data_8VI1
# 
_entry.id   8VI1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   8VI1         pdb_00008vi1 10.2210/pdb8vi1/pdb 
WWPDB D_1000279910 ?            ?                   
# 
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 2025-04-02 ? 
2 'Structure model' 1 1 2025-06-18 ? 
# 
_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             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.country'                 
2 2 'Structure model' '_citation.journal_abbrev'          
3 2 'Structure model' '_citation.journal_id_ASTM'         
4 2 'Structure model' '_citation.journal_id_CSD'          
5 2 'Structure model' '_citation.journal_id_ISSN'         
6 2 'Structure model' '_citation.pdbx_database_id_DOI'    
7 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8 2 'Structure model' '_citation.title'                   
9 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VI1 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-02 
_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                 2 
_pdbx_contact_author.email              shawn.ouyang@gmail.com 
_pdbx_contact_author.name_first         Xiaohu 
_pdbx_contact_author.name_last          Ouyang 
_pdbx_contact_author.name_mi            Shawn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1600-0251 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ouyang, X.' 1 0000-0003-1600-0251 
'Kania, R.'  2 0009-0005-1505-9835 
'Cox, J.'    3 0000-0002-6247-9155 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Discovery of KIN-8741, a Highly Selective Type IIb c-Met Kinase Inhibitor with Broad Mutation Coverage and Quality Drug-Like Properties for the Treatment of Cancer.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.5c00834 
_citation.pdbx_database_id_PubMed   40459881 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ouyang, X.S.'      1  0000-0003-1600-0251 
primary 'Grandinetti, K.B.' 2  0009-0000-6917-0372 
primary 'Boren, M.'         3  ?                   
primary 'Chakravorty, S.'   4  ?                   
primary 'Chopade, S.'       5  ?                   
primary 'Jiang, P.'         6  ?                   
primary 'Kanouni, T.'       7  ?                   
primary 'Koudriakova, T.'   8  ?                   
primary 'Makwana, O.'       9  ?                   
primary 'Pack, S.K.'        10 0009-0005-5759-6268 
primary 'Perez, M.'         11 ?                   
primary 'Suriben, R.'       12 ?                   
primary 'Timple, N.'        13 ?                   
primary 'Thohan, S.'        14 ?                   
primary 'Uryu, S.'          15 ?                   
primary 'Womble, S.'        16 ?                   
primary 'Yuan, D.'          17 ?                   
primary 'Kania, R.S.'       18 ?                   
primary 'Cox, J.M.'         19 ?                   
# 
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 'Hepatocyte growth factor receptor'                                                                          
34841.332 2 2.7.10.1 ? ? ? 
2 non-polymer syn 'N-(3,5-difluoro-4-{[6-(2-hydroxyethoxy)-7-methoxyquinolin-4-yl]oxy}phenyl)-4-methoxypyridine-3-carboxamide' 
497.448   2 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'HGF receptor,HGF/SF receptor,Proto-oncogene c-Met,Scatter factor receptor,SF receptor,Tyrosine-protein kinase Met' 
# 
_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       
;GDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITD
IGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLAS
KKFVHRDLAARNCMLDEKFTVKVADFGLARNMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELM
TRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITD
IGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLAS
KKFVHRDLAARNCMLDEKFTVKVADFGLARNMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELM
TRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        
'N-(3,5-difluoro-4-{[6-(2-hydroxyethoxy)-7-methoxyquinolin-4-yl]oxy}phenyl)-4-methoxypyridine-3-carboxamide' 
_pdbx_entity_nonpoly.comp_id     A1AB1 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ASP n 
1 3   SER n 
1 4   ASP n 
1 5   ILE n 
1 6   SER n 
1 7   SER n 
1 8   PRO n 
1 9   LEU n 
1 10  LEU n 
1 11  GLN n 
1 12  ASN n 
1 13  THR n 
1 14  VAL n 
1 15  HIS n 
1 16  ILE n 
1 17  ASP n 
1 18  LEU n 
1 19  SER n 
1 20  ALA n 
1 21  LEU n 
1 22  ASN n 
1 23  PRO n 
1 24  GLU n 
1 25  LEU n 
1 26  VAL n 
1 27  GLN n 
1 28  ALA n 
1 29  VAL n 
1 30  GLN n 
1 31  HIS n 
1 32  VAL n 
1 33  VAL n 
1 34  ILE n 
1 35  GLY n 
1 36  PRO n 
1 37  SER n 
1 38  SER n 
1 39  LEU n 
1 40  ILE n 
1 41  VAL n 
1 42  HIS n 
1 43  PHE n 
1 44  ASN n 
1 45  GLU n 
1 46  VAL n 
1 47  ILE n 
1 48  GLY n 
1 49  ARG n 
1 50  GLY n 
1 51  HIS n 
1 52  PHE n 
1 53  GLY n 
1 54  CYS n 
1 55  VAL n 
1 56  TYR n 
1 57  HIS n 
1 58  GLY n 
1 59  THR n 
1 60  LEU n 
1 61  LEU n 
1 62  ASP n 
1 63  ASN n 
1 64  ASP n 
1 65  GLY n 
1 66  LYS n 
1 67  LYS n 
1 68  ILE n 
1 69  HIS n 
1 70  CYS n 
1 71  ALA n 
1 72  VAL n 
1 73  LYS n 
1 74  SER n 
1 75  LEU n 
1 76  ASN n 
1 77  ARG n 
1 78  ILE n 
1 79  THR n 
1 80  ASP n 
1 81  ILE n 
1 82  GLY n 
1 83  GLU n 
1 84  VAL n 
1 85  SER n 
1 86  GLN n 
1 87  PHE n 
1 88  LEU n 
1 89  THR n 
1 90  GLU n 
1 91  GLY n 
1 92  ILE n 
1 93  ILE n 
1 94  MET n 
1 95  LYS n 
1 96  ASP n 
1 97  PHE n 
1 98  SER n 
1 99  HIS n 
1 100 PRO n 
1 101 ASN n 
1 102 VAL n 
1 103 LEU n 
1 104 SER n 
1 105 LEU n 
1 106 LEU n 
1 107 GLY n 
1 108 ILE n 
1 109 CYS n 
1 110 LEU n 
1 111 ARG n 
1 112 SER n 
1 113 GLU n 
1 114 GLY n 
1 115 SER n 
1 116 PRO n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 LEU n 
1 121 PRO n 
1 122 TYR n 
1 123 MET n 
1 124 LYS n 
1 125 HIS n 
1 126 GLY n 
1 127 ASP n 
1 128 LEU n 
1 129 ARG n 
1 130 ASN n 
1 131 PHE n 
1 132 ILE n 
1 133 ARG n 
1 134 ASN n 
1 135 GLU n 
1 136 THR n 
1 137 HIS n 
1 138 ASN n 
1 139 PRO n 
1 140 THR n 
1 141 VAL n 
1 142 LYS n 
1 143 ASP n 
1 144 LEU n 
1 145 ILE n 
1 146 GLY n 
1 147 PHE n 
1 148 GLY n 
1 149 LEU n 
1 150 GLN n 
1 151 VAL n 
1 152 ALA n 
1 153 LYS n 
1 154 GLY n 
1 155 MET n 
1 156 LYS n 
1 157 TYR n 
1 158 LEU n 
1 159 ALA n 
1 160 SER n 
1 161 LYS n 
1 162 LYS n 
1 163 PHE n 
1 164 VAL n 
1 165 HIS n 
1 166 ARG n 
1 167 ASP n 
1 168 LEU n 
1 169 ALA n 
1 170 ALA n 
1 171 ARG n 
1 172 ASN n 
1 173 CYS n 
1 174 MET n 
1 175 LEU n 
1 176 ASP n 
1 177 GLU n 
1 178 LYS n 
1 179 PHE n 
1 180 THR n 
1 181 VAL n 
1 182 LYS n 
1 183 VAL n 
1 184 ALA n 
1 185 ASP n 
1 186 PHE n 
1 187 GLY n 
1 188 LEU n 
1 189 ALA n 
1 190 ARG n 
1 191 ASN n 
1 192 MET n 
1 193 TYR n 
1 194 ASP n 
1 195 LYS n 
1 196 GLU n 
1 197 TYR n 
1 198 TYR n 
1 199 SER n 
1 200 VAL n 
1 201 HIS n 
1 202 ASN n 
1 203 LYS n 
1 204 THR n 
1 205 GLY n 
1 206 ALA n 
1 207 LYS n 
1 208 LEU n 
1 209 PRO n 
1 210 VAL n 
1 211 LYS n 
1 212 TRP n 
1 213 MET n 
1 214 ALA n 
1 215 LEU n 
1 216 GLU n 
1 217 SER n 
1 218 LEU n 
1 219 GLN n 
1 220 THR n 
1 221 GLN n 
1 222 LYS n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 LYS n 
1 227 SER n 
1 228 ASP n 
1 229 VAL n 
1 230 TRP n 
1 231 SER n 
1 232 PHE n 
1 233 GLY n 
1 234 VAL n 
1 235 LEU n 
1 236 LEU n 
1 237 TRP n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 THR n 
1 242 ARG n 
1 243 GLY n 
1 244 ALA n 
1 245 PRO n 
1 246 PRO n 
1 247 TYR n 
1 248 PRO n 
1 249 ASP n 
1 250 VAL n 
1 251 ASN n 
1 252 THR n 
1 253 PHE n 
1 254 ASP n 
1 255 ILE n 
1 256 THR n 
1 257 VAL n 
1 258 TYR n 
1 259 LEU n 
1 260 LEU n 
1 261 GLN n 
1 262 GLY n 
1 263 ARG n 
1 264 ARG n 
1 265 LEU n 
1 266 LEU n 
1 267 GLN n 
1 268 PRO n 
1 269 GLU n 
1 270 TYR n 
1 271 CYS n 
1 272 PRO n 
1 273 ASP n 
1 274 PRO n 
1 275 LEU n 
1 276 TYR n 
1 277 GLU n 
1 278 VAL n 
1 279 MET n 
1 280 LEU n 
1 281 LYS n 
1 282 CYS n 
1 283 TRP n 
1 284 HIS n 
1 285 PRO n 
1 286 LYS n 
1 287 ALA n 
1 288 GLU n 
1 289 MET n 
1 290 ARG n 
1 291 PRO n 
1 292 SER n 
1 293 PHE n 
1 294 SER n 
1 295 GLU n 
1 296 LEU n 
1 297 VAL n 
1 298 SER n 
1 299 ARG n 
1 300 ILE n 
1 301 SER n 
1 302 ALA n 
1 303 ILE n 
1 304 PHE n 
1 305 SER n 
1 306 THR n 
1 307 PHE n 
1 308 ILE n 
1 309 GLY 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                   309 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 MET 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1AB1 non-polymer         . 
'N-(3,5-difluoro-4-{[6-(2-hydroxyethoxy)-7-methoxyquinolin-4-yl]oxy}phenyl)-4-methoxypyridine-3-carboxamide' ? 'C25 H21 F2 N3 O6' 
497.448 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'   156.162 
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
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   GLY 1   1038 ?    ?   ?   A . n 
A 1 2   ASP 2   1039 ?    ?   ?   A . n 
A 1 3   SER 3   1040 ?    ?   ?   A . n 
A 1 4   ASP 4   1041 ?    ?   ?   A . n 
A 1 5   ILE 5   1042 ?    ?   ?   A . n 
A 1 6   SER 6   1043 ?    ?   ?   A . n 
A 1 7   SER 7   1044 ?    ?   ?   A . n 
A 1 8   PRO 8   1045 ?    ?   ?   A . n 
A 1 9   LEU 9   1046 ?    ?   ?   A . n 
A 1 10  LEU 10  1047 ?    ?   ?   A . n 
A 1 11  GLN 11  1048 ?    ?   ?   A . n 
A 1 12  ASN 12  1049 ?    ?   ?   A . n 
A 1 13  THR 13  1050 ?    ?   ?   A . n 
A 1 14  VAL 14  1051 ?    ?   ?   A . n 
A 1 15  HIS 15  1052 ?    ?   ?   A . n 
A 1 16  ILE 16  1053 1053 ILE ILE A . n 
A 1 17  ASP 17  1054 1054 ASP ASP A . n 
A 1 18  LEU 18  1055 1055 LEU LEU A . n 
A 1 19  SER 19  1056 1056 SER SER A . n 
A 1 20  ALA 20  1057 1057 ALA ALA A . n 
A 1 21  LEU 21  1058 1058 LEU LEU A . n 
A 1 22  ASN 22  1059 1059 ASN ASN A . n 
A 1 23  PRO 23  1060 1060 PRO PRO A . n 
A 1 24  GLU 24  1061 1061 GLU GLU A . n 
A 1 25  LEU 25  1062 1062 LEU LEU A . n 
A 1 26  VAL 26  1063 1063 VAL VAL A . n 
A 1 27  GLN 27  1064 1064 GLN GLN A . n 
A 1 28  ALA 28  1065 1065 ALA ALA A . n 
A 1 29  VAL 29  1066 1066 VAL VAL A . n 
A 1 30  GLN 30  1067 1067 GLN GLN A . n 
A 1 31  HIS 31  1068 1068 HIS HIS A . n 
A 1 32  VAL 32  1069 1069 VAL VAL A . n 
A 1 33  VAL 33  1070 1070 VAL VAL A . n 
A 1 34  ILE 34  1071 1071 ILE ILE A . n 
A 1 35  GLY 35  1072 1072 GLY GLY A . n 
A 1 36  PRO 36  1073 1073 PRO PRO A . n 
A 1 37  SER 37  1074 1074 SER SER A . n 
A 1 38  SER 38  1075 1075 SER SER A . n 
A 1 39  LEU 39  1076 1076 LEU LEU A . n 
A 1 40  ILE 40  1077 1077 ILE ILE A . n 
A 1 41  VAL 41  1078 1078 VAL VAL A . n 
A 1 42  HIS 42  1079 1079 HIS HIS A . n 
A 1 43  PHE 43  1080 1080 PHE PHE A . n 
A 1 44  ASN 44  1081 1081 ASN ASN A . n 
A 1 45  GLU 45  1082 1082 GLU GLU A . n 
A 1 46  VAL 46  1083 1083 VAL VAL A . n 
A 1 47  ILE 47  1084 1084 ILE ILE A . n 
A 1 48  GLY 48  1085 1085 GLY GLY A . n 
A 1 49  ARG 49  1086 1086 ARG ARG A . n 
A 1 50  GLY 50  1087 1087 GLY GLY A . n 
A 1 51  HIS 51  1088 1088 HIS HIS A . n 
A 1 52  PHE 52  1089 1089 PHE PHE A . n 
A 1 53  GLY 53  1090 1090 GLY GLY A . n 
A 1 54  CYS 54  1091 1091 CYS CYS A . n 
A 1 55  VAL 55  1092 1092 VAL VAL A . n 
A 1 56  TYR 56  1093 1093 TYR TYR A . n 
A 1 57  HIS 57  1094 1094 HIS HIS A . n 
A 1 58  GLY 58  1095 1095 GLY GLY A . n 
A 1 59  THR 59  1096 1096 THR THR A . n 
A 1 60  LEU 60  1097 1097 LEU LEU A . n 
A 1 61  LEU 61  1098 1098 LEU LEU A . n 
A 1 62  ASP 62  1099 1099 ASP ASP A . n 
A 1 63  ASN 63  1100 1100 ASN ASN A . n 
A 1 64  ASP 64  1101 1101 ASP ASP A . n 
A 1 65  GLY 65  1102 1102 GLY GLY A . n 
A 1 66  LYS 66  1103 1103 LYS LYS A . n 
A 1 67  LYS 67  1104 1104 LYS LYS A . n 
A 1 68  ILE 68  1105 1105 ILE ILE A . n 
A 1 69  HIS 69  1106 1106 HIS HIS A . n 
A 1 70  CYS 70  1107 1107 CYS CYS A . n 
A 1 71  ALA 71  1108 1108 ALA ALA A . n 
A 1 72  VAL 72  1109 1109 VAL VAL A . n 
A 1 73  LYS 73  1110 1110 LYS LYS A . n 
A 1 74  SER 74  1111 1111 SER SER A . n 
A 1 75  LEU 75  1112 1112 LEU LEU A . n 
A 1 76  ASN 76  1113 1113 ASN ASN A . n 
A 1 77  ARG 77  1114 1114 ARG ARG A . n 
A 1 78  ILE 78  1115 1115 ILE ILE A . n 
A 1 79  THR 79  1116 1116 THR THR A . n 
A 1 80  ASP 80  1117 ?    ?   ?   A . n 
A 1 81  ILE 81  1118 ?    ?   ?   A . n 
A 1 82  GLY 82  1119 ?    ?   ?   A . n 
A 1 83  GLU 83  1120 1120 GLU GLU A . n 
A 1 84  VAL 84  1121 1121 VAL VAL A . n 
A 1 85  SER 85  1122 1122 SER SER A . n 
A 1 86  GLN 86  1123 1123 GLN GLN A . n 
A 1 87  PHE 87  1124 1124 PHE PHE A . n 
A 1 88  LEU 88  1125 1125 LEU LEU A . n 
A 1 89  THR 89  1126 1126 THR THR A . n 
A 1 90  GLU 90  1127 1127 GLU GLU A . n 
A 1 91  GLY 91  1128 1128 GLY GLY A . n 
A 1 92  ILE 92  1129 1129 ILE ILE A . n 
A 1 93  ILE 93  1130 1130 ILE ILE A . n 
A 1 94  MET 94  1131 1131 MET MET A . n 
A 1 95  LYS 95  1132 1132 LYS LYS A . n 
A 1 96  ASP 96  1133 1133 ASP ASP A . n 
A 1 97  PHE 97  1134 1134 PHE PHE A . n 
A 1 98  SER 98  1135 1135 SER SER A . n 
A 1 99  HIS 99  1136 1136 HIS HIS A . n 
A 1 100 PRO 100 1137 1137 PRO PRO A . n 
A 1 101 ASN 101 1138 1138 ASN ASN A . n 
A 1 102 VAL 102 1139 1139 VAL VAL A . n 
A 1 103 LEU 103 1140 1140 LEU LEU A . n 
A 1 104 SER 104 1141 1141 SER SER A . n 
A 1 105 LEU 105 1142 1142 LEU LEU A . n 
A 1 106 LEU 106 1143 1143 LEU LEU A . n 
A 1 107 GLY 107 1144 1144 GLY GLY A . n 
A 1 108 ILE 108 1145 1145 ILE ILE A . n 
A 1 109 CYS 109 1146 1146 CYS CYS A . n 
A 1 110 LEU 110 1147 1147 LEU LEU A . n 
A 1 111 ARG 111 1148 1148 ARG ARG A . n 
A 1 112 SER 112 1149 1149 SER SER A . n 
A 1 113 GLU 113 1150 1150 GLU GLU A . n 
A 1 114 GLY 114 1151 1151 GLY GLY A . n 
A 1 115 SER 115 1152 1152 SER SER A . n 
A 1 116 PRO 116 1153 1153 PRO PRO A . n 
A 1 117 LEU 117 1154 1154 LEU LEU A . n 
A 1 118 VAL 118 1155 1155 VAL VAL A . n 
A 1 119 VAL 119 1156 1156 VAL VAL A . n 
A 1 120 LEU 120 1157 1157 LEU LEU A . n 
A 1 121 PRO 121 1158 1158 PRO PRO A . n 
A 1 122 TYR 122 1159 1159 TYR TYR A . n 
A 1 123 MET 123 1160 1160 MET MET A . n 
A 1 124 LYS 124 1161 1161 LYS LYS A . n 
A 1 125 HIS 125 1162 1162 HIS HIS A . n 
A 1 126 GLY 126 1163 1163 GLY GLY A . n 
A 1 127 ASP 127 1164 1164 ASP ASP A . n 
A 1 128 LEU 128 1165 1165 LEU LEU A . n 
A 1 129 ARG 129 1166 1166 ARG ARG A . n 
A 1 130 ASN 130 1167 1167 ASN ASN A . n 
A 1 131 PHE 131 1168 1168 PHE PHE A . n 
A 1 132 ILE 132 1169 1169 ILE ILE A . n 
A 1 133 ARG 133 1170 1170 ARG ARG A . n 
A 1 134 ASN 134 1171 1171 ASN ASN A . n 
A 1 135 GLU 135 1172 1172 GLU GLU A . n 
A 1 136 THR 136 1173 1173 THR THR A . n 
A 1 137 HIS 137 1174 1174 HIS HIS A . n 
A 1 138 ASN 138 1175 1175 ASN ASN A . n 
A 1 139 PRO 139 1176 1176 PRO PRO A . n 
A 1 140 THR 140 1177 1177 THR THR A . n 
A 1 141 VAL 141 1178 1178 VAL VAL A . n 
A 1 142 LYS 142 1179 1179 LYS LYS A . n 
A 1 143 ASP 143 1180 1180 ASP ASP A . n 
A 1 144 LEU 144 1181 1181 LEU LEU A . n 
A 1 145 ILE 145 1182 1182 ILE ILE A . n 
A 1 146 GLY 146 1183 1183 GLY GLY A . n 
A 1 147 PHE 147 1184 1184 PHE PHE A . n 
A 1 148 GLY 148 1185 1185 GLY GLY A . n 
A 1 149 LEU 149 1186 1186 LEU LEU A . n 
A 1 150 GLN 150 1187 1187 GLN GLN A . n 
A 1 151 VAL 151 1188 1188 VAL VAL A . n 
A 1 152 ALA 152 1189 1189 ALA ALA A . n 
A 1 153 LYS 153 1190 1190 LYS LYS A . n 
A 1 154 GLY 154 1191 1191 GLY GLY A . n 
A 1 155 MET 155 1192 1192 MET MET A . n 
A 1 156 LYS 156 1193 1193 LYS LYS A . n 
A 1 157 TYR 157 1194 1194 TYR TYR A . n 
A 1 158 LEU 158 1195 1195 LEU LEU A . n 
A 1 159 ALA 159 1196 1196 ALA ALA A . n 
A 1 160 SER 160 1197 1197 SER SER A . n 
A 1 161 LYS 161 1198 1198 LYS LYS A . n 
A 1 162 LYS 162 1199 1199 LYS LYS A . n 
A 1 163 PHE 163 1200 1200 PHE PHE A . n 
A 1 164 VAL 164 1201 1201 VAL VAL A . n 
A 1 165 HIS 165 1202 1202 HIS HIS A . n 
A 1 166 ARG 166 1203 1203 ARG ARG A . n 
A 1 167 ASP 167 1204 1204 ASP ASP A . n 
A 1 168 LEU 168 1205 1205 LEU LEU A . n 
A 1 169 ALA 169 1206 1206 ALA ALA A . n 
A 1 170 ALA 170 1207 1207 ALA ALA A . n 
A 1 171 ARG 171 1208 1208 ARG ARG A . n 
A 1 172 ASN 172 1209 1209 ASN ASN A . n 
A 1 173 CYS 173 1210 1210 CYS CYS A . n 
A 1 174 MET 174 1211 1211 MET MET A . n 
A 1 175 LEU 175 1212 1212 LEU LEU A . n 
A 1 176 ASP 176 1213 1213 ASP ASP A . n 
A 1 177 GLU 177 1214 1214 GLU GLU A . n 
A 1 178 LYS 178 1215 1215 LYS LYS A . n 
A 1 179 PHE 179 1216 1216 PHE PHE A . n 
A 1 180 THR 180 1217 1217 THR THR A . n 
A 1 181 VAL 181 1218 1218 VAL VAL A . n 
A 1 182 LYS 182 1219 1219 LYS LYS A . n 
A 1 183 VAL 183 1220 1220 VAL VAL A . n 
A 1 184 ALA 184 1221 1221 ALA ALA A . n 
A 1 185 ASP 185 1222 1222 ASP ASP A . n 
A 1 186 PHE 186 1223 1223 PHE PHE A . n 
A 1 187 GLY 187 1224 1224 GLY GLY A . n 
A 1 188 LEU 188 1225 1225 LEU LEU A . n 
A 1 189 ALA 189 1226 1226 ALA ALA A . n 
A 1 190 ARG 190 1227 1227 ARG ARG A . n 
A 1 191 ASN 191 1228 1228 ASN ASN A . n 
A 1 192 MET 192 1229 1229 MET MET A . n 
A 1 193 TYR 193 1230 ?    ?   ?   A . n 
A 1 194 ASP 194 1231 ?    ?   ?   A . n 
A 1 195 LYS 195 1232 ?    ?   ?   A . n 
A 1 196 GLU 196 1233 1233 GLU GLU A . n 
A 1 197 TYR 197 1234 1234 TYR TYR A . n 
A 1 198 TYR 198 1235 1235 TYR TYR A . n 
A 1 199 SER 199 1236 1236 SER SER A . n 
A 1 200 VAL 200 1237 1237 VAL VAL A . n 
A 1 201 HIS 201 1238 1238 HIS HIS A . n 
A 1 202 ASN 202 1239 ?    ?   ?   A . n 
A 1 203 LYS 203 1240 ?    ?   ?   A . n 
A 1 204 THR 204 1241 ?    ?   ?   A . n 
A 1 205 GLY 205 1242 ?    ?   ?   A . n 
A 1 206 ALA 206 1243 1243 ALA ALA A . n 
A 1 207 LYS 207 1244 1244 LYS LYS A . n 
A 1 208 LEU 208 1245 1245 LEU LEU A . n 
A 1 209 PRO 209 1246 1246 PRO PRO A . n 
A 1 210 VAL 210 1247 1247 VAL VAL A . n 
A 1 211 LYS 211 1248 1248 LYS LYS A . n 
A 1 212 TRP 212 1249 1249 TRP TRP A . n 
A 1 213 MET 213 1250 1250 MET MET A . n 
A 1 214 ALA 214 1251 1251 ALA ALA A . n 
A 1 215 LEU 215 1252 1252 LEU LEU A . n 
A 1 216 GLU 216 1253 1253 GLU GLU A . n 
A 1 217 SER 217 1254 1254 SER SER A . n 
A 1 218 LEU 218 1255 1255 LEU LEU A . n 
A 1 219 GLN 219 1256 1256 GLN GLN A . n 
A 1 220 THR 220 1257 1257 THR THR A . n 
A 1 221 GLN 221 1258 1258 GLN GLN A . n 
A 1 222 LYS 222 1259 1259 LYS LYS A . n 
A 1 223 PHE 223 1260 1260 PHE PHE A . n 
A 1 224 THR 224 1261 1261 THR THR A . n 
A 1 225 THR 225 1262 1262 THR THR A . n 
A 1 226 LYS 226 1263 1263 LYS LYS A . n 
A 1 227 SER 227 1264 1264 SER SER A . n 
A 1 228 ASP 228 1265 1265 ASP ASP A . n 
A 1 229 VAL 229 1266 1266 VAL VAL A . n 
A 1 230 TRP 230 1267 1267 TRP TRP A . n 
A 1 231 SER 231 1268 1268 SER SER A . n 
A 1 232 PHE 232 1269 1269 PHE PHE A . n 
A 1 233 GLY 233 1270 1270 GLY GLY A . n 
A 1 234 VAL 234 1271 1271 VAL VAL A . n 
A 1 235 LEU 235 1272 1272 LEU LEU A . n 
A 1 236 LEU 236 1273 1273 LEU LEU A . n 
A 1 237 TRP 237 1274 1274 TRP TRP A . n 
A 1 238 GLU 238 1275 1275 GLU GLU A . n 
A 1 239 LEU 239 1276 1276 LEU LEU A . n 
A 1 240 MET 240 1277 1277 MET MET A . n 
A 1 241 THR 241 1278 1278 THR THR A . n 
A 1 242 ARG 242 1279 1279 ARG ARG A . n 
A 1 243 GLY 243 1280 1280 GLY GLY A . n 
A 1 244 ALA 244 1281 1281 ALA ALA A . n 
A 1 245 PRO 245 1282 1282 PRO PRO A . n 
A 1 246 PRO 246 1283 1283 PRO PRO A . n 
A 1 247 TYR 247 1284 1284 TYR TYR A . n 
A 1 248 PRO 248 1285 1285 PRO PRO A . n 
A 1 249 ASP 249 1286 1286 ASP ASP A . n 
A 1 250 VAL 250 1287 1287 VAL VAL A . n 
A 1 251 ASN 251 1288 1288 ASN ASN A . n 
A 1 252 THR 252 1289 1289 THR THR A . n 
A 1 253 PHE 253 1290 1290 PHE PHE A . n 
A 1 254 ASP 254 1291 1291 ASP ASP A . n 
A 1 255 ILE 255 1292 1292 ILE ILE A . n 
A 1 256 THR 256 1293 1293 THR THR A . n 
A 1 257 VAL 257 1294 1294 VAL VAL A . n 
A 1 258 TYR 258 1295 1295 TYR TYR A . n 
A 1 259 LEU 259 1296 1296 LEU LEU A . n 
A 1 260 LEU 260 1297 1297 LEU LEU A . n 
A 1 261 GLN 261 1298 1298 GLN GLN A . n 
A 1 262 GLY 262 1299 1299 GLY GLY A . n 
A 1 263 ARG 263 1300 1300 ARG ARG A . n 
A 1 264 ARG 264 1301 1301 ARG ARG A . n 
A 1 265 LEU 265 1302 1302 LEU LEU A . n 
A 1 266 LEU 266 1303 1303 LEU LEU A . n 
A 1 267 GLN 267 1304 1304 GLN GLN A . n 
A 1 268 PRO 268 1305 1305 PRO PRO A . n 
A 1 269 GLU 269 1306 1306 GLU GLU A . n 
A 1 270 TYR 270 1307 1307 TYR TYR A . n 
A 1 271 CYS 271 1308 1308 CYS CYS A . n 
A 1 272 PRO 272 1309 1309 PRO PRO A . n 
A 1 273 ASP 273 1310 1310 ASP ASP A . n 
A 1 274 PRO 274 1311 1311 PRO PRO A . n 
A 1 275 LEU 275 1312 1312 LEU LEU A . n 
A 1 276 TYR 276 1313 1313 TYR TYR A . n 
A 1 277 GLU 277 1314 1314 GLU GLU A . n 
A 1 278 VAL 278 1315 1315 VAL VAL A . n 
A 1 279 MET 279 1316 1316 MET MET A . n 
A 1 280 LEU 280 1317 1317 LEU LEU A . n 
A 1 281 LYS 281 1318 1318 LYS LYS A . n 
A 1 282 CYS 282 1319 1319 CYS CYS A . n 
A 1 283 TRP 283 1320 1320 TRP TRP A . n 
A 1 284 HIS 284 1321 1321 HIS HIS A . n 
A 1 285 PRO 285 1322 1322 PRO PRO A . n 
A 1 286 LYS 286 1323 1323 LYS LYS A . n 
A 1 287 ALA 287 1324 1324 ALA ALA A . n 
A 1 288 GLU 288 1325 1325 GLU GLU A . n 
A 1 289 MET 289 1326 1326 MET MET A . n 
A 1 290 ARG 290 1327 1327 ARG ARG A . n 
A 1 291 PRO 291 1328 1328 PRO PRO A . n 
A 1 292 SER 292 1329 1329 SER SER A . n 
A 1 293 PHE 293 1330 1330 PHE PHE A . n 
A 1 294 SER 294 1331 1331 SER SER A . n 
A 1 295 GLU 295 1332 1332 GLU GLU A . n 
A 1 296 LEU 296 1333 1333 LEU LEU A . n 
A 1 297 VAL 297 1334 1334 VAL VAL A . n 
A 1 298 SER 298 1335 1335 SER SER A . n 
A 1 299 ARG 299 1336 1336 ARG ARG A . n 
A 1 300 ILE 300 1337 1337 ILE ILE A . n 
A 1 301 SER 301 1338 1338 SER SER A . n 
A 1 302 ALA 302 1339 1339 ALA ALA A . n 
A 1 303 ILE 303 1340 1340 ILE ILE A . n 
A 1 304 PHE 304 1341 1341 PHE PHE A . n 
A 1 305 SER 305 1342 1342 SER SER A . n 
A 1 306 THR 306 1343 1343 THR THR A . n 
A 1 307 PHE 307 1344 1344 PHE PHE A . n 
A 1 308 ILE 308 1345 1345 ILE ILE A . n 
A 1 309 GLY 309 1346 1346 GLY GLY A . n 
B 1 1   GLY 1   1038 ?    ?   ?   B . n 
B 1 2   ASP 2   1039 ?    ?   ?   B . n 
B 1 3   SER 3   1040 ?    ?   ?   B . n 
B 1 4   ASP 4   1041 ?    ?   ?   B . n 
B 1 5   ILE 5   1042 ?    ?   ?   B . n 
B 1 6   SER 6   1043 ?    ?   ?   B . n 
B 1 7   SER 7   1044 ?    ?   ?   B . n 
B 1 8   PRO 8   1045 ?    ?   ?   B . n 
B 1 9   LEU 9   1046 ?    ?   ?   B . n 
B 1 10  LEU 10  1047 ?    ?   ?   B . n 
B 1 11  GLN 11  1048 ?    ?   ?   B . n 
B 1 12  ASN 12  1049 ?    ?   ?   B . n 
B 1 13  THR 13  1050 1050 THR THR B . n 
B 1 14  VAL 14  1051 1051 VAL VAL B . n 
B 1 15  HIS 15  1052 1052 HIS HIS B . n 
B 1 16  ILE 16  1053 1053 ILE ILE B . n 
B 1 17  ASP 17  1054 1054 ASP ASP B . n 
B 1 18  LEU 18  1055 1055 LEU LEU B . n 
B 1 19  SER 19  1056 1056 SER SER B . n 
B 1 20  ALA 20  1057 1057 ALA ALA B . n 
B 1 21  LEU 21  1058 1058 LEU LEU B . n 
B 1 22  ASN 22  1059 1059 ASN ASN B . n 
B 1 23  PRO 23  1060 1060 PRO PRO B . n 
B 1 24  GLU 24  1061 1061 GLU GLU B . n 
B 1 25  LEU 25  1062 1062 LEU LEU B . n 
B 1 26  VAL 26  1063 1063 VAL VAL B . n 
B 1 27  GLN 27  1064 1064 GLN GLN B . n 
B 1 28  ALA 28  1065 1065 ALA ALA B . n 
B 1 29  VAL 29  1066 1066 VAL VAL B . n 
B 1 30  GLN 30  1067 1067 GLN GLN B . n 
B 1 31  HIS 31  1068 1068 HIS HIS B . n 
B 1 32  VAL 32  1069 1069 VAL VAL B . n 
B 1 33  VAL 33  1070 1070 VAL VAL B . n 
B 1 34  ILE 34  1071 1071 ILE ILE B . n 
B 1 35  GLY 35  1072 1072 GLY GLY B . n 
B 1 36  PRO 36  1073 1073 PRO PRO B . n 
B 1 37  SER 37  1074 1074 SER SER B . n 
B 1 38  SER 38  1075 1075 SER SER B . n 
B 1 39  LEU 39  1076 1076 LEU LEU B . n 
B 1 40  ILE 40  1077 1077 ILE ILE B . n 
B 1 41  VAL 41  1078 1078 VAL VAL B . n 
B 1 42  HIS 42  1079 1079 HIS HIS B . n 
B 1 43  PHE 43  1080 1080 PHE PHE B . n 
B 1 44  ASN 44  1081 1081 ASN ASN B . n 
B 1 45  GLU 45  1082 1082 GLU GLU B . n 
B 1 46  VAL 46  1083 1083 VAL VAL B . n 
B 1 47  ILE 47  1084 1084 ILE ILE B . n 
B 1 48  GLY 48  1085 1085 GLY GLY B . n 
B 1 49  ARG 49  1086 1086 ARG ARG B . n 
B 1 50  GLY 50  1087 1087 GLY GLY B . n 
B 1 51  HIS 51  1088 1088 HIS HIS B . n 
B 1 52  PHE 52  1089 1089 PHE PHE B . n 
B 1 53  GLY 53  1090 1090 GLY GLY B . n 
B 1 54  CYS 54  1091 1091 CYS CYS B . n 
B 1 55  VAL 55  1092 1092 VAL VAL B . n 
B 1 56  TYR 56  1093 1093 TYR TYR B . n 
B 1 57  HIS 57  1094 1094 HIS HIS B . n 
B 1 58  GLY 58  1095 1095 GLY GLY B . n 
B 1 59  THR 59  1096 1096 THR THR B . n 
B 1 60  LEU 60  1097 1097 LEU LEU B . n 
B 1 61  LEU 61  1098 1098 LEU LEU B . n 
B 1 62  ASP 62  1099 1099 ASP ASP B . n 
B 1 63  ASN 63  1100 1100 ASN ASN B . n 
B 1 64  ASP 64  1101 1101 ASP ASP B . n 
B 1 65  GLY 65  1102 1102 GLY GLY B . n 
B 1 66  LYS 66  1103 1103 LYS LYS B . n 
B 1 67  LYS 67  1104 1104 LYS LYS B . n 
B 1 68  ILE 68  1105 1105 ILE ILE B . n 
B 1 69  HIS 69  1106 1106 HIS HIS B . n 
B 1 70  CYS 70  1107 1107 CYS CYS B . n 
B 1 71  ALA 71  1108 1108 ALA ALA B . n 
B 1 72  VAL 72  1109 1109 VAL VAL B . n 
B 1 73  LYS 73  1110 1110 LYS LYS B . n 
B 1 74  SER 74  1111 1111 SER SER B . n 
B 1 75  LEU 75  1112 1112 LEU LEU B . n 
B 1 76  ASN 76  1113 1113 ASN ASN B . n 
B 1 77  ARG 77  1114 1114 ARG ARG B . n 
B 1 78  ILE 78  1115 1115 ILE ILE B . n 
B 1 79  THR 79  1116 1116 THR THR B . n 
B 1 80  ASP 80  1117 1117 ASP ASP B . n 
B 1 81  ILE 81  1118 1118 ILE ILE B . n 
B 1 82  GLY 82  1119 1119 GLY GLY B . n 
B 1 83  GLU 83  1120 1120 GLU GLU B . n 
B 1 84  VAL 84  1121 1121 VAL VAL B . n 
B 1 85  SER 85  1122 1122 SER SER B . n 
B 1 86  GLN 86  1123 1123 GLN GLN B . n 
B 1 87  PHE 87  1124 1124 PHE PHE B . n 
B 1 88  LEU 88  1125 1125 LEU LEU B . n 
B 1 89  THR 89  1126 1126 THR THR B . n 
B 1 90  GLU 90  1127 1127 GLU GLU B . n 
B 1 91  GLY 91  1128 1128 GLY GLY B . n 
B 1 92  ILE 92  1129 1129 ILE ILE B . n 
B 1 93  ILE 93  1130 1130 ILE ILE B . n 
B 1 94  MET 94  1131 1131 MET MET B . n 
B 1 95  LYS 95  1132 1132 LYS LYS B . n 
B 1 96  ASP 96  1133 1133 ASP ASP B . n 
B 1 97  PHE 97  1134 1134 PHE PHE B . n 
B 1 98  SER 98  1135 1135 SER SER B . n 
B 1 99  HIS 99  1136 1136 HIS HIS B . n 
B 1 100 PRO 100 1137 1137 PRO PRO B . n 
B 1 101 ASN 101 1138 1138 ASN ASN B . n 
B 1 102 VAL 102 1139 1139 VAL VAL B . n 
B 1 103 LEU 103 1140 1140 LEU LEU B . n 
B 1 104 SER 104 1141 1141 SER SER B . n 
B 1 105 LEU 105 1142 1142 LEU LEU B . n 
B 1 106 LEU 106 1143 1143 LEU LEU B . n 
B 1 107 GLY 107 1144 1144 GLY GLY B . n 
B 1 108 ILE 108 1145 1145 ILE ILE B . n 
B 1 109 CYS 109 1146 1146 CYS CYS B . n 
B 1 110 LEU 110 1147 1147 LEU LEU B . n 
B 1 111 ARG 111 1148 1148 ARG ARG B . n 
B 1 112 SER 112 1149 1149 SER SER B . n 
B 1 113 GLU 113 1150 1150 GLU GLU B . n 
B 1 114 GLY 114 1151 1151 GLY GLY B . n 
B 1 115 SER 115 1152 1152 SER SER B . n 
B 1 116 PRO 116 1153 1153 PRO PRO B . n 
B 1 117 LEU 117 1154 1154 LEU LEU B . n 
B 1 118 VAL 118 1155 1155 VAL VAL B . n 
B 1 119 VAL 119 1156 1156 VAL VAL B . n 
B 1 120 LEU 120 1157 1157 LEU LEU B . n 
B 1 121 PRO 121 1158 1158 PRO PRO B . n 
B 1 122 TYR 122 1159 1159 TYR TYR B . n 
B 1 123 MET 123 1160 1160 MET MET B . n 
B 1 124 LYS 124 1161 1161 LYS LYS B . n 
B 1 125 HIS 125 1162 1162 HIS HIS B . n 
B 1 126 GLY 126 1163 1163 GLY GLY B . n 
B 1 127 ASP 127 1164 1164 ASP ASP B . n 
B 1 128 LEU 128 1165 1165 LEU LEU B . n 
B 1 129 ARG 129 1166 1166 ARG ARG B . n 
B 1 130 ASN 130 1167 1167 ASN ASN B . n 
B 1 131 PHE 131 1168 1168 PHE PHE B . n 
B 1 132 ILE 132 1169 1169 ILE ILE B . n 
B 1 133 ARG 133 1170 1170 ARG ARG B . n 
B 1 134 ASN 134 1171 1171 ASN ASN B . n 
B 1 135 GLU 135 1172 1172 GLU GLU B . n 
B 1 136 THR 136 1173 1173 THR THR B . n 
B 1 137 HIS 137 1174 1174 HIS HIS B . n 
B 1 138 ASN 138 1175 1175 ASN ASN B . n 
B 1 139 PRO 139 1176 1176 PRO PRO B . n 
B 1 140 THR 140 1177 1177 THR THR B . n 
B 1 141 VAL 141 1178 1178 VAL VAL B . n 
B 1 142 LYS 142 1179 1179 LYS LYS B . n 
B 1 143 ASP 143 1180 1180 ASP ASP B . n 
B 1 144 LEU 144 1181 1181 LEU LEU B . n 
B 1 145 ILE 145 1182 1182 ILE ILE B . n 
B 1 146 GLY 146 1183 1183 GLY GLY B . n 
B 1 147 PHE 147 1184 1184 PHE PHE B . n 
B 1 148 GLY 148 1185 1185 GLY GLY B . n 
B 1 149 LEU 149 1186 1186 LEU LEU B . n 
B 1 150 GLN 150 1187 1187 GLN GLN B . n 
B 1 151 VAL 151 1188 1188 VAL VAL B . n 
B 1 152 ALA 152 1189 1189 ALA ALA B . n 
B 1 153 LYS 153 1190 1190 LYS LYS B . n 
B 1 154 GLY 154 1191 1191 GLY GLY B . n 
B 1 155 MET 155 1192 1192 MET MET B . n 
B 1 156 LYS 156 1193 1193 LYS LYS B . n 
B 1 157 TYR 157 1194 1194 TYR TYR B . n 
B 1 158 LEU 158 1195 1195 LEU LEU B . n 
B 1 159 ALA 159 1196 1196 ALA ALA B . n 
B 1 160 SER 160 1197 1197 SER SER B . n 
B 1 161 LYS 161 1198 1198 LYS LYS B . n 
B 1 162 LYS 162 1199 1199 LYS LYS B . n 
B 1 163 PHE 163 1200 1200 PHE PHE B . n 
B 1 164 VAL 164 1201 1201 VAL VAL B . n 
B 1 165 HIS 165 1202 1202 HIS HIS B . n 
B 1 166 ARG 166 1203 1203 ARG ARG B . n 
B 1 167 ASP 167 1204 1204 ASP ASP B . n 
B 1 168 LEU 168 1205 1205 LEU LEU B . n 
B 1 169 ALA 169 1206 1206 ALA ALA B . n 
B 1 170 ALA 170 1207 1207 ALA ALA B . n 
B 1 171 ARG 171 1208 1208 ARG ARG B . n 
B 1 172 ASN 172 1209 1209 ASN ASN B . n 
B 1 173 CYS 173 1210 1210 CYS CYS B . n 
B 1 174 MET 174 1211 1211 MET MET B . n 
B 1 175 LEU 175 1212 1212 LEU LEU B . n 
B 1 176 ASP 176 1213 1213 ASP ASP B . n 
B 1 177 GLU 177 1214 1214 GLU GLU B . n 
B 1 178 LYS 178 1215 1215 LYS LYS B . n 
B 1 179 PHE 179 1216 1216 PHE PHE B . n 
B 1 180 THR 180 1217 1217 THR THR B . n 
B 1 181 VAL 181 1218 1218 VAL VAL B . n 
B 1 182 LYS 182 1219 1219 LYS LYS B . n 
B 1 183 VAL 183 1220 1220 VAL VAL B . n 
B 1 184 ALA 184 1221 1221 ALA ALA B . n 
B 1 185 ASP 185 1222 1222 ASP ASP B . n 
B 1 186 PHE 186 1223 1223 PHE PHE B . n 
B 1 187 GLY 187 1224 1224 GLY GLY B . n 
B 1 188 LEU 188 1225 1225 LEU LEU B . n 
B 1 189 ALA 189 1226 1226 ALA ALA B . n 
B 1 190 ARG 190 1227 1227 ARG ARG B . n 
B 1 191 ASN 191 1228 1228 ASN ASN B . n 
B 1 192 MET 192 1229 1229 MET MET B . n 
B 1 193 TYR 193 1230 1230 TYR TYR B . n 
B 1 194 ASP 194 1231 1231 ASP ASP B . n 
B 1 195 LYS 195 1232 1232 LYS LYS B . n 
B 1 196 GLU 196 1233 1233 GLU GLU B . n 
B 1 197 TYR 197 1234 ?    ?   ?   B . n 
B 1 198 TYR 198 1235 ?    ?   ?   B . n 
B 1 199 SER 199 1236 ?    ?   ?   B . n 
B 1 200 VAL 200 1237 ?    ?   ?   B . n 
B 1 201 HIS 201 1238 ?    ?   ?   B . n 
B 1 202 ASN 202 1239 ?    ?   ?   B . n 
B 1 203 LYS 203 1240 ?    ?   ?   B . n 
B 1 204 THR 204 1241 ?    ?   ?   B . n 
B 1 205 GLY 205 1242 ?    ?   ?   B . n 
B 1 206 ALA 206 1243 1243 ALA ALA B . n 
B 1 207 LYS 207 1244 1244 LYS LYS B . n 
B 1 208 LEU 208 1245 1245 LEU LEU B . n 
B 1 209 PRO 209 1246 1246 PRO PRO B . n 
B 1 210 VAL 210 1247 1247 VAL VAL B . n 
B 1 211 LYS 211 1248 1248 LYS LYS B . n 
B 1 212 TRP 212 1249 1249 TRP TRP B . n 
B 1 213 MET 213 1250 1250 MET MET B . n 
B 1 214 ALA 214 1251 1251 ALA ALA B . n 
B 1 215 LEU 215 1252 1252 LEU LEU B . n 
B 1 216 GLU 216 1253 1253 GLU GLU B . n 
B 1 217 SER 217 1254 1254 SER SER B . n 
B 1 218 LEU 218 1255 1255 LEU LEU B . n 
B 1 219 GLN 219 1256 1256 GLN GLN B . n 
B 1 220 THR 220 1257 1257 THR THR B . n 
B 1 221 GLN 221 1258 1258 GLN GLN B . n 
B 1 222 LYS 222 1259 1259 LYS LYS B . n 
B 1 223 PHE 223 1260 1260 PHE PHE B . n 
B 1 224 THR 224 1261 1261 THR THR B . n 
B 1 225 THR 225 1262 1262 THR THR B . n 
B 1 226 LYS 226 1263 1263 LYS LYS B . n 
B 1 227 SER 227 1264 1264 SER SER B . n 
B 1 228 ASP 228 1265 1265 ASP ASP B . n 
B 1 229 VAL 229 1266 1266 VAL VAL B . n 
B 1 230 TRP 230 1267 1267 TRP TRP B . n 
B 1 231 SER 231 1268 1268 SER SER B . n 
B 1 232 PHE 232 1269 1269 PHE PHE B . n 
B 1 233 GLY 233 1270 1270 GLY GLY B . n 
B 1 234 VAL 234 1271 1271 VAL VAL B . n 
B 1 235 LEU 235 1272 1272 LEU LEU B . n 
B 1 236 LEU 236 1273 1273 LEU LEU B . n 
B 1 237 TRP 237 1274 1274 TRP TRP B . n 
B 1 238 GLU 238 1275 1275 GLU GLU B . n 
B 1 239 LEU 239 1276 1276 LEU LEU B . n 
B 1 240 MET 240 1277 1277 MET MET B . n 
B 1 241 THR 241 1278 1278 THR THR B . n 
B 1 242 ARG 242 1279 1279 ARG ARG B . n 
B 1 243 GLY 243 1280 1280 GLY GLY B . n 
B 1 244 ALA 244 1281 1281 ALA ALA B . n 
B 1 245 PRO 245 1282 1282 PRO PRO B . n 
B 1 246 PRO 246 1283 1283 PRO PRO B . n 
B 1 247 TYR 247 1284 1284 TYR TYR B . n 
B 1 248 PRO 248 1285 1285 PRO PRO B . n 
B 1 249 ASP 249 1286 1286 ASP ASP B . n 
B 1 250 VAL 250 1287 1287 VAL VAL B . n 
B 1 251 ASN 251 1288 1288 ASN ASN B . n 
B 1 252 THR 252 1289 1289 THR THR B . n 
B 1 253 PHE 253 1290 1290 PHE PHE B . n 
B 1 254 ASP 254 1291 1291 ASP ASP B . n 
B 1 255 ILE 255 1292 1292 ILE ILE B . n 
B 1 256 THR 256 1293 1293 THR THR B . n 
B 1 257 VAL 257 1294 1294 VAL VAL B . n 
B 1 258 TYR 258 1295 1295 TYR TYR B . n 
B 1 259 LEU 259 1296 1296 LEU LEU B . n 
B 1 260 LEU 260 1297 1297 LEU LEU B . n 
B 1 261 GLN 261 1298 1298 GLN GLN B . n 
B 1 262 GLY 262 1299 1299 GLY GLY B . n 
B 1 263 ARG 263 1300 1300 ARG ARG B . n 
B 1 264 ARG 264 1301 1301 ARG ARG B . n 
B 1 265 LEU 265 1302 1302 LEU LEU B . n 
B 1 266 LEU 266 1303 1303 LEU LEU B . n 
B 1 267 GLN 267 1304 1304 GLN GLN B . n 
B 1 268 PRO 268 1305 1305 PRO PRO B . n 
B 1 269 GLU 269 1306 1306 GLU GLU B . n 
B 1 270 TYR 270 1307 1307 TYR TYR B . n 
B 1 271 CYS 271 1308 1308 CYS CYS B . n 
B 1 272 PRO 272 1309 1309 PRO PRO B . n 
B 1 273 ASP 273 1310 1310 ASP ASP B . n 
B 1 274 PRO 274 1311 1311 PRO PRO B . n 
B 1 275 LEU 275 1312 1312 LEU LEU B . n 
B 1 276 TYR 276 1313 1313 TYR TYR B . n 
B 1 277 GLU 277 1314 1314 GLU GLU B . n 
B 1 278 VAL 278 1315 1315 VAL VAL B . n 
B 1 279 MET 279 1316 1316 MET MET B . n 
B 1 280 LEU 280 1317 1317 LEU LEU B . n 
B 1 281 LYS 281 1318 1318 LYS LYS B . n 
B 1 282 CYS 282 1319 1319 CYS CYS B . n 
B 1 283 TRP 283 1320 1320 TRP TRP B . n 
B 1 284 HIS 284 1321 1321 HIS HIS B . n 
B 1 285 PRO 285 1322 1322 PRO PRO B . n 
B 1 286 LYS 286 1323 1323 LYS LYS B . n 
B 1 287 ALA 287 1324 1324 ALA ALA B . n 
B 1 288 GLU 288 1325 1325 GLU GLU B . n 
B 1 289 MET 289 1326 1326 MET MET B . n 
B 1 290 ARG 290 1327 1327 ARG ARG B . n 
B 1 291 PRO 291 1328 1328 PRO PRO B . n 
B 1 292 SER 292 1329 1329 SER SER B . n 
B 1 293 PHE 293 1330 1330 PHE PHE B . n 
B 1 294 SER 294 1331 1331 SER SER B . n 
B 1 295 GLU 295 1332 1332 GLU GLU B . n 
B 1 296 LEU 296 1333 1333 LEU LEU B . n 
B 1 297 VAL 297 1334 1334 VAL VAL B . n 
B 1 298 SER 298 1335 1335 SER SER B . n 
B 1 299 ARG 299 1336 1336 ARG ARG B . n 
B 1 300 ILE 300 1337 1337 ILE ILE B . n 
B 1 301 SER 301 1338 1338 SER SER B . n 
B 1 302 ALA 302 1339 1339 ALA ALA B . n 
B 1 303 ILE 303 1340 1340 ILE ILE B . n 
B 1 304 PHE 304 1341 1341 PHE PHE B . n 
B 1 305 SER 305 1342 1342 SER SER B . n 
B 1 306 THR 306 1343 1343 THR THR B . n 
B 1 307 PHE 307 1344 1344 PHE PHE B . n 
B 1 308 ILE 308 1345 1345 ILE ILE B . n 
B 1 309 GLY 309 1346 ?    ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AB1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AB1 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_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 A1AB1 1 1401 1 A1AB1 LIG A . 
D 2 A1AB1 1 1401 2 A1AB1 LIG B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0352 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.84 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VI1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.660 
_cell.length_a_esd                 ? 
_cell.length_b                     69.820 
_cell.length_b_esd                 ? 
_cell.length_c                     78.060 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8VI1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   8VI1 
_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             2.87 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.08 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.1M HEPES pH7.5, 12.5% PEG4000, 10% isopropanol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-14 
_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   1.00000 
_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                        'SPRING-8 BEAMLINE BL45XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL45XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8VI1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.11 
_reflns.d_resolution_low                               43.83 
_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                                     11252 
_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                           78.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.105 
_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                                    3.11 
_reflns_shell.d_res_low                                     3.32 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             384 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.372 
_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]                            0.27 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.26 
_refine.aniso_B[2][2]                            0.02 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.33 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               72.851 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.877 
_refine.correlation_coeff_Fo_to_Fc_free          0.804 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8VI1 
_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                            3.11 
_refine.ls_d_res_low                             43.83 
_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                     10751 
_refine.ls_number_reflns_R_free                  500 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    78.20 
_refine.ls_percent_reflns_R_free                 4.4 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.25310 
_refine.ls_R_factor_R_free                       0.29791 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.25112 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.669 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             64.504 
_refine.overall_SU_ML                            0.488 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.11 
_refine_hist.d_res_low                        43.83 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               4617 
_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        4545 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.002 0.012  4732  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001 0.016  4418  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.610 1.654  6408  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.230 1.565  10276 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 4.335 5.000  565   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.509 10.000 26    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.965 10.000 819   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.029 0.200  711   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.002 0.020  5241  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001 0.020  943   ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 0.344 3.859  2278  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.344 3.859  2278  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 0.649 5.783  2837  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 0.649 5.785  2838  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 0.163 3.867  2454  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.163 3.867  2455  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 0.349 5.808  3572  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.314 49.546 5360  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 2.313 49.542 5361  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       3.11 
_refine_ls_shell.d_res_low                        3.190 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             4 
_refine_ls_shell.number_reflns_R_work             74 
_refine_ls_shell.percent_reflns_obs               7.31 
_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                  0.282 
_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                  0.361 
# 
_struct.entry_id                     8VI1 
_struct.title                        'Crystal structure of c-Met-D1228N in complex with KIN-7615' 
_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        8VI1 
_struct_keywords.text            'c-Met D1228N KIN-7615, 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 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MET_HUMAN 
_struct_ref.pdbx_db_accession          P08581 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITD
IGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLAS
KKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELM
TRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIG
;
_struct_ref.pdbx_align_begin           1038 
# 
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 8VI1 A 1 ? 309 ? P08581 1038 ? 1346 ? 1038 1346 
2 1 8VI1 B 1 ? 309 ? P08581 1038 ? 1346 ? 1038 1346 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8VI1 ASN A 191 ? UNP P08581 ASP 1228 variant 1228 1 
2 8VI1 ASN B 191 ? UNP P08581 ASP 1228 variant 1228 2 
# 
_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)' 4230  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  27850 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 PRO A 23  ? VAL A 29  ? PRO A 1060 VAL A 1066 1 ? 7  
HELX_P HELX_P2  AA2 GLY A 35  ? SER A 37  ? GLY A 1072 SER A 1074 5 ? 3  
HELX_P HELX_P3  AA3 GLY A 48  ? HIS A 51  ? GLY A 1085 HIS A 1088 5 ? 4  
HELX_P HELX_P4  AA4 VAL A 84  ? ASP A 96  ? VAL A 1121 ASP A 1133 1 ? 13 
HELX_P HELX_P5  AA5 LEU A 128 ? ASN A 134 ? LEU A 1165 ASN A 1171 1 ? 7  
HELX_P HELX_P6  AA6 THR A 140 ? LYS A 161 ? THR A 1177 LYS A 1198 1 ? 22 
HELX_P HELX_P7  AA7 ALA A 169 ? ARG A 171 ? ALA A 1206 ARG A 1208 5 ? 3  
HELX_P HELX_P8  AA8 ALA A 214 ? GLN A 221 ? ALA A 1251 GLN A 1258 1 ? 8  
HELX_P HELX_P9  AA9 THR A 224 ? THR A 241 ? THR A 1261 THR A 1278 1 ? 18 
HELX_P HELX_P10 AB1 ASP A 254 ? GLN A 261 ? ASP A 1291 GLN A 1298 1 ? 8  
HELX_P HELX_P11 AB2 PRO A 272 ? TRP A 283 ? PRO A 1309 TRP A 1320 1 ? 12 
HELX_P HELX_P12 AB3 SER A 292 ? SER A 305 ? SER A 1329 SER A 1342 1 ? 14 
HELX_P HELX_P13 AB4 ASP B 17  ? LEU B 21  ? ASP B 1054 LEU B 1058 5 ? 5  
HELX_P HELX_P14 AB5 ASN B 22  ? ALA B 28  ? ASN B 1059 ALA B 1065 1 ? 7  
HELX_P HELX_P15 AB6 ASN B 63  ? GLY B 65  ? ASN B 1100 GLY B 1102 5 ? 3  
HELX_P HELX_P16 AB7 ASP B 80  ? PHE B 97  ? ASP B 1117 PHE B 1134 1 ? 18 
HELX_P HELX_P17 AB8 LEU B 128 ? ASN B 134 ? LEU B 1165 ASN B 1171 1 ? 7  
HELX_P HELX_P18 AB9 THR B 140 ? LYS B 161 ? THR B 1177 LYS B 1198 1 ? 22 
HELX_P HELX_P19 AC1 GLY B 187 ? LYS B 195 ? GLY B 1224 LYS B 1232 1 ? 9  
HELX_P HELX_P20 AC2 ALA B 214 ? THR B 220 ? ALA B 1251 THR B 1257 1 ? 7  
HELX_P HELX_P21 AC3 THR B 224 ? THR B 241 ? THR B 1261 THR B 1278 1 ? 18 
HELX_P HELX_P22 AC4 ASN B 251 ? PHE B 253 ? ASN B 1288 PHE B 1290 5 ? 3  
HELX_P HELX_P23 AC5 ASP B 254 ? GLN B 261 ? ASP B 1291 GLN B 1298 1 ? 8  
HELX_P HELX_P24 AC6 PRO B 272 ? TRP B 283 ? PRO B 1309 TRP B 1320 1 ? 12 
HELX_P HELX_P25 AC7 SER B 292 ? PHE B 307 ? SER B 1329 PHE B 1344 1 ? 16 
# 
_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 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 5 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
# 
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 LEU A 39  ? VAL A 46  ? LEU A 1076 VAL A 1083 
AA1 2 VAL A 55  ? LEU A 61  ? VAL A 1092 LEU A 1098 
AA1 3 LYS A 67  ? SER A 74  ? LYS A 1104 SER A 1111 
AA1 4 LEU A 117 ? PRO A 121 ? LEU A 1154 PRO A 1158 
AA1 5 GLY A 107 ? CYS A 109 ? GLY A 1144 CYS A 1146 
AA2 1 GLY A 126 ? ASP A 127 ? GLY A 1163 ASP A 1164 
AA2 2 CYS A 173 ? LEU A 175 ? CYS A 1210 LEU A 1212 
AA2 3 VAL A 181 ? VAL A 183 ? VAL A 1218 VAL A 1220 
AA3 1 LEU B 39  ? ARG B 49  ? LEU B 1076 ARG B 1086 
AA3 2 CYS B 54  ? LEU B 61  ? CYS B 1091 LEU B 1098 
AA3 3 LYS B 67  ? SER B 74  ? LYS B 1104 SER B 1111 
AA3 4 LEU B 117 ? PRO B 121 ? LEU B 1154 PRO B 1158 
AA3 5 GLY B 107 ? CYS B 109 ? GLY B 1144 CYS B 1146 
AA4 1 GLY B 126 ? ASP B 127 ? GLY B 1163 ASP B 1164 
AA4 2 CYS B 173 ? LEU B 175 ? CYS B 1210 LEU B 1212 
AA4 3 VAL B 181 ? VAL B 183 ? VAL B 1218 VAL B 1220 
# 
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 N ILE A 40  ? N ILE A 1077 O THR A 59  ? O THR A 1096 
AA1 2 3 N TYR A 56  ? N TYR A 1093 O VAL A 72  ? O VAL A 1109 
AA1 3 4 N ALA A 71  ? N ALA A 1108 O LEU A 120 ? O LEU A 1157 
AA1 4 5 O LEU A 117 ? O LEU A 1154 N CYS A 109 ? N CYS A 1146 
AA2 1 2 N GLY A 126 ? N GLY A 1163 O LEU A 175 ? O LEU A 1212 
AA2 2 3 N MET A 174 ? N MET A 1211 O LYS A 182 ? O LYS A 1219 
AA3 1 2 N HIS B 42  ? N HIS B 1079 O HIS B 57  ? O HIS B 1094 
AA3 2 3 N LEU B 60  ? N LEU B 1097 O ILE B 68  ? O ILE B 1105 
AA3 3 4 N ALA B 71  ? N ALA B 1108 O LEU B 120 ? O LEU B 1157 
AA3 4 5 O VAL B 119 ? O VAL B 1156 N GLY B 107 ? N GLY B 1144 
AA4 1 2 N GLY B 126 ? N GLY B 1163 O LEU B 175 ? O LEU B 1212 
AA4 2 3 N MET B 174 ? N MET B 1211 O LYS B 182 ? O LYS B 1219 
# 
_pdbx_entry_details.entry_id                   8VI1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 ASN A 1059 ? ? -32.39  117.51 
2  1 VAL A 1066 ? ? -106.95 50.47  
3  1 SER A 1075 ? ? -100.45 50.04  
4  1 LEU A 1076 ? ? -167.73 112.47 
5  1 PHE A 1089 ? ? -103.61 45.40  
6  1 ASN A 1113 ? ? -99.91  58.44  
7  1 ARG A 1114 ? ? -145.89 49.21  
8  1 ASP A 1133 ? ? -92.72  32.34  
9  1 SER A 1135 ? ? -160.24 106.86 
10 1 ARG A 1203 ? ? 80.85   -53.90 
11 1 ASP A 1204 ? ? -111.56 68.40  
12 1 TRP A 1320 ? ? -94.37  45.27  
13 1 ASP B 1204 ? ? -167.46 55.44  
14 1 ASN B 1209 ? ? -99.48  32.01  
15 1 GLN B 1256 ? ? -90.89  -64.59 
16 1 TYR B 1307 ? ? -106.32 63.60  
17 1 TRP B 1320 ? ? -95.68  54.46  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 8.6416   14.9793  27.1084 0.3851 ? -0.1130 ? -0.0115 ? 0.4870 ? -0.0258 ? 0.3042 ? 0.9436 ? 
-2.1928 ? 0.1470  ? 8.0594  ? -3.2772 ? 2.9681 ? 0.1259  ? 0.0631  ? -0.0046 ? -0.2517 ? -0.1070 ? -0.0423 ? -0.0898 ? -0.0566 ? 
-0.0189 ? 
2  'X-RAY DIFFRACTION' ? refined 17.7583  -3.5941  16.0126 0.1873 ? -0.0590 ? 0.0648  ? 0.3552 ? 0.0455  ? 0.1868 ? 4.2851 ? 
1.1378  ? 2.8615  ? 9.1466  ? 3.9785  ? 4.7692 ? 0.0553  ? 0.2735  ? -0.0365 ? -0.1554 ? 0.1597  ? -0.2384 ? 0.1055  ? 0.5191  ? 
-0.2150 ? 
3  'X-RAY DIFFRACTION' ? refined 10.9636  2.0667   25.1511 0.6546 ? -0.2839 ? -0.1545 ? 0.6314 ? 0.0975  ? 0.9362 ? 3.1179 ? 
0.7444  ? -2.8838 ? 4.5725  ? 0.6978  ? 4.1147 ? 0.6068  ? 0.2325  ? 0.7807  ? 0.2004  ? -0.2802 ? -0.6653 ? -1.1773 ? -0.0145 ? 
-0.3266 ? 
4  'X-RAY DIFFRACTION' ? refined 4.6983   -14.8797 27.3634 0.2210 ? -0.0463 ? -0.0054 ? 0.2329 ? 0.0766  ? 0.2223 ? 3.9024 ? 
1.4393  ? -1.4271 ? 4.6029  ? 0.2558  ? 4.7308 ? 0.1128  ? 0.1186  ? -0.1567 ? 0.0207  ? -0.2093 ? -0.9561 ? 0.2881  ? 0.5021  ? 
0.0965  ? 
5  'X-RAY DIFFRACTION' ? refined -3.3755  -1.5184  16.8843 0.5887 ? -0.2033 ? -0.0565 ? 0.7335 ? 0.0950  ? 0.5078 ? 5.1691 ? 
-7.1303 ? 4.0764  ? 9.9053  ? -5.6136 ? 3.2455 ? -0.6346 ? -0.0938 ? 0.3044  ? 0.8867  ? 0.3318  ? -0.3280 ? -0.6178 ? -0.0154 ? 
0.3028  ? 
6  'X-RAY DIFFRACTION' ? refined -10.3065 -12.9698 21.9167 0.0298 ? -0.0337 ? 0.0103  ? 0.0605 ? -0.0319 ? 0.0481 ? 7.0294 ? 
-5.5733 ? 0.9160  ? 6.3147  ? -0.6846 ? 5.8889 ? 0.1167  ? -0.1233 ? -0.3786 ? -0.1614 ? -0.0087 ? 0.4320  ? -0.1240 ? 0.0587  ? 
-0.1080 ? 
7  'X-RAY DIFFRACTION' ? refined -11.5516 -22.3560 26.2291 0.1408 ? -0.0837 ? 0.0549  ? 0.1132 ? -0.0030 ? 0.1890 ? 3.7653 ? 
-0.4203 ? 1.5114  ? 4.1529  ? -0.2722 ? 6.1416 ? 0.0865  ? -0.1316 ? -0.6178 ? 0.1220  ? 0.0753  ? 0.5792  ? 0.5222  ? -0.0942 ? 
-0.1617 ? 
8  'X-RAY DIFFRACTION' ? refined -16.3449 37.6619  -1.4561 0.4220 ? -0.0453 ? 0.0297  ? 0.7240 ? 0.1153  ? 0.5103 ? 0.8968 ? 
-2.6980 ? -0.8962 ? 12.2090 ? 0.4066  ? 2.3038 ? 0.2349  ? -0.0979 ? 0.1507  ? -0.7612 ? -0.1298 ? -0.2531 ? -0.0969 ? 0.5583  ? 
-0.1051 ? 
9  'X-RAY DIFFRACTION' ? refined -17.3482 29.1612  13.4605 0.2835 ? -0.2025 ? -0.0186 ? 0.2697 ? -0.0623 ? 0.4425 ? 1.5401 ? 
-3.3184 ? 0.6828  ? 9.4728  ? 0.0424  ? 5.4598 ? -0.1938 ? -0.0131 ? -0.1776 ? 0.4998  ? -0.1184 ? 0.6523  ? -0.5512 ? -0.0235 ? 
0.3122  ? 
10 'X-RAY DIFFRACTION' ? refined -26.2098 19.7728  9.0014  0.0738 ? -0.0255 ? 0.0579  ? 0.2449 ? -0.0313 ? 0.4220 ? 1.1689 ? 
0.4947  ? 0.4760  ? 7.5064  ? -2.1929 ? 2.4693 ? 0.0951  ? -0.1814 ? 0.1372  ? 0.0969  ? 0.1818  ? 0.6556  ? -0.2900 ? -0.0486 ? 
-0.2769 ? 
11 'X-RAY DIFFRACTION' ? refined -21.5438 11.5861  2.5775  0.3950 ? 0.0241  ? 0.0878  ? 0.2926 ? 0.1410  ? 0.6009 ? 0.6070 ? 
-0.4284 ? 1.7166  ? 3.8192  ? 0.1017  ? 6.7813 ? 0.2140  ? 0.1977  ? 0.1154  ? -1.1077 ? 0.1239  ? 0.3299  ? -0.0311 ? 0.3689  ? 
-0.3378 ? 
12 'X-RAY DIFFRACTION' ? refined -26.3489 -2.8086  5.7036  0.2876 ? -0.1437 ? -0.1824 ? 0.1235 ? 0.0269  ? 0.3173 ? 5.3467 ? 
-2.1016 ? 0.4514  ? 6.0354  ? -0.4387 ? 3.7581 ? 0.1486  ? 0.0993  ? -0.1035 ? -0.8187 ? -0.0246 ? 1.1238  ? 0.4569  ? -0.3496 ? 
-0.1240 ? 
13 'X-RAY DIFFRACTION' ? refined -41.3194 3.4751   9.0189  0.1567 ? -0.0119 ? -0.0734 ? 0.3131 ? 0.0041  ? 0.3727 ? 6.5522 ? 
5.4147  ? -4.1662 ? 10.2577 ? -9.3307 ? 8.6478 ? -0.0080 ? -0.0591 ? 0.1083  ? 0.0838  ? 0.1023  ? 0.1034  ? -0.0960 ? -0.1460 ? 
-0.0943 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? A 1053 ? ? ? A 1072 ? ? ? 
2  'X-RAY DIFFRACTION' 2  ? ? A 1073 ? ? ? A 1091 ? ? ? 
3  'X-RAY DIFFRACTION' 3  ? ? A 1092 ? ? ? A 1152 ? ? ? 
4  'X-RAY DIFFRACTION' 4  ? ? A 1153 ? ? ? A 1217 ? ? ? 
5  'X-RAY DIFFRACTION' 5  ? ? A 1218 ? ? ? A 1238 ? ? ? 
6  'X-RAY DIFFRACTION' 6  ? ? A 1243 ? ? ? A 1278 ? ? ? 
7  'X-RAY DIFFRACTION' 7  ? ? A 1279 ? ? ? A 1346 ? ? ? 
8  'X-RAY DIFFRACTION' 8  ? ? B 1050 ? ? ? B 1075 ? ? ? 
9  'X-RAY DIFFRACTION' 9  ? ? B 1076 ? ? ? B 1117 ? ? ? 
10 'X-RAY DIFFRACTION' 10 ? ? B 1118 ? ? ? B 1197 ? ? ? 
11 'X-RAY DIFFRACTION' 11 ? ? B 1198 ? ? ? B 1261 ? ? ? 
12 'X-RAY DIFFRACTION' 12 ? ? B 1262 ? ? ? B 1329 ? ? ? 
13 'X-RAY DIFFRACTION' 13 ? ? B 1330 ? ? ? B 1345 ? ? ? 
