data_9BXN
# 
_entry.id   9BXN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BXN         pdb_00009bxn 10.2210/pdb9bxn/pdb 
WWPDB D_1000281549 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-08 ? 
2 'Structure model' 1 1 2025-02-05 ? 
3 'Structure model' 1 2 2025-03-19 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_DOI'    
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation.year'                    
5 2 'Structure model' '_citation_author.identifier_ORCID' 
6 3 'Structure model' '_citation.journal_volume'          
7 3 'Structure model' '_citation.page_first'              
8 3 'Structure model' '_citation.page_last'               
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BXN 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              katherine.davis@emory.edu 
_pdbx_contact_author.name_first         Katherine 
_pdbx_contact_author.name_last          Davis 
_pdbx_contact_author.name_mi            M 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0258-8907 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ireland, K.A.' 1 0000-0003-0986-5142 
'Davis, K.M.'   2 0000-0002-0258-8907 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                528 
_citation.page_last                 538.e5 
_citation.title                     
'Structural and functional analysis of SAM-dependent N-methyltransferases involved in ovoselenol and ovothiol biosynthesis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2024.12.020 
_citation.pdbx_database_id_PubMed   39862859 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ireland, K.A.'        1 ? 
primary 'Kayrouz, C.M.'        2 ? 
primary 'Abbott, M.L.'         3 ? 
primary 'Seyedsayamdost, M.R.' 4 ? 
primary 'Davis, K.M.'          5 ? 
# 
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 '5-thiohistidine N-methyltransferase OvoM' 31352.225 2   ? ? ? ? 
2 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE                  384.411   2   ? ? ? ? 
3 non-polymer syn 5-sulfanyl-L-histidine                     187.220   1   ? ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                             62.068    11  ? ? ? ? 
5 water       nat water                                      18.015    400 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMIFKEKNIYETDESVSQYCDFQYGEDCFGVLNFALACATKAIGYTKETPKNRALDLGCAT
GRASFELARSYKHVDGVDYSQAFVDAATELQKNGCIGYSQNGEGELKNYKVIDREGYAFRDSFTKVEFFQGDACNLTPQF
KEYDLIMATNLIDRLYEPRLFLENIHKRINEKGYLILTSPYTWREEYTAKKFWIGGYVDENGKEVSTLEGLKEILEIHFE
LVATEDIPFVIRETSRKFQHTISQMSVWKVIST
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMIFKEKNIYETDESVSQYCDFQYGEDCFGVLNFALACATKAIGYTKETPKNRALDLGCAT
GRASFELARSYKHVDGVDYSQAFVDAATELQKNGCIGYSQNGEGELKNYKVIDREGYAFRDSFTKVEFFQGDACNLTPQF
KEYDLIMATNLIDRLYEPRLFLENIHKRINEKGYLILTSPYTWREEYTAKKFWIGGYVDENGKEVSTLEGLKEILEIHFE
LVATEDIPFVIRETSRKFQHTISQMSVWKVIST
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 S-ADENOSYL-L-HOMOCYSTEINE SAH   
3 5-sulfanyl-L-histidine    A1ASZ 
4 1,2-ETHANEDIOL            EDO   
5 water                     HOH   
# 
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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ILE n 
1 23  PHE n 
1 24  LYS n 
1 25  GLU n 
1 26  LYS n 
1 27  ASN n 
1 28  ILE n 
1 29  TYR n 
1 30  GLU n 
1 31  THR n 
1 32  ASP n 
1 33  GLU n 
1 34  SER n 
1 35  VAL n 
1 36  SER n 
1 37  GLN n 
1 38  TYR n 
1 39  CYS n 
1 40  ASP n 
1 41  PHE n 
1 42  GLN n 
1 43  TYR n 
1 44  GLY n 
1 45  GLU n 
1 46  ASP n 
1 47  CYS n 
1 48  PHE n 
1 49  GLY n 
1 50  VAL n 
1 51  LEU n 
1 52  ASN n 
1 53  PHE n 
1 54  ALA n 
1 55  LEU n 
1 56  ALA n 
1 57  CYS n 
1 58  ALA n 
1 59  THR n 
1 60  LYS n 
1 61  ALA n 
1 62  ILE n 
1 63  GLY n 
1 64  TYR n 
1 65  THR n 
1 66  LYS n 
1 67  GLU n 
1 68  THR n 
1 69  PRO n 
1 70  LYS n 
1 71  ASN n 
1 72  ARG n 
1 73  ALA n 
1 74  LEU n 
1 75  ASP n 
1 76  LEU n 
1 77  GLY n 
1 78  CYS n 
1 79  ALA n 
1 80  THR n 
1 81  GLY n 
1 82  ARG n 
1 83  ALA n 
1 84  SER n 
1 85  PHE n 
1 86  GLU n 
1 87  LEU n 
1 88  ALA n 
1 89  ARG n 
1 90  SER n 
1 91  TYR n 
1 92  LYS n 
1 93  HIS n 
1 94  VAL n 
1 95  ASP n 
1 96  GLY n 
1 97  VAL n 
1 98  ASP n 
1 99  TYR n 
1 100 SER n 
1 101 GLN n 
1 102 ALA n 
1 103 PHE n 
1 104 VAL n 
1 105 ASP n 
1 106 ALA n 
1 107 ALA n 
1 108 THR n 
1 109 GLU n 
1 110 LEU n 
1 111 GLN n 
1 112 LYS n 
1 113 ASN n 
1 114 GLY n 
1 115 CYS n 
1 116 ILE n 
1 117 GLY n 
1 118 TYR n 
1 119 SER n 
1 120 GLN n 
1 121 ASN n 
1 122 GLY n 
1 123 GLU n 
1 124 GLY n 
1 125 GLU n 
1 126 LEU n 
1 127 LYS n 
1 128 ASN n 
1 129 TYR n 
1 130 LYS n 
1 131 VAL n 
1 132 ILE n 
1 133 ASP n 
1 134 ARG n 
1 135 GLU n 
1 136 GLY n 
1 137 TYR n 
1 138 ALA n 
1 139 PHE n 
1 140 ARG n 
1 141 ASP n 
1 142 SER n 
1 143 PHE n 
1 144 THR n 
1 145 LYS n 
1 146 VAL n 
1 147 GLU n 
1 148 PHE n 
1 149 PHE n 
1 150 GLN n 
1 151 GLY n 
1 152 ASP n 
1 153 ALA n 
1 154 CYS n 
1 155 ASN n 
1 156 LEU n 
1 157 THR n 
1 158 PRO n 
1 159 GLN n 
1 160 PHE n 
1 161 LYS n 
1 162 GLU n 
1 163 TYR n 
1 164 ASP n 
1 165 LEU n 
1 166 ILE n 
1 167 MET n 
1 168 ALA n 
1 169 THR n 
1 170 ASN n 
1 171 LEU n 
1 172 ILE n 
1 173 ASP n 
1 174 ARG n 
1 175 LEU n 
1 176 TYR n 
1 177 GLU n 
1 178 PRO n 
1 179 ARG n 
1 180 LEU n 
1 181 PHE n 
1 182 LEU n 
1 183 GLU n 
1 184 ASN n 
1 185 ILE n 
1 186 HIS n 
1 187 LYS n 
1 188 ARG n 
1 189 ILE n 
1 190 ASN n 
1 191 GLU n 
1 192 LYS n 
1 193 GLY n 
1 194 TYR n 
1 195 LEU n 
1 196 ILE n 
1 197 LEU n 
1 198 THR n 
1 199 SER n 
1 200 PRO n 
1 201 TYR n 
1 202 THR n 
1 203 TRP n 
1 204 ARG n 
1 205 GLU n 
1 206 GLU n 
1 207 TYR n 
1 208 THR n 
1 209 ALA n 
1 210 LYS n 
1 211 LYS n 
1 212 PHE n 
1 213 TRP n 
1 214 ILE n 
1 215 GLY n 
1 216 GLY n 
1 217 TYR n 
1 218 VAL n 
1 219 ASP n 
1 220 GLU n 
1 221 ASN n 
1 222 GLY n 
1 223 LYS n 
1 224 GLU n 
1 225 VAL n 
1 226 SER n 
1 227 THR n 
1 228 LEU n 
1 229 GLU n 
1 230 GLY n 
1 231 LEU n 
1 232 LYS n 
1 233 GLU n 
1 234 ILE n 
1 235 LEU n 
1 236 GLU n 
1 237 ILE n 
1 238 HIS n 
1 239 PHE n 
1 240 GLU n 
1 241 LEU n 
1 242 VAL n 
1 243 ALA n 
1 244 THR n 
1 245 GLU n 
1 246 ASP n 
1 247 ILE n 
1 248 PRO n 
1 249 PHE n 
1 250 VAL n 
1 251 ILE n 
1 252 ARG n 
1 253 GLU n 
1 254 THR n 
1 255 SER n 
1 256 ARG n 
1 257 LYS n 
1 258 PHE n 
1 259 GLN n 
1 260 HIS n 
1 261 THR n 
1 262 ILE n 
1 263 SER n 
1 264 GLN n 
1 265 MET n 
1 266 SER n 
1 267 VAL n 
1 268 TRP n 
1 269 LYS n 
1 270 VAL n 
1 271 ILE n 
1 272 SER n 
1 273 THR 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                   273 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    STB_99 
_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      'Sulfuricurvum sp.' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2025608 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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                   ? 
# 
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 
A1ASZ 'L-peptide linking' n 5-sulfanyl-L-histidine    ?                 'C6 H9 N3 O2 S'   187.220 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL            'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
GLN   'L-peptide linking' y GLUTAMINE                 ?                 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'           ?                 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                   ?                 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                 ?                 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                     ?                 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                ?                 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                   ?                 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                    ?                 'C6 H15 N2 O2 1'  147.195 
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 
SAH   non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE ?                 'C14 H20 N6 O5 S' 384.411 
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 
# 
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   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  ILE 22  2   ?   ?   ?   A . n 
A 1 23  PHE 23  3   ?   ?   ?   A . n 
A 1 24  LYS 24  4   ?   ?   ?   A . n 
A 1 25  GLU 25  5   5   GLU GLU A . n 
A 1 26  LYS 26  6   6   LYS LYS A . n 
A 1 27  ASN 27  7   7   ASN ASN A . n 
A 1 28  ILE 28  8   8   ILE ILE A . n 
A 1 29  TYR 29  9   9   TYR TYR A . n 
A 1 30  GLU 30  10  10  GLU GLU A . n 
A 1 31  THR 31  11  11  THR THR A . n 
A 1 32  ASP 32  12  12  ASP ASP A . n 
A 1 33  GLU 33  13  13  GLU GLU A . n 
A 1 34  SER 34  14  14  SER SER A . n 
A 1 35  VAL 35  15  15  VAL VAL A . n 
A 1 36  SER 36  16  16  SER SER A . n 
A 1 37  GLN 37  17  17  GLN GLN A . n 
A 1 38  TYR 38  18  18  TYR TYR A . n 
A 1 39  CYS 39  19  19  CYS CYS A . n 
A 1 40  ASP 40  20  20  ASP ASP A . n 
A 1 41  PHE 41  21  21  PHE PHE A . n 
A 1 42  GLN 42  22  22  GLN GLN A . n 
A 1 43  TYR 43  23  23  TYR TYR A . n 
A 1 44  GLY 44  24  24  GLY GLY A . n 
A 1 45  GLU 45  25  25  GLU GLU A . n 
A 1 46  ASP 46  26  26  ASP ASP A . n 
A 1 47  CYS 47  27  27  CYS CYS A . n 
A 1 48  PHE 48  28  28  PHE PHE A . n 
A 1 49  GLY 49  29  29  GLY GLY A . n 
A 1 50  VAL 50  30  30  VAL VAL A . n 
A 1 51  LEU 51  31  31  LEU LEU A . n 
A 1 52  ASN 52  32  32  ASN ASN A . n 
A 1 53  PHE 53  33  33  PHE PHE A . n 
A 1 54  ALA 54  34  34  ALA ALA A . n 
A 1 55  LEU 55  35  35  LEU LEU A . n 
A 1 56  ALA 56  36  36  ALA ALA A . n 
A 1 57  CYS 57  37  37  CYS CYS A . n 
A 1 58  ALA 58  38  38  ALA ALA A . n 
A 1 59  THR 59  39  39  THR THR A . n 
A 1 60  LYS 60  40  40  LYS LYS A . n 
A 1 61  ALA 61  41  41  ALA ALA A . n 
A 1 62  ILE 62  42  42  ILE ILE A . n 
A 1 63  GLY 63  43  43  GLY GLY A . n 
A 1 64  TYR 64  44  44  TYR TYR A . n 
A 1 65  THR 65  45  45  THR THR A . n 
A 1 66  LYS 66  46  46  LYS LYS A . n 
A 1 67  GLU 67  47  47  GLU GLU A . n 
A 1 68  THR 68  48  48  THR THR A . n 
A 1 69  PRO 69  49  49  PRO PRO A . n 
A 1 70  LYS 70  50  50  LYS LYS A . n 
A 1 71  ASN 71  51  51  ASN ASN A . n 
A 1 72  ARG 72  52  52  ARG ARG A . n 
A 1 73  ALA 73  53  53  ALA ALA A . n 
A 1 74  LEU 74  54  54  LEU LEU A . n 
A 1 75  ASP 75  55  55  ASP ASP A . n 
A 1 76  LEU 76  56  56  LEU LEU A . n 
A 1 77  GLY 77  57  57  GLY GLY A . n 
A 1 78  CYS 78  58  58  CYS CYS A . n 
A 1 79  ALA 79  59  59  ALA ALA A . n 
A 1 80  THR 80  60  60  THR THR A . n 
A 1 81  GLY 81  61  61  GLY GLY A . n 
A 1 82  ARG 82  62  62  ARG ARG A . n 
A 1 83  ALA 83  63  63  ALA ALA A . n 
A 1 84  SER 84  64  64  SER SER A . n 
A 1 85  PHE 85  65  65  PHE PHE A . n 
A 1 86  GLU 86  66  66  GLU GLU A . n 
A 1 87  LEU 87  67  67  LEU LEU A . n 
A 1 88  ALA 88  68  68  ALA ALA A . n 
A 1 89  ARG 89  69  69  ARG ARG A . n 
A 1 90  SER 90  70  70  SER SER A . n 
A 1 91  TYR 91  71  71  TYR TYR A . n 
A 1 92  LYS 92  72  72  LYS LYS A . n 
A 1 93  HIS 93  73  73  HIS HIS A . n 
A 1 94  VAL 94  74  74  VAL VAL A . n 
A 1 95  ASP 95  75  75  ASP ASP A . n 
A 1 96  GLY 96  76  76  GLY GLY A . n 
A 1 97  VAL 97  77  77  VAL VAL A . n 
A 1 98  ASP 98  78  78  ASP ASP A . n 
A 1 99  TYR 99  79  79  TYR TYR A . n 
A 1 100 SER 100 80  80  SER SER A . n 
A 1 101 GLN 101 81  81  GLN GLN A . n 
A 1 102 ALA 102 82  82  ALA ALA A . n 
A 1 103 PHE 103 83  83  PHE PHE A . n 
A 1 104 VAL 104 84  84  VAL VAL A . n 
A 1 105 ASP 105 85  85  ASP ASP A . n 
A 1 106 ALA 106 86  86  ALA ALA A . n 
A 1 107 ALA 107 87  87  ALA ALA A . n 
A 1 108 THR 108 88  88  THR THR A . n 
A 1 109 GLU 109 89  89  GLU GLU A . n 
A 1 110 LEU 110 90  90  LEU LEU A . n 
A 1 111 GLN 111 91  91  GLN GLN A . n 
A 1 112 LYS 112 92  92  LYS LYS A . n 
A 1 113 ASN 113 93  93  ASN ASN A . n 
A 1 114 GLY 114 94  94  GLY GLY A . n 
A 1 115 CYS 115 95  95  CYS CYS A . n 
A 1 116 ILE 116 96  96  ILE ILE A . n 
A 1 117 GLY 117 97  97  GLY GLY A . n 
A 1 118 TYR 118 98  98  TYR TYR A . n 
A 1 119 SER 119 99  99  SER SER A . n 
A 1 120 GLN 120 100 100 GLN GLN A . n 
A 1 121 ASN 121 101 101 ASN ASN A . n 
A 1 122 GLY 122 102 102 GLY GLY A . n 
A 1 123 GLU 123 103 103 GLU GLU A . n 
A 1 124 GLY 124 104 104 GLY GLY A . n 
A 1 125 GLU 125 105 105 GLU GLU A . n 
A 1 126 LEU 126 106 106 LEU LEU A . n 
A 1 127 LYS 127 107 107 LYS LYS A . n 
A 1 128 ASN 128 108 108 ASN ASN A . n 
A 1 129 TYR 129 109 109 TYR TYR A . n 
A 1 130 LYS 130 110 110 LYS LYS A . n 
A 1 131 VAL 131 111 111 VAL VAL A . n 
A 1 132 ILE 132 112 112 ILE ILE A . n 
A 1 133 ASP 133 113 113 ASP ASP A . n 
A 1 134 ARG 134 114 114 ARG ARG A . n 
A 1 135 GLU 135 115 115 GLU GLU A . n 
A 1 136 GLY 136 116 116 GLY GLY A . n 
A 1 137 TYR 137 117 117 TYR TYR A . n 
A 1 138 ALA 138 118 118 ALA ALA A . n 
A 1 139 PHE 139 119 119 PHE PHE A . n 
A 1 140 ARG 140 120 120 ARG ARG A . n 
A 1 141 ASP 141 121 121 ASP ASP A . n 
A 1 142 SER 142 122 122 SER SER A . n 
A 1 143 PHE 143 123 123 PHE PHE A . n 
A 1 144 THR 144 124 124 THR THR A . n 
A 1 145 LYS 145 125 125 LYS LYS A . n 
A 1 146 VAL 146 126 126 VAL VAL A . n 
A 1 147 GLU 147 127 127 GLU GLU A . n 
A 1 148 PHE 148 128 128 PHE PHE A . n 
A 1 149 PHE 149 129 129 PHE PHE A . n 
A 1 150 GLN 150 130 130 GLN GLN A . n 
A 1 151 GLY 151 131 131 GLY GLY A . n 
A 1 152 ASP 152 132 132 ASP ASP A . n 
A 1 153 ALA 153 133 133 ALA ALA A . n 
A 1 154 CYS 154 134 134 CYS CYS A . n 
A 1 155 ASN 155 135 135 ASN ASN A . n 
A 1 156 LEU 156 136 136 LEU LEU A . n 
A 1 157 THR 157 137 137 THR THR A . n 
A 1 158 PRO 158 138 138 PRO PRO A . n 
A 1 159 GLN 159 139 139 GLN GLN A . n 
A 1 160 PHE 160 140 140 PHE PHE A . n 
A 1 161 LYS 161 141 141 LYS LYS A . n 
A 1 162 GLU 162 142 142 GLU GLU A . n 
A 1 163 TYR 163 143 143 TYR TYR A . n 
A 1 164 ASP 164 144 144 ASP ASP A . n 
A 1 165 LEU 165 145 145 LEU LEU A . n 
A 1 166 ILE 166 146 146 ILE ILE A . n 
A 1 167 MET 167 147 147 MET MET A . n 
A 1 168 ALA 168 148 148 ALA ALA A . n 
A 1 169 THR 169 149 149 THR THR A . n 
A 1 170 ASN 170 150 150 ASN ASN A . n 
A 1 171 LEU 171 151 151 LEU LEU A . n 
A 1 172 ILE 172 152 152 ILE ILE A . n 
A 1 173 ASP 173 153 153 ASP ASP A . n 
A 1 174 ARG 174 154 154 ARG ARG A . n 
A 1 175 LEU 175 155 155 LEU LEU A . n 
A 1 176 TYR 176 156 156 TYR TYR A . n 
A 1 177 GLU 177 157 157 GLU GLU A . n 
A 1 178 PRO 178 158 158 PRO PRO A . n 
A 1 179 ARG 179 159 159 ARG ARG A . n 
A 1 180 LEU 180 160 160 LEU LEU A . n 
A 1 181 PHE 181 161 161 PHE PHE A . n 
A 1 182 LEU 182 162 162 LEU LEU A . n 
A 1 183 GLU 183 163 163 GLU GLU A . n 
A 1 184 ASN 184 164 164 ASN ASN A . n 
A 1 185 ILE 185 165 165 ILE ILE A . n 
A 1 186 HIS 186 166 166 HIS HIS A . n 
A 1 187 LYS 187 167 167 LYS LYS A . n 
A 1 188 ARG 188 168 168 ARG ARG A . n 
A 1 189 ILE 189 169 169 ILE ILE A . n 
A 1 190 ASN 190 170 170 ASN ASN A . n 
A 1 191 GLU 191 171 171 GLU GLU A . n 
A 1 192 LYS 192 172 172 LYS LYS A . n 
A 1 193 GLY 193 173 173 GLY GLY A . n 
A 1 194 TYR 194 174 174 TYR TYR A . n 
A 1 195 LEU 195 175 175 LEU LEU A . n 
A 1 196 ILE 196 176 176 ILE ILE A . n 
A 1 197 LEU 197 177 177 LEU LEU A . n 
A 1 198 THR 198 178 178 THR THR A . n 
A 1 199 SER 199 179 179 SER SER A . n 
A 1 200 PRO 200 180 180 PRO PRO A . n 
A 1 201 TYR 201 181 181 TYR TYR A . n 
A 1 202 THR 202 182 182 THR THR A . n 
A 1 203 TRP 203 183 183 TRP TRP A . n 
A 1 204 ARG 204 184 184 ARG ARG A . n 
A 1 205 GLU 205 185 185 GLU GLU A . n 
A 1 206 GLU 206 186 186 GLU GLU A . n 
A 1 207 TYR 207 187 187 TYR TYR A . n 
A 1 208 THR 208 188 188 THR THR A . n 
A 1 209 ALA 209 189 189 ALA ALA A . n 
A 1 210 LYS 210 190 190 LYS LYS A . n 
A 1 211 LYS 211 191 191 LYS LYS A . n 
A 1 212 PHE 212 192 192 PHE PHE A . n 
A 1 213 TRP 213 193 193 TRP TRP A . n 
A 1 214 ILE 214 194 194 ILE ILE A . n 
A 1 215 GLY 215 195 195 GLY GLY A . n 
A 1 216 GLY 216 196 196 GLY GLY A . n 
A 1 217 TYR 217 197 197 TYR TYR A . n 
A 1 218 VAL 218 198 198 VAL VAL A . n 
A 1 219 ASP 219 199 199 ASP ASP A . n 
A 1 220 GLU 220 200 200 GLU GLU A . n 
A 1 221 ASN 221 201 201 ASN ASN A . n 
A 1 222 GLY 222 202 202 GLY GLY A . n 
A 1 223 LYS 223 203 203 LYS LYS A . n 
A 1 224 GLU 224 204 204 GLU GLU A . n 
A 1 225 VAL 225 205 205 VAL VAL A . n 
A 1 226 SER 226 206 206 SER SER A . n 
A 1 227 THR 227 207 207 THR THR A . n 
A 1 228 LEU 228 208 208 LEU LEU A . n 
A 1 229 GLU 229 209 209 GLU GLU A . n 
A 1 230 GLY 230 210 210 GLY GLY A . n 
A 1 231 LEU 231 211 211 LEU LEU A . n 
A 1 232 LYS 232 212 212 LYS LYS A . n 
A 1 233 GLU 233 213 213 GLU GLU A . n 
A 1 234 ILE 234 214 214 ILE ILE A . n 
A 1 235 LEU 235 215 215 LEU LEU A . n 
A 1 236 GLU 236 216 216 GLU GLU A . n 
A 1 237 ILE 237 217 217 ILE ILE A . n 
A 1 238 HIS 238 218 218 HIS HIS A . n 
A 1 239 PHE 239 219 219 PHE PHE A . n 
A 1 240 GLU 240 220 220 GLU GLU A . n 
A 1 241 LEU 241 221 221 LEU LEU A . n 
A 1 242 VAL 242 222 222 VAL VAL A . n 
A 1 243 ALA 243 223 223 ALA ALA A . n 
A 1 244 THR 244 224 224 THR THR A . n 
A 1 245 GLU 245 225 225 GLU GLU A . n 
A 1 246 ASP 246 226 226 ASP ASP A . n 
A 1 247 ILE 247 227 227 ILE ILE A . n 
A 1 248 PRO 248 228 228 PRO PRO A . n 
A 1 249 PHE 249 229 229 PHE PHE A . n 
A 1 250 VAL 250 230 230 VAL VAL A . n 
A 1 251 ILE 251 231 231 ILE ILE A . n 
A 1 252 ARG 252 232 232 ARG ARG A . n 
A 1 253 GLU 253 233 233 GLU GLU A . n 
A 1 254 THR 254 234 234 THR THR A . n 
A 1 255 SER 255 235 235 SER SER A . n 
A 1 256 ARG 256 236 236 ARG ARG A . n 
A 1 257 LYS 257 237 237 LYS LYS A . n 
A 1 258 PHE 258 238 238 PHE PHE A . n 
A 1 259 GLN 259 239 239 GLN GLN A . n 
A 1 260 HIS 260 240 240 HIS HIS A . n 
A 1 261 THR 261 241 241 THR THR A . n 
A 1 262 ILE 262 242 242 ILE ILE A . n 
A 1 263 SER 263 243 243 SER SER A . n 
A 1 264 GLN 264 244 244 GLN GLN A . n 
A 1 265 MET 265 245 245 MET MET A . n 
A 1 266 SER 266 246 246 SER SER A . n 
A 1 267 VAL 267 247 247 VAL VAL A . n 
A 1 268 TRP 268 248 248 TRP TRP A . n 
A 1 269 LYS 269 249 249 LYS LYS A . n 
A 1 270 VAL 270 250 250 VAL VAL A . n 
A 1 271 ILE 271 251 251 ILE ILE A . n 
A 1 272 SER 272 252 ?   ?   ?   A . n 
A 1 273 THR 273 253 ?   ?   ?   A . n 
B 1 1   MET 1   -19 ?   ?   ?   B . n 
B 1 2   GLY 2   -18 ?   ?   ?   B . n 
B 1 3   SER 3   -17 ?   ?   ?   B . n 
B 1 4   SER 4   -16 ?   ?   ?   B . n 
B 1 5   HIS 5   -15 ?   ?   ?   B . n 
B 1 6   HIS 6   -14 ?   ?   ?   B . n 
B 1 7   HIS 7   -13 ?   ?   ?   B . n 
B 1 8   HIS 8   -12 ?   ?   ?   B . n 
B 1 9   HIS 9   -11 ?   ?   ?   B . n 
B 1 10  HIS 10  -10 ?   ?   ?   B . n 
B 1 11  SER 11  -9  ?   ?   ?   B . n 
B 1 12  SER 12  -8  ?   ?   ?   B . n 
B 1 13  GLY 13  -7  ?   ?   ?   B . n 
B 1 14  LEU 14  -6  ?   ?   ?   B . n 
B 1 15  VAL 15  -5  ?   ?   ?   B . n 
B 1 16  PRO 16  -4  ?   ?   ?   B . n 
B 1 17  ARG 17  -3  ?   ?   ?   B . n 
B 1 18  GLY 18  -2  ?   ?   ?   B . n 
B 1 19  SER 19  -1  ?   ?   ?   B . n 
B 1 20  HIS 20  0   ?   ?   ?   B . n 
B 1 21  MET 21  1   ?   ?   ?   B . n 
B 1 22  ILE 22  2   ?   ?   ?   B . n 
B 1 23  PHE 23  3   ?   ?   ?   B . n 
B 1 24  LYS 24  4   ?   ?   ?   B . n 
B 1 25  GLU 25  5   ?   ?   ?   B . n 
B 1 26  LYS 26  6   ?   ?   ?   B . n 
B 1 27  ASN 27  7   7   ASN ASN B . n 
B 1 28  ILE 28  8   8   ILE ILE B . n 
B 1 29  TYR 29  9   9   TYR TYR B . n 
B 1 30  GLU 30  10  10  GLU GLU B . n 
B 1 31  THR 31  11  11  THR THR B . n 
B 1 32  ASP 32  12  12  ASP ASP B . n 
B 1 33  GLU 33  13  13  GLU GLU B . n 
B 1 34  SER 34  14  14  SER SER B . n 
B 1 35  VAL 35  15  15  VAL VAL B . n 
B 1 36  SER 36  16  16  SER SER B . n 
B 1 37  GLN 37  17  17  GLN GLN B . n 
B 1 38  TYR 38  18  18  TYR TYR B . n 
B 1 39  CYS 39  19  19  CYS CYS B . n 
B 1 40  ASP 40  20  20  ASP ASP B . n 
B 1 41  PHE 41  21  21  PHE PHE B . n 
B 1 42  GLN 42  22  22  GLN GLN B . n 
B 1 43  TYR 43  23  23  TYR TYR B . n 
B 1 44  GLY 44  24  24  GLY GLY B . n 
B 1 45  GLU 45  25  25  GLU GLU B . n 
B 1 46  ASP 46  26  26  ASP ASP B . n 
B 1 47  CYS 47  27  27  CYS CYS B . n 
B 1 48  PHE 48  28  28  PHE PHE B . n 
B 1 49  GLY 49  29  29  GLY GLY B . n 
B 1 50  VAL 50  30  30  VAL VAL B . n 
B 1 51  LEU 51  31  31  LEU LEU B . n 
B 1 52  ASN 52  32  32  ASN ASN B . n 
B 1 53  PHE 53  33  33  PHE PHE B . n 
B 1 54  ALA 54  34  34  ALA ALA B . n 
B 1 55  LEU 55  35  35  LEU LEU B . n 
B 1 56  ALA 56  36  36  ALA ALA B . n 
B 1 57  CYS 57  37  37  CYS CYS B . n 
B 1 58  ALA 58  38  38  ALA ALA B . n 
B 1 59  THR 59  39  39  THR THR B . n 
B 1 60  LYS 60  40  40  LYS LYS B . n 
B 1 61  ALA 61  41  41  ALA ALA B . n 
B 1 62  ILE 62  42  42  ILE ILE B . n 
B 1 63  GLY 63  43  43  GLY GLY B . n 
B 1 64  TYR 64  44  44  TYR TYR B . n 
B 1 65  THR 65  45  45  THR THR B . n 
B 1 66  LYS 66  46  46  LYS LYS B . n 
B 1 67  GLU 67  47  47  GLU GLU B . n 
B 1 68  THR 68  48  48  THR THR B . n 
B 1 69  PRO 69  49  49  PRO PRO B . n 
B 1 70  LYS 70  50  50  LYS LYS B . n 
B 1 71  ASN 71  51  51  ASN ASN B . n 
B 1 72  ARG 72  52  52  ARG ARG B . n 
B 1 73  ALA 73  53  53  ALA ALA B . n 
B 1 74  LEU 74  54  54  LEU LEU B . n 
B 1 75  ASP 75  55  55  ASP ASP B . n 
B 1 76  LEU 76  56  56  LEU LEU B . n 
B 1 77  GLY 77  57  57  GLY GLY B . n 
B 1 78  CYS 78  58  58  CYS CYS B . n 
B 1 79  ALA 79  59  59  ALA ALA B . n 
B 1 80  THR 80  60  60  THR THR B . n 
B 1 81  GLY 81  61  61  GLY GLY B . n 
B 1 82  ARG 82  62  62  ARG ARG B . n 
B 1 83  ALA 83  63  63  ALA ALA B . n 
B 1 84  SER 84  64  64  SER SER B . n 
B 1 85  PHE 85  65  65  PHE PHE B . n 
B 1 86  GLU 86  66  66  GLU GLU B . n 
B 1 87  LEU 87  67  67  LEU LEU B . n 
B 1 88  ALA 88  68  68  ALA ALA B . n 
B 1 89  ARG 89  69  69  ARG ARG B . n 
B 1 90  SER 90  70  70  SER SER B . n 
B 1 91  TYR 91  71  71  TYR TYR B . n 
B 1 92  LYS 92  72  72  LYS LYS B . n 
B 1 93  HIS 93  73  73  HIS HIS B . n 
B 1 94  VAL 94  74  74  VAL VAL B . n 
B 1 95  ASP 95  75  75  ASP ASP B . n 
B 1 96  GLY 96  76  76  GLY GLY B . n 
B 1 97  VAL 97  77  77  VAL VAL B . n 
B 1 98  ASP 98  78  78  ASP ASP B . n 
B 1 99  TYR 99  79  79  TYR TYR B . n 
B 1 100 SER 100 80  80  SER SER B . n 
B 1 101 GLN 101 81  81  GLN GLN B . n 
B 1 102 ALA 102 82  82  ALA ALA B . n 
B 1 103 PHE 103 83  83  PHE PHE B . n 
B 1 104 VAL 104 84  84  VAL VAL B . n 
B 1 105 ASP 105 85  85  ASP ASP B . n 
B 1 106 ALA 106 86  86  ALA ALA B . n 
B 1 107 ALA 107 87  87  ALA ALA B . n 
B 1 108 THR 108 88  88  THR THR B . n 
B 1 109 GLU 109 89  89  GLU GLU B . n 
B 1 110 LEU 110 90  90  LEU LEU B . n 
B 1 111 GLN 111 91  91  GLN GLN B . n 
B 1 112 LYS 112 92  92  LYS LYS B . n 
B 1 113 ASN 113 93  93  ASN ASN B . n 
B 1 114 GLY 114 94  94  GLY GLY B . n 
B 1 115 CYS 115 95  95  CYS CYS B . n 
B 1 116 ILE 116 96  96  ILE ILE B . n 
B 1 117 GLY 117 97  97  GLY GLY B . n 
B 1 118 TYR 118 98  98  TYR TYR B . n 
B 1 119 SER 119 99  99  SER SER B . n 
B 1 120 GLN 120 100 100 GLN GLN B . n 
B 1 121 ASN 121 101 101 ASN ASN B . n 
B 1 122 GLY 122 102 102 GLY GLY B . n 
B 1 123 GLU 123 103 103 GLU GLU B . n 
B 1 124 GLY 124 104 104 GLY GLY B . n 
B 1 125 GLU 125 105 105 GLU GLU B . n 
B 1 126 LEU 126 106 106 LEU LEU B . n 
B 1 127 LYS 127 107 107 LYS LYS B . n 
B 1 128 ASN 128 108 108 ASN ASN B . n 
B 1 129 TYR 129 109 109 TYR TYR B . n 
B 1 130 LYS 130 110 110 LYS LYS B . n 
B 1 131 VAL 131 111 111 VAL VAL B . n 
B 1 132 ILE 132 112 112 ILE ILE B . n 
B 1 133 ASP 133 113 113 ASP ASP B . n 
B 1 134 ARG 134 114 114 ARG ARG B . n 
B 1 135 GLU 135 115 115 GLU GLU B . n 
B 1 136 GLY 136 116 116 GLY GLY B . n 
B 1 137 TYR 137 117 117 TYR TYR B . n 
B 1 138 ALA 138 118 118 ALA ALA B . n 
B 1 139 PHE 139 119 119 PHE PHE B . n 
B 1 140 ARG 140 120 120 ARG ARG B . n 
B 1 141 ASP 141 121 121 ASP ASP B . n 
B 1 142 SER 142 122 122 SER SER B . n 
B 1 143 PHE 143 123 123 PHE PHE B . n 
B 1 144 THR 144 124 124 THR THR B . n 
B 1 145 LYS 145 125 125 LYS LYS B . n 
B 1 146 VAL 146 126 126 VAL VAL B . n 
B 1 147 GLU 147 127 127 GLU GLU B . n 
B 1 148 PHE 148 128 128 PHE PHE B . n 
B 1 149 PHE 149 129 129 PHE PHE B . n 
B 1 150 GLN 150 130 130 GLN GLN B . n 
B 1 151 GLY 151 131 131 GLY GLY B . n 
B 1 152 ASP 152 132 132 ASP ASP B . n 
B 1 153 ALA 153 133 133 ALA ALA B . n 
B 1 154 CYS 154 134 134 CYS CYS B . n 
B 1 155 ASN 155 135 135 ASN ASN B . n 
B 1 156 LEU 156 136 136 LEU LEU B . n 
B 1 157 THR 157 137 137 THR THR B . n 
B 1 158 PRO 158 138 138 PRO PRO B . n 
B 1 159 GLN 159 139 139 GLN GLN B . n 
B 1 160 PHE 160 140 140 PHE PHE B . n 
B 1 161 LYS 161 141 141 LYS LYS B . n 
B 1 162 GLU 162 142 142 GLU GLU B . n 
B 1 163 TYR 163 143 143 TYR TYR B . n 
B 1 164 ASP 164 144 144 ASP ASP B . n 
B 1 165 LEU 165 145 145 LEU LEU B . n 
B 1 166 ILE 166 146 146 ILE ILE B . n 
B 1 167 MET 167 147 147 MET MET B . n 
B 1 168 ALA 168 148 148 ALA ALA B . n 
B 1 169 THR 169 149 149 THR THR B . n 
B 1 170 ASN 170 150 150 ASN ASN B . n 
B 1 171 LEU 171 151 151 LEU LEU B . n 
B 1 172 ILE 172 152 152 ILE ILE B . n 
B 1 173 ASP 173 153 153 ASP ASP B . n 
B 1 174 ARG 174 154 154 ARG ARG B . n 
B 1 175 LEU 175 155 155 LEU LEU B . n 
B 1 176 TYR 176 156 156 TYR TYR B . n 
B 1 177 GLU 177 157 157 GLU GLU B . n 
B 1 178 PRO 178 158 158 PRO PRO B . n 
B 1 179 ARG 179 159 159 ARG ARG B . n 
B 1 180 LEU 180 160 160 LEU LEU B . n 
B 1 181 PHE 181 161 161 PHE PHE B . n 
B 1 182 LEU 182 162 162 LEU LEU B . n 
B 1 183 GLU 183 163 163 GLU GLU B . n 
B 1 184 ASN 184 164 164 ASN ASN B . n 
B 1 185 ILE 185 165 165 ILE ILE B . n 
B 1 186 HIS 186 166 166 HIS HIS B . n 
B 1 187 LYS 187 167 167 LYS LYS B . n 
B 1 188 ARG 188 168 168 ARG ARG B . n 
B 1 189 ILE 189 169 169 ILE ILE B . n 
B 1 190 ASN 190 170 170 ASN ASN B . n 
B 1 191 GLU 191 171 171 GLU GLU B . n 
B 1 192 LYS 192 172 172 LYS LYS B . n 
B 1 193 GLY 193 173 173 GLY GLY B . n 
B 1 194 TYR 194 174 174 TYR TYR B . n 
B 1 195 LEU 195 175 175 LEU LEU B . n 
B 1 196 ILE 196 176 176 ILE ILE B . n 
B 1 197 LEU 197 177 177 LEU LEU B . n 
B 1 198 THR 198 178 178 THR THR B . n 
B 1 199 SER 199 179 179 SER SER B . n 
B 1 200 PRO 200 180 180 PRO PRO B . n 
B 1 201 TYR 201 181 181 TYR TYR B . n 
B 1 202 THR 202 182 182 THR THR B . n 
B 1 203 TRP 203 183 183 TRP TRP B . n 
B 1 204 ARG 204 184 184 ARG ARG B . n 
B 1 205 GLU 205 185 185 GLU GLU B . n 
B 1 206 GLU 206 186 186 GLU GLU B . n 
B 1 207 TYR 207 187 187 TYR TYR B . n 
B 1 208 THR 208 188 188 THR THR B . n 
B 1 209 ALA 209 189 189 ALA ALA B . n 
B 1 210 LYS 210 190 190 LYS LYS B . n 
B 1 211 LYS 211 191 191 LYS LYS B . n 
B 1 212 PHE 212 192 192 PHE PHE B . n 
B 1 213 TRP 213 193 193 TRP TRP B . n 
B 1 214 ILE 214 194 194 ILE ILE B . n 
B 1 215 GLY 215 195 195 GLY GLY B . n 
B 1 216 GLY 216 196 196 GLY GLY B . n 
B 1 217 TYR 217 197 197 TYR TYR B . n 
B 1 218 VAL 218 198 198 VAL VAL B . n 
B 1 219 ASP 219 199 199 ASP ASP B . n 
B 1 220 GLU 220 200 200 GLU GLU B . n 
B 1 221 ASN 221 201 201 ASN ASN B . n 
B 1 222 GLY 222 202 202 GLY GLY B . n 
B 1 223 LYS 223 203 203 LYS LYS B . n 
B 1 224 GLU 224 204 204 GLU GLU B . n 
B 1 225 VAL 225 205 205 VAL VAL B . n 
B 1 226 SER 226 206 206 SER SER B . n 
B 1 227 THR 227 207 207 THR THR B . n 
B 1 228 LEU 228 208 208 LEU LEU B . n 
B 1 229 GLU 229 209 209 GLU GLU B . n 
B 1 230 GLY 230 210 210 GLY GLY B . n 
B 1 231 LEU 231 211 211 LEU LEU B . n 
B 1 232 LYS 232 212 212 LYS LYS B . n 
B 1 233 GLU 233 213 213 GLU GLU B . n 
B 1 234 ILE 234 214 214 ILE ILE B . n 
B 1 235 LEU 235 215 215 LEU LEU B . n 
B 1 236 GLU 236 216 216 GLU GLU B . n 
B 1 237 ILE 237 217 217 ILE ILE B . n 
B 1 238 HIS 238 218 218 HIS HIS B . n 
B 1 239 PHE 239 219 219 PHE PHE B . n 
B 1 240 GLU 240 220 220 GLU GLU B . n 
B 1 241 LEU 241 221 221 LEU LEU B . n 
B 1 242 VAL 242 222 222 VAL VAL B . n 
B 1 243 ALA 243 223 223 ALA ALA B . n 
B 1 244 THR 244 224 224 THR THR B . n 
B 1 245 GLU 245 225 225 GLU GLU B . n 
B 1 246 ASP 246 226 226 ASP ASP B . n 
B 1 247 ILE 247 227 227 ILE ILE B . n 
B 1 248 PRO 248 228 228 PRO PRO B . n 
B 1 249 PHE 249 229 229 PHE PHE B . n 
B 1 250 VAL 250 230 230 VAL VAL B . n 
B 1 251 ILE 251 231 231 ILE ILE B . n 
B 1 252 ARG 252 232 232 ARG ARG B . n 
B 1 253 GLU 253 233 233 GLU GLU B . n 
B 1 254 THR 254 234 234 THR THR B . n 
B 1 255 SER 255 235 235 SER SER B . n 
B 1 256 ARG 256 236 236 ARG ARG B . n 
B 1 257 LYS 257 237 237 LYS LYS B . n 
B 1 258 PHE 258 238 238 PHE PHE B . n 
B 1 259 GLN 259 239 239 GLN GLN B . n 
B 1 260 HIS 260 240 240 HIS HIS B . n 
B 1 261 THR 261 241 241 THR THR B . n 
B 1 262 ILE 262 242 242 ILE ILE B . n 
B 1 263 SER 263 243 243 SER SER B . n 
B 1 264 GLN 264 244 244 GLN GLN B . n 
B 1 265 MET 265 245 245 MET MET B . n 
B 1 266 SER 266 246 246 SER SER B . n 
B 1 267 VAL 267 247 247 VAL VAL B . n 
B 1 268 TRP 268 248 248 TRP TRP B . n 
B 1 269 LYS 269 249 249 LYS LYS B . n 
B 1 270 VAL 270 250 250 VAL VAL B . n 
B 1 271 ILE 271 251 251 ILE ILE B . n 
B 1 272 SER 272 252 ?   ?   ?   B . n 
B 1 273 THR 273 253 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1ASZ ? ? A1ASZ ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SAH   ? ? SAH   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SAH   1   401 401 SAH   SAH A . 
D 3 A1ASZ 1   402 402 A1ASZ HI7 A . 
E 4 EDO   1   403 501 EDO   EDO A . 
F 4 EDO   1   404 502 EDO   EDO A . 
G 4 EDO   1   405 1   EDO   EDO A . 
H 4 EDO   1   406 3   EDO   EDO A . 
I 4 EDO   1   407 10  EDO   EDO A . 
J 4 EDO   1   408 11  EDO   EDO A . 
K 4 EDO   1   409 12  EDO   EDO A . 
L 4 EDO   1   410 13  EDO   EDO A . 
M 2 SAH   1   301 301 SAH   SAH B . 
N 4 EDO   1   302 5   EDO   EDO B . 
O 4 EDO   1   303 6   EDO   EDO B . 
P 4 EDO   1   304 7   EDO   EDO B . 
Q 5 HOH   1   501 307 HOH   HOH A . 
Q 5 HOH   2   502 431 HOH   HOH A . 
Q 5 HOH   3   503 408 HOH   HOH A . 
Q 5 HOH   4   504 49  HOH   HOH A . 
Q 5 HOH   5   505 86  HOH   HOH A . 
Q 5 HOH   6   506 66  HOH   HOH A . 
Q 5 HOH   7   507 3   HOH   HOH A . 
Q 5 HOH   8   508 216 HOH   HOH A . 
Q 5 HOH   9   509 164 HOH   HOH A . 
Q 5 HOH   10  510 11  HOH   HOH A . 
Q 5 HOH   11  511 16  HOH   HOH A . 
Q 5 HOH   12  512 38  HOH   HOH A . 
Q 5 HOH   13  513 150 HOH   HOH A . 
Q 5 HOH   14  514 7   HOH   HOH A . 
Q 5 HOH   15  515 102 HOH   HOH A . 
Q 5 HOH   16  516 12  HOH   HOH A . 
Q 5 HOH   17  517 36  HOH   HOH A . 
Q 5 HOH   18  518 250 HOH   HOH A . 
Q 5 HOH   19  519 429 HOH   HOH A . 
Q 5 HOH   20  520 107 HOH   HOH A . 
Q 5 HOH   21  521 187 HOH   HOH A . 
Q 5 HOH   22  522 147 HOH   HOH A . 
Q 5 HOH   23  523 35  HOH   HOH A . 
Q 5 HOH   24  524 20  HOH   HOH A . 
Q 5 HOH   25  525 283 HOH   HOH A . 
Q 5 HOH   26  526 302 HOH   HOH A . 
Q 5 HOH   27  527 18  HOH   HOH A . 
Q 5 HOH   28  528 6   HOH   HOH A . 
Q 5 HOH   29  529 424 HOH   HOH A . 
Q 5 HOH   30  530 73  HOH   HOH A . 
Q 5 HOH   31  531 42  HOH   HOH A . 
Q 5 HOH   32  532 248 HOH   HOH A . 
Q 5 HOH   33  533 205 HOH   HOH A . 
Q 5 HOH   34  534 403 HOH   HOH A . 
Q 5 HOH   35  535 113 HOH   HOH A . 
Q 5 HOH   36  536 118 HOH   HOH A . 
Q 5 HOH   37  537 4   HOH   HOH A . 
Q 5 HOH   38  538 420 HOH   HOH A . 
Q 5 HOH   39  539 246 HOH   HOH A . 
Q 5 HOH   40  540 54  HOH   HOH A . 
Q 5 HOH   41  541 28  HOH   HOH A . 
Q 5 HOH   42  542 10  HOH   HOH A . 
Q 5 HOH   43  543 186 HOH   HOH A . 
Q 5 HOH   44  544 190 HOH   HOH A . 
Q 5 HOH   45  545 318 HOH   HOH A . 
Q 5 HOH   46  546 409 HOH   HOH A . 
Q 5 HOH   47  547 197 HOH   HOH A . 
Q 5 HOH   48  548 140 HOH   HOH A . 
Q 5 HOH   49  549 25  HOH   HOH A . 
Q 5 HOH   50  550 2   HOH   HOH A . 
Q 5 HOH   51  551 298 HOH   HOH A . 
Q 5 HOH   52  552 143 HOH   HOH A . 
Q 5 HOH   53  553 117 HOH   HOH A . 
Q 5 HOH   54  554 31  HOH   HOH A . 
Q 5 HOH   55  555 157 HOH   HOH A . 
Q 5 HOH   56  556 169 HOH   HOH A . 
Q 5 HOH   57  557 237 HOH   HOH A . 
Q 5 HOH   58  558 259 HOH   HOH A . 
Q 5 HOH   59  559 21  HOH   HOH A . 
Q 5 HOH   60  560 221 HOH   HOH A . 
Q 5 HOH   61  561 411 HOH   HOH A . 
Q 5 HOH   62  562 202 HOH   HOH A . 
Q 5 HOH   63  563 438 HOH   HOH A . 
Q 5 HOH   64  564 93  HOH   HOH A . 
Q 5 HOH   65  565 242 HOH   HOH A . 
Q 5 HOH   66  566 82  HOH   HOH A . 
Q 5 HOH   67  567 379 HOH   HOH A . 
Q 5 HOH   68  568 328 HOH   HOH A . 
Q 5 HOH   69  569 78  HOH   HOH A . 
Q 5 HOH   70  570 50  HOH   HOH A . 
Q 5 HOH   71  571 60  HOH   HOH A . 
Q 5 HOH   72  572 52  HOH   HOH A . 
Q 5 HOH   73  573 425 HOH   HOH A . 
Q 5 HOH   74  574 40  HOH   HOH A . 
Q 5 HOH   75  575 105 HOH   HOH A . 
Q 5 HOH   76  576 72  HOH   HOH A . 
Q 5 HOH   77  577 101 HOH   HOH A . 
Q 5 HOH   78  578 80  HOH   HOH A . 
Q 5 HOH   79  579 133 HOH   HOH A . 
Q 5 HOH   80  580 200 HOH   HOH A . 
Q 5 HOH   81  581 30  HOH   HOH A . 
Q 5 HOH   82  582 322 HOH   HOH A . 
Q 5 HOH   83  583 168 HOH   HOH A . 
Q 5 HOH   84  584 134 HOH   HOH A . 
Q 5 HOH   85  585 130 HOH   HOH A . 
Q 5 HOH   86  586 56  HOH   HOH A . 
Q 5 HOH   87  587 222 HOH   HOH A . 
Q 5 HOH   88  588 13  HOH   HOH A . 
Q 5 HOH   89  589 51  HOH   HOH A . 
Q 5 HOH   90  590 139 HOH   HOH A . 
Q 5 HOH   91  591 419 HOH   HOH A . 
Q 5 HOH   92  592 166 HOH   HOH A . 
Q 5 HOH   93  593 144 HOH   HOH A . 
Q 5 HOH   94  594 255 HOH   HOH A . 
Q 5 HOH   95  595 121 HOH   HOH A . 
Q 5 HOH   96  596 323 HOH   HOH A . 
Q 5 HOH   97  597 350 HOH   HOH A . 
Q 5 HOH   98  598 378 HOH   HOH A . 
Q 5 HOH   99  599 142 HOH   HOH A . 
Q 5 HOH   100 600 89  HOH   HOH A . 
Q 5 HOH   101 601 227 HOH   HOH A . 
Q 5 HOH   102 602 433 HOH   HOH A . 
Q 5 HOH   103 603 125 HOH   HOH A . 
Q 5 HOH   104 604 207 HOH   HOH A . 
Q 5 HOH   105 605 295 HOH   HOH A . 
Q 5 HOH   106 606 88  HOH   HOH A . 
Q 5 HOH   107 607 176 HOH   HOH A . 
Q 5 HOH   108 608 184 HOH   HOH A . 
Q 5 HOH   109 609 406 HOH   HOH A . 
Q 5 HOH   110 610 183 HOH   HOH A . 
Q 5 HOH   111 611 137 HOH   HOH A . 
Q 5 HOH   112 612 201 HOH   HOH A . 
Q 5 HOH   113 613 108 HOH   HOH A . 
Q 5 HOH   114 614 264 HOH   HOH A . 
Q 5 HOH   115 615 9   HOH   HOH A . 
Q 5 HOH   116 616 257 HOH   HOH A . 
Q 5 HOH   117 617 63  HOH   HOH A . 
Q 5 HOH   118 618 236 HOH   HOH A . 
Q 5 HOH   119 619 64  HOH   HOH A . 
Q 5 HOH   120 620 69  HOH   HOH A . 
Q 5 HOH   121 621 77  HOH   HOH A . 
Q 5 HOH   122 622 84  HOH   HOH A . 
Q 5 HOH   123 623 154 HOH   HOH A . 
Q 5 HOH   124 624 337 HOH   HOH A . 
Q 5 HOH   125 625 175 HOH   HOH A . 
Q 5 HOH   126 626 135 HOH   HOH A . 
Q 5 HOH   127 627 145 HOH   HOH A . 
Q 5 HOH   128 628 132 HOH   HOH A . 
Q 5 HOH   129 629 217 HOH   HOH A . 
Q 5 HOH   130 630 156 HOH   HOH A . 
Q 5 HOH   131 631 269 HOH   HOH A . 
Q 5 HOH   132 632 299 HOH   HOH A . 
Q 5 HOH   133 633 380 HOH   HOH A . 
Q 5 HOH   134 634 356 HOH   HOH A . 
Q 5 HOH   135 635 119 HOH   HOH A . 
Q 5 HOH   136 636 428 HOH   HOH A . 
Q 5 HOH   137 637 195 HOH   HOH A . 
Q 5 HOH   138 638 159 HOH   HOH A . 
Q 5 HOH   139 639 426 HOH   HOH A . 
Q 5 HOH   140 640 430 HOH   HOH A . 
Q 5 HOH   141 641 276 HOH   HOH A . 
Q 5 HOH   142 642 124 HOH   HOH A . 
Q 5 HOH   143 643 267 HOH   HOH A . 
Q 5 HOH   144 644 287 HOH   HOH A . 
Q 5 HOH   145 645 377 HOH   HOH A . 
Q 5 HOH   146 646 375 HOH   HOH A . 
Q 5 HOH   147 647 178 HOH   HOH A . 
Q 5 HOH   148 648 300 HOH   HOH A . 
Q 5 HOH   149 649 336 HOH   HOH A . 
Q 5 HOH   150 650 104 HOH   HOH A . 
Q 5 HOH   151 651 348 HOH   HOH A . 
Q 5 HOH   152 652 373 HOH   HOH A . 
Q 5 HOH   153 653 313 HOH   HOH A . 
Q 5 HOH   154 654 266 HOH   HOH A . 
Q 5 HOH   155 655 445 HOH   HOH A . 
Q 5 HOH   156 656 405 HOH   HOH A . 
Q 5 HOH   157 657 262 HOH   HOH A . 
Q 5 HOH   158 658 231 HOH   HOH A . 
Q 5 HOH   159 659 280 HOH   HOH A . 
Q 5 HOH   160 660 293 HOH   HOH A . 
Q 5 HOH   161 661 286 HOH   HOH A . 
Q 5 HOH   162 662 272 HOH   HOH A . 
Q 5 HOH   163 663 289 HOH   HOH A . 
Q 5 HOH   164 664 414 HOH   HOH A . 
Q 5 HOH   165 665 427 HOH   HOH A . 
Q 5 HOH   166 666 381 HOH   HOH A . 
Q 5 HOH   167 667 441 HOH   HOH A . 
Q 5 HOH   168 668 422 HOH   HOH A . 
Q 5 HOH   169 669 194 HOH   HOH A . 
Q 5 HOH   170 670 370 HOH   HOH A . 
Q 5 HOH   171 671 252 HOH   HOH A . 
Q 5 HOH   172 672 282 HOH   HOH A . 
Q 5 HOH   173 673 284 HOH   HOH A . 
Q 5 HOH   174 674 308 HOH   HOH A . 
Q 5 HOH   175 675 374 HOH   HOH A . 
Q 5 HOH   176 676 123 HOH   HOH A . 
Q 5 HOH   177 677 188 HOH   HOH A . 
Q 5 HOH   178 678 362 HOH   HOH A . 
Q 5 HOH   179 679 436 HOH   HOH A . 
Q 5 HOH   180 680 291 HOH   HOH A . 
Q 5 HOH   181 681 223 HOH   HOH A . 
Q 5 HOH   182 682 95  HOH   HOH A . 
Q 5 HOH   183 683 402 HOH   HOH A . 
Q 5 HOH   184 684 412 HOH   HOH A . 
Q 5 HOH   185 685 245 HOH   HOH A . 
Q 5 HOH   186 686 234 HOH   HOH A . 
Q 5 HOH   187 687 439 HOH   HOH A . 
Q 5 HOH   188 688 129 HOH   HOH A . 
Q 5 HOH   189 689 309 HOH   HOH A . 
Q 5 HOH   190 690 219 HOH   HOH A . 
Q 5 HOH   191 691 413 HOH   HOH A . 
Q 5 HOH   192 692 296 HOH   HOH A . 
Q 5 HOH   193 693 275 HOH   HOH A . 
Q 5 HOH   194 694 285 HOH   HOH A . 
Q 5 HOH   195 695 258 HOH   HOH A . 
Q 5 HOH   196 696 225 HOH   HOH A . 
Q 5 HOH   197 697 256 HOH   HOH A . 
R 5 HOH   1   401 171 HOH   HOH B . 
R 5 HOH   2   402 75  HOH   HOH B . 
R 5 HOH   3   403 67  HOH   HOH B . 
R 5 HOH   4   404 74  HOH   HOH B . 
R 5 HOH   5   405 393 HOH   HOH B . 
R 5 HOH   6   406 193 HOH   HOH B . 
R 5 HOH   7   407 5   HOH   HOH B . 
R 5 HOH   8   408 327 HOH   HOH B . 
R 5 HOH   9   409 76  HOH   HOH B . 
R 5 HOH   10  410 260 HOH   HOH B . 
R 5 HOH   11  411 162 HOH   HOH B . 
R 5 HOH   12  412 37  HOH   HOH B . 
R 5 HOH   13  413 360 HOH   HOH B . 
R 5 HOH   14  414 339 HOH   HOH B . 
R 5 HOH   15  415 32  HOH   HOH B . 
R 5 HOH   16  416 23  HOH   HOH B . 
R 5 HOH   17  417 27  HOH   HOH B . 
R 5 HOH   18  418 209 HOH   HOH B . 
R 5 HOH   19  419 85  HOH   HOH B . 
R 5 HOH   20  420 153 HOH   HOH B . 
R 5 HOH   21  421 181 HOH   HOH B . 
R 5 HOH   22  422 177 HOH   HOH B . 
R 5 HOH   23  423 371 HOH   HOH B . 
R 5 HOH   24  424 240 HOH   HOH B . 
R 5 HOH   25  425 180 HOH   HOH B . 
R 5 HOH   26  426 167 HOH   HOH B . 
R 5 HOH   27  427 99  HOH   HOH B . 
R 5 HOH   28  428 112 HOH   HOH B . 
R 5 HOH   29  429 59  HOH   HOH B . 
R 5 HOH   30  430 47  HOH   HOH B . 
R 5 HOH   31  431 24  HOH   HOH B . 
R 5 HOH   32  432 312 HOH   HOH B . 
R 5 HOH   33  433 127 HOH   HOH B . 
R 5 HOH   34  434 198 HOH   HOH B . 
R 5 HOH   35  435 126 HOH   HOH B . 
R 5 HOH   36  436 44  HOH   HOH B . 
R 5 HOH   37  437 288 HOH   HOH B . 
R 5 HOH   38  438 114 HOH   HOH B . 
R 5 HOH   39  439 68  HOH   HOH B . 
R 5 HOH   40  440 8   HOH   HOH B . 
R 5 HOH   41  441 58  HOH   HOH B . 
R 5 HOH   42  442 158 HOH   HOH B . 
R 5 HOH   43  443 62  HOH   HOH B . 
R 5 HOH   44  444 218 HOH   HOH B . 
R 5 HOH   45  445 214 HOH   HOH B . 
R 5 HOH   46  446 97  HOH   HOH B . 
R 5 HOH   47  447 14  HOH   HOH B . 
R 5 HOH   48  448 29  HOH   HOH B . 
R 5 HOH   49  449 254 HOH   HOH B . 
R 5 HOH   50  450 1   HOH   HOH B . 
R 5 HOH   51  451 401 HOH   HOH B . 
R 5 HOH   52  452 53  HOH   HOH B . 
R 5 HOH   53  453 161 HOH   HOH B . 
R 5 HOH   54  454 57  HOH   HOH B . 
R 5 HOH   55  455 271 HOH   HOH B . 
R 5 HOH   56  456 172 HOH   HOH B . 
R 5 HOH   57  457 215 HOH   HOH B . 
R 5 HOH   58  458 26  HOH   HOH B . 
R 5 HOH   59  459 326 HOH   HOH B . 
R 5 HOH   60  460 361 HOH   HOH B . 
R 5 HOH   61  461 100 HOH   HOH B . 
R 5 HOH   62  462 34  HOH   HOH B . 
R 5 HOH   63  463 15  HOH   HOH B . 
R 5 HOH   64  464 303 HOH   HOH B . 
R 5 HOH   65  465 208 HOH   HOH B . 
R 5 HOH   66  466 206 HOH   HOH B . 
R 5 HOH   67  467 39  HOH   HOH B . 
R 5 HOH   68  468 122 HOH   HOH B . 
R 5 HOH   69  469 274 HOH   HOH B . 
R 5 HOH   70  470 321 HOH   HOH B . 
R 5 HOH   71  471 46  HOH   HOH B . 
R 5 HOH   72  472 111 HOH   HOH B . 
R 5 HOH   73  473 131 HOH   HOH B . 
R 5 HOH   74  474 83  HOH   HOH B . 
R 5 HOH   75  475 106 HOH   HOH B . 
R 5 HOH   76  476 196 HOH   HOH B . 
R 5 HOH   77  477 17  HOH   HOH B . 
R 5 HOH   78  478 238 HOH   HOH B . 
R 5 HOH   79  479 79  HOH   HOH B . 
R 5 HOH   80  480 92  HOH   HOH B . 
R 5 HOH   81  481 109 HOH   HOH B . 
R 5 HOH   82  482 55  HOH   HOH B . 
R 5 HOH   83  483 96  HOH   HOH B . 
R 5 HOH   84  484 19  HOH   HOH B . 
R 5 HOH   85  485 192 HOH   HOH B . 
R 5 HOH   86  486 311 HOH   HOH B . 
R 5 HOH   87  487 268 HOH   HOH B . 
R 5 HOH   88  488 94  HOH   HOH B . 
R 5 HOH   89  489 115 HOH   HOH B . 
R 5 HOH   90  490 45  HOH   HOH B . 
R 5 HOH   91  491 120 HOH   HOH B . 
R 5 HOH   92  492 278 HOH   HOH B . 
R 5 HOH   93  493 90  HOH   HOH B . 
R 5 HOH   94  494 185 HOH   HOH B . 
R 5 HOH   95  495 116 HOH   HOH B . 
R 5 HOH   96  496 98  HOH   HOH B . 
R 5 HOH   97  497 70  HOH   HOH B . 
R 5 HOH   98  498 210 HOH   HOH B . 
R 5 HOH   99  499 160 HOH   HOH B . 
R 5 HOH   100 500 174 HOH   HOH B . 
R 5 HOH   101 501 43  HOH   HOH B . 
R 5 HOH   102 502 33  HOH   HOH B . 
R 5 HOH   103 503 163 HOH   HOH B . 
R 5 HOH   104 504 203 HOH   HOH B . 
R 5 HOH   105 505 91  HOH   HOH B . 
R 5 HOH   106 506 385 HOH   HOH B . 
R 5 HOH   107 507 423 HOH   HOH B . 
R 5 HOH   108 508 22  HOH   HOH B . 
R 5 HOH   109 509 155 HOH   HOH B . 
R 5 HOH   110 510 128 HOH   HOH B . 
R 5 HOH   111 511 199 HOH   HOH B . 
R 5 HOH   112 512 141 HOH   HOH B . 
R 5 HOH   113 513 212 HOH   HOH B . 
R 5 HOH   114 514 148 HOH   HOH B . 
R 5 HOH   115 515 213 HOH   HOH B . 
R 5 HOH   116 516 87  HOH   HOH B . 
R 5 HOH   117 517 65  HOH   HOH B . 
R 5 HOH   118 518 232 HOH   HOH B . 
R 5 HOH   119 519 41  HOH   HOH B . 
R 5 HOH   120 520 211 HOH   HOH B . 
R 5 HOH   121 521 81  HOH   HOH B . 
R 5 HOH   122 522 251 HOH   HOH B . 
R 5 HOH   123 523 61  HOH   HOH B . 
R 5 HOH   124 524 110 HOH   HOH B . 
R 5 HOH   125 525 305 HOH   HOH B . 
R 5 HOH   126 526 304 HOH   HOH B . 
R 5 HOH   127 527 387 HOH   HOH B . 
R 5 HOH   128 528 136 HOH   HOH B . 
R 5 HOH   129 529 319 HOH   HOH B . 
R 5 HOH   130 530 243 HOH   HOH B . 
R 5 HOH   131 531 320 HOH   HOH B . 
R 5 HOH   132 532 400 HOH   HOH B . 
R 5 HOH   133 533 404 HOH   HOH B . 
R 5 HOH   134 534 297 HOH   HOH B . 
R 5 HOH   135 535 440 HOH   HOH B . 
R 5 HOH   136 536 138 HOH   HOH B . 
R 5 HOH   137 537 146 HOH   HOH B . 
R 5 HOH   138 538 103 HOH   HOH B . 
R 5 HOH   139 539 263 HOH   HOH B . 
R 5 HOH   140 540 249 HOH   HOH B . 
R 5 HOH   141 541 152 HOH   HOH B . 
R 5 HOH   142 542 317 HOH   HOH B . 
R 5 HOH   143 543 391 HOH   HOH B . 
R 5 HOH   144 544 306 HOH   HOH B . 
R 5 HOH   145 545 149 HOH   HOH B . 
R 5 HOH   146 546 310 HOH   HOH B . 
R 5 HOH   147 547 330 HOH   HOH B . 
R 5 HOH   148 548 173 HOH   HOH B . 
R 5 HOH   149 549 324 HOH   HOH B . 
R 5 HOH   150 550 247 HOH   HOH B . 
R 5 HOH   151 551 432 HOH   HOH B . 
R 5 HOH   152 552 358 HOH   HOH B . 
R 5 HOH   153 553 437 HOH   HOH B . 
R 5 HOH   154 554 386 HOH   HOH B . 
R 5 HOH   155 555 435 HOH   HOH B . 
R 5 HOH   156 556 189 HOH   HOH B . 
R 5 HOH   157 557 151 HOH   HOH B . 
R 5 HOH   158 558 229 HOH   HOH B . 
R 5 HOH   159 559 364 HOH   HOH B . 
R 5 HOH   160 560 265 HOH   HOH B . 
R 5 HOH   161 561 170 HOH   HOH B . 
R 5 HOH   162 562 421 HOH   HOH B . 
R 5 HOH   163 563 416 HOH   HOH B . 
R 5 HOH   164 564 389 HOH   HOH B . 
R 5 HOH   165 565 182 HOH   HOH B . 
R 5 HOH   166 566 382 HOH   HOH B . 
R 5 HOH   167 567 273 HOH   HOH B . 
R 5 HOH   168 568 395 HOH   HOH B . 
R 5 HOH   169 569 434 HOH   HOH B . 
R 5 HOH   170 570 394 HOH   HOH B . 
R 5 HOH   171 571 315 HOH   HOH B . 
R 5 HOH   172 572 384 HOH   HOH B . 
R 5 HOH   173 573 407 HOH   HOH B . 
R 5 HOH   174 574 396 HOH   HOH B . 
R 5 HOH   175 575 277 HOH   HOH B . 
R 5 HOH   176 576 341 HOH   HOH B . 
R 5 HOH   177 577 392 HOH   HOH B . 
R 5 HOH   178 578 338 HOH   HOH B . 
R 5 HOH   179 579 294 HOH   HOH B . 
R 5 HOH   180 580 399 HOH   HOH B . 
R 5 HOH   181 581 369 HOH   HOH B . 
R 5 HOH   182 582 390 HOH   HOH B . 
R 5 HOH   183 583 345 HOH   HOH B . 
R 5 HOH   184 584 443 HOH   HOH B . 
R 5 HOH   185 585 241 HOH   HOH B . 
R 5 HOH   186 586 261 HOH   HOH B . 
R 5 HOH   187 587 279 HOH   HOH B . 
R 5 HOH   188 588 444 HOH   HOH B . 
R 5 HOH   189 589 281 HOH   HOH B . 
R 5 HOH   190 590 383 HOH   HOH B . 
R 5 HOH   191 591 388 HOH   HOH B . 
R 5 HOH   192 592 290 HOH   HOH B . 
R 5 HOH   193 593 349 HOH   HOH B . 
R 5 HOH   194 594 239 HOH   HOH B . 
R 5 HOH   195 595 165 HOH   HOH B . 
R 5 HOH   196 596 244 HOH   HOH B . 
R 5 HOH   197 597 335 HOH   HOH B . 
R 5 HOH   198 598 342 HOH   HOH B . 
R 5 HOH   199 599 253 HOH   HOH B . 
R 5 HOH   200 600 191 HOH   HOH B . 
R 5 HOH   201 601 233 HOH   HOH B . 
R 5 HOH   202 602 292 HOH   HOH B . 
R 5 HOH   203 603 220 HOH   HOH B . 
# 
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 GLU 5   ? CB  ? A GLU 25  CB  
2   1 Y 1 A GLU 5   ? CG  ? A GLU 25  CG  
3   1 Y 1 A GLU 5   ? CD  ? A GLU 25  CD  
4   1 Y 1 A GLU 5   ? OE1 ? A GLU 25  OE1 
5   1 Y 1 A GLU 5   ? OE2 ? A GLU 25  OE2 
6   1 Y 1 A LYS 6   ? CB  ? A LYS 26  CB  
7   1 Y 1 A LYS 6   ? CG  ? A LYS 26  CG  
8   1 Y 1 A LYS 6   ? CD  ? A LYS 26  CD  
9   1 Y 1 A LYS 6   ? CE  ? A LYS 26  CE  
10  1 Y 1 A LYS 6   ? NZ  ? A LYS 26  NZ  
11  1 Y 1 A ASP 12  ? OD1 ? A ASP 32  OD1 
12  1 Y 1 A ASP 12  ? OD2 ? A ASP 32  OD2 
13  1 Y 1 A GLU 13  ? CG  ? A GLU 33  CG  
14  1 Y 1 A GLU 13  ? CD  ? A GLU 33  CD  
15  1 Y 1 A GLU 13  ? OE1 ? A GLU 33  OE1 
16  1 Y 1 A GLU 13  ? OE2 ? A GLU 33  OE2 
17  1 Y 1 A GLU 25  ? CG  ? A GLU 45  CG  
18  1 Y 1 A GLU 25  ? CD  ? A GLU 45  CD  
19  1 Y 1 A GLU 25  ? OE1 ? A GLU 45  OE1 
20  1 Y 1 A GLU 25  ? OE2 ? A GLU 45  OE2 
21  1 Y 1 A ASP 26  ? OD1 ? A ASP 46  OD1 
22  1 Y 1 A ASP 26  ? OD2 ? A ASP 46  OD2 
23  1 Y 1 A LYS 46  ? CG  ? A LYS 66  CG  
24  1 Y 1 A LYS 46  ? CD  ? A LYS 66  CD  
25  1 Y 1 A LYS 46  ? CE  ? A LYS 66  CE  
26  1 Y 1 A LYS 46  ? NZ  ? A LYS 66  NZ  
27  1 Y 1 A GLU 47  ? CD  ? A GLU 67  CD  
28  1 Y 1 A GLU 47  ? OE1 ? A GLU 67  OE1 
29  1 Y 1 A GLU 47  ? OE2 ? A GLU 67  OE2 
30  1 Y 1 A LYS 50  ? NZ  ? A LYS 70  NZ  
31  1 Y 1 A LYS 72  ? CE  ? A LYS 92  CE  
32  1 Y 1 A LYS 72  ? NZ  ? A LYS 92  NZ  
33  1 Y 1 A LYS 92  ? CE  ? A LYS 112 CE  
34  1 Y 1 A LYS 92  ? NZ  ? A LYS 112 NZ  
35  1 Y 1 A LYS 107 ? NZ  ? A LYS 127 NZ  
36  1 Y 1 A ASN 108 ? OD1 ? A ASN 128 OD1 
37  1 Y 1 A ASN 108 ? ND2 ? A ASN 128 ND2 
38  1 Y 1 A LYS 110 ? NZ  ? A LYS 130 NZ  
39  1 Y 1 A GLN 139 ? CD  ? A GLN 159 CD  
40  1 Y 1 A GLN 139 ? OE1 ? A GLN 159 OE1 
41  1 Y 1 A GLN 139 ? NE2 ? A GLN 159 NE2 
42  1 Y 1 A LYS 141 ? NZ  ? A LYS 161 NZ  
43  1 Y 1 A LYS 167 ? CE  ? A LYS 187 CE  
44  1 Y 1 A LYS 167 ? NZ  ? A LYS 187 NZ  
45  1 Y 1 A GLU 171 ? CG  ? A GLU 191 CG  
46  1 Y 1 A GLU 171 ? CD  ? A GLU 191 CD  
47  1 Y 1 A GLU 171 ? OE1 ? A GLU 191 OE1 
48  1 Y 1 A GLU 171 ? OE2 ? A GLU 191 OE2 
49  1 Y 1 A LYS 172 ? CG  ? A LYS 192 CG  
50  1 Y 1 A LYS 172 ? CD  ? A LYS 192 CD  
51  1 Y 1 A LYS 172 ? CE  ? A LYS 192 CE  
52  1 Y 1 A LYS 172 ? NZ  ? A LYS 192 NZ  
53  1 Y 1 A ARG 184 ? CZ  ? A ARG 204 CZ  
54  1 Y 1 A ARG 184 ? NH1 ? A ARG 204 NH1 
55  1 Y 1 A ARG 184 ? NH2 ? A ARG 204 NH2 
56  1 Y 1 A LYS 190 ? NZ  ? A LYS 210 NZ  
57  1 Y 1 A LYS 191 ? NZ  ? A LYS 211 NZ  
58  1 Y 1 A GLU 200 ? CD  ? A GLU 220 CD  
59  1 Y 1 A GLU 200 ? OE1 ? A GLU 220 OE1 
60  1 Y 1 A GLU 200 ? OE2 ? A GLU 220 OE2 
61  1 Y 1 A GLU 213 ? CD  ? A GLU 233 CD  
62  1 Y 1 A GLU 213 ? OE1 ? A GLU 233 OE1 
63  1 Y 1 A GLU 213 ? OE2 ? A GLU 233 OE2 
64  1 Y 1 A LYS 249 ? NZ  ? A LYS 269 NZ  
65  1 Y 1 A ILE 251 ? CD1 ? A ILE 271 CD1 
66  1 Y 1 B ASN 7   ? CG  ? B ASN 27  CG  
67  1 Y 1 B ASN 7   ? OD1 ? B ASN 27  OD1 
68  1 Y 1 B ASN 7   ? ND2 ? B ASN 27  ND2 
69  1 Y 1 B ILE 8   ? CG1 ? B ILE 28  CG1 
70  1 Y 1 B ILE 8   ? CD1 ? B ILE 28  CD1 
71  1 Y 1 B GLU 13  ? CD  ? B GLU 33  CD  
72  1 Y 1 B GLU 13  ? OE1 ? B GLU 33  OE1 
73  1 Y 1 B GLU 13  ? OE2 ? B GLU 33  OE2 
74  1 Y 1 B SER 14  ? OG  ? B SER 34  OG  
75  1 Y 1 B GLU 25  ? CD  ? B GLU 45  CD  
76  1 Y 1 B GLU 25  ? OE1 ? B GLU 45  OE1 
77  1 Y 1 B GLU 25  ? OE2 ? B GLU 45  OE2 
78  1 Y 1 B LYS 46  ? CE  ? B LYS 66  CE  
79  1 Y 1 B LYS 46  ? NZ  ? B LYS 66  NZ  
80  1 Y 1 B GLU 47  ? CG  ? B GLU 67  CG  
81  1 Y 1 B GLU 47  ? CD  ? B GLU 67  CD  
82  1 Y 1 B GLU 47  ? OE1 ? B GLU 67  OE1 
83  1 Y 1 B GLU 47  ? OE2 ? B GLU 67  OE2 
84  1 Y 1 B LYS 72  ? CE  ? B LYS 92  CE  
85  1 Y 1 B LYS 72  ? NZ  ? B LYS 92  NZ  
86  1 Y 1 B LYS 92  ? CD  ? B LYS 112 CD  
87  1 Y 1 B LYS 92  ? CE  ? B LYS 112 CE  
88  1 Y 1 B LYS 92  ? NZ  ? B LYS 112 NZ  
89  1 Y 1 B ASN 93  ? ND2 ? B ASN 113 ND2 
90  1 Y 1 B ARG 120 ? NH1 ? B ARG 140 NH1 
91  1 Y 1 B ARG 120 ? NH2 ? B ARG 140 NH2 
92  1 Y 1 B GLN 139 ? CG  ? B GLN 159 CG  
93  1 Y 1 B GLN 139 ? CD  ? B GLN 159 CD  
94  1 Y 1 B GLN 139 ? OE1 ? B GLN 159 OE1 
95  1 Y 1 B GLN 139 ? NE2 ? B GLN 159 NE2 
96  1 Y 1 B LYS 141 ? NZ  ? B LYS 161 NZ  
97  1 Y 1 B GLU 171 ? CG  ? B GLU 191 CG  
98  1 Y 1 B GLU 171 ? CD  ? B GLU 191 CD  
99  1 Y 1 B GLU 171 ? OE1 ? B GLU 191 OE1 
100 1 Y 1 B GLU 171 ? OE2 ? B GLU 191 OE2 
101 1 Y 1 B LYS 172 ? CG  ? B LYS 192 CG  
102 1 Y 1 B LYS 172 ? CD  ? B LYS 192 CD  
103 1 Y 1 B LYS 172 ? CE  ? B LYS 192 CE  
104 1 Y 1 B LYS 172 ? NZ  ? B LYS 192 NZ  
105 1 Y 1 B ARG 184 ? NE  ? B ARG 204 NE  
106 1 Y 1 B ARG 184 ? CZ  ? B ARG 204 CZ  
107 1 Y 1 B ARG 184 ? NH1 ? B ARG 204 NH1 
108 1 Y 1 B ARG 184 ? NH2 ? B ARG 204 NH2 
109 1 Y 1 B GLU 186 ? CG  ? B GLU 206 CG  
110 1 Y 1 B GLU 186 ? CD  ? B GLU 206 CD  
111 1 Y 1 B GLU 186 ? OE1 ? B GLU 206 OE1 
112 1 Y 1 B GLU 186 ? OE2 ? B GLU 206 OE2 
113 1 Y 1 B LYS 190 ? NZ  ? B LYS 210 NZ  
114 1 Y 1 B GLU 209 ? CG  ? B GLU 229 CG  
115 1 Y 1 B GLU 209 ? CD  ? B GLU 229 CD  
116 1 Y 1 B GLU 209 ? OE1 ? B GLU 229 OE1 
117 1 Y 1 B GLU 209 ? OE2 ? B GLU 229 OE2 
118 1 Y 1 B LYS 212 ? NZ  ? B LYS 232 NZ  
119 1 Y 1 B GLU 213 ? CG  ? B GLU 233 CG  
120 1 Y 1 B GLU 213 ? CD  ? B GLU 233 CD  
121 1 Y 1 B GLU 213 ? OE1 ? B GLU 233 OE1 
122 1 Y 1 B GLU 213 ? OE2 ? B GLU 233 OE2 
123 1 Y 1 B ILE 217 ? CD1 ? B ILE 237 CD1 
124 1 Y 1 B LYS 249 ? NZ  ? B LYS 269 NZ  
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? XDS-Apple_M1 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? XDS-Apple_M1 2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 1.20.1_4487  3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.9.8.7      4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487  5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BXN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.800 
_cell.length_a_esd                 ? 
_cell.length_b                     92.010 
_cell.length_b_esd                 ? 
_cell.length_c                     96.200 
_cell.length_c_esd                 ? 
_cell.volume                       617825.068 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9BXN 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   9BXN 
_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             2.51 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.1 
_exptl_crystal.description                  Plates 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M citrate, pH 5, 19% v/v PEG6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_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   0.95302 
_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                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95302 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          26.02 
_reflns.entry_id                                       9BXN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.7 
_reflns.d_resolution_low                               48.1 
_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                                     68782 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.97 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.00 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.03907 
_reflns.pdbx_Rpim_I_all                                0.02763 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.02763 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_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_shell.d_res_high                                    1.7 
_reflns_shell.d_res_low                                     1.761 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.11 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6777 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_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                               1.9 
_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                               0.8534 
_reflns_shell.pdbx_Rpim_I_all                               0.6035 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.597 
_reflns_shell.pdbx_CC_star                                  0.865 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.96 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.6035 
_reflns_shell.pdbx_Rsym_value                               ? 
_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               ? 
# 
_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                                ? 
_refine.B_iso_mean                               28.92 
_refine.B_iso_min                                ? 
_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                                 9BXN 
_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                            1.70 
_refine.ls_d_res_low                             48.1 
_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                     68773 
_refine.ls_number_reflns_R_free                  6535 
_refine.ls_number_reflns_R_work                  125106 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1700 
_refine.ls_R_factor_R_free                       0.1933 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1688 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          SIR 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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                 20.3804 
_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                            0.2211 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        48.1 
_refine_hist.number_atoms_solvent             400 
_refine_hist.number_atoms_total               4378 
_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       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3870 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         108 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0129  ? 4063 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2007  ? 5485 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0698  ? 595  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0149  ? 698  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.1237 ? 1418 ? f_dihedral_angle_d ? ? 
# 
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_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 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.70 1.72 . . 242 4132 99.50  . . . . 0.3782 . . . . . . . . . . . 0.3751 
'X-RAY DIFFRACTION' 1.72 1.74 . . 186 4184 99.89  . . . . 0.3538 . . . . . . . . . . . 0.3329 
'X-RAY DIFFRACTION' 1.74 1.76 . . 206 4181 99.95  . . . . 0.3167 . . . . . . . . . . . 0.3171 
'X-RAY DIFFRACTION' 1.76 1.78 . . 238 4159 99.95  . . . . 0.2939 . . . . . . . . . . . 0.3009 
'X-RAY DIFFRACTION' 1.78 1.81 . . 239 4139 99.93  . . . . 0.2588 . . . . . . . . . . . 0.2693 
'X-RAY DIFFRACTION' 1.81 1.83 . . 197 4213 99.93  . . . . 0.2484 . . . . . . . . . . . 0.2562 
'X-RAY DIFFRACTION' 1.83 1.86 . . 228 4195 100.00 . . . . 0.2286 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 1.86 1.89 . . 184 4210 100.00 . . . . 0.2275 . . . . . . . . . . . 0.2448 
'X-RAY DIFFRACTION' 1.89 1.91 . . 250 4055 100.00 . . . . 0.2229 . . . . . . . . . . . 0.2304 
'X-RAY DIFFRACTION' 1.91 1.95 . . 210 4207 99.93  . . . . 0.2138 . . . . . . . . . . . 0.2556 
'X-RAY DIFFRACTION' 1.95 1.98 . . 200 4207 100.00 . . . . 0.2047 . . . . . . . . . . . 0.2430 
'X-RAY DIFFRACTION' 1.98 2.02 . . 208 4156 99.98  . . . . 0.2033 . . . . . . . . . . . 0.2105 
'X-RAY DIFFRACTION' 2.02 2.05 . . 237 4192 100.00 . . . . 0.2004 . . . . . . . . . . . 0.2206 
'X-RAY DIFFRACTION' 2.05 2.10 . . 219 4127 100.00 . . . . 0.1852 . . . . . . . . . . . 0.2074 
'X-RAY DIFFRACTION' 2.10 2.14 . . 215 4222 100.00 . . . . 0.1698 . . . . . . . . . . . 0.2104 
'X-RAY DIFFRACTION' 2.14 2.19 . . 223 4140 100.00 . . . . 0.1710 . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 2.19 2.25 . . 219 4157 99.82  . . . . 0.1684 . . . . . . . . . . . 0.2414 
'X-RAY DIFFRACTION' 2.25 2.31 . . 220 4175 100.00 . . . . 0.1707 . . . . . . . . . . . 0.2337 
'X-RAY DIFFRACTION' 2.31 2.38 . . 213 4169 100.00 . . . . 0.1660 . . . . . . . . . . . 0.1829 
'X-RAY DIFFRACTION' 2.38 2.45 . . 220 4166 100.00 . . . . 0.1610 . . . . . . . . . . . 0.1981 
'X-RAY DIFFRACTION' 2.45 2.54 . . 228 4164 100.00 . . . . 0.1618 . . . . . . . . . . . 0.1991 
'X-RAY DIFFRACTION' 2.54 2.64 . . 222 4181 100.00 . . . . 0.1608 . . . . . . . . . . . 0.1899 
'X-RAY DIFFRACTION' 2.64 2.76 . . 206 4186 100.00 . . . . 0.1549 . . . . . . . . . . . 0.1701 
'X-RAY DIFFRACTION' 2.76 2.91 . . 211 4153 99.95  . . . . 0.1563 . . . . . . . . . . . 0.1986 
'X-RAY DIFFRACTION' 2.91 3.09 . . 208 4200 99.98  . . . . 0.1566 . . . . . . . . . . . 0.1678 
'X-RAY DIFFRACTION' 3.09 3.33 . . 212 4192 100.00 . . . . 0.1589 . . . . . . . . . . . 0.1890 
'X-RAY DIFFRACTION' 3.33 3.66 . . 217 4153 100.00 . . . . 0.1464 . . . . . . . . . . . 0.1818 
'X-RAY DIFFRACTION' 3.66 4.19 . . 220 4167 100.00 . . . . 0.1349 . . . . . . . . . . . 0.1461 
'X-RAY DIFFRACTION' 4.19 5.28 . . 225 4160 100.00 . . . . 0.1312 . . . . . . . . . . . 0.1517 
'X-RAY DIFFRACTION' 5.28 48.1 . . 232 4164 99.89  . . . . 0.1755 . . . . . . . . . . . 0.1896 
# 
_struct.entry_id                     9BXN 
_struct.title                        
'OvoM from Sulfuricurvum sp. isolate STB_99, an ovothiol-biosynthetic N-methyltransferase in complex with 5-thiohistidine and SAH' 
_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        9BXN 
_struct_keywords.text            'ovothiol, S-adenosyl-L-methionine, 5-thiohistidine, 5-selenohistidine, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 2 ? 
N N N 4 ? 
O N N 4 ? 
P N N 4 ? 
Q N N 5 ? 
R N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9BXN 
_struct_ref.pdbx_db_accession          9BXN 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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 9BXN A 1 ? 273 ? 9BXN -19 ? 253 ? -19 253 
2 1 9BXN B 1 ? 273 ? 9BXN -19 ? 253 ? -19 253 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 4510  ? 
1 MORE         21    ? 
1 'SSA (A^2)'  20210 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 B,M,N,O,P,R             
1 2 A,C,D,E,F,G,H,I,J,K,L,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z           1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000  
2 'crystal symmetry operation' 2_455 -x-1/2,-y,z+1/2 -1.0000000000 0.0000000000 0.0000000000 -34.9000000000 0.0000000000 
-1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 48.1000000000 
# 
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 ASN A 27  ? GLU A 30  ? ASN A 7   GLU A 10  5 ? 4  
HELX_P HELX_P2  AA2 THR A 31  ? GLY A 44  ? THR A 11  GLY A 24  1 ? 14 
HELX_P HELX_P3  AA3 ASN A 52  ? THR A 65  ? ASN A 32  THR A 45  1 ? 14 
HELX_P HELX_P4  AA4 GLY A 81  ? ALA A 88  ? GLY A 61  ALA A 68  1 ? 8  
HELX_P HELX_P5  AA5 SER A 100 ? GLY A 114 ? SER A 80  GLY A 94  1 ? 15 
HELX_P HELX_P6  AA6 GLU A 135 ? THR A 144 ? GLU A 115 THR A 124 5 ? 10 
HELX_P HELX_P7  AA7 LEU A 171 ? LEU A 175 ? LEU A 151 LEU A 155 5 ? 5  
HELX_P HELX_P8  AA8 GLU A 177 ? GLU A 183 ? GLU A 157 GLU A 163 1 ? 7  
HELX_P HELX_P9  AA9 ASN A 184 ? LYS A 187 ? ASN A 164 LYS A 167 5 ? 4  
HELX_P HELX_P10 AB1 ALA A 209 ? TRP A 213 ? ALA A 189 TRP A 193 5 ? 5  
HELX_P HELX_P11 AB2 SER A 226 ? GLU A 236 ? SER A 206 GLU A 216 1 ? 11 
HELX_P HELX_P12 AB3 ASP B 32  ? GLY B 44  ? ASP B 12  GLY B 24  1 ? 13 
HELX_P HELX_P13 AB4 ASN B 52  ? THR B 65  ? ASN B 32  THR B 45  1 ? 14 
HELX_P HELX_P14 AB5 GLY B 81  ? ALA B 88  ? GLY B 61  ALA B 68  1 ? 8  
HELX_P HELX_P15 AB6 SER B 100 ? GLY B 114 ? SER B 80  GLY B 94  1 ? 15 
HELX_P HELX_P16 AB7 GLU B 135 ? THR B 144 ? GLU B 115 THR B 124 5 ? 10 
HELX_P HELX_P17 AB8 LEU B 171 ? LEU B 175 ? LEU B 151 LEU B 155 5 ? 5  
HELX_P HELX_P18 AB9 GLU B 177 ? GLU B 183 ? GLU B 157 GLU B 163 1 ? 7  
HELX_P HELX_P19 AC1 ASN B 184 ? LYS B 187 ? ASN B 164 LYS B 167 5 ? 4  
HELX_P HELX_P20 AC2 ALA B 209 ? TRP B 213 ? ALA B 189 TRP B 193 5 ? 5  
HELX_P HELX_P21 AC3 SER B 226 ? GLU B 236 ? SER B 206 GLU B 216 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 7 ? 
