956  C  CD  . GLN G  1 49  ? 82.983  81.317  -0.166  1.00 43.66 ? 22  GLN F CD  1 
ATOM   6957  O  OE1 . GLN G  1 49  ? 83.944  81.943  -0.573  1.00 46.64 ? 22  GLN F OE1 1 
ATOM   6958  N  NE2 . GLN G  1 49  ? 83.112  80.293  0.648   1.00 47.51 ? 22  GLN F NE2 1 
ATOM   6959  N  N   . LYS G  1 50  ? 78.159  83.334  -1.160  1.00 46.78 ? 23  LYS F N   1 
ATOM   6960  C  CA  . LYS G  1 50  ? 77.429  84.305  -0.309  1.00 49.90 ? 23  LYS F CA  1 
ATOM   6961  C  C   . LYS G  1 50  ? 78.062  84.400  1.080   1.00 51.29 ? 23  LYS F C   1 
ATOM   6962  O  O   . LYS G  1 50  ? 78.302  85.516  1.528   1.00 53.20 ? 23  LYS F O   1 
ATOM   6963  C  CB  . LYS G  1 50  ? 75.984  83.841  -0.124  1.00 48.11 ? 23  LYS F CB  1 
ATOM   6964  C  CG  . LYS G  1 50  ? 75.160  83.748  -1.394  1.00 41.90 ? 23  LYS F CG  1 
ATOM   6965  C  CD  . LYS G  1 50  ? 75.205  85.009  -2.198  1.00 53.54 ? 23  LYS F CD  1 
ATOM   6966  C  CE  . LYS G  1 50  ? 74.057  85.110  -3.174  1.00 54.17 ? 23  LYS F CE  1 
ATOM   6967  N  NZ  . LYS G  1 50  ? 73.843  86.505  -3.617  1.00 62.13 ? 23  LYS F NZ  1 
ATOM   6968  N  N   . GLU G  1 51  ? 78.332  83.261  1.718   1.00 51.05 ? 24  GLU F N   1 
ATOM   6969  C  CA  . GLU G  1 51  ? 78.866  83.237  3.105   1.00 47.50 ? 24  GLU F CA  1 
ATOM   6970  C  C   . GLU G  1 51  ? 80.310  82.749  3.112   1.00 50.51 ? 24  GLU F C   1 
ATOM   6971  O  O   . GLU G  1 51  ? 80.569  81.727  2.500   1.00 50.37 ? 24  GLU F O   1 
ATOM   6972  C  CB  . GLU G  1 51  ? 78.015  82.313  3.976   1.00 51.88 ? 24  GLU F CB  1 
ATOM   6973  C  CG  . GLU G  1 51  ? 76.528  82.589  3.896   1.00 51.42 ? 24  GLU F CG  1 
ATOM   6974  C  CD  . GLU G  1 51  ? 76.080  83.928  4.457   1.00 62.51 ? 24  GLU F CD  1 
ATOM   6975  O  OE1 . GLU G  1 51  ? 76.929  84.660  4.978   1.00 65.43 ? 24  GLU F OE1 1 
ATOM   6976  O  OE2 . GLU G  1 51  ? 74.886  84.227  4.375   1.00 64.00 ? 24  GLU F OE2 1 
ATOM   6977  N  N   . SER G  1 52  ? 81.181  83.430  3.855   1.00 47.41 ? 25  SER F N   1 
ATOM   6978  C  CA  . SER G  1 52  ? 82.601  83.082  3.900   1.00 47.54 ? 25  SER F CA  1 
ATOM   6979  C  C   . SER G  1 52  ? 82.805  81.622  4.277   1.00 49.90 ? 25  SER F C   1 
ATOM   6980  O  O   . SER G  1 52  ? 83.721  80.959  3.775   1.00 51.46 ? 25  SER F O   1 
ATOM   6981  C  CB  . SER G  1 52  ? 83.334  83.982  4.900   1.00 45.88 ? 25  SER F CB  1 
ATOM   6982  O  OG  . SER G  1 52  ? 82.796  85.295  4.911   1.00 60.29 ? 25  SER F OG  1 
ATOM   6983  N  N   . ASN G  1 53  ? 81.964  81.111  5.175   1.00 53.67 ? 26  ASN F N   1 
ATOM   6984  C  CA  . ASN G  1 53  ? 82.010  79.712  5.571   1.00 55.57 ? 26  ASN F CA  1 
ATOM   6985  C  C   . ASN G  1 53  ? 81.383  78.798  4.530   1.00 54.61 ? 26  ASN F C   1 
ATOM   6986  O  O   . ASN G  1 53  ? 81.646  77.590  4.542   1.00 62.64 ? 26  ASN F O   1 
ATOM   6987  C  CB  . ASN G  1 53  ? 81.262  79.518  6.893   1.00 59.27 ? 26  ASN F CB  1 
ATOM   6988  C  CG  . ASN G  1 53  ? 81.367  80.723  7.806   1.00 64.96 ? 26  ASN F CG  1 
ATOM   6989  O  OD1 . ASN G  1 53  ? 80.365  81.390  8.088   1.00 68.14 ? 26  ASN F OD1 1 
ATOM   6990  N  ND2 . ASN G  1 53  ? 82.579  81.006  8.281   1.00 63.07 ? 26  ASN F ND2 1 
ATOM   6991  N  N   . GLY G  1 54  ? 80.556  79.349  3.643   1.00 56.60 ? 27  GLY F N   1 
ATOM   6992  C  CA  . GLY G  1 54  ? 79.642  78.566  2.847   1.00 50.43 ? 27  GLY F CA  1 
ATOM   6993  C  C   . GLY G  1 54  ? 80.259  77.952  1.609   1.00 43.19 ? 27  GLY F C   1 
ATOM   6994  O  O   . GLY G  1 54  ? 81.404  78.234  1.233   1.00 44.88 ? 27  GLY F O   1 
ATOM   6995  N  N   . PRO G  1 55  ? 79.498  77.072  0.961   1.00 48.95 ? 28  PRO F N   1 
ATOM   6996  C  CA  . PRO G  1 55  ? 79.968  76.460  -0.284  1.00 47.20 ? 28  PRO F CA  1 
ATOM   6997  C  C   . PRO G  1 55  ? 80.108  77.484  -1.403  1.00 38.70 ? 28  PRO F C   1 
ATOM   6998  O  O   . PRO G  1 55  ? 79.546  78.584  -1.364  1.00 42.65 ? 28  PRO F O   1 
ATOM   6999  C  CB  . PRO G  1 55  ? 78.878  75.431  -0.611  1.00 47.35 ? 28  PRO F CB  1 
ATOM   7000  C  CG  . PRO G  1 55  ? 77.684  75.860  0.179   1.00 45.05 ? 28  PRO F CG  1 
ATOM   7001  C  CD  . PRO G  1 55  ? 78.214  76.511  1.410   1.00 40.63 ? 28  PRO F CD  1 
ATOM   7002  N  N   . VAL G  1 56  ? 80.867  77.096  -2.422  1.00 38.84 ? 29  VAL F N   1 
ATOM   7003  C  CA  . VAL G  1 56  ? 81.093  77.922  -3.599  1.00 30.85 ? 29  VAL F CA  1 
ATOM   7004  C  C   . VAL G  1 56  ? 80.333  77.299  -4.759  1.00 35.53 ? 29  VAL F C   1 
ATOM   7005  O  O   . VAL G  1 56  ? 80.565  76.134  -5.104  1.00 35.96 ? 29  VAL F O   1 
ATOM   7006  C  CB  . VAL G  1 56  ? 82.589  78.041  -3.928  1.00 32.75 ? 29  VAL F CB  1 
ATOM   7007  C  CG1 . VAL G  1 56  ? 82.792  78.809  -5.249  1.00 31.60 ? 29  VAL F CG1 1 
ATOM   7008  C  CG2 . VAL G  1 56  ? 83.321  78.724  -2.791  1.00 38.33 ? 29  VAL F CG2 1 
ATOM   7009  N  N   . LYS G  1 57  ? 79.435  78.075  -5.364  1.00 33.11 ? 30  LYS F N   1 
ATOM   7010  C  CA  . LYS G  1 57  ? 78.757  77.647  -6.579  1.00 34.95 ? 30  LYS F CA  1 
ATOM   7011  C  C   . LYS G  1 57  ? 79.663  77.930  -7.771  1.00 36.33 ? 30  LYS F C   1 
ATOM   7012  O  O   . LYS G  1 57  ? 80.227  79.023  -7.883  1.00 32.61 ? 30  LYS F O   1 
ATOM   7013  C  CB  . LYS G  1 57  ? 77.418  78.378  -6.722  1.00 35.15 ? 30  LYS F CB  1 
ATOM   7014  C  CG  . LYS G  1 57  ? 76.581  77.942  -7.925  1.00 42.24 ? 30  LYS F CG  1 
ATOM   7015  C  CD  . LYS G  1 57  ? 75.202  78.617  -7.922  1.00 45.95 ? 30  LYS F CD  1 
ATOM   7016  C  CE  . LYS G  1 57  ? 74.610  78.730  -9.333  1.00 44.98 ? 30  LYS F CE  1 
ATOM   7017  N  NZ  . LYS G  1 57  ? 73.590  79.832  -9.414  1.00 51.75 ? 30  LYS F NZ  1 
ATOM   7018  N  N   . VAL G  1 58  ? 79.829  76.939  -8.646  1.00 33.30 ? 31  VAL F N   1 
ATOM   7019  C  CA  . VAL G  1 58  ? 80.702  77.042  -9.811  1.00 30.03 ? 31  VAL F CA  1 
ATOM   7020  C  C   . VAL G  1 58  ? 79.883  76.660  -11.033 1.00 33.95 ? 31  VAL F C   1 
ATOM   7021  O  O   . VAL G  1 58  ? 79.357  75.540  -11.101 1.00 32.15 ? 31  VAL F O   1 
ATOM   7022  C  CB  . VAL G  1 58  ? 81.931  76.126  -9.688  1.00 27.83 ? 31  VAL F CB  1 
ATOM   7023  C  CG1 . VAL G  1 58  ? 82.888  76.371  -10.831 1.00 30.05 ? 31  VAL F CG1 1 
ATOM   7024  C  CG2 . VAL G  1 58  ? 82.613  76.305  -8.319  1.00 30.55 ? 31  VAL F CG2 1 
ATOM   7025  N  N   . TRP G  1 59  ? 79.772  77.575  -11.997 1.00 30.02 ? 32  TRP F N   1 
ATOM   7026  C  CA  . TRP G  1 59  ? 78.930  77.289  -13.147 1.00 29.81 ? 32  TRP F CA  1 
ATOM   7027  C  C   . TRP G  1 59  ? 79.411  78.032  -14.380 1.00 28.86 ? 32  TRP F C   1 
ATOM   7028  O  O   . TRP G  1 59  ? 80.006  79.109  -14.293 1.00 29.47 ? 32  TRP F O   1 
ATOM   7029  C  CB  . TRP G  1 59  ? 77.453  77.643  -12.878 1.00 31.32 ? 32  TRP F CB  1 
ATOM   7030  C  CG  . TRP G  1 59  ? 77.130  79.119  -12.903 1.00 30.22 ? 32  TRP F CG  1 
ATOM   7031  C  CD1 . TRP G  1 59  ? 76.544  79.824  -13.921 1.00 33.28 ? 32  TRP F CD1 1 
ATOM   7032  C  CD2 . TRP G  1 59  ? 77.358  80.058  -11.844 1.00 30.09 ? 32  TRP F CD2 1 
ATOM   7033  N  NE1 . TRP G  1 59  ? 76.401  81.144  -13.558 1.00 34.48 ? 32  TRP F NE1 1 
ATOM   7034  C  CE2 . TRP G  1 59  ? 76.895  81.311  -12.288 1.00 31.93 ? 32  TRP F CE2 1 
ATOM   7035  C  CE3 . TRP G  1 59  ? 77.918  79.960  -10.566 1.00 36.00 ? 32  TRP F CE3 1 
ATOM   7036  C  CZ2 . TRP G  1 59  ? 76.962  82.454  -11.497 1.00 35.75 ? 32  TRP F CZ2 1 
ATOM   7037  C  CZ3 . TRP G  1 59  ? 77.995  81.101  -9.783  1.00 42.89 ? 32  TRP F CZ3 1 
ATOM   7038  C  CH2 . TRP G  1 59  ? 77.522  82.333  -10.254 1.00 40.34 ? 32  TRP F CH2 1 
ATOM   7039  N  N   . GLY G  1 60  ? 79.112  77.455  -15.528 1.00 28.32 ? 33  GLY F N   1 
ATOM   7040  C  CA  . GLY G  1 60  ? 79.458  78.076  -16.788 1.00 27.65 ? 33  GLY F CA  1 
ATOM   7041  C  C   . GLY G  1 60  ? 79.422  77.047  -17.898 1.00 32.11 ? 33  GLY F C   1 
ATOM   7042  O  O   . GLY G  1 60  ? 78.710  76.044  -17.813 1.00 28.89 ? 33  GLY F O   1 
ATOM   7043  N  N   . SER G  1 61  ? 80.219  77.305  -18.924 1.00 29.62 ? 34  SER F N   1 
ATOM   7044  C  CA  . SER G  1 61  ? 80.189  76.445  -20.090 1.00 27.69 ? 34  SER F CA  1 
ATOM   7045  C  C   . SER G  1 61  ? 81.553  76.491  -20.758 1.00 31.41 ? 34  SER F C   1 
ATOM   7046  O  O   . SER G  1 61  ? 82.207  77.535  -20.779 1.00 30.56 ? 34  SER F O   1 
ATOM   7047  C  CB  . SER G  1 61  ? 79.077  76.875  -21.050 1.00 33.25 ? 34  SER F CB  1 
ATOM   7048  O  OG  . SER G  1 61  ? 79.101  76.091  -22.228 1.00 42.76 ? 34  SER F OG  1 
ATOM   7049  N  N   . ILE G  1 62  ? 81.992  75.333  -21.241 1.00 30.13 ? 35  ILE F N   1 
ATOM   7050  C  CA  . ILE G  1 62  ? 83.245  75.162  -21.960 1.00 26.51 ? 35  ILE F CA  1 
ATOM   7051  C  C   . ILE G  1 62  ? 82.908  74.492  -23.279 1.00 33.74 ? 35  ILE F C   1 
ATOM   7052  O  O   . ILE G  1 62  ? 82.149  73.514  -23.301 1.00 30.69 ? 35  ILE F O   1 
ATOM   7053  C  CB  . ILE G  1 62  ? 84.252  74.310  -21.165 1.00 28.37 ? 35  ILE F CB  1 
ATOM   7054  C  CG1 . ILE G  1 62  ? 84.429  74.860  -19.745 1.00 28.19 ? 35  ILE F CG1 1 
ATOM   7055  C  CG2 . ILE G  1 62  ? 85.595  74.211  -21.915 1.00 32.88 ? 35  ILE F CG2 1 
ATOM   7056  C  CD1 . ILE G  1 62  ? 85.222  73.938  -18.856 1.00 32.11 ? 35  ILE F CD1 1 
ATOM   7057  N  N   . LYS G  1 63  ? 83.446  75.021  -24.374 1.00 28.81 ? 36  LYS F N   1 
ATOM   7058  C  CA  . LYS G  1 63  ? 83.190  74.464  -25.692 1.00 27.56 ? 36  LYS F CA  1 
ATOM   7059  C  C   . LYS G  1 63  ? 84.512  74.050  -26.332 1.00 33.07 ? 36  LYS F C   1 
ATOM   7060  O  O   . LYS G  1 63  ? 85.594  74.399  -25.856 1.00 31.11 ? 36  LYS F O   1 
ATOM   7061  C  CB  . LYS G  1 63  ? 82.449  75.461  -26.593 1.00 36.44 ? 36  LYS F CB  1 
ATOM   7062  C  CG  . LYS G  1 63  ? 83.326  76.581  -27.143 1.00 40.64 ? 36  LYS F CG  1 
ATOM   7063  C  CD  . LYS G  1 63  ? 82.480  77.702  -27.749 1.00 47.10 ? 36  LYS F CD  1 
ATOM   7064  C  CE  . LYS G  1 63  ? 83.217  78.386  -28.895 1.00 46.42 ? 36  LYS F CE  1 
ATOM   7065  N  NZ  . LYS G  1 63  ? 82.304  79.198  -29.751 1.00 52.12 ? 36  LYS F NZ  1 
ATOM   7066  N  N   . GLY G  1 64  ? 84.412  73.285  -27.419 1.00 31.86 ? 37  GLY F N   1 
ATOM   7067  C  CA  . GLY G  1 64  ? 85.577  72.829  -28.155 1.00 36.34 ? 37  GLY F CA  1 
ATOM   7068  C  C   . GLY G  1 64  ? 86.227  71.564  -27.632 1.00 41.42 ? 37  GLY F C   1 
ATOM   7069  O  O   . GLY G  1 64  ? 87.283  71.166  -28.154 1.00 36.59 ? 37  GLY F O   1 
ATOM   7070  N  N   . LEU G  1 65  ? 85.630  70.910  -26.637 1.00 29.79 ? 38  LEU F N   1 
ATOM   7071  C  CA  . LEU G  1 65  ? 86.198  69.713  -26.031 1.00 28.80 ? 38  LEU F CA  1 
ATOM   7072  C  C   . LEU G  1 65  ? 85.816  68.474  -26.818 1.00 30.84 ? 38  LEU F C   1 
ATOM   7073  O  O   . LEU G  1 65  ? 84.771  68.435  -27.465 1.00 33.24 ? 38  LEU F O   1 
ATOM   7074  C  CB  . LEU G  1 65  ? 85.698  69.545  -24.600 1.00 29.69 ? 38  LEU F CB  1 
ATOM   7075  C  CG  . LEU G  1 65  ? 86.011  70.671  -23.624 1.00 32.49 ? 38  LEU F CG  1 
ATOM   7076  C  CD1 . LEU G  1 65  ? 85.001  70.629  -22.484 1.00 27.68 ? 38  LEU F CD1 1 
ATOM   7077  C  CD2 . LEU G  1 65  ? 87.438  70.516  -23.098 1.00 33.11 ? 38  LEU F CD2 1 
ATOM   7078  N  N   . THR G  1 66  ? 86.651  67.442  -26.728 1.00 30.22 ? 39  THR F N   1 
ATOM   7079  C  CA  . THR G  1 66  ? 86.216  66.126  -27.176 1.00 37.93 ? 39  THR F CA  1 
ATOM   7080  C  C   . THR G  1 66  ? 85.120  65.620  -26.246 1.00 30.76 ? 39  THR F C   1 
ATOM   7081  O  O   . THR G  1 66  ? 85.126  65.896  -25.038 1.00 28.39 ? 39  THR F O   1 
ATOM   7082  C  CB  . THR G  1 66  ? 87.378  65.128  -27.196 1.00 35.74 ? 39  THR F CB  1 
ATOM   7083  O  OG1 . THR G  1 66  ? 88.046  65.146  -25.929 1.00 35.10 ? 39  THR F OG1 1 
ATOM   7084  C  CG2 . THR G  1 66  ? 88.371  65.467  -28.317 1.00 36.54 ? 39  THR F CG2 1 
ATOM   7085  N  N   . GLU G  1 67  ? 84.164  64.886  -26.815 1.00 33.15 ? 40  GLU F N   1 
ATOM   7086  C  CA  . GLU G  1 67  ? 83.057  64.396  -26.003 1.00 33.64 ? 40  GLU F CA  1 
ATOM   7087  C  C   . GLU G  1 67  ? 83.564  63.494  -24.883 1.00 34.42 ? 40  GLU F C   1 
ATOM   7088  O  O   . GLU G  1 67  ? 84.522  62.734  -25.050 1.00 33.83 ? 40  GLU F O   1 
ATOM   7089  C  CB  . GLU G  1 67  ? 82.046  63.642  -26.862 1.00 37.31 ? 40  GLU F CB  1 
ATOM   7090  C  CG  . GLU G  1 67  ? 82.561  62.339  -27.432 1.00 36.04 ? 40  GLU F CG  1 
ATOM   7091  C  CD  . GLU G  1 67  ? 81.504  61.596  -28.238 1.00 46.87 ? 40  GLU F CD  1 
ATOM   7092  O  OE1 . GLU G  1 67  ? 80.605  62.247  -28.815 1.00 52.03 ? 40  GLU F OE1 1 
ATOM   7093  O  OE2 . GLU G  1 67  ? 81.565  60.349  -28.273 1.00 53.83 ? 40  GLU F OE2 1 
ATOM   7094  N  N   . GLY G  1 68  ? 82.923  63.591  -23.728 1.00 28.53 ? 41  GLY F N   1 
ATOM   7095  C  CA  . GLY G  1 68  ? 83.266  62.768  -22.590 1.00 23.54 ? 41  GLY F CA  1 
ATOM   7096  C  C   . GLY G  1 68  ? 83.772  63.572  -21.408 1.00 26.81 ? 41  GLY F C   1 
ATOM   7097  O  O   . GLY G  1 68  ? 83.578  64.785  -21.309 1.00 29.57 ? 41  GLY F O   1 
ATOM   7098  N  N   . LEU G  1 69  ? 84.457  62.870  -20.505 1.00 28.88 ? 42  LEU F N   1 
ATOM   7099  C  CA  . LEU G  1 69  ? 84.851  63.417  -19.213 1.00 27.76 ? 42  LEU F CA  1 
ATOM   7100  C  C   . LEU G  1 69  ? 86.179  64.158  -19.338 1.00 34.07 ? 42  LEU F C   1 
ATOM   7101  O  O   . LEU G  1 69  ? 87.056  63.756  -20.110 1.00 32.60 ? 42  LEU F O   1 
ATOM   7102  C  CB  . LEU G  1 69  ? 84.965  62.303  -18.163 1.00 31.58 ? 42  LEU F CB  1 
ATOM   7103  C  CG  . LEU G  1 69  ? 83.698  61.760  -17.477 1.00 29.19 ? 42  LEU F CG  1 
ATOM   7104  C  CD1 . LEU G  1 69  ? 82.761  61.142  -18.497 1.00 28.50 ? 42  LEU F CD1 1 
ATOM   7105  C  CD2 . LEU G  1 69  ? 84.027  60.736  -16.378 1.00 26.90 ? 42  LEU F CD2 1 
ATOM   7106  N  N   . HIS G  1 70  ? 86.325  65.235  -18.567 1.00 30.01 ? 43  HIS F N   1 
ATOM   7107  C  CA  . HIS G  1 70  ? 87.551  66.025  -18.599 1.00 30.42 ? 43  HIS F CA  1 
ATOM   7108  C  C   . HIS G  1 70  ? 87.869  66.497  -17.191 1.00 31.35 ? 43  HIS F C   1 
ATOM   7109  O  O   . HIS G  1 70  ? 87.011  67.091  -16.534 1.00 30.43 ? 43  HIS F O   1 
ATOM   7110  C  CB  . HIS G  1 70  ? 87.418  67.222  -19.548 1.00 30.38 ? 43  HIS F CB  1 
ATOM   7111  C  CG  . HIS G  1 70  ? 87.306  66.846  -20.997 1.00 27.66 ? 43  HIS F CG  1 
ATOM   7112  N  ND1 . HIS G  1 70  ? 88.403  66.708  -21.823 1.00 34.83 ? 43  HIS F ND1 1 
ATOM   7113  C  CD2 . HIS G  1 70  ? 86.223  66.593  -21.771 1.00 28.42 ? 43  HIS F CD2 1 
ATOM   7114  C  CE1 . HIS G  1 70  ? 88.001  66.390  -23.042 1.00 34.09 ? 43  HIS F CE1 1 
ATOM   7115  N  NE2 . HIS G  1 70  ? 86.682  66.312  -23.038 1.00 32.95 ? 43  HIS F NE2 1 
ATOM   7116  N  N   . GLY G  1 71  ? 89.092  66.223  -16.728 1.00 30.96 ? 44  GLY F N   1 
ATOM   7117  C  CA  . GLY G  1 71  ? 89.503  66.709  -15.425 1.00 29.31 ? 44  GLY F CA  1 
ATOM   7118  C  C   . GLY G  1 71  ? 89.388  68.220  -15.331 1.00 30.59 ? 44  GLY F C   1 
ATOM   7119  O  O   . GLY G  1 71  ? 89.589  68.942  -16.305 1.00 32.04 ? 44  GLY F O   1 
ATOM   7120  N  N   . PHE G  1 72  ? 89.066  68.689  -14.127 1.00 30.46 ? 45  PHE F N   1 
ATOM   7121  C  CA  . PHE G  1 72  ? 88.673  70.073  -13.869 1.00 32.81 ? 45  PHE F CA  1 
ATOM   7122  C  C   . PHE G  1 72  ? 89.282  70.464  -12.534 1.00 34.35 ? 45  PHE F C   1 
ATOM   7123  O  O   . PHE G  1 72  ? 88.792  70.029  -11.484 1.00 36.46 ? 45  PHE F O   1 
ATOM   7124  C  CB  . PHE G  1 72  ? 87.150  70.188  -13.833 1.00 28.41 ? 45  PHE F CB  1 
ATOM   7125  C  CG  . PHE G  1 72  ? 86.625  71.591  -13.966 1.00 28.67 ? 45  PHE F CG  1 
ATOM   7126  C  CD1 . PHE G  1 72  ? 86.955  72.371  -15.061 1.00 29.21 ? 45  PHE F CD1 1 
ATOM   7127  C  CD2 . PHE G  1 72  ? 85.759  72.106  -13.015 1.00 31.01 ? 45  PHE F CD2 1 
ATOM   7128  C  CE1 . PHE G  1 72  ? 86.441  73.654  -15.196 1.00 32.51 ? 45  PHE F CE1 1 
ATOM   7129  C  CE2 . PHE G  1 72  ? 85.244  73.386  -13.138 1.00 30.08 ? 45  PHE F CE2 1 
ATOM   7130  C  CZ  . PHE G  1 72  ? 85.590  74.161  -14.233 1.00 27.98 ? 45  PHE F CZ  1 
ATOM   7131  N  N   . HIS G  1 73  ? 90.348  71.271  -12.558 1.00 35.83 ? 46  HIS F N   1 
ATOM   7132  C  CA  . HIS G  1 73  ? 91.127  71.499  -11.348 1.00 35.98 ? 46  HIS F CA  1 
ATOM   7133  C  C   . HIS G  1 73  ? 91.584  72.945  -11.226 1.00 37.32 ? 46  HIS F C   1 
ATOM   7134  O  O   . HIS G  1 73  ? 91.910  73.602  -12.217 1.00 36.63 ? 46  HIS F O   1 
ATOM   7135  C  CB  . HIS G  1 73  ? 92.363  70.594  -11.291 1.00 43.04 ? 46  HIS F CB  1 
ATOM   7136  C  CG  . HIS G  1 73  ? 92.059  69.147  -11.506 1.00 39.18 ? 46  HIS F CG  1 
ATOM   7137  N  ND1 . HIS G  1 73  ? 92.476  68.457  -12.622 1.00 40.30 ? 46  HIS F ND1 1 
ATOM   7138  C  CD2 . HIS G  1 73  ? 91.359  68.264  -10.754 1.00 37.44 ? 46  HIS F CD2 1 
ATOM   7139  C  CE1 . HIS G  1 73  ? 92.057  67.207  -12.544 1.00 40.97 ? 46  HIS F CE1 1 
ATOM   7140  N  NE2 . HIS G  1 73  ? 91.372  67.065  -11.423 1.00 47.25 ? 46  HIS F NE2 1 
ATOM   7141  N  N   . VAL G  1 74  ? 91.636  73.410  -9.982  1.00 37.48 ? 47  VAL F N   1 
ATOM   7142  C  CA  . VAL G  1 74  ? 92.281  74.671  -9.641  1.00 41.59 ? 47  VAL F CA  1 
ATOM   7143  C  C   . VAL G  1 74  ? 93.741  74.376  -9.327  1.00 38.73 ? 47  VAL F C   1 
ATOM   7144  O  O   . VAL G  1 74  ? 94.040  73.637  -8.382  1.00 39.53 ? 47  VAL F O   1 
ATOM   7145  C  CB  . VAL G  1 74  ? 91.596  75.344  -8.446  1.00 36.39 ? 47  VAL F CB  1 
ATOM   7146  C  CG1 . VAL G  1 74  ? 92.386  76.598  -8.021  1.00 32.95 ? 47  VAL F CG1 1 
ATOM   7147  C  CG2 . VAL G  1 74  ? 90.145  75.682  -8.779  1.00 35.92 ? 47  VAL F CG2 1 
ATOM   7148  N  N   . HIS G  1 75  ? 94.646  74.947  -10.111 1.00 38.20 ? 48  HIS F N   1 
ATOM   7149  C  CA  . HIS G  1 75  ? 96.074  74.779  -9.894  1.00 36.70 ? 48  HIS F CA  1 
ATOM   7150  C  C   . HIS G  1 75  ? 96.625  75.938  -9.063  1.00 46.23 ? 48  HIS F C   1 
ATOM   7151  O  O   . HIS G  1 75  ? 95.947  76.942  -8.819  1.00 39.04 ? 48  HIS F O   1 
ATOM   7152  C  CB  . HIS G  1 75  ? 96.803  74.648  -11.233 1.00 35.97 ? 48  HIS F CB  1 
ATOM   7153  C  CG  . HIS G  1 75  ? 96.456  73.400  -11.984 1.00 39.32 ? 48  HIS F CG  1 
ATOM   7154  N  ND1 . HIS G  1 75  ? 97.410  72.533  -12.473 1.00 45.32 ? 48  HIS F ND1 1 
ATOM   7155  C  CD2 . HIS G  1 75  ? 95.256  72.883  -12.347 1.00 37.40 ? 48  HIS F CD2 1 
ATOM   7156  C  CE1 . HIS G  1 75  ? 96.814  71.531  -13.098 1.00 40.01 ? 48  HIS F CE1 1 
ATOM   7157  N  NE2 . HIS G  1 75  ? 95.507  71.721  -13.038 1.00 42.10 ? 48  HIS F NE2 1 
ATOM   7158  N  N   . GLU G  1 76  ? 97.880  75.786  -8.618  1.00 43.45 ? 49  GLU F N   1 
ATOM   7159  C  CA  . GLU G  1 76  ? 98.363  76.607  -7.508  1.00 39.06 ? 49  GLU F CA  1 
ATOM   7160  C  C   . GLU G  1 76  ? 98.606  78.058  -7.923  1.00 34.80 ? 49  GLU F C   1 
ATOM   7161  O  O   . GLU G  1 76  ? 98.280  78.985  -7.172  1.00 41.40 ? 49  GLU F O   1 
ATOM   7162  C  CB  . GLU G  1 76  ? 99.639  76.009  -6.914  1.00 41.13 ? 49  GLU F CB  1 
ATOM   7163  C  CG  . GLU G  1 76  ? 100.014 76.623  -5.552  1.00 46.13 ? 49  GLU F CG  1 
ATOM   7164  C  CD  . GLU G  1 76  ? 101.311 76.064  -4.966  1.00 55.25 ? 49  GLU F CD  1 
ATOM   7165  O  OE1 . GLU G  1 76  ? 101.951 75.216  -5.626  1.00 51.16 ? 49  GLU F OE1 1 
ATOM   7166  O  OE2 . GLU G  1 76  ? 101.685 76.474  -3.842  1.00 54.48 ? 49  GLU F OE2 1 
ATOM   7167  N  N   . PHE G  1 77  ? 99.177  78.281  -9.100  1.00 37.98 ? 50  PHE F N   1 
ATOM   7168  C  CA  . PHE G  1 77  ? 99.651  79.603  -9.484  1.00 41.32 ? 50  PHE F CA  1 
ATOM   7169  C  C   . PHE G  1 77  ? 98.793  80.179  -10.600 1.00 38.65 ? 50  PHE F C   1 
ATOM   7170  O  O   . PHE G  1 77  ? 98.425  79.471  -11.542 1.00 38.65 ? 50  PHE F O   1 
ATOM   7171  C  CB  . PHE G  1 77  ? 101.118 79.538  -9.921  1.00 39.00 ? 50  PHE F CB  1 
ATOM   7172  C  CG  . PHE G  1 77  ? 102.016 78.948  -8.875  1.00 38.33 ? 50  PHE F CG  1 
ATOM   7173  C  CD1 . PHE G  1 77  ? 102.126 79.551  -7.629  1.00 42.62 ? 50  PHE F CD1 1 
ATOM   7174  C  CD2 . PHE G  1 77  ? 102.714 77.773  -9.116  1.00 42.21 ? 50  PHE F CD2 1 
ATOM   7175  C  CE1 . PHE G  1 77  ? 102.934 79.010  -6.652  1.00 43.65 ? 50  PHE F CE1 1 
ATOM   7176  C  CE2 . PHE G  1 77  ? 103.524 77.222  -8.135  1.00 45.21 ? 50  PHE F CE2 1 
ATOM   7177  C  CZ  . PHE G  1 77  ? 103.633 77.841  -6.905  1.00 40.71 ? 50  PHE F CZ  1 
ATOM   7178  N  N   . GLY G  1 78  ? 98.485  81.470  -10.489 1.00 36.35 ? 51  GLY F N   1 
ATOM   7179  C  CA  . GLY G  1 78  ? 97.824  82.180  -11.565 1.00 36.09 ? 51  GLY F CA  1 
ATOM   7180  C  C   . GLY G  1 78  ? 98.838  82.735  -12.536 1.00 38.54 ? 51  GLY F C   1 
ATOM   7181  O  O   . GLY G  1 78  ? 98.789  83.909  -12.917 1.00 43.47 ? 51  GLY F O   1 
ATOM   7182  N  N   . ASP G  1 79  ? 99.775  81.880  -12.928 1.00 40.10 ? 52  ASP F N   1 
ATOM   7183  C  CA  . ASP G  1 79  ? 100.891 82.226  -13.795 1.00 34.91 ? 52  ASP F CA  1 
ATOM   7184  C  C   . ASP G  1 79  ? 100.630 81.608  -15.158 1.00 37.54 ? 52  ASP F C   1 
ATOM   7185  O  O   . ASP G  1 79  ? 100.567 80.382  -15.285 1.00 45.42 ? 52  ASP F O   1 
ATOM   7186  C  CB  . ASP G  1 79  ? 102.202 81.723  -13.181 1.00 40.81 ? 52  ASP F CB  1 
ATOM   7187  C  CG  . ASP G  1 79  ? 103.438 82.100  -13.990 1.00 37.70 ? 52  ASP F CG  1 
ATOM   7188  O  OD1 . ASP G  1 79  ? 103.345 82.358  -15.214 1.00 39.03 ? 52  ASP F OD1 1 
ATOM   7189  O  OD2 . ASP G  1 79  ? 104.525 82.130  -13.377 1.00 47.68 ? 52  ASP F OD2 1 
ATOM   7190  N  N   . ASN G  1 80  ? 100.471 82.458  -16.170 1.00 38.20 ? 53  ASN F N   1 
ATOM   7191  C  CA  . ASN G  1 80  ? 100.163 82.032  -17.530 1.00 34.48 ? 53  ASN F CA  1 
ATOM   7192  C  C   . ASN G  1 80  ? 101.291 82.369  -18.502 1.00 38.82 ? 53  ASN F C   1 
ATOM   7193  O  O   . ASN G  1 80  ? 101.089 82.346  -19.721 1.00 44.31 ? 53  ASN F O   1 
ATOM   7194  C  CB  . ASN G  1 80  ? 98.859  82.689  -17.990 1.00 45.05 ? 53  ASN F CB  1 
ATOM   7195  C  CG  . ASN G  1 80  ? 98.321  82.089  -19.258 1.00 48.23 ? 53  ASN F CG  1 
ATOM   7196  O  OD1 . ASN G  1 80  ? 97.569  82.730  -19.995 1.00 57.33 ? 53  ASN F OD1 1 
ATOM   7197  N  ND2 . ASN G  1 80  ? 98.691  80.844  -19.519 1.00 52.05 ? 53  ASN F ND2 1 
ATOM   7198  N  N   . THR G  1 81  ? 102.478 82.692  -17.983 1.00 39.92 ? 54  THR F N   1 
ATOM   7199  C  CA  . THR G  1 81  ? 103.565 83.166  -18.838 1.00 39.62 ? 54  THR F CA  1 
ATOM   7200  C  C   . THR G  1 81  ? 103.980 82.115  -19.858 1.00 41.97 ? 54  THR F C   1 
ATOM   7201  O  O   . THR G  1 81  ? 104.273 82.443  -21.013 1.00 43.73 ? 54  THR F O   1 
ATOM   7202  C  CB  . THR G  1 81  ? 104.757 83.572  -17.978 1.00 36.11 ? 54  THR F CB  1 
ATOM   7203  O  OG1 . THR G  1 81  ? 105.019 82.534  -17.030 1.00 45.88 ? 54  THR F OG1 1 
ATOM   7204  C  CG2 . THR G  1 81  ? 104.450 84.859  -17.224 1.00 37.05 ? 54  THR F CG2 1 
ATOM   7205  N  N   . ALA G  1 82  ? 104.023 80.848  -19.454 1.00 45.34 ? 55  ALA F N   1 
ATOM   7206  C  CA  . ALA G  1 82  ? 104.359 79.751  -20.356 1.00 49.59 ? 55  ALA F CA  1 
ATOM   7207  C  C   . ALA G  1 82  ? 103.120 78.913  -20.657 1.00 55.88 ? 55  ALA F C   1 
ATOM   7208  O  O   . ALA G  1 82  ? 103.163 77.678  -20.689 1.00 51.56 ? 55  ALA F O   1 
ATOM   7209  C  CB  . ALA G  1 82  ? 105.477 78.887  -19.773 1.00 46.81 ? 55  ALA F CB  1 
ATOM   7210  N  N   . GLY G  1 83  ? 101.994 79.593  -20.873 1.00 46.80 ? 56  GLY F N   1 
ATOM   7211  C  CA  . GLY G  1 83  ? 100.744 78.889  -21.048 1.00 40.88 ? 56  GLY F CA  1 
ATOM   7212  C  C   . GLY G  1 83  ? 100.298 78.212  -19.762 1.00 41.55 ? 56  GLY F C   1 
ATOM   7213  O  O   . GLY G  1 83  ? 100.662 78.605  -18.646 1.00 42.28 ? 56  GLY F O   1 
ATOM   7214  N  N   . CYS G  1 84  ? 99.507  77.154  -19.929 1.00 40.43 ? 57  CYS F N   1 
ATOM   7215  C  CA  . CYS G  1 84  ? 98.942  76.466  -18.779 1.00 44.42 ? 57  CYS F CA  1 
ATOM   7216  C  C   . CYS G  1 84  ? 100.014 75.736  -17.971 1.00 38.75 ? 57  CYS F C   1 
ATOM   7217  O  O   . CYS G  1 84  ? 99.799  75.456  -16.787 1.00 38.97 ? 57  CYS F O   1 
ATOM   7218  C  CB  . CYS G  1 84  ? 97.852  75.505  -19.262 1.00 50.10 ? 57  CYS F CB  1 
ATOM   7219  S  SG  . CYS G  1 84  ? 96.404  76.330  -20.055 1.00 64.09 ? 57  CYS F SG  1 
ATOM   7220  N  N   . THR G  1 85  ? 101.178 75.459  -18.572 1.00 46.08 ? 58  THR F N   1 
ATOM   7221  C  CA  . THR G  1 85  ? 102.255 74.790  -17.840 1.00 44.21 ? 58  THR F CA  1 
ATOM   7222  C  C   . THR G  1 85  ? 102.668 75.570  -16.601 1.00 43.89 ? 58  THR F C   1 
ATOM   7223  O  O   . THR G  1 85  ? 103.014 74.971  -15.575 1.00 46.77 ? 58  THR F O   1 
ATOM   7224  C  CB  . THR G  1 85  ? 103.479 74.599  -18.738 1.00 49.51 ? 58  THR F CB  1 
ATOM   7225  O  OG1 . THR G  1 85  ? 103.064 74.238  -20.061 1.00 54.40 ? 58  THR F OG1 1 
ATOM   7226  C  CG2 . THR G  1 85  ? 104.389 73.514  -18.168 1.00 46.71 ? 58  THR F CG2 1 
ATOM   7227  N  N   . SER G  1 86  ? 102.632 76.905  -16.671 1.00 44.73 ? 59  SER F N   1 
ATOM   7228  C  CA  . SER G  1 86  ? 103.099 77.747  -15.575 1.00 41.47 ? 59  SER F CA  1 
ATOM   7229  C  C   . SER G  1 86  ? 102.207 77.675  -14.346 1.00 40.04 ? 59  SER F C   1 
ATOM   7230  O  O   . SER G  1 86  ? 102.605 78.164  -13.280 1.00 38.91 ? 59  SER F O   1 
ATOM   7231  C  CB  . SER G  1 86  ? 103.179 79.201  -16.032 1.00 39.78 ? 59  SER F CB  1 
ATOM   7232  O  OG  . SER G  1 86  ? 103.597 79.278  -17.373 1.00 47.99 ? 59  SER F OG  1 
ATOM   7233  N  N   . ALA G  1 87  ? 101.007 77.102  -14.458 1.00 41.45 ? 60  ALA F N   1 
ATOM   7234  C  CA  . ALA G  1 87  ? 100.106 77.115  -13.311 1.00 37.86 ? 60  ALA F CA  1 
ATOM   7235  C  C   . ALA G  1 87  ? 100.569 76.209  -12.177 1.00 38.00 ? 60  ALA F C   1 
ATOM   7236  O  O   . ALA G  1 87  ? 100.062 76.342  -11.054 1.00 41.60 ? 60  ALA F O   1 
ATOM   7237  C  CB  . ALA G  1 87  ? 98.696  76.726  -13.755 1.00 39.03 ? 60  ALA F CB  1 
ATOM   7238  N  N   . GLY G  1 88  ? 101.521 75.309  -12.426 1.00 40.07 ? 61  GLY F N   1 
ATOM   7239  C  CA  . GLY G  1 88  ? 102.014 74.429  -11.391 1.00 43.40 ? 61  GLY F CA  1 
ATOM   7240  C  C   . GLY G  1 88  ? 101.077 73.262  -11.146 1.00 42.42 ? 61  GLY F C   1 
ATOM   7241  O  O   . GLY G  1 88  ? 100.254 72.911  -11.999 1.00 44.19 ? 61  GLY F O   1 
ATOM   7242  N  N   . PRO G  1 89  ? 101.179 72.645  -9.973  1.00 43.94 ? 62  PRO F N   1 
ATOM   7243  C  CA  . PRO G  1 89  ? 100.351 71.479  -9.655  1.00 45.30 ? 62  PRO F CA  1 
ATOM   7244  C  C   . PRO G  1 89  ? 98.965  71.915  -9.193  1.00 44.40 ? 62  PRO F C   1 
ATOM   7245  O  O   . PRO G  1 89  ? 98.658  73.104  -9.101  1.00 47.11 ? 62  PRO F O   1 
ATOM   7246  C  CB  . PRO G  1 89  ? 101.125 70.822  -8.512  1.00 43.74 ? 62  PRO F CB  1 
ATOM   7247  C  CG  . PRO G  1 89  ? 101.668 72.017  -7.744  1.00 39.29 ? 62  PRO F CG  1 
ATOM   7248  C  CD  . PRO G  1 89  ? 102.006 73.055  -8.818  1.00 45.17 ? 62  PRO F CD  1 
ATOM   7249  N  N   . HIS G  1 90  ? 98.131  70.923  -8.878  1.00 41.88 ? 63  HIS F N   1 
ATOM   7250  C  CA  . HIS G  1 90  ? 96.864  71.210  -8.218  1.00 38.86 ? 63  HIS F CA  1 
ATOM   7251  C  C   . HIS G  1 90  ? 97.112  72.018  -6.951  1.00 46.38 ? 63  HIS F C   1 
ATOM   7252  O  O   . HIS G  1 90  ? 98.051  71.752  -6.196  1.00 47.82 ? 63  HIS F O   1 
ATOM   7253  C  CB  . HIS G  1 90  ? 96.114  69.909  -7.873  1.00 39.03 ? 63  HIS F CB  1 
ATOM   7254  C  CG  . HIS G  1 90  ? 95.797  69.054  -9.062  1.00 42.51 ? 63  HIS F CG  1 
ATOM   7255  N  ND1 . HIS G  1 90  ? 95.182  67.825  -8.952  1.00 49.57 ? 63  HIS F ND1 1 
ATOM   7256  C  CD2 . HIS G  1 90  ? 96.009  69.250  -10.386 1.00 42.19 ? 63  HIS F CD2 1 
ATOM   7257  C  CE1 . HIS G  1 90  ? 95.026  67.304  -10.157 1.00 43.03 ? 63  HIS F CE1 1 
ATOM   7258  N  NE2 . HIS G  1 90  ? 95.520  68.148  -11.044 1.00 41.88 ? 63  HIS F NE2 1 
ATOM   7259  N  N   . PHE G  1 91  ? 96.267  73.016  -6.723  1.00 39.20 ? 64  PHE F N   1 
ATOM   7260  C  CA  . PHE G  1 91  ? 96.350  73.793  -5.498  1.00 41.22 ? 64  PHE F CA  1 
ATOM   7261  C  C   . PHE G  1 91  ? 96.083  72.895  -4.292  1.00 46.13 ? 64  PHE F C   1 
ATOM   7262  O  O   . PHE G  1 91  ? 95.015  72.282  -4.181  1.00 42.96 ? 64  PHE F O   1 
ATOM   7263  C  CB  . PHE G  1 91  ? 95.366  74.961  -5.579  1.00 38.26 ? 64  PHE F CB  1 
ATOM   7264  C  CG  . PHE G  1 91  ? 95.216  75.733  -4.298  1.00 40.15 ? 64  PHE F CG  1 
ATOM   7265  C  CD1 . PHE G  1 91  ? 96.324  76.248  -3.641  1.00 41.39 ? 64  PHE F CD1 1 
ATOM   7266  C  CD2 . PHE G  1 91  ? 93.964  75.921  -3.734  1.00 38.65 ? 64  PHE F CD2 1 
ATOM   7267  C  CE1 . PHE G  1 91  ? 96.176  76.953  -2.454  1.00 33.41 ? 64  PHE F CE1 1 
ATOM   7268  C  CE2 . PHE G  1 91  ? 93.808  76.633  -2.555  1.00 41.82 ? 64  PHE F CE2 1 
ATOM   7269  C  CZ  . PHE G  1 91  ? 94.920  77.143  -1.911  1.00 43.63 ? 64  PHE F CZ  1 
ATOM   7270  N  N   . ASN G  1 92  ? 97.064  72.811  -3.387  1.00 44.87 ? 65  ASN F N   1 
ATOM   7271  C  CA  . ASN G  1 92  ? 97.098  71.759  -2.367  1.00 46.73 ? 65  ASN F CA  1 
ATOM   7272  C  C   . ASN G  1 92  ? 97.740  72.285  -1.088  1.00 51.11 ? 65  ASN F C   1 
ATOM   7273  O  O   . ASN G  1 92  ? 98.810  71.825  -0.673  1.00 52.71 ? 65  ASN F O   1 
ATOM   7274  C  CB  . ASN G  1 92  ? 97.853  70.538  -2.899  1.00 45.03 ? 65  ASN F CB  1 
ATOM   7275  C  CG  . ASN G  1 92  ? 97.805  69.349  -1.952  1.00 47.33 ? 65  ASN F CG  1 
ATOM   7276  O  OD1 . ASN G  1 92  ? 96.980  69.293  -1.029  1.00 47.30 ? 65  ASN F OD1 1 
ATOM   7277  N  ND2 . ASN G  1 92  ? 98.700  68.386  -2.178  1.00 46.45 ? 65  ASN F ND2 1 
ATOM   7278  N  N   . PRO G  1 93  ? 97.086  73.238  -0.410  1.00 46.63 ? 66  PRO F N   1 
ATOM   7279  C  CA  . PRO G  1 93  ? 97.699  73.843  0.788   1.00 45.22 ? 66  PRO F CA  1 
ATOM   7280  C  C   . PRO G  1 93  ? 97.689  72.954  2.024   1.00 53.88 ? 66  PRO F C   1 
ATOM   7281  O  O   . PRO G  1 93  ? 98.343  73.308  3.015   1.00 59.50 ? 66  PRO F O   1 
ATOM   7282  C  CB  . PRO G  1 93  ? 96.850  75.099  1.011   1.00 43.30 ? 66  PRO F CB  1 
ATOM   7283  C  CG  . PRO G  1 93  ? 95.508  74.702  0.501   1.00 45.15 ? 66  PRO F CG  1 
ATOM   7284  C  CD  . PRO G  1 93  ? 95.774  73.836  -0.707  1.00 44.05 ? 66  PRO F CD  1 
ATOM   7285  N  N   . LEU G  1 94  ? 96.975  71.829  2.016   1.00 54.16 ? 67  LEU F N   1 
ATOM   7286  C  CA  . LEU G  1 94  ? 96.979  70.912  3.150   1.00 47.66 ? 67  LEU F CA  1 
ATOM   7287  C  C   . LEU G  1 94  ? 97.817  69.667  2.892   1.00 48.61 ? 67  LEU F C   1 
ATOM   7288  O  O   . LEU G  1 94  ? 97.773  68.727  3.694   1.00 51.87 ? 67  LEU F O   1 
ATOM   7289  C  CB  . LEU G  1 94  ? 95.553  70.506  3.542   1.00 48.02 ? 67  LEU F CB  1 
ATOM   7290  C  CG  . LEU G  1 94  ? 94.538  71.530  4.071   1.00 49.49 ? 67  LEU F CG  1 
ATOM   7291  C  CD1 . LEU G  1 94  ? 95.009  72.085  5.415   1.00 47.29 ? 67  LEU F CD1 1 
ATOM   7292  C  CD2 . LEU G  1 94  ? 94.216  72.660  3.086   1.00 55.11 ? 67  LEU F CD2 1 
ATOM   7293  N  N   . SER G  1 95  ? 98.564  69.630  1.789   1.00 47.77 ? 68  SER F N   1 
ATOM   7294  C  CA  . SER G  1 95  ? 99.527  68.574  1.479   1.00 50.08 ? 68  SER F CA  1 
ATOM   7295  C  C   . SER G  1 95  ? 98.895  67.189  1.343   1.00 57.30 ? 68  SER F C   1 
ATOM   7296  O  O   . SER G  1 95  ? 99.617  66.180  1.369   1.00 55.13 ? 68  SER F O   1 
ATOM   7297  C  CB  . SER G  1 95  ? 100.649 68.529  2.525   1.00 48.62 ? 68  SER F CB  1 
ATOM   7298  O  OG  . SER G  1 95  ? 101.459 69.691  2.440   1.00 60.63 ? 68  SER F OG  1 
ATOM   7299  N  N   . ARG G  1 96  ? 97.572  67.111  1.187   1.00 59.82 ? 69  ARG F N   1 
ATOM   7300  C  CA  . ARG G  1 96  ? 96.890  65.836  1.001   1.00 49.04 ? 69  ARG F CA  1 
ATOM   7301  C  C   . ARG G  1 96  ? 97.199  65.272  -0.386  1.00 52.33 ? 69  ARG F C   1 
ATOM   7302  O  O   . ARG G  1 96  ? 97.929  65.865  -1.185  1.00 52.51 ? 69  ARG F O   1 
ATOM   7303  C  CB  . ARG G  1 96  ? 95.387  66.006  1.191   1.00 43.08 ? 69  ARG F CB  1 
ATOM   7304  C  CG  . ARG G  1 96  ? 94.994  66.864  2.382   1.00 51.93 ? 69  ARG F CG  1 
ATOM   7305  C  CD  . ARG G  1 96  ? 94.381  66.038  3.499   1.00 49.80 ? 69  ARG F CD  1 
ATOM   7306  N  NE  . ARG G  1 96  ? 93.757  66.884  4.511   1.00 58.08 ? 69  ARG F NE  1 
ATOM   7307  C  CZ  . ARG G  1 96  ? 92.489  67.273  4.479   1.00 62.13 ? 69  ARG F CZ  1 
ATOM   7308  N  NH1 . ARG G  1 96  ? 91.683  66.923  3.489   1.00 59.31 ? 69  ARG F NH1 1 
ATOM   7309  N  NH2 . ARG G  1 96  ? 92.017  68.039  5.462   1.00 58.44 ? 69  ARG F NH2 1 
ATOM   7310  N  N   . LYS G  1 97  ? 96.638  64.101  -0.678  1.00 49.35 ? 70  LYS F N   1 
ATOM   7311  C  CA  . LYS G  1 97  ? 96.807  63.479  -1.983  1.00 50.37 ? 70  LYS F CA  1 
ATOM   7312  C  C   . LYS G  1 97  ? 95.555  63.676  -2.840  1.00 48.13 ? 70  LYS F C   1 
ATOM   7313  O  O   . LYS G  1 97  ? 94.486  64.055  -2.354  1.00 47.97 ? 70  LYS F O   1 
ATOM   7314  C  CB  . LYS G  1 97  ? 97.148  61.989  -1.833  1.00 52.30 ? 70  LYS F CB  1 
ATOM   7315  C  CG  . LYS G  1 97  ? 98.185  61.689  -0.757  1.00 51.60 ? 70  LYS F CG  1 
ATOM   7316  C  CD  . LYS G  1 97  ? 99.391  60.973  -1.358  1.00 52.26 ? 70  LYS F CD  1 
ATOM   7317  C  CE  . LYS G  1 97  ? 100.598 61.023  -0.440  1.00 54.11 ? 70  LYS F CE  1 
ATOM   7318  N  NZ  . LYS G  1 97  ? 101.254 62.375  -0.500  1.00 62.34 ? 70  LYS F NZ  1 
ATOM   7319  N  N   . HIS G  1 98  ? 95.705  63.417  -4.139  1.00 49.03 ? 71  HIS F N   1 
ATOM   7320  C  CA  . HIS G  1 98  ? 94.651  63.743  -5.092  1.00 50.59 ? 71  HIS F CA  1 
ATOM   7321  C  C   . HIS G  1 98  ? 93.462  62.806  -4.928  1.00 50.16 ? 71  HIS F C   1 
ATOM   7322  O  O   . HIS G  1 98  ? 93.624  61.584  -4.875  1.00 52.12 ? 71  HIS F O   1 
ATOM   7323  C  CB  . HIS G  1 98  ? 95.182  63.664  -6.524  1.00 47.46 ? 71  HIS F CB  1 
ATOM   7324  C  CG  . HIS G  1 98  ? 94.126  63.829  -7.574  1.00 50.62 ? 71  HIS F CG  1 
ATOM   7325  N  ND1 . HIS G  1 98  ? 93.705  65.065  -8.017  1.00 57.02 ? 71  HIS F ND1 1 
ATOM   7326  C  CD2 . HIS G  1 98  ? 93.412  62.915  -8.276  1.00 51.38 ? 71  HIS F CD2 1 
ATOM   7327  C  CE1 . HIS G  1 98  ? 92.775  64.906  -8.943  1.00 47.75 ? 71  HIS F CE1 1 
ATOM   7328  N  NE2 . HIS G  1 98  ? 92.580  63.611  -9.121  1.00 51.83 ? 71  HIS F NE2 1 
ATOM   7329  N  N   . GLY G  1 99  ? 92.265  63.386  -4.858  1.00 47.89 ? 72  GLY F N   1 
ATOM   7330  C  CA  . GLY G  1 99  ? 91.040  62.614  -4.916  1.00 43.65 ? 72  GLY F CA  1 
ATOM   7331  C  C   . GLY G  1 99  ? 89.952  63.311  -5.710  1.00 46.52 ? 72  GLY F C   1 
ATOM   7332  O  O   . GLY G  1 99  ? 90.225  64.254  -6.462  1.00 43.51 ? 72  GLY F O   1 
ATOM   7333  N  N   . GLY G  1 100 ? 88.711  62.858  -5.543  1.00 46.44 ? 73  GLY F N   1 
ATOM   7334  C  CA  . GLY G  1 100 ? 87.567  63.520  -6.120  1.00 43.03 ? 73  GLY F CA  1 
ATOM   7335  C  C   . GLY G  1 100 ? 86.978  64.555  -5.181  1.00 44.07 ? 73  GLY F C   1 
ATOM   7336  O  O   . GLY G  1 100 ? 87.338  64.641  -3.999  1.00 47.40 ? 73  GLY F O   1 
ATOM   7337  N  N   . PRO G  1 101 ? 86.058  65.372  -5.696  1.00 43.66 ? 74  PRO F N   1 
ATOM   7338  C  CA  . PRO G  1 101 ? 85.450  66.412  -4.850  1.00 40.98 ? 74  PRO F CA  1 
ATOM   7339  C  C   . PRO G  1 101 ? 84.692  65.869  -3.649  1.00 43.35 ? 74  PRO F C   1 
ATOM   7340  O  O   . PRO G  1 101 ? 84.539  66.593  -2.657  1.00 45.72 ? 74  PRO F O   1 
ATOM   7341  C  CB  . PRO G  1 101 ? 84.513  67.155  -5.821  1.00 46.53 ? 74  PRO F CB  1 
ATOM   7342  C  CG  . PRO G  1 101 ? 84.295  66.198  -6.978  1.00 37.00 ? 74  PRO F CG  1 
ATOM   7343  C  CD  . PRO G  1 101 ? 85.596  65.448  -7.093  1.00 37.46 ? 74  PRO F CD  1 
ATOM   7344  N  N   . LYS G  1 102 ? 84.213  64.629  -3.696  1.00 41.71 ? 75  LYS F N   1 
ATOM   7345  C  CA  . LYS G  1 102 ? 83.459  64.065  -2.587  1.00 46.25 ? 75  LYS F CA  1 
ATOM   7346  C  C   . LYS G  1 102 ? 84.342  63.307  -1.606  1.00 47.36 ? 75  LYS F C   1 
ATOM   7347  O  O   . LYS G  1 102 ? 83.846  62.860  -0.568  1.00 52.85 ? 75  LYS F O   1 
ATOM   7348  C  CB  . LYS G  1 102 ? 82.348  63.145  -3.112  1.00 41.61 ? 75  LYS F CB  1 
ATOM   7349  C  CG  . LYS G  1 102 ? 81.380  63.848  -4.063  1.00 50.96 ? 75  LYS F CG  1 
ATOM   7350  C  CD  . LYS G  1 102 ? 80.131  63.015  -4.389  1.00 54.50 ? 75  LYS F CD  1 
ATOM   7351  C  CE  . LYS G  1 102 ? 80.346  61.932  -5.460  1.00 55.71 ? 75  LYS F CE  1 
ATOM   7352  N  NZ  . LYS G  1 102 ? 81.477  60.989  -5.228  1.00 58.95 ? 75  LYS F NZ  1 
ATOM   7353  N  N   . ASP G  1 103 ? 85.629  63.163  -1.907  1.00 46.42 ? 76  ASP F N   1 
ATOM   7354  C  CA  . ASP G  1 103 ? 86.551  62.479  -1.013  1.00 46.85 ? 76  ASP F CA  1 
ATOM   7355  C  C   . ASP G  1 103 ? 87.038  63.432  0.077   1.00 50.92 ? 76  ASP F C   1 
ATOM   7356  O  O   . ASP G  1 103 ? 87.069  64.656  -0.101  1.00 49.54 ? 76  ASP F O   1 
ATOM   7357  C  CB  . ASP G  1 103 ? 87.744  61.926  -1.801  1.00 45.08 ? 76  ASP F CB  1 
ATOM   7358  C  CG  . ASP G  1 103 ? 87.334  60.865  -2.824  1.00 56.76 ? 76  ASP F CG  1 
ATOM   7359  O  OD1 . ASP G  1 103 ? 86.362  60.126  -2.558  1.00 59.84 ? 76  ASP F OD1 1 
ATOM   7360  O  OD2 . ASP G  1 103 ? 87.990  60.760  -3.889  1.00 51.32 ? 76  ASP F OD2 1 
ATOM   7361  N  N   . GLU G  1 104 ? 87.413  62.861  1.226   1.00 58.75 ? 77  GLU F N   1 
ATOM   7362  C  CA  . GLU G  1 104 ? 88.049  63.693  2.243   1.00 54.25 ? 77  GLU F CA  1 
ATOM   7363  C  C   . GLU G  1 104 ? 89.525  63.907  1.923   1.00 53.90 ? 77  GLU F C   1 
ATOM   7364  O  O   . GLU G  1 104 ? 90.038  65.023  2.062   1.00 66.97 ? 77  GLU F O   1 
ATOM   7365  C  CB  . GLU G  1 104 ? 87.884  63.086  3.637   1.00 47.30 ? 77  GLU F CB  1 
ATOM   7366  C  CG  . GLU G  1 104 ? 87.528  64.130  4.711   1.00 54.23 ? 77  GLU F CG  1 
ATOM   7367  C  CD  . GLU G  1 104 ? 88.746  64.876  5.286   1.00 69.04 ? 77  GLU F CD  1 
ATOM   7368  O  OE1 . GLU G  1 104 ? 89.787  64.232  5.556   1.00 69.06 ? 77  GLU F OE1 1 
ATOM   7369  O  OE2 . GLU G  1 104 ? 88.656  66.115  5.475   1.00 62.53 ? 77  GLU F OE2 1 
ATOM   7370  N  N   . GLU G  1 105 ? 90.217  62.861  1.476   1.00 48.03 ? 78  GLU F N   1 
ATOM   7371  C  CA  . GLU G  1 105 ? 91.580  63.005  0.965   1.00 54.42 ? 78  GLU F CA  1 
ATOM   7372  C  C   . GLU G  1 105 ? 91.493  63.541  -0.461  1.00 51.03 ? 78  GLU F C   1 
ATOM   7373  O  O   . GLU G  1 105 ? 91.328  62.789  -1.425  1.00 50.31 ? 78  GLU F O   1 
ATOM   7374  C  CB  . GLU G  1 105 ? 92.330  61.677  1.037   1.00 49.39 ? 78  GLU F CB  1 
ATOM   7375  C  CG  . GLU G  1 105 ? 93.845  61.754  0.787   1.00 42.69 ? 78  GLU F CG  1 
ATOM   7376  C  CD  . GLU G  1 105 ? 94.631  62.446  1.903   1.00 58.38 ? 78  GLU F CD  1 
ATOM   7377  O  OE1 . GLU G  1 105 ? 94.028  62.873  2.921   1.00 62.32 ? 78  GLU F OE1 1 
ATOM   7378  O  OE2 . GLU G  1 105 ? 95.870  62.554  1.756   1.00 62.09 ? 78  GLU F OE2 1 
ATOM   7379  N  N   . ARG G  1 106 ? 91.585  64.867  -0.587  1.00 50.60 ? 79  ARG F N   1 
ATOM   7380  C  CA  . ARG G  1 106 ? 91.610  65.526  -1.886  1.00 48.99 ? 79  ARG F CA  1 
ATOM   7381  C  C   . ARG G  1 106 ? 92.461  66.785  -1.797  1.00 49.24 ? 79  ARG F C   1 
ATOM   7382  O  O   . ARG G  1 106 ? 92.637  67.365  -0.722  1.00 47.24 ? 79  ARG F O   1 
ATOM   7383  C  CB  . ARG G  1 106 ? 90.205  65.911  -2.370  1.00 39.81 ? 79  ARG F CB  1 
ATOM   7384  C  CG  . ARG G  1 106 ? 89.400  66.701  -1.342  1.00 41.93 ? 79  ARG F CG  1 
ATOM   7385  C  CD  . ARG G  1 106 ? 88.132  67.280  -1.960  1.00 43.90 ? 79  ARG F CD  1 
ATOM   7386  N  NE  . ARG G  1 106 ? 88.393  68.553  -2.627  1.00 44.64 ? 79  ARG F NE  1 
ATOM   7387  C  CZ  . ARG G  1 106 ? 87.450  69.386  -3.050  1.00 43.13 ? 79  ARG F CZ  1 
ATOM   7388  N  NH1 . ARG G  1 106 ? 86.164  69.105  -2.907  1.00 43.84 ? 79  ARG F NH1 1 
ATOM   7389  N  NH2 . ARG G  1 106 ? 87.804  70.533  -3.625  1.00 41.98 ? 79  ARG F NH2 1 
ATOM   7390  N  N   . HIS G  1 107 ? 92.984  67.207  -2.945  1.00 49.83 ? 80  HIS F N   1 
ATOM   7391  C  CA  . HIS G  1 107 ? 93.518  68.557  -3.050  1.00 46.28 ? 80  HIS F CA  1 
ATOM   7392  C  C   . HIS G  1 107 ? 92.370  69.556  -2.939  1.00 44.51 ? 80  HIS F C   1 
ATOM   7393  O  O   . HIS G  1 107 ? 91.215  69.241  -3.243  1.00 42.77 ? 80  HIS F O   1 
ATOM   7394  C  CB  . HIS G  1 107 ? 94.254  68.755  -4.376  1.00 43.33 ? 80  HIS F CB  1 
ATOM   7395  C  CG  . HIS G  1 107 ? 95.385  67.798  -4.591  1.00 45.04 ? 80  HIS F CG  1 
ATOM   7396  N  ND1 . HIS G  1 107 ? 95.715  67.304  -5.833  1.00 55.35 ? 80  HIS F ND1 1 
ATOM   7397  C  CD2 . HIS G  1 107 ? 96.232  67.208  -3.714  1.00 43.77 ? 80  HIS F CD2 1 
ATOM   7398  C  CE1 . HIS G  1 107 ? 96.745  66.484  -5.719  1.00 44.93 ? 80  HIS F CE1 1 
ATOM   7399  N  NE2 . HIS G  1 107 ? 97.072  66.402  -4.442  1.00 46.90 ? 80  HIS F NE2 1 
ATOM   7400  N  N   . VAL G  1 108 ? 92.683  70.768  -2.477  1.00 43.99 ? 81  VAL F N   1 
ATOM   7401  C  CA  . VAL G  1 108 ? 91.655  71.805  -2.441  1.00 40.34 ? 81  VAL F CA  1 
ATOM   7402  C  C   . VAL G  1 108 ? 91.113  72.063  -3.846  1.00 33.30 ? 81  VAL F C   1 
ATOM   7403  O  O   . VAL G  1 108 ? 89.907  72.257  -4.033  1.00 40.65 ? 81  VAL F O   1 
ATOM   7404  C  CB  . VAL G  1 108 ? 92.200  73.089  -1.786  1.00 36.79 ? 81  VAL F CB  1 
ATOM   7405  C  CG1 . VAL G  1 108 ? 91.221  74.249  -1.974  1.00 34.81 ? 81  VAL F CG1 1 
ATOM   7406  C  CG2 . VAL G  1 108 ? 92.439  72.853  -0.296  1.00 37.88 ? 81  VAL F CG2 1 
ATOM   7407  N  N   . GLY G  1 109 ? 91.980  72.038  -4.852  1.00 33.89 ? 82  GLY F N   1 
ATOM   7408  C  CA  . GLY G  1 109 ? 91.549  72.303  -6.213  1.00 40.51 ? 82  GLY F CA  1 
ATOM   7409  C  C   . GLY G  1 109 ? 91.005  71.109  -6.979  1.00 39.46 ? 82  GLY F C   1 
ATOM   7410  O  O   . GLY G  1 109 ? 90.869  71.168  -8.203  1.00 39.83 ? 82  GLY F O   1 
ATOM   7411  N  N   . ASP G  1 110 ? 90.681  70.026  -6.273  1.00 40.20 ? 83  ASP F N   1 
ATOM   7412  C  CA  . ASP G  1 110 ? 90.154  68.802  -6.885  1.00 39.32 ? 83  ASP F CA  1 
ATOM   7413  C  C   . ASP G  1 110 ? 88.660  68.989  -7.136  1.00 35.01 ? 83  ASP F C   1 
ATOM   7414  O  O   . ASP G  1 110 ? 87.819  68.662  -6.295  1.00 39.34 ? 83  ASP F O   1 
ATOM   7415  C  CB  . ASP G  1 110 ? 90.401  67.599  -5.976  1.00 38.48 ? 83  ASP F CB  1 
ATOM   7416  C  CG  . ASP G  1 110 ? 91.828  67.073  -6.049  1.00 47.31 ? 83  ASP F CG  1 
ATOM   7417  O  OD1 . ASP G  1 110 ? 92.584  67.489  -6.956  1.00 53.61 ? 83  ASP F OD1 1 
ATOM   7418  O  OD2 . ASP G  1 110 ? 92.200  66.243  -5.179  1.00 42.37 ? 83  ASP F OD2 1 
ATOM   7419  N  N   . LEU G  1 111 ? 88.311  69.511  -8.309  1.00 33.09 ? 84  LEU F N   1 
ATOM   7420  C  CA  . LEU G  1 111 ? 86.911  69.740  -8.641  1.00 33.97 ? 84  LEU F CA  1 
ATOM   7421  C  C   . LEU G  1 111 ? 86.308  68.614  -9.473  1.00 33.58 ? 84  LEU F C   1 
ATOM   7422  O  O   . LEU G  1 111 ? 85.163  68.736  -9.919  1.00 36.62 ? 84  LEU F O   1 
ATOM   7423  C  CB  . LEU G  1 111 ? 86.748  71.086  -9.360  1.00 35.71 ? 84  LEU F CB  1 
ATOM   7424  C  CG  . LEU G  1 111 ? 87.043  72.331  -8.517  1.00 34.23 ? 84  LEU F CG  1 
ATOM   7425  C  CD1 . LEU G  1 111 ? 86.358  73.547  -9.127  1.00 34.73 ? 84  LEU F CD1 1 
ATOM   7426  C  CD2 . LEU G  1 111 ? 86.548  72.133  -7.087  1.00 32.24 ? 84  LEU F CD2 1 
ATOM   7427  N  N   . GLY G  1 112 ? 87.044  67.528  -9.698  1.00 35.94 ? 85  GLY F N   1 
ATOM   7428  C  CA  . GLY G  1 112 ? 86.476  66.367  -10.360 1.00 32.76 ? 85  GLY F CA  1 
ATOM   7429  C  C   . GLY G  1 112 ? 86.488  66.432  -11.871 1.00 35.31 ? 85  GLY F C   1 
ATOM   7430  O  O   . GLY G  1 112 ? 87.484  66.863  -12.467 1.00 34.18 ? 85  GLY F O   1 
ATOM   7431  N  N   . ASN G  1 113 ? 85.379  66.020  -12.501 1.00 29.51 ? 86  ASN F N   1 
ATOM   7432  C  CA  . ASN G  1 113 ? 85.258  65.953  -13.954 1.00 30.37 ? 86  ASN F CA  1 
ATOM   7433  C  C   . ASN G  1 113 ? 84.083  66.793  -14.435 1.00 32.14 ? 86  ASN F C   1 
ATOM   7434  O  O   . ASN G  1 113 ? 83.031  66.825  -13.792 1.00 28.93 ? 86  ASN F O   1 
ATOM   7435  C  CB  . ASN G  1 113 ? 85.037  64.513  -14.438 1.00 32.60 ? 86  ASN F CB  1 
ATOM   7436  C  CG  . ASN G  1 113 ? 86.284  63.659  -14.350 1.00 34.88 ? 86  ASN F CG  1 
ATOM   7437  O  OD1 . ASN G  1 113 ? 87.263  63.903  -15.056 1.00 36.81 ? 86  ASN F OD1 1 
ATOM   7438  N  ND2 . ASN G  1 113 ? 86.239  62.623  -13.516 1.00 33.96 ? 86  ASN F ND2 1 
ATOM   7439  N  N   . VAL G  1 114 ? 84.257  67.445  -15.585 1.00 28.25 ? 87  VAL F N   1 
ATOM   7440  C  CA  . VAL G  1 114 ? 83.153  68.017  -16.348 1.00 28.84 ? 87  VAL F CA  1 
ATOM   7441  C  C   . VAL G  1 114 ? 82.940  67.139  -17.573 1.00 33.56 ? 87  VAL F C   1 
ATOM   7442  O  O   . VAL G  1 114 ? 83.877  66.506  -18.076 1.00 32.41 ? 87  VAL F O   1 
ATOM   7443  C  CB  . VAL G  1 114 ? 83.410  69.486  -16.762 1.00 28.08 ? 87  VAL F CB  1 
ATOM   7444  C  CG1 . VAL G  1 114 ? 83.554  70.357  -15.524 1.00 30.53 ? 87  VAL F CG1 1 
ATOM   7445  C  CG2 . VAL G  1 114 ? 84.650  69.583  -17.655 1.00 29.46 ? 87  VAL F CG2 1 
ATOM   7446  N  N   . THR G  1 115 ? 81.697  67.083  -18.046 1.00 27.28 ? 88  THR F N   1 
ATOM   7447  C  CA  . THR G  1 115 ? 81.312  66.168  -19.117 1.00 27.36 ? 88  THR F CA  1 
ATOM   7448  C  C   . THR G  1 115 ? 80.928  66.968  -20.352 1.00 28.50 ? 88  THR F C   1 
ATOM   7449  O  O   . THR G  1 115 ? 79.987  67.762  -20.313 1.00 28.66 ? 88  THR F O   1 
ATOM   7450  C  CB  . THR G  1 115 ? 80.145  65.267  -18.679 1.00 30.13 ? 88  THR F CB  1 
ATOM   7451  O  OG1 . THR G  1 115 ? 80.510  64.537  -17.500 1.00 31.62 ? 88  THR F OG1 1 
ATOM   7452  C  CG2 . THR G  1 115 ? 79.785  64.286  -19.777 1.00 27.55 ? 88  THR F CG2 1 
ATOM   7453  N  N   . ALA G  1 116 ? 81.652  66.759  -21.444 1.00 24.12 ? 89  ALA F N   1 
ATOM   7454  C  CA  . ALA G  1 116 ? 81.329  67.405  -22.708 1.00 28.46 ? 89  ALA F CA  1 
ATOM   7455  C  C   . ALA G  1 116 ? 80.405  66.500  -23.510 1.00 33.43 ? 89  ALA F C   1 
ATOM   7456  O  O   . ALA G  1 116 ? 80.651  65.291  -23.601 1.00 25.39 ? 89  ALA F O   1 
ATOM   7457  C  CB  . ALA G  1 116 ? 82.599  67.698  -23.506 1.00 25.93 ? 89  ALA F CB  1 
ATOM   7458  N  N   . ASP G  1 117 ? 79.353  67.086  -24.089 1.00 25.75 ? 90  ASP F N   1 
ATOM   7459  C  CA  . ASP G  1 117 ? 78.387  66.321  -24.867 1.00 25.89 ? 90  ASP F CA  1 
ATOM   7460  C  C   . ASP G  1 117 ? 78.925  66.070  -26.277 1.00 30.48 ? 90  ASP F C   1 
ATOM   7461  O  O   . ASP G  1 117 ? 80.073  66.387  -26.600 1.00 29.25 ? 90  ASP F O   1 
ATOM   7462  C  CB  . ASP G  1 117 ? 77.022  67.020  -24.891 1.00 25.66 ? 90  ASP F CB  1 
ATOM   7463  C  CG  . ASP G  1 117 ? 77.023  68.373  -25.624 1.00 37.55 ? 90  ASP F CG  1 
ATOM   7464  O  OD1 . ASP G  1 117 ? 77.922  68.669  -26.445 1.00 32.01 ? 90  ASP F OD1 1 
ATOM   7465  O  OD2 . ASP G  1 117 ? 76.086  69.161  -25.356 1.00 34.67 ? 90  ASP F OD2 1 
ATOM   7466  N  N   . LYS G  1 118 ? 78.062  65.516  -27.134 1.00 30.17 ? 91  LYS F N   1 
ATOM   7467  C  CA  . LYS G  1 118 ? 78.460  65.109  -28.476 1.00 34.53 ? 91  LYS F CA  1 
ATOM   7468  C  C   . LYS G  1 118 ? 78.935  66.290  -29.313 1.00 39.67 ? 91  LYS F C   1 
ATOM   7469  O  O   . LYS G  1 118 ? 79.699  66.104  -30.266 1.00 35.88 ? 91  LYS F O   1 
ATOM   7470  C  CB  . LYS G  1 118 ? 77.291  64.399  -29.179 1.00 28.45 ? 91  LYS F CB  1 
ATOM   7471  C  CG  . LYS G  1 118 ? 77.209  62.913  -28.908 1.00 41.95 ? 91  LYS F CG  1 
ATOM   7472  C  CD  . LYS G  1 118 ? 76.238  62.208  -29.864 1.00 49.06 ? 91  LYS F CD  1 
ATOM   7473  C  CE  . LYS G  1 118 ? 75.862  60.805  -29.362 1.00 47.95 ? 91  LYS F CE  1 
ATOM   7474  N  NZ  . LYS G  1 118 ? 74.838  60.137  -30.237 1.00 47.37 ? 91  LYS F NZ  1 
ATOM   7475  N  N   . ASP G  1 119 ? 78.491  67.504  -28.988 1.00 34.58 ? 92  ASP F N   1 
ATOM   7476  C  CA  . ASP G  1 119 ? 78.901  68.685  -29.733 1.00 34.41 ? 92  ASP F CA  1 
ATOM   7477  C  C   . ASP G  1 119 ? 80.089  69.381  -29.103 1.00 33.02 ? 92  ASP F C   1 
ATOM   7478  O  O   . ASP G  1 119 ? 80.420  70.496  -29.512 1.00 36.22 ? 92  ASP F O   1 
ATOM   7479  C  CB  . ASP G  1 119 ? 77.747  69.677  -29.848 1.00 38.29 ? 92  ASP F CB  1 
ATOM   7480  C  CG  . ASP G  1 119 ? 76.604  69.131  -30.648 1.00 42.32 ? 92  ASP F CG  1 
ATOM   7481  O  OD1 . ASP G  1 119 ? 76.867  68.405  -31.634 1.00 48.35 ? 92  ASP F OD1 1 
ATOM   7482  O  OD2 . ASP G  1 119 ? 75.447  69.431  -30.290 1.00 49.55 ? 92  ASP F OD2 1 
ATOM   7483  N  N   . GLY G  1 120 ? 80.716  68.763  -28.109 1.00 33.18 ? 93  GLY F N   1 
ATOM   7484  C  CA  . GLY G  1 120 ? 81.911  69.322  -27.518 1.00 30.31 ? 93  GLY F CA  1 
ATOM   7485  C  C   . GLY G  1 120 ? 81.675  70.349  -26.438 1.00 31.34 ? 93  GLY F C   1 
ATOM   7486  O  O   . GLY G  1 120 ? 82.621  71.037  -26.038 1.00 29.07 ? 93  GLY F O   1 
ATOM   7487  N  N   . VAL G  1 121 ? 80.447  70.459  -25.931 1.00 29.48 ? 94  VAL F N   1 
ATOM   7488  C  CA  . VAL G  1 121 ? 80.074  71.486  -24.966 1.00 27.03 ? 94  VAL F CA  1 
ATOM   7489  C  C   . VAL G  1 121 ? 79.892  70.846  -23.601 1.00 26.77 ? 94  VAL F C   1 
ATOM   7490  O  O   . VAL G  1 121 ? 79.176  69.847  -23.462 1.00 27.54 ? 94  VAL F O   1 
ATOM   7491  C  CB  . VAL G  1 121 ? 78.796  72.225  -25.402 1.00 31.53 ? 94  VAL F CB  1 
ATOM   7492  C  CG1 . VAL G  1 121 ? 78.327  73.163  -24.293 1.00 31.44 ? 94  VAL F CG1 1 
ATOM   7493  C  CG2 . VAL G  1 121 ? 79.064  72.992  -26.678 1.00 34.06 ? 94  VAL F CG2 1 
ATOM   7494  N  N   . ALA G  1 122 ? 80.542  71.412  -22.593 1.00 26.67 ? 95  ALA F N   1 
ATOM   7495  C  CA  . ALA G  1 122 ? 80.391  70.953  -21.219 1.00 28.64 ? 95  ALA F CA  1 
ATOM   7496  C  C   . ALA G  1 122 ? 79.720  72.074  -20.436 1.00 35.23 ? 95  ALA F C   1 
ATOM   7497  O  O   . ALA G  1 122 ? 80.316  73.140  -20.232 1.00 33.11 ? 95  ALA F O   1 
ATOM   7498  C  CB  . ALA G  1 122 ? 81.739  70.569  -20.607 1.00 28.14 ? 95  ALA F CB  1 
ATOM   7499  N  N   . ASP G  1 123 ? 78.476  71.850  -20.026 1.00 27.43 ? 96  ASP F N   1 
ATOM   7500  C  CA  . ASP G  1 123 ? 77.818  72.790  -19.132 1.00 30.56 ? 96  ASP F CA  1 
ATOM   7501  C  C   . ASP G  1 123 ? 78.217  72.422  -17.709 1.00 33.32 ? 96  ASP F C   1 
ATOM   7502  O  O   . ASP G  1 123 ? 78.031  71.279  -17.281 1.00 37.87 ? 96  ASP F O   1 
ATOM   7503  C  CB  . ASP G  1 123 ? 76.303  72.755  -19.338 1.00 35.86 ? 96  ASP F CB  1 
ATOM   7504  C  CG  . ASP G  1 123 ? 75.886  73.387  -20.670 1.00 48.28 ? 96  ASP F CG  1 
ATOM   7505  O  OD1 . ASP G  1 123 ? 76.302  74.536  -20.950 1.00 46.97 ? 96  ASP F OD1 1 
ATOM   7506  O  OD2 . ASP G  1 123 ? 75.147  72.732  -21.444 1.00 55.25 ? 96  ASP F OD2 1 
ATOM   7507  N  N   . VAL G  1 124 ? 78.808  73.372  -16.992 1.00 24.56 ? 97  VAL F N   1 
ATOM   7508  C  CA  . VAL G  1 124 ? 79.380  73.117  -15.678 1.00 25.39 ? 97  VAL F CA  1 
ATOM   7509  C  C   . VAL G  1 124 ? 78.419  73.616  -14.612 1.00 28.32 ? 97  VAL F C   1 
ATOM   7510  O  O   . VAL G  1 124 ? 77.943  74.756  -14.672 1.00 27.95 ? 97  VAL F O   1 
ATOM   7511  C  CB  . VAL G  1 124 ? 80.752  73.800  -15.535 1.00 29.15 ? 97  VAL F CB  1 
ATOM   7512  C  CG1 . VAL G  1 124 ? 81.372  73.449  -14.185 1.00 29.54 ? 97  VAL F CG1 1 
ATOM   7513  C  CG2 . VAL G  1 124 ? 81.657  73.388  -16.689 1.00 25.64 ? 97  VAL F CG2 1 
ATOM   7514  N  N   . SER G  1 125 ? 78.142  72.774  -13.627 1.00 30.44 ? 98  SER F N   1 
ATOM   7515  C  CA  . SER G  1 125 ? 77.385  73.223  -12.466 1.00 27.62 ? 98  SER F CA  1 
ATOM   7516  C  C   . SER G  1 125 ? 77.836  72.365  -11.298 1.00 34.04 ? 98  SER F C   1 
ATOM   7517  O  O   . SER G  1 125 ? 77.570  71.158  -11.258 1.00 34.90 ? 98  SER F O   1 
ATOM   7518  C  CB  . SER G  1 125 ? 75.878  73.123  -12.707 1.00 35.23 ? 98  SER F CB  1 
ATOM   7519  O  OG  . SER G  1 125 ? 75.162  73.529  -11.555 1.00 37.03 ? 98  SER F OG  1 
ATOM   7520  N  N   . ILE G  1 126 ? 78.545  72.995  -10.367 1.00 30.29 ? 99  ILE F N   1 
ATOM   7521  C  CA  . ILE G  1 126 ? 79.195  72.325  -9.253  1.00 30.04 ? 99  ILE F CA  1 
ATOM   7522  C  C   . ILE G  1 126 ? 78.945  73.177  -8.022  1.00 34.99 ? 99  ILE F C   1 
ATOM   7523  O  O   . ILE G  1 126 ? 78.858  74.407  -8.104  1.00 35.36 ? 99  ILE F O   1 
ATOM   7524  C  CB  . ILE G  1 126 ? 80.720  72.141  -9.491  1.00 38.03 ? 99  ILE F CB  1 
ATOM   7525  C  CG1 . ILE G  1 126 ? 81.005  71.310  -10.751 1.00 38.51 ? 99  ILE F CG1 1 
ATOM   7526  C  CG2 . ILE G  1 126 ? 81.413  71.546  -8.269  1.00 34.68 ? 99  ILE F CG2 1 
ATOM   7527  C  CD1 . ILE G  1 126 ? 82.501  71.304  -11.158 1.00 34.88 ? 99  ILE F CD1 1 
ATOM   7528  N  N   . GLU G  1 127 ? 78.783  72.513  -6.884  1.00 35.53 ? 100 GLU F N   1 
ATOM   7529  C  CA  . GLU G  1 127 ? 78.829  73.169  -5.588  1.00 38.09 ? 100 GLU F CA  1 
ATOM   7530  C  C   . GLU G  1 127 ? 79.929  72.496  -4.790  1.00 42.14 ? 100 GLU F C   1 
ATOM   7531  O  O   . GLU G  1 127 ? 79.947  71.266  -4.669  1.00 38.56 ? 100 GLU F O   1 
ATOM   7532  C  CB  . GLU G  1 127 ? 77.486  73.093  -4.865  1.00 36.82 ? 100 GLU F CB  1 
ATOM   7533  C  CG  . GLU G  1 127 ? 77.457  73.987  -3.636  1.00 46.91 ? 100 GLU F CG  1 
ATOM   7534  C  CD  . GLU G  1 127 ? 76.059  74.426  -3.260  1.00 61.23 ? 100 GLU F CD  1 
ATOM   7535  O  OE1 . GLU G  1 127 ? 75.457  75.202  -4.041  1.00 57.36 ? 100 GLU F OE1 1 
ATOM   7536  O  OE2 . GLU G  1 127 ? 75.567  73.998  -2.187  1.00 62.30 ? 100 GLU F OE2 1 
ATOM   7537  N  N   . ASP G  1 128 ? 80.873  73.291  -4.292  1.00 34.67 ? 101 ASP F N   1 
ATOM   7538  C  CA  . ASP G  1 128 ? 82.010  72.747  -3.567  1.00 38.94 ? 101 ASP F CA  1 
ATOM   7539  C  C   . ASP G  1 128 ? 82.232  73.564  -2.306  1.00 40.04 ? 101 ASP F C   1 
ATOM   7540  O  O   . ASP G  1 128 ? 82.224  74.798  -2.356  1.00 41.43 ? 101 ASP F O   1 
ATOM   7541  C  CB  . ASP G  1 128 ? 83.276  72.732  -4.431  1.00 35.61 ? 101 ASP F CB  1 
ATOM   7542  C  CG  . ASP G  1 128 ? 84.365  71.862  -3.830  1.00 43.50 ? 101 ASP F CG  1 
ATOM   7543  O  OD1 . ASP G  1 128 ? 84.261  70.623  -3.945  1.00 43.66 ? 101 ASP F OD1 1 
ATOM   7544  O  OD2 . ASP G  1 128 ? 85.303  72.415  -3.208  1.00 43.34 ? 101 ASP F OD2 1 
ATOM   7545  N  N   . SER G  1 129 ? 82.416  72.873  -1.180  1.00 40.20 ? 102 SER F N   1 
ATOM   7546  C  CA  . SER G  1 129 ? 82.610  73.510  0.114   1.00 42.92 ? 102 SER F CA  1 
ATOM   7547  C  C   . SER G  1 129 ? 84.055  73.444  0.601   1.00 40.95 ? 102 SER F C   1 
ATOM   7548  O  O   . SER G  1 129 ? 84.329  73.833  1.742   1.00 47.90 ? 102 SER F O   1 
ATOM   7549  C  CB  . SER G  1 129 ? 81.671  72.886  1.154   1.00 45.05 ? 102 SER F CB  1 
ATOM   7550  O  OG  . SER G  1 129 ? 82.081  71.565  1.485   1.00 50.56 ? 102 SER F OG  1 
ATOM   7551  N  N   . VAL G  1 130 ? 84.979  72.957  -0.225  1.00 36.80 ? 103 VAL F N   1 
ATOM   7552  C  CA  . VAL G  1 130 ? 86.400  72.959  0.122   1.00 37.87 ? 103 VAL F CA  1 
ATOM   7553  C  C   . VAL G  1 130 ? 87.101  74.204  -0.416  1.00 45.64 ? 103 VAL F C   1 
ATOM   7554  O  O   . VAL G  1 130 ? 87.778  74.919  0.328   1.00 48.91 ? 103 VAL F O   1 
ATOM   7555  C  CB  . VAL G  1 130 ? 87.077  71.669  -0.389  1.00 38.27 ? 103 VAL F CB  1 
ATOM   7556  C  CG1 . VAL G  1 130 ? 88.591  71.766  -0.231  1.00 42.72 ? 103 VAL F CG1 1 
ATOM   7557  C  CG2 . VAL G  1 130 ? 86.530  70.458  0.362   1.00 41.78 ? 103 VAL F CG2 1 
ATOM   7558  N  N   . ILE G  1 131 ? 86.954  74.489  -1.714  1.00 42.98 ? 104 ILE F N   1 
ATOM   7559  C  CA  . ILE G  1 131 ? 87.449  75.760  -2.238  1.00 39.17 ? 104 ILE F CA  1 
ATOM   7560  C  C   . ILE G  1 131 ? 86.751  76.921  -1.526  1.00 45.56 ? 104 ILE F C   1 
ATOM   7561  O  O   . ILE G  1 131 ? 85.705  76.763  -0.878  1.00 39.43 ? 104 ILE F O   1 
ATOM   7562  C  CB  . ILE G  1 131 ? 87.251  75.864  -3.760  1.00 33.93 ? 104 ILE F CB  1 
ATOM   7563  C  CG1 . ILE G  1 131 ? 85.760  75.750  -4.099  1.00 36.38 ? 104 ILE F CG1 1 
ATOM   7564  C  CG2 . ILE G  1 131 ? 88.098  74.826  -4.492  1.00 35.61 ? 104 ILE F CG2 1 
ATOM   7565  C  CD1 . ILE G  1 131 ? 85.429  75.992  -5.552  1.00 31.33 ? 104 ILE F CD1 1 
ATOM   7566  N  N   . SER G  1 132 ? 87.353  78.104  -1.644  1.00 39.93 ? 105 SER F N   1 
ATOM   7567  C  CA  . SER G  1 132 ? 86.789  79.319  -1.083  1.00 34.64 ? 105 SER F CA  1 
ATOM   7568  C  C   . SER G  1 132 ? 87.209  80.506  -1.935  1.00 37.67 ? 105 SER F C   1 
ATOM   7569  O  O   . SER G  1 132 ? 88.185  80.445  -2.689  1.00 38.50 ? 105 SER F O   1 
ATOM   7570  C  CB  . SER G  1 132 ? 87.232  79.541  0.368   1.00 39.36 ? 105 SER F CB  1 
ATOM   7571  O  OG  . SER G  1 132 ? 86.341  80.431  1.014   1.00 39.80 ? 105 SER F OG  1 
ATOM   7572  N  N   . LEU G  1 133 ? 86.449  81.591  -1.818  1.00 40.92 ? 106 LEU F N   1 
ATOM   7573  C  CA  . LEU G  1 133 ? 86.872  82.869  -2.370  1.00 41.90 ? 106 LEU F CA  1 
ATOM   7574  C  C   . LEU G  1 133 ? 87.489  83.770  -1.301  1.00 40.95 ? 106 LEU F C   1 
ATOM   7575  O  O   . LEU G  1 133 ? 87.623  84.977  -1.520  1.00 44.37 ? 106 LEU F O   1 
ATOM   7576  C  CB  . LEU G  1 133 ? 85.698  83.564  -3.064  1.00 38.62 ? 106 LEU F CB  1 
ATOM   7577  C  CG  . LEU G  1 133 ? 84.987  82.732  -4.139  1.00 35.70 ? 106 LEU F CG  1 
ATOM   7578  C  CD1 . LEU G  1 133 ? 83.883  83.539  -4.854  1.00 31.75 ? 106 LEU F CD1 1 
ATOM   7579  C  CD2 . LEU G  1 133 ? 85.983  82.143  -5.139  1.00 32.47 ? 106 LEU F CD2 1 
ATOM   7580  N  N   . SER G  1 134 ? 87.886  83.194  -0.163  1.00 45.07 ? 107 SER F N   1 
ATOM   7581  C  CA  . SER G  1 134 ? 88.451  83.930  0.965   1.00 45.10 ? 107 SER F CA  1 
ATOM   7582  C  C   . SER G  1 134 ? 89.278  82.970  1.812   1.00 48.21 ? 107 SER F C   1 
ATOM   7583  O  O   . SER G  1 134 ? 89.067  81.756  1.785   1.00 48.66 ? 107 SER F O   1 
ATOM   7584  C  CB  . SER G  1 134 ? 87.350  84.566  1.820   1.00 44.11 ? 107 SER F CB  1 
ATOM   7585  O  OG  . SER G  1 134 ? 86.934  85.800  1.263   1.00 57.00 ? 107 SER F OG  1 
ATOM   7586  N  N   . GLY G  1 135 ? 90.227  83.530  2.566   1.00 50.97 ? 108 GLY F N   1 
ATOM   7587  C  CA  . GLY G  1 135 ? 90.924  82.757  3.584   1.00 41.18 ? 108 GLY F CA  1 
ATOM   7588  C  C   . GLY G  1 135 ? 91.989  81.815  3.042   1.00 44.99 ? 108 GLY F C   1 
ATOM   7589  O  O   . GLY G  1 135 ? 92.544  82.001  1.953   1.00 52.60 ? 108 GLY F O   1 
ATOM   7590  N  N   . ASP G  1 136 ? 92.266  80.769  3.833   1.00 46.96 ? 109 ASP F N   1 
ATOM   7591  C  CA  . ASP G  1 136 ? 93.374  79.863  3.528   1.00 49.26 ? 109 ASP F CA  1 
ATOM   7592  C  C   . ASP G  1 136 ? 93.151  79.090  2.235   1.00 49.35 ? 109 ASP F C   1 
ATOM   7593  O  O   . ASP G  1 136 ? 94.117  78.787  1.521   1.00 53.47 ? 109 ASP F O   1 
ATOM   7594  C  CB  . ASP G  1 136 ? 93.597  78.878  4.680   1.00 52.24 ? 109 ASP F CB  1 
ATOM   7595  C  CG  . ASP G  1 136 ? 94.147  79.550  5.931   1.00 63.19 ? 109 ASP F CG  1 
ATOM   7596  O  OD1 . ASP G  1 136 ? 94.477  80.757  5.855   1.00 65.77 ? 109 ASP F OD1 1 
ATOM   7597  O  OD2 . ASP G  1 136 ? 94.247  78.875  6.987   1.00 64.56 ? 109 ASP F OD2 1 
ATOM   7598  N  N   . HIS G  1 137 ? 91.905  78.746  1.921   1.00 45.17 ? 110 HIS F N   1 
ATOM   7599  C  CA  . HIS G  1 137 ? 91.608  77.976  0.720   1.00 48.07 ? 110 HIS F CA  1 
ATOM   7600  C  C   . HIS G  1 137 ? 91.229  78.865  -0.457  1.00 43.46 ? 110 HIS F C   1 
ATOM   7601  O  O   . HIS G  1 137 ? 90.718  78.357  -1.463  1.00 44.94 ? 110 HIS F O   1 
ATOM   7602  C  CB  . HIS G  1 137 ? 90.488  76.970  1.002   1.00 52.03 ? 110 HIS F CB  1 
ATOM   7603  C  CG  . HIS G  1 137 ? 90.829  75.961  2.058   1.00 56.23 ? 110 HIS F CG  1 
ATOM   7604  N  ND1 . HIS G  1 137 ? 89.892  75.105  2.601   1.00 59.03 ? 110 HIS F ND1 1 
ATOM   7605  C  CD2 . HIS G  1 137 ? 91.999  75.683  2.683   1.00 51.69 ? 110 HIS F CD2 1 
ATOM   7606  C  CE1 . HIS G  1 137 ? 90.471  74.343  3.513   1.00 55.41 ? 110 HIS F CE1 1 
ATOM   7607  N  NE2 . HIS G  1 137 ? 91.749  74.673  3.581   1.00 56.95 ? 110 HIS F NE2 1 
ATOM   7608  N  N   . CYS G  1 138 ? 91.474  80.175  -0.357  1.00 42.97 ? 111 CYS F N   1 
ATOM   7609  C  CA  . CYS G  1 138 ? 91.063  81.108  -1.400  1.00 41.05 ? 111 CYS F CA  1 
ATOM   7610  C  C   . CYS G  1 138 ? 91.706  80.753  -2.736  1.00 43.33 ? 111 CYS F C   1 
ATOM   7611  O  O   . CYS G  1 138 ? 92.907  80.476  -2.810  1.00 42.05 ? 111 CYS F O   1 
ATOM   7612  C  CB  . CYS G  1 138 ? 91.427  82.540  -0.998  1.00 44.63 ? 111 CYS F CB  1 
ATOM   7613  S  SG  . CYS G  1 138 ? 91.114  83.768  -2.283  1.00 45.33 ? 111 CYS F SG  1 
ATOM   7614  N  N   . ILE G  1 139 ? 90.895  80.759  -3.797  1.00 38.98 ? 112 ILE F N   1 
ATOM   7615  C  CA  . ILE G  1 139 ? 91.344  80.397  -5.140  1.00 32.87 ? 112 ILE F CA  1 
ATOM   7616  C  C   . ILE G  1 139 ? 91.441  81.601  -6.074  1.00 33.00 ? 112 ILE F C   1 
ATOM   7617  O  O   . ILE G  1 139 ? 91.835  81.433  -7.240  1.00 33.09 ? 112 ILE F O   1 
ATOM   7618  C  CB  . ILE G  1 139 ? 90.440  79.305  -5.751  1.00 36.53 ? 112 ILE F CB  1 
ATOM   7619  C  CG1 . ILE G  1 139 ? 88.992  79.785  -5.848  1.00 33.87 ? 112 ILE F CG1 1 
ATOM   7620  C  CG2 . ILE G  1 139 ? 90.473  78.039  -4.894  1.00 37.30 ? 112 ILE F CG2 1 
ATOM   7621  C  CD1 . ILE G  1 139 ? 88.124  78.875  -6.696  1.00 33.65 ? 112 ILE F CD1 1 
ATOM   7622  N  N   . ILE G  1 140 ? 91.088  82.807  -5.608  1.00 37.15 ? 113 ILE F N   1 
ATOM   7623  C  CA  . ILE G  1 140 ? 91.304  84.015  -6.404  1.00 31.57 ? 113 ILE F CA  1 
ATOM   7624  C  C   . ILE G  1 140 ? 92.786  84.150  -6.697  1.00 36.58 ? 113 ILE F C   1 
ATOM   7625  O  O   . ILE G  1 140 ? 93.628  83.955  -5.812  1.00 44.73 ? 113 ILE F O   1 
ATOM   7626  C  CB  . ILE G  1 140 ? 90.805  85.275  -5.676  1.00 39.57 ? 113 ILE F CB  1 
ATOM   7627  C  CG1 . ILE G  1 140 ? 89.408  85.080  -5.070  1.00 37.11 ? 113 ILE F CG1 1 
ATOM   7628  C  CG2 . ILE G  1 140 ? 90.879  86.499  -6.602  1.00 35.40 ? 113 ILE F CG2 1 
ATOM   7629  C  CD1 . ILE G  1 140 ? 88.327  84.941  -6.065  1.00 37.34 ? 113 ILE F CD1 1 
ATOM   7630  N  N   . GLY G  1 141 ? 93.117  84.485  -7.944  1.00 33.80 ? 114 GLY F N   1 
ATOM   7631  C  CA  . GLY G  1 141 ? 94.504  84.620  -8.327  1.00 36.12 ? 114 GLY F CA  1 
ATOM   7632  C  C   . GLY G  1 141 ? 95.201  83.319  -8.653  1.00 44.16 ? 114 GLY F C   1 
ATOM   7633  O  O   . GLY G  1 141 ? 96.388  83.338  -9.005  1.00 38.63 ? 114 GLY F O   1 
ATOM   7634  N  N   . ARG G  1 142 ? 94.514  82.191  -8.542  1.00 34.01 ? 115 ARG F N   1 
ATOM   7635  C  CA  . ARG G  1 142 ? 95.052  80.926  -8.994  1.00 32.50 ? 115 ARG F CA  1 
ATOM   7636  C  C   . ARG G  1 142 ? 94.439  80.603  -10.357 1.00 34.58 ? 115 ARG F C   1 
ATOM   7637  O  O   . ARG G  1 142 ? 93.659  81.385  -10.908 1.00 38.30 ? 115 ARG F O   1 
ATOM   7638  C  CB  . ARG G  1 142 ? 94.795  79.858  -7.934  1.00 34.74 ? 115 ARG F CB  1 
ATOM   7639  C  CG  . ARG G  1 142 ? 95.073  80.384  -6.522  1.00 37.58 ? 115 ARG F CG  1 
ATOM   7640  C  CD  . ARG G  1 142 ? 95.433  79.285  -5.557  1.00 37.21 ? 115 ARG F CD  1 
ATOM   7641  N  NE  . ARG G  1 142 ? 95.678  79.789  -4.210  1.00 37.48 ? 115 ARG F NE  1 
ATOM   7642  C  CZ  . ARG G  1 142 ? 96.883  80.005  -3.691  1.00 38.14 ? 115 ARG F CZ  1 
ATOM   7643  N  NH1 . ARG G  1 142 ? 97.988  79.745  -4.372  1.00 40.63 ? 115 ARG F NH1 1 
ATOM   7644  N  NH2 . ARG G  1 142 ? 96.980  80.482  -2.452  1.00 38.76 ? 115 ARG F NH2 1 
ATOM   7645  N  N   . THR G  1 143 ? 94.801  79.448  -10.918 1.00 35.45 ? 116 THR F N   1 
ATOM   7646  C  CA  . THR G  1 143 ? 94.439  79.107  -12.287 1.00 38.09 ? 116 THR F CA  1 
ATOM   7647  C  C   . THR G  1 143 ? 93.450  77.946  -12.296 1.00 36.52 ? 116 THR F C   1 
ATOM   7648  O  O   . THR G  1 143 ? 93.615  76.974  -11.556 1.00 35.60 ? 116 THR F O   1 
ATOM   7649  C  CB  . THR G  1 143 ? 95.681  78.745  -13.114 1.00 35.28 ? 116 THR F CB  1 
ATOM   7650  O  OG1 . THR G  1 143 ? 96.433  79.932  -13.409 1.00 40.59 ? 116 THR F OG1 1 
ATOM   7651  C  CG2 . THR G  1 143 ? 95.275  78.144  -14.446 1.00 36.61 ? 116 THR F CG2 1 
ATOM   7652  N  N   . LEU G  1 144 ? 92.423  78.052  -13.137 1.00 35.40 ? 117 LEU F N   1 
ATOM   7653  C  CA  . LEU G  1 144 ? 91.485  76.962  -13.373 1.00 30.97 ? 117 LEU F CA  1 
ATOM   7654  C  C   . LEU G  1 144 ? 91.867  76.285  -14.684 1.00 35.84 ? 117 LEU F C   1 
ATOM   7655  O  O   . LEU G  1 144 ? 92.082  76.963  -15.693 1.00 32.21 ? 117 LEU F O   1 
ATOM   7656  C  CB  . LEU G  1 144 ? 90.048  77.493  -13.422 1.00 30.61 ? 117 LEU F CB  1 
ATOM   7657  C  CG  . LEU G  1 144 ? 88.872  76.516  -13.536 1.00 35.18 ? 117 LEU F CG  1 
ATOM   7658  C  CD1 . LEU G  1 144 ? 88.697  75.708  -12.253 1.00 31.78 ? 117 LEU F CD1 1 
ATOM   7659  C  CD2 . LEU G  1 144 ? 87.588  77.267  -13.872 1.00 33.79 ? 117 LEU F CD2 1 
ATOM   7660  N  N   . VAL G  1 145 ? 91.973  74.954  -14.673 1.00 29.84 ? 118 VAL F N   1 
ATOM   7661  C  CA  . VAL G  1 145 ? 92.430  74.210  -15.842 1.00 31.53 ? 118 VAL F CA  1 
ATOM   7662  C  C   . VAL G  1 145 ? 91.417  73.119  -16.180 1.00 32.01 ? 118 VAL F C   1 
ATOM   7663  O  O   . VAL G  1 145 ? 90.929  72.414  -15.289 1.00 33.21 ? 118 VAL F O   1 
ATOM   7664  C  CB  . VAL G  1 145 ? 93.826  73.589  -15.607 1.00 33.74 ? 118 VAL F CB  1 
ATOM   7665  C  CG1 . VAL G  1 145 ? 94.305  72.835  -16.856 1.00 31.75 ? 118 VAL F CG1 1 
ATOM   7666  C  CG2 . VAL G  1 145 ? 94.834  74.660  -15.195 1.00 35.87 ? 118 VAL F CG2 1 
ATOM   7667  N  N   . VAL G  1 146 ? 91.106  72.982  -17.465 1.00 27.88 ? 119 VAL F N   1 
ATOM   7668  C  CA  . VAL G  1 146 ? 90.343  71.844  -17.969 1.00 32.87 ? 119 VAL F CA  1 
ATOM   7669  C  C   . VAL G  1 146 ? 91.323  70.934  -18.703 1.00 32.06 ? 119 VAL F C   1 
ATOM   7670  O  O   . VAL G  1 146 ? 92.095  71.399  -19.550 1.00 33.44 ? 119 VAL F O   1 
ATOM   7671  C  CB  . VAL G  1 146 ? 89.167  72.278  -18.868 1.00 33.18 ? 119 VAL F CB  1 
ATOM   7672  C  CG1 . VAL G  1 146 ? 89.625  73.144  -20.054 1.00 29.47 ? 119 VAL F CG1 1 
ATOM   7673  C  CG2 . VAL G  1 146 ? 88.357  71.049  -19.353 1.00 32.67 ? 119 VAL F CG2 1 
ATOM   7674  N  N   . HIS G  1 147 ? 91.306  69.647  -18.365 1.00 35.00 ? 120 HIS F N   1 
ATOM   7675  C  CA  . HIS G  1 147 ? 92.331  68.709  -18.811 1.00 35.67 ? 120 HIS F CA  1 
ATOM   7676  C  C   . HIS G  1 147 ? 91.860  67.836  -19.979 1.00 38.57 ? 120 HIS F C   1 
ATOM   7677  O  O   . HIS G  1 147 ? 90.676  67.777  -20.336 1.00 34.62 ? 120 HIS F O   1 
ATOM   7678  C  CB  . HIS G  1 147 ? 92.779  67.827  -17.649 1.00 32.14 ? 120 HIS F CB  1 
ATOM   7679  C  CG  . HIS G  1 147 ? 93.605  68.542  -16.626 1.00 38.83 ? 120 HIS F CG  1 
ATOM   7680  N  ND1 . HIS G  1 147 ? 94.982  68.601  -16.691 1.00 42.16 ? 120 HIS F ND1 1 
ATOM   7681  C  CD2 . HIS G  1 147 ? 93.251  69.229  -15.515 1.00 37.47 ? 120 HIS F CD2 1 
ATOM   7682  C  CE1 . HIS G  1 147 ? 95.440  69.294  -15.662 1.00 38.95 ? 120 HIS F CE1 1 
ATOM   7683  N  NE2 . HIS G  1 147 ? 94.411  69.679  -14.928 1.00 43.96 ? 120 HIS F NE2 1 
ATOM   7684  N  N   . GLU G  1 148 ? 92.831  67.126  -20.560 1.00 36.19 ? 121 GLU F N   1 
ATOM   7685  C  CA  . GLU G  1 148 ? 92.612  66.379  -21.796 1.00 35.94 ? 121 GLU F CA  1 
ATOM   7686  C  C   . GLU G  1 148 ? 91.729  65.154  -21.577 1.00 34.58 ? 121 GLU F C   1 
ATOM   7687  O  O   . GLU G  1 148 ? 90.947  64.780  -22.463 1.00 38.28 ? 121 GLU F O   1 
ATOM   7688  C  CB  . GLU G  1 148 ? 93.965  65.954  -22.367 1.00 42.31 ? 121 GLU F CB  1 
ATOM   7689  C  CG  . GLU G  1 148 ? 93.911  65.189  -23.678 1.00 42.95 ? 121 GLU F CG  1 
ATOM   7690  C  CD  . GLU G  1 148 ? 95.225  64.451  -23.981 1.00 60.03 ? 121 GLU F CD  1 
ATOM   7691  O  OE1 . GLU G  1 148 ? 96.101  64.369  -23.081 1.00 50.96 ? 121 GLU F OE1 1 
ATOM   7692  O  OE2 . GLU G  1 148 ? 95.371  63.945  -25.120 1.00 55.72 ? 121 GLU F OE2 1 
ATOM   7693  N  N   . LYS G  1 149 ? 91.854  64.516  -20.418 1.00 36.27 ? 122 LYS F N   1 
ATOM   7694  C  CA  . LYS G  1 149 ? 91.289  63.205  -20.137 1.00 39.10 ? 122 LYS F CA  1 
ATOM   7695  C  C   . LYS G  1 149 ? 90.576  63.215  -18.796 1.00 40.11 ? 122 LYS F C   1 
ATOM   7696  O  O   . LYS G  1 149 ? 90.726  64.133  -17.984 1.00 39.52 ? 122 LYS F O   1 
ATOM   7697  C  CB  . LYS G  1 149 ? 92.372  62.096  -20.146 1.00 41.27 ? 122 LYS F CB  1 
ATOM   7698  C  CG  . LYS G  1 149 ? 93.321  62.124  -21.363 1.00 49.05 ? 122 LYS F CG  1 
ATOM   7699  C  CD  . LYS G  1 149 ? 94.421  61.036  -21.343 1.00 46.94 ? 122 LYS F CD  1 
ATOM   7700  C  CE  . LYS G  1 149 ? 95.586  61.352  -20.388 1.00 51.31 ? 122 LYS F CE  1 
ATOM   7701  N  NZ  . LYS G  1 149 ? 95.254  61.258  -18.945 1.00 50.62 ? 122 LYS F NZ  1 
ATOM   7702  N  N   . ALA G  1 150 ? 89.803  62.153  -18.572 1.00 33.94 ? 123 ALA F N   1 
ATOM   7703  C  CA  . ALA G  1 150 ? 89.065  62.014  -17.330 1.00 34.64 ? 123 ALA F CA  1 
ATOM   7704  C  C   . ALA G  1 150 ? 90.012  61.948  -16.139 1.00 37.38 ? 123 ALA F C   1 
ATOM   7705  O  O   . ALA G  1 150 ? 91.092  61.353  -16.200 1.00 42.72 ? 123 ALA F O   1 
ATOM   7706  C  CB  . ALA G  1 150 ? 88.187  60.762  -17.376 1.00 35.73 ? 123 ALA F CB  1 
ATOM   7707  N  N   . ASP G  1 151 ? 89.600  62.588  -15.061 1.00 36.52 ? 124 ASP F N   1 
ATOM   7708  C  CA  . ASP G  1 151 ? 90.230  62.435  -13.763 1.00 40.31 ? 124 ASP F CA  1 
ATOM   7709  C  C   . ASP G  1 151 ? 89.753  61.112  -13.168 1.00 45.25 ? 124 ASP F C   1 
ATOM   7710  O  O   . ASP G  1 151 ? 88.545  60.915  -12.984 1.00 40.96 ? 124 ASP F O   1 
ATOM   7711  C  CB  . ASP G  1 151 ? 89.834  63.631  -12.899 1.00 42.43 ? 124 ASP F CB  1 
ATOM   7712  C  CG  . ASP G  1 151 ? 90.493  63.654  -11.531 1.00 45.62 ? 124 ASP F CG  1 
ATOM   7713  O  OD1 . ASP G  1 151 ? 90.993  62.616  -11.045 1.00 44.66 ? 124 ASP F OD1 1 
ATOM   7714  O  OD2 . ASP G  1 151 ? 90.466  64.746  -10.918 1.00 44.71 ? 124 ASP F OD2 1 
ATOM   7715  N  N   . ASP G  1 152 ? 90.688  60.193  -12.889 1.00 45.06 ? 125 ASP F N   1 
ATOM   7716  C  CA  . ASP G  1 152 ? 90.306  58.940  -12.240 1.00 39.57 ? 125 ASP F CA  1 
ATOM   7717  C  C   . ASP G  1 152 ? 90.025  59.120  -10.759 1.00 44.04 ? 125 ASP F C   1 
ATOM   7718  O  O   . ASP G  1 152 ? 89.750  58.126  -10.072 1.00 47.74 ? 125 ASP F O   1 
ATOM   7719  C  CB  . ASP G  1 152 ? 91.376  57.848  -12.446 1.00 42.26 ? 125 ASP F CB  1 
ATOM   7720  C  CG  . ASP G  1 152 ? 92.734  58.207  -11.841 1.00 43.89 ? 125 ASP F CG  1 
ATOM   7721  O  OD1 . ASP G  1 152 ? 92.784  58.778  -10.729 1.00 45.17 ? 125 ASP F OD1 1 
ATOM   7722  O  OD2 . ASP G  1 152 ? 93.761  57.884  -12.478 1.00 46.26 ? 125 ASP F OD2 1 
ATOM   7723  N  N   . LEU G  1 153 ? 90.097  60.358  -10.259 1.00 41.08 ? 126 LEU F N   1 
ATOM   7724  C  CA  . LEU G  1 153 ? 89.737  60.699  -8.884  1.00 37.21 ? 126 LEU F CA  1 
ATOM   7725  C  C   . LEU G  1 153 ? 90.609  59.980  -7.851  1.00 43.58 ? 126 LEU F C   1 
ATOM   7726  O  O   . LEU G  1 153 ? 90.152  59.667  -6.748  1.00 45.36 ? 126 LEU F O   1 
ATOM   7727  C  CB  . LEU G  1 153 ? 88.247  60.450  -8.619  1.00 41.06 ? 126 LEU F CB  1 
ATOM   7728  C  CG  . LEU G  1 153 ? 87.249  60.733  -9.746  1.00 44.79 ? 126 LEU F CG  1 
ATOM   7729  C  CD1 . LEU G  1 153 ? 85.832  60.683  -9.206  1.00 44.38 ? 126 LEU F CD1 1 
ATOM   7730  C  CD2 . LEU G  1 153 ? 87.501  62.135  -10.288 1.00 41.92 ? 126 LEU F CD2 1 
ATOM   7731  N  N   . GLY G  1 154 ? 91.880  59.757  -8.175  1.00 50.34 ? 127 GLY F N   1 
ATOM   7732  C  CA  . GLY G  1 154 ? 92.780  59.121  -7.226  1.00 52.23 ? 127 GLY F CA  1 
ATOM   7733  C  C   . GLY G  1 154 ? 92.525  57.643  -7.035  1.00 53.45 ? 127 GLY F C   1 
ATOM   7734  O  O   . GLY G  1 154 ? 92.811  57.097  -5.961  1.00 55.03 ? 127 GLY F O   1 
ATOM   7735  N  N   . LYS G  1 155 ? 91.982  56.980  -8.054  1.00 50.37 ? 128 LYS F N   1 
ATOM   7736  C  CA  . LYS G  1 155 ? 91.593  55.578  -7.990  1.00 47.76 ? 128 LYS F CA  1 
ATOM   7737  C  C   . LYS G  1 155 ? 92.093  54.835  -9.219  1.00 51.60 ? 128 LYS F C   1 
ATOM   7738  O  O   . LYS G  1 155 ? 91.429  53.918  -9.708  1.00 57.44 ? 128 LYS F O   1 
ATOM   7739  C  CB  . LYS G  1 155 ? 90.076  55.446  -7.874  1.00 45.56 ? 128 LYS F CB  1 
ATOM   7740  C  CG  . LYS G  1 155 ? 89.520  55.872  -6.531  1.00 50.48 ? 128 LYS F CG  1 
ATOM   7741  C  CD  . LYS G  1 155 ? 88.101  56.407  -6.693  1.00 45.90 ? 128 LYS F CD  1 
ATOM   7742  C  CE  . LYS G  1 155 ? 87.539  56.934  -5.374  1.00 49.96 ? 128 LYS F CE  1 
ATOM   7743  N  NZ  . LYS G  1 155 ? 88.581  57.099  -4.316  1.00 56.38 ? 128 LYS F NZ  1 
ATOM   7744  N  N   . GLY G  1 156 ? 93.244  55.248  -9.753  1.00 46.74 ? 129 GLY F N   1 
ATOM   7745  C  CA  . GLY G  1 156 ? 93.837  54.605  -10.910 1.00 49.35 ? 129 GLY F CA  1 
ATOM   7746  C  C   . GLY G  1 156 ? 94.871  53.543  -10.604 1.00 51.35 ? 129 GLY F C   1 
ATOM   7747  O  O   . GLY G  1 156 ? 95.325  52.849  -11.520 1.00 52.43 ? 129 GLY F O   1 
ATOM   7748  N  N   . GLY G  1 157 ? 95.264  53.408  -9.337  1.00 52.18 ? 130 GLY F N   1 
ATOM   7749  C  CA  . GLY G  1 157 ? 96.196  52.369  -8.942  1.00 58.40 ? 130 GLY F CA  1 
ATOM   7750  C  C   . GLY G  1 157 ? 97.636  52.593  -9.352  1.00 62.69 ? 130 GLY F C   1 
ATOM   7751  O  O   . GLY G  1 157 ? 98.400  51.627  -9.444  1.00 64.53 ? 130 GLY F O   1 
ATOM   7752  N  N   . ASN G  1 158 ? 98.038  53.837  -9.607  1.00 56.77 ? 131 ASN F N   1 
ATOM   7753  C  CA  . ASN G  1 158 ? 99.426  54.148  -9.919  1.00 50.99 ? 131 ASN F CA  1 
ATOM   7754  C  C   . ASN G  1 158 ? 99.814  55.413  -9.164  1.00 60.15 ? 131 ASN F C   1 
ATOM   7755  O  O   . ASN G  1 158 ? 98.987  56.024  -8.475  1.00 62.85 ? 131 ASN F O   1 
ATOM   7756  C  CB  . ASN G  1 158 ? 99.640  54.250  -11.439 1.00 50.71 ? 131 ASN F CB  1 
ATOM   7757  C  CG  . ASN G  1 158 ? 98.820  55.362  -12.090 1.00 56.26 ? 131 ASN F CG  1 
ATOM   7758  O  OD1 . ASN G  1 158 ? 98.285  56.241  -11.416 1.00 57.15 ? 131 ASN F OD1 1 
ATOM   7759  N  ND2 . ASN G  1 158 ? 98.729  55.323  -13.417 1.00 51.23 ? 131 ASN F ND2 1 
ATOM   7760  N  N   . GLU G  1 159 ? 101.092 55.797  -9.267  1.00 60.08 ? 132 GLU F N   1 
ATOM   7761  C  CA  . GLU G  1 159 ? 101.537 57.004  -8.574  1.00 57.97 ? 132 GLU F CA  1 
ATOM   7762  C  C   . GLU G  1 159 ? 100.903 58.247  -9.182  1.00 48.92 ? 132 GLU F C   1 
ATOM   7763  O  O   . GLU G  1 159 ? 100.566 59.195  -8.462  1.00 50.19 ? 132 GLU F O   1 
ATOM   7764  C  CB  . GLU G  1 159 ? 103.061 57.132  -8.615  1.00 49.60 ? 132 GLU F CB  1 
ATOM   7765  C  CG  . GLU G  1 159 ? 103.557 58.349  -7.829  1.00 61.07 ? 132 GLU F CG  1 
ATOM   7766  C  CD  . GLU G  1 159 ? 105.069 58.495  -7.813  1.00 70.90 ? 132 GLU F CD  1 
ATOM   7767  O  OE1 . GLU G  1 159 ? 105.762 57.667  -8.448  1.00 75.16 ? 132 GLU F OE1 1 
ATOM   7768  O  OE2 . GLU G  1 159 ? 105.559 59.449  -7.162  1.00 68.83 ? 132 GLU F OE2 1 
ATOM   7769  N  N   . GLU G  1 160 ? 100.748 58.258  -10.509 1.00 53.41 ? 133 GLU F N   1 
ATOM   7770  C  CA  . GLU G  1 160 ? 100.208 59.422  -11.203 1.00 55.32 ? 133 GLU F CA  1 
ATOM   7771  C  C   . GLU G  1 160 ? 98.822  59.783  -10.675 1.00 54.71 ? 133 GLU F C   1 
ATOM   7772  O  O   . GLU G  1 160 ? 98.534  60.953  -10.394 1.00 53.27 ? 133 GLU F O   1 
ATOM   7773  C  CB  . GLU G  1 160 ? 100.173 59.139  -12.708 1.00 46.36 ? 133 GLU F CB  1 
ATOM   7774  C  CG  . GLU G  1 160 ? 100.323 60.363  -13.603 1.00 53.59 ? 133 GLU F CG  1 
ATOM   7775  C  CD  . GLU G  1 160 ? 101.295 61.392  -13.045 1.00 65.95 ? 133 GLU F CD  1 
ATOM   7776  O  OE1 . GLU G  1 160 ? 102.515 61.112  -13.000 1.00 64.03 ? 133 GLU F OE1 1 
ATOM   7777  O  OE2 . GLU G  1 160 ? 100.839 62.488  -12.661 1.00 65.07 ? 133 GLU F OE2 1 
ATOM   7778  N  N   . SER G  1 161 ? 97.961  58.776  -10.499 1.00 50.46 ? 134 SER F N   1 
ATOM   7779  C  CA  . SER G  1 161 ? 96.596  59.007  -10.037 1.00 55.62 ? 134 SER F CA  1 
ATOM   7780  C  C   . SER G  1 161 ? 96.565  59.646  -8.652  1.00 54.64 ? 134 SER F C   1 
ATOM   7781  O  O   . SER G  1 161 ? 95.588  60.326  -8.311  1.00 48.88 ? 134 SER F O   1 
ATOM   7782  C  CB  . SER G  1 161 ? 95.820  57.681  -10.068 1.00 46.02 ? 134 SER F CB  1 
ATOM   7783  O  OG  . SER G  1 161 ? 94.783  57.625  -9.105  1.00 51.57 ? 134 SER F OG  1 
ATOM   7784  N  N   . THR G  1 162 ? 97.628  59.467  -7.864  1.00 50.15 ? 135 THR F N   1 
ATOM   7785  C  CA  . THR G  1 162 ? 97.763  60.085  -6.549  1.00 48.28 ? 135 THR F CA  1 
ATOM   7786  C  C   . THR G  1 162 ? 98.146  61.567  -6.632  1.00 50.28 ? 135 THR F C   1 
ATOM   7787  O  O   . THR G  1 162 ? 97.908  62.317  -5.673  1.00 46.36 ? 135 THR F O   1 
ATOM   7788  C  CB  . THR G  1 162 ? 98.785  59.268  -5.734  1.00 53.39 ? 135 THR F CB  1 
ATOM   7789  O  OG1 . THR G  1 162 ? 98.100  58.264  -4.970  1.00 61.82 ? 135 THR F OG1 1 
ATOM   7790  C  CG2 . THR G  1 162 ? 99.644  60.127  -4.793  1.00 54.85 ? 135 THR F CG2 1 
ATOM   7791  N  N   . LYS G  1 163 ? 98.693  62.012  -7.766  1.00 50.80 ? 136 LYS F N   1 
ATOM   7792  C  CA  . LYS G  1 163 ? 99.088  63.404  -7.964  1.00 46.80 ? 136 LYS F CA  1 
ATOM   7793  C  C   . LYS G  1 163 ? 98.117  64.153  -8.871  1.00 46.17 ? 136 LYS F C   1 
ATOM   7794  O  O   . LYS G  1 163 ? 97.494  65.127  -8.444  1.00 51.65 ? 136 LYS F O   1 
ATOM   7795  C  CB  . LYS G  1 163 ? 100.512 63.475  -8.547  1.00 49.16 ? 136 LYS F CB  1 
ATOM   7796  C  CG  . LYS G  1 163 ? 101.531 62.517  -7.899  1.00 54.07 ? 136 LYS F CG  1 
ATOM   7797  C  CD  . LYS G  1 163 ? 102.385 63.197  -6.830  1.00 50.52 ? 136 LYS F CD  1 
ATOM   7798  C  CE  . LYS G  1 163 ? 101.649 63.263  -5.486  1.00 58.96 ? 136 LYS F CE  1 
ATOM   7799  N  NZ  . LYS G  1 163 ? 102.537 63.535  -4.311  1.00 55.70 ? 136 LYS F NZ  1 
ATOM   7800  N  N   . THR G  1 164 ? 97.966  63.715  -10.120 1.00 47.02 ? 137 THR F N   1 
ATOM   7801  C  CA  . THR G  1 164 ? 97.127  64.386  -11.104 1.00 48.61 ? 137 THR F CA  1 