# 
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 GLY 1038 ? A GLY 1   
2  1 Y 1 A ASP 1039 ? A ASP 2   
3  1 Y 1 A SER 1040 ? A SER 3   
4  1 Y 1 A ASP 1041 ? A ASP 4   
5  1 Y 1 A ILE 1042 ? A ILE 5   
6  1 Y 1 A SER 1043 ? A SER 6   
7  1 Y 1 A SER 1044 ? A SER 7   
8  1 Y 1 A PRO 1045 ? A PRO 8   
9  1 Y 1 A LEU 1046 ? A LEU 9   
10 1 Y 1 A LEU 1047 ? A LEU 10  
11 1 Y 1 A GLN 1048 ? A GLN 11  
12 1 Y 1 A ASN 1049 ? A ASN 12  
13 1 Y 1 A THR 1050 ? A THR 13  
14 1 Y 1 A VAL 1051 ? A VAL 14  
15 1 Y 1 A HIS 1052 ? A HIS 15  
16 1 Y 1 A ASP 1117 ? A ASP 80  
17 1 Y 1 A ILE 1118 ? A ILE 81  
18 1 Y 1 A GLY 1119 ? A GLY 82  
19 1 Y 1 A TYR 1230 ? A TYR 193 
20 1 Y 1 A ASP 1231 ? A ASP 194 
21 1 Y 1 A LYS 1232 ? A LYS 195 
22 1 Y 1 A ASN 1239 ? A ASN 202 
23 1 Y 1 A LYS 1240 ? A LYS 203 
24 1 Y 1 A THR 1241 ? A THR 204 
25 1 Y 1 A GLY 1242 ? A GLY 205 
26 1 Y 1 B GLY 1038 ? B GLY 1   
27 1 Y 1 B ASP 1039 ? B ASP 2   
28 1 Y 1 B SER 1040 ? B SER 3   
29 1 Y 1 B ASP 1041 ? B ASP 4   
30 1 Y 1 B ILE 1042 ? B ILE 5   
31 1 Y 1 B SER 1043 ? B SER 6   
32 1 Y 1 B SER 1044 ? B SER 7   
33 1 Y 1 B PRO 1045 ? B PRO 8   
34 1 Y 1 B LEU 1046 ? B LEU 9   
35 1 Y 1 B LEU 1047 ? B LEU 10  
36 1 Y 1 B GLN 1048 ? B GLN 11  
37 1 Y 1 B ASN 1049 ? B ASN 12  
38 1 Y 1 B TYR 1234 ? B TYR 197 
39 1 Y 1 B TYR 1235 ? B TYR 198 
40 1 Y 1 B SER 1236 ? B SER 199 
41 1 Y 1 B VAL 1237 ? B VAL 200 
42 1 Y 1 B HIS 1238 ? B HIS 201 
43 1 Y 1 B ASN 1239 ? B ASN 202 
44 1 Y 1 B LYS 1240 ? B LYS 203 
45 1 Y 1 B THR 1241 ? B THR 204 
46 1 Y 1 B GLY 1242 ? B GLY 205 
47 1 Y 1 B GLY 1346 ? B GLY 309 
# 
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 
A1AB1 C4   C Y N 1   
A1AB1 C5   C Y N 2   
A1AB1 C6   C Y N 3   
A1AB1 C8   C Y N 4   
A1AB1 C10  C Y N 5   
A1AB1 C13  C Y N 6   
A1AB1 C15  C Y N 7   
A1AB1 C17  C Y N 8   
A1AB1 C20  C Y N 9   
A1AB1 C21  C Y N 10  
A1AB1 C22  C Y N 11  
A1AB1 C1   C Y N 12  
A1AB1 C2   C Y N 13  
A1AB1 C3   C Y N 14  
A1AB1 O7   O N N 15  
A1AB1 C9   C Y N 16  
A1AB1 N11  N Y N 17  
A1AB1 C12  C Y N 18  
A1AB1 C14  C Y N 19  
A1AB1 C16  C Y N 20  
A1AB1 N18  N N N 21  
A1AB1 C19  C N N 22  
A1AB1 C23  C Y N 23  
A1AB1 N24  N Y N 24  
A1AB1 C25  C Y N 25  
A1AB1 F26  F N N 26  
A1AB1 F27  F N N 27  
A1AB1 O28  O N N 28  
A1AB1 C29  C N N 29  
A1AB1 C30  C N N 30  
A1AB1 O31  O N N 31  
A1AB1 O32  O N N 32  
A1AB1 C33  C N N 33  
A1AB1 O34  O N N 34  
A1AB1 O35  O N N 35  
A1AB1 C36  C N N 36  
A1AB1 H1   H N N 37  
A1AB1 H2   H N N 38  
A1AB1 H3   H N N 39  
A1AB1 H4   H N N 40  
A1AB1 H5   H N N 41  
A1AB1 H6   H N N 42  
A1AB1 H7   H N N 43  
A1AB1 H8   H N N 44  
A1AB1 H9   H N N 45  
A1AB1 H10  H N N 46  
A1AB1 H11  H N N 47  
A1AB1 H12  H N N 48  
A1AB1 H13  H N N 49  
A1AB1 H14  H N N 50  
A1AB1 H15  H N N 51  
A1AB1 H16  H N N 52  
A1AB1 H17  H N N 53  
A1AB1 H18  H N N 54  
A1AB1 H19  H N N 55  
A1AB1 H20  H N N 56  
A1AB1 H21  H N N 57  
ALA   N    N N N 58  
ALA   CA   C N S 59  
ALA   C    C N N 60  
ALA   O    O N N 61  
ALA   CB   C N N 62  
ALA   OXT  O N N 63  
ALA   H    H N N 64  
ALA   H2   H N N 65  
ALA   HA   H N N 66  
ALA   HB1  H N N 67  
ALA   HB2  H N N 68  
ALA   HB3  H N N 69  
ALA   HXT  H N N 70  
ARG   N    N N N 71  
ARG   CA   C N S 72  
ARG   C    C N N 73  
ARG   O    O N N 74  
ARG   CB   C N N 75  
ARG   CG   C N N 76  
ARG   CD   C N N 77  
ARG   NE   N N N 78  
ARG   CZ   C N N 79  
ARG   NH1  N N N 80  
ARG   NH2  N N N 81  
ARG   OXT  O N N 82  
ARG   H    H N N 83  
ARG   H2   H N N 84  
ARG   HA   H N N 85  
ARG   HB2  H N N 86  
ARG   HB3  H N N 87  
ARG   HG2  H N N 88  
ARG   HG3  H N N 89  
ARG   HD2  H N N 90  
ARG   HD3  H N N 91  
ARG   HE   H N N 92  
ARG   HH11 H N N 93  
ARG   HH12 H N N 94  
ARG   HH21 H N N 95  
ARG   HH22 H N N 96  
ARG   HXT  H N N 97  
ASN   N    N N N 98  
ASN   CA   C N S 99  
ASN   C    C N N 100 
ASN   O    O N N 101 
ASN   CB   C N N 102 
ASN   CG   C N N 103 
ASN   OD1  O N N 104 
ASN   ND2  N N N 105 
ASN   OXT  O N N 106 
ASN   H    H N N 107 
ASN   H2   H N N 108 
ASN   HA   H N N 109 
ASN   HB2  H N N 110 
ASN   HB3  H N N 111 
ASN   HD21 H N N 112 
ASN   HD22 H N N 113 
ASN   HXT  H N N 114 
ASP   N    N N N 115 
ASP   CA   C N S 116 
ASP   C    C N N 117 
ASP   O    O N N 118 
ASP   CB   C N N 119 
ASP   CG   C N N 120 
ASP   OD1  O N N 121 
ASP   OD2  O N N 122 
ASP   OXT  O N N 123 
ASP   H    H N N 124 
ASP   H2   H N N 125 
ASP   HA   H N N 126 
ASP   HB2  H N N 127 
ASP   HB3  H N N 128 
ASP   HD2  H N N 129 
ASP   HXT  H N N 130 
CYS   N    N N N 131 
CYS   CA   C N R 132 
CYS   C    C N N 133 
CYS   O    O N N 134 
CYS   CB   C N N 135 
CYS   SG   S N N 136 
CYS   OXT  O N N 137 
CYS   H    H N N 138 
CYS   H2   H N N 139 
CYS   HA   H N N 140 
CYS   HB2  H N N 141 
CYS   HB3  H N N 142 
CYS   HG   H N N 143 
CYS   HXT  H N N 144 
GLN   N    N N N 145 
GLN   CA   C N S 146 
GLN   C    C N N 147 
GLN   O    O N N 148 
GLN   CB   C N N 149 
GLN   CG   C N N 150 
GLN   CD   C N N 151 
GLN   OE1  O N N 152 
GLN   NE2  N N N 153 
GLN   OXT  O N N 154 
GLN   H    H N N 155 
GLN   H2   H N N 156 
GLN   HA   H N N 157 
GLN   HB2  H N N 158 
GLN   HB3  H N N 159 
GLN   HG2  H N N 160 
GLN   HG3  H N N 161 
GLN   HE21 H N N 162 
GLN   HE22 H N N 163 
GLN   HXT  H N N 164 
GLU   N    N N N 165 
GLU   CA   C N S 166 
GLU   C    C N N 167 
GLU   O    O N N 168 
GLU   CB   C N N 169 
GLU   CG   C N N 170 
GLU   CD   C N N 171 
GLU   OE1  O N N 172 
GLU   OE2  O N N 173 
GLU   OXT  O N N 174 
GLU   H    H N N 175 
GLU   H2   H N N 176 
GLU   HA   H N N 177 
GLU   HB2  H N N 178 
GLU   HB3  H N N 179 
GLU   HG2  H N N 180 
GLU   HG3  H N N 181 
GLU   HE2  H N N 182 
GLU   HXT  H N N 183 
GLY   N    N N N 184 
GLY   CA   C N N 185 
GLY   C    C N N 186 
GLY   O    O N N 187 
GLY   OXT  O N N 188 
GLY   H    H N N 189 
GLY   H2   H N N 190 
GLY   HA2  H N N 191 
GLY   HA3  H N N 192 
GLY   HXT  H N N 193 
HIS   N    N N N 194 
HIS   CA   C N S 195 
HIS   C    C N N 196 
HIS   O    O N N 197 
HIS   CB   C N N 198 
HIS   CG   C Y N 199 
HIS   ND1  N Y N 200 
HIS   CD2  C Y N 201 
HIS   CE1  C Y N 202 
HIS   NE2  N Y N 203 
HIS   OXT  O N N 204 
HIS   H    H N N 205 
HIS   H2   H N N 206 
HIS   HA   H N N 207 
HIS   HB2  H N N 208 
HIS   HB3  H N N 209 
HIS   HD1  H N N 210 
HIS   HD2  H N N 211 
HIS   HE1  H N N 212 
HIS   HE2  H N N 213 
HIS   HXT  H N N 214 
ILE   N    N N N 215 
ILE   CA   C N S 216 
ILE   C    C N N 217 
ILE   O    O N N 218 
ILE   CB   C N S 219 
ILE   CG1  C N N 220 
ILE   CG2  C N N 221 
ILE   CD1  C N N 222 
ILE   OXT  O N N 223 
ILE   H    H N N 224 
ILE   H2   H N N 225 
ILE   HA   H N N 226 
ILE   HB   H N N 227 
ILE   HG12 H N N 228 
ILE   HG13 H N N 229 
ILE   HG21 H N N 230 
ILE   HG22 H N N 231 
ILE   HG23 H N N 232 
ILE   HD11 H N N 233 
ILE   HD12 H N N 234 
ILE   HD13 H N N 235 
ILE   HXT  H N N 236 
LEU   N    N N N 237 
LEU   CA   C N S 238 
LEU   C    C N N 239 
LEU   O    O N N 240 
LEU   CB   C N N 241 
LEU   CG   C N N 242 
LEU   CD1  C N N 243 
LEU   CD2  C N N 244 
LEU   OXT  O N N 245 
LEU   H    H N N 246 
LEU   H2   H N N 247 
LEU   HA   H N N 248 
LEU   HB2  H N N 249 
LEU   HB3  H N N 250 
LEU   HG   H N N 251 
LEU   HD11 H N N 252 
LEU   HD12 H N N 253 
LEU   HD13 H N N 254 
LEU   HD21 H N N 255 
LEU   HD22 H N N 256 
LEU   HD23 H N N 257 
LEU   HXT  H N N 258 
LYS   N    N N N 259 
LYS   CA   C N S 260 
LYS   C    C N N 261 
LYS   O    O N N 262 
LYS   CB   C N N 263 
LYS   CG   C N N 264 
LYS   CD   C N N 265 
LYS   CE   C N N 266 
LYS   NZ   N N N 267 
LYS   OXT  O N N 268 
LYS   H    H N N 269 
LYS   H2   H N N 270 
LYS   HA   H N N 271 
LYS   HB2  H N N 272 
LYS   HB3  H N N 273 
LYS   HG2  H N N 274 
LYS   HG3  H N N 275 
LYS   HD2  H N N 276 
LYS   HD3  H N N 277 
LYS   HE2  H N N 278 
LYS   HE3  H N N 279 
LYS   HZ1  H N N 280 
LYS   HZ2  H N N 281 
LYS   HZ3  H N N 282 
LYS   HXT  H N N 283 
MET   N    N N N 284 
MET   CA   C N S 285 
MET   C    C N N 286 
MET   O    O N N 287 
MET   CB   C N N 288 
MET   CG   C N N 289 
MET   SD   S N N 290 
MET   CE   C N N 291 
MET   OXT  O N N 292 
MET   H    H N N 293 
MET   H2   H N N 294 
MET   HA   H N N 295 
MET   HB2  H N N 296 
MET   HB3  H N N 297 
MET   HG2  H N N 298 
MET   HG3  H N N 299 
MET   HE1  H N N 300 
MET   HE2  H N N 301 
MET   HE3  H N N 302 
MET   HXT  H N N 303 
PHE   N    N N N 304 
PHE   CA   C N S 305 
PHE   C    C N N 306 
PHE   O    O N N 307 
PHE   CB   C N N 308 
PHE   CG   C Y N 309 
PHE   CD1  C Y N 310 
PHE   CD2  C Y N 311 
PHE   CE1  C Y N 312 
PHE   CE2  C Y N 313 
PHE   CZ   C Y N 314 
PHE   OXT  O N N 315 
PHE   H    H N N 316 
PHE   H2   H N N 317 
PHE   HA   H N N 318 
PHE   HB2  H N N 319 
PHE   HB3  H N N 320 
PHE   HD1  H N N 321 
PHE   HD2  H N N 322 
PHE   HE1  H N N 323 
PHE   HE2  H N N 324 
PHE   HZ   H N N 325 
PHE   HXT  H N N 326 
PRO   N    N N N 327 
PRO   CA   C N S 328 
PRO   C    C N N 329 
PRO   O    O N N 330 
PRO   CB   C N N 331 
PRO   CG   C N N 332 
PRO   CD   C N N 333 
PRO   OXT  O N N 334 
PRO   H    H N N 335 
PRO   HA   H N N 336 
PRO   HB2  H N N 337 
PRO   HB3  H N N 338 
PRO   HG2  H N N 339 
PRO   HG3  H N N 340 
PRO   HD2  H N N 341 
PRO   HD3  H N N 342 
PRO   HXT  H N N 343 
SER   N    N N N 344 
SER   CA   C N S 345 
SER   C    C N N 346 
SER   O    O N N 347 
SER   CB   C N N 348 
SER   OG   O N N 349 
SER   OXT  O N N 350 
SER   H    H N N 351 
SER   H2   H N N 352 
SER   HA   H N N 353 
SER   HB2  H N N 354 
SER   HB3  H N N 355 
SER   HG   H N N 356 
SER   HXT  H N N 357 
THR   N    N N N 358 
THR   CA   C N S 359 
THR   C    C N N 360 
THR   O    O N N 361 
THR   CB   C N R 362 
THR   OG1  O N N 363 
THR   CG2  C N N 364 
THR   OXT  O N N 365 
THR   H    H N N 366 
THR   H2   H N N 367 
THR   HA   H N N 368 
THR   HB   H N N 369 
THR   HG1  H N N 370 
THR   HG21 H N N 371 
THR   HG22 H N N 372 
THR   HG23 H N N 373 
THR   HXT  H N N 374 
TRP   N    N N N 375 
TRP   CA   C N S 376 
TRP   C    C N N 377 
TRP   O    O N N 378 
TRP   CB   C N N 379 
TRP   CG   C Y N 380 
TRP   CD1  C Y N 381 
TRP   CD2  C Y N 382 
TRP   NE1  N Y N 383 
TRP   CE2  C Y N 384 
TRP   CE3  C Y N 385 
TRP   CZ2  C Y N 386 
TRP   CZ3  C Y N 387 
TRP   CH2  C Y N 388 
TRP   OXT  O N N 389 
TRP   H    H N N 390 
TRP   H2   H N N 391 
TRP   HA   H N N 392 
TRP   HB2  H N N 393 
TRP   HB3  H N N 394 
TRP   HD1  H N N 395 
TRP   HE1  H N N 396 
TRP   HE3  H N N 397 
TRP   HZ2  H N N 398 
TRP   HZ3  H N N 399 
TRP   HH2  H N N 400 
TRP   HXT  H N N 401 
TYR   N    N N N 402 
TYR   CA   C N S 403 
TYR   C    C N N 404 
TYR   O    O N N 405 
TYR   CB   C N N 406 
TYR   CG   C Y N 407 
TYR   CD1  C Y N 408 
TYR   CD2  C Y N 409 
TYR   CE1  C Y N 410 
TYR   CE2  C Y N 411 
TYR   CZ   C Y N 412 
TYR   OH   O N N 413 
TYR   OXT  O N N 414 
TYR   H    H N N 415 
TYR   H2   H N N 416 
TYR   HA   H N N 417 
TYR   HB2  H N N 418 
TYR   HB3  H N N 419 
TYR   HD1  H N N 420 
TYR   HD2  H N N 421 
TYR   HE1  H N N 422 
TYR   HE2  H N N 423 
TYR   HH   H N N 424 
TYR   HXT  H N N 425 
VAL   N    N N N 426 
VAL   CA   C N S 427 
VAL   C    C N N 428 
VAL   O    O N N 429 
VAL   CB   C N N 430 
VAL   CG1  C N N 431 
VAL   CG2  C N N 432 
VAL   OXT  O N N 433 
VAL   H    H N N 434 
VAL   H2   H N N 435 
VAL   HA   H N N 436 
VAL   HB   H N N 437 
VAL   HG11 H N N 438 
VAL   HG12 H N N 439 
VAL   HG13 H N N 440 
VAL   HG21 H N N 441 
VAL   HG22 H N N 442 
VAL   HG23 H N N 443 
VAL   HXT  H N N 444 
# 
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 
A1AB1 C30 O31  sing N N 1   
A1AB1 C30 C29  sing N N 2   
A1AB1 C29 O28  sing N N 3   
A1AB1 O28 C15  sing N N 4   
A1AB1 C33 O32  sing N N 5   
A1AB1 F27 C3   sing N N 6   
A1AB1 C15 C14  doub Y N 7   
A1AB1 C15 C16  sing Y N 8   
A1AB1 O34 C19  doub N N 9   
A1AB1 C14 C9   sing Y N 10  
A1AB1 O32 C16  sing N N 11  
A1AB1 C3  C4   doub Y N 12  
A1AB1 C3  C2   sing Y N 13  
A1AB1 C16 C17  doub Y N 14  
A1AB1 C25 N24  doub Y N 15  
A1AB1 C25 C20  sing Y N 16  
A1AB1 O7  C2   sing N N 17  
A1AB1 O7  C8   sing N N 18  
A1AB1 C4  C5   sing Y N 19  
A1AB1 N24 C23  sing Y N 20  
A1AB1 C2  C1   doub Y N 21  
A1AB1 C19 C20  sing N N 22  
A1AB1 C19 N18  sing N N 23  
A1AB1 C9  C8   doub Y N 24  
A1AB1 C9  C10  sing Y N 25  
A1AB1 C8  C13  sing Y N 26  
A1AB1 C20 C21  doub Y N 27  
A1AB1 C17 C10  sing Y N 28  
A1AB1 C5  N18  sing N N 29  
A1AB1 C5  C6   doub Y N 30  
A1AB1 C1  C6   sing Y N 31  
A1AB1 C1  F26  sing N N 32  
A1AB1 C10 N11  doub Y N 33  
A1AB1 C23 C22  doub Y N 34  
A1AB1 C13 C12  doub Y N 35  
A1AB1 C21 C22  sing Y N 36  
A1AB1 C21 O35  sing N N 37  
A1AB1 N11 C12  sing Y N 38  
A1AB1 O35 C36  sing N N 39  
A1AB1 C4  H1   sing N N 40  
A1AB1 C6  H2   sing N N 41  
A1AB1 C13 H3   sing N N 42  
A1AB1 C17 H4   sing N N 43  
A1AB1 C22 H5   sing N N 44  
A1AB1 C12 H6   sing N N 45  
A1AB1 C14 H7   sing N N 46  
A1AB1 N18 H8   sing N N 47  
A1AB1 C23 H9   sing N N 48  
A1AB1 C25 H10  sing N N 49  
A1AB1 C29 H11  sing N N 50  
A1AB1 C29 H12  sing N N 51  
A1AB1 C30 H13  sing N N 52  
A1AB1 C30 H14  sing N N 53  
A1AB1 O31 H15  sing N N 54  
A1AB1 C33 H16  sing N N 55  
A1AB1 C33 H17  sing N N 56  
A1AB1 C33 H18  sing N N 57  
A1AB1 C36 H19  sing N N 58  
A1AB1 C36 H20  sing N N 59  
A1AB1 C36 H21  sing N N 60  
ALA   N   CA   sing N N 61  
ALA   N   H    sing N N 62  
ALA   N   H2   sing N N 63  
ALA   CA  C    sing N N 64  
ALA   CA  CB   sing N N 65  
ALA   CA  HA   sing N N 66  
ALA   C   O    doub N N 67  
ALA   C   OXT  sing N N 68  
ALA   CB  HB1  sing N N 69  
ALA   CB  HB2  sing N N 70  
ALA   CB  HB3  sing N N 71  
ALA   OXT HXT  sing N N 72  
ARG   N   CA   sing N N 73  
ARG   N   H    sing N N 74  
ARG   N   H2   sing N N 75  
ARG   CA  C    sing N N 76  
ARG   CA  CB   sing N N 77  
ARG   CA  HA   sing N N 78  
ARG   C   O    doub N N 79  
ARG   C   OXT  sing N N 80  
ARG   CB  CG   sing N N 81  
ARG   CB  HB2  sing N N 82  
ARG   CB  HB3  sing N N 83  
ARG   CG  CD   sing N N 84  
ARG   CG  HG2  sing N N 85  
ARG   CG  HG3  sing N N 86  
ARG   CD  NE   sing N N 87  
ARG   CD  HD2  sing N N 88  
ARG   CD  HD3  sing N N 89  
ARG   NE  CZ   sing N N 90  
ARG   NE  HE   sing N N 91  
ARG   CZ  NH1  sing N N 92  
ARG   CZ  NH2  doub N N 93  
ARG   NH1 HH11 sing N N 94  
ARG   NH1 HH12 sing N N 95  
ARG   NH2 HH21 sing N N 96  
ARG   NH2 HH22 sing N N 97  
ARG   OXT HXT  sing N N 98  
ASN   N   CA   sing N N 99  
ASN   N   H    sing N N 100 
ASN   N   H2   sing N N 101 
ASN   CA  C    sing N N 102 
ASN   CA  CB   sing N N 103 
ASN   CA  HA   sing N N 104 
ASN   C   O    doub N N 105 
ASN   C   OXT  sing N N 106 
ASN   CB  CG   sing N N 107 
ASN   CB  HB2  sing N N 108 
ASN   CB  HB3  sing N N 109 
ASN   CG  OD1  doub N N 110 
ASN   CG  ND2  sing N N 111 
ASN   ND2 HD21 sing N N 112 
ASN   ND2 HD22 sing N N 113 
ASN   OXT HXT  sing N N 114 
ASP   N   CA   sing N N 115 
ASP   N   H    sing N N 116 
ASP   N   H2   sing N N 117 
ASP   CA  C    sing N N 118 
ASP   CA  CB   sing N N 119 
ASP   CA  HA   sing N N 120 
ASP   C   O    doub N N 121 
ASP   C   OXT  sing N N 122 
ASP   CB  CG   sing N N 123 
ASP   CB  HB2  sing N N 124 
ASP   CB  HB3  sing N N 125 
ASP   CG  OD1  doub N N 126 
ASP   CG  OD2  sing N N 127 
ASP   OD2 HD2  sing N N 128 
ASP   OXT HXT  sing N N 129 
CYS   N   CA   sing N N 130 
CYS   N   H    sing N N 131 
CYS   N   H2   sing N N 132 
CYS   CA  C    sing N N 133 
CYS   CA  CB   sing N N 134 
CYS   CA  HA   sing N N 135 
CYS   C   O    doub N N 136 
CYS   C   OXT  sing N N 137 
CYS   CB  SG   sing N N 138 
CYS   CB  HB2  sing N N 139 
CYS   CB  HB3  sing N N 140 
CYS   SG  HG   sing N N 141 
CYS   OXT HXT  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
HIS   N   CA   sing N N 189 
HIS   N   H    sing N N 190 
HIS   N   H2   sing N N 191 
HIS   CA  C    sing N N 192 
HIS   CA  CB   sing N N 193 
HIS   CA  HA   sing N N 194 
HIS   C   O    doub N N 195 
HIS   C   OXT  sing N N 196 
HIS   CB  CG   sing N N 197 
HIS   CB  HB2  sing N N 198 
HIS   CB  HB3  sing N N 199 
HIS   CG  ND1  sing Y N 200 
HIS   CG  CD2  doub Y N 201 
HIS   ND1 CE1  doub Y N 202 
HIS   ND1 HD1  sing N N 203 
HIS   CD2 NE2  sing Y N 204 
HIS   CD2 HD2  sing N N 205 
HIS   CE1 NE2  sing Y N 206 
HIS   CE1 HE1  sing N N 207 
HIS   NE2 HE2  sing N N 208 
HIS   OXT HXT  sing N N 209 
ILE   N   CA   sing N N 210 
ILE   N   H    sing N N 211 
ILE   N   H2   sing N N 212 
ILE   CA  C    sing N N 213 
ILE   CA  CB   sing N N 214 
ILE   CA  HA   sing N N 215 
ILE   C   O    doub N N 216 
ILE   C   OXT  sing N N 217 
ILE   CB  CG1  sing N N 218 
ILE   CB  CG2  sing N N 219 
ILE   CB  HB   sing N N 220 
ILE   CG1 CD1  sing N N 221 
ILE   CG1 HG12 sing N N 222 
ILE   CG1 HG13 sing N N 223 
ILE   CG2 HG21 sing N N 224 
ILE   CG2 HG22 sing N N 225 
ILE   CG2 HG23 sing N N 226 
ILE   CD1 HD11 sing N N 227 
ILE   CD1 HD12 sing N N 228 
ILE   CD1 HD13 sing N N 229 
ILE   OXT HXT  sing N N 230 
LEU   N   CA   sing N N 231 
LEU   N   H    sing N N 232 
LEU   N   H2   sing N N 233 
LEU   CA  C    sing N N 234 
LEU   CA  CB   sing N N 235 
LEU   CA  HA   sing N N 236 
LEU   C   O    doub N N 237 
LEU   C   OXT  sing N N 238 
LEU   CB  CG   sing N N 239 
LEU   CB  HB2  sing N N 240 
LEU   CB  HB3  sing N N 241 
LEU   CG  CD1  sing N N 242 
LEU   CG  CD2  sing N N 243 
LEU   CG  HG   sing N N 244 
LEU   CD1 HD11 sing N N 245 
LEU   CD1 HD12 sing N N 246 
LEU   CD1 HD13 sing N N 247 
LEU   CD2 HD21 sing N N 248 
LEU   CD2 HD22 sing N N 249 
LEU   CD2 HD23 sing N N 250 
LEU   OXT HXT  sing N N 251 
LYS   N   CA   sing N N 252 
LYS   N   H    sing N N 253 
LYS   N   H2   sing N N 254 
LYS   CA  C    sing N N 255 
LYS   CA  CB   sing N N 256 
LYS   CA  HA   sing N N 257 
LYS   C   O    doub N N 258 
LYS   C   OXT  sing N N 259 
LYS   CB  CG   sing N N 260 
LYS   CB  HB2  sing N N 261 
LYS   CB  HB3  sing N N 262 
LYS   CG  CD   sing N N 263 
LYS   CG  HG2  sing N N 264 
LYS   CG  HG3  sing N N 265 
LYS   CD  CE   sing N N 266 
LYS   CD  HD2  sing N N 267 
LYS   CD  HD3  sing N N 268 
LYS   CE  NZ   sing N N 269 
LYS   CE  HE2  sing N N 270 
LYS   CE  HE3  sing N N 271 
LYS   NZ  HZ1  sing N N 272 
LYS   NZ  HZ2  sing N N 273 
LYS   NZ  HZ3  sing N N 274 
LYS   OXT HXT  sing N N 275 
MET   N   CA   sing N N 276 
MET   N   H    sing N N 277 
MET   N   H2   sing N N 278 
MET   CA  C    sing N N 279 
MET   CA  CB   sing N N 280 
MET   CA  HA   sing N N 281 
MET   C   O    doub N N 282 
MET   C   OXT  sing N N 283 
MET   CB  CG   sing N N 284 
MET   CB  HB2  sing N N 285 
MET   CB  HB3  sing N N 286 
MET   CG  SD   sing N N 287 
MET   CG  HG2  sing N N 288 
MET   CG  HG3  sing N N 289 
MET   SD  CE   sing N N 290 
MET   CE  HE1  sing N N 291 
MET   CE  HE2  sing N N 292 
MET   CE  HE3  sing N N 293 
MET   OXT HXT  sing N N 294 
PHE   N   CA   sing N N 295 
PHE   N   H    sing N N 296 
PHE   N   H2   sing N N 297 
PHE   CA  C    sing N N 298 
PHE   CA  CB   sing N N 299 
PHE   CA  HA   sing N N 300 
PHE   C   O    doub N N 301 
PHE   C   OXT  sing N N 302 
PHE   CB  CG   sing N N 303 
PHE   CB  HB2  sing N N 304 
PHE   CB  HB3  sing N N 305 
PHE   CG  CD1  doub Y N 306 
PHE   CG  CD2  sing Y N 307 
PHE   CD1 CE1  sing Y N 308 
PHE   CD1 HD1  sing N N 309 
PHE   CD2 CE2  doub Y N 310 
PHE   CD2 HD2  sing N N 311 
PHE   CE1 CZ   doub Y N 312 
PHE   CE1 HE1  sing N N 313 
PHE   CE2 CZ   sing Y N 314 
PHE   CE2 HE2  sing N N 315 
PHE   CZ  HZ   sing N N 316 
PHE   OXT HXT  sing N N 317 
PRO   N   CA   sing N N 318 
PRO   N   CD   sing N N 319 
PRO   N   H    sing N N 320 
PRO   CA  C    sing N N 321 
PRO   CA  CB   sing N N 322 
PRO   CA  HA   sing N N 323 
PRO   C   O    doub N N 324 
PRO   C   OXT  sing N N 325 
PRO   CB  CG   sing N N 326 
PRO   CB  HB2  sing N N 327 
PRO   CB  HB3  sing N N 328 
PRO   CG  CD   sing N N 329 
PRO   CG  HG2  sing N N 330 
PRO   CG  HG3  sing N N 331 
PRO   CD  HD2  sing N N 332 
PRO   CD  HD3  sing N N 333 
PRO   OXT HXT  sing N N 334 
SER   N   CA   sing N N 335 
SER   N   H    sing N N 336 
SER   N   H2   sing N N 337 
SER   CA  C    sing N N 338 
SER   CA  CB   sing N N 339 
SER   CA  HA   sing N N 340 
SER   C   O    doub N N 341 
SER   C   OXT  sing N N 342 
SER   CB  OG   sing N N 343 
SER   CB  HB2  sing N N 344 
SER   CB  HB3  sing N N 345 
SER   OG  HG   sing N N 346 
SER   OXT HXT  sing N N 347 
THR   N   CA   sing N N 348 
THR   N   H    sing N N 349 
THR   N   H2   sing N N 350 
THR   CA  C    sing N N 351 
THR   CA  CB   sing N N 352 
THR   CA  HA   sing N N 353 
THR   C   O    doub N N 354 
THR   C   OXT  sing N N 355 
THR   CB  OG1  sing N N 356 
THR   CB  CG2  sing N N 357 
THR   CB  HB   sing N N 358 
THR   OG1 HG1  sing N N 359 
THR   CG2 HG21 sing N N 360 
THR   CG2 HG22 sing N N 361 
THR   CG2 HG23 sing N N 362 
THR   OXT HXT  sing N N 363 
TRP   N   CA   sing N N 364 
TRP   N   H    sing N N 365 
TRP   N   H2   sing N N 366 
TRP   CA  C    sing N N 367 
TRP   CA  CB   sing N N 368 
TRP   CA  HA   sing N N 369 
TRP   C   O    doub N N 370 
TRP   C   OXT  sing N N 371 
TRP   CB  CG   sing N N 372 
TRP   CB  HB2  sing N N 373 
TRP   CB  HB3  sing N N 374 
TRP   CG  CD1  doub Y N 375 
TRP   CG  CD2  sing Y N 376 
TRP   CD1 NE1  sing Y N 377 
TRP   CD1 HD1  sing N N 378 
TRP   CD2 CE2  doub Y N 379 
TRP   CD2 CE3  sing Y N 380 
TRP   NE1 CE2  sing Y N 381 
TRP   NE1 HE1  sing N N 382 
TRP   CE2 CZ2  sing Y N 383 
TRP   CE3 CZ3  doub Y N 384 
TRP   CE3 HE3  sing N N 385 
TRP   CZ2 CH2  doub Y N 386 
TRP   CZ2 HZ2  sing N N 387 
TRP   CZ3 CH2  sing Y N 388 
TRP   CZ3 HZ3  sing N N 389 
TRP   CH2 HH2  sing N N 390 
TRP   OXT HXT  sing N N 391 
TYR   N   CA   sing N N 392 
TYR   N   H    sing N N 393 
TYR   N   H2   sing N N 394 
TYR   CA  C    sing N N 395 
TYR   CA  CB   sing N N 396 
TYR   CA  HA   sing N N 397 
TYR   C   O    doub N N 398 
TYR   C   OXT  sing N N 399 
TYR   CB  CG   sing N N 400 
TYR   CB  HB2  sing N N 401 
TYR   CB  HB3  sing N N 402 
TYR   CG  CD1  doub Y N 403 
TYR   CG  CD2  sing Y N 404 
TYR   CD1 CE1  sing Y N 405 
TYR   CD1 HD1  sing N N 406 
TYR   CD2 CE2  doub Y N 407 
TYR   CD2 HD2  sing N N 408 
TYR   CE1 CZ   doub Y N 409 
TYR   CE1 HE1  sing N N 410 
TYR   CE2 CZ   sing Y N 411 
TYR   CE2 HE2  sing N N 412 
TYR   CZ  OH   sing N N 413 
TYR   OH  HH   sing N N 414 
TYR   OXT HXT  sing N N 415 
VAL   N   CA   sing N N 416 
VAL   N   H    sing N N 417 
VAL   N   H2   sing N N 418 
VAL   CA  C    sing N N 419 
VAL   CA  CB   sing N N 420 
VAL   CA  HA   sing N N 421 
VAL   C   O    doub N N 422 
VAL   C   OXT  sing N N 423 
VAL   CB  CG1  sing N N 424 
VAL   CB  CG2  sing N N 425 
VAL   CB  HB   sing N N 426 
VAL   CG1 HG11 sing N N 427 
VAL   CG1 HG12 sing N N 428 
VAL   CG1 HG13 sing N N 429 
VAL   CG2 HG21 sing N N 430 
VAL   CG2 HG22 sing N N 431 
VAL   CG2 HG23 sing N N 432 
VAL   OXT HXT  sing N N 433 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   6SDC 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    8VI1 
_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]   0.013576 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001389 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014323 
_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]   0.012878 
_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 
C 
F 
N 
O 
S 
# 
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   . ILE   A 1 16  ? 10.671  14.869  13.813  1.00 150.40 ? 1053 ILE   A N   1 
ATOM   2    C CA  . ILE   A 1 16  ? 9.548   15.341  14.681  1.00 148.43 ? 1053 ILE   A CA  1 
ATOM   3    C C   . ILE   A 1 16  ? 10.141  16.048  15.899  1.00 146.66 ? 1053 ILE   A C   1 
ATOM   4    O O   . ILE   A 1 16  ? 11.142  15.598  16.453  1.00 146.32 ? 1053 ILE   A O   1 
ATOM   5    C CB  . ILE   A 1 16  ? 8.619   14.175  15.086  1.00 147.84 ? 1053 ILE   A CB  1 
ATOM   6    C CG1 . ILE   A 1 16  ? 7.998   13.477  13.870  1.00 150.68 ? 1053 ILE   A CG1 1 
ATOM   7    C CG2 . ILE   A 1 16  ? 7.550   14.651  16.062  1.00 145.45 ? 1053 ILE   A CG2 1 
ATOM   8    C CD1 . ILE   A 1 16  ? 8.897   12.462  13.194  1.00 152.63 ? 1053 ILE   A CD1 1 
ATOM   9    N N   . ASP   A 1 17  ? 9.506   17.156  16.303  1.00 145.84 ? 1054 ASP   A N   1 
ATOM   10   C CA  . ASP   A 1 17  ? 9.956   17.951  17.435  1.00 143.66 ? 1054 ASP   A CA  1 
ATOM   11   C C   . ASP   A 1 17  ? 9.526   17.254  18.725  1.00 141.86 ? 1054 ASP   A C   1 
ATOM   12   O O   . ASP   A 1 17  ? 8.338   17.013  18.933  1.00 141.30 ? 1054 ASP   A O   1 
ATOM   13   C CB  . ASP   A 1 17  ? 9.408   19.379  17.346  1.00 142.94 ? 1054 ASP   A CB  1 
ATOM   14   C CG  . ASP   A 1 17  ? 9.981   20.347  18.368  1.00 141.35 ? 1054 ASP   A CG  1 
ATOM   15   O OD1 . ASP   A 1 17  ? 9.489   21.492  18.422  1.00 140.67 ? 1054 ASP   A OD1 1 
ATOM   16   O OD2 . ASP   A 1 17  ? 10.921  19.959  19.092  1.00 140.60 ? 1054 ASP   A OD2 1 
ATOM   17   N N   . LEU   A 1 18  ? 10.507  16.946  19.586  1.00 140.93 ? 1055 LEU   A N   1 
ATOM   18   C CA  . LEU   A 1 18  ? 10.269  16.154  20.786  1.00 139.16 ? 1055 LEU   A CA  1 
ATOM   19   C C   . LEU   A 1 18  ? 9.755   17.027  21.933  1.00 137.38 ? 1055 LEU   A C   1 
ATOM   20   O O   . LEU   A 1 18  ? 9.308   16.495  22.951  1.00 136.62 ? 1055 LEU   A O   1 
ATOM   21   C CB  . LEU   A 1 18  ? 11.542  15.376  21.163  1.00 139.19 ? 1055 LEU   A CB  1 
ATOM   22   C CG  . LEU   A 1 18  ? 12.671  16.108  21.901  1.00 138.77 ? 1055 LEU   A CG  1 
ATOM   23   C CD1 . LEU   A 1 18  ? 13.062  17.417  21.226  1.00 139.61 ? 1055 LEU   A CD1 1 
ATOM   24   C CD2 . LEU   A 1 18  ? 12.329  16.343  23.369  1.00 136.94 ? 1055 LEU   A CD2 1 
ATOM   25   N N   . SER   A 1 19  ? 9.811   18.358  21.768  1.00 136.38 ? 1056 SER   A N   1 
ATOM   26   C CA  . SER   A 1 19  ? 9.284   19.286  22.758  1.00 134.19 ? 1056 SER   A CA  1 
ATOM   27   C C   . SER   A 1 19  ? 8.461   20.368  22.061  1.00 133.50 ? 1056 SER   A C   1 
ATOM   28   O O   . SER   A 1 19  ? 8.784   21.552  22.142  1.00 133.94 ? 1056 SER   A O   1 
ATOM   29   C CB  . SER   A 1 19  ? 10.394  19.879  23.593  1.00 134.03 ? 1056 SER   A CB  1 
ATOM   30   O OG  . SER   A 1 19  ? 11.347  20.544  22.777  1.00 135.26 ? 1056 SER   A OG  1 
ATOM   31   N N   . ALA   A 1 20  ? 7.391   19.935  21.384  1.00 132.21 ? 1057 ALA   A N   1 
ATOM   32   C CA  . ALA   A 1 20  ? 6.534   20.823  20.614  1.00 131.61 ? 1057 ALA   A CA  1 
ATOM   33   C C   . ALA   A 1 20  ? 5.323   21.238  21.448  1.00 130.05 ? 1057 ALA   A C   1 
ATOM   34   O O   . ALA   A 1 20  ? 5.070   22.427  21.627  1.00 130.64 ? 1057 ALA   A O   1 
ATOM   35   C CB  . ALA   A 1 20  ? 6.114   20.143  19.333  1.00 132.78 ? 1057 ALA   A CB  1 
ATOM   36   N N   . LEU   A 1 21  ? 4.589   20.240  21.958  1.00 128.13 ? 1058 LEU   A N   1 
ATOM   37   C CA  . LEU   A 1 21  ? 3.317   20.463  22.628  1.00 126.84 ? 1058 LEU   A CA  1 
ATOM   38   C C   . LEU   A 1 21  ? 3.551   20.729  24.116  1.00 125.10 ? 1058 LEU   A C   1 
ATOM   39   O O   . LEU   A 1 21  ? 4.684   20.968  24.533  1.00 124.05 ? 1058 LEU   A O   1 
ATOM   40   C CB  . LEU   A 1 21  ? 2.427   19.233  22.399  1.00 126.84 ? 1058 LEU   A CB  1 
ATOM   41   C CG  . LEU   A 1 21  ? 2.255   18.800  20.943  1.00 127.75 ? 1058 LEU   A CG  1 
ATOM   42   C CD1 . LEU   A 1 21  ? 1.156   17.755  20.818  1.00 129.07 ? 1058 LEU   A CD1 1 
ATOM   43   C CD2 . LEU   A 1 21  ? 1.959   19.994  20.043  1.00 128.43 ? 1058 LEU   A CD2 1 
ATOM   44   N N   . ASN   A 1 22  ? 2.459   20.704  24.895  1.00 124.49 ? 1059 ASN   A N   1 
ATOM   45   C CA  . ASN   A 1 22  ? 2.459   20.998  26.322  1.00 123.37 ? 1059 ASN   A CA  1 
ATOM   46   C C   . ASN   A 1 22  ? 3.775   20.562  26.966  1.00 122.25 ? 1059 ASN   A C   1 
ATOM   47   O O   . ASN   A 1 22  ? 4.091   19.373  26.982  1.00 121.83 ? 1059 ASN   A O   1 
ATOM   48   C CB  . ASN   A 1 22  ? 1.263   20.334  27.010  1.00 123.41 ? 1059 ASN   A CB  1 
ATOM   49   C CG  . ASN   A 1 22  ? 1.143   20.681  28.478  1.00 123.26 ? 1059 ASN   A CG  1 
ATOM   50   O OD1 . ASN   A 1 22  ? 1.113   19.796  29.329  1.00 122.52 ? 1059 ASN   A OD1 1 
ATOM   51   N ND2 . ASN   A 1 22  ? 1.062   21.966  28.784  1.00 123.48 ? 1059 ASN   A ND2 1 
ATOM   52   N N   . PRO   A 1 23  ? 4.572   21.502  27.534  1.00 121.75 ? 1060 PRO   A N   1 
ATOM   53   C CA  . PRO   A 1 23  ? 5.878   21.175  28.111  1.00 120.76 ? 1060 PRO   A CA  1 
ATOM   54   C C   . PRO   A 1 23  ? 5.863   20.696  29.563  1.00 120.79 ? 1060 PRO   A C   1 
ATOM   55   O O   . PRO   A 1 23  ? 6.913   20.624  30.199  1.00 120.11 ? 1060 PRO   A O   1 
ATOM   56   C CB  . PRO   A 1 23  ? 6.599   22.528  28.013  1.00 121.10 ? 1060 PRO   A CB  1 
ATOM   57   C CG  . PRO   A 1 23  ? 5.503   23.535  28.284  1.00 122.01 ? 1060 PRO   A CG  1 
ATOM   58   C CD  . PRO   A 1 23  ? 4.267   22.940  27.638  1.00 122.22 ? 1060 PRO   A CD  1 
ATOM   59   N N   . GLU   A 1 24  ? 4.670   20.380  30.085  1.00 121.54 ? 1061 GLU   A N   1 
ATOM   60   C CA  . GLU   A 1 24  ? 4.537   19.804  31.414  1.00 122.01 ? 1061 GLU   A CA  1 
ATOM   61   C C   . GLU   A 1 24  ? 4.757   18.293  31.340  1.00 120.93 ? 1061 GLU   A C   1 
ATOM   62   O O   . GLU   A 1 24  ? 5.179   17.683  32.320  1.00 120.92 ? 1061 GLU   A O   1 
ATOM   63   C CB  . GLU   A 1 24  ? 3.161   20.131  32.002  1.00 123.55 ? 1061 GLU   A CB  1 
ATOM   64   C CG  . GLU   A 1 24  ? 3.015   19.767  33.471  1.00 124.48 ? 1061 GLU   A CG  1 
ATOM   65   C CD  . GLU   A 1 24  ? 3.970   20.490  34.407  1.00 124.64 ? 1061 GLU   A CD  1 
ATOM   66   O OE1 . GLU   A 1 24  ? 4.820   19.814  35.020  1.00 124.04 ? 1061 GLU   A OE1 1 
ATOM   67   O OE2 . GLU   A 1 24  ? 3.858   21.727  34.524  1.00 125.02 ? 1061 GLU   A OE2 1 
ATOM   68   N N   . LEU   A 1 25  ? 4.464   17.703  30.173  1.00 119.71 ? 1062 LEU   A N   1 
ATOM   69   C CA  . LEU   A 1 25  ? 4.644   16.276  29.956  1.00 118.78 ? 1062 LEU   A CA  1 
ATOM   70   C C   . LEU   A 1 25  ? 6.115   15.908  30.139  1.00 118.84 ? 1062 LEU   A C   1 
ATOM   71   O O   . LEU   A 1 25  ? 6.437   15.072  30.978  1.00 118.83 ? 1062 LEU   A O   1 
ATOM   72   C CB  . LEU   A 1 25  ? 4.155   15.897  28.553  1.00 117.78 ? 1062 LEU   A CB  1 
ATOM   73   C CG  . LEU   A 1 25  ? 2.655   15.633  28.411  1.00 118.47 ? 1062 LEU   A CG  1 
ATOM   74   C CD1 . LEU   A 1 25  ? 2.201   14.518  29.343  1.00 118.85 ? 1062 LEU   A CD1 1 
ATOM   75   C CD2 . LEU   A 1 25  ? 1.850   16.899  28.660  1.00 118.98 ? 1062 LEU   A CD2 1 
ATOM   76   N N   . VAL   A 1 26  ? 6.992   16.560  29.363  1.00 119.79 ? 1063 VAL   A N   1 
ATOM   77   C CA  . VAL   A 1 26  ? 8.417   16.256  29.352  1.00 120.76 ? 1063 VAL   A CA  1 
ATOM   78   C C   . VAL   A 1 26  ? 8.973   16.277  30.777  1.00 121.45 ? 1063 VAL   A C   1 
ATOM   79   O O   . VAL   A 1 26  ? 9.843   15.474  31.109  1.00 121.06 ? 1063 VAL   A O   1 
ATOM   80   C CB  . VAL   A 1 26  ? 9.198   17.210  28.422  1.00 121.56 ? 1063 VAL   A CB  1 
ATOM   81   C CG1 . VAL   A 1 26  ? 9.057   18.671  28.827  1.00 122.18 ? 1063 VAL   A CG1 1 
ATOM   82   C CG2 . VAL   A 1 26  ? 10.667  16.824  28.325  1.00 121.85 ? 1063 VAL   A CG2 1 
ATOM   83   N N   . GLN   A 1 27  ? 8.469   17.200  31.607  1.00 122.40 ? 1064 GLN   A N   1 
ATOM   84   C CA  . GLN   A 1 27  ? 8.872   17.299  33.001  1.00 123.15 ? 1064 GLN   A CA  1 
ATOM   85   C C   . GLN   A 1 27  ? 8.355   16.087  33.775  1.00 123.12 ? 1064 GLN   A C   1 
ATOM   86   O O   . GLN   A 1 27  ? 9.098   15.477  34.542  1.00 123.42 ? 1064 GLN   A O   1 
ATOM   87   C CB  . GLN   A 1 27  ? 8.343   18.602  33.609  1.00 123.94 ? 1064 GLN   A CB  1 
ATOM   88   C CG  . GLN   A 1 27  ? 8.869   18.900  35.008  1.00 125.10 ? 1064 GLN   A CG  1 
ATOM   89   C CD  . GLN   A 1 27  ? 10.309  19.354  35.011  1.00 125.40 ? 1064 GLN   A CD  1 
ATOM   90   O OE1 . GLN   A 1 27  ? 11.222  18.598  34.685  1.00 124.42 ? 1064 GLN   A OE1 1 
ATOM   91   N NE2 . GLN   A 1 27  ? 10.525  20.601  35.396  1.00 126.67 ? 1064 GLN   A NE2 1 
ATOM   92   N N   . ALA   A 1 28  ? 7.076   15.753  33.562  1.00 122.67 ? 1065 ALA   A N   1 
ATOM   93   C CA  . ALA   A 1 28  ? 6.419   14.667  34.274  1.00 122.23 ? 1065 ALA   A CA  1 
ATOM   94   C C   . ALA   A 1 28  ? 6.895   13.307  33.763  1.00 120.39 ? 1065 ALA   A C   1 
ATOM   95   O O   . ALA   A 1 28  ? 6.903   12.338  34.520  1.00 120.46 ? 1065 ALA   A O   1 
ATOM   96   C CB  . ALA   A 1 28  ? 4.922   14.805  34.139  1.00 123.05 ? 1065 ALA   A CB  1 
ATOM   97   N N   . VAL   A 1 29  ? 7.288   13.242  32.482  1.00 118.28 ? 1066 VAL   A N   1 
ATOM   98   C CA  . VAL   A 1 29  ? 7.687   11.991  31.854  1.00 116.53 ? 1066 VAL   A CA  1 
ATOM   99   C C   . VAL   A 1 29  ? 9.205   11.980  31.664  1.00 115.54 ? 1066 VAL   A C   1 
ATOM   100  O O   . VAL   A 1 29  ? 9.702   11.684  30.580  1.00 114.70 ? 1066 VAL   A O   1 
ATOM   101  C CB  . VAL   A 1 29  ? 6.928   11.763  30.528  1.00 115.98 ? 1066 VAL   A CB  1 
ATOM   102  C CG1 . VAL   A 1 29  ? 5.422   11.837  30.736  1.00 116.46 ? 1066 VAL   A CG1 1 
ATOM   103  C CG2 . VAL   A 1 29  ? 7.363   12.712  29.419  1.00 115.69 ? 1066 VAL   A CG2 1 
ATOM   104  N N   . GLN   A 1 30  ? 9.935   12.284  32.745  1.00 115.43 ? 1067 GLN   A N   1 
ATOM   105  C CA  . GLN   A 1 30  ? 11.389  12.285  32.734  1.00 115.15 ? 1067 GLN   A CA  1 
ATOM   106  C C   . GLN   A 1 30  ? 11.895  10.846  32.828  1.00 113.85 ? 1067 GLN   A C   1 
ATOM   107  O O   . GLN   A 1 30  ? 12.784  10.446  32.079  1.00 113.93 ? 1067 GLN   A O   1 
ATOM   108  C CB  . GLN   A 1 30  ? 11.921  13.130  33.895  1.00 116.49 ? 1067 GLN   A CB  1 
ATOM   109  C CG  . GLN   A 1 30  ? 13.438  13.261  33.925  1.00 117.65 ? 1067 GLN   A CG  1 
ATOM   110  C CD  . GLN   A 1 30  ? 13.919  14.080  35.097  1.00 119.32 ? 1067 GLN   A CD  1 
ATOM   111  O OE1 . GLN   A 1 30  ? 14.540  15.129  34.934  1.00 120.47 ? 1067 GLN   A OE1 1 
ATOM   112  N NE2 . GLN   A 1 30  ? 13.635  13.604  36.299  1.00 119.55 ? 1067 GLN   A NE2 1 
ATOM   113  N N   . HIS   A 1 31  ? 11.313  10.089  33.767  1.00 112.14 ? 1068 HIS   A N   1 
ATOM   114  C CA  . HIS   A 1 31  ? 11.716  8.722   34.063  1.00 110.70 ? 1068 HIS   A CA  1 
ATOM   115  C C   . HIS   A 1 31  ? 11.637  7.830   32.823  1.00 109.50 ? 1068 HIS   A C   1 
ATOM   116  O O   . HIS   A 1 31  ? 12.514  6.994   32.614  1.00 109.51 ? 1068 HIS   A O   1 
ATOM   117  C CB  . HIS   A 1 31  ? 10.870  8.158   35.215  1.00 110.43 ? 1068 HIS   A CB  1 
ATOM   118  C CG  . HIS   A 1 31  ? 9.391   8.101   34.967  1.00 110.04 ? 1068 HIS   A CG  1 
ATOM   119  N ND1 . HIS   A 1 31  ? 8.633   9.181   34.585  1.00 109.69 ? 1068 HIS   A ND1 1 
ATOM   120  C CD2 . HIS   A 1 31  ? 8.541   7.040   35.071  1.00 110.22 ? 1068 HIS   A CD2 1 
ATOM   121  C CE1 . HIS   A 1 31  ? 7.364   8.802   34.452  1.00 110.14 ? 1068 HIS   A CE1 1 
ATOM   122  N NE2 . HIS   A 1 31  ? 7.284   7.475   34.750  1.00 110.45 ? 1068 HIS   A NE2 1 
ATOM   123  N N   . VAL   A 1 32  ? 10.588  8.010   32.010  1.00 108.47 ? 1069 VAL   A N   1 
ATOM   124  C CA  . VAL   A 1 32  ? 10.339  7.141   30.868  1.00 107.79 ? 1069 VAL   A CA  1 
ATOM   125  C C   . VAL   A 1 32  ? 11.284  7.501   29.721  1.00 107.18 ? 1069 VAL   A C   1 
ATOM   126  O O   . VAL   A 1 32  ? 11.773  6.611   29.028  1.00 107.34 ? 1069 VAL   A O   1 
ATOM   127  C CB  . VAL   A 1 32  ? 8.862   7.187   30.422  1.00 108.15 ? 1069 VAL   A CB  1 
ATOM   128  C CG1 . VAL   A 1 32  ? 8.472   8.531   29.825  1.00 108.02 ? 1069 VAL   A CG1 1 
ATOM   129  C CG2 . VAL   A 1 32  ? 8.535   6.065   29.447  1.00 109.02 ? 1069 VAL   A CG2 1 
ATOM   130  N N   . VAL   A 1 33  ? 11.535  8.802   29.524  1.00 106.27 ? 1070 VAL   A N   1 
ATOM   131  C CA  . VAL   A 1 33  ? 12.346  9.274   28.412  1.00 106.22 ? 1070 VAL   A CA  1 
ATOM   132  C C   . VAL   A 1 33  ? 13.808  8.911   28.670  1.00 106.16 ? 1070 VAL   A C   1 
ATOM   133  O O   . VAL   A 1 33  ? 14.274  8.973   29.806  1.00 106.07 ? 1070 VAL   A O   1 
ATOM   134  C CB  . VAL   A 1 33  ? 12.165  10.790  28.190  1.00 106.16 ? 1070 VAL   A CB  1 
ATOM   135  C CG1 . VAL   A 1 33  ? 13.171  11.351  27.194  1.00 107.07 ? 1070 VAL   A CG1 1 
ATOM   136  C CG2 . VAL   A 1 33  ? 10.746  11.130  27.758  1.00 105.97 ? 1070 VAL   A CG2 1 
ATOM   137  N N   . ILE   A 1 34  ? 14.515  8.533   27.596  1.00 106.43 ? 1071 ILE   A N   1 
ATOM   138  C CA  . ILE   A 1 34  ? 15.919  8.160   27.665  1.00 107.37 ? 1071 ILE   A CA  1 
ATOM   139  C C   . ILE   A 1 34  ? 16.689  8.953   26.610  1.00 108.53 ? 1071 ILE   A C   1 
ATOM   140  O O   . ILE   A 1 34  ? 16.172  9.215   25.525  1.00 108.33 ? 1071 ILE   A O   1 
ATOM   141  C CB  . ILE   A 1 34  ? 16.097  6.636   27.493  1.00 107.73 ? 1071 ILE   A CB  1 
ATOM   142  C CG1 . ILE   A 1 34  ? 17.519  6.180   27.838  1.00 109.21 ? 1071 ILE   A CG1 1 
ATOM   143  C CG2 . ILE   A 1 34  ? 15.691  6.180   26.098  1.00 108.28 ? 1071 ILE   A CG2 1 
ATOM   144  C CD1 . ILE   A 1 34  ? 17.913  6.417   29.279  1.00 108.86 ? 1071 ILE   A CD1 1 
ATOM   145  N N   . GLY   A 1 35  ? 17.930  9.325   26.946  1.00 109.73 ? 1072 GLY   A N   1 
ATOM   146  C CA  . GLY   A 1 35  ? 18.763  10.138  26.074  1.00 111.34 ? 1072 GLY   A CA  1 
ATOM   147  C C   . GLY   A 1 35  ? 19.344  9.323   24.919  1.00 113.03 ? 1072 GLY   A C   1 
ATOM   148  O O   . GLY   A 1 35  ? 19.681  8.154   25.098  1.00 113.17 ? 1072 GLY   A O   1 
ATOM   149  N N   . PRO   A 1 36  ? 19.473  9.906   23.702  1.00 99.69  ? 1073 PRO   A N   1 
ATOM   150  C CA  . PRO   A 1 36  ? 20.105  9.217   22.573  1.00 98.88  ? 1073 PRO   A CA  1 
ATOM   151  C C   . PRO   A 1 36  ? 21.554  8.796   22.818  1.00 99.28  ? 1073 PRO   A C   1 
ATOM   152  O O   . PRO   A 1 36  ? 22.004  7.789   22.275  1.00 98.79  ? 1073 PRO   A O   1 
ATOM   153  C CB  . PRO   A 1 36  ? 20.065  10.248  21.433  1.00 100.37 ? 1073 PRO   A CB  1 
ATOM   154  C CG  . PRO   A 1 36  ? 18.947  11.194  21.817  1.00 101.11 ? 1073 PRO   A CG  1 
ATOM   155  C CD  . PRO   A 1 36  ? 18.979  11.242  23.330  1.00 101.27 ? 1073 PRO   A CD  1 
ATOM   156  N N   . SER   A 1 37  ? 22.276  9.581   23.629  1.00 100.62 ? 1074 SER   A N   1 
ATOM   157  C CA  . SER   A 1 37  ? 23.672  9.315   23.936  1.00 101.79 ? 1074 SER   A CA  1 
ATOM   158  C C   . SER   A 1 37  ? 23.820  7.999   24.700  1.00 100.80 ? 1074 SER   A C   1 
ATOM   159  O O   . SER   A 1 37  ? 24.807  7.289   24.518  1.00 101.60 ? 1074 SER   A O   1 
ATOM   160  C CB  . SER   A 1 37  ? 24.282  10.461  24.705  1.00 104.07 ? 1074 SER   A CB  1 
ATOM   161  O OG  . SER   A 1 37  ? 23.597  10.673  25.931  1.00 103.78 ? 1074 SER   A OG  1 
ATOM   162  N N   . SER   A 1 38  ? 22.831  7.684   25.548  1.00 99.39  ? 1075 SER   A N   1 
ATOM   163  C CA  . SER   A 1 38  ? 22.861  6.489   26.378  1.00 98.98  ? 1075 SER   A CA  1 
ATOM   164  C C   . SER   A 1 38  ? 21.997  5.387   25.764  1.00 96.48  ? 1075 SER   A C   1 
ATOM   165  O O   . SER   A 1 38  ? 21.173  4.786   26.453  1.00 96.16  ? 1075 SER   A O   1 
ATOM   166  C CB  . SER   A 1 38  ? 22.427  6.818   27.786  1.00 100.24 ? 1075 SER   A CB  1 
ATOM   167  O OG  . SER   A 1 38  ? 21.124  7.383   27.798  1.00 99.50  ? 1075 SER   A OG  1 
ATOM   168  N N   . LEU   A 1 39  ? 22.208  5.117   24.469  1.00 94.97  ? 1076 LEU   A N   1 
ATOM   169  C CA  . LEU   A 1 39  ? 21.484  4.075   23.756  1.00 92.73  ? 1076 LEU   A CA  1 
ATOM   170  C C   . LEU   A 1 39  ? 22.159  3.817   22.410  1.00 92.47  ? 1076 LEU   A C   1 
ATOM   171  O O   . LEU   A 1 39  ? 22.136  4.676   21.531  1.00 92.41  ? 1076 LEU   A O   1 
ATOM   172  C CB  . LEU   A 1 39  ? 20.025  4.507   23.561  1.00 91.70  ? 1076 LEU   A CB  1 
ATOM   173  C CG  . LEU   A 1 39  ? 19.164  3.574   22.708  1.00 90.21  ? 1076 LEU   A CG  1 
ATOM   174  C CD1 . LEU   A 1 39  ? 18.973  2.229   23.392  1.00 89.98  ? 1076 LEU   A CD1 1 
ATOM   175  C CD2 . LEU   A 1 39  ? 17.817  4.210   22.402  1.00 89.81  ? 1076 LEU   A CD2 1 
ATOM   176  N N   . ILE   A 1 40  ? 22.751  2.625   22.266  1.00 92.83  ? 1077 ILE   A N   1 
ATOM   177  C CA  . ILE   A 1 40  ? 23.335  2.188   21.007  1.00 93.42  ? 1077 ILE   A CA  1 
ATOM   178  C C   . ILE   A 1 40  ? 22.391  1.167   20.376  1.00 91.27  ? 1077 ILE   A C   1 
ATOM   179  O O   . ILE   A 1 40  ? 22.011  0.193   21.023  1.00 90.46  ? 1077 ILE   A O   1 
ATOM   180  C CB  . ILE   A 1 40  ? 24.752  1.612   21.214  1.00 96.11  ? 1077 ILE   A CB  1 
ATOM   181  C CG1 . ILE   A 1 40  ? 25.729  2.663   21.754  1.00 98.61  ? 1077 ILE   A CG1 1 
ATOM   182  C CG2 . ILE   A 1 40  ? 25.272  0.979   19.929  1.00 97.01  ? 1077 ILE   A CG2 1 
ATOM   183  C CD1 . ILE   A 1 40  ? 25.500  3.053   23.198  1.00 98.61  ? 1077 ILE   A CD1 1 
ATOM   184  N N   . VAL   A 1 41  ? 22.023  1.407   19.111  1.00 90.54  ? 1078 VAL   A N   1 
ATOM   185  C CA  . VAL   A 1 41  ? 21.103  0.546   18.385  1.00 89.17  ? 1078 VAL   A CA  1 
ATOM   186  C C   . VAL   A 1 41  ? 21.889  -0.219  17.322  1.00 90.78  ? 1078 VAL   A C   1 
ATOM   187  O O   . VAL   A 1 41  ? 22.437  0.382   16.400  1.00 92.20  ? 1078 VAL   A O   1 
ATOM   188  C CB  . VAL   A 1 41  ? 19.952  1.358   17.759  1.00 88.10  ? 1078 VAL   A CB  1 
ATOM   189  C CG1 . VAL   A 1 41  ? 19.060  0.496   16.876  1.00 87.31  ? 1078 VAL   A CG1 1 
ATOM   190  C CG2 . VAL   A 1 41  ? 19.126  2.074   18.818  1.00 87.06  ? 1078 VAL   A CG2 1 
ATOM   191  N N   . HIS   A 1 42  ? 21.932  -1.549  17.467  1.00 91.17  ? 1079 HIS   A N   1 
ATOM   192  C CA  . HIS   A 1 42  ? 22.591  -2.416  16.505  1.00 93.34  ? 1079 HIS   A CA  1 
ATOM   193  C C   . HIS   A 1 42  ? 21.655  -2.656  15.324  1.00 93.22  ? 1079 HIS   A C   1 
ATOM   194  O O   . HIS   A 1 42  ? 20.895  -3.622  15.320  1.00 92.40  ? 1079 HIS   A O   1 
ATOM   195  C CB  . HIS   A 1 42  ? 23.004  -3.736  17.168  1.00 94.09  ? 1079 HIS   A CB  1 
ATOM   196  C CG  . HIS   A 1 42  ? 23.843  -3.582  18.400  1.00 95.56  ? 1079 HIS   A CG  1 
ATOM   197  N ND1 . HIS   A 1 42  ? 24.984  -2.821  18.453  1.00 98.10  ? 1079 HIS   A ND1 1 
ATOM   198  C CD2 . HIS   A 1 42  ? 23.658  -4.110  19.643  1.00 95.62  ? 1079 HIS   A CD2 1 
ATOM   199  C CE1 . HIS   A 1 42  ? 25.492  -2.883  19.682  1.00 99.25  ? 1079 HIS   A CE1 1 
ATOM   200  N NE2 . HIS   A 1 42  ? 24.685  -3.679  20.438  1.00 97.79  ? 1079 HIS   A NE2 1 
ATOM   201  N N   . PHE   A 1 43  ? 21.719  -1.765  14.328  1.00 95.18  ? 1080 PHE   A N   1 
ATOM   202  C CA  . PHE   A 1 43  ? 20.835  -1.827  13.173  1.00 95.91  ? 1080 PHE   A CA  1 
ATOM   203  C C   . PHE   A 1 43  ? 21.179  -3.033  12.297  1.00 96.29  ? 1080 PHE   A C   1 
ATOM   204  O O   . PHE   A 1 43  ? 20.319  -3.531  11.573  1.00 95.77  ? 1080 PHE   A O   1 
ATOM   205  C CB  . PHE   A 1 43  ? 20.878  -0.513  12.386  1.00 99.34  ? 1080 PHE   A CB  1 
ATOM   206  C CG  . PHE   A 1 43  ? 22.243  -0.084  11.905  1.00 104.90 ? 1080 PHE   A CG  1 
ATOM   207  C CD1 . PHE   A 1 43  ? 22.870  -0.733  10.850  1.00 108.78 ? 1080 PHE   A CD1 1 
ATOM   208  C CD2 . PHE   A 1 43  ? 22.904  0.975   12.511  1.00 106.92 ? 1080 PHE   A CD2 1 
ATOM   209  C CE1 . PHE   A 1 43  ? 24.124  -0.332  10.413  1.00 112.91 ? 1080 PHE   A CE1 1 
ATOM   210  C CE2 . PHE   A 1 43  ? 24.158  1.374   12.073  1.00 111.04 ? 1080 PHE   A CE2 1 
ATOM   211  C CZ  . PHE   A 1 43  ? 24.765  0.720   11.026  1.00 113.96 ? 1080 PHE   A CZ  1 
ATOM   212  N N   . ASN   A 1 44  ? 22.439  -3.487  12.360  1.00 97.31  ? 1081 ASN   A N   1 
ATOM   213  C CA  . ASN   A 1 44  ? 22.889  -4.641  11.596  1.00 98.40  ? 1081 ASN   A CA  1 
ATOM   214  C C   . ASN   A 1 44  ? 22.212  -5.910  12.116  1.00 95.49  ? 1081 ASN   A C   1 
ATOM   215  O O   . ASN   A 1 44  ? 21.782  -6.746  11.324  1.00 95.65  ? 1081 ASN   A O   1 
ATOM   216  C CB  . ASN   A 1 44  ? 24.417  -4.772  11.597  1.00 101.93 ? 1081 ASN   A CB  1 
ATOM   217  C CG  . ASN   A 1 44  ? 25.039  -4.759  12.979  1.00 101.53 ? 1081 ASN   A CG  1 
ATOM   218  O OD1 . ASN   A 1 44  ? 24.358  -4.531  13.976  1.00 98.79  ? 1081 ASN   A OD1 1 
ATOM   219  N ND2 . ASN   A 1 44  ? 26.341  -4.987  13.047  1.00 104.76 ? 1081 ASN   A ND2 1 
ATOM   220  N N   . GLU   A 1 45  ? 22.122  -6.041  13.446  1.00 92.91  ? 1082 GLU   A N   1 
ATOM   221  C CA  . GLU   A 1 45  ? 21.478  -7.184  14.074  1.00 91.17  ? 1082 GLU   A CA  1 
ATOM   222  C C   . GLU   A 1 45  ? 19.974  -6.929  14.158  1.00 88.24  ? 1082 GLU   A C   1 
ATOM   223  O O   . GLU   A 1 45  ? 19.531  -6.082  14.932  1.00 87.12  ? 1082 GLU   A O   1 
ATOM   224  C CB  . GLU   A 1 45  ? 22.064  -7.430  15.466  1.00 91.31  ? 1082 GLU   A CB  1 
ATOM   225  C CG  . GLU   A 1 45  ? 23.548  -7.746  15.459  1.00 94.16  ? 1082 GLU   A CG  1 
ATOM   226  C CD  . GLU   A 1 45  ? 24.144  -7.964  16.839  1.00 94.95  ? 1082 GLU   A CD  1 
ATOM   227  O OE1 . GLU   A 1 45  ? 23.681  -8.884  17.542  1.00 94.51  ? 1082 GLU   A OE1 1 
ATOM   228  O OE2 . GLU   A 1 45  ? 25.068  -7.212  17.210  1.00 96.32  ? 1082 GLU   A OE2 1 
ATOM   229  N N   . VAL   A 1 46  ? 19.199  -7.683  13.368  1.00 87.09  ? 1083 VAL   A N   1 
ATOM   230  C CA  . VAL   A 1 46  ? 17.763  -7.476  13.254  1.00 84.69  ? 1083 VAL   A CA  1 
ATOM   231  C C   . VAL   A 1 46  ? 17.045  -8.723  13.770  1.00 84.36  ? 1083 VAL   A C   1 
ATOM   232  O O   . VAL   A 1 46  ? 17.454  -9.845  13.477  1.00 85.55  ? 1083 VAL   A O   1 
ATOM   233  C CB  . VAL   A 1 46  ? 17.360  -7.121  11.807  1.00 85.02  ? 1083 VAL   A CB  1 
ATOM   234  C CG1 . VAL   A 1 46  ? 17.988  -8.055  10.784  1.00 87.06  ? 1083 VAL   A CG1 1 
ATOM   235  C CG2 . VAL   A 1 46  ? 15.849  -7.065  11.628  1.00 84.02  ? 1083 VAL   A CG2 1 
ATOM   236  N N   . ILE   A 1 47  ? 15.968  -8.501  14.536  1.00 83.35  ? 1084 ILE   A N   1 
ATOM   237  C CA  . ILE   A 1 47  ? 15.291  -9.557  15.274  1.00 83.94  ? 1084 ILE   A CA  1 
ATOM   238  C C   . ILE   A 1 47  ? 14.064  -10.022 14.492  1.00 84.42  ? 1084 ILE   A C   1 
ATOM   239  O O   . ILE   A 1 47  ? 13.324  -9.208  13.942  1.00 83.94  ? 1084 ILE   A O   1 
ATOM   240  C CB  . ILE   A 1 47  ? 14.910  -9.071  16.688  1.00 83.28  ? 1084 ILE   A CB  1 
ATOM   241  C CG1 . ILE   A 1 47  ? 16.145  -8.670  17.500  1.00 83.34  ? 1084 ILE   A CG1 1 
ATOM   242  C CG2 . ILE   A 1 47  ? 14.070  -10.115 17.411  1.00 84.47  ? 1084 ILE   A CG2 1 
ATOM   243  C CD1 . ILE   A 1 47  ? 15.836  -8.078  18.858  1.00 83.30  ? 1084 ILE   A CD1 1 
ATOM   244  N N   . GLY   A 1 48  ? 13.860  -11.346 14.465  1.00 85.73  ? 1085 GLY   A N   1 
ATOM   245  C CA  . GLY   A 1 48  ? 12.695  -11.950 13.839  1.00 86.80  ? 1085 GLY   A CA  1 
ATOM   246  C C   . GLY   A 1 48  ? 12.739  -11.877 12.313  1.00 87.46  ? 1085 GLY   A C   1 
ATOM   247  O O   . GLY   A 1 48  ? 11.722  -12.095 11.660  1.00 88.69  ? 1085 GLY   A O   1 
ATOM   248  N N   . ARG   A 1 49  ? 13.922  -11.573 11.761  1.00 87.34  ? 1086 ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 49  ? 14.117  -11.400 10.329  1.00 88.11  ? 1086 ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 49  ? 13.083  -10.433 9.748   1.00 87.60  ? 1086 ARG   A C   1 
ATOM   251  O O   . ARG   A 1 49  ? 12.628  -10.614 8.621   1.00 88.65  ? 1086 ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 49  ? 14.070  -12.758 9.621   1.00 90.22  ? 1086 ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 49  ? 15.167  -13.720 10.057  1.00 91.53  ? 1086 ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 49  ? 15.186  -14.998 9.241   1.00 94.28  ? 1086 ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 49  ? 15.236  -14.735 7.806   1.00 95.95  ? 1086 ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 49  ? 16.328  -14.822 7.051   1.00 98.14  ? 1086 ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 49  ? 16.275  -14.476 5.776   1.00 99.67  ? 1086 ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 49  ? 17.472  -15.238 7.570   1.00 99.26  ? 1086 ARG   A NH2 1 
ATOM   259  N N   . GLY   A 1 50  ? 12.730  -9.400  10.524  1.00 86.23  ? 1087 GLY   A N   1 
ATOM   260  C CA  . GLY   A 1 50  ? 11.839  -8.346  10.067  1.00 86.20  ? 1087 GLY   A CA  1 
ATOM   261  C C   . GLY   A 1 50  ? 10.397  -8.809  9.858   1.00 86.73  ? 1087 GLY   A C   1 
ATOM   262  O O   . GLY   A 1 50  ? 9.659   -8.189  9.095   1.00 87.93  ? 1087 GLY   A O   1 
ATOM   263  N N   . HIS   A 1 51  ? 9.999   -9.890  10.543  1.00 86.21  ? 1088 HIS   A N   1 
ATOM   264  C CA  . HIS   A 1 51  ? 8.633   -10.387 10.469  1.00 87.23  ? 1088 HIS   A CA  1 
ATOM   265  C C   . HIS   A 1 51  ? 7.749   -9.642  11.466  1.00 86.79  ? 1088 HIS   A C   1 
ATOM   266  O O   . HIS   A 1 51  ? 6.558   -9.460  11.217  1.00 88.27  ? 1088 HIS   A O   1 
ATOM   267  C CB  . HIS   A 1 51  ? 8.590   -11.903 10.706  1.00 88.12  ? 1088 HIS   A CB  1 
ATOM   268  C CG  . HIS   A 1 51  ? 9.114   -12.726 9.568   1.00 89.17  ? 1088 HIS   A CG  1 
ATOM   269  N ND1 . HIS   A 1 51  ? 8.669   -12.603 8.275   1.00 90.58  ? 1088 HIS   A ND1 1 
ATOM   270  C CD2 . HIS   A 1 51  ? 10.074  -13.694 9.566   1.00 89.41  ? 1088 HIS   A CD2 1 
ATOM   271  C CE1 . HIS   A 1 51  ? 9.325   -13.464 7.502   1.00 91.63  ? 1088 HIS   A CE1 1 
ATOM   272  N NE2 . HIS   A 1 51  ? 10.204  -14.152 8.283   1.00 90.96  ? 1088 HIS   A NE2 1 
ATOM   273  N N   . PHE   A 1 52  ? 8.345   -9.216  12.588  1.00 85.02  ? 1089 PHE   A N   1 
ATOM   274  C CA  . PHE   A 1 52  ? 7.638   -8.470  13.617  1.00 85.07  ? 1089 PHE   A CA  1 
ATOM   275  C C   . PHE   A 1 52  ? 8.011   -6.990  13.530  1.00 82.68  ? 1089 PHE   A C   1 
ATOM   276  O O   . PHE   A 1 52  ? 8.271   -6.353  14.549  1.00 82.33  ? 1089 PHE   A O   1 
ATOM   277  C CB  . PHE   A 1 52  ? 7.951   -9.061  14.995  1.00 85.97  ? 1089 PHE   A CB  1 
ATOM   278  C CG  . PHE   A 1 52  ? 7.426   -10.458 15.209  1.00 88.89  ? 1089 PHE   A CG  1 
ATOM   279  C CD1 . PHE   A 1 52  ? 6.071   -10.685 15.407  1.00 91.84  ? 1089 PHE   A CD1 1 
ATOM   280  C CD2 . PHE   A 1 52  ? 8.281   -11.550 15.197  1.00 89.22  ? 1089 PHE   A CD2 1 
ATOM   281  C CE1 . PHE   A 1 52  ? 5.586   -11.970 15.601  1.00 94.14  ? 1089 PHE   A CE1 1 
ATOM   282  C CE2 . PHE   A 1 52  ? 7.794   -12.835 15.387  1.00 91.61  ? 1089 PHE   A CE2 1 
ATOM   283  C CZ  . PHE   A 1 52  ? 6.448   -13.043 15.590  1.00 94.00  ? 1089 PHE   A CZ  1 
ATOM   284  N N   . GLY   A 1 53  ? 8.017   -6.448  12.305  1.00 81.04  ? 1090 GLY   A N   1 
ATOM   285  C CA  . GLY   A 1 53  ? 8.361   -5.055  12.073  1.00 79.03  ? 1090 GLY   A CA  1 
ATOM   286  C C   . GLY   A 1 53  ? 9.861   -4.804  12.206  1.00 75.83  ? 1090 GLY   A C   1 
ATOM   287  O O   . GLY   A 1 53  ? 10.653  -5.745  12.242  1.00 74.97  ? 1090 GLY   A O   1 
ATOM   288  N N   . CYS   A 1 54  ? 10.231  -3.520  12.280  1.00 73.78  ? 1091 CYS   A N   1 
ATOM   289  C CA  . CYS   A 1 54  ? 11.623  -3.107  12.372  1.00 71.40  ? 1091 CYS   A CA  1 
ATOM   290  C C   . CYS   A 1 54  ? 12.101  -3.202  13.819  1.00 68.51  ? 1091 CYS   A C   1 
ATOM   291  O O   . CYS   A 1 54  ? 12.144  -2.197  14.526  1.00 68.20  ? 1091 CYS   A O   1 
ATOM   292  C CB  . CYS   A 1 54  ? 11.804  -1.685  11.854  1.00 72.46  ? 1091 CYS   A CB  1 
ATOM   293  S SG  . CYS   A 1 54  ? 11.408  -1.499  10.096  1.00 75.28  ? 1091 CYS   A SG  1 
ATOM   294  N N   . VAL   A 1 55  ? 12.463  -4.421  14.242  1.00 103.81 ? 1092 VAL   A N   1 
ATOM   295  C CA  . VAL   A 1 55  ? 12.935  -4.673  15.595  1.00 101.10 ? 1092 VAL   A CA  1 
ATOM   296  C C   . VAL   A 1 55  ? 14.404  -5.083  15.526  1.00 100.63 ? 1092 VAL   A C   1 
ATOM   297  O O   . VAL   A 1 55  ? 14.742  -6.055  14.852  1.00 100.54 ? 1092 VAL   A O   1 
ATOM   298  C CB  . VAL   A 1 55  ? 12.086  -5.752  16.298  1.00 98.79  ? 1092 VAL   A CB  1 
ATOM   299  C CG1 . VAL   A 1 55  ? 12.570  -6.017  17.716  1.00 97.54  ? 1092 VAL   A CG1 1 
ATOM   300  C CG2 . VAL   A 1 55  ? 10.607  -5.399  16.305  1.00 98.61  ? 1092 VAL   A CG2 1 
ATOM   301  N N   . TYR   A 1 56  ? 15.263  -4.340  16.237  1.00 100.28 ? 1093 TYR   A N   1 
ATOM   302  C CA  . TYR   A 1 56  ? 16.697  -4.587  16.242  1.00 100.45 ? 1093 TYR   A CA  1 
ATOM   303  C C   . TYR   A 1 56  ? 17.177  -4.831  17.670  1.00 99.14  ? 1093 TYR   A C   1 
ATOM   304  O O   . TYR   A 1 56  ? 16.441  -4.597  18.627  1.00 97.82  ? 1093 TYR   A O   1 
ATOM   305  C CB  . TYR   A 1 56  ? 17.459  -3.404  15.639  1.00 102.81 ? 1093 TYR   A CB  1 
ATOM   306  C CG  . TYR   A 1 56  ? 16.882  -2.842  14.364  1.00 103.92 ? 1093 TYR   A CG  1 
ATOM   307  C CD1 . TYR   A 1 56  ? 17.404  -3.188  13.128  1.00 105.28 ? 1093 TYR   A CD1 1 
ATOM   308  C CD2 . TYR   A 1 56  ? 15.837  -1.932  14.392  1.00 104.10 ? 1093 TYR   A CD2 1 
ATOM   309  C CE1 . TYR   A 1 56  ? 16.886  -2.669  11.952  1.00 106.86 ? 1093 TYR   A CE1 1 
ATOM   310  C CE2 . TYR   A 1 56  ? 15.308  -1.401  13.227  1.00 105.79 ? 1093 TYR   A CE2 1 
ATOM   311  C CZ  . TYR   A 1 56  ? 15.834  -1.770  12.001  1.00 107.18 ? 1093 TYR   A CZ  1 
ATOM   312  O OH  . TYR   A 1 56  ? 15.316  -1.247  10.842  1.00 109.27 ? 1093 TYR   A OH  1 
ATOM   313  N N   . HIS   A 1 57  ? 18.425  -5.299  17.794  1.00 99.63  ? 1094 HIS   A N   1 
ATOM   314  C CA  . HIS   A 1 57  ? 19.097  -5.397  19.080  1.00 99.69  ? 1094 HIS   A CA  1 
ATOM   315  C C   . HIS   A 1 57  ? 19.492  -3.998  19.548  1.00 101.48 ? 1094 HIS   A C   1 
ATOM   316  O O   . HIS   A 1 57  ? 19.382  -3.035  18.791  1.00 102.79 ? 1094 HIS   A O   1 
ATOM   317  C CB  . HIS   A 1 57  ? 20.324  -6.314  18.982  1.00 100.76 ? 1094 HIS   A CB  1 
ATOM   318  C CG  . HIS   A 1 57  ? 20.019  -7.762  18.738  1.00 99.17  ? 1094 HIS   A CG  1 
ATOM   319  N ND1 . HIS   A 1 57  ? 20.316  -8.762  19.630  1.00 98.82  ? 1094 HIS   A ND1 1 
ATOM   320  C CD2 . HIS   A 1 57  ? 19.431  -8.356  17.660  1.00 98.22  ? 1094 HIS   A CD2 1 
ATOM   321  C CE1 . HIS   A 1 57  ? 19.926  -9.930  19.125  1.00 97.65  ? 1094 HIS   A CE1 1 
ATOM   322  N NE2 . HIS   A 1 57  ? 19.374  -9.701  17.901  1.00 97.24  ? 1094 HIS   A NE2 1 
ATOM   323  N N   . GLY   A 1 58  ? 19.954  -3.896  20.800  1.00 102.03 ? 1095 GLY   A N   1 
ATOM   324  C CA  . GLY   A 1 58  ? 20.372  -2.619  21.356  1.00 104.11 ? 1095 GLY   A CA  1 
ATOM   325  C C   . GLY   A 1 58  ? 21.217  -2.777  22.618  1.00 105.52 ? 1095 GLY   A C   1 
ATOM   326  O O   . GLY   A 1 58  ? 21.333  -3.873  23.164  1.00 104.74 ? 1095 GLY   A O   1 
ATOM   327  N N   . THR   A 1 59  ? 21.806  -1.658  23.059  1.00 107.94 ? 1096 THR   A N   1 
ATOM   328  C CA  . THR   A 1 59  ? 22.588  -1.605  24.284  1.00 109.94 ? 1096 THR   A CA  1 
ATOM   329  C C   . THR   A 1 59  ? 22.235  -0.325  25.038  1.00 111.12 ? 1096 THR   A C   1 
ATOM   330  O O   . THR   A 1 59  ? 22.537  0.772   24.573  1.00 113.04 ? 1096 THR   A O   1 
ATOM   331  C CB  . THR   A 1 59  ? 24.090  -1.687  23.985  1.00 113.16 ? 1096 THR   A CB  1 
ATOM   332  O OG1 . THR   A 1 59  ? 24.338  -2.900  23.274  1.00 112.04 ? 1096 THR   A OG1 1 
ATOM   333  C CG2 . THR   A 1 59  ? 24.945  -1.650  25.233  1.00 116.03 ? 1096 THR   A CG2 1 
ATOM   334  N N   . LEU   A 1 60  ? 21.592  -0.485  26.202  1.00 110.23 ? 1097 LEU   A N   1 
ATOM   335  C CA  . LEU   A 1 60  ? 21.125  0.637   27.000  1.00 111.50 ? 1097 LEU   A CA  1 
ATOM   336  C C   . LEU   A 1 60  ? 22.144  0.943   28.096  1.00 115.17 ? 1097 LEU   A C   1 
ATOM   337  O O   . LEU   A 1 60  ? 22.404  0.102   28.954  1.00 115.33 ? 1097 LEU   A O   1 
ATOM   338  C CB  . LEU   A 1 60  ? 19.759  0.282   27.597  1.00 108.65 ? 1097 LEU   A CB  1 
ATOM   339  C CG  . LEU   A 1 60  ? 19.087  1.379   28.424  1.00 109.68 ? 1097 LEU   A CG  1 
ATOM   340  C CD1 . LEU   A 1 60  ? 18.602  2.518   27.536  1.00 110.10 ? 1097 LEU   A CD1 1 
ATOM   341  C CD2 . LEU   A 1 60  ? 17.936  0.811   29.241  1.00 107.36 ? 1097 LEU   A CD2 1 
ATOM   342  N N   . LEU   A 1 61  ? 22.705  2.158   28.055  1.00 118.55 ? 1098 LEU   A N   1 
ATOM   343  C CA  . LEU   A 1 61  ? 23.650  2.614   29.064  1.00 122.75 ? 1098 LEU   A CA  1 
ATOM   344  C C   . LEU   A 1 61  ? 22.886  3.047   30.313  1.00 122.78 ? 1098 LEU   A C   1 
ATOM   345  O O   . LEU   A 1 61  ? 22.218  4.079   30.309  1.00 122.92 ? 1098 LEU   A O   1 
ATOM   346  C CB  . LEU   A 1 61  ? 24.484  3.771   28.499  1.00 126.58 ? 1098 LEU   A CB  1 