AA6 ? 2 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? 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 VAL A 146 ? GLN A 150 ? VAL A 126 GLN A 130 
AA1 2 HIS A 93  ? ASP A 98  ? HIS A 73  ASP A 78  
AA1 3 ARG A 72  ? LEU A 76  ? ARG A 52  LEU A 56  
AA1 4 TYR A 163 ? THR A 169 ? TYR A 143 THR A 149 
AA1 5 ILE A 189 ? SER A 199 ? ILE A 169 SER A 179 
AA1 6 PHE A 258 ? VAL A 270 ? PHE A 238 VAL A 250 
AA1 7 PHE A 239 ? ARG A 252 ? PHE A 219 ARG A 232 
AA2 1 CYS A 115 ? ASN A 121 ? CYS A 95  ASN A 101 
AA2 2 LYS A 127 ? ASP A 133 ? LYS A 107 ASP A 113 
AA3 1 TYR A 217 ? VAL A 218 ? TYR A 197 VAL A 198 
AA3 2 GLU A 224 ? VAL A 225 ? GLU A 204 VAL A 205 
AA4 1 TYR B 29  ? GLU B 30  ? TYR B 9   GLU B 10  
AA4 2 CYS B 115 ? ASN B 121 ? CYS B 95  ASN B 101 
AA4 3 LYS B 127 ? ASP B 133 ? LYS B 107 ASP B 113 
AA5 1 VAL B 146 ? GLN B 150 ? VAL B 126 GLN B 130 
AA5 2 HIS B 93  ? ASP B 98  ? HIS B 73  ASP B 78  
AA5 3 ARG B 72  ? LEU B 76  ? ARG B 52  LEU B 56  
AA5 4 TYR B 163 ? THR B 169 ? TYR B 143 THR B 149 
AA5 5 ILE B 189 ? SER B 199 ? ILE B 169 SER B 179 
AA5 6 PHE B 258 ? VAL B 270 ? PHE B 238 VAL B 250 
AA5 7 PHE B 239 ? ARG B 252 ? PHE B 219 ARG B 232 
AA6 1 TYR B 217 ? VAL B 218 ? TYR B 197 VAL B 198 
AA6 2 GLU B 224 ? VAL B 225 ? GLU B 204 VAL B 205 
# 
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 GLU A 147 ? O GLU A 127 N GLY A 96  ? N GLY A 76  
AA1 2 3 O ASP A 95  ? O ASP A 75  N ASP A 75  ? N ASP A 55  
AA1 3 4 N LEU A 74  ? N LEU A 54  O MET A 167 ? O MET A 147 
AA1 4 5 N TYR A 163 ? N TYR A 143 O ASN A 190 ? O ASN A 170 
AA1 5 6 N LEU A 195 ? N LEU A 175 O TRP A 268 ? O TRP A 248 
AA1 6 7 O VAL A 267 ? O VAL A 247 N VAL A 242 ? N VAL A 222 
AA2 1 2 N ILE A 116 ? N ILE A 96  O ILE A 132 ? O ILE A 112 
AA3 1 2 N TYR A 217 ? N TYR A 197 O VAL A 225 ? O VAL A 205 
AA4 1 2 N TYR B 29  ? N TYR B 9   O GLY B 117 ? O GLY B 97  
AA4 2 3 N GLN B 120 ? N GLN B 100 O ASN B 128 ? O ASN B 108 
AA5 1 2 O PHE B 149 ? O PHE B 129 N GLY B 96  ? N GLY B 76  
AA5 2 3 O ASP B 95  ? O ASP B 75  N ASP B 75  ? N ASP B 55  
AA5 3 4 N LEU B 74  ? N LEU B 54  O MET B 167 ? O MET B 147 
AA5 4 5 N ALA B 168 ? N ALA B 148 O ILE B 196 ? O ILE B 176 
AA5 5 6 N SER B 199 ? N SER B 179 O GLN B 264 ? O GLN B 244 
AA5 6 7 O MET B 265 ? O MET B 245 N GLU B 245 ? N GLU B 225 
AA6 1 2 N TYR B 217 ? N TYR B 197 O VAL B 225 ? O VAL B 205 
# 
_pdbx_entry_details.entry_id                   9BXN 
_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 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 59  ? ? 49.53   -128.26 
2 1 ASN A 135 ? ? -161.06 67.26   
3 1 ALA B 59  ? ? 50.84   -126.29 
4 1 ASN B 135 ? ? -155.69 60.63   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     159 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.198 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A PRO -4  ? A PRO 16  
17 1 Y 1 A ARG -3  ? A ARG 17  
18 1 Y 1 A GLY -2  ? A GLY 18  
19 1 Y 1 A SER -1  ? A SER 19  
20 1 Y 1 A HIS 0   ? A HIS 20  
21 1 Y 1 A MET 1   ? A MET 21  
22 1 Y 1 A ILE 2   ? A ILE 22  
23 1 Y 1 A PHE 3   ? A PHE 23  
24 1 Y 1 A LYS 4   ? A LYS 24  
25 1 Y 1 A SER 252 ? A SER 272 
26 1 Y 1 A THR 253 ? A THR 273 
27 1 Y 1 B MET -19 ? B MET 1   
28 1 Y 1 B GLY -18 ? B GLY 2   
29 1 Y 1 B SER -17 ? B SER 3   
30 1 Y 1 B SER -16 ? B SER 4   
31 1 Y 1 B HIS -15 ? B HIS 5   
32 1 Y 1 B HIS -14 ? B HIS 6   
33 1 Y 1 B HIS -13 ? B HIS 7   
34 1 Y 1 B HIS -12 ? B HIS 8   
35 1 Y 1 B HIS -11 ? B HIS 9   
36 1 Y 1 B HIS -10 ? B HIS 10  
37 1 Y 1 B SER -9  ? B SER 11  
38 1 Y 1 B SER -8  ? B SER 12  
39 1 Y 1 B GLY -7  ? B GLY 13  
40 1 Y 1 B LEU -6  ? B LEU 14  
41 1 Y 1 B VAL -5  ? B VAL 15  
42 1 Y 1 B PRO -4  ? B PRO 16  
43 1 Y 1 B ARG -3  ? B ARG 17  
44 1 Y 1 B GLY -2  ? B GLY 18  
45 1 Y 1 B SER -1  ? B SER 19  
46 1 Y 1 B HIS 0   ? B HIS 20  
47 1 Y 1 B MET 1   ? B MET 21  
48 1 Y 1 B ILE 2   ? B ILE 22  
49 1 Y 1 B PHE 3   ? B PHE 23  
50 1 Y 1 B LYS 4   ? B LYS 24  
51 1 Y 1 B GLU 5   ? B GLU 25  
52 1 Y 1 B LYS 6   ? B LYS 26  
53 1 Y 1 B SER 252 ? B SER 272 
54 1 Y 1 B THR 253 ? B THR 273 
# 
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 
A1ASZ N      N N N 1   
A1ASZ CA     C N R 2   
A1ASZ C      C N N 3   
A1ASZ O      O N N 4   
A1ASZ CB     C N N 5   
A1ASZ CG     C Y N 6   
A1ASZ ND1    N Y N 7   
A1ASZ CD2    C Y N 8   
A1ASZ CE1    C Y N 9   
A1ASZ NE2    N Y N 10  
A1ASZ OXT    O N N 11  
A1ASZ S1     S N N 12  
A1ASZ H2     H N N 13  
A1ASZ H      H N N 14  
A1ASZ HA     H N N 15  
A1ASZ HB3    H N N 16  
A1ASZ HB2    H N N 17  
A1ASZ HE1    H N N 18  
A1ASZ HE2    H N N 19  
A1ASZ HXT    H N N 20  
A1ASZ HS1    H N N 21  
ALA   N      N N N 22  
ALA   CA     C N S 23  
ALA   C      C N N 24  
ALA   O      O N N 25  
ALA   CB     C N N 26  
ALA   OXT    O N N 27  
ALA   H      H N N 28  
ALA   H2     H N N 29  
ALA   HA     H N N 30  
ALA   HB1    H N N 31  
ALA   HB2    H N N 32  
ALA   HB3    H N N 33  
ALA   HXT    H N N 34  
ARG   N      N N N 35  
ARG   CA     C N S 36  
ARG   C      C N N 37  
ARG   O      O N N 38  
ARG   CB     C N N 39  
ARG   CG     C N N 40  
ARG   CD     C N N 41  
ARG   NE     N N N 42  
ARG   CZ     C N N 43  
ARG   NH1    N N N 44  
ARG   NH2    N N N 45  
ARG   OXT    O N N 46  
ARG   H      H N N 47  
ARG   H2     H N N 48  
ARG   HA     H N N 49  
ARG   HB2    H N N 50  
ARG   HB3    H N N 51  
ARG   HG2    H N N 52  
ARG   HG3    H N N 53  
ARG   HD2    H N N 54  
ARG   HD3    H N N 55  
ARG   HE     H N N 56  
ARG   HH11   H N N 57  
ARG   HH12   H N N 58  
ARG   HH21   H N N 59  
ARG   HH22   H N N 60  
ARG   HXT    H N N 61  
ASN   N      N N N 62  
ASN   CA     C N S 63  
ASN   C      C N N 64  
ASN   O      O N N 65  
ASN   CB     C N N 66  
ASN   CG     C N N 67  
ASN   OD1    O N N 68  
ASN   ND2    N N N 69  
ASN   OXT    O N N 70  
ASN   H      H N N 71  
ASN   H2     H N N 72  
ASN   HA     H N N 73  
ASN   HB2    H N N 74  
ASN   HB3    H N N 75  
ASN   HD21   H N N 76  
ASN   HD22   H N N 77  
ASN   HXT    H N N 78  
ASP   N      N N N 79  
ASP   CA     C N S 80  
ASP   C      C N N 81  
ASP   O      O N N 82  
ASP   CB     C N N 83  
ASP   CG     C N N 84  
ASP   OD1    O N N 85  
ASP   OD2    O N N 86  
ASP   OXT    O N N 87  
ASP   H      H N N 88  
ASP   H2     H N N 89  
ASP   HA     H N N 90  
ASP   HB2    H N N 91  
ASP   HB3    H N N 92  
ASP   HD2    H N N 93  
ASP   HXT    H N N 94  
CYS   N      N N N 95  
CYS   CA     C N R 96  
CYS   C      C N N 97  
CYS   O      O N N 98  
CYS   CB     C N N 99  
CYS   SG     S N N 100 
CYS   OXT    O N N 101 
CYS   H      H N N 102 
CYS   H2     H N N 103 
CYS   HA     H N N 104 
CYS   HB2    H N N 105 
CYS   HB3    H N N 106 
CYS   HG     H N N 107 
CYS   HXT    H N N 108 
EDO   C1     C N N 109 
EDO   O1     O N N 110 
EDO   C2     C N N 111 
EDO   O2     O N N 112 
EDO   H11    H N N 113 
EDO   H12    H N N 114 
EDO   HO1    H N N 115 
EDO   H21    H N N 116 
EDO   H22    H N N 117 
EDO   HO2    H N N 118 
GLN   N      N N N 119 
GLN   CA     C N S 120 
GLN   C      C N N 121 
GLN   O      O N N 122 
GLN   CB     C N N 123 
GLN   CG     C N N 124 
GLN   CD     C N N 125 
GLN   OE1    O N N 126 
GLN   NE2    N N N 127 
GLN   OXT    O N N 128 
GLN   H      H N N 129 
GLN   H2     H N N 130 
GLN   HA     H N N 131 
GLN   HB2    H N N 132 
GLN   HB3    H N N 133 
GLN   HG2    H N N 134 
GLN   HG3    H N N 135 
GLN   HE21   H N N 136 
GLN   HE22   H N N 137 
GLN   HXT    H N N 138 
GLU   N      N N N 139 
GLU   CA     C N S 140 
GLU   C      C N N 141 
GLU   O      O N N 142 
GLU   CB     C N N 143 
GLU   CG     C N N 144 
GLU   CD     C N N 145 
GLU   OE1    O N N 146 
GLU   OE2    O N N 147 
GLU   OXT    O N N 148 
GLU   H      H N N 149 
GLU   H2     H N N 150 
GLU   HA     H N N 151 
GLU   HB2    H N N 152 
GLU   HB3    H N N 153 
GLU   HG2    H N N 154 
GLU   HG3    H N N 155 
GLU   HE2    H N N 156 
GLU   HXT    H N N 157 
GLY   N      N N N 158 
GLY   CA     C N N 159 
GLY   C      C N N 160 
GLY   O      O N N 161 
GLY   OXT    O N N 162 
GLY   H      H N N 163 
GLY   H2     H N N 164 
GLY   HA2    H N N 165 
GLY   HA3    H N N 166 
GLY   HXT    H N N 167 
HIS   N      N N N 168 
HIS   CA     C N S 169 
HIS   C      C N N 170 
HIS   O      O N N 171 
HIS   CB     C N N 172 
HIS   CG     C Y N 173 
HIS   ND1    N Y N 174 
HIS   CD2    C Y N 175 
HIS   CE1    C Y N 176 
HIS   NE2    N Y N 177 
HIS   OXT    O N N 178 
HIS   H      H N N 179 
HIS   H2     H N N 180 
HIS   HA     H N N 181 
HIS   HB2    H N N 182 
HIS   HB3    H N N 183 
HIS   HD1    H N N 184 
HIS   HD2    H N N 185 
HIS   HE1    H N N 186 
HIS   HE2    H N N 187 
HIS   HXT    H N N 188 
HOH   O      O N N 189 
HOH   H1     H N N 190 
HOH   H2     H N N 191 
ILE   N      N N N 192 
ILE   CA     C N S 193 
ILE   C      C N N 194 
ILE   O      O N N 195 
ILE   CB     C N S 196 
ILE   CG1    C N N 197 
ILE   CG2    C N N 198 
ILE   CD1    C N N 199 
ILE   OXT    O N N 200 
ILE   H      H N N 201 
ILE   H2     H N N 202 
ILE   HA     H N N 203 
ILE   HB     H N N 204 
ILE   HG12   H N N 205 
ILE   HG13   H N N 206 
ILE   HG21   H N N 207 
ILE   HG22   H N N 208 
ILE   HG23   H N N 209 
ILE   HD11   H N N 210 
ILE   HD12   H N N 211 
ILE   HD13   H N N 212 
ILE   HXT    H N N 213 
LEU   N      N N N 214 
LEU   CA     C N S 215 
LEU   C      C N N 216 
LEU   O      O N N 217 
LEU   CB     C N N 218 
LEU   CG     C N N 219 
LEU   CD1    C N N 220 
LEU   CD2    C N N 221 
LEU   OXT    O N N 222 
LEU   H      H N N 223 
LEU   H2     H N N 224 
LEU   HA     H N N 225 
LEU   HB2    H N N 226 
LEU   HB3    H N N 227 
LEU   HG     H N N 228 
LEU   HD11   H N N 229 
LEU   HD12   H N N 230 
LEU   HD13   H N N 231 
LEU   HD21   H N N 232 
LEU   HD22   H N N 233 
LEU   HD23   H N N 234 
LEU   HXT    H N N 235 
LYS   N      N N N 236 
LYS   CA     C N S 237 
LYS   C      C N N 238 
LYS   O      O N N 239 
LYS   CB     C N N 240 
LYS   CG     C N N 241 
LYS   CD     C N N 242 
LYS   CE     C N N 243 
LYS   NZ     N N N 244 
LYS   OXT    O N N 245 
LYS   H      H N N 246 
LYS   H2     H N N 247 
LYS   HA     H N N 248 
LYS   HB2    H N N 249 
LYS   HB3    H N N 250 
LYS   HG2    H N N 251 
LYS   HG3    H N N 252 
LYS   HD2    H N N 253 
LYS   HD3    H N N 254 
LYS   HE2    H N N 255 
LYS   HE3    H N N 256 
LYS   HZ1    H N N 257 
LYS   HZ2    H N N 258 
LYS   HZ3    H N N 259 
LYS   HXT    H N N 260 
MET   N      N N N 261 
MET   CA     C N S 262 
MET   C      C N N 263 
MET   O      O N N 264 
MET   CB     C N N 265 
MET   CG     C N N 266 
MET   SD     S N N 267 
MET   CE     C N N 268 
MET   OXT    O N N 269 
MET   H      H N N 270 
MET   H2     H N N 271 
MET   HA     H N N 272 
MET   HB2    H N N 273 
MET   HB3    H N N 274 
MET   HG2    H N N 275 
MET   HG3    H N N 276 
MET   HE1    H N N 277 
MET   HE2    H N N 278 
MET   HE3    H N N 279 
MET   HXT    H N N 280 
PHE   N      N N N 281 
PHE   CA     C N S 282 
PHE   C      C N N 283 
PHE   O      O N N 284 
PHE   CB     C N N 285 
PHE   CG     C Y N 286 
PHE   CD1    C Y N 287 
PHE   CD2    C Y N 288 
PHE   CE1    C Y N 289 
PHE   CE2    C Y N 290 
PHE   CZ     C Y N 291 
PHE   OXT    O N N 292 
PHE   H      H N N 293 
PHE   H2     H N N 294 
PHE   HA     H N N 295 
PHE   HB2    H N N 296 
PHE   HB3    H N N 297 
PHE   HD1    H N N 298 
PHE   HD2    H N N 299 
PHE   HE1    H N N 300 
PHE   HE2    H N N 301 
PHE   HZ     H N N 302 
PHE   HXT    H N N 303 
PRO   N      N N N 304 
PRO   CA     C N S 305 
PRO   C      C N N 306 
PRO   O      O N N 307 
PRO   CB     C N N 308 
PRO   CG     C N N 309 
PRO   CD     C N N 310 
PRO   OXT    O N N 311 
PRO   H      H N N 312 
PRO   HA     H N N 313 
PRO   HB2    H N N 314 
PRO   HB3    H N N 315 
PRO   HG2    H N N 316 
PRO   HG3    H N N 317 
PRO   HD2    H N N 318 
PRO   HD3    H N N 319 
PRO   HXT    H N N 320 
SAH   N      N N N 321 
SAH   CA     C N S 322 
SAH   CB     C N N 323 
SAH   CG     C N N 324 
SAH   SD     S N N 325 
SAH   C      C N N 326 
SAH   O      O N N 327 
SAH   OXT    O N N 328 
SAH   "C5'"  C N N 329 
SAH   "C4'"  C N S 330 
SAH   "O4'"  O N N 331 
SAH   "C3'"  C N S 332 
SAH   "O3'"  O N N 333 
SAH   "C2'"  C N R 334 
SAH   "O2'"  O N N 335 
SAH   "C1'"  C N R 336 
SAH   N9     N Y N 337 
SAH   C8     C Y N 338 
SAH   N7     N Y N 339 
SAH   C5     C Y N 340 
SAH   C6     C Y N 341 
SAH   N6     N N N 342 
SAH   N1     N Y N 343 
SAH   C2     C Y N 344 
SAH   N3     N Y N 345 
SAH   C4     C Y N 346 
SAH   HN1    H N N 347 
SAH   HN2    H N N 348 
SAH   HA     H N N 349 
SAH   HB1    H N N 350 
SAH   HB2    H N N 351 
SAH   HG1    H N N 352 
SAH   HG2    H N N 353 
SAH   HXT    H N N 354 
SAH   "H5'1" H N N 355 
SAH   "H5'2" H N N 356 
SAH   "H4'"  H N N 357 
SAH   "H3'"  H N N 358 
SAH   "HO3'" H N N 359 
SAH   "H2'"  H N N 360 
SAH   "HO2'" H N N 361 
SAH   "H1'"  H N N 362 
SAH   H8     H N N 363 
SAH   HN61   H N N 364 
SAH   HN62   H N N 365 
SAH   H2     H N N 366 
SER   N      N N N 367 
SER   CA     C N S 368 
SER   C      C N N 369 
SER   O      O N N 370 
SER   CB     C N N 371 
SER   OG     O N N 372 
SER   OXT    O N N 373 
SER   H      H N N 374 
SER   H2     H N N 375 
SER   HA     H N N 376 
SER   HB2    H N N 377 
SER   HB3    H N N 378 
SER   HG     H N N 379 
SER   HXT    H N N 380 
THR   N      N N N 381 
THR   CA     C N S 382 
THR   C      C N N 383 
THR   O      O N N 384 
THR   CB     C N R 385 
THR   OG1    O N N 386 
THR   CG2    C N N 387 
THR   OXT    O N N 388 
THR   H      H N N 389 
THR   H2     H N N 390 
THR   HA     H N N 391 
THR   HB     H N N 392 
THR   HG1    H N N 393 
THR   HG21   H N N 394 
THR   HG22   H N N 395 
THR   HG23   H N N 396 
THR   HXT    H N N 397 
TRP   N      N N N 398 
TRP   CA     C N S 399 
TRP   C      C N N 400 
TRP   O      O N N 401 
TRP   CB     C N N 402 
TRP   CG     C Y N 403 
TRP   CD1    C Y N 404 
TRP   CD2    C Y N 405 
TRP   NE1    N Y N 406 
TRP   CE2    C Y N 407 
TRP   CE3    C Y N 408 
TRP   CZ2    C Y N 409 
TRP   CZ3    C Y N 410 
TRP   CH2    C Y N 411 
TRP   OXT    O N N 412 
TRP   H      H N N 413 
TRP   H2     H N N 414 
TRP   HA     H N N 415 
TRP   HB2    H N N 416 
TRP   HB3    H N N 417 
TRP   HD1    H N N 418 
TRP   HE1    H N N 419 
TRP   HE3    H N N 420 
TRP   HZ2    H N N 421 
TRP   HZ3    H N N 422 
TRP   HH2    H N N 423 
TRP   HXT    H N N 424 
TYR   N      N N N 425 
TYR   CA     C N S 426 
TYR   C      C N N 427 
TYR   O      O N N 428 
TYR   CB     C N N 429 
TYR   CG     C Y N 430 
TYR   CD1    C Y N 431 
TYR   CD2    C Y N 432 
TYR   CE1    C Y N 433 
TYR   CE2    C Y N 434 
TYR   CZ     C Y N 435 
TYR   OH     O N N 436 
TYR   OXT    O N N 437 
TYR   H      H N N 438 
TYR   H2     H N N 439 
TYR   HA     H N N 440 
TYR   HB2    H N N 441 
TYR   HB3    H N N 442 
TYR   HD1    H N N 443 
TYR   HD2    H N N 444 
TYR   HE1    H N N 445 
TYR   HE2    H N N 446 
TYR   HH     H N N 447 
TYR   HXT    H N N 448 
VAL   N      N N N 449 
VAL   CA     C N S 450 
VAL   C      C N N 451 
VAL   O      O N N 452 
VAL   CB     C N N 453 
VAL   CG1    C N N 454 
VAL   CG2    C N N 455 
VAL   OXT    O N N 456 
VAL   H      H N N 457 
VAL   H2     H N N 458 
VAL   HA     H N N 459 
VAL   HB     H N N 460 
VAL   HG11   H N N 461 
VAL   HG12   H N N 462 
VAL   HG13   H N N 463 
VAL   HG21   H N N 464 
VAL   HG22   H N N 465 
VAL   HG23   H N N 466 
VAL   HXT    H N N 467 
# 
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 
A1ASZ N     CA     sing N N 1   
A1ASZ CA    C      sing N N 2   
A1ASZ CA    CB     sing N N 3   
A1ASZ C     O      doub N N 4   
A1ASZ C     OXT    sing N N 5   
A1ASZ CB    CG     sing N N 6   
A1ASZ CG    ND1    sing Y N 7   
A1ASZ CG    CD2    doub Y N 8   
A1ASZ ND1   CE1    doub Y N 9   
A1ASZ CD2   NE2    sing Y N 10  
A1ASZ CD2   S1     sing N N 11  
A1ASZ CE1   NE2    sing Y N 12  
A1ASZ N     H2     sing N N 13  
A1ASZ N     H      sing N N 14  
A1ASZ CA    HA     sing N N 15  
A1ASZ CB    HB3    sing N N 16  
A1ASZ CB    HB2    sing N N 17  
A1ASZ CE1   HE1    sing N N 18  
A1ASZ NE2   HE2    sing N N 19  
A1ASZ OXT   HXT    sing N N 20  
A1ASZ S1    HS1    sing N N 21  
ALA   N     CA     sing N N 22  
ALA   N     H      sing N N 23  
ALA   N     H2     sing N N 24  
ALA   CA    C      sing N N 25  
ALA   CA    CB     sing N N 26  
ALA   CA    HA     sing N N 27  
ALA   C     O      doub N N 28  
ALA   C     OXT    sing N N 29  
ALA   CB    HB1    sing N N 30  
ALA   CB    HB2    sing N N 31  
ALA   CB    HB3    sing N N 32  
ALA   OXT   HXT    sing N N 33  
ARG   N     CA     sing N N 34  
ARG   N     H      sing N N 35  
ARG   N     H2     sing N N 36  
ARG   CA    C      sing N N 37  
ARG   CA    CB     sing N N 38  
ARG   CA    HA     sing N N 39  
ARG   C     O      doub N N 40  
ARG   C     OXT    sing N N 41  
ARG   CB    CG     sing N N 42  
ARG   CB    HB2    sing N N 43  
ARG   CB    HB3    sing N N 44  
ARG   CG    CD     sing N N 45  
ARG   CG    HG2    sing N N 46  
ARG   CG    HG3    sing N N 47  
ARG   CD    NE     sing N N 48  
ARG   CD    HD2    sing N N 49  
ARG   CD    HD3    sing N N 50  
ARG   NE    CZ     sing N N 51  
ARG   NE    HE     sing N N 52  
ARG   CZ    NH1    sing N N 53  
ARG   CZ    NH2    doub N N 54  
ARG   NH1   HH11   sing N N 55  
ARG   NH1   HH12   sing N N 56  
ARG   NH2   HH21   sing N N 57  
ARG   NH2   HH22   sing N N 58  
ARG   OXT   HXT    sing N N 59  
ASN   N     CA     sing N N 60  
ASN   N     H      sing N N 61  
ASN   N     H2     sing N N 62  
ASN   CA    C      sing N N 63  
ASN   CA    CB     sing N N 64  
ASN   CA    HA     sing N N 65  
ASN   C     O      doub N N 66  
ASN   C     OXT    sing N N 67  
ASN   CB    CG     sing N N 68  
ASN   CB    HB2    sing N N 69  
ASN   CB    HB3    sing N N 70  
ASN   CG    OD1    doub N N 71  
ASN   CG    ND2    sing N N 72  
ASN   ND2   HD21   sing N N 73  
ASN   ND2   HD22   sing N N 74  
ASN   OXT   HXT    sing N N 75  
ASP   N     CA     sing N N 76  
ASP   N     H      sing N N 77  
ASP   N     H2     sing N N 78  
ASP   CA    C      sing N N 79  
ASP   CA    CB     sing N N 80  
ASP   CA    HA     sing N N 81  
ASP   C     O      doub N N 82  
ASP   C     OXT    sing N N 83  
ASP   CB    CG     sing N N 84  
ASP   CB    HB2    sing N N 85  
ASP   CB    HB3    sing N N 86  
ASP   CG    OD1    doub N N 87  
ASP   CG    OD2    sing N N 88  
ASP   OD2   HD2    sing N N 89  
ASP   OXT   HXT    sing N N 90  
CYS   N     CA     sing N N 91  
CYS   N     H      sing N N 92  
CYS   N     H2     sing N N 93  
CYS   CA    C      sing N N 94  
CYS   CA    CB     sing N N 95  
CYS   CA    HA     sing N N 96  
CYS   C     O      doub N N 97  
CYS   C     OXT    sing N N 98  
CYS   CB    SG     sing N N 99  
CYS   CB    HB2    sing N N 100 
CYS   CB    HB3    sing N N 101 
CYS   SG    HG     sing N N 102 
CYS   OXT   HXT    sing N N 103 
EDO   C1    O1     sing N N 104 
EDO   C1    C2     sing N N 105 
EDO   C1    H11    sing N N 106 
EDO   C1    H12    sing N N 107 
EDO   O1    HO1    sing N N 108 
EDO   C2    O2     sing N N 109 
EDO   C2    H21    sing N N 110 
EDO   C2    H22    sing N N 111 
EDO   O2    HO2    sing N N 112 
GLN   N     CA     sing N N 113 
GLN   N     H      sing N N 114 
GLN   N     H2     sing N N 115 
GLN   CA    C      sing N N 116 
GLN   CA    CB     sing N N 117 
GLN   CA    HA     sing N N 118 
GLN   C     O      doub N N 119 
GLN   C     OXT    sing N N 120 
GLN   CB    CG     sing N N 121 
GLN   CB    HB2    sing N N 122 
GLN   CB    HB3    sing N N 123 
GLN   CG    CD     sing N N 124 
GLN   CG    HG2    sing N N 125 
GLN   CG    HG3    sing N N 126 
GLN   CD    OE1    doub N N 127 
GLN   CD    NE2    sing N N 128 
GLN   NE2   HE21   sing N N 129 
GLN   NE2   HE22   sing N N 130 
GLN   OXT   HXT    sing N N 131 
GLU   N     CA     sing N N 132 
GLU   N     H      sing N N 133 
GLU   N     H2     sing N N 134 
GLU   CA    C      sing N N 135 
GLU   CA    CB     sing N N 136 
GLU   CA    HA     sing N N 137 
GLU   C     O      doub N N 138 
GLU   C     OXT    sing N N 139 
GLU   CB    CG     sing N N 140 
GLU   CB    HB2    sing N N 141 
GLU   CB    HB3    sing N N 142 
GLU   CG    CD     sing N N 143 
GLU   CG    HG2    sing N N 144 
GLU   CG    HG3    sing N N 145 
GLU   CD    OE1    doub N N 146 
GLU   CD    OE2    sing N N 147 
GLU   OE2   HE2    sing N N 148 
GLU   OXT   HXT    sing N N 149 
GLY   N     CA     sing N N 150 
GLY   N     H      sing N N 151 
GLY   N     H2     sing N N 152 
GLY   CA    C      sing N N 153 
GLY   CA    HA2    sing N N 154 
GLY   CA    HA3    sing N N 155 
GLY   C     O      doub N N 156 
GLY   C     OXT    sing N N 157 
GLY   OXT   HXT    sing N N 158 
HIS   N     CA     sing N N 159 
HIS   N     H      sing N N 160 
HIS   N     H2     sing N N 161 
HIS   CA    C      sing N N 162 
HIS   CA    CB     sing N N 163 
HIS   CA    HA     sing N N 164 
HIS   C     O      doub N N 165 
HIS   C     OXT    sing N N 166 
HIS   CB    CG     sing N N 167 
HIS   CB    HB2    sing N N 168 
HIS   CB    HB3    sing N N 169 
HIS   CG    ND1    sing Y N 170 
HIS   CG    CD2    doub Y N 171 
HIS   ND1   CE1    doub Y N 172 
HIS   ND1   HD1    sing N N 173 
HIS   CD2   NE2    sing Y N 174 
HIS   CD2   HD2    sing N N 175 
HIS   CE1   NE2    sing Y N 176 
HIS   CE1   HE1    sing N N 177 
HIS   NE2   HE2    sing N N 178 
HIS   OXT   HXT    sing N N 179 
HOH   O     H1     sing N N 180 
HOH   O     H2     sing N N 181 
ILE   N     CA     sing N N 182 
ILE   N     H      sing N N 183 
ILE   N     H2     sing N N 184 
ILE   CA    C      sing N N 185 
ILE   CA    CB     sing N N 186 
ILE   CA    HA     sing N N 187 
ILE   C     O      doub N N 188 
ILE   C     OXT    sing N N 189 
ILE   CB    CG1    sing N N 190 
ILE   CB    CG2    sing N N 191 
ILE   CB    HB     sing N N 192 
ILE   CG1   CD1    sing N N 193 
ILE   CG1   HG12   sing N N 194 
ILE   CG1   HG13   sing N N 195 
ILE   CG2   HG21   sing N N 196 
ILE   CG2   HG22   sing N N 197 
ILE   CG2   HG23   sing N N 198 
ILE   CD1   HD11   sing N N 199 
ILE   CD1   HD12   sing N N 200 
ILE   CD1   HD13   sing N N 201 
ILE   OXT   HXT    sing N N 202 
LEU   N     CA     sing N N 203 
LEU   N     H      sing N N 204 
LEU   N     H2     sing N N 205 
LEU   CA    C      sing N N 206 
LEU   CA    CB     sing N N 207 
LEU   CA    HA     sing N N 208 
LEU   C     O      doub N N 209 
LEU   C     OXT    sing N N 210 
LEU   CB    CG     sing N N 211 
LEU   CB    HB2    sing N N 212 
LEU   CB    HB3    sing N N 213 
LEU   CG    CD1    sing N N 214 
LEU   CG    CD2    sing N N 215 
LEU   CG    HG     sing N N 216 
LEU   CD1   HD11   sing N N 217 
LEU   CD1   HD12   sing N N 218 
LEU   CD1   HD13   sing N N 219 
LEU   CD2   HD21   sing N N 220 
LEU   CD2   HD22   sing N N 221 
LEU   CD2   HD23   sing N N 222 
LEU   OXT   HXT    sing N N 223 
LYS   N     CA     sing N N 224 
LYS   N     H      sing N N 225 
LYS   N     H2     sing N N 226 
LYS   CA    C      sing N N 227 
LYS   CA    CB     sing N N 228 
LYS   CA    HA     sing N N 229 
LYS   C     O      doub N N 230 
LYS   C     OXT    sing N N 231 
LYS   CB    CG     sing N N 232 
LYS   CB    HB2    sing N N 233 
LYS   CB    HB3    sing N N 234 
LYS   CG    CD     sing N N 235 
LYS   CG    HG2    sing N N 236 
LYS   CG    HG3    sing N N 237 
LYS   CD    CE     sing N N 238 
LYS   CD    HD2    sing N N 239 
LYS   CD    HD3    sing N N 240 
LYS   CE    NZ     sing N N 241 
LYS   CE    HE2    sing N N 242 
LYS   CE    HE3    sing N N 243 
LYS   NZ    HZ1    sing N N 244 
LYS   NZ    HZ2    sing N N 245 
LYS   NZ    HZ3    sing N N 246 
LYS   OXT   HXT    sing N N 247 
MET   N     CA     sing N N 248 
MET   N     H      sing N N 249 
MET   N     H2     sing N N 250 
MET   CA    C      sing N N 251 
MET   CA    CB     sing N N 252 
MET   CA    HA     sing N N 253 
MET   C     O      doub N N 254 
MET   C     OXT    sing N N 255 
MET   CB    CG     sing N N 256 
MET   CB    HB2    sing N N 257 
MET   CB    HB3    sing N N 258 
MET   CG    SD     sing N N 259 
MET   CG    HG2    sing N N 260 
MET   CG    HG3    sing N N 261 
MET   SD    CE     sing N N 262 
MET   CE    HE1    sing N N 263 
MET   CE    HE2    sing N N 264 
MET   CE    HE3    sing N N 265 
MET   OXT   HXT    sing N N 266 
PHE   N     CA     sing N N 267 
PHE   N     H      sing N N 268 
PHE   N     H2     sing N N 269 
PHE   CA    C      sing N N 270 
PHE   CA    CB     sing N N 271 
PHE   CA    HA     sing N N 272 
PHE   C     O      doub N N 273 
PHE   C     OXT    sing N N 274 
PHE   CB    CG     sing N N 275 
PHE   CB    HB2    sing N N 276 
PHE   CB    HB3    sing N N 277 
PHE   CG    CD1    doub Y N 278 
PHE   CG    CD2    sing Y N 279 
PHE   CD1   CE1    sing Y N 280 
PHE   CD1   HD1    sing N N 281 
PHE   CD2   CE2    doub Y N 282 
PHE   CD2   HD2    sing N N 283 
PHE   CE1   CZ     doub Y N 284 
PHE   CE1   HE1    sing N N 285 
PHE   CE2   CZ     sing Y N 286 
PHE   CE2   HE2    sing N N 287 
PHE   CZ    HZ     sing N N 288 
PHE   OXT   HXT    sing N N 289 
PRO   N     CA     sing N N 290 
PRO   N     CD     sing N N 291 
PRO   N     H      sing N N 292 
PRO   CA    C      sing N N 293 
PRO   CA    CB     sing N N 294 
PRO   CA    HA     sing N N 295 
PRO   C     O      doub N N 296 
PRO   C     OXT    sing N N 297 
PRO   CB    CG     sing N N 298 
PRO   CB    HB2    sing N N 299 
PRO   CB    HB3    sing N N 300 
PRO   CG    CD     sing N N 301 
PRO   CG    HG2    sing N N 302 
PRO   CG    HG3    sing N N 303 
PRO   CD    HD2    sing N N 304 
PRO   CD    HD3    sing N N 305 
PRO   OXT   HXT    sing N N 306 
SAH   N     CA     sing N N 307 
SAH   N     HN1    sing N N 308 
SAH   N     HN2    sing N N 309 
SAH   CA    CB     sing N N 310 
SAH   CA    C      sing N N 311 
SAH   CA    HA     sing N N 312 
SAH   CB    CG     sing N N 313 
SAH   CB    HB1    sing N N 314 
SAH   CB    HB2    sing N N 315 
SAH   CG    SD     sing N N 316 
SAH   CG    HG1    sing N N 317 
SAH   CG    HG2    sing N N 318 
SAH   SD    "C5'"  sing N N 319 
SAH   C     O      doub N N 320 
SAH   C     OXT    sing N N 321 
SAH   OXT   HXT    sing N N 322 
SAH   "C5'" "C4'"  sing N N 323 
SAH   "C5'" "H5'1" sing N N 324 
SAH   "C5'" "H5'2" sing N N 325 
SAH   "C4'" "O4'"  sing N N 326 
SAH   "C4'" "C3'"  sing N N 327 
SAH   "C4'" "H4'"  sing N N 328 
SAH   "O4'" "C1'"  sing N N 329 
SAH   "C3'" "O3'"  sing N N 330 
SAH   "C3'" "C2'"  sing N N 331 
SAH   "C3'" "H3'"  sing N N 332 
SAH   "O3'" "HO3'" sing N N 333 
SAH   "C2'" "O2'"  sing N N 334 
SAH   "C2'" "C1'"  sing N N 335 
SAH   "C2'" "H2'"  sing N N 336 
SAH   "O2'" "HO2'" sing N N 337 
SAH   "C1'" N9     sing N N 338 
SAH   "C1'" "H1'"  sing N N 339 
SAH   N9    C8     sing Y N 340 
SAH   N9    C4     sing Y N 341 
SAH   C8    N7     doub Y N 342 
SAH   C8    H8     sing N N 343 
SAH   N7    C5     sing Y N 344 
SAH   C5    C6     sing Y N 345 
SAH   C5    C4     doub Y N 346 
SAH   C6    N6     sing N N 347 
SAH   C6    N1     doub Y N 348 
SAH   N6    HN61   sing N N 349 
SAH   N6    HN62   sing N N 350 
SAH   N1    C2     sing Y N 351 
SAH   C2    N3     doub Y N 352 
SAH   C2    H2     sing N N 353 
SAH   N3    C4     sing Y N 354 
SER   N     CA     sing N N 355 
SER   N     H      sing N N 356 
SER   N     H2     sing N N 357 
SER   CA    C      sing N N 358 
SER   CA    CB     sing N N 359 
SER   CA    HA     sing N N 360 
SER   C     O      doub N N 361 
SER   C     OXT    sing N N 362 
SER   CB    OG     sing N N 363 
SER   CB    HB2    sing N N 364 
SER   CB    HB3    sing N N 365 
SER   OG    HG     sing N N 366 
SER   OXT   HXT    sing N N 367 
THR   N     CA     sing N N 368 
THR   N     H      sing N N 369 
THR   N     H2     sing N N 370 
THR   CA    C      sing N N 371 
THR   CA    CB     sing N N 372 
THR   CA    HA     sing N N 373 
THR   C     O      doub N N 374 
THR   C     OXT    sing N N 375 
THR   CB    OG1    sing N N 376 
THR   CB    CG2    sing N N 377 
THR   CB    HB     sing N N 378 
THR   OG1   HG1    sing N N 379 
THR   CG2   HG21   sing N N 380 
THR   CG2   HG22   sing N N 381 
THR   CG2   HG23   sing N N 382 
THR   OXT   HXT    sing N N 383 
TRP   N     CA     sing N N 384 
TRP   N     H      sing N N 385 
TRP   N     H2     sing N N 386 
TRP   CA    C      sing N N 387 
TRP   CA    CB     sing N N 388 
TRP   CA    HA     sing N N 389 
TRP   C     O      doub N N 390 
TRP   C     OXT    sing N N 391 
TRP   CB    CG     sing N N 392 
TRP   CB    HB2    sing N N 393 
TRP   CB    HB3    sing N N 394 
TRP   CG    CD1    doub Y N 395 
TRP   CG    CD2    sing Y N 396 
TRP   CD1   NE1    sing Y N 397 
TRP   CD1   HD1    sing N N 398 
TRP   CD2   CE2    doub Y N 399 
TRP   CD2   CE3    sing Y N 400 
TRP   NE1   CE2    sing Y N 401 
TRP   NE1   HE1    sing N N 402 
TRP   CE2   CZ2    sing Y N 403 
TRP   CE3   CZ3    doub Y N 404 
TRP   CE3   HE3    sing N N 405 
TRP   CZ2   CH2    doub Y N 406 
TRP   CZ2   HZ2    sing N N 407 
TRP   CZ3   CH2    sing Y N 408 
TRP   CZ3   HZ3    sing N N 409 
TRP   CH2   HH2    sing N N 410 
TRP   OXT   HXT    sing N N 411 
TYR   N     CA     sing N N 412 
TYR   N     H      sing N N 413 
TYR   N     H2     sing N N 414 
TYR   CA    C      sing N N 415 
TYR   CA    CB     sing N N 416 
TYR   CA    HA     sing N N 417 
TYR   C     O      doub N N 418 
TYR   C     OXT    sing N N 419 
TYR   CB    CG     sing N N 420 
TYR   CB    HB2    sing N N 421 
TYR   CB    HB3    sing N N 422 
TYR   CG    CD1    doub Y N 423 
TYR   CG    CD2    sing Y N 424 
TYR   CD1   CE1    sing Y N 425 
TYR   CD1   HD1    sing N N 426 
TYR   CD2   CE2    doub Y N 427 
TYR   CD2   HD2    sing N N 428 
TYR   CE1   CZ     doub Y N 429 
TYR   CE1   HE1    sing N N 430 
TYR   CE2   CZ     sing Y N 431 
TYR   CE2   HE2    sing N N 432 
TYR   CZ    OH     sing N N 433 
TYR   OH    HH     sing N N 434 
TYR   OXT   HXT    sing N N 435 
VAL   N     CA     sing N N 436 
VAL   N     H      sing N N 437 
VAL   N     H2     sing N N 438 
VAL   CA    C      sing N N 439 
VAL   CA    CB     sing N N 440 
VAL   CA    HA     sing N N 441 
VAL   C     O      doub N N 442 
VAL   C     OXT    sing N N 443 
VAL   CB    CG1    sing N N 444 
VAL   CB    CG2    sing N N 445 
VAL   CB    HB     sing N N 446 
VAL   CG1   HG11   sing N N 447 
VAL   CG1   HG12   sing N N 448 
VAL   CG1   HG13   sing N N 449 
VAL   CG2   HG21   sing N N 450 
VAL   CG2   HG22   sing N N 451 
VAL   CG2   HG23   sing N N 452 
VAL   OXT   HXT    sing N N 453 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)'                                         'United States' 1937971      1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35-GM147557 2 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BXN 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014327 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010868 
_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]   0.010395 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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     . GLU   A 1 25  ? -25.59600 -8.84600  18.03800 1.000 58.14377 ?  5   GLU   A N     1 
ATOM   2    C CA    . GLU   A 1 25  ? -26.40900 -7.75300  17.51300 1.000 68.84222 ?  5   GLU   A CA    1 
ATOM   3    C C     . GLU   A 1 25  ? -25.55600 -6.50200  17.37700 1.000 63.68137 ?  5   GLU   A C     1 
ATOM   4    O O     . GLU   A 1 25  ? -24.94700 -6.26500  16.33600 1.000 77.77359 ?  5   GLU   A O     1 
ATOM   5    N N     . LYS   A 1 26  ? -25.51800 -5.69800  18.43800 1.000 52.19102 ?  6   LYS   A N     1 
ATOM   6    C CA    . LYS   A 1 26  ? -24.59300 -4.57300  18.46600 1.000 62.21354 ?  6   LYS   A CA    1 
ATOM   7    C C     . LYS   A 1 26  ? -23.19400 -5.01000  18.89600 1.000 54.87894 ?  6   LYS   A C     1 
ATOM   8    O O     . LYS   A 1 26  ? -22.19700 -4.54600  18.32800 1.000 52.82929 ?  6   LYS   A O     1 
ATOM   9    N N     . ASN   A 1 27  ? -23.09700 -5.88600  19.89800 1.000 36.38026 ?  7   ASN   A N     1 
ATOM   10   C CA    . ASN   A 1 27  ? -21.79800 -6.31700  20.40900 1.000 32.02260 ?  7   ASN   A CA    1 
ATOM   11   C C     . ASN   A 1 27  ? -21.23700 -7.41900  19.53000 1.000 29.00304 ?  7   ASN   A C     1 
ATOM   12   O O     . ASN   A 1 27  ? -21.80300 -8.51300  19.44700 1.000 28.98238 ?  7   ASN   A O     1 
ATOM   13   C CB    . ASN   A 1 27  ? -21.89800 -6.76300  21.87000 1.000 28.83416 ?  7   ASN   A CB    1 
ATOM   14   C CG    . ASN   A 1 27  ? -20.52700 -7.05000  22.50100 1.000 29.39248 ?  7   ASN   A CG    1 
ATOM   15   O OD1   . ASN   A 1 27  ? -19.47200 -6.80500  21.89400 1.000 27.54901 ?  7   ASN   A OD1   1 
ATOM   16   N ND2   . ASN   A 1 27  ? -20.54200 -7.55900  23.74900 1.000 32.32662 ?  7   ASN   A ND2   1 
ATOM   17   N N     . ILE   A 1 28  ? -20.11500 -7.12300  18.87600 1.000 27.13687 ?  8   ILE   A N     1 
ATOM   18   C CA    . ILE   A 1 28  ? -19.48600 -8.10600  18.01200 1.000 25.37001 ?  8   ILE   A CA    1 
ATOM   19   C C     . ILE   A 1 28  ? -19.15900 -9.38100  18.78500 1.000 23.32921 ?  8   ILE   A C     1 
ATOM   20   O O     . ILE   A 1 28  ? -19.19000 -10.48200 18.22000 1.000 24.34122 ?  8   ILE   A O     1 
ATOM   21   C CB    . ILE   A 1 28  ? -18.22600 -7.51800  17.36000 1.000 26.83455 ?  8   ILE   A CB    1 
ATOM   22   C CG1   . ILE   A 1 28  ? -17.68900 -8.47900  16.29400 1.000 28.35938 ?  8   ILE   A CG1   1 
ATOM   23   C CG2   . ILE   A 1 28  ? -17.17500 -7.15500  18.41200 1.000 29.36035 ?  8   ILE   A CG2   1 
ATOM   24   C CD1   . ILE   A 1 28  ? -16.38000 -8.02400  15.67000 1.000 42.29741 ?  8   ILE   A CD1   1 
ATOM   25   N N     . TYR   A 1 29  ? -18.84200 -9.26000  20.06900 1.000 19.69818 ?  9   TYR   A N     1 
ATOM   26   C CA    . TYR   A 1 29  ? -18.44500 -10.43100 20.84400 1.000 18.33116 ?  9   TYR   A CA    1 
ATOM   27   C C     . TYR   A 1 29  ? -19.63200 -11.32900 21.21300 1.000 27.06778 ?  9   TYR   A C     1 
ATOM   28   O O     . TYR   A 1 29  ? -19.43000 -12.40400 21.80400 1.000 23.18858 ?  9   TYR   A O     1 
ATOM   29   C CB    . TYR   A 1 29  ? -17.71700 -9.96000  22.10700 1.000 19.68328 ?  9   TYR   A CB    1 
ATOM   30   C CG    . TYR   A 1 29  ? -16.34500 -9.37900  21.83200 1.000 20.19832 ?  9   TYR   A CG    1 
ATOM   31   C CD1   . TYR   A 1 29  ? -15.36500 -10.14900 21.20500 1.000 19.52513 ?  9   TYR   A CD1   1 
ATOM   32   C CD2   . TYR   A 1 29  ? -16.03300 -8.06500  22.20200 1.000 22.18939 ?  9   TYR   A CD2   1 
ATOM   33   C CE1   . TYR   A 1 29  ? -14.09600 -9.63300  20.96800 1.000 22.41302 ?  9   TYR   A CE1   1 
ATOM   34   C CE2   . TYR   A 1 29  ? -14.76900 -7.53200  21.98100 1.000 22.77830 ?  9   TYR   A CE2   1 
ATOM   35   C CZ    . TYR   A 1 29  ? -13.80500 -8.32700  21.35800 1.000 22.66919 ?  9   TYR   A CZ    1 
ATOM   36   O OH    . TYR   A 1 29  ? -12.55300 -7.82600  21.13000 1.000 21.27066 ?  9   TYR   A OH    1 
ATOM   37   N N     . GLU   A 1 30  ? -20.85700 -10.91400 20.88300 1.000 25.83649 ?  10  GLU   A N     1 
ATOM   38   C CA    . GLU   A 1 30  ? -22.03800 -11.74900 21.08100 1.000 26.38941 ?  10  GLU   A CA    1 
ATOM   39   C C     . GLU   A 1 30  ? -22.38600 -12.57800 19.84300 1.000 26.31869 ?  10  GLU   A C     1 
ATOM   40   O O     . GLU   A 1 30  ? -23.28200 -13.42900 19.91800 1.000 28.01884 ?  10  GLU   A O     1 
ATOM   41   C CB    . GLU   A 1 30  ? -23.24900 -10.86600 21.49000 1.000 25.64997 ?  10  GLU   A CB    1 
ATOM   42   C CG    . GLU   A 1 30  ? -23.10300 -10.24800 22.89400 1.000 27.70367 ?  10  GLU   A CG    1 
ATOM   43   C CD    . GLU   A 1 30  ? -23.53200 -11.19100 24.02600 1.000 26.61730 ?  10  GLU   A CD    1 
ATOM   44   O OE1   . GLU   A 1 30  ? -23.68100 -12.41300 23.78400 1.000 29.69462 ?  10  GLU   A OE1   1 
ATOM   45   O OE2   . GLU   A 1 30  ? -23.65800 -10.73300 25.18500 1.000 28.81164 -1 10  GLU   A OE2   1 
ATOM   46   N N     . THR   A 1 31  ? -21.69400 -12.37400 18.71700 1.000 23.92319 ?  11  THR   A N     1 
ATOM   47   C CA    . THR   A 1 31  ? -22.06900 -13.05300 17.48200 1.000 24.10224 ?  11  THR   A CA    1 
ATOM   48   C C     . THR   A 1 31  ? -21.50500 -14.46800 17.43700 1.000 32.84099 ?  11  THR   A C     1 
ATOM   49   O O     . THR   A 1 31  ? -20.43800 -14.76300 17.98700 1.000 25.32048 ?  11  THR   A O     1 
ATOM   50   C CB    . THR   A 1 31  ? -21.59300 -12.29100 16.24200 1.000 28.98463 ?  11  THR   A CB    1 
ATOM   51   O OG1   . THR   A 1 31  ? -20.15300 -12.29100 16.17500 1.000 26.81445 ?  11  THR   A OG1   1 
ATOM   52   C CG2   . THR   A 1 31  ? -22.13000 -10.85800 16.25700 1.000 25.38930 ?  11  THR   A CG2   1 
ATOM   53   N N     . ASP   A 1 32  ? -22.23200 -15.34600 16.74700 1.000 26.35761 ?  12  ASP   A N     1 
ATOM   54   C CA    . ASP   A 1 32  ? -21.76300 -16.72000 16.59500 1.000 32.23035 ?  12  ASP   A CA    1 
ATOM   55   C C     . ASP   A 1 32  ? -20.39600 -16.76600 15.92000 1.000 27.58386 ?  12  ASP   A C     1 
ATOM   56   O O     . ASP   A 1 32  ? -19.56500 -17.61600 16.25400 1.000 27.49416 ?  12  ASP   A O     1 
ATOM   57   C CB    . ASP   A 1 32  ? -22.78300 -17.53600 15.80300 1.000 36.25634 ?  12  ASP   A CB    1 
ATOM   58   C CG    . ASP   A 1 32  ? -24.14300 -17.58100 16.48000 1.000 32.42203 ?  12  ASP   A CG    1 
ATOM   59   N N     . GLU   A 1 33  ? -20.13800 -15.85200 14.97900 1.000 25.44649 ?  13  GLU   A N     1 
ATOM   60   C CA    . GLU   A 1 33  ? -18.84100 -15.82000 14.30500 1.000 30.18695 ?  13  GLU   A CA    1 
ATOM   61   C C     . GLU   A 1 33  ? -17.69900 -15.52400 15.28000 1.000 25.16417 ?  13  GLU   A C     1 
ATOM   62   O O     . GLU   A 1 33  ? -16.62100 -16.12300 15.17500 1.000 22.15542 ?  13  GLU   A O     1 
ATOM   63   C CB    . GLU   A 1 33  ? -18.85400 -14.78800 13.17500 1.000 33.25653 ?  13  GLU   A CB    1 
ATOM   64   N N     . SER   A 1 34  ? -17.90900 -14.59800 16.22100 1.000 22.83153 ?  14  SER   A N     1 
ATOM   65   C CA    A SER   A 1 34  ? -16.88400 -14.31600 17.22300 0.472 23.24229 ?  14  SER   A CA    1 
ATOM   66   C CA    B SER   A 1 34  ? -16.87400 -14.32400 17.21800 0.528 23.24477 ?  14  SER   A CA    1 
ATOM   67   C C     . SER   A 1 34  ? -16.70700 -15.48900 18.17900 1.000 21.65193 ?  14  SER   A C     1 
ATOM   68   O O     . SER   A 1 34  ? -15.58100 -15.78500 18.60600 1.000 22.77045 ?  14  SER   A O     1 
ATOM   69   C CB    A SER   A 1 34  ? -17.23600 -13.05000 18.00200 0.472 24.91235 ?  14  SER   A CB    1 
ATOM   70   C CB    B SER   A 1 34  ? -17.17700 -13.04400 17.99900 0.528 24.92831 ?  14  SER   A CB    1 
ATOM   71   O OG    A SER   A 1 34  ? -16.16100 -12.68200 18.84800 0.472 22.80356 ?  14  SER   A OG    1 
ATOM   72   O OG    B SER   A 1 34  ? -17.25200 -11.92400 17.15000 0.528 23.61345 ?  14  SER   A OG    1 
ATOM   73   N N     . VAL   A 1 35  ? -17.80700 -16.14700 18.54900 1.000 22.69856 ?  15  VAL   A N     1 
ATOM   74   C CA    . VAL   A 1 35  ? -17.69300 -17.34400 19.38900 1.000 18.88988 ?  15  VAL   A CA    1 
ATOM   75   C C     . VAL   A 1 35  ? -16.83800 -18.38800 18.68500 1.000 19.56787 ?  15  VAL   A C     1 
ATOM   76   O O     . VAL   A 1 35  ? -15.91600 -18.96400 19.27500 1.000 22.09929 ?  15  VAL   A O     1 
ATOM   77   C CB    . VAL   A 1 35  ? -19.08100 -17.91000 19.74200 1.000 23.42700 ?  15  VAL   A CB    1 
ATOM   78   C CG1   . VAL   A 1 35  ? -18.92700 -19.23300 20.51300 1.000 26.16382 ?  15  VAL   A CG1   1 
ATOM   79   C CG2   . VAL   A 1 35  ? -19.90100 -16.92100 20.58200 1.000 26.16316 ?  15  VAL   A CG2   1 
ATOM   80   N N     . SER   A 1 36  ? -17.11800 -18.64800 17.40300 1.000 22.09574 ?  16  SER   A N     1 
ATOM   81   C CA    . SER   A 1 36  ? -16.30400 -19.63500 16.69500 1.000 22.36858 ?  16  SER   A CA    1 
ATOM   82   C C     . SER   A 1 36  ? -14.86600 -19.17500 16.57200 1.000 24.76900 ?  16  SER   A C     1 
ATOM   83   O O     . SER   A 1 36  ? -13.94500 -19.98200 16.70600 1.000 20.99777 ?  16  SER   A O     1 
ATOM   84   C CB    . SER   A 1 36  ? -16.86300 -19.94000 15.29700 1.000 26.34619 ?  16  SER   A CB    1 
ATOM   85   O OG    . SER   A 1 36  ? -17.85300 -20.95500 15.37400 1.000 28.31223 ?  16  SER   A OG    1 
ATOM   86   N N     . GLN   A 1 37  ? -14.65200 -17.88400 16.32200 1.000 18.92938 ?  17  GLN   A N     1 
ATOM   87   C CA    . GLN   A 1 37  ? -13.29000 -17.38500 16.22100 1.000 20.28379 ?  17  GLN   A CA    1 
ATOM   88   C C     . GLN   A 1 37  ? -12.52000 -17.60900 17.51700 1.000 20.43685 ?  17  GLN   A C     1 
ATOM   89   O O     . GLN   A 1 37  ? -11.36600 -18.05700 17.48700 1.000 19.32544 ?  17  GLN   A O     1 
ATOM   90   C CB    . GLN   A 1 37  ? -13.30100 -15.90000 15.88200 1.000 17.86382 ?  17  GLN   A CB    1 
ATOM   91   C CG    . GLN   A 1 37  ? -11.88700 -15.32400 15.72900 1.000 23.73173 ?  17  GLN   A CG    1 
ATOM   92   C CD    . GLN   A 1 37  ? -11.90000 -13.86100 15.29000 1.000 29.25263 ?  17  GLN   A CD    1 
ATOM   93   O OE1   . GLN   A 1 37  ? -12.04100 -12.96500 16.11500 1.000 33.35781 ?  17  GLN   A OE1   1 
ATOM   94   N NE2   . GLN   A 1 37  ? -11.75000 -13.62600 13.99100 1.000 29.65614 ?  17  GLN   A NE2   1 
ATOM   95   N N     . TYR   A 1 38  ? -13.14300 -17.31600 18.66900 1.000 19.56443 ?  18  TYR   A N     1 
ATOM   96   C CA    . TYR   A 1 38  ? -12.42400 -17.47000 19.93500 1.000 20.56767 ?  18  TYR   A CA    1 
ATOM   97   C C     . TYR   A 1 38  ? -12.30100 -18.93700 20.36600 1.000 18.91408 ?  18  TYR   A C     1 
ATOM   98   O O     . TYR   A 1 38  ? -11.31000 -19.30500 21.01100 1.000 18.67556 ?  18  TYR   A O     1 
ATOM   99   C CB    . TYR   A 1 38  ? -13.07000 -16.59000 21.01100 1.000 18.70352 ?  18  TYR   A CB    1 
ATOM   100  C CG    . TYR   A 1 38  ? -12.29300 -15.28900 21.03000 1.000 19.08908 ?  18  TYR   A CG    1 
ATOM   101  C CD1   . TYR   A 1 38  ? -11.12500 -15.16100 21.78600 1.000 21.50281 ?  18  TYR   A CD1   1 
ATOM   102  C CD2   . TYR   A 1 38  ? -12.63500 -14.24800 20.16900 1.000 21.72655 ?  18  TYR   A CD2   1 
ATOM   103  C CE1   . TYR   A 1 38  ? -10.35800 -13.98700 21.73800 1.000 19.28341 ?  18  TYR   A CE1   1 
ATOM   104  C CE2   . TYR   A 1 38  ? -11.86700 -13.07500 20.11000 1.000 24.92358 ?  18  TYR   A CE2   1 
ATOM   105  C CZ    . TYR   A 1 38  ? -10.73800 -12.95800 20.90700 1.000 21.01368 ?  18  TYR   A CZ    1 
ATOM   106  O OH    . TYR   A 1 38  ? -9.94700  -11.81900 20.83900 1.000 20.85204 ?  18  TYR   A OH    1 
ATOM   107  N N     . CYS   A 1 39  ? -13.27600 -19.78400 20.02800 1.000 18.63767 ?  19  CYS   A N     1 
ATOM   108  C CA    . CYS   A 1 39  ? -13.10500 -21.22500 20.24300 1.000 19.01573 ?  19  CYS   A CA    1 
ATOM   109  C C     . CYS   A 1 39  ? -11.84300 -21.73200 19.54800 1.000 18.17317 ?  19  CYS   A C     1 
ATOM   110  O O     . CYS   A 1 39  ? -11.04300 -22.47300 20.13400 1.000 18.51862 ?  19  CYS   A O     1 
ATOM   111  C CB    . CYS   A 1 39  ? -14.33200 -21.97100 19.71800 1.000 20.52467 ?  19  CYS   A CB    1 
ATOM   112  S SG    . CYS   A 1 39  ? -15.73900 -21.91100 20.83600 1.000 24.78825 ?  19  CYS   A SG    1 
ATOM   113  N N     . ASP   A 1 40  ? -11.65500 -21.34600 18.28100 1.000 18.90559 ?  20  ASP   A N     1 
ATOM   114  C CA    . ASP   A 1 40  ? -10.50200 -21.81700 17.51300 1.000 20.78742 ?  20  ASP   A CA    1 
ATOM   115  C C     . ASP   A 1 40  ? -9.20600  -21.25400 18.07600 1.000 22.43889 ?  20  ASP   A C     1 
ATOM   116  O O     . ASP   A 1 40  ? -8.21300  -21.96900 18.24300 1.000 19.27743 ?  20  ASP   A O     1 
ATOM   117  C CB    . ASP   A 1 40  ? -10.68500 -21.40600 16.04900 1.000 21.20024 ?  20  ASP   A CB    1 
ATOM   118  C CG    . ASP   A 1 40  ? -9.86000  -22.23500 15.09100 1.000 29.00510 ?  20  ASP   A CG    1 
ATOM   119  O OD1   . ASP   A 1 40  ? -9.56000  -23.41300 15.38100 1.000 30.75568 ?  20  ASP   A OD1   1 
ATOM   120  O OD2   . ASP   A 1 40  ? -9.49700  -21.68200 14.04500 1.000 38.44976 -1 20  ASP   A OD2   1 
ATOM   121  N N     . PHE   A 1 41  ? -9.21500  -19.96200 18.39300 1.000 18.55540 ?  21  PHE   A N     1 
ATOM   122  C CA    . PHE   A 1 41  ? -8.05100  -19.31200 18.98100 1.000 19.47665 ?  21  PHE   A CA    1 
ATOM   123  C C     . PHE   A 1 41  ? -7.64700  -19.95200 20.30300 1.000 20.81277 ?  21  PHE   A C     1 
ATOM   124  O O     . PHE   A 1 41  ? -6.46100  -20.19100 20.55600 1.000 22.19504 ?  21  PHE   A O     1 
ATOM   125  C CB    . PHE   A 1 41  ? -8.40600  -17.84000 19.18200 1.000 15.62183 ?  21  PHE   A CB    1 
ATOM   126  C CG    . PHE   A 1 41  ? -7.33200  -17.01000 19.82800 1.000 19.83097 ?  21  PHE   A CG    1 
ATOM   127  C CD1   . PHE   A 1 41  ? -6.01500  -17.03400 19.36100 1.000 19.69376 ?  21  PHE   A CD1   1 
ATOM   128  C CD2   . PHE   A 1 41  ? -7.66300  -16.15600 20.88200 1.000 19.32756 ?  21  PHE   A CD2   1 
ATOM   129  C CE1   . PHE   A 1 41  ? -5.03200  -16.19400 19.94300 1.000 20.93484 ?  21  PHE   A CE1   1 
ATOM   130  C CE2   . PHE   A 1 41  ? -6.70000  -15.32800 21.47300 1.000 23.79836 ?  21  PHE   A CE2   1 
ATOM   131  C CZ    . PHE   A 1 41  ? -5.39000  -15.33700 21.00300 1.000 18.05942 ?  21  PHE   A CZ    1 
ATOM   132  N N     . GLN   A 1 42  ? -8.61700  -20.22300 21.16900 1.000 18.05663 ?  22  GLN   A N     1 
ATOM   133  C CA    . GLN   A 1 42  ? -8.29500  -20.64000 22.52200 1.000 18.35448 ?  22  GLN   A CA    1 
ATOM   134  C C     . GLN   A 1 42  ? -8.10100  -22.13300 22.65800 1.000 21.37642 ?  22  GLN   A C     1 
ATOM   135  O O     . GLN   A 1 42  ? -7.42800  -22.57000 23.59200 1.000 21.20277 ?  22  GLN   A O     1 
ATOM   136  C CB    . GLN   A 1 42  ? -9.39100  -20.23200 23.49000 1.000 19.04933 ?  22  GLN   A CB    1 
ATOM   137  C CG    . GLN   A 1 42  ? -9.48500  -18.70700 23.69500 1.000 20.39859 ?  22  GLN   A CG    1 
ATOM   138  C CD    . GLN   A 1 42  ? -10.00600 -18.40900 25.06200 1.000 21.82405 ?  22  GLN   A CD    1 
ATOM   139  O OE1   . GLN   A 1 42  ? -10.89500 -19.10200 25.56200 1.000 22.16664 ?  22  GLN   A OE1   1 
ATOM   140  N NE2   . GLN   A 1 42  ? -9.41800  -17.40300 25.71400 1.000 27.28529 ?  22  GLN   A NE2   1 
ATOM   141  N N     . TYR   A 1 43  ? -8.66300  -22.91300 21.75400 1.000 21.25183 ?  23  TYR   A N     1 
ATOM   142  C CA    . TYR   A 1 43  ? -8.64400  -24.36500 21.90500 1.000 18.46579 ?  23  TYR   A CA    1 
ATOM   143  C C     . TYR   A 1 43  ? -8.11200  -25.10800 20.69300 1.000 26.43059 ?  23  TYR   A C     1 
ATOM   144  O O     . TYR   A 1 43  ? -7.97200  -26.33500 20.76700 1.000 24.27268 ?  23  TYR   A O     1 
ATOM   145  C CB    . TYR   A 1 43  ? -10.06800 -24.88300 22.22000 1.000 19.32862 ?  23  TYR   A CB    1 
ATOM   146  C CG    . TYR   A 1 43  ? -10.65200 -24.35800 23.52800 1.000 24.13970 ?  23  TYR   A CG    1 
ATOM   147  C CD1   . TYR   A 1 43  ? -10.30600 -24.94600 24.76200 1.000 21.72785 ?  23  TYR   A CD1   1 
ATOM   148  C CD2   . TYR   A 1 43  ? -11.51400 -23.26300 23.53500 1.000 19.37588 ?  23  TYR   A CD2   1 
ATOM   149  C CE1   . TYR   A 1 43  ? -10.81400 -24.47300 25.93300 1.000 19.40464 ?  23  TYR   A CE1   1 
ATOM   150  C CE2   . TYR   A 1 43  ? -12.04400 -22.76400 24.73200 1.000 18.05221 ?  23  TYR   A CE2   1 
ATOM   151  C CZ    . TYR   A 1 43  ? -11.68700 -23.38300 25.92200 1.000 18.20548 ?  23  TYR   A CZ    1 
ATOM   152  O OH    . TYR   A 1 43  ? -12.19300 -22.89800 27.08900 1.000 19.44224 ?  23  TYR   A OH    1 
ATOM   153  N N     . GLY   A 1 44  ? -7.85600  -24.39600 19.60200 1.000 29.24006 ?  24  GLY   A N     1 
ATOM   154  C CA    . GLY   A 1 44  ? -7.46400  -25.07800 18.35600 1.000 29.20666 ?  24  GLY   A CA    1 
ATOM   155  C C     . GLY   A 1 44  ? -5.97300  -25.24100 18.15600 1.000 31.15944 ?  24  GLY   A C     1 
ATOM   156  O O     . GLY   A 1 44  ? -5.22700  -25.16400 19.13600 1.000 36.24448 ?  24  GLY   A O     1 
ATOM   157  N N     . GLU   A 1 45  ? -5.56900  -25.43500 16.90100 1.000 49.45209 ?  25  GLU   A N     1 
ATOM   158  C CA    . GLU   A 1 45  ? -4.14600  -25.71600 16.57800 1.000 55.27005 ?  25  GLU   A CA    1 
ATOM   159  C C     . GLU   A 1 45  ? -3.29800  -24.44900 16.47700 1.000 46.77717 ?  25  GLU   A C     1 
ATOM   160  O O     . GLU   A 1 45  ? -3.82900  -23.43600 16.00900 1.000 46.85386 ?  25  GLU   A O     1 
ATOM   161  C CB    . GLU   A 1 45  ? -4.06600  -26.45700 15.24400 1.000 43.30933 ?  25  GLU   A CB    1 
ATOM   162  N N     . ASP   A 1 46  ? -2.02600  -24.54700 16.86500 1.000 44.97567 ?  26  ASP   A N     1 
ATOM   163  C CA    . ASP   A 1 46  ? -1.06700  -23.42200 16.76700 1.000 46.95966 ?  26  ASP   A CA    1 
ATOM   164  C C     . ASP   A 1 46  ? -0.77200  -23.05500 15.31100 1.000 45.93883 ?  26  ASP   A C     1 
ATOM   165  O O     . ASP   A 1 46  ? -0.92100  -23.91400 14.44000 1.000 37.89303 ?  26  ASP   A O     1 
ATOM   166  C CB    . ASP   A 1 46  ? 0.25500   -23.76400 17.44400 1.000 45.50463 ?  26  ASP   A CB    1 
ATOM   167  C CG    . ASP   A 1 46  ? 1.29300   -24.37800 16.52200 1.000 61.57016 ?  26  ASP   A CG    1 
ATOM   168  N N     . CYS   A 1 47  ? -0.33900  -21.81300 15.09200 1.000 36.08485 ?  27  CYS   A N     1 
ATOM   169  C CA    . CYS   A 1 47  ? -0.07800  -21.31200 13.72200 1.000 32.66017 ?  27  CYS   A CA    1 
ATOM   170  C C     . CYS   A 1 47  ? 1.24900   -20.55400 13.66700 1.000 33.44258 ?  27  CYS   A C     1 
ATOM   171  O O     . CYS   A 1 47  ? 1.56400   -19.86500 14.64200 1.000 32.55025 ?  27  CYS   A O     1 
ATOM   172  C CB    . CYS   A 1 47  ? -1.20100  -20.38100 13.28600 1.000 33.40101 ?  27  CYS   A CB    1 
ATOM   173  S SG    . CYS   A 1 47  ? -2.81000  -21.18900 13.12400 1.000 47.20747 ?  27  CYS   A SG    1 
ATOM   174  N N     . PHE   A 1 48  ? 1.98400   -20.69200 12.56000 1.000 27.17184 ?  28  PHE   A N     1 
ATOM   175  C CA    . PHE   A 1 48  ? 3.25300   -19.94600 12.36300 1.000 29.95404 ?  28  PHE   A CA    1 
ATOM   176  C C     . PHE   A 1 48  ? 4.22900   -20.17400 13.52700 1.000 26.22252 ?  28  PHE   A C     1 
ATOM   177  O O     . PHE   A 1 48  ? 5.04100   -19.29700 13.80500 1.000 37.55031 ?  28  PHE   A O     1 
ATOM   178  C CB    . PHE   A 1 48  ? 2.97000   -18.45900 12.13900 1.000 29.13544 ?  28  PHE   A CB    1 
ATOM   179  C CG    . PHE   A 1 48  ? 1.96500   -18.14400 11.06200 1.000 30.14142 ?  28  PHE   A CG    1 
ATOM   180  C CD1   . PHE   A 1 48  ? 2.20700   -18.48400 9.74200  1.000 34.75258 ?  28  PHE   A CD1   1 
ATOM   181  C CD2   . PHE   A 1 48  ? 0.78300   -17.49100 11.36400 1.000 32.16156 ?  28  PHE   A CD2   1 
ATOM   182  C CE1   . PHE   A 1 48  ? 1.28400   -18.18600 8.75300  1.000 30.61900 ?  28  PHE   A CE1   1 
ATOM   183  C CE2   . PHE   A 1 48  ? -0.13700  -17.19300 10.37400 1.000 29.99624 ?  28  PHE   A CE2   1 
ATOM   184  C CZ    . PHE   A 1 48  ? 0.11400   -17.54100 9.07100  1.000 24.54255 ?  28  PHE   A CZ    1 
ATOM   185  N N     . GLY   A 1 49  ? 4.14600   -21.33500 14.16300 1.000 33.95901 ?  29  GLY   A N     1 
ATOM   186  C CA    . GLY   A 1 49  ? 5.03700   -21.61600 15.27300 1.000 41.83835 ?  29  GLY   A CA    1 
ATOM   187  C C     . GLY   A 1 49  ? 4.72900   -20.85100 16.53900 1.000 44.71165 ?  29  GLY   A C     1 
ATOM   188  O O     . GLY   A 1 49  ? 5.54200   -20.85900 17.47000 1.000 38.36081 ?  29  GLY   A O     1 
ATOM   189  N N     . VAL   A 1 50  ? 3.58900   -20.18700 16.60000 1.000 29.61807 ?  30  VAL   A N     1 
ATOM   190  C CA    . VAL   A 1 50  ? 3.20200   -19.41500 17.77000 1.000 25.84021 ?  30  VAL   A CA    1 
ATOM   191  C C     . VAL   A 1 50  ? 2.36500   -20.31400 18.67400 1.000 25.62332 ?  30  VAL   A C     1 
ATOM   192  O O     . VAL   A 1 50  ? 1.36100   -20.89500 18.23700 1.000 26.65828 ?  30  VAL   A O     1 
ATOM   193  C CB    . VAL   A 1 50  ? 2.43000   -18.15100 17.35100 1.000 22.92345 ?  30  VAL   A CB    1 
ATOM   194  C CG1   . VAL   A 1 50  ? 1.96000   -17.34700 18.57600 1.000 24.11867 ?  30  VAL   A CG1   1 
ATOM   195  C CG2   . VAL   A 1 50  ? 3.31600   -17.25900 16.48100 1.000 29.68827 ?  30  VAL   A CG2   1 
ATOM   196  N N     . LEU   A 1 51  ? 2.76000   -20.40400 19.94000 1.000 24.64665 ?  31  LEU   A N     1 
ATOM   197  C CA    . LEU   A 1 51  ? 2.08600   -21.27600 20.89500 1.000 32.22097 ?  31  LEU   A CA    1 
ATOM   198  C C     . LEU   A 1 51  ? 0.76000   -20.67000 21.34900 1.000 23.61409 ?  31  LEU   A C     1 
ATOM   199  O O     . LEU   A 1 51  ? 0.56100   -19.45800 21.29700 1.000 21.77675 ?  31  LEU   A O     1 
ATOM   200  C CB    . LEU   A 1 51  ? 2.98800   -21.50700 22.10800 1.000 37.88378 ?  31  LEU   A CB    1 
ATOM   201  C CG    . LEU   A 1 51  ? 4.24500   -22.31100 21.74600 1.000 46.12353 ?  31  LEU   A CG    1 
ATOM   202  C CD1   . LEU   A 1 51  ? 4.89500   -22.90200 22.96200 1.000 48.27673 ?  31  LEU   A CD1   1 
ATOM   203  C CD2   . LEU   A 1 51  ? 3.87600   -23.41600 20.77400 1.000 42.10737 ?  31  LEU   A CD2   1 
ATOM   204  N N     . ASN   A 1 52  ? -0.13000  -21.53800 21.83600 1.000 24.02329 ?  32  ASN   A N     1 
ATOM   205  C CA    . ASN   A 1 52  ? -1.43000  -21.11800 22.34900 1.000 24.09499 ?  32  ASN   A CA    1 
ATOM   206  C C     . ASN   A 1 52  ? -1.29400  -19.97700 23.36000 1.000 24.23857 ?  32  ASN   A C     1 
ATOM   207  O O     . ASN   A 1 52  ? -0.56900  -20.07700 24.35500 1.000 21.69188 ?  32  ASN   A O     1 
ATOM   208  C CB    . ASN   A 1 52  ? -2.13700  -22.31900 22.98700 1.000 20.40637 ?  32  ASN   A CB    1 
ATOM   209  C CG    . ASN   A 1 52  ? -3.51000  -21.97400 23.51700 1.000 22.24277 ?  32  ASN   A CG    1 
ATOM   210  O OD1   . ASN   A 1 52  ? -3.63600  -21.50900 24.62600 1.000 24.77994 ?  32  ASN   A OD1   1 
ATOM   211  N ND2   . ASN   A 1 52  ? -4.54600  -22.19800 22.71300 1.000 23.01279 ?  32  ASN   A ND2   1 
ATOM   212  N N     . PHE   A 1 53  ? -2.02100  -18.89300 23.10400 1.000 19.62749 ?  33  PHE   A N     1 
ATOM   213  C CA    . PHE   A 1 53  ? -1.83800  -17.64600 23.84100 1.000 18.84099 ?  33  PHE   A CA    1 
ATOM   214  C C     . PHE   A 1 53  ? -2.42700  -17.71600 25.24200 1.000 19.50764 ?  33  PHE   A C     1 
ATOM   215  O O     . PHE   A 1 53  ? -1.80300  -17.25200 26.20400 1.000 19.59563 ?  33  PHE   A O     1 
ATOM   216  C CB    . PHE   A 1 53  ? -2.47400  -16.51900 23.02600 1.000 20.66325 ?  33  PHE   A CB    1 
ATOM   217  C CG    . PHE   A 1 53  ? -2.36900  -15.14200 23.65900 1.000 19.82856 ?  33  PHE   A CG    1 
ATOM   218  C CD1   . PHE   A 1 53  ? -1.14700  -14.50100 23.74000 1.000 18.01163 ?  33  PHE   A CD1   1 
ATOM   219  C CD2   . PHE   A 1 53  ? -3.51600  -14.48300 24.11300 1.000 22.05461 ?  33  PHE   A CD2   1 
ATOM   220  C CE1   . PHE   A 1 53  ? -1.04900  -13.20000 24.28100 1.000 17.35526 ?  33  PHE   A CE1   1 
ATOM   221  C CE2   . PHE   A 1 53  ? -3.44000  -13.20800 24.67100 1.000 22.17787 ?  33  PHE   A CE2   1 
ATOM   222  C CZ    . PHE   A 1 53  ? -2.19900  -12.56600 24.76700 1.000 19.92070 ?  33  PHE   A CZ    1 
ATOM   223  N N     . ALA   A 1 54  ? -3.62800  -18.28600 25.38100 1.000 19.98871 ?  34  ALA   A N     1 
ATOM   224  C CA    . ALA   A 1 54  ? -4.21900  -18.42600 26.70900 1.000 23.24931 ?  34  ALA   A CA    1 
ATOM   225  C C     . ALA   A 1 54  ? -3.31900  -19.23300 27.63400 1.000 21.19066 ?  34  ALA   A C     1 
ATOM   226  O O     . ALA   A 1 54  ? -3.15900  -18.88800 28.81300 1.000 20.00521 ?  34  ALA   A O     1 
ATOM   227  C CB    . ALA   A 1 54  ? -5.59000  -19.08900 26.60800 1.000 19.60705 ?  34  ALA   A CB    1 
ATOM   228  N N     . LEU   A 1 55  ? -2.75900  -20.34200 27.13000 1.000 19.57812 ?  35  LEU   A N     1 
ATOM   229  C CA    . LEU   A 1 55  ? -1.86200  -21.15000 27.95000 1.000 19.92227 ?  35  LEU   A CA    1 
ATOM   230  C C     . LEU   A 1 55  ? -0.56300  -20.40900 28.24600 1.000 19.59288 ?  35  LEU   A C     1 
ATOM   231  O O     . LEU   A 1 55  ? -0.08300  -20.44300 29.37600 1.000 21.51469 ?  35  LEU   A O     1 
ATOM   232  C CB    . LEU   A 1 55  ? -1.57700  -22.49300 27.26100 1.000 20.30921 ?  35  LEU   A CB    1 
ATOM   233  C CG    . LEU   A 1 55  ? -0.53600  -23.39600 27.94200 1.000 23.61626 ?  35  LEU   A CG    1 
ATOM   234  C CD1   . LEU   A 1 55  ? -0.98600  -23.75400 29.35400 1.000 23.64036 ?  35  LEU   A CD1   1 
ATOM   235  C CD2   . LEU   A 1 55  ? -0.34100  -24.67200 27.06600 1.000 23.32118 ?  35  LEU   A CD2   1 
ATOM   236  N N     . ALA   A 1 56  ? 0.00500   -19.71000 27.25100 1.000 19.26041 ?  36  ALA   A N     1 
ATOM   237  C CA    . ALA   A 1 56  ? 1.22700   -18.94100 27.49100 1.000 21.20746 ?  36  ALA   A CA    1 
ATOM   238  C C     . ALA   A 1 56  ? 1.01700   -17.91200 28.59300 1.000 21.15785 ?  36  ALA   A C     1 
ATOM   239  O O     . ALA   A 1 56  ? 1.85000   -17.77100 29.50300 1.000 23.13124 ?  36  ALA   A O     1 
ATOM   240  C CB    . ALA   A 1 56  ? 1.68500   -18.24000 26.20100 1.000 23.28141 ?  36  ALA   A CB    1 
ATOM   241  N N     . CYS   A 1 57  ? -0.08200  -17.15400 28.50800 1.000 23.08555 ?  37  CYS   A N     1 
ATOM   242  C CA    . CYS   A 1 57  ? -0.35000  -16.12100 29.50800 1.000 25.57310 ?  37  CYS   A CA    1 
ATOM   243  C C     . CYS   A 1 57  ? -0.57400  -16.72100 30.88900 1.000 24.67575 ?  37  CYS   A C     1 
ATOM   244  O O     . CYS   A 1 57  ? -0.04300  -16.21600 31.88900 1.000 20.75826 ?  37  CYS   A O     1 
ATOM   245  C CB    . CYS   A 1 57  ? -1.56500  -15.28800 29.10400 1.000 23.03807 ?  37  CYS   A CB    1 
ATOM   246  S SG    . CYS   A 1 57  ? -1.26100  -14.21200 27.68100 1.000 25.40143 ?  37  CYS   A SG    1 
ATOM   247  N N     . ALA   A 1 58  ? -1.42000  -17.75500 30.96800 1.000 21.46700 ?  38  ALA   A N     1 
ATOM   248  C CA    . ALA   A 1 58  ? -1.68300  -18.40000 32.25300 1.000 23.45966 ?  38  ALA   A CA    1 
ATOM   249  C C     . ALA   A 1 58  ? -0.39800  -18.97400 32.84100 1.000 24.68980 ?  38  ALA   A C     1 
ATOM   250  O O     . ALA   A 1 58  ? -0.11500  -18.79200 34.03000 1.000 24.81932 ?  38  ALA   A O     1 
ATOM   251  C CB    . ALA   A 1 58  ? -2.75000  -19.49400 32.09400 1.000 24.84035 ?  38  ALA   A CB    1 
ATOM   252  N N     . THR   A 1 59  ? 0.42200   -19.61700 32.00900 1.000 23.93767 ?  39  THR   A N     1 
ATOM   253  C CA    . THR   A 1 59  ? 1.68400   -20.17300 32.50500 1.000 24.92992 ?  39  THR   A CA    1 
ATOM   254  C C     . THR   A 1 59  ? 2.60300   -19.07800 33.03400 1.000 25.83486 ?  39  THR   A C     1 
ATOM   255  O O     . THR   A 1 59  ? 3.17600   -19.20800 34.12100 1.000 25.75141 ?  39  THR   A O     1 
ATOM   256  C CB    . THR   A 1 59  ? 2.36700   -20.96400 31.39400 1.000 27.33693 ?  39  THR   A CB    1 
ATOM   257  O OG1   . THR   A 1 59  ? 1.50700   -22.04600 31.04000 1.000 27.66384 ?  39  THR   A OG1   1 
ATOM   258  C CG2   . THR   A 1 59  ? 3.73700   -21.52900 31.86500 1.000 31.73998 ?  39  THR   A CG2   1 
ATOM   259  N N     . LYS   A 1 60  ? 2.72900   -17.97700 32.29700 1.000 23.22814 ?  40  LYS   A N     1 
ATOM   260  C CA    . LYS   A 1 60  ? 3.55800   -16.88000 32.78500 1.000 27.39423 ?  40  LYS   A CA    1 
ATOM   261  C C     . LYS   A 1 60  ? 2.97600   -16.28800 34.06200 1.000 25.14210 ?  40  LYS   A C     1 
ATOM   262  O O     . LYS   A 1 60  ? 3.71300   -16.00300 35.01600 1.000 27.46737 ?  40  LYS   A O     1 
ATOM   263  C CB    . LYS   A 1 60  ? 3.71200   -15.82000 31.68900 1.000 23.63938 ?  40  LYS   A CB    1 
ATOM   264  C CG    . LYS   A 1 60  ? 4.59400   -16.28100 30.53000 1.000 29.45009 ?  40  LYS   A CG    1 
ATOM   265  C CD    . LYS   A 1 60  ? 4.37200   -15.40300 29.29600 1.000 27.49022 ?  40  LYS   A CD    1 
ATOM   266  C CE    . LYS   A 1 60  ? 5.19700   -15.88400 28.11000 1.000 31.68118 ?  40  LYS   A CE    1 
ATOM   267  N NZ    . LYS   A 1 60  ? 6.66300   -15.87000 28.41500 1.000 35.13801 ?  40  LYS   A NZ    1 
ATOM   268  N N     . ALA   A 1 61  ? 1.64800   -16.14000 34.12500 1.000 24.86021 ?  41  ALA   A N     1 
ATOM   269  C CA    . ALA   A 1 61  ? 1.04000   -15.57000 35.32300 1.000 23.24702 ?  41  ALA   A CA    1 
ATOM   270  C C     . ALA   A 1 61  ? 1.31600   -16.43200 36.54500 1.000 29.00267 ?  41  ALA   A C     1 
ATOM   271  O O     . ALA   A 1 61  ? 1.57400   -15.91200 37.63800 1.000 29.89540 ?  41  ALA   A O     1 
ATOM   272  C CB    . ALA   A 1 61  ? -0.46900  -15.40400 35.14500 1.000 29.89447 ?  41  ALA   A CB    1 
ATOM   273  N N     . ILE   A 1 62  ? 1.23700   -17.75000 36.38800 1.000 26.50099 ?  42  ILE   A N     1 
ATOM   274  C CA    . ILE   A 1 62  ? 1.51200   -18.63600 37.51700 1.000 28.47590 ?  42  ILE   A CA    1 
ATOM   275  C C     . ILE   A 1 62  ? 2.96400   -18.48600 37.95700 1.000 36.09067 ?  42  ILE   A C     1 
ATOM   276  O O     . ILE   A 1 62  ? 3.26800   -18.46700 39.15700 1.000 35.08429 ?  42  ILE   A O     1 
ATOM   277  C CB    . ILE   A 1 62  ? 1.14900   -20.09000 37.16000 1.000 28.02261 ?  42  ILE   A CB    1 
ATOM   278  C CG1   . ILE   A 1 62  ? -0.37800  -20.25500 37.11300 1.000 27.89691 ?  42  ILE   A CG1   1 
ATOM   279  C CG2   . ILE   A 1 62  ? 1.78300   -21.08000 38.14300 1.000 32.37154 ?  42  ILE   A CG2   1 
ATOM   280  C CD1   . ILE   A 1 62  ? -0.86600  -21.35300 36.14400 1.000 34.32308 ?  42  ILE   A CD1   1 
ATOM   281  N N     . GLY   A 1 63  ? 3.87200   -18.33000 36.99500 1.000 29.25696 ?  43  GLY   A N     1 
ATOM   282  C CA    . GLY   A 1 63  ? 5.26300   -18.06600 37.33100 1.000 28.42998 ?  43  GLY   A CA    1 
ATOM   283  C C     . GLY   A 1 63  ? 5.45000   -16.78800 38.12500 1.000 37.30394 ?  43  GLY   A C     1 
ATOM   284  O O     . GLY   A 1 63  ? 6.11600   -16.78000 39.16100 1.000 33.59838 ?  43  GLY   A O     1 
ATOM   285  N N     . TYR   A 1 64  ? 4.86000   -15.68600 37.65300 1.000 34.32166 ?  44  TYR   A N     1 
ATOM   286  C CA    . TYR   A 1 64  ? 5.00300   -14.41500 38.35700 1.000 32.37618 ?  44  TYR   A CA    1 
ATOM   287  C C     . TYR   A 1 64  ? 4.41000   -14.45700 39.76500 1.000 36.11563 ?  44  TYR   A C     1 
ATOM   288  O O     . TYR   A 1 64  ? 4.87500   -13.73300 40.65000 1.000 37.57572 ?  44  TYR   A O     1 
ATOM   289  C CB    . TYR   A 1 64  ? 4.35800   -13.28800 37.54100 1.000 28.33984 ?  44  TYR   A CB    1 
ATOM   290  C CG    . TYR   A 1 64  ? 5.18500   -12.85300 36.34800 1.000 29.56748 ?  44  TYR   A CG    1 
ATOM   291  C CD1   . TYR   A 1 64  ? 6.44100   -12.29600 36.51700 1.000 29.58186 ?  44  TYR   A CD1   1 
ATOM   292  C CD2   . TYR   A 1 64  ? 4.72100   -13.04000 35.04300 1.000 26.33115 ?  44  TYR   A CD2   1 
ATOM   293  C CE1   . TYR   A 1 64  ? 7.20400   -11.91200 35.43000 1.000 29.79696 ?  44  TYR   A CE1   1 
ATOM   294  C CE2   . TYR   A 1 64  ? 5.47400   -12.66000 33.95300 1.000 30.05784 ?  44  TYR   A CE2   1 
ATOM   295  C CZ    . TYR   A 1 64  ? 6.71200   -12.08400 34.15100 1.000 29.68862 ?  44  TYR   A CZ    1 
ATOM   296  O OH    . TYR   A 1 64  ? 7.46100   -11.70700 33.05600 1.000 31.97568 ?  44  TYR   A OH    1 
ATOM   297  N N     . THR   A 1 65  ? 3.38400   -15.27500 39.99600 1.000 29.06195 ?  45  THR   A N     1 
ATOM   298  C CA    . THR   A 1 65  ? 2.69300   -15.31000 41.28000 1.000 35.16753 ?  45  THR   A CA    1 
ATOM   299  C C     . THR   A 1 65  ? 3.11900   -16.50700 42.12800 1.000 37.62042 ?  45  THR   A C     1 
ATOM   300  O O     . THR   A 1 65  ? 2.35700   -16.97100 42.98400 1.000 42.77313 ?  45  THR   A O     1 
ATOM   301  C CB    . THR   A 1 65  ? 1.17900   -15.31700 41.07600 1.000 28.91230 ?  45  THR   A CB    1 
ATOM   302  O OG1   . THR   A 1 65  ? 0.79700   -16.47200 40.31300 1.000 38.69385 ?  45  THR   A OG1   1 
ATOM   303  C CG2   . THR   A 1 65  ? 0.75000   -14.08100 40.30400 1.000 29.01682 ?  45  THR   A CG2   1 
ATOM   304  N N     . LYS   A 1 66  ? 4.34300   -16.99300 41.91800 1.000 38.28632 ?  46  LYS   A N     1 
ATOM   305  C CA    . LYS   A 1 66  ? 4.79100   -18.23200 42.54900 1.000 45.76924 ?  46  LYS   A CA    1 
ATOM   306  C C     . LYS   A 1 66  ? 4.85800   -18.11500 44.06600 1.000 50.65925 ?  46  LYS   A C     1 
ATOM   307  O O     . LYS   A 1 66  ? 4.64800   -19.11000 44.76900 1.000 60.73140 ?  46  LYS   A O     1 
ATOM   308  C CB    . LYS   A 1 66  ? 6.15800   -18.62700 41.99000 1.000 39.86164 ?  46  LYS   A CB    1 
ATOM   309  N N     . GLU   A 1 67  ? 5.13600   -16.92600 44.59200 1.000 42.95365 ?  47  GLU   A N     1 
ATOM   310  C CA    . GLU   A 1 67  ? 5.25200   -16.75500 46.03200 1.000 50.02101 ?  47  GLU   A CA    1 
ATOM   311  C C     . GLU   A 1 67  ? 3.93000   -16.41800 46.71800 1.000 45.48012 ?  47  GLU   A C     1 
ATOM   312  O O     . GLU   A 1 67  ? 3.90200   -16.31900 47.94700 1.000 63.15855 ?  47  GLU   A O     1 
ATOM   313  C CB    . GLU   A 1 67  ? 6.29100   -15.66900 46.34600 1.000 55.39584 ?  47  GLU   A CB    1 
ATOM   314  C CG    . GLU   A 1 67  ? 7.70800   -16.02100 45.89800 1.000 49.88626 ?  47  GLU   A CG    1 
ATOM   315  N N     . THR   A 1 68  ? 2.84400   -16.23900 45.97800 1.000 35.27671 ?  48  THR   A N     1 
ATOM   316  C CA    . THR   A 1 68  ? 1.56200   -15.92500 46.58900 1.000 37.42951 ?  48  THR   A CA    1 
ATOM   317  C C     . THR   A 1 68  ? 0.80900   -17.20500 46.93700 1.000 38.36524 ?  48  THR   A C     1 
ATOM   318  O O     . THR   A 1 68  ? 1.14000   -18.28500 46.44400 1.000 38.96275 ?  48  THR   A O     1 
ATOM   319  C CB    . THR   A 1 68  ? 0.72500   -15.05000 45.64200 1.000 42.08128 ?  48  THR   A CB    1 
ATOM   320  O OG1   . THR   A 1 68  ? -0.01100  -15.88200 44.73200 1.000 48.64167 ?  48  THR   A OG1   1 
ATOM   321  C CG2   . THR   A 1 68  ? 1.60300   -14.08200 44.87000 1.000 38.46956 ?  48  THR   A CG2   1 
ATOM   322  N N     . PRO   A 1 69  ? -0.21200  -17.11700 47.79800 1.000 32.61485 ?  49  PRO   A N     1 
ATOM   323  C CA    . PRO   A 1 69  ? -0.92300  -18.33400 48.23600 1.000 37.11459 ?  49  PRO   A CA    1 
ATOM   324  C C     . PRO   A 1 69  ? -1.69300  -19.08700 47.15100 1.000 50.06445 ?  49  PRO   A C     1 
ATOM   325  O O     . PRO   A 1 69  ? -1.99000  -20.27300 47.34900 1.000 52.45111 ?  49  PRO   A O     1 
ATOM   326  C CB    . PRO   A 1 69  ? -1.87700  -17.79600 49.31200 1.000 43.31372 ?  49  PRO   A CB    1 
ATOM   327  C CG    . PRO   A 1 69  ? -1.17500  -16.56700 49.81500 1.000 41.47208 ?  49  PRO   A CG    1 
ATOM   328  C CD    . PRO   A 1 69  ? -0.62700  -15.94500 48.58700 1.000 37.10487 ?  49  PRO   A CD    1 
ATOM   329  N N     . LYS   A 1 70  ? -2.05500  -18.45100 46.04300 1.000 45.84055 ?  50  LYS   A N     1 
ATOM   330  C CA    . LYS   A 1 70  ? -2.76600  -19.13800 44.95400 1.000 34.07439 ?  50  LYS   A CA    1 
ATOM   331  C C     . LYS   A 1 70  ? -4.12100  -19.70500 45.41000 1.000 31.60245 ?  50  LYS   A C     1 
ATOM   332  O O     . LYS   A 1 70  ? -4.51300  -20.82400 45.05200 1.000 33.13203 ?  50  LYS   A O     1 
ATOM   333  C CB    . LYS   A 1 70  ? -1.87700  -20.21500 44.33100 1.000 39.69830 ?  50  LYS   A CB    1 
ATOM   334  C CG    . LYS   A 1 70  ? -0.59700  -19.61300 43.72800 1.000 38.47047 ?  50  LYS   A CG    1 
ATOM   335  C CD    . LYS   A 1 70  ? -0.18000  -20.28700 42.45500 1.000 42.54298 ?  50  LYS   A CD    1 
ATOM   336  C CE    . LYS   A 1 70  ? 0.66200   -19.34400 41.63800 1.000 41.36666 ?  50  LYS   A CE    1 
ATOM   337  N N     . ASN   A 1 71  ? -4.87600  -18.90200 46.16500 1.000 31.74203 ?  51  ASN   A N     1 
ATOM   338  C CA    . ASN   A 1 71  ? -6.21600  -19.28500 46.60300 1.000 29.69981 ?  51  ASN   A CA    1 
ATOM   339  C C     . ASN   A 1 71  ? -7.30400  -18.86700 45.60800 1.000 28.28426 ?  51  ASN   A C     1 
ATOM   340  O O     . ASN   A 1 71  ? -8.22500  -19.63900 45.32600 1.000 29.25612 ?  51  ASN   A O     1 
ATOM   341  C CB    . ASN   A 1 71  ? -6.52600  -18.66500 47.97200 1.000 28.43997 ?  51  ASN   A CB    1 
ATOM   342  C CG    . ASN   A 1 71  ? -5.72000  -19.29900 49.10200 1.000 41.88538 ?  51  ASN   A CG    1 
ATOM   343  O OD1   . ASN   A 1 71  ? -5.60500  -20.52800 49.19200 1.000 37.51238 ?  51  ASN   A OD1   1 
ATOM   344  N ND2   . ASN   A 1 71  ? -5.15500  -18.46100 49.96600 1.000 37.32440 ?  51  ASN   A ND2   1 
ATOM   345  N N     . ARG   A 1 72  ? -7.24300  -17.63400 45.10600 1.000 27.13986 ?  52  ARG   A N     1 
ATOM   346  C CA    . ARG   A 1 72  ? -8.31600  -17.09700 44.28200 1.000 28.95518 ?  52  ARG   A CA    1 
ATOM   347  C C     . ARG   A 1 72  ? -7.70600  -16.31300 43.13100 1.000 27.03342 ?  52  ARG   A C     1 
ATOM   348  O O     . ARG   A 1 72  ? -6.79700  -15.50400 43.33800 1.000 24.05465 ?  52  ARG   A O     1 
ATOM   349  C CB    . ARG   A 1 72  ? -9.23700  -16.18500 45.10100 1.000 29.68788 ?  52  ARG   A CB    1 
ATOM   350  C CG    . ARG   A 1 72  ? -10.16700 -16.93700 46.05400 1.000 28.36874 ?  52  ARG   A CG    1 
ATOM   351  C CD    . ARG   A 1 72  ? -10.95800 -15.99200 46.96300 1.000 29.94270 ?  52  ARG   A CD    1 
ATOM   352  N NE    . ARG   A 1 72  ? -11.67900 -14.96800 46.22100 1.000 27.72755 ?  52  ARG   A NE    1 
ATOM   353  C CZ    . ARG   A 1 72  ? -12.86500 -15.15500 45.66300 1.000 26.79992 ?  52  ARG   A CZ    1 
ATOM   354  N NH1   . ARG   A 1 72  ? -13.44000 -16.34700 45.65200 1.000 31.52954 ?  52  ARG   A NH1   1 
ATOM   355  N NH2   . ARG   A 1 72  ? -13.47500 -14.12900 45.07300 1.000 25.45442 ?  52  ARG   A NH2   1 
ATOM   356  N N     . ALA   A 1 73  ? -8.20800  -16.54700 41.92700 1.000 21.95563 ?  53  ALA   A N     1 
ATOM   357  C CA    . ALA   A 1 73  ? -7.78600  -15.76100 40.77900 1.000 20.98211 ?  53  ALA   A CA    1 
ATOM   358  C C     . ALA   A 1 73  ? -9.01100  -15.38900 39.95300 1.000 21.94344 ?  53  ALA   A C     1 
ATOM   359  O O     . ALA   A 1 73  ? -10.02200 -16.09800 39.94500 1.000 22.59527 ?  53  ALA   A O     1 
ATOM   360  C CB    . ALA   A 1 73  ? -6.77500  -16.52000 39.90500 1.000 22.46678 ?  53  ALA   A CB    1 
ATOM   361  N N     . LEU   A 1 74  ? -8.91300  -14.25800 39.27000 1.000 21.21990 ?  54  LEU   A N     1 
ATOM   362  C CA    . LEU   A 1 74  ? -9.96700  -13.77000 38.39200 1.000 21.08915 ?  54  LEU   A CA    1 
ATOM   363  C C     . LEU   A 1 74  ? -9.40300  -13.64900 36.98400 1.000 19.31539 ?  54  LEU   A C     1 
ATOM   364  O O     . LEU   A 1 74  ? -8.34000  -13.04500 36.79400 1.000 21.58233 ?  54  LEU   A O     1 
ATOM   365  C CB    . LEU   A 1 74  ? -10.48300 -12.41100 38.89100 1.000 20.53381 ?  54  LEU   A CB    1 
ATOM   366  C CG    . LEU   A 1 74  ? -11.47100 -11.65800 37.99600 1.000 24.21562 ?  54  LEU   A CG    1 
ATOM   367  C CD1   . LEU   A 1 74  ? -12.77500 -12.42700 37.86900 1.000 23.16963 ?  54  LEU   A CD1   1 
ATOM   368  C CD2   . LEU   A 1 74  ? -11.70100 -10.26100 38.58100 1.000 23.49728 ?  54  LEU   A CD2   1 
ATOM   369  N N     . ASP   A 1 75  ? -10.09000 -14.25400 36.00100 1.000 18.90144 ?  55  ASP   A N     1 
ATOM   370  C CA    . ASP   A 1 75  ? -9.73400  -14.11900 34.58400 1.000 20.83957 ?  55  ASP   A CA    1 
ATOM   371  C C     . ASP   A 1 75  ? -10.78000 -13.18300 33.96900 1.000 20.77874 ?  55  ASP   A C     1 
ATOM   372  O O     . ASP   A 1 75  ? -11.91300 -13.59100 33.69900 1.000 19.66109 ?  55  ASP   A O     1 
ATOM   373  C CB    . ASP   A 1 75  ? -9.66500  -15.51500 33.93100 1.000 20.98306 ?  55  ASP   A CB    1 
ATOM   374  C CG    . ASP   A 1 75  ? -9.49300  -15.48000 32.39800 1.000 28.17601 ?  55  ASP   A CG    1 
ATOM   375  O OD1   . ASP   A 1 75  ? -8.92000  -14.49000 31.86000 1.000 28.62487 ?  55  ASP   A OD1   1 
ATOM   376  O OD2   . ASP   A 1 75  ? -10.00700 -16.42800 31.72100 1.000 28.42986 -1 55  ASP   A OD2   1 