ATOM   7802  C  C   . THR G  1 164 ? 95.851  63.629  -11.452 1.00 53.37 ? 137 THR F C   1 
ATOM   7803  O  O   . THR G  1 164 ? 95.058  64.120  -12.269 1.00 43.81 ? 137 THR F O   1 
ATOM   7804  C  CB  . THR G  1 164 ? 97.931  64.647  -12.385 1.00 51.58 ? 137 THR F CB  1 
ATOM   7805  O  OG1 . THR G  1 164 ? 97.902  63.485  -13.237 1.00 51.90 ? 137 THR F OG1 1 
ATOM   7806  C  CG2 . THR G  1 164 ? 99.369  65.058  -12.063 1.00 49.25 ? 137 THR F CG2 1 
ATOM   7807  N  N   . GLY G  1 165 ? 95.629  62.450  -10.872 1.00 56.03 ? 138 GLY F N   1 
ATOM   7808  C  CA  . GLY G  1 165 ? 94.466  61.656  -11.226 1.00 47.25 ? 138 GLY F CA  1 
ATOM   7809  C  C   . GLY G  1 165 ? 94.487  61.216  -12.673 1.00 45.70 ? 138 GLY F C   1 
ATOM   7810  O  O   . GLY G  1 165 ? 93.459  60.802  -13.223 1.00 49.20 ? 138 GLY F O   1 
ATOM   7811  N  N   . ASN G  1 166 ? 95.664  61.326  -13.303 1.00 48.95 ? 139 ASN F N   1 
ATOM   7812  C  CA  . ASN G  1 166 ? 95.905  60.897  -14.680 1.00 40.95 ? 139 ASN F CA  1 
ATOM   7813  C  C   . ASN G  1 166 ? 95.088  61.682  -15.704 1.00 49.31 ? 139 ASN F C   1 
ATOM   7814  O  O   . ASN G  1 166 ? 94.743  61.147  -16.762 1.00 44.95 ? 139 ASN F O   1 
ATOM   7815  C  CB  . ASN G  1 166 ? 95.644  59.396  -14.854 1.00 48.37 ? 139 ASN F CB  1 
ATOM   7816  C  CG  . ASN G  1 166 ? 96.731  58.547  -14.244 1.00 51.14 ? 139 ASN F CG  1 
ATOM   7817  O  OD1 . ASN G  1 166 ? 96.575  58.014  -13.141 1.00 48.65 ? 139 ASN F OD1 1 
ATOM   7818  N  ND2 . ASN G  1 166 ? 97.855  58.428  -14.953 1.00 50.66 ? 139 ASN F ND2 1 
ATOM   7819  N  N   . ALA G  1 167 ? 94.796  62.958  -15.433 1.00 45.12 ? 140 ALA F N   1 
ATOM   7820  C  CA  . ALA G  1 167 ? 93.949  63.730  -16.337 1.00 41.04 ? 140 ALA F CA  1 
ATOM   7821  C  C   . ALA G  1 167 ? 94.685  64.238  -17.577 1.00 45.91 ? 140 ALA F C   1 
ATOM   7822  O  O   . ALA G  1 167 ? 94.039  64.784  -18.481 1.00 40.34 ? 140 ALA F O   1 
ATOM   7823  C  CB  . ALA G  1 167 ? 93.310  64.898  -15.579 1.00 38.24 ? 140 ALA F CB  1 
ATOM   7824  N  N   . GLY G  1 168 ? 96.006  64.076  -17.657 1.00 43.28 ? 141 GLY F N   1 
ATOM   7825  C  CA  . GLY G  1 168 ? 96.702  64.380  -18.896 1.00 36.58 ? 141 GLY F CA  1 
ATOM   7826  C  C   . GLY G  1 168 ? 96.935  65.867  -19.128 1.00 34.01 ? 141 GLY F C   1 
ATOM   7827  O  O   . GLY G  1 168 ? 96.985  66.674  -18.198 1.00 42.20 ? 141 GLY F O   1 
ATOM   7828  N  N   . SER G  1 169 ? 97.060  66.227  -20.404 1.00 39.81 ? 142 SER F N   1 
ATOM   7829  C  CA  . SER G  1 169 ? 97.523  67.556  -20.776 1.00 43.30 ? 142 SER F CA  1 
ATOM   7830  C  C   . SER G  1 169 ? 96.470  68.621  -20.445 1.00 47.71 ? 142 SER F C   1 
ATOM   7831  O  O   . SER G  1 169 ? 95.301  68.328  -20.163 1.00 37.97 ? 142 SER F O   1 
ATOM   7832  C  CB  . SER G  1 169 ? 97.895  67.589  -22.259 1.00 41.84 ? 142 SER F CB  1 
ATOM   7833  O  OG  . SER G  1 169 ? 96.822  68.056  -23.059 1.00 49.88 ? 142 SER F OG  1 
ATOM   7834  N  N   . ARG G  1 170 ? 96.911  69.880  -20.483 1.00 43.75 ? 143 ARG F N   1 
ATOM   7835  C  CA  . ARG G  1 170 ? 96.093  71.025  -20.099 1.00 41.77 ? 143 ARG F CA  1 
ATOM   7836  C  C   . ARG G  1 170 ? 95.573  71.692  -21.369 1.00 44.25 ? 143 ARG F C   1 
ATOM   7837  O  O   . ARG G  1 170 ? 96.348  72.260  -22.145 1.00 44.82 ? 143 ARG F O   1 
ATOM   7838  C  CB  . ARG G  1 170 ? 96.907  71.987  -19.233 1.00 37.10 ? 143 ARG F CB  1 
ATOM   7839  C  CG  . ARG G  1 170 ? 97.784  71.256  -18.222 1.00 36.13 ? 143 ARG F CG  1 
ATOM   7840  C  CD  . ARG G  1 170 ? 98.486  72.189  -17.235 1.00 41.73 ? 143 ARG F CD  1 
ATOM   7841  N  NE  . ARG G  1 170 ? 99.083  71.437  -16.136 1.00 40.07 ? 143 ARG F NE  1 
ATOM   7842  C  CZ  . ARG G  1 170 ? 99.744  71.973  -15.119 1.00 45.85 ? 143 ARG F CZ  1 
ATOM   7843  N  NH1 . ARG G  1 170 ? 99.954  73.279  -15.041 1.00 47.95 ? 143 ARG F NH1 1 
ATOM   7844  N  NH2 . ARG G  1 170 ? 100.190 71.182  -14.146 1.00 43.17 ? 143 ARG F NH2 1 
ATOM   7845  N  N   . LEU G  1 171 ? 94.256  71.615  -21.585 1.00 40.18 ? 144 LEU F N   1 
ATOM   7846  C  CA  . LEU G  1 171 ? 93.675  72.112  -22.827 1.00 35.37 ? 144 LEU F CA  1 
ATOM   7847  C  C   . LEU G  1 171 ? 93.448  73.620  -22.777 1.00 34.99 ? 144 LEU F C   1 
ATOM   7848  O  O   . LEU G  1 171 ? 93.636  74.307  -23.786 1.00 35.82 ? 144 LEU F O   1 
ATOM   7849  C  CB  . LEU G  1 171 ? 92.355  71.391  -23.114 1.00 37.60 ? 144 LEU F CB  1 
ATOM   7850  C  CG  . LEU G  1 171 ? 92.353  69.854  -23.127 1.00 38.71 ? 144 LEU F CG  1 
ATOM   7851  C  CD1 . LEU G  1 171 ? 90.927  69.313  -23.261 1.00 37.55 ? 144 LEU F CD1 1 
ATOM   7852  C  CD2 . LEU G  1 171 ? 93.240  69.315  -24.235 1.00 35.57 ? 144 LEU F CD2 1 
ATOM   7853  N  N   . ALA G  1 172 ? 93.032  74.145  -21.622 1.00 36.99 ? 145 ALA F N   1 
ATOM   7854  C  CA  . ALA G  1 172 ? 92.721  75.563  -21.495 1.00 33.72 ? 145 ALA F CA  1 
ATOM   7855  C  C   . ALA G  1 172 ? 92.766  75.952  -20.027 1.00 36.06 ? 145 ALA F C   1 
ATOM   7856  O  O   . ALA G  1 172 ? 92.534  75.120  -19.144 1.00 34.83 ? 145 ALA F O   1 
ATOM   7857  C  CB  . ALA G  1 172 ? 91.350  75.898  -22.096 1.00 36.95 ? 145 ALA F CB  1 
ATOM   7858  N  N   . CYS G  1 173 ? 93.069  77.224  -19.772 1.00 29.33 ? 146 CYS F N   1 
ATOM   7859  C  CA  . CYS G  1 173 ? 93.207  77.696  -18.403 1.00 31.40 ? 146 CYS F CA  1 
ATOM   7860  C  C   . CYS G  1 173 ? 92.933  79.195  -18.354 1.00 30.99 ? 146 CYS F C   1 
ATOM   7861  O  O   . CYS G  1 173 ? 92.890  79.878  -19.378 1.00 32.33 ? 146 CYS F O   1 
ATOM   7862  C  CB  . CYS G  1 173 ? 94.606  77.416  -17.843 1.00 38.50 ? 146 CYS F CB  1 
ATOM   7863  S  SG  . CYS G  1 173 ? 95.935  77.988  -18.924 1.00 46.15 ? 146 CYS F SG  1 
ATOM   7864  N  N   . GLY G  1 174 ? 92.754  79.699  -17.143 1.00 34.29 ? 147 GLY F N   1 
ATOM   7865  C  CA  . GLY G  1 174 ? 92.629  81.130  -16.948 1.00 35.48 ? 147 GLY F CA  1 
ATOM   7866  C  C   . GLY G  1 174 ? 92.821  81.438  -15.487 1.00 32.73 ? 147 GLY F C   1 
ATOM   7867  O  O   . GLY G  1 174 ? 92.599  80.585  -14.627 1.00 33.29 ? 147 GLY F O   1 
ATOM   7868  N  N   . VAL G  1 175 ? 93.250  82.673  -15.210 1.00 32.46 ? 148 VAL F N   1 
ATOM   7869  C  CA  . VAL G  1 175 ? 93.401  83.133  -13.832 1.00 29.83 ? 148 VAL F CA  1 
ATOM   7870  C  C   . VAL G  1 175 ? 92.026  83.482  -13.271 1.00 28.89 ? 148 VAL F C   1 
ATOM   7871  O  O   . VAL G  1 175 ? 91.194  84.088  -13.952 1.00 37.20 ? 148 VAL F O   1 
ATOM   7872  C  CB  . VAL G  1 175 ? 94.365  84.338  -13.773 1.00 25.56 ? 148 VAL F CB  1 
ATOM   7873  C  CG1 . VAL G  1 175 ? 94.622  84.725  -12.339 1.00 33.63 ? 148 VAL F CG1 1 
ATOM   7874  C  CG2 . VAL G  1 175 ? 95.674  83.995  -14.479 1.00 32.71 ? 148 VAL F CG2 1 
ATOM   7875  N  N   . ILE G  1 176 ? 91.777  83.086  -12.028 1.00 30.60 ? 149 ILE F N   1 
ATOM   7876  C  CA  . ILE G  1 176 ? 90.499  83.357  -11.380 1.00 34.08 ? 149 ILE F CA  1 
ATOM   7877  C  C   . ILE G  1 176 ? 90.529  84.759  -10.782 1.00 35.89 ? 149 ILE F C   1 
ATOM   7878  O  O   . ILE G  1 176 ? 91.317  85.041  -9.874  1.00 38.90 ? 149 ILE F O   1 
ATOM   7879  C  CB  . ILE G  1 176 ? 90.197  82.308  -10.306 1.00 28.31 ? 149 ILE F CB  1 
ATOM   7880  C  CG1 . ILE G  1 176 ? 90.126  80.915  -10.952 1.00 32.93 ? 149 ILE F CG1 1 
ATOM   7881  C  CG2 . ILE G  1 176 ? 88.916  82.660  -9.579  1.00 34.72 ? 149 ILE F CG2 1 
ATOM   7882  C  CD1 . ILE G  1 176 ? 90.273  79.769  -9.955  1.00 31.65 ? 149 ILE F CD1 1 
ATOM   7883  N  N   . GLY G  1 177 ? 89.649  85.629  -11.269 1.00 35.52 ? 150 GLY F N   1 
ATOM   7884  C  CA  . GLY G  1 177 ? 89.660  87.029  -10.892 1.00 32.29 ? 150 GLY F CA  1 
ATOM   7885  C  C   . GLY G  1 177 ? 88.390  87.451  -10.180 1.00 39.05 ? 150 GLY F C   1 
ATOM   7886  O  O   . GLY G  1 177 ? 87.328  86.837  -10.346 1.00 36.28 ? 150 GLY F O   1 
ATOM   7887  N  N   . ILE G  1 178 ? 88.514  88.514  -9.374  1.00 36.28 ? 151 ILE F N   1 
ATOM   7888  C  CA  . ILE G  1 178 ? 87.375  89.063  -8.651  1.00 33.09 ? 151 ILE F CA  1 
ATOM   7889  C  C   . ILE G  1 178 ? 86.375  89.636  -9.644  1.00 37.71 ? 151 ILE F C   1 
ATOM   7890  O  O   . ILE G  1 178 ? 86.739  90.381  -10.567 1.00 34.67 ? 151 ILE F O   1 
ATOM   7891  C  CB  . ILE G  1 178 ? 87.852  90.132  -7.655  1.00 40.69 ? 151 ILE F CB  1 
ATOM   7892  C  CG1 . ILE G  1 178 ? 88.954  89.559  -6.763  1.00 38.04 ? 151 ILE F CG1 1 
ATOM   7893  C  CG2 . ILE G  1 178 ? 86.691  90.632  -6.811  1.00 37.64 ? 151 ILE F CG2 1 
ATOM   7894  C  CD1 . ILE G  1 178 ? 89.385  90.480  -5.618  1.00 38.49 ? 151 ILE F CD1 1 
ATOM   7895  N  N   . ALA G  1 179 ? 85.106  89.283  -9.468  1.00 30.88 ? 152 ALA F N   1 
ATOM   7896  C  CA  . ALA G  1 179 ? 84.049  89.748  -10.350 1.00 33.82 ? 152 ALA F CA  1 
ATOM   7897  C  C   . ALA G  1 179 ? 83.110  90.680  -9.597  1.00 33.48 ? 152 ALA F C   1 
ATOM   7898  O  O   . ALA G  1 179 ? 83.083  90.720  -8.364  1.00 38.07 ? 152 ALA F O   1 
ATOM   7899  C  CB  . ALA G  1 179 ? 83.259  88.574  -10.938 1.00 35.76 ? 152 ALA F CB  1 
ATOM   7900  N  N   . GLN G  1 180 ? 82.345  91.443  -10.364 1.00 41.85 ? 153 GLN F N   1 
ATOM   7901  C  CA  . GLN G  1 180 ? 81.397  92.383  -9.779  1.00 47.60 ? 153 GLN F CA  1 
ATOM   7902  C  C   . GLN G  1 180 ? 80.104  91.676  -9.380  1.00 63.39 ? 153 GLN F C   1 
ATOM   7903  O  O   . GLN G  1 180 ? 79.429  91.057  -10.216 1.00 53.63 ? 153 GLN F O   1 
ATOM   7904  C  CB  . GLN G  1 180 ? 81.097  93.519  -10.752 1.00 41.81 ? 153 GLN F CB  1 
ATOM   7905  C  CG  . GLN G  1 180 ? 80.307  94.643  -10.127 1.00 46.33 ? 153 GLN F CG  1 
ATOM   7906  C  CD  . GLN G  1 180 ? 80.196  95.833  -11.047 1.00 51.48 ? 153 GLN F CD  1 
ATOM   7907  O  OE1 . GLN G  1 180 ? 79.942  95.683  -12.245 1.00 55.48 ? 153 GLN F OE1 1 
ATOM   7908  N  NE2 . GLN G  1 180 ? 80.382  97.033  -10.493 1.00 52.68 ? 153 GLN F NE2 1 
ATOM   7909  O  OXT . GLN G  1 180 ? 79.715  91.718  -8.208  1.00 66.67 ? 153 GLN F OXT 1 
ATOM   7910  N  N   . THR H  1 29  ? 105.995 87.247  -1.097  1.00 45.20 ? 2   THR G N   1 
ATOM   7911  C  CA  . THR H  1 29  ? 104.952 87.052  -2.106  1.00 47.08 ? 2   THR G CA  1 
ATOM   7912  C  C   . THR H  1 29  ? 105.312 87.647  -3.464  1.00 47.89 ? 2   THR G C   1 
ATOM   7913  O  O   . THR H  1 29  ? 105.840 88.760  -3.555  1.00 46.25 ? 2   THR G O   1 
ATOM   7914  C  CB  . THR H  1 29  ? 103.604 87.676  -1.683  1.00 45.34 ? 2   THR G CB  1 
ATOM   7915  O  OG1 . THR H  1 29  ? 103.430 87.562  -0.269  1.00 62.20 ? 2   THR G OG1 1 
ATOM   7916  C  CG2 . THR H  1 29  ? 102.461 86.974  -2.387  1.00 46.92 ? 2   THR G CG2 1 
ATOM   7917  N  N   . LYS H  1 30  ? 105.007 86.897  -4.521  1.00 41.64 ? 3   LYS G N   1 
ATOM   7918  C  CA  . LYS H  1 30  ? 105.117 87.373  -5.886  1.00 32.15 ? 3   LYS G CA  1 
ATOM   7919  C  C   . LYS H  1 30  ? 103.780 87.223  -6.597  1.00 45.57 ? 3   LYS G C   1 
ATOM   7920  O  O   . LYS H  1 30  ? 102.895 86.475  -6.162  1.00 41.59 ? 3   LYS G O   1 
ATOM   7921  C  CB  . LYS H  1 30  ? 106.210 86.630  -6.672  1.00 42.73 ? 3   LYS G CB  1 
ATOM   7922  C  CG  . LYS H  1 30  ? 107.576 86.571  -5.974  1.00 49.53 ? 3   LYS G CG  1 
ATOM   7923  C  CD  . LYS H  1 30  ? 108.514 85.551  -6.638  1.00 53.65 ? 3   LYS G CD  1 
ATOM   7924  C  CE  . LYS H  1 30  ? 109.211 86.124  -7.874  1.00 53.88 ? 3   LYS G CE  1 
ATOM   7925  N  NZ  . LYS H  1 30  ? 110.106 87.285  -7.552  1.00 54.56 ? 3   LYS G NZ  1 
ATOM   7926  N  N   . ALA H  1 31  ? 103.648 87.968  -7.695  1.00 38.00 ? 4   ALA G N   1 
ATOM   7927  C  CA  . ALA H  1 31  ? 102.499 87.882  -8.584  1.00 34.31 ? 4   ALA G CA  1 
ATOM   7928  C  C   . ALA H  1 31  ? 102.977 88.147  -10.002 1.00 41.64 ? 4   ALA G C   1 
ATOM   7929  O  O   . ALA H  1 31  ? 104.103 88.604  -10.226 1.00 42.91 ? 4   ALA G O   1 
ATOM   7930  C  CB  . ALA H  1 31  ? 101.392 88.863  -8.183  1.00 36.47 ? 4   ALA G CB  1 
ATOM   7931  N  N   . VAL H  1 32  ? 102.113 87.836  -10.969 1.00 35.84 ? 5   VAL G N   1 
ATOM   7932  C  CA  . VAL H  1 32  ? 102.459 87.958  -12.376 1.00 34.43 ? 5   VAL G CA  1 
ATOM   7933  C  C   . VAL H  1 32  ? 101.184 88.226  -13.159 1.00 37.77 ? 5   VAL G C   1 
ATOM   7934  O  O   . VAL H  1 32  ? 100.078 87.870  -12.738 1.00 38.38 ? 5   VAL G O   1 
ATOM   7935  C  CB  . VAL H  1 32  ? 103.176 86.696  -12.917 1.00 35.74 ? 5   VAL G CB  1 
ATOM   7936  C  CG1 . VAL H  1 32  ? 102.180 85.539  -13.102 1.00 39.39 ? 5   VAL G CG1 1 
ATOM   7937  C  CG2 . VAL H  1 32  ? 103.931 87.001  -14.202 1.00 32.98 ? 5   VAL G CG2 1 
ATOM   7938  N  N   . CYS H  1 33  ? 101.350 88.862  -14.313 1.00 32.60 ? 6   CYS G N   1 
ATOM   7939  C  CA  . CYS H  1 33  ? 100.231 89.264  -15.146 1.00 35.25 ? 6   CYS G CA  1 
ATOM   7940  C  C   . CYS H  1 33  ? 100.654 89.183  -16.601 1.00 37.88 ? 6   CYS G C   1 
ATOM   7941  O  O   . CYS H  1 33  ? 101.672 89.759  -16.991 1.00 36.74 ? 6   CYS G O   1 
ATOM   7942  C  CB  . CYS H  1 33  ? 99.765  90.686  -14.800 1.00 36.37 ? 6   CYS G CB  1 
ATOM   7943  S  SG  . CYS H  1 33  ? 98.378  91.256  -15.822 1.00 41.15 ? 6   CYS G SG  1 
ATOM   7944  N  N   . VAL H  1 34  ? 99.878  88.456  -17.395 1.00 32.19 ? 7   VAL G N   1 
ATOM   7945  C  CA  . VAL H  1 34  ? 100.069 88.383  -18.833 1.00 30.08 ? 7   VAL G CA  1 
ATOM   7946  C  C   . VAL H  1 34  ? 99.075  89.346  -19.463 1.00 40.43 ? 7   VAL G C   1 
ATOM   7947  O  O   . VAL H  1 34  ? 97.857  89.185  -19.300 1.00 35.96 ? 7   VAL G O   1 
ATOM   7948  C  CB  . VAL H  1 34  ? 99.873  86.949  -19.355 1.00 38.76 ? 7   VAL G CB  1 
ATOM   7949  C  CG1 . VAL H  1 34  ? 100.029 86.897  -20.869 1.00 35.08 ? 7   VAL G CG1 1 
ATOM   7950  C  CG2 . VAL H  1 34  ? 100.841 85.991  -18.671 1.00 34.60 ? 7   VAL G CG2 1 
ATOM   7951  N  N   . LEU H  1 35  ? 99.587  90.351  -20.172 1.00 35.56 ? 8   LEU G N   1 
ATOM   7952  C  CA  . LEU H  1 35  ? 98.760  91.377  -20.789 1.00 33.70 ? 8   LEU G CA  1 
ATOM   7953  C  C   . LEU H  1 35  ? 98.531  91.016  -22.249 1.00 37.16 ? 8   LEU G C   1 
ATOM   7954  O  O   . LEU H  1 35  ? 99.491  90.801  -22.991 1.00 40.47 ? 8   LEU G O   1 
ATOM   7955  C  CB  . LEU H  1 35  ? 99.437  92.746  -20.691 1.00 30.94 ? 8   LEU G CB  1 
ATOM   7956  C  CG  . LEU H  1 35  ? 99.707  93.295  -19.291 1.00 35.45 ? 8   LEU G CG  1 
ATOM   7957  C  CD1 . LEU H  1 35  ? 100.813 94.332  -19.350 1.00 41.52 ? 8   LEU G CD1 1 
ATOM   7958  C  CD2 . LEU H  1 35  ? 98.460  93.910  -18.726 1.00 36.79 ? 8   LEU G CD2 1 
ATOM   7959  N  N   . LYS H  1 36  ? 97.264  90.938  -22.656 1.00 36.63 ? 9   LYS G N   1 
ATOM   7960  C  CA  . LYS H  1 36  ? 96.919  90.718  -24.054 1.00 38.31 ? 9   LYS G CA  1 
ATOM   7961  C  C   . LYS H  1 36  ? 95.721  91.582  -24.412 1.00 34.01 ? 9   LYS G C   1 
ATOM   7962  O  O   . LYS H  1 36  ? 94.924  91.969  -23.554 1.00 32.57 ? 9   LYS G O   1 
ATOM   7963  C  CB  . LYS H  1 36  ? 96.598  89.246  -24.360 1.00 42.17 ? 9   LYS G CB  1 
ATOM   7964  C  CG  . LYS H  1 36  ? 97.714  88.251  -24.055 1.00 40.59 ? 9   LYS G CG  1 
ATOM   7965  C  CD  . LYS H  1 36  ? 97.495  86.930  -24.795 1.00 50.90 ? 9   LYS G CD  1 
ATOM   7966  C  CE  . LYS H  1 36  ? 96.488  87.077  -25.950 1.00 54.80 ? 9   LYS G CE  1 
ATOM   7967  N  NZ  . LYS H  1 36  ? 96.276  85.825  -26.741 1.00 58.43 ? 9   LYS G NZ  1 
ATOM   7968  N  N   . GLY H  1 37  ? 95.592  91.874  -25.699 1.00 37.51 ? 10  GLY G N   1 
ATOM   7969  C  CA  . GLY H  1 37  ? 94.493  92.711  -26.139 1.00 42.74 ? 10  GLY G CA  1 
ATOM   7970  C  C   . GLY H  1 37  ? 93.937  92.344  -27.499 1.00 47.80 ? 10  GLY G C   1 
ATOM   7971  O  O   . GLY H  1 37  ? 94.312  91.320  -28.081 1.00 46.49 ? 10  GLY G O   1 
ATOM   7972  N  N   . ASP H  1 38  ? 93.038  93.188  -28.015 1.00 46.65 ? 11  ASP G N   1 
ATOM   7973  C  CA  . ASP H  1 38  ? 92.457  92.999  -29.339 1.00 47.38 ? 11  ASP G CA  1 
ATOM   7974  C  C   . ASP H  1 38  ? 93.443  93.261  -30.461 1.00 49.55 ? 11  ASP G C   1 
ATOM   7975  O  O   . ASP H  1 38  ? 93.100  93.036  -31.627 1.00 53.04 ? 11  ASP G O   1 
ATOM   7976  C  CB  . ASP H  1 38  ? 91.247  93.920  -29.520 1.00 48.01 ? 11  ASP G CB  1 
ATOM   7977  C  CG  . ASP H  1 38  ? 89.990  93.346  -28.906 1.00 66.02 ? 11  ASP G CG  1 
ATOM   7978  O  OD1 . ASP H  1 38  ? 90.048  92.196  -28.410 1.00 68.31 ? 11  ASP G OD1 1 
ATOM   7979  O  OD2 . ASP H  1 38  ? 88.947  94.044  -28.913 1.00 72.93 ? 11  ASP G OD2 1 
ATOM   7980  N  N   . GLY H  1 39  ? 94.641  93.740  -30.146 1.00 47.63 ? 12  GLY G N   1 
ATOM   7981  C  CA  . GLY H  1 39  ? 95.612  94.074  -31.159 1.00 38.30 ? 12  GLY G CA  1 
ATOM   7982  C  C   . GLY H  1 39  ? 96.998  93.580  -30.809 1.00 40.58 ? 12  GLY G C   1 
ATOM   7983  O  O   . GLY H  1 39  ? 97.166  92.552  -30.138 1.00 50.56 ? 12  GLY G O   1 
ATOM   7984  N  N   . PRO H  1 40  ? 98.023  94.318  -31.240 1.00 44.40 ? 13  PRO G N   1 
ATOM   7985  C  CA  . PRO H  1 40  ? 99.399  93.830  -31.129 1.00 44.88 ? 13  PRO G CA  1 
ATOM   7986  C  C   . PRO H  1 40  ? 100.018 94.014  -29.752 1.00 45.43 ? 13  PRO G C   1 
ATOM   7987  O  O   . PRO H  1 40  ? 101.150 93.560  -29.541 1.00 48.84 ? 13  PRO G O   1 
ATOM   7988  C  CB  . PRO H  1 40  ? 100.158 94.657  -32.167 1.00 41.44 ? 13  PRO G CB  1 
ATOM   7989  C  CG  . PRO H  1 40  ? 99.287  95.826  -32.486 1.00 43.96 ? 13  PRO G CG  1 
ATOM   7990  C  CD  . PRO H  1 40  ? 97.920  95.597  -31.929 1.00 40.42 ? 13  PRO G CD  1 
ATOM   7991  N  N   . VAL H  1 41  ? 99.348  94.674  -28.810 1.00 42.76 ? 14  VAL G N   1 
ATOM   7992  C  CA  . VAL H  1 41  ? 99.973  94.962  -27.524 1.00 34.35 ? 14  VAL G CA  1 
ATOM   7993  C  C   . VAL H  1 41  ? 99.929  93.722  -26.642 1.00 42.23 ? 14  VAL G C   1 
ATOM   7994  O  O   . VAL H  1 41  ? 98.861  93.145  -26.402 1.00 42.54 ? 14  VAL G O   1 
ATOM   7995  C  CB  . VAL H  1 41  ? 99.293  96.152  -26.837 1.00 35.03 ? 14  VAL G CB  1 
ATOM   7996  C  CG1 . VAL H  1 41  ? 99.946  96.390  -25.493 1.00 32.73 ? 14  VAL G CG1 1 
ATOM   7997  C  CG2 . VAL H  1 41  ? 99.399  97.401  -27.698 1.00 35.58 ? 14  VAL G CG2 1 
ATOM   7998  N  N   . GLN H  1 42  ? 101.096 93.315  -26.149 1.00 36.84 ? 15  GLN G N   1 
ATOM   7999  C  CA  . GLN H  1 42  ? 101.202 92.181  -25.246 1.00 37.59 ? 15  GLN G CA  1 
ATOM   8000  C  C   . GLN H  1 42  ? 102.445 92.348  -24.391 1.00 38.83 ? 15  GLN G C   1 
ATOM   8001  O  O   . GLN H  1 42  ? 103.415 92.997  -24.799 1.00 44.31 ? 15  GLN G O   1 
ATOM   8002  C  CB  . GLN H  1 42  ? 101.255 90.854  -26.010 1.00 41.76 ? 15  GLN G CB  1 
ATOM   8003  C  CG  . GLN H  1 42  ? 102.634 90.525  -26.556 1.00 44.50 ? 15  GLN G CG  1 
ATOM   8004  C  CD  . GLN H  1 42  ? 102.684 89.171  -27.240 1.00 61.60 ? 15  GLN G CD  1 
ATOM   8005  O  OE1 . GLN H  1 42  ? 102.049 88.962  -28.278 1.00 59.12 ? 15  GLN G OE1 1 
ATOM   8006  N  NE2 . GLN H  1 42  ? 103.459 88.245  -26.670 1.00 57.95 ? 15  GLN G NE2 1 
ATOM   8007  N  N   . GLY H  1 43  ? 102.413 91.754  -23.207 1.00 33.08 ? 16  GLY G N   1 
ATOM   8008  C  CA  . GLY H  1 43  ? 103.536 91.887  -22.303 1.00 36.41 ? 16  GLY G CA  1 
ATOM   8009  C  C   . GLY H  1 43  ? 103.337 91.035  -21.074 1.00 40.73 ? 16  GLY G C   1 
ATOM   8010  O  O   . GLY H  1 43  ? 102.293 90.399  -20.886 1.00 37.80 ? 16  GLY G O   1 
ATOM   8011  N  N   . ILE H  1 44  ? 104.366 91.032  -20.230 1.00 38.15 ? 17  ILE G N   1 
ATOM   8012  C  CA  . ILE H  1 44  ? 104.362 90.306  -18.969 1.00 33.98 ? 17  ILE G CA  1 
ATOM   8013  C  C   . ILE H  1 44  ? 104.890 91.237  -17.890 1.00 40.37 ? 17  ILE G C   1 
ATOM   8014  O  O   . ILE H  1 44  ? 105.955 91.843  -18.055 1.00 45.56 ? 17  ILE G O   1 
ATOM   8015  C  CB  . ILE H  1 44  ? 105.223 89.028  -19.039 1.00 37.32 ? 17  ILE G CB  1 
ATOM   8016  C  CG1 . ILE H  1 44  ? 104.529 87.956  -19.873 1.00 38.48 ? 17  ILE G CG1 1 
ATOM   8017  C  CG2 . ILE H  1 44  ? 105.487 88.501  -17.649 1.00 34.60 ? 17  ILE G CG2 1 
ATOM   8018  C  CD1 . ILE H  1 44  ? 105.470 87.163  -20.774 1.00 42.18 ? 17  ILE G CD1 1 
ATOM   8019  N  N   . ILE H  1 45  ? 104.158 91.345  -16.790 1.00 34.21 ? 18  ILE G N   1 
ATOM   8020  C  CA  . ILE H  1 45  ? 104.530 92.219  -15.689 1.00 32.94 ? 18  ILE G CA  1 
ATOM   8021  C  C   . ILE H  1 45  ? 104.591 91.387  -14.416 1.00 36.52 ? 18  ILE G C   1 
ATOM   8022  O  O   . ILE H  1 45  ? 103.658 90.633  -14.112 1.00 35.65 ? 18  ILE G O   1 
ATOM   8023  C  CB  . ILE H  1 45  ? 103.536 93.385  -15.531 1.00 31.34 ? 18  ILE G CB  1 
ATOM   8024  C  CG1 . ILE H  1 45  ? 103.463 94.229  -16.819 1.00 33.08 ? 18  ILE G CG1 1 
ATOM   8025  C  CG2 . ILE H  1 45  ? 103.858 94.209  -14.301 1.00 34.50 ? 18  ILE G CG2 1 
ATOM   8026  C  CD1 . ILE H  1 45  ? 104.724 95.002  -17.157 1.00 37.54 ? 18  ILE G CD1 1 
ATOM   8027  N  N   . ASN H  1 46  ? 105.686 91.528  -13.672 1.00 37.57 ? 19  ASN G N   1 
ATOM   8028  C  CA  . ASN H  1 46  ? 105.890 90.855  -12.398 1.00 33.55 ? 19  ASN G CA  1 
ATOM   8029  C  C   . ASN H  1 46  ? 105.633 91.802  -11.240 1.00 37.40 ? 19  ASN G C   1 
ATOM   8030  O  O   . ASN H  1 46  ? 105.801 93.018  -11.362 1.00 39.34 ? 19  ASN G O   1 
ATOM   8031  C  CB  . ASN H  1 46  ? 107.317 90.323  -12.295 1.00 39.95 ? 19  ASN G CB  1 
ATOM   8032  C  CG  . ASN H  1 46  ? 107.686 89.468  -13.466 1.00 37.97 ? 19  ASN G CG  1 
ATOM   8033  O  OD1 . ASN H  1 46  ? 108.297 89.943  -14.436 1.00 45.94 ? 19  ASN G OD1 1 
ATOM   8034  N  ND2 . ASN H  1 46  ? 107.291 88.197  -13.413 1.00 41.35 ? 19  ASN G ND2 1 
ATOM   8035  N  N   . PHE H  1 47  ? 105.242 91.221  -10.105 1.00 36.45 ? 20  PHE G N   1 
ATOM   8036  C  CA  . PHE H  1 47  ? 105.071 91.927  -8.844  1.00 36.81 ? 20  PHE G CA  1 
ATOM   8037  C  C   . PHE H  1 47  ? 105.814 91.170  -7.757  1.00 45.95 ? 20  PHE G C   1 
ATOM   8038  O  O   . PHE H  1 47  ? 105.798 89.936  -7.728  1.00 47.88 ? 20  PHE G O   1 
ATOM   8039  C  CB  . PHE H  1 47  ? 103.597 92.055  -8.450  1.00 39.25 ? 20  PHE G CB  1 
ATOM   8040  C  CG  . PHE H  1 47  ? 102.736 92.679  -9.506  1.00 35.20 ? 20  PHE G CG  1 
ATOM   8041  C  CD1 . PHE H  1 47  ? 102.353 91.951  -10.628 1.00 37.72 ? 20  PHE G CD1 1 
ATOM   8042  C  CD2 . PHE H  1 47  ? 102.276 93.978  -9.362  1.00 33.92 ? 20  PHE G CD2 1 
ATOM   8043  C  CE1 . PHE H  1 47  ? 101.547 92.519  -11.608 1.00 40.36 ? 20  PHE G CE1 1 
ATOM   8044  C  CE2 . PHE H  1 47  ? 101.465 94.554  -10.336 1.00 39.07 ? 20  PHE G CE2 1 
ATOM   8045  C  CZ  . PHE H  1 47  ? 101.104 93.824  -11.460 1.00 36.05 ? 20  PHE G CZ  1 
ATOM   8046  N  N   . GLU H  1 48  ? 106.455 91.908  -6.858  1.00 46.16 ? 21  GLU G N   1 
ATOM   8047  C  CA  . GLU H  1 48  ? 107.168 91.292  -5.747  1.00 41.22 ? 21  GLU G CA  1 
ATOM   8048  C  C   . GLU H  1 48  ? 107.089 92.213  -4.543  1.00 40.27 ? 21  GLU G C   1 
ATOM   8049  O  O   . GLU H  1 48  ? 107.327 93.417  -4.664  1.00 44.88 ? 21  GLU G O   1 
ATOM   8050  C  CB  . GLU H  1 48  ? 108.623 91.010  -6.119  1.00 40.33 ? 21  GLU G CB  1 
ATOM   8051  C  CG  . GLU H  1 48  ? 109.489 90.684  -4.909  1.00 52.93 ? 21  GLU G CG  1 
ATOM   8052  C  CD  . GLU H  1 48  ? 110.581 89.658  -5.204  1.00 63.28 ? 21  GLU G CD  1 
ATOM   8053  O  OE1 . GLU H  1 48  ? 111.319 89.827  -6.204  1.00 63.87 ? 21  GLU G OE1 1 
ATOM   8054  O  OE2 . GLU H  1 48  ? 110.712 88.690  -4.419  1.00 69.15 ? 21  GLU G OE2 1 
ATOM   8055  N  N   . GLN H  1 49  ? 106.740 91.649  -3.392  1.00 36.62 ? 22  GLN G N   1 
ATOM   8056  C  CA  . GLN H  1 49  ? 106.547 92.416  -2.164  1.00 39.49 ? 22  GLN G CA  1 
ATOM   8057  C  C   . GLN H  1 49  ? 107.166 91.592  -1.036  1.00 51.78 ? 22  GLN G C   1 
ATOM   8058  O  O   . GLN H  1 49  ? 106.508 90.723  -0.456  1.00 51.94 ? 22  GLN G O   1 
ATOM   8059  C  CB  . GLN H  1 49  ? 105.073 92.693  -1.918  1.00 39.65 ? 22  GLN G CB  1 
ATOM   8060  C  CG  . GLN H  1 49  ? 104.810 93.666  -0.793  1.00 41.33 ? 22  GLN G CG  1 
ATOM   8061  C  CD  . GLN H  1 49  ? 103.343 93.720  -0.423  1.00 48.96 ? 22  GLN G CD  1 
ATOM   8062  O  OE1 . GLN H  1 49  ? 102.551 92.885  -0.874  1.00 48.79 ? 22  GLN G OE1 1 
ATOM   8063  N  NE2 . GLN H  1 49  ? 102.963 94.714  0.383   1.00 45.73 ? 22  GLN G NE2 1 
ATOM   8064  N  N   . LYS H  1 50  ? 108.428 91.880  -0.736  1.00 52.06 ? 23  LYS G N   1 
ATOM   8065  C  CA  . LYS H  1 50  ? 109.197 91.107  0.269   1.00 53.47 ? 23  LYS G CA  1 
ATOM   8066  C  C   . LYS H  1 50  ? 108.625 91.261  1.675   1.00 49.02 ? 23  LYS G C   1 
ATOM   8067  O  O   . LYS H  1 50  ? 108.746 90.314  2.435   1.00 60.82 ? 23  LYS G O   1 
ATOM   8068  C  CB  . LYS H  1 50  ? 110.690 91.394  0.131   1.00 51.31 ? 23  LYS G CB  1 
ATOM   8069  C  CG  . LYS H  1 50  ? 111.352 90.647  -1.014  1.00 49.90 ? 23  LYS G CG  1 
ATOM   8070  C  CD  . LYS H  1 50  ? 111.590 91.517  -2.223  1.00 54.29 ? 23  LYS G CD  1 
ATOM   8071  C  CE  . LYS H  1 50  ? 112.942 92.195  -2.205  1.00 55.02 ? 23  LYS G CE  1 
ATOM   8072  N  NZ  . LYS H  1 50  ? 113.362 92.647  -3.555  1.00 56.05 ? 23  LYS G NZ  1 
ATOM   8073  N  N   . GLU H  1 51  ? 108.011 92.391  2.009   1.00 54.28 ? 24  GLU G N   1 
ATOM   8074  C  CA  . GLU H  1 51  ? 107.429 92.514  3.371   1.00 47.30 ? 24  GLU G CA  1 
ATOM   8075  C  C   . GLU H  1 51  ? 105.937 92.849  3.270   1.00 52.02 ? 24  GLU G C   1 
ATOM   8076  O  O   . GLU H  1 51  ? 105.574 93.655  2.438   1.00 58.23 ? 24  GLU G O   1 
ATOM   8077  C  CB  . GLU H  1 51  ? 108.275 93.424  4.261   1.00 51.20 ? 24  GLU G CB  1 
ATOM   8078  C  CG  . GLU H  1 51  ? 109.712 92.962  4.398   1.00 51.87 ? 24  GLU G CG  1 
ATOM   8079  C  CD  . GLU H  1 51  ? 110.051 92.066  5.581   1.00 67.69 ? 24  GLU G CD  1 
ATOM   8080  O  OE1 . GLU H  1 51  ? 109.209 91.924  6.490   1.00 71.89 ? 24  GLU G OE1 1 
ATOM   8081  O  OE2 . GLU H  1 51  ? 111.168 91.527  5.599   1.00 74.31 ? 24  GLU G OE2 1 
ATOM   8082  N  N   . SER H  1 52  ? 105.129 92.237  4.133   1.00 60.33 ? 25  SER G N   1 
ATOM   8083  C  CA  . SER H  1 52  ? 103.639 92.295  4.150   1.00 53.49 ? 25  SER G CA  1 
ATOM   8084  C  C   . SER H  1 52  ? 103.055 93.674  3.834   1.00 60.87 ? 25  SER G C   1 
ATOM   8085  O  O   . SER H  1 52  ? 102.067 93.733  3.079   1.00 64.41 ? 25  SER G O   1 
ATOM   8086  C  CB  . SER H  1 52  ? 103.090 91.745  5.428   1.00 50.76 ? 25  SER G CB  1 
ATOM   8087  O  OG  . SER H  1 52  ? 103.079 92.738  6.429   1.00 65.62 ? 25  SER G OG  1 
ATOM   8088  N  N   . ASN H  1 53  ? 103.568 94.731  4.449   1.00 62.19 ? 26  ASN G N   1 
ATOM   8089  C  CA  . ASN H  1 53  ? 103.008 96.068  4.131   1.00 56.30 ? 26  ASN G CA  1 
ATOM   8090  C  C   . ASN H  1 53  ? 104.126 96.957  3.605   1.00 56.68 ? 26  ASN G C   1 
ATOM   8091  O  O   . ASN H  1 53  ? 104.119 98.135  3.907   1.00 62.03 ? 26  ASN G O   1 
ATOM   8092  C  CB  . ASN H  1 53  ? 102.325 96.720  5.324   1.00 47.23 ? 26  ASN G CB  1 
ATOM   8093  C  CG  . ASN H  1 53  ? 100.938 97.186  4.958   1.00 35.75 ? 26  ASN G CG  1 
ATOM   8094  O  OD1 . ASN H  1 53  ? 99.952  96.543  5.318   1.00 34.37 ? 26  ASN G OD1 1 
ATOM   8095  N  ND2 . ASN H  1 53  ? 100.863 98.275  4.208   1.00 34.67 ? 26  ASN G ND2 1 
ATOM   8096  N  N   . GLY H  1 54  ? 105.058 96.371  2.871   1.00 53.98 ? 27  GLY G N   1 
ATOM   8097  C  CA  . GLY H  1 54  ? 106.160 97.164  2.313   1.00 51.65 ? 27  GLY G CA  1 
ATOM   8098  C  C   . GLY H  1 54  ? 105.859 97.559  0.888   1.00 49.76 ? 27  GLY G C   1 
ATOM   8099  O  O   . GLY H  1 54  ? 104.736 97.317  0.433   1.00 54.34 ? 27  GLY G O   1 
ATOM   8100  N  N   . PRO H  1 55  ? 106.820 98.151  0.165   1.00 50.20 ? 28  PRO G N   1 
ATOM   8101  C  CA  . PRO H  1 55  ? 106.599 98.546  -1.200  1.00 45.28 ? 28  PRO G CA  1 
ATOM   8102  C  C   . PRO H  1 55  ? 106.615 97.317  -2.110  1.00 43.42 ? 28  PRO G C   1 
ATOM   8103  O  O   . PRO H  1 55  ? 107.208 96.346  -1.791  1.00 44.37 ? 28  PRO G O   1 
ATOM   8104  C  CB  . PRO H  1 55  ? 107.819 99.413  -1.496  1.00 46.81 ? 28  PRO G CB  1 
ATOM   8105  C  CG  . PRO H  1 55  ? 108.883 98.806  -0.652  1.00 47.09 ? 28  PRO G CG  1 
ATOM   8106  C  CD  . PRO H  1 55  ? 108.160 98.473  0.628   1.00 47.26 ? 28  PRO G CD  1 
ATOM   8107  N  N   . VAL H  1 56  ? 105.930 97.438  -3.234  1.00 43.62 ? 29  VAL G N   1 
ATOM   8108  C  CA  . VAL H  1 56  ? 105.839 96.403  -4.257  1.00 39.02 ? 29  VAL G CA  1 
ATOM   8109  C  C   . VAL H  1 56  ? 106.680 96.824  -5.453  1.00 35.78 ? 29  VAL G C   1 
ATOM   8110  O  O   . VAL H  1 56  ? 106.546 97.950  -5.946  1.00 40.11 ? 29  VAL G O   1 
ATOM   8111  C  CB  . VAL H  1 56  ? 104.380 96.167  -4.687  1.00 34.47 ? 29  VAL G CB  1 
ATOM   8112  C  CG1 . VAL H  1 56  ? 104.294 95.010  -5.674  1.00 34.70 ? 29  VAL G CG1 1 
ATOM   8113  C  CG2 . VAL H  1 56  ? 103.495 95.942  -3.468  1.00 37.03 ? 29  VAL G CG2 1 
ATOM   8114  N  N   . LYS H  1 57  ? 107.533 95.924  -5.930  1.00 35.22 ? 30  LYS G N   1 
ATOM   8115  C  CA  . LYS H  1 57  ? 108.267 96.155  -7.162  1.00 34.29 ? 30  LYS G CA  1 
ATOM   8116  C  C   . LYS H  1 57  ? 107.461 95.617  -8.341  1.00 40.80 ? 30  LYS G C   1 
ATOM   8117  O  O   . LYS H  1 57  ? 106.952 94.494  -8.292  1.00 42.07 ? 30  LYS G O   1 
ATOM   8118  C  CB  . LYS H  1 57  ? 109.648 95.500  -7.106  1.00 39.59 ? 30  LYS G CB  1 
ATOM   8119  C  CG  . LYS H  1 57  ? 110.389 95.547  -8.436  1.00 44.63 ? 30  LYS G CG  1 
ATOM   8120  C  CD  . LYS H  1 57  ? 111.872 95.151  -8.307  1.00 53.14 ? 30  LYS G CD  1 
ATOM   8121  C  CE  . LYS H  1 57  ? 112.723 95.854  -9.380  1.00 49.94 ? 30  LYS G CE  1 
ATOM   8122  N  NZ  . LYS H  1 57  ? 113.766 94.967  -9.989  1.00 54.05 ? 30  LYS G NZ  1 
ATOM   8123  N  N   . VAL H  1 58  ? 107.345 96.425  -9.393  1.00 38.75 ? 31  VAL G N   1 
ATOM   8124  C  CA  . VAL H  1 58  ? 106.537 96.104  -10.566 1.00 37.17 ? 31  VAL G CA  1 
ATOM   8125  C  C   . VAL H  1 58  ? 107.454 96.230  -11.772 1.00 37.44 ? 31  VAL G C   1 
ATOM   8126  O  O   . VAL H  1 58  ? 107.922 97.331  -12.087 1.00 41.58 ? 31  VAL G O   1 
ATOM   8127  C  CB  . VAL H  1 58  ? 105.320 97.036  -10.709 1.00 34.98 ? 31  VAL G CB  1 
ATOM   8128  C  CG1 . VAL H  1 58  ? 104.454 96.623  -11.897 1.00 32.35 ? 31  VAL G CG1 1 
ATOM   8129  C  CG2 . VAL H  1 58  ? 104.514 97.092  -9.420  1.00 33.79 ? 31  VAL G CG2 1 
ATOM   8130  N  N   . TRP H  1 59  ? 107.712 95.120  -12.452 1.00 33.85 ? 32  TRP G N   1 
ATOM   8131  C  CA  . TRP H  1 59  ? 108.663 95.177  -13.549 1.00 37.15 ? 32  TRP G CA  1 
ATOM   8132  C  C   . TRP H  1 59  ? 108.314 94.149  -14.605 1.00 33.78 ? 32  TRP G C   1 
ATOM   8133  O  O   . TRP H  1 59  ? 107.686 93.123  -14.329 1.00 42.99 ? 32  TRP G O   1 
ATOM   8134  C  CB  . TRP H  1 59  ? 110.098 94.952  -13.060 1.00 37.50 ? 32  TRP G CB  1 
ATOM   8135  C  CG  . TRP H  1 59  ? 110.489 93.512  -12.955 1.00 36.84 ? 32  TRP G CG  1 
ATOM   8136  C  CD1 . TRP H  1 59  ? 111.093 92.745  -13.914 1.00 33.29 ? 32  TRP G CD1 1 
ATOM   8137  C  CD2 . TRP H  1 59  ? 110.281 92.658  -11.828 1.00 32.22 ? 32  TRP G CD2 1 
ATOM   8138  N  NE1 . TRP H  1 59  ? 111.283 91.467  -13.441 1.00 37.32 ? 32  TRP G NE1 1 
ATOM   8139  C  CE2 . TRP H  1 59  ? 110.794 91.391  -12.163 1.00 35.29 ? 32  TRP G CE2 1 
ATOM   8140  C  CE3 . TRP H  1 59  ? 109.714 92.845  -10.565 1.00 36.87 ? 32  TRP G CE3 1 
ATOM   8141  C  CZ2 . TRP H  1 59  ? 110.758 90.316  -11.279 1.00 40.85 ? 32  TRP G CZ2 1 
ATOM   8142  C  CZ3 . TRP H  1 59  ? 109.683 91.774  -9.681  1.00 46.24 ? 32  TRP G CZ3 1 
ATOM   8143  C  CH2 . TRP H  1 59  ? 110.202 90.527  -10.045 1.00 43.61 ? 32  TRP G CH2 1 
ATOM   8144  N  N   . GLY H  1 60  ? 108.786 94.415  -15.808 1.00 35.38 ? 33  GLY G N   1 
ATOM   8145  C  CA  . GLY H  1 60  ? 108.523 93.547  -16.931 1.00 35.19 ? 33  GLY G CA  1 
ATOM   8146  C  C   . GLY H  1 60  ? 108.683 94.333  -18.212 1.00 38.90 ? 33  GLY G C   1 
ATOM   8147  O  O   . GLY H  1 60  ? 109.358 95.361  -18.244 1.00 40.35 ? 33  GLY G O   1 
ATOM   8148  N  N   . SER H  1 61  ? 108.026 93.835  -19.251 1.00 39.62 ? 34  SER G N   1 
ATOM   8149  C  CA  . SER H  1 61  ? 108.136 94.391  -20.586 1.00 39.65 ? 34  SER G CA  1 
ATOM   8150  C  C   . SER H  1 61  ? 106.789 94.296  -21.290 1.00 46.15 ? 34  SER G C   1 
ATOM   8151  O  O   . SER H  1 61  ? 106.051 93.324  -21.116 1.00 45.47 ? 34  SER G O   1 
ATOM   8152  C  CB  . SER H  1 61  ? 109.212 93.652  -21.397 1.00 37.78 ? 34  SER G CB  1 
ATOM   8153  O  OG  . SER H  1 61  ? 109.177 94.060  -22.753 1.00 53.75 ? 34  SER G OG  1 
ATOM   8154  N  N   . ILE H  1 62  ? 106.480 95.296  -22.103 1.00 39.57 ? 35  ILE G N   1 
ATOM   8155  C  CA  . ILE H  1 62  ? 105.234 95.345  -22.910 1.00 33.41 ? 35  ILE G CA  1 
ATOM   8156  C  C   . ILE H  1 62  ? 105.657 95.764  -24.311 1.00 39.92 ? 35  ILE G C   1 
ATOM   8157  O  O   . ILE H  1 62  ? 106.361 96.746  -24.430 1.00 40.83 ? 35  ILE G O   1 
ATOM   8158  C  CB  . ILE H  1 62  ? 104.214 96.341  -22.331 1.00 33.59 ? 35  ILE G CB  1 
ATOM   8159  C  CG1 . ILE H  1 62  ? 103.858 96.048  -20.878 1.00 38.22 ? 35  ILE G CG1 1 
ATOM   8160  C  CG2 . ILE H  1 62  ? 102.981 96.411  -23.198 1.00 36.24 ? 35  ILE G CG2 1 
ATOM   8161  C  CD1 . ILE H  1 62  ? 103.134 97.167  -20.200 1.00 37.91 ? 35  ILE G CD1 1 
ATOM   8162  N  N   . LYS H  1 63  ? 105.223 95.035  -25.328 1.00 44.06 ? 36  LYS G N   1 
ATOM   8163  C  CA  . LYS H  1 63  ? 105.611 95.371  -26.715 1.00 41.10 ? 36  LYS G CA  1 
ATOM   8164  C  C   . LYS H  1 63  ? 104.375 95.706  -27.538 1.00 40.54 ? 36  LYS G C   1 
ATOM   8165  O  O   . LYS H  1 63  ? 103.279 95.497  -27.052 1.00 38.76 ? 36  LYS G O   1 
ATOM   8166  C  CB  . LYS H  1 63  ? 106.412 94.221  -27.328 1.00 48.26 ? 36  LYS G CB  1 
ATOM   8167  C  CG  . LYS H  1 63  ? 105.633 92.952  -27.644 1.00 51.68 ? 36  LYS G CG  1 
ATOM   8168  C  CD  . LYS H  1 63  ? 106.396 92.031  -28.573 1.00 59.37 ? 36  LYS G CD  1 
ATOM   8169  C  CE  . LYS H  1 63  ? 105.632 90.791  -28.990 1.00 58.88 ? 36  LYS G CE  1 
ATOM   8170  N  NZ  . LYS H  1 63  ? 106.545 89.761  -29.541 1.00 50.76 ? 36  LYS G NZ  1 
ATOM   8171  N  N   . GLY H  1 64  ? 104.594 96.246  -28.732 1.00 39.13 ? 37  GLY G N   1 
ATOM   8172  C  CA  . GLY H  1 64  ? 103.515 96.572  -29.674 1.00 37.07 ? 37  GLY G CA  1 
ATOM   8173  C  C   . GLY H  1 64  ? 102.872 97.911  -29.411 1.00 36.62 ? 37  GLY G C   1 
ATOM   8174  O  O   . GLY H  1 64  ? 101.853 98.170  -30.001 1.00 40.75 ? 37  GLY G O   1 
ATOM   8175  N  N   . LEU H  1 65  ? 103.478 98.744  -28.575 1.00 40.85 ? 38  LEU G N   1 
ATOM   8176  C  CA  . LEU H  1 65  ? 102.853 100.048 -28.247 1.00 40.73 ? 38  LEU G CA  1 
ATOM   8177  C  C   . LEU H  1 65  ? 103.373 101.155 -29.159 1.00 42.30 ? 38  LEU G C   1 
ATOM   8178  O  O   . LEU H  1 65  ? 104.409 100.987 -29.775 1.00 48.98 ? 38  LEU G O   1 
ATOM   8179  C  CB  . LEU H  1 65  ? 103.219 100.416 -26.809 1.00 37.81 ? 38  LEU G CB  1 
ATOM   8180  C  CG  . LEU H  1 65  ? 102.669 99.530  -25.702 1.00 36.67 ? 38  LEU G CG  1 
ATOM   8181  C  CD1 . LEU H  1 65  ? 103.465 99.733  -24.436 1.00 30.54 ? 38  LEU G CD1 1 
ATOM   8182  C  CD2 . LEU H  1 65  ? 101.202 99.827  -25.471 1.00 36.68 ? 38  LEU G CD2 1 
ATOM   8183  N  N   . THR H  1 66  ? 102.596 102.216 -29.281 1.00 43.40 ? 39  THR G N   1 
ATOM   8184  C  CA  . THR H  1 66  ? 103.104 103.430 -29.900 1.00 38.33 ? 39  THR G CA  1 
ATOM   8185  C  C   . THR H  1 66  ? 104.139 104.076 -28.982 1.00 44.34 ? 39  THR G C   1 
ATOM   8186  O  O   . THR H  1 66  ? 104.030 104.009 -27.751 1.00 42.22 ? 39  THR G O   1 
ATOM   8187  C  CB  . THR H  1 66  ? 101.963 104.403 -30.198 1.00 39.35 ? 39  THR G CB  1 
ATOM   8188  O  OG1 . THR H  1 66  ? 101.276 104.734 -28.986 1.00 45.00 ? 39  THR G OG1 1 
ATOM   8189  C  CG2 . THR H  1 66  ? 100.974 103.795 -31.183 1.00 37.45 ? 39  THR G CG2 1 
ATOM   8190  N  N   . GLU H  1 67  ? 105.166 104.677 -29.585 1.00 43.99 ? 40  GLU G N   1 
ATOM   8191  C  CA  . GLU H  1 67  ? 106.193 105.355 -28.800 1.00 41.38 ? 40  GLU G CA  1 
ATOM   8192  C  C   . GLU H  1 67  ? 105.570 106.493 -27.993 1.00 38.52 ? 40  GLU G C   1 
ATOM   8193  O  O   . GLU H  1 67  ? 104.733 107.249 -28.499 1.00 45.88 ? 40  GLU G O   1 
ATOM   8194  C  CB  . GLU H  1 67  ? 107.307 105.871 -29.722 1.00 46.91 ? 40  GLU G CB  1 
ATOM   8195  C  CG  . GLU H  1 67  ? 107.010 107.205 -30.405 1.00 51.74 ? 40  GLU G CG  1 
ATOM   8196  C  CD  . GLU H  1 67  ? 108.246 107.893 -30.990 1.00 62.96 ? 40  GLU G CD  1 
ATOM   8197  O  OE1 . GLU H  1 67  ? 109.374 107.356 -30.855 1.00 55.81 ? 40  GLU G OE1 1 
ATOM   8198  O  OE2 . GLU H  1 67  ? 108.074 108.977 -31.599 1.00 59.54 ? 40  GLU G OE2 1 
ATOM   8199  N  N   . GLY H  1 68  ? 105.940 106.581 -26.721 1.00 38.33 ? 41  GLY G N   1 
ATOM   8200  C  CA  . GLY H  1 68  ? 105.427 107.616 -25.854 1.00 39.99 ? 41  GLY G CA  1 
ATOM   8201  C  C   . GLY H  1 68  ? 104.931 107.052 -24.544 1.00 38.04 ? 41  GLY G C   1 
ATOM   8202  O  O   . GLY H  1 68  ? 105.202 105.901 -24.185 1.00 41.45 ? 41  GLY G O   1 
ATOM   8203  N  N   . LEU H  1 69  ? 104.204 107.884 -23.804 1.00 35.94 ? 42  LEU G N   1 
ATOM   8204  C  CA  . LEU H  1 69  ? 103.691 107.506 -22.497 1.00 37.20 ? 42  LEU G CA  1 
ATOM   8205  C  C   . LEU H  1 69  ? 102.338 106.821 -22.627 1.00 33.21 ? 42  LEU G C   1 
ATOM   8206  O  O   . LEU H  1 69  ? 101.536 107.157 -23.501 1.00 36.97 ? 42  LEU G O   1 
ATOM   8207  C  CB  . LEU H  1 69  ? 103.572 108.728 -21.587 1.00 34.89 ? 42  LEU G CB  1 
ATOM   8208  C  CG  . LEU H  1 69  ? 104.855 109.505 -21.328 1.00 38.31 ? 42  LEU G CG  1 
ATOM   8209  C  CD1 . LEU H  1 69  ? 104.501 110.865 -20.784 1.00 40.15 ? 42  LEU G CD1 1 
ATOM   8210  C  CD2 . LEU H  1 69  ? 105.705 108.742 -20.320 1.00 39.42 ? 42  LEU G CD2 1 
ATOM   8211  N  N   . HIS H  1 70  ? 102.095 105.849 -21.742 1.00 38.59 ? 43  HIS G N   1 
ATOM   8212  C  CA  . HIS H  1 70  ? 100.849 105.083 -21.732 1.00 33.30 ? 43  HIS G CA  1 
ATOM   8213  C  C   . HIS H  1 70  ? 100.418 104.883 -20.291 1.00 28.07 ? 43  HIS G C   1 
ATOM   8214  O  O   . HIS H  1 70  ? 101.183 104.337 -19.490 1.00 30.98 ? 43  HIS G O   1 
ATOM   8215  C  CB  . HIS H  1 70  ? 101.024 103.724 -22.424 1.00 33.82 ? 43  HIS G CB  1 
ATOM   8216  C  CG  . HIS H  1 70  ? 101.225 103.823 -23.902 1.00 35.11 ? 43  HIS G CG  1 
ATOM   8217  N  ND1 . HIS H  1 70  ? 100.177 103.817 -24.795 1.00 37.58 ? 43  HIS G ND1 1 
ATOM   8218  C  CD2 . HIS H  1 70  ? 102.354 103.930 -24.646 1.00 33.88 ? 43  HIS G CD2 1 
ATOM   8219  C  CE1 . HIS H  1 70  ? 100.649 103.924 -26.027 1.00 40.66 ? 43  HIS G CE1 1 
ATOM   8220  N  NE2 . HIS H  1 70  ? 101.968 103.990 -25.962 1.00 34.30 ? 43  HIS G NE2 1 
ATOM   8221  N  N   . GLY H  1 71  ? 99.199  105.321 -19.966 1.00 26.53 ? 44  GLY G N   1 
ATOM   8222  C  CA  . GLY H  1 71  ? 98.606  105.064 -18.664 1.00 28.70 ? 44  GLY G CA  1 
ATOM   8223  C  C   . GLY H  1 71  ? 98.691  103.597 -18.277 1.00 31.33 ? 44  GLY G C   1 
ATOM   8224  O  O   . GLY H  1 71  ? 98.582  102.711 -19.131 1.00 34.48 ? 44  GLY G O   1 
ATOM   8225  N  N   . PHE H  1 72  ? 98.858  103.337 -16.985 1.00 27.78 ? 45  PHE G N   1 
ATOM   8226  C  CA  . PHE H  1 72  ? 99.219  102.017 -16.467 1.00 29.84 ? 45  PHE G CA  1 
ATOM   8227  C  C   . PHE H  1 72  ? 98.501  101.887 -15.127 1.00 36.41 ? 45  PHE G C   1 
ATOM   8228  O  O   . PHE H  1 72  ? 98.910  102.516 -14.146 1.00 33.61 ? 45  PHE G O   1 
ATOM   8229  C  CB  . PHE H  1 72  ? 100.740 101.934 -16.332 1.00 33.35 ? 45  PHE G CB  1 
ATOM   8230  C  CG  . PHE H  1 72  ? 101.290 100.554 -16.090 1.00 32.13 ? 45  PHE G CG  1 
ATOM   8231  C  CD1 . PHE H  1 72  ? 101.182 99.551  -17.044 1.00 34.16 ? 45  PHE G CD1 1 
ATOM   8232  C  CD2 . PHE H  1 72  ? 101.982 100.288 -14.912 1.00 25.63 ? 45  PHE G CD2 1 
ATOM   8233  C  CE1 . PHE H  1 72  ? 101.733 98.287  -16.813 1.00 30.37 ? 45  PHE G CE1 1 
ATOM   8234  C  CE2 . PHE H  1 72  ? 102.524 99.043  -14.673 1.00 33.20 ? 45  PHE G CE2 1 
ATOM   8235  C  CZ  . PHE H  1 72  ? 102.399 98.037  -15.629 1.00 34.53 ? 45  PHE G CZ  1 
ATOM   8236  N  N   . HIS H  1 73  ? 97.413  101.103 -15.085 1.00 29.49 ? 46  HIS G N   1 
ATOM   8237  C  CA  . HIS H  1 73  ? 96.537  101.130 -13.923 1.00 30.79 ? 46  HIS G CA  1 
ATOM   8238  C  C   . HIS H  1 73  ? 96.057  99.732  -13.543 1.00 30.55 ? 46  HIS G C   1 
ATOM   8239  O  O   . HIS H  1 73  ? 95.781  98.896  -14.406 1.00 29.47 ? 46  HIS G O   1 
ATOM   8240  C  CB  . HIS H  1 73  ? 95.301  102.004 -14.170 1.00 31.98 ? 46  HIS G CB  1 
ATOM   8241  C  CG  . HIS H  1 73  ? 95.615  103.352 -14.735 1.00 30.85 ? 46  HIS G CG  1 
ATOM   8242  N  ND1 . HIS H  1 73  ? 95.199  103.745 -15.987 1.00 34.08 ? 46  HIS G ND1 1 
ATOM   8243  C  CD2 . HIS H  1 73  ? 96.338  104.383 -14.237 1.00 31.45 ? 46  HIS G CD2 1 
ATOM   8244  C  CE1 . HIS H  1 73  ? 95.622  104.975 -16.223 1.00 34.68 ? 46  HIS G CE1 1 
ATOM   8245  N  NE2 . HIS H  1 73  ? 96.322  105.381 -15.181 1.00 29.64 ? 46  HIS G NE2 1 
ATOM   8246  N  N   . VAL H  1 74  ? 95.911  99.509  -12.243 1.00 28.63 ? 47  VAL G N   1 
ATOM   8247  C  CA  . VAL H  1 74  ? 95.189  98.343  -11.740 1.00 29.97 ? 47  VAL G CA  1 
ATOM   8248  C  C   . VAL H  1 74  ? 93.717  98.724  -11.633 1.00 30.78 ? 47  VAL G C   1 
ATOM   8249  O  O   . VAL H  1 74  ? 93.363  99.675  -10.925 1.00 29.06 ? 47  VAL G O   1 
ATOM   8250  C  CB  . VAL H  1 74  ? 95.743  97.867  -10.386 1.00 32.16 ? 47  VAL G CB  1 
ATOM   8251  C  CG1 . VAL H  1 74  ? 94.933  96.680  -9.876  1.00 30.73 ? 47  VAL G CG1 1 
ATOM   8252  C  CG2 . VAL H  1 74  ? 97.220  97.487  -10.511 1.00 28.86 ? 47  VAL G CG2 1 
ATOM   8253  N  N   . HIS H  1 75  ? 92.867  98.005  -12.363 1.00 29.35 ? 48  HIS G N   1 
ATOM   8254  C  CA  . HIS H  1 75  ? 91.428  98.217  -12.357 1.00 29.26 ? 48  HIS G CA  1 
ATOM   8255  C  C   . HIS H  1 75  ? 90.767  97.219  -11.407 1.00 30.40 ? 48  HIS G C   1 
ATOM   8256  O  O   . HIS H  1 75  ? 91.358  96.220  -10.998 1.00 31.22 ? 48  HIS G O   1 
ATOM   8257  C  CB  . HIS H  1 75  ? 90.842  98.071  -13.768 1.00 27.73 ? 48  HIS G CB  1 
ATOM   8258  C  CG  . HIS H  1 75  ? 91.233  99.165  -14.719 1.00 27.15 ? 48  HIS G CG  1 
ATOM   8259  N  ND1 . HIS H  1 75  ? 90.306  99.933  -15.394 1.00 31.59 ? 48  HIS G ND1 1 
ATOM   8260  C  CD2 . HIS H  1 75  ? 92.449  99.580  -15.155 1.00 29.69 ? 48  HIS G CD2 1 
ATOM   8261  C  CE1 . HIS H  1 75  ? 90.931  100.792 -16.184 1.00 28.89 ? 48  HIS G CE1 1 
ATOM   8262  N  NE2 . HIS H  1 75  ? 92.232  100.598 -16.060 1.00 30.74 ? 48  HIS G NE2 1 
ATOM   8263  N  N   . GLU H  1 76  ? 89.503  97.479  -11.094 1.00 30.64 ? 49  GLU G N   1 
ATOM   8264  C  CA  . GLU H  1 76  ? 88.894  96.845  -9.931  1.00 29.26 ? 49  GLU G CA  1 
ATOM   8265  C  C   . GLU H  1 76  ? 88.680  95.345  -10.116 1.00 31.64 ? 49  GLU G C   1 
ATOM   8266  O  O   . GLU H  1 76  ? 88.921  94.564  -9.188  1.00 31.37 ? 49  GLU G O   1 
ATOM   8267  C  CB  . GLU H  1 76  ? 87.572  97.521  -9.602  1.00 30.40 ? 49  GLU G CB  1 
ATOM   8268  C  CG  . GLU H  1 76  ? 87.009  97.002  -8.302  1.00 38.75 ? 49  GLU G CG  1 
ATOM   8269  C  CD  . GLU H  1 76  ? 85.790  97.761  -7.846  1.00 45.21 ? 49  GLU G CD  1 
ATOM   8270  O  OE1 . GLU H  1 76  ? 85.301  97.468  -6.730  1.00 45.57 ? 49  GLU G OE1 1 
ATOM   8271  O  OE2 . GLU H  1 76  ? 85.334  98.652  -8.599  1.00 45.20 ? 49  GLU G OE2 1 
ATOM   8272  N  N   . PHE H  1 77  ? 88.213  94.914  -11.278 1.00 31.39 ? 50  PHE G N   1 
ATOM   8273  C  CA  . PHE H  1 77  ? 87.734  93.545  -11.420 1.00 31.87 ? 50  PHE G CA  1 
ATOM   8274  C  C   . PHE H  1 77  ? 88.663  92.719  -12.299 1.00 28.31 ? 50  PHE G C   1 
ATOM   8275  O  O   . PHE H  1 77  ? 89.148  93.191  -13.334 1.00 30.94 ? 50  PHE G O   1 
ATOM   8276  C  CB  . PHE H  1 77  ? 86.306  93.530  -11.980 1.00 32.16 ? 50  PHE G CB  1 
ATOM   8277  C  CG  . PHE H  1 77  ? 85.346  94.336  -11.153 1.00 31.68 ? 50  PHE G CG  1 
ATOM   8278  C  CD1 . PHE H  1 77  ? 85.028  93.944  -9.863  1.00 34.62 ? 50  PHE G CD1 1 
ATOM   8279  C  CD2 . PHE H  1 77  ? 84.783  95.505  -11.657 1.00 40.32 ? 50  PHE G CD2 1 
ATOM   8280  C  CE1 . PHE H  1 77  ? 84.159  94.699  -9.082  1.00 37.82 ? 50  PHE G CE1 1 
ATOM   8281  C  CE2 . PHE H  1 77  ? 83.906  96.264  -10.885 1.00 37.43 ? 50  PHE G CE2 1 
ATOM   8282  C  CZ  . PHE H  1 77  ? 83.600  95.860  -9.594  1.00 35.68 ? 50  PHE G CZ  1 
ATOM   8283  N  N   . GLY H  1 78  ? 88.894  91.474  -11.882 1.00 33.34 ? 51  GLY G N   1 
ATOM   8284  C  CA  . GLY H  1 78  ? 89.638  90.527  -12.694 1.00 32.76 ? 51  GLY G CA  1 
ATOM   8285  C  C   . GLY H  1 78  ? 88.732  89.796  -13.664 1.00 38.96 ? 51  GLY G C   1 
ATOM   8286  O  O   . GLY H  1 78  ? 88.784  88.568  -13.785 1.00 36.02 ? 51  GLY G O   1 
ATOM   8287  N  N   . ASP H  1 79  ? 87.895  90.557  -14.361 1.00 38.06 ? 52  ASP G N   1 
ATOM   8288  C  CA  . ASP H  1 79  ? 86.832  90.032  -15.208 1.00 29.98 ? 52  ASP G CA  1 
ATOM   8289  C  C   . ASP H  1 79  ? 87.189  90.382  -16.643 1.00 30.49 ? 52  ASP G C   1 
ATOM   8290  O  O   . ASP H  1 79  ? 87.147  91.552  -17.033 1.00 35.28 ? 52  ASP G O   1 
ATOM   8291  C  CB  . ASP H  1 79  ? 85.482  90.623  -14.791 1.00 34.89 ? 52  ASP G CB  1 
ATOM   8292  C  CG  . ASP H  1 79  ? 84.295  90.066  -15.592 1.00 29.60 ? 52  ASP G CG  1 
ATOM   8293  O  OD1 . ASP H  1 79  ? 84.464  89.650  -16.758 1.00 32.05 ? 52  ASP G OD1 1 
ATOM   8294  O  OD2 . ASP H  1 79  ? 83.172  90.075  -15.039 1.00 35.82 ? 52  ASP G OD2 1 
ATOM   8295  N  N   . ASN H  1 80  ? 87.533  89.362  -17.426 1.00 32.97 ? 53  ASN G N   1 
ATOM   8296  C  CA  . ASN H  1 80  ? 87.942  89.527  -18.812 1.00 37.55 ? 53  ASN G CA  1 
ATOM   8297  C  C   . ASN H  1 80  ? 86.889  88.990  -19.785 1.00 32.09 ? 53  ASN G C   1 
ATOM   8298  O  O   . ASN H  1 80  ? 87.181  88.794  -20.968 1.00 35.56 ? 53  ASN G O   1 
ATOM   8299  C  CB  . ASN H  1 80  ? 89.289  88.830  -19.023 1.00 41.31 ? 53  ASN G CB  1 
ATOM   8300  C  CG  . ASN H  1 80  ? 89.847  89.029  -20.417 1.00 50.09 ? 53  ASN G CG  1 
ATOM   8301  O  OD1 . ASN H  1 80  ? 90.224  88.065  -21.086 1.00 57.34 ? 53  ASN G OD1 1 
ATOM   8302  N  ND2 . ASN H  1 80  ? 89.912  90.282  -20.860 1.00 53.61 ? 53  ASN G ND2 1 
ATOM   8303  N  N   . THR H  1 81  ? 85.658  88.764  -19.313 1.00 37.09 ? 54  THR G N   1 
ATOM   8304  C  CA  . THR H  1 81  ? 84.638  88.178  -20.182 1.00 36.82 ? 54  THR G CA  1 
ATOM   8305  C  C   . THR H  1 81  ? 84.308  89.085  -21.358 1.00 40.96 ? 54  THR G C   1 
ATOM   8306  O  O   . THR H  1 81  ? 84.068  88.599  -22.470 1.00 40.07 ? 54  THR G O   1 
ATOM   8307  C  CB  . THR H  1 81  ? 83.361  87.878  -19.395 1.00 35.73 ? 54  THR G CB  1 
ATOM   8308  O  OG1 . THR H  1 81  ? 82.859  89.088  -18.828 1.00 38.98 ? 54  THR G OG1 1 
ATOM   8309  C  CG2 . THR H  1 81  ? 83.627  86.874  -18.283 1.00 31.62 ? 54  THR G CG2 1 
ATOM   8310  N  N   . ALA H  1 82  ? 84.286  90.400  -21.140 1.00 42.31 ? 55  ALA G N   1 
ATOM   8311  C  CA  . ALA H  1 82  ? 84.026  91.355  -22.212 1.00 44.36 ? 55  ALA G CA  1 
ATOM   8312  C  C   . ALA H  1 82  ? 85.302  92.080  -22.628 1.00 45.75 ? 55  ALA G C   1 
ATOM   8313  O  O   . ALA H  1 82  ? 85.278  93.268  -22.963 1.00 46.18 ? 55  ALA G O   1 
ATOM   8314  C  CB  . ALA H  1 82  ? 82.942  92.349  -21.794 1.00 37.88 ? 55  ALA G CB  1 
ATOM   8315  N  N   . GLY H  1 83  ? 86.429  91.372  -22.602 1.00 42.18 ? 56  GLY G N   1 
ATOM   8316  C  CA  . GLY H  1 83  ? 87.682  92.022  -22.888 1.00 38.03 ? 56  GLY G CA  1 
ATOM   8317  C  C   . GLY H  1 83  ? 88.089  92.910  -21.727 1.00 39.36 ? 56  GLY G C   1 
ATOM   8318  O  O   . GLY H  1 83  ? 87.668  92.721  -20.576 1.00 37.56 ? 56  GLY G O   1 
ATOM   8319  N  N   . CYS H  1 84  ? 88.920  93.909  -22.036 1.00 33.84 ? 57  CYS G N   1 
ATOM   8320  C  CA  . CYS H  1 84  ? 89.389  94.806  -20.990 1.00 38.51 ? 57  CYS G CA  1 
ATOM   8321  C  C   . CYS H  1 84  ? 88.262  95.670  -20.427 1.00 36.17 ? 57  CYS G C   1 
ATOM   8322  O  O   . CYS H  1 84  ? 88.386  96.182  -19.307 1.00 36.01 ? 57  CYS G O   1 
ATOM   8323  C  CB  . CYS H  1 84  ? 90.534  95.667  -21.533 1.00 38.66 ? 57  CYS G CB  1 
ATOM   8324  S  SG  . CYS H  1 84  ? 91.973  94.677  -22.053 1.00 47.49 ? 57  CYS G SG  1 
ATOM   8325  N  N   . THR H  1 85  ? 87.152  95.804  -21.161 1.00 39.14 ? 58  THR G N   1 
ATOM   8326  C  CA  . THR H  1 85  ? 86.058  96.658  -20.707 1.00 35.70 ? 58  THR G CA  1 
ATOM   8327  C  C   . THR H  1 85  ? 85.467  96.169  -19.392 1.00 36.47 ? 58  THR G C   1 
ATOM   8328  O  O   . THR H  1 85  ? 85.070  96.983  -18.551 1.00 36.37 ? 58  THR G O   1 
ATOM   8329  C  CB  . THR H  1 85  ? 84.965  96.710  -21.771 1.00 42.06 ? 58  THR G CB  1 
ATOM   8330  O  OG1 . THR H  1 85  ? 85.538  97.116  -23.020 1.00 48.84 ? 58  THR G OG1 1 
ATOM   8331  C  CG2 . THR H  1 85  ? 83.892  97.710  -21.372 1.00 46.64 ? 58  THR G CG2 1 
ATOM   8332  N  N   . SER H  1 86  ? 85.398  94.848  -19.186 1.00 29.46 ? 59  SER G N   1 
ATOM   8333  C  CA  . SER H  1 86  ? 84.737  94.328  -17.994 1.00 31.22 ? 59  SER G CA  1 
ATOM   8334  C  C   . SER H  1 86  ? 85.592  94.425  -16.739 1.00 33.39 ? 59  SER G C   1 
ATOM   8335  O  O   . SER H  1 86  ? 85.121  94.040  -15.665 1.00 32.04 ? 59  SER G O   1 
ATOM   8336  C  CB  . SER H  1 86  ? 84.295  92.869  -18.202 1.00 35.35 ? 59  SER G CB  1 
ATOM   8337  O  OG  . SER H  1 86  ? 85.213  92.131  -18.984 1.00 37.67 ? 59  SER G OG  1 
ATOM   8338  N  N   . ALA H  1 87  ? 86.823  94.941  -16.836 1.00 32.45 ? 60  ALA G N   1 
ATOM   8339  C  CA  . ALA H  1 87  ? 87.656  95.109  -15.651 1.00 27.34 ? 60  ALA G CA  1 
ATOM   8340  C  C   . ALA H  1 87  ? 87.176  96.232  -14.734 1.00 34.52 ? 60  ALA G C   1 
ATOM   8341  O  O   . ALA H  1 87  ? 87.644  96.319  -13.592 1.00 32.29 ? 60  ALA G O   1 
ATOM   8342  C  CB  . ALA H  1 87  ? 89.109  95.359  -16.067 1.00 32.48 ? 60  ALA G CB  1 
ATOM   8343  N  N   . GLY H  1 88  ? 86.268  97.089  -15.191 1.00 31.18 ? 61  GLY G N   1 
ATOM   8344  C  CA  . GLY H  1 88  ? 85.742  98.138  -14.349 1.00 32.81 ? 61  GLY G CA  1 
ATOM   8345  C  C   . GLY H  1 88  ? 86.638  99.361  -14.308 1.00 30.33 ? 61  GLY G C   1 
ATOM   8346  O  O   . GLY H  1 88  ? 87.520  99.540  -15.155 1.00 29.16 ? 61  GLY G O   1 
ATOM   8347  N  N   . PRO H  1 89  ? 86.428  100.227 -13.321 1.00 38.18 ? 62  PRO G N   1 
ATOM   8348  C  CA  . PRO H  1 89  ? 87.222  101.458 -13.207 1.00 32.57 ? 62  PRO G CA  1 
ATOM   8349  C  C   . PRO H  1 89  ? 88.533  101.184 -12.472 1.00 35.03 ? 62  PRO G C   1 
ATOM   8350  O  O   . PRO H  1 89  ? 88.830  100.054 -12.082 1.00 28.33 ? 62  PRO G O   1 
ATOM   8351  C  CB  . PRO H  1 89  ? 86.304  102.377 -12.401 1.00 38.43 ? 62  PRO G CB  1 
ATOM   8352  C  CG  . PRO H  1 89  ? 85.532  101.425 -11.501 1.00 36.08 ? 62  PRO G CG  1 
ATOM   8353  C  CD  . PRO H  1 89  ? 85.438  100.099 -12.232 1.00 35.40 ? 62  PRO G CD  1 
ATOM   8354  N  N   . HIS H  1 90  ? 89.327  102.243 -12.295 1.00 32.13 ? 63  HIS G N   1 
ATOM   8355  C  CA  . HIS H  1 90  ? 90.541  102.126 -11.493 1.00 33.40 ? 63  HIS G CA  1 
ATOM   8356  C  C   . HIS H  1 90  ? 90.202  101.619 -10.096 1.00 30.62 ? 63  HIS G C   1 
ATOM   8357  O  O   . HIS H  1 90  ? 89.200  102.019 -9.500  1.00 30.23 ? 63  HIS G O   1 
ATOM   8358  C  CB  . HIS H  1 90  ? 91.268  103.476 -11.395 1.00 33.67 ? 63  HIS G CB  1 
ATOM   8359  C  CG  . HIS H  1 90  ? 91.753  104.000 -12.711 1.00 29.90 ? 63  HIS G CG  1 
ATOM   8360  N  ND1 . HIS H  1 90  ? 92.413  105.204 -12.836 1.00 33.84 ? 63  HIS G ND1 1 
ATOM   8361  C  CD2 . HIS H  1 90  ? 91.661  103.488 -13.963 1.00 33.32 ? 63  HIS G CD2 1 
ATOM   8362  C  CE1 . HIS H  1 90  ? 92.713  105.407 -14.105 1.00 30.78 ? 63  HIS G CE1 1 
ATOM   8363  N  NE2 . HIS H  1 90  ? 92.269  104.380 -14.811 1.00 38.73 ? 63  HIS G NE2 1 
ATOM   8364  N  N   . PHE H  1 91  ? 91.031  100.706 -9.591  1.00 27.99 ? 64  PHE G N   1 
ATOM   8365  C  CA  . PHE H  1 91  ? 90.822  100.164 -8.259  1.00 32.69 ? 64  PHE G CA  1 
ATOM   8366  C  C   . PHE H  1 91  ? 90.935  101.285 -7.235  1.00 34.47 ? 64  PHE G C   1 
ATOM   8367  O  O   . PHE H  1 91  ? 92.005  101.886 -7.082  1.00 32.55 ? 64  PHE G O   1 
ATOM   8368  C  CB  . PHE H  1 91  ? 91.837  99.053  -7.989  1.00 29.18 ? 64  PHE G CB  1 
ATOM   8369  C  CG  . PHE H  1 91  ? 91.687  98.409  -6.643  1.00 35.87 ? 64  PHE G CG  1 
ATOM   8370  C  CD1 . PHE H  1 91  ? 90.434  98.146  -6.121  1.00 36.19 ? 64  PHE G CD1 1 
ATOM   8371  C  CD2 . PHE H  1 91  ? 92.801  98.055  -5.907  1.00 33.08 ? 64  PHE G CD2 1 
ATOM   8372  C  CE1 . PHE H  1 91  ? 90.296  97.546  -4.879  1.00 33.80 ? 64  PHE G CE1 1 
ATOM   8373  C  CE2 . PHE H  1 91  ? 92.669  97.453  -4.663  1.00 37.15 ? 64  PHE G CE2 1 
ATOM   8374  C  CZ  . PHE H  1 91  ? 91.413  97.200  -4.149  1.00 36.57 ? 64  PHE G CZ  1 
ATOM   8375  N  N   . ASN H  1 92  ? 89.823  101.586 -6.552  1.00 34.94 ? 65  ASN G N   1 
ATOM   8376  C  CA  . ASN H  1 92  ? 89.697  102.805 -5.746  1.00 29.92 ? 65  ASN G CA  1 
ATOM   8377  C  C   . ASN H  1 92  ? 88.932  102.534 -4.453  1.00 35.87 ? 65  ASN G C   1 
ATOM   8378  O  O   . ASN H  1 92  ? 87.868  103.113 -4.207  1.00 38.63 ? 65  ASN G O   1 
ATOM   8379  C  CB  . ASN H  1 92  ? 89.018  103.904 -6.561  1.00 33.18 ? 65  ASN G CB  1 
ATOM   8380  C  CG  . ASN H  1 92  ? 89.039  105.251 -5.862  1.00 39.96 ? 65  ASN G CG  1 
ATOM   8381  O  OD1 . ASN H  1 92  ? 89.882  105.509 -4.996  1.00 37.75 ? 65  ASN G OD1 1 
ATOM   8382  N  ND2 . ASN H  1 92  ? 88.124  106.129 -6.259  1.00 36.31 ? 65  ASN G ND2 1 
ATOM   8383  N  N   . PRO H  1 93  ? 89.486  101.697 -3.569  1.00 33.11 ? 66  PRO G N   1 
ATOM   8384  C  CA  . PRO H  1 93  ? 88.734  101.331 -2.355  1.00 38.58 ? 66  PRO G CA  1 
ATOM   8385  C  C   . PRO H  1 93  ? 88.500  102.497 -1.406  1.00 46.29 ? 66  PRO G C   1 
ATOM   8386  O  O   . PRO H  1 93  ? 87.532  102.465 -0.636  1.00 42.19 ? 66  PRO G O   1 
ATOM   8387  C  CB  . PRO H  1 93  ? 89.605  100.243 -1.712  1.00 38.11 ? 66  PRO G CB  1 
ATOM   8388  C  CG  . PRO H  1 93  ? 90.991  100.477 -2.269  1.00 37.85 ? 66  PRO G CG  1 
ATOM   8389  C  CD  . PRO H  1 93  ? 90.795  101.024 -3.645  1.00 34.74 ? 66  PRO G CD  1 
ATOM   8390  N  N   . LEU H  1 94  ? 89.342  103.529 -1.441  1.00 42.68 ? 67  LEU G N   1 
ATOM   8391  C  CA  . LEU H  1 94  ? 89.201  104.674 -0.547  1.00 38.46 ? 67  LEU G CA  1 
ATOM   8392  C  C   . LEU H  1 94  ? 88.415  105.820 -1.178  1.00 44.34 ? 67  LEU G C   1 
ATOM   8393  O  O   . LEU H  1 94  ? 88.360  106.906 -0.594  1.00 44.19 ? 67  LEU G O   1 
ATOM   8394  C  CB  . LEU H  1 94  ? 90.581  105.159 -0.097  1.00 40.61 ? 67  LEU G CB  1 
ATOM   8395  C  CG  . LEU H  1 94  ? 91.390  104.087 0.647   1.00 41.12 ? 67  LEU G CG  1 
ATOM   8396  C  CD1 . LEU H  1 94  ? 92.835  104.501 0.871   1.00 40.17 ? 67  LEU G CD1 1 
ATOM   8397  C  CD2 . LEU H  1 94  ? 90.711  103.734 1.966   1.00 42.70 ? 67  LEU G CD2 1 
ATOM   8398  N  N   . SER H  1 95  ? 87.812  105.600 -2.351  1.00 38.92 ? 68  SER G N   1 
ATOM   8399  C  CA  . SER H  1 95  ? 86.919  106.570 -3.000  1.00 41.40 ? 68  SER G CA  1 
ATOM   8400  C  C   . SER H  1 95  ? 87.586  107.935 -3.181  1.00 44.45 ? 68  SER G C   1 
ATOM   8401  O  O   . SER H  1 95  ? 87.021  108.984 -2.857  1.00 42.05 ? 68  SER G O   1 
ATOM   8402  C  CB  . SER H  1 95  ? 85.614  106.707 -2.220  1.00 46.63 ? 68  SER G CB  1 
ATOM   8403  O  OG  . SER H  1 95  ? 84.967  105.453 -2.113  1.00 55.29 ? 68  SER G OG  1 
ATOM   8404  N  N   . ARG H  1 96  ? 88.802  107.921 -3.708  1.00 39.85 ? 69  ARG G N   1 
ATOM   8405  C  CA  . ARG H  1 96  ? 89.553  109.146 -3.930  1.00 35.86 ? 69  ARG G CA  1 
ATOM   8406  C  C   . ARG H  1 96  ? 89.523  109.527 -5.411  1.00 41.45 ? 69  ARG G C   1 
ATOM   8407  O  O   . ARG H  1 96  ? 88.998  108.794 -6.251  1.00 40.29 ? 69  ARG G O   1 
ATOM   8408  C  CB  . ARG H  1 96  ? 90.982  108.975 -3.417  1.00 37.28 ? 69  ARG G CB  1 
ATOM   8409  C  CG  . ARG H  1 96  ? 91.037  108.710 -1.917  1.00 43.64 ? 69  ARG G CG  1 
ATOM   8410  C  CD  . ARG H  1 96  ? 92.225  109.404 -1.284  1.00 47.47 ? 69  ARG G CD  1 
ATOM   8411  N  NE  . ARG H  1 96  ? 93.285  108.473 -0.920  1.00 57.06 ? 69  ARG G NE  1 
ATOM   8412  C  CZ  . ARG H  1 96  ? 93.734  108.297 0.317   1.00 56.39 ? 69  ARG G CZ  1 
ATOM   8413  N  NH1 . ARG H  1 96  ? 93.254  108.999 1.333   1.00 51.45 ? 69  ARG G NH1 1 
ATOM   8414  N  NH2 . ARG H  1 96  ? 94.694  107.400 0.537   1.00 58.96 ? 69  ARG G NH2 1 
ATOM   8415  N  N   . LYS H  1 97  ? 90.046  110.717 -5.718  1.00 37.03 ? 70  LYS G N   1 
ATOM   8416  C  CA  . LYS H  1 97  ? 90.182  111.150 -7.103  1.00 34.54 ? 70  LYS G CA  1 
ATOM   8417  C  C   . LYS H  1 97  ? 91.456  110.583 -7.714  1.00 32.88 ? 70  LYS G C   1 
ATOM   8418  O  O   . LYS H  1 97  ? 92.396  110.194 -7.015  1.00 37.69 ? 70  LYS G O   1 
ATOM   8419  C  CB  . LYS H  1 97  ? 90.209  112.677 -7.214  1.00 35.49 ? 70  LYS G CB  1 
ATOM   8420  C  CG  . LYS H  1 97  ? 88.930  113.360 -6.796  1.00 41.73 ? 70  LYS G CG  1 
ATOM   8421  C  CD  . LYS H  1 97  ? 88.859  114.781 -7.335  1.00 46.35 ? 70  LYS G CD  1 
ATOM   8422  C  CE  . LYS H  1 97  ? 89.860  115.678 -6.610  1.00 50.65 ? 70  LYS G CE  1 
ATOM   8423  N  NZ  . LYS H  1 97  ? 89.507  117.138 -6.663  1.00 51.47 ? 70  LYS G NZ  1 
ATOM   8424  N  N   . HIS H  1 98  ? 91.484  110.564 -9.046  1.00 31.86 ? 71  HIS G N   1 
ATOM   8425  C  CA  . HIS H  1 98  ? 92.628  110.033 -9.772  1.00 31.09 ? 71  HIS G CA  1 
ATOM   8426  C  C   . HIS H  1 98  ? 93.841  110.948 -9.610  1.00 34.68 ? 71  HIS G C   1 
ATOM   8427  O  O   . HIS H  1 98  ? 93.724  112.175 -9.615  1.00 34.76 ? 71  HIS G O   1 
ATOM   8428  C  CB  . HIS H  1 98  ? 92.264  109.859 -11.258 1.00 29.84 ? 71  HIS G CB  1 
ATOM   8429  C  CG  . HIS H  1 98  ? 93.406  109.426 -12.120 1.00 30.87 ? 71  HIS G CG  1 
ATOM   8430  N  ND1 . HIS H  1 98  ? 93.770  108.104 -12.261 1.00 36.49 ? 71  HIS G ND1 1 
ATOM   8431  C  CD2 . HIS H  1 98  ? 94.251  110.134 -12.908 1.00 29.58 ? 71  HIS G CD2 1 
ATOM   8432  C  CE1 . HIS H  1 98  ? 94.799  108.018 -13.084 1.00 26.78 ? 71  HIS G CE1 1 
ATOM   8433  N  NE2 . HIS H  1 98  ? 95.110  109.236 -13.493 1.00 29.84 ? 71  HIS G NE2 1 
ATOM   8434  N  N   . GLY H  1 99  ? 95.014  110.343 -9.446  1.00 36.48 ? 72  GLY G N   1 
ATOM   8435  C  CA  . GLY H  1 99  ? 96.235  111.120 -9.416  1.00 33.06 ? 72  GLY G CA  1 
ATOM   8436  C  C   . GLY H  1 99  ? 97.408  110.347 -9.972  1.00 37.94 ? 72  GLY G C   1 
ATOM   8437  O  O   . GLY H  1 99  ? 97.234  109.253 -10.522 1.00 30.54 ? 72  GLY G O   1 
ATOM   8438  N  N   . GLY H  1 100 ? 98.606  110.911 -9.860  1.00 32.55 ? 73  GLY G N   1 
ATOM   8439  C  CA  . GLY H  1 100 ? 99.813  110.168 -10.145 1.00 28.47 ? 73  GLY G CA  1 
ATOM   8440  C  C   . GLY H  1 100 ? 100.231 109.342 -8.949  1.00 31.09 ? 73  GLY G C   1 
ATOM   8441  O  O   . GLY H  1 100 ? 99.762  109.536 -7.811  1.00 32.74 ? 73  GLY G O   1 
ATOM   8442  N  N   . PRO H  1 101 ? 101.139 108.390 -9.181  1.00 30.61 ? 74  PRO G N   1 
ATOM   8443  C  CA  . PRO H  1 101 ? 101.539 107.498 -8.076  1.00 35.07 ? 74  PRO G CA  1 
ATOM   8444  C  C   . PRO H  1 101 ? 102.172 108.223 -6.896  1.00 40.67 ? 74  PRO G C   1 
ATOM   8445  O  O   . PRO H  1 101 ? 102.104 107.713 -5.772  1.00 38.14 ? 74  PRO G O   1 
ATOM   8446  C  CB  . PRO H  1 101 ? 102.522 106.521 -8.736  1.00 29.86 ? 74  PRO G CB  1 
ATOM   8447  C  CG  . PRO H  1 101 ? 102.864 107.115 -10.060 1.00 32.87 ? 74  PRO G CG  1 
ATOM   8448  C  CD  . PRO H  1 101 ? 101.718 107.983 -10.467 1.00 31.95 ? 74  PRO G CD  1 
ATOM   8449  N  N   . LYS H  1 102 ? 102.758 109.401 -7.101  1.00 38.60 ? 75  LYS G N   1 
ATOM   8450  C  CA  . LYS H  1 102 ? 103.403 110.133 -6.017  1.00 38.51 ? 75  LYS G CA  1 
ATOM   8451  C  C   . LYS H  1 102 ? 102.439 110.999 -5.213  1.00 40.01 ? 75  LYS G C   1 
ATOM   8452  O  O   . LYS H  1 102 ? 102.828 111.511 -4.161  1.00 39.00 ? 75  LYS G O   1 
ATOM   8453  C  CB  . LYS H  1 102 ? 104.538 111.002 -6.577  1.00 39.93 ? 75  LYS G CB  1 
ATOM   8454  C  CG  . LYS H  1 102 ? 105.694 110.205 -7.193  1.00 42.71 ? 75  LYS G CG  1 
ATOM   8455  C  CD  . LYS H  1 102 ? 106.833 111.128 -7.687  1.00 49.50 ? 75  LYS G CD  1 
ATOM   8456  C  CE  . LYS H  1 102 ? 108.147 110.359 -7.916  1.00 58.57 ? 75  LYS G CE  1 
ATOM   8457  N  NZ  . LYS H  1 102 ? 108.353 109.862 -9.323  1.00 54.21 ? 75  LYS G NZ  1 
ATOM   8458  N  N   . ASP H  1 103 ? 101.201 111.169 -5.669  1.00 38.50 ? 76  ASP G N   1 
ATOM   8459  C  CA  . ASP H  1 103 ? 100.226 112.009 -4.988  1.00 34.59 ? 76  ASP G CA  1 
ATOM   8460  C  C   . ASP H  1 103 ? 99.563  111.259 -3.838  1.00 42.87 ? 76  ASP G C   1 
ATOM   8461  O  O   . ASP H  1 103 ? 99.347  110.045 -3.907  1.00 44.04 ? 76  ASP G O   1 
ATOM   8462  C  CB  . ASP H  1 103 ? 99.154  112.492 -5.970  1.00 35.10 ? 76  ASP G CB  1 
ATOM   8463  C  CG  . ASP H  1 103 ? 99.728  113.325 -7.094  1.00 40.95 ? 76  ASP G CG  1 
ATOM   8464  O  OD1 . ASP H  1 103 ? 100.768 113.973 -6.855  1.00 47.74 ? 76  ASP G OD1 1 
ATOM   8465  O  OD2 . ASP H  1 103 ? 99.157  113.317 -8.212  1.00 37.33 ? 76  ASP G OD2 1 
ATOM   8466  N  N   . GLU H  1 104 ? 99.234  111.998 -2.773  1.00 41.39 ? 77  GLU G N   1 
ATOM   8467  C  CA  . GLU H  1 104 ? 98.393  111.421 -1.727  1.00 43.06 ? 77  GLU G CA  1 
ATOM   8468  C  C   . GLU H  1 104 ? 97.009  111.110 -2.276  1.00 45.73 ? 77  GLU G C   1 
ATOM   8469  O  O   . GLU H  1 104 ? 96.484  110.007 -2.085  1.00 50.81 ? 77  GLU G O   1 
ATOM   8470  C  CB  . GLU H  1 104 ? 98.289  112.366 -0.523  1.00 44.56 ? 77  GLU G CB  1 
ATOM   8471  C  CG  . GLU H  1 104 ? 97.843  111.677 0.797   1.00 50.65 ? 77  GLU G CG  1 
ATOM   8472  C  CD  . GLU H  1 104 ? 96.316  111.617 1.008   1.00 64.87 ? 77  GLU G CD  1 
ATOM   8473  O  OE1 . GLU H  1 104 ? 95.542  111.764 0.033   1.00 68.68 ? 77  GLU G OE1 1 
ATOM   8474  O  OE2 . GLU H  1 104 ? 95.883  111.401 2.168   1.00 68.92 ? 77  GLU G OE2 1 
ATOM   8475  N  N   . GLU H  1 105 ? 96.403  112.078 -2.962  1.00 44.27 ? 78  GLU G N   1 
ATOM   8476  C  CA  . GLU H  1 105 ? 95.062  111.922 -3.512  1.00 38.85 ? 78  GLU G CA  1 
ATOM   8477  C  C   . GLU H  1 105 ? 95.194  111.151 -4.817  1.00 42.05 ? 78  GLU G C   1 
ATOM   8478  O  O   . GLU H  1 105 ? 95.505  111.728 -5.860  1.00 37.31 ? 78  GLU G O   1 
ATOM   8479  C  CB  . GLU H  1 105 ? 94.405  113.280 -3.734  1.00 36.11 ? 78  GLU G CB  1 
ATOM   8480  C  CG  . GLU H  1 105 ? 93.084  113.198 -4.467  1.00 39.34 ? 78  GLU G CG  1 
ATOM   8481  C  CD  . GLU H  1 105 ? 91.942  112.789 -3.538  1.00 53.16 ? 78  GLU G CD  1 
ATOM   8482  O  OE1 . GLU H  1 105 ? 92.210  112.441 -2.361  1.00 62.92 ? 78  GLU G OE1 1 
ATOM   8483  O  OE2 . GLU H  1 105 ? 90.778  112.792 -3.992  1.00 51.79 ? 78  GLU G OE2 1 
ATOM   8484  N  N   . ARG H  1 106 ? 94.989  109.836 -4.750  1.00 39.98 ? 79  ARG G N   1 
ATOM   8485  C  CA  . ARG H  1 106 ? 95.094  108.962 -5.912  1.00 38.35 ? 79  ARG G CA  1 
ATOM   8486  C  C   . ARG H  1 106 ? 94.224  107.736 -5.673  1.00 37.70 ? 79  ARG G C   1 
ATOM   8487  O  O   . ARG H  1 106 ? 93.826  107.441 -4.541  1.00 36.62 ? 79  ARG G O   1 
ATOM   8488  C  CB  . ARG H  1 106 ? 96.540  108.520 -6.161  1.00 36.75 ? 79  ARG G CB  1 
ATOM   8489  C  CG  . ARG H  1 106 ? 97.150  107.799 -4.946  1.00 32.92 ? 79  ARG G CG  1 
ATOM   8490  C  CD  . ARG H  1 106 ? 98.462  107.106 -5.281  1.00 31.99 ? 79  ARG G CD  1 
ATOM   8491  N  NE  . ARG H  1 106 ? 98.302  105.717 -5.708  1.00 31.85 ? 79  ARG G NE  1 
ATOM   8492  C  CZ  . ARG H  1 106 ? 99.314  104.877 -5.888  1.00 34.54 ? 79  ARG G CZ  1 
ATOM   8493  N  NH1 . ARG H  1 106 ? 100.568 105.260 -5.719  1.00 37.05 ? 79  ARG G NH1 1 
ATOM   8494  N  NH2 . ARG H  1 106 ? 99.064  103.617 -6.233  1.00 33.23 ? 79  ARG G NH2 1 
ATOM   8495  N  N   . HIS H  1 107 ? 93.948  107.020 -6.755  1.00 30.97 ? 80  HIS G N   1 
ATOM   8496  C  CA  . HIS H  1 107 ? 93.403  105.676 -6.637  1.00 32.39 ? 80  HIS G CA  1 
ATOM   8497  C  C   . HIS H  1 107 ? 94.508  104.714 -6.215  1.00 35.20 ? 80  HIS G C   1 
ATOM   8498  O  O   . HIS H  1 107 ? 95.686  104.912 -6.527  1.00 34.01 ? 80  HIS G O   1 
ATOM   8499  C  CB  . HIS H  1 107 ? 92.797  105.236 -7.969  1.00 31.44 ? 80  HIS G CB  1 
ATOM   8500  C  CG  . HIS H  1 107 ? 91.728  106.154 -8.466  1.00 28.71 ? 80  HIS G CG  1 
ATOM   8501  N  ND1 . HIS H  1 107 ? 91.517  106.402 -9.805  1.00 32.84 ? 80  HIS G ND1 1 
ATOM   8502  C  CD2 . HIS H  1 107 ? 90.807  106.888 -7.798  1.00 31.09 ? 80  HIS G CD2 1 
ATOM   8503  C  CE1 . HIS H  1 107 ? 90.509  107.246 -9.941  1.00 27.51 ? 80  HIS G CE1 1 
ATOM   8504  N  NE2 . HIS H  1 107 ? 90.059  107.555 -8.737  1.00 36.28 ? 80  HIS G NE2 1 
ATOM   8505  N  N   . VAL H  1 108 ? 94.127  103.664 -5.488  1.00 30.46 ? 81  VAL G N   1 
ATOM   8506  C  CA  . VAL H  1 108 ? 95.101  102.623 -5.179  1.00 28.81 ? 81  VAL G CA  1 
ATOM   8507  C  C   . VAL H  1 108 ? 95.747  102.097 -6.458  1.00 30.32 ? 81  VAL G C   1 
ATOM   8508  O  O   . VAL H  1 108 ? 96.959  101.866 -6.507  1.00 34.25 ? 81  VAL G O   1 
ATOM   8509  C  CB  . VAL H  1 108 ? 94.443  101.494 -4.363  1.00 35.34 ? 81  VAL G CB  1 
ATOM   8510  C  CG1 . VAL H  1 108 ? 95.306  100.233 -4.393  1.00 34.50 ? 81  VAL G CG1 1 
ATOM   8511  C  CG2 . VAL H  1 108 ? 94.206  101.951 -2.940  1.00 32.01 ? 81  VAL G CG2 1 
ATOM   8512  N  N   . GLY H  1 109 ? 94.957  101.929 -7.526  1.00 32.63 ? 82  GLY G N   1 
ATOM   8513  C  CA  . GLY H  1 109 ? 95.465  101.410 -8.786  1.00 29.27 ? 82  GLY G CA  1 
ATOM   8514  C  C   . GLY H  1 109 ? 96.208  102.388 -9.678  1.00 33.27 ? 82  GLY G C   1 
ATOM   8515  O  O   . GLY H  1 109 ? 96.533  102.052 -10.820 1.00 29.42 ? 82  GLY G O   1 
ATOM   8516  N  N   . ASP H  1 110 ? 96.512  103.592 -9.198  1.00 32.61 ? 83  ASP G N   1 
ATOM   8517  C  CA  . ASP H  1 110 ? 97.119  104.616 -10.053 1.00 33.92 ? 83  ASP G CA  1 
ATOM   8518  C  C   . ASP H  1 110 ? 98.635  104.468 -10.055 1.00 34.29 ? 83  ASP G C   1 
ATOM   8519  O  O   . ASP H  1 110 ? 99.344  105.002 -9.201  1.00 35.53 ? 83  ASP G O   1 
ATOM   8520  C  CB  . ASP H  1 110 ? 96.675  105.997 -9.602  1.00 29.01 ? 83  ASP G CB  1 
ATOM   8521  C  CG  . ASP H  1 110 ? 95.262  106.286 -10.030 1.00 29.27 ? 83  ASP G CG  1 
ATOM   8522  O  OD1 . ASP H  1 110 ? 94.737  105.482 -10.837 1.00 34.86 ? 83  ASP G OD1 1 
ATOM   8523  O  OD2 . ASP H  1 110 ? 94.651  107.276 -9.583  1.00 30.62 ? 83  ASP G OD2 1 
ATOM   8524  N  N   . LEU H  1 111 ? 99.140  103.741 -11.044 1.00 27.86 ? 84  LEU G N   1 
ATOM   8525  C  CA  . LEU H  1 111 ? 100.568 103.499 -11.176 1.00 32.45 ? 84  LEU G CA  1 
ATOM   8526  C  C   . LEU H  1 111 ? 101.226 104.414 -12.202 1.00 29.78 ? 84  LEU G C   1 
ATOM   8527  O  O   . LEU H  1 111 ? 102.388 104.195 -12.546 1.00 34.47 ? 84  LEU G O   1 
ATOM   8528  C  CB  . LEU H  1 111 ? 100.821 102.031 -11.534 1.00 30.66 ? 84  LEU G CB  1 
ATOM   8529  C  CG  . LEU H  1 111 ? 100.424 101.051 -10.419 1.00 31.69 ? 84  LEU G CG  1 
ATOM   8530  C  CD1 . LEU H  1 111 ? 100.717 99.603  -10.804 1.00 33.05 ? 84  LEU G CD1 1 
ATOM   8531  C  CD2 . LEU H  1 111 ? 101.127 101.406 -9.113  1.00 33.69 ? 84  LEU G CD2 1 
ATOM   8532  N  N   . GLY H  1 112 ? 100.510 105.424 -12.703 1.00 29.03 ? 85  GLY G N   1 
ATOM   8533  C  CA  . GLY H  1 112 ? 101.098 106.410 -13.600 1.00 30.73 ? 85  GLY G CA  1 
ATOM   8534  C  C   . GLY H  1 112 ? 101.260 105.975 -15.040 1.00 31.49 ? 85  GLY G C   1 
ATOM   8535  O  O   . GLY H  1 112 ? 100.368 105.332 -15.605 1.00 31.79 ? 85  GLY G O   1 
ATOM   8536  N  N   . ASN H  1 113 ? 102.392 106.327 -15.652 1.00 25.86 ? 86  ASN G N   1 
ATOM   8537  C  CA  . ASN H  1 113 ? 102.667 106.022 -17.048 1.00 27.88 ? 86  ASN G CA  1 
ATOM   8538  C  C   . ASN H  1 113 ? 103.836 105.047 -17.184 1.00 29.13 ? 86  ASN G C   1 
ATOM   8539  O  O   . ASN H  1 113 ? 104.707 104.942 -16.309 1.00 32.27 ? 86  ASN G O   1 
ATOM   8540  C  CB  . ASN H  1 113 ? 103.004 107.296 -17.852 1.00 30.21 ? 86  ASN G CB  1 
ATOM   8541  C  CG  . ASN H  1 113 ? 101.812 108.202 -18.051 1.00 35.42 ? 86  ASN G CG  1 
ATOM   8542  O  OD1 . ASN H  1 113 ? 100.859 107.855 -18.762 1.00 33.22 ? 86  ASN G OD1 1 
ATOM   8543  N  ND2 . ASN H  1 113 ? 101.867 109.398 -17.447 1.00 31.64 ? 86  ASN G ND2 1 
ATOM   8544  N  N   . VAL H  1 114 ? 103.852 104.349 -18.316 1.00 32.26 ? 87  VAL G N   1 
ATOM   8545  C  CA  . VAL H  1 114 ? 105.017 103.609 -18.776 1.00 33.25 ? 87  VAL G CA  1 
ATOM   8546  C  C   . VAL H  1 114 ? 105.390 104.172 -20.143 1.00 32.77 ? 87  VAL G C   1 
ATOM   8547  O  O   . VAL H  1 114 ? 104.565 104.774 -20.831 1.00 36.48 ? 87  VAL G O   1 
ATOM   8548  C  CB  . VAL H  1 114 ? 104.761 102.086 -18.842 1.00 32.00 ? 87  VAL G CB  1 
ATOM   8549  C  CG1 . VAL H  1 114 ? 104.545 101.530 -17.434 1.00 28.24 ? 87  VAL G CG1 1 
ATOM   8550  C  CG2 . VAL H  1 114 ? 103.573 101.776 -19.751 1.00 36.80 ? 87  VAL G CG2 1 
ATOM   8551  N  N   . THR H  1 115 ? 106.652 103.979 -20.530 1.00 36.80 ? 88  THR G N   1 
ATOM   8552  C  CA  . THR H  1 115 ? 107.239 104.640 -21.693 1.00 35.58 ? 88  THR G CA  1 
ATOM   8553  C  C   . THR H  1 115 ? 107.632 103.615 -22.748 1.00 34.44 ? 88  THR G C   1 
ATOM   8554  O  O   . THR H  1 115 ? 108.462 102.740 -22.486 1.00 39.71 ? 88  THR G O   1 
ATOM   8555  C  CB  . THR H  1 115 ? 108.474 105.454 -21.293 1.00 39.00 ? 88  THR G CB  1 
ATOM   8556  O  OG1 . THR H  1 115 ? 108.124 106.377 -20.262 1.00 36.30 ? 88  THR G OG1 1 
ATOM   8557  C  CG2 . THR H  1 115 ? 109.013 106.223 -22.488 1.00 37.44 ? 88  THR G CG2 1 
ATOM   8558  N  N   . ALA H  1 116 ? 107.075 103.748 -23.945 1.00 38.61 ? 89  ALA G N   1 
ATOM   8559  C  CA  . ALA H  1 116 ? 107.438 102.897 -25.069 1.00 41.64 ? 89  ALA G CA  1 
ATOM   8560  C  C   . ALA H  1 116 ? 108.429 103.621 -25.973 1.00 46.87 ? 89  ALA G C   1 
ATOM   8561  O  O   . ALA H  1 116 ? 108.224 104.786 -26.319 1.00 47.55 ? 89  ALA G O   1 
ATOM   8562  C  CB  . ALA H  1 116 ? 106.202 102.499 -25.878 1.00 38.43 ? 89  ALA G CB  1 
ATOM   8563  N  N   . ASP H  1 117 ? 109.487 102.913 -26.381 1.00 51.06 ? 90  ASP G N   1 
ATOM   8564  C  CA  . ASP H  1 117 ? 110.546 103.495 -27.202 1.00 45.23 ? 90  ASP G CA  1 
ATOM   8565  C  C   . ASP H  1 117 ? 110.120 103.557 -28.672 1.00 51.29 ? 90  ASP G C   1 
ATOM   8566  O  O   . ASP H  1 117 ? 108.973 103.268 -29.027 1.00 47.31 ? 90  ASP G O   1 
ATOM   8567  C  CB  . ASP H  1 117 ? 111.851 102.718 -27.015 1.00 45.49 ? 90  ASP G CB  1 
ATOM   8568  C  CG  . ASP H  1 117 ? 111.763 101.260 -27.485 1.00 55.72 ? 90  ASP G CG  1 
ATOM   8569  O  OD1 . ASP H  1 117 ? 110.791 100.887 -28.183 1.00 54.96 ? 90  ASP G OD1 1 
ATOM   8570  O  OD2 . ASP H  1 117 ? 112.685 100.478 -27.155 1.00 54.16 ? 90  ASP G OD2 1 
ATOM   8571  N  N   . LYS H  1 118 ? 111.062 103.944 -29.545 1.00 50.53 ? 91  LYS G N   1 
ATOM   8572  C  CA  . LYS H  1 118 ? 110.808 103.980 -30.985 1.00 51.05 ? 91  LYS G CA  1 
ATOM   8573  C  C   . LYS H  1 118 ? 110.371 102.621 -31.514 1.00 45.70 ? 91  LYS G C   1 
ATOM   8574  O  O   . LYS H  1 118 ? 109.604 102.547 -32.484 1.00 51.06 ? 91  LYS G O   1 
ATOM   8575  C  CB  . LYS H  1 118 ? 112.071 104.431 -31.727 1.00 48.79 ? 91  LYS G CB  1 
ATOM   8576  C  CG  . LYS H  1 118 ? 113.344 103.812 -31.130 1.00 46.58 ? 91  LYS G CG  1 
ATOM   8577  C  CD  . LYS H  1 118 ? 114.636 104.426 -31.677 1.00 51.52 ? 91  LYS G CD  1 
ATOM   8578  C  CE  . LYS H  1 118 ? 115.633 103.324 -32.046 1.00 46.67 ? 91  LYS G CE  1 
ATOM   8579  N  NZ  . LYS H  1 118 ? 116.949 103.861 -32.525 1.00 57.58 ? 91  LYS G NZ  1 
ATOM   8580  N  N   . ASP H  1 119 ? 110.867 101.540 -30.904 1.00 48.43 ? 92  ASP G N   1 
ATOM   8581  C  CA  . ASP H  1 119 ? 110.547 100.176 -31.306 1.00 54.14 ? 92  ASP G CA  1 
ATOM   8582  C  C   . ASP H  1 119 ? 109.166 99.728  -30.847 1.00 53.26 ? 92  ASP G C   1 
ATOM   8583  O  O   . ASP H  1 119 ? 108.674 98.697  -31.323 1.00 54.72 ? 92  ASP G O   1 
ATOM   8584  C  CB  . ASP H  1 119 ? 111.599 99.216  -30.750 1.00 48.50 ? 92  ASP G CB  1 
ATOM   8585  C  CG  . ASP H  1 119 ? 112.955 99.395  -31.418 1.00 67.01 ? 92  ASP G CG  1 
ATOM   8586  O  OD1 . ASP H  1 119 ? 112.988 99.693  -32.633 1.00 68.67 ? 92  ASP G OD1 1 
ATOM   8587  O  OD2 . ASP H  1 119 ? 113.987 99.257  -30.722 1.00 62.24 ? 92  ASP G OD2 1 
ATOM   8588  N  N   . GLY H  1 120 ? 108.531 100.469 -29.945 1.00 52.75 ? 93  GLY G N   1 
ATOM   8589  C  CA  . GLY H  1 120 ? 107.258 100.068 -29.397 1.00 44.28 ? 93  GLY G CA  1 
ATOM   8590  C  C   . GLY H  1 120 ? 107.350 99.228  -28.150 1.00 44.05 ? 93  GLY G C   1 
ATOM   8591  O  O   . GLY H  1 120 ? 106.335 98.663  -27.726 1.00 46.20 ? 93  GLY G O   1 
ATOM   8592  N  N   . VAL H  1 121 ? 108.530 99.121  -27.550 1.00 43.30 ? 94  VAL G N   1 
ATOM   8593  C  CA  . VAL H  1 121 ? 108.734 98.335  -26.343 1.00 42.74 ? 94  VAL G CA  1 
ATOM   8594  C  C   . VAL H  1 121 ? 108.766 99.274  -25.150 1.00 41.28 ? 94  VAL G C   1 
ATOM   8595  O  O   . VAL H  1 121 ? 109.422 100.323 -25.191 1.00 47.31 ? 94  VAL G O   1 
ATOM   8596  C  CB  . VAL H  1 121 ? 110.033 97.512  -26.424 1.00 41.88 ? 94  VAL G CB  1 
ATOM   8597  C  CG1 . VAL H  1 121 ? 110.181 96.640  -25.187 1.00 40.18 ? 94  VAL G CG1 1 
ATOM   8598  C  CG2 . VAL H  1 121 ? 110.037 96.672  -27.695 1.00 37.53 ? 94  VAL G CG2 1 
ATOM   8599  N  N   . ALA H  1 122 ? 108.060 98.902  -24.090 1.00 35.62 ? 95  ALA G N   1 
ATOM   8600  C  CA  . ALA H  1 122 ? 108.151 99.582  -22.806 1.00 36.61 ? 95  ALA G CA  1 
ATOM   8601  C  C   . ALA H  1 122 ? 108.748 98.608  -21.802 1.00 41.69 ? 95  ALA G C   1 
ATOM   8602  O  O   . ALA H  1 122 ? 108.122 97.600  -21.453 1.00 43.23 ? 95  ALA G O   1 
ATOM   8603  C  CB  . ALA H  1 122 ? 106.781 100.075 -22.340 1.00 39.21 ? 95  ALA G CB  1 
ATOM   8604  N  N   . ASP H  1 123 ? 109.970 98.882  -21.368 1.00 40.65 ? 96  ASP G N   1 
ATOM   8605  C  CA  . ASP H  1 123 ? 110.480 98.244  -20.169 1.00 41.21 ? 96  ASP G CA  1 
ATOM   8606  C  C   . ASP H  1 123 ? 109.861 98.962  -18.987 1.00 41.03 ? 96  ASP G C   1 
ATOM   8607  O  O   . ASP H  1 123 ? 109.793 100.194 -18.971 1.00 43.91 ? 96  ASP G O   1 
ATOM   8608  C  CB  . ASP H  1 123 ? 112.010 98.303  -20.115 1.00 46.19 ? 96  ASP G CB  1 
ATOM   8609  C  CG  . ASP H  1 123 ? 112.667 97.615  -21.307 1.00 56.13 ? 96  ASP G CG  1 
ATOM   8610  O  OD1 . ASP H  1 123 ? 112.075 96.655  -21.856 1.00 58.67 ? 96  ASP G OD1 1 
ATOM   8611  O  OD2 . ASP H  1 123 ? 113.787 98.027  -21.693 1.00 69.35 ? 96  ASP G OD2 1 
ATOM   8612  N  N   . VAL H  1 124 ? 109.355 98.198  -18.028 1.00 38.49 ? 97  VAL G N   1 
ATOM   8613  C  CA  . VAL H  1 124 ? 108.629 98.747  -16.896 1.00 35.10 ? 97  VAL G CA  1 
ATOM   8614  C  C   . VAL H  1 124 ? 109.424 98.451  -15.637 1.00 40.33 ? 97  VAL G C   1 
ATOM   8615  O  O   . VAL H  1 124 ? 109.911 97.328  -15.456 1.00 43.40 ? 97  VAL G O   1 
ATOM   8616  C  CB  . VAL H  1 124 ? 107.206 98.161  -16.801 1.00 33.89 ? 97  VAL G CB  1 
ATOM   8617  C  CG1 . VAL H  1 124 ? 106.519 98.605  -15.515 1.00 35.55 ? 97  VAL G CG1 1 
ATOM   8618  C  CG2 . VAL H  1 124 ? 106.398 98.527  -18.033 1.00 33.79 ? 97  VAL G CG2 1 
ATOM   8619  N  N   . SER H  1 125 ? 109.553 99.459  -14.774 1.00 36.79 ? 98  SER G N   1 
ATOM   8620  C  CA  . SER H  1 125 ? 110.203 99.298  -13.478 1.00 37.72 ? 98  SER G CA  1 
ATOM   8621  C  C   . SER H  1 125 ? 109.658 100.376 -12.554 1.00 37.77 ? 98  SER G C   1 
ATOM   8622  O  O   . SER H  1 125 ? 110.020 101.549 -12.683 1.00 38.67 ? 98  SER G O   1 
ATOM   8623  C  CB  . SER H  1 125 ? 111.721 99.381  -13.596 1.00 41.35 ? 98  SER G CB  1 
ATOM   8624  O  OG  . SER H  1 125 ? 112.324 98.574  -12.600 1.00 48.86 ? 98  SER G OG  1 
ATOM   8625  N  N   . ILE H  1 126 ? 108.807 99.967  -11.622 1.00 37.76 ? 99  ILE G N   1 
ATOM   8626  C  CA  . ILE H  1 126 ? 108.063 100.859 -10.751 1.00 29.91 ? 99  ILE G CA  1 
ATOM   8627  C  C   . ILE H  1 126 ? 108.128 100.280 -9.343  1.00 37.02 ? 99  ILE G C   1 
ATOM   8628  O  O   . ILE H  1 126 ? 108.167 99.060  -9.157  1.00 37.45 ? 99  ILE G O   1 
ATOM   8629  C  CB  . ILE H  1 126 ? 106.597 100.993 -11.261 1.00 36.08 ? 99  ILE G CB  1 
ATOM   8630  C  CG1 . ILE H  1 126 ? 106.551 101.676 -12.631 1.00 41.90 ? 99  ILE G CG1 1 
ATOM   8631  C  CG2 . ILE H  1 126 ? 105.704 101.703 -10.276 1.00 38.30 ? 99  ILE G CG2 1 
ATOM   8632  C  CD1 . ILE H  1 126 ? 105.134 102.060 -13.070 1.00 40.96 ? 99  ILE G CD1 1 
ATOM   8633  N  N   . GLU H  1 127 ? 108.171 101.159 -8.344  1.00 31.16 ? 100 GLU G N   1 
ATOM   8634  C  CA  . GLU H  1 127 ? 108.065 100.759 -6.952  1.00 39.79 ? 100 GLU G CA  1 
ATOM   8635  C  C   . GLU H  1 127 ? 106.921 101.547 -6.335  1.00 42.60 ? 100 GLU G C   1 
ATOM   8636  O  O   . GLU H  1 127 ? 106.873 102.775 -6.458  1.00 43.88 ? 100 GLU G O   1 
ATOM   8637  C  CB  . GLU H  1 127 ? 109.381 101.004 -6.192  1.00 38.92 ? 100 GLU G CB  1 
ATOM   8638  C  CG  . GLU H  1 127 ? 109.288 100.705 -4.708  1.00 48.40 ? 100 GLU G CG  1 
ATOM   8639  C  CD  . GLU H  1 127 ? 110.643 100.422 -4.078  1.00 61.16 ? 100 GLU G CD  1 
ATOM   8640  O  OE1 . GLU H  1 127 ? 111.474 99.731  -4.714  1.00 61.36 ? 100 GLU G OE1 1 
ATOM   8641  O  OE2 . GLU H  1 127 ? 110.874 100.892 -2.943  1.00 61.59 ? 100 GLU G OE2 1 
ATOM   8642  N  N   . ASP H  1 128 ? 105.991 100.844 -5.697  1.00 39.74 ? 101 ASP G N   1 
ATOM   8643  C  CA  . ASP H  1 128 ? 104.798 101.491 -5.185  1.00 37.32 ? 101 ASP G CA  1 
ATOM   8644  C  C   . ASP H  1 128 ? 104.473 100.952 -3.807  1.00 38.51 ? 101 ASP G C   1 
ATOM   8645  O  O   . ASP H  1 128 ? 104.613 99.756  -3.549  1.00 50.00 ? 101 ASP G O   1 
ATOM   8646  C  CB  . ASP H  1 128 ? 103.591 101.293 -6.123  1.00 37.61 ? 101 ASP G CB  1 
ATOM   8647  C  CG  . ASP H  1 128 ? 102.464 102.272 -5.829  1.00 42.07 ? 101 ASP G CG  1 