ATOM   347  C CG  . LEU   A 1 61  ? 25.720  3.379   27.688  1.00 128.54 ? 1098 LEU   A CG  1 
ATOM   348  C CD1 . LEU   A 1 61  ? 26.782  2.742   28.574  1.00 131.41 ? 1098 LEU   A CD1 1 
ATOM   349  C CD2 . LEU   A 1 61  ? 25.353  2.456   26.535  1.00 125.05 ? 1098 LEU   A CD2 1 
ATOM   350  N N   . ASP   A 1 62  ? 22.996  2.239   31.375  1.00 122.84 ? 1099 ASP   A N   1 
ATOM   351  C CA  . ASP   A 1 62  ? 22.416  2.566   32.667  1.00 123.49 ? 1099 ASP   A CA  1 
ATOM   352  C C   . ASP   A 1 62  ? 23.286  3.629   33.335  1.00 128.49 ? 1099 ASP   A C   1 
ATOM   353  O O   . ASP   A 1 62  ? 24.483  3.710   33.063  1.00 131.53 ? 1099 ASP   A O   1 
ATOM   354  C CB  . ASP   A 1 62  ? 22.285  1.310   33.536  1.00 122.42 ? 1099 ASP   A CB  1 
ATOM   355  C CG  . ASP   A 1 62  ? 21.416  1.480   34.772  1.00 122.40 ? 1099 ASP   A CG  1 
ATOM   356  O OD1 . ASP   A 1 62  ? 20.802  2.555   34.920  1.00 122.75 ? 1099 ASP   A OD1 1 
ATOM   357  O OD2 . ASP   A 1 62  ? 21.362  0.532   35.579  1.00 122.23 ? 1099 ASP   A OD2 1 
ATOM   358  N N   . ASN   A 1 63  ? 22.673  4.433   34.213  1.00 129.54 ? 1100 ASN   A N   1 
ATOM   359  C CA  . ASN   A 1 63  ? 23.368  5.519   34.890  1.00 134.37 ? 1100 ASN   A CA  1 
ATOM   360  C C   . ASN   A 1 63  ? 24.313  4.963   35.957  1.00 137.66 ? 1100 ASN   A C   1 
ATOM   361  O O   . ASN   A 1 63  ? 25.193  5.679   36.430  1.00 142.53 ? 1100 ASN   A O   1 
ATOM   362  C CB  . ASN   A 1 63  ? 22.396  6.544   35.487  1.00 134.84 ? 1100 ASN   A CB  1 
ATOM   363  C CG  . ASN   A 1 63  ? 21.439  5.965   36.508  1.00 133.05 ? 1100 ASN   A CG  1 
ATOM   364  O OD1 . ASN   A 1 63  ? 21.385  4.754   36.709  1.00 130.88 ? 1100 ASN   A OD1 1 
ATOM   365  N ND2 . ASN   A 1 63  ? 20.668  6.826   37.152  1.00 134.08 ? 1100 ASN   A ND2 1 
ATOM   366  N N   . ASP   A 1 64  ? 24.116  3.693   36.338  1.00 135.17 ? 1101 ASP   A N   1 
ATOM   367  C CA  . ASP   A 1 64  ? 25.012  3.006   37.255  1.00 138.19 ? 1101 ASP   A CA  1 
ATOM   368  C C   . ASP   A 1 64  ? 26.395  2.891   36.618  1.00 140.76 ? 1101 ASP   A C   1 
ATOM   369  O O   . ASP   A 1 64  ? 27.377  3.374   37.179  1.00 146.02 ? 1101 ASP   A O   1 
ATOM   370  C CB  . ASP   A 1 64  ? 24.468  1.626   37.638  1.00 135.20 ? 1101 ASP   A CB  1 
ATOM   371  C CG  . ASP   A 1 64  ? 23.135  1.659   38.368  1.00 132.83 ? 1101 ASP   A CG  1 
ATOM   372  O OD1 . ASP   A 1 64  ? 22.617  0.570   38.684  1.00 130.37 ? 1101 ASP   A OD1 1 
ATOM   373  O OD2 . ASP   A 1 64  ? 22.626  2.770   38.615  1.00 133.66 ? 1101 ASP   A OD2 1 
ATOM   374  N N   . GLY   A 1 65  ? 26.455  2.252   35.443  1.00 137.15 ? 1102 GLY   A N   1 
ATOM   375  C CA  . GLY   A 1 65  ? 27.704  2.089   34.717  1.00 139.24 ? 1102 GLY   A CA  1 
ATOM   376  C C   . GLY   A 1 65  ? 27.631  0.968   33.683  1.00 135.11 ? 1102 GLY   A C   1 
ATOM   377  O O   . GLY   A 1 65  ? 27.902  1.192   32.504  1.00 134.21 ? 1102 GLY   A O   1 
ATOM   378  N N   . LYS   A 1 66  ? 27.262  -0.234  34.142  1.00 132.76 ? 1103 LYS   A N   1 
ATOM   379  C CA  . LYS   A 1 66  ? 27.289  -1.430  33.313  1.00 129.61 ? 1103 LYS   A CA  1 
ATOM   380  C C   . LYS   A 1 66  ? 26.141  -1.394  32.307  1.00 123.91 ? 1103 LYS   A C   1 
ATOM   381  O O   . LYS   A 1 66  ? 25.119  -0.752  32.542  1.00 121.99 ? 1103 LYS   A O   1 
ATOM   382  C CB  . LYS   A 1 66  ? 27.221  -2.687  34.187  1.00 129.70 ? 1103 LYS   A CB  1 
ATOM   383  C CG  . LYS   A 1 66  ? 28.367  -2.855  35.178  1.00 135.45 ? 1103 LYS   A CG  1 
ATOM   384  C CD  . LYS   A 1 66  ? 29.726  -3.030  34.527  1.00 138.88 ? 1103 LYS   A CD  1 
ATOM   385  C CE  . LYS   A 1 66  ? 30.861  -3.110  35.526  1.00 145.30 ? 1103 LYS   A CE  1 
ATOM   386  N NZ  . LYS   A 1 66  ? 30.716  -4.269  36.438  1.00 145.98 ? 1103 LYS   A NZ  1 
ATOM   387  N N   . LYS   A 1 67  ? 26.331  -2.111  31.193  1.00 121.47 ? 1104 LYS   A N   1 
ATOM   388  C CA  . LYS   A 1 67  ? 25.429  -2.060  30.053  1.00 116.86 ? 1104 LYS   A CA  1 
ATOM   389  C C   . LYS   A 1 67  ? 24.384  -3.167  30.170  1.00 112.46 ? 1104 LYS   A C   1 
ATOM   390  O O   . LYS   A 1 67  ? 24.586  -4.143  30.890  1.00 113.13 ? 1104 LYS   A O   1 
ATOM   391  C CB  . LYS   A 1 67  ? 26.233  -2.189  28.755  1.00 117.51 ? 1104 LYS   A CB  1 
ATOM   392  C CG  . LYS   A 1 67  ? 27.273  -1.098  28.539  1.00 121.68 ? 1104 LYS   A CG  1 
ATOM   393  C CD  . LYS   A 1 67  ? 28.164  -1.318  27.336  1.00 122.87 ? 1104 LYS   A CD  1 
ATOM   394  C CE  . LYS   A 1 67  ? 29.179  -0.210  27.149  1.00 127.37 ? 1104 LYS   A CE  1 
ATOM   395  N NZ  . LYS   A 1 67  ? 30.085  -0.084  28.315  1.00 131.99 ? 1104 LYS   A NZ  1 
ATOM   396  N N   . ILE   A 1 68  ? 23.271  -2.994  29.446  1.00 108.23 ? 1105 ILE   A N   1 
ATOM   397  C CA  . ILE   A 1 68  ? 22.152  -3.922  29.486  1.00 104.19 ? 1105 ILE   A CA  1 
ATOM   398  C C   . ILE   A 1 68  ? 21.790  -4.319  28.057  1.00 101.14 ? 1105 ILE   A C   1 
ATOM   399  O O   . ILE   A 1 68  ? 21.688  -3.462  27.181  1.00 100.92 ? 1105 ILE   A O   1 
ATOM   400  C CB  . ILE   A 1 68  ? 20.946  -3.298  30.221  1.00 102.80 ? 1105 ILE   A CB  1 
ATOM   401  C CG1 . ILE   A 1 68  ? 21.314  -2.832  31.633  1.00 105.91 ? 1105 ILE   A CG1 1 
ATOM   402  C CG2 . ILE   A 1 68  ? 19.766  -4.261  30.230  1.00 99.28  ? 1105 ILE   A CG2 1 
ATOM   403  C CD1 . ILE   A 1 68  ? 20.212  -2.081  32.346  1.00 105.12 ? 1105 ILE   A CD1 1 
ATOM   404  N N   . HIS   A 1 69  ? 21.593  -5.626  27.840  1.00 98.94  ? 1106 HIS   A N   1 
ATOM   405  C CA  . HIS   A 1 69  ? 21.144  -6.146  26.559  1.00 96.17  ? 1106 HIS   A CA  1 
ATOM   406  C C   . HIS   A 1 69  ? 19.638  -5.925  26.431  1.00 92.94  ? 1106 HIS   A C   1 
ATOM   407  O O   . HIS   A 1 69  ? 18.873  -6.371  27.284  1.00 91.70  ? 1106 HIS   A O   1 
ATOM   408  C CB  . HIS   A 1 69  ? 21.506  -7.632  26.435  1.00 95.81  ? 1106 HIS   A CB  1 
ATOM   409  C CG  . HIS   A 1 69  ? 21.304  -8.229  25.073  1.00 94.02  ? 1106 HIS   A CG  1 
ATOM   410  N ND1 . HIS   A 1 69  ? 21.401  -9.574  24.812  1.00 93.43  ? 1106 HIS   A ND1 1 
ATOM   411  C CD2 . HIS   A 1 69  ? 20.996  -7.620  23.892  1.00 93.01  ? 1106 HIS   A CD2 1 
ATOM   412  C CE1 . HIS   A 1 69  ? 21.169  -9.789  23.519  1.00 92.20  ? 1106 HIS   A CE1 1 
ATOM   413  N NE2 . HIS   A 1 69  ? 20.915  -8.588  22.928  1.00 91.96  ? 1106 HIS   A NE2 1 
ATOM   414  N N   . CYS   A 1 70  ? 19.228  -5.227  25.364  1.00 91.87  ? 1107 CYS   A N   1 
ATOM   415  C CA  . CYS   A 1 70  ? 17.833  -4.874  25.150  1.00 89.40  ? 1107 CYS   A CA  1 
ATOM   416  C C   . CYS   A 1 70  ? 17.461  -5.063  23.681  1.00 87.94  ? 1107 CYS   A C   1 
ATOM   417  O O   . CYS   A 1 70  ? 18.328  -5.287  22.839  1.00 88.88  ? 1107 CYS   A O   1 
ATOM   418  C CB  . CYS   A 1 70  ? 17.575  -3.432  25.571  1.00 90.61  ? 1107 CYS   A CB  1 
ATOM   419  S SG  . CYS   A 1 70  ? 18.609  -2.230  24.694  1.00 93.47  ? 1107 CYS   A SG  1 
ATOM   420  N N   . ALA   A 1 71  ? 16.155  -4.976  23.398  1.00 85.85  ? 1108 ALA   A N   1 
ATOM   421  C CA  . ALA   A 1 71  ? 15.633  -5.049  22.042  1.00 85.01  ? 1108 ALA   A CA  1 
ATOM   422  C C   . ALA   A 1 71  ? 14.883  -3.758  21.724  1.00 85.45  ? 1108 ALA   A C   1 
ATOM   423  O O   . ALA   A 1 71  ? 14.011  -3.346  22.486  1.00 84.88  ? 1108 ALA   A O   1 
ATOM   424  C CB  . ALA   A 1 71  ? 14.738  -6.256  21.902  1.00 82.93  ? 1108 ALA   A CB  1 
ATOM   425  N N   . VAL   A 1 72  ? 15.231  -3.136  20.590  1.00 86.77  ? 1109 VAL   A N   1 
ATOM   426  C CA  . VAL   A 1 72  ? 14.698  -1.837  20.213  1.00 88.00  ? 1109 VAL   A CA  1 
ATOM   427  C C   . VAL   A 1 72  ? 13.810  -2.005  18.982  1.00 87.69  ? 1109 VAL   A C   1 
ATOM   428  O O   . VAL   A 1 72  ? 14.118  -2.807  18.103  1.00 87.45  ? 1109 VAL   A O   1 
ATOM   429  C CB  . VAL   A 1 72  ? 15.833  -0.827  19.949  1.00 90.61  ? 1109 VAL   A CB  1 
ATOM   430  C CG1 . VAL   A 1 72  ? 15.293  0.554   19.604  1.00 92.34  ? 1109 VAL   A CG1 1 
ATOM   431  C CG2 . VAL   A 1 72  ? 16.801  -0.748  21.121  1.00 91.48  ? 1109 VAL   A CG2 1 
ATOM   432  N N   . LYS   A 1 73  ? 12.714  -1.236  18.932  1.00 88.15  ? 1110 LYS   A N   1 
ATOM   433  C CA  . LYS   A 1 73  ? 11.803  -1.244  17.797  1.00 88.64  ? 1110 LYS   A CA  1 
ATOM   434  C C   . LYS   A 1 73  ? 11.497  0.191   17.375  1.00 91.37  ? 1110 LYS   A C   1 
ATOM   435  O O   . LYS   A 1 73  ? 11.304  1.061   18.220  1.00 91.99  ? 1110 LYS   A O   1 
ATOM   436  C CB  . LYS   A 1 73  ? 10.503  -1.977  18.146  1.00 86.77  ? 1110 LYS   A CB  1 
ATOM   437  C CG  . LYS   A 1 73  ? 9.485   -2.055  17.014  1.00 87.57  ? 1110 LYS   A CG  1 
ATOM   438  C CD  . LYS   A 1 73  ? 8.195   -2.745  17.395  1.00 86.19  ? 1110 LYS   A CD  1 
ATOM   439  C CE  . LYS   A 1 73  ? 7.179   -2.748  16.273  1.00 87.63  ? 1110 LYS   A CE  1 
ATOM   440  N NZ  . LYS   A 1 73  ? 5.912   -3.400  16.680  1.00 86.70  ? 1110 LYS   A NZ  1 
ATOM   441  N N   . SER   A 1 74  ? 11.439  0.410   16.055  1.00 93.37  ? 1111 SER   A N   1 
ATOM   442  C CA  . SER   A 1 74  ? 11.095  1.703   15.485  1.00 96.52  ? 1111 SER   A CA  1 
ATOM   443  C C   . SER   A 1 74  ? 9.606   1.731   15.150  1.00 97.28  ? 1111 SER   A C   1 
ATOM   444  O O   . SER   A 1 74  ? 9.128   0.897   14.384  1.00 96.82  ? 1111 SER   A O   1 
ATOM   445  C CB  . SER   A 1 74  ? 11.935  1.990   14.268  1.00 98.73  ? 1111 SER   A CB  1 
ATOM   446  O OG  . SER   A 1 74  ? 11.624  3.266   13.726  1.00 101.93 ? 1111 SER   A OG  1 
ATOM   447  N N   . LEU   A 1 75  ? 8.888   2.702   15.730  1.00 99.04  ? 1112 LEU   A N   1 
ATOM   448  C CA  . LEU   A 1 75  ? 7.451   2.835   15.545  1.00 100.40 ? 1112 LEU   A CA  1 
ATOM   449  C C   . LEU   A 1 75  ? 7.170   3.881   14.470  1.00 104.71 ? 1112 LEU   A C   1 
ATOM   450  O O   . LEU   A 1 75  ? 7.121   5.074   14.761  1.00 107.06 ? 1112 LEU   A O   1 
ATOM   451  C CB  . LEU   A 1 75  ? 6.808   3.233   16.878  1.00 99.77  ? 1112 LEU   A CB  1 
ATOM   452  C CG  . LEU   A 1 75  ? 6.644   2.109   17.900  1.00 96.46  ? 1112 LEU   A CG  1 
ATOM   453  C CD1 . LEU   A 1 75  ? 7.996   1.630   18.414  1.00 94.75  ? 1112 LEU   A CD1 1 
ATOM   454  C CD2 . LEU   A 1 75  ? 5.755   2.560   19.051  1.00 96.52  ? 1112 LEU   A CD2 1 
ATOM   455  N N   . ASN   A 1 76  ? 6.967   3.413   13.232  1.00 106.32 ? 1113 ASN   A N   1 
ATOM   456  C CA  . ASN   A 1 76  ? 6.744   4.289   12.093  1.00 110.83 ? 1113 ASN   A CA  1 
ATOM   457  C C   . ASN   A 1 76  ? 5.248   4.356   11.794  1.00 112.89 ? 1113 ASN   A C   1 
ATOM   458  O O   . ASN   A 1 76  ? 4.815   4.024   10.691  1.00 114.74 ? 1113 ASN   A O   1 
ATOM   459  C CB  . ASN   A 1 76  ? 7.549   3.824   10.876  1.00 111.87 ? 1113 ASN   A CB  1 
ATOM   460  C CG  . ASN   A 1 76  ? 9.034   3.730   11.158  1.00 110.65 ? 1113 ASN   A CG  1 
ATOM   461  O OD1 . ASN   A 1 76  ? 9.671   4.724   11.499  1.00 112.21 ? 1113 ASN   A OD1 1 
ATOM   462  N ND2 . ASN   A 1 76  ? 9.595   2.539   11.018  1.00 108.31 ? 1113 ASN   A ND2 1 
ATOM   463  N N   . ARG   A 1 77  ? 4.469   4.791   12.794  1.00 112.99 ? 1114 ARG   A N   1 
ATOM   464  C CA  . ARG   A 1 77  ? 3.027   4.933   12.667  1.00 115.29 ? 1114 ARG   A CA  1 
ATOM   465  C C   . ARG   A 1 77  ? 2.562   6.130   13.496  1.00 117.11 ? 1114 ARG   A C   1 
ATOM   466  O O   . ARG   A 1 77  ? 1.611   6.021   14.269  1.00 116.55 ? 1114 ARG   A O   1 
ATOM   467  C CB  . ARG   A 1 77  ? 2.309   3.663   13.140  1.00 112.49 ? 1114 ARG   A CB  1 
ATOM   468  C CG  . ARG   A 1 77  ? 2.700   2.389   12.404  1.00 110.90 ? 1114 ARG   A CG  1 
ATOM   469  C CD  . ARG   A 1 77  ? 1.810   1.232   12.817  1.00 108.97 ? 1114 ARG   A CD  1 
ATOM   470  N NE  . ARG   A 1 77  ? 2.204   -0.036  12.218  1.00 107.50 ? 1114 ARG   A NE  1 
ATOM   471  C CZ  . ARG   A 1 77  ? 1.549   -1.180  12.380  1.00 106.14 ? 1114 ARG   A CZ  1 
ATOM   472  N NH1 . ARG   A 1 77  ? 0.409   -1.203  13.048  1.00 106.24 ? 1114 ARG   A NH1 1 
ATOM   473  N NH2 . ARG   A 1 77  ? 2.032   -2.299  11.868  1.00 104.88 ? 1114 ARG   A NH2 1 
ATOM   474  N N   . ILE   A 1 78  ? 3.238   7.273   13.321  1.00 119.49 ? 1115 ILE   A N   1 
ATOM   475  C CA  . ILE   A 1 78  ? 2.990   8.443   14.149  1.00 121.23 ? 1115 ILE   A CA  1 
ATOM   476  C C   . ILE   A 1 78  ? 3.326   9.706   13.357  1.00 125.74 ? 1115 ILE   A C   1 
ATOM   477  O O   . ILE   A 1 78  ? 4.275   9.719   12.575  1.00 126.29 ? 1115 ILE   A O   1 
ATOM   478  C CB  . ILE   A 1 78  ? 3.789   8.351   15.466  1.00 117.93 ? 1115 ILE   A CB  1 
ATOM   479  C CG1 . ILE   A 1 78  ? 3.289   9.355   16.508  1.00 119.56 ? 1115 ILE   A CG1 1 
ATOM   480  C CG2 . ILE   A 1 78  ? 5.285   8.489   15.216  1.00 117.45 ? 1115 ILE   A CG2 1 
ATOM   481  C CD1 . ILE   A 1 78  ? 3.933   9.202   17.868  1.00 116.62 ? 1115 ILE   A CD1 1 
ATOM   482  N N   . THR   A 1 79  ? 2.533   10.763  13.579  1.00 129.19 ? 1116 THR   A N   1 
ATOM   483  C CA  . THR   A 1 79  ? 2.729   12.042  12.915  1.00 134.14 ? 1116 THR   A CA  1 
ATOM   484  C C   . THR   A 1 79  ? 3.801   12.840  13.668  1.00 133.95 ? 1116 THR   A C   1 
ATOM   485  O O   . THR   A 1 79  ? 4.105   13.958  13.207  1.00 138.16 ? 1116 THR   A O   1 
ATOM   486  C CB  . THR   A 1 79  ? 1.410   12.819  12.813  1.00 138.56 ? 1116 THR   A CB  1 
ATOM   487  O OG1 . THR   A 1 79  ? 0.967   13.149  14.130  1.00 137.53 ? 1116 THR   A OG1 1 
ATOM   488  C CG2 . THR   A 1 79  ? 0.327   12.046  12.092  1.00 139.22 ? 1116 THR   A CG2 1 
ATOM   489  N N   . GLU   A 1 83  ? -1.963  12.965  18.905  1.00 130.20 ? 1120 GLU   A N   1 
ATOM   490  C CA  . GLU   A 1 83  ? -1.384  11.736  18.293  1.00 126.26 ? 1120 GLU   A CA  1 
ATOM   491  C C   . GLU   A 1 83  ? -0.142  11.320  19.079  1.00 122.04 ? 1120 GLU   A C   1 
ATOM   492  O O   . GLU   A 1 83  ? -0.077  10.203  19.591  1.00 117.77 ? 1120 GLU   A O   1 
ATOM   493  C CB  . GLU   A 1 83  ? -1.069  11.985  16.814  1.00 128.93 ? 1120 GLU   A CB  1 
ATOM   494  C CG  . GLU   A 1 83  ? -0.474  10.785  16.095  1.00 125.49 ? 1120 GLU   A CG  1 
ATOM   495  C CD  . GLU   A 1 83  ? -1.337  9.534   16.110  1.00 123.00 ? 1120 GLU   A CD  1 
ATOM   496  O OE1 . GLU   A 1 83  ? -0.883  8.511   16.659  1.00 118.34 ? 1120 GLU   A OE1 1 
ATOM   497  O OE2 . GLU   A 1 83  ? -2.460  9.587   15.572  1.00 126.03 ? 1120 GLU   A OE2 1 
ATOM   498  N N   . VAL   A 1 84  ? 0.836   12.231  19.161  1.00 123.64 ? 1121 VAL   A N   1 
ATOM   499  C CA  . VAL   A 1 84  ? 2.061   11.998  19.912  1.00 120.61 ? 1121 VAL   A CA  1 
ATOM   500  C C   . VAL   A 1 84  ? 1.749   12.034  21.407  1.00 119.37 ? 1121 VAL   A C   1 
ATOM   501  O O   . VAL   A 1 84  ? 2.351   11.295  22.183  1.00 115.68 ? 1121 VAL   A O   1 
ATOM   502  C CB  . VAL   A 1 84  ? 3.162   13.014  19.542  1.00 123.28 ? 1121 VAL   A CB  1 
ATOM   503  C CG1 . VAL   A 1 84  ? 3.502   12.960  18.060  1.00 124.73 ? 1121 VAL   A CG1 1 
ATOM   504  C CG2 . VAL   A 1 84  ? 2.809   14.437  19.957  1.00 127.81 ? 1121 VAL   A CG2 1 
ATOM   505  N N   . SER   A 1 85  ? 0.803   12.899  21.795  1.00 122.76 ? 1122 SER   A N   1 
ATOM   506  C CA  . SER   A 1 85  ? 0.410   13.065  23.186  1.00 122.43 ? 1122 SER   A CA  1 
ATOM   507  C C   . SER   A 1 85  ? -0.121  11.751  23.756  1.00 118.38 ? 1122 SER   A C   1 
ATOM   508  O O   . SER   A 1 85  ? 0.181   11.403  24.895  1.00 116.24 ? 1122 SER   A O   1 
ATOM   509  C CB  . SER   A 1 85  ? -0.615  14.163  23.321  1.00 127.19 ? 1122 SER   A CB  1 
ATOM   510  O OG  . SER   A 1 85  ? -0.150  15.369  22.731  1.00 131.42 ? 1122 SER   A OG  1 
ATOM   511  N N   . GLN   A 1 86  ? -0.908  11.033  22.945  1.00 117.77 ? 1123 GLN   A N   1 
ATOM   512  C CA  . GLN   A 1 86  ? -1.565  9.806   23.367  1.00 114.49 ? 1123 GLN   A CA  1 
ATOM   513  C C   . GLN   A 1 86  ? -0.527  8.700   23.569  1.00 109.74 ? 1123 GLN   A C   1 
ATOM   514  O O   . GLN   A 1 86  ? -0.706  7.835   24.423  1.00 106.99 ? 1123 GLN   A O   1 
ATOM   515  C CB  . GLN   A 1 86  ? -2.630  9.417   22.337  1.00 115.97 ? 1123 GLN   A CB  1 
ATOM   516  C CG  . GLN   A 1 86  ? -3.642  8.391   22.835  1.00 114.19 ? 1123 GLN   A CG  1 
ATOM   517  C CD  . GLN   A 1 86  ? -3.206  6.955   22.660  1.00 109.92 ? 1123 GLN   A CD  1 
ATOM   518  O OE1 . GLN   A 1 86  ? -2.172  6.658   22.066  1.00 108.40 ? 1123 GLN   A OE1 1 
ATOM   519  N NE2 . GLN   A 1 86  ? -4.017  6.041   23.168  1.00 108.33 ? 1123 GLN   A NE2 1 
ATOM   520  N N   . PHE   A 1 87  ? 0.557   8.743   22.783  1.00 109.05 ? 1124 PHE   A N   1 
ATOM   521  C CA  . PHE   A 1 87  ? 1.603   7.733   22.840  1.00 105.12 ? 1124 PHE   A CA  1 
ATOM   522  C C   . PHE   A 1 87  ? 2.379   7.842   24.152  1.00 103.69 ? 1124 PHE   A C   1 
ATOM   523  O O   . PHE   A 1 87  ? 2.596   6.836   24.825  1.00 100.53 ? 1124 PHE   A O   1 
ATOM   524  C CB  . PHE   A 1 87  ? 2.534   7.866   21.632  1.00 105.71 ? 1124 PHE   A CB  1 
ATOM   525  C CG  . PHE   A 1 87  ? 3.692   6.899   21.614  1.00 102.37 ? 1124 PHE   A CG  1 
ATOM   526  C CD1 . PHE   A 1 87  ? 3.478   5.532   21.715  1.00 99.10  ? 1124 PHE   A CD1 1 
ATOM   527  C CD2 . PHE   A 1 87  ? 4.997   7.354   21.488  1.00 102.83 ? 1124 PHE   A CD2 1 
ATOM   528  C CE1 . PHE   A 1 87  ? 4.543   4.644   21.697  1.00 96.47  ? 1124 PHE   A CE1 1 
ATOM   529  C CE2 . PHE   A 1 87  ? 6.060   6.464   21.469  1.00 100.21 ? 1124 PHE   A CE2 1 
ATOM   530  C CZ  . PHE   A 1 87  ? 5.832   5.111   21.573  1.00 97.06  ? 1124 PHE   A CZ  1 
ATOM   531  N N   . LEU   A 1 88  ? 2.797   9.067   24.501  1.00 106.33 ? 1125 LEU   A N   1 
ATOM   532  C CA  . LEU   A 1 88  ? 3.604   9.304   25.690  1.00 105.88 ? 1125 LEU   A CA  1 
ATOM   533  C C   . LEU   A 1 88  ? 2.785   9.062   26.957  1.00 105.08 ? 1125 LEU   A C   1 
ATOM   534  O O   . LEU   A 1 88  ? 3.344   8.688   27.986  1.00 103.60 ? 1125 LEU   A O   1 
ATOM   535  C CB  . LEU   A 1 88  ? 4.162   10.733  25.663  1.00 109.67 ? 1125 LEU   A CB  1 
ATOM   536  C CG  . LEU   A 1 88  ? 5.461   10.924  24.879  1.00 110.04 ? 1125 LEU   A CG  1 
ATOM   537  C CD1 . LEU   A 1 88  ? 5.194   11.063  23.388  1.00 111.28 ? 1125 LEU   A CD1 1 
ATOM   538  C CD2 . LEU   A 1 88  ? 6.233   12.129  25.395  1.00 113.22 ? 1125 LEU   A CD2 1 
ATOM   539  N N   . THR   A 1 89  ? 1.466   9.284   26.877  1.00 106.36 ? 1126 THR   A N   1 
ATOM   540  C CA  . THR   A 1 89  ? 0.569   9.043   27.997  1.00 106.01 ? 1126 THR   A CA  1 
ATOM   541  C C   . THR   A 1 89  ? 0.638   7.575   28.417  1.00 101.98 ? 1126 THR   A C   1 
ATOM   542  O O   . THR   A 1 89  ? 0.652   7.271   29.608  1.00 101.08 ? 1126 THR   A O   1 
ATOM   543  C CB  . THR   A 1 89  ? -0.869  9.447   27.649  1.00 108.52 ? 1126 THR   A CB  1 
ATOM   544  O OG1 . THR   A 1 89  ? -0.866  10.833  27.306  1.00 112.68 ? 1126 THR   A OG1 1 
ATOM   545  C CG2 . THR   A 1 89  ? -1.845  9.205   28.781  1.00 108.53 ? 1126 THR   A CG2 1 
ATOM   546  N N   . GLU   A 1 90  ? 0.680   6.678   27.423  1.00 99.95  ? 1127 GLU   A N   1 
ATOM   547  C CA  . GLU   A 1 90  ? 0.749   5.245   27.662  1.00 96.48  ? 1127 GLU   A CA  1 
ATOM   548  C C   . GLU   A 1 90  ? 2.133   4.862   28.186  1.00 94.57  ? 1127 GLU   A C   1 
ATOM   549  O O   . GLU   A 1 90  ? 2.266   3.884   28.918  1.00 92.40  ? 1127 GLU   A O   1 
ATOM   550  C CB  . GLU   A 1 90  ? 0.417   4.482   26.378  1.00 95.50  ? 1127 GLU   A CB  1 
ATOM   551  C CG  . GLU   A 1 90  ? -1.022  4.660   25.927  1.00 97.53  ? 1127 GLU   A CG  1 
ATOM   552  C CD  . GLU   A 1 90  ? -1.385  3.957   24.630  1.00 97.25  ? 1127 GLU   A CD  1 
ATOM   553  O OE1 . GLU   A 1 90  ? -2.571  4.009   24.245  1.00 99.17  ? 1127 GLU   A OE1 1 
ATOM   554  O OE2 . GLU   A 1 90  ? -0.484  3.362   24.005  1.00 95.53  ? 1127 GLU   A OE2 1 
ATOM   555  N N   . GLY   A 1 91  ? 3.156   5.634   27.796  1.00 95.77  ? 1128 GLY   A N   1 
ATOM   556  C CA  . GLY   A 1 91  ? 4.515   5.433   28.271  1.00 94.85  ? 1128 GLY   A CA  1 
ATOM   557  C C   . GLY   A 1 91  ? 4.629   5.540   29.791  1.00 95.26  ? 1128 GLY   A C   1 
ATOM   558  O O   . GLY   A 1 91  ? 5.424   4.829   30.402  1.00 93.85  ? 1128 GLY   A O   1 
ATOM   559  N N   . ILE   A 1 92  ? 3.829   6.435   30.388  1.00 97.61  ? 1129 ILE   A N   1 
ATOM   560  C CA  . ILE   A 1 92  ? 3.808   6.627   31.831  1.00 98.50  ? 1129 ILE   A CA  1 
ATOM   561  C C   . ILE   A 1 92  ? 3.246   5.371   32.495  1.00 95.76  ? 1129 ILE   A C   1 
ATOM   562  O O   . ILE   A 1 92  ? 3.750   4.935   33.528  1.00 95.28  ? 1129 ILE   A O   1 
ATOM   563  C CB  . ILE   A 1 92  ? 2.990   7.878   32.216  1.00 102.05 ? 1129 ILE   A CB  1 
ATOM   564  C CG1 . ILE   A 1 92  ? 3.554   9.154   31.583  1.00 105.13 ? 1129 ILE   A CG1 1 
ATOM   565  C CG2 . ILE   A 1 92  ? 2.882   8.007   33.731  1.00 103.15 ? 1129 ILE   A CG2 1 
ATOM   566  C CD1 . ILE   A 1 92  ? 2.668   10.369  31.751  1.00 108.82 ? 1129 ILE   A CD1 1 
ATOM   567  N N   . ILE   A 1 93  ? 2.194   4.806   31.890  1.00 94.24  ? 1130 ILE   A N   1 
ATOM   568  C CA  . ILE   A 1 93  ? 1.507   3.644   32.432  1.00 92.04  ? 1130 ILE   A CA  1 
ATOM   569  C C   . ILE   A 1 93  ? 2.408   2.418   32.298  1.00 89.05  ? 1130 ILE   A C   1 
ATOM   570  O O   . ILE   A 1 93  ? 2.516   1.623   33.230  1.00 88.02  ? 1130 ILE   A O   1 
ATOM   571  C CB  . ILE   A 1 93  ? 0.146   3.437   31.732  1.00 92.05  ? 1130 ILE   A CB  1 
ATOM   572  C CG1 . ILE   A 1 93  ? -0.747  4.680   31.819  1.00 95.23  ? 1130 ILE   A CG1 1 
ATOM   573  C CG2 . ILE   A 1 93  ? -0.558  2.198   32.267  1.00 90.29  ? 1130 ILE   A CG2 1 
ATOM   574  C CD1 . ILE   A 1 93  ? -1.012  5.165   33.228  1.00 96.88  ? 1130 ILE   A CD1 1 
ATOM   575  N N   . MET   A 1 94  ? 3.052   2.283   31.132  1.00 87.94  ? 1131 MET   A N   1 
ATOM   576  C CA  . MET   A 1 94  ? 3.865   1.119   30.811  1.00 85.43  ? 1131 MET   A CA  1 
ATOM   577  C C   . MET   A 1 94  ? 5.124   1.093   31.676  1.00 85.26  ? 1131 MET   A C   1 
ATOM   578  O O   . MET   A 1 94  ? 5.527   0.032   32.149  1.00 83.68  ? 1131 MET   A O   1 
ATOM   579  C CB  . MET   A 1 94  ? 4.272   1.139   29.334  1.00 85.31  ? 1131 MET   A CB  1 
ATOM   580  C CG  . MET   A 1 94  ? 3.160   0.719   28.390  1.00 84.90  ? 1131 MET   A CG  1 
ATOM   581  S SD  . MET   A 1 94  ? 2.767   -1.042  28.510  1.00 82.53  ? 1131 MET   A SD  1 
ATOM   582  C CE  . MET   A 1 94  ? 2.041   -1.324  26.896  1.00 82.53  ? 1131 MET   A CE  1 
ATOM   583  N N   . LYS   A 1 95  ? 5.741   2.267   31.865  1.00 87.00  ? 1132 LYS   A N   1 
ATOM   584  C CA  . LYS   A 1 95  ? 6.988   2.389   32.605  1.00 87.64  ? 1132 LYS   A CA  1 
ATOM   585  C C   . LYS   A 1 95  ? 6.780   1.990   34.065  1.00 87.54  ? 1132 LYS   A C   1 
ATOM   586  O O   . LYS   A 1 95  ? 7.660   1.377   34.667  1.00 87.49  ? 1132 LYS   A O   1 
ATOM   587  C CB  . LYS   A 1 95  ? 7.525   3.821   32.496  1.00 90.55  ? 1132 LYS   A CB  1 
ATOM   588  C CG  . LYS   A 1 95  ? 8.760   4.135   33.333  1.00 92.57  ? 1132 LYS   A CG  1 
ATOM   589  C CD  . LYS   A 1 95  ? 9.954   3.250   33.046  1.00 91.48  ? 1132 LYS   A CD  1 
ATOM   590  C CE  . LYS   A 1 95  ? 11.169  3.626   33.867  1.00 94.09  ? 1132 LYS   A CE  1 
ATOM   591  N NZ  . LYS   A 1 95  ? 12.332  2.761   33.559  1.00 93.48  ? 1132 LYS   A NZ  1 
ATOM   592  N N   . ASP   A 1 96  ? 5.610   2.332   34.622  1.00 87.69  ? 1133 ASP   A N   1 
ATOM   593  C CA  . ASP   A 1 96  ? 5.317   2.088   36.026  1.00 88.10  ? 1133 ASP   A CA  1 
ATOM   594  C C   . ASP   A 1 96  ? 4.613   0.742   36.199  1.00 85.41  ? 1133 ASP   A C   1 
ATOM   595  O O   . ASP   A 1 96  ? 3.789   0.589   37.099  1.00 86.00  ? 1133 ASP   A O   1 
ATOM   596  C CB  . ASP   A 1 96  ? 4.494   3.239   36.612  1.00 90.62  ? 1133 ASP   A CB  1 
ATOM   597  C CG  . ASP   A 1 96  ? 5.256   4.551   36.691  1.00 93.47  ? 1133 ASP   A CG  1 
ATOM   598  O OD1 . ASP   A 1 96  ? 5.358   5.102   37.805  1.00 95.95  ? 1133 ASP   A OD1 1 
ATOM   599  O OD2 . ASP   A 1 96  ? 5.750   5.008   35.641  1.00 93.48  ? 1133 ASP   A OD2 1 
ATOM   600  N N   . PHE   A 1 97  ? 4.946   -0.229  35.337  1.00 82.60  ? 1134 PHE   A N   1 
ATOM   601  C CA  . PHE   A 1 97  ? 4.553   -1.616  35.525  1.00 80.30  ? 1134 PHE   A CA  1 
ATOM   602  C C   . PHE   A 1 97  ? 5.777   -2.427  35.942  1.00 79.79  ? 1134 PHE   A C   1 
ATOM   603  O O   . PHE   A 1 97  ? 6.890   -2.152  35.498  1.00 80.10  ? 1134 PHE   A O   1 
ATOM   604  C CB  . PHE   A 1 97  ? 3.935   -2.195  34.248  1.00 78.18  ? 1134 PHE   A CB  1 
ATOM   605  C CG  . PHE   A 1 97  ? 2.519   -1.772  33.933  1.00 78.41  ? 1134 PHE   A CG  1 
ATOM   606  C CD1 . PHE   A 1 97  ? 1.763   -1.016  34.819  1.00 80.22  ? 1134 PHE   A CD1 1 
ATOM   607  C CD2 . PHE   A 1 97  ? 1.937   -2.144  32.730  1.00 77.18  ? 1134 PHE   A CD2 1 
ATOM   608  C CE1 . PHE   A 1 97  ? 0.464   -0.644  34.508  1.00 80.87  ? 1134 PHE   A CE1 1 
ATOM   609  C CE2 . PHE   A 1 97  ? 0.638   -1.769  32.420  1.00 77.97  ? 1134 PHE   A CE2 1 
ATOM   610  C CZ  . PHE   A 1 97  ? -0.096  -1.020  33.310  1.00 79.83  ? 1134 PHE   A CZ  1 
ATOM   611  N N   . SER   A 1 98  ? 5.548   -3.428  36.799  1.00 79.22  ? 1135 SER   A N   1 
ATOM   612  C CA  . SER   A 1 98  ? 6.605   -4.299  37.283  1.00 79.28  ? 1135 SER   A CA  1 
ATOM   613  C C   . SER   A 1 98  ? 5.996   -5.591  37.821  1.00 78.22  ? 1135 SER   A C   1 
ATOM   614  O O   . SER   A 1 98  ? 5.380   -5.594  38.885  1.00 79.36  ? 1135 SER   A O   1 
ATOM   615  C CB  . SER   A 1 98  ? 7.439   -3.605  38.331  1.00 82.07  ? 1135 SER   A CB  1 
ATOM   616  O OG  . SER   A 1 98  ? 8.497   -4.443  38.774  1.00 82.88  ? 1135 SER   A OG  1 
ATOM   617  N N   . HIS   A 1 99  ? 6.167   -6.680  37.063  1.00 76.19  ? 1136 HIS   A N   1 
ATOM   618  C CA  . HIS   A 1 99  ? 5.681   -7.991  37.458  1.00 75.50  ? 1136 HIS   A CA  1 
ATOM   619  C C   . HIS   A 1 99  ? 6.538   -9.062  36.787  1.00 74.59  ? 1136 HIS   A C   1 
ATOM   620  O O   . HIS   A 1 99  ? 6.946   -8.890  35.640  1.00 73.48  ? 1136 HIS   A O   1 
ATOM   621  C CB  . HIS   A 1 99  ? 4.199   -8.139  37.089  1.00 74.16  ? 1136 HIS   A CB  1 
ATOM   622  C CG  . HIS   A 1 99  ? 3.514   -9.335  37.678  1.00 74.02  ? 1136 HIS   A CG  1 
ATOM   623  N ND1 . HIS   A 1 99  ? 3.240   -9.477  39.016  1.00 75.72  ? 1136 HIS   A ND1 1 
ATOM   624  C CD2 . HIS   A 1 99  ? 3.031   -10.447 37.056  1.00 72.65  ? 1136 HIS   A CD2 1 
ATOM   625  C CE1 . HIS   A 1 99  ? 2.623   -10.640 39.216  1.00 75.43  ? 1136 HIS   A CE1 1 
ATOM   626  N NE2 . HIS   A 1 99  ? 2.484   -11.260 38.011  1.00 73.51  ? 1136 HIS   A NE2 1 
ATOM   627  N N   . PRO   A 1 100 ? 6.849   -10.190 37.472  1.00 75.35  ? 1137 PRO   A N   1 
ATOM   628  C CA  . PRO   A 1 100 ? 7.655   -11.261 36.877  1.00 74.83  ? 1137 PRO   A CA  1 
ATOM   629  C C   . PRO   A 1 100 ? 7.146   -11.782 35.533  1.00 72.51  ? 1137 PRO   A C   1 
ATOM   630  O O   . PRO   A 1 100 ? 7.940   -12.219 34.703  1.00 72.00  ? 1137 PRO   A O   1 
ATOM   631  C CB  . PRO   A 1 100 ? 7.579   -12.387 37.920  1.00 76.22  ? 1137 PRO   A CB  1 
ATOM   632  C CG  . PRO   A 1 100 ? 7.358   -11.663 39.228  1.00 78.20  ? 1137 PRO   A CG  1 
ATOM   633  C CD  . PRO   A 1 100 ? 6.477   -10.486 38.865  1.00 77.10  ? 1137 PRO   A CD  1 
ATOM   634  N N   . ASN   A 1 101 ? 5.822   -11.735 35.335  1.00 71.43  ? 1138 ASN   A N   1 
ATOM   635  C CA  . ASN   A 1 101 ? 5.197   -12.246 34.126  1.00 69.81  ? 1138 ASN   A CA  1 
ATOM   636  C C   . ASN   A 1 101 ? 4.586   -11.098 33.323  1.00 69.22  ? 1138 ASN   A C   1 
ATOM   637  O O   . ASN   A 1 101 ? 3.496   -11.241 32.770  1.00 68.59  ? 1138 ASN   A O   1 
ATOM   638  C CB  . ASN   A 1 101 ? 4.151   -13.314 34.459  1.00 69.63  ? 1138 ASN   A CB  1 
ATOM   639  C CG  . ASN   A 1 101 ? 4.702   -14.416 35.339  1.00 70.77  ? 1138 ASN   A CG  1 
ATOM   640  O OD1 . ASN   A 1 101 ? 4.237   -14.613 36.460  1.00 71.86  ? 1138 ASN   A OD1 1 
ATOM   641  N ND2 . ASN   A 1 101 ? 5.700   -15.131 34.846  1.00 70.79  ? 1138 ASN   A ND2 1 
ATOM   642  N N   . VAL   A 1 102 ? 5.301   -9.966  33.259  1.00 69.81  ? 1139 VAL   A N   1 
ATOM   643  C CA  . VAL   A 1 102 ? 4.923   -8.842  32.415  1.00 69.68  ? 1139 VAL   A CA  1 
ATOM   644  C C   . VAL   A 1 102 ? 6.202   -8.193  31.889  1.00 70.27  ? 1139 VAL   A C   1 
ATOM   645  O O   . VAL   A 1 102 ? 7.081   -7.836  32.670  1.00 71.50  ? 1139 VAL   A O   1 
ATOM   646  C CB  . VAL   A 1 102 ? 4.051   -7.817  33.168  1.00 70.64  ? 1139 VAL   A CB  1 
ATOM   647  C CG1 . VAL   A 1 102 ? 3.810   -6.562  32.341  1.00 70.96  ? 1139 VAL   A CG1 1 
ATOM   648  C CG2 . VAL   A 1 102 ? 2.727   -8.416  33.623  1.00 70.56  ? 1139 VAL   A CG2 1 
ATOM   649  N N   . LEU   A 1 103 ? 6.287   -8.042  30.561  1.00 69.85  ? 1140 LEU   A N   1 
ATOM   650  C CA  . LEU   A 1 103 ? 7.446   -7.434  29.927  1.00 70.62  ? 1140 LEU   A CA  1 
ATOM   651  C C   . LEU   A 1 103 ? 7.407   -5.928  30.169  1.00 72.20  ? 1140 LEU   A C   1 
ATOM   652  O O   . LEU   A 1 103 ? 6.548   -5.232  29.630  1.00 72.26  ? 1140 LEU   A O   1 
ATOM   653  C CB  . LEU   A 1 103 ? 7.433   -7.765  28.430  1.00 69.73  ? 1140 LEU   A CB  1 
ATOM   654  C CG  . LEU   A 1 103 ? 8.659   -7.307  27.639  1.00 70.32  ? 1140 LEU   A CG  1 
ATOM   655  C CD1 . LEU   A 1 103 ? 9.903   -8.072  28.067  1.00 70.71  ? 1140 LEU   A CD1 1 
ATOM   656  C CD2 . LEU   A 1 103 ? 8.427   -7.463  26.144  1.00 69.85  ? 1140 LEU   A CD2 1 
ATOM   657  N N   . SER   A 1 104 ? 8.346   -5.441  30.990  1.00 74.06  ? 1141 SER   A N   1 
ATOM   658  C CA  . SER   A 1 104 ? 8.378   -4.045  31.394  1.00 76.03  ? 1141 SER   A CA  1 
ATOM   659  C C   . SER   A 1 104 ? 8.950   -3.181  30.272  1.00 76.84  ? 1141 SER   A C   1 
ATOM   660  O O   . SER   A 1 104 ? 9.811   -3.624  29.514  1.00 76.37  ? 1141 SER   A O   1 
ATOM   661  C CB  . SER   A 1 104 ? 9.164   -3.869  32.670  1.00 77.84  ? 1141 SER   A CB  1 
ATOM   662  O OG  . SER   A 1 104 ? 10.525  -4.233  32.485  1.00 78.53  ? 1141 SER   A OG  1 
ATOM   663  N N   . LEU   A 1 105 ? 8.450   -1.943  30.189  1.00 78.38  ? 1142 LEU   A N   1 
ATOM   664  C CA  . LEU   A 1 105 ? 8.936   -0.954  29.241  1.00 79.84  ? 1142 LEU   A CA  1 
ATOM   665  C C   . LEU   A 1 105 ? 10.084  -0.186  29.892  1.00 82.30  ? 1142 LEU   A C   1 
ATOM   666  O O   . LEU   A 1 105 ? 9.892   0.454   30.925  1.00 83.88  ? 1142 LEU   A O   1 
ATOM   667  C CB  . LEU   A 1 105 ? 7.763   -0.043  28.858  1.00 80.52  ? 1142 LEU   A CB  1 
ATOM   668  C CG  . LEU   A 1 105 ? 8.063   1.135   27.926  1.00 82.27  ? 1142 LEU   A CG  1 
ATOM   669  C CD1 . LEU   A 1 105 ? 8.691   2.303   28.675  1.00 84.79  ? 1142 LEU   A CD1 1 
ATOM   670  C CD2 . LEU   A 1 105 ? 8.936   0.707   26.755  1.00 81.74  ? 1142 LEU   A CD2 1 
ATOM   671  N N   . LEU   A 1 106 ? 11.278  -0.273  29.291  1.00 83.11  ? 1143 LEU   A N   1 
ATOM   672  C CA  . LEU   A 1 106 ? 12.464  0.375   29.830  1.00 85.77  ? 1143 LEU   A CA  1 
ATOM   673  C C   . LEU   A 1 106 ? 12.366  1.882   29.609  1.00 88.41  ? 1143 LEU   A C   1 
ATOM   674  O O   . LEU   A 1 106 ? 12.431  2.654   30.563  1.00 90.51  ? 1143 LEU   A O   1 
ATOM   675  C CB  . LEU   A 1 106 ? 13.717  -0.201  29.160  1.00 85.73  ? 1143 LEU   A CB  1 
ATOM   676  C CG  . LEU   A 1 106 ? 14.002  -1.679  29.427  1.00 84.12  ? 1143 LEU   A CG  1 
ATOM   677  C CD1 . LEU   A 1 106 ? 15.393  -2.055  28.937  1.00 85.18  ? 1143 LEU   A CD1 1 
ATOM   678  C CD2 . LEU   A 1 106 ? 13.852  -2.016  30.904  1.00 84.58  ? 1143 LEU   A CD2 1 
ATOM   679  N N   . GLY   A 1 107 ? 12.209  2.288   28.344  1.00 88.88  ? 1144 GLY   A N   1 
ATOM   680  C CA  . GLY   A 1 107 ? 12.069  3.696   28.012  1.00 91.72  ? 1144 GLY   A CA  1 
ATOM   681  C C   . GLY   A 1 107 ? 11.843  3.923   26.520  1.00 92.03  ? 1144 GLY   A C   1 
ATOM   682  O O   . GLY   A 1 107 ? 12.015  3.011   25.713  1.00 90.22  ? 1144 GLY   A O   1 
ATOM   683  N N   . ILE   A 1 108 ? 11.451  5.157   26.180  1.00 94.88  ? 1145 ILE   A N   1 
ATOM   684  C CA  . ILE   A 1 108 ? 11.260  5.576   24.801  1.00 96.23  ? 1145 ILE   A CA  1 
ATOM   685  C C   . ILE   A 1 108 ? 12.290  6.658   24.491  1.00 99.88  ? 1145 ILE   A C   1 
ATOM   686  O O   . ILE   A 1 108 ? 12.451  7.599   25.266  1.00 102.36 ? 1145 ILE   A O   1 
ATOM   687  C CB  . ILE   A 1 108 ? 9.818   6.072   24.567  1.00 96.76  ? 1145 ILE   A CB  1 
ATOM   688  C CG1 . ILE   A 1 108 ? 8.779   5.082   25.102  1.00 94.18  ? 1145 ILE   A CG1 1 
ATOM   689  C CG2 . ILE   A 1 108 ? 9.587   6.389   23.095  1.00 97.87  ? 1145 ILE   A CG2 1 
ATOM   690  C CD1 . ILE   A 1 108 ? 7.351   5.568   24.998  1.00 95.09  ? 1145 ILE   A CD1 1 
ATOM   691  N N   . CYS   A 1 109 ? 12.976  6.514   23.350  1.00 100.77 ? 1146 CYS   A N   1 
ATOM   692  C CA  . CYS   A 1 109 ? 14.027  7.437   22.954  1.00 104.32 ? 1146 CYS   A CA  1 
ATOM   693  C C   . CYS   A 1 109 ? 13.523  8.348   21.837  1.00 106.92 ? 1146 CYS   A C   1 
ATOM   694  O O   . CYS   A 1 109 ? 13.348  7.904   20.703  1.00 106.16 ? 1146 CYS   A O   1 
ATOM   695  C CB  . CYS   A 1 109 ? 15.270  6.681   22.498  1.00 103.84 ? 1146 CYS   A CB  1 
ATOM   696  S SG  . CYS   A 1 109 ? 16.667  7.765   22.105  1.00 108.17 ? 1146 CYS   A SG  1 
ATOM   697  N N   . LEU   A 1 110 ? 13.287  9.622   22.177  1.00 110.47 ? 1147 LEU   A N   1 
ATOM   698  C CA  . LEU   A 1 110 ? 12.881  10.629  21.209  1.00 113.83 ? 1147 LEU   A CA  1 
ATOM   699  C C   . LEU   A 1 110 ? 14.122  11.328  20.659  1.00 117.40 ? 1147 LEU   A C   1 
ATOM   700  O O   . LEU   A 1 110 ? 15.168  11.349  21.306  1.00 118.09 ? 1147 LEU   A O   1 
ATOM   701  C CB  . LEU   A 1 110 ? 11.940  11.639  21.878  1.00 115.85 ? 1147 LEU   A CB  1 
ATOM   702  C CG  . LEU   A 1 110 ? 10.528  11.146  22.198  1.00 113.67 ? 1147 LEU   A CG  1 
ATOM   703  C CD1 . LEU   A 1 110 ? 9.887   10.478  20.990  1.00 112.29 ? 1147 LEU   A CD1 1 
ATOM   704  C CD2 . LEU   A 1 110 ? 10.530  10.203  23.394  1.00 110.54 ? 1147 LEU   A CD2 1 
ATOM   705  N N   . ARG   A 1 111 ? 13.982  11.897  19.456  1.00 120.29 ? 1148 ARG   A N   1 
ATOM   706  C CA  . ARG   A 1 111 ? 15.063  12.604  18.787  1.00 124.07 ? 1148 ARG   A CA  1 
ATOM   707  C C   . ARG   A 1 111 ? 14.487  13.792  18.020  1.00 128.23 ? 1148 ARG   A C   1 
ATOM   708  O O   . ARG   A 1 111 ? 13.271  13.939  17.916  1.00 128.27 ? 1148 ARG   A O   1 
ATOM   709  C CB  . ARG   A 1 111 ? 15.812  11.659  17.840  1.00 122.75 ? 1148 ARG   A CB  1 
ATOM   710  C CG  . ARG   A 1 111 ? 16.531  10.509  18.531  1.00 119.71 ? 1148 ARG   A CG  1 
ATOM   711  C CD  . ARG   A 1 111 ? 17.251  9.604   17.547  1.00 118.80 ? 1148 ARG   A CD  1 
ATOM   712  N NE  . ARG   A 1 111 ? 16.334  8.912   16.650  1.00 116.96 ? 1148 ARG   A NE  1 
ATOM   713  C CZ  . ARG   A 1 111 ? 16.708  8.129   15.643  1.00 116.28 ? 1148 ARG   A CZ  1 
ATOM   714  N NH1 . ARG   A 1 111 ? 15.796  7.556   14.878  1.00 114.88 ? 1148 ARG   A NH1 1 
ATOM   715  N NH2 . ARG   A 1 111 ? 17.992  7.922   15.402  1.00 117.27 ? 1148 ARG   A NH2 1 
ATOM   716  N N   . SER   A 1 112 ? 15.381  14.636  17.490  1.00 132.23 ? 1149 SER   A N   1 
ATOM   717  C CA  . SER   A 1 112 ? 14.990  15.770  16.666  1.00 136.73 ? 1149 SER   A CA  1 
ATOM   718  C C   . SER   A 1 112 ? 14.471  15.285  15.313  1.00 136.50 ? 1149 SER   A C   1 
ATOM   719  O O   . SER   A 1 112 ? 13.573  15.899  14.740  1.00 139.01 ? 1149 SER   A O   1 
ATOM   720  C CB  . SER   A 1 112 ? 16.135  16.736  16.500  1.00 141.04 ? 1149 SER   A CB  1 
ATOM   721  O OG  . SER   A 1 112 ? 17.257  16.098  15.908  1.00 140.36 ? 1149 SER   A OG  1 
ATOM   722  N N   . GLU   A 1 113 ? 15.050  14.184  14.815  1.00 133.95 ? 1150 GLU   A N   1 
ATOM   723  C CA  . GLU   A 1 113 ? 14.643  13.584  13.553  1.00 133.60 ? 1150 GLU   A CA  1 
ATOM   724  C C   . GLU   A 1 113 ? 14.477  12.078  13.745  1.00 128.52 ? 1150 GLU   A C   1 
ATOM   725  O O   . GLU   A 1 113 ? 15.126  11.482  14.603  1.00 125.98 ? 1150 GLU   A O   1 
ATOM   726  C CB  . GLU   A 1 113 ? 15.652  13.903  12.444  1.00 136.85 ? 1150 GLU   A CB  1 
ATOM   727  C CG  . GLU   A 1 113 ? 16.979  13.162  12.551  1.00 135.20 ? 1150 GLU   A CG  1 
ATOM   728  C CD  . GLU   A 1 113 ? 17.865  13.564  13.718  1.00 135.68 ? 1150 GLU   A CD  1 
ATOM   729  O OE1 . GLU   A 1 113 ? 18.270  14.743  13.771  1.00 139.87 ? 1150 GLU   A OE1 1 
ATOM   730  O OE2 . GLU   A 1 113 ? 18.149  12.698  14.570  1.00 132.23 ? 1150 GLU   A OE2 1 
ATOM   731  N N   . GLY   A 1 114 ? 13.604  11.476  12.928  1.00 127.46 ? 1151 GLY   A N   1 
ATOM   732  C CA  . GLY   A 1 114 ? 13.332  10.049  12.989  1.00 123.00 ? 1151 GLY   A CA  1 
ATOM   733  C C   . GLY   A 1 114 ? 12.132  9.737   13.880  1.00 120.40 ? 1151 GLY   A C   1 
ATOM   734  O O   . GLY   A 1 114 ? 11.641  10.606  14.598  1.00 121.79 ? 1151 GLY   A O   1 
ATOM   735  N N   . SER   A 1 115 ? 11.678  8.480   13.820  1.00 116.85 ? 1152 SER   A N   1 
ATOM   736  C CA  . SER   A 1 115 ? 10.523  8.025   14.576  1.00 114.44 ? 1152 SER   A CA  1 
ATOM   737  C C   . SER   A 1 115 ? 10.931  7.707   16.014  1.00 111.71 ? 1152 SER   A C   1 
ATOM   738  O O   . SER   A 1 115 ? 12.120  7.638   16.316  1.00 111.28 ? 1152 SER   A O   1 
ATOM   739  C CB  . SER   A 1 115 ? 9.892   6.832   13.906  1.00 112.40 ? 1152 SER   A CB  1 
ATOM   740  O OG  . SER   A 1 115 ? 9.375   7.184   12.631  1.00 115.45 ? 1152 SER   A OG  1 
ATOM   741  N N   . PRO   A 1 116 ? 9.966   7.527   16.949  1.00 93.18  ? 1153 PRO   A N   1 
ATOM   742  C CA  . PRO   A 1 116 ? 10.280  7.114   18.319  1.00 90.69  ? 1153 PRO   A CA  1 
ATOM   743  C C   . PRO   A 1 116 ? 10.757  5.665   18.411  1.00 87.68  ? 1153 PRO   A C   1 
ATOM   744  O O   . PRO   A 1 116 ? 10.241  4.794   17.711  1.00 85.77  ? 1153 PRO   A O   1 
ATOM   745  C CB  . PRO   A 1 116 ? 8.952   7.276   19.082  1.00 88.37  ? 1153 PRO   A CB  1 
ATOM   746  C CG  . PRO   A 1 116 ? 8.073   8.110   18.168  1.00 90.73  ? 1153 PRO   A CG  1 
ATOM   747  C CD  . PRO   A 1 116 ? 8.527   7.769   16.765  1.00 92.31  ? 1153 PRO   A CD  1 
ATOM   748  N N   . LEU   A 1 117 ? 11.737  5.425   19.292  1.00 87.63  ? 1154 LEU   A N   1 
ATOM   749  C CA  . LEU   A 1 117 ? 12.301  4.101   19.506  1.00 85.45  ? 1154 LEU   A CA  1 
ATOM   750  C C   . LEU   A 1 117 ? 11.880  3.583   20.879  1.00 81.99  ? 1154 LEU   A C   1 
ATOM   751  O O   . LEU   A 1 117 ? 12.229  4.176   21.897  1.00 83.02  ? 1154 LEU   A O   1 
ATOM   752  C CB  . LEU   A 1 117 ? 13.828  4.178   19.399  1.00 88.91  ? 1154 LEU   A CB  1 
ATOM   753  C CG  . LEU   A 1 117 ? 14.399  4.152   17.981  1.00 91.81  ? 1154 LEU   A CG  1 
ATOM   754  C CD1 . LEU   A 1 117 ? 14.034  5.415   17.215  1.00 94.80  ? 1154 LEU   A CD1 1 
ATOM   755  C CD2 . LEU   A 1 117 ? 15.909  3.966   18.008  1.00 94.88  ? 1154 LEU   A CD2 1 
ATOM   756  N N   . VAL   A 1 118 ? 11.131  2.473   20.886  1.00 78.17  ? 1155 VAL   A N   1 
ATOM   757  C CA  . VAL   A 1 118 ? 10.749  1.791   22.112  1.00 75.07  ? 1155 VAL   A CA  1 
ATOM   758  C C   . VAL   A 1 118 ? 11.804  0.729   22.418  1.00 74.82  ? 1155 VAL   A C   1 
ATOM   759  O O   . VAL   A 1 118 ? 12.288  0.061   21.507  1.00 75.43  ? 1155 VAL   A O   1 
ATOM   760  C CB  . VAL   A 1 118 ? 9.341   1.175   21.990  1.00 71.76  ? 1155 VAL   A CB  1 
ATOM   761  C CG1 . VAL   A 1 118 ? 8.994   0.303   23.186  1.00 68.90  ? 1155 VAL   A CG1 1 
ATOM   762  C CG2 . VAL   A 1 118 ? 8.279   2.244   21.781  1.00 72.39  ? 1155 VAL   A CG2 1 
ATOM   763  N N   . VAL   A 1 119 ? 12.142  0.579   23.707  1.00 74.26  ? 1156 VAL   A N   1 
ATOM   764  C CA  . VAL   A 1 119 ? 13.201  -0.321  24.139  1.00 74.71  ? 1156 VAL   A CA  1 
ATOM   765  C C   . VAL   A 1 119 ? 12.657  -1.238  25.234  1.00 71.70  ? 1156 VAL   A C   1 
ATOM   766  O O   . VAL   A 1 119 ? 12.012  -0.769  26.169  1.00 70.62  ? 1156 VAL   A O   1 
ATOM   767  C CB  . VAL   A 1 119 ? 14.433  0.463   24.632  1.00 78.52  ? 1156 VAL   A CB  1 
ATOM   768  C CG1 . VAL   A 1 119 ? 15.586  -0.464  24.990  1.00 79.95  ? 1156 VAL   A CG1 1 
ATOM   769  C CG2 . VAL   A 1 119 ? 14.878  1.509   23.619  1.00 81.61  ? 1156 VAL   A CG2 1 
ATOM   770  N N   . LEU   A 1 120 ? 12.933  -2.543  25.103  1.00 70.60  ? 1157 LEU   A N   1 
ATOM   771  C CA  . LEU   A 1 120 ? 12.497  -3.540  26.070  1.00 68.28  ? 1157 LEU   A CA  1 
ATOM   772  C C   . LEU   A 1 120 ? 13.649  -4.499  26.368  1.00 69.83  ? 1157 LEU   A C   1 
ATOM   773  O O   . LEU   A 1 120 ? 14.582  -4.606  25.575  1.00 72.04  ? 1157 LEU   A O   1 
ATOM   774  C CB  . LEU   A 1 120 ? 11.292  -4.306  25.510  1.00 65.16  ? 1157 LEU   A CB  1 
ATOM   775  C CG  . LEU   A 1 120 ? 10.135  -3.451  24.992  1.00 63.96  ? 1157 LEU   A CG  1 
ATOM   776  C CD1 . LEU   A 1 120 ? 10.278  -3.183  23.500  1.00 65.13  ? 1157 LEU   A CD1 1 
ATOM   777  C CD2 . LEU   A 1 120 ? 8.797   -4.116  25.277  1.00 60.93  ? 1157 LEU   A CD2 1 
ATOM   778  N N   . PRO   A 1 121 ? 13.618  -5.235  27.506  1.00 69.00  ? 1158 PRO   A N   1 
ATOM   779  C CA  . PRO   A 1 121 ? 14.661  -6.211  27.826  1.00 70.93  ? 1158 PRO   A CA  1 
ATOM   780  C C   . PRO   A 1 121 ? 14.662  -7.384  26.849  1.00 70.08  ? 1158 PRO   A C   1 
ATOM   781  O O   . PRO   A 1 121 ? 13.601  -7.886  26.483  1.00 67.20  ? 1158 PRO   A O   1 
ATOM   782  C CB  . PRO   A 1 121 ? 14.313  -6.704  29.242  1.00 70.17  ? 1158 PRO   A CB  1 
ATOM   783  C CG  . PRO   A 1 121 ? 13.309  -5.697  29.773  1.00 68.39  ? 1158 PRO   A CG  1 
ATOM   784  C CD  . PRO   A 1 121 ? 12.586  -5.168  28.552  1.00 66.68  ? 1158 PRO   A CD  1 
ATOM   785  N N   . TYR   A 1 122 ? 15.862  -7.820  26.446  1.00 72.95  ? 1159 TYR   A N   1 
ATOM   786  C CA  . TYR   A 1 122 ? 16.007  -8.857  25.437  1.00 73.03  ? 1159 TYR   A CA  1 
ATOM   787  C C   . TYR   A 1 122 ? 15.430  -10.173 25.953  1.00 71.04  ? 1159 TYR   A C   1 
ATOM   788  O O   . TYR   A 1 122 ? 15.929  -10.733 26.927  1.00 72.72  ? 1159 TYR   A O   1 
ATOM   789  C CB  . TYR   A 1 122 ? 17.476  -9.031  25.041  1.00 77.44  ? 1159 TYR   A CB  1 
ATOM   790  C CG  . TYR   A 1 122 ? 17.705  -10.049 23.952  1.00 78.37  ? 1159 TYR   A CG  1 
ATOM   791  C CD1 . TYR   A 1 122 ? 17.192  -9.857  22.679  1.00 77.27  ? 1159 TYR   A CD1 1 
ATOM   792  C CD2 . TYR   A 1 122 ? 18.414  -11.215 24.196  1.00 80.71  ? 1159 TYR   A CD2 1 
ATOM   793  C CE1 . TYR   A 1 122 ? 17.389  -10.788 21.672  1.00 78.49  ? 1159 TYR   A CE1 1 
ATOM   794  C CE2 . TYR   A 1 122 ? 18.621  -12.156 23.200  1.00 81.94  ? 1159 TYR   A CE2 1 
ATOM   795  C CZ  . TYR   A 1 122 ? 18.106  -11.943 21.933  1.00 80.79  ? 1159 TYR   A CZ  1 
ATOM   796  O OH  . TYR   A 1 122 ? 18.302  -12.869 20.937  1.00 82.37  ? 1159 TYR   A OH  1 
ATOM   797  N N   . MET   A 1 123 ? 14.374  -10.650 25.283  1.00 67.83  ? 1160 MET   A N   1 
ATOM   798  C CA  . MET   A 1 123 ? 13.732  -11.911 25.613  1.00 65.94  ? 1160 MET   A CA  1 
ATOM   799  C C   . MET   A 1 123 ? 14.334  -13.016 24.746  1.00 67.79  ? 1160 MET   A C   1 
ATOM   800  O O   . MET   A 1 123 ? 13.970  -13.163 23.582  1.00 67.33  ? 1160 MET   A O   1 
ATOM   801  C CB  . MET   A 1 123 ? 12.222  -11.818 25.369  1.00 62.19  ? 1160 MET   A CB  1 
ATOM   802  C CG  . MET   A 1 123 ? 11.508  -10.900 26.347  1.00 60.33  ? 1160 MET   A CG  1 
ATOM   803  S SD  . MET   A 1 123 ? 11.545  -11.504 28.055  1.00 60.40  ? 1160 MET   A SD  1 
ATOM   804  C CE  . MET   A 1 123 ? 12.873  -10.513 28.736  1.00 63.70  ? 1160 MET   A CE  1 
ATOM   805  N N   . LYS   A 1 124 ? 15.246  -13.796 25.341  1.00 70.30  ? 1161 LYS   A N   1 
ATOM   806  C CA  . LYS   A 1 124 ? 16.112  -14.709 24.610  1.00 73.26  ? 1161 LYS   A CA  1 
ATOM   807  C C   . LYS   A 1 124 ? 15.307  -15.578 23.645  1.00 71.61  ? 1161 LYS   A C   1 
ATOM   808  O O   . LYS   A 1 124 ? 15.522  -15.520 22.436  1.00 72.62  ? 1161 LYS   A O   1 
ATOM   809  C CB  . LYS   A 1 124 ? 16.897  -15.588 25.591  1.00 76.16  ? 1161 LYS   A CB  1 
ATOM   810  C CG  . LYS   A 1 124 ? 17.906  -16.535 24.954  1.00 80.29  ? 1161 LYS   A CG  1 
ATOM   811  C CD  . LYS   A 1 124 ? 18.608  -17.433 25.951  1.00 83.52  ? 1161 LYS   A CD  1 
ATOM   812  C CE  . LYS   A 1 124 ? 19.550  -18.419 25.295  1.00 87.96  ? 1161 LYS   A CE  1 
ATOM   813  N NZ  . LYS   A 1 124 ? 20.171  -19.326 26.289  1.00 91.50  ? 1161 LYS   A NZ  1 
ATOM   814  N N   . HIS   A 1 125 ? 14.374  -16.370 24.189  1.00 69.24  ? 1162 HIS   A N   1 
ATOM   815  C CA  . HIS   A 1 125 ? 13.743  -17.452 23.447  1.00 68.56  ? 1162 HIS   A CA  1 
ATOM   816  C C   . HIS   A 1 125 ? 12.548  -16.964 22.624  1.00 65.28  ? 1162 HIS   A C   1 
ATOM   817  O O   . HIS   A 1 125 ? 11.820  -17.779 22.061  1.00 64.67  ? 1162 HIS   A O   1 
ATOM   818  C CB  . HIS   A 1 125 ? 13.336  -18.578 24.407  1.00 68.29  ? 1162 HIS   A CB  1 
ATOM   819  C CG  . HIS   A 1 125 ? 14.485  -19.308 25.035  1.00 72.18  ? 1162 HIS   A CG  1 
ATOM   820  N ND1 . HIS   A 1 125 ? 15.552  -19.800 24.325  1.00 76.10  ? 1162 HIS   A ND1 1 
ATOM   821  C CD2 . HIS   A 1 125 ? 14.709  -19.609 26.346  1.00 73.13  ? 1162 HIS   A CD2 1 
ATOM   822  C CE1 . HIS   A 1 125 ? 16.403  -20.388 25.164  1.00 79.42  ? 1162 HIS   A CE1 1 
ATOM   823  N NE2 . HIS   A 1 125 ? 15.898  -20.282 26.425  1.00 77.67  ? 1162 HIS   A NE2 1 
ATOM   824  N N   . GLY   A 1 126 ? 12.347  -15.642 22.551  1.00 63.51  ? 1163 GLY   A N   1 
ATOM   825  C CA  . GLY   A 1 126 ? 11.374  -15.064 21.638  1.00 61.21  ? 1163 GLY   A CA  1 
ATOM   826  C C   . GLY   A 1 126 ? 9.938   -15.293 22.102  1.00 57.72  ? 1163 GLY   A C   1 
ATOM   827  O O   . GLY   A 1 126 ? 9.688   -15.463 23.293  1.00 56.49  ? 1163 GLY   A O   1 
ATOM   828  N N   . ASP   A 1 127 ? 9.005   -15.305 21.140  1.00 56.49  ? 1164 ASP   A N   1 
ATOM   829  C CA  . ASP   A 1 127 ? 7.583   -15.367 21.437  1.00 53.64  ? 1164 ASP   A CA  1 
ATOM   830  C C   . ASP   A 1 127 ? 7.191   -16.798 21.800  1.00 53.40  ? 1164 ASP   A C   1 
ATOM   831  O O   . ASP   A 1 127 ? 7.878   -17.750 21.438  1.00 55.54  ? 1164 ASP   A O   1 
ATOM   832  C CB  . ASP   A 1 127 ? 6.740   -14.823 20.278  1.00 53.18  ? 1164 ASP   A CB  1 
ATOM   833  C CG  . ASP   A 1 127 ? 6.757   -15.683 19.025  1.00 55.02  ? 1164 ASP   A CG  1 
ATOM   834  O OD1 . ASP   A 1 127 ? 7.856   -15.904 18.481  1.00 57.55  ? 1164 ASP   A OD1 1 
ATOM   835  O OD2 . ASP   A 1 127 ? 5.668   -16.118 18.600  1.00 54.26  ? 1164 ASP   A OD2 1 
ATOM   836  N N   . LEU   A 1 128 ? 6.064   -16.921 22.511  1.00 51.14  ? 1165 LEU   A N   1 
ATOM   837  C CA  . LEU   A 1 128 ? 5.606   -18.186 23.063  1.00 51.20  ? 1165 LEU   A CA  1 
ATOM   838  C C   . LEU   A 1 128 ? 5.002   -19.060 21.965  1.00 51.98  ? 1165 LEU   A C   1 
ATOM   839  O O   . LEU   A 1 128 ? 5.099   -20.283 22.031  1.00 53.19  ? 1165 LEU   A O   1 
ATOM   840  C CB  . LEU   A 1 128 ? 4.584   -17.889 24.169  1.00 48.92  ? 1165 LEU   A CB  1 
ATOM   841  C CG  . LEU   A 1 128 ? 3.935   -19.101 24.839  1.00 48.90  ? 1165 LEU   A CG  1 
ATOM   842  C CD1 . LEU   A 1 128 ? 4.934   -19.845 25.713  1.00 50.77  ? 1165 LEU   A CD1 1 
ATOM   843  C CD2 . LEU   A 1 128 ? 2.720   -18.679 25.655  1.00 46.72  ? 1165 LEU   A CD2 1 
ATOM   844  N N   . ARG   A 1 129 ? 4.384   -18.425 20.961  1.00 51.68  ? 1166 ARG   A N   1 
ATOM   845  C CA  . ARG   A 1 129 ? 3.663   -19.138 19.917  1.00 52.76  ? 1166 ARG   A CA  1 
ATOM   846  C C   . ARG   A 1 129 ? 4.647   -19.976 19.102  1.00 55.96  ? 1166 ARG   A C   1 
ATOM   847  O O   . ARG   A 1 129 ? 4.432   -21.171 18.912  1.00 57.36  ? 1166 ARG   A O   1 
ATOM   848  C CB  . ARG   A 1 129 ? 2.896   -18.149 19.031  1.00 52.22  ? 1166 ARG   A CB  1 
ATOM   849  C CG  . ARG   A 1 129 ? 1.631   -18.713 18.395  1.00 52.45  ? 1166 ARG   A CG  1 
ATOM   850  C CD  . ARG   A 1 129 ? 1.870   -19.724 17.289  1.00 55.20  ? 1166 ARG   A CD  1 
ATOM   851  N NE  . ARG   A 1 129 ? 2.564   -19.153 16.140  1.00 57.12  ? 1166 ARG   A NE  1 
ATOM   852  C CZ  . ARG   A 1 129 ? 2.111   -19.174 14.889  1.00 59.02  ? 1166 ARG   A CZ  1 
ATOM   853  N NH1 . ARG   A 1 129 ? 2.791   -18.568 13.933  1.00 60.96  ? 1166 ARG   A NH1 1 
ATOM   854  N NH2 . ARG   A 1 129 ? 0.984   -19.800 14.596  1.00 59.38  ? 1166 ARG   A NH2 1 
ATOM   855  N N   . ASN   A 1 130 ? 5.732   -19.343 18.641  1.00 57.56  ? 1167 ASN   A N   1 
ATOM   856  C CA  . ASN   A 1 130 ? 6.735   -20.016 17.830  1.00 61.02  ? 1167 ASN   A CA  1 
ATOM   857  C C   . ASN   A 1 130 ? 7.536   -21.000 18.681  1.00 62.72  ? 1167 ASN   A C   1 
ATOM   858  O O   . ASN   A 1 130 ? 8.043   -21.989 18.157  1.00 65.70  ? 1167 ASN   A O   1 
ATOM   859  C CB  . ASN   A 1 130 ? 7.672   -19.023 17.137  1.00 62.39  ? 1167 ASN   A CB  1 
ATOM   860  C CG  . ASN   A 1 130 ? 7.008   -18.277 15.999  1.00 62.35  ? 1167 ASN   A CG  1 
ATOM   861  O OD1 . ASN   A 1 130 ? 7.424   -18.396 14.849  1.00 65.02  ? 1167 ASN   A OD1 1 
ATOM   862  N ND2 . ASN   A 1 130 ? 5.974   -17.511 16.305  1.00 59.81  ? 1167 ASN   A ND2 1 
ATOM   863  N N   . PHE   A 1 131 ? 7.649   -20.719 19.986  1.00 61.41  ? 1168 PHE   A N   1 
ATOM   864  C CA  . PHE   A 1 131 ? 8.433   -21.540 20.896  1.00 63.33  ? 1168 PHE   A CA  1 
ATOM   865  C C   . PHE   A 1 131 ? 7.811   -22.929 21.031  1.00 64.37  ? 1168 PHE   A C   1 
ATOM   866  O O   . PHE   A 1 131 ? 8.518   -23.931 20.940  1.00 67.55  ? 1168 PHE   A O   1 
ATOM   867  C CB  . PHE   A 1 131 ? 8.565   -20.843 22.254  1.00 61.62  ? 1168 PHE   A CB  1 
ATOM   868  C CG  . PHE   A 1 131 ? 9.440   -21.555 23.256  1.00 63.83  ? 1168 PHE   A CG  1 
ATOM   869  C CD1 . PHE   A 1 131 ? 10.748  -21.146 23.468  1.00 66.08  ? 1168 PHE   A CD1 1 
ATOM   870  C CD2 . PHE   A 1 131 ? 8.950   -22.612 24.010  1.00 64.11  ? 1168 PHE   A CD2 1 
ATOM   871  C CE1 . PHE   A 1 131 ? 11.553  -21.793 24.393  1.00 68.62  ? 1168 PHE   A CE1 1 
ATOM   872  C CE2 . PHE   A 1 131 ? 9.757   -23.257 24.935  1.00 66.58  ? 1168 PHE   A CE2 1 
ATOM   873  C CZ  . PHE   A 1 131 ? 11.056  -22.846 25.126  1.00 68.87  ? 1168 PHE   A CZ  1 
ATOM   874  N N   . ILE   A 1 132 ? 6.492   -22.977 21.259  1.00 62.18  ? 1169 ILE   A N   1 
ATOM   875  C CA  . ILE   A 1 132 ? 5.784   -24.236 21.440  1.00 63.14  ? 1169 ILE   A CA  1 
ATOM   876  C C   . ILE   A 1 132 ? 5.652   -24.958 20.098  1.00 65.73  ? 1169 ILE   A C   1 
ATOM   877  O O   . ILE   A 1 132 ? 5.649   -26.186 20.060  1.00 68.16  ? 1169 ILE   A O   1 
ATOM   878  C CB  . ILE   A 1 132 ? 4.415   -24.022 22.122  1.00 60.15  ? 1169 ILE   A CB  1 
ATOM   879  C CG1 . ILE   A 1 132 ? 3.450   -23.196 21.266  1.00 58.35  ? 1169 ILE   A CG1 1 
ATOM   880  C CG2 . ILE   A 1 132 ? 4.597   -23.419 23.508  1.00 58.51  ? 1169 ILE   A CG2 1 
ATOM   881  C CD1 . ILE   A 1 132 ? 2.095   -22.979 21.899  1.00 55.95  ? 1169 ILE   A CD1 1 
ATOM   882  N N   . ARG   A 1 133 ? 5.536   -24.189 19.006  1.00 65.75  ? 1170 ARG   A N   1 
ATOM   883  C CA  . ARG   A 1 133 ? 5.458   -24.752 17.666  1.00 68.54  ? 1170 ARG   A CA  1 
ATOM   884  C C   . ARG   A 1 133 ? 6.811   -25.326 17.250  1.00 72.55  ? 1170 ARG   A C   1 
ATOM   885  O O   . ARG   A 1 133 ? 6.860   -26.306 16.510  1.00 75.61  ? 1170 ARG   A O   1 
ATOM   886  C CB  . ARG   A 1 133 ? 5.014   -23.696 16.649  1.00 67.64  ? 1170 ARG   A CB  1 
ATOM   887  C CG  . ARG   A 1 133 ? 3.532   -23.357 16.699  1.00 65.20  ? 1170 ARG   A CG  1 
ATOM   888  C CD  . ARG   A 1 133 ? 3.145   -22.381 15.605  1.00 65.22  ? 1170 ARG   A CD  1 
ATOM   889  N NE  . ARG   A 1 133 ? 3.267   -22.976 14.280  1.00 68.61  ? 1170 ARG   A NE  1 
ATOM   890  C CZ  . ARG   A 1 133 ? 4.181   -22.638 13.375  1.00 70.97  ? 1170 ARG   A CZ  1 
ATOM   891  N NH1 . ARG   A 1 133 ? 4.168   -23.206 12.182  1.00 74.27  ? 1170 ARG   A NH1 1 
ATOM   892  N NH2 . ARG   A 1 133 ? 5.106   -21.738 13.662  1.00 70.32  ? 1170 ARG   A NH2 1 
ATOM   893  N N   . ASN   A 1 134 ? 7.900   -24.695 17.714  1.00 73.09  ? 1171 ASN   A N   1 
ATOM   894  C CA  . ASN   A 1 134 ? 9.249   -25.115 17.367  1.00 77.30  ? 1171 ASN   A CA  1 
ATOM   895  C C   . ASN   A 1 134 ? 9.400   -26.604 17.672  1.00 80.65  ? 1171 ASN   A C   1 
ATOM   896  O O   . ASN   A 1 134 ? 9.268   -27.021 18.821  1.00 80.02  ? 1171 ASN   A O   1 
ATOM   897  C CB  . ASN   A 1 134 ? 10.307  -24.280 18.097  1.00 76.96  ? 1171 ASN   A CB  1 
ATOM   898  C CG  . ASN   A 1 134 ? 11.705  -24.456 17.543  1.00 81.08  ? 1171 ASN   A CG  1 
ATOM   899  O OD1 . ASN   A 1 134 ? 11.918  -25.196 16.584  1.00 84.19  ? 1171 ASN   A OD1 1 
ATOM   900  N ND2 . ASN   A 1 134 ? 12.668  -23.772 18.138  1.00 81.48  ? 1171 ASN   A ND2 1 
ATOM   901  N N   . GLU   A 1 135 ? 9.673   -27.390 16.623  1.00 84.79  ? 1172 GLU   A N   1 
ATOM   902  C CA  . GLU   A 1 135 ? 9.679   -28.843 16.706  1.00 88.43  ? 1172 GLU   A CA  1 
ATOM   903  C C   . GLU   A 1 135 ? 10.910  -29.336 17.468  1.00 91.58  ? 1172 GLU   A C   1 
ATOM   904  O O   . GLU   A 1 135 ? 10.879  -30.423 18.043  1.00 93.57  ? 1172 GLU   A O   1 
ATOM   905  C CB  . GLU   A 1 135 ? 9.594   -29.468 15.309  1.00 92.12  ? 1172 GLU   A CB  1 
ATOM   906  C CG  . GLU   A 1 135 ? 10.818  -29.255 14.426  1.00 95.99  ? 1172 GLU   A CG  1 
ATOM   907  C CD  . GLU   A 1 135 ? 11.013  -27.847 13.887  1.00 94.19  ? 1172 GLU   A CD  1 
ATOM   908  O OE1 . GLU   A 1 135 ? 12.125  -27.302 14.046  1.00 95.44  ? 1172 GLU   A OE1 1 
ATOM   909  O OE2 . GLU   A 1 135 ? 10.050  -27.293 13.318  1.00 91.97  ? 1172 GLU   A OE2 1 
ATOM   910  N N   . THR   A 1 136 ? 11.990  -28.542 17.463  1.00 92.41  ? 1173 THR   A N   1 
ATOM   911  C CA  . THR   A 1 136 ? 13.212  -28.891 18.171  1.00 95.72  ? 1173 THR   A CA  1 
ATOM   912  C C   . THR   A 1 136 ? 12.946  -28.927 19.675  1.00 93.72  ? 1173 THR   A C   1 
ATOM   913  O O   . THR   A 1 136 ? 13.321  -29.885 20.348  1.00 96.52  ? 1173 THR   A O   1 
ATOM   914  C CB  . THR   A 1 136 ? 14.353  -27.926 17.823  1.00 96.89  ? 1173 THR   A CB  1 
ATOM   915  O OG1 . THR   A 1 136 ? 13.940  -26.600 18.156  1.00 92.29  ? 1173 THR   A OG1 1 
ATOM   916  C CG2 . THR   A 1 136 ? 14.749  -27.984 16.363  1.00 99.89  ? 1173 THR   A CG2 1 
ATOM   917  N N   . HIS   A 1 137 ? 12.299  -27.872 20.188  1.00 89.24  ? 1174 HIS   A N   1 
ATOM   918  C CA  . HIS   A 1 137 ? 11.870  -27.825 21.577  1.00 87.02  ? 1174 HIS   A CA  1 
ATOM   919  C C   . HIS   A 1 137 ? 10.755  -28.845 21.799  1.00 86.25  ? 1174 HIS   A C   1 
ATOM   920  O O   . HIS   A 1 137 ? 9.917   -29.051 20.921  1.00 85.39  ? 1174 HIS   A O   1 
ATOM   921  C CB  . HIS   A 1 137 ? 11.405  -26.411 21.955  1.00 82.74  ? 1174 HIS   A CB  1 
ATOM   922  C CG  . HIS   A 1 137 ? 12.461  -25.349 21.869  1.00 83.55  ? 1174 HIS   A CG  1 
ATOM   923  N ND1 . HIS   A 1 137 ? 12.321  -24.193 21.142  1.00 81.57  ? 1174 HIS   A ND1 1 
ATOM   924  C CD2 . HIS   A 1 137 ? 13.687  -25.297 22.464  1.00 86.57  ? 1174 HIS   A CD2 1 
ATOM   925  C CE1 . HIS   A 1 137 ? 13.422  -23.456 21.274  1.00 83.07  ? 1174 HIS   A CE1 1 
ATOM   926  N NE2 . HIS   A 1 137 ? 14.285  -24.124 22.091  1.00 86.23  ? 1174 HIS   A NE2 1 
ATOM   927  N N   . ASN   A 1 138 ? 10.757  -29.477 22.979  1.00 86.85  ? 1175 ASN   A N   1 
ATOM   928  C CA  . ASN   A 1 138 ? 9.760   -30.477 23.324  1.00 86.68  ? 1175 ASN   A CA  1 
ATOM   929  C C   . ASN   A 1 138 ? 9.357   -30.295 24.786  1.00 84.48  ? 1175 ASN   A C   1 
ATOM   930  O O   . ASN   A 1 138 ? 9.736   -31.092 25.643  1.00 87.38  ? 1175 ASN   A O   1 
ATOM   931  C CB  . ASN   A 1 138 ? 10.266  -31.893 23.030  1.00 92.01  ? 1175 ASN   A CB  1 
ATOM   932  C CG  . ASN   A 1 138 ? 9.220   -32.959 23.278  1.00 92.56  ? 1175 ASN   A CG  1 
ATOM   933  O OD1 . ASN   A 1 138 ? 8.119   -32.893 22.737  1.00 90.23  ? 1175 ASN   A OD1 1 
ATOM   934  N ND2 . ASN   A 1 138 ? 9.550   -33.939 24.104  1.00 95.98  ? 1175 ASN   A ND2 1 
ATOM   935  N N   . PRO   A 1 139 ? 8.584   -29.234 25.119  1.00 79.59  ? 1176 PRO   A N   1 
ATOM   936  C CA  . PRO   A 1 139 ? 8.100   -29.029 26.484  1.00 77.37  ? 1176 PRO   A CA  1 
ATOM   937  C C   . PRO   A 1 139 ? 6.927   -29.949 26.809  1.00 76.63  ? 1176 PRO   A C   1 
ATOM   938  O O   . PRO   A 1 139 ? 6.044   -30.149 25.977  1.00 75.42  ? 1176 PRO   A O   1 
ATOM   939  C CB  . PRO   A 1 139 ? 7.670   -27.555 26.481  1.00 73.18  ? 1176 PRO   A CB  1 
ATOM   940  C CG  . PRO   A 1 139 ? 7.228   -27.307 25.054  1.00 72.18  ? 1176 PRO   A CG  1 