ATOM   377  N N     . LEU   A 1 76  ? -10.40500 -11.90600 33.79300 1.000 19.54294 ?  56  LEU   A N     1 
ATOM   378  C CA    . LEU   A 1 76  ? -11.31900 -10.83600 33.40100 1.000 17.82384 ?  56  LEU   A CA    1 
ATOM   379  C C     . LEU   A 1 76  ? -11.28300 -10.60900 31.89600 1.000 17.59404 ?  56  LEU   A C     1 
ATOM   380  O O     . LEU   A 1 76  ? -10.22300 -10.31000 31.34500 1.000 22.01360 ?  56  LEU   A O     1 
ATOM   381  C CB    . LEU   A 1 76  ? -10.94800 -9.54100  34.12100 1.000 20.29365 ?  56  LEU   A CB    1 
ATOM   382  C CG    . LEU   A 1 76  ? -12.03200 -8.49700  34.33900 1.000 25.30852 ?  56  LEU   A CG    1 
ATOM   383  C CD1   . LEU   A 1 76  ? -13.42100 -9.02700  34.73900 1.000 26.83398 ?  56  LEU   A CD1   1 
ATOM   384  C CD2   . LEU   A 1 76  ? -11.48000 -7.50300  35.39300 1.000 28.02484 ?  56  LEU   A CD2   1 
ATOM   385  N N     . GLY   A 1 77  ? -12.44600 -10.70000 31.25200 1.000 19.52370 ?  57  GLY   A N     1 
ATOM   386  C CA    . GLY   A 1 77  ? -12.48400 -10.77000 29.80600 1.000 19.54558 ?  57  GLY   A CA    1 
ATOM   387  C C     . GLY   A 1 77  ? -12.13900 -12.15700 29.30300 1.000 19.98184 ?  57  GLY   A C     1 
ATOM   388  O O     . GLY   A 1 77  ? -11.38600 -12.29500 28.33000 1.000 21.65603 ?  57  GLY   A O     1 
ATOM   389  N N     . CYS   A 1 78  ? -12.65600 -13.19100 29.96100 1.000 19.37251 ?  58  CYS   A N     1 
ATOM   390  C CA    . CYS   A 1 78  ? -12.19400 -14.57200 29.76000 1.000 17.69631 ?  58  CYS   A CA    1 
ATOM   391  C C     . CYS   A 1 78  ? -12.56600 -15.16700 28.40700 1.000 22.75339 ?  58  CYS   A C     1 
ATOM   392  O O     . CYS   A 1 78  ? -12.03500 -16.23900 28.04800 1.000 21.39285 ?  58  CYS   A O     1 
ATOM   393  C CB    . CYS   A 1 78  ? -12.74500 -15.45200 30.89100 1.000 18.89683 ?  58  CYS   A CB    1 
ATOM   394  S SG    . CYS   A 1 78  ? -14.52000 -15.64400 30.89900 1.000 22.46587 ?  58  CYS   A SG    1 
ATOM   395  N N     . ALA   A 1 79  ? -13.43700 -14.51400 27.64200 1.000 18.28565 ?  59  ALA   A N     1 
ATOM   396  C CA    . ALA   A 1 79  ? -13.92600 -15.02900 26.35000 1.000 17.23406 ?  59  ALA   A CA    1 
ATOM   397  C C     . ALA   A 1 79  ? -14.38500 -16.47500 26.56200 1.000 19.06234 ?  59  ALA   A C     1 
ATOM   398  O O     . ALA   A 1 79  ? -15.20100 -16.72100 27.46000 1.000 20.15886 ?  59  ALA   A O     1 
ATOM   399  C CB    . ALA   A 1 79  ? -12.86400 -14.82800 25.27100 1.000 20.17566 ?  59  ALA   A CB    1 
ATOM   400  N N     . THR   A 1 80  ? -13.92400 -17.43900 25.75800 1.000 18.53492 ?  60  THR   A N     1 
ATOM   401  C CA    . THR   A 1 80  ? -14.43800 -18.80000 25.82700 1.000 20.91102 ?  60  THR   A CA    1 
ATOM   402  C C     . THR   A 1 80  ? -13.75400 -19.63000 26.91200 1.000 22.89254 ?  60  THR   A C     1 
ATOM   403  O O     . THR   A 1 80  ? -13.92300 -20.86200 26.94500 1.000 21.08521 ?  60  THR   A O     1 
ATOM   404  C CB    . THR   A 1 80  ? -14.32500 -19.47300 24.45400 1.000 21.31564 ?  60  THR   A CB    1 
ATOM   405  O OG1   . THR   A 1 80  ? -13.04500 -19.17700 23.86900 1.000 19.69171 ?  60  THR   A OG1   1 
ATOM   406  C CG2   . THR   A 1 80  ? -15.40800 -18.92300 23.51800 1.000 22.71634 ?  60  THR   A CG2   1 
ATOM   407  N N     . GLY   A 1 81  ? -13.01600 -18.98200 27.81200 1.000 17.80072 ?  61  GLY   A N     1 
ATOM   408  C CA    . GLY   A 1 81  ? -12.67200 -19.55900 29.11100 1.000 21.12654 ?  61  GLY   A CA    1 
ATOM   409  C C     . GLY   A 1 81  ? -11.34000 -20.29400 29.24400 1.000 17.08133 ?  61  GLY   A C     1 
ATOM   410  O O     . GLY   A 1 81  ? -11.02000 -20.74800 30.36200 1.000 18.51058 ?  61  GLY   A O     1 
ATOM   411  N N     . ARG   A 1 82  ? -10.53500 -20.41500 28.17900 1.000 19.02281 ?  62  ARG   A N     1 
ATOM   412  C CA    . ARG   A 1 82  ? -9.32100  -21.25700 28.25900 1.000 18.83276 ?  62  ARG   A CA    1 
ATOM   413  C C     . ARG   A 1 82  ? -8.37300  -20.83700 29.38500 1.000 19.09670 ?  62  ARG   A C     1 
ATOM   414  O O     . ARG   A 1 82  ? -7.79800  -21.68900 30.08100 1.000 18.36631 ?  62  ARG   A O     1 
ATOM   415  C CB    . ARG   A 1 82  ? -8.55800  -21.24900 26.93700 1.000 17.51462 ?  62  ARG   A CB    1 
ATOM   416  C CG    . ARG   A 1 82  ? -7.26200  -22.10400 26.91100 1.000 19.20356 ?  62  ARG   A CG    1 
ATOM   417  C CD    . ARG   A 1 82  ? -7.52000  -23.59900 27.13400 1.000 21.21919 ?  62  ARG   A CD    1 
ATOM   418  N NE    . ARG   A 1 82  ? -6.26000  -24.34500 27.19700 1.000 20.59083 ?  62  ARG   A NE    1 
ATOM   419  C CZ    . ARG   A 1 82  ? -5.61400  -24.83900 26.14600 1.000 22.74732 ?  62  ARG   A CZ    1 
ATOM   420  N NH1   . ARG   A 1 82  ? -6.03600  -24.62700 24.90100 1.000 21.82172 ?  62  ARG   A NH1   1 
ATOM   421  N NH2   . ARG   A 1 82  ? -4.50800  -25.56400 26.34500 1.000 21.98150 ?  62  ARG   A NH2   1 
ATOM   422  N N     . ALA   A 1 83  ? -8.10700  -19.54100 29.52200 1.000 17.32091 ?  63  ALA   A N     1 
ATOM   423  C CA    . ALA   A 1 83  ? -7.13900  -19.15300 30.54400 1.000 20.33484 ?  63  ALA   A CA    1 
ATOM   424  C C     . ALA   A 1 83  ? -7.68000  -19.42200 31.93900 1.000 21.05517 ?  63  ALA   A C     1 
ATOM   425  O O     . ALA   A 1 83  ? -6.89700  -19.62600 32.87500 1.000 19.85530 ?  63  ALA   A O     1 
ATOM   426  C CB    . ALA   A 1 83  ? -6.76100  -17.66500 30.40000 1.000 19.73398 ?  63  ALA   A CB    1 
ATOM   427  N N     . SER   A 1 84  ? -9.00600  -19.41000 32.10400 1.000 17.36898 ?  64  SER   A N     1 
ATOM   428  C CA    . SER   A 1 84  ? -9.59000  -19.71900 33.40700 1.000 20.01263 ?  64  SER   A CA    1 
ATOM   429  C C     . SER   A 1 84  ? -9.32800  -21.16700 33.77400 1.000 21.73029 ?  64  SER   A C     1 
ATOM   430  O O     . SER   A 1 84  ? -8.92200  -21.46500 34.90500 1.000 21.07675 ?  64  SER   A O     1 
ATOM   431  C CB    . SER   A 1 84  ? -11.10000 -19.46800 33.41600 1.000 19.39822 ?  64  SER   A CB    1 
ATOM   432  O OG    . SER   A 1 84  ? -11.43900 -18.12200 33.09600 1.000 23.01921 ?  64  SER   A OG    1 
ATOM   433  N N     . PHE   A 1 85  ? -9.59000  -22.07200 32.82700 1.000 19.41759 ?  65  PHE   A N     1 
ATOM   434  C CA    . PHE   A 1 85  ? -9.30200  -23.49300 33.04700 1.000 21.66744 ?  65  PHE   A CA    1 
ATOM   435  C C     . PHE   A 1 85  ? -7.83200  -23.72000 33.37000 1.000 24.84928 ?  65  PHE   A C     1 
ATOM   436  O O     . PHE   A 1 85  ? -7.49600  -24.58400 34.19300 1.000 19.90720 ?  65  PHE   A O     1 
ATOM   437  C CB    . PHE   A 1 85  ? -9.67600  -24.30300 31.80500 1.000 18.36110 ?  65  PHE   A CB    1 
ATOM   438  C CG    . PHE   A 1 85  ? -11.16000 -24.38700 31.54200 1.000 20.24505 ?  65  PHE   A CG    1 
ATOM   439  C CD1   . PHE   A 1 85  ? -12.03500 -24.80700 32.54400 1.000 21.26012 ?  65  PHE   A CD1   1 
ATOM   440  C CD2   . PHE   A 1 85  ? -11.66900 -24.08500 30.28900 1.000 19.53860 ?  65  PHE   A CD2   1 
ATOM   441  C CE1   . PHE   A 1 85  ? -13.39500 -24.90100 32.28300 1.000 21.49577 ?  65  PHE   A CE1   1 
ATOM   442  C CE2   . PHE   A 1 85  ? -13.02700 -24.17200 30.01400 1.000 20.73849 ?  65  PHE   A CE2   1 
ATOM   443  C CZ    . PHE   A 1 85  ? -13.89100 -24.59000 31.02100 1.000 23.14410 ?  65  PHE   A CZ    1 
ATOM   444  N N     . GLU   A 1 86  ? -6.93600  -22.99000 32.69200 1.000 18.42043 ?  66  GLU   A N     1 
ATOM   445  C CA    . GLU   A 1 86  ? -5.50700  -23.20300 32.89900 1.000 21.08453 ?  66  GLU   A CA    1 
ATOM   446  C C     . GLU   A 1 86  ? -5.05900  -22.63500 34.24500 1.000 22.71528 ?  66  GLU   A C     1 
ATOM   447  O O     . GLU   A 1 86  ? -4.24900  -23.25600 34.94200 1.000 21.34634 ?  66  GLU   A O     1 
ATOM   448  C CB    . GLU   A 1 86  ? -4.69200  -22.57600 31.74900 1.000 18.96391 ?  66  GLU   A CB    1 
ATOM   449  C CG    . GLU   A 1 86  ? -4.93800  -23.24100 30.38400 1.000 17.86234 ?  66  GLU   A CG    1 
ATOM   450  C CD    . GLU   A 1 86  ? -4.38700  -24.67600 30.30200 1.000 24.23007 ?  66  GLU   A CD    1 
ATOM   451  O OE1   . GLU   A 1 86  ? -3.70100  -25.11600 31.25300 1.000 25.72648 ?  66  GLU   A OE1   1 
ATOM   452  O OE2   . GLU   A 1 86  ? -4.66800  -25.35000 29.28400 1.000 21.55949 -1 66  GLU   A OE2   1 
ATOM   453  N N     . LEU   A 1 87  ? -5.56000  -21.44800 34.63400 1.000 18.89377 ?  67  LEU   A N     1 
ATOM   454  C CA    . LEU   A 1 87  ? -5.23400  -20.91800 35.96000 1.000 19.89372 ?  67  LEU   A CA    1 
ATOM   455  C C     . LEU   A 1 87  ? -5.68200  -21.87900 37.05700 1.000 25.81695 ?  67  LEU   A C     1 
ATOM   456  O O     . LEU   A 1 87  ? -5.04800  -21.97200 38.11500 1.000 23.27209 ?  67  LEU   A O     1 
ATOM   457  C CB    . LEU   A 1 87  ? -5.91700  -19.56600 36.17800 1.000 18.41495 ?  67  LEU   A CB    1 
ATOM   458  C CG    . LEU   A 1 87  ? -5.23000  -18.40200 35.46200 1.000 19.39799 ?  67  LEU   A CG    1 
ATOM   459  C CD1   . LEU   A 1 87  ? -6.03500  -17.10500 35.69000 1.000 23.03921 ?  67  LEU   A CD1   1 
ATOM   460  C CD2   . LEU   A 1 87  ? -3.75900  -18.20700 35.86900 1.000 22.00274 ?  67  LEU   A CD2   1 
ATOM   461  N N     . ALA   A 1 88  ? -6.81000  -22.55300 36.83800 1.000 20.43996 ?  68  ALA   A N     1 
ATOM   462  C CA    . ALA   A 1 88  ? -7.39100  -23.43000 37.84500 1.000 21.07861 ?  68  ALA   A CA    1 
ATOM   463  C C     . ALA   A 1 88  ? -6.52600  -24.65900 38.11900 1.000 25.28892 ?  68  ALA   A C     1 
ATOM   464  O O     . ALA   A 1 88  ? -6.75700  -25.35100 39.12500 1.000 25.63467 ?  68  ALA   A O     1 
ATOM   465  C CB    . ALA   A 1 88  ? -8.78700  -23.87700 37.39500 1.000 22.73454 ?  68  ALA   A CB    1 
ATOM   466  N N     . ARG   A 1 89  ? -5.57200  -24.96800 37.23500 1.000 21.95502 ?  69  ARG   A N     1 
ATOM   467  C CA    . ARG   A 1 89  ? -4.61500  -26.04200 37.53200 1.000 21.00889 ?  69  ARG   A CA    1 
ATOM   468  C C     . ARG   A 1 89  ? -3.71000  -25.67000 38.70000 1.000 30.16152 ?  69  ARG   A C     1 
ATOM   469  O O     . ARG   A 1 89  ? -3.17500  -26.55800 39.37000 1.000 29.65994 ?  69  ARG   A O     1 
ATOM   470  C CB    . ARG   A 1 89  ? -3.76300  -26.36400 36.30100 1.000 23.08236 ?  69  ARG   A CB    1 
ATOM   471  C CG    . ARG   A 1 89  ? -4.58800  -26.82100 35.09100 1.000 23.36858 ?  69  ARG   A CG    1 
ATOM   472  C CD    . ARG   A 1 89  ? -3.75200  -27.52100 34.02700 1.000 22.37317 ?  69  ARG   A CD    1 
ATOM   473  N NE    . ARG   A 1 89  ? -3.52100  -28.91900 34.41200 1.000 26.25742 ?  69  ARG   A NE    1 
ATOM   474  C CZ    . ARG   A 1 89  ? -2.42600  -29.60700 34.12300 1.000 29.74645 ?  69  ARG   A CZ    1 
ATOM   475  N NH1   . ARG   A 1 89  ? -1.45600  -29.08600 33.38500 1.000 25.13506 ?  69  ARG   A NH1   1 
ATOM   476  N NH2   . ARG   A 1 89  ? -2.31600  -30.86800 34.56100 1.000 29.07163 ?  69  ARG   A NH2   1 
ATOM   477  N N     . SER   A 1 90  ? -3.53400  -24.37700 38.97000 1.000 25.93314 ?  70  SER   A N     1 
ATOM   478  C CA    . SER   A 1 90  ? -2.68900  -23.95000 40.06900 1.000 28.33937 ?  70  SER   A CA    1 
ATOM   479  C C     . SER   A 1 90  ? -3.42100  -23.21100 41.17200 1.000 29.26583 ?  70  SER   A C     1 
ATOM   480  O O     . SER   A 1 90  ? -2.90900  -23.17100 42.29100 1.000 32.82414 ?  70  SER   A O     1 
ATOM   481  C CB    . SER   A 1 90  ? -1.55200  -23.05200 39.55900 1.000 27.02221 ?  70  SER   A CB    1 
ATOM   482  O OG    . SER   A 1 90  ? -0.68200  -23.80700 38.73800 1.000 39.33036 ?  70  SER   A OG    1 
ATOM   483  N N     . TYR   A 1 91  ? -4.58500  -22.62100 40.90100 1.000 25.64661 ?  71  TYR   A N     1 
ATOM   484  C CA    . TYR   A 1 91  ? -5.33500  -21.87800 41.90300 1.000 23.67174 ?  71  TYR   A CA    1 
ATOM   485  C C     . TYR   A 1 91  ? -6.47200  -22.73000 42.46200 1.000 28.31372 ?  71  TYR   A C     1 
ATOM   486  O O     . TYR   A 1 91  ? -7.04400  -23.57400 41.76000 1.000 28.00025 ?  71  TYR   A O     1 
ATOM   487  C CB    . TYR   A 1 91  ? -5.88700  -20.57400 41.30600 1.000 23.78338 ?  71  TYR   A CB    1 
ATOM   488  C CG    . TYR   A 1 91  ? -4.81500  -19.48400 41.24700 1.000 25.89037 ?  71  TYR   A CG    1 
ATOM   489  C CD1   . TYR   A 1 91  ? -3.82700  -19.49900 40.27200 1.000 24.11795 ?  71  TYR   A CD1   1 
ATOM   490  C CD2   . TYR   A 1 91  ? -4.75500  -18.49100 42.22000 1.000 26.97242 ?  71  TYR   A CD2   1 
ATOM   491  C CE1   . TYR   A 1 91  ? -2.82800  -18.51700 40.23500 1.000 23.36226 ?  71  TYR   A CE1   1 
ATOM   492  C CE2   . TYR   A 1 91  ? -3.76500  -17.52400 42.20100 1.000 26.12783 ?  71  TYR   A CE2   1 
ATOM   493  C CZ    . TYR   A 1 91  ? -2.80300  -17.53900 41.21400 1.000 24.68809 ?  71  TYR   A CZ    1 
ATOM   494  O OH    . TYR   A 1 91  ? -1.82400  -16.58100 41.21800 1.000 28.19414 ?  71  TYR   A OH    1 
ATOM   495  N N     . LYS   A 1 92  ? -6.80800  -22.49100 43.73800 1.000 26.58087 ?  72  LYS   A N     1 
ATOM   496  C CA    . LYS   A 1 92  ? -7.88600  -23.25500 44.36800 1.000 26.88414 ?  72  LYS   A CA    1 
ATOM   497  C C     . LYS   A 1 92  ? -9.25100  -22.87000 43.81900 1.000 27.22742 ?  72  LYS   A C     1 
ATOM   498  O O     . LYS   A 1 92  ? -10.16100 -23.70500 43.76700 1.000 25.60905 ?  72  LYS   A O     1 
ATOM   499  C CB    . LYS   A 1 92  ? -7.85000  -23.06400 45.89000 1.000 30.33560 ?  72  LYS   A CB    1 
ATOM   500  C CG    . LYS   A 1 92  ? -6.53500  -23.45800 46.53300 1.000 38.72118 ?  72  LYS   A CG    1 
ATOM   501  C CD    . LYS   A 1 92  ? -6.65900  -23.48600 48.05700 1.000 42.29833 ?  72  LYS   A CD    1 
ATOM   502  N N     . HIS   A 1 93  ? -9.42600  -21.60800 43.42400 1.000 26.74636 ?  73  HIS   A N     1 
ATOM   503  C CA    . HIS   A 1 93  ? -10.67500 -21.17900 42.82900 1.000 24.02631 ?  73  HIS   A CA    1 
ATOM   504  C C     . HIS   A 1 93  ? -10.36000 -20.15000 41.76400 1.000 21.89217 ?  73  HIS   A C     1 
ATOM   505  O O     . HIS   A 1 93  ? -9.51400  -19.28100 41.98600 1.000 25.15972 ?  73  HIS   A O     1 
ATOM   506  C CB    . HIS   A 1 93  ? -11.63300 -20.56600 43.84400 1.000 25.44819 ?  73  HIS   A CB    1 
ATOM   507  C CG    . HIS   A 1 93  ? -12.93100 -20.15300 43.23100 1.000 30.45498 ?  73  HIS   A CG    1 
ATOM   508  N ND1   . HIS   A 1 93  ? -13.80700 -21.06400 42.67800 1.000 33.86349 ?  73  HIS   A ND1   1 
ATOM   509  C CD2   . HIS   A 1 93  ? -13.45900 -18.92700 42.99100 1.000 31.27589 ?  73  HIS   A CD2   1 
ATOM   510  C CE1   . HIS   A 1 93  ? -14.84200 -20.42000 42.16700 1.000 34.04006 ?  73  HIS   A CE1   1 
ATOM   511  N NE2   . HIS   A 1 93  ? -14.65800 -19.12300 42.34700 1.000 33.61048 ?  73  HIS   A NE2   1 
ATOM   512  N N     . VAL   A 1 94  ? -11.03900 -20.24200 40.61900 1.000 22.37903 ?  74  VAL   A N     1 
ATOM   513  C CA    . VAL   A 1 94  ? -10.90000 -19.23700 39.55900 1.000 21.25452 ?  74  VAL   A CA    1 
ATOM   514  C C     . VAL   A 1 94  ? -12.28600 -18.78900 39.11600 1.000 21.54094 ?  74  VAL   A C     1 
ATOM   515  O O     . VAL   A 1 94  ? -13.16100 -19.62300 38.85300 1.000 23.33322 ?  74  VAL   A O     1 
ATOM   516  C CB    . VAL   A 1 94  ? -10.11400 -19.76500 38.34000 1.000 20.29915 ?  74  VAL   A CB    1 
ATOM   517  C CG1   . VAL   A 1 94  ? -10.02100 -18.67400 37.25700 1.000 21.54419 ?  74  VAL   A CG1   1 
ATOM   518  C CG2   . VAL   A 1 94  ? -8.73100  -20.27400 38.74200 1.000 20.60855 ?  74  VAL   A CG2   1 
ATOM   519  N N     . ASP   A 1 95  ? -12.48000 -17.47500 39.01100 1.000 22.41500 ?  75  ASP   A N     1 
ATOM   520  C CA    . ASP   A 1 95  ? -13.68400 -16.89300 38.43200 1.000 19.55699 ?  75  ASP   A CA    1 
ATOM   521  C C     . ASP   A 1 95  ? -13.32900 -16.40300 37.03200 1.000 20.02511 ?  75  ASP   A C     1 
ATOM   522  O O     . ASP   A 1 95  ? -12.33000 -15.69700 36.86400 1.000 24.26383 ?  75  ASP   A O     1 
ATOM   523  C CB    . ASP   A 1 95  ? -14.19200 -15.70500 39.25700 1.000 22.58938 ?  75  ASP   A CB    1 
ATOM   524  C CG    . ASP   A 1 95  ? -14.74800 -16.13400 40.61600 1.000 25.95707 ?  75  ASP   A CG    1 
ATOM   525  O OD1   . ASP   A 1 95  ? -15.57900 -17.08000 40.67800 1.000 26.45467 ?  75  ASP   A OD1   1 
ATOM   526  O OD2   . ASP   A 1 95  ? -14.39300 -15.46500 41.60900 1.000 29.20030 -1 75  ASP   A OD2   1 
ATOM   527  N N     . GLY   A 1 96  ? -14.12500 -16.77100 36.03000 1.000 20.55934 ?  76  GLY   A N     1 
ATOM   528  C CA    . GLY   A 1 96  ? -13.96400 -16.23600 34.68000 1.000 19.17875 ?  76  GLY   A CA    1 
ATOM   529  C C     . GLY   A 1 96  ? -15.15700 -15.33300 34.41100 1.000 20.42629 ?  76  GLY   A C     1 
ATOM   530  O O     . GLY   A 1 96  ? -16.29700 -15.74500 34.59400 1.000 22.12018 ?  76  GLY   A O     1 
ATOM   531  N N     . VAL   A 1 97  ? -14.88200 -14.08000 34.04600 1.000 17.44546 ?  77  VAL   A N     1 
ATOM   532  C CA    . VAL   A 1 97  ? -15.93900 -13.09300 33.85700 1.000 18.03731 ?  77  VAL   A CA    1 
ATOM   533  C C     . VAL   A 1 97  ? -15.78700 -12.50500 32.46000 1.000 19.83526 ?  77  VAL   A C     1 
ATOM   534  O O     . VAL   A 1 97  ? -14.67300 -12.14200 32.05400 1.000 21.12790 ?  77  VAL   A O     1 
ATOM   535  C CB    . VAL   A 1 97  ? -15.87500 -11.97800 34.93300 1.000 17.71179 ?  77  VAL   A CB    1 
ATOM   536  C CG1   . VAL   A 1 97  ? -16.88200 -10.87100 34.64200 1.000 21.24418 ?  77  VAL   A CG1   1 
ATOM   537  C CG2   . VAL   A 1 97  ? -16.12800 -12.58400 36.30400 1.000 21.33195 ?  77  VAL   A CG2   1 
ATOM   538  N N     . ASP   A 1 98  ? -16.89300 -12.41300 31.72900 1.000 20.42806 ?  78  ASP   A N     1 
ATOM   539  C CA    . ASP   A 1 98  ? -16.88700 -11.74500 30.43100 1.000 19.45493 ?  78  ASP   A CA    1 
ATOM   540  C C     . ASP   A 1 98  ? -18.17900 -10.97100 30.24000 1.000 22.32197 ?  78  ASP   A C     1 
ATOM   541  O O     . ASP   A 1 98  ? -19.23000 -11.35900 30.73800 1.000 22.92004 ?  78  ASP   A O     1 
ATOM   542  C CB    . ASP   A 1 98  ? -16.70900 -12.72800 29.25500 1.000 21.03887 ?  78  ASP   A CB    1 
ATOM   543  C CG    . ASP   A 1 98  ? -16.12000 -12.04400 28.02800 1.000 21.88375 ?  78  ASP   A CG    1 
ATOM   544  O OD1   . ASP   A 1 98  ? -16.90100 -11.46200 27.23900 1.000 21.01146 ?  78  ASP   A OD1   1 
ATOM   545  O OD2   . ASP   A 1 98  ? -14.87200 -12.01000 27.90200 1.000 21.09194 -1 78  ASP   A OD2   1 
ATOM   546  N N     . TYR   A 1 99  ? -18.08500 -9.88200  29.47800 1.000 19.63398 ?  79  TYR   A N     1 
ATOM   547  C CA    . TYR   A 1 99  ? -19.26200 -9.08100  29.17100 1.000 20.85928 ?  79  TYR   A CA    1 
ATOM   548  C C     . TYR   A 1 99  ? -20.17700 -9.75900  28.16300 1.000 25.47850 ?  79  TYR   A C     1 
ATOM   549  O O     . TYR   A 1 99  ? -21.38600 -9.49000  28.15700 1.000 23.29578 ?  79  TYR   A O     1 
ATOM   550  C CB    . TYR   A 1 99  ? -18.79700 -7.71700  28.67000 1.000 20.09937 ?  79  TYR   A CB    1 
ATOM   551  C CG    . TYR   A 1 99  ? -19.86600 -6.66900  28.63300 1.000 25.46179 ?  79  TYR   A CG    1 
ATOM   552  C CD1   . TYR   A 1 99  ? -20.17800 -5.91800  29.76100 1.000 33.10035 ?  79  TYR   A CD1   1 
ATOM   553  C CD2   . TYR   A 1 99  ? -20.52100 -6.38600  27.43700 1.000 34.76212 ?  79  TYR   A CD2   1 
ATOM   554  C CE1   . TYR   A 1 99  ? -21.15600 -4.92500  29.70900 1.000 39.28131 ?  79  TYR   A CE1   1 
ATOM   555  C CE2   . TYR   A 1 99  ? -21.49300 -5.40500  27.37400 1.000 45.93851 ?  79  TYR   A CE2   1 
ATOM   556  C CZ    . TYR   A 1 99  ? -21.80300 -4.67600  28.51000 1.000 46.70691 ?  79  TYR   A CZ    1 
ATOM   557  O OH    . TYR   A 1 99  ? -22.77100 -3.69300  28.43800 1.000 63.16334 ?  79  TYR   A OH    1 
ATOM   558  N N     . SER   A 1 100 ? -19.63700 -10.65100 27.32400 1.000 20.21403 ?  80  SER   A N     1 
ATOM   559  C CA    . SER   A 1 100 ? -20.42400 -11.35400 26.31800 1.000 20.81427 ?  80  SER   A CA    1 
ATOM   560  C C     . SER   A 1 100 ? -21.09400 -12.59600 26.90900 1.000 22.41875 ?  80  SER   A C     1 
ATOM   561  O O     . SER   A 1 100 ? -20.41600 -13.54300 27.34000 1.000 21.39190 ?  80  SER   A O     1 
ATOM   562  C CB    . SER   A 1 100 ? -19.55400 -11.75700 25.13500 1.000 21.90166 ?  80  SER   A CB    1 
ATOM   563  O OG    . SER   A 1 100 ? -20.20200 -12.76700 24.39700 1.000 22.80985 ?  80  SER   A OG    1 
ATOM   564  N N     . GLN   A 1 101 ? -22.42600 -12.60800 26.89000 1.000 21.88151 ?  81  GLN   A N     1 
ATOM   565  C CA    . GLN   A 1 101 ? -23.15500 -13.78500 27.35300 1.000 24.66871 ?  81  GLN   A CA    1 
ATOM   566  C C     . GLN   A 1 101 ? -22.85000 -14.98800 26.47100 1.000 23.05863 ?  81  GLN   A C     1 
ATOM   567  O O     . GLN   A 1 101 ? -22.79300 -16.12300 26.95600 1.000 22.81036 ?  81  GLN   A O     1 
ATOM   568  C CB    . GLN   A 1 101 ? -24.65400 -13.50100 27.36600 1.000 26.88251 ?  81  GLN   A CB    1 
ATOM   569  C CG    . GLN   A 1 101 ? -25.48000 -14.62500 28.03400 1.000 25.71868 ?  81  GLN   A CG    1 
ATOM   570  C CD    . GLN   A 1 101 ? -25.22600 -14.75900 29.52600 1.000 26.49542 ?  81  GLN   A CD    1 
ATOM   571  O OE1   . GLN   A 1 101 ? -25.40500 -13.80300 30.28800 1.000 30.49433 ?  81  GLN   A OE1   1 
ATOM   572  N NE2   . GLN   A 1 101 ? -24.82500 -15.95400 29.95900 1.000 27.95710 ?  81  GLN   A NE2   1 
ATOM   573  N N     . ALA   A 1 102 ? -22.66200 -14.76100 25.16400 1.000 22.08669 ?  82  ALA   A N     1 
ATOM   574  C CA    . ALA   A 1 102 ? -22.37400 -15.87000 24.25600 1.000 24.69209 ?  82  ALA   A CA    1 
ATOM   575  C C     . ALA   A 1 102 ? -21.06000 -16.55300 24.61200 1.000 23.20314 ?  82  ALA   A C     1 
ATOM   576  O O     . ALA   A 1 102 ? -20.95100 -17.78500 24.52900 1.000 22.14470 ?  82  ALA   A O     1 
ATOM   577  C CB    . ALA   A 1 102 ? -22.32900 -15.38900 22.81200 1.000 23.44027 ?  82  ALA   A CB    1 
ATOM   578  N N     . PHE   A 1 103 ? -20.03900 -15.76500 24.97900 1.000 20.67561 ?  83  PHE   A N     1 
ATOM   579  C CA    . PHE   A 1 103 ? -18.76400 -16.34600 25.40100 1.000 19.92579 ?  83  PHE   A CA    1 
ATOM   580  C C     . PHE   A 1 103 ? -18.92600 -17.13400 26.69900 1.000 19.40164 ?  83  PHE   A C     1 
ATOM   581  O O     . PHE   A 1 103 ? -18.37400 -18.23400 26.84200 1.000 20.97790 ?  83  PHE   A O     1 
ATOM   582  C CB    . PHE   A 1 103 ? -17.72500 -15.23600 25.60900 1.000 17.66989 ?  83  PHE   A CB    1 
ATOM   583  C CG    . PHE   A 1 103 ? -17.09200 -14.71700 24.33500 1.000 21.02351 ?  83  PHE   A CG    1 
ATOM   584  C CD1   . PHE   A 1 103 ? -17.19500 -15.40900 23.14600 1.000 22.61687 ?  83  PHE   A CD1   1 
ATOM   585  C CD2   . PHE   A 1 103 ? -16.35600 -13.52700 24.35200 1.000 20.83023 ?  83  PHE   A CD2   1 
ATOM   586  C CE1   . PHE   A 1 103 ? -16.59300 -14.92700 21.97300 1.000 24.68451 ?  83  PHE   A CE1   1 
ATOM   587  C CE2   . PHE   A 1 103 ? -15.74400 -13.04600 23.20000 1.000 22.45912 ?  83  PHE   A CE2   1 
ATOM   588  C CZ    . PHE   A 1 103 ? -15.85800 -13.75600 22.00500 1.000 19.64358 ?  83  PHE   A CZ    1 
ATOM   589  N N     . VAL   A 1 104 ? -19.65000 -16.55900 27.66500 1.000 19.33236 ?  84  VAL   A N     1 
ATOM   590  C CA    . VAL   A 1 104 ? -19.87500 -17.21600 28.94800 1.000 21.36896 ?  84  VAL   A CA    1 
ATOM   591  C C     . VAL   A 1 104 ? -20.63400 -18.52300 28.74400 1.000 20.40606 ?  84  VAL   A C     1 
ATOM   592  O O     . VAL   A 1 104 ? -20.32200 -19.54600 29.37600 1.000 21.57601 ?  84  VAL   A O     1 
ATOM   593  C CB    . VAL   A 1 104 ? -20.63200 -16.27400 29.91300 1.000 25.07232 ?  84  VAL   A CB    1 
ATOM   594  C CG1   . VAL   A 1 104 ? -21.09100 -17.05600 31.17500 1.000 25.66727 ?  84  VAL   A CG1   1 
ATOM   595  C CG2   . VAL   A 1 104 ? -19.77800 -15.09100 30.31000 1.000 23.86907 ?  84  VAL   A CG2   1 
ATOM   596  N N     . ASP   A 1 105 ? -21.65000 -18.50400 27.87200 1.000 23.17086 ?  85  ASP   A N     1 
ATOM   597  C CA    . ASP   A 1 105 ? -22.40200 -19.72100 27.58000 1.000 26.14642 ?  85  ASP   A CA    1 
ATOM   598  C C     . ASP   A 1 105 ? -21.49300 -20.79700 26.99400 1.000 24.91087 ?  85  ASP   A C     1 
ATOM   599  O O     . ASP   A 1 105 ? -21.58300 -21.96800 27.38700 1.000 22.16660 ?  85  ASP   A O     1 
ATOM   600  C CB    . ASP   A 1 105 ? -23.56300 -19.44100 26.61500 1.000 24.56631 ?  85  ASP   A CB    1 
ATOM   601  C CG    . ASP   A 1 105 ? -24.68500 -18.57300 27.22200 1.000 28.07140 ?  85  ASP   A CG    1 
ATOM   602  O OD1   . ASP   A 1 105 ? -24.77500 -18.42600 28.45200 1.000 27.15131 ?  85  ASP   A OD1   1 
ATOM   603  O OD2   . ASP   A 1 105 ? -25.49700 -18.04100 26.42900 1.000 35.12398 -1 85  ASP   A OD2   1 
ATOM   604  N N     . ALA   A 1 106 ? -20.60500 -20.41800 26.06100 1.000 17.93595 ?  86  ALA   A N     1 
ATOM   605  C CA    . ALA   A 1 106 ? -19.70600 -21.39700 25.43500 1.000 19.08283 ?  86  ALA   A CA    1 
ATOM   606  C C     . ALA   A 1 106 ? -18.76700 -22.02000 26.45200 1.000 22.23713 ?  86  ALA   A C     1 
ATOM   607  O O     . ALA   A 1 106 ? -18.56600 -23.24500 26.46900 1.000 23.04470 ?  86  ALA   A O     1 
ATOM   608  C CB    . ALA   A 1 106 ? -18.89900 -20.74800 24.30500 1.000 20.12694 ?  86  ALA   A CB    1 
ATOM   609  N N     . ALA   A 1 107 ? -18.16100 -21.19000 27.29900 1.000 19.15510 ?  87  ALA   A N     1 
ATOM   610  C CA    . ALA   A 1 107 ? -17.25800 -21.71600 28.31600 1.000 19.64002 ?  87  ALA   A CA    1 
ATOM   611  C C     . ALA   A 1 107 ? -17.99700 -22.64800 29.27100 1.000 21.28123 ?  87  ALA   A C     1 
ATOM   612  O O     . ALA   A 1 107 ? -17.47400 -23.70900 29.65500 1.000 22.66078 ?  87  ALA   A O     1 
ATOM   613  C CB    . ALA   A 1 107 ? -16.62900 -20.54300 29.08800 1.000 19.38394 ?  87  ALA   A CB    1 
ATOM   614  N N     . THR   A 1 108 ? -19.21100 -22.25300 29.67500 1.000 21.36778 ?  88  THR   A N     1 
ATOM   615  C CA    . THR   A 1 108 ? -19.99800 -23.04800 30.61700 1.000 20.22231 ?  88  THR   A CA    1 
ATOM   616  C C     . THR   A 1 108 ? -20.41500 -24.37500 29.98500 1.000 22.25054 ?  88  THR   A C     1 
ATOM   617  O O     . THR   A 1 108 ? -20.42100 -25.42500 30.64900 1.000 22.10431 ?  88  THR   A O     1 
ATOM   618  C CB    . THR   A 1 108 ? -21.21700 -22.23600 31.06800 1.000 22.45999 ?  88  THR   A CB    1 
ATOM   619  O OG1   . THR   A 1 108 ? -20.78300 -20.99500 31.65600 1.000 24.93227 ?  88  THR   A OG1   1 
ATOM   620  C CG2   . THR   A 1 108 ? -22.02800 -22.99300 32.10800 1.000 23.63802 ?  88  THR   A CG2   1 
ATOM   621  N N     . GLU   A 1 109 ? -20.71900 -24.34200 28.68700 1.000 22.63584 ?  89  GLU   A N     1 
ATOM   622  C CA    . GLU   A 1 109 ? -21.11600 -25.55000 27.97300 1.000 23.63608 ?  89  GLU   A CA    1 
ATOM   623  C C     . GLU   A 1 109 ? -19.96000 -26.52800 27.89300 1.000 25.15529 ?  89  GLU   A C     1 
ATOM   624  O O     . GLU   A 1 109 ? -20.13500 -27.72900 28.12000 1.000 23.64277 ?  89  GLU   A O     1 
ATOM   625  C CB    . GLU   A 1 109 ? -21.61900 -25.19400 26.56600 1.000 23.89981 ?  89  GLU   A CB    1 
ATOM   626  C CG    . GLU   A 1 109 ? -23.04500 -24.59300 26.56400 1.000 23.42187 ?  89  GLU   A CG    1 
ATOM   627  C CD    . GLU   A 1 109 ? -23.30100 -23.64300 25.38500 1.000 32.45723 ?  89  GLU   A CD    1 
ATOM   628  O OE1   . GLU   A 1 109 ? -22.42100 -23.51000 24.50800 1.000 31.53193 ?  89  GLU   A OE1   1 
ATOM   629  O OE2   . GLU   A 1 109 ? -24.40300 -23.06200 25.32100 1.000 30.89883 -1 89  GLU   A OE2   1 
ATOM   630  N N     . LEU   A 1 110 ? -18.76700 -26.03700 27.55800 1.000 20.30605 ?  90  LEU   A N     1 
ATOM   631  C CA    . LEU   A 1 110 ? -17.60600 -26.92200 27.55000 1.000 20.93907 ?  90  LEU   A CA    1 
ATOM   632  C C     . LEU   A 1 110 ? -17.37300 -27.49900 28.93900 1.000 25.45583 ?  90  LEU   A C     1 
ATOM   633  O O     . LEU   A 1 110 ? -17.15300 -28.70800 29.10400 1.000 25.91117 ?  90  LEU   A O     1 
ATOM   634  C CB    . LEU   A 1 110 ? -16.37200 -26.17000 27.05000 1.000 20.96582 ?  90  LEU   A CB    1 
ATOM   635  C CG    . LEU   A 1 110 ? -15.04700 -26.93600 26.99500 1.000 23.40161 ?  90  LEU   A CG    1 
ATOM   636  C CD1   . LEU   A 1 110 ? -15.14800 -28.17300 26.06800 1.000 20.28360 ?  90  LEU   A CD1   1 
ATOM   637  C CD2   . LEU   A 1 110 ? -13.90500 -25.99100 26.53600 1.000 23.02154 ?  90  LEU   A CD2   1 
ATOM   638  N N     . GLN   A 1 111 ? -17.44300 -26.63900 29.95900 1.000 22.41537 ?  91  GLN   A N     1 
ATOM   639  C CA    . GLN   A 1 111 ? -17.20400 -27.06700 31.33200 1.000 19.51717 ?  91  GLN   A CA    1 
ATOM   640  C C     . GLN   A 1 111 ? -18.19600 -28.14000 31.77400 1.000 25.36194 ?  91  GLN   A C     1 
ATOM   641  O O     . GLN   A 1 111 ? -17.81000 -29.14600 32.37900 1.000 27.28059 ?  91  GLN   A O     1 
ATOM   642  C CB    . GLN   A 1 111 ? -17.30300 -25.86000 32.26100 1.000 22.29334 ?  91  GLN   A CB    1 
ATOM   643  C CG    . GLN   A 1 111 ? -17.06400 -26.18300 33.71700 1.000 23.05007 ?  91  GLN   A CG    1 
ATOM   644  C CD    . GLN   A 1 111 ? -17.38000 -24.98100 34.60600 1.000 21.72833 ?  91  GLN   A CD    1 
ATOM   645  O OE1   . GLN   A 1 111 ? -18.34000 -24.23800 34.35700 1.000 22.92178 ?  91  GLN   A OE1   1 
ATOM   646  N NE2   . GLN   A 1 111 ? -16.59500 -24.80100 35.64600 1.000 22.86782 ?  91  GLN   A NE2   1 
ATOM   647  N N     . LYS   A 1 112 ? -19.48300 -27.91600 31.52100 1.000 21.90535 ?  92  LYS   A N     1 
ATOM   648  C CA    . LYS   A 1 112 ? -20.54000 -28.77100 32.05300 1.000 28.37308 ?  92  LYS   A CA    1 
ATOM   649  C C     . LYS   A 1 112 ? -20.90200 -29.92500 31.12600 1.000 30.84635 ?  92  LYS   A C     1 
ATOM   650  O O     . LYS   A 1 112 ? -21.18000 -31.02800 31.60900 1.000 33.73889 ?  92  LYS   A O     1 
ATOM   651  C CB    . LYS   A 1 112 ? -21.78900 -27.94400 32.34500 1.000 26.27507 ?  92  LYS   A CB    1 
ATOM   652  C CG    . LYS   A 1 112 ? -21.52300 -26.72000 33.21100 1.000 36.48885 ?  92  LYS   A CG    1 
ATOM   653  C CD    . LYS   A 1 112 ? -21.70400 -26.97400 34.68400 1.000 45.10165 ?  92  LYS   A CD    1 
ATOM   654  N N     . ASN   A 1 113 ? -20.92300 -29.71300 29.80900 1.000 23.36919 ?  93  ASN   A N     1 
ATOM   655  C CA    . ASN   A 1 113 ? -21.22700 -30.81500 28.89600 1.000 27.16788 ?  93  ASN   A CA    1 
ATOM   656  C C     . ASN   A 1 113 ? -19.99700 -31.59700 28.46900 1.000 32.47046 ?  93  ASN   A C     1 
ATOM   657  O O     . ASN   A 1 113 ? -20.14200 -32.72500 27.99300 1.000 30.87076 ?  93  ASN   A O     1 
ATOM   658  C CB    . ASN   A 1 113 ? -21.93900 -30.30700 27.63400 1.000 28.61788 ?  93  ASN   A CB    1 
ATOM   659  C CG    . ASN   A 1 113 ? -23.23600 -29.59100 27.93800 1.000 31.09260 ?  93  ASN   A CG    1 
ATOM   660  O OD1   . ASN   A 1 113 ? -23.89400 -29.87000 28.94200 1.000 40.48005 ?  93  ASN   A OD1   1 
ATOM   661  N ND2   . ASN   A 1 113 ? -23.62300 -28.67300 27.05800 1.000 35.43947 ?  93  ASN   A ND2   1 
ATOM   662  N N     . GLY   A 1 114 ? -18.80000 -31.02600 28.60400 1.000 21.77465 ?  94  GLY   A N     1 
ATOM   663  C CA    . GLY   A 1 114 ? -17.57700 -31.69800 28.22400 1.000 23.69643 ?  94  GLY   A CA    1 
ATOM   664  C C     . GLY   A 1 114 ? -17.18600 -31.56200 26.77000 1.000 25.21883 ?  94  GLY   A C     1 
ATOM   665  O O     . GLY   A 1 114 ? -16.14100 -32.09700 26.36900 1.000 25.13701 ?  94  GLY   A O     1 
ATOM   666  N N     . CYS   A 1 115 ? -17.99300 -30.88500 25.96000 1.000 22.25570 ?  95  CYS   A N     1 
ATOM   667  C CA    . CYS   A 1 115 ? -17.63400 -30.65300 24.57200 1.000 25.53003 ?  95  CYS   A CA    1 
ATOM   668  C C     . CYS   A 1 115 ? -18.44500 -29.48000 24.04700 1.000 23.42098 ?  95  CYS   A C     1 
ATOM   669  O O     . CYS   A 1 115 ? -19.51000 -29.15100 24.57700 1.000 26.94923 ?  95  CYS   A O     1 
ATOM   670  C CB    . CYS   A 1 115 ? -17.85700 -31.89700 23.71100 1.000 29.96686 ?  95  CYS   A CB    1 
ATOM   671  S SG    . CYS   A 1 115 ? -19.58900 -32.38200 23.66000 1.000 39.15804 ?  95  CYS   A SG    1 
ATOM   672  N N     . ILE   A 1 116 ? -17.89800 -28.83100 23.02000 1.000 22.13937 ?  96  ILE   A N     1 
ATOM   673  C CA    . ILE   A 1 116 ? -18.63000 -27.83500 22.24300 1.000 20.60009 ?  96  ILE   A CA    1 
ATOM   674  C C     . ILE   A 1 116 ? -18.12900 -27.93600 20.81700 1.000 24.13669 ?  96  ILE   A C     1 
ATOM   675  O O     . ILE   A 1 116 ? -16.97200 -28.28800 20.57200 1.000 24.74881 ?  96  ILE   A O     1 
ATOM   676  C CB    . ILE   A 1 116 ? -18.46300 -26.37500 22.74200 1.000 25.21722 ?  96  ILE   A CB    1 
ATOM   677  C CG1   . ILE   A 1 116 ? -17.00400 -26.04900 23.05300 1.000 25.09748 ?  96  ILE   A CG1   1 
ATOM   678  C CG2   . ILE   A 1 116 ? -19.34500 -26.10100 23.94400 1.000 33.46331 ?  96  ILE   A CG2   1 
ATOM   679  C CD1   . ILE   A 1 116 ? -16.79200 -24.53800 23.36600 1.000 30.96613 ?  96  ILE   A CD1   1 
ATOM   680  N N     . GLY   A 1 117 ? -19.00200 -27.59800 19.87500 1.000 24.25957 ?  97  GLY   A N     1 
ATOM   681  C CA    . GLY   A 1 117 ? -18.59500 -27.53600 18.48800 1.000 24.62166 ?  97  GLY   A CA    1 
ATOM   682  C C     . GLY   A 1 117 ? -18.43600 -26.10700 18.00900 1.000 21.49464 ?  97  GLY   A C     1 
ATOM   683  O O     . GLY   A 1 117 ? -18.98200 -25.17000 18.61600 1.000 22.37475 ?  97  GLY   A O     1 
ATOM   684  N N     . TYR   A 1 118 ? -17.69900 -25.92100 16.91400 1.000 21.61771 ?  98  TYR   A N     1 
ATOM   685  C CA    . TYR   A 1 118 ? -17.55100 -24.59600 16.32300 1.000 25.91480 ?  98  TYR   A CA    1 
ATOM   686  C C     . TYR   A 1 118 ? -17.21800 -24.73000 14.83900 1.000 25.05176 ?  98  TYR   A C     1 
ATOM   687  O O     . TYR   A 1 118 ? -16.91700 -25.81600 14.35300 1.000 24.02165 ?  98  TYR   A O     1 
ATOM   688  C CB    . TYR   A 1 118 ? -16.49300 -23.77700 17.08600 1.000 23.59751 ?  98  TYR   A CB    1 
ATOM   689  C CG    . TYR   A 1 118 ? -15.06800 -24.23100 16.86900 1.000 20.42642 ?  98  TYR   A CG    1 
ATOM   690  C CD1   . TYR   A 1 118 ? -14.50200 -25.21200 17.67300 1.000 23.69639 ?  98  TYR   A CD1   1 
ATOM   691  C CD2   . TYR   A 1 118 ? -14.28500 -23.66400 15.87000 1.000 25.94782 ?  98  TYR   A CD2   1 
ATOM   692  C CE1   . TYR   A 1 118 ? -13.17700 -25.62100 17.48900 1.000 25.21026 ?  98  TYR   A CE1   1 
ATOM   693  C CE2   . TYR   A 1 118 ? -12.98500 -24.06300 15.67200 1.000 26.45773 ?  98  TYR   A CE2   1 
ATOM   694  C CZ    . TYR   A 1 118 ? -12.43200 -25.02700 16.47700 1.000 27.24574 ?  98  TYR   A CZ    1 
ATOM   695  O OH    . TYR   A 1 118 ? -11.12800 -25.40100 16.26700 1.000 36.00549 ?  98  TYR   A OH    1 
ATOM   696  N N     . SER   A 1 119 ? -17.24200 -23.60000 14.12200 1.000 24.31881 ?  99  SER   A N     1 
ATOM   697  C CA    . SER   A 1 119 ? -16.97000 -23.59600 12.68400 1.000 26.84460 ?  99  SER   A CA    1 
ATOM   698  C C     . SER   A 1 119 ? -15.67100 -22.86300 12.38100 1.000 31.38320 ?  99  SER   A C     1 
ATOM   699  O O     . SER   A 1 119 ? -15.46800 -21.73800 12.84100 1.000 30.82874 ?  99  SER   A O     1 
ATOM   700  C CB    . SER   A 1 119 ? -18.10400 -22.92400 11.90500 1.000 32.38644 ?  99  SER   A CB    1 
ATOM   701  O OG    . SER   A 1 119 ? -19.29200 -23.66100 12.01800 1.000 42.07920 ?  99  SER   A OG    1 
ATOM   702  N N     . GLN   A 1 120 ? -14.80500 -23.49600 11.60200 1.000 27.06574 ?  100 GLN   A N     1 
ATOM   703  C CA    . GLN   A 1 120 ? -13.66300 -22.82400 11.00000 1.000 32.60701 ?  100 GLN   A CA    1 
ATOM   704  C C     . GLN   A 1 120 ? -14.06900 -22.28100 9.63600  1.000 38.23667 ?  100 GLN   A C     1 
ATOM   705  O O     . GLN   A 1 120 ? -14.86800 -22.88900 8.92400  1.000 30.87444 ?  100 GLN   A O     1 
ATOM   706  C CB    . GLN   A 1 120 ? -12.51900 -23.80100 10.81800 1.000 35.69621 ?  100 GLN   A CB    1 
ATOM   707  C CG    . GLN   A 1 120 ? -11.72100 -24.04300 12.04000 1.000 34.42395 ?  100 GLN   A CG    1 
ATOM   708  C CD    . GLN   A 1 120 ? -10.49800 -24.86400 11.74100 1.000 43.11414 ?  100 GLN   A CD    1 
ATOM   709  O OE1   . GLN   A 1 120 ? -10.53900 -25.78500 10.91500 1.000 39.25539 ?  100 GLN   A OE1   1 
ATOM   710  N NE2   . GLN   A 1 120 ? -9.40000  -24.54600 12.40800 1.000 36.27728 ?  100 GLN   A NE2   1 
ATOM   711  N N     . ASN   A 1 121 ? -13.50100 -21.14300 9.26100  1.000 27.34273 ?  101 ASN   A N     1 
ATOM   712  C CA    . ASN   A 1 121 ? -13.79100 -20.53500 7.97200  1.000 29.24771 ?  101 ASN   A CA    1 
ATOM   713  C C     . ASN   A 1 121 ? -12.73900 -20.91500 6.94500  1.000 32.07804 ?  101 ASN   A C     1 
ATOM   714  O O     . ASN   A 1 121 ? -11.54300 -20.90600 7.24600  1.000 33.36936 ?  101 ASN   A O     1 
ATOM   715  C CB    . ASN   A 1 121 ? -13.85300 -19.01100 8.09400  1.000 27.27913 ?  101 ASN   A CB    1 
ATOM   716  C CG    . ASN   A 1 121 ? -14.78600 -18.56400 9.15900  1.000 43.86198 ?  101 ASN   A CG    1 
ATOM   717  O OD1   . ASN   A 1 121 ? -15.94000 -18.98800 9.18200  1.000 42.47655 ?  101 ASN   A OD1   1 
ATOM   718  N ND2   . ASN   A 1 121 ? -14.31600 -17.68400 10.04700 1.000 43.32573 ?  101 ASN   A ND2   1 
ATOM   719  N N     . GLY   A 1 122 ? -13.19600 -21.26600 5.73600  1.000 30.07376 ?  102 GLY   A N     1 
ATOM   720  C CA    . GLY   A 1 122 ? -12.32300 -21.45600 4.58700  1.000 30.95093 ?  102 GLY   A CA    1 
ATOM   721  C C     . GLY   A 1 122 ? -12.42700 -20.30700 3.60200  1.000 39.17238 ?  102 GLY   A C     1 
ATOM   722  O O     . GLY   A 1 122 ? -12.52300 -19.14500 4.00700  1.000 31.53057 ?  102 GLY   A O     1 
ATOM   723  N N     . GLU   A 1 123 ? -12.41000 -20.61100 2.30400  1.000 26.41162 ?  103 GLU   A N     1 
ATOM   724  C CA    . GLU   A 1 123 ? -12.56900 -19.58100 1.29300  1.000 28.24703 ?  103 GLU   A CA    1 
ATOM   725  C C     . GLU   A 1 123 ? -13.97700 -19.04700 1.34700  1.000 32.04431 ?  103 GLU   A C     1 
ATOM   726  O O     . GLU   A 1 123 ? -14.93500 -19.81500 1.48300  1.000 26.58428 ?  103 GLU   A O     1 
ATOM   727  C CB    . GLU   A 1 123 ? -12.33100 -20.15400 -0.10500 1.000 24.65970 ?  103 GLU   A CB    1 
ATOM   728  C CG    . GLU   A 1 123 ? -10.94400 -20.64400 -0.32200 1.000 26.67479 ?  103 GLU   A CG    1 
ATOM   729  C CD    . GLU   A 1 123 ? -10.80500 -21.31200 -1.65100 1.000 25.21163 ?  103 GLU   A CD    1 
ATOM   730  O OE1   . GLU   A 1 123 ? -11.66700 -21.07400 -2.54200 1.000 25.70100 ?  103 GLU   A OE1   1 
ATOM   731  O OE2   . GLU   A 1 123 ? -9.83900  -22.09300 -1.79600 1.000 26.61386 -1 103 GLU   A OE2   1 
ATOM   732  N N     . GLY   A 1 124 ? -14.10100 -17.73200 1.21200  1.000 25.84039 ?  104 GLY   A N     1 
ATOM   733  C CA    . GLY   A 1 124 ? -15.42800 -17.15700 1.07000  1.000 30.76062 ?  104 GLY   A CA    1 
ATOM   734  C C     . GLY   A 1 124 ? -16.28600 -17.52600 2.26300  1.000 26.01907 ?  104 GLY   A C     1 
ATOM   735  O O     . GLY   A 1 124 ? -15.92100 -17.28500 3.41700  1.000 38.77098 ?  104 GLY   A O     1 
ATOM   736  N N     . GLU   A 1 125 ? -17.44100 -18.11400 1.98100  1.000 30.51391 ?  105 GLU   A N     1 
ATOM   737  C CA    . GLU   A 1 125 ? -18.40400 -18.45400 3.01100  1.000 36.51078 ?  105 GLU   A CA    1 
ATOM   738  C C     . GLU   A 1 125 ? -18.25300 -19.88800 3.51400  1.000 34.02327 ?  105 GLU   A C     1 
ATOM   739  O O     . GLU   A 1 125 ? -19.09000 -20.33000 4.30700  1.000 35.22849 ?  105 GLU   A O     1 
ATOM   740  C CB    . GLU   A 1 125 ? -19.82400 -18.25800 2.48300  1.000 29.33841 ?  105 GLU   A CB    1 
ATOM   741  C CG    . GLU   A 1 125 ? -20.17500 -19.27800 1.38400  1.000 38.04756 ?  105 GLU   A CG    1 
ATOM   742  C CD    . GLU   A 1 125 ? -21.63500 -19.22400 0.97000  1.000 42.33929 ?  105 GLU   A CD    1 
ATOM   743  O OE1   . GLU   A 1 125 ? -22.30900 -18.26400 1.39200  1.000 50.36766 ?  105 GLU   A OE1   1 
ATOM   744  O OE2   . GLU   A 1 125 ? -22.08600 -20.09700 0.18500  1.000 39.92548 -1 105 GLU   A OE2   1 
ATOM   745  N N     . LEU   A 1 126 ? -17.23000 -20.62400 3.06800  1.000 26.75873 ?  106 LEU   A N     1 
ATOM   746  C CA    . LEU   A 1 126 ? -17.13100 -22.05000 3.38200  1.000 26.26790 ?  106 LEU   A CA    1 
ATOM   747  C C     . LEU   A 1 126 ? -16.69300 -22.26100 4.82800  1.000 28.03246 ?  106 LEU   A C     1 
ATOM   748  O O     . LEU   A 1 126 ? -15.88900 -21.50400 5.37300  1.000 26.25454 ?  106 LEU   A O     1 
ATOM   749  C CB    . LEU   A 1 126 ? -16.14200 -22.74000 2.44600  1.000 27.76071 ?  106 LEU   A CB    1 
ATOM   750  C CG    . LEU   A 1 126 ? -16.54000 -22.74800 0.96700  1.000 33.71508 ?  106 LEU   A CG    1 
ATOM   751  C CD1   . LEU   A 1 126 ? -15.58200 -23.62100 0.18600  1.000 32.76874 ?  106 LEU   A CD1   1 
ATOM   752  C CD2   . LEU   A 1 126 ? -18.00500 -23.21200 0.76700  1.000 25.76408 ?  106 LEU   A CD2   1 
ATOM   753  N N     . LYS   A 1 127 ? -17.22300 -23.31400 5.45400  1.000 28.25151 ?  107 LYS   A N     1 
ATOM   754  C CA    . LYS   A 1 127 ? -16.95000 -23.54900 6.86700  1.000 27.34342 ?  107 LYS   A CA    1 
ATOM   755  C C     . LYS   A 1 127 ? -16.67300 -25.02700 7.09400  1.000 36.54855 ?  107 LYS   A C     1 
ATOM   756  O O     . LYS   A 1 127 ? -17.11100 -25.87700 6.31500  1.000 35.74333 ?  107 LYS   A O     1 
ATOM   757  C CB    . LYS   A 1 127 ? -18.10300 -23.08500 7.77300  1.000 30.44837 ?  107 LYS   A CB    1 
ATOM   758  C CG    . LYS   A 1 127 ? -18.60800 -21.67400 7.47800  1.000 36.25325 ?  107 LYS   A CG    1 
ATOM   759  C CD    . LYS   A 1 127 ? -18.60900 -20.79100 8.69000  1.000 40.88553 ?  107 LYS   A CD    1 
ATOM   760  C CE    . LYS   A 1 127 ? -19.16500 -19.41300 8.35500  1.000 45.33228 ?  107 LYS   A CE    1 
ATOM   761  N N     . ASN   A 1 128 ? -15.89800 -25.32400 8.13700  1.000 28.00631 ?  108 ASN   A N     1 
ATOM   762  C CA    . ASN   A 1 128 ? -15.61200 -26.70500 8.53600  1.000 31.37963 ?  108 ASN   A CA    1 
ATOM   763  C C     . ASN   A 1 128 ? -15.98100 -26.88100 10.00500 1.000 40.37457 ?  108 ASN   A C     1 
ATOM   764  O O     . ASN   A 1 128 ? -15.62700 -26.04400 10.84000 1.000 31.72093 ?  108 ASN   A O     1 
ATOM   765  C CB    . ASN   A 1 128 ? -14.12900 -27.05500 8.33300  1.000 38.74759 ?  108 ASN   A CB    1 
ATOM   766  C CG    . ASN   A 1 128 ? -13.30200 -25.87300 7.84200  1.000 46.08276 ?  108 ASN   A CG    1 
ATOM   767  N N     . TYR   A 1 129 ? -16.68300 -27.96600 10.32300 1.000 28.83215 ?  109 TYR   A N     1 
ATOM   768  C CA    . TYR   A 1 129 ? -17.10300 -28.21500 11.69900 1.000 31.74732 ?  109 TYR   A CA    1 
ATOM   769  C C     . TYR   A 1 129 ? -15.98000 -28.86500 12.49900 1.000 33.16276 ?  109 TYR   A C     1 
ATOM   770  O O     . TYR   A 1 129 ? -15.36600 -29.83000 12.03900 1.000 28.00219 ?  109 TYR   A O     1 
ATOM   771  C CB    . TYR   A 1 129 ? -18.34000 -29.10900 11.70200 1.000 38.40780 ?  109 TYR   A CB    1 
ATOM   772  C CG    . TYR   A 1 129 ? -18.85000 -29.43800 13.08100 1.000 33.89415 ?  109 TYR   A CG    1 
ATOM   773  C CD1   . TYR   A 1 129 ? -19.64800 -28.53200 13.77200 1.000 41.94218 ?  109 TYR   A CD1   1 
ATOM   774  C CD2   . TYR   A 1 129 ? -18.54200 -30.65900 13.69200 1.000 31.74984 ?  109 TYR   A CD2   1 
ATOM   775  C CE1   . TYR   A 1 129 ? -20.12400 -28.81400 15.03600 1.000 39.12122 ?  109 TYR   A CE1   1 
ATOM   776  C CE2   . TYR   A 1 129 ? -19.02400 -30.95600 14.96700 1.000 36.57532 ?  109 TYR   A CE2   1 
ATOM   777  C CZ    . TYR   A 1 129 ? -19.81600 -30.02100 15.63000 1.000 38.35598 ?  109 TYR   A CZ    1 
ATOM   778  O OH    . TYR   A 1 129 ? -20.31200 -30.29100 16.89000 1.000 52.83070 ?  109 TYR   A OH    1 
ATOM   779  N N     . LYS   A 1 130 ? -15.72800 -28.35600 13.70900 1.000 23.04733 ?  110 LYS   A N     1 
ATOM   780  C CA    . LYS   A 1 130 ? -14.71100 -28.89900 14.61100 1.000 23.72411 ?  110 LYS   A CA    1 
ATOM   781  C C     . LYS   A 1 130 ? -15.31300 -29.09000 16.00800 1.000 21.64862 ?  110 LYS   A C     1 
ATOM   782  O O     . LYS   A 1 130 ? -16.27100 -28.42000 16.38800 1.000 24.21942 ?  110 LYS   A O     1 
ATOM   783  C CB    . LYS   A 1 130 ? -13.48800 -27.96800 14.71500 1.000 29.63128 ?  110 LYS   A CB    1 
ATOM   784  C CG    . LYS   A 1 130 ? -12.72500 -27.77500 13.40800 1.000 36.77942 ?  110 LYS   A CG    1 
ATOM   785  C CD    . LYS   A 1 130 ? -11.35900 -28.43800 13.46000 1.000 37.87190 ?  110 LYS   A CD    1 
ATOM   786  C CE    . LYS   A 1 130 ? -10.87800 -28.80800 12.07200 1.000 49.57104 ?  110 LYS   A CE    1 
ATOM   787  N N     . VAL   A 1 131 ? -14.74400 -30.00600 16.78500 1.000 21.48950 ?  111 VAL   A N     1 
ATOM   788  C CA    . VAL   A 1 131 ? -15.23100 -30.25400 18.13900 1.000 21.54371 ?  111 VAL   A CA    1 
ATOM   789  C C     . VAL   A 1 131 ? -14.11300 -30.02400 19.13400 1.000 24.03160 ?  111 VAL   A C     1 
ATOM   790  O O     . VAL   A 1 131 ? -12.97100 -30.44200 18.91600 1.000 26.85662 ?  111 VAL   A O     1 
ATOM   791  C CB    . VAL   A 1 131 ? -15.79700 -31.67800 18.31200 1.000 35.75881 ?  111 VAL   A CB    1 
ATOM   792  C CG1   . VAL   A 1 131 ? -16.60600 -31.74000 19.59600 1.000 32.84554 ?  111 VAL   A CG1   1 
ATOM   793  C CG2   . VAL   A 1 131 ? -16.67200 -32.02800 17.15000 1.000 33.82098 ?  111 VAL   A CG2   1 
ATOM   794  N N     . ILE   A 1 132 ? -14.44700 -29.36000 20.23400 1.000 20.02613 ?  112 ILE   A N     1 
ATOM   795  C CA    . ILE   A 1 132 ? -13.53600 -29.22900 21.35300 1.000 20.24439 ?  112 ILE   A CA    1 
ATOM   796  C C     . ILE   A 1 132 ? -13.98400 -30.21400 22.42100 1.000 20.88196 ?  112 ILE   A C     1 
ATOM   797  O O     . ILE   A 1 132 ? -15.10600 -30.10300 22.92900 1.000 22.11379 ?  112 ILE   A O     1 
ATOM   798  C CB    . ILE   A 1 132 ? -13.52500 -27.79600 21.91000 1.000 18.06913 ?  112 ILE   A CB    1 
ATOM   799  C CG1   . ILE   A 1 132 ? -13.02300 -26.82400 20.82500 1.000 18.30933 ?  112 ILE   A CG1   1 
ATOM   800  C CG2   . ILE   A 1 132 ? -12.69500 -27.76500 23.20000 1.000 19.40737 ?  112 ILE   A CG2   1 
ATOM   801  C CD1   . ILE   A 1 132 ? -13.42700 -25.36700 21.08900 1.000 22.23512 ?  112 ILE   A CD1   1 
ATOM   802  N N     . ASP   A 1 133 ? -13.12000 -31.17800 22.76500 1.000 21.66392 ?  113 ASP   A N     1 
ATOM   803  C CA    . ASP   A 1 133 ? -13.41200 -32.17400 23.80200 1.000 20.59321 ?  113 ASP   A CA    1 
ATOM   804  C C     . ASP   A 1 133 ? -12.64100 -31.82500 25.07700 1.000 20.33059 ?  113 ASP   A C     1 
ATOM   805  O O     . ASP   A 1 133 ? -11.40700 -31.85100 25.08300 1.000 24.64102 ?  113 ASP   A O     1 
ATOM   806  C CB    . ASP   A 1 133 ? -13.02700 -33.56500 23.29400 1.000 24.39381 ?  113 ASP   A CB    1 
ATOM   807  C CG    . ASP   A 1 133 ? -13.16400 -34.65200 24.35000 1.000 34.07446 ?  113 ASP   A CG    1 
ATOM   808  O OD1   . ASP   A 1 133 ? -13.65100 -34.39300 25.46600 1.000 32.42633 ?  113 ASP   A OD1   1 
ATOM   809  O OD2   . ASP   A 1 133 ? -12.76300 -35.79800 24.03600 1.000 45.55495 -1 113 ASP   A OD2   1 
ATOM   810  N N     . ARG   A 1 134 ? -13.37300 -31.47100 26.14100 1.000 21.18117 ?  114 ARG   A N     1 
ATOM   811  C CA    . ARG   A 1 134 ? -12.75400 -31.11200 27.42900 1.000 21.67103 ?  114 ARG   A CA    1 
ATOM   812  C C     . ARG   A 1 134 ? -11.70100 -32.13600 27.86400 1.000 24.30313 ?  114 ARG   A C     1 
ATOM   813  O O     . ARG   A 1 134 ? -10.63200 -31.77600 28.38700 1.000 21.62171 ?  114 ARG   A O     1 
ATOM   814  C CB    . ARG   A 1 134 ? -13.84600 -31.00700 28.49700 1.000 23.85300 ?  114 ARG   A CB    1 
ATOM   815  C CG    . ARG   A 1 134 ? -13.37800 -30.58200 29.89700 1.000 25.28883 ?  114 ARG   A CG    1 
ATOM   816  C CD    . ARG   A 1 134 ? -14.50500 -30.73000 30.90100 1.000 25.73977 ?  114 ARG   A CD    1 
ATOM   817  N NE    . ARG   A 1 134 ? -14.83200 -32.15100 31.06700 1.000 25.32564 ?  114 ARG   A NE    1 
ATOM   818  C CZ    . ARG   A 1 134 ? -16.01100 -32.60600 31.45800 1.000 28.03538 ?  114 ARG   A CZ    1 
ATOM   819  N NH1   . ARG   A 1 134 ? -17.03000 -31.78700 31.68200 1.000 24.55037 ?  114 ARG   A NH1   1 
ATOM   820  N NH2   . ARG   A 1 134 ? -16.17300 -33.91800 31.63100 1.000 29.06524 ?  114 ARG   A NH2   1 
ATOM   821  N N     . GLU   A 1 135 ? -12.00000 -33.41800 27.66100 1.000 23.12117 ?  115 GLU   A N     1 
ATOM   822  C CA    . GLU   A 1 135 ? -11.13500 -34.50300 28.11100 1.000 26.11798 ?  115 GLU   A CA    1 
ATOM   823  C C     . GLU   A 1 135 ? -9.87800  -34.65800 27.26700 1.000 26.93122 ?  115 GLU   A C     1 
ATOM   824  O O     . GLU   A 1 135 ? -9.05100  -35.52700 27.57000 1.000 27.94290 ?  115 GLU   A O     1 
ATOM   825  C CB    . GLU   A 1 135 ? -11.96300 -35.79500 28.11900 1.000 26.16341 ?  115 GLU   A CB    1 
ATOM   826  C CG    . GLU   A 1 135 ? -13.12400 -35.72600 29.12700 1.000 29.80264 ?  115 GLU   A CG    1 
ATOM   827  C CD    . GLU   A 1 135 ? -12.65300 -35.44500 30.55200 1.000 39.05823 ?  115 GLU   A CD    1 
ATOM   828  O OE1   . GLU   A 1 135 ? -11.71300 -36.12700 31.01800 1.000 37.68336 ?  115 GLU   A OE1   1 
ATOM   829  O OE2   . GLU   A 1 135 ? -13.24000 -34.57200 31.23400 1.000 30.92727 -1 115 GLU   A OE2   1 
ATOM   830  N N     . GLY   A 1 136 ? -9.70300  -33.84300 26.22300 1.000 22.78993 ?  116 GLY   A N     1 
ATOM   831  C CA    . GLY   A 1 136 ? -8.48000  -33.86300 25.45200 1.000 24.64924 ?  116 GLY   A CA    1 
ATOM   832  C C     . GLY   A 1 136 ? -7.40400  -32.90400 25.91800 1.000 21.49243 ?  116 GLY   A C     1 
ATOM   833  O O     . GLY   A 1 136 ? -6.33900  -32.82700 25.28800 1.000 23.85956 ?  116 GLY   A O     1 
ATOM   834  N N     . TYR   A 1 137 ? -7.63700  -32.15100 27.00000 1.000 21.07082 ?  117 TYR   A N     1 
ATOM   835  C CA    . TYR   A 1 137 ? -6.68900  -31.16200 27.49100 1.000 18.46279 ?  117 TYR   A CA    1 
ATOM   836  C C     . TYR   A 1 137 ? -6.25600  -31.48400 28.91500 1.000 18.35872 ?  117 TYR   A C     1 
ATOM   837  O O     . TYR   A 1 137 ? -7.03600  -32.00400 29.71700 1.000 22.36806 ?  117 TYR   A O     1 
ATOM   838  C CB    . TYR   A 1 137 ? -7.31400  -29.73200 27.47500 1.000 17.67387 ?  117 TYR   A CB    1 
ATOM   839  C CG    . TYR   A 1 137 ? -7.76600  -29.31200 26.11000 1.000 19.25461 ?  117 TYR   A CG    1 
ATOM   840  C CD1   . TYR   A 1 137 ? -9.00100  -29.73900 25.60800 1.000 18.98437 ?  117 TYR   A CD1   1 
ATOM   841  C CD2   . TYR   A 1 137 ? -6.98100  -28.47400 25.31100 1.000 21.79613 ?  117 TYR   A CD2   1 
ATOM   842  C CE1   . TYR   A 1 137 ? -9.41900  -29.38800 24.32600 1.000 20.97283 ?  117 TYR   A CE1   1 
ATOM   843  C CE2   . TYR   A 1 137 ? -7.40500  -28.09800 24.04600 1.000 19.16465 ?  117 TYR   A CE2   1 
ATOM   844  C CZ    . TYR   A 1 137 ? -8.62600  -28.55600 23.55600 1.000 24.40307 ?  117 TYR   A CZ    1 
ATOM   845  O OH    . TYR   A 1 137 ? -9.06400  -28.19100 22.27900 1.000 24.40756 ?  117 TYR   A OH    1 
ATOM   846  N N     . ALA   A 1 138 ? -5.02600  -31.10800 29.25100 1.000 20.05880 ?  118 ALA   A N     1 
ATOM   847  C CA    . ALA   A 1 138 ? -4.54400  -31.32400 30.61400 1.000 24.95478 ?  118 ALA   A CA    1 
ATOM   848  C C     . ALA   A 1 138 ? -5.39700  -30.58500 31.64600 1.000 28.42735 ?  118 ALA   A C     1 
ATOM   849  O O     . ALA   A 1 138 ? -5.54100  -31.06200 32.77700 1.000 23.08086 ?  118 ALA   A O     1 
ATOM   850  C CB    . ALA   A 1 138 ? -3.08300  -30.89600 30.73700 1.000 22.03142 ?  118 ALA   A CB    1 
ATOM   851  N N     . PHE   A 1 139 ? -6.00200  -29.44200 31.28100 1.000 22.28399 ?  119 PHE   A N     1 
ATOM   852  C CA    . PHE   A 1 139 ? -6.81000  -28.74300 32.28100 1.000 17.56449 ?  119 PHE   A CA    1 
ATOM   853  C C     . PHE   A 1 139 ? -8.03400  -29.55100 32.72100 1.000 19.22029 ?  119 PHE   A C     1 
ATOM   854  O O     . PHE   A 1 139 ? -8.73200  -29.13400 33.65200 1.000 22.33108 ?  119 PHE   A O     1 
ATOM   855  C CB    . PHE   A 1 139 ? -7.21000  -27.34400 31.74800 1.000 18.91041 ?  119 PHE   A CB    1 
ATOM   856  C CG    . PHE   A 1 139 ? -8.21500  -27.33500 30.59400 1.000 19.62319 ?  119 PHE   A CG    1 
ATOM   857  C CD1   . PHE   A 1 139 ? -9.53700  -27.70200 30.77200 1.000 18.90681 ?  119 PHE   A CD1   1 
ATOM   858  C CD2   . PHE   A 1 139 ? -7.82300  -26.90200 29.33200 1.000 20.84676 ?  119 PHE   A CD2   1 
ATOM   859  C CE1   . PHE   A 1 139 ? -10.44800 -27.64000 29.72200 1.000 25.12739 ?  119 PHE   A CE1   1 
ATOM   860  C CE2   . PHE   A 1 139 ? -8.73500  -26.85700 28.26300 1.000 18.89637 ?  119 PHE   A CE2   1 
ATOM   861  C CZ    . PHE   A 1 139 ? -10.03900 -27.24100 28.45900 1.000 21.39957 ?  119 PHE   A CZ    1 
ATOM   862  N N     . ARG   A 1 140 ? -8.30500  -30.69900 32.08900 1.000 21.94129 ?  120 ARG   A N     1 
ATOM   863  C CA    . ARG   A 1 140 ? -9.42900  -31.52400 32.51700 1.000 19.11053 ?  120 ARG   A CA    1 
ATOM   864  C C     . ARG   A 1 140 ? -9.30300  -31.95500 33.97300 1.000 21.07619 ?  120 ARG   A C     1 
ATOM   865  O O     . ARG   A 1 140 ? -10.29800 -32.39200 34.56100 1.000 25.34679 ?  120 ARG   A O     1 
ATOM   866  C CB    . ARG   A 1 140 ? -9.56000  -32.76000 31.63000 1.000 22.61382 ?  120 ARG   A CB    1 
ATOM   867  C CG    . ARG   A 1 140 ? -8.43500  -33.77300 31.83100 1.000 21.91501 ?  120 ARG   A CG    1 
ATOM   868  C CD    . ARG   A 1 140 ? -8.61300  -34.89300 30.80100 1.000 25.43732 ?  120 ARG   A CD    1 
ATOM   869  N NE    . ARG   A 1 140 ? -7.44300  -35.74800 30.73000 1.000 29.64940 ?  120 ARG   A NE    1 
ATOM   870  C CZ    . ARG   A 1 140 ? -7.22300  -36.80200 31.50400 1.000 43.64334 ?  120 ARG   A CZ    1 
ATOM   871  N NH1   . ARG   A 1 140 ? -8.12900  -37.22700 32.37300 1.000 33.14020 ?  120 ARG   A NH1   1 
ATOM   872  N NH2   . ARG   A 1 140 ? -6.06300  -37.44900 31.39900 1.000 34.05112 ?  120 ARG   A NH2   1 
ATOM   873  N N     . ASP   A 1 141 ? -8.12400  -31.83600 34.57700 1.000 21.52160 ?  121 ASP   A N     1 
ATOM   874  C CA    . ASP   A 1 141 ? -8.00500  -32.24200 35.97400 1.000 25.99959 ?  121 ASP   A CA    1 
ATOM   875  C C     . ASP   A 1 141 ? -8.51200  -31.17600 36.93400 1.000 31.18772 ?  121 ASP   A C     1 
ATOM   876  O O     . ASP   A 1 141 ? -8.51700  -31.41500 38.13900 1.000 25.57965 ?  121 ASP   A O     1 
ATOM   877  C CB    . ASP   A 1 141 ? -6.55000  -32.59400 36.34100 1.000 23.30020 ?  121 ASP   A CB    1 
ATOM   878  C CG    . ASP   A 1 141 ? -5.56500  -31.41400 36.22500 1.000 34.34892 ?  121 ASP   A CG    1 
ATOM   879  O OD1   . ASP   A 1 141 ? -5.91600  -30.26800 35.81500 1.000 25.84970 ?  121 ASP   A OD1   1 
ATOM   880  O OD2   . ASP   A 1 141 ? -4.37800  -31.67000 36.52200 1.000 30.23006 -1 121 ASP   A OD2   1 
ATOM   881  N N     . SER   A 1 142 ? -8.94000  -30.00800 36.44200 1.000 23.34911 ?  122 SER   A N     1 
ATOM   882  C CA    . SER   A 1 142 ? -9.20800  -28.90400 37.36100 1.000 25.24716 ?  122 SER   A CA    1 
ATOM   883  C C     . SER   A 1 142 ? -10.46900 -28.10500 37.04500 1.000 25.91171 ?  122 SER   A C     1 
ATOM   884  O O     . SER   A 1 142 ? -10.71300 -27.08100 37.70400 1.000 24.59278 ?  122 SER   A O     1 
ATOM   885  C CB    . SER   A 1 142 ? -8.01700  -27.93400 37.40600 1.000 24.55071 ?  122 SER   A CB    1 
ATOM   886  O OG    . SER   A 1 142 ? -6.78400  -28.59900 37.59700 1.000 25.73976 ?  122 SER   A OG    1 
ATOM   887  N N     . PHE   A 1 143 ? -11.28600 -28.54000 36.09200 1.000 21.54713 ?  123 PHE   A N     1 
ATOM   888  C CA    . PHE   A 1 143 ? -12.32800 -27.65600 35.57400 1.000 21.83571 ?  123 PHE   A CA    1 
ATOM   889  C C     . PHE   A 1 143 ? -13.47800 -27.41000 36.54500 1.000 26.66291 ?  123 PHE   A C     1 
ATOM   890  O O     . PHE   A 1 143 ? -14.23400 -26.45700 36.33200 1.000 26.05948 ?  123 PHE   A O     1 
ATOM   891  C CB    . PHE   A 1 143 ? -12.84500 -28.21500 34.23900 1.000 23.73227 ?  123 PHE   A CB    1 
ATOM   892  C CG    . PHE   A 1 143 ? -13.62400 -29.51500 34.37500 1.000 28.27138 ?  123 PHE   A CG    1 
ATOM   893  C CD1   . PHE   A 1 143 ? -14.99600 -29.51400 34.58900 1.000 28.26126 ?  123 PHE   A CD1   1 
ATOM   894  C CD2   . PHE   A 1 143 ? -12.97100 -30.73700 34.30200 1.000 28.33139 ?  123 PHE   A CD2   1 
ATOM   895  C CE1   . PHE   A 1 143 ? -15.69900 -30.70300 34.73000 1.000 31.87533 ?  123 PHE   A CE1   1 
ATOM   896  C CE2   . PHE   A 1 143 ? -13.67600 -31.93300 34.44500 1.000 31.69532 ?  123 PHE   A CE2   1 
ATOM   897  C CZ    . PHE   A 1 143 ? -15.03500 -31.90900 34.65800 1.000 25.94158 ?  123 PHE   A CZ    1 
ATOM   898  N N     . THR   A 1 144 ? -13.63600 -28.20500 37.61100 1.000 22.45237 ?  124 THR   A N     1 
ATOM   899  C CA    . THR   A 1 144 ? -14.70200 -27.87500 38.54900 1.000 24.81577 ?  124 THR   A CA    1 
ATOM   900  C C     . THR   A 1 144 ? -14.31700 -26.73800 39.48800 1.000 29.05991 ?  124 THR   A C     1 
ATOM   901  O O     . THR   A 1 144 ? -15.17000 -26.29100 40.26000 1.000 27.90484 ?  124 THR   A O     1 
ATOM   902  C CB    . THR   A 1 144 ? -15.10900 -29.10200 39.38500 1.000 27.61494 ?  124 THR   A CB    1 
ATOM   903  O OG1   . THR   A 1 144 ? -13.98400 -29.55500 40.14600 1.000 30.06645 ?  124 THR   A OG1   1 
ATOM   904  C CG2   . THR   A 1 144 ? -15.59700 -30.22600 38.46100 1.000 29.81280 ?  124 THR   A CG2   1 
ATOM   905  N N     . LYS   A 1 145 ? -13.05800 -26.26900 39.44900 1.000 22.63849 ?  125 LYS   A N     1 
ATOM   906  C CA    . LYS   A 1 145 ? -12.60400 -25.16300 40.27800 1.000 22.17060 ?  125 LYS   A CA    1 
ATOM   907  C C     . LYS   A 1 145 ? -12.84700 -23.81000 39.62500 1.000 25.96145 ?  125 LYS   A C     1 
ATOM   908  O O     . LYS   A 1 145 ? -12.40700 -22.80100 40.17900 1.000 24.40414 ?  125 LYS   A O     1 
ATOM   909  C CB    . LYS   A 1 145 ? -11.11500 -25.30600 40.60800 1.000 23.11069 ?  125 LYS   A CB    1 
ATOM   910  C CG    . LYS   A 1 145 ? -10.81200 -26.60600 41.38800 1.000 29.88297 ?  125 LYS   A CG    1 
ATOM   911  C CD    . LYS   A 1 145 ? -9.44700  -26.56200 42.06800 1.000 34.54872 ?  125 LYS   A CD    1 
ATOM   912  C CE    . LYS   A 1 145 ? -8.37900  -27.08700 41.14300 1.000 30.83083 ?  125 LYS   A CE    1 
ATOM   913  N NZ    . LYS   A 1 145 ? -7.04600  -26.48700 41.46200 1.000 30.53023 ?  125 LYS   A NZ    1 
ATOM   914  N N     . VAL   A 1 146 ? -13.55200 -23.77800 38.48200 1.000 23.14529 ?  126 VAL   A N     1 
ATOM   915  C CA    . VAL   A 1 146 ? -13.86100 -22.54900 37.73800 1.000 21.07600 ?  126 VAL   A CA    1 
ATOM   916  C C     . VAL   A 1 146 ? -15.34600 -22.24100 37.84900 1.000 24.22522 ?  126 VAL   A C     1 
ATOM   917  O O     . VAL   A 1 146 ? -16.19200 -23.13700 37.77600 1.000 23.31116 ?  126 VAL   A O     1 
ATOM   918  C CB    . VAL   A 1 146 ? -13.46300 -22.65200 36.24100 1.000 18.79928 ?  126 VAL   A CB    1 
ATOM   919  C CG1   . VAL   A 1 146 ? -13.64200 -21.27400 35.55300 1.000 23.38907 ?  126 VAL   A CG1   1 
ATOM   920  C CG2   . VAL   A 1 146 ? -12.01800 -23.02000 36.10600 1.000 23.58162 ?  126 VAL   A CG2   1 
ATOM   921  N N     . GLU   A 1 147 ? -15.66700 -20.96100 37.97600 1.000 21.51965 ?  127 GLU   A N     1 
ATOM   922  C CA    . GLU   A 1 147 ? -17.03500 -20.49900 37.81400 1.000 24.15080 ?  127 GLU   A CA    1 
ATOM   923  C C     . GLU   A 1 147 ? -17.02900 -19.37700 36.78500 1.000 19.69550 ?  127 GLU   A C     1 
ATOM   924  O O     . GLU   A 1 147 ? -16.20500 -18.46500 36.88800 1.000 23.79477 ?  127 GLU   A O     1 
ATOM   925  C CB    . GLU   A 1 147 ? -17.58800 -20.00000 39.14700 1.000 28.45280 ?  127 GLU   A CB    1 
ATOM   926  C CG    . GLU   A 1 147 ? -18.59900 -20.93300 39.75700 1.000 43.91748 ?  127 GLU   A CG    1 
ATOM   927  C CD    . GLU   A 1 147 ? -19.40900 -20.24800 40.83800 1.000 56.11151 ?  127 GLU   A CD    1 
ATOM   928  O OE1   . GLU   A 1 147 ? -18.80800 -19.88600 41.87500 1.000 45.04880 ?  127 GLU   A OE1   1 
ATOM   929  O OE2   . GLU   A 1 147 ? -20.62700 -20.03800 40.62600 1.000 58.64077 -1 127 GLU   A OE2   1 
ATOM   930  N N     . PHE   A 1 148 ? -17.93200 -19.45200 35.80600 1.000 19.94555 ?  128 PHE   A N     1 
ATOM   931  C CA    . PHE   A 1 148 ? -18.02400 -18.45900 34.73500 1.000 22.49185 ?  128 PHE   A CA    1 
ATOM   932  C C     . PHE   A 1 148 ? -19.23300 -17.55900 34.96400 1.000 25.01016 ?  128 PHE   A C     1 
ATOM   933  O O     . PHE   A 1 148 ? -20.31400 -18.04600 35.30300 1.000 24.51520 ?  128 PHE   A O     1 
ATOM   934  C CB    . PHE   A 1 148 ? -18.14300 -19.14500 33.37200 1.000 22.33514 ?  128 PHE   A CB    1 
ATOM   935  C CG    . PHE   A 1 148 ? -16.88000 -19.83700 32.94700 1.000 22.39188 ?  128 PHE   A CG    1 
ATOM   936  C CD1   . PHE   A 1 148 ? -15.72700 -19.10600 32.66700 1.000 18.23463 ?  128 PHE   A CD1   1 
ATOM   937  C CD2   . PHE   A 1 148 ? -16.83100 -21.21400 32.88100 1.000 20.99794 ?  128 PHE   A CD2   1 
ATOM   938  C CE1   . PHE   A 1 148 ? -14.54600 -19.74700 32.28900 1.000 19.84394 ?  128 PHE   A CE1   1 
ATOM   939  C CE2   . PHE   A 1 148 ? -15.67500 -21.86200 32.49600 1.000 21.29085 ?  128 PHE   A CE2   1 
ATOM   940  C CZ    . PHE   A 1 148 ? -14.52700 -21.14500 32.21600 1.000 18.36880 ?  128 PHE   A CZ    1 
ATOM   941  N N     . PHE   A 1 149 ? -19.05400 -16.25200 34.75600 1.000 19.23651 ?  129 PHE   A N     1 
ATOM   942  C CA    . PHE   A 1 149 ? -20.10700 -15.26300 34.98100 1.000 19.37092 ?  129 PHE   A CA    1 
ATOM   943  C C     . PHE   A 1 149 ? -20.09600 -14.22700 33.87500 1.000 21.69969 ?  129 PHE   A C     1 
ATOM   944  O O     . PHE   A 1 149 ? -19.02800 -13.82600 33.40800 1.000 22.14453 ?  129 PHE   A O     1 
ATOM   945  C CB    . PHE   A 1 149 ? -19.93500 -14.47300 36.28900 1.000 21.75859 ?  129 PHE   A CB    1 
ATOM   946  C CG    . PHE   A 1 149 ? -19.81200 -15.32100 37.51500 1.000 24.41374 ?  129 PHE   A CG    1 
ATOM   947  C CD1   . PHE   A 1 149 ? -18.59000 -15.85100 37.89300 1.000 23.62496 ?  129 PHE   A CD1   1 
ATOM   948  C CD2   . PHE   A 1 149 ? -20.91700 -15.53700 38.32000 1.000 26.83078 ?  129 PHE   A CD2   1 
ATOM   949  C CE1   . PHE   A 1 149 ? -18.47100 -16.61600 39.03500 1.000 29.02787 ?  129 PHE   A CE1   1 
ATOM   950  C CE2   . PHE   A 1 149 ? -20.79500 -16.30300 39.47700 1.000 31.50484 ?  129 PHE   A CE2   1 
ATOM   951  C CZ    . PHE   A 1 149 ? -19.57600 -16.83800 39.82800 1.000 31.69138 ?  129 PHE   A CZ    1 
ATOM   952  N N     . GLN   A 1 150 ? -21.27600 -13.75800 33.49100 1.000 21.36730 ?  130 GLN   A N     1 
ATOM   953  C CA    . GLN   A 1 150 ? -21.35300 -12.53900 32.68600 1.000 21.79905 ?  130 GLN   A CA    1 
ATOM   954  C C     . GLN   A 1 150 ? -21.16200 -11.34800 33.62800 1.000 21.05050 ?  130 GLN   A C     1 
ATOM   955  O O     . GLN   A 1 150 ? -21.67900 -11.34300 34.74800 1.000 22.78960 ?  130 GLN   A O     1 
ATOM   956  C CB    . GLN   A 1 150 ? -22.69800 -12.45000 31.95900 1.000 22.97791 ?  130 GLN   A CB    1 
ATOM   957  C CG    . GLN   A 1 150 ? -22.76400 -11.38800 30.85800 1.000 22.75318 ?  130 GLN   A CG    1 
ATOM   958  C CD    . GLN   A 1 150 ? -23.09800 -10.01200 31.42300 1.000 29.94935 ?  130 GLN   A CD    1 
ATOM   959  O OE1   . GLN   A 1 150 ? -23.70100 -9.90700  32.49600 1.000 35.29345 ?  130 GLN   A OE1   1 
ATOM   960  N NE2   . GLN   A 1 150 ? -22.69000 -8.94700  30.71400 1.000 32.86038 ?  130 GLN   A NE2   1 
ATOM   961  N N     . GLY   A 1 151 ? -20.36500 -10.37000 33.20600 1.000 17.17552 ?  131 GLY   A N     1 
ATOM   962  C CA    . GLY   A 1 151 ? -20.09500 -9.21900  34.06400 1.000 23.51228 ?  131 GLY   A CA    1 
ATOM   963  C C     . GLY   A 1 151 ? -19.29900 -8.16500  33.32500 1.000 21.73022 ?  131 GLY   A C     1 
ATOM   964  O O     . GLY   A 1 151 ? -18.78800 -8.39700  32.22500 1.000 21.60112 ?  131 GLY   A O     1 
ATOM   965  N N     . ASP   A 1 152 ? -19.22300 -6.97100  33.94300 1.000 20.97340 ?  132 ASP   A N     1 
ATOM   966  C CA    . ASP   A 1 152 ? -18.59500 -5.78600  33.35900 1.000 22.06910 ?  132 ASP   A CA    1 
ATOM   967  C C     . ASP   A 1 152 ? -17.33500 -5.43800  34.14100 1.000 22.40053 ?  132 ASP   A C     1 
ATOM   968  O O     . ASP   A 1 152 ? -17.41200 -5.04300  35.31100 1.000 22.38816 ?  132 ASP   A O     1 
ATOM   969  C CB    . ASP   A 1 152 ? -19.60300 -4.63000  33.36700 1.000 22.93797 ?  132 ASP   A CB    1 
ATOM   970  C CG    . ASP   A 1 152 ? -19.05000 -3.34900  32.78500 1.000 26.93674 ?  132 ASP   A CG    1 
ATOM   971  O OD1   . ASP   A 1 152 ? -17.91500 -3.35900  32.26900 1.000 20.92109 ?  132 ASP   A OD1   1 
ATOM   972  O OD2   . ASP   A 1 152 ? -19.80300 -2.33200  32.82200 1.000 25.12013 -1 132 ASP   A OD2   1 
ATOM   973  N N     . ALA   A 1 153 ? -16.17500 -5.58400  33.48800 1.000 20.06545 ?  133 ALA   A N     1 
ATOM   974  C CA    . ALA   A 1 153 ? -14.89500 -5.25600  34.11700 1.000 21.96878 ?  133 ALA   A CA    1 
ATOM   975  C C     . ALA   A 1 153 ? -14.84600 -3.81100  34.60500 1.000 22.35033 ?  133 ALA   A C     1 
ATOM   976  O O     . ALA   A 1 153 ? -14.08900 -3.48900  35.52600 1.000 22.88864 ?  133 ALA   A O     1 
ATOM   977  C CB    . ALA   A 1 153 ? -13.74800 -5.50600  33.13000 1.000 22.79964 ?  133 ALA   A CB    1 
ATOM   978  N N     . CYS   A 1 154 ? -15.58900 -2.92300  33.95600 1.000 22.32397 ?  134 CYS   A N     1 
ATOM   979  C CA    . CYS   A 1 154 ? -15.59800 -1.51600  34.33800 1.000 23.20051 ?  134 CYS   A CA    1 
ATOM   980  C C     . CYS   A 1 154 ? -16.51800 -1.24700  35.52200 1.000 26.29201 ?  134 CYS   A C     1 
ATOM   981  O O     . CYS   A 1 154 ? -16.51800 -0.12600  36.03600 1.000 27.36641 ?  134 CYS   A O     1 
ATOM   982  C CB    . CYS   A 1 154 ? -16.04800 -0.67600  33.14900 1.000 19.50820 ?  134 CYS   A CB    1 
ATOM   983  S SG    . CYS   A 1 154 ? -14.84700 -0.62300  31.78300 1.000 24.58534 ?  134 CYS   A SG    1 
ATOM   984  N N     . ASN   A 1 155 ? -17.28200 -2.24700  35.96400 1.000 24.38367 ?  135 ASN   A N     1 
ATOM   985  C CA    . ASN   A 1 155 ? -18.20700 -2.10500  37.09200 1.000 24.92582 ?  135 ASN   A CA    1 
ATOM   986  C C     . ASN   A 1 155 ? -18.57800 -3.47800  37.65600 1.000 25.31463 ?  135 ASN   A C     1 
ATOM   987  O O     . ASN   A 1 155 ? -19.72100 -3.91500  37.55900 1.000 23.64331 ?  135 ASN   A O     1 
ATOM   988  C CB    . ASN   A 1 155 ? -19.43600 -1.31000  36.64900 1.000 21.64205 ?  135 ASN   A CB    1 
ATOM   989  C CG    . ASN   A 1 155 ? -20.14800 -0.62000  37.81900 1.000 27.01492 ?  135 ASN   A CG    1 
ATOM   990  O OD1   . ASN   A 1 155 ? -19.74300 -0.76700  38.98000 1.000 22.79127 ?  135 ASN   A OD1   1 
ATOM   991  N ND2   . ASN   A 1 155 ? -21.21900 0.11100   37.51200 1.000 22.90836 ?  135 ASN   A ND2   1 
ATOM   992  N N     . LEU   A 1 156 ? -17.60300 -4.15800  38.25100 1.000 22.87341 ?  136 LEU   A N     1 
ATOM   993  C CA    . LEU   A 1 156 ? -17.80400 -5.50600  38.76600 1.000 24.10690 ?  136 LEU   A CA    1 
ATOM   994  C C     . LEU   A 1 156 ? -18.65600 -5.46300  40.03100 1.000 25.19042 ?  136 LEU   A C     1 
ATOM   995  O O     . LEU   A 1 156 ? -18.51000 -4.55500  40.85300 1.000 25.73150 ?  136 LEU   A O     1 
ATOM   996  C CB    . LEU   A 1 156 ? -16.45100 -6.12900  39.09700 1.000 23.84719 ?  136 LEU   A CB    1 
ATOM   997  C CG    . LEU   A 1 156 ? -15.55400 -6.58200  37.94200 1.000 28.87927 ?  136 LEU   A CG    1 
ATOM   998  C CD1   . LEU   A 1 156 ? -14.15800 -6.96000  38.47500 1.000 27.07540 ?  136 LEU   A CD1   1 
ATOM   999  C CD2   . LEU   A 1 156 ? -16.20100 -7.73200  37.16300 1.000 24.19788 ?  136 LEU   A CD2   1 
ATOM   1000 N N     . THR   A 1 157 ? -19.51900 -6.46700  40.21100 1.000 26.15423 ?  137 THR   A N     1 
ATOM   1001 C CA    . THR   A 1 157 ? -20.28600 -6.54500  41.44700 1.000 24.64166 ?  137 THR   A CA    1 
ATOM   1002 C C     . THR   A 1 157 ? -19.35200 -6.81600  42.62900 1.000 26.97988 ?  137 THR   A C     1 
ATOM   1003 O O     . THR   A 1 157 ? -18.22000 -7.29300  42.45200 1.000 26.89108 ?  137 THR   A O     1 
ATOM   1004 C CB    . THR   A 1 157 ? -21.38700 -7.61400  41.35300 1.000 27.32721 ?  137 THR   A CB    1 
ATOM   1005 O OG1   . THR   A 1 157 ? -20.81100 -8.91800  41.12800 1.000 30.81739 ?  137 THR   A OG1   1 
ATOM   1006 C CG2   . THR   A 1 157 ? -22.35800 -7.27100  40.21500 1.000 32.69126 ?  137 THR   A CG2   1 
ATOM   1007 N N     . PRO   A 1 158 ? -19.80400 -6.51200  43.85400 1.000 33.52061 ?  138 PRO   A N     1 
ATOM   1008 C CA    . PRO   A 1 158 ? -18.88200 -6.52800  45.00900 1.000 34.18088 ?  138 PRO   A CA    1 
ATOM   1009 C C     . PRO   A 1 158 ? -18.30100 -7.88700  45.36200 1.000 27.62567 ?  138 PRO   A C     1 
ATOM   1010 O O     . PRO   A 1 158 ? -17.23900 -7.93500  46.00000 1.000 33.30578 ?  138 PRO   A O     1 
ATOM   1011 C CB    . PRO   A 1 158 ? -19.76400 -6.00600  46.15500 1.000 37.93337 ?  138 PRO   A CB    1 
ATOM   1012 C CG    . PRO   A 1 158 ? -20.78900 -5.18200  45.47900 1.000 46.68110 ?  138 PRO   A CG    1 
ATOM   1013 C CD    . PRO   A 1 158 ? -21.11600 -5.94800  44.23400 1.000 39.71038 ?  138 PRO   A CD    1 
ATOM   1014 N N     . GLN   A 1 159 ? -18.97200 -8.98700  45.00400 1.000 31.52606 ?  139 GLN   A N     1 
ATOM   1015 C CA    . GLN   A 1 159 ? -18.52500 -10.31300 45.42000 1.000 34.06328 ?  139 GLN   A CA    1 
ATOM   1016 C C     . GLN   A 1 159 ? -17.22400 -10.73200 44.74100 1.000 32.13536 ?  139 GLN   A C     1 
ATOM   1017 O O     . GLN   A 1 159 ? -16.57800 -11.68700 45.19100 1.000 33.09946 ?  139 GLN   A O     1 
ATOM   1018 C CB    . GLN   A 1 159 ? -19.61500 -11.34700 45.13500 1.000 34.95249 ?  139 GLN   A CB    1 
ATOM   1019 C CG    . GLN   A 1 159 ? -20.56000 -10.97300 43.99800 1.000 47.41133 ?  139 GLN   A CG    1 
ATOM   1020 N N     . PHE   A 1 160 ? -16.81900 -10.04000 43.67500 1.000 30.01522 ?  140 PHE   A N     1 
ATOM   1021 C CA    . PHE   A 1 160 ? -15.58000 -10.36200 42.96800 1.000 26.05061 ?  140 PHE   A CA    1 
ATOM   1022 C C     . PHE   A 1 160 ? -14.43700 -9.60300  43.62100 1.000 25.35999 ?  140 PHE   A C     1 
ATOM   1023 O O     . PHE   A 1 160 ? -14.02600 -8.52800  43.17700 1.000 24.89117 ?  140 PHE   A O     1 
ATOM   1024 C CB    . PHE   A 1 160 ? -15.71600 -10.03700 41.48800 1.000 25.04234 ?  140 PHE   A CB    1 
ATOM   1025 C CG    . PHE   A 1 160 ? -16.73700 -10.90000 40.79800 1.000 28.22723 ?  140 PHE   A CG    1 
ATOM   1026 C CD1   . PHE   A 1 160 ? -16.39000 -12.16400 40.35600 1.000 22.34258 ?  140 PHE   A CD1   1 
ATOM   1027 C CD2   . PHE   A 1 160 ? -18.05500 -10.50000 40.69500 1.000 42.81344 ?  140 PHE   A CD2   1 
ATOM   1028 C CE1   . PHE   A 1 160 ? -17.33100 -12.97000 39.73800 1.000 25.45996 ?  140 PHE   A CE1   1 
ATOM   1029 C CE2   . PHE   A 1 160 ? -19.00200 -11.31500 40.09400 1.000 41.64989 ?  140 PHE   A CE2   1 
ATOM   1030 C CZ    . PHE   A 1 160 ? -18.63500 -12.55200 39.61500 1.000 31.12350 ?  140 PHE   A CZ    1 
ATOM   1031 N N     . LYS   A 1 161 ? -13.92100 -10.18000 44.70900 1.000 24.89356 ?  141 LYS   A N     1 
ATOM   1032 C CA    . LYS   A 1 161 ? -12.90400 -9.50700  45.50000 1.000 29.03107 ?  141 LYS   A CA    1 
ATOM   1033 C C     . LYS   A 1 161 ? -11.98400 -10.55500 46.11300 1.000 29.20955 ?  141 LYS   A C     1 
ATOM   1034 O O     . LYS   A 1 161 ? -12.17500 -11.75900 45.93000 1.000 29.72739 ?  141 LYS   A O     1 
ATOM   1035 C CB    . LYS   A 1 161 ? -13.54500 -8.64400  46.59100 1.000 32.36370 ?  141 LYS   A CB    1 
ATOM   1036 C CG    . LYS   A 1 161 ? -14.46600 -9.44600  47.49000 1.000 35.30214 ?  141 LYS   A CG    1 
ATOM   1037 C CD    . LYS   A 1 161 ? -14.83300 -8.67200  48.76500 1.000 43.07967 ?  141 LYS   A CD    1 
ATOM   1038 C CE    . LYS   A 1 161 ? -15.74100 -9.50400  49.68000 1.000 41.38382 ?  141 LYS   A CE    1 
ATOM   1039 N N     . GLU   A 1 162 ? -10.97000 -10.08200 46.83500 1.000 26.56333 ?  142 GLU   A N     1 
ATOM   1040 C CA    . GLU   A 1 162 ? -10.06200 -10.95400 47.58000 1.000 29.08113 ?  142 GLU   A CA    1 
ATOM   1041 C C     . GLU   A 1 162 ? -9.35100  -11.94400 46.65100 1.000 33.68431 ?  142 GLU   A C     1 
ATOM   1042 O O     . GLU   A 1 162 ? -9.27900  -13.15000 46.90900 1.000 28.17345 ?  142 GLU   A O     1 
ATOM   1043 C CB    . GLU   A 1 162 ? -10.81200 -11.66800 48.71000 1.000 32.44416 ?  142 GLU   A CB    1 
ATOM   1044 C CG    . GLU   A 1 162 ? -11.29500 -10.67300 49.78500 1.000 35.19763 ?  142 GLU   A CG    1 