ATOM   8648  O  OD1 . ASP H  1 128 ? 102.517 103.416 -6.333  1.00 52.90 ? 101 ASP G OD1 1 
ATOM   8649  O  OD2 . ASP H  1 128 ? 101.525 101.906 -5.092  1.00 42.38 ? 101 ASP G OD2 1 
ATOM   8650  N  N   . SER H  1 129 ? 104.017 101.844 -2.933  1.00 41.48 ? 102 SER G N   1 
ATOM   8651  C  CA  . SER H  1 129 ? 103.720 101.498 -1.557  1.00 41.67 ? 102 SER G CA  1 
ATOM   8652  C  C   . SER H  1 129 ? 102.235 101.507 -1.246  1.00 38.77 ? 102 SER G C   1 
ATOM   8653  O  O   . SER H  1 129 ? 101.854 101.132 -0.132  1.00 49.77 ? 102 SER G O   1 
ATOM   8654  C  CB  . SER H  1 129 ? 104.447 102.463 -0.610  1.00 45.80 ? 102 SER G CB  1 
ATOM   8655  O  OG  . SER H  1 129 ? 105.804 102.079 -0.477  1.00 58.31 ? 102 SER G OG  1 
ATOM   8656  N  N   . VAL H  1 130 ? 101.392 101.912 -2.198  1.00 42.39 ? 103 VAL G N   1 
ATOM   8657  C  CA  . VAL H  1 130 ? 99.946  101.955 -1.992  1.00 34.49 ? 103 VAL G CA  1 
ATOM   8658  C  C   . VAL H  1 130 ? 99.281  100.643 -2.417  1.00 42.95 ? 103 VAL G C   1 
ATOM   8659  O  O   . VAL H  1 130 ? 98.369  100.153 -1.741  1.00 39.53 ? 103 VAL G O   1 
ATOM   8660  C  CB  . VAL H  1 130 ? 99.369  103.166 -2.751  1.00 39.50 ? 103 VAL G CB  1 
ATOM   8661  C  CG1 . VAL H  1 130 ? 97.854  103.170 -2.691  1.00 39.77 ? 103 VAL G CG1 1 
ATOM   8662  C  CG2 . VAL H  1 130 ? 99.948  104.477 -2.180  1.00 42.12 ? 103 VAL G CG2 1 
ATOM   8663  N  N   . ILE H  1 131 ? 99.716  100.057 -3.538  1.00 36.49 ? 104 ILE G N   1 
ATOM   8664  C  CA  . ILE H  1 131 ? 99.299  98.700  -3.880  1.00 35.63 ? 104 ILE G CA  1 
ATOM   8665  C  C   . ILE H  1 131 ? 99.985  97.695  -2.958  1.00 46.66 ? 104 ILE G C   1 
ATOM   8666  O  O   . ILE H  1 131 ? 101.088 97.931  -2.444  1.00 45.85 ? 104 ILE G O   1 
ATOM   8667  C  CB  . ILE H  1 131 ? 99.606  98.385  -5.355  1.00 32.44 ? 104 ILE G CB  1 
ATOM   8668  C  CG1 . ILE H  1 131 ? 101.121 98.411  -5.611  1.00 33.32 ? 104 ILE G CG1 1 
ATOM   8669  C  CG2 . ILE H  1 131 ? 98.847  99.325  -6.276  1.00 35.70 ? 104 ILE G CG2 1 
ATOM   8670  C  CD1 . ILE H  1 131 ? 101.551 97.774  -6.926  1.00 29.97 ? 104 ILE G CD1 1 
ATOM   8671  N  N   . SER H  1 132 ? 99.327  96.552  -2.758  1.00 41.56 ? 105 SER G N   1 
ATOM   8672  C  CA  . SER H  1 132 ? 99.835  95.481  -1.911  1.00 42.64 ? 105 SER G CA  1 
ATOM   8673  C  C   . SER H  1 132 ? 99.476  94.143  -2.543  1.00 46.53 ? 105 SER G C   1 
ATOM   8674  O  O   . SER H  1 132 ? 98.575  94.052  -3.384  1.00 41.55 ? 105 SER G O   1 
ATOM   8675  C  CB  . SER H  1 132 ? 99.260  95.569  -0.488  1.00 39.21 ? 105 SER G CB  1 
ATOM   8676  O  OG  . SER H  1 132 ? 99.863  94.623  0.382   1.00 45.13 ? 105 SER G OG  1 
ATOM   8677  N  N   . LEU H  1 133 ? 100.199 93.097  -2.139  1.00 43.03 ? 106 LEU G N   1 
ATOM   8678  C  CA  . LEU H  1 133 ? 99.849  91.739  -2.530  1.00 40.40 ? 106 LEU G CA  1 
ATOM   8679  C  C   . LEU H  1 133 ? 99.084  91.010  -1.431  1.00 39.15 ? 106 LEU G C   1 
ATOM   8680  O  O   . LEU H  1 133 ? 98.984  89.781  -1.465  1.00 48.40 ? 106 LEU G O   1 
ATOM   8681  C  CB  . LEU H  1 133 ? 101.098 90.957  -2.943  1.00 38.83 ? 106 LEU G CB  1 
ATOM   8682  C  CG  . LEU H  1 133 ? 101.854 91.527  -4.153  1.00 38.30 ? 106 LEU G CG  1 
ATOM   8683  C  CD1 . LEU H  1 133 ? 102.998 90.610  -4.553  1.00 35.55 ? 106 LEU G CD1 1 
ATOM   8684  C  CD2 . LEU H  1 133 ? 100.943 91.796  -5.370  1.00 39.15 ? 106 LEU G CD2 1 
ATOM   8685  N  N   . SER H  1 134 ? 98.534  91.753  -0.472  1.00 42.42 ? 107 SER G N   1 
ATOM   8686  C  CA  . SER H  1 134 ? 97.686  91.228  0.593   1.00 46.37 ? 107 SER G CA  1 
ATOM   8687  C  C   . SER H  1 134 ? 96.950  92.399  1.230   1.00 45.67 ? 107 SER G C   1 
ATOM   8688  O  O   . SER H  1 134 ? 97.251  93.565  0.961   1.00 49.93 ? 107 SER G O   1 
ATOM   8689  C  CB  . SER H  1 134 ? 98.499  90.467  1.645   1.00 47.34 ? 107 SER G CB  1 
ATOM   8690  O  OG  . SER H  1 134 ? 98.943  91.349  2.669   1.00 59.11 ? 107 SER G OG  1 
ATOM   8691  N  N   . GLY H  1 135 ? 95.971  92.079  2.071   1.00 40.71 ? 108 GLY G N   1 
ATOM   8692  C  CA  . GLY H  1 135 ? 95.282  93.117  2.820   1.00 40.89 ? 108 GLY G CA  1 
ATOM   8693  C  C   . GLY H  1 135 ? 94.226  93.877  2.029   1.00 49.66 ? 108 GLY G C   1 
ATOM   8694  O  O   . GLY H  1 135 ? 93.719  93.433  0.988   1.00 52.07 ? 108 GLY G O   1 
ATOM   8695  N  N   . ASP H  1 136 ? 93.903  95.069  2.547   1.00 52.00 ? 109 ASP G N   1 
ATOM   8696  C  CA  . ASP H  1 136 ? 92.781  95.850  2.027   1.00 52.82 ? 109 ASP G CA  1 
ATOM   8697  C  C   . ASP H  1 136 ? 93.065  96.410  0.639   1.00 49.71 ? 109 ASP G C   1 
ATOM   8698  O  O   . ASP H  1 136 ? 92.126  96.697  -0.114  1.00 50.63 ? 109 ASP G O   1 
ATOM   8699  C  CB  . ASP H  1 136 ? 92.459  97.003  2.977   1.00 49.89 ? 109 ASP G CB  1 
ATOM   8700  C  CG  . ASP H  1 136 ? 92.031  96.529  4.353   1.00 60.46 ? 109 ASP G CG  1 
ATOM   8701  O  OD1 . ASP H  1 136 ? 91.281  95.531  4.446   1.00 60.32 ? 109 ASP G OD1 1 
ATOM   8702  O  OD2 . ASP H  1 136 ? 92.455  97.157  5.347   1.00 68.19 ? 109 ASP G OD2 1 
ATOM   8703  N  N   . HIS H  1 137 ? 94.342  96.606  0.303   1.00 44.71 ? 110 HIS G N   1 
ATOM   8704  C  CA  . HIS H  1 137 ? 94.755  97.098  -1.005  1.00 42.75 ? 110 HIS G CA  1 
ATOM   8705  C  C   . HIS H  1 137 ? 95.310  95.988  -1.888  1.00 39.12 ? 110 HIS G C   1 
ATOM   8706  O  O   . HIS H  1 137 ? 96.078  96.270  -2.814  1.00 38.99 ? 110 HIS G O   1 
ATOM   8707  C  CB  . HIS H  1 137 ? 95.802  98.210  -0.862  1.00 38.95 ? 110 HIS G CB  1 
ATOM   8708  C  CG  . HIS H  1 137 ? 95.303  99.438  -0.161  1.00 42.28 ? 110 HIS G CG  1 
ATOM   8709  N  ND1 . HIS H  1 137 ? 96.083  100.564 0.011   1.00 43.86 ? 110 HIS G ND1 1 
ATOM   8710  C  CD2 . HIS H  1 137 ? 94.114  99.711  0.429   1.00 44.26 ? 110 HIS G CD2 1 
ATOM   8711  C  CE1 . HIS H  1 137 ? 95.392  101.481 0.667   1.00 46.46 ? 110 HIS G CE1 1 
ATOM   8712  N  NE2 . HIS H  1 137 ? 94.193  100.988 0.932   1.00 49.46 ? 110 HIS G NE2 1 
ATOM   8713  N  N   . CYS H  1 138 ? 94.951  94.733  -1.618  1.00 38.73 ? 111 CYS G N   1 
ATOM   8714  C  CA  . CYS H  1 138 ? 95.475  93.629  -2.413  1.00 40.29 ? 111 CYS G CA  1 
ATOM   8715  C  C   . CYS H  1 138 ? 94.997  93.735  -3.856  1.00 29.87 ? 111 CYS G C   1 
ATOM   8716  O  O   . CYS H  1 138 ? 93.818  94.005  -4.109  1.00 37.52 ? 111 CYS G O   1 
ATOM   8717  C  CB  . CYS H  1 138 ? 95.039  92.294  -1.813  1.00 41.09 ? 111 CYS G CB  1 
ATOM   8718  S  SG  . CYS H  1 138 ? 95.678  90.878  -2.709  1.00 44.90 ? 111 CYS G SG  1 
ATOM   8719  N  N   . ILE H  1 139 ? 95.910  93.517  -4.805  1.00 30.88 ? 112 ILE G N   1 
ATOM   8720  C  CA  . ILE H  1 139 ? 95.572  93.569  -6.228  1.00 34.11 ? 112 ILE G CA  1 
ATOM   8721  C  C   . ILE H  1 139 ? 95.579  92.194  -6.879  1.00 34.14 ? 112 ILE G C   1 
ATOM   8722  O  O   . ILE H  1 139 ? 95.358  92.102  -8.098  1.00 30.76 ? 112 ILE G O   1 
ATOM   8723  C  CB  . ILE H  1 139 ? 96.496  94.529  -7.008  1.00 29.32 ? 112 ILE G CB  1 
ATOM   8724  C  CG1 . ILE H  1 139 ? 97.954  94.071  -6.925  1.00 34.09 ? 112 ILE G CG1 1 
ATOM   8725  C  CG2 . ILE H  1 139 ? 96.343  95.955  -6.490  1.00 36.04 ? 112 ILE G CG2 1 
ATOM   8726  C  CD1 . ILE H  1 139 ? 98.896  94.816  -7.861  1.00 32.55 ? 112 ILE G CD1 1 
ATOM   8727  N  N   . ILE H  1 140 ? 95.831  91.122  -6.118  1.00 38.87 ? 113 ILE G N   1 
ATOM   8728  C  CA  . ILE H  1 140 ? 95.695  89.778  -6.674  1.00 39.81 ? 113 ILE G CA  1 
ATOM   8729  C  C   . ILE H  1 140 ? 94.250  89.546  -7.073  1.00 35.80 ? 113 ILE G C   1 
ATOM   8730  O  O   . ILE H  1 140 ? 93.322  89.842  -6.310  1.00 33.97 ? 113 ILE G O   1 
ATOM   8731  C  CB  . ILE H  1 140 ? 96.154  88.708  -5.673  1.00 40.28 ? 113 ILE G CB  1 
ATOM   8732  C  CG1 . ILE H  1 140 ? 97.477  89.103  -5.021  1.00 42.00 ? 113 ILE G CG1 1 
ATOM   8733  C  CG2 . ILE H  1 140 ? 96.269  87.358  -6.375  1.00 36.87 ? 113 ILE G CG2 1 
ATOM   8734  C  CD1 . ILE H  1 140 ? 98.635  88.932  -5.951  1.00 42.15 ? 113 ILE G CD1 1 
ATOM   8735  N  N   . GLY H  1 141 ? 94.052  89.005  -8.270  1.00 34.59 ? 114 GLY G N   1 
ATOM   8736  C  CA  . GLY H  1 141 ? 92.712  88.782  -8.760  1.00 34.79 ? 114 GLY G CA  1 
ATOM   8737  C  C   . GLY H  1 141 ? 92.073  89.982  -9.417  1.00 41.83 ? 114 GLY G C   1 
ATOM   8738  O  O   . GLY H  1 141 ? 90.899  89.907  -9.800  1.00 32.29 ? 114 GLY G O   1 
ATOM   8739  N  N   . ARG H  1 142 ? 92.797  91.088  -9.549  1.00 37.84 ? 115 ARG G N   1 
ATOM   8740  C  CA  . ARG H  1 142 ? 92.324  92.269  -10.251 1.00 33.39 ? 115 ARG G CA  1 
ATOM   8741  C  C   . ARG H  1 142 ? 93.046  92.348  -11.593 1.00 32.50 ? 115 ARG G C   1 
ATOM   8742  O  O   . ARG H  1 142 ? 93.801  91.447  -11.961 1.00 30.89 ? 115 ARG G O   1 
ATOM   8743  C  CB  . ARG H  1 142 ? 92.516  93.503  -9.365  1.00 29.89 ? 115 ARG G CB  1 
ATOM   8744  C  CG  . ARG H  1 142 ? 91.929  93.288  -7.960  1.00 32.83 ? 115 ARG G CG  1 
ATOM   8745  C  CD  . ARG H  1 142 ? 91.636  94.589  -7.201  1.00 30.45 ? 115 ARG G CD  1 
ATOM   8746  N  NE  . ARG H  1 142 ? 91.234  94.345  -5.818  1.00 34.62 ? 115 ARG G NE  1 
ATOM   8747  C  CZ  . ARG H  1 142 ? 89.976  94.326  -5.395  1.00 31.88 ? 115 ARG G CZ  1 
ATOM   8748  N  NH1 . ARG H  1 142 ? 88.965  94.508  -6.226  1.00 37.69 ? 115 ARG G NH1 1 
ATOM   8749  N  NH2 . ARG H  1 142 ? 89.728  94.132  -4.102  1.00 38.45 ? 115 ARG G NH2 1 
ATOM   8750  N  N   . THR H  1 143 ? 92.798  93.421  -12.346 1.00 31.23 ? 116 THR G N   1 
ATOM   8751  C  CA  . THR H  1 143 ? 93.245  93.515  -13.729 1.00 32.68 ? 116 THR G CA  1 
ATOM   8752  C  C   . THR H  1 143 ? 94.233  94.660  -13.906 1.00 31.96 ? 116 THR G C   1 
ATOM   8753  O  O   . THR H  1 143 ? 93.956  95.791  -13.500 1.00 32.62 ? 116 THR G O   1 
ATOM   8754  C  CB  . THR H  1 143 ? 92.054  93.713  -14.669 1.00 34.83 ? 116 THR G CB  1 
ATOM   8755  O  OG1 . THR H  1 143 ? 91.197  92.568  -14.601 1.00 34.16 ? 116 THR G OG1 1 
ATOM   8756  C  CG2 . THR H  1 143 ? 92.529  93.905  -16.096 1.00 28.39 ? 116 THR G CG2 1 
ATOM   8757  N  N   . LEU H  1 144 ? 95.369  94.370  -14.527 1.00 30.98 ? 117 LEU G N   1 
ATOM   8758  C  CA  . LEU H  1 144 ? 96.299  95.410  -14.938 1.00 32.41 ? 117 LEU G CA  1 
ATOM   8759  C  C   . LEU H  1 144 ? 96.004  95.783  -16.384 1.00 28.51 ? 117 LEU G C   1 
ATOM   8760  O  O   . LEU H  1 144 ? 95.826  94.908  -17.227 1.00 30.54 ? 117 LEU G O   1 
ATOM   8761  C  CB  . LEU H  1 144 ? 97.744  94.926  -14.795 1.00 29.75 ? 117 LEU G CB  1 
ATOM   8762  C  CG  . LEU H  1 144 ? 98.869  95.888  -15.164 1.00 32.04 ? 117 LEU G CG  1 
ATOM   8763  C  CD1 . LEU H  1 144 ? 98.921  97.003  -14.124 1.00 30.92 ? 117 LEU G CD1 1 
ATOM   8764  C  CD2 . LEU H  1 144 ? 100.188 95.133  -15.213 1.00 29.04 ? 117 LEU G CD2 1 
ATOM   8765  N  N   . VAL H  1 145 ? 95.938  97.087  -16.664 1.00 22.73 ? 118 VAL G N   1 
ATOM   8766  C  CA  . VAL H  1 145 ? 95.565  97.599  -17.978 1.00 23.99 ? 118 VAL G CA  1 
ATOM   8767  C  C   . VAL H  1 145 ? 96.617  98.600  -18.427 1.00 29.42 ? 118 VAL G C   1 
ATOM   8768  O  O   . VAL H  1 145 ? 97.021  99.469  -17.647 1.00 29.45 ? 118 VAL G O   1 
ATOM   8769  C  CB  . VAL H  1 145 ? 94.177  98.283  -17.947 1.00 26.40 ? 118 VAL G CB  1 
ATOM   8770  C  CG1 . VAL H  1 145 ? 93.830  98.869  -19.314 1.00 29.69 ? 118 VAL G CG1 1 
ATOM   8771  C  CG2 . VAL H  1 145 ? 93.108  97.304  -17.481 1.00 28.87 ? 118 VAL G CG2 1 
ATOM   8772  N  N   . VAL H  1 146 ? 97.054  98.491  -19.677 1.00 26.65 ? 119 VAL G N   1 
ATOM   8773  C  CA  . VAL H  1 146 ? 97.883  99.515  -20.307 1.00 32.91 ? 119 VAL G CA  1 
ATOM   8774  C  C   . VAL H  1 146 ? 97.013  100.273 -21.301 1.00 32.76 ? 119 VAL G C   1 
ATOM   8775  O  O   . VAL H  1 146 ? 96.286  99.664  -22.096 1.00 31.12 ? 119 VAL G O   1 
ATOM   8776  C  CB  . VAL H  1 146 ? 99.135  98.922  -20.979 1.00 32.50 ? 119 VAL G CB  1 
ATOM   8777  C  CG1 . VAL H  1 146 ? 98.768  97.807  -21.937 1.00 35.31 ? 119 VAL G CG1 1 
ATOM   8778  C  CG2 . VAL H  1 146 ? 99.914  100.018 -21.711 1.00 33.43 ? 119 VAL G CG2 1 
ATOM   8779  N  N   . HIS H  1 147 ? 97.063  101.597 -21.239 1.00 30.40 ? 120 HIS G N   1 
ATOM   8780  C  CA  . HIS H  1 147 ? 96.095  102.425 -21.943 1.00 31.37 ? 120 HIS G CA  1 
ATOM   8781  C  C   . HIS H  1 147 ? 96.674  103.043 -23.211 1.00 33.62 ? 120 HIS G C   1 
ATOM   8782  O  O   . HIS H  1 147 ? 97.881  103.030 -23.467 1.00 34.18 ? 120 HIS G O   1 
ATOM   8783  C  CB  . HIS H  1 147 ? 95.559  103.524 -21.026 1.00 29.06 ? 120 HIS G CB  1 
ATOM   8784  C  CG  . HIS H  1 147 ? 94.582  103.021 -20.017 1.00 27.71 ? 120 HIS G CG  1 
ATOM   8785  N  ND1 . HIS H  1 147 ? 93.220  103.180 -20.161 1.00 28.42 ? 120 HIS G ND1 1 
ATOM   8786  C  CD2 . HIS H  1 147 ? 94.766  102.340 -18.861 1.00 27.77 ? 120 HIS G CD2 1 
ATOM   8787  C  CE1 . HIS H  1 147 ? 92.607  102.624 -19.129 1.00 26.57 ? 120 HIS G CE1 1 
ATOM   8788  N  NE2 . HIS H  1 147 ? 93.523  102.113 -18.323 1.00 33.30 ? 120 HIS G NE2 1 
ATOM   8789  N  N   . GLU H  1 148 ? 95.765  103.636 -23.986 1.00 29.78 ? 121 GLU G N   1 
ATOM   8790  C  CA  . GLU H  1 148 ? 96.087  104.115 -25.326 1.00 34.03 ? 121 GLU G CA  1 
ATOM   8791  C  C   . GLU H  1 148 ? 96.940  105.379 -25.278 1.00 34.17 ? 121 GLU G C   1 
ATOM   8792  O  O   . GLU H  1 148 ? 97.939  105.489 -26.001 1.00 36.37 ? 121 GLU G O   1 
ATOM   8793  C  CB  . GLU H  1 148 ? 94.777  104.347 -26.084 1.00 32.06 ? 121 GLU G CB  1 
ATOM   8794  C  CG  . GLU H  1 148 ? 94.851  105.135 -27.367 1.00 37.65 ? 121 GLU G CG  1 
ATOM   8795  C  CD  . GLU H  1 148 ? 93.485  105.704 -27.762 1.00 42.19 ? 121 GLU G CD  1 
ATOM   8796  O  OE1 . GLU H  1 148 ? 93.249  105.887 -28.970 1.00 54.73 ? 121 GLU G OE1 1 
ATOM   8797  O  OE2 . GLU H  1 148 ? 92.648  105.968 -26.864 1.00 40.69 ? 121 GLU G OE2 1 
ATOM   8798  N  N   . LYS H  1 149 ? 96.574  106.330 -24.416 1.00 37.17 ? 122 LYS G N   1 
ATOM   8799  C  CA  . LYS H  1 149 ? 97.210  107.638 -24.302 1.00 35.53 ? 122 LYS G CA  1 
ATOM   8800  C  C   . LYS H  1 149 ? 97.909  107.776 -22.958 1.00 37.25 ? 122 LYS G C   1 
ATOM   8801  O  O   . LYS H  1 149 ? 97.789  106.926 -22.073 1.00 32.05 ? 122 LYS G O   1 
ATOM   8802  C  CB  . LYS H  1 149 ? 96.185  108.772 -24.459 1.00 37.07 ? 122 LYS G CB  1 
ATOM   8803  C  CG  . LYS H  1 149 ? 95.094  108.500 -25.474 1.00 42.34 ? 122 LYS G CG  1 
ATOM   8804  C  CD  . LYS H  1 149 ? 94.262  109.753 -25.761 1.00 45.04 ? 122 LYS G CD  1 
ATOM   8805  C  CE  . LYS H  1 149 ? 92.959  109.757 -24.947 1.00 52.06 ? 122 LYS G CE  1 
ATOM   8806  N  NZ  . LYS H  1 149 ? 92.287  111.103 -24.854 1.00 57.66 ? 122 LYS G NZ  1 
ATOM   8807  N  N   . ALA H  1 150 ? 98.636  108.880 -22.806 1.00 35.27 ? 123 ALA G N   1 
ATOM   8808  C  CA  . ALA H  1 150 ? 99.296  109.159 -21.540 1.00 32.74 ? 123 ALA G CA  1 
ATOM   8809  C  C   . ALA H  1 150 ? 98.272  109.493 -20.457 1.00 28.07 ? 123 ALA G C   1 
ATOM   8810  O  O   . ALA H  1 150 ? 97.212  110.062 -20.724 1.00 30.93 ? 123 ALA G O   1 
ATOM   8811  C  CB  . ALA H  1 150 ? 100.290 110.311 -21.708 1.00 33.02 ? 123 ALA G CB  1 
ATOM   8812  N  N   . ASP H  1 151 ? 98.590  109.091 -19.228 1.00 25.96 ? 124 ASP G N   1 
ATOM   8813  C  CA  . ASP H  1 151 ? 97.835  109.491 -18.044 1.00 28.28 ? 124 ASP G CA  1 
ATOM   8814  C  C   . ASP H  1 151 ? 98.265  110.899 -17.650 1.00 34.95 ? 124 ASP G C   1 
ATOM   8815  O  O   . ASP H  1 151 ? 99.460  111.155 -17.494 1.00 27.57 ? 124 ASP G O   1 
ATOM   8816  C  CB  . ASP H  1 151 ? 98.112  108.482 -16.931 1.00 29.15 ? 124 ASP G CB  1 
ATOM   8817  C  CG  . ASP H  1 151 ? 97.365  108.758 -15.627 1.00 29.53 ? 124 ASP G CG  1 
ATOM   8818  O  OD1 . ASP H  1 151 ? 96.852  109.873 -15.365 1.00 28.30 ? 124 ASP G OD1 1 
ATOM   8819  O  OD2 . ASP H  1 151 ? 97.333  107.814 -14.814 1.00 34.64 ? 124 ASP G OD2 1 
ATOM   8820  N  N   . ASP H  1 152 ? 97.309  111.825 -17.533 1.00 26.59 ? 125 ASP G N   1 
ATOM   8821  C  CA  . ASP H  1 152 ? 97.701  113.190 -17.184 1.00 28.02 ? 125 ASP G CA  1 
ATOM   8822  C  C   . ASP H  1 152 ? 97.840  113.393 -15.677 1.00 31.84 ? 125 ASP G C   1 
ATOM   8823  O  O   . ASP H  1 152 ? 98.017  114.532 -15.228 1.00 29.19 ? 125 ASP G O   1 
ATOM   8824  C  CB  . ASP H  1 152 ? 96.737  114.223 -17.807 1.00 26.99 ? 125 ASP G CB  1 
ATOM   8825  C  CG  . ASP H  1 152 ? 95.307  114.179 -17.240 1.00 30.72 ? 125 ASP G CG  1 
ATOM   8826  O  OD1 . ASP H  1 152 ? 95.079  113.741 -16.080 1.00 27.21 ? 125 ASP G OD1 1 
ATOM   8827  O  OD2 . ASP H  1 152 ? 94.399  114.652 -17.984 1.00 29.21 ? 125 ASP G OD2 1 
ATOM   8828  N  N   . LEU H  1 153 ? 97.781  112.302 -14.906 1.00 24.43 ? 126 LEU G N   1 
ATOM   8829  C  CA  . LEU H  1 153 ? 98.041  112.301 -13.464 1.00 31.05 ? 126 LEU G CA  1 
ATOM   8830  C  C   . LEU H  1 153 ? 97.079  113.198 -12.690 1.00 30.77 ? 126 LEU G C   1 
ATOM   8831  O  O   . LEU H  1 153 ? 97.402  113.665 -11.592 1.00 31.34 ? 126 LEU G O   1 
ATOM   8832  C  CB  . LEU H  1 153 ? 99.494  112.682 -13.164 1.00 29.39 ? 126 LEU G CB  1 
ATOM   8833  C  CG  . LEU H  1 153 ? 100.526 111.940 -14.007 1.00 34.96 ? 126 LEU G CG  1 
ATOM   8834  C  CD1 . LEU H  1 153 ? 101.937 112.229 -13.517 1.00 34.04 ? 126 LEU G CD1 1 
ATOM   8835  C  CD2 . LEU H  1 153 ? 100.250 110.430 -13.957 1.00 38.12 ? 126 LEU G CD2 1 
ATOM   8836  N  N   . GLY H  1 154 ? 95.877  113.416 -13.228 1.00 27.56 ? 127 GLY G N   1 
ATOM   8837  C  CA  . GLY H  1 154 ? 94.876  114.212 -12.535 1.00 28.23 ? 127 GLY G CA  1 
ATOM   8838  C  C   . GLY H  1 154 ? 95.003  115.704 -12.753 1.00 29.90 ? 127 GLY G C   1 
ATOM   8839  O  O   . GLY H  1 154 ? 94.293  116.482 -12.102 1.00 25.35 ? 127 GLY G O   1 
ATOM   8840  N  N   . LYS H  1 155 ? 95.866  116.125 -13.676 1.00 26.56 ? 128 LYS G N   1 
ATOM   8841  C  CA  . LYS H  1 155 ? 96.201  117.529 -13.865 1.00 30.20 ? 128 LYS G CA  1 
ATOM   8842  C  C   . LYS H  1 155 ? 95.645  118.078 -15.181 1.00 32.64 ? 128 LYS G C   1 
ATOM   8843  O  O   . LYS H  1 155 ? 96.096  119.127 -15.660 1.00 30.33 ? 128 LYS G O   1 
ATOM   8844  C  CB  . LYS H  1 155 ? 97.723  117.686 -13.803 1.00 27.79 ? 128 LYS G CB  1 
ATOM   8845  C  CG  . LYS H  1 155 ? 98.280  117.684 -12.382 1.00 34.60 ? 128 LYS G CG  1 
ATOM   8846  C  CD  . LYS H  1 155 ? 99.804  117.676 -12.421 1.00 47.10 ? 128 LYS G CD  1 
ATOM   8847  C  CE  . LYS H  1 155 ? 100.385 118.899 -11.727 1.00 55.42 ? 128 LYS G CE  1 
ATOM   8848  N  NZ  . LYS H  1 155 ? 100.490 118.741 -10.250 1.00 57.26 ? 128 LYS G NZ  1 
ATOM   8849  N  N   . GLY H  1 156 ? 94.680  117.381 -15.777 1.00 25.50 ? 129 GLY G N   1 
ATOM   8850  C  CA  . GLY H  1 156 ? 94.113  117.785 -17.053 1.00 22.37 ? 129 GLY G CA  1 
ATOM   8851  C  C   . GLY H  1 156 ? 93.051  118.865 -16.980 1.00 30.94 ? 129 GLY G C   1 
ATOM   8852  O  O   . GLY H  1 156 ? 92.722  119.458 -18.009 1.00 27.53 ? 129 GLY G O   1 
ATOM   8853  N  N   . GLY H  1 157 ? 92.499  119.126 -15.794 1.00 23.53 ? 130 GLY G N   1 
ATOM   8854  C  CA  . GLY H  1 157 ? 91.560  120.221 -15.632 1.00 26.17 ? 130 GLY G CA  1 
ATOM   8855  C  C   . GLY H  1 157 ? 90.161  119.988 -16.167 1.00 29.86 ? 130 GLY G C   1 
ATOM   8856  O  O   . GLY H  1 157 ? 89.341  120.914 -16.131 1.00 27.35 ? 130 GLY G O   1 
ATOM   8857  N  N   . ASN H  1 158 ? 89.861  118.801 -16.688 1.00 27.05 ? 131 ASN G N   1 
ATOM   8858  C  CA  . ASN H  1 158 ? 88.485  118.443 -16.992 1.00 29.53 ? 131 ASN G CA  1 
ATOM   8859  C  C   . ASN H  1 158 ? 88.003  117.383 -16.002 1.00 32.73 ? 131 ASN G C   1 
ATOM   8860  O  O   . ASN H  1 158 ? 88.766  116.891 -15.164 1.00 29.10 ? 131 ASN G O   1 
ATOM   8861  C  CB  . ASN H  1 158 ? 88.341  117.990 -18.453 1.00 28.36 ? 131 ASN G CB  1 
ATOM   8862  C  CG  . ASN H  1 158 ? 89.079  116.693 -18.770 1.00 29.29 ? 131 ASN G CG  1 
ATOM   8863  O  OD1 . ASN H  1 158 ? 89.834  116.159 -17.957 1.00 33.07 ? 131 ASN G OD1 1 
ATOM   8864  N  ND2 . ASN H  1 158 ? 88.872  116.197 -19.984 1.00 30.12 ? 131 ASN G ND2 1 
ATOM   8865  N  N   . GLU H  1 159 ? 86.706  117.067 -16.066 1.00 33.62 ? 132 GLU G N   1 
ATOM   8866  C  CA  . GLU H  1 159 ? 86.156  116.058 -15.157 1.00 34.76 ? 132 GLU G CA  1 
ATOM   8867  C  C   . GLU H  1 159 ? 86.814  114.697 -15.361 1.00 34.04 ? 132 GLU G C   1 
ATOM   8868  O  O   . GLU H  1 159 ? 87.096  113.980 -14.389 1.00 33.58 ? 132 GLU G O   1 
ATOM   8869  C  CB  . GLU H  1 159 ? 84.646  115.945 -15.350 1.00 37.37 ? 132 GLU G CB  1 
ATOM   8870  C  CG  . GLU H  1 159 ? 83.924  117.280 -15.346 1.00 49.02 ? 132 GLU G CG  1 
ATOM   8871  C  CD  . GLU H  1 159 ? 82.417  117.125 -15.384 1.00 52.02 ? 132 GLU G CD  1 
ATOM   8872  O  OE1 . GLU H  1 159 ? 81.741  117.637 -14.464 1.00 61.50 ? 132 GLU G OE1 1 
ATOM   8873  O  OE2 . GLU H  1 159 ? 81.910  116.535 -16.365 1.00 59.92 ? 132 GLU G OE2 1 
ATOM   8874  N  N   . GLU H  1 160 ? 87.060  114.326 -16.620 1.00 31.93 ? 133 GLU G N   1 
ATOM   8875  C  CA  . GLU H  1 160 ? 87.656  113.028 -16.930 1.00 38.70 ? 133 GLU G CA  1 
ATOM   8876  C  C   . GLU H  1 160 ? 89.033  112.856 -16.298 1.00 36.05 ? 133 GLU G C   1 
ATOM   8877  O  O   . GLU H  1 160 ? 89.407  111.740 -15.918 1.00 29.39 ? 133 GLU G O   1 
ATOM   8878  C  CB  . GLU H  1 160 ? 87.743  112.857 -18.449 1.00 35.11 ? 133 GLU G CB  1 
ATOM   8879  C  CG  . GLU H  1 160 ? 87.985  111.424 -18.912 1.00 40.43 ? 133 GLU G CG  1 
ATOM   8880  C  CD  . GLU H  1 160 ? 86.868  110.487 -18.497 1.00 46.60 ? 133 GLU G CD  1 
ATOM   8881  O  OE1 . GLU H  1 160 ? 85.729  110.672 -18.971 1.00 51.85 ? 133 GLU G OE1 1 
ATOM   8882  O  OE2 . GLU H  1 160 ? 87.125  109.570 -17.688 1.00 46.82 ? 133 GLU G OE2 1 
ATOM   8883  N  N   . SER H  1 161 ? 89.797  113.944 -16.165 1.00 30.67 ? 134 SER G N   1 
ATOM   8884  C  CA  . SER H  1 161 ? 91.150  113.824 -15.633 1.00 32.25 ? 134 SER G CA  1 
ATOM   8885  C  C   . SER H  1 161 ? 91.137  113.263 -14.218 1.00 29.92 ? 134 SER G C   1 
ATOM   8886  O  O   . SER H  1 161 ? 92.017  112.475 -13.852 1.00 30.70 ? 134 SER G O   1 
ATOM   8887  C  CB  . SER H  1 161 ? 91.850  115.184 -15.668 1.00 31.30 ? 134 SER G CB  1 
ATOM   8888  O  OG  . SER H  1 161 ? 93.064  115.155 -14.942 1.00 28.91 ? 134 SER G OG  1 
ATOM   8889  N  N   . THR H  1 162 ? 90.146  113.662 -13.410 1.00 33.67 ? 135 THR G N   1 
ATOM   8890  C  CA  . THR H  1 162 ? 90.024  113.199 -12.032 1.00 27.71 ? 135 THR G CA  1 
ATOM   8891  C  C   . THR H  1 162 ? 89.436  111.797 -11.923 1.00 30.24 ? 135 THR G C   1 
ATOM   8892  O  O   . THR H  1 162 ? 89.378  111.251 -10.811 1.00 31.53 ? 135 THR G O   1 
ATOM   8893  C  CB  . THR H  1 162 ? 89.156  114.160 -11.210 1.00 39.79 ? 135 THR G CB  1 
ATOM   8894  O  OG1 . THR H  1 162 ? 87.801  114.110 -11.692 1.00 48.33 ? 135 THR G OG1 1 
ATOM   8895  C  CG2 . THR H  1 162 ? 89.682  115.572 -11.302 1.00 38.27 ? 135 THR G CG2 1 
ATOM   8896  N  N   . LYS H  1 163 ? 89.002  111.208 -13.035 1.00 34.00 ? 136 LYS G N   1 
ATOM   8897  C  CA  . LYS H  1 163 ? 88.525  109.830 -13.064 1.00 35.46 ? 136 LYS G CA  1 
ATOM   8898  C  C   . LYS H  1 163 ? 89.537  108.873 -13.682 1.00 33.62 ? 136 LYS G C   1 
ATOM   8899  O  O   . LYS H  1 163 ? 89.899  107.863 -13.071 1.00 38.37 ? 136 LYS G O   1 
ATOM   8900  C  CB  . LYS H  1 163 ? 87.207  109.748 -13.843 1.00 36.04 ? 136 LYS G CB  1 
ATOM   8901  C  CG  . LYS H  1 163 ? 86.001  110.350 -13.132 1.00 40.35 ? 136 LYS G CG  1 
ATOM   8902  C  CD  . LYS H  1 163 ? 84.906  110.703 -14.130 1.00 44.52 ? 136 LYS G CD  1 
ATOM   8903  C  CE  . LYS H  1 163 ? 83.569  110.903 -13.424 1.00 47.71 ? 136 LYS G CE  1 
ATOM   8904  N  NZ  . LYS H  1 163 ? 83.328  112.334 -13.064 1.00 57.17 ? 136 LYS G NZ  1 
ATOM   8905  N  N   . THR H  1 164 ? 89.998  109.172 -14.894 1.00 33.12 ? 137 THR G N   1 
ATOM   8906  C  CA  . THR H  1 164 ? 90.850  108.268 -15.647 1.00 37.65 ? 137 THR G CA  1 
ATOM   8907  C  C   . THR H  1 164 ? 92.192  108.863 -16.052 1.00 33.14 ? 137 THR G C   1 
ATOM   8908  O  O   . THR H  1 164 ? 93.002  108.153 -16.657 1.00 30.01 ? 137 THR G O   1 
ATOM   8909  C  CB  . THR H  1 164 ? 90.127  107.805 -16.919 1.00 35.47 ? 137 THR G CB  1 
ATOM   8910  O  OG1 . THR H  1 164 ? 89.855  108.946 -17.750 1.00 38.03 ? 137 THR G OG1 1 
ATOM   8911  C  CG2 . THR H  1 164 ? 88.820  107.085 -16.562 1.00 37.11 ? 137 THR G CG2 1 
ATOM   8912  N  N   . GLY H  1 165 ? 92.443  110.140 -15.773 1.00 26.92 ? 138 GLY G N   1 
ATOM   8913  C  CA  . GLY H  1 165 ? 93.634  110.776 -16.307 1.00 29.01 ? 138 GLY G CA  1 
ATOM   8914  C  C   . GLY H  1 165 ? 93.622  110.973 -17.808 1.00 29.33 ? 138 GLY G C   1 
ATOM   8915  O  O   . GLY H  1 165 ? 94.672  111.247 -18.395 1.00 28.03 ? 138 GLY G O   1 
ATOM   8916  N  N   . ASN H  1 166 ? 92.455  110.837 -18.449 1.00 34.84 ? 139 ASN G N   1 
ATOM   8917  C  CA  . ASN H  1 166 ? 92.323  110.943 -19.909 1.00 29.82 ? 139 ASN G CA  1 
ATOM   8918  C  C   . ASN H  1 166 ? 93.261  109.978 -20.636 1.00 30.45 ? 139 ASN G C   1 
ATOM   8919  O  O   . ASN H  1 166 ? 93.724  110.257 -21.744 1.00 34.51 ? 139 ASN G O   1 
ATOM   8920  C  CB  . ASN H  1 166 ? 92.558  112.382 -20.386 1.00 28.87 ? 139 ASN G CB  1 
ATOM   8921  C  CG  . ASN H  1 166 ? 91.501  113.347 -19.871 1.00 34.95 ? 139 ASN G CG  1 
ATOM   8922  O  OD1 . ASN H  1 166 ? 90.374  113.381 -20.365 1.00 36.47 ? 139 ASN G OD1 1 
ATOM   8923  N  ND2 . ASN H  1 166 ? 91.859  114.127 -18.860 1.00 31.27 ? 139 ASN G ND2 1 
ATOM   8924  N  N   . ALA H  1 167 ? 93.555  108.825 -20.035 1.00 27.52 ? 140 ALA G N   1 
ATOM   8925  C  CA  . ALA H  1 167 ? 94.455  107.865 -20.679 1.00 28.67 ? 140 ALA G CA  1 
ATOM   8926  C  C   . ALA H  1 167 ? 93.802  107.084 -21.826 1.00 31.87 ? 140 ALA G C   1 
ATOM   8927  O  O   . ALA H  1 167 ? 94.489  106.305 -22.496 1.00 31.35 ? 140 ALA G O   1 
ATOM   8928  C  CB  . ALA H  1 167 ? 95.023  106.886 -19.642 1.00 31.17 ? 140 ALA G CB  1 
ATOM   8929  N  N   . GLY H  1 168 ? 92.507  107.253 -22.071 1.00 32.15 ? 141 GLY G N   1 
ATOM   8930  C  CA  . GLY H  1 168 ? 91.923  106.690 -23.276 1.00 33.80 ? 141 GLY G CA  1 
ATOM   8931  C  C   . GLY H  1 168 ? 91.625  105.202 -23.173 1.00 34.32 ? 141 GLY G C   1 
ATOM   8932  O  O   . GLY H  1 168 ? 91.451  104.639 -22.085 1.00 32.38 ? 141 GLY G O   1 
ATOM   8933  N  N   A SER H  1 169 ? 91.566  104.564 -24.342 0.45 34.05 ? 142 SER G N   1 
ATOM   8934  N  N   B SER H  1 169 ? 91.606  104.553 -24.338 0.55 33.73 ? 142 SER G N   1 
ATOM   8935  C  CA  A SER H  1 169 ? 91.088  103.193 -24.446 0.45 30.43 ? 142 SER G CA  1 
ATOM   8936  C  CA  B SER H  1 169 ? 91.116  103.187 -24.484 0.55 31.36 ? 142 SER G CA  1 
ATOM   8937  C  C   A SER H  1 169 ? 92.045  102.220 -23.756 0.45 33.42 ? 142 SER G C   1 
ATOM   8938  C  C   B SER H  1 169 ? 92.113  102.160 -23.944 0.55 33.50 ? 142 SER G C   1 
ATOM   8939  O  O   A SER H  1 169 ? 93.166  102.563 -23.363 0.45 32.48 ? 142 SER G O   1 
ATOM   8940  O  O   B SER H  1 169 ? 93.320  102.407 -23.838 0.55 32.59 ? 142 SER G O   1 
ATOM   8941  C  CB  A SER H  1 169 ? 90.912  102.797 -25.911 0.45 31.59 ? 142 SER G CB  1 
ATOM   8942  C  CB  B SER H  1 169 ? 90.811  102.882 -25.951 0.55 31.71 ? 142 SER G CB  1 
ATOM   8943  O  OG  A SER H  1 169 ? 89.927  103.593 -26.540 0.45 29.83 ? 142 SER G OG  1 
ATOM   8944  O  OG  B SER H  1 169 ? 91.965  103.053 -26.757 0.55 32.30 ? 142 SER G OG  1 
ATOM   8945  N  N   . ARG H  1 170 ? 91.581  100.982 -23.619 1.00 33.59 ? 143 ARG G N   1 
ATOM   8946  C  CA  . ARG H  1 170 ? 92.342  99.918  -22.988 1.00 31.93 ? 143 ARG G CA  1 
ATOM   8947  C  C   . ARG H  1 170 ? 92.958  99.037  -24.066 1.00 39.15 ? 143 ARG G C   1 
ATOM   8948  O  O   . ARG H  1 170 ? 92.244  98.339  -24.797 1.00 39.74 ? 143 ARG G O   1 
ATOM   8949  C  CB  . ARG H  1 170 ? 91.438  99.114  -22.058 1.00 35.79 ? 143 ARG G CB  1 
ATOM   8950  C  CG  . ARG H  1 170 ? 90.443  100.000 -21.334 1.00 32.86 ? 143 ARG G CG  1 
ATOM   8951  C  CD  . ARG H  1 170 ? 89.681  99.282  -20.242 1.00 30.74 ? 143 ARG G CD  1 
ATOM   8952  N  NE  . ARG H  1 170 ? 88.964  100.262 -19.433 1.00 30.50 ? 143 ARG G NE  1 
ATOM   8953  C  CZ  . ARG H  1 170 ? 88.264  99.974  -18.346 1.00 37.10 ? 143 ARG G CZ  1 
ATOM   8954  N  NH1 . ARG H  1 170 ? 88.150  98.730  -17.906 1.00 34.25 ? 143 ARG G NH1 1 
ATOM   8955  N  NH2 . ARG H  1 170 ? 87.675  100.963 -17.676 1.00 32.55 ? 143 ARG G NH2 1 
ATOM   8956  N  N   . LEU H  1 171 ? 94.282  99.056  -24.152 1.00 35.53 ? 144 LEU G N   1 
ATOM   8957  C  CA  . LEU H  1 171 ? 94.972  98.375  -25.238 1.00 30.17 ? 144 LEU G CA  1 
ATOM   8958  C  C   . LEU H  1 171 ? 95.193  96.902  -24.939 1.00 32.71 ? 144 LEU G C   1 
ATOM   8959  O  O   . LEU H  1 171 ? 95.090  96.071  -25.842 1.00 31.44 ? 144 LEU G O   1 
ATOM   8960  C  CB  . LEU H  1 171 ? 96.309  99.054  -25.497 1.00 33.82 ? 144 LEU G CB  1 
ATOM   8961  C  CG  . LEU H  1 171 ? 96.233  100.444 -26.131 1.00 35.14 ? 144 LEU G CG  1 
ATOM   8962  C  CD1 . LEU H  1 171 ? 97.633  100.881 -26.526 1.00 37.87 ? 144 LEU G CD1 1 
ATOM   8963  C  CD2 . LEU H  1 171 ? 95.287  100.481 -27.327 1.00 36.78 ? 144 LEU G CD2 1 
ATOM   8964  N  N   . ALA H  1 172 ? 95.491  96.567  -23.685 1.00 33.20 ? 145 ALA G N   1 
ATOM   8965  C  CA  . ALA H  1 172 ? 95.709  95.184  -23.284 1.00 33.00 ? 145 ALA G CA  1 
ATOM   8966  C  C   . ALA H  1 172 ? 95.600  95.105  -21.770 1.00 31.75 ? 145 ALA G C   1 
ATOM   8967  O  O   . ALA H  1 172 ? 95.761  96.108  -21.068 1.00 26.65 ? 145 ALA G O   1 
ATOM   8968  C  CB  . ALA H  1 172 ? 97.069  94.665  -23.765 1.00 34.15 ? 145 ALA G CB  1 
ATOM   8969  N  N   . CYS H  1 173 ? 95.332  93.896  -21.276 1.00 27.89 ? 146 CYS G N   1 
ATOM   8970  C  CA  . CYS H  1 173 ? 95.060  93.701  -19.862 1.00 28.07 ? 146 CYS G CA  1 
ATOM   8971  C  C   . CYS H  1 173 ? 95.239  92.230  -19.507 1.00 28.16 ? 146 CYS G C   1 
ATOM   8972  O  O   . CYS H  1 173 ? 95.375  91.372  -20.381 1.00 33.97 ? 146 CYS G O   1 
ATOM   8973  C  CB  . CYS H  1 173 ? 93.653  94.186  -19.500 1.00 34.94 ? 146 CYS G CB  1 
ATOM   8974  S  SG  . CYS H  1 173 ? 92.321  93.407  -20.458 1.00 42.16 ? 146 CYS G SG  1 
ATOM   8975  N  N   . GLY H  1 174 ? 95.264  91.960  -18.205 1.00 32.65 ? 147 GLY G N   1 
ATOM   8976  C  CA  . GLY H  1 174 ? 95.364  90.597  -17.723 1.00 31.16 ? 147 GLY G CA  1 
ATOM   8977  C  C   . GLY H  1 174 ? 95.044  90.556  -16.250 1.00 32.58 ? 147 GLY G C   1 
ATOM   8978  O  O   . GLY H  1 174 ? 95.171  91.561  -15.545 1.00 31.66 ? 147 GLY G O   1 
ATOM   8979  N  N   . VAL H  1 175 ? 94.608  89.381  -15.785 1.00 29.73 ? 148 VAL G N   1 
ATOM   8980  C  CA  . VAL H  1 175 ? 94.341  89.204  -14.363 1.00 32.97 ? 148 VAL G CA  1 
ATOM   8981  C  C   . VAL H  1 175 ? 95.663  89.012  -13.630 1.00 34.28 ? 148 VAL G C   1 
ATOM   8982  O  O   . VAL H  1 175 ? 96.589  88.365  -14.139 1.00 35.51 ? 148 VAL G O   1 
ATOM   8983  C  CB  . VAL H  1 175 ? 93.375  88.025  -14.123 1.00 30.96 ? 148 VAL G CB  1 
ATOM   8984  C  CG1 . VAL H  1 175 ? 93.055  87.895  -12.645 1.00 29.23 ? 148 VAL G CG1 1 
ATOM   8985  C  CG2 . VAL H  1 175 ? 92.084  88.245  -14.892 1.00 36.02 ? 148 VAL G CG2 1 
ATOM   8986  N  N   . ILE H  1 176 ? 95.755  89.586  -12.435 1.00 31.87 ? 149 ILE G N   1 
ATOM   8987  C  CA  . ILE H  1 176 ? 96.962  89.521  -11.620 1.00 35.14 ? 149 ILE G CA  1 
ATOM   8988  C  C   . ILE H  1 176 ? 96.885  88.261  -10.762 1.00 35.57 ? 149 ILE G C   1 
ATOM   8989  O  O   . ILE H  1 176 ? 96.018  88.145  -9.889  1.00 33.33 ? 149 ILE G O   1 
ATOM   8990  C  CB  . ILE H  1 176 ? 97.118  90.779  -10.758 1.00 33.39 ? 149 ILE G CB  1 
ATOM   8991  C  CG1 . ILE H  1 176 ? 97.192  92.031  -11.639 1.00 31.81 ? 149 ILE G CG1 1 
ATOM   8992  C  CG2 . ILE H  1 176 ? 98.353  90.664  -9.859  1.00 35.00 ? 149 ILE G CG2 1 
ATOM   8993  C  CD1 . ILE H  1 176 ? 97.065  93.343  -10.868 1.00 30.07 ? 149 ILE G CD1 1 
ATOM   8994  N  N   . GLY H  1 177 ? 97.795  87.322  -11.010 1.00 31.58 ? 150 GLY G N   1 
ATOM   8995  C  CA  . GLY H  1 177 ? 97.744  86.013  -10.390 1.00 35.25 ? 150 GLY G CA  1 
ATOM   8996  C  C   . GLY H  1 177 ? 98.931  85.746  -9.483  1.00 40.87 ? 150 GLY G C   1 
ATOM   8997  O  O   . GLY H  1 177 ? 100.010 86.317  -9.660  1.00 38.90 ? 150 GLY G O   1 
ATOM   8998  N  N   . ILE H  1 178 ? 98.714  84.865  -8.500  1.00 40.17 ? 151 ILE G N   1 
ATOM   8999  C  CA  . ILE H  1 178 ? 99.778  84.441  -7.599  1.00 36.89 ? 151 ILE G CA  1 
ATOM   9000  C  C   . ILE H  1 178 ? 100.861 83.738  -8.400  1.00 39.24 ? 151 ILE G C   1 
ATOM   9001  O  O   . ILE H  1 178 ? 100.578 82.906  -9.271  1.00 39.64 ? 151 ILE G O   1 
ATOM   9002  C  CB  . ILE H  1 178 ? 99.209  83.535  -6.496  1.00 42.10 ? 151 ILE G CB  1 
ATOM   9003  C  CG1 . ILE H  1 178 ? 97.960  84.176  -5.885  1.00 40.46 ? 151 ILE G CG1 1 
ATOM   9004  C  CG2 . ILE H  1 178 ? 100.260 83.256  -5.421  1.00 40.64 ? 151 ILE G CG2 1 
ATOM   9005  C  CD1 . ILE H  1 178 ? 97.567  83.620  -4.528  1.00 40.85 ? 151 ILE G CD1 1 
ATOM   9006  N  N   . ALA H  1 179 ? 102.114 84.102  -8.137  1.00 42.81 ? 152 ALA G N   1 
ATOM   9007  C  CA  . ALA H  1 179 ? 103.250 83.470  -8.785  1.00 39.40 ? 152 ALA G CA  1 
ATOM   9008  C  C   . ALA H  1 179 ? 104.124 82.813  -7.726  1.00 39.15 ? 152 ALA G C   1 
ATOM   9009  O  O   . ALA H  1 179 ? 104.007 83.093  -6.526  1.00 40.63 ? 152 ALA G O   1 
ATOM   9010  C  CB  . ALA H  1 179 ? 104.065 84.470  -9.620  1.00 40.35 ? 152 ALA G CB  1 
ATOM   9011  N  N   . GLN H  1 180 ? 104.992 81.918  -8.182  1.00 45.38 ? 153 GLN G N   1 
ATOM   9012  C  CA  . GLN H  1 180 ? 105.819 81.151  -7.262  1.00 52.95 ? 153 GLN G CA  1 
ATOM   9013  C  C   . GLN H  1 180 ? 106.953 82.008  -6.718  1.00 54.16 ? 153 GLN G C   1 
ATOM   9014  O  O   . GLN H  1 180 ? 107.686 82.605  -7.509  1.00 61.14 ? 153 GLN G O   1 
ATOM   9015  C  CB  . GLN H  1 180 ? 106.384 79.914  -7.950  1.00 47.86 ? 153 GLN G CB  1 
ATOM   9016  C  CG  . GLN H  1 180 ? 107.164 79.017  -7.004  1.00 49.48 ? 153 GLN G CG  1 
ATOM   9017  C  CD  . GLN H  1 180 ? 107.219 77.590  -7.491  1.00 54.36 ? 153 GLN G CD  1 
ATOM   9018  O  OE1 . GLN H  1 180 ? 107.485 77.334  -8.671  1.00 55.36 ? 153 GLN G OE1 1 
ATOM   9019  N  NE2 . GLN H  1 180 ? 106.966 76.645  -6.588  1.00 52.79 ? 153 GLN G NE2 1 
ATOM   9020  O  OXT . GLN H  1 180 ? 107.156 82.122  -5.501  1.00 54.33 ? 153 GLN G OXT 1 
ATOM   9021  N  N   . ALA I  1 28  ? 41.617  69.820  -68.124 1.00 47.51 ? 1   ALA I N   1 
ATOM   9022  C  CA  . ALA I  1 28  ? 41.957  71.218  -67.871 1.00 58.44 ? 1   ALA I CA  1 
ATOM   9023  C  C   . ALA I  1 28  ? 43.399  71.562  -68.254 1.00 50.33 ? 1   ALA I C   1 
ATOM   9024  O  O   . ALA I  1 28  ? 44.231  70.687  -68.488 1.00 48.93 ? 1   ALA I O   1 
ATOM   9025  C  CB  . ALA I  1 28  ? 41.718  71.567  -66.398 1.00 40.79 ? 1   ALA I CB  1 
ATOM   9026  N  N   . THR I  1 29  ? 43.677  72.861  -68.310 1.00 40.91 ? 2   THR I N   1 
ATOM   9027  C  CA  . THR I  1 29  ? 45.022  73.364  -68.523 1.00 42.90 ? 2   THR I CA  1 
ATOM   9028  C  C   . THR I  1 29  ? 45.683  73.812  -67.227 1.00 37.71 ? 2   THR I C   1 
ATOM   9029  O  O   . THR I  1 29  ? 46.894  74.054  -67.224 1.00 32.44 ? 2   THR I O   1 
ATOM   9030  C  CB  . THR I  1 29  ? 45.000  74.537  -69.521 1.00 40.70 ? 2   THR I CB  1 
ATOM   9031  O  OG1 . THR I  1 29  ? 44.390  75.682  -68.906 1.00 51.69 ? 2   THR I OG1 1 
ATOM   9032  C  CG2 . THR I  1 29  ? 44.197  74.159  -70.754 1.00 45.67 ? 2   THR I CG2 1 
ATOM   9033  N  N   . LYS I  1 30  ? 44.914  73.940  -66.139 1.00 31.46 ? 3   LYS I N   1 
ATOM   9034  C  CA  . LYS I  1 30  ? 45.441  74.331  -64.842 1.00 27.11 ? 3   LYS I CA  1 
ATOM   9035  C  C   . LYS I  1 30  ? 44.776  73.494  -63.753 1.00 28.99 ? 3   LYS I C   1 
ATOM   9036  O  O   . LYS I  1 30  ? 43.580  73.191  -63.827 1.00 28.48 ? 3   LYS I O   1 
ATOM   9037  C  CB  . LYS I  1 30  ? 45.215  75.823  -64.584 1.00 38.39 ? 3   LYS I CB  1 
ATOM   9038  C  CG  . LYS I  1 30  ? 46.402  76.693  -65.019 1.00 45.00 ? 3   LYS I CG  1 
ATOM   9039  C  CD  . LYS I  1 30  ? 46.040  78.174  -65.068 1.00 46.33 ? 3   LYS I CD  1 
ATOM   9040  C  CE  . LYS I  1 30  ? 47.136  79.034  -64.446 1.00 48.38 ? 3   LYS I CE  1 
ATOM   9041  N  NZ  . LYS I  1 30  ? 47.309  80.326  -65.192 1.00 50.58 ? 3   LYS I NZ  1 
ATOM   9042  N  N   . ALA I  1 31  ? 45.567  73.103  -62.756 1.00 27.01 ? 4   ALA I N   1 
ATOM   9043  C  CA  . ALA I  1 31  ? 45.054  72.362  -61.614 1.00 26.00 ? 4   ALA I CA  1 
ATOM   9044  C  C   . ALA I  1 31  ? 45.706  72.920  -60.355 1.00 26.93 ? 4   ALA I C   1 
ATOM   9045  O  O   . ALA I  1 31  ? 46.692  73.656  -60.425 1.00 22.24 ? 4   ALA I O   1 
ATOM   9046  C  CB  . ALA I  1 31  ? 45.311  70.859  -61.754 1.00 23.32 ? 4   ALA I CB  1 
ATOM   9047  N  N   . VAL I  1 32  ? 45.127  72.596  -59.197 1.00 24.20 ? 5   VAL I N   1 
ATOM   9048  C  CA  . VAL I  1 32  ? 45.634  73.126  -57.938 1.00 21.72 ? 5   VAL I CA  1 
ATOM   9049  C  C   . VAL I  1 32  ? 45.406  72.083  -56.857 1.00 21.45 ? 5   VAL I C   1 
ATOM   9050  O  O   . VAL I  1 32  ? 44.504  71.246  -56.950 1.00 24.10 ? 5   VAL I O   1 
ATOM   9051  C  CB  . VAL I  1 32  ? 44.978  74.483  -57.581 1.00 22.45 ? 5   VAL I CB  1 
ATOM   9052  C  CG1 . VAL I  1 32  ? 43.496  74.283  -57.209 1.00 25.45 ? 5   VAL I CG1 1 
ATOM   9053  C  CG2 . VAL I  1 32  ? 45.721  75.171  -56.455 1.00 30.38 ? 5   VAL I CG2 1 
ATOM   9054  N  N   . CYS I  1 33  ? 46.245  72.122  -55.833 1.00 24.00 ? 6   CYS I N   1 
ATOM   9055  C  CA  . CYS I  1 33  ? 46.152  71.152  -54.761 1.00 21.79 ? 6   CYS I CA  1 
ATOM   9056  C  C   . CYS I  1 33  ? 46.443  71.867  -53.455 1.00 20.67 ? 6   CYS I C   1 
ATOM   9057  O  O   . CYS I  1 33  ? 47.460  72.554  -53.343 1.00 22.15 ? 6   CYS I O   1 
ATOM   9058  C  CB  . CYS I  1 33  ? 47.151  70.011  -54.990 1.00 22.59 ? 6   CYS I CB  1 
ATOM   9059  S  SG  . CYS I  1 33  ? 47.143  68.761  -53.712 1.00 28.12 ? 6   CYS I SG  1 
ATOM   9060  N  N   . VAL I  1 34  ? 45.559  71.715  -52.475 1.00 19.65 ? 7   VAL I N   1 
ATOM   9061  C  CA  . VAL I  1 34  ? 45.804  72.242  -51.135 1.00 19.28 ? 7   VAL I CA  1 
ATOM   9062  C  C   . VAL I  1 34  ? 46.255  71.082  -50.264 1.00 23.59 ? 7   VAL I C   1 
ATOM   9063  O  O   . VAL I  1 34  ? 45.504  70.121  -50.068 1.00 22.26 ? 7   VAL I O   1 
ATOM   9064  C  CB  . VAL I  1 34  ? 44.560  72.934  -50.556 1.00 22.33 ? 7   VAL I CB  1 
ATOM   9065  C  CG1 . VAL I  1 34  ? 44.845  73.432  -49.130 1.00 24.90 ? 7   VAL I CG1 1 
ATOM   9066  C  CG2 . VAL I  1 34  ? 44.148  74.095  -51.440 1.00 23.86 ? 7   VAL I CG2 1 
ATOM   9067  N  N   . LEU I  1 35  ? 47.496  71.159  -49.780 1.00 22.23 ? 8   LEU I N   1 
ATOM   9068  C  CA  . LEU I  1 35  ? 48.100  70.114  -48.965 1.00 21.47 ? 8   LEU I CA  1 
ATOM   9069  C  C   . LEU I  1 35  ? 47.842  70.413  -47.492 1.00 22.07 ? 8   LEU I C   1 
ATOM   9070  O  O   . LEU I  1 35  ? 48.158  71.507  -47.020 1.00 22.02 ? 8   LEU I O   1 
ATOM   9071  C  CB  . LEU I  1 35  ? 49.607  70.040  -49.202 1.00 22.12 ? 8   LEU I CB  1 
ATOM   9072  C  CG  . LEU I  1 35  ? 50.044  69.748  -50.652 1.00 25.40 ? 8   LEU I CG  1 
ATOM   9073  C  CD1 . LEU I  1 35  ? 51.535  70.062  -50.830 1.00 26.30 ? 8   LEU I CD1 1 
ATOM   9074  C  CD2 . LEU I  1 35  ? 49.785  68.297  -50.977 1.00 27.41 ? 8   LEU I CD2 1 
ATOM   9075  N  N   . LYS I  1 36  ? 47.280  69.437  -46.787 1.00 22.83 ? 9   LYS I N   1 
ATOM   9076  C  CA  . LYS I  1 36  ? 46.991  69.501  -45.357 1.00 25.52 ? 9   LYS I CA  1 
ATOM   9077  C  C   . LYS I  1 36  ? 47.353  68.164  -44.735 1.00 26.50 ? 9   LYS I C   1 
ATOM   9078  O  O   . LYS I  1 36  ? 47.262  67.121  -45.389 1.00 21.65 ? 9   LYS I O   1 
ATOM   9079  C  CB  . LYS I  1 36  ? 45.500  69.793  -45.099 1.00 29.08 ? 9   LYS I CB  1 
ATOM   9080  C  CG  . LYS I  1 36  ? 45.022  71.208  -45.406 1.00 39.41 ? 9   LYS I CG  1 
ATOM   9081  C  CD  . LYS I  1 36  ? 46.083  72.261  -45.123 1.00 41.33 ? 9   LYS I CD  1 
ATOM   9082  C  CE  . LYS I  1 36  ? 45.637  73.634  -45.631 1.00 44.97 ? 9   LYS I CE  1 
ATOM   9083  N  NZ  . LYS I  1 36  ? 44.287  74.027  -45.125 1.00 44.97 ? 9   LYS I NZ  1 
ATOM   9084  N  N   . GLY I  1 37  ? 47.716  68.185  -43.450 1.00 23.57 ? 10  GLY I N   1 
ATOM   9085  C  CA  . GLY I  1 37  ? 48.035  66.938  -42.776 1.00 22.57 ? 10  GLY I CA  1 
ATOM   9086  C  C   . GLY I  1 37  ? 47.727  66.996  -41.294 1.00 33.31 ? 10  GLY I C   1 
ATOM   9087  O  O   . GLY I  1 37  ? 46.997  67.884  -40.856 1.00 29.87 ? 10  GLY I O   1 
ATOM   9088  N  N   . ASP I  1 38  ? 48.294  66.071  -40.518 1.00 37.64 ? 11  ASP I N   1 
ATOM   9089  C  CA  . ASP I  1 38  ? 48.072  66.022  -39.075 1.00 39.85 ? 11  ASP I CA  1 
ATOM   9090  C  C   . ASP I  1 38  ? 48.930  67.009  -38.308 1.00 37.03 ? 11  ASP I C   1 
ATOM   9091  O  O   . ASP I  1 38  ? 48.590  67.351  -37.168 1.00 54.50 ? 11  ASP I O   1 
ATOM   9092  C  CB  . ASP I  1 38  ? 48.362  64.620  -38.547 1.00 45.16 ? 11  ASP I CB  1 
ATOM   9093  C  CG  . ASP I  1 38  ? 47.286  63.635  -38.915 1.00 54.60 ? 11  ASP I CG  1 
ATOM   9094  O  OD1 . ASP I  1 38  ? 46.203  64.078  -39.358 1.00 55.87 ? 11  ASP I OD1 1 
ATOM   9095  O  OD2 . ASP I  1 38  ? 47.530  62.417  -38.774 1.00 70.81 ? 11  ASP I OD2 1 
ATOM   9096  N  N   . GLY I  1 39  ? 50.037  67.447  -38.884 1.00 32.98 ? 12  GLY I N   1 
ATOM   9097  C  CA  . GLY I  1 39  ? 50.942  68.341  -38.218 1.00 33.33 ? 12  GLY I CA  1 
ATOM   9098  C  C   . GLY I  1 39  ? 50.940  69.705  -38.855 1.00 28.91 ? 12  GLY I C   1 
ATOM   9099  O  O   . GLY I  1 39  ? 49.929  70.171  -39.378 1.00 32.78 ? 12  GLY I O   1 
ATOM   9100  N  N   . PRO I  1 40  ? 52.087  70.383  -38.812 1.00 32.34 ? 13  PRO I N   1 
ATOM   9101  C  CA  . PRO I  1 40  ? 52.144  71.767  -39.288 1.00 34.07 ? 13  PRO I CA  1 
ATOM   9102  C  C   . PRO I  1 40  ? 52.346  71.895  -40.792 1.00 33.80 ? 13  PRO I C   1 
ATOM   9103  O  O   . PRO I  1 40  ? 52.307  73.019  -41.311 1.00 30.04 ? 13  PRO I O   1 
ATOM   9104  C  CB  . PRO I  1 40  ? 53.345  72.328  -38.528 1.00 33.21 ? 13  PRO I CB  1 
ATOM   9105  C  CG  . PRO I  1 40  ? 54.272  71.151  -38.440 1.00 32.93 ? 13  PRO I CG  1 
ATOM   9106  C  CD  . PRO I  1 40  ? 53.391  69.923  -38.304 1.00 32.57 ? 13  PRO I CD  1 
ATOM   9107  N  N   . VAL I  1 41  ? 52.567  70.792  -41.506 1.00 29.79 ? 14  VAL I N   1 
ATOM   9108  C  CA  . VAL I  1 41  ? 52.891  70.890  -42.928 1.00 21.48 ? 14  VAL I CA  1 
ATOM   9109  C  C   . VAL I  1 41  ? 51.644  71.299  -43.699 1.00 23.17 ? 14  VAL I C   1 
ATOM   9110  O  O   . VAL I  1 41  ? 50.589  70.654  -43.603 1.00 24.90 ? 14  VAL I O   1 
ATOM   9111  C  CB  . VAL I  1 41  ? 53.454  69.558  -43.444 1.00 22.51 ? 14  VAL I CB  1 
ATOM   9112  C  CG1 . VAL I  1 41  ? 53.673  69.616  -44.962 1.00 24.24 ? 14  VAL I CG1 1 
ATOM   9113  C  CG2 . VAL I  1 41  ? 54.754  69.229  -42.721 1.00 29.49 ? 14  VAL I CG2 1 
ATOM   9114  N  N   . GLN I  1 42  ? 51.766  72.358  -44.496 1.00 26.57 ? 15  GLN I N   1 
ATOM   9115  C  CA  . GLN I  1 42  ? 50.652  72.775  -45.336 1.00 28.43 ? 15  GLN I CA  1 
ATOM   9116  C  C   . GLN I  1 42  ? 51.190  73.590  -46.499 1.00 24.69 ? 15  GLN I C   1 
ATOM   9117  O  O   . GLN I  1 42  ? 52.284  74.159  -46.427 1.00 26.37 ? 15  GLN I O   1 
ATOM   9118  C  CB  . GLN I  1 42  ? 49.616  73.567  -44.531 1.00 35.79 ? 15  GLN I CB  1 
ATOM   9119  C  CG  . GLN I  1 42  ? 50.021  74.999  -44.267 1.00 35.18 ? 15  GLN I CG  1 
ATOM   9120  C  CD  . GLN I  1 42  ? 48.968  75.761  -43.468 1.00 46.53 ? 15  GLN I CD  1 
ATOM   9121  O  OE1 . GLN I  1 42  ? 48.746  75.489  -42.294 1.00 48.71 ? 15  GLN I OE1 1 
ATOM   9122  N  NE2 . GLN I  1 42  ? 48.311  76.716  -44.116 1.00 55.11 ? 15  GLN I NE2 1 
ATOM   9123  N  N   . GLY I  1 43  ? 50.413  73.621  -47.581 1.00 25.89 ? 16  GLY I N   1 
ATOM   9124  C  CA  . GLY I  1 43  ? 50.875  74.327  -48.759 1.00 24.07 ? 16  GLY I CA  1 
ATOM   9125  C  C   . GLY I  1 43  ? 49.824  74.384  -49.842 1.00 21.54 ? 16  GLY I C   1 
ATOM   9126  O  O   . GLY I  1 43  ? 48.745  73.796  -49.734 1.00 22.07 ? 16  GLY I O   1 
ATOM   9127  N  N   . ILE I  1 44  ? 50.174  75.100  -50.909 1.00 23.76 ? 17  ILE I N   1 
ATOM   9128  C  CA  . ILE I  1 44  ? 49.364  75.188  -52.117 1.00 21.02 ? 17  ILE I CA  1 
ATOM   9129  C  C   . ILE I  1 44  ? 50.291  74.905  -53.289 1.00 19.56 ? 17  ILE I C   1 
ATOM   9130  O  O   . ILE I  1 44  ? 51.365  75.508  -53.392 1.00 23.10 ? 17  ILE I O   1 
ATOM   9131  C  CB  . ILE I  1 44  ? 48.698  76.574  -52.280 1.00 21.23 ? 17  ILE I CB  1 
ATOM   9132  C  CG1 . ILE I  1 44  ? 47.608  76.784  -51.216 1.00 26.93 ? 17  ILE I CG1 1 
ATOM   9133  C  CG2 . ILE I  1 44  ? 48.120  76.749  -53.686 1.00 23.86 ? 17  ILE I CG2 1 
ATOM   9134  C  CD1 . ILE I  1 44  ? 47.116  78.219  -51.142 1.00 30.60 ? 17  ILE I CD1 1 
ATOM   9135  N  N   . ILE I  1 45  ? 49.912  73.955  -54.132 1.00 21.92 ? 18  ILE I N   1 
ATOM   9136  C  CA  . ILE I  1 45  ? 50.718  73.585  -55.286 1.00 20.41 ? 18  ILE I CA  1 
ATOM   9137  C  C   . ILE I  1 45  ? 49.876  73.817  -56.531 1.00 24.33 ? 18  ILE I C   1 
ATOM   9138  O  O   . ILE I  1 45  ? 48.726  73.369  -56.603 1.00 22.58 ? 18  ILE I O   1 
ATOM   9139  C  CB  . ILE I  1 45  ? 51.198  72.125  -55.188 1.00 21.76 ? 18  ILE I CB  1 
ATOM   9140  C  CG1 . ILE I  1 45  ? 52.151  71.962  -53.998 1.00 17.23 ? 18  ILE I CG1 1 
ATOM   9141  C  CG2 . ILE I  1 45  ? 51.880  71.690  -56.476 1.00 25.77 ? 18  ILE I CG2 1 
ATOM   9142  C  CD1 . ILE I  1 45  ? 53.431  72.747  -54.117 1.00 22.06 ? 18  ILE I CD1 1 
ATOM   9143  N  N   . ASN I  1 46  ? 50.433  74.545  -57.487 1.00 21.42 ? 19  ASN I N   1 
ATOM   9144  C  CA  . ASN I  1 46  ? 49.765  74.836  -58.748 1.00 27.40 ? 19  ASN I CA  1 
ATOM   9145  C  C   . ASN I  1 46  ? 50.342  73.967  -59.853 1.00 27.35 ? 19  ASN I C   1 
ATOM   9146  O  O   . ASN I  1 46  ? 51.527  73.630  -59.833 1.00 25.12 ? 19  ASN I O   1 
ATOM   9147  C  CB  . ASN I  1 46  ? 49.932  76.312  -59.120 1.00 26.70 ? 19  ASN I CB  1 
ATOM   9148  C  CG  . ASN I  1 46  ? 49.491  77.231  -58.019 1.00 30.26 ? 19  ASN I CG  1 
ATOM   9149  O  OD1 . ASN I  1 46  ? 50.312  77.771  -57.262 1.00 33.14 ? 19  ASN I OD1 1 
ATOM   9150  N  ND2 . ASN I  1 46  ? 48.186  77.437  -57.923 1.00 28.83 ? 19  ASN I ND2 1 
ATOM   9151  N  N   . PHE I  1 47  ? 49.485  73.597  -60.816 1.00 27.80 ? 20  PHE I N   1 
ATOM   9152  C  CA  . PHE I  1 47  ? 49.882  72.830  -61.986 1.00 23.00 ? 20  PHE I CA  1 
ATOM   9153  C  C   . PHE I  1 47  ? 49.425  73.590  -63.221 1.00 31.48 ? 20  PHE I C   1 
ATOM   9154  O  O   . PHE I  1 47  ? 48.324  74.146  -63.244 1.00 25.22 ? 20  PHE I O   1 
ATOM   9155  C  CB  . PHE I  1 47  ? 49.263  71.421  -62.026 1.00 25.82 ? 20  PHE I CB  1 
ATOM   9156  C  CG  . PHE I  1 47  ? 49.630  70.534  -60.852 1.00 28.12 ? 20  PHE I CG  1 
ATOM   9157  C  CD1 . PHE I  1 47  ? 48.953  70.640  -59.640 1.00 28.14 ? 20  PHE I CD1 1 
ATOM   9158  C  CD2 . PHE I  1 47  ? 50.642  69.593  -60.965 1.00 26.95 ? 20  PHE I CD2 1 
ATOM   9159  C  CE1 . PHE I  1 47  ? 49.284  69.816  -58.566 1.00 25.90 ? 20  PHE I CE1 1 
ATOM   9160  C  CE2 . PHE I  1 47  ? 50.975  68.763  -59.892 1.00 28.92 ? 20  PHE I CE2 1 
ATOM   9161  C  CZ  . PHE I  1 47  ? 50.285  68.880  -58.695 1.00 22.47 ? 20  PHE I CZ  1 
ATOM   9162  N  N   . GLU I  1 48  ? 50.261  73.616  -64.249 1.00 27.72 ? 21  GLU I N   1 
ATOM   9163  C  CA  . GLU I  1 48  ? 49.881  74.299  -65.479 1.00 32.84 ? 21  GLU I CA  1 
ATOM   9164  C  C   . GLU I  1 48  ? 50.426  73.522  -66.664 1.00 33.69 ? 21  GLU I C   1 
ATOM   9165  O  O   . GLU I  1 48  ? 51.596  73.134  -66.662 1.00 33.05 ? 21  GLU I O   1 
ATOM   9166  C  CB  . GLU I  1 48  ? 50.413  75.732  -65.477 1.00 32.83 ? 21  GLU I CB  1 
ATOM   9167  C  CG  . GLU I  1 48  ? 50.191  76.531  -66.742 1.00 50.79 ? 21  GLU I CG  1 
ATOM   9168  C  CD  . GLU I  1 48  ? 50.926  77.865  -66.684 1.00 62.42 ? 21  GLU I CD  1 
ATOM   9169  O  OE1 . GLU I  1 48  ? 50.736  78.599  -65.684 1.00 59.14 ? 21  GLU I OE1 1 
ATOM   9170  O  OE2 . GLU I  1 48  ? 51.696  78.176  -67.626 1.00 70.63 ? 21  GLU I OE2 1 
ATOM   9171  N  N   . GLN I  1 49  ? 49.584  73.292  -67.670 1.00 39.58 ? 22  GLN I N   1 
ATOM   9172  C  CA  . GLN I  1 49  ? 49.978  72.546  -68.866 1.00 33.13 ? 22  GLN I CA  1 
ATOM   9173  C  C   . GLN I  1 49  ? 49.550  73.357  -70.089 1.00 45.00 ? 22  GLN I C   1 
ATOM   9174  O  O   . GLN I  1 49  ? 48.380  73.331  -70.479 1.00 38.75 ? 22  GLN I O   1 
ATOM   9175  C  CB  . GLN I  1 49  ? 49.355  71.157  -68.867 1.00 32.44 ? 22  GLN I CB  1 
ATOM   9176  C  CG  . GLN I  1 49  ? 50.015  70.172  -69.836 1.00 36.65 ? 22  GLN I CG  1 
ATOM   9177  C  CD  . GLN I  1 49  ? 49.353  68.801  -69.808 1.00 35.55 ? 22  GLN I CD  1 
ATOM   9178  O  OE1 . GLN I  1 49  ? 48.220  68.660  -69.343 1.00 38.69 ? 22  GLN I OE1 1 
ATOM   9179  N  NE2 . GLN I  1 49  ? 50.047  67.789  -70.313 1.00 36.60 ? 22  GLN I NE2 1 
ATOM   9180  N  N   . LYS I  1 50  ? 50.494  74.077  -70.701 1.00 42.75 ? 23  LYS I N   1 
ATOM   9181  C  CA  . LYS I  1 50  ? 50.112  75.022  -71.745 1.00 48.62 ? 23  LYS I CA  1 
ATOM   9182  C  C   . LYS I  1 50  ? 49.787  74.332  -73.068 1.00 39.96 ? 23  LYS I C   1 
ATOM   9183  O  O   . LYS I  1 50  ? 48.956  74.840  -73.827 1.00 50.09 ? 23  LYS I O   1 
ATOM   9184  C  CB  . LYS I  1 50  ? 51.199  76.088  -71.925 1.00 49.02 ? 23  LYS I CB  1 
ATOM   9185  C  CG  . LYS I  1 50  ? 51.235  77.069  -70.732 1.00 53.71 ? 23  LYS I CG  1 
ATOM   9186  C  CD  . LYS I  1 50  ? 52.112  78.310  -70.943 1.00 55.43 ? 23  LYS I CD  1 
ATOM   9187  C  CE  . LYS I  1 50  ? 51.335  79.623  -70.659 1.00 52.26 ? 23  LYS I CE  1 
ATOM   9188  N  NZ  . LYS I  1 50  ? 50.584  80.153  -71.841 1.00 50.40 ? 23  LYS I NZ  1 
ATOM   9189  N  N   . GLU I  1 51  ? 50.387  73.180  -73.360 1.00 42.81 ? 24  GLU I N   1 
ATOM   9190  C  CA  . GLU I  1 51  ? 50.000  72.399  -74.529 1.00 48.05 ? 24  GLU I CA  1 
ATOM   9191  C  C   . GLU I  1 51  ? 49.524  71.022  -74.092 1.00 44.99 ? 24  GLU I C   1 
ATOM   9192  O  O   . GLU I  1 51  ? 50.034  70.450  -73.125 1.00 46.27 ? 24  GLU I O   1 
ATOM   9193  C  CB  . GLU I  1 51  ? 51.140  72.261  -75.560 1.00 52.73 ? 24  GLU I CB  1 
ATOM   9194  C  CG  . GLU I  1 51  ? 52.125  73.428  -75.624 1.00 52.27 ? 24  GLU I CG  1 
ATOM   9195  C  CD  . GLU I  1 51  ? 53.329  73.122  -76.519 1.00 61.14 ? 24  GLU I CD  1 
ATOM   9196  O  OE1 . GLU I  1 51  ? 53.211  72.222  -77.382 1.00 65.78 ? 24  GLU I OE1 1 
ATOM   9197  O  OE2 . GLU I  1 51  ? 54.393  73.768  -76.355 1.00 64.52 ? 24  GLU I OE2 1 
ATOM   9198  N  N   . SER I  1 52  ? 48.555  70.486  -74.840 1.00 45.99 ? 25  SER I N   1 
ATOM   9199  C  CA  . SER I  1 52  ? 47.697  69.420  -74.330 1.00 43.24 ? 25  SER I CA  1 
ATOM   9200  C  C   . SER I  1 52  ? 48.440  68.125  -74.025 1.00 50.94 ? 25  SER I C   1 
ATOM   9201  O  O   . SER I  1 52  ? 47.902  67.280  -73.300 1.00 64.50 ? 25  SER I O   1 
ATOM   9202  C  CB  . SER I  1 52  ? 46.556  69.142  -75.308 1.00 52.77 ? 25  SER I CB  1 
ATOM   9203  O  OG  . SER I  1 52  ? 45.559  68.342  -74.684 1.00 62.54 ? 25  SER I OG  1 
ATOM   9204  N  N   . ASN I  1 53  ? 49.648  67.934  -74.538 1.00 47.37 ? 26  ASN I N   1 
ATOM   9205  C  CA  . ASN I  1 53  ? 50.468  66.834  -74.030 1.00 51.52 ? 26  ASN I CA  1 
ATOM   9206  C  C   . ASN I  1 53  ? 51.929  67.246  -73.983 1.00 53.82 ? 26  ASN I C   1 
ATOM   9207  O  O   . ASN I  1 53  ? 52.837  66.445  -74.237 1.00 58.58 ? 26  ASN I O   1 
ATOM   9208  C  CB  . ASN I  1 53  ? 50.255  65.547  -74.833 1.00 53.91 ? 26  ASN I CB  1 
ATOM   9209  C  CG  . ASN I  1 53  ? 50.634  65.683  -76.298 1.00 64.03 ? 26  ASN I CG  1 
ATOM   9210  O  OD1 . ASN I  1 53  ? 51.598  66.363  -76.660 1.00 67.58 ? 26  ASN I OD1 1 
ATOM   9211  N  ND2 . ASN I  1 53  ? 49.862  65.021  -77.160 1.00 68.73 ? 26  ASN I ND2 1 
ATOM   9212  N  N   . GLY I  1 54  ? 52.167  68.512  -73.653 1.00 46.84 ? 27  GLY I N   1 
ATOM   9213  C  CA  . GLY I  1 54  ? 53.488  68.974  -73.320 1.00 43.13 ? 27  GLY I CA  1 
ATOM   9214  C  C   . GLY I  1 54  ? 53.750  68.762  -71.844 1.00 43.96 ? 27  GLY I C   1 
ATOM   9215  O  O   . GLY I  1 54  ? 53.002  68.067  -71.148 1.00 45.77 ? 27  GLY I O   1 
ATOM   9216  N  N   . PRO I  1 55  ? 54.809  69.370  -71.333 1.00 39.73 ? 28  PRO I N   1 
ATOM   9217  C  CA  . PRO I  1 55  ? 55.133  69.222  -69.913 1.00 39.35 ? 28  PRO I CA  1 
ATOM   9218  C  C   . PRO I  1 55  ? 54.172  70.014  -69.032 1.00 34.78 ? 28  PRO I C   1 
ATOM   9219  O  O   . PRO I  1 55  ? 53.403  70.866  -69.489 1.00 31.20 ? 28  PRO I O   1 
ATOM   9220  C  CB  . PRO I  1 55  ? 56.557  69.768  -69.817 1.00 33.77 ? 28  PRO I CB  1 
ATOM   9221  C  CG  . PRO I  1 55  ? 56.665  70.743  -70.945 1.00 38.36 ? 28  PRO I CG  1 
ATOM   9222  C  CD  . PRO I  1 55  ? 55.693  70.329  -72.018 1.00 39.39 ? 28  PRO I CD  1 
ATOM   9223  N  N   . VAL I  1 56  ? 54.230  69.696  -67.740 1.00 35.31 ? 29  VAL I N   1 
ATOM   9224  C  CA  . VAL I  1 56  ? 53.439  70.347  -66.701 1.00 32.05 ? 29  VAL I CA  1 
ATOM   9225  C  C   . VAL I  1 56  ? 54.378  71.124  -65.791 1.00 27.46 ? 29  VAL I C   1 
ATOM   9226  O  O   . VAL I  1 56  ? 55.376  70.579  -65.304 1.00 27.50 ? 29  VAL I O   1 
ATOM   9227  C  CB  . VAL I  1 56  ? 52.633  69.321  -65.889 1.00 30.80 ? 29  VAL I CB  1 
ATOM   9228  C  CG1 . VAL I  1 56  ? 51.840  70.023  -64.812 1.00 25.34 ? 29  VAL I CG1 1 
ATOM   9229  C  CG2 . VAL I  1 56  ? 51.701  68.556  -66.800 1.00 29.46 ? 29  VAL I CG2 1 
ATOM   9230  N  N   . LYS I  1 57  ? 54.075  72.399  -65.578 1.00 24.83 ? 30  LYS I N   1 
ATOM   9231  C  CA  . LYS I  1 57  ? 54.811  73.195  -64.607 1.00 29.71 ? 30  LYS I CA  1 
ATOM   9232  C  C   . LYS I  1 57  ? 54.140  73.016  -63.244 1.00 27.33 ? 30  LYS I C   1 
ATOM   9233  O  O   . LYS I  1 57  ? 52.911  73.076  -63.138 1.00 30.76 ? 30  LYS I O   1 
ATOM   9234  C  CB  . LYS I  1 57  ? 54.854  74.670  -65.015 1.00 31.75 ? 30  LYS I CB  1 
ATOM   9235  C  CG  . LYS I  1 57  ? 55.793  75.526  -64.133 1.00 45.59 ? 30  LYS I CG  1 
ATOM   9236  C  CD  . LYS I  1 57  ? 55.476  77.036  -64.167 1.00 47.38 ? 30  LYS I CD  1 
ATOM   9237  C  CE  . LYS I  1 57  ? 56.461  77.832  -63.292 1.00 44.84 ? 30  LYS I CE  1 
ATOM   9238  N  NZ  . LYS I  1 57  ? 56.066  79.274  -63.181 1.00 51.90 ? 30  LYS I NZ  1 
ATOM   9239  N  N   . VAL I  1 58  ? 54.941  72.738  -62.225 1.00 29.79 ? 31  VAL I N   1 
ATOM   9240  C  CA  . VAL I  1 58  ? 54.459  72.514  -60.865 1.00 25.77 ? 31  VAL I CA  1 
ATOM   9241  C  C   . VAL I  1 58  ? 55.125  73.569  -59.992 1.00 27.76 ? 31  VAL I C   1 
ATOM   9242  O  O   . VAL I  1 58  ? 56.361  73.643  -59.943 1.00 28.53 ? 31  VAL I O   1 
ATOM   9243  C  CB  . VAL I  1 58  ? 54.789  71.092  -60.373 1.00 30.04 ? 31  VAL I CB  1 
ATOM   9244  C  CG1 . VAL I  1 58  ? 54.112  70.802  -59.019 1.00 27.98 ? 31  VAL I CG1 1 
ATOM   9245  C  CG2 . VAL I  1 58  ? 54.357  70.048  -61.397 1.00 22.31 ? 31  VAL I CG2 1 
ATOM   9246  N  N   . TRP I  1 59  ? 54.322  74.410  -59.333 1.00 26.99 ? 32  TRP I N   1 
ATOM   9247  C  CA  . TRP I  1 59  ? 54.929  75.436  -58.497 1.00 28.96 ? 32  TRP I CA  1 
ATOM   9248  C  C   . TRP I  1 59  ? 54.019  75.776  -57.324 1.00 24.10 ? 32  TRP I C   1 
ATOM   9249  O  O   . TRP I  1 59  ? 52.792  75.636  -57.399 1.00 24.92 ? 32  TRP I O   1 
ATOM   9250  C  CB  . TRP I  1 59  ? 55.258  76.698  -59.315 1.00 26.60 ? 32  TRP I CB  1 
ATOM   9251  C  CG  . TRP I  1 59  ? 54.069  77.571  -59.672 1.00 31.99 ? 32  TRP I CG  1 
ATOM   9252  C  CD1 . TRP I  1 59  ? 53.604  78.655  -58.984 1.00 33.17 ? 32  TRP I CD1 1 
ATOM   9253  C  CD2 . TRP I  1 59  ? 53.184  77.393  -60.778 1.00 32.33 ? 32  TRP I CD2 1 
ATOM   9254  N  NE1 . TRP I  1 59  ? 52.504  79.183  -59.622 1.00 33.76 ? 32  TRP I NE1 1 
ATOM   9255  C  CE2 . TRP I  1 59  ? 52.224  78.420  -60.720 1.00 31.91 ? 32  TRP I CE2 1 
ATOM   9256  C  CE3 . TRP I  1 59  ? 53.111  76.463  -61.812 1.00 40.62 ? 32  TRP I CE3 1 
ATOM   9257  C  CZ2 . TRP I  1 59  ? 51.206  78.548  -61.662 1.00 48.93 ? 32  TRP I CZ2 1 
ATOM   9258  C  CZ3 . TRP I  1 59  ? 52.103  76.598  -62.757 1.00 45.91 ? 32  TRP I CZ3 1 
ATOM   9259  C  CH2 . TRP I  1 59  ? 51.164  77.633  -62.674 1.00 48.38 ? 32  TRP I CH2 1 
ATOM   9260  N  N   . GLY I  1 60  ? 54.643  76.235  -56.250 1.00 27.76 ? 33  GLY I N   1 
ATOM   9261  C  CA  . GLY I  1 60  ? 53.919  76.653  -55.069 1.00 25.65 ? 33  GLY I CA  1 
ATOM   9262  C  C   . GLY I  1 60  ? 54.850  76.639  -53.877 1.00 23.35 ? 33  GLY I C   1 
ATOM   9263  O  O   . GLY I  1 60  ? 56.069  76.571  -54.022 1.00 27.86 ? 33  GLY I O   1 
ATOM   9264  N  N   A SER I  1 61  ? 54.250  76.720  -52.699 0.50 28.51 ? 34  SER I N   1 
ATOM   9265  N  N   B SER I  1 61  ? 54.245  76.703  -52.696 0.50 28.51 ? 34  SER I N   1 
ATOM   9266  C  CA  A SER I  1 61  ? 55.017  76.750  -51.465 0.50 25.71 ? 34  SER I CA  1 
ATOM   9267  C  CA  B SER I  1 61  ? 54.996  76.771  -51.453 0.50 25.79 ? 34  SER I CA  1 
ATOM   9268  C  C   A SER I  1 61  ? 54.402  75.788  -50.462 0.50 26.58 ? 34  SER I C   1 
ATOM   9269  C  C   B SER I  1 61  ? 54.397  75.793  -50.453 0.50 26.58 ? 34  SER I C   1 
ATOM   9270  O  O   A SER I  1 61  ? 53.181  75.633  -50.404 0.50 24.03 ? 34  SER I O   1 
ATOM   9271  O  O   B SER I  1 61  ? 53.178  75.635  -50.385 0.50 24.02 ? 34  SER I O   1 
ATOM   9272  C  CB  A SER I  1 61  ? 55.088  78.177  -50.883 0.50 30.93 ? 34  SER I CB  1 
ATOM   9273  C  CB  B SER I  1 61  ? 54.990  78.207  -50.881 0.50 31.55 ? 34  SER I CB  1 
ATOM   9274  O  OG  A SER I  1 61  ? 55.255  79.138  -51.914 0.50 33.28 ? 34  SER I OG  1 
ATOM   9275  O  OG  B SER I  1 61  ? 55.693  78.284  -49.655 0.50 31.56 ? 34  SER I OG  1 
ATOM   9276  N  N   . ILE I  1 62  ? 55.265  75.114  -49.708 1.00 23.28 ? 35  ILE I N   1 
ATOM   9277  C  CA  . ILE I  1 62  ? 54.877  74.244  -48.606 1.00 24.62 ? 35  ILE I CA  1 
ATOM   9278  C  C   . ILE I  1 62  ? 55.667  74.707  -47.393 1.00 26.51 ? 35  ILE I C   1 
ATOM   9279  O  O   . ILE I  1 62  ? 56.883  74.895  -47.485 1.00 23.75 ? 35  ILE I O   1 
ATOM   9280  C  CB  . ILE I  1 62  ? 55.173  72.755  -48.885 1.00 25.17 ? 35  ILE I CB  1 
ATOM   9281  C  CG1 . ILE I  1 62  ? 54.652  72.312  -50.256 1.00 27.95 ? 35  ILE I CG1 1 
ATOM   9282  C  CG2 . ILE I  1 62  ? 54.574  71.902  -47.789 1.00 23.19 ? 35  ILE I CG2 1 
ATOM   9283  C  CD1 . ILE I  1 62  ? 55.109  70.906  -50.666 1.00 22.65 ? 35  ILE I CD1 1 
ATOM   9284  N  N   . LYS I  1 63  ? 54.987  74.885  -46.266 1.00 25.40 ? 36  LYS I N   1 
ATOM   9285  C  CA  . LYS I  1 63  ? 55.651  75.291  -45.039 1.00 30.77 ? 36  LYS I CA  1 
ATOM   9286  C  C   . LYS I  1 63  ? 55.464  74.224  -43.970 1.00 25.65 ? 36  LYS I C   1 
ATOM   9287  O  O   . LYS I  1 63  ? 54.680  73.283  -44.123 1.00 25.42 ? 36  LYS I O   1 
ATOM   9288  C  CB  . LYS I  1 63  ? 55.135  76.654  -44.555 1.00 27.03 ? 36  LYS I CB  1 
ATOM   9289  C  CG  . LYS I  1 63  ? 53.657  76.693  -44.257 1.00 32.04 ? 36  LYS I CG  1 
ATOM   9290  C  CD  . LYS I  1 63  ? 53.214  78.100  -43.794 1.00 35.67 ? 36  LYS I CD  1 
ATOM   9291  C  CE  . LYS I  1 63  ? 51.952  78.043  -42.936 1.00 44.12 ? 36  LYS I CE  1 
ATOM   9292  N  NZ  . LYS I  1 63  ? 51.648  79.331  -42.235 1.00 48.29 ? 36  LYS I NZ  1 
ATOM   9293  N  N   . GLY I  1 64  ? 56.216  74.377  -42.879 1.00 25.73 ? 37  GLY I N   1 
ATOM   9294  C  CA  . GLY I  1 64  ? 56.135  73.445  -41.773 1.00 26.84 ? 37  GLY I CA  1 
ATOM   9295  C  C   . GLY I  1 64  ? 57.019  72.223  -41.885 1.00 26.73 ? 37  GLY I C   1 
ATOM   9296  O  O   . GLY I  1 64  ? 56.857  71.296  -41.085 1.00 24.89 ? 37  GLY I O   1 
ATOM   9297  N  N   . LEU I  1 65  ? 57.945  72.194  -42.849 1.00 25.07 ? 38  LEU I N   1 
ATOM   9298  C  CA  . LEU I  1 65  ? 58.792  71.035  -43.118 1.00 25.27 ? 38  LEU I CA  1 
ATOM   9299  C  C   . LEU I  1 65  ? 60.135  71.130  -42.395 1.00 25.56 ? 38  LEU I C   1 
ATOM   9300  O  O   . LEU I  1 65  ? 60.643  72.219  -42.131 1.00 27.19 ? 38  LEU I O   1 
ATOM   9301  C  CB  . LEU I  1 65  ? 59.056  70.906  -44.623 1.00 25.82 ? 38  LEU I CB  1 
ATOM   9302  C  CG  . LEU I  1 65  ? 57.847  70.657  -45.520 1.00 25.28 ? 38  LEU I CG  1 
ATOM   9303  C  CD1 . LEU I  1 65  ? 58.127  71.032  -47.013 1.00 24.74 ? 38  LEU I CD1 1 
ATOM   9304  C  CD2 . LEU I  1 65  ? 57.468  69.196  -45.377 1.00 22.06 ? 38  LEU I CD2 1 
ATOM   9305  N  N   . THR I  1 66  ? 60.736  69.976  -42.130 1.00 28.77 ? 39  THR I N   1 
ATOM   9306  C  CA  . THR I  1 66  ? 62.130  69.964  -41.706 1.00 26.72 ? 39  THR I CA  1 
ATOM   9307  C  C   . THR I  1 66  ? 63.046  70.336  -42.863 1.00 35.80 ? 39  THR I C   1 
ATOM   9308  O  O   . THR I  1 66  ? 62.812  69.963  -44.018 1.00 26.81 ? 39  THR I O   1 
ATOM   9309  C  CB  . THR I  1 66  ? 62.519  68.591  -41.164 1.00 29.62 ? 39  THR I CB  1 
ATOM   9310  O  OG1 . THR I  1 66  ? 62.313  67.604  -42.188 1.00 29.67 ? 39  THR I OG1 1 
ATOM   9311  C  CG2 . THR I  1 66  ? 61.698  68.245  -39.943 1.00 29.62 ? 39  THR I CG2 1 
ATOM   9312  N  N   . GLU I  1 67  ? 64.096  71.079  -42.541 1.00 26.39 ? 40  GLU I N   1 
ATOM   9313  C  CA  . GLU I  1 67  ? 65.057  71.509  -43.545 1.00 30.55 ? 40  GLU I CA  1 
ATOM   9314  C  C   . GLU I  1 67  ? 65.571  70.318  -44.343 1.00 31.84 ? 40  GLU I C   1 
ATOM   9315  O  O   . GLU I  1 67  ? 65.905  69.279  -43.773 1.00 28.07 ? 40  GLU I O   1 
ATOM   9316  C  CB  . GLU I  1 67  ? 66.219  72.218  -42.854 1.00 33.70 ? 40  GLU I CB  1 
ATOM   9317  C  CG  . GLU I  1 67  ? 67.328  72.613  -43.792 1.00 38.18 ? 40  GLU I CG  1 
ATOM   9318  C  CD  . GLU I  1 67  ? 68.395  73.426  -43.091 1.00 45.38 ? 40  GLU I CD  1 
ATOM   9319  O  OE1 . GLU I  1 67  ? 68.416  73.411  -41.842 1.00 47.99 ? 40  GLU I OE1 1 
ATOM   9320  O  OE2 . GLU I  1 67  ? 69.180  74.107  -43.786 1.00 53.68 ? 40  GLU I OE2 1 
ATOM   9321  N  N   . GLY I  1 68  ? 65.601  70.457  -45.668 1.00 27.44 ? 41  GLY I N   1 
ATOM   9322  C  CA  . GLY I  1 68  ? 66.170  69.412  -46.502 1.00 33.77 ? 41  GLY I CA  1 
ATOM   9323  C  C   . GLY I  1 68  ? 65.230  68.790  -47.522 1.00 30.12 ? 41  GLY I C   1 
ATOM   9324  O  O   . GLY I  1 68  ? 64.226  69.399  -47.896 1.00 25.59 ? 41  GLY I O   1 
ATOM   9325  N  N   . LEU I  1 69  ? 65.555  67.567  -47.965 1.00 28.82 ? 42  LEU I N   1 
ATOM   9326  C  CA  . LEU I  1 69  ? 64.855  66.899  -49.060 1.00 28.84 ? 42  LEU I CA  1 
ATOM   9327  C  C   . LEU I  1 69  ? 63.620  66.151  -48.570 1.00 24.73 ? 42  LEU I C   1 
ATOM   9328  O  O   . LEU I  1 69  ? 63.657  65.459  -47.549 1.00 26.56 ? 42  LEU I O   1 
ATOM   9329  C  CB  . LEU I  1 69  ? 65.793  65.906  -49.756 1.00 25.05 ? 42  LEU I CB  1 
ATOM   9330  C  CG  . LEU I  1 69  ? 66.990  66.452  -50.524 1.00 30.86 ? 42  LEU I CG  1 
ATOM   9331  C  CD1 . LEU I  1 69  ? 67.892  65.289  -50.896 1.00 37.88 ? 42  LEU I CD1 1 
ATOM   9332  C  CD2 . LEU I  1 69  ? 66.547  67.169  -51.786 1.00 27.82 ? 42  LEU I CD2 1 
ATOM   9333  N  N   . HIS I  1 70  ? 62.532  66.251  -49.332 1.00 23.35 ? 43  HIS I N   1 
ATOM   9334  C  CA  . HIS I  1 70  ? 61.295  65.545  -49.021 1.00 26.41 ? 43  HIS I CA  1 
ATOM   9335  C  C   . HIS I  1 70  ? 60.707  64.929  -50.282 1.00 23.39 ? 43  HIS I C   1 
ATOM   9336  O  O   . HIS I  1 70  ? 60.495  65.634  -51.272 1.00 21.36 ? 43  HIS I O   1 
ATOM   9337  C  CB  . HIS I  1 70  ? 60.267  66.496  -48.403 1.00 22.81 ? 43  HIS I CB  1 
ATOM   9338  C  CG  . HIS I  1 70  ? 60.629  66.947  -47.024 1.00 25.88 ? 43  HIS I CG  1 
ATOM   9339  N  ND1 . HIS I  1 70  ? 60.191  66.289  -45.896 1.00 26.20 ? 43  HIS I ND1 1 
ATOM   9340  C  CD2 . HIS I  1 70  ? 61.370  67.993  -46.591 1.00 24.33 ? 43  HIS I CD2 1 
ATOM   9341  C  CE1 . HIS I  1 70  ? 60.660  66.905  -44.821 1.00 28.77 ? 43  HIS I CE1 1 
ATOM   9342  N  NE2 . HIS I  1 70  ? 61.383  67.939  -45.217 1.00 26.35 ? 43  HIS I NE2 1 
ATOM   9343  N  N   . GLY I  1 71  ? 60.375  63.641  -50.215 1.00 22.82 ? 44  GLY I N   1 
ATOM   9344  C  CA  . GLY I  1 71  ? 59.721  62.998  -51.345 1.00 23.64 ? 44  GLY I CA  1 
ATOM   9345  C  C   . GLY I  1 71  ? 58.395  63.651  -51.681 1.00 27.02 ? 44  GLY I C   1 
ATOM   9346  O  O   . GLY I  1 71  ? 57.652  64.092  -50.802 1.00 22.25 ? 44  GLY I O   1 
ATOM   9347  N  N   . PHE I  1 72  ? 58.083  63.689  -52.977 1.00 21.89 ? 45  PHE I N   1 
ATOM   9348  C  CA  . PHE I  1 72  ? 56.997  64.528  -53.483 1.00 22.35 ? 45  PHE I CA  1 
ATOM   9349  C  C   . PHE I  1 72  ? 56.328  63.744  -54.610 1.00 25.04 ? 45  PHE I C   1 
ATOM   9350  O  O   . PHE I  1 72  ? 56.870  63.687  -55.714 1.00 24.25 ? 45  PHE I O   1 
ATOM   9351  C  CB  . PHE I  1 72  ? 57.590  65.851  -53.961 1.00 21.46 ? 45  PHE I CB  1 
ATOM   9352  C  CG  . PHE I  1 72  ? 56.577  66.912  -54.324 1.00 24.87 ? 45  PHE I CG  1 
ATOM   9353  C  CD1 . PHE I  1 72  ? 55.779  67.515  -53.367 1.00 24.80 ? 45  PHE I CD1 1 
ATOM   9354  C  CD2 . PHE I  1 72  ? 56.486  67.356  -55.631 1.00 22.99 ? 45  PHE I CD2 1 
ATOM   9355  C  CE1 . PHE I  1 72  ? 54.886  68.512  -53.717 1.00 20.65 ? 45  PHE I CE1 1 
ATOM   9356  C  CE2 . PHE I  1 72  ? 55.596  68.359  -55.985 1.00 24.99 ? 45  PHE I CE2 1 
ATOM   9357  C  CZ  . PHE I  1 72  ? 54.796  68.930  -55.036 1.00 22.28 ? 45  PHE I CZ  1 
ATOM   9358  N  N   . HIS I  1 73  ? 55.178  63.116  -54.336 1.00 23.62 ? 46  HIS I N   1 
ATOM   9359  C  CA  . HIS I  1 73  ? 54.637  62.107  -55.251 1.00 24.16 ? 46  HIS I CA  1 
ATOM   9360  C  C   . HIS I  1 73  ? 53.143  62.252  -55.476 1.00 27.51 ? 46  HIS I C   1 
ATOM   9361  O  O   . HIS I  1 73  ? 52.392  62.659  -54.586 1.00 23.86 ? 46  HIS I O   1 
ATOM   9362  C  CB  . HIS I  1 73  ? 54.886  60.686  -54.743 1.00 22.77 ? 46  HIS I CB  1 
ATOM   9363  C  CG  . HIS I  1 73  ? 56.303  60.433  -54.356 1.00 26.94 ? 46  HIS I CG  1 
ATOM   9364  N  ND1 . HIS I  1 73  ? 56.656  59.887  -53.143 1.00 31.03 ? 46  HIS I ND1 1 
ATOM   9365  C  CD2 . HIS I  1 73  ? 57.459  60.661  -55.019 1.00 23.46 ? 46  HIS I CD2 1 
ATOM   9366  C  CE1 . HIS I  1 73  ? 57.969  59.790  -53.077 1.00 27.03 ? 46  HIS I CE1 1 
ATOM   9367  N  NE2 . HIS I  1 73  ? 58.481  60.264  -54.197 1.00 26.20 ? 46  HIS I NE2 1 
ATOM   9368  N  N   . VAL I  1 74  ? 52.707  61.876  -56.677 1.00 25.74 ? 47  VAL I N   1 
ATOM   9369  C  CA  . VAL I  1 74  ? 51.285  61.741  -56.961 1.00 25.95 ? 47  VAL I CA  1 
ATOM   9370  C  C   . VAL I  1 74  ? 50.897  60.302  -56.666 1.00 29.05 ? 47  VAL I C   1 
ATOM   9371  O  O   . VAL I  1 74  ? 51.451  59.358  -57.245 1.00 22.30 ? 47  VAL I O   1 
ATOM   9372  C  CB  . VAL I  1 74  ? 50.947  62.119  -58.410 1.00 23.56 ? 47  VAL I CB  1 
ATOM   9373  C  CG1 . VAL I  1 74  ? 49.444  62.000  -58.621 1.00 22.25 ? 47  VAL I CG1 1 
ATOM   9374  C  CG2 . VAL I  1 74  ? 51.409  63.543  -58.695 1.00 25.54 ? 47  VAL I CG2 1 
ATOM   9375  N  N   . HIS I  1 75  ? 49.963  60.131  -55.751 1.00 21.55 ? 48  HIS I N   1 
ATOM   9376  C  CA  . HIS I  1 75  ? 49.496  58.808  -55.368 1.00 21.48 ? 48  HIS I CA  1 
ATOM   9377  C  C   . HIS I  1 75  ? 48.205  58.495  -56.115 1.00 23.33 ? 48  HIS I C   1 
ATOM   9378  O  O   . HIS I  1 75  ? 47.543  59.387  -56.660 1.00 27.68 ? 48  HIS I O   1 
ATOM   9379  C  CB  . HIS I  1 75  ? 49.299  58.716  -53.850 1.00 23.82 ? 48  HIS I CB  1 
ATOM   9380  C  CG  . HIS I  1 75  ? 50.585  58.689  -53.085 1.00 25.29 ? 48  HIS I CG  1 
ATOM   9381  N  ND1 . HIS I  1 75  ? 50.933  57.650  -52.252 1.00 24.84 ? 48  HIS I ND1 1 
ATOM   9382  C  CD2 . HIS I  1 75  ? 51.604  59.582  -53.017 1.00 21.48 ? 48  HIS I CD2 1 
ATOM   9383  C  CE1 . HIS I  1 75  ? 52.115  57.893  -51.714 1.00 21.85 ? 48  HIS I CE1 1 
ATOM   9384  N  NE2 . HIS I  1 75  ? 52.547  59.057  -52.168 1.00 24.38 ? 48  HIS I NE2 1 
ATOM   9385  N  N   . GLU I  1 76  ? 47.841  57.209  -56.117 1.00 27.56 ? 49  GLU I N   1 
ATOM   9386  C  CA  . GLU I  1 76  ? 46.876  56.713  -57.094 1.00 28.75 ? 49  GLU I CA  1 
ATOM   9387  C  C   . GLU I  1 76  ? 45.477  57.285  -56.890 1.00 29.40 ? 49  GLU I C   1 
ATOM   9388  O  O   . GLU I  1 76  ? 44.823  57.668  -57.864 1.00 27.86 ? 49  GLU I O   1 
ATOM   9389  C  CB  . GLU I  1 76  ? 46.823  55.185  -57.064 1.00 31.54 ? 49  GLU I CB  1 
ATOM   9390  C  CG  . GLU I  1 76  ? 45.979  54.653  -58.207 1.00 33.55 ? 49  GLU I CG  1 
ATOM   9391  C  CD  . GLU I  1 76  ? 45.905  53.146  -58.244 1.00 40.91 ? 49  GLU I CD  1 
ATOM   9392  O  OE1 . GLU I  1 76  ? 46.544  52.486  -57.389 1.00 35.80 ? 49  GLU I OE1 1 
ATOM   9393  O  OE2 . GLU I  1 76  ? 45.190  52.629  -59.133 1.00 43.55 ? 49  GLU I OE2 1 
ATOM   9394  N  N   . PHE I  1 77  ? 45.001  57.359  -55.645 1.00 29.58 ? 50  PHE I N   1 
ATOM   9395  C  CA  . PHE I  1 77  ? 43.605  57.670  -55.363 1.00 27.89 ? 50  PHE I CA  1 
ATOM   9396  C  C   . PHE I  1 77  ? 43.457  59.049  -54.736 1.00 28.08 ? 50  PHE I C   1 
ATOM   9397  O  O   . PHE I  1 77  ? 44.274  59.450  -53.908 1.00 29.84 ? 50  PHE I O   1 
ATOM   9398  C  CB  . PHE I  1 77  ? 43.006  56.616  -54.432 1.00 31.12 ? 50  PHE I CB  1 
ATOM   9399  C  CG  . PHE I  1 77  ? 43.185  55.227  -54.935 1.00 33.33 ? 50  PHE I CG  1 
ATOM   9400  C  CD1 . PHE I  1 77  ? 42.556  54.827  -56.098 1.00 36.03 ? 50  PHE I CD1 1 
ATOM   9401  C  CD2 . PHE I  1 77  ? 44.013  54.336  -54.275 1.00 35.38 ? 50  PHE I CD2 1 
ATOM   9402  C  CE1 . PHE I  1 77  ? 42.730  53.538  -56.589 1.00 40.16 ? 50  PHE I CE1 1 
ATOM   9403  C  CE2 . PHE I  1 77  ? 44.198  53.051  -54.763 1.00 42.64 ? 50  PHE I CE2 1 
ATOM   9404  C  CZ  . PHE I  1 77  ? 43.554  52.655  -55.916 1.00 37.58 ? 50  PHE I CZ  1 
ATOM   9405  N  N   . GLY I  1 78  ? 42.409  59.765  -55.135 1.00 24.20 ? 51  GLY I N   1 
ATOM   9406  C  CA  . GLY I  1 78  ? 42.056  61.017  -54.496 1.00 23.96 ? 51  GLY I CA  1 
ATOM   9407  C  C   . GLY I  1 78  ? 41.121  60.725  -53.338 1.00 29.76 ? 51  GLY I C   1 
ATOM   9408  O  O   . GLY I  1 78  ? 40.016  61.266  -53.254 1.00 29.98 ? 51  GLY I O   1 
ATOM   9409  N  N   . ASP I  1 79  ? 41.564  59.841  -52.456 1.00 29.28 ? 52  ASP I N   1 
ATOM   9410  C  CA  . ASP I  1 79  ? 40.760  59.317  -51.361 1.00 29.96 ? 52  ASP I CA  1 
ATOM   9411  C  C   . ASP I  1 79  ? 41.434  59.751  -50.069 1.00 30.07 ? 52  ASP I C   1 
ATOM   9412  O  O   . ASP I  1 79  ? 42.511  59.254  -49.722 1.00 29.06 ? 52  ASP I O   1 
ATOM   9413  C  CB  . ASP I  1 79  ? 40.641  57.795  -51.449 1.00 33.13 ? 52  ASP I CB  1 
ATOM   9414  C  CG  . ASP I  1 79  ? 39.754  57.203  -50.364 1.00 38.23 ? 52  ASP I CG  1 
ATOM   9415  O  OD1 . ASP I  1 79  ? 39.653  57.795  -49.264 1.00 35.73 ? 52  ASP I OD1 1 
ATOM   9416  O  OD2 . ASP I  1 79  ? 39.181  56.121  -50.613 1.00 36.65 ? 52  ASP I OD2 1 
ATOM   9417  N  N   . ASN I  1 80  ? 40.803  60.695  -49.380 1.00 27.80 ? 53  ASN I N   1 
ATOM   9418  C  CA  . ASN I  1 80  ? 41.304  61.235  -48.129 1.00 26.51 ? 53  ASN I CA  1 
ATOM   9419  C  C   . ASN I  1 80  ? 40.475  60.761  -46.937 1.00 32.23 ? 53  ASN I C   1 
ATOM   9420  O  O   . ASN I  1 80  ? 40.578  61.339  -45.847 1.00 33.38 ? 53  ASN I O   1 
ATOM   9421  C  CB  . ASN I  1 80  ? 41.314  62.761  -48.201 1.00 29.09 ? 53  ASN I CB  1 
ATOM   9422  C  CG  . ASN I  1 80  ? 42.204  63.388  -47.140 1.00 48.39 ? 53  ASN I CG  1 
ATOM   9423  O  OD1 . ASN I  1 80  ? 41.834  64.383  -46.509 1.00 50.93 ? 53  ASN I OD1 1 
ATOM   9424  N  ND2 . ASN I  1 80  ? 43.385  62.811  -46.943 1.00 46.07 ? 53  ASN I ND2 1 
ATOM   9425  N  N   . THR I  1 81  ? 39.659  59.717  -47.123 1.00 28.49 ? 54  THR I N   1 
ATOM   9426  C  CA  . THR I  1 81  ? 38.708  59.334  -46.081 1.00 32.84 ? 54  THR I CA  1 
ATOM   9427  C  C   . THR I  1 81  ? 39.420  58.910  -44.804 1.00 39.20 ? 54  THR I C   1 
ATOM   9428  O  O   . THR I  1 81  ? 38.879  59.089  -43.706 1.00 39.67 ? 54  THR I O   1 
ATOM   9429  C  CB  . THR I  1 81  ? 37.794  58.207  -46.565 1.00 32.54 ? 54  THR I CB  1 
ATOM   9430  O  OG1 . THR I  1 81  ? 38.581  57.068  -46.935 1.00 34.92 ? 54  THR I OG1 1 
ATOM   9431  C  CG2 . THR I  1 81  ? 36.987  58.645  -47.763 1.00 38.83 ? 54  THR I CG2 1 
ATOM   9432  N  N   . ALA I  1 82  ? 40.629  58.362  -44.920 1.00 37.32 ? 55  ALA I N   1 
ATOM   9433  C  CA  . ALA I  1 82  ? 41.441  57.954  -43.779 1.00 34.08 ? 55  ALA I CA  1 
ATOM   9434  C  C   . ALA I  1 82  ? 42.710  58.791  -43.680 1.00 33.88 ? 55  ALA I C   1 
ATOM   9435  O  O   . ALA I  1 82  ? 43.778  58.292  -43.320 1.00 40.47 ? 55  ALA I O   1 
ATOM   9436  C  CB  . ALA I  1 82  ? 41.796  56.469  -43.865 1.00 39.71 ? 55  ALA I CB  1 
ATOM   9437  N  N   . GLY I  1 83  ? 42.615  60.075  -44.006 1.00 31.37 ? 56  GLY I N   1 
ATOM   9438  C  CA  . GLY I  1 83  ? 43.843  60.829  -44.078 1.00 32.12 ? 56  GLY I CA  1 
ATOM   9439  C  C   . GLY I  1 83  ? 44.636  60.449  -45.329 1.00 34.77 ? 56  GLY I C   1 
ATOM   9440  O  O   . GLY I  1 83  ? 44.115  59.890  -46.299 1.00 28.64 ? 56  GLY I O   1 
ATOM   9441  N  N   . CYS I  1 84  ? 45.930  60.758  -45.285 1.00 30.49 ? 57  CYS I N   1 
ATOM   9442  C  CA  . CYS I  1 84  ? 46.779  60.536  -46.447 1.00 29.73 ? 57  CYS I CA  1 
ATOM   9443  C  C   . CYS I  1 84  ? 46.983  59.049  -46.736 1.00 33.76 ? 57  CYS I C   1 
ATOM   9444  O  O   . CYS I  1 84  ? 47.314  58.686  -47.872 1.00 30.81 ? 57  CYS I O   1 
ATOM   9445  C  CB  . CYS I  1 84  ? 48.107  61.261  -46.234 1.00 33.04 ? 57  CYS I CB  1 
ATOM   9446  S  SG  . CYS I  1 84  ? 47.913  63.105  -46.149 1.00 38.46 ? 57  CYS I SG  1 
ATOM   9447  N  N   . THR I  1 85  ? 46.754  58.187  -45.741 1.00 32.00 ? 58  THR I N   1 
ATOM   9448  C  CA  . THR I  1 85  ? 46.915  56.745  -45.922 1.00 30.37 ? 58  THR I CA  1 
ATOM   9449  C  C   . THR I  1 85  ? 46.027  56.210  -47.036 1.00 34.00 ? 58  THR I C   1 
ATOM   9450  O  O   . THR I  1 85  ? 46.433  55.316  -47.790 1.00 37.05 ? 58  THR I O   1 
ATOM   9451  C  CB  . THR I  1 85  ? 46.602  56.023  -44.609 1.00 31.11 ? 58  THR I CB  1 
ATOM   9452  O  OG1 . THR I  1 85  ? 47.550  56.413  -43.612 1.00 43.40 ? 58  THR I OG1 1 
ATOM   9453  C  CG2 . THR I  1 85  ? 46.658  54.520  -44.791 1.00 39.76 ? 58  THR I CG2 1 
ATOM   9454  N  N   . SER I  1 86  ? 44.811  56.736  -47.169 1.00 27.88 ? 59  SER I N   1 
ATOM   9455  C  CA  . SER I  1 86  ? 43.901  56.137  -48.132 1.00 29.37 ? 59  SER I CA  1 
ATOM   9456  C  C   . SER I  1 86  ? 44.196  56.563  -49.568 1.00 30.87 ? 59  SER I C   1 
ATOM   9457  O  O   . SER I  1 86  ? 43.449  56.179  -50.477 1.00 27.29 ? 59  SER I O   1 
ATOM   9458  C  CB  . SER I  1 86  ? 42.449  56.457  -47.764 1.00 33.95 ? 59  SER I CB  1 
ATOM   9459  O  OG  . SER I  1 86  ? 42.368  57.751  -47.222 1.00 37.00 ? 59  SER I OG  1 
ATOM   9460  N  N   . ALA I  1 87  ? 45.261  57.338  -49.790 1.00 27.58 ? 60  ALA I N   1 
ATOM   9461  C  CA  . ALA I  1 87  ? 45.637  57.695  -51.156 1.00 30.78 ? 60  ALA I CA  1 
ATOM   9462  C  C   . ALA I  1 87  ? 46.234  56.521  -51.920 1.00 29.98 ? 60  ALA I C   1 
ATOM   9463  O  O   . ALA I  1 87  ? 46.388  56.616  -53.141 1.00 28.26 ? 60  ALA I O   1 
ATOM   9464  C  CB  . ALA I  1 87  ? 46.635  58.860  -51.155 1.00 26.23 ? 60  ALA I CB  1 
ATOM   9465  N  N   . GLY I  1 88  ? 46.566  55.425  -51.245 1.00 31.21 ? 61  GLY I N   1 
ATOM   9466  C  CA  . GLY I  1 88  ? 47.121  54.269  -51.915 1.00 33.59 ? 61  GLY I CA  1 
ATOM   9467  C  C   . GLY I  1 88  ? 48.560  54.515  -52.323 1.00 30.66 ? 61  GLY I C   1 
ATOM   9468  O  O   . GLY I  1 88  ? 49.196  55.460  -51.845 1.00 29.10 ? 61  GLY I O   1 
ATOM   9469  N  N   . PRO I  1 89  ? 49.094  53.693  -53.227 1.00 29.50 ? 62  PRO I N   1 
ATOM   9470  C  CA  . PRO I  1 89  ? 50.509  53.791  -53.601 1.00 29.87 ? 62  PRO I CA  1 
ATOM   9471  C  C   . PRO I  1 89  ? 50.738  54.891  -54.636 1.00 23.81 ? 62  PRO I C   1 
ATOM   9472  O  O   . PRO I  1 89  ? 49.817  55.591  -55.050 1.00 28.94 ? 62  PRO I O   1 
ATOM   9473  C  CB  . PRO I  1 89  ? 50.797  52.407  -54.190 1.00 32.65 ? 62  PRO I CB  1 
ATOM   9474  C  CG  . PRO I  1 89  ? 49.517  52.047  -54.866 1.00 32.78 ? 62  PRO I CG  1 
ATOM   9475  C  CD  . PRO I  1 89  ? 48.416  52.601  -53.948 1.00 32.40 ? 62  PRO I CD  1 
ATOM   9476  N  N   . HIS I  1 90  ? 51.998  55.026  -55.061 1.00 30.63 ? 63  HIS I N   1 
ATOM   9477  C  CA  . HIS I  1 90  ? 52.321  55.974  -56.122 1.00 24.94 ? 63  HIS I CA  1 
ATOM   9478  C  C   . HIS I  1 90  ? 51.535  55.638  -57.383 1.00 29.03 ? 63  HIS I C   1 
ATOM   9479  O  O   . HIS I  1 90  ? 51.358  54.471  -57.724 1.00 31.37 ? 63  HIS I O   1 
ATOM   9480  C  CB  . HIS I  1 90  ? 53.826  55.966  -56.424 1.00 23.11 ? 63  HIS I CB  1 
ATOM   9481  C  CG  . HIS I  1 90  ? 54.675  56.397  -55.277 1.00 26.40 ? 63  HIS I CG  1 
ATOM   9482  N  ND1 . HIS I  1 90  ? 56.045  56.463  -55.351 1.00 31.12 ? 63  HIS I ND1 1 
ATOM   9483  C  CD2 . HIS I  1 90  ? 54.351  56.768  -54.012 1.00 24.64 ? 63  HIS I CD2 1 
ATOM   9484  C  CE1 . HIS I  1 90  ? 56.536  56.856  -54.194 1.00 26.67 ? 63  HIS I CE1 1 
ATOM   9485  N  NE2 . HIS I  1 90  ? 55.528  57.053  -53.362 1.00 27.77 ? 63  HIS I NE2 1 
ATOM   9486  N  N   . PHE I  1 91  ? 51.018  56.671  -58.040 1.00 25.18 ? 64  PHE I N   1 
ATOM   9487  C  CA  . PHE I  1 91  ? 50.295  56.508  -59.295 1.00 31.65 ? 64  PHE I CA  1 
ATOM   9488  C  C   . PHE I  1 91  ? 51.188  55.832  -60.331 1.00 29.33 ? 64  PHE I C   1 
ATOM   9489  O  O   . PHE I  1 91  ? 52.232  56.373  -60.702 1.00 27.47 ? 64  PHE I O   1 
ATOM   9490  C  CB  . PHE I  1 91  ? 49.835  57.875  -59.785 1.00 24.67 ? 64  PHE I CB  1 
ATOM   9491  C  CG  . PHE I  1 91  ? 49.038  57.833  -61.056 1.00 27.80 ? 64  PHE I CG  1 
ATOM   9492  C  CD1 . PHE I  1 91  ? 48.149  56.798  -61.306 1.00 26.99 ? 64  PHE I CD1 1 
ATOM   9493  C  CD2 . PHE I  1 91  ? 49.156  58.846  -61.987 1.00 30.65 ? 64  PHE I CD2 1 