ATOM   941  C CD  . PRO   A 1 139 ? 8.135   -28.173 24.202  1.00 76.38  ? 1176 PRO   A CD  1 
ATOM   942  N N   . THR   A 1 140 ? 6.930   -30.500 28.029  1.00 77.45  ? 1177 THR   A N   1 
ATOM   943  C CA  . THR   A 1 140 ? 5.884   -31.405 28.475  1.00 77.39  ? 1177 THR   A CA  1 
ATOM   944  C C   . THR   A 1 140 ? 4.588   -30.623 28.672  1.00 72.46  ? 1177 THR   A C   1 
ATOM   945  O O   . THR   A 1 140 ? 4.582   -29.396 28.608  1.00 69.17  ? 1177 THR   A O   1 
ATOM   946  C CB  . THR   A 1 140 ? 6.306   -32.145 29.752  1.00 80.62  ? 1177 THR   A CB  1 
ATOM   947  O OG1 . THR   A 1 140 ? 6.558   -31.178 30.772  1.00 78.89  ? 1177 THR   A OG1 1 
ATOM   948  C CG2 . THR   A 1 140 ? 7.535   -33.006 29.555  1.00 85.68  ? 1177 THR   A CG2 1 
ATOM   949  N N   . VAL   A 1 141 ? 3.492   -31.351 28.914  1.00 72.19  ? 1178 VAL   A N   1 
ATOM   950  C CA  . VAL   A 1 141 ? 2.186   -30.743 29.122  1.00 68.43  ? 1178 VAL   A CA  1 
ATOM   951  C C   . VAL   A 1 141 ? 2.229   -29.886 30.387  1.00 66.50  ? 1178 VAL   A C   1 
ATOM   952  O O   . VAL   A 1 141 ? 1.587   -28.840 30.448  1.00 63.10  ? 1178 VAL   A O   1 
ATOM   953  C CB  . VAL   A 1 141 ? 1.074   -31.809 29.193  1.00 69.67  ? 1178 VAL   A CB  1 
ATOM   954  C CG1 . VAL   A 1 141 ? -0.285  -31.193 29.497  1.00 66.51  ? 1178 VAL   A CG1 1 
ATOM   955  C CG2 . VAL   A 1 141 ? 1.011   -32.644 27.922  1.00 71.78  ? 1178 VAL   A CG2 1 
ATOM   956  N N   . LYS   A 1 142 ? 2.996   -30.339 31.388  1.00 68.95  ? 1179 LYS   A N   1 
ATOM   957  C CA  . LYS   A 1 142 ? 3.166   -29.616 32.640  1.00 67.85  ? 1179 LYS   A CA  1 
ATOM   958  C C   . LYS   A 1 142 ? 3.847   -28.272 32.381  1.00 65.43  ? 1179 LYS   A C   1 
ATOM   959  O O   . LYS   A 1 142 ? 3.506   -27.277 33.016  1.00 63.10  ? 1179 LYS   A O   1 
ATOM   960  C CB  . LYS   A 1 142 ? 3.976   -30.464 33.627  1.00 71.98  ? 1179 LYS   A CB  1 
ATOM   961  C CG  . LYS   A 1 142 ? 4.014   -29.946 35.059  1.00 72.07  ? 1179 LYS   A CG  1 
ATOM   962  C CD  . LYS   A 1 142 ? 4.720   -30.889 36.011  1.00 76.86  ? 1179 LYS   A CD  1 
ATOM   963  C CE  . LYS   A 1 142 ? 4.646   -30.456 37.461  1.00 77.40  ? 1179 LYS   A CE  1 
ATOM   964  N NZ  . LYS   A 1 142 ? 5.382   -29.192 37.709  1.00 76.09  ? 1179 LYS   A NZ  1 
ATOM   965  N N   . ASP   A 1 143 ? 4.812   -28.256 31.451  1.00 66.24  ? 1180 ASP   A N   1 
ATOM   966  C CA  . ASP   A 1 143 ? 5.482   -27.029 31.047  1.00 64.32  ? 1180 ASP   A CA  1 
ATOM   967  C C   . ASP   A 1 143 ? 4.480   -26.093 30.374  1.00 60.11  ? 1180 ASP   A C   1 
ATOM   968  O O   . ASP   A 1 143 ? 4.466   -24.897 30.657  1.00 57.90  ? 1180 ASP   A O   1 
ATOM   969  C CB  . ASP   A 1 143 ? 6.659   -27.302 30.105  1.00 66.79  ? 1180 ASP   A CB  1 
ATOM   970  C CG  . ASP   A 1 143 ? 7.791   -28.098 30.731  1.00 71.29  ? 1180 ASP   A CG  1 
ATOM   971  O OD1 . ASP   A 1 143 ? 8.309   -27.658 31.776  1.00 72.09  ? 1180 ASP   A OD1 1 
ATOM   972  O OD2 . ASP   A 1 143 ? 8.156   -29.144 30.158  1.00 74.38  ? 1180 ASP   A OD2 1 
ATOM   973  N N   . LEU   A 1 144 ? 3.648   -26.657 29.488  1.00 59.34  ? 1181 LEU   A N   1 
ATOM   974  C CA  . LEU   A 1 144 ? 2.670   -25.892 28.727  1.00 56.07  ? 1181 LEU   A CA  1 
ATOM   975  C C   . LEU   A 1 144 ? 1.628   -25.281 29.663  1.00 53.54  ? 1181 LEU   A C   1 
ATOM   976  O O   . LEU   A 1 144 ? 1.225   -24.135 29.470  1.00 51.08  ? 1181 LEU   A O   1 
ATOM   977  C CB  . LEU   A 1 144 ? 2.014   -26.812 27.691  1.00 56.96  ? 1181 LEU   A CB  1 
ATOM   978  C CG  . LEU   A 1 144 ? 2.932   -27.308 26.574  1.00 59.24  ? 1181 LEU   A CG  1 
ATOM   979  C CD1 . LEU   A 1 144 ? 2.223   -28.336 25.704  1.00 60.75  ? 1181 LEU   A CD1 1 
ATOM   980  C CD2 . LEU   A 1 144 ? 3.435   -26.150 25.725  1.00 57.74  ? 1181 LEU   A CD2 1 
ATOM   981  N N   . ILE   A 1 145 ? 1.198   -26.055 30.669  1.00 54.36  ? 1182 ILE   A N   1 
ATOM   982  C CA  . ILE   A 1 145 ? 0.296   -25.563 31.701  1.00 52.48  ? 1182 ILE   A CA  1 
ATOM   983  C C   . ILE   A 1 145 ? 1.037   -24.547 32.571  1.00 51.60  ? 1182 ILE   A C   1 
ATOM   984  O O   . ILE   A 1 145 ? 0.437   -23.587 33.050  1.00 49.49  ? 1182 ILE   A O   1 
ATOM   985  C CB  . ILE   A 1 145 ? -0.285  -26.730 32.529  1.00 54.46  ? 1182 ILE   A CB  1 
ATOM   986  C CG1 . ILE   A 1 145 ? -1.178  -27.636 31.675  1.00 55.02  ? 1182 ILE   A CG1 1 
ATOM   987  C CG2 . ILE   A 1 145 ? -1.025  -26.214 33.755  1.00 53.59  ? 1182 ILE   A CG2 1 
ATOM   988  C CD1 . ILE   A 1 145 ? -1.592  -28.921 32.355  1.00 57.69  ? 1182 ILE   A CD1 1 
ATOM   989  N N   . GLY   A 1 146 ? 2.341   -24.776 32.773  1.00 53.44  ? 1183 GLY   A N   1 
ATOM   990  C CA  . GLY   A 1 146 ? 3.203   -23.829 33.461  1.00 53.35  ? 1183 GLY   A CA  1 
ATOM   991  C C   . GLY   A 1 146 ? 3.264   -22.478 32.751  1.00 50.68  ? 1183 GLY   A C   1 
ATOM   992  O O   . GLY   A 1 146 ? 3.196   -21.436 33.399  1.00 49.42  ? 1183 GLY   A O   1 
ATOM   993  N N   . PHE   A 1 147 ? 3.387   -22.511 31.418  1.00 49.99  ? 1184 PHE   A N   1 
ATOM   994  C CA  . PHE   A 1 147 ? 3.458   -21.300 30.613  1.00 48.00  ? 1184 PHE   A CA  1 
ATOM   995  C C   . PHE   A 1 147 ? 2.110   -20.581 30.619  1.00 45.25  ? 1184 PHE   A C   1 
ATOM   996  O O   . PHE   A 1 147 ? 2.066   -19.353 30.592  1.00 43.88  ? 1184 PHE   A O   1 
ATOM   997  C CB  . PHE   A 1 147 ? 3.891   -21.618 29.178  1.00 48.74  ? 1184 PHE   A CB  1 
ATOM   998  C CG  . PHE   A 1 147 ? 5.242   -22.276 29.043  1.00 51.87  ? 1184 PHE   A CG  1 
ATOM   999  C CD1 . PHE   A 1 147 ? 6.333   -21.832 29.777  1.00 53.34  ? 1184 PHE   A CD1 1 
ATOM   1000 C CD2 . PHE   A 1 147 ? 5.431   -23.329 28.159  1.00 53.77  ? 1184 PHE   A CD2 1 
ATOM   1001 C CE1 . PHE   A 1 147 ? 7.573   -22.439 29.645  1.00 56.60  ? 1184 PHE   A CE1 1 
ATOM   1002 C CE2 . PHE   A 1 147 ? 6.672   -23.934 28.028  1.00 56.98  ? 1184 PHE   A CE2 1 
ATOM   1003 C CZ  . PHE   A 1 147 ? 7.741   -23.488 28.770  1.00 58.42  ? 1184 PHE   A CZ  1 
ATOM   1004 N N   . GLY   A 1 148 ? 1.019   -21.357 30.644  1.00 44.85  ? 1185 GLY   A N   1 
ATOM   1005 C CA  . GLY   A 1 148 ? -0.327  -20.806 30.681  1.00 42.87  ? 1185 GLY   A CA  1 
ATOM   1006 C C   . GLY   A 1 148 ? -0.635  -20.111 32.006  1.00 42.28  ? 1185 GLY   A C   1 
ATOM   1007 O O   . GLY   A 1 148 ? -1.312  -19.085 32.024  1.00 40.69  ? 1185 GLY   A O   1 
ATOM   1008 N N   . LEU   A 1 149 ? -0.131  -20.685 33.107  1.00 43.91  ? 1186 LEU   A N   1 
ATOM   1009 C CA  . LEU   A 1 149 ? -0.356  -20.154 34.443  1.00 43.98  ? 1186 LEU   A CA  1 
ATOM   1010 C C   . LEU   A 1 149 ? 0.331   -18.798 34.594  1.00 43.17  ? 1186 LEU   A C   1 
ATOM   1011 O O   . LEU   A 1 149 ? -0.245  -17.874 35.164  1.00 42.34  ? 1186 LEU   A O   1 
ATOM   1012 C CB  . LEU   A 1 149 ? 0.173   -21.158 35.474  1.00 46.59  ? 1186 LEU   A CB  1 
ATOM   1013 C CG  . LEU   A 1 149 ? 0.125   -20.704 36.933  1.00 47.60  ? 1186 LEU   A CG  1 
ATOM   1014 C CD1 . LEU   A 1 149 ? -1.310  -20.550 37.414  1.00 46.69  ? 1186 LEU   A CD1 1 
ATOM   1015 C CD2 . LEU   A 1 149 ? 0.884   -21.676 37.824  1.00 50.72  ? 1186 LEU   A CD2 1 
ATOM   1016 N N   . GLN   A 1 150 ? 1.565   -18.698 34.088  1.00 43.73  ? 1187 GLN   A N   1 
ATOM   1017 C CA  . GLN   A 1 150 ? 2.351   -17.477 34.184  1.00 43.69  ? 1187 GLN   A CA  1 
ATOM   1018 C C   . GLN   A 1 150 ? 1.604   -16.312 33.537  1.00 41.60  ? 1187 GLN   A C   1 
ATOM   1019 O O   . GLN   A 1 150 ? 1.619   -15.201 34.062  1.00 41.37  ? 1187 GLN   A O   1 
ATOM   1020 C CB  . GLN   A 1 150 ? 3.721   -17.683 33.535  1.00 45.13  ? 1187 GLN   A CB  1 
ATOM   1021 C CG  . GLN   A 1 150 ? 4.639   -18.593 34.339  1.00 47.98  ? 1187 GLN   A CG  1 
ATOM   1022 C CD  . GLN   A 1 150 ? 5.948   -18.854 33.636  1.00 49.83  ? 1187 GLN   A CD  1 
ATOM   1023 O OE1 . GLN   A 1 150 ? 6.716   -17.937 33.355  1.00 50.07  ? 1187 GLN   A OE1 1 
ATOM   1024 N NE2 . GLN   A 1 150 ? 6.214   -20.118 33.344  1.00 51.44  ? 1187 GLN   A NE2 1 
ATOM   1025 N N   . VAL   A 1 151 ? 0.950   -16.580 32.399  1.00 40.53  ? 1188 VAL   A N   1 
ATOM   1026 C CA  . VAL   A 1 151 ? 0.202   -15.564 31.674  1.00 39.15  ? 1188 VAL   A CA  1 
ATOM   1027 C C   . VAL   A 1 151 ? -0.961  -15.077 32.538  1.00 38.63  ? 1188 VAL   A C   1 
ATOM   1028 O O   . VAL   A 1 151 ? -1.232  -13.879 32.588  1.00 38.16  ? 1188 VAL   A O   1 
ATOM   1029 C CB  . VAL   A 1 151 ? -0.290  -16.093 30.312  1.00 38.58  ? 1188 VAL   A CB  1 
ATOM   1030 C CG1 . VAL   A 1 151 ? -1.270  -15.137 29.646  1.00 37.50  ? 1188 VAL   A CG1 1 
ATOM   1031 C CG2 . VAL   A 1 151 ? 0.869   -16.404 29.377  1.00 39.46  ? 1188 VAL   A CG2 1 
ATOM   1032 N N   . ALA   A 1 152 ? -1.639  -16.016 33.211  1.00 38.99  ? 1189 ALA   A N   1 
ATOM   1033 C CA  . ALA   A 1 152 ? -2.773  -15.695 34.065  1.00 38.90  ? 1189 ALA   A CA  1 
ATOM   1034 C C   . ALA   A 1 152 ? -2.332  -14.780 35.206  1.00 39.72  ? 1189 ALA   A C   1 
ATOM   1035 O O   . ALA   A 1 152 ? -3.046  -13.842 35.558  1.00 39.56  ? 1189 ALA   A O   1 
ATOM   1036 C CB  . ALA   A 1 152 ? -3.401  -16.965 34.588  1.00 39.60  ? 1189 ALA   A CB  1 
ATOM   1037 N N   . LYS   A 1 153 ? -1.154  -15.065 35.774  1.00 41.05  ? 1190 LYS   A N   1 
ATOM   1038 C CA  . LYS   A 1 153 ? -0.585  -14.259 36.843  1.00 42.45  ? 1190 LYS   A CA  1 
ATOM   1039 C C   . LYS   A 1 153 ? -0.187  -12.884 36.306  1.00 42.14  ? 1190 LYS   A C   1 
ATOM   1040 O O   . LYS   A 1 153 ? -0.279  -11.888 37.022  1.00 42.85  ? 1190 LYS   A O   1 
ATOM   1041 C CB  . LYS   A 1 153 ? 0.619   -14.976 37.462  1.00 44.42  ? 1190 LYS   A CB  1 
ATOM   1042 C CG  . LYS   A 1 153 ? 0.288   -16.257 38.217  1.00 45.64  ? 1190 LYS   A CG  1 
ATOM   1043 C CD  . LYS   A 1 153 ? 1.507   -16.979 38.751  1.00 48.14  ? 1190 LYS   A CD  1 
ATOM   1044 C CE  . LYS   A 1 153 ? 1.155   -18.181 39.602  1.00 49.92  ? 1190 LYS   A CE  1 
ATOM   1045 N NZ  . LYS   A 1 153 ? 2.365   -18.885 40.086  1.00 52.87  ? 1190 LYS   A NZ  1 
ATOM   1046 N N   . GLY   A 1 154 ? 0.267   -12.847 35.047  1.00 41.40  ? 1191 GLY   A N   1 
ATOM   1047 C CA  . GLY   A 1 154 ? 0.600   -11.602 34.374  1.00 41.14  ? 1191 GLY   A CA  1 
ATOM   1048 C C   . GLY   A 1 154 ? -0.633  -10.743 34.103  1.00 40.24  ? 1191 GLY   A C   1 
ATOM   1049 O O   . GLY   A 1 154 ? -0.596  -9.528  34.282  1.00 40.45  ? 1191 GLY   A O   1 
ATOM   1050 N N   . MET   A 1 155 ? -1.721  -11.394 33.671  1.00 39.44  ? 1192 MET   A N   1 
ATOM   1051 C CA  . MET   A 1 155 ? -2.955  -10.705 33.328  1.00 39.19  ? 1192 MET   A CA  1 
ATOM   1052 C C   . MET   A 1 155 ? -3.688  -10.275 34.598  1.00 40.15  ? 1192 MET   A C   1 
ATOM   1053 O O   . MET   A 1 155 ? -4.447  -9.310  34.572  1.00 40.49  ? 1192 MET   A O   1 
ATOM   1054 C CB  . MET   A 1 155 ? -3.874  -11.606 32.495  1.00 38.38  ? 1192 MET   A CB  1 
ATOM   1055 C CG  . MET   A 1 155 ? -3.450  -11.733 31.039  1.00 37.95  ? 1192 MET   A CG  1 
ATOM   1056 S SD  . MET   A 1 155 ? -3.299  -10.151 30.160  1.00 38.37  ? 1192 MET   A SD  1 
ATOM   1057 C CE  . MET   A 1 155 ? -4.740  -9.271  30.762  1.00 38.92  ? 1192 MET   A CE  1 
ATOM   1058 N N   . LYS   A 1 156 ? -3.463  -11.006 35.698  1.00 41.10  ? 1193 LYS   A N   1 
ATOM   1059 C CA  . LYS   A 1 156 ? -4.023  -10.659 36.995  1.00 42.58  ? 1193 LYS   A CA  1 
ATOM   1060 C C   . LYS   A 1 156 ? -3.481  -9.303  37.446  1.00 44.01  ? 1193 LYS   A C   1 
ATOM   1061 O O   . LYS   A 1 156 ? -4.227  -8.483  37.979  1.00 44.98  ? 1193 LYS   A O   1 
ATOM   1062 C CB  . LYS   A 1 156 ? -3.692  -11.751 38.018  1.00 43.54  ? 1193 LYS   A CB  1 
ATOM   1063 C CG  . LYS   A 1 156 ? -4.228  -11.520 39.425  1.00 45.32  ? 1193 LYS   A CG  1 
ATOM   1064 C CD  . LYS   A 1 156 ? -3.814  -12.597 40.405  1.00 46.76  ? 1193 LYS   A CD  1 
ATOM   1065 C CE  . LYS   A 1 156 ? -4.290  -12.330 41.817  1.00 48.91  ? 1193 LYS   A CE  1 
ATOM   1066 N NZ  . LYS   A 1 156 ? -3.866  -13.403 42.747  1.00 50.73  ? 1193 LYS   A NZ  1 
ATOM   1067 N N   . TYR   A 1 157 ? -2.176  -9.087  37.231  1.00 44.51  ? 1194 TYR   A N   1 
ATOM   1068 C CA  . TYR   A 1 157 ? -1.517  -7.840  37.587  1.00 46.06  ? 1194 TYR   A CA  1 
ATOM   1069 C C   . TYR   A 1 157 ? -2.058  -6.698  36.728  1.00 45.95  ? 1194 TYR   A C   1 
ATOM   1070 O O   . TYR   A 1 157 ? -2.435  -5.654  37.254  1.00 47.35  ? 1194 TYR   A O   1 
ATOM   1071 C CB  . TYR   A 1 157 ? 0.001   -7.987  37.445  1.00 46.76  ? 1194 TYR   A CB  1 
ATOM   1072 C CG  . TYR   A 1 157 ? 0.794   -6.725  37.681  1.00 48.60  ? 1194 TYR   A CG  1 
ATOM   1073 C CD1 . TYR   A 1 157 ? 1.448   -6.506  38.884  1.00 50.96  ? 1194 TYR   A CD1 1 
ATOM   1074 C CD2 . TYR   A 1 157 ? 0.920   -5.760  36.694  1.00 48.40  ? 1194 TYR   A CD2 1 
ATOM   1075 C CE1 . TYR   A 1 157 ? 2.183   -5.354  39.109  1.00 52.96  ? 1194 TYR   A CE1 1 
ATOM   1076 C CE2 . TYR   A 1 157 ? 1.653   -4.603  36.901  1.00 50.40  ? 1194 TYR   A CE2 1 
ATOM   1077 C CZ  . TYR   A 1 157 ? 2.287   -4.398  38.114  1.00 52.68  ? 1194 TYR   A CZ  1 
ATOM   1078 O OH  . TYR   A 1 157 ? 3.019   -3.255  38.325  1.00 55.05  ? 1194 TYR   A OH  1 
ATOM   1079 N N   . LEU   A 1 158 ? -2.076  -6.906  35.406  1.00 44.78  ? 1195 LEU   A N   1 
ATOM   1080 C CA  . LEU   A 1 158 ? -2.532  -5.893  34.466  1.00 45.02  ? 1195 LEU   A CA  1 
ATOM   1081 C C   . LEU   A 1 158 ? -3.996  -5.550  34.733  1.00 45.55  ? 1195 LEU   A C   1 
ATOM   1082 O O   . LEU   A 1 158 ? -4.363  -4.376  34.738  1.00 46.91  ? 1195 LEU   A O   1 
ATOM   1083 C CB  . LEU   A 1 158 ? -2.345  -6.412  33.036  1.00 43.85  ? 1195 LEU   A CB  1 
ATOM   1084 C CG  . LEU   A 1 158 ? -0.899  -6.574  32.569  1.00 44.03  ? 1195 LEU   A CG  1 
ATOM   1085 C CD1 . LEU   A 1 158 ? -0.850  -7.046  31.123  1.00 43.15  ? 1195 LEU   A CD1 1 
ATOM   1086 C CD2 . LEU   A 1 158 ? -0.119  -5.276  32.728  1.00 45.70  ? 1195 LEU   A CD2 1 
ATOM   1087 N N   . ALA   A 1 159 ? -4.819  -6.584  34.952  1.00 44.87  ? 1196 ALA   A N   1 
ATOM   1088 C CA  . ALA   A 1 159 ? -6.243  -6.414  35.197  1.00 45.64  ? 1196 ALA   A CA  1 
ATOM   1089 C C   . ALA   A 1 159 ? -6.471  -5.562  36.444  1.00 47.82  ? 1196 ALA   A C   1 
ATOM   1090 O O   . ALA   A 1 159 ? -7.358  -4.710  36.456  1.00 49.17  ? 1196 ALA   A O   1 
ATOM   1091 C CB  . ALA   A 1 159 ? -6.909  -7.761  35.332  1.00 44.71  ? 1196 ALA   A CB  1 
ATOM   1092 N N   . SER   A 1 160 ? -5.657  -5.798  37.482  1.00 48.62  ? 1197 SER   A N   1 
ATOM   1093 C CA  . SER   A 1 160 ? -5.792  -5.103  38.754  1.00 51.01  ? 1197 SER   A CA  1 
ATOM   1094 C C   . SER   A 1 160 ? -5.496  -3.612  38.596  1.00 52.81  ? 1197 SER   A C   1 
ATOM   1095 O O   . SER   A 1 160 ? -6.035  -2.799  39.344  1.00 55.14  ? 1197 SER   A O   1 
ATOM   1096 C CB  . SER   A 1 160 ? -4.911  -5.728  39.807  1.00 51.53  ? 1197 SER   A CB  1 
ATOM   1097 O OG  . SER   A 1 160 ? -3.539  -5.610  39.461  1.00 51.21  ? 1197 SER   A OG  1 
ATOM   1098 N N   . LYS   A 1 161 ? -4.645  -3.264  37.620  1.00 52.34  ? 1198 LYS   A N   1 
ATOM   1099 C CA  . LYS   A 1 161 ? -4.307  -1.877  37.336  1.00 54.27  ? 1198 LYS   A CA  1 
ATOM   1100 C C   . LYS   A 1 161 ? -5.158  -1.343  36.182  1.00 54.07  ? 1198 LYS   A C   1 
ATOM   1101 O O   . LYS   A 1 161 ? -4.822  -0.315  35.597  1.00 55.15  ? 1198 LYS   A O   1 
ATOM   1102 C CB  . LYS   A 1 161 ? -2.811  -1.758  37.016  1.00 54.40  ? 1198 LYS   A CB  1 
ATOM   1103 C CG  . LYS   A 1 161 ? -1.867  -2.283  38.091  1.00 55.29  ? 1198 LYS   A CG  1 
ATOM   1104 C CD  . LYS   A 1 161 ? -1.983  -1.563  39.423  1.00 58.33  ? 1198 LYS   A CD  1 
ATOM   1105 C CE  . LYS   A 1 161 ? -1.109  -2.157  40.508  1.00 59.46  ? 1198 LYS   A CE  1 
ATOM   1106 N NZ  . LYS   A 1 161 ? 0.334   -2.008  40.203  1.00 60.15  ? 1198 LYS   A NZ  1 
ATOM   1107 N N   . LYS   A 1 162 ? -6.270  -2.032  35.883  1.00 52.95  ? 1199 LYS   A N   1 
ATOM   1108 C CA  . LYS   A 1 162 ? -7.185  -1.660  34.813  1.00 53.14  ? 1199 LYS   A CA  1 
ATOM   1109 C C   . LYS   A 1 162 ? -6.412  -1.421  33.518  1.00 52.35  ? 1199 LYS   A C   1 
ATOM   1110 O O   . LYS   A 1 162 ? -6.315  -0.292  33.042  1.00 54.12  ? 1199 LYS   A O   1 
ATOM   1111 C CB  . LYS   A 1 162 ? -8.022  -0.438  35.210  1.00 56.04  ? 1199 LYS   A CB  1 
ATOM   1112 C CG  . LYS   A 1 162 ? -9.122  -0.722  36.224  1.00 57.17  ? 1199 LYS   A CG  1 
ATOM   1113 C CD  . LYS   A 1 162 ? -9.953  0.489   36.595  1.00 60.60  ? 1199 LYS   A CD  1 
ATOM   1114 C CE  . LYS   A 1 162 ? -10.738 1.073   35.439  1.00 61.84  ? 1199 LYS   A CE  1 
ATOM   1115 N NZ  . LYS   A 1 162 ? -11.627 2.172   35.886  1.00 65.60  ? 1199 LYS   A NZ  1 
ATOM   1116 N N   . PHE   A 1 163 ? -5.872  -2.509  32.960  1.00 50.09  ? 1200 PHE   A N   1 
ATOM   1117 C CA  . PHE   A 1 163 ? -5.197  -2.475  31.674  1.00 49.46  ? 1200 PHE   A CA  1 
ATOM   1118 C C   . PHE   A 1 163 ? -5.805  -3.548  30.776  1.00 47.84  ? 1200 PHE   A C   1 
ATOM   1119 O O   . PHE   A 1 163 ? -5.643  -4.740  31.032  1.00 46.25  ? 1200 PHE   A O   1 
ATOM   1120 C CB  . PHE   A 1 163 ? -3.688  -2.660  31.861  1.00 49.10  ? 1200 PHE   A CB  1 
ATOM   1121 C CG  . PHE   A 1 163 ? -2.875  -2.577  30.592  1.00 49.14  ? 1200 PHE   A CG  1 
ATOM   1122 C CD1 . PHE   A 1 163 ? -2.208  -1.408  30.253  1.00 51.11  ? 1200 PHE   A CD1 1 
ATOM   1123 C CD2 . PHE   A 1 163 ? -2.753  -3.672  29.750  1.00 47.63  ? 1200 PHE   A CD2 1 
ATOM   1124 C CE1 . PHE   A 1 163 ? -1.456  -1.331  29.090  1.00 51.35  ? 1200 PHE   A CE1 1 
ATOM   1125 C CE2 . PHE   A 1 163 ? -1.999  -3.595  28.589  1.00 47.93  ? 1200 PHE   A CE2 1 
ATOM   1126 C CZ  . PHE   A 1 163 ? -1.351  -2.425  28.261  1.00 49.77  ? 1200 PHE   A CZ  1 
ATOM   1127 N N   . VAL   A 1 164 ? -6.519  -3.104  29.734  1.00 48.61  ? 1201 VAL   A N   1 
ATOM   1128 C CA  . VAL   A 1 164 ? -7.102  -3.999  28.749  1.00 47.75  ? 1201 VAL   A CA  1 
ATOM   1129 C C   . VAL   A 1 164 ? -6.080  -4.213  27.635  1.00 47.11  ? 1201 VAL   A C   1 
ATOM   1130 O O   . VAL   A 1 164 ? -5.706  -3.265  26.947  1.00 48.57  ? 1201 VAL   A O   1 
ATOM   1131 C CB  . VAL   A 1 164 ? -8.431  -3.440  28.203  1.00 49.68  ? 1201 VAL   A CB  1 
ATOM   1132 C CG1 . VAL   A 1 164 ? -9.070  -4.388  27.200  1.00 49.38  ? 1201 VAL   A CG1 1 
ATOM   1133 C CG2 . VAL   A 1 164 ? -9.404  -3.109  29.325  1.00 50.76  ? 1201 VAL   A CG2 1 
ATOM   1134 N N   . HIS   A 1 165 ? -5.639  -5.466  27.470  1.00 45.29  ? 1202 HIS   A N   1 
ATOM   1135 C CA  . HIS   A 1 165 ? -4.581  -5.807  26.532  1.00 44.99  ? 1202 HIS   A CA  1 
ATOM   1136 C C   . HIS   A 1 165 ? -5.098  -5.744  25.095  1.00 46.07  ? 1202 HIS   A C   1 
ATOM   1137 O O   . HIS   A 1 165 ? -4.383  -5.294  24.202  1.00 46.72  ? 1202 HIS   A O   1 
ATOM   1138 C CB  . HIS   A 1 165 ? -4.014  -7.194  26.859  1.00 43.41  ? 1202 HIS   A CB  1 
ATOM   1139 C CG  . HIS   A 1 165 ? -2.702  -7.500  26.202  1.00 43.41  ? 1202 HIS   A CG  1 
ATOM   1140 N ND1 . HIS   A 1 165 ? -2.522  -7.564  24.842  1.00 44.18  ? 1202 HIS   A ND1 1 
ATOM   1141 C CD2 . HIS   A 1 165 ? -1.493  -7.757  26.776  1.00 43.20  ? 1202 HIS   A CD2 1 
ATOM   1142 C CE1 . HIS   A 1 165 ? -1.248  -7.850  24.585  1.00 44.34  ? 1202 HIS   A CE1 1 
ATOM   1143 N NE2 . HIS   A 1 165 ? -0.591  -7.975  25.771  1.00 43.76  ? 1202 HIS   A NE2 1 
ATOM   1144 N N   . ARG   A 1 166 ? -6.325  -6.241  24.888  1.00 46.41  ? 1203 ARG   A N   1 
ATOM   1145 C CA  . ARG   A 1 166 ? -7.037  -6.169  23.618  1.00 47.94  ? 1203 ARG   A CA  1 
ATOM   1146 C C   . ARG   A 1 166 ? -6.556  -7.269  22.671  1.00 47.40  ? 1203 ARG   A C   1 
ATOM   1147 O O   . ARG   A 1 166 ? -7.377  -8.031  22.156  1.00 48.27  ? 1203 ARG   A O   1 
ATOM   1148 C CB  . ARG   A 1 166 ? -6.934  -4.778  22.980  1.00 50.12  ? 1203 ARG   A CB  1 
ATOM   1149 C CG  . ARG   A 1 166 ? -7.656  -3.694  23.768  1.00 51.47  ? 1203 ARG   A CG  1 
ATOM   1150 C CD  . ARG   A 1 166 ? -7.710  -2.354  23.060  1.00 54.42  ? 1203 ARG   A CD  1 
ATOM   1151 N NE  . ARG   A 1 166 ? -8.859  -1.573  23.503  1.00 56.69  ? 1203 ARG   A NE  1 
ATOM   1152 C CZ  . ARG   A 1 166 ? -8.809  -0.543  24.343  1.00 57.92  ? 1203 ARG   A CZ  1 
ATOM   1153 N NH1 . ARG   A 1 166 ? -9.907  0.142   24.612  1.00 60.27  ? 1203 ARG   A NH1 1 
ATOM   1154 N NH2 . ARG   A 1 166 ? -7.667  -0.203  24.917  1.00 57.07  ? 1203 ARG   A NH2 1 
ATOM   1155 N N   . ASP   A 1 167 ? -5.236  -7.341  22.438  1.00 46.45  ? 1204 ASP   A N   1 
ATOM   1156 C CA  . ASP   A 1 167 ? -4.666  -8.348  21.556  1.00 46.04  ? 1204 ASP   A CA  1 
ATOM   1157 C C   . ASP   A 1 167 ? -3.846  -9.336  22.383  1.00 43.99  ? 1204 ASP   A C   1 
ATOM   1158 O O   . ASP   A 1 167 ? -2.623  -9.381  22.274  1.00 43.89  ? 1204 ASP   A O   1 
ATOM   1159 C CB  . ASP   A 1 167 ? -3.846  -7.693  20.439  1.00 47.60  ? 1204 ASP   A CB  1 
ATOM   1160 C CG  . ASP   A 1 167 ? -3.264  -8.674  19.434  1.00 48.03  ? 1204 ASP   A CG  1 
ATOM   1161 O OD1 . ASP   A 1 167 ? -4.017  -9.554  18.973  1.00 48.39  ? 1204 ASP   A OD1 1 
ATOM   1162 O OD2 . ASP   A 1 167 ? -2.067  -8.541  19.111  1.00 48.37  ? 1204 ASP   A OD2 1 
ATOM   1163 N N   . LEU   A 1 168 ? -4.541  -10.128 23.209  1.00 42.64  ? 1205 LEU   A N   1 
ATOM   1164 C CA  . LEU   A 1 168 ? -3.902  -11.165 24.003  1.00 41.22  ? 1205 LEU   A CA  1 
ATOM   1165 C C   . LEU   A 1 168 ? -3.817  -12.447 23.177  1.00 41.20  ? 1205 LEU   A C   1 
ATOM   1166 O O   . LEU   A 1 168 ? -4.834  -12.962 22.718  1.00 41.52  ? 1205 LEU   A O   1 
ATOM   1167 C CB  . LEU   A 1 168 ? -4.699  -11.385 25.294  1.00 40.41  ? 1205 LEU   A CB  1 
ATOM   1168 C CG  . LEU   A 1 168 ? -4.162  -12.470 26.229  1.00 39.50  ? 1205 LEU   A CG  1 
ATOM   1169 C CD1 . LEU   A 1 168 ? -2.788  -12.097 26.768  1.00 39.37  ? 1205 LEU   A CD1 1 
ATOM   1170 C CD2 . LEU   A 1 168 ? -5.130  -12.726 27.373  1.00 39.09  ? 1205 LEU   A CD2 1 
ATOM   1171 N N   . ALA   A 1 169 ? -2.590  -12.946 22.999  1.00 41.04  ? 1206 ALA   A N   1 
ATOM   1172 C CA  . ALA   A 1 169 ? -2.344  -14.169 22.253  1.00 41.68  ? 1206 ALA   A CA  1 
ATOM   1173 C C   . ALA   A 1 169 ? -0.947  -14.688 22.578  1.00 41.78  ? 1206 ALA   A C   1 
ATOM   1174 O O   . ALA   A 1 169 ? -0.145  -13.981 23.185  1.00 41.47  ? 1206 ALA   A O   1 
ATOM   1175 C CB  . ALA   A 1 169 ? -2.507  -13.912 20.775  1.00 43.22  ? 1206 ALA   A CB  1 
ATOM   1176 N N   . ALA   A 1 170 ? -0.669  -15.927 22.156  1.00 42.64  ? 1207 ALA   A N   1 
ATOM   1177 C CA  . ALA   A 1 170 ? 0.620   -16.557 22.389  1.00 43.43  ? 1207 ALA   A CA  1 
ATOM   1178 C C   . ALA   A 1 170 ? 1.727   -15.768 21.692  1.00 44.50  ? 1207 ALA   A C   1 
ATOM   1179 O O   . ALA   A 1 170 ? 2.834   -15.660 22.214  1.00 44.93  ? 1207 ALA   A O   1 
ATOM   1180 C CB  . ALA   A 1 170 ? 0.584   -17.989 21.913  1.00 44.73  ? 1207 ALA   A CB  1 
ATOM   1181 N N   . ARG   A 1 171 ? 1.410   -15.214 20.514  1.00 45.36  ? 1208 ARG   A N   1 
ATOM   1182 C CA  . ARG   A 1 171 ? 2.368   -14.460 19.720  1.00 46.89  ? 1208 ARG   A CA  1 
ATOM   1183 C C   . ARG   A 1 171 ? 2.820   -13.197 20.457  1.00 46.22  ? 1208 ARG   A C   1 
ATOM   1184 O O   . ARG   A 1 171 ? 3.901   -12.682 20.178  1.00 47.65  ? 1208 ARG   A O   1 
ATOM   1185 C CB  . ARG   A 1 171 ? 1.774   -14.103 18.352  1.00 48.22  ? 1208 ARG   A CB  1 
ATOM   1186 C CG  . ARG   A 1 171 ? 0.510   -13.255 18.408  1.00 47.39  ? 1208 ARG   A CG  1 
ATOM   1187 C CD  . ARG   A 1 171 ? 0.013   -12.867 17.027  1.00 49.33  ? 1208 ARG   A CD  1 
ATOM   1188 N NE  . ARG   A 1 171 ? -1.266  -12.171 17.074  1.00 49.02  ? 1208 ARG   A NE  1 
ATOM   1189 C CZ  . ARG   A 1 171 ? -2.422  -12.732 17.413  1.00 48.30  ? 1208 ARG   A CZ  1 
ATOM   1190 N NH1 . ARG   A 1 171 ? -2.507  -14.043 17.561  1.00 48.01  ? 1208 ARG   A NH1 1 
ATOM   1191 N NH2 . ARG   A 1 171 ? -3.496  -11.982 17.591  1.00 48.24  ? 1208 ARG   A NH2 1 
ATOM   1192 N N   . ASN   A 1 172 ? 1.992   -12.703 21.390  1.00 44.40  ? 1209 ASN   A N   1 
ATOM   1193 C CA  . ASN   A 1 172 ? 2.301   -11.494 22.140  1.00 43.88  ? 1209 ASN   A CA  1 
ATOM   1194 C C   . ASN   A 1 172 ? 2.777   -11.844 23.551  1.00 43.04  ? 1209 ASN   A C   1 
ATOM   1195 O O   . ASN   A 1 172 ? 2.660   -11.025 24.460  1.00 42.35  ? 1209 ASN   A O   1 
ATOM   1196 C CB  . ASN   A 1 172 ? 1.095   -10.552 22.193  1.00 43.19  ? 1209 ASN   A CB  1 
ATOM   1197 C CG  . ASN   A 1 172 ? 0.516   -10.262 20.825  1.00 44.34  ? 1209 ASN   A CG  1 
ATOM   1198 O OD1 . ASN   A 1 172 ? 1.228   -9.823  19.924  1.00 45.85  ? 1209 ASN   A OD1 1 
ATOM   1199 N ND2 . ASN   A 1 172 ? -0.771  -10.516 20.655  1.00 44.06  ? 1209 ASN   A ND2 1 
ATOM   1200 N N   . CYS   A 1 173 ? 3.315   -13.058 23.726  1.00 43.46  ? 1210 CYS   A N   1 
ATOM   1201 C CA  . CYS   A 1 173 ? 3.938   -13.469 24.975  1.00 43.63  ? 1210 CYS   A CA  1 
ATOM   1202 C C   . CYS   A 1 173 ? 5.371   -13.912 24.689  1.00 45.89  ? 1210 CYS   A C   1 
ATOM   1203 O O   . CYS   A 1 173 ? 5.621   -14.556 23.673  1.00 47.00  ? 1210 CYS   A O   1 
ATOM   1204 C CB  . CYS   A 1 173 ? 3.154   -14.596 25.637  1.00 42.67  ? 1210 CYS   A CB  1 
ATOM   1205 S SG  . CYS   A 1 173 ? 1.475   -14.118 26.126  1.00 40.54  ? 1210 CYS   A SG  1 
ATOM   1206 N N   . MET   A 1 174 ? 6.297   -13.570 25.595  1.00 47.02  ? 1211 MET   A N   1 
ATOM   1207 C CA  . MET   A 1 174 ? 7.722   -13.710 25.335  1.00 49.65  ? 1211 MET   A CA  1 
ATOM   1208 C C   . MET   A 1 174 ? 8.379   -14.547 26.432  1.00 51.00  ? 1211 MET   A C   1 
ATOM   1209 O O   . MET   A 1 174 ? 7.861   -14.632 27.543  1.00 50.03  ? 1211 MET   A O   1 
ATOM   1210 C CB  . MET   A 1 174 ? 8.390   -12.332 25.283  1.00 50.66  ? 1211 MET   A CB  1 
ATOM   1211 C CG  . MET   A 1 174 ? 7.886   -11.455 24.148  1.00 50.31  ? 1211 MET   A CG  1 
ATOM   1212 S SD  . MET   A 1 174 ? 8.263   -12.122 22.506  1.00 52.04  ? 1211 MET   A SD  1 
ATOM   1213 C CE  . MET   A 1 174 ? 7.928   -10.689 21.483  1.00 52.35  ? 1211 MET   A CE  1 
ATOM   1214 N N   . LEU   A 1 175 ? 9.528   -15.153 26.098  1.00 53.78  ? 1212 LEU   A N   1 
ATOM   1215 C CA  . LEU   A 1 175 ? 10.275  -16.013 27.006  1.00 55.97  ? 1212 LEU   A CA  1 
ATOM   1216 C C   . LEU   A 1 175 ? 11.688  -15.462 27.192  1.00 58.88  ? 1212 LEU   A C   1 
ATOM   1217 O O   . LEU   A 1 175 ? 12.354  -15.126 26.214  1.00 60.26  ? 1212 LEU   A O   1 
ATOM   1218 C CB  . LEU   A 1 175 ? 10.332  -17.431 26.425  1.00 57.38  ? 1212 LEU   A CB  1 
ATOM   1219 C CG  . LEU   A 1 175 ? 9.095   -18.308 26.626  1.00 55.64  ? 1212 LEU   A CG  1 
ATOM   1220 C CD1 . LEU   A 1 175 ? 8.768   -18.468 28.105  1.00 55.22  ? 1212 LEU   A CD1 1 
ATOM   1221 C CD2 . LEU   A 1 175 ? 7.895   -17.761 25.864  1.00 52.94  ? 1212 LEU   A CD2 1 
ATOM   1222 N N   . ASP   A 1 176 ? 12.140  -15.398 28.452  1.00 60.16  ? 1213 ASP   A N   1 
ATOM   1223 C CA  . ASP   A 1 176 ? 13.496  -14.978 28.778  1.00 63.49  ? 1213 ASP   A CA  1 
ATOM   1224 C C   . ASP   A 1 176 ? 14.384  -16.221 28.860  1.00 66.83  ? 1213 ASP   A C   1 
ATOM   1225 O O   . ASP   A 1 176 ? 13.970  -17.304 28.452  1.00 66.44  ? 1213 ASP   A O   1 
ATOM   1226 C CB  . ASP   A 1 176 ? 13.513  -14.127 30.054  1.00 63.56  ? 1213 ASP   A CB  1 
ATOM   1227 C CG  . ASP   A 1 176 ? 13.180  -14.876 31.334  1.00 63.82  ? 1213 ASP   A CG  1 
ATOM   1228 O OD1 . ASP   A 1 176 ? 12.854  -16.076 31.251  1.00 63.74  ? 1213 ASP   A OD1 1 
ATOM   1229 O OD2 . ASP   A 1 176 ? 13.253  -14.250 32.410  1.00 64.45  ? 1213 ASP   A OD2 1 
ATOM   1230 N N   . GLU   A 1 177 ? 15.603  -16.057 29.392  1.00 70.49  ? 1214 GLU   A N   1 
ATOM   1231 C CA  . GLU   A 1 177 ? 16.571  -17.143 29.460  1.00 74.60  ? 1214 GLU   A CA  1 
ATOM   1232 C C   . GLU   A 1 177 ? 16.204  -18.129 30.572  1.00 75.14  ? 1214 GLU   A C   1 
ATOM   1233 O O   . GLU   A 1 177 ? 16.646  -19.276 30.538  1.00 77.90  ? 1214 GLU   A O   1 
ATOM   1234 C CB  . GLU   A 1 177 ? 17.998  -16.609 29.633  1.00 78.90  ? 1214 GLU   A CB  1 
ATOM   1235 C CG  . GLU   A 1 177 ? 18.281  -15.924 30.964  1.00 80.04  ? 1214 GLU   A CG  1 
ATOM   1236 C CD  . GLU   A 1 177 ? 17.816  -14.482 31.088  1.00 77.43  ? 1214 GLU   A CD  1 
ATOM   1237 O OE1 . GLU   A 1 177 ? 18.175  -13.836 32.091  1.00 79.00  ? 1214 GLU   A OE1 1 
ATOM   1238 O OE2 . GLU   A 1 177 ? 17.092  -14.009 30.189  1.00 74.25  ? 1214 GLU   A OE2 1 
ATOM   1239 N N   . LYS   A 1 178 ? 15.398  -17.685 31.548  1.00 72.87  ? 1215 LYS   A N   1 
ATOM   1240 C CA  . LYS   A 1 178 ? 14.902  -18.561 32.600  1.00 73.23  ? 1215 LYS   A CA  1 
ATOM   1241 C C   . LYS   A 1 178 ? 13.591  -19.227 32.175  1.00 69.78  ? 1215 LYS   A C   1 
ATOM   1242 O O   . LYS   A 1 178 ? 12.933  -19.860 32.998  1.00 69.31  ? 1215 LYS   A O   1 
ATOM   1243 C CB  . LYS   A 1 178 ? 14.678  -17.790 33.906  1.00 73.03  ? 1215 LYS   A CB  1 
ATOM   1244 C CG  . LYS   A 1 178 ? 15.921  -17.180 34.541  1.00 77.13  ? 1215 LYS   A CG  1 
ATOM   1245 C CD  . LYS   A 1 178 ? 16.166  -15.736 34.158  1.00 76.27  ? 1215 LYS   A CD  1 
ATOM   1246 C CE  . LYS   A 1 178 ? 17.350  -15.129 34.881  1.00 80.60  ? 1215 LYS   A CE  1 
ATOM   1247 N NZ  . LYS   A 1 178 ? 17.448  -13.669 34.648  1.00 79.71  ? 1215 LYS   A NZ  1 
ATOM   1248 N N   . PHE   A 1 179 ? 13.227  -19.089 30.891  1.00 67.73  ? 1216 PHE   A N   1 
ATOM   1249 C CA  . PHE   A 1 179 ? 11.986  -19.628 30.353  1.00 64.68  ? 1216 PHE   A CA  1 
ATOM   1250 C C   . PHE   A 1 179 ? 10.801  -19.091 31.154  1.00 61.24  ? 1216 PHE   A C   1 
ATOM   1251 O O   . PHE   A 1 179 ? 9.930   -19.854 31.569  1.00 60.28  ? 1216 PHE   A O   1 
ATOM   1252 C CB  . PHE   A 1 179 ? 12.014  -21.161 30.331  1.00 67.01  ? 1216 PHE   A CB  1 
ATOM   1253 C CG  . PHE   A 1 179 ? 13.147  -21.769 29.542  1.00 70.88  ? 1216 PHE   A CG  1 
ATOM   1254 C CD1 . PHE   A 1 179 ? 12.921  -22.322 28.289  1.00 70.84  ? 1216 PHE   A CD1 1 
ATOM   1255 C CD2 . PHE   A 1 179 ? 14.434  -21.816 30.059  1.00 75.11  ? 1216 PHE   A CD2 1 
ATOM   1256 C CE1 . PHE   A 1 179 ? 13.960  -22.887 27.565  1.00 74.68  ? 1216 PHE   A CE1 1 
ATOM   1257 C CE2 . PHE   A 1 179 ? 15.471  -22.384 29.334  1.00 78.99  ? 1216 PHE   A CE2 1 
ATOM   1258 C CZ  . PHE   A 1 179 ? 15.233  -22.919 28.089  1.00 78.72  ? 1216 PHE   A CZ  1 
ATOM   1259 N N   . THR   A 1 180 ? 10.783  -17.767 31.356  1.00 59.64  ? 1217 THR   A N   1 
ATOM   1260 C CA  . THR   A 1 180 ? 9.729   -17.101 32.104  1.00 56.83  ? 1217 THR   A CA  1 
ATOM   1261 C C   . THR   A 1 180 ? 8.838   -16.334 31.130  1.00 53.34  ? 1217 THR   A C   1 
ATOM   1262 O O   . THR   A 1 180 ? 9.309   -15.441 30.429  1.00 53.30  ? 1217 THR   A O   1 
ATOM   1263 C CB  . THR   A 1 180 ? 10.309  -16.168 33.175  1.00 58.35  ? 1217 THR   A CB  1 
ATOM   1264 O OG1 . THR   A 1 180 ? 11.267  -16.902 33.939  1.00 62.04  ? 1217 THR   A OG1 1 
ATOM   1265 C CG2 . THR   A 1 180 ? 9.253   -15.596 34.096  1.00 56.41  ? 1217 THR   A CG2 1 
ATOM   1266 N N   . VAL   A 1 181 ? 7.549   -16.695 31.104  1.00 81.69  ? 1218 VAL   A N   1 
ATOM   1267 C CA  . VAL   A 1 181 ? 6.589   -16.104 30.188  1.00 80.24  ? 1218 VAL   A CA  1 
ATOM   1268 C C   . VAL   A 1 181 ? 6.243   -14.701 30.680  1.00 83.03  ? 1218 VAL   A C   1 
ATOM   1269 O O   . VAL   A 1 181 ? 5.866   -14.527 31.837  1.00 86.26  ? 1218 VAL   A O   1 
ATOM   1270 C CB  . VAL   A 1 181 ? 5.327   -16.979 30.054  1.00 79.38  ? 1218 VAL   A CB  1 
ATOM   1271 C CG1 . VAL   A 1 181 ? 4.266   -16.319 29.185  1.00 78.75  ? 1218 VAL   A CG1 1 
ATOM   1272 C CG2 . VAL   A 1 181 ? 5.655   -18.369 29.530  1.00 76.97  ? 1218 VAL   A CG2 1 
ATOM   1273 N N   . LYS   A 1 182 ? 6.376   -13.714 29.784  1.00 82.15  ? 1219 LYS   A N   1 
ATOM   1274 C CA  . LYS   A 1 182 ? 6.052   -12.329 30.087  1.00 84.93  ? 1219 LYS   A CA  1 
ATOM   1275 C C   . LYS   A 1 182 ? 5.047   -11.812 29.060  1.00 83.10  ? 1219 LYS   A C   1 
ATOM   1276 O O   . LYS   A 1 182 ? 5.250   -11.970 27.858  1.00 80.20  ? 1219 LYS   A O   1 
ATOM   1277 C CB  . LYS   A 1 182 ? 7.318   -11.467 30.084  1.00 86.87  ? 1219 LYS   A CB  1 
ATOM   1278 C CG  . LYS   A 1 182 ? 8.336   -11.796 31.168  1.00 89.60  ? 1219 LYS   A CG  1 
ATOM   1279 C CD  . LYS   A 1 182 ? 9.499   -10.826 31.214  1.00 92.83  ? 1219 LYS   A CD  1 
ATOM   1280 C CE  . LYS   A 1 182 ? 10.564  -11.207 32.220  1.00 95.78  ? 1219 LYS   A CE  1 
ATOM   1281 N NZ  . LYS   A 1 182 ? 10.067  -11.119 33.614  1.00 99.66  ? 1219 LYS   A NZ  1 
ATOM   1282 N N   . VAL   A 1 183 ? 3.967   -11.191 29.554  1.00 85.34  ? 1220 VAL   A N   1 
ATOM   1283 C CA  . VAL   A 1 183 ? 2.924   -10.642 28.703  1.00 84.18  ? 1220 VAL   A CA  1 
ATOM   1284 C C   . VAL   A 1 183 ? 3.429   -9.333  28.102  1.00 84.84  ? 1220 VAL   A C   1 
ATOM   1285 O O   . VAL   A 1 183 ? 3.622   -8.354  28.821  1.00 88.29  ? 1220 VAL   A O   1 
ATOM   1286 C CB  . VAL   A 1 183 ? 1.611   -10.434 29.484  1.00 86.90  ? 1220 VAL   A CB  1 
ATOM   1287 C CG1 . VAL   A 1 183 ? 0.531   -9.801  28.618  1.00 85.88  ? 1220 VAL   A CG1 1 
ATOM   1288 C CG2 . VAL   A 1 183 ? 1.108   -11.730 30.103  1.00 87.33  ? 1220 VAL   A CG2 1 
ATOM   1289 N N   . ALA   A 1 184 ? 3.634   -9.333  26.778  1.00 82.27  ? 1221 ALA   A N   1 
ATOM   1290 C CA  . ALA   A 1 184 ? 4.170   -8.185  26.066  1.00 83.15  ? 1221 ALA   A CA  1 
ATOM   1291 C C   . ALA   A 1 184 ? 3.071   -7.532  25.232  1.00 82.37  ? 1221 ALA   A C   1 
ATOM   1292 O O   . ALA   A 1 184 ? 2.179   -8.215  24.732  1.00 80.11  ? 1221 ALA   A O   1 
ATOM   1293 C CB  . ALA   A 1 184 ? 5.326   -8.619  25.200  1.00 81.58  ? 1221 ALA   A CB  1 
ATOM   1294 N N   . ASP   A 1 185 ? 3.157   -6.204  25.088  1.00 84.84  ? 1222 ASP   A N   1 
ATOM   1295 C CA  . ASP   A 1 185 ? 2.221   -5.439  24.280  1.00 84.46  ? 1222 ASP   A CA  1 
ATOM   1296 C C   . ASP   A 1 185 ? 2.987   -4.784  23.134  1.00 84.44  ? 1222 ASP   A C   1 
ATOM   1297 O O   . ASP   A 1 185 ? 4.035   -4.180  23.354  1.00 87.03  ? 1222 ASP   A O   1 
ATOM   1298 C CB  . ASP   A 1 185 ? 1.493   -4.389  25.124  1.00 87.70  ? 1222 ASP   A CB  1 
ATOM   1299 C CG  . ASP   A 1 185 ? 0.401   -3.632  24.385  1.00 86.89  ? 1222 ASP   A CG  1 
ATOM   1300 O OD1 . ASP   A 1 185 ? 0.067   -4.031  23.251  1.00 83.82  ? 1222 ASP   A OD1 1 
ATOM   1301 O OD2 . ASP   A 1 185 ? -0.104  -2.641  24.948  1.00 89.74  ? 1222 ASP   A OD2 1 
ATOM   1302 N N   . PHE   A 1 186 ? 2.451   -4.914  21.914  1.00 82.47  ? 1223 PHE   A N   1 
ATOM   1303 C CA  . PHE   A 1 186 ? 3.034   -4.295  20.734  1.00 82.95  ? 1223 PHE   A CA  1 
ATOM   1304 C C   . PHE   A 1 186 ? 2.348   -2.962  20.437  1.00 84.56  ? 1223 PHE   A C   1 
ATOM   1305 O O   . PHE   A 1 186 ? 2.876   -2.155  19.676  1.00 85.75  ? 1223 PHE   A O   1 
ATOM   1306 C CB  . PHE   A 1 186 ? 2.962   -5.255  19.544  1.00 80.28  ? 1223 PHE   A CB  1 
ATOM   1307 C CG  . PHE   A 1 186 ? 3.992   -6.356  19.567  1.00 79.88  ? 1223 PHE   A CG  1 
ATOM   1308 C CD1 . PHE   A 1 186 ? 5.297   -6.112  19.164  1.00 81.67  ? 1223 PHE   A CD1 1 
ATOM   1309 C CD2 . PHE   A 1 186 ? 3.666   -7.628  20.011  1.00 78.30  ? 1223 PHE   A CD2 1 
ATOM   1310 C CE1 . PHE   A 1 186 ? 6.247   -7.122  19.185  1.00 81.66  ? 1223 PHE   A CE1 1 
ATOM   1311 C CE2 . PHE   A 1 186 ? 4.618   -8.636  20.036  1.00 78.09  ? 1223 PHE   A CE2 1 
ATOM   1312 C CZ  . PHE   A 1 186 ? 5.906   -8.381  19.623  1.00 79.66  ? 1223 PHE   A CZ  1 
ATOM   1313 N N   . GLY   A 1 187 ? 1.166   -2.743  21.029  1.00 85.30  ? 1224 GLY   A N   1 
ATOM   1314 C CA  . GLY   A 1 187 ? 0.484   -1.461  20.950  1.00 87.27  ? 1224 GLY   A CA  1 
ATOM   1315 C C   . GLY   A 1 187 ? -0.143  -1.208  19.580  1.00 85.74  ? 1224 GLY   A C   1 
ATOM   1316 O O   . GLY   A 1 187 ? -0.238  -0.061  19.148  1.00 86.95  ? 1224 GLY   A O   1 
ATOM   1317 N N   . LEU   A 1 188 ? -0.577  -2.287  18.913  1.00 83.87  ? 1225 LEU   A N   1 
ATOM   1318 C CA  . LEU   A 1 188 ? -1.245  -2.192  17.623  1.00 82.85  ? 1225 LEU   A CA  1 
ATOM   1319 C C   . LEU   A 1 188 ? -2.760  -2.125  17.815  1.00 83.01  ? 1225 LEU   A C   1 
ATOM   1320 O O   . LEU   A 1 188 ? -3.493  -1.901  16.853  1.00 82.17  ? 1225 LEU   A O   1 
ATOM   1321 C CB  . LEU   A 1 188 ? -0.858  -3.397  16.758  1.00 81.31  ? 1225 LEU   A CB  1 
ATOM   1322 C CG  . LEU   A 1 188 ? 0.456   -3.262  15.989  1.00 82.18  ? 1225 LEU   A CG  1 
ATOM   1323 C CD1 . LEU   A 1 188 ? 1.640   -3.151  16.937  1.00 83.84  ? 1225 LEU   A CD1 1 
ATOM   1324 C CD2 . LEU   A 1 188 ? 0.642   -4.428  15.029  1.00 81.29  ? 1225 LEU   A CD2 1 
ATOM   1325 N N   . ALA   A 1 189 ? -3.219  -2.304  19.061  1.00 84.84  ? 1226 ALA   A N   1 
ATOM   1326 C CA  . ALA   A 1 189 ? -4.639  -2.353  19.372  1.00 85.78  ? 1226 ALA   A CA  1 
ATOM   1327 C C   . ALA   A 1 189 ? -5.247  -0.951  19.400  1.00 87.68  ? 1226 ALA   A C   1 
ATOM   1328 O O   . ALA   A 1 189 ? -6.464  -0.817  19.512  1.00 88.63  ? 1226 ALA   A O   1 
ATOM   1329 C CB  . ALA   A 1 189 ? -4.843  -3.060  20.690  1.00 87.37  ? 1226 ALA   A CB  1 
ATOM   1330 N N   . ARG   A 1 190 ? -4.404  0.087   19.297  1.00 88.90  ? 1227 ARG   A N   1 
ATOM   1331 C CA  . ARG   A 1 190 ? -4.868  1.464   19.357  1.00 90.98  ? 1227 ARG   A CA  1 
ATOM   1332 C C   . ARG   A 1 190 ? -5.072  2.009   17.941  1.00 89.47  ? 1227 ARG   A C   1 
ATOM   1333 O O   . ARG   A 1 190 ? -5.400  3.183   17.775  1.00 90.78  ? 1227 ARG   A O   1 
ATOM   1334 C CB  . ARG   A 1 190 ? -3.865  2.326   20.136  1.00 94.10  ? 1227 ARG   A CB  1 
ATOM   1335 C CG  . ARG   A 1 190 ? -4.465  3.156   21.265  1.00 97.92  ? 1227 ARG   A CG  1 
ATOM   1336 C CD  . ARG   A 1 190 ? -5.728  3.935   20.929  1.00 98.32  ? 1227 ARG   A CD  1 
ATOM   1337 N NE  . ARG   A 1 190 ? -5.564  4.890   19.839  1.00 97.49  ? 1227 ARG   A NE  1 
ATOM   1338 C CZ  . ARG   A 1 190 ? -6.545  5.643   19.346  1.00 97.33  ? 1227 ARG   A CZ  1 
ATOM   1339 N NH1 . ARG   A 1 190 ? -6.300  6.486   18.356  1.00 96.67  ? 1227 ARG   A NH1 1 
ATOM   1340 N NH2 . ARG   A 1 190 ? -7.769  5.547   19.841  1.00 98.22  ? 1227 ARG   A NH2 1 
ATOM   1341 N N   . ASN   A 1 191 ? -4.876  1.158   16.923  1.00 87.27  ? 1228 ASN   A N   1 
ATOM   1342 C CA  . ASN   A 1 191 ? -5.038  1.554   15.532  1.00 86.09  ? 1228 ASN   A CA  1 
ATOM   1343 C C   . ASN   A 1 191 ? -6.517  1.547   15.154  1.00 85.39  ? 1228 ASN   A C   1 
ATOM   1344 O O   . ASN   A 1 191 ? -7.002  2.493   14.536  1.00 85.43  ? 1228 ASN   A O   1 
ATOM   1345 C CB  . ASN   A 1 191 ? -4.243  0.650   14.585  1.00 84.90  ? 1228 ASN   A CB  1 
ATOM   1346 C CG  . ASN   A 1 191 ? -2.747  0.741   14.799  1.00 86.12  ? 1228 ASN   A CG  1 
ATOM   1347 O OD1 . ASN   A 1 191 ? -2.173  1.826   14.747  1.00 87.99  ? 1228 ASN   A OD1 1 
ATOM   1348 N ND2 . ASN   A 1 191 ? -2.109  -0.392  15.042  1.00 85.55  ? 1228 ASN   A ND2 1 
ATOM   1349 N N   . MET   A 1 192 ? -7.215  0.460   15.510  1.00 85.00  ? 1229 MET   A N   1 
ATOM   1350 C CA  . MET   A 1 192 ? -8.634  0.311   15.219  1.00 84.99  ? 1229 MET   A CA  1 
ATOM   1351 C C   . MET   A 1 192 ? -9.426  1.384   15.976  1.00 86.48  ? 1229 MET   A C   1 
ATOM   1352 O O   . MET   A 1 192 ? -10.620 1.543   15.655  1.00 86.52  ? 1229 MET   A O   1 
ATOM   1353 C CB  . MET   A 1 192 ? -9.154  -1.076  15.622  1.00 85.48  ? 1229 MET   A CB  1 
ATOM   1354 C CG  . MET   A 1 192 ? -8.881  -1.453  17.073  1.00 86.97  ? 1229 MET   A CG  1 
ATOM   1355 S SD  . MET   A 1 192 ? -9.548  -3.081  17.512  1.00 88.09  ? 1229 MET   A SD  1 
ATOM   1356 C CE  . MET   A 1 192 ? -8.086  -4.101  17.322  1.00 86.15  ? 1229 MET   A CE  1 
ATOM   1357 N N   . GLU   A 1 196 ? -10.480 3.361   12.540  1.00 83.51  ? 1233 GLU   A N   1 
ATOM   1358 C CA  . GLU   A 1 196 ? -10.388 4.306   11.393  1.00 82.89  ? 1233 GLU   A CA  1 
ATOM   1359 C C   . GLU   A 1 196 ? -11.773 4.477   10.771  1.00 82.67  ? 1233 GLU   A C   1 
ATOM   1360 O O   . GLU   A 1 196 ? -12.532 3.515   10.664  1.00 83.13  ? 1233 GLU   A O   1 
ATOM   1361 C CB  . GLU   A 1 196 ? -9.359  3.827   10.362  1.00 82.43  ? 1233 GLU   A CB  1 
ATOM   1362 C CG  . GLU   A 1 196 ? -9.607  2.428   9.808   1.00 82.29  ? 1233 GLU   A CG  1 
ATOM   1363 C CD  . GLU   A 1 196 ? -9.184  1.263   10.690  1.00 82.31  ? 1233 GLU   A CD  1 
ATOM   1364 O OE1 . GLU   A 1 196 ? -8.584  1.508   11.757  1.00 82.57  ? 1233 GLU   A OE1 1 
ATOM   1365 O OE2 . GLU   A 1 196 ? -9.460  0.108   10.307  1.00 82.44  ? 1233 GLU   A OE2 1 
ATOM   1366 N N   . TYR   A 1 197 ? -12.088 5.717   10.373  1.00 82.30  ? 1234 TYR   A N   1 
ATOM   1367 C CA  . TYR   A 1 197 ? -13.371 6.043   9.771   1.00 82.13  ? 1234 TYR   A CA  1 
ATOM   1368 C C   . TYR   A 1 197 ? -13.205 6.175   8.259   1.00 80.93  ? 1234 TYR   A C   1 
ATOM   1369 O O   . TYR   A 1 197 ? -13.887 5.492   7.498   1.00 81.13  ? 1234 TYR   A O   1 
ATOM   1370 C CB  . TYR   A 1 197 ? -13.939 7.328   10.378  1.00 83.26  ? 1234 TYR   A CB  1 
ATOM   1371 C CG  . TYR   A 1 197 ? -14.082 7.307   11.879  1.00 85.07  ? 1234 TYR   A CG  1 
ATOM   1372 C CD1 . TYR   A 1 197 ? -13.465 8.264   12.671  1.00 86.38  ? 1234 TYR   A CD1 1 
ATOM   1373 C CD2 . TYR   A 1 197 ? -14.830 6.327   12.512  1.00 86.31  ? 1234 TYR   A CD2 1 
ATOM   1374 C CE1 . TYR   A 1 197 ? -13.591 8.251   14.051  1.00 88.73  ? 1234 TYR   A CE1 1 
ATOM   1375 C CE2 . TYR   A 1 197 ? -14.965 6.299   13.891  1.00 88.59  ? 1234 TYR   A CE2 1 
ATOM   1376 C CZ  . TYR   A 1 197 ? -14.343 7.264   14.664  1.00 89.80  ? 1234 TYR   A CZ  1 
ATOM   1377 O OH  . TYR   A 1 197 ? -14.472 7.244   16.032  1.00 92.75  ? 1234 TYR   A OH  1 
ATOM   1378 N N   . TYR   A 1 198 ? -12.292 7.063   7.846   1.00 80.15  ? 1235 TYR   A N   1 
ATOM   1379 C CA  . TYR   A 1 198 ? -12.019 7.316   6.440   1.00 79.94  ? 1235 TYR   A CA  1 
ATOM   1380 C C   . TYR   A 1 198 ? -10.699 6.649   6.060   1.00 80.38  ? 1235 TYR   A C   1 
ATOM   1381 O O   . TYR   A 1 198 ? -9.633  7.105   6.470   1.00 80.81  ? 1235 TYR   A O   1 
ATOM   1382 C CB  . TYR   A 1 198 ? -11.979 8.822   6.161   1.00 79.98  ? 1235 TYR   A CB  1 
ATOM   1383 C CG  . TYR   A 1 198 ? -13.239 9.573   6.515   1.00 79.56  ? 1235 TYR   A CG  1 
ATOM   1384 C CD1 . TYR   A 1 198 ? -13.550 9.873   7.832   1.00 79.75  ? 1235 TYR   A CD1 1 
ATOM   1385 C CD2 . TYR   A 1 198 ? -14.127 9.983   5.533   1.00 79.40  ? 1235 TYR   A CD2 1 
ATOM   1386 C CE1 . TYR   A 1 198 ? -14.705 10.564  8.164   1.00 80.09  ? 1235 TYR   A CE1 1 
ATOM   1387 C CE2 . TYR   A 1 198 ? -15.287 10.672  5.847   1.00 79.35  ? 1235 TYR   A CE2 1 
ATOM   1388 C CZ  . TYR   A 1 198 ? -15.578 10.965  7.168   1.00 79.77  ? 1235 TYR   A CZ  1 
ATOM   1389 O OH  . TYR   A 1 198 ? -16.726 11.647  7.489   1.00 80.38  ? 1235 TYR   A OH  1 
ATOM   1390 N N   . SER   A 1 199 ? -10.787 5.566   5.275   1.00 80.95  ? 1236 SER   A N   1 
ATOM   1391 C CA  . SER   A 1 199 ? -9.623  4.792   4.871   1.00 81.96  ? 1236 SER   A CA  1 
ATOM   1392 C C   . SER   A 1 199 ? -9.305  5.048   3.400   1.00 84.18  ? 1236 SER   A C   1 
ATOM   1393 O O   . SER   A 1 199 ? -10.181 5.437   2.630   1.00 84.57  ? 1236 SER   A O   1 
ATOM   1394 C CB  . SER   A 1 199 ? -9.839  3.324   5.133   1.00 81.73  ? 1236 SER   A CB  1 
ATOM   1395 O OG  . SER   A 1 199 ? -9.996  3.076   6.522   1.00 80.32  ? 1236 SER   A OG  1 
ATOM   1396 N N   . VAL   A 1 200 ? -8.040  4.806   3.030   1.00 86.23  ? 1237 VAL   A N   1 
ATOM   1397 C CA  . VAL   A 1 200 ? -7.552  5.028   1.677   1.00 89.41  ? 1237 VAL   A CA  1 
ATOM   1398 C C   . VAL   A 1 200 ? -7.066  3.694   1.108   1.00 91.68  ? 1237 VAL   A C   1 
ATOM   1399 O O   . VAL   A 1 200 ? -5.910  3.318   1.289   1.00 93.06  ? 1237 VAL   A O   1 
ATOM   1400 C CB  . VAL   A 1 200 ? -6.460  6.121   1.641   1.00 90.99  ? 1237 VAL   A CB  1 
ATOM   1401 C CG1 . VAL   A 1 200 ? -5.384  5.916   2.701   1.00 90.69  ? 1237 VAL   A CG1 1 
ATOM   1402 C CG2 . VAL   A 1 200 ? -5.833  6.256   0.260   1.00 94.88  ? 1237 VAL   A CG2 1 
ATOM   1403 N N   . HIS   A 1 201 ? -7.977  2.986   0.425   1.00 92.65  ? 1238 HIS   A N   1 
ATOM   1404 C CA  . HIS   A 1 201 ? -7.690  1.691   -0.175  1.00 95.23  ? 1238 HIS   A CA  1 
ATOM   1405 C C   . HIS   A 1 201 ? -7.171  0.719   0.893   1.00 93.50  ? 1238 HIS   A C   1 
ATOM   1406 O O   . HIS   A 1 201 ? -6.855  -0.427  0.518   1.00 95.46  ? 1238 HIS   A O   1 
ATOM   1407 C CB  . HIS   A 1 201 ? -6.694  1.838   -1.335  1.00 99.41  ? 1238 HIS   A CB  1 
ATOM   1408 C CG  . HIS   A 1 201 ? -7.120  2.795   -2.408  1.00 101.56 ? 1238 HIS   A CG  1 
ATOM   1409 N ND1 . HIS   A 1 201 ? -8.268  2.651   -3.148  1.00 102.76 ? 1238 HIS   A ND1 1 
ATOM   1410 C CD2 . HIS   A 1 201 ? -6.505  3.930   -2.847  1.00 103.11 ? 1238 HIS   A CD2 1 
ATOM   1411 C CE1 . HIS   A 1 201 ? -8.360  3.658   -4.013  1.00 104.56 ? 1238 HIS   A CE1 1 
ATOM   1412 N NE2 . HIS   A 1 201 ? -7.275  4.465   -3.844  1.00 104.84 ? 1238 HIS   A NE2 1 
ATOM   1413 N N   . ALA   A 1 206 ? -2.559  -4.434  11.108  1.00 67.45  ? 1243 ALA   A N   1 
ATOM   1414 C CA  . ALA   A 1 206 ? -3.571  -4.372  10.026  1.00 68.19  ? 1243 ALA   A CA  1 
ATOM   1415 C C   . ALA   A 1 206 ? -4.749  -5.287  10.357  1.00 63.54  ? 1243 ALA   A C   1 
ATOM   1416 O O   . ALA   A 1 206 ? -5.890  -4.832  10.415  1.00 62.57  ? 1243 ALA   A O   1 
ATOM   1417 C CB  . ALA   A 1 206 ? -2.936  -4.741  8.707   1.00 72.18  ? 1243 ALA   A CB  1 
ATOM   1418 N N   . LYS   A 1 207 ? -4.456  -6.574  10.578  1.00 61.21  ? 1244 LYS   A N   1 
ATOM   1419 C CA  . LYS   A 1 207 ? -5.480  -7.582  10.805  1.00 57.83  ? 1244 LYS   A CA  1 
ATOM   1420 C C   . LYS   A 1 207 ? -6.087  -7.420  12.197  1.00 53.87  ? 1244 LYS   A C   1 
ATOM   1421 O O   . LYS   A 1 207 ? -5.383  -7.097  13.152  1.00 53.25  ? 1244 LYS   A O   1 
ATOM   1422 C CB  . LYS   A 1 207 ? -4.898  -8.993  10.650  1.00 57.61  ? 1244 LYS   A CB  1 
ATOM   1423 C CG  . LYS   A 1 207 ? -4.832  -9.526  9.224   1.00 61.10  ? 1244 LYS   A CG  1 
ATOM   1424 C CD  . LYS   A 1 207 ? -3.947  -8.723  8.293   1.00 65.78  ? 1244 LYS   A CD  1 
ATOM   1425 C CE  . LYS   A 1 207 ? -3.904  -9.294  6.892   1.00 69.69  ? 1244 LYS   A CE  1 
ATOM   1426 N NZ  . LYS   A 1 207 ? -3.100  -8.447  5.980   1.00 75.02  ? 1244 LYS   A NZ  1 
ATOM   1427 N N   . LEU   A 1 208 ? -7.403  -7.651  12.288  1.00 51.70  ? 1245 LEU   A N   1 
ATOM   1428 C CA  . LEU   A 1 208 ? -8.092  -7.767  13.563  1.00 48.28  ? 1245 LEU   A CA  1 
ATOM   1429 C C   . LEU   A 1 208 ? -7.952  -9.200  14.068  1.00 46.03  ? 1245 LEU   A C   1 
ATOM   1430 O O   . LEU   A 1 208 ? -8.108  -10.144 13.296  1.00 46.77  ? 1245 LEU   A O   1 
ATOM   1431 C CB  . LEU   A 1 208 ? -9.571  -7.409  13.379  1.00 48.21  ? 1245 LEU   A CB  1 
ATOM   1432 C CG  . LEU   A 1 208 ? -9.870  -5.968  12.967  1.00 50.51  ? 1245 LEU   A CG  1 
ATOM   1433 C CD1 . LEU   A 1 208 ? -11.369 -5.708  12.982  1.00 50.26  ? 1245 LEU   A CD1 1 
ATOM   1434 C CD2 . LEU   A 1 208 ? -9.149  -4.975  13.867  1.00 50.85  ? 1245 LEU   A CD2 1 
ATOM   1435 N N   . PRO   A 1 209 ? -7.670  -9.415  15.374  1.00 43.67  ? 1246 PRO   A N   1 
ATOM   1436 C CA  . PRO   A 1 209 ? -7.580  -10.765 15.932  1.00 42.08  ? 1246 PRO   A CA  1 
ATOM   1437 C C   . PRO   A 1 209 ? -8.967  -11.340 16.213  1.00 40.93  ? 1246 PRO   A C   1 
ATOM   1438 O O   . PRO   A 1 209 ? -9.355  -11.509 17.367  1.00 39.96  ? 1246 PRO   A O   1 
ATOM   1439 C CB  . PRO   A 1 209 ? -6.768  -10.525 17.213  1.00 41.16  ? 1246 PRO   A CB  1 
ATOM   1440 C CG  . PRO   A 1 209 ? -7.219  -9.153  17.668  1.00 41.30  ? 1246 PRO   A CG  1 
ATOM   1441 C CD  . PRO   A 1 209 ? -7.429  -8.373  16.386  1.00 43.20  ? 1246 PRO   A CD  1 
ATOM   1442 N N   . VAL   A 1 210 ? -9.699  -11.652 15.138  1.00 41.81  ? 1247 VAL   A N   1 
ATOM   1443 C CA  . VAL   A 1 210 ? -11.116 -11.972 15.226  1.00 41.65  ? 1247 VAL   A CA  1 
ATOM   1444 C C   . VAL   A 1 210 ? -11.311 -13.323 15.914  1.00 40.89  ? 1247 VAL   A C   1 
ATOM   1445 O O   . VAL   A 1 210 ? -12.330 -13.541 16.567  1.00 40.72  ? 1247 VAL   A O   1 
ATOM   1446 C CB  . VAL   A 1 210 ? -11.786 -11.951 13.837  1.00 44.12  ? 1247 VAL   A CB  1 
ATOM   1447 C CG1 . VAL   A 1 210 ? -11.636 -10.595 13.164  1.00 45.14  ? 1247 VAL   A CG1 1 
ATOM   1448 C CG2 . VAL   A 1 210 ? -11.273 -13.058 12.928  1.00 46.01  ? 1247 VAL   A CG2 1 
ATOM   1449 N N   . LYS   A 1 211 ? -10.331 -14.220 15.761  1.00 40.81  ? 1248 LYS   A N   1 
ATOM   1450 C CA  . LYS   A 1 211 ? -10.429 -15.569 16.294  1.00 40.96  ? 1248 LYS   A CA  1 
ATOM   1451 C C   . LYS   A 1 211 ? -10.023 -15.590 17.768  1.00 38.98  ? 1248 LYS   A C   1 
ATOM   1452 O O   . LYS   A 1 211 ? -10.286 -16.569 18.462  1.00 39.34  ? 1248 LYS   A O   1 
ATOM   1453 C CB  . LYS   A 1 211 ? -9.583  -16.517 15.439  1.00 42.67  ? 1248 LYS   A CB  1 
ATOM   1454 C CG  . LYS   A 1 211 ? -9.986  -16.557 13.971  1.00 45.43  ? 1248 LYS   A CG  1 
ATOM   1455 C CD  . LYS   A 1 211 ? -9.421  -17.728 13.200  1.00 47.96  ? 1248 LYS   A CD  1 
ATOM   1456 C CE  . LYS   A 1 211 ? -9.934  -17.791 11.776  1.00 51.30  ? 1248 LYS   A CE  1 
ATOM   1457 N NZ  . LYS   A 1 211 ? -9.455  -19.004 11.073  1.00 54.51  ? 1248 LYS   A NZ  1 
ATOM   1458 N N   . TRP   A 1 212 ? -9.388  -14.506 18.236  1.00 37.38  ? 1249 TRP   A N   1 
ATOM   1459 C CA  . TRP   A 1 212 ? -9.061  -14.335 19.643  1.00 35.97  ? 1249 TRP   A CA  1 
ATOM   1460 C C   . TRP   A 1 212 ? -10.060 -13.399 20.323  1.00 35.59  ? 1249 TRP   A C   1 
ATOM   1461 O O   . TRP   A 1 212 ? -10.125 -13.356 21.550  1.00 35.45  ? 1249 TRP   A O   1 
ATOM   1462 C CB  . TRP   A 1 212 ? -7.626  -13.815 19.803  1.00 35.55  ? 1249 TRP   A CB  1 
ATOM   1463 C CG  . TRP   A 1 212 ? -6.569  -14.826 19.484  1.00 36.15  ? 1249 TRP   A CG  1 
ATOM   1464 C CD1 . TRP   A 1 212 ? -5.799  -15.511 20.379  1.00 36.03  ? 1249 TRP   A CD1 1 
ATOM   1465 C CD2 . TRP   A 1 212 ? -6.141  -15.253 18.178  1.00 37.47  ? 1249 TRP   A CD2 1 
ATOM   1466 N NE1 . TRP   A 1 212 ? -4.933  -16.342 19.723  1.00 37.09  ? 1249 TRP   A NE1 1 
ATOM   1467 C CE2 . TRP   A 1 212 ? -5.117  -16.206 18.372  1.00 38.00  ? 1249 TRP   A CE2 1 
ATOM   1468 C CE3 . TRP   A 1 212 ? -6.521  -14.933 16.868  1.00 38.63  ? 1249 TRP   A CE3 1 
ATOM   1469 C CZ2 . TRP   A 1 212 ? -4.475  -16.835 17.306  1.00 39.65  ? 1249 TRP   A CZ2 1 
ATOM   1470 C CZ3 . TRP   A 1 212 ? -5.886  -15.555 15.816  1.00 40.38  ? 1249 TRP   A CZ3 1 
ATOM   1471 C CH2 . TRP   A 1 212 ? -4.876  -16.493 16.035  1.00 40.91  ? 1249 TRP   A CH2 1 
ATOM   1472 N N   . MET   A 1 213 ? -10.831 -12.653 19.520  1.00 35.95  ? 1250 MET   A N   1 
ATOM   1473 C CA  . MET   A 1 213 ? -11.723 -11.622 20.029  1.00 35.84  ? 1250 MET   A CA  1 
ATOM   1474 C C   . MET   A 1 213 ? -12.950 -12.260 20.675  1.00 36.36  ? 1250 MET   A C   1 
ATOM   1475 O O   . MET   A 1 213 ? -13.382 -13.340 20.274  1.00 37.19  ? 1250 MET   A O   1 
ATOM   1476 C CB  . MET   A 1 213 ? -12.173 -10.684 18.903  1.00 36.52  ? 1250 MET   A CB  1 
ATOM   1477 C CG  . MET   A 1 213 ? -11.310 -9.445  18.769  1.00 36.53  ? 1250 MET   A CG  1 
ATOM   1478 S SD  . MET   A 1 213 ? -11.502 -8.645  17.158  1.00 38.12  ? 1250 MET   A SD  1 
ATOM   1479 C CE  . MET   A 1 213 ? -12.902 -7.575  17.488  1.00 38.91  ? 1250 MET   A CE  1 
ATOM   1480 N N   . ALA   A 1 214 ? -13.504 -11.563 21.676  1.00 36.36  ? 1251 ALA   A N   1 
ATOM   1481 C CA  . ALA   A 1 214 ? -14.692 -12.014 22.382  1.00 37.57  ? 1251 ALA   A CA  1 
ATOM   1482 C C   . ALA   A 1 214 ? -15.927 -11.750 21.525  1.00 38.78  ? 1251 ALA   A C   1 
ATOM   1483 O O   . ALA   A 1 214 ? -15.860 -11.015 20.542  1.00 38.27  ? 1251 ALA   A O   1 
ATOM   1484 C CB  . ALA   A 1 214 ? -14.790 -11.325 23.722  1.00 37.74  ? 1251 ALA   A CB  1 
ATOM   1485 N N   . LEU   A 1 215 ? -17.053 -12.350 21.927  1.00 40.80  ? 1252 LEU   A N   1 
ATOM   1486 C CA  . LEU   A 1 215 ? -18.279 -12.306 21.146  1.00 42.90  ? 1252 LEU   A CA  1 
ATOM   1487 C C   . LEU   A 1 215 ? -18.771 -10.862 21.048  1.00 42.88  ? 1252 LEU   A C   1 
ATOM   1488 O O   . LEU   A 1 215 ? -19.133 -10.405 19.966  1.00 43.59  ? 1252 LEU   A O   1 
ATOM   1489 C CB  . LEU   A 1 215 ? -19.328 -13.211 21.805  1.00 45.88  ? 1252 LEU   A CB  1 
ATOM   1490 C CG  . LEU   A 1 215 ? -20.304 -13.914 20.859  1.00 49.05  ? 1252 LEU   A CG  1 
ATOM   1491 C CD1 . LEU   A 1 215 ? -21.459 -14.528 21.638  1.00 52.88  ? 1252 LEU   A CD1 1 
ATOM   1492 C CD2 . LEU   A 1 215 ? -20.834 -12.973 19.788  1.00 49.38  ? 1252 LEU   A CD2 1 
ATOM   1493 N N   . GLU   A 1 216 ? -18.770 -10.151 22.183  1.00 42.55  ? 1253 GLU   A N   1 
ATOM   1494 C CA  . GLU   A 1 216 ? -19.246 -8.776  22.233  1.00 42.90  ? 1253 GLU   A CA  1 
ATOM   1495 C C   . GLU   A 1 216 ? -18.252 -7.845  21.538  1.00 41.05  ? 1253 GLU   A C   1 
ATOM   1496 O O   . GLU   A 1 216 ? -18.654 -6.820  20.992  1.00 41.82  ? 1253 GLU   A O   1 
ATOM   1497 C CB  . GLU   A 1 216 ? -19.526 -8.332  23.674  1.00 43.96  ? 1253 GLU   A CB  1 
ATOM   1498 C CG  . GLU   A 1 216 ? -18.299 -8.204  24.570  1.00 42.57  ? 1253 GLU   A CG  1 
ATOM   1499 C CD  . GLU   A 1 216 ? -17.769 -9.493  25.177  1.00 42.27  ? 1253 GLU   A CD  1 
ATOM   1500 O OE1 . GLU   A 1 216 ? -18.298 -10.572 24.839  1.00 43.18  ? 1253 GLU   A OE1 1 
ATOM   1501 O OE2 . GLU   A 1 216 ? -16.832 -9.414  25.997  1.00 41.60  ? 1253 GLU   A OE2 1 
ATOM   1502 N N   . SER   A 1 217 ? -16.962 -8.206  21.559  1.00 39.21  ? 1254 SER   A N   1 
ATOM   1503 C CA  . SER   A 1 217 ? -15.921 -7.409  20.926  1.00 38.32  ? 1254 SER   A CA  1 
ATOM   1504 C C   . SER   A 1 217 ? -16.040 -7.476  19.404  1.00 38.68  ? 1254 SER   A C   1 
ATOM   1505 O O   . SER   A 1 217 ? -15.685 -6.524  18.713  1.00 38.88  ? 1254 SER   A O   1 
ATOM   1506 C CB  . SER   A 1 217 ? -14.549 -7.842  21.382  1.00 37.10  ? 1254 SER   A CB  1 
ATOM   1507 O OG  . SER   A 1 217 ? -14.350 -7.536  22.754  1.00 37.35  ? 1254 SER   A OG  1 
ATOM   1508 N N   . LEU   A 1 218 ? -16.539 -8.608  18.892  1.00 39.23  ? 1255 LEU   A N   1 
ATOM   1509 C CA  . LEU   A 1 218 ? -16.740 -8.789  17.463  1.00 40.57  ? 1255 LEU   A CA  1 
ATOM   1510 C C   . LEU   A 1 218 ? -17.925 -7.953  16.977  1.00 42.68  ? 1255 LEU   A C   1 
ATOM   1511 O O   . LEU   A 1 218 ? -18.016 -7.660  15.788  1.00 44.44  ? 1255 LEU   A O   1 
ATOM   1512 C CB  . LEU   A 1 218 ? -16.967 -10.278 17.171  1.00 41.32  ? 1255 LEU   A CB  1 
ATOM   1513 C CG  . LEU   A 1 218 ? -15.733 -11.174 17.276  1.00 39.87  ? 1255 LEU   A CG  1 
ATOM   1514 C CD1 . LEU   A 1 218 ? -16.112 -12.637 17.099  1.00 41.29  ? 1255 LEU   A CD1 1 
ATOM   1515 C CD2 . LEU   A 1 218 ? -14.677 -10.775 16.256  1.00 39.65  ? 1255 LEU   A CD2 1 
ATOM   1516 N N   . GLN   A 1 219 ? -18.827 -7.582  17.897  1.00 43.17  ? 1256 GLN   A N   1 
ATOM   1517 C CA  . GLN   A 1 219 ? -20.042 -6.859  17.550  1.00 45.38  ? 1256 GLN   A CA  1 
ATOM   1518 C C   . GLN   A 1 219 ? -19.895 -5.360  17.811  1.00 45.32  ? 1256 GLN   A C   1 
ATOM   1519 O O   . GLN   A 1 219 ? -20.498 -4.557  17.102  1.00 47.03  ? 1256 GLN   A O   1 
ATOM   1520 C CB  . GLN   A 1 219 ? -21.224 -7.412  18.349  1.00 47.02  ? 1256 GLN   A CB  1 
ATOM   1521 C CG  . GLN   A 1 219 ? -21.495 -8.888  18.096  1.00 48.13  ? 1256 GLN   A CG  1 
ATOM   1522 C CD  . GLN   A 1 219 ? -22.650 -9.400  18.919  1.00 50.54  ? 1256 GLN   A CD  1 
ATOM   1523 O OE1 . GLN   A 1 219 ? -22.472 -10.153 19.874  1.00 50.20  ? 1256 GLN   A OE1 1 
ATOM   1524 N NE2 . GLN   A 1 219 ? -23.851 -8.977  18.563  1.00 53.58  ? 1256 GLN   A NE2 1 
ATOM   1525 N N   . THR   A 1 220 ? -19.115 -4.987  18.837  1.00 43.82  ? 1257 THR   A N   1 
ATOM   1526 C CA  . THR   A 1 220 ? -19.072 -3.611  19.314  1.00 44.49  ? 1257 THR   A CA  1 
ATOM   1527 C C   . THR   A 1 220 ? -17.676 -2.996  19.188  1.00 43.62  ? 1257 THR   A C   1 
ATOM   1528 O O   . THR   A 1 220 ? -17.550 -1.773  19.219  1.00 44.88  ? 1257 THR   A O   1 
ATOM   1529 C CB  . THR   A 1 220 ? -19.543 -3.533  20.772  1.00 44.89  ? 1257 THR   A CB  1 
ATOM   1530 O OG1 . THR   A 1 220 ? -18.617 -4.256  21.583  1.00 43.07  ? 1257 THR   A OG1 1 
ATOM   1531 C CG2 . THR   A 1 220 ? -20.937 -4.089  20.968  1.00 46.54  ? 1257 THR   A CG2 1 
ATOM   1532 N N   . GLN   A 1 221 ? -16.641 -3.838  19.054  1.00 41.90  ? 1258 GLN   A N   1 
ATOM   1533 C CA  . GLN   A 1 221 ? -15.250 -3.416  19.164  1.00 41.48  ? 1258 GLN   A CA  1 
ATOM   1534 C C   . GLN   A 1 221 ? -15.025 -2.705  20.499  1.00 41.86  ? 1258 GLN   A C   1 