ATOM   1045 C CD    . GLU   A 1 162 ? -12.02700 -11.34300 50.94100 1.000 49.83542 ?  142 GLU   A CD    1 
ATOM   1046 O OE1   . GLU   A 1 162 ? -11.80600 -12.54600 51.18000 1.000 54.27657 ?  142 GLU   A OE1   1 
ATOM   1047 O OE2   . GLU   A 1 162 ? -12.84100 -10.66500 51.59800 1.000 56.14272 -1 142 GLU   A OE2   1 
ATOM   1048 N N     . TYR   A 1 163 ? -8.80900  -11.41500 45.55700 1.000 25.97146 ?  143 TYR   A N     1 
ATOM   1049 C CA    . TYR   A 1 163 ? -8.04600  -12.20900 44.61000 1.000 25.35436 ?  143 TYR   A CA    1 
ATOM   1050 C C     . TYR   A 1 163 ? -6.55500  -12.09000 44.88200 1.000 26.99543 ?  143 TYR   A C     1 
ATOM   1051 O O     . TYR   A 1 163 ? -6.04900  -11.00800 45.18600 1.000 26.60067 ?  143 TYR   A O     1 
ATOM   1052 C CB    . TYR   A 1 163 ? -8.34100  -11.76800 43.17300 1.000 24.25322 ?  143 TYR   A CB    1 
ATOM   1053 C CG    . TYR   A 1 163 ? -9.75500  -12.09300 42.76400 1.000 23.65566 ?  143 TYR   A CG    1 
ATOM   1054 C CD1   . TYR   A 1 163 ? -10.15600 -13.41600 42.57400 1.000 22.46027 ?  143 TYR   A CD1   1 
ATOM   1055 C CD2   . TYR   A 1 163 ? -10.69200 -11.08300 42.58700 1.000 23.23510 ?  143 TYR   A CD2   1 
ATOM   1056 C CE1   . TYR   A 1 163 ? -11.45500 -13.72600 42.20400 1.000 23.92536 ?  143 TYR   A CE1   1 
ATOM   1057 C CE2   . TYR   A 1 163 ? -11.99800 -11.38200 42.21500 1.000 23.54477 ?  143 TYR   A CE2   1 
ATOM   1058 C CZ    . TYR   A 1 163 ? -12.36600 -12.69900 42.03000 1.000 23.70367 ?  143 TYR   A CZ    1 
ATOM   1059 O OH    . TYR   A 1 163 ? -13.64900 -13.00400 41.66500 1.000 25.88333 ?  143 TYR   A OH    1 
ATOM   1060 N N     . ASP   A 1 164 ? -5.86300  -13.22600 44.79100 1.000 27.71228 ?  144 ASP   A N     1 
ATOM   1061 C CA    . ASP   A 1 164 ? -4.40700  -13.22900 44.77700 1.000 23.27212 ?  144 ASP   A CA    1 
ATOM   1062 C C     . ASP   A 1 164 ? -3.88000  -12.81300 43.41200 1.000 30.08794 ?  144 ASP   A C     1 
ATOM   1063 O O     . ASP   A 1 164 ? -2.78700  -12.24300 43.31200 1.000 26.66861 ?  144 ASP   A O     1 
ATOM   1064 C CB    . ASP   A 1 164 ? -3.88100  -14.61700 45.12900 1.000 28.35700 ?  144 ASP   A CB    1 
ATOM   1065 C CG    . ASP   A 1 164 ? -4.40600  -15.10200 46.46900 1.000 35.49098 ?  144 ASP   A CG    1 
ATOM   1066 O OD1   . ASP   A 1 164 ? -4.17400  -14.41500 47.47300 1.000 33.21132 ?  144 ASP   A OD1   1 
ATOM   1067 O OD2   . ASP   A 1 164 ? -5.08300  -16.14500 46.51100 1.000 33.63850 -1 144 ASP   A OD2   1 
ATOM   1068 N N     . LEU   A 1 165 ? -4.65400  -13.08200 42.36100 1.000 22.28152 ?  145 LEU   A N     1 
ATOM   1069 C CA    . LEU   A 1 165 ? -4.26400  -12.72800 41.00600 1.000 21.99469 ?  145 LEU   A CA    1 
ATOM   1070 C C     . LEU   A 1 165 ? -5.48900  -12.26400 40.23400 1.000 22.72809 ?  145 LEU   A C     1 
ATOM   1071 O O     . LEU   A 1 165 ? -6.52700  -12.92900 40.23700 1.000 21.87544 ?  145 LEU   A O     1 
ATOM   1072 C CB    . LEU   A 1 165 ? -3.60500  -13.92200 40.28800 1.000 23.74165 ?  145 LEU   A CB    1 
ATOM   1073 C CG    . LEU   A 1 165 ? -3.48500  -13.81300 38.76200 1.000 20.36885 ?  145 LEU   A CG    1 
ATOM   1074 C CD1   . LEU   A 1 165 ? -2.47600  -12.76300 38.35200 1.000 23.40882 ?  145 LEU   A CD1   1 
ATOM   1075 C CD2   . LEU   A 1 165 ? -3.13100  -15.16800 38.15000 1.000 22.12227 ?  145 LEU   A CD2   1 
ATOM   1076 N N     . ILE   A 1 166 ? -5.36500  -11.13700 39.55000 1.000 19.18903 ?  146 ILE   A N     1 
ATOM   1077 C CA    . ILE   A 1 166 ? -6.36000  -10.73700 38.56600 1.000 21.63092 ?  146 ILE   A CA    1 
ATOM   1078 C C     . ILE   A 1 166 ? -5.63300  -10.63600 37.24200 1.000 26.85317 ?  146 ILE   A C     1 
ATOM   1079 O O     . ILE   A 1 166 ? -4.64500  -9.89000  37.12500 1.000 21.62380 ?  146 ILE   A O     1 
ATOM   1080 C CB    . ILE   A 1 166 ? -7.03700  -9.40800  38.94000 1.000 23.23500 ?  146 ILE   A CB    1 
ATOM   1081 C CG1   . ILE   A 1 166 ? -7.87000  -9.58300  40.22500 1.000 21.70530 ?  146 ILE   A CG1   1 
ATOM   1082 C CG2   . ILE   A 1 166 ? -7.88700  -8.90800  37.76800 1.000 21.80547 ?  146 ILE   A CG2   1 
ATOM   1083 C CD1   . ILE   A 1 166 ? -8.79700  -8.38500  40.55400 1.000 22.72121 ?  146 ILE   A CD1   1 
ATOM   1084 N N     . MET   A 1 167 ? -6.08800  -11.40500 36.25200 1.000 22.28125 ?  147 MET   A N     1 
ATOM   1085 C CA    . MET   A 1 167 ? -5.41000  -11.42300 34.96700 1.000 20.55151 ?  147 MET   A CA    1 
ATOM   1086 C C     . MET   A 1 167 ? -6.41200  -10.95200 33.92100 1.000 20.85046 ?  147 MET   A C     1 
ATOM   1087 O O     . MET   A 1 167 ? -7.53200  -11.47100 33.85100 1.000 24.48404 ?  147 MET   A O     1 
ATOM   1088 C CB    . MET   A 1 167 ? -4.85800  -12.82300 34.65100 1.000 22.66503 ?  147 MET   A CB    1 
ATOM   1089 C CG    . MET   A 1 167 ? -4.19300  -12.87700 33.30600 1.000 25.91548 ?  147 MET   A CG    1 
ATOM   1090 S SD    . MET   A 1 167 ? -3.39400  -14.47500 32.99000 1.000 34.43311 ?  147 MET   A SD    1 
ATOM   1091 C CE    . MET   A 1 167 ? -4.85400  -15.35100 32.49600 1.000 29.61633 ?  147 MET   A CE    1 
ATOM   1092 N N     . ALA   A 1 168 ? -6.04200  -9.92700  33.15300 1.000 20.37429 ?  148 ALA   A N     1 
ATOM   1093 C CA    . ALA   A 1 168 ? -6.95800  -9.32700  32.18600 1.000 18.61227 ?  148 ALA   A CA    1 
ATOM   1094 C C     . ALA   A 1 168 ? -6.18300  -9.27800  30.87700 1.000 22.59700 ?  148 ALA   A C     1 
ATOM   1095 O O     . ALA   A 1 168 ? -5.42000  -8.33100  30.64700 1.000 21.48886 ?  148 ALA   A O     1 
ATOM   1096 C CB    . ALA   A 1 168 ? -7.44000  -7.95000  32.62500 1.000 21.60594 ?  148 ALA   A CB    1 
ATOM   1097 N N     . THR   A 1 169 ? -6.35000  -10.29900 30.03700 1.000 21.51219 ?  149 THR   A N     1 
ATOM   1098 C CA    . THR   A 1 169 ? -5.53100  -10.39200 28.83000 1.000 20.66028 ?  149 THR   A CA    1 
ATOM   1099 C C     . THR   A 1 169 ? -6.29500  -9.83000  27.64100 1.000 18.63000 ?  149 THR   A C     1 
ATOM   1100 O O     . THR   A 1 169 ? -7.43900  -10.23000 27.38300 1.000 18.84961 ?  149 THR   A O     1 
ATOM   1101 C CB    . THR   A 1 169 ? -5.06000  -11.82600 28.54600 1.000 29.88229 ?  149 THR   A CB    1 
ATOM   1102 O OG1   . THR   A 1 169 ? -6.17600  -12.66400 28.24700 1.000 30.09033 ?  149 THR   A OG1   1 
ATOM   1103 C CG2   . THR   A 1 169 ? -4.34300  -12.39300 29.76500 1.000 23.25034 ?  149 THR   A CG2   1 
ATOM   1104 N N     . ASN   A 1 170 ? -5.64700  -8.89800  26.93000 1.000 18.44900 ?  150 ASN   A N     1 
ATOM   1105 C CA    . ASN   A 1 170 ? -6.20300  -8.27000  25.73100 1.000 16.86947 ?  150 ASN   A CA    1 
ATOM   1106 C C     . ASN   A 1 170 ? -7.55600  -7.64700  26.00400 1.000 19.15084 ?  150 ASN   A C     1 
ATOM   1107 O O     . ASN   A 1 170 ? -8.45100  -7.68800  25.16200 1.000 21.11208 ?  150 ASN   A O     1 
ATOM   1108 C CB    . ASN   A 1 170 ? -6.28900  -9.26900  24.56800 1.000 19.92209 ?  150 ASN   A CB    1 
ATOM   1109 C CG    . ASN   A 1 170 ? -4.92000  -9.64700  24.03600 1.000 18.31625 ?  150 ASN   A CG    1 
ATOM   1110 O OD1   . ASN   A 1 170 ? -3.91000  -9.18500  24.55700 1.000 20.01541 ?  150 ASN   A OD1   1 
ATOM   1111 N ND2   . ASN   A 1 170 ? -4.87900  -10.49200 23.01000 1.000 20.19587 ?  150 ASN   A ND2   1 
ATOM   1112 N N     . LEU   A 1 171 ? -7.70600  -7.06500  27.20000 1.000 16.96379 ?  151 LEU   A N     1 
ATOM   1113 C CA    . LEU   A 1 171 ? -8.98300  -6.51200  27.62500 1.000 17.87954 ?  151 LEU   A CA    1 
ATOM   1114 C C     . LEU   A 1 171 ? -9.04700  -4.99700  27.50300 1.000 18.17016 ?  151 LEU   A C     1 
ATOM   1115 O O     . LEU   A 1 171 ? -10.06500 -4.46500  27.03400 1.000 19.20439 ?  151 LEU   A O     1 
ATOM   1116 C CB    . LEU   A 1 171 ? -9.28000  -6.89300  29.08500 1.000 18.67834 ?  151 LEU   A CB    1 
ATOM   1117 C CG    . LEU   A 1 171 ? -10.56100 -6.23200  29.60500 1.000 19.48663 ?  151 LEU   A CG    1 
ATOM   1118 C CD1   . LEU   A 1 171 ? -11.79900 -6.79300  28.92400 1.000 19.86506 ?  151 LEU   A CD1   1 
ATOM   1119 C CD2   . LEU   A 1 171 ? -10.66700 -6.44000  31.13100 1.000 23.57697 ?  151 LEU   A CD2   1 
ATOM   1120 N N     . ILE   A 1 172 ? -7.99800  -4.29200  27.95200 1.000 16.47510 ?  152 ILE   A N     1 
ATOM   1121 C CA    . ILE   A 1 172 ? -8.15400  -2.84500  28.15500 1.000 17.32602 ?  152 ILE   A CA    1 
ATOM   1122 C C     . ILE   A 1 172 ? -8.48500  -2.11100  26.85800 1.000 18.45973 ?  152 ILE   A C     1 
ATOM   1123 O O     . ILE   A 1 172 ? -9.23100  -1.11600  26.89000 1.000 19.37129 ?  152 ILE   A O     1 
ATOM   1124 C CB    . ILE   A 1 172 ? -6.91800  -2.24200  28.85900 1.000 19.07769 ?  152 ILE   A CB    1 
ATOM   1125 C CG1   . ILE   A 1 172 ? -5.64600  -2.39300  28.00900 1.000 19.95969 ?  152 ILE   A CG1   1 
ATOM   1126 C CG2   . ILE   A 1 172 ? -6.78600  -2.75700  30.30600 1.000 21.63776 ?  152 ILE   A CG2   1 
ATOM   1127 C CD1   . ILE   A 1 172 ? -4.43800  -1.52100  28.53700 1.000 23.85695 ?  152 ILE   A CD1   1 
ATOM   1128 N N     . ASP   A 1 173 ? -7.99000  -2.58900  25.69200 1.000 18.00939 ?  153 ASP   A N     1 
ATOM   1129 C CA    . ASP   A 1 173 ? -8.29400  -1.90700  24.42600 1.000 18.75567 ?  153 ASP   A CA    1 
ATOM   1130 C C     . ASP   A 1 173 ? -9.65800  -2.31300  23.85100 1.000 15.59644 ?  153 ASP   A C     1 
ATOM   1131 O O     . ASP   A 1 173 ? -9.99000  -1.99300  22.68900 1.000 18.63409 ?  153 ASP   A O     1 
ATOM   1132 C CB    . ASP   A 1 173 ? -7.16500  -2.10600  23.38300 1.000 19.07420 ?  153 ASP   A CB    1 
ATOM   1133 C CG    . ASP   A 1 173 ? -6.77400  -3.58500  23.16200 1.000 26.44319 ?  153 ASP   A CG    1 
ATOM   1134 O OD1   . ASP   A 1 173 ? -6.90300  -4.40800  24.09100 1.000 26.69498 ?  153 ASP   A OD1   1 
ATOM   1135 O OD2   . ASP   A 1 173 ? -6.27100  -3.89600  22.04900 1.000 20.11866 -1 153 ASP   A OD2   1 
ATOM   1136 N N     . ARG   A 1 174 ? -10.47100 -2.97900  24.65300 1.000 16.12083 ?  154 ARG   A N     1 
ATOM   1137 C CA    . ARG   A 1 174 ? -11.85200 -3.25200  24.28000 1.000 18.76442 ?  154 ARG   A CA    1 
ATOM   1138 C C     . ARG   A 1 174 ? -12.85400 -2.72900  25.31800 1.000 20.94104 ?  154 ARG   A C     1 
ATOM   1139 O O     . ARG   A 1 174 ? -14.05800 -3.00700  25.20000 1.000 22.66435 ?  154 ARG   A O     1 
ATOM   1140 C CB    . ARG   A 1 174 ? -12.01700 -4.76400  24.05500 1.000 17.41572 ?  154 ARG   A CB    1 
ATOM   1141 C CG    . ARG   A 1 174 ? -11.12900 -5.31300  22.90300 1.000 16.85677 ?  154 ARG   A CG    1 
ATOM   1142 C CD    . ARG   A 1 174 ? -11.60600 -4.78900  21.53300 1.000 18.11675 ?  154 ARG   A CD    1 
ATOM   1143 N NE    . ARG   A 1 174 ? -10.82800 -5.32200  20.40600 1.000 18.47825 ?  154 ARG   A NE    1 
ATOM   1144 C CZ    . ARG   A 1 174 ? -9.89000  -4.62800  19.76400 1.000 20.76807 ?  154 ARG   A CZ    1 
ATOM   1145 N NH1   . ARG   A 1 174 ? -9.45100  -3.45600  20.22200 1.000 21.31322 ?  154 ARG   A NH1   1 
ATOM   1146 N NH2   . ARG   A 1 174 ? -9.37700  -5.11200  18.64000 1.000 20.14639 ?  154 ARG   A NH2   1 
ATOM   1147 N N     . LEU   A 1 175 ? -12.40200 -1.95500  26.30900 1.000 18.64485 ?  155 LEU   A N     1 
ATOM   1148 C CA    . LEU   A 1 175 ? -13.27800 -1.42000  27.34600 1.000 19.78268 ?  155 LEU   A CA    1 
ATOM   1149 C C     . LEU   A 1 175 ? -13.84400 -0.06000  26.93000 1.000 21.13832 ?  155 LEU   A C     1 
ATOM   1150 O O     . LEU   A 1 175 ? -13.12600 0.78800   26.39000 1.000 20.31472 ?  155 LEU   A O     1 
ATOM   1151 C CB    . LEU   A 1 175 ? -12.51200 -1.27200  28.66600 1.000 19.84451 ?  155 LEU   A CB    1 
ATOM   1152 C CG    . LEU   A 1 175 ? -11.97700 -2.56700  29.29000 1.000 19.39678 ?  155 LEU   A CG    1 
ATOM   1153 C CD1   . LEU   A 1 175 ? -11.18700 -2.21700  30.57600 1.000 19.67603 ?  155 LEU   A CD1   1 
ATOM   1154 C CD2   . LEU   A 1 175 ? -13.11200 -3.57300  29.54600 1.000 19.29017 ?  155 LEU   A CD2   1 
ATOM   1155 N N     . TYR   A 1 176 ? -15.11000 0.18900   27.26400 1.000 20.11582 ?  156 TYR   A N     1 
ATOM   1156 C CA    . TYR   A 1 176 ? -15.73600 1.49700   26.93600 1.000 21.88651 ?  156 TYR   A CA    1 
ATOM   1157 C C     . TYR   A 1 176 ? -15.06000 2.64600   27.69900 1.000 21.38132 ?  156 TYR   A C     1 
ATOM   1158 O O     . TYR   A 1 176 ? -14.99800 3.74700   27.17300 1.000 23.91862 ?  156 TYR   A O     1 
ATOM   1159 C CB    . TYR   A 1 176 ? -17.24400 1.45800   27.17800 1.000 21.42833 ?  156 TYR   A CB    1 
ATOM   1160 C CG    . TYR   A 1 176 ? -17.72300 1.11800   28.56400 1.000 24.05265 ?  156 TYR   A CG    1 
ATOM   1161 C CD1   . TYR   A 1 176 ? -17.94600 -0.19400  28.94100 1.000 24.44353 ?  156 TYR   A CD1   1 
ATOM   1162 C CD2   . TYR   A 1 176 ? -18.02500 2.11100   29.47900 1.000 25.42044 ?  156 TYR   A CD2   1 
ATOM   1163 C CE1   . TYR   A 1 176 ? -18.41800 -0.51400  30.20100 1.000 22.25978 ?  156 TYR   A CE1   1 
ATOM   1164 C CE2   . TYR   A 1 176 ? -18.49500 1.80900   30.74400 1.000 24.83316 ?  156 TYR   A CE2   1 
ATOM   1165 C CZ    . TYR   A 1 176 ? -18.69800 0.49100   31.10600 1.000 20.12641 ?  156 TYR   A CZ    1 
ATOM   1166 O OH    . TYR   A 1 176 ? -19.16200 0.17900   32.35400 1.000 22.71692 ?  156 TYR   A OH    1 
ATOM   1167 N N     . GLU   A 1 177 ? -14.60200 2.37700   28.91300 1.000 20.48971 ?  157 GLU   A N     1 
ATOM   1168 C CA    . GLU   A 1 177 ? -13.89300 3.40500   29.71200 1.000 21.67671 ?  157 GLU   A CA    1 
ATOM   1169 C C     . GLU   A 1 177 ? -12.87600 2.69500   30.60200 1.000 20.94699 ?  157 GLU   A C     1 
ATOM   1170 O O     . GLU   A 1 177 ? -13.19100 2.38900   31.74100 1.000 20.15058 ?  157 GLU   A O     1 
ATOM   1171 C CB    . GLU   A 1 177 ? -14.84500 4.28300   30.52300 1.000 22.07054 ?  157 GLU   A CB    1 
ATOM   1172 C CG    . GLU   A 1 177 ? -14.40100 5.73500   30.64000 1.000 21.05384 ?  157 GLU   A CG    1 
ATOM   1173 C CD    . GLU   A 1 177 ? -13.02900 6.03800   31.22400 1.000 29.80493 ?  157 GLU   A CD    1 
ATOM   1174 O OE1   . GLU   A 1 177 ? -12.03800 5.48700   30.74400 1.000 25.55534 ?  157 GLU   A OE1   1 
ATOM   1175 O OE2   . GLU   A 1 177 ? -12.95000 6.86800   32.13200 1.000 30.17723 -1 157 GLU   A OE2   1 
ATOM   1176 N N     . PRO   A 1 178 ? -11.64900 2.47000   30.09800 1.000 21.94766 ?  158 PRO   A N     1 
ATOM   1177 C CA    . PRO   A 1 178 ? -10.64900 1.69500   30.83500 1.000 21.56023 ?  158 PRO   A CA    1 
ATOM   1178 C C     . PRO   A 1 178 ? -10.33100 2.15900   32.27000 1.000 23.73072 ?  158 PRO   A C     1 
ATOM   1179 O O     . PRO   A 1 178 ? -9.98900  1.35100   33.07200 1.000 22.38254 ?  158 PRO   A O     1 
ATOM   1180 C CB    . PRO   A 1 178 ? -9.42600  1.83300   29.91900 1.000 24.14492 ?  158 PRO   A CB    1 
ATOM   1181 C CG    . PRO   A 1 178 ? -9.99500  2.04400   28.54800 1.000 27.21541 ?  158 PRO   A CG    1 
ATOM   1182 C CD    . PRO   A 1 178 ? -11.18600 2.93500   28.79400 1.000 19.09519 ?  158 PRO   A CD    1 
ATOM   1183 N N     . ARG   A 1 179 ? -10.47900 3.45300   32.54000 1.000 22.07182 ?  159 ARG   A N     1 
ATOM   1184 C CA    . ARG   A 1 179 ? -10.11800 3.97900   33.88100 1.000 18.86796 ?  159 ARG   A CA    1 
ATOM   1185 C C     . ARG   A 1 179 ? -11.06800 3.43800   34.95400 1.000 21.91391 ?  159 ARG   A C     1 
ATOM   1186 O O     . ARG   A 1 179 ? -10.61800 3.23400   36.07200 1.000 23.72938 ?  159 ARG   A O     1 
ATOM   1187 C CB    . ARG   A 1 179 ? -10.13500 5.50700   33.87900 1.000 21.57444 ?  159 ARG   A CB    1 
ATOM   1188 C CG    . ARG   A 1 179 ? -8.87900  6.14500   33.31700 1.000 31.80506 ?  159 ARG   A CG    1 
ATOM   1189 C CD    . ARG   A 1 179 ? -9.15800  7.62200   33.17100 1.000 31.79717 ?  159 ARG   A CD    1 
ATOM   1190 N NE    . ARG   A 1 179 ? -8.40100  8.39200   34.13500 1.000 49.08769 ?  159 ARG   A NE    1 
ATOM   1191 C CZ    . ARG   A 1 179 ? -7.08200  8.50900   34.12000 1.000 51.77871 ?  159 ARG   A CZ    1 
ATOM   1192 N NH1   . ARG   A 1 179 ? -6.45200  8.71300   32.97900 1.000 42.54358 ?  159 ARG   A NH1   1 
ATOM   1193 N NH2   . ARG   A 1 179 ? -6.40100  8.41600   35.24900 1.000 37.72377 ?  159 ARG   A NH2   1 
ATOM   1194 N N     . LEU   A 1 180 ? -12.33500 3.22500   34.60900 1.000 21.66444 ?  160 LEU   A N     1 
ATOM   1195 C CA    . LEU   A 1 180 ? -13.28800 2.63700   35.58600 1.000 21.23124 ?  160 LEU   A CA    1 
ATOM   1196 C C     . LEU   A 1 180 ? -12.70100 1.32900   36.11700 1.000 25.54551 ?  160 LEU   A C     1 
ATOM   1197 O O     . LEU   A 1 180 ? -12.85400 1.04700   37.30300 1.000 24.65967 ?  160 LEU   A O     1 
ATOM   1198 C CB    . LEU   A 1 180 ? -14.62300 2.36200   34.89700 1.000 20.96054 ?  160 LEU   A CB    1 
ATOM   1199 C CG    . LEU   A 1 180 ? -15.33000 3.56700   34.28400 1.000 37.37378 ?  160 LEU   A CG    1 
ATOM   1200 C CD1   . LEU   A 1 180 ? -16.74800 3.20500   33.87700 1.000 26.22183 ?  160 LEU   A CD1   1 
ATOM   1201 C CD2   . LEU   A 1 180 ? -15.34100 4.73700   35.24600 1.000 29.24403 ?  160 LEU   A CD2   1 
ATOM   1202 N N     . PHE   A 1 181 ? -12.11500 0.54400   35.22300 1.000 21.24566 ?  161 PHE   A N     1 
ATOM   1203 C CA    . PHE   A 1 181 ? -11.46800 -0.71900  35.63800 1.000 21.73257 ?  161 PHE   A CA    1 
ATOM   1204 C C     . PHE   A 1 181 ? -10.12800 -0.43600  36.32700 1.000 22.05327 ?  161 PHE   A C     1 
ATOM   1205 O O     . PHE   A 1 181 ? -9.95700  -0.84400  37.47000 1.000 23.87730 ?  161 PHE   A O     1 
ATOM   1206 C CB    . PHE   A 1 181 ? -11.28500 -1.59900  34.39900 1.000 20.59296 ?  161 PHE   A CB    1 
ATOM   1207 C CG    . PHE   A 1 181 ? -10.26700 -2.69800  34.54400 1.000 20.49148 ?  161 PHE   A CG    1 
ATOM   1208 C CD1   . PHE   A 1 181 ? -10.43800 -3.70700  35.47400 1.000 20.71425 ?  161 PHE   A CD1   1 
ATOM   1209 C CD2   . PHE   A 1 181 ? -9.13800  -2.72300  33.74600 1.000 25.05441 ?  161 PHE   A CD2   1 
ATOM   1210 C CE1   . PHE   A 1 181 ? -9.49600  -4.71200  35.60600 1.000 19.57726 ?  161 PHE   A CE1   1 
ATOM   1211 C CE2   . PHE   A 1 181 ? -8.19800  -3.73000  33.87900 1.000 23.82400 ?  161 PHE   A CE2   1 
ATOM   1212 C CZ    . PHE   A 1 181 ? -8.38000  -4.72400  34.80800 1.000 21.92206 ?  161 PHE   A CZ    1 
ATOM   1213 N N     . LEU   A 1 182 ? -9.22900  0.28100   35.65800 1.000 22.96647 ?  162 LEU   A N     1 
ATOM   1214 C CA    . LEU   A 1 182 ? -7.84700  0.44000   36.18300 1.000 20.99894 ?  162 LEU   A CA    1 
ATOM   1215 C C     . LEU   A 1 182 ? -7.78500  1.20000   37.51200 1.000 24.59199 ?  162 LEU   A C     1 
ATOM   1216 O O     . LEU   A 1 182 ? -6.97600  0.82600   38.34700 1.000 23.66125 ?  162 LEU   A O     1 
ATOM   1217 C CB    . LEU   A 1 182 ? -7.00100  1.14600   35.12300 1.000 20.09847 ?  162 LEU   A CB    1 
ATOM   1218 C CG    . LEU   A 1 182 ? -6.80900  0.37000   33.82300 1.000 22.06968 ?  162 LEU   A CG    1 
ATOM   1219 C CD1   . LEU   A 1 182 ? -6.35700  1.29200   32.70400 1.000 20.53137 ?  162 LEU   A CD1   1 
ATOM   1220 C CD2   . LEU   A 1 182 ? -5.82200  -0.77100  34.01500 1.000 26.67831 ?  162 LEU   A CD2   1 
ATOM   1221 N N     . GLU   A 1 183 ? -8.58300  2.25000   37.66300 1.000 23.68848 ?  163 GLU   A N     1 
ATOM   1222 C CA    . GLU   A 1 183 ? -8.45500  3.05100   38.88200 1.000 20.88954 ?  163 GLU   A CA    1 
ATOM   1223 C C     . GLU   A 1 183 ? -9.00200  2.33500   40.10700 1.000 28.99587 ?  163 GLU   A C     1 
ATOM   1224 O O     . GLU   A 1 183 ? -8.65100  2.69800   41.23600 1.000 27.20437 ?  163 GLU   A O     1 
ATOM   1225 C CB    . GLU   A 1 183 ? -9.16000  4.40700   38.69900 1.000 21.59949 ?  163 GLU   A CB    1 
ATOM   1226 C CG    . GLU   A 1 183 ? -8.43500  5.29300   37.69700 1.000 23.04318 ?  163 GLU   A CG    1 
ATOM   1227 C CD    . GLU   A 1 183 ? -9.03300  6.71700   37.57600 1.000 33.12778 ?  163 GLU   A CD    1 
ATOM   1228 O OE1   . GLU   A 1 183 ? -10.05000 7.03000   38.23300 1.000 28.69807 ?  163 GLU   A OE1   1 
ATOM   1229 O OE2   . GLU   A 1 183 ? -8.47100  7.52600   36.80700 1.000 33.59879 -1 163 GLU   A OE2   1 
ATOM   1230 N N     . ASN   A 1 184 ? -9.83800  1.31900   39.91100 1.000 24.65633 ?  164 ASN   A N     1 
ATOM   1231 C CA    . ASN   A 1 184 ? -10.51000 0.66100   41.01600 1.000 23.14342 ?  164 ASN   A CA    1 
ATOM   1232 C C     . ASN   A 1 184 ? -10.07400 -0.76700  41.27000 1.000 26.63565 ?  164 ASN   A C     1 
ATOM   1233 O O     . ASN   A 1 184 ? -10.34400 -1.28500  42.35000 1.000 23.70245 ?  164 ASN   A O     1 
ATOM   1234 C CB    . ASN   A 1 184 ? -12.02200 0.69200   40.78900 1.000 24.16322 ?  164 ASN   A CB    1 
ATOM   1235 C CG    . ASN   A 1 184 ? -12.55900 2.08400   40.84400 1.000 30.67623 ?  164 ASN   A CG    1 
ATOM   1236 O OD1   . ASN   A 1 184 ? -12.60300 2.67200   41.92800 1.000 30.90074 ?  164 ASN   A OD1   1 
ATOM   1237 N ND2   . ASN   A 1 184 ? -12.93700 2.64300   39.69500 1.000 23.69090 ?  164 ASN   A ND2   1 
ATOM   1238 N N     . ILE   A 1 185 ? -9.38900  -1.41500  40.33000 1.000 24.51522 ?  165 ILE   A N     1 
ATOM   1239 C CA    . ILE   A 1 185 ? -9.16100  -2.85800  40.46900 1.000 19.45221 ?  165 ILE   A CA    1 
ATOM   1240 C C     . ILE   A 1 185 ? -8.31100  -3.23500  41.68600 1.000 24.05681 ?  165 ILE   A C     1 
ATOM   1241 O O     . ILE   A 1 185 ? -8.42100  -4.36900  42.17500 1.000 25.59517 ?  165 ILE   A O     1 
ATOM   1242 C CB    . ILE   A 1 185 ? -8.54100  -3.39800  39.15800 1.000 20.81748 ?  165 ILE   A CB    1 
ATOM   1243 C CG1   . ILE   A 1 185 ? -8.70800  -4.91900  39.07400 1.000 24.36050 ?  165 ILE   A CG1   1 
ATOM   1244 C CG2   . ILE   A 1 185 ? -7.08900  -2.93300  39.00100 1.000 26.05429 ?  165 ILE   A CG2   1 
ATOM   1245 C CD1   . ILE   A 1 185 ? -10.14000 -5.37000  39.17800 1.000 23.60186 ?  165 ILE   A CD1   1 
ATOM   1246 N N     . HIS   A 1 186 ? -7.48000  -2.31100  42.21600 1.000 26.13128 ?  166 HIS   A N     1 
ATOM   1247 C CA    . HIS   A 1 186 ? -6.66000  -2.66200  43.37100 1.000 28.12809 ?  166 HIS   A CA    1 
ATOM   1248 C C     . HIS   A 1 186 ? -7.52700  -3.02900  44.56900 1.000 26.82643 ?  166 HIS   A C     1 
ATOM   1249 O O     . HIS   A 1 186 ? -7.09600  -3.79700  45.43100 1.000 27.56825 ?  166 HIS   A O     1 
ATOM   1250 C CB    . HIS   A 1 186 ? -5.72800  -1.51400  43.74700 1.000 27.59799 ?  166 HIS   A CB    1 
ATOM   1251 C CG    . HIS   A 1 186 ? -6.45500  -0.28700  44.19200 1.000 28.49268 ?  166 HIS   A CG    1 
ATOM   1252 N ND1   . HIS   A 1 186 ? -7.07600  0.57400   43.30900 1.000 29.77762 ?  166 HIS   A ND1   1 
ATOM   1253 C CD2   . HIS   A 1 186 ? -6.68600  0.20800   45.43100 1.000 28.47495 ?  166 HIS   A CD2   1 
ATOM   1254 C CE1   . HIS   A 1 186 ? -7.64500  1.55800   43.98600 1.000 32.03990 ?  166 HIS   A CE1   1 
ATOM   1255 N NE2   . HIS   A 1 186 ? -7.42400  1.36100   45.27400 1.000 27.53338 ?  166 HIS   A NE2   1 
ATOM   1256 N N     . LYS   A 1 187 ? -8.75900  -2.51400  44.62300 1.000 26.16259 ?  167 LYS   A N     1 
ATOM   1257 C CA    . LYS   A 1 187 ? -9.65000  -2.84500  45.72700 1.000 25.94376 ?  167 LYS   A CA    1 
ATOM   1258 C C     . LYS   A 1 187 ? -10.07200 -4.30300  45.73100 1.000 26.09835 ?  167 LYS   A C     1 
ATOM   1259 O O     . LYS   A 1 187 ? -10.58400 -4.77500  46.75100 1.000 27.08972 ?  167 LYS   A O     1 
ATOM   1260 C CB    . LYS   A 1 187 ? -10.90400 -1.98000  45.68800 1.000 24.38988 ?  167 LYS   A CB    1 
ATOM   1261 C CG    . LYS   A 1 187 ? -10.65000 -0.48100  45.93000 1.000 31.38151 ?  167 LYS   A CG    1 
ATOM   1262 C CD    . LYS   A 1 187 ? -11.80600 0.35700   45.41800 1.000 38.05469 ?  167 LYS   A CD    1 
ATOM   1263 N N     . ARG   A 1 188 ? -9.88700  -5.02400  44.62400 1.000 24.67114 ?  168 ARG   A N     1 
ATOM   1264 C CA    . ARG   A 1 188 ? -10.30600 -6.42200  44.54000 1.000 24.13873 ?  168 ARG   A CA    1 
ATOM   1265 C C     . ARG   A 1 188 ? -9.15900  -7.40200  44.71800 1.000 28.72770 ?  168 ARG   A C     1 
ATOM   1266 O O     . ARG   A 1 188 ? -9.36700  -8.60600  44.54700 1.000 27.85152 ?  168 ARG   A O     1 
ATOM   1267 C CB    . ARG   A 1 188 ? -10.98500 -6.68200  43.19100 1.000 26.73249 ?  168 ARG   A CB    1 
ATOM   1268 C CG    . ARG   A 1 188 ? -11.97700 -5.58500  42.81800 1.000 27.66555 ?  168 ARG   A CG    1 
ATOM   1269 C CD    . ARG   A 1 188 ? -13.11800 -5.47000  43.81600 1.000 32.35886 ?  168 ARG   A CD    1 
ATOM   1270 N NE    . ARG   A 1 188 ? -14.16200 -4.56400  43.33400 1.000 30.02626 ?  168 ARG   A NE    1 
ATOM   1271 C CZ    . ARG   A 1 188 ? -15.30600 -4.95900  42.79100 1.000 31.01023 ?  168 ARG   A CZ    1 
ATOM   1272 N NH1   . ARG   A 1 188 ? -15.58000 -6.23800  42.62000 1.000 26.33875 ?  168 ARG   A NH1   1 
ATOM   1273 N NH2   . ARG   A 1 188 ? -16.19800 -4.04700  42.41700 1.000 30.11642 ?  168 ARG   A NH2   1 
ATOM   1274 N N     . ILE   A 1 189 ? -7.95500  -6.91800  45.01700 1.000 25.50901 ?  169 ILE   A N     1 
ATOM   1275 C CA    . ILE   A 1 189 ? -6.74800  -7.73800  45.11700 1.000 22.32930 ?  169 ILE   A CA    1 
ATOM   1276 C C     . ILE   A 1 189 ? -6.22200  -7.73300  46.54400 1.000 33.37919 ?  169 ILE   A C     1 
ATOM   1277 O O     . ILE   A 1 189 ? -6.17000  -6.68300  47.19800 1.000 30.86788 ?  169 ILE   A O     1 
ATOM   1278 C CB    . ILE   A 1 189 ? -5.65200  -7.26900  44.13200 1.000 28.79180 ?  169 ILE   A CB    1 
ATOM   1279 C CG1   . ILE   A 1 189 ? -6.24400  -7.05100  42.73000 1.000 26.22649 ?  169 ILE   A CG1   1 
ATOM   1280 C CG2   . ILE   A 1 189 ? -4.42800  -8.19500  44.15400 1.000 28.20064 ?  169 ILE   A CG2   1 
ATOM   1281 C CD1   . ILE   A 1 189 ? -5.18200  -6.64700  41.69400 1.000 24.74357 ?  169 ILE   A CD1   1 
ATOM   1282 N N     . ASN   A 1 190 ? -5.82600  -8.91800  47.01400 1.000 33.85668 ?  170 ASN   A N     1 
ATOM   1283 C CA    . ASN   A 1 190 ? -5.22400  -9.06100  48.33200 1.000 33.19459 ?  170 ASN   A CA    1 
ATOM   1284 C C     . ASN   A 1 190 ? -3.88100  -8.34000  48.38300 1.000 38.16992 ?  170 ASN   A C     1 
ATOM   1285 O O     . ASN   A 1 190 ? -3.23500  -8.09000  47.36000 1.000 34.20242 ?  170 ASN   A O     1 
ATOM   1286 C CB    . ASN   A 1 190 ? -5.03800  -10.53600 48.67800 1.000 33.17072 ?  170 ASN   A CB    1 
ATOM   1287 C CG    . ASN   A 1 190 ? -6.35100  -11.25800 48.79400 1.000 36.48133 ?  170 ASN   A CG    1 
ATOM   1288 O OD1   . ASN   A 1 190 ? -7.32500  -10.70800 49.31500 1.000 35.95747 ?  170 ASN   A OD1   1 
ATOM   1289 N ND2   . ASN   A 1 190 ? -6.39800  -12.49400 48.30900 1.000 36.99508 ?  170 ASN   A ND2   1 
ATOM   1290 N N     . GLU   A 1 191 ? -3.46300  -7.99100  49.59900 1.000 42.31817 ?  171 GLU   A N     1 
ATOM   1291 C CA    . GLU   A 1 191 ? -2.16100  -7.36400  49.76800 1.000 34.40778 ?  171 GLU   A CA    1 
ATOM   1292 C C     . GLU   A 1 191 ? -1.07900  -8.30700  49.25700 1.000 29.00337 ?  171 GLU   A C     1 
ATOM   1293 O O     . GLU   A 1 191 ? -1.15600  -9.52000  49.44900 1.000 36.32452 ?  171 GLU   A O     1 
ATOM   1294 C CB    . GLU   A 1 191 ? -1.93200  -7.01300  51.24800 1.000 45.79816 ?  171 GLU   A CB    1 
ATOM   1295 N N     . LYS   A 1 192 ? -0.09300  -7.75000  48.55300 1.000 41.05492 ?  172 LYS   A N     1 
ATOM   1296 C CA    . LYS   A 1 192 ? 0.97900   -8.50200  47.89200 1.000 50.40861 ?  172 LYS   A CA    1 
ATOM   1297 C C     . LYS   A 1 192 ? 0.49200   -9.34600  46.71600 1.000 42.81437 ?  172 LYS   A C     1 
ATOM   1298 O O     . LYS   A 1 192 ? 1.27700   -10.13300 46.16700 1.000 41.49302 ?  172 LYS   A O     1 
ATOM   1299 C CB    . LYS   A 1 192 ? 1.74200   -9.41900  48.86100 1.000 41.49157 ?  172 LYS   A CB    1 
ATOM   1300 N N     . GLY   A 1 193 ? -0.77700  -9.22200  46.32300 1.000 35.93789 ?  173 GLY   A N     1 
ATOM   1301 C CA    . GLY   A 1 193 ? -1.28400  -9.89300  45.13900 1.000 30.09731 ?  173 GLY   A CA    1 
ATOM   1302 C C     . GLY   A 1 193 ? -0.88200  -9.15800  43.86900 1.000 30.37331 ?  173 GLY   A C     1 
ATOM   1303 O O     . GLY   A 1 193 ? -0.20000  -8.13100  43.89500 1.000 28.72642 ?  173 GLY   A O     1 
ATOM   1304 N N     . TYR   A 1 194 ? -1.32700  -9.70400  42.72700 1.000 24.35424 ?  174 TYR   A N     1 
ATOM   1305 C CA    . TYR   A 1 194 ? -0.85900  -9.25500  41.41800 1.000 24.11719 ?  174 TYR   A CA    1 
ATOM   1306 C C     . TYR   A 1 194 ? -2.01700  -8.93200  40.48400 1.000 23.43345 ?  174 TYR   A C     1 
ATOM   1307 O O     . TYR   A 1 194 ? -3.03500  -9.63100  40.46800 1.000 25.02406 ?  174 TYR   A O     1 
ATOM   1308 C CB    . TYR   A 1 194 ? 0.00200   -10.31700 40.73500 1.000 27.78218 ?  174 TYR   A CB    1 
ATOM   1309 C CG    . TYR   A 1 194 ? 1.36700   -10.46200 41.34100 1.000 29.48670 ?  174 TYR   A CG    1 
ATOM   1310 C CD1   . TYR   A 1 194 ? 1.55600   -11.17700 42.52600 1.000 29.67538 ?  174 TYR   A CD1   1 
ATOM   1311 C CD2   . TYR   A 1 194 ? 2.47100   -9.87800  40.74700 1.000 31.36503 ?  174 TYR   A CD2   1 
ATOM   1312 C CE1   . TYR   A 1 194 ? 2.82200   -11.30900 43.08600 1.000 30.97962 ?  174 TYR   A CE1   1 
ATOM   1313 C CE2   . TYR   A 1 194 ? 3.74100   -10.00800 41.30200 1.000 32.98276 ?  174 TYR   A CE2   1 
ATOM   1314 C CZ    . TYR   A 1 194 ? 3.90700   -10.72000 42.46900 1.000 39.34404 ?  174 TYR   A CZ    1 
ATOM   1315 O OH    . TYR   A 1 194 ? 5.16500   -10.84000 43.00900 1.000 37.68682 ?  174 TYR   A OH    1 
ATOM   1316 N N     . LEU   A 1 195 ? -1.82800  -7.88700  39.68300 1.000 25.39593 ?  175 LEU   A N     1 
ATOM   1317 C CA    . LEU   A 1 195 ? -2.64000  -7.63200  38.50300 1.000 21.01616 ?  175 LEU   A CA    1 
ATOM   1318 C C     . LEU   A 1 195 ? -1.74400  -7.86200  37.29600 1.000 22.24637 ?  175 LEU   A C     1 
ATOM   1319 O O     . LEU   A 1 195 ? -0.66900  -7.26500  37.21000 1.000 23.60791 ?  175 LEU   A O     1 
ATOM   1320 C CB    . LEU   A 1 195 ? -3.14800  -6.19200  38.48400 1.000 22.69040 ?  175 LEU   A CB    1 
ATOM   1321 C CG    . LEU   A 1 195 ? -3.79300  -5.66800  37.19400 1.000 22.82748 ?  175 LEU   A CG    1 
ATOM   1322 C CD1   . LEU   A 1 195 ? -5.16600  -6.27400  36.98500 1.000 25.14371 ?  175 LEU   A CD1   1 
ATOM   1323 C CD2   . LEU   A 1 195 ? -3.86100  -4.11900  37.18000 1.000 25.55974 ?  175 LEU   A CD2   1 
ATOM   1324 N N     . ILE   A 1 196 ? -2.17100  -8.70400  36.35600 1.000 21.73616 ?  176 ILE   A N     1 
ATOM   1325 C CA    . ILE   A 1 196 ? -1.37300  -8.95800  35.16100 1.000 19.90575 ?  176 ILE   A CA    1 
ATOM   1326 C C     . ILE   A 1 196 ? -2.21400  -8.59600  33.94500 1.000 21.44243 ?  176 ILE   A C     1 
ATOM   1327 O O     . ILE   A 1 196 ? -3.28800  -9.16700  33.74000 1.000 21.69324 ?  176 ILE   A O     1 
ATOM   1328 C CB    . ILE   A 1 196 ? -0.86700  -10.40700 35.10000 1.000 22.28871 ?  176 ILE   A CB    1 
ATOM   1329 C CG1   . ILE   A 1 196 ? -0.00600  -10.67600 36.34400 1.000 23.73348 ?  176 ILE   A CG1   1 
ATOM   1330 C CG2   . ILE   A 1 196 ? -0.11800  -10.62900 33.79000 1.000 21.22702 ?  176 ILE   A CG2   1 
ATOM   1331 C CD1   . ILE   A 1 196 ? 0.75100   -12.01800 36.36500 1.000 26.80635 ?  176 ILE   A CD1   1 
ATOM   1332 N N     . LEU   A 1 197 ? -1.75900  -7.59200  33.19600 1.000 18.74844 ?  177 LEU   A N     1 
ATOM   1333 C CA    . LEU   A 1 197 ? -2.44600  -7.12100  32.00700 1.000 20.29514 ?  177 LEU   A CA    1 
ATOM   1334 C C     . LEU   A 1 197 ? -1.68200  -7.61000  30.78300 1.000 20.50040 ?  177 LEU   A C     1 
ATOM   1335 O O     . LEU   A 1 197 ? -0.45700  -7.71400  30.80900 1.000 26.88636 ?  177 LEU   A O     1 
ATOM   1336 C CB    . LEU   A 1 197 ? -2.48900  -5.59200  31.98200 1.000 20.66297 ?  177 LEU   A CB    1 
ATOM   1337 C CG    . LEU   A 1 197 ? -3.20600  -4.92600  33.14600 1.000 21.20161 ?  177 LEU   A CG    1 
ATOM   1338 C CD1   . LEU   A 1 197 ? -3.07500  -3.40400  32.96000 1.000 21.62024 ?  177 LEU   A CD1   1 
ATOM   1339 C CD2   . LEU   A 1 197 ? -4.65600  -5.38500  33.28500 1.000 23.51857 ?  177 LEU   A CD2   1 
ATOM   1340 N N     . THR   A 1 198 ? -2.39700  -7.89900  29.70600 1.000 18.67887 ?  178 THR   A N     1 
ATOM   1341 C CA    . THR   A 1 198 ? -1.75800  -7.92000  28.39400 1.000 16.47595 ?  178 THR   A CA    1 
ATOM   1342 C C     . THR   A 1 198 ? -2.60400  -7.11200  27.42700 1.000 18.90121 ?  178 THR   A C     1 
ATOM   1343 O O     . THR   A 1 198 ? -3.82800  -7.03900  27.56300 1.000 20.36836 ?  178 THR   A O     1 
ATOM   1344 C CB    . THR   A 1 198 ? -1.54200  -9.33100  27.83300 1.000 22.32237 ?  178 THR   A CB    1 
ATOM   1345 O OG1   . THR   A 1 198 ? -2.77900  -9.78900  27.26700 1.000 26.77096 ?  178 THR   A OG1   1 
ATOM   1346 C CG2   . THR   A 1 198 ? -1.07000  -10.27400 28.93500 1.000 21.29552 ?  178 THR   A CG2   1 
ATOM   1347 N N     . SER   A 1 199 ? -1.93600  -6.49700  26.46100 1.000 19.94520 ?  179 SER   A N     1 
ATOM   1348 C CA    . SER   A 1 199 ? -2.70600  -5.80300  25.44300 1.000 21.39757 ?  179 SER   A CA    1 
ATOM   1349 C C     . SER   A 1 199 ? -1.77800  -5.47600  24.28800 1.000 17.69367 ?  179 SER   A C     1 
ATOM   1350 O O     . SER   A 1 199 ? -0.60700  -5.12700  24.50300 1.000 18.77911 ?  179 SER   A O     1 
ATOM   1351 C CB    . SER   A 1 199 ? -3.33300  -4.49900  25.98400 1.000 18.13350 ?  179 SER   A CB    1 
ATOM   1352 O OG    . SER   A 1 199 ? -4.05000  -3.83800  24.94200 1.000 19.94395 ?  179 SER   A OG    1 
ATOM   1353 N N     . PRO   A 1 200 ? -2.28200  -5.53400  23.05800 1.000 16.30193 ?  180 PRO   A N     1 
ATOM   1354 C CA    . PRO   A 1 200 ? -1.55800  -4.96900  21.92000 1.000 14.89457 ?  180 PRO   A CA    1 
ATOM   1355 C C     . PRO   A 1 200 ? -1.86700  -3.49400  21.69000 1.000 17.88636 ?  180 PRO   A C     1 
ATOM   1356 O O     . PRO   A 1 200 ? -1.33000  -2.91000  20.74100 1.000 18.60600 ?  180 PRO   A O     1 
ATOM   1357 C CB    . PRO   A 1 200 ? -2.08100  -5.79300  20.74500 1.000 19.58462 ?  180 PRO   A CB    1 
ATOM   1358 C CG    . PRO   A 1 200 ? -3.50500  -6.10400  21.15300 1.000 22.12978 ?  180 PRO   A CG    1 
ATOM   1359 C CD    . PRO   A 1 200 ? -3.50800  -6.24000  22.65800 1.000 17.80580 ?  180 PRO   A CD    1 
ATOM   1360 N N     . TYR   A 1 201 ? -2.75000  -2.91100  22.50200 1.000 16.88917 ?  181 TYR   A N     1 
ATOM   1361 C CA    . TYR   A 1 201 ? -3.03700  -1.48200  22.45300 1.000 18.69795 ?  181 TYR   A CA    1 
ATOM   1362 C C     . TYR   A 1 201 ? -3.71300  -1.08900  21.13900 1.000 17.19491 ?  181 TYR   A C     1 
ATOM   1363 O O     . TYR   A 1 201 ? -3.41800  -0.03300  20.56100 1.000 18.25999 ?  181 TYR   A O     1 
ATOM   1364 C CB    . TYR   A 1 201 ? -1.76600  -0.65400  22.69200 1.000 19.00252 ?  181 TYR   A CB    1 
ATOM   1365 C CG    . TYR   A 1 201 ? -0.95000  -1.07600  23.90300 1.000 17.09358 ?  181 TYR   A CG    1 
ATOM   1366 C CD1   . TYR   A 1 201 ? -1.56800  -1.38700  25.10500 1.000 18.44670 ?  181 TYR   A CD1   1 
ATOM   1367 C CD2   . TYR   A 1 201 ? 0.43500   -1.18600  23.82600 1.000 20.61881 ?  181 TYR   A CD2   1 
ATOM   1368 C CE1   . TYR   A 1 201 ? -0.82600  -1.75900  26.23700 1.000 18.74811 ?  181 TYR   A CE1   1 
ATOM   1369 C CE2   . TYR   A 1 201 ? 1.19400   -1.57800  24.94000 1.000 18.52105 ?  181 TYR   A CE2   1 
ATOM   1370 C CZ    . TYR   A 1 201 ? 0.55300   -1.85400  26.14700 1.000 20.11626 ?  181 TYR   A CZ    1 
ATOM   1371 O OH    . TYR   A 1 201 ? 1.29500   -2.22300  27.25300 1.000 21.83977 ?  181 TYR   A OH    1 
ATOM   1372 N N     . THR   A 1 202 ? -4.64400  -1.94300  20.67600 1.000 17.18619 ?  182 THR   A N     1 
ATOM   1373 C CA    . THR   A 1 202 ? -5.40400  -1.69800  19.44600 1.000 16.48079 ?  182 THR   A CA    1 
ATOM   1374 C C     . THR   A 1 202 ? -6.61700  -0.80600  19.74000 1.000 16.08116 ?  182 THR   A C     1 
ATOM   1375 O O     . THR   A 1 202 ? -7.77900  -1.20400  19.64200 1.000 18.51346 ?  182 THR   A O     1 
ATOM   1376 C CB    . THR   A 1 202 ? -5.81800  -3.02700  18.81100 1.000 18.75845 ?  182 THR   A CB    1 
ATOM   1377 O OG1   . THR   A 1 202 ? -4.66200  -3.88600  18.74100 1.000 19.68197 ?  182 THR   A OG1   1 
ATOM   1378 C CG2   . THR   A 1 202 ? -6.37800  -2.79800  17.40800 1.000 21.04997 ?  182 THR   A CG2   1 
ATOM   1379 N N     . TRP   A 1 203 ? -6.32600  0.44400   20.09700 1.000 17.73897 ?  183 TRP   A N     1 
ATOM   1380 C CA    . TRP   A 1 203 ? -7.39000  1.40200   20.41400 1.000 14.77470 ?  183 TRP   A CA    1 
ATOM   1381 C C     . TRP   A 1 203 ? -8.18500  1.72300   19.16200 1.000 17.87746 ?  183 TRP   A C     1 
ATOM   1382 O O     . TRP   A 1 203 ? -7.61200  2.01600   18.11000 1.000 21.34188 ?  183 TRP   A O     1 
ATOM   1383 C CB    . TRP   A 1 203 ? -6.77400  2.69200   20.99000 1.000 17.49999 ?  183 TRP   A CB    1 
ATOM   1384 C CG    . TRP   A 1 203 ? -6.05000  2.42800   22.26900 1.000 18.98952 ?  183 TRP   A CG    1 
ATOM   1385 C CD1   . TRP   A 1 203 ? -4.68300  2.42700   22.46000 1.000 17.38955 ?  183 TRP   A CD1   1 
ATOM   1386 C CD2   . TRP   A 1 203 ? -6.62900  2.10700   23.53500 1.000 16.51945 ?  183 TRP   A CD2   1 
ATOM   1387 N NE1   . TRP   A 1 203 ? -4.39600  2.12200   23.76600 1.000 18.59742 ?  183 TRP   A NE1   1 
ATOM   1388 C CE2   . TRP   A 1 203 ? -5.56500  1.92200   24.44900 1.000 15.87132 ?  183 TRP   A CE2   1 
ATOM   1389 C CE3   . TRP   A 1 203 ? -7.95100  1.95100   23.99200 1.000 17.16665 ?  183 TRP   A CE3   1 
ATOM   1390 C CZ2   . TRP   A 1 203 ? -5.77400  1.57300   25.79500 1.000 17.99966 ?  183 TRP   A CZ2   1 
ATOM   1391 C CZ3   . TRP   A 1 203 ? -8.16100  1.61500   25.32900 1.000 16.12687 ?  183 TRP   A CZ3   1 
ATOM   1392 C CH2   . TRP   A 1 203 ? -7.07400  1.43900   26.21900 1.000 19.98883 ?  183 TRP   A CH2   1 
ATOM   1393 N N     . ARG   A 1 204 ? -9.50500  1.66000   19.27300 1.000 19.12455 ?  184 ARG   A N     1 
ATOM   1394 C CA    . ARG   A 1 204 ? -10.38100 1.93500   18.14500 1.000 23.52216 ?  184 ARG   A CA    1 
ATOM   1395 C C     . ARG   A 1 204 ? -11.63900 2.61100   18.67600 1.000 26.04700 ?  184 ARG   A C     1 
ATOM   1396 O O     . ARG   A 1 204 ? -12.16300 2.22500   19.72900 1.000 21.08675 ?  184 ARG   A O     1 
ATOM   1397 C CB    . ARG   A 1 204 ? -10.74100 0.64200   17.40300 1.000 26.42735 ?  184 ARG   A CB    1 
ATOM   1398 C CG    . ARG   A 1 204 ? -9.57600  0.04800   16.58600 1.000 28.77559 ?  184 ARG   A CG    1 
ATOM   1399 C CD    . ARG   A 1 204 ? -10.06200 -1.02200  15.62900 1.000 41.63244 ?  184 ARG   A CD    1 
ATOM   1400 N NE    . ARG   A 1 204 ? -10.52100 -0.43000  14.37200 1.000 42.56754 ?  184 ARG   A NE    1 
ATOM   1401 N N     . GLU   A 1 205 ? -12.11600 3.62300   17.94500 1.000 24.41440 ?  185 GLU   A N     1 
ATOM   1402 C CA    . GLU   A 1 205 ? -13.30800 4.34300   18.38400 1.000 26.79549 ?  185 GLU   A CA    1 
ATOM   1403 C C     . GLU   A 1 205 ? -14.54500 3.44400   18.44700 1.000 25.90737 ?  185 GLU   A C     1 
ATOM   1404 O O     . GLU   A 1 205 ? -15.47400 3.74600   19.20500 1.000 26.14283 ?  185 GLU   A O     1 
ATOM   1405 C CB    . GLU   A 1 205 ? -13.54900 5.55300   17.45900 1.000 30.87775 ?  185 GLU   A CB    1 
ATOM   1406 C CG    . GLU   A 1 205 ? -12.44900 6.60600   17.59600 1.000 36.20830 ?  185 GLU   A CG    1 
ATOM   1407 C CD    . GLU   A 1 205 ? -12.80900 7.97200   17.00000 1.000 47.78541 ?  185 GLU   A CD    1 
ATOM   1408 O OE1   . GLU   A 1 205 ? -13.84700 8.08500   16.32100 1.000 65.71300 ?  185 GLU   A OE1   1 
ATOM   1409 O OE2   . GLU   A 1 205 ? -12.04100 8.93400   17.20400 1.000 59.03316 -1 185 GLU   A OE2   1 
ATOM   1410 N N     . GLU   A 1 206 ? -14.56400 2.32100   17.72000 1.000 26.38730 ?  186 GLU   A N     1 
ATOM   1411 C CA    . GLU   A 1 206 ? -15.70800 1.41600   17.81200 1.000 29.19943 ?  186 GLU   A CA    1 
ATOM   1412 C C     . GLU   A 1 206 ? -15.81400 0.78700   19.19300 1.000 27.81606 ?  186 GLU   A C     1 
ATOM   1413 O O     . GLU   A 1 206 ? -16.90500 0.37500   19.59300 1.000 26.68621 ?  186 GLU   A O     1 
ATOM   1414 C CB    . GLU   A 1 206 ? -15.62600 0.30200   16.76000 1.000 33.52241 ?  186 GLU   A CB    1 
ATOM   1415 C CG    . GLU   A 1 206 ? -14.21700 -0.10200  16.41800 1.000 39.05339 ?  186 GLU   A CG    1 
ATOM   1416 C CD    . GLU   A 1 206 ? -14.13200 -1.36300  15.56900 1.000 54.62303 ?  186 GLU   A CD    1 
ATOM   1417 O OE1   . GLU   A 1 206 ? -15.07000 -2.18600  15.61600 1.000 67.74072 ?  186 GLU   A OE1   1 
ATOM   1418 O OE2   . GLU   A 1 206 ? -13.12300 -1.52700  14.84200 1.000 54.27954 -1 186 GLU   A OE2   1 
ATOM   1419 N N     . TYR   A 1 207 ? -14.70300 0.68200   19.93000 1.000 21.59618 ?  187 TYR   A N     1 
ATOM   1420 C CA    . TYR   A 1 207 ? -14.74000 0.14500   21.28600 1.000 21.10472 ?  187 TYR   A CA    1 
ATOM   1421 C C     . TYR   A 1 207 ? -14.62500 1.20600   22.37000 1.000 24.78413 ?  187 TYR   A C     1 
ATOM   1422 O O     . TYR   A 1 207 ? -15.19100 1.04100   23.46100 1.000 21.75078 ?  187 TYR   A O     1 
ATOM   1423 C CB    . TYR   A 1 207 ? -13.61100 -0.86700  21.49000 1.000 20.97289 ?  187 TYR   A CB    1 
ATOM   1424 C CG    . TYR   A 1 207 ? -13.72700 -2.04600  20.54900 1.000 25.71817 ?  187 TYR   A CG    1 
ATOM   1425 C CD1   . TYR   A 1 207 ? -14.67400 -3.02900  20.76800 1.000 27.99708 ?  187 TYR   A CD1   1 
ATOM   1426 C CD2   . TYR   A 1 207 ? -12.90500 -2.14900  19.43600 1.000 25.41917 ?  187 TYR   A CD2   1 
ATOM   1427 C CE1   . TYR   A 1 207 ? -14.80100 -4.11600  19.90400 1.000 27.16453 ?  187 TYR   A CE1   1 
ATOM   1428 C CE2   . TYR   A 1 207 ? -13.01900 -3.23600  18.56200 1.000 26.53434 ?  187 TYR   A CE2   1 
ATOM   1429 C CZ    . TYR   A 1 207 ? -13.97800 -4.20300  18.80400 1.000 27.99085 ?  187 TYR   A CZ    1 
ATOM   1430 O OH    . TYR   A 1 207 ? -14.11600 -5.27400  17.95800 1.000 37.12523 ?  187 TYR   A OH    1 
ATOM   1431 N N     . THR   A 1 208 ? -13.87200 2.27000   22.11500 1.000 22.66268 ?  188 THR   A N     1 
ATOM   1432 C CA    . THR   A 1 208 ? -13.48200 3.20900   23.15500 1.000 21.41410 ?  188 THR   A CA    1 
ATOM   1433 C C     . THR   A 1 208 ? -13.42800 4.58900   22.52700 1.000 24.83932 ?  188 THR   A C     1 
ATOM   1434 O O     . THR   A 1 208 ? -12.63800 4.80000   21.60200 1.000 22.28495 ?  188 THR   A O     1 
ATOM   1435 C CB    . THR   A 1 208 ? -12.10000 2.86900   23.74300 1.000 23.23538 ?  188 THR   A CB    1 
ATOM   1436 O OG1   . THR   A 1 208 ? -11.98500 1.45500   24.00400 1.000 21.83499 ?  188 THR   A OG1   1 
ATOM   1437 C CG2   . THR   A 1 208 ? -11.83400 3.70600   25.02300 1.000 20.79335 ?  188 THR   A CG2   1 
ATOM   1438 N N     . ALA   A 1 209 ? -14.22800 5.53300   23.03300 1.000 23.37196 ?  189 ALA   A N     1 
ATOM   1439 C CA    . ALA   A 1 209 ? -14.08300 6.91500   22.58100 1.000 22.66867 ?  189 ALA   A CA    1 
ATOM   1440 C C     . ALA   A 1 209 ? -12.63600 7.37300   22.75100 1.000 23.51516 ?  189 ALA   A C     1 
ATOM   1441 O O     . ALA   A 1 209 ? -11.96500 7.02100   23.72600 1.000 22.17062 ?  189 ALA   A O     1 
ATOM   1442 C CB    . ALA   A 1 209 ? -15.01800 7.85100   23.36500 1.000 25.78598 ?  189 ALA   A CB    1 
ATOM   1443 N N     . LYS   A 1 210 ? -12.15700 8.17900   21.80300 1.000 23.14858 ?  190 LYS   A N     1 
ATOM   1444 C CA    . LYS   A 1 210 ? -10.73900 8.52900   21.80000 1.000 22.34847 ?  190 LYS   A CA    1 
ATOM   1445 C C     . LYS   A 1 210 ? -10.30200 9.23700   23.07500 1.000 25.06721 ?  190 LYS   A C     1 
ATOM   1446 O O     . LYS   A 1 210 ? -9.16500  9.03000   23.53100 1.000 22.39892 ?  190 LYS   A O     1 
ATOM   1447 C CB    . LYS   A 1 210 ? -10.40700 9.37500   20.56500 1.000 27.25927 ?  190 LYS   A CB    1 
ATOM   1448 C CG    . LYS   A 1 210 ? -8.91600  9.63700   20.45400 1.000 30.24827 ?  190 LYS   A CG    1 
ATOM   1449 C CD    . LYS   A 1 210 ? -8.49000  10.04900  19.06100 1.000 48.35838 ?  190 LYS   A CD    1 
ATOM   1450 C CE    . LYS   A 1 210 ? -7.24100  10.89400  19.15600 1.000 40.90215 ?  190 LYS   A CE    1 
ATOM   1451 N N     . LYS   A 1 211 ? -11.19500 10.03400  23.69300 1.000 25.20548 ?  191 LYS   A N     1 
ATOM   1452 C CA    . LYS   A 1 211 ? -10.85600 10.72200  24.93300 1.000 25.23715 ?  191 LYS   A CA    1 
ATOM   1453 C C     . LYS   A 1 211 ? -10.54800 9.75900   26.07200 1.000 24.76091 ?  191 LYS   A C     1 
ATOM   1454 O O     . LYS   A 1 211 ? -9.98300  10.18400  27.08600 1.000 24.71228 ?  191 LYS   A O     1 
ATOM   1455 C CB    . LYS   A 1 211 ? -11.99800 11.65600  25.37500 1.000 29.70368 ?  191 LYS   A CB    1 
ATOM   1456 C CG    . LYS   A 1 211 ? -13.34900 10.96500  25.47400 1.000 33.22520 ?  191 LYS   A CG    1 
ATOM   1457 C CD    . LYS   A 1 211 ? -14.47400 11.88500  26.01000 1.000 45.83111 ?  191 LYS   A CD    1 
ATOM   1458 C CE    . LYS   A 1 211 ? -14.01200 12.72300  27.18900 1.000 45.88603 ?  191 LYS   A CE    1 
ATOM   1459 N N     . PHE   A 1 212 ? -10.90200 8.47200   25.93800 1.000 22.26157 ?  192 PHE   A N     1 
ATOM   1460 C CA    . PHE   A 1 212 ? -10.65700 7.50300   26.99900 1.000 22.18759 ?  192 PHE   A CA    1 
ATOM   1461 C C     . PHE   A 1 212 ? -9.52400  6.52500   26.67600 1.000 23.21199 ?  192 PHE   A C     1 
ATOM   1462 O O     . PHE   A 1 212 ? -9.21400  5.65400   27.51200 1.000 21.53771 ?  192 PHE   A O     1 
ATOM   1463 C CB    . PHE   A 1 212 ? -11.93400 6.71700   27.30300 1.000 20.54307 ?  192 PHE   A CB    1 
ATOM   1464 C CG    . PHE   A 1 212 ? -13.09300 7.59500   27.76400 1.000 20.82303 ?  192 PHE   A CG    1 
ATOM   1465 C CD1   . PHE   A 1 212 ? -12.91900 8.50700   28.80400 1.000 24.71249 ?  192 PHE   A CD1   1 
ATOM   1466 C CD2   . PHE   A 1 212 ? -14.32800 7.52400   27.12500 1.000 22.30348 ?  192 PHE   A CD2   1 
ATOM   1467 C CE1   . PHE   A 1 212 ? -13.99200 9.32700   29.22000 1.000 28.13277 ?  192 PHE   A CE1   1 
ATOM   1468 C CE2   . PHE   A 1 212 ? -15.40700 8.34200   27.52900 1.000 26.90169 ?  192 PHE   A CE2   1 
ATOM   1469 C CZ    . PHE   A 1 212 ? -15.24100 9.22800   28.56900 1.000 28.51385 ?  192 PHE   A CZ    1 
ATOM   1470 N N     . TRP   A 1 213 ? -8.89400  6.63800   25.49900 1.000 21.92332 ?  193 TRP   A N     1 
ATOM   1471 C CA    . TRP   A 1 213 ? -7.72300  5.79500   25.23200 1.000 22.23467 ?  193 TRP   A CA    1 
ATOM   1472 C C     . TRP   A 1 213 ? -6.64100  6.05100   26.27800 1.000 22.59783 ?  193 TRP   A C     1 
ATOM   1473 O O     . TRP   A 1 213 ? -6.33200  7.20500   26.59400 1.000 23.58653 ?  193 TRP   A O     1 
ATOM   1474 C CB    . TRP   A 1 213 ? -7.14800  6.07500   23.84400 1.000 19.06753 ?  193 TRP   A CB    1 
ATOM   1475 C CG    . TRP   A 1 213 ? -8.02700  5.79400   22.68200 1.000 19.73144 ?  193 TRP   A CG    1 
ATOM   1476 C CD1   . TRP   A 1 213 ? -9.31200  5.29800   22.69200 1.000 20.31349 ?  193 TRP   A CD1   1 
ATOM   1477 C CD2   . TRP   A 1 213 ? -7.66900  5.96400   21.30500 1.000 17.95022 ?  193 TRP   A CD2   1 
ATOM   1478 N NE1   . TRP   A 1 213 ? -9.76900  5.17200   21.39700 1.000 19.10954 ?  193 TRP   A NE1   1 
ATOM   1479 C CE2   . TRP   A 1 213 ? -8.77900  5.57000   20.53100 1.000 19.86630 ?  193 TRP   A CE2   1 
ATOM   1480 C CE3   . TRP   A 1 213 ? -6.51300  6.41700   20.65400 1.000 21.26624 ?  193 TRP   A CE3   1 
ATOM   1481 C CZ2   . TRP   A 1 213 ? -8.77100  5.62100   19.12700 1.000 23.04020 ?  193 TRP   A CZ2   1 
ATOM   1482 C CZ3   . TRP   A 1 213 ? -6.50800  6.46900   19.25700 1.000 21.68727 ?  193 TRP   A CZ3   1 
ATOM   1483 C CH2   . TRP   A 1 213 ? -7.62900  6.08600   18.51400 1.000 20.52547 ?  193 TRP   A CH2   1 
ATOM   1484 N N     . ILE   A 1 214 ? -6.05800  4.97500   26.81900 1.000 20.32712 ?  194 ILE   A N     1 
ATOM   1485 C CA    . ILE   A 1 214 ? -4.98500  5.11800   27.80200 1.000 22.49190 ?  194 ILE   A CA    1 
ATOM   1486 C C     . ILE   A 1 214 ? -3.67100  5.56400   27.16200 1.000 27.48733 ?  194 ILE   A C     1 
ATOM   1487 O O     . ILE   A 1 214 ? -2.82400  6.16100   27.84400 1.000 23.49352 ?  194 ILE   A O     1 
ATOM   1488 C CB    . ILE   A 1 214 ? -4.82200  3.79800   28.58600 1.000 19.89186 ?  194 ILE   A CB    1 
ATOM   1489 C CG1   . ILE   A 1 214 ? -6.13300  3.43600   29.29500 1.000 25.10686 ?  194 ILE   A CG1   1 
ATOM   1490 C CG2   . ILE   A 1 214 ? -3.66800  3.86500   29.58600 1.000 22.05930 ?  194 ILE   A CG2   1 
ATOM   1491 C CD1   . ILE   A 1 214 ? -6.62300  4.50600   30.26600 1.000 27.65295 ?  194 ILE   A CD1   1 
ATOM   1492 N N     . GLY   A 1 215 ? -3.49100  5.30900   25.87300 1.000 22.43374 ?  195 GLY   A N     1 
ATOM   1493 C CA    . GLY   A 1 215 ? -2.30700  5.72000   25.14800 1.000 22.95461 ?  195 GLY   A CA    1 
ATOM   1494 C C     . GLY   A 1 215 ? -2.58400  5.70800   23.66100 1.000 20.01458 ?  195 GLY   A C     1 
ATOM   1495 O O     . GLY   A 1 215 ? -3.72300  5.52600   23.22400 1.000 20.89233 ?  195 GLY   A O     1 
ATOM   1496 N N     . GLY   A 1 216 ? -1.52400  5.90600   22.87100 1.000 19.11479 ?  196 GLY   A N     1 
ATOM   1497 C CA    . GLY   A 1 216 ? -1.70600  5.91700   21.43000 1.000 19.56199 ?  196 GLY   A CA    1 
ATOM   1498 C C     . GLY   A 1 216 ? -2.31600  7.19000   20.89200 1.000 20.62511 ?  196 GLY   A C     1 
ATOM   1499 O O     . GLY   A 1 216 ? -3.02500  7.16600   19.87300 1.000 20.35863 ?  196 GLY   A O     1 
ATOM   1500 N N     . TYR   A 1 217 ? -2.05700  8.27800   21.59700 1.000 19.18290 ?  197 TYR   A N     1 
ATOM   1501 C CA    . TYR   A 1 217 ? -2.62100  9.57400   21.18100 1.000 23.32382 ?  197 TYR   A CA    1 
ATOM   1502 C C     . TYR   A 1 217 ? -1.63000  10.71200  21.43200 1.000 19.11235 ?  197 TYR   A C     1 
ATOM   1503 O O     . TYR   A 1 217 ? -0.71700  10.56200  22.22700 1.000 20.94209 ?  197 TYR   A O     1 
ATOM   1504 C CB    . TYR   A 1 217 ? -3.93600  9.84400   21.91700 1.000 21.06243 ?  197 TYR   A CB    1 
ATOM   1505 C CG    . TYR   A 1 217 ? -3.82100  10.04300  23.40400 1.000 23.65999 ?  197 TYR   A CG    1 
ATOM   1506 C CD1   . TYR   A 1 217 ? -3.63300  11.30200  23.94600 1.000 23.18152 ?  197 TYR   A CD1   1 
ATOM   1507 C CD2   . TYR   A 1 217 ? -3.91700  8.97300   24.27300 1.000 24.53670 ?  197 TYR   A CD2   1 
ATOM   1508 C CE1   . TYR   A 1 217 ? -3.52500  11.48900  25.31200 1.000 26.72756 ?  197 TYR   A CE1   1 
ATOM   1509 C CE2   . TYR   A 1 217 ? -3.81100  9.14200   25.64100 1.000 24.46847 ?  197 TYR   A CE2   1 
ATOM   1510 C CZ    . TYR   A 1 217 ? -3.61600  10.40500  26.16400 1.000 29.88391 ?  197 TYR   A CZ    1 
ATOM   1511 O OH    . TYR   A 1 217 ? -3.50700  10.57400  27.51700 1.000 27.79172 ?  197 TYR   A OH    1 
ATOM   1512 N N     . VAL   A 1 218 ? -1.84700  11.81500  20.72900 1.000 21.16937 ?  198 VAL   A N     1 
ATOM   1513 C CA    . VAL   A 1 218 ? -1.05000  13.04200  20.97300 1.000 21.64450 ?  198 VAL   A CA    1 
ATOM   1514 C C     . VAL   A 1 218 ? -1.87400  13.89800  21.93500 1.000 19.52602 ?  198 VAL   A C     1 
ATOM   1515 O O     . VAL   A 1 218 ? -3.03600  14.15900  21.64400 1.000 24.32542 ?  198 VAL   A O     1 
ATOM   1516 C CB    . VAL   A 1 218 ? -0.76600  13.78600  19.65900 1.000 24.22535 ?  198 VAL   A CB    1 
ATOM   1517 C CG1   . VAL   A 1 218 ? 0.03300   15.05700  19.89100 1.000 22.00816 ?  198 VAL   A CG1   1 
ATOM   1518 C CG2   . VAL   A 1 218 ? -0.08000  12.88900  18.64400 1.000 22.98479 ?  198 VAL   A CG2   1 
ATOM   1519 N N     . ASP   A 1 219 ? -1.28100  14.29600  23.05200 1.000 22.18398 ?  199 ASP   A N     1 
ATOM   1520 C CA    . ASP   A 1 219 ? -2.04700  15.06200  24.06600 1.000 21.81088 ?  199 ASP   A CA    1 
ATOM   1521 C C     . ASP   A 1 219 ? -2.22200  16.52500  23.63400 1.000 26.07943 ?  199 ASP   A C     1 
ATOM   1522 O O     . ASP   A 1 219 ? -1.68900  16.90700  22.59300 1.000 24.69122 ?  199 ASP   A O     1 
ATOM   1523 C CB    . ASP   A 1 219 ? -1.45400  14.90000  25.46700 1.000 21.17629 ?  199 ASP   A CB    1 
ATOM   1524 C CG    . ASP   A 1 219 ? -0.05900  15.46000  25.69300 1.000 34.91107 ?  199 ASP   A CG    1 
ATOM   1525 O OD1   . ASP   A 1 219 ? 0.43400   16.21400  24.84400 1.000 31.69649 ?  199 ASP   A OD1   1 
ATOM   1526 O OD2   . ASP   A 1 219 ? 0.51700   15.13200  26.73900 1.000 31.54359 -1 199 ASP   A OD2   1 
ATOM   1527 N N     . GLU   A 1 220 ? -2.93100  17.30400  24.44700 1.000 23.35975 ?  200 GLU   A N     1 
ATOM   1528 C CA    . GLU   A 1 220 ? -3.25400  18.70400  24.07700 1.000 24.81583 ?  200 GLU   A CA    1 
ATOM   1529 C C     . GLU   A 1 220 ? -1.99200  19.56800  24.06900 1.000 31.21304 ?  200 GLU   A C     1 
ATOM   1530 O O     . GLU   A 1 220 ? -2.06600  20.66800  23.52300 1.000 32.97457 ?  200 GLU   A O     1 
ATOM   1531 C CB    . GLU   A 1 220 ? -4.30700  19.23900  25.05100 1.000 29.60086 ?  200 GLU   A CB    1 
ATOM   1532 C CG    . GLU   A 1 220 ? -3.88100  19.14200  26.50200 1.000 40.20617 ?  200 GLU   A CG    1 
ATOM   1533 N N     . ASN   A 1 221 ? -0.91100  19.11100  24.69300 1.000 25.02859 ?  201 ASN   A N     1 
ATOM   1534 C CA    . ASN   A 1 221 ? 0.35900   19.81900  24.65000 1.000 22.94245 ?  201 ASN   A CA    1 
ATOM   1535 C C     . ASN   A 1 221 ? 1.32700   19.25800  23.61300 1.000 27.89699 ?  201 ASN   A C     1 
ATOM   1536 O O     . ASN   A 1 221 ? 2.50900   19.61100  23.62600 1.000 23.82667 ?  201 ASN   A O     1 
ATOM   1537 C CB    . ASN   A 1 221 ? 0.98400   19.79800  26.02900 1.000 24.38604 ?  201 ASN   A CB    1 
ATOM   1538 C CG    . ASN   A 1 221 ? 0.08900   20.47400  27.04700 1.000 37.92303 ?  201 ASN   A CG    1 
ATOM   1539 O OD1   . ASN   A 1 221 ? -0.43300  21.57400  26.79900 1.000 32.95775 ?  201 ASN   A OD1   1 
ATOM   1540 N ND2   . ASN   A 1 221 ? -0.15800  19.79600  28.16000 1.000 31.87537 ?  201 ASN   A ND2   1 
ATOM   1541 N N     . GLY   A 1 222 ? 0.85100   18.41400  22.70400 1.000 27.43826 ?  202 GLY   A N     1 
ATOM   1542 C CA    . GLY   A 1 222 ? 1.68900   17.94400  21.61300 1.000 22.43119 ?  202 GLY   A CA    1 
ATOM   1543 C C     . GLY   A 1 222 ? 2.62700   16.80000  21.93800 1.000 22.07926 ?  202 GLY   A C     1 
ATOM   1544 O O     . GLY   A 1 222 ? 3.47600   16.47800  21.10300 1.000 21.55474 ?  202 GLY   A O     1 
ATOM   1545 N N     . LYS   A 1 223 ? 2.49900   16.16700  23.10400 1.000 21.96929 ?  203 LYS   A N     1 
ATOM   1546 C CA    . LYS   A 1 223 ? 3.37200   15.05400  23.46400 1.000 20.38844 ?  203 LYS   A CA    1 
ATOM   1547 C C     . LYS   A 1 223 ? 2.68800   13.74800  23.08000 1.000 24.59264 ?  203 LYS   A C     1 
ATOM   1548 O O     . LYS   A 1 223 ? 1.46800   13.62700  23.18400 1.000 24.90374 ?  203 LYS   A O     1 
ATOM   1549 C CB    . LYS   A 1 223 ? 3.63500   15.05500  24.96400 1.000 21.16201 ?  203 LYS   A CB    1 
ATOM   1550 C CG    . LYS   A 1 223 ? 4.63100   16.13800  25.43200 1.000 26.85570 ?  203 LYS   A CG    1 
ATOM   1551 C CD    . LYS   A 1 223 ? 4.92900   15.94900  26.91300 1.000 35.72287 ?  203 LYS   A CD    1 
ATOM   1552 C CE    . LYS   A 1 223 ? 5.39400   17.23400  27.57900 1.000 46.37716 ?  203 LYS   A CE    1 
ATOM   1553 N NZ    . LYS   A 1 223 ? 6.54500   16.94900  28.49300 1.000 46.14201 ?  203 LYS   A NZ    1 
ATOM   1554 N N     . GLU   A 1 224 ? 3.48500   12.77000  22.65200 1.000 23.67426 ?  204 GLU   A N     1 
ATOM   1555 C CA    . GLU   A 1 224 ? 2.94800   11.45600  22.29900 1.000 24.48327 ?  204 GLU   A CA    1 
ATOM   1556 C C     . GLU   A 1 224 ? 2.81000   10.64800  23.57700 1.000 24.21290 ?  204 GLU   A C     1 
ATOM   1557 O O     . GLU   A 1 224 ? 3.73200   10.63100  24.39300 1.000 25.73875 ?  204 GLU   A O     1 
ATOM   1558 C CB    . GLU   A 1 224 ? 3.88600   10.76000  21.31500 1.000 25.86067 ?  204 GLU   A CB    1 
ATOM   1559 C CG    . GLU   A 1 224 ? 3.86000   11.43300  19.95300 1.000 25.21374 ?  204 GLU   A CG    1 
ATOM   1560 C CD    . GLU   A 1 224 ? 4.38100   10.55600  18.84100 1.000 36.42762 ?  204 GLU   A CD    1 
ATOM   1561 O OE1   . GLU   A 1 224 ? 5.18300   9.64100   19.13500 1.000 36.22455 ?  204 GLU   A OE1   1 
ATOM   1562 O OE2   . GLU   A 1 224 ? 4.03600   10.81700  17.67000 1.000 52.46598 -1 204 GLU   A OE2   1 
ATOM   1563 N N     . VAL   A 1 225 ? 1.65100   10.02200  23.78100 1.000 19.91501 ?  205 VAL   A N     1 
ATOM   1564 C CA    . VAL   A 1 225 ? 1.38900   9.25100   25.00100 1.000 17.93428 ?  205 VAL   A CA    1 
ATOM   1565 C C     . VAL   A 1 225 ? 1.35900   7.78100   24.61500 1.000 21.97023 ?  205 VAL   A C     1 
ATOM   1566 O O     . VAL   A 1 225 ? 0.51200   7.35600   23.82100 1.000 21.11048 ?  205 VAL   A O     1 
ATOM   1567 C CB    . VAL   A 1 225 ? 0.07500   9.66400   25.67900 1.000 23.66008 ?  205 VAL   A CB    1 
ATOM   1568 C CG1   . VAL   A 1 225 ? -0.16000  8.85200   26.96600 1.000 22.40487 ?  205 VAL   A CG1   1 
ATOM   1569 C CG2   . VAL   A 1 225 ? 0.12900   11.17500  26.02000 1.000 28.47327 ?  205 VAL   A CG2   1 
ATOM   1570 N N     . SER   A 1 226 ? 2.27100   7.01700   25.18000 1.000 20.03766 ?  206 SER   A N     1 
ATOM   1571 C CA    . SER   A 1 226 ? 2.26300   5.58000   24.97000 1.000 20.98455 ?  206 SER   A CA    1 
ATOM   1572 C C     . SER   A 1 226 ? 1.35200   4.93100   26.00300 1.000 21.47191 ?  206 SER   A C     1 
ATOM   1573 O O     . SER   A 1 226 ? 1.20900   5.42600   27.12600 1.000 20.79173 ?  206 SER   A O     1 
ATOM   1574 C CB    . SER   A 1 226 ? 3.68100   5.04100   25.06000 1.000 29.19812 ?  206 SER   A CB    1 
ATOM   1575 O OG    . SER   A 1 226 ? 3.96900   4.53300   26.33500 1.000 30.73722 ?  206 SER   A OG    1 
ATOM   1576 N N     . THR   A 1 227 ? 0.70700   3.82300   25.61200 1.000 21.87667 ?  207 THR   A N     1 
ATOM   1577 C CA    . THR   A 1 227 ? -0.21700  3.18600   26.55000 1.000 21.32393 ?  207 THR   A CA    1 
ATOM   1578 C C     . THR   A 1 227 ? 0.47900   2.70100   27.80800 1.000 19.09207 ?  207 THR   A C     1 
ATOM   1579 O O     . THR   A 1 227 ? -0.07700  2.81200   28.90100 1.000 21.54489 ?  207 THR   A O     1 
ATOM   1580 C CB    . THR   A 1 227 ? -0.98200  2.03800   25.88400 1.000 19.92194 ?  207 THR   A CB    1 
ATOM   1581 O OG1   . THR   A 1 227 ? -1.59700  2.51500   24.67800 1.000 20.38043 ?  207 THR   A OG1   1 
ATOM   1582 C CG2   . THR   A 1 227 ? -2.02500  1.49800   26.84700 1.000 16.84960 ?  207 THR   A CG2   1 
ATOM   1583 N N     . LEU   A 1 228 ? 1.67400   2.12500   27.68300 1.000 19.88787 ?  208 LEU   A N     1 
ATOM   1584 C CA    . LEU   A 1 228 ? 2.36100   1.66700   28.88600 1.000 20.82167 ?  208 LEU   A CA    1 
ATOM   1585 C C     . LEU   A 1 228 ? 2.65000   2.83300   29.82900 1.000 19.71457 ?  208 LEU   A C     1 
ATOM   1586 O O     . LEU   A 1 228 ? 2.53500   2.69700   31.04900 1.000 21.92489 ?  208 LEU   A O     1 
ATOM   1587 C CB    . LEU   A 1 228 ? 3.64800   0.94700   28.50500 1.000 22.99275 ?  208 LEU   A CB    1 
ATOM   1588 C CG    . LEU   A 1 228 ? 4.44500   0.43700   29.71000 1.000 24.68664 ?  208 LEU   A CG    1 
ATOM   1589 C CD1   . LEU   A 1 228 ? 3.59100   -0.51400  30.54000 1.000 28.06585 ?  208 LEU   A CD1   1 
ATOM   1590 C CD2   . LEU   A 1 228 ? 5.72700   -0.22800  29.22700 1.000 27.71475 ?  208 LEU   A CD2   1 
ATOM   1591 N N     . GLU   A 1 229 ? 2.98600   3.99300   29.27700 1.000 23.00713 ?  209 GLU   A N     1 
ATOM   1592 C CA    . GLU   A 1 229 ? 3.18000   5.16300   30.13500 1.000 26.55644 ?  209 GLU   A CA    1 
ATOM   1593 C C     . GLU   A 1 229 ? 1.87000   5.56700   30.80900 1.000 23.83998 ?  209 GLU   A C     1 
ATOM   1594 O O     . GLU   A 1 229 ? 1.85100   5.84700   32.01800 1.000 27.41609 ?  209 GLU   A O     1 
ATOM   1595 C CB    . GLU   A 1 229 ? 3.76300   6.31500   29.31700 1.000 29.21442 ?  209 GLU   A CB    1 
ATOM   1596 C CG    . GLU   A 1 229 ? 5.25700   6.12900   29.02500 1.000 46.95702 ?  209 GLU   A CG    1 
ATOM   1597 C CD    . GLU   A 1 229 ? 6.08100   5.69600   30.25000 1.000 66.33854 ?  209 GLU   A CD    1 
ATOM   1598 O OE1   . GLU   A 1 229 ? 6.18000   6.47900   31.23500 1.000 56.59392 ?  209 GLU   A OE1   1 
ATOM   1599 O OE2   . GLU   A 1 229 ? 6.63100   4.56100   30.21200 1.000 54.91961 -1 209 GLU   A OE2   1 
ATOM   1600 N N     . GLY   A 1 230 ? 0.75400   5.55000   30.06400 1.000 20.73551 ?  210 GLY   A N     1 
ATOM   1601 C CA    . GLY   A 1 230 ? -0.53400  5.85300   30.66400 1.000 22.51950 ?  210 GLY   A CA    1 
ATOM   1602 C C     . GLY   A 1 230 ? -0.90600  4.85900   31.74700 1.000 24.15309 ?  210 GLY   A C     1 
ATOM   1603 O O     . GLY   A 1 230 ? -1.49800  5.22200   32.77300 1.000 24.24631 ?  210 GLY   A O     1 
ATOM   1604 N N     . LEU   A 1 231 ? -0.57100  3.58600   31.53200 1.000 22.76206 ?  211 LEU   A N     1 
ATOM   1605 C CA    . LEU   A 1 231 ? -0.81500  2.57400   32.54800 1.000 23.97017 ?  211 LEU   A CA    1 
ATOM   1606 C C     . LEU   A 1 231 ? 0.01000   2.85700   33.80200 1.000 22.60282 ?  211 LEU   A C     1 
ATOM   1607 O O     . LEU   A 1 231 ? -0.49600  2.75300   34.91900 1.000 24.02260 ?  211 LEU   A O     1 
ATOM   1608 C CB    . LEU   A 1 231 ? -0.50100  1.17800   31.98500 1.000 19.97425 ?  211 LEU   A CB    1 
ATOM   1609 C CG    . LEU   A 1 231 ? -1.54400  0.64100   30.99200 1.000 21.74745 ?  211 LEU   A CG    1 
ATOM   1610 C CD1   . LEU   A 1 231 ? -0.97600  -0.68200  30.38400 1.000 20.75203 ?  211 LEU   A CD1   1 
ATOM   1611 C CD2   . LEU   A 1 231 ? -2.93300  0.38200   31.64700 1.000 20.66468 ?  211 LEU   A CD2   1 
ATOM   1612 N N     . LYS   A 1 232 ? 1.29500   3.19500   33.63600 1.000 23.01565 ?  212 LYS   A N     1 
ATOM   1613 C CA    . LYS   A 1 232 ? 2.11700   3.53800   34.80200 1.000 26.86014 ?  212 LYS   A CA    1 
ATOM   1614 C C     . LYS   A 1 232 ? 1.52000   4.70900   35.58900 1.000 25.04117 ?  212 LYS   A C     1 
ATOM   1615 O O     . LYS   A 1 232 ? 1.47500   4.67500   36.82800 1.000 27.07604 ?  212 LYS   A O     1 
ATOM   1616 C CB    . LYS   A 1 232 ? 3.53500   3.87800   34.35400 1.000 25.01935 ?  212 LYS   A CB    1 
ATOM   1617 C CG    . LYS   A 1 232 ? 4.29400   2.73500   33.68500 1.000 30.23577 ?  212 LYS   A CG    1 
ATOM   1618 C CD    . LYS   A 1 232 ? 5.78700   3.02100   33.65900 1.000 35.03850 ?  212 LYS   A CD    1 
ATOM   1619 C CE    . LYS   A 1 232 ? 6.49500   2.06100   32.71100 1.000 47.85731 ?  212 LYS   A CE    1 
ATOM   1620 N NZ    . LYS   A 1 232 ? 7.92900   2.39700   32.44600 1.000 50.01496 ?  212 LYS   A NZ    1 
ATOM   1621 N N     . GLU   A 1 233 ? 1.07200   5.75600   34.88900 1.000 25.55550 ?  213 GLU   A N     1 
ATOM   1622 C CA    . GLU   A 1 233 ? 0.51200   6.91800   35.57600 1.000 30.20786 ?  213 GLU   A CA    1 
ATOM   1623 C C     . GLU   A 1 233 ? -0.68900  6.52600   36.42900 1.000 32.35014 ?  213 GLU   A C     1 
ATOM   1624 O O     . GLU   A 1 233 ? -0.84500  7.01200   37.55500 1.000 32.23572 ?  213 GLU   A O     1 
ATOM   1625 C CB    . GLU   A 1 233 ? 0.12500   7.99600   34.55600 1.000 29.08086 ?  213 GLU   A CB    1 
ATOM   1626 C CG    . GLU   A 1 233 ? -0.49700  9.24600   35.16500 1.000 44.64174 ?  213 GLU   A CG    1 
ATOM   1627 N N     . ILE   A 1 234 ? -1.54000  5.63500   35.92500 1.000 22.35024 ?  214 ILE   A N     1 
ATOM   1628 C CA    . ILE   A 1 234 ? -2.72000  5.22600   36.68200 1.000 22.80794 ?  214 ILE   A CA    1 
ATOM   1629 C C     . ILE   A 1 234 ? -2.35200  4.22800   37.76900 1.000 29.98788 ?  214 ILE   A C     1 
ATOM   1630 O O     . ILE   A 1 234 ? -2.80100  4.33200   38.91700 1.000 29.65244 ?  214 ILE   A O     1 
ATOM   1631 C CB    . ILE   A 1 234 ? -3.78200  4.63600   35.72900 1.000 26.63547 ?  214 ILE   A CB    1 
ATOM   1632 C CG1   . ILE   A 1 234 ? -4.27800  5.71200   34.76100 1.000 32.96496 ?  214 ILE   A CG1   1 
ATOM   1633 C CG2   . ILE   A 1 234 ? -4.93600  3.97300   36.50800 1.000 27.75289 ?  214 ILE   A CG2   1 
ATOM   1634 C CD1   . ILE   A 1 234 ? -5.11800  5.16600   33.62900 1.000 34.33114 ?  214 ILE   A CD1   1 
ATOM   1635 N N     . LEU   A 1 235 ? -1.56100  3.21800   37.42000 1.000 22.99137 ?  215 LEU   A N     1 
ATOM   1636 C CA    . LEU   A 1 235 ? -1.41500  2.07400   38.31200 1.000 23.47472 ?  215 LEU   A CA    1 
ATOM   1637 C C     . LEU   A 1 235 ? -0.32500  2.26200   39.36000 1.000 27.96679 ?  215 LEU   A C     1 
ATOM   1638 O O     . LEU   A 1 235 ? -0.36200  1.58900   40.39500 1.000 27.32011 ?  215 LEU   A O     1 
ATOM   1639 C CB    . LEU   A 1 235 ? -1.14700  0.80400   37.48900 1.000 22.58018 ?  215 LEU   A CB    1 
ATOM   1640 C CG    . LEU   A 1 235 ? -2.33500  0.36700   36.61300 1.000 22.81490 ?  215 LEU   A CG    1 
ATOM   1641 C CD1   . LEU   A 1 235 ? -1.92100  -0.79000  35.73300 1.000 22.12979 ?  215 LEU   A CD1   1 
ATOM   1642 C CD2   . LEU   A 1 235 ? -3.51300  -0.09100  37.49300 1.000 21.65747 ?  215 LEU   A CD2   1 
ATOM   1643 N N     . GLU   A 1 236 ? 0.61800   3.18000   39.14900 1.000 31.25968 ?  216 GLU   A N     1 
ATOM   1644 C CA    . GLU   A 1 236 ? 1.69000   3.29000   40.13300 1.000 29.27811 ?  216 GLU   A CA    1 
ATOM   1645 C C     . GLU   A 1 236 ? 1.22900   3.94900   41.43200 1.000 31.95308 ?  216 GLU   A C     1 
ATOM   1646 O O     . GLU   A 1 236 ? 1.97500   3.91600   42.41400 1.000 32.85708 ?  216 GLU   A O     1 
ATOM   1647 C CB    . GLU   A 1 236 ? 2.89100   4.00200   39.50100 1.000 30.97795 ?  216 GLU   A CB    1 
ATOM   1648 C CG    . GLU   A 1 236 ? 3.69300   2.97100   38.65900 1.000 37.16377 ?  216 GLU   A CG    1 
ATOM   1649 C CD    . GLU   A 1 236 ? 4.88500   3.52300   37.88400 1.000 49.67361 ?  216 GLU   A CD    1 
ATOM   1650 O OE1   . GLU   A 1 236 ? 5.03100   4.75700   37.77600 1.000 50.92149 ?  216 GLU   A OE1   1 
ATOM   1651 O OE2   . GLU   A 1 236 ? 5.67600   2.69800   37.36900 1.000 42.58094 -1 216 GLU   A OE2   1 
ATOM   1652 N N     . ILE   A 1 237 ? -0.00800  4.44700   41.48600 1.000 29.67720 ?  217 ILE   A N     1 
ATOM   1653 C CA    . ILE   A 1 237 ? -0.59600  4.88300   42.75200 1.000 29.13397 ?  217 ILE   A CA    1 
ATOM   1654 C C     . ILE   A 1 237 ? -0.71200  3.72600   43.73800 1.000 37.10233 ?  217 ILE   A C     1 
ATOM   1655 O O     . ILE   A 1 237 ? -0.46500  3.89700   44.93800 1.000 36.65732 ?  217 ILE   A O     1 
ATOM   1656 C CB    . ILE   A 1 237 ? -1.96800  5.53100   42.50400 1.000 32.95437 ?  217 ILE   A CB    1 
ATOM   1657 C CG1   . ILE   A 1 237 ? -1.85700  6.62800   41.43000 1.000 42.14599 ?  217 ILE   A CG1   1 
ATOM   1658 C CG2   . ILE   A 1 237 ? -2.53900  6.06100   43.81300 1.000 36.22211 ?  217 ILE   A CG2   1 
ATOM   1659 C CD1   . ILE   A 1 237 ? -1.65800  8.00700   41.98600 1.000 51.90293 ?  217 ILE   A CD1   1 
ATOM   1660 N N     . HIS   A 1 238 ? -1.13400  2.53900   43.26800 1.000 26.99766 ?  218 HIS   A N     1 
ATOM   1661 C CA    . HIS   A 1 238 ? -1.36100  1.39800   44.15700 1.000 29.79562 ?  218 HIS   A CA    1 
ATOM   1662 C C     . HIS   A 1 238 ? -0.54500  0.15800   43.82300 1.000 32.17981 ?  218 HIS   A C     1 
ATOM   1663 O O     . HIS   A 1 238 ? -0.62000  -0.82900  44.57200 1.000 31.02399 ?  218 HIS   A O     1 
ATOM   1664 C CB    . HIS   A 1 238 ? -2.84900  1.03200   44.17700 1.000 30.19981 ?  218 HIS   A CB    1 
ATOM   1665 C CG    . HIS   A 1 238 ? -3.71200  2.10200   44.76400 1.000 31.65096 ?  218 HIS   A CG    1 
ATOM   1666 N ND1   . HIS   A 1 238 ? -3.69200  2.41600   46.10700 1.000 38.65707 ?  218 HIS   A ND1   1 
ATOM   1667 C CD2   . HIS   A 1 238 ? -4.59400  2.95200   44.19100 1.000 33.78673 ?  218 HIS   A CD2   1 
ATOM   1668 C CE1   . HIS   A 1 238 ? -4.53700  3.40500   46.33900 1.000 35.44167 ?  218 HIS   A CE1   1 
ATOM   1669 N NE2   . HIS   A 1 238 ? -5.09400  3.75200   45.19200 1.000 35.02988 ?  218 HIS   A NE2   1 
ATOM   1670 N N     . PHE   A 1 239 ? 0.25100   0.18100   42.75300 1.000 29.79022 ?  219 PHE   A N     1 
ATOM   1671 C CA    . PHE   A 1 239 ? 0.99800   -0.98200  42.29400 1.000 29.10007 ?  219 PHE   A CA    1 
ATOM   1672 C C     . PHE   A 1 239 ? 2.44700   -0.60500  42.02000 1.000 25.92467 ?  219 PHE   A C     1 
ATOM   1673 O O     . PHE   A 1 239 ? 2.77200   0.55000   41.70700 1.000 30.17869 ?  219 PHE   A O     1 
ATOM   1674 C CB    . PHE   A 1 239 ? 0.44500   -1.57400  40.97500 1.000 27.23772 ?  219 PHE   A CB    1 
ATOM   1675 C CG    . PHE   A 1 239 ? -0.95600  -2.09800  41.05300 1.000 26.51463 ?  219 PHE   A CG    1 
ATOM   1676 C CD1   . PHE   A 1 239 ? -2.04000  -1.24500  40.89000 1.000 26.32313 ?  219 PHE   A CD1   1 
ATOM   1677 C CD2   . PHE   A 1 239 ? -1.19400  -3.45700  41.24100 1.000 24.63717 ?  219 PHE   A CD2   1 
ATOM   1678 C CE1   . PHE   A 1 239 ? -3.35400  -1.73000  40.92800 1.000 24.73693 ?  219 PHE   A CE1   1 
ATOM   1679 C CE2   . PHE   A 1 239 ? -2.50600  -3.93900  41.28500 1.000 26.79896 ?  219 PHE   A CE2   1 
ATOM   1680 C CZ    . PHE   A 1 239 ? -3.57800  -3.07800  41.13900 1.000 24.90744 ?  219 PHE   A CZ    1 
ATOM   1681 N N     . GLU   A 1 240 ? 3.30400   -1.61800  42.06000 1.000 27.14929 ?  220 GLU   A N     1 
ATOM   1682 C CA    . GLU   A 1 240 ? 4.64700   -1.53300  41.51100 1.000 30.70631 ?  220 GLU   A CA    1 
ATOM   1683 C C     . GLU   A 1 240 ? 4.71300   -2.35100  40.22200 1.000 26.22667 ?  220 GLU   A C     1 
ATOM   1684 O O     . GLU   A 1 240 ? 4.27900   -3.50900  40.19000 1.000 29.61097 ?  220 GLU   A O     1 
ATOM   1685 C CB    . GLU   A 1 240 ? 5.67200   -2.03600  42.53300 1.000 32.32652 ?  220 GLU   A CB    1 
ATOM   1686 C CG    . GLU   A 1 240 ? 7.00400   -2.43000  41.94200 1.000 50.19705 ?  220 GLU   A CG    1 
ATOM   1687 C CD    . GLU   A 1 240 ? 7.94400   -3.02600  42.97700 1.000 60.86159 ?  220 GLU   A CD    1 
ATOM   1688 O OE1   . GLU   A 1 240 ? 7.44300   -3.62500  43.95500 1.000 56.93393 ?  220 GLU   A OE1   1 
ATOM   1689 O OE2   . GLU   A 1 240 ? 9.17700   -2.88700  42.81000 1.000 62.06844 -1 220 GLU   A OE2   1 
ATOM   1690 N N     . LEU   A 1 241 ? 5.25600   -1.75800  39.16800 1.000 26.79762 ?  221 LEU   A N     1 
ATOM   1691 C CA    . LEU   A 1 241 ? 5.48900   -2.49500  37.93100 1.000 26.03716 ?  221 LEU   A CA    1 
ATOM   1692 C C     . LEU   A 1 241 ? 6.67900   -3.42500  38.12200 1.000 33.85363 ?  221 LEU   A C     1 
ATOM   1693 O O     . LEU   A 1 241 ? 7.79600   -2.96500  38.37400 1.000 31.56229 ?  221 LEU   A O     1 
ATOM   1694 C CB    . LEU   A 1 241 ? 5.73600   -1.53700  36.77000 1.000 26.93585 ?  221 LEU   A CB    1 
ATOM   1695 C CG    . LEU   A 1 241 ? 5.97000   -2.19500  35.40200 1.000 29.50886 ?  221 LEU   A CG    1 
ATOM   1696 C CD1   . LEU   A 1 241 ? 4.83400   -3.13700  34.97900 1.000 21.63192 ?  221 LEU   A CD1   1 
ATOM   1697 C CD2   . LEU   A 1 241 ? 6.21100   -1.12200  34.36900 1.000 31.25539 ?  221 LEU   A CD2   1 
ATOM   1698 N N     . VAL   A 1 242 ? 6.44900   -4.72600  37.96300 1.000 25.99071 ?  222 VAL   A N     1 
ATOM   1699 C CA    . VAL   A 1 242 ? 7.44000   -5.75100  38.25500 1.000 26.37572 ?  222 VAL   A CA    1 
ATOM   1700 C C     . VAL   A 1 242 ? 8.12200   -6.24600  36.98200 1.000 28.73040 ?  222 VAL   A C     1 
ATOM   1701 O O     . VAL   A 1 242 ? 9.31500   -6.57100  36.99700 1.000 33.35238 ?  222 VAL   A O     1 
ATOM   1702 C CB    . VAL   A 1 242 ? 6.76800   -6.91200  39.02200 1.000 32.67772 ?  222 VAL   A CB    1 
ATOM   1703 C CG1   . VAL   A 1 242 ? 7.57600   -8.19400  38.90800 1.000 40.67009 ?  222 VAL   A CG1   1 
ATOM   1704 C CG2   . VAL   A 1 242 ? 6.55200   -6.51400  40.46500 1.000 45.60900 ?  222 VAL   A CG2   1 
ATOM   1705 N N     . ALA   A 1 243 ? 7.39100   -6.31900  35.87000 1.000 26.29279 ?  223 ALA   A N     1 
ATOM   1706 C CA    . ALA   A 1 243 ? 7.98200   -6.85600  34.64500 1.000 26.05735 ?  223 ALA   A CA    1 
ATOM   1707 C C     . ALA   A 1 243 ? 7.09000   -6.53400  33.45400 1.000 25.64298 ?  223 ALA   A C     1 
ATOM   1708 O O     . ALA   A 1 243 ? 5.88800   -6.31100  33.60600 1.000 25.57372 ?  223 ALA   A O     1 
ATOM   1709 C CB    . ALA   A 1 243 ? 8.17500   -8.37000  34.73400 1.000 28.54235 ?  223 ALA   A CB    1 
ATOM   1710 N N     . THR   A 1 244 ? 7.69900   -6.52100  32.26900 1.000 25.57075 ?  224 THR   A N     1 
ATOM   1711 C CA    . THR   A 1 244 ? 6.96300   -6.49900  31.00500 1.000 25.07645 ?  224 THR   A CA    1 