ATOM   9494  C  CE1 . PHE I  1 91  ? 47.416  56.772  -62.487 1.00 35.66 ? 64  PHE I CE1 1 
ATOM   9495  C  CE2 . PHE I  1 91  ? 48.421  58.824  -63.171 1.00 34.40 ? 64  PHE I CE2 1 
ATOM   9496  C  CZ  . PHE I  1 91  ? 47.549  57.795  -63.409 1.00 28.51 ? 64  PHE I CZ  1 
ATOM   9497  N  N   . ASN I  1 92  ? 50.780  54.650  -60.793 1.00 32.11 ? 65  ASN I N   1 
ATOM   9498  C  CA  . ASN I  1 92  ? 51.690  53.751  -61.505 1.00 32.69 ? 65  ASN I CA  1 
ATOM   9499  C  C   . ASN I  1 92  ? 50.921  52.883  -62.499 1.00 37.20 ? 65  ASN I C   1 
ATOM   9500  O  O   . ASN I  1 92  ? 50.890  51.654  -62.367 1.00 35.92 ? 65  ASN I O   1 
ATOM   9501  C  CB  . ASN I  1 92  ? 52.446  52.883  -60.499 1.00 32.10 ? 65  ASN I CB  1 
ATOM   9502  C  CG  . ASN I  1 92  ? 53.516  52.001  -61.144 1.00 34.33 ? 65  ASN I CG  1 
ATOM   9503  O  OD1 . ASN I  1 92  ? 54.028  52.297  -62.222 1.00 33.24 ? 65  ASN I OD1 1 
ATOM   9504  N  ND2 . ASN I  1 92  ? 53.871  50.915  -60.453 1.00 27.19 ? 65  ASN I ND2 1 
ATOM   9505  N  N   . PRO I  1 93  ? 50.289  53.482  -63.509 1.00 30.43 ? 66  PRO I N   1 
ATOM   9506  C  CA  . PRO I  1 93  ? 49.458  52.679  -64.414 1.00 39.30 ? 66  PRO I CA  1 
ATOM   9507  C  C   . PRO I  1 93  ? 50.266  51.751  -65.321 1.00 41.36 ? 66  PRO I C   1 
ATOM   9508  O  O   . PRO I  1 93  ? 49.696  50.788  -65.842 1.00 43.47 ? 66  PRO I O   1 
ATOM   9509  C  CB  . PRO I  1 93  ? 48.683  53.737  -65.209 1.00 35.28 ? 66  PRO I CB  1 
ATOM   9510  C  CG  . PRO I  1 93  ? 49.569  54.945  -65.187 1.00 38.99 ? 66  PRO I CG  1 
ATOM   9511  C  CD  . PRO I  1 93  ? 50.327  54.905  -63.891 1.00 32.48 ? 66  PRO I CD  1 
ATOM   9512  N  N   . LEU I  1 94  ? 51.570  51.972  -65.491 1.00 41.58 ? 67  LEU I N   1 
ATOM   9513  C  CA  . LEU I  1 94  ? 52.401  51.089  -66.305 1.00 40.80 ? 67  LEU I CA  1 
ATOM   9514  C  C   . LEU I  1 94  ? 53.131  50.038  -65.477 1.00 45.55 ? 67  LEU I C   1 
ATOM   9515  O  O   . LEU I  1 94  ? 53.984  49.326  -66.016 1.00 50.99 ? 67  LEU I O   1 
ATOM   9516  C  CB  . LEU I  1 94  ? 53.406  51.908  -67.117 1.00 43.30 ? 67  LEU I CB  1 
ATOM   9517  C  CG  . LEU I  1 94  ? 52.799  53.025  -67.967 1.00 44.95 ? 67  LEU I CG  1 
ATOM   9518  C  CD1 . LEU I  1 94  ? 53.855  54.090  -68.291 1.00 48.42 ? 67  LEU I CD1 1 
ATOM   9519  C  CD2 . LEU I  1 94  ? 52.167  52.492  -69.243 1.00 39.96 ? 67  LEU I CD2 1 
ATOM   9520  N  N   . SER I  1 95  ? 52.825  49.940  -64.179 1.00 37.14 ? 68  SER I N   1 
ATOM   9521  C  CA  . SER I  1 95  ? 53.379  48.915  -63.292 1.00 41.75 ? 68  SER I CA  1 
ATOM   9522  C  C   . SER I  1 95  ? 54.905  48.889  -63.316 1.00 46.66 ? 68  SER I C   1 
ATOM   9523  O  O   . SER I  1 95  ? 55.531  47.824  -63.286 1.00 50.79 ? 68  SER I O   1 
ATOM   9524  C  CB  . SER I  1 95  ? 52.808  47.542  -63.634 1.00 43.31 ? 68  SER I CB  1 
ATOM   9525  O  OG  . SER I  1 95  ? 51.462  47.666  -64.047 1.00 52.48 ? 68  SER I OG  1 
ATOM   9526  N  N   . ARG I  1 96  ? 55.512  50.070  -63.348 1.00 37.07 ? 69  ARG I N   1 
ATOM   9527  C  CA  . ARG I  1 96  ? 56.960  50.172  -63.328 1.00 34.46 ? 69  ARG I CA  1 
ATOM   9528  C  C   . ARG I  1 96  ? 57.475  50.192  -61.896 1.00 43.92 ? 69  ARG I C   1 
ATOM   9529  O  O   . ARG I  1 96  ? 56.713  50.237  -60.927 1.00 37.92 ? 69  ARG I O   1 
ATOM   9530  C  CB  . ARG I  1 96  ? 57.420  51.411  -64.091 1.00 36.31 ? 69  ARG I CB  1 
ATOM   9531  C  CG  . ARG I  1 96  ? 56.767  51.562  -65.451 1.00 48.21 ? 69  ARG I CG  1 
ATOM   9532  C  CD  . ARG I  1 96  ? 57.705  51.153  -66.577 1.00 41.88 ? 69  ARG I CD  1 
ATOM   9533  N  NE  . ARG I  1 96  ? 57.276  51.714  -67.855 1.00 59.38 ? 69  ARG I NE  1 
ATOM   9534  C  CZ  . ARG I  1 96  ? 58.009  52.523  -68.612 1.00 52.87 ? 69  ARG I CZ  1 
ATOM   9535  N  NH1 . ARG I  1 96  ? 59.242  52.866  -68.269 1.00 52.65 ? 69  ARG I NH1 1 
ATOM   9536  N  NH2 . ARG I  1 96  ? 57.491  52.999  -69.741 1.00 48.00 ? 69  ARG I NH2 1 
ATOM   9537  N  N   . LYS I  1 97  ? 58.793  50.138  -61.759 1.00 38.06 ? 70  LYS I N   1 
ATOM   9538  C  CA  . LYS I  1 97  ? 59.389  50.333  -60.454 1.00 38.00 ? 70  LYS I CA  1 
ATOM   9539  C  C   . LYS I  1 97  ? 59.561  51.829  -60.181 1.00 32.26 ? 70  LYS I C   1 
ATOM   9540  O  O   . LYS I  1 97  ? 59.554  52.660  -61.097 1.00 27.60 ? 70  LYS I O   1 
ATOM   9541  C  CB  . LYS I  1 97  ? 60.726  49.601  -60.366 1.00 43.05 ? 70  LYS I CB  1 
ATOM   9542  C  CG  . LYS I  1 97  ? 60.601  48.075  -60.467 1.00 44.10 ? 70  LYS I CG  1 
ATOM   9543  C  CD  . LYS I  1 97  ? 61.753  47.361  -59.761 1.00 46.64 ? 70  LYS I CD  1 
ATOM   9544  C  CE  . LYS I  1 97  ? 62.337  46.240  -60.620 1.00 54.06 ? 70  LYS I CE  1 
ATOM   9545  N  NZ  . LYS I  1 97  ? 62.934  46.764  -61.888 1.00 53.16 ? 70  LYS I NZ  1 
ATOM   9546  N  N   . HIS I  1 98  ? 59.697  52.164  -58.899 1.00 32.64 ? 71  HIS I N   1 
ATOM   9547  C  CA  . HIS I  1 98  ? 59.886  53.555  -58.506 1.00 28.06 ? 71  HIS I CA  1 
ATOM   9548  C  C   . HIS I  1 98  ? 61.222  54.080  -59.021 1.00 30.75 ? 71  HIS I C   1 
ATOM   9549  O  O   . HIS I  1 98  ? 62.243  53.388  -58.975 1.00 30.45 ? 71  HIS I O   1 
ATOM   9550  C  CB  . HIS I  1 98  ? 59.820  53.681  -56.982 1.00 26.95 ? 71  HIS I CB  1 
ATOM   9551  C  CG  . HIS I  1 98  ? 60.101  55.062  -56.472 1.00 28.57 ? 71  HIS I CG  1 
ATOM   9552  N  ND1 . HIS I  1 98  ? 59.159  56.069  -56.494 1.00 34.74 ? 71  HIS I ND1 1 
ATOM   9553  C  CD2 . HIS I  1 98  ? 61.208  55.596  -55.904 1.00 27.41 ? 71  HIS I CD2 1 
ATOM   9554  C  CE1 . HIS I  1 98  ? 59.679  57.166  -55.972 1.00 26.19 ? 71  HIS I CE1 1 
ATOM   9555  N  NE2 . HIS I  1 98  ? 60.921  56.906  -55.607 1.00 29.87 ? 71  HIS I NE2 1 
ATOM   9556  N  N   . GLY I  1 99  ? 61.213  55.310  -59.527 1.00 25.84 ? 72  GLY I N   1 
ATOM   9557  C  CA  . GLY I  1 99  ? 62.455  55.975  -59.882 1.00 29.73 ? 72  GLY I CA  1 
ATOM   9558  C  C   . GLY I  1 99  ? 62.408  57.476  -59.656 1.00 32.35 ? 72  GLY I C   1 
ATOM   9559  O  O   . GLY I  1 99  ? 61.453  57.997  -59.059 1.00 27.09 ? 72  GLY I O   1 
ATOM   9560  N  N   . GLY I  1 100 ? 63.439  58.184  -60.116 1.00 28.71 ? 73  GLY I N   1 
ATOM   9561  C  CA  . GLY I  1 100 ? 63.445  59.629  -60.096 1.00 30.17 ? 73  GLY I CA  1 
ATOM   9562  C  C   . GLY I  1 100 ? 62.762  60.173  -61.332 1.00 30.76 ? 73  GLY I C   1 
ATOM   9563  O  O   . GLY I  1 100 ? 62.558  59.449  -62.311 1.00 32.19 ? 73  GLY I O   1 
ATOM   9564  N  N   . PRO I  1 101 ? 62.383  61.456  -61.323 1.00 29.73 ? 74  PRO I N   1 
ATOM   9565  C  CA  . PRO I  1 101 ? 61.585  61.980  -62.449 1.00 30.38 ? 74  PRO I CA  1 
ATOM   9566  C  C   . PRO I  1 101 ? 62.299  61.893  -63.786 1.00 33.03 ? 74  PRO I C   1 
ATOM   9567  O  O   . PRO I  1 101 ? 61.631  61.849  -64.832 1.00 30.91 ? 74  PRO I O   1 
ATOM   9568  C  CB  . PRO I  1 101 ? 61.318  63.439  -62.050 1.00 32.80 ? 74  PRO I CB  1 
ATOM   9569  C  CG  . PRO I  1 101 ? 62.350  63.762  -61.021 1.00 30.04 ? 74  PRO I CG  1 
ATOM   9570  C  CD  . PRO I  1 101 ? 62.617  62.477  -60.287 1.00 31.22 ? 74  PRO I CD  1 
ATOM   9571  N  N   . LYS I  1 102 ? 63.626  61.840  -63.786 1.00 32.01 ? 75  LYS I N   1 
ATOM   9572  C  CA  . LYS I  1 102 ? 64.384  61.811  -65.028 1.00 38.58 ? 75  LYS I CA  1 
ATOM   9573  C  C   . LYS I  1 102 ? 64.709  60.396  -65.484 1.00 35.22 ? 75  LYS I C   1 
ATOM   9574  O  O   . LYS I  1 102 ? 65.261  60.228  -66.576 1.00 39.39 ? 75  LYS I O   1 
ATOM   9575  C  CB  . LYS I  1 102 ? 65.670  62.627  -64.870 1.00 39.02 ? 75  LYS I CB  1 
ATOM   9576  C  CG  . LYS I  1 102 ? 65.391  64.126  -64.806 1.00 45.01 ? 75  LYS I CG  1 
ATOM   9577  C  CD  . LYS I  1 102 ? 64.467  64.534  -65.968 1.00 49.84 ? 75  LYS I CD  1 
ATOM   9578  C  CE  . LYS I  1 102 ? 64.165  66.032  -65.979 1.00 47.89 ? 75  LYS I CE  1 
ATOM   9579  N  NZ  . LYS I  1 102 ? 63.338  66.461  -64.803 1.00 49.70 ? 75  LYS I NZ  1 
ATOM   9580  N  N   . ASP I  1 103 ? 64.373  59.384  -64.688 1.00 35.48 ? 76  ASP I N   1 
ATOM   9581  C  CA  . ASP I  1 103 ? 64.608  57.998  -65.069 1.00 36.71 ? 76  ASP I CA  1 
ATOM   9582  C  C   . ASP I  1 103 ? 63.538  57.512  -66.038 1.00 44.46 ? 76  ASP I C   1 
ATOM   9583  O  O   . ASP I  1 103 ? 62.403  58.006  -66.051 1.00 38.54 ? 76  ASP I O   1 
ATOM   9584  C  CB  . ASP I  1 103 ? 64.627  57.101  -63.833 1.00 37.91 ? 76  ASP I CB  1 
ATOM   9585  C  CG  . ASP I  1 103 ? 65.712  57.485  -62.854 1.00 47.59 ? 76  ASP I CG  1 
ATOM   9586  O  OD1 . ASP I  1 103 ? 66.678  58.150  -63.291 1.00 52.90 ? 76  ASP I OD1 1 
ATOM   9587  O  OD2 . ASP I  1 103 ? 65.622  57.098  -61.661 1.00 51.38 ? 76  ASP I OD2 1 
ATOM   9588  N  N   . GLU I  1 104 ? 63.906  56.524  -66.859 1.00 42.38 ? 77  GLU I N   1 
ATOM   9589  C  CA  . GLU I  1 104 ? 62.898  55.946  -67.736 1.00 41.86 ? 77  GLU I CA  1 
ATOM   9590  C  C   . GLU I  1 104 ? 62.040  54.921  -67.005 1.00 36.49 ? 77  GLU I C   1 
ATOM   9591  O  O   . GLU I  1 104 ? 60.834  54.831  -67.260 1.00 44.06 ? 77  GLU I O   1 
ATOM   9592  C  CB  . GLU I  1 104 ? 63.552  55.338  -68.979 1.00 47.83 ? 77  GLU I CB  1 
ATOM   9593  C  CG  . GLU I  1 104 ? 62.553  54.571  -69.833 1.00 57.47 ? 77  GLU I CG  1 
ATOM   9594  C  CD  . GLU I  1 104 ? 61.907  55.447  -70.898 1.00 71.69 ? 77  GLU I CD  1 
ATOM   9595  O  OE1 . GLU I  1 104 ? 62.570  56.407  -71.367 1.00 70.31 ? 77  GLU I OE1 1 
ATOM   9596  O  OE2 . GLU I  1 104 ? 60.723  55.190  -71.238 1.00 67.30 ? 77  GLU I OE2 1 
ATOM   9597  N  N   . GLU I  1 105 ? 62.629  54.165  -66.084 1.00 34.00 ? 78  GLU I N   1 
ATOM   9598  C  CA  . GLU I  1 105 ? 61.869  53.315  -65.180 1.00 36.83 ? 78  GLU I CA  1 
ATOM   9599  C  C   . GLU I  1 105 ? 61.444  54.173  -63.990 1.00 37.85 ? 78  GLU I C   1 
ATOM   9600  O  O   . GLU I  1 105 ? 62.274  54.536  -63.149 1.00 35.52 ? 78  GLU I O   1 
ATOM   9601  C  CB  . GLU I  1 105 ? 62.696  52.109  -64.739 1.00 30.75 ? 78  GLU I CB  1 
ATOM   9602  C  CG  . GLU I  1 105 ? 61.988  51.181  -63.749 1.00 40.67 ? 78  GLU I CG  1 
ATOM   9603  C  CD  . GLU I  1 105 ? 60.996  50.230  -64.409 1.00 52.94 ? 78  GLU I CD  1 
ATOM   9604  O  OE1 . GLU I  1 105 ? 60.612  50.472  -65.575 1.00 57.92 ? 78  GLU I OE1 1 
ATOM   9605  O  OE2 . GLU I  1 105 ? 60.593  49.240  -63.756 1.00 59.44 ? 78  GLU I OE2 1 
ATOM   9606  N  N   . ARG I  1 106 ? 60.161  54.519  -63.939 1.00 33.93 ? 79  ARG I N   1 
ATOM   9607  C  CA  . ARG I  1 106 ? 59.628  55.333  -62.856 1.00 35.37 ? 79  ARG I CA  1 
ATOM   9608  C  C   . ARG I  1 106 ? 58.116  55.205  -62.865 1.00 37.44 ? 79  ARG I C   1 
ATOM   9609  O  O   . ARG I  1 106 ? 57.512  54.847  -63.878 1.00 34.02 ? 79  ARG I O   1 
ATOM   9610  C  CB  . ARG I  1 106 ? 60.031  56.808  -62.997 1.00 29.33 ? 79  ARG I CB  1 
ATOM   9611  C  CG  . ARG I  1 106 ? 59.533  57.446  -64.294 1.00 33.30 ? 79  ARG I CG  1 
ATOM   9612  C  CD  . ARG I  1 106 ? 59.611  58.971  -64.265 1.00 34.45 ? 79  ARG I CD  1 
ATOM   9613  N  NE  . ARG I  1 106 ? 58.376  59.571  -63.761 1.00 30.53 ? 79  ARG I NE  1 
ATOM   9614  C  CZ  . ARG I  1 106 ? 58.083  60.861  -63.848 1.00 31.29 ? 79  ARG I CZ  1 
ATOM   9615  N  NH1 . ARG I  1 106 ? 58.916  61.724  -64.414 1.00 33.12 ? 79  ARG I NH1 1 
ATOM   9616  N  NH2 . ARG I  1 106 ? 56.913  61.297  -63.374 1.00 28.62 ? 79  ARG I NH2 1 
ATOM   9617  N  N   . HIS I  1 107 ? 57.510  55.502  -61.718 1.00 29.93 ? 80  HIS I N   1 
ATOM   9618  C  CA  . HIS I  1 107 ? 56.069  55.673  -61.667 1.00 24.53 ? 80  HIS I CA  1 
ATOM   9619  C  C   . HIS I  1 107 ? 55.685  56.984  -62.342 1.00 23.54 ? 80  HIS I C   1 
ATOM   9620  O  O   . HIS I  1 107 ? 56.478  57.919  -62.421 1.00 30.60 ? 80  HIS I O   1 
ATOM   9621  C  CB  . HIS I  1 107 ? 55.576  55.670  -60.206 1.00 31.31 ? 80  HIS I CB  1 
ATOM   9622  C  CG  . HIS I  1 107 ? 55.949  54.437  -59.439 1.00 25.94 ? 80  HIS I CG  1 
ATOM   9623  N  ND1 . HIS I  1 107 ? 56.199  54.442  -58.087 1.00 28.28 ? 80  HIS I ND1 1 
ATOM   9624  C  CD2 . HIS I  1 107 ? 56.093  53.150  -59.841 1.00 31.40 ? 80  HIS I CD2 1 
ATOM   9625  C  CE1 . HIS I  1 107 ? 56.492  53.216  -57.687 1.00 26.62 ? 80  HIS I CE1 1 
ATOM   9626  N  NE2 . HIS I  1 107 ? 56.435  52.412  -58.735 1.00 31.65 ? 80  HIS I NE2 1 
ATOM   9627  N  N   . VAL I  1 108 ? 54.449  57.049  -62.842 1.00 24.36 ? 81  VAL I N   1 
ATOM   9628  C  CA  . VAL I  1 108 ? 53.952  58.319  -63.377 1.00 22.79 ? 81  VAL I CA  1 
ATOM   9629  C  C   . VAL I  1 108 ? 53.970  59.397  -62.292 1.00 24.07 ? 81  VAL I C   1 
ATOM   9630  O  O   . VAL I  1 108 ? 54.253  60.569  -62.565 1.00 24.87 ? 81  VAL I O   1 
ATOM   9631  C  CB  . VAL I  1 108 ? 52.540  58.143  -63.969 1.00 27.25 ? 81  VAL I CB  1 
ATOM   9632  C  CG1 . VAL I  1 108 ? 51.886  59.504  -64.239 1.00 30.12 ? 81  VAL I CG1 1 
ATOM   9633  C  CG2 . VAL I  1 108 ? 52.595  57.285  -65.263 1.00 31.78 ? 81  VAL I CG2 1 
ATOM   9634  N  N   . GLY I  1 109 ? 53.708  59.012  -61.044 1.00 26.69 ? 82  GLY I N   1 
ATOM   9635  C  CA  . GLY I  1 109 ? 53.660  59.981  -59.952 1.00 26.22 ? 82  GLY I CA  1 
ATOM   9636  C  C   . GLY I  1 109 ? 54.983  60.354  -59.320 1.00 29.31 ? 82  GLY I C   1 
ATOM   9637  O  O   . GLY I  1 109 ? 54.995  61.039  -58.289 1.00 26.57 ? 82  GLY I O   1 
ATOM   9638  N  N   . ASP I  1 110 ? 56.110  59.935  -59.904 1.00 23.61 ? 83  ASP I N   1 
ATOM   9639  C  CA  . ASP I  1 110 ? 57.426  60.102  -59.281 1.00 26.54 ? 83  ASP I CA  1 
ATOM   9640  C  C   . ASP I  1 110 ? 57.973  61.478  -59.646 1.00 30.99 ? 83  ASP I C   1 
ATOM   9641  O  O   . ASP I  1 110 ? 58.711  61.637  -60.615 1.00 27.07 ? 83  ASP I O   1 
ATOM   9642  C  CB  . ASP I  1 110 ? 58.373  58.997  -59.734 1.00 24.61 ? 83  ASP I CB  1 
ATOM   9643  C  CG  . ASP I  1 110 ? 58.089  57.675  -59.060 1.00 28.97 ? 83  ASP I CG  1 
ATOM   9644  O  OD1 . ASP I  1 110 ? 57.324  57.680  -58.076 1.00 30.66 ? 83  ASP I OD1 1 
ATOM   9645  O  OD2 . ASP I  1 110 ? 58.613  56.622  -59.516 1.00 24.45 ? 83  ASP I OD2 1 
ATOM   9646  N  N   . LEU I  1 111 ? 57.635  62.487  -58.839 1.00 25.16 ? 84  LEU I N   1 
ATOM   9647  C  CA  . LEU I  1 111 ? 58.139  63.833  -59.071 1.00 25.13 ? 84  LEU I CA  1 
ATOM   9648  C  C   . LEU I  1 111 ? 59.440  64.111  -58.320 1.00 28.63 ? 84  LEU I C   1 
ATOM   9649  O  O   . LEU I  1 111 ? 59.923  65.244  -58.336 1.00 32.91 ? 84  LEU I O   1 
ATOM   9650  C  CB  . LEU I  1 111 ? 57.064  64.870  -58.708 1.00 23.70 ? 84  LEU I CB  1 
ATOM   9651  C  CG  . LEU I  1 111 ? 55.756  64.776  -59.504 1.00 28.88 ? 84  LEU I CG  1 
ATOM   9652  C  CD1 . LEU I  1 111 ? 54.803  65.872  -59.067 1.00 26.81 ? 84  LEU I CD1 1 
ATOM   9653  C  CD2 . LEU I  1 111 ? 56.019  64.871  -61.019 1.00 31.36 ? 84  LEU I CD2 1 
ATOM   9654  N  N   . GLY I  1 112 ? 60.024  63.106  -57.679 1.00 23.59 ? 85  GLY I N   1 
ATOM   9655  C  CA  . GLY I  1 112 ? 61.308  63.282  -57.030 1.00 21.71 ? 85  GLY I CA  1 
ATOM   9656  C  C   . GLY I  1 112 ? 61.210  63.940  -55.671 1.00 27.28 ? 85  GLY I C   1 
ATOM   9657  O  O   . GLY I  1 112 ? 60.305  63.637  -54.894 1.00 24.82 ? 85  GLY I O   1 
ATOM   9658  N  N   . ASN I  1 113 ? 62.137  64.841  -55.370 1.00 24.61 ? 86  ASN I N   1 
ATOM   9659  C  CA  . ASN I  1 113 ? 62.173  65.520  -54.083 1.00 22.84 ? 86  ASN I CA  1 
ATOM   9660  C  C   . ASN I  1 113 ? 61.804  66.988  -54.244 1.00 25.99 ? 86  ASN I C   1 
ATOM   9661  O  O   . ASN I  1 113 ? 61.931  67.568  -55.328 1.00 21.89 ? 86  ASN I O   1 
ATOM   9662  C  CB  . ASN I  1 113 ? 63.558  65.439  -53.446 1.00 23.50 ? 86  ASN I CB  1 
ATOM   9663  C  CG  . ASN I  1 113 ? 63.860  64.082  -52.881 1.00 27.92 ? 86  ASN I CG  1 
ATOM   9664  O  OD1 . ASN I  1 113 ? 63.197  63.630  -51.941 1.00 23.68 ? 86  ASN I OD1 1 
ATOM   9665  N  ND2 . ASN I  1 113 ? 64.860  63.407  -53.453 1.00 26.56 ? 86  ASN I ND2 1 
ATOM   9666  N  N   . VAL I  1 114 ? 61.351  67.580  -53.141 1.00 24.23 ? 87  VAL I N   1 
ATOM   9667  C  CA  . VAL I  1 114 ? 61.343  69.028  -52.984 1.00 26.00 ? 87  VAL I CA  1 
ATOM   9668  C  C   . VAL I  1 114 ? 62.167  69.357  -51.748 1.00 26.34 ? 87  VAL I C   1 
ATOM   9669  O  O   . VAL I  1 114 ? 62.285  68.540  -50.829 1.00 29.39 ? 87  VAL I O   1 
ATOM   9670  C  CB  . VAL I  1 114 ? 59.912  69.610  -52.884 1.00 20.73 ? 87  VAL I CB  1 
ATOM   9671  C  CG1 . VAL I  1 114 ? 59.146  69.353  -54.173 1.00 22.46 ? 87  VAL I CG1 1 
ATOM   9672  C  CG2 . VAL I  1 114 ? 59.164  69.034  -51.682 1.00 23.31 ? 87  VAL I CG2 1 
ATOM   9673  N  N   . THR I  1 115 ? 62.751  70.553  -51.729 1.00 22.13 ? 88  THR I N   1 
ATOM   9674  C  CA  . THR I  1 115 ? 63.711  70.934  -50.699 1.00 25.44 ? 88  THR I CA  1 
ATOM   9675  C  C   . THR I  1 115 ? 63.159  72.078  -49.858 1.00 27.01 ? 88  THR I C   1 
ATOM   9676  O  O   . THR I  1 115 ? 62.735  73.102  -50.404 1.00 23.50 ? 88  THR I O   1 
ATOM   9677  C  CB  . THR I  1 115 ? 65.039  71.365  -51.326 1.00 29.77 ? 88  THR I CB  1 
ATOM   9678  O  OG1 . THR I  1 115 ? 65.644  70.252  -51.990 1.00 29.64 ? 88  THR I OG1 1 
ATOM   9679  C  CG2 . THR I  1 115 ? 65.988  71.874  -50.257 1.00 27.78 ? 88  THR I CG2 1 
ATOM   9680  N  N   . ALA I  1 116 ? 63.171  71.901  -48.540 1.00 26.86 ? 89  ALA I N   1 
ATOM   9681  C  CA  . ALA I  1 116 ? 62.780  72.952  -47.613 1.00 27.77 ? 89  ALA I CA  1 
ATOM   9682  C  C   . ALA I  1 116 ? 64.020  73.675  -47.104 1.00 32.11 ? 89  ALA I C   1 
ATOM   9683  O  O   . ALA I  1 116 ? 65.049  73.046  -46.825 1.00 30.69 ? 89  ALA I O   1 
ATOM   9684  C  CB  . ALA I  1 116 ? 61.988  72.375  -46.435 1.00 28.88 ? 89  ALA I CB  1 
ATOM   9685  N  N   . ASP I  1 117 ? 63.917  75.000  -46.986 1.00 29.16 ? 90  ASP I N   1 
ATOM   9686  C  CA  . ASP I  1 117 ? 65.031  75.818  -46.521 1.00 33.10 ? 90  ASP I CA  1 
ATOM   9687  C  C   . ASP I  1 117 ? 65.095  75.795  -44.994 1.00 36.90 ? 90  ASP I C   1 
ATOM   9688  O  O   . ASP I  1 117 ? 64.371  75.048  -44.327 1.00 28.80 ? 90  ASP I O   1 
ATOM   9689  C  CB  . ASP I  1 117 ? 64.914  77.240  -47.067 1.00 32.29 ? 90  ASP I CB  1 
ATOM   9690  C  CG  . ASP I  1 117 ? 63.659  77.969  -46.589 1.00 35.15 ? 90  ASP I CG  1 
ATOM   9691  O  OD1 . ASP I  1 117 ? 63.046  77.588  -45.561 1.00 31.24 ? 90  ASP I OD1 1 
ATOM   9692  O  OD2 . ASP I  1 117 ? 63.293  78.959  -47.246 1.00 37.21 ? 90  ASP I OD2 1 
ATOM   9693  N  N   . LYS I  1 118 ? 65.952  76.659  -44.426 1.00 42.41 ? 91  LYS I N   1 
ATOM   9694  C  CA  . LYS I  1 118 ? 66.185  76.686  -42.983 1.00 36.42 ? 91  LYS I CA  1 
ATOM   9695  C  C   . LYS I  1 118 ? 64.933  77.065  -42.199 1.00 36.77 ? 91  LYS I C   1 
ATOM   9696  O  O   . LYS I  1 118 ? 64.827  76.732  -41.012 1.00 38.53 ? 91  LYS I O   1 
ATOM   9697  C  CB  . LYS I  1 118 ? 67.300  77.681  -42.635 1.00 43.87 ? 91  LYS I CB  1 
ATOM   9698  C  CG  . LYS I  1 118 ? 66.977  79.134  -43.028 1.00 47.12 ? 91  LYS I CG  1 
ATOM   9699  C  CD  . LYS I  1 118 ? 68.048  80.128  -42.543 1.00 51.76 ? 91  LYS I CD  1 
ATOM   9700  C  CE  . LYS I  1 118 ? 68.880  80.690  -43.700 1.00 54.14 ? 91  LYS I CE  1 
ATOM   9701  N  NZ  . LYS I  1 118 ? 69.629  81.934  -43.317 1.00 59.66 ? 91  LYS I NZ  1 
ATOM   9702  N  N   . ASP I  1 119 ? 64.007  77.784  -42.824 1.00 35.47 ? 92  ASP I N   1 
ATOM   9703  C  CA  . ASP I  1 119 ? 62.737  78.171  -42.229 1.00 33.74 ? 92  ASP I CA  1 
ATOM   9704  C  C   . ASP I  1 119 ? 61.654  77.130  -42.412 1.00 37.52 ? 92  ASP I C   1 
ATOM   9705  O  O   . ASP I  1 119 ? 60.514  77.375  -42.005 1.00 34.30 ? 92  ASP I O   1 
ATOM   9706  C  CB  . ASP I  1 119 ? 62.268  79.484  -42.835 1.00 34.83 ? 92  ASP I CB  1 
ATOM   9707  C  CG  . ASP I  1 119 ? 63.201  80.620  -42.519 1.00 47.31 ? 92  ASP I CG  1 
ATOM   9708  O  OD1 . ASP I  1 119 ? 63.831  80.576  -41.432 1.00 47.87 ? 92  ASP I OD1 1 
ATOM   9709  O  OD2 . ASP I  1 119 ? 63.295  81.552  -43.351 1.00 48.09 ? 92  ASP I OD2 1 
ATOM   9710  N  N   . GLY I  1 120 ? 61.971  75.990  -43.026 1.00 35.88 ? 93  GLY I N   1 
ATOM   9711  C  CA  . GLY I  1 120 ? 60.972  74.961  -43.226 1.00 32.31 ? 93  GLY I CA  1 
ATOM   9712  C  C   . GLY I  1 120 ? 60.067  75.166  -44.415 1.00 25.94 ? 93  GLY I C   1 
ATOM   9713  O  O   . GLY I  1 120 ? 59.016  74.526  -44.495 1.00 26.25 ? 93  GLY I O   1 
ATOM   9714  N  N   . VAL I  1 121 ? 60.454  76.018  -45.361 1.00 25.77 ? 94  VAL I N   1 
ATOM   9715  C  CA  . VAL I  1 121 ? 59.625  76.363  -46.508 1.00 29.65 ? 94  VAL I CA  1 
ATOM   9716  C  C   . VAL I  1 121 ? 60.224  75.746  -47.764 1.00 26.79 ? 94  VAL I C   1 
ATOM   9717  O  O   . VAL I  1 121 ? 61.403  75.965  -48.071 1.00 28.61 ? 94  VAL I O   1 
ATOM   9718  C  CB  . VAL I  1 121 ? 59.506  77.886  -46.673 1.00 32.48 ? 94  VAL I CB  1 
ATOM   9719  C  CG1 . VAL I  1 121 ? 58.857  78.206  -48.013 1.00 24.72 ? 94  VAL I CG1 1 
ATOM   9720  C  CG2 . VAL I  1 121 ? 58.697  78.474  -45.532 1.00 28.17 ? 94  VAL I CG2 1 
ATOM   9721  N  N   . ALA I  1 122 ? 59.415  74.988  -48.490 1.00 28.35 ? 95  ALA I N   1 
ATOM   9722  C  CA  . ALA I  1 122 ? 59.788  74.481  -49.804 1.00 23.56 ? 95  ALA I CA  1 
ATOM   9723  C  C   . ALA I  1 122 ? 59.125  75.368  -50.850 1.00 26.59 ? 95  ALA I C   1 
ATOM   9724  O  O   . ALA I  1 122 ? 57.895  75.393  -50.963 1.00 29.35 ? 95  ALA I O   1 
ATOM   9725  C  CB  . ALA I  1 122 ? 59.360  73.021  -49.975 1.00 24.62 ? 95  ALA I CB  1 
ATOM   9726  N  N   . ASP I  1 123 ? 59.936  76.105  -51.607 1.00 27.69 ? 96  ASP I N   1 
ATOM   9727  C  CA  . ASP I  1 123 ? 59.433  76.903  -52.729 1.00 32.18 ? 96  ASP I CA  1 
ATOM   9728  C  C   . ASP I  1 123 ? 59.544  76.028  -53.972 1.00 28.42 ? 96  ASP I C   1 
ATOM   9729  O  O   . ASP I  1 123 ? 60.553  76.035  -54.675 1.00 29.42 ? 96  ASP I O   1 
ATOM   9730  C  CB  . ASP I  1 123 ? 60.211  78.207  -52.858 1.00 32.14 ? 96  ASP I CB  1 
ATOM   9731  C  CG  . ASP I  1 123 ? 59.773  79.265  -51.827 1.00 50.19 ? 96  ASP I CG  1 
ATOM   9732  O  OD1 . ASP I  1 123 ? 58.579  79.292  -51.425 1.00 44.36 ? 96  ASP I OD1 1 
ATOM   9733  O  OD2 . ASP I  1 123 ? 60.645  80.052  -51.384 1.00 48.39 ? 96  ASP I OD2 1 
ATOM   9734  N  N   . VAL I  1 124 ? 58.479  75.266  -54.237 1.00 28.38 ? 97  VAL I N   1 
ATOM   9735  C  CA  . VAL I  1 124 ? 58.504  74.194  -55.230 1.00 25.40 ? 97  VAL I CA  1 
ATOM   9736  C  C   . VAL I  1 124 ? 58.555  74.768  -56.636 1.00 29.97 ? 97  VAL I C   1 
ATOM   9737  O  O   . VAL I  1 124 ? 57.769  75.654  -56.992 1.00 25.82 ? 97  VAL I O   1 
ATOM   9738  C  CB  . VAL I  1 124 ? 57.273  73.291  -55.060 1.00 30.02 ? 97  VAL I CB  1 
ATOM   9739  C  CG1 . VAL I  1 124 ? 57.281  72.194  -56.087 1.00 24.75 ? 97  VAL I CG1 1 
ATOM   9740  C  CG2 . VAL I  1 124 ? 57.251  72.698  -53.637 1.00 22.50 ? 97  VAL I CG2 1 
ATOM   9741  N  N   . SER I  1 125 ? 59.452  74.232  -57.458 1.00 29.88 ? 98  SER I N   1 
ATOM   9742  C  CA  . SER I  1 125 ? 59.506  74.615  -58.865 1.00 30.69 ? 98  SER I CA  1 
ATOM   9743  C  C   . SER I  1 125 ? 60.011  73.410  -59.648 1.00 33.16 ? 98  SER I C   1 
ATOM   9744  O  O   . SER I  1 125 ? 61.199  73.076  -59.594 1.00 29.70 ? 98  SER I O   1 
ATOM   9745  C  CB  . SER I  1 125 ? 60.395  75.834  -59.078 1.00 34.94 ? 98  SER I CB  1 
ATOM   9746  O  OG  . SER I  1 125 ? 60.839  75.892  -60.424 1.00 49.68 ? 98  SER I OG  1 
ATOM   9747  N  N   . ILE I  1 126 ? 59.099  72.761  -60.365 1.00 25.99 ? 99  ILE I N   1 
ATOM   9748  C  CA  . ILE I  1 126 ? 59.351  71.487  -61.020 1.00 27.54 ? 99  ILE I CA  1 
ATOM   9749  C  C   . ILE I  1 126 ? 58.713  71.549  -62.397 1.00 30.01 ? 99  ILE I C   1 
ATOM   9750  O  O   . ILE I  1 126 ? 57.706  72.230  -62.602 1.00 31.43 ? 99  ILE I O   1 
ATOM   9751  C  CB  . ILE I  1 126 ? 58.778  70.312  -60.180 1.00 30.96 ? 99  ILE I CB  1 
ATOM   9752  C  CG1 . ILE I  1 126 ? 59.733  69.934  -59.049 1.00 30.70 ? 99  ILE I CG1 1 
ATOM   9753  C  CG2 . ILE I  1 126 ? 58.454  69.087  -61.013 1.00 30.95 ? 99  ILE I CG2 1 
ATOM   9754  C  CD1 . ILE I  1 126 ? 59.022  69.237  -57.895 1.00 35.55 ? 99  ILE I CD1 1 
ATOM   9755  N  N   . GLU I  1 127 ? 59.305  70.850  -63.354 1.00 28.91 ? 100 GLU I N   1 
ATOM   9756  C  CA  . GLU I  1 127 ? 58.649  70.660  -64.640 1.00 30.40 ? 100 GLU I CA  1 
ATOM   9757  C  C   . GLU I  1 127 ? 58.753  69.187  -64.999 1.00 31.46 ? 100 GLU I C   1 
ATOM   9758  O  O   . GLU I  1 127 ? 59.826  68.591  -64.861 1.00 36.47 ? 100 GLU I O   1 
ATOM   9759  C  CB  . GLU I  1 127 ? 59.267  71.562  -65.710 1.00 33.04 ? 100 GLU I CB  1 
ATOM   9760  C  CG  . GLU I  1 127 ? 58.867  71.201  -67.135 1.00 45.37 ? 100 GLU I CG  1 
ATOM   9761  C  CD  . GLU I  1 127 ? 59.827  71.773  -68.179 1.00 65.23 ? 100 GLU I CD  1 
ATOM   9762  O  OE1 . GLU I  1 127 ? 60.130  72.987  -68.106 1.00 69.78 ? 100 GLU I OE1 1 
ATOM   9763  O  OE2 . GLU I  1 127 ? 60.254  71.018  -69.083 1.00 61.16 ? 100 GLU I OE2 1 
ATOM   9764  N  N   . ASP I  1 128 ? 57.636  68.587  -65.406 1.00 30.85 ? 101 ASP I N   1 
ATOM   9765  C  CA  . ASP I  1 128 ? 57.610  67.151  -65.650 1.00 30.80 ? 101 ASP I CA  1 
ATOM   9766  C  C   . ASP I  1 128 ? 56.785  66.857  -66.893 1.00 32.61 ? 101 ASP I C   1 
ATOM   9767  O  O   . ASP I  1 128 ? 55.728  67.464  -67.102 1.00 33.37 ? 101 ASP I O   1 
ATOM   9768  C  CB  . ASP I  1 128 ? 57.023  66.379  -64.453 1.00 33.11 ? 101 ASP I CB  1 
ATOM   9769  C  CG  . ASP I  1 128 ? 57.286  64.876  -64.542 1.00 36.58 ? 101 ASP I CG  1 
ATOM   9770  O  OD1 . ASP I  1 128 ? 58.456  64.463  -64.374 1.00 40.29 ? 101 ASP I OD1 1 
ATOM   9771  O  OD2 . ASP I  1 128 ? 56.335  64.111  -64.798 1.00 33.12 ? 101 ASP I OD2 1 
ATOM   9772  N  N   A SER I  1 129 ? 57.259  65.917  -67.710 0.47 34.64 ? 102 SER I N   1 
ATOM   9773  N  N   B SER I  1 129 ? 57.273  65.919  -67.712 0.53 34.67 ? 102 SER I N   1 
ATOM   9774  C  CA  A SER I  1 129 ? 56.592  65.586  -68.960 0.47 37.37 ? 102 SER I CA  1 
ATOM   9775  C  CA  B SER I  1 129 ? 56.636  65.564  -68.974 0.53 37.37 ? 102 SER I CA  1 
ATOM   9776  C  C   A SER I  1 129 ? 55.862  64.252  -68.912 0.47 35.19 ? 102 SER I C   1 
ATOM   9777  C  C   B SER I  1 129 ? 55.908  64.228  -68.927 0.53 35.18 ? 102 SER I C   1 
ATOM   9778  O  O   A SER I  1 129 ? 55.228  63.875  -69.901 0.47 36.23 ? 102 SER I O   1 
ATOM   9779  O  O   B SER I  1 129 ? 55.322  63.824  -69.935 0.53 36.80 ? 102 SER I O   1 
ATOM   9780  C  CB  A SER I  1 129 ? 57.602  65.589  -70.116 0.47 36.61 ? 102 SER I CB  1 
ATOM   9781  C  CB  B SER I  1 129 ? 57.672  65.541  -70.110 0.53 36.72 ? 102 SER I CB  1 
ATOM   9782  O  OG  A SER I  1 129 ? 58.315  66.816  -70.146 0.47 36.83 ? 102 SER I OG  1 
ATOM   9783  O  OG  B SER I  1 129 ? 58.772  64.706  -69.784 0.53 37.79 ? 102 SER I OG  1 
ATOM   9784  N  N   . VAL I  1 130 ? 55.918  63.537  -67.794 1.00 31.99 ? 103 VAL I N   1 
ATOM   9785  C  CA  . VAL I  1 130 ? 55.231  62.255  -67.689 1.00 30.64 ? 103 VAL I CA  1 
ATOM   9786  C  C   . VAL I  1 130 ? 53.823  62.424  -67.126 1.00 37.19 ? 103 VAL I C   1 
ATOM   9787  O  O   . VAL I  1 130 ? 52.857  61.895  -67.681 1.00 32.39 ? 103 VAL I O   1 
ATOM   9788  C  CB  . VAL I  1 130 ? 56.071  61.275  -66.851 1.00 31.99 ? 103 VAL I CB  1 
ATOM   9789  C  CG1 . VAL I  1 130 ? 55.347  59.943  -66.739 1.00 30.89 ? 103 VAL I CG1 1 
ATOM   9790  C  CG2 . VAL I  1 130 ? 57.450  61.099  -67.493 1.00 36.17 ? 103 VAL I CG2 1 
ATOM   9791  N  N   . ILE I  1 131 ? 53.681  63.159  -66.014 1.00 34.21 ? 104 ILE I N   1 
ATOM   9792  C  CA  . ILE I  1 131 ? 52.348  63.523  -65.545 1.00 27.88 ? 104 ILE I CA  1 
ATOM   9793  C  C   . ILE I  1 131 ? 51.679  64.421  -66.578 1.00 33.74 ? 104 ILE I C   1 
ATOM   9794  O  O   . ILE I  1 131 ? 52.337  65.083  -67.394 1.00 33.19 ? 104 ILE I O   1 
ATOM   9795  C  CB  . ILE I  1 131 ? 52.399  64.235  -64.184 1.00 28.19 ? 104 ILE I CB  1 
ATOM   9796  C  CG1 . ILE I  1 131 ? 53.210  65.527  -64.308 1.00 26.40 ? 104 ILE I CG1 1 
ATOM   9797  C  CG2 . ILE I  1 131 ? 52.984  63.328  -63.153 1.00 26.72 ? 104 ILE I CG2 1 
ATOM   9798  C  CD1 . ILE I  1 131 ? 53.070  66.510  -63.111 1.00 24.79 ? 104 ILE I CD1 1 
ATOM   9799  N  N   . SER I  1 132 ? 50.352  64.471  -66.516 1.00 25.20 ? 105 SER I N   1 
ATOM   9800  C  CA  . SER I  1 132 ? 49.606  65.314  -67.435 1.00 27.60 ? 105 SER I CA  1 
ATOM   9801  C  C   . SER I  1 132 ? 48.326  65.768  -66.745 1.00 30.45 ? 105 SER I C   1 
ATOM   9802  O  O   . SER I  1 132 ? 47.905  65.192  -65.734 1.00 30.07 ? 105 SER I O   1 
ATOM   9803  C  CB  . SER I  1 132 ? 49.331  64.553  -68.749 1.00 38.58 ? 105 SER I CB  1 
ATOM   9804  O  OG  . SER I  1 132 ? 48.407  65.230  -69.583 1.00 37.46 ? 105 SER I OG  1 
ATOM   9805  N  N   . LEU I  1 133 ? 47.728  66.836  -67.271 1.00 28.94 ? 106 LEU I N   1 
ATOM   9806  C  CA  . LEU I  1 133 ? 46.434  67.305  -66.785 1.00 28.64 ? 106 LEU I CA  1 
ATOM   9807  C  C   . LEU I  1 133 ? 45.293  66.881  -67.698 1.00 36.26 ? 106 LEU I C   1 
ATOM   9808  O  O   . LEU I  1 133 ? 44.169  67.361  -67.539 1.00 33.75 ? 106 LEU I O   1 
ATOM   9809  C  CB  . LEU I  1 133 ? 46.445  68.823  -66.618 1.00 27.30 ? 106 LEU I CB  1 
ATOM   9810  C  CG  . LEU I  1 133 ? 47.543  69.371  -65.704 1.00 30.54 ? 106 LEU I CG  1 
ATOM   9811  C  CD1 . LEU I  1 133 ? 47.401  70.864  -65.536 1.00 28.78 ? 106 LEU I CD1 1 
ATOM   9812  C  CD2 . LEU I  1 133 ? 47.503  68.672  -64.332 1.00 26.85 ? 106 LEU I CD2 1 
ATOM   9813  N  N   . SER I  1 134 ? 45.567  66.003  -68.656 1.00 34.24 ? 107 SER I N   1 
ATOM   9814  C  CA  . SER I  1 134 ? 44.548  65.399  -69.499 1.00 38.20 ? 107 SER I CA  1 
ATOM   9815  C  C   . SER I  1 134 ? 45.092  64.057  -69.966 1.00 41.86 ? 107 SER I C   1 
ATOM   9816  O  O   . SER I  1 134 ? 46.288  63.772  -69.842 1.00 42.40 ? 107 SER I O   1 
ATOM   9817  C  CB  . SER I  1 134 ? 44.181  66.300  -70.692 1.00 37.64 ? 107 SER I CB  1 
ATOM   9818  O  OG  . SER I  1 134 ? 45.298  66.536  -71.548 1.00 41.02 ? 107 SER I OG  1 
ATOM   9819  N  N   . GLY I  1 135 ? 44.199  63.218  -70.479 1.00 41.32 ? 108 GLY I N   1 
ATOM   9820  C  CA  . GLY I  1 135 ? 44.641  61.980  -71.087 1.00 42.65 ? 108 GLY I CA  1 
ATOM   9821  C  C   . GLY I  1 135 ? 44.946  60.885  -70.082 1.00 45.24 ? 108 GLY I C   1 
ATOM   9822  O  O   . GLY I  1 135 ? 44.534  60.932  -68.917 1.00 40.57 ? 108 GLY I O   1 
ATOM   9823  N  N   . ASP I  1 136 ? 45.707  59.883  -70.555 1.00 38.02 ? 109 ASP I N   1 
ATOM   9824  C  CA  . ASP I  1 136 ? 45.895  58.644  -69.797 1.00 41.36 ? 109 ASP I CA  1 
ATOM   9825  C  C   . ASP I  1 136 ? 46.614  58.881  -68.480 1.00 43.49 ? 109 ASP I C   1 
ATOM   9826  O  O   . ASP I  1 136 ? 46.296  58.245  -67.467 1.00 48.65 ? 109 ASP I O   1 
ATOM   9827  C  CB  . ASP I  1 136 ? 46.696  57.630  -70.607 1.00 47.48 ? 109 ASP I CB  1 
ATOM   9828  C  CG  . ASP I  1 136 ? 46.153  57.437  -72.000 1.00 55.53 ? 109 ASP I CG  1 
ATOM   9829  O  OD1 . ASP I  1 136 ? 46.346  58.343  -72.840 1.00 55.17 ? 109 ASP I OD1 1 
ATOM   9830  O  OD2 . ASP I  1 136 ? 45.566  56.362  -72.253 1.00 53.91 ? 109 ASP I OD2 1 
ATOM   9831  N  N   . HIS I  1 137 ? 47.629  59.739  -68.490 1.00 33.15 ? 110 HIS I N   1 
ATOM   9832  C  CA  . HIS I  1 137 ? 48.424  60.014  -67.303 1.00 41.01 ? 110 HIS I CA  1 
ATOM   9833  C  C   . HIS I  1 137 ? 47.893  61.201  -66.507 1.00 32.57 ? 110 HIS I C   1 
ATOM   9834  O  O   . HIS I  1 137 ? 48.672  61.879  -65.826 1.00 31.00 ? 110 HIS I O   1 
ATOM   9835  C  CB  . HIS I  1 137 ? 49.883  60.247  -67.698 1.00 39.38 ? 110 HIS I CB  1 
ATOM   9836  C  CG  . HIS I  1 137 ? 50.559  59.033  -68.253 1.00 38.28 ? 110 HIS I CG  1 
ATOM   9837  N  ND1 . HIS I  1 137 ? 51.862  59.051  -68.705 1.00 38.27 ? 110 HIS I ND1 1 
ATOM   9838  C  CD2 . HIS I  1 137 ? 50.123  57.759  -68.406 1.00 34.16 ? 110 HIS I CD2 1 
ATOM   9839  C  CE1 . HIS I  1 137 ? 52.198  57.841  -69.116 1.00 41.66 ? 110 HIS I CE1 1 
ATOM   9840  N  NE2 . HIS I  1 137 ? 51.160  57.038  -68.945 1.00 40.21 ? 110 HIS I NE2 1 
ATOM   9841  N  N   . CYS I  1 138 ? 46.597  61.483  -66.614 1.00 33.52 ? 111 CYS I N   1 
ATOM   9842  C  CA  . CYS I  1 138 ? 45.999  62.607  -65.912 1.00 35.52 ? 111 CYS I CA  1 
ATOM   9843  C  C   . CYS I  1 138 ? 46.093  62.398  -64.402 1.00 25.10 ? 111 CYS I C   1 
ATOM   9844  O  O   . CYS I  1 138 ? 45.766  61.321  -63.890 1.00 28.57 ? 111 CYS I O   1 
ATOM   9845  C  CB  . CYS I  1 138 ? 44.539  62.753  -66.329 1.00 32.60 ? 111 CYS I CB  1 
ATOM   9846  S  SG  . CYS I  1 138 ? 43.766  64.239  -65.745 1.00 38.01 ? 111 CYS I SG  1 
ATOM   9847  N  N   . ILE I  1 139 ? 46.534  63.438  -63.687 1.00 29.78 ? 112 ILE I N   1 
ATOM   9848  C  CA  . ILE I  1 139 ? 46.608  63.378  -62.227 1.00 25.74 ? 112 ILE I CA  1 
ATOM   9849  C  C   . ILE I  1 139 ? 45.460  64.111  -61.553 1.00 29.22 ? 112 ILE I C   1 
ATOM   9850  O  O   . ILE I  1 139 ? 45.440  64.195  -60.319 1.00 27.59 ? 112 ILE I O   1 
ATOM   9851  C  CB  . ILE I  1 139 ? 47.952  63.927  -61.721 1.00 25.00 ? 112 ILE I CB  1 
ATOM   9852  C  CG1 . ILE I  1 139 ? 48.133  65.380  -62.164 1.00 21.99 ? 112 ILE I CG1 1 
ATOM   9853  C  CG2 . ILE I  1 139 ? 49.097  63.051  -62.221 1.00 26.33 ? 112 ILE I CG2 1 
ATOM   9854  C  CD1 . ILE I  1 139 ? 49.453  65.979  -61.719 1.00 23.82 ? 112 ILE I CD1 1 
ATOM   9855  N  N   . ILE I  1 140 ? 44.508  64.648  -62.322 1.00 29.53 ? 113 ILE I N   1 
ATOM   9856  C  CA  . ILE I  1 140 ? 43.337  65.294  -61.738 1.00 29.80 ? 113 ILE I CA  1 
ATOM   9857  C  C   . ILE I  1 140 ? 42.515  64.263  -60.994 1.00 31.96 ? 113 ILE I C   1 
ATOM   9858  O  O   . ILE I  1 140 ? 42.204  63.193  -61.529 1.00 28.37 ? 113 ILE I O   1 
ATOM   9859  C  CB  . ILE I  1 140 ? 42.489  65.959  -62.832 1.00 31.83 ? 113 ILE I CB  1 
ATOM   9860  C  CG1 . ILE I  1 140 ? 43.336  66.924  -63.644 1.00 34.42 ? 113 ILE I CG1 1 
ATOM   9861  C  CG2 . ILE I  1 140 ? 41.252  66.634  -62.225 1.00 27.46 ? 113 ILE I CG2 1 
ATOM   9862  C  CD1 . ILE I  1 140 ? 43.479  68.237  -63.022 1.00 31.80 ? 113 ILE I CD1 1 
ATOM   9863  N  N   . GLY I  1 141 ? 42.124  64.584  -59.765 1.00 29.33 ? 114 GLY I N   1 
ATOM   9864  C  CA  . GLY I  1 141 ? 41.398  63.601  -58.993 1.00 23.47 ? 114 GLY I CA  1 
ATOM   9865  C  C   . GLY I  1 141 ? 42.274  62.592  -58.301 1.00 23.91 ? 114 GLY I C   1 
ATOM   9866  O  O   . GLY I  1 141 ? 41.753  61.655  -57.686 1.00 27.01 ? 114 GLY I O   1 
ATOM   9867  N  N   . ARG I  1 142 ? 43.588  62.749  -58.372 1.00 20.07 ? 115 ARG I N   1 
ATOM   9868  C  CA  . ARG I  1 142 ? 44.493  61.936  -57.581 1.00 23.74 ? 115 ARG I CA  1 
ATOM   9869  C  C   . ARG I  1 142 ? 45.051  62.789  -56.443 1.00 22.70 ? 115 ARG I C   1 
ATOM   9870  O  O   . ARG I  1 142 ? 44.680  63.945  -56.273 1.00 23.61 ? 115 ARG I O   1 
ATOM   9871  C  CB  . ARG I  1 142 ? 45.580  61.340  -58.470 1.00 23.28 ? 115 ARG I CB  1 
ATOM   9872  C  CG  . ARG I  1 142 ? 44.920  60.639  -59.683 1.00 31.37 ? 115 ARG I CG  1 
ATOM   9873  C  CD  . ARG I  1 142 ? 45.828  59.651  -60.392 1.00 34.56 ? 115 ARG I CD  1 
ATOM   9874  N  NE  . ARG I  1 142 ? 45.162  59.089  -61.562 1.00 32.16 ? 115 ARG I NE  1 
ATOM   9875  C  CZ  . ARG I  1 142 ? 44.463  57.959  -61.573 1.00 35.08 ? 115 ARG I CZ  1 
ATOM   9876  N  NH1 . ARG I  1 142 ? 44.354  57.198  -60.496 1.00 29.75 ? 115 ARG I NH1 1 
ATOM   9877  N  NH2 . ARG I  1 142 ? 43.880  57.569  -62.704 1.00 36.43 ? 115 ARG I NH2 1 
ATOM   9878  N  N   . THR I  1 143 ? 45.946  62.202  -55.665 1.00 23.65 ? 116 THR I N   1 
ATOM   9879  C  CA  . THR I  1 143 ? 46.422  62.824  -54.437 1.00 24.26 ? 116 THR I CA  1 
ATOM   9880  C  C   . THR I  1 143 ? 47.899  63.146  -54.565 1.00 22.51 ? 116 THR I C   1 
ATOM   9881  O  O   . THR I  1 143 ? 48.704  62.273  -54.906 1.00 28.05 ? 116 THR I O   1 
ATOM   9882  C  CB  . THR I  1 143 ? 46.179  61.919  -53.225 1.00 25.46 ? 116 THR I CB  1 
ATOM   9883  O  OG1 . THR I  1 143 ? 44.766  61.771  -53.012 1.00 25.19 ? 116 THR I OG1 1 
ATOM   9884  C  CG2 . THR I  1 143 ? 46.811  62.532  -51.973 1.00 22.37 ? 116 THR I CG2 1 
ATOM   9885  N  N   . LEU I  1 144 ? 48.245  64.403  -54.301 1.00 20.65 ? 117 LEU I N   1 
ATOM   9886  C  CA  . LEU I  1 144 ? 49.633  64.821  -54.142 1.00 18.43 ? 117 LEU I CA  1 
ATOM   9887  C  C   . LEU I  1 144 ? 50.034  64.684  -52.678 1.00 25.04 ? 117 LEU I C   1 
ATOM   9888  O  O   . LEU I  1 144 ? 49.296  65.130  -51.795 1.00 19.59 ? 117 LEU I O   1 
ATOM   9889  C  CB  . LEU I  1 144 ? 49.793  66.274  -54.593 1.00 19.90 ? 117 LEU I CB  1 
ATOM   9890  C  CG  . LEU I  1 144 ? 51.194  66.886  -54.515 1.00 22.75 ? 117 LEU I CG  1 
ATOM   9891  C  CD1 . LEU I  1 144 ? 52.141  66.199  -55.509 1.00 22.09 ? 117 LEU I CD1 1 
ATOM   9892  C  CD2 . LEU I  1 144 ? 51.106  68.386  -54.777 1.00 19.48 ? 117 LEU I CD2 1 
ATOM   9893  N  N   . VAL I  1 145 ? 51.192  64.078  -52.417 1.00 20.71 ? 118 VAL I N   1 
ATOM   9894  C  CA  . VAL I  1 145 ? 51.653  63.833  -51.046 1.00 19.83 ? 118 VAL I CA  1 
ATOM   9895  C  C   . VAL I  1 145 ? 53.076  64.350  -50.890 1.00 22.79 ? 118 VAL I C   1 
ATOM   9896  O  O   . VAL I  1 145 ? 53.935  64.081  -51.737 1.00 23.38 ? 118 VAL I O   1 
ATOM   9897  C  CB  . VAL I  1 145 ? 51.599  62.332  -50.684 1.00 22.19 ? 118 VAL I CB  1 
ATOM   9898  C  CG1 . VAL I  1 145 ? 52.167  62.090  -49.263 1.00 26.55 ? 118 VAL I CG1 1 
ATOM   9899  C  CG2 . VAL I  1 145 ? 50.178  61.802  -50.781 1.00 25.86 ? 118 VAL I CG2 1 
ATOM   9900  N  N   . VAL I  1 146 ? 53.350  65.067  -49.795 1.00 21.40 ? 119 VAL I N   1 
ATOM   9901  C  CA  . VAL I  1 146 ? 54.720  65.414  -49.430 1.00 17.33 ? 119 VAL I CA  1 
ATOM   9902  C  C   . VAL I  1 146 ? 55.117  64.519  -48.263 1.00 20.70 ? 119 VAL I C   1 
ATOM   9903  O  O   . VAL I  1 146 ? 54.334  64.331  -47.322 1.00 23.10 ? 119 VAL I O   1 
ATOM   9904  C  CB  . VAL I  1 146 ? 54.887  66.912  -49.102 1.00 21.07 ? 119 VAL I CB  1 
ATOM   9905  C  CG1 . VAL I  1 146 ? 54.086  67.316  -47.825 1.00 19.55 ? 119 VAL I CG1 1 
ATOM   9906  C  CG2 . VAL I  1 146 ? 56.365  67.245  -48.938 1.00 18.71 ? 119 VAL I CG2 1 
ATOM   9907  N  N   . HIS I  1 147 ? 56.304  63.917  -48.354 1.00 20.06 ? 120 HIS I N   1 
ATOM   9908  C  CA  . HIS I  1 147 ? 56.725  62.874  -47.421 1.00 23.89 ? 120 HIS I CA  1 
ATOM   9909  C  C   . HIS I  1 147 ? 57.760  63.367  -46.414 1.00 20.21 ? 120 HIS I C   1 
ATOM   9910  O  O   . HIS I  1 147 ? 58.400  64.412  -46.572 1.00 23.90 ? 120 HIS I O   1 
ATOM   9911  C  CB  . HIS I  1 147 ? 57.292  61.639  -48.162 1.00 18.44 ? 120 HIS I CB  1 
ATOM   9912  C  CG  . HIS I  1 147 ? 56.265  60.866  -48.926 1.00 24.00 ? 120 HIS I CG  1 
ATOM   9913  N  ND1 . HIS I  1 147 ? 55.706  59.707  -48.440 1.00 23.67 ? 120 HIS I ND1 1 
ATOM   9914  C  CD2 . HIS I  1 147 ? 55.711  61.065  -50.145 1.00 24.41 ? 120 HIS I CD2 1 
ATOM   9915  C  CE1 . HIS I  1 147 ? 54.826  59.241  -49.310 1.00 20.92 ? 120 HIS I CE1 1 
ATOM   9916  N  NE2 . HIS I  1 147 ? 54.815  60.044  -50.359 1.00 21.00 ? 120 HIS I NE2 1 
ATOM   9917  N  N   . GLU I  1 148 ? 57.965  62.507  -45.414 1.00 26.70 ? 121 GLU I N   1 
ATOM   9918  C  CA  . GLU I  1 148 ? 58.763  62.818  -44.233 1.00 23.48 ? 121 GLU I CA  1 
ATOM   9919  C  C   . GLU I  1 148 ? 60.245  62.923  -44.563 1.00 29.95 ? 121 GLU I C   1 
ATOM   9920  O  O   . GLU I  1 148 ? 60.940  63.796  -44.024 1.00 26.01 ? 121 GLU I O   1 
ATOM   9921  C  CB  . GLU I  1 148 ? 58.502  61.731  -43.181 1.00 23.57 ? 121 GLU I CB  1 
ATOM   9922  C  CG  . GLU I  1 148 ? 59.416  61.725  -41.984 1.00 32.31 ? 121 GLU I CG  1 
ATOM   9923  C  CD  . GLU I  1 148 ? 59.464  60.353  -41.294 1.00 50.54 ? 121 GLU I CD  1 
ATOM   9924  O  OE1 . GLU I  1 148 ? 59.048  59.337  -41.911 1.00 45.49 ? 121 GLU I OE1 1 
ATOM   9925  O  OE2 . GLU I  1 148 ? 59.922  60.292  -40.131 1.00 52.34 ? 121 GLU I OE2 1 
ATOM   9926  N  N   . LYS I  1 149 ? 60.750  62.048  -45.447 1.00 24.65 ? 122 LYS I N   1 
ATOM   9927  C  CA  . LYS I  1 149 ? 62.181  61.928  -45.700 1.00 28.45 ? 122 LYS I CA  1 
ATOM   9928  C  C   . LYS I  1 149 ? 62.475  62.048  -47.190 1.00 27.86 ? 122 LYS I C   1 
ATOM   9929  O  O   . LYS I  1 149 ? 61.575  62.070  -48.036 1.00 23.47 ? 122 LYS I O   1 
ATOM   9930  C  CB  . LYS I  1 149 ? 62.753  60.590  -45.187 1.00 30.05 ? 122 LYS I CB  1 
ATOM   9931  C  CG  . LYS I  1 149 ? 62.560  60.306  -43.700 1.00 41.54 ? 122 LYS I CG  1 
ATOM   9932  C  CD  . LYS I  1 149 ? 62.087  58.885  -43.501 1.00 41.29 ? 122 LYS I CD  1 
ATOM   9933  C  CE  . LYS I  1 149 ? 63.236  57.921  -43.758 1.00 51.72 ? 122 LYS I CE  1 
ATOM   9934  N  NZ  . LYS I  1 149 ? 62.771  56.542  -44.123 1.00 56.10 ? 122 LYS I NZ  1 
ATOM   9935  N  N   . ALA I  1 150 ? 63.766  62.096  -47.501 1.00 25.53 ? 123 ALA I N   1 
ATOM   9936  C  CA  . ALA I  1 150 ? 64.185  62.207  -48.892 1.00 31.19 ? 123 ALA I CA  1 
ATOM   9937  C  C   . ALA I  1 150 ? 63.778  60.960  -49.668 1.00 28.84 ? 123 ALA I C   1 
ATOM   9938  O  O   . ALA I  1 150 ? 63.763  59.844  -49.140 1.00 25.58 ? 123 ALA I O   1 
ATOM   9939  C  CB  . ALA I  1 150 ? 65.695  62.422  -48.982 1.00 26.78 ? 123 ALA I CB  1 
ATOM   9940  N  N   . ASP I  1 151 ? 63.403  61.166  -50.920 1.00 26.23 ? 124 ASP I N   1 
ATOM   9941  C  CA  . ASP I  1 151 ? 63.150  60.059  -51.827 1.00 26.85 ? 124 ASP I CA  1 
ATOM   9942  C  C   . ASP I  1 151 ? 64.511  59.621  -52.378 1.00 23.80 ? 124 ASP I C   1 
ATOM   9943  O  O   . ASP I  1 151 ? 65.293  60.458  -52.837 1.00 26.47 ? 124 ASP I O   1 
ATOM   9944  C  CB  . ASP I  1 151 ? 62.177  60.546  -52.909 1.00 23.49 ? 124 ASP I CB  1 
ATOM   9945  C  CG  . ASP I  1 151 ? 62.010  59.586  -54.082 1.00 30.37 ? 124 ASP I CG  1 
ATOM   9946  O  OD1 . ASP I  1 151 ? 62.593  58.487  -54.114 1.00 26.13 ? 124 ASP I OD1 1 
ATOM   9947  O  OD2 . ASP I  1 151 ? 61.235  59.963  -54.983 1.00 34.56 ? 124 ASP I OD2 1 
ATOM   9948  N  N   . ASP I  1 152 ? 64.841  58.330  -52.260 1.00 27.88 ? 125 ASP I N   1 
ATOM   9949  C  CA  . ASP I  1 152 ? 66.150  57.902  -52.761 1.00 29.14 ? 125 ASP I CA  1 
ATOM   9950  C  C   . ASP I  1 152 ? 66.148  57.627  -54.273 1.00 29.09 ? 125 ASP I C   1 
ATOM   9951  O  O   . ASP I  1 152 ? 67.146  57.122  -54.801 1.00 28.48 ? 125 ASP I O   1 
ATOM   9952  C  CB  . ASP I  1 152 ? 66.674  56.683  -51.964 1.00 24.53 ? 125 ASP I CB  1 
ATOM   9953  C  CG  . ASP I  1 152 ? 65.850  55.402  -52.166 1.00 26.01 ? 125 ASP I CG  1 
ATOM   9954  O  OD1 . ASP I  1 152 ? 65.075  55.291  -53.141 1.00 25.12 ? 125 ASP I OD1 1 
ATOM   9955  O  OD2 . ASP I  1 152 ? 65.993  54.476  -51.323 1.00 25.13 ? 125 ASP I OD2 1 
ATOM   9956  N  N   . LEU I  1 153 ? 65.049  57.949  -54.958 1.00 25.87 ? 126 LEU I N   1 
ATOM   9957  C  CA  . LEU I  1 153 ? 64.951  57.901  -56.419 1.00 26.07 ? 126 LEU I CA  1 
ATOM   9958  C  C   . LEU I  1 153 ? 65.087  56.473  -56.946 1.00 30.88 ? 126 LEU I C   1 
ATOM   9959  O  O   . LEU I  1 153 ? 65.478  56.257  -58.101 1.00 26.84 ? 126 LEU I O   1 
ATOM   9960  C  CB  . LEU I  1 153 ? 65.971  58.834  -57.088 1.00 24.96 ? 126 LEU I CB  1 
ATOM   9961  C  CG  . LEU I  1 153 ? 65.963  60.301  -56.603 1.00 31.88 ? 126 LEU I CG  1 
ATOM   9962  C  CD1 . LEU I  1 153 ? 66.867  61.189  -57.448 1.00 32.92 ? 126 LEU I CD1 1 
ATOM   9963  C  CD2 . LEU I  1 153 ? 64.541  60.863  -56.600 1.00 25.89 ? 126 LEU I CD2 1 
ATOM   9964  N  N   . GLY I  1 154 ? 64.729  55.497  -56.112 1.00 28.76 ? 127 GLY I N   1 
ATOM   9965  C  CA  . GLY I  1 154 ? 64.819  54.104  -56.493 1.00 27.50 ? 127 GLY I CA  1 
ATOM   9966  C  C   . GLY I  1 154 ? 66.213  53.517  -56.436 1.00 29.14 ? 127 GLY I C   1 
ATOM   9967  O  O   . GLY I  1 154 ? 66.426  52.421  -56.966 1.00 32.70 ? 127 GLY I O   1 
ATOM   9968  N  N   . LYS I  1 155 ? 67.173  54.209  -55.825 1.00 28.01 ? 128 LYS I N   1 
ATOM   9969  C  CA  . LYS I  1 155 ? 68.565  53.782  -55.805 1.00 25.43 ? 128 LYS I CA  1 
ATOM   9970  C  C   . LYS I  1 155 ? 68.982  53.164  -54.475 1.00 27.59 ? 128 LYS I C   1 
ATOM   9971  O  O   . LYS I  1 155 ? 70.184  53.013  -54.224 1.00 27.23 ? 128 LYS I O   1 
ATOM   9972  C  CB  . LYS I  1 155 ? 69.478  54.963  -56.150 1.00 27.84 ? 128 LYS I CB  1 
ATOM   9973  C  CG  . LYS I  1 155 ? 69.132  55.687  -57.461 1.00 28.37 ? 128 LYS I CG  1 
ATOM   9974  C  CD  . LYS I  1 155 ? 70.207  56.731  -57.786 1.00 32.37 ? 128 LYS I CD  1 
ATOM   9975  C  CE  . LYS I  1 155 ? 69.907  57.544  -59.041 1.00 40.39 ? 128 LYS I CE  1 
ATOM   9976  N  NZ  . LYS I  1 155 ? 69.625  56.692  -60.229 1.00 44.10 ? 128 LYS I NZ  1 
ATOM   9977  N  N   . GLY I  1 156 ? 68.025  52.804  -53.627 1.00 23.54 ? 129 GLY I N   1 
ATOM   9978  C  CA  . GLY I  1 156 ? 68.339  52.316  -52.298 1.00 23.80 ? 129 GLY I CA  1 
ATOM   9979  C  C   . GLY I  1 156 ? 68.593  50.824  -52.177 1.00 27.59 ? 129 GLY I C   1 
ATOM   9980  O  O   . GLY I  1 156 ? 69.048  50.367  -51.126 1.00 23.82 ? 129 GLY I O   1 
ATOM   9981  N  N   . GLY I  1 157 ? 68.283  50.047  -53.217 1.00 24.45 ? 130 GLY I N   1 
ATOM   9982  C  CA  . GLY I  1 157 ? 68.642  48.644  -53.279 1.00 23.93 ? 130 GLY I CA  1 
ATOM   9983  C  C   . GLY I  1 157 ? 67.842  47.718  -52.390 1.00 33.08 ? 130 GLY I C   1 
ATOM   9984  O  O   . GLY I  1 157 ? 68.178  46.528  -52.303 1.00 23.64 ? 130 GLY I O   1 
ATOM   9985  N  N   . ASN I  1 158 ? 66.826  48.218  -51.698 1.00 29.21 ? 131 ASN I N   1 
ATOM   9986  C  CA  . ASN I  1 158 ? 65.938  47.360  -50.935 1.00 27.93 ? 131 ASN I CA  1 
ATOM   9987  C  C   . ASN I  1 158 ? 64.549  47.423  -51.552 1.00 25.44 ? 131 ASN I C   1 
ATOM   9988  O  O   . ASN I  1 158 ? 64.291  48.196  -52.477 1.00 29.27 ? 131 ASN I O   1 
ATOM   9989  C  CB  . ASN I  1 158 ? 65.936  47.724  -49.432 1.00 29.93 ? 131 ASN I CB  1 
ATOM   9990  C  CG  . ASN I  1 158 ? 65.398  49.134  -49.134 1.00 31.81 ? 131 ASN I CG  1 
ATOM   9991  O  OD1 . ASN I  1 158 ? 65.121  49.930  -50.032 1.00 32.67 ? 131 ASN I OD1 1 
ATOM   9992  N  ND2 . ASN I  1 158 ? 65.267  49.439  -47.843 1.00 34.08 ? 131 ASN I ND2 1 
ATOM   9993  N  N   . GLU I  1 159 ? 63.659  46.556  -51.058 1.00 30.98 ? 132 GLU I N   1 
ATOM   9994  C  CA  . GLU I  1 159 ? 62.312  46.491  -51.615 1.00 29.31 ? 132 GLU I CA  1 
ATOM   9995  C  C   . GLU I  1 159 ? 61.579  47.818  -51.463 1.00 28.87 ? 132 GLU I C   1 
ATOM   9996  O  O   . GLU I  1 159 ? 60.835  48.230  -52.361 1.00 30.00 ? 132 GLU I O   1 
ATOM   9997  C  CB  . GLU I  1 159 ? 61.509  45.386  -50.940 1.00 38.17 ? 132 GLU I CB  1 
ATOM   9998  C  CG  . GLU I  1 159 ? 62.313  44.164  -50.551 1.00 44.23 ? 132 GLU I CG  1 
ATOM   9999  C  CD  . GLU I  1 159 ? 61.433  43.089  -49.917 1.00 62.89 ? 132 GLU I CD  1 
ATOM   10000 O  OE1 . GLU I  1 159 ? 60.428  43.454  -49.256 1.00 60.92 ? 132 GLU I OE1 1 
ATOM   10001 O  OE2 . GLU I  1 159 ? 61.734  41.887  -50.098 1.00 62.48 ? 132 GLU I OE2 1 
ATOM   10002 N  N   . GLU I  1 160 ? 61.774  48.494  -50.329 1.00 32.90 ? 133 GLU I N   1 
ATOM   10003 C  CA  . GLU I  1 160 ? 61.098  49.769  -50.093 1.00 32.39 ? 133 GLU I CA  1 
ATOM   10004 C  C   . GLU I  1 160 ? 61.452  50.793  -51.167 1.00 31.84 ? 133 GLU I C   1 
ATOM   10005 O  O   . GLU I  1 160 ? 60.575  51.498  -51.683 1.00 31.41 ? 133 GLU I O   1 
ATOM   10006 C  CB  . GLU I  1 160 ? 61.457  50.296  -48.702 1.00 38.70 ? 133 GLU I CB  1 
ATOM   10007 C  CG  . GLU I  1 160 ? 60.459  51.288  -48.140 1.00 41.88 ? 133 GLU I CG  1 
ATOM   10008 C  CD  . GLU I  1 160 ? 59.045  50.736  -48.093 1.00 50.02 ? 133 GLU I CD  1 
ATOM   10009 O  OE1 . GLU I  1 160 ? 58.808  49.735  -47.383 1.00 45.83 ? 133 GLU I OE1 1 
ATOM   10010 O  OE2 . GLU I  1 160 ? 58.171  51.294  -48.786 1.00 50.68 ? 133 GLU I OE2 1 
ATOM   10011 N  N   . SER I  1 161 ? 62.735  50.877  -51.523 1.00 31.58 ? 134 SER I N   1 
ATOM   10012 C  CA  . SER I  1 161 ? 63.175  51.839  -52.525 1.00 28.52 ? 134 SER I CA  1 
ATOM   10013 C  C   . SER I  1 161 ? 62.411  51.676  -53.830 1.00 31.76 ? 134 SER I C   1 
ATOM   10014 O  O   . SER I  1 161 ? 61.988  52.665  -54.442 1.00 28.80 ? 134 SER I O   1 
ATOM   10015 C  CB  . SER I  1 161 ? 64.672  51.696  -52.759 1.00 27.46 ? 134 SER I CB  1 
ATOM   10016 O  OG  . SER I  1 161 ? 65.099  52.652  -53.710 1.00 26.88 ? 134 SER I OG  1 
ATOM   10017 N  N   . THR I  1 162 ? 62.222  50.427  -54.265 1.00 28.48 ? 135 THR I N   1 
ATOM   10018 C  CA  . THR I  1 162 ? 61.510  50.109  -55.495 1.00 31.33 ? 135 THR I CA  1 
ATOM   10019 C  C   . THR I  1 162 ? 60.028  50.478  -55.458 1.00 27.39 ? 135 THR I C   1 
ATOM   10020 O  O   . THR I  1 162 ? 59.378  50.463  -56.511 1.00 31.29 ? 135 THR I O   1 
ATOM   10021 C  CB  . THR I  1 162 ? 61.648  48.603  -55.786 1.00 36.56 ? 135 THR I CB  1 
ATOM   10022 O  OG1 . THR I  1 162 ? 60.758  47.869  -54.938 1.00 40.52 ? 135 THR I OG1 1 
ATOM   10023 C  CG2 . THR I  1 162 ? 63.069  48.128  -55.503 1.00 35.49 ? 135 THR I CG2 1 
ATOM   10024 N  N   . LYS I  1 163 ? 59.468  50.770  -54.286 1.00 33.23 ? 136 LYS I N   1 
ATOM   10025 C  CA  . LYS I  1 163 ? 58.063  51.149  -54.165 1.00 27.80 ? 136 LYS I CA  1 
ATOM   10026 C  C   . LYS I  1 163 ? 57.865  52.614  -53.805 1.00 28.25 ? 136 LYS I C   1 
ATOM   10027 O  O   . LYS I  1 163 ? 57.095  53.326  -54.462 1.00 27.79 ? 136 LYS I O   1 
ATOM   10028 C  CB  . LYS I  1 163 ? 57.369  50.262  -53.117 1.00 32.12 ? 136 LYS I CB  1 
ATOM   10029 C  CG  . LYS I  1 163 ? 57.600  48.786  -53.346 1.00 36.91 ? 136 LYS I CG  1 
ATOM   10030 C  CD  . LYS I  1 163 ? 56.859  47.926  -52.338 1.00 42.62 ? 136 LYS I CD  1 
ATOM   10031 C  CE  . LYS I  1 163 ? 57.780  47.496  -51.206 1.00 45.97 ? 136 LYS I CE  1 
ATOM   10032 N  NZ  . LYS I  1 163 ? 57.027  47.238  -49.937 1.00 57.81 ? 136 LYS I NZ  1 
ATOM   10033 N  N   . THR I  1 164 ? 58.558  53.086  -52.771 1.00 29.76 ? 137 THR I N   1 
ATOM   10034 C  CA  . THR I  1 164 ? 58.336  54.411  -52.223 1.00 27.69 ? 137 THR I CA  1 
ATOM   10035 C  C   . THR I  1 164 ? 59.561  55.304  -52.235 1.00 34.83 ? 137 THR I C   1 
ATOM   10036 O  O   . THR I  1 164 ? 59.449  56.473  -51.838 1.00 27.78 ? 137 THR I O   1 
ATOM   10037 C  CB  . THR I  1 164 ? 57.851  54.305  -50.769 1.00 30.00 ? 137 THR I CB  1 
ATOM   10038 O  OG1 . THR I  1 164 ? 58.922  53.808  -49.958 1.00 31.62 ? 137 THR I OG1 1 
ATOM   10039 C  CG2 . THR I  1 164 ? 56.658  53.371  -50.669 1.00 31.89 ? 137 THR I CG2 1 
ATOM   10040 N  N   . GLY I  1 165 ? 60.724  54.796  -52.647 1.00 23.91 ? 138 GLY I N   1 
ATOM   10041 C  CA  . GLY I  1 165 ? 61.925  55.590  -52.515 1.00 22.84 ? 138 GLY I CA  1 
ATOM   10042 C  C   . GLY I  1 165 ? 62.395  55.756  -51.087 1.00 23.45 ? 138 GLY I C   1 
ATOM   10043 O  O   . GLY I  1 165 ? 63.268  56.589  -50.834 1.00 24.38 ? 138 GLY I O   1 
ATOM   10044 N  N   . ASN I  1 166 ? 61.860  54.968  -50.152 1.00 26.97 ? 139 ASN I N   1 
ATOM   10045 C  CA  . ASN I  1 166 ? 62.145  55.107  -48.722 1.00 27.45 ? 139 ASN I CA  1 
ATOM   10046 C  C   . ASN I  1 166 ? 61.781  56.500  -48.201 1.00 26.69 ? 139 ASN I C   1 
ATOM   10047 O  O   . ASN I  1 166 ? 62.417  56.997  -47.271 1.00 27.85 ? 139 ASN I O   1 
ATOM   10048 C  CB  . ASN I  1 166 ? 63.620  54.801  -48.407 1.00 25.75 ? 139 ASN I CB  1 
ATOM   10049 C  CG  . ASN I  1 166 ? 63.944  53.311  -48.495 1.00 34.81 ? 139 ASN I CG  1 
ATOM   10050 O  OD1 . ASN I  1 166 ? 63.489  52.526  -47.671 1.00 38.68 ? 139 ASN I OD1 1 
ATOM   10051 N  ND2 . ASN I  1 166 ? 64.710  52.922  -49.507 1.00 28.73 ? 139 ASN I ND2 1 
ATOM   10052 N  N   . ALA I  1 167 ? 60.778  57.159  -48.794 1.00 25.61 ? 140 ALA I N   1 
ATOM   10053 C  CA  . ALA I  1 167 ? 60.477  58.535  -48.391 1.00 30.26 ? 140 ALA I CA  1 
ATOM   10054 C  C   . ALA I  1 167 ? 59.703  58.621  -47.078 1.00 28.16 ? 140 ALA I C   1 
ATOM   10055 O  O   . ALA I  1 167 ? 59.459  59.735  -46.594 1.00 26.94 ? 140 ALA I O   1 
ATOM   10056 C  CB  . ALA I  1 167 ? 59.692  59.265  -49.489 1.00 25.47 ? 140 ALA I CB  1 
ATOM   10057 N  N   . GLY I  1 168 ? 59.307  57.488  -46.499 1.00 30.91 ? 141 GLY I N   1 
ATOM   10058 C  CA  . GLY I  1 168 ? 58.717  57.505  -45.173 1.00 29.45 ? 141 GLY I CA  1 
ATOM   10059 C  C   . GLY I  1 168 ? 57.289  58.029  -45.157 1.00 33.13 ? 141 GLY I C   1 
ATOM   10060 O  O   . GLY I  1 168 ? 56.562  57.992  -46.150 1.00 24.17 ? 141 GLY I O   1 
ATOM   10061 N  N   . SER I  1 169 ? 56.889  58.532  -43.992 1.00 27.01 ? 142 SER I N   1 
ATOM   10062 C  CA  . SER I  1 169 ? 55.478  58.786  -43.740 1.00 25.79 ? 142 SER I CA  1 
ATOM   10063 C  C   . SER I  1 169 ? 54.958  59.963  -44.575 1.00 26.23 ? 142 SER I C   1 
ATOM   10064 O  O   . SER I  1 169 ? 55.715  60.755  -45.148 1.00 25.45 ? 142 SER I O   1 
ATOM   10065 C  CB  . SER I  1 169 ? 55.258  59.050  -42.245 1.00 32.29 ? 142 SER I CB  1 
ATOM   10066 O  OG  . SER I  1 169 ? 55.549  60.405  -41.939 1.00 41.74 ? 142 SER I OG  1 
ATOM   10067 N  N   . ARG I  1 170 ? 53.633  60.068  -44.630 1.00 25.86 ? 143 ARG I N   1 
ATOM   10068 C  CA  . ARG I  1 170 ? 52.946  61.083  -45.419 1.00 26.12 ? 143 ARG I CA  1 
ATOM   10069 C  C   . ARG I  1 170 ? 52.626  62.270  -44.512 1.00 28.31 ? 143 ARG I C   1 
ATOM   10070 O  O   . ARG I  1 170 ? 51.781  62.164  -43.620 1.00 25.28 ? 143 ARG I O   1 
ATOM   10071 C  CB  . ARG I  1 170 ? 51.687  60.488  -46.041 1.00 23.73 ? 143 ARG I CB  1 
ATOM   10072 C  CG  . ARG I  1 170 ? 51.982  59.141  -46.733 1.00 26.87 ? 143 ARG I CG  1 
ATOM   10073 C  CD  . ARG I  1 170 ? 50.764  58.483  -47.363 1.00 28.25 ? 143 ARG I CD  1 
ATOM   10074 N  NE  . ARG I  1 170 ? 51.183  57.231  -47.987 1.00 35.58 ? 143 ARG I NE  1 
ATOM   10075 C  CZ  . ARG I  1 170 ? 50.461  56.504  -48.827 1.00 32.26 ? 143 ARG I CZ  1 
ATOM   10076 N  NH1 . ARG I  1 170 ? 49.245  56.873  -49.199 1.00 26.74 ? 143 ARG I NH1 1 
ATOM   10077 N  NH2 . ARG I  1 170 ? 50.985  55.384  -49.326 1.00 30.99 ? 143 ARG I NH2 1 
ATOM   10078 N  N   . LEU I  1 171 ? 53.308  63.393  -44.748 1.00 22.67 ? 144 LEU I N   1 
ATOM   10079 C  CA  . LEU I  1 171 ? 53.179  64.576  -43.899 1.00 20.51 ? 144 LEU I CA  1 
ATOM   10080 C  C   . LEU I  1 171 ? 51.947  65.403  -44.235 1.00 29.82 ? 144 LEU I C   1 
ATOM   10081 O  O   . LEU I  1 171 ? 51.259  65.884  -43.328 1.00 23.20 ? 144 LEU I O   1 
ATOM   10082 C  CB  . LEU I  1 171 ? 54.428  65.444  -44.028 1.00 20.50 ? 144 LEU I CB  1 
ATOM   10083 C  CG  . LEU I  1 171 ? 55.725  64.808  -43.540 1.00 26.03 ? 144 LEU I CG  1 
ATOM   10084 C  CD1 . LEU I  1 171 ? 56.851  65.826  -43.623 1.00 30.46 ? 144 LEU I CD1 1 
ATOM   10085 C  CD2 . LEU I  1 171 ? 55.567  64.264  -42.120 1.00 32.43 ? 144 LEU I CD2 1 
ATOM   10086 N  N   . ALA I  1 172 ? 51.671  65.616  -45.523 1.00 24.92 ? 145 ALA I N   1 
ATOM   10087 C  CA  . ALA I  1 172 ? 50.487  66.360  -45.926 1.00 25.27 ? 145 ALA I CA  1 
ATOM   10088 C  C   . ALA I  1 172 ? 50.080  65.903  -47.319 1.00 21.53 ? 145 ALA I C   1 
ATOM   10089 O  O   . ALA I  1 172 ? 50.903  65.402  -48.093 1.00 23.21 ? 145 ALA I O   1 
ATOM   10090 C  CB  . ALA I  1 172 ? 50.733  67.872  -45.907 1.00 21.38 ? 145 ALA I CB  1 
ATOM   10091 N  N   . CYS I  1 173 ? 48.806  66.089  -47.636 1.00 22.27 ? 146 CYS I N   1 
ATOM   10092 C  CA  . CYS I  1 173 ? 48.324  65.686  -48.956 1.00 22.03 ? 146 CYS I CA  1 
ATOM   10093 C  C   . CYS I  1 173 ? 47.063  66.460  -49.305 1.00 23.99 ? 146 CYS I C   1 
ATOM   10094 O  O   . CYS I  1 173 ? 46.431  67.080  -48.450 1.00 23.47 ? 146 CYS I O   1 
ATOM   10095 C  CB  . CYS I  1 173 ? 48.034  64.188  -49.005 1.00 27.08 ? 146 CYS I CB  1 
ATOM   10096 S  SG  . CYS I  1 173 ? 46.779  63.679  -47.812 1.00 29.35 ? 146 CYS I SG  1 
ATOM   10097 N  N   . GLY I  1 174 ? 46.688  66.385  -50.578 1.00 20.44 ? 147 GLY I N   1 
ATOM   10098 C  CA  . GLY I  1 174 ? 45.441  66.969  -51.037 1.00 24.03 ? 147 GLY I CA  1 
ATOM   10099 C  C   . GLY I  1 174 ? 45.053  66.344  -52.356 1.00 25.18 ? 147 GLY I C   1 
ATOM   10100 O  O   . GLY I  1 174 ? 45.892  65.768  -53.057 1.00 24.04 ? 147 GLY I O   1 
ATOM   10101 N  N   . VAL I  1 175 ? 43.769  66.423  -52.676 1.00 23.10 ? 148 VAL I N   1 
ATOM   10102 C  CA  . VAL I  1 175 ? 43.307  65.966  -53.985 1.00 25.34 ? 148 VAL I CA  1 
ATOM   10103 C  C   . VAL I  1 175 ? 43.580  67.051  -55.019 1.00 25.74 ? 148 VAL I C   1 
ATOM   10104 O  O   . VAL I  1 175 ? 43.366  68.247  -54.767 1.00 24.42 ? 148 VAL I O   1 
ATOM   10105 C  CB  . VAL I  1 175 ? 41.817  65.601  -53.936 1.00 24.49 ? 148 VAL I CB  1 
ATOM   10106 C  CG1 . VAL I  1 175 ? 41.359  65.091  -55.286 1.00 29.88 ? 148 VAL I CG1 1 
ATOM   10107 C  CG2 . VAL I  1 175 ? 41.566  64.554  -52.842 1.00 28.57 ? 148 VAL I CG2 1 
ATOM   10108 N  N   . ILE I  1 176 ? 44.067  66.634  -56.187 1.00 24.45 ? 149 ILE I N   1 
ATOM   10109 C  CA  . ILE I  1 176 ? 44.399  67.559  -57.265 1.00 26.64 ? 149 ILE I CA  1 
ATOM   10110 C  C   . ILE I  1 176 ? 43.120  67.906  -58.021 1.00 26.61 ? 149 ILE I C   1 
ATOM   10111 O  O   . ILE I  1 176 ? 42.481  67.034  -58.617 1.00 27.14 ? 149 ILE I O   1 
ATOM   10112 C  CB  . ILE I  1 176 ? 45.459  66.959  -58.207 1.00 21.61 ? 149 ILE I CB  1 
ATOM   10113 C  CG1 . ILE I  1 176 ? 46.748  66.658  -57.445 1.00 25.01 ? 149 ILE I CG1 1 
ATOM   10114 C  CG2 . ILE I  1 176 ? 45.739  67.914  -59.371 1.00 21.74 ? 149 ILE I CG2 1 
ATOM   10115 C  CD1 . ILE I  1 176 ? 47.648  65.594  -58.085 1.00 23.69 ? 149 ILE I CD1 1 
ATOM   10116 N  N   . GLY I  1 177 ? 42.753  69.189  -58.005 1.00 22.60 ? 150 GLY I N   1 
ATOM   10117 C  CA  . GLY I  1 177 ? 41.498  69.615  -58.584 1.00 22.02 ? 150 GLY I CA  1 
ATOM   10118 C  C   . GLY I  1 177 ? 41.643  70.556  -59.767 1.00 30.28 ? 150 GLY I C   1 
ATOM   10119 O  O   . GLY I  1 177 ? 42.683  71.203  -59.929 1.00 22.82 ? 150 GLY I O   1 
ATOM   10120 N  N   . ILE I  1 178 ? 40.587  70.650  -60.579 1.00 25.31 ? 151 ILE I N   1 
ATOM   10121 C  CA  . ILE I  1 178 ? 40.580  71.520  -61.756 1.00 27.58 ? 151 ILE I CA  1 
ATOM   10122 C  C   . ILE I  1 178 ? 40.561  72.983  -61.328 1.00 33.53 ? 151 ILE I C   1 
ATOM   10123 O  O   . ILE I  1 178 ? 39.749  73.389  -60.488 1.00 31.52 ? 151 ILE I O   1 
ATOM   10124 C  CB  . ILE I  1 178 ? 39.364  71.194  -62.640 1.00 28.31 ? 151 ILE I CB  1 
ATOM   10125 C  CG1 . ILE I  1 178 ? 39.490  69.776  -63.198 1.00 33.21 ? 151 ILE I CG1 1 
ATOM   10126 C  CG2 . ILE I  1 178 ? 39.235  72.228  -63.750 1.00 34.37 ? 151 ILE I CG2 1 
ATOM   10127 C  CD1 . ILE I  1 178 ? 38.209  69.234  -63.861 1.00 36.23 ? 151 ILE I CD1 1 
ATOM   10128 N  N   . ALA I  1 179 ? 41.439  73.792  -61.922 1.00 22.68 ? 152 ALA I N   1 
ATOM   10129 C  CA  . ALA I  1 179 ? 41.537  75.206  -61.591 1.00 31.05 ? 152 ALA I CA  1 
ATOM   10130 C  C   . ALA I  1 179 ? 41.100  76.062  -62.771 1.00 39.00 ? 152 ALA I C   1 
ATOM   10131 O  O   . ALA I  1 179 ? 41.181  75.645  -63.932 1.00 36.87 ? 152 ALA I O   1 
ATOM   10132 C  CB  . ALA I  1 179 ? 42.965  75.585  -61.191 1.00 30.23 ? 152 ALA I CB  1 
ATOM   10133 N  N   . GLN I  1 180 ? 40.633  77.266  -62.465 1.00 37.36 ? 153 GLN I N   1 
ATOM   10134 C  CA  . GLN I  1 180 ? 40.248  78.199  -63.515 1.00 48.18 ? 153 GLN I CA  1 
ATOM   10135 C  C   . GLN I  1 180 ? 41.489  78.727  -64.245 1.00 55.95 ? 153 GLN I C   1 
ATOM   10136 O  O   . GLN I  1 180 ? 42.376  79.357  -63.658 1.00 58.02 ? 153 GLN I O   1 
ATOM   10137 C  CB  . GLN I  1 180 ? 39.424  79.356  -62.941 1.00 42.78 ? 153 GLN I CB  1 
ATOM   10138 C  CG  . GLN I  1 180 ? 38.573  80.078  -63.991 1.00 40.45 ? 153 GLN I CG  1 
ATOM   10139 C  CD  . GLN I  1 180 ? 37.596  81.067  -63.373 1.00 53.66 ? 153 GLN I CD  1 
ATOM   10140 O  OE1 . GLN I  1 180 ? 37.615  81.303  -62.159 1.00 59.09 ? 153 GLN I OE1 1 
ATOM   10141 N  NE2 . GLN I  1 180 ? 36.731  81.646  -64.203 1.00 49.62 ? 153 GLN I NE2 1 
ATOM   10142 O  OXT . GLN I  1 180 ? 41.628  78.521  -65.451 1.00 66.25 ? 153 GLN I OXT 1 
ATOM   10143 N  N   . ALA J  1 28  ? 36.989  54.965  -65.118 1.00 52.36 ? 1   ALA J N   1 
ATOM   10144 C  CA  . ALA J  1 28  ? 36.697  55.562  -63.810 1.00 50.02 ? 1   ALA J CA  1 
ATOM   10145 C  C   . ALA J  1 28  ? 35.332  55.113  -63.287 1.00 41.82 ? 1   ALA J C   1 
ATOM   10146 O  O   . ALA J  1 28  ? 34.302  55.651  -63.695 1.00 51.37 ? 1   ALA J O   1 
ATOM   10147 C  CB  . ALA J  1 28  ? 36.756  57.087  -63.899 1.00 46.90 ? 1   ALA J CB  1 
ATOM   10148 N  N   . THR J  1 29  ? 35.317  54.137  -62.380 1.00 42.35 ? 2   THR J N   1 
ATOM   10149 C  CA  . THR J  1 29  ? 34.052  53.591  -61.900 1.00 45.95 ? 2   THR J CA  1 
ATOM   10150 C  C   . THR J  1 29  ? 33.673  54.054  -60.494 1.00 41.23 ? 2   THR J C   1 
ATOM   10151 O  O   . THR J  1 29  ? 32.479  54.075  -60.177 1.00 43.08 ? 2   THR J O   1 
ATOM   10152 C  CB  . THR J  1 29  ? 34.074  52.054  -61.950 1.00 34.77 ? 2   THR J CB  1 
ATOM   10153 O  OG1 . THR J  1 29  ? 34.990  51.542  -60.980 1.00 49.42 ? 2   THR J OG1 1 
ATOM   10154 C  CG2 . THR J  1 29  ? 34.523  51.592  -63.329 1.00 43.55 ? 2   THR J CG2 1 
ATOM   10155 N  N   . LYS J  1 30  ? 34.642  54.455  -59.656 1.00 39.01 ? 3   LYS J N   1 
ATOM   10156 C  CA  . LYS J  1 30  ? 34.374  54.886  -58.286 1.00 35.51 ? 3   LYS J CA  1 
ATOM   10157 C  C   . LYS J  1 30  ? 35.087  56.194  -57.962 1.00 35.94 ? 3   LYS J C   1 
ATOM   10158 O  O   . LYS J  1 30  ? 36.235  56.402  -58.360 1.00 32.30 ? 3   LYS J O   1 
ATOM   10159 C  CB  . LYS J  1 30  ? 34.810  53.820  -57.267 1.00 36.04 ? 3   LYS J CB  1 
ATOM   10160 C  CG  . LYS J  1 30  ? 33.744  52.776  -56.926 1.00 47.02 ? 3   LYS J CG  1 
ATOM   10161 C  CD  . LYS J  1 30  ? 34.386  51.542  -56.295 1.00 50.74 ? 3   LYS J CD  1 
ATOM   10162 C  CE  . LYS J  1 30  ? 33.356  50.648  -55.615 1.00 48.16 ? 3   LYS J CE  1 
ATOM   10163 N  NZ  . LYS J  1 30  ? 33.864  50.044  -54.340 1.00 56.56 ? 3   LYS J NZ  1 
ATOM   10164 N  N   . ALA J  1 31  ? 34.411  57.056  -57.198 1.00 32.21 ? 4   ALA J N   1 
ATOM   10165 C  CA  . ALA J  1 31  ? 34.965  58.326  -56.746 1.00 26.91 ? 4   ALA J CA  1 
ATOM   10166 C  C   . ALA J  1 31  ? 34.575  58.546  -55.289 1.00 33.14 ? 4   ALA J C   1 
ATOM   10167 O  O   . ALA J  1 31  ? 33.672  57.894  -54.752 1.00 30.16 ? 4   ALA J O   1 
ATOM   10168 C  CB  . ALA J  1 31  ? 34.480  59.501  -57.603 1.00 31.70 ? 4   ALA J CB  1 
ATOM   10169 N  N   . VAL J  1 32  ? 35.252  59.492  -54.648 1.00 26.53 ? 5   VAL J N   1 
ATOM   10170 C  CA  . VAL J  1 32  ? 34.988  59.772  -53.244 1.00 29.30 ? 5   VAL J CA  1 
ATOM   10171 C  C   . VAL J  1 32  ? 35.266  61.244  -52.988 1.00 30.71 ? 5   VAL J C   1 
ATOM   10172 O  O   . VAL J  1 32  ? 36.028  61.896  -53.709 1.00 26.74 ? 5   VAL J O   1 
ATOM   10173 C  CB  . VAL J  1 32  ? 35.820  58.847  -52.321 1.00 33.94 ? 5   VAL J CB  1 
ATOM   10174 C  CG1 . VAL J  1 32  ? 37.310  59.206  -52.375 1.00 28.31 ? 5   VAL J CG1 1 
ATOM   10175 C  CG2 . VAL J  1 32  ? 35.286  58.873  -50.880 1.00 35.35 ? 5   VAL J CG2 1 
ATOM   10176 N  N   . CYS J  1 33  ? 34.610  61.773  -51.961 1.00 28.79 ? 6   CYS J N   1 
ATOM   10177 C  CA  . CYS J  1 33  ? 34.749  63.169  -51.608 1.00 22.43 ? 6   CYS J CA  1 
ATOM   10178 C  C   . CYS J  1 33  ? 34.682  63.280  -50.090 1.00 24.99 ? 6   CYS J C   1 
ATOM   10179 O  O   . CYS J  1 33  ? 33.788  62.707  -49.462 1.00 26.96 ? 6   CYS J O   1 
ATOM   10180 C  CB  . CYS J  1 33  ? 33.648  64.001  -52.258 1.00 22.40 ? 6   CYS J CB  1 
ATOM   10181 S  SG  . CYS J  1 33  ? 33.774  65.754  -51.950 1.00 31.73 ? 6   CYS J SG  1 
ATOM   10182 N  N   . VAL J  1 34  ? 35.629  64.000  -49.511 1.00 22.98 ? 7   VAL J N   1 
ATOM   10183 C  CA  . VAL J  1 34  ? 35.651  64.279  -48.076 1.00 26.51 ? 7   VAL J CA  1 
ATOM   10184 C  C   . VAL J  1 34  ? 35.283  65.739  -47.894 1.00 26.27 ? 7   VAL J C   1 
ATOM   10185 O  O   . VAL J  1 34  ? 36.004  66.627  -48.365 1.00 26.87 ? 7   VAL J O   1 
ATOM   10186 C  CB  . VAL J  1 34  ? 37.023  63.977  -47.466 1.00 26.53 ? 7   VAL J CB  1 
ATOM   10187 C  CG1 . VAL J  1 34  ? 37.077  64.418  -46.005 1.00 25.51 ? 7   VAL J CG1 1 
ATOM   10188 C  CG2 . VAL J  1 34  ? 37.316  62.495  -47.592 1.00 28.51 ? 7   VAL J CG2 1 
ATOM   10189 N  N   . LEU J  1 35  ? 34.154  65.997  -47.243 1.00 27.49 ? 8   LEU J N   1 
ATOM   10190 C  CA  . LEU J  1 35  ? 33.669  67.364  -47.104 1.00 22.69 ? 8   LEU J CA  1 
ATOM   10191 C  C   . LEU J  1 35  ? 34.159  67.949  -45.788 1.00 30.76 ? 8   LEU J C   1 
ATOM   10192 O  O   . LEU J  1 35  ? 34.041  67.311  -44.740 1.00 25.49 ? 8   LEU J O   1 
ATOM   10193 C  CB  . LEU J  1 35  ? 32.148  67.407  -47.165 1.00 25.50 ? 8   LEU J CB  1 
ATOM   10194 C  CG  . LEU J  1 35  ? 31.481  66.931  -48.457 1.00 32.03 ? 8   LEU J CG  1 
ATOM   10195 C  CD1 . LEU J  1 35  ? 30.046  66.532  -48.159 1.00 35.88 ? 8   LEU J CD1 1 
ATOM   10196 C  CD2 . LEU J  1 35  ? 31.501  68.040  -49.459 1.00 29.54 ? 8   LEU J CD2 1 
ATOM   10197 N  N   . LYS J  1 36  ? 34.709  69.159  -45.854 1.00 26.64 ? 9   LYS J N   1 
ATOM   10198 C  CA  . LYS J  1 36  ? 35.223  69.883  -44.696 1.00 29.79 ? 9   LYS J CA  1 
ATOM   10199 C  C   . LYS J  1 36  ? 34.925  71.357  -44.907 1.00 31.12 ? 9   LYS J C   1 
ATOM   10200 O  O   . LYS J  1 36  ? 34.783  71.821  -46.043 1.00 30.05 ? 9   LYS J O   1 
ATOM   10201 C  CB  . LYS J  1 36  ? 36.739  69.695  -44.499 1.00 28.34 ? 9   LYS J CB  1 
ATOM   10202 C  CG  . LYS J  1 36  ? 37.214  68.331  -44.005 1.00 35.41 ? 9   LYS J CG  1 
ATOM   10203 C  CD  . LYS J  1 36  ? 36.748  68.028  -42.595 1.00 43.56 ? 9   LYS J CD  1 
ATOM   10204 C  CE  . LYS J  1 36  ? 36.874  66.542  -42.268 1.00 45.50 ? 9   LYS J CE  1 
ATOM   10205 N  NZ  . LYS J  1 36  ? 35.943  65.692  -43.063 1.00 45.73 ? 9   LYS J NZ  1 
ATOM   10206 N  N   . GLY J  1 37  ? 34.844  72.101  -43.805 1.00 25.15 ? 10  GLY J N   1 
ATOM   10207 C  CA  . GLY J  1 37  ? 34.615  73.533  -43.904 1.00 26.73 ? 10  GLY J CA  1 
ATOM   10208 C  C   . GLY J  1 37  ? 35.151  74.320  -42.721 1.00 33.97 ? 10  GLY J C   1 
ATOM   10209 O  O   . GLY J  1 37  ? 35.929  73.791  -41.922 1.00 33.82 ? 10  GLY J O   1 
ATOM   10210 N  N   . ASP J  1 38  ? 34.741  75.586  -42.606 1.00 37.78 ? 11  ASP J N   1 
ATOM   10211 C  CA  . ASP J  1 38  ? 35.197  76.451  -41.524 1.00 37.30 ? 11  ASP J CA  1 
ATOM   10212 C  C   . ASP J  1 38  ? 34.490  76.166  -40.210 1.00 37.92 ? 11  ASP J C   1 
ATOM   10213 O  O   . ASP J  1 38  ? 34.987  76.564  -39.150 1.00 40.22 ? 11  ASP J O   1 
ATOM   10214 C  CB  . ASP J  1 38  ? 34.984  77.917  -41.895 1.00 42.34 ? 11  ASP J CB  1 
ATOM   10215 C  CG  . ASP J  1 38  ? 35.758  78.319  -43.126 1.00 57.27 ? 11  ASP J CG  1 
ATOM   10216 O  OD1 . ASP J  1 38  ? 36.849  77.744  -43.352 1.00 67.76 ? 11  ASP J OD1 1 
ATOM   10217 O  OD2 . ASP J  1 38  ? 35.286  79.218  -43.861 1.00 64.26 ? 11  ASP J OD2 1 
ATOM   10218 N  N   . GLY J  1 39  ? 33.335  75.510  -40.262 1.00 36.57 ? 12  GLY J N   1 
ATOM   10219 C  CA  . GLY J  1 39  ? 32.633  75.090  -39.080 1.00 29.67 ? 12  GLY J CA  1 
ATOM   10220 C  C   . GLY J  1 39  ? 32.724  73.596  -38.874 1.00 32.30 ? 12  GLY J C   1 
ATOM   10221 O  O   . GLY J  1 39  ? 33.716  72.947  -39.221 1.00 37.73 ? 12  GLY J O   1 
ATOM   10222 N  N   . PRO J  1 40  ? 31.672  73.017  -38.301 1.00 30.41 ? 13  PRO J N   1 
ATOM   10223 C  CA  . PRO J  1 40  ? 31.693  71.593  -37.926 1.00 25.27 ? 13  PRO J CA  1 
ATOM   10224 C  C   . PRO J  1 40  ? 31.163  70.628  -38.979 1.00 26.27 ? 13  PRO J C   1 
ATOM   10225 O  O   . PRO J  1 40  ? 31.107  69.426  -38.696 1.00 26.08 ? 13  PRO J O   1 
ATOM   10226 C  CB  . PRO J  1 40  ? 30.777  71.590  -36.700 1.00 26.92 ? 13  PRO J CB  1 
ATOM   10227 C  CG  . PRO J  1 40  ? 29.708  72.609  -37.083 1.00 28.15 ? 13  PRO J CG  1 
ATOM   10228 C  CD  . PRO J  1 40  ? 30.429  73.691  -37.877 1.00 32.49 ? 13  PRO J CD  1 
ATOM   10229 N  N   . VAL J  1 41  ? 30.763  71.112  -40.152 1.00 30.94 ? 14  VAL J N   1 
ATOM   10230 C  CA  . VAL J  1 41  ? 30.176  70.233  -41.160 1.00 28.02 ? 14  VAL J CA  1 
ATOM   10231 C  C   . VAL J  1 41  ? 31.278  69.360  -41.748 1.00 30.16 ? 14  VAL J C   1 
ATOM   10232 O  O   . VAL J  1 41  ? 32.270  69.873  -42.279 1.00 28.58 ? 14  VAL J O   1 
ATOM   10233 C  CB  . VAL J  1 41  ? 29.467  71.049  -42.245 1.00 25.39 ? 14  VAL J CB  1 
ATOM   10234 C  CG1 . VAL J  1 41  ? 28.976  70.133  -43.363 1.00 27.06 ? 14  VAL J CG1 1 
ATOM   10235 C  CG2 . VAL J  1 41  ? 28.316  71.856  -41.623 1.00 30.42 ? 14  VAL J CG2 1 
ATOM   10236 N  N   . GLN J  1 42  ? 31.133  68.043  -41.608 1.00 30.07 ? 15  GLN J N   1 
ATOM   10237 C  CA  . GLN J  1 42  ? 32.063  67.064  -42.161 1.00 31.53 ? 15  GLN J CA  1 
ATOM   10238 C  C   . GLN J  1 42  ? 31.277  65.915  -42.765 1.00 32.85 ? 15  GLN J C   1 
ATOM   10239 O  O   . GLN J  1 42  ? 30.202  65.560  -42.281 1.00 31.37 ? 15  GLN J O   1 
ATOM   10240 C  CB  . GLN J  1 42  ? 33.033  66.496  -41.102 1.00 35.92 ? 15  GLN J CB  1 
ATOM   10241 C  CG  . GLN J  1 42  ? 33.484  67.484  -40.061 1.00 33.64 ? 15  GLN J CG  1 
ATOM   10242 C  CD  . GLN J  1 42  ? 34.248  66.834  -38.917 1.00 41.13 ? 15  GLN J CD  1 
ATOM   10243 O  OE1 . GLN J  1 42  ? 34.350  65.605  -38.831 1.00 49.03 ? 15  GLN J OE1 1 
ATOM   10244 N  NE2 . GLN J  1 42  ? 34.796  67.659  -38.036 1.00 49.58 ? 15  GLN J NE2 1 
ATOM   10245 N  N   . GLY J  1 43  ? 31.828  65.311  -43.810 1.00 30.31 ? 16  GLY J N   1 
ATOM   10246 C  CA  . GLY J  1 43  ? 31.139  64.193  -44.419 1.00 34.69 ? 16  GLY J CA  1 
ATOM   10247 C  C   . GLY J  1 43  ? 32.014  63.454  -45.403 1.00 31.79 ? 16  GLY J C   1 
ATOM   10248 O  O   . GLY J  1 43  ? 33.054  63.956  -45.834 1.00 24.31 ? 16  GLY J O   1 
ATOM   10249 N  N   . ILE J  1 44  ? 31.595  62.228  -45.706 1.00 30.59 ? 17  ILE J N   1 
ATOM   10250 C  CA  . ILE J  1 44  ? 32.159  61.401  -46.767 1.00 31.68 ? 17  ILE J CA  1 
ATOM   10251 C  C   . ILE J  1 44  ? 31.040  61.005  -47.709 1.00 32.45 ? 17  ILE J C   1 
ATOM   10252 O  O   . ILE J  1 44  ? 30.048  60.398  -47.283 1.00 31.84 ? 17  ILE J O   1 
ATOM   10253 C  CB  . ILE J  1 44  ? 32.865  60.149  -46.228 1.00 30.69 ? 17  ILE J CB  1 
ATOM   10254 C  CG1 . ILE J  1 44  ? 33.993  60.523  -45.272 1.00 30.02 ? 17  ILE J CG1 1 
ATOM   10255 C  CG2 . ILE J  1 44  ? 33.281  59.234  -47.379 1.00 33.17 ? 17  ILE J CG2 1 
ATOM   10256 C  CD1 . ILE J  1 44  ? 34.579  59.333  -44.560 1.00 36.71 ? 17  ILE J CD1 1 
ATOM   10257 N  N   . ILE J  1 45  ? 31.220  61.313  -48.990 1.00 34.06 ? 18  ILE J N   1 
ATOM   10258 C  CA  . ILE J  1 45  ? 30.267  60.987  -50.041 1.00 28.83 ? 18  ILE J CA  1 
ATOM   10259 C  C   . ILE J  1 45  ? 30.969  60.090  -51.049 1.00 35.00 ? 18  ILE J C   1 
ATOM   10260 O  O   . ILE J  1 45  ? 32.082  60.406  -51.494 1.00 28.19 ? 18  ILE J O   1 
ATOM   10261 C  CB  . ILE J  1 45  ? 29.738  62.258  -50.724 1.00 29.88 ? 18  ILE J CB  1 
ATOM   10262 C  CG1 . ILE J  1 45  ? 28.999  63.129  -49.711 1.00 30.61 ? 18  ILE J CG1 1 
ATOM   10263 C  CG2 . ILE J  1 45  ? 28.795  61.904  -51.838 1.00 26.16 ? 18  ILE J CG2 1 
ATOM   10264 C  CD1 . ILE J  1 45  ? 27.778  62.437  -49.082 1.00 29.69 ? 18  ILE J CD1 1 
ATOM   10265 N  N   . ASN J  1 46  ? 30.326  58.976  -51.403 1.00 31.17 ? 19  ASN J N   1 
ATOM   10266 C  CA  . ASN J  1 46  ? 30.854  58.021  -52.363 1.00 35.25 ? 19  ASN J CA  1 
ATOM   10267 C  C   . ASN J  1 46  ? 30.089  58.091  -53.682 1.00 33.16 ? 19  ASN J C   1 
ATOM   10268 O  O   . ASN J  1 46  ? 28.884  58.359  -53.710 1.00 33.93 ? 19  ASN J O   1 
ATOM   10269 C  CB  . ASN J  1 46  ? 30.796  56.591  -51.814 1.00 29.84 ? 19  ASN J CB  1 
ATOM   10270 C  CG  . ASN J  1 46  ? 31.372  56.475  -50.413 1.00 35.97 ? 19  ASN J CG  1 
ATOM   10271 O  OD1 . ASN J  1 46  ? 32.582  56.316  -50.245 1.00 44.89 ? 19  ASN J OD1 1 
ATOM   10272 N  ND2 . ASN J  1 46  ? 30.503  56.498  -49.401 1.00 36.87 ? 19  ASN J ND2 1 
ATOM   10273 N  N   . PHE J  1 47  ? 30.803  57.823  -54.780 1.00 32.58 ? 20  PHE J N   1 
ATOM   10274 C  CA  . PHE J  1 47  ? 30.248  57.810  -56.127 1.00 33.07 ? 20  PHE J CA  1 
ATOM   10275 C  C   . PHE J  1 47  ? 30.558  56.480  -56.799 1.00 31.36 ? 20  PHE J C   1 
ATOM   10276 O  O   . PHE J  1 47  ? 31.664  55.947  -56.653 1.00 33.71 ? 20  PHE J O   1 
ATOM   10277 C  CB  . PHE J  1 47  ? 30.830  58.945  -56.975 1.00 32.21 ? 20  PHE J CB  1 
ATOM   10278 C  CG  . PHE J  1 47  ? 30.521  60.314  -56.452 1.00 27.66 ? 20  PHE J CG  1 
ATOM   10279 C  CD1 . PHE J  1 47  ? 31.359  60.928  -55.532 1.00 32.14 ? 20  PHE J CD1 1 
ATOM   10280 C  CD2 . PHE J  1 47  ? 29.420  61.001  -56.908 1.00 28.22 ? 20  PHE J CD2 1 
ATOM   10281 C  CE1 . PHE J  1 47  ? 31.078  62.201  -55.064 1.00 29.12 ? 20  PHE J CE1 1 
ATOM   10282 C  CE2 . PHE J  1 47  ? 29.135  62.272  -56.443 1.00 36.30 ? 20  PHE J CE2 1 
ATOM   10283 C  CZ  . PHE J  1 47  ? 29.967  62.867  -55.518 1.00 28.73 ? 20  PHE J CZ  1 
ATOM   10284 N  N   . GLU J  1 48  ? 29.587  55.941  -57.537 1.00 34.92 ? 21  GLU J N   1 
ATOM   10285 C  CA  . GLU J  1 48  ? 29.837  54.715  -58.287 1.00 40.40 ? 21  GLU J CA  1 
ATOM   10286 C  C   . GLU J  1 48  ? 29.042  54.720  -59.587 1.00 39.68 ? 21  GLU J C   1 
ATOM   10287 O  O   . GLU J  1 48  ? 27.842  55.020  -59.595 1.00 37.11 ? 21  GLU J O   1 
ATOM   10288 C  CB  . GLU J  1 48  ? 29.503  53.474  -57.453 1.00 39.08 ? 21  GLU J CB  1 
ATOM   10289 C  CG  . GLU J  1 48  ? 29.637  52.174  -58.222 1.00 51.33 ? 21  GLU J CG  1 
ATOM   10290 C  CD  . GLU J  1 48  ? 30.125  51.016  -57.371 1.00 54.92 ? 21  GLU J CD  1 
ATOM   10291 O  OE1 . GLU J  1 48  ? 29.430  50.647  -56.399 1.00 61.01 ? 21  GLU J OE1 1 
ATOM   10292 O  OE2 . GLU J  1 48  ? 31.191  50.452  -57.698 1.00 63.68 ? 21  GLU J OE2 1 
ATOM   10293 N  N   . GLN J  1 49  ? 29.729  54.387  -60.685 1.00 40.08 ? 22  GLN J N   1 
ATOM   10294 C  CA  . GLN J  1 49  ? 29.152  54.346  -62.033 1.00 42.49 ? 22  GLN J CA  1 
ATOM   10295 C  C   . GLN J  1 49  ? 29.704  53.092  -62.709 1.00 46.84 ? 22  GLN J C   1 
ATOM   10296 O  O   . GLN J  1 49  ? 30.758  53.131  -63.347 1.00 45.09 ? 22  GLN J O   1 
ATOM   10297 C  CB  . GLN J  1 49  ? 29.482  55.603  -62.821 1.00 38.00 ? 22  GLN J CB  1 
ATOM   10298 C  CG  . GLN J  1 49  ? 28.707  55.752  -64.137 1.00 39.88 ? 22  GLN J CG  1 
ATOM   10299 C  CD  . GLN J  1 49  ? 29.065  57.031  -64.874 1.00 43.48 ? 22  GLN J CD  1 
ATOM   10300 O  OE1 . GLN J  1 49  ? 30.209  57.484  -64.824 1.00 44.54 ? 22  GLN J OE1 1 
ATOM   10301 N  NE2 . GLN J  1 49  ? 28.087  57.620  -65.563 1.00 41.90 ? 22  GLN J NE2 1 
ATOM   10302 N  N   . LYS J  1 50  ? 29.002  51.977  -62.520 1.00 49.64 ? 23  LYS J N   1 
ATOM   10303 C  CA  . LYS J  1 50  ? 29.456  50.658  -63.033 1.00 57.24 ? 23  LYS J CA  1 
ATOM   10304 C  C   . LYS J  1 50  ? 29.413  50.601  -64.566 1.00 50.58 ? 23  LYS J C   1 
ATOM   10305 O  O   . LYS J  1 50  ? 30.196  49.831  -65.122 1.00 59.38 ? 23  LYS J O   1 
ATOM   10306 C  CB  . LYS J  1 50  ? 28.696  49.517  -62.347 1.00 52.76 ? 23  LYS J CB  1 
ATOM   10307 C  CG  . LYS J  1 50  ? 29.413  48.898  -61.153 1.00 52.29 ? 23  LYS J CG  1 
ATOM   10308 C  CD  . LYS J  1 50  ? 28.524  48.617  -59.959 1.00 51.99 ? 23  LYS J CD  1 
ATOM   10309 C  CE  . LYS J  1 50  ? 27.383  47.669  -60.256 1.00 57.92 ? 23  LYS J CE  1 
ATOM   10310 N  NZ  . LYS J  1 50  ? 26.613  47.316  -59.040 1.00 64.52 ? 23  LYS J NZ  1 
ATOM   10311 N  N   . GLU J  1 51  ? 28.554  51.383  -65.214 1.00 45.82 ? 24  GLU J N   1 
ATOM   10312 C  CA  . GLU J  1 51  ? 28.492  51.361  -66.698 1.00 45.71 ? 24  GLU J CA  1 
ATOM   10313 C  C   . GLU J  1 51  ? 28.820  52.746  -67.253 1.00 52.84 ? 24  GLU J C   1 
ATOM   10314 O  O   . GLU J  1 51  ? 28.225  53.718  -66.784 1.00 53.80 ? 24  GLU J O   1 
ATOM   10315 C  CB  . GLU J  1 51  ? 27.117  50.914  -67.199 1.00 44.29 ? 24  GLU J CB  1 
ATOM   10316 C  CG  . GLU J  1 51  ? 26.750  49.486  -66.826 1.00 35.11 ? 24  GLU J CG  1 
ATOM   10317 C  CD  . GLU J  1 51  ? 27.603  48.393  -67.451 1.00 33.29 ? 24  GLU J CD  1 
ATOM   10318 O  OE1 . GLU J  1 51  ? 27.804  48.430  -68.678 1.00 33.31 ? 24  GLU J OE1 1 
ATOM   10319 O  OE2 . GLU J  1 51  ? 28.063  47.513  -66.712 1.00 32.71 ? 24  GLU J OE2 1 
ATOM   10320 N  N   . SER J  1 52  ? 29.720  52.801  -68.236 1.00 52.99 ? 25  SER J N   1 
ATOM   10321 C  CA  . SER J  1 52  ? 30.137  54.066  -68.889 1.00 52.88 ? 25  SER J CA  1 
ATOM   10322 C  C   . SER J  1 52  ? 28.884  54.819  -69.313 1.00 55.02 ? 25  SER J C   1 
ATOM   10323 O  O   . SER J  1 52  ? 28.045  54.248  -69.991 1.00 67.08 ? 25  SER J O   1 
ATOM   10324 C  CB  . SER J  1 52  ? 31.032  53.809  -70.069 1.00 54.04 ? 25  SER J CB  1 
ATOM   10325 O  OG  . SER J  1 52  ? 30.875  54.841  -71.029 1.00 60.39 ? 25  SER J OG  1 
ATOM   10326 N  N   . ASN J  1 53  ? 28.738  56.043  -68.830 1.00 51.09 ? 26  ASN J N   1 
ATOM   10327 C  CA  . ASN J  1 53  ? 27.556  56.910  -69.067 1.00 52.58 ? 26  ASN J CA  1 
ATOM   10328 C  C   . ASN J  1 53  ? 26.222  56.305  -68.595 1.00 51.09 ? 26  ASN J C   1 
ATOM   10329 O  O   . ASN J  1 53  ? 25.196  56.693  -69.149 1.00 59.04 ? 26  ASN J O   1 
ATOM   10330 C  CB  . ASN J  1 53  ? 27.473  57.587  -70.431 1.00 53.80 ? 26  ASN J CB  1 
ATOM   10331 C  CG  . ASN J  1 53  ? 26.489  58.739  -70.354 1.00 67.17 ? 26  ASN J CG  1 
ATOM   10332 O  OD1 . ASN J  1 53  ? 26.188  59.226  -69.264 1.00 66.72 ? 26  ASN J OD1 1 
ATOM   10333 N  ND2 . ASN J  1 53  ? 25.959  59.160  -71.490 1.00 63.27 ? 26  ASN J ND2 1 
ATOM   10334 N  N   . GLY J  1 54  ? 26.248  55.411  -67.609 1.00 49.38 ? 27  GLY J N   1 
ATOM   10335 C  CA  . GLY J  1 54  ? 25.033  54.909  -66.957 1.00 49.07 ? 27  GLY J CA  1 
ATOM   10336 C  C   . GLY J  1 54  ? 24.797  55.726  -65.693 1.00 51.02 ? 27  GLY J C   1 
ATOM   10337 O  O   . GLY J  1 54  ? 25.474  56.732  -65.494 1.00 47.25 ? 27  GLY J O   1 
ATOM   10338 N  N   . PRO J  1 55  ? 23.828  55.389  -64.828 1.00 51.22 ? 28  PRO J N   1 
ATOM   10339 C  CA  . PRO J  1 55  ? 23.628  56.159  -63.616 1.00 49.47 ? 28  PRO J CA  1 