ATOM   1535 O O   . GLN   A 1 221 ? -14.303 -1.712  20.564  1.00 43.05  ? 1258 GLN   A O   1 
ATOM   1536 C CB  . GLN   A 1 221 ? -14.834 -2.527  17.988  1.00 43.26  ? 1258 GLN   A CB  1 
ATOM   1537 C CG  . GLN   A 1 221 ? -14.807 -3.250  16.649  1.00 43.46  ? 1258 GLN   A CG  1 
ATOM   1538 C CD  . GLN   A 1 221 ? -14.134 -2.442  15.565  1.00 45.64  ? 1258 GLN   A CD  1 
ATOM   1539 O OE1 . GLN   A 1 221 ? -13.710 -1.307  15.774  1.00 47.11  ? 1258 GLN   A OE1 1 
ATOM   1540 N NE2 . GLN   A 1 221 ? -14.024 -3.031  14.385  1.00 46.39  ? 1258 GLN   A NE2 1 
ATOM   1541 N N   . LYS   A 1 222 ? -15.644 -3.235  21.561  1.00 41.45  ? 1259 LYS   A N   1 
ATOM   1542 C CA  . LYS   A 1 222 ? -15.436 -2.737  22.910  1.00 42.47  ? 1259 LYS   A CA  1 
ATOM   1543 C C   . LYS   A 1 222 ? -14.712 -3.813  23.711  1.00 40.99  ? 1259 LYS   A C   1 
ATOM   1544 O O   . LYS   A 1 222 ? -15.150 -4.962  23.746  1.00 39.72  ? 1259 LYS   A O   1 
ATOM   1545 C CB  . LYS   A 1 222 ? -16.766 -2.347  23.561  1.00 44.31  ? 1259 LYS   A CB  1 
ATOM   1546 C CG  . LYS   A 1 222 ? -17.449 -1.133  22.944  1.00 46.50  ? 1259 LYS   A CG  1 
ATOM   1547 C CD  . LYS   A 1 222 ? -18.586 -0.585  23.779  1.00 48.82  ? 1259 LYS   A CD  1 
ATOM   1548 C CE  . LYS   A 1 222 ? -19.119 0.731   23.255  1.00 51.37  ? 1259 LYS   A CE  1 
ATOM   1549 N NZ  . LYS   A 1 222 ? -20.125 1.318   24.172  1.00 54.07  ? 1259 LYS   A NZ  1 
ATOM   1550 N N   . PHE   A 1 223 ? -13.602 -3.419  24.344  1.00 41.67  ? 1260 PHE   A N   1 
ATOM   1551 C CA  . PHE   A 1 223 ? -12.715 -4.351  25.019  1.00 40.80  ? 1260 PHE   A CA  1 
ATOM   1552 C C   . PHE   A 1 223 ? -12.697 -4.043  26.513  1.00 42.50  ? 1260 PHE   A C   1 
ATOM   1553 O O   . PHE   A 1 223 ? -12.680 -2.880  26.910  1.00 44.86  ? 1260 PHE   A O   1 
ATOM   1554 C CB  . PHE   A 1 223 ? -11.311 -4.282  24.413  1.00 40.79  ? 1260 PHE   A CB  1 
ATOM   1555 C CG  . PHE   A 1 223 ? -11.261 -4.502  22.921  1.00 40.10  ? 1260 PHE   A CG  1 
ATOM   1556 C CD1 . PHE   A 1 223 ? -11.667 -3.508  22.041  1.00 41.37  ? 1260 PHE   A CD1 1 
ATOM   1557 C CD2 . PHE   A 1 223 ? -10.829 -5.710  22.394  1.00 38.70  ? 1260 PHE   A CD2 1 
ATOM   1558 C CE1 . PHE   A 1 223 ? -11.627 -3.712  20.670  1.00 41.15  ? 1260 PHE   A CE1 1 
ATOM   1559 C CE2 . PHE   A 1 223 ? -10.792 -5.914  21.022  1.00 38.47  ? 1260 PHE   A CE2 1 
ATOM   1560 C CZ  . PHE   A 1 223 ? -11.190 -4.915  20.163  1.00 39.79  ? 1260 PHE   A CZ  1 
ATOM   1561 N N   . THR   A 1 224 ? -12.703 -5.108  27.323  1.00 41.91  ? 1261 THR   A N   1 
ATOM   1562 C CA  . THR   A 1 224 ? -12.653 -5.010  28.772  1.00 43.97  ? 1261 THR   A CA  1 
ATOM   1563 C C   . THR   A 1 224 ? -11.684 -6.069  29.293  1.00 43.24  ? 1261 THR   A C   1 
ATOM   1564 O O   . THR   A 1 224 ? -11.014 -6.735  28.507  1.00 41.18  ? 1261 THR   A O   1 
ATOM   1565 C CB  . THR   A 1 224 ? -14.057 -5.163  29.376  1.00 45.26  ? 1261 THR   A CB  1 
ATOM   1566 O OG1 . THR   A 1 224 ? -14.511 -6.494  29.129  1.00 43.86  ? 1261 THR   A OG1 1 
ATOM   1567 C CG2 . THR   A 1 224 ? -15.053 -4.174  28.811  1.00 46.06  ? 1261 THR   A CG2 1 
ATOM   1568 N N   . THR   A 1 225 ? -11.614 -6.213  30.621  1.00 45.43  ? 1262 THR   A N   1 
ATOM   1569 C CA  . THR   A 1 225 ? -10.860 -7.291  31.240  1.00 45.47  ? 1262 THR   A CA  1 
ATOM   1570 C C   . THR   A 1 225 ? -11.532 -8.629  30.929  1.00 43.81  ? 1262 THR   A C   1 
ATOM   1571 O O   . THR   A 1 225 ? -10.859 -9.654  30.838  1.00 42.71  ? 1262 THR   A O   1 
ATOM   1572 C CB  . THR   A 1 225 ? -10.725 -7.068  32.751  1.00 49.19  ? 1262 THR   A CB  1 
ATOM   1573 O OG1 . THR   A 1 225 ? -10.201 -5.755  32.960  1.00 51.52  ? 1262 THR   A OG1 1 
ATOM   1574 C CG2 . THR   A 1 225 ? -9.830  -8.084  33.426  1.00 49.81  ? 1262 THR   A CG2 1 
ATOM   1575 N N   . LYS   A 1 226 ? -12.861 -8.602  30.768  1.00 44.07  ? 1263 LYS   A N   1 
ATOM   1576 C CA  . LYS   A 1 226 ? -13.643 -9.795  30.486  1.00 43.65  ? 1263 LYS   A CA  1 
ATOM   1577 C C   . LYS   A 1 226 ? -13.444 -10.242 29.038  1.00 40.82  ? 1263 LYS   A C   1 
ATOM   1578 O O   . LYS   A 1 226 ? -13.615 -11.420 28.731  1.00 40.40  ? 1263 LYS   A O   1 
ATOM   1579 C CB  . LYS   A 1 226 ? -15.126 -9.533  30.771  1.00 45.84  ? 1263 LYS   A CB  1 
ATOM   1580 C CG  . LYS   A 1 226 ? -15.460 -9.177  32.215  1.00 49.44  ? 1263 LYS   A CG  1 
ATOM   1581 C CD  . LYS   A 1 226 ? -15.143 -10.277 33.208  1.00 51.33  ? 1263 LYS   A CD  1 
ATOM   1582 C CE  . LYS   A 1 226 ? -15.598 -9.955  34.616  1.00 55.64  ? 1263 LYS   A CE  1 
ATOM   1583 N NZ  . LYS   A 1 226 ? -15.236 -11.033 35.566  1.00 57.95  ? 1263 LYS   A NZ  1 
ATOM   1584 N N   . SER   A 1 227 ? -13.103 -9.298  28.150  1.00 39.41  ? 1264 SER   A N   1 
ATOM   1585 C CA  . SER   A 1 227 ? -12.799 -9.623  26.764  1.00 37.45  ? 1264 SER   A CA  1 
ATOM   1586 C C   . SER   A 1 227 ? -11.407 -10.245 26.659  1.00 36.44  ? 1264 SER   A C   1 
ATOM   1587 O O   . SER   A 1 227 ? -11.153 -11.039 25.756  1.00 35.62  ? 1264 SER   A O   1 
ATOM   1588 C CB  . SER   A 1 227 ? -12.923 -8.413  25.874  1.00 37.17  ? 1264 SER   A CB  1 
ATOM   1589 O OG  . SER   A 1 227 ? -11.913 -7.459  26.164  1.00 37.78  ? 1264 SER   A OG  1 
ATOM   1590 N N   . ASP   A 1 228 ? -10.512 -9.865  27.581  1.00 37.21  ? 1265 ASP   A N   1 
ATOM   1591 C CA  . ASP   A 1 228 ? -9.176  -10.436 27.652  1.00 36.89  ? 1265 ASP   A CA  1 
ATOM   1592 C C   . ASP   A 1 228 ? -9.248  -11.867 28.180  1.00 36.97  ? 1265 ASP   A C   1 
ATOM   1593 O O   . ASP   A 1 228 ? -8.394  -12.688 27.853  1.00 36.14  ? 1265 ASP   A O   1 
ATOM   1594 C CB  . ASP   A 1 228 ? -8.250  -9.586  28.528  1.00 38.81  ? 1265 ASP   A CB  1 
ATOM   1595 C CG  . ASP   A 1 228 ? -7.876  -8.242  27.924  1.00 39.51  ? 1265 ASP   A CG  1 
ATOM   1596 O OD1 . ASP   A 1 228 ? -8.292  -7.972  26.776  1.00 38.51  ? 1265 ASP   A OD1 1 
ATOM   1597 O OD2 . ASP   A 1 228 ? -7.165  -7.476  28.605  1.00 41.62  ? 1265 ASP   A OD2 1 
ATOM   1598 N N   . VAL   A 1 229 ? -10.260 -12.148 29.011  1.00 38.41  ? 1266 VAL   A N   1 
ATOM   1599 C CA  . VAL   A 1 229 ? -10.475 -13.483 29.549  1.00 39.58  ? 1266 VAL   A CA  1 
ATOM   1600 C C   . VAL   A 1 229 ? -10.804 -14.437 28.401  1.00 38.50  ? 1266 VAL   A C   1 
ATOM   1601 O O   . VAL   A 1 229 ? -10.273 -15.544 28.348  1.00 38.79  ? 1266 VAL   A O   1 
ATOM   1602 C CB  . VAL   A 1 229 ? -11.575 -13.483 30.631  1.00 42.07  ? 1266 VAL   A CB  1 
ATOM   1603 C CG1 . VAL   A 1 229 ? -12.010 -14.894 31.007  1.00 43.92  ? 1266 VAL   A CG1 1 
ATOM   1604 C CG2 . VAL   A 1 229 ? -11.146 -12.707 31.869  1.00 43.90  ? 1266 VAL   A CG2 1 
ATOM   1605 N N   . TRP   A 1 230 ? -11.681 -13.997 27.488  1.00 37.73  ? 1267 TRP   A N   1 
ATOM   1606 C CA  . TRP   A 1 230 ? -12.028 -14.776 26.310  1.00 37.32  ? 1267 TRP   A CA  1 
ATOM   1607 C C   . TRP   A 1 230 ? -10.768 -15.101 25.511  1.00 35.65  ? 1267 TRP   A C   1 
ATOM   1608 O O   . TRP   A 1 230 ? -10.550 -16.251 25.137  1.00 36.03  ? 1267 TRP   A O   1 
ATOM   1609 C CB  . TRP   A 1 230 ? -13.062 -14.031 25.453  1.00 37.40  ? 1267 TRP   A CB  1 
ATOM   1610 C CG  . TRP   A 1 230 ? -13.534 -14.796 24.253  1.00 38.10  ? 1267 TRP   A CG  1 
ATOM   1611 C CD1 . TRP   A 1 230 ? -12.804 -15.140 23.151  1.00 37.31  ? 1267 TRP   A CD1 1 
ATOM   1612 C CD2 . TRP   A 1 230 ? -14.857 -15.317 24.032  1.00 40.46  ? 1267 TRP   A CD2 1 
ATOM   1613 N NE1 . TRP   A 1 230 ? -13.579 -15.836 22.263  1.00 38.86  ? 1267 TRP   A NE1 1 
ATOM   1614 C CE2 . TRP   A 1 230 ? -14.844 -15.960 22.775  1.00 40.84  ? 1267 TRP   A CE2 1 
ATOM   1615 C CE3 . TRP   A 1 230 ? -16.048 -15.299 24.767  1.00 42.82  ? 1267 TRP   A CE3 1 
ATOM   1616 C CZ2 . TRP   A 1 230 ? -15.975 -16.580 22.246  1.00 43.53  ? 1267 TRP   A CZ2 1 
ATOM   1617 C CZ3 . TRP   A 1 230 ? -17.165 -15.915 24.245  1.00 45.44  ? 1267 TRP   A CZ3 1 
ATOM   1618 C CH2 . TRP   A 1 230 ? -17.126 -16.545 23.000  1.00 45.84  ? 1267 TRP   A CH2 1 
ATOM   1619 N N   . SER   A 1 231 ? -9.950  -14.072 25.257  1.00 34.31  ? 1268 SER   A N   1 
ATOM   1620 C CA  . SER   A 1 231 ? -8.714  -14.218 24.503  1.00 33.44  ? 1268 SER   A CA  1 
ATOM   1621 C C   . SER   A 1 231 ? -7.754  -15.171 25.216  1.00 34.06  ? 1268 SER   A C   1 
ATOM   1622 O O   . SER   A 1 231 ? -7.044  -15.935 24.564  1.00 34.03  ? 1268 SER   A O   1 
ATOM   1623 C CB  . SER   A 1 231 ? -8.072  -12.875 24.266  1.00 32.98  ? 1268 SER   A CB  1 
ATOM   1624 O OG  . SER   A 1 231 ? -8.948  -12.009 23.558  1.00 32.73  ? 1268 SER   A OG  1 
ATOM   1625 N N   . PHE   A 1 232 ? -7.736  -15.115 26.555  1.00 34.96  ? 1269 PHE   A N   1 
ATOM   1626 C CA  . PHE   A 1 232 ? -6.884  -15.981 27.354  1.00 35.92  ? 1269 PHE   A CA  1 
ATOM   1627 C C   . PHE   A 1 232 ? -7.299  -17.440 27.174  1.00 36.86  ? 1269 PHE   A C   1 
ATOM   1628 O O   . PHE   A 1 232 ? -6.445  -18.320 27.101  1.00 37.66  ? 1269 PHE   A O   1 
ATOM   1629 C CB  . PHE   A 1 232 ? -6.935  -15.588 28.832  1.00 37.46  ? 1269 PHE   A CB  1 
ATOM   1630 C CG  . PHE   A 1 232 ? -6.166  -16.512 29.742  1.00 39.23  ? 1269 PHE   A CG  1 
ATOM   1631 C CD1 . PHE   A 1 232 ? -4.780  -16.549 29.710  1.00 39.45  ? 1269 PHE   A CD1 1 
ATOM   1632 C CD2 . PHE   A 1 232 ? -6.829  -17.368 30.608  1.00 41.22  ? 1269 PHE   A CD2 1 
ATOM   1633 C CE1 . PHE   A 1 232 ? -4.074  -17.406 30.541  1.00 41.40  ? 1269 PHE   A CE1 1 
ATOM   1634 C CE2 . PHE   A 1 232 ? -6.122  -18.225 31.438  1.00 43.31  ? 1269 PHE   A CE2 1 
ATOM   1635 C CZ  . PHE   A 1 232 ? -4.747  -18.243 31.403  1.00 43.28  ? 1269 PHE   A CZ  1 
ATOM   1636 N N   . GLY   A 1 233 ? -8.614  -17.683 27.114  1.00 37.42  ? 1270 GLY   A N   1 
ATOM   1637 C CA  . GLY   A 1 233 ? -9.143  -19.012 26.849  1.00 38.86  ? 1270 GLY   A CA  1 
ATOM   1638 C C   . GLY   A 1 233 ? -8.550  -19.617 25.578  1.00 38.11  ? 1270 GLY   A C   1 
ATOM   1639 O O   . GLY   A 1 233 ? -8.186  -20.791 25.559  1.00 39.57  ? 1270 GLY   A O   1 
ATOM   1640 N N   . VAL   A 1 234 ? -8.453  -18.794 24.526  1.00 36.21  ? 1271 VAL   A N   1 
ATOM   1641 C CA  . VAL   A 1 234 ? -7.891  -19.212 23.252  1.00 36.10  ? 1271 VAL   A CA  1 
ATOM   1642 C C   . VAL   A 1 234 ? -6.387  -19.435 23.413  1.00 35.84  ? 1271 VAL   A C   1 
ATOM   1643 O O   . VAL   A 1 234 ? -5.829  -20.350 22.814  1.00 36.77  ? 1271 VAL   A O   1 
ATOM   1644 C CB  . VAL   A 1 234 ? -8.188  -18.182 22.142  1.00 35.04  ? 1271 VAL   A CB  1 
ATOM   1645 C CG1 . VAL   A 1 234 ? -7.530  -18.564 20.823  1.00 35.57  ? 1271 VAL   A CG1 1 
ATOM   1646 C CG2 . VAL   A 1 234 ? -9.684  -17.969 21.956  1.00 35.60  ? 1271 VAL   A CG2 1 
ATOM   1647 N N   . LEU   A 1 235 ? -5.744  -18.586 24.225  1.00 34.96  ? 1272 LEU   A N   1 
ATOM   1648 C CA  . LEU   A 1 235 ? -4.311  -18.668 24.462  1.00 35.27  ? 1272 LEU   A CA  1 
ATOM   1649 C C   . LEU   A 1 235 ? -3.967  -20.017 25.095  1.00 36.95  ? 1272 LEU   A C   1 
ATOM   1650 O O   . LEU   A 1 235 ? -2.965  -20.629 24.733  1.00 37.68  ? 1272 LEU   A O   1 
ATOM   1651 C CB  . LEU   A 1 235 ? -3.888  -17.490 25.347  1.00 34.91  ? 1272 LEU   A CB  1 
ATOM   1652 C CG  . LEU   A 1 235 ? -2.388  -17.194 25.403  1.00 35.83  ? 1272 LEU   A CG  1 
ATOM   1653 C CD1 . LEU   A 1 235 ? -2.140  -15.796 25.948  1.00 36.13  ? 1272 LEU   A CD1 1 
ATOM   1654 C CD2 . LEU   A 1 235 ? -1.646  -18.226 26.244  1.00 37.47  ? 1272 LEU   A CD2 1 
ATOM   1655 N N   . LEU   A 1 236 ? -4.805  -20.476 26.033  1.00 38.04  ? 1273 LEU   A N   1 
ATOM   1656 C CA  . LEU   A 1 236 ? -4.644  -21.792 26.634  1.00 40.43  ? 1273 LEU   A CA  1 
ATOM   1657 C C   . LEU   A 1 236 ? -4.779  -22.871 25.561  1.00 41.52  ? 1273 LEU   A C   1 
ATOM   1658 O O   . LEU   A 1 236 ? -4.027  -23.842 25.559  1.00 43.02  ? 1273 LEU   A O   1 
ATOM   1659 C CB  . LEU   A 1 236 ? -5.697  -21.986 27.731  1.00 42.09  ? 1273 LEU   A CB  1 
ATOM   1660 C CG  . LEU   A 1 236 ? -5.521  -21.141 28.993  1.00 42.32  ? 1273 LEU   A CG  1 
ATOM   1661 C CD1 . LEU   A 1 236 ? -6.616  -21.452 30.003  1.00 44.63  ? 1273 LEU   A CD1 1 
ATOM   1662 C CD2 . LEU   A 1 236 ? -4.147  -21.360 29.613  1.00 43.30  ? 1273 LEU   A CD2 1 
ATOM   1663 N N   . TRP   A 1 237 ? -5.750  -22.686 24.657  1.00 41.23  ? 1274 TRP   A N   1 
ATOM   1664 C CA  . TRP   A 1 237 ? -6.016  -23.634 23.587  1.00 43.09  ? 1274 TRP   A CA  1 
ATOM   1665 C C   . TRP   A 1 237 ? -4.830  -23.703 22.625  1.00 42.81  ? 1274 TRP   A C   1 
ATOM   1666 O O   . TRP   A 1 237 ? -4.549  -24.765 22.074  1.00 44.96  ? 1274 TRP   A O   1 
ATOM   1667 C CB  . TRP   A 1 237 ? -7.327  -23.273 22.873  1.00 43.20  ? 1274 TRP   A CB  1 
ATOM   1668 C CG  . TRP   A 1 237 ? -7.725  -24.215 21.777  1.00 45.87  ? 1274 TRP   A CG  1 
ATOM   1669 C CD1 . TRP   A 1 237 ? -8.626  -25.236 21.859  1.00 49.27  ? 1274 TRP   A CD1 1 
ATOM   1670 C CD2 . TRP   A 1 237 ? -7.268  -24.194 20.412  1.00 46.09  ? 1274 TRP   A CD2 1 
ATOM   1671 N NE1 . TRP   A 1 237 ? -8.743  -25.867 20.649  1.00 51.59  ? 1274 TRP   A NE1 1 
ATOM   1672 C CE2 . TRP   A 1 237 ? -7.925  -25.249 19.742  1.00 49.58  ? 1274 TRP   A CE2 1 
ATOM   1673 C CE3 . TRP   A 1 237 ? -6.366  -23.400 19.694  1.00 44.28  ? 1274 TRP   A CE3 1 
ATOM   1674 C CZ2 . TRP   A 1 237 ? -7.705  -25.525 18.392  1.00 51.20  ? 1274 TRP   A CZ2 1 
ATOM   1675 C CZ3 . TRP   A 1 237 ? -6.149  -23.674 18.361  1.00 45.83  ? 1274 TRP   A CZ3 1 
ATOM   1676 C CH2 . TRP   A 1 237 ? -6.812  -24.722 17.721  1.00 49.22  ? 1274 TRP   A CH2 1 
ATOM   1677 N N   . GLU   A 1 238 ? -4.140  -22.571 22.432  1.00 40.81  ? 1275 GLU   A N   1 
ATOM   1678 C CA  . GLU   A 1 238 ? -2.924  -22.536 21.633  1.00 41.19  ? 1275 GLU   A CA  1 
ATOM   1679 C C   . GLU   A 1 238 ? -1.848  -23.400 22.287  1.00 42.73  ? 1275 GLU   A C   1 
ATOM   1680 O O   . GLU   A 1 238 ? -1.227  -24.226 21.622  1.00 44.46  ? 1275 GLU   A O   1 
ATOM   1681 C CB  . GLU   A 1 238 ? -2.400  -21.107 21.477  1.00 39.57  ? 1275 GLU   A CB  1 
ATOM   1682 C CG  . GLU   A 1 238 ? -3.224  -20.242 20.544  1.00 38.68  ? 1275 GLU   A CG  1 
ATOM   1683 C CD  . GLU   A 1 238 ? -2.653  -18.848 20.345  1.00 37.97  ? 1275 GLU   A CD  1 
ATOM   1684 O OE1 . GLU   A 1 238 ? -2.308  -18.509 19.197  1.00 38.79  ? 1275 GLU   A OE1 1 
ATOM   1685 O OE2 . GLU   A 1 238 ? -2.548  -18.107 21.343  1.00 37.37  ? 1275 GLU   A OE2 1 
ATOM   1686 N N   . LEU   A 1 239 ? -1.636  -23.186 23.592  1.00 42.53  ? 1276 LEU   A N   1 
ATOM   1687 C CA  . LEU   A 1 239 ? -0.612  -23.890 24.350  1.00 44.38  ? 1276 LEU   A CA  1 
ATOM   1688 C C   . LEU   A 1 239 ? -0.837  -25.399 24.281  1.00 47.15  ? 1276 LEU   A C   1 
ATOM   1689 O O   . LEU   A 1 239 ? 0.108   -26.155 24.064  1.00 49.10  ? 1276 LEU   A O   1 
ATOM   1690 C CB  . LEU   A 1 239 ? -0.640  -23.399 25.801  1.00 44.11  ? 1276 LEU   A CB  1 
ATOM   1691 C CG  . LEU   A 1 239 ? -0.060  -22.006 26.038  1.00 42.82  ? 1276 LEU   A CG  1 
ATOM   1692 C CD1 . LEU   A 1 239 ? -0.283  -21.564 27.476  1.00 43.25  ? 1276 LEU   A CD1 1 
ATOM   1693 C CD2 . LEU   A 1 239 ? 1.424   -21.967 25.695  1.00 43.97  ? 1276 LEU   A CD2 1 
ATOM   1694 N N   . MET   A 1 240 ? -2.095  -25.823 24.451  1.00 47.87  ? 1277 MET   A N   1 
ATOM   1695 C CA  . MET   A 1 240 ? -2.430  -27.234 24.570  1.00 51.21  ? 1277 MET   A CA  1 
ATOM   1696 C C   . MET   A 1 240 ? -2.386  -27.922 23.205  1.00 52.63  ? 1277 MET   A C   1 
ATOM   1697 O O   . MET   A 1 240 ? -2.380  -29.150 23.141  1.00 56.01  ? 1277 MET   A O   1 
ATOM   1698 C CB  . MET   A 1 240 ? -3.824  -27.408 25.182  1.00 52.47  ? 1277 MET   A CB  1 
ATOM   1699 C CG  . MET   A 1 240 ? -3.888  -27.087 26.669  1.00 52.74  ? 1277 MET   A CG  1 
ATOM   1700 S SD  . MET   A 1 240 ? -2.772  -28.093 27.687  1.00 56.09  ? 1277 MET   A SD  1 
ATOM   1701 C CE  . MET   A 1 240 ? -1.443  -26.925 27.976  1.00 53.22  ? 1277 MET   A CE  1 
ATOM   1702 N N   . THR   A 1 241 ? -2.361  -27.131 22.122  1.00 50.64  ? 1278 THR   A N   1 
ATOM   1703 C CA  . THR   A 1 241 ? -2.272  -27.659 20.769  1.00 52.47  ? 1278 THR   A CA  1 
ATOM   1704 C C   . THR   A 1 241 ? -0.908  -27.342 20.156  1.00 52.25  ? 1278 THR   A C   1 
ATOM   1705 O O   . THR   A 1 241 ? -0.742  -27.443 18.941  1.00 53.57  ? 1278 THR   A O   1 
ATOM   1706 C CB  . THR   A 1 241 ? -3.394  -27.095 19.887  1.00 51.69  ? 1278 THR   A CB  1 
ATOM   1707 O OG1 . THR   A 1 241 ? -3.247  -25.675 19.838  1.00 48.13  ? 1278 THR   A OG1 1 
ATOM   1708 C CG2 . THR   A 1 241 ? -4.778  -27.450 20.385  1.00 52.88  ? 1278 THR   A CG2 1 
ATOM   1709 N N   . ARG   A 1 242 ? 0.065   -26.974 21.000  1.00 53.60  ? 1279 ARG   A N   1 
ATOM   1710 C CA  . ARG   A 1 242 ? 1.385   -26.557 20.549  1.00 55.43  ? 1279 ARG   A CA  1 
ATOM   1711 C C   . ARG   A 1 242 ? 1.248   -25.560 19.397  1.00 54.70  ? 1279 ARG   A C   1 
ATOM   1712 O O   . ARG   A 1 242 ? 1.827   -25.751 18.329  1.00 56.94  ? 1279 ARG   A O   1 
ATOM   1713 C CB  . ARG   A 1 242 ? 2.232   -27.773 20.156  1.00 59.57  ? 1279 ARG   A CB  1 
ATOM   1714 C CG  . ARG   A 1 242 ? 2.735   -28.589 21.339  1.00 61.28  ? 1279 ARG   A CG  1 
ATOM   1715 C CD  . ARG   A 1 242 ? 3.700   -29.679 20.910  1.00 65.98  ? 1279 ARG   A CD  1 
ATOM   1716 N NE  . ARG   A 1 242 ? 4.427   -30.269 22.027  1.00 68.14  ? 1279 ARG   A NE  1 
ATOM   1717 C CZ  . ARG   A 1 242 ? 3.883   -31.020 22.979  1.00 68.37  ? 1279 ARG   A CZ  1 
ATOM   1718 N NH1 . ARG   A 1 242 ? 4.623   -31.446 23.987  1.00 70.34  ? 1279 ARG   A NH1 1 
ATOM   1719 N NH2 . ARG   A 1 242 ? 2.602   -31.346 22.922  1.00 66.94  ? 1279 ARG   A NH2 1 
ATOM   1720 N N   . GLY   A 1 243 ? 0.461   -24.504 19.635  1.00 51.80  ? 1280 GLY   A N   1 
ATOM   1721 C CA  . GLY   A 1 243 ? 0.352   -23.377 18.722  1.00 51.10  ? 1280 GLY   A CA  1 
ATOM   1722 C C   . GLY   A 1 243 ? -0.353  -23.740 17.418  1.00 51.85  ? 1280 GLY   A C   1 
ATOM   1723 O O   . GLY   A 1 243 ? 0.186   -23.509 16.337  1.00 53.65  ? 1280 GLY   A O   1 
ATOM   1724 N N   . ALA   A 1 244 ? -1.562  -24.300 17.532  1.00 50.87  ? 1281 ALA   A N   1 
ATOM   1725 C CA  . ALA   A 1 244 ? -2.387  -24.588 16.370  1.00 51.86  ? 1281 ALA   A CA  1 
ATOM   1726 C C   . ALA   A 1 244 ? -3.162  -23.332 15.981  1.00 50.10  ? 1281 ALA   A C   1 
ATOM   1727 O O   . ALA   A 1 244 ? -3.378  -22.456 16.817  1.00 47.74  ? 1281 ALA   A O   1 
ATOM   1728 C CB  . ALA   A 1 244 ? -3.314  -25.740 16.667  1.00 52.22  ? 1281 ALA   A CB  1 
ATOM   1729 N N   . PRO   A 1 245 ? -3.588  -23.193 14.703  1.00 51.63  ? 1282 PRO   A N   1 
ATOM   1730 C CA  . PRO   A 1 245 ? -4.429  -22.070 14.289  1.00 50.48  ? 1282 PRO   A CA  1 
ATOM   1731 C C   . PRO   A 1 245 ? -5.870  -22.257 14.762  1.00 49.34  ? 1282 PRO   A C   1 
ATOM   1732 O O   . PRO   A 1 245 ? -6.506  -23.250 14.413  1.00 50.61  ? 1282 PRO   A O   1 
ATOM   1733 C CB  . PRO   A 1 245 ? -4.332  -22.099 12.757  1.00 52.88  ? 1282 PRO   A CB  1 
ATOM   1734 C CG  . PRO   A 1 245 ? -4.089  -23.558 12.429  1.00 55.36  ? 1282 PRO   A CG  1 
ATOM   1735 C CD  . PRO   A 1 245 ? -3.272  -24.098 13.587  1.00 54.88  ? 1282 PRO   A CD  1 
ATOM   1736 N N   . PRO   A 1 246 ? -6.425  -21.329 15.578  1.00 47.47  ? 1283 PRO   A N   1 
ATOM   1737 C CA  . PRO   A 1 246 ? -7.808  -21.443 16.044  1.00 46.75  ? 1283 PRO   A CA  1 
ATOM   1738 C C   . PRO   A 1 246 ? -8.809  -21.476 14.893  1.00 48.30  ? 1283 PRO   A C   1 
ATOM   1739 O O   . PRO   A 1 246 ? -8.607  -20.809 13.879  1.00 48.98  ? 1283 PRO   A O   1 
ATOM   1740 C CB  . PRO   A 1 246 ? -8.032  -20.180 16.891  1.00 44.69  ? 1283 PRO   A CB  1 
ATOM   1741 C CG  . PRO   A 1 246 ? -6.639  -19.725 17.273  1.00 44.40  ? 1283 PRO   A CG  1 
ATOM   1742 C CD  . PRO   A 1 246 ? -5.756  -20.133 16.113  1.00 46.30  ? 1283 PRO   A CD  1 
ATOM   1743 N N   . TYR   A 1 247 ? -9.876  -22.265 15.065  1.00 49.43  ? 1284 TYR   A N   1 
ATOM   1744 C CA  . TYR   A 1 247 ? -10.964 -22.336 14.102  1.00 51.47  ? 1284 TYR   A CA  1 
ATOM   1745 C C   . TYR   A 1 247 ? -10.394 -22.585 12.706  1.00 53.89  ? 1284 TYR   A C   1 
ATOM   1746 O O   . TYR   A 1 247 ? -10.570 -21.767 11.804  1.00 54.42  ? 1284 TYR   A O   1 
ATOM   1747 C CB  . TYR   A 1 247 ? -11.799 -21.054 14.170  1.00 50.56  ? 1284 TYR   A CB  1 
ATOM   1748 C CG  . TYR   A 1 247 ? -12.297 -20.703 15.550  1.00 48.97  ? 1284 TYR   A CG  1 
ATOM   1749 C CD1 . TYR   A 1 247 ? -13.351 -21.391 16.131  1.00 49.68  ? 1284 TYR   A CD1 1 
ATOM   1750 C CD2 . TYR   A 1 247 ? -11.702 -19.692 16.288  1.00 47.21  ? 1284 TYR   A CD2 1 
ATOM   1751 C CE1 . TYR   A 1 247 ? -13.810 -21.073 17.400  1.00 48.73  ? 1284 TYR   A CE1 1 
ATOM   1752 C CE2 . TYR   A 1 247 ? -12.146 -19.363 17.559  1.00 46.11  ? 1284 TYR   A CE2 1 
ATOM   1753 C CZ  . TYR   A 1 247 ? -13.204 -20.057 18.119  1.00 46.90  ? 1284 TYR   A CZ  1 
ATOM   1754 O OH  . TYR   A 1 247 ? -13.647 -19.737 19.381  1.00 46.26  ? 1284 TYR   A OH  1 
ATOM   1755 N N   . PRO   A 1 248 ? -9.700  -23.726 12.484  1.00 55.98  ? 1285 PRO   A N   1 
ATOM   1756 C CA  . PRO   A 1 248 ? -8.972  -23.960 11.235  1.00 58.58  ? 1285 PRO   A CA  1 
ATOM   1757 C C   . PRO   A 1 248 ? -9.855  -24.279 10.029  1.00 61.22  ? 1285 PRO   A C   1 
ATOM   1758 O O   . PRO   A 1 248 ? -9.402  -24.179 8.891   1.00 63.22  ? 1285 PRO   A O   1 
ATOM   1759 C CB  . PRO   A 1 248 ? -8.087  -25.168 11.579  1.00 59.98  ? 1285 PRO   A CB  1 
ATOM   1760 C CG  . PRO   A 1 248 ? -8.893  -25.930 12.608  1.00 59.32  ? 1285 PRO   A CG  1 
ATOM   1761 C CD  . PRO   A 1 248 ? -9.595  -24.859 13.417  1.00 56.29  ? 1285 PRO   A CD  1 
ATOM   1762 N N   . ASP   A 1 249 ? -11.110 -24.666 10.292  1.00 61.70  ? 1286 ASP   A N   1 
ATOM   1763 C CA  . ASP   A 1 249 ? -12.063 -25.001 9.245   1.00 64.71  ? 1286 ASP   A CA  1 
ATOM   1764 C C   . ASP   A 1 249 ? -13.310 -24.130 9.410   1.00 63.64  ? 1286 ASP   A C   1 
ATOM   1765 O O   . ASP   A 1 249 ? -14.432 -24.601 9.234   1.00 65.12  ? 1286 ASP   A O   1 
ATOM   1766 C CB  . ASP   A 1 249 ? -12.358 -26.506 9.247   1.00 67.52  ? 1286 ASP   A CB  1 
ATOM   1767 C CG  . ASP   A 1 249 ? -12.646 -27.093 10.620  1.00 66.43  ? 1286 ASP   A CG  1 
ATOM   1768 O OD1 . ASP   A 1 249 ? -12.877 -26.307 11.563  1.00 63.90  ? 1286 ASP   A OD1 1 
ATOM   1769 O OD2 . ASP   A 1 249 ? -12.608 -28.334 10.744  1.00 68.48  ? 1286 ASP   A OD2 1 
ATOM   1770 N N   . VAL   A 1 250 ? -13.086 -22.851 9.739   1.00 61.54  ? 1287 VAL   A N   1 
ATOM   1771 C CA  . VAL   A 1 250 ? -14.148 -21.870 9.891   1.00 60.94  ? 1287 VAL   A CA  1 
ATOM   1772 C C   . VAL   A 1 250 ? -13.672 -20.557 9.275   1.00 60.59  ? 1287 VAL   A C   1 
ATOM   1773 O O   . VAL   A 1 250 ? -12.529 -20.151 9.482   1.00 59.39  ? 1287 VAL   A O   1 
ATOM   1774 C CB  . VAL   A 1 250 ? -14.542 -21.679 11.369  1.00 58.55  ? 1287 VAL   A CB  1 
ATOM   1775 C CG1 . VAL   A 1 250 ? -15.591 -20.588 11.541  1.00 58.00  ? 1287 VAL   A CG1 1 
ATOM   1776 C CG2 . VAL   A 1 250 ? -15.009 -22.981 12.005  1.00 59.49  ? 1287 VAL   A CG2 1 
ATOM   1777 N N   . ASN   A 1 251 ? -14.567 -19.897 8.531   1.00 62.03  ? 1288 ASN   A N   1 
ATOM   1778 C CA  . ASN   A 1 251 ? -14.229 -18.688 7.798   1.00 62.52  ? 1288 ASN   A CA  1 
ATOM   1779 C C   . ASN   A 1 251 ? -14.083 -17.524 8.777   1.00 59.89  ? 1288 ASN   A C   1 
ATOM   1780 O O   . ASN   A 1 251 ? -14.694 -17.522 9.845   1.00 58.37  ? 1288 ASN   A O   1 
ATOM   1781 C CB  . ASN   A 1 251 ? -15.270 -18.387 6.715   1.00 65.36  ? 1288 ASN   A CB  1 
ATOM   1782 C CG  . ASN   A 1 251 ? -14.840 -17.309 5.740   1.00 66.78  ? 1288 ASN   A CG  1 
ATOM   1783 O OD1 . ASN   A 1 251 ? -13.712 -16.822 5.793   1.00 65.87  ? 1288 ASN   A OD1 1 
ATOM   1784 N ND2 . ASN   A 1 251 ? -15.732 -16.934 4.839   1.00 69.48  ? 1288 ASN   A ND2 1 
ATOM   1785 N N   . THR   A 1 252 ? -13.259 -16.542 8.391   1.00 59.80  ? 1289 THR   A N   1 
ATOM   1786 C CA  . THR   A 1 252 ? -13.039 -15.332 9.167   1.00 57.94  ? 1289 THR   A CA  1 
ATOM   1787 C C   . THR   A 1 252 ? -14.356 -14.577 9.345   1.00 58.21  ? 1289 THR   A C   1 
ATOM   1788 O O   . THR   A 1 252 ? -14.632 -14.056 10.422  1.00 56.56  ? 1289 THR   A O   1 
ATOM   1789 C CB  . THR   A 1 252 ? -11.990 -14.439 8.488   1.00 58.97  ? 1289 THR   A CB  1 
ATOM   1790 O OG1 . THR   A 1 252 ? -10.855 -15.245 8.171   1.00 59.56  ? 1289 THR   A OG1 1 
ATOM   1791 C CG2 . THR   A 1 252 ? -11.551 -13.267 9.339   1.00 57.45  ? 1289 THR   A CG2 1 
ATOM   1792 N N   . PHE   A 1 253 ? -15.157 -14.526 8.274   1.00 60.70  ? 1290 PHE   A N   1 
ATOM   1793 C CA  . PHE   A 1 253 ? -16.378 -13.737 8.243   1.00 61.81  ? 1290 PHE   A CA  1 
ATOM   1794 C C   . PHE   A 1 253 ? -17.480 -14.414 9.058   1.00 61.17  ? 1290 PHE   A C   1 
ATOM   1795 O O   . PHE   A 1 253 ? -18.253 -13.734 9.730   1.00 60.99  ? 1290 PHE   A O   1 
ATOM   1796 C CB  . PHE   A 1 253 ? -16.821 -13.510 6.794   1.00 65.23  ? 1290 PHE   A CB  1 
ATOM   1797 C CG  . PHE   A 1 253 ? -15.848 -12.756 5.919   1.00 66.57  ? 1290 PHE   A CG  1 
ATOM   1798 C CD1 . PHE   A 1 253 ? -14.769 -12.063 6.454   1.00 64.95  ? 1290 PHE   A CD1 1 
ATOM   1799 C CD2 . PHE   A 1 253 ? -16.011 -12.747 4.541   1.00 69.88  ? 1290 PHE   A CD2 1 
ATOM   1800 C CE1 . PHE   A 1 253 ? -13.887 -11.376 5.634   1.00 66.71  ? 1290 PHE   A CE1 1 
ATOM   1801 C CE2 . PHE   A 1 253 ? -15.127 -12.060 3.722   1.00 71.55  ? 1290 PHE   A CE2 1 
ATOM   1802 C CZ  . PHE   A 1 253 ? -14.066 -11.376 4.270   1.00 70.03  ? 1290 PHE   A CZ  1 
ATOM   1803 N N   . ASP   A 1 254 ? -17.536 -15.752 9.004   1.00 61.09  ? 1291 ASP   A N   1 
ATOM   1804 C CA  . ASP   A 1 254 ? -18.597 -16.514 9.647   1.00 61.13  ? 1291 ASP   A CA  1 
ATOM   1805 C C   . ASP   A 1 254 ? -18.191 -16.916 11.065  1.00 58.06  ? 1291 ASP   A C   1 
ATOM   1806 O O   . ASP   A 1 254 ? -18.715 -17.892 11.601  1.00 58.28  ? 1291 ASP   A O   1 
ATOM   1807 C CB  . ASP   A 1 254 ? -18.951 -17.761 8.830   1.00 63.49  ? 1291 ASP   A CB  1 
ATOM   1808 C CG  . ASP   A 1 254 ? -19.368 -17.467 7.399   1.00 66.72  ? 1291 ASP   A CG  1 
ATOM   1809 O OD1 . ASP   A 1 254 ? -20.326 -16.692 7.216   1.00 68.40  ? 1291 ASP   A OD1 1 
ATOM   1810 O OD2 . ASP   A 1 254 ? -18.735 -18.024 6.479   1.00 67.99  ? 1291 ASP   A OD2 1 
ATOM   1811 N N   . ILE   A 1 255 ? -17.275 -16.153 11.678  1.00 55.42  ? 1292 ILE   A N   1 
ATOM   1812 C CA  . ILE   A 1 255 ? -16.740 -16.491 12.987  1.00 52.72  ? 1292 ILE   A CA  1 
ATOM   1813 C C   . ILE   A 1 255 ? -17.688 -15.991 14.078  1.00 52.10  ? 1292 ILE   A C   1 
ATOM   1814 O O   . ILE   A 1 255 ? -17.767 -16.591 15.147  1.00 51.00  ? 1292 ILE   A O   1 
ATOM   1815 C CB  . ILE   A 1 255 ? -15.313 -15.927 13.158  1.00 50.98  ? 1292 ILE   A CB  1 
ATOM   1816 C CG1 . ILE   A 1 255 ? -14.541 -16.651 14.263  1.00 48.96  ? 1292 ILE   A CG1 1 
ATOM   1817 C CG2 . ILE   A 1 255 ? -15.331 -14.420 13.379  1.00 50.92  ? 1292 ILE   A CG2 1 
ATOM   1818 C CD1 . ILE   A 1 255 ? -14.186 -18.081 13.929  1.00 49.61  ? 1292 ILE   A CD1 1 
ATOM   1819 N N   . THR   A 1 256 ? -18.396 -14.888 13.802  1.00 52.97  ? 1293 THR   A N   1 
ATOM   1820 C CA  . THR   A 1 256 ? -19.298 -14.283 14.770  1.00 53.10  ? 1293 THR   A CA  1 
ATOM   1821 C C   . THR   A 1 256 ? -20.553 -15.141 14.920  1.00 54.83  ? 1293 THR   A C   1 
ATOM   1822 O O   . THR   A 1 256 ? -21.011 -15.377 16.036  1.00 54.63  ? 1293 THR   A O   1 
ATOM   1823 C CB  . THR   A 1 256 ? -19.645 -12.845 14.367  1.00 54.38  ? 1293 THR   A CB  1 
ATOM   1824 O OG1 . THR   A 1 256 ? -18.419 -12.124 14.238  1.00 52.94  ? 1293 THR   A OG1 1 
ATOM   1825 C CG2 . THR   A 1 256 ? -20.548 -12.149 15.363  1.00 55.21  ? 1293 THR   A CG2 1 
ATOM   1826 N N   . VAL   A 1 257 ? -21.096 -15.601 13.785  1.00 56.84  ? 1294 VAL   A N   1 
ATOM   1827 C CA  . VAL   A 1 257 ? -22.294 -16.427 13.765  1.00 59.14  ? 1294 VAL   A CA  1 
ATOM   1828 C C   . VAL   A 1 257 ? -22.012 -17.739 14.496  1.00 58.09  ? 1294 VAL   A C   1 
ATOM   1829 O O   . VAL   A 1 257 ? -22.852 -18.222 15.252  1.00 59.20  ? 1294 VAL   A O   1 
ATOM   1830 C CB  . VAL   A 1 257 ? -22.773 -16.683 12.321  1.00 61.80  ? 1294 VAL   A CB  1 
ATOM   1831 C CG1 . VAL   A 1 257 ? -23.928 -17.673 12.271  1.00 64.77  ? 1294 VAL   A CG1 1 
ATOM   1832 C CG2 . VAL   A 1 257 ? -23.149 -15.391 11.608  1.00 63.21  ? 1294 VAL   A CG2 1 
ATOM   1833 N N   . TYR   A 1 258 ? -20.820 -18.298 14.256  1.00 56.25  ? 1295 TYR   A N   1 
ATOM   1834 C CA  . TYR   A 1 258 ? -20.392 -19.558 14.844  1.00 55.67  ? 1295 TYR   A CA  1 
ATOM   1835 C C   . TYR   A 1 258 ? -20.488 -19.493 16.368  1.00 54.40  ? 1295 TYR   A C   1 
ATOM   1836 O O   . TYR   A 1 258 ? -20.947 -20.443 17.000  1.00 55.44  ? 1295 TYR   A O   1 
ATOM   1837 C CB  . TYR   A 1 258 ? -18.975 -19.880 14.359  1.00 54.12  ? 1295 TYR   A CB  1 
ATOM   1838 C CG  . TYR   A 1 258 ? -18.370 -21.157 14.887  1.00 53.81  ? 1295 TYR   A CG  1 
ATOM   1839 C CD1 . TYR   A 1 258 ? -18.375 -22.315 14.126  1.00 55.79  ? 1295 TYR   A CD1 1 
ATOM   1840 C CD2 . TYR   A 1 258 ? -17.739 -21.196 16.120  1.00 51.81  ? 1295 TYR   A CD2 1 
ATOM   1841 C CE1 . TYR   A 1 258 ? -17.806 -23.489 14.592  1.00 55.88  ? 1295 TYR   A CE1 1 
ATOM   1842 C CE2 . TYR   A 1 258 ? -17.162 -22.361 16.600  1.00 51.74  ? 1295 TYR   A CE2 1 
ATOM   1843 C CZ  . TYR   A 1 258 ? -17.194 -23.512 15.833  1.00 53.82  ? 1295 TYR   A CZ  1 
ATOM   1844 O OH  . TYR   A 1 258 ? -16.626 -24.670 16.302  1.00 54.51  ? 1295 TYR   A OH  1 
ATOM   1845 N N   . LEU   A 1 259 ? -20.052 -18.367 16.946  1.00 52.60  ? 1296 LEU   A N   1 
ATOM   1846 C CA  . LEU   A 1 259 ? -20.071 -18.171 18.387  1.00 51.75  ? 1296 LEU   A CA  1 
ATOM   1847 C C   . LEU   A 1 259 ? -21.497 -17.906 18.869  1.00 54.23  ? 1296 LEU   A C   1 
ATOM   1848 O O   . LEU   A 1 259 ? -21.870 -18.346 19.955  1.00 54.68  ? 1296 LEU   A O   1 
ATOM   1849 C CB  . LEU   A 1 259 ? -19.141 -17.006 18.745  1.00 49.54  ? 1296 LEU   A CB  1 
ATOM   1850 C CG  . LEU   A 1 259 ? -17.656 -17.231 18.459  1.00 47.46  ? 1296 LEU   A CG  1 
ATOM   1851 C CD1 . LEU   A 1 259 ? -16.842 -16.003 18.838  1.00 45.91  ? 1296 LEU   A CD1 1 
ATOM   1852 C CD2 . LEU   A 1 259 ? -17.136 -18.461 19.190  1.00 46.87  ? 1296 LEU   A CD2 1 
ATOM   1853 N N   . LEU   A 1 260 ? -22.285 -17.187 18.058  1.00 56.25  ? 1297 LEU   A N   1 
ATOM   1854 C CA  . LEU   A 1 260 ? -23.679 -16.906 18.374  1.00 59.36  ? 1297 LEU   A CA  1 
ATOM   1855 C C   . LEU   A 1 260 ? -24.494 -18.198 18.378  1.00 61.99  ? 1297 LEU   A C   1 
ATOM   1856 O O   . LEU   A 1 260 ? -25.457 -18.315 19.133  1.00 64.39  ? 1297 LEU   A O   1 
ATOM   1857 C CB  . LEU   A 1 260 ? -24.243 -15.906 17.357  1.00 61.11  ? 1297 LEU   A CB  1 
ATOM   1858 C CG  . LEU   A 1 260 ? -23.854 -14.442 17.570  1.00 60.05  ? 1297 LEU   A CG  1 
ATOM   1859 C CD1 . LEU   A 1 260 ? -24.406 -13.571 16.452  1.00 62.16  ? 1297 LEU   A CD1 1 
ATOM   1860 C CD2 . LEU   A 1 260 ? -24.341 -13.935 18.921  1.00 60.71  ? 1297 LEU   A CD2 1 
ATOM   1861 N N   . GLN   A 1 261 ? -24.103 -19.160 17.531  1.00 62.12  ? 1298 GLN   A N   1 
ATOM   1862 C CA  . GLN   A 1 261 ? -24.752 -20.462 17.473  1.00 64.86  ? 1298 GLN   A CA  1 
ATOM   1863 C C   . GLN   A 1 261 ? -24.436 -21.277 18.727  1.00 64.32  ? 1298 GLN   A C   1 
ATOM   1864 O O   . GLN   A 1 261 ? -25.136 -22.244 19.022  1.00 67.16  ? 1298 GLN   A O   1 
ATOM   1865 C CB  . GLN   A 1 261 ? -24.319 -21.215 16.213  1.00 65.27  ? 1298 GLN   A CB  1 
ATOM   1866 C CG  . GLN   A 1 261 ? -24.963 -20.685 14.939  1.00 67.43  ? 1298 GLN   A CG  1 
ATOM   1867 C CD  . GLN   A 1 261 ? -24.406 -21.326 13.692  1.00 67.94  ? 1298 GLN   A CD  1 
ATOM   1868 O OE1 . GLN   A 1 261 ? -23.474 -22.125 13.739  1.00 66.68  ? 1298 GLN   A OE1 1 
ATOM   1869 N NE2 . GLN   A 1 261 ? -24.979 -20.972 12.553  1.00 70.35  ? 1298 GLN   A NE2 1 
ATOM   1870 N N   . GLY   A 1 262 ? -23.375 -20.889 19.448  1.00 61.09  ? 1299 GLY   A N   1 
ATOM   1871 C CA  . GLY   A 1 262 ? -23.015 -21.510 20.713  1.00 60.52  ? 1299 GLY   A CA  1 
ATOM   1872 C C   . GLY   A 1 262 ? -21.794 -22.418 20.587  1.00 58.87  ? 1299 GLY   A C   1 
ATOM   1873 O O   . GLY   A 1 262 ? -21.351 -22.998 21.576  1.00 58.15  ? 1299 GLY   A O   1 
ATOM   1874 N N   . ARG   A 1 263 ? -21.252 -22.522 19.367  1.00 58.67  ? 1300 ARG   A N   1 
ATOM   1875 C CA  . ARG   A 1 263 ? -20.118 -23.390 19.092  1.00 58.01  ? 1300 ARG   A CA  1 
ATOM   1876 C C   . ARG   A 1 263 ? -18.839 -22.723 19.593  1.00 54.68  ? 1300 ARG   A C   1 
ATOM   1877 O O   . ARG   A 1 263 ? -18.711 -21.501 19.541  1.00 53.15  ? 1300 ARG   A O   1 
ATOM   1878 C CB  . ARG   A 1 263 ? -20.021 -23.684 17.592  1.00 59.49  ? 1300 ARG   A CB  1 
ATOM   1879 C CG  . ARG   A 1 263 ? -21.280 -24.283 16.980  1.00 63.54  ? 1300 ARG   A CG  1 
ATOM   1880 C CD  . ARG   A 1 263 ? -21.123 -24.521 15.490  1.00 65.09  ? 1300 ARG   A CD  1 
ATOM   1881 N NE  . ARG   A 1 263 ? -22.375 -24.913 14.856  1.00 69.18  ? 1300 ARG   A NE  1 
ATOM   1882 C CZ  . ARG   A 1 263 ? -22.511 -25.192 13.563  1.00 71.49  ? 1300 ARG   A CZ  1 
ATOM   1883 N NH1 . ARG   A 1 263 ? -21.471 -25.105 12.753  1.00 70.32  ? 1300 ARG   A NH1 1 
ATOM   1884 N NH2 . ARG   A 1 263 ? -23.690 -25.553 13.085  1.00 75.28  ? 1300 ARG   A NH2 1 
ATOM   1885 N N   . ARG   A 1 264 ? -17.903 -23.549 20.076  1.00 53.98  ? 1301 ARG   A N   1 
ATOM   1886 C CA  . ARG   A 1 264 ? -16.635 -23.086 20.620  1.00 51.33  ? 1301 ARG   A CA  1 
ATOM   1887 C C   . ARG   A 1 264 ? -15.523 -24.008 20.122  1.00 51.44  ? 1301 ARG   A C   1 
ATOM   1888 O O   . ARG   A 1 264 ? -15.786 -24.950 19.377  1.00 53.50  ? 1301 ARG   A O   1 
ATOM   1889 C CB  . ARG   A 1 264 ? -16.703 -23.063 22.151  1.00 50.88  ? 1301 ARG   A CB  1 
ATOM   1890 C CG  . ARG   A 1 264 ? -17.755 -22.125 22.729  1.00 51.19  ? 1301 ARG   A CG  1 
ATOM   1891 C CD  . ARG   A 1 264 ? -17.406 -20.662 22.533  1.00 49.21  ? 1301 ARG   A CD  1 
ATOM   1892 N NE  . ARG   A 1 264 ? -18.373 -19.761 23.151  1.00 49.85  ? 1301 ARG   A NE  1 
ATOM   1893 C CZ  . ARG   A 1 264 ? -19.582 -19.496 22.667  1.00 51.67  ? 1301 ARG   A CZ  1 
ATOM   1894 N NH1 . ARG   A 1 264 ? -19.973 -20.030 21.524  1.00 52.87  ? 1301 ARG   A NH1 1 
ATOM   1895 N NH2 . ARG   A 1 264 ? -20.394 -18.685 23.324  1.00 52.66  ? 1301 ARG   A NH2 1 
ATOM   1896 N N   . LEU   A 1 265 ? -14.280 -23.723 20.532  1.00 49.68  ? 1302 LEU   A N   1 
ATOM   1897 C CA  . LEU   A 1 265 ? -13.143 -24.568 20.199  1.00 50.16  ? 1302 LEU   A CA  1 
ATOM   1898 C C   . LEU   A 1 265 ? -13.310 -25.933 20.863  1.00 52.33  ? 1302 LEU   A C   1 
ATOM   1899 O O   . LEU   A 1 265 ? -13.753 -26.018 22.007  1.00 52.47  ? 1302 LEU   A O   1 
ATOM   1900 C CB  . LEU   A 1 265 ? -11.852 -23.890 20.670  1.00 48.06  ? 1302 LEU   A CB  1 
ATOM   1901 C CG  . LEU   A 1 265 ? -11.470 -22.598 19.946  1.00 46.70  ? 1302 LEU   A CG  1 
ATOM   1902 C CD1 . LEU   A 1 265 ? -10.245 -21.958 20.582  1.00 45.22  ? 1302 LEU   A CD1 1 
ATOM   1903 C CD2 . LEU   A 1 265 ? -11.216 -22.855 18.468  1.00 47.98  ? 1302 LEU   A CD2 1 
ATOM   1904 N N   . LEU   A 1 266 ? -12.944 -26.993 20.131  1.00 54.60  ? 1303 LEU   A N   1 
ATOM   1905 C CA  . LEU   A 1 266 ? -13.038 -28.356 20.630  1.00 57.40  ? 1303 LEU   A CA  1 
ATOM   1906 C C   . LEU   A 1 266 ? -11.861 -28.639 21.559  1.00 56.95  ? 1303 LEU   A C   1 
ATOM   1907 O O   . LEU   A 1 266 ? -10.859 -27.929 21.526  1.00 54.94  ? 1303 LEU   A O   1 
ATOM   1908 C CB  . LEU   A 1 266 ? -13.047 -29.326 19.442  1.00 60.23  ? 1303 LEU   A CB  1 
ATOM   1909 C CG  . LEU   A 1 266 ? -14.165 -29.118 18.420  1.00 61.48  ? 1303 LEU   A CG  1 
ATOM   1910 C CD1 . LEU   A 1 266 ? -14.179 -30.248 17.401  1.00 64.82  ? 1303 LEU   A CD1 1 
ATOM   1911 C CD2 . LEU   A 1 266 ? -15.522 -28.998 19.101  1.00 62.17  ? 1303 LEU   A CD2 1 
ATOM   1912 N N   . GLN   A 1 267 ? -11.996 -29.687 22.379  1.00 59.38  ? 1304 GLN   A N   1 
ATOM   1913 C CA  . GLN   A 1 267 ? -10.979 -30.045 23.355  1.00 59.70  ? 1304 GLN   A CA  1 
ATOM   1914 C C   . GLN   A 1 267 ? -9.769  -30.637 22.634  1.00 61.07  ? 1304 GLN   A C   1 
ATOM   1915 O O   . GLN   A 1 267 ? -9.910  -31.612 21.898  1.00 63.79  ? 1304 GLN   A O   1 
ATOM   1916 C CB  . GLN   A 1 267 ? -11.540 -31.041 24.373  1.00 62.22  ? 1304 GLN   A CB  1 
ATOM   1917 C CG  . GLN   A 1 267 ? -10.588 -31.336 25.526  1.00 62.36  ? 1304 GLN   A CG  1 
ATOM   1918 C CD  . GLN   A 1 267 ? -11.195 -32.242 26.569  1.00 65.15  ? 1304 GLN   A CD  1 
ATOM   1919 O OE1 . GLN   A 1 267 ? -12.339 -32.678 26.457  1.00 67.17  ? 1304 GLN   A OE1 1 
ATOM   1920 N NE2 . GLN   A 1 267 ? -10.423 -32.535 27.603  1.00 65.71  ? 1304 GLN   A NE2 1 
ATOM   1921 N N   . PRO   A 1 268 ? -8.552  -30.064 22.808  1.00 59.78  ? 1305 PRO   A N   1 
ATOM   1922 C CA  . PRO   A 1 268 ? -7.330  -30.655 22.255  1.00 61.53  ? 1305 PRO   A CA  1 
ATOM   1923 C C   . PRO   A 1 268 ? -7.066  -32.087 22.716  1.00 65.05  ? 1305 PRO   A C   1 
ATOM   1924 O O   . PRO   A 1 268 ? -7.675  -32.564 23.672  1.00 65.90  ? 1305 PRO   A O   1 
ATOM   1925 C CB  . PRO   A 1 268 ? -6.204  -29.741 22.766  1.00 59.40  ? 1305 PRO   A CB  1 
ATOM   1926 C CG  . PRO   A 1 268 ? -6.888  -28.423 23.067  1.00 56.29  ? 1305 PRO   A CG  1 
ATOM   1927 C CD  . PRO   A 1 268 ? -8.295  -28.788 23.493  1.00 56.79  ? 1305 PRO   A CD  1 
ATOM   1928 N N   . GLU   A 1 269 ? -6.133  -32.754 22.025  1.00 67.48  ? 1306 GLU   A N   1 
ATOM   1929 C CA  . GLU   A 1 269 ? -5.811  -34.149 22.281  1.00 71.52  ? 1306 GLU   A CA  1 
ATOM   1930 C C   . GLU   A 1 269 ? -5.257  -34.303 23.695  1.00 71.75  ? 1306 GLU   A C   1 
ATOM   1931 O O   . GLU   A 1 269 ? -5.719  -35.157 24.449  1.00 74.04  ? 1306 GLU   A O   1 
ATOM   1932 C CB  . GLU   A 1 269 ? -4.811  -34.659 21.241  1.00 74.04  ? 1306 GLU   A CB  1 
ATOM   1933 C CG  . GLU   A 1 269 ? -4.460  -36.130 21.396  1.00 78.74  ? 1306 GLU   A CG  1 
ATOM   1934 C CD  . GLU   A 1 269 ? -3.539  -36.676 20.318  1.00 81.93  ? 1306 GLU   A CD  1 
ATOM   1935 O OE1 . GLU   A 1 269 ? -3.910  -37.680 19.677  1.00 85.49  ? 1306 GLU   A OE1 1 
ATOM   1936 O OE2 . GLU   A 1 269 ? -2.455  -36.093 20.119  1.00 81.20  ? 1306 GLU   A OE2 1 
ATOM   1937 N N   . TYR   A 1 270 ? -4.271  -33.465 24.042  1.00 69.77  ? 1307 TYR   A N   1 
ATOM   1938 C CA  . TYR   A 1 270 ? -3.573  -33.565 25.315  1.00 70.19  ? 1307 TYR   A CA  1 
ATOM   1939 C C   . TYR   A 1 270 ? -4.025  -32.461 26.271  1.00 66.70  ? 1307 TYR   A C   1 
ATOM   1940 O O   . TYR   A 1 270 ? -3.254  -32.040 27.133  1.00 66.27  ? 1307 TYR   A O   1 
ATOM   1941 C CB  . TYR   A 1 270 ? -2.059  -33.514 25.087  1.00 71.42  ? 1307 TYR   A CB  1 
ATOM   1942 C CG  . TYR   A 1 270 ? -1.483  -34.706 24.364  1.00 75.70  ? 1307 TYR   A CG  1 
ATOM   1943 C CD1 . TYR   A 1 270 ? -1.557  -35.978 24.911  1.00 79.35  ? 1307 TYR   A CD1 1 
ATOM   1944 C CD2 . TYR   A 1 270 ? -0.855  -34.566 23.137  1.00 76.57  ? 1307 TYR   A CD2 1 
ATOM   1945 C CE1 . TYR   A 1 270 ? -1.027  -37.079 24.257  1.00 83.66  ? 1307 TYR   A CE1 1 
ATOM   1946 C CE2 . TYR   A 1 270 ? -0.319  -35.657 22.469  1.00 80.82  ? 1307 TYR   A CE2 1 
ATOM   1947 C CZ  . TYR   A 1 270 ? -0.405  -36.918 23.031  1.00 84.41  ? 1307 TYR   A CZ  1 
ATOM   1948 O OH  . TYR   A 1 270 ? 0.123   -38.004 22.375  1.00 89.11  ? 1307 TYR   A OH  1 
ATOM   1949 N N   . CYS   A 1 271 ? -5.278  -32.006 26.129  1.00 64.60  ? 1308 CYS   A N   1 
ATOM   1950 C CA  . CYS   A 1 271 ? -5.851  -31.031 27.044  1.00 61.92  ? 1308 CYS   A CA  1 
ATOM   1951 C C   . CYS   A 1 271 ? -6.664  -31.753 28.115  1.00 63.66  ? 1308 CYS   A C   1 
ATOM   1952 O O   . CYS   A 1 271 ? -7.606  -32.471 27.788  1.00 65.36  ? 1308 CYS   A O   1 
ATOM   1953 C CB  . CYS   A 1 271 ? -6.745  -30.037 26.313  1.00 59.35  ? 1308 CYS   A CB  1 
ATOM   1954 S SG  . CYS   A 1 271 ? -7.538  -28.835 27.414  1.00 56.61  ? 1308 CYS   A SG  1 
ATOM   1955 N N   . PRO   A 1 272 ? -6.327  -31.598 29.419  1.00 63.63  ? 1309 PRO   A N   1 
ATOM   1956 C CA  . PRO   A 1 272 ? -7.138  -32.167 30.498  1.00 65.62  ? 1309 PRO   A CA  1 
ATOM   1957 C C   . PRO   A 1 272 ? -8.559  -31.607 30.519  1.00 64.49  ? 1309 PRO   A C   1 
ATOM   1958 O O   . PRO   A 1 272 ? -8.790  -30.477 30.093  1.00 61.61  ? 1309 PRO   A O   1 
ATOM   1959 C CB  . PRO   A 1 272 ? -6.391  -31.771 31.782  1.00 65.45  ? 1309 PRO   A CB  1 
ATOM   1960 C CG  . PRO   A 1 272 ? -4.979  -31.477 31.323  1.00 64.63  ? 1309 PRO   A CG  1 
ATOM   1961 C CD  . PRO   A 1 272 ? -5.132  -30.908 29.929  1.00 62.41  ? 1309 PRO   A CD  1 
ATOM   1962 N N   . ASP   A 1 273 ? -9.499  -32.415 31.026  1.00 67.32  ? 1310 ASP   A N   1 
ATOM   1963 C CA  . ASP   A 1 273 ? -10.901 -32.033 31.094  1.00 67.25  ? 1310 ASP   A CA  1 
ATOM   1964 C C   . ASP   A 1 273 ? -11.059 -30.799 31.983  1.00 65.22  ? 1310 ASP   A C   1 
ATOM   1965 O O   . ASP   A 1 273 ? -11.768 -29.869 31.606  1.00 63.37  ? 1310 ASP   A O   1 
ATOM   1966 C CB  . ASP   A 1 273 ? -11.781 -33.196 31.568  1.00 71.36  ? 1310 ASP   A CB  1 
ATOM   1967 C CG  . ASP   A 1 273 ? -11.788 -34.397 30.636  1.00 73.94  ? 1310 ASP   A CG  1 
ATOM   1968 O OD1 . ASP   A 1 273 ? -11.089 -34.349 29.604  1.00 72.66  ? 1310 ASP   A OD1 1 
ATOM   1969 O OD2 . ASP   A 1 273 ? -12.495 -35.375 30.950  1.00 77.58  ? 1310 ASP   A OD2 1 
ATOM   1970 N N   . PRO   A 1 274 ? -10.412 -30.735 33.174  1.00 65.87  ? 1311 PRO   A N   1 
ATOM   1971 C CA  . PRO   A 1 274 ? -10.491 -29.548 34.030  1.00 64.30  ? 1311 PRO   A CA  1 
ATOM   1972 C C   . PRO   A 1 274 ? -10.034 -28.257 33.350  1.00 60.79  ? 1311 PRO   A C   1 
ATOM   1973 O O   . PRO   A 1 274 ? -10.640 -27.206 33.548  1.00 59.40  ? 1311 PRO   A O   1 
ATOM   1974 C CB  . PRO   A 1 274 ? -9.551  -29.876 35.201  1.00 65.79  ? 1311 PRO   A CB  1 
ATOM   1975 C CG  . PRO   A 1 274 ? -9.512  -31.387 35.234  1.00 69.29  ? 1311 PRO   A CG  1 
ATOM   1976 C CD  . PRO   A 1 274 ? -9.592  -31.797 33.779  1.00 68.59  ? 1311 PRO   A CD  1 
ATOM   1977 N N   . LEU   A 1 275 ? -8.960  -28.353 32.556  1.00 59.77  ? 1312 LEU   A N   1 
ATOM   1978 C CA  . LEU   A 1 275 ? -8.393  -27.203 31.868  1.00 56.81  ? 1312 LEU   A CA  1 
ATOM   1979 C C   . LEU   A 1 275 ? -9.309  -26.769 30.725  1.00 55.34  ? 1312 LEU   A C   1 
ATOM   1980 O O   . LEU   A 1 275 ? -9.387  -25.582 30.415  1.00 52.94  ? 1312 LEU   A O   1 
ATOM   1981 C CB  . LEU   A 1 275 ? -6.998  -27.568 31.348  1.00 56.94  ? 1312 LEU   A CB  1 
ATOM   1982 C CG  . LEU   A 1 275 ? -6.221  -26.433 30.681  1.00 54.64  ? 1312 LEU   A CG  1 
ATOM   1983 C CD1 . LEU   A 1 275 ? -5.807  -25.382 31.699  1.00 53.78  ? 1312 LEU   A CD1 1 
ATOM   1984 C CD2 . LEU   A 1 275 ? -5.003  -26.971 29.946  1.00 55.46  ? 1312 LEU   A CD2 1 
ATOM   1985 N N   . TYR   A 1 276 ? -9.985  -27.740 30.096  1.00 56.91  ? 1313 TYR   A N   1 
ATOM   1986 C CA  . TYR   A 1 276 ? -10.907 -27.453 29.009  1.00 56.29  ? 1313 TYR   A CA  1 
ATOM   1987 C C   . TYR   A 1 276 ? -12.164 -26.776 29.553  1.00 56.55  ? 1313 TYR   A C   1 
ATOM   1988 O O   . TYR   A 1 276 ? -12.756 -25.942 28.872  1.00 55.29  ? 1313 TYR   A O   1 
ATOM   1989 C CB  . TYR   A 1 276 ? -11.264 -28.726 28.239  1.00 58.51  ? 1313 TYR   A CB  1 
ATOM   1990 C CG  . TYR   A 1 276 ? -12.160 -28.495 27.048  1.00 58.18  ? 1313 TYR   A CG  1 
ATOM   1991 C CD1 . TYR   A 1 276 ? -11.772 -27.653 26.017  1.00 55.86  ? 1313 TYR   A CD1 1 
ATOM   1992 C CD2 . TYR   A 1 276 ? -13.402 -29.103 26.953  1.00 60.53  ? 1313 TYR   A CD2 1 
ATOM   1993 C CE1 . TYR   A 1 276 ? -12.589 -27.427 24.921  1.00 55.81  ? 1313 TYR   A CE1 1 
ATOM   1994 C CE2 . TYR   A 1 276 ? -14.231 -28.889 25.863  1.00 60.57  ? 1313 TYR   A CE2 1 
ATOM   1995 C CZ  . TYR   A 1 276 ? -13.823 -28.048 24.843  1.00 58.13  ? 1313 TYR   A CZ  1 
ATOM   1996 O OH  . TYR   A 1 276 ? -14.638 -27.830 23.759  1.00 58.49  ? 1313 TYR   A OH  1 
ATOM   1997 N N   . GLU   A 1 277 ? -12.571 -27.145 30.774  1.00 58.75  ? 1314 GLU   A N   1 
ATOM   1998 C CA  . GLU   A 1 277 ? -13.700 -26.503 31.430  1.00 59.62  ? 1314 GLU   A CA  1 
ATOM   1999 C C   . GLU   A 1 277 ? -13.384 -25.027 31.664  1.00 56.91  ? 1314 GLU   A C   1 
ATOM   2000 O O   . GLU   A 1 277 ? -14.253 -24.177 31.487  1.00 56.52  ? 1314 GLU   A O   1 
ATOM   2001 C CB  . GLU   A 1 277 ? -14.041 -27.202 32.749  1.00 63.09  ? 1314 GLU   A CB  1 
ATOM   2002 C CG  . GLU   A 1 277 ? -14.605 -28.602 32.577  1.00 66.74  ? 1314 GLU   A CG  1 
ATOM   2003 C CD  . GLU   A 1 277 ? -15.855 -28.690 31.717  1.00 68.17  ? 1314 GLU   A CD  1 
ATOM   2004 O OE1 . GLU   A 1 277 ? -16.850 -28.017 32.053  1.00 69.09  ? 1314 GLU   A OE1 1 
ATOM   2005 O OE2 . GLU   A 1 277 ? -15.829 -29.430 30.712  1.00 69.05  ? 1314 GLU   A OE2 1 
ATOM   2006 N N   . VAL   A 1 278 ? -12.133 -24.740 32.050  1.00 55.42  ? 1315 VAL   A N   1 
ATOM   2007 C CA  . VAL   A 1 278 ? -11.673 -23.377 32.272  1.00 53.27  ? 1315 VAL   A CA  1 
ATOM   2008 C C   . VAL   A 1 278 ? -11.725 -22.604 30.954  1.00 50.87  ? 1315 VAL   A C   1 
ATOM   2009 O O   . VAL   A 1 278 ? -12.068 -21.424 30.943  1.00 49.93  ? 1315 VAL   A O   1 
ATOM   2010 C CB  . VAL   A 1 278 ? -10.258 -23.357 32.885  1.00 53.09  ? 1315 VAL   A CB  1 
ATOM   2011 C CG1 . VAL   A 1 278 ? -9.663  -21.955 32.914  1.00 51.50  ? 1315 VAL   A CG1 1 
ATOM   2012 C CG2 . VAL   A 1 278 ? -10.235 -23.973 34.277  1.00 55.41  ? 1315 VAL   A CG2 1 
ATOM   2013 N N   . MET   A 1 279 ? -11.373 -23.277 29.852  1.00 50.13  ? 1316 MET   A N   1 
ATOM   2014 C CA  . MET   A 1 279 ? -11.428 -22.679 28.527  1.00 48.32  ? 1316 MET   A CA  1 
ATOM   2015 C C   . MET   A 1 279 ? -12.869 -22.297 28.194  1.00 48.27  ? 1316 MET   A C   1 
ATOM   2016 O O   . MET   A 1 279 ? -13.132 -21.165 27.796  1.00 47.00  ? 1316 MET   A O   1 
ATOM   2017 C CB  . MET   A 1 279 ? -10.905 -23.649 27.463  1.00 48.94  ? 1316 MET   A CB  1 
ATOM   2018 C CG  . MET   A 1 279 ? -9.395  -23.690 27.365  1.00 48.55  ? 1316 MET   A CG  1 
ATOM   2019 S SD  . MET   A 1 279 ? -8.832  -24.867 26.110  1.00 50.10  ? 1316 MET   A SD  1 
ATOM   2020 C CE  . MET   A 1 279 ? -7.332  -25.478 26.878  1.00 51.08  ? 1316 MET   A CE  1 
ATOM   2021 N N   . LEU   A 1 280 ? -13.790 -23.254 28.363  1.00 49.85  ? 1317 LEU   A N   1 
ATOM   2022 C CA  . LEU   A 1 280 ? -15.207 -23.029 28.116  1.00 50.79  ? 1317 LEU   A CA  1 
ATOM   2023 C C   . LEU   A 1 280 ? -15.737 -21.948 29.054  1.00 50.69  ? 1317 LEU   A C   1 
ATOM   2024 O O   . LEU   A 1 280 ? -16.586 -21.151 28.660  1.00 50.89  ? 1317 LEU   A O   1 
ATOM   2025 C CB  . LEU   A 1 280 ? -15.972 -24.343 28.315  1.00 53.60  ? 1317 LEU   A CB  1 
ATOM   2026 C CG  . LEU   A 1 280 ? -15.739 -25.423 27.259  1.00 54.39  ? 1317 LEU   A CG  1 
ATOM   2027 C CD1 . LEU   A 1 280 ? -16.584 -26.654 27.553  1.00 57.83  ? 1317 LEU   A CD1 1 
ATOM   2028 C CD2 . LEU   A 1 280 ? -16.037 -24.899 25.861  1.00 53.51  ? 1317 LEU   A CD2 1 
ATOM   2029 N N   . LYS   A 1 281 ? -15.230 -21.936 30.294  1.00 50.81  ? 1318 LYS   A N   1 
ATOM   2030 C CA  . LYS   A 1 281 ? -15.619 -20.953 31.294  1.00 51.32  ? 1318 LYS   A CA  1 
ATOM   2031 C C   . LYS   A 1 281 ? -15.265 -19.549 30.802  1.00 49.07  ? 1318 LYS   A C   1 
ATOM   2032 O O   . LYS   A 1 281 ? -16.007 -18.600 31.050  1.00 49.73  ? 1318 LYS   A O   1 
ATOM   2033 C CB  . LYS   A 1 281 ? -14.926 -21.251 32.629  1.00 52.27  ? 1318 LYS   A CB  1 
ATOM   2034 C CG  . LYS   A 1 281 ? -15.588 -20.653 33.863  1.00 54.41  ? 1318 LYS   A CG  1 
ATOM   2035 C CD  . LYS   A 1 281 ? -16.790 -21.436 34.348  1.00 57.69  ? 1318 LYS   A CD  1 
ATOM   2036 C CE  . LYS   A 1 281 ? -17.349 -20.909 35.653  1.00 60.26  ? 1318 LYS   A CE  1 
ATOM   2037 N NZ  . LYS   A 1 281 ? -18.502 -21.714 36.121  1.00 63.99  ? 1318 LYS   A NZ  1 
ATOM   2038 N N   . CYS   A 1 282 ? -14.123 -19.432 30.109  1.00 46.52  ? 1319 CYS   A N   1 
ATOM   2039 C CA  . CYS   A 1 282 ? -13.662 -18.164 29.565  1.00 44.44  ? 1319 CYS   A CA  1 
ATOM   2040 C C   . CYS   A 1 282 ? -14.557 -17.705 28.416  1.00 44.24  ? 1319 CYS   A C   1 
ATOM   2041 O O   . CYS   A 1 282 ? -14.784 -16.507 28.256  1.00 44.07  ? 1319 CYS   A O   1 
ATOM   2042 C CB  . CYS   A 1 282 ? -12.223 -18.264 29.070  1.00 42.61  ? 1319 CYS   A CB  1 
ATOM   2043 S SG  . CYS   A 1 282 ? -11.028 -18.622 30.383  1.00 42.52  ? 1319 CYS   A SG  1 
ATOM   2044 N N   . TRP   A 1 283 ? -15.058 -18.661 27.621  1.00 44.42  ? 1320 TRP   A N   1 
ATOM   2045 C CA  . TRP   A 1 283 ? -15.863 -18.346 26.451  1.00 44.67  ? 1320 TRP   A CA  1 
ATOM   2046 C C   . TRP   A 1 283 ? -17.352 -18.381 26.791  1.00 47.03  ? 1320 TRP   A C   1 
ATOM   2047 O O   . TRP   A 1 283 ? -18.147 -18.937 26.034  1.00 48.36  ? 1320 TRP   A O   1 
ATOM   2048 C CB  . TRP   A 1 283 ? -15.547 -19.300 25.291  1.00 44.29  ? 1320 TRP   A CB  1 
ATOM   2049 C CG  . TRP   A 1 283 ? -14.091 -19.466 24.984  1.00 42.61  ? 1320 TRP   A CG  1 
ATOM   2050 C CD1 . TRP   A 1 283 ? -13.141 -18.490 24.909  1.00 41.16  ? 1320 TRP   A CD1 1 
ATOM   2051 C CD2 . TRP   A 1 283 ? -13.425 -20.699 24.663  1.00 42.80  ? 1320 TRP   A CD2 1 
ATOM   2052 N NE1 . TRP   A 1 283 ? -11.926 -19.033 24.587  1.00 40.56  ? 1320 TRP   A NE1 1 
ATOM   2053 C CE2 . TRP   A 1 283 ? -12.069 -20.386 24.428  1.00 41.52  ? 1320 TRP   A CE2 1 
ATOM   2054 C CE3 . TRP   A 1 283 ? -13.837 -22.034 24.565  1.00 44.39  ? 1320 TRP   A CE3 1 
ATOM   2055 C CZ2 . TRP   A 1 283 ? -11.129 -21.362 24.100  1.00 41.80  ? 1320 TRP   A CZ2 1 
ATOM   2056 C CZ3 . TRP   A 1 283 ? -12.907 -22.997 24.241  1.00 44.61  ? 1320 TRP   A CZ3 1 
ATOM   2057 C CH2 . TRP   A 1 283 ? -11.571 -22.662 24.012  1.00 43.37  ? 1320 TRP   A CH2 1 
ATOM   2058 N N   . HIS   A 1 284 ? -17.728 -17.774 27.922  1.00 47.98  ? 1321 HIS   A N   1 
ATOM   2059 C CA  . HIS   A 1 284 ? -19.128 -17.619 28.280  1.00 50.56  ? 1321 HIS   A CA  1 
ATOM   2060 C C   . HIS   A 1 284 ? -19.706 -16.459 27.472  1.00 50.90  ? 1321 HIS   A C   1 
ATOM   2061 O O   . HIS   A 1 284 ? -19.080 -15.404 27.388  1.00 49.58  ? 1321 HIS   A O   1 
ATOM   2062 C CB  . HIS   A 1 284 ? -19.267 -17.388 29.792  1.00 51.90  ? 1321 HIS   A CB  1 
ATOM   2063 C CG  . HIS   A 1 284 ? -20.652 -17.563 30.338  1.00 55.31  ? 1321 HIS   A CG  1 
ATOM   2064 N ND1 . HIS   A 1 284 ? -21.715 -16.760 30.007  1.00 57.13  ? 1321 HIS   A ND1 1 
ATOM   2065 C CD2 . HIS   A 1 284 ? -21.117 -18.485 31.229  1.00 57.64  ? 1321 HIS   A CD2 1 
ATOM   2066 C CE1 . HIS   A 1 284 ? -22.798 -17.174 30.659  1.00 60.47  ? 1321 HIS   A CE1 1 
ATOM   2067 N NE2 . HIS   A 1 284 ? -22.449 -18.244 31.426  1.00 60.89  ? 1321 HIS   A NE2 1 
ATOM   2068 N N   . PRO   A 1 285 ? -20.892 -16.610 26.836  1.00 53.03  ? 1322 PRO   A N   1 
ATOM   2069 C CA  . PRO   A 1 285 ? -21.468 -15.535 26.024  1.00 53.78  ? 1322 PRO   A CA  1 
ATOM   2070 C C   . PRO   A 1 285 ? -21.701 -14.261 26.835  1.00 54.90  ? 1322 PRO   A C   1 
ATOM   2071 O O   . PRO   A 1 285 ? -21.399 -13.164 26.369  1.00 54.24  ? 1322 PRO   A O   1 
ATOM   2072 C CB  . PRO   A 1 285 ? -22.792 -16.114 25.497  1.00 56.61  ? 1322 PRO   A CB  1 
ATOM   2073 C CG  . PRO   A 1 285 ? -23.095 -17.288 26.409  1.00 58.08  ? 1322 PRO   A CG  1 
ATOM   2074 C CD  . PRO   A 1 285 ? -21.746 -17.807 26.863  1.00 55.29  ? 1322 PRO   A CD  1 
ATOM   2075 N N   . LYS   A 1 286 ? -22.241 -14.428 28.048  1.00 57.09  ? 1323 LYS   A N   1 
ATOM   2076 C CA  . LYS   A 1 286 ? -22.369 -13.341 29.006  1.00 58.57  ? 1323 LYS   A CA  1 
ATOM   2077 C C   . LYS   A 1 286 ? -20.983 -13.028 29.569  1.00 55.97  ? 1323 LYS   A C   1 
ATOM   2078 O O   . LYS   A 1 286 ? -20.322 -13.910 30.112  1.00 54.67  ? 1323 LYS   A O   1 
ATOM   2079 C CB  . LYS   A 1 286 ? -23.353 -13.734 30.114  1.00 62.10  ? 1323 LYS   A CB  1 
ATOM   2080 C CG  . LYS   A 1 286 ? -24.023 -12.572 30.834  1.00 65.17  ? 1323 LYS   A CG  1 
ATOM   2081 C CD  . LYS   A 1 286 ? -25.123 -11.915 30.027  1.00 67.76  ? 1323 LYS   A CD  1 
ATOM   2082 C CE  . LYS   A 1 286 ? -25.848 -10.825 30.788  1.00 71.49  ? 1323 LYS   A CE  1 
ATOM   2083 N NZ  . LYS   A 1 286 ? -26.924 -10.210 29.975  1.00 74.31  ? 1323 LYS   A NZ  1 
ATOM   2084 N N   . ALA   A 1 287 ? -20.554 -11.767 29.429  1.00 55.68  ? 1324 ALA   A N   1 
ATOM   2085 C CA  . ALA   A 1 287 ? -19.196 -11.361 29.762  1.00 53.72  ? 1324 ALA   A CA  1 
ATOM   2086 C C   . ALA   A 1 287 ? -18.987 -11.353 31.275  1.00 55.06  ? 1324 ALA   A C   1 
ATOM   2087 O O   . ALA   A 1 287 ? -17.936 -11.768 31.759  1.00 53.16  ? 1324 ALA   A O   1 
ATOM   2088 C CB  . ALA   A 1 287 ? -18.907 -10.006 29.162  1.00 53.70  ? 1324 ALA   A CB  1 
ATOM   2089 N N   . GLU   A 1 288 ? -19.999 -10.875 32.010  1.00 58.68  ? 1325 GLU   A N   1 
ATOM   2090 C CA  . GLU   A 1 288 ? -19.937 -10.764 33.459  1.00 60.68  ? 1325 GLU   A CA  1 
ATOM   2091 C C   . GLU   A 1 288 ? -19.787 -12.143 34.101  1.00 60.19  ? 1325 GLU   A C   1 
ATOM   2092 O O   . GLU   A 1 288 ? -19.220 -12.258 35.185  1.00 60.69  ? 1325 GLU   A O   1 
ATOM   2093 C CB  . GLU   A 1 288 ? -21.191 -10.055 33.980  1.00 65.11  ? 1325 GLU   A CB  1 
ATOM   2094 C CG  . GLU   A 1 288 ? -22.466 -10.867 33.814  1.00 67.62  ? 1325 GLU   A CG  1 
ATOM   2095 C CD  . GLU   A 1 288 ? -23.763 -10.087 33.954  1.00 72.30  ? 1325 GLU   A CD  1 
ATOM   2096 O OE1 . GLU   A 1 288 ? -23.701 -8.860  34.180  1.00 74.06  ? 1325 GLU   A OE1 1 
ATOM   2097 O OE2 . GLU   A 1 288 ? -24.838 -10.711 33.835  1.00 74.96  ? 1325 GLU   A OE2 1 
ATOM   2098 N N   . MET   A 1 289 ? -20.299 -13.180 33.423  1.00 59.60  ? 1326 MET   A N   1 
ATOM   2099 C CA  . MET   A 1 289 ? -20.320 -14.535 33.953  1.00 59.86  ? 1326 MET   A CA  1 
ATOM   2100 C C   . MET   A 1 289 ? -18.939 -15.184 33.852  1.00 56.24  ? 1326 MET   A C   1 
ATOM   2101 O O   . MET   A 1 289 ? -18.694 -16.202 34.496  1.00 56.33  ? 1326 MET   A O   1 
ATOM   2102 C CB  . MET   A 1 289 ? -21.332 -15.396 33.188  1.00 61.33  ? 1326 MET   A CB  1 
ATOM   2103 C CG  . MET   A 1 289 ? -22.784 -15.084 33.524  1.00 65.67  ? 1326 MET   A CG  1 
ATOM   2104 S SD  . MET   A 1 289 ? -23.231 -15.338 35.267  1.00 69.90  ? 1326 MET   A SD  1 
ATOM   2105 C CE  . MET   A 1 289 ? -22.357 -16.857 35.640  1.00 68.37  ? 1326 MET   A CE  1 
ATOM   2106 N N   . ARG   A 1 290 ? -18.049 -14.601 33.038  1.00 53.25  ? 1327 ARG   A N   1 
ATOM   2107 C CA  . ARG   A 1 290 ? -16.707 -15.132 32.847  1.00 50.58  ? 1327 ARG   A CA  1 
ATOM   2108 C C   . ARG   A 1 290 ? -15.882 -14.914 34.113  1.00 50.86  ? 1327 ARG   A C   1 
ATOM   2109 O O   . ARG   A 1 290 ? -16.104 -13.947 34.839  1.00 52.54  ? 1327 ARG   A O   1 
ATOM   2110 C CB  . ARG   A 1 290 ? -16.030 -14.457 31.649  1.00 48.28  ? 1327 ARG   A CB  1 
ATOM   2111 C CG  . ARG   A 1 290 ? -16.751 -14.663 30.325  1.00 48.00  ? 1327 ARG   A CG  1 
ATOM   2112 C CD  . ARG   A 1 290 ? -16.262 -13.716 29.246  1.00 46.55  ? 1327 ARG   A CD  1 
ATOM   2113 N NE  . ARG   A 1 290 ? -17.120 -13.748 28.070  1.00 46.92  ? 1327 ARG   A NE  1 
ATOM   2114 C CZ  . ARG   A 1 290 ? -17.091 -12.854 27.088  1.00 46.77  ? 1327 ARG   A CZ  1 
ATOM   2115 N NH1 . ARG   A 1 290 ? -16.208 -11.870 27.109  1.00 46.11  ? 1327 ARG   A NH1 1 
ATOM   2116 N NH2 . ARG   A 1 290 ? -17.948 -12.948 26.086  1.00 47.61  ? 1327 ARG   A NH2 1 
ATOM   2117 N N   . PRO   A 1 291 ? -14.898 -15.796 34.411  1.00 49.60  ? 1328 PRO   A N   1 
ATOM   2118 C CA  . PRO   A 1 291 ? -14.080 -15.667 35.618  1.00 50.22  ? 1328 PRO   A CA  1 
ATOM   2119 C C   . PRO   A 1 291 ? -12.982 -14.615 35.481  1.00 48.93  ? 1328 PRO   A C   1 
ATOM   2120 O O   . PRO   A 1 291 ? -12.504 -14.352 34.380  1.00 47.01  ? 1328 PRO   A O   1 
ATOM   2121 C CB  . PRO   A 1 291 ? -13.473 -17.070 35.761  1.00 49.75  ? 1328 PRO   A CB  1 
ATOM   2122 C CG  . PRO   A 1 291 ? -13.327 -17.549 34.334  1.00 47.64  ? 1328 PRO   A CG  1 
ATOM   2123 C CD  . PRO   A 1 291 ? -14.518 -16.964 33.601  1.00 48.02  ? 1328 PRO   A CD  1 
ATOM   2124 N N   . SER   A 1 292 ? -12.589 -14.023 36.615  1.00 50.49  ? 1329 SER   A N   1 
ATOM   2125 C CA  . SER   A 1 292 ? -11.502 -13.058 36.649  1.00 50.04  ? 1329 SER   A CA  1 
ATOM   2126 C C   . SER   A 1 292 ? -10.166 -13.790 36.570  1.00 48.80  ? 1329 SER   A C   1 
ATOM   2127 O O   . SER   A 1 292 ? -10.105 -15.000 36.773  1.00 48.78  ? 1329 SER   A O   1 
ATOM   2128 C CB  . SER   A 1 292 ? -11.582 -12.194 37.883  1.00 52.71  ? 1329 SER   A CB  1 