ATOM   1712 C C     . THR   A 1 244 ? 7.56200   -7.54800  30.07900 1.000 32.57726 ?  224 THR   A C     1 
ATOM   1713 O O     . THR   A 1 244 ? 8.76200   -7.84600  30.14300 1.000 28.87775 ?  224 THR   A O     1 
ATOM   1714 C CB    . THR   A 1 244 ? 7.03900   -5.13700  30.26800 1.000 29.22315 ?  224 THR   A CB    1 
ATOM   1715 O OG1   . THR   A 1 244 ? 8.40600   -4.76300  30.10700 1.000 31.23247 ?  224 THR   A OG1   1 
ATOM   1716 C CG2   . THR   A 1 244 ? 6.33100   -4.04900  31.07300 1.000 27.13694 ?  224 THR   A CG2   1 
ATOM   1717 N N     . GLU   A 1 245 ? 6.73100   -8.10900  29.20300 1.000 23.33463 ?  225 GLU   A N     1 
ATOM   1718 C CA    . GLU   A 1 245 ? 7.30000   -8.91200  28.13500 1.000 24.45660 ?  225 GLU   A CA    1 
ATOM   1719 C C     . GLU   A 1 245 ? 6.35900   -8.89300  26.93800 1.000 25.21750 ?  225 GLU   A C     1 
ATOM   1720 O O     . GLU   A 1 245 ? 5.16700   -8.60100  27.06300 1.000 25.42529 ?  225 GLU   A O     1 
ATOM   1721 C CB    . GLU   A 1 245 ? 7.61100   -10.34400 28.60700 1.000 29.52861 ?  225 GLU   A CB    1 
ATOM   1722 C CG    . GLU   A 1 245 ? 6.46400   -11.15800 29.08300 1.000 30.53418 ?  225 GLU   A CG    1 
ATOM   1723 C CD    . GLU   A 1 245 ? 6.93500   -12.54700 29.56100 1.000 36.38347 ?  225 GLU   A CD    1 
ATOM   1724 O OE1   . GLU   A 1 245 ? 7.22500   -13.39200 28.70300 1.000 34.63451 ?  225 GLU   A OE1   1 
ATOM   1725 O OE2   . GLU   A 1 245 ? 7.02000   -12.79100 30.78500 1.000 35.87479 -1 225 GLU   A OE2   1 
ATOM   1726 N N     . ASP   A 1 246 ? 6.92400   -9.17300  25.76700 1.000 22.59704 ?  226 ASP   A N     1 
ATOM   1727 C CA    . ASP   A 1 246 ? 6.14600   -9.25600  24.53400 1.000 23.51539 ?  226 ASP   A CA    1 
ATOM   1728 C C     . ASP   A 1 246 ? 5.73300   -10.69900 24.28500 1.000 29.55731 ?  226 ASP   A C     1 
ATOM   1729 O O     . ASP   A 1 246 ? 6.56000   -11.60500 24.41200 1.000 26.62786 ?  226 ASP   A O     1 
ATOM   1730 C CB    . ASP   A 1 246 ? 6.95800   -8.73900  23.35500 1.000 26.59423 ?  226 ASP   A CB    1 
ATOM   1731 C CG    . ASP   A 1 246 ? 6.96300   -7.21300  23.27100 1.000 31.91547 ?  226 ASP   A CG    1 
ATOM   1732 O OD1   . ASP   A 1 246 ? 6.10300   -6.53400  23.88000 1.000 27.10714 ?  226 ASP   A OD1   1 
ATOM   1733 O OD2   . ASP   A 1 246 ? 7.85000   -6.69800  22.58100 1.000 39.63320 -1 226 ASP   A OD2   1 
ATOM   1734 N N     . ILE   A 1 247 ? 4.46200   -10.90800 23.93400 1.000 21.03536 ?  227 ILE   A N     1 
ATOM   1735 C CA    . ILE   A 1 247 ? 3.90200   -12.24400 23.68000 1.000 18.79251 ?  227 ILE   A CA    1 
ATOM   1736 C C     . ILE   A 1 247 ? 3.13100   -12.24700 22.36500 1.000 22.10358 ?  227 ILE   A C     1 
ATOM   1737 O O     . ILE   A 1 247 ? 2.07700   -11.61000 22.26600 1.000 19.77930 ?  227 ILE   A O     1 
ATOM   1738 C CB    . ILE   A 1 247 ? 2.99900   -12.71900 24.83700 1.000 19.21437 ?  227 ILE   A CB    1 
ATOM   1739 C CG1   . ILE   A 1 247 ? 3.67900   -12.55400 26.21100 1.000 21.79539 ?  227 ILE   A CG1   1 
ATOM   1740 C CG2   . ILE   A 1 247 ? 2.46600   -14.16000 24.61400 1.000 18.92531 ?  227 ILE   A CG2   1 
ATOM   1741 C CD1   . ILE   A 1 247 ? 2.74100   -12.83000 27.36900 1.000 21.97217 ?  227 ILE   A CD1   1 
ATOM   1742 N N     . PRO   A 1 248 ? 3.60300   -12.97200 21.35300 1.000 20.19785 ?  228 PRO   A N     1 
ATOM   1743 C CA    . PRO   A 1 248 ? 2.87000   -13.04300 20.08600 1.000 21.05982 ?  228 PRO   A CA    1 
ATOM   1744 C C     . PRO   A 1 248 ? 1.63600   -13.92200 20.20800 1.000 21.14919 ?  228 PRO   A C     1 
ATOM   1745 O O     . PRO   A 1 248 ? 1.55900   -14.81900 21.05800 1.000 21.34364 ?  228 PRO   A O     1 
ATOM   1746 C CB    . PRO   A 1 248 ? 3.89200   -13.65800 19.11500 1.000 22.22135 ?  228 PRO   A CB    1 
ATOM   1747 C CG    . PRO   A 1 248 ? 4.80700   -14.49400 20.03000 1.000 36.25048 ?  228 PRO   A CG    1 
ATOM   1748 C CD    . PRO   A 1 248 ? 4.88100   -13.71500 21.33000 1.000 28.35492 ?  228 PRO   A CD    1 
ATOM   1749 N N     . PHE   A 1 249 ? 0.64100   -13.62700 19.37100 1.000 18.22525 ?  229 PHE   A N     1 
ATOM   1750 C CA    . PHE   A 1 249 ? -0.52200  -14.50000 19.26100 1.000 19.86202 ?  229 PHE   A CA    1 
ATOM   1751 C C     . PHE   A 1 249 ? -1.03000  -14.42900 17.83300 1.000 20.08200 ?  229 PHE   A C     1 
ATOM   1752 O O     . PHE   A 1 249 ? -0.75000  -13.48200 17.09700 1.000 20.33324 ?  229 PHE   A O     1 
ATOM   1753 C CB    . PHE   A 1 249 ? -1.62600  -14.15900 20.29100 1.000 19.82981 ?  229 PHE   A CB    1 
ATOM   1754 C CG    . PHE   A 1 249 ? -2.30200  -12.79100 20.09800 1.000 20.57151 ?  229 PHE   A CG    1 
ATOM   1755 C CD1   . PHE   A 1 249 ? -3.41500  -12.65700 19.26700 1.000 18.40065 ?  229 PHE   A CD1   1 
ATOM   1756 C CD2   . PHE   A 1 249 ? -1.83200  -11.66500 20.77400 1.000 21.31490 ?  229 PHE   A CD2   1 
ATOM   1757 C CE1   . PHE   A 1 249 ? -4.04100  -11.40800 19.09200 1.000 25.01197 ?  229 PHE   A CE1   1 
ATOM   1758 C CE2   . PHE   A 1 249 ? -2.45700  -10.39900 20.62300 1.000 23.02804 ?  229 PHE   A CE2   1 
ATOM   1759 C CZ    . PHE   A 1 249 ? -3.56000  -10.27300 19.79000 1.000 19.29536 ?  229 PHE   A CZ    1 
ATOM   1760 N N     . VAL   A 1 250 ? -1.74600  -15.47700 17.43700 1.000 18.87122 ?  230 VAL   A N     1 
ATOM   1761 C CA    . VAL   A 1 250 ? -2.26300  -15.58900 16.08200 1.000 18.29921 ?  230 VAL   A CA    1 
ATOM   1762 C C     . VAL   A 1 250 ? -3.73100  -15.96300 16.17300 1.000 22.26526 ?  230 VAL   A C     1 
ATOM   1763 O O     . VAL   A 1 250 ? -4.08400  -16.97300 16.80000 1.000 22.25958 ?  230 VAL   A O     1 
ATOM   1764 C CB    . VAL   A 1 250 ? -1.49300  -16.63800 15.24500 1.000 21.35299 ?  230 VAL   A CB    1 
ATOM   1765 C CG1   . VAL   A 1 250 ? -2.17300  -16.81100 13.87900 1.000 18.68605 ?  230 VAL   A CG1   1 
ATOM   1766 C CG2   . VAL   A 1 250 ? 0.01600   -16.24700 15.10500 1.000 20.25960 ?  230 VAL   A CG2   1 
ATOM   1767 N N     . ILE   A 1 251 ? -4.57800  -15.18300 15.51200 1.000 20.10946 ?  231 ILE   A N     1 
ATOM   1768 C CA    . ILE   A 1 251 ? -6.01100  -15.47500 15.41100 1.000 19.11694 ?  231 ILE   A CA    1 
ATOM   1769 C C     . ILE   A 1 251 ? -6.33300  -15.81800 13.97000 1.000 24.37534 ?  231 ILE   A C     1 
ATOM   1770 O O     . ILE   A 1 251 ? -6.17500  -14.98100 13.06800 1.000 20.46177 ?  231 ILE   A O     1 
ATOM   1771 C CB    . ILE   A 1 251 ? -6.87400  -14.30200 15.90500 1.000 21.20858 ?  231 ILE   A CB    1 
ATOM   1772 C CG1   . ILE   A 1 251 ? -6.51800  -13.94200 17.34300 1.000 21.75337 ?  231 ILE   A CG1   1 
ATOM   1773 C CG2   . ILE   A 1 251 ? -8.36200  -14.64400 15.76400 1.000 22.90194 ?  231 ILE   A CG2   1 
ATOM   1774 C CD1   . ILE   A 1 251 ? -7.42900  -12.83000 17.96400 1.000 23.04197 ?  231 ILE   A CD1   1 
ATOM   1775 N N     . ARG   A 1 252 ? -6.80900  -17.04600 13.74700 1.000 21.31492 ?  232 ARG   A N     1 
ATOM   1776 C CA    . ARG   A 1 252 ? -7.23400  -17.42600 12.40800 1.000 19.30719 ?  232 ARG   A CA    1 
ATOM   1777 C C     . ARG   A 1 252 ? -8.55300  -16.74600 12.07600 1.000 22.42492 ?  232 ARG   A C     1 
ATOM   1778 O O     . ARG   A 1 252 ? -9.48200  -16.74700 12.88900 1.000 28.77248 ?  232 ARG   A O     1 
ATOM   1779 C CB    . ARG   A 1 252 ? -7.36900  -18.95300 12.30900 1.000 23.56035 ?  232 ARG   A CB    1 
ATOM   1780 C CG    . ARG   A 1 252 ? -8.05400  -19.37400 11.01400 1.000 26.55268 ?  232 ARG   A CG    1 
ATOM   1781 C CD    . ARG   A 1 252 ? -8.67500  -20.78400 11.09500 1.000 33.19887 ?  232 ARG   A CD    1 
ATOM   1782 N NE    . ARG   A 1 252 ? -7.84300  -21.79000 10.45500 1.000 48.00856 ?  232 ARG   A NE    1 
ATOM   1783 C CZ    . ARG   A 1 252 ? -8.25300  -22.61700 9.49600  1.000 48.62710 ?  232 ARG   A CZ    1 
ATOM   1784 N NH1   . ARG   A 1 252 ? -9.44400  -22.49300 8.92600  1.000 39.11889 ?  232 ARG   A NH1   1 
ATOM   1785 N NH2   . ARG   A 1 252 ? -7.43600  -23.57900 9.07900  1.000 44.36024 ?  232 ARG   A NH2   1 
ATOM   1786 N N     . GLU   A 1 253 ? -8.62000  -16.11500 10.90100 1.000 19.20814 ?  233 GLU   A N     1 
ATOM   1787 C CA    . GLU   A 1 253 ? -9.86400  -15.59900 10.33700 1.000 22.56987 ?  233 GLU   A CA    1 
ATOM   1788 C C     . GLU   A 1 253 ? -10.41300 -16.55900 9.28600  1.000 32.69802 ?  233 GLU   A C     1 
ATOM   1789 O O     . GLU   A 1 253 ? -11.54500 -17.04300 9.41900  1.000 28.94258 ?  233 GLU   A O     1 
ATOM   1790 C CB    . GLU   A 1 253 ? -9.61200  -14.20600 9.74300  1.000 23.05224 ?  233 GLU   A CB    1 
ATOM   1791 C CG    . GLU   A 1 253 ? -9.24400  -13.21600 10.86900 1.000 26.42343 ?  233 GLU   A CG    1 
ATOM   1792 C CD    . GLU   A 1 253 ? -9.23600  -11.75900 10.42600 1.000 41.78975 ?  233 GLU   A CD    1 
ATOM   1793 O OE1   . GLU   A 1 253 ? -9.21900  -11.51400 9.20500  1.000 52.61336 ?  233 GLU   A OE1   1 
ATOM   1794 O OE2   . GLU   A 1 253 ? -9.25000  -10.86400 11.29800 1.000 37.11728 -1 233 GLU   A OE2   1 
ATOM   1795 N N     . THR   A 1 254 ? -9.60500  -16.87800 8.26800  1.000 24.59074 ?  234 THR   A N     1 
ATOM   1796 C CA    . THR   A 1 254 ? -9.88100  -17.93200 7.28900  1.000 21.94883 ?  234 THR   A CA    1 
ATOM   1797 C C     . THR   A 1 254 ? -8.68700  -18.88100 7.24800  1.000 22.70718 ?  234 THR   A C     1 
ATOM   1798 O O     . THR   A 1 254 ? -7.66800  -18.64800 7.90600  1.000 21.51010 ?  234 THR   A O     1 
ATOM   1799 C CB    . THR   A 1 254 ? -10.16600 -17.35800 5.89400  1.000 25.59509 ?  234 THR   A CB    1 
ATOM   1800 O OG1   . THR   A 1 254 ? -8.92900  -17.04400 5.24800  1.000 24.01592 ?  234 THR   A OG1   1 
ATOM   1801 C CG2   . THR   A 1 254 ? -11.05600 -16.10000 5.95300  1.000 28.46968 ?  234 THR   A CG2   1 
ATOM   1802 N N     . SER   A 1 255 ? -8.78700  -19.96400 6.45800  1.000 24.41953 ?  235 SER   A N     1 
ATOM   1803 C CA    . SER   A 1 255 ? -7.63400  -20.85700 6.37200  1.000 25.36346 ?  235 SER   A CA    1 
ATOM   1804 C C     . SER   A 1 255 ? -6.43300  -20.16400 5.75100  1.000 21.71276 ?  235 SER   A C     1 
ATOM   1805 O O     . SER   A 1 255 ? -5.32700  -20.70500 5.82700  1.000 23.65246 ?  235 SER   A O     1 
ATOM   1806 C CB    . SER   A 1 255 ? -7.93000  -22.10900 5.52400  1.000 27.91187 ?  235 SER   A CB    1 
ATOM   1807 O OG    . SER   A 1 255 ? -8.71100  -21.76200 4.39400  1.000 26.30824 ?  235 SER   A OG    1 
ATOM   1808 N N     . ARG   A 1 256 ? -6.62600  -18.98000 5.17000  1.000 21.06949 ?  236 ARG   A N     1 
ATOM   1809 C CA    . ARG   A 1 256 ? -5.50500  -18.27900 4.49100  1.000 17.84388 ?  236 ARG   A CA    1 
ATOM   1810 C C     . ARG   A 1 256 ? -5.24100  -16.90200 5.12100  1.000 22.72694 ?  236 ARG   A C     1 
ATOM   1811 O O     . ARG   A 1 256 ? -4.21400  -16.32600 4.82200  1.000 24.15165 ?  236 ARG   A O     1 
ATOM   1812 C CB    . ARG   A 1 256 ? -5.76300  -18.12300 2.99500  1.000 19.08190 ?  236 ARG   A CB    1 
ATOM   1813 C CG    . ARG   A 1 256 ? -5.64800  -19.42600 2.22100  1.000 16.83912 ?  236 ARG   A CG    1 
ATOM   1814 C CD    . ARG   A 1 256 ? -5.83400  -19.25700 0.72700  1.000 22.17042 ?  236 ARG   A CD    1 
ATOM   1815 N NE    . ARG   A 1 256 ? -5.56000  -20.49100 0.01000  1.000 20.79595 ?  236 ARG   A NE    1 
ATOM   1816 C CZ    . ARG   A 1 256 ? -4.34400  -20.91300 -0.31100 1.000 23.25481 ?  236 ARG   A CZ    1 
ATOM   1817 N NH1   . ARG   A 1 256 ? -3.29700  -20.14900 -0.06900 1.000 20.25645 ?  236 ARG   A NH1   1 
ATOM   1818 N NH2   . ARG   A 1 256 ? -4.17800  -22.09600 -0.87300 1.000 20.24986 ?  236 ARG   A NH2   1 
ATOM   1819 N N     . LYS   A 1 257 ? -6.14200  -16.42500 5.96900  1.000 17.14088 ?  237 LYS   A N     1 
ATOM   1820 C CA    . LYS   A 1 257 ? -5.99100  -15.05000 6.50700  1.000 18.13708 ?  237 LYS   A CA    1 
ATOM   1821 C C     . LYS   A 1 257 ? -5.95300  -15.06800 8.03000  1.000 19.09746 ?  237 LYS   A C     1 
ATOM   1822 O O     . LYS   A 1 257 ? -6.84800  -15.64700 8.64700  1.000 19.55171 ?  237 LYS   A O     1 
ATOM   1823 C CB    . LYS   A 1 257 ? -7.14400  -14.16300 6.06000  1.000 20.70639 ?  237 LYS   A CB    1 
ATOM   1824 C CG    . LYS   A 1 257 ? -7.10800  -12.73000 6.56400  1.000 20.51911 ?  237 LYS   A CG    1 
ATOM   1825 C CD    . LYS   A 1 257 ? -8.14400  -11.87200 5.88200  1.000 24.47040 ?  237 LYS   A CD    1 
ATOM   1826 C CE    . LYS   A 1 257 ? -7.91600  -10.39100 6.08500  1.000 40.11871 ?  237 LYS   A CE    1 
ATOM   1827 N NZ    . LYS   A 1 257 ? -8.47900  -9.93100  7.37300  1.000 46.06977 ?  237 LYS   A NZ    1 
ATOM   1828 N N     . PHE   A 1 258 ? -4.94500  -14.40700 8.58000  1.000 16.98169 ?  238 PHE   A N     1 
ATOM   1829 C CA    . PHE   A 1 258 ? -4.78400  -14.43300 10.04200 1.000 18.18506 ?  238 PHE   A CA    1 
ATOM   1830 C C     . PHE   A 1 258 ? -4.36000  -13.09300 10.64600 1.000 19.95253 ?  238 PHE   A C     1 
ATOM   1831 O O     . PHE   A 1 258 ? -3.77500  -12.28100 9.94000  1.000 19.34933 ?  238 PHE   A O     1 
ATOM   1832 C CB    . PHE   A 1 258 ? -3.66200  -15.40600 10.41000 1.000 17.99973 ?  238 PHE   A CB    1 
ATOM   1833 C CG    . PHE   A 1 258 ? -3.82400  -16.82400 9.92700  1.000 20.60186 ?  238 PHE   A CG    1 
ATOM   1834 C CD1   . PHE   A 1 258 ? -3.54000  -17.16800 8.61600  1.000 23.40696 ?  238 PHE   A CD1   1 
ATOM   1835 C CD2   . PHE   A 1 258 ? -4.23100  -17.82300 10.79100 1.000 24.51833 ?  238 PHE   A CD2   1 
ATOM   1836 C CE1   . PHE   A 1 258 ? -3.69600  -18.47000 8.17400  1.000 24.43650 ?  238 PHE   A CE1   1 
ATOM   1837 C CE2   . PHE   A 1 258 ? -4.38100  -19.12600 10.34800 1.000 26.10826 ?  238 PHE   A CE2   1 
ATOM   1838 C CZ    . PHE   A 1 258 ? -4.11500  -19.44600 9.04100  1.000 21.07969 ?  238 PHE   A CZ    1 
ATOM   1839 N N     . GLN   A 1 259 ? -4.75700  -12.86100 11.89300 1.000 16.89683 ?  239 GLN   A N     1 
ATOM   1840 C CA    . GLN   A 1 259 ? -4.17400  -11.76000 12.66500 1.000 17.79562 ?  239 GLN   A CA    1 
ATOM   1841 C C     . GLN   A 1 259 ? -2.93000  -12.31000 13.34100 1.000 19.55781 ?  239 GLN   A C     1 
ATOM   1842 O O     . GLN   A 1 259 ? -2.96400  -13.40900 13.90000 1.000 20.92484 ?  239 GLN   A O     1 
ATOM   1843 C CB    . GLN   A 1 259 ? -5.13400  -11.26800 13.74400 1.000 19.37186 ?  239 GLN   A CB    1 
ATOM   1844 C CG    . GLN   A 1 259 ? -6.50800  -10.89400 13.23300 1.000 18.83650 ?  239 GLN   A CG    1 
ATOM   1845 C CD    . GLN   A 1 259 ? -7.45000  -10.49300 14.35300 1.000 22.29573 ?  239 GLN   A CD    1 
ATOM   1846 O OE1   . GLN   A 1 259 ? -7.02000  -10.06600 15.43900 1.000 21.79607 ?  239 GLN   A OE1   1 
ATOM   1847 N NE2   . GLN   A 1 259 ? -8.74700  -10.69000 14.11700 1.000 23.61136 ?  239 GLN   A NE2   1 
ATOM   1848 N N     . HIS   A 1 260 ? -1.84000  -11.56300 13.28500 1.000 17.31338 ?  240 HIS   A N     1 
ATOM   1849 C CA    . HIS   A 1 260 ? -0.58200  -11.95900 13.91700 1.000 17.49385 ?  240 HIS   A CA    1 
ATOM   1850 C C     . HIS   A 1 260 ? -0.08900  -10.73800 14.68400 1.000 18.43314 ?  240 HIS   A C     1 
ATOM   1851 O O     . HIS   A 1 260 ? 0.24100   -9.72900  14.06400 1.000 18.45838 ?  240 HIS   A O     1 
ATOM   1852 C CB    . HIS   A 1 260 ? 0.42700   -12.41400 12.85800 1.000 19.52173 ?  240 HIS   A CB    1 
ATOM   1853 C CG    . HIS   A 1 260 ? 1.65800   -13.07200 13.41300 1.000 20.21018 ?  240 HIS   A CG    1 
ATOM   1854 N ND1   . HIS   A 1 260 ? 2.53900   -13.77800 12.61700 1.000 22.68908 ?  240 HIS   A ND1   1 
ATOM   1855 C CD2   . HIS   A 1 260 ? 2.17600   -13.09600 14.66500 1.000 21.78403 ?  240 HIS   A CD2   1 
ATOM   1856 C CE1   . HIS   A 1 260 ? 3.54200   -14.21700 13.35700 1.000 27.08789 ?  240 HIS   A CE1   1 
ATOM   1857 N NE2   . HIS   A 1 260 ? 3.34300   -13.82500 14.60600 1.000 25.12513 ?  240 HIS   A NE2   1 
ATOM   1858 N N     . THR   A 1 261 ? -0.07000  -10.81700 16.01500 1.000 17.09826 ?  241 THR   A N     1 
ATOM   1859 C CA    . THR   A 1 261 ? -0.02200  -9.61700  16.85500 1.000 18.69811 ?  241 THR   A CA    1 
ATOM   1860 C C     . THR   A 1 261 ? 0.87600   -9.83500  18.06300 1.000 19.36790 ?  241 THR   A C     1 
ATOM   1861 O O     . THR   A 1 261 ? 0.95300   -10.94000 18.59800 1.000 21.31369 ?  241 THR   A O     1 
ATOM   1862 C CB    . THR   A 1 261 ? -1.45200  -9.18700  17.25900 1.000 18.93994 ?  241 THR   A CB    1 
ATOM   1863 O OG1   . THR   A 1 261 ? -2.27100  -8.98600  16.08900 1.000 20.24590 ?  241 THR   A OG1   1 
ATOM   1864 C CG2   . THR   A 1 261 ? -1.49800  -7.96900  18.18500 1.000 15.95819 ?  241 THR   A CG2   1 
ATOM   1865 N N     . ILE   A 1 262 ? 1.57900   -8.78200  18.47000 1.000 19.46054 ?  242 ILE   A N     1 
ATOM   1866 C CA    . ILE   A 1 262 ? 2.49100   -8.84600  19.60600 1.000 18.00151 ?  242 ILE   A CA    1 
ATOM   1867 C C     . ILE   A 1 262 ? 1.84700   -8.12200  20.77300 1.000 20.81234 ?  242 ILE   A C     1 
ATOM   1868 O O     . ILE   A 1 262 ? 1.79500   -6.88600  20.79500 1.000 20.86142 ?  242 ILE   A O     1 
ATOM   1869 C CB    . ILE   A 1 262 ? 3.86700   -8.24300  19.28900 1.000 20.60341 ?  242 ILE   A CB    1 
ATOM   1870 C CG1   . ILE   A 1 262 ? 4.35900   -8.70600  17.91200 1.000 22.31793 ?  242 ILE   A CG1   1 
ATOM   1871 C CG2   . ILE   A 1 262 ? 4.82600   -8.52800  20.43300 1.000 23.27985 ?  242 ILE   A CG2   1 
ATOM   1872 C CD1   . ILE   A 1 262 ? 4.56800   -10.18100 17.81800 1.000 31.11583 ?  242 ILE   A CD1   1 
ATOM   1873 N N     . SER   A 1 263 ? 1.37300   -8.88100  21.74800 1.000 18.69808 ?  243 SER   A N     1 
ATOM   1874 C CA    . SER   A 1 263 ? 0.77500   -8.27000  22.92400 1.000 20.46992 ?  243 SER   A CA    1 
ATOM   1875 C C     . SER   A 1 263 ? 1.87800   -7.94200  23.93300 1.000 22.91922 ?  243 SER   A C     1 
ATOM   1876 O O     . SER   A 1 263 ? 2.92000   -8.60300  23.97700 1.000 22.66804 ?  243 SER   A O     1 
ATOM   1877 C CB    . SER   A 1 263 ? -0.27600  -9.21800  23.51900 1.000 25.84328 ?  243 SER   A CB    1 
ATOM   1878 O OG    . SER   A 1 263 ? -1.11000  -8.55100  24.44900 1.000 29.05691 ?  243 SER   A OG    1 
ATOM   1879 N N     . GLN   A 1 264 ? 1.67000   -6.88500  24.71700 1.000 18.72100 ?  244 GLN   A N     1 
ATOM   1880 C CA    . GLN   A 1 264 ? 2.59600   -6.56400  25.80300 1.000 18.27664 ?  244 GLN   A CA    1 
ATOM   1881 C C     . GLN   A 1 264 ? 1.95700   -6.95800  27.12100 1.000 17.95415 ?  244 GLN   A C     1 
ATOM   1882 O O     . GLN   A 1 264 ? 0.90400   -6.42800  27.48200 1.000 19.16862 ?  244 GLN   A O     1 
ATOM   1883 C CB    . GLN   A 1 264 ? 2.95200   -5.07600  25.83600 1.000 20.86864 ?  244 GLN   A CB    1 
ATOM   1884 C CG    . GLN   A 1 264 ? 3.90100   -4.76100  27.01500 1.000 20.34895 ?  244 GLN   A CG    1 
ATOM   1885 C CD    . GLN   A 1 264 ? 4.54600   -3.40500  26.85500 1.000 25.27928 ?  244 GLN   A CD    1 
ATOM   1886 O OE1   . GLN   A 1 264 ? 3.84600   -2.39500  26.76800 1.000 23.35663 ?  244 GLN   A OE1   1 
ATOM   1887 N NE2   . GLN   A 1 264 ? 5.88500   -3.37200  26.78700 1.000 23.38068 ?  244 GLN   A NE2   1 
ATOM   1888 N N     . MET   A 1 265 ? 2.59500   -7.89500  27.82800 1.000 18.06818 ?  245 MET   A N     1 
ATOM   1889 C CA    . MET   A 1 265 ? 2.25100   -8.21900  29.20300 1.000 19.02577 ?  245 MET   A CA    1 
ATOM   1890 C C     . MET   A 1 265 ? 2.91600   -7.24800  30.16300 1.000 20.72805 ?  245 MET   A C     1 
ATOM   1891 O O     . MET   A 1 265 ? 4.10500   -6.96400  30.02000 1.000 24.79921 ?  245 MET   A O     1 
ATOM   1892 C CB    . MET   A 1 265 ? 2.68900   -9.65300  29.54000 1.000 20.19313 ?  245 MET   A CB    1 
ATOM   1893 C CG    . MET   A 1 265 ? 2.17500   -10.06800 30.91500 1.000 18.05683 ?  245 MET   A CG    1 
ATOM   1894 S SD    . MET   A 1 265 ? 2.61300   -11.79500 31.31300 1.000 22.49102 ?  245 MET   A SD    1 
ATOM   1895 C CE    . MET   A 1 265 ? 1.17100   -12.62400 30.55500 1.000 18.70991 ?  245 MET   A CE    1 
ATOM   1896 N N     . SER   A 1 266 ? 2.15300   -6.74800  31.14100 1.000 19.10666 ?  246 SER   A N     1 
ATOM   1897 C CA    . SER   A 1 266 ? 2.71900   -5.94900  32.21800 1.000 20.76291 ?  246 SER   A CA    1 
ATOM   1898 C C     . SER   A 1 266 ? 2.25000   -6.53100  33.54200 1.000 26.02410 ?  246 SER   A C     1 
ATOM   1899 O O     . SER   A 1 266 ? 1.07000   -6.87300  33.70500 1.000 21.60062 ?  246 SER   A O     1 
ATOM   1900 C CB    . SER   A 1 266 ? 2.33300   -4.44900  32.11200 1.000 22.13061 ?  246 SER   A CB    1 
ATOM   1901 O OG    . SER   A 1 266 ? 0.94900   -4.24600  31.81600 1.000 22.72865 ?  246 SER   A OG    1 
ATOM   1902 N N     . VAL   A 1 267 ? 3.18400   -6.65800  34.48600 1.000 22.37875 ?  247 VAL   A N     1 
ATOM   1903 C CA    . VAL   A 1 267 ? 2.94400   -7.35600  35.74200 1.000 22.19396 ?  247 VAL   A CA    1 
ATOM   1904 C C     . VAL   A 1 267 ? 3.02000   -6.33900  36.86600 1.000 26.70544 ?  247 VAL   A C     1 
ATOM   1905 O O     . VAL   A 1 267 ? 4.04100   -5.65200  37.01700 1.000 27.23263 ?  247 VAL   A O     1 
ATOM   1906 C CB    . VAL   A 1 267 ? 3.95000   -8.49300  35.95500 1.000 20.12839 ?  247 VAL   A CB    1 
ATOM   1907 C CG1   . VAL   A 1 267 ? 3.63600   -9.23300  37.24200 1.000 23.17682 ?  247 VAL   A CG1   1 
ATOM   1908 C CG2   . VAL   A 1 267 ? 3.91900   -9.47500  34.74100 1.000 24.19551 ?  247 VAL   A CG2   1 
ATOM   1909 N N     . TRP   A 1 268 ? 1.95700   -6.26400  37.67200 1.000 22.19121 ?  248 TRP   A N     1 
ATOM   1910 C CA    . TRP   A 1 268 ? 1.79600   -5.19700  38.65600 1.000 24.73258 ?  248 TRP   A CA    1 
ATOM   1911 C C     . TRP   A 1 268 ? 1.54400   -5.81500  40.02500 1.000 26.35163 ?  248 TRP   A C     1 
ATOM   1912 O O     . TRP   A 1 268 ? 0.61200   -6.61100  40.18600 1.000 26.87309 ?  248 TRP   A O     1 
ATOM   1913 C CB    . TRP   A 1 268 ? 0.64700   -4.26000  38.26700 1.000 22.13635 ?  248 TRP   A CB    1 
ATOM   1914 C CG    . TRP   A 1 268 ? 0.72000   -3.79300  36.85600 1.000 22.00061 ?  248 TRP   A CG    1 
ATOM   1915 C CD1   . TRP   A 1 268 ? 0.26000   -4.46200  35.75000 1.000 22.57239 ?  248 TRP   A CD1   1 
ATOM   1916 C CD2   . TRP   A 1 268 ? 1.25700   -2.54700  36.37900 1.000 21.45337 ?  248 TRP   A CD2   1 
ATOM   1917 N NE1   . TRP   A 1 268 ? 0.48700   -3.71200  34.61300 1.000 22.60598 ?  248 TRP   A NE1   1 
ATOM   1918 C CE2   . TRP   A 1 268 ? 1.09000   -2.53000  34.97000 1.000 20.20464 ?  248 TRP   A CE2   1 
ATOM   1919 C CE3   . TRP   A 1 268 ? 1.85100   -1.43100  37.00700 1.000 23.62064 ?  248 TRP   A CE3   1 
ATOM   1920 C CZ2   . TRP   A 1 268 ? 1.51400   -1.46500  34.17600 1.000 21.63744 ?  248 TRP   A CZ2   1 
ATOM   1921 C CZ3   . TRP   A 1 268 ? 2.27700   -0.36300  36.20800 1.000 25.06626 ?  248 TRP   A CZ3   1 
ATOM   1922 C CH2   . TRP   A 1 268 ? 2.10100   -0.38300  34.80700 1.000 25.65530 ?  248 TRP   A CH2   1 
ATOM   1923 N N     . LYS   A 1 269 ? 2.38400   -5.46500  41.00400 1.000 26.34692 ?  249 LYS   A N     1 
ATOM   1924 C CA    . LYS   A 1 269 ? 2.26100   -5.97900  42.36700 1.000 24.37433 ?  249 LYS   A CA    1 
ATOM   1925 C C     . LYS   A 1 269 ? 1.64100   -4.91100  43.25200 1.000 30.95456 ?  249 LYS   A C     1 
ATOM   1926 O O     . LYS   A 1 269 ? 2.12100   -3.77000  43.26300 1.000 27.88481 ?  249 LYS   A O     1 
ATOM   1927 C CB    . LYS   A 1 269 ? 3.62300   -6.38700  42.92900 1.000 29.28526 ?  249 LYS   A CB    1 
ATOM   1928 C CG    . LYS   A 1 269 ? 3.53600   -7.08400  44.28700 1.000 38.46715 ?  249 LYS   A CG    1 
ATOM   1929 C CD    . LYS   A 1 269 ? 4.85700   -7.75100  44.67300 1.000 43.69732 ?  249 LYS   A CD    1 
ATOM   1930 C CE    . LYS   A 1 269 ? 4.70800   -8.58400  45.96000 1.000 46.46679 ?  249 LYS   A CE    1 
ATOM   1931 N N     . VAL   A 1 270 ? 0.56400   -5.26500  43.97100 1.000 26.53150 ?  250 VAL   A N     1 
ATOM   1932 C CA    . VAL   A 1 270 ? -0.12700  -4.27000  44.79300 1.000 33.37775 ?  250 VAL   A CA    1 
ATOM   1933 C C     . VAL   A 1 270 ? 0.78300   -3.84500  45.93700 1.000 38.15108 ?  250 VAL   A C     1 
ATOM   1934 O O     . VAL   A 1 270 ? 1.49300   -4.67000  46.53200 1.000 32.25877 ?  250 VAL   A O     1 
ATOM   1935 C CB    . VAL   A 1 270 ? -1.47700  -4.78800  45.32600 1.000 39.00299 ?  250 VAL   A CB    1 
ATOM   1936 C CG1   . VAL   A 1 270 ? -1.30900  -5.95900  46.23000 1.000 40.03903 ?  250 VAL   A CG1   1 
ATOM   1937 C CG2   . VAL   A 1 270 ? -2.19400  -3.71500  46.09000 1.000 47.70234 ?  250 VAL   A CG2   1 
ATOM   1938 N N     . ILE   A 1 271 ? 0.80100   -2.54500  46.21600 1.000 33.89711 ?  251 ILE   A N     1 
ATOM   1939 C CA    . ILE   A 1 271 ? 1.61500   -2.01300  47.30500 1.000 42.57392 ?  251 ILE   A CA    1 
ATOM   1940 C C     . ILE   A 1 271 ? 0.76600   -1.93800  48.56300 1.000 40.05776 ?  251 ILE   A C     1 
ATOM   1941 O O     . ILE   A 1 271 ? 1.15200   -2.47900  49.60000 1.000 62.21103 ?  251 ILE   A O     1 
ATOM   1942 C CB    . ILE   A 1 271 ? 2.22500   -0.62900  46.96300 1.000 47.99533 ?  251 ILE   A CB    1 
ATOM   1943 C CG1   . ILE   A 1 271 ? 1.14200   0.44600   46.89000 1.000 52.35404 ?  251 ILE   A CG1   1 
ATOM   1944 C CG2   . ILE   A 1 271 ? 3.00300   -0.67900  45.66500 1.000 46.03391 ?  251 ILE   A CG2   1 
ATOM   1945 N N     . ASN   B 1 27  ? -47.16400 -18.94000 46.79600 1.000 48.34012 ?  7   ASN   B N     1 
ATOM   1946 C CA    . ASN   B 1 27  ? -45.74600 -18.75800 47.20400 1.000 57.43336 ?  7   ASN   B CA    1 
ATOM   1947 C C     . ASN   B 1 27  ? -45.26800 -17.38100 46.72800 1.000 60.95661 ?  7   ASN   B C     1 
ATOM   1948 O O     . ASN   B 1 27  ? -45.17800 -17.17300 45.50500 1.000 64.47796 ?  7   ASN   B O     1 
ATOM   1949 C CB    . ASN   B 1 27  ? -44.85300 -19.90500 46.72800 1.000 63.43085 ?  7   ASN   B CB    1 
ATOM   1950 N N     . ILE   B 1 28  ? -44.96300 -16.49100 47.66600 1.000 54.17286 ?  8   ILE   B N     1 
ATOM   1951 C CA    . ILE   B 1 28  ? -44.58900 -15.09600 47.29800 1.000 56.17860 ?  8   ILE   B CA    1 
ATOM   1952 C C     . ILE   B 1 28  ? -43.07300 -14.99900 47.12800 1.000 57.46447 ?  8   ILE   B C     1 
ATOM   1953 O O     . ILE   B 1 28  ? -42.35600 -15.58000 47.95500 1.000 51.53580 ?  8   ILE   B O     1 
ATOM   1954 C CB    . ILE   B 1 28  ? -45.11100 -14.11700 48.36900 1.000 49.01843 ?  8   ILE   B CB    1 
ATOM   1955 C CG2   . ILE   B 1 28  ? -44.68300 -12.69200 48.08000 1.000 41.44184 ?  8   ILE   B CG2   1 
ATOM   1956 N N     . TYR   B 1 29  ? -42.61500 -14.29100 46.09600 1.000 48.42102 ?  9   TYR   B N     1 
ATOM   1957 C CA    . TYR   B 1 29  ? -41.16300 -14.05000 45.92600 1.000 45.21425 ?  9   TYR   B CA    1 
ATOM   1958 C C     . TYR   B 1 29  ? -40.66500 -13.23700 47.11500 1.000 44.83945 ?  9   TYR   B C     1 
ATOM   1959 O O     . TYR   B 1 29  ? -41.29400 -12.22800 47.46300 1.000 39.92669 ?  9   TYR   B O     1 
ATOM   1960 C CB    . TYR   B 1 29  ? -40.90900 -13.26800 44.64500 1.000 49.10906 ?  9   TYR   B CB    1 
ATOM   1961 C CG    . TYR   B 1 29  ? -39.49800 -12.85400 44.32600 1.000 57.63804 ?  9   TYR   B CG    1 
ATOM   1962 C CD1   . TYR   B 1 29  ? -38.64200 -13.71300 43.66200 1.000 52.57369 ?  9   TYR   B CD1   1 
ATOM   1963 C CD2   . TYR   B 1 29  ? -39.05000 -11.57400 44.60100 1.000 59.00000 ?  9   TYR   B CD2   1 
ATOM   1964 C CE1   . TYR   B 1 29  ? -37.35500 -13.33000 43.32900 1.000 70.78074 ?  9   TYR   B CE1   1 
ATOM   1965 C CE2   . TYR   B 1 29  ? -37.76600 -11.17400 44.27600 1.000 45.96511 ?  9   TYR   B CE2   1 
ATOM   1966 C CZ    . TYR   B 1 29  ? -36.91800 -12.05600 43.63400 1.000 61.65000 ?  9   TYR   B CZ    1 
ATOM   1967 O OH    . TYR   B 1 29  ? -35.64500 -11.69000 43.29600 1.000 70.46000 ?  9   TYR   B OH    1 
ATOM   1968 N N     . GLU   B 1 30  ? -39.55500 -13.68000 47.69600 1.000 50.66968 ?  10  GLU   B N     1 
ATOM   1969 C CA    . GLU   B 1 30  ? -38.98800 -13.00100 48.88100 1.000 48.92207 ?  10  GLU   B CA    1 
ATOM   1970 C C     . GLU   B 1 30  ? -37.70100 -12.28600 48.48600 1.000 52.40000 ?  10  GLU   B C     1 
ATOM   1971 O O     . GLU   B 1 30  ? -36.83700 -12.92500 47.88000 1.000 65.54000 ?  10  GLU   B O     1 
ATOM   1972 C CB    . GLU   B 1 30  ? -38.71500 -14.03300 49.96700 1.000 52.46949 ?  10  GLU   B CB    1 
ATOM   1973 C CG    . GLU   B 1 30  ? -39.97400 -14.49200 50.67800 1.000 51.35027 ?  10  GLU   B CG    1 
ATOM   1974 C CD    . GLU   B 1 30  ? -39.73100 -15.53100 51.75800 1.000 65.73622 ?  10  GLU   B CD    1 
ATOM   1975 O OE1   . GLU   B 1 30  ? -38.63700 -15.51900 52.34800 1.000 65.29065 ?  10  GLU   B OE1   1 
ATOM   1976 O OE2   . GLU   B 1 30  ? -40.63600 -16.34900 52.00400 1.000 73.13444 ?  10  GLU   B OE2   1 
ATOM   1977 N N     . THR   B 1 31  ? -37.60100 -11.01000 48.83400 1.000 51.00405 ?  11  THR   B N     1 
ATOM   1978 C CA    . THR   B 1 31  ? -36.40000 -10.20100 48.53000 1.000 43.19867 ?  11  THR   B CA    1 
ATOM   1979 C C     . THR   B 1 31  ? -35.36700 -10.31700 49.65500 1.000 43.06134 ?  11  THR   B C     1 
ATOM   1980 O O     . THR   B 1 31  ? -35.77600 -10.63200 50.77600 1.000 49.06657 ?  11  THR   B O     1 
ATOM   1981 C CB    . THR   B 1 31  ? -36.83400 -8.74500  48.37200 1.000 35.29503 ?  11  THR   B CB    1 
ATOM   1982 O OG1   . THR   B 1 31  ? -37.28100 -8.28300  49.64200 1.000 36.01427 ?  11  THR   B OG1   1 
ATOM   1983 C CG2   . THR   B 1 31  ? -37.93600 -8.59200  47.34700 1.000 38.26367 ?  11  THR   B CG2   1 
ATOM   1984 N N     . ASP   B 1 32  ? -34.09000 -10.05200 49.36900 1.000 42.98304 ?  12  ASP   B N     1 
ATOM   1985 C CA    . ASP   B 1 32  ? -33.02300 -10.04100 50.41200 1.000 49.17972 ?  12  ASP   B CA    1 
ATOM   1986 C C     . ASP   B 1 32  ? -33.00900 -8.71100  51.18000 1.000 48.69003 ?  12  ASP   B C     1 
ATOM   1987 O O     . ASP   B 1 32  ? -33.88900 -7.89400  50.92600 1.000 40.18821 ?  12  ASP   B O     1 
ATOM   1988 C CB    . ASP   B 1 32  ? -31.64400 -10.31000 49.80800 1.000 50.89873 ?  12  ASP   B CB    1 
ATOM   1989 C CG    . ASP   B 1 32  ? -31.12700 -9.24800  48.85200 1.000 57.62535 ?  12  ASP   B CG    1 
ATOM   1990 O OD1   . ASP   B 1 32  ? -30.99100 -8.08300  49.26700 1.000 48.37026 ?  12  ASP   B OD1   1 
ATOM   1991 O OD2   . ASP   B 1 32  ? -30.82700 -9.60800  47.70300 1.000 67.38006 -1 12  ASP   B OD2   1 
ATOM   1992 N N     . GLU   B 1 33  ? -31.97900 -8.46900  52.00700 1.000 50.37319 ?  13  GLU   B N     1 
ATOM   1993 C CA    . GLU   B 1 33  ? -31.93700 -7.25800  52.88400 1.000 50.36643 ?  13  GLU   B CA    1 
ATOM   1994 C C     . GLU   B 1 33  ? -31.67100 -5.96300  52.10100 1.000 42.59582 ?  13  GLU   B C     1 
ATOM   1995 O O     . GLU   B 1 33  ? -32.32700 -4.95700  52.39400 1.000 37.26483 ?  13  GLU   B O     1 
ATOM   1996 C CB    . GLU   B 1 33  ? -30.92800 -7.44900  54.02400 1.000 53.34566 ?  13  GLU   B CB    1 
ATOM   1997 C CG    . GLU   B 1 33  ? -30.95100 -6.33500  55.05200 1.000 50.93690 ?  13  GLU   B CG    1 
ATOM   1998 N N     . SER   B 1 34  ? -30.74000 -5.98300  51.15300 1.000 40.58136 ?  14  SER   B N     1 
ATOM   1999 C CA    . SER   B 1 34  ? -30.49600 -4.78000  50.32500 1.000 40.83202 ?  14  SER   B CA    1 
ATOM   2000 C C     . SER   B 1 34  ? -31.75400 -4.44000  49.52000 1.000 37.27733 ?  14  SER   B C     1 
ATOM   2001 O O     . SER   B 1 34  ? -32.14100 -3.27000  49.47200 1.000 30.94173 ?  14  SER   B O     1 
ATOM   2002 C CB    . SER   B 1 34  ? -29.31400 -4.98400  49.42300 1.000 55.37985 ?  14  SER   B CB    1 
ATOM   2003 N N     . VAL   B 1 35  ? -32.35800 -5.45000  48.90200 1.000 32.22069 ?  15  VAL   B N     1 
ATOM   2004 C CA    . VAL   B 1 35  ? -33.56600 -5.19700  48.07300 1.000 23.79549 ?  15  VAL   B CA    1 
ATOM   2005 C C     . VAL   B 1 35  ? -34.69900 -4.75100  49.00200 1.000 23.34340 ?  15  VAL   B C     1 
ATOM   2006 O O     . VAL   B 1 35  ? -35.43900 -3.85000  48.62600 1.000 24.63822 ?  15  VAL   B O     1 
ATOM   2007 C CB    . VAL   B 1 35  ? -33.94500 -6.43700  47.24100 1.000 29.98330 ?  15  VAL   B CB    1 
ATOM   2008 C CG1   . VAL   B 1 35  ? -35.14200 -6.17900  46.34800 1.000 30.48001 ?  15  VAL   B CG1   1 
ATOM   2009 C CG2   . VAL   B 1 35  ? -32.76700 -6.92000  46.41300 1.000 29.85025 ?  15  VAL   B CG2   1 
ATOM   2010 N N     . SER   B 1 36  ? -34.77800 -5.35300  50.18700 1.000 23.73275 ?  16  SER   B N     1 
ATOM   2011 C CA    . SER   B 1 36  ? -35.86500 -5.02100  51.14200 1.000 25.78382 ?  16  SER   B CA    1 
ATOM   2012 C C     . SER   B 1 36  ? -35.84600 -3.52400  51.48300 1.000 23.67405 ?  16  SER   B C     1 
ATOM   2013 O O     . SER   B 1 36  ? -36.90900 -2.93700  51.61000 1.000 21.99984 ?  16  SER   B O     1 
ATOM   2014 C CB    . SER   B 1 36  ? -35.79200 -5.90000  52.37000 1.000 28.44491 ?  16  SER   B CB    1 
ATOM   2015 O OG    . SER   B 1 36  ? -36.18000 -7.22900  52.07400 1.000 29.00389 ?  16  SER   B OG    1 
ATOM   2016 N N     . GLN   B 1 37  ? -34.65200 -2.95300  51.61800 1.000 22.83391 ?  17  GLN   B N     1 
ATOM   2017 C CA    . GLN   B 1 37  ? -34.55900 -1.52000  51.99100 1.000 21.42143 ?  17  GLN   B CA    1 
ATOM   2018 C C     . GLN   B 1 37  ? -35.25400 -0.67500  50.91800 1.000 22.85404 ?  17  GLN   B C     1 
ATOM   2019 O O     . GLN   B 1 37  ? -35.98000 0.24700   51.27200 1.000 22.83458 ?  17  GLN   B O     1 
ATOM   2020 C CB    . GLN   B 1 37  ? -33.11000 -1.07200  52.14500 1.000 23.11119 ?  17  GLN   B CB    1 
ATOM   2021 C CG    . GLN   B 1 37  ? -32.97200 0.39600   52.51100 1.000 28.72382 ?  17  GLN   B CG    1 
ATOM   2022 C CD    . GLN   B 1 37  ? -33.39800 0.66800   53.93200 1.000 38.94466 ?  17  GLN   B CD    1 
ATOM   2023 O OE1   . GLN   B 1 37  ? -32.59800 0.59300   54.85900 1.000 39.12446 ?  17  GLN   B OE1   1 
ATOM   2024 N NE2   . GLN   B 1 37  ? -34.66700 0.99500   54.11200 1.000 31.79852 ?  17  GLN   B NE2   1 
ATOM   2025 N N     . TYR   B 1 38  ? -35.00300 -0.99500  49.65400 1.000 19.73945 ?  18  TYR   B N     1 
ATOM   2026 C CA    . TYR   B 1 38  ? -35.60000 -0.17600  48.61100 1.000 23.18748 ?  18  TYR   B CA    1 
ATOM   2027 C C     . TYR   B 1 38  ? -37.05500 -0.52900  48.38000 1.000 27.29579 ?  18  TYR   B C     1 
ATOM   2028 O O     . TYR   B 1 38  ? -37.84600 0.35000   48.03800 1.000 22.64832 ?  18  TYR   B O     1 
ATOM   2029 C CB    . TYR   B 1 38  ? -34.76500 -0.27400  47.33400 1.000 27.86143 ?  18  TYR   B CB    1 
ATOM   2030 C CG    . TYR   B 1 38  ? -33.64400 0.71800   47.44100 1.000 29.59122 ?  18  TYR   B CG    1 
ATOM   2031 C CD1   . TYR   B 1 38  ? -33.83200 2.04500   47.05100 1.000 34.65688 ?  18  TYR   B CD1   1 
ATOM   2032 C CD2   . TYR   B 1 38  ? -32.44300 0.37600   48.05400 1.000 38.28240 ?  18  TYR   B CD2   1 
ATOM   2033 C CE1   . TYR   B 1 38  ? -32.82700 2.98300   47.19800 1.000 35.84238 ?  18  TYR   B CE1   1 
ATOM   2034 C CE2   . TYR   B 1 38  ? -31.42600 1.31800   48.20800 1.000 40.20838 ?  18  TYR   B CE2   1 
ATOM   2035 C CZ    . TYR   B 1 38  ? -31.62900 2.61900   47.77300 1.000 41.75467 ?  18  TYR   B CZ    1 
ATOM   2036 O OH    . TYR   B 1 38  ? -30.63500 3.56400   47.91500 1.000 37.93351 ?  18  TYR   B OH    1 
ATOM   2037 N N     . CYS   B 1 39  ? -37.44300 -1.78000  48.61900 1.000 21.49319 ?  19  CYS   B N     1 
ATOM   2038 C CA    . CYS   B 1 39  ? -38.86400 -2.10900  48.62900 1.000 20.39364 ?  19  CYS   B CA    1 
ATOM   2039 C C     . CYS   B 1 39  ? -39.58900 -1.27800  49.66800 1.000 22.69191 ?  19  CYS   B C     1 
ATOM   2040 O O     . CYS   B 1 39  ? -40.67800 -0.75100  49.42200 1.000 22.10408 ?  19  CYS   B O     1 
ATOM   2041 C CB    . CYS   B 1 39  ? -39.05900 -3.58700  48.96400 1.000 18.74088 ?  19  CYS   B CB    1 
ATOM   2042 S SG    . CYS   B 1 39  ? -38.60900 -4.67900  47.62300 1.000 24.85643 ?  19  CYS   B SG    1 
ATOM   2043 N N     . ASP   B 1 40  ? -39.02400 -1.21200  50.87600 1.000 20.85309 ?  20  ASP   B N     1 
ATOM   2044 C CA    . ASP   B 1 40  ? -39.65500 -0.43200  51.93800 1.000 20.50912 ?  20  ASP   B CA    1 
ATOM   2045 C C     . ASP   B 1 40  ? -39.75100 1.03800   51.54900 1.000 20.60733 ?  20  ASP   B C     1 
ATOM   2046 O O     . ASP   B 1 40  ? -40.79700 1.68300   51.73000 1.000 19.58577 ?  20  ASP   B O     1 
ATOM   2047 C CB    . ASP   B 1 40  ? -38.85500 -0.58200  53.23500 1.000 20.99967 ?  20  ASP   B CB    1 
ATOM   2048 C CG    . ASP   B 1 40  ? -39.61500 -0.10200  54.44200 1.000 25.82802 ?  20  ASP   B CG    1 
ATOM   2049 O OD1   . ASP   B 1 40  ? -40.79200 -0.47700  54.59800 1.000 22.64161 ?  20  ASP   B OD1   1 
ATOM   2050 O OD2   . ASP   B 1 40  ? -39.03800 0.67300   55.23700 1.000 23.65117 -1 20  ASP   B OD2   1 
ATOM   2051 N N     . PHE   B 1 41  ? -38.67100 1.56500   50.98400 1.000 19.99330 ?  21  PHE   B N     1 
ATOM   2052 C CA    . PHE   B 1 41  ? -38.60900 2.98400   50.63500 1.000 20.88429 ?  21  PHE   B CA    1 
ATOM   2053 C C     . PHE   B 1 41  ? -39.62900 3.32400   49.55400 1.000 19.95183 ?  21  PHE   B C     1 
ATOM   2054 O O     . PHE   B 1 41  ? -40.32600 4.34400   49.62600 1.000 22.97093 ?  21  PHE   B O     1 
ATOM   2055 C CB    . PHE   B 1 41  ? -37.19600 3.29700   50.15500 1.000 23.43884 ?  21  PHE   B CB    1 
ATOM   2056 C CG    . PHE   B 1 41  ? -36.99900 4.72200   49.69600 1.000 19.55280 ?  21  PHE   B CG    1 
ATOM   2057 C CD1   . PHE   B 1 41  ? -37.34500 5.78300   50.53300 1.000 21.30387 ?  21  PHE   B CD1   1 
ATOM   2058 C CD2   . PHE   B 1 41  ? -36.44600 4.98300   48.45300 1.000 23.48575 ?  21  PHE   B CD2   1 
ATOM   2059 C CE1   . PHE   B 1 41  ? -37.14300 7.10400   50.10600 1.000 22.03857 ?  21  PHE   B CE1   1 
ATOM   2060 C CE2   . PHE   B 1 41  ? -36.24200 6.29000   48.02800 1.000 22.61485 ?  21  PHE   B CE2   1 
ATOM   2061 C CZ    . PHE   B 1 41  ? -36.58600 7.34100   48.86600 1.000 20.55581 ?  21  PHE   B CZ    1 
ATOM   2062 N N     . GLN   B 1 42  ? -39.72100 2.47800   48.54900 1.000 19.66983 ?  22  GLN   B N     1 
ATOM   2063 C CA    . GLN   B 1 42  ? -40.53800 2.76500   47.38300 1.000 22.44626 ?  22  GLN   B CA    1 
ATOM   2064 C C     . GLN   B 1 42  ? -41.99400 2.36800   47.55300 1.000 23.97612 ?  22  GLN   B C     1 
ATOM   2065 O O     . GLN   B 1 42  ? -42.86200 2.97200   46.92500 1.000 26.30454 ?  22  GLN   B O     1 
ATOM   2066 C CB    . GLN   B 1 42  ? -39.96400 2.04600   46.16900 1.000 22.64440 ?  22  GLN   B CB    1 
ATOM   2067 C CG    . GLN   B 1 42  ? -38.67100 2.66800   45.67200 1.000 24.09178 ?  22  GLN   B CG    1 
ATOM   2068 C CD    . GLN   B 1 42  ? -38.43900 2.41200   44.20600 1.000 26.55539 ?  22  GLN   B CD    1 
ATOM   2069 O OE1   . GLN   B 1 42  ? -38.79100 1.35700   43.69300 1.000 25.17402 ?  22  GLN   B OE1   1 
ATOM   2070 N NE2   . GLN   B 1 42  ? -37.86600 3.39900   43.50700 1.000 28.27627 ?  22  GLN   B NE2   1 
ATOM   2071 N N     . TYR   B 1 43  ? -42.29900 1.38900   48.39100 1.000 20.29775 ?  23  TYR   B N     1 
ATOM   2072 C CA    . TYR   B 1 43  ? -43.66200 0.88300   48.46100 1.000 19.40708 ?  23  TYR   B CA    1 
ATOM   2073 C C     . TYR   B 1 43  ? -44.28800 0.93500   49.83700 1.000 27.08300 ?  23  TYR   B C     1 
ATOM   2074 O O     . TYR   B 1 43  ? -45.49500 0.68400   49.94800 1.000 24.54570 ?  23  TYR   B O     1 
ATOM   2075 C CB    . TYR   B 1 43  ? -43.72800 -0.56600  47.92700 1.000 21.24761 ?  23  TYR   B CB    1 
ATOM   2076 C CG    . TYR   B 1 43  ? -43.35400 -0.69300  46.46500 1.000 21.58320 ?  23  TYR   B CG    1 
ATOM   2077 C CD1   . TYR   B 1 43  ? -44.26900 -0.38800  45.45600 1.000 24.28089 ?  23  TYR   B CD1   1 
ATOM   2078 C CD2   . TYR   B 1 43  ? -42.08000 -1.08900  46.08700 1.000 19.49304 ?  23  TYR   B CD2   1 
ATOM   2079 C CE1   . TYR   B 1 43  ? -43.91100 -0.50000  44.10600 1.000 24.23842 ?  23  TYR   B CE1   1 
ATOM   2080 C CE2   . TYR   B 1 43  ? -41.71900 -1.21300  44.74600 1.000 20.06564 ?  23  TYR   B CE2   1 
ATOM   2081 C CZ    . TYR   B 1 43  ? -42.64000 -0.90200  43.76100 1.000 26.41493 ?  23  TYR   B CZ    1 
ATOM   2082 O OH    . TYR   B 1 43  ? -42.27500 -1.01900  42.43800 1.000 23.10018 ?  23  TYR   B OH    1 
ATOM   2083 N N     . GLY   B 1 44  ? -43.52100 1.29400   50.88200 1.000 24.35020 ?  24  GLY   B N     1 
ATOM   2084 C CA    . GLY   B 1 44  ? -44.05200 1.36800   52.22600 1.000 23.70504 ?  24  GLY   B CA    1 
ATOM   2085 C C     . GLY   B 1 44  ? -44.88800 2.60900   52.45900 1.000 26.40729 ?  24  GLY   B C     1 
ATOM   2086 O O     . GLY   B 1 44  ? -44.99400 3.50000   51.61000 1.000 25.09312 ?  24  GLY   B O     1 
ATOM   2087 N N     . GLU   B 1 45  ? -45.48700 2.66000   53.64400 1.000 25.34720 ?  25  GLU   B N     1 
ATOM   2088 C CA    . GLU   B 1 45  ? -46.26200 3.82900   54.04300 1.000 30.45731 ?  25  GLU   B CA    1 
ATOM   2089 C C     . GLU   B 1 45  ? -45.35400 5.04000   54.27700 1.000 25.25237 ?  25  GLU   B C     1 
ATOM   2090 O O     . GLU   B 1 45  ? -44.20300 4.91400   54.70000 1.000 26.04542 ?  25  GLU   B O     1 
ATOM   2091 C CB    . GLU   B 1 45  ? -47.05900 3.52200   55.31300 1.000 32.88458 ?  25  GLU   B CB    1 
ATOM   2092 C CG    . GLU   B 1 45  ? -48.13600 2.46900   55.11900 1.000 36.40181 ?  25  GLU   B CG    1 
ATOM   2093 N N     . ASP   B 1 46  ? -45.89600 6.22400   53.99900 1.000 22.65187 ?  26  ASP   B N     1 
ATOM   2094 C CA    . ASP   B 1 46  ? -45.15100 7.47100   54.15000 1.000 27.79370 ?  26  ASP   B CA    1 
ATOM   2095 C C     . ASP   B 1 46  ? -44.78700 7.72600   55.60500 1.000 27.04363 ?  26  ASP   B C     1 
ATOM   2096 O O     . ASP   B 1 46  ? -45.59300 7.49800   56.51300 1.000 30.23733 ?  26  ASP   B O     1 
ATOM   2097 C CB    . ASP   B 1 46  ? -45.99000 8.65000   53.63400 1.000 29.29574 ?  26  ASP   B CB    1 
ATOM   2098 C CG    . ASP   B 1 46  ? -46.31700 8.56100   52.15500 1.000 29.28858 ?  26  ASP   B CG    1 
ATOM   2099 O OD1   . ASP   B 1 46  ? -45.69300 7.76500   51.41900 1.000 29.87745 ?  26  ASP   B OD1   1 
ATOM   2100 O OD2   . ASP   B 1 46  ? -47.21600 9.31900   51.71700 1.000 37.90952 -1 26  ASP   B OD2   1 
ATOM   2101 N N     . CYS   B 1 47  ? -43.57700 8.23900   55.82100 1.000 27.33547 ?  27  CYS   B N     1 
ATOM   2102 C CA    . CYS   B 1 47  ? -43.06100 8.56200   57.14900 1.000 29.12881 ?  27  CYS   B CA    1 
ATOM   2103 C C     . CYS   B 1 47  ? -42.95800 10.06900  57.35400 1.000 25.06353 ?  27  CYS   B C     1 
ATOM   2104 O O     . CYS   B 1 47  ? -42.61800 10.80500  56.42300 1.000 25.60282 ?  27  CYS   B O     1 
ATOM   2105 C CB    . CYS   B 1 47  ? -41.68000 7.95300   57.35100 1.000 28.83529 ?  27  CYS   B CB    1 
ATOM   2106 S SG    . CYS   B 1 47  ? -41.70300 6.15900   57.27100 1.000 35.15445 ?  27  CYS   B SG    1 
ATOM   2107 N N     . PHE   B 1 48  ? -43.23400 10.51500  58.59000 1.000 25.15863 ?  28  PHE   B N     1 
ATOM   2108 C CA    . PHE   B 1 48  ? -43.09200 11.91900  58.98600 1.000 25.55441 ?  28  PHE   B CA    1 
ATOM   2109 C C     . PHE   B 1 48  ? -43.90200 12.85900  58.09300 1.000 28.07099 ?  28  PHE   B C     1 
ATOM   2110 O O     . PHE   B 1 48  ? -43.54400 14.03100  57.91100 1.000 30.76252 ?  28  PHE   B O     1 
ATOM   2111 C CB    . PHE   B 1 48  ? -41.61400 12.34800  59.00700 1.000 26.27049 ?  28  PHE   B CB    1 
ATOM   2112 C CG    . PHE   B 1 48  ? -40.77600 11.61700  60.02300 1.000 26.87755 ?  28  PHE   B CG    1 
ATOM   2113 C CD1   . PHE   B 1 48  ? -41.11300 11.63400  61.37500 1.000 31.60634 ?  28  PHE   B CD1   1 
ATOM   2114 C CD2   . PHE   B 1 48  ? -39.63600 10.92500  59.63500 1.000 28.25276 ?  28  PHE   B CD2   1 
ATOM   2115 C CE1   . PHE   B 1 48  ? -40.32900 10.96500  62.31400 1.000 32.57460 ?  28  PHE   B CE1   1 
ATOM   2116 C CE2   . PHE   B 1 48  ? -38.84200 10.24100  60.58200 1.000 23.33363 ?  28  PHE   B CE2   1 
ATOM   2117 C CZ    . PHE   B 1 48  ? -39.19200 10.26800  61.90900 1.000 27.47790 ?  28  PHE   B CZ    1 
ATOM   2118 N N     . GLY   B 1 49  ? -44.98800 12.35500  57.51600 1.000 29.09998 ?  29  GLY   B N     1 
ATOM   2119 C CA    . GLY   B 1 49  ? -45.80700 13.18800  56.65800 1.000 31.07593 ?  29  GLY   B CA    1 
ATOM   2120 C C     . GLY   B 1 49  ? -45.20900 13.50800  55.30900 1.000 32.17579 ?  29  GLY   B C     1 
ATOM   2121 O O     . GLY   B 1 49  ? -45.72600 14.39200  54.61900 1.000 30.18653 ?  29  GLY   B O     1 
ATOM   2122 N N     . VAL   B 1 50  ? -44.13900 12.82000  54.91000 1.000 25.13005 ?  30  VAL   B N     1 
ATOM   2123 C CA    . VAL   B 1 50  ? -43.45300 13.09000  53.64800 1.000 23.63875 ?  30  VAL   B CA    1 
ATOM   2124 C C     . VAL   B 1 50  ? -44.05800 12.22500  52.54700 1.000 24.78415 ?  30  VAL   B C     1 
ATOM   2125 O O     . VAL   B 1 50  ? -44.21800 11.01200  52.72100 1.000 24.34571 ?  30  VAL   B O     1 
ATOM   2126 C CB    . VAL   B 1 50  ? -41.94100 12.83400  53.79300 1.000 21.40321 ?  30  VAL   B CB    1 
ATOM   2127 C CG1   . VAL   B 1 50  ? -41.20200 13.08500  52.46400 1.000 20.26373 ?  30  VAL   B CG1   1 
ATOM   2128 C CG2   . VAL   B 1 50  ? -41.38600 13.75100  54.92200 1.000 22.30862 ?  30  VAL   B CG2   1 
ATOM   2129 N N     . LEU   B 1 51  ? -44.36500 12.84600  51.40100 1.000 23.28861 ?  31  LEU   B N     1 
ATOM   2130 C CA    . LEU   B 1 51  ? -44.90900 12.10800  50.26500 1.000 25.64252 ?  31  LEU   B CA    1 
ATOM   2131 C C     . LEU   B 1 51  ? -43.90400 11.08400  49.74000 1.000 24.45276 ?  31  LEU   B C     1 
ATOM   2132 O O     . LEU   B 1 51  ? -42.70300 11.35100  49.68200 1.000 24.74494 ?  31  LEU   B O     1 
ATOM   2133 C CB    . LEU   B 1 51  ? -45.27900 13.08800  49.15100 1.000 23.21885 ?  31  LEU   B CB    1 
ATOM   2134 C CG    . LEU   B 1 51  ? -46.01600 12.50600  47.95000 1.000 23.97164 ?  31  LEU   B CG    1 
ATOM   2135 C CD1   . LEU   B 1 51  ? -47.37500 11.96200  48.38700 1.000 29.48411 ?  31  LEU   B CD1   1 
ATOM   2136 C CD2   . LEU   B 1 51  ? -46.20400 13.62200  46.90700 1.000 30.52109 ?  31  LEU   B CD2   1 
ATOM   2137 N N     . ASN   B 1 52  ? -44.40600 9.91500   49.34300 1.000 21.33660 ?  32  ASN   B N     1 
ATOM   2138 C CA    . ASN   B 1 52  ? -43.56000 8.90700   48.71600 1.000 20.85869 ?  32  ASN   B CA    1 
ATOM   2139 C C     . ASN   B 1 52  ? -42.68700 9.53100   47.63300 1.000 22.55579 ?  32  ASN   B C     1 
ATOM   2140 O O     . ASN   B 1 52  ? -43.18100 10.25400  46.75500 1.000 21.77165 ?  32  ASN   B O     1 
ATOM   2141 C CB    . ASN   B 1 52  ? -44.42700 7.81200   48.10800 1.000 21.78768 ?  32  ASN   B CB    1 
ATOM   2142 C CG    . ASN   B 1 52  ? -43.59400 6.74600   47.42900 1.000 24.52343 ?  32  ASN   B CG    1 
ATOM   2143 O OD1   . ASN   B 1 52  ? -43.33500 6.82700   46.22900 1.000 24.15747 ?  32  ASN   B OD1   1 
ATOM   2144 N ND2   . ASN   B 1 52  ? -43.12100 5.75900   48.21500 1.000 23.94827 ?  32  ASN   B ND2   1 
ATOM   2145 N N     . PHE   B 1 53  ? -41.37900 9.24800   47.69700 1.000 22.00642 ?  33  PHE   B N     1 
ATOM   2146 C CA    . PHE   B 1 53  ? -40.41900 9.95600   46.84000 1.000 20.70593 ?  33  PHE   B CA    1 
ATOM   2147 C C     . PHE   B 1 53  ? -40.61000 9.61700   45.36600 1.000 19.22982 ?  33  PHE   B C     1 
ATOM   2148 O O     . PHE   B 1 53  ? -40.58300 10.50400  44.50300 1.000 20.98778 ?  33  PHE   B O     1 
ATOM   2149 C CB    . PHE   B 1 53  ? -38.99300 9.62400   47.28300 1.000 20.13263 ?  33  PHE   B CB    1 
ATOM   2150 C CG    . PHE   B 1 53  ? -37.93200 10.42000  46.56900 1.000 18.22554 ?  33  PHE   B CG    1 
ATOM   2151 C CD1   . PHE   B 1 53  ? -37.87200 11.81200  46.70600 1.000 18.09397 ?  33  PHE   B CD1   1 
ATOM   2152 C CD2   . PHE   B 1 53  ? -36.99600 9.78100   45.77700 1.000 21.24434 ?  33  PHE   B CD2   1 
ATOM   2153 C CE1   . PHE   B 1 53  ? -36.87600 12.53600  46.05500 1.000 22.54603 ?  33  PHE   B CE1   1 
ATOM   2154 C CE2   . PHE   B 1 53  ? -35.98700 10.50800  45.11600 1.000 19.54996 ?  33  PHE   B CE2   1 
ATOM   2155 C CZ    . PHE   B 1 53  ? -35.93000 11.88300  45.25700 1.000 19.00950 ?  33  PHE   B CZ    1 
ATOM   2156 N N     . ALA   B 1 54  ? -40.74700 8.32700   45.04300 1.000 18.78292 ?  34  ALA   B N     1 
ATOM   2157 C CA    . ALA   B 1 54  ? -40.92200 7.95600   43.64100 1.000 20.20437 ?  34  ALA   B CA    1 
ATOM   2158 C C     . ALA   B 1 54  ? -42.19900 8.57300   43.08400 1.000 23.15600 ?  34  ALA   B C     1 
ATOM   2159 O O     . ALA   B 1 54  ? -42.22500 9.06800   41.95100 1.000 21.18451 ?  34  ALA   B O     1 
ATOM   2160 C CB    . ALA   B 1 54  ? -40.96200 6.42900   43.49000 1.000 21.20722 ?  34  ALA   B CB    1 
ATOM   2161 N N     . LEU   B 1 55  ? -43.27100 8.55100   43.87400 1.000 24.67614 ?  35  LEU   B N     1 
ATOM   2162 C CA    . LEU   B 1 55  ? -44.51700 9.17500   43.43600 1.000 25.66426 ?  35  LEU   B CA    1 
ATOM   2163 C C     . LEU   B 1 55  ? -44.34300 10.68200  43.27200 1.000 23.47082 ?  35  LEU   B C     1 
ATOM   2164 O O     . LEU   B 1 55  ? -44.81800 11.26600  42.28700 1.000 24.63665 ?  35  LEU   B O     1 
ATOM   2165 C CB    . LEU   B 1 55  ? -45.63300 8.85700   44.43800 1.000 24.32537 ?  35  LEU   B CB    1 
ATOM   2166 C CG    . LEU   B 1 55  ? -46.98300 9.54500   44.19000 1.000 27.50272 ?  35  LEU   B CG    1 
ATOM   2167 C CD1   . LEU   B 1 55  ? -47.60100 9.09000   42.88000 1.000 29.21835 ?  35  LEU   B CD1   1 
ATOM   2168 C CD2   . LEU   B 1 55  ? -47.91200 9.27900   45.35600 1.000 32.95813 ?  35  LEU   B CD2   1 
ATOM   2169 N N     . ALA   B 1 56  ? -43.64400 11.33000  44.20800 1.000 21.14478 ?  36  ALA   B N     1 
ATOM   2170 C CA    . ALA   B 1 56  ? -43.41100 12.77100  44.08900 1.000 20.09102 ?  36  ALA   B CA    1 
ATOM   2171 C C     . ALA   B 1 56  ? -42.59400 13.08900  42.84300 1.000 22.28314 ?  36  ALA   B C     1 
ATOM   2172 O O     . ALA   B 1 56  ? -42.89600 14.04400  42.10700 1.000 22.89765 ?  36  ALA   B O     1 
ATOM   2173 C CB    . ALA   B 1 56  ? -42.70300 13.30300  45.34200 1.000 21.83770 ?  36  ALA   B CB    1 
ATOM   2174 N N     . CYS   B 1 57  ? -41.55800 12.29400  42.57600 1.000 20.19532 ?  37  CYS   B N     1 
ATOM   2175 C CA    . CYS   B 1 57  ? -40.71400 12.57700  41.41600 1.000 23.77587 ?  37  CYS   B CA    1 
ATOM   2176 C C     . CYS   B 1 57  ? -41.47200 12.33900  40.11300 1.000 26.27611 ?  37  CYS   B C     1 
ATOM   2177 O O     . CYS   B 1 57  ? -41.38900 13.14600  39.17600 1.000 22.40429 ?  37  CYS   B O     1 
ATOM   2178 C CB    . CYS   B 1 57  ? -39.44700 11.71500  41.44100 1.000 25.98199 ?  37  CYS   B CB    1 
ATOM   2179 S SG    . CYS   B 1 57  ? -38.21600 12.20600  42.68500 1.000 26.00637 ?  37  CYS   B SG    1 
ATOM   2180 N N     . ALA   B 1 58  ? -42.18700 11.22300  40.03200 1.000 24.21795 ?  38  ALA   B N     1 
ATOM   2181 C CA    . ALA   B 1 58  ? -42.88200 10.90700  38.76700 1.000 21.86610 ?  38  ALA   B CA    1 
ATOM   2182 C C     . ALA   B 1 58  ? -43.96200 11.96000  38.52300 1.000 23.46845 ?  38  ALA   B C     1 
ATOM   2183 O O     . ALA   B 1 58  ? -44.12500 12.37900  37.38100 1.000 26.38419 ?  38  ALA   B O     1 
ATOM   2184 C CB    . ALA   B 1 58  ? -43.46100 9.52600   38.82300 1.000 23.33726 ?  38  ALA   B CB    1 
ATOM   2185 N N     . THR   B 1 59  ? -44.62100 12.38600  39.58900 1.000 20.94123 ?  39  THR   B N     1 
ATOM   2186 C CA    . THR   B 1 59  ? -45.72200 13.36300  39.45600 1.000 27.59264 ?  39  THR   B CA    1 
ATOM   2187 C C     . THR   B 1 59  ? -45.16300 14.66200  38.87500 1.000 31.52087 ?  39  THR   B C     1 
ATOM   2188 O O     . THR   B 1 59  ? -45.74700 15.19400  37.92500 1.000 32.01751 ?  39  THR   B O     1 
ATOM   2189 C CB    . THR   B 1 59  ? -46.43800 13.54400  40.80000 1.000 27.52511 ?  39  THR   B CB    1 
ATOM   2190 O OG1   . THR   B 1 59  ? -47.02400 12.29800  41.16900 1.000 31.29383 ?  39  THR   B OG1   1 
ATOM   2191 C CG2   . THR   B 1 59  ? -47.50300 14.61700  40.75700 1.000 34.40719 ?  39  THR   B CG2   1 
ATOM   2192 N N     . LYS   B 1 60  ? -44.05800 15.13400  39.43300 1.000 26.10454 ?  40  LYS   B N     1 
ATOM   2193 C CA    . LYS   B 1 60  ? -43.45200 16.40100  38.95900 1.000 26.70245 ?  40  LYS   B CA    1 
ATOM   2194 C C     . LYS   B 1 60  ? -42.97900 16.23300  37.51100 1.000 30.77172 ?  40  LYS   B C     1 
ATOM   2195 O O     . LYS   B 1 60  ? -43.21400 17.13000  36.71300 1.000 28.83022 ?  40  LYS   B O     1 
ATOM   2196 C CB    . LYS   B 1 60  ? -42.34400 16.80800  39.93200 1.000 23.48565 ?  40  LYS   B CB    1 
ATOM   2197 C CG    . LYS   B 1 60  ? -42.84000 17.33200  41.27000 1.000 30.38769 ?  40  LYS   B CG    1 
ATOM   2198 C CD    . LYS   B 1 60  ? -41.83900 17.17900  42.38200 1.000 30.57197 ?  40  LYS   B CD    1 
ATOM   2199 C CE    . LYS   B 1 60  ? -42.45800 17.30300  43.75600 1.000 36.92599 ?  40  LYS   B CE    1 
ATOM   2200 N NZ    . LYS   B 1 60  ? -43.26300 18.53800  43.88400 1.000 36.42280 ?  40  LYS   B NZ    1 
ATOM   2201 N N     . ALA   B 1 61  ? -42.35900 15.09900  37.20200 1.000 23.09637 ?  41  ALA   B N     1 
ATOM   2202 C CA    . ALA   B 1 61  ? -41.84300 14.86400  35.84100 1.000 21.56093 ?  41  ALA   B CA    1 
ATOM   2203 C C     . ALA   B 1 61  ? -42.99600 14.95500  34.84600 1.000 31.01099 ?  41  ALA   B C     1 
ATOM   2204 O O     . ALA   B 1 61  ? -42.82200 15.56800  33.79700 1.000 27.41420 ?  41  ALA   B O     1 
ATOM   2205 C CB    . ALA   B 1 61  ? -41.18200 13.52200  35.75300 1.000 22.80701 ?  41  ALA   B CB    1 
ATOM   2206 N N     . ILE   B 1 62  ? -44.11300 14.32000  35.18900 1.000 28.57793 ?  42  ILE   B N     1 
ATOM   2207 C CA    . ILE   B 1 62  ? -45.27400 14.39800  34.31100 1.000 28.33108 ?  42  ILE   B CA    1 
ATOM   2208 C C     . ILE   B 1 62  ? -45.69700 15.85400  34.14100 1.000 29.35428 ?  42  ILE   B C     1 
ATOM   2209 O O     . ILE   B 1 62  ? -45.93500 16.31600  33.02000 1.000 34.18422 ?  42  ILE   B O     1 
ATOM   2210 C CB    . ILE   B 1 62  ? -46.41000 13.50800  34.86000 1.000 28.37273 ?  42  ILE   B CB    1 
ATOM   2211 C CG1   . ILE   B 1 62  ? -46.07700 12.01700  34.68900 1.000 25.18798 ?  42  ILE   B CG1   1 
ATOM   2212 C CG2   . ILE   B 1 62  ? -47.75700 13.83600  34.22500 1.000 33.46890 ?  42  ILE   B CG2   1 
ATOM   2213 C CD1   . ILE   B 1 62  ? -46.86000 11.16100  35.67400 1.000 28.01903 ?  42  ILE   B CD1   1 
ATOM   2214 N N     . GLY   B 1 63  ? -45.74300 16.61000  35.24000 1.000 26.93087 ?  43  GLY   B N     1 
ATOM   2215 C CA    . GLY   B 1 63  ? -46.05000 18.03700  35.14900 1.000 27.29956 ?  43  GLY   B CA    1 
ATOM   2216 C C     . GLY   B 1 63  ? -45.09800 18.79700  34.23900 1.000 36.83533 ?  43  GLY   B C     1 
ATOM   2217 O O     . GLY   B 1 63  ? -45.53100 19.55900  33.36700 1.000 34.74131 ?  43  GLY   B O     1 
ATOM   2218 N N     . TYR   B 1 64  ? -43.78600 18.57900  34.40500 1.000 26.58749 ?  44  TYR   B N     1 
ATOM   2219 C CA    . TYR   B 1 64  ? -42.77900 19.31200  33.63500 1.000 27.21548 ?  44  TYR   B CA    1 
ATOM   2220 C C     . TYR   B 1 64  ? -42.75700 18.94300  32.15900 1.000 28.80190 ?  44  TYR   B C     1 
ATOM   2221 O O     . TYR   B 1 64  ? -42.23500 19.72400  31.34900 1.000 33.35356 ?  44  TYR   B O     1 
ATOM   2222 C CB    . TYR   B 1 64  ? -41.37000 19.08700  34.21600 1.000 25.93610 ?  44  TYR   B CB    1 
ATOM   2223 C CG    . TYR   B 1 64  ? -41.12000 19.87700  35.47000 1.000 25.34462 ?  44  TYR   B CG    1 
ATOM   2224 C CD1   . TYR   B 1 64  ? -41.13000 21.26500  35.44700 1.000 28.94593 ?  44  TYR   B CD1   1 
ATOM   2225 C CD2   . TYR   B 1 64  ? -40.89400 19.24200  36.68200 1.000 31.74888 ?  44  TYR   B CD2   1 
ATOM   2226 C CE1   . TYR   B 1 64  ? -40.91900 21.99300  36.59800 1.000 32.81103 ?  44  TYR   B CE1   1 
ATOM   2227 C CE2   . TYR   B 1 64  ? -40.68200 19.96900  37.84300 1.000 31.06091 ?  44  TYR   B CE2   1 
ATOM   2228 C CZ    . TYR   B 1 64  ? -40.69400 21.34300  37.79200 1.000 35.84727 ?  44  TYR   B CZ    1 
ATOM   2229 O OH    . TYR   B 1 64  ? -40.48500 22.07700  38.93900 1.000 33.30842 ?  44  TYR   B OH    1 
ATOM   2230 N N     . THR   B 1 65  ? -43.26700 17.77200  31.78900 1.000 28.97525 ?  45  THR   B N     1 
ATOM   2231 C CA    . THR   B 1 65  ? -43.23200 17.30500  30.41000 1.000 28.97287 ?  45  THR   B CA    1 
ATOM   2232 C C     . THR   B 1 65  ? -44.61100 17.40400  29.75300 1.000 29.48410 ?  45  THR   B C     1 
ATOM   2233 O O     . THR   B 1 65  ? -44.92000 16.65300  28.82300 1.000 34.67924 ?  45  THR   B O     1 
ATOM   2234 C CB    . THR   B 1 65  ? -42.69800 15.87400  30.33800 1.000 31.09148 ?  45  THR   B CB    1 
ATOM   2235 O OG1   . THR   B 1 65  ? -43.50400 15.01300  31.15300 1.000 35.21693 ?  45  THR   B OG1   1 
ATOM   2236 C CG2   . THR   B 1 65  ? -41.25100 15.79500  30.83900 1.000 29.82207 ?  45  THR   B CG2   1 
ATOM   2237 N N     . LYS   B 1 66  ? -45.44200 18.33700  30.22700 1.000 31.82597 ?  46  LYS   B N     1 
ATOM   2238 C CA    . LYS   B 1 66  ? -46.81500 18.43000  29.74300 1.000 40.01570 ?  46  LYS   B CA    1 
ATOM   2239 C C     . LYS   B 1 66  ? -46.90100 18.86000  28.28100 1.000 35.93530 ?  46  LYS   B C     1 
ATOM   2240 O O     . LYS   B 1 66  ? -47.94300 18.66900  27.64800 1.000 31.52454 ?  46  LYS   B O     1 
ATOM   2241 C CB    . LYS   B 1 66  ? -47.62000 19.40200  30.60800 1.000 35.35257 ?  46  LYS   B CB    1 
ATOM   2242 C CG    . LYS   B 1 66  ? -47.03100 20.78600  30.71300 1.000 34.90368 ?  46  LYS   B CG    1 
ATOM   2243 C CD    . LYS   B 1 66  ? -47.73900 21.60200  31.79700 1.000 47.75846 ?  46  LYS   B CD    1 
ATOM   2244 N N     . GLU   B 1 67  ? -45.84500 19.42800  27.71700 1.000 29.25016 ?  47  GLU   B N     1 
ATOM   2245 C CA    . GLU   B 1 67  ? -45.89800 19.83200  26.32000 1.000 36.43642 ?  47  GLU   B CA    1 
ATOM   2246 C C     . GLU   B 1 67  ? -45.29100 18.79600  25.37500 1.000 37.33990 ?  47  GLU   B C     1 
ATOM   2247 O O     . GLU   B 1 67  ? -45.14100 19.08400  24.18100 1.000 34.72060 ?  47  GLU   B O     1 
ATOM   2248 C CB    . GLU   B 1 67  ? -45.21000 21.18600  26.14100 1.000 42.55517 ?  47  GLU   B CB    1 
ATOM   2249 N N     . THR   B 1 68  ? -44.92400 17.59000  25.88500 1.000 26.50854 ?  48  THR   B N     1 
ATOM   2250 C CA    . THR   B 1 68  ? -44.36900 16.49100  25.09900 1.000 31.32933 ?  48  THR   B CA    1 
ATOM   2251 C C     . THR   B 1 68  ? -45.45000 15.47300  24.75500 1.000 30.15312 ?  48  THR   B C     1 
ATOM   2252 O O     . THR   B 1 68  ? -46.50700 15.44100  25.39000 1.000 36.79166 ?  48  THR   B O     1 
ATOM   2253 C CB    . THR   B 1 68  ? -43.23700 15.77400  25.86800 1.000 35.81569 ?  48  THR   B CB    1 
ATOM   2254 O OG1   . THR   B 1 68  ? -43.80000 14.88300  26.84200 1.000 35.20380 ?  48  THR   B OG1   1 
ATOM   2255 C CG2   . THR   B 1 68  ? -42.28800 16.75400  26.53800 1.000 32.72151 ?  48  THR   B CG2   1 
ATOM   2256 N N     . PRO   B 1 69  ? -45.21800 14.60900  23.75700 1.000 31.98352 ?  49  PRO   B N     1 
ATOM   2257 C CA    . PRO   B 1 69  ? -46.22900 13.58200  23.42600 1.000 34.74926 ?  49  PRO   B CA    1 
ATOM   2258 C C     . PRO   B 1 69  ? -46.34900 12.45300  24.44200 1.000 50.31303 ?  49  PRO   B C     1 
ATOM   2259 O O     . PRO   B 1 69  ? -47.33100 11.70000  24.38600 1.000 47.91707 ?  49  PRO   B O     1 
ATOM   2260 C CB    . PRO   B 1 69  ? -45.77000 13.04000  22.06500 1.000 36.09377 ?  49  PRO   B CB    1 
ATOM   2261 C CG    . PRO   B 1 69  ? -44.45700 13.67800  21.76100 1.000 45.34275 ?  49  PRO   B CG    1 
ATOM   2262 C CD    . PRO   B 1 69  ? -44.02200 14.52800  22.89500 1.000 37.75191 ?  49  PRO   B CD    1 
ATOM   2263 N N     . LYS   B 1 70  ? -45.39100 12.29500  25.34500 1.000 32.49792 ?  50  LYS   B N     1 
ATOM   2264 C CA    . LYS   B 1 70  ? -45.45700 11.24000  26.37400 1.000 34.57037 ?  50  LYS   B CA    1 
ATOM   2265 C C     . LYS   B 1 70  ? -45.53400 9.83300   25.77100 1.000 32.48206 ?  50  LYS   B C     1 
ATOM   2266 O O     . LYS   B 1 70  ? -46.28200 8.97100   26.24800 1.000 35.01967 ?  50  LYS   B O     1 
ATOM   2267 C CB    . LYS   B 1 70  ? -46.63000 11.48700  27.32900 1.000 37.66500 ?  50  LYS   B CB    1 
ATOM   2268 C CG    . LYS   B 1 70  ? -46.41100 12.67200  28.26500 1.000 41.57861 ?  50  LYS   B CG    1 
ATOM   2269 C CD    . LYS   B 1 70  ? -46.87100 12.35800  29.67800 1.000 45.82131 ?  50  LYS   B CD    1 
ATOM   2270 C CE    . LYS   B 1 70  ? -46.46300 13.45400  30.64700 1.000 39.72938 ?  50  LYS   B CE    1 
ATOM   2271 N NZ    . LYS   B 1 70  ? -46.46600 14.79700  29.99600 1.000 44.93810 ?  50  LYS   B NZ    1 
ATOM   2272 N N     . ASN   B 1 71  ? -44.73400 9.57600   24.73600 1.000 29.54229 ?  51  ASN   B N     1 
ATOM   2273 C CA    . ASN   B 1 71  ? -44.69700 8.23400   24.15500 1.000 28.33927 ?  51  ASN   B CA    1 
ATOM   2274 C C     . ASN   B 1 71  ? -43.76700 7.29400   24.90900 1.000 31.50524 ?  51  ASN   B C     1 
ATOM   2275 O O     . ASN   B 1 71  ? -44.09700 6.11500   25.08700 1.000 29.04027 ?  51  ASN   B O     1 
ATOM   2276 C CB    . ASN   B 1 71  ? -44.23900 8.29100   22.70200 1.000 28.41249 ?  51  ASN   B CB    1 
ATOM   2277 C CG    . ASN   B 1 71  ? -45.26800 8.93200   21.78900 1.000 46.15504 ?  51  ASN   B CG    1 
ATOM   2278 O OD1   . ASN   B 1 71  ? -46.46900 8.70800   21.94300 1.000 37.94398 ?  51  ASN   B OD1   1 
ATOM   2279 N ND2   . ASN   B 1 71  ? -44.80500 9.75900   20.85700 1.000 36.00250 ?  51  ASN   B ND2   1 
ATOM   2280 N N     . ARG   B 1 72  ? -42.58500 7.77900   25.29900 1.000 26.74779 ?  52  ARG   B N     1 
ATOM   2281 C CA    . ARG   B 1 72  ? -41.51100 6.93500   25.82400 1.000 23.86615 ?  52  ARG   B CA    1 
ATOM   2282 C C     . ARG   B 1 72  ? -40.78400 7.64700   26.95200 1.000 24.83354 ?  52  ARG   B C     1 
ATOM   2283 O O     . ARG   B 1 72  ? -40.30400 8.76900   26.76100 1.000 25.66639 ?  52  ARG   B O     1 
ATOM   2284 C CB    . ARG   B 1 72  ? -40.49500 6.58600   24.72500 1.000 27.75957 ?  52  ARG   B CB    1 
ATOM   2285 C CG    . ARG   B 1 72  ? -41.03200 5.61700   23.69800 1.000 29.41273 ?  52  ARG   B CG    1 
ATOM   2286 C CD    . ARG   B 1 72  ? -40.10000 5.43200   22.53300 1.000 30.34816 ?  52  ARG   B CD    1 
ATOM   2287 N NE    . ARG   B 1 72  ? -38.76000 5.02700   22.94700 1.000 25.84721 ?  52  ARG   B NE    1 
ATOM   2288 C CZ    . ARG   B 1 72  ? -38.42900 3.78600   23.28100 1.000 29.53234 ?  52  ARG   B CZ    1 
ATOM   2289 N NH1   . ARG   B 1 72  ? -39.33700 2.82300   23.36400 1.000 29.23189 ?  52  ARG   B NH1   1 
ATOM   2290 N NH2   . ARG   B 1 72  ? -37.16300 3.51200   23.57200 1.000 27.93658 ?  52  ARG   B NH2   1 
ATOM   2291 N N     . ALA   B 1 73  ? -40.67100 6.98100   28.11500 1.000 27.68699 ?  53  ALA   B N     1 
ATOM   2292 C CA    . ALA   B 1 73  ? -39.85100 7.48000   29.21600 1.000 27.28522 ?  53  ALA   B CA    1 
ATOM   2293 C C     . ALA   B 1 73  ? -38.88900 6.39500   29.68600 1.000 27.80445 ?  53  ALA   B C     1 
ATOM   2294 O O     . ALA   B 1 73  ? -39.16700 5.19600   29.56300 1.000 26.01668 ?  53  ALA   B O     1 
ATOM   2295 C CB    . ALA   B 1 73  ? -40.69600 7.92700   30.39200 1.000 21.29498 ?  53  ALA   B CB    1 
ATOM   2296 N N     . LEU   B 1 74  ? -37.75900 6.83500   30.24100 1.000 24.31706 ?  54  LEU   B N     1 
ATOM   2297 C CA    . LEU   B 1 74  ? -36.73800 5.96000   30.81400 1.000 21.58953 ?  54  LEU   B CA    1 
ATOM   2298 C C     . LEU   B 1 74  ? -36.53900 6.37500   32.26600 1.000 22.44499 ?  54  LEU   B C     1 
ATOM   2299 O O     . LEU   B 1 74  ? -36.21800 7.53900   32.53700 1.000 23.63664 ?  54  LEU   B O     1 
ATOM   2300 C CB    . LEU   B 1 74  ? -35.41900 6.07400   30.05800 1.000 22.96119 ?  54  LEU   B CB    1 
ATOM   2301 C CG    . LEU   B 1 74  ? -34.22000 5.35000   30.69800 1.000 22.36520 ?  54  LEU   B CG    1 
ATOM   2302 C CD1   . LEU   B 1 74  ? -34.44000 3.82800   30.78600 1.000 26.25718 ?  54  LEU   B CD1   1 
ATOM   2303 C CD2   . LEU   B 1 74  ? -32.92200 5.68000   29.95400 1.000 23.99510 ?  54  LEU   B CD2   1 
ATOM   2304 N N     . ASP   B 1 75  ? -36.74600 5.43300   33.19100 1.000 21.90024 ?  55  ASP   B N     1 
ATOM   2305 C CA    . ASP   B 1 75  ? -36.44000 5.62000   34.61600 1.000 23.53529 ?  55  ASP   B CA    1 
ATOM   2306 C C     . ASP   B 1 75  ? -35.09000 4.92600   34.83200 1.000 26.48315 ?  55  ASP   B C     1 
ATOM   2307 O O     . ASP   B 1 75  ? -35.00800 3.69500   34.84700 1.000 24.20472 ?  55  ASP   B O     1 
ATOM   2308 C CB    . ASP   B 1 75  ? -37.58000 5.05200   35.46500 1.000 22.80768 ?  55  ASP   B CB    1 
ATOM   2309 C CG    . ASP   B 1 75  ? -37.30100 5.04300   36.98000 1.000 34.47711 ?  55  ASP   B CG    1 
ATOM   2310 O OD1   . ASP   B 1 75  ? -36.39500 5.75800   37.49300 1.000 28.42906 ?  55  ASP   B OD1   1 
ATOM   2311 O OD2   . ASP   B 1 75  ? -38.03500 4.28900   37.67000 1.000 30.54502 -1 55  ASP   B OD2   1 
ATOM   2312 N N     . LEU   B 1 76  ? -34.02000 5.72600   34.92600 1.000 20.45652 ?  56  LEU   B N     1 
ATOM   2313 C CA    . LEU   B 1 76  ? -32.64800 5.22700   34.95800 1.000 23.13645 ?  56  LEU   B CA    1 
ATOM   2314 C C     . LEU   B 1 76  ? -32.16500 5.15500   36.40200 1.000 24.88410 ?  56  LEU   B C     1 
ATOM   2315 O O     . LEU   B 1 76  ? -32.16700 6.16900   37.10600 1.000 23.39960 ?  56  LEU   B O     1 
ATOM   2316 C CB    . LEU   B 1 76  ? -31.73300 6.11400   34.11900 1.000 24.52552 ?  56  LEU   B CB    1 
ATOM   2317 C CG    . LEU   B 1 76  ? -30.36500 5.59100   33.68700 1.000 22.88850 ?  56  LEU   B CG    1 
ATOM   2318 C CD1   . LEU   B 1 76  ? -30.36000 4.15600   33.14900 1.000 22.88092 ?  56  LEU   B CD1   1 
ATOM   2319 C CD2   . LEU   B 1 76  ? -29.75900 6.54700   32.67600 1.000 24.51229 ?  56  LEU   B CD2   1 
ATOM   2320 N N     . GLY   B 1 77  ? -31.72900 3.95900   36.82900 1.000 22.56077 ?  57  GLY   B N     1 
ATOM   2321 C CA    . GLY   B 1 77  ? -31.52000 3.69200   38.24200 1.000 21.83629 ?  57  GLY   B CA    1 
ATOM   2322 C C     . GLY   B 1 77  ? -32.85500 3.48700   38.94000 1.000 22.33622 ?  57  GLY   B C     1 
ATOM   2323 O O     . GLY   B 1 77  ? -33.08000 4.01800   40.03000 1.000 23.62540 ?  57  GLY   B O     1 
ATOM   2324 N N     . CYS   B 1 78  ? -33.73800 2.67500   38.33600 1.000 22.10899 ?  58  CYS   B N     1 
ATOM   2325 C CA    . CYS   B 1 78  ? -35.12300 2.55400   38.78400 1.000 23.02485 ?  58  CYS   B CA    1 
ATOM   2326 C C     . CYS   B 1 78  ? -35.28800 1.77300   40.09300 1.000 21.12817 ?  58  CYS   B C     1 
ATOM   2327 O O     . CYS   B 1 78  ? -36.37800 1.82200   40.67700 1.000 24.03056 ?  58  CYS   B O     1 
ATOM   2328 C CB    . CYS   B 1 78  ? -35.97400 1.87000   37.70100 1.000 25.37592 ?  58  CYS   B CB    1 
ATOM   2329 S SG    . CYS   B 1 78  ? -35.46200 0.14400   37.35800 1.000 25.24258 ?  58  CYS   B SG    1 
ATOM   2330 N N     . ALA   B 1 79  ? -34.23900 1.11000   40.59200 1.000 21.87941 ?  59  ALA   B N     1 
ATOM   2331 C CA    . ALA   B 1 79  ? -34.28200 0.29600   41.82700 1.000 18.75241 ?  59  ALA   B CA    1 
ATOM   2332 C C     . ALA   B 1 79  ? -35.46800 -0.66000  41.71500 1.000 21.11973 ?  59  ALA   B C     1 
ATOM   2333 O O     . ALA   B 1 79  ? -35.57500 -1.37300  40.70700 1.000 23.38569 ?  59  ALA   B O     1 
ATOM   2334 C CB    . ALA   B 1 79  ? -34.28200 1.18000   43.07600 1.000 20.67201 ?  59  ALA   B CB    1 
ATOM   2335 N N     . THR   B 1 80  ? -36.38100 -0.69200  42.68600 1.000 21.86680 ?  60  THR   B N     1 
ATOM   2336 C CA    . THR   B 1 80  ? -37.46000 -1.67600  42.67900 1.000 24.52221 ?  60  THR   B CA    1 
ATOM   2337 C C     . THR   B 1 80  ? -38.69400 -1.18300  41.91900 1.000 23.61808 ?  60  THR   B C     1 
ATOM   2338 O O     . THR   B 1 80  ? -39.76400 -1.81000  41.99500 1.000 23.33275 ?  60  THR   B O     1 
ATOM   2339 C CB    . THR   B 1 80  ? -37.80200 -2.07600  44.11400 1.000 22.08381 ?  60  THR   B CB    1 
ATOM   2340 O OG1   . THR   B 1 80  ? -37.95800 -0.89700  44.91400 1.000 23.84855 ?  60  THR   B OG1   1 
ATOM   2341 C CG2   . THR   B 1 80  ? -36.65600 -2.90900  44.71400 1.000 21.43829 ?  60  THR   B CG2   1 
ATOM   2342 N N     . GLY   B 1 81  ? -38.55800 -0.08400  41.17300 1.000 21.20714 ?  61  GLY   B N     1 
ATOM   2343 C CA    . GLY   B 1 81  ? -39.43100 0.21000   40.04200 1.000 23.88016 ?  61  GLY   B CA    1 
ATOM   2344 C C     . GLY   B 1 81  ? -40.62700 1.11000   40.29300 1.000 23.73002 ?  61  GLY   B C     1 
ATOM   2345 O O     . GLY   B 1 81  ? -41.39200 1.35800   39.34500 1.000 22.98531 ?  61  GLY   B O     1 
ATOM   2346 N N     . ARG   B 1 82  ? -40.81100 1.63600   41.50900 1.000 22.21407 ?  62  ARG   B N     1 
ATOM   2347 C CA    . ARG   B 1 82  ? -42.02300 2.41100   41.78200 1.000 21.17627 ?  62  ARG   B CA    1 
ATOM   2348 C C     . ARG   B 1 82  ? -42.16600 3.60000   40.83500 1.000 22.59010 ?  62  ARG   B C     1 
ATOM   2349 O O     . ARG   B 1 82  ? -43.26600 3.86300   40.34000 1.000 24.93914 ?  62  ARG   B O     1 
ATOM   2350 C CB    . ARG   B 1 82  ? -42.05900 2.87700   43.24600 1.000 20.04470 ?  62  ARG   B CB    1 
ATOM   2351 C CG    . ARG   B 1 82  ? -43.25900 3.82100   43.58300 1.000 22.32716 ?  62  ARG   B CG    1 
ATOM   2352 C CD    . ARG   B 1 82  ? -44.57500 3.07500   43.72800 1.000 25.85637 ?  62  ARG   B CD    1 
ATOM   2353 N NE    . ARG   B 1 82  ? -45.69000 3.99000   43.96300 1.000 24.82382 ?  62  ARG   B NE    1 
ATOM   2354 C CZ    . ARG   B 1 82  ? -46.12000 4.34900   45.16300 1.000 28.07788 ?  62  ARG   B CZ    1 
ATOM   2355 N NH1   . ARG   B 1 82  ? -45.54800 3.88800   46.26600 1.000 26.67492 ?  62  ARG   B NH1   1 
ATOM   2356 N NH2   . ARG   B 1 82  ? -47.14400 5.20200   45.26200 1.000 26.75713 ?  62  ARG   B NH2   1 
ATOM   2357 N N     . ALA   B 1 83  ? -41.07300 4.32900   40.54900 1.000 19.71113 ?  63  ALA   B N     1 
ATOM   2358 C CA    . ALA   B 1 83  ? -41.23800 5.50300   39.69000 1.000 23.63659 ?  63  ALA   B CA    1 
ATOM   2359 C C     . ALA   B 1 83  ? -41.57900 5.11000   38.25100 1.000 25.23421 ?  63  ALA   B C     1 
ATOM   2360 O O     . ALA   B 1 83  ? -42.27400 5.86200   37.55300 1.000 25.49737 ?  63  ALA   B O     1 
ATOM   2361 C CB    . ALA   B 1 83  ? -39.98600 6.37100   39.72200 1.000 23.38870 ?  63  ALA   B CB    1 
ATOM   2362 N N     . SER   B 1 84  ? -41.10000 3.95000   37.78400 1.000 21.99105 ?  64  SER   B N     1 
ATOM   2363 C CA    . SER   B 1 84  ? -41.47700 3.48600   36.45100 1.000 27.47903 ?  64  SER   B CA    1 
ATOM   2364 C C     . SER   B 1 84  ? -42.97200 3.19500   36.38100 1.000 25.98232 ?  64  SER   B C     1 
ATOM   2365 O O     . SER   B 1 84  ? -43.65700 3.59800   35.42600 1.000 25.96341 ?  64  SER   B O     1 
ATOM   2366 C CB    . SER   B 1 84  ? -40.68400 2.23600   36.07800 1.000 26.84028 ?  64  SER   B CB    1 
ATOM   2367 O OG    . SER   B 1 84  ? -39.29600 2.41000   36.28000 1.000 30.03673 ?  64  SER   B OG    1 
ATOM   2368 N N     . PHE   B 1 85  ? -43.49300 2.48100   37.38400 1.000 25.03139 ?  65  PHE   B N     1 
ATOM   2369 C CA    . PHE   B 1 85  ? -44.92900 2.23100   37.45000 1.000 28.04159 ?  65  PHE   B CA    1 
ATOM   2370 C C     . PHE   B 1 85  ? -45.69900 3.54500   37.48500 1.000 29.60384 ?  65  PHE   B C     1 
ATOM   2371 O O     . PHE   B 1 85  ? -46.73200 3.69300   36.82700 1.000 25.29537 ?  65  PHE   B O     1 
ATOM   2372 C CB    . PHE   B 1 85  ? -45.26000 1.39600   38.69000 1.000 21.31115 ?  65  PHE   B CB    1 
ATOM   2373 C CG    . PHE   B 1 85  ? -44.81700 -0.04400  38.60300 1.000 23.77919 ?  65  PHE   B CG    1 
ATOM   2374 C CD1   . PHE   B 1 85  ? -45.14700 -0.84300  37.51200 1.000 26.10794 ?  65  PHE   B CD1   1 
ATOM   2375 C CD2   . PHE   B 1 85  ? -44.09200 -0.61200  39.64700 1.000 24.92208 ?  65  PHE   B CD2   1 
ATOM   2376 C CE1   . PHE   B 1 85  ? -44.73100 -2.18600  37.45500 1.000 23.39033 ?  65  PHE   B CE1   1 
ATOM   2377 C CE2   . PHE   B 1 85  ? -43.68700 -1.93900  39.59800 1.000 26.81278 ?  65  PHE   B CE2   1 
ATOM   2378 C CZ    . PHE   B 1 85  ? -44.00600 -2.72400  38.50100 1.000 25.21415 ?  65  PHE   B CZ    1 
ATOM   2379 N N     . GLU   B 1 86  ? -45.20700 4.52400   38.24300 1.000 23.64980 ?  66  GLU   B N     1 