ATOM   10340 C  C   . PRO J  1 55  ? 24.805  56.082  -62.634 1.00 40.22 ? 28  PRO J C   1 
ATOM   10341 O  O   . PRO J  1 55  ? 25.470  55.106  -62.573 1.00 39.02 ? 28  PRO J O   1 
ATOM   10342 C  CB  . PRO J  1 55  ? 22.402  55.497  -62.979 1.00 47.41 ? 28  PRO J CB  1 
ATOM   10343 C  CG  . PRO J  1 55  ? 22.343  54.133  -63.602 1.00 45.03 ? 28  PRO J CG  1 
ATOM   10344 C  CD  . PRO J  1 55  ? 22.851  54.333  -65.007 1.00 50.17 ? 28  PRO J CD  1 
ATOM   10345 N  N   . VAL J  1 56  ? 25.001  57.170  -61.901 1.00 43.82 ? 29  VAL J N   1 
ATOM   10346 C  CA  . VAL J  1 56  ? 25.980  57.297  -60.826 1.00 39.94 ? 29  VAL J CA  1 
ATOM   10347 C  C   . VAL J  1 56  ? 25.230  57.151  -59.508 1.00 36.85 ? 29  VAL J C   1 
ATOM   10348 O  O   . VAL J  1 56  ? 24.307  57.927  -59.233 1.00 34.92 ? 29  VAL J O   1 
ATOM   10349 C  CB  . VAL J  1 56  ? 26.703  58.653  -60.904 1.00 37.64 ? 29  VAL J CB  1 
ATOM   10350 C  CG1 . VAL J  1 56  ? 27.812  58.726  -59.874 1.00 39.06 ? 29  VAL J CG1 1 
ATOM   10351 C  CG2 . VAL J  1 56  ? 27.240  58.903  -62.321 1.00 32.23 ? 29  VAL J CG2 1 
ATOM   10352 N  N   . LYS J  1 57  ? 25.587  56.158  -58.701 1.00 38.10 ? 30  LYS J N   1 
ATOM   10353 C  CA  . LYS J  1 57  ? 25.060  56.136  -57.343 1.00 38.54 ? 30  LYS J CA  1 
ATOM   10354 C  C   . LYS J  1 57  ? 25.895  57.060  -56.468 1.00 38.54 ? 30  LYS J C   1 
ATOM   10355 O  O   . LYS J  1 57  ? 27.122  57.096  -56.578 1.00 36.33 ? 30  LYS J O   1 
ATOM   10356 C  CB  . LYS J  1 57  ? 25.040  54.730  -56.722 1.00 41.02 ? 30  LYS J CB  1 
ATOM   10357 C  CG  . LYS J  1 57  ? 24.391  53.606  -57.544 1.00 49.43 ? 30  LYS J CG  1 
ATOM   10358 C  CD  . LYS J  1 57  ? 25.249  52.325  -57.545 1.00 56.28 ? 30  LYS J CD  1 
ATOM   10359 C  CE  . LYS J  1 57  ? 26.280  52.264  -58.668 1.00 58.25 ? 30  LYS J CE  1 
ATOM   10360 N  NZ  . LYS J  1 57  ? 25.739  52.147  -60.063 1.00 57.16 ? 30  LYS J NZ  1 
ATOM   10361 N  N   . VAL J  1 58  ? 25.216  57.828  -55.619 1.00 40.46 ? 31  VAL J N   1 
ATOM   10362 C  CA  . VAL J  1 58  ? 25.852  58.766  -54.700 1.00 37.55 ? 31  VAL J CA  1 
ATOM   10363 C  C   . VAL J  1 58  ? 25.357  58.431  -53.301 1.00 35.16 ? 31  VAL J C   1 
ATOM   10364 O  O   . VAL J  1 58  ? 24.148  58.463  -53.050 1.00 37.61 ? 31  VAL J O   1 
ATOM   10365 C  CB  . VAL J  1 58  ? 25.519  60.224  -55.054 1.00 35.37 ? 31  VAL J CB  1 
ATOM   10366 C  CG1 . VAL J  1 58  ? 26.259  61.204  -54.122 1.00 28.71 ? 31  VAL J CG1 1 
ATOM   10367 C  CG2 . VAL J  1 58  ? 25.847  60.507  -56.501 1.00 36.31 ? 31  VAL J CG2 1 
ATOM   10368 N  N   . TRP J  1 59  ? 26.274  58.111  -52.391 1.00 34.71 ? 32  TRP J N   1 
ATOM   10369 C  CA  . TRP J  1 59  ? 25.831  57.770  -51.044 1.00 33.77 ? 32  TRP J CA  1 
ATOM   10370 C  C   . TRP J  1 59  ? 26.892  58.126  -50.018 1.00 34.70 ? 32  TRP J C   1 
ATOM   10371 O  O   . TRP J  1 59  ? 28.083  58.219  -50.318 1.00 34.91 ? 32  TRP J O   1 
ATOM   10372 C  CB  . TRP J  1 59  ? 25.458  56.289  -50.923 1.00 32.35 ? 32  TRP J CB  1 
ATOM   10373 C  CG  . TRP J  1 59  ? 26.627  55.392  -50.847 1.00 36.49 ? 32  TRP J CG  1 
ATOM   10374 C  CD1 . TRP J  1 59  ? 27.186  54.846  -49.722 1.00 33.61 ? 32  TRP J CD1 1 
ATOM   10375 C  CD2 . TRP J  1 59  ? 27.386  54.903  -51.953 1.00 33.44 ? 32  TRP J CD2 1 
ATOM   10376 N  NE1 . TRP J  1 59  ? 28.260  54.055  -50.067 1.00 38.52 ? 32  TRP J NE1 1 
ATOM   10377 C  CE2 . TRP J  1 59  ? 28.400  54.074  -51.432 1.00 36.00 ? 32  TRP J CE2 1 
ATOM   10378 C  CE3 . TRP J  1 59  ? 27.309  55.091  -53.338 1.00 34.86 ? 32  TRP J CE3 1 
ATOM   10379 C  CZ2 . TRP J  1 59  ? 29.328  53.434  -52.247 1.00 39.86 ? 32  TRP J CZ2 1 
ATOM   10380 C  CZ3 . TRP J  1 59  ? 28.235  54.461  -54.145 1.00 41.68 ? 32  TRP J CZ3 1 
ATOM   10381 C  CH2 . TRP J  1 59  ? 29.232  53.638  -53.597 1.00 42.63 ? 32  TRP J CH2 1 
ATOM   10382 N  N   . GLY J  1 60  ? 26.437  58.307  -48.790 1.00 35.81 ? 33  GLY J N   1 
ATOM   10383 C  CA  . GLY J  1 60  ? 27.346  58.667  -47.725 1.00 27.38 ? 33  GLY J CA  1 
ATOM   10384 C  C   . GLY J  1 60  ? 26.579  59.357  -46.614 1.00 35.75 ? 33  GLY J C   1 
ATOM   10385 O  O   . GLY J  1 60  ? 25.375  59.157  -46.459 1.00 37.52 ? 33  GLY J O   1 
ATOM   10386 N  N   . SER J  1 61  ? 27.294  60.189  -45.874 1.00 31.81 ? 34  SER J N   1 
ATOM   10387 C  CA  . SER J  1 61  ? 26.719  60.788  -44.686 1.00 35.41 ? 34  SER J CA  1 
ATOM   10388 C  C   . SER J  1 61  ? 27.428  62.104  -44.420 1.00 37.26 ? 34  SER J C   1 
ATOM   10389 O  O   . SER J  1 61  ? 28.632  62.222  -44.664 1.00 33.82 ? 34  SER J O   1 
ATOM   10390 C  CB  . SER J  1 61  ? 26.848  59.832  -43.499 1.00 35.31 ? 34  SER J CB  1 
ATOM   10391 O  OG  . SER J  1 61  ? 26.154  60.325  -42.376 1.00 47.54 ? 34  SER J OG  1 
ATOM   10392 N  N   . ILE J  1 62  ? 26.665  63.095  -43.963 1.00 31.88 ? 35  ILE J N   1 
ATOM   10393 C  CA  . ILE J  1 62  ? 27.183  64.399  -43.568 1.00 29.85 ? 35  ILE J CA  1 
ATOM   10394 C  C   . ILE J  1 62  ? 26.674  64.699  -42.161 1.00 35.06 ? 35  ILE J C   1 
ATOM   10395 O  O   . ILE J  1 62  ? 25.478  64.556  -41.893 1.00 38.95 ? 35  ILE J O   1 
ATOM   10396 C  CB  . ILE J  1 62  ? 26.745  65.506  -44.544 1.00 28.21 ? 35  ILE J CB  1 
ATOM   10397 C  CG1 . ILE J  1 62  ? 27.014  65.063  -45.997 1.00 30.02 ? 35  ILE J CG1 1 
ATOM   10398 C  CG2 . ILE J  1 62  ? 27.450  66.803  -44.238 1.00 29.83 ? 35  ILE J CG2 1 
ATOM   10399 C  CD1 . ILE J  1 62  ? 26.549  66.046  -47.025 1.00 32.62 ? 35  ILE J CD1 1 
ATOM   10400 N  N   A LYS J  1 63  ? 27.573  65.116  -41.273 0.48 32.79 ? 36  LYS J N   1 
ATOM   10401 N  N   B LYS J  1 63  ? 27.574  65.118  -41.275 0.52 32.80 ? 36  LYS J N   1 
ATOM   10402 C  CA  A LYS J  1 63  ? 27.218  65.448  -39.898 0.48 32.40 ? 36  LYS J CA  1 
ATOM   10403 C  CA  B LYS J  1 63  ? 27.228  65.449  -39.898 0.52 32.38 ? 36  LYS J CA  1 
ATOM   10404 C  C   A LYS J  1 63  ? 27.599  66.892  -39.601 0.48 33.49 ? 36  LYS J C   1 
ATOM   10405 C  C   B LYS J  1 63  ? 27.597  66.898  -39.604 0.52 33.58 ? 36  LYS J C   1 
ATOM   10406 O  O   A LYS J  1 63  ? 28.361  67.518  -40.346 0.48 31.15 ? 36  LYS J O   1 
ATOM   10407 O  O   B LYS J  1 63  ? 28.346  67.532  -40.356 0.52 30.96 ? 36  LYS J O   1 
ATOM   10408 C  CB  A LYS J  1 63  ? 27.891  64.487  -38.905 0.48 31.97 ? 36  LYS J CB  1 
ATOM   10409 C  CB  B LYS J  1 63  ? 27.919  64.496  -38.910 0.52 31.87 ? 36  LYS J CB  1 
ATOM   10410 C  CG  A LYS J  1 63  ? 29.408  64.574  -38.851 0.48 32.77 ? 36  LYS J CG  1 
ATOM   10411 C  CG  B LYS J  1 63  ? 29.422  64.687  -38.762 0.52 32.44 ? 36  LYS J CG  1 
ATOM   10412 C  CD  A LYS J  1 63  ? 29.983  63.491  -37.936 0.48 35.37 ? 36  LYS J CD  1 
ATOM   10413 C  CD  B LYS J  1 63  ? 30.030  63.514  -37.989 0.52 35.37 ? 36  LYS J CD  1 
ATOM   10414 C  CE  A LYS J  1 63  ? 31.491  63.629  -37.795 0.48 35.23 ? 36  LYS J CE  1 
ATOM   10415 C  CE  B LYS J  1 63  ? 31.496  63.747  -37.657 0.52 35.45 ? 36  LYS J CE  1 
ATOM   10416 N  NZ  A LYS J  1 63  ? 31.876  64.998  -37.341 0.48 35.37 ? 36  LYS J NZ  1 
ATOM   10417 N  NZ  B LYS J  1 63  ? 32.126  62.524  -37.079 0.52 32.72 ? 36  LYS J NZ  1 
ATOM   10418 N  N   . GLY J  1 64  ? 27.030  67.440  -38.525 1.00 27.58 ? 37  GLY J N   1 
ATOM   10419 C  CA  . GLY J  1 64  ? 27.247  68.838  -38.174 1.00 24.23 ? 37  GLY J CA  1 
ATOM   10420 C  C   . GLY J  1 64  ? 26.333  69.860  -38.835 1.00 30.02 ? 37  GLY J C   1 
ATOM   10421 O  O   . GLY J  1 64  ? 26.636  71.062  -38.785 1.00 31.60 ? 37  GLY J O   1 
ATOM   10422 N  N   . LEU J  1 65  ? 25.242  69.431  -39.479 1.00 24.48 ? 38  LEU J N   1 
ATOM   10423 C  CA  . LEU J  1 65  ? 24.303  70.365  -40.086 1.00 27.27 ? 38  LEU J CA  1 
ATOM   10424 C  C   . LEU J  1 65  ? 23.191  70.739  -39.111 1.00 29.88 ? 38  LEU J C   1 
ATOM   10425 O  O   . LEU J  1 65  ? 22.964  70.069  -38.105 1.00 34.83 ? 38  LEU J O   1 
ATOM   10426 C  CB  . LEU J  1 65  ? 23.670  69.780  -41.355 1.00 30.18 ? 38  LEU J CB  1 
ATOM   10427 C  CG  . LEU J  1 65  ? 24.595  69.327  -42.478 1.00 35.17 ? 38  LEU J CG  1 
ATOM   10428 C  CD1 . LEU J  1 65  ? 23.963  68.256  -43.371 1.00 33.23 ? 38  LEU J CD1 1 
ATOM   10429 C  CD2 . LEU J  1 65  ? 25.013  70.550  -43.275 1.00 28.84 ? 38  LEU J CD2 1 
ATOM   10430 N  N   . THR J  1 66  ? 22.491  71.820  -39.431 1.00 33.97 ? 39  THR J N   1 
ATOM   10431 C  CA  . THR J  1 66  ? 21.234  72.128  -38.757 1.00 36.42 ? 39  THR J CA  1 
ATOM   10432 C  C   . THR J  1 66  ? 20.135  71.249  -39.339 1.00 38.98 ? 39  THR J C   1 
ATOM   10433 O  O   . THR J  1 66  ? 20.140  70.944  -40.536 1.00 35.68 ? 39  THR J O   1 
ATOM   10434 C  CB  . THR J  1 66  ? 20.872  73.600  -38.928 1.00 28.49 ? 39  THR J CB  1 
ATOM   10435 O  OG1 . THR J  1 66  ? 20.742  73.889  -40.325 1.00 39.44 ? 39  THR J OG1 1 
ATOM   10436 C  CG2 . THR J  1 66  ? 21.946  74.495  -38.355 1.00 31.45 ? 39  THR J CG2 1 
ATOM   10437 N  N   . GLU J  1 67  ? 19.209  70.816  -38.486 1.00 36.92 ? 40  GLU J N   1 
ATOM   10438 C  CA  . GLU J  1 67  ? 18.131  69.952  -38.955 1.00 33.04 ? 40  GLU J CA  1 
ATOM   10439 C  C   . GLU J  1 67  ? 17.384  70.618  -40.106 1.00 33.84 ? 40  GLU J C   1 
ATOM   10440 O  O   . GLU J  1 67  ? 17.158  71.833  -40.113 1.00 37.37 ? 40  GLU J O   1 
ATOM   10441 C  CB  . GLU J  1 67  ? 17.182  69.618  -37.799 1.00 40.93 ? 40  GLU J CB  1 
ATOM   10442 C  CG  . GLU J  1 67  ? 15.920  68.872  -38.204 1.00 37.99 ? 40  GLU J CG  1 
ATOM   10443 C  CD  . GLU J  1 67  ? 14.992  68.597  -37.023 1.00 52.71 ? 40  GLU J CD  1 
ATOM   10444 O  OE1 . GLU J  1 67  ? 15.040  69.351  -36.025 1.00 53.44 ? 40  GLU J OE1 1 
ATOM   10445 O  OE2 . GLU J  1 67  ? 14.211  67.617  -37.104 1.00 50.15 ? 40  GLU J OE2 1 
ATOM   10446 N  N   . GLY J  1 68  ? 17.066  69.823  -41.123 1.00 35.02 ? 41  GLY J N   1 
ATOM   10447 C  CA  . GLY J  1 68  ? 16.371  70.345  -42.282 1.00 40.18 ? 41  GLY J CA  1 
ATOM   10448 C  C   . GLY J  1 68  ? 17.126  70.143  -43.581 1.00 36.85 ? 41  GLY J C   1 
ATOM   10449 O  O   . GLY J  1 68  ? 18.081  69.357  -43.637 1.00 35.16 ? 41  GLY J O   1 
ATOM   10450 N  N   . LEU J  1 69  ? 16.711  70.866  -44.622 1.00 33.49 ? 42  LEU J N   1 
ATOM   10451 C  CA  . LEU J  1 69  ? 17.210  70.672  -45.979 1.00 36.35 ? 42  LEU J CA  1 
ATOM   10452 C  C   . LEU J  1 69  ? 18.361  71.618  -46.283 1.00 31.84 ? 42  LEU J C   1 
ATOM   10453 O  O   . LEU J  1 69  ? 18.324  72.801  -45.924 1.00 29.83 ? 42  LEU J O   1 
ATOM   10454 C  CB  . LEU J  1 69  ? 16.100  70.892  -47.018 1.00 31.16 ? 42  LEU J CB  1 
ATOM   10455 C  CG  . LEU J  1 69  ? 14.939  69.906  -47.026 1.00 34.71 ? 42  LEU J CG  1 
ATOM   10456 C  CD1 . LEU J  1 69  ? 14.082  70.110  -48.239 1.00 39.43 ? 42  LEU J CD1 1 
ATOM   10457 C  CD2 . LEU J  1 69  ? 15.510  68.525  -47.037 1.00 34.90 ? 42  LEU J CD2 1 
ATOM   10458 N  N   . HIS J  1 70  ? 19.365  71.093  -46.987 1.00 35.38 ? 43  HIS J N   1 
ATOM   10459 C  CA  . HIS J  1 70  ? 20.535  71.864  -47.389 1.00 31.89 ? 43  HIS J CA  1 
ATOM   10460 C  C   . HIS J  1 70  ? 20.859  71.556  -48.843 1.00 25.14 ? 43  HIS J C   1 
ATOM   10461 O  O   . HIS J  1 70  ? 20.920  70.382  -49.228 1.00 30.93 ? 43  HIS J O   1 
ATOM   10462 C  CB  . HIS J  1 70  ? 21.746  71.532  -46.507 1.00 31.13 ? 43  HIS J CB  1 
ATOM   10463 C  CG  . HIS J  1 70  ? 21.524  71.807  -45.053 1.00 29.86 ? 43  HIS J CG  1 
ATOM   10464 N  ND1 . HIS J  1 70  ? 21.713  73.053  -44.494 1.00 35.88 ? 43  HIS J ND1 1 
ATOM   10465 C  CD2 . HIS J  1 70  ? 21.082  71.009  -44.057 1.00 32.43 ? 43  HIS J CD2 1 
ATOM   10466 C  CE1 . HIS J  1 70  ? 21.416  73.005  -43.207 1.00 33.67 ? 43  HIS J CE1 1 
ATOM   10467 N  NE2 . HIS J  1 70  ? 21.033  71.775  -42.914 1.00 35.36 ? 43  HIS J NE2 1 
ATOM   10468 N  N   . GLY J  1 71  ? 21.097  72.605  -49.627 1.00 31.88 ? 44  GLY J N   1 
ATOM   10469 C  CA  . GLY J  1 71  ? 21.490  72.446  -51.017 1.00 34.58 ? 44  GLY J CA  1 
ATOM   10470 C  C   . GLY J  1 71  ? 22.755  71.625  -51.184 1.00 35.54 ? 44  GLY J C   1 
ATOM   10471 O  O   . GLY J  1 71  ? 23.633  71.633  -50.317 1.00 31.23 ? 44  GLY J O   1 
ATOM   10472 N  N   . PHE J  1 72  ? 22.859  70.909  -52.300 1.00 26.35 ? 45  PHE J N   1 
ATOM   10473 C  CA  . PHE J  1 72  ? 23.901  69.910  -52.510 1.00 24.19 ? 45  PHE J CA  1 
ATOM   10474 C  C   . PHE J  1 72  ? 24.272  70.006  -53.984 1.00 32.99 ? 45  PHE J C   1 
ATOM   10475 O  O   . PHE J  1 72  ? 23.468  69.621  -54.840 1.00 32.98 ? 45  PHE J O   1 
ATOM   10476 C  CB  . PHE J  1 72  ? 23.365  68.523  -52.160 1.00 23.74 ? 45  PHE J CB  1 
ATOM   10477 C  CG  . PHE J  1 72  ? 24.410  67.474  -51.908 1.00 30.94 ? 45  PHE J CG  1 
ATOM   10478 C  CD1 . PHE J  1 72  ? 25.568  67.752  -51.203 1.00 30.64 ? 45  PHE J CD1 1 
ATOM   10479 C  CD2 . PHE J  1 72  ? 24.205  66.174  -52.361 1.00 28.17 ? 45  PHE J CD2 1 
ATOM   10480 C  CE1 . PHE J  1 72  ? 26.507  66.745  -50.953 1.00 27.44 ? 45  PHE J CE1 1 
ATOM   10481 C  CE2 . PHE J  1 72  ? 25.129  65.174  -52.113 1.00 29.31 ? 45  PHE J CE2 1 
ATOM   10482 C  CZ  . PHE J  1 72  ? 26.281  65.459  -51.413 1.00 30.72 ? 45  PHE J CZ  1 
ATOM   10483 N  N   . HIS J  1 73  ? 25.454  70.538  -54.289 1.00 32.77 ? 46  HIS J N   1 
ATOM   10484 C  CA  . HIS J  1 73  ? 25.814  70.849  -55.670 1.00 31.30 ? 46  HIS J CA  1 
ATOM   10485 C  C   . HIS J  1 73  ? 27.262  70.485  -55.953 1.00 32.82 ? 46  HIS J C   1 
ATOM   10486 O  O   . HIS J  1 73  ? 28.129  70.565  -55.076 1.00 35.95 ? 46  HIS J O   1 
ATOM   10487 C  CB  . HIS J  1 73  ? 25.615  72.340  -55.975 1.00 25.61 ? 46  HIS J CB  1 
ATOM   10488 C  CG  . HIS J  1 73  ? 24.195  72.793  -55.863 1.00 43.84 ? 46  HIS J CG  1 
ATOM   10489 N  ND1 . HIS J  1 73  ? 23.268  72.596  -56.865 1.00 46.90 ? 46  HIS J ND1 1 
ATOM   10490 C  CD2 . HIS J  1 73  ? 23.528  73.386  -54.843 1.00 44.76 ? 46  HIS J CD2 1 
ATOM   10491 C  CE1 . HIS J  1 73  ? 22.099  73.078  -56.480 1.00 50.59 ? 46  HIS J CE1 1 
ATOM   10492 N  NE2 . HIS J  1 73  ? 22.228  73.556  -55.254 1.00 45.75 ? 46  HIS J NE2 1 
ATOM   10493 N  N   . VAL J  1 74  ? 27.517  70.104  -57.200 1.00 29.57 ? 47  VAL J N   1 
ATOM   10494 C  CA  . VAL J  1 74  ? 28.867  70.065  -57.736 1.00 26.52 ? 47  VAL J CA  1 
ATOM   10495 C  C   . VAL J  1 74  ? 29.172  71.431  -58.325 1.00 29.69 ? 47  VAL J C   1 
ATOM   10496 O  O   . VAL J  1 74  ? 28.418  71.941  -59.166 1.00 35.43 ? 47  VAL J O   1 
ATOM   10497 C  CB  . VAL J  1 74  ? 29.014  68.972  -58.807 1.00 30.70 ? 47  VAL J CB  1 
ATOM   10498 C  CG1 . VAL J  1 74  ? 30.434  68.990  -59.350 1.00 25.57 ? 47  VAL J CG1 1 
ATOM   10499 C  CG2 . VAL J  1 74  ? 28.667  67.611  -58.225 1.00 27.48 ? 47  VAL J CG2 1 
ATOM   10500 N  N   . HIS J  1 75  ? 30.275  72.028  -57.894 1.00 28.52 ? 48  HIS J N   1 
ATOM   10501 C  CA  . HIS J  1 75  ? 30.700  73.304  -58.441 1.00 28.80 ? 48  HIS J CA  1 
ATOM   10502 C  C   . HIS J  1 75  ? 31.861  73.087  -59.409 1.00 28.12 ? 48  HIS J C   1 
ATOM   10503 O  O   . HIS J  1 75  ? 32.516  72.040  -59.409 1.00 30.25 ? 48  HIS J O   1 
ATOM   10504 C  CB  . HIS J  1 75  ? 31.082  74.268  -57.317 1.00 27.29 ? 48  HIS J CB  1 
ATOM   10505 C  CG  . HIS J  1 75  ? 29.903  74.737  -56.520 1.00 25.46 ? 48  HIS J CG  1 
ATOM   10506 N  ND1 . HIS J  1 75  ? 29.561  76.064  -56.405 1.00 27.29 ? 48  HIS J ND1 1 
ATOM   10507 C  CD2 . HIS J  1 75  ? 28.972  74.048  -55.820 1.00 27.91 ? 48  HIS J CD2 1 
ATOM   10508 C  CE1 . HIS J  1 75  ? 28.489  76.175  -55.639 1.00 30.24 ? 48  HIS J CE1 1 
ATOM   10509 N  NE2 . HIS J  1 75  ? 28.104  74.964  -55.282 1.00 29.56 ? 48  HIS J NE2 1 
ATOM   10510 N  N   . GLU J  1 76  ? 32.104  74.100  -60.240 1.00 27.59 ? 49  GLU J N   1 
ATOM   10511 C  CA  . GLU J  1 76  ? 32.942  73.885  -61.414 1.00 34.80 ? 49  GLU J CA  1 
ATOM   10512 C  C   . GLU J  1 76  ? 34.391  73.557  -61.057 1.00 28.80 ? 49  GLU J C   1 
ATOM   10513 O  O   . GLU J  1 76  ? 34.984  72.663  -61.664 1.00 32.09 ? 49  GLU J O   1 
ATOM   10514 C  CB  . GLU J  1 76  ? 32.897  75.095  -62.335 1.00 32.55 ? 49  GLU J CB  1 
ATOM   10515 C  CG  . GLU J  1 76  ? 33.855  74.922  -63.498 1.00 45.25 ? 49  GLU J CG  1 
ATOM   10516 C  CD  . GLU J  1 76  ? 33.592  75.868  -64.639 1.00 54.36 ? 49  GLU J CD  1 
ATOM   10517 O  OE1 . GLU J  1 76  ? 33.741  75.439  -65.809 1.00 60.11 ? 49  GLU J OE1 1 
ATOM   10518 O  OE2 . GLU J  1 76  ? 33.227  77.033  -64.367 1.00 57.17 ? 49  GLU J OE2 1 
ATOM   10519 N  N   . PHE J  1 77  ? 34.998  74.270  -60.112 1.00 30.87 ? 50  PHE J N   1 
ATOM   10520 C  CA  . PHE J  1 77  ? 36.438  74.133  -59.907 1.00 27.36 ? 50  PHE J CA  1 
ATOM   10521 C  C   . PHE J  1 77  ? 36.776  73.322  -58.667 1.00 32.55 ? 50  PHE J C   1 
ATOM   10522 O  O   . PHE J  1 77  ? 36.115  73.433  -57.633 1.00 30.20 ? 50  PHE J O   1 
ATOM   10523 C  CB  . PHE J  1 77  ? 37.116  75.497  -59.826 1.00 29.10 ? 50  PHE J CB  1 
ATOM   10524 C  CG  . PHE J  1 77  ? 36.750  76.398  -60.953 1.00 32.93 ? 50  PHE J CG  1 
ATOM   10525 C  CD1 . PHE J  1 77  ? 37.045  76.035  -62.259 1.00 36.29 ? 50  PHE J CD1 1 
ATOM   10526 C  CD2 . PHE J  1 77  ? 36.094  77.595  -60.718 1.00 35.80 ? 50  PHE J CD2 1 
ATOM   10527 C  CE1 . PHE J  1 77  ? 36.699  76.860  -63.321 1.00 36.47 ? 50  PHE J CE1 1 
ATOM   10528 C  CE2 . PHE J  1 77  ? 35.745  78.421  -61.764 1.00 40.75 ? 50  PHE J CE2 1 
ATOM   10529 C  CZ  . PHE J  1 77  ? 36.045  78.047  -63.074 1.00 38.70 ? 50  PHE J CZ  1 
ATOM   10530 N  N   . GLY J  1 78  ? 37.829  72.521  -58.781 1.00 27.13 ? 51  GLY J N   1 
ATOM   10531 C  CA  . GLY J  1 78  ? 38.351  71.755  -57.672 1.00 23.38 ? 51  GLY J CA  1 
ATOM   10532 C  C   . GLY J  1 78  ? 39.381  72.563  -56.909 1.00 30.57 ? 51  GLY J C   1 
ATOM   10533 O  O   . GLY J  1 78  ? 40.415  72.040  -56.486 1.00 26.97 ? 51  GLY J O   1 
ATOM   10534 N  N   . ASP J  1 79  ? 39.107  73.853  -56.757 1.00 29.39 ? 52  ASP J N   1 
ATOM   10535 C  CA  . ASP J  1 79  ? 40.047  74.809  -56.188 1.00 23.31 ? 52  ASP J CA  1 
ATOM   10536 C  C   . ASP J  1 79  ? 39.572  75.100  -54.762 1.00 30.34 ? 52  ASP J C   1 
ATOM   10537 O  O   . ASP J  1 79  ? 38.498  75.679  -54.562 1.00 30.95 ? 52  ASP J O   1 
ATOM   10538 C  CB  . ASP J  1 79  ? 40.092  76.073  -57.047 1.00 33.67 ? 52  ASP J CB  1 
ATOM   10539 C  CG  . ASP J  1 79  ? 41.155  77.067  -56.600 1.00 34.64 ? 52  ASP J CG  1 
ATOM   10540 O  OD1 . ASP J  1 79  ? 41.560  77.055  -55.415 1.00 31.46 ? 52  ASP J OD1 1 
ATOM   10541 O  OD2 . ASP J  1 79  ? 41.602  77.848  -57.470 1.00 34.10 ? 52  ASP J OD2 1 
ATOM   10542 N  N   . ASN J  1 80  ? 40.369  74.696  -53.777 1.00 25.05 ? 53  ASN J N   1 
ATOM   10543 C  CA  . ASN J  1 80  ? 40.052  74.927  -52.369 1.00 29.76 ? 53  ASN J CA  1 
ATOM   10544 C  C   . ASN J  1 80  ? 40.963  75.977  -51.732 1.00 28.95 ? 53  ASN J C   1 
ATOM   10545 O  O   . ASN J  1 80  ? 40.996  76.097  -50.508 1.00 27.66 ? 53  ASN J O   1 
ATOM   10546 C  CB  . ASN J  1 80  ? 40.127  73.597  -51.611 1.00 31.31 ? 53  ASN J CB  1 
ATOM   10547 C  CG  . ASN J  1 80  ? 39.475  73.656  -50.231 1.00 48.48 ? 53  ASN J CG  1 
ATOM   10548 O  OD1 . ASN J  1 80  ? 38.378  74.197  -50.064 1.00 45.06 ? 53  ASN J OD1 1 
ATOM   10549 N  ND2 . ASN J  1 80  ? 40.157  73.093  -49.232 1.00 46.77 ? 53  ASN J ND2 1 
ATOM   10550 N  N   . THR J  1 81  ? 41.699  76.748  -52.536 1.00 25.36 ? 54  THR J N   1 
ATOM   10551 C  CA  . THR J  1 81  ? 42.684  77.674  -51.986 1.00 30.05 ? 54  THR J CA  1 
ATOM   10552 C  C   . THR J  1 81  ? 42.051  78.797  -51.172 1.00 30.84 ? 54  THR J C   1 
ATOM   10553 O  O   . THR J  1 81  ? 42.722  79.378  -50.317 1.00 36.58 ? 54  THR J O   1 
ATOM   10554 C  CB  . THR J  1 81  ? 43.551  78.277  -53.096 1.00 32.68 ? 54  THR J CB  1 
ATOM   10555 O  OG1 . THR J  1 81  ? 42.721  78.947  -54.047 1.00 31.80 ? 54  THR J OG1 1 
ATOM   10556 C  CG2 . THR J  1 81  ? 44.362  77.185  -53.810 1.00 26.63 ? 54  THR J CG2 1 
ATOM   10557 N  N   . ALA J  1 82  ? 40.792  79.137  -51.422 1.00 28.66 ? 55  ALA J N   1 
ATOM   10558 C  CA  . ALA J  1 82  ? 40.091  80.147  -50.636 1.00 33.98 ? 55  ALA J CA  1 
ATOM   10559 C  C   . ALA J  1 82  ? 38.910  79.523  -49.912 1.00 32.43 ? 55  ALA J C   1 
ATOM   10560 O  O   . ALA J  1 82  ? 37.829  80.103  -49.834 1.00 39.25 ? 55  ALA J O   1 
ATOM   10561 C  CB  . ALA J  1 82  ? 39.634  81.306  -51.518 1.00 30.23 ? 55  ALA J CB  1 
ATOM   10562 N  N   . GLY J  1 83  ? 39.098  78.309  -49.407 1.00 33.58 ? 56  GLY J N   1 
ATOM   10563 C  CA  . GLY J  1 83  ? 37.951  77.604  -48.879 1.00 32.37 ? 56  GLY J CA  1 
ATOM   10564 C  C   . GLY J  1 83  ? 36.968  77.242  -49.983 1.00 36.79 ? 56  GLY J C   1 
ATOM   10565 O  O   . GLY J  1 83  ? 37.320  77.076  -51.158 1.00 30.82 ? 56  GLY J O   1 
ATOM   10566 N  N   . CYS J  1 84  ? 35.703  77.125  -49.597 1.00 33.61 ? 57  CYS J N   1 
ATOM   10567 C  CA  . CYS J  1 84  ? 34.707  76.703  -50.566 1.00 33.10 ? 57  CYS J CA  1 
ATOM   10568 C  C   . CYS J  1 84  ? 34.369  77.799  -51.567 1.00 34.01 ? 57  CYS J C   1 
ATOM   10569 O  O   . CYS J  1 84  ? 33.738  77.505  -52.587 1.00 34.81 ? 57  CYS J O   1 
ATOM   10570 C  CB  . CYS J  1 84  ? 33.464  76.215  -49.820 1.00 32.94 ? 57  CYS J CB  1 
ATOM   10571 S  SG  . CYS J  1 84  ? 33.818  74.771  -48.769 1.00 46.70 ? 57  CYS J SG  1 
ATOM   10572 N  N   . THR J  1 85  ? 34.819  79.036  -51.329 1.00 33.32 ? 58  THR J N   1 
ATOM   10573 C  CA  . THR J  1 85  ? 34.556  80.129  -52.264 1.00 34.58 ? 58  THR J CA  1 
ATOM   10574 C  C   . THR J  1 85  ? 35.260  79.925  -53.604 1.00 34.52 ? 58  THR J C   1 
ATOM   10575 O  O   . THR J  1 85  ? 34.712  80.263  -54.660 1.00 33.60 ? 58  THR J O   1 
ATOM   10576 C  CB  . THR J  1 85  ? 34.973  81.465  -51.633 1.00 32.80 ? 58  THR J CB  1 
ATOM   10577 O  OG1 . THR J  1 85  ? 34.108  81.759  -50.535 1.00 44.85 ? 58  THR J OG1 1 
ATOM   10578 C  CG2 . THR J  1 85  ? 34.902  82.609  -52.636 1.00 38.55 ? 58  THR J CG2 1 
ATOM   10579 N  N   . SER J  1 86  ? 36.473  79.389  -53.599 1.00 30.14 ? 59  SER J N   1 
ATOM   10580 C  CA  . SER J  1 86  ? 37.177  79.284  -54.866 1.00 33.98 ? 59  SER J CA  1 
ATOM   10581 C  C   . SER J  1 86  ? 36.695  78.101  -55.717 1.00 28.70 ? 59  SER J C   1 
ATOM   10582 O  O   . SER J  1 86  ? 37.236  77.877  -56.802 1.00 29.25 ? 59  SER J O   1 
ATOM   10583 C  CB  . SER J  1 86  ? 38.689  79.216  -54.618 1.00 33.38 ? 59  SER J CB  1 
ATOM   10584 O  OG  . SER J  1 86  ? 38.974  78.495  -53.445 1.00 31.12 ? 59  SER J OG  1 
ATOM   10585 N  N   . ALA J  1 87  ? 35.672  77.364  -55.281 1.00 28.77 ? 60  ALA J N   1 
ATOM   10586 C  CA  . ALA J  1 87  ? 35.117  76.324  -56.139 1.00 26.39 ? 60  ALA J CA  1 
ATOM   10587 C  C   . ALA J  1 87  ? 34.306  76.893  -57.299 1.00 29.64 ? 60  ALA J C   1 
ATOM   10588 O  O   . ALA J  1 87  ? 33.915  76.132  -58.186 1.00 29.01 ? 60  ALA J O   1 
ATOM   10589 C  CB  . ALA J  1 87  ? 34.242  75.361  -55.331 1.00 24.06 ? 60  ALA J CB  1 
ATOM   10590 N  N   . GLY J  1 88  ? 34.017  78.193  -57.290 1.00 33.23 ? 61  GLY J N   1 
ATOM   10591 C  CA  . GLY J  1 88  ? 33.310  78.831  -58.372 1.00 38.02 ? 61  GLY J CA  1 
ATOM   10592 C  C   . GLY J  1 88  ? 31.824  78.541  -58.352 1.00 34.03 ? 61  GLY J C   1 
ATOM   10593 O  O   . GLY J  1 88  ? 31.266  78.087  -57.344 1.00 33.10 ? 61  GLY J O   1 
ATOM   10594 N  N   . PRO J  1 89  ? 31.157  78.778  -59.479 1.00 35.27 ? 62  PRO J N   1 
ATOM   10595 C  CA  . PRO J  1 89  ? 29.707  78.583  -59.554 1.00 32.84 ? 62  PRO J CA  1 
ATOM   10596 C  C   . PRO J  1 89  ? 29.369  77.114  -59.780 1.00 33.82 ? 62  PRO J C   1 
ATOM   10597 O  O   . PRO J  1 89  ? 30.242  76.252  -59.874 1.00 34.10 ? 62  PRO J O   1 
ATOM   10598 C  CB  . PRO J  1 89  ? 29.309  79.439  -60.755 1.00 37.11 ? 62  PRO J CB  1 
ATOM   10599 C  CG  . PRO J  1 89  ? 30.481  79.329  -61.656 1.00 34.50 ? 62  PRO J CG  1 
ATOM   10600 C  CD  . PRO J  1 89  ? 31.712  79.245  -60.763 1.00 35.70 ? 62  PRO J CD  1 
ATOM   10601 N  N   . HIS J  1 90  ? 28.067  76.853  -59.898 1.00 37.19 ? 63  HIS J N   1 
ATOM   10602 C  CA  . HIS J  1 90  ? 27.585  75.515  -60.206 1.00 37.09 ? 63  HIS J CA  1 
ATOM   10603 C  C   . HIS J  1 90  ? 28.204  74.998  -61.496 1.00 37.26 ? 63  HIS J C   1 
ATOM   10604 O  O   . HIS J  1 90  ? 28.467  75.759  -62.432 1.00 40.32 ? 63  HIS J O   1 
ATOM   10605 C  CB  . HIS J  1 90  ? 26.063  75.523  -60.334 1.00 41.73 ? 63  HIS J CB  1 
ATOM   10606 C  CG  . HIS J  1 90  ? 25.353  75.821  -59.054 1.00 42.90 ? 63  HIS J CG  1 
ATOM   10607 N  ND1 . HIS J  1 90  ? 24.000  76.079  -58.997 1.00 47.64 ? 63  HIS J ND1 1 
ATOM   10608 C  CD2 . HIS J  1 90  ? 25.807  75.904  -57.781 1.00 40.34 ? 63  HIS J CD2 1 
ATOM   10609 C  CE1 . HIS J  1 90  ? 23.651  76.307  -57.743 1.00 50.94 ? 63  HIS J CE1 1 
ATOM   10610 N  NE2 . HIS J  1 90  ? 24.729  76.209  -56.985 1.00 51.08 ? 63  HIS J NE2 1 
ATOM   10611 N  N   . PHE J  1 91  ? 28.456  73.696  -61.534 1.00 33.10 ? 64  PHE J N   1 
ATOM   10612 C  CA  . PHE J  1 91  ? 29.003  73.068  -62.731 1.00 38.99 ? 64  PHE J CA  1 
ATOM   10613 C  C   . PHE J  1 91  ? 27.920  73.047  -63.809 1.00 38.62 ? 64  PHE J C   1 
ATOM   10614 O  O   . PHE J  1 91  ? 26.912  72.347  -63.664 1.00 37.29 ? 64  PHE J O   1 
ATOM   10615 C  CB  . PHE J  1 91  ? 29.494  71.662  -62.397 1.00 34.29 ? 64  PHE J CB  1 
ATOM   10616 C  CG  . PHE J  1 91  ? 30.131  70.958  -63.550 1.00 37.35 ? 64  PHE J CG  1 
ATOM   10617 C  CD1 . PHE J  1 91  ? 30.971  71.642  -64.413 1.00 36.14 ? 64  PHE J CD1 1 
ATOM   10618 C  CD2 . PHE J  1 91  ? 29.895  69.609  -63.768 1.00 38.18 ? 64  PHE J CD2 1 
ATOM   10619 C  CE1 . PHE J  1 91  ? 31.557  70.998  -65.481 1.00 36.54 ? 64  PHE J CE1 1 
ATOM   10620 C  CE2 . PHE J  1 91  ? 30.480  68.955  -64.837 1.00 38.04 ? 64  PHE J CE2 1 
ATOM   10621 C  CZ  . PHE J  1 91  ? 31.318  69.651  -65.689 1.00 37.03 ? 64  PHE J CZ  1 
ATOM   10622 N  N   . ASN J  1 92  ? 28.114  73.818  -64.880 1.00 49.22 ? 65  ASN J N   1 
ATOM   10623 C  CA  . ASN J  1 92  ? 27.065  74.013  -65.885 1.00 41.29 ? 65  ASN J CA  1 
ATOM   10624 C  C   . ASN J  1 92  ? 27.672  74.157  -67.264 1.00 56.07 ? 65  ASN J C   1 
ATOM   10625 O  O   . ASN J  1 92  ? 27.901  75.276  -67.746 1.00 60.28 ? 65  ASN J O   1 
ATOM   10626 C  CB  . ASN J  1 92  ? 26.205  75.233  -65.570 1.00 42.02 ? 65  ASN J CB  1 
ATOM   10627 C  CG  . ASN J  1 92  ? 24.956  75.289  -66.421 1.00 47.85 ? 65  ASN J CG  1 
ATOM   10628 O  OD1 . ASN J  1 92  ? 24.638  74.338  -67.144 1.00 54.88 ? 65  ASN J OD1 1 
ATOM   10629 N  ND2 . ASN J  1 92  ? 24.235  76.399  -66.341 1.00 49.92 ? 65  ASN J ND2 1 
ATOM   10630 N  N   . PRO J  1 93  ? 27.942  73.037  -67.949 1.00 59.80 ? 66  PRO J N   1 
ATOM   10631 C  CA  . PRO J  1 93  ? 28.311  73.061  -69.370 1.00 56.38 ? 66  PRO J CA  1 
ATOM   10632 C  C   . PRO J  1 93  ? 27.087  73.042  -70.294 1.00 51.65 ? 66  PRO J C   1 
ATOM   10633 O  O   . PRO J  1 93  ? 26.618  74.097  -70.736 1.00 53.22 ? 66  PRO J O   1 
ATOM   10634 C  CB  . PRO J  1 93  ? 29.135  71.785  -69.531 1.00 50.30 ? 66  PRO J CB  1 
ATOM   10635 C  CG  . PRO J  1 93  ? 28.526  70.843  -68.539 1.00 40.21 ? 66  PRO J CG  1 
ATOM   10636 C  CD  . PRO J  1 93  ? 28.113  71.700  -67.355 1.00 46.31 ? 66  PRO J CD  1 
ATOM   10637 N  N   . ARG J  1 106 ? 18.291  73.889  -64.532 1.00 62.07 ? 79  ARG J N   1 
ATOM   10638 C  CA  . ARG J  1 106 ? 19.254  73.423  -63.538 1.00 55.47 ? 79  ARG J CA  1 
ATOM   10639 C  C   . ARG J  1 106 ? 20.667  73.394  -64.126 1.00 53.79 ? 79  ARG J C   1 
ATOM   10640 O  O   . ARG J  1 106 ? 21.038  74.262  -64.923 1.00 54.09 ? 79  ARG J O   1 
ATOM   10641 C  CB  . ARG J  1 106 ? 18.858  72.036  -63.024 1.00 51.40 ? 79  ARG J CB  1 
ATOM   10642 C  CG  . ARG J  1 106 ? 18.150  71.179  -64.067 1.00 54.92 ? 79  ARG J CG  1 
ATOM   10643 C  CD  . ARG J  1 106 ? 17.751  69.808  -63.514 1.00 55.36 ? 79  ARG J CD  1 
ATOM   10644 N  NE  . ARG J  1 106 ? 18.899  69.030  -63.056 1.00 65.10 ? 79  ARG J NE  1 
ATOM   10645 C  CZ  . ARG J  1 106 ? 19.843  68.537  -63.849 1.00 53.72 ? 79  ARG J CZ  1 
ATOM   10646 N  NH1 . ARG J  1 106 ? 19.807  68.712  -65.160 1.00 55.44 ? 79  ARG J NH1 1 
ATOM   10647 N  NH2 . ARG J  1 106 ? 20.846  67.847  -63.311 1.00 56.56 ? 79  ARG J NH2 1 
ATOM   10648 N  N   . HIS J  1 107 ? 21.448  72.393  -63.727 1.00 50.96 ? 80  HIS J N   1 
ATOM   10649 C  CA  . HIS J  1 107 ? 22.830  72.258  -64.168 1.00 43.59 ? 80  HIS J CA  1 
ATOM   10650 C  C   . HIS J  1 107 ? 23.288  70.838  -63.864 1.00 39.72 ? 80  HIS J C   1 
ATOM   10651 O  O   . HIS J  1 107 ? 22.598  70.077  -63.183 1.00 45.85 ? 80  HIS J O   1 
ATOM   10652 C  CB  . HIS J  1 107 ? 23.736  73.295  -63.490 1.00 49.84 ? 80  HIS J CB  1 
ATOM   10653 C  CG  . HIS J  1 107 ? 23.835  73.133  -62.002 1.00 52.39 ? 80  HIS J CG  1 
ATOM   10654 N  ND1 . HIS J  1 107 ? 24.812  72.368  -61.396 1.00 54.12 ? 80  HIS J ND1 1 
ATOM   10655 C  CD2 . HIS J  1 107 ? 23.075  73.636  -60.997 1.00 53.94 ? 80  HIS J CD2 1 
ATOM   10656 C  CE1 . HIS J  1 107 ? 24.652  72.411  -60.083 1.00 49.54 ? 80  HIS J CE1 1 
ATOM   10657 N  NE2 . HIS J  1 107 ? 23.603  73.170  -59.816 1.00 56.02 ? 80  HIS J NE2 1 
ATOM   10658 N  N   . VAL J  1 108 ? 24.478  70.493  -64.362 1.00 39.02 ? 81  VAL J N   1 
ATOM   10659 C  CA  . VAL J  1 108 ? 24.950  69.118  -64.222 1.00 35.87 ? 81  VAL J CA  1 
ATOM   10660 C  C   . VAL J  1 108 ? 25.170  68.765  -62.754 1.00 48.88 ? 81  VAL J C   1 
ATOM   10661 O  O   . VAL J  1 108 ? 24.754  67.696  -62.292 1.00 48.17 ? 81  VAL J O   1 
ATOM   10662 C  CB  . VAL J  1 108 ? 26.214  68.896  -65.069 1.00 30.65 ? 81  VAL J CB  1 
ATOM   10663 C  CG1 . VAL J  1 108 ? 26.701  67.473  -64.933 1.00 39.80 ? 81  VAL J CG1 1 
ATOM   10664 C  CG2 . VAL J  1 108 ? 25.899  69.168  -66.533 1.00 43.50 ? 81  VAL J CG2 1 
ATOM   10665 N  N   . GLY J  1 109 ? 25.794  69.651  -61.992 1.00 48.50 ? 82  GLY J N   1 
ATOM   10666 C  CA  . GLY J  1 109 ? 26.055  69.264  -60.613 1.00 49.92 ? 82  GLY J CA  1 
ATOM   10667 C  C   . GLY J  1 109 ? 24.895  69.306  -59.631 1.00 47.66 ? 82  GLY J C   1 
ATOM   10668 O  O   . GLY J  1 109 ? 25.124  69.130  -58.432 1.00 43.03 ? 82  GLY J O   1 
ATOM   10669 N  N   . ASP J  1 110 ? 23.660  69.516  -60.082 1.00 42.74 ? 83  ASP J N   1 
ATOM   10670 C  CA  . ASP J  1 110 ? 22.541  69.773  -59.179 1.00 45.19 ? 83  ASP J CA  1 
ATOM   10671 C  C   . ASP J  1 110 ? 22.075  68.443  -58.595 1.00 45.14 ? 83  ASP J C   1 
ATOM   10672 O  O   . ASP J  1 110 ? 21.428  67.649  -59.285 1.00 46.13 ? 83  ASP J O   1 
ATOM   10673 C  CB  . ASP J  1 110 ? 21.420  70.488  -59.933 1.00 46.44 ? 83  ASP J CB  1 
ATOM   10674 C  CG  . ASP J  1 110 ? 20.266  70.931  -59.032 1.00 60.56 ? 83  ASP J CG  1 
ATOM   10675 O  OD1 . ASP J  1 110 ? 20.033  70.325  -57.959 1.00 63.60 ? 83  ASP J OD1 1 
ATOM   10676 O  OD2 . ASP J  1 110 ? 19.592  71.923  -59.399 1.00 63.22 ? 83  ASP J OD2 1 
ATOM   10677 N  N   . LEU J  1 111 ? 22.398  68.191  -57.322 1.00 35.32 ? 84  LEU J N   1 
ATOM   10678 C  CA  . LEU J  1 111 ? 21.977  66.966  -56.653 1.00 35.37 ? 84  LEU J CA  1 
ATOM   10679 C  C   . LEU J  1 111 ? 20.857  67.203  -55.647 1.00 37.60 ? 84  LEU J C   1 
ATOM   10680 O  O   . LEU J  1 111 ? 20.615  66.352  -54.784 1.00 44.79 ? 84  LEU J O   1 
ATOM   10681 C  CB  . LEU J  1 111 ? 23.166  66.282  -55.975 1.00 32.66 ? 84  LEU J CB  1 
ATOM   10682 C  CG  . LEU J  1 111 ? 24.337  66.033  -56.923 1.00 37.09 ? 84  LEU J CG  1 
ATOM   10683 C  CD1 . LEU J  1 111 ? 25.545  65.511  -56.162 1.00 32.81 ? 84  LEU J CD1 1 
ATOM   10684 C  CD2 . LEU J  1 111 ? 23.905  65.046  -57.999 1.00 37.21 ? 84  LEU J CD2 1 
ATOM   10685 N  N   . GLY J  1 112 ? 20.182  68.347  -55.728 1.00 32.52 ? 85  GLY J N   1 
ATOM   10686 C  CA  . GLY J  1 112 ? 19.002  68.573  -54.924 1.00 34.36 ? 85  GLY J CA  1 
ATOM   10687 C  C   . GLY J  1 112 ? 19.324  69.061  -53.530 1.00 39.29 ? 85  GLY J C   1 
ATOM   10688 O  O   . GLY J  1 112 ? 20.144  69.969  -53.361 1.00 37.87 ? 85  GLY J O   1 
ATOM   10689 N  N   . ASN J  1 113 ? 18.653  68.488  -52.533 1.00 39.37 ? 86  ASN J N   1 
ATOM   10690 C  CA  . ASN J  1 113 ? 18.897  68.779  -51.127 1.00 34.67 ? 86  ASN J CA  1 
ATOM   10691 C  C   . ASN J  1 113 ? 19.236  67.494  -50.396 1.00 32.70 ? 86  ASN J C   1 
ATOM   10692 O  O   . ASN J  1 113 ? 18.694  66.432  -50.708 1.00 36.79 ? 86  ASN J O   1 
ATOM   10693 C  CB  . ASN J  1 113 ? 17.677  69.409  -50.449 1.00 36.92 ? 86  ASN J CB  1 
ATOM   10694 C  CG  . ASN J  1 113 ? 17.288  70.730  -51.053 1.00 41.29 ? 86  ASN J CG  1 
ATOM   10695 O  OD1 . ASN J  1 113 ? 18.098  71.658  -51.124 1.00 44.05 ? 86  ASN J OD1 1 
ATOM   10696 N  ND2 . ASN J  1 113 ? 16.029  70.842  -51.468 1.00 41.62 ? 86  ASN J ND2 1 
ATOM   10697 N  N   . VAL J  1 114 ? 20.121  67.592  -49.418 1.00 38.07 ? 87  VAL J N   1 
ATOM   10698 C  CA  . VAL J  1 114 ? 20.253  66.536  -48.434 1.00 32.99 ? 87  VAL J CA  1 
ATOM   10699 C  C   . VAL J  1 114 ? 19.411  66.924  -47.227 1.00 34.07 ? 87  VAL J C   1 
ATOM   10700 O  O   . VAL J  1 114 ? 19.140  68.104  -46.983 1.00 32.77 ? 87  VAL J O   1 
ATOM   10701 C  CB  . VAL J  1 114 ? 21.719  66.276  -48.037 1.00 32.74 ? 87  VAL J CB  1 
ATOM   10702 C  CG1 . VAL J  1 114 ? 22.556  66.001  -49.287 1.00 35.95 ? 87  VAL J CG1 1 
ATOM   10703 C  CG2 . VAL J  1 114 ? 22.279  67.458  -47.240 1.00 34.49 ? 87  VAL J CG2 1 
ATOM   10704 N  N   . THR J  1 115 ? 18.989  65.916  -46.465 1.00 35.38 ? 88  THR J N   1 
ATOM   10705 C  CA  . THR J  1 115 ? 18.084  66.103  -45.331 1.00 36.22 ? 88  THR J CA  1 
ATOM   10706 C  C   . THR J  1 115 ? 18.794  65.697  -44.048 1.00 31.76 ? 88  THR J C   1 
ATOM   10707 O  O   . THR J  1 115 ? 19.094  64.513  -43.844 1.00 34.68 ? 88  THR J O   1 
ATOM   10708 C  CB  . THR J  1 115 ? 16.802  65.286  -45.509 1.00 39.07 ? 88  THR J CB  1 
ATOM   10709 O  OG1 . THR J  1 115 ? 16.197  65.611  -46.764 1.00 45.97 ? 88  THR J OG1 1 
ATOM   10710 C  CG2 . THR J  1 115 ? 15.817  65.586  -44.379 1.00 33.31 ? 88  THR J CG2 1 
ATOM   10711 N  N   . ALA J  1 116 ? 19.037  66.675  -43.175 1.00 31.81 ? 89  ALA J N   1 
ATOM   10712 C  CA  . ALA J  1 116 ? 19.632  66.429  -41.866 1.00 33.41 ? 89  ALA J CA  1 
ATOM   10713 C  C   . ALA J  1 116 ? 18.543  66.134  -40.838 1.00 35.74 ? 89  ALA J C   1 
ATOM   10714 O  O   . ALA J  1 116 ? 17.574  66.892  -40.717 1.00 35.10 ? 89  ALA J O   1 
ATOM   10715 C  CB  . ALA J  1 116 ? 20.456  67.636  -41.411 1.00 32.76 ? 89  ALA J CB  1 
ATOM   10716 N  N   . ASP J  1 117 ? 18.717  65.044  -40.098 1.00 34.36 ? 90  ASP J N   1 
ATOM   10717 C  CA  . ASP J  1 117 ? 17.798  64.660  -39.037 1.00 37.73 ? 90  ASP J CA  1 
ATOM   10718 C  C   . ASP J  1 117 ? 17.984  65.584  -37.822 1.00 43.50 ? 90  ASP J C   1 
ATOM   10719 O  O   . ASP J  1 117 ? 18.746  66.557  -37.848 1.00 36.61 ? 90  ASP J O   1 
ATOM   10720 C  CB  . ASP J  1 117 ? 17.980  63.177  -38.703 1.00 32.71 ? 90  ASP J CB  1 
ATOM   10721 C  CG  . ASP J  1 117 ? 19.340  62.848  -38.051 1.00 40.38 ? 90  ASP J CG  1 
ATOM   10722 O  OD1 . ASP J  1 117 ? 20.070  63.749  -37.582 1.00 40.16 ? 90  ASP J OD1 1 
ATOM   10723 O  OD2 . ASP J  1 117 ? 19.684  61.650  -38.002 1.00 45.21 ? 90  ASP J OD2 1 
ATOM   10724 N  N   . LYS J  1 118 ? 17.266  65.277  -36.735 1.00 45.91 ? 91  LYS J N   1 
ATOM   10725 C  CA  . LYS J  1 118 ? 17.323  66.093  -35.523 1.00 41.82 ? 91  LYS J CA  1 
ATOM   10726 C  C   . LYS J  1 118 ? 18.707  66.084  -34.881 1.00 40.00 ? 91  LYS J C   1 
ATOM   10727 O  O   . LYS J  1 118 ? 19.020  66.979  -34.086 1.00 39.65 ? 91  LYS J O   1 
ATOM   10728 C  CB  . LYS J  1 118 ? 16.272  65.603  -34.514 1.00 37.59 ? 91  LYS J CB  1 
ATOM   10729 C  CG  . LYS J  1 118 ? 16.457  64.142  -34.103 1.00 40.00 ? 91  LYS J CG  1 
ATOM   10730 C  CD  . LYS J  1 118 ? 16.091  63.922  -32.635 1.00 53.86 ? 91  LYS J CD  1 
ATOM   10731 C  CE  . LYS J  1 118 ? 16.435  62.510  -32.158 1.00 48.80 ? 91  LYS J CE  1 
ATOM   10732 N  NZ  . LYS J  1 118 ? 16.465  62.430  -30.660 1.00 54.59 ? 91  LYS J NZ  1 
ATOM   10733 N  N   . ASP J  1 119 ? 19.539  65.097  -35.197 1.00 36.13 ? 92  ASP J N   1 
ATOM   10734 C  CA  . ASP J  1 119 ? 20.902  65.047  -34.689 1.00 33.21 ? 92  ASP J CA  1 
ATOM   10735 C  C   . ASP J  1 119 ? 21.901  65.727  -35.616 1.00 34.29 ? 92  ASP J C   1 
ATOM   10736 O  O   . ASP J  1 119 ? 23.111  65.620  -35.383 1.00 33.05 ? 92  ASP J O   1 
ATOM   10737 C  CB  . ASP J  1 119 ? 21.311  63.599  -34.440 1.00 31.37 ? 92  ASP J CB  1 
ATOM   10738 C  CG  . ASP J  1 119 ? 20.486  62.954  -33.332 1.00 57.53 ? 92  ASP J CG  1 
ATOM   10739 O  OD1 . ASP J  1 119 ? 20.067  63.686  -32.409 1.00 61.24 ? 92  ASP J OD1 1 
ATOM   10740 O  OD2 . ASP J  1 119 ? 20.251  61.727  -33.378 1.00 64.30 ? 92  ASP J OD2 1 
ATOM   10741 N  N   . GLY J  1 120 ? 21.421  66.432  -36.642 1.00 34.66 ? 93  GLY J N   1 
ATOM   10742 C  CA  . GLY J  1 120 ? 22.285  67.123  -37.587 1.00 34.10 ? 93  GLY J CA  1 
ATOM   10743 C  C   . GLY J  1 120 ? 22.979  66.239  -38.601 1.00 36.52 ? 93  GLY J C   1 
ATOM   10744 O  O   . GLY J  1 120 ? 23.955  66.676  -39.219 1.00 33.04 ? 93  GLY J O   1 
ATOM   10745 N  N   . VAL J  1 121 ? 22.509  65.006  -38.786 1.00 32.88 ? 94  VAL J N   1 
ATOM   10746 C  CA  . VAL J  1 121 ? 23.137  64.028  -39.665 1.00 31.48 ? 94  VAL J CA  1 
ATOM   10747 C  C   . VAL J  1 121 ? 22.251  63.835  -40.888 1.00 39.75 ? 94  VAL J C   1 
ATOM   10748 O  O   . VAL J  1 121 ? 21.047  63.570  -40.763 1.00 38.41 ? 94  VAL J O   1 
ATOM   10749 C  CB  . VAL J  1 121 ? 23.375  62.690  -38.943 1.00 34.15 ? 94  VAL J CB  1 
ATOM   10750 C  CG1 . VAL J  1 121 ? 23.891  61.629  -39.923 1.00 33.44 ? 94  VAL J CG1 1 
ATOM   10751 C  CG2 . VAL J  1 121 ? 24.346  62.878  -37.772 1.00 33.77 ? 94  VAL J CG2 1 
ATOM   10752 N  N   . ALA J  1 122 ? 22.839  63.972  -42.067 1.00 33.31 ? 95  ALA J N   1 
ATOM   10753 C  CA  . ALA J  1 122 ? 22.136  63.725  -43.316 1.00 37.14 ? 95  ALA J CA  1 
ATOM   10754 C  C   . ALA J  1 122 ? 22.696  62.452  -43.926 1.00 36.13 ? 95  ALA J C   1 
ATOM   10755 O  O   . ALA J  1 122 ? 23.888  62.384  -44.241 1.00 34.99 ? 95  ALA J O   1 
ATOM   10756 C  CB  . ALA J  1 122 ? 22.282  64.904  -44.278 1.00 32.91 ? 95  ALA J CB  1 
ATOM   10757 N  N   . ASP J  1 123 ? 21.851  61.440  -44.074 1.00 34.25 ? 96  ASP J N   1 
ATOM   10758 C  CA  . ASP J  1 123 ? 22.243  60.249  -44.810 1.00 39.15 ? 96  ASP J CA  1 
ATOM   10759 C  C   . ASP J  1 123 ? 21.869  60.459  -46.275 1.00 38.52 ? 96  ASP J C   1 
ATOM   10760 O  O   . ASP J  1 123 ? 20.775  60.946  -46.580 1.00 44.89 ? 96  ASP J O   1 
ATOM   10761 C  CB  . ASP J  1 123 ? 21.585  58.993  -44.232 1.00 41.61 ? 96  ASP J CB  1 
ATOM   10762 C  CG  . ASP J  1 123 ? 22.254  58.525  -42.934 1.00 53.07 ? 96  ASP J CG  1 
ATOM   10763 O  OD1 . ASP J  1 123 ? 23.470  58.780  -42.750 1.00 53.84 ? 96  ASP J OD1 1 
ATOM   10764 O  OD2 . ASP J  1 123 ? 21.572  57.883  -42.101 1.00 56.79 ? 96  ASP J OD2 1 
ATOM   10765 N  N   . VAL J  1 124 ? 22.799  60.151  -47.174 1.00 33.61 ? 97  VAL J N   1 
ATOM   10766 C  CA  . VAL J  1 124 ? 22.653  60.446  -48.595 1.00 38.12 ? 97  VAL J CA  1 
ATOM   10767 C  C   . VAL J  1 124 ? 22.601  59.130  -49.350 1.00 30.68 ? 97  VAL J C   1 
ATOM   10768 O  O   . VAL J  1 124 ? 23.453  58.259  -49.148 1.00 35.89 ? 97  VAL J O   1 
ATOM   10769 C  CB  . VAL J  1 124 ? 23.805  61.328  -49.110 1.00 40.69 ? 97  VAL J CB  1 
ATOM   10770 C  CG1 . VAL J  1 124 ? 23.731  61.488  -50.633 1.00 34.35 ? 97  VAL J CG1 1 
ATOM   10771 C  CG2 . VAL J  1 124 ? 23.798  62.679  -48.407 1.00 40.10 ? 97  VAL J CG2 1 
ATOM   10772 N  N   . SER J  1 125 ? 21.589  58.980  -50.206 1.00 37.20 ? 98  SER J N   1 
ATOM   10773 C  CA  . SER J  1 125 ? 21.469  57.799  -51.064 1.00 37.54 ? 98  SER J CA  1 
ATOM   10774 C  C   . SER J  1 125 ? 20.654  58.218  -52.287 1.00 46.02 ? 98  SER J C   1 
ATOM   10775 O  O   . SER J  1 125 ? 19.423  58.189  -52.272 1.00 50.65 ? 98  SER J O   1 
ATOM   10776 C  CB  . SER J  1 125 ? 20.839  56.615  -50.350 1.00 39.07 ? 98  SER J CB  1 
ATOM   10777 O  OG  . SER J  1 125 ? 21.153  55.414  -51.048 1.00 46.72 ? 98  SER J OG  1 
ATOM   10778 N  N   . ILE J  1 126 ? 21.367  58.585  -53.342 1.00 39.05 ? 99  ILE J N   1 
ATOM   10779 C  CA  . ILE J  1 126 ? 20.815  59.233  -54.519 1.00 36.83 ? 99  ILE J CA  1 
ATOM   10780 C  C   . ILE J  1 126 ? 21.308  58.460  -55.736 1.00 37.55 ? 99  ILE J C   1 
ATOM   10781 O  O   . ILE J  1 126 ? 22.369  57.830  -55.701 1.00 40.67 ? 99  ILE J O   1 
ATOM   10782 C  CB  . ILE J  1 126 ? 21.254  60.726  -54.558 1.00 41.81 ? 99  ILE J CB  1 
ATOM   10783 C  CG1 . ILE J  1 126 ? 20.446  61.562  -53.554 1.00 43.52 ? 99  ILE J CG1 1 
ATOM   10784 C  CG2 . ILE J  1 126 ? 21.196  61.331  -55.961 1.00 40.12 ? 99  ILE J CG2 1 
ATOM   10785 C  CD1 . ILE J  1 126 ? 18.987  61.134  -53.396 1.00 49.71 ? 99  ILE J CD1 1 
ATOM   10786 N  N   . GLU J  1 127 ? 20.506  58.459  -56.798 1.00 40.12 ? 100 GLU J N   1 
ATOM   10787 C  CA  . GLU J  1 127 ? 20.963  58.036  -58.114 1.00 45.12 ? 100 GLU J CA  1 
ATOM   10788 C  C   . GLU J  1 127 ? 20.769  59.195  -59.077 1.00 42.60 ? 100 GLU J C   1 
ATOM   10789 O  O   . GLU J  1 127 ? 19.726  59.857  -59.060 1.00 44.38 ? 100 GLU J O   1 
ATOM   10790 C  CB  . GLU J  1 127 ? 20.213  56.804  -58.620 1.00 49.55 ? 100 GLU J CB  1 
ATOM   10791 C  CG  . GLU J  1 127 ? 21.096  55.572  -58.716 1.00 49.20 ? 100 GLU J CG  1 
ATOM   10792 C  CD  . GLU J  1 127 ? 20.344  54.339  -59.182 1.00 59.40 ? 100 GLU J CD  1 
ATOM   10793 O  OE1 . GLU J  1 127 ? 20.849  53.217  -58.940 1.00 63.13 ? 100 GLU J OE1 1 
ATOM   10794 O  OE2 . GLU J  1 127 ? 19.264  54.486  -59.800 1.00 55.81 ? 100 GLU J OE2 1 
ATOM   10795 N  N   . ASP J  1 128 ? 21.783  59.462  -59.894 1.00 38.82 ? 101 ASP J N   1 
ATOM   10796 C  CA  . ASP J  1 128 ? 21.716  60.615  -60.777 1.00 41.31 ? 101 ASP J CA  1 
ATOM   10797 C  C   . ASP J  1 128 ? 22.307  60.259  -62.134 1.00 41.12 ? 101 ASP J C   1 
ATOM   10798 O  O   . ASP J  1 128 ? 23.406  59.702  -62.215 1.00 43.08 ? 101 ASP J O   1 
ATOM   10799 C  CB  . ASP J  1 128 ? 22.444  61.813  -60.159 1.00 43.38 ? 101 ASP J CB  1 
ATOM   10800 C  CG  . ASP J  1 128 ? 22.274  63.076  -60.980 1.00 48.03 ? 101 ASP J CG  1 
ATOM   10801 O  OD1 . ASP J  1 128 ? 22.721  63.101  -62.146 1.00 44.54 ? 101 ASP J OD1 1 
ATOM   10802 O  OD2 . ASP J  1 128 ? 21.679  64.044  -60.460 1.00 59.53 ? 101 ASP J OD2 1 
ATOM   10803 N  N   . SER J  1 129 ? 21.570  60.585  -63.197 1.00 45.48 ? 102 SER J N   1 
ATOM   10804 C  CA  . SER J  1 129 ? 21.956  60.217  -64.553 1.00 42.63 ? 102 SER J CA  1 
ATOM   10805 C  C   . SER J  1 129 ? 22.506  61.390  -65.350 1.00 45.52 ? 102 SER J C   1 
ATOM   10806 O  O   . SER J  1 129 ? 22.897  61.199  -66.505 1.00 50.23 ? 102 SER J O   1 
ATOM   10807 C  CB  . SER J  1 129 ? 20.763  59.612  -65.306 1.00 43.46 ? 102 SER J CB  1 
ATOM   10808 O  OG  . SER J  1 129 ? 19.585  60.374  -65.103 1.00 51.56 ? 102 SER J OG  1 
ATOM   10809 N  N   . VAL J  1 130 ? 22.539  62.592  -64.776 1.00 39.19 ? 103 VAL J N   1 
ATOM   10810 C  CA  . VAL J  1 130 ? 23.148  63.726  -65.466 1.00 40.31 ? 103 VAL J CA  1 
ATOM   10811 C  C   . VAL J  1 130 ? 24.644  63.827  -65.174 1.00 45.09 ? 103 VAL J C   1 
ATOM   10812 O  O   . VAL J  1 130 ? 25.446  64.044  -66.087 1.00 39.50 ? 103 VAL J O   1 
ATOM   10813 C  CB  . VAL J  1 130 ? 22.412  65.028  -65.109 1.00 39.40 ? 103 VAL J CB  1 
ATOM   10814 C  CG1 . VAL J  1 130 ? 23.026  66.200  -65.869 1.00 41.88 ? 103 VAL J CG1 1 
ATOM   10815 C  CG2 . VAL J  1 130 ? 20.931  64.895  -65.443 1.00 44.50 ? 103 VAL J CG2 1 
ATOM   10816 N  N   . ILE J  1 131 ? 25.063  63.685  -63.912 1.00 36.43 ? 104 ILE J N   1 
ATOM   10817 C  CA  . ILE J  1 131 ? 26.502  63.638  -63.643 1.00 36.23 ? 104 ILE J CA  1 
ATOM   10818 C  C   . ILE J  1 131 ? 27.094  62.357  -64.217 1.00 37.57 ? 104 ILE J C   1 
ATOM   10819 O  O   . ILE J  1 131 ? 26.390  61.390  -64.529 1.00 40.08 ? 104 ILE J O   1 
ATOM   10820 C  CB  . ILE J  1 131 ? 26.806  63.745  -62.138 1.00 36.08 ? 104 ILE J CB  1 
ATOM   10821 C  CG1 . ILE J  1 131 ? 26.425  62.432  -61.435 1.00 34.14 ? 104 ILE J CG1 1 
ATOM   10822 C  CG2 . ILE J  1 131 ? 26.128  64.973  -61.534 1.00 32.52 ? 104 ILE J CG2 1 
ATOM   10823 C  CD1 . ILE J  1 131 ? 26.401  62.503  -59.919 1.00 38.55 ? 104 ILE J CD1 1 
ATOM   10824 N  N   . SER J  1 132 ? 28.419  62.347  -64.336 1.00 36.42 ? 105 SER J N   1 
ATOM   10825 C  CA  . SER J  1 132 ? 29.140  61.148  -64.727 1.00 33.67 ? 105 SER J CA  1 
ATOM   10826 C  C   . SER J  1 132 ? 30.530  61.197  -64.113 1.00 35.01 ? 105 SER J C   1 
ATOM   10827 O  O   . SER J  1 132 ? 31.008  62.254  -63.690 1.00 37.14 ? 105 SER J O   1 
ATOM   10828 C  CB  . SER J  1 132 ? 29.225  61.011  -66.261 1.00 44.85 ? 105 SER J CB  1 
ATOM   10829 O  OG  . SER J  1 132 ? 29.913  59.826  -66.634 1.00 43.13 ? 105 SER J OG  1 
ATOM   10830 N  N   . LEU J  1 133 ? 31.171  60.035  -64.054 1.00 31.56 ? 106 LEU J N   1 
ATOM   10831 C  CA  . LEU J  1 133 ? 32.569  59.941  -63.665 1.00 35.70 ? 106 LEU J CA  1 
ATOM   10832 C  C   . LEU J  1 133 ? 33.517  59.972  -64.866 1.00 39.11 ? 106 LEU J C   1 
ATOM   10833 O  O   . LEU J  1 133 ? 34.717  59.729  -64.698 1.00 37.94 ? 106 LEU J O   1 
ATOM   10834 C  CB  . LEU J  1 133 ? 32.809  58.673  -62.843 1.00 33.21 ? 106 LEU J CB  1 
ATOM   10835 C  CG  . LEU J  1 133 ? 31.951  58.579  -61.580 1.00 39.26 ? 106 LEU J CG  1 
ATOM   10836 C  CD1 . LEU J  1 133 ? 32.487  57.486  -60.660 1.00 31.93 ? 106 LEU J CD1 1 
ATOM   10837 C  CD2 . LEU J  1 133 ? 31.901  59.933  -60.879 1.00 33.24 ? 106 LEU J CD2 1 
ATOM   10838 N  N   . SER J  1 134 ? 33.004  60.279  -66.056 1.00 42.08 ? 107 SER J N   1 
ATOM   10839 C  CA  . SER J  1 134 ? 33.803  60.347  -67.277 1.00 40.87 ? 107 SER J CA  1 
ATOM   10840 C  C   . SER J  1 134 ? 33.001  61.078  -68.346 1.00 41.76 ? 107 SER J C   1 
ATOM   10841 O  O   . SER J  1 134 ? 31.782  61.237  -68.231 1.00 42.80 ? 107 SER J O   1 
ATOM   10842 C  CB  . SER J  1 134 ? 34.181  58.954  -67.772 1.00 39.08 ? 107 SER J CB  1 
ATOM   10843 O  OG  . SER J  1 134 ? 33.028  58.329  -68.303 1.00 44.50 ? 107 SER J OG  1 
ATOM   10844 N  N   . GLY J  1 135 ? 33.697  61.519  -69.395 1.00 34.31 ? 108 GLY J N   1 
ATOM   10845 C  CA  . GLY J  1 135 ? 32.989  62.080  -70.530 1.00 36.36 ? 108 GLY J CA  1 
ATOM   10846 C  C   . GLY J  1 135 ? 32.621  63.538  -70.320 1.00 38.04 ? 108 GLY J C   1 
ATOM   10847 O  O   . GLY J  1 135 ? 33.270  64.265  -69.566 1.00 49.79 ? 108 GLY J O   1 
ATOM   10848 N  N   . ASP J  1 136 ? 31.550  63.963  -70.992 1.00 39.82 ? 109 ASP J N   1 
ATOM   10849 C  CA  . ASP J  1 136 ? 31.187  65.378  -70.974 1.00 49.63 ? 109 ASP J CA  1 
ATOM   10850 C  C   . ASP J  1 136 ? 30.898  65.849  -69.555 1.00 51.35 ? 109 ASP J C   1 
ATOM   10851 O  O   . ASP J  1 136 ? 31.370  66.910  -69.124 1.00 46.09 ? 109 ASP J O   1 
ATOM   10852 C  CB  . ASP J  1 136 ? 29.974  65.633  -71.874 1.00 44.81 ? 109 ASP J CB  1 
ATOM   10853 C  CG  . ASP J  1 136 ? 30.345  65.775  -73.347 1.00 51.81 ? 109 ASP J CG  1 
ATOM   10854 O  OD1 . ASP J  1 136 ? 31.537  65.998  -73.655 1.00 56.35 ? 109 ASP J OD1 1 
ATOM   10855 O  OD2 . ASP J  1 136 ? 29.441  65.642  -74.198 1.00 56.00 ? 109 ASP J OD2 1 
ATOM   10856 N  N   . HIS J  1 137 ? 30.125  65.066  -68.810 1.00 43.39 ? 110 HIS J N   1 
ATOM   10857 C  CA  . HIS J  1 137 ? 29.621  65.485  -67.512 1.00 41.40 ? 110 HIS J CA  1 
ATOM   10858 C  C   . HIS J  1 137 ? 30.473  64.959  -66.356 1.00 42.07 ? 110 HIS J C   1 
ATOM   10859 O  O   . HIS J  1 137 ? 29.967  64.783  -65.244 1.00 39.89 ? 110 HIS J O   1 
ATOM   10860 C  CB  . HIS J  1 137 ? 28.157  65.059  -67.388 1.00 41.43 ? 110 HIS J CB  1 
ATOM   10861 C  CG  . HIS J  1 137 ? 27.242  65.781  -68.337 1.00 41.71 ? 110 HIS J CG  1 
ATOM   10862 N  ND1 . HIS J  1 137 ? 25.867  65.664  -68.288 1.00 40.09 ? 110 HIS J ND1 1 
ATOM   10863 C  CD2 . HIS J  1 137 ? 27.505  66.661  -69.334 1.00 42.86 ? 110 HIS J CD2 1 
ATOM   10864 C  CE1 . HIS J  1 137 ? 25.324  66.421  -69.225 1.00 38.24 ? 110 HIS J CE1 1 
ATOM   10865 N  NE2 . HIS J  1 137 ? 26.297  67.037  -69.876 1.00 45.57 ? 110 HIS J NE2 1 
ATOM   10866 N  N   . CYS J  1 138 ? 31.768  64.750  -66.591 1.00 36.12 ? 111 CYS J N   1 
ATOM   10867 C  CA  . CYS J  1 138 ? 32.657  64.208  -65.568 1.00 41.74 ? 111 CYS J CA  1 
ATOM   10868 C  C   . CYS J  1 138 ? 32.813  65.188  -64.410 1.00 33.80 ? 111 CYS J C   1 
ATOM   10869 O  O   . CYS J  1 138 ? 33.108  66.369  -64.617 1.00 32.87 ? 111 CYS J O   1 
ATOM   10870 C  CB  . CYS J  1 138 ? 34.029  63.901  -66.160 1.00 32.63 ? 111 CYS J CB  1 
ATOM   10871 S  SG  . CYS J  1 138 ? 35.186  63.158  -65.001 1.00 44.79 ? 111 CYS J SG  1 
ATOM   10872 N  N   . ILE J  1 139 ? 32.638  64.688  -63.186 1.00 35.39 ? 112 ILE J N   1 
ATOM   10873 C  CA  . ILE J  1 139 ? 32.730  65.525  -61.995 1.00 29.97 ? 112 ILE J CA  1 
ATOM   10874 C  C   . ILE J  1 139 ? 34.016  65.298  -61.219 1.00 34.49 ? 112 ILE J C   1 
ATOM   10875 O  O   . ILE J  1 139 ? 34.234  65.963  -60.196 1.00 31.03 ? 112 ILE J O   1 
ATOM   10876 C  CB  . ILE J  1 139 ? 31.516  65.298  -61.075 1.00 32.46 ? 112 ILE J CB  1 
ATOM   10877 C  CG1 . ILE J  1 139 ? 31.548  63.869  -60.519 1.00 28.10 ? 112 ILE J CG1 1 
ATOM   10878 C  CG2 . ILE J  1 139 ? 30.229  65.602  -61.824 1.00 32.68 ? 112 ILE J CG2 1 
ATOM   10879 C  CD1 . ILE J  1 139 ? 30.408  63.529  -59.574 1.00 32.81 ? 112 ILE J CD1 1 
ATOM   10880 N  N   . ILE J  1 140 ? 34.873  64.376  -61.666 1.00 32.00 ? 113 ILE J N   1 
ATOM   10881 C  CA  . ILE J  1 140 ? 36.117  64.101  -60.957 1.00 30.96 ? 113 ILE J CA  1 
ATOM   10882 C  C   . ILE J  1 140 ? 37.017  65.327  -61.063 1.00 36.07 ? 113 ILE J C   1 
ATOM   10883 O  O   . ILE J  1 140 ? 37.119  65.947  -62.125 1.00 30.70 ? 113 ILE J O   1 
ATOM   10884 C  CB  . ILE J  1 140 ? 36.783  62.843  -61.530 1.00 33.38 ? 113 ILE J CB  1 
ATOM   10885 C  CG1 . ILE J  1 140 ? 36.121  61.602  -60.934 1.00 35.67 ? 113 ILE J CG1 1 
ATOM   10886 C  CG2 . ILE J  1 140 ? 38.266  62.798  -61.162 1.00 27.88 ? 113 ILE J CG2 1 
ATOM   10887 C  CD1 . ILE J  1 140 ? 36.606  60.309  -61.532 1.00 41.26 ? 113 ILE J CD1 1 
ATOM   10888 N  N   . GLY J  1 141 ? 37.627  65.730  -59.949 1.00 25.58 ? 114 GLY J N   1 
ATOM   10889 C  CA  . GLY J  1 141 ? 38.434  66.934  -59.957 1.00 23.22 ? 114 GLY J CA  1 
ATOM   10890 C  C   . GLY J  1 141 ? 37.662  68.218  -59.754 1.00 24.32 ? 114 GLY J C   1 
ATOM   10891 O  O   . GLY J  1 141 ? 38.266  69.297  -59.752 1.00 26.70 ? 114 GLY J O   1 
ATOM   10892 N  N   . ARG J  1 142 ? 36.350  68.144  -59.612 1.00 26.25 ? 115 ARG J N   1 
ATOM   10893 C  CA  . ARG J  1 142 ? 35.534  69.300  -59.287 1.00 23.94 ? 115 ARG J CA  1 
ATOM   10894 C  C   . ARG J  1 142 ? 35.203  69.248  -57.799 1.00 20.08 ? 115 ARG J C   1 
ATOM   10895 O  O   . ARG J  1 142 ? 35.653  68.350  -57.086 1.00 25.76 ? 115 ARG J O   1 
ATOM   10896 C  CB  . ARG J  1 142 ? 34.288  69.327  -60.168 1.00 26.28 ? 115 ARG J CB  1 
ATOM   10897 C  CG  . ARG J  1 142 ? 34.675  69.140  -61.648 1.00 28.50 ? 115 ARG J CG  1 
ATOM   10898 C  CD  . ARG J  1 142 ? 33.623  69.637  -62.594 1.00 35.87 ? 115 ARG J CD  1 
ATOM   10899 N  NE  . ARG J  1 142 ? 34.019  69.375  -63.975 1.00 37.21 ? 115 ARG J NE  1 
ATOM   10900 C  CZ  . ARG J  1 142 ? 34.674  70.232  -64.746 1.00 37.70 ? 115 ARG J CZ  1 
ATOM   10901 N  NH1 . ARG J  1 142 ? 34.997  71.444  -64.315 1.00 32.63 ? 115 ARG J NH1 1 
ATOM   10902 N  NH2 . ARG J  1 142 ? 35.000  69.869  -65.985 1.00 35.08 ? 115 ARG J NH2 1 
ATOM   10903 N  N   . THR J  1 143 ? 34.417  70.213  -57.322 1.00 23.64 ? 116 THR J N   1 
ATOM   10904 C  CA  . THR J  1 143 ? 34.159  70.340  -55.888 1.00 21.99 ? 116 THR J CA  1 
ATOM   10905 C  C   . THR J  1 143 ? 32.699  70.049  -55.572 1.00 28.71 ? 116 THR J C   1 
ATOM   10906 O  O   . THR J  1 143 ? 31.799  70.578  -56.230 1.00 33.05 ? 116 THR J O   1 
ATOM   10907 C  CB  . THR J  1 143 ? 34.538  71.733  -55.381 1.00 27.37 ? 116 THR J CB  1 
ATOM   10908 O  OG1 . THR J  1 143 ? 35.966  71.881  -55.445 1.00 26.40 ? 116 THR J OG1 1 
ATOM   10909 C  CG2 . THR J  1 143 ? 34.091  71.907  -53.926 1.00 28.55 ? 116 THR J CG2 1 
ATOM   10910 N  N   . LEU J  1 144 ? 32.471  69.199  -54.573 1.00 24.17 ? 117 LEU J N   1 
ATOM   10911 C  CA  . LEU J  1 144 ? 31.136  68.966  -54.034 1.00 22.76 ? 117 LEU J CA  1 
ATOM   10912 C  C   . LEU J  1 144 ? 30.930  69.916  -52.859 1.00 32.71 ? 117 LEU J C   1 
ATOM   10913 O  O   . LEU J  1 144 ? 31.797  70.006  -51.991 1.00 24.96 ? 117 LEU J O   1 
ATOM   10914 C  CB  . LEU J  1 144 ? 30.998  67.513  -53.580 1.00 23.64 ? 117 LEU J CB  1 
ATOM   10915 C  CG  . LEU J  1 144 ? 29.633  67.041  -53.080 1.00 27.65 ? 117 LEU J CG  1 
ATOM   10916 C  CD1 . LEU J  1 144 ? 28.617  67.116  -54.214 1.00 31.38 ? 117 LEU J CD1 1 
ATOM   10917 C  CD2 . LEU J  1 144 ? 29.737  65.627  -52.556 1.00 27.58 ? 117 LEU J CD2 1 
ATOM   10918 N  N   . VAL J  1 145 ? 29.801  70.627  -52.835 1.00 27.30 ? 118 VAL J N   1 
ATOM   10919 C  CA  . VAL J  1 145 ? 29.526  71.639  -51.818 1.00 32.11 ? 118 VAL J CA  1 
ATOM   10920 C  C   . VAL J  1 145 ? 28.190  71.338  -51.156 1.00 33.55 ? 118 VAL J C   1 
ATOM   10921 O  O   . VAL J  1 145 ? 27.224  70.955  -51.826 1.00 26.84 ? 118 VAL J O   1 
ATOM   10922 C  CB  . VAL J  1 145 ? 29.513  73.057  -52.422 1.00 29.43 ? 118 VAL J CB  1 
ATOM   10923 C  CG1 . VAL J  1 145 ? 29.241  74.103  -51.360 1.00 30.49 ? 118 VAL J CG1 1 
ATOM   10924 C  CG2 . VAL J  1 145 ? 30.842  73.339  -53.134 1.00 28.46 ? 118 VAL J CG2 1 
ATOM   10925 N  N   . VAL J  1 146 ? 28.132  71.500  -49.834 1.00 26.06 ? 119 VAL J N   1 
ATOM   10926 C  CA  . VAL J  1 146 ? 26.869  71.484  -49.109 1.00 29.95 ? 119 VAL J CA  1 
ATOM   10927 C  C   . VAL J  1 146 ? 26.595  72.906  -48.631 1.00 35.38 ? 119 VAL J C   1 
ATOM   10928 O  O   . VAL J  1 146 ? 27.491  73.576  -48.100 1.00 33.39 ? 119 VAL J O   1 
ATOM   10929 C  CB  . VAL J  1 146 ? 26.894  70.462  -47.961 1.00 34.90 ? 119 VAL J CB  1 
ATOM   10930 C  CG1 . VAL J  1 146 ? 28.069  70.728  -47.044 1.00 32.64 ? 119 VAL J CG1 1 
ATOM   10931 C  CG2 . VAL J  1 146 ? 25.575  70.481  -47.196 1.00 38.51 ? 119 VAL J CG2 1 
ATOM   10932 N  N   . HIS J  1 147 ? 25.378  73.388  -48.870 1.00 32.10 ? 120 HIS J N   1 
ATOM   10933 C  CA  . HIS J  1 147 ? 25.061  74.791  -48.658 1.00 31.67 ? 120 HIS J CA  1 
ATOM   10934 C  C   . HIS J  1 147 ? 24.265  74.987  -47.368 1.00 31.68 ? 120 HIS J C   1 
ATOM   10935 O  O   . HIS J  1 147 ? 23.676  74.053  -46.819 1.00 31.25 ? 120 HIS J O   1 
ATOM   10936 C  CB  . HIS J  1 147 ? 24.285  75.351  -49.849 1.00 33.52 ? 120 HIS J CB  1 
ATOM   10937 C  CG  . HIS J  1 147 ? 25.117  75.513  -51.086 1.00 34.31 ? 120 HIS J CG  1 
ATOM   10938 N  ND1 . HIS J  1 147 ? 25.592  76.736  -51.513 1.00 32.57 ? 120 HIS J ND1 1 
ATOM   10939 C  CD2 . HIS J  1 147 ? 25.573  74.600  -51.977 1.00 32.97 ? 120 HIS J CD2 1 
ATOM   10940 C  CE1 . HIS J  1 147 ? 26.293  76.570  -52.623 1.00 34.01 ? 120 HIS J CE1 1 
ATOM   10941 N  NE2 . HIS J  1 147 ? 26.301  75.282  -52.921 1.00 29.91 ? 120 HIS J NE2 1 
ATOM   10942 N  N   . GLU J  1 148 ? 24.277  76.213  -46.881 1.00 35.05 ? 121 GLU J N   1 
ATOM   10943 C  CA  . GLU J  1 148 ? 23.597  76.568  -45.618 1.00 40.30 ? 121 GLU J CA  1 
ATOM   10944 C  C   . GLU J  1 148 ? 22.087  76.399  -45.771 1.00 45.19 ? 121 GLU J C   1 
ATOM   10945 O  O   . GLU J  1 148 ? 21.485  75.750  -44.940 1.00 42.77 ? 121 GLU J O   1 
ATOM   10946 C  CB  . GLU J  1 148 ? 23.861  78.044  -45.365 1.00 37.67 ? 121 GLU J CB  1 
ATOM   10947 C  CG  . GLU J  1 148 ? 23.224  78.598  -44.118 1.00 43.27 ? 121 GLU J CG  1 
ATOM   10948 C  CD  . GLU J  1 148 ? 23.719  80.002  -43.833 1.00 53.00 ? 121 GLU J CD  1 
ATOM   10949 O  OE1 . GLU J  1 148 ? 23.785  80.803  -44.767 1.00 58.11 ? 121 GLU J OE1 1 
ATOM   10950 O  OE2 . GLU J  1 148 ? 24.049  80.279  -42.688 1.00 61.74 ? 121 GLU J OE2 1 
ATOM   10951 N  N   . LYS J  1 149 ? 21.544  76.939  -46.849 1.00 40.35 ? 122 LYS J N   1 
ATOM   10952 C  CA  . LYS J  1 149 ? 20.081  76.955  -47.027 1.00 47.68 ? 122 LYS J CA  1 
ATOM   10953 C  C   . LYS J  1 149 ? 19.628  75.878  -48.007 1.00 46.87 ? 122 LYS J C   1 
ATOM   10954 O  O   . LYS J  1 149 ? 20.422  75.394  -48.795 1.00 42.63 ? 122 LYS J O   1 
ATOM   10955 C  CB  . LYS J  1 149 ? 19.636  78.349  -47.476 1.00 45.45 ? 122 LYS J CB  1 
ATOM   10956 C  CG  . LYS J  1 149 ? 19.610  79.376  -46.354 1.00 49.85 ? 122 LYS J CG  1 
ATOM   10957 C  CD  . LYS J  1 149 ? 18.952  80.669  -46.715 1.00 53.09 ? 122 LYS J CD  1 
ATOM   10958 C  CE  . LYS J  1 149 ? 19.298  81.792  -45.760 1.00 52.99 ? 122 LYS J CE  1 
ATOM   10959 N  NZ  . LYS J  1 149 ? 18.698  83.078  -46.191 1.00 58.07 ? 122 LYS J NZ  1 
ATOM   10960 N  N   . ALA J  1 150 ? 18.347  75.555  -47.939 1.00 46.56 ? 123 ALA J N   1 
ATOM   10961 C  CA  . ALA J  1 150 ? 17.783  74.564  -48.864 1.00 43.74 ? 123 ALA J CA  1 
ATOM   10962 C  C   . ALA J  1 150 ? 17.700  75.194  -50.246 1.00 47.47 ? 123 ALA J C   1 
ATOM   10963 O  O   . ALA J  1 150 ? 17.524  76.403  -50.362 1.00 51.36 ? 123 ALA J O   1 
ATOM   10964 C  CB  . ALA J  1 150 ? 16.421  74.130  -48.404 1.00 42.33 ? 123 ALA J CB  1 
ATOM   10965 N  N   . ASP J  1 151 ? 17.919  74.380  -51.256 1.00 44.06 ? 124 ASP J N   1 
ATOM   10966 C  CA  . ASP J  1 151 ? 17.706  74.840  -52.612 1.00 50.38 ? 124 ASP J CA  1 
ATOM   10967 C  C   . ASP J  1 151 ? 16.243  74.566  -52.950 1.00 53.87 ? 124 ASP J C   1 
ATOM   10968 O  O   . ASP J  1 151 ? 15.788  73.418  -52.872 1.00 52.41 ? 124 ASP J O   1 
ATOM   10969 C  CB  . ASP J  1 151 ? 18.675  74.144  -53.565 1.00 48.30 ? 124 ASP J CB  1 
ATOM   10970 C  CG  . ASP J  1 151 ? 18.565  74.655  -54.978 1.00 59.87 ? 124 ASP J CG  1 
ATOM   10971 O  OD1 . ASP J  1 151 ? 17.457  74.594  -55.554 1.00 62.90 ? 124 ASP J OD1 1 
ATOM   10972 O  OD2 . ASP J  1 151 ? 19.585  75.153  -55.502 1.00 64.32 ? 124 ASP J OD2 1 
ATOM   10973 N  N   . ASP J  1 152 ? 15.492  75.631  -53.256 1.00 54.22 ? 125 ASP J N   1 
ATOM   10974 C  CA  . ASP J  1 152 ? 14.070  75.501  -53.568 1.00 59.99 ? 125 ASP J CA  1 
ATOM   10975 C  C   . ASP J  1 152 ? 13.818  75.008  -54.989 1.00 60.71 ? 125 ASP J C   1 
ATOM   10976 O  O   . ASP J  1 152 ? 12.695  74.574  -55.294 1.00 63.56 ? 125 ASP J O   1 
ATOM   10977 C  CB  . ASP J  1 152 ? 13.353  76.843  -53.359 1.00 51.14 ? 125 ASP J CB  1 
ATOM   10978 C  CG  . ASP J  1 152 ? 14.018  78.004  -54.119 1.00 69.15 ? 125 ASP J CG  1 
ATOM   10979 O  OD1 . ASP J  1 152 ? 14.494  77.803  -55.263 1.00 58.76 ? 125 ASP J OD1 1 
ATOM   10980 O  OD2 . ASP J  1 152 ? 14.042  79.135  -53.575 1.00 67.77 ? 125 ASP J OD2 1 
ATOM   10981 N  N   . LEU J  1 153 ? 14.833  75.069  -55.848 1.00 56.55 ? 126 LEU J N   1 
ATOM   10982 C  CA  . LEU J  1 153 ? 14.726  74.785  -57.280 1.00 59.41 ? 126 LEU J CA  1 
ATOM   10983 C  C   . LEU J  1 153 ? 13.672  75.688  -57.930 1.00 63.47 ? 126 LEU J C   1 
ATOM   10984 O  O   . LEU J  1 153 ? 13.920  76.878  -58.171 1.00 65.55 ? 126 LEU J O   1 
ATOM   10985 C  CB  . LEU J  1 153 ? 14.402  73.304  -57.522 1.00 55.87 ? 126 LEU J CB  1 
ATOM   10986 C  CG  . LEU J  1 153 ? 14.509  72.778  -58.958 0.00 55.41 ? 126 LEU J CG  1 
ATOM   10987 C  CD1 . LEU J  1 153 ? 15.597  73.538  -59.723 0.00 51.40 ? 126 LEU J CD1 1 
ATOM   10988 C  CD2 . LEU J  1 153 ? 14.793  71.268  -58.985 0.00 54.72 ? 126 LEU J CD2 1 
ATOM   10989 N  N   . SER J  1 169 ? 25.438  80.692  -47.793 1.00 48.97 ? 142 SER J N   1 
ATOM   10990 C  CA  . SER J  1 169 ? 26.860  80.395  -47.688 1.00 44.69 ? 142 SER J CA  1 
ATOM   10991 C  C   . SER J  1 169 ? 27.157  78.902  -47.872 1.00 40.71 ? 142 SER J C   1 
ATOM   10992 O  O   . SER J  1 169 ? 26.254  78.056  -47.844 1.00 39.79 ? 142 SER J O   1 
ATOM   10993 C  CB  . SER J  1 169 ? 27.397  80.878  -46.340 1.00 40.75 ? 142 SER J CB  1 
ATOM   10994 O  OG  . SER J  1 169 ? 27.244  79.880  -45.345 1.00 46.54 ? 142 SER J OG  1 
ATOM   10995 N  N   . ARG J  1 170 ? 28.440  78.590  -48.043 1.00 40.66 ? 143 ARG J N   1 
ATOM   10996 C  CA  . ARG J  1 170 ? 28.899  77.233  -48.303 1.00 35.87 ? 143 ARG J CA  1 
ATOM   10997 C  C   . ARG J  1 170 ? 29.477  76.662  -47.016 1.00 30.25 ? 143 ARG J C   1 
ATOM   10998 O  O   . ARG J  1 170 ? 30.483  77.169  -46.505 1.00 34.75 ? 143 ARG J O   1 
ATOM   10999 C  CB  . ARG J  1 170 ? 29.928  77.234  -49.432 1.00 29.76 ? 143 ARG J CB  1 
ATOM   11000 C  CG  . ARG J  1 170 ? 29.414  77.993  -50.683 1.00 31.40 ? 143 ARG J CG  1 
ATOM   11001 C  CD  . ARG J  1 170 ? 30.411  78.057  -51.827 1.00 33.29 ? 143 ARG J CD  1 
ATOM   11002 N  NE  . ARG J  1 170 ? 29.816  78.688  -53.003 1.00 36.87 ? 143 ARG J NE  1 
ATOM   11003 C  CZ  . ARG J  1 170 ? 30.397  78.797  -54.192 1.00 38.89 ? 143 ARG J CZ  1 
ATOM   11004 N  NH1 . ARG J  1 170 ? 31.615  78.325  -54.417 1.00 34.45 ? 143 ARG J NH1 1 
ATOM   11005 N  NH2 . ARG J  1 170 ? 29.734  79.388  -55.184 1.00 35.45 ? 143 ARG J NH2 1 
ATOM   11006 N  N   . LEU J  1 171 ? 28.858  75.591  -46.515 1.00 25.10 ? 144 LEU J N   1 
ATOM   11007 C  CA  . LEU J  1 171 ? 29.213  75.066  -45.199 1.00 29.78 ? 144 LEU J CA  1 
ATOM   11008 C  C   . LEU J  1 171 ? 30.422  74.141  -45.249 1.00 32.12 ? 144 LEU J C   1 
ATOM   11009 O  O   . LEU J  1 171 ? 31.254  74.154  -44.334 1.00 26.05 ? 144 LEU J O   1 
ATOM   11010 C  CB  . LEU J  1 171 ? 28.023  74.330  -44.587 1.00 31.78 ? 144 LEU J CB  1 
ATOM   11011 C  CG  . LEU J  1 171 ? 26.721  75.128  -44.432 1.00 34.78 ? 144 LEU J CG  1 
ATOM   11012 C  CD1 . LEU J  1 171 ? 25.680  74.277  -43.732 1.00 32.30 ? 144 LEU J CD1 1 
ATOM   11013 C  CD2 . LEU J  1 171 ? 26.955  76.410  -43.663 1.00 32.47 ? 144 LEU J CD2 1 
ATOM   11014 N  N   . ALA J  1 172 ? 30.529  73.311  -46.281 1.00 26.97 ? 145 ALA J N   1 
ATOM   11015 C  CA  . ALA J  1 172 ? 31.652  72.392  -46.385 1.00 26.76 ? 145 ALA J CA  1 
ATOM   11016 C  C   . ALA J  1 172 ? 31.794  71.986  -47.841 1.00 27.23 ? 145 ALA J C   1 
ATOM   11017 O  O   . ALA J  1 172 ? 30.843  72.087  -48.619 1.00 26.09 ? 145 ALA J O   1 
ATOM   11018 C  CB  . ALA J  1 172 ? 31.470  71.154  -45.504 1.00 24.56 ? 145 ALA J CB  1 
ATOM   11019 N  N   . CYS J  1 173 ? 32.990  71.528  -48.200 1.00 24.46 ? 146 CYS J N   1 
ATOM   11020 C  CA  . CYS J  1 173 ? 33.232  71.129  -49.584 1.00 24.33 ? 146 CYS J CA  1 
ATOM   11021 C  C   . CYS J  1 173 ? 34.455  70.232  -49.631 1.00 29.23 ? 146 CYS J C   1 
ATOM   11022 O  O   . CYS J  1 173 ? 35.223  70.139  -48.673 1.00 25.89 ? 146 CYS J O   1 
ATOM   11023 C  CB  . CYS J  1 173 ? 33.439  72.335  -50.497 1.00 27.74 ? 146 CYS J CB  1 
ATOM   11024 S  SG  . CYS J  1 173 ? 34.803  73.399  -49.989 1.00 34.66 ? 146 CYS J SG  1 
ATOM   11025 N  N   . GLY J  1 174 ? 34.640  69.588  -50.776 1.00 24.30 ? 147 GLY J N   1 
ATOM   11026 C  CA  . GLY J  1 174 ? 35.804  68.746  -50.963 1.00 24.52 ? 147 GLY J CA  1 
ATOM   11027 C  C   . GLY J  1 174 ? 35.979  68.481  -52.441 1.00 29.50 ? 147 GLY J C   1 
ATOM   11028 O  O   . GLY J  1 174 ? 35.024  68.565  -53.215 1.00 25.73 ? 147 GLY J O   1 
ATOM   11029 N  N   . VAL J  1 175 ? 37.208  68.182  -52.833 1.00 24.24 ? 148 VAL J N   1 
ATOM   11030 C  CA  . VAL J  1 175 ? 37.478  67.805  -54.220 1.00 22.40 ? 148 VAL J CA  1 
ATOM   11031 C  C   . VAL J  1 175 ? 37.046  66.357  -54.422 1.00 27.29 ? 148 VAL J C   1 
ATOM   11032 O  O   . VAL J  1 175 ? 37.338  65.484  -53.594 1.00 25.10 ? 148 VAL J O   1 
ATOM   11033 C  CB  . VAL J  1 175 ? 38.967  68.000  -54.558 1.00 24.00 ? 148 VAL J CB  1 
ATOM   11034 C  CG1 . VAL J  1 175 ? 39.189  67.845  -56.076 1.00 23.53 ? 148 VAL J CG1 1 
ATOM   11035 C  CG2 . VAL J  1 175 ? 39.434  69.356  -54.090 1.00 24.46 ? 148 VAL J CG2 1 
ATOM   11036 N  N   . ILE J  1 176 ? 36.337  66.104  -55.519 1.00 27.36 ? 149 ILE J N   1 
ATOM   11037 C  CA  . ILE J  1 176 ? 35.902  64.757  -55.875 1.00 23.23 ? 149 ILE J CA  1 
ATOM   11038 C  C   . ILE J  1 176 ? 37.075  64.008  -56.496 1.00 27.33 ? 149 ILE J C   1 
ATOM   11039 O  O   . ILE J  1 176 ? 37.612  64.423  -57.529 1.00 27.48 ? 149 ILE J O   1 
ATOM   11040 C  CB  . ILE J  1 176 ? 34.710  64.805  -56.838 1.00 23.31 ? 149 ILE J CB  1 
ATOM   11041 C  CG1 . ILE J  1 176 ? 33.553  65.594  -56.201 1.00 24.31 ? 149 ILE J CG1 1 
ATOM   11042 C  CG2 . ILE J  1 176 ? 34.331  63.397  -57.268 1.00 26.85 ? 149 ILE J CG2 1 
ATOM   11043 C  CD1 . ILE J  1 176 ? 32.447  66.019  -57.181 1.00 27.98 ? 149 ILE J CD1 1 
ATOM   11044 N  N   . GLY J  1 177 ? 37.474  62.906  -55.865 1.00 24.15 ? 150 GLY J N   1 
ATOM   11045 C  CA  . GLY J  1 177 ? 38.676  62.200  -56.252 1.00 24.16 ? 150 GLY J CA  1 
ATOM   11046 C  C   . GLY J  1 177 ? 38.422  60.765  -56.670 1.00 34.70 ? 150 GLY J C   1 
ATOM   11047 O  O   . GLY J  1 177 ? 37.420  60.163  -56.263 1.00 29.24 ? 150 GLY J O   1 
ATOM   11048 N  N   . ILE J  1 178 ? 39.329  60.201  -57.474 1.00 32.74 ? 151 ILE J N   1 
ATOM   11049 C  CA  . ILE J  1 178 ? 39.189  58.817  -57.918 1.00 26.65 ? 151 ILE J CA  1 
ATOM   11050 C  C   . ILE J  1 178 ? 39.422  57.880  -56.742 1.00 27.98 ? 151 ILE J C   1 
ATOM   11051 O  O   . ILE J  1 178 ? 40.392  58.027  -55.988 1.00 31.01 ? 151 ILE J O   1 
ATOM   11052 C  CB  . ILE J  1 178 ? 40.179  58.516  -59.052 1.00 26.69 ? 151 ILE J CB  1 
ATOM   11053 C  CG1 . ILE J  1 178 ? 40.025  59.554  -60.167 1.00 27.87 ? 151 ILE J CG1 1 
ATOM   11054 C  CG2 . ILE J  1 178 ? 39.941  57.116  -59.559 1.00 28.38 ? 151 ILE J CG2 1 
ATOM   11055 C  CD1 . ILE J  1 178 ? 41.065  59.452  -61.268 1.00 38.87 ? 151 ILE J CD1 1 
ATOM   11056 N  N   . ALA J  1 179 ? 38.546  56.897  -56.586 1.00 27.73 ? 152 ALA J N   1 
ATOM   11057 C  CA  . ALA J  1 179 ? 38.640  55.969  -55.475 1.00 33.44 ? 152 ALA J CA  1 
ATOM   11058 C  C   . ALA J  1 179 ? 38.916  54.562  -55.985 1.00 34.18 ? 152 ALA J C   1 
ATOM   11059 O  O   . ALA J  1 179 ? 38.727  54.253  -57.165 1.00 38.15 ? 152 ALA J O   1 
ATOM   11060 C  CB  . ALA J  1 179 ? 37.355  55.984  -54.628 1.00 33.39 ? 152 ALA J CB  1 
ATOM   11061 N  N   . GLN J  1 180 ? 39.371  53.714  -55.069 1.00 42.34 ? 153 GLN J N   1 
ATOM   11062 C  CA  . GLN J  1 180 ? 39.653  52.313  -55.360 1.00 43.77 ? 153 GLN J CA  1 
ATOM   11063 C  C   . GLN J  1 180 ? 38.364  51.560  -55.667 1.00 55.28 ? 153 GLN J C   1 
ATOM   11064 O  O   . GLN J  1 180 ? 37.718  51.021  -54.762 1.00 60.24 ? 153 GLN J O   1 
ATOM   11065 C  CB  . GLN J  1 180 ? 40.373  51.664  -54.178 1.00 49.09 ? 153 GLN J CB  1 
ATOM   11066 C  CG  . GLN J  1 180 ? 40.783  50.217  -54.386 1.00 48.30 ? 153 GLN J CG  1 
ATOM   11067 C  CD  . GLN J  1 180 ? 41.834  49.787  -53.380 1.00 55.87 ? 153 GLN J CD  1 
ATOM   11068 O  OE1 . GLN J  1 180 ? 41.743  50.117  -52.194 1.00 61.67 ? 153 GLN J OE1 1 
ATOM   11069 N  NE2 . GLN J  1 180 ? 42.843  49.058  -53.847 1.00 56.05 ? 153 GLN J NE2 1 
ATOM   11070 O  OXT . GLN J  1 180 ? 37.936  51.487  -56.822 1.00 61.91 ? 153 GLN J OXT 1 
HETATM 11071 ZN ZN  . ZN  K  2 .   ? 84.732  46.823  -13.011 1.00 54.63 ? 201 ZN  A ZN  1 
HETATM 11072 C  C1  . GOL L  3 .   ? 87.420  53.215  -21.588 1.00 49.36 ? 202 GOL A C1  1 
HETATM 11073 O  O1  . GOL L  3 .   ? 87.844  53.716  -20.344 1.00 57.90 ? 202 GOL A O1  1 
HETATM 11074 C  C2  . GOL L  3 .   ? 86.077  52.500  -21.308 1.00 49.24 ? 202 GOL A C2  1 
HETATM 11075 O  O2  . GOL L  3 .   ? 85.561  51.882  -22.435 1.00 53.50 ? 202 GOL A O2  1 
HETATM 11076 C  C3  . GOL L  3 .   ? 86.368  51.536  -20.121 1.00 45.30 ? 202 GOL A C3  1 
HETATM 11077 O  O3  . GOL L  3 .   ? 85.151  51.059  -19.576 1.00 44.26 ? 202 GOL A O3  1 
HETATM 11078 ZN ZN  . ZN  M  2 .   ? 49.745  64.978  -15.550 1.00 26.88 ? 201 ZN  B ZN  1 
HETATM 11079 C  C1  . I2G N  4 .   ? 43.427  74.177  -28.178 1.00 49.68 ? 202 I2G B C1  1 
HETATM 11080 C  C2  . I2G N  4 .   ? 43.458  73.269  -29.402 1.00 54.94 ? 202 I2G B C2  1 
HETATM 11081 C  C4  . I2G N  4 .   ? 45.369  76.833  -26.540 1.00 54.61 ? 202 I2G B C4  1 
HETATM 11082 C  C5  . I2G N  4 .   ? 44.264  76.444  -27.492 1.00 47.53 ? 202 I2G B C5  1 
HETATM 11083 C  C6  . I2G N  4 .   ? 44.619  75.126  -28.170 1.00 48.90 ? 202 I2G B C6  1 
HETATM 11084 C  C7  . I2G N  4 .   ? 44.927  74.769  -25.277 1.00 47.87 ? 202 I2G B C7  1 
HETATM 11085 C  C8  . I2G N  4 .   ? 44.065  77.551  -28.520 1.00 50.18 ? 202 I2G B C8  1 
HETATM 11086 C  C9  . I2G N  4 .   ? 45.680  76.047  -25.501 1.00 55.81 ? 202 I2G B C9  1 
HETATM 11087 C  C10 . I2G N  4 .   ? 46.762  76.437  -24.577 1.00 50.70 ? 202 I2G B C10 1 
HETATM 11088 C  C11 . I2G N  4 .   ? 46.509  76.578  -23.279 1.00 54.22 ? 202 I2G B C11 1 
HETATM 11089 C  C12 . I2G N  4 .   ? 47.590  76.968  -22.354 1.00 56.33 ? 202 I2G B C12 1 
HETATM 11090 C  C3  . I2G N  4 .   ? 42.764  71.955  -29.121 1.00 42.68 ? 202 I2G B C3  1 
HETATM 11091 O  O13 . I2G N  4 .   ? 47.914  76.183  -21.437 1.00 50.63 ? 202 I2G B O13 1 
HETATM 11092 O  O14 . I2G N  4 .   ? 48.154  78.072  -22.510 1.00 56.89 ? 202 I2G B O14 1 
HETATM 11093 C  C1  . GOL O  3 .   ? 50.361  61.453  -21.816 1.00 29.08 ? 203 GOL B C1  1 
HETATM 11094 O  O1  . GOL O  3 .   ? 49.836  60.336  -21.083 1.00 51.26 ? 203 GOL B O1  1 
HETATM 11095 C  C2  . GOL O  3 .   ? 50.250  61.332  -23.380 1.00 38.77 ? 203 GOL B C2  1 
HETATM 11096 O  O2  . GOL O  3 .   ? 49.595  62.450  -23.983 1.00 46.09 ? 203 GOL B O2  1 
HETATM 11097 C  C3  . GOL O  3 .   ? 49.618  59.972  -23.767 1.00 46.80 ? 203 GOL B C3  1 
HETATM 11098 O  O3  . GOL O  3 .   ? 49.993  59.761  -25.122 1.00 46.30 ? 203 GOL B O3  1 
HETATM 11099 C  C1  . GOL P  3 .   ? 71.631  76.731  -15.322 1.00 46.93 ? 204 GOL B C1  1 
HETATM 11100 O  O1  . GOL P  3 .   ? 70.336  77.160  -14.967 1.00 58.98 ? 204 GOL B O1  1 
HETATM 11101 C  C2  . GOL P  3 .   ? 72.296  76.054  -14.064 1.00 52.15 ? 204 GOL B C2  1 
HETATM 11102 O  O2  . GOL P  3 .   ? 73.682  76.310  -14.003 1.00 54.77 ? 204 GOL B O2  1 
HETATM 11103 C  C3  . GOL P  3 .   ? 71.526  76.604  -12.828 1.00 49.90 ? 204 GOL B C3  1 
HETATM 11104 O  O3  . GOL P  3 .   ? 72.177  76.108  -11.685 1.00 56.92 ? 204 GOL B O3  1 
HETATM 11105 C  C1  . GOL Q  3 .   ? 45.634  77.598  -11.688 1.00 52.14 ? 205 GOL B C1  1 
HETATM 11106 O  O1  . GOL Q  3 .   ? 44.896  76.415  -11.521 1.00 53.23 ? 205 GOL B O1  1 
HETATM 11107 C  C2  . GOL Q  3 .   ? 44.810  78.738  -11.017 1.00 58.31 ? 205 GOL B C2  1 
HETATM 11108 O  O2  . GOL Q  3 .   ? 43.690  79.066  -11.762 1.00 56.16 ? 205 GOL B O2  1 
HETATM 11109 C  C3  . GOL Q  3 .   ? 44.447  78.202  -9.600  1.00 48.97 ? 205 GOL B C3  1 
HETATM 11110 O  O3  . GOL Q  3 .   ? 43.917  79.279  -8.867  1.00 56.11 ? 205 GOL B O3  1 
HETATM 11111 ZN ZN  . ZN  R  2 .   ? 57.025  130.212 -12.776 1.00 45.53 ? 201 ZN  D ZN  1 
HETATM 11112 C  C1  . I2G S  4 .   ? 62.939  111.059 -32.794 1.00 53.45 ? 202 I2G D C1  1 
HETATM 11113 C  C2  . I2G S  4 .   ? 63.418  109.674 -33.212 1.00 53.93 ? 202 I2G D C2  1 
HETATM 11114 C  C4  . I2G S  4 .   ? 59.475  112.706 -32.818 1.00 41.16 ? 202 I2G D C4  1 
HETATM 11115 C  C5  . I2G S  4 .   ? 60.978  112.626 -32.696 1.00 52.83 ? 202 I2G D C5  1 
HETATM 11116 C  C6  . I2G S  4 .   ? 61.442  111.215 -33.035 1.00 44.34 ? 202 I2G D C6  1 
HETATM 11117 C  C7  . I2G S  4 .   ? 59.625  115.125 -32.394 1.00 29.43 ? 202 I2G D C7  1 
HETATM 11118 C  C8  . I2G S  4 .   ? 61.393  113.012 -31.282 1.00 50.06 ? 202 I2G D C8  1 
HETATM 11119 C  C9  . I2G S  4 .   ? 58.841  113.878 -32.676 1.00 40.67 ? 202 I2G D C9  1 
HETATM 11120 C  C10 . I2G S  4 .   ? 57.372  113.942 -32.797 1.00 37.16 ? 202 I2G D C10 1 
HETATM 11121 C  C11 . I2G S  4 .   ? 56.765  115.119 -32.916 1.00 46.00 ? 202 I2G D C11 1 
HETATM 11122 C  C12 . I2G S  4 .   ? 55.296  115.182 -33.037 1.00 54.77 ? 202 I2G D C12 1 
HETATM 11123 C  C3  . I2G S  4 .   ? 63.383  109.518 -34.716 1.00 44.91 ? 202 I2G D C3  1 
HETATM 11124 O  O13 . I2G S  4 .   ? 54.593  114.891 -32.045 1.00 57.17 ? 202 I2G D O13 1 
HETATM 11125 O  O14 . I2G S  4 .   ? 54.791  115.524 -34.128 1.00 53.56 ? 202 I2G D O14 1 
HETATM 11126 C  C1  . GOL T  3 .   ? 63.536  111.568 -37.531 1.00 51.65 ? 203 GOL D C1  1 
HETATM 11127 O  O1  . GOL T  3 .   ? 64.453  111.339 -38.561 1.00 53.65 ? 203 GOL D O1  1 
HETATM 11128 C  C2  . GOL T  3 .   ? 63.664  113.060 -37.099 1.00 52.56 ? 203 GOL D C2  1 
HETATM 11129 O  O2  . GOL T  3 .   ? 62.834  113.907 -37.860 1.00 47.54 ? 203 GOL D O2  1 
HETATM 11130 C  C3  . GOL T  3 .   ? 63.290  113.094 -35.577 1.00 51.50 ? 203 GOL D C3  1 
HETATM 11131 O  O3  . GOL T  3 .   ? 64.441  113.449 -34.862 1.00 59.25 ? 203 GOL D O3  1 
HETATM 11132 ZN ZN  . ZN  U  2 .   ? 57.764  90.919  -15.728 1.00 48.80 ? 201 ZN  C ZN  1 
HETATM 11133 C  C1  . I2G V  4 .   ? 50.217  80.955  -26.611 1.00 43.36 ? 202 I2G C C1  1 
HETATM 11134 C  C2  . I2G V  4 .   ? 49.888  81.045  -28.097 1.00 47.20 ? 202 I2G C C2  1 
HETATM 11135 C  C4  . I2G V  4 .   ? 48.036  82.168  -23.712 1.00 55.24 ? 202 I2G C C4  1 
HETATM 11136 C  C5  . I2G V  4 .   ? 49.305  81.727  -24.401 1.00 48.32 ? 202 I2G C C5  1 
HETATM 11137 C  C6  . I2G V  4 .   ? 48.964  81.132  -25.762 1.00 48.88 ? 202 I2G C C6  1 
HETATM 11138 C  C7  . I2G V  4 .   ? 49.354  83.857  -22.501 1.00 41.94 ? 202 I2G C C7  1 
HETATM 11139 C  C8  . I2G V  4 .   ? 50.032  80.711  -23.527 1.00 49.71 ? 202 I2G C C8  1 
HETATM 11140 C  C9  . I2G V  4 .   ? 48.060  83.168  -22.820 1.00 50.19 ? 202 I2G C C9  1 
HETATM 11141 C  C10 . I2G V  4 .   ? 46.815  83.592  -22.152 1.00 47.14 ? 202 I2G C C10 1 
HETATM 11142 C  C11 . I2G V  4 .   ? 46.848  84.555  -21.235 1.00 45.23 ? 202 I2G C C11 1 
HETATM 11143 C  C12 . I2G V  4 .   ? 45.605  84.980  -20.565 1.00 50.40 ? 202 I2G C C12 1 
HETATM 11144 C  C3  . I2G V  4 .   ? 49.435  79.704  -28.633 1.00 45.73 ? 202 I2G C C3  1 
HETATM 11145 O  O13 . I2G V  4 .   ? 45.612  86.027  -19.882 1.00 30.70 ? 202 I2G C O13 1 
HETATM 11146 O  O14 . I2G V  4 .   ? 44.576  84.283  -20.698 1.00 46.05 ? 202 I2G C O14 1 
HETATM 11147 ZN ZN  . ZN  W  2 .   ? 58.779  30.579  12.959  1.00 49.23 ? 201 ZN  H ZN  1 
HETATM 11148 S  S   . DMS X  5 .   ? 48.856  77.001  23.564  1.00 65.02 ? 201 DMS E S   1 
HETATM 11149 O  O   . DMS X  5 .   ? 50.215  77.589  23.819  1.00 53.59 ? 201 DMS E O   1 
HETATM 11150 C  C1  . DMS X  5 .   ? 48.459  77.052  21.797  1.00 42.54 ? 201 DMS E C1  1 
HETATM 11151 C  C2  . DMS X  5 .   ? 47.520  78.012  24.274  1.00 42.66 ? 201 DMS E C2  1 
HETATM 11152 ZN ZN  . ZN  Y  2 .   ? 57.668  69.786  15.466  1.00 37.95 ? 202 ZN  E ZN  1 
HETATM 11153 ZN ZN  . ZN  Z  2 .   ? 94.422  66.911  -7.356  1.00 53.73 ? 201 ZN  F ZN  1 
HETATM 11154 ZN ZN  . ZN  AA 2 .   ? 93.056  106.423 -11.217 1.00 48.77 ? 201 ZN  G ZN  1 
HETATM 11155 ZN ZN  . ZN  BA 2 .   ? 57.163  55.976  -57.032 1.00 52.01 ? 201 ZN  I ZN  1 
HETATM 11156 C  C1  . I2G CA 4 .   ? 69.994  59.464  -48.060 1.00 37.63 ? 202 I2G I C1  1 
HETATM 11157 C  C2  . I2G CA 4 .   ? 71.395  59.174  -47.535 1.00 42.08 ? 202 I2G I C2  1 
HETATM 11158 C  C4  . I2G CA 4 .   ? 68.712  61.830  -50.784 1.00 55.06 ? 202 I2G I C4  1 
HETATM 11159 C  C5  . I2G CA 4 .   ? 68.639  60.730  -49.752 1.00 49.40 ? 202 I2G I C5  1 
HETATM 11160 C  C6  . I2G CA 4 .   ? 70.044  60.399  -49.262 1.00 47.93 ? 202 I2G I C6  1 
HETATM 11161 C  C7  . I2G CA 4 .   ? 69.972  60.298  -52.241 1.00 58.68 ? 202 I2G I C7  1 
HETATM 11162 C  C8  . I2G CA 4 .   ? 67.970  59.504  -50.363 1.00 34.83 ? 202 I2G I C8  1 
HETATM 11163 C  C9  . I2G CA 4 .   ? 69.338  61.626  -51.952 1.00 52.13 ? 202 I2G I C9  1 
HETATM 11164 C  C10 . I2G CA 4 .   ? 69.403  62.708  -52.953 1.00 53.21 ? 202 I2G I C10 1 
HETATM 11165 C  C11 . I2G CA 4 .   ? 68.302  63.086  -53.596 1.00 51.22 ? 202 I2G I C11 1 
HETATM 11166 C  C12 . I2G CA 4 .   ? 68.368  64.167  -54.597 1.00 59.28 ? 202 I2G I C12 1 
HETATM 11167 C  C3  . I2G CA 4 .   ? 71.339  58.565  -46.151 1.00 36.97 ? 202 I2G I C3  1 
HETATM 11168 O  O13 . I2G CA 4 .   ? 69.447  64.777  -54.760 1.00 58.76 ? 202 I2G I O13 1 
HETATM 11169 O  O14 . I2G CA 4 .   ? 67.344  64.446  -55.257 1.00 43.68 ? 202 I2G I O14 1 
HETATM 11170 O  O   . HOH DA 6 .   ? 62.771  37.410  -10.136 1.00 53.89 ? 301 HOH A O   1 
HETATM 11171 O  O   . HOH DA 6 .   ? 71.998  30.879  -32.155 1.00 73.10 ? 302 HOH A O   1 
HETATM 11172 O  O   . HOH DA 6 .   ? 66.508  46.120  -31.480 1.00 55.21 ? 303 HOH A O   1 
HETATM 11173 O  O   . HOH DA 6 .   ? 73.041  50.276  -31.975 1.00 28.80 ? 304 HOH A O   1 
HETATM 11174 O  O   . HOH DA 6 .   ? 89.047  38.959  -2.573  1.00 50.71 ? 305 HOH A O   1 
HETATM 11175 O  O   . HOH DA 6 .   ? 73.668  53.455  3.657   1.00 51.81 ? 306 HOH A O   1 
HETATM 11176 O  O   . HOH DA 6 .   ? 82.133  49.112  -5.561  1.00 27.79 ? 307 HOH A O   1 
HETATM 11177 O  O   . HOH DA 6 .   ? 68.915  33.316  -29.790 1.00 45.48 ? 308 HOH A O   1 
HETATM 11178 O  O   . HOH DA 6 .   ? 69.631  54.761  -8.341  1.00 40.22 ? 309 HOH A O   1 
HETATM 11179 O  O   . HOH DA 6 .   ? 88.916  45.852  -0.971  1.00 51.83 ? 310 HOH A O   1 
HETATM 11180 O  O   . HOH DA 6 .   ? 70.815  33.138  -32.362 1.00 50.33 ? 311 HOH A O   1 
HETATM 11181 O  O   . HOH DA 6 .   ? 89.295  41.112  -7.994  1.00 38.52 ? 312 HOH A O   1 
HETATM 11182 O  O   . HOH DA 6 .   ? 83.402  58.545  -10.493 1.00 43.16 ? 313 HOH A O   1 
HETATM 11183 O  O   . HOH DA 6 .   ? 84.389  36.363  -33.003 1.00 44.94 ? 314 HOH A O   1 
HETATM 11184 O  O   . HOH DA 6 .   ? 62.408  44.452  -4.689  1.00 35.80 ? 315 HOH A O   1 
HETATM 11185 O  O   . HOH DA 6 .   ? 72.834  53.810  -6.287  1.00 31.24 ? 316 HOH A O   1 
HETATM 11186 O  O   . HOH DA 6 .   ? 83.263  55.541  -25.115 1.00 43.30 ? 317 HOH A O   1 