ATOM   2129 O OG  . SER   A 1 292 ? -11.465 -12.978 39.061  1.00 54.32  ? 1329 SER   A OG  1 
ATOM   2130 N N   . PHE   A 1 293 ? -9.099  -13.036 36.284  1.00 48.38  ? 1330 PHE   A N   1 
ATOM   2131 C CA  . PHE   A 1 293 ? -7.761  -13.595 36.168  1.00 47.84  ? 1330 PHE   A CA  1 
ATOM   2132 C C   . PHE   A 1 293 ? -7.282  -14.100 37.528  1.00 49.80  ? 1330 PHE   A C   1 
ATOM   2133 O O   . PHE   A 1 293 ? -6.537  -15.075 37.595  1.00 49.58  ? 1330 PHE   A O   1 
ATOM   2134 C CB  . PHE   A 1 293 ? -6.802  -12.564 35.567  1.00 47.57  ? 1330 PHE   A CB  1 
ATOM   2135 C CG  . PHE   A 1 293 ? -7.003  -12.322 34.092  1.00 45.93  ? 1330 PHE   A CG  1 
ATOM   2136 C CD1 . PHE   A 1 293 ? -6.688  -13.304 33.164  1.00 44.33  ? 1330 PHE   A CD1 1 
ATOM   2137 C CD2 . PHE   A 1 293 ? -7.525  -11.123 33.630  1.00 46.33  ? 1330 PHE   A CD2 1 
ATOM   2138 C CE1 . PHE   A 1 293 ? -6.877  -13.087 31.808  1.00 43.11  ? 1330 PHE   A CE1 1 
ATOM   2139 C CE2 . PHE   A 1 293 ? -7.715  -10.908 32.272  1.00 45.06  ? 1330 PHE   A CE2 1 
ATOM   2140 C CZ  . PHE   A 1 293 ? -7.391  -11.890 31.365  1.00 43.43  ? 1330 PHE   A CZ  1 
ATOM   2141 N N   . SER   A 1 294 ? -7.714  -13.427 38.602  1.00 52.19  ? 1331 SER   A N   1 
ATOM   2142 C CA  . SER   A 1 294 ? -7.460  -13.883 39.960  1.00 54.70  ? 1331 SER   A CA  1 
ATOM   2143 C C   . SER   A 1 294 ? -8.111  -15.246 40.188  1.00 55.30  ? 1331 SER   A C   1 
ATOM   2144 O O   . SER   A 1 294 ? -7.519  -16.121 40.817  1.00 56.30  ? 1331 SER   A O   1 
ATOM   2145 C CB  . SER   A 1 294 ? -7.947  -12.870 40.965  1.00 57.28  ? 1331 SER   A CB  1 
ATOM   2146 O OG  . SER   A 1 294 ? -7.706  -13.314 42.293  1.00 59.78  ? 1331 SER   A OG  1 
ATOM   2147 N N   . GLU   A 1 295 ? -9.335  -15.406 39.669  1.00 55.13  ? 1332 GLU   A N   1 
ATOM   2148 C CA  . GLU   A 1 295 ? -10.093 -16.639 39.808  1.00 55.99  ? 1332 GLU   A CA  1 
ATOM   2149 C C   . GLU   A 1 295 ? -9.446  -17.746 38.977  1.00 54.12  ? 1332 GLU   A C   1 
ATOM   2150 O O   . GLU   A 1 295 ? -9.403  -18.894 39.410  1.00 55.23  ? 1332 GLU   A O   1 
ATOM   2151 C CB  . GLU   A 1 295 ? -11.547 -16.411 39.385  1.00 56.56  ? 1332 GLU   A CB  1 
ATOM   2152 C CG  . GLU   A 1 295 ? -12.494 -17.514 39.824  1.00 58.82  ? 1332 GLU   A CG  1 
ATOM   2153 C CD  . GLU   A 1 295 ? -13.955 -17.256 39.492  1.00 60.12  ? 1332 GLU   A CD  1 
ATOM   2154 O OE1 . GLU   A 1 295 ? -14.469 -16.189 39.883  1.00 61.50  ? 1332 GLU   A OE1 1 
ATOM   2155 O OE2 . GLU   A 1 295 ? -14.578 -18.125 38.849  1.00 60.26  ? 1332 GLU   A OE2 1 
ATOM   2156 N N   . LEU   A 1 296 ? -8.946  -17.391 37.786  1.00 51.82  ? 1333 LEU   A N   1 
ATOM   2157 C CA  . LEU   A 1 296 ? -8.334  -18.356 36.885  1.00 50.63  ? 1333 LEU   A CA  1 
ATOM   2158 C C   . LEU   A 1 296 ? -7.028  -18.885 37.475  1.00 51.50  ? 1333 LEU   A C   1 
ATOM   2159 O O   . LEU   A 1 296 ? -6.770  -20.086 37.414  1.00 52.24  ? 1333 LEU   A O   1 
ATOM   2160 C CB  . LEU   A 1 296 ? -8.090  -17.705 35.518  1.00 48.48  ? 1333 LEU   A CB  1 
ATOM   2161 C CG  . LEU   A 1 296 ? -9.328  -17.499 34.644  1.00 47.77  ? 1333 LEU   A CG  1 
ATOM   2162 C CD1 . LEU   A 1 296 ? -8.935  -17.003 33.261  1.00 45.89  ? 1333 LEU   A CD1 1 
ATOM   2163 C CD2 . LEU   A 1 296 ? -10.146 -18.778 34.533  1.00 48.53  ? 1333 LEU   A CD2 1 
ATOM   2164 N N   . VAL   A 1 297 ? -6.210  -17.985 38.035  1.00 51.94  ? 1334 VAL   A N   1 
ATOM   2165 C CA  . VAL   A 1 297 ? -4.938  -18.363 38.633  1.00 53.19  ? 1334 VAL   A CA  1 
ATOM   2166 C C   . VAL   A 1 297 ? -5.176  -19.455 39.675  1.00 55.51  ? 1334 VAL   A C   1 
ATOM   2167 O O   . VAL   A 1 297 ? -4.431  -20.431 39.727  1.00 56.17  ? 1334 VAL   A O   1 
ATOM   2168 C CB  . VAL   A 1 297 ? -4.213  -17.144 39.240  1.00 54.05  ? 1334 VAL   A CB  1 
ATOM   2169 C CG1 . VAL   A 1 297 ? -3.047  -17.554 40.130  1.00 56.15  ? 1334 VAL   A CG1 1 
ATOM   2170 C CG2 . VAL   A 1 297 ? -3.746  -16.171 38.166  1.00 52.31  ? 1334 VAL   A CG2 1 
ATOM   2171 N N   . SER   A 1 298 ? -6.225  -19.282 40.491  1.00 57.12  ? 1335 SER   A N   1 
ATOM   2172 C CA  . SER   A 1 298 ? -6.560  -20.220 41.551  1.00 59.93  ? 1335 SER   A CA  1 
ATOM   2173 C C   . SER   A 1 298 ? -6.866  -21.604 40.979  1.00 60.13  ? 1335 SER   A C   1 
ATOM   2174 O O   . SER   A 1 298 ? -6.433  -22.611 41.536  1.00 61.99  ? 1335 SER   A O   1 
ATOM   2175 C CB  . SER   A 1 298 ? -7.715  -19.708 42.372  1.00 61.53  ? 1335 SER   A CB  1 
ATOM   2176 O OG  . SER   A 1 298 ? -7.432  -18.419 42.896  1.00 61.98  ? 1335 SER   A OG  1 
ATOM   2177 N N   . ARG   A 1 299 ? -7.618  -21.639 39.870  1.00 58.59  ? 1336 ARG   A N   1 
ATOM   2178 C CA  . ARG   A 1 299 ? -8.035  -22.887 39.248  1.00 59.06  ? 1336 ARG   A CA  1 
ATOM   2179 C C   . ARG   A 1 299 ? -6.829  -23.620 38.665  1.00 58.21  ? 1336 ARG   A C   1 
ATOM   2180 O O   . ARG   A 1 299 ? -6.643  -24.807 38.923  1.00 60.25  ? 1336 ARG   A O   1 
ATOM   2181 C CB  . ARG   A 1 299 ? -9.061  -22.627 38.139  1.00 57.91  ? 1336 ARG   A CB  1 
ATOM   2182 C CG  . ARG   A 1 299 ? -10.397 -22.084 38.625  1.00 59.67  ? 1336 ARG   A CG  1 
ATOM   2183 C CD  . ARG   A 1 299 ? -11.330 -21.771 37.468  1.00 58.65  ? 1336 ARG   A CD  1 
ATOM   2184 N NE  . ARG   A 1 299 ? -12.547 -21.082 37.881  1.00 60.45  ? 1336 ARG   A NE  1 
ATOM   2185 C CZ  . ARG   A 1 299 ? -13.512 -21.619 38.622  1.00 63.76  ? 1336 ARG   A CZ  1 
ATOM   2186 N NH1 . ARG   A 1 299 ? -14.542 -20.881 38.999  1.00 65.43  ? 1336 ARG   A NH1 1 
ATOM   2187 N NH2 . ARG   A 1 299 ? -13.449 -22.889 38.984  1.00 65.65  ? 1336 ARG   A NH2 1 
ATOM   2188 N N   . ILE   A 1 300 ? -6.019  -22.900 37.879  1.00 55.67  ? 1337 ILE   A N   1 
ATOM   2189 C CA  . ILE   A 1 300 ? -4.937  -23.503 37.115  1.00 55.05  ? 1337 ILE   A CA  1 
ATOM   2190 C C   . ILE   A 1 300 ? -3.798  -23.901 38.053  1.00 57.00  ? 1337 ILE   A C   1 
ATOM   2191 O O   . ILE   A 1 300 ? -3.032  -24.809 37.737  1.00 57.95  ? 1337 ILE   A O   1 
ATOM   2192 C CB  . ILE   A 1 300 ? -4.464  -22.556 35.991  1.00 52.65  ? 1337 ILE   A CB  1 
ATOM   2193 C CG1 . ILE   A 1 300 ? -5.601  -22.220 35.020  1.00 50.80  ? 1337 ILE   A CG1 1 
ATOM   2194 C CG2 . ILE   A 1 300 ? -3.261  -23.139 35.261  1.00 52.86  ? 1337 ILE   A CG2 1 
ATOM   2195 C CD1 . ILE   A 1 300 ? -5.255  -21.155 34.005  1.00 48.86  ? 1337 ILE   A CD1 1 
ATOM   2196 N N   . SER   A 1 301 ? -3.690  -23.217 39.199  1.00 57.90  ? 1338 SER   A N   1 
ATOM   2197 C CA  . SER   A 1 301 ? -2.709  -23.564 40.217  1.00 60.43  ? 1338 SER   A CA  1 
ATOM   2198 C C   . SER   A 1 301 ? -2.955  -24.980 40.735  1.00 62.87  ? 1338 SER   A C   1 
ATOM   2199 O O   . SER   A 1 301 ? -2.008  -25.732 40.955  1.00 64.66  ? 1338 SER   A O   1 
ATOM   2200 C CB  . SER   A 1 301 ? -2.723  -22.563 41.344  1.00 61.57  ? 1338 SER   A CB  1 
ATOM   2201 O OG  . SER   A 1 301 ? -2.296  -21.286 40.892  1.00 59.97  ? 1338 SER   A OG  1 
ATOM   2202 N N   . ALA   A 1 302 ? -4.235  -25.326 40.928  1.00 63.19  ? 1339 ALA   A N   1 
ATOM   2203 C CA  . ALA   A 1 302 ? -4.628  -26.643 41.404  1.00 65.88  ? 1339 ALA   A CA  1 
ATOM   2204 C C   . ALA   A 1 302 ? -4.386  -27.695 40.323  1.00 65.50  ? 1339 ALA   A C   1 
ATOM   2205 O O   . ALA   A 1 302 ? -4.000  -28.820 40.631  1.00 68.44  ? 1339 ALA   A O   1 
ATOM   2206 C CB  . ALA   A 1 302 ? -6.077  -26.622 41.829  1.00 66.70  ? 1339 ALA   A CB  1 
ATOM   2207 N N   . ILE   A 1 303 ? -4.626  -27.316 39.060  1.00 62.35  ? 1340 ILE   A N   1 
ATOM   2208 C CA  . ILE   A 1 303 ? -4.450  -28.213 37.928  1.00 62.13  ? 1340 ILE   A CA  1 
ATOM   2209 C C   . ILE   A 1 303 ? -2.959  -28.456 37.700  1.00 62.75  ? 1340 ILE   A C   1 
ATOM   2210 O O   . ILE   A 1 303 ? -2.548  -29.587 37.449  1.00 64.82  ? 1340 ILE   A O   1 
ATOM   2211 C CB  . ILE   A 1 303 ? -5.143  -27.649 36.670  1.00 59.13  ? 1340 ILE   A CB  1 
ATOM   2212 C CG1 . ILE   A 1 303 ? -6.656  -27.518 36.868  1.00 59.15  ? 1340 ILE   A CG1 1 
ATOM   2213 C CG2 . ILE   A 1 303 ? -4.811  -28.491 35.445  1.00 59.23  ? 1340 ILE   A CG2 1 
ATOM   2214 C CD1 . ILE   A 1 303 ? -7.360  -26.742 35.778  1.00 56.39  ? 1340 ILE   A CD1 1 
ATOM   2215 N N   . PHE   A 1 304 ? -2.161  -27.383 37.788  1.00 61.40  ? 1341 PHE   A N   1 
ATOM   2216 C CA  . PHE   A 1 304 ? -0.723  -27.449 37.572  1.00 62.32  ? 1341 PHE   A CA  1 
ATOM   2217 C C   . PHE   A 1 304 ? -0.065  -28.358 38.610  1.00 66.36  ? 1341 PHE   A C   1 
ATOM   2218 O O   . PHE   A 1 304 ? 0.854   -29.107 38.283  1.00 68.32  ? 1341 PHE   A O   1 
ATOM   2219 C CB  . PHE   A 1 304 ? -0.118  -26.043 37.616  1.00 60.43  ? 1341 PHE   A CB  1 
ATOM   2220 C CG  . PHE   A 1 304 ? 1.386   -25.993 37.512  1.00 61.73  ? 1341 PHE   A CG  1 
ATOM   2221 C CD1 . PHE   A 1 304 ? 2.038   -26.464 36.382  1.00 61.77  ? 1341 PHE   A CD1 1 
ATOM   2222 C CD2 . PHE   A 1 304 ? 2.152   -25.476 38.546  1.00 63.39  ? 1341 PHE   A CD2 1 
ATOM   2223 C CE1 . PHE   A 1 304 ? 3.421   -26.417 36.289  1.00 63.54  ? 1341 PHE   A CE1 1 
ATOM   2224 C CE2 . PHE   A 1 304 ? 3.535   -25.431 38.452  1.00 65.11  ? 1341 PHE   A CE2 1 
ATOM   2225 C CZ  . PHE   A 1 304 ? 4.167   -25.899 37.323  1.00 65.19  ? 1341 PHE   A CZ  1 
ATOM   2226 N N   . SER   A 1 305 ? -0.551  -28.289 39.856  1.00 68.00  ? 1342 SER   A N   1 
ATOM   2227 C CA  . SER   A 1 305 ? 0.049   -29.006 40.971  1.00 71.92  ? 1342 SER   A CA  1 
ATOM   2228 C C   . SER   A 1 305 ? -0.342  -30.485 40.966  1.00 74.78  ? 1342 SER   A C   1 
ATOM   2229 O O   . SER   A 1 305 ? 0.215   -31.264 41.738  1.00 78.41  ? 1342 SER   A O   1 
ATOM   2230 C CB  . SER   A 1 305 ? -0.320  -28.352 42.279  1.00 72.83  ? 1342 SER   A CB  1 
ATOM   2231 O OG  . SER   A 1 305 ? -1.730  -28.283 42.432  1.00 72.09  ? 1342 SER   A OG  1 
ATOM   2232 N N   . THR   A 1 306 ? -1.293  -30.869 40.101  1.00 73.60  ? 1343 THR   A N   1 
ATOM   2233 C CA  . THR   A 1 306 ? -1.706  -32.258 39.967  1.00 76.67  ? 1343 THR   A CA  1 
ATOM   2234 C C   . THR   A 1 306 ? -1.073  -32.880 38.720  1.00 77.02  ? 1343 THR   A C   1 
ATOM   2235 O O   . THR   A 1 306 ? -1.699  -33.700 38.050  1.00 77.74  ? 1343 THR   A O   1 
ATOM   2236 C CB  . THR   A 1 306 ? -3.237  -32.373 39.943  1.00 76.10  ? 1343 THR   A CB  1 
ATOM   2237 O OG1 . THR   A 1 306 ? -3.727  -31.598 38.847  1.00 72.15  ? 1343 THR   A OG1 1 
ATOM   2238 C CG2 . THR   A 1 306 ? -3.887  -31.910 41.229  1.00 77.01  ? 1343 THR   A CG2 1 
ATOM   2239 N N   . PHE   A 1 307 ? 0.175   -32.488 38.426  1.00 77.03  ? 1344 PHE   A N   1 
ATOM   2240 C CA  . PHE   A 1 307 ? 0.950   -33.067 37.339  1.00 78.11  ? 1344 PHE   A CA  1 
ATOM   2241 C C   . PHE   A 1 307 ? 2.351   -33.409 37.840  1.00 81.75  ? 1344 PHE   A C   1 
ATOM   2242 O O   . PHE   A 1 307 ? 2.917   -32.679 38.652  1.00 81.79  ? 1344 PHE   A O   1 
ATOM   2243 C CB  . PHE   A 1 307 ? 1.012   -32.113 36.141  1.00 74.24  ? 1344 PHE   A CB  1 
ATOM   2244 C CG  . PHE   A 1 307 ? -0.063  -32.332 35.107  1.00 72.39  ? 1344 PHE   A CG  1 
ATOM   2245 C CD1 . PHE   A 1 307 ? -1.391  -32.047 35.386  1.00 70.73  ? 1344 PHE   A CD1 1 
ATOM   2246 C CD2 . PHE   A 1 307 ? 0.253   -32.845 33.857  1.00 72.77  ? 1344 PHE   A CD2 1 
ATOM   2247 C CE1 . PHE   A 1 307 ? -2.376  -32.257 34.433  1.00 69.57  ? 1344 PHE   A CE1 1 
ATOM   2248 C CE2 . PHE   A 1 307 ? -0.733  -33.056 32.906  1.00 71.52  ? 1344 PHE   A CE2 1 
ATOM   2249 C CZ  . PHE   A 1 307 ? -2.045  -32.762 33.196  1.00 69.95  ? 1344 PHE   A CZ  1 
ATOM   2250 N N   . ILE   A 1 308 ? 2.900   -34.521 37.334  1.00 85.35  ? 1345 ILE   A N   1 
ATOM   2251 C CA  . ILE   A 1 308 ? 4.193   -35.025 37.771  1.00 89.63  ? 1345 ILE   A CA  1 
ATOM   2252 C C   . ILE   A 1 308 ? 5.283   -34.354 36.936  1.00 88.81  ? 1345 ILE   A C   1 
ATOM   2253 O O   . ILE   A 1 308 ? 5.178   -34.291 35.712  1.00 87.13  ? 1345 ILE   A O   1 
ATOM   2254 C CB  . ILE   A 1 308 ? 4.260   -36.565 37.674  1.00 94.28  ? 1345 ILE   A CB  1 
ATOM   2255 C CG1 . ILE   A 1 308 ? 3.192   -37.250 38.535  1.00 95.91  ? 1345 ILE   A CG1 1 
ATOM   2256 C CG2 . ILE   A 1 308 ? 5.658   -37.067 38.017  1.00 98.64  ? 1345 ILE   A CG2 1 
ATOM   2257 C CD1 . ILE   A 1 308 ? 1.801   -37.251 37.935  1.00 93.21  ? 1345 ILE   A CD1 1 
ATOM   2258 N N   . GLY   A 1 309 ? 6.327   -33.863 37.616  1.00 90.40  ? 1346 GLY   A N   1 
ATOM   2259 C CA  . GLY   A 1 309 ? 7.443   -33.201 36.962  1.00 90.23  ? 1346 GLY   A CA  1 
ATOM   2260 C C   . GLY   A 1 309 ? 8.108   -32.186 37.875  1.00 90.21  ? 1346 GLY   A C   1 
ATOM   2261 O O   . GLY   A 1 309 ? 8.886   -32.630 38.746  1.00 94.28  ? 1346 GLY   A O   1 
ATOM   2262 O OXT . GLY   A 1 309 ? 7.827   -30.984 37.688  1.00 86.39  ? 1346 GLY   A OXT 1 
ATOM   2263 N N   . THR   B 1 13  ? -0.480  31.704  7.121   1.00 137.76 ? 1050 THR   B N   1 
ATOM   2264 C CA  . THR   B 1 13  ? -1.905  31.614  6.700   1.00 131.22 ? 1050 THR   B CA  1 
ATOM   2265 C C   . THR   B 1 13  ? -2.019  31.951  5.214   1.00 129.39 ? 1050 THR   B C   1 
ATOM   2266 O O   . THR   B 1 13  ? -1.062  32.429  4.607   1.00 132.89 ? 1050 THR   B O   1 
ATOM   2267 C CB  . THR   B 1 13  ? -2.791  32.522  7.564   1.00 129.30 ? 1050 THR   B CB  1 
ATOM   2268 O OG1 . THR   B 1 13  ? -2.355  33.872  7.396   1.00 131.42 ? 1050 THR   B OG1 1 
ATOM   2269 C CG2 . THR   B 1 13  ? -2.757  32.155  9.031   1.00 131.62 ? 1050 THR   B CG2 1 
ATOM   2270 N N   . VAL   B 1 14  ? -3.204  31.694  4.646   1.00 124.52 ? 1051 VAL   B N   1 
ATOM   2271 C CA  . VAL   B 1 14  ? -3.449  31.864  3.222   1.00 122.72 ? 1051 VAL   B CA  1 
ATOM   2272 C C   . VAL   B 1 14  ? -4.046  33.249  2.980   1.00 121.03 ? 1051 VAL   B C   1 
ATOM   2273 O O   . VAL   B 1 14  ? -5.194  33.503  3.341   1.00 117.43 ? 1051 VAL   B O   1 
ATOM   2274 C CB  . VAL   B 1 14  ? -4.372  30.752  2.684   1.00 118.94 ? 1051 VAL   B CB  1 
ATOM   2275 C CG1 . VAL   B 1 14  ? -4.639  30.908  1.193   1.00 117.69 ? 1051 VAL   B CG1 1 
ATOM   2276 C CG2 . VAL   B 1 14  ? -3.821  29.365  2.987   1.00 120.54 ? 1051 VAL   B CG2 1 
ATOM   2277 N N   . HIS   B 1 15  ? -3.254  34.134  2.359   1.00 123.87 ? 1052 HIS   B N   1 
ATOM   2278 C CA  . HIS   B 1 15  ? -3.704  35.469  1.998   1.00 122.72 ? 1052 HIS   B CA  1 
ATOM   2279 C C   . HIS   B 1 15  ? -4.388  35.428  0.633   1.00 120.06 ? 1052 HIS   B C   1 
ATOM   2280 O O   . HIS   B 1 15  ? -3.721  35.316  -0.393  1.00 122.24 ? 1052 HIS   B O   1 
ATOM   2281 C CB  . HIS   B 1 15  ? -2.524  36.450  1.995   1.00 127.66 ? 1052 HIS   B CB  1 
ATOM   2282 C CG  . HIS   B 1 15  ? -1.877  36.660  3.330   1.00 130.87 ? 1052 HIS   B CG  1 
ATOM   2283 N ND1 . HIS   B 1 15  ? -2.548  37.108  4.442   1.00 129.12 ? 1052 HIS   B ND1 1 
ATOM   2284 C CD2 . HIS   B 1 15  ? -0.579  36.467  3.702   1.00 136.43 ? 1052 HIS   B CD2 1 
ATOM   2285 C CE1 . HIS   B 1 15  ? -1.698  37.189  5.463   1.00 133.66 ? 1052 HIS   B CE1 1 
ATOM   2286 N NE2 . HIS   B 1 15  ? -0.469  36.796  5.025   1.00 138.29 ? 1052 HIS   B NE2 1 
ATOM   2287 N N   . ILE   B 1 16  ? -5.724  35.522  0.640   1.00 116.01 ? 1053 ILE   B N   1 
ATOM   2288 C CA  . ILE   B 1 16  ? -6.516  35.487  -0.579  1.00 114.10 ? 1053 ILE   B CA  1 
ATOM   2289 C C   . ILE   B 1 16  ? -6.850  36.919  -0.988  1.00 114.16 ? 1053 ILE   B C   1 
ATOM   2290 O O   . ILE   B 1 16  ? -7.324  37.705  -0.170  1.00 113.02 ? 1053 ILE   B O   1 
ATOM   2291 C CB  . ILE   B 1 16  ? -7.792  34.641  -0.383  1.00 110.36 ? 1053 ILE   B CB  1 
ATOM   2292 C CG1 . ILE   B 1 16  ? -7.471  33.236  0.138   1.00 110.68 ? 1053 ILE   B CG1 1 
ATOM   2293 C CG2 . ILE   B 1 16  ? -8.610  34.597  -1.667  1.00 108.73 ? 1053 ILE   B CG2 1 
ATOM   2294 C CD1 . ILE   B 1 16  ? -8.689  32.409  0.484   1.00 107.39 ? 1053 ILE   B CD1 1 
ATOM   2295 N N   . ASP   B 1 17  ? -6.599  37.242  -2.264  1.00 115.85 ? 1054 ASP   B N   1 
ATOM   2296 C CA  . ASP   B 1 17  ? -6.962  38.533  -2.826  1.00 116.11 ? 1054 ASP   B CA  1 
ATOM   2297 C C   . ASP   B 1 17  ? -8.456  38.514  -3.144  1.00 112.04 ? 1054 ASP   B C   1 
ATOM   2298 O O   . ASP   B 1 17  ? -8.854  38.166  -4.253  1.00 111.69 ? 1054 ASP   B O   1 
ATOM   2299 C CB  . ASP   B 1 17  ? -6.108  38.856  -4.056  1.00 120.19 ? 1054 ASP   B CB  1 
ATOM   2300 C CG  . ASP   B 1 17  ? -6.334  40.252  -4.613  1.00 121.26 ? 1054 ASP   B CG  1 
ATOM   2301 O OD1 . ASP   B 1 17  ? -6.078  41.225  -3.876  1.00 122.06 ? 1054 ASP   B OD1 1 
ATOM   2302 O OD2 . ASP   B 1 17  ? -6.764  40.354  -5.779  1.00 121.65 ? 1054 ASP   B OD2 1 
ATOM   2303 N N   . LEU   B 1 18  ? -9.270  38.901  -2.153  1.00 109.47 ? 1055 LEU   B N   1 
ATOM   2304 C CA  . LEU   B 1 18  ? -10.720 38.777  -2.229  1.00 106.08 ? 1055 LEU   B CA  1 
ATOM   2305 C C   . LEU   B 1 18  ? -11.326 39.809  -3.185  1.00 105.58 ? 1055 LEU   B C   1 
ATOM   2306 O O   . LEU   B 1 18  ? -12.515 39.733  -3.488  1.00 103.79 ? 1055 LEU   B O   1 
ATOM   2307 C CB  . LEU   B 1 18  ? -11.320 38.872  -0.816  1.00 104.39 ? 1055 LEU   B CB  1 
ATOM   2308 C CG  . LEU   B 1 18  ? -11.448 40.252  -0.155  1.00 104.82 ? 1055 LEU   B CG  1 
ATOM   2309 C CD1 . LEU   B 1 18  ? -10.166 41.069  -0.251  1.00 108.18 ? 1055 LEU   B CD1 1 
ATOM   2310 C CD2 . LEU   B 1 18  ? -12.629 41.040  -0.712  1.00 103.20 ? 1055 LEU   B CD2 1 
ATOM   2311 N N   . SER   B 1 19  ? -10.508 40.750  -3.679  1.00 107.29 ? 1056 SER   B N   1 
ATOM   2312 C CA  . SER   B 1 19  ? -10.972 41.778  -4.599  1.00 107.05 ? 1056 SER   B CA  1 
ATOM   2313 C C   . SER   B 1 19  ? -10.871 41.312  -6.053  1.00 108.05 ? 1056 SER   B C   1 
ATOM   2314 O O   . SER   B 1 19  ? -11.122 42.096  -6.966  1.00 109.28 ? 1056 SER   B O   1 
ATOM   2315 C CB  . SER   B 1 19  ? -10.202 43.058  -4.385  1.00 109.43 ? 1056 SER   B CB  1 
ATOM   2316 O OG  . SER   B 1 19  ? -8.812  42.854  -4.590  1.00 112.98 ? 1056 SER   B OG  1 
ATOM   2317 N N   . ALA   B 1 20  ? -10.518 40.036  -6.262  1.00 107.40 ? 1057 ALA   B N   1 
ATOM   2318 C CA  . ALA   B 1 20  ? -10.292 39.497  -7.594  1.00 109.18 ? 1057 ALA   B CA  1 
ATOM   2319 C C   . ALA   B 1 20  ? -11.572 38.888  -8.168  1.00 106.87 ? 1057 ALA   B C   1 
ATOM   2320 O O   . ALA   B 1 20  ? -11.612 38.548  -9.349  1.00 108.80 ? 1057 ALA   B O   1 
ATOM   2321 C CB  . ALA   B 1 20  ? -9.184  38.473  -7.541  1.00 110.93 ? 1057 ALA   B CB  1 
ATOM   2322 N N   . LEU   B 1 21  ? -12.613 38.752  -7.335  1.00 103.00 ? 1058 LEU   B N   1 
ATOM   2323 C CA  . LEU   B 1 21  ? -13.843 38.090  -7.744  1.00 101.53 ? 1058 LEU   B CA  1 
ATOM   2324 C C   . LEU   B 1 21  ? -14.620 38.972  -8.720  1.00 102.81 ? 1058 LEU   B C   1 
ATOM   2325 O O   . LEU   B 1 21  ? -14.460 40.191  -8.734  1.00 103.51 ? 1058 LEU   B O   1 
ATOM   2326 C CB  . LEU   B 1 21  ? -14.685 37.760  -6.506  1.00 98.23  ? 1058 LEU   B CB  1 
ATOM   2327 C CG  . LEU   B 1 21  ? -14.310 36.467  -5.782  1.00 97.15  ? 1058 LEU   B CG  1 
ATOM   2328 C CD1 . LEU   B 1 21  ? -12.939 36.578  -5.133  1.00 98.04  ? 1058 LEU   B CD1 1 
ATOM   2329 C CD2 . LEU   B 1 21  ? -15.362 36.101  -4.746  1.00 94.65  ? 1058 LEU   B CD2 1 
ATOM   2330 N N   . ASN   B 1 22  ? -15.467 38.321  -9.527  1.00 103.54 ? 1059 ASN   B N   1 
ATOM   2331 C CA  . ASN   B 1 22  ? -16.273 38.981  -10.542 1.00 105.74 ? 1059 ASN   B CA  1 
ATOM   2332 C C   . ASN   B 1 22  ? -17.355 39.812  -9.852  1.00 103.72 ? 1059 ASN   B C   1 
ATOM   2333 O O   . ASN   B 1 22  ? -18.102 39.281  -9.034  1.00 101.33 ? 1059 ASN   B O   1 
ATOM   2334 C CB  . ASN   B 1 22  ? -16.872 37.946  -11.502 1.00 107.66 ? 1059 ASN   B CB  1 
ATOM   2335 C CG  . ASN   B 1 22  ? -17.644 38.538  -12.664 1.00 110.88 ? 1059 ASN   B CG  1 
ATOM   2336 O OD1 . ASN   B 1 22  ? -17.633 39.747  -12.887 1.00 111.92 ? 1059 ASN   B OD1 1 
ATOM   2337 N ND2 . ASN   B 1 22  ? -18.311 37.685  -13.425 1.00 112.78 ? 1059 ASN   B ND2 1 
ATOM   2338 N N   . PRO   B 1 23  ? -17.470 41.134  -10.134 1.00 104.85 ? 1060 PRO   B N   1 
ATOM   2339 C CA  . PRO   B 1 23  ? -18.528 41.961  -9.548  1.00 103.28 ? 1060 PRO   B CA  1 
ATOM   2340 C C   . PRO   B 1 23  ? -19.937 41.380  -9.684  1.00 103.11 ? 1060 PRO   B C   1 
ATOM   2341 O O   . PRO   B 1 23  ? -20.739 41.494  -8.759  1.00 101.14 ? 1060 PRO   B O   1 
ATOM   2342 C CB  . PRO   B 1 23  ? -18.434 43.308  -10.290 1.00 105.76 ? 1060 PRO   B CB  1 
ATOM   2343 C CG  . PRO   B 1 23  ? -17.430 43.093  -11.411 1.00 109.06 ? 1060 PRO   B CG  1 
ATOM   2344 C CD  . PRO   B 1 23  ? -16.567 41.925  -10.984 1.00 107.93 ? 1060 PRO   B CD  1 
ATOM   2345 N N   . GLU   B 1 24  ? -20.229 40.764  -10.838 1.00 105.68 ? 1061 GLU   B N   1 
ATOM   2346 C CA  . GLU   B 1 24  ? -21.520 40.133  -11.074 1.00 106.36 ? 1061 GLU   B CA  1 
ATOM   2347 C C   . GLU   B 1 24  ? -21.707 38.957  -10.117 1.00 103.56 ? 1061 GLU   B C   1 
ATOM   2348 O O   . GLU   B 1 24  ? -22.790 38.781  -9.562  1.00 102.82 ? 1061 GLU   B O   1 
ATOM   2349 C CB  . GLU   B 1 24  ? -21.654 39.668  -12.528 1.00 110.48 ? 1061 GLU   B CB  1 
ATOM   2350 C CG  . GLU   B 1 24  ? -22.099 40.764  -13.484 1.00 113.91 ? 1061 GLU   B CG  1 
ATOM   2351 C CD  . GLU   B 1 24  ? -21.094 41.878  -13.729 1.00 114.55 ? 1061 GLU   B CD  1 
ATOM   2352 O OE1 . GLU   B 1 24  ? -21.468 42.868  -14.388 1.00 117.25 ? 1061 GLU   B OE1 1 
ATOM   2353 O OE2 . GLU   B 1 24  ? -19.940 41.750  -13.274 1.00 112.72 ? 1061 GLU   B OE2 1 
ATOM   2354 N N   . LEU   B 1 25  ? -20.649 38.155  -9.941  1.00 102.31 ? 1062 LEU   B N   1 
ATOM   2355 C CA  . LEU   B 1 25  ? -20.667 37.047  -8.999  1.00 99.86  ? 1062 LEU   B CA  1 
ATOM   2356 C C   . LEU   B 1 25  ? -20.800 37.585  -7.577  1.00 96.81  ? 1062 LEU   B C   1 
ATOM   2357 O O   . LEU   B 1 25  ? -21.555 37.035  -6.779  1.00 95.73  ? 1062 LEU   B O   1 
ATOM   2358 C CB  . LEU   B 1 25  ? -19.387 36.218  -9.160  1.00 99.83  ? 1062 LEU   B CB  1 
ATOM   2359 C CG  . LEU   B 1 25  ? -19.231 35.040  -8.198  1.00 97.69  ? 1062 LEU   B CG  1 
ATOM   2360 C CD1 . LEU   B 1 25  ? -20.189 33.912  -8.551  1.00 98.79  ? 1062 LEU   B CD1 1 
ATOM   2361 C CD2 . LEU   B 1 25  ? -17.796 34.534  -8.189  1.00 97.72  ? 1062 LEU   B CD2 1 
ATOM   2362 N N   . VAL   B 1 26  ? -20.067 38.666  -7.278  1.00 95.93  ? 1063 VAL   B N   1 
ATOM   2363 C CA  . VAL   B 1 26  ? -20.049 39.256  -5.948  1.00 93.67  ? 1063 VAL   B CA  1 
ATOM   2364 C C   . VAL   B 1 26  ? -21.448 39.754  -5.587  1.00 93.53  ? 1063 VAL   B C   1 
ATOM   2365 O O   . VAL   B 1 26  ? -21.897 39.557  -4.460  1.00 92.12  ? 1063 VAL   B O   1 
ATOM   2366 C CB  . VAL   B 1 26  ? -19.004 40.386  -5.851  1.00 93.78  ? 1063 VAL   B CB  1 
ATOM   2367 C CG1 . VAL   B 1 26  ? -19.138 41.183  -4.560  1.00 92.10  ? 1063 VAL   B CG1 1 
ATOM   2368 C CG2 . VAL   B 1 26  ? -17.585 39.856  -6.008  1.00 94.39  ? 1063 VAL   B CG2 1 
ATOM   2369 N N   . GLN   B 1 27  ? -22.128 40.393  -6.549  1.00 95.50  ? 1064 GLN   B N   1 
ATOM   2370 C CA  . GLN   B 1 27  ? -23.446 40.968  -6.319  1.00 95.96  ? 1064 GLN   B CA  1 
ATOM   2371 C C   . GLN   B 1 27  ? -24.497 39.862  -6.213  1.00 96.37  ? 1064 GLN   B C   1 
ATOM   2372 O O   . GLN   B 1 27  ? -25.539 40.059  -5.589  1.00 96.80  ? 1064 GLN   B O   1 
ATOM   2373 C CB  . GLN   B 1 27  ? -23.798 41.955  -7.435  1.00 98.55  ? 1064 GLN   B CB  1 
ATOM   2374 C CG  . GLN   B 1 27  ? -25.038 42.789  -7.140  1.00 99.40  ? 1064 GLN   B CG  1 
ATOM   2375 C CD  . GLN   B 1 27  ? -25.227 43.915  -8.127  1.00 101.95 ? 1064 GLN   B CD  1 
ATOM   2376 O OE1 . GLN   B 1 27  ? -26.226 43.981  -8.839  1.00 105.05 ? 1064 GLN   B OE1 1 
ATOM   2377 N NE2 . GLN   B 1 27  ? -24.263 44.820  -8.171  1.00 101.21 ? 1064 GLN   B NE2 1 
ATOM   2378 N N   . ALA   B 1 28  ? -24.210 38.703  -6.820  1.00 96.42  ? 1065 ALA   B N   1 
ATOM   2379 C CA  . ALA   B 1 28  ? -25.101 37.552  -6.789  1.00 96.85  ? 1065 ALA   B CA  1 
ATOM   2380 C C   . ALA   B 1 28  ? -24.817 36.671  -5.573  1.00 93.76  ? 1065 ALA   B C   1 
ATOM   2381 O O   . ALA   B 1 28  ? -25.421 35.608  -5.426  1.00 94.42  ? 1065 ALA   B O   1 
ATOM   2382 C CB  . ALA   B 1 28  ? -24.941 36.770  -8.069  1.00 99.24  ? 1065 ALA   B CB  1 
ATOM   2383 N N   . VAL   B 1 29  ? -23.897 37.120  -4.708  1.00 90.52  ? 1066 VAL   B N   1 
ATOM   2384 C CA  . VAL   B 1 29  ? -23.415 36.331  -3.587  1.00 88.10  ? 1066 VAL   B CA  1 
ATOM   2385 C C   . VAL   B 1 29  ? -23.517 37.168  -2.308  1.00 86.33  ? 1066 VAL   B C   1 
ATOM   2386 O O   . VAL   B 1 29  ? -22.953 36.808  -1.279  1.00 85.10  ? 1066 VAL   B O   1 
ATOM   2387 C CB  . VAL   B 1 29  ? -21.984 35.836  -3.900  1.00 87.30  ? 1066 VAL   B CB  1 
ATOM   2388 C CG1 . VAL   B 1 29  ? -21.173 35.434  -2.677  1.00 85.66  ? 1066 VAL   B CG1 1 
ATOM   2389 C CG2 . VAL   B 1 29  ? -22.007 34.694  -4.909  1.00 88.65  ? 1066 VAL   B CG2 1 
ATOM   2390 N N   . GLN   B 1 30  ? -24.298 38.258  -2.362  1.00 86.50  ? 1067 GLN   B N   1 
ATOM   2391 C CA  . GLN   B 1 30  ? -24.391 39.205  -1.261  1.00 85.30  ? 1067 GLN   B CA  1 
ATOM   2392 C C   . GLN   B 1 30  ? -25.183 38.605  -0.101  1.00 85.07  ? 1067 GLN   B C   1 
ATOM   2393 O O   . GLN   B 1 30  ? -24.902 38.901  1.059   1.00 84.15  ? 1067 GLN   B O   1 
ATOM   2394 C CB  . GLN   B 1 30  ? -25.051 40.509  -1.719  1.00 86.51  ? 1067 GLN   B CB  1 
ATOM   2395 C CG  . GLN   B 1 30  ? -24.176 41.360  -2.630  1.00 86.56  ? 1067 GLN   B CG  1 
ATOM   2396 C CD  . GLN   B 1 30  ? -23.017 42.029  -1.926  1.00 85.10  ? 1067 GLN   B CD  1 
ATOM   2397 O OE1 . GLN   B 1 30  ? -22.182 42.677  -2.554  1.00 85.38  ? 1067 GLN   B OE1 1 
ATOM   2398 N NE2 . GLN   B 1 30  ? -22.952 41.882  -0.612  1.00 84.03  ? 1067 GLN   B NE2 1 
ATOM   2399 N N   . HIS   B 1 31  ? -26.179 37.772  -0.426  1.00 86.18  ? 1068 HIS   B N   1 
ATOM   2400 C CA  . HIS   B 1 31  ? -27.073 37.208  0.575   1.00 86.89  ? 1068 HIS   B CA  1 
ATOM   2401 C C   . HIS   B 1 31  ? -26.396 36.069  1.337   1.00 85.26  ? 1068 HIS   B C   1 
ATOM   2402 O O   . HIS   B 1 31  ? -26.775 35.785  2.472   1.00 85.80  ? 1068 HIS   B O   1 
ATOM   2403 C CB  . HIS   B 1 31  ? -28.393 36.752  -0.066  1.00 89.91  ? 1068 HIS   B CB  1 
ATOM   2404 C CG  . HIS   B 1 31  ? -28.269 35.723  -1.150  1.00 90.77  ? 1068 HIS   B CG  1 
ATOM   2405 N ND1 . HIS   B 1 31  ? -27.769 35.984  -2.403  1.00 90.73  ? 1068 HIS   B ND1 1 
ATOM   2406 C CD2 . HIS   B 1 31  ? -28.635 34.409  -1.136  1.00 92.21  ? 1068 HIS   B CD2 1 
ATOM   2407 C CE1 . HIS   B 1 31  ? -27.806 34.869  -3.130  1.00 91.99  ? 1068 HIS   B CE1 1 
ATOM   2408 N NE2 . HIS   B 1 31  ? -28.340 33.878  -2.362  1.00 92.87  ? 1068 HIS   B NE2 1 
ATOM   2409 N N   . VAL   B 1 32  ? -25.395 35.428  0.718   1.00 83.37  ? 1069 VAL   B N   1 
ATOM   2410 C CA  . VAL   B 1 32  ? -24.744 34.268  1.310   1.00 82.16  ? 1069 VAL   B CA  1 
ATOM   2411 C C   . VAL   B 1 32  ? -23.485 34.687  2.071   1.00 79.99  ? 1069 VAL   B C   1 
ATOM   2412 O O   . VAL   B 1 32  ? -23.040 33.954  2.951   1.00 79.88  ? 1069 VAL   B O   1 
ATOM   2413 C CB  . VAL   B 1 32  ? -24.431 33.185  0.256   1.00 82.36  ? 1069 VAL   B CB  1 
ATOM   2414 C CG1 . VAL   B 1 32  ? -25.694 32.684  -0.428  1.00 84.85  ? 1069 VAL   B CG1 1 
ATOM   2415 C CG2 . VAL   B 1 32  ? -23.419 33.649  -0.778  1.00 81.39  ? 1069 VAL   B CG2 1 
ATOM   2416 N N   . VAL   B 1 33  ? -22.900 35.846  1.732   1.00 78.55  ? 1070 VAL   B N   1 
ATOM   2417 C CA  . VAL   B 1 33  ? -21.702 36.313  2.418   1.00 77.25  ? 1070 VAL   B CA  1 
ATOM   2418 C C   . VAL   B 1 33  ? -22.083 36.834  3.801   1.00 77.47  ? 1070 VAL   B C   1 
ATOM   2419 O O   . VAL   B 1 33  ? -23.248 37.133  4.060   1.00 78.52  ? 1070 VAL   B O   1 
ATOM   2420 C CB  . VAL   B 1 33  ? -20.925 37.380  1.620   1.00 76.76  ? 1070 VAL   B CB  1 
ATOM   2421 C CG1 . VAL   B 1 33  ? -20.319 36.805  0.349   1.00 76.75  ? 1070 VAL   B CG1 1 
ATOM   2422 C CG2 . VAL   B 1 33  ? -21.765 38.612  1.313   1.00 77.13  ? 1070 VAL   B CG2 1 
ATOM   2423 N N   . ILE   B 1 34  ? -21.073 36.946  4.673   1.00 77.03  ? 1071 ILE   B N   1 
ATOM   2424 C CA  . ILE   B 1 34  ? -21.254 37.384  6.048   1.00 77.94  ? 1071 ILE   B CA  1 
ATOM   2425 C C   . ILE   B 1 34  ? -20.601 38.754  6.233   1.00 77.88  ? 1071 ILE   B C   1 
ATOM   2426 O O   . ILE   B 1 34  ? -21.273 39.712  6.608   1.00 78.43  ? 1071 ILE   B O   1 
ATOM   2427 C CB  . ILE   B 1 34  ? -20.708 36.320  7.027   1.00 78.79  ? 1071 ILE   B CB  1 
ATOM   2428 C CG1 . ILE   B 1 34  ? -21.805 35.351  7.475   1.00 79.80  ? 1071 ILE   B CG1 1 
ATOM   2429 C CG2 . ILE   B 1 34  ? -20.030 36.944  8.237   1.00 80.23  ? 1071 ILE   B CG2 1 
ATOM   2430 C CD1 . ILE   B 1 34  ? -22.506 34.641  6.348   1.00 79.17  ? 1071 ILE   B CD1 1 
ATOM   2431 N N   . GLY   B 1 35  ? -19.292 38.833  5.965   1.00 77.57  ? 1072 GLY   B N   1 
ATOM   2432 C CA  . GLY   B 1 35  ? -18.502 40.000  6.323   1.00 78.26  ? 1072 GLY   B CA  1 
ATOM   2433 C C   . GLY   B 1 35  ? -17.958 39.870  7.745   1.00 80.06  ? 1072 GLY   B C   1 
ATOM   2434 O O   . GLY   B 1 35  ? -18.730 39.877  8.701   1.00 80.92  ? 1072 GLY   B O   1 
ATOM   2435 N N   . PRO   B 1 36  ? -16.621 39.742  7.929   1.00 81.26  ? 1073 PRO   B N   1 
ATOM   2436 C CA  . PRO   B 1 36  ? -16.031 39.464  9.244   1.00 83.82  ? 1073 PRO   B CA  1 
ATOM   2437 C C   . PRO   B 1 36  ? -16.498 40.314  10.427  1.00 85.83  ? 1073 PRO   B C   1 
ATOM   2438 O O   . PRO   B 1 36  ? -16.398 39.874  11.571  1.00 88.10  ? 1073 PRO   B O   1 
ATOM   2439 C CB  . PRO   B 1 36  ? -14.538 39.734  9.004   1.00 85.32  ? 1073 PRO   B CB  1 
ATOM   2440 C CG  . PRO   B 1 36  ? -14.328 39.379  7.553   1.00 83.35  ? 1073 PRO   B CG  1 
ATOM   2441 C CD  . PRO   B 1 36  ? -15.603 39.825  6.869   1.00 81.03  ? 1073 PRO   B CD  1 
ATOM   2442 N N   . SER   B 1 37  ? -16.988 41.530  10.153  1.00 85.42  ? 1074 SER   B N   1 
ATOM   2443 C CA  . SER   B 1 37  ? -17.437 42.439  11.197  1.00 87.43  ? 1074 SER   B CA  1 
ATOM   2444 C C   . SER   B 1 37  ? -18.707 41.922  11.874  1.00 88.02  ? 1074 SER   B C   1 
ATOM   2445 O O   . SER   B 1 37  ? -18.909 42.160  13.063  1.00 90.62  ? 1074 SER   B O   1 
ATOM   2446 C CB  . SER   B 1 37  ? -17.644 43.828  10.646  1.00 86.62  ? 1074 SER   B CB  1 
ATOM   2447 O OG  . SER   B 1 37  ? -18.619 43.825  9.614   1.00 84.03  ? 1074 SER   B OG  1 
ATOM   2448 N N   . SER   B 1 38  ? -19.552 41.216  11.111  1.00 86.30  ? 1075 SER   B N   1 
ATOM   2449 C CA  . SER   B 1 38  ? -20.851 40.766  11.590  1.00 87.27  ? 1075 SER   B CA  1 
ATOM   2450 C C   . SER   B 1 38  ? -20.741 39.460  12.377  1.00 89.21  ? 1075 SER   B C   1 
ATOM   2451 O O   . SER   B 1 38  ? -21.671 39.105  13.099  1.00 90.91  ? 1075 SER   B O   1 
ATOM   2452 C CB  . SER   B 1 38  ? -21.819 40.616  10.444  1.00 85.09  ? 1075 SER   B CB  1 
ATOM   2453 O OG  . SER   B 1 38  ? -22.048 41.862  9.804   1.00 84.17  ? 1075 SER   B OG  1 
ATOM   2454 N N   . LEU   B 1 39  ? -19.615 38.749  12.231  1.00 71.38  ? 1076 LEU   B N   1 
ATOM   2455 C CA  . LEU   B 1 39  ? -19.468 37.404  12.766  1.00 70.15  ? 1076 LEU   B CA  1 
ATOM   2456 C C   . LEU   B 1 39  ? -18.299 37.361  13.749  1.00 70.01  ? 1076 LEU   B C   1 
ATOM   2457 O O   . LEU   B 1 39  ? -17.192 37.783  13.421  1.00 70.07  ? 1076 LEU   B O   1 
ATOM   2458 C CB  . LEU   B 1 39  ? -19.268 36.446  11.585  1.00 68.84  ? 1076 LEU   B CB  1 
ATOM   2459 C CG  . LEU   B 1 39  ? -19.151 34.953  11.900  1.00 67.51  ? 1076 LEU   B CG  1 
ATOM   2460 C CD1 . LEU   B 1 39  ? -17.819 34.615  12.555  1.00 66.64  ? 1076 LEU   B CD1 1 
ATOM   2461 C CD2 . LEU   B 1 39  ? -20.309 34.482  12.769  1.00 68.43  ? 1076 LEU   B CD2 1 
ATOM   2462 N N   . ILE   B 1 40  ? -18.566 36.831  14.950  1.00 70.49  ? 1077 ILE   B N   1 
ATOM   2463 C CA  . ILE   B 1 40  ? -17.568 36.705  16.001  1.00 71.08  ? 1077 ILE   B CA  1 
ATOM   2464 C C   . ILE   B 1 40  ? -17.301 35.221  16.241  1.00 69.95  ? 1077 ILE   B C   1 
ATOM   2465 O O   . ILE   B 1 40  ? -18.225 34.472  16.548  1.00 69.88  ? 1077 ILE   B O   1 
ATOM   2466 C CB  . ILE   B 1 40  ? -18.044 37.408  17.289  1.00 73.44  ? 1077 ILE   B CB  1 
ATOM   2467 C CG1 . ILE   B 1 40  ? -18.381 38.882  17.044  1.00 75.35  ? 1077 ILE   B CG1 1 
ATOM   2468 C CG2 . ILE   B 1 40  ? -17.022 37.237  18.405  1.00 74.27  ? 1077 ILE   B CG2 1 
ATOM   2469 C CD1 . ILE   B 1 40  ? -19.090 39.556  18.198  1.00 78.07  ? 1077 ILE   B CD1 1 
ATOM   2470 N N   . VAL   B 1 41  ? -16.032 34.815  16.100  1.00 69.69  ? 1078 VAL   B N   1 
ATOM   2471 C CA  . VAL   B 1 41  ? -15.617 33.439  16.328  1.00 68.91  ? 1078 VAL   B CA  1 
ATOM   2472 C C   . VAL   B 1 41  ? -14.994 33.341  17.718  1.00 70.81  ? 1078 VAL   B C   1 
ATOM   2473 O O   . VAL   B 1 41  ? -14.428 34.312  18.216  1.00 72.80  ? 1078 VAL   B O   1 
ATOM   2474 C CB  . VAL   B 1 41  ? -14.632 32.961  15.242  1.00 67.53  ? 1078 VAL   B CB  1 
ATOM   2475 C CG1 . VAL   B 1 41  ? -14.217 31.510  15.448  1.00 66.53  ? 1078 VAL   B CG1 1 
ATOM   2476 C CG2 . VAL   B 1 41  ? -15.192 33.159  13.842  1.00 66.64  ? 1078 VAL   B CG2 1 
ATOM   2477 N N   . HIS   B 1 42  ? -15.108 32.156  18.332  1.00 71.03  ? 1079 HIS   B N   1 
ATOM   2478 C CA  . HIS   B 1 42  ? -14.469 31.868  19.606  1.00 73.06  ? 1079 HIS   B CA  1 
ATOM   2479 C C   . HIS   B 1 42  ? -13.433 30.764  19.408  1.00 72.43  ? 1079 HIS   B C   1 
ATOM   2480 O O   . HIS   B 1 42  ? -13.758 29.581  19.480  1.00 71.90  ? 1079 HIS   B O   1 
ATOM   2481 C CB  . HIS   B 1 42  ? -15.517 31.476  20.656  1.00 74.61  ? 1079 HIS   B CB  1 
ATOM   2482 C CG  . HIS   B 1 42  ? -16.668 32.428  20.779  1.00 75.90  ? 1079 HIS   B CG  1 
ATOM   2483 N ND1 . HIS   B 1 42  ? -17.983 32.033  20.794  1.00 76.46  ? 1079 HIS   B ND1 1 
ATOM   2484 C CD2 . HIS   B 1 42  ? -16.660 33.786  20.902  1.00 77.19  ? 1079 HIS   B CD2 1 
ATOM   2485 C CE1 . HIS   B 1 42  ? -18.761 33.106  20.916  1.00 77.95  ? 1079 HIS   B CE1 1 
ATOM   2486 N NE2 . HIS   B 1 42  ? -17.960 34.207  20.984  1.00 78.31  ? 1079 HIS   B NE2 1 
ATOM   2487 N N   . PHE   B 1 43  ? -12.184 31.172  19.153  1.00 73.16  ? 1080 PHE   B N   1 
ATOM   2488 C CA  . PHE   B 1 43  ? -11.102 30.243  18.866  1.00 72.98  ? 1080 PHE   B CA  1 
ATOM   2489 C C   . PHE   B 1 43  ? -10.688 29.497  20.134  1.00 74.70  ? 1080 PHE   B C   1 
ATOM   2490 O O   . PHE   B 1 43  ? -10.155 28.391  20.052  1.00 74.50  ? 1080 PHE   B O   1 
ATOM   2491 C CB  . PHE   B 1 43  ? -9.919  30.988  18.241  1.00 74.17  ? 1080 PHE   B CB  1 
ATOM   2492 C CG  . PHE   B 1 43  ? -10.199 31.573  16.879  1.00 72.97  ? 1080 PHE   B CG  1 
ATOM   2493 C CD1 . PHE   B 1 43  ? -10.480 30.750  15.798  1.00 70.79  ? 1080 PHE   B CD1 1 
ATOM   2494 C CD2 . PHE   B 1 43  ? -10.187 32.945  16.676  1.00 74.43  ? 1080 PHE   B CD2 1 
ATOM   2495 C CE1 . PHE   B 1 43  ? -10.737 31.286  14.546  1.00 70.17  ? 1080 PHE   B CE1 1 
ATOM   2496 C CE2 . PHE   B 1 43  ? -10.445 33.480  15.423  1.00 73.63  ? 1080 PHE   B CE2 1 
ATOM   2497 C CZ  . PHE   B 1 43  ? -10.720 32.650  14.360  1.00 71.60  ? 1080 PHE   B CZ  1 
ATOM   2498 N N   . ASN   B 1 44  ? -10.929 30.111  21.299  1.00 76.79  ? 1081 ASN   B N   1 
ATOM   2499 C CA  . ASN   B 1 44  ? -10.685 29.468  22.581  1.00 78.88  ? 1081 ASN   B CA  1 
ATOM   2500 C C   . ASN   B 1 44  ? -11.676 28.323  22.778  1.00 77.74  ? 1081 ASN   B C   1 
ATOM   2501 O O   . ASN   B 1 44  ? -11.298 27.247  23.237  1.00 78.30  ? 1081 ASN   B O   1 
ATOM   2502 C CB  . ASN   B 1 44  ? -10.780 30.460  23.743  1.00 82.11  ? 1081 ASN   B CB  1 
ATOM   2503 C CG  . ASN   B 1 44  ? -9.782  31.593  23.639  1.00 84.14  ? 1081 ASN   B CG  1 
ATOM   2504 O OD1 . ASN   B 1 44  ? -9.813  32.367  22.684  1.00 83.22  ? 1081 ASN   B OD1 1 
ATOM   2505 N ND2 . ASN   B 1 44  ? -8.896  31.702  24.615  1.00 87.61  ? 1081 ASN   B ND2 1 
ATOM   2506 N N   . GLU   B 1 45  ? -12.943 28.573  22.423  1.00 76.51  ? 1082 GLU   B N   1 
ATOM   2507 C CA  . GLU   B 1 45  ? -14.022 27.626  22.651  1.00 76.42  ? 1082 GLU   B CA  1 
ATOM   2508 C C   . GLU   B 1 45  ? -14.146 26.684  21.454  1.00 73.70  ? 1082 GLU   B C   1 
ATOM   2509 O O   . GLU   B 1 45  ? -14.853 26.983  20.493  1.00 71.77  ? 1082 GLU   B O   1 
ATOM   2510 C CB  . GLU   B 1 45  ? -15.334 28.377  22.896  1.00 77.47  ? 1082 GLU   B CB  1 
ATOM   2511 C CG  . GLU   B 1 45  ? -15.268 29.379  24.034  1.00 80.44  ? 1082 GLU   B CG  1 
ATOM   2512 C CD  . GLU   B 1 45  ? -16.570 30.118  24.294  1.00 81.88  ? 1082 GLU   B CD  1 
ATOM   2513 O OE1 . GLU   B 1 45  ? -16.591 31.354  24.127  1.00 82.19  ? 1082 GLU   B OE1 1 
ATOM   2514 O OE2 . GLU   B 1 45  ? -17.561 29.456  24.665  1.00 83.08  ? 1082 GLU   B OE2 1 
ATOM   2515 N N   . VAL   B 1 46  ? -13.452 25.542  21.532  1.00 73.72  ? 1083 VAL   B N   1 
ATOM   2516 C CA  . VAL   B 1 46  ? -13.520 24.509  20.509  1.00 71.89  ? 1083 VAL   B CA  1 
ATOM   2517 C C   . VAL   B 1 46  ? -14.619 23.522  20.896  1.00 72.80  ? 1083 VAL   B C   1 
ATOM   2518 O O   . VAL   B 1 46  ? -14.599 22.979  21.999  1.00 74.95  ? 1083 VAL   B O   1 
ATOM   2519 C CB  . VAL   B 1 46  ? -12.162 23.800  20.340  1.00 71.85  ? 1083 VAL   B CB  1 
ATOM   2520 C CG1 . VAL   B 1 46  ? -12.213 22.724  19.265  1.00 70.27  ? 1083 VAL   B CG1 1 
ATOM   2521 C CG2 . VAL   B 1 46  ? -11.042 24.791  20.055  1.00 72.04  ? 1083 VAL   B CG2 1 
ATOM   2522 N N   . ILE   B 1 47  ? -15.568 23.293  19.977  1.00 71.69  ? 1084 ILE   B N   1 
ATOM   2523 C CA  . ILE   B 1 47  ? -16.724 22.451  20.250  1.00 73.21  ? 1084 ILE   B CA  1 
ATOM   2524 C C   . ILE   B 1 47  ? -16.437 21.012  19.819  1.00 72.71  ? 1084 ILE   B C   1 
ATOM   2525 O O   . ILE   B 1 47  ? -17.042 20.080  20.349  1.00 74.53  ? 1084 ILE   B O   1 
ATOM   2526 C CB  . ILE   B 1 47  ? -17.994 23.014  19.575  1.00 73.26  ? 1084 ILE   B CB  1 
ATOM   2527 C CG1 . ILE   B 1 47  ? -18.040 22.746  18.068  1.00 71.19  ? 1084 ILE   B CG1 1 
ATOM   2528 C CG2 . ILE   B 1 47  ? -18.146 24.495  19.884  1.00 73.58  ? 1084 ILE   B CG2 1 
ATOM   2529 C CD1 . ILE   B 1 47  ? -19.307 23.236  17.404  1.00 71.86  ? 1084 ILE   B CD1 1 
ATOM   2530 N N   . GLY   B 1 48  ? -15.530 20.837  18.850  1.00 70.57  ? 1085 GLY   B N   1 
ATOM   2531 C CA  . GLY   B 1 48  ? -15.170 19.508  18.383  1.00 70.35  ? 1085 GLY   B CA  1 
ATOM   2532 C C   . GLY   B 1 48  ? -14.013 19.534  17.388  1.00 68.43  ? 1085 GLY   B C   1 
ATOM   2533 O O   . GLY   B 1 48  ? -13.652 20.589  16.868  1.00 66.90  ? 1085 GLY   B O   1 
ATOM   2534 N N   . ARG   B 1 49  ? -13.443 18.349  17.144  1.00 68.93  ? 1086 ARG   B N   1 
ATOM   2535 C CA  . ARG   B 1 49  ? -12.374 18.163  16.176  1.00 68.07  ? 1086 ARG   B CA  1 
ATOM   2536 C C   . ARG   B 1 49  ? -12.511 16.767  15.572  1.00 68.10  ? 1086 ARG   B C   1 
ATOM   2537 O O   . ARG   B 1 49  ? -12.927 15.834  16.256  1.00 69.67  ? 1086 ARG   B O   1 
ATOM   2538 C CB  . ARG   B 1 49  ? -11.012 18.357  16.850  1.00 69.25  ? 1086 ARG   B CB  1 
ATOM   2539 C CG  . ARG   B 1 49  ? -9.821  18.275  15.905  1.00 69.40  ? 1086 ARG   B CG  1 
ATOM   2540 C CD  . ARG   B 1 49  ? -8.499  18.474  16.624  1.00 71.33  ? 1086 ARG   B CD  1 
ATOM   2541 N NE  . ARG   B 1 49  ? -8.403  19.784  17.258  1.00 72.09  ? 1086 ARG   B NE  1 
ATOM   2542 C CZ  . ARG   B 1 49  ? -8.316  19.995  18.569  1.00 73.83  ? 1086 ARG   B CZ  1 
ATOM   2543 N NH1 . ARG   B 1 49  ? -8.322  18.978  19.414  1.00 75.41  ? 1086 ARG   B NH1 1 
ATOM   2544 N NH2 . ARG   B 1 49  ? -8.226  21.230  19.033  1.00 74.29  ? 1086 ARG   B NH2 1 
ATOM   2545 N N   . GLY   B 1 50  ? -12.163 16.636  14.286  1.00 66.65  ? 1087 GLY   B N   1 
ATOM   2546 C CA  . GLY   B 1 50  ? -12.319 15.374  13.581  1.00 67.00  ? 1087 GLY   B CA  1 
ATOM   2547 C C   . GLY   B 1 50  ? -11.477 15.309  12.310  1.00 66.25  ? 1087 GLY   B C   1 
ATOM   2548 O O   . GLY   B 1 50  ? -10.427 15.941  12.221  1.00 65.95  ? 1087 GLY   B O   1 
ATOM   2549 N N   . HIS   B 1 51  ? -11.963 14.529  11.338  1.00 66.42  ? 1088 HIS   B N   1 
ATOM   2550 C CA  . HIS   B 1 51  ? -11.250 14.272  10.097  1.00 66.45  ? 1088 HIS   B CA  1 
ATOM   2551 C C   . HIS   B 1 51  ? -11.185 15.537  9.243   1.00 65.45  ? 1088 HIS   B C   1 
ATOM   2552 O O   . HIS   B 1 51  ? -10.169 15.800  8.603   1.00 65.80  ? 1088 HIS   B O   1 
ATOM   2553 C CB  . HIS   B 1 51  ? -11.928 13.124  9.336   1.00 67.64  ? 1088 HIS   B CB  1 
ATOM   2554 C CG  . HIS   B 1 51  ? -11.316 12.794  8.008   1.00 68.36  ? 1088 HIS   B CG  1 
ATOM   2555 N ND1 . HIS   B 1 51  ? -10.030 12.339  7.849   1.00 69.09  ? 1088 HIS   B ND1 1 
ATOM   2556 C CD2 . HIS   B 1 51  ? -11.869 12.864  6.763   1.00 68.98  ? 1088 HIS   B CD2 1 
ATOM   2557 C CE1 . HIS   B 1 51  ? -9.795  12.138  6.555   1.00 70.30  ? 1088 HIS   B CE1 1 
ATOM   2558 N NE2 . HIS   B 1 51  ? -10.924 12.458  5.862   1.00 70.22  ? 1088 HIS   B NE2 1 
ATOM   2559 N N   . PHE   B 1 52  ? -12.278 16.308  9.243   1.00 64.72  ? 1089 PHE   B N   1 
ATOM   2560 C CA  . PHE   B 1 52  ? -12.410 17.471  8.380   1.00 64.31  ? 1089 PHE   B CA  1 
ATOM   2561 C C   . PHE   B 1 52  ? -11.628 18.651  8.956   1.00 63.71  ? 1089 PHE   B C   1 
ATOM   2562 O O   . PHE   B 1 52  ? -10.887 19.312  8.231   1.00 64.04  ? 1089 PHE   B O   1 
ATOM   2563 C CB  . PHE   B 1 52  ? -13.890 17.800  8.177   1.00 64.23  ? 1089 PHE   B CB  1 
ATOM   2564 C CG  . PHE   B 1 52  ? -14.651 16.741  7.420   1.00 65.80  ? 1089 PHE   B CG  1 
ATOM   2565 C CD1 . PHE   B 1 52  ? -14.483 16.590  6.052   1.00 66.74  ? 1089 PHE   B CD1 1 
ATOM   2566 C CD2 . PHE   B 1 52  ? -15.511 15.874  8.078   1.00 66.97  ? 1089 PHE   B CD2 1 
ATOM   2567 C CE1 . PHE   B 1 52  ? -15.176 15.612  5.355   1.00 68.77  ? 1089 PHE   B CE1 1 
ATOM   2568 C CE2 . PHE   B 1 52  ? -16.202 14.895  7.380   1.00 69.06  ? 1089 PHE   B CE2 1 
ATOM   2569 C CZ  . PHE   B 1 52  ? -16.034 14.766  6.020   1.00 69.95  ? 1089 PHE   B CZ  1 
ATOM   2570 N N   . GLY   B 1 53  ? -11.805 18.909  10.258  1.00 63.51  ? 1090 GLY   B N   1 
ATOM   2571 C CA  . GLY   B 1 53  ? -11.072 19.966  10.937  1.00 63.39  ? 1090 GLY   B CA  1 
ATOM   2572 C C   . GLY   B 1 53  ? -11.672 20.297  12.301  1.00 63.37  ? 1090 GLY   B C   1 
ATOM   2573 O O   . GLY   B 1 53  ? -12.455 19.520  12.843  1.00 63.81  ? 1090 GLY   B O   1 
ATOM   2574 N N   . CYS   B 1 54  ? -11.282 21.458  12.841  1.00 63.58  ? 1091 CYS   B N   1 
ATOM   2575 C CA  . CYS   B 1 54  ? -11.797 21.943  14.111  1.00 64.12  ? 1091 CYS   B CA  1 
ATOM   2576 C C   . CYS   B 1 54  ? -13.042 22.793  13.874  1.00 63.67  ? 1091 CYS   B C   1 
ATOM   2577 O O   . CYS   B 1 54  ? -13.110 23.538  12.898  1.00 63.21  ? 1091 CYS   B O   1 
ATOM   2578 C CB  . CYS   B 1 54  ? -10.754 22.773  14.851  1.00 65.18  ? 1091 CYS   B CB  1 
ATOM   2579 S SG  . CYS   B 1 54  ? -9.266  21.838  15.289  1.00 67.37  ? 1091 CYS   B SG  1 
ATOM   2580 N N   . VAL   B 1 55  ? -14.018 22.667  14.783  1.00 64.31  ? 1092 VAL   B N   1 
ATOM   2581 C CA  . VAL   B 1 55  ? -15.221 23.482  14.760  1.00 64.41  ? 1092 VAL   B CA  1 
ATOM   2582 C C   . VAL   B 1 55  ? -15.215 24.362  16.007  1.00 65.37  ? 1092 VAL   B C   1 
ATOM   2583 O O   . VAL   B 1 55  ? -14.821 23.913  17.081  1.00 66.28  ? 1092 VAL   B O   1 
ATOM   2584 C CB  . VAL   B 1 55  ? -16.493 22.614  14.685  1.00 65.07  ? 1092 VAL   B CB  1 
ATOM   2585 C CG1 . VAL   B 1 55  ? -17.742 23.462  14.496  1.00 65.71  ? 1092 VAL   B CG1 1 
ATOM   2586 C CG2 . VAL   B 1 55  ? -16.396 21.561  13.591  1.00 64.65  ? 1092 VAL   B CG2 1 
ATOM   2587 N N   . TYR   B 1 56  ? -15.660 25.614  15.847  1.00 65.76  ? 1093 TYR   B N   1 
ATOM   2588 C CA  . TYR   B 1 56  ? -15.598 26.605  16.909  1.00 67.56  ? 1093 TYR   B CA  1 
ATOM   2589 C C   . TYR   B 1 56  ? -16.998 27.132  17.211  1.00 68.91  ? 1093 TYR   B C   1 
ATOM   2590 O O   . TYR   B 1 56  ? -17.886 27.059  16.365  1.00 68.54  ? 1093 TYR   B O   1 
ATOM   2591 C CB  . TYR   B 1 56  ? -14.683 27.764  16.503  1.00 67.67  ? 1093 TYR   B CB  1 
ATOM   2592 C CG  . TYR   B 1 56  ? -13.294 27.361  16.076  1.00 67.48  ? 1093 TYR   B CG  1 
ATOM   2593 C CD1 . TYR   B 1 56  ? -12.877 27.515  14.763  1.00 66.72  ? 1093 TYR   B CD1 1 
ATOM   2594 C CD2 . TYR   B 1 56  ? -12.387 26.838  16.985  1.00 68.60  ? 1093 TYR   B CD2 1 
ATOM   2595 C CE1 . TYR   B 1 56  ? -11.602 27.151  14.361  1.00 67.03  ? 1093 TYR   B CE1 1 
ATOM   2596 C CE2 . TYR   B 1 56  ? -11.107 26.470  16.600  1.00 68.85  ? 1093 TYR   B CE2 1 
ATOM   2597 C CZ  . TYR   B 1 56  ? -10.713 26.627  15.282  1.00 68.15  ? 1093 TYR   B CZ  1 
ATOM   2598 O OH  . TYR   B 1 56  ? -9.448  26.266  14.888  1.00 69.14  ? 1093 TYR   B OH  1 
ATOM   2599 N N   . HIS   B 1 57  ? -17.176 27.665  18.427  1.00 71.01  ? 1094 HIS   B N   1 
ATOM   2600 C CA  . HIS   B 1 57  ? -18.356 28.446  18.762  1.00 73.05  ? 1094 HIS   B CA  1 
ATOM   2601 C C   . HIS   B 1 57  ? -18.304 29.777  18.017  1.00 72.69  ? 1094 HIS   B C   1 
ATOM   2602 O O   . HIS   B 1 57  ? -17.222 30.280  17.718  1.00 71.52  ? 1094 HIS   B O   1 
ATOM   2603 C CB  . HIS   B 1 57  ? -18.463 28.665  20.278  1.00 75.61  ? 1094 HIS   B CB  1 
ATOM   2604 C CG  . HIS   B 1 57  ? -19.093 27.538  21.042  1.00 77.52  ? 1094 HIS   B CG  1 
ATOM   2605 N ND1 . HIS   B 1 57  ? -20.323 27.008  20.741  1.00 78.63  ? 1094 HIS   B ND1 1 
ATOM   2606 C CD2 . HIS   B 1 57  ? -18.627 26.858  22.128  1.00 79.04  ? 1094 HIS   B CD2 1 
ATOM   2607 C CE1 . HIS   B 1 57  ? -20.604 26.035  21.605  1.00 80.80  ? 1094 HIS   B CE1 1 
ATOM   2608 N NE2 . HIS   B 1 57  ? -19.562 25.923  22.474  1.00 80.96  ? 1094 HIS   B NE2 1 
ATOM   2609 N N   . GLY   B 1 58  ? -19.485 30.338  17.729  1.00 74.25  ? 1095 GLY   B N   1 
ATOM   2610 C CA  . GLY   B 1 58  ? -19.592 31.582  16.985  1.00 74.32  ? 1095 GLY   B CA  1 
ATOM   2611 C C   . GLY   B 1 58  ? -20.744 32.451  17.482  1.00 77.09  ? 1095 GLY   B C   1 
ATOM   2612 O O   . GLY   B 1 58  ? -21.587 31.993  18.252  1.00 79.10  ? 1095 GLY   B O   1 
ATOM   2613 N N   . THR   B 1 59  ? -20.757 33.711  17.030  1.00 77.69  ? 1096 THR   B N   1 
ATOM   2614 C CA  . THR   B 1 59  ? -21.807 34.658  17.370  1.00 80.51  ? 1096 THR   B CA  1 
ATOM   2615 C C   . THR   B 1 59  ? -22.068 35.572  16.175  1.00 80.84  ? 1096 THR   B C   1 
ATOM   2616 O O   . THR   B 1 59  ? -21.320 36.518  15.939  1.00 80.17  ? 1096 THR   B O   1 
ATOM   2617 C CB  . THR   B 1 59  ? -21.445 35.461  18.626  1.00 82.17  ? 1096 THR   B CB  1 
ATOM   2618 O OG1 . THR   B 1 59  ? -21.367 34.554  19.726  1.00 82.98  ? 1096 THR   B OG1 1 
ATOM   2619 C CG2 . THR   B 1 59  ? -22.445 36.552  18.943  1.00 84.96  ? 1096 THR   B CG2 1 
ATOM   2620 N N   . LEU   B 1 60  ? -23.133 35.260  15.428  1.00 82.83  ? 1097 LEU   B N   1 
ATOM   2621 C CA  . LEU   B 1 60  ? -23.597 36.091  14.328  1.00 84.62  ? 1097 LEU   B CA  1 
ATOM   2622 C C   . LEU   B 1 60  ? -24.756 36.954  14.822  1.00 88.92  ? 1097 LEU   B C   1 
ATOM   2623 O O   . LEU   B 1 60  ? -25.461 36.571  15.753  1.00 91.18  ? 1097 LEU   B O   1 
ATOM   2624 C CB  . LEU   B 1 60  ? -24.034 35.179  13.175  1.00 84.23  ? 1097 LEU   B CB  1 
ATOM   2625 C CG  . LEU   B 1 60  ? -24.414 35.878  11.869  1.00 85.00  ? 1097 LEU   B CG  1 
ATOM   2626 C CD1 . LEU   B 1 60  ? -23.180 36.384  11.136  1.00 83.10  ? 1097 LEU   B CD1 1 
ATOM   2627 C CD2 . LEU   B 1 60  ? -25.219 34.949  10.972  1.00 85.81  ? 1097 LEU   B CD2 1 
ATOM   2628 N N   . LEU   B 1 61  ? -24.933 38.123  14.193  1.00 90.95  ? 1098 LEU   B N   1 
ATOM   2629 C CA  . LEU   B 1 61  ? -26.061 38.998  14.473  1.00 95.13  ? 1098 LEU   B CA  1 
ATOM   2630 C C   . LEU   B 1 61  ? -26.656 39.475  13.149  1.00 96.91  ? 1098 LEU   B C   1 
ATOM   2631 O O   . LEU   B 1 61  ? -26.021 40.232  12.417  1.00 96.21  ? 1098 LEU   B O   1 
ATOM   2632 C CB  . LEU   B 1 61  ? -25.617 40.174  15.352  1.00 96.10  ? 1098 LEU   B CB  1 
ATOM   2633 C CG  . LEU   B 1 61  ? -24.216 40.735  15.097  1.00 93.84  ? 1098 LEU   B CG  1 
ATOM   2634 C CD1 . LEU   B 1 61  ? -24.128 42.180  15.562  1.00 96.12  ? 1098 LEU   B CD1 1 
ATOM   2635 C CD2 . LEU   B 1 61  ? -23.148 39.904  15.798  1.00 91.60  ? 1098 LEU   B CD2 1 
ATOM   2636 N N   . ASP   B 1 62  ? -27.882 39.016  12.862  1.00 100.17 ? 1099 ASP   B N   1 
ATOM   2637 C CA  . ASP   B 1 62  ? -28.518 39.221  11.571  1.00 102.25 ? 1099 ASP   B CA  1 
ATOM   2638 C C   . ASP   B 1 62  ? -29.412 40.457  11.640  1.00 106.16 ? 1099 ASP   B C   1 
ATOM   2639 O O   . ASP   B 1 62  ? -30.188 40.612  12.581  1.00 109.02 ? 1099 ASP   B O   1 
ATOM   2640 C CB  . ASP   B 1 62  ? -29.309 37.975  11.159  1.00 103.84 ? 1099 ASP   B CB  1 
ATOM   2641 C CG  . ASP   B 1 62  ? -29.815 37.987  9.725   1.00 105.62 ? 1099 ASP   B CG  1 
ATOM   2642 O OD1 . ASP   B 1 62  ? -29.540 38.971  9.007   1.00 105.91 ? 1099 ASP   B OD1 1 
ATOM   2643 O OD2 . ASP   B 1 62  ? -30.479 37.006  9.335   1.00 107.31 ? 1099 ASP   B OD2 1 
ATOM   2644 N N   . ASN   B 1 63  ? -29.288 41.325  10.625  1.00 106.62 ? 1100 ASN   B N   1 
ATOM   2645 C CA  . ASN   B 1 63  ? -30.076 42.543  10.510  1.00 110.20 ? 1100 ASN   B CA  1 
ATOM   2646 C C   . ASN   B 1 63  ? -29.907 43.392  11.769  1.00 110.96 ? 1100 ASN   B C   1 
ATOM   2647 O O   . ASN   B 1 63  ? -30.873 43.974  12.260  1.00 114.57 ? 1100 ASN   B O   1 
ATOM   2648 C CB  . ASN   B 1 63  ? -31.552 42.238  10.234  1.00 114.45 ? 1100 ASN   B CB  1 
ATOM   2649 C CG  . ASN   B 1 63  ? -31.757 41.373  9.008   1.00 114.36 ? 1100 ASN   B CG  1 
ATOM   2650 O OD1 . ASN   B 1 63  ? -32.325 40.287  9.096   1.00 115.31 ? 1100 ASN   B OD1 1 
ATOM   2651 N ND2 . ASN   B 1 63  ? -31.297 41.846  7.861   1.00 113.65 ? 1100 ASN   B ND2 1 
ATOM   2652 N N   . ASP   B 1 64  ? -28.666 43.457  12.271  1.00 107.80 ? 1101 ASP   B N   1 
ATOM   2653 C CA  . ASP   B 1 64  ? -28.349 44.151  13.510  1.00 108.36 ? 1101 ASP   B CA  1 
ATOM   2654 C C   . ASP   B 1 64  ? -29.294 43.661  14.609  1.00 110.72 ? 1101 ASP   B C   1 
ATOM   2655 O O   . ASP   B 1 64  ? -29.855 44.460  15.357  1.00 114.26 ? 1101 ASP   B O   1 
ATOM   2656 C CB  . ASP   B 1 64  ? -28.403 45.669  13.310  1.00 110.49 ? 1101 ASP   B CB  1 
ATOM   2657 C CG  . ASP   B 1 64  ? -27.772 46.466  14.439  1.00 110.87 ? 1101 ASP   B CG  1 
ATOM   2658 O OD1 . ASP   B 1 64  ? -28.483 47.296  15.040  1.00 114.21 ? 1101 ASP   B OD1 1 
ATOM   2659 O OD2 . ASP   B 1 64  ? -26.573 46.251  14.707  1.00 107.96 ? 1101 ASP   B OD2 1 
ATOM   2660 N N   . GLY   B 1 65  ? -29.453 42.334  14.692  1.00 109.01 ? 1102 GLY   B N   1 
ATOM   2661 C CA  . GLY   B 1 65  ? -30.405 41.713  15.599  1.00 111.55 ? 1102 GLY   B CA  1 
ATOM   2662 C C   . GLY   B 1 65  ? -29.712 41.058  16.790  1.00 109.73 ? 1102 GLY   B C   1 
ATOM   2663 O O   . GLY   B 1 65  ? -28.591 41.424  17.140  1.00 107.50 ? 1102 GLY   B O   1 
ATOM   2664 N N   . LYS   B 1 66  ? -30.398 40.082  17.397  1.00 111.16 ? 1103 LYS   B N   1 
ATOM   2665 C CA  . LYS   B 1 66  ? -29.903 39.388  18.575  1.00 110.07 ? 1103 LYS   B CA  1 
ATOM   2666 C C   . LYS   B 1 66  ? -28.780 38.440  18.157  1.00 104.61 ? 1103 LYS   B C   1 
ATOM   2667 O O   . LYS   B 1 66  ? -28.686 38.065  16.989  1.00 102.11 ? 1103 LYS   B O   1 
ATOM   2668 C CB  . LYS   B 1 66  ? -31.052 38.634  19.255  1.00 114.35 ? 1103 LYS   B CB  1 
ATOM   2669 C CG  . LYS   B 1 66  ? -30.813 38.220  20.702  1.00 115.77 ? 1103 LYS   B CG  1 
ATOM   2670 C CD  . LYS   B 1 66  ? -30.717 39.390  21.662  1.00 118.21 ? 1103 LYS   B CD  1 
ATOM   2671 C CE  . LYS   B 1 66  ? -30.629 38.966  23.114  1.00 120.82 ? 1103 LYS   B CE  1 
ATOM   2672 N NZ  . LYS   B 1 66  ? -29.394 38.195  23.391  1.00 116.92 ? 1103 LYS   B NZ  1 
ATOM   2673 N N   . LYS   B 1 67  ? -27.926 38.074  19.121  1.00 102.68 ? 1104 LYS   B N   1 
ATOM   2674 C CA  . LYS   B 1 67  ? -26.837 37.142  18.873  1.00 98.28  ? 1104 LYS   B CA  1 
ATOM   2675 C C   . LYS   B 1 67  ? -27.412 35.777  18.499  1.00 97.73  ? 1104 LYS   B C   1 
ATOM   2676 O O   . LYS   B 1 67  ? -28.295 35.262  19.181  1.00 101.01 ? 1104 LYS   B O   1 
ATOM   2677 C CB  . LYS   B 1 67  ? -25.901 37.042  20.084  1.00 98.10  ? 1104 LYS   B CB  1 
ATOM   2678 C CG  . LYS   B 1 67  ? -26.552 36.682  21.415  1.00 102.03 ? 1104 LYS   B CG  1 
ATOM   2679 C CD  . LYS   B 1 67  ? -25.562 36.267  22.489  1.00 101.57 ? 1104 LYS   B CD  1 
ATOM   2680 C CE  . LYS   B 1 67  ? -24.543 37.336  22.830  1.00 100.96 ? 1104 LYS   B CE  1 
ATOM   2681 N NZ  . LYS   B 1 67  ? -25.185 38.580  23.317  1.00 104.55 ? 1104 LYS   B NZ  1 
ATOM   2682 N N   . ILE   B 1 68  ? -26.906 35.215  17.394  1.00 93.79  ? 1105 ILE   B N   1 
ATOM   2683 C CA  . ILE   B 1 68  ? -27.310 33.902  16.918  1.00 93.14  ? 1105 ILE   B CA  1 
ATOM   2684 C C   . ILE   B 1 68  ? -26.170 32.926  17.196  1.00 89.63  ? 1105 ILE   B C   1 
ATOM   2685 O O   . ILE   B 1 68  ? -25.104 33.034  16.594  1.00 86.26  ? 1105 ILE   B O   1 
ATOM   2686 C CB  . ILE   B 1 68  ? -27.674 33.944  15.419  1.00 92.45  ? 1105 ILE   B CB  1 
ATOM   2687 C CG1 . ILE   B 1 68  ? -28.754 34.989  15.121  1.00 95.61  ? 1105 ILE   B CG1 1 
ATOM   2688 C CG2 . ILE   B 1 68  ? -28.074 32.559  14.925  1.00 92.87  ? 1105 ILE   B CG2 1 
ATOM   2689 C CD1 . ILE   B 1 68  ? -29.038 35.186  13.648  1.00 95.32  ? 1105 ILE   B CD1 1 
ATOM   2690 N N   . HIS   B 1 69  ? -26.407 31.983  18.116  1.00 90.72  ? 1106 HIS   B N   1 
ATOM   2691 C CA  . HIS   B 1 69  ? -25.416 30.979  18.463  1.00 88.10  ? 1106 HIS   B CA  1 
ATOM   2692 C C   . HIS   B 1 69  ? -25.236 30.027  17.283  1.00 85.46  ? 1106 HIS   B C   1 
ATOM   2693 O O   . HIS   B 1 69  ? -26.190 29.376  16.861  1.00 87.36  ? 1106 HIS   B O   1 
ATOM   2694 C CB  . HIS   B 1 69  ? -25.838 30.230  19.735  1.00 91.30  ? 1106 HIS   B CB  1 
ATOM   2695 C CG  . HIS   B 1 69  ? -24.751 29.430  20.390  1.00 89.82  ? 1106 HIS   B CG  1 
ATOM   2696 N ND1 . HIS   B 1 69  ? -24.956 28.623  21.483  1.00 92.55  ? 1106 HIS   B ND1 1 
ATOM   2697 C CD2 . HIS   B 1 69  ? -23.428 29.337  20.073  1.00 86.20  ? 1106 HIS   B CD2 1 
ATOM   2698 C CE1 . HIS   B 1 69  ? -23.804 28.053  21.829  1.00 90.47  ? 1106 HIS   B CE1 1 
ATOM   2699 N NE2 . HIS   B 1 69  ? -22.841 28.483  20.967  1.00 86.63  ? 1106 HIS   B NE2 1 
ATOM   2700 N N   . CYS   B 1 70  ? -24.008 29.971  16.751  1.00 81.32  ? 1107 CYS   B N   1 
ATOM   2701 C CA  . CYS   B 1 70  ? -23.713 29.213  15.546  1.00 78.88  ? 1107 CYS   B CA  1 
ATOM   2702 C C   . CYS   B 1 70  ? -22.389 28.468  15.702  1.00 75.92  ? 1107 CYS   B C   1 
ATOM   2703 O O   . CYS   B 1 70  ? -21.660 28.682  16.669  1.00 75.16  ? 1107 CYS   B O   1 
ATOM   2704 C CB  . CYS   B 1 70  ? -23.664 30.133  14.331  1.00 77.79  ? 1107 CYS   B CB  1 
ATOM   2705 S SG  . CYS   B 1 70  ? -22.501 31.510  14.513  1.00 75.86  ? 1107 CYS   B SG  1 
ATOM   2706 N N   . ALA   B 1 71  ? -22.108 27.581  14.739  1.00 74.44  ? 1108 ALA   B N   1 
ATOM   2707 C CA  . ALA   B 1 71  ? -20.858 26.839  14.685  1.00 72.15  ? 1108 ALA   B CA  1 
ATOM   2708 C C   . ALA   B 1 71  ? -20.090 27.238  13.427  1.00 69.92  ? 1108 ALA   B C   1 
ATOM   2709 O O   . ALA   B 1 71  ? -20.668 27.305  12.345  1.00 69.80  ? 1108 ALA   B O   1 
ATOM   2710 C CB  . ALA   B 1 71  ? -21.141 25.357  14.712  1.00 73.01  ? 1108 ALA   B CB  1 
ATOM   2711 N N   . VAL   B 1 72  ? -18.784 27.490  13.587  1.00 68.52  ? 1109 VAL   B N   1 
ATOM   2712 C CA  . VAL   B 1 72  ? -17.949 27.997  12.509  1.00 67.62  ? 1109 VAL   B CA  1 
ATOM   2713 C C   . VAL   B 1 72  ? -16.815 27.006  12.249  1.00 66.72  ? 1109 VAL   B C   1 
ATOM   2714 O O   . VAL   B 1 72  ? -16.295 26.393  13.180  1.00 66.33  ? 1109 VAL   B O   1 
ATOM   2715 C CB  . VAL   B 1 72  ? -17.406 29.402  12.836  1.00 67.72  ? 1109 VAL   B CB  1 
ATOM   2716 C CG1 . VAL   B 1 72  ? -16.559 29.960  11.700  1.00 67.25  ? 1109 VAL   B CG1 1 
ATOM   2717 C CG2 . VAL   B 1 72  ? -18.525 30.370  13.193  1.00 68.98  ? 1109 VAL   B CG2 1 
ATOM   2718 N N   . LYS   B 1 73  ? -16.440 26.875  10.970  1.00 66.70  ? 1110 LYS   B N   1 
ATOM   2719 C CA  . LYS   B 1 73  ? -15.399 25.953  10.542  1.00 66.63  ? 1110 LYS   B CA  1 
ATOM   2720 C C   . LYS   B 1 73  ? -14.711 26.514  9.299   1.00 67.05  ? 1110 LYS   B C   1 
ATOM   2721 O O   . LYS   B 1 73  ? -15.347 27.179  8.484   1.00 67.45  ? 1110 LYS   B O   1 
ATOM   2722 C CB  . LYS   B 1 73  ? -16.005 24.573  10.268  1.00 67.10  ? 1110 LYS   B CB  1 