ATOM   2380 C CA    . GLU   B 1 86  ? -45.93400 5.78800   38.32700 1.000 27.61396 ?  66  GLU   B CA    1 
ATOM   2381 C C     . GLU   B 1 86  ? -45.87100 6.56900   37.01000 1.000 28.18787 ?  66  GLU   B C     1 
ATOM   2382 O O     . GLU   B 1 86  ? -46.87600 7.16000   36.58400 1.000 28.06378 ?  66  GLU   B O     1 
ATOM   2383 C CB    . GLU   B 1 86  ? -45.39900 6.63300   39.48600 1.000 20.98446 ?  66  GLU   B CB    1 
ATOM   2384 C CG    . GLU   B 1 86  ? -45.63700 6.01500   40.85000 1.000 23.38331 ?  66  GLU   B CG    1 
ATOM   2385 C CD    . GLU   B 1 86  ? -47.10300 5.94400   41.26800 1.000 35.77774 ?  66  GLU   B CD    1 
ATOM   2386 O OE1   . GLU   B 1 86  ? -47.98800 6.45900   40.54700 1.000 31.95405 ?  66  GLU   B OE1   1 
ATOM   2387 O OE2   . GLU   B 1 86  ? -47.37900 5.33300   42.32500 1.000 31.61115 -1 66  GLU   B OE2   1 
ATOM   2388 N N     . LEU   B 1 87  ? -44.70300 6.60800   36.36100 1.000 22.00295 ?  67  LEU   B N     1 
ATOM   2389 C CA    . LEU   B 1 87  ? -44.61700 7.25900   35.05200 1.000 24.07488 ?  67  LEU   B CA    1 
ATOM   2390 C C     . LEU   B 1 87  ? -45.55900 6.60500   34.04900 1.000 29.01338 ?  67  LEU   B C     1 
ATOM   2391 O O     . LEU   B 1 87  ? -46.12200 7.29300   33.18200 1.000 31.08154 ?  67  LEU   B O     1 
ATOM   2392 C CB    . LEU   B 1 87  ? -43.19300 7.20800   34.51700 1.000 24.57494 ?  67  LEU   B CB    1 
ATOM   2393 C CG    . LEU   B 1 87  ? -42.23100 8.22700   35.16600 1.000 24.42651 ?  67  LEU   B CG    1 
ATOM   2394 C CD1   . LEU   B 1 87  ? -40.81800 8.00600   34.68900 1.000 23.15980 ?  67  LEU   B CD1   1 
ATOM   2395 C CD2   . LEU   B 1 87  ? -42.63900 9.67700   34.89300 1.000 22.14002 ?  67  LEU   B CD2   1 
ATOM   2396 N N     . ALA   B 1 88  ? -45.75500 5.28900   34.16200 1.000 22.95243 ?  68  ALA   B N     1 
ATOM   2397 C CA    . ALA   B 1 88  ? -46.55300 4.56700   33.17700 1.000 28.61422 ?  68  ALA   B CA    1 
ATOM   2398 C C     . ALA   B 1 88  ? -48.02500 4.94800   33.23000 1.000 28.04873 ?  68  ALA   B C     1 
ATOM   2399 O O     . ALA   B 1 88  ? -48.77500 4.61800   32.30400 1.000 30.39543 ?  68  ALA   B O     1 
ATOM   2400 C CB    . ALA   B 1 88  ? -46.38100 3.06100   33.38400 1.000 28.58740 ?  68  ALA   B CB    1 
ATOM   2401 N N     . ARG   B 1 89  ? -48.45700 5.62700   34.28400 1.000 26.55172 ?  69  ARG   B N     1 
ATOM   2402 C CA    . ARG   B 1 89  ? -49.82500 6.10600   34.30800 1.000 29.77213 ?  69  ARG   B CA    1 
ATOM   2403 C C     . ARG   B 1 89  ? -50.05000 7.19600   33.26800 1.000 37.88458 ?  69  ARG   B C     1 
ATOM   2404 O O     . ARG   B 1 89  ? -51.18700 7.38800   32.82800 1.000 37.54199 ?  69  ARG   B O     1 
ATOM   2405 C CB    . ARG   B 1 89  ? -50.17600 6.60100   35.70400 1.000 33.40563 ?  69  ARG   B CB    1 
ATOM   2406 C CG    . ARG   B 1 89  ? -49.99500 5.50800   36.75200 1.000 30.11590 ?  69  ARG   B CG    1 
ATOM   2407 C CD    . ARG   B 1 89  ? -50.74300 5.85400   38.01000 1.000 30.98224 ?  69  ARG   B CD    1 
ATOM   2408 N NE    . ARG   B 1 89  ? -52.17000 5.60300   37.84000 1.000 41.18725 ?  69  ARG   B NE    1 
ATOM   2409 C CZ    . ARG   B 1 89  ? -53.11900 6.23500   38.51200 1.000 34.90678 ?  69  ARG   B CZ    1 
ATOM   2410 N NH1   . ARG   B 1 89  ? -52.82600 7.15400   39.41400 1.000 32.73160 ?  69  ARG   B NH1   1 
ATOM   2411 N NH2   . ARG   B 1 89  ? -54.39000 5.91600   38.29100 1.000 38.66878 ?  69  ARG   B NH2   1 
ATOM   2412 N N     . SER   B 1 90  ? -48.99000 7.88500   32.84700 1.000 30.97281 ?  70  SER   B N     1 
ATOM   2413 C CA    . SER   B 1 90  ? -49.08800 8.93700   31.84800 1.000 31.60843 ?  70  SER   B CA    1 
ATOM   2414 C C     . SER   B 1 90  ? -48.37200 8.62500   30.54600 1.000 34.55125 ?  70  SER   B C     1 
ATOM   2415 O O     . SER   B 1 90  ? -48.81000 9.09600   29.49800 1.000 40.77541 ?  70  SER   B O     1 
ATOM   2416 C CB    . SER   B 1 90  ? -48.53800 10.25800  32.40700 1.000 34.81526 ?  70  SER   B CB    1 
ATOM   2417 O OG    . SER   B 1 90  ? -49.46600 10.85500  33.30400 1.000 45.53908 ?  70  SER   B OG    1 
ATOM   2418 N N     . TYR   B 1 91  ? -47.28600 7.86800   30.57000 1.000 27.45357 ?  71  TYR   B N     1 
ATOM   2419 C CA    . TYR   B 1 91  ? -46.54400 7.58100   29.35000 1.000 25.57967 ?  71  TYR   B CA    1 
ATOM   2420 C C     . TYR   B 1 91  ? -47.08000 6.30800   28.69900 1.000 27.11800 ?  71  TYR   B C     1 
ATOM   2421 O O     . TYR   B 1 91  ? -47.57900 5.40800   29.38100 1.000 33.92755 ?  71  TYR   B O     1 
ATOM   2422 C CB    . TYR   B 1 91  ? -45.04500 7.44000   29.64800 1.000 27.83111 ?  71  TYR   B CB    1 
ATOM   2423 C CG    . TYR   B 1 91  ? -44.36400 8.79300   29.76100 1.000 28.15888 ?  71  TYR   B CG    1 
ATOM   2424 C CD1   . TYR   B 1 91  ? -44.52400 9.57400   30.90000 1.000 26.81574 ?  71  TYR   B CD1   1 
ATOM   2425 C CD2   . TYR   B 1 91  ? -43.60400 9.30000   28.71000 1.000 31.31873 ?  71  TYR   B CD2   1 
ATOM   2426 C CE1   . TYR   B 1 91  ? -43.93000 10.82400  31.00100 1.000 29.57534 ?  71  TYR   B CE1   1 
ATOM   2427 C CE2   . TYR   B 1 91  ? -42.99400 10.52700  28.80500 1.000 27.44042 ?  71  TYR   B CE2   1 
ATOM   2428 C CZ    . TYR   B 1 91  ? -43.16300 11.28900  29.95600 1.000 25.13092 ?  71  TYR   B CZ    1 
ATOM   2429 O OH    . TYR   B 1 91  ? -42.59000 12.53500  30.05400 1.000 29.50365 ?  71  TYR   B OH    1 
ATOM   2430 N N     . LYS   B 1 92  ? -46.99600 6.25100   27.36500 1.000 25.76002 ?  72  LYS   B N     1 
ATOM   2431 C CA    . LYS   B 1 92  ? -47.41400 5.03800   26.66000 1.000 29.19413 ?  72  LYS   B CA    1 
ATOM   2432 C C     . LYS   B 1 92  ? -46.47900 3.87100   26.93900 1.000 36.06095 ?  72  LYS   B C     1 
ATOM   2433 O O     . LYS   B 1 92  ? -46.91500 2.71300   26.94500 1.000 30.34177 ?  72  LYS   B O     1 
ATOM   2434 C CB    . LYS   B 1 92  ? -47.47800 5.29000   25.15000 1.000 29.94001 ?  72  LYS   B CB    1 
ATOM   2435 C CG    . LYS   B 1 92  ? -48.44000 6.39700   24.76600 1.000 38.66055 ?  72  LYS   B CG    1 
ATOM   2436 C CD    . LYS   B 1 92  ? -48.72500 6.37100   23.27200 1.000 39.23774 ?  72  LYS   B CD    1 
ATOM   2437 N N     . HIS   B 1 93  ? -45.19100 4.14800   27.13600 1.000 28.44102 ?  73  HIS   B N     1 
ATOM   2438 C CA    . HIS   B 1 93  ? -44.20800 3.09900   27.36300 1.000 28.62169 ?  73  HIS   B CA    1 
ATOM   2439 C C     . HIS   B 1 93  ? -43.12700 3.63400   28.28700 1.000 31.56915 ?  73  HIS   B C     1 
ATOM   2440 O O     . HIS   B 1 93  ? -42.66400 4.76600   28.11000 1.000 25.15169 ?  73  HIS   B O     1 
ATOM   2441 C CB    . HIS   B 1 93  ? -43.54600 2.62800   26.06800 1.000 30.50092 ?  73  HIS   B CB    1 
ATOM   2442 C CG    . HIS   B 1 93  ? -42.55300 1.52600   26.29000 1.000 32.41761 ?  73  HIS   B CG    1 
ATOM   2443 N ND1   . HIS   B 1 93  ? -42.92200 0.27600   26.74100 1.000 37.13132 ?  73  HIS   B ND1   1 
ATOM   2444 C CD2   . HIS   B 1 93  ? -41.20000 1.51800   26.22600 1.000 32.78523 ?  73  HIS   B CD2   1 
ATOM   2445 C CE1   . HIS   B 1 93  ? -41.84100 -0.46700  26.90300 1.000 37.72993 ?  73  HIS   B CE1   1 
ATOM   2446 N NE2   . HIS   B 1 93  ? -40.78300 0.25900   26.58700 1.000 35.95530 ?  73  HIS   B NE2   1 
ATOM   2447 N N     . VAL   B 1 94  ? -42.71800 2.81900   29.25900 1.000 28.51909 ?  74  VAL   B N     1 
ATOM   2448 C CA    . VAL   B 1 94  ? -41.68100 3.21500   30.20900 1.000 25.36134 ?  74  VAL   B CA    1 
ATOM   2449 C C     . VAL   B 1 94  ? -40.69900 2.06300   30.32200 1.000 28.44321 ?  74  VAL   B C     1 
ATOM   2450 O O     . VAL   B 1 94  ? -41.10800 0.90900   30.50300 1.000 25.48426 ?  74  VAL   B O     1 
ATOM   2451 C CB    . VAL   B 1 94  ? -42.25100 3.57900   31.59500 1.000 23.93766 ?  74  VAL   B CB    1 
ATOM   2452 C CG1   . VAL   B 1 94  ? -41.08700 3.90900   32.56300 1.000 24.04648 ?  74  VAL   B CG1   1 
ATOM   2453 C CG2   . VAL   B 1 94  ? -43.23000 4.75500   31.51500 1.000 23.15555 ?  74  VAL   B CG2   1 
ATOM   2454 N N     . ASP   B 1 95  ? -39.41500 2.36400   30.15200 1.000 24.37052 ?  75  ASP   B N     1 
ATOM   2455 C CA    . ASP   B 1 95  ? -38.34800 1.41300   30.43100 1.000 21.82793 ?  75  ASP   B CA    1 
ATOM   2456 C C     . ASP   B 1 95  ? -37.76100 1.78300   31.78500 1.000 24.46522 ?  75  ASP   B C     1 
ATOM   2457 O O     . ASP   B 1 95  ? -37.47300 2.95900   32.03300 1.000 23.19381 ?  75  ASP   B O     1 
ATOM   2458 C CB    . ASP   B 1 95  ? -37.24100 1.47300   29.38700 1.000 21.37794 ?  75  ASP   B CB    1 
ATOM   2459 C CG    . ASP   B 1 95  ? -37.70900 1.02100   28.01100 1.000 29.29597 ?  75  ASP   B CG    1 
ATOM   2460 O OD1   . ASP   B 1 95  ? -38.39700 -0.02200  27.92100 1.000 31.86346 ?  75  ASP   B OD1   1 
ATOM   2461 O OD2   . ASP   B 1 95  ? -37.36200 1.72100   27.02900 1.000 29.73746 -1 75  ASP   B OD2   1 
ATOM   2462 N N     . GLY   B 1 96  ? -37.60400 0.79200   32.65600 1.000 24.73485 ?  76  GLY   B N     1 
ATOM   2463 C CA    . GLY   B 1 96  ? -36.88800 0.96400   33.91000 1.000 22.04242 ?  76  GLY   B CA    1 
ATOM   2464 C C     . GLY   B 1 96  ? -35.60400 0.15800   33.85100 1.000 28.16735 ?  76  GLY   B C     1 
ATOM   2465 O O     . GLY   B 1 96  ? -35.63300 -1.04900  33.58600 1.000 26.26921 ?  76  GLY   B O     1 
ATOM   2466 N N     . VAL   B 1 97  ? -34.47700 0.83500   34.08000 1.000 21.64795 ?  77  VAL   B N     1 
ATOM   2467 C CA    . VAL   B 1 97  ? -33.17300 0.19600   33.95600 1.000 19.54157 ?  77  VAL   B CA    1 
ATOM   2468 C C     . VAL   B 1 97  ? -32.42100 0.36000   35.26400 1.000 25.81262 ?  77  VAL   B C     1 
ATOM   2469 O O     . VAL   B 1 97  ? -32.39000 1.46100   35.83300 1.000 21.50619 ?  77  VAL   B O     1 
ATOM   2470 C CB    . VAL   B 1 97  ? -32.34700 0.79500   32.80400 1.000 23.81204 ?  77  VAL   B CB    1 
ATOM   2471 C CG1   . VAL   B 1 97  ? -30.94500 0.20000   32.80800 1.000 21.46495 ?  77  VAL   B CG1   1 
ATOM   2472 C CG2   . VAL   B 1 97  ? -33.03700 0.53300   31.46800 1.000 26.00634 ?  77  VAL   B CG2   1 
ATOM   2473 N N     . ASP   B 1 98  ? -31.79300 -0.71800  35.72800 1.000 20.69482 ?  78  ASP   B N     1 
ATOM   2474 C CA    . ASP   B 1 98  ? -30.96400 -0.62200  36.92600 1.000 22.46528 ?  78  ASP   B CA    1 
ATOM   2475 C C     . ASP   B 1 98  ? -29.74600 -1.52800  36.82000 1.000 22.27866 ?  78  ASP   B C     1 
ATOM   2476 O O     . ASP   B 1 98  ? -29.80900 -2.61600  36.24600 1.000 24.55770 ?  78  ASP   B O     1 
ATOM   2477 C CB    . ASP   B 1 98  ? -31.74100 -0.97900  38.19100 1.000 19.56806 ?  78  ASP   B CB    1 
ATOM   2478 C CG    . ASP   B 1 98  ? -31.12100 -0.34600  39.45100 1.000 22.71452 ?  78  ASP   B CG    1 
ATOM   2479 O OD1   . ASP   B 1 98  ? -30.18000 -0.96200  40.02300 1.000 23.40654 ?  78  ASP   B OD1   1 
ATOM   2480 O OD2   . ASP   B 1 98  ? -31.52600 0.77900   39.82300 1.000 22.88435 -1 78  ASP   B OD2   1 
ATOM   2481 N N     . TYR   B 1 99  ? -28.64100 -1.06200  37.40700 1.000 21.71759 ?  79  TYR   B N     1 
ATOM   2482 C CA    . TYR   B 1 99  ? -27.42300 -1.86600  37.45700 1.000 19.08207 ?  79  TYR   B CA    1 
ATOM   2483 C C     . TYR   B 1 99  ? -27.66000 -3.18100  38.17900 1.000 26.61021 ?  79  TYR   B C     1 
ATOM   2484 O O     . TYR   B 1 99  ? -27.05800 -4.20500  37.82400 1.000 24.12912 ?  79  TYR   B O     1 
ATOM   2485 C CB    . TYR   B 1 99  ? -26.32200 -1.08200  38.16300 1.000 21.29967 ?  79  TYR   B CB    1 
ATOM   2486 C CG    . TYR   B 1 99  ? -25.08000 -1.86400  38.50700 1.000 19.59418 ?  79  TYR   B CG    1 
ATOM   2487 C CD1   . TYR   B 1 99  ? -24.11600 -2.13600  37.54200 1.000 26.28450 ?  79  TYR   B CD1   1 
ATOM   2488 C CD2   . TYR   B 1 99  ? -24.86100 -2.32100  39.79500 1.000 29.76477 ?  79  TYR   B CD2   1 
ATOM   2489 C CE1   . TYR   B 1 99  ? -22.95600 -2.82900  37.86500 1.000 23.43861 ?  79  TYR   B CE1   1 
ATOM   2490 C CE2   . TYR   B 1 99  ? -23.71700 -3.02000  40.12400 1.000 32.78723 ?  79  TYR   B CE2   1 
ATOM   2491 C CZ    . TYR   B 1 99  ? -22.76800 -3.27100  39.15200 1.000 27.10064 ?  79  TYR   B CZ    1 
ATOM   2492 O OH    . TYR   B 1 99  ? -21.63300 -3.95900  39.48900 1.000 31.46117 ?  79  TYR   B OH    1 
ATOM   2493 N N     . SER   B 1 100 ? -28.51400 -3.16900  39.20100 1.000 23.03463 ?  80  SER   B N     1 
ATOM   2494 C CA    . SER   B 1 100 ? -28.70200 -4.32600  40.06700 1.000 24.71270 ?  80  SER   B CA    1 
ATOM   2495 C C     . SER   B 1 100 ? -29.71800 -5.29000  39.46300 1.000 23.53589 ?  80  SER   B C     1 
ATOM   2496 O O     . SER   B 1 100 ? -30.89600 -4.94900  39.31900 1.000 22.96526 ?  80  SER   B O     1 
ATOM   2497 C CB    . SER   B 1 100 ? -29.16400 -3.87900  41.45500 1.000 26.05042 ?  80  SER   B CB    1 
ATOM   2498 O OG    . SER   B 1 100 ? -29.66000 -4.98900  42.18600 1.000 28.71648 ?  80  SER   B OG    1 
ATOM   2499 N N     . GLN   B 1 101 ? -29.27100 -6.51400  39.15800 1.000 24.76986 ?  81  GLN   B N     1 
ATOM   2500 C CA    . GLN   B 1 101 ? -30.20800 -7.53000  38.70000 1.000 23.05099 ?  81  GLN   B CA    1 
ATOM   2501 C C     . GLN   B 1 101 ? -31.24800 -7.84000  39.76800 1.000 22.42248 ?  81  GLN   B C     1 
ATOM   2502 O O     . GLN   B 1 101 ? -32.42000 -8.07200  39.45100 1.000 26.50684 ?  81  GLN   B O     1 
ATOM   2503 C CB    . GLN   B 1 101 ? -29.45200 -8.80200  38.29400 1.000 27.61598 ?  81  GLN   B CB    1 
ATOM   2504 C CG    . GLN   B 1 101 ? -30.36000 -9.86000  37.67000 1.000 27.59181 ?  81  GLN   B CG    1 
ATOM   2505 C CD    . GLN   B 1 101 ? -30.89200 -9.45100  36.31700 1.000 23.74681 ?  81  GLN   B CD    1 
ATOM   2506 O OE1   . GLN   B 1 101 ? -30.11800 -9.16500  35.40000 1.000 26.82914 ?  81  GLN   B OE1   1 
ATOM   2507 N NE2   . GLN   B 1 101 ? -32.21400 -9.46300  36.16400 1.000 30.46114 ?  81  GLN   B NE2   1 
ATOM   2508 N N     . ALA   B 1 102 ? -30.84700 -7.83100  41.04300 1.000 22.63286 ?  82  ALA   B N     1 
ATOM   2509 C CA    . ALA   B 1 102 ? -31.77700 -8.15800  42.12500 1.000 25.35798 ?  82  ALA   B CA    1 
ATOM   2510 C C     . ALA   B 1 102 ? -32.91300 -7.14200  42.22000 1.000 24.67927 ?  82  ALA   B C     1 
ATOM   2511 O O     . ALA   B 1 102 ? -34.06900 -7.50900  42.47400 1.000 22.66531 ?  82  ALA   B O     1 
ATOM   2512 C CB    . ALA   B 1 102 ? -31.02400 -8.24300  43.44500 1.000 30.05134 ?  82  ALA   B CB    1 
ATOM   2513 N N     . PHE   B 1 103 ? -32.60600 -5.85600  42.02700 1.000 23.24586 ?  83  PHE   B N     1 
ATOM   2514 C CA    . PHE   B 1 103 ? -33.66100 -4.83900  42.00100 1.000 22.70115 ?  83  PHE   B CA    1 
ATOM   2515 C C     . PHE   B 1 103 ? -34.62800 -5.08600  40.84500 1.000 22.32851 ?  83  PHE   B C     1 
ATOM   2516 O O     . PHE   B 1 103 ? -35.85500 -5.00800  41.00700 1.000 23.47803 ?  83  PHE   B O     1 
ATOM   2517 C CB    . PHE   B 1 103 ? -33.04100 -3.43600  41.85200 1.000 21.34071 ?  83  PHE   B CB    1 
ATOM   2518 C CG    . PHE   B 1 103 ? -32.43400 -2.88200  43.10900 1.000 22.03001 ?  83  PHE   B CG    1 
ATOM   2519 C CD1   . PHE   B 1 103 ? -32.76300 -3.37900  44.34400 1.000 27.94494 ?  83  PHE   B CD1   1 
ATOM   2520 C CD2   . PHE   B 1 103 ? -31.53700 -1.81200  43.03100 1.000 22.90827 ?  83  PHE   B CD2   1 
ATOM   2521 C CE1   . PHE   B 1 103 ? -32.20400 -2.83500  45.49800 1.000 43.85895 ?  83  PHE   B CE1   1 
ATOM   2522 C CE2   . PHE   B 1 103 ? -30.97800 -1.26600  44.16500 1.000 28.29892 ?  83  PHE   B CE2   1 
ATOM   2523 C CZ    . PHE   B 1 103 ? -31.31000 -1.76800  45.40500 1.000 33.47657 ?  83  PHE   B CZ    1 
ATOM   2524 N N     . VAL   B 1 104 ? -34.07700 -5.32200  39.65900 1.000 21.53955 ?  84  VAL   B N     1 
ATOM   2525 C CA    . VAL   B 1 104 ? -34.87600 -5.57700  38.45900 1.000 25.96449 ?  84  VAL   B CA    1 
ATOM   2526 C C     . VAL   B 1 104 ? -35.74300 -6.82400  38.62900 1.000 24.92572 ?  84  VAL   B C     1 
ATOM   2527 O O     . VAL   B 1 104 ? -36.92400 -6.84000  38.23400 1.000 24.88711 ?  84  VAL   B O     1 
ATOM   2528 C CB    . VAL   B 1 104 ? -33.94000 -5.70200  37.24100 1.000 27.94372 ?  84  VAL   B CB    1 
ATOM   2529 C CG1   . VAL   B 1 104 ? -34.68300 -6.33500  36.05200 1.000 44.34523 ?  84  VAL   B CG1   1 
ATOM   2530 C CG2   . VAL   B 1 104 ? -33.38400 -4.35100  36.87900 1.000 36.13904 ?  84  VAL   B CG2   1 
ATOM   2531 N N     . ASP   B 1 105 ? -35.17900 -7.88600  39.22900 1.000 25.83301 ?  85  ASP   B N     1 
ATOM   2532 C CA    . ASP   B 1 105 ? -35.96900 -9.09000  39.49700 1.000 26.90207 ?  85  ASP   B CA    1 
ATOM   2533 C C     . ASP   B 1 105 ? -37.15200 -8.78700  40.40900 1.000 28.39446 ?  85  ASP   B C     1 
ATOM   2534 O O     . ASP   B 1 105 ? -38.26400 -9.29900  40.20000 1.000 27.96980 ?  85  ASP   B O     1 
ATOM   2535 C CB    . ASP   B 1 105 ? -35.08500 -10.19000 40.10500 1.000 26.56814 ?  85  ASP   B CB    1 
ATOM   2536 C CG    . ASP   B 1 105 ? -34.09900 -10.79000 39.09600 1.000 30.64999 ?  85  ASP   B CG    1 
ATOM   2537 O OD1   . ASP   B 1 105 ? -34.20400 -10.50800 37.88700 1.000 36.81398 ?  85  ASP   B OD1   1 
ATOM   2538 O OD2   . ASP   B 1 105 ? -33.20900 -11.55100 39.51400 1.000 33.72831 -1 85  ASP   B OD2   1 
ATOM   2539 N N     . ALA   B 1 106 ? -36.94000 -7.95000  41.42700 1.000 25.16483 ?  86  ALA   B N     1 
ATOM   2540 C CA    . ALA   B 1 106 ? -38.02100 -7.62500  42.35000 1.000 22.93110 ?  86  ALA   B CA    1 
ATOM   2541 C C     . ALA   B 1 106 ? -39.11700 -6.82800  41.64900 1.000 24.37569 ?  86  ALA   B C     1 
ATOM   2542 O O     . ALA   B 1 106 ? -40.30700 -7.13100  41.79200 1.000 27.19494 ?  86  ALA   B O     1 
ATOM   2543 C CB    . ALA   B 1 106 ? -37.46900 -6.85100  43.55300 1.000 25.35662 ?  86  ALA   B CB    1 
ATOM   2544 N N     . ALA   B 1 107 ? -38.72900 -5.80400  40.87700 1.000 24.99376 ?  87  ALA   B N     1 
ATOM   2545 C CA    . ALA   B 1 107 ? -39.71000 -5.04600  40.11000 1.000 23.42538 ?  87  ALA   B CA    1 
ATOM   2546 C C     . ALA   B 1 107 ? -40.49800 -5.96900  39.18800 1.000 22.61861 ?  87  ALA   B C     1 
ATOM   2547 O O     . ALA   B 1 107 ? -41.73300 -5.86000  39.07900 1.000 25.34453 ?  87  ALA   B O     1 
ATOM   2548 C CB    . ALA   B 1 107 ? -39.00900 -3.95400  39.28000 1.000 20.45284 ?  87  ALA   B CB    1 
ATOM   2549 N N     . THR   B 1 108 ? -39.78600 -6.85600  38.49200 1.000 26.40712 ?  88  THR   B N     1 
ATOM   2550 C CA    . THR   B 1 108 ? -40.42400 -7.74300  37.51700 1.000 25.35880 ?  88  THR   B CA    1 
ATOM   2551 C C     . THR   B 1 108 ? -41.36600 -8.72900  38.20000 1.000 26.84377 ?  88  THR   B C     1 
ATOM   2552 O O     . THR   B 1 108 ? -42.46600 -9.00800  37.69200 1.000 30.83331 ?  88  THR   B O     1 
ATOM   2553 C CB    . THR   B 1 108 ? -39.36200 -8.48500  36.70700 1.000 25.25484 ?  88  THR   B CB    1 
ATOM   2554 O OG1   . THR   B 1 108 ? -38.47000 -7.55000  36.07100 1.000 28.11085 ?  88  THR   B OG1   1 
ATOM   2555 C CG2   . THR   B 1 108 ? -40.00000 -9.36700  35.64600 1.000 33.37649 ?  88  THR   B CG2   1 
ATOM   2556 N N     . GLU   B 1 109 ? -40.96200 -9.25800  39.36000 1.000 28.25862 ?  89  GLU   B N     1 
ATOM   2557 C CA    . GLU   B 1 109 ? -41.83600 -10.16900 40.09300 1.000 27.22664 ?  89  GLU   B CA    1 
ATOM   2558 C C     . GLU   B 1 109 ? -43.09700 -9.46000  40.57200 1.000 34.12827 ?  89  GLU   B C     1 
ATOM   2559 O O     . GLU   B 1 109 ? -44.20500 -10.00000 40.45600 1.000 31.02857 ?  89  GLU   B O     1 
ATOM   2560 C CB    . GLU   B 1 109 ? -41.07900 -10.80600 41.26200 1.000 26.20697 ?  89  GLU   B CB    1 
ATOM   2561 C CG    . GLU   B 1 109 ? -41.88500 -11.84300 42.03500 1.000 52.47267 ?  89  GLU   B CG    1 
ATOM   2562 C CD    . GLU   B 1 109 ? -42.05100 -13.16500 41.29500 1.000 53.60600 ?  89  GLU   B CD    1 
ATOM   2563 O OE1   . GLU   B 1 109 ? -41.16200 -13.53100 40.49200 1.000 49.72345 ?  89  GLU   B OE1   1 
ATOM   2564 O OE2   . GLU   B 1 109 ? -43.08600 -13.83000 41.51500 1.000 57.06068 -1 89  GLU   B OE2   1 
ATOM   2565 N N     . LEU   B 1 110 ? -42.96300 -8.23700  41.09100 1.000 30.74592 ?  90  LEU   B N     1 
ATOM   2566 C CA    . LEU   B 1 110 ? -44.15700 -7.48600  41.45100 1.000 25.40199 ?  90  LEU   B CA    1 
ATOM   2567 C C     . LEU   B 1 110 ? -45.02600 -7.24600  40.22900 1.000 32.28835 ?  90  LEU   B C     1 
ATOM   2568 O O     . LEU   B 1 110 ? -46.25900 -7.30200  40.30300 1.000 30.08939 ?  90  LEU   B O     1 
ATOM   2569 C CB    . LEU   B 1 110 ? -43.77000 -6.15200  42.10100 1.000 25.03519 ?  90  LEU   B CB    1 
ATOM   2570 C CG    . LEU   B 1 110 ? -44.92700 -5.28900  42.59300 1.000 27.49158 ?  90  LEU   B CG    1 
ATOM   2571 C CD1   . LEU   B 1 110 ? -45.77400 -6.01800  43.63500 1.000 26.70657 ?  90  LEU   B CD1   1 
ATOM   2572 C CD2   . LEU   B 1 110 ? -44.39000 -3.96900  43.15800 1.000 28.09341 ?  90  LEU   B CD2   1 
ATOM   2573 N N     . GLN   B 1 111 ? -44.39400 -7.00100  39.08700 1.000 32.57093 ?  91  GLN   B N     1 
ATOM   2574 C CA    . GLN   B 1 111 ? -45.14400 -6.70200  37.87600 1.000 31.75806 ?  91  GLN   B CA    1 
ATOM   2575 C C     . GLN   B 1 111 ? -45.89900 -7.92800  37.38500 1.000 40.31797 ?  91  GLN   B C     1 
ATOM   2576 O O     . GLN   B 1 111 ? -47.08400 -7.84300  37.04100 1.000 36.59518 ?  91  GLN   B O     1 
ATOM   2577 C CB    . GLN   B 1 111 ? -44.18400 -6.18700  36.80200 1.000 34.90738 ?  91  GLN   B CB    1 
ATOM   2578 C CG    . GLN   B 1 111 ? -44.84400 -5.81400  35.49400 1.000 38.08997 ?  91  GLN   B CG    1 
ATOM   2579 C CD    . GLN   B 1 111 ? -43.82500 -5.43200  34.44200 1.000 36.02492 ?  91  GLN   B CD    1 
ATOM   2580 O OE1   . GLN   B 1 111 ? -42.76400 -6.05100  34.34100 1.000 27.32587 ?  91  GLN   B OE1   1 
ATOM   2581 N NE2   . GLN   B 1 111 ? -44.14200 -4.41400  33.64600 1.000 28.59231 ?  91  GLN   B NE2   1 
ATOM   2582 N N     . LYS   B 1 112 ? -45.23000 -9.08400  37.37500 1.000 34.55717 ?  92  LYS   B N     1 
ATOM   2583 C CA    . LYS   B 1 112 ? -45.77800 -10.28800 36.76200 1.000 36.52714 ?  92  LYS   B CA    1 
ATOM   2584 C C     . LYS   B 1 112 ? -46.66900 -11.07400 37.72100 1.000 44.54291 ?  92  LYS   B C     1 
ATOM   2585 O O     . LYS   B 1 112 ? -47.77100 -11.49300 37.34700 1.000 42.12020 ?  92  LYS   B O     1 
ATOM   2586 C CB    . LYS   B 1 112 ? -44.64300 -11.17100 36.24600 1.000 42.10087 ?  92  LYS   B CB    1 
ATOM   2587 C CG    . LYS   B 1 112 ? -43.88500 -10.56000 35.06100 1.000 50.35158 ?  92  LYS   B CG    1 
ATOM   2588 N N     . ASN   B 1 113 ? -46.20900 -11.30400 38.95200 1.000 35.08604 ?  93  ASN   B N     1 
ATOM   2589 C CA    . ASN   B 1 113 ? -46.98300 -12.09600 39.90300 1.000 37.44818 ?  93  ASN   B CA    1 
ATOM   2590 C C     . ASN   B 1 113 ? -47.84800 -11.26600 40.83300 1.000 33.99956 ?  93  ASN   B C     1 
ATOM   2591 O O     . ASN   B 1 113 ? -48.66900 -11.83600 41.54800 1.000 36.46431 ?  93  ASN   B O     1 
ATOM   2592 C CB    . ASN   B 1 113 ? -46.07200 -13.00200 40.73700 1.000 38.38540 ?  93  ASN   B CB    1 
ATOM   2593 C CG    . ASN   B 1 113 ? -45.64500 -14.23800 39.98500 1.000 51.62586 ?  93  ASN   B CG    1 
ATOM   2594 O OD1   . ASN   B 1 113 ? -44.66600 -14.22100 39.24900 1.000 60.43711 ?  93  ASN   B OD1   1 
ATOM   2595 N N     . GLY   B 1 114 ? -47.67900 -9.95000  40.87000 1.000 33.85999 ?  94  GLY   B N     1 
ATOM   2596 C CA    . GLY   B 1 114 ? -48.59300 -9.11100  41.61300 1.000 28.16070 ?  94  GLY   B CA    1 
ATOM   2597 C C     . GLY   B 1 114 ? -48.27300 -8.90700  43.07800 1.000 29.68624 ?  94  GLY   B C     1 
ATOM   2598 O O     . GLY   B 1 114 ? -48.96200 -8.11300  43.74000 1.000 30.30655 ?  94  GLY   B O     1 
ATOM   2599 N N     . CYS   B 1 115 ? -47.24900 -9.56900  43.60500 1.000 27.69044 ?  95  CYS   B N     1 
ATOM   2600 C CA    . CYS   B 1 115 ? -46.87400 -9.34600  44.99100 1.000 30.64545 ?  95  CYS   B CA    1 
ATOM   2601 C C     . CYS   B 1 115 ? -45.42600 -9.77300  45.21100 1.000 30.57535 ?  95  CYS   B C     1 
ATOM   2602 O O     . CYS   B 1 115 ? -44.88400 -10.59800 44.47100 1.000 32.52976 ?  95  CYS   B O     1 
ATOM   2603 C CB    . CYS   B 1 115 ? -47.83200 -10.08000 45.93200 1.000 37.68711 ?  95  CYS   B CB    1 
ATOM   2604 S SG    . CYS   B 1 115 ? -47.69800 -11.86900 45.76300 1.000 47.00285 ?  95  CYS   B SG    1 
ATOM   2605 N N     . ILE   B 1 116 ? -44.79600 -9.16500  46.22500 1.000 26.57492 ?  96  ILE   B N     1 
ATOM   2606 C CA    . ILE   B 1 116 ? -43.46200 -9.55800  46.67300 1.000 24.93644 ?  96  ILE   B CA    1 
ATOM   2607 C C     . ILE   B 1 116 ? -43.41900 -9.33700  48.17900 1.000 22.60879 ?  96  ILE   B C     1 
ATOM   2608 O O     . ILE   B 1 116 ? -44.16100 -8.51900  48.72600 1.000 25.77433 ?  96  ILE   B O     1 
ATOM   2609 C CB    . ILE   B 1 116 ? -42.31300 -8.76500  46.00300 1.000 28.03692 ?  96  ILE   B CB    1 
ATOM   2610 C CG1   . ILE   B 1 116 ? -42.55800 -7.26900  46.13300 1.000 25.36619 ?  96  ILE   B CG1   1 
ATOM   2611 C CG2   . ILE   B 1 116 ? -42.15900 -9.12300  44.52900 1.000 36.19205 ?  96  ILE   B CG2   1 
ATOM   2612 C CD1   . ILE   B 1 116 ? -41.39800 -6.44300  45.60000 1.000 36.77528 ?  96  ILE   B CD1   1 
ATOM   2613 N N     . GLY   B 1 117 ? -42.55800 -10.08700 48.85600 1.000 25.00469 ?  97  GLY   B N     1 
ATOM   2614 C CA    . GLY   B 1 117 ? -42.37900 -9.95000  50.28800 1.000 30.90317 ?  97  GLY   B CA    1 
ATOM   2615 C C     . GLY   B 1 117 ? -41.02000 -9.34900  50.58600 1.000 25.97516 ?  97  GLY   B C     1 
ATOM   2616 O O     . GLY   B 1 117 ? -40.06000 -9.55400  49.83700 1.000 30.07861 ?  97  GLY   B O     1 
ATOM   2617 N N     . TYR   B 1 118 ? -40.94600 -8.59200  51.68200 1.000 23.71369 ?  98  TYR   B N     1 
ATOM   2618 C CA    . TYR   B 1 118 ? -39.68200 -7.98800  52.08800 1.000 24.00111 ?  98  TYR   B CA    1 
ATOM   2619 C C     . TYR   B 1 118 ? -39.63000 -7.85100  53.60400 1.000 23.45489 ?  98  TYR   B C     1 
ATOM   2620 O O     . TYR   B 1 118 ? -40.65500 -7.90300  54.28800 1.000 24.26417 ?  98  TYR   B O     1 
ATOM   2621 C CB    . TYR   B 1 118 ? -39.47900 -6.62900  51.37900 1.000 24.93816 ?  98  TYR   B CB    1 
ATOM   2622 C CG    . TYR   B 1 118 ? -40.27100 -5.45300  51.92800 1.000 24.54421 ?  98  TYR   B CG    1 
ATOM   2623 C CD1   . TYR   B 1 118 ? -39.76200 -4.67200  52.96200 1.000 23.60214 ?  98  TYR   B CD1   1 
ATOM   2624 C CD2   . TYR   B 1 118 ? -41.51300 -5.10300  51.39800 1.000 23.39169 ?  98  TYR   B CD2   1 
ATOM   2625 C CE1   . TYR   B 1 118 ? -40.47500 -3.59500  53.47000 1.000 25.51205 ?  98  TYR   B CE1   1 
ATOM   2626 C CE2   . TYR   B 1 118 ? -42.23300 -4.00100  51.89200 1.000 24.07406 ?  98  TYR   B CE2   1 
ATOM   2627 C CZ    . TYR   B 1 118 ? -41.70600 -3.25200  52.92800 1.000 24.32746 ?  98  TYR   B CZ    1 
ATOM   2628 O OH    . TYR   B 1 118 ? -42.38300 -2.15200  53.45300 1.000 26.97598 ?  98  TYR   B OH    1 
ATOM   2629 N N     . SER   B 1 119 ? -38.41700 -7.62500  54.12200 1.000 24.91585 ?  99  SER   B N     1 
ATOM   2630 C CA    . SER   B 1 119 ? -38.17700 -7.48300  55.55900 1.000 24.84180 ?  99  SER   B CA    1 
ATOM   2631 C C     . SER   B 1 119 ? -37.94100 -6.01700  55.88900 1.000 22.51367 ?  99  SER   B C     1 
ATOM   2632 O O     . SER   B 1 119 ? -36.90700 -5.45900  55.52500 1.000 28.93622 ?  99  SER   B O     1 
ATOM   2633 C CB    . SER   B 1 119 ? -36.97500 -8.30900  56.02100 1.000 25.63717 ?  99  SER   B CB    1 
ATOM   2634 O OG    . SER   B 1 119 ? -37.13800 -9.66400  55.66700 1.000 38.16555 ?  99  SER   B OG    1 
ATOM   2635 N N     . GLN   B 1 120 ? -38.90200 -5.41200  56.56700 1.000 21.98219 ?  100 GLN   B N     1 
ATOM   2636 C CA    . GLN   B 1 120 ? -38.73500 -4.05400  57.06600 1.000 21.21064 ?  100 GLN   B CA    1 
ATOM   2637 C C     . GLN   B 1 120 ? -37.81400 -4.05000  58.28300 1.000 26.11598 ?  100 GLN   B C     1 
ATOM   2638 O O     . GLN   B 1 120 ? -37.91400 -4.91400  59.16200 1.000 21.61712 ?  100 GLN   B O     1 
ATOM   2639 C CB    . GLN   B 1 120 ? -40.09200 -3.46800  57.42100 1.000 21.49663 ?  100 GLN   B CB    1 
ATOM   2640 C CG    . GLN   B 1 120 ? -40.04800 -2.00600  57.81900 1.000 20.39616 ?  100 GLN   B CG    1 
ATOM   2641 C CD    . GLN   B 1 120 ? -41.40800 -1.48800  58.20700 1.000 31.28507 ?  100 GLN   B CD    1 
ATOM   2642 O OE1   . GLN   B 1 120 ? -41.90500 -1.79000  59.29400 1.000 32.49757 ?  100 GLN   B OE1   1 
ATOM   2643 N NE2   . GLN   B 1 120 ? -42.04400 -0.75000  57.30200 1.000 32.60167 ?  100 GLN   B NE2   1 
ATOM   2644 N N     . ASN   B 1 121 ? -36.90400 -3.07100  58.32700 1.000 23.63943 ?  101 ASN   B N     1 
ATOM   2645 C CA    . ASN   B 1 121 ? -35.99000 -2.95000  59.45800 1.000 25.50774 ?  101 ASN   B CA    1 
ATOM   2646 C C     . ASN   B 1 121 ? -36.75700 -2.64700  60.73500 1.000 23.95888 ?  101 ASN   B C     1 
ATOM   2647 O O     . ASN   B 1 121 ? -37.69900 -1.85000  60.74400 1.000 20.73557 ?  101 ASN   B O     1 
ATOM   2648 C CB    . ASN   B 1 121 ? -34.96100 -1.83600  59.21400 1.000 25.88345 ?  101 ASN   B CB    1 
ATOM   2649 C CG    . ASN   B 1 121 ? -34.03000 -2.13700  58.05000 1.000 28.62168 ?  101 ASN   B CG    1 
ATOM   2650 O OD1   . ASN   B 1 121 ? -33.53700 -3.25200  57.91900 1.000 30.28611 ?  101 ASN   B OD1   1 
ATOM   2651 N ND2   . ASN   B 1 121 ? -33.77200 -1.12700  57.21000 1.000 29.90099 ?  101 ASN   B ND2   1 
ATOM   2652 N N     . GLY   B 1 122 ? -36.34500 -3.29300  61.82100 1.000 22.86887 ?  102 GLY   B N     1 
ATOM   2653 C CA    . GLY   B 1 122 ? -36.94900 -3.07400  63.11200 1.000 22.46816 ?  102 GLY   B CA    1 
ATOM   2654 C C     . GLY   B 1 122 ? -35.88000 -2.67400  64.11100 1.000 22.83330 ?  102 GLY   B C     1 
ATOM   2655 O O     . GLY   B 1 122 ? -34.85800 -2.08500  63.73600 1.000 25.23057 ?  102 GLY   B O     1 
ATOM   2656 N N     . GLU   B 1 123 ? -36.06800 -3.05800  65.36500 1.000 21.59250 ?  103 GLU   B N     1 
ATOM   2657 C CA    . GLU   B 1 123 ? -35.08000 -2.80800  66.41800 1.000 20.66892 ?  103 GLU   B CA    1 
ATOM   2658 C C     . GLU   B 1 123 ? -33.92900 -3.82100  66.35700 1.000 28.01532 ?  103 GLU   B C     1 
ATOM   2659 O O     . GLU   B 1 123 ? -34.15500 -5.03300  66.44600 1.000 22.90247 ?  103 GLU   B O     1 
ATOM   2660 C CB    . GLU   B 1 123 ? -35.77800 -2.86600  67.77700 1.000 23.82832 ?  103 GLU   B CB    1 
ATOM   2661 C CG    . GLU   B 1 123 ? -34.98500 -2.23200  68.90800 1.000 23.02388 ?  103 GLU   B CG    1 
ATOM   2662 C CD    . GLU   B 1 123 ? -35.72200 -2.31900  70.23700 1.000 28.12265 ?  103 GLU   B CD    1 
ATOM   2663 O OE1   . GLU   B 1 123 ? -36.82500 -1.74700  70.36200 1.000 26.14054 ?  103 GLU   B OE1   1 
ATOM   2664 O OE2   . GLU   B 1 123 ? -35.18700 -2.97100  71.15600 1.000 30.81997 -1 103 GLU   B OE2   1 
ATOM   2665 N N     . GLY   B 1 124 ? -32.69300 -3.33200  66.23000 1.000 23.93797 ?  104 GLY   B N     1 
ATOM   2666 C CA    . GLY   B 1 124 ? -31.53700 -4.22500  66.22300 1.000 24.94075 ?  104 GLY   B CA    1 
ATOM   2667 C C     . GLY   B 1 124 ? -31.58200 -5.16400  65.02600 1.000 27.00958 ?  104 GLY   B C     1 
ATOM   2668 O O     . GLY   B 1 124 ? -31.69100 -4.73100  63.87800 1.000 28.58441 ?  104 GLY   B O     1 
ATOM   2669 N N     . GLU   B 1 125 ? -31.51200 -6.47100  65.26400 1.000 25.84256 ?  105 GLU   B N     1 
ATOM   2670 C CA    . GLU   B 1 125 ? -31.64700 -7.43000  64.18000 1.000 28.58599 ?  105 GLU   B CA    1 
ATOM   2671 C C     . GLU   B 1 125 ? -33.10500 -7.78000  63.89700 1.000 25.68426 ?  105 GLU   B C     1 
ATOM   2672 O O     . GLU   B 1 125 ? -33.38200 -8.56000  62.97800 1.000 26.31358 ?  105 GLU   B O     1 
ATOM   2673 C CB    . GLU   B 1 125 ? -30.83300 -8.69700  64.50800 1.000 30.12170 ?  105 GLU   B CB    1 
ATOM   2674 C CG    . GLU   B 1 125 ? -31.39500 -9.50000  65.67700 1.000 27.61359 ?  105 GLU   B CG    1 
ATOM   2675 C CD    . GLU   B 1 125 ? -30.70500 -10.86100 65.86100 1.000 38.78533 ?  105 GLU   B CD    1 
ATOM   2676 O OE1   . GLU   B 1 125 ? -29.77600 -11.17800 65.08600 1.000 35.65930 ?  105 GLU   B OE1   1 
ATOM   2677 O OE2   . GLU   B 1 125 ? -31.09900 -11.60900 66.78000 1.000 31.63140 -1 105 GLU   B OE2   1 
ATOM   2678 N N     . LEU   B 1 126 ? -34.04600 -7.23400  64.65600 1.000 24.79114 ?  106 LEU   B N     1 
ATOM   2679 C CA    . LEU   B 1 126 ? -35.43600 -7.63700  64.49000 1.000 23.04294 ?  106 LEU   B CA    1 
ATOM   2680 C C     . LEU   B 1 126 ? -35.99200 -7.03200  63.19600 1.000 26.07003 ?  106 LEU   B C     1 
ATOM   2681 O O     . LEU   B 1 126 ? -35.53900 -5.97700  62.73100 1.000 24.84921 ?  106 LEU   B O     1 
ATOM   2682 C CB    . LEU   B 1 126 ? -36.27000 -7.18600  65.68200 1.000 20.56438 ?  106 LEU   B CB    1 
ATOM   2683 C CG    . LEU   B 1 126 ? -35.82800 -7.75300  67.04000 1.000 20.24699 ?  106 LEU   B CG    1 
ATOM   2684 C CD1   . LEU   B 1 126 ? -36.73700 -7.27600  68.15000 1.000 25.48414 ?  106 LEU   B CD1   1 
ATOM   2685 C CD2   . LEU   B 1 126 ? -35.75000 -9.30500  66.98200 1.000 24.54838 ?  106 LEU   B CD2   1 
ATOM   2686 N N     . LYS   B 1 127 ? -36.96900 -7.72200  62.60700 1.000 24.57248 ?  107 LYS   B N     1 
ATOM   2687 C CA    . LYS   B 1 127 ? -37.54800 -7.33200  61.32300 1.000 24.73845 ?  107 LYS   B CA    1 
ATOM   2688 C C     . LYS   B 1 127 ? -39.06200 -7.45100  61.38400 1.000 30.72012 ?  107 LYS   B C     1 
ATOM   2689 O O     . LYS   B 1 127 ? -39.61300 -8.16000  62.22600 1.000 27.81406 ?  107 LYS   B O     1 
ATOM   2690 C CB    . LYS   B 1 127 ? -37.03200 -8.22100  60.16600 1.000 26.02042 ?  107 LYS   B CB    1 
ATOM   2691 C CG    . LYS   B 1 127 ? -35.51000 -8.27600  60.03700 1.000 32.43779 ?  107 LYS   B CG    1 
ATOM   2692 C CD    . LYS   B 1 127 ? -34.94300 -7.04500  59.34700 1.000 27.67385 ?  107 LYS   B CD    1 
ATOM   2693 C CE    . LYS   B 1 127 ? -33.43800 -7.14900  59.18000 1.000 32.31708 ?  107 LYS   B CE    1 
ATOM   2694 N NZ    . LYS   B 1 127 ? -32.85300 -5.82400  58.78500 1.000 32.55526 ?  107 LYS   B NZ    1 
ATOM   2695 N N     . ASN   B 1 128 ? -39.74000 -6.78100  60.45300 1.000 24.02565 ?  108 ASN   B N     1 
ATOM   2696 C CA    . ASN   B 1 128 ? -41.17100 -6.98300  60.24200 1.000 22.78326 ?  108 ASN   B CA    1 
ATOM   2697 C C     . ASN   B 1 128 ? -41.38200 -7.39400  58.79100 1.000 30.60711 ?  108 ASN   B C     1 
ATOM   2698 O O     . ASN   B 1 128 ? -41.00500 -6.66300  57.87300 1.000 26.98358 ?  108 ASN   B O     1 
ATOM   2699 C CB    . ASN   B 1 128 ? -41.95700 -5.72200  60.58800 1.000 23.39487 ?  108 ASN   B CB    1 
ATOM   2700 C CG    . ASN   B 1 128 ? -41.89700 -5.41300  62.06400 1.000 30.43044 ?  108 ASN   B CG    1 
ATOM   2701 O OD1   . ASN   B 1 128 ? -42.34600 -6.20600  62.89500 1.000 32.14719 ?  108 ASN   B OD1   1 
ATOM   2702 N ND2   . ASN   B 1 128 ? -41.32500 -4.26900  62.40500 1.000 33.98736 ?  108 ASN   B ND2   1 
ATOM   2703 N N     . TYR   B 1 129 ? -41.95300 -8.57400  58.58100 1.000 24.12030 ?  109 TYR   B N     1 
ATOM   2704 C CA    . TYR   B 1 129 ? -42.16200 -9.06000  57.22700 1.000 23.58989 ?  109 TYR   B CA    1 
ATOM   2705 C C     . TYR   B 1 129 ? -43.37600 -8.36000  56.64000 1.000 29.21806 ?  109 TYR   B C     1 
ATOM   2706 O O     . TYR   B 1 129 ? -44.41400 -8.24000  57.30300 1.000 28.13676 ?  109 TYR   B O     1 
ATOM   2707 C CB    . TYR   B 1 129 ? -42.34400 -10.58200 57.23100 1.000 24.86423 ?  109 TYR   B CB    1 
ATOM   2708 C CG    . TYR   B 1 129 ? -42.52700 -11.19200 55.84700 1.000 27.58161 ?  109 TYR   B CG    1 
ATOM   2709 C CD1   . TYR   B 1 129 ? -41.47100 -11.25600 54.94200 1.000 29.86361 ?  109 TYR   B CD1   1 
ATOM   2710 C CD2   . TYR   B 1 129 ? -43.76000 -11.68800 55.44600 1.000 36.68938 ?  109 TYR   B CD2   1 
ATOM   2711 C CE1   . TYR   B 1 129 ? -41.64300 -11.81200 53.67000 1.000 35.68061 ?  109 TYR   B CE1   1 
ATOM   2712 C CE2   . TYR   B 1 129 ? -43.94100 -12.25100 54.17700 1.000 39.73484 ?  109 TYR   B CE2   1 
ATOM   2713 C CZ    . TYR   B 1 129 ? -42.88100 -12.31000 53.29800 1.000 46.51564 ?  109 TYR   B CZ    1 
ATOM   2714 O OH    . TYR   B 1 129 ? -43.06300 -12.87100 52.04600 1.000 45.14980 ?  109 TYR   B OH    1 
ATOM   2715 N N     . LYS   B 1 130 ? -43.23600 -7.86400  55.41000 1.000 28.51830 ?  110 LYS   B N     1 
ATOM   2716 C CA    . LYS   B 1 130 ? -44.28500 -7.09900  54.75300 1.000 23.27320 ?  110 LYS   B CA    1 
ATOM   2717 C C     . LYS   B 1 130 ? -44.51700 -7.65300  53.35200 1.000 22.97064 ?  110 LYS   B C     1 
ATOM   2718 O O     . LYS   B 1 130 ? -43.60700 -8.18400  52.71500 1.000 26.72621 ?  110 LYS   B O     1 
ATOM   2719 C CB    . LYS   B 1 130 ? -43.93200 -5.59500  54.66700 1.000 27.68565 ?  110 LYS   B CB    1 
ATOM   2720 C CG    . LYS   B 1 130 ? -43.62100 -4.95300  56.01200 1.000 30.47990 ?  110 LYS   B CG    1 
ATOM   2721 C CD    . LYS   B 1 130 ? -44.88500 -4.41700  56.64800 1.000 30.79805 ?  110 LYS   B CD    1 
ATOM   2722 C CE    . LYS   B 1 130 ? -44.58000 -3.72000  57.94200 1.000 39.65688 ?  110 LYS   B CE    1 
ATOM   2723 N NZ    . LYS   B 1 130 ? -45.80000 -3.59000  58.77400 1.000 45.54872 ?  110 LYS   B NZ    1 
ATOM   2724 N N     . VAL   B 1 131 ? -45.75400 -7.55100  52.88100 1.000 27.90889 ?  111 VAL   B N     1 
ATOM   2725 C CA    . VAL   B 1 131 ? -46.09900 -7.98300  51.53200 1.000 23.99824 ?  111 VAL   B CA    1 
ATOM   2726 C C     . VAL   B 1 131 ? -46.57600 -6.76900  50.76000 1.000 25.64853 ?  111 VAL   B C     1 
ATOM   2727 O O     . VAL   B 1 131 ? -47.42500 -6.01400  51.24900 1.000 32.18117 ?  111 VAL   B O     1 
ATOM   2728 C CB    . VAL   B 1 131 ? -47.17300 -9.08500  51.53600 1.000 32.44531 ?  111 VAL   B CB    1 
ATOM   2729 C CG1   . VAL   B 1 131 ? -47.59100 -9.42100  50.10400 1.000 34.46622 ?  111 VAL   B CG1   1 
ATOM   2730 C CG2   . VAL   B 1 131 ? -46.63700 -10.31500 52.23100 1.000 35.53946 ?  111 VAL   B CG2   1 
ATOM   2731 N N     . ILE   B 1 132 ? -45.99600 -6.55800  49.58000 1.000 28.43683 ?  112 ILE   B N     1 
ATOM   2732 C CA    . ILE   B 1 132 ? -46.43500 -5.50800  48.66200 1.000 28.15078 ?  112 ILE   B CA    1 
ATOM   2733 C C     . ILE   B 1 132 ? -47.40300 -6.14500  47.67900 1.000 27.02791 ?  112 ILE   B C     1 
ATOM   2734 O O     . ILE   B 1 132 ? -47.03000 -7.08100  46.96600 1.000 30.25759 ?  112 ILE   B O     1 
ATOM   2735 C CB    . ILE   B 1 132 ? -45.26100 -4.87100  47.90000 1.000 26.52449 ?  112 ILE   B CB    1 
ATOM   2736 C CG1   . ILE   B 1 132 ? -44.25800 -4.21600  48.86100 1.000 28.72082 ?  112 ILE   B CG1   1 
ATOM   2737 C CG2   . ILE   B 1 132 ? -45.78400 -3.83900  46.86400 1.000 24.89605 ?  112 ILE   B CG2   1 
ATOM   2738 C CD1   . ILE   B 1 132 ? -42.87000 -3.99400  48.23700 1.000 25.13167 ?  112 ILE   B CD1   1 
ATOM   2739 N N     . ASP   B 1 133 ? -48.62200 -5.62300  47.61900 1.000 27.87934 ?  113 ASP   B N     1 
ATOM   2740 C CA    . ASP   B 1 133 ? -49.64700 -6.10000  46.69300 1.000 29.67304 ?  113 ASP   B CA    1 
ATOM   2741 C C     . ASP   B 1 133 ? -49.86100 -5.04600  45.61200 1.000 23.34661 ?  113 ASP   B C     1 
ATOM   2742 O O     . ASP   B 1 133 ? -50.37500 -3.96200  45.89900 1.000 31.91506 ?  113 ASP   B O     1 
ATOM   2743 C CB    . ASP   B 1 133 ? -50.94500 -6.39900  47.44500 1.000 33.40427 ?  113 ASP   B CB    1 
ATOM   2744 C CG    . ASP   B 1 133 ? -52.01800 -7.03000  46.55800 1.000 41.06199 ?  113 ASP   B CG    1 
ATOM   2745 O OD1   . ASP   B 1 133 ? -51.82600 -7.14400  45.32500 1.000 47.53816 ?  113 ASP   B OD1   1 
ATOM   2746 O OD2   . ASP   B 1 133 ? -53.05900 -7.44600  47.11300 1.000 58.72693 -1 113 ASP   B OD2   1 
ATOM   2747 N N     . ARG   B 1 134 ? -49.47400 -5.38700  44.38100 1.000 30.31819 ?  114 ARG   B N     1 
ATOM   2748 C CA    . ARG   B 1 134 ? -49.65400 -4.56400  43.18800 1.000 29.85026 ?  114 ARG   B CA    1 
ATOM   2749 C C     . ARG   B 1 134 ? -51.03300 -3.92600  43.16400 1.000 34.93364 ?  114 ARG   B C     1 
ATOM   2750 O O     . ARG   B 1 134 ? -51.17500 -2.72800  42.89400 1.000 37.90079 ?  114 ARG   B O     1 
ATOM   2751 C CB    . ARG   B 1 134 ? -49.46900 -5.41500  41.92700 1.000 34.93698 ?  114 ARG   B CB    1 
ATOM   2752 C CG    . ARG   B 1 134 ? -49.49200 -4.64100  40.61300 1.000 30.45747 ?  114 ARG   B CG    1 
ATOM   2753 C CD    . ARG   B 1 134 ? -49.39900 -5.58700  39.42500 1.000 34.78737 ?  114 ARG   B CD    1 
ATOM   2754 N NE    . ARG   B 1 134 ? -50.56400 -6.46300  39.35700 1.000 35.15963 ?  114 ARG   B NE    1 
ATOM   2755 C CZ    . ARG   B 1 134 ? -50.56600 -7.66600  38.79600 1.000 35.76001 ?  114 ARG   B CZ    1 
ATOM   2756 N NH1   . ARG   B 1 134 ? -49.47000 -8.19100  38.28100 1.000 37.54501 ?  114 ARG   B NH1   1 
ATOM   2757 N NH2   . ARG   B 1 134 ? -51.69300 -8.37100  38.77200 1.000 41.87710 ?  114 ARG   B NH2   1 
ATOM   2758 N N     . GLU   B 1 135 ? -52.05700 -4.72400  43.46300 1.000 34.65166 ?  115 GLU   B N     1 
ATOM   2759 C CA    . GLU   B 1 135 ? -53.41900 -4.22000  43.37100 1.000 37.34409 ?  115 GLU   B CA    1 
ATOM   2760 C C     . GLU   B 1 135 ? -53.78700 -3.25000  44.48800 1.000 37.90877 ?  115 GLU   B C     1 
ATOM   2761 O O     . GLU   B 1 135 ? -54.89400 -2.69800  44.44500 1.000 38.92221 ?  115 GLU   B O     1 
ATOM   2762 C CB    . GLU   B 1 135 ? -54.40300 -5.39500  43.32400 1.000 43.46669 ?  115 GLU   B CB    1 
ATOM   2763 C CG    . GLU   B 1 135 ? -54.15400 -6.33700  42.13800 1.000 42.00320 ?  115 GLU   B CG    1 
ATOM   2764 C CD    . GLU   B 1 135 ? -54.24800 -5.63200  40.78700 1.000 53.13080 ?  115 GLU   B CD    1 
ATOM   2765 O OE1   . GLU   B 1 135 ? -55.22200 -4.88000  40.57000 1.000 48.81320 ?  115 GLU   B OE1   1 
ATOM   2766 O OE2   . GLU   B 1 135 ? -53.34400 -5.82200  39.94000 1.000 50.42156 -1 115 GLU   B OE2   1 
ATOM   2767 N N     . GLY   B 1 136 ? -52.90200 -2.97900  45.45000 1.000 33.75041 ?  116 GLY   B N     1 
ATOM   2768 C CA    . GLY   B 1 136 ? -53.16800 -1.95000  46.43000 1.000 27.06367 ?  116 GLY   B CA    1 
ATOM   2769 C C     . GLY   B 1 136 ? -52.74800 -0.53900  46.06100 1.000 31.71354 ?  116 GLY   B C     1 
ATOM   2770 O O     . GLY   B 1 136 ? -52.86100 0.36900   46.89000 1.000 36.89234 ?  116 GLY   B O     1 
ATOM   2771 N N     . TYR   B 1 137 ? -52.25300 -0.31700  44.85100 1.000 26.99468 ?  117 TYR   B N     1 
ATOM   2772 C CA    . TYR   B 1 137 ? -51.75700 0.98800   44.42700 1.000 30.33723 ?  117 TYR   B CA    1 
ATOM   2773 C C     . TYR   B 1 137 ? -52.49200 1.44000   43.17300 1.000 29.25155 ?  117 TYR   B C     1 
ATOM   2774 O O     . TYR   B 1 137 ? -52.86100 0.62000   42.32900 1.000 33.01229 ?  117 TYR   B O     1 
ATOM   2775 C CB    . TYR   B 1 137 ? -50.24800 0.93200   44.13300 1.000 27.27859 ?  117 TYR   B CB    1 
ATOM   2776 C CG    . TYR   B 1 137 ? -49.42800 0.46800   45.32000 1.000 24.74499 ?  117 TYR   B CG    1 
ATOM   2777 C CD1   . TYR   B 1 137 ? -49.29200 -0.88100  45.62000 1.000 28.66059 ?  117 TYR   B CD1   1 
ATOM   2778 C CD2   . TYR   B 1 137 ? -48.77200 1.39000   46.12500 1.000 32.69221 ?  117 TYR   B CD2   1 
ATOM   2779 C CE1   . TYR   B 1 137 ? -48.54100 -1.30100  46.72300 1.000 30.51028 ?  117 TYR   B CE1   1 
ATOM   2780 C CE2   . TYR   B 1 137 ? -48.02200 0.99100   47.21800 1.000 28.51808 ?  117 TYR   B CE2   1 
ATOM   2781 C CZ    . TYR   B 1 137 ? -47.90700 -0.35200  47.51100 1.000 30.35588 ?  117 TYR   B CZ    1 
ATOM   2782 O OH    . TYR   B 1 137 ? -47.17500 -0.73100  48.60000 1.000 26.85037 ?  117 TYR   B OH    1 
ATOM   2783 N N     . ALA   B 1 138 ? -52.64200 2.75800   43.03300 1.000 32.63025 ?  118 ALA   B N     1 
ATOM   2784 C CA    . ALA   B 1 138 ? -53.29200 3.30900   41.84600 1.000 35.65926 ?  118 ALA   B CA    1 
ATOM   2785 C C     . ALA   B 1 138 ? -52.57100 2.92100   40.56000 1.000 38.24307 ?  118 ALA   B C     1 
ATOM   2786 O O     . ALA   B 1 138 ? -53.21500 2.80300   39.51200 1.000 39.55552 ?  118 ALA   B O     1 
ATOM   2787 C CB    . ALA   B 1 138 ? -53.37900 4.83400   41.95300 1.000 35.48621 ?  118 ALA   B CB    1 
ATOM   2788 N N     . PHE   B 1 139 ? -51.23900 2.72500   40.60600 1.000 31.05738 ?  119 PHE   B N     1 
ATOM   2789 C CA    . PHE   B 1 139 ? -50.53200 2.34500   39.38000 1.000 27.65059 ?  119 PHE   B CA    1 
ATOM   2790 C C     . PHE   B 1 139 ? -50.92100 0.96300   38.86000 1.000 28.43855 ?  119 PHE   B C     1 
ATOM   2791 O O     . PHE   B 1 139 ? -50.43500 0.55800   37.79600 1.000 28.99044 ?  119 PHE   B O     1 
ATOM   2792 C CB    . PHE   B 1 139 ? -49.00000 2.47000   39.58200 1.000 29.93493 ?  119 PHE   B CB    1 
ATOM   2793 C CG    . PHE   B 1 139 ? -48.37800 1.41000   40.48800 1.000 28.86533 ?  119 PHE   B CG    1 
ATOM   2794 C CD1   . PHE   B 1 139 ? -48.29400 0.08000   40.08800 1.000 27.43575 ?  119 PHE   B CD1   1 
ATOM   2795 C CD2   . PHE   B 1 139 ? -47.86100 1.76600   41.73400 1.000 26.45643 ?  119 PHE   B CD2   1 
ATOM   2796 C CE1   . PHE   B 1 139 ? -47.72200 -0.89100  40.90500 1.000 32.05338 ?  119 PHE   B CE1   1 
ATOM   2797 C CE2   . PHE   B 1 139 ? -47.28600 0.79200   42.56500 1.000 25.09015 ?  119 PHE   B CE2   1 
ATOM   2798 C CZ    . PHE   B 1 139 ? -47.21900 -0.52900  42.15100 1.000 29.28274 ?  119 PHE   B CZ    1 
ATOM   2799 N N     . ARG   B 1 140 ? -51.77600 0.21900   39.56000 1.000 31.68718 ?  120 ARG   B N     1 
ATOM   2800 C CA    . ARG   B 1 140 ? -52.24200 -1.05900  39.02600 1.000 35.39164 ?  120 ARG   B CA    1 
ATOM   2801 C C     . ARG   B 1 140 ? -52.92500 -0.91400  37.66700 1.000 33.28730 ?  120 ARG   B C     1 
ATOM   2802 O O     . ARG   B 1 140 ? -53.02200 -1.89700  36.93500 1.000 32.17909 ?  120 ARG   B O     1 
ATOM   2803 C CB    . ARG   B 1 140 ? -53.21100 -1.72800  40.00100 1.000 30.87694 ?  120 ARG   B CB    1 
ATOM   2804 C CG    . ARG   B 1 140 ? -54.51200 -0.94700  40.13800 1.000 32.56448 ?  120 ARG   B CG    1 
ATOM   2805 C CD    . ARG   B 1 140 ? -55.40900 -1.47300  41.24900 1.000 36.54146 ?  120 ARG   B CD    1 
ATOM   2806 N NE    . ARG   B 1 140 ? -56.48500 -0.53200  41.54600 1.000 48.44915 ?  120 ARG   B NE    1 
ATOM   2807 C CZ    . ARG   B 1 140 ? -57.51100 -0.79000  42.34600 1.000 61.83066 ?  120 ARG   B CZ    1 
ATOM   2808 N N     . ASP   B 1 141 ? -53.36500 0.28400   37.29400 1.000 37.25425 ?  121 ASP   B N     1 
ATOM   2809 C CA    . ASP   B 1 141 ? -54.04100 0.43400   36.00900 1.000 39.40063 ?  121 ASP   B CA    1 
ATOM   2810 C C     . ASP   B 1 141 ? -53.08200 0.56900   34.82900 1.000 45.55333 ?  121 ASP   B C     1 
ATOM   2811 O O     . ASP   B 1 141 ? -53.54700 0.63400   33.68000 1.000 40.62045 ?  121 ASP   B O     1 
ATOM   2812 C CB    . ASP   B 1 141 ? -54.98600 1.63500   36.05900 1.000 33.84027 ?  121 ASP   B CB    1 
ATOM   2813 C CG    . ASP   B 1 141 ? -54.25500 2.97100   36.22400 1.000 43.99614 ?  121 ASP   B CG    1 
ATOM   2814 O OD1   . ASP   B 1 141 ? -53.02700 2.99300   36.48300 1.000 42.60403 ?  121 ASP   B OD1   1 
ATOM   2815 O OD2   . ASP   B 1 141 ? -54.93000 4.01800   36.13500 1.000 40.92098 -1 121 ASP   B OD2   1 
ATOM   2816 N N     . SER   B 1 142 ? -51.76100 0.60200   35.06600 1.000 31.65789 ?  122 SER   B N     1 
ATOM   2817 C CA    . SER   B 1 142 ? -50.83100 0.87400   33.97400 1.000 28.67805 ?  122 SER   B CA    1 
ATOM   2818 C C     . SER   B 1 142 ? -49.60800 -0.03300  33.93400 1.000 29.65807 ?  122 SER   B C     1 
ATOM   2819 O O     . SER   B 1 142 ? -48.72000 0.19600   33.10100 1.000 29.33079 ?  122 SER   B O     1 
ATOM   2820 C CB    . SER   B 1 142 ? -50.37100 2.33200   34.02700 1.000 32.03511 ?  122 SER   B CB    1 
ATOM   2821 O OG    . SER   B 1 142 ? -51.47900 3.17900   34.25500 1.000 32.27665 ?  122 SER   B OG    1 
ATOM   2822 N N     . PHE   B 1 143 ? -49.53700 -1.06900  34.77100 1.000 33.00132 ?  123 PHE   B N     1 
ATOM   2823 C CA    . PHE   B 1 143 ? -48.25900 -1.74200  34.97900 1.000 29.67859 ?  123 PHE   B CA    1 
ATOM   2824 C C     . PHE   B 1 143 ? -47.79500 -2.55000  33.78100 1.000 30.38687 ?  123 PHE   B C     1 
ATOM   2825 O O     . PHE   B 1 143 ? -46.60400 -2.89000  33.72200 1.000 32.49144 ?  123 PHE   B O     1 
ATOM   2826 C CB    . PHE   B 1 143 ? -48.32400 -2.61900  36.23000 1.000 28.78400 ?  123 PHE   B CB    1 
ATOM   2827 C CG    . PHE   B 1 143 ? -49.20300 -3.83300  36.07900 1.000 34.09532 ?  123 PHE   B CG    1 
ATOM   2828 C CD1   . PHE   B 1 143 ? -48.69100 -5.03500  35.59200 1.000 33.66569 ?  123 PHE   B CD1   1 
ATOM   2829 C CD2   . PHE   B 1 143 ? -50.53600 -3.77000  36.44300 1.000 33.79099 ?  123 PHE   B CD2   1 
ATOM   2830 C CE1   . PHE   B 1 143 ? -49.50800 -6.15100  35.45300 1.000 39.93460 ?  123 PHE   B CE1   1 
ATOM   2831 C CE2   . PHE   B 1 143 ? -51.35900 -4.88800  36.31000 1.000 37.20364 ?  123 PHE   B CE2   1 
ATOM   2832 C CZ    . PHE   B 1 143 ? -50.84300 -6.07200  35.81500 1.000 33.17469 ?  123 PHE   B CZ    1 
ATOM   2833 N N     . THR   B 1 144 ? -48.67400 -2.84100  32.81200 1.000 29.69574 ?  124 THR   B N     1 
ATOM   2834 C CA    . THR   B 1 144 ? -48.22600 -3.57000  31.63200 1.000 30.46073 ?  124 THR   B CA    1 
ATOM   2835 C C     . THR   B 1 144 ? -47.49100 -2.68500  30.63800 1.000 28.48839 ?  124 THR   B C     1 
ATOM   2836 O O     . THR   B 1 144 ? -46.94900 -3.20200  29.65500 1.000 32.93692 ?  124 THR   B O     1 
ATOM   2837 C CB    . THR   B 1 144 ? -49.40400 -4.25400  30.91800 1.000 36.71286 ?  124 THR   B CB    1 
ATOM   2838 O OG1   . THR   B 1 144 ? -50.32700 -3.26600  30.44900 1.000 38.67240 ?  124 THR   B OG1   1 
ATOM   2839 C CG2   . THR   B 1 144 ? -50.11900 -5.20900  31.86900 1.000 38.80394 ?  124 THR   B CG2   1 
ATOM   2840 N N     . LYS   B 1 145 ? -47.44000 -1.37800  30.87000 1.000 32.68604 ?  125 LYS   B N     1 
ATOM   2841 C CA    . LYS   B 1 145 ? -46.74000 -0.47700  29.96700 1.000 28.58781 ?  125 LYS   B CA    1 
ATOM   2842 C C     . LYS   B 1 145 ? -45.26400 -0.30500  30.31000 1.000 37.57584 ?  125 LYS   B C     1 
ATOM   2843 O O     . LYS   B 1 145 ? -44.58200 0.48200   29.64700 1.000 27.41301 ?  125 LYS   B O     1 
ATOM   2844 C CB    . LYS   B 1 145 ? -47.44700 0.87400   29.95900 1.000 31.01432 ?  125 LYS   B CB    1 
ATOM   2845 C CG    . LYS   B 1 145 ? -48.89500 0.75600   29.50800 1.000 34.02831 ?  125 LYS   B CG    1 
ATOM   2846 C CD    . LYS   B 1 145 ? -49.78400 1.86000   30.07200 1.000 40.05307 ?  125 LYS   B CD    1 
ATOM   2847 C CE    . LYS   B 1 145 ? -49.68300 3.10000   29.26000 1.000 32.95121 ?  125 LYS   B CE    1 
ATOM   2848 N NZ    . LYS   B 1 145 ? -50.15600 4.30600   30.02600 1.000 31.98542 ?  125 LYS   B NZ    1 
ATOM   2849 N N     . VAL   B 1 146 ? -44.75700 -1.04300  31.30400 1.000 27.65335 ?  126 VAL   B N     1 
ATOM   2850 C CA    . VAL   B 1 146 ? -43.38000 -0.95100  31.78000 1.000 26.66000 ?  126 VAL   B CA    1 
ATOM   2851 C C     . VAL   B 1 146 ? -42.61400 -2.19200  31.36500 1.000 27.99445 ?  126 VAL   B C     1 
ATOM   2852 O O     . VAL   B 1 146 ? -43.14000 -3.31000  31.42700 1.000 27.87603 ?  126 VAL   B O     1 
ATOM   2853 C CB    . VAL   B 1 146 ? -43.31200 -0.80700  33.31800 1.000 29.49808 ?  126 VAL   B CB    1 
ATOM   2854 C CG1   . VAL   B 1 146 ? -41.87900 -0.49900  33.76800 1.000 30.18396 ?  126 VAL   B CG1   1 
ATOM   2855 C CG2   . VAL   B 1 146 ? -44.24300 0.27600   33.80100 1.000 30.62891 ?  126 VAL   B CG2   1 
ATOM   2856 N N     . GLU   B 1 147 ? -41.35800 -1.99500  30.98400 1.000 23.96976 ?  127 GLU   B N     1 
ATOM   2857 C CA    . GLU   B 1 147 ? -40.39000 -3.07200  30.81600 1.000 24.19795 ?  127 GLU   B CA    1 
ATOM   2858 C C     . GLU   B 1 147 ? -39.16300 -2.75900  31.66400 1.000 26.61400 ?  127 GLU   B C     1 
ATOM   2859 O O     . GLU   B 1 147 ? -38.60500 -1.66300  31.55700 1.000 27.26036 ?  127 GLU   B O     1 
ATOM   2860 C CB    . GLU   B 1 147 ? -39.98500 -3.19500  29.35100 1.000 31.43804 ?  127 GLU   B CB    1 
ATOM   2861 C CG    . GLU   B 1 147 ? -41.11500 -3.66400  28.45200 1.000 42.42322 ?  127 GLU   B CG    1 
ATOM   2862 C CD    . GLU   B 1 147 ? -40.61100 -4.21200  27.13200 1.000 50.73768 ?  127 GLU   B CD    1 
ATOM   2863 O OE1   . GLU   B 1 147 ? -39.55200 -4.87400  27.13000 1.000 55.97898 ?  127 GLU   B OE1   1 
ATOM   2864 O OE2   . GLU   B 1 147 ? -41.27600 -3.97400  26.09900 1.000 66.11916 -1 127 GLU   B OE2   1 
ATOM   2865 N N     . PHE   B 1 148 ? -38.72500 -3.72700  32.46500 1.000 24.80919 ?  128 PHE   B N     1 
ATOM   2866 C CA    . PHE   B 1 148 ? -37.57500 -3.59000  33.35000 1.000 29.01717 ?  128 PHE   B CA    1 
ATOM   2867 C C     . PHE   B 1 148 ? -36.37300 -4.33800  32.79000 1.000 32.24107 ?  128 PHE   B C     1 
ATOM   2868 O O     . PHE   B 1 148 ? -36.50000 -5.46900  32.30200 1.000 26.45080 ?  128 PHE   B O     1 
ATOM   2869 C CB    . PHE   B 1 148 ? -37.89500 -4.12100  34.75200 1.000 27.36512 ?  128 PHE   B CB    1 
ATOM   2870 C CG    . PHE   B 1 148 ? -38.92100 -3.30100  35.49500 1.000 28.10228 ?  128 PHE   B CG    1 
ATOM   2871 C CD1   . PHE   B 1 148 ? -38.61000 -2.01800  35.96200 1.000 21.65057 ?  128 PHE   B CD1   1 
ATOM   2872 C CD2   . PHE   B 1 148 ? -40.19600 -3.80400  35.73000 1.000 23.68345 ?  128 PHE   B CD2   1 
ATOM   2873 C CE1   . PHE   B 1 148 ? -39.53900 -1.27200  36.66300 1.000 20.98183 ?  128 PHE   B CE1   1 
ATOM   2874 C CE2   . PHE   B 1 148 ? -41.14000 -3.05800  36.42200 1.000 22.13101 ?  128 PHE   B CE2   1 
ATOM   2875 C CZ    . PHE   B 1 148 ? -40.81000 -1.77000  36.88900 1.000 24.21769 ?  128 PHE   B CZ    1 
ATOM   2876 N N     . PHE   B 1 149 ? -35.20000 -3.71900  32.88700 1.000 23.33600 ?  129 PHE   B N     1 
ATOM   2877 C CA    . PHE   B 1 149 ? -33.97500 -4.28500  32.33600 1.000 23.65595 ?  129 PHE   B CA    1 
ATOM   2878 C C     . PHE   B 1 149 ? -32.81900 -4.03600  33.29200 1.000 27.78773 ?  129 PHE   B C     1 
ATOM   2879 O O     . PHE   B 1 149 ? -32.73600 -2.97700  33.93000 1.000 25.86746 ?  129 PHE   B O     1 
ATOM   2880 C CB    . PHE   B 1 149 ? -33.57400 -3.65400  30.98400 1.000 24.46352 ?  129 PHE   B CB    1 
ATOM   2881 C CG    . PHE   B 1 149 ? -34.63800 -3.69800  29.92800 1.000 27.03190 ?  129 PHE   B CG    1 
ATOM   2882 C CD1   . PHE   B 1 149 ? -35.61300 -2.71300  29.85900 1.000 30.35781 ?  129 PHE   B CD1   1 
ATOM   2883 C CD2   . PHE   B 1 149 ? -34.60800 -4.67900  28.94900 1.000 32.57768 ?  129 PHE   B CD2   1 
ATOM   2884 C CE1   . PHE   B 1 149 ? -36.57800 -2.72800  28.86500 1.000 33.22764 ?  129 PHE   B CE1   1 
ATOM   2885 C CE2   . PHE   B 1 149 ? -35.57800 -4.70600  27.94400 1.000 35.12783 ?  129 PHE   B CE2   1 
ATOM   2886 C CZ    . PHE   B 1 149 ? -36.56100 -3.72800  27.90400 1.000 31.82230 ?  129 PHE   B CZ    1 
ATOM   2887 N N     . GLN   B 1 150 ? -31.89600 -4.99200  33.35000 1.000 24.18476 ?  130 GLN   B N     1 
ATOM   2888 C CA    . GLN   B 1 150 ? -30.59900 -4.71100  33.94800 1.000 26.42701 ?  130 GLN   B CA    1 
ATOM   2889 C C     . GLN   B 1 150 ? -29.77100 -3.96000  32.91500 1.000 28.60507 ?  130 GLN   B C     1 
ATOM   2890 O O     . GLN   B 1 150 ? -29.80100 -4.28900  31.72100 1.000 25.04446 ?  130 GLN   B O     1 
ATOM   2891 C CB    . GLN   B 1 150 ? -29.88500 -6.00500  34.35100 1.000 24.56244 ?  130 GLN   B CB    1 
ATOM   2892 C CG    . GLN   B 1 150 ? -28.62300 -5.80500  35.19500 1.000 27.36579 ?  130 GLN   B CG    1 
ATOM   2893 C CD    . GLN   B 1 150 ? -27.38600 -5.44800  34.39500 1.000 28.23541 ?  130 GLN   B CD    1 
ATOM   2894 O OE1   . GLN   B 1 150 ? -27.27900 -5.75300  33.19900 1.000 29.93718 ?  130 GLN   B OE1   1 
ATOM   2895 N NE2   . GLN   B 1 150 ? -26.45200 -4.73800  35.04600 1.000 23.98973 ?  130 GLN   B NE2   1 
ATOM   2896 N N     . GLY   B 1 151 ? -29.03600 -2.94600  33.36300 1.000 20.93538 ?  131 GLY   B N     1 
ATOM   2897 C CA    . GLY   B 1 151 ? -28.20100 -2.19300  32.44300 1.000 20.60657 ?  131 GLY   B CA    1 
ATOM   2898 C C     . GLY   B 1 151 ? -27.46900 -1.11100  33.21300 1.000 22.72076 ?  131 GLY   B C     1 
ATOM   2899 O O     . GLY   B 1 151 ? -27.73500 -0.87500  34.39400 1.000 23.36303 ?  131 GLY   B O     1 
ATOM   2900 N N     . ASP   B 1 152 ? -26.53600 -0.45000  32.52500 1.000 22.00567 ?  132 ASP   B N     1 
ATOM   2901 C CA    . ASP   B 1 152 ? -25.62600 0.50900   33.15600 1.000 21.33529 ?  132 ASP   B CA    1 
ATOM   2902 C C     . ASP   B 1 152 ? -25.82100 1.86500   32.50500 1.000 23.82354 ?  132 ASP   B C     1 
ATOM   2903 O O     . ASP   B 1 152 ? -25.70900 1.99200   31.28000 1.000 25.08324 ?  132 ASP   B O     1 
ATOM   2904 C CB    . ASP   B 1 152 ? -24.16000 0.05900   33.04600 1.000 24.32470 ?  132 ASP   B CB    1 
ATOM   2905 C CG    . ASP   B 1 152 ? -23.21300 0.81900   34.01200 1.000 24.75203 ?  132 ASP   B CG    1 
ATOM   2906 O OD1   . ASP   B 1 152 ? -23.24400 2.06500   34.02300 1.000 25.10423 ?  132 ASP   B OD1   1 
ATOM   2907 O OD2   . ASP   B 1 152 ? -22.39600 0.17700   34.71700 1.000 25.35322 -1 132 ASP   B OD2   1 
ATOM   2908 N N     . ALA   B 1 153 ? -26.12100 2.87100   33.33400 1.000 21.03032 ?  133 ALA   B N     1 
ATOM   2909 C CA    . ALA   B 1 153 ? -26.33900 4.22600   32.86500 1.000 20.95379 ?  133 ALA   B CA    1 
ATOM   2910 C C     . ALA   B 1 153 ? -25.14400 4.78000   32.10200 1.000 24.39559 ?  133 ALA   B C     1 
ATOM   2911 O O     . ALA   B 1 153 ? -25.30800 5.69000   31.27700 1.000 27.78368 ?  133 ALA   B O     1 
ATOM   2912 C CB    . ALA   B 1 153 ? -26.64100 5.14200   34.05900 1.000 21.16983 ?  133 ALA   B CB    1 
ATOM   2913 N N     . CYS   B 1 154 ? -23.95000 4.26400   32.35900 1.000 22.83728 ?  134 CYS   B N     1 
ATOM   2914 C CA    . CYS   B 1 154 ? -22.74600 4.75300   31.70600 1.000 26.80388 ?  134 CYS   B CA    1 
ATOM   2915 C C     . CYS   B 1 154 ? -22.42600 4.02100   30.41200 1.000 29.55254 ?  134 CYS   B C     1 
ATOM   2916 O O     . CYS   B 1 154 ? -21.44100 4.37200   29.75500 1.000 24.34402 ?  134 CYS   B O     1 
ATOM   2917 C CB    . CYS   B 1 154 ? -21.55800 4.63200   32.65400 1.000 25.28003 ?  134 CYS   B CB    1 
ATOM   2918 S SG    . CYS   B 1 154 ? -21.75700 5.73700   34.08200 1.000 29.90932 ?  134 CYS   B SG    1 
ATOM   2919 N N     . ASN   B 1 155 ? -23.20600 3.00400   30.05200 1.000 24.38846 ?  135 ASN   B N     1 
ATOM   2920 C CA    . ASN   B 1 155 ? -22.96400 2.23500   28.82900 1.000 23.78103 ?  135 ASN   B CA    1 
ATOM   2921 C C     . ASN   B 1 155 ? -24.26600 1.59000   28.36700 1.000 27.04699 ?  135 ASN   B C     1 
ATOM   2922 O O     . ASN   B 1 155 ? -24.37300 0.36100   28.30400 1.000 26.60084 ?  135 ASN   B O     1 
ATOM   2923 C CB    . ASN   B 1 155 ? -21.88200 1.16900   29.07200 1.000 26.91041 ?  135 ASN   B CB    1 
ATOM   2924 C CG    . ASN   B 1 155 ? -21.34100 0.57100   27.77600 1.000 28.67000 ?  135 ASN   B CG    1 
ATOM   2925 O OD1   . ASN   B 1 155 ? -21.08800 1.28300   26.81800 1.000 31.96335 ?  135 ASN   B OD1   1 
ATOM   2926 N ND2   . ASN   B 1 155 ? -21.17200 -0.75000  27.75200 1.000 31.40488 ?  135 ASN   B ND2   1 
ATOM   2927 N N     . LEU   B 1 156 ? -25.27100 2.40700   28.06900 1.000 25.10208 ?  136 LEU   B N     1 
ATOM   2928 C CA    . LEU   B 1 156 ? -26.58400 1.87700   27.72400 1.000 27.61376 ?  136 LEU   B CA    1 
ATOM   2929 C C     . LEU   B 1 156 ? -26.55700 1.29100   26.31300 1.000 28.91617 ?  136 LEU   B C     1 
ATOM   2930 O O     . LEU   B 1 156 ? -25.94600 1.86500   25.40600 1.000 28.51441 ?  136 LEU   B O     1 
ATOM   2931 C CB    . LEU   B 1 156 ? -27.62500 2.98600   27.79000 1.000 28.69951 ?  136 LEU   B CB    1 
ATOM   2932 C CG    . LEU   B 1 156 ? -28.09100 3.43500   29.18100 1.000 28.74809 ?  136 LEU   B CG    1 
ATOM   2933 C CD1   . LEU   B 1 156 ? -29.00800 4.66100   29.05100 1.000 27.25683 ?  136 LEU   B CD1   1 
ATOM   2934 C CD2   . LEU   B 1 156 ? -28.79300 2.32800   29.92900 1.000 27.46052 ?  136 LEU   B CD2   1 
ATOM   2935 N N     . THR   B 1 157 ? -27.25700 0.17200   26.11100 1.000 30.39085 ?  137 THR   B N     1 
ATOM   2936 C CA    . THR   B 1 157 ? -27.30300 -0.39500  24.76100 1.000 30.68475 ?  137 THR   B CA    1 
ATOM   2937 C C     . THR   B 1 157 ? -28.05900 0.55600   23.83000 1.000 41.49993 ?  137 THR   B C     1 
ATOM   2938 O O     . THR   B 1 157 ? -28.84100 1.39300   24.29000 1.000 34.04824 ?  137 THR   B O     1 
ATOM   2939 C CB    . THR   B 1 157 ? -27.93400 -1.79000  24.76500 1.000 31.97109 ?  137 THR   B CB    1 
ATOM   2940 O OG1   . THR   B 1 157 ? -29.30700 -1.71400  25.15700 1.000 36.91970 ?  137 THR   B OG1   1 
ATOM   2941 C CG2   . THR   B 1 157 ? -27.17500 -2.70000  25.70500 1.000 35.09060 ?  137 THR   B CG2   1 
ATOM   2942 N N     . PRO   B 1 158 ? -27.81400 0.46600   22.50900 1.000 39.32058 ?  138 PRO   B N     1 
ATOM   2943 C CA    . PRO   B 1 158 ? -28.31600 1.50800   21.59500 1.000 33.72907 ?  138 PRO   B CA    1 
ATOM   2944 C C     . PRO   B 1 158 ? -29.82600 1.58100   21.49200 1.000 36.28225 ?  138 PRO   B C     1 
ATOM   2945 O O     . PRO   B 1 158 ? -30.34400 2.64500   21.12400 1.000 43.20742 ?  138 PRO   B O     1 
ATOM   2946 C CB    . PRO   B 1 158 ? -27.69500 1.13700   20.24000 1.000 39.65754 ?  138 PRO   B CB    1 
ATOM   2947 C CG    . PRO   B 1 158 ? -26.69300 0.10000   20.50800 1.000 38.94284 ?  138 PRO   B CG    1 
ATOM   2948 C CD    . PRO   B 1 158 ? -26.98300 -0.53300  21.81400 1.000 37.93834 ?  138 PRO   B CD    1 
ATOM   2949 N N     . GLN   B 1 159 ? -30.55200 0.50600   21.80700 1.000 30.28672 ?  139 GLN   B N     1 
ATOM   2950 C CA    . GLN   B 1 159 ? -32.00500 0.52500   21.66400 1.000 37.40176 ?  139 GLN   B CA    1 
ATOM   2951 C C     . GLN   B 1 159 ? -32.67900 1.45200   22.66700 1.000 39.23758 ?  139 GLN   B C     1 
ATOM   2952 O O     . GLN   B 1 159 ? -33.86300 1.77500   22.50500 1.000 34.30641 ?  139 GLN   B O     1 
ATOM   2953 C CB    . GLN   B 1 159 ? -32.56900 -0.88500  21.82000 1.000 30.41239 ?  139 GLN   B CB    1 
ATOM   2954 N N     . PHE   B 1 160 ? -31.96000 1.88000   23.70200 1.000 32.93671 ?  140 PHE   B N     1 
ATOM   2955 C CA    . PHE   B 1 160 ? -32.53700 2.73000   24.74300 1.000 24.94829 ?  140 PHE   B CA    1 
ATOM   2956 C C     . PHE   B 1 160 ? -32.39500 4.17400   24.27600 1.000 33.03417 ?  140 PHE   B C     1 
ATOM   2957 O O     . PHE   B 1 160 ? -31.46000 4.89100   24.62700 1.000 28.56995 ?  140 PHE   B O     1 
ATOM   2958 C CB    . PHE   B 1 160 ? -31.85600 2.43600   26.08100 1.000 26.41434 ?  140 PHE   B CB    1 
ATOM   2959 C CG    . PHE   B 1 160 ? -32.33200 1.14400   26.69800 1.000 29.73688 ?  140 PHE   B CG    1 
ATOM   2960 C CD1   . PHE   B 1 160 ? -33.45900 1.11400   27.48700 1.000 32.61452 ?  140 PHE   B CD1   1 
ATOM   2961 C CD2   . PHE   B 1 160 ? -31.68200 -0.04800  26.43500 1.000 47.35362 ?  140 PHE   B CD2   1 
ATOM   2962 C CE1   . PHE   B 1 160 ? -33.91700 -0.07100  28.02900 1.000 33.57440 ?  140 PHE   B CE1   1 
ATOM   2963 C CE2   . PHE   B 1 160 ? -32.14700 -1.24400  26.97500 1.000 45.12630 ?  140 PHE   B CE2   1 
ATOM   2964 C CZ    . PHE   B 1 160 ? -33.26300 -1.24200  27.77400 1.000 37.47162 ?  140 PHE   B CZ    1 
ATOM   2965 N N     . LYS   B 1 161 ? -33.34100 4.59300   23.43200 1.000 28.33449 ?  141 LYS   B N     1 
ATOM   2966 C CA    . LYS   B 1 161 ? -33.23500 5.86700   22.74700 1.000 23.05132 ?  141 LYS   B CA    1 
ATOM   2967 C C     . LYS   B 1 161 ? -34.62600 6.40900   22.45500 1.000 25.14291 ?  141 LYS   B C     1 
ATOM   2968 O O     . LYS   B 1 161 ? -35.64500 5.79600   22.78700 1.000 30.64208 ?  141 LYS   B O     1 
ATOM   2969 C CB    . LYS   B 1 161 ? -32.43300 5.73000   21.44500 1.000 42.08329 ?  141 LYS   B CB    1 
ATOM   2970 C CG    . LYS   B 1 161 ? -32.98800 4.68800   20.47300 1.000 33.93313 ?  141 LYS   B CG    1 
ATOM   2971 C CD    . LYS   B 1 161 ? -32.44700 4.96700   19.07400 1.000 42.77250 ?  141 LYS   B CD    1 
ATOM   2972 C CE    . LYS   B 1 161 ? -32.81700 3.87600   18.09300 1.000 44.32635 ?  141 LYS   B CE    1 
ATOM   2973 N N     . GLU   B 1 162 ? -34.65300 7.58700   21.83400 1.000 28.05684 ?  142 GLU   B N     1 
ATOM   2974 C CA    . GLU   B 1 162 ? -35.89400 8.22400   21.39600 1.000 31.79398 ?  142 GLU   B CA    1 
ATOM   2975 C C     . GLU   B 1 162 ? -36.87000 8.41300   22.55400 1.000 30.70666 ?  142 GLU   B C     1 
ATOM   2976 O O     . GLU   B 1 162 ? -38.07000 8.16700   22.43400 1.000 28.79845 ?  142 GLU   B O     1 
ATOM   2977 C CB    . GLU   B 1 162 ? -36.52100 7.43000   20.24000 1.000 34.45270 ?  142 GLU   B CB    1 
ATOM   2978 C CG    . GLU   B 1 162 ? -35.60000 7.43000   19.01800 1.000 36.18230 ?  142 GLU   B CG    1 
ATOM   2979 C CD    . GLU   B 1 162 ? -36.26300 6.87000   17.76700 1.000 48.44000 ?  142 GLU   B CD    1 
ATOM   2980 O OE1   . GLU   B 1 162 ? -37.17000 6.02400   17.89700 1.000 59.08050 ?  142 GLU   B OE1   1 
ATOM   2981 O OE2   . GLU   B 1 162 ? -35.87400 7.27900   16.65600 1.000 68.63259 -1 142 GLU   B OE2   1 
ATOM   2982 N N     . TYR   B 1 163 ? -36.35000 8.87700   23.68900 1.000 28.96834 ?  143 TYR   B N     1 
ATOM   2983 C CA    . TYR   B 1 163 ? -37.18600 9.16000   24.84900 1.000 25.63537 ?  143 TYR   B CA    1 
ATOM   2984 C C     . TYR   B 1 163 ? -37.68900 10.59100  24.84700 1.000 28.97816 ?  143 TYR   B C     1 
ATOM   2985 O O     . TYR   B 1 163 ? -36.96200 11.52600  24.49600 1.000 28.79103 ?  143 TYR   B O     1 
ATOM   2986 C CB    . TYR   B 1 163 ? -36.40700 8.90400   26.14000 1.000 26.16511 ?  143 TYR   B CB    1 
ATOM   2987 C CG    . TYR   B 1 163 ? -36.13500 7.44600   26.32200 1.000 24.72775 ?  143 TYR   B CG    1 
ATOM   2988 C CD1   . TYR   B 1 163 ? -37.16400 6.57200   26.63700 1.000 25.17056 ?  143 TYR   B CD1   1 
ATOM   2989 C CD2   . TYR   B 1 163 ? -34.85100 6.93400   26.17400 1.000 27.56239 ?  143 TYR   B CD2   1 
ATOM   2990 C CE1   . TYR   B 1 163 ? -36.91500 5.21900   26.81000 1.000 25.01391 ?  143 TYR   B CE1   1 
ATOM   2991 C CE2   . TYR   B 1 163 ? -34.59800 5.59300   26.34000 1.000 24.59507 ?  143 TYR   B CE2   1 
ATOM   2992 C CZ    . TYR   B 1 163 ? -35.62300 4.74200   26.65100 1.000 24.06552 ?  143 TYR   B CZ    1 
ATOM   2993 O OH    . TYR   B 1 163 ? -35.35700 3.39800   26.81600 1.000 26.25892 ?  143 TYR   B OH    1 
ATOM   2994 N N     . ASP   B 1 164 ? -38.94400 10.75000  25.25600 1.000 25.54945 ?  144 ASP   B N     1 
ATOM   2995 C CA    . ASP   B 1 164 ? -39.46700 12.06800  25.56600 1.000 26.37460 ?  144 ASP   B CA    1 
ATOM   2996 C C     . ASP   B 1 164 ? -38.94100 12.54800  26.90400 1.000 30.04865 ?  144 ASP   B C     1 
ATOM   2997 O O     . ASP   B 1 164 ? -38.78100 13.75300  27.10700 1.000 26.18409 ?  144 ASP   B O     1 
ATOM   2998 C CB    . ASP   B 1 164 ? -40.99100 12.01900  25.59400 1.000 26.66208 ?  144 ASP   B CB    1 
ATOM   2999 C CG    . ASP   B 1 164 ? -41.56500 11.57600  24.26300 1.000 34.99753 ?  144 ASP   B CG    1 
ATOM   3000 O OD1   . ASP   B 1 164 ? -41.28000 12.24400  23.23800 1.000 38.15948 ?  144 ASP   B OD1   1 
ATOM   3001 O OD2   . ASP   B 1 164 ? -42.26900 10.54800  24.24300 1.000 35.34348 -1 144 ASP   B OD2   1 
ATOM   3002 N N     . LEU   B 1 165 ? -38.63500 11.60800  27.80400 1.000 24.98133 ?  145 LEU   B N     1 
ATOM   3003 C CA    . LEU   B 1 165 ? -38.17800 11.91800  29.15500 1.000 23.20715 ?  145 LEU   B CA    1 
ATOM   3004 C C     . LEU   B 1 165 ? -37.17400 10.86200  29.58300 1.000 22.56721 ?  145 LEU   B C     1 
ATOM   3005 O O     . LEU   B 1 165 ? -37.42600 9.66300   29.43000 1.000 21.59557 ?  145 LEU   B O     1 
ATOM   3006 C CB    . LEU   B 1 165 ? -39.34300 11.93400  30.14600 1.000 23.33109 ?  145 LEU   B CB    1 
ATOM   3007 C CG    . LEU   B 1 165 ? -38.96400 11.87900  31.63600 1.000 23.99361 ?  145 LEU   B CG    1 
ATOM   3008 C CD1   . LEU   B 1 165 ? -38.32500 13.20900  32.07100 1.000 23.08777 ?  145 LEU   B CD1   1 
ATOM   3009 C CD2   . LEU   B 1 165 ? -40.16600 11.52500  32.52900 1.000 23.48906 ?  145 LEU   B CD2   1 
ATOM   3010 N N     . ILE   B 1 166 ? -36.05200 11.29600  30.14100 1.000 22.35368 ?  146 ILE   B N     1 
ATOM   3011 C CA    . ILE   B 1 166 ? -35.18400 10.38600  30.88900 1.000 20.67316 ?  146 ILE   B CA    1 
ATOM   3012 C C     . ILE   B 1 166 ? -35.11900 10.93900  32.30200 1.000 23.39254 ?  146 ILE   B C     1 
ATOM   3013 O O     . ILE   B 1 166 ? -34.73000 12.09300  32.49600 1.000 22.25955 ?  146 ILE   B O     1 
ATOM   3014 C CB    . ILE   B 1 166 ? -33.78500 10.28200  30.27000 1.000 27.28451 ?  146 ILE   B CB    1 
ATOM   3015 C CG1   . ILE   B 1 166 ? -33.88400 9.65800   28.87200 1.000 23.01904 ?  146 ILE   B CG1   1 
ATOM   3016 C CG2   . ILE   B 1 166 ? -32.86900 9.43600   31.18900 1.000 20.78820 ?  146 ILE   B CG2   1 
ATOM   3017 C CD1   . ILE   B 1 166 ? -32.56200 9.35800   28.24600 1.000 23.03013 ?  146 ILE   B CD1   1 
ATOM   3018 N N     . MET   B 1 167 ? -35.52300 10.13700  33.28600 1.000 22.28412 ?  147 MET   B N     1 
ATOM   3019 C CA    . MET   B 1 167 ? -35.51400 10.58100  34.66800 1.000 21.36866 ?  147 MET   B CA    1 
ATOM   3020 C C     . MET   B 1 167 ? -34.50100 9.73800   35.41800 1.000 25.56251 ?  147 MET   B C     1 
ATOM   3021 O O     . MET   B 1 167 ? -34.55700 8.51200   35.35600 1.000 25.06907 ?  147 MET   B O     1 
ATOM   3022 C CB    . MET   B 1 167 ? -36.89500 10.46000  35.30900 1.000 23.52883 ?  147 MET   B CB    1 
ATOM   3023 C CG    . MET   B 1 167 ? -36.95200 11.06600  36.71000 1.000 26.13620 ?  147 MET   B CG    1 
ATOM   3024 S SD    . MET   B 1 167 ? -38.64000 11.11800  37.37900 1.000 33.81080 ?  147 MET   B SD    1 
ATOM   3025 C CE    . MET   B 1 167 ? -38.85000 9.44600   38.00000 1.000 26.71769 ?  147 MET   B CE    1 
ATOM   3026 N N     . ALA   B 1 168 ? -33.56700 10.38600  36.10200 1.000 20.98872 ?  148 ALA   B N     1 
ATOM   3027 C CA    . ALA   B 1 168 ? -32.53500 9.66100   36.84800 1.000 20.60736 ?  148 ALA   B CA    1 
ATOM   3028 C C     . ALA   B 1 168 ? -32.50800 10.24700  38.25800 1.000 18.83845 ?  148 ALA   B C     1 
ATOM   3029 O O     . ALA   B 1 168 ? -31.88200 11.28900  38.48200 1.000 21.40673 ?  148 ALA   B O     1 
ATOM   3030 C CB    . ALA   B 1 168 ? -31.18200 9.78400   36.15600 1.000 23.64460 ?  148 ALA   B CB    1 
ATOM   3031 N N     . THR   B 1 169 ? -33.19800 9.61200   39.20000 1.000 21.56170 ?  149 THR   B N     1 
ATOM   3032 C CA    . THR   B 1 169 ? -33.33800 10.19800  40.53000 1.000 24.90114 ?  149 THR   B CA    1 
ATOM   3033 C C     . THR   B 1 169 ? -32.31200 9.58400   41.47200 1.000 21.60921 ?  149 THR   B C     1 
ATOM   3034 O O     . THR   B 1 169 ? -32.21200 8.35300   41.57400 1.000 21.38944 ?  149 THR   B O     1 
ATOM   3035 C CB    . THR   B 1 169 ? -34.76500 10.06000  41.08900 1.000 25.88226 ?  149 THR   B CB    1 
ATOM   3036 O OG1   . THR   B 1 169 ? -35.11700 8.69000   41.29500 1.000 29.28031 ?  149 THR   B OG1   1 
ATOM   3037 C CG2   . THR   B 1 169 ? -35.78200 10.70600  40.11700 1.000 24.34313 ?  149 THR   B CG2   1 
ATOM   3038 N N     . ASN   B 1 170 ? -31.54800 10.45900  42.14200 1.000 18.48225 ?  150 ASN   B N     1 
ATOM   3039 C CA    . ASN   B 1 170 ? -30.55400 10.07700  43.14900 1.000 19.56437 ?  150 ASN   B CA    1 
ATOM   3040 C C     . ASN   B 1 170 ? -29.55500 9.06500   42.59400 1.000 20.64338 ?  150 ASN   B C     1 
ATOM   3041 O O     . ASN   B 1 170 ? -29.17800 8.09000   43.25600 1.000 22.64371 ?  150 ASN   B O     1 
ATOM   3042 C CB    . ASN   B 1 170 ? -31.23600 9.56700   44.41200 1.000 19.46188 ?  150 ASN   B CB    1 
ATOM   3043 C CG    . ASN   B 1 170 ? -32.03700 10.67200  45.12800 1.000 23.32102 ?  150 ASN   B CG    1 
ATOM   3044 O OD1   . ASN   B 1 170 ? -31.99300 11.86500  44.73600 1.000 20.22538 ?  150 ASN   B OD1   1 
ATOM   3045 N ND2   . ASN   B 1 170 ? -32.75600 10.28400  46.17800 1.000 21.19861 ?  150 ASN   B ND2   1 
ATOM   3046 N N     . LEU   B 1 171 ? -29.13400 9.30100   41.35600 1.000 18.38104 ?  151 LEU   B N     1 