HETATM 11187 O  O   . HOH DA 6 .   ? 61.191  38.813  -20.600 1.00 49.21 ? 318 HOH A O   1 
HETATM 11188 O  O   . HOH DA 6 .   ? 76.464  37.403  -10.811 1.00 35.30 ? 319 HOH A O   1 
HETATM 11189 O  O   . HOH DA 6 .   ? 71.443  45.624  -35.591 1.00 40.83 ? 320 HOH A O   1 
HETATM 11190 O  O   . HOH DA 6 .   ? 81.184  54.524  -8.781  1.00 37.82 ? 321 HOH A O   1 
HETATM 11191 O  O   . HOH DA 6 .   ? 78.500  37.217  -16.516 1.00 27.31 ? 322 HOH A O   1 
HETATM 11192 O  O   . HOH DA 6 .   ? 65.291  39.182  -5.147  1.00 29.77 ? 323 HOH A O   1 
HETATM 11193 O  O   . HOH DA 6 .   ? 93.369  40.667  -20.671 1.00 38.43 ? 324 HOH A O   1 
HETATM 11194 O  O   . HOH DA 6 .   ? 89.940  41.307  -23.459 1.00 36.24 ? 325 HOH A O   1 
HETATM 11195 O  O   . HOH DA 6 .   ? 82.008  46.413  -4.599  1.00 30.69 ? 326 HOH A O   1 
HETATM 11196 O  O   . HOH DA 6 .   ? 79.386  44.531  -33.199 1.00 30.78 ? 327 HOH A O   1 
HETATM 11197 O  O   . HOH DA 6 .   ? 69.044  53.683  -25.132 1.00 33.00 ? 328 HOH A O   1 
HETATM 11198 O  O   . HOH DA 6 .   ? 64.615  46.494  -4.915  1.00 33.20 ? 329 HOH A O   1 
HETATM 11199 O  O   . HOH DA 6 .   ? 71.821  54.675  -25.634 1.00 36.98 ? 330 HOH A O   1 
HETATM 11200 O  O   . HOH DA 6 .   ? 76.255  66.047  -18.625 1.00 36.53 ? 331 HOH A O   1 
HETATM 11201 O  O   . HOH DA 6 .   ? 69.524  30.656  -17.285 1.00 47.67 ? 332 HOH A O   1 
HETATM 11202 O  O   . HOH DA 6 .   ? 72.402  32.508  -28.143 1.00 41.24 ? 333 HOH A O   1 
HETATM 11203 O  O   . HOH DA 6 .   ? 70.925  41.918  -4.642  1.00 24.02 ? 334 HOH A O   1 
HETATM 11204 O  O   . HOH DA 6 .   ? 95.840  41.185  -13.051 1.00 35.47 ? 335 HOH A O   1 
HETATM 11205 O  O   . HOH DA 6 .   ? 66.848  52.303  -21.541 1.00 19.03 ? 336 HOH A O   1 
HETATM 11206 O  O   . HOH DA 6 .   ? 83.118  41.815  -14.234 1.00 28.58 ? 337 HOH A O   1 
HETATM 11207 O  O   . HOH DA 6 .   ? 74.053  52.698  -35.430 1.00 46.02 ? 338 HOH A O   1 
HETATM 11208 O  O   . HOH DA 6 .   ? 99.698  42.394  -18.690 1.00 41.69 ? 339 HOH A O   1 
HETATM 11209 O  O   . HOH DA 6 .   ? 71.408  60.477  -20.182 1.00 22.17 ? 340 HOH A O   1 
HETATM 11210 O  O   . HOH DA 6 .   ? 73.236  35.758  -7.117  1.00 43.49 ? 341 HOH A O   1 
HETATM 11211 O  O   . HOH DA 6 .   ? 64.039  51.733  -6.372  1.00 37.74 ? 342 HOH A O   1 
HETATM 11212 O  O   . HOH DA 6 .   ? 73.915  33.584  -26.323 1.00 33.40 ? 343 HOH A O   1 
HETATM 11213 O  O   . HOH DA 6 .   ? 77.231  49.279  -31.862 1.00 30.94 ? 344 HOH A O   1 
HETATM 11214 O  O   . HOH DA 6 .   ? 89.140  49.828  -9.991  1.00 39.25 ? 345 HOH A O   1 
HETATM 11215 O  O   . HOH DA 6 .   ? 79.668  61.944  -16.737 1.00 29.19 ? 346 HOH A O   1 
HETATM 11216 O  O   . HOH DA 6 .   ? 79.029  55.953  -27.641 1.00 43.89 ? 347 HOH A O   1 
HETATM 11217 O  O   . HOH DA 6 .   ? 85.539  52.138  -17.004 1.00 35.52 ? 348 HOH A O   1 
HETATM 11218 O  O   . HOH DA 6 .   ? 78.135  37.964  -35.491 1.00 37.05 ? 349 HOH A O   1 
HETATM 11219 O  O   . HOH DA 6 .   ? 61.734  44.605  -17.587 1.00 30.20 ? 350 HOH A O   1 
HETATM 11220 O  O   . HOH DA 6 .   ? 84.589  57.716  -20.302 1.00 45.00 ? 351 HOH A O   1 
HETATM 11221 O  O   . HOH DA 6 .   ? 72.673  54.189  -34.050 1.00 50.82 ? 352 HOH A O   1 
HETATM 11222 O  O   . HOH DA 6 .   ? 57.708  40.994  -4.935  1.00 49.83 ? 353 HOH A O   1 
HETATM 11223 O  O   . HOH DA 6 .   ? 77.348  66.853  -21.345 1.00 33.56 ? 354 HOH A O   1 
HETATM 11224 O  O   . HOH DA 6 .   ? 90.133  35.742  -16.898 1.00 41.94 ? 355 HOH A O   1 
HETATM 11225 O  O   . HOH DA 6 .   ? 85.085  47.615  -19.223 1.00 32.67 ? 356 HOH A O   1 
HETATM 11226 O  O   . HOH DA 6 .   ? 79.396  31.589  -28.756 1.00 42.41 ? 357 HOH A O   1 
HETATM 11227 O  O   . HOH DA 6 .   ? 76.995  58.234  -8.513  1.00 34.58 ? 358 HOH A O   1 
HETATM 11228 O  O   . HOH DA 6 .   ? 71.602  48.319  -2.283  1.00 33.29 ? 359 HOH A O   1 
HETATM 11229 O  O   . HOH DA 6 .   ? 99.562  48.554  -16.878 1.00 46.12 ? 360 HOH A O   1 
HETATM 11230 O  O   . HOH DA 6 .   ? 85.303  52.341  -11.312 1.00 42.26 ? 361 HOH A O   1 
HETATM 11231 O  O   . HOH DA 6 .   ? 73.737  63.733  -27.178 1.00 40.69 ? 362 HOH A O   1 
HETATM 11232 O  O   . HOH DA 6 .   ? 84.242  53.403  -26.193 1.00 34.03 ? 363 HOH A O   1 
HETATM 11233 O  O   . HOH DA 6 .   ? 80.558  38.696  -5.014  1.00 41.93 ? 364 HOH A O   1 
HETATM 11234 O  O   . HOH DA 6 .   ? 97.281  48.617  -18.394 1.00 45.57 ? 365 HOH A O   1 
HETATM 11235 O  O   . HOH DA 6 .   ? 85.205  55.016  -6.267  1.00 50.03 ? 366 HOH A O   1 
HETATM 11236 O  O   . HOH DA 6 .   ? 86.047  51.263  -14.423 1.00 26.80 ? 367 HOH A O   1 
HETATM 11237 O  O   . HOH DA 6 .   ? 61.487  42.911  -15.423 1.00 46.64 ? 368 HOH A O   1 
HETATM 11238 O  O   . HOH DA 6 .   ? 73.018  40.011  -35.169 1.00 40.62 ? 369 HOH A O   1 
HETATM 11239 O  O   A HOH DA 6 .   ? 68.741  54.995  -22.584 0.50 13.42 ? 370 HOH A O   1 
HETATM 11240 O  O   B HOH DA 6 .   ? 67.071  54.168  -23.351 0.50 31.84 ? 370 HOH A O   1 
HETATM 11241 O  O   . HOH DA 6 .   ? 70.601  39.522  2.100   1.00 40.69 ? 371 HOH A O   1 
HETATM 11242 O  O   . HOH DA 6 .   ? 84.325  53.896  -0.935  1.00 53.95 ? 372 HOH A O   1 
HETATM 11243 O  O   . HOH DA 6 .   ? 88.156  39.288  -26.359 1.00 39.46 ? 373 HOH A O   1 
HETATM 11244 O  O   . HOH DA 6 .   ? 86.925  48.691  -20.942 1.00 43.17 ? 374 HOH A O   1 
HETATM 11245 O  O   . HOH DA 6 .   ? 89.688  48.297  -21.650 1.00 41.28 ? 375 HOH A O   1 
HETATM 11246 O  O   . HOH DA 6 .   ? 74.957  33.539  -15.409 1.00 37.54 ? 376 HOH A O   1 
HETATM 11247 O  O   . HOH DA 6 .   ? 81.030  43.140  -31.578 1.00 31.93 ? 377 HOH A O   1 
HETATM 11248 O  O   . HOH DA 6 .   ? 72.471  29.736  -30.408 1.00 51.64 ? 378 HOH A O   1 
HETATM 11249 O  O   . HOH DA 6 .   ? 83.457  43.535  -31.014 1.00 37.85 ? 379 HOH A O   1 
HETATM 11250 O  O   . HOH DA 6 .   ? 76.529  37.699  -7.072  1.00 32.27 ? 380 HOH A O   1 
HETATM 11251 O  O   . HOH DA 6 .   ? 86.717  36.113  -3.923  1.00 47.78 ? 381 HOH A O   1 
HETATM 11252 O  O   . HOH DA 6 .   ? 73.236  60.803  -27.453 1.00 41.77 ? 382 HOH A O   1 
HETATM 11253 O  O   . HOH DA 6 .   ? 85.709  35.451  -26.927 1.00 36.92 ? 383 HOH A O   1 
HETATM 11254 O  O   . HOH DA 6 .   ? 75.150  33.613  -10.401 1.00 52.73 ? 384 HOH A O   1 
HETATM 11255 O  O   . HOH DA 6 .   ? 88.122  38.388  -4.701  1.00 39.60 ? 385 HOH A O   1 
HETATM 11256 O  O   . HOH DA 6 .   ? 59.537  48.448  -10.520 1.00 32.06 ? 386 HOH A O   1 
HETATM 11257 O  O   . HOH DA 6 .   ? 79.758  55.814  -6.722  1.00 44.58 ? 387 HOH A O   1 
HETATM 11258 O  O   . HOH DA 6 .   ? 58.375  37.140  -13.313 1.00 48.73 ? 388 HOH A O   1 
HETATM 11259 O  O   . HOH DA 6 .   ? 74.977  34.713  -13.146 1.00 33.19 ? 389 HOH A O   1 
HETATM 11260 O  O   . HOH DA 6 .   ? 82.822  51.577  -29.868 1.00 43.73 ? 390 HOH A O   1 
HETATM 11261 O  O   . HOH DA 6 .   ? 96.448  35.880  -13.749 1.00 41.95 ? 391 HOH A O   1 
HETATM 11262 O  O   . HOH DA 6 .   ? 87.764  35.899  -19.466 1.00 43.06 ? 392 HOH A O   1 
HETATM 11263 O  O   . HOH DA 6 .   ? 64.923  41.134  -24.761 1.00 39.60 ? 393 HOH A O   1 
HETATM 11264 O  O   . HOH DA 6 .   ? 65.955  37.648  0.765   1.00 48.35 ? 394 HOH A O   1 
HETATM 11265 O  O   . HOH DA 6 .   ? 85.090  33.375  -6.343  1.00 45.20 ? 395 HOH A O   1 
HETATM 11266 O  O   . HOH DA 6 .   ? 64.386  38.304  -8.356  1.00 40.57 ? 396 HOH A O   1 
HETATM 11267 O  O   . HOH DA 6 .   ? 80.473  34.229  -36.486 1.00 44.00 ? 397 HOH A O   1 
HETATM 11268 O  O   . HOH DA 6 .   ? 80.532  36.855  -35.571 1.00 39.02 ? 398 HOH A O   1 
HETATM 11269 O  O   . HOH DA 6 .   ? 60.933  44.591  -22.167 1.00 38.90 ? 399 HOH A O   1 
HETATM 11270 O  O   . HOH DA 6 .   ? 78.250  58.177  -29.591 1.00 50.42 ? 400 HOH A O   1 
HETATM 11271 O  O   . HOH DA 6 .   ? 74.244  55.321  -26.806 1.00 44.52 ? 401 HOH A O   1 
HETATM 11272 O  O   . HOH DA 6 .   ? 75.374  42.205  -1.175  1.00 46.73 ? 402 HOH A O   1 
HETATM 11273 O  O   . HOH DA 6 .   ? 69.952  30.608  -25.648 1.00 46.43 ? 403 HOH A O   1 
HETATM 11274 O  O   . HOH DA 6 .   ? 81.358  41.680  -3.106  1.00 48.56 ? 404 HOH A O   1 
HETATM 11275 O  O   . HOH DA 6 .   ? 88.710  52.194  -6.693  1.00 46.12 ? 405 HOH A O   1 
HETATM 11276 O  O   . HOH DA 6 .   ? 86.401  35.567  -11.134 1.00 44.61 ? 406 HOH A O   1 
HETATM 11277 O  O   . HOH DA 6 .   ? 66.766  33.573  -18.587 1.00 45.28 ? 407 HOH A O   1 
HETATM 11278 O  O   . HOH DA 6 .   ? 83.352  35.474  -11.775 1.00 25.84 ? 408 HOH A O   1 
HETATM 11279 O  O   . HOH DA 6 .   ? 68.197  35.149  -15.187 1.00 38.17 ? 409 HOH A O   1 
HETATM 11280 O  O   . HOH DA 6 .   ? 81.083  55.165  -26.410 1.00 50.45 ? 410 HOH A O   1 
HETATM 11281 O  O   . HOH DA 6 .   ? 62.764  41.410  -23.785 1.00 43.98 ? 411 HOH A O   1 
HETATM 11282 O  O   . HOH DA 6 .   ? 57.237  50.373  -11.016 1.00 41.64 ? 412 HOH A O   1 
HETATM 11283 O  O   . HOH DA 6 .   ? 69.060  40.994  -37.136 1.00 37.77 ? 413 HOH A O   1 
HETATM 11284 O  O   . HOH DA 6 .   ? 67.979  41.993  -29.661 1.00 44.79 ? 414 HOH A O   1 
HETATM 11285 O  O   . HOH DA 6 .   ? 84.863  51.718  1.177   1.00 53.20 ? 415 HOH A O   1 
HETATM 11286 O  O   . HOH DA 6 .   ? 62.144  31.966  -10.555 1.00 55.50 ? 416 HOH A O   1 
HETATM 11287 O  O   . HOH DA 6 .   ? 70.896  37.620  -2.103  1.00 48.96 ? 417 HOH A O   1 
HETATM 11288 O  O   . HOH DA 6 .   ? 53.061  50.880  -19.775 1.00 52.11 ? 418 HOH A O   1 
HETATM 11289 O  O   . HOH DA 6 .   ? 49.571  47.522  -18.958 1.00 50.85 ? 419 HOH A O   1 
HETATM 11290 O  O   . HOH DA 6 .   ? 65.523  53.104  -3.869  1.00 45.39 ? 420 HOH A O   1 
HETATM 11291 O  O   . HOH DA 6 .   ? 58.079  51.371  -4.224  1.00 53.27 ? 421 HOH A O   1 
HETATM 11292 O  O   . HOH DA 6 .   ? 70.950  51.183  -33.047 1.00 49.13 ? 422 HOH A O   1 
HETATM 11293 O  O   . HOH DA 6 .   ? 85.402  56.890  -17.842 1.00 25.55 ? 423 HOH A O   1 
HETATM 11294 O  O   . HOH DA 6 .   ? 90.656  33.800  -7.462  1.00 51.63 ? 424 HOH A O   1 
HETATM 11295 O  O   . HOH DA 6 .   ? 65.541  42.227  -27.589 1.00 44.85 ? 425 HOH A O   1 
HETATM 11296 O  O   . HOH DA 6 .   ? 85.830  56.016  -22.250 1.00 43.83 ? 426 HOH A O   1 
HETATM 11297 O  O   . HOH DA 6 .   ? 51.168  45.845  -13.993 1.00 58.30 ? 427 HOH A O   1 
HETATM 11298 O  O   . HOH DA 6 .   ? 58.994  41.941  -19.861 1.00 54.01 ? 428 HOH A O   1 
HETATM 11299 O  O   . HOH DA 6 .   ? 63.394  34.768  -17.317 1.00 50.39 ? 429 HOH A O   1 
HETATM 11300 O  O   . HOH DA 6 .   ? 88.417  54.776  -0.372  1.00 53.02 ? 430 HOH A O   1 
HETATM 11301 O  O   . HOH DA 6 .   ? 77.657  56.174  -5.339  1.00 45.45 ? 431 HOH A O   1 
HETATM 11302 O  O   . HOH DA 6 .   ? 66.459  44.608  -29.820 1.00 49.38 ? 432 HOH A O   1 
HETATM 11303 O  O   . HOH DA 6 .   ? 75.454  36.340  -1.631  1.00 46.68 ? 433 HOH A O   1 
HETATM 11304 O  O   . HOH DA 6 .   ? 60.933  35.804  -17.063 1.00 50.08 ? 434 HOH A O   1 
HETATM 11305 O  O   . HOH DA 6 .   ? 62.407  34.166  -19.467 1.00 53.67 ? 435 HOH A O   1 
HETATM 11306 O  O   . HOH DA 6 .   ? 97.234  39.108  -11.839 1.00 41.37 ? 436 HOH A O   1 
HETATM 11307 O  O   . HOH DA 6 .   ? 79.520  48.013  -32.811 1.00 35.53 ? 437 HOH A O   1 
HETATM 11308 O  O   . HOH DA 6 .   ? 50.469  45.803  -20.200 1.00 52.80 ? 438 HOH A O   1 
HETATM 11309 O  O   . HOH DA 6 .   ? 86.922  57.618  -15.642 1.00 46.57 ? 439 HOH A O   1 
HETATM 11310 O  O   . HOH DA 6 .   ? 86.927  53.529  -27.498 1.00 55.01 ? 440 HOH A O   1 
HETATM 11311 O  O   . HOH DA 6 .   ? 61.042  43.409  -24.350 1.00 48.96 ? 441 HOH A O   1 
HETATM 11312 O  O   . HOH DA 6 .   ? 69.893  57.558  -7.393  1.00 48.29 ? 442 HOH A O   1 
HETATM 11313 O  O   . HOH DA 6 .   ? 89.395  33.747  -15.152 1.00 46.67 ? 443 HOH A O   1 
HETATM 11314 O  O   . HOH DA 6 .   ? 83.035  46.168  -32.882 1.00 47.24 ? 444 HOH A O   1 
HETATM 11315 O  O   . HOH DA 6 .   ? 68.237  29.122  -6.373  1.00 53.99 ? 445 HOH A O   1 
HETATM 11316 O  O   . HOH DA 6 .   ? 88.924  51.863  3.040   1.00 50.95 ? 446 HOH A O   1 
HETATM 11317 O  O   . HOH DA 6 .   ? 46.834  49.454  -20.128 1.00 52.30 ? 447 HOH A O   1 
HETATM 11318 O  O   . HOH EA 6 .   ? 37.034  66.095  -13.016 1.00 47.95 ? 301 HOH B O   1 
HETATM 11319 O  O   . HOH EA 6 .   ? 62.379  83.805  -30.991 1.00 52.82 ? 302 HOH B O   1 
HETATM 11320 O  O   . HOH EA 6 .   ? 44.222  73.267  -13.625 1.00 43.17 ? 303 HOH B O   1 
HETATM 11321 O  O   . HOH EA 6 .   ? 67.877  64.974  -3.868  1.00 38.38 ? 304 HOH B O   1 
HETATM 11322 O  O   . HOH EA 6 .   ? 42.243  80.325  -13.335 1.00 39.58 ? 305 HOH B O   1 
HETATM 11323 O  O   . HOH EA 6 .   ? 63.074  64.861  -1.839  1.00 34.68 ? 306 HOH B O   1 
HETATM 11324 O  O   . HOH EA 6 .   ? 40.505  66.080  -26.034 1.00 40.79 ? 307 HOH B O   1 
HETATM 11325 O  O   . HOH EA 6 .   ? 52.963  64.706  -15.964 1.00 46.23 ? 308 HOH B O   1 
HETATM 11326 O  O   . HOH EA 6 .   ? 57.659  46.669  -24.395 1.00 47.53 ? 309 HOH B O   1 
HETATM 11327 O  O   . HOH EA 6 .   ? 69.988  77.421  -27.013 1.00 43.50 ? 310 HOH B O   1 
HETATM 11328 O  O   . HOH EA 6 .   ? 42.104  63.632  -6.873  1.00 41.52 ? 311 HOH B O   1 
HETATM 11329 O  O   . HOH EA 6 .   ? 64.835  62.643  -32.311 1.00 32.37 ? 312 HOH B O   1 
HETATM 11330 O  O   . HOH EA 6 .   ? 67.323  58.975  -25.141 1.00 33.40 ? 313 HOH B O   1 
HETATM 11331 O  O   . HOH EA 6 .   ? 51.499  70.083  -16.321 1.00 23.25 ? 314 HOH B O   1 
HETATM 11332 O  O   . HOH EA 6 .   ? 56.989  73.731  -7.369  1.00 39.77 ? 315 HOH B O   1 
HETATM 11333 O  O   . HOH EA 6 .   ? 50.575  52.853  -14.131 1.00 42.97 ? 316 HOH B O   1 
HETATM 11334 O  O   . HOH EA 6 .   ? 39.125  70.756  -16.653 1.00 23.53 ? 317 HOH B O   1 
HETATM 11335 O  O   . HOH EA 6 .   ? 57.436  82.609  -36.593 1.00 50.45 ? 318 HOH B O   1 
HETATM 11336 O  O   . HOH EA 6 .   ? 66.714  54.250  -26.268 1.00 42.90 ? 319 HOH B O   1 
HETATM 11337 O  O   . HOH EA 6 .   ? 48.139  56.612  -5.054  1.00 46.59 ? 320 HOH B O   1 
HETATM 11338 O  O   . HOH EA 6 .   ? 57.273  48.932  -18.298 1.00 29.23 ? 321 HOH B O   1 
HETATM 11339 O  O   . HOH EA 6 .   ? 53.523  74.503  -31.291 1.00 42.01 ? 322 HOH B O   1 
HETATM 11340 O  O   . HOH EA 6 .   ? 57.475  74.328  -11.091 1.00 34.30 ? 323 HOH B O   1 
HETATM 11341 O  O   . HOH EA 6 .   ? 56.815  56.702  -5.613  1.00 38.84 ? 324 HOH B O   1 
HETATM 11342 O  O   . HOH EA 6 .   ? 60.142  69.943  -2.120  1.00 48.72 ? 325 HOH B O   1 
HETATM 11343 O  O   . HOH EA 6 .   ? 58.482  68.931  -34.477 1.00 31.00 ? 326 HOH B O   1 
HETATM 11344 O  O   . HOH EA 6 .   ? 77.478  63.136  -15.769 1.00 31.38 ? 327 HOH B O   1 
HETATM 11345 O  O   . HOH EA 6 .   ? 45.229  76.179  -19.580 1.00 42.16 ? 328 HOH B O   1 
HETATM 11346 O  O   . HOH EA 6 .   ? 76.098  70.110  -15.496 1.00 43.49 ? 329 HOH B O   1 
HETATM 11347 O  O   . HOH EA 6 .   ? 41.920  68.280  -4.762  1.00 48.22 ? 330 HOH B O   1 
HETATM 11348 O  O   . HOH EA 6 .   ? 45.471  75.651  -8.107  1.00 49.34 ? 331 HOH B O   1 
HETATM 11349 O  O   . HOH EA 6 .   ? 38.440  75.777  -17.733 1.00 31.18 ? 332 HOH B O   1 
HETATM 11350 O  O   . HOH EA 6 .   ? 51.717  74.124  -29.637 1.00 41.81 ? 333 HOH B O   1 
HETATM 11351 O  O   . HOH EA 6 .   ? 56.137  54.752  -29.384 1.00 46.62 ? 334 HOH B O   1 
HETATM 11352 O  O   . HOH EA 6 .   ? 56.434  74.807  -17.259 1.00 23.46 ? 335 HOH B O   1 
HETATM 11353 O  O   . HOH EA 6 .   ? 66.998  79.975  -31.233 1.00 38.44 ? 336 HOH B O   1 
HETATM 11354 O  O   . HOH EA 6 .   ? 49.836  68.509  -34.660 1.00 50.39 ? 337 HOH B O   1 
HETATM 11355 O  O   . HOH EA 6 .   ? 65.099  73.784  -34.127 1.00 27.48 ? 338 HOH B O   1 
HETATM 11356 O  O   . HOH EA 6 .   ? 64.723  80.299  -27.296 1.00 35.06 ? 339 HOH B O   1 
HETATM 11357 O  O   . HOH EA 6 .   ? 42.032  71.703  -23.961 1.00 24.25 ? 340 HOH B O   1 
HETATM 11358 O  O   . HOH EA 6 .   ? 52.134  72.196  -6.394  1.00 39.33 ? 341 HOH B O   1 
HETATM 11359 O  O   . HOH EA 6 .   ? 57.365  79.327  -36.625 1.00 42.34 ? 342 HOH B O   1 
HETATM 11360 O  O   . HOH EA 6 .   ? 61.697  68.404  -4.313  1.00 36.34 ? 343 HOH B O   1 
HETATM 11361 O  O   . HOH EA 6 .   ? 68.815  59.934  -21.217 1.00 13.42 ? 344 HOH B O   1 
HETATM 11362 O  O   . HOH EA 6 .   ? 51.300  54.650  -23.260 1.00 40.01 ? 345 HOH B O   1 
HETATM 11363 O  O   . HOH EA 6 .   ? 46.477  64.064  -24.780 1.00 35.28 ? 346 HOH B O   1 
HETATM 11364 O  O   . HOH EA 6 .   ? 44.308  70.104  -11.288 1.00 30.86 ? 347 HOH B O   1 
HETATM 11365 O  O   . HOH EA 6 .   ? 50.843  64.649  -6.719  1.00 25.09 ? 348 HOH B O   1 
HETATM 11366 O  O   . HOH EA 6 .   ? 54.131  69.740  -32.613 1.00 26.46 ? 349 HOH B O   1 
HETATM 11367 O  O   . HOH EA 6 .   ? 64.223  57.895  -26.465 1.00 38.38 ? 350 HOH B O   1 
HETATM 11368 O  O   . HOH EA 6 .   ? 52.685  56.861  -11.314 1.00 28.54 ? 351 HOH B O   1 
HETATM 11369 O  O   . HOH EA 6 .   ? 55.250  50.245  -19.671 1.00 34.44 ? 352 HOH B O   1 
HETATM 11370 O  O   . HOH EA 6 .   ? 64.192  51.775  -21.208 1.00 22.11 ? 353 HOH B O   1 
HETATM 11371 O  O   . HOH EA 6 .   ? 74.538  68.045  -19.892 1.00 34.55 ? 354 HOH B O   1 
HETATM 11372 O  O   . HOH EA 6 .   ? 60.068  79.287  -17.131 1.00 35.56 ? 355 HOH B O   1 
HETATM 11373 O  O   . HOH EA 6 .   ? 46.140  71.232  -26.223 1.00 34.35 ? 356 HOH B O   1 
HETATM 11374 O  O   . HOH EA 6 .   ? 48.576  60.621  -17.546 1.00 25.37 ? 357 HOH B O   1 
HETATM 11375 O  O   . HOH EA 6 .   ? 56.889  70.030  -32.545 1.00 22.26 ? 358 HOH B O   1 
HETATM 11376 O  O   . HOH EA 6 .   ? 50.452  64.530  -21.775 1.00 26.27 ? 359 HOH B O   1 
HETATM 11377 O  O   . HOH EA 6 .   ? 47.048  58.559  -13.055 1.00 40.05 ? 360 HOH B O   1 
HETATM 11378 O  O   . HOH EA 6 .   ? 56.806  47.635  -21.983 1.00 39.66 ? 361 HOH B O   1 
HETATM 11379 O  O   . HOH EA 6 .   ? 60.672  62.678  -2.819  1.00 23.29 ? 362 HOH B O   1 
HETATM 11380 O  O   . HOH EA 6 .   ? 70.092  67.230  1.118   1.00 50.55 ? 363 HOH B O   1 
HETATM 11381 O  O   . HOH EA 6 .   ? 60.262  57.489  -7.243  1.00 25.76 ? 364 HOH B O   1 
HETATM 11382 O  O   . HOH EA 6 .   ? 64.349  56.421  -8.652  1.00 38.23 ? 365 HOH B O   1 
HETATM 11383 O  O   . HOH EA 6 .   ? 59.345  46.130  -20.747 1.00 40.44 ? 366 HOH B O   1 
HETATM 11384 O  O   . HOH EA 6 .   ? 69.909  66.758  -2.954  1.00 41.43 ? 367 HOH B O   1 
HETATM 11385 O  O   . HOH EA 6 .   ? 48.932  59.312  -14.333 1.00 37.08 ? 368 HOH B O   1 
HETATM 11386 O  O   . HOH EA 6 .   ? 44.915  61.613  -13.784 1.00 28.27 ? 369 HOH B O   1 
HETATM 11387 O  O   . HOH EA 6 .   ? 62.739  78.925  -25.854 1.00 25.23 ? 370 HOH B O   1 
HETATM 11388 O  O   . HOH EA 6 .   ? 57.115  76.477  -36.101 1.00 35.69 ? 371 HOH B O   1 
HETATM 11389 O  O   . HOH EA 6 .   ? 52.771  59.376  -29.087 1.00 27.07 ? 372 HOH B O   1 
HETATM 11390 O  O   . HOH EA 6 .   ? 46.233  74.895  -6.074  1.00 45.04 ? 373 HOH B O   1 
HETATM 11391 O  O   . HOH EA 6 .   ? 51.177  62.282  -7.858  1.00 22.56 ? 374 HOH B O   1 
HETATM 11392 O  O   . HOH EA 6 .   ? 60.585  63.884  -33.064 1.00 29.48 ? 375 HOH B O   1 
HETATM 11393 O  O   A HOH EA 6 .   ? 73.026  67.504  -15.456 0.61 22.42 ? 376 HOH B O   1 
HETATM 11394 O  O   B HOH EA 6 .   ? 72.713  68.060  -13.822 0.39 25.58 ? 376 HOH B O   1 
HETATM 11395 O  O   . HOH EA 6 .   ? 69.135  76.368  -22.793 1.00 41.85 ? 377 HOH B O   1 
HETATM 11396 O  O   . HOH EA 6 .   ? 54.774  61.360  -31.997 1.00 40.73 ? 378 HOH B O   1 
HETATM 11397 O  O   . HOH EA 6 .   ? 64.922  83.073  -29.357 1.00 44.53 ? 379 HOH B O   1 
HETATM 11398 O  O   . HOH EA 6 .   ? 42.265  68.217  -14.356 1.00 31.72 ? 380 HOH B O   1 
HETATM 11399 O  O   . HOH EA 6 .   ? 51.388  77.445  -28.605 1.00 29.93 ? 381 HOH B O   1 
HETATM 11400 O  O   . HOH EA 6 .   ? 56.288  53.160  -10.644 1.00 36.67 ? 382 HOH B O   1 
HETATM 11401 O  O   . HOH EA 6 .   ? 34.284  61.194  -20.149 1.00 47.14 ? 383 HOH B O   1 
HETATM 11402 O  O   . HOH EA 6 .   ? 51.701  77.139  -19.788 1.00 32.20 ? 384 HOH B O   1 
HETATM 11403 O  O   . HOH EA 6 .   ? 67.126  57.127  -22.595 1.00 23.95 ? 385 HOH B O   1 
HETATM 11404 O  O   . HOH EA 6 .   ? 62.063  68.367  -1.479  1.00 49.52 ? 386 HOH B O   1 
HETATM 11405 O  O   . HOH EA 6 .   ? 57.441  53.268  -8.504  1.00 42.26 ? 387 HOH B O   1 
HETATM 11406 O  O   . HOH EA 6 .   ? 67.436  72.053  -3.785  1.00 32.38 ? 388 HOH B O   1 
HETATM 11407 O  O   . HOH EA 6 .   ? 59.717  75.185  -36.108 1.00 42.71 ? 389 HOH B O   1 
HETATM 11408 O  O   . HOH EA 6 .   ? 75.357  75.793  -16.390 1.00 45.26 ? 390 HOH B O   1 
HETATM 11409 O  O   . HOH EA 6 .   ? 40.907  71.407  -13.004 1.00 44.65 ? 391 HOH B O   1 
HETATM 11410 O  O   . HOH EA 6 .   ? 60.912  70.521  -37.030 1.00 42.67 ? 392 HOH B O   1 
HETATM 11411 O  O   . HOH EA 6 .   ? 69.072  60.299  -0.582  1.00 57.83 ? 393 HOH B O   1 
HETATM 11412 O  O   . HOH EA 6 .   ? 45.003  72.782  -7.450  1.00 40.48 ? 394 HOH B O   1 
HETATM 11413 O  O   . HOH EA 6 .   ? 68.982  59.308  -5.600  1.00 49.16 ? 395 HOH B O   1 
HETATM 11414 O  O   . HOH EA 6 .   ? 48.973  73.531  -28.938 1.00 36.07 ? 396 HOH B O   1 
HETATM 11415 O  O   . HOH EA 6 .   ? 74.368  63.170  -8.670  1.00 31.73 ? 397 HOH B O   1 
HETATM 11416 O  O   A HOH EA 6 .   ? 58.323  59.603  -30.758 0.50 27.20 ? 398 HOH B O   1 
HETATM 11417 O  O   B HOH EA 6 .   ? 58.828  60.736  -32.159 0.50 31.85 ? 398 HOH B O   1 
HETATM 11418 O  O   . HOH EA 6 .   ? 50.779  56.861  -25.358 1.00 43.01 ? 399 HOH B O   1 
HETATM 11419 O  O   . HOH EA 6 .   ? 65.917  57.686  -2.337  1.00 46.10 ? 400 HOH B O   1 
HETATM 11420 O  O   . HOH EA 6 .   ? 50.756  76.033  -13.229 1.00 23.77 ? 401 HOH B O   1 
HETATM 11421 O  O   . HOH EA 6 .   ? 59.166  57.073  -29.683 1.00 38.28 ? 402 HOH B O   1 
HETATM 11422 O  O   . HOH EA 6 .   ? 63.450  56.304  -4.805  1.00 51.50 ? 403 HOH B O   1 
HETATM 11423 O  O   . HOH EA 6 .   ? 40.445  61.559  -25.835 1.00 51.62 ? 404 HOH B O   1 
HETATM 11424 O  O   . HOH EA 6 .   ? 44.282  59.694  -10.577 1.00 42.24 ? 405 HOH B O   1 
HETATM 11425 O  O   . HOH EA 6 .   ? 69.637  62.621  -1.414  1.00 50.46 ? 406 HOH B O   1 
HETATM 11426 O  O   . HOH EA 6 .   ? 39.430  60.462  -22.495 1.00 55.61 ? 407 HOH B O   1 
HETATM 11427 O  O   . HOH EA 6 .   ? 60.317  83.643  -31.400 1.00 40.92 ? 408 HOH B O   1 
HETATM 11428 O  O   . HOH EA 6 .   ? 51.343  68.771  -5.455  1.00 38.14 ? 409 HOH B O   1 
HETATM 11429 O  O   . HOH EA 6 .   ? 59.290  77.205  -13.123 1.00 25.93 ? 410 HOH B O   1 
HETATM 11430 O  O   . HOH EA 6 .   ? 65.175  60.542  -35.486 1.00 52.96 ? 411 HOH B O   1 
HETATM 11431 O  O   . HOH EA 6 .   ? 57.478  81.718  -29.613 1.00 51.91 ? 412 HOH B O   1 
HETATM 11432 O  O   . HOH EA 6 .   ? 62.407  56.890  -28.322 1.00 44.86 ? 413 HOH B O   1 
HETATM 11433 O  O   . HOH EA 6 .   ? 54.802  58.907  -30.813 1.00 53.05 ? 414 HOH B O   1 
HETATM 11434 O  O   . HOH EA 6 .   ? 56.596  70.124  -1.982  1.00 45.79 ? 415 HOH B O   1 
HETATM 11435 O  O   . HOH EA 6 .   ? 58.433  63.180  -33.640 1.00 51.92 ? 416 HOH B O   1 
HETATM 11436 O  O   . HOH EA 6 .   ? 52.608  55.067  -5.216  1.00 49.87 ? 417 HOH B O   1 
HETATM 11437 O  O   . HOH EA 6 .   ? 68.726  73.192  -6.880  1.00 40.04 ? 418 HOH B O   1 
HETATM 11438 O  O   . HOH EA 6 .   ? 41.982  61.205  -8.926  1.00 46.70 ? 419 HOH B O   1 
HETATM 11439 O  O   . HOH EA 6 .   ? 84.119  59.463  -12.565 1.00 35.65 ? 420 HOH B O   1 
HETATM 11440 O  O   . HOH EA 6 .   ? 50.123  55.763  -21.190 1.00 30.96 ? 421 HOH B O   1 
HETATM 11441 O  O   . HOH EA 6 .   ? 71.332  71.558  -22.959 1.00 38.75 ? 422 HOH B O   1 
HETATM 11442 O  O   . HOH EA 6 .   ? 66.729  81.732  -24.204 1.00 44.53 ? 423 HOH B O   1 
HETATM 11443 O  O   . HOH EA 6 .   ? 63.706  49.586  -28.756 1.00 44.55 ? 424 HOH B O   1 
HETATM 11444 O  O   . HOH EA 6 .   ? 45.398  64.791  -29.735 1.00 48.55 ? 425 HOH B O   1 
HETATM 11445 O  O   . HOH EA 6 .   ? 58.714  66.580  -2.853  1.00 45.92 ? 426 HOH B O   1 
HETATM 11446 O  O   . HOH EA 6 .   ? 76.758  60.942  -9.015  1.00 45.29 ? 427 HOH B O   1 
HETATM 11447 O  O   . HOH EA 6 .   ? 70.465  65.565  -27.990 1.00 44.42 ? 428 HOH B O   1 
HETATM 11448 O  O   . HOH EA 6 .   ? 53.732  55.543  -9.187  1.00 39.69 ? 429 HOH B O   1 
HETATM 11449 O  O   . HOH EA 6 .   ? 70.758  63.091  -34.959 1.00 53.11 ? 430 HOH B O   1 
HETATM 11450 O  O   . HOH EA 6 .   ? 51.695  66.577  -5.032  1.00 40.63 ? 431 HOH B O   1 
HETATM 11451 O  O   . HOH EA 6 .   ? 70.915  70.256  -26.493 1.00 41.30 ? 432 HOH B O   1 
HETATM 11452 O  O   . HOH EA 6 .   ? 63.062  79.164  -13.590 1.00 41.80 ? 433 HOH B O   1 
HETATM 11453 O  O   . HOH EA 6 .   ? 66.218  58.020  -32.221 1.00 48.30 ? 434 HOH B O   1 
HETATM 11454 O  O   . HOH EA 6 .   ? 55.928  57.591  -28.921 1.00 44.13 ? 435 HOH B O   1 
HETATM 11455 O  O   . HOH EA 6 .   ? 59.976  75.779  -6.900  1.00 45.45 ? 436 HOH B O   1 
HETATM 11456 O  O   . HOH EA 6 .   ? 45.345  64.054  1.191   1.00 51.09 ? 437 HOH B O   1 
HETATM 11457 O  O   . HOH EA 6 .   ? 71.972  58.161  -5.888  1.00 50.26 ? 438 HOH B O   1 
HETATM 11458 O  O   . HOH EA 6 .   ? 55.736  54.995  -7.440  1.00 44.31 ? 439 HOH B O   1 
HETATM 11459 O  O   . HOH EA 6 .   ? 75.529  67.195  -16.548 1.00 54.43 ? 440 HOH B O   1 
HETATM 11460 O  O   . HOH EA 6 .   ? 78.812  62.477  -8.500  1.00 52.81 ? 441 HOH B O   1 
HETATM 11461 O  O   . HOH EA 6 .   ? 38.865  63.769  -25.559 1.00 53.01 ? 442 HOH B O   1 
HETATM 11462 O  O   . HOH EA 6 .   ? 47.412  61.800  -28.015 1.00 53.49 ? 443 HOH B O   1 
HETATM 11463 O  O   . HOH EA 6 .   ? 54.235  49.877  -24.613 1.00 48.72 ? 444 HOH B O   1 
HETATM 11464 O  O   . HOH EA 6 .   ? 48.241  78.771  -9.383  1.00 47.56 ? 445 HOH B O   1 
HETATM 11465 O  O   . HOH EA 6 .   ? 64.282  56.859  -30.846 1.00 50.28 ? 446 HOH B O   1 
HETATM 11466 O  O   . HOH EA 6 .   ? 71.952  80.699  -14.682 1.00 56.18 ? 447 HOH B O   1 
HETATM 11467 O  O   . HOH EA 6 .   ? 59.286  45.500  -18.538 1.00 47.55 ? 448 HOH B O   1 
HETATM 11468 O  O   . HOH EA 6 .   ? 62.188  64.207  -39.671 1.00 46.69 ? 449 HOH B O   1 
HETATM 11469 O  O   . HOH EA 6 .   ? 71.441  65.861  -1.353  1.00 49.23 ? 450 HOH B O   1 
HETATM 11470 O  O   . HOH EA 6 .   ? 70.724  58.771  -31.510 1.00 54.66 ? 451 HOH B O   1 
HETATM 11471 O  O   . HOH EA 6 .   ? 46.633  72.824  -28.313 1.00 43.79 ? 452 HOH B O   1 
HETATM 11472 O  O   . HOH EA 6 .   ? 58.527  70.149  -37.367 1.00 44.51 ? 453 HOH B O   1 
HETATM 11473 O  O   . HOH EA 6 .   ? 39.718  75.911  -15.127 1.00 39.19 ? 454 HOH B O   1 
HETATM 11474 O  O   . HOH EA 6 .   ? 47.376  72.912  2.879   1.00 49.81 ? 455 HOH B O   1 
HETATM 11475 O  O   . HOH EA 6 .   ? 39.470  73.792  -13.762 1.00 51.00 ? 456 HOH B O   1 
HETATM 11476 O  O   . HOH EA 6 .   ? 74.469  77.472  -17.892 1.00 51.55 ? 457 HOH B O   1 
HETATM 11477 O  O   . HOH EA 6 .   ? 37.531  72.722  -15.653 1.00 28.76 ? 458 HOH B O   1 
HETATM 11478 O  O   . HOH EA 6 .   ? 43.406  70.982  -26.278 1.00 43.24 ? 459 HOH B O   1 
HETATM 11479 O  O   . HOH EA 6 .   ? 43.256  76.658  -21.156 1.00 50.65 ? 460 HOH B O   1 
HETATM 11480 O  O   . HOH EA 6 .   ? 53.040  68.721  -34.709 1.00 42.89 ? 461 HOH B O   1 
HETATM 11481 O  O   . HOH EA 6 .   ? 56.446  61.789  -33.716 1.00 43.55 ? 462 HOH B O   1 
HETATM 11482 O  O   . HOH EA 6 .   ? 71.189  68.506  -28.170 1.00 47.66 ? 463 HOH B O   1 
HETATM 11483 O  O   . HOH EA 6 .   ? 58.295  65.351  -34.369 1.00 39.10 ? 464 HOH B O   1 
HETATM 11484 O  O   . HOH EA 6 .   ? 54.695  81.392  -28.739 1.00 44.62 ? 465 HOH B O   1 
HETATM 11485 O  O   . HOH EA 6 .   ? 54.520  48.447  -21.738 1.00 49.58 ? 466 HOH B O   1 
HETATM 11486 O  O   . HOH EA 6 .   ? 57.326  44.695  -22.145 1.00 55.84 ? 467 HOH B O   1 
HETATM 11487 O  O   . HOH EA 6 .   ? 80.599  65.431  -6.905  1.00 49.47 ? 468 HOH B O   1 
HETATM 11488 O  O   . HOH EA 6 .   ? 63.766  70.755  -37.756 1.00 44.39 ? 469 HOH B O   1 
HETATM 11489 O  O   . HOH EA 6 .   ? 72.771  73.627  -28.417 1.00 58.40 ? 470 HOH B O   1 
HETATM 11490 O  O   . HOH EA 6 .   ? 63.846  77.227  -1.638  1.00 51.01 ? 471 HOH B O   1 
HETATM 11491 O  O   . HOH FA 6 .   ? 64.444  117.016 -22.955 1.00 57.36 ? 301 HOH D O   1 
HETATM 11492 O  O   . HOH FA 6 .   ? 67.894  121.490 -7.245  1.00 50.31 ? 302 HOH D O   1 
HETATM 11493 O  O   . HOH FA 6 .   ? 63.340  116.021 -37.453 1.00 40.51 ? 303 HOH D O   1 
HETATM 11494 O  O   . HOH FA 6 .   ? 68.451  120.084 -4.829  1.00 37.92 ? 304 HOH D O   1 
HETATM 11495 O  O   . HOH FA 6 .   ? 78.789  123.321 -8.041  1.00 53.39 ? 305 HOH D O   1 
HETATM 11496 O  O   . HOH FA 6 .   ? 57.414  114.223 -0.229  1.00 47.45 ? 306 HOH D O   1 
HETATM 11497 O  O   . HOH FA 6 .   ? 53.695  116.106 -30.193 1.00 47.99 ? 307 HOH D O   1 
HETATM 11498 O  O   . HOH FA 6 .   ? 73.033  127.819 -25.472 1.00 43.17 ? 308 HOH D O   1 
HETATM 11499 O  O   . HOH FA 6 .   ? 65.442  115.383 -2.048  1.00 36.43 ? 309 HOH D O   1 
HETATM 11500 O  O   . HOH FA 6 .   ? 68.620  128.827 -15.994 1.00 40.08 ? 310 HOH D O   1 
HETATM 11501 O  O   . HOH FA 6 .   ? 58.219  113.475 -25.121 1.00 32.79 ? 311 HOH D O   1 
HETATM 11502 O  O   . HOH FA 6 .   ? 44.127  116.042 -18.992 1.00 49.91 ? 312 HOH D O   1 
HETATM 11503 O  O   . HOH FA 6 .   ? 70.168  126.765 -7.235  1.00 47.58 ? 313 HOH D O   1 
HETATM 11504 O  O   . HOH FA 6 .   ? 59.085  118.417 -32.100 1.00 24.49 ? 314 HOH D O   1 
HETATM 11505 O  O   . HOH FA 6 .   ? 56.924  116.619 -6.058  1.00 39.43 ? 315 HOH D O   1 
HETATM 11506 O  O   . HOH FA 6 .   ? 60.442  112.179 -21.571 1.00 16.91 ? 316 HOH D O   1 
HETATM 11507 O  O   . HOH FA 6 .   ? 52.166  123.367 -8.723  1.00 44.73 ? 317 HOH D O   1 
HETATM 11508 O  O   . HOH FA 6 .   ? 54.239  122.371 -30.306 1.00 44.23 ? 318 HOH D O   1 
HETATM 11509 O  O   . HOH FA 6 .   ? 51.283  112.109 -20.066 1.00 22.38 ? 319 HOH D O   1 
HETATM 11510 O  O   . HOH FA 6 .   ? 66.745  123.625 -1.410  1.00 44.13 ? 320 HOH D O   1 
HETATM 11511 O  O   . HOH FA 6 .   ? 61.989  117.767 -2.317  1.00 40.81 ? 321 HOH D O   1 
HETATM 11512 O  O   . HOH FA 6 .   ? 62.349  130.867 -14.648 1.00 43.10 ? 322 HOH D O   1 
HETATM 11513 O  O   . HOH FA 6 .   ? 46.108  116.343 -15.731 1.00 31.13 ? 323 HOH D O   1 
HETATM 11514 O  O   . HOH FA 6 .   ? 63.839  119.146 -35.391 1.00 27.40 ? 324 HOH D O   1 
HETATM 11515 O  O   . HOH FA 6 .   ? 55.812  130.300 -18.835 1.00 41.42 ? 325 HOH D O   1 
HETATM 11516 O  O   . HOH FA 6 .   ? 65.831  109.851 -1.048  1.00 51.14 ? 326 HOH D O   1 
HETATM 11517 O  O   . HOH FA 6 .   ? 44.255  113.437 -18.295 1.00 44.73 ? 327 HOH D O   1 
HETATM 11518 O  O   . HOH FA 6 .   ? 60.396  136.774 -8.063  1.00 46.14 ? 328 HOH D O   1 
HETATM 11519 O  O   . HOH FA 6 .   ? 70.061  105.538 -11.211 1.00 51.57 ? 329 HOH D O   1 
HETATM 11520 O  O   . HOH FA 6 .   ? 69.966  111.242 -17.897 1.00 36.84 ? 330 HOH D O   1 
HETATM 11521 O  O   . HOH FA 6 .   ? 63.317  134.618 -28.036 1.00 45.21 ? 331 HOH D O   1 
HETATM 11522 O  O   . HOH FA 6 .   ? 69.876  111.963 -4.691  1.00 36.64 ? 332 HOH D O   1 
HETATM 11523 O  O   . HOH FA 6 .   ? 67.409  112.477 -5.006  1.00 34.38 ? 333 HOH D O   1 
HETATM 11524 O  O   . HOH FA 6 .   ? 60.456  113.526 -39.111 1.00 25.56 ? 334 HOH D O   1 
HETATM 11525 O  O   . HOH FA 6 .   ? 53.641  111.831 -25.968 1.00 44.70 ? 335 HOH D O   1 
HETATM 11526 O  O   . HOH FA 6 .   ? 46.072  118.871 -16.855 1.00 40.13 ? 336 HOH D O   1 
HETATM 11527 O  O   . HOH FA 6 .   ? 63.773  134.192 -30.215 1.00 44.07 ? 337 HOH D O   1 
HETATM 11528 O  O   . HOH FA 6 .   ? 60.902  127.071 -33.412 1.00 32.23 ? 338 HOH D O   1 
HETATM 11529 O  O   . HOH FA 6 .   ? 70.983  112.179 -16.168 1.00 52.83 ? 339 HOH D O   1 
HETATM 11530 O  O   . HOH FA 6 .   ? 55.983  115.145 -25.491 1.00 37.44 ? 340 HOH D O   1 
HETATM 11531 O  O   . HOH FA 6 .   ? 52.534  133.996 -21.081 1.00 49.07 ? 341 HOH D O   1 
HETATM 11532 O  O   . HOH FA 6 .   ? 67.588  134.110 -11.838 1.00 45.28 ? 342 HOH D O   1 
HETATM 11533 O  O   . HOH FA 6 .   ? 68.084  123.931 -34.884 1.00 28.81 ? 343 HOH D O   1 
HETATM 11534 O  O   . HOH FA 6 .   ? 66.559  131.977 -35.560 1.00 37.29 ? 344 HOH D O   1 
HETATM 11535 O  O   . HOH FA 6 .   ? 62.785  114.824 -29.271 1.00 40.56 ? 345 HOH D O   1 
HETATM 11536 O  O   . HOH FA 6 .   ? 76.921  128.272 -30.656 1.00 54.50 ? 346 HOH D O   1 
HETATM 11537 O  O   . HOH FA 6 .   ? 57.928  122.465 -31.827 1.00 29.31 ? 347 HOH D O   1 
HETATM 11538 O  O   . HOH FA 6 .   ? 69.611  127.309 -11.064 1.00 43.63 ? 348 HOH D O   1 
HETATM 11539 O  O   . HOH FA 6 .   ? 51.442  128.556 -21.736 1.00 45.69 ? 349 HOH D O   1 
HETATM 11540 O  O   . HOH FA 6 .   ? 56.875  126.624 -5.400  1.00 34.15 ? 350 HOH D O   1 
HETATM 11541 O  O   . HOH FA 6 .   ? 51.558  116.864 -6.788  1.00 49.82 ? 351 HOH D O   1 
HETATM 11542 O  O   . HOH FA 6 .   ? 69.634  105.940 -8.085  1.00 49.79 ? 352 HOH D O   1 
HETATM 11543 O  O   . HOH FA 6 .   ? 74.021  126.913 -27.927 1.00 38.11 ? 353 HOH D O   1 
HETATM 11544 O  O   . HOH FA 6 .   ? 60.012  131.148 -30.739 1.00 33.01 ? 354 HOH D O   1 
HETATM 11545 O  O   . HOH FA 6 .   ? 73.350  127.120 -13.198 1.00 42.63 ? 355 HOH D O   1 
HETATM 11546 O  O   . HOH FA 6 .   ? 60.337  117.343 1.018   1.00 38.42 ? 356 HOH D O   1 
HETATM 11547 O  O   . HOH FA 6 .   ? 53.397  130.920 -20.714 1.00 47.09 ? 357 HOH D O   1 
HETATM 11548 O  O   . HOH FA 6 .   ? 73.406  116.459 -5.254  1.00 34.37 ? 358 HOH D O   1 
HETATM 11549 O  O   . HOH FA 6 .   ? 74.509  117.463 -26.013 1.00 52.92 ? 359 HOH D O   1 
HETATM 11550 O  O   . HOH FA 6 .   ? 50.768  118.185 -8.229  1.00 41.56 ? 360 HOH D O   1 
HETATM 11551 O  O   . HOH FA 6 .   ? 69.352  121.907 -2.292  1.00 45.01 ? 361 HOH D O   1 
HETATM 11552 O  O   . HOH FA 6 .   ? 67.841  107.153 -10.901 1.00 38.45 ? 362 HOH D O   1 
HETATM 11553 O  O   . HOH FA 6 .   ? 61.366  128.689 -31.394 1.00 31.80 ? 363 HOH D O   1 
HETATM 11554 O  O   . HOH FA 6 .   ? 53.680  122.456 -36.819 1.00 38.89 ? 364 HOH D O   1 
HETATM 11555 O  O   . HOH FA 6 .   ? 52.267  129.377 -14.017 1.00 42.14 ? 365 HOH D O   1 
HETATM 11556 O  O   . HOH FA 6 .   ? 57.355  112.327 -22.577 1.00 26.54 ? 366 HOH D O   1 
HETATM 11557 O  O   . HOH FA 6 .   ? 66.322  117.025 -37.730 1.00 41.13 ? 367 HOH D O   1 
HETATM 11558 O  O   . HOH FA 6 .   ? 62.813  109.443 -6.301  1.00 45.86 ? 368 HOH D O   1 
HETATM 11559 O  O   . HOH FA 6 .   ? 69.638  124.841 -38.188 1.00 44.08 ? 369 HOH D O   1 
HETATM 11560 O  O   . HOH FA 6 .   ? 65.759  136.798 -27.116 1.00 36.27 ? 370 HOH D O   1 
HETATM 11561 O  O   . HOH FA 6 .   ? 73.217  135.866 -35.482 1.00 45.80 ? 371 HOH D O   1 
HETATM 11562 O  O   . HOH FA 6 .   ? 61.724  136.938 -26.386 1.00 46.34 ? 372 HOH D O   1 
HETATM 11563 O  O   . HOH FA 6 .   ? 75.623  120.759 -15.759 1.00 46.03 ? 373 HOH D O   1 
HETATM 11564 O  O   . HOH FA 6 .   ? 42.712  115.950 -21.842 1.00 52.43 ? 374 HOH D O   1 
HETATM 11565 O  O   . HOH FA 6 .   ? 77.904  125.522 -25.814 1.00 50.11 ? 375 HOH D O   1 
HETATM 11566 O  O   . HOH FA 6 .   ? 70.675  110.798 -22.447 1.00 42.93 ? 376 HOH D O   1 
HETATM 11567 O  O   . HOH FA 6 .   ? 71.902  113.885 -23.857 1.00 51.30 ? 377 HOH D O   1 
HETATM 11568 O  O   . HOH FA 6 .   ? 53.324  126.311 -29.823 1.00 49.48 ? 378 HOH D O   1 
HETATM 11569 O  O   . HOH FA 6 .   ? 50.777  126.688 -25.977 1.00 34.83 ? 379 HOH D O   1 
HETATM 11570 O  O   . HOH FA 6 .   ? 74.764  115.967 -9.192  1.00 49.04 ? 380 HOH D O   1 
HETATM 11571 O  O   . HOH FA 6 .   ? 49.805  128.439 -17.359 1.00 48.03 ? 381 HOH D O   1 
HETATM 11572 O  O   . HOH FA 6 .   ? 60.515  110.660 -3.377  1.00 46.52 ? 382 HOH D O   1 
HETATM 11573 O  O   . HOH FA 6 .   ? 69.607  99.099  -13.337 1.00 54.02 ? 383 HOH D O   1 
HETATM 11574 O  O   . HOH FA 6 .   ? 50.305  113.597 -27.445 1.00 51.19 ? 384 HOH D O   1 
HETATM 11575 O  O   . HOH FA 6 .   ? 76.333  129.228 -38.699 1.00 53.73 ? 385 HOH D O   1 
HETATM 11576 O  O   . HOH FA 6 .   ? 74.588  120.416 -29.559 1.00 46.88 ? 386 HOH D O   1 
HETATM 11577 O  O   . HOH FA 6 .   ? 76.949  126.928 -17.497 1.00 38.13 ? 387 HOH D O   1 
HETATM 11578 O  O   . HOH FA 6 .   ? 63.507  137.299 -4.817  1.00 50.96 ? 388 HOH D O   1 
HETATM 11579 O  O   . HOH FA 6 .   ? 47.985  126.163 -17.456 1.00 42.91 ? 389 HOH D O   1 
HETATM 11580 O  O   . HOH FA 6 .   ? 71.626  126.899 -19.776 1.00 36.06 ? 390 HOH D O   1 
HETATM 11581 O  O   . HOH FA 6 .   ? 71.582  116.088 -25.159 1.00 44.37 ? 391 HOH D O   1 
HETATM 11582 O  O   . HOH FA 6 .   ? 49.055  131.633 -16.280 1.00 59.41 ? 392 HOH D O   1 
HETATM 11583 O  O   . HOH FA 6 .   ? 52.626  128.977 -19.062 1.00 43.81 ? 393 HOH D O   1 
HETATM 11584 O  O   . HOH FA 6 .   ? 47.511  143.274 -14.885 1.00 53.90 ? 394 HOH D O   1 
HETATM 11585 O  O   . HOH FA 6 .   ? 68.263  134.201 -18.001 1.00 40.50 ? 395 HOH D O   1 
HETATM 11586 O  O   . HOH FA 6 .   ? 68.409  100.164 -19.884 1.00 47.28 ? 396 HOH D O   1 
HETATM 11587 O  O   . HOH FA 6 .   ? 76.003  131.170 -32.263 1.00 55.36 ? 397 HOH D O   1 
HETATM 11588 O  O   . HOH FA 6 .   ? 54.084  111.582 -23.315 1.00 38.93 ? 398 HOH D O   1 
HETATM 11589 O  O   . HOH FA 6 .   ? 63.485  139.114 -20.801 1.00 51.04 ? 399 HOH D O   1 
HETATM 11590 O  O   . HOH FA 6 .   ? 79.394  113.874 -3.504  1.00 61.56 ? 400 HOH D O   1 
HETATM 11591 O  O   . HOH FA 6 .   ? 51.871  128.754 -16.601 1.00 50.59 ? 401 HOH D O   1 
HETATM 11592 O  O   . HOH FA 6 .   ? 69.904  115.951 -27.734 1.00 47.63 ? 402 HOH D O   1 
HETATM 11593 O  O   . HOH FA 6 .   ? 65.221  114.676 -29.833 1.00 50.49 ? 403 HOH D O   1 
HETATM 11594 O  O   . HOH FA 6 .   ? 74.908  128.596 -23.879 1.00 44.16 ? 404 HOH D O   1 
HETATM 11595 O  O   . HOH FA 6 .   ? 70.280  109.897 -3.117  1.00 43.37 ? 405 HOH D O   1 
HETATM 11596 O  O   . HOH FA 6 .   ? 78.385  120.748 -13.598 1.00 50.75 ? 406 HOH D O   1 
HETATM 11597 O  O   . HOH FA 6 .   ? 69.709  101.757 -11.902 1.00 48.89 ? 407 HOH D O   1 
HETATM 11598 O  O   . HOH FA 6 .   ? 54.385  113.096 -6.505  1.00 48.41 ? 408 HOH D O   1 
HETATM 11599 O  O   . HOH FA 6 .   ? 67.526  115.907 -30.146 1.00 46.83 ? 409 HOH D O   1 
HETATM 11600 O  O   . HOH FA 6 .   ? 58.634  141.810 -8.581  1.00 49.72 ? 410 HOH D O   1 
HETATM 11601 O  O   . HOH FA 6 .   ? 72.166  129.855 -40.610 1.00 53.70 ? 411 HOH D O   1 
HETATM 11602 O  O   . HOH FA 6 .   ? 57.254  125.270 -32.796 1.00 36.93 ? 412 HOH D O   1 
HETATM 11603 O  O   . HOH FA 6 .   ? 41.848  115.775 -24.065 1.00 51.90 ? 413 HOH D O   1 
HETATM 11604 O  O   . HOH FA 6 .   ? 41.446  114.470 -19.960 1.00 56.80 ? 414 HOH D O   1 
HETATM 11605 O  O   . HOH FA 6 .   ? 80.292  111.415 -3.875  1.00 52.45 ? 415 HOH D O   1 
HETATM 11606 O  O   . HOH FA 6 .   ? 45.460  120.505 -3.887  1.00 49.28 ? 416 HOH D O   1 
HETATM 11607 O  O   . HOH GA 6 .   ? 48.757  105.460 -22.632 1.00 52.77 ? 301 HOH C O   1 
HETATM 11608 O  O   . HOH GA 6 .   ? 40.026  100.152 -5.694  1.00 55.09 ? 302 HOH C O   1 
HETATM 11609 O  O   . HOH GA 6 .   ? 68.086  83.045  -18.691 1.00 49.50 ? 303 HOH C O   1 
HETATM 11610 O  O   . HOH GA 6 .   ? 40.525  93.172  -16.015 1.00 44.91 ? 304 HOH C O   1 
HETATM 11611 O  O   . HOH GA 6 .   ? 66.064  93.280  -5.004  1.00 39.64 ? 305 HOH C O   1 
HETATM 11612 O  O   . HOH GA 6 .   ? 57.729  85.737  -4.289  1.00 46.25 ? 306 HOH C O   1 
HETATM 11613 O  O   . HOH GA 6 .   ? 48.366  88.339  -29.367 1.00 40.52 ? 307 HOH C O   1 
HETATM 11614 O  O   . HOH GA 6 .   ? 46.705  93.028  -7.358  1.00 42.86 ? 308 HOH C O   1 
HETATM 11615 O  O   . HOH GA 6 .   ? 51.937  105.312 -32.346 1.00 43.70 ? 309 HOH C O   1 
HETATM 11616 O  O   . HOH GA 6 .   ? 65.074  89.043  -22.270 1.00 48.23 ? 310 HOH C O   1 
HETATM 11617 O  O   . HOH GA 6 .   ? 54.261  109.293 -25.202 1.00 37.52 ? 311 HOH C O   1 
HETATM 11618 O  O   . HOH GA 6 .   ? 51.628  102.767 -1.675  1.00 37.90 ? 312 HOH C O   1 
HETATM 11619 O  O   . HOH GA 6 .   ? 35.834  98.322  -31.234 1.00 44.25 ? 313 HOH C O   1 
HETATM 11620 O  O   . HOH GA 6 .   ? 37.011  96.657  -27.112 1.00 31.03 ? 314 HOH C O   1 
HETATM 11621 O  O   . HOH GA 6 .   ? 44.342  110.099 -15.785 1.00 35.71 ? 315 HOH C O   1 
HETATM 11622 O  O   . HOH GA 6 .   ? 43.605  94.828  -2.955  1.00 47.78 ? 316 HOH C O   1 
HETATM 11623 O  O   . HOH GA 6 .   ? 53.725  84.845  -26.143 1.00 31.27 ? 317 HOH C O   1 
HETATM 11624 O  O   . HOH GA 6 .   ? 45.960  92.995  -10.809 1.00 38.90 ? 318 HOH C O   1 
HETATM 11625 O  O   . HOH GA 6 .   ? 58.575  110.917 -26.066 1.00 45.01 ? 319 HOH C O   1 
HETATM 11626 O  O   . HOH GA 6 .   ? 62.719  84.731  -6.934  1.00 39.44 ? 320 HOH C O   1 
HETATM 11627 O  O   . HOH GA 6 .   ? 59.193  91.529  -24.305 1.00 33.38 ? 321 HOH C O   1 
HETATM 11628 O  O   . HOH GA 6 .   ? 45.958  92.019  -17.154 1.00 18.92 ? 322 HOH C O   1 
HETATM 11629 O  O   . HOH GA 6 .   ? 52.507  90.017  -16.300 1.00 22.19 ? 323 HOH C O   1 
HETATM 11630 O  O   . HOH GA 6 .   ? 47.251  89.295  -31.594 1.00 38.67 ? 324 HOH C O   1 
HETATM 11631 O  O   . HOH GA 6 .   ? 57.682  92.029  -6.937  1.00 25.81 ? 325 HOH C O   1 
HETATM 11632 O  O   . HOH GA 6 .   ? 59.991  88.423  -24.998 1.00 34.83 ? 326 HOH C O   1 
HETATM 11633 O  O   . HOH GA 6 .   ? 63.581  86.938  -5.048  1.00 41.18 ? 327 HOH C O   1 
HETATM 11634 O  O   . HOH GA 6 .   ? 49.879  96.466  -34.405 1.00 21.84 ? 328 HOH C O   1 
HETATM 11635 O  O   . HOH GA 6 .   ? 40.134  99.018  -37.047 1.00 42.64 ? 329 HOH C O   1 
HETATM 11636 O  O   . HOH GA 6 .   ? 55.061  80.903  -23.867 1.00 22.67 ? 330 HOH C O   1 
HETATM 11637 O  O   . HOH GA 6 .   ? 67.810  102.962 -20.101 1.00 32.85 ? 331 HOH C O   1 
HETATM 11638 O  O   . HOH GA 6 .   ? 57.698  78.928  -16.706 1.00 22.06 ? 332 HOH C O   1 
HETATM 11639 O  O   . HOH GA 6 .   ? 68.053  76.923  -20.691 1.00 34.54 ? 333 HOH C O   1 
HETATM 11640 O  O   . HOH GA 6 .   ? 52.875  110.064 -21.166 1.00 18.33 ? 334 HOH C O   1 
HETATM 11641 O  O   . HOH GA 6 .   ? 63.518  97.280  -11.637 1.00 31.33 ? 335 HOH C O   1 
HETATM 11642 O  O   . HOH GA 6 .   ? 53.738  75.722  -17.540 1.00 27.81 ? 336 HOH C O   1 
HETATM 11643 O  O   . HOH GA 6 .   ? 56.765  101.118 -32.380 1.00 37.25 ? 337 HOH C O   1 
HETATM 11644 O  O   . HOH GA 6 .   ? 34.466  95.913  -29.001 1.00 48.78 ? 338 HOH C O   1 
HETATM 11645 O  O   . HOH GA 6 .   ? 46.774  107.574 -3.147  1.00 42.02 ? 339 HOH C O   1 
HETATM 11646 O  O   . HOH GA 6 .   ? 51.282  92.121  -32.638 1.00 26.86 ? 340 HOH C O   1 
HETATM 11647 O  O   . HOH GA 6 .   ? 56.297  83.718  -11.454 1.00 31.00 ? 341 HOH C O   1 
HETATM 11648 O  O   . HOH GA 6 .   ? 62.266  110.067 -21.282 1.00 21.39 ? 342 HOH C O   1 
HETATM 11649 O  O   . HOH GA 6 .   ? 59.325  103.555 -7.316  1.00 29.36 ? 343 HOH C O   1 
HETATM 11650 O  O   . HOH GA 6 .   ? 43.232  109.119 -13.355 1.00 36.70 ? 344 HOH C O   1 
HETATM 11651 O  O   . HOH GA 6 .   ? 42.506  99.874  -34.250 1.00 22.23 ? 345 HOH C O   1 
HETATM 11652 O  O   . HOH GA 6 .   ? 57.747  91.695  -21.856 1.00 23.95 ? 346 HOH C O   1 
HETATM 11653 O  O   . HOH GA 6 .   ? 56.912  106.990 -26.625 1.00 43.89 ? 347 HOH C O   1 
HETATM 11654 O  O   . HOH GA 6 .   ? 68.186  105.164 -18.533 1.00 34.32 ? 348 HOH C O   1 
HETATM 11655 O  O   . HOH GA 6 .   ? 69.257  105.602 -22.454 1.00 41.66 ? 349 HOH C O   1 
HETATM 11656 O  O   . HOH GA 6 .   ? 37.453  88.642  -35.398 1.00 42.94 ? 350 HOH C O   1 
HETATM 11657 O  O   . HOH GA 6 .   ? 59.645  93.354  -8.021  1.00 21.81 ? 351 HOH C O   1 
HETATM 11658 O  O   . HOH GA 6 .   ? 63.068  88.275  -13.959 1.00 29.04 ? 352 HOH C O   1 
HETATM 11659 O  O   . HOH GA 6 .   ? 58.577  107.792 -8.733  1.00 41.09 ? 353 HOH C O   1 
HETATM 11660 O  O   . HOH GA 6 .   ? 46.619  87.479  -6.054  1.00 45.44 ? 354 HOH C O   1 
HETATM 11661 O  O   . HOH GA 6 .   ? 50.694  86.364  -28.964 1.00 35.66 ? 355 HOH C O   1 
HETATM 11662 O  O   . HOH GA 6 .   ? 49.438  99.919  -4.036  1.00 36.82 ? 356 HOH C O   1 
HETATM 11663 O  O   . HOH GA 6 .   ? 54.726  101.567 -2.765  1.00 25.43 ? 357 HOH C O   1 
HETATM 11664 O  O   . HOH GA 6 .   ? 61.003  96.153  -29.095 1.00 27.57 ? 358 HOH C O   1 
HETATM 11665 O  O   . HOH GA 6 .   ? 69.453  108.675 -20.498 1.00 42.40 ? 359 HOH C O   1 
HETATM 11666 O  O   . HOH GA 6 .   ? 63.050  92.874  -14.542 1.00 38.24 ? 360 HOH C O   1 
HETATM 11667 O  O   . HOH GA 6 .   ? 50.111  89.566  -6.549  1.00 42.01 ? 361 HOH C O   1 
HETATM 11668 O  O   . HOH GA 6 .   ? 58.485  82.837  -14.430 1.00 31.45 ? 362 HOH C O   1 
HETATM 11669 O  O   . HOH GA 6 .   ? 43.150  103.060 -3.728  1.00 31.79 ? 363 HOH C O   1 
HETATM 11670 O  O   . HOH GA 6 .   ? 41.126  91.857  -36.461 1.00 43.13 ? 364 HOH C O   1 
HETATM 11671 O  O   . HOH GA 6 .   ? 45.303  114.029 -8.176  1.00 50.39 ? 365 HOH C O   1 
HETATM 11672 O  O   . HOH GA 6 .   ? 38.426  102.971 -22.345 1.00 46.28 ? 366 HOH C O   1 
HETATM 11673 O  O   . HOH GA 6 .   ? 47.375  113.280 -8.658  1.00 31.47 ? 367 HOH C O   1 
HETATM 11674 O  O   . HOH GA 6 .   ? 49.801  94.301  -2.141  1.00 48.70 ? 368 HOH C O   1 
HETATM 11675 O  O   . HOH GA 6 .   ? 38.980  95.419  -25.678 1.00 20.85 ? 369 HOH C O   1 
HETATM 11676 O  O   . HOH GA 6 .   ? 43.703  92.001  -35.882 1.00 23.80 ? 370 HOH C O   1 
HETATM 11677 O  O   . HOH GA 6 .   ? 62.054  92.048  -17.773 1.00 25.30 ? 371 HOH C O   1 
HETATM 11678 O  O   . HOH GA 6 .   ? 49.677  94.507  -32.542 1.00 23.17 ? 372 HOH C O   1 
HETATM 11679 O  O   . HOH GA 6 .   ? 50.176  81.143  -20.030 1.00 41.37 ? 373 HOH C O   1 
HETATM 11680 O  O   . HOH GA 6 .   ? 65.787  97.222  -23.106 1.00 42.91 ? 374 HOH C O   1 
HETATM 11681 O  O   . HOH GA 6 .   ? 42.486  93.510  -13.002 1.00 26.35 ? 375 HOH C O   1 
HETATM 11682 O  O   . HOH GA 6 .   ? 64.326  103.404 -8.582  1.00 41.36 ? 376 HOH C O   1 
HETATM 11683 O  O   . HOH GA 6 .   ? 61.989  100.784 -5.469  1.00 43.54 ? 377 HOH C O   1 
HETATM 11684 O  O   . HOH GA 6 .   ? 45.812  107.306 1.718   1.00 47.27 ? 378 HOH C O   1 
HETATM 11685 O  O   . HOH GA 6 .   ? 50.617  88.822  -31.745 1.00 46.00 ? 379 HOH C O   1 
HETATM 11686 O  O   . HOH GA 6 .   ? 56.153  109.862 -22.822 1.00 26.26 ? 380 HOH C O   1 
HETATM 11687 O  O   . HOH GA 6 .   ? 47.712  86.539  -13.120 1.00 23.45 ? 381 HOH C O   1 
HETATM 11688 O  O   . HOH GA 6 .   ? 38.231  108.417 -18.072 1.00 45.27 ? 382 HOH C O   1 
HETATM 11689 O  O   . HOH GA 6 .   ? 64.876  102.331 -10.688 1.00 35.33 ? 383 HOH C O   1 
HETATM 11690 O  O   . HOH GA 6 .   ? 43.369  94.686  -6.891  1.00 43.25 ? 384 HOH C O   1 
HETATM 11691 O  O   . HOH GA 6 .   ? 64.057  81.457  -23.729 1.00 24.71 ? 385 HOH C O   1 
HETATM 11692 O  O   . HOH GA 6 .   ? 54.662  107.827 -34.846 1.00 52.99 ? 386 HOH C O   1 
HETATM 11693 O  O   . HOH GA 6 .   ? 40.152  99.596  -14.256 1.00 47.15 ? 387 HOH C O   1 
HETATM 11694 O  O   . HOH GA 6 .   ? 56.324  108.640 -3.333  1.00 45.86 ? 388 HOH C O   1 
HETATM 11695 O  O   . HOH GA 6 .   ? 49.439  100.173 -1.696  1.00 46.93 ? 389 HOH C O   1 
HETATM 11696 O  O   . HOH GA 6 .   ? 43.249  111.541 -19.697 1.00 40.13 ? 390 HOH C O   1 
HETATM 11697 O  O   . HOH GA 6 .   ? 45.828  86.125  -28.344 1.00 30.20 ? 391 HOH C O   1 
HETATM 11698 O  O   . HOH GA 6 .   ? 68.109  97.448  -15.192 1.00 43.74 ? 392 HOH C O   1 
HETATM 11699 O  O   . HOH GA 6 .   ? 35.996  91.414  -30.923 1.00 40.54 ? 393 HOH C O   1 
HETATM 11700 O  O   . HOH GA 6 .   ? 55.776  80.000  -13.028 1.00 37.51 ? 394 HOH C O   1 
HETATM 11701 O  O   . HOH GA 6 .   ? 61.514  93.647  -25.116 1.00 44.50 ? 395 HOH C O   1 
HETATM 11702 O  O   . HOH GA 6 .   ? 53.255  82.996  -7.425  1.00 40.00 ? 396 HOH C O   1 
HETATM 11703 O  O   . HOH GA 6 .   ? 51.212  82.761  -6.701  1.00 52.13 ? 397 HOH C O   1 
HETATM 11704 O  O   . HOH GA 6 .   ? 65.052  92.352  -13.186 1.00 41.74 ? 398 HOH C O   1 
HETATM 11705 O  O   . HOH GA 6 .   ? 38.503  104.365 -28.246 1.00 48.21 ? 399 HOH C O   1 
HETATM 11706 O  O   . HOH GA 6 .   ? 53.644  90.359  -5.426  1.00 43.97 ? 400 HOH C O   1 
HETATM 11707 O  O   . HOH GA 6 .   ? 59.327  106.806 -4.933  1.00 48.79 ? 401 HOH C O   1 
HETATM 11708 O  O   . HOH GA 6 .   ? 41.518  103.056 -6.795  1.00 41.26 ? 402 HOH C O   1 
HETATM 11709 O  O   . HOH GA 6 .   ? 64.791  98.038  -4.456  1.00 48.87 ? 403 HOH C O   1 
HETATM 11710 O  O   . HOH GA 6 .   ? 66.024  93.231  -10.147 1.00 55.16 ? 404 HOH C O   1 
HETATM 11711 O  O   . HOH GA 6 .   ? 64.792  86.081  -9.296  1.00 42.33 ? 405 HOH C O   1 
HETATM 11712 O  O   . HOH GA 6 .   ? 62.131  109.389 -28.990 1.00 50.15 ? 406 HOH C O   1 
HETATM 11713 O  O   . HOH GA 6 .   ? 41.590  106.439 -23.210 1.00 38.02 ? 407 HOH C O   1 
HETATM 11714 O  O   . HOH GA 6 .   ? 39.452  89.588  -28.734 1.00 40.25 ? 408 HOH C O   1 
HETATM 11715 O  O   . HOH GA 6 .   ? 58.026  98.077  0.020   1.00 50.94 ? 409 HOH C O   1 
HETATM 11716 O  O   . HOH GA 6 .   ? 65.082  95.625  -12.647 1.00 45.68 ? 410 HOH C O   1 
HETATM 11717 O  O   . HOH GA 6 .   ? 40.920  108.525 -21.459 1.00 44.29 ? 411 HOH C O   1 
HETATM 11718 O  O   . HOH GA 6 .   ? 46.442  109.017 -35.189 1.00 52.46 ? 412 HOH C O   1 
HETATM 11719 O  O   . HOH GA 6 .   ? 42.763  106.762 -26.028 1.00 40.84 ? 413 HOH C O   1 
HETATM 11720 O  O   . HOH GA 6 .   ? 60.715  93.360  -22.984 1.00 42.13 ? 414 HOH C O   1 
HETATM 11721 O  O   . HOH GA 6 .   ? 38.808  95.713  -13.576 1.00 39.56 ? 415 HOH C O   1 
HETATM 11722 O  O   . HOH GA 6 .   ? 58.608  106.250 -28.776 1.00 47.06 ? 416 HOH C O   1 
HETATM 11723 O  O   . HOH GA 6 .   ? 65.655  95.592  -21.255 1.00 32.31 ? 417 HOH C O   1 
HETATM 11724 O  O   . HOH GA 6 .   ? 60.155  82.102  -27.702 1.00 46.33 ? 418 HOH C O   1 
HETATM 11725 O  O   . HOH GA 6 .   ? 46.125  82.176  -18.576 1.00 55.23 ? 419 HOH C O   1 
HETATM 11726 O  O   . HOH GA 6 .   ? 48.606  83.785  -13.274 1.00 40.60 ? 420 HOH C O   1 
HETATM 11727 O  O   . HOH GA 6 .   ? 48.744  92.125  -3.037  1.00 46.67 ? 421 HOH C O   1 
HETATM 11728 O  O   . HOH GA 6 .   ? 63.394  92.821  -23.794 1.00 45.99 ? 422 HOH C O   1 
HETATM 11729 O  O   . HOH GA 6 .   ? 50.793  109.370 -0.977  1.00 50.85 ? 423 HOH C O   1 
HETATM 11730 O  O   . HOH GA 6 .   ? 30.398  91.317  -35.294 1.00 55.82 ? 424 HOH C O   1 
HETATM 11731 O  O   . HOH GA 6 .   ? 47.187  82.939  -8.712  1.00 50.32 ? 425 HOH C O   1 
HETATM 11732 O  O   . HOH GA 6 .   ? 33.867  95.956  -31.158 1.00 48.36 ? 426 HOH C O   1 
HETATM 11733 O  O   . HOH GA 6 .   ? 64.314  96.192  -26.152 1.00 43.83 ? 427 HOH C O   1 
HETATM 11734 O  O   . HOH GA 6 .   ? 56.368  108.266 -31.802 1.00 50.63 ? 428 HOH C O   1 
HETATM 11735 O  O   . HOH GA 6 .   ? 63.598  100.414 -1.463  1.00 51.23 ? 429 HOH C O   1 
HETATM 11736 O  O   . HOH GA 6 .   ? 46.226  82.651  -10.922 1.00 55.22 ? 430 HOH C O   1 
HETATM 11737 O  O   . HOH GA 6 .   ? 62.107  93.388  -20.251 1.00 34.56 ? 431 HOH C O   1 
HETATM 11738 O  O   . HOH GA 6 .   ? 69.723  91.352  -7.223  1.00 53.53 ? 432 HOH C O   1 
HETATM 11739 O  O   . HOH GA 6 .   ? 44.795  107.665 -28.983 1.00 48.90 ? 433 HOH C O   1 
HETATM 11740 O  O   . HOH GA 6 .   ? 63.673  90.527  -16.035 1.00 41.03 ? 434 HOH C O   1 
HETATM 11741 O  O   . HOH GA 6 .   ? 43.199  105.385 -28.741 1.00 41.71 ? 435 HOH C O   1 
HETATM 11742 O  O   . HOH GA 6 .   ? 47.387  111.390 -28.141 1.00 50.86 ? 436 HOH C O   1 
HETATM 11743 O  O   . HOH GA 6 .   ? 47.150  109.033 -28.240 1.00 45.57 ? 437 HOH C O   1 
HETATM 11744 O  O   . HOH GA 6 .   ? 65.212  90.696  -20.519 1.00 43.91 ? 438 HOH C O   1 
HETATM 11745 O  O   . HOH GA 6 .   ? 63.694  82.456  -25.947 1.00 40.13 ? 439 HOH C O   1 
HETATM 11746 O  O   . HOH GA 6 .   ? 38.126  95.126  -39.130 1.00 50.08 ? 440 HOH C O   1 
HETATM 11747 O  O   . HOH GA 6 .   ? 61.855  91.160  -28.157 1.00 48.88 ? 441 HOH C O   1 
HETATM 11748 O  O   . HOH GA 6 .   ? 63.314  98.075  -0.473  1.00 47.73 ? 442 HOH C O   1 
HETATM 11749 O  O   . HOH GA 6 .   ? 58.889  80.831  -12.301 1.00 47.84 ? 443 HOH C O   1 
HETATM 11750 O  O   . HOH GA 6 .   ? 56.438  83.208  -27.937 1.00 55.28 ? 444 HOH C O   1 
HETATM 11751 O  O   . HOH GA 6 .   ? 36.728  103.589 -15.286 1.00 49.99 ? 445 HOH C O   1 
HETATM 11752 O  O   . HOH GA 6 .   ? 48.514  79.628  -11.780 1.00 50.56 ? 446 HOH C O   1 
HETATM 11753 O  O   . HOH GA 6 .   ? 52.656  76.813  -15.390 1.00 35.85 ? 447 HOH C O   1 
HETATM 11754 O  O   . HOH GA 6 .   ? 64.483  85.205  -3.119  1.00 49.58 ? 448 HOH C O   1 
HETATM 11755 O  O   . HOH GA 6 .   ? 61.809  106.831 -7.217  1.00 48.06 ? 449 HOH C O   1 
HETATM 11756 O  O   . HOH GA 6 .   ? 44.856  90.819  -11.091 1.00 42.88 ? 450 HOH C O   1 
HETATM 11757 O  O   . HOH GA 6 .   ? 55.270  77.703  -13.678 1.00 43.56 ? 451 HOH C O   1 
HETATM 11758 O  O   . HOH GA 6 .   ? 68.982  101.878 -25.010 1.00 48.63 ? 452 HOH C O   1 
HETATM 11759 O  O   . HOH GA 6 .   ? 57.027  76.779  -15.493 1.00 29.07 ? 453 HOH C O   1 
HETATM 11760 O  O   . HOH GA 6 .   ? 52.780  99.685  -2.060  1.00 50.95 ? 454 HOH C O   1 
HETATM 11761 O  O   . HOH GA 6 .   ? 40.662  87.025  -29.245 1.00 51.56 ? 455 HOH C O   1 
HETATM 11762 O  O   . HOH GA 6 .   ? 54.413  93.187  -3.170  1.00 46.42 ? 456 HOH C O   1 
HETATM 11763 O  O   . HOH GA 6 .   ? 54.810  82.440  -26.138 1.00 40.53 ? 457 HOH C O   1 
HETATM 11764 O  O   . HOH GA 6 .   ? 42.536  85.648  -27.514 1.00 44.45 ? 458 HOH C O   1 
HETATM 11765 O  O   . HOH GA 6 .   ? 37.021  108.858 -13.508 1.00 54.33 ? 459 HOH C O   1 
HETATM 11766 O  O   . HOH GA 6 .   ? 55.494  92.042  -4.972  1.00 45.56 ? 460 HOH C O   1 
HETATM 11767 O  O   . HOH GA 6 .   ? 68.255  111.152 -30.941 1.00 54.76 ? 461 HOH C O   1 
HETATM 11768 O  O   . HOH GA 6 .   ? 70.912  110.940 -24.833 1.00 48.01 ? 462 HOH C O   1 
HETATM 11769 O  O   . HOH GA 6 .   ? 50.693  81.833  -3.179  1.00 56.29 ? 463 HOH C O   1 
HETATM 11770 O  O   . HOH HA 6 .   ? 53.612  42.692  21.647  1.00 41.09 ? 301 HOH H O   1 
HETATM 11771 O  O   . HOH HA 6 .   ? 66.669  27.544  30.543  1.00 47.50 ? 302 HOH H O   1 
HETATM 11772 O  O   . HOH HA 6 .   ? 66.315  47.174  28.843  1.00 45.00 ? 303 HOH H O   1 
HETATM 11773 O  O   . HOH HA 6 .   ? 54.727  48.802  25.627  1.00 38.80 ? 304 HOH H O   1 
HETATM 11774 O  O   . HOH HA 6 .   ? 59.514  47.687  24.939  1.00 35.21 ? 305 HOH H O   1 
HETATM 11775 O  O   . HOH HA 6 .   ? 67.786  48.447  4.713   1.00 30.83 ? 306 HOH H O   1 
HETATM 11776 O  O   . HOH HA 6 .   ? 53.359  37.086  8.858   1.00 44.92 ? 307 HOH H O   1 
HETATM 11777 O  O   . HOH HA 6 .   ? 55.160  16.749  12.214  1.00 53.89 ? 308 HOH H O   1 
HETATM 11778 O  O   . HOH HA 6 .   ? 71.345  50.797  21.662  1.00 42.77 ? 309 HOH H O   1 
HETATM 11779 O  O   . HOH HA 6 .   ? 48.108  39.411  8.520   1.00 45.89 ? 310 HOH H O   1 
HETATM 11780 O  O   . HOH HA 6 .   ? 57.422  30.619  19.027  1.00 43.93 ? 311 HOH H O   1 
HETATM 11781 O  O   . HOH HA 6 .   ? 67.795  46.815  -2.003  1.00 27.07 ? 312 HOH H O   1 
HETATM 11782 O  O   . HOH HA 6 .   ? 60.502  42.992  31.967  1.00 29.05 ? 313 HOH H O   1 
HETATM 11783 O  O   . HOH HA 6 .   ? 75.738  34.995  27.831  1.00 47.51 ? 314 HOH H O   1 
HETATM 11784 O  O   . HOH HA 6 .   ? 61.418  48.910  21.392  1.00 19.69 ? 315 HOH H O   1 
HETATM 11785 O  O   . HOH HA 6 .   ? 66.049  45.610  1.800   1.00 28.74 ? 316 HOH H O   1 
HETATM 11786 O  O   . HOH HA 6 .   ? 69.172  33.184  35.788  1.00 40.12 ? 317 HOH H O   1 
HETATM 11787 O  O   . HOH HA 6 .   ? 72.996  34.347  22.550  1.00 37.41 ? 318 HOH H O   1 
HETATM 11788 O  O   . HOH HA 6 .   ? 71.796  40.354  -2.071  1.00 38.73 ? 319 HOH H O   1 
HETATM 11789 O  O   . HOH HA 6 .   ? 47.222  41.450  17.119  1.00 36.93 ? 320 HOH H O   1 
HETATM 11790 O  O   . HOH HA 6 .   ? 69.153  40.852  4.600   1.00 29.07 ? 321 HOH H O   1 
HETATM 11791 O  O   . HOH HA 6 .   ? 62.941  42.876  2.181   1.00 36.86 ? 322 HOH H O   1 
HETATM 11792 O  O   . HOH HA 6 .   ? 48.207  37.076  10.828  1.00 46.67 ? 323 HOH H O   1 
HETATM 11793 O  O   . HOH HA 6 .   ? 59.536  38.686  31.756  1.00 30.64 ? 324 HOH H O   1 
HETATM 11794 O  O   . HOH HA 6 .   ? 57.260  45.611  25.638  1.00 40.00 ? 325 HOH H O   1 
HETATM 11795 O  O   . HOH HA 6 .   ? 57.444  44.180  6.215   1.00 34.92 ? 326 HOH H O   1 
HETATM 11796 O  O   . HOH HA 6 .   ? 46.998  44.006  15.801  1.00 33.11 ? 327 HOH H O   1 
HETATM 11797 O  O   . HOH HA 6 .   ? 52.221  48.527  20.117  1.00 23.47 ? 328 HOH H O   1 
HETATM 11798 O  O   . HOH HA 6 .   ? 60.005  20.771  21.094  1.00 53.84 ? 329 HOH H O   1 
HETATM 11799 O  O   . HOH HA 6 .   ? 45.067  46.762  18.326  1.00 43.33 ? 330 HOH H O   1 
HETATM 11800 O  O   . HOH HA 6 .   ? 63.755  32.401  31.640  1.00 34.99 ? 331 HOH H O   1 
HETATM 11801 O  O   . HOH HA 6 .   ? 53.901  31.357  14.515  1.00 38.12 ? 332 HOH H O   1 
HETATM 11802 O  O   . HOH HA 6 .   ? 65.614  42.417  35.318  1.00 38.26 ? 333 HOH H O   1 
HETATM 11803 O  O   . HOH HA 6 .   ? 45.357  43.520  19.153  1.00 41.18 ? 334 HOH H O   1 
HETATM 11804 O  O   . HOH HA 6 .   ? 53.122  34.460  26.822  1.00 38.89 ? 335 HOH H O   1 
HETATM 11805 O  O   A HOH HA 6 .   ? 61.081  43.733  -1.008  0.47 24.56 ? 336 HOH H O   1 
HETATM 11806 O  O   B HOH HA 6 .   ? 60.447  44.524  -2.863  0.53 28.70 ? 336 HOH H O   1 
HETATM 11807 O  O   . HOH HA 6 .   ? 72.140  50.104  0.654   1.00 38.25 ? 337 HOH H O   1 
HETATM 11808 O  O   . HOH HA 6 .   ? 58.445  43.625  35.120  1.00 44.18 ? 338 HOH H O   1 
HETATM 11809 O  O   . HOH HA 6 .   ? 63.895  30.271  14.616  1.00 48.73 ? 339 HOH H O   1 
HETATM 11810 O  O   . HOH HA 6 .   ? 74.206  44.699  4.938   1.00 33.65 ? 340 HOH H O   1 
HETATM 11811 O  O   A HOH HA 6 .   ? 73.363  47.920  23.077  0.49 26.83 ? 341 HOH H O   1 
HETATM 11812 O  O   B HOH HA 6 .   ? 72.900  46.338  24.048  0.51 28.43 ? 341 HOH H O   1 
HETATM 11813 O  O   . HOH HA 6 .   ? 70.669  50.251  17.504  1.00 35.96 ? 342 HOH H O   1 
HETATM 11814 O  O   . HOH HA 6 .   ? 76.638  41.050  22.072  1.00 42.37 ? 343 HOH H O   1 
HETATM 11815 O  O   . HOH HA 6 .   ? 62.765  34.469  33.196  1.00 35.67 ? 344 HOH H O   1 
HETATM 11816 O  O   . HOH HA 6 .   ? 64.081  24.840  26.694  1.00 45.45 ? 345 HOH H O   1 
HETATM 11817 O  O   . HOH HA 6 .   ? 53.618  32.416  11.080  1.00 46.08 ? 346 HOH H O   1 
HETATM 11818 O  O   . HOH HA 6 .   ? 70.484  49.481  4.320   1.00 39.86 ? 347 HOH H O   1 
HETATM 11819 O  O   . HOH HA 6 .   ? 71.556  33.449  10.838  1.00 50.04 ? 348 HOH H O   1 
HETATM 11820 O  O   . HOH HA 6 .   ? 70.031  38.076  35.013  1.00 37.92 ? 349 HOH H O   1 
HETATM 11821 O  O   . HOH HA 6 .   ? 52.505  43.140  6.531   1.00 46.63 ? 350 HOH H O   1 
HETATM 11822 O  O   . HOH HA 6 .   ? 56.920  13.404  13.440  1.00 51.71 ? 351 HOH H O   1 
HETATM 11823 O  O   . HOH HA 6 .   ? 63.239  51.332  5.987   1.00 42.18 ? 352 HOH H O   1 
HETATM 11824 O  O   . HOH HA 6 .   ? 77.227  29.874  32.104  1.00 40.26 ? 353 HOH H O   1 
HETATM 11825 O  O   . HOH HA 6 .   ? 75.024  24.804  33.775  1.00 54.47 ? 354 HOH H O   1 
HETATM 11826 O  O   . HOH HA 6 .   ? 74.077  35.885  6.918   1.00 46.94 ? 355 HOH H O   1 
HETATM 11827 O  O   . HOH HA 6 .   ? 50.628  39.024  27.299  1.00 48.89 ? 356 HOH H O   1 
HETATM 11828 O  O   . HOH HA 6 .   ? 58.221  48.554  22.436  1.00 27.26 ? 357 HOH H O   1 
HETATM 11829 O  O   . HOH HA 6 .   ? 51.481  42.241  8.346   1.00 44.20 ? 358 HOH H O   1 
HETATM 11830 O  O   . HOH HA 6 .   ? 50.496  47.138  27.378  1.00 44.98 ? 359 HOH H O   1 
HETATM 11831 O  O   . HOH HA 6 .   ? 68.192  53.859  10.318  1.00 32.29 ? 360 HOH H O   1 
HETATM 11832 O  O   . HOH HA 6 .   ? 75.654  44.463  -1.013  1.00 48.09 ? 361 HOH H O   1 
HETATM 11833 O  O   . HOH HA 6 .   ? 73.598  35.026  19.655  1.00 35.65 ? 362 HOH H O   1 
HETATM 11834 O  O   . HOH HA 6 .   ? 53.581  40.600  28.017  1.00 50.78 ? 363 HOH H O   1 
HETATM 11835 O  O   . HOH HA 6 .   ? 55.594  38.612  29.530  1.00 49.35 ? 364 HOH H O   1 
HETATM 11836 O  O   . HOH HA 6 .   ? 62.074  30.473  30.945  1.00 43.26 ? 365 HOH H O   1 
HETATM 11837 O  O   . HOH HA 6 .   ? 67.027  24.374  3.078   1.00 59.57 ? 366 HOH H O   1 
HETATM 11838 O  O   . HOH HA 6 .   ? 71.371  54.517  18.181  1.00 49.28 ? 367 HOH H O   1 
HETATM 11839 O  O   . HOH HA 6 .   ? 72.809  39.543  1.544   1.00 47.55 ? 368 HOH H O   1 
HETATM 11840 O  O   . HOH HA 6 .   ? 70.673  33.925  7.036   1.00 42.08 ? 369 HOH H O   1 
HETATM 11841 O  O   . HOH HA 6 .   ? 68.912  30.099  35.910  1.00 42.91 ? 370 HOH H O   1 
HETATM 11842 O  O   . HOH HA 6 .   ? 53.327  31.792  21.963  1.00 48.02 ? 371 HOH H O   1 
HETATM 11843 O  O   . HOH HA 6 .   ? 75.304  45.311  8.365   1.00 42.09 ? 372 HOH H O   1 
HETATM 11844 O  O   . HOH HA 6 .   ? 74.282  34.217  13.076  1.00 38.35 ? 373 HOH H O   1 
HETATM 11845 O  O   . HOH HA 6 .   ? 55.322  29.620  20.883  1.00 54.04 ? 374 HOH H O   1 
HETATM 11846 O  O   . HOH HA 6 .   ? 75.518  33.975  19.312  1.00 50.46 ? 375 HOH H O   1 
HETATM 11847 O  O   . HOH HA 6 .   ? 68.804  34.250  2.207   1.00 45.92 ? 376 HOH H O   1 
HETATM 11848 O  O   . HOH HA 6 .   ? 69.542  63.458  16.983  1.00 50.58 ? 377 HOH H O   1 
HETATM 11849 O  O   . HOH HA 6 .   ? 68.833  61.409  18.923  1.00 51.43 ? 378 HOH H O   1 
HETATM 11850 O  O   . HOH HA 6 .   ? 51.533  32.053  17.653  1.00 50.26 ? 379 HOH H O   1 
HETATM 11851 O  O   . HOH HA 6 .   ? 74.449  28.345  28.620  1.00 47.49 ? 380 HOH H O   1 
HETATM 11852 O  O   . HOH HA 6 .   ? 49.814  34.318  17.669  1.00 39.20 ? 381 HOH H O   1 
HETATM 11853 O  O   . HOH HA 6 .   ? 54.502  31.821  19.671  1.00 48.56 ? 382 HOH H O   1 
HETATM 11854 O  O   . HOH HA 6 .   ? 67.811  46.737  30.459  1.00 46.90 ? 383 HOH H O   1 
HETATM 11855 O  O   . HOH HA 6 .   ? 68.034  30.863  5.199   1.00 52.15 ? 384 HOH H O   1 
HETATM 11856 O  O   . HOH HA 6 .   ? 62.307  27.809  -0.827  1.00 50.65 ? 385 HOH H O   1 
HETATM 11857 O  O   . HOH HA 6 .   ? 62.608  32.536  -2.888  1.00 51.48 ? 386 HOH H O   1 
HETATM 11858 O  O   . HOH HA 6 .   ? 55.012  43.679  27.871  1.00 50.25 ? 387 HOH H O   1 
HETATM 11859 O  O   . HOH HA 6 .   ? 55.888  45.510  30.251  1.00 52.81 ? 388 HOH H O   1 
HETATM 11860 O  O   . HOH HA 6 .   ? 61.122  50.333  3.853   1.00 43.43 ? 389 HOH H O   1 
HETATM 11861 O  O   . HOH HA 6 .   ? 75.616  34.295  8.752   1.00 51.38 ? 390 HOH H O   1 
HETATM 11862 O  O   . HOH HA 6 .   ? 72.602  32.828  8.680   1.00 50.88 ? 391 HOH H O   1 
HETATM 11863 O  O   . HOH HA 6 .   ? 48.404  48.668  27.245  1.00 46.29 ? 392 HOH H O   1 
HETATM 11864 O  O   . HOH HA 6 .   ? 48.056  17.031  14.363  1.00 51.29 ? 393 HOH H O   1 
HETATM 11865 O  O   . HOH HA 6 .   ? 77.333  35.054  20.975  1.00 54.00 ? 394 HOH H O   1 
HETATM 11866 O  O   . HOH HA 6 .   ? 70.942  51.383  2.466   1.00 48.46 ? 395 HOH H O   1 
HETATM 11867 O  O   . HOH HA 6 .   ? 56.506  48.251  7.546   1.00 52.59 ? 396 HOH H O   1 
HETATM 11868 O  O   . HOH HA 6 .   ? 62.144  33.651  2.765   1.00 59.72 ? 397 HOH H O   1 
HETATM 11869 O  O   . HOH HA 6 .   ? 75.220  44.783  24.919  1.00 43.52 ? 398 HOH H O   1 
HETATM 11870 O  O   . HOH HA 6 .   ? 67.514  30.565  2.953   1.00 50.63 ? 399 HOH H O   1 
HETATM 11871 O  O   . HOH HA 6 .   ? 78.437  46.262  16.310  1.00 52.01 ? 400 HOH H O   1 
HETATM 11872 O  O   . HOH HA 6 .   ? 59.502  36.019  32.987  1.00 39.31 ? 401 HOH H O   1 
HETATM 11873 O  O   . HOH HA 6 .   ? 71.863  40.417  35.378  1.00 44.80 ? 402 HOH H O   1 
HETATM 11874 O  O   . HOH HA 6 .   ? 60.321  45.569  32.798  1.00 48.72 ? 403 HOH H O   1 
HETATM 11875 O  O   . HOH HA 6 .   ? 75.876  32.887  11.135  1.00 52.96 ? 404 HOH H O   1 
HETATM 11876 O  O   . HOH HA 6 .   ? 79.617  44.871  17.572  1.00 55.35 ? 405 HOH H O   1 
HETATM 11877 O  O   . HOH HA 6 .   ? 80.021  47.122  18.621  1.00 54.46 ? 406 HOH H O   1 
HETATM 11878 O  O   . HOH HA 6 .   ? 76.349  41.212  0.626   1.00 49.34 ? 407 HOH H O   1 
HETATM 11879 O  O   . HOH HA 6 .   ? 73.403  32.038  16.197  1.00 49.25 ? 408 HOH H O   1 
HETATM 11880 O  O   . HOH HA 6 .   ? 48.538  23.199  8.910   1.00 56.10 ? 409 HOH H O   1 
HETATM 11881 O  O   . HOH HA 6 .   ? 59.494  48.164  31.943  1.00 47.78 ? 410 HOH H O   1 
HETATM 11882 O  O   . HOH HA 6 .   ? 82.357  39.530  20.105  1.00 51.89 ? 411 HOH H O   1 
HETATM 11883 O  O   . HOH IA 6 .   ? 51.264  77.458  13.727  1.00 42.80 ? 301 HOH E O   1 
HETATM 11884 O  O   . HOH IA 6 .   ? 48.517  51.072  22.203  1.00 56.04 ? 302 HOH E O   1 
HETATM 11885 O  O   . HOH IA 6 .   ? 67.568  78.829  23.082  1.00 48.96 ? 303 HOH E O   1 
HETATM 11886 O  O   . HOH IA 6 .   ? 66.051  67.733  4.980   1.00 46.20 ? 304 HOH E O   1 
HETATM 11887 O  O   . HOH IA 6 .   ? 55.399  51.589  24.939  1.00 33.41 ? 305 HOH E O   1 
HETATM 11888 O  O   . HOH IA 6 .   ? 40.360  66.763  16.196  1.00 38.08 ? 306 HOH E O   1 
HETATM 11889 O  O   . HOH IA 6 .   ? 36.781  61.262  30.972  1.00 46.73 ? 307 HOH E O   1 
HETATM 11890 O  O   . HOH IA 6 .   ? 48.844  71.941  29.707  1.00 41.93 ? 308 HOH E O   1 
HETATM 11891 O  O   . HOH IA 6 .   ? 50.133  71.171  6.614   1.00 44.95 ? 309 HOH E O   1 
HETATM 11892 O  O   . HOH IA 6 .   ? 68.324  58.500  19.574  1.00 39.41 ? 310 HOH E O   1 
HETATM 11893 O  O   . HOH IA 6 .   ? 44.089  49.081  19.631  1.00 36.97 ? 311 HOH E O   1 
HETATM 11894 O  O   . HOH IA 6 .   ? 38.426  57.571  23.680  1.00 46.72 ? 312 HOH E O   1 
HETATM 11895 O  O   . HOH IA 6 .   ? 57.404  68.757  6.785   1.00 31.27 ? 313 HOH E O   1 
HETATM 11896 O  O   . HOH IA 6 .   ? 52.425  70.481  16.355  1.00 21.57 ? 314 HOH E O   1 
HETATM 11897 O  O   . HOH IA 6 .   ? 68.686  56.135  18.114  1.00 31.26 ? 315 HOH E O   1 
HETATM 11898 O  O   . HOH IA 6 .   ? 50.584  63.465  34.369  1.00 25.49 ? 316 HOH E O   1 
HETATM 11899 O  O   . HOH IA 6 .   ? 59.883  50.103  26.216  1.00 40.48 ? 317 HOH E O   1 
HETATM 11900 O  O   . HOH IA 6 .   ? 52.007  57.544  1.660   1.00 39.28 ? 318 HOH E O   1 
HETATM 11901 O  O   . HOH IA 6 .   ? 45.968  67.197  11.136  1.00 36.91 ? 319 HOH E O   1 
HETATM 11902 O  O   . HOH IA 6 .   ? 53.330  55.251  32.322  1.00 26.45 ? 320 HOH E O   1 
HETATM 11903 O  O   . HOH IA 6 .   ? 45.995  68.098  17.444  1.00 25.07 ? 321 HOH E O   1 
HETATM 11904 O  O   . HOH IA 6 .   ? 60.974  77.799  26.823  1.00 44.05 ? 322 HOH E O   1 
HETATM 11905 O  O   . HOH IA 6 .   ? 59.489  67.521  7.836   1.00 23.85 ? 323 HOH E O   1 
HETATM 11906 O  O   . HOH IA 6 .   ? 65.014  71.307  21.639  1.00 49.41 ? 324 HOH E O   1 
HETATM 11907 O  O   . HOH IA 6 .   ? 49.776  53.692  3.466   1.00 41.18 ? 325 HOH E O   1 
HETATM 11908 O  O   . HOH IA 6 .   ? 68.356  83.938  20.465  1.00 31.58 ? 326 HOH E O   1 
HETATM 11909 O  O   . HOH IA 6 .   ? 58.813  53.375  8.553   1.00 37.23 ? 327 HOH E O   1 
HETATM 11910 O  O   . HOH IA 6 .   ? 57.108  71.594  3.699   1.00 46.33 ? 328 HOH E O   1 
HETATM 11911 O  O   . HOH IA 6 .   ? 49.237  60.808  4.202   1.00 38.53 ? 329 HOH E O   1 
HETATM 11912 O  O   . HOH IA 6 .   ? 53.687  75.874  26.177  1.00 30.22 ? 330 HOH E O   1 
HETATM 11913 O  O   . HOH IA 6 .   ? 57.945  68.770  21.657  1.00 30.54 ? 331 HOH E O   1 
HETATM 11914 O  O   . HOH IA 6 .   ? 53.807  50.561  21.073  1.00 18.87 ? 332 HOH E O   1 
HETATM 11915 O  O   . HOH IA 6 .   ? 62.546  76.113  6.779   1.00 45.46 ? 333 HOH E O   1 
HETATM 11916 O  O   . HOH IA 6 .   ? 46.690  67.417  7.589   1.00 38.79 ? 334 HOH E O   1 
HETATM 11917 O  O   . HOH IA 6 .   ? 37.736  63.390  26.945  1.00 42.25 ? 335 HOH E O   1 
HETATM 11918 O  O   . HOH IA 6 .   ? 57.476  53.320  26.078  1.00 39.43 ? 336 HOH E O   1 
HETATM 11919 O  O   . HOH IA 6 .   ? 60.136  70.586  31.939  1.00 46.50 ? 337 HOH E O   1 
HETATM 11920 O  O   . HOH IA 6 .   ? 60.277  72.224  24.869  1.00 35.05 ? 338 HOH E O   1 
HETATM 11921 O  O   . HOH IA 6 .   ? 63.122  51.039  21.022  1.00 22.71 ? 339 HOH E O   1 
HETATM 11922 O  O   . HOH IA 6 .   ? 59.712  57.074  7.235   1.00 27.68 ? 340 HOH E O   1 
HETATM 11923 O  O   . HOH IA 6 .   ? 59.649  69.228  24.033  1.00 38.90 ? 341 HOH E O   1 
HETATM 11924 O  O   . HOH IA 6 .   ? 57.934  81.558  16.555  1.00 22.26 ? 342 HOH E O   1 
HETATM 11925 O  O   . HOH IA 6 .   ? 57.875  57.699  38.826  1.00 49.45 ? 343 HOH E O   1 
HETATM 11926 O  O   . HOH IA 6 .   ? 40.079  70.169  29.462  1.00 40.70 ? 344 HOH E O   1 
HETATM 11927 O  O   . HOH IA 6 .   ? 48.057  70.592  31.782  1.00 42.38 ? 345 HOH E O   1 
HETATM 11928 O  O   . HOH IA 6 .   ? 60.509  75.769  4.148   1.00 54.08 ? 346 HOH E O   1 
HETATM 11929 O  O   . HOH IA 6 .   ? 55.915  76.987  11.429  1.00 29.36 ? 347 HOH E O   1 
HETATM 11930 O  O   . HOH IA 6 .   ? 55.286  79.610  24.001  1.00 23.98 ? 348 HOH E O   1 
HETATM 11931 O  O   . HOH IA 6 .   ? 63.029  72.352  13.684  1.00 29.05 ? 349 HOH E O   1 
HETATM 11932 O  O   . HOH IA 6 .   ? 38.843  59.053  20.888  1.00 39.21 ? 350 HOH E O   1 
HETATM 11933 O  O   . HOH IA 6 .   ? 62.032  59.799  5.339   1.00 36.51 ? 351 HOH E O   1 
HETATM 11934 O  O   . HOH IA 6 .   ? 63.571  63.537  11.178  1.00 29.34 ? 352 HOH E O   1 
HETATM 11935 O  O   . HOH IA 6 .   ? 65.428  58.836  10.384  1.00 34.71 ? 353 HOH E O   1 
HETATM 11936 O  O   . HOH IA 6 .   ? 44.091  64.933  36.000  1.00 39.41 ? 354 HOH E O   1 
HETATM 11937 O  O   . HOH IA 6 .   ? 65.551  75.894  25.407  1.00 50.34 ? 355 HOH E O   1 
HETATM 11938 O  O   . HOH IA 6 .   ? 63.252  67.913  14.140  1.00 37.56 ? 356 HOH E O   1 
HETATM 11939 O  O   . HOH IA 6 .   ? 54.123  59.557  32.875  1.00 23.62 ? 357 HOH E O   1 
HETATM 11940 O  O   . HOH IA 6 .   ? 54.088  84.913  17.327  1.00 24.28 ? 358 HOH E O   1 
HETATM 11941 O  O   . HOH IA 6 .   ? 58.411  77.780  14.275  1.00 23.17 ? 359 HOH E O   1 
HETATM 11942 O  O   . HOH IA 6 .   ? 55.149  54.232  35.280  1.00 42.64 ? 360 HOH E O   1 
HETATM 11943 O  O   . HOH IA 6 .   ? 39.545  64.543  25.557  1.00 33.53 ? 361 HOH E O   1 
HETATM 11944 O  O   . HOH IA 6 .   ? 66.322  63.863  23.010  1.00 42.07 ? 362 HOH E O   1 
HETATM 11945 O  O   . HOH IA 6 .   ? 57.126  74.837  3.898   1.00 48.78 ? 363 HOH E O   1 
HETATM 11946 O  O   . HOH IA 6 .   ? 46.756  72.839  5.952   1.00 48.39 ? 364 HOH E O   1 
HETATM 11947 O  O   . HOH IA 6 .   ? 43.554  65.578  6.991   1.00 41.70 ? 365 HOH E O   1 
HETATM 11948 O  O   . HOH IA 6 .   ? 62.192  68.711  17.365  1.00 26.16 ? 366 HOH E O   1 
HETATM 11949 O  O   . HOH IA 6 .   ? 60.925  57.888  29.632  1.00 46.75 ? 367 HOH E O   1 
HETATM 11950 O  O   . HOH IA 6 .   ? 47.205  52.772  3.031   1.00 44.51 ? 368 HOH E O   1 
HETATM 11951 O  O   . HOH IA 6 .   ? 56.820  50.977  22.520  1.00 28.42 ? 369 HOH E O   1 
HETATM 11952 O  O   . HOH IA 6 .   ? 45.230  49.970  15.728  1.00 33.65 ? 370 HOH E O   1 
HETATM 11953 O  O   . HOH IA 6 .   ? 54.742  59.189  2.655   1.00 24.22 ? 371 HOH E O   1 
HETATM 11954 O  O   . HOH IA 6 .   ? 39.570  51.675  18.703  1.00 44.39 ? 372 HOH E O   1 
HETATM 11955 O  O   . HOH IA 6 .   ? 61.517  64.505  28.935  1.00 26.94 ? 373 HOH E O   1 
HETATM 11956 O  O   . HOH IA 6 .   ? 70.267  52.803  19.886  1.00 43.73 ? 374 HOH E O   1 
HETATM 11957 O  O   . HOH IA 6 .   ? 43.563  57.208  3.780   1.00 29.00 ? 375 HOH E O   1 
HETATM 11958 O  O   . HOH IA 6 .   ? 46.100  73.912  20.123  1.00 30.22 ? 376 HOH E O   1 
HETATM 11959 O  O   . HOH IA 6 .   ? 53.882  78.420  13.049  1.00 41.25 ? 377 HOH E O   1 
HETATM 11960 O  O   . HOH IA 6 .   ? 51.725  67.900  32.735  1.00 28.58 ? 378 HOH E O   1 
HETATM 11961 O  O   . HOH IA 6 .   ? 64.427  79.026  23.311  1.00 28.00 ? 379 HOH E O   1 
HETATM 11962 O  O   . HOH IA 6 .   ? 35.088  64.521  28.853  1.00 50.38 ? 380 HOH E O   1 
HETATM 11963 O  O   . HOH IA 6 .   ? 42.451  64.965  23.069  1.00 34.83 ? 381 HOH E O   1 
HETATM 11964 O  O   . HOH IA 6 .   ? 54.046  50.208  5.539   1.00 46.83 ? 382 HOH E O   1 
HETATM 11965 O  O   . HOH IA 6 .   ? 41.529  68.148  36.989  1.00 49.86 ? 383 HOH E O   1 
HETATM 11966 O  O   . HOH IA 6 .   ? 42.368  66.655  13.141  1.00 31.43 ? 384 HOH E O   1 
HETATM 11967 O  O   . HOH IA 6 .   ? 66.013  66.670  9.489   1.00 49.11 ? 385 HOH E O   1 
HETATM 11968 O  O   . HOH IA 6 .   ? 46.060  74.081  28.618  1.00 32.64 ? 386 HOH E O   1 
HETATM 11969 O  O   . HOH IA 6 .   ? 52.952  77.647  7.370   1.00 45.30 ? 387 HOH E O   1 
HETATM 11970 O  O   . HOH IA 6 .   ? 42.563  53.773  23.418  1.00 39.48 ? 388 HOH E O   1 
HETATM 11971 O  O   . HOH IA 6 .   ? 44.566  45.263  15.344  1.00 57.61 ? 389 HOH E O   1 
HETATM 11972 O  O   . HOH IA 6 .   ? 50.345  65.720  32.722  1.00 29.61 ? 390 HOH E O   1 
HETATM 11973 O  O   . HOH IA 6 .   ? 50.788  74.580  28.836  1.00 37.34 ? 391 HOH E O   1 
HETATM 11974 O  O   . HOH IA 6 .   ? 48.448  47.173  8.661   1.00 34.21 ? 392 HOH E O   1 
HETATM 11975 O  O   . HOH IA 6 .   ? 50.260  77.528  5.956   1.00 55.12 ? 393 HOH E O   1 
HETATM 11976 O  O   . HOH IA 6 .   ? 50.671  51.570  28.900  1.00 42.23 ? 394 HOH E O   1 
HETATM 11977 O  O   . HOH IA 6 .   ? 53.396  70.301  5.413   1.00 43.23 ? 395 HOH E O   1 
HETATM 11978 O  O   . HOH IA 6 .   ? 61.028  67.385  22.605  1.00 39.04 ? 396 HOH E O   1 
HETATM 11979 O  O   . HOH IA 6 .   ? 44.168  67.672  36.428  1.00 39.38 ? 397 HOH E O   1 
HETATM 11980 O  O   . HOH IA 6 .   ? 65.468  65.476  12.447  1.00 45.45 ? 398 HOH E O   1 
HETATM 11981 O  O   . HOH IA 6 .   ? 58.487  63.879  32.211  1.00 46.66 ? 399 HOH E O   1 
HETATM 11982 O  O   . HOH IA 6 .   ? 42.003  56.662  6.589   1.00 46.43 ? 400 HOH E O   1 
HETATM 11983 O  O   . HOH IA 6 .   ? 37.796  64.177  15.004  1.00 51.19 ? 401 HOH E O   1 
HETATM 11984 O  O   . HOH IA 6 .   ? 36.509  68.325  31.329  1.00 41.18 ? 402 HOH E O   1 
HETATM 11985 O  O   . HOH IA 6 .   ? 64.876  57.651  8.509   1.00 42.62 ? 403 HOH E O   1 
HETATM 11986 O  O   . HOH IA 6 .   ? 49.565  60.434  1.646   1.00 47.68 ? 404 HOH E O   1 
HETATM 11987 O  O   A HOH IA 6 .   ? 60.501  54.922  22.165  0.55 27.13 ? 405 HOH E O   1 
HETATM 11988 O  O   B HOH IA 6 .   ? 61.408  56.468  23.122  0.45 20.62 ? 405 HOH E O   1 
HETATM 11989 O  O   . HOH IA 6 .   ? 58.771  59.525  30.609  1.00 42.37 ? 406 HOH E O   1 
HETATM 11990 O  O   . HOH IA 6 .   ? 55.628  80.641  12.974  1.00 35.22 ? 407 HOH E O   1 
HETATM 11991 O  O   . HOH IA 6 .   ? 62.533  66.617  26.018  1.00 42.10 ? 408 HOH E O   1 
HETATM 11992 O  O   . HOH IA 6 .   ? 41.886  51.749  21.575  1.00 43.54 ? 409 HOH E O   1 
HETATM 11993 O  O   . HOH IA 6 .   ? 56.722  51.955  2.777   1.00 49.35 ? 410 HOH E O   1 
HETATM 11994 O  O   . HOH IA 6 .   ? 46.790  49.948  3.595   1.00 52.79 ? 411 HOH E O   1 
HETATM 11995 O  O   . HOH IA 6 .   ? 47.271  73.958  13.445  1.00 24.09 ? 412 HOH E O   1 
HETATM 11996 O  O   . HOH IA 6 .   ? 69.873  56.613  24.172  1.00 60.12 ? 413 HOH E O   1 
HETATM 11997 O  O   . HOH IA 6 .   ? 53.018  78.408  25.145  1.00 41.29 ? 414 HOH E O   1 
HETATM 11998 O  O   . HOH IA 6 .   ? 53.015  56.247  -0.026  1.00 43.01 ? 415 HOH E O   1 
HETATM 11999 O  O   . HOH IA 6 .   ? 59.306  55.462  28.120  1.00 44.21 ? 416 HOH E O   1 
HETATM 12000 O  O   . HOH IA 6 .   ? 55.730  76.725  27.481  1.00 51.60 ? 417 HOH E O   1 
HETATM 12001 O  O   . HOH IA 6 .   ? 59.262  53.779  4.660   1.00 48.48 ? 418 HOH E O   1 
HETATM 12002 O  O   . HOH IA 6 .   ? 35.903  51.643  9.438   1.00 53.52 ? 419 HOH E O   1 
HETATM 12003 O  O   . HOH IA 6 .   ? 64.444  67.512  20.944  1.00 47.57 ? 420 HOH E O   1 
HETATM 12004 O  O   . HOH IA 6 .   ? 55.354  52.245  33.010  1.00 45.53 ? 421 HOH E O   1 
HETATM 12005 O  O   . HOH IA 6 .   ? 59.012  53.152  28.928  1.00 49.39 ? 422 HOH E O   1 
HETATM 12006 O  O   . HOH IA 6 .   ? 58.986  52.851  23.475  1.00 37.75 ? 423 HOH E O   1 
HETATM 12007 O  O   . HOH IA 6 .   ? 65.192  72.353  10.605  1.00 46.74 ? 424 HOH E O   1 
HETATM 12008 O  O   . HOH IA 6 .   ? 66.011  65.349  21.044  1.00 36.76 ? 425 HOH E O   1 
HETATM 12009 O  O   . HOH IA 6 .   ? 66.219  69.612  11.118  1.00 50.40 ? 426 HOH E O   1 
HETATM 12010 O  O   . HOH IA 6 .   ? 62.266  67.473  20.162  1.00 35.07 ? 427 HOH E O   1 
HETATM 12011 O  O   . HOH IA 6 .   ? 58.925  53.403  31.198  1.00 51.79 ? 428 HOH E O   1 
HETATM 12012 O  O   . HOH IA 6 .   ? 64.257  61.770  8.892   1.00 42.23 ? 429 HOH E O   1 
HETATM 12013 O  O   . HOH IA 6 .   ? 61.801  61.762  29.017  1.00 44.86 ? 430 HOH E O   1 
HETATM 12014 O  O   . HOH IA 6 .   ? 63.866  68.222  23.496  1.00 48.06 ? 431 HOH E O   1 
HETATM 12015 O  O   . HOH IA 6 .   ? 50.602  51.621  0.632   1.00 53.53 ? 432 HOH E O   1 
HETATM 12016 O  O   . HOH IA 6 .   ? 43.338  58.358  34.903  1.00 48.09 ? 433 HOH E O   1 
HETATM 12017 O  O   . HOH IA 6 .   ? 66.872  73.496  5.855   1.00 50.48 ? 434 HOH E O   1 
HETATM 12018 O  O   . HOH IA 6 .   ? 61.897  69.964  28.458  1.00 48.56 ? 435 HOH E O   1 
HETATM 12019 O  O   . HOH IA 6 .   ? 58.787  74.592  0.935   1.00 49.07 ? 436 HOH E O   1 
HETATM 12020 O  O   . HOH IA 6 .   ? 63.916  78.224  26.033  1.00 37.15 ? 437 HOH E O   1 
HETATM 12021 O  O   . HOH IA 6 .   ? 58.558  79.718  12.669  1.00 44.44 ? 438 HOH E O   1 
HETATM 12022 O  O   . HOH IA 6 .   ? 44.262  68.235  13.071  1.00 43.31 ? 439 HOH E O   1 
HETATM 12023 O  O   . HOH IA 6 .   ? 63.739  70.175  15.418  1.00 39.06 ? 440 HOH E O   1 
HETATM 12024 O  O   . HOH IA 6 .   ? 62.367  62.326  2.891   1.00 45.04 ? 441 HOH E O   1 
HETATM 12025 O  O   . HOH IA 6 .   ? 57.325  61.766  33.424  1.00 47.14 ? 442 HOH E O   1 
HETATM 12026 O  O   . HOH IA 6 .   ? 52.653  60.897  2.104   1.00 46.10 ? 443 HOH E O   1 
HETATM 12027 O  O   . HOH IA 6 .   ? 53.943  62.026  34.292  1.00 32.71 ? 444 HOH E O   1 
HETATM 12028 O  O   . HOH IA 6 .   ? 69.580  58.902  11.024  1.00 46.15 ? 445 HOH E O   1 
HETATM 12029 O  O   . HOH IA 6 .   ? 57.231  83.834  15.393  1.00 24.68 ? 446 HOH E O   1 
HETATM 12030 O  O   . HOH IA 6 .   ? 71.817  51.203  23.938  1.00 46.82 ? 447 HOH E O   1 
HETATM 12031 O  O   . HOH IA 6 .   ? 38.331  54.783  24.960  1.00 53.67 ? 448 HOH E O   1 
HETATM 12032 O  O   . HOH IA 6 .   ? 53.044  83.790  15.024  1.00 27.23 ? 449 HOH E O   1 