ATOM   2723 C CG  . LYS   B 1 73  ? -15.042 23.531  9.713   1.00 67.19  ? 1110 LYS   B CG  1 
ATOM   2724 C CD  . LYS   B 1 73  ? -15.675 22.170  9.516   1.00 68.08  ? 1110 LYS   B CD  1 
ATOM   2725 C CE  . LYS   B 1 73  ? -14.753 21.176  8.841   1.00 68.39  ? 1110 LYS   B CE  1 
ATOM   2726 N NZ  . LYS   B 1 73  ? -14.379 21.609  7.472   1.00 68.84  ? 1110 LYS   B NZ  1 
ATOM   2727 N N   . SER   B 1 74  ? -13.411 26.223  9.166   1.00 67.37  ? 1111 SER   B N   1 
ATOM   2728 C CA  . SER   B 1 74  ? -12.605 26.709  8.057   1.00 68.36  ? 1111 SER   B CA  1 
ATOM   2729 C C   . SER   B 1 74  ? -12.405 25.600  7.026   1.00 69.08  ? 1111 SER   B C   1 
ATOM   2730 O O   . SER   B 1 74  ? -12.456 24.419  7.363   1.00 68.28  ? 1111 SER   B O   1 
ATOM   2731 C CB  . SER   B 1 74  ? -11.282 27.233  8.550   1.00 69.11  ? 1111 SER   B CB  1 
ATOM   2732 O OG  . SER   B 1 74  ? -10.549 26.213  9.212   1.00 69.11  ? 1111 SER   B OG  1 
ATOM   2733 N N   . LEU   B 1 75  ? -12.168 26.007  5.772   1.00 70.96  ? 1112 LEU   B N   1 
ATOM   2734 C CA  . LEU   B 1 75  ? -11.916 25.089  4.672   1.00 72.54  ? 1112 LEU   B CA  1 
ATOM   2735 C C   . LEU   B 1 75  ? -10.514 25.344  4.123   1.00 74.77  ? 1112 LEU   B C   1 
ATOM   2736 O O   . LEU   B 1 75  ? -10.334 26.164  3.224   1.00 76.48  ? 1112 LEU   B O   1 
ATOM   2737 C CB  . LEU   B 1 75  ? -12.981 25.304  3.591   1.00 73.44  ? 1112 LEU   B CB  1 
ATOM   2738 C CG  . LEU   B 1 75  ? -14.428 25.071  4.027   1.00 72.72  ? 1112 LEU   B CG  1 
ATOM   2739 C CD1 . LEU   B 1 75  ? -15.377 25.217  2.848   1.00 74.41  ? 1112 LEU   B CD1 1 
ATOM   2740 C CD2 . LEU   B 1 75  ? -14.594 23.705  4.675   1.00 72.06  ? 1112 LEU   B CD2 1 
ATOM   2741 N N   . ASN   B 1 76  ? -9.529  24.617  4.663   1.00 75.41  ? 1113 ASN   B N   1 
ATOM   2742 C CA  . ASN   B 1 76  ? -8.124  24.873  4.385   1.00 77.97  ? 1113 ASN   B CA  1 
ATOM   2743 C C   . ASN   B 1 76  ? -7.751  24.403  2.979   1.00 80.74  ? 1113 ASN   B C   1 
ATOM   2744 O O   . ASN   B 1 76  ? -6.744  24.852  2.434   1.00 83.44  ? 1113 ASN   B O   1 
ATOM   2745 C CB  . ASN   B 1 76  ? -7.220  24.222  5.434   1.00 77.94  ? 1113 ASN   B CB  1 
ATOM   2746 C CG  . ASN   B 1 76  ? -7.425  24.796  6.820   1.00 76.54  ? 1113 ASN   B CG  1 
ATOM   2747 O OD1 . ASN   B 1 76  ? -7.828  24.085  7.738   1.00 75.18  ? 1113 ASN   B OD1 1 
ATOM   2748 N ND2 . ASN   B 1 76  ? -7.155  26.081  6.980   1.00 77.41  ? 1113 ASN   B ND2 1 
ATOM   2749 N N   . ARG   B 1 77  ? -8.554  23.499  2.401   1.00 80.96  ? 1114 ARG   B N   1 
ATOM   2750 C CA  . ARG   B 1 77  ? -8.330  23.022  1.044   1.00 84.03  ? 1114 ARG   B CA  1 
ATOM   2751 C C   . ARG   B 1 77  ? -8.405  24.180  0.049   1.00 85.95  ? 1114 ARG   B C   1 
ATOM   2752 O O   . ARG   B 1 77  ? -7.684  24.180  -0.946  1.00 89.09  ? 1114 ARG   B O   1 
ATOM   2753 C CB  . ARG   B 1 77  ? -9.344  21.936  0.668   1.00 84.17  ? 1114 ARG   B CB  1 
ATOM   2754 C CG  . ARG   B 1 77  ? -8.989  20.537  1.155   1.00 84.42  ? 1114 ARG   B CG  1 
ATOM   2755 C CD  . ARG   B 1 77  ? -7.657  20.049  0.611   1.00 87.54  ? 1114 ARG   B CD  1 
ATOM   2756 N NE  . ARG   B 1 77  ? -7.546  18.596  0.585   1.00 88.47  ? 1114 ARG   B NE  1 
ATOM   2757 C CZ  . ARG   B 1 77  ? -8.155  17.805  -0.294  1.00 89.93  ? 1114 ARG   B CZ  1 
ATOM   2758 N NH1 . ARG   B 1 77  ? -8.881  18.327  -1.267  1.00 90.95  ? 1114 ARG   B NH1 1 
ATOM   2759 N NH2 . ARG   B 1 77  ? -8.028  16.492  -0.202  1.00 90.54  ? 1114 ARG   B NH2 1 
ATOM   2760 N N   . ILE   B 1 78  ? -9.284  25.154  0.322   1.00 84.40  ? 1115 ILE   B N   1 
ATOM   2761 C CA  . ILE   B 1 78  ? -9.451  26.312  -0.542  1.00 86.21  ? 1115 ILE   B CA  1 
ATOM   2762 C C   . ILE   B 1 78  ? -8.230  27.219  -0.387  1.00 88.01  ? 1115 ILE   B C   1 
ATOM   2763 O O   . ILE   B 1 78  ? -8.049  27.842  0.658   1.00 86.48  ? 1115 ILE   B O   1 
ATOM   2764 C CB  . ILE   B 1 78  ? -10.766 27.056  -0.226  1.00 84.37  ? 1115 ILE   B CB  1 
ATOM   2765 C CG1 . ILE   B 1 78  ? -11.988 26.145  -0.385  1.00 83.28  ? 1115 ILE   B CG1 1 
ATOM   2766 C CG2 . ILE   B 1 78  ? -10.888 28.315  -1.074  1.00 86.75  ? 1115 ILE   B CG2 1 
ATOM   2767 C CD1 . ILE   B 1 78  ? -13.285 26.759  0.093   1.00 81.87  ? 1115 ILE   B CD1 1 
ATOM   2768 N N   . THR   B 1 79  ? -7.406  27.283  -1.441  1.00 91.65  ? 1116 THR   B N   1 
ATOM   2769 C CA  . THR   B 1 79  ? -6.167  28.044  -1.426  1.00 94.56  ? 1116 THR   B CA  1 
ATOM   2770 C C   . THR   B 1 79  ? -6.259  29.199  -2.422  1.00 97.74  ? 1116 THR   B C   1 
ATOM   2771 O O   . THR   B 1 79  ? -6.229  30.362  -2.026  1.00 98.27  ? 1116 THR   B O   1 
ATOM   2772 C CB  . THR   B 1 79  ? -4.963  27.140  -1.727  1.00 97.25  ? 1116 THR   B CB  1 
ATOM   2773 O OG1 . THR   B 1 79  ? -4.929  26.110  -0.739  1.00 94.38  ? 1116 THR   B OG1 1 
ATOM   2774 C CG2 . THR   B 1 79  ? -3.646  27.886  -1.731  1.00 101.27 ? 1116 THR   B CG2 1 
ATOM   2775 N N   . ASP   B 1 80  ? -6.378  28.860  -3.712  1.00 100.27 ? 1117 ASP   B N   1 
ATOM   2776 C CA  . ASP   B 1 80  ? -6.327  29.846  -4.781  1.00 104.05 ? 1117 ASP   B CA  1 
ATOM   2777 C C   . ASP   B 1 80  ? -7.686  30.532  -4.909  1.00 101.99 ? 1117 ASP   B C   1 
ATOM   2778 O O   . ASP   B 1 80  ? -8.654  30.140  -4.259  1.00 97.70  ? 1117 ASP   B O   1 
ATOM   2779 C CB  . ASP   B 1 80  ? -5.857  29.212  -6.096  1.00 108.52 ? 1117 ASP   B CB  1 
ATOM   2780 C CG  . ASP   B 1 80  ? -6.784  28.146  -6.657  1.00 107.45 ? 1117 ASP   B CG  1 
ATOM   2781 O OD1 . ASP   B 1 80  ? -6.412  26.957  -6.593  1.00 107.22 ? 1117 ASP   B OD1 1 
ATOM   2782 O OD2 . ASP   B 1 80  ? -7.856  28.513  -7.179  1.00 107.40 ? 1117 ASP   B OD2 1 
ATOM   2783 N N   . ILE   B 1 81  ? -7.734  31.565  -5.760  1.00 95.24  ? 1118 ILE   B N   1 
ATOM   2784 C CA  . ILE   B 1 81  ? -8.907  32.412  -5.918  1.00 93.03  ? 1118 ILE   B CA  1 
ATOM   2785 C C   . ILE   B 1 81  ? -10.026 31.645  -6.624  1.00 90.99  ? 1118 ILE   B C   1 
ATOM   2786 O O   . ILE   B 1 81  ? -11.202 31.906  -6.377  1.00 88.16  ? 1118 ILE   B O   1 
ATOM   2787 C CB  . ILE   B 1 81  ? -8.539  33.713  -6.665  1.00 95.86  ? 1118 ILE   B CB  1 
ATOM   2788 C CG1 . ILE   B 1 81  ? -9.641  34.771  -6.552  1.00 94.03  ? 1118 ILE   B CG1 1 
ATOM   2789 C CG2 . ILE   B 1 81  ? -8.170  33.442  -8.118  1.00 99.00  ? 1118 ILE   B CG2 1 
ATOM   2790 C CD1 . ILE   B 1 81  ? -9.906  35.237  -5.139  1.00 91.87  ? 1118 ILE   B CD1 1 
ATOM   2791 N N   . GLY   B 1 82  ? -9.655  30.709  -7.507  1.00 92.57  ? 1119 GLY   B N   1 
ATOM   2792 C CA  . GLY   B 1 82  ? -10.622 29.932  -8.267  1.00 91.48  ? 1119 GLY   B CA  1 
ATOM   2793 C C   . GLY   B 1 82  ? -11.464 29.019  -7.378  1.00 87.71  ? 1119 GLY   B C   1 
ATOM   2794 O O   . GLY   B 1 82  ? -12.666 28.881  -7.592  1.00 86.04  ? 1119 GLY   B O   1 
ATOM   2795 N N   . GLU   B 1 83  ? -10.818 28.410  -6.376  1.00 86.66  ? 1120 GLU   B N   1 
ATOM   2796 C CA  . GLU   B 1 83  ? -11.465 27.453  -5.492  1.00 83.59  ? 1120 GLU   B CA  1 
ATOM   2797 C C   . GLU   B 1 83  ? -12.465 28.160  -4.576  1.00 80.16  ? 1120 GLU   B C   1 
ATOM   2798 O O   . GLU   B 1 83  ? -13.378 27.522  -4.056  1.00 77.55  ? 1120 GLU   B O   1 
ATOM   2799 C CB  . GLU   B 1 83  ? -10.410 26.690  -4.687  1.00 84.44  ? 1120 GLU   B CB  1 
ATOM   2800 C CG  . GLU   B 1 83  ? -9.528  25.799  -5.546  1.00 87.74  ? 1120 GLU   B CG  1 
ATOM   2801 C CD  . GLU   B 1 83  ? -8.378  25.115  -4.824  1.00 89.21  ? 1120 GLU   B CD  1 
ATOM   2802 O OE1 . GLU   B 1 83  ? -7.664  24.325  -5.473  1.00 91.97  ? 1120 GLU   B OE1 1 
ATOM   2803 O OE2 . GLU   B 1 83  ? -8.191  25.378  -3.620  1.00 88.10  ? 1120 GLU   B OE2 1 
ATOM   2804 N N   . VAL   B 1 84  ? -12.281 29.472  -4.379  1.00 80.32  ? 1121 VAL   B N   1 
ATOM   2805 C CA  . VAL   B 1 84  ? -13.219 30.282  -3.617  1.00 78.12  ? 1121 VAL   B CA  1 
ATOM   2806 C C   . VAL   B 1 84  ? -14.500 30.459  -4.430  1.00 77.31  ? 1121 VAL   B C   1 
ATOM   2807 O O   . VAL   B 1 84  ? -15.596 30.246  -3.916  1.00 75.11  ? 1121 VAL   B O   1 
ATOM   2808 C CB  . VAL   B 1 84  ? -12.606 31.644  -3.232  1.00 79.25  ? 1121 VAL   B CB  1 
ATOM   2809 C CG1 . VAL   B 1 84  ? -13.623 32.560  -2.566  1.00 77.56  ? 1121 VAL   B CG1 1 
ATOM   2810 C CG2 . VAL   B 1 84  ? -11.377 31.482  -2.349  1.00 80.29  ? 1121 VAL   B CG2 1 
ATOM   2811 N N   . SER   B 1 85  ? -14.344 30.849  -5.702  1.00 79.32  ? 1122 SER   B N   1 
ATOM   2812 C CA  . SER   B 1 85  ? -15.467 31.101  -6.593  1.00 79.38  ? 1122 SER   B CA  1 
ATOM   2813 C C   . SER   B 1 85  ? -16.300 29.835  -6.790  1.00 78.39  ? 1122 SER   B C   1 
ATOM   2814 O O   . SER   B 1 85  ? -17.517 29.914  -6.943  1.00 77.45  ? 1122 SER   B O   1 
ATOM   2815 C CB  . SER   B 1 85  ? -14.987 31.646  -7.914  1.00 82.33  ? 1122 SER   B CB  1 
ATOM   2816 O OG  . SER   B 1 85  ? -14.238 32.837  -7.727  1.00 83.45  ? 1122 SER   B OG  1 
ATOM   2817 N N   . GLN   B 1 86  ? -15.627 28.677  -6.799  1.00 78.96  ? 1123 GLN   B N   1 
ATOM   2818 C CA  . GLN   B 1 86  ? -16.285 27.382  -6.889  1.00 78.32  ? 1123 GLN   B CA  1 
ATOM   2819 C C   . GLN   B 1 86  ? -17.292 27.229  -5.751  1.00 75.20  ? 1123 GLN   B C   1 
ATOM   2820 O O   . GLN   B 1 86  ? -18.444 26.873  -5.986  1.00 74.39  ? 1123 GLN   B O   1 
ATOM   2821 C CB  . GLN   B 1 86  ? -15.238 26.263  -6.854  1.00 79.65  ? 1123 GLN   B CB  1 
ATOM   2822 C CG  . GLN   B 1 86  ? -15.806 24.864  -6.638  1.00 78.67  ? 1123 GLN   B CG  1 
ATOM   2823 C CD  . GLN   B 1 86  ? -16.667 24.373  -7.777  1.00 80.02  ? 1123 GLN   B CD  1 
ATOM   2824 O OE1 . GLN   B 1 86  ? -16.751 24.991  -8.835  1.00 82.18  ? 1123 GLN   B OE1 1 
ATOM   2825 N NE2 . GLN   B 1 86  ? -17.304 23.232  -7.574  1.00 79.20  ? 1123 GLN   B NE2 1 
ATOM   2826 N N   . PHE   B 1 87  ? -16.840 27.506  -4.523  1.00 73.68  ? 1124 PHE   B N   1 
ATOM   2827 C CA  . PHE   B 1 87  ? -17.613 27.223  -3.324  1.00 71.32  ? 1124 PHE   B CA  1 
ATOM   2828 C C   . PHE   B 1 87  ? -18.746 28.236  -3.155  1.00 70.52  ? 1124 PHE   B C   1 
ATOM   2829 O O   . PHE   B 1 87  ? -19.792 27.899  -2.602  1.00 69.36  ? 1124 PHE   B O   1 
ATOM   2830 C CB  . PHE   B 1 87  ? -16.691 27.197  -2.102  1.00 70.82  ? 1124 PHE   B CB  1 
ATOM   2831 C CG  . PHE   B 1 87  ? -17.378 26.877  -0.798  1.00 69.00  ? 1124 PHE   B CG  1 
ATOM   2832 C CD1 . PHE   B 1 87  ? -18.190 25.758  -0.678  1.00 68.04  ? 1124 PHE   B CD1 1 
ATOM   2833 C CD2 . PHE   B 1 87  ? -17.207 27.689  0.314   1.00 68.67  ? 1124 PHE   B CD2 1 
ATOM   2834 C CE1 . PHE   B 1 87  ? -18.821 25.464  0.521   1.00 66.59  ? 1124 PHE   B CE1 1 
ATOM   2835 C CE2 . PHE   B 1 87  ? -17.837 27.391  1.513   1.00 67.49  ? 1124 PHE   B CE2 1 
ATOM   2836 C CZ  . PHE   B 1 87  ? -18.643 26.280  1.614   1.00 66.38  ? 1124 PHE   B CZ  1 
ATOM   2837 N N   . LEU   B 1 88  ? -18.531 29.472  -3.623  1.00 71.34  ? 1125 LEU   B N   1 
ATOM   2838 C CA  . LEU   B 1 88  ? -19.529 30.525  -3.508  1.00 70.77  ? 1125 LEU   B CA  1 
ATOM   2839 C C   . LEU   B 1 88  ? -20.775 30.169  -4.318  1.00 70.98  ? 1125 LEU   B C   1 
ATOM   2840 O O   . LEU   B 1 88  ? -21.892 30.394  -3.857  1.00 70.30  ? 1125 LEU   B O   1 
ATOM   2841 C CB  . LEU   B 1 88  ? -18.928 31.853  -3.985  1.00 72.22  ? 1125 LEU   B CB  1 
ATOM   2842 C CG  . LEU   B 1 88  ? -17.999 32.555  -2.994  1.00 71.93  ? 1125 LEU   B CG  1 
ATOM   2843 C CD1 . LEU   B 1 88  ? -17.464 33.850  -3.585  1.00 73.71  ? 1125 LEU   B CD1 1 
ATOM   2844 C CD2 . LEU   B 1 88  ? -18.708 32.828  -1.674  1.00 70.32  ? 1125 LEU   B CD2 1 
ATOM   2845 N N   . THR   B 1 89  ? -20.571 29.617  -5.520  1.00 72.35  ? 1126 THR   B N   1 
ATOM   2846 C CA  . THR   B 1 89  ? -21.667 29.229  -6.395  1.00 73.24  ? 1126 THR   B CA  1 
ATOM   2847 C C   . THR   B 1 89  ? -22.435 28.053  -5.790  1.00 71.71  ? 1126 THR   B C   1 
ATOM   2848 O O   . THR   B 1 89  ? -23.653 27.974  -5.932  1.00 71.97  ? 1126 THR   B O   1 
ATOM   2849 C CB  . THR   B 1 89  ? -21.159 28.903  -7.806  1.00 75.64  ? 1126 THR   B CB  1 
ATOM   2850 O OG1 . THR   B 1 89  ? -20.157 27.891  -7.704  1.00 75.49  ? 1126 THR   B OG1 1 
ATOM   2851 C CG2 . THR   B 1 89  ? -20.591 30.111  -8.518  1.00 77.39  ? 1126 THR   B CG2 1 
ATOM   2852 N N   . GLU   B 1 90  ? -21.711 27.144  -5.124  1.00 70.24  ? 1127 GLU   B N   1 
ATOM   2853 C CA  . GLU   B 1 90  ? -22.322 26.017  -4.435  1.00 68.82  ? 1127 GLU   B CA  1 
ATOM   2854 C C   . GLU   B 1 90  ? -23.145 26.513  -3.247  1.00 67.17  ? 1127 GLU   B C   1 
ATOM   2855 O O   . GLU   B 1 90  ? -24.211 25.970  -2.962  1.00 66.98  ? 1127 GLU   B O   1 
ATOM   2856 C CB  . GLU   B 1 90  ? -21.254 25.035  -3.949  1.00 68.22  ? 1127 GLU   B CB  1 
ATOM   2857 C CG  . GLU   B 1 90  ? -20.500 24.336  -5.066  1.00 70.09  ? 1127 GLU   B CG  1 
ATOM   2858 C CD  . GLU   B 1 90  ? -19.378 23.425  -4.597  1.00 69.85  ? 1127 GLU   B CD  1 
ATOM   2859 O OE1 . GLU   B 1 90  ? -19.147 23.347  -3.372  1.00 68.19  ? 1127 GLU   B OE1 1 
ATOM   2860 O OE2 . GLU   B 1 90  ? -18.737 22.790  -5.457  1.00 71.63  ? 1127 GLU   B OE2 1 
ATOM   2861 N N   . GLY   B 1 91  ? -22.636 27.546  -2.563  1.00 66.37  ? 1128 GLY   B N   1 
ATOM   2862 C CA  . GLY   B 1 91  ? -23.265 28.088  -1.368  1.00 65.25  ? 1128 GLY   B CA  1 
ATOM   2863 C C   . GLY   B 1 91  ? -24.646 28.686  -1.633  1.00 66.08  ? 1128 GLY   B C   1 
ATOM   2864 O O   . GLY   B 1 91  ? -25.466 28.757  -0.722  1.00 65.42  ? 1128 GLY   B O   1 
ATOM   2865 N N   . ILE   B 1 92  ? -24.887 29.121  -2.878  1.00 67.90  ? 1129 ILE   B N   1 
ATOM   2866 C CA  . ILE   B 1 92  ? -26.170 29.684  -3.274  1.00 69.55  ? 1129 ILE   B CA  1 
ATOM   2867 C C   . ILE   B 1 92  ? -27.256 28.620  -3.129  1.00 69.55  ? 1129 ILE   B C   1 
ATOM   2868 O O   . ILE   B 1 92  ? -28.340 28.905  -2.624  1.00 70.31  ? 1129 ILE   B O   1 
ATOM   2869 C CB  . ILE   B 1 92  ? -26.112 30.240  -4.714  1.00 71.75  ? 1129 ILE   B CB  1 
ATOM   2870 C CG1 . ILE   B 1 92  ? -25.114 31.395  -4.843  1.00 72.25  ? 1129 ILE   B CG1 1 
ATOM   2871 C CG2 . ILE   B 1 92  ? -27.500 30.646  -5.194  1.00 73.53  ? 1129 ILE   B CG2 1 
ATOM   2872 C CD1 . ILE   B 1 92  ? -24.809 31.793  -6.270  1.00 74.40  ? 1129 ILE   B CD1 1 
ATOM   2873 N N   . ILE   B 1 93  ? -26.950 27.398  -3.584  1.00 69.08  ? 1130 ILE   B N   1 
ATOM   2874 C CA  . ILE   B 1 93  ? -27.898 26.295  -3.571  1.00 69.23  ? 1130 ILE   B CA  1 
ATOM   2875 C C   . ILE   B 1 93  ? -28.089 25.810  -2.134  1.00 67.15  ? 1130 ILE   B C   1 
ATOM   2876 O O   . ILE   B 1 93  ? -29.192 25.423  -1.752  1.00 67.66  ? 1130 ILE   B O   1 
ATOM   2877 C CB  . ILE   B 1 93  ? -27.430 25.159  -4.506  1.00 69.95  ? 1130 ILE   B CB  1 
ATOM   2878 C CG1 . ILE   B 1 93  ? -27.255 25.645  -5.949  1.00 72.13  ? 1130 ILE   B CG1 1 
ATOM   2879 C CG2 . ILE   B 1 93  ? -28.375 23.967  -4.424  1.00 70.51  ? 1130 ILE   B CG2 1 
ATOM   2880 C CD1 . ILE   B 1 93  ? -26.626 24.628  -6.876  1.00 73.08  ? 1130 ILE   B CD1 1 
ATOM   2881 N N   . MET   B 1 94  ? -27.005 25.840  -1.349  1.00 65.12  ? 1131 MET   B N   1 
ATOM   2882 C CA  . MET   B 1 94  ? -27.010 25.348  0.020   1.00 63.59  ? 1131 MET   B CA  1 
ATOM   2883 C C   . MET   B 1 94  ? -27.855 26.257  0.912   1.00 63.99  ? 1131 MET   B C   1 
ATOM   2884 O O   . MET   B 1 94  ? -28.475 25.786  1.863   1.00 63.57  ? 1131 MET   B O   1 
ATOM   2885 C CB  . MET   B 1 94  ? -25.584 25.293  0.576   1.00 62.13  ? 1131 MET   B CB  1 
ATOM   2886 C CG  . MET   B 1 94  ? -24.760 24.154  0.015   1.00 61.67  ? 1131 MET   B CG  1 
ATOM   2887 S SD  . MET   B 1 94  ? -23.076 24.161  0.675   1.00 60.63  ? 1131 MET   B SD  1 
ATOM   2888 C CE  . MET   B 1 94  ? -22.154 23.530  -0.731  1.00 61.88  ? 1131 MET   B CE  1 
ATOM   2889 N N   . LYS   B 1 95  ? -27.855 27.560  0.607   1.00 64.96  ? 1132 LYS   B N   1 
ATOM   2890 C CA  . LYS   B 1 95  ? -28.609 28.540  1.375   1.00 65.97  ? 1132 LYS   B CA  1 
ATOM   2891 C C   . LYS   B 1 95  ? -30.103 28.328  1.129   1.00 67.51  ? 1132 LYS   B C   1 
ATOM   2892 O O   . LYS   B 1 95  ? -30.909 28.454  2.049   1.00 68.40  ? 1132 LYS   B O   1 
ATOM   2893 C CB  . LYS   B 1 95  ? -28.165 29.957  0.995   1.00 66.96  ? 1132 LYS   B CB  1 
ATOM   2894 C CG  . LYS   B 1 95  ? -28.309 31.017  2.081   1.00 67.90  ? 1132 LYS   B CG  1 
ATOM   2895 C CD  . LYS   B 1 95  ? -29.737 31.336  2.469   1.00 70.19  ? 1132 LYS   B CD  1 
ATOM   2896 C CE  . LYS   B 1 95  ? -29.865 32.638  3.234   1.00 71.65  ? 1132 LYS   B CE  1 
ATOM   2897 N NZ  . LYS   B 1 95  ? -29.032 32.643  4.462   1.00 70.77  ? 1132 LYS   B NZ  1 
ATOM   2898 N N   . ASP   B 1 96  ? -30.455 27.982  -0.118  1.00 68.18  ? 1133 ASP   B N   1 
ATOM   2899 C CA  . ASP   B 1 96  ? -31.842 27.812  -0.525  1.00 69.95  ? 1133 ASP   B CA  1 
ATOM   2900 C C   . ASP   B 1 96  ? -32.466 26.598  0.163   1.00 69.34  ? 1133 ASP   B C   1 
ATOM   2901 O O   . ASP   B 1 96  ? -33.681 26.559  0.348   1.00 71.28  ? 1133 ASP   B O   1 
ATOM   2902 C CB  . ASP   B 1 96  ? -31.964 27.687  -2.047  1.00 71.34  ? 1133 ASP   B CB  1 
ATOM   2903 C CG  . ASP   B 1 96  ? -31.586 28.945  -2.811  1.00 72.15  ? 1133 ASP   B CG  1 
ATOM   2904 O OD1 . ASP   B 1 96  ? -31.180 29.931  -2.163  1.00 71.38  ? 1133 ASP   B OD1 1 
ATOM   2905 O OD2 . ASP   B 1 96  ? -31.703 28.930  -4.052  1.00 73.64  ? 1133 ASP   B OD2 1 
ATOM   2906 N N   . PHE   B 1 97  ? -31.638 25.607  0.522   1.00 66.69  ? 1134 PHE   B N   1 
ATOM   2907 C CA  . PHE   B 1 97  ? -32.107 24.438  1.251   1.00 66.00  ? 1134 PHE   B CA  1 
ATOM   2908 C C   . PHE   B 1 97  ? -32.807 24.883  2.533   1.00 66.51  ? 1134 PHE   B C   1 
ATOM   2909 O O   . PHE   B 1 97  ? -32.188 25.498  3.399   1.00 65.35  ? 1134 PHE   B O   1 
ATOM   2910 C CB  . PHE   B 1 97  ? -30.949 23.489  1.577   1.00 63.51  ? 1134 PHE   B CB  1 
ATOM   2911 C CG  . PHE   B 1 97  ? -30.303 22.790  0.403   1.00 62.99  ? 1134 PHE   B CG  1 
ATOM   2912 C CD1 . PHE   B 1 97  ? -30.827 22.878  -0.881  1.00 64.73  ? 1134 PHE   B CD1 1 
ATOM   2913 C CD2 . PHE   B 1 97  ? -29.156 22.033  0.591   1.00 61.10  ? 1134 PHE   B CD2 1 
ATOM   2914 C CE1 . PHE   B 1 97  ? -30.217 22.226  -1.943  1.00 64.85  ? 1134 PHE   B CE1 1 
ATOM   2915 C CE2 . PHE   B 1 97  ? -28.548 21.383  -0.473  1.00 61.22  ? 1134 PHE   B CE2 1 
ATOM   2916 C CZ  . PHE   B 1 97  ? -29.080 21.480  -1.737  1.00 63.13  ? 1134 PHE   B CZ  1 
ATOM   2917 N N   . SER   B 1 98  ? -34.106 24.571  2.626   1.00 68.58  ? 1135 SER   B N   1 
ATOM   2918 C CA  . SER   B 1 98  ? -34.921 24.911  3.781   1.00 69.94  ? 1135 SER   B CA  1 
ATOM   2919 C C   . SER   B 1 98  ? -35.790 23.714  4.160   1.00 70.91  ? 1135 SER   B C   1 
ATOM   2920 O O   . SER   B 1 98  ? -36.818 23.467  3.530   1.00 73.25  ? 1135 SER   B O   1 
ATOM   2921 C CB  . SER   B 1 98  ? -35.756 26.136  3.502   1.00 72.53  ? 1135 SER   B CB  1 
ATOM   2922 O OG  . SER   B 1 98  ? -36.589 26.448  4.608   1.00 74.51  ? 1135 SER   B OG  1 
ATOM   2923 N N   . HIS   B 1 99  ? -35.358 22.974  5.188   1.00 69.21  ? 1136 HIS   B N   1 
ATOM   2924 C CA  . HIS   B 1 99  ? -36.073 21.796  5.653   1.00 69.94  ? 1136 HIS   B CA  1 
ATOM   2925 C C   . HIS   B 1 99  ? -35.787 21.582  7.138   1.00 69.22  ? 1136 HIS   B C   1 
ATOM   2926 O O   . HIS   B 1 99  ? -34.682 21.871  7.597   1.00 67.05  ? 1136 HIS   B O   1 
ATOM   2927 C CB  . HIS   B 1 99  ? -35.669 20.575  4.818   1.00 68.54  ? 1136 HIS   B CB  1 
ATOM   2928 C CG  . HIS   B 1 99  ? -36.568 19.385  4.959   1.00 70.11  ? 1136 HIS   B CG  1 
ATOM   2929 N ND1 . HIS   B 1 99  ? -37.872 19.359  4.530   1.00 73.50  ? 1136 HIS   B ND1 1 
ATOM   2930 C CD2 . HIS   B 1 99  ? -36.304 18.159  5.493   1.00 69.07  ? 1136 HIS   B CD2 1 
ATOM   2931 C CE1 . HIS   B 1 99  ? -38.397 18.165  4.795   1.00 74.39  ? 1136 HIS   B CE1 1 
ATOM   2932 N NE2 . HIS   B 1 99  ? -37.440 17.403  5.395   1.00 71.62  ? 1136 HIS   B NE2 1 
ATOM   2933 N N   . PRO   B 1 100 ? -36.757 21.079  7.941   1.00 71.29  ? 1137 PRO   B N   1 
ATOM   2934 C CA  . PRO   B 1 100 ? -36.548 20.889  9.379   1.00 71.14  ? 1137 PRO   B CA  1 
ATOM   2935 C C   . PRO   B 1 100 ? -35.617 19.732  9.743   1.00 68.55  ? 1137 PRO   B C   1 
ATOM   2936 O O   . PRO   B 1 100 ? -35.232 19.600  10.903  1.00 68.44  ? 1137 PRO   B O   1 
ATOM   2937 C CB  . PRO   B 1 100 ? -37.956 20.610  9.938   1.00 74.69  ? 1137 PRO   B CB  1 
ATOM   2938 C CG  . PRO   B 1 100 ? -38.909 20.936  8.802   1.00 76.96  ? 1137 PRO   B CG  1 
ATOM   2939 C CD  . PRO   B 1 100 ? -38.118 20.700  7.534   1.00 74.41  ? 1137 PRO   B CD  1 
ATOM   2940 N N   . ASN   B 1 101 ? -35.273 18.894  8.755   1.00 66.84  ? 1138 ASN   B N   1 
ATOM   2941 C CA  . ASN   B 1 101 ? -34.326 17.808  8.956   1.00 64.45  ? 1138 ASN   B CA  1 
ATOM   2942 C C   . ASN   B 1 101 ? -33.148 17.962  7.995   1.00 62.01  ? 1138 ASN   B C   1 
ATOM   2943 O O   . ASN   B 1 101 ? -32.603 16.969  7.516   1.00 60.57  ? 1138 ASN   B O   1 
ATOM   2944 C CB  . ASN   B 1 101 ? -34.997 16.441  8.802   1.00 65.31  ? 1138 ASN   B CB  1 
ATOM   2945 C CG  . ASN   B 1 101 ? -36.143 16.235  9.768   1.00 67.84  ? 1138 ASN   B CG  1 
ATOM   2946 O OD1 . ASN   B 1 101 ? -37.272 15.983  9.354   1.00 70.29  ? 1138 ASN   B OD1 1 
ATOM   2947 N ND2 . ASN   B 1 101 ? -35.864 16.340  11.057  1.00 67.66  ? 1138 ASN   B ND2 1 
ATOM   2948 N N   . VAL   B 1 102 ? -32.760 19.217  7.731   1.00 61.65  ? 1139 VAL   B N   1 
ATOM   2949 C CA  . VAL   B 1 102 ? -31.557 19.525  6.972   1.00 59.66  ? 1139 VAL   B CA  1 
ATOM   2950 C C   . VAL   B 1 102 ? -30.897 20.744  7.611   1.00 58.94  ? 1139 VAL   B C   1 
ATOM   2951 O O   . VAL   B 1 102 ? -31.545 21.772  7.800   1.00 60.40  ? 1139 VAL   B O   1 
ATOM   2952 C CB  . VAL   B 1 102 ? -31.863 19.768  5.480   1.00 60.33  ? 1139 VAL   B CB  1 
ATOM   2953 C CG1 . VAL   B 1 102 ? -30.628 20.227  4.716   1.00 58.87  ? 1139 VAL   B CG1 1 
ATOM   2954 C CG2 . VAL   B 1 102 ? -32.476 18.542  4.818   1.00 61.13  ? 1139 VAL   B CG2 1 
ATOM   2955 N N   . LEU   B 1 103 ? -29.607 20.611  7.945   1.00 56.91  ? 1140 LEU   B N   1 
ATOM   2956 C CA  . LEU   B 1 103 ? -28.843 21.696  8.537   1.00 56.59  ? 1140 LEU   B CA  1 
ATOM   2957 C C   . LEU   B 1 103 ? -28.211 22.523  7.420   1.00 56.13  ? 1140 LEU   B C   1 
ATOM   2958 O O   . LEU   B 1 103 ? -27.091 22.248  6.993   1.00 54.87  ? 1140 LEU   B O   1 
ATOM   2959 C CB  . LEU   B 1 103 ? -27.785 21.111  9.478   1.00 55.49  ? 1140 LEU   B CB  1 
ATOM   2960 C CG  . LEU   B 1 103 ? -26.999 22.130  10.304  1.00 55.68  ? 1140 LEU   B CG  1 
ATOM   2961 C CD1 . LEU   B 1 103 ? -27.875 22.743  11.386  1.00 57.47  ? 1140 LEU   B CD1 1 
ATOM   2962 C CD2 . LEU   B 1 103 ? -25.761 21.494  10.917  1.00 54.78  ? 1140 LEU   B CD2 1 
ATOM   2963 N N   . SER   B 1 104 ? -28.957 23.530  6.947   1.00 57.55  ? 1141 SER   B N   1 
ATOM   2964 C CA  . SER   B 1 104 ? -28.481 24.434  5.913   1.00 57.56  ? 1141 SER   B CA  1 
ATOM   2965 C C   . SER   B 1 104 ? -27.600 25.514  6.537   1.00 57.32  ? 1141 SER   B C   1 
ATOM   2966 O O   . SER   B 1 104 ? -27.817 25.911  7.681   1.00 57.90  ? 1141 SER   B O   1 
ATOM   2967 C CB  . SER   B 1 104 ? -29.633 25.039  5.151   1.00 59.29  ? 1141 SER   B CB  1 
ATOM   2968 O OG  . SER   B 1 104 ? -30.485 25.775  6.017   1.00 60.87  ? 1141 SER   B OG  1 
ATOM   2969 N N   . LEU   B 1 105 ? -26.610 25.978  5.766   1.00 56.65  ? 1142 LEU   B N   1 
ATOM   2970 C CA  . LEU   B 1 105 ? -25.666 26.981  6.234   1.00 56.62  ? 1142 LEU   B CA  1 
ATOM   2971 C C   . LEU   B 1 105 ? -26.350 28.345  6.304   1.00 57.94  ? 1142 LEU   B C   1 
ATOM   2972 O O   . LEU   B 1 105 ? -27.253 28.635  5.520   1.00 58.63  ? 1142 LEU   B O   1 
ATOM   2973 C CB  . LEU   B 1 105 ? -24.437 27.014  5.314   1.00 55.91  ? 1142 LEU   B CB  1 
ATOM   2974 C CG  . LEU   B 1 105 ? -24.687 27.297  3.830   1.00 56.32  ? 1142 LEU   B CG  1 
ATOM   2975 C CD1 . LEU   B 1 105 ? -24.879 28.782  3.559   1.00 57.47  ? 1142 LEU   B CD1 1 
ATOM   2976 C CD2 . LEU   B 1 105 ? -23.546 26.753  2.984   1.00 55.91  ? 1142 LEU   B CD2 1 
ATOM   2977 N N   . LEU   B 1 106 ? -25.903 29.167  7.260   1.00 58.46  ? 1143 LEU   B N   1 
ATOM   2978 C CA  . LEU   B 1 106 ? -26.332 30.553  7.361   1.00 60.03  ? 1143 LEU   B CA  1 
ATOM   2979 C C   . LEU   B 1 106 ? -25.674 31.352  6.241   1.00 60.08  ? 1143 LEU   B C   1 
ATOM   2980 O O   . LEU   B 1 106 ? -26.344 32.098  5.529   1.00 60.98  ? 1143 LEU   B O   1 
ATOM   2981 C CB  . LEU   B 1 106 ? -25.942 31.105  8.737   1.00 60.89  ? 1143 LEU   B CB  1 
ATOM   2982 C CG  . LEU   B 1 106 ? -26.529 30.370  9.942   1.00 61.32  ? 1143 LEU   B CG  1 
ATOM   2983 C CD1 . LEU   B 1 106 ? -26.240 31.127  11.231  1.00 63.05  ? 1143 LEU   B CD1 1 
ATOM   2984 C CD2 . LEU   B 1 106 ? -28.026 30.151  9.778   1.00 62.31  ? 1143 LEU   B CD2 1 
ATOM   2985 N N   . GLY   B 1 107 ? -24.354 31.179  6.097   1.00 59.41  ? 1144 GLY   B N   1 
ATOM   2986 C CA  . GLY   B 1 107 ? -23.615 31.780  5.000   1.00 59.75  ? 1144 GLY   B CA  1 
ATOM   2987 C C   . GLY   B 1 107 ? -22.108 31.558  5.121   1.00 59.51  ? 1144 GLY   B C   1 
ATOM   2988 O O   . GLY   B 1 107 ? -21.634 30.986  6.101   1.00 58.89  ? 1144 GLY   B O   1 
ATOM   2989 N N   . ILE   B 1 108 ? -21.376 32.028  4.104   1.00 60.37  ? 1145 ILE   B N   1 
ATOM   2990 C CA  . ILE   B 1 108 ? -19.931 31.884  4.023   1.00 60.83  ? 1145 ILE   B CA  1 
ATOM   2991 C C   . ILE   B 1 108 ? -19.294 33.220  4.399   1.00 62.51  ? 1145 ILE   B C   1 
ATOM   2992 O O   . ILE   B 1 108 ? -19.772 34.272  3.980   1.00 63.26  ? 1145 ILE   B O   1 
ATOM   2993 C CB  . ILE   B 1 108 ? -19.511 31.431  2.607   1.00 60.91  ? 1145 ILE   B CB  1 
ATOM   2994 C CG1 . ILE   B 1 108 ? -20.347 30.246  2.113   1.00 59.99  ? 1145 ILE   B CG1 1 
ATOM   2995 C CG2 . ILE   B 1 108 ? -18.020 31.128  2.548   1.00 61.41  ? 1145 ILE   B CG2 1 
ATOM   2996 C CD1 . ILE   B 1 108 ? -20.156 29.921  0.648   1.00 60.54  ? 1145 ILE   B CD1 1 
ATOM   2997 N N   . CYS   B 1 109 ? -18.212 33.167  5.185   1.00 63.57  ? 1146 CYS   B N   1 
ATOM   2998 C CA  . CYS   B 1 109 ? -17.492 34.365  5.589   1.00 65.86  ? 1146 CYS   B CA  1 
ATOM   2999 C C   . CYS   B 1 109 ? -16.077 34.339  5.015   1.00 67.43  ? 1146 CYS   B C   1 
ATOM   3000 O O   . CYS   B 1 109 ? -15.215 33.615  5.511   1.00 67.67  ? 1146 CYS   B O   1 
ATOM   3001 C CB  . CYS   B 1 109 ? -17.439 34.493  7.107   1.00 66.46  ? 1146 CYS   B CB  1 
ATOM   3002 S SG  . CYS   B 1 109 ? -16.582 35.987  7.669   1.00 68.76  ? 1146 CYS   B SG  1 
ATOM   3003 N N   . LEU   B 1 110 ? -15.856 35.137  3.964   1.00 69.04  ? 1147 LEU   B N   1 
ATOM   3004 C CA  . LEU   B 1 110 ? -14.536 35.300  3.375   1.00 71.16  ? 1147 LEU   B CA  1 
ATOM   3005 C C   . LEU   B 1 110 ? -13.718 36.253  4.240   1.00 73.65  ? 1147 LEU   B C   1 
ATOM   3006 O O   . LEU   B 1 110 ? -14.275 37.143  4.882   1.00 74.14  ? 1147 LEU   B O   1 
ATOM   3007 C CB  . LEU   B 1 110 ? -14.673 35.843  1.948   1.00 71.87  ? 1147 LEU   B CB  1 
ATOM   3008 C CG  . LEU   B 1 110 ? -15.103 34.829  0.888   1.00 70.99  ? 1147 LEU   B CG  1 
ATOM   3009 C CD1 . LEU   B 1 110 ? -16.586 34.507  1.000   1.00 69.36  ? 1147 LEU   B CD1 1 
ATOM   3010 C CD2 . LEU   B 1 110 ? -14.772 35.333  -0.509  1.00 72.57  ? 1147 LEU   B CD2 1 
ATOM   3011 N N   . ARG   B 1 111 ? -12.395 36.053  4.249   1.00 75.84  ? 1148 ARG   B N   1 
ATOM   3012 C CA  . ARG   B 1 111 ? -11.486 36.952  4.941   1.00 78.86  ? 1148 ARG   B CA  1 
ATOM   3013 C C   . ARG   B 1 111 ? -10.096 36.836  4.318   1.00 81.54  ? 1148 ARG   B C   1 
ATOM   3014 O O   . ARG   B 1 111 ? -9.793  35.851  3.647   1.00 81.37  ? 1148 ARG   B O   1 
ATOM   3015 C CB  . ARG   B 1 111 ? -11.479 36.656  6.446   1.00 79.01  ? 1148 ARG   B CB  1 
ATOM   3016 C CG  . ARG   B 1 111 ? -10.894 35.305  6.834   1.00 78.57  ? 1148 ARG   B CG  1 
ATOM   3017 C CD  . ARG   B 1 111 ? -10.997 35.060  8.330   1.00 78.82  ? 1148 ARG   B CD  1 
ATOM   3018 N NE  . ARG   B 1 111 ? -10.049 34.067  8.820   1.00 79.55  ? 1148 ARG   B NE  1 
ATOM   3019 C CZ  . ARG   B 1 111 ? -10.048 32.783  8.480   1.00 77.82  ? 1148 ARG   B CZ  1 
ATOM   3020 N NH1 . ARG   B 1 111 ? -11.014 32.298  7.723   1.00 75.04  ? 1148 ARG   B NH1 1 
ATOM   3021 N NH2 . ARG   B 1 111 ? -9.084  31.985  8.906   1.00 79.12  ? 1148 ARG   B NH2 1 
ATOM   3022 N N   . SER   B 1 112 ? -9.266  37.861  4.553   1.00 84.55  ? 1149 SER   B N   1 
ATOM   3023 C CA  . SER   B 1 112 ? -7.931  37.941  3.982   1.00 87.55  ? 1149 SER   B CA  1 
ATOM   3024 C C   . SER   B 1 112 ? -6.896  37.311  4.914   1.00 89.46  ? 1149 SER   B C   1 
ATOM   3025 O O   . SER   B 1 112 ? -5.736  37.165  4.532   1.00 92.21  ? 1149 SER   B O   1 
ATOM   3026 C CB  . SER   B 1 112 ? -7.572  39.370  3.664   1.00 89.98  ? 1149 SER   B CB  1 
ATOM   3027 O OG  . SER   B 1 112 ? -8.445  39.904  2.679   1.00 88.83  ? 1149 SER   B OG  1 
ATOM   3028 N N   . GLU   B 1 113 ? -7.317  36.946  6.133   1.00 88.45  ? 1150 GLU   B N   1 
ATOM   3029 C CA  . GLU   B 1 113 ? -6.423  36.356  7.117   1.00 90.19  ? 1150 GLU   B CA  1 
ATOM   3030 C C   . GLU   B 1 113 ? -6.006  34.960  6.658   1.00 89.18  ? 1150 GLU   B C   1 
ATOM   3031 O O   . GLU   B 1 113 ? -4.822  34.707  6.446   1.00 92.05  ? 1150 GLU   B O   1 
ATOM   3032 C CB  . GLU   B 1 113 ? -7.094  36.303  8.491   1.00 89.44  ? 1150 GLU   B CB  1 
ATOM   3033 C CG  . GLU   B 1 113 ? -7.387  37.670  9.081   1.00 91.04  ? 1150 GLU   B CG  1 
ATOM   3034 C CD  . GLU   B 1 113 ? -8.016  37.636  10.463  1.00 90.92  ? 1150 GLU   B CD  1 
ATOM   3035 O OE1 . GLU   B 1 113 ? -9.105  37.045  10.601  1.00 88.10  ? 1150 GLU   B OE1 1 
ATOM   3036 O OE2 . GLU   B 1 113 ? -7.415  38.201  11.399  1.00 94.05  ? 1150 GLU   B OE2 1 
ATOM   3037 N N   . GLY   B 1 114 ? -6.996  34.071  6.504   1.00 85.40  ? 1151 GLY   B N   1 
ATOM   3038 C CA  . GLY   B 1 114 ? -6.757  32.690  6.116   1.00 84.26  ? 1151 GLY   B CA  1 
ATOM   3039 C C   . GLY   B 1 114 ? -7.778  32.209  5.088   1.00 81.06  ? 1151 GLY   B C   1 
ATOM   3040 O O   . GLY   B 1 114 ? -8.242  32.988  4.257   1.00 80.62  ? 1151 GLY   B O   1 
ATOM   3041 N N   . SER   B 1 115 ? -8.116  30.916  5.159   1.00 79.03  ? 1152 SER   B N   1 
ATOM   3042 C CA  . SER   B 1 115 ? -9.071  30.306  4.247   1.00 76.45  ? 1152 SER   B CA  1 
ATOM   3043 C C   . SER   B 1 115 ? -10.493 30.692  4.651   1.00 73.56  ? 1152 SER   B C   1 
ATOM   3044 O O   . SER   B 1 115 ? -10.717 31.109  5.784   1.00 73.40  ? 1152 SER   B O   1 
ATOM   3045 C CB  . SER   B 1 115 ? -8.893  28.810  4.212   1.00 75.85  ? 1152 SER   B CB  1 
ATOM   3046 O OG  . SER   B 1 115 ? -7.570  28.464  3.830   1.00 78.66  ? 1152 SER   B OG  1 
ATOM   3047 N N   . PRO   B 1 116 ? -11.497 30.569  3.748   1.00 71.47  ? 1153 PRO   B N   1 
ATOM   3048 C CA  . PRO   B 1 116 ? -12.874 30.960  4.062   1.00 69.42  ? 1153 PRO   B CA  1 
ATOM   3049 C C   . PRO   B 1 116 ? -13.499 30.171  5.211   1.00 67.62  ? 1153 PRO   B C   1 
ATOM   3050 O O   . PRO   B 1 116 ? -13.074 29.056  5.508   1.00 67.32  ? 1153 PRO   B O   1 
ATOM   3051 C CB  . PRO   B 1 116 ? -13.651 30.670  2.766   1.00 68.47  ? 1153 PRO   B CB  1 
ATOM   3052 C CG  . PRO   B 1 116 ? -12.592 30.635  1.686   1.00 70.38  ? 1153 PRO   B CG  1 
ATOM   3053 C CD  . PRO   B 1 116 ? -11.362 30.076  2.368   1.00 71.76  ? 1153 PRO   B CD  1 
ATOM   3054 N N   . LEU   B 1 117 ? -14.518 30.770  5.842   1.00 66.53  ? 1154 LEU   B N   1 
ATOM   3055 C CA  . LEU   B 1 117 ? -15.262 30.136  6.918   1.00 65.20  ? 1154 LEU   B CA  1 
ATOM   3056 C C   . LEU   B 1 117 ? -16.682 29.834  6.448   1.00 63.55  ? 1154 LEU   B C   1 
ATOM   3057 O O   . LEU   B 1 117 ? -17.205 30.513  5.567   1.00 63.44  ? 1154 LEU   B O   1 
ATOM   3058 C CB  . LEU   B 1 117 ? -15.291 31.070  8.133   1.00 66.29  ? 1154 LEU   B CB  1 
ATOM   3059 C CG  . LEU   B 1 117 ? -13.933 31.452  8.716   1.00 68.38  ? 1154 LEU   B CG  1 
ATOM   3060 C CD1 . LEU   B 1 117 ? -14.105 32.213  10.022  1.00 69.75  ? 1154 LEU   B CD1 1 
ATOM   3061 C CD2 . LEU   B 1 117 ? -13.058 30.225  8.927   1.00 68.47  ? 1154 LEU   B CD2 1 
ATOM   3062 N N   . VAL   B 1 118 ? -17.293 28.814  7.064   1.00 62.42  ? 1155 VAL   B N   1 
ATOM   3063 C CA  . VAL   B 1 118 ? -18.680 28.459  6.808   1.00 61.16  ? 1155 VAL   B CA  1 
ATOM   3064 C C   . VAL   B 1 118 ? -19.414 28.414  8.148   1.00 61.20  ? 1155 VAL   B C   1 
ATOM   3065 O O   . VAL   B 1 118 ? -18.953 27.771  9.089   1.00 61.06  ? 1155 VAL   B O   1 
ATOM   3066 C CB  . VAL   B 1 118 ? -18.799 27.131  6.030   1.00 59.96  ? 1155 VAL   B CB  1 
ATOM   3067 C CG1 . VAL   B 1 118 ? -18.072 25.980  6.712   1.00 59.67  ? 1155 VAL   B CG1 1 
ATOM   3068 C CG2 . VAL   B 1 118 ? -20.251 26.762  5.764   1.00 59.21  ? 1155 VAL   B CG2 1 
ATOM   3069 N N   . VAL   B 1 119 ? -20.551 29.120  8.218   1.00 61.65  ? 1156 VAL   B N   1 
ATOM   3070 C CA  . VAL   B 1 119 ? -21.309 29.273  9.451   1.00 62.33  ? 1156 VAL   B CA  1 
ATOM   3071 C C   . VAL   B 1 119 ? -22.609 28.482  9.326   1.00 61.62  ? 1156 VAL   B C   1 
ATOM   3072 O O   . VAL   B 1 119 ? -23.339 28.642  8.350   1.00 61.53  ? 1156 VAL   B O   1 
ATOM   3073 C CB  . VAL   B 1 119 ? -21.586 30.759  9.754   1.00 63.81  ? 1156 VAL   B CB  1 
ATOM   3074 C CG1 . VAL   B 1 119 ? -22.322 30.940  11.074  1.00 65.10  ? 1156 VAL   B CG1 1 
ATOM   3075 C CG2 . VAL   B 1 119 ? -20.308 31.587  9.735   1.00 64.75  ? 1156 VAL   B CG2 1 
ATOM   3076 N N   . LEU   B 1 120 ? -22.882 27.630  10.325  1.00 61.44  ? 1157 LEU   B N   1 
ATOM   3077 C CA  . LEU   B 1 120 ? -24.108 26.849  10.376  1.00 61.08  ? 1157 LEU   B CA  1 
ATOM   3078 C C   . LEU   B 1 120 ? -24.789 27.068  11.726  1.00 62.56  ? 1157 LEU   B C   1 
ATOM   3079 O O   . LEU   B 1 120 ? -24.128 27.424  12.700  1.00 63.39  ? 1157 LEU   B O   1 
ATOM   3080 C CB  . LEU   B 1 120 ? -23.784 25.365  10.172  1.00 59.58  ? 1157 LEU   B CB  1 
ATOM   3081 C CG  . LEU   B 1 120 ? -23.107 25.002  8.850   1.00 58.41  ? 1157 LEU   B CG  1 
ATOM   3082 C CD1 . LEU   B 1 120 ? -21.590 25.094  8.966   1.00 58.44  ? 1157 LEU   B CD1 1 
ATOM   3083 C CD2 . LEU   B 1 120 ? -23.521 23.608  8.400   1.00 57.49  ? 1157 LEU   B CD2 1 
ATOM   3084 N N   . PRO   B 1 121 ? -26.123 26.854  11.832  1.00 63.21  ? 1158 PRO   B N   1 
ATOM   3085 C CA  . PRO   B 1 121 ? -26.823 26.970  13.112  1.00 65.15  ? 1158 PRO   B CA  1 
ATOM   3086 C C   . PRO   B 1 121 ? -26.270 25.986  14.140  1.00 64.87  ? 1158 PRO   B C   1 
ATOM   3087 O O   . PRO   B 1 121 ? -26.055 24.820  13.819  1.00 63.43  ? 1158 PRO   B O   1 
ATOM   3088 C CB  . PRO   B 1 121 ? -28.287 26.630  12.787  1.00 65.86  ? 1158 PRO   B CB  1 
ATOM   3089 C CG  . PRO   B 1 121 ? -28.403 26.803  11.284  1.00 64.71  ? 1158 PRO   B CG  1 
ATOM   3090 C CD  . PRO   B 1 121 ? -27.028 26.493  10.730  1.00 62.60  ? 1158 PRO   B CD  1 
ATOM   3091 N N   . TYR   B 1 122 ? -26.053 26.462  15.373  1.00 66.70  ? 1159 TYR   B N   1 
ATOM   3092 C CA  . TYR   B 1 122 ? -25.459 25.638  16.413  1.00 67.02  ? 1159 TYR   B CA  1 
ATOM   3093 C C   . TYR   B 1 122 ? -26.429 24.526  16.802  1.00 67.10  ? 1159 TYR   B C   1 
ATOM   3094 O O   . TYR   B 1 122 ? -27.635 24.751  16.889  1.00 68.69  ? 1159 TYR   B O   1 
ATOM   3095 C CB  . TYR   B 1 122 ? -25.082 26.468  17.643  1.00 69.83  ? 1159 TYR   B CB  1 
ATOM   3096 C CG  . TYR   B 1 122 ? -24.549 25.647  18.791  1.00 70.91  ? 1159 TYR   B CG  1 
ATOM   3097 C CD1 . TYR   B 1 122 ? -23.408 24.874  18.644  1.00 69.51  ? 1159 TYR   B CD1 1 
ATOM   3098 C CD2 . TYR   B 1 122 ? -25.198 25.615  20.015  1.00 73.75  ? 1159 TYR   B CD2 1 
ATOM   3099 C CE1 . TYR   B 1 122 ? -22.916 24.104  19.685  1.00 70.61  ? 1159 TYR   B CE1 1 
ATOM   3100 C CE2 . TYR   B 1 122 ? -24.719 24.852  21.068  1.00 74.92  ? 1159 TYR   B CE2 1 
ATOM   3101 C CZ  . TYR   B 1 122 ? -23.575 24.092  20.903  1.00 73.28  ? 1159 TYR   B CZ  1 
ATOM   3102 O OH  . TYR   B 1 122 ? -23.089 23.333  21.940  1.00 74.66  ? 1159 TYR   B OH  1 
ATOM   3103 N N   . MET   B 1 123 ? -25.875 23.333  17.045  1.00 65.66  ? 1160 MET   B N   1 
ATOM   3104 C CA  . MET   B 1 123 ? -26.654 22.151  17.370  1.00 65.39  ? 1160 MET   B CA  1 
ATOM   3105 C C   . MET   B 1 123 ? -26.351 21.748  18.811  1.00 67.03  ? 1160 MET   B C   1 
ATOM   3106 O O   . MET   B 1 123 ? -25.233 21.346  19.124  1.00 66.18  ? 1160 MET   B O   1 
ATOM   3107 C CB  . MET   B 1 123 ? -26.296 21.014  16.409  1.00 62.75  ? 1160 MET   B CB  1 
ATOM   3108 C CG  . MET   B 1 123 ? -26.717 21.293  14.976  1.00 61.47  ? 1160 MET   B CG  1 
ATOM   3109 S SD  . MET   B 1 123 ? -28.499 21.094  14.707  1.00 62.87  ? 1160 MET   B SD  1 
ATOM   3110 C CE  . MET   B 1 123 ? -29.064 22.787  14.865  1.00 64.87  ? 1160 MET   B CE  1 
ATOM   3111 N N   . LYS   B 1 124 ? -27.367 21.864  19.676  1.00 69.69  ? 1161 LYS   B N   1 
ATOM   3112 C CA  . LYS   B 1 124 ? -27.187 21.820  21.120  1.00 72.55  ? 1161 LYS   B CA  1 
ATOM   3113 C C   . LYS   B 1 124 ? -26.604 20.475  21.550  1.00 71.91  ? 1161 LYS   B C   1 
ATOM   3114 O O   . LYS   B 1 124 ? -25.564 20.435  22.203  1.00 72.62  ? 1161 LYS   B O   1 
ATOM   3115 C CB  . LYS   B 1 124 ? -28.523 22.086  21.823  1.00 75.67  ? 1161 LYS   B CB  1 
ATOM   3116 C CG  . LYS   B 1 124 ? -28.443 22.266  23.334  1.00 79.18  ? 1161 LYS   B CG  1 
ATOM   3117 C CD  . LYS   B 1 124 ? -29.753 22.699  23.960  1.00 82.83  ? 1161 LYS   B CD  1 
ATOM   3118 C CE  . LYS   B 1 124 ? -29.645 22.983  25.443  1.00 86.84  ? 1161 LYS   B CE  1 
ATOM   3119 N NZ  . LYS   B 1 124 ? -29.286 21.769  26.213  1.00 87.06  ? 1161 LYS   B NZ  1 
ATOM   3120 N N   . HIS   B 1 125 ? -27.280 19.383  21.172  1.00 70.92  ? 1162 HIS   B N   1 
ATOM   3121 C CA  . HIS   B 1 125 ? -26.944 18.055  21.662  1.00 70.58  ? 1162 HIS   B CA  1 
ATOM   3122 C C   . HIS   B 1 125 ? -25.953 17.349  20.735  1.00 67.58  ? 1162 HIS   B C   1 
ATOM   3123 O O   . HIS   B 1 125 ? -25.625 16.185  20.960  1.00 67.20  ? 1162 HIS   B O   1 
ATOM   3124 C CB  . HIS   B 1 125 ? -28.225 17.237  21.865  1.00 71.70  ? 1162 HIS   B CB  1 
ATOM   3125 C CG  . HIS   B 1 125 ? -29.080 17.714  23.000  1.00 75.48  ? 1162 HIS   B CG  1 
ATOM   3126 N ND1 . HIS   B 1 125 ? -28.642 17.790  24.300  1.00 77.94  ? 1162 HIS   B ND1 1 
ATOM   3127 C CD2 . HIS   B 1 125 ? -30.370 18.155  22.991  1.00 77.56  ? 1162 HIS   B CD2 1 
ATOM   3128 C CE1 . HIS   B 1 125 ? -29.626 18.254  25.067  1.00 81.38  ? 1162 HIS   B CE1 1 
ATOM   3129 N NE2 . HIS   B 1 125 ? -30.708 18.489  24.274  1.00 81.23  ? 1162 HIS   B NE2 1 
ATOM   3130 N N   . GLY   B 1 126 ? -25.478 18.052  19.699  1.00 65.82  ? 1163 GLY   B N   1 
ATOM   3131 C CA  . GLY   B 1 126 ? -24.345 17.594  18.911  1.00 63.49  ? 1163 GLY   B CA  1 
ATOM   3132 C C   . GLY   B 1 126 ? -24.721 16.490  17.926  1.00 61.36  ? 1163 GLY   B C   1 
ATOM   3133 O O   . GLY   B 1 126 ? -25.875 16.388  17.514  1.00 61.15  ? 1163 GLY   B O   1 
ATOM   3134 N N   . ASP   B 1 127 ? -23.728 15.665  17.568  1.00 59.96  ? 1164 ASP   B N   1 
ATOM   3135 C CA  . ASP   B 1 127 ? -23.879 14.660  16.527  1.00 58.17  ? 1164 ASP   B CA  1 
ATOM   3136 C C   . ASP   B 1 127 ? -24.677 13.473  17.062  1.00 58.47  ? 1164 ASP   B C   1 
ATOM   3137 O O   . ASP   B 1 127 ? -24.792 13.284  18.271  1.00 59.85  ? 1164 ASP   B O   1 
ATOM   3138 C CB  . ASP   B 1 127 ? -22.520 14.226  15.967  1.00 57.22  ? 1164 ASP   B CB  1 
ATOM   3139 C CG  . ASP   B 1 127 ? -21.646 13.468  16.952  1.00 58.08  ? 1164 ASP   B CG  1 
ATOM   3140 O OD1 . ASP   B 1 127 ? -20.661 14.060  17.436  1.00 58.93  ? 1164 ASP   B OD1 1 
ATOM   3141 O OD2 . ASP   B 1 127 ? -21.942 12.284  17.208  1.00 58.13  ? 1164 ASP   B OD2 1 
ATOM   3142 N N   . LEU   B 1 128 ? -25.199 12.669  16.130  1.00 57.33  ? 1165 LEU   B N   1 
ATOM   3143 C CA  . LEU   B 1 128 ? -26.158 11.622  16.442  1.00 58.03  ? 1165 LEU   B CA  1 
ATOM   3144 C C   . LEU   B 1 128 ? -25.447 10.394  17.008  1.00 57.94  ? 1165 LEU   B C   1 
ATOM   3145 O O   . LEU   B 1 128 ? -26.008 9.702   17.856  1.00 59.29  ? 1165 LEU   B O   1 
ATOM   3146 C CB  . LEU   B 1 128 ? -26.940 11.281  15.168  1.00 57.35  ? 1165 LEU   B CB  1 
ATOM   3147 C CG  . LEU   B 1 128 ? -28.069 10.262  15.319  1.00 58.31  ? 1165 LEU   B CG  1 
ATOM   3148 C CD1 . LEU   B 1 128 ? -29.190 10.814  16.187  1.00 60.24  ? 1165 LEU   B CD1 1 
ATOM   3149 C CD2 . LEU   B 1 128 ? -28.602 9.849   13.953  1.00 57.79  ? 1165 LEU   B CD2 1 
ATOM   3150 N N   . ARG   B 1 129 ? -24.221 10.127  16.541  1.00 56.71  ? 1166 ARG   B N   1 
ATOM   3151 C CA  . ARG   B 1 129 ? -23.514 8.914   16.921  1.00 56.77  ? 1166 ARG   B CA  1 
ATOM   3152 C C   . ARG   B 1 129 ? -23.107 8.982   18.392  1.00 58.34  ? 1166 ARG   B C   1 
ATOM   3153 O O   . ARG   B 1 129 ? -23.366 8.049   19.147  1.00 59.31  ? 1166 ARG   B O   1 
ATOM   3154 C CB  . ARG   B 1 129 ? -22.276 8.686   16.049  1.00 55.85  ? 1166 ARG   B CB  1 
ATOM   3155 C CG  . ARG   B 1 129 ? -21.759 7.255   16.111  1.00 56.19  ? 1166 ARG   B CG  1 
ATOM   3156 C CD  . ARG   B 1 129 ? -20.281 7.112   15.809  1.00 56.38  ? 1166 ARG   B CD  1 
ATOM   3157 N NE  . ARG   B 1 129 ? -19.834 5.746   16.046  1.00 57.01  ? 1166 ARG   B NE  1 
ATOM   3158 C CZ  . ARG   B 1 129 ? -18.564 5.358   16.080  1.00 57.96  ? 1166 ARG   B CZ  1 
ATOM   3159 N NH1 . ARG   B 1 129 ? -17.596 6.238   15.896  1.00 58.46  ? 1166 ARG   B NH1 1 
ATOM   3160 N NH2 . ARG   B 1 129 ? -18.268 4.090   16.304  1.00 58.72  ? 1166 ARG   B NH2 1 
ATOM   3161 N N   . ASN   B 1 130 ? -22.466 10.088  18.787  1.00 59.03  ? 1167 ASN   B N   1 
ATOM   3162 C CA  . ASN   B 1 130 ? -21.984 10.252  20.150  1.00 61.03  ? 1167 ASN   B CA  1 
ATOM   3163 C C   . ASN   B 1 130 ? -23.160 10.347  21.122  1.00 62.90  ? 1167 ASN   B C   1 
ATOM   3164 O O   . ASN   B 1 130 ? -23.020 9.987   22.288  1.00 64.94  ? 1167 ASN   B O   1 
ATOM   3165 C CB  . ASN   B 1 130 ? -21.060 11.465  20.289  1.00 61.49  ? 1167 ASN   B CB  1 
ATOM   3166 C CG  . ASN   B 1 130 ? -19.696 11.242  19.669  1.00 60.85  ? 1167 ASN   B CG  1 
ATOM   3167 O OD1 . ASN   B 1 130 ? -18.984 10.313  20.043  1.00 61.44  ? 1167 ASN   B OD1 1 
ATOM   3168 N ND2 . ASN   B 1 130 ? -19.323 12.088  18.723  1.00 59.92  ? 1167 ASN   B ND2 1 
ATOM   3169 N N   . PHE   B 1 131 ? -24.309 10.832  20.635  1.00 62.83  ? 1168 PHE   B N   1 
ATOM   3170 C CA  . PHE   B 1 131 ? -25.506 10.968  21.450  1.00 65.01  ? 1168 PHE   B CA  1 
ATOM   3171 C C   . PHE   B 1 131 ? -25.971 9.593   21.932  1.00 65.68  ? 1168 PHE   B C   1 
ATOM   3172 O O   . PHE   B 1 131 ? -26.157 9.387   23.131  1.00 67.75  ? 1168 PHE   B O   1 
ATOM   3173 C CB  . PHE   B 1 131 ? -26.600 11.694  20.660  1.00 64.87  ? 1168 PHE   B CB  1 
ATOM   3174 C CG  . PHE   B 1 131 ? -27.843 12.033  21.444  1.00 67.43  ? 1168 PHE   B CG  1 
ATOM   3175 C CD1 . PHE   B 1 131 ? -28.068 13.327  21.889  1.00 69.08  ? 1168 PHE   B CD1 1 
ATOM   3176 C CD2 . PHE   B 1 131 ? -28.805 11.069  21.711  1.00 68.49  ? 1168 PHE   B CD2 1 
ATOM   3177 C CE1 . PHE   B 1 131 ? -29.213 13.643  22.604  1.00 71.98  ? 1168 PHE   B CE1 1 
ATOM   3178 C CE2 . PHE   B 1 131 ? -29.950 11.387  22.425  1.00 71.33  ? 1168 PHE   B CE2 1 
ATOM   3179 C CZ  . PHE   B 1 131 ? -30.152 12.674  22.870  1.00 73.16  ? 1168 PHE   B CZ  1 
ATOM   3180 N N   . ILE   B 1 132 ? -26.158 8.665   20.985  1.00 64.15  ? 1169 ILE   B N   1 
ATOM   3181 C CA  . ILE   B 1 132 ? -26.674 7.336   21.283  1.00 64.85  ? 1169 ILE   B CA  1 
ATOM   3182 C C   . ILE   B 1 132 ? -25.606 6.503   21.993  1.00 65.52  ? 1169 ILE   B C   1 
ATOM   3183 O O   . ILE   B 1 132 ? -25.940 5.632   22.794  1.00 66.94  ? 1169 ILE   B O   1 
ATOM   3184 C CB  . ILE   B 1 132 ? -27.204 6.642   20.008  1.00 63.11  ? 1169 ILE   B CB  1 
ATOM   3185 C CG1 . ILE   B 1 132 ? -26.107 6.405   18.964  1.00 60.86  ? 1169 ILE   B CG1 1 
ATOM   3186 C CG2 . ILE   B 1 132 ? -28.375 7.418   19.424  1.00 63.44  ? 1169 ILE   B CG2 1 
ATOM   3187 C CD1 . ILE   B 1 132 ? -26.604 5.781   17.679  1.00 59.80  ? 1169 ILE   B CD1 1 
ATOM   3188 N N   . ARG   B 1 133 ? -24.328 6.775   21.692  1.00 64.82  ? 1170 ARG   B N   1 
ATOM   3189 C CA  . ARG   B 1 133 ? -23.215 6.073   22.315  1.00 65.68  ? 1170 ARG   B CA  1 
ATOM   3190 C C   . ARG   B 1 133 ? -23.059 6.497   23.774  1.00 68.63  ? 1170 ARG   B C   1 
ATOM   3191 O O   . ARG   B 1 133 ? -22.602 5.705   24.595  1.00 69.80  ? 1170 ARG   B O   1 
ATOM   3192 C CB  . ARG   B 1 133 ? -21.910 6.338   21.556  1.00 64.34  ? 1170 ARG   B CB  1 
ATOM   3193 C CG  . ARG   B 1 133 ? -21.779 5.571   20.249  1.00 62.58  ? 1170 ARG   B CG  1 
ATOM   3194 C CD  . ARG   B 1 133 ? -20.494 5.905   19.514  1.00 61.97  ? 1170 ARG   B CD  1 
ATOM   3195 N NE  . ARG   B 1 133 ? -19.299 5.531   20.261  1.00 63.46  ? 1170 ARG   B NE  1 
ATOM   3196 C CZ  . ARG   B 1 133 ? -18.921 4.282   20.516  1.00 64.27  ? 1170 ARG   B CZ  1 
ATOM   3197 N NH1 . ARG   B 1 133 ? -19.594 3.265   20.008  1.00 63.72  ? 1170 ARG   B NH1 1 
ATOM   3198 N NH2 . ARG   B 1 133 ? -17.862 4.054   21.273  1.00 66.08  ? 1170 ARG   B NH2 1 
ATOM   3199 N N   . ASN   B 1 134 ? -23.428 7.749   24.080  1.00 70.41  ? 1171 ASN   B N   1 
ATOM   3200 C CA  . ASN   B 1 134 ? -23.246 8.316   25.409  1.00 73.88  ? 1171 ASN   B CA  1 
ATOM   3201 C C   . ASN   B 1 134 ? -24.001 7.473   26.435  1.00 76.64  ? 1171 ASN   B C   1 
ATOM   3202 O O   . ASN   B 1 134 ? -25.106 7.006   26.168  1.00 76.43  ? 1171 ASN   B O   1 
ATOM   3203 C CB  . ASN   B 1 134 ? -23.696 9.779   25.464  1.00 74.63  ? 1171 ASN   B CB  1 
ATOM   3204 C CG  . ASN   B 1 134 ? -23.319 10.484  26.751  1.00 77.83  ? 1171 ASN   B CG  1 
ATOM   3205 O OD1 . ASN   B 1 134 ? -22.639 9.921   27.606  1.00 79.52  ? 1171 ASN   B OD1 1 
ATOM   3206 N ND2 . ASN   B 1 134 ? -23.749 11.727  26.894  1.00 78.97  ? 1171 ASN   B ND2 1 
ATOM   3207 N N   . GLU   B 1 135 ? -23.384 7.297   27.610  1.00 79.87  ? 1172 GLU   B N   1 
ATOM   3208 C CA  . GLU   B 1 135 ? -23.932 6.466   28.671  1.00 82.96  ? 1172 GLU   B CA  1 
ATOM   3209 C C   . GLU   B 1 135 ? -24.999 7.243   29.439  1.00 86.14  ? 1172 GLU   B C   1 
ATOM   3210 O O   . GLU   B 1 135 ? -26.019 6.673   29.824  1.00 87.69  ? 1172 GLU   B O   1 
ATOM   3211 C CB  . GLU   B 1 135 ? -22.811 6.001   29.603  1.00 85.10  ? 1172 GLU   B CB  1 
ATOM   3212 C CG  . GLU   B 1 135 ? -23.263 5.005   30.658  1.00 87.90  ? 1172 GLU   B CG  1 
ATOM   3213 C CD  . GLU   B 1 135 ? -22.163 4.503   31.579  1.00 90.38  ? 1172 GLU   B CD  1 
ATOM   3214 O OE1 . GLU   B 1 135 ? -22.474 3.705   32.486  1.00 92.94  ? 1172 GLU   B OE1 1 
ATOM   3215 O OE2 . GLU   B 1 135 ? -20.999 4.910   31.390  1.00 90.17  ? 1172 GLU   B OE2 1 
ATOM   3216 N N   . THR   B 1 136 ? -24.748 8.541   29.665  1.00 87.47  ? 1173 THR   B N   1 
ATOM   3217 C CA  . THR   B 1 136 ? -25.661 9.396   30.409  1.00 90.47  ? 1173 THR   B CA  1 
ATOM   3218 C C   . THR   B 1 136 ? -26.996 9.490   29.673  1.00 89.40  ? 1173 THR   B C   1 
ATOM   3219 O O   . THR   B 1 136 ? -28.052 9.355   30.287  1.00 91.96  ? 1173 THR   B O   1 
ATOM   3220 C CB  . THR   B 1 136 ? -25.050 10.782  30.658  1.00 91.71  ? 1173 THR   B CB  1 
ATOM   3221 O OG1 . THR   B 1 136 ? -24.784 11.393  29.395  1.00 88.43  ? 1173 THR   B OG1 1 
ATOM   3222 C CG2 . THR   B 1 136 ? -23.779 10.727  31.476  1.00 93.50  ? 1173 THR   B CG2 1 
ATOM   3223 N N   . HIS   B 1 137 ? -26.933 9.731   28.356  1.00 85.86  ? 1174 HIS   B N   1 
ATOM   3224 C CA  . HIS   B 1 137 ? -28.102 9.625   27.497  1.00 84.54  ? 1174 HIS   B CA  1 
ATOM   3225 C C   . HIS   B 1 137 ? -28.502 8.157   27.374  1.00 83.64  ? 1174 HIS   B C   1 
ATOM   3226 O O   . HIS   B 1 137 ? -27.646 7.294   27.191  1.00 82.02  ? 1174 HIS   B O   1 
ATOM   3227 C CB  . HIS   B 1 137 ? -27.826 10.237  26.117  1.00 81.43  ? 1174 HIS   B CB  1 
ATOM   3228 C CG  . HIS   B 1 137 ? -27.765 11.734  26.089  1.00 82.22  ? 1174 HIS   B CG  1 
ATOM   3229 N ND1 . HIS   B 1 137 ? -26.688 12.446  25.620  1.00 80.69  ? 1174 HIS   B ND1 1 
ATOM   3230 C CD2 . HIS   B 1 137 ? -28.703 12.644  26.478  1.00 84.69  ? 1174 HIS   B CD2 1 
ATOM   3231 C CE1 . HIS   B 1 137 ? -26.947 13.748  25.723  1.00 81.97  ? 1174 HIS   B CE1 1 
ATOM   3232 N NE2 . HIS   B 1 137 ? -28.194 13.894  26.254  1.00 84.51  ? 1174 HIS   B NE2 1 
ATOM   3233 N N   . ASN   B 1 138 ? -29.807 7.886   27.484  1.00 84.81  ? 1175 ASN   B N   1 
ATOM   3234 C CA  . ASN   B 1 138 ? -30.320 6.530   27.388  1.00 84.38  ? 1175 ASN   B CA  1 
ATOM   3235 C C   . ASN   B 1 138 ? -31.693 6.571   26.720  1.00 84.59  ? 1175 ASN   B C   1 
ATOM   3236 O O   . ASN   B 1 138 ? -32.713 6.353   27.371  1.00 87.57  ? 1175 ASN   B O   1 
ATOM   3237 C CB  . ASN   B 1 138 ? -30.348 5.852   28.762  1.00 87.45  ? 1175 ASN   B CB  1 
ATOM   3238 C CG  . ASN   B 1 138 ? -30.570 4.355   28.693  1.00 87.16  ? 1175 ASN   B CG  1 
ATOM   3239 O OD1 . ASN   B 1 138 ? -30.675 3.780   27.612  1.00 84.51  ? 1175 ASN   B OD1 1 
ATOM   3240 N ND2 . ASN   B 1 138 ? -30.635 3.711   29.847  1.00 90.10  ? 1175 ASN   B ND2 1 
ATOM   3241 N N   . PRO   B 1 139 ? -31.759 6.859   25.398  1.00 81.67  ? 1176 PRO   B N   1 
ATOM   3242 C CA  . PRO   B 1 139 ? -33.029 6.880   24.673  1.00 82.19  ? 1176 PRO   B CA  1 
ATOM   3243 C C   . PRO   B 1 139 ? -33.529 5.473   24.358  1.00 82.08  ? 1176 PRO   B C   1 
ATOM   3244 O O   . PRO   B 1 139 ? -32.734 4.582   24.064  1.00 80.10  ? 1176 PRO   B O   1 
ATOM   3245 C CB  . PRO   B 1 139 ? -32.678 7.645   23.389  1.00 79.23  ? 1176 PRO   B CB  1 
ATOM   3246 C CG  . PRO   B 1 139 ? -31.224 7.300   23.147  1.00 76.43  ? 1176 PRO   B CG  1 
ATOM   3247 C CD  . PRO   B 1 139 ? -30.614 7.180   24.529  1.00 78.23  ? 1176 PRO   B CD  1 
ATOM   3248 N N   . THR   B 1 140 ? -34.854 5.292   24.417  1.00 84.42  ? 1177 THR   B N   1 
ATOM   3249 C CA  . THR   B 1 140 ? -35.479 4.008   24.141  1.00 84.72  ? 1177 THR   B CA  1 
ATOM   3250 C C   . THR   B 1 140 ? -35.431 3.729   22.640  1.00 81.57  ? 1177 THR   B C   1 
ATOM   3251 O O   . THR   B 1 140 ? -35.106 4.612   21.850  1.00 79.51  ? 1177 THR   B O   1 
ATOM   3252 C CB  . THR   B 1 140 ? -36.918 3.974   24.674  1.00 89.04  ? 1177 THR   B CB  1 
ATOM   3253 O OG1 . THR   B 1 140 ? -37.654 5.021   24.040  1.00 89.79  ? 1177 THR   B OG1 1 
ATOM   3254 C CG2 . THR   B 1 140 ? -36.992 4.136   26.177  1.00 92.36  ? 1177 THR   B CG2 1 
ATOM   3255 N N   . VAL   B 1 141 ? -35.777 2.491   22.265  1.00 81.34  ? 1178 VAL   B N   1 
ATOM   3256 C CA  . VAL   B 1 141 ? -35.740 2.052   20.878  1.00 79.05  ? 1178 VAL   B CA  1 
ATOM   3257 C C   . VAL   B 1 141 ? -36.762 2.848   20.065  1.00 79.86  ? 1178 VAL   B C   1 
ATOM   3258 O O   . VAL   B 1 141 ? -36.573 3.056   18.869  1.00 77.58  ? 1178 VAL   B O   1 
ATOM   3259 C CB  . VAL   B 1 141 ? -35.986 0.533   20.763  1.00 79.76  ? 1178 VAL   B CB  1 
ATOM   3260 C CG1 . VAL   B 1 141 ? -36.010 0.069   19.312  1.00 78.15  ? 1178 VAL   B CG1 1 
ATOM   3261 C CG2 . VAL   B 1 141 ? -34.966 -0.267  21.563  1.00 78.94  ? 1178 VAL   B CG2 1 
ATOM   3262 N N   . LYS   B 1 142 ? -37.843 3.282   20.727  1.00 83.30  ? 1179 LYS   B N   1 
ATOM   3263 C CA  . LYS   B 1 142 ? -38.856 4.128   20.114  1.00 85.06  ? 1179 LYS   B CA  1 
ATOM   3264 C C   . LYS   B 1 142 ? -38.202 5.368   19.506  1.00 82.63  ? 1179 LYS   B C   1 
ATOM   3265 O O   . LYS   B 1 142 ? -38.521 5.748   18.381  1.00 82.06  ? 1179 LYS   B O   1 
ATOM   3266 C CB  . LYS   B 1 142 ? -39.904 4.531   21.158  1.00 89.38  ? 1179 LYS   B CB  1 
ATOM   3267 C CG  . LYS   B 1 142 ? -41.168 5.180   20.608  1.00 92.28  ? 1179 LYS   B CG  1 
ATOM   3268 C CD  . LYS   B 1 142 ? -42.086 4.210   19.895  1.00 94.13  ? 1179 LYS   B CD  1 
ATOM   3269 C CE  . LYS   B 1 142 ? -43.406 4.832   19.491  1.00 97.90  ? 1179 LYS   B CE  1 
ATOM   3270 N NZ  . LYS   B 1 142 ? -44.349 3.820   18.961  1.00 100.50 ? 1179 LYS   B NZ  1 
ATOM   3271 N N   . ASP   B 1 143 ? -37.287 5.986   20.265  1.00 81.49  ? 1180 ASP   B N   1 
ATOM   3272 C CA  . ASP   B 1 143 ? -36.606 7.199   19.841  1.00 79.43  ? 1180 ASP   B CA  1 
ATOM   3273 C C   . ASP   B 1 143 ? -35.642 6.890   18.697  1.00 75.67  ? 1180 ASP   B C   1 
ATOM   3274 O O   . ASP   B 1 143 ? -35.554 7.657   17.740  1.00 74.29  ? 1180 ASP   B O   1 
ATOM   3275 C CB  . ASP   B 1 143 ? -35.852 7.852   21.004  1.00 79.70  ? 1180 ASP   B CB  1 
ATOM   3276 C CG  . ASP   B 1 143 ? -36.730 8.255   22.177  1.00 83.79  ? 1180 ASP   B CG  1 
ATOM   3277 O OD1 . ASP   B 1 143 ? -37.948 7.996   22.117  1.00 86.68  ? 1180 ASP   B OD1 1 
ATOM   3278 O OD2 . ASP   B 1 143 ? -36.187 8.827   23.143  1.00 84.54  ? 1180 ASP   B OD2 1 
ATOM   3279 N N   . LEU   B 1 144 ? -34.927 5.762   18.810  1.00 74.25  ? 1181 LEU   B N   1 
ATOM   3280 C CA  . LEU   B 1 144 ? -33.893 5.385   17.857  1.00 71.17  ? 1181 LEU   B CA  1 
ATOM   3281 C C   . LEU   B 1 144 ? -34.492 5.190   16.464  1.00 71.05  ? 1181 LEU   B C   1 
ATOM   3282 O O   . LEU   B 1 144 ? -33.849 5.508   15.467  1.00 69.12  ? 1181 LEU   B O   1 
ATOM   3283 C CB  . LEU   B 1 144 ? -33.205 4.105   18.345  1.00 70.48  ? 1181 LEU   B CB  1 
ATOM   3284 C CG  . LEU   B 1 144 ? -32.424 4.227   19.654  1.00 70.68  ? 1181 LEU   B CG  1 
ATOM   3285 C CD1 . LEU   B 1 144 ? -31.782 2.898   20.031  1.00 70.32  ? 1181 LEU   B CD1 1 
ATOM   3286 C CD2 . LEU   B 1 144 ? -31.367 5.319   19.564  1.00 68.90  ? 1181 LEU   B CD2 1 
ATOM   3287 N N   . ILE   B 1 145 ? -35.720 4.658   16.408  1.00 73.67  ? 1182 ILE   B N   1 
ATOM   3288 C CA  . ILE   B 1 145 ? -36.434 4.487   15.151  1.00 74.38  ? 1182 ILE   B CA  1 
ATOM   3289 C C   . ILE   B 1 145 ? -36.885 5.856   14.643  1.00 74.78  ? 1182 ILE   B C   1 
ATOM   3290 O O   . ILE   B 1 145 ? -36.870 6.106   13.439  1.00 73.92  ? 1182 ILE   B O   1 
ATOM   3291 C CB  . ILE   B 1 145 ? -37.617 3.511   15.322  1.00 77.46  ? 1182 ILE   B CB  1 
ATOM   3292 C CG1 . ILE   B 1 145 ? -37.140 2.113   15.729  1.00 77.06  ? 1182 ILE   B CG1 1 
ATOM   3293 C CG2 . ILE   B 1 145 ? -38.469 3.467   14.060  1.00 78.82  ? 1182 ILE   B CG2 1 
ATOM   3294 C CD1 . ILE   B 1 145 ? -38.246 1.187   16.180  1.00 80.43  ? 1182 ILE   B CD1 1 
ATOM   3295 N N   . GLY   B 1 146 ? -37.287 6.731   15.574  1.00 76.23  ? 1183 GLY   B N   1 
ATOM   3296 C CA  . GLY   B 1 146 ? -37.714 8.083   15.251  1.00 76.85  ? 1183 GLY   B CA  1 
ATOM   3297 C C   . GLY   B 1 146 ? -36.605 8.910   14.603  1.00 73.60  ? 1183 GLY   B C   1 
ATOM   3298 O O   . GLY   B 1 146 ? -36.871 9.700   13.700  1.00 73.65  ? 1183 GLY   B O   1 
ATOM   3299 N N   . PHE   B 1 147 ? -35.366 8.722   15.078  1.00 71.12  ? 1184 PHE   B N   1 
ATOM   3300 C CA  . PHE   B 1 147 ? -34.206 9.414   14.536  1.00 68.18  ? 1184 PHE   B CA  1 
ATOM   3301 C C   . PHE   B 1 147 ? -33.996 9.026   13.074  1.00 66.59  ? 1184 PHE   B C   1 
ATOM   3302 O O   . PHE   B 1 147 ? -33.650 9.872   12.253  1.00 65.32  ? 1184 PHE   B O   1 
ATOM   3303 C CB  . PHE   B 1 147 ? -32.951 9.093   15.354  1.00 66.57  ? 1184 PHE   B CB  1 
ATOM   3304 C CG  . PHE   B 1 147 ? -32.946 9.576   16.784  1.00 68.01  ? 1184 PHE   B CG  1 
ATOM   3305 C CD1 . PHE   B 1 147 ? -33.875 10.499  17.247  1.00 70.46  ? 1184 PHE   B CD1 1 
ATOM   3306 C CD2 . PHE   B 1 147 ? -32.002 9.094   17.679  1.00 67.42  ? 1184 PHE   B CD2 1 
ATOM   3307 C CE1 . PHE   B 1 147 ? -33.853 10.931  18.565  1.00 72.31  ? 1184 PHE   B CE1 1 
ATOM   3308 C CE2 . PHE   B 1 147 ? -31.982 9.526   18.996  1.00 69.20  ? 1184 PHE   B CE2 1 
ATOM   3309 C CZ  . PHE   B 1 147 ? -32.907 10.443  19.437  1.00 71.67  ? 1184 PHE   B CZ  1 
ATOM   3310 N N   . GLY   B 1 148 ? -34.200 7.739   12.766  1.00 66.80  ? 1185 GLY   B N   1 
ATOM   3311 C CA  . GLY   B 1 148 ? -34.042 7.224   11.416  1.00 66.17  ? 1185 GLY   B CA  1 
ATOM   3312 C C   . GLY   B 1 148 ? -35.031 7.849   10.433  1.00 67.78  ? 1185 GLY   B C   1 
ATOM   3313 O O   . GLY   B 1 148 ? -34.683 8.090   9.278   1.00 67.07  ? 1185 GLY   B O   1 
ATOM   3314 N N   . LEU   B 1 149 ? -36.259 8.101   10.904  1.00 70.28  ? 1186 LEU   B N   1 
ATOM   3315 C CA  . LEU   B 1 149 ? -37.311 8.678   10.080  1.00 72.35  ? 1186 LEU   B CA  1 
ATOM   3316 C C   . LEU   B 1 149 ? -36.926 10.094  9.655   1.00 71.17  ? 1186 LEU   B C   1 