ATOM   3047 C CA    . LEU   B 1 171 ? -28.18900 8.44200   40.64900 1.000 22.29269 ?  151 LEU   B CA    1 
ATOM   3048 C C     . LEU   B 1 171 ? -26.79600 9.05200   40.52100 1.000 19.74684 ?  151 LEU   B C     1 
ATOM   3049 O O     . LEU   B 1 171 ? -25.80400 8.35300   40.75300 1.000 21.86101 ?  151 LEU   B O     1 
ATOM   3050 C CB    . LEU   B 1 171 ? -28.72000 8.11000   39.24500 1.000 19.41516 ?  151 LEU   B CB    1 
ATOM   3051 C CG    . LEU   B 1 171 ? -27.78200 7.23300   38.40300 1.000 21.78081 ?  151 LEU   B CG    1 
ATOM   3052 C CD1   . LEU   B 1 171 ? -27.60700 5.88600   39.09800 1.000 24.67711 ?  151 LEU   B CD1   1 
ATOM   3053 C CD2   . LEU   B 1 171 ? -28.34300 7.05100   36.98600 1.000 23.15567 ?  151 LEU   B CD2   1 
ATOM   3054 N N     . ILE   B 1 172 ? -26.68300 10.34800  40.20800 1.000 19.01411 ?  152 ILE   B N     1 
ATOM   3055 C CA    . ILE   B 1 172 ? -25.37200 10.87100  39.82600 1.000 20.04778 ?  152 ILE   B CA    1 
ATOM   3056 C C     . ILE   B 1 172 ? -24.35600 10.73800  40.95900 1.000 21.18838 ?  152 ILE   B C     1 
ATOM   3057 O O     . ILE   B 1 172 ? -23.18100 10.46100  40.69500 1.000 20.78338 ?  152 ILE   B O     1 
ATOM   3058 C CB    . ILE   B 1 172 ? -25.47000 12.32100  39.29600 1.000 19.32032 ?  152 ILE   B CB    1 
ATOM   3059 C CG1   . ILE   B 1 172 ? -26.04000 13.28300  40.36200 1.000 18.96876 ?  152 ILE   B CG1   1 
ATOM   3060 C CG2   . ILE   B 1 172 ? -26.25700 12.36700  37.96600 1.000 23.90201 ?  152 ILE   B CG2   1 
ATOM   3061 C CD1   . ILE   B 1 172 ? -25.88500 14.76700  39.98400 1.000 23.14718 ?  152 ILE   B CD1   1 
ATOM   3062 N N     . ASP   B 1 173 ? -24.77400 10.87800  42.23100 1.000 18.27649 ?  153 ASP   B N     1 
ATOM   3063 C CA    . ASP   B 1 173 ? -23.77600 10.76200  43.29200 1.000 23.67421 ?  153 ASP   B CA    1 
ATOM   3064 C C     . ASP   B 1 173 ? -23.59300 9.31100   43.75000 1.000 23.65665 ?  153 ASP   B C     1 
ATOM   3065 O O     . ASP   B 1 173 ? -22.96100 9.06200   44.78000 1.000 24.08933 ?  153 ASP   B O     1 
ATOM   3066 C CB    . ASP   B 1 173 ? -24.07700 11.69600  44.47900 1.000 27.12928 ?  153 ASP   B CB    1 
ATOM   3067 C CG    . ASP   B 1 173 ? -25.52800 11.70300  44.91800 1.000 29.08310 ?  153 ASP   B CG    1 
ATOM   3068 O OD1   . ASP   B 1 173 ? -26.48300 11.48100  44.12100 1.000 24.54521 ?  153 ASP   B OD1   1 
ATOM   3069 O OD2   . ASP   B 1 173 ? -25.70300 12.06500  46.10700 1.000 39.12380 -1 153 ASP   B OD2   1 
ATOM   3070 N N     . ARG   B 1 174 ? -24.10200 8.35800   42.97700 1.000 18.47789 ?  154 ARG   B N     1 
ATOM   3071 C CA    . ARG   B 1 174 ? -23.74400 6.94700   43.11000 1.000 20.17964 ?  154 ARG   B CA    1 
ATOM   3072 C C     . ARG   B 1 174 ? -22.82000 6.46100   42.00200 1.000 24.10424 ?  154 ARG   B C     1 
ATOM   3073 O O     . ARG   B 1 174 ? -22.38700 5.29400   42.04200 1.000 26.53815 ?  154 ARG   B O     1 
ATOM   3074 C CB    . ARG   B 1 174 ? -25.01200 6.08400   43.12300 1.000 21.15559 ?  154 ARG   B CB    1 
ATOM   3075 C CG    . ARG   B 1 174 ? -25.94200 6.50000   44.25000 1.000 30.47993 ?  154 ARG   B CG    1 
ATOM   3076 C CD    . ARG   B 1 174 ? -25.54800 5.87100   45.55600 1.000 34.49512 ?  154 ARG   B CD    1 
ATOM   3077 N NE    . ARG   B 1 174 ? -26.67400 5.88400   46.48300 1.000 46.53447 ?  154 ARG   B NE    1 
ATOM   3078 C CZ    . ARG   B 1 174 ? -26.62800 5.42700   47.72700 1.000 59.62918 ?  154 ARG   B CZ    1 
ATOM   3079 N NH1   . ARG   B 1 174 ? -25.54200 4.84000   48.20500 1.000 52.54666 ?  154 ARG   B NH1   1 
ATOM   3080 N NH2   . ARG   B 1 174 ? -27.69700 5.56400   48.51100 1.000 49.25785 ?  154 ARG   B NH2   1 
ATOM   3081 N N     . LEU   B 1 175 ? -22.52100 7.30000   41.01000 1.000 20.09951 ?  155 LEU   B N     1 
ATOM   3082 C CA    . LEU   B 1 175 ? -21.70100 6.89800   39.86100 1.000 21.09907 ?  155 LEU   B CA    1 
ATOM   3083 C C     . LEU   B 1 175 ? -20.23200 7.22800   40.10400 1.000 24.21087 ?  155 LEU   B C     1 
ATOM   3084 O O     . LEU   B 1 175 ? -19.90500 8.26100   40.69500 1.000 22.18659 ?  155 LEU   B O     1 
ATOM   3085 C CB    . LEU   B 1 175 ? -22.17000 7.61500   38.59200 1.000 22.14760 ?  155 LEU   B CB    1 
ATOM   3086 C CG    . LEU   B 1 175 ? -23.61900 7.33900   38.22200 1.000 21.49297 ?  155 LEU   B CG    1 
ATOM   3087 C CD1   . LEU   B 1 175 ? -23.99900 8.15100   36.99800 1.000 20.98081 ?  155 LEU   B CD1   1 
ATOM   3088 C CD2   . LEU   B 1 175 ? -23.83800 5.77200   38.03200 1.000 21.99426 ?  155 LEU   B CD2   1 
ATOM   3089 N N     . TYR   B 1 176 ? -19.33700 6.34600   39.63600 1.000 19.62058 ?  156 TYR   B N     1 
ATOM   3090 C CA    . TYR   B 1 176 ? -17.90900 6.61200   39.80400 1.000 18.08376 ?  156 TYR   B CA    1 
ATOM   3091 C C     . TYR   B 1 176 ? -17.46600 7.78500   38.94000 1.000 23.64101 ?  156 TYR   B C     1 
ATOM   3092 O O     . TYR   B 1 176 ? -16.63500 8.60400   39.36000 1.000 23.06507 ?  156 TYR   B O     1 
ATOM   3093 C CB    . TYR   B 1 176 ? -17.08400 5.37800   39.43700 1.000 20.28961 ?  156 TYR   B CB    1 
ATOM   3094 C CG    . TYR   B 1 176 ? -15.60100 5.60700   39.61600 1.000 21.07601 ?  156 TYR   B CG    1 
ATOM   3095 C CD1   . TYR   B 1 176 ? -15.02500 5.68200   40.89700 1.000 22.99795 ?  156 TYR   B CD1   1 
ATOM   3096 C CD2   . TYR   B 1 176 ? -14.77900 5.81400   38.51500 1.000 23.17339 ?  156 TYR   B CD2   1 
ATOM   3097 C CE1   . TYR   B 1 176 ? -13.66500 5.90400   41.06100 1.000 23.58332 ?  156 TYR   B CE1   1 
ATOM   3098 C CE2   . TYR   B 1 176 ? -13.42100 6.04400   38.67000 1.000 23.23378 ?  156 TYR   B CE2   1 
ATOM   3099 C CZ    . TYR   B 1 176 ? -12.87300 6.07900   39.93500 1.000 23.79531 ?  156 TYR   B CZ    1 
ATOM   3100 O OH    . TYR   B 1 176 ? -11.52100 6.31100   40.04500 1.000 30.48286 ?  156 TYR   B OH    1 
ATOM   3101 N N     . GLU   B 1 177 ? -18.00700 7.87800   37.73000 1.000 21.59044 ?  157 GLU   B N     1 
ATOM   3102 C CA    . GLU   B 1 177 ? -17.65500 8.93400   36.78100 1.000 20.14857 ?  157 GLU   B CA    1 
ATOM   3103 C C     . GLU   B 1 177 ? -18.93800 9.47200   36.16400 1.000 21.24754 ?  157 GLU   B C     1 
ATOM   3104 O O     . GLU   B 1 177 ? -19.27500 9.15100   35.02300 1.000 20.51216 ?  157 GLU   B O     1 
ATOM   3105 C CB    . GLU   B 1 177 ? -16.70900 8.39600   35.69500 1.000 23.70939 ?  157 GLU   B CB    1 
ATOM   3106 C CG    . GLU   B 1 177 ? -16.13700 9.48500   34.77500 1.000 24.48586 ?  157 GLU   B CG    1 
ATOM   3107 C CD    . GLU   B 1 177 ? -15.15700 8.93600   33.75100 1.000 32.10511 ?  157 GLU   B CD    1 
ATOM   3108 O OE1   . GLU   B 1 177 ? -14.79600 7.73700   33.83800 1.000 28.48514 ?  157 GLU   B OE1   1 
ATOM   3109 O OE2   . GLU   B 1 177 ? -14.76500 9.70300   32.85500 1.000 29.28248 -1 157 GLU   B OE2   1 
ATOM   3110 N N     . PRO   B 1 178 ? -19.68700 10.30200  36.90200 1.000 25.67198 ?  158 PRO   B N     1 
ATOM   3111 C CA    . PRO   B 1 178 ? -21.03700 10.68100  36.43100 1.000 24.90756 ?  158 PRO   B CA    1 
ATOM   3112 C C     . PRO   B 1 178 ? -21.04000 11.40900  35.09900 1.000 21.67195 ?  158 PRO   B C     1 
ATOM   3113 O O     . PRO   B 1 178 ? -22.01700 11.32100  34.33900 1.000 22.45451 ?  158 PRO   B O     1 
ATOM   3114 C CB    . PRO   B 1 178 ? -21.59500 11.55600  37.57800 1.000 23.94795 ?  158 PRO   B CB    1 
ATOM   3115 C CG    . PRO   B 1 178 ? -20.38200 11.95900  38.42200 1.000 22.70082 ?  158 PRO   B CG    1 
ATOM   3116 C CD    . PRO   B 1 178 ? -19.38300 10.80800  38.25700 1.000 21.39757 ?  158 PRO   B CD    1 
ATOM   3117 N N     . ARG   B 1 179 ? -19.95400 12.09900  34.76700 1.000 23.75273 ?  159 ARG   B N     1 
ATOM   3118 C CA    . ARG   B 1 179 ? -19.90600 12.79900  33.49300 1.000 23.17162 ?  159 ARG   B CA    1 
ATOM   3119 C C     . ARG   B 1 179 ? -20.00900 11.82800  32.32000 1.000 26.14815 ?  159 ARG   B C     1 
ATOM   3120 O O     . ARG   B 1 179 ? -20.50900 12.18600  31.25100 1.000 28.15262 ?  159 ARG   B O     1 
ATOM   3121 C CB    . ARG   B 1 179 ? -18.62700 13.63200  33.43000 1.000 29.12869 ?  159 ARG   B CB    1 
ATOM   3122 C CG    . ARG   B 1 179 ? -18.56400 14.59900  32.28600 1.000 40.59248 ?  159 ARG   B CG    1 
ATOM   3123 C CD    . ARG   B 1 179 ? -17.15700 15.17800  32.15200 1.000 42.39620 ?  159 ARG   B CD    1 
ATOM   3124 N NE    . ARG   B 1 179 ? -17.03300 16.46500  32.82000 1.000 55.40005 ?  159 ARG   B NE    1 
ATOM   3125 C CZ    . ARG   B 1 179 ? -17.17800 17.63300  32.20400 1.000 55.24322 ?  159 ARG   B CZ    1 
ATOM   3126 N NH1   . ARG   B 1 179 ? -17.51400 17.70000  30.92500 1.000 52.47709 ?  159 ARG   B NH1   1 
ATOM   3127 N NH2   . ARG   B 1 179 ? -17.00000 18.76000  32.89200 1.000 53.94120 ?  159 ARG   B NH2   1 
ATOM   3128 N N     . LEU   B 1 180 ? -19.59600 10.57500  32.52100 1.000 24.87617 ?  160 LEU   B N     1 
ATOM   3129 C CA    . LEU   B 1 180 ? -19.72200 9.58200   31.46800 1.000 27.81372 ?  160 LEU   B CA    1 
ATOM   3130 C C     . LEU   B 1 180 ? -21.18300 9.36900   31.08400 1.000 33.78998 ?  160 LEU   B C     1 
ATOM   3131 O O     . LEU   B 1 180 ? -21.50800 9.23600   29.90000 1.000 30.47603 ?  160 LEU   B O     1 
ATOM   3132 C CB    . LEU   B 1 180 ? -19.07100 8.28200   31.95100 1.000 26.90386 ?  160 LEU   B CB    1 
ATOM   3133 C CG    . LEU   B 1 180 ? -18.92100 7.06400   31.07300 1.000 35.78748 ?  160 LEU   B CG    1 
ATOM   3134 C CD1   . LEU   B 1 180 ? -18.27700 7.45800   29.75600 1.000 34.58314 ?  160 LEU   B CD1   1 
ATOM   3135 C CD2   . LEU   B 1 180 ? -18.06800 6.06900   31.86300 1.000 24.21845 ?  160 LEU   B CD2   1 
ATOM   3136 N N     . PHE   B 1 181 ? -22.08700 9.35600   32.07500 1.000 26.47590 ?  161 PHE   B N     1 
ATOM   3137 C CA    . PHE   B 1 181 ? -23.51600 9.27300   31.78100 1.000 21.38452 ?  161 PHE   B CA    1 
ATOM   3138 C C     . PHE   B 1 181 ? -24.01900 10.60400  31.22300 1.000 25.38826 ?  161 PHE   B C     1 
ATOM   3139 O O     . PHE   B 1 181 ? -24.67100 10.65700  30.17100 1.000 28.96802 ?  161 PHE   B O     1 
ATOM   3140 C CB    . PHE   B 1 181 ? -24.24800 8.87200   33.06600 1.000 22.40069 ?  161 PHE   B CB    1 
ATOM   3141 C CG    . PHE   B 1 181 ? -25.66600 9.35300   33.17500 1.000 24.22521 ?  161 PHE   B CG    1 
ATOM   3142 C CD1   . PHE   B 1 181 ? -26.63500 8.93400   32.25600 1.000 25.13633 ?  161 PHE   B CD1   1 
ATOM   3143 C CD2   . PHE   B 1 181 ? -26.05100 10.16600  34.24200 1.000 27.06263 ?  161 PHE   B CD2   1 
ATOM   3144 C CE1   . PHE   B 1 181 ? -27.95700 9.35700   32.38100 1.000 26.43323 ?  161 PHE   B CE1   1 
ATOM   3145 C CE2   . PHE   B 1 181 ? -27.35800 10.57800  34.37500 1.000 25.15360 ?  161 PHE   B CE2   1 
ATOM   3146 C CZ    . PHE   B 1 181 ? -28.31600 10.18700  33.44600 1.000 26.42923 ?  161 PHE   B CZ    1 
ATOM   3147 N N     . LEU   B 1 182 ? -23.68200 11.69400  31.90100 1.000 23.18757 ?  162 LEU   B N     1 
ATOM   3148 C CA    . LEU   B 1 182 ? -24.29000 12.99600  31.61200 1.000 22.74763 ?  162 LEU   B CA    1 
ATOM   3149 C C     . LEU   B 1 182 ? -23.88900 13.54200  30.25100 1.000 29.68812 ?  162 LEU   B C     1 
ATOM   3150 O O     . LEU   B 1 182 ? -24.70500 14.17800  29.57700 1.000 28.02876 ?  162 LEU   B O     1 
ATOM   3151 C CB    . LEU   B 1 182 ? -23.90800 13.98400  32.70600 1.000 22.64633 ?  162 LEU   B CB    1 
ATOM   3152 C CG    . LEU   B 1 182 ? -24.52000 13.70100  34.07900 1.000 28.11820 ?  162 LEU   B CG    1 
ATOM   3153 C CD1   . LEU   B 1 182 ? -23.83900 14.54800  35.17500 1.000 26.75016 ?  162 LEU   B CD1   1 
ATOM   3154 C CD2   . LEU   B 1 182 ? -26.03300 13.94000  34.05900 1.000 27.92596 ?  162 LEU   B CD2   1 
ATOM   3155 N N     . GLU   B 1 183 ? -22.63700 13.35500  29.83900 1.000 27.33500 ?  163 GLU   B N     1 
ATOM   3156 C CA    . GLU   B 1 183 ? -22.20100 14.07000  28.63600 1.000 30.72742 ?  163 GLU   B CA    1 
ATOM   3157 C C     . GLU   B 1 183 ? -22.72700 13.44300  27.35100 1.000 31.81228 ?  163 GLU   B C     1 
ATOM   3158 O O     . GLU   B 1 183 ? -22.70000 14.09300  26.29800 1.000 33.31769 ?  163 GLU   B O     1 
ATOM   3159 C CB    . GLU   B 1 183 ? -20.66800 14.16800  28.62200 1.000 33.26164 ?  163 GLU   B CB    1 
ATOM   3160 C CG    . GLU   B 1 183 ? -19.91800 12.92400  28.20000 1.000 31.50508 ?  163 GLU   B CG    1 
ATOM   3161 C CD    . GLU   B 1 183 ? -18.41000 13.08900  28.38600 1.000 46.75561 ?  163 GLU   B CD    1 
ATOM   3162 O OE1   . GLU   B 1 183 ? -17.96800 14.20800  28.76200 1.000 47.37079 ?  163 GLU   B OE1   1 
ATOM   3163 O OE2   . GLU   B 1 183 ? -17.67500 12.10700  28.14800 1.000 54.24511 -1 163 GLU   B OE2   1 
ATOM   3164 N N     . ASN   B 1 184 ? -23.25100 12.22100  27.42700 1.000 30.73285 ?  164 ASN   B N     1 
ATOM   3165 C CA    . ASN   B 1 184 ? -23.76100 11.50000  26.27200 1.000 37.88986 ?  164 ASN   B CA    1 
ATOM   3166 C C     . ASN   B 1 184 ? -25.27500 11.34200  26.26200 1.000 40.88373 ?  164 ASN   B C     1 
ATOM   3167 O O     . ASN   B 1 184 ? -25.83400 10.99600  25.21400 1.000 38.58577 ?  164 ASN   B O     1 
ATOM   3168 C CB    . ASN   B 1 184 ? -23.11900 10.10600  26.21400 1.000 38.80067 ?  164 ASN   B CB    1 
ATOM   3169 C CG    . ASN   B 1 184 ? -21.61600 10.17200  26.04100 1.000 47.81952 ?  164 ASN   B CG    1 
ATOM   3170 O OD1   . ASN   B 1 184 ? -21.11800 10.58800  24.99200 1.000 40.25130 ?  164 ASN   B OD1   1 
ATOM   3171 N ND2   . ASN   B 1 184 ? -20.88300 9.78500   27.07800 1.000 40.76217 ?  164 ASN   B ND2   1 
ATOM   3172 N N     . ILE   B 1 185 ? -25.95300 11.58800  27.38700 1.000 34.21849 ?  165 ILE   B N     1 
ATOM   3173 C CA    . ILE   B 1 185 ? -27.36600 11.22800  27.51400 1.000 30.61707 ?  165 ILE   B CA    1 
ATOM   3174 C C     . ILE   B 1 185 ? -28.26300 11.98400  26.53400 1.000 27.35747 ?  165 ILE   B C     1 
ATOM   3175 O O     . ILE   B 1 185 ? -29.35900 11.50800  26.20700 1.000 28.00257 ?  165 ILE   B O     1 
ATOM   3176 C CB    . ILE   B 1 185 ? -27.83200 11.44100  28.97600 1.000 30.98640 ?  165 ILE   B CB    1 
ATOM   3177 C CG1   . ILE   B 1 185 ? -29.06700 10.59000  29.28000 1.000 28.79100 ?  165 ILE   B CG1   1 
ATOM   3178 C CG2   . ILE   B 1 185 ? -28.02000 12.91800  29.29900 1.000 28.03683 ?  165 ILE   B CG2   1 
ATOM   3179 C CD1   . ILE   B 1 185 ? -28.90500 9.10900   28.94700 1.000 23.83464 ?  165 ILE   B CD1   1 
ATOM   3180 N N     . HIS   B 1 186 ? -27.83300 13.15100  26.05400 1.000 31.25799 ?  166 HIS   B N     1 
ATOM   3181 C CA    . HIS   B 1 186 ? -28.66100 13.89900  25.10700 1.000 30.48831 ?  166 HIS   B CA    1 
ATOM   3182 C C     . HIS   B 1 186 ? -28.90200 13.11500  23.82000 1.000 27.83954 ?  166 HIS   B C     1 
ATOM   3183 O O     . HIS   B 1 186 ? -29.88300 13.37900  23.12200 1.000 34.72260 ?  166 HIS   B O     1 
ATOM   3184 C CB    . HIS   B 1 186 ? -28.02000 15.24900  24.76100 1.000 30.31117 ?  166 HIS   B CB    1 
ATOM   3185 C CG    . HIS   B 1 186 ? -26.72600 15.12800  24.01300 1.000 37.15655 ?  166 HIS   B CG    1 
ATOM   3186 N ND1   . HIS   B 1 186 ? -25.54300 14.75800  24.61900 1.000 37.23163 ?  166 HIS   B ND1   1 
ATOM   3187 C CD2   . HIS   B 1 186 ? -26.43200 15.32400  22.70300 1.000 39.17716 ?  166 HIS   B CD2   1 
ATOM   3188 C CE1   . HIS   B 1 186 ? -24.57900 14.72000  23.71400 1.000 40.53144 ?  166 HIS   B CE1   1 
ATOM   3189 N NE2   . HIS   B 1 186 ? -25.09200 15.05800  22.54400 1.000 40.72321 ?  166 HIS   B NE2   1 
ATOM   3190 N N     . LYS   B 1 187 ? -28.03800 12.15000  23.51000 1.000 32.97915 ?  167 LYS   B N     1 
ATOM   3191 C CA    . LYS   B 1 187 ? -28.19700 11.34100  22.30700 1.000 34.46925 ?  167 LYS   B CA    1 
ATOM   3192 C C     . LYS   B 1 187 ? -29.41900 10.43300  22.36700 1.000 35.97772 ?  167 LYS   B C     1 
ATOM   3193 O O     . LYS   B 1 187 ? -29.89600 9.99600   21.31400 1.000 34.17135 ?  167 LYS   B O     1 
ATOM   3194 C CB    . LYS   B 1 187 ? -26.93100 10.51000  22.08200 1.000 29.67877 ?  167 LYS   B CB    1 
ATOM   3195 C CG    . LYS   B 1 187 ? -25.69900 11.37000  21.79100 1.000 39.55405 ?  167 LYS   B CG    1 
ATOM   3196 C CD    . LYS   B 1 187 ? -24.46600 10.52100  21.51300 1.000 52.61367 ?  167 LYS   B CD    1 
ATOM   3197 C CE    . LYS   B 1 187 ? -23.17300 11.24800  21.89300 1.000 58.91228 ?  167 LYS   B CE    1 
ATOM   3198 N NZ    . LYS   B 1 187 ? -22.01600 10.30300  22.01200 1.000 53.87823 ?  167 LYS   B NZ    1 
ATOM   3199 N N     . ARG   B 1 188 ? -29.94500 10.15900  23.56400 1.000 28.04713 ?  168 ARG   B N     1 
ATOM   3200 C CA    . ARG   B 1 188 ? -31.05200 9.23300   23.75100 1.000 25.90994 ?  168 ARG   B CA    1 
ATOM   3201 C C     . ARG   B 1 188 ? -32.40000 9.93200   23.93100 1.000 27.05903 ?  168 ARG   B C     1 
ATOM   3202 O O     . ARG   B 1 188 ? -33.41200 9.25600   24.16400 1.000 28.49672 ?  168 ARG   B O     1 
ATOM   3203 C CB    . ARG   B 1 188 ? -30.75800 8.33100   24.96000 1.000 25.53711 ?  168 ARG   B CB    1 
ATOM   3204 C CG    . ARG   B 1 188 ? -29.30200 7.80300   24.98600 1.000 28.25885 ?  168 ARG   B CG    1 
ATOM   3205 C CD    . ARG   B 1 188 ? -29.00700 6.91600   23.79500 1.000 32.56916 ?  168 ARG   B CD    1 
ATOM   3206 N NE    . ARG   B 1 188 ? -27.75000 6.19000   23.96100 1.000 39.73781 ?  168 ARG   B NE    1 
ATOM   3207 C CZ    . ARG   B 1 188 ? -27.65700 4.90400   24.26400 1.000 34.37049 ?  168 ARG   B CZ    1 
ATOM   3208 N NH1   . ARG   B 1 188 ? -28.73200 4.17000   24.49600 1.000 30.68486 ?  168 ARG   B NH1   1 
ATOM   3209 N NH2   . ARG   B 1 188 ? -26.45200 4.34100   24.34100 1.000 40.13406 ?  168 ARG   B NH2   1 
ATOM   3210 N N     . ILE   B 1 189 ? -32.43500 11.25500  23.82800 1.000 25.19557 ?  169 ILE   B N     1 
ATOM   3211 C CA    . ILE   B 1 189 ? -33.62300 12.06000  24.07300 1.000 25.33254 ?  169 ILE   B CA    1 
ATOM   3212 C C     . ILE   B 1 189 ? -33.98900 12.81300  22.80300 1.000 35.52036 ?  169 ILE   B C     1 
ATOM   3213 O O     . ILE   B 1 189 ? -33.11700 13.37300  22.12400 1.000 33.14567 ?  169 ILE   B O     1 
ATOM   3214 C CB    . ILE   B 1 189 ? -33.39700 13.04300  25.24400 1.000 27.22479 ?  169 ILE   B CB    1 
ATOM   3215 C CG1   . ILE   B 1 189 ? -32.78100 12.31300  26.44700 1.000 24.04524 ?  169 ILE   B CG1   1 
ATOM   3216 C CG2   . ILE   B 1 189 ? -34.67600 13.83300  25.59500 1.000 28.60140 ?  169 ILE   B CG2   1 
ATOM   3217 C CD1   . ILE   B 1 189 ? -32.53400 13.25000  27.66100 1.000 25.40976 ?  169 ILE   B CD1   1 
ATOM   3218 N N     . ASN   B 1 190 ? -35.28700 12.83700  22.49900 1.000 30.00692 ?  170 ASN   B N     1 
ATOM   3219 C CA    . ASN   B 1 190 ? -35.79000 13.57300  21.34600 1.000 35.53645 ?  170 ASN   B CA    1 
ATOM   3220 C C     . ASN   B 1 190 ? -35.59500 15.07200  21.56000 1.000 35.13444 ?  170 ASN   B C     1 
ATOM   3221 O O     . ASN   B 1 190 ? -35.55600 15.55800  22.69200 1.000 32.39127 ?  170 ASN   B O     1 
ATOM   3222 C CB    . ASN   B 1 190 ? -37.27700 13.28400  21.12400 1.000 31.96460 ?  170 ASN   B CB    1 
ATOM   3223 C CG    . ASN   B 1 190 ? -37.58400 11.79900  20.92800 1.000 35.18880 ?  170 ASN   B CG    1 
ATOM   3224 O OD1   . ASN   B 1 190 ? -36.83000 11.05500  20.29600 1.000 34.27221 ?  170 ASN   B OD1   1 
ATOM   3225 N ND2   . ASN   B 1 190 ? -38.72300 11.37100  21.45100 1.000 40.38884 ?  170 ASN   B ND2   1 
ATOM   3226 N N     . GLU   B 1 191 ? -35.48200 15.81600  20.46000 1.000 40.22765 ?  171 GLU   B N     1 
ATOM   3227 C CA    . GLU   B 1 191 ? -35.42200 17.27100  20.57700 1.000 28.66664 ?  171 GLU   B CA    1 
ATOM   3228 C C     . GLU   B 1 191 ? -36.69300 17.78300  21.24100 1.000 29.90621 ?  171 GLU   B C     1 
ATOM   3229 O O     . GLU   B 1 191 ? -37.78900 17.26500  21.00500 1.000 33.56929 ?  171 GLU   B O     1 
ATOM   3230 C CB    . GLU   B 1 191 ? -35.23900 17.91500  19.20200 1.000 43.15790 ?  171 GLU   B CB    1 
ATOM   3231 N N     . LYS   B 1 192 ? -36.52900 18.77800  22.11000 1.000 31.82707 ?  172 LYS   B N     1 
ATOM   3232 C CA    . LYS   B 1 192 ? -37.54100 19.30500  23.02000 1.000 34.34353 ?  172 LYS   B CA    1 
ATOM   3233 C C     . LYS   B 1 192 ? -37.97100 18.30500  24.09500 1.000 30.63384 ?  172 LYS   B C     1 
ATOM   3234 O O     . LYS   B 1 192 ? -38.89100 18.62200  24.85900 1.000 31.20381 ?  172 LYS   B O     1 
ATOM   3235 C CB    . LYS   B 1 192 ? -38.79400 19.80500  22.28600 1.000 41.07043 ?  172 LYS   B CB    1 
ATOM   3236 N N     . GLY   B 1 193 ? -37.35600 17.11300  24.17200 1.000 30.47684 ?  173 GLY   B N     1 
ATOM   3237 C CA    . GLY   B 1 193 ? -37.55600 16.20900  25.29700 1.000 25.55121 ?  173 GLY   B CA    1 
ATOM   3238 C C     . GLY   B 1 193 ? -36.78900 16.66800  26.53700 1.000 24.75199 ?  173 GLY   B C     1 
ATOM   3239 O O     . GLY   B 1 193 ? -36.12000 17.70300  26.54200 1.000 27.99019 ?  173 GLY   B O     1 
ATOM   3240 N N     . TYR   B 1 194 ? -36.89100 15.87200  27.61900 1.000 24.68253 ?  174 TYR   B N     1 
ATOM   3241 C CA    . TYR   B 1 194 ? -36.41100 16.31400  28.93400 1.000 21.72585 ?  174 TYR   B CA    1 
ATOM   3242 C C     . TYR   B 1 194 ? -35.48800 15.28900  29.57200 1.000 24.77749 ?  174 TYR   B C     1 
ATOM   3243 O O     . TYR   B 1 194 ? -35.71600 14.08300  29.46500 1.000 21.97568 ?  174 TYR   B O     1 
ATOM   3244 C CB    . TYR   B 1 194 ? -37.56200 16.58300  29.91000 1.000 20.74757 ?  174 TYR   B CB    1 
ATOM   3245 C CG    . TYR   B 1 194 ? -38.32900 17.85500  29.57900 1.000 23.94804 ?  174 TYR   B CG    1 
ATOM   3246 C CD1   . TYR   B 1 194 ? -39.29900 17.87000  28.57800 1.000 31.25583 ?  174 TYR   B CD1   1 
ATOM   3247 C CD2   . TYR   B 1 194 ? -38.05800 19.03600  30.24600 1.000 27.95010 ?  174 TYR   B CD2   1 
ATOM   3248 C CE1   . TYR   B 1 194 ? -39.99400 19.05900  28.27100 1.000 31.04814 ?  174 TYR   B CE1   1 
ATOM   3249 C CE2   . TYR   B 1 194 ? -38.74100 20.20900  29.94900 1.000 33.52304 ?  174 TYR   B CE2   1 
ATOM   3250 C CZ    . TYR   B 1 194 ? -39.70400 20.21100  28.96700 1.000 34.47720 ?  174 TYR   B CZ    1 
ATOM   3251 O OH    . TYR   B 1 194 ? -40.37800 21.38800  28.69700 1.000 44.00796 ?  174 TYR   B OH    1 
ATOM   3252 N N     . LEU   B 1 195 ? -34.46500 15.79500  30.25000 1.000 22.57143 ?  175 LEU   B N     1 
ATOM   3253 C CA    . LEU   B 1 195 ? -33.68300 15.03100  31.21100 1.000 26.66530 ?  175 LEU   B CA    1 
ATOM   3254 C C     . LEU   B 1 195 ? -34.03500 15.59200  32.58200 1.000 23.55346 ?  175 LEU   B C     1 
ATOM   3255 O O     . LEU   B 1 195 ? -33.96500 16.81100  32.78900 1.000 23.21095 ?  175 LEU   B O     1 
ATOM   3256 C CB    . LEU   B 1 195 ? -32.17800 15.18500  30.94400 1.000 23.90319 ?  175 LEU   B CB    1 
ATOM   3257 C CG    . LEU   B 1 195 ? -31.27700 14.62200  32.06600 1.000 23.38456 ?  175 LEU   B CG    1 
ATOM   3258 C CD1   . LEU   B 1 195 ? -31.31300 13.06800  32.03500 1.000 21.22497 ?  175 LEU   B CD1   1 
ATOM   3259 C CD2   . LEU   B 1 195 ? -29.84200 15.15300  31.95600 1.000 24.33272 ?  175 LEU   B CD2   1 
ATOM   3260 N N     . ILE   B 1 196 ? -34.43800 14.73400  33.51700 1.000 20.80663 ?  176 ILE   B N     1 
ATOM   3261 C CA    . ILE   B 1 196 ? -34.76800 15.20400  34.86300 1.000 20.60596 ?  176 ILE   B CA    1 
ATOM   3262 C C     . ILE   B 1 196 ? -33.90200 14.44100  35.85300 1.000 18.11378 ?  176 ILE   B C     1 
ATOM   3263 O O     . ILE   B 1 196 ? -33.90200 13.20400  35.86000 1.000 20.57316 ?  176 ILE   B O     1 
ATOM   3264 C CB    . ILE   B 1 196 ? -36.26000 15.05100  35.18300 1.000 22.18979 ?  176 ILE   B CB    1 
ATOM   3265 C CG1   . ILE   B 1 196 ? -37.08400 15.89400  34.19100 1.000 22.04643 ?  176 ILE   B CG1   1 
ATOM   3266 C CG2   . ILE   B 1 196 ? -36.55400 15.46200  36.64700 1.000 22.24791 ?  176 ILE   B CG2   1 
ATOM   3267 C CD1   . ILE   B 1 196 ? -38.54400 16.06800  34.61800 1.000 21.13645 ?  176 ILE   B CD1   1 
ATOM   3268 N N     . LEU   B 1 197 ? -33.12500 15.18200  36.63300 1.000 19.81296 ?  177 LEU   B N     1 
ATOM   3269 C CA    . LEU   B 1 197 ? -32.20600 14.63800  37.62000 1.000 19.56695 ?  177 LEU   B CA    1 
ATOM   3270 C C     . LEU   B 1 197 ? -32.68300 15.00100  39.00700 1.000 20.47503 ?  177 LEU   B C     1 
ATOM   3271 O O     . LEU   B 1 197 ? -33.24700 16.07200  39.20600 1.000 21.66877 ?  177 LEU   B O     1 
ATOM   3272 C CB    . LEU   B 1 197 ? -30.79700 15.21100  37.42800 1.000 18.84951 ?  177 LEU   B CB    1 
ATOM   3273 C CG    . LEU   B 1 197 ? -30.12200 14.95000  36.07800 1.000 23.92499 ?  177 LEU   B CG    1 
ATOM   3274 C CD1   . LEU   B 1 197 ? -28.76500 15.69900  36.02400 1.000 21.40635 ?  177 LEU   B CD1   1 
ATOM   3275 C CD2   . LEU   B 1 197 ? -29.99300 13.42000  35.81500 1.000 22.71079 ?  177 LEU   B CD2   1 
ATOM   3276 N N     . THR   B 1 198 ? -32.43800 14.12000  39.98400 1.000 19.41056 ?  178 THR   B N     1 
ATOM   3277 C CA    . THR   B 1 198 ? -32.46600 14.55100  41.37900 1.000 18.10225 ?  178 THR   B CA    1 
ATOM   3278 C C     . THR   B 1 198 ? -31.21500 14.07300  42.09000 1.000 18.92343 ?  178 THR   B C     1 
ATOM   3279 O O     . THR   B 1 198 ? -30.62800 13.04500  41.73500 1.000 20.04335 ?  178 THR   B O     1 
ATOM   3280 C CB    . THR   B 1 198 ? -33.67700 14.04600  42.17200 1.000 20.95411 ?  178 THR   B CB    1 
ATOM   3281 O OG1   . THR   B 1 198 ? -33.48300 12.65700  42.48600 1.000 23.65326 ?  178 THR   B OG1   1 
ATOM   3282 C CG2   . THR   B 1 198 ? -34.98500 14.27200  41.39100 1.000 23.76519 ?  178 THR   B CG2   1 
ATOM   3283 N N     . SER   B 1 199 ? -30.80300 14.84000  43.10100 1.000 18.51621 ?  179 SER   B N     1 
ATOM   3284 C CA    . SER   B 1 199 ? -29.66600 14.40300  43.89700 1.000 21.61286 ?  179 SER   B CA    1 
ATOM   3285 C C     . SER   B 1 199 ? -29.58100 15.24900  45.15100 1.000 21.70014 ?  179 SER   B C     1 
ATOM   3286 O O     . SER   B 1 199 ? -29.87000 16.45300  45.09900 1.000 19.46887 ?  179 SER   B O     1 
ATOM   3287 C CB    . SER   B 1 199 ? -28.34900 14.52800  43.12800 1.000 22.30604 ?  179 SER   B CB    1 
ATOM   3288 O OG    . SER   B 1 199 ? -27.25200 14.21600  43.97300 1.000 21.22393 ?  179 SER   B OG    1 
ATOM   3289 N N     . PRO   B 1 200 ? -29.20800 14.66200  46.28400 1.000 18.70544 ?  180 PRO   B N     1 
ATOM   3290 C CA    . PRO   B 1 200 ? -28.86100 15.45800  47.46500 1.000 20.01481 ?  180 PRO   B CA    1 
ATOM   3291 C C     . PRO   B 1 200 ? -27.41000 15.91700  47.48100 1.000 20.14333 ?  180 PRO   B C     1 
ATOM   3292 O O     . PRO   B 1 200 ? -26.99500 16.54900  48.45700 1.000 20.60729 ?  180 PRO   B O     1 
ATOM   3293 C CB    . PRO   B 1 200 ? -29.13100 14.47100  48.60300 1.000 23.10284 ?  180 PRO   B CB    1 
ATOM   3294 C CG    . PRO   B 1 200 ? -28.74800 13.14100  48.00400 1.000 22.74551 ?  180 PRO   B CG    1 
ATOM   3295 C CD    . PRO   B 1 200 ? -29.15400 13.20400  46.54800 1.000 20.00787 ?  180 PRO   B CD    1 
ATOM   3296 N N     . TYR   B 1 201 ? -26.63000 15.58300  46.44200 1.000 18.67245 ?  181 TYR   B N     1 
ATOM   3297 C CA    . TYR   B 1 201 ? -25.26300 16.09700  46.28600 1.000 15.26288 ?  181 TYR   B CA    1 
ATOM   3298 C C     . TYR   B 1 201 ? -24.34000 15.63400  47.40900 1.000 20.52880 ?  181 TYR   B C     1 
ATOM   3299 O O     . TYR   B 1 201 ? -23.42500 16.34800  47.82800 1.000 22.19760 ?  181 TYR   B O     1 
ATOM   3300 C CB    . TYR   B 1 201 ? -25.28000 17.63100  46.18500 1.000 16.86527 ?  181 TYR   B CB    1 
ATOM   3301 C CG    . TYR   B 1 201 ? -26.18700 18.17800  45.09300 1.000 19.54710 ?  181 TYR   B CG    1 
ATOM   3302 C CD1   . TYR   B 1 201 ? -26.37200 17.49500  43.88900 1.000 21.32578 ?  181 TYR   B CD1   1 
ATOM   3303 C CD2   . TYR   B 1 201 ? -26.85300 19.41100  45.26600 1.000 19.55655 ?  181 TYR   B CD2   1 
ATOM   3304 C CE1   . TYR   B 1 201 ? -27.19900 18.02400  42.87900 1.000 22.18308 ?  181 TYR   B CE1   1 
ATOM   3305 C CE2   . TYR   B 1 201 ? -27.67800 19.94400  44.27500 1.000 21.06953 ?  181 TYR   B CE2   1 
ATOM   3306 C CZ    . TYR   B 1 201 ? -27.83500 19.25400  43.08200 1.000 22.57130 ?  181 TYR   B CZ    1 
ATOM   3307 O OH    . TYR   B 1 201 ? -28.64400 19.78300  42.10400 1.000 24.43460 ?  181 TYR   B OH    1 
ATOM   3308 N N     . THR   B 1 202 ? -24.57200 14.42600  47.90300 1.000 19.25337 ?  182 THR   B N     1 
ATOM   3309 C CA    . THR   B 1 202 ? -23.75400 13.87000  48.97900 1.000 22.69423 ?  182 THR   B CA    1 
ATOM   3310 C C     . THR   B 1 202 ? -22.55200 13.10600  48.40200 1.000 24.95202 ?  182 THR   B C     1 
ATOM   3311 O O     . THR   B 1 202 ? -22.38200 11.90000  48.59000 1.000 24.47056 ?  182 THR   B O     1 
ATOM   3312 C CB    . THR   B 1 202 ? -24.63000 12.99100  49.86300 1.000 25.14054 ?  182 THR   B CB    1 
ATOM   3313 O OG1   . THR   B 1 202 ? -25.33600 12.09000  49.02900 1.000 23.89844 ?  182 THR   B OG1   1 
ATOM   3314 C CG2   . THR   B 1 202 ? -25.66300 13.83100  50.61000 1.000 24.50733 ?  182 THR   B CG2   1 
ATOM   3315 N N     . TRP   B 1 203 ? -21.69800 13.84500  47.69200 1.000 20.15269 ?  183 TRP   B N     1 
ATOM   3316 C CA    . TRP   B 1 203 ? -20.52000 13.24400  47.06100 1.000 19.05789 ?  183 TRP   B CA    1 
ATOM   3317 C C     . TRP   B 1 203 ? -19.60200 12.62400  48.10100 1.000 23.97210 ?  183 TRP   B C     1 
ATOM   3318 O O     . TRP   B 1 203 ? -19.30400 13.23000  49.13600 1.000 22.55464 ?  183 TRP   B O     1 
ATOM   3319 C CB    . TRP   B 1 203 ? -19.75500 14.31200  46.27000 1.000 18.71095 ?  183 TRP   B CB    1 
ATOM   3320 C CG    . TRP   B 1 203 ? -20.61700 14.93000  45.21500 1.000 17.25443 ?  183 TRP   B CG    1 
ATOM   3321 C CD1   . TRP   B 1 203 ? -21.24700 16.15000  45.27400 1.000 18.76590 ?  183 TRP   B CD1   1 
ATOM   3322 C CD2   . TRP   B 1 203 ? -20.97100 14.34800  43.96200 1.000 20.10306 ?  183 TRP   B CD2   1 
ATOM   3323 N NE1   . TRP   B 1 203 ? -21.97500 16.35400  44.11800 1.000 19.73271 ?  183 TRP   B NE1   1 
ATOM   3324 C CE2   . TRP   B 1 203 ? -21.81600 15.25800  43.30100 1.000 19.52686 ?  183 TRP   B CE2   1 
ATOM   3325 C CE3   . TRP   B 1 203 ? -20.64800 13.12600  43.32800 1.000 20.14603 ?  183 TRP   B CE3   1 
ATOM   3326 C CZ2   . TRP   B 1 203 ? -22.34300 15.00400  42.03200 1.000 21.02728 ?  183 TRP   B CZ2   1 
ATOM   3327 C CZ3   . TRP   B 1 203 ? -21.17900 12.87200  42.06900 1.000 20.05504 ?  183 TRP   B CZ3   1 
ATOM   3328 C CH2   . TRP   B 1 203 ? -22.01700 13.80200  41.43100 1.000 21.72405 ?  183 TRP   B CH2   1 
ATOM   3329 N N     . ARG   B 1 204 ? -19.12600 11.41900  47.80800 1.000 21.02796 ?  184 ARG   B N     1 
ATOM   3330 C CA    . ARG   B 1 204 ? -18.26500 10.68900  48.73300 1.000 22.10818 ?  184 ARG   B CA    1 
ATOM   3331 C C     . ARG   B 1 204 ? -17.24300 9.92700   47.90800 1.000 23.17233 ?  184 ARG   B C     1 
ATOM   3332 O O     . ARG   B 1 204 ? -17.59200 9.35200   46.87300 1.000 24.69703 ?  184 ARG   B O     1 
ATOM   3333 C CB    . ARG   B 1 204 ? -19.07100 9.69800   49.57600 1.000 26.53614 ?  184 ARG   B CB    1 
ATOM   3334 C CG    . ARG   B 1 204 ? -19.88000 10.33000  50.70900 1.000 37.17154 ?  184 ARG   B CG    1 
ATOM   3335 C CD    . ARG   B 1 204 ? -20.50800 9.23100   51.55400 1.000 47.51249 ?  184 ARG   B CD    1 
ATOM   3336 N N     . GLU   B 1 205 ? -15.99000 9.90800   48.37600 1.000 23.62672 ?  185 GLU   B N     1 
ATOM   3337 C CA    . GLU   B 1 205 ? -14.96200 9.13700   47.67300 1.000 24.95626 ?  185 GLU   B CA    1 
ATOM   3338 C C     . GLU   B 1 205 ? -15.24600 7.64700   47.62400 1.000 29.83234 ?  185 GLU   B C     1 
ATOM   3339 O O     . GLU   B 1 205 ? -14.69200 6.96600   46.75800 1.000 34.40309 ?  185 GLU   B O     1 
ATOM   3340 C CB    . GLU   B 1 205 ? -13.59300 9.38300   48.30800 1.000 28.14148 ?  185 GLU   B CB    1 
ATOM   3341 C CG    . GLU   B 1 205 ? -13.12500 10.82000  48.06300 1.000 41.20606 ?  185 GLU   B CG    1 
ATOM   3342 C CD    . GLU   B 1 205 ? -11.86100 11.18800  48.81700 1.000 63.12427 ?  185 GLU   B CD    1 
ATOM   3343 O OE1   . GLU   B 1 205 ? -11.46700 10.43000  49.73100 1.000 65.13066 ?  185 GLU   B OE1   1 
ATOM   3344 O OE2   . GLU   B 1 205 ? -11.27000 12.24700  48.49500 1.000 69.48477 -1 185 GLU   B OE2   1 
ATOM   3345 N N     . GLU   B 1 206 ? -16.09500 7.11600   48.50900 1.000 30.88490 ?  186 GLU   B N     1 
ATOM   3346 C CA    . GLU   B 1 206 ? -16.44200 5.69700   48.40300 1.000 31.02948 ?  186 GLU   B CA    1 
ATOM   3347 C C     . GLU   B 1 206 ? -17.16200 5.38200   47.09700 1.000 36.41263 ?  186 GLU   B C     1 
ATOM   3348 O O     . GLU   B 1 206 ? -17.08100 4.25000   46.60500 1.000 32.37813 ?  186 GLU   B O     1 
ATOM   3349 C CB    . GLU   B 1 206 ? -17.31500 5.25900   49.58500 1.000 34.13420 ?  186 GLU   B CB    1 
ATOM   3350 N N     . TYR   B 1 207 ? -17.88200 6.34800   46.52400 1.000 25.15969 ?  187 TYR   B N     1 
ATOM   3351 C CA    . TYR   B 1 207 ? -18.65000 6.11100   45.30800 1.000 20.61024 ?  187 TYR   B CA    1 
ATOM   3352 C C     . TYR   B 1 207 ? -18.04800 6.77100   44.08300 1.000 23.40146 ?  187 TYR   B C     1 
ATOM   3353 O O     . TYR   B 1 207 ? -18.10900 6.20500   42.99000 1.000 23.79872 ?  187 TYR   B O     1 
ATOM   3354 C CB    . TYR   B 1 207 ? -20.08800 6.62600   45.47600 1.000 24.71720 ?  187 TYR   B CB    1 
ATOM   3355 C CG    . TYR   B 1 207 ? -20.93200 5.75400   46.39000 1.000 29.97848 ?  187 TYR   B CG    1 
ATOM   3356 C CD1   . TYR   B 1 207 ? -21.56400 4.61900   45.90300 1.000 34.00574 ?  187 TYR   B CD1   1 
ATOM   3357 C CD2   . TYR   B 1 207 ? -21.10700 6.08300   47.72400 1.000 34.43926 ?  187 TYR   B CD2   1 
ATOM   3358 C CE1   . TYR   B 1 207 ? -22.33100 3.81100   46.73700 1.000 39.86609 ?  187 TYR   B CE1   1 
ATOM   3359 C CE2   . TYR   B 1 207 ? -21.87100 5.28600   48.56900 1.000 40.27792 ?  187 TYR   B CE2   1 
ATOM   3360 C CZ    . TYR   B 1 207 ? -22.47900 4.15500   48.06600 1.000 44.22199 ?  187 TYR   B CZ    1 
ATOM   3361 O OH    . TYR   B 1 207 ? -23.24300 3.36500   48.90000 1.000 53.30550 ?  187 TYR   B OH    1 
ATOM   3362 N N     . THR   B 1 208 ? -17.49900 7.97500   44.23700 1.000 25.21149 ?  188 THR   B N     1 
ATOM   3363 C CA    . THR   B 1 208 ? -17.09200 8.81300   43.11700 1.000 22.95826 ?  188 THR   B CA    1 
ATOM   3364 C C     . THR   B 1 208 ? -15.69100 9.33900   43.37200 1.000 22.35091 ?  188 THR   B C     1 
ATOM   3365 O O     . THR   B 1 208 ? -15.44100 9.94400   44.41500 1.000 24.20525 ?  188 THR   B O     1 
ATOM   3366 C CB    . THR   B 1 208 ? -18.06400 10.00100  42.93400 1.000 22.74487 ?  188 THR   B CB    1 
ATOM   3367 O OG1   . THR   B 1 208 ? -19.42000 9.54400   43.01600 1.000 24.11699 ?  188 THR   B OG1   1 
ATOM   3368 C CG2   . THR   B 1 208 ? -17.81700 10.75600  41.61600 1.000 20.61097 ?  188 THR   B CG2   1 
ATOM   3369 N N     . ALA   B 1 209 ? -14.78800 9.14400   42.41800 1.000 22.87449 ?  189 ALA   B N     1 
ATOM   3370 C CA    . ALA   B 1 209 ? -13.46300 9.73200   42.55700 1.000 26.35290 ?  189 ALA   B CA    1 
ATOM   3371 C C     . ALA   B 1 209 ? -13.59100 11.23600  42.69600 1.000 23.59530 ?  189 ALA   B C     1 
ATOM   3372 O O     . ALA   B 1 209 ? -14.37900 11.86800  41.98800 1.000 21.37182 ?  189 ALA   B O     1 
ATOM   3373 C CB    . ALA   B 1 209 ? -12.58300 9.40900   41.34800 1.000 27.57382 ?  189 ALA   B CB    1 
ATOM   3374 N N     . LYS   B 1 210 ? -12.81300 11.80800  43.61700 1.000 27.38409 ?  190 LYS   B N     1 
ATOM   3375 C CA    . LYS   B 1 210 ? -12.91100 13.25100  43.86000 1.000 25.71459 ?  190 LYS   B CA    1 
ATOM   3376 C C     . LYS   B 1 210 ? -12.79300 14.06200  42.57200 1.000 23.44436 ?  190 LYS   B C     1 
ATOM   3377 O O     . LYS   B 1 210 ? -13.54700 15.01800  42.34500 1.000 23.57269 ?  190 LYS   B O     1 
ATOM   3378 C CB    . LYS   B 1 210 ? -11.84100 13.66900  44.86700 1.000 27.59643 ?  190 LYS   B CB    1 
ATOM   3379 C CG    . LYS   B 1 210 ? -11.90800 15.14200  45.21600 1.000 35.36622 ?  190 LYS   B CG    1 
ATOM   3380 C CD    . LYS   B 1 210 ? -12.25900 15.38500  46.66700 1.000 50.43956 ?  190 LYS   B CD    1 
ATOM   3381 C CE    . LYS   B 1 210 ? -11.84300 16.80500  47.05100 1.000 43.52820 ?  190 LYS   B CE    1 
ATOM   3382 N N     . LYS   B 1 211 ? -11.88000 13.67600  41.68200 1.000 24.31586 ?  191 LYS   B N     1 
ATOM   3383 C CA    . LYS   B 1 211 ? -11.73700 14.43200  40.44400 1.000 24.42538 ?  191 LYS   B CA    1 
ATOM   3384 C C     . LYS   B 1 211 ? -12.97400 14.35900  39.55500 1.000 27.04674 ?  191 LYS   B C     1 
ATOM   3385 O O     . LYS   B 1 211 ? -13.10900 15.18500  38.64900 1.000 25.12639 ?  191 LYS   B O     1 
ATOM   3386 C CB    . LYS   B 1 211 ? -10.50700 13.93800  39.67600 1.000 24.32886 ?  191 LYS   B CB    1 
ATOM   3387 C CG    . LYS   B 1 211 ? -10.63700 12.48500  39.23100 1.000 25.55488 ?  191 LYS   B CG    1 
ATOM   3388 C CD    . LYS   B 1 211 ? -9.30900  11.91300  38.74700 1.000 30.53371 ?  191 LYS   B CD    1 
ATOM   3389 C CE    . LYS   B 1 211 ? -9.47900  10.45900  38.29500 1.000 28.91801 ?  191 LYS   B CE    1 
ATOM   3390 N NZ    . LYS   B 1 211 ? -8.51200  10.10100  37.23100 1.000 31.77064 ?  191 LYS   B NZ    1 
ATOM   3391 N N     . PHE   B 1 212 ? -13.89300 13.42200  39.81600 1.000 23.95561 ?  192 PHE   B N     1 
ATOM   3392 C CA    . PHE   B 1 212 ? -15.12100 13.29900  39.04900 1.000 22.30304 ?  192 PHE   B CA    1 
ATOM   3393 C C     . PHE   B 1 212 ? -16.35300 13.84500  39.77800 1.000 29.16664 ?  192 PHE   B C     1 
ATOM   3394 O O     . PHE   B 1 212 ? -17.45700 13.76600  39.22900 1.000 23.97063 ?  192 PHE   B O     1 
ATOM   3395 C CB    . PHE   B 1 212 ? -15.35900 11.82500  38.68300 1.000 20.46188 ?  192 PHE   B CB    1 
ATOM   3396 C CG    . PHE   B 1 212 ? -14.36000 11.26700  37.69000 1.000 26.35955 ?  192 PHE   B CG    1 
ATOM   3397 C CD1   . PHE   B 1 212 ? -13.84200 12.07100  36.66200 1.000 25.92550 ?  192 PHE   B CD1   1 
ATOM   3398 C CD2   . PHE   B 1 212 ? -13.94200 9.93500   37.80000 1.000 24.74881 ?  192 PHE   B CD2   1 
ATOM   3399 C CE1   . PHE   B 1 212 ? -12.91100 11.53200  35.74400 1.000 25.96611 ?  192 PHE   B CE1   1 
ATOM   3400 C CE2   . PHE   B 1 212 ? -13.02300 9.39600   36.89000 1.000 28.55988 ?  192 PHE   B CE2   1 
ATOM   3401 C CZ    . PHE   B 1 212 ? -12.51000 10.19400  35.86700 1.000 23.07240 ?  192 PHE   B CZ    1 
ATOM   3402 N N     . TRP   B 1 213 ? -16.21400 14.37400  40.99800 1.000 24.04258 ?  193 TRP   B N     1 
ATOM   3403 C CA    . TRP   B 1 213 ? -17.35300 15.03500  41.62700 1.000 21.30796 ?  193 TRP   B CA    1 
ATOM   3404 C C     . TRP   B 1 213 ? -17.83500 16.18700  40.74900 1.000 24.11641 ?  193 TRP   B C     1 
ATOM   3405 O O     . TRP   B 1 213 ? -17.03200 16.98500  40.26100 1.000 22.55554 ?  193 TRP   B O     1 
ATOM   3406 C CB    . TRP   B 1 213 ? -16.99100 15.59900  43.00500 1.000 19.30143 ?  193 TRP   B CB    1 
ATOM   3407 C CG    . TRP   B 1 213 ? -16.66200 14.59300  44.07400 1.000 17.16905 ?  193 TRP   B CG    1 
ATOM   3408 C CD1   . TRP   B 1 213 ? -16.51600 13.22600  43.93300 1.000 21.77559 ?  193 TRP   B CD1   1 
ATOM   3409 C CD2   . TRP   B 1 213 ? -16.43400 14.88200  45.44900 1.000 21.28352 ?  193 TRP   B CD2   1 
ATOM   3410 N NE1   . TRP   B 1 213 ? -16.22700 12.65900  45.15300 1.000 23.22031 ?  193 TRP   B NE1   1 
ATOM   3411 C CE2   . TRP   B 1 213 ? -16.14500 13.66200  46.09300 1.000 20.96028 ?  193 TRP   B CE2   1 
ATOM   3412 C CE3   . TRP   B 1 213 ? -16.44100 16.07100  46.20700 1.000 23.79733 ?  193 TRP   B CE3   1 
ATOM   3413 C CZ2   . TRP   B 1 213 ? -15.88700 13.58600  47.46100 1.000 22.48117 ?  193 TRP   B CZ2   1 
ATOM   3414 C CZ3   . TRP   B 1 213 ? -16.16800 15.99700  47.55500 1.000 26.15954 ?  193 TRP   B CZ3   1 
ATOM   3415 C CH2   . TRP   B 1 213 ? -15.89500 14.76700  48.17500 1.000 27.07744 ?  193 TRP   B CH2   1 
ATOM   3416 N N     . ILE   B 1 214 ? -19.15100 16.27900  40.55500 1.000 19.61966 ?  194 ILE   B N     1 
ATOM   3417 C CA    . ILE   B 1 214 ? -19.68900 17.36600  39.73600 1.000 21.67575 ?  194 ILE   B CA    1 
ATOM   3418 C C     . ILE   B 1 214 ? -19.69800 18.69300  40.50500 1.000 21.46154 ?  194 ILE   B C     1 
ATOM   3419 O O     . ILE   B 1 214 ? -19.58000 19.76900  39.90000 1.000 21.82364 ?  194 ILE   B O     1 
ATOM   3420 C CB    . ILE   B 1 214 ? -21.08800 16.99000  39.20800 1.000 18.03385 ?  194 ILE   B CB    1 
ATOM   3421 C CG1   . ILE   B 1 214 ? -21.03800 15.66500  38.42700 1.000 23.87269 ?  194 ILE   B CG1   1 
ATOM   3422 C CG2   . ILE   B 1 214 ? -21.68000 18.11600  38.32900 1.000 21.61752 ?  194 ILE   B CG2   1 
ATOM   3423 C CD1   . ILE   B 1 214 ? -19.98100 15.66500  37.39000 1.000 36.12153 ?  194 ILE   B CD1   1 
ATOM   3424 N N     . GLY   B 1 215 ? -19.81100 18.64000  41.82400 1.000 19.68982 ?  195 GLY   B N     1 
ATOM   3425 C CA    . GLY   B 1 215 ? -19.63300 19.81300  42.65300 1.000 22.46479 ?  195 GLY   B CA    1 
ATOM   3426 C C     . GLY   B 1 215 ? -19.38800 19.36300  44.07500 1.000 18.43220 ?  195 GLY   B C     1 
ATOM   3427 O O     . GLY   B 1 215 ? -19.05200 18.20800  44.31800 1.000 21.10812 ?  195 GLY   B O     1 
ATOM   3428 N N     . GLY   B 1 216 ? -19.58100 20.28500  45.01900 1.000 20.30670 ?  196 GLY   B N     1 
ATOM   3429 C CA    . GLY   B 1 216 ? -19.24000 20.00600  46.40100 1.000 21.02471 ?  196 GLY   B CA    1 
ATOM   3430 C C     . GLY   B 1 216 ? -17.75400 19.92700  46.67700 1.000 29.02575 ?  196 GLY   B C     1 
ATOM   3431 O O     . GLY   B 1 216 ? -17.33200 19.17700  47.56100 1.000 25.35985 ?  196 GLY   B O     1 
ATOM   3432 N N     . TYR   B 1 217 ? -16.94000 20.68400  45.94500 1.000 28.10559 ?  197 TYR   B N     1 
ATOM   3433 C CA    . TYR   B 1 217 ? -15.49900 20.66300  46.15900 1.000 21.85740 ?  197 TYR   B CA    1 
ATOM   3434 C C     . TYR   B 1 217 ? -14.98100 22.08500  45.98800 1.000 29.49135 ?  197 TYR   B C     1 
ATOM   3435 O O     . TYR   B 1 217 ? -15.66000 22.94300  45.42500 1.000 23.83675 ?  197 TYR   B O     1 
ATOM   3436 C CB    . TYR   B 1 217 ? -14.77700 19.69500  45.20200 1.000 26.29303 ?  197 TYR   B CB    1 
ATOM   3437 C CG    . TYR   B 1 217 ? -14.87300 20.08300  43.74700 1.000 33.67550 ?  197 TYR   B CG    1 
ATOM   3438 C CD1   . TYR   B 1 217 ? -15.93100 19.64200  42.96600 1.000 25.29200 ?  197 TYR   B CD1   1 
ATOM   3439 C CD2   . TYR   B 1 217 ? -13.91200 20.89600  43.14800 1.000 29.08511 ?  197 TYR   B CD2   1 
ATOM   3440 C CE1   . TYR   B 1 217 ? -16.04200 20.00400  41.63900 1.000 30.63578 ?  197 TYR   B CE1   1 
ATOM   3441 C CE2   . TYR   B 1 217 ? -14.01700 21.26000  41.80500 1.000 30.69514 ?  197 TYR   B CE2   1 
ATOM   3442 C CZ    . TYR   B 1 217 ? -15.07800 20.80600  41.05700 1.000 29.26236 ?  197 TYR   B CZ    1 
ATOM   3443 O OH    . TYR   B 1 217 ? -15.21300 21.15500  39.73600 1.000 32.03969 ?  197 TYR   B OH    1 
ATOM   3444 N N     . VAL   B 1 218 ? -13.79600 22.34300  46.53600 1.000 26.54249 ?  198 VAL   B N     1 
ATOM   3445 C CA    . VAL   B 1 218 ? -13.12700 23.63300  46.36200 1.000 25.79550 ?  198 VAL   B CA    1 
ATOM   3446 C C     . VAL   B 1 218 ? -12.14000 23.44500  45.22500 1.000 28.48218 ?  198 VAL   B C     1 
ATOM   3447 O O     . VAL   B 1 218 ? -11.34700 22.49500  45.25300 1.000 28.30854 ?  198 VAL   B O     1 
ATOM   3448 C CB    . VAL   B 1 218 ? -12.41200 24.07400  47.64900 1.000 33.94354 ?  198 VAL   B CB    1 
ATOM   3449 C CG1   . VAL   B 1 218 ? -11.53600 25.32800  47.36500 1.000 34.47379 ?  198 VAL   B CG1   1 
ATOM   3450 C CG2   . VAL   B 1 218 ? -13.40700 24.32600  48.76400 1.000 31.71396 ?  198 VAL   B CG2   1 
ATOM   3451 N N     . ASP   B 1 219 ? -12.21500 24.29400  44.19800 1.000 23.47557 ?  199 ASP   B N     1 
ATOM   3452 C CA    . ASP   B 1 219 ? -11.34200 24.06400  43.05300 1.000 25.19317 ?  199 ASP   B CA    1 
ATOM   3453 C C     . ASP   B 1 219 ? -9.91600  24.52100  43.38900 1.000 30.14918 ?  199 ASP   B C     1 
ATOM   3454 O O     . ASP   B 1 219 ? -9.62900  24.96200  44.50600 1.000 30.06901 ?  199 ASP   B O     1 
ATOM   3455 C CB    . ASP   B 1 219 ? -11.88500 24.72700  41.78200 1.000 23.59218 ?  199 ASP   B CB    1 
ATOM   3456 C CG    . ASP   B 1 219 ? -11.89400 26.27100  41.83500 1.000 37.52657 ?  199 ASP   B CG    1 
ATOM   3457 O OD1   . ASP   B 1 219 ? -11.24200 26.89100  42.70200 1.000 29.24904 ?  199 ASP   B OD1   1 
ATOM   3458 O OD2   . ASP   B 1 219 ? -12.56400 26.86700  40.97400 1.000 31.36272 -1 199 ASP   B OD2   1 
ATOM   3459 N N     . GLU   B 1 220 ? -9.00700  24.38900  42.41200 1.000 30.29819 ?  200 GLU   B N     1 
ATOM   3460 C CA    . GLU   B 1 220 ? -7.59700  24.67900  42.65800 1.000 36.68212 ?  200 GLU   B CA    1 
ATOM   3461 C C     . GLU   B 1 220 ? -7.36900  26.15400  42.98300 1.000 31.44092 ?  200 GLU   B C     1 
ATOM   3462 O O     . GLU   B 1 220 ? -6.33600  26.50500  43.56800 1.000 33.63054 ?  200 GLU   B O     1 
ATOM   3463 C CB    . GLU   B 1 220 ? -6.75300  24.25600  41.44900 1.000 38.08579 ?  200 GLU   B CB    1 
ATOM   3464 C CG    . GLU   B 1 220 ? -6.59500  25.34300  40.39500 1.000 41.98994 ?  200 GLU   B CG    1 
ATOM   3465 C CD    . GLU   B 1 220 ? -5.77900  24.91300  39.17300 1.000 66.11582 ?  200 GLU   B CD    1 
ATOM   3466 O OE1   . GLU   B 1 220 ? -4.83400  24.11200  39.33200 1.000 63.97001 ?  200 GLU   B OE1   1 
ATOM   3467 O OE2   . GLU   B 1 220 ? -6.05600  25.41600  38.05600 1.000 68.65382 -1 200 GLU   B OE2   1 
ATOM   3468 N N     . ASN   B 1 221 ? -8.31900  27.01000  42.64400 1.000 29.22995 ?  201 ASN   B N     1 
ATOM   3469 C CA    . ASN   B 1 221 ? -8.19200  28.44800  42.85200 1.000 26.74575 ?  201 ASN   B CA    1 
ATOM   3470 C C     . ASN   B 1 221 ? -8.80400  28.92300  44.16300 1.000 31.17248 ?  201 ASN   B C     1 
ATOM   3471 O O     . ASN   B 1 221 ? -8.76100  30.12400  44.44700 1.000 27.74510 ?  201 ASN   B O     1 
ATOM   3472 C CB    . ASN   B 1 221 ? -8.83100  29.20400  41.68500 1.000 29.55058 ?  201 ASN   B CB    1 
ATOM   3473 C CG    . ASN   B 1 221 ? -8.30300  28.76000  40.33800 1.000 34.68575 ?  201 ASN   B CG    1 
ATOM   3474 O OD1   . ASN   B 1 221 ? -7.09800  28.60300  40.15500 1.000 34.12442 ?  201 ASN   B OD1   1 
ATOM   3475 N ND2   . ASN   B 1 221 ? -9.20300  28.60500  39.36700 1.000 34.83347 ?  201 ASN   B ND2   1 
ATOM   3476 N N     . GLY   B 1 222 ? -9.39000  28.02800  44.95900 1.000 26.27408 ?  202 GLY   B N     1 
ATOM   3477 C CA    . GLY   B 1 222 ? -9.96900  28.39900  46.23000 1.000 28.37079 ?  202 GLY   B CA    1 
ATOM   3478 C C     . GLY   B 1 222 ? -11.45200 28.69500  46.21200 1.000 27.17942 ?  202 GLY   B C     1 
ATOM   3479 O O     . GLY   B 1 222 ? -11.98100 29.14800  47.23400 1.000 30.02902 ?  202 GLY   B O     1 
ATOM   3480 N N     . LYS   B 1 223 ? -12.13200 28.47700  45.08500 1.000 28.94971 ?  203 LYS   B N     1 
ATOM   3481 C CA    . LYS   B 1 223 ? -13.54300 28.80800  44.94200 1.000 30.12118 ?  203 LYS   B CA    1 
ATOM   3482 C C     . LYS   B 1 223 ? -14.39700 27.55300  45.08800 1.000 29.74320 ?  203 LYS   B C     1 
ATOM   3483 O O     . LYS   B 1 223 ? -14.06200 26.49300  44.54900 1.000 27.29453 ?  203 LYS   B O     1 
ATOM   3484 C CB    . LYS   B 1 223 ? -13.82500 29.47000  43.59300 1.000 36.49868 ?  203 LYS   B CB    1 
ATOM   3485 C CG    . LYS   B 1 223 ? -13.02500 30.75800  43.32800 1.000 49.63432 ?  203 LYS   B CG    1 
ATOM   3486 C CD    . LYS   B 1 223 ? -13.72100 32.04800  43.80700 1.000 47.87757 ?  203 LYS   B CD    1 
ATOM   3487 C CE    . LYS   B 1 223 ? -12.86700 33.29000  43.47600 1.000 38.25673 ?  203 LYS   B CE    1 
ATOM   3488 N NZ    . LYS   B 1 223 ? -13.63500 34.56100  43.28900 1.000 39.50757 ?  203 LYS   B NZ    1 
ATOM   3489 N N     . GLU   B 1 224 ? -15.48500 27.69100  45.83200 1.000 25.56014 ?  204 GLU   B N     1 
ATOM   3490 C CA    . GLU   B 1 224 ? -16.44000 26.59800  46.02100 1.000 29.44693 ?  204 GLU   B CA    1 
ATOM   3491 C C     . GLU   B 1 224 ? -17.20200 26.35900  44.72600 1.000 26.04705 ?  204 GLU   B C     1 
ATOM   3492 O O     . GLU   B 1 224 ? -17.63600 27.31300  44.07200 1.000 27.80010 ?  204 GLU   B O     1 
ATOM   3493 C CB    . GLU   B 1 224 ? -17.41400 26.95300  47.14700 1.000 30.74716 ?  204 GLU   B CB    1 
ATOM   3494 C CG    . GLU   B 1 224 ? -16.74100 27.13000  48.51200 1.000 43.35943 ?  204 GLU   B CG    1 
ATOM   3495 C CD    . GLU   B 1 224 ? -17.73200 27.11500  49.67000 1.000 47.06775 ?  204 GLU   B CD    1 
ATOM   3496 O OE1   . GLU   B 1 224 ? -18.95200 27.18200  49.40300 1.000 52.19019 ?  204 GLU   B OE1   1 
ATOM   3497 O OE2   . GLU   B 1 224 ? -17.29400 27.02400  50.84100 1.000 59.55823 -1 204 GLU   B OE2   1 
ATOM   3498 N N     . VAL   B 1 225 ? -17.33800 25.09100  44.33600 1.000 22.91476 ?  205 VAL   B N     1 
ATOM   3499 C CA    . VAL   B 1 225 ? -18.09300 24.70800  43.14900 1.000 23.22293 ?  205 VAL   B CA    1 
ATOM   3500 C C     . VAL   B 1 225 ? -19.36200 24.00800  43.60800 1.000 28.38255 ?  205 VAL   B C     1 
ATOM   3501 O O     . VAL   B 1 225 ? -19.30200 22.96500  44.27000 1.000 25.93871 ?  205 VAL   B O     1 
ATOM   3502 C CB    . VAL   B 1 225 ? -17.29000 23.77600  42.22400 1.000 29.97720 ?  205 VAL   B CB    1 
ATOM   3503 C CG1   . VAL   B 1 225 ? -18.13200 23.41000  40.98400 1.000 24.75117 ?  205 VAL   B CG1   1 
ATOM   3504 C CG2   . VAL   B 1 225 ? -15.96700 24.42000  41.81000 1.000 32.35094 ?  205 VAL   B CG2   1 
ATOM   3505 N N     . SER   B 1 226 ? -20.49900 24.55200  43.22200 1.000 23.08032 ?  206 SER   B N     1 
ATOM   3506 C CA    . SER   B 1 226 ? -21.77200 23.92500  43.53500 1.000 23.71729 ?  206 SER   B CA    1 
ATOM   3507 C C     . SER   B 1 226 ? -22.10700 22.87700  42.47500 1.000 21.84214 ?  206 SER   B C     1 
ATOM   3508 O O     . SER   B 1 226 ? -21.72000 23.00000  41.30900 1.000 25.01753 ?  206 SER   B O     1 
ATOM   3509 C CB    . SER   B 1 226 ? -22.84900 25.00300  43.64800 1.000 33.90861 ?  206 SER   B CB    1 
ATOM   3510 O OG    . SER   B 1 226 ? -23.58000 25.14600  42.45900 1.000 26.19598 ?  206 SER   B OG    1 
ATOM   3511 N N     . THR   B 1 227 ? -22.80100 21.81300  42.89600 1.000 19.03123 ?  207 THR   B N     1 
ATOM   3512 C CA    . THR   B 1 227 ? -23.11200 20.75800  41.92900 1.000 17.30824 ?  207 THR   B CA    1 
ATOM   3513 C C     . THR   B 1 227 ? -24.02400 21.26400  40.82500 1.000 18.37571 ?  207 THR   B C     1 
ATOM   3514 O O     . THR   B 1 227 ? -23.85800 20.87600  39.66600 1.000 19.04325 ?  207 THR   B O     1 
ATOM   3515 C CB    . THR   B 1 227 ? -23.73200 19.53100  42.62600 1.000 19.64732 ?  207 THR   B CB    1 
ATOM   3516 O OG1   . THR   B 1 227 ? -22.89400 19.11600  43.70200 1.000 19.02037 ?  207 THR   B OG1   1 
ATOM   3517 C CG2   . THR   B 1 227 ? -23.93100 18.37400  41.63700 1.000 19.33639 ?  207 THR   B CG2   1 
ATOM   3518 N N     . LEU   B 1 228 ? -24.95000 22.16900  41.14000 1.000 21.03925 ?  208 LEU   B N     1 
ATOM   3519 C CA    . LEU   B 1 228 ? -25.81100 22.67700  40.07500 1.000 20.12179 ?  208 LEU   B CA    1 
ATOM   3520 C C     . LEU   B 1 228 ? -24.99300 23.44100  39.03800 1.000 22.22364 ?  208 LEU   B C     1 
ATOM   3521 O O     . LEU   B 1 228 ? -25.23900 23.32100  37.82700 1.000 24.00778 ?  208 LEU   B O     1 
ATOM   3522 C CB    . LEU   B 1 228 ? -26.92200 23.55200  40.65400 1.000 20.23558 ?  208 LEU   B CB    1 
ATOM   3523 C CG    . LEU   B 1 228 ? -27.97700 24.01700  39.63500 1.000 23.74454 ?  208 LEU   B CG    1 
ATOM   3524 C CD1   . LEU   B 1 228 ? -28.64400 22.85900  38.89500 1.000 28.25924 ?  208 LEU   B CD1   1 
ATOM   3525 C CD2   . LEU   B 1 228 ? -29.03600 24.90400  40.31000 1.000 22.46574 ?  208 LEU   B CD2   1 
ATOM   3526 N N     . GLU   B 1 229 ? -24.00300 24.21300  39.49200 1.000 22.40263 ?  209 GLU   B N     1 
ATOM   3527 C CA    . GLU   B 1 229 ? -23.09700 24.88600  38.55100 1.000 25.67774 ?  209 GLU   B CA    1 
ATOM   3528 C C     . GLU   B 1 229 ? -22.33100 23.87300  37.70700 1.000 25.96994 ?  209 GLU   B C     1 
ATOM   3529 O O     . GLU   B 1 229 ? -22.17600 24.04900  36.49100 1.000 26.07109 ?  209 GLU   B O     1 
ATOM   3530 C CB    . GLU   B 1 229 ? -22.11900 25.79100  39.31000 1.000 29.09103 ?  209 GLU   B CB    1 
ATOM   3531 N N     . GLY   B 1 230 ? -21.83500 22.80300  38.33500 1.000 19.40976 ?  210 GLY   B N     1 
ATOM   3532 C CA    . GLY   B 1 230 ? -21.15000 21.77400  37.57100 1.000 21.28322 ?  210 GLY   B CA    1 
ATOM   3533 C C     . GLY   B 1 230 ? -22.05700 21.10200  36.55000 1.000 22.45966 ?  210 GLY   B C     1 
ATOM   3534 O O     . GLY   B 1 230 ? -21.61700 20.75100  35.44900 1.000 23.17191 ?  210 GLY   B O     1 
ATOM   3535 N N     . LEU   B 1 231 ? -23.33100 20.90300  36.90700 1.000 22.85384 ?  211 LEU   B N     1 
ATOM   3536 C CA    . LEU   B 1 231 ? -24.30000 20.32700  35.96700 1.000 20.64336 ?  211 LEU   B CA    1 
ATOM   3537 C C     . LEU   B 1 231 ? -24.54300 21.26200  34.79200 1.000 24.69170 ?  211 LEU   B C     1 
ATOM   3538 O O     . LEU   B 1 231 ? -24.61600 20.81800  33.63900 1.000 23.81742 ?  211 LEU   B O     1 
ATOM   3539 C CB    . LEU   B 1 231 ? -25.62400 20.04400  36.68200 1.000 19.08779 ?  211 LEU   B CB    1 
ATOM   3540 C CG    . LEU   B 1 231 ? -25.54000 18.84400  37.64600 1.000 18.30243 ?  211 LEU   B CG    1 
ATOM   3541 C CD1   . LEU   B 1 231 ? -26.82800 18.78800  38.49600 1.000 20.47512 ?  211 LEU   B CD1   1 
ATOM   3542 C CD2   . LEU   B 1 231 ? -25.35800 17.50200  36.90300 1.000 20.24925 ?  211 LEU   B CD2   1 
ATOM   3543 N N     . LYS   B 1 232 ? -24.69300 22.55600  35.07000 1.000 25.32819 ?  212 LYS   B N     1 
ATOM   3544 C CA    . LYS   B 1 232 ? -24.85500 23.52400  33.98900 1.000 26.11681 ?  212 LYS   B CA    1 
ATOM   3545 C C     . LYS   B 1 232 ? -23.67900 23.45200  33.02500 1.000 26.10590 ?  212 LYS   B C     1 
ATOM   3546 O O     . LYS   B 1 232 ? -23.86100 23.42200  31.80100 1.000 27.46747 ?  212 LYS   B O     1 
ATOM   3547 C CB    . LYS   B 1 232 ? -24.99400 24.93100  34.56900 1.000 25.20527 ?  212 LYS   B CB    1 
ATOM   3548 C CG    . LYS   B 1 232 ? -26.34700 25.20100  35.22400 1.000 24.41263 ?  212 LYS   B CG    1 
ATOM   3549 C CD    . LYS   B 1 232 ? -26.45500 26.66700  35.67000 1.000 29.56884 ?  212 LYS   B CD    1 
ATOM   3550 C CE    . LYS   B 1 232 ? -27.13400 26.79400  37.00600 1.000 40.97842 ?  212 LYS   B CE    1 
ATOM   3551 N N     . GLU   B 1 233 ? -22.46000 23.40000  33.56100 1.000 24.97225 ?  213 GLU   B N     1 
ATOM   3552 C CA    . GLU   B 1 233 ? -21.28700 23.37200  32.69300 1.000 25.22647 ?  213 GLU   B CA    1 
ATOM   3553 C C     . GLU   B 1 233 ? -21.31200 22.15100  31.78600 1.000 28.70409 ?  213 GLU   B C     1 
ATOM   3554 O O     . GLU   B 1 233 ? -20.93100 22.23000  30.61700 1.000 28.51686 ?  213 GLU   B O     1 
ATOM   3555 C CB    . GLU   B 1 233 ? -19.99900 23.38500  33.51700 1.000 27.74786 ?  213 GLU   B CB    1 
ATOM   3556 N N     . ILE   B 1 234 ? -21.76800 21.01000  32.29600 1.000 24.73931 ?  214 ILE   B N     1 
ATOM   3557 C CA    . ILE   B 1 234 ? -21.77800 19.81600  31.45900 1.000 24.48424 ?  214 ILE   B CA    1 
ATOM   3558 C C     . ILE   B 1 234 ? -22.94100 19.85900  30.47400 1.000 30.25486 ?  214 ILE   B C     1 
ATOM   3559 O O     . ILE   B 1 234 ? -22.78300 19.54400  29.28500 1.000 31.70093 ?  214 ILE   B O     1 
ATOM   3560 C CB    . ILE   B 1 234 ? -21.82800 18.54800  32.33900 1.000 23.26721 ?  214 ILE   B CB    1 
ATOM   3561 C CG1   . ILE   B 1 234 ? -20.53100 18.38100  33.13100 1.000 27.52628 ?  214 ILE   B CG1   1 
ATOM   3562 C CG2   . ILE   B 1 234 ? -22.11200 17.30900  31.49500 1.000 25.74534 ?  214 ILE   B CG2   1 
ATOM   3563 C CD1   . ILE   B 1 234 ? -20.65300 17.33800  34.23300 1.000 28.89179 ?  214 ILE   B CD1   1 
ATOM   3564 N N     . LEU   B 1 235 ? -24.12000 20.24700  30.94900 1.000 25.25801 ?  215 LEU   B N     1 
ATOM   3565 C CA    . LEU   B 1 235 ? -25.35000 20.01000  30.21100 1.000 25.47597 ?  215 LEU   B CA    1 
ATOM   3566 C C     . LEU   B 1 235 ? -25.74700 21.17500  29.32200 1.000 25.44429 ?  215 LEU   B C     1 
ATOM   3567 O O     . LEU   B 1 235 ? -26.50600 20.97200  28.36800 1.000 27.48549 ?  215 LEU   B O     1 
ATOM   3568 C CB    . LEU   B 1 235 ? -26.50200 19.69300  31.18600 1.000 25.61126 ?  215 LEU   B CB    1 
ATOM   3569 C CG    . LEU   B 1 235 ? -26.35000 18.39700  31.99200 1.000 23.71717 ?  215 LEU   B CG    1 
ATOM   3570 C CD1   . LEU   B 1 235 ? -27.43800 18.23000  33.06000 1.000 22.43379 ?  215 LEU   B CD1   1 
ATOM   3571 C CD2   . LEU   B 1 235 ? -26.39600 17.20000  31.02500 1.000 23.50566 ?  215 LEU   B CD2   1 
ATOM   3572 N N     . GLU   B 1 236 ? -25.24600 22.38100  29.58600 1.000 23.16338 ?  216 GLU   B N     1 
ATOM   3573 C CA    . GLU   B 1 236 ? -25.77900 23.49600  28.80800 1.000 29.07052 ?  216 GLU   B CA    1 
ATOM   3574 C C     . GLU   B 1 236 ? -25.29600 23.51300  27.36000 1.000 31.99232 ?  216 GLU   B C     1 
ATOM   3575 O O     . GLU   B 1 236 ? -25.80900 24.32100  26.57300 1.000 31.24131 ?  216 GLU   B O     1 
ATOM   3576 C CB    . GLU   B 1 236 ? -25.47000 24.81700  29.52100 1.000 27.03187 ?  216 GLU   B CB    1 
ATOM   3577 C CG    . GLU   B 1 236 ? -26.49700 25.05600  30.61900 1.000 33.33340 ?  216 GLU   B CG    1 
ATOM   3578 C CD    . GLU   B 1 236 ? -26.33000 26.37200  31.34800 1.000 41.29819 ?  216 GLU   B CD    1 
ATOM   3579 O OE1   . GLU   B 1 236 ? -25.21900 26.95400  31.32100 1.000 46.70773 ?  216 GLU   B OE1   1 
ATOM   3580 O OE2   . GLU   B 1 236 ? -27.32300 26.80600  31.95800 1.000 42.41057 -1 216 GLU   B OE2   1 
ATOM   3581 N N     . ILE   B 1 237 ? -24.34900 22.63800  26.99500 1.000 32.11469 ?  217 ILE   B N     1 
ATOM   3582 C CA    . ILE   B 1 237 ? -24.01100 22.40800  25.59000 1.000 33.82309 ?  217 ILE   B CA    1 
ATOM   3583 C C     . ILE   B 1 237 ? -25.25000 21.98600  24.80200 1.000 45.02050 ?  217 ILE   B C     1 
ATOM   3584 O O     . ILE   B 1 237 ? -25.50700 22.48200  23.69700 1.000 34.83571 ?  217 ILE   B O     1 
ATOM   3585 C CB    . ILE   B 1 237 ? -22.89300 21.35600  25.47900 1.000 37.05986 ?  217 ILE   B CB    1 
ATOM   3586 C CG1   . ILE   B 1 237 ? -21.71900 21.72300  26.39400 1.000 49.01349 ?  217 ILE   B CG1   1 
ATOM   3587 C CG2   . ILE   B 1 237 ? -22.46300 21.16400  24.02000 1.000 35.09307 ?  217 ILE   B CG2   1 
ATOM   3588 N N     . HIS   B 1 238 ? -26.04400 21.06600  25.35800 1.000 30.16995 ?  218 HIS   B N     1 
ATOM   3589 C CA    . HIS   B 1 238 ? -27.19100 20.51600  24.64500 1.000 28.49237 ?  218 HIS   B CA    1 
ATOM   3590 C C     . HIS   B 1 238 ? -28.53300 20.72700  25.33200 1.000 30.93516 ?  218 HIS   B C     1 
ATOM   3591 O O     . HIS   B 1 238 ? -29.56100 20.35300  24.75700 1.000 33.70279 ?  218 HIS   B O     1 
ATOM   3592 C CB    . HIS   B 1 238 ? -26.97100 19.02000  24.40100 1.000 31.15130 ?  218 HIS   B CB    1 
ATOM   3593 C CG    . HIS   B 1 238 ? -25.82900 18.73500  23.47900 1.000 37.09116 ?  218 HIS   B CG    1 
ATOM   3594 N ND1   . HIS   B 1 238 ? -24.66000 18.14400  23.90500 1.000 40.11250 ?  218 HIS   B ND1   1 
ATOM   3595 C CD2   . HIS   B 1 238 ? -25.67500 18.96600  22.15400 1.000 40.36626 ?  218 HIS   B CD2   1 
ATOM   3596 C CE1   . HIS   B 1 238 ? -23.83700 18.01400  22.87900 1.000 41.43816 ?  218 HIS   B CE1   1 
ATOM   3597 N NE2   . HIS   B 1 238 ? -24.43100 18.49900  21.80400 1.000 41.31855 ?  218 HIS   B NE2   1 
ATOM   3598 N N     . PHE   B 1 239 ? -28.56900 21.32500  26.51800 1.000 28.50657 ?  219 PHE   B N     1 
ATOM   3599 C CA    . PHE   B 1 239 ? -29.80200 21.49300  27.27300 1.000 26.86339 ?  219 PHE   B CA    1 
ATOM   3600 C C     . PHE   B 1 239 ? -29.94600 22.92500  27.75300 1.000 23.80203 ?  219 PHE   B C     1 
ATOM   3601 O O     . PHE   B 1 239 ? -28.96400 23.63700  27.95100 1.000 30.01714 ?  219 PHE   B O     1 
ATOM   3602 C CB    . PHE   B 1 239 ? -29.86300 20.60400  28.53500 1.000 24.87967 ?  219 PHE   B CB    1 
ATOM   3603 C CG    . PHE   B 1 239 ? -29.86800 19.12000  28.26300 1.000 22.00192 ?  219 PHE   B CG    1 
ATOM   3604 C CD1   . PHE   B 1 239 ? -28.68000 18.42100  28.09500 1.000 24.00626 ?  219 PHE   B CD1   1 
ATOM   3605 C CD2   . PHE   B 1 239 ? -31.05600 18.42600  28.23100 1.000 22.55719 ?  219 PHE   B CD2   1 
ATOM   3606 C CE1   . PHE   B 1 239 ? -28.68200 17.05400  27.87600 1.000 26.80402 ?  219 PHE   B CE1   1 
ATOM   3607 C CE2   . PHE   B 1 239 ? -31.07400 17.05700  28.01500 1.000 26.07628 ?  219 PHE   B CE2   1 
ATOM   3608 C CZ    . PHE   B 1 239 ? -29.89600 16.36200  27.83500 1.000 27.31863 ?  219 PHE   B CZ    1 
ATOM   3609 N N     . GLU   B 1 240 ? -31.19000 23.30500  28.02900 1.000 23.96093 ?  220 GLU   B N     1 
ATOM   3610 C CA    . GLU   B 1 240 ? -31.50200 24.49900  28.80200 1.000 24.49692 ?  220 GLU   B CA    1 
ATOM   3611 C C     . GLU   B 1 240 ? -32.05000 24.06900  30.16100 1.000 28.00480 ?  220 GLU   B C     1 
ATOM   3612 O O     . GLU   B 1 240 ? -32.89200 23.15800  30.23800 1.000 24.43933 ?  220 GLU   B O     1 
ATOM   3613 C CB    . GLU   B 1 240 ? -32.52500 25.36700  28.06900 1.000 29.34711 ?  220 GLU   B CB    1 
ATOM   3614 C CG    . GLU   B 1 240 ? -33.36300 26.25000  28.94900 1.000 45.49559 ?  220 GLU   B CG    1 
ATOM   3615 C CD    . GLU   B 1 240 ? -34.46400 26.96100  28.16900 1.000 62.61746 ?  220 GLU   B CD    1 
ATOM   3616 O OE1   . GLU   B 1 240 ? -34.85800 26.45200  27.09200 1.000 55.98480 ?  220 GLU   B OE1   1 
ATOM   3617 O OE2   . GLU   B 1 240 ? -34.93900 28.01800  28.64000 1.000 71.28754 -1 220 GLU   B OE2   1 
ATOM   3618 N N     . LEU   B 1 241 ? -31.56100 24.70400  31.22200 1.000 24.02458 ?  221 LEU   B N     1 
ATOM   3619 C CA    . LEU   B 1 241 ? -32.08900 24.46900  32.55800 1.000 23.56535 ?  221 LEU   B CA    1 
ATOM   3620 C C     . LEU   B 1 241 ? -33.42100 25.19300  32.70500 1.000 28.38987 ?  221 LEU   B C     1 
ATOM   3621 O O     . LEU   B 1 241 ? -33.48000 26.42500  32.61200 1.000 28.04645 ?  221 LEU   B O     1 
ATOM   3622 C CB    . LEU   B 1 241 ? -31.10200 24.93400  33.62600 1.000 25.33350 ?  221 LEU   B CB    1 
ATOM   3623 C CG    . LEU   B 1 241 ? -31.62400 24.76500  35.06000 1.000 24.20133 ?  221 LEU   B CG    1 
ATOM   3624 C CD1   . LEU   B 1 241 ? -31.93900 23.29300  35.39400 1.000 22.92127 ?  221 LEU   B CD1   1 
ATOM   3625 C CD2   . LEU   B 1 241 ? -30.65500 25.34900  36.07200 1.000 30.36115 ?  221 LEU   B CD2   1 
ATOM   3626 N N     . VAL   B 1 242 ? -34.47900 24.42400  32.94400 1.000 27.04758 ?  222 VAL   B N     1 
ATOM   3627 C CA    . VAL   B 1 242 ? -35.85100 24.92200  32.96900 1.000 28.03721 ?  222 VAL   B CA    1 
ATOM   3628 C C     . VAL   B 1 242 ? -36.33100 25.21000  34.39100 1.000 36.61427 ?  222 VAL   B C     1 
ATOM   3629 O O     . VAL   B 1 242 ? -37.04000 26.18700  34.62900 1.000 29.37461 ?  222 VAL   B O     1 
ATOM   3630 C CB    . VAL   B 1 242 ? -36.75900 23.88800  32.26000 1.000 33.98697 ?  222 VAL   B CB    1 
ATOM   3631 C CG1   . VAL   B 1 242 ? -38.21000 24.07600  32.64000 1.000 44.34742 ?  222 VAL   B CG1   1 
ATOM   3632 C CG2   . VAL   B 1 242 ? -36.57400 23.99200  30.75200 1.000 42.91283 ?  222 VAL   B CG2   1 
ATOM   3633 N N     . ALA   B 1 243 ? -35.96100 24.38500  35.36400 1.000 24.17637 ?  223 ALA   B N     1 
ATOM   3634 C CA    . ALA   B 1 243 ? -36.55700 24.52800  36.68900 1.000 23.30354 ?  223 ALA   B CA    1 
ATOM   3635 C C     . ALA   B 1 243 ? -35.72900 23.74400  37.69500 1.000 26.61391 ?  223 ALA   B C     1 
ATOM   3636 O O     . ALA   B 1 243 ? -35.06600 22.76500  37.33800 1.000 22.37758 ?  223 ALA   B O     1 
ATOM   3637 C CB    . ALA   B 1 243 ? -38.00700 24.01800  36.71400 1.000 24.30209 ?  223 ALA   B CB    1 
ATOM   3638 N N     . THR   B 1 244 ? -35.79600 24.17200  38.95600 1.000 22.35409 ?  224 THR   B N     1 
ATOM   3639 C CA    . THR   B 1 244 ? -35.22000 23.41300  40.06200 1.000 21.88931 ?  224 THR   B CA    1 
ATOM   3640 C C     . THR   B 1 244 ? -36.23900 23.39700  41.18500 1.000 26.80886 ?  224 THR   B C     1 
ATOM   3641 O O     . THR   B 1 244 ? -37.06500 24.30400  41.30300 1.000 27.15416 ?  224 THR   B O     1 
ATOM   3642 C CB    . THR   B 1 244 ? -33.90200 23.98900  40.63100 1.000 24.32823 ?  224 THR   B CB    1 
ATOM   3643 O OG1   . THR   B 1 244 ? -34.08200 25.36300  40.99600 1.000 30.39632 ?  224 THR   B OG1   1 
ATOM   3644 C CG2   . THR   B 1 244 ? -32.77000 23.89800  39.60900 1.000 25.61251 ?  224 THR   B CG2   1 
ATOM   3645 N N     . GLU   B 1 245 ? -36.16700 22.36600  42.02100 1.000 20.18025 ?  225 GLU   B N     1 
ATOM   3646 C CA    . GLU   B 1 245 ? -37.13300 22.19200  43.08900 1.000 22.50315 ?  225 GLU   B CA    1 
ATOM   3647 C C     . GLU   B 1 245 ? -36.49700 21.27800  44.12800 1.000 27.56223 ?  225 GLU   B C     1 
ATOM   3648 O O     . GLU   B 1 245 ? -35.77100 20.35000  43.76900 1.000 23.66170 ?  225 GLU   B O     1 
ATOM   3649 C CB    . GLU   B 1 245 ? -38.40100 21.54400  42.52500 1.000 32.28067 ?  225 GLU   B CB    1 
ATOM   3650 C CG    . GLU   B 1 245 ? -39.65100 21.71300  43.30300 1.000 47.22001 ?  225 GLU   B CG    1 
ATOM   3651 C CD    . GLU   B 1 245 ? -40.80000 20.96200  42.64300 1.000 46.35111 ?  225 GLU   B CD    1 
ATOM   3652 O OE1   . GLU   B 1 245 ? -40.84600 20.89300  41.38700 1.000 43.63540 ?  225 GLU   B OE1   1 
ATOM   3653 O OE2   . GLU   B 1 245 ? -41.64700 20.41900  43.38100 1.000 52.64841 -1 225 GLU   B OE2   1 
ATOM   3654 N N     . ASP   B 1 246 ? -36.80200 21.51400  45.39600 1.000 20.37548 ?  226 ASP   B N     1 
ATOM   3655 C CA    . ASP   B 1 246 ? -36.32600 20.64100  46.47800 1.000 21.04607 ?  226 ASP   B CA    1 
ATOM   3656 C C     . ASP   B 1 246 ? -37.39800 19.60100  46.81800 1.000 25.26567 ?  226 ASP   B C     1 
ATOM   3657 O O     . ASP   B 1 246 ? -38.58000 19.93900  46.97500 1.000 23.21125 ?  226 ASP   B O     1 
ATOM   3658 C CB    . ASP   B 1 246 ? -35.99800 21.46700  47.72200 1.000 25.35368 ?  226 ASP   B CB    1 
ATOM   3659 C CG    . ASP   B 1 246 ? -34.59600 22.08800  47.68500 1.000 29.31350 ?  226 ASP   B CG    1 
ATOM   3660 O OD1   . ASP   B 1 246 ? -33.75100 21.76900  46.80800 1.000 24.51164 ?  226 ASP   B OD1   1 
ATOM   3661 O OD2   . ASP   B 1 246 ? -34.33400 22.90600  48.58200 1.000 45.05364 -1 226 ASP   B OD2   1 
ATOM   3662 N N     . ILE   B 1 247 ? -36.99700 18.33000  46.95400 1.000 21.51815 ?  227 ILE   B N     1 
ATOM   3663 C CA    . ILE   B 1 247 ? -37.92800 17.24300  47.21400 1.000 18.24890 ?  227 ILE   B CA    1 
ATOM   3664 C C     . ILE   B 1 247 ? -37.39500 16.40700  48.37100 1.000 18.15459 ?  227 ILE   B C     1 
ATOM   3665 O O     . ILE   B 1 247 ? -36.33000 15.79800  48.25100 1.000 20.44861 ?  227 ILE   B O     1 
ATOM   3666 C CB    . ILE   B 1 247 ? -38.15300 16.34300  45.98700 1.000 19.77279 ?  227 ILE   B CB    1 
ATOM   3667 C CG1   . ILE   B 1 247 ? -38.48000 17.15400  44.71900 1.000 23.57582 ?  227 ILE   B CG1   1 
ATOM   3668 C CG2   . ILE   B 1 247 ? -39.24000 15.27500  46.30100 1.000 22.26204 ?  227 ILE   B CG2   1 
ATOM   3669 C CD1   . ILE   B 1 247 ? -38.64000 16.25600  43.51200 1.000 23.25957 ?  227 ILE   B CD1   1 
ATOM   3670 N N     . PRO   B 1 248 ? -38.09100 16.33600  49.49900 1.000 17.94257 ?  228 PRO   B N     1 
ATOM   3671 C CA    . PRO   B 1 248 ? -37.60700 15.52900  50.63000 1.000 18.24195 ?  228 PRO   B CA    1 
ATOM   3672 C C     . PRO   B 1 248 ? -37.91600 14.05400  50.44000 1.000 20.10919 ?  228 PRO   B C     1 
ATOM   3673 O O     . PRO   B 1 248 ? -38.83800 13.66100  49.72400 1.000 19.16700 ?  228 PRO   B O     1 
ATOM   3674 C CB    . PRO   B 1 248 ? -38.40100 16.07500  51.81600 1.000 23.89950 ?  228 PRO   B CB    1 
ATOM   3675 C CG    . PRO   B 1 248 ? -39.72500 16.50500  51.17700 1.000 26.82647 ?  228 PRO   B CG    1 
ATOM   3676 C CD    . PRO   B 1 248 ? -39.35500 17.03200  49.81000 1.000 20.70857 ?  228 PRO   B CD    1 
ATOM   3677 N N     . PHE   B 1 249 ? -37.13900 13.22200  51.13400 1.000 18.59355 ?  229 PHE   B N     1 
ATOM   3678 C CA    . PHE   B 1 249 ? -37.47400 11.80600  51.22200 1.000 19.53152 ?  229 PHE   B CA    1 
ATOM   3679 C C     . PHE   B 1 249 ? -36.99400 11.28000  52.56300 1.000 17.85656 ?  229 PHE   B C     1 
ATOM   3680 O O     . PHE   B 1 249 ? -36.14100 11.88300  53.21300 1.000 18.92938 ?  229 PHE   B O     1 
ATOM   3681 C CB    . PHE   B 1 249 ? -36.89000 11.00200  50.04400 1.000 18.07032 ?  229 PHE   B CB    1 
ATOM   3682 C CG    . PHE   B 1 249 ? -35.38600 10.95900  49.97800 1.000 21.39974 ?  229 PHE   B CG    1 
ATOM   3683 C CD1   . PHE   B 1 249 ? -34.66200 9.98000   50.66000 1.000 22.54331 ?  229 PHE   B CD1   1 
ATOM   3684 C CD2   . PHE   B 1 249 ? -34.69600 11.84700  49.17900 1.000 23.03676 ?  229 PHE   B CD2   1 
ATOM   3685 C CE1   . PHE   B 1 249 ? -33.27800 9.91100   50.55800 1.000 25.51762 ?  229 PHE   B CE1   1 
ATOM   3686 C CE2   . PHE   B 1 249 ? -33.29600 11.79900  49.08500 1.000 25.73922 ?  229 PHE   B CE2   1 
ATOM   3687 C CZ    . PHE   B 1 249 ? -32.59400 10.81000  49.76800 1.000 25.06217 ?  229 PHE   B CZ    1 
ATOM   3688 N N     . VAL   B 1 250 ? -37.56800 10.14000  52.97500 1.000 18.34567 ?  230 VAL   B N     1 
ATOM   3689 C CA    . VAL   B 1 250 ? -37.28900 9.54500   54.27100 1.000 17.43567 ?  230 VAL   B CA    1 
ATOM   3690 C C     . VAL   B 1 250 ? -37.04300 8.06000   54.05400 1.000 20.22745 ?  230 VAL   B C     1 
ATOM   3691 O O     . VAL   B 1 250 ? -37.87300 7.37700   53.43300 1.000 20.00156 ?  230 VAL   B O     1 
ATOM   3692 C CB    . VAL   B 1 250 ? -38.45300 9.73000   55.25800 1.000 18.18924 ?  230 VAL   B CB    1 
ATOM   3693 C CG1   . VAL   B 1 250 ? -38.15400 9.00600   56.56600 1.000 21.18960 ?  230 VAL   B CG1   1 
ATOM   3694 C CG2   . VAL   B 1 250 ? -38.73700 11.22100  55.49700 1.000 18.74153 ?  230 VAL   B CG2   1 
ATOM   3695 N N     . ILE   B 1 251 ? -35.91500 7.56800   54.56000 1.000 17.83516 ?  231 ILE   B N     1 
ATOM   3696 C CA    . ILE   B 1 251 ? -35.55000 6.14400   54.48700 1.000 21.68364 ?  231 ILE   B CA    1 
ATOM   3697 C C     . ILE   B 1 251 ? -35.48600 5.56900   55.89600 1.000 23.66720 ?  231 ILE   B C     1 
ATOM   3698 O O     . ILE   B 1 251 ? -34.83200 6.13800   56.77300 1.000 20.23406 ?  231 ILE   B O     1 
ATOM   3699 C CB    . ILE   B 1 251 ? -34.20000 5.93600   53.77500 1.000 23.06366 ?  231 ILE   B CB    1 
ATOM   3700 C CG1   . ILE   B 1 251 ? -34.28700 6.47200   52.36300 1.000 25.10361 ?  231 ILE   B CG1   1 
ATOM   3701 C CG2   . ILE   B 1 251 ? -33.78900 4.40100   53.79100 1.000 22.07670 ?  231 ILE   B CG2   1 
ATOM   3702 C CD1   . ILE   B 1 251 ? -32.96000 6.41000   51.60600 1.000 36.72189 ?  231 ILE   B CD1   1 
ATOM   3703 N N     . ARG   B 1 252 ? -36.14600 4.43500   56.10500 1.000 21.37972 ?  232 ARG   B N     1 
ATOM   3704 C CA    . ARG   B 1 252 ? -36.13600 3.78700   57.41000 1.000 21.62037 ?  232 ARG   B CA    1 
ATOM   3705 C C     . ARG   B 1 252 ? -34.88300 2.93100   57.58200 1.000 28.58695 ?  232 ARG   B C     1 
ATOM   3706 O O     . ARG   B 1 252 ? -34.58600 2.06300   56.75400 1.000 27.55707 ?  232 ARG   B O     1 
ATOM   3707 C CB    . ARG   B 1 252 ? -37.39400 2.92500   57.57100 1.000 21.16753 ?  232 ARG   B CB    1 
ATOM   3708 C CG    . ARG   B 1 252 ? -37.45000 2.16200   58.90000 1.000 23.96261 ?  232 ARG   B CG    1 
ATOM   3709 C CD    . ARG   B 1 252 ? -38.67100 1.21900   58.94400 1.000 24.40199 ?  232 ARG   B CD    1 
ATOM   3710 N NE    . ARG   B 1 252 ? -39.91100 1.91100   59.27200 1.000 24.06152 ?  232 ARG   B NE    1 
ATOM   3711 C CZ    . ARG   B 1 252 ? -40.83800 2.28400   58.39100 1.000 49.25211 ?  232 ARG   B CZ    1 
ATOM   3712 N NH1   . ARG   B 1 252 ? -40.68300 2.08700   57.08200 1.000 29.43220 ?  232 ARG   B NH1   1 
ATOM   3713 N NH2   . ARG   B 1 252 ? -41.94900 2.87700   58.83500 1.000 48.54639 ?  232 ARG   B NH2   1 
ATOM   3714 N N     . GLU   B 1 253 ? -34.15400 3.16800   58.66400 1.000 18.80757 ?  233 GLU   B N     1 