HETATM 12033 O  O   . HOH IA 6 .   ? 55.494  83.110  13.603  1.00 35.01 ? 450 HOH E O   1 
HETATM 12034 O  O   . HOH IA 6 .   ? 37.185  56.223  14.652  1.00 46.47 ? 451 HOH E O   1 
HETATM 12035 O  O   . HOH IA 6 .   ? 41.246  57.288  33.989  1.00 35.46 ? 452 HOH E O   1 
HETATM 12036 O  O   . HOH IA 6 .   ? 53.641  66.839  34.530  1.00 42.71 ? 453 HOH E O   1 
HETATM 12037 O  O   . HOH IA 6 .   ? 56.908  51.187  4.851   1.00 55.90 ? 454 HOH E O   1 
HETATM 12038 O  O   . HOH IA 6 .   ? 49.306  77.258  3.480   1.00 51.00 ? 455 HOH E O   1 
HETATM 12039 O  O   . HOH IA 6 .   ? 43.957  70.524  3.607   1.00 51.30 ? 456 HOH E O   1 
HETATM 12040 O  O   . HOH IA 6 .   ? 41.468  46.938  16.452  1.00 56.61 ? 457 HOH E O   1 
HETATM 12041 O  O   . HOH IA 6 .   ? 56.518  66.111  37.397  1.00 56.35 ? 458 HOH E O   1 
HETATM 12042 O  O   . HOH IA 6 .   ? 34.958  51.235  11.518  1.00 54.15 ? 459 HOH E O   1 
HETATM 12043 O  O   . HOH IA 6 .   ? 51.409  51.388  -6.085  1.00 55.52 ? 460 HOH E O   1 
HETATM 12044 O  O   . HOH JA 6 .   ? 80.347  58.436  -27.824 1.00 42.84 ? 301 HOH F O   1 
HETATM 12045 O  O   . HOH JA 6 .   ? 92.051  83.557  -20.078 1.00 43.14 ? 302 HOH F O   1 
HETATM 12046 O  O   . HOH JA 6 .   ? 96.556  78.779  1.194   1.00 48.94 ? 303 HOH F O   1 
HETATM 12047 O  O   . HOH JA 6 .   ? 96.813  84.992  -20.616 1.00 45.63 ? 304 HOH F O   1 
HETATM 12048 O  O   . HOH JA 6 .   ? 95.083  70.666  -0.180  1.00 49.48 ? 305 HOH F O   1 
HETATM 12049 O  O   . HOH JA 6 .   ? 81.325  86.733  3.444   1.00 58.54 ? 306 HOH F O   1 
HETATM 12050 O  O   . HOH JA 6 .   ? 73.372  70.922  -21.449 1.00 36.48 ? 307 HOH F O   1 
HETATM 12051 O  O   . HOH JA 6 .   ? 89.658  79.367  2.923   1.00 53.57 ? 308 HOH F O   1 
HETATM 12052 O  O   . HOH JA 6 .   ? 90.867  65.694  -24.833 1.00 44.12 ? 309 HOH F O   1 
HETATM 12053 O  O   . HOH JA 6 .   ? 87.179  63.265  -24.374 1.00 44.51 ? 310 HOH F O   1 
HETATM 12054 O  O   . HOH JA 6 .   ? 99.305  74.153  -3.025  1.00 48.16 ? 311 HOH F O   1 
HETATM 12055 O  O   . HOH JA 6 .   ? 91.740  78.282  -26.843 1.00 46.04 ? 312 HOH F O   1 
HETATM 12056 O  O   . HOH JA 6 .   ? 80.279  85.816  -16.615 1.00 42.85 ? 313 HOH F O   1 
HETATM 12057 O  O   . HOH JA 6 .   ? 91.930  59.223  -17.550 1.00 47.49 ? 314 HOH F O   1 
HETATM 12058 O  O   . HOH JA 6 .   ? 74.805  69.507  -23.024 1.00 47.72 ? 315 HOH F O   1 
HETATM 12059 O  O   . HOH JA 6 .   ? 80.882  65.894  -15.163 1.00 44.19 ? 316 HOH F O   1 
HETATM 12060 O  O   . HOH JA 6 .   ? 82.657  67.773  -10.324 1.00 40.99 ? 317 HOH F O   1 
HETATM 12061 O  O   . HOH JA 6 .   ? 89.323  65.844  -8.689  1.00 46.31 ? 318 HOH F O   1 
HETATM 12062 O  O   . HOH JA 6 .   ? 80.012  77.474  -24.410 1.00 46.35 ? 319 HOH F O   1 
HETATM 12063 O  O   . HOH JA 6 .   ? 94.609  80.608  -0.643  1.00 51.02 ? 320 HOH F O   1 
HETATM 12064 O  O   . HOH JA 6 .   ? 82.191  72.594  -29.205 1.00 31.49 ? 321 HOH F O   1 
HETATM 12065 O  O   . HOH JA 6 .   ? 90.135  84.817  -16.401 1.00 32.99 ? 322 HOH F O   1 
HETATM 12066 O  O   . HOH JA 6 .   ? 80.906  68.192  -12.619 1.00 37.94 ? 323 HOH F O   1 
HETATM 12067 O  O   . HOH JA 6 .   ? 87.621  56.757  -11.242 1.00 42.65 ? 324 HOH F O   1 
HETATM 12068 O  O   . HOH JA 6 .   ? 92.696  69.337  1.260   1.00 51.90 ? 325 HOH F O   1 
HETATM 12069 O  O   . HOH JA 6 .   ? 99.319  64.792  -3.991  1.00 48.69 ? 326 HOH F O   1 
HETATM 12070 O  O   . HOH JA 6 .   ? 86.685  58.808  -13.260 1.00 38.71 ? 327 HOH F O   1 
HETATM 12071 O  O   . HOH JA 6 .   ? 77.111  79.251  -2.634  1.00 49.22 ? 328 HOH F O   1 
HETATM 12072 O  O   . HOH JA 6 .   ? 78.411  80.421  0.461   1.00 44.22 ? 329 HOH F O   1 
HETATM 12073 O  O   . HOH JA 6 .   ? 76.982  69.523  -21.667 1.00 37.35 ? 330 HOH F O   1 
HETATM 12074 O  O   . HOH JA 6 .   ? 93.467  84.553  -17.346 1.00 36.48 ? 331 HOH F O   1 
HETATM 12075 O  O   . HOH JA 6 .   ? 82.159  69.325  -5.396  1.00 49.21 ? 332 HOH F O   1 
HETATM 12076 O  O   . HOH JA 6 .   ? 81.089  85.618  -12.087 1.00 46.07 ? 333 HOH F O   1 
HETATM 12077 O  O   . HOH JA 6 .   ? 103.510 72.347  -14.515 1.00 50.39 ? 334 HOH F O   1 
HETATM 12078 O  O   . HOH JA 6 .   ? 89.315  68.042  -25.823 1.00 40.05 ? 335 HOH F O   1 
HETATM 12079 O  O   . HOH JA 6 .   ? 99.370  85.161  -15.445 1.00 42.85 ? 336 HOH F O   1 
HETATM 12080 O  O   . HOH JA 6 .   ? 95.329  66.833  -13.607 1.00 46.55 ? 337 HOH F O   1 
HETATM 12081 O  O   . HOH JA 6 .   ? 83.348  89.603  -5.529  1.00 44.87 ? 338 HOH F O   1 
HETATM 12082 O  O   . HOH JA 6 .   ? 89.704  69.604  -27.876 1.00 42.77 ? 339 HOH F O   1 
HETATM 12083 O  O   . HOH JA 6 .   ? 84.173  84.528  0.719   1.00 51.33 ? 340 HOH F O   1 
HETATM 12084 O  O   . HOH JA 6 .   ? 75.563  76.325  -23.142 1.00 49.87 ? 341 HOH F O   1 
HETATM 12085 O  O   . HOH JA 6 .   ? 100.598 79.377  -3.080  1.00 50.36 ? 342 HOH F O   1 
HETATM 12086 O  O   . HOH JA 6 .   ? 82.459  77.525  -32.166 1.00 48.87 ? 343 HOH F O   1 
HETATM 12087 O  O   . HOH JA 6 .   ? 77.432  68.696  -18.558 1.00 48.96 ? 344 HOH F O   1 
HETATM 12088 O  O   . HOH JA 6 .   ? 96.441  74.746  -24.703 1.00 48.18 ? 345 HOH F O   1 
HETATM 12089 O  O   . HOH JA 6 .   ? 84.320  64.472  -29.750 1.00 42.31 ? 346 HOH F O   1 
HETATM 12090 O  O   . HOH JA 6 .   ? 99.813  70.348  -20.961 1.00 44.66 ? 347 HOH F O   1 
HETATM 12091 O  O   . HOH JA 6 .   ? 89.517  59.999  -20.611 1.00 51.51 ? 348 HOH F O   1 
HETATM 12092 O  O   . HOH JA 6 .   ? 85.519  60.147  -21.137 1.00 31.84 ? 349 HOH F O   1 
HETATM 12093 O  O   . HOH JA 6 .   ? 98.903  68.077  -8.373  1.00 51.37 ? 350 HOH F O   1 
HETATM 12094 O  O   . HOH JA 6 .   ? 79.689  68.538  -16.345 1.00 37.76 ? 351 HOH F O   1 
HETATM 12095 O  O   . HOH JA 6 .   ? 89.159  60.034  1.126   1.00 50.72 ? 352 HOH F O   1 
HETATM 12096 O  O   . HOH JA 6 .   ? 97.259  80.939  -16.171 1.00 45.71 ? 353 HOH F O   1 
HETATM 12097 O  O   . HOH JA 6 .   ? 79.533  70.080  -14.006 1.00 33.22 ? 354 HOH F O   1 
HETATM 12098 O  O   . HOH JA 6 .   ? 102.752 70.890  -11.939 1.00 47.70 ? 355 HOH F O   1 
HETATM 12099 O  O   . HOH JA 6 .   ? 83.130  65.123  -10.600 1.00 43.90 ? 356 HOH F O   1 
HETATM 12100 O  O   . HOH JA 6 .   ? 84.306  62.562  -5.980  1.00 41.38 ? 357 HOH F O   1 
HETATM 12101 O  O   . HOH JA 6 .   ? 99.393  68.965  -5.832  1.00 51.52 ? 358 HOH F O   1 
HETATM 12102 O  O   . HOH JA 6 .   ? 78.658  69.390  -7.162  1.00 46.22 ? 359 HOH F O   1 
HETATM 12103 O  O   . HOH JA 6 .   ? 97.408  66.272  -15.076 1.00 53.55 ? 360 HOH F O   1 
HETATM 12104 O  O   . HOH JA 6 .   ? 78.201  66.339  -15.995 1.00 48.83 ? 361 HOH F O   1 
HETATM 12105 O  O   . HOH JA 6 .   ? 98.575  68.295  -14.051 1.00 47.91 ? 362 HOH F O   1 
HETATM 12106 O  O   . HOH JA 6 .   ? 99.181  68.718  -11.702 1.00 53.63 ? 363 HOH F O   1 
HETATM 12107 O  O   . HOH JA 6 .   ? 89.521  68.538  -30.458 1.00 56.59 ? 364 HOH F O   1 
HETATM 12108 O  O   . HOH JA 6 .   ? 81.386  68.070  -7.922  1.00 48.34 ? 365 HOH F O   1 
HETATM 12109 O  O   . HOH JA 6 .   ? 75.459  75.296  -26.304 1.00 50.73 ? 366 HOH F O   1 
HETATM 12110 O  O   . HOH KA 6 .   ? 99.354  114.751 -10.054 1.00 42.40 ? 301 HOH G O   1 
HETATM 12111 O  O   . HOH KA 6 .   ? 95.874  105.779 -0.809  1.00 45.64 ? 302 HOH G O   1 
HETATM 12112 O  O   . HOH KA 6 .   ? 96.373  96.150  1.637   1.00 47.67 ? 303 HOH G O   1 
HETATM 12113 O  O   . HOH KA 6 .   ? 94.796  115.694 -20.267 1.00 30.09 ? 304 HOH G O   1 
HETATM 12114 O  O   . HOH KA 6 .   ? 105.155 104.418 -7.355  1.00 40.44 ? 305 HOH G O   1 
HETATM 12115 O  O   . HOH KA 6 .   ? 91.456  104.191 -3.444  1.00 36.92 ? 306 HOH G O   1 
HETATM 12116 O  O   . HOH KA 6 .   ? 82.891  94.083  -14.342 1.00 42.97 ? 307 HOH G O   1 
HETATM 12117 O  O   . HOH KA 6 .   ? 82.521  91.665  -13.043 1.00 42.20 ? 308 HOH G O   1 
HETATM 12118 O  O   . HOH KA 6 .   ? 90.040  108.370 -20.341 1.00 43.18 ? 309 HOH G O   1 
HETATM 12119 O  O   . HOH KA 6 .   ? 98.267  107.434 -12.315 1.00 32.90 ? 310 HOH G O   1 
HETATM 12120 O  O   . HOH KA 6 .   ? 95.809  87.515  -19.836 1.00 41.55 ? 311 HOH G O   1 
HETATM 12121 O  O   . HOH KA 6 .   ? 92.782  118.472 -13.117 1.00 26.86 ? 312 HOH G O   1 
HETATM 12122 O  O   . HOH KA 6 .   ? 116.232 94.208  -9.157  1.00 49.01 ? 313 HOH G O   1 
HETATM 12123 O  O   . HOH KA 6 .   ? 87.550  102.316 -26.252 1.00 47.07 ? 314 HOH G O   1 
HETATM 12124 O  O   . HOH KA 6 .   ? 81.074  88.366  -14.758 1.00 42.43 ? 315 HOH G O   1 
HETATM 12125 O  O   . HOH KA 6 .   ? 92.763  105.109 -17.387 1.00 36.94 ? 316 HOH G O   1 
HETATM 12126 O  O   . HOH KA 6 .   ? 88.294  87.010  -15.964 1.00 36.11 ? 317 HOH G O   1 
HETATM 12127 O  O   . HOH KA 6 .   ? 93.591  105.596 -2.550  1.00 41.40 ? 318 HOH G O   1 
HETATM 12128 O  O   . HOH KA 6 .   ? 91.624  94.028  -2.129  1.00 47.89 ? 319 HOH G O   1 
HETATM 12129 O  O   . HOH KA 6 .   ? 110.144 104.239 -12.157 1.00 45.70 ? 320 HOH G O   1 
HETATM 12130 O  O   . HOH KA 6 .   ? 90.435  110.216 -23.027 1.00 51.11 ? 321 HOH G O   1 
HETATM 12131 O  O   . HOH KA 6 .   ? 95.845  113.884 -7.535  1.00 43.32 ? 322 HOH G O   1 
HETATM 12132 O  O   . HOH KA 6 .   ? 97.682  87.005  -16.272 1.00 29.18 ? 323 HOH G O   1 
HETATM 12133 O  O   . HOH KA 6 .   ? 103.039 99.831  2.013   1.00 55.11 ? 324 HOH G O   1 
HETATM 12134 O  O   . HOH KA 6 .   ? 100.002 101.565 -28.570 1.00 44.60 ? 325 HOH G O   1 
HETATM 12135 O  O   . HOH KA 6 .   ? 88.672  102.823 -20.451 1.00 45.58 ? 326 HOH G O   1 
HETATM 12136 O  O   . HOH KA 6 .   ? 96.748  121.646 -14.702 1.00 33.28 ? 327 HOH G O   1 
HETATM 12137 O  O   . HOH KA 6 .   ? 99.626  99.829  -30.246 1.00 44.81 ? 328 HOH G O   1 
HETATM 12138 O  O   . HOH KA 6 .   ? 110.903 101.605 -21.722 1.00 46.02 ? 329 HOH G O   1 
HETATM 12139 O  O   . HOH KA 6 .   ? 90.732  105.685 -19.566 1.00 37.65 ? 330 HOH G O   1 
HETATM 12140 O  O   . HOH KA 6 .   ? 104.775 105.349 -13.514 1.00 39.41 ? 331 HOH G O   1 
HETATM 12141 O  O   . HOH KA 6 .   ? 107.069 96.281  -30.090 1.00 49.73 ? 332 HOH G O   1 
HETATM 12142 O  O   . HOH KA 6 .   ? 99.966  114.729 -2.909  1.00 51.97 ? 333 HOH G O   1 
HETATM 12143 O  O   . HOH KA 6 .   ? 89.743  92.249  -17.946 1.00 39.69 ? 334 HOH G O   1 
HETATM 12144 O  O   . HOH KA 6 .   ? 104.246 110.411 -16.273 1.00 42.66 ? 335 HOH G O   1 
HETATM 12145 O  O   . HOH KA 6 .   ? 101.277 108.246 -2.853  1.00 48.86 ? 336 HOH G O   1 
HETATM 12146 O  O   . HOH KA 6 .   ? 88.838  100.510 -24.201 1.00 37.08 ? 337 HOH G O   1 
HETATM 12147 O  O   . HOH KA 6 .   ? 108.016 94.859  0.498   1.00 49.34 ? 338 HOH G O   1 
HETATM 12148 O  O   . HOH KA 6 .   ? 104.251 110.541 -24.920 1.00 46.52 ? 339 HOH G O   1 
HETATM 12149 O  O   . HOH KA 6 .   ? 96.062  112.059 -22.470 1.00 33.65 ? 340 HOH G O   1 
HETATM 12150 O  O   . HOH KA 6 .   ? 85.789  115.572 -18.920 1.00 34.79 ? 341 HOH G O   1 
HETATM 12151 O  O   . HOH KA 6 .   ? 101.917 85.151  0.364   1.00 52.47 ? 342 HOH G O   1 
HETATM 12152 O  O   . HOH KA 6 .   ? 111.117 108.425 -32.968 1.00 49.97 ? 343 HOH G O   1 
HETATM 12153 O  O   . HOH KA 6 .   ? 88.650  105.215 -12.784 1.00 42.11 ? 344 HOH G O   1 
HETATM 12154 O  O   . HOH KA 6 .   ? 87.578  108.901 -9.602  1.00 44.30 ? 345 HOH G O   1 
HETATM 12155 O  O   . HOH KA 6 .   ? 98.282  104.121 -28.598 1.00 38.16 ? 346 HOH G O   1 
HETATM 12156 O  O   . HOH KA 6 .   ? 104.417 104.692 -3.660  1.00 43.80 ? 347 HOH G O   1 
HETATM 12157 O  O   . HOH KA 6 .   ? 87.972  117.693 -9.169  1.00 51.33 ? 348 HOH G O   1 
HETATM 12158 O  O   . HOH KA 6 .   ? 86.069  94.768  -5.518  1.00 49.53 ? 349 HOH G O   1 
HETATM 12159 O  O   . HOH KA 6 .   ? 94.586  87.040  -17.688 1.00 44.95 ? 350 HOH G O   1 
HETATM 12160 O  O   . HOH KA 6 .   ? 101.869 90.471  0.898   1.00 47.90 ? 351 HOH G O   1 
HETATM 12161 O  O   . HOH KA 6 .   ? 89.757  108.833 1.382   1.00 48.59 ? 352 HOH G O   1 
HETATM 12162 O  O   . HOH KA 6 .   ? 88.878  95.228  -24.851 1.00 56.16 ? 353 HOH G O   1 
HETATM 12163 O  O   . HOH KA 6 .   ? 108.571 104.116 -9.304  1.00 43.42 ? 354 HOH G O   1 
HETATM 12164 O  O   . HOH KA 6 .   ? 113.664 105.084 -28.109 1.00 51.37 ? 355 HOH G O   1 
HETATM 12165 O  O   . HOH KA 6 .   ? 84.661  101.207 -15.789 1.00 41.57 ? 356 HOH G O   1 
HETATM 12166 O  O   . HOH KA 6 .   ? 103.174 110.960 -9.901  1.00 37.41 ? 357 HOH G O   1 
HETATM 12167 O  O   . HOH KA 6 .   ? 99.090  116.404 -5.484  1.00 50.41 ? 358 HOH G O   1 
HETATM 12168 O  O   . HOH KA 6 .   ? 115.350 101.727 -25.665 1.00 50.56 ? 359 HOH G O   1 
HETATM 12169 O  O   . HOH KA 6 .   ? 97.739  114.999 -3.725  1.00 48.92 ? 360 HOH G O   1 
HETATM 12170 O  O   . HOH KA 6 .   ? 82.600  99.727  -10.123 1.00 43.96 ? 361 HOH G O   1 
HETATM 12171 O  O   . HOH KA 6 .   ? 91.450  90.633  -17.907 1.00 48.67 ? 362 HOH G O   1 
HETATM 12172 O  O   . HOH KA 6 .   ? 92.473  88.524  -18.640 1.00 47.48 ? 363 HOH G O   1 
HETATM 12173 O  O   . HOH KA 6 .   ? 103.304 114.832 -3.990  1.00 49.44 ? 364 HOH G O   1 
HETATM 12174 O  O   . HOH KA 6 .   ? 99.934  86.644  -0.634  1.00 55.95 ? 365 HOH G O   1 
HETATM 12175 O  O   . HOH KA 6 .   ? 107.160 90.469  -22.550 1.00 50.06 ? 366 HOH G O   1 
HETATM 12176 O  O   . HOH KA 6 .   ? 89.631  103.715 -17.925 1.00 43.03 ? 367 HOH G O   1 
HETATM 12177 O  O   . HOH KA 6 .   ? 92.032  90.807  -0.380  1.00 52.43 ? 368 HOH G O   1 
HETATM 12178 O  O   . HOH KA 6 .   ? 88.733  96.605  -0.898  1.00 48.43 ? 369 HOH G O   1 
HETATM 12179 O  O   . HOH KA 6 .   ? 86.663  119.328 -6.926  1.00 55.80 ? 370 HOH G O   1 
HETATM 12180 O  O   . HOH KA 6 .   ? 81.437  96.592  -18.127 1.00 52.91 ? 371 HOH G O   1 
HETATM 12181 O  O   . HOH KA 6 .   ? 85.449  101.021 -20.898 1.00 49.30 ? 372 HOH G O   1 
HETATM 12182 O  O   . HOH KA 6 .   ? 98.001  120.853 -12.368 1.00 38.63 ? 373 HOH G O   1 
HETATM 12183 O  O   . HOH KA 6 .   ? 82.650  100.674 -14.245 1.00 51.25 ? 374 HOH G O   1 
HETATM 12184 O  O   . HOH KA 6 .   ? 101.954 114.646 -1.729  1.00 57.63 ? 375 HOH G O   1 
HETATM 12185 O  O   . HOH KA 6 .   ? 85.668  103.908 -8.530  1.00 48.89 ? 376 HOH G O   1 
HETATM 12186 O  O   . HOH KA 6 .   ? 78.509  117.222 -18.555 1.00 51.00 ? 377 HOH G O   1 
HETATM 12187 O  O   . HOH KA 6 .   ? 88.023  86.700  -24.451 1.00 52.69 ? 378 HOH G O   1 
HETATM 12188 O  O   . HOH KA 6 .   ? 111.863 109.145 -6.734  1.00 44.31 ? 379 HOH G O   1 
HETATM 12189 O  O   . HOH KA 6 .   ? 77.567  117.729 -16.353 1.00 54.45 ? 380 HOH G O   1 
HETATM 12190 O  O   . HOH KA 6 .   ? 78.672  89.515  -15.379 1.00 56.12 ? 381 HOH G O   1 
HETATM 12191 O  O   . HOH KA 6 .   ? 100.758 115.951 -0.112  1.00 50.44 ? 382 HOH G O   1 
HETATM 12192 O  O   . HOH LA 6 .   ? 49.687  64.155  -79.236 1.00 49.55 ? 301 HOH I O   1 
HETATM 12193 O  O   . HOH LA 6 .   ? 63.153  75.892  -39.692 1.00 43.74 ? 302 HOH I O   1 
HETATM 12194 O  O   . HOH LA 6 .   ? 38.238  54.956  -46.054 1.00 52.23 ? 303 HOH I O   1 
HETATM 12195 O  O   . HOH LA 6 .   ? 54.050  80.237  -53.695 1.00 43.04 ? 304 HOH I O   1 
HETATM 12196 O  O   . HOH LA 6 .   ? 62.656  80.943  -52.562 1.00 49.65 ? 305 HOH I O   1 
HETATM 12197 O  O   . HOH LA 6 .   ? 43.594  69.189  -48.749 1.00 36.54 ? 306 HOH I O   1 
HETATM 12198 O  O   . HOH LA 6 .   ? 62.724  78.750  -49.689 1.00 42.72 ? 307 HOH I O   1 
HETATM 12199 O  O   . HOH LA 6 .   ? 65.077  66.890  -43.515 1.00 46.03 ? 308 HOH I O   1 
HETATM 12200 O  O   . HOH LA 6 .   ? 57.606  81.393  -50.351 1.00 48.69 ? 309 HOH I O   1 
HETATM 12201 O  O   . HOH LA 6 .   ? 65.197  58.355  -47.623 1.00 40.62 ? 310 HOH I O   1 
HETATM 12202 O  O   . HOH LA 6 .   ? 48.486  70.596  -42.130 1.00 35.95 ? 311 HOH I O   1 
HETATM 12203 O  O   . HOH LA 6 .   ? 46.175  50.123  -56.435 1.00 48.96 ? 312 HOH I O   1 
HETATM 12204 O  O   . HOH LA 6 .   ? 55.945  80.758  -61.079 1.00 52.25 ? 313 HOH I O   1 
HETATM 12205 O  O   . HOH LA 6 .   ? 64.481  65.173  -45.093 1.00 44.97 ? 314 HOH I O   1 
HETATM 12206 O  O   . HOH LA 6 .   ? 47.191  79.336  -56.432 1.00 49.60 ? 315 HOH I O   1 
HETATM 12207 O  O   . HOH LA 6 .   ? 46.647  76.842  -59.949 1.00 45.12 ? 316 HOH I O   1 
HETATM 12208 O  O   . HOH LA 6 .   ? 46.476  58.632  -42.732 1.00 45.84 ? 317 HOH I O   1 
HETATM 12209 O  O   . HOH LA 6 .   ? 63.744  72.838  -59.011 1.00 42.25 ? 318 HOH I O   1 
HETATM 12210 O  O   . HOH LA 6 .   ? 65.387  54.532  -66.014 1.00 50.71 ? 319 HOH I O   1 
HETATM 12211 O  O   . HOH LA 6 .   ? 56.559  79.682  -54.125 1.00 47.13 ? 320 HOH I O   1 
HETATM 12212 O  O   . HOH LA 6 .   ? 72.083  52.177  -55.834 1.00 38.05 ? 321 HOH I O   1 
HETATM 12213 O  O   . HOH LA 6 .   ? 66.976  55.436  -60.110 1.00 45.57 ? 322 HOH I O   1 
HETATM 12214 O  O   . HOH LA 6 .   ? 55.601  54.907  -65.695 1.00 43.32 ? 323 HOH I O   1 
HETATM 12215 O  O   . HOH LA 6 .   ? 52.502  65.606  -70.328 1.00 44.43 ? 324 HOH I O   1 
HETATM 12216 O  O   . HOH LA 6 .   ? 57.938  76.778  -42.062 1.00 32.88 ? 325 HOH I O   1 
HETATM 12217 O  O   . HOH LA 6 .   ? 60.795  66.480  -63.583 1.00 45.13 ? 326 HOH I O   1 
HETATM 12218 O  O   . HOH LA 6 .   ? 54.537  65.706  -72.341 1.00 52.07 ? 327 HOH I O   1 
HETATM 12219 O  O   . HOH LA 6 .   ? 67.829  54.503  -49.408 1.00 30.49 ? 328 HOH I O   1 
HETATM 12220 O  O   . HOH LA 6 .   ? 44.123  66.960  -47.132 1.00 41.40 ? 329 HOH I O   1 
HETATM 12221 O  O   . HOH LA 6 .   ? 67.517  50.261  -55.828 1.00 35.99 ? 330 HOH I O   1 
HETATM 12222 O  O   . HOH LA 6 .   ? 57.595  78.280  -56.492 1.00 41.38 ? 331 HOH I O   1 
HETATM 12223 O  O   . HOH LA 6 .   ? 57.422  68.818  -40.224 1.00 37.65 ? 332 HOH I O   1 
HETATM 12224 O  O   . HOH LA 6 .   ? 42.532  53.650  -50.675 1.00 44.08 ? 333 HOH I O   1 
HETATM 12225 O  O   . HOH LA 6 .   ? 62.057  66.885  -57.948 1.00 26.83 ? 334 HOH I O   1 
HETATM 12226 O  O   . HOH LA 6 .   ? 60.366  65.225  -41.777 1.00 27.16 ? 335 HOH I O   1 
HETATM 12227 O  O   . HOH LA 6 .   ? 50.030  64.184  -41.438 1.00 42.75 ? 336 HOH I O   1 
HETATM 12228 O  O   . HOH LA 6 .   ? 43.069  70.330  -53.029 1.00 22.59 ? 337 HOH I O   1 
HETATM 12229 O  O   . HOH LA 6 .   ? 38.976  62.208  -50.888 1.00 27.00 ? 338 HOH I O   1 
HETATM 12230 O  O   . HOH LA 6 .   ? 41.637  61.931  -63.908 1.00 41.89 ? 339 HOH I O   1 
HETATM 12231 O  O   . HOH LA 6 .   ? 59.778  64.667  -66.788 1.00 47.28 ? 340 HOH I O   1 
HETATM 12232 O  O   . HOH LA 6 .   ? 64.341  40.983  -50.192 1.00 40.34 ? 341 HOH I O   1 
HETATM 12233 O  O   . HOH LA 6 .   ? 37.047  58.694  -41.677 1.00 52.04 ? 342 HOH I O   1 
HETATM 12234 O  O   . HOH LA 6 .   ? 48.328  53.498  -60.239 1.00 38.84 ? 343 HOH I O   1 
HETATM 12235 O  O   . HOH LA 6 .   ? 61.766  81.006  -46.170 1.00 40.71 ? 344 HOH I O   1 
HETATM 12236 O  O   . HOH LA 6 .   ? 60.376  60.207  -57.607 1.00 24.17 ? 345 HOH I O   1 
HETATM 12237 O  O   . HOH LA 6 .   ? 53.667  54.120  -64.280 1.00 36.57 ? 346 HOH I O   1 
HETATM 12238 O  O   . HOH LA 6 .   ? 57.023  57.764  -51.109 1.00 36.42 ? 347 HOH I O   1 
HETATM 12239 O  O   . HOH LA 6 .   ? 63.946  51.374  -58.037 1.00 39.71 ? 348 HOH I O   1 
HETATM 12240 O  O   . HOH LA 6 .   ? 60.936  59.643  -67.801 1.00 45.28 ? 349 HOH I O   1 
HETATM 12241 O  O   . HOH LA 6 .   ? 58.999  54.604  -47.264 1.00 38.24 ? 350 HOH I O   1 
HETATM 12242 O  O   . HOH LA 6 .   ? 59.004  67.751  -42.134 1.00 27.70 ? 351 HOH I O   1 
HETATM 12243 O  O   . HOH LA 6 .   ? 36.687  55.010  -49.897 1.00 47.10 ? 352 HOH I O   1 
HETATM 12244 O  O   . HOH LA 6 .   ? 49.135  62.493  -42.692 1.00 42.94 ? 353 HOH I O   1 
HETATM 12245 O  O   . HOH LA 6 .   ? 51.728  67.634  -41.139 1.00 31.68 ? 354 HOH I O   1 
HETATM 12246 O  O   . HOH LA 6 .   ? 44.525  59.004  -65.054 1.00 42.43 ? 355 HOH I O   1 
HETATM 12247 O  O   . HOH LA 6 .   ? 48.486  53.375  -47.620 1.00 46.50 ? 356 HOH I O   1 
HETATM 12248 O  O   . HOH LA 6 .   ? 58.907  47.656  -65.404 1.00 55.40 ? 357 HOH I O   1 
HETATM 12249 O  O   . HOH LA 6 .   ? 42.013  67.733  -50.860 1.00 32.48 ? 358 HOH I O   1 
HETATM 12250 O  O   . HOH LA 6 .   ? 67.974  77.655  -46.183 1.00 41.04 ? 359 HOH I O   1 
HETATM 12251 O  O   . HOH LA 6 .   ? 56.540  56.140  -48.327 1.00 43.02 ? 360 HOH I O   1 
HETATM 12252 O  O   . HOH LA 6 .   ? 52.752  72.306  -71.872 1.00 45.12 ? 361 HOH I O   1 
HETATM 12253 O  O   . HOH LA 6 .   ? 54.254  53.061  -54.262 1.00 28.45 ? 362 HOH I O   1 
HETATM 12254 O  O   . HOH LA 6 .   ? 52.022  58.107  -43.303 1.00 32.40 ? 363 HOH I O   1 
HETATM 12255 O  O   . HOH LA 6 .   ? 69.735  58.250  -54.314 1.00 48.34 ? 364 HOH I O   1 
HETATM 12256 O  O   . HOH LA 6 .   ? 64.003  53.078  -61.381 1.00 42.61 ? 365 HOH I O   1 
HETATM 12257 O  O   . HOH LA 6 .   ? 56.760  49.697  -57.449 1.00 40.93 ? 366 HOH I O   1 
HETATM 12258 O  O   . HOH LA 6 .   ? 39.598  53.978  -48.716 1.00 44.03 ? 367 HOH I O   1 
HETATM 12259 O  O   . HOH LA 6 .   ? 62.706  76.196  -50.755 1.00 30.88 ? 368 HOH I O   1 
HETATM 12260 O  O   . HOH LA 6 .   ? 44.642  61.127  -49.059 1.00 37.82 ? 369 HOH I O   1 
HETATM 12261 O  O   . HOH LA 6 .   ? 61.992  69.867  -62.750 1.00 35.76 ? 370 HOH I O   1 
HETATM 12262 O  O   . HOH LA 6 .   ? 39.926  66.582  -46.812 1.00 42.18 ? 371 HOH I O   1 
HETATM 12263 O  O   . HOH LA 6 .   ? 55.440  50.368  -49.347 1.00 51.43 ? 372 HOH I O   1 
HETATM 12264 O  O   . HOH LA 6 .   ? 48.655  64.015  -72.249 1.00 51.02 ? 373 HOH I O   1 
HETATM 12265 O  O   . HOH LA 6 .   ? 46.091  77.942  -42.608 1.00 55.83 ? 374 HOH I O   1 
HETATM 12266 O  O   . HOH LA 6 .   ? 60.410  48.916  -45.038 1.00 52.21 ? 375 HOH I O   1 
HETATM 12267 O  O   . HOH LA 6 .   ? 46.600  62.298  -42.848 1.00 47.61 ? 376 HOH I O   1 
HETATM 12268 O  O   . HOH LA 6 .   ? 39.806  80.037  -67.226 1.00 51.22 ? 377 HOH I O   1 
HETATM 12269 O  O   . HOH LA 6 .   ? 65.915  62.441  -45.492 1.00 39.65 ? 378 HOH I O   1 
HETATM 12270 O  O   . HOH LA 6 .   ? 53.340  75.617  -40.298 1.00 42.41 ? 379 HOH I O   1 
HETATM 12271 O  O   . HOH LA 6 .   ? 44.057  63.409  -41.315 1.00 55.12 ? 380 HOH I O   1 
HETATM 12272 O  O   . HOH LA 6 .   ? 43.365  54.389  -60.789 1.00 40.65 ? 381 HOH I O   1 
HETATM 12273 O  O   . HOH LA 6 .   ? 64.245  78.140  -38.400 1.00 49.42 ? 382 HOH I O   1 
HETATM 12274 O  O   . HOH LA 6 .   ? 64.481  51.071  -45.205 1.00 41.84 ? 383 HOH I O   1 
HETATM 12275 O  O   . HOH LA 6 .   ? 61.788  53.588  -45.388 1.00 48.46 ? 384 HOH I O   1 
HETATM 12276 O  O   . HOH LA 6 .   ? 40.561  63.274  -43.500 1.00 48.88 ? 385 HOH I O   1 
HETATM 12277 O  O   . HOH LA 6 .   ? 62.230  73.766  -40.030 1.00 48.29 ? 386 HOH I O   1 
HETATM 12278 O  O   . HOH LA 6 .   ? 64.215  72.388  -39.779 1.00 43.63 ? 387 HOH I O   1 
HETATM 12279 O  O   . HOH LA 6 .   ? 43.608  62.604  -50.289 1.00 39.29 ? 388 HOH I O   1 
HETATM 12280 O  O   . HOH LA 6 .   ? 62.869  47.189  -47.768 1.00 36.05 ? 389 HOH I O   1 
HETATM 12281 O  O   . HOH LA 6 .   ? 53.379  73.986  -69.082 1.00 47.87 ? 390 HOH I O   1 
HETATM 12282 O  O   . HOH LA 6 .   ? 51.827  78.656  -53.197 1.00 39.67 ? 391 HOH I O   1 
HETATM 12283 O  O   . HOH LA 6 .   ? 57.765  72.575  -38.329 1.00 46.72 ? 392 HOH I O   1 
HETATM 12284 O  O   . HOH LA 6 .   ? 65.803  62.056  -61.415 1.00 30.66 ? 393 HOH I O   1 
HETATM 12285 O  O   A HOH LA 6 .   ? 43.326  64.732  -49.548 0.50 30.31 ? 394 HOH I O   1 
HETATM 12286 O  O   B HOH LA 6 .   ? 42.397  66.244  -48.508 0.50 32.17 ? 394 HOH I O   1 
HETATM 12287 O  O   . HOH LA 6 .   ? 59.146  74.531  -64.413 1.00 50.22 ? 395 HOH I O   1 
HETATM 12288 O  O   . HOH LA 6 .   ? 49.492  52.443  -50.219 1.00 44.98 ? 396 HOH I O   1 
HETATM 12289 O  O   . HOH LA 6 .   ? 53.639  82.308  -59.944 1.00 56.96 ? 397 HOH I O   1 
HETATM 12290 O  O   . HOH LA 6 .   ? 54.248  55.931  -49.841 1.00 41.79 ? 398 HOH I O   1 
HETATM 12291 O  O   . HOH LA 6 .   ? 53.359  55.631  -45.877 1.00 49.23 ? 399 HOH I O   1 
HETATM 12292 O  O   . HOH LA 6 .   ? 59.576  73.513  -71.460 1.00 50.05 ? 400 HOH I O   1 
HETATM 12293 O  O   . HOH LA 6 .   ? 65.445  54.133  -45.295 1.00 49.74 ? 401 HOH I O   1 
HETATM 12294 O  O   . HOH LA 6 .   ? 53.485  54.281  -51.497 1.00 34.71 ? 402 HOH I O   1 
HETATM 12295 O  O   . HOH LA 6 .   ? 63.039  48.636  -45.248 1.00 44.30 ? 403 HOH I O   1 
HETATM 12296 O  O   . HOH LA 6 .   ? 56.625  53.206  -46.132 1.00 52.59 ? 404 HOH I O   1 
HETATM 12297 O  O   . HOH LA 6 .   ? 54.665  50.932  -55.744 1.00 44.65 ? 405 HOH I O   1 
HETATM 12298 O  O   . HOH LA 6 .   ? 47.870  76.980  -69.207 1.00 51.54 ? 406 HOH I O   1 
HETATM 12299 O  O   . HOH LA 6 .   ? 62.997  49.762  -58.261 1.00 58.70 ? 407 HOH I O   1 
HETATM 12300 O  O   . HOH LA 6 .   ? 55.597  76.926  -40.129 1.00 50.81 ? 408 HOH I O   1 
HETATM 12301 O  O   . HOH LA 6 .   ? 64.689  49.858  -60.509 1.00 51.61 ? 409 HOH I O   1 
HETATM 12302 O  O   . HOH LA 6 .   ? 56.659  56.267  -67.929 1.00 47.32 ? 410 HOH I O   1 
HETATM 12303 O  O   . HOH LA 6 .   ? 58.950  75.425  -39.102 1.00 51.30 ? 411 HOH I O   1 
HETATM 12304 O  O   . HOH LA 6 .   ? 53.786  53.480  -47.510 1.00 52.18 ? 412 HOH I O   1 
HETATM 12305 O  O   . HOH LA 6 .   ? 57.844  61.423  -71.660 1.00 48.44 ? 413 HOH I O   1 
HETATM 12306 O  O   . HOH LA 6 .   ? 54.045  81.438  -68.008 1.00 56.08 ? 414 HOH I O   1 
HETATM 12307 O  O   . HOH LA 6 .   ? 48.732  50.260  -51.063 1.00 49.21 ? 415 HOH I O   1 
HETATM 12308 O  O   . HOH LA 6 .   ? 45.006  79.010  -60.108 1.00 49.17 ? 416 HOH I O   1 
HETATM 12309 O  O   . HOH LA 6 .   ? 69.759  49.892  -57.356 1.00 40.54 ? 417 HOH I O   1 
HETATM 12310 O  O   . HOH LA 6 .   ? 66.232  58.752  -71.075 1.00 56.46 ? 418 HOH I O   1 
HETATM 12311 O  O   . HOH LA 6 .   ? 54.667  66.914  -39.501 1.00 35.94 ? 419 HOH I O   1 
HETATM 12312 O  O   . HOH LA 6 .   ? 51.097  80.065  -50.682 1.00 44.28 ? 420 HOH I O   1 
HETATM 12313 O  O   . HOH LA 6 .   ? 60.045  82.125  -47.325 1.00 47.70 ? 421 HOH I O   1 
HETATM 12314 O  O   . HOH LA 6 .   ? 54.043  50.399  -51.295 1.00 46.90 ? 422 HOH I O   1 
HETATM 12315 O  O   A HOH LA 6 .   ? 67.624  65.156  -41.998 0.46 29.64 ? 423 HOH I O   1 
HETATM 12316 O  O   B HOH LA 6 .   ? 68.105  73.447  -47.629 0.54 27.84 ? 423 HOH I O   1 
HETATM 12317 O  O   . HOH LA 6 .   ? 56.216  74.953  -37.997 1.00 40.51 ? 424 HOH I O   1 
HETATM 12318 O  O   . HOH LA 6 .   ? 72.906  62.638  -57.501 1.00 51.31 ? 425 HOH I O   1 
HETATM 12319 O  O   . HOH MA 6 .   ? 27.256  68.855  -41.489 1.00 52.56 ? 201 HOH J O   1 
HETATM 12320 O  O   . HOH MA 6 .   ? 38.049  67.918  -48.105 1.00 35.19 ? 202 HOH J O   1 
HETATM 12321 O  O   . HOH MA 6 .   ? 29.738  68.491  -70.130 1.00 60.36 ? 203 HOH J O   1 
HETATM 12322 O  O   . HOH MA 6 .   ? 32.802  68.283  -70.645 1.00 55.26 ? 204 HOH J O   1 
HETATM 12323 O  O   . HOH MA 6 .   ? 31.103  67.597  -36.953 1.00 41.70 ? 205 HOH J O   1 
HETATM 12324 O  O   . HOH MA 6 .   ? 27.606  47.205  -70.905 1.00 61.17 ? 206 HOH J O   1 
HETATM 12325 O  O   . HOH MA 6 .   ? 30.006  53.183  -48.425 1.00 48.90 ? 207 HOH J O   1 
HETATM 12326 O  O   . HOH MA 6 .   ? 19.837  63.180  -47.489 1.00 42.57 ? 208 HOH J O   1 
HETATM 12327 O  O   . HOH MA 6 .   ? 26.481  52.633  -62.501 1.00 70.56 ? 209 HOH J O   1 
HETATM 12328 O  O   . HOH MA 6 .   ? 42.130  81.473  -54.295 1.00 48.81 ? 210 HOH J O   1 
HETATM 12329 O  O   . HOH MA 6 .   ? 37.872  64.896  -51.103 1.00 22.77 ? 211 HOH J O   1 
HETATM 12330 O  O   . HOH MA 6 .   ? 22.474  66.456  -61.807 1.00 50.94 ? 212 HOH J O   1 
HETATM 12331 O  O   . HOH MA 6 .   ? 37.820  79.830  -58.459 1.00 45.75 ? 213 HOH J O   1 
HETATM 12332 O  O   . HOH MA 6 .   ? 39.952  54.382  -52.564 1.00 39.52 ? 214 HOH J O   1 
HETATM 12333 O  O   . HOH MA 6 .   ? 42.221  80.394  -57.024 1.00 51.89 ? 215 HOH J O   1 
HETATM 12334 O  O   . HOH MA 6 .   ? 34.391  71.153  -41.294 1.00 33.79 ? 216 HOH J O   1 
HETATM 12335 O  O   . HOH MA 6 .   ? 40.337  78.190  -59.793 1.00 40.41 ? 217 HOH J O   1 
HETATM 12336 O  O   . HOH MA 6 .   ? 21.817  56.712  -66.011 1.00 62.11 ? 218 HOH J O   1 
HETATM 12337 O  O   . HOH MA 6 .   ? 25.675  66.127  -36.147 1.00 39.89 ? 219 HOH J O   1 
HETATM 12338 O  O   . HOH MA 6 .   ? 23.742  77.125  -54.616 1.00 48.74 ? 220 HOH J O   1 
HETATM 12339 O  O   . HOH MA 6 .   ? 37.624  71.250  -47.979 1.00 38.05 ? 221 HOH J O   1 
HETATM 12340 O  O   . HOH MA 6 .   ? 18.111  74.006  -41.482 1.00 43.92 ? 222 HOH J O   1 
HETATM 12341 O  O   . HOH MA 6 .   ? 16.521  76.429  -46.092 1.00 48.55 ? 223 HOH J O   1 
HETATM 12342 O  O   . HOH MA 6 .   ? 42.085  72.567  -54.349 1.00 25.59 ? 224 HOH J O   1 
HETATM 12343 O  O   . HOH MA 6 .   ? 20.290  60.911  -40.719 1.00 50.33 ? 225 HOH J O   1 
HETATM 12344 O  O   . HOH MA 6 .   ? 36.725  74.637  -52.710 1.00 39.56 ? 226 HOH J O   1 
HETATM 12345 O  O   . HOH MA 6 .   ? 26.023  73.602  -39.749 1.00 33.84 ? 227 HOH J O   1 
HETATM 12346 O  O   . HOH MA 6 .   ? 31.187  73.843  -41.562 1.00 32.33 ? 228 HOH J O   1 
HETATM 12347 O  O   . HOH MA 6 .   ? 14.814  66.611  -41.100 1.00 47.46 ? 229 HOH J O   1 
HETATM 12348 O  O   . HOH MA 6 .   ? 30.099  59.416  -69.545 1.00 52.92 ? 230 HOH J O   1 
HETATM 12349 O  O   . HOH MA 6 .   ? 34.665  55.800  -48.436 1.00 46.11 ? 231 HOH J O   1 
HETATM 12350 O  O   . HOH MA 6 .   ? 39.197  67.724  -50.899 1.00 33.48 ? 232 HOH J O   1 
HETATM 12351 O  O   . HOH MA 6 .   ? 27.243  79.756  -53.512 1.00 48.47 ? 233 HOH J O   1 
HETATM 12352 O  O   . HOH MA 6 .   ? 22.115  70.695  -35.468 1.00 40.79 ? 234 HOH J O   1 
HETATM 12353 O  O   . HOH MA 6 .   ? 33.969  55.780  -52.692 1.00 46.36 ? 235 HOH J O   1 
HETATM 12354 O  O   . HOH MA 6 .   ? 23.798  73.819  -41.012 1.00 42.19 ? 236 HOH J O   1 
HETATM 12355 O  O   . HOH MA 6 .   ? 19.609  71.474  -35.717 1.00 36.77 ? 237 HOH J O   1 
HETATM 12356 O  O   . HOH MA 6 .   ? 36.053  73.517  -66.010 1.00 45.80 ? 238 HOH J O   1 
HETATM 12357 O  O   . HOH MA 6 .   ? 26.228  52.995  -64.652 1.00 54.92 ? 239 HOH J O   1 
HETATM 12358 O  O   . HOH MA 6 .   ? 15.066  63.418  -36.941 1.00 39.50 ? 240 HOH J O   1 
HETATM 12359 O  O   . HOH MA 6 .   ? 30.517  80.570  -47.707 1.00 49.56 ? 241 HOH J O   1 
HETATM 12360 O  O   . HOH MA 6 .   ? 18.334  62.390  -59.049 1.00 46.99 ? 242 HOH J O   1 
HETATM 12361 O  O   . HOH MA 6 .   ? 19.622  61.084  -49.961 1.00 49.32 ? 243 HOH J O   1 
HETATM 12362 O  O   . HOH MA 6 .   ? 37.344  72.212  -52.923 1.00 42.55 ? 244 HOH J O   1 
HETATM 12363 O  O   . HOH MA 6 .   ? 16.957  73.658  -37.844 1.00 47.14 ? 245 HOH J O   1 
HETATM 12364 O  O   . HOH MA 6 .   ? 35.364  76.871  -46.659 1.00 47.09 ? 246 HOH J O   1 
HETATM 12365 O  O   . HOH MA 6 .   ? 37.776  53.528  -59.885 1.00 48.76 ? 247 HOH J O   1 
HETATM 12366 O  O   . HOH MA 6 .   ? 32.998  76.643  -44.956 1.00 46.44 ? 248 HOH J O   1 
HETATM 12367 O  O   . HOH MA 6 .   ? 31.542  56.234  -46.544 1.00 50.25 ? 249 HOH J O   1 
HETATM 12368 O  O   . HOH MA 6 .   ? 14.298  72.801  -44.223 1.00 41.73 ? 250 HOH J O   1 
HETATM 12369 O  O   . HOH MA 6 .   ? 26.243  79.407  -59.623 1.00 46.50 ? 251 HOH J O   1 
HETATM 12370 O  O   . HOH MA 6 .   ? 30.826  81.536  -57.837 1.00 44.48 ? 252 HOH J O   1 
HETATM 12371 O  O   . HOH MA 6 .   ? 37.117  74.213  -47.076 1.00 44.42 ? 253 HOH J O   1 
HETATM 12372 O  O   . HOH MA 6 .   ? 37.958  71.901  -40.138 1.00 53.68 ? 254 HOH J O   1 
HETATM 12373 O  O   . HOH MA 6 .   ? 16.973  56.401  -50.787 1.00 50.79 ? 255 HOH J O   1 
HETATM 12374 O  O   . HOH MA 6 .   ? 28.419  81.396  -51.490 1.00 49.95 ? 256 HOH J O   1 
HETATM 12375 O  O   . HOH MA 6 .   ? 27.193  62.528  -69.563 1.00 52.47 ? 257 HOH J O   1 
HETATM 12376 O  O   . HOH MA 6 .   ? 45.181  50.891  -52.005 1.00 57.00 ? 258 HOH J O   1 
HETATM 12377 O  O   . HOH MA 6 .   ? 30.335  61.941  -41.542 1.00 49.18 ? 259 HOH J O   1 
HETATM 12378 O  O   . HOH MA 6 .   ? 37.311  69.535  -39.955 1.00 51.61 ? 260 HOH J O   1 
HETATM 12379 O  O   . HOH MA 6 .   ? 32.856  62.000  -41.241 1.00 49.11 ? 261 HOH J O   1 
HETATM 12380 O  O   . HOH MA 6 .   ? 28.679  75.506  -40.117 1.00 39.25 ? 262 HOH J O   1 
HETATM 12381 O  O   . HOH MA 6 .   ? 39.021  81.836  -57.047 1.00 55.19 ? 263 HOH J O   1 
HETATM 12382 O  O   . HOH MA 6 .   ? 33.764  55.632  -46.024 1.00 54.91 ? 264 HOH J O   1 
HETATM 12383 O  O   . HOH MA 6 .   ? 30.623  82.866  -46.422 1.00 53.65 ? 265 HOH J O   1 
HETATM 12384 O  O   . HOH MA 6 .   ? 19.226  68.963  -70.532 1.00 46.82 ? 266 HOH J O   1 
HETATM 12385 O  O   . HOH MA 6 .   ? 19.241  71.838  -71.169 1.00 50.72 ? 267 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  ?   ?   ?   A . n 
A 1 27  MET 27  0   0   MET ALA 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 ?   ?   ?   D . n 
C 1 2   LYS 2   -25 ?   ?   ?   D . n 
C 1 3   HIS 3   -24 ?   ?   ?   D . n 
C 1 4   HIS 4   -23 ?   ?   ?   D . n 
C 1 5   HIS 5   -22 ?   ?   ?   D . n 
C 1 6   HIS 6   -21 ?   ?   ?   D . n 
C 1 7   HIS 7   -20 ?   ?   ?   D . n 
C 1 8   HIS 8   -19 ?   ?   ?   D . n 
C 1 9   PRO 9   -18 ?   ?   ?   D . n 
C 1 10  MET 10  -17 ?   ?   ?   D . n 
C 1 11  SER 11  -16 ?   ?   ?   D . n 
C 1 12  ASP 12  -15 ?   ?   ?   D . n 
C 1 13  TYR 13  -14 ?   ?   ?   D . n 
C 1 14  ASP 14  -13 ?   ?   ?   D . n 
C 1 15  ILE 15  -12 ?   ?   ?   D . n 
C 1 16  PRO 16  -11 ?   ?   ?   D . n 
C 1 17  THR 17  -10 ?   ?   ?   D . n 
C 1 18  THR 18  -9  ?   ?   ?   D . n 
C 1 19  GLU 19  -8  ?   ?   ?   D . n 
C 1 20  ASN 20  -7  ?   ?   ?   D . n 
C 1 21  LEU 21  -6  ?   ?   ?   D . n 
C 1 22  TYR 22  -5  ?   ?   ?   D . n 
C 1 23  PHE 23  -4  ?   ?   ?   D . n 
C 1 24  GLN 24  -3  ?   ?   ?   D . n 
C 1 25  GLY 25  -2  ?   ?   ?   D . n 
C 1 26  ALA 26  -1  ?   ?   ?   D . n 
C 1 27  MET 27  0   0   MET ALA D . n 
C 1 28  ALA 28  1   1   ALA ALA D . n 
C 1 29  THR 29  2   2   THR THR D . n 
C 1 30  LYS 30  3   3   LYS LYS D . n 
C 1 31  ALA 31  4   4   ALA ALA D . n 
C 1 32  VAL 32  5   5   VAL VAL D . n 
C 1 33  CYS 33  6   6   CYS CYS D . n 
C 1 34  VAL 34  7   7   VAL VAL D . n 
C 1 35  LEU 35  8   8   LEU LEU D . n 
C 1 36  LYS 36  9   9   LYS LYS D . n 
C 1 37  GLY 37  10  10  GLY GLY D . n 
C 1 38  ASP 38  11  11  ASP ASP D . n 
C 1 39  GLY 39  12  12  GLY GLY D . n 
C 1 40  PRO 40  13  13  PRO PRO D . n 
C 1 41  VAL 41  14  14  VAL VAL D . n 
C 1 42  GLN 42  15  15  GLN GLN D . n 
C 1 43  GLY 43  16  16  GLY GLY D . n 
C 1 44  ILE 44  17  17  ILE ILE D . n 
C 1 45  ILE 45  18  18  ILE ILE D . n 
C 1 46  ASN 46  19  19  ASN ASN D . n 
C 1 47  PHE 47  20  20  PHE PHE D . n 
C 1 48  GLU 48  21  21  GLU GLU D . n 
C 1 49  GLN 49  22  22  GLN GLN D . n 
C 1 50  LYS 50  23  23  LYS LYS D . n 
C 1 51  GLU 51  24  24  GLU GLU D . n 
C 1 52  SER 52  25  25  SER SER D . n 
C 1 53  ASN 53  26  26  ASN ASN D . n 
C 1 54  GLY 54  27  27  GLY GLY D . n 
C 1 55  PRO 55  28  28  PRO PRO D . n 
C 1 56  VAL 56  29  29  VAL VAL D . n 
C 1 57  LYS 57  30  30  LYS LYS D . n 
C 1 58  VAL 58  31  31  VAL VAL D . n 
C 1 59  TRP 59  32  32  TRP TRP D . n 
C 1 60  GLY 60  33  33  GLY GLY D . n 
C 1 61  SER 61  34  34  SER SER D . n 
C 1 62  ILE 62  35  35  ILE ILE D . n 
C 1 63  LYS 63  36  36  LYS LYS D . n 
C 1 64  GLY 64  37  37  GLY GLY D . n 
C 1 65  LEU 65  38  38  LEU LEU D . n 
C 1 66  THR 66  39  39  THR THR D . n 
C 1 67  GLU 67  40  40  GLU GLU D . n 
C 1 68  GLY 68  41  41  GLY GLY D . n 
C 1 69  LEU 69  42  42  LEU LEU D . n 
C 1 70  HIS 70  43  43  HIS HIS D . n 
C 1 71  GLY 71  44  44  GLY GLY D . n 
C 1 72  PHE 72  45  45  PHE PHE D . n 
C 1 73  HIS 73  46  46  HIS HIS D . n 
C 1 74  VAL 74  47  47  VAL VAL D . n 
C 1 75  HIS 75  48  48  HIS HIS D . n 
C 1 76  GLU 76  49  49  GLU GLU D . n 
C 1 77  PHE 77  50  50  PHE PHE D . n 
C 1 78  GLY 78  51  51  GLY GLY D . n 
C 1 79  ASP 79  52  52  ASP ASP D . n 
C 1 80  ASN 80  53  53  ASN ASN D . n 
C 1 81  THR 81  54  54  THR THR D . n 
C 1 82  ALA 82  55  55  ALA ALA D . n 
C 1 83  GLY 83  56  56  GLY GLY D . n 
C 1 84  CYS 84  57  57  CYS CYS D . n 
C 1 85  THR 85  58  58  THR THR D . n 
C 1 86  SER 86  59  59  SER SER D . n 
C 1 87  ALA 87  60  60  ALA ALA D . n 
C 1 88  GLY 88  61  61  GLY GLY D . n 
C 1 89  PRO 89  62  62  PRO PRO D . n 
C 1 90  HIS 90  63  63  HIS HIS D . n 
C 1 91  PHE 91  64  64  PHE PHE D . n 
C 1 92  ASN 92  65  65  ASN ASN D . n 
C 1 93  PRO 93  66  66  PRO PRO D . n 
C 1 94  LEU 94  67  67  LEU LEU D . n 
C 1 95  SER 95  68  68  SER SER D . n 
C 1 96  ARG 96  69  69  ARG ARG D . n 
C 1 97  LYS 97  70  70  LYS LYS D . n 
C 1 98  HIS 98  71  71  HIS HIS D . n 
C 1 99  GLY 99  72  72  GLY GLY D . n 
C 1 100 GLY 100 73  73  GLY GLY D . n 
C 1 101 PRO 101 74  74  PRO PRO D . n 
C 1 102 LYS 102 75  75  LYS ALA D . n 
C 1 103 ASP 103 76  76  ASP ASP D . n 
C 1 104 GLU 104 77  77  GLU GLU D . n 
C 1 105 GLU 105 78  78  GLU GLU D . n 
C 1 106 ARG 106 79  79  ARG ARG D . n 
C 1 107 HIS 107 80  80  HIS HIS D . n 
C 1 108 VAL 108 81  81  VAL VAL D . n 
C 1 109 GLY 109 82  82  GLY GLY D . n 
C 1 110 ASP 110 83  83  ASP ASP D . n 
C 1 111 LEU 111 84  84  LEU LEU D . n 
C 1 112 GLY 112 85  85  GLY GLY D . n 
C 1 113 ASN 113 86  86  ASN ASN D . n 
C 1 114 VAL 114 87  87  VAL VAL D . n 
C 1 115 THR 115 88  88  THR THR D . n 
C 1 116 ALA 116 89  89  ALA ALA D . n 
C 1 117 ASP 117 90  90  ASP ASP D . n 
C 1 118 LYS 118 91  91  LYS LYS D . n 
C 1 119 ASP 119 92  92  ASP ASP D . n 
C 1 120 GLY 120 93  93  GLY GLY D . n 
C 1 121 VAL 121 94  94  VAL VAL D . n 
C 1 122 ALA 122 95  95  ALA ALA D . n 
C 1 123 ASP 123 96  96  ASP ASP D . n 
C 1 124 VAL 124 97  97  VAL VAL D . n 
C 1 125 SER 125 98  98  SER SER D . n 
C 1 126 ILE 126 99  99  ILE ILE D . n 
C 1 127 GLU 127 100 100 GLU GLU D . n 
C 1 128 ASP 128 101 101 ASP ASP D . n 
C 1 129 SER 129 102 102 SER SER D . n 
C 1 130 VAL 130 103 103 VAL VAL D . n 
C 1 131 ILE 131 104 104 ILE ILE D . n 
C 1 132 SER 132 105 105 SER SER D . n 
C 1 133 LEU 133 106 106 LEU LEU D . n 
C 1 134 SER 134 107 107 SER SER D . n 
C 1 135 GLY 135 108 108 GLY GLY D . n 
C 1 136 ASP 136 109 109 ASP ASP D . n 
C 1 137 HIS 137 110 110 HIS HIS D . n 
C 1 138 CYS 138 111 111 CYS CYS D . n 
C 1 139 ILE 139 112 112 ILE ILE D . n 
C 1 140 ILE 140 113 113 ILE ILE D . n 
C 1 141 GLY 141 114 114 GLY GLY D . n 
C 1 142 ARG 142 115 115 ARG ARG D . n 
C 1 143 THR 143 116 116 THR THR D . n 
C 1 144 LEU 144 117 117 LEU LEU D . n 
C 1 145 VAL 145 118 118 VAL VAL D . n 
C 1 146 VAL 146 119 119 VAL VAL D . n 
C 1 147 HIS 147 120 120 HIS HIS D . n 
C 1 148 GLU 148 121 121 GLU GLU D . n 
C 1 149 LYS 149 122 122 LYS LYS D . n 
C 1 150 ALA 150 123 123 ALA ALA D . n 
C 1 151 ASP 151 124 124 ASP ASP D . n 
C 1 152 ASP 152 125 125 ASP ASP D . n 
C 1 153 LEU 153 126 126 LEU LEU D . n 
C 1 154 GLY 154 127 127 GLY GLY D . n 
C 1 155 LYS 155 128 128 LYS LYS D . n 
C 1 156 GLY 156 129 129 GLY GLY D . n 
C 1 157 GLY 157 130 130 GLY GLY D . n 
C 1 158 ASN 158 131 131 ASN ASN D . n 
C 1 159 GLU 159 132 132 GLU GLU D . n 
C 1 160 GLU 160 133 133 GLU GLU D . n 
C 1 161 SER 161 134 134 SER SER D . n 
C 1 162 THR 162 135 135 THR THR D . n 
C 1 163 LYS 163 136 136 LYS LYS D . n 
C 1 164 THR 164 137 137 THR THR D . n 
C 1 165 GLY 165 138 138 GLY GLY D . n 
C 1 166 ASN 166 139 139 ASN ASN D . n 
C 1 167 ALA 167 140 140 ALA ALA D . n 
C 1 168 GLY 168 141 141 GLY GLY D . n 
C 1 169 SER 169 142 142 SER SER D . n 
C 1 170 ARG 170 143 143 ARG ARG D . n 
C 1 171 LEU 171 144 144 LEU LEU D . n 
C 1 172 ALA 172 145 145 ALA ALA D . n 
C 1 173 CYS 173 146 146 CYS CYS D . n 
C 1 174 GLY 174 147 147 GLY GLY D . n 
C 1 175 VAL 175 148 148 VAL VAL D . n 
C 1 176 ILE 176 149 149 ILE ILE D . n 
C 1 177 GLY 177 150 150 GLY GLY D . n 
C 1 178 ILE 178 151 151 ILE ILE D . n 
C 1 179 ALA 179 152 152 ALA ALA D . n 
C 1 180 GLN 180 153 153 GLN GLN D . n 
D 1 1   MET 1   -26 ?   ?   ?   C . n 
D 1 2   LYS 2   -25 ?   ?   ?   C . n 
D 1 3   HIS 3   -24 ?   ?   ?   C . n 
D 1 4   HIS 4   -23 ?   ?   ?   C . n 
D 1 5   HIS 5   -22 ?   ?   ?   C . n 
D 1 6   HIS 6   -21 ?   ?   ?   C . n 
D 1 7   HIS 7   -20 ?   ?   ?   C . n 
D 1 8   HIS 8   -19 ?   ?   ?   C . n 
D 1 9   PRO 9   -18 ?   ?   ?   C . n 
D 1 10  MET 10  -17 ?   ?   ?   C . n 
D 1 11  SER 11  -16 ?   ?   ?   C . n 
D 1 12  ASP 12  -15 ?   ?   ?   C . n 
D 1 13  TYR 13  -14 ?   ?   ?   C . n 
D 1 14  ASP 14  -13 ?   ?   ?   C . n 
D 1 15  ILE 15  -12 ?   ?   ?   C . n 
D 1 16  PRO 16  -11 ?   ?   ?   C . n 
D 1 17  THR 17  -10 ?   ?   ?   C . n 
D 1 18  THR 18  -9  ?   ?   ?   C . n 
D 1 19  GLU 19  -8  ?   ?   ?   C . n 
D 1 20  ASN 20  -7  ?   ?   ?   C . n 
D 1 21  LEU 21  -6  ?   ?   ?   C . n 
D 1 22  TYR 22  -5  ?   ?   ?   C . n 
D 1 23  PHE 23  -4  ?   ?   ?   C . n 
D 1 24  GLN 24  -3  ?   ?   ?   C . n 
D 1 25  GLY 25  -2  ?   ?   ?   C . n 
D 1 26  ALA 26  -1  ?   ?   ?   C . n 
D 1 27  MET 27  0   ?   ?   ?   C . n 
D 1 28  ALA 28  1   1   ALA ALA C . n 
D 1 29  THR 29  2   2   THR THR C . n 
D 1 30  LYS 30  3   3   LYS LYS C . n 
D 1 31  ALA 31  4   4   ALA ALA C . n 
D 1 32  VAL 32  5   5   VAL VAL C . n 
D 1 33  CYS 33  6   6   CYS CYS C . n 
D 1 34  VAL 34  7   7   VAL VAL C . n 
D 1 35  LEU 35  8   8   LEU LEU C . n 
D 1 36  LYS 36  9   9   LYS LYS C . n 
D 1 37  GLY 37  10  10  GLY GLY C . n 
D 1 38  ASP 38  11  11  ASP ASP C . n 
D 1 39  GLY 39  12  12  GLY GLY C . n 
D 1 40  PRO 40  13  13  PRO PRO C . n 
D 1 41  VAL 41  14  14  VAL VAL C . n 
D 1 42  GLN 42  15  15  GLN GLN C . n 
D 1 43  GLY 43  16  16  GLY GLY C . n 
D 1 44  ILE 44  17  17  ILE ILE C . n 
D 1 45  ILE 45  18  18  ILE ILE C . n 
D 1 46  ASN 46  19  19  ASN ASN C . n 
D 1 47  PHE 47  20  20  PHE PHE C . n 
D 1 48  GLU 48  21  21  GLU GLU C . n 
D 1 49  GLN 49  22  22  GLN GLN C . n 
D 1 50  LYS 50  23  23  LYS LYS C . n 
D 1 51  GLU 51  24  24  GLU GLU C . n 
D 1 52  SER 52  25  25  SER SER C . n 
D 1 53  ASN 53  26  26  ASN ASN C . n 
D 1 54  GLY 54  27  27  GLY GLY C . n 
D 1 55  PRO 55  28  28  PRO PRO C . n 
D 1 56  VAL 56  29  29  VAL VAL C . n 
D 1 57  LYS 57  30  30  LYS LYS C . n 
D 1 58  VAL 58  31  31  VAL VAL C . n 
D 1 59  TRP 59  32  32  TRP TRP C . n 
D 1 60  GLY 60  33  33  GLY GLY C . n 
D 1 61  SER 61  34  34  SER SER C . n 
D 1 62  ILE 62  35  35  ILE ILE C . n 
D 1 63  LYS 63  36  36  LYS LYS C . n 
D 1 64  GLY 64  37  37  GLY GLY C . n 
D 1 65  LEU 65  38  38  LEU LEU C . n 
D 1 66  THR 66  39  39  THR THR C . n 
D 1 67  GLU 67  40  40  GLU GLU C . n 
D 1 68  GLY 68  41  41  GLY GLY C . n 
D 1 69  LEU 69  42  42  LEU LEU C . n 
D 1 70  HIS 70  43  43  HIS HIS C . n 
D 1 71  GLY 71  44  44  GLY GLY C . n 
D 1 72  PHE 72  45  45  PHE PHE C . n 
D 1 73  HIS 73  46  46  HIS HIS C . n 
D 1 74  VAL 74  47  47  VAL VAL C . n 
D 1 75  HIS 75  48  48  HIS HIS C . n 
D 1 76  GLU 76  49  49  GLU GLU C . n 
D 1 77  PHE 77  50  50  PHE PHE C . n 
D 1 78  GLY 78  51  51  GLY GLY C . n 
D 1 79  ASP 79  52  52  ASP ASP C . n 
D 1 80  ASN 80  53  53  ASN ASN C . n 
D 1 81  THR 81  54  54  THR THR C . n 
D 1 82  ALA 82  55  55  ALA ALA C . n 
D 1 83  GLY 83  56  56  GLY GLY C . n 
D 1 84  CYS 84  57  57  CYS CYS C . n 
D 1 85  THR 85  58  58  THR THR C . n 
D 1 86  SER 86  59  59  SER SER C . n 
D 1 87  ALA 87  60  60  ALA ALA C . n 
D 1 88  GLY 88  61  61  GLY GLY C . n 
D 1 89  PRO 89  62  62  PRO PRO C . n 
D 1 90  HIS 90  63  63  HIS HIS C . n 
D 1 91  PHE 91  64  64  PHE PHE C . n 
D 1 92  ASN 92  65  65  ASN ASN C . n 
D 1 93  PRO 93  66  66  PRO PRO C . n 
D 1 94  LEU 94  67  67  LEU LEU C . n 
D 1 95  SER 95  68  68  SER SER C . n 
D 1 96  ARG 96  69  69  ARG ARG C . n 
D 1 97  LYS 97  70  70  LYS LYS C . n 
D 1 98  HIS 98  71  71  HIS HIS C . n 
D 1 99  GLY 99  72  72  GLY GLY C . n 
D 1 100 GLY 100 73  73  GLY GLY C . n 
D 1 101 PRO 101 74  74  PRO PRO C . n 
D 1 102 LYS 102 75  75  LYS LYS C . n 
D 1 103 ASP 103 76  76  ASP ASP C . n 
D 1 104 GLU 104 77  77  GLU GLU C . n 
D 1 105 GLU 105 78  78  GLU GLU C . n 
D 1 106 ARG 106 79  79  ARG ARG C . n 
D 1 107 HIS 107 80  80  HIS HIS C . n 
D 1 108 VAL 108 81  81  VAL VAL C . n 
D 1 109 GLY 109 82  82  GLY GLY C . n 
D 1 110 ASP 110 83  83  ASP ASP C . n 
D 1 111 LEU 111 84  84  LEU LEU C . n 
D 1 112 GLY 112 85  85  GLY GLY C . n 
D 1 113 ASN 113 86  86  ASN ASN C . n 
D 1 114 VAL 114 87  87  VAL VAL C . n 
D 1 115 THR 115 88  88  THR THR C . n 
D 1 116 ALA 116 89  89  ALA ALA C . n 
D 1 117 ASP 117 90  90  ASP ASP C . n 
D 1 118 LYS 118 91  91  LYS LYS C . n 
D 1 119 ASP 119 92  92  ASP ASP C . n 
D 1 120 GLY 120 93  93  GLY GLY C . n 
D 1 121 VAL 121 94  94  VAL VAL C . n 
D 1 122 ALA 122 95  95  ALA ALA C . n 
D 1 123 ASP 123 96  96  ASP ASP C . n 
D 1 124 VAL 124 97  97  VAL VAL C . n 
D 1 125 SER 125 98  98  SER SER C . n 
D 1 126 ILE 126 99  99  ILE ILE C . n 
D 1 127 GLU 127 100 100 GLU GLU C . n 
D 1 128 ASP 128 101 101 ASP ASP C . n 
D 1 129 SER 129 102 102 SER SER C . n 
D 1 130 VAL 130 103 103 VAL VAL C . n 
D 1 131 ILE 131 104 104 ILE ILE C . n 
D 1 132 SER 132 105 105 SER SER C . n 
D 1 133 LEU 133 106 106 LEU LEU C . n 
D 1 134 SER 134 107 107 SER SER C . n 
D 1 135 GLY 135 108 108 GLY GLY C . n 
D 1 136 ASP 136 109 109 ASP ASP C . n 
D 1 137 HIS 137 110 110 HIS HIS C . n 
D 1 138 CYS 138 111 111 CYS CYS C . n 
D 1 139 ILE 139 112 112 ILE ILE C . n 
D 1 140 ILE 140 113 113 ILE ILE C . n 
D 1 141 GLY 141 114 114 GLY GLY C . n 
D 1 142 ARG 142 115 115 ARG ARG C . n 
D 1 143 THR 143 116 116 THR THR C . n 
D 1 144 LEU 144 117 117 LEU LEU C . n 
D 1 145 VAL 145 118 118 VAL VAL C . n 
D 1 146 VAL 146 119 119 VAL VAL C . n 
D 1 147 HIS 147 120 120 HIS HIS C . n 
D 1 148 GLU 148 121 121 GLU GLU C . n 
D 1 149 LYS 149 122 122 LYS LYS C . n 
D 1 150 ALA 150 123 123 ALA ALA C . n 
D 1 151 ASP 151 124 124 ASP ASP C . n 
D 1 152 ASP 152 125 125 ASP ASP C . n 
D 1 153 LEU 153 126 126 LEU LEU C . n 
D 1 154 GLY 154 127 127 GLY GLY C . n 
D 1 155 LYS 155 128 128 LYS LYS C . n 
D 1 156 GLY 156 129 129 GLY GLY C . n 
D 1 157 GLY 157 130 130 GLY GLY C . n 
D 1 158 ASN 158 131 131 ASN ASN C . n 
D 1 159 GLU 159 132 132 GLU GLU C . n 
D 1 160 GLU 160 133 133 GLU GLU C . n 
D 1 161 SER 161 134 134 SER SER C . n 
D 1 162 THR 162 135 135 THR THR C . n 
D 1 163 LYS 163 136 136 LYS LYS C . n 
D 1 164 THR 164 137 137 THR THR C . n 
D 1 165 GLY 165 138 138 GLY GLY C . n 
D 1 166 ASN 166 139 139 ASN ASN C . n 
D 1 167 ALA 167 140 140 ALA ALA C . n 
D 1 168 GLY 168 141 141 GLY GLY C . n 
D 1 169 SER 169 142 142 SER SER C . n 
D 1 170 ARG 170 143 143 ARG ARG C . n 
D 1 171 LEU 171 144 144 LEU LEU C . n 
D 1 172 ALA 172 145 145 ALA ALA C . n 
D 1 173 CYS 173 146 146 CYS CYS C . n 
D 1 174 GLY 174 147 147 GLY GLY C . n 
D 1 175 VAL 175 148 148 VAL VAL C . n 
D 1 176 ILE 176 149 149 ILE ILE C . n 
D 1 177 GLY 177 150 150 GLY GLY C . n 
D 1 178 ILE 178 151 151 ILE ILE C . n 
D 1 179 ALA 179 152 152 ALA ALA C . n 
D 1 180 GLN 180 153 153 GLN GLN C . n 
E 1 1   MET 1   -26 ?   ?   ?   H . n 
E 1 2   LYS 2   -25 ?   ?   ?   H . n 
E 1 3   HIS 3   -24 ?   ?   ?   H . n 
E 1 4   HIS 4   -23 ?   ?   ?   H . n 
E 1 5   HIS 5   -22 ?   ?   ?   H . n 
E 1 6   HIS 6   -21 ?   ?   ?   H . n 
E 1 7   HIS 7   -20 ?   ?   ?   H . n 
E 1 8   HIS 8   -19 ?   ?   ?   H . n 
E 1 9   PRO 9   -18 ?   ?   ?   H . n 
E 1 10  MET 10  -17 ?   ?   ?   H . n 
E 1 11  SER 11  -16 ?   ?   ?   H . n 
E 1 12  ASP 12  -15 ?   ?   ?   H . n 
E 1 13  TYR 13  -14 ?   ?   ?   H . n 
E 1 14  ASP 14  -13 ?   ?   ?   H . n 
E 1 15  ILE 15  -12 ?   ?   ?   H . n 
E 1 16  PRO 16  -11 ?   ?   ?   H . n 
E 1 17  THR 17  -10 ?   ?   ?   H . n 
E 1 18  THR 18  -9  ?   ?   ?   H . n 
E 1 19  GLU 19  -8  ?   ?   ?   H . n 
E 1 20  ASN 20  -7  ?   ?   ?   H . n 
E 1 21  LEU 21  -6  ?   ?   ?   H . n 
E 1 22  TYR 22  -5  ?   ?   ?   H . n 
E 1 23  PHE 23  -4  ?   ?   ?   H . n 
E 1 24  GLN 24  -3  ?   ?   ?   H . n 
E 1 25  GLY 25  -2  ?   ?   ?   H . n 
E 1 26  ALA 26  -1  ?   ?   ?   H . n 
E 1 27  MET 27  0   0   MET ALA H . n 
E 1 28  ALA 28  1   1   ALA ALA H . n 
E 1 29  THR 29  2   2   THR THR H . n 
E 1 30  LYS 30  3   3   LYS LYS H . n 
E 1 31  ALA 31  4   4   ALA ALA H . n 
E 1 32  VAL 32  5   5   VAL VAL H . n 
E 1 33  CYS 33  6   6   CYS CYS H . n 
E 1 34  VAL 34  7   7   VAL VAL H . n 
E 1 35  LEU 35  8   8   LEU LEU H . n 
E 1 36  LYS 36  9   9   LYS LYS H . n 
E 1 37  GLY 37  10  10  GLY GLY H . n 
E 1 38  ASP 38  11  11  ASP ASP H . n 
E 1 39  GLY 39  12  12  GLY GLY H . n 
E 1 40  PRO 40  13  13  PRO PRO H . n 
E 1 41  VAL 41  14  14  VAL VAL H . n 
E 1 42  GLN 42  15  15  GLN GLN H . n 
E 1 43  GLY 43  16  16  GLY GLY H . n 
E 1 44  ILE 44  17  17  ILE ILE H . n 
E 1 45  ILE 45  18  18  ILE ILE H . n 
E 1 46  ASN 46  19  19  ASN ASN H . n 
E 1 47  PHE 47  20  20  PHE PHE H . n 
E 1 48  GLU 48  21  21  GLU GLU H . n 
E 1 49  GLN 49  22  22  GLN GLN H . n 
E 1 50  LYS 50  23  23  LYS LYS H . n 
E 1 51  GLU 51  24  24  GLU GLU H . n 
E 1 52  SER 52  25  25  SER SER H . n 
E 1 53  ASN 53  26  26  ASN ASN H . n 
E 1 54  GLY 54  27  27  GLY GLY H . n 
E 1 55  PRO 55  28  28  PRO PRO H . n 
E 1 56  VAL 56  29  29  VAL VAL H . n 
E 1 57  LYS 57  30  30  LYS LYS H . n 
E 1 58  VAL 58  31  31  VAL VAL H . n 
E 1 59  TRP 59  32  32  TRP TRP H . n 
E 1 60  GLY 60  33  33  GLY GLY H . n 
E 1 61  SER 61  34  34  SER SER H . n 
E 1 62  ILE 62  35  35  ILE ILE H . n 
E 1 63  LYS 63  36  36  LYS LYS H . n 
E 1 64  GLY 64  37  37  GLY GLY H . n 
E 1 65  LEU 65  38  38  LEU LEU H . n 
E 1 66  THR 66  39  39  THR THR H . n 
E 1 67  GLU 67  40  40  GLU GLU H . n 
E 1 68  GLY 68  41  41  GLY GLY H . n 
E 1 69  LEU 69  42  42  LEU LEU H . n 
E 1 70  HIS 70  43  43  HIS HIS H . n 
E 1 71  GLY 71  44  44  GLY GLY H . n 
E 1 72  PHE 72  45  45  PHE PHE H . n 
E 1 73  HIS 73  46  46  HIS HIS H . n 
E 1 74  VAL 74  47  47  VAL VAL H . n 
E 1 75  HIS 75  48  48  HIS HIS H . n 
E 1 76  GLU 76  49  49  GLU GLU H . n 
E 1 77  PHE 77  50  50  PHE PHE H . n 
E 1 78  GLY 78  51  51  GLY GLY H . n 
E 1 79  ASP 79  52  52  ASP ASP H . n 
E 1 80  ASN 80  53  53  ASN ASN H . n 
E 1 81  THR 81  54  54  THR THR H . n 
E 1 82  ALA 82  55  55  ALA ALA H . n 
E 1 83  GLY 83  56  56  GLY GLY H . n 
E 1 84  CYS 84  57  57  CYS CYS H . n 
E 1 85  THR 85  58  58  THR THR H . n 
E 1 86  SER 86  59  59  SER SER H . n 
E 1 87  ALA 87  60  60  ALA ALA H . n 
E 1 88  GLY 88  61  61  GLY GLY H . n 
E 1 89  PRO 89  62  62  PRO PRO H . n 
E 1 90  HIS 90  63  63  HIS HIS H . n 
E 1 91  PHE 91  64  64  PHE PHE H . n 
E 1 92  ASN 92  65  65  ASN ASN H . n 
E 1 93  PRO 93  66  66  PRO PRO H . n 
E 1 94  LEU 94  67  67  LEU LEU H . n 
E 1 95  SER 95  68  68  SER SER H . n 
E 1 96  ARG 96  69  69  ARG ARG H . n 
E 1 97  LYS 97  70  70  LYS ALA H . n 
E 1 98  HIS 98  71  71  HIS HIS H . n 
E 1 99  GLY 99  72  72  GLY GLY H . n 
E 1 100 GLY 100 73  73  GLY GLY H . n 
E 1 101 PRO 101 74  74  PRO PRO H . n 
E 1 102 LYS 102 75  75  LYS LYS H . n 
E 1 103 ASP 103 76  76  ASP ASP H . n 
E 1 104 GLU 104 77  77  GLU ALA H . n 
E 1 105 GLU 105 78  78  GLU GLU H . n 
E 1 106 ARG 106 79  79  ARG ARG H . n 
E 1 107 HIS 107 80  80  HIS HIS H . n 
E 1 108 VAL 108 81  81  VAL VAL H . n 
E 1 109 GLY 109 82  82  GLY GLY H . n 
E 1 110 ASP 110 83  83  ASP ASP H . n 
E 1 111 LEU 111 84  84  LEU LEU H . n 
E 1 112 GLY 112 85  85  GLY GLY H . n 
E 1 113 ASN 113 86  86  ASN ASN H . n 
E 1 114 VAL 114 87  87  VAL VAL H . n 
E 1 115 THR 115 88  88  THR THR H . n 
E 1 116 ALA 116 89  89  ALA ALA H . n 
E 1 117 ASP 117 90  90  ASP ASP H . n 
E 1 118 LYS 118 91  91  LYS LYS H . n 
E 1 119 ASP 119 92  92  ASP ASP H . n 
E 1 120 GLY 120 93  93  GLY GLY H . n 
E 1 121 VAL 121 94  94  VAL VAL H . n 
E 1 122 ALA 122 95  95  ALA ALA H . n 
E 1 123 ASP 123 96  96  ASP ASP H . n 
E 1 124 VAL 124 97  97  VAL VAL H . n 
E 1 125 SER 125 98  98  SER SER H . n 
E 1 126 ILE 126 99  99  ILE ILE H . n 
E 1 127 GLU 127 100 100 GLU GLU H . n 
E 1 128 ASP 128 101 101 ASP ASP H . n 
E 1 129 SER 129 102 102 SER SER H . n 
E 1 130 VAL 130 103 103 VAL VAL H . n 
E 1 131 ILE 131 104 104 ILE ILE H . n 
E 1 132 SER 132 105 105 SER SER H . n 
E 1 133 LEU 133 106 106 LEU LEU H . n 
E 1 134 SER 134 107 107 SER SER H . n 
E 1 135 GLY 135 108 108 GLY GLY H . n 
E 1 136 ASP 136 109 109 ASP ASP H . n 
E 1 137 HIS 137 110 110 HIS HIS H . n 
E 1 138 CYS 138 111 111 CYS CYS H . n 
E 1 139 ILE 139 112 112 ILE ILE H . n 
E 1 140 ILE 140 113 113 ILE ILE H . n 
E 1 141 GLY 141 114 114 GLY GLY H . n 
E 1 142 ARG 142 115 115 ARG ARG H . n 
E 1 143 THR 143 116 116 THR THR H . n 
E 1 144 LEU 144 117 117 LEU LEU H . n 
E 1 145 VAL 145 118 118 VAL VAL H . n 
E 1 146 VAL 146 119 119 VAL VAL H . n 
E 1 147 HIS 147 120 120 HIS HIS H . n 
E 1 148 GLU 148 121 121 GLU GLU H . n 
E 1 149 LYS 149 122 122 LYS LYS H . n 
E 1 150 ALA 150 123 123 ALA ALA H . n 
E 1 151 ASP 151 124 124 ASP ASP H . n 
E 1 152 ASP 152 125 125 ASP ASP H . n 
E 1 153 LEU 153 126 126 LEU LEU H . n 
E 1 154 GLY 154 127 127 GLY GLY H . n 
E 1 155 LYS 155 128 128 LYS ALA H . n 
E 1 156 GLY 156 129 129 GLY GLY H . n 
E 1 157 GLY 157 130 130 GLY GLY H . n 
E 1 158 ASN 158 131 131 ASN ASN H . n 
E 1 159 GLU 159 132 132 GLU GLU H . n 
E 1 160 GLU 160 133 133 GLU GLU H . n 
E 1 161 SER 161 134 134 SER SER H . n 
E 1 162 THR 162 135 135 THR THR H . n 
E 1 163 LYS 163 136 136 LYS LYS H . n 
E 1 164 THR 164 137 137 THR THR H . n 
E 1 165 GLY 165 138 138 GLY GLY H . n 
E 1 166 ASN 166 139 139 ASN ASN H . n 
E 1 167 ALA 167 140 140 ALA ALA H . n 
E 1 168 GLY 168 141 141 GLY GLY H . n 
E 1 169 SER 169 142 142 SER SER H . n 
E 1 170 ARG 170 143 143 ARG ARG H . n 
E 1 171 LEU 171 144 144 LEU LEU H . n 
E 1 172 ALA 172 145 145 ALA ALA H . n 
E 1 173 CYS 173 146 146 CYS CYS H . n 
E 1 174 GLY 174 147 147 GLY GLY H . n 
E 1 175 VAL 175 148 148 VAL VAL H . n 
E 1 176 ILE 176 149 149 ILE ILE H . n 
E 1 177 GLY 177 150 150 GLY GLY H . n 
E 1 178 ILE 178 151 151 ILE ILE H . n 
E 1 179 ALA 179 152 152 ALA ALA H . n 
E 1 180 GLN 180 153 153 GLN GLN H . n 
F 1 1   MET 1   -26 ?   ?   ?   E . n 
F 1 2   LYS 2   -25 ?   ?   ?   E . n 
F 1 3   HIS 3   -24 ?   ?   ?   E . n 
F 1 4   HIS 4   -23 ?   ?   ?   E . n 
F 1 5   HIS 5   -22 ?   ?   ?   E . n 
F 1 6   HIS 6   -21 ?   ?   ?   E . n 
F 1 7   HIS 7   -20 ?   ?   ?   E . n 
F 1 8   HIS 8   -19 ?   ?   ?   E . n 
F 1 9   PRO 9   -18 ?   ?   ?   E . n 
F 1 10  MET 10  -17 ?   ?   ?   E . n 
F 1 11  SER 11  -16 ?   ?   ?   E . n 
F 1 12  ASP 12  -15 ?   ?   ?   E . n 
F 1 13  TYR 13  -14 ?   ?   ?   E . n 
F 1 14  ASP 14  -13 ?   ?   ?   E . n 
F 1 15  ILE 15  -12 ?   ?   ?   E . n 
F 1 16  PRO 16  -11 ?   ?   ?   E . n 
F 1 17  THR 17  -10 ?   ?   ?   E . n 
F 1 18  THR 18  -9  ?   ?   ?   E . n 
F 1 19  GLU 19  -8  ?   ?   ?   E . n 
F 1 20  ASN 20  -7  ?   ?   ?   E . n 
F 1 21  LEU 21  -6  ?   ?   ?   E . n 
F 1 22  TYR 22  -5  ?   ?   ?   E . n 
F 1 23  PHE 23  -4  ?   ?   ?   E . n 
F 1 24  GLN 24  -3  ?   ?   ?   E . n 
F 1 25  GLY 25  -2  ?   ?   ?   E . n 
F 1 26  ALA 26  -1  ?   ?   ?   E . n 
F 1 27  MET 27  0   ?   ?   ?   E . n 
F 1 28  ALA 28  1   1   ALA ALA E . n 
F 1 29  THR 29  2   2   THR ALA E . n 
F 1 30  LYS 30  3   3   LYS LYS E . n 
F 1 31  ALA 31  4   4   ALA ALA E . n 
F 1 32  VAL 32  5   5   VAL VAL E . n 
F 1 33  CYS 33  6   6   CYS CYS E . n 
F 1 34  VAL 34  7   7   VAL VAL E . n 
F 1 35  LEU 35  8   8   LEU LEU E . n 
F 1 36  LYS 36  9   9   LYS LYS E . n 
F 1 37  GLY 37  10  10  GLY GLY E . n 
F 1 38  ASP 38  11  11  ASP ASP E . n 
F 1 39  GLY 39  12  12  GLY GLY E . n 
F 1 40  PRO 40  13  13  PRO PRO E . n 
F 1 41  VAL 41  14  14  VAL VAL E . n 
F 1 42  GLN 42  15  15  GLN GLN E . n 
F 1 43  GLY 43  16  16  GLY GLY E . n 
F 1 44  ILE 44  17  17  ILE ILE E . n 
F 1 45  ILE 45  18  18  ILE ILE E . n 
F 1 46  ASN 46  19  19  ASN ASN E . n 
F 1 47  PHE 47  20  20  PHE PHE E . n 
F 1 48  GLU 48  21  21  GLU GLU E . n 
F 1 49  GLN 49  22  22  GLN GLN E . n 
F 1 50  LYS 50  23  23  LYS LYS E . n 
F 1 51  GLU 51  24  24  GLU GLU E . n 
F 1 52  SER 52  25  25  SER SER E . n 
F 1 53  ASN 53  26  26  ASN ASN E . n 
F 1 54  GLY 54  27  27  GLY GLY E . n 
F 1 55  PRO 55  28  28  PRO PRO E . n 
F 1 56  VAL 56  29  29  VAL VAL E . n 
F 1 57  LYS 57  30  30  LYS LYS E . n 
F 1 58  VAL 58  31  31  VAL VAL E . n 
F 1 59  TRP 59  32  32  TRP TRP E . n 
F 1 60  GLY 60  33  33  GLY GLY E . n 
F 1 61  SER 61  34  34  SER SER E . n 
F 1 62  ILE 62  35  35  ILE ILE E . n 
F 1 63  LYS 63  36  36  LYS LYS E . n 
F 1 64  GLY 64  37  37  GLY GLY E . n 
F 1 65  LEU 65  38  38  LEU LEU E . n 
F 1 66  THR 66  39  39  THR THR E . n 
F 1 67  GLU 67  40  40  GLU GLU E . n 
F 1 68  GLY 68  41  41  GLY GLY E . n 
F 1 69  LEU 69  42  42  LEU LEU E . n 
F 1 70  HIS 70  43  43  HIS HIS E . n 
F 1 71  GLY 71  44  44  GLY GLY E . n 
F 1 72  PHE 72  45  45  PHE PHE E . n 
F 1 73  HIS 73  46  46  HIS HIS E . n 
F 1 74  VAL 74  47  47  VAL VAL E . n 
F 1 75  HIS 75  48  48  HIS HIS E . n 
F 1 76  GLU 76  49  49  GLU GLU E . n 
F 1 77  PHE 77  50  50  PHE PHE E . n 
F 1 78  GLY 78  51  51  GLY GLY E . n 
F 1 79  ASP 79  52  52  ASP ASP E . n 
F 1 80  ASN 80  53  53  ASN ASN E . n 
F 1 81  THR 81  54  54  THR THR E . n 
F 1 82  ALA 82  55  55  ALA ALA E . n 
F 1 83  GLY 83  56  56  GLY GLY E . n 
F 1 84  CYS 84  57  57  CYS CYS E . n 
F 1 85  THR 85  58  58  THR THR E . n 
F 1 86  SER 86  59  59  SER SER E . n 
F 1 87  ALA 87  60  60  ALA ALA E . n 
F 1 88  GLY 88  61  61  GLY GLY E . n 
F 1 89  PRO 89  62  62  PRO PRO E . n 
F 1 90  HIS 90  63  63  HIS HIS E . n 
F 1 91  PHE 91  64  64  PHE PHE E . n 
F 1 92  ASN 92  65  65  ASN ASN E . n 
F 1 93  PRO 93  66  66  PRO PRO E . n 
F 1 94  LEU 94  67  67  LEU LEU E . n 
F 1 95  SER 95  68  68  SER SER E . n 
F 1 96  ARG 96  69  69  ARG ARG E . n 
F 1 97  LYS 97  70  70  LYS LYS E . n 
F 1 98  HIS 98  71  71  HIS HIS E . n 
F 1 99  GLY 99  72  72  GLY GLY E . n 
F 1 100 GLY 100 73  73  GLY GLY E . n 
F 1 101 PRO 101 74  74  PRO PRO E . n 
F 1 102 LYS 102 75  75  LYS LYS E . n 
F 1 103 ASP 103 76  76  ASP ASP E . n 
F 1 104 GLU 104 77  77  GLU GLU E . n 
F 1 105 GLU 105 78  78  GLU GLU E . n 
F 1 106 ARG 106 79  79  ARG ARG E . n 
F 1 107 HIS 107 80  80  HIS HIS E . n 
F 1 108 VAL 108 81  81  VAL VAL E . n 
F 1 109 GLY 109 82  82  GLY GLY E . n 
F 1 110 ASP 110 83  83  ASP ASP E . n 
F 1 111 LEU 111 84  84  LEU LEU E . n 
F 1 112 GLY 112 85  85  GLY GLY E . n 
F 1 113 ASN 113 86  86  ASN ASN E . n 
F 1 114 VAL 114 87  87  VAL VAL E . n 
F 1 115 THR 115 88  88  THR THR E . n 
F 1 116 ALA 116 89  89  ALA ALA E . n 
F 1 117 ASP 117 90  90  ASP ASP E . n 
F 1 118 LYS 118 91  91  LYS LYS E . n 
F 1 119 ASP 119 92  92  ASP ASP E . n 
F 1 120 GLY 120 93  93  GLY GLY E . n 
F 1 121 VAL 121 94  94  VAL VAL E . n 
F 1 122 ALA 122 95  95  ALA ALA E . n 
F 1 123 ASP 123 96  96  ASP ASP E . n 
F 1 124 VAL 124 97  97  VAL VAL E . n 
F 1 125 SER 125 98  98  SER SER E . n 
F 1 126 ILE 126 99  99  ILE ILE E . n 
F 1 127 GLU 127 100 100 GLU GLU E . n 
F 1 128 ASP 128 101 101 ASP ASP E . n 
F 1 129 SER 129 102 102 SER SER E . n 
F 1 130 VAL 130 103 103 VAL VAL E . n 
F 1 131 ILE 131 104 104 ILE ILE E . n 
F 1 132 SER 132 105 105 SER SER E . n 
F 1 133 LEU 133 106 106 LEU LEU E . n 
F 1 134 SER 134 107 107 SER SER E . n 
F 1 135 GLY 135 108 108 GLY GLY E . n 
F 1 136 ASP 136 109 109 ASP ASP E . n 
F 1 137 HIS 137 110 110 HIS HIS E . n 
F 1 138 CYS 138 111 111 CYS CYS E . n 
F 1 139 ILE 139 112 112 ILE ILE E . n 
F 1 140 ILE 140 113 113 ILE ILE E . n 
F 1 141 GLY 141 114 114 GLY GLY E . n 
F 1 142 ARG 142 115 115 ARG ARG E . n 
F 1 143 THR 143 116 116 THR THR E . n 
F 1 144 LEU 144 117 117 LEU LEU E . n 
F 1 145 VAL 145 118 118 VAL VAL E . n 
F 1 146 VAL 146 119 119 VAL VAL E . n 
F 1 147 HIS 147 120 120 HIS HIS E . n 
F 1 148 GLU 148 121 121 GLU GLU E . n 
F 1 149 LYS 149 122 122 LYS LYS E . n 
F 1 150 ALA 150 123 123 ALA ALA E . n 
F 1 151 ASP 151 124 124 ASP ASP E . n 
F 1 152 ASP 152 125 125 ASP ASP E . n 
F 1 153 LEU 153 126 126 LEU LEU E . n 
F 1 154 GLY 154 127 127 GLY GLY E . n 
F 1 155 LYS 155 128 128 LYS LYS E . n 
F 1 156 GLY 156 129 129 GLY GLY E . n 
F 1 157 GLY 157 130 130 GLY GLY E . n 
F 1 158 ASN 158 131 131 ASN ASN E . n 
F 1 159 GLU 159 132 132 GLU GLU E . n 
F 1 160 GLU 160 133 133 GLU GLU E . n 
F 1 161 SER 161 134 134 SER SER E . n 
F 1 162 THR 162 135 135 THR THR E . n 
F 1 163 LYS 163 136 136 LYS LYS E . n 
F 1 164 THR 164 137 137 THR THR E . n 
F 1 165 GLY 165 138 138 GLY GLY E . n 
F 1 166 ASN 166 139 139 ASN ASN E . n 
F 1 167 ALA 167 140 140 ALA ALA E . n 
F 1 168 GLY 168 141 141 GLY GLY E . n 
F 1 169 SER 169 142 142 SER SER E . n 
F 1 170 ARG 170 143 143 ARG ARG E . n 
F 1 171 LEU 171 144 144 LEU LEU E . n 
F 1 172 ALA 172 145 145 ALA ALA E . n 
F 1 173 CYS 173 146 146 CYS CYS E . n 
F 1 174 GLY 174 147 147 GLY GLY E . n 
F 1 175 VAL 175 148 148 VAL VAL E . n 
F 1 176 ILE 176 149 149 ILE ILE E . n 
F 1 177 GLY 177 150 150 GLY GLY E . n 
F 1 178 ILE 178 151 151 ILE ILE E . n 
F 1 179 ALA 179 152 152 ALA ALA E . n 
F 1 180 GLN 180 153 153 GLN GLN E . n 
G 1 1   MET 1   -26 ?   ?   ?   F . n 
G 1 2   LYS 2   -25 ?   ?   ?   F . n 
G 1 3   HIS 3   -24 ?   ?   ?   F . n 
G 1 4   HIS 4   -23 ?   ?   ?   F . n 
G 1 5   HIS 5   -22 ?   ?   ?   F . n 
G 1 6   HIS 6   -21 ?   ?   ?   F . n 
G 1 7   HIS 7   -20 ?   ?   ?   F . n 
G 1 8   HIS 8   -19 ?   ?   ?   F . n 
G 1 9   PRO 9   -18 ?   ?   ?   F . n 
G 1 10  MET 10  -17 ?   ?   ?   F . n 
G 1 11  SER 11  -16 ?   ?   ?   F . n 
G 1 12  ASP 12  -15 ?   ?   ?   F . n 
G 1 13  TYR 13  -14 ?   ?   ?   F . n 
G 1 14  ASP 14  -13 ?   ?   ?   F . n 
G 1 15  ILE 15  -12 ?   ?   ?   F . n 
G 1 16  PRO 16  -11 ?   ?   ?   F . n 
G 1 17  THR 17  -10 ?   ?   ?   F . n 
G 1 18  THR 18  -9  ?   ?   ?   F . n 
G 1 19  GLU 19  -8  ?   ?   ?   F . n 
G 1 20  ASN 20  -7  ?   ?   ?   F . n 
G 1 21  LEU 21  -6  ?   ?   ?   F . n 
G 1 22  TYR 22  -5  ?   ?   ?   F . n 
G 1 23  PHE 23  -4  ?   ?   ?   F . n 
G 1 24  GLN 24  -3  ?   ?   ?   F . n 
G 1 25  GLY 25  -2  ?   ?   ?   F . n 
G 1 26  ALA 26  -1  ?   ?   ?   F . n 
G 1 27  MET 27  0   ?   ?   ?   F . n 
G 1 28  ALA 28  1   1   ALA ALA F . n 
G 1 29  THR 29  2   2   THR THR F . n 
G 1 30  LYS 30  3   3   LYS LYS F . n 
G 1 31  ALA 31  4   4   ALA ALA F . n 
G 1 32  VAL 32  5   5   VAL VAL F . n 
G 1 33  CYS 33  6   6   CYS CYS F . n 
G 1 34  VAL 34  7   7   VAL VAL F . n 
G 1 35  LEU 35  8   8   LEU LEU F . n 
G 1 36  LYS 36  9   9   LYS LYS F . n 
G 1 37  GLY 37  10  10  GLY GLY F . n 
G 1 38  ASP 38  11  11  ASP ASP F . n 
G 1 39  GLY 39  12  12  GLY GLY F . n 
G 1 40  PRO 40  13  13  PRO PRO F . n 
G 1 41  VAL 41  14  14  VAL VAL F . n 
G 1 42  GLN 42  15  15  GLN GLN F . n 
G 1 43  GLY 43  16  16  GLY GLY F . n 
G 1 44  ILE 44  17  17  ILE ILE F . n 
G 1 45  ILE 45  18  18  ILE ILE F . n 
G 1 46  ASN 46  19  19  ASN ASN F . n 
G 1 47  PHE 47  20  20  PHE PHE F . n 
G 1 48  GLU 48  21  21  GLU GLU F . n 
G 1 49  GLN 49  22  22  GLN GLN F . n 
G 1 50  LYS 50  23  23  LYS LYS F . n 
G 1 51  GLU 51  24  24  GLU GLU F . n 
G 1 52  SER 52  25  25  SER SER F . n 
G 1 53  ASN 53  26  26  ASN ASN F . n 
G 1 54  GLY 54  27  27  GLY GLY F . n 
G 1 55  PRO 55  28  28  PRO PRO F . n 
G 1 56  VAL 56  29  29  VAL VAL F . n 
G 1 57  LYS 57  30  30  LYS LYS F . n 
G 1 58  VAL 58  31  31  VAL VAL F . n 
G 1 59  TRP 59  32  32  TRP TRP F . n 
G 1 60  GLY 60  33  33  GLY GLY F . n 
G 1 61  SER 61  34  34  SER SER F . n 
G 1 62  ILE 62  35  35  ILE ILE F . n 
G 1 63  LYS 63  36  36  LYS LYS F . n 
G 1 64  GLY 64  37  37  GLY GLY F . n 
G 1 65  LEU 65  38  38  LEU LEU F . n 
G 1 66  THR 66  39  39  THR THR F . n 
G 1 67  GLU 67  40  40  GLU GLU F . n 
G 1 68  GLY 68  41  41  GLY GLY F . n 
G 1 69  LEU 69  42  42  LEU LEU F . n 
G 1 70  HIS 70  43  43  HIS HIS F . n 
G 1 71  GLY 71  44  44  GLY GLY F . n 
G 1 72  PHE 72  45  45  PHE PHE F . n 
G 1 73  HIS 73  46  46  HIS HIS F . n 
G 1 74  VAL 74  47  47  VAL VAL F . n 
G 1 75  HIS 75  48  48  HIS HIS F . n 
G 1 76  GLU 76  49  49  GLU GLU F . n 
G 1 77  PHE 77  50  50  PHE PHE F . n 
G 1 78  GLY 78  51  51  GLY GLY F . n 
G 1 79  ASP 79  52  52  ASP ASP F . n 
G 1 80  ASN 80  53  53  ASN ASN F . n 
G 1 81  THR 81  54  54  THR THR F . n 
G 1 82  ALA 82  55  55  ALA ALA F . n 
G 1 83  GLY 83  56  56  GLY GLY F . n 
G 1 84  CYS 84  57  57  CYS CYS F . n 
G 1 85  THR 85  58  58  THR THR F . n 
G 1 86  SER 86  59  59  SER SER F . n 
G 1 87  ALA 87  60  60  ALA ALA F . n 
G 1 88  GLY 88  61  61  GLY GLY F . n 
G 1 89  PRO 89  62  62  PRO PRO F . n 
G 1 90  HIS 90  63  63  HIS HIS F . n 
G 1 91  PHE 91  64  64  PHE PHE F . n 
G 1 92  ASN 92  65  65  ASN ASN F . n 
G 1 93  PRO 93  66  66  PRO PRO F . n 
G 1 94  LEU 94  67  67  LEU LEU F . n 
G 1 95  SER 95  68  68  SER SER F . n 
G 1 96  ARG 96  69  69  ARG ARG F . n 
G 1 97  LYS 97  70  70  LYS LYS F . n 
G 1 98  HIS 98  71  71  HIS HIS F . n 
G 1 99  GLY 99  72  72  GLY GLY F . n 
G 1 100 GLY 100 73  73  GLY GLY F . n 
G 1 101 PRO 101 74  74  PRO PRO F . n 
G 1 102 LYS 102 75  75  LYS LYS F . n 
G 1 103 ASP 103 76  76  ASP ASP F . n 
G 1 104 GLU 104 77  77  GLU GLU F . n 
G 1 105 GLU 105 78  78  GLU GLU F . n 
G 1 106 ARG 106 79  79  ARG ARG F . n 
G 1 107 HIS 107 80  80  HIS HIS F . n 
G 1 108 VAL 108 81  81  VAL VAL F . n 
G 1 109 GLY 109 82  82  GLY GLY F . n 
G 1 110 ASP 110 83  83  ASP ASP F . n 
G 1 111 LEU 111 84  84  LEU LEU F . n 
G 1 112 GLY 112 85  85  GLY GLY F . n 
G 1 113 ASN 113 86  86  ASN ASN F . n 
G 1 114 VAL 114 87  87  VAL VAL F . n 
G 1 115 THR 115 88  88  THR THR F . n 
G 1 116 ALA 116 89  89  ALA ALA F . n 
G 1 117 ASP 117 90  90  ASP ASP F . n 
G 1 118 LYS 118 91  91  LYS LYS F . n 
G 1 119 ASP 119 92  92  ASP ASP F . n 
G 1 120 GLY 120 93  93  GLY GLY F . n 
G 1 121 VAL 121 94  94  VAL VAL F . n 
G 1 122 ALA 122 95  95  ALA ALA F . n 
G 1 123 ASP 123 96  96  ASP ASP F . n 
G 1 124 VAL 124 97  97  VAL VAL F . n 
G 1 125 SER 125 98  98  SER SER F . n 
G 1 126 ILE 126 99  99  ILE ILE F . n 
G 1 127 GLU 127 100 100 GLU GLU F . n 
G 1 128 ASP 128 101 101 ASP ASP F . n 
G 1 129 SER 129 102 102 SER SER F . n 
G 1 130 VAL 130 103 103 VAL VAL F . n 
G 1 131 ILE 131 104 104 ILE ILE F . n 
G 1 132 SER 132 105 105 SER SER F . n 
G 1 133 LEU 133 106 106 LEU LEU F . n 
G 1 134 SER 134 107 107 SER SER F . n 
G 1 135 GLY 135 108 108 GLY GLY F . n 
G 1 136 ASP 136 109 109 ASP ASP F . n 
G 1 137 HIS 137 110 110 HIS HIS F . n 
G 1 138 CYS 138 111 111 CYS CYS F . n 
G 1 139 ILE 139 112 112 ILE ILE F . n 
G 1 140 ILE 140 113 113 ILE ILE F . n 
G 1 141 GLY 141 114 114 GLY GLY F . n 
G 1 142 ARG 142 115 115 ARG ARG F . n 
G 1 143 THR 143 116 116 THR THR F . n 
G 1 144 LEU 144 117 117 LEU LEU F . n 
G 1 145 VAL 145 118 118 VAL VAL F . n 
G 1 146 VAL 146 119 119 VAL VAL F . n 
G 1 147 HIS 147 120 120 HIS HIS F . n 
G 1 148 GLU 148 121 121 GLU GLU F . n 
G 1 149 LYS 149 122 122 LYS LYS F . n 
G 1 150 ALA 150 123 123 ALA ALA F . n 
G 1 151 ASP 151 124 124 ASP ASP F . n 
G 1 152 ASP 152 125 125 ASP ASP F . n 
G 1 153 LEU 153 126 126 LEU LEU F . n 
G 1 154 GLY 154 127 127 GLY GLY F . n 
G 1 155 LYS 155 128 128 LYS LYS F . n 
G 1 156 GLY 156 129 129 GLY GLY F . n 
G 1 157 GLY 157 130 130 GLY GLY F . n 
G 1 158 ASN 158 131 131 ASN ASN F . n 
G 1 159 GLU 159 132 132 GLU GLU F . n 
G 1 160 GLU 160 133 133 GLU GLU F . n 
G 1 161 SER 161 134 134 SER SER F . n 
G 1 162 THR 162 135 135 THR THR F . n 
G 1 163 LYS 163 136 136 LYS LYS F . n 
G 1 164 THR 164 137 137 THR THR F . n 
G 1 165 GLY 165 138 138 GLY GLY F . n 
G 1 166 ASN 166 139 139 ASN ASN F . n 
G 1 167 ALA 167 140 140 ALA ALA F . n 
G 1 168 GLY 168 141 141 GLY GLY F . n 
G 1 169 SER 169 142 142 SER SER F . n 
G 1 170 ARG 170 143 143 ARG ARG F . n 
G 1 171 LEU 171 144 144 LEU LEU F . n 
G 1 172 ALA 172 145 145 ALA ALA F . n 
G 1 173 CYS 173 146 146 CYS CYS F . n 
G 1 174 GLY 174 147 147 GLY GLY F . n 
G 1 175 VAL 175 148 148 VAL VAL F . n 
G 1 176 ILE 176 149 149 ILE ILE F . n 
G 1 177 GLY 177 150 150 GLY GLY F . n 
G 1 178 ILE 178 151 151 ILE ILE F . n 
G 1 179 ALA 179 152 152 ALA ALA F . n 
G 1 180 GLN 180 153 153 GLN GLN F . n 
H 1 1   MET 1   -26 ?   ?   ?   G . n 
H 1 2   LYS 2   -25 ?   ?   ?   G . n 
H 1 3   HIS 3   -24 ?   ?   ?   G . n 
H 1 4   HIS 4   -23 ?   ?   ?   G . n 
H 1 5   HIS 5   -22 ?   ?   ?   G . n 
H 1 6   HIS 6   -21 ?   ?   ?   G . n 
H 1 7   HIS 7   -20 ?   ?   ?   G . n 
H 1 8   HIS 8   -19 ?   ?   ?   G . n 
H 1 9   PRO 9   -18 ?   ?   ?   G . n 
H 1 10  MET 10  -17 ?   ?   ?   G . n 
H 1 11  SER 11  -16 ?   ?   ?   G . n 
H 1 12  ASP 12  -15 ?   ?   ?   G . n 
H 1 13  TYR 13  -14 ?   ?   ?   G . n 
H 1 14  ASP 14  -13 ?   ?   ?   G . n 
H 1 15  ILE 15  -12 ?   ?   ?   G . n 
H 1 16  PRO 16  -11 ?   ?   ?   G . n 
H 1 17  THR 17  -10 ?   ?   ?   G . n 
H 1 18  THR 18  -9  ?   ?   ?   G . n 
H 1 19  GLU 19  -8  ?   ?   ?   G . n 
H 1 20  ASN 20  -7  ?   ?   ?   G . n 
H 1 21  LEU 21  -6  ?   ?   ?   G . n 
H 1 22  TYR 22  -5  ?   ?   ?   G . n 
H 1 23  PHE 23  -4  ?   ?   ?   G . n 
H 1 24  GLN 24  -3  ?   ?   ?   G . n 
H 1 25  GLY 25  -2  ?   ?   ?   G . n 
H 1 26  ALA 26  -1  ?   ?   ?   G . n 
H 1 27  MET 27  0   ?   ?   ?   G . n 
H 1 28  ALA 28  1   ?   ?   ?   G . n 
H 1 29  THR 29  2   2   THR THR G . n 
H 1 30  LYS 30  3   3   LYS LYS G . n 
H 1 31  ALA 31  4   4   ALA ALA G . n 
H 1 32  VAL 32  5   5   VAL VAL G . n 
H 1 33  CYS 33  6   6   CYS CYS G . n 
H 1 34  VAL 34  7   7   VAL VAL G . n 
H 1 35  LEU 35  8   8   LEU LEU G . n 
H 1 36  LYS 36  9   9   LYS LYS G . n 
H 1 37  GLY 37  10  10  GLY GLY G . n 
H 1 38  ASP 38  11  11  ASP ASP G . n 
H 1 39  GLY 39  12  12  GLY GLY G . n 
H 1 40  PRO 40  13  13  PRO PRO G . n 
H 1 41  VAL 41  14  14  VAL VAL G . n 
H 1 42  GLN 42  15  15  GLN GLN G . n 
H 1 43  GLY 43  16  16  GLY GLY G . n 
H 1 44  ILE 44  17  17  ILE ILE G . n 
H 1 45  ILE 45  18  18  ILE ILE G . n 
H 1 46  ASN 46  19  19  ASN ASN G . n 
H 1 47  PHE 47  20  20  PHE PHE G . n 
H 1 48  GLU 48  21  21  GLU GLU G . n 
H 1 49  GLN 49  22  22  GLN GLN G . n 
H 1 50  LYS 50  23  23  LYS LYS G . n 
H 1 51  GLU 51  24  24  GLU GLU G . n 
H 1 52  SER 52  25  25  SER SER G . n 
H 1 53  ASN 53  26  26  ASN ASN G . n 
H 1 54  GLY 54  27  27  GLY GLY G . n 
H 1 55  PRO 55  28  28  PRO PRO G . n 
H 1 56  VAL 56  29  29  VAL VAL G . n 
H 1 57  LYS 57  30  30  LYS LYS G . n 
H 1 58  VAL 58  31  31  VAL VAL G . n 
H 1 59  TRP 59  32  32  TRP TRP G . n 
H 1 60  GLY 60  33  33  GLY GLY G . n 
H 1 61  SER 61  34  34  SER SER G . n 
H 1 62  ILE 62  35  35  ILE ILE G . n 
H 1 63  LYS 63  36  36  LYS LYS G . n 
H 1 64  GLY 64  37  37  GLY GLY G . n 
H 1 65  LEU 65  38  38  LEU LEU G . n 
H 1 66  THR 66  39  39  THR THR G . n 
H 1 67  GLU 67  40  40  GLU GLU G . n 
H 1 68  GLY 68  41  41  GLY GLY G . n 
H 1 69  LEU 69  42  42  LEU LEU G . n 
H 1 70  HIS 70  43  43  HIS HIS G . n 
H 1 71  GLY 71  44  44  GLY GLY G . n 
H 1 72  PHE 72  45  45  PHE PHE G . n 
H 1 73  HIS 73  46  46  HIS HIS G . n 
H 1 74  VAL 74  47  47  VAL VAL G . n 
H 1 75  HIS 75  48  48  HIS HIS G . n 
H 1 76  GLU 76  49  49  GLU GLU G . n 
H 1 77  PHE 77  50  50  PHE PHE G . n 
H 1 78  GLY 78  51  51  GLY GLY G . n 
H 1 79  ASP 79  52  52  ASP ASP G . n 
H 1 80  ASN 80  53  53  ASN ASN G . n 
H 1 81  THR 81  54  54  THR THR G . n 
H 1 82  ALA 82  55  55  ALA ALA G . n 
H 1 83  GLY 83  56  56  GLY GLY G . n 
H 1 84  CYS 84  57  57  CYS CYS G . n 
H 1 85  THR 85  58  58  THR THR G . n 
H 1 86  SER 86  59  59  SER SER G . n 
H 1 87  ALA 87  60  60  ALA ALA G . n 
H 1 88  GLY 88  61  61  GLY GLY G . n 
H 1 89  PRO 89  62  62  PRO PRO G . n 
H 1 90  HIS 90  63  63  HIS HIS G . n 
H 1 91  PHE 91  64  64  PHE PHE G . n 
H 1 92  ASN 92  65  65  ASN ASN G . n 
H 1 93  PRO 93  66  66  PRO PRO G . n 
H 1 94  LEU 94  67  67  LEU LEU G . n 
H 1 95  SER 95  68  68  SER SER G . n 
H 1 96  ARG 96  69  69  ARG ARG G . n 
H 1 97  LYS 97  70  70  LYS LYS G . n 
H 1 98  HIS 98  71  71  HIS HIS G . n 
H 1 99  GLY 99  72  72  GLY GLY G . n 
H 1 100 GLY 100 73  73  GLY GLY G . n 
H 1 101 PRO 101 74  74  PRO PRO G . n 
H 1 102 LYS 102 75  75  LYS LYS G . n 
H 1 103 ASP 103 76  76  ASP ASP G . n 
H 1 104 GLU 104 77  77  GLU GLU G . n 
H 1 105 GLU 105 78  78  GLU GLU G . n 
H 1 106 ARG 106 79  79  ARG ARG G . n 
H 1 107 HIS 107 80  80  HIS HIS G . n 
H 1 108 VAL 108 81  81  VAL VAL G . n 
H 1 109 GLY 109 82  82  GLY GLY G . n 
H 1 110 ASP 110 83  83  ASP ASP G . n 
H 1 111 LEU 111 84  84  LEU LEU G . n 
H 1 112 GLY 112 85  85  GLY GLY G . n 
H 1 113 ASN 113 86  86  ASN ASN G . n 
H 1 114 VAL 114 87  87  VAL VAL G . n 
H 1 115 THR 115 88  88  THR THR G . n 
H 1 116 ALA 116 89  89  ALA ALA G . n 
H 1 117 ASP 117 90  90  ASP ASP G . n 
H 1 118 LYS 118 91  91  LYS LYS G . n 
H 1 119 ASP 119 92  92  ASP ASP G . n 
H 1 120 GLY 120 93  93  GLY GLY G . n 
H 1 121 VAL 121 94  94  VAL VAL G . n 
H 1 122 ALA 122 95  95  ALA ALA G . n 
H 1 123 ASP 123 96  96  ASP ASP G . n 
H 1 124 VAL 124 97  97  VAL VAL G . n 
H 1 125 SER 125 98  98  SER SER G . n 
H 1 126 ILE 126 99  99  ILE ILE G . n 
H 1 127 GLU 127 100 100 GLU GLU G . n 
H 1 128 ASP 128 101 101 ASP ASP G . n 
H 1 129 SER 129 102 102 SER SER G . n 
H 1 130 VAL 130 103 103 VAL VAL G . n 
H 1 131 ILE 131 104 104 ILE ILE G . n 
H 1 132 SER 132 105 105 SER SER G . n 
H 1 133 LEU 133 106 106 LEU LEU G . n 
H 1 134 SER 134 107 107 SER SER G . n 
H 1 135 GLY 135 108 108 GLY GLY G . n 
H 1 136 ASP 136 109 109 ASP ASP G . n 
H 1 137 HIS 137 110 110 HIS HIS G . n 
H 1 138 CYS 138 111 111 CYS CYS G . n 
H 1 139 ILE 139 112 112 ILE ILE G . n 
H 1 140 ILE 140 113 113 ILE ILE G . n 
H 1 141 GLY 141 114 114 GLY GLY G . n 
H 1 142 ARG 142 115 115 ARG ARG G . n 
H 1 143 THR 143 116 116 THR THR G . n 
H 1 144 LEU 144 117 117 LEU LEU G . n 
H 1 145 VAL 145 118 118 VAL VAL G . n 
H 1 146 VAL 146 119 119 VAL VAL G . n 
H 1 147 HIS 147 120 120 HIS HIS G . n 
H 1 148 GLU 148 121 121 GLU GLU G . n 
H 1 149 LYS 149 122 122 LYS LYS G . n 
H 1 150 ALA 150 123 123 ALA ALA G . n 
H 1 151 ASP 151 124 124 ASP ASP G . n 
H 1 152 ASP 152 125 125 ASP ASP G . n 
H 1 153 LEU 153 126 126 LEU LEU G . n 
H 1 154 GLY 154 127 127 GLY GLY G . n 
H 1 155 LYS 155 128 128 LYS LYS G . n 
H 1 156 GLY 156 129 129 GLY GLY G . n 
H 1 157 GLY 157 130 130 GLY GLY G . n 
H 1 158 ASN 158 131 131 ASN ASN G . n 
H 1 159 GLU 159 132 132 GLU GLU G . n 
H 1 160 GLU 160 133 133 GLU GLU G . n 
H 1 161 SER 161 134 134 SER SER G . n 
H 1 162 THR 162 135 135 THR THR G . n 
H 1 163 LYS 163 136 136 LYS LYS G . n 
H 1 164 THR 164 137 137 THR THR G . n 
H 1 165 GLY 165 138 138 GLY GLY G . n 
H 1 166 ASN 166 139 139 ASN ASN G . n 
H 1 167 ALA 167 140 140 ALA ALA G . n 
H 1 168 GLY 168 141 141 GLY GLY G . n 
H 1 169 SER 169 142 142 SER SER G . n 
H 1 170 ARG 170 143 143 ARG ARG G . n 
H 1 171 LEU 171 144 144 LEU LEU G . n 
H 1 172 ALA 172 145 145 ALA ALA G . n 
H 1 173 CYS 173 146 146 CYS CYS G . n 
H 1 174 GLY 174 147 147 GLY GLY G . n 
H 1 175 VAL 175 148 148 VAL VAL G . n 
H 1 176 ILE 176 149 149 ILE ILE G . n 
H 1 177 GLY 177 150 150 GLY GLY G . n 
H 1 178 ILE 178 151 151 ILE ILE G . n 
H 1 179 ALA 179 152 152 ALA ALA G . n 
H 1 180 GLN 180 153 153 GLN GLN G . 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 153 126 126 LEU LEU 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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              balapaddy@gmail.com 
_pdbx_contact_author.name_first         Balasundaram 
_pdbx_contact_author.name_last          Padmanabhan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9905-9464 
# 
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 2    GOL GOL A . 
M  2 ZN  1   201 3    ZN  ZN  B . 
N  4 I2G 1   202 2    I2G MI2 B . 
O  3 GOL 1   203 1    GOL GOL B . 
P  3 GOL 1   204 3    GOL GOL B . 
Q  3 GOL 1   205 4    GOL GOL B . 
R  2 ZN  1   201 1    ZN  ZN  D . 
S  4 I2G 1   202 1    I2G MI2 D . 
T  3 GOL 1   203 5    GOL GOL D . 
U  2 ZN  1   201 4    ZN  ZN  C . 
V  4 I2G 1   202 3    I2G MI2 C . 
W  2 ZN  1   201 5    ZN  ZN  H . 
X  5 DMS 1   201 201  DMS DMS E . 
Y  2 ZN  1   202 6    ZN  ZN  E . 
Z  2 ZN  1   201 7    ZN  ZN  F . 
AA 2 ZN  1   201 8    ZN  ZN  G . 
BA 2 ZN  1   201 9    ZN  ZN  I . 
CA 4 I2G 1   202 4    I2G MI2 I . 
DA 6 HOH 1   301 1190 HOH HOH A . 
DA 6 HOH 2   302 806  HOH HOH A . 
DA 6 HOH 3   303 283  HOH HOH A . 
DA 6 HOH 4   304 989  HOH HOH A . 
DA 6 HOH 5   305 683  HOH HOH A . 
DA 6 HOH 6   306 685  HOH HOH A . 
DA 6 HOH 7   307 8    HOH HOH A . 
DA 6 HOH 8   308 1010 HOH HOH A . 
DA 6 HOH 9   309 454  HOH HOH A . 
DA 6 HOH 10  310 579  HOH HOH A . 
DA 6 HOH 11  311 807  HOH HOH A . 
DA 6 HOH 12  312 378  HOH HOH A . 
DA 6 HOH 13  313 915  HOH HOH A . 
DA 6 HOH 14  314 618  HOH HOH A . 
DA 6 HOH 15  315 897  HOH HOH A . 
DA 6 HOH 16  316 145  HOH HOH A . 
DA 6 HOH 17  317 1080 HOH HOH A . 
DA 6 HOH 18  318 486  HOH HOH A . 
DA 6 HOH 19  319 520  HOH HOH A . 
DA 6 HOH 20  320 484  HOH HOH A . 
DA 6 HOH 21  321 185  HOH HOH A . 
DA 6 HOH 22  322 133  HOH HOH A . 
DA 6 HOH 23  323 159  HOH HOH A . 
DA 6 HOH 24  324 176  HOH HOH A . 
DA 6 HOH 25  325 390  HOH HOH A . 
DA 6 HOH 26  326 174  HOH HOH A . 
DA 6 HOH 27  327 273  HOH HOH A . 
DA 6 HOH 28  328 330  HOH HOH A . 
DA 6 HOH 29  329 27   HOH HOH A . 
DA 6 HOH 30  330 501  HOH HOH A . 
DA 6 HOH 31  331 747  HOH HOH A . 
DA 6 HOH 32  332 1160 HOH HOH A . 
DA 6 HOH 33  333 218  HOH HOH A . 
DA 6 HOH 34  334 64   HOH HOH A . 
DA 6 HOH 35  335 259  HOH HOH A . 
DA 6 HOH 36  336 39   HOH HOH A . 
DA 6 HOH 37  337 13   HOH HOH A . 
DA 6 HOH 38  338 1111 HOH HOH A . 
DA 6 HOH 39  339 335  HOH HOH A . 
DA 6 HOH 40  340 32   HOH HOH A . 
DA 6 HOH 41  341 1073 HOH HOH A . 
DA 6 HOH 42  342 138  HOH HOH A . 
DA 6 HOH 43  343 111  HOH HOH A . 
DA 6 HOH 44  344 98   HOH HOH A . 