ATOM   3715 C CA    . GLU   B 1 253 ? -32.97000 2.38900   58.99500 1.000 19.40073 ?  233 GLU   B CA    1 
ATOM   3716 C C     . GLU   B 1 253 ? -33.21900 1.39200   60.10700 1.000 22.20262 ?  233 GLU   B C     1 
ATOM   3717 O O     . GLU   B 1 253 ? -32.72600 0.26200   60.04000 1.000 20.36125 ?  233 GLU   B O     1 
ATOM   3718 C CB    . GLU   B 1 253 ? -31.84200 3.34400   59.38600 1.000 21.20653 ?  233 GLU   B CB    1 
ATOM   3719 C CG    . GLU   B 1 253 ? -31.44000 4.13300   58.14400 1.000 29.32667 ?  233 GLU   B CG    1 
ATOM   3720 C CD    . GLU   B 1 253 ? -30.44900 5.24400   58.42300 1.000 44.52971 ?  233 GLU   B CD    1 
ATOM   3721 O OE1   . GLU   B 1 253 ? -30.26100 5.56800   59.60900 1.000 52.04233 ?  233 GLU   B OE1   1 
ATOM   3722 O OE2   . GLU   B 1 253 ? -29.88100 5.80200   57.45800 1.000 43.40428 -1 233 GLU   B OE2   1 
ATOM   3723 N N     . THR   B 1 254 ? -33.98800 1.78100   61.12400 1.000 20.42683 ?  234 THR   B N     1 
ATOM   3724 C CA    . THR   B 1 254 ? -34.41700 0.89900   62.21600 1.000 23.74101 ?  234 THR   B CA    1 
ATOM   3725 C C     . THR   B 1 254 ? -35.88800 1.18300   62.51700 1.000 20.44129 ?  234 THR   B C     1 
ATOM   3726 O O     . THR   B 1 254 ? -36.54900 1.95800   61.82500 1.000 24.79029 ?  234 THR   B O     1 
ATOM   3727 C CB    . THR   B 1 254 ? -33.54500 1.08700   63.47300 1.000 22.32432 ?  234 THR   B CB    1 
ATOM   3728 O OG1   . THR   B 1 254 ? -33.92800 2.32000   64.10400 1.000 19.90340 ?  234 THR   B OG1   1 
ATOM   3729 C CG2   . THR   B 1 254 ? -32.04800 1.08700   63.16800 1.000 23.53743 ?  234 THR   B CG2   1 
ATOM   3730 N N     . SER   B 1 255 ? -36.39100 0.59600   63.60000 1.000 21.06458 ?  235 SER   B N     1 
ATOM   3731 C CA    . SER   B 1 255 ? -37.72700 0.92800   64.07300 1.000 23.27698 ?  235 SER   B CA    1 
ATOM   3732 C C     . SER   B 1 255 ? -37.84100 2.41500   64.42200 1.000 22.12630 ?  235 SER   B C     1 
ATOM   3733 O O     . SER   B 1 255 ? -38.93100 2.99300   64.33400 1.000 24.76038 ?  235 SER   B O     1 
ATOM   3734 C CB    . SER   B 1 255 ? -38.05300 0.05900   65.29100 1.000 27.44645 ?  235 SER   B CB    1 
ATOM   3735 O OG    . SER   B 1 255 ? -37.05000 0.25200   66.30000 1.000 34.34856 ?  235 SER   B OG    1 
ATOM   3736 N N     . ARG   B 1 256 ? -36.73000 3.05500   64.80400 1.000 19.09431 ?  236 ARG   B N     1 
ATOM   3737 C CA    . ARG   B 1 256 ? -36.76600 4.43400   65.31600 1.000 19.18777 ?  236 ARG   B CA    1 
ATOM   3738 C C     . ARG   B 1 256 ? -35.88200 5.41700   64.57400 1.000 20.43216 ?  236 ARG   B C     1 
ATOM   3739 O O     . ARG   B 1 256 ? -36.08500 6.62600   64.73300 1.000 20.81714 ?  236 ARG   B O     1 
ATOM   3740 C CB    . ARG   B 1 256 ? -36.35500 4.46300   66.80300 1.000 23.81731 ?  236 ARG   B CB    1 
ATOM   3741 C CG    . ARG   B 1 256 ? -37.32400 3.70600   67.67400 1.000 23.23673 ?  236 ARG   B CG    1 
ATOM   3742 C CD    . ARG   B 1 256 ? -36.95100 3.69000   69.15400 1.000 18.46834 ?  236 ARG   B CD    1 
ATOM   3743 N NE    . ARG   B 1 256 ? -38.09600 3.30400   69.98800 1.000 21.85101 ?  236 ARG   B NE    1 
ATOM   3744 C CZ    . ARG   B 1 256 ? -38.98100 4.14800   70.51100 1.000 27.36713 ?  236 ARG   B CZ    1 
ATOM   3745 N NH1   . ARG   B 1 256 ? -38.84600 5.46400   70.38600 1.000 23.69392 ?  236 ARG   B NH1   1 
ATOM   3746 N NH2   . ARG   B 1 256 ? -40.02000 3.66100   71.19800 1.000 24.50416 ?  236 ARG   B NH2   1 
ATOM   3747 N N     . LYS   B 1 257 ? -34.90200 4.91400   63.82500 1.000 18.25365 ?  237 LYS   B N     1 
ATOM   3748 C CA    . LYS   B 1 257 ? -33.91200 5.77900   63.14200 1.000 20.55104 ?  237 LYS   B CA    1 
ATOM   3749 C C     . LYS   B 1 257 ? -34.20100 5.87600   61.64400 1.000 20.93108 ?  237 LYS   B C     1 
ATOM   3750 O O     . LYS   B 1 257 ? -34.41300 4.85000   61.00500 1.000 20.08333 ?  237 LYS   B O     1 
ATOM   3751 C CB    . LYS   B 1 257 ? -32.49500 5.23900   63.33500 1.000 19.25950 ?  237 LYS   B CB    1 
ATOM   3752 C CG    . LYS   B 1 257 ? -31.37700 6.04600   62.69500 1.000 20.98997 ?  237 LYS   B CG    1 
ATOM   3753 C CD    . LYS   B 1 257 ? -30.13400 6.06400   63.54300 1.000 33.12869 ?  237 LYS   B CD    1 
ATOM   3754 C CE    . LYS   B 1 257 ? -28.86400 5.74100   62.78900 1.000 38.00623 ?  237 LYS   B CE    1 
ATOM   3755 N NZ    . LYS   B 1 257 ? -28.70800 6.56800   61.57500 1.000 29.03853 ?  237 LYS   B NZ    1 
ATOM   3756 N N     . PHE   B 1 258 ? -34.17700 7.10200   61.14700 1.000 16.36965 ?  238 PHE   B N     1 
ATOM   3757 C CA    . PHE   B 1 258 ? -34.48200 7.33600   59.73000 1.000 18.58385 ?  238 PHE   B CA    1 
ATOM   3758 C C     . PHE   B 1 258 ? -33.49700 8.33100   59.12300 1.000 18.25418 ?  238 PHE   B C     1 
ATOM   3759 O O     . PHE   B 1 258 ? -32.89700 9.11200   59.85400 1.000 18.85199 ?  238 PHE   B O     1 
ATOM   3760 C CB    . PHE   B 1 258 ? -35.87900 7.93600   59.59200 1.000 18.39377 ?  238 PHE   B CB    1 
ATOM   3761 C CG    . PHE   B 1 258 ? -37.01700 7.09300   60.11000 1.000 20.86639 ?  238 PHE   B CG    1 
ATOM   3762 C CD1   . PHE   B 1 258 ? -37.31500 7.04800   61.46000 1.000 21.44840 ?  238 PHE   B CD1   1 
ATOM   3763 C CD2   . PHE   B 1 258 ? -37.81400 6.37000   59.23900 1.000 20.96394 ?  238 PHE   B CD2   1 
ATOM   3764 C CE1   . PHE   B 1 258 ? -38.36100 6.27400   61.93300 1.000 21.72065 ?  238 PHE   B CE1   1 
ATOM   3765 C CE2   . PHE   B 1 258 ? -38.86300 5.60100   59.71100 1.000 20.89269 ?  238 PHE   B CE2   1 
ATOM   3766 C CZ    . PHE   B 1 258 ? -39.13300 5.55400   61.05600 1.000 25.47795 ?  238 PHE   B CZ    1 
ATOM   3767 N N     . GLN   B 1 259 ? -33.33500 8.25200   57.81300 1.000 18.94741 ?  239 GLN   B N     1 
ATOM   3768 C CA    . GLN   B 1 259 ? -32.55400 9.27900   57.10000 1.000 17.76271 ?  239 GLN   B CA    1 
ATOM   3769 C C     . GLN   B 1 259 ? -33.59700 10.20700  56.47500 1.000 18.43486 ?  239 GLN   B C     1 
ATOM   3770 O O     . GLN   B 1 259 ? -34.52500 9.69600   55.86000 1.000 19.13371 ?  239 GLN   B O     1 
ATOM   3771 C CB    . GLN   B 1 259 ? -31.66200 8.67400   56.02200 1.000 20.85392 ?  239 GLN   B CB    1 
ATOM   3772 C CG    . GLN   B 1 259 ? -30.90200 9.71600   55.21800 1.000 22.33113 ?  239 GLN   B CG    1 
ATOM   3773 C CD    . GLN   B 1 259 ? -30.29400 9.18200   53.94400 1.000 27.69030 ?  239 GLN   B CD    1 
ATOM   3774 O OE1   . GLN   B 1 259 ? -30.19200 9.88600   52.94300 1.000 28.20000 ?  239 GLN   B OE1   1 
ATOM   3775 N NE2   . GLN   B 1 259 ? -29.87200 7.93000   53.97600 1.000 29.88766 ?  239 GLN   B NE2   1 
ATOM   3776 N N     . HIS   B 1 260 ? -33.45800 11.50600  56.69200 1.000 16.62097 ?  240 HIS   B N     1 
ATOM   3777 C CA    . HIS   B 1 260 ? -34.41000 12.50200  56.15000 1.000 18.28237 ?  240 HIS   B CA    1 
ATOM   3778 C C     . HIS   B 1 260 ? -33.55100 13.41900  55.28900 1.000 17.94687 ?  240 HIS   B C     1 
ATOM   3779 O O     . HIS   B 1 260 ? -32.70000 14.12200  55.82800 1.000 19.06408 ?  240 HIS   B O     1 
ATOM   3780 C CB    . HIS   B 1 260 ? -35.13800 13.19900  57.29700 1.000 19.54978 ?  240 HIS   B CB    1 
ATOM   3781 C CG    . HIS   B 1 260 ? -36.32000 13.99600  56.89600 1.000 20.84330 ?  240 HIS   B CG    1 
ATOM   3782 N ND1   . HIS   B 1 260 ? -37.28000 14.37900  57.80300 1.000 24.74594 ?  240 HIS   B ND1   1 
ATOM   3783 C CD2   . HIS   B 1 260 ? -36.69600 14.48600  55.71800 1.000 23.71328 ?  240 HIS   B CD2   1 
ATOM   3784 C CE1   . HIS   B 1 260 ? -38.20600 15.07800  57.17300 1.000 30.68743 ?  240 HIS   B CE1   1 
ATOM   3785 N NE2   . HIS   B 1 260 ? -37.86900 15.15400  55.90800 1.000 22.78448 ?  240 HIS   B NE2   1 
ATOM   3786 N N     . THR   B 1 261 ? -33.76900 13.37000  53.98900 1.000 17.10662 ?  241 THR   B N     1 
ATOM   3787 C CA    . THR   B 1 261 ? -32.85000 14.08400  53.07900 1.000 17.74534 ?  241 THR   B CA    1 
ATOM   3788 C C     . THR   B 1 261 ? -33.64300 14.93600  52.08600 1.000 18.87584 ?  241 THR   B C     1 
ATOM   3789 O O     . THR   B 1 261 ? -34.77700 14.59400  51.78100 1.000 19.84766 ?  241 THR   B O     1 
ATOM   3790 C CB    . THR   B 1 261 ? -31.90400 13.05300  52.43700 1.000 19.61146 ?  241 THR   B CB    1 
ATOM   3791 O OG1   . THR   B 1 261 ? -31.15900 12.41100  53.46700 1.000 20.84663 ?  241 THR   B OG1   1 
ATOM   3792 C CG2   . THR   B 1 261 ? -30.95500 13.64800  51.42100 1.000 20.36086 ?  241 THR   B CG2   1 
ATOM   3793 N N     . ILE   B 1 262 ? -33.01300 16.00800  51.61700 1.000 19.46809 ?  242 ILE   B N     1 
ATOM   3794 C CA    . ILE   B 1 262 ? -33.66400 16.91700  50.64000 1.000 15.88688 ?  242 ILE   B CA    1 
ATOM   3795 C C     . ILE   B 1 262 ? -32.88800 16.87000  49.31900 1.000 18.52536 ?  242 ILE   B C     1 
ATOM   3796 O O     . ILE   B 1 262 ? -31.80300 17.43400  49.25700 1.000 19.44508 ?  242 ILE   B O     1 
ATOM   3797 C CB    . ILE   B 1 262 ? -33.76100 18.34000  51.21900 1.000 21.37425 ?  242 ILE   B CB    1 
ATOM   3798 C CG1   . ILE   B 1 262 ? -34.32100 18.32700  52.64200 1.000 25.56465 ?  242 ILE   B CG1   1 
ATOM   3799 C CG2   . ILE   B 1 262 ? -34.58100 19.23200  50.30300 1.000 21.26132 ?  242 ILE   B CG2   1 
ATOM   3800 C CD1   . ILE   B 1 262 ? -33.98700 19.55400  53.44100 1.000 36.10361 ?  242 ILE   B CD1   1 
ATOM   3801 N N     . SER   B 1 263 ? -33.44500 16.17700  48.32400 1.000 18.72277 ?  243 SER   B N     1 
ATOM   3802 C CA    . SER   B 1 263 ? -32.81400 16.16400  47.01600 1.000 17.18334 ?  243 SER   B CA    1 
ATOM   3803 C C     . SER   B 1 263 ? -33.17100 17.42900  46.26500 1.000 22.04089 ?  243 SER   B C     1 
ATOM   3804 O O     . SER   B 1 263 ? -34.20400 18.04900  46.52400 1.000 22.11548 ?  243 SER   B O     1 
ATOM   3805 C CB    . SER   B 1 263 ? -33.26900 14.96200  46.17900 1.000 20.67878 ?  243 SER   B CB    1 
ATOM   3806 O OG    . SER   B 1 263 ? -32.48200 13.85400  46.48600 1.000 32.44832 ?  243 SER   B OG    1 
ATOM   3807 N N     . GLN   B 1 264 ? -32.29500 17.83500  45.35700 1.000 17.19449 ?  244 GLN   B N     1 
ATOM   3808 C CA    . GLN   B 1 264 ? -32.64600 18.88700  44.41500 1.000 17.09363 ?  244 GLN   B CA    1 
ATOM   3809 C C     . GLN   B 1 264 ? -32.99000 18.24700  43.07600 1.000 22.03964 ?  244 GLN   B C     1 
ATOM   3810 O O     . GLN   B 1 264 ? -32.18400 17.49300  42.51400 1.000 19.37516 ?  244 GLN   B O     1 
ATOM   3811 C CB    . GLN   B 1 264 ? -31.51200 19.89000  44.24200 1.000 18.00376 ?  244 GLN   B CB    1 
ATOM   3812 C CG    . GLN   B 1 264 ? -31.89900 20.94900  43.18400 1.000 20.69464 ?  244 GLN   B CG    1 
ATOM   3813 C CD    . GLN   B 1 264 ? -30.96700 22.14000  43.21500 1.000 23.77473 ?  244 GLN   B CD    1 
ATOM   3814 O OE1   . GLN   B 1 264 ? -29.81100 22.01200  42.83700 1.000 22.67891 ?  244 GLN   B OE1   1 
ATOM   3815 N NE2   . GLN   B 1 264 ? -31.47500 23.31600  43.64500 1.000 23.91588 ?  244 GLN   B NE2   1 
ATOM   3816 N N     . MET   B 1 265 ? -34.19400 18.52400  42.58000 1.000 18.24736 ?  245 MET   B N     1 
ATOM   3817 C CA    . MET   B 1 265 ? -34.56600 18.18800  41.21300 1.000 19.36232 ?  245 MET   B CA    1 
ATOM   3818 C C     . MET   B 1 265 ? -34.14000 19.29800  40.26400 1.000 21.03339 ?  245 MET   B C     1 
ATOM   3819 O O     . MET   B 1 265 ? -34.39000 20.47600  40.53200 1.000 21.96941 ?  245 MET   B O     1 
ATOM   3820 C CB    . MET   B 1 265 ? -36.07600 17.95600  41.10200 1.000 20.02413 ?  245 MET   B CB    1 
ATOM   3821 C CG    . MET   B 1 265 ? -36.54100 17.62900  39.68300 1.000 23.74558 ?  245 MET   B CG    1 
ATOM   3822 S SD    . MET   B 1 265 ? -38.28900 17.20900  39.56800 1.000 23.00454 ?  245 MET   B SD    1 
ATOM   3823 C CE    . MET   B 1 265 ? -38.18400 15.41800  39.95900 1.000 20.89273 ?  245 MET   B CE    1 
ATOM   3824 N N     . SER   B 1 266 ? -33.50200 18.91300  39.15900 1.000 21.14019 ?  246 SER   B N     1 
ATOM   3825 C CA    . SER   B 1 266 ? -33.21500 19.85800  38.08700 1.000 22.63640 ?  246 SER   B CA    1 
ATOM   3826 C C     . SER   B 1 266 ? -33.77800 19.30500  36.78400 1.000 21.47926 ?  246 SER   B C     1 
ATOM   3827 O O     . SER   B 1 266 ? -33.66100 18.10700  36.49600 1.000 21.34375 ?  246 SER   B O     1 
ATOM   3828 C CB    . SER   B 1 266 ? -31.70600 20.14200  37.94600 1.000 19.24349 ?  246 SER   B CB    1 
ATOM   3829 O OG    . SER   B 1 266 ? -30.94900 18.96100  37.91400 1.000 21.48391 ?  246 SER   B OG    1 
ATOM   3830 N N     . VAL   B 1 267 ? -34.39000 20.19400  36.00500 1.000 21.76054 ?  247 VAL   B N     1 
ATOM   3831 C CA    . VAL   B 1 267 ? -35.17200 19.85500  34.82100 1.000 22.41486 ?  247 VAL   B CA    1 
ATOM   3832 C C     . VAL   B 1 267 ? -34.50000 20.49100  33.61100 1.000 21.25970 ?  247 VAL   B C     1 
ATOM   3833 O O     . VAL   B 1 267 ? -34.33500 21.71100  33.57800 1.000 22.45447 ?  247 VAL   B O     1 
ATOM   3834 C CB    . VAL   B 1 267 ? -36.61600 20.36000  34.95900 1.000 20.94701 ?  247 VAL   B CB    1 
ATOM   3835 C CG1   . VAL   B 1 267 ? -37.45700 19.99300  33.73600 1.000 21.46281 ?  247 VAL   B CG1   1 
ATOM   3836 C CG2   . VAL   B 1 267 ? -37.24500 19.82100  36.28600 1.000 23.69770 ?  247 VAL   B CG2   1 
ATOM   3837 N N     . TRP   B 1 268 ? -34.16300 19.67100  32.61000 1.000 22.91283 ?  248 TRP   B N     1 
ATOM   3838 C CA    . TRP   B 1 268 ? -33.32400 20.08100  31.48500 1.000 26.06771 ?  248 TRP   B CA    1 
ATOM   3839 C C     . TRP   B 1 268 ? -34.03400 19.73900  30.18000 1.000 23.92536 ?  248 TRP   B C     1 
ATOM   3840 O O     . TRP   B 1 268 ? -34.42400 18.58600  29.97000 1.000 23.07788 ?  248 TRP   B O     1 
ATOM   3841 C CB    . TRP   B 1 268 ? -31.94500 19.38600  31.53900 1.000 22.83668 ?  248 TRP   B CB    1 
ATOM   3842 C CG    . TRP   B 1 268 ? -31.27600 19.49900  32.91000 1.000 23.76408 ?  248 TRP   B CG    1 
ATOM   3843 C CD1   . TRP   B 1 268 ? -31.49400 18.69500  34.00900 1.000 22.62611 ?  248 TRP   B CD1   1 
ATOM   3844 C CD2   . TRP   B 1 268 ? -30.28800 20.46000  33.30800 1.000 25.95150 ?  248 TRP   B CD2   1 
ATOM   3845 N NE1   . TRP   B 1 268 ? -30.71100 19.12100  35.06800 1.000 20.43398 ?  248 TRP   B NE1   1 
ATOM   3846 C CE2   . TRP   B 1 268 ? -29.95900 20.19300  34.66400 1.000 23.79101 ?  248 TRP   B CE2   1 
ATOM   3847 C CE3   . TRP   B 1 268 ? -29.63500 21.51400  32.65200 1.000 25.72111 ?  248 TRP   B CE3   1 
ATOM   3848 C CZ2   . TRP   B 1 268 ? -29.02600 20.95300  35.37300 1.000 21.77543 ?  248 TRP   B CZ2   1 
ATOM   3849 C CZ3   . TRP   B 1 268 ? -28.70400 22.27300  33.37100 1.000 25.24111 ?  248 TRP   B CZ3   1 
ATOM   3850 C CH2   . TRP   B 1 268 ? -28.40400 21.98100  34.70800 1.000 23.97598 ?  248 TRP   B CH2   1 
ATOM   3851 N N     . LYS   B 1 269 ? -34.18600 20.73400  29.29900 1.000 25.25204 ?  249 LYS   B N     1 
ATOM   3852 C CA    . LYS   B 1 269 ? -34.86200 20.55100  28.01400 1.000 22.77669 ?  249 LYS   B CA    1 
ATOM   3853 C C     . LYS   B 1 269 ? -33.82600 20.53000  26.89600 1.000 25.92648 ?  249 LYS   B C     1 
ATOM   3854 O O     . LYS   B 1 269 ? -32.96300 21.40700  26.83100 1.000 27.97390 ?  249 LYS   B O     1 
ATOM   3855 C CB    . LYS   B 1 269 ? -35.88700 21.67600  27.78400 1.000 29.50938 ?  249 LYS   B CB    1 
ATOM   3856 C CG    . LYS   B 1 269 ? -36.82300 21.48100  26.58100 1.000 26.76625 ?  249 LYS   B CG    1 
ATOM   3857 C CD    . LYS   B 1 269 ? -37.73700 22.70500  26.43300 1.000 30.82469 ?  249 LYS   B CD    1 
ATOM   3858 C CE    . LYS   B 1 269 ? -38.85800 22.47900  25.42100 1.000 46.01308 ?  249 LYS   B CE    1 
ATOM   3859 N N     . VAL   B 1 270 ? -33.89100 19.51000  26.04000 1.000 24.73415 ?  250 VAL   B N     1 
ATOM   3860 C CA    . VAL   B 1 270 ? -32.94200 19.37800  24.94300 1.000 23.85241 ?  250 VAL   B CA    1 
ATOM   3861 C C     . VAL   B 1 270 ? -33.14700 20.52300  23.96200 1.000 33.82436 ?  250 VAL   B C     1 
ATOM   3862 O O     . VAL   B 1 270 ? -34.27800 20.80500  23.53700 1.000 36.99064 ?  250 VAL   B O     1 
ATOM   3863 C CB    . VAL   B 1 270 ? -33.11500 18.03000  24.22500 1.000 32.17680 ?  250 VAL   B CB    1 
ATOM   3864 C CG1   . VAL   B 1 270 ? -32.17100 17.95700  23.02200 1.000 35.72652 ?  250 VAL   B CG1   1 
ATOM   3865 C CG2   . VAL   B 1 270 ? -32.83000 16.89000  25.15200 1.000 33.97137 ?  250 VAL   B CG2   1 
ATOM   3866 N N     . ILE   B 1 271 ? -32.05600 21.18300  23.60400 1.000 33.81171 ?  251 ILE   B N     1 
ATOM   3867 C CA    . ILE   B 1 271 ? -32.07200 22.25900  22.62200 1.000 40.95204 ?  251 ILE   B CA    1 
ATOM   3868 C C     . ILE   B 1 271 ? -32.20900 21.69700  21.20800 1.000 44.60535 ?  251 ILE   B C     1 
ATOM   3869 O O     . ILE   B 1 271 ? -33.22500 21.90600  20.54100 1.000 62.97351 ?  251 ILE   B O     1 
ATOM   3870 C CB    . ILE   B 1 271 ? -30.80300 23.09600  22.73700 1.000 35.71728 ?  251 ILE   B CB    1 
ATOM   3871 C CG1   . ILE   B 1 271 ? -30.85300 23.96900  23.98700 1.000 42.01173 ?  251 ILE   B CG1   1 
ATOM   3872 C CG2   . ILE   B 1 271 ? -30.62400 23.94900  21.49000 1.000 48.17326 ?  251 ILE   B CG2   1 
ATOM   3873 C CD1   . ILE   B 1 271 ? -29.47800 24.33900  24.47800 1.000 41.11767 ?  251 ILE   B CD1   1 
HETATM 3874 N N     . SAH   C 2 .   ? -9.02000  -12.72400 27.18200 1.000 23.65394 ?  401 SAH   A N     1 
HETATM 3875 C CA    . SAH   C 2 .   ? -9.23000  -13.23600 25.80400 1.000 21.80705 ?  401 SAH   A CA    1 
HETATM 3876 C CB    . SAH   C 2 .   ? -10.17700 -12.32800 25.02000 1.000 20.76478 ?  401 SAH   A CB    1 
HETATM 3877 C CG    . SAH   C 2 .   ? -9.63200  -10.95000 24.71200 1.000 19.84584 ?  401 SAH   A CG    1 
HETATM 3878 S SD    . SAH   C 2 .   ? -10.65700 -10.07800 23.50100 1.000 20.70201 ?  401 SAH   A SD    1 
HETATM 3879 C C     . SAH   C 2 .   ? -7.89000  -13.32800 25.06200 1.000 26.87648 ?  401 SAH   A C     1 
HETATM 3880 O O     . SAH   C 2 .   ? -7.88800  -13.86900 23.98000 1.000 29.91253 ?  401 SAH   A O     1 
HETATM 3881 O OXT   . SAH   C 2 .   ? -6.91700  -12.85200 25.62300 1.000 31.62225 ?  401 SAH   A OXT   1 
HETATM 3882 C "C5'" . SAH   C 2 .   ? -11.58600 -8.91500  24.52500 1.000 17.96261 ?  401 SAH   A "C5'" 1 
HETATM 3883 C "C4'" . SAH   C 2 .   ? -12.48600 -9.63300  25.49700 1.000 19.19061 ?  401 SAH   A "C4'" 1 
HETATM 3884 O "O4'" . SAH   C 2 .   ? -12.93100 -8.70900  26.51400 1.000 21.01715 ?  401 SAH   A "O4'" 1 
HETATM 3885 C "C3'" . SAH   C 2 .   ? -13.75500 -10.22400 24.88300 1.000 18.02738 ?  401 SAH   A "C3'" 1 
HETATM 3886 O "O3'" . SAH   C 2 .   ? -13.98500 -11.51400 25.42500 1.000 20.65016 ?  401 SAH   A "O3'" 1 
HETATM 3887 C "C2'" . SAH   C 2 .   ? -14.83500 -9.22400  25.30400 1.000 20.56761 ?  401 SAH   A "C2'" 1 
HETATM 3888 O "O2'" . SAH   C 2 .   ? -16.13000 -9.77400  25.36700 1.000 21.65324 ?  401 SAH   A "O2'" 1 
HETATM 3889 C "C1'" . SAH   C 2 .   ? -14.31800 -8.85200  26.68300 1.000 19.02193 ?  401 SAH   A "C1'" 1 
HETATM 3890 N N9    . SAH   C 2 .   ? -14.83600 -7.60000  27.20700 1.000 22.40529 ?  401 SAH   A N9    1 
HETATM 3891 C C8    . SAH   C 2 .   ? -14.95500 -6.41100  26.53900 1.000 22.81043 ?  401 SAH   A C8    1 
HETATM 3892 N N7    . SAH   C 2 .   ? -15.42100 -5.44700  27.28700 1.000 23.23956 ?  401 SAH   A N7    1 
HETATM 3893 C C5    . SAH   C 2 .   ? -15.61800 -6.03100  28.52900 1.000 22.44421 ?  401 SAH   A C5    1 
HETATM 3894 C C6    . SAH   C 2 .   ? -16.09900 -5.53000  29.75400 1.000 19.97692 ?  401 SAH   A C6    1 
HETATM 3895 N N6    . SAH   C 2 .   ? -16.48900 -4.27400  29.94500 1.000 21.33224 ?  401 SAH   A N6    1 
HETATM 3896 N N1    . SAH   C 2 .   ? -16.16000 -6.39000  30.79400 1.000 19.77582 ?  401 SAH   A N1    1 
HETATM 3897 C C2    . SAH   C 2 .   ? -15.76000 -7.65200  30.60900 1.000 20.67174 ?  401 SAH   A C2    1 
HETATM 3898 N N3    . SAH   C 2 .   ? -15.30000 -8.23200  29.50900 1.000 19.69348 ?  401 SAH   A N3    1 
HETATM 3899 C C4    . SAH   C 2 .   ? -15.25000 -7.36000  28.49200 1.000 20.31412 ?  401 SAH   A C4    1 
HETATM 3900 N N     . A1ASZ D 3 .   ? -8.50600  -8.48800  17.26200 1.000 19.75871 ?  402 A1ASZ A N     1 
HETATM 3901 C CA    . A1ASZ D 3 .   ? -8.96100  -9.37300  18.37600 1.000 22.28693 ?  402 A1ASZ A CA    1 
HETATM 3902 C C     . A1ASZ D 3 .   ? -10.24000 -8.80300  19.00500 1.000 23.63554 ?  402 A1ASZ A C     1 
HETATM 3903 O O     . A1ASZ D 3 .   ? -10.62900 -7.67100  18.63600 1.000 21.38285 ?  402 A1ASZ A O     1 
HETATM 3904 C CB    . A1ASZ D 3 .   ? -7.87600  -9.51500  19.45500 1.000 22.69978 ?  402 A1ASZ A CB    1 
HETATM 3905 C CG    . A1ASZ D 3 .   ? -7.70200  -8.30900  20.33900 1.000 20.54573 ?  402 A1ASZ A CG    1 
HETATM 3906 N ND1   . A1ASZ D 3 .   ? -8.20100  -8.19100  21.60200 1.000 21.24179 ?  402 A1ASZ A ND1   1 
HETATM 3907 C CD2   . A1ASZ D 3 .   ? -7.02600  -7.13300  20.08500 1.000 19.53803 ?  402 A1ASZ A CD2   1 
HETATM 3908 C CE1   . A1ASZ D 3 .   ? -7.85100  -7.00200  22.09900 1.000 20.02689 ?  402 A1ASZ A CE1   1 
HETATM 3909 N NE2   . A1ASZ D 3 .   ? -7.13500  -6.35500  21.18600 1.000 18.35950 ?  402 A1ASZ A NE2   1 
HETATM 3910 O OXT   . A1ASZ D 3 .   ? -10.78900 -9.50200  19.88800 1.000 20.87656 -1 402 A1ASZ A OXT   1 
HETATM 3911 S S1    . A1ASZ D 3 .   ? -6.19100  -6.72300  18.60400 1.000 21.55259 ?  402 A1ASZ A S1    1 
HETATM 3912 C C1    . EDO   E 4 .   ? -4.60100  -20.08200 15.92600 1.000 34.37832 ?  403 EDO   A C1    1 
HETATM 3913 O O1    . EDO   E 4 .   ? -4.40100  -19.64400 17.28000 1.000 38.31664 ?  403 EDO   A O1    1 
HETATM 3914 C C2    . EDO   E 4 .   ? -6.08700  -20.26400 15.63500 1.000 40.33543 ?  403 EDO   A C2    1 
HETATM 3915 O O2    . EDO   E 4 .   ? -6.79900  -19.04100 15.84300 1.000 28.36705 ?  403 EDO   A O2    1 
HETATM 3916 C C1    . EDO   F 4 .   ? -3.20100  -34.29100 33.19400 1.000 44.79861 ?  404 EDO   A C1    1 
HETATM 3917 O O1    . EDO   F 4 .   ? -2.75000  -35.50400 32.54700 1.000 33.66690 ?  404 EDO   A O1    1 
HETATM 3918 C C2    . EDO   F 4 .   ? -4.73200  -34.20800 33.32600 1.000 34.69360 ?  404 EDO   A C2    1 
HETATM 3919 O O2    . EDO   F 4 .   ? -5.28500  -35.30900 34.09700 1.000 38.28132 ?  404 EDO   A O2    1 
HETATM 3920 C C1    . EDO   G 4 .   ? 7.34400   -8.04200  12.70400 1.000 43.92082 ?  405 EDO   A C1    1 
HETATM 3921 O O1    . EDO   G 4 .   ? 8.68800   -8.44800  12.39000 1.000 41.08070 ?  405 EDO   A O1    1 
HETATM 3922 C C2    . EDO   G 4 .   ? 7.16700   -7.85200  14.20800 1.000 40.59431 ?  405 EDO   A C2    1 
HETATM 3923 O O2    . EDO   G 4 .   ? 7.93100   -6.71400  14.63000 1.000 52.03235 ?  405 EDO   A O2    1 
HETATM 3924 C C1    . EDO   H 4 .   ? -16.62900 1.40900   39.98100 1.000 35.34140 ?  406 EDO   A C1    1 
HETATM 3925 O O1    . EDO   H 4 .   ? -16.91500 0.01000   39.92900 1.000 40.55055 ?  406 EDO   A O1    1 
HETATM 3926 C C2    . EDO   H 4 .   ? -16.31400 1.84800   38.56300 1.000 28.97963 ?  406 EDO   A C2    1 
HETATM 3927 O O2    . EDO   H 4 .   ? -17.44700 1.56600   37.74200 1.000 28.57068 ?  406 EDO   A O2    1 
HETATM 3928 C C1    . EDO   I 4 .   ? -6.37600  9.55000   28.96900 1.000 38.90736 ?  407 EDO   A C1    1 
HETATM 3929 O O1    . EDO   I 4 .   ? -5.53100  9.12800   30.04700 1.000 55.71805 ?  407 EDO   A O1    1 
HETATM 3930 C C2    . EDO   I 4 .   ? -7.63900  8.70200   28.98900 1.000 34.54775 ?  407 EDO   A C2    1 
HETATM 3931 O O2    . EDO   I 4 .   ? -8.25300  8.75700   30.28600 1.000 39.41949 ?  407 EDO   A O2    1 
HETATM 3932 C C1    . EDO   J 4 .   ? -14.52000 -2.02400  39.05100 1.000 40.20834 ?  408 EDO   A C1    1 
HETATM 3933 O O1    . EDO   J 4 .   ? -14.93700 -2.92100  38.02700 1.000 32.04903 ?  408 EDO   A O1    1 
HETATM 3934 C C2    . EDO   J 4 .   ? -13.36700 -2.66100  39.80100 1.000 37.37916 ?  408 EDO   A C2    1 
HETATM 3935 O O2    . EDO   J 4 .   ? -12.26700 -2.69800  38.89400 1.000 51.01619 ?  408 EDO   A O2    1 
HETATM 3936 C C1    . EDO   K 4 .   ? -17.88300 -3.38500  27.20700 1.000 41.08279 ?  409 EDO   A C1    1 
HETATM 3937 O O1    . EDO   K 4 .   ? -16.61500 -2.77700  27.07000 1.000 21.35030 ?  409 EDO   A O1    1 
HETATM 3938 C C2    . EDO   K 4 .   ? -18.90900 -3.00900  26.21300 1.000 41.16022 ?  409 EDO   A C2    1 
HETATM 3939 O O2    . EDO   K 4 .   ? -18.64600 -1.79600  25.55500 1.000 48.96163 ?  409 EDO   A O2    1 
HETATM 3940 C C1    . EDO   L 4 .   ? -7.78500  -23.29100 0.65400  1.000 44.22623 ?  410 EDO   A C1    1 
HETATM 3941 O O1    . EDO   L 4 .   ? -7.93000  -21.93900 0.20100  1.000 26.94760 ?  410 EDO   A O1    1 
HETATM 3942 C C2    . EDO   L 4 .   ? -7.53400  -24.24200 -0.51900 1.000 46.00852 ?  410 EDO   A C2    1 
HETATM 3943 O O2    . EDO   L 4 .   ? -6.22600  -24.04300 -1.08300 1.000 38.96294 ?  410 EDO   A O2    1 
HETATM 3944 N N     . SAH   M 2 .   ? -34.00900 6.01100   41.61700 1.000 23.73279 ?  301 SAH   B N     1 
HETATM 3945 C CA    . SAH   M 2 .   ? -34.12200 5.41900   42.97100 1.000 27.62360 ?  301 SAH   B CA    1 
HETATM 3946 C CB    . SAH   M 2 .   ? -32.81200 4.76800   43.41800 1.000 27.61381 ?  301 SAH   B CB    1 
HETATM 3947 C CG    . SAH   M 2 .   ? -31.71200 5.71900   43.80500 1.000 25.27167 ?  301 SAH   B CG    1 
HETATM 3948 S SD    . SAH   M 2 .   ? -30.30900 4.82300   44.51500 1.000 24.51446 ?  301 SAH   B SD    1 
HETATM 3949 C C     . SAH   M 2 .   ? -34.50400 6.50400   43.98500 1.000 34.01114 ?  301 SAH   B C     1 
HETATM 3950 O O     . SAH   M 2 .   ? -34.48500 7.67700   43.61300 1.000 31.29194 ?  301 SAH   B O     1 
HETATM 3951 O OXT   . SAH   M 2 .   ? -34.80300 6.11700   45.08000 1.000 29.05541 ?  301 SAH   B OXT   1 
HETATM 3952 C "C5'" . SAH   M 2 .   ? -29.25000 4.54400   43.07800 1.000 21.90786 ?  301 SAH   B "C5'" 1 
HETATM 3953 C "C4'" . SAH   M 2 .   ? -29.83200 3.50700   42.15200 1.000 19.64961 ?  301 SAH   B "C4'" 1 
HETATM 3954 O "O4'" . SAH   M 2 .   ? -29.08600 3.49500   40.91700 1.000 22.04409 ?  301 SAH   B "O4'" 1 
HETATM 3955 C "C3'" . SAH   M 2 .   ? -29.79300 2.07500   42.68500 1.000 20.93254 ?  301 SAH   B "C3'" 1 
HETATM 3956 O "O3'" . SAH   M 2 .   ? -30.96400 1.37700   42.29400 1.000 22.78958 ?  301 SAH   B "O3'" 1 
HETATM 3957 C "C2'" . SAH   M 2 .   ? -28.55000 1.49800   42.00800 1.000 20.38629 ?  301 SAH   B "C2'" 1 
HETATM 3958 O "O2'" . SAH   M 2 .   ? -28.59300 0.09600   41.86900 1.000 20.82274 ?  301 SAH   B "O2'" 1 
HETATM 3959 C "C1'" . SAH   M 2 .   ? -28.62900 2.19100   40.65500 1.000 22.83395 ?  301 SAH   B "C1'" 1 
HETATM 3960 N N9    . SAH   M 2 .   ? -27.35500 2.29700   39.96300 1.000 22.56026 ?  301 SAH   B N9    1 
HETATM 3961 C C8    . SAH   M 2 .   ? -26.11700 2.48100   40.52100 1.000 21.11883 ?  301 SAH   B C8    1 
HETATM 3962 N N7    . SAH   M 2 .   ? -25.16000 2.56100   39.63500 1.000 20.56964 ?  301 SAH   B N7    1 
HETATM 3963 C C5    . SAH   M 2 .   ? -25.80700 2.42900   38.41600 1.000 18.50960 ?  301 SAH   B C5    1 
HETATM 3964 C C6    . SAH   M 2 .   ? -25.33900 2.42700   37.09000 1.000 22.05098 ?  301 SAH   B C6    1 
HETATM 3965 N N6    . SAH   M 2 .   ? -24.06100 2.57300   36.75600 1.000 20.45348 ?  301 SAH   B N6    1 
HETATM 3966 N N1    . SAH   M 2 .   ? -26.25500 2.27500   36.10800 1.000 22.64268 ?  301 SAH   B N1    1 
HETATM 3967 C C2    . SAH   M 2 .   ? -27.54100 2.13500   36.44700 1.000 20.59545 ?  301 SAH   B C2    1 
HETATM 3968 N N3    . SAH   M 2 .   ? -28.09300 2.11500   37.65400 1.000 21.05746 ?  301 SAH   B N3    1 
HETATM 3969 C C4    . SAH   M 2 .   ? -27.16300 2.27400   38.60700 1.000 17.87274 ?  301 SAH   B C4    1 
HETATM 3970 C C1    . EDO   N 4 .   ? -31.38100 7.15100   48.26500 1.000 35.73157 ?  302 EDO   B C1    1 
HETATM 3971 O O1    . EDO   N 4 .   ? -30.75700 6.10200   47.51900 1.000 40.60496 ?  302 EDO   B O1    1 
HETATM 3972 C C2    . EDO   N 4 .   ? -32.87700 7.06400   48.02500 1.000 32.20675 ?  302 EDO   B C2    1 
HETATM 3973 O O2    . EDO   N 4 .   ? -33.16800 7.58800   46.72900 1.000 28.31544 ?  302 EDO   B O2    1 
HETATM 3974 C C1    . EDO   O 4 .   ? -40.76800 9.69800   51.87300 1.000 28.55470 ?  303 EDO   B C1    1 
HETATM 3975 O O1    . EDO   O 4 .   ? -39.71300 8.83300   51.47500 1.000 27.84485 ?  303 EDO   B O1    1 
HETATM 3976 C C2    . EDO   O 4 .   ? -41.97800 8.83900   52.27400 1.000 28.47216 ?  303 EDO   B C2    1 
HETATM 3977 O O2    . EDO   O 4 .   ? -41.83300 8.35900   53.61200 1.000 35.02324 ?  303 EDO   B O2    1 
HETATM 3978 C C1    . EDO   P 4 .   ? -47.31700 4.73200   49.76300 1.000 28.14481 ?  304 EDO   B C1    1 
HETATM 3979 O O1    . EDO   P 4 .   ? -46.26500 3.97700   49.15100 1.000 29.36311 ?  304 EDO   B O1    1 
HETATM 3980 C C2    . EDO   P 4 .   ? -48.31700 5.13400   48.68900 1.000 42.38248 ?  304 EDO   B C2    1 
HETATM 3981 O O2    . EDO   P 4 .   ? -47.71800 6.17000   47.90800 1.000 32.95090 ?  304 EDO   B O2    1 
HETATM 3982 O O     . HOH   Q 5 .   ? -25.25700 -17.98700 24.16400 1.000 51.44828 ?  501 HOH   A O     1 
HETATM 3983 O O     . HOH   Q 5 .   ? -9.935    -36.240   33.594   1.000 49.20373 ?  502 HOH   A O     1 
HETATM 3984 O O     . HOH   Q 5 .   ? -3.79900  -28.70200 40.27700 1.000 31.98792 ?  503 HOH   A O     1 
HETATM 3985 O O     . HOH   Q 5 .   ? -3.33600  8.43300   29.31700 1.000 30.95775 ?  504 HOH   A O     1 
HETATM 3986 O O     . HOH   Q 5 .   ? 2.88700   -23.38400 13.80200 1.000 44.70196 ?  505 HOH   A O     1 
HETATM 3987 O O     . HOH   Q 5 .   ? -8.91400  -20.08800 2.56800  1.000 32.62664 ?  506 HOH   A O     1 
HETATM 3988 O O     . HOH   Q 5 .   ? -9.72300  6.29900   30.04200 1.000 26.00936 ?  507 HOH   A O     1 
HETATM 3989 O O     . HOH   Q 5 .   ? -11.20200 -20.08300 13.00400 1.000 39.15465 ?  508 HOH   A O     1 
HETATM 3990 O O     . HOH   Q 5 .   ? -4.61200  -22.84200 7.14600  1.000 36.66499 ?  509 HOH   A O     1 
HETATM 3991 O O     . HOH   Q 5 .   ? -9.84500  -17.13900 29.14900 1.000 22.99816 ?  510 HOH   A O     1 
HETATM 3992 O O     . HOH   Q 5 .   ? -4.56500  -27.96800 29.19400 1.000 24.92722 ?  511 HOH   A O     1 
HETATM 3993 O O     . HOH   Q 5 .   ? -16.37700 -1.17500  24.22200 1.000 29.95392 ?  512 HOH   A O     1 
HETATM 3994 O O     . HOH   Q 5 .   ? -21.41700 -20.44700 34.14600 1.000 39.42151 ?  513 HOH   A O     1 
HETATM 3995 O O     . HOH   Q 5 .   ? -4.81200  -9.15500  16.76300 1.000 21.94859 ?  514 HOH   A O     1 
HETATM 3996 O O     . HOH   Q 5 .   ? -22.03900 -28.39600 24.61000 1.000 36.46726 ?  515 HOH   A O     1 
HETATM 3997 O O     . HOH   Q 5 .   ? -9.32200  -18.37200 15.43600 1.000 26.87083 ?  516 HOH   A O     1 
HETATM 3998 O O     . HOH   Q 5 .   ? -22.04000 -2.42300  34.24400 1.000 24.88220 ?  517 HOH   A O     1 
HETATM 3999 O O     . HOH   Q 5 .   ? -22.41300 -21.81700 22.45300 1.000 45.73757 ?  518 HOH   A O     1 
HETATM 4000 O O     . HOH   Q 5 .   ? 3.95900   7.13300   38.33100 1.000 50.25690 ?  519 HOH   A O     1 
HETATM 4001 O O     . HOH   Q 5 .   ? 1.55200   -17.27600 22.47800 1.000 28.66840 ?  520 HOH   A O     1 
HETATM 4002 O O     . HOH   Q 5 .   ? -19.79500 -20.90700 17.21300 1.000 40.13604 ?  521 HOH   A O     1 
HETATM 4003 O O     . HOH   Q 5 .   ? -15.92200 -15.25700 43.80300 1.000 34.71159 ?  522 HOH   A O     1 
HETATM 4004 O O     . HOH   Q 5 .   ? -16.24300 4.89800   25.09400 1.000 27.00393 ?  523 HOH   A O     1 
HETATM 4005 O O     . HOH   Q 5 .   ? -9.16900  -22.98500 -4.24600 1.000 22.48777 ?  524 HOH   A O     1 
HETATM 4006 O O     . HOH   Q 5 .   ? 7.99400   -15.18700 31.53400 1.000 47.34575 ?  525 HOH   A O     1 
HETATM 4007 O O     . HOH   Q 5 .   ? -26.00600 -13.62900 23.16900 1.000 51.30744 ?  526 HOH   A O     1 
HETATM 4008 O O     . HOH   Q 5 .   ? -8.43600  -12.15400 30.51600 1.000 24.94149 ?  527 HOH   A O     1 
HETATM 4009 O O     . HOH   Q 5 .   ? 0.51300   -4.20600  29.15300 1.000 22.08904 ?  528 HOH   A O     1 
HETATM 4010 O O     . HOH   Q 5 .   ? -8.45900  -8.30600  10.95600 1.000 51.75908 ?  529 HOH   A O     1 
HETATM 4011 O O     . HOH   Q 5 .   ? -12.06100 -30.55600 38.53700 1.000 32.07142 ?  530 HOH   A O     1 
HETATM 4012 O O     . HOH   Q 5 .   ? -5.82300  0.84100   40.79100 1.000 30.98709 ?  531 HOH   A O     1 
HETATM 4013 O O     . HOH   Q 5 .   ? -25.93900 -13.98600 32.93500 1.000 46.48087 ?  532 HOH   A O     1 
HETATM 4014 O O     . HOH   Q 5 .   ? -2.23700  -12.56900 47.88900 1.000 44.39472 ?  533 HOH   A O     1 
HETATM 4015 O O     . HOH   Q 5 .   ? -0.65500  -24.39500 43.16300 1.000 46.82906 ?  534 HOH   A O     1 
HETATM 4016 O O     . HOH   Q 5 .   ? -17.01100 -19.37700 11.64100 1.000 34.58645 ?  535 HOH   A O     1 
HETATM 4017 O O     . HOH   Q 5 .   ? -19.27200 3.20800   36.58700 1.000 31.51114 ?  536 HOH   A O     1 
HETATM 4018 O O     . HOH   Q 5 .   ? -5.71500  -5.96900  29.19400 1.000 20.69747 ?  537 HOH   A O     1 
HETATM 4019 O O     . HOH   Q 5 .   ? -16.09200 -18.81400 5.71600  1.000 43.15985 ?  538 HOH   A O     1 
HETATM 4020 O O     . HOH   Q 5 .   ? 1.23500   17.25400  28.28400 1.000 41.45988 ?  539 HOH   A O     1 
HETATM 4021 O O     . HOH   Q 5 .   ? -5.56900  0.73300   16.84100 1.000 25.78409 ?  540 HOH   A O     1 
HETATM 4022 O O     . HOH   Q 5 .   ? -1.88300  -27.14700 31.15300 1.000 27.81441 ?  541 HOH   A O     1 
HETATM 4023 O O     . HOH   Q 5 .   ? -19.32200 -22.05800 35.67600 1.000 22.80780 ?  542 HOH   A O     1 
HETATM 4024 O O     . HOH   Q 5 .   ? 5.18800   -14.43100 43.27200 1.000 46.91775 ?  543 HOH   A O     1 
HETATM 4025 O O     . HOH   Q 5 .   ? -10.13600 -7.16800  15.51100 1.000 39.45273 ?  544 HOH   A O     1 
HETATM 4026 O O     . HOH   Q 5 .   ? -2.98600  13.03900  28.57500 1.000 44.90535 ?  545 HOH   A O     1 
HETATM 4027 O O     . HOH   Q 5 .   ? -6.00000  -28.93900 40.19800 1.000 32.34107 ?  546 HOH   A O     1 
HETATM 4028 O O     . HOH   Q 5 .   ? -24.05400 -16.01400 19.44000 1.000 40.68219 ?  547 HOH   A O     1 
HETATM 4029 O O     . HOH   Q 5 .   ? -5.997    -34.044   22.847   1.000 36.86240 ?  548 HOH   A O     1 
HETATM 4030 O O     . HOH   Q 5 .   ? -7.30900  -11.82400 22.23200 1.000 23.66973 ?  549 HOH   A O     1 
HETATM 4031 O O     . HOH   Q 5 .   ? -10.31600 0.61300   21.85500 1.000 20.13158 ?  550 HOH   A O     1 
HETATM 4032 O O     . HOH   Q 5 .   ? 9.03200   0.09400   31.40600 1.000 53.72566 ?  551 HOH   A O     1 
HETATM 4033 O O     . HOH   Q 5 .   ? -14.01000 -11.43300 17.31100 1.000 40.17193 ?  552 HOH   A O     1 
HETATM 4034 O O     . HOH   Q 5 .   ? 6.34200   0.93600   39.40000 1.000 35.69468 ?  553 HOH   A O     1 
HETATM 4035 O O     . HOH   Q 5 .   ? -10.84900 -10.46100 16.10000 1.000 28.18261 ?  554 HOH   A O     1 
HETATM 4036 O O     . HOH   Q 5 .   ? -19.76500 -22.57500 19.20300 1.000 35.89773 ?  555 HOH   A O     1 
HETATM 4037 O O     . HOH   Q 5 .   ? 4.21800   -21.55700 35.18000 1.000 42.32270 ?  556 HOH   A O     1 
HETATM 4038 O O     . HOH   Q 5 .   ? -1.20600  -20.12900 17.49300 1.000 35.96951 ?  557 HOH   A O     1 
HETATM 4039 O O     . HOH   Q 5 .   ? 6.45400   3.44800   26.95200 1.000 44.49398 ?  558 HOH   A O     1 
HETATM 4040 O O     . HOH   Q 5 .   ? -9.47800  -26.49600 34.58700 1.000 23.82417 ?  559 HOH   A O     1 
HETATM 4041 O O     . HOH   Q 5 .   ? -5.46700  -15.63000 49.62100 1.000 37.17000 ?  560 HOH   A O     1 
HETATM 4042 O O     . HOH   Q 5 .   ? -4.01300  -21.48700 19.33400 1.000 49.24694 ?  561 HOH   A O     1 
HETATM 4043 O O     . HOH   Q 5 .   ? -17.70500 -4.64700  21.90300 1.000 40.23506 ?  562 HOH   A O     1 
HETATM 4044 O O     . HOH   Q 5 .   ? -8.527    -7.148    7.667    1.000 55.45299 ?  563 HOH   A O     1 
HETATM 4045 O O     . HOH   Q 5 .   ? -23.62400 -14.87100 34.53800 1.000 37.92333 ?  564 HOH   A O     1 
HETATM 4046 O O     . HOH   Q 5 .   ? 5.59100   -12.36000 45.33100 1.000 45.77080 ?  565 HOH   A O     1 
HETATM 4047 O O     . HOH   Q 5 .   ? -19.24700 -24.69600 4.08200  1.000 34.64181 ?  566 HOH   A O     1 
HETATM 4048 O O     . HOH   Q 5 .   ? -21.41800 -10.10100 37.25400 1.000 33.46549 ?  567 HOH   A O     1 
HETATM 4049 O O     . HOH   Q 5 .   ? 1.49900   -22.28100 10.29300 1.000 48.97269 ?  568 HOH   A O     1 
HETATM 4050 O O     . HOH   Q 5 .   ? 4.90600   -0.25900  25.27900 1.000 31.12126 ?  569 HOH   A O     1 
HETATM 4051 O O     . HOH   Q 5 .   ? -18.09600 -7.77600  25.13700 1.000 27.88844 ?  570 HOH   A O     1 
HETATM 4052 O O     . HOH   Q 5 .   ? -8.30300  -14.87600 28.85000 1.000 29.11736 ?  571 HOH   A O     1 
HETATM 4053 O O     . HOH   Q 5 .   ? -22.51800 -19.27200 22.72200 1.000 27.71671 ?  572 HOH   A O     1 
HETATM 4054 O O     . HOH   Q 5 .   ? -8.14900  3.21500   47.27000 1.000 48.82942 ?  573 HOH   A O     1 
HETATM 4055 O O     . HOH   Q 5 .   ? 5.64400   -14.32800 16.16300 1.000 27.53644 ?  574 HOH   A O     1 
HETATM 4056 O O     . HOH   Q 5 .   ? -12.24200 -16.52700 2.96300  1.000 32.10592 ?  575 HOH   A O     1 
HETATM 4057 O O     . HOH   Q 5 .   ? -22.81900 -8.05800  25.53000 1.000 33.29614 ?  576 HOH   A O     1 
HETATM 4058 O O     . HOH   Q 5 .   ? -7.74700  3.59300   15.76800 1.000 30.67474 ?  577 HOH   A O     1 
HETATM 4059 O O     . HOH   Q 5 .   ? -2.00700  -24.36100 33.61900 1.000 34.25965 ?  578 HOH   A O     1 
HETATM 4060 O O     . HOH   Q 5 .   ? 0.40900   -23.55600 33.16500 1.000 42.75551 ?  579 HOH   A O     1 
HETATM 4061 O O     . HOH   Q 5 .   ? 1.12400   -22.28300 24.92200 1.000 33.15913 ?  580 HOH   A O     1 
HETATM 4062 O O     . HOH   Q 5 .   ? -5.49100  -18.48900 23.24900 1.000 23.89744 ?  581 HOH   A O     1 
HETATM 4063 O O     . HOH   Q 5 .   ? 0.73200   -30.81300 32.83800 1.000 48.09323 ?  582 HOH   A O     1 
HETATM 4064 O O     . HOH   Q 5 .   ? -13.64400 -1.78400  43.05200 1.000 43.81302 ?  583 HOH   A O     1 
HETATM 4065 O O     . HOH   Q 5 .   ? -12.98900 -23.89900 43.55600 1.000 37.69460 ?  584 HOH   A O     1 
HETATM 4066 O O     . HOH   Q 5 .   ? -10.62600 4.42500   15.65900 1.000 30.74865 ?  585 HOH   A O     1 
HETATM 4067 O O     . HOH   Q 5 .   ? -4.763    -25.994   22.754   1.000 24.76306 ?  586 HOH   A O     1 
HETATM 4068 O O     . HOH   Q 5 .   ? -15.73600 -17.26200 12.71900 1.000 38.10339 ?  587 HOH   A O     1 
HETATM 4069 O O     . HOH   Q 5 .   ? -6.76400  -16.37200 24.75900 1.000 23.42005 ?  588 HOH   A O     1 
HETATM 4070 O O     . HOH   Q 5 .   ? -10.34600 -7.53200  47.96000 1.000 30.34168 ?  589 HOH   A O     1 
HETATM 4071 O O     . HOH   Q 5 .   ? 9.74800   -9.60900  25.75000 1.000 39.21544 ?  590 HOH   A O     1 
HETATM 4072 O O     . HOH   Q 5 .   ? -19.34300 -11.27100 13.62900 1.000 46.96356 ?  591 HOH   A O     1 
HETATM 4073 O O     . HOH   Q 5 .   ? -13.81600 9.09400   19.65600 1.000 41.72753 ?  592 HOH   A O     1 
HETATM 4074 O O     . HOH   Q 5 .   ? -3.83000  2.70700   41.05200 1.000 40.60736 ?  593 HOH   A O     1 
HETATM 4075 O O     . HOH   Q 5 .   ? -0.69300  13.71000  28.93500 1.000 41.06379 ?  594 HOH   A O     1 
HETATM 4076 O O     . HOH   Q 5 .   ? -21.95800 -14.37300 13.29800 1.000 34.23260 ?  595 HOH   A O     1 
HETATM 4077 O O     . HOH   Q 5 .   ? -3.48100  -34.41000 36.65200 1.000 44.60406 ?  596 HOH   A O     1 
HETATM 4078 O O     . HOH   Q 5 .   ? -18.15000 -24.97900 38.83300 1.000 57.39391 ?  597 HOH   A O     1 
HETATM 4079 O O     . HOH   Q 5 .   ? -20.83000 -6.33500  36.42700 1.000 29.15976 ?  598 HOH   A O     1 
HETATM 4080 O O     . HOH   Q 5 .   ? 4.30700   8.28600   26.79700 1.000 36.22037 ?  599 HOH   A O     1 
HETATM 4081 O O     . HOH   Q 5 .   ? -15.91300 -4.77100  23.85000 1.000 34.40186 ?  600 HOH   A O     1 
HETATM 4082 O O     . HOH   Q 5 .   ? 2.36900   13.41100  28.16400 1.000 45.42783 ?  601 HOH   A O     1 
HETATM 4083 O O     . HOH   Q 5 .   ? -5.18300  -8.48700  51.88800 1.000 52.58701 ?  602 HOH   A O     1 
HETATM 4084 O O     . HOH   Q 5 .   ? -24.57900 -14.26600 15.41600 1.000 41.90212 ?  603 HOH   A O     1 
HETATM 4085 O O     . HOH   Q 5 .   ? -13.40000 -19.69200 12.85200 1.000 42.32953 ?  604 HOH   A O     1 
HETATM 4086 O O     . HOH   Q 5 .   ? -5.38800  8.01300   37.94700 1.000 49.79354 ?  605 HOH   A O     1 
HETATM 4087 O O     . HOH   Q 5 .   ? -12.79600 -18.87700 46.97100 1.000 36.50766 ?  606 HOH   A O     1 
HETATM 4088 O O     . HOH   Q 5 .   ? -5.27400  5.67500   39.71800 1.000 41.29102 ?  607 HOH   A O     1 
HETATM 4089 O O     . HOH   Q 5 .   ? -2.64600  17.67900  19.93300 1.000 51.75559 ?  608 HOH   A O     1 
HETATM 4090 O O     . HOH   Q 5 .   ? -3.05300  -29.65900 38.19200 1.000 36.14265 ?  609 HOH   A O     1 
HETATM 4091 O O     . HOH   Q 5 .   ? -22.19200 -18.96900 37.35900 1.000 52.98908 ?  610 HOH   A O     1 
HETATM 4092 O O     . HOH   Q 5 .   ? -6.51100  4.64900   41.71500 1.000 36.27690 ?  611 HOH   A O     1 
HETATM 4093 O O     . HOH   Q 5 .   ? -26.07900 -27.05900 26.98100 1.000 50.30486 ?  612 HOH   A O     1 
HETATM 4094 O O     . HOH   Q 5 .   ? -5.65800  -15.38500 27.23600 1.000 32.01427 ?  613 HOH   A O     1 
HETATM 4095 O O     . HOH   Q 5 .   ? -11.68100 9.54400   32.23900 1.000 36.10481 ?  614 HOH   A O     1 
HETATM 4096 O O     . HOH   Q 5 .   ? -3.67700  -19.08100 20.65100 1.000 23.20356 ?  615 HOH   A O     1 
HETATM 4097 O O     . HOH   Q 5 .   ? -17.07500 -30.18100 8.38800  1.000 44.26540 ?  616 HOH   A O     1 
HETATM 4098 O O     . HOH   Q 5 .   ? -10.43500 -31.31800 21.50900 1.000 35.84400 ?  617 HOH   A O     1 
HETATM 4099 O O     . HOH   Q 5 .   ? 6.95400   -11.64200 40.30400 1.000 53.15234 ?  618 HOH   A O     1 
HETATM 4100 O O     . HOH   Q 5 .   ? 7.47200   -5.86700  26.43300 1.000 29.15937 ?  619 HOH   A O     1 
HETATM 4101 O O     . HOH   Q 5 .   ? -13.48000 11.18700  22.18000 1.000 29.67782 ?  620 HOH   A O     1 
HETATM 4102 O O     . HOH   Q 5 .   ? 4.95700   -18.68600 20.97800 1.000 35.33671 ?  621 HOH   A O     1 
HETATM 4103 O O     . HOH   Q 5 .   ? -1.71600  -17.89100 19.21500 1.000 28.74061 ?  622 HOH   A O     1 
HETATM 4104 O O     . HOH   Q 5 .   ? -23.94400 -12.45300 36.37300 1.000 43.82879 ?  623 HOH   A O     1 
HETATM 4105 O O     . HOH   Q 5 .   ? -20.94600 -0.53300  41.72000 1.000 44.99676 ?  624 HOH   A O     1 
HETATM 4106 O O     . HOH   Q 5 .   ? 7.02200   -18.49000 29.85000 1.000 43.19958 ?  625 HOH   A O     1 
HETATM 4107 O O     . HOH   Q 5 .   ? -12.17800 -23.58600 1.91200  1.000 34.62727 ?  626 HOH   A O     1 
HETATM 4108 O O     . HOH   Q 5 .   ? 7.80300   -1.11300  26.25900 1.000 42.14248 ?  627 HOH   A O     1 
HETATM 4109 O O     . HOH   Q 5 .   ? -12.09400 -10.93300 12.68700 1.000 37.60204 ?  628 HOH   A O     1 
HETATM 4110 O O     . HOH   Q 5 .   ? -10.30600 -26.12700 45.55600 1.000 47.84819 ?  629 HOH   A O     1 
HETATM 4111 O O     . HOH   Q 5 .   ? -10.39100 -20.35300 47.32800 1.000 39.56998 ?  630 HOH   A O     1 
HETATM 4112 O O     . HOH   Q 5 .   ? -12.81200 -31.86300 15.35900 1.000 41.62446 ?  631 HOH   A O     1 
HETATM 4113 O O     . HOH   Q 5 .   ? -8.67300  -7.99500  49.56300 1.000 53.18288 ?  632 HOH   A O     1 
HETATM 4114 O O     . HOH   Q 5 .   ? -19.73800 -8.34600  37.81400 1.000 31.30614 ?  633 HOH   A O     1 
HETATM 4115 O O     . HOH   Q 5 .   ? -10.07400 10.78900  33.25200 1.000 49.04229 ?  634 HOH   A O     1 
HETATM 4116 O O     . HOH   Q 5 .   ? -11.33800 -24.56300 -0.78900 1.000 41.51181 ?  635 HOH   A O     1 
HETATM 4117 O O     . HOH   Q 5 .   ? 5.10800   2.48600   42.15100 1.000 47.46069 ?  636 HOH   A O     1 
HETATM 4118 O O     . HOH   Q 5 .   ? -15.79000 -5.41200  46.97800 1.000 44.67333 ?  637 HOH   A O     1 
HETATM 4119 O O     . HOH   Q 5 .   ? -7.11500  10.05700  25.57800 1.000 39.07047 ?  638 HOH   A O     1 
HETATM 4120 O O     . HOH   Q 5 .   ? -5.36200  -3.42000  47.96900 1.000 54.36116 ?  639 HOH   A O     1 
HETATM 4121 O O     . HOH   Q 5 .   ? 4.82700   7.12800   35.77700 1.000 52.80855 ?  640 HOH   A O     1 
HETATM 4122 O O     . HOH   Q 5 .   ? -16.32200 -35.39300 26.73400 1.000 50.25377 ?  641 HOH   A O     1 
HETATM 4123 O O     . HOH   Q 5 .   ? 10.81300  -6.76300  32.41600 1.000 41.94317 ?  642 HOH   A O     1 
HETATM 4124 O O     . HOH   Q 5 .   ? -12.46100 -17.70100 12.93000 1.000 39.33235 ?  643 HOH   A O     1 
HETATM 4125 O O     . HOH   Q 5 .   ? 9.55600   16.89800  29.36400 1.000 55.95519 ?  644 HOH   A O     1 
HETATM 4126 O O     . HOH   Q 5 .   ? -27.68000 -17.71500 29.40500 1.000 56.82041 ?  645 HOH   A O     1 
HETATM 4127 O O     . HOH   Q 5 .   ? -19.66700 -33.77000 31.84300 1.000 50.29761 ?  646 HOH   A O     1 
HETATM 4128 O O     . HOH   Q 5 .   ? -6.56800  -22.84200 13.90400 1.000 40.32924 ?  647 HOH   A O     1 
HETATM 4129 O O     . HOH   Q 5 .   ? -9.61400  -4.19500  15.62700 1.000 47.79350 ?  648 HOH   A O     1 
HETATM 4130 O O     . HOH   Q 5 .   ? 9.50700   -5.84200  27.33500 1.000 49.98573 ?  649 HOH   A O     1 
HETATM 4131 O O     . HOH   Q 5 .   ? -18.96200 -4.16300  18.98400 1.000 41.03499 ?  650 HOH   A O     1 
HETATM 4132 O O     . HOH   Q 5 .   ? -16.28700 -17.71900 45.15100 1.000 51.08826 ?  651 HOH   A O     1 
HETATM 4133 O O     . HOH   Q 5 .   ? -15.78600 -23.56400 41.82400 1.000 47.20576 ?  652 HOH   A O     1 
HETATM 4134 O O     . HOH   Q 5 .   ? -0.03900  -32.81100 33.40900 1.000 53.47008 ?  653 HOH   A O     1 
HETATM 4135 O O     . HOH   Q 5 .   ? -17.99400 -5.47800  24.42000 1.000 42.74647 ?  654 HOH   A O     1 
HETATM 4136 O O     . HOH   Q 5 .   ? -1.27800  1.99800   48.22300 1.000 56.44051 ?  655 HOH   A O     1 
HETATM 4137 O O     . HOH   Q 5 .   ? -4.96200  -25.92400 43.87900 1.000 49.94461 ?  656 HOH   A O     1 
HETATM 4138 O O     . HOH   Q 5 .   ? 6.86500   -16.02900 34.25100 1.000 39.53364 ?  657 HOH   A O     1 
HETATM 4139 O O     . HOH   Q 5 .   ? -3.35800  9.09300   37.39700 1.000 54.95341 ?  658 HOH   A O     1 
HETATM 4140 O O     . HOH   Q 5 .   ? -6.188    -9.779    9.704    1.000 39.05627 ?  659 HOH   A O     1 
HETATM 4141 O O     . HOH   Q 5 .   ? -24.29700 -17.19400 32.96000 1.000 53.76231 ?  660 HOH   A O     1 
HETATM 4142 O O     . HOH   Q 5 .   ? -20.59900 -2.61400  42.52800 1.000 47.80688 ?  661 HOH   A O     1 
HETATM 4143 O O     . HOH   Q 5 .   ? 6.194     -16.280   12.968   1.000 46.82107 ?  662 HOH   A O     1 
HETATM 4144 O O     . HOH   Q 5 .   ? -10.64500 4.86000   43.51400 1.000 50.63445 ?  663 HOH   A O     1 
HETATM 4145 O O     . HOH   Q 5 .   ? -17.89500 3.02900   23.12500 1.000 48.04016 ?  664 HOH   A O     1 
HETATM 4146 O O     . HOH   Q 5 .   ? -1.73300  -0.54300  47.81500 1.000 52.79973 ?  665 HOH   A O     1 
HETATM 4147 O O     . HOH   Q 5 .   ? -15.60000 3.30000   43.51800 1.000 48.93143 ?  666 HOH   A O     1 
HETATM 4148 O O     . HOH   Q 5 .   ? -14.02800 -14.02700 48.89700 1.000 51.73473 ?  667 HOH   A O     1 
HETATM 4149 O O     . HOH   Q 5 .   ? -22.70500 -6.69000  34.48500 1.000 49.00080 ?  668 HOH   A O     1 
HETATM 4150 O O     . HOH   Q 5 .   ? -7.27500  12.39500  26.43100 1.000 48.45064 ?  669 HOH   A O     1 
HETATM 4151 O O     . HOH   Q 5 .   ? -18.85600 -29.02100 7.70200  1.000 58.58849 ?  670 HOH   A O     1 
HETATM 4152 O O     . HOH   Q 5 .   ? 3.84600   11.78500  27.77900 1.000 49.24771 ?  671 HOH   A O     1 
HETATM 4153 O O     . HOH   Q 5 .   ? 8.318     14.118    27.172   1.000 49.14220 ?  672 HOH   A O     1 
HETATM 4154 O O     . HOH   Q 5 .   ? -12.02400 -32.65600 37.73200 1.000 48.89784 ?  673 HOH   A O     1 
HETATM 4155 O O     . HOH   Q 5 .   ? -18.33000 -2.80400  20.64000 1.000 55.21005 ?  674 HOH   A O     1 
HETATM 4156 O O     . HOH   Q 5 .   ? -18.55400 -27.76500 36.83400 1.000 47.49401 ?  675 HOH   A O     1 
HETATM 4157 O O     . HOH   Q 5 .   ? 0.17000   -27.51200 30.37800 1.000 40.10648 ?  676 HOH   A O     1 
HETATM 4158 O O     . HOH   Q 5 .   ? -13.46600 -9.16800  16.66000 1.000 45.22309 ?  677 HOH   A O     1 
HETATM 4159 O O     . HOH   Q 5 .   ? -18.80500 -1.43600  43.25900 1.000 57.45475 ?  678 HOH   A O     1 
HETATM 4160 O O     . HOH   Q 5 .   ? -18.05700 -16.05200 43.41200 1.000 53.37752 ?  679 HOH   A O     1 
HETATM 4161 O O     . HOH   Q 5 .   ? -19.88000 -19.16400 12.63600 1.000 45.32752 ?  680 HOH   A O     1 
HETATM 4162 O O     . HOH   Q 5 .   ? 5.11600   -19.74500 28.72800 1.000 52.49977 ?  681 HOH   A O     1 
HETATM 4163 O O     . HOH   Q 5 .   ? -6.58100  -0.39800  14.41600 1.000 34.05785 ?  682 HOH   A O     1 
HETATM 4164 O O     . HOH   Q 5 .   ? 0.37700   -26.94800 36.24200 1.000 46.63201 ?  683 HOH   A O     1 
HETATM 4165 O O     . HOH   Q 5 .   ? -2.981    16.919    29.085   1.000 58.93663 ?  684 HOH   A O     1 
HETATM 4166 O O     . HOH   Q 5 .   ? -20.53800 -23.19200 37.89900 1.000 50.24717 ?  685 HOH   A O     1 
HETATM 4167 O O     . HOH   Q 5 .   ? -16.53500 -35.65500 22.20800 1.000 60.58593 ?  686 HOH   A O     1 
HETATM 4168 O O     . HOH   Q 5 .   ? -6.79300  12.47200  22.45900 1.000 51.47766 ?  687 HOH   A O     1 
HETATM 4169 O O     . HOH   Q 5 .   ? 4.09100   -17.59800 23.13900 1.000 38.89049 ?  688 HOH   A O     1 
HETATM 4170 O O     . HOH   Q 5 .   ? -24.62900 -6.45900  24.50800 1.000 50.68988 ?  689 HOH   A O     1 
HETATM 4171 O O     . HOH   Q 5 .   ? -19.29300 1.68400   43.21100 1.000 39.69115 ?  690 HOH   A O     1 
HETATM 4172 O O     . HOH   Q 5 .   ? -0.93300  -21.54200 9.28200  1.000 53.64557 ?  691 HOH   A O     1 
HETATM 4173 O O     . HOH   Q 5 .   ? 7.71200   -11.28100 20.06400 1.000 43.20736 ?  692 HOH   A O     1 
HETATM 4174 O O     . HOH   Q 5 .   ? 7.21600   1.31800   26.05900 1.000 42.99205 ?  693 HOH   A O     1 
HETATM 4175 O O     . HOH   Q 5 .   ? 5.114     5.599     21.576   1.000 53.06137 ?  694 HOH   A O     1 
HETATM 4176 O O     . HOH   Q 5 .   ? -18.235   -32.154   8.484    1.000 48.76715 ?  695 HOH   A O     1 
HETATM 4177 O O     . HOH   Q 5 .   ? 7.25900   -12.44200 17.12200 1.000 52.68563 ?  696 HOH   A O     1 
HETATM 4178 O O     . HOH   Q 5 .   ? 9.38100   -11.43300 38.62700 1.000 61.78967 ?  697 HOH   A O     1 
HETATM 4179 O O     . HOH   R 5 .   ? -30.30600 5.41800   55.10400 1.000 40.47569 ?  401 HOH   B O     1 
HETATM 4180 O O     . HOH   R 5 .   ? -40.16700 2.33600   61.66500 1.000 36.55740 ?  402 HOH   B O     1 
HETATM 4181 O O     . HOH   R 5 .   ? -40.06400 -1.93800  61.35700 1.000 37.62160 ?  403 HOH   B O     1 
HETATM 4182 O O     . HOH   R 5 .   ? -34.88900 -9.51600  44.20300 1.000 31.00027 ?  404 HOH   B O     1 
HETATM 4183 O O     . HOH   R 5 .   ? -44.87500 -2.15700  53.46800 1.000 43.97462 ?  405 HOH   B O     1 
HETATM 4184 O O     . HOH   R 5 .   ? -41.94300 21.82400  26.78600 1.000 54.37549 ?  406 HOH   B O     1 
HETATM 4185 O O     . HOH   R 5 .   ? -32.71800 3.00900   66.21100 1.000 25.24432 ?  407 HOH   B O     1 
HETATM 4186 O O     . HOH   R 5 .   ? -27.62000 -9.63600  35.43100 1.000 50.92232 ?  408 HOH   B O     1 
HETATM 4187 O O     . HOH   R 5 .   ? -47.59900 8.71500   49.26700 1.000 33.05602 ?  409 HOH   B O     1 
HETATM 4188 O O     . HOH   R 5 .   ? -34.18700 6.98000   38.47600 1.000 28.46978 ?  410 HOH   B O     1 
HETATM 4189 O O     . HOH   R 5 .   ? -29.73600 -13.54900 67.78300 1.000 41.40721 ?  411 HOH   B O     1 
HETATM 4190 O O     . HOH   R 5 .   ? -30.08500 8.13400   59.72100 1.000 26.80822 ?  412 HOH   B O     1 
HETATM 4191 O O     . HOH   R 5 .   ? -38.58600 -11.05500 57.32300 1.000 53.94878 ?  413 HOH   B O     1 
HETATM 4192 O O     . HOH   R 5 .   ? -40.67700 24.64000  39.37800 1.000 48.97648 ?  414 HOH   B O     1 
HETATM 4193 O O     . HOH   R 5 .   ? -43.81500 5.95700   51.05800 1.000 29.82574 ?  415 HOH   B O     1 
HETATM 4194 O O     . HOH   R 5 .   ? -38.28700 3.61100   40.30600 1.000 27.11872 ?  416 HOH   B O     1 
HETATM 4195 O O     . HOH   R 5 .   ? -28.66700 7.73200   45.83100 1.000 31.97866 ?  417 HOH   B O     1 
HETATM 4196 O O     . HOH   R 5 .   ? -31.99800 -10.09500 61.31900 1.000 40.70183 ?  418 HOH   B O     1 
HETATM 4197 O O     . HOH   R 5 .   ? -15.12800 12.32200  32.66500 1.000 37.82859 ?  419 HOH   B O     1 
HETATM 4198 O O     . HOH   R 5 .   ? -51.60200 -1.97700  32.38400 1.000 45.10664 ?  420 HOH   B O     1 
HETATM 4199 O O     . HOH   R 5 .   ? -32.53300 -2.44100  62.50200 1.000 39.01394 ?  421 HOH   B O     1 
HETATM 4200 O O     . HOH   R 5 .   ? -26.65300 -1.25400  43.08600 1.000 36.30080 ?  422 HOH   B O     1 
HETATM 4201 O O     . HOH   R 5 .   ? -36.73200 0.99700   24.54700 1.000 39.46882 ?  423 HOH   B O     1 
HETATM 4202 O O     . HOH   R 5 .   ? -24.47300 1.13200   48.12700 1.000 55.21835 ?  424 HOH   B O     1 
HETATM 4203 O O     . HOH   R 5 .   ? -13.61300 25.74100  38.79300 1.000 44.16228 ?  425 HOH   B O     1 
HETATM 4204 O O     . HOH   R 5 .   ? -44.34500 -13.12500 43.78000 1.000 43.09875 ?  426 HOH   B O     1 
HETATM 4205 O O     . HOH   R 5 .   ? -19.70100 4.09900   42.56100 1.000 32.05415 ?  427 HOH   B O     1 
HETATM 4206 O O     . HOH   R 5 .   ? -11.87600 29.31100  40.11800 1.000 34.18667 ?  428 HOH   B O     1 
HETATM 4207 O O     . HOH   R 5 .   ? -29.73300 26.80800  30.78700 1.000 31.81288 ?  429 HOH   B O     1 
HETATM 4208 O O     . HOH   R 5 .   ? -40.39100 7.15000   49.50200 1.000 27.00166 ?  430 HOH   B O     1 
HETATM 4209 O O     . HOH   R 5 .   ? -37.70400 0.35300   68.89800 1.000 27.79793 ?  431 HOH   B O     1 
HETATM 4210 O O     . HOH   R 5 .   ? -52.37000 -9.14100  43.60400 1.000 49.51673 ?  432 HOH   B O     1 
HETATM 4211 O O     . HOH   R 5 .   ? -41.98400 10.95500  20.98100 1.000 37.85327 ?  433 HOH   B O     1 
HETATM 4212 O O     . HOH   R 5 .   ? -43.41300 20.72200  40.55700 1.000 47.43895 ?  434 HOH   B O     1 
HETATM 4213 O O     . HOH   R 5 .   ? -29.23600 9.63200   50.42500 1.000 36.88821 ?  435 HOH   B O     1 
HETATM 4214 O O     . HOH   R 5 .   ? -41.30900 13.47600  48.63300 1.000 27.64409 ?  436 HOH   B O     1 
HETATM 4215 O O     . HOH   R 5 .   ? -32.01900 -13.11300 37.64700 1.000 47.02567 ?  437 HOH   B O     1 
HETATM 4216 O O     . HOH   R 5 .   ? -43.07600 2.78000   56.00300 1.000 38.65815 ?  438 HOH   B O     1 
HETATM 4217 O O     . HOH   R 5 .   ? -49.87400 4.28700   42.62200 1.000 30.19980 ?  439 HOH   B O     1 
HETATM 4218 O O     . HOH   R 5 .   ? -30.30800 18.17300  40.43900 1.000 22.61740 ?  440 HOH   B O     1 
HETATM 4219 O O     . HOH   R 5 .   ? -40.59500 -6.06900  32.69500 1.000 29.64022 ?  441 HOH   B O     1 
HETATM 4220 O O     . HOH   R 5 .   ? -33.61300 -10.32600 46.69300 1.000 35.82549 ?  442 HOH   B O     1 
HETATM 4221 O O     . HOH   R 5 .   ? -34.04500 23.44500  44.57600 1.000 31.92989 ?  443 HOH   B O     1 
HETATM 4222 O O     . HOH   R 5 .   ? -17.88700 30.01100  44.47700 1.000 48.01883 ?  444 HOH   B O     1 
HETATM 4223 O O     . HOH   R 5 .   ? -48.75900 11.09900  39.41800 1.000 43.46419 ?  445 HOH   B O     1 
HETATM 4224 O O     . HOH   R 5 .   ? -34.25600 -6.02000  55.94900 1.000 35.47649 ?  446 HOH   B O     1 
HETATM 4225 O O     . HOH   R 5 .   ? -20.42700 10.21300  45.47800 1.000 22.96193 ?  447 HOH   B O     1 
HETATM 4226 O O     . HOH   R 5 .   ? -20.16900 1.76600   34.40600 1.000 27.73686 ?  448 HOH   B O     1 
HETATM 4227 O O     . HOH   R 5 .   ? -41.58100 22.32700  31.97400 1.000 44.02195 ?  449 HOH   B O     1 
HETATM 4228 O O     . HOH   R 5 .   ? -29.37700 11.66400  39.56800 1.000 19.82168 ?  450 HOH   B O     1 
HETATM 4229 O O     . HOH   R 5 .   ? -29.27300 -3.43000  29.15600 1.000 35.52217 ?  451 HOH   B O     1 
HETATM 4230 O O     . HOH   R 5 .   ? -17.61200 20.44600  38.08300 1.000 30.46620 ?  452 HOH   B O     1 
HETATM 4231 O O     . HOH   R 5 .   ? -50.55100 7.35300   41.06700 1.000 39.82957 ?  453 HOH   B O     1 
HETATM 4232 O O     . HOH   R 5 .   ? -31.98400 -0.65800  66.01600 1.000 25.29382 ?  454 HOH   B O     1 
HETATM 4233 O O     . HOH   R 5 .   ? -52.36900 4.04400   31.77000 1.000 38.87031 ?  455 HOH   B O     1 
HETATM 4234 O O     . HOH   R 5 .   ? -44.40800 4.31600   22.98300 1.000 39.48755 ?  456 HOH   B O     1 
HETATM 4235 O O     . HOH   R 5 .   ? -28.82600 -4.83200  44.84400 1.000 53.07093 ?  457 HOH   B O     1 
HETATM 4236 O O     . HOH   R 5 .   ? -39.41700 17.17100  54.75100 1.000 25.15400 ?  458 HOH   B O     1 
HETATM 4237 O O     . HOH   R 5 .   ? -49.29700 2.10700   25.61400 1.000 47.98835 ?  459 HOH   B O     1 
HETATM 4238 O O     . HOH   R 5 .   ? -32.34200 24.86500  48.43800 1.000 46.98255 ?  460 HOH   B O     1 
HETATM 4239 O O     . HOH   R 5 .   ? -22.42300 1.96000   39.70100 1.000 34.58815 ?  461 HOH   B O     1 
HETATM 4240 O O     . HOH   R 5 .   ? -25.91600 -1.38100  29.86800 1.000 28.11940 ?  462 HOH   B O     1 
HETATM 4241 O O     . HOH   R 5 .   ? -37.57900 6.11400   44.68300 1.000 25.41638 ?  463 HOH   B O     1 
HETATM 4242 O O     . HOH   R 5 .   ? -37.88200 -11.07800 52.58100 1.000 49.34223 ?  464 HOH   B O     1 
HETATM 4243 O O     . HOH   R 5 .   ? -35.40600 1.62800   20.15900 1.000 48.71643 ?  465 HOH   B O     1 
HETATM 4244 O O     . HOH   R 5 .   ? -20.80800 17.96800  28.05000 1.000 40.12475 ?  466 HOH   B O     1 
HETATM 4245 O O     . HOH   R 5 .   ? -38.52300 -4.23300  66.09600 1.000 34.57015 ?  467 HOH   B O     1 
HETATM 4246 O O     . HOH   R 5 .   ? -33.42300 -4.73500  61.34400 1.000 29.58675 ?  468 HOH   B O     1 
HETATM 4247 O O     . HOH   R 5 .   ? -45.20400 -7.00100  59.71100 1.000 43.88152 ?  469 HOH   B O     1 
HETATM 4248 O O     . HOH   R 5 .   ? -28.44700 26.38100  27.54500 1.000 46.32658 ?  470 HOH   B O     1 
HETATM 4249 O O     . HOH   R 5 .   ? -25.34200 17.44800  50.56100 1.000 28.27847 ?  471 HOH   B O     1 
HETATM 4250 O O     . HOH   R 5 .   ? -48.35300 8.65900   38.46600 1.000 33.82524 ?  472 HOH   B O     1 
HETATM 4251 O O     . HOH   R 5 .   ? -43.32100 20.30000  28.63800 1.000 37.12242 ?  473 HOH   B O     1 
HETATM 4252 O O     . HOH   R 5 .   ? -46.52000 9.98700   57.68500 1.000 31.25385 ?  474 HOH   B O     1 
HETATM 4253 O O     . HOH   R 5 .   ? -39.12600 4.87800   53.84600 1.000 31.87687 ?  475 HOH   B O     1 
HETATM 4254 O O     . HOH   R 5 .   ? -6.471    30.155    37.874   1.000 38.14340 ?  476 HOH   B O     1 
HETATM 4255 O O     . HOH   R 5 .   ? -19.31800 5.87300   36.22200 1.000 23.44601 ?  477 HOH   B O     1 
HETATM 4256 O O     . HOH   R 5 .   ? -45.79200 18.45100  42.61000 1.000 51.63768 ?  478 HOH   B O     1 
HETATM 4257 O O     . HOH   R 5 .   ? -17.62800 12.91900  36.52700 1.000 32.06841 ?  479 HOH   B O     1 
HETATM 4258 O O     . HOH   R 5 .   ? -36.88000 -0.87100  56.24300 1.000 30.41473 ?  480 HOH   B O     1 
HETATM 4259 O O     . HOH   R 5 .   ? -9.74800  11.93200  42.38000 1.000 37.15951 ?  481 HOH   B O     1 
HETATM 4260 O O     . HOH   R 5 .   ? -42.06700 2.55100   22.60700 1.000 32.63933 ?  482 HOH   B O     1 
HETATM 4261 O O     . HOH   R 5 .   ? -15.45000 11.43100  50.71900 1.000 32.74835 ?  483 HOH   B O     1 
HETATM 4262 O O     . HOH   R 5 .   ? -42.71800 -10.23300 60.76400 1.000 27.05480 ?  484 HOH   B O     1 
HETATM 4263 O O     . HOH   R 5 .   ? -17.32000 13.48000  51.16400 1.000 40.34630 ?  485 HOH   B O     1 
HETATM 4264 O O     . HOH   R 5 .   ? -23.08700 9.32200   49.59000 1.000 43.72354 ?  486 HOH   B O     1 
HETATM 4265 O O     . HOH   R 5 .   ? -16.50300 7.80900   51.24800 1.000 42.38707 ?  487 HOH   B O     1 
HETATM 4266 O O     . HOH   R 5 .   ? -35.87300 -2.88800  54.83100 1.000 29.52860 ?  488 HOH   B O     1 
HETATM 4267 O O     . HOH   R 5 .   ? -25.54400 15.77700  27.36100 1.000 31.67475 ?  489 HOH   B O     1 
HETATM 4268 O O     . HOH   R 5 .   ? -32.58600 9.27900   20.65300 1.000 34.18686 ?  490 HOH   B O     1 
HETATM 4269 O O     . HOH   R 5 .   ? -36.59200 5.90900   40.37800 1.000 29.70850 ?  491 HOH   B O     1 
HETATM 4270 O O     . HOH   R 5 .   ? -15.92800 30.40500  46.64400 1.000 43.42721 ?  492 HOH   B O     1 
HETATM 4271 O O     . HOH   R 5 .   ? -21.12900 14.19900  51.12600 1.000 33.47499 ?  493 HOH   B O     1 
HETATM 4272 O O     . HOH   R 5 .   ? -39.95600 14.78200  22.98800 1.000 43.26550 ?  494 HOH   B O     1 
HETATM 4273 O O     . HOH   R 5 .   ? -38.43500 23.79200  46.04000 1.000 32.47724 ?  495 HOH   B O     1 
HETATM 4274 O O     . HOH   R 5 .   ? -27.99200 23.84000  44.11200 1.000 33.51656 ?  496 HOH   B O     1 
HETATM 4275 O O     . HOH   R 5 .   ? -48.00400 1.07000   36.34000 1.000 33.63246 ?  497 HOH   B O     1 
HETATM 4276 O O     . HOH   R 5 .   ? -39.93800 0.78200   71.08500 1.000 43.41190 ?  498 HOH   B O     1 
HETATM 4277 O O     . HOH   R 5 .   ? -10.98600 10.28900  45.26800 1.000 44.41201 ?  499 HOH   B O     1 
HETATM 4278 O O     . HOH   R 5 .   ? -30.79100 14.54000  20.62900 1.000 56.57734 ?  500 HOH   B O     1 
HETATM 4279 O O     . HOH   R 5 .   ? -20.47100 3.80300   38.83600 1.000 27.55601 ?  501 HOH   B O     1 
HETATM 4280 O O     . HOH   R 5 .   ? -37.82900 -1.51800  73.07500 1.000 26.48836 ?  502 HOH   B O     1 
HETATM 4281 O O     . HOH   R 5 .   ? -32.34500 -7.45100  31.87400 1.000 34.39248 ?  503 HOH   B O     1 
HETATM 4282 O O     . HOH   R 5 .   ? -28.84700 5.04600   20.46700 1.000 53.46008 ?  504 HOH   B O     1 
HETATM 4283 O O     . HOH   R 5 .   ? -26.43100 -7.13500  39.16600 1.000 38.19738 ?  505 HOH   B O     1 
HETATM 4284 O O     . HOH   R 5 .   ? -25.08000 5.36100   28.39600 1.000 34.40049 ?  506 HOH   B O     1 
HETATM 4285 O O     . HOH   R 5 .   ? -25.961   7.325     60.967   1.000 46.74028 ?  507 HOH   B O     1 
HETATM 4286 O O     . HOH   R 5 .   ? -37.35000 2.74800   54.05700 1.000 27.08618 ?  508 HOH   B O     1 
HETATM 4287 O O     . HOH   R 5 .   ? -34.35500 -12.84800 46.34500 1.000 55.15808 ?  509 HOH   B O     1 
HETATM 4288 O O     . HOH   R 5 .   ? -45.16700 0.29400   55.33400 1.000 39.18829 ?  510 HOH   B O     1 
HETATM 4289 O O     . HOH   R 5 .   ? -45.99700 -0.01400  26.41600 1.000 45.54380 ?  511 HOH   B O     1 
HETATM 4290 O O     . HOH   R 5 .   ? -37.18900 26.74500  39.22800 1.000 36.71928 ?  512 HOH   B O     1 
HETATM 4291 O O     . HOH   R 5 .   ? -13.15300 23.00900  38.74000 1.000 46.52239 ?  513 HOH   B O     1 
HETATM 4292 O O     . HOH   R 5 .   ? -48.68300 6.19800   53.03600 1.000 36.54612 ?  514 HOH   B O     1 
HETATM 4293 O O     . HOH   R 5 .   ? -26.95900 10.14100  50.53700 1.000 45.07424 ?  515 HOH   B O     1 
HETATM 4294 O O     . HOH   R 5 .   ? -33.23200 -3.60600  54.85800 1.000 31.11624 ?  516 HOH   B O     1 
HETATM 4295 O O     . HOH   R 5 .   ? -51.65000 4.46000   45.23200 1.000 36.21961 ?  517 HOH   B O     1 
HETATM 4296 O O     . HOH   R 5 .   ? -21.91600 16.92700  26.02800 1.000 46.06719 ?  518 HOH   B O     1 
HETATM 4297 O O     . HOH   R 5 .   ? -39.70100 6.16500   46.77200 1.000 22.46590 ?  519 HOH   B O     1 
HETATM 4298 O O     . HOH   R 5 .   ? -24.46200 18.23500  27.22400 1.000 38.47969 ?  520 HOH   B O     1 
HETATM 4299 O O     . HOH   R 5 .   ? -37.61600 7.73500   42.57200 1.000 28.98492 ?  521 HOH   B O     1 
HETATM 4300 O O     . HOH   R 5 .   ? -12.35500 7.32400   44.96900 1.000 48.89606 ?  522 HOH   B O     1 
HETATM 4301 O O     . HOH   R 5 .   ? -20.28800 27.09100  41.70400 1.000 36.41705 ?  523 HOH   B O     1 
HETATM 4302 O O     . HOH   R 5 .   ? -23.91300 -4.07500  33.64100 1.000 30.62630 ?  524 HOH   B O     1 
HETATM 4303 O O     . HOH   R 5 .   ? -35.69800 23.08900  51.22800 1.000 49.48823 ?  525 HOH   B O     1 
HETATM 4304 O O     . HOH   R 5 .   ? -40.39900 8.88800   20.71300 1.000 49.79941 ?  526 HOH   B O     1 
HETATM 4305 O O     . HOH   R 5 .   ? -32.48500 23.72300  18.28500 1.000 58.98925 ?  527 HOH   B O     1 
HETATM 4306 O O     . HOH   R 5 .   ? -27.95500 -7.80200  41.83400 1.000 39.80907 ?  528 HOH   B O     1 
HETATM 4307 O O     . HOH   R 5 .   ? -13.85300 19.43600  37.68800 1.000 55.99965 ?  529 HOH   B O     1 
HETATM 4308 O O     . HOH   R 5 .   ? -50.97000 6.78000   28.53700 1.000 56.91702 ?  530 HOH   B O     1 
HETATM 4309 O O     . HOH   R 5 .   ? -23.41000 2.75200   43.27000 1.000 47.59416 ?  531 HOH   B O     1 
HETATM 4310 O O     . HOH   R 5 .   ? -28.41900 -1.02300  28.61200 1.000 32.32213 ?  532 HOH   B O     1 
HETATM 4311 O O     . HOH   R 5 .   ? -38.793   -18.317   53.463   1.000 40.91265 ?  533 HOH   B O     1 
HETATM 4312 O O     . HOH   R 5 .   ? -56.22500 2.56700   39.58200 1.000 48.65718 ?  534 HOH   B O     1 
HETATM 4313 O O     . HOH   R 5 .   ? -49.77500 -2.70400  27.53200 1.000 55.41581 ?  535 HOH   B O     1 
HETATM 4314 O O     . HOH   R 5 .   ? -30.25800 26.08300  43.68100 1.000 43.03667 ?  536 HOH   B O     1 
HETATM 4315 O O     . HOH   R 5 .   ? -19.86100 4.25900   27.17900 1.000 41.53369 ?  537 HOH   B O     1 
HETATM 4316 O O     . HOH   R 5 .   ? -33.97800 -9.00700  33.73300 1.000 42.01505 ?  538 HOH   B O     1 
HETATM 4317 O O     . HOH   R 5 .   ? -24.06900 9.08600   47.61000 1.000 39.72672 ?  539 HOH   B O     1 
HETATM 4318 O O     . HOH   R 5 .   ? -13.88100 35.14700  40.30800 1.000 54.49748 ?  540 HOH   B O     1 
HETATM 4319 O O     . HOH   R 5 .   ? -46.97100 11.23700  19.28500 1.000 39.50436 ?  541 HOH   B O     1 
HETATM 4320 O O     . HOH   R 5 .   ? -31.67300 27.07800  41.80200 1.000 55.15639 ?  542 HOH   B O     1 
HETATM 4321 O O     . HOH   R 5 .   ? -49.40900 -3.43500  49.61800 1.000 42.48972 ?  543 HOH   B O     1 
HETATM 4322 O O     . HOH   R 5 .   ? -8.38100  26.94800  36.76500 1.000 49.00937 ?  544 HOH   B O     1 
HETATM 4323 O O     . HOH   R 5 .   ? -38.82100 -3.73300  69.13800 1.000 43.17393 ?  545 HOH   B O     1 
HETATM 4324 O O     . HOH   R 5 .   ? -52.70600 7.14800   30.17000 1.000 54.89219 ?  546 HOH   B O     1 
HETATM 4325 O O     . HOH   R 5 .   ? -47.97500 1.44500   51.60500 1.000 46.25550 ?  547 HOH   B O     1 
HETATM 4326 O O     . HOH   R 5 .   ? -14.03900 17.63300  40.63000 1.000 42.47986 ?  548 HOH   B O     1 
HETATM 4327 O O     . HOH   R 5 .   ? -51.02300 10.95600  35.97000 1.000 53.10947 ?  549 HOH   B O     1 
HETATM 4328 O O     . HOH   R 5 .   ? -28.87600 10.80400  18.50300 1.000 52.52961 ?  550 HOH   B O     1 
HETATM 4329 O O     . HOH   R 5 .   ? -47.94800 -6.71300  54.92900 1.000 49.49206 ?  551 HOH   B O     1 
HETATM 4330 O O     . HOH   R 5 .   ? -46.35200 -14.95100 43.64600 1.000 53.16958 ?  552 HOH   B O     1 
HETATM 4331 O O     . HOH   R 5 .   ? -37.81000 -16.20800 47.07300 1.000 43.55362 ?  553 HOH   B O     1 
HETATM 4332 O O     . HOH   R 5 .   ? -35.95500 14.13800  17.84700 1.000 47.59182 ?  554 HOH   B O     1 
HETATM 4333 O O     . HOH   R 5 .   ? -54.08400 6.68700   34.68000 1.000 55.52846 ?  555 HOH   B O     1 
HETATM 4334 O O     . HOH   R 5 .   ? -52.93200 -0.02800  30.62600 1.000 47.50642 ?  556 HOH   B O     1 
HETATM 4335 O O     . HOH   R 5 .   ? -41.34300 5.28400   52.75000 1.000 47.96910 ?  557 HOH   B O     1 
HETATM 4336 O O     . HOH   R 5 .   ? -34.79900 25.49100  44.14700 1.000 53.14751 ?  558 HOH   B O     1 
HETATM 4337 O O     . HOH   R 5 .   ? -37.95700 27.38300  27.21400 1.000 52.34199 ?  559 HOH   B O     1 
HETATM 4338 O O     . HOH   R 5 .   ? -3.484    26.432    42.034   1.000 35.12861 ?  560 HOH   B O     1 
HETATM 4339 O O     . HOH   R 5 .   ? -44.34900 19.85200  38.05600 1.000 44.67907 ?  561 HOH   B O     1 
HETATM 4340 O O     . HOH   R 5 .   ? -48.983   15.149    27.935   1.000 49.83468 ?  562 HOH   B O     1 
HETATM 4341 O O     . HOH   R 5 .   ? -17.69000 10.86100  25.08700 1.000 56.42403 ?  563 HOH   B O     1 
HETATM 4342 O O     . HOH   R 5 .   ? -44.92500 16.95500  46.28200 1.000 40.28377 ?  564 HOH   B O     1 
HETATM 4343 O O     . HOH   R 5 .   ? -37.16900 3.32800   19.87900 1.000 46.61242 ?  565 HOH   B O     1 
HETATM 4344 O O     . HOH   R 5 .   ? -27.25200 2.59900   45.93400 1.000 52.23393 ?  566 HOH   B O     1 
HETATM 4345 O O     . HOH   R 5 .   ? -16.03300 15.04300  35.74800 1.000 43.19451 ?  567 HOH   B O     1 
HETATM 4346 O O     . HOH   R 5 .   ? -45.31000 5.07200   58.91000 1.000 52.40152 ?  568 HOH   B O     1 
HETATM 4347 O O     . HOH   R 5 .   ? -49.56500 12.81600  43.50600 1.000 54.68867 ?  569 HOH   B O     1 
HETATM 4348 O O     . HOH   R 5 .   ? -44.52800 -1.14100  61.52100 1.000 58.28069 ?  570 HOH   B O     1 
HETATM 4349 O O     . HOH   R 5 .   ? -41.88600 18.78300  47.43700 1.000 47.61461 ?  571 HOH   B O     1 
HETATM 4350 O O     . HOH   R 5 .   ? -28.27400 9.68800   46.77800 1.000 44.48401 ?  572 HOH   B O     1 
HETATM 4351 O O     . HOH   R 5 .   ? -40.413   -14.986   55.488   1.000 40.71303 ?  573 HOH   B O     1 
HETATM 4352 O O     . HOH   R 5 .   ? -29.78600 19.84700  21.06100 1.000 55.78004 ?  574 HOH   B O     1 
HETATM 4353 O O     . HOH   R 5 .   ? -40.07100 0.39700   68.36600 1.000 55.31754 ?  575 HOH   B O     1 
HETATM 4354 O O     . HOH   R 5 .   ? -33.44000 -8.61400  55.37800 1.000 54.47608 ?  576 HOH   B O     1 
HETATM 4355 O O     . HOH   R 5 .   ? -46.69700 -2.11000  52.02000 1.000 49.88128 ?  577 HOH   B O     1 
HETATM 4356 O O     . HOH   R 5 .   ? -16.66500 17.06700  36.56400 1.000 51.15361 ?  578 HOH   B O     1 
HETATM 4357 O O     . HOH   R 5 .   ? -46.23100 18.43500  39.67800 1.000 47.14219 ?  579 HOH   B O     1 
HETATM 4358 O O     . HOH   R 5 .   ? -31.72200 22.68300  51.21900 1.000 44.05499 ?  580 HOH   B O     1 
HETATM 4359 O O     . HOH   R 5 .   ? -48.17100 17.99900  38.31000 1.000 50.04483 ?  581 HOH   B O     1 
HETATM 4360 O O     . HOH   R 5 .   ? -55.91500 2.25600   44.76500 1.000 52.24803 ?  582 HOH   B O     1 
HETATM 4361 O O     . HOH   R 5 .   ? -44.45300 23.05700  34.30800 1.000 53.51105 ?  583 HOH   B O     1 
HETATM 4362 O O     . HOH   R 5 .   ? -41.111   3.520     67.388   1.000 46.27713 ?  584 HOH   B O     1 
HETATM 4363 O O     . HOH   R 5 .   ? -13.92400 14.71800  34.16100 1.000 45.46279 ?  585 HOH   B O     1 
HETATM 4364 O O     . HOH   R 5 .   ? -28.487   2.682     61.478   1.000 40.75277 ?  586 HOH   B O     1 
HETATM 4365 O O     . HOH   R 5 .   ? -7.805    30.094    48.204   1.000 42.74185 ?  587 HOH   B O     1 
HETATM 4366 O O     . HOH   R 5 .   ? -25.24400 7.44000   27.68400 1.000 45.91130 ?  588 HOH   B O     1 
HETATM 4367 O O     . HOH   R 5 .   ? -36.57900 -1.42500  24.63600 1.000 51.56004 ?  589 HOH   B O     1 
HETATM 4368 O O     . HOH   R 5 .   ? -28.11300 0.58100   46.57900 1.000 58.94132 ?  590 HOH   B O     1 
HETATM 4369 O O     . HOH   R 5 .   ? -34.03300 28.00000  36.89600 1.000 56.30260 ?  591 HOH   B O     1 
HETATM 4370 O O     . HOH   R 5 .   ? -25.63800 2.27300   43.94000 1.000 43.01190 ?  592 HOH   B O     1 
HETATM 4371 O O     . HOH   R 5 .   ? -23.97900 0.23300   42.96900 1.000 46.95190 ?  593 HOH   B O     1 
HETATM 4372 O O     . HOH   R 5 .   ? -51.395   11.118    26.802   1.000 50.78266 ?  594 HOH   B O     1 
HETATM 4373 O O     . HOH   R 5 .   ? -24.87900 28.32100  38.83600 1.000 51.13206 ?  595 HOH   B O     1 
HETATM 4374 O O     . HOH   R 5 .   ? -23.03200 28.12200  37.56400 1.000 48.26616 ?  596 HOH   B O     1 
HETATM 4375 O O     . HOH   R 5 .   ? -42.18600 12.42600  18.72400 1.000 51.97497 ?  597 HOH   B O     1 
HETATM 4376 O O     . HOH   R 5 .   ? -50.36800 1.71900   50.19200 1.000 53.64768 ?  598 HOH   B O     1 
HETATM 4377 O O     . HOH   R 5 .   ? -12.69600 26.85300  36.64000 1.000 51.58871 ?  599 HOH   B O     1 
HETATM 4378 O O     . HOH   R 5 .   ? -43.48900 23.68100  26.69600 1.000 58.04499 ?  600 HOH   B O     1 
HETATM 4379 O O     . HOH   R 5 .   ? -49.69200 13.32900  37.67800 1.000 39.47709 ?  601 HOH   B O     1 
HETATM 4380 O O     . HOH   R 5 .   ? -22.14100 12.23100  53.06400 1.000 48.13361 ?  602 HOH   B O     1 
HETATM 4381 O O     . HOH   R 5 .   ? -18.82400 5.95900   25.76000 1.000 54.48049 ?  603 HOH   B O     1 
# 