DA 6 HOH 45  345 83   HOH HOH A . 
DA 6 HOH 46  346 59   HOH HOH A . 
DA 6 HOH 47  347 556  HOH HOH A . 
DA 6 HOH 48  348 312  HOH HOH A . 
DA 6 HOH 49  349 429  HOH HOH A . 
DA 6 HOH 50  350 156  HOH HOH A . 
DA 6 HOH 51  351 1074 HOH HOH A . 
DA 6 HOH 52  352 1040 HOH HOH A . 
DA 6 HOH 53  353 1025 HOH HOH A . 
DA 6 HOH 54  354 748  HOH HOH A . 
DA 6 HOH 55  355 492  HOH HOH A . 
DA 6 HOH 56  356 68   HOH HOH A . 
DA 6 HOH 57  357 531  HOH HOH A . 
DA 6 HOH 58  358 115  HOH HOH A . 
DA 6 HOH 59  359 126  HOH HOH A . 
DA 6 HOH 60  360 1096 HOH HOH A . 
DA 6 HOH 61  361 422  HOH HOH A . 
DA 6 HOH 62  362 565  HOH HOH A . 
DA 6 HOH 63  363 191  HOH HOH A . 
DA 6 HOH 64  364 269  HOH HOH A . 
DA 6 HOH 65  365 878  HOH HOH A . 
DA 6 HOH 66  366 519  HOH HOH A . 
DA 6 HOH 67  367 86   HOH HOH A . 
DA 6 HOH 68  368 667  HOH HOH A . 
DA 6 HOH 69  369 151  HOH HOH A . 
DA 6 HOH 70  370 95   HOH HOH A . 
DA 6 HOH 71  371 188  HOH HOH A . 
DA 6 HOH 72  372 687  HOH HOH A . 
DA 6 HOH 73  373 270  HOH HOH A . 
DA 6 HOH 74  374 609  HOH HOH A . 
DA 6 HOH 75  375 272  HOH HOH A . 
DA 6 HOH 76  376 1055 HOH HOH A . 
DA 6 HOH 77  377 50   HOH HOH A . 
DA 6 HOH 78  378 1021 HOH HOH A . 
DA 6 HOH 79  379 929  HOH HOH A . 
DA 6 HOH 80  380 225  HOH HOH A . 
DA 6 HOH 81  381 1028 HOH HOH A . 
DA 6 HOH 82  382 180  HOH HOH A . 
DA 6 HOH 83  383 304  HOH HOH A . 
DA 6 HOH 84  384 1100 HOH HOH A . 
DA 6 HOH 85  385 376  HOH HOH A . 
DA 6 HOH 86  386 202  HOH HOH A . 
DA 6 HOH 87  387 395  HOH HOH A . 
DA 6 HOH 88  388 641  HOH HOH A . 
DA 6 HOH 89  389 210  HOH HOH A . 
DA 6 HOH 90  390 637  HOH HOH A . 
DA 6 HOH 91  391 705  HOH HOH A . 
DA 6 HOH 92  392 54   HOH HOH A . 
DA 6 HOH 93  393 417  HOH HOH A . 
DA 6 HOH 94  394 950  HOH HOH A . 
DA 6 HOH 95  395 510  HOH HOH A . 
DA 6 HOH 96  396 608  HOH HOH A . 
DA 6 HOH 97  397 590  HOH HOH A . 
DA 6 HOH 98  398 1163 HOH HOH A . 
DA 6 HOH 99  399 372  HOH HOH A . 
DA 6 HOH 100 400 613  HOH HOH A . 
DA 6 HOH 101 401 555  HOH HOH A . 
DA 6 HOH 102 402 1009 HOH HOH A . 
DA 6 HOH 103 403 636  HOH HOH A . 
DA 6 HOH 104 404 580  HOH HOH A . 
DA 6 HOH 105 405 858  HOH HOH A . 
DA 6 HOH 106 406 701  HOH HOH A . 
DA 6 HOH 107 407 1123 HOH HOH A . 
DA 6 HOH 108 408 5    HOH HOH A . 
DA 6 HOH 109 409 397  HOH HOH A . 
DA 6 HOH 110 410 1199 HOH HOH A . 
DA 6 HOH 111 411 534  HOH HOH A . 
DA 6 HOH 112 412 432  HOH HOH A . 
DA 6 HOH 113 413 346  HOH HOH A . 
DA 6 HOH 114 414 809  HOH HOH A . 
DA 6 HOH 115 415 594  HOH HOH A . 
DA 6 HOH 116 416 678  HOH HOH A . 
DA 6 HOH 117 417 862  HOH HOH A . 
DA 6 HOH 118 418 818  HOH HOH A . 
DA 6 HOH 119 419 860  HOH HOH A . 
DA 6 HOH 120 420 532  HOH HOH A . 
DA 6 HOH 121 421 368  HOH HOH A . 
DA 6 HOH 122 422 819  HOH HOH A . 
DA 6 HOH 123 423 727  HOH HOH A . 
DA 6 HOH 124 424 767  HOH HOH A . 
DA 6 HOH 125 425 808  HOH HOH A . 
DA 6 HOH 126 426 1168 HOH HOH A . 
DA 6 HOH 127 427 1071 HOH HOH A . 
DA 6 HOH 128 428 813  HOH HOH A . 
DA 6 HOH 129 429 816  HOH HOH A . 
DA 6 HOH 130 430 856  HOH HOH A . 
DA 6 HOH 131 431 1172 HOH HOH A . 
DA 6 HOH 132 432 810  HOH HOH A . 
DA 6 HOH 133 433 639  HOH HOH A . 
DA 6 HOH 134 434 814  HOH HOH A . 
DA 6 HOH 135 435 815  HOH HOH A . 
DA 6 HOH 136 436 474  HOH HOH A . 
DA 6 HOH 137 437 292  HOH HOH A . 
DA 6 HOH 138 438 859  HOH HOH A . 
DA 6 HOH 139 439 681  HOH HOH A . 
DA 6 HOH 140 440 513  HOH HOH A . 
DA 6 HOH 141 441 812  HOH HOH A . 
DA 6 HOH 142 442 632  HOH HOH A . 
DA 6 HOH 143 443 516  HOH HOH A . 
DA 6 HOH 144 444 1200 HOH HOH A . 
DA 6 HOH 145 445 863  HOH HOH A . 
DA 6 HOH 146 446 857  HOH HOH A . 
DA 6 HOH 147 447 861  HOH HOH A . 
EA 6 HOH 1   301 1175 HOH HOH B . 
EA 6 HOH 2   302 1053 HOH HOH B . 
EA 6 HOH 3   303 968  HOH HOH B . 
EA 6 HOH 4   304 898  HOH HOH B . 
EA 6 HOH 5   305 421  HOH HOH B . 
EA 6 HOH 6   306 250  HOH HOH B . 
EA 6 HOH 7   307 282  HOH HOH B . 
EA 6 HOH 8   308 587  HOH HOH B . 
EA 6 HOH 9   309 496  HOH HOH B . 
EA 6 HOH 10  310 675  HOH HOH B . 
EA 6 HOH 11  311 1024 HOH HOH B . 
EA 6 HOH 12  312 917  HOH HOH B . 
EA 6 HOH 13  313 334  HOH HOH B . 
EA 6 HOH 14  314 23   HOH HOH B . 
EA 6 HOH 15  315 896  HOH HOH B . 
EA 6 HOH 16  316 598  HOH HOH B . 
EA 6 HOH 17  317 34   HOH HOH B . 
EA 6 HOH 18  318 1136 HOH HOH B . 
EA 6 HOH 19  319 444  HOH HOH B . 
EA 6 HOH 20  320 947  HOH HOH B . 
EA 6 HOH 21  321 103  HOH HOH B . 
EA 6 HOH 22  322 1184 HOH HOH B . 
EA 6 HOH 23  323 1177 HOH HOH B . 
EA 6 HOH 24  324 663  HOH HOH B . 
EA 6 HOH 25  325 697  HOH HOH B . 
EA 6 HOH 26  326 337  HOH HOH B . 
EA 6 HOH 27  327 84   HOH HOH B . 
EA 6 HOH 28  328 1002 HOH HOH B . 
EA 6 HOH 29  329 116  HOH HOH B . 
EA 6 HOH 30  330 713  HOH HOH B . 
EA 6 HOH 31  331 993  HOH HOH B . 
EA 6 HOH 32  332 248  HOH HOH B . 
EA 6 HOH 33  333 426  HOH HOH B . 
EA 6 HOH 34  334 1115 HOH HOH B . 
EA 6 HOH 35  335 25   HOH HOH B . 
EA 6 HOH 36  336 409  HOH HOH B . 
EA 6 HOH 37  337 980  HOH HOH B . 
EA 6 HOH 38  338 195  HOH HOH B . 
EA 6 HOH 39  339 206  HOH HOH B . 
EA 6 HOH 40  340 61   HOH HOH B . 
EA 6 HOH 41  341 249  HOH HOH B . 
EA 6 HOH 42  342 1090 HOH HOH B . 
EA 6 HOH 43  343 310  HOH HOH B . 
EA 6 HOH 44  344 24   HOH HOH B . 
EA 6 HOH 45  345 976  HOH HOH B . 
EA 6 HOH 46  346 239  HOH HOH B . 
EA 6 HOH 47  347 756  HOH HOH B . 
EA 6 HOH 48  348 72   HOH HOH B . 
EA 6 HOH 49  349 797  HOH HOH B . 
EA 6 HOH 50  350 633  HOH HOH B . 
EA 6 HOH 51  351 91   HOH HOH B . 
EA 6 HOH 52  352 751  HOH HOH B . 
EA 6 HOH 53  353 60   HOH HOH B . 
EA 6 HOH 54  354 746  HOH HOH B . 
EA 6 HOH 55  355 905  HOH HOH B . 
EA 6 HOH 56  356 240  HOH HOH B . 
EA 6 HOH 57  357 90   HOH HOH B . 
EA 6 HOH 58  358 1089 HOH HOH B . 
EA 6 HOH 59  359 92   HOH HOH B . 
EA 6 HOH 60  360 262  HOH HOH B . 
EA 6 HOH 61  361 242  HOH HOH B . 
EA 6 HOH 62  362 35   HOH HOH B . 
EA 6 HOH 63  363 582  HOH HOH B . 
EA 6 HOH 64  364 75   HOH HOH B . 
EA 6 HOH 65  365 535  HOH HOH B . 
EA 6 HOH 66  366 381  HOH HOH B . 
EA 6 HOH 67  367 936  HOH HOH B . 
EA 6 HOH 68  368 958  HOH HOH B . 
EA 6 HOH 69  369 200  HOH HOH B . 
EA 6 HOH 70  370 82   HOH HOH B . 
EA 6 HOH 71  371 179  HOH HOH B . 
EA 6 HOH 72  372 167  HOH HOH B . 
EA 6 HOH 73  373 971  HOH HOH B . 
EA 6 HOH 74  374 55   HOH HOH B . 
EA 6 HOH 75  375 150  HOH HOH B . 
EA 6 HOH 76  376 749  HOH HOH B . 
EA 6 HOH 77  377 704  HOH HOH B . 
EA 6 HOH 78  378 1187 HOH HOH B . 
EA 6 HOH 79  379 1008 HOH HOH B . 
EA 6 HOH 80  380 241  HOH HOH B . 
EA 6 HOH 81  381 155  HOH HOH B . 
EA 6 HOH 82  382 44   HOH HOH B . 
EA 6 HOH 83  383 581  HOH HOH B . 
EA 6 HOH 84  384 108  HOH HOH B . 
EA 6 HOH 85  385 120  HOH HOH B . 
EA 6 HOH 86  386 468  HOH HOH B . 
EA 6 HOH 87  387 914  HOH HOH B . 
EA 6 HOH 88  388 70   HOH HOH B . 
EA 6 HOH 89  389 175  HOH HOH B . 
EA 6 HOH 90  390 187  HOH HOH B . 
EA 6 HOH 91  391 104  HOH HOH B . 
EA 6 HOH 92  392 596  HOH HOH B . 
EA 6 HOH 93  393 690  HOH HOH B . 
EA 6 HOH 94  394 158  HOH HOH B . 
EA 6 HOH 95  395 285  HOH HOH B . 
EA 6 HOH 96  396 265  HOH HOH B . 
EA 6 HOH 97  397 198  HOH HOH B . 
EA 6 HOH 98  398 916  HOH HOH B . 
EA 6 HOH 99  399 1033 HOH HOH B . 
EA 6 HOH 100 400 456  HOH HOH B . 
EA 6 HOH 101 401 4    HOH HOH B . 
EA 6 HOH 102 402 186  HOH HOH B . 
EA 6 HOH 103 403 975  HOH HOH B . 
EA 6 HOH 104 404 576  HOH HOH B . 
EA 6 HOH 105 405 723  HOH HOH B . 
EA 6 HOH 106 406 996  HOH HOH B . 
EA 6 HOH 107 407 1161 HOH HOH B . 
EA 6 HOH 108 408 777  HOH HOH B . 
EA 6 HOH 109 409 499  HOH HOH B . 
EA 6 HOH 110 410 118  HOH HOH B . 
EA 6 HOH 111 411 721  HOH HOH B . 
EA 6 HOH 112 412 775  HOH HOH B . 
EA 6 HOH 113 413 358  HOH HOH B . 
EA 6 HOH 114 414 1201 HOH HOH B . 
EA 6 HOH 115 415 741  HOH HOH B . 
EA 6 HOH 116 416 1202 HOH HOH B . 
EA 6 HOH 117 417 388  HOH HOH B . 
EA 6 HOH 118 418 223  HOH HOH B . 
EA 6 HOH 119 419 757  HOH HOH B . 
EA 6 HOH 120 420 141  HOH HOH B . 
EA 6 HOH 121 421 93   HOH HOH B . 
EA 6 HOH 122 422 745  HOH HOH B . 
EA 6 HOH 123 423 419  HOH HOH B . 
EA 6 HOH 124 424 811  HOH HOH B . 
EA 6 HOH 125 425 977  HOH HOH B . 
EA 6 HOH 126 426 436  HOH HOH B . 
EA 6 HOH 127 427 530  HOH HOH B . 
EA 6 HOH 128 428 607  HOH HOH B . 
EA 6 HOH 129 429 566  HOH HOH B . 
EA 6 HOH 130 430 821  HOH HOH B . 
EA 6 HOH 131 431 497  HOH HOH B . 
EA 6 HOH 132 432 642  HOH HOH B . 
EA 6 HOH 133 433 1166 HOH HOH B . 
EA 6 HOH 134 434 820  HOH HOH B . 
EA 6 HOH 135 435 664  HOH HOH B . 
EA 6 HOH 136 436 1142 HOH HOH B . 
EA 6 HOH 137 437 1069 HOH HOH B . 
EA 6 HOH 138 438 734  HOH HOH B . 
EA 6 HOH 139 439 629  HOH HOH B . 
EA 6 HOH 140 440 1191 HOH HOH B . 
EA 6 HOH 141 441 1072 HOH HOH B . 
EA 6 HOH 142 442 653  HOH HOH B . 
EA 6 HOH 143 443 889  HOH HOH B . 
EA 6 HOH 144 444 752  HOH HOH B . 
EA 6 HOH 145 445 755  HOH HOH B . 
EA 6 HOH 146 446 994  HOH HOH B . 
EA 6 HOH 147 447 986  HOH HOH B . 
EA 6 HOH 148 448 817  HOH HOH B . 
EA 6 HOH 149 449 928  HOH HOH B . 
EA 6 HOH 150 450 1128 HOH HOH B . 
EA 6 HOH 151 451 1125 HOH HOH B . 
EA 6 HOH 152 452 1169 HOH HOH B . 
EA 6 HOH 153 453 578  HOH HOH B . 
EA 6 HOH 154 454 644  HOH HOH B . 
EA 6 HOH 155 455 824  HOH HOH B . 
EA 6 HOH 156 456 1189 HOH HOH B . 
EA 6 HOH 157 457 640  HOH HOH B . 
EA 6 HOH 158 458 244  HOH HOH B . 
EA 6 HOH 159 459 714  HOH HOH B . 
EA 6 HOH 160 460 698  HOH HOH B . 
EA 6 HOH 161 461 1185 HOH HOH B . 
EA 6 HOH 162 462 1186 HOH HOH B . 
EA 6 HOH 163 463 1197 HOH HOH B . 
EA 6 HOH 164 464 471  HOH HOH B . 
EA 6 HOH 165 465 776  HOH HOH B . 
EA 6 HOH 166 466 753  HOH HOH B . 
EA 6 HOH 167 467 525  HOH HOH B . 
EA 6 HOH 168 468 1016 HOH HOH B . 
EA 6 HOH 169 469 735  HOH HOH B . 
EA 6 HOH 170 470 981  HOH HOH B . 
EA 6 HOH 171 471 831  HOH HOH B . 
FA 6 HOH 1   301 542  HOH HOH D . 
FA 6 HOH 2   302 611  HOH HOH D . 
FA 6 HOH 3   303 190  HOH HOH D . 
FA 6 HOH 4   304 253  HOH HOH D . 
FA 6 HOH 5   305 933  HOH HOH D . 
FA 6 HOH 6   306 702  HOH HOH D . 
FA 6 HOH 7   307 645  HOH HOH D . 
FA 6 HOH 8   308 979  HOH HOH D . 
FA 6 HOH 9   309 36   HOH HOH D . 
FA 6 HOH 10  310 439  HOH HOH D . 
FA 6 HOH 11  311 425  HOH HOH D . 
FA 6 HOH 12  312 1065 HOH HOH D . 
FA 6 HOH 13  313 908  HOH HOH D . 
FA 6 HOH 14  314 20   HOH HOH D . 
FA 6 HOH 15  315 1139 HOH HOH D . 
FA 6 HOH 16  316 63   HOH HOH D . 
FA 6 HOH 17  317 961  HOH HOH D . 
FA 6 HOH 18  318 785  HOH HOH D . 
FA 6 HOH 19  319 106  HOH HOH D . 
FA 6 HOH 20  320 715  HOH HOH D . 
FA 6 HOH 21  321 350  HOH HOH D . 
FA 6 HOH 22  322 798  HOH HOH D . 
FA 6 HOH 23  323 71   HOH HOH D . 
FA 6 HOH 24  324 162  HOH HOH D . 
FA 6 HOH 25  325 762  HOH HOH D . 
FA 6 HOH 26  326 56   HOH HOH D . 
FA 6 HOH 27  327 659  HOH HOH D . 
FA 6 HOH 28  328 434  HOH HOH D . 
FA 6 HOH 29  329 864  HOH HOH D . 
FA 6 HOH 30  330 230  HOH HOH D . 
FA 6 HOH 31  331 1102 HOH HOH D . 
FA 6 HOH 32  332 911  HOH HOH D . 
FA 6 HOH 33  333 906  HOH HOH D . 
FA 6 HOH 34  334 21   HOH HOH D . 
FA 6 HOH 35  335 491  HOH HOH D . 
FA 6 HOH 36  336 290  HOH HOH D . 
FA 6 HOH 37  337 301  HOH HOH D . 
FA 6 HOH 38  338 293  HOH HOH D . 
FA 6 HOH 39  339 626  HOH HOH D . 
FA 6 HOH 40  340 540  HOH HOH D . 
FA 6 HOH 41  341 668  HOH HOH D . 
FA 6 HOH 42  342 894  HOH HOH D . 
FA 6 HOH 43  343 136  HOH HOH D . 
FA 6 HOH 44  344 891  HOH HOH D . 
FA 6 HOH 45  345 361  HOH HOH D . 
FA 6 HOH 46  346 585  HOH HOH D . 
FA 6 HOH 47  347 123  HOH HOH D . 
FA 6 HOH 48  348 1030 HOH HOH D . 
FA 6 HOH 49  349 763  HOH HOH D . 
FA 6 HOH 50  350 877  HOH HOH D . 
FA 6 HOH 51  351 1063 HOH HOH D . 
FA 6 HOH 52  352 1081 HOH HOH D . 
FA 6 HOH 53  353 448  HOH HOH D . 
FA 6 HOH 54  354 170  HOH HOH D . 
FA 6 HOH 55  355 533  HOH HOH D . 
FA 6 HOH 56  356 243  HOH HOH D . 
FA 6 HOH 57  357 333  HOH HOH D . 
FA 6 HOH 58  358 53   HOH HOH D . 
FA 6 HOH 59  359 772  HOH HOH D . 
FA 6 HOH 60  360 231  HOH HOH D . 
FA 6 HOH 61  361 319  HOH HOH D . 
FA 6 HOH 62  362 289  HOH HOH D . 
FA 6 HOH 63  363 203  HOH HOH D . 
FA 6 HOH 64  364 569  HOH HOH D . 
FA 6 HOH 65  365 412  HOH HOH D . 
FA 6 HOH 66  366 1204 HOH HOH D . 
FA 6 HOH 67  367 783  HOH HOH D . 
FA 6 HOH 68  368 46   HOH HOH D . 
FA 6 HOH 69  369 568  HOH HOH D . 
FA 6 HOH 70  370 325  HOH HOH D . 
FA 6 HOH 71  371 1158 HOH HOH D . 
FA 6 HOH 72  372 586  HOH HOH D . 
FA 6 HOH 73  373 366  HOH HOH D . 
FA 6 HOH 74  374 854  HOH HOH D . 
FA 6 HOH 75  375 307  HOH HOH D . 
FA 6 HOH 76  376 768  HOH HOH D . 
FA 6 HOH 77  377 770  HOH HOH D . 
FA 6 HOH 78  378 551  HOH HOH D . 
FA 6 HOH 79  379 178  HOH HOH D . 
FA 6 HOH 80  380 559  HOH HOH D . 
FA 6 HOH 81  381 362  HOH HOH D . 
FA 6 HOH 82  382 374  HOH HOH D . 
FA 6 HOH 83  383 665  HOH HOH D . 
FA 6 HOH 84  384 786  HOH HOH D . 
FA 6 HOH 85  385 357  HOH HOH D . 
FA 6 HOH 86  386 321  HOH HOH D . 
FA 6 HOH 87  387 257  HOH HOH D . 
FA 6 HOH 88  388 407  HOH HOH D . 
FA 6 HOH 89  389 345  HOH HOH D . 
FA 6 HOH 90  390 297  HOH HOH D . 
FA 6 HOH 91  391 771  HOH HOH D . 
FA 6 HOH 92  392 1005 HOH HOH D . 
FA 6 HOH 93  393 761  HOH HOH D . 
FA 6 HOH 94  394 1156 HOH HOH D . 
FA 6 HOH 95  395 1153 HOH HOH D . 
FA 6 HOH 96  396 872  HOH HOH D . 
FA 6 HOH 97  397 264  HOH HOH D . 
FA 6 HOH 98  398 1206 HOH HOH D . 
FA 6 HOH 99  399 1104 HOH HOH D . 
FA 6 HOH 100 400 1159 HOH HOH D . 
FA 6 HOH 101 401 1181 HOH HOH D . 
FA 6 HOH 102 402 792  HOH HOH D . 
FA 6 HOH 103 403 790  HOH HOH D . 
FA 6 HOH 104 404 909  HOH HOH D . 
FA 6 HOH 105 405 1042 HOH HOH D . 
FA 6 HOH 106 406 963  HOH HOH D . 
FA 6 HOH 107 407 740  HOH HOH D . 
FA 6 HOH 108 408 918  HOH HOH D . 
FA 6 HOH 109 409 791  HOH HOH D . 
FA 6 HOH 110 410 925  HOH HOH D . 
FA 6 HOH 111 411 411  HOH HOH D . 
FA 6 HOH 112 412 331  HOH HOH D . 
FA 6 HOH 113 413 855  HOH HOH D . 
FA 6 HOH 114 414 853  HOH HOH D . 
FA 6 HOH 115 415 1176 HOH HOH D . 
FA 6 HOH 116 416 515  HOH HOH D . 
GA 6 HOH 1   301 600  HOH HOH C . 
GA 6 HOH 2   302 647  HOH HOH C . 
GA 6 HOH 3   303 548  HOH HOH C . 
GA 6 HOH 4   304 354  HOH HOH C . 
GA 6 HOH 5   305 935  HOH HOH C . 
GA 6 HOH 6   306 1013 HOH HOH C . 
GA 6 HOH 7   307 780  HOH HOH C . 
GA 6 HOH 8   308 73   HOH HOH C . 
GA 6 HOH 9   309 1087 HOH HOH C . 
GA 6 HOH 10  310 1130 HOH HOH C . 
GA 6 HOH 11  311 1205 HOH HOH C . 
GA 6 HOH 12  312 338  HOH HOH C . 
GA 6 HOH 13  313 267  HOH HOH C . 
GA 6 HOH 14  314 164  HOH HOH C . 
GA 6 HOH 15  315 902  HOH HOH C . 
GA 6 HOH 16  316 1134 HOH HOH C . 
GA 6 HOH 17  317 778  HOH HOH C . 
GA 6 HOH 18  318 887  HOH HOH C . 
GA 6 HOH 19  319 550  HOH HOH C . 
GA 6 HOH 20  320 829  HOH HOH C . 
GA 6 HOH 21  321 774  HOH HOH C . 
GA 6 HOH 22  322 3    HOH HOH C . 
GA 6 HOH 23  323 17   HOH HOH C . 
GA 6 HOH 24  324 781  HOH HOH C . 
GA 6 HOH 25  325 112  HOH HOH C . 
GA 6 HOH 26  326 288  HOH HOH C . 
GA 6 HOH 27  327 834  HOH HOH C . 
GA 6 HOH 28  328 172  HOH HOH C . 
GA 6 HOH 29  329 1048 HOH HOH C . 
GA 6 HOH 30  330 7    HOH HOH C . 
GA 6 HOH 31  331 387  HOH HOH C . 
GA 6 HOH 32  332 18   HOH HOH C . 
GA 6 HOH 33  333 711  HOH HOH C . 
GA 6 HOH 34  334 57   HOH HOH C . 
GA 6 HOH 35  335 147  HOH HOH C . 
GA 6 HOH 36  336 205  HOH HOH C . 
GA 6 HOH 37  337 788  HOH HOH C . 
GA 6 HOH 38  338 595  HOH HOH C . 
GA 6 HOH 39  339 931  HOH HOH C . 
GA 6 HOH 40  340 221  HOH HOH C . 
GA 6 HOH 41  341 876  HOH HOH C . 
GA 6 HOH 42  342 37   HOH HOH C . 
GA 6 HOH 43  343 105  HOH HOH C . 
GA 6 HOH 44  344 340  HOH HOH C . 
GA 6 HOH 45  345 65   HOH HOH C . 
GA 6 HOH 46  346 79   HOH HOH C . 
GA 6 HOH 47  347 1208 HOH HOH C . 
GA 6 HOH 48  348 101  HOH HOH C . 
GA 6 HOH 49  349 527  HOH HOH C . 
GA 6 HOH 50  350 962  HOH HOH C . 
GA 6 HOH 51  351 40   HOH HOH C . 
GA 6 HOH 52  352 238  HOH HOH C . 
GA 6 HOH 53  353 226  HOH HOH C . 
GA 6 HOH 54  354 674  HOH HOH C . 
GA 6 HOH 55  355 779  HOH HOH C . 
GA 6 HOH 56  356 490  HOH HOH C . 
GA 6 HOH 57  357 129  HOH HOH C . 
GA 6 HOH 58  358 88   HOH HOH C . 
GA 6 HOH 59  359 508  HOH HOH C . 
GA 6 HOH 60  360 960  HOH HOH C . 
GA 6 HOH 61  361 165  HOH HOH C . 
GA 6 HOH 62  362 370  HOH HOH C . 
GA 6 HOH 63  363 154  HOH HOH C . 
GA 6 HOH 64  364 677  HOH HOH C . 
GA 6 HOH 65  365 1099 HOH HOH C . 
GA 6 HOH 66  366 617  HOH HOH C . 
GA 6 HOH 67  367 224  HOH HOH C . 
GA 6 HOH 68  368 628  HOH HOH C . 
GA 6 HOH 69  369 43   HOH HOH C . 
GA 6 HOH 70  370 124  HOH HOH C . 
GA 6 HOH 71  371 87   HOH HOH C . 
GA 6 HOH 72  372 26   HOH HOH C . 
GA 6 HOH 73  373 161  HOH HOH C . 
GA 6 HOH 74  374 870  HOH HOH C . 
GA 6 HOH 75  375 274  HOH HOH C . 
GA 6 HOH 76  376 939  HOH HOH C . 
GA 6 HOH 77  377 982  HOH HOH C . 
GA 6 HOH 78  378 599  HOH HOH C . 
GA 6 HOH 79  379 782  HOH HOH C . 
GA 6 HOH 80  380 1203 HOH HOH C . 
GA 6 HOH 81  381 2    HOH HOH C . 
GA 6 HOH 82  382 554  HOH HOH C . 
GA 6 HOH 83  383 41   HOH HOH C . 
GA 6 HOH 84  384 932  HOH HOH C . 
GA 6 HOH 85  385 119  HOH HOH C . 
GA 6 HOH 86  386 306  HOH HOH C . 
GA 6 HOH 87  387 942  HOH HOH C . 
GA 6 HOH 88  388 398  HOH HOH C . 
GA 6 HOH 89  389 758  HOH HOH C . 
GA 6 HOH 90  390 517  HOH HOH C . 
GA 6 HOH 91  391 424  HOH HOH C . 
GA 6 HOH 92  392 452  HOH HOH C . 
GA 6 HOH 93  393 400  HOH HOH C . 
GA 6 HOH 94  394 913  HOH HOH C . 
GA 6 HOH 95  395 42   HOH HOH C . 
GA 6 HOH 96  396 473  HOH HOH C . 
GA 6 HOH 97  397 1132 HOH HOH C . 
GA 6 HOH 98  398 209  HOH HOH C . 
GA 6 HOH 99  399 1133 HOH HOH C . 
GA 6 HOH 100 400 377  HOH HOH C . 
GA 6 HOH 101 401 539  HOH HOH C . 
GA 6 HOH 102 402 110  HOH HOH C . 
GA 6 HOH 103 403 1083 HOH HOH C . 
GA 6 HOH 104 404 621  HOH HOH C . 
GA 6 HOH 105 405 934  HOH HOH C . 
GA 6 HOH 106 406 708  HOH HOH C . 
GA 6 HOH 107 407 227  HOH HOH C . 
GA 6 HOH 108 408 266  HOH HOH C . 
GA 6 HOH 109 409 759  HOH HOH C . 
GA 6 HOH 110 410 709  HOH HOH C . 
GA 6 HOH 111 411 393  HOH HOH C . 
GA 6 HOH 112 412 394  HOH HOH C . 
GA 6 HOH 113 413 794  HOH HOH C . 
GA 6 HOH 114 414 773  HOH HOH C . 
GA 6 HOH 115 415 463  HOH HOH C . 
GA 6 HOH 116 416 1207 HOH HOH C . 
GA 6 HOH 117 417 869  HOH HOH C . 
GA 6 HOH 118 418 538  HOH HOH C . 
GA 6 HOH 119 419 418  HOH HOH C . 
GA 6 HOH 120 420 656  HOH HOH C . 
GA 6 HOH 121 421 1173 HOH HOH C . 
GA 6 HOH 122 422 623  HOH HOH C . 
GA 6 HOH 123 423 1015 HOH HOH C . 
GA 6 HOH 124 424 643  HOH HOH C . 
GA 6 HOH 125 425 1091 HOH HOH C . 
GA 6 HOH 126 426 1112 HOH HOH C . 
GA 6 HOH 127 427 871  HOH HOH C . 
GA 6 HOH 128 428 787  HOH HOH C . 
GA 6 HOH 129 429 1026 HOH HOH C . 
GA 6 HOH 130 430 1044 HOH HOH C . 
GA 6 HOH 131 431 466  HOH HOH C . 
GA 6 HOH 132 432 1126 HOH HOH C . 
GA 6 HOH 133 433 128  HOH HOH C . 
GA 6 HOH 134 434 1170 HOH HOH C . 
GA 6 HOH 135 435 795  HOH HOH C . 
GA 6 HOH 136 436 796  HOH HOH C . 
GA 6 HOH 137 437 789  HOH HOH C . 
GA 6 HOH 138 438 1178 HOH HOH C . 
GA 6 HOH 139 439 514  HOH HOH C . 
GA 6 HOH 140 440 1146 HOH HOH C . 
GA 6 HOH 141 441 873  HOH HOH C . 
GA 6 HOH 142 442 359  HOH HOH C . 
GA 6 HOH 143 443 1180 HOH HOH C . 
GA 6 HOH 144 444 1188 HOH HOH C . 
GA 6 HOH 145 445 1052 HOH HOH C . 
GA 6 HOH 146 446 754  HOH HOH C . 
GA 6 HOH 147 447 355  HOH HOH C . 
GA 6 HOH 148 448 830  HOH HOH C . 
GA 6 HOH 149 449 700  HOH HOH C . 
GA 6 HOH 150 450 1124 HOH HOH C . 
GA 6 HOH 151 451 612  HOH HOH C . 
GA 6 HOH 152 452 728  HOH HOH C . 
GA 6 HOH 153 453 233  HOH HOH C . 
GA 6 HOH 154 454 760  HOH HOH C . 
GA 6 HOH 155 455 737  HOH HOH C . 
GA 6 HOH 156 456 560  HOH HOH C . 
GA 6 HOH 157 457 342  HOH HOH C . 
GA 6 HOH 158 458 733  HOH HOH C . 
GA 6 HOH 159 459 1105 HOH HOH C . 
GA 6 HOH 160 460 528  HOH HOH C . 
GA 6 HOH 161 461 793  HOH HOH C . 
GA 6 HOH 162 462 769  HOH HOH C . 
GA 6 HOH 163 463 512  HOH HOH C . 
HA 6 HOH 1   301 879  HOH HOH H . 
HA 6 HOH 2   302 1093 HOH HOH H . 
HA 6 HOH 3   303 1079 HOH HOH H . 
HA 6 HOH 4   304 276  HOH HOH H . 
HA 6 HOH 5   305 19   HOH HOH H . 
HA 6 HOH 6   306 966  HOH HOH H . 
HA 6 HOH 7   307 294  HOH HOH H . 
HA 6 HOH 8   308 597  HOH HOH H . 
HA 6 HOH 9   309 1045 HOH HOH H . 
HA 6 HOH 10  310 699  HOH HOH H . 
HA 6 HOH 11  311 865  HOH HOH H . 
HA 6 HOH 12  312 14   HOH HOH H . 
HA 6 HOH 13  313 78   HOH HOH H . 
HA 6 HOH 14  314 967  HOH HOH H . 
HA 6 HOH 15  315 1    HOH HOH H . 
HA 6 HOH 16  316 11   HOH HOH H . 
HA 6 HOH 17  317 603  HOH HOH H . 
HA 6 HOH 18  318 177  HOH HOH H . 
HA 6 HOH 19  319 211  HOH HOH H . 
HA 6 HOH 20  320 404  HOH HOH H . 
HA 6 HOH 21  321 33   HOH HOH H . 
HA 6 HOH 22  322 800  HOH HOH H . 
HA 6 HOH 23  323 570  HOH HOH H . 
HA 6 HOH 24  324 107  HOH HOH H . 
HA 6 HOH 25  325 281  HOH HOH H . 
HA 6 HOH 26  326 173  HOH HOH H . 
HA 6 HOH 27  327 89   HOH HOH H . 
HA 6 HOH 28  328 85   HOH HOH H . 
HA 6 HOH 29  329 470  HOH HOH H . 
HA 6 HOH 30  330 880  HOH HOH H . 
HA 6 HOH 31  331 31   HOH HOH H . 
HA 6 HOH 32  332 277  HOH HOH H . 
HA 6 HOH 33  333 258  HOH HOH H . 
HA 6 HOH 34  334 511  HOH HOH H . 
HA 6 HOH 35  335 143  HOH HOH H . 
HA 6 HOH 36  336 99   HOH HOH H . 
HA 6 HOH 37  337 152  HOH HOH H . 
HA 6 HOH 38  338 610  HOH HOH H . 
HA 6 HOH 39  339 76   HOH HOH H . 
HA 6 HOH 40  340 183  HOH HOH H . 
HA 6 HOH 41  341 438  HOH HOH H . 
HA 6 HOH 42  342 157  HOH HOH H . 
HA 6 HOH 43  343 680  HOH HOH H . 
HA 6 HOH 44  344 910  HOH HOH H . 
HA 6 HOH 45  345 572  HOH HOH H . 
HA 6 HOH 46  346 1014 HOH HOH H . 
HA 6 HOH 47  347 547  HOH HOH H . 
HA 6 HOH 48  348 261  HOH HOH H . 
HA 6 HOH 49  349 405  HOH HOH H . 
HA 6 HOH 50  350 1082 HOH HOH H . 
HA 6 HOH 51  351 949  HOH HOH H . 
HA 6 HOH 52  352 121  HOH HOH H . 
HA 6 HOH 53  353 413  HOH HOH H . 
HA 6 HOH 54  354 988  HOH HOH H . 
HA 6 HOH 55  355 997  HOH HOH H . 
HA 6 HOH 56  356 649  HOH HOH H . 
HA 6 HOH 57  357 194  HOH HOH H . 
HA 6 HOH 58  358 884  HOH HOH H . 
HA 6 HOH 59  359 693  HOH HOH H . 
HA 6 HOH 60  360 314  HOH HOH H . 
HA 6 HOH 61  361 895  HOH HOH H . 
HA 6 HOH 62  362 184  HOH HOH H . 
HA 6 HOH 63  363 577  HOH HOH H . 
HA 6 HOH 64  364 379  HOH HOH H . 
HA 6 HOH 65  365 943  HOH HOH H . 
HA 6 HOH 66  366 1150 HOH HOH H . 
HA 6 HOH 67  367 1147 HOH HOH H . 
HA 6 HOH 68  368 957  HOH HOH H . 
HA 6 HOH 69  369 169  HOH HOH H . 
HA 6 HOH 70  370 336  HOH HOH H . 
HA 6 HOH 71  371 148  HOH HOH H . 
HA 6 HOH 72  372 383  HOH HOH H . 
HA 6 HOH 73  373 363  HOH HOH H . 
HA 6 HOH 74  374 193  HOH HOH H . 
HA 6 HOH 75  375 1037 HOH HOH H . 
HA 6 HOH 76  376 998  HOH HOH H . 
HA 6 HOH 77  377 1019 HOH HOH H . 
HA 6 HOH 78  378 1141 HOH HOH H . 
HA 6 HOH 79  379 509  HOH HOH H . 
HA 6 HOH 80  380 662  HOH HOH H . 
HA 6 HOH 81  381 435  HOH HOH H . 
HA 6 HOH 82  382 1085 HOH HOH H . 
HA 6 HOH 83  383 846  HOH HOH H . 
HA 6 HOH 84  384 627  HOH HOH H . 
HA 6 HOH 85  385 694  HOH HOH H . 
HA 6 HOH 86  386 543  HOH HOH H . 
HA 6 HOH 87  387 443  HOH HOH H . 
HA 6 HOH 88  388 716  HOH HOH H . 
HA 6 HOH 89  389 344  HOH HOH H . 
HA 6 HOH 90  390 1108 HOH HOH H . 
HA 6 HOH 91  391 453  HOH HOH H . 
HA 6 HOH 92  392 743  HOH HOH H . 
HA 6 HOH 93  393 1001 HOH HOH H . 
HA 6 HOH 94  394 1135 HOH HOH H . 
HA 6 HOH 95  395 1022 HOH HOH H . 
HA 6 HOH 96  396 941  HOH HOH H . 
HA 6 HOH 97  397 1075 HOH HOH H . 
HA 6 HOH 98  398 1164 HOH HOH H . 
HA 6 HOH 99  399 732  HOH HOH H . 
HA 6 HOH 100 400 1121 HOH HOH H . 
HA 6 HOH 101 401 423  HOH HOH H . 
HA 6 HOH 102 402 730  HOH HOH H . 
HA 6 HOH 103 403 545  HOH HOH H . 
HA 6 HOH 104 404 196  HOH HOH H . 
HA 6 HOH 105 405 999  HOH HOH H . 
HA 6 HOH 106 406 825  HOH HOH H . 
HA 6 HOH 107 407 488  HOH HOH H . 
HA 6 HOH 108 408 679  HOH HOH H . 
HA 6 HOH 109 409 1088 HOH HOH H . 
HA 6 HOH 110 410 1162 HOH HOH H . 
HA 6 HOH 111 411 826  HOH HOH H . 
IA 6 HOH 1   301 80   HOH HOH E . 
IA 6 HOH 2   302 445  HOH HOH E . 
IA 6 HOH 3   303 428  HOH HOH E . 
IA 6 HOH 4   304 984  HOH HOH E . 
IA 6 HOH 5   305 229  HOH HOH E . 
IA 6 HOH 6   306 153  HOH HOH E . 
IA 6 HOH 7   307 349  HOH HOH E . 
IA 6 HOH 8   308 313  HOH HOH E . 
IA 6 HOH 9   309 406  HOH HOH E . 
IA 6 HOH 10  310 985  HOH HOH E . 
IA 6 HOH 11  311 219  HOH HOH E . 
IA 6 HOH 12  312 672  HOH HOH E . 
IA 6 HOH 13  313 316  HOH HOH E . 
IA 6 HOH 14  314 9    HOH HOH E . 
IA 6 HOH 15  315 69   HOH HOH E . 
IA 6 HOH 16  316 127  HOH HOH E . 
IA 6 HOH 17  317 990  HOH HOH E . 
IA 6 HOH 18  318 430  HOH HOH E . 
IA 6 HOH 19  319 885  HOH HOH E . 
IA 6 HOH 20  320 125  HOH HOH E . 
IA 6 HOH 21  321 66   HOH HOH E . 
IA 6 HOH 22  322 446  HOH HOH E . 
IA 6 HOH 23  323 29   HOH HOH E . 
IA 6 HOH 24  324 973  HOH HOH E . 
IA 6 HOH 25  325 396  HOH HOH E . 
IA 6 HOH 26  326 255  HOH HOH E . 
IA 6 HOH 27  327 207  HOH HOH E . 
IA 6 HOH 28  328 912  HOH HOH E . 
IA 6 HOH 29  329 339  HOH HOH E . 
IA 6 HOH 30  330 146  HOH HOH E . 
IA 6 HOH 31  331 96   HOH HOH E . 
IA 6 HOH 32  332 28   HOH HOH E . 
IA 6 HOH 33  333 1149 HOH HOH E . 
IA 6 HOH 34  334 695  HOH HOH E . 
IA 6 HOH 35  335 955  HOH HOH E . 
IA 6 HOH 36  336 1034 HOH HOH E . 
IA 6 HOH 37  337 725  HOH HOH E . 
IA 6 HOH 38  338 160  HOH HOH E . 
IA 6 HOH 39  339 875  HOH HOH E . 
IA 6 HOH 40  340 122  HOH HOH E . 
IA 6 HOH 41  341 322  HOH HOH E . 
IA 6 HOH 42  342 38   HOH HOH E . 
IA 6 HOH 43  343 1143 HOH HOH E . 
IA 6 HOH 44  344 593  HOH HOH E . 
IA 6 HOH 45  345 311  HOH HOH E . 
IA 6 HOH 46  346 275  HOH HOH E . 
IA 6 HOH 47  347 208  HOH HOH E . 
IA 6 HOH 48  348 134  HOH HOH E . 
IA 6 HOH 49  349 97   HOH HOH E . 
IA 6 HOH 50  350 564  HOH HOH E . 
IA 6 HOH 51  351 450  HOH HOH E . 
IA 6 HOH 52  352 214  HOH HOH E . 
IA 6 HOH 53  353 77   HOH HOH E . 
IA 6 HOH 54  354 571  HOH HOH E . 
IA 6 HOH 55  355 1076 HOH HOH E . 
IA 6 HOH 56  356 584  HOH HOH E . 
IA 6 HOH 57  357 197  HOH HOH E . 
IA 6 HOH 58  358 51   HOH HOH E . 
IA 6 HOH 59  359 62   HOH HOH E . 
IA 6 HOH 60  360 189  HOH HOH E . 
IA 6 HOH 61  361 30   HOH HOH E . 
IA 6 HOH 62  362 635  HOH HOH E . 
IA 6 HOH 63  363 833  HOH HOH E . 
IA 6 HOH 64  364 1127 HOH HOH E . 
IA 6 HOH 65  365 485  HOH HOH E . 
IA 6 HOH 66  366 94   HOH HOH E . 
IA 6 HOH 67  367 1039 HOH HOH E . 
IA 6 HOH 68  368 536  HOH HOH E . 
IA 6 HOH 69  369 117  HOH HOH E . 
IA 6 HOH 70  370 329  HOH HOH E . 
IA 6 HOH 71  371 102  HOH HOH E . 
IA 6 HOH 72  372 503  HOH HOH E . 
IA 6 HOH 73  373 131  HOH HOH E . 
IA 6 HOH 74  374 978  HOH HOH E . 
IA 6 HOH 75  375 135  HOH HOH E . 
IA 6 HOH 76  376 171  HOH HOH E . 
IA 6 HOH 77  377 953  HOH HOH E . 
IA 6 HOH 78  378 881  HOH HOH E . 
IA 6 HOH 79  379 144  HOH HOH E . 
IA 6 HOH 80  380 1107 HOH HOH E . 
IA 6 HOH 81  381 408  HOH HOH E . 
IA 6 HOH 82  382 460  HOH HOH E . 
IA 6 HOH 83  383 624  HOH HOH E . 
IA 6 HOH 84  384 324  HOH HOH E . 
IA 6 HOH 85  385 380  HOH HOH E . 
IA 6 HOH 86  386 784  HOH HOH E . 
IA 6 HOH 87  387 401  HOH HOH E . 
IA 6 HOH 88  388 493  HOH HOH E . 
IA 6 HOH 89  389 479  HOH HOH E . 
IA 6 HOH 90  390 6    HOH HOH E . 
IA 6 HOH 91  391 232  HOH HOH E . 
IA 6 HOH 92  392 260  HOH HOH E . 
IA 6 HOH 93  393 420  HOH HOH E . 
IA 6 HOH 94  394 236  HOH HOH E . 
IA 6 HOH 95  395 505  HOH HOH E . 
IA 6 HOH 96  396 100  HOH HOH E . 
IA 6 HOH 97  397 220  HOH HOH E . 
IA 6 HOH 98  398 1058 HOH HOH E . 
IA 6 HOH 99  399 840  HOH HOH E . 
IA 6 HOH 100 400 930  HOH HOH E . 
IA 6 HOH 101 401 1179 HOH HOH E . 
IA 6 HOH 102 402 622  HOH HOH E . 
IA 6 HOH 103 403 926  HOH HOH E . 
IA 6 HOH 104 404 922  HOH HOH E . 
IA 6 HOH 105 405 15   HOH HOH E . 
IA 6 HOH 106 406 367  HOH HOH E . 
IA 6 HOH 107 407 924  HOH HOH E . 
IA 6 HOH 108 408 838  HOH HOH E . 
IA 6 HOH 109 409 494  HOH HOH E . 
IA 6 HOH 110 410 498  HOH HOH E . 
IA 6 HOH 111 411 465  HOH HOH E . 
IA 6 HOH 112 412 10   HOH HOH E . 
IA 6 HOH 113 413 604  HOH HOH E . 
IA 6 HOH 114 414 475  HOH HOH E . 
IA 6 HOH 115 415 959  HOH HOH E . 
IA 6 HOH 116 416 256  HOH HOH E . 
IA 6 HOH 117 417 589  HOH HOH E . 
IA 6 HOH 118 418 1038 HOH HOH E . 
IA 6 HOH 119 419 469  HOH HOH E . 
IA 6 HOH 120 420 835  HOH HOH E . 
IA 6 HOH 121 421 591  HOH HOH E . 
IA 6 HOH 122 422 1094 HOH HOH E . 
IA 6 HOH 123 423 888  HOH HOH E . 
IA 6 HOH 124 424 495  HOH HOH E . 
IA 6 HOH 125 425 168  HOH HOH E . 
IA 6 HOH 126 426 736  HOH HOH E . 
IA 6 HOH 127 427 451  HOH HOH E . 
IA 6 HOH 128 428 1041 HOH HOH E . 
IA 6 HOH 129 429 296  HOH HOH E . 
IA 6 HOH 130 430 839  HOH HOH E . 
IA 6 HOH 131 431 836  HOH HOH E . 
IA 6 HOH 132 432 1144 HOH HOH E . 
IA 6 HOH 133 433 802  HOH HOH E . 
IA 6 HOH 134 434 832  HOH HOH E . 
IA 6 HOH 135 435 837  HOH HOH E . 
IA 6 HOH 136 436 1118 HOH HOH E . 
IA 6 HOH 137 437 487  HOH HOH E . 
IA 6 HOH 138 438 983  HOH HOH E . 
IA 6 HOH 139 439 1032 HOH HOH E . 
IA 6 HOH 140 440 437  HOH HOH E . 
IA 6 HOH 141 441 506  HOH HOH E . 
IA 6 HOH 142 442 841  HOH HOH E . 
IA 6 HOH 143 443 1068 HOH HOH E . 
IA 6 HOH 144 444 402  HOH HOH E . 
IA 6 HOH 145 445 951  HOH HOH E . 
IA 6 HOH 146 446 320  HOH HOH E . 
IA 6 HOH 147 447 1117 HOH HOH E . 
IA 6 HOH 148 448 1165 HOH HOH E . 
IA 6 HOH 149 449 482  HOH HOH E . 
IA 6 HOH 150 450 348  HOH HOH E . 
IA 6 HOH 151 451 1097 HOH HOH E . 
IA 6 HOH 152 452 801  HOH HOH E . 
IA 6 HOH 153 453 907  HOH HOH E . 
IA 6 HOH 154 454 620  HOH HOH E . 
IA 6 HOH 155 455 630  HOH HOH E . 
IA 6 HOH 156 456 823  HOH HOH E . 
IA 6 HOH 157 457 1145 HOH HOH E . 
IA 6 HOH 158 458 842  HOH HOH E . 
IA 6 HOH 159 459 731  HOH HOH E . 
IA 6 HOH 160 460 1114 HOH HOH E . 
JA 6 HOH 1   301 1137 HOH HOH F . 
JA 6 HOH 2   302 441  HOH HOH F . 
JA 6 HOH 3   303 1152 HOH HOH F . 
JA 6 HOH 4   304 614  HOH HOH F . 
JA 6 HOH 5   305 1195 HOH HOH F . 
JA 6 HOH 6   306 1092 HOH HOH F . 
JA 6 HOH 7   307 744  HOH HOH F . 
JA 6 HOH 8   308 1196 HOH HOH F . 
JA 6 HOH 9   309 843  HOH HOH F . 
JA 6 HOH 10  310 844  HOH HOH F . 
JA 6 HOH 11  311 634  HOH HOH F . 
JA 6 HOH 12  312 343  HOH HOH F . 
JA 6 HOH 13  313 1012 HOH HOH F . 
JA 6 HOH 14  314 654  HOH HOH F . 
JA 6 HOH 15  315 1043 HOH HOH F . 
JA 6 HOH 16  316 1119 HOH HOH F . 
JA 6 HOH 17  317 945  HOH HOH F . 
JA 6 HOH 18  318 251  HOH HOH F . 
JA 6 HOH 19  319 673  HOH HOH F . 
JA 6 HOH 20  320 352  HOH HOH F . 
JA 6 HOH 21  321 245  HOH HOH F . 
JA 6 HOH 22  322 140  HOH HOH F . 
JA 6 HOH 23  323 964  HOH HOH F . 
JA 6 HOH 24  324 353  HOH HOH F . 
JA 6 HOH 25  325 937  HOH HOH F . 
JA 6 HOH 26  326 1062 HOH HOH F . 
JA 6 HOH 27  327 369  HOH HOH F . 
JA 6 HOH 28  328 1120 HOH HOH F . 
JA 6 HOH 29  329 631  HOH HOH F . 
JA 6 HOH 30  330 940  HOH HOH F . 
JA 6 HOH 31  331 956  HOH HOH F . 
JA 6 HOH 32  332 537  HOH HOH F . 
JA 6 HOH 33  333 904  HOH HOH F . 
JA 6 HOH 34  334 1154 HOH HOH F . 
JA 6 HOH 35  335 373  HOH HOH F . 
JA 6 HOH 36  336 799  HOH HOH F . 
JA 6 HOH 37  337 130  HOH HOH F . 
JA 6 HOH 38  338 459  HOH HOH F . 
JA 6 HOH 39  339 658  HOH HOH F . 
JA 6 HOH 40  340 592  HOH HOH F . 
JA 6 HOH 41  341 403  HOH HOH F . 
JA 6 HOH 42  342 472  HOH HOH F . 
JA 6 HOH 43  343 660  HOH HOH F . 
JA 6 HOH 44  344 1148 HOH HOH F . 
JA 6 HOH 45  345 1198 HOH HOH F . 
JA 6 HOH 46  346 455  HOH HOH F . 
JA 6 HOH 47  347 524  HOH HOH F . 
JA 6 HOH 48  348 1020 HOH HOH F . 
JA 6 HOH 49  349 182  HOH HOH F . 
JA 6 HOH 50  350 1192 HOH HOH F . 
JA 6 HOH 51  351 750  HOH HOH F . 
JA 6 HOH 52  352 1070 HOH HOH F . 
JA 6 HOH 53  353 900  HOH HOH F . 
JA 6 HOH 54  354 601  HOH HOH F . 
JA 6 HOH 55  355 382  HOH HOH F . 
JA 6 HOH 56  356 972  HOH HOH F . 
JA 6 HOH 57  357 920  HOH HOH F . 
JA 6 HOH 58  358 1140 HOH HOH F . 
JA 6 HOH 59  359 1017 HOH HOH F . 
JA 6 HOH 60  360 1194 HOH HOH F . 
JA 6 HOH 61  361 1036 HOH HOH F . 
JA 6 HOH 62  362 726  HOH HOH F . 
JA 6 HOH 63  363 1193 HOH HOH F . 
JA 6 HOH 64  364 845  HOH HOH F . 
JA 6 HOH 65  365 969  HOH HOH F . 
JA 6 HOH 66  366 991  HOH HOH F . 
KA 6 HOH 1   301 323  HOH HOH G . 
KA 6 HOH 2   302 987  HOH HOH G . 
KA 6 HOH 3   303 287  HOH HOH G . 
KA 6 HOH 4   304 575  HOH HOH G . 
KA 6 HOH 5   305 371  HOH HOH G . 
KA 6 HOH 6   306 546  HOH HOH G . 
KA 6 HOH 7   307 1078 HOH HOH G . 
KA 6 HOH 8   308 284  HOH HOH G . 
KA 6 HOH 9   309 302  HOH HOH G . 
KA 6 HOH 10  310 52   HOH HOH G . 
KA 6 HOH 11  311 521  HOH HOH G . 
KA 6 HOH 12  312 45   HOH HOH G . 
KA 6 HOH 13  313 489  HOH HOH G . 
KA 6 HOH 14  314 389  HOH HOH G . 
KA 6 HOH 15  315 605  HOH HOH G . 
KA 6 HOH 16  316 47   HOH HOH G . 
KA 6 HOH 17  317 268  HOH HOH G . 
KA 6 HOH 18  318 298  HOH HOH G . 
KA 6 HOH 19  319 309  HOH HOH G . 
KA 6 HOH 20  320 638  HOH HOH G . 
KA 6 HOH 21  321 1027 HOH HOH G . 
KA 6 HOH 22  322 410  HOH HOH G . 
KA 6 HOH 23  323 235  HOH HOH G . 
KA 6 HOH 24  324 518  HOH HOH G . 
KA 6 HOH 25  325 201  HOH HOH G . 
KA 6 HOH 26  326 710  HOH HOH G . 
KA 6 HOH 27  327 16   HOH HOH G . 
KA 6 HOH 28  328 364  HOH HOH G . 
KA 6 HOH 29  329 305  HOH HOH G . 
KA 6 HOH 30  330 385  HOH HOH G . 
KA 6 HOH 31  331 326  HOH HOH G . 
KA 6 HOH 32  332 552  HOH HOH G . 
KA 6 HOH 33  333 602  HOH HOH G . 
KA 6 HOH 34  334 557  HOH HOH G . 
KA 6 HOH 35  335 923  HOH HOH G . 
KA 6 HOH 36  336 563  HOH HOH G . 
KA 6 HOH 37  337 447  HOH HOH G . 
KA 6 HOH 38  338 507  HOH HOH G . 
KA 6 HOH 39  339 327  HOH HOH G . 
KA 6 HOH 40  340 461  HOH HOH G . 
KA 6 HOH 41  341 109  HOH HOH G . 
KA 6 HOH 42  342 286  HOH HOH G . 
KA 6 HOH 43  343 1084 HOH HOH G . 
KA 6 HOH 44  344 464  HOH HOH G . 
KA 6 HOH 45  345 414  HOH HOH G . 
KA 6 HOH 46  346 965  HOH HOH G . 
KA 6 HOH 47  347 893  HOH HOH G . 
KA 6 HOH 48  348 1174 HOH HOH G . 
KA 6 HOH 49  349 946  HOH HOH G . 
KA 6 HOH 50  350 544  HOH HOH G . 
KA 6 HOH 51  351 1151 HOH HOH G . 
KA 6 HOH 52  352 449  HOH HOH G . 
KA 6 HOH 53  353 1031 HOH HOH G . 
KA 6 HOH 54  354 529  HOH HOH G . 
KA 6 HOH 55  355 696  HOH HOH G . 
KA 6 HOH 56  356 944  HOH HOH G . 
KA 6 HOH 57  357 213  HOH HOH G . 
KA 6 HOH 58  358 553  HOH HOH G . 
KA 6 HOH 59  359 573  HOH HOH G . 
KA 6 HOH 60  360 365  HOH HOH G . 
KA 6 HOH 61  361 651  HOH HOH G . 
KA 6 HOH 62  362 588  HOH HOH G . 
KA 6 HOH 63  363 1049 HOH HOH G . 
KA 6 HOH 64  364 766  HOH HOH G . 
KA 6 HOH 65  365 341  HOH HOH G . 
KA 6 HOH 66  366 1157 HOH HOH G . 
KA 6 HOH 67  367 729  HOH HOH G . 
KA 6 HOH 68  368 1000 HOH HOH G . 
KA 6 HOH 69  369 303  HOH HOH G . 
KA 6 HOH 70  370 1101 HOH HOH G . 
KA 6 HOH 71  371 1011 HOH HOH G . 
KA 6 HOH 72  372 828  HOH HOH G . 
KA 6 HOH 73  373 676  HOH HOH G . 
KA 6 HOH 74  374 1004 HOH HOH G . 
KA 6 HOH 75  375 765  HOH HOH G . 
KA 6 HOH 76  376 827  HOH HOH G . 
KA 6 HOH 77  377 822  HOH HOH G . 
KA 6 HOH 78  378 874  HOH HOH G . 
KA 6 HOH 79  379 139  HOH HOH G . 
KA 6 HOH 80  380 992  HOH HOH G . 
KA 6 HOH 81  381 739  HOH HOH G . 
KA 6 HOH 82  382 899  HOH HOH G . 
LA 6 HOH 1   301 318  HOH HOH I . 
LA 6 HOH 2   302 805  HOH HOH I . 
LA 6 HOH 3   303 1110 HOH HOH I . 
LA 6 HOH 4   304 706  HOH HOH I . 
LA 6 HOH 5   305 1183 HOH HOH I . 
LA 6 HOH 6   306 280  HOH HOH I . 
LA 6 HOH 7   307 1051 HOH HOH I . 
LA 6 HOH 8   308 717  HOH HOH I . 
LA 6 HOH 9   309 804  HOH HOH I . 
LA 6 HOH 10  310 391  HOH HOH I . 
LA 6 HOH 11  311 886  HOH HOH I . 
LA 6 HOH 12  312 561  HOH HOH I . 
LA 6 HOH 13  313 919  HOH HOH I . 
LA 6 HOH 14  314 655  HOH HOH I . 
LA 6 HOH 15  315 1106 HOH HOH I . 
LA 6 HOH 16  316 1023 HOH HOH I . 
LA 6 HOH 17  317 1182 HOH HOH I . 
LA 6 HOH 18  318 199  HOH HOH I . 
LA 6 HOH 19  319 462  HOH HOH I . 
LA 6 HOH 20  320 970  HOH HOH I . 
LA 6 HOH 21  321 703  HOH HOH I . 
LA 6 HOH 22  322 216  HOH HOH I . 
LA 6 HOH 23  323 384  HOH HOH I . 
LA 6 HOH 24  324 616  HOH HOH I . 
LA 6 HOH 25  325 163  HOH HOH I . 
LA 6 HOH 26  326 652  HOH HOH I . 
LA 6 HOH 27  327 549  HOH HOH I . 
LA 6 HOH 28  328 113  HOH HOH I . 
LA 6 HOH 29  329 948  HOH HOH I . 
LA 6 HOH 30  330 279  HOH HOH I . 
LA 6 HOH 31  331 478  HOH HOH I . 
LA 6 HOH 32  332 237  HOH HOH I . 
LA 6 HOH 33  333 1064 HOH HOH I . 
LA 6 HOH 34  334 883  HOH HOH I . 
LA 6 HOH 35  335 892  HOH HOH I . 
LA 6 HOH 36  336 308  HOH HOH I . 
LA 6 HOH 37  337 22   HOH HOH I . 
LA 6 HOH 38  338 114  HOH HOH I . 
LA 6 HOH 39  339 1113 HOH HOH I . 
LA 6 HOH 40  340 399  HOH HOH I . 
LA 6 HOH 41  341 299  HOH HOH I . 
LA 6 HOH 42  342 1057 HOH HOH I . 
LA 6 HOH 43  343 247  HOH HOH I . 
LA 6 HOH 44  344 567  HOH HOH I . 
LA 6 HOH 45  345 12   HOH HOH I . 
LA 6 HOH 46  346 215  HOH HOH I . 
LA 6 HOH 47  347 217  HOH HOH I . 
LA 6 HOH 48  348 278  HOH HOH I . 
LA 6 HOH 49  349 347  HOH HOH I . 
LA 6 HOH 50  350 315  HOH HOH I . 
LA 6 HOH 51  351 74   HOH HOH I . 
LA 6 HOH 52  352 440  HOH HOH I . 
LA 6 HOH 53  353 1103 HOH HOH I . 
LA 6 HOH 54  354 142  HOH HOH I . 
LA 6 HOH 55  355 868  HOH HOH I . 
LA 6 HOH 56  356 974  HOH HOH I . 
LA 6 HOH 57  357 1129 HOH HOH I . 
LA 6 HOH 58  358 222  HOH HOH I . 
LA 6 HOH 59  359 228  HOH HOH I . 
LA 6 HOH 60  360 689  HOH HOH I . 
LA 6 HOH 61  361 254  HOH HOH I . 
LA 6 HOH 62  362 137  HOH HOH I . 
LA 6 HOH 63  363 212  HOH HOH I . 
LA 6 HOH 64  364 476  HOH HOH I . 
LA 6 HOH 65  365 1066 HOH HOH I . 
LA 6 HOH 66  366 291  HOH HOH I . 
LA 6 HOH 67  367 718  HOH HOH I . 
LA 6 HOH 68  368 81   HOH HOH I . 
LA 6 HOH 69  369 921  HOH HOH I . 
LA 6 HOH 70  370 317  HOH HOH I . 
LA 6 HOH 71  371 1086 HOH HOH I . 
LA 6 HOH 72  372 691  HOH HOH I . 
LA 6 HOH 73  373 375  HOH HOH I . 
LA 6 HOH 74  374 1155 HOH HOH I . 
LA 6 HOH 75  375 686  HOH HOH I . 
LA 6 HOH 76  376 415  HOH HOH I . 
LA 6 HOH 77  377 903  HOH HOH I . 
LA 6 HOH 78  378 234  HOH HOH I . 
LA 6 HOH 79  379 1054 HOH HOH I . 
LA 6 HOH 80  380 707  HOH HOH I . 
LA 6 HOH 81  381 300  HOH HOH I . 
LA 6 HOH 82  382 442  HOH HOH I . 
LA 6 HOH 83  383 995  HOH HOH I . 
LA 6 HOH 84  384 583  HOH HOH I . 
LA 6 HOH 85  385 1122 HOH HOH I . 
LA 6 HOH 86  386 1109 HOH HOH I . 
LA 6 HOH 87  387 646  HOH HOH I . 
LA 6 HOH 88  388 271  HOH HOH I . 
LA 6 HOH 89  389 416  HOH HOH I . 
LA 6 HOH 90  390 392  HOH HOH I . 
LA 6 HOH 91  391 558  HOH HOH I . 
LA 6 HOH 92  392 650  HOH HOH I . 
LA 6 HOH 93  393 48   HOH HOH I . 
LA 6 HOH 94  394 483  HOH HOH I . 
LA 6 HOH 95  395 1006 HOH HOH I . 
LA 6 HOH 96  396 606  HOH HOH I . 
LA 6 HOH 97  397 574  HOH HOH I . 
LA 6 HOH 98  398 328  HOH HOH I . 
LA 6 HOH 99  399 851  HOH HOH I . 
LA 6 HOH 100 400 661  HOH HOH I . 
LA 6 HOH 101 401 523  HOH HOH I . 
LA 6 HOH 102 402 657  HOH HOH I . 
LA 6 HOH 103 403 541  HOH HOH I . 
LA 6 HOH 104 404 852  HOH HOH I . 
LA 6 HOH 105 405 1056 HOH HOH I . 
LA 6 HOH 106 406 712  HOH HOH I . 
LA 6 HOH 107 407 562  HOH HOH I . 
LA 6 HOH 108 408 1059 HOH HOH I . 
LA 6 HOH 109 409 1167 HOH HOH I . 
LA 6 HOH 110 410 458  HOH HOH I . 
LA 6 HOH 111 411 1046 HOH HOH I . 
LA 6 HOH 112 412 850  HOH HOH I . 
LA 6 HOH 113 413 467  HOH HOH I . 
LA 6 HOH 114 414 500  HOH HOH I . 
LA 6 HOH 115 415 849  HOH HOH I . 
LA 6 HOH 116 416 1171 HOH HOH I . 
LA 6 HOH 117 417 682  HOH HOH I . 
LA 6 HOH 118 418 722  HOH HOH I . 
LA 6 HOH 119 419 252  HOH HOH I . 
LA 6 HOH 120 420 764  HOH HOH I . 
LA 6 HOH 121 421 1007 HOH HOH I . 
LA 6 HOH 122 422 742  HOH HOH I . 
LA 6 HOH 123 423 502  HOH HOH I . 
LA 6 HOH 124 424 1061 HOH HOH I . 
LA 6 HOH 125 425 688  HOH HOH I . 
MA 6 HOH 1   201 477  HOH HOH J . 
MA 6 HOH 2   202 901  HOH HOH J . 
MA 6 HOH 3   203 481  HOH HOH J . 
MA 6 HOH 4   204 1138 HOH HOH J . 
MA 6 HOH 5   205 522  HOH HOH J . 
MA 6 HOH 6   206 648  HOH HOH J . 
MA 6 HOH 7   207 666  HOH HOH J . 
MA 6 HOH 8   208 263  HOH HOH J . 
MA 6 HOH 9   209 684  HOH HOH J . 
MA 6 HOH 10  210 847  HOH HOH J . 
MA 6 HOH 11  211 49   HOH HOH J . 
MA 6 HOH 12  212 58   HOH HOH J . 
MA 6 HOH 13  213 1060 HOH HOH J . 
MA 6 HOH 14  214 882  HOH HOH J . 
MA 6 HOH 15  215 1050 HOH HOH J . 
MA 6 HOH 16  216 67   HOH HOH J . 
MA 6 HOH 17  217 332  HOH HOH J . 
MA 6 HOH 18  218 504  HOH HOH J . 
MA 6 HOH 19  219 803  HOH HOH J . 
MA 6 HOH 20  220 1116 HOH HOH J . 
MA 6 HOH 21  221 356  HOH HOH J . 
MA 6 HOH 22  222 927  HOH HOH J . 
MA 6 HOH 23  223 1131 HOH HOH J . 
MA 6 HOH 24  224 181  HOH HOH J . 
MA 6 HOH 25  225 457  HOH HOH J . 
MA 6 HOH 26  226 890  HOH HOH J . 
MA 6 HOH 27  227 1047 HOH HOH J . 
MA 6 HOH 28  228 132  HOH HOH J . 
MA 6 HOH 29  229 1077 HOH HOH J . 
MA 6 HOH 30  230 724  HOH HOH J . 
MA 6 HOH 31  231 866  HOH HOH J . 
MA 6 HOH 32  232 246  HOH HOH J . 
MA 6 HOH 33  233 360  HOH HOH J . 
MA 6 HOH 34  234 386  HOH HOH J . 
MA 6 HOH 35  235 295  HOH HOH J . 
MA 6 HOH 36  236 166  HOH HOH J . 
MA 6 HOH 37  237 351  HOH HOH J . 
MA 6 HOH 38  238 431  HOH HOH J . 
MA 6 HOH 39  239 719  HOH HOH J . 
MA 6 HOH 40  240 204  HOH HOH J . 
MA 6 HOH 41  241 670  HOH HOH J . 
MA 6 HOH 42  242 1018 HOH HOH J . 
MA 6 HOH 43  243 720  HOH HOH J . 
MA 6 HOH 44  244 149  HOH HOH J . 
MA 6 HOH 45  245 427  HOH HOH J . 
MA 6 HOH 46  246 433  HOH HOH J . 
MA 6 HOH 47  247 615  HOH HOH J . 
MA 6 HOH 48  248 938  HOH HOH J . 
MA 6 HOH 49  249 1067 HOH HOH J . 
MA 6 HOH 50  250 192  HOH HOH J . 
MA 6 HOH 51  251 669  HOH HOH J . 
MA 6 HOH 52  252 692  HOH HOH J . 
MA 6 HOH 53  253 1035 HOH HOH J . 
MA 6 HOH 54  254 625  HOH HOH J . 
MA 6 HOH 55  255 952  HOH HOH J . 
MA 6 HOH 56  256 1098 HOH HOH J . 
MA 6 HOH 57  257 954  HOH HOH J . 
MA 6 HOH 58  258 848  HOH HOH J . 
MA 6 HOH 59  259 619  HOH HOH J . 
MA 6 HOH 60  260 738  HOH HOH J . 
MA 6 HOH 61  261 1003 HOH HOH J . 
MA 6 HOH 62  262 480  HOH HOH J . 
MA 6 HOH 63  263 1095 HOH HOH J . 
MA 6 HOH 64  264 867  HOH HOH J . 
MA 6 HOH 65  265 671  HOH HOH J . 
MA 6 HOH 66  266 526  HOH HOH J . 
MA 6 HOH 67  267 1029 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,Q,DA,EA 
2 1 C,D,R,S,T,U,V,FA,GA     
3 1 E,F,W,X,Y,HA,IA         
4 1 G,H,Z,AA,JA,KA          
5 1 I,J,BA,CA,LA,MA         
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2190  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  14120 ? 
2 'ABSA (A^2)' 1640  ? 
2 MORE         -12   ? 
2 'SSA (A^2)'  14230 ? 
3 'ABSA (A^2)' 1590  ? 
3 MORE         -12   ? 
3 'SSA (A^2)'  13860 ? 
4 'ABSA (A^2)' 1380  ? 
4 MORE         -12   ? 
4 'SSA (A^2)'  13930 ? 
5 'ABSA (A^2)' 1390  ? 
5 MORE         -12   ? 
5 'SSA (A^2)'  12970 ? 
# 
_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_555 110.8 ? 
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_555 111.1 ? 
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_555 127.0 ? 
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_555 104.2 ? 
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 84.1  ? 
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_555 114.8 ? 
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_555 106.2 ? 
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_555 108.3 ? 
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_555 128.1 ? 
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_555 103.0 ? 
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 90.5  ? 
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_555 117.4 ? 
13 ND1 ? C HIS 90  ? D HIS 63 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 ND1 ? C HIS 98  ? D HIS 71 ? 1_555 105.7 ? 
14 ND1 ? C HIS 90  ? D HIS 63 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 ND1 ? C HIS 107 ? D HIS 80 ? 1_555 108.5 ? 
15 ND1 ? C HIS 98  ? D HIS 71 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 ND1 ? C HIS 107 ? D HIS 80 ? 1_555 128.0 ? 
16 ND1 ? C HIS 90  ? D HIS 63 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 OD1 ? C ASP 110 ? D ASP 83 ? 1_555 103.5 ? 
17 ND1 ? C HIS 98  ? D HIS 71 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 OD1 ? C ASP 110 ? D ASP 83 ? 1_555 89.2  ? 
18 ND1 ? C HIS 107 ? D HIS 80 ? 1_555 ZN ? R  ZN . ? D ZN 201 ? 1_555 OD1 ? C ASP 110 ? D ASP 83 ? 1_555 118.5 ? 
19 ND1 ? D HIS 90  ? C HIS 63 ? 1_555 ZN ? U  ZN . ? C ZN 201 ? 1_555 ND1 ? D HIS 98  ? C HIS 71 ? 1_555 108.2 ? 
20 ND1 ? D HIS 90  ? C HIS 63 ? 1_555 ZN ? U  ZN . ? C ZN 201 ? 1_555 ND1 ? D HIS 107 ? C HIS 80 ? 1_555 112.4 ? 
21 ND1 ? D HIS 98  ? C HIS 71 ? 1_555 ZN ? U  ZN . ? C ZN 201 ? 1_555 ND1 ? D HIS 107 ? C HIS 80 ? 1_555 124.5 ? 
22 ND1 ? D HIS 90  ? C HIS 63 ? 1_555 ZN ? U  ZN . ? C ZN 201 ? 1_555 OD1 ? D ASP 110 ? C ASP 83 ? 1_555 101.0 ? 
23 ND1 ? D HIS 98  ? C HIS 71 ? 1_555 ZN ? U  ZN . ? C ZN 201 ? 1_555 OD1 ? D ASP 110 ? C ASP 83 ? 1_555 93.0  ? 
24 ND1 ? D HIS 107 ? C HIS 80 ? 1_555 ZN ? U  ZN . ? C ZN 201 ? 1_555 OD1 ? D ASP 110 ? C ASP 83 ? 1_555 113.9 ? 
25 ND1 ? E HIS 90  ? H HIS 63 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 ND1 ? E HIS 98  ? H HIS 71 ? 1_555 97.8  ? 
26 ND1 ? E HIS 90  ? H HIS 63 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 ND1 ? E HIS 107 ? H HIS 80 ? 1_555 106.1 ? 
27 ND1 ? E HIS 98  ? H HIS 71 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 ND1 ? E HIS 107 ? H HIS 80 ? 1_555 121.0 ? 
28 ND1 ? E HIS 90  ? H HIS 63 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 OD1 ? E ASP 110 ? H ASP 83 ? 1_555 95.1  ? 
29 ND1 ? E HIS 98  ? H HIS 71 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 OD1 ? E ASP 110 ? H ASP 83 ? 1_555 113.2 ? 
30 ND1 ? E HIS 107 ? H HIS 80 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 OD1 ? E ASP 110 ? H ASP 83 ? 1_555 117.2 ? 
31 ND1 ? E HIS 90  ? H HIS 63 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 OD2 ? E ASP 110 ? H ASP 83 ? 1_555 156.4 ? 
32 ND1 ? E HIS 98  ? H HIS 71 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 OD2 ? E ASP 110 ? H ASP 83 ? 1_555 82.5  ? 
33 ND1 ? E HIS 107 ? H HIS 80 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 OD2 ? E ASP 110 ? H ASP 83 ? 1_555 93.7  ? 
34 OD1 ? E ASP 110 ? H ASP 83 ? 1_555 ZN ? W  ZN . ? H ZN 201 ? 1_555 OD2 ? E ASP 110 ? H ASP 83 ? 1_555 63.8  ? 
35 ND1 ? F HIS 90  ? E HIS 63 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 ND1 ? F HIS 98  ? E HIS 71 ? 1_555 106.5 ? 
36 ND1 ? F HIS 90  ? E HIS 63 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 ND1 ? F HIS 107 ? E HIS 80 ? 1_555 107.2 ? 
37 ND1 ? F HIS 98  ? E HIS 71 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 ND1 ? F HIS 107 ? E HIS 80 ? 1_555 125.9 ? 
38 ND1 ? F HIS 90  ? E HIS 63 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 OD1 ? F ASP 110 ? E ASP 83 ? 1_555 97.3  ? 
39 ND1 ? F HIS 98  ? E HIS 71 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 OD1 ? F ASP 110 ? E ASP 83 ? 1_555 94.7  ? 
40 ND1 ? F HIS 107 ? E HIS 80 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 OD1 ? F ASP 110 ? E ASP 83 ? 1_555 121.2 ? 
41 ND1 ? F HIS 90  ? E HIS 63 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 OD2 ? F ASP 110 ? E ASP 83 ? 1_555 151.8 ? 
42 ND1 ? F HIS 98  ? E HIS 71 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 OD2 ? F ASP 110 ? E ASP 83 ? 1_555 78.0  ? 
43 ND1 ? F HIS 107 ? E HIS 80 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 OD2 ? F ASP 110 ? E ASP 83 ? 1_555 90.8  ? 
44 OD1 ? F ASP 110 ? E ASP 83 ? 1_555 ZN ? Y  ZN . ? E ZN 202 ? 1_555 OD2 ? F ASP 110 ? E ASP 83 ? 1_555 54.5  ? 
45 ND1 ? G HIS 90  ? F HIS 63 ? 1_555 ZN ? Z  ZN . ? F ZN 201 ? 1_555 ND1 ? G HIS 98  ? F HIS 71 ? 1_555 106.5 ? 
46 ND1 ? G HIS 90  ? F HIS 63 ? 1_555 ZN ? Z  ZN . ? F ZN 201 ? 1_555 ND1 ? G HIS 107 ? F HIS 80 ? 1_555 105.6 ? 
47 ND1 ? G HIS 98  ? F HIS 71 ? 1_555 ZN ? Z  ZN . ? F ZN 201 ? 1_555 ND1 ? G HIS 107 ? F HIS 80 ? 1_555 128.7 ? 
48 ND1 ? G HIS 90  ? F HIS 63 ? 1_555 ZN ? Z  ZN . ? F ZN 201 ? 1_555 OD1 ? G ASP 110 ? F ASP 83 ? 1_555 112.6 ? 
49 ND1 ? G HIS 98  ? F HIS 71 ? 1_555 ZN ? Z  ZN . ? F ZN 201 ? 1_555 OD1 ? G ASP 110 ? F ASP 83 ? 1_555 90.2  ? 
50 ND1 ? G HIS 107 ? F HIS 80 ? 1_555 ZN ? Z  ZN . ? F ZN 201 ? 1_555 OD1 ? G ASP 110 ? F ASP 83 ? 1_555 112.6 ? 
51 ND1 ? H HIS 90  ? G HIS 63 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 ND1 ? H HIS 98  ? G HIS 71 ? 1_555 100.5 ? 
52 ND1 ? H HIS 90  ? G HIS 63 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 ND1 ? H HIS 107 ? G HIS 80 ? 1_555 106.6 ? 
53 ND1 ? H HIS 98  ? G HIS 71 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 ND1 ? H HIS 107 ? G HIS 80 ? 1_555 126.4 ? 
54 ND1 ? H HIS 90  ? G HIS 63 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 OD1 ? H ASP 110 ? G ASP 83 ? 1_555 97.6  ? 
55 ND1 ? H HIS 98  ? G HIS 71 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 OD1 ? H ASP 110 ? G ASP 83 ? 1_555 100.9 ? 
56 ND1 ? H HIS 107 ? G HIS 80 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 OD1 ? H ASP 110 ? G ASP 83 ? 1_555 119.7 ? 
57 ND1 ? H HIS 90  ? G HIS 63 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 OD2 ? H ASP 110 ? G ASP 83 ? 1_555 155.4 ? 
58 ND1 ? H HIS 98  ? G HIS 71 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 OD2 ? H ASP 110 ? G ASP 83 ? 1_555 80.3  ? 
59 ND1 ? H HIS 107 ? G HIS 80 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 OD2 ? H ASP 110 ? G ASP 83 ? 1_555 91.9  ? 
60 OD1 ? H ASP 110 ? G ASP 83 ? 1_555 ZN ? AA ZN . ? G ZN 201 ? 1_555 OD2 ? H ASP 110 ? G ASP 83 ? 1_555 58.5  ? 
61 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_555 107.4 ? 
62 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_555 109.4 ? 
63 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_555 127.4 ? 
64 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_555 105.4 ? 
65 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 91.1  ? 
66 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_555 113.4 ? 
# 
_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       2023-12-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_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        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.20.1_4487 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .           2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27        3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .           5 
# 
_pdbx_entry_details.entry_id                 7XX3 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   Y 
# 
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   I HOH 348 ? ? O   I HOH 407 ? ? 1.88 
2  1 OD1 H ASN 53  ? B O   H HOH 301 ? ? 2.03 
3  1 O   J LYS 36  ? B O   J HOH 201 ? ? 2.05 
4  1 O   J LYS 36  ? A O   J HOH 201 ? ? 2.08 
5  1 O   B HOH 302 ? ? O   B HOH 408 ? ? 2.11 
6  1 O   D HOH 351 ? ? O   D HOH 360 ? ? 2.11 
7  1 O   A HOH 302 ? ? O   A HOH 378 ? ? 2.14 
8  1 OD2 E ASP 76  ? ? O   E HOH 301 ? ? 2.15 
9  1 O   C CYS 6   ? ? O   C HOH 301 ? ? 2.15 
10 1 NZ  A LYS 3   ? ? OE2 A GLU 21  ? ? 2.18 
11 1 O   C HOH 396 ? ? O   C HOH 397 ? ? 2.18 
12 1 NZ  C LYS 30  ? ? O   C HOH 302 ? ? 2.18 
13 1 O   I HOH 369 ? ? O   I HOH 388 ? ? 2.18 
# 
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 ARG D 69  ? ? -90.80  -146.33 
2 1 LYS D 128 ? ? -96.65  54.10   
3 1 ASN H 65  ? ? -151.04 72.67   
4 1 ALA F 55  ? ? -108.45 41.64   
5 1 LYS F 136 ? ? -105.15 -61.29  
6 1 ASN I 26  ? ? -143.24 36.16   
7 1 ASN I 65  ? ? -151.23 63.28   
# 
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 446 ? 6.35 . 
2 1 O ? A HOH 447 ? 6.43 . 
3 1 O ? D HOH 416 ? 6.58 . 
4 1 O ? E HOH 460 ? 6.23 . 
5 1 O ? J HOH 267 ? 6.80 . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A MET 0   ? CG  ? A MET 27  CG  
2  1 Y 1 A MET 0   ? SD  ? A MET 27  SD  
3  1 Y 1 A MET 0   ? CE  ? A MET 27  CE  
4  1 Y 1 B MET 0   ? CG  ? B MET 27  CG  
5  1 Y 1 B MET 0   ? SD  ? B MET 27  SD  
6  1 Y 1 B MET 0   ? CE  ? B MET 27  CE  
7  1 Y 1 D MET 0   ? CG  ? C MET 27  CG  
8  1 Y 1 D MET 0   ? SD  ? C MET 27  SD  
9  1 Y 1 D MET 0   ? CE  ? C MET 27  CE  
10 1 Y 1 D LYS 75  ? CG  ? C LYS 102 CG  
11 1 Y 1 D LYS 75  ? CD  ? C LYS 102 CD  
12 1 Y 1 D LYS 75  ? CE  ? C LYS 102 CE  
13 1 Y 1 D LYS 75  ? NZ  ? C LYS 102 NZ  
14 1 Y 1 H MET 0   ? CG  ? E MET 27  CG  
15 1 Y 1 H MET 0   ? SD  ? E MET 27  SD  
16 1 Y 1 H MET 0   ? CE  ? E MET 27  CE  
17 1 Y 1 H LYS 70  ? CG  ? E LYS 97  CG  
18 1 Y 1 H LYS 70  ? CD  ? E LYS 97  CD  
19 1 Y 1 H LYS 70  ? CE  ? E LYS 97  CE  
20 1 Y 1 H LYS 70  ? NZ  ? E LYS 97  NZ  
21 1 Y 1 H GLU 77  ? CG  ? E GLU 104 CG  
22 1 Y 1 H GLU 77  ? CD  ? E GLU 104 CD  
23 1 Y 1 H GLU 77  ? OE1 ? E GLU 104 OE1 
24 1 Y 1 H GLU 77  ? OE2 ? E GLU 104 OE2 
25 1 Y 1 H LYS 128 ? CG  ? E LYS 155 CG  
26 1 Y 1 H LYS 128 ? CD  ? E LYS 155 CD  
27 1 Y 1 H LYS 128 ? CE  ? E LYS 155 CE  
28 1 Y 1 H LYS 128 ? NZ  ? E LYS 155 NZ  
29 1 Y 0 H GLU 132 ? CD  ? E GLU 159 CD  
30 1 Y 0 H GLU 132 ? OE1 ? E GLU 159 OE1 
31 1 Y 0 H GLU 132 ? OE2 ? E GLU 159 OE2 
32 1 Y 1 E THR 2   ? OG1 ? F THR 29  OG1 
33 1 Y 1 E THR 2   ? CG2 ? F THR 29  CG2 
34 1 Y 0 J LEU 126 ? CG  ? J LEU 153 CG  
35 1 Y 0 J LEU 126 ? CD1 ? J LEU 153 CD1 
36 1 Y 0 J LEU 126 ? CD2 ? J LEU 153 CD2 
# 
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 A ALA -1  ? A ALA 26  
27  1 Y 1 B MET -26 ? B MET 1   
28  1 Y 1 B LYS -25 ? B LYS 2   
29  1 Y 1 B HIS -24 ? B HIS 3   
30  1 Y 1 B HIS -23 ? B HIS 4   
31  1 Y 1 B HIS -22 ? B HIS 5   
32  1 Y 1 B HIS -21 ? B HIS 6   
33  1 Y 1 B HIS -20 ? B HIS 7   
34  1 Y 1 B HIS -19 ? B HIS 8   
35  1 Y 1 B PRO -18 ? B PRO 9   
36  1 Y 1 B MET -17 ? B MET 10  
37  1 Y 1 B SER -16 ? B SER 11  
38  1 Y 1 B ASP -15 ? B ASP 12  
39  1 Y 1 B TYR -14 ? B TYR 13  
40  1 Y 1 B ASP -13 ? B ASP 14  
41  1 Y 1 B ILE -12 ? B ILE 15  
42  1 Y 1 B PRO -11 ? B PRO 16  
43  1 Y 1 B THR -10 ? B THR 17  
44  1 Y 1 B THR -9  ? B THR 18  
45  1 Y 1 B GLU -8  ? B GLU 19  
46  1 Y 1 B ASN -7  ? B ASN 20  
47  1 Y 1 B LEU -6  ? B LEU 21  
48  1 Y 1 B TYR -5  ? B TYR 22  
49  1 Y 1 B PHE -4  ? B PHE 23  
50  1 Y 1 B GLN -3  ? B GLN 24  
51  1 Y 1 B GLY -2  ? B GLY 25  
52  1 Y 1 B ALA -1  ? B ALA 26  
53  1 Y 1 D MET -26 ? C MET 1   
54  1 Y 1 D LYS -25 ? C LYS 2   
55  1 Y 1 D HIS -24 ? C HIS 3   
56  1 Y 1 D HIS -23 ? C HIS 4   
57  1 Y 1 D HIS -22 ? C HIS 5   
58  1 Y 1 D HIS -21 ? C HIS 6   
59  1 Y 1 D HIS -20 ? C HIS 7   
60  1 Y 1 D HIS -19 ? C HIS 8   
61  1 Y 1 D PRO -18 ? C PRO 9   
62  1 Y 1 D MET -17 ? C MET 10  
63  1 Y 1 D SER -16 ? C SER 11  
64  1 Y 1 D ASP -15 ? C ASP 12  
65  1 Y 1 D TYR -14 ? C TYR 13  
66  1 Y 1 D ASP -13 ? C ASP 14  
67  1 Y 1 D ILE -12 ? C ILE 15  
68  1 Y 1 D PRO -11 ? C PRO 16  
69  1 Y 1 D THR -10 ? C THR 17  
70  1 Y 1 D THR -9  ? C THR 18  
71  1 Y 1 D GLU -8  ? C GLU 19  
72  1 Y 1 D ASN -7  ? C ASN 20  
73  1 Y 1 D LEU -6  ? C LEU 21  
74  1 Y 1 D TYR -5  ? C TYR 22  
75  1 Y 1 D PHE -4  ? C PHE 23  
76  1 Y 1 D GLN -3  ? C GLN 24  
77  1 Y 1 D GLY -2  ? C GLY 25  
78  1 Y 1 D ALA -1  ? C ALA 26  
79  1 Y 1 C MET -26 ? D MET 1   
80  1 Y 1 C LYS -25 ? D LYS 2   
81  1 Y 1 C HIS -24 ? D HIS 3   
82  1 Y 1 C HIS -23 ? D HIS 4   
83  1 Y 1 C HIS -22 ? D HIS 5   
84  1 Y 1 C HIS -21 ? D HIS 6   
85  1 Y 1 C HIS -20 ? D HIS 7   
86  1 Y 1 C HIS -19 ? D HIS 8   
87  1 Y 1 C PRO -18 ? D PRO 9   
88  1 Y 1 C MET -17 ? D MET 10  
89  1 Y 1 C SER -16 ? D SER 11  
90  1 Y 1 C ASP -15 ? D ASP 12  
91  1 Y 1 C TYR -14 ? D TYR 13  
92  1 Y 1 C ASP -13 ? D ASP 14  
93  1 Y 1 C ILE -12 ? D ILE 15  
94  1 Y 1 C PRO -11 ? D PRO 16  
95  1 Y 1 C THR -10 ? D THR 17  
96  1 Y 1 C THR -9  ? D THR 18  
97  1 Y 1 C GLU -8  ? D GLU 19  
98  1 Y 1 C ASN -7  ? D ASN 20  
99  1 Y 1 C LEU -6  ? D LEU 21  
100 1 Y 1 C TYR -5  ? D TYR 22  
101 1 Y 1 C PHE -4  ? D PHE 23  
102 1 Y 1 C GLN -3  ? D GLN 24  
103 1 Y 1 C GLY -2  ? D GLY 25  
104 1 Y 1 C ALA -1  ? D ALA 26  
105 1 Y 1 C MET 0   ? D MET 27  
106 1 Y 1 H MET -26 ? E MET 1   
107 1 Y 1 H LYS -25 ? E LYS 2   
108 1 Y 1 H HIS -24 ? E HIS 3   
109 1 Y 1 H HIS -23 ? E HIS 4   
110 1 Y 1 H HIS -22 ? E HIS 5   
111 1 Y 1 H HIS -21 ? E HIS 6   
112 1 Y 1 H HIS -20 ? E HIS 7   
113 1 Y 1 H HIS -19 ? E HIS 8   
114 1 Y 1 H PRO -18 ? E PRO 9   
115 1 Y 1 H MET -17 ? E MET 10  
116 1 Y 1 H SER -16 ? E SER 11  
117 1 Y 1 H ASP -15 ? E ASP 12  
118 1 Y 1 H TYR -14 ? E TYR 13  
119 1 Y 1 H ASP -13 ? E ASP 14  
120 1 Y 1 H ILE -12 ? E ILE 15  
121 1 Y 1 H PRO -11 ? E PRO 16  
122 1 Y 1 H THR -10 ? E THR 17  
123 1 Y 1 H THR -9  ? E THR 18  
124 1 Y 1 H GLU -8  ? E GLU 19  
125 1 Y 1 H ASN -7  ? E ASN 20  
126 1 Y 1 H LEU -6  ? E LEU 21  
127 1 Y 1 H TYR -5  ? E TYR 22  
128 1 Y 1 H PHE -4  ? E PHE 23  
129 1 Y 1 H GLN -3  ? E GLN 24  
130 1 Y 1 H GLY -2  ? E GLY 25  
131 1 Y 1 H ALA -1  ? E ALA 26  
132 1 Y 1 E MET -26 ? F MET 1   
133 1 Y 1 E LYS -25 ? F LYS 2   
134 1 Y 1 E HIS -24 ? F HIS 3   
135 1 Y 1 E HIS -23 ? F HIS 4   
136 1 Y 1 E HIS -22 ? F HIS 5   
137 1 Y 1 E HIS -21 ? F HIS 6   
138 1 Y 1 E HIS -20 ? F HIS 7   
139 1 Y 1 E HIS -19 ? F HIS 8   
140 1 Y 1 E PRO -18 ? F PRO 9   
141 1 Y 1 E MET -17 ? F MET 10  
142 1 Y 1 E SER -16 ? F SER 11  
143 1 Y 1 E ASP -15 ? F ASP 12  
144 1 Y 1 E TYR -14 ? F TYR 13  
145 1 Y 1 E ASP -13 ? F ASP 14  
146 1 Y 1 E ILE -12 ? F ILE 15  
147 1 Y 1 E PRO -11 ? F PRO 16  
148 1 Y 1 E THR -10 ? F THR 17  
149 1 Y 1 E THR -9  ? F THR 18  
150 1 Y 1 E GLU -8  ? F GLU 19  
151 1 Y 1 E ASN -7  ? F ASN 20  
152 1 Y 1 E LEU -6  ? F LEU 21  
153 1 Y 1 E TYR -5  ? F TYR 22  
154 1 Y 1 E PHE -4  ? F PHE 23  
155 1 Y 1 E GLN -3  ? F GLN 24  
156 1 Y 1 E GLY -2  ? F GLY 25  
157 1 Y 1 E ALA -1  ? F ALA 26  
158 1 Y 1 E MET 0   ? F MET 27  
159 1 Y 1 F MET -26 ? G MET 1   
160 1 Y 1 F LYS -25 ? G LYS 2   
161 1 Y 1 F HIS -24 ? G HIS 3   
162 1 Y 1 F HIS -23 ? G HIS 4   
163 1 Y 1 F HIS -22 ? G HIS 5   
164 1 Y 1 F HIS -21 ? G HIS 6   
165 1 Y 1 F HIS -20 ? G HIS 7   
166 1 Y 1 F HIS -19 ? G HIS 8   
167 1 Y 1 F PRO -18 ? G PRO 9   
168 1 Y 1 F MET -17 ? G MET 10  
169 1 Y 1 F SER -16 ? G SER 11  
170 1 Y 1 F ASP -15 ? G ASP 12  
171 1 Y 1 F TYR -14 ? G TYR 13  
172 1 Y 1 F ASP -13 ? G ASP 14  
173 1 Y 1 F ILE -12 ? G ILE 15  
174 1 Y 1 F PRO -11 ? G PRO 16  
175 1 Y 1 F THR -10 ? G THR 17  
176 1 Y 1 F THR -9  ? G THR 18  
177 1 Y 1 F GLU -8  ? G GLU 19  
178 1 Y 1 F ASN -7  ? G ASN 20  
179 1 Y 1 F LEU -6  ? G LEU 21  
180 1 Y 1 F TYR -5  ? G TYR 22  
181 1 Y 1 F PHE -4  ? G PHE 23  
182 1 Y 1 F GLN -3  ? G GLN 24  
183 1 Y 1 F GLY -2  ? G GLY 25  
184 1 Y 1 F ALA -1  ? G ALA 26  
185 1 Y 1 F MET 0   ? G MET 27  
186 1 Y 1 G MET -26 ? H MET 1   
187 1 Y 1 G LYS -25 ? H LYS 2   
188 1 Y 1 G HIS -24 ? H HIS 3   
189 1 Y 1 G HIS -23 ? H HIS 4   
190 1 Y 1 G HIS -22 ? H HIS 5   
191 1 Y 1 G HIS -21 ? H HIS 6   
192 1 Y 1 G HIS -20 ? H HIS 7   
193 1 Y 1 G HIS -19 ? H HIS 8   
194 1 Y 1 G PRO -18 ? H PRO 9   
195 1 Y 1 G MET -17 ? H MET 10  
196 1 Y 1 G SER -16 ? H SER 11  
197 1 Y 1 G ASP -15 ? H ASP 12  
198 1 Y 1 G TYR -14 ? H TYR 13  
199 1 Y 1 G ASP -13 ? H ASP 14  
200 1 Y 1 G ILE -12 ? H ILE 15  
201 1 Y 1 G PRO -11 ? H PRO 16  
202 1 Y 1 G THR -10 ? H THR 17  
203 1 Y 1 G THR -9  ? H THR 18  
204 1 Y 1 G GLU -8  ? H GLU 19  
205 1 Y 1 G ASN -7  ? H ASN 20  
206 1 Y 1 G LEU -6  ? H LEU 21  
207 1 Y 1 G TYR -5  ? H TYR 22  
208 1 Y 1 G PHE -4  ? H PHE 23  
209 1 Y 1 G GLN -3  ? H GLN 24  
210 1 Y 1 G GLY -2  ? H GLY 25  
211 1 Y 1 G ALA -1  ? H ALA 26  
212 1 Y 1 G MET 0   ? H MET 27  
213 1 Y 1 G ALA 1   ? H ALA 28  
214 1 Y 1 I MET -26 ? I MET 1   
215 1 Y 1 I LYS -25 ? I LYS 2   
216 1 Y 1 I HIS -24 ? I HIS 3   
217 1 Y 1 I HIS -23 ? I HIS 4   
218 1 Y 1 I HIS -22 ? I HIS 5   
219 1 Y 1 I HIS -21 ? I HIS 6   
220 1 Y 1 I HIS -20 ? I HIS 7   
221 1 Y 1 I HIS -19 ? I HIS 8   
222 1 Y 1 I PRO -18 ? I PRO 9   
223 1 Y 1 I MET -17 ? I MET 10  
224 1 Y 1 I SER -16 ? I SER 11  
225 1 Y 1 I ASP -15 ? I ASP 12  
226 1 Y 1 I TYR -14 ? I TYR 13  
227 1 Y 1 I ASP -13 ? I ASP 14  
228 1 Y 1 I ILE -12 ? I ILE 15  
229 1 Y 1 I PRO -11 ? I PRO 16  
230 1 Y 1 I THR -10 ? I THR 17  
231 1 Y 1 I THR -9  ? I THR 18  
232 1 Y 1 I GLU -8  ? I GLU 19  
233 1 Y 1 I ASN -7  ? I ASN 20  
234 1 Y 1 I LEU -6  ? I LEU 21  
235 1 Y 1 I TYR -5  ? I TYR 22  
236 1 Y 1 I PHE -4  ? I PHE 23  
237 1 Y 1 I GLN -3  ? I GLN 24  
238 1 Y 1 I GLY -2  ? I GLY 25  
239 1 Y 1 I ALA -1  ? I ALA 26  
240 1 Y 1 I MET 0   ? I MET 27  
241 1 Y 1 J MET -26 ? J MET 1   
242 1 Y 1 J LYS -25 ? J LYS 2   
243 1 Y 1 J HIS -24 ? J HIS 3   
244 1 Y 1 J HIS -23 ? J HIS 4   
245 1 Y 1 J HIS -22 ? J HIS 5   
246 1 Y 1 J HIS -21 ? J HIS 6   
247 1 Y 1 J HIS -20 ? J HIS 7   
248 1 Y 1 J HIS -19 ? J HIS 8   
249 1 Y 1 J PRO -18 ? J PRO 9   
250 1 Y 1 J MET -17 ? J MET 10  
251 1 Y 1 J SER -16 ? J SER 11  
252 1 Y 1 J ASP -15 ? J ASP 12  
253 1 Y 1 J TYR -14 ? J TYR 13  
254 1 Y 1 J ASP -13 ? J ASP 14  
255 1 Y 1 J ILE -12 ? J ILE 15  
256 1 Y 1 J PRO -11 ? J PRO 16  
257 1 Y 1 J THR -10 ? J THR 17  
258 1 Y 1 J THR -9  ? J THR 18  
259 1 Y 1 J GLU -8  ? J GLU 19  
260 1 Y 1 J ASN -7  ? J ASN 20  
261 1 Y 1 J LEU -6  ? J LEU 21  
262 1 Y 1 J TYR -5  ? J TYR 22  
263 1 Y 1 J PHE -4  ? J PHE 23  
264 1 Y 1 J GLN -3  ? J GLN 24  
265 1 Y 1 J GLY -2  ? J GLY 25  
266 1 Y 1 J ALA -1  ? J ALA 26  
267 1 Y 1 J MET 0   ? J MET 27  
268 1 Y 1 J LEU 67  ? J LEU 94  
269 1 Y 1 J SER 68  ? J SER 95  
270 1 Y 1 J ARG 69  ? J ARG 96  
271 1 Y 1 J LYS 70  ? J LYS 97  
272 1 Y 1 J HIS 71  ? J HIS 98  
273 1 Y 1 J GLY 72  ? J GLY 99  
274 1 Y 1 J GLY 73  ? J GLY 100 
275 1 Y 1 J PRO 74  ? J PRO 101 
276 1 Y 1 J LYS 75  ? J LYS 102 
277 1 Y 1 J ASP 76  ? J ASP 103 
278 1 Y 1 J GLU 77  ? J GLU 104 
279 1 Y 1 J GLU 78  ? J GLU 105 
280 1 Y 1 J GLY 127 ? J GLY 154 
281 1 Y 1 J LYS 128 ? J LYS 155 
282 1 Y 1 J GLY 129 ? J GLY 156 
283 1 Y 1 J GLY 130 ? J GLY 157 
284 1 Y 1 J ASN 131 ? J ASN 158 
285 1 Y 1 J GLU 132 ? J GLU 159 
286 1 Y 1 J GLU 133 ? J GLU 160 
287 1 Y 1 J SER 134 ? J SER 161 
288 1 Y 1 J THR 135 ? J THR 162 
289 1 Y 1 J LYS 136 ? J LYS 163 
290 1 Y 1 J THR 137 ? J THR 164 
291 1 Y 1 J GLY 138 ? J GLY 165 
292 1 Y 1 J ASN 139 ? J ASN 166 
293 1 Y 1 J ALA 140 ? J ALA 167 
294 1 Y 1 J GLY 141 ? J GLY 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
GOL C1   C  N N 147 
GOL O1   O  N N 148 
GOL C2   C  N N 149 
GOL O2   O  N N 150 
GOL C3   C  N N 151 
GOL O3   O  N N 152 
GOL H11  H  N N 153 
GOL H12  H  N N 154 
GOL HO1  H  N N 155 
GOL H2   H  N N 156 
GOL HO2  H  N N 157 
GOL H31  H  N N 158 
GOL H32  H  N N 159 
GOL HO3  H  N N 160 
HIS N    N  N N 161 
HIS CA   C  N S 162 
HIS C    C  N N 163 
HIS O    O  N N 164 
HIS CB   C  N N 165 
HIS CG   C  Y N 166 
HIS ND1  N  Y N 167 
HIS CD2  C  Y N 168 
HIS CE1  C  Y N 169 
HIS NE2  N  Y N 170 
HIS OXT  O  N N 171 
HIS H    H  N N 172 
HIS H2   H  N N 173 
HIS HA   H  N N 174 
HIS HB2  H  N N 175 
HIS HB3  H  N N 176 
HIS HD1  H  N N 177 
HIS HD2  H  N N 178 
HIS HE1  H  N N 179 
HIS HE2  H  N N 180 
HIS HXT  H  N N 181 
HOH O    O  N N 182 
HOH H1   H  N N 183 
HOH H2   H  N N 184 
I2G C1   C  N N 185 
I2G C2   C  N N 186 
I2G C4   C  N N 187 
I2G C5   C  N S 188 
I2G C6   C  N N 189 
I2G C7   C  N N 190 
I2G C8   C  N N 191 
I2G C9   C  N N 192 
I2G C10  C  N N 193 
I2G C11  C  N N 194 
I2G C12  C  N N 195 
I2G C3   C  N N 196 
I2G O13  O  N N 197 
I2G O14  O  N N 198 
I2G H1   H  N N 199 
I2G H2   H  N N 200 
I2G H3   H  N N 201 
I2G H4   H  N N 202 
I2G H5   H  N N 203 
I2G H6   H  N N 204 
I2G H7   H  N N 205 
I2G H8   H  N N 206 
I2G H9   H  N N 207 
I2G H10  H  N N 208 
I2G H11  H  N N 209 
I2G H12  H  N N 210 
I2G H13  H  N N 211 
I2G H14  H  N N 212 
I2G H15  H  N N 213 
I2G H16  H  N N 214 
I2G H17  H  N N 215 
I2G H18  H  N N 216 
I2G H19  H  N N 217 
I2G H20  H  N N 218 
ILE N    N  N N 219 
ILE CA   C  N S 220 
ILE C    C  N N 221 
ILE O    O  N N 222 
ILE CB   C  N S 223 
ILE CG1  C  N N 224 
ILE CG2  C  N N 225 
ILE CD1  C  N N 226 
ILE OXT  O  N N 227 
ILE H    H  N N 228 
ILE H2   H  N N 229 
ILE HA   H  N N 230 
ILE HB   H  N N 231 
ILE HG12 H  N N 232 
ILE HG13 H  N N 233 
ILE HG21 H  N N 234 
ILE HG22 H  N N 235 
ILE HG23 H  N N 236 
ILE HD11 H  N N 237 
ILE HD12 H  N N 238 
ILE HD13 H  N N 239 
ILE HXT  H  N N 240 
LEU N    N  N N 241 
LEU CA   C  N S 242 
LEU C    C  N N 243 
LEU O    O  N N 244 
LEU CB   C  N N 245 
LEU CG   C  N N 246 
LEU CD1  C  N N 247 
LEU CD2  C  N N 248 
LEU OXT  O  N N 249 
LEU H    H  N N 250 
LEU H2   H  N N 251 
LEU HA   H  N N 252 
LEU HB2  H  N N 253 
LEU HB3  H  N N 254 
LEU HG   H  N N 255 
LEU HD11 H  N N 256 
LEU HD12 H  N N 257 
LEU HD13 H  N N 258 
LEU HD21 H  N N 259 
LEU HD22 H  N N 260 
LEU HD23 H  N N 261 
LEU HXT  H  N N 262 
LYS N    N  N N 263 
LYS CA   C  N S 264 
LYS C    C  N N 265 
LYS O    O  N N 266 
LYS CB   C  N N 267 
LYS CG   C  N N 268 
LYS CD   C  N N 269 
LYS CE   C  N N 270 
LYS NZ   N  N N 271 
LYS OXT  O  N N 272 
LYS H    H  N N 273 
LYS H2   H  N N 274 
LYS HA   H  N N 275 
LYS HB2  H  N N 276 
LYS HB3  H  N N 277 
LYS HG2  H  N N 278 
LYS HG3  H  N N 279 
LYS HD2  H  N N 280 
LYS HD3  H  N N 281 
LYS HE2  H  N N 282 
LYS HE3  H  N N 283 
LYS HZ1  H  N N 284 
LYS HZ2  H  N N 285 
LYS HZ3  H  N N 286 
LYS HXT  H  N N 287 
MET N    N  N N 288 
MET CA   C  N S 289 
MET C    C  N N 290 
MET O    O  N N 291 
MET CB   C  N N 292 
MET CG   C  N N 293 
MET SD   S  N N 294 
MET CE   C  N N 295 
MET OXT  O  N N 296 
MET H    H  N N 297 
MET H2   H  N N 298 
MET HA   H  N N 299 
MET HB2  H  N N 300 
MET HB3  H  N N 301 
MET HG2  H  N N 302 
MET HG3  H  N N 303 
MET HE1  H  N N 304 
MET HE2  H  N N 305 
MET HE3  H  N N 306 
MET HXT  H  N N 307 
PHE N    N  N N 308 
PHE CA   C  N S 309 
PHE C    C  N N 310 
PHE O    O  N N 311 
PHE CB   C  N N 312 
PHE CG   C  Y N 313 
PHE CD1  C  Y N 314 
PHE CD2  C  Y N 315 
PHE CE1  C  Y N 316 
PHE CE2  C  Y N 317 
PHE CZ   C  Y N 318 
PHE OXT  O  N N 319 
PHE H    H  N N 320 
PHE H2   H  N N 321 
PHE HA   H  N N 322 
PHE HB2  H  N N 323 
PHE HB3  H  N N 324 
PHE HD1  H  N N 325 
PHE HD2  H  N N 326 
PHE HE1  H  N N 327 
PHE HE2  H  N N 328 
PHE HZ   H  N N 329 
PHE HXT  H  N N 330 
PRO N    N  N N 331 
PRO CA   C  N S 332 
PRO C    C  N N 333 
PRO O    O  N N 334 
PRO CB   C  N N 335 
PRO CG   C  N N 336 
PRO CD   C  N N 337 
PRO OXT  O  N N 338 
PRO H    H  N N 339 
PRO HA   H  N N 340 
PRO HB2  H  N N 341 
PRO HB3  H  N N 342 
PRO HG2  H  N N 343 
PRO HG3  H  N N 344 
PRO HD2  H  N N 345 
PRO HD3  H  N N 346 
PRO HXT  H  N N 347 
SER N    N  N N 348 
SER CA   C  N S 349 
SER C    C  N N 350 
SER O    O  N N 351 
SER CB   C  N N 352 
SER OG   O  N N 353 
SER OXT  O  N N 354 
SER H    H  N N 355 
SER H2   H  N N 356 
SER HA   H  N N 357 
SER HB2  H  N N 358 
SER HB3  H  N N 359 
SER HG   H  N N 360 
SER HXT  H  N N 361 
THR N    N  N N 362 
THR CA   C  N S 363 
THR C    C  N N 364 
THR O    O  N N 365 
THR CB   C  N R 366 
THR OG1  O  N N 367 
THR CG2  C  N N 368 
THR OXT  O  N N 369 
THR H    H  N N 370 
THR H2   H  N N 371 
THR HA   H  N N 372 
THR HB   H  N N 373 
THR HG1  H  N N 374 
THR HG21 H  N N 375 
THR HG22 H  N N 376 
THR HG23 H  N N 377 
THR HXT  H  N N 378 
TRP N    N  N N 379 
TRP CA   C  N S 380 
TRP C    C  N N 381 
TRP O    O  N N 382 
TRP CB   C  N N 383 
TRP CG   C  Y N 384 
TRP CD1  C  Y N 385 
TRP CD2  C  Y N 386 
TRP NE1  N  Y N 387 
TRP CE2  C  Y N 388 
TRP CE3  C  Y N 389 
TRP CZ2  C  Y N 390 
TRP CZ3  C  Y N 391 
TRP CH2  C  Y N 392 
TRP OXT  O  N N 393 
TRP H    H  N N 394 
TRP H2   H  N N 395 
TRP HA   H  N N 396 
TRP HB2  H  N N 397 
TRP HB3  H  N N 398 
TRP HD1  H  N N 399 
TRP HE1  H  N N 400 
TRP HE3  H  N N 401 
TRP HZ2  H  N N 402 
TRP HZ3  H  N N 403 
TRP HH2  H  N N 404 
TRP HXT  H  N N 405 
TYR N    N  N N 406 
TYR CA   C  N S 407 
TYR C    C  N N 408 
TYR O    O  N N 409 
TYR CB   C  N N 410 
TYR CG   C  Y N 411 
TYR CD1  C  Y N 412 
TYR CD2  C  Y N 413 
TYR CE1  C  Y N 414 
TYR CE2  C  Y N 415 
TYR CZ   C  Y N 416 
TYR OH   O  N N 417 
TYR OXT  O  N N 418 
TYR H    H  N N 419 
TYR H2   H  N N 420 
TYR HA   H  N N 421 
TYR HB2  H  N N 422 
TYR HB3  H  N N 423 
TYR HD1  H  N N 424 
TYR HD2  H  N N 425 
TYR HE1  H  N N 426 
TYR HE2  H  N N 427 
TYR HH   H  N N 428 
TYR HXT  H  N N 429 
VAL N    N  N N 430 
VAL CA   C  N S 431 
VAL C    C  N N 432 
VAL O    O  N N 433 
VAL CB   C  N N 434 
VAL CG1  C  N N 435 
VAL CG2  C  N N 436 
VAL OXT  O  N N 437 
VAL H    H  N N 438 
VAL H2   H  N N 439 
VAL HA   H  N N 440 
VAL HB   H  N N 441 
VAL HG11 H  N N 442 
VAL HG12 H  N N 443 
VAL HG13 H  N N 444 
VAL HG21 H  N N 445 
VAL HG22 H  N N 446 
VAL HG23 H  N N 447 
VAL HXT  H  N N 448 
ZN  ZN   ZN N N 449 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
GOL C1  O1   sing N N 138 
GOL C1  C2   sing N N 139 
GOL C1  H11  sing N N 140 
GOL C1  H12  sing N N 141 
GOL O1  HO1  sing N N 142 
GOL C2  O2   sing N N 143 
GOL C2  C3   sing N N 144 
GOL C2  H2   sing N N 145 
GOL O2  HO2  sing N N 146 
GOL C3  O3   sing N N 147 
GOL C3  H31  sing N N 148 
GOL C3  H32  sing N N 149 
GOL O3  HO3  sing N N 150 
HIS N   CA   sing N N 151 
HIS N   H    sing N N 152 
HIS N   H2   sing N N 153 
HIS CA  C    sing N N 154 
HIS CA  CB   sing N N 155 
HIS CA  HA   sing N N 156 
HIS C   O    doub N N 157 
HIS C   OXT  sing N N 158 
HIS CB  CG   sing N N 159 
HIS CB  HB2  sing N N 160 
HIS CB  HB3  sing N N 161 
HIS CG  ND1  sing Y N 162 
HIS CG  CD2  doub Y N 163 
HIS ND1 CE1  doub Y N 164 
HIS ND1 HD1  sing N N 165 
HIS CD2 NE2  sing Y N 166 
HIS CD2 HD2  sing N N 167 
HIS CE1 NE2  sing Y N 168 
HIS CE1 HE1  sing N N 169 
HIS NE2 HE2  sing N N 170 
HIS OXT HXT  sing N N 171 
HOH O   H1   sing N N 172 
HOH O   H2   sing N N 173 
I2G C3  C2   sing N N 174 
I2G O14 C12  doub N N 175 
I2G C2  C1   sing N N 176 
I2G C12 C11  sing N N 177 
I2G C12 O13  sing N N 178 
I2G C6  C1   sing N N 179 
I2G C6  C5   sing N N 180 
I2G C11 C10  doub N E 181 
I2G C4  C5   sing N N 182 
I2G C4  C9   doub N E 183 
I2G C10 C9   sing N N 184 
I2G C5  C8   sing N N 185 
I2G C9  C7   sing N N 186 
I2G C1  H1   sing N N 187 
I2G C1  H2   sing N N 188 
I2G C2  H3   sing N N 189 
I2G C2  H4   sing N N 190 
I2G C4  H5   sing N N 191 
I2G C5  H6   sing N N 192 
I2G C6  H7   sing N N 193 
I2G C6  H8   sing N N 194 
I2G C7  H9   sing N N 195 
I2G C7  H10  sing N N 196 
I2G C7  H11  sing N N 197 
I2G C8  H12  sing N N 198 
I2G C8  H13  sing N N 199 
I2G C8  H14  sing N N 200 
I2G C10 H15  sing N N 201 
I2G C11 H16  sing N N 202 
I2G C3  H17  sing N N 203 
I2G C3  H18  sing N N 204 
I2G C3  H19  sing N N 205 
I2G O13 H20  sing N N 206 
ILE N   CA   sing N N 207 
ILE N   H    sing N N 208 
ILE N   H2   sing N N 209 
ILE CA  C    sing N N 210 
ILE CA  CB   sing N N 211 
ILE CA  HA   sing N N 212 
ILE C   O    doub N N 213 
ILE C   OXT  sing N N 214 
ILE CB  CG1  sing N N 215 
ILE CB  CG2  sing N N 216 
ILE CB  HB   sing N N 217 
ILE CG1 CD1  sing N N 218 
ILE CG1 HG12 sing N N 219 
ILE CG1 HG13 sing N N 220 
ILE CG2 HG21 sing N N 221 
ILE CG2 HG22 sing N N 222 
ILE CG2 HG23 sing N N 223 
ILE CD1 HD11 sing N N 224 
ILE CD1 HD12 sing N N 225 
ILE CD1 HD13 sing N N 226 
ILE OXT HXT  sing N N 227 
LEU N   CA   sing N N 228 
LEU N   H    sing N N 229 
LEU N   H2   sing N N 230 
LEU CA  C    sing N N 231 
LEU CA  CB   sing N N 232 
LEU CA  HA   sing N N 233 
LEU C   O    doub N N 234 
LEU C   OXT  sing N N 235 
LEU CB  CG   sing N N 236 
LEU CB  HB2  sing N N 237 
LEU CB  HB3  sing N N 238 
LEU CG  CD1  sing N N 239 
LEU CG  CD2  sing N N 240 
LEU CG  HG   sing N N 241 
LEU CD1 HD11 sing N N 242 
LEU CD1 HD12 sing N N 243 
LEU CD1 HD13 sing N N 244 
LEU CD2 HD21 sing N N 245 
LEU CD2 HD22 sing N N 246 
LEU CD2 HD23 sing N N 247 
LEU OXT HXT  sing N N 248 
LYS N   CA   sing N N 249 
LYS N   H    sing N N 250 
LYS N   H2   sing N N 251 
LYS CA  C    sing N N 252 
LYS CA  CB   sing N N 253 
LYS CA  HA   sing N N 254 
LYS C   O    doub N N 255 
LYS C   OXT  sing N N 256 
LYS CB  CG   sing N N 257 
LYS CB  HB2  sing N N 258 
LYS CB  HB3  sing N N 259 
LYS CG  CD   sing N N 260 
LYS CG  HG2  sing N N 261 
LYS CG  HG3  sing N N 262 
LYS CD  CE   sing N N 263 
LYS CD  HD2  sing N N 264 
LYS CD  HD3  sing N N 265 
LYS CE  NZ   sing N N 266 
LYS CE  HE2  sing N N 267 
LYS CE  HE3  sing N N 268 
LYS NZ  HZ1  sing N N 269 
LYS NZ  HZ2  sing N N 270 
LYS NZ  HZ3  sing N N 271 
LYS OXT HXT  sing N N 272 
MET N   CA   sing N N 273 
MET N   H    sing N N 274 
MET N   H2   sing N N 275 
MET CA  C    sing N N 276 
MET CA  CB   sing N N 277 
MET CA  HA   sing N N 278 
MET C   O    doub N N 279 
MET C   OXT  sing N N 280 
MET CB  CG   sing N N 281 
MET CB  HB2  sing N N 282 
MET CB  HB3  sing N N 283 
MET CG  SD   sing N N 284 
MET CG  HG2  sing N N 285 
MET CG  HG3  sing N N 286 
MET SD  CE   sing N N 287 
MET CE  HE1  sing N N 288 
MET CE  HE2  sing N N 289 
MET CE  HE3  sing N N 290 
MET OXT HXT  sing N N 291 
PHE N   CA   sing N N 292 
PHE N   H    sing N N 293 
PHE N   H2   sing N N 294 
PHE CA  C    sing N N 295 
PHE CA  CB   sing N N 296 
PHE CA  HA   sing N N 297 
PHE C   O    doub N N 298 
PHE C   OXT  sing N N 299 
PHE CB  CG   sing N N 300 
PHE CB  HB2  sing N N 301 
PHE CB  HB3  sing N N 302 
PHE CG  CD1  doub Y N 303 
PHE CG  CD2  sing Y N 304 
PHE CD1 CE1  sing Y N 305 
PHE CD1 HD1  sing N N 306 
PHE CD2 CE2  doub Y N 307 
PHE CD2 HD2  sing N N 308 
PHE CE1 CZ   doub Y N 309 
PHE CE1 HE1  sing N N 310 
PHE CE2 CZ   sing Y N 311 
PHE CE2 HE2  sing N N 312 
PHE CZ  HZ   sing N N 313 
PHE OXT HXT  sing N N 314 
PRO N   CA   sing N N 315 
PRO N   CD   sing N N 316 
PRO N   H    sing N N 317 
PRO CA  C    sing N N 318 
PRO CA  CB   sing N N 319 
PRO CA  HA   sing N N 320 
PRO C   O    doub N N 321 
PRO C   OXT  sing N N 322 
PRO CB  CG   sing N N 323 
PRO CB  HB2  sing N N 324 
PRO CB  HB3  sing N N 325 
PRO CG  CD   sing N N 326 
PRO CG  HG2  sing N N 327 
PRO CG  HG3  sing N N 328 
PRO CD  HD2  sing N N 329 
PRO CD  HD3  sing N N 330 
PRO OXT HXT  sing N N 331 
SER N   CA   sing N N 332 
SER N   H    sing N N 333 
SER N   H2   sing N N 334 
SER CA  C    sing N N 335 
SER CA  CB   sing N N 336 
SER CA  HA   sing N N 337 
SER C   O    doub N N 338 
SER C   OXT  sing N N 339 
SER CB  OG   sing N N 340 
SER CB  HB2  sing N N 341 
SER CB  HB3  sing N N 342 
SER OG  HG   sing N N 343 
SER OXT HXT  sing N N 344 
THR N   CA   sing N N 345 
THR N   H    sing N N 346 
THR N   H2   sing N N 347 
THR CA  C    sing N N 348 
THR CA  CB   sing N N 349 
THR CA  HA   sing N N 350 
THR C   O    doub N N 351 
THR C   OXT  sing N N 352 
THR CB  OG1  sing N N 353 
THR CB  CG2  sing N N 354 
THR CB  HB   sing N N 355 
THR OG1 HG1  sing N N 356 
THR CG2 HG21 sing N N 357 
THR CG2 HG22 sing N N 358 
THR CG2 HG23 sing N N 359 
THR OXT HXT  sing N N 360 
TRP N   CA   sing N N 361 
TRP N   H    sing N N 362 
TRP N   H2   sing N N 363 
TRP CA  C    sing N N 364 
TRP CA  CB   sing N N 365 
TRP CA  HA   sing N N 366 
TRP C   O    doub N N 367 
TRP C   OXT  sing N N 368 
TRP CB  CG   sing N N 369 
TRP CB  HB2  sing N N 370 
TRP CB  HB3  sing N N 371 
TRP CG  CD1  doub Y N 372 
TRP CG  CD2  sing Y N 373 
TRP CD1 NE1  sing Y N 374 
TRP CD1 HD1  sing N N 375 
TRP CD2 CE2  doub Y N 376 
TRP CD2 CE3  sing Y N 377 
TRP NE1 CE2  sing Y N 378 
TRP NE1 HE1  sing N N 379 
TRP CE2 CZ2  sing Y N 380 
TRP CE3 CZ3  doub Y N 381 
TRP CE3 HE3  sing N N 382 
TRP CZ2 CH2  doub Y N 383 
TRP CZ2 HZ2  sing N N 384 
TRP CZ3 CH2  sing Y N 385 
TRP CZ3 HZ3  sing N N 386 
TRP CH2 HH2  sing N N 387 
TRP OXT HXT  sing N N 388 
TYR N   CA   sing N N 389 
TYR N   H    sing N N 390 
TYR N   H2   sing N N 391 
TYR CA  C    sing N N 392 
TYR CA  CB   sing N N 393 
TYR CA  HA   sing N N 394 
TYR C   O    doub N N 395 
TYR C   OXT  sing N N 396 
TYR CB  CG   sing N N 397 
TYR CB  HB2  sing N N 398 
TYR CB  HB3  sing N N 399 
TYR CG  CD1  doub Y N 400 
TYR CG  CD2  sing Y N 401 
TYR CD1 CE1  sing Y N 402 
TYR CD1 HD1  sing N N 403 
TYR CD2 CE2  doub Y N 404 
TYR CD2 HD2  sing N N 405 
TYR CE1 CZ   doub Y N 406 
TYR CE1 HE1  sing N N 407 
TYR CE2 CZ   sing Y N 408 
TYR CE2 HE2  sing N N 409 
TYR CZ  OH   sing N N 410 
TYR OH  HH   sing N N 411 
TYR OXT HXT  sing N N 412 
VAL N   CA   sing N N 413 
VAL N   H    sing N N 414 
VAL N   H2   sing N N 415 
VAL CA  C    sing N N 416 
VAL CA  CB   sing N N 417 
VAL CA  HA   sing N N 418 
VAL C   O    doub N N 419 
VAL C   OXT  sing N N 420 
VAL CB  CG1  sing N N 421 
VAL CB  CG2  sing N N 422 
VAL CB  HB   sing N N 423 
VAL CG1 HG11 sing N N 424 
VAL CG1 HG12 sing N N 425 
VAL CG1 HG13 sing N N 426 
VAL CG2 HG21 sing N N 427 
VAL CG2 HG22 sing N N 428 
VAL CG2 HG23 sing N N 429 
VAL OXT HXT  sing N N 430 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Indian Council of Medical Research'              India 'Indian Council of Medical Research (ICMR),' 1 
'Department of Science & Technology (DST, India)' India 'DST-FIST: SR/FST/LS-I/2017(C)'              2 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        I2G 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   I2G 
_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 '(2~{E},4~{E},6~{S})-4,6-dimethyldeca-2,4-dienoic acid' I2G 
5 'DIMETHYL SULFOXIDE'                                    DMS 
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   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