ATOM   3317 O O   . LEU   B 1 149 ? -37.098 10.463  8.495   1.00 71.47  ? 1186 LEU   B O   1 
ATOM   3318 C CB  . LEU   B 1 149 ? -38.621 8.684   10.875  1.00 75.65  ? 1186 LEU   B CB  1 
ATOM   3319 C CG  . LEU   B 1 149 ? -39.852 9.186   10.121  1.00 78.76  ? 1186 LEU   B CG  1 
ATOM   3320 C CD1 . LEU   B 1 149 ? -40.308 8.170   9.084   1.00 80.11  ? 1186 LEU   B CD1 1 
ATOM   3321 C CD2 . LEU   B 1 149 ? -40.984 9.508   11.085  1.00 82.20  ? 1186 LEU   B CD2 1 
ATOM   3322 N N   . GLN   B 1 150 ? -36.410 10.877  10.611  1.00 69.98  ? 1187 GLN   B N   1 
ATOM   3323 C CA  . GLN   B 1 150 ? -36.063 12.270  10.381  1.00 69.13  ? 1187 GLN   B CA  1 
ATOM   3324 C C   . GLN   B 1 150 ? -34.958 12.376  9.330   1.00 66.59  ? 1187 GLN   B C   1 
ATOM   3325 O O   . GLN   B 1 150 ? -34.965 13.301  8.519   1.00 66.72  ? 1187 GLN   B O   1 
ATOM   3326 C CB  . GLN   B 1 150 ? -35.643 12.927  11.697  1.00 68.76  ? 1187 GLN   B CB  1 
ATOM   3327 C CG  . GLN   B 1 150 ? -36.789 13.087  12.686  1.00 71.91  ? 1187 GLN   B CG  1 
ATOM   3328 C CD  . GLN   B 1 150 ? -36.348 13.730  13.978  1.00 72.03  ? 1187 GLN   B CD  1 
ATOM   3329 O OE1 . GLN   B 1 150 ? -35.837 14.848  13.993  1.00 71.36  ? 1187 GLN   B OE1 1 
ATOM   3330 N NE2 . GLN   B 1 150 ? -36.542 13.024  15.080  1.00 73.29  ? 1187 GLN   B NE2 1 
ATOM   3331 N N   . VAL   B 1 151 ? -34.017 11.425  9.351   1.00 64.63  ? 1188 VAL   B N   1 
ATOM   3332 C CA  . VAL   B 1 151 ? -32.933 11.384  8.381   1.00 62.64  ? 1188 VAL   B CA  1 
ATOM   3333 C C   . VAL   B 1 151 ? -33.510 11.114  6.992   1.00 63.95  ? 1188 VAL   B C   1 
ATOM   3334 O O   . VAL   B 1 151 ? -33.083 11.726  6.016   1.00 63.26  ? 1188 VAL   B O   1 
ATOM   3335 C CB  . VAL   B 1 151 ? -31.875 10.329  8.760   1.00 60.91  ? 1188 VAL   B CB  1 
ATOM   3336 C CG1 . VAL   B 1 151 ? -30.847 10.134  7.654   1.00 59.60  ? 1188 VAL   B CG1 1 
ATOM   3337 C CG2 . VAL   B 1 151 ? -31.185 10.662  10.075  1.00 59.95  ? 1188 VAL   B CG2 1 
ATOM   3338 N N   . ALA   B 1 152 ? -34.475 10.187  6.920   1.00 66.06  ? 1189 ALA   B N   1 
ATOM   3339 C CA  . ALA   B 1 152 ? -35.092 9.794   5.663   1.00 68.01  ? 1189 ALA   B CA  1 
ATOM   3340 C C   . ALA   B 1 152 ? -35.869 10.966  5.066   1.00 69.79  ? 1189 ALA   B C   1 
ATOM   3341 O O   . ALA   B 1 152 ? -35.763 11.235  3.872   1.00 70.14  ? 1189 ALA   B O   1 
ATOM   3342 C CB  . ALA   B 1 152 ? -35.985 8.597   5.879   1.00 70.08  ? 1189 ALA   B CB  1 
ATOM   3343 N N   . LYS   B 1 153 ? -36.656 11.645  5.911   1.00 71.24  ? 1190 LYS   B N   1 
ATOM   3344 C CA  . LYS   B 1 153 ? -37.400 12.827  5.505   1.00 73.25  ? 1190 LYS   B CA  1 
ATOM   3345 C C   . LYS   B 1 153 ? -36.427 13.931  5.093   1.00 71.11  ? 1190 LYS   B C   1 
ATOM   3346 O O   . LYS   B 1 153 ? -36.687 14.663  4.140   1.00 72.10  ? 1190 LYS   B O   1 
ATOM   3347 C CB  . LYS   B 1 153 ? -38.316 13.303  6.638   1.00 75.36  ? 1190 LYS   B CB  1 
ATOM   3348 C CG  . LYS   B 1 153 ? -39.495 12.389  6.944   1.00 78.49  ? 1190 LYS   B CG  1 
ATOM   3349 C CD  . LYS   B 1 153 ? -40.401 12.916  8.036   1.00 81.01  ? 1190 LYS   B CD  1 
ATOM   3350 C CE  . LYS   B 1 153 ? -41.625 12.051  8.255   1.00 84.77  ? 1190 LYS   B CE  1 
ATOM   3351 N NZ  . LYS   B 1 153 ? -42.507 12.607  9.308   1.00 87.80  ? 1190 LYS   B NZ  1 
ATOM   3352 N N   . GLY   B 1 154 ? -35.315 14.042  5.829   1.00 68.46  ? 1191 GLY   B N   1 
ATOM   3353 C CA  . GLY   B 1 154 ? -34.247 14.970  5.494   1.00 66.43  ? 1191 GLY   B CA  1 
ATOM   3354 C C   . GLY   B 1 154 ? -33.600 14.637  4.152   1.00 65.69  ? 1191 GLY   B C   1 
ATOM   3355 O O   . GLY   B 1 154 ? -33.357 15.528  3.341   1.00 65.61  ? 1191 GLY   B O   1 
ATOM   3356 N N   . MET   B 1 155 ? -33.333 13.343  3.934   1.00 65.20  ? 1192 MET   B N   1 
ATOM   3357 C CA  . MET   B 1 155 ? -32.686 12.871  2.720   1.00 64.98  ? 1192 MET   B CA  1 
ATOM   3358 C C   . MET   B 1 155 ? -33.657 12.945  1.542   1.00 67.54  ? 1192 MET   B C   1 
ATOM   3359 O O   . MET   B 1 155 ? -33.226 13.098  0.401   1.00 67.88  ? 1192 MET   B O   1 
ATOM   3360 C CB  . MET   B 1 155 ? -32.198 11.427  2.888   1.00 64.43  ? 1192 MET   B CB  1 
ATOM   3361 C CG  . MET   B 1 155 ? -30.854 11.309  3.595   1.00 62.02  ? 1192 MET   B CG  1 
ATOM   3362 S SD  . MET   B 1 155 ? -29.479 12.162  2.766   1.00 60.93  ? 1192 MET   B SD  1 
ATOM   3363 C CE  . MET   B 1 155 ? -29.840 11.838  1.040   1.00 63.08  ? 1192 MET   B CE  1 
ATOM   3364 N N   . LYS   B 1 156 ? -34.962 12.826  1.824   1.00 69.58  ? 1193 LYS   B N   1 
ATOM   3365 C CA  . LYS   B 1 156 ? -35.988 12.920  0.796   1.00 72.58  ? 1193 LYS   B CA  1 
ATOM   3366 C C   . LYS   B 1 156 ? -35.971 14.315  0.174   1.00 72.69  ? 1193 LYS   B C   1 
ATOM   3367 O O   . LYS   B 1 156 ? -36.129 14.453  -1.037  1.00 74.33  ? 1193 LYS   B O   1 
ATOM   3368 C CB  . LYS   B 1 156 ? -37.372 12.613  1.378   1.00 75.31  ? 1193 LYS   B CB  1 
ATOM   3369 C CG  . LYS   B 1 156 ? -38.524 12.701  0.384   1.00 79.31  ? 1193 LYS   B CG  1 
ATOM   3370 C CD  . LYS   B 1 156 ? -39.881 12.423  0.993   1.00 82.47  ? 1193 LYS   B CD  1 
ATOM   3371 C CE  . LYS   B 1 156 ? -41.015 12.595  0.005   1.00 86.81  ? 1193 LYS   B CE  1 
ATOM   3372 N NZ  . LYS   B 1 156 ? -42.330 12.297  0.620   1.00 90.22  ? 1193 LYS   B NZ  1 
ATOM   3373 N N   . TYR   B 1 157 ? -35.795 15.339  1.020   1.00 71.12  ? 1194 TYR   B N   1 
ATOM   3374 C CA  . TYR   B 1 157 ? -35.741 16.723  0.574   1.00 71.09  ? 1194 TYR   B CA  1 
ATOM   3375 C C   . TYR   B 1 157 ? -34.541 16.930  -0.347  1.00 69.21  ? 1194 TYR   B C   1 
ATOM   3376 O O   . TYR   B 1 157 ? -34.673 17.512  -1.420  1.00 70.41  ? 1194 TYR   B O   1 
ATOM   3377 C CB  . TYR   B 1 157 ? -35.668 17.673  1.772   1.00 69.97  ? 1194 TYR   B CB  1 
ATOM   3378 C CG  . TYR   B 1 157 ? -35.606 19.135  1.407   1.00 70.43  ? 1194 TYR   B CG  1 
ATOM   3379 C CD1 . TYR   B 1 157 ? -36.699 19.779  0.848   1.00 73.50  ? 1194 TYR   B CD1 1 
ATOM   3380 C CD2 . TYR   B 1 157 ? -34.448 19.873  1.596   1.00 68.24  ? 1194 TYR   B CD2 1 
ATOM   3381 C CE1 . TYR   B 1 157 ? -36.650 21.120  0.504   1.00 74.03  ? 1194 TYR   B CE1 1 
ATOM   3382 C CE2 . TYR   B 1 157 ? -34.382 21.214  1.257   1.00 68.68  ? 1194 TYR   B CE2 1 
ATOM   3383 C CZ  . TYR   B 1 157 ? -35.486 21.841  0.707   1.00 71.52  ? 1194 TYR   B CZ  1 
ATOM   3384 O OH  . TYR   B 1 157 ? -35.427 23.171  0.368   1.00 72.14  ? 1194 TYR   B OH  1 
ATOM   3385 N N   . LEU   B 1 158 ? -33.373 16.448  0.092   1.00 66.34  ? 1195 LEU   B N   1 
ATOM   3386 C CA  . LEU   B 1 158 ? -32.139 16.582  -0.665  1.00 64.98  ? 1195 LEU   B CA  1 
ATOM   3387 C C   . LEU   B 1 158 ? -32.234 15.792  -1.970  1.00 66.55  ? 1195 LEU   B C   1 
ATOM   3388 O O   . LEU   B 1 158 ? -31.766 16.254  -3.008  1.00 66.98  ? 1195 LEU   B O   1 
ATOM   3389 C CB  . LEU   B 1 158 ? -30.974 16.083  0.198   1.00 62.55  ? 1195 LEU   B CB  1 
ATOM   3390 C CG  . LEU   B 1 158 ? -30.689 16.891  1.464   1.00 60.94  ? 1195 LEU   B CG  1 
ATOM   3391 C CD1 . LEU   B 1 158 ? -29.465 16.348  2.187   1.00 58.99  ? 1195 LEU   B CD1 1 
ATOM   3392 C CD2 . LEU   B 1 158 ? -30.504 18.368  1.146   1.00 61.03  ? 1195 LEU   B CD2 1 
ATOM   3393 N N   . ALA   B 1 159 ? -32.851 14.605  -1.901  1.00 67.55  ? 1196 ALA   B N   1 
ATOM   3394 C CA  . ALA   B 1 159 ? -33.000 13.730  -3.054  1.00 69.72  ? 1196 ALA   B CA  1 
ATOM   3395 C C   . ALA   B 1 159 ? -33.804 14.420  -4.156  1.00 72.62  ? 1196 ALA   B C   1 
ATOM   3396 O O   . ALA   B 1 159 ? -33.511 14.239  -5.336  1.00 74.21  ? 1196 ALA   B O   1 
ATOM   3397 C CB  . ALA   B 1 159 ? -33.654 12.436  -2.633  1.00 70.59  ? 1196 ALA   B CB  1 
ATOM   3398 N N   . SER   B 1 160 ? -34.812 15.208  -3.758  1.00 73.56  ? 1197 SER   B N   1 
ATOM   3399 C CA  . SER   B 1 160 ? -35.669 15.913  -4.699  1.00 76.49  ? 1197 SER   B CA  1 
ATOM   3400 C C   . SER   B 1 160 ? -34.909 17.048  -5.385  1.00 75.74  ? 1197 SER   B C   1 
ATOM   3401 O O   . SER   B 1 160 ? -35.249 17.426  -6.505  1.00 78.49  ? 1197 SER   B O   1 
ATOM   3402 C CB  . SER   B 1 160 ? -36.916 16.425  -4.020  1.00 77.89  ? 1197 SER   B CB  1 
ATOM   3403 O OG  . SER   B 1 160 ? -36.600 17.409  -3.047  1.00 75.53  ? 1197 SER   B OG  1 
ATOM   3404 N N   . LYS   B 1 161 ? -33.882 17.582  -4.710  1.00 91.19  ? 1198 LYS   B N   1 
ATOM   3405 C CA  . LYS   B 1 161 ? -33.061 18.653  -5.256  1.00 91.25  ? 1198 LYS   B CA  1 
ATOM   3406 C C   . LYS   B 1 161 ? -31.887 18.082  -6.053  1.00 89.97  ? 1198 LYS   B C   1 
ATOM   3407 O O   . LYS   B 1 161 ? -31.022 18.838  -6.491  1.00 90.11  ? 1198 LYS   B O   1 
ATOM   3408 C CB  . LYS   B 1 161 ? -32.545 19.552  -4.126  1.00 89.67  ? 1198 LYS   B CB  1 
ATOM   3409 C CG  . LYS   B 1 161 ? -33.614 20.145  -3.215  1.00 90.86  ? 1198 LYS   B CG  1 
ATOM   3410 C CD  . LYS   B 1 161 ? -34.597 21.057  -3.920  1.00 94.59  ? 1198 LYS   B CD  1 
ATOM   3411 C CE  . LYS   B 1 161 ? -35.635 21.635  -2.982  1.00 96.17  ? 1198 LYS   B CE  1 
ATOM   3412 N NZ  . LYS   B 1 161 ? -36.594 22.510  -3.698  1.00 100.33 ? 1198 LYS   B NZ  1 
ATOM   3413 N N   . LYS   B 1 162 ? -31.866 16.753  -6.237  1.00 89.10  ? 1199 LYS   B N   1 
ATOM   3414 C CA  . LYS   B 1 162 ? -30.820 16.062  -6.978  1.00 88.33  ? 1199 LYS   B CA  1 
ATOM   3415 C C   . LYS   B 1 162 ? -29.475 16.263  -6.281  1.00 85.56  ? 1199 LYS   B C   1 
ATOM   3416 O O   . LYS   B 1 162 ? -28.460 16.497  -6.935  1.00 85.84  ? 1199 LYS   B O   1 
ATOM   3417 C CB  . LYS   B 1 162 ? -30.778 16.533  -8.437  1.00 91.14  ? 1199 LYS   B CB  1 
ATOM   3418 C CG  . LYS   B 1 162 ? -32.114 16.512  -9.172  1.00 94.22  ? 1199 LYS   B CG  1 
ATOM   3419 C CD  . LYS   B 1 162 ? -32.831 15.173  -9.139  1.00 94.54  ? 1199 LYS   B CD  1 
ATOM   3420 C CE  . LYS   B 1 162 ? -32.034 14.037  -9.748  1.00 93.97  ? 1199 LYS   B CE  1 
ATOM   3421 N NZ  . LYS   B 1 162 ? -31.685 14.303  -11.164 1.00 96.27  ? 1199 LYS   B NZ  1 
ATOM   3422 N N   . PHE   B 1 163 ? -29.484 16.151  -4.947  1.00 83.09  ? 1200 PHE   B N   1 
ATOM   3423 C CA  . PHE   B 1 163 ? -28.289 16.316  -4.138  1.00 80.60  ? 1200 PHE   B CA  1 
ATOM   3424 C C   . PHE   B 1 163 ? -27.697 14.944  -3.826  1.00 78.50  ? 1200 PHE   B C   1 
ATOM   3425 O O   . PHE   B 1 163 ? -28.424 14.027  -3.447  1.00 78.14  ? 1200 PHE   B O   1 
ATOM   3426 C CB  . PHE   B 1 163 ? -28.623 17.067  -2.848  1.00 79.78  ? 1200 PHE   B CB  1 
ATOM   3427 C CG  . PHE   B 1 163 ? -27.437 17.367  -1.965  1.00 78.00  ? 1200 PHE   B CG  1 
ATOM   3428 C CD1 . PHE   B 1 163 ? -26.509 18.332  -2.327  1.00 78.80  ? 1200 PHE   B CD1 1 
ATOM   3429 C CD2 . PHE   B 1 163 ? -27.241 16.675  -0.779  1.00 75.84  ? 1200 PHE   B CD2 1 
ATOM   3430 C CE1 . PHE   B 1 163 ? -25.418 18.606  -1.516  1.00 77.41  ? 1200 PHE   B CE1 1 
ATOM   3431 C CE2 . PHE   B 1 163 ? -26.149 16.948  0.030   1.00 74.25  ? 1200 PHE   B CE2 1 
ATOM   3432 C CZ  . PHE   B 1 163 ? -25.240 17.913  -0.340  1.00 75.09  ? 1200 PHE   B CZ  1 
ATOM   3433 N N   . VAL   B 1 164 ? -26.373 14.821  -3.985  1.00 77.37  ? 1201 VAL   B N   1 
ATOM   3434 C CA  . VAL   B 1 164 ? -25.661 13.588  -3.691  1.00 75.65  ? 1201 VAL   B CA  1 
ATOM   3435 C C   . VAL   B 1 164 ? -24.722 13.853  -2.516  1.00 73.33  ? 1201 VAL   B C   1 
ATOM   3436 O O   . VAL   B 1 164 ? -23.753 14.599  -2.650  1.00 73.71  ? 1201 VAL   B O   1 
ATOM   3437 C CB  . VAL   B 1 164 ? -24.902 13.073  -4.931  1.00 77.13  ? 1201 VAL   B CB  1 
ATOM   3438 C CG1 . VAL   B 1 164 ? -24.360 11.667  -4.723  1.00 76.36  ? 1201 VAL   B CG1 1 
ATOM   3439 C CG2 . VAL   B 1 164 ? -25.765 13.122  -6.182  1.00 79.56  ? 1201 VAL   B CG2 1 
ATOM   3440 N N   . HIS   B 1 165 ? -25.025 13.235  -1.367  1.00 71.19  ? 1202 HIS   B N   1 
ATOM   3441 C CA  . HIS   B 1 165 ? -24.329 13.508  -0.119  1.00 69.11  ? 1202 HIS   B CA  1 
ATOM   3442 C C   . HIS   B 1 165 ? -22.936 12.879  -0.143  1.00 68.67  ? 1202 HIS   B C   1 
ATOM   3443 O O   . HIS   B 1 165 ? -21.948 13.558  0.128   1.00 68.55  ? 1202 HIS   B O   1 
ATOM   3444 C CB  . HIS   B 1 165 ? -25.156 12.992  1.066   1.00 67.64  ? 1202 HIS   B CB  1 
ATOM   3445 C CG  . HIS   B 1 165 ? -24.737 13.516  2.407   1.00 65.82  ? 1202 HIS   B CG  1 
ATOM   3446 N ND1 . HIS   B 1 165 ? -23.465 13.405  2.912   1.00 64.58  ? 1202 HIS   B ND1 1 
ATOM   3447 C CD2 . HIS   B 1 165 ? -25.480 14.171  3.343   1.00 65.38  ? 1202 HIS   B CD2 1 
ATOM   3448 C CE1 . HIS   B 1 165 ? -23.423 13.970  4.116   1.00 63.39  ? 1202 HIS   B CE1 1 
ATOM   3449 N NE2 . HIS   B 1 165 ? -24.663 14.450  4.405   1.00 63.84  ? 1202 HIS   B NE2 1 
ATOM   3450 N N   . ARG   B 1 166 ? -22.889 11.572  -0.439  1.00 68.92  ? 1203 ARG   B N   1 
ATOM   3451 C CA  . ARG   B 1 166 ? -21.654 10.820  -0.632  1.00 69.09  ? 1203 ARG   B CA  1 
ATOM   3452 C C   . ARG   B 1 166 ? -20.972 10.522  0.705   1.00 67.09  ? 1203 ARG   B C   1 
ATOM   3453 O O   . ARG   B 1 166 ? -19.845 10.031  0.714   1.00 67.44  ? 1203 ARG   B O   1 
ATOM   3454 C CB  . ARG   B 1 166 ? -20.682 11.561  -1.560  1.00 70.91  ? 1203 ARG   B CB  1 
ATOM   3455 C CG  . ARG   B 1 166 ? -21.286 11.998  -2.887  1.00 73.10  ? 1203 ARG   B CG  1 
ATOM   3456 C CD  . ARG   B 1 166 ? -20.400 12.976  -3.636  1.00 75.04  ? 1203 ARG   B CD  1 
ATOM   3457 N NE  . ARG   B 1 166 ? -19.163 12.374  -4.116  1.00 76.45  ? 1203 ARG   B NE  1 
ATOM   3458 C CZ  . ARG   B 1 166 ? -18.816 12.276  -5.395  1.00 79.19  ? 1203 ARG   B CZ  1 
ATOM   3459 N NH1 . ARG   B 1 166 ? -19.707 12.492  -6.347  1.00 80.50  ? 1203 ARG   B NH1 1 
ATOM   3460 N NH2 . ARG   B 1 166 ? -17.577 11.948  -5.721  1.00 80.93  ? 1203 ARG   B NH2 1 
ATOM   3461 N N   . ASP   B 1 167 ? -21.656 10.795  1.826   1.00 65.24  ? 1204 ASP   B N   1 
ATOM   3462 C CA  . ASP   B 1 167 ? -21.079 10.584  3.146   1.00 63.40  ? 1204 ASP   B CA  1 
ATOM   3463 C C   . ASP   B 1 167 ? -22.178 10.681  4.203   1.00 61.95  ? 1204 ASP   B C   1 
ATOM   3464 O O   . ASP   B 1 167 ? -22.070 11.464  5.146   1.00 60.99  ? 1204 ASP   B O   1 
ATOM   3465 C CB  . ASP   B 1 167 ? -19.952 11.586  3.426   1.00 63.35  ? 1204 ASP   B CB  1 
ATOM   3466 C CG  . ASP   B 1 167 ? -19.120 11.280  4.662   1.00 62.15  ? 1204 ASP   B CG  1 
ATOM   3467 O OD1 . ASP   B 1 167 ? -19.329 10.208  5.268   1.00 61.35  ? 1204 ASP   B OD1 1 
ATOM   3468 O OD2 . ASP   B 1 167 ? -18.269 12.121  5.013   1.00 62.20  ? 1204 ASP   B OD2 1 
ATOM   3469 N N   . LEU   B 1 168 ? -23.229 9.869   4.044   1.00 62.03  ? 1205 LEU   B N   1 
ATOM   3470 C CA  . LEU   B 1 168 ? -24.326 9.844   4.999   1.00 61.29  ? 1205 LEU   B CA  1 
ATOM   3471 C C   . LEU   B 1 168 ? -23.972 8.892   6.140   1.00 59.89  ? 1205 LEU   B C   1 
ATOM   3472 O O   . LEU   B 1 168 ? -23.633 7.734   5.903   1.00 60.17  ? 1205 LEU   B O   1 
ATOM   3473 C CB  . LEU   B 1 168 ? -25.609 9.414   4.280   1.00 62.89  ? 1205 LEU   B CB  1 
ATOM   3474 C CG  . LEU   B 1 168 ? -26.887 9.470   5.118   1.00 63.26  ? 1205 LEU   B CG  1 
ATOM   3475 C CD1 . LEU   B 1 168 ? -27.234 10.904  5.488   1.00 63.18  ? 1205 LEU   B CD1 1 
ATOM   3476 C CD2 . LEU   B 1 168 ? -28.046 8.818   4.381   1.00 65.31  ? 1205 LEU   B CD2 1 
ATOM   3477 N N   . ALA   B 1 169 ? -24.048 9.403   7.375   1.00 58.44  ? 1206 ALA   B N   1 
ATOM   3478 C CA  . ALA   B 1 169 ? -23.736 8.627   8.564   1.00 57.26  ? 1206 ALA   B CA  1 
ATOM   3479 C C   . ALA   B 1 169 ? -24.320 9.319   9.794   1.00 56.51  ? 1206 ALA   B C   1 
ATOM   3480 O O   . ALA   B 1 169 ? -24.816 10.440  9.701   1.00 56.83  ? 1206 ALA   B O   1 
ATOM   3481 C CB  . ALA   B 1 169 ? -22.242 8.456   8.686   1.00 56.57  ? 1206 ALA   B CB  1 
ATOM   3482 N N   . ALA   B 1 170 ? -24.254 8.633   10.941  1.00 55.79  ? 1207 ALA   B N   1 
ATOM   3483 C CA  . ALA   B 1 170 ? -24.752 9.167   12.199  1.00 55.44  ? 1207 ALA   B CA  1 
ATOM   3484 C C   . ALA   B 1 170 ? -23.918 10.374  12.625  1.00 54.51  ? 1207 ALA   B C   1 
ATOM   3485 O O   . ALA   B 1 170 ? -24.461 11.361  13.117  1.00 54.76  ? 1207 ALA   B O   1 
ATOM   3486 C CB  . ALA   B 1 170 ? -24.735 8.089   13.255  1.00 55.35  ? 1207 ALA   B CB  1 
ATOM   3487 N N   . ARG   B 1 171 ? -22.597 10.279  12.424  1.00 53.78  ? 1208 ARG   B N   1 
ATOM   3488 C CA  . ARG   B 1 171 ? -21.665 11.341  12.775  1.00 53.11  ? 1208 ARG   B CA  1 
ATOM   3489 C C   . ARG   B 1 171 ? -22.048 12.648  12.080  1.00 53.72  ? 1208 ARG   B C   1 
ATOM   3490 O O   . ARG   B 1 171 ? -21.840 13.723  12.639  1.00 53.76  ? 1208 ARG   B O   1 
ATOM   3491 C CB  . ARG   B 1 171 ? -20.231 10.931  12.417  1.00 52.98  ? 1208 ARG   B CB  1 
ATOM   3492 C CG  . ARG   B 1 171 ? -20.004 10.658  10.936  1.00 53.84  ? 1208 ARG   B CG  1 
ATOM   3493 C CD  . ARG   B 1 171 ? -18.592 10.200  10.625  1.00 54.30  ? 1208 ARG   B CD  1 
ATOM   3494 N NE  . ARG   B 1 171 ? -18.419 9.967   9.196   1.00 55.43  ? 1208 ARG   B NE  1 
ATOM   3495 C CZ  . ARG   B 1 171 ? -18.236 8.776   8.634   1.00 56.07  ? 1208 ARG   B CZ  1 
ATOM   3496 N NH1 . ARG   B 1 171 ? -18.070 7.702   9.385   1.00 55.72  ? 1208 ARG   B NH1 1 
ATOM   3497 N NH2 . ARG   B 1 171 ? -18.220 8.662   7.316   1.00 57.24  ? 1208 ARG   B NH2 1 
ATOM   3498 N N   . ASN   B 1 172 ? -22.608 12.548  10.865  1.00 54.55  ? 1209 ASN   B N   1 
ATOM   3499 C CA  . ASN   B 1 172 ? -22.992 13.714  10.082  1.00 55.60  ? 1209 ASN   B CA  1 
ATOM   3500 C C   . ASN   B 1 172 ? -24.493 13.977  10.215  1.00 56.42  ? 1209 ASN   B C   1 
ATOM   3501 O O   . ASN   B 1 172 ? -25.120 14.476  9.283   1.00 57.42  ? 1209 ASN   B O   1 
ATOM   3502 C CB  . ASN   B 1 172 ? -22.580 13.546  8.617   1.00 56.43  ? 1209 ASN   B CB  1 
ATOM   3503 C CG  . ASN   B 1 172 ? -21.081 13.431  8.429   1.00 56.30  ? 1209 ASN   B CG  1 
ATOM   3504 O OD1 . ASN   B 1 172 ? -20.311 13.654  9.361   1.00 55.66  ? 1209 ASN   B OD1 1 
ATOM   3505 N ND2 . ASN   B 1 172 ? -20.656 13.097  7.222   1.00 57.33  ? 1209 ASN   B ND2 1 
ATOM   3506 N N   . CYS   B 1 173 ? -25.057 13.650  11.385  1.00 56.25  ? 1210 CYS   B N   1 
ATOM   3507 C CA  . CYS   B 1 173 ? -26.435 13.974  11.715  1.00 57.68  ? 1210 CYS   B CA  1 
ATOM   3508 C C   . CYS   B 1 173 ? -26.467 14.626  13.095  1.00 57.54  ? 1210 CYS   B C   1 
ATOM   3509 O O   . CYS   B 1 173 ? -25.894 14.091  14.041  1.00 56.31  ? 1210 CYS   B O   1 
ATOM   3510 C CB  . CYS   B 1 173 ? -27.315 12.731  11.691  1.00 58.40  ? 1210 CYS   B CB  1 
ATOM   3511 S SG  . CYS   B 1 173 ? -27.429 11.964  10.054  1.00 59.29  ? 1210 CYS   B SG  1 
ATOM   3512 N N   . MET   B 1 174 ? -27.145 15.776  13.196  1.00 59.06  ? 1211 MET   B N   1 
ATOM   3513 C CA  . MET   B 1 174 ? -26.995 16.654  14.345  1.00 59.41  ? 1211 MET   B CA  1 
ATOM   3514 C C   . MET   B 1 174 ? -28.348 16.876  15.018  1.00 61.35  ? 1211 MET   B C   1 
ATOM   3515 O O   . MET   B 1 174 ? -29.366 17.010  14.342  1.00 62.93  ? 1211 MET   B O   1 
ATOM   3516 C CB  . MET   B 1 174 ? -26.426 18.007  13.907  1.00 60.02  ? 1211 MET   B CB  1 
ATOM   3517 C CG  . MET   B 1 174 ? -25.046 17.917  13.273  1.00 58.96  ? 1211 MET   B CG  1 
ATOM   3518 S SD  . MET   B 1 174 ? -23.753 17.392  14.428  1.00 57.39  ? 1211 MET   B SD  1 
ATOM   3519 C CE  . MET   B 1 174 ? -22.284 17.886  13.529  1.00 57.45  ? 1211 MET   B CE  1 
ATOM   3520 N N   . LEU   B 1 175 ? -28.332 16.927  16.358  1.00 61.54  ? 1212 LEU   B N   1 
ATOM   3521 C CA  . LEU   B 1 175 ? -29.518 17.192  17.158  1.00 63.78  ? 1212 LEU   B CA  1 
ATOM   3522 C C   . LEU   B 1 175 ? -29.489 18.639  17.644  1.00 65.05  ? 1212 LEU   B C   1 
ATOM   3523 O O   . LEU   B 1 175 ? -28.485 19.083  18.199  1.00 64.00  ? 1212 LEU   B O   1 
ATOM   3524 C CB  . LEU   B 1 175 ? -29.548 16.236  18.356  1.00 63.40  ? 1212 LEU   B CB  1 
ATOM   3525 C CG  . LEU   B 1 175 ? -29.804 14.760  18.047  1.00 63.19  ? 1212 LEU   B CG  1 
ATOM   3526 C CD1 . LEU   B 1 175 ? -31.020 14.586  17.150  1.00 65.36  ? 1212 LEU   B CD1 1 
ATOM   3527 C CD2 . LEU   B 1 175 ? -28.578 14.105  17.426  1.00 60.89  ? 1212 LEU   B CD2 1 
ATOM   3528 N N   . ASP   B 1 176 ? -30.604 19.356  17.450  1.00 67.78  ? 1213 ASP   B N   1 
ATOM   3529 C CA  . ASP   B 1 176 ? -30.763 20.701  17.981  1.00 69.59  ? 1213 ASP   B CA  1 
ATOM   3530 C C   . ASP   B 1 176 ? -31.252 20.591  19.426  1.00 70.82  ? 1213 ASP   B C   1 
ATOM   3531 O O   . ASP   B 1 176 ? -31.159 19.525  20.031  1.00 69.58  ? 1213 ASP   B O   1 
ATOM   3532 C CB  . ASP   B 1 176 ? -31.659 21.549  17.068  1.00 72.07  ? 1213 ASP   B CB  1 
ATOM   3533 C CG  . ASP   B 1 176 ? -33.124 21.145  17.031  1.00 74.60  ? 1213 ASP   B CG  1 
ATOM   3534 O OD1 . ASP   B 1 176 ? -33.480 20.143  17.682  1.00 74.47  ? 1213 ASP   B OD1 1 
ATOM   3535 O OD2 . ASP   B 1 176 ? -33.901 21.840  16.345  1.00 76.92  ? 1213 ASP   B OD2 1 
ATOM   3536 N N   . GLU   B 1 177 ? -31.764 21.699  19.979  1.00 73.52  ? 1214 GLU   B N   1 
ATOM   3537 C CA  . GLU   B 1 177 ? -32.209 21.737  21.364  1.00 75.18  ? 1214 GLU   B CA  1 
ATOM   3538 C C   . GLU   B 1 177 ? -33.487 20.915  21.539  1.00 77.29  ? 1214 GLU   B C   1 
ATOM   3539 O O   . GLU   B 1 177 ? -33.752 20.420  22.632  1.00 77.92  ? 1214 GLU   B O   1 
ATOM   3540 C CB  . GLU   B 1 177 ? -32.394 23.182  21.844  1.00 77.81  ? 1214 GLU   B CB  1 
ATOM   3541 C CG  . GLU   B 1 177 ? -33.613 23.901  21.281  1.00 81.55  ? 1214 GLU   B CG  1 
ATOM   3542 C CD  . GLU   B 1 177 ? -33.534 24.338  19.827  1.00 81.51  ? 1214 GLU   B CD  1 
ATOM   3543 O OE1 . GLU   B 1 177 ? -34.547 24.855  19.315  1.00 84.63  ? 1214 GLU   B OE1 1 
ATOM   3544 O OE2 . GLU   B 1 177 ? -32.461 24.172  19.212  1.00 78.61  ? 1214 GLU   B OE2 1 
ATOM   3545 N N   . LYS   B 1 178 ? -34.269 20.771  20.458  1.00 78.69  ? 1215 LYS   B N   1 
ATOM   3546 C CA  . LYS   B 1 178 ? -35.513 20.015  20.485  1.00 81.31  ? 1215 LYS   B CA  1 
ATOM   3547 C C   . LYS   B 1 178 ? -35.285 18.578  20.008  1.00 79.25  ? 1215 LYS   B C   1 
ATOM   3548 O O   . LYS   B 1 178 ? -36.240 17.896  19.640  1.00 81.30  ? 1215 LYS   B O   1 
ATOM   3549 C CB  . LYS   B 1 178 ? -36.565 20.708  19.612  1.00 84.63  ? 1215 LYS   B CB  1 
ATOM   3550 C CG  . LYS   B 1 178 ? -36.902 22.139  20.013  1.00 87.46  ? 1215 LYS   B CG  1 
ATOM   3551 C CD  . LYS   B 1 178 ? -37.899 22.817  19.094  1.00 91.00  ? 1215 LYS   B CD  1 
ATOM   3552 C CE  . LYS   B 1 178 ? -39.277 22.189  19.129  1.00 94.70  ? 1215 LYS   B CE  1 
ATOM   3553 N NZ  . LYS   B 1 178 ? -40.239 22.935  18.284  1.00 98.59  ? 1215 LYS   B NZ  1 
ATOM   3554 N N   . PHE   B 1 179 ? -34.023 18.124  20.028  1.00 75.54  ? 1216 PHE   B N   1 
ATOM   3555 C CA  . PHE   B 1 179 ? -33.654 16.769  19.645  1.00 73.45  ? 1216 PHE   B CA  1 
ATOM   3556 C C   . PHE   B 1 179 ? -34.156 16.456  18.235  1.00 73.96  ? 1216 PHE   B C   1 
ATOM   3557 O O   . PHE   B 1 179 ? -34.681 15.371  17.988  1.00 74.69  ? 1216 PHE   B O   1 
ATOM   3558 C CB  . PHE   B 1 179 ? -34.185 15.747  20.657  1.00 74.65  ? 1216 PHE   B CB  1 
ATOM   3559 C CG  . PHE   B 1 179 ? -33.768 15.982  22.088  1.00 74.47  ? 1216 PHE   B CG  1 
ATOM   3560 C CD1 . PHE   B 1 179 ? -32.733 15.251  22.653  1.00 71.90  ? 1216 PHE   B CD1 1 
ATOM   3561 C CD2 . PHE   B 1 179 ? -34.432 16.905  22.883  1.00 77.23  ? 1216 PHE   B CD2 1 
ATOM   3562 C CE1 . PHE   B 1 179 ? -32.354 15.458  23.971  1.00 71.89  ? 1216 PHE   B CE1 1 
ATOM   3563 C CE2 . PHE   B 1 179 ? -34.053 17.109  24.202  1.00 77.23  ? 1216 PHE   B CE2 1 
ATOM   3564 C CZ  . PHE   B 1 179 ? -33.016 16.384  24.744  1.00 74.52  ? 1216 PHE   B CZ  1 
ATOM   3565 N N   . THR   B 1 180 ? -33.974 17.411  17.314  1.00 73.78  ? 1217 THR   B N   1 
ATOM   3566 C CA  . THR   B 1 180 ? -34.408 17.257  15.934  1.00 74.54  ? 1217 THR   B CA  1 
ATOM   3567 C C   . THR   B 1 180 ? -33.201 16.905  15.068  1.00 71.46  ? 1217 THR   B C   1 
ATOM   3568 O O   . THR   B 1 180 ? -32.248 17.677  14.992  1.00 69.96  ? 1217 THR   B O   1 
ATOM   3569 C CB  . THR   B 1 180 ? -35.103 18.528  15.428  1.00 77.21  ? 1217 THR   B CB  1 
ATOM   3570 O OG1 . THR   B 1 180 ? -36.114 18.890  16.370  1.00 80.26  ? 1217 THR   B OG1 1 
ATOM   3571 C CG2 . THR   B 1 180 ? -35.720 18.359  14.057  1.00 78.64  ? 1217 THR   B CG2 1 
ATOM   3572 N N   . VAL   B 1 181 ? -33.260 15.737  14.417  1.00 71.03  ? 1218 VAL   B N   1 
ATOM   3573 C CA  . VAL   B 1 181 ? -32.165 15.248  13.595  1.00 68.59  ? 1218 VAL   B CA  1 
ATOM   3574 C C   . VAL   B 1 181 ? -32.134 16.051  12.297  1.00 69.29  ? 1218 VAL   B C   1 
ATOM   3575 O O   . VAL   B 1 181 ? -33.127 16.097  11.573  1.00 71.43  ? 1218 VAL   B O   1 
ATOM   3576 C CB  . VAL   B 1 181 ? -32.295 13.738  13.313  1.00 68.32  ? 1218 VAL   B CB  1 
ATOM   3577 C CG1 . VAL   B 1 181 ? -31.220 13.245  12.354  1.00 66.20  ? 1218 VAL   B CG1 1 
ATOM   3578 C CG2 . VAL   B 1 181 ? -32.283 12.915  14.593  1.00 68.01  ? 1218 VAL   B CG2 1 
ATOM   3579 N N   . LYS   B 1 182 ? -30.982 16.676  12.022  1.00 67.80  ? 1219 LYS   B N   1 
ATOM   3580 C CA  . LYS   B 1 182 ? -30.768 17.431  10.797  1.00 68.52  ? 1219 LYS   B CA  1 
ATOM   3581 C C   . LYS   B 1 182 ? -29.549 16.867  10.072  1.00 66.56  ? 1219 LYS   B C   1 
ATOM   3582 O O   . LYS   B 1 182 ? -28.506 16.650  10.685  1.00 64.50  ? 1219 LYS   B O   1 
ATOM   3583 C CB  . LYS   B 1 182 ? -30.574 18.919  11.108  1.00 69.39  ? 1219 LYS   B CB  1 
ATOM   3584 C CG  . LYS   B 1 182 ? -31.760 19.606  11.773  1.00 72.00  ? 1219 LYS   B CG  1 
ATOM   3585 C CD  . LYS   B 1 182 ? -31.526 21.077  12.051  1.00 73.12  ? 1219 LYS   B CD  1 
ATOM   3586 C CE  . LYS   B 1 182 ? -32.663 21.732  12.806  1.00 75.99  ? 1219 LYS   B CE  1 
ATOM   3587 N NZ  . LYS   B 1 182 ? -33.928 21.708  12.033  1.00 78.84  ? 1219 LYS   B NZ  1 
ATOM   3588 N N   . VAL   B 1 183 ? -29.699 16.639  8.761   1.00 67.58  ? 1220 VAL   B N   1 
ATOM   3589 C CA  . VAL   B 1 183 ? -28.637 16.085  7.938   1.00 66.58  ? 1220 VAL   B CA  1 
ATOM   3590 C C   . VAL   B 1 183 ? -27.611 17.183  7.666   1.00 66.64  ? 1220 VAL   B C   1 
ATOM   3591 O O   . VAL   B 1 183 ? -27.943 18.207  7.071   1.00 68.38  ? 1220 VAL   B O   1 
ATOM   3592 C CB  . VAL   B 1 183 ? -29.194 15.498  6.625   1.00 67.82  ? 1220 VAL   B CB  1 
ATOM   3593 C CG1 . VAL   B 1 183 ? -28.084 15.007  5.707   1.00 66.83  ? 1220 VAL   B CG1 1 
ATOM   3594 C CG2 . VAL   B 1 183 ? -30.203 14.388  6.886   1.00 68.61  ? 1220 VAL   B CG2 1 
ATOM   3595 N N   . ALA   B 1 184 ? -26.368 16.953  8.111   1.00 65.32  ? 1221 ALA   B N   1 
ATOM   3596 C CA  . ALA   B 1 184 ? -25.284 17.906  7.937   1.00 65.64  ? 1221 ALA   B CA  1 
ATOM   3597 C C   . ALA   B 1 184 ? -24.295 17.380  6.900   1.00 65.75  ? 1221 ALA   B C   1 
ATOM   3598 O O   . ALA   B 1 184 ? -24.146 16.171  6.739   1.00 64.81  ? 1221 ALA   B O   1 
ATOM   3599 C CB  . ALA   B 1 184 ? -24.608 18.155  9.263   1.00 64.51  ? 1221 ALA   B CB  1 
ATOM   3600 N N   . ASP   B 1 185 ? -23.622 18.311  6.209   1.00 67.31  ? 1222 ASP   B N   1 
ATOM   3601 C CA  . ASP   B 1 185 ? -22.638 17.983  5.190   1.00 68.12  ? 1222 ASP   B CA  1 
ATOM   3602 C C   . ASP   B 1 185 ? -21.311 18.643  5.561   1.00 68.73  ? 1222 ASP   B C   1 
ATOM   3603 O O   . ASP   B 1 185 ? -21.294 19.802  5.965   1.00 69.60  ? 1222 ASP   B O   1 
ATOM   3604 C CB  . ASP   B 1 185 ? -23.111 18.443  3.807   1.00 70.02  ? 1222 ASP   B CB  1 
ATOM   3605 C CG  . ASP   B 1 185 ? -22.239 17.979  2.652   1.00 70.75  ? 1222 ASP   B CG  1 
ATOM   3606 O OD1 . ASP   B 1 185 ? -21.415 17.064  2.860   1.00 69.85  ? 1222 ASP   B OD1 1 
ATOM   3607 O OD2 . ASP   B 1 185 ? -22.378 18.549  1.552   1.00 72.53  ? 1222 ASP   B OD2 1 
ATOM   3608 N N   . PHE   B 1 186 ? -20.209 17.895  5.412   1.00 68.98  ? 1223 PHE   B N   1 
ATOM   3609 C CA  . PHE   B 1 186 ? -18.878 18.391  5.730   1.00 70.09  ? 1223 PHE   B CA  1 
ATOM   3610 C C   . PHE   B 1 186 ? -18.052 18.590  4.459   1.00 73.00  ? 1223 PHE   B C   1 
ATOM   3611 O O   . PHE   B 1 186 ? -16.841 18.789  4.535   1.00 74.04  ? 1223 PHE   B O   1 
ATOM   3612 C CB  . PHE   B 1 186 ? -18.174 17.436  6.699   1.00 68.37  ? 1223 PHE   B CB  1 
ATOM   3613 C CG  . PHE   B 1 186 ? -18.500 17.653  8.156   1.00 66.85  ? 1223 PHE   B CG  1 
ATOM   3614 C CD1 . PHE   B 1 186 ? -18.073 18.796  8.816   1.00 67.51  ? 1223 PHE   B CD1 1 
ATOM   3615 C CD2 . PHE   B 1 186 ? -19.227 16.713  8.871   1.00 65.16  ? 1223 PHE   B CD2 1 
ATOM   3616 C CE1 . PHE   B 1 186 ? -18.367 18.995  10.157  1.00 66.48  ? 1223 PHE   B CE1 1 
ATOM   3617 C CE2 . PHE   B 1 186 ? -19.522 16.913  10.211  1.00 64.21  ? 1223 PHE   B CE2 1 
ATOM   3618 C CZ  . PHE   B 1 186 ? -19.092 18.054  10.852  1.00 64.82  ? 1223 PHE   B CZ  1 
ATOM   3619 N N   . GLY   B 1 187 ? -18.711 18.545  3.294   1.00 75.20  ? 1224 GLY   B N   1 
ATOM   3620 C CA  . GLY   B 1 187 ? -18.057 18.807  2.023   1.00 78.55  ? 1224 GLY   B CA  1 
ATOM   3621 C C   . GLY   B 1 187 ? -17.111 17.680  1.615   1.00 79.91  ? 1224 GLY   B C   1 
ATOM   3622 O O   . GLY   B 1 187 ? -15.956 17.932  1.275   1.00 81.81  ? 1224 GLY   B O   1 
ATOM   3623 N N   . LEU   B 1 188 ? -17.617 16.442  1.652   1.00 79.99  ? 1225 LEU   B N   1 
ATOM   3624 C CA  . LEU   B 1 188 ? -16.872 15.282  1.189   1.00 81.56  ? 1225 LEU   B CA  1 
ATOM   3625 C C   . LEU   B 1 188 ? -16.868 15.285  -0.339  1.00 84.89  ? 1225 LEU   B C   1 
ATOM   3626 O O   . LEU   B 1 188 ? -15.852 14.977  -0.960  1.00 86.87  ? 1225 LEU   B O   1 
ATOM   3627 C CB  . LEU   B 1 188 ? -17.521 14.014  1.760   1.00 79.66  ? 1225 LEU   B CB  1 
ATOM   3628 C CG  . LEU   B 1 188 ? -16.658 12.749  1.791   1.00 79.97  ? 1225 LEU   B CG  1 
ATOM   3629 C CD1 . LEU   B 1 188 ? -16.295 12.274  0.390   1.00 82.27  ? 1225 LEU   B CD1 1 
ATOM   3630 C CD2 . LEU   B 1 188 ? -15.401 12.963  2.624   1.00 80.23  ? 1225 LEU   B CD2 1 
ATOM   3631 N N   . ALA   B 1 189 ? -18.015 15.656  -0.927  1.00 86.18  ? 1226 ALA   B N   1 
ATOM   3632 C CA  . ALA   B 1 189 ? -18.169 15.774  -2.369  1.00 89.22  ? 1226 ALA   B CA  1 
ATOM   3633 C C   . ALA   B 1 189 ? -17.044 16.622  -2.961  1.00 92.58  ? 1226 ALA   B C   1 
ATOM   3634 O O   . ALA   B 1 189 ? -16.453 16.247  -3.972  1.00 94.92  ? 1226 ALA   B O   1 
ATOM   3635 C CB  . ALA   B 1 189 ? -19.521 16.365  -2.691  1.00 89.22  ? 1226 ALA   B CB  1 
ATOM   3636 N N   . ARG   B 1 190 ? -16.763 17.763  -2.319  1.00 93.44  ? 1227 ARG   B N   1 
ATOM   3637 C CA  . ARG   B 1 190 ? -15.730 18.684  -2.767  1.00 96.90  ? 1227 ARG   B CA  1 
ATOM   3638 C C   . ARG   B 1 190 ? -14.374 17.984  -2.805  1.00 98.70  ? 1227 ARG   B C   1 
ATOM   3639 O O   . ARG   B 1 190 ? -13.718 17.958  -3.845  1.00 101.32 ? 1227 ARG   B O   1 
ATOM   3640 C CB  . ARG   B 1 190 ? -15.654 19.899  -1.836  1.00 96.76  ? 1227 ARG   B CB  1 
ATOM   3641 C CG  . ARG   B 1 190 ? -16.862 20.823  -1.898  1.00 96.61  ? 1227 ARG   B CG  1 
ATOM   3642 C CD  . ARG   B 1 190 ? -16.838 21.849  -0.781  1.00 96.16  ? 1227 ARG   B CD  1 
ATOM   3643 N NE  . ARG   B 1 190 ? -15.556 22.541  -0.703  1.00 98.55  ? 1227 ARG   B NE  1 
ATOM   3644 C CZ  . ARG   B 1 190 ? -14.655 22.370  0.262   1.00 97.98  ? 1227 ARG   B CZ  1 
ATOM   3645 N NH1 . ARG   B 1 190 ? -13.503 23.014  0.210   1.00 100.71 ? 1227 ARG   B NH1 1 
ATOM   3646 N NH2 . ARG   B 1 190 ? -14.902 21.551  1.270   1.00 94.88  ? 1227 ARG   B NH2 1 
ATOM   3647 N N   . ASN   B 1 191 ? -13.978 17.413  -1.660  1.00 97.69  ? 1228 ASN   B N   1 
ATOM   3648 C CA  . ASN   B 1 191 ? -12.648 16.853  -1.466  1.00 99.66  ? 1228 ASN   B CA  1 
ATOM   3649 C C   . ASN   B 1 191 ? -12.350 15.786  -2.518  1.00 101.86 ? 1228 ASN   B C   1 
ATOM   3650 O O   . ASN   B 1 191 ? -11.217 15.678  -2.983  1.00 104.83 ? 1228 ASN   B O   1 
ATOM   3651 C CB  . ASN   B 1 191 ? -12.480 16.268  -0.060  1.00 97.08  ? 1228 ASN   B CB  1 
ATOM   3652 C CG  . ASN   B 1 191 ? -12.600 17.302  1.040   1.00 95.92  ? 1228 ASN   B CG  1 
ATOM   3653 O OD1 . ASN   B 1 191 ? -12.848 18.477  0.777   1.00 97.09  ? 1228 ASN   B OD1 1 
ATOM   3654 N ND2 . ASN   B 1 191 ? -12.427 16.873  2.280   1.00 93.94  ? 1228 ASN   B ND2 1 
ATOM   3655 N N   . MET   B 1 192 ? -13.371 14.997  -2.876  1.00 100.95 ? 1229 MET   B N   1 
ATOM   3656 C CA  . MET   B 1 192 ? -13.217 13.918  -3.838  1.00 102.90 ? 1229 MET   B CA  1 
ATOM   3657 C C   . MET   B 1 192 ? -12.896 14.482  -5.221  1.00 107.18 ? 1229 MET   B C   1 
ATOM   3658 O O   . MET   B 1 192 ? -11.986 13.996  -5.889  1.00 110.02 ? 1229 MET   B O   1 
ATOM   3659 C CB  . MET   B 1 192 ? -14.489 13.068  -3.921  1.00 100.47 ? 1229 MET   B CB  1 
ATOM   3660 C CG  . MET   B 1 192 ? -14.520 11.934  -2.917  1.00 98.12  ? 1229 MET   B CG  1 
ATOM   3661 S SD  . MET   B 1 192 ? -15.946 10.848  -3.156  1.00 96.64  ? 1229 MET   B SD  1 
ATOM   3662 C CE  . MET   B 1 192 ? -15.336 9.792   -4.470  1.00 99.53  ? 1229 MET   B CE  1 
ATOM   3663 N N   . TYR   B 1 193 ? -13.650 15.506  -5.641  1.00 108.20 ? 1230 TYR   B N   1 
ATOM   3664 C CA  . TYR   B 1 193 ? -13.504 16.079  -6.971  1.00 112.32 ? 1230 TYR   B CA  1 
ATOM   3665 C C   . TYR   B 1 193 ? -12.253 16.956  -7.057  1.00 116.08 ? 1230 TYR   B C   1 
ATOM   3666 O O   . TYR   B 1 193 ? -11.744 17.186  -8.152  1.00 119.55 ? 1230 TYR   B O   1 
ATOM   3667 C CB  . TYR   B 1 193 ? -14.760 16.864  -7.363  1.00 111.77 ? 1230 TYR   B CB  1 
ATOM   3668 C CG  . TYR   B 1 193 ? -15.954 16.011  -7.712  1.00 110.13 ? 1230 TYR   B CG  1 
ATOM   3669 C CD1 . TYR   B 1 193 ? -15.884 15.064  -8.723  1.00 111.77 ? 1230 TYR   B CD1 1 
ATOM   3670 C CD2 . TYR   B 1 193 ? -17.160 16.153  -7.044  1.00 107.28 ? 1230 TYR   B CD2 1 
ATOM   3671 C CE1 . TYR   B 1 193 ? -16.975 14.277  -9.055  1.00 110.58 ? 1230 TYR   B CE1 1 
ATOM   3672 C CE2 . TYR   B 1 193 ? -18.261 15.375  -7.364  1.00 106.27 ? 1230 TYR   B CE2 1 
ATOM   3673 C CZ  . TYR   B 1 193 ? -18.169 14.433  -8.374  1.00 107.87 ? 1230 TYR   B CZ  1 
ATOM   3674 O OH  . TYR   B 1 193 ? -19.254 13.656  -8.700  1.00 107.10 ? 1230 TYR   B OH  1 
ATOM   3675 N N   . ASP   B 1 194 ? -11.767 17.446  -5.908  1.00 115.85 ? 1231 ASP   B N   1 
ATOM   3676 C CA  . ASP   B 1 194 ? -10.549 18.241  -5.867  1.00 119.58 ? 1231 ASP   B CA  1 
ATOM   3677 C C   . ASP   B 1 194 ? -9.339  17.330  -6.065  1.00 122.24 ? 1231 ASP   B C   1 
ATOM   3678 O O   . ASP   B 1 194 ? -8.597  17.486  -7.033  1.00 126.22 ? 1231 ASP   B O   1 
ATOM   3679 C CB  . ASP   B 1 194 ? -10.430 19.033  -4.562  1.00 118.07 ? 1231 ASP   B CB  1 
ATOM   3680 C CG  . ASP   B 1 194 ? -11.446 20.154  -4.418  1.00 116.97 ? 1231 ASP   B CG  1 
ATOM   3681 O OD1 . ASP   B 1 194 ? -11.565 20.962  -5.361  1.00 119.63 ? 1231 ASP   B OD1 1 
ATOM   3682 O OD2 . ASP   B 1 194 ? -12.097 20.222  -3.356  1.00 113.64 ? 1231 ASP   B OD2 1 
ATOM   3683 N N   . LYS   B 1 195 ? -9.158  16.381  -5.138  1.00 120.45 ? 1232 LYS   B N   1 
ATOM   3684 C CA  . LYS   B 1 195 ? -7.996  15.506  -5.124  1.00 123.04 ? 1232 LYS   B CA  1 
ATOM   3685 C C   . LYS   B 1 195 ? -8.332  14.202  -5.846  1.00 123.52 ? 1232 LYS   B C   1 
ATOM   3686 O O   . LYS   B 1 195 ? -8.703  13.214  -5.211  1.00 121.25 ? 1232 LYS   B O   1 
ATOM   3687 C CB  . LYS   B 1 195 ? -7.555  15.256  -3.677  1.00 120.75 ? 1232 LYS   B CB  1 
ATOM   3688 C CG  . LYS   B 1 195 ? -6.287  14.427  -3.511  1.00 123.07 ? 1232 LYS   B CG  1 
ATOM   3689 C CD  . LYS   B 1 195 ? -5.939  14.144  -2.066  1.00 120.71 ? 1232 LYS   B CD  1 
ATOM   3690 C CE  . LYS   B 1 195 ? -4.715  13.265  -1.914  1.00 123.43 ? 1232 LYS   B CE  1 
ATOM   3691 N NZ  . LYS   B 1 195 ? -4.424  12.975  -0.490  1.00 121.39 ? 1232 LYS   B NZ  1 
ATOM   3692 N N   . GLU   B 1 196 ? -8.200  14.217  -7.181  1.00 126.92 ? 1233 GLU   B N   1 
ATOM   3693 C CA  . GLU   B 1 196 ? -8.407  13.032  -8.000  1.00 127.59 ? 1233 GLU   B CA  1 
ATOM   3694 C C   . GLU   B 1 196 ? -7.795  13.274  -9.388  1.00 132.25 ? 1233 GLU   B C   1 
ATOM   3695 O O   . GLU   B 1 196 ? -8.092  14.341  -9.965  1.00 133.12 ? 1233 GLU   B O   1 
ATOM   3696 C CB  . GLU   B 1 196 ? -9.901  12.696  -8.086  1.00 124.21 ? 1233 GLU   B CB  1 
ATOM   3697 C CG  . GLU   B 1 196 ? -10.203 11.380  -8.789  1.00 124.82 ? 1233 GLU   B CG  1 
ATOM   3698 C CD  . GLU   B 1 196 ? -10.360 11.439  -10.301 1.00 128.20 ? 1233 GLU   B CD  1 
ATOM   3699 O OE1 . GLU   B 1 196 ? -10.382 12.556  -10.860 1.00 130.01 ? 1233 GLU   B OE1 1 
ATOM   3700 O OE2 . GLU   B 1 196 ? -10.465 10.360  -10.919 1.00 129.29 ? 1233 GLU   B OE2 1 
ATOM   3701 N N   . ALA   B 1 206 ? -6.584  9.495   -1.168  1.00 85.30  ? 1243 ALA   B N   1 
ATOM   3702 C CA  . ALA   B 1 206 ? -7.834  10.099  -0.645  1.00 81.18  ? 1243 ALA   B CA  1 
ATOM   3703 C C   . ALA   B 1 206 ? -8.494  9.137   0.340   1.00 77.84  ? 1243 ALA   B C   1 
ATOM   3704 O O   . ALA   B 1 206 ? -8.605  7.944   0.062   1.00 78.18  ? 1243 ALA   B O   1 
ATOM   3705 C CB  . ALA   B 1 206 ? -8.758  10.439  -1.789  1.00 81.08  ? 1243 ALA   B CB  1 
ATOM   3706 N N   . LYS   B 1 207 ? -8.932  9.677   1.485   1.00 74.89  ? 1244 LYS   B N   1 
ATOM   3707 C CA  . LYS   B 1 207 ? -9.549  8.888   2.540   1.00 71.96  ? 1244 LYS   B CA  1 
ATOM   3708 C C   . LYS   B 1 207 ? -11.070 8.988   2.427   1.00 69.07  ? 1244 LYS   B C   1 
ATOM   3709 O O   . LYS   B 1 207 ? -11.644 10.045  2.687   1.00 67.56  ? 1244 LYS   B O   1 
ATOM   3710 C CB  . LYS   B 1 207 ? -9.058  9.367   3.911   1.00 70.99  ? 1244 LYS   B CB  1 
ATOM   3711 C CG  . LYS   B 1 207 ? -7.601  9.050   4.220   1.00 73.90  ? 1244 LYS   B CG  1 
ATOM   3712 C CD  . LYS   B 1 207 ? -7.169  9.467   5.611   1.00 73.00  ? 1244 LYS   B CD  1 
ATOM   3713 C CE  . LYS   B 1 207 ? -5.785  8.973   5.979   1.00 76.00  ? 1244 LYS   B CE  1 
ATOM   3714 N NZ  . LYS   B 1 207 ? -4.749  9.490   5.053   1.00 80.12  ? 1244 LYS   B NZ  1 
ATOM   3715 N N   . LEU   B 1 208 ? -11.704 7.873   2.040   1.00 68.56  ? 1245 LEU   B N   1 
ATOM   3716 C CA  . LEU   B 1 208 ? -13.144 7.812   1.837   1.00 66.46  ? 1245 LEU   B CA  1 
ATOM   3717 C C   . LEU   B 1 208 ? -13.770 6.882   2.875   1.00 64.11  ? 1245 LEU   B C   1 
ATOM   3718 O O   . LEU   B 1 208 ? -13.112 5.965   3.361   1.00 64.65  ? 1245 LEU   B O   1 
ATOM   3719 C CB  . LEU   B 1 208 ? -13.431 7.305   0.420   1.00 68.49  ? 1245 LEU   B CB  1 
ATOM   3720 C CG  . LEU   B 1 208 ? -13.129 8.282   -0.717  1.00 70.66  ? 1245 LEU   B CG  1 
ATOM   3721 C CD1 . LEU   B 1 208 ? -11.631 8.424   -0.946  1.00 73.57  ? 1245 LEU   B CD1 1 
ATOM   3722 C CD2 . LEU   B 1 208 ? -13.827 7.845   -1.996  1.00 71.95  ? 1245 LEU   B CD2 1 
ATOM   3723 N N   . PRO   B 1 209 ? -15.061 7.084   3.234   1.00 61.77  ? 1246 PRO   B N   1 
ATOM   3724 C CA  . PRO   B 1 209 ? -15.760 6.195   4.165   1.00 60.14  ? 1246 PRO   B CA  1 
ATOM   3725 C C   . PRO   B 1 209 ? -16.256 4.926   3.474   1.00 61.13  ? 1246 PRO   B C   1 
ATOM   3726 O O   . PRO   B 1 209 ? -17.374 4.884   2.965   1.00 60.96  ? 1246 PRO   B O   1 
ATOM   3727 C CB  . PRO   B 1 209 ? -16.917 7.079   4.656   1.00 58.21  ? 1246 PRO   B CB  1 
ATOM   3728 C CG  . PRO   B 1 209 ? -17.244 7.953   3.462   1.00 59.13  ? 1246 PRO   B CG  1 
ATOM   3729 C CD  . PRO   B 1 209 ? -15.917 8.187   2.768   1.00 61.11  ? 1246 PRO   B CD  1 
ATOM   3730 N N   . VAL   B 1 210 ? -15.411 3.887   3.480   1.00 62.42  ? 1247 VAL   B N   1 
ATOM   3731 C CA  . VAL   B 1 210 ? -15.624 2.701   2.664   1.00 64.10  ? 1247 VAL   B CA  1 
ATOM   3732 C C   . VAL   B 1 210 ? -16.779 1.870   3.221   1.00 63.01  ? 1247 VAL   B C   1 
ATOM   3733 O O   . VAL   B 1 210 ? -17.461 1.181   2.465   1.00 64.31  ? 1247 VAL   B O   1 
ATOM   3734 C CB  . VAL   B 1 210 ? -14.338 1.858   2.545   1.00 66.41  ? 1247 VAL   B CB  1 
ATOM   3735 C CG1 . VAL   B 1 210 ? -13.178 2.675   1.995   1.00 67.95  ? 1247 VAL   B CG1 1 
ATOM   3736 C CG2 . VAL   B 1 210 ? -13.952 1.202   3.863   1.00 65.77  ? 1247 VAL   B CG2 1 
ATOM   3737 N N   . LYS   B 1 211 ? -16.994 1.936   4.541   1.00 60.97  ? 1248 LYS   B N   1 
ATOM   3738 C CA  . LYS   B 1 211 ? -17.976 1.090   5.200   1.00 60.40  ? 1248 LYS   B CA  1 
ATOM   3739 C C   . LYS   B 1 211 ? -19.389 1.623   4.963   1.00 59.50  ? 1248 LYS   B C   1 
ATOM   3740 O O   . LYS   B 1 211 ? -20.348 0.856   5.000   1.00 60.09  ? 1248 LYS   B O   1 
ATOM   3741 C CB  . LYS   B 1 211 ? -17.643 0.967   6.689   1.00 59.07  ? 1248 LYS   B CB  1 
ATOM   3742 C CG  . LYS   B 1 211 ? -16.274 0.365   6.978   1.00 60.32  ? 1248 LYS   B CG  1 
ATOM   3743 C CD  . LYS   B 1 211 ? -16.133 -0.209  8.369   1.00 59.78  ? 1248 LYS   B CD  1 
ATOM   3744 C CE  . LYS   B 1 211 ? -14.808 -0.910  8.584   1.00 61.55  ? 1248 LYS   B CE  1 
ATOM   3745 N NZ  . LYS   B 1 211 ? -14.747 -1.576  9.906   1.00 61.34  ? 1248 LYS   B NZ  1 
ATOM   3746 N N   . TRP   B 1 212 ? -19.511 2.933   4.711   1.00 58.48  ? 1249 TRP   B N   1 
ATOM   3747 C CA  . TRP   B 1 212 ? -20.795 3.545   4.403   1.00 58.12  ? 1249 TRP   B CA  1 
ATOM   3748 C C   . TRP   B 1 212 ? -21.030 3.569   2.893   1.00 59.92  ? 1249 TRP   B C   1 
ATOM   3749 O O   . TRP   B 1 212 ? -22.162 3.754   2.448   1.00 60.40  ? 1249 TRP   B O   1 
ATOM   3750 C CB  . TRP   B 1 212 ? -20.887 4.952   5.009   1.00 56.34  ? 1249 TRP   B CB  1 
ATOM   3751 C CG  . TRP   B 1 212 ? -21.007 4.963   6.502   1.00 54.75  ? 1249 TRP   B CG  1 
ATOM   3752 C CD1 . TRP   B 1 212 ? -22.144 5.158   7.230   1.00 54.05  ? 1249 TRP   B CD1 1 
ATOM   3753 C CD2 . TRP   B 1 212 ? -19.945 4.791   7.459   1.00 53.98  ? 1249 TRP   B CD2 1 
ATOM   3754 N NE1 . TRP   B 1 212 ? -21.868 5.106   8.570   1.00 52.90  ? 1249 TRP   B NE1 1 
ATOM   3755 C CE2 . TRP   B 1 212 ? -20.527 4.885   8.741   1.00 52.77  ? 1249 TRP   B CE2 1 
ATOM   3756 C CE3 . TRP   B 1 212 ? -18.566 4.564   7.360   1.00 54.56  ? 1249 TRP   B CE3 1 
ATOM   3757 C CZ2 . TRP   B 1 212 ? -19.776 4.759   9.910   1.00 52.02  ? 1249 TRP   B CZ2 1 
ATOM   3758 C CZ3 . TRP   B 1 212 ? -17.825 4.439   8.516   1.00 53.89  ? 1249 TRP   B CZ3 1 
ATOM   3759 C CH2 . TRP   B 1 212 ? -18.425 4.535   9.772   1.00 52.58  ? 1249 TRP   B CH2 1 
ATOM   3760 N N   . MET   B 1 213 ? -19.956 3.380   2.114   1.00 61.23  ? 1250 MET   B N   1 
ATOM   3761 C CA  . MET   B 1 213 ? -20.020 3.443   0.662   1.00 63.02  ? 1250 MET   B CA  1 
ATOM   3762 C C   . MET   B 1 213 ? -20.723 2.201   0.118   1.00 64.81  ? 1250 MET   B C   1 
ATOM   3763 O O   . MET   B 1 213 ? -20.674 1.135   0.729   1.00 65.06  ? 1250 MET   B O   1 
ATOM   3764 C CB  . MET   B 1 213 ? -18.613 3.534   0.059   1.00 64.20  ? 1250 MET   B CB  1 
ATOM   3765 C CG  . MET   B 1 213 ? -18.121 4.957   -0.117  1.00 63.59  ? 1250 MET   B CG  1 
ATOM   3766 S SD  . MET   B 1 213 ? -16.318 5.049   -0.249  1.00 64.93  ? 1250 MET   B SD  1 
ATOM   3767 C CE  . MET   B 1 213 ? -16.099 4.852   -2.016  1.00 68.20  ? 1250 MET   B CE  1 
ATOM   3768 N N   . ALA   B 1 214 ? -21.368 2.364   -1.044  1.00 66.34  ? 1251 ALA   B N   1 
ATOM   3769 C CA  . ALA   B 1 214 ? -22.056 1.277   -1.720  1.00 68.52  ? 1251 ALA   B CA  1 
ATOM   3770 C C   . ALA   B 1 214 ? -21.054 0.464   -2.537  1.00 70.92  ? 1251 ALA   B C   1 
ATOM   3771 O O   . ALA   B 1 214 ? -19.923 0.897   -2.748  1.00 71.07  ? 1251 ALA   B O   1 
ATOM   3772 C CB  . ALA   B 1 214 ? -23.156 1.830   -2.592  1.00 69.32  ? 1251 ALA   B CB  1 
ATOM   3773 N N   . LEU   B 1 215 ? -21.499 -0.707  -3.005  1.00 73.25  ? 1252 LEU   B N   1 
ATOM   3774 C CA  . LEU   B 1 215 ? -20.653 -1.637  -3.738  1.00 76.05  ? 1252 LEU   B CA  1 
ATOM   3775 C C   . LEU   B 1 215 ? -20.172 -1.002  -5.043  1.00 77.70  ? 1252 LEU   B C   1 
ATOM   3776 O O   . LEU   B 1 215 ? -19.080 -1.312  -5.516  1.00 79.41  ? 1252 LEU   B O   1 
ATOM   3777 C CB  . LEU   B 1 215 ? -21.448 -2.922  -4.000  1.00 78.32  ? 1252 LEU   B CB  1 
ATOM   3778 C CG  . LEU   B 1 215 ? -20.659 -4.083  -4.605  1.00 81.48  ? 1252 LEU   B CG  1 
ATOM   3779 C CD1 . LEU   B 1 215 ? -19.610 -4.598  -3.630  1.00 81.06  ? 1252 LEU   B CD1 1 
ATOM   3780 C CD2 . LEU   B 1 215 ? -21.593 -5.209  -5.022  1.00 84.06  ? 1252 LEU   B CD2 1 
ATOM   3781 N N   . GLU   B 1 216 ? -20.996 -0.113  -5.615  1.00 77.49  ? 1253 GLU   B N   1 
ATOM   3782 C CA  . GLU   B 1 216 ? -20.624 0.631   -6.808  1.00 79.05  ? 1253 GLU   B CA  1 
ATOM   3783 C C   . GLU   B 1 216 ? -19.511 1.617   -6.464  1.00 77.98  ? 1253 GLU   B C   1 
ATOM   3784 O O   . GLU   B 1 216 ? -18.507 1.692   -7.167  1.00 79.94  ? 1253 GLU   B O   1 
ATOM   3785 C CB  . GLU   B 1 216 ? -21.812 1.405   -7.386  1.00 79.02  ? 1253 GLU   B CB  1 
ATOM   3786 C CG  . GLU   B 1 216 ? -22.994 0.535   -7.777  1.00 80.68  ? 1253 GLU   B CG  1 
ATOM   3787 C CD  . GLU   B 1 216 ? -23.955 0.223   -6.644  1.00 79.11  ? 1253 GLU   B CD  1 
ATOM   3788 O OE1 . GLU   B 1 216 ? -24.114 -0.969  -6.318  1.00 80.17  ? 1253 GLU   B OE1 1 
ATOM   3789 O OE2 . GLU   B 1 216 ? -24.539 1.176   -6.088  1.00 77.17  ? 1253 GLU   B OE2 1 
ATOM   3790 N N   . SER   B 1 217 ? -19.713 2.365   -5.372  1.00 75.25  ? 1254 SER   B N   1 
ATOM   3791 C CA  . SER   B 1 217 ? -18.815 3.436   -4.973  1.00 74.25  ? 1254 SER   B CA  1 
ATOM   3792 C C   . SER   B 1 217 ? -17.409 2.901   -4.705  1.00 75.34  ? 1254 SER   B C   1 
ATOM   3793 O O   . SER   B 1 217 ? -16.425 3.564   -5.024  1.00 76.32  ? 1254 SER   B O   1 
ATOM   3794 C CB  . SER   B 1 217 ? -19.358 4.169   -3.773  1.00 71.33  ? 1254 SER   B CB  1 
ATOM   3795 O OG  . SER   B 1 217 ? -20.623 4.747   -4.061  1.00 70.89  ? 1254 SER   B OG  1 
ATOM   3796 N N   . LEU   B 1 218 ? -17.325 1.704   -4.112  1.00 75.59  ? 1255 LEU   B N   1 
ATOM   3797 C CA  . LEU   B 1 218 ? -16.044 1.091   -3.793  1.00 77.09  ? 1255 LEU   B CA  1 
ATOM   3798 C C   . LEU   B 1 218 ? -15.271 0.785   -5.075  1.00 80.91  ? 1255 LEU   B C   1 
ATOM   3799 O O   . LEU   B 1 218 ? -14.062 1.000   -5.133  1.00 82.36  ? 1255 LEU   B O   1 
ATOM   3800 C CB  . LEU   B 1 218 ? -16.286 -0.183  -2.976  1.00 76.80  ? 1255 LEU   B CB  1 
ATOM   3801 C CG  . LEU   B 1 218 ? -16.845 0.027   -1.569  1.00 73.62  ? 1255 LEU   B CG  1 
ATOM   3802 C CD1 . LEU   B 1 218 ? -16.948 -1.296  -0.825  1.00 74.09  ? 1255 LEU   B CD1 1 
ATOM   3803 C CD2 . LEU   B 1 218 ? -15.996 1.013   -0.780  1.00 72.01  ? 1255 LEU   B CD2 1 
ATOM   3804 N N   . GLN   B 1 219 ? -15.981 0.290   -6.097  1.00 82.94  ? 1256 GLN   B N   1 
ATOM   3805 C CA  . GLN   B 1 219 ? -15.358 -0.124  -7.344  1.00 86.97  ? 1256 GLN   B CA  1 
ATOM   3806 C C   . GLN   B 1 219 ? -15.323 1.047   -8.325  1.00 88.04  ? 1256 GLN   B C   1 
ATOM   3807 O O   . GLN   B 1 219 ? -14.249 1.525   -8.684  1.00 89.80  ? 1256 GLN   B O   1 
ATOM   3808 C CB  . GLN   B 1 219 ? -16.110 -1.319  -7.934  1.00 88.78  ? 1256 GLN   B CB  1 
ATOM   3809 C CG  . GLN   B 1 219 ? -16.045 -2.566  -7.062  1.00 88.83  ? 1256 GLN   B CG  1 
ATOM   3810 C CD  . GLN   B 1 219 ? -16.755 -3.748  -7.678  1.00 91.14  ? 1256 GLN   B CD  1 
ATOM   3811 O OE1 . GLN   B 1 219 ? -17.334 -3.661  -8.759  1.00 92.72  ? 1256 GLN   B OE1 1 
ATOM   3812 N NE2 . GLN   B 1 219 ? -16.714 -4.874  -6.984  1.00 91.62  ? 1256 GLN   B NE2 1 
ATOM   3813 N N   . THR   B 1 220 ? -16.510 1.506   -8.742  1.00 87.41  ? 1257 THR   B N   1 
ATOM   3814 C CA  . THR   B 1 220 ? -16.643 2.458   -9.834  1.00 89.08  ? 1257 THR   B CA  1 
ATOM   3815 C C   . THR   B 1 220 ? -16.429 3.889   -9.343  1.00 87.41  ? 1257 THR   B C   1 
ATOM   3816 O O   . THR   B 1 220 ? -15.931 4.725   -10.093 1.00 89.12  ? 1257 THR   B O   1 
ATOM   3817 C CB  . THR   B 1 220 ? -18.015 2.325   -10.509 1.00 89.29  ? 1257 THR   B CB  1 
ATOM   3818 O OG1 . THR   B 1 220 ? -19.021 2.683   -9.561  1.00 86.05  ? 1257 THR   B OG1 1 
ATOM   3819 C CG2 . THR   B 1 220 ? -18.281 0.930   -11.032 1.00 91.61  ? 1257 THR   B CG2 1 
ATOM   3820 N N   . GLN   B 1 221 ? -16.821 4.155   -8.089  1.00 84.58  ? 1258 GLN   B N   1 
ATOM   3821 C CA  . GLN   B 1 221 ? -16.828 5.494   -7.515  1.00 82.93  ? 1258 GLN   B CA  1 
ATOM   3822 C C   . GLN   B 1 221 ? -17.903 6.338   -8.199  1.00 83.12  ? 1258 GLN   B C   1 
ATOM   3823 O O   . GLN   B 1 221 ? -17.698 7.522   -8.461  1.00 83.36  ? 1258 GLN   B O   1 
ATOM   3824 C CB  . GLN   B 1 221 ? -15.448 6.154   -7.601  1.00 84.47  ? 1258 GLN   B CB  1 
ATOM   3825 C CG  . GLN   B 1 221 ? -14.332 5.321   -6.987  1.00 85.25  ? 1258 GLN   B CG  1 
ATOM   3826 C CD  . GLN   B 1 221 ? -13.002 6.036   -7.000  1.00 87.16  ? 1258 GLN   B CD  1 
ATOM   3827 O OE1 . GLN   B 1 221 ? -12.892 7.182   -7.430  1.00 87.93  ? 1258 GLN   B OE1 1 
ATOM   3828 N NE2 . GLN   B 1 221 ? -11.973 5.356   -6.520  1.00 88.46  ? 1258 GLN   B NE2 1 
ATOM   3829 N N   . LYS   B 1 222 ? -19.050 5.706   -8.480  1.00 83.44  ? 1259 LYS   B N   1 
ATOM   3830 C CA  . LYS   B 1 222 ? -20.245 6.404   -8.924  1.00 83.55  ? 1259 LYS   B CA  1 
ATOM   3831 C C   . LYS   B 1 222 ? -21.134 6.647   -7.708  1.00 80.83  ? 1259 LYS   B C   1 
ATOM   3832 O O   . LYS   B 1 222 ? -21.333 5.742   -6.899  1.00 79.65  ? 1259 LYS   B O   1 
ATOM   3833 C CB  . LYS   B 1 222 ? -20.987 5.584   -9.984  1.00 85.87  ? 1259 LYS   B CB  1 
ATOM   3834 C CG  . LYS   B 1 222 ? -20.215 5.333   -11.273 1.00 89.23  ? 1259 LYS   B CG  1 
ATOM   3835 C CD  . LYS   B 1 222 ? -20.948 4.430   -12.244 1.00 91.63  ? 1259 LYS   B CD  1 
ATOM   3836 C CE  . LYS   B 1 222 ? -20.161 4.140   -13.505 1.00 95.25  ? 1259 LYS   B CE  1 
ATOM   3837 N NZ  . LYS   B 1 222 ? -19.912 5.369   -14.296 1.00 96.58  ? 1259 LYS   B NZ  1 
ATOM   3838 N N   . PHE   B 1 223 ? -21.659 7.872   -7.588  1.00 80.27  ? 1260 PHE   B N   1 
ATOM   3839 C CA  . PHE   B 1 223 ? -22.445 8.263   -6.430  1.00 78.14  ? 1260 PHE   B CA  1 
ATOM   3840 C C   . PHE   B 1 223 ? -23.786 8.830   -6.888  1.00 79.09  ? 1260 PHE   B C   1 
ATOM   3841 O O   . PHE   B 1 223 ? -23.831 9.728   -7.726  1.00 80.66  ? 1260 PHE   B O   1 
ATOM   3842 C CB  . PHE   B 1 223 ? -21.674 9.268   -5.572  1.00 76.56  ? 1260 PHE   B CB  1 
ATOM   3843 C CG  . PHE   B 1 223 ? -20.377 8.743   -5.008  1.00 76.09  ? 1260 PHE   B CG  1 
ATOM   3844 C CD1 . PHE   B 1 223 ? -19.255 8.603   -5.813  1.00 78.11  ? 1260 PHE   B CD1 1 
ATOM   3845 C CD2 . PHE   B 1 223 ? -20.283 8.366   -3.677  1.00 73.94  ? 1260 PHE   B CD2 1 
ATOM   3846 C CE1 . PHE   B 1 223 ? -18.067 8.113   -5.294  1.00 78.11  ? 1260 PHE   B CE1 1 
ATOM   3847 C CE2 . PHE   B 1 223 ? -19.094 7.876   -3.160  1.00 73.75  ? 1260 PHE   B CE2 1 
ATOM   3848 C CZ  . PHE   B 1 223 ? -17.988 7.750   -3.970  1.00 75.88  ? 1260 PHE   B CZ  1 
ATOM   3849 N N   . THR   B 1 224 ? -24.869 8.285   -6.321  1.00 78.64  ? 1261 THR   B N   1 
ATOM   3850 C CA  . THR   B 1 224 ? -26.227 8.686   -6.651  1.00 79.85  ? 1261 THR   B CA  1 
ATOM   3851 C C   . THR   B 1 224 ? -27.069 8.654   -5.376  1.00 78.46  ? 1261 THR   B C   1 
ATOM   3852 O O   . THR   B 1 224 ? -26.533 8.496   -4.282  1.00 76.40  ? 1261 THR   B O   1 
ATOM   3853 C CB  . THR   B 1 224 ? -26.796 7.785   -7.757  1.00 82.36  ? 1261 THR   B CB  1 
ATOM   3854 O OG1 . THR   B 1 224 ? -26.730 6.433   -7.301  1.00 82.01  ? 1261 THR   B OG1 1 
ATOM   3855 C CG2 . THR   B 1 224 ? -26.056 7.915   -9.070  1.00 84.29  ? 1261 THR   B CG2 1 
ATOM   3856 N N   . THR   B 1 225 ? -28.389 8.820   -5.529  1.00 76.97  ? 1262 THR   B N   1 
ATOM   3857 C CA  . THR   B 1 225 ? -29.331 8.640   -4.435  1.00 75.36  ? 1262 THR   B CA  1 
ATOM   3858 C C   . THR   B 1 225 ? -29.276 7.198   -3.931  1.00 72.98  ? 1262 THR   B C   1 
ATOM   3859 O O   . THR   B 1 225 ? -29.473 6.950   -2.744  1.00 70.05  ? 1262 THR   B O   1 
ATOM   3860 C CB  . THR   B 1 225 ? -30.753 9.017   -4.871  1.00 79.03  ? 1262 THR   B CB  1 
ATOM   3861 O OG1 . THR   B 1 225 ? -30.718 10.347  -5.389  1.00 81.87  ? 1262 THR   B OG1 1 
ATOM   3862 C CG2 . THR   B 1 225 ? -31.766 8.939   -3.749  1.00 77.79  ? 1262 THR   B CG2 1 
ATOM   3863 N N   . LYS   B 1 226 ? -29.006 6.259   -4.848  1.00 74.73  ? 1263 LYS   B N   1 
ATOM   3864 C CA  . LYS   B 1 226 ? -28.980 4.837   -4.539  1.00 73.35  ? 1263 LYS   B CA  1 
ATOM   3865 C C   . LYS   B 1 226 ? -27.810 4.515   -3.610  1.00 69.36  ? 1263 LYS   B C   1 
ATOM   3866 O O   . LYS   B 1 226 ? -27.929 3.647   -2.747  1.00 66.97  ? 1263 LYS   B O   1 
ATOM   3867 C CB  . LYS   B 1 226 ? -28.883 4.010   -5.826  1.00 76.56  ? 1263 LYS   B CB  1 
ATOM   3868 C CG  . LYS   B 1 226 ? -29.987 4.249   -6.851  1.00 81.37  ? 1263 LYS   B CG  1 
ATOM   3869 C CD  . LYS   B 1 226 ? -31.386 4.013   -6.321  1.00 82.16  ? 1263 LYS   B CD  1 
ATOM   3870 C CE  . LYS   B 1 226 ? -32.455 4.177   -7.380  1.00 87.51  ? 1263 LYS   B CE  1 
ATOM   3871 N NZ  . LYS   B 1 226 ? -33.808 3.925   -6.833  1.00 88.67  ? 1263 LYS   B NZ  1 
ATOM   3872 N N   . SER   B 1 227 ? -26.680 5.208   -3.802  1.00 69.01  ? 1264 SER   B N   1 
ATOM   3873 C CA  . SER   B 1 227 ? -25.514 5.035   -2.950  1.00 65.74  ? 1264 SER   B CA  1 
ATOM   3874 C C   . SER   B 1 227 ? -25.779 5.625   -1.565  1.00 63.30  ? 1264 SER   B C   1 
ATOM   3875 O O   . SER   B 1 227 ? -25.243 5.136   -0.573  1.00 60.55  ? 1264 SER   B O   1 
ATOM   3876 C CB  . SER   B 1 227 ? -24.283 5.641   -3.578  1.00 66.76  ? 1264 SER   B CB  1 
ATOM   3877 O OG  . SER   B 1 227 ? -24.427 7.045   -3.736  1.00 68.56  ? 1264 SER   B OG  1 
ATOM   3878 N N   . ASP   B 1 228 ? -26.602 6.681   -1.514  1.00 64.78  ? 1265 ASP   B N   1 
ATOM   3879 C CA  . ASP   B 1 228 ? -26.995 7.306   -0.260  1.00 63.24  ? 1265 ASP   B CA  1 
ATOM   3880 C C   . ASP   B 1 228 ? -27.989 6.411   0.479   1.00 62.34  ? 1265 ASP   B C   1 
ATOM   3881 O O   . ASP   B 1 228 ? -28.003 6.392   1.708   1.00 60.16  ? 1265 ASP   B O   1 
ATOM   3882 C CB  . ASP   B 1 228 ? -27.576 8.704   -0.492  1.00 65.65  ? 1265 ASP   B CB  1 
ATOM   3883 C CG  . ASP   B 1 228 ? -26.568 9.720   -1.004  1.00 66.72  ? 1265 ASP   B CG  1 
ATOM   3884 O OD1 . ASP   B 1 228 ? -25.389 9.347   -1.178  1.00 65.50  ? 1265 ASP   B OD1 1 
ATOM   3885 O OD2 . ASP   B 1 228 ? -26.971 10.880  -1.222  1.00 68.96  ? 1265 ASP   B OD2 1 
ATOM   3886 N N   . VAL   B 1 229 ? -28.824 5.685   -0.277  1.00 64.49  ? 1266 VAL   B N   1 
ATOM   3887 C CA  . VAL   B 1 229 ? -29.755 4.728   0.299   1.00 64.48  ? 1266 VAL   B CA  1 
ATOM   3888 C C   . VAL   B 1 229 ? -28.961 3.626   1.000   1.00 61.75  ? 1266 VAL   B C   1 
ATOM   3889 O O   . VAL   B 1 229 ? -29.292 3.242   2.119   1.00 60.48  ? 1266 VAL   B O   1 
ATOM   3890 C CB  . VAL   B 1 229 ? -30.712 4.153   -0.767  1.00 67.84  ? 1266 VAL   B CB  1 
ATOM   3891 C CG1 . VAL   B 1 229 ? -31.504 2.962   -0.244  1.00 68.14  ? 1266 VAL   B CG1 1 
ATOM   3892 C CG2 . VAL   B 1 229 ? -31.649 5.219   -1.317  1.00 71.05  ? 1266 VAL   B CG2 1 
ATOM   3893 N N   . TRP   B 1 230 ? -27.915 3.127   0.329   1.00 61.38  ? 1267 TRP   B N   1 
ATOM   3894 C CA  . TRP   B 1 230 ? -27.011 2.149   0.914   1.00 59.07  ? 1267 TRP   B CA  1 
ATOM   3895 C C   . TRP   B 1 230 ? -26.416 2.705   2.205   1.00 56.33  ? 1267 TRP   B C   1 
ATOM   3896 O O   . TRP   B 1 230 ? -26.386 2.016   3.223   1.00 54.69  ? 1267 TRP   B O   1 
ATOM   3897 C CB  . TRP   B 1 230 ? -25.917 1.760   -0.091  1.00 59.80  ? 1267 TRP   B CB  1 
ATOM   3898 C CG  . TRP   B 1 230 ? -24.943 0.737   0.413   1.00 58.10  ? 1267 TRP   B CG  1 
ATOM   3899 C CD1 . TRP   B 1 230 ? -24.007 0.897   1.395   1.00 55.71  ? 1267 TRP   B CD1 1 
ATOM   3900 C CD2 . TRP   B 1 230 ? -24.808 -0.619  -0.047  1.00 59.12  ? 1267 TRP   B CD2 1 
ATOM   3901 N NE1 . TRP   B 1 230 ? -23.302 -0.262  1.577   1.00 54.98  ? 1267 TRP   B NE1 1 
ATOM   3902 C CE2 . TRP   B 1 230 ? -23.771 -1.210  0.706   1.00 56.95  ? 1267 TRP   B CE2 1 
ATOM   3903 C CE3 . TRP   B 1 230 ? -25.458 -1.389  -1.019  1.00 61.92  ? 1267 TRP   B CE3 1 
ATOM   3904 C CZ2 . TRP   B 1 230 ? -23.375 -2.534  0.515   1.00 57.44  ? 1267 TRP   B CZ2 1 
ATOM   3905 C CZ3 . TRP   B 1 230 ? -25.067 -2.697  -1.207  1.00 62.46  ? 1267 TRP   B CZ3 1 
ATOM   3906 C CH2 . TRP   B 1 230 ? -24.039 -3.259  -0.449  1.00 60.26  ? 1267 TRP   B CH2 1 
ATOM   3907 N N   . SER   B 1 231 ? -25.946 3.957   2.142   1.00 56.21  ? 1268 SER   B N   1 
ATOM   3908 C CA  . SER   B 1 231 ? -25.337 4.627   3.280   1.00 54.29  ? 1268 SER   B CA  1 
ATOM   3909 C C   . SER   B 1 231 ? -26.359 4.820   4.399   1.00 54.21  ? 1268 SER   B C   1 
ATOM   3910 O O   . SER   B 1 231 ? -26.010 4.744   5.575   1.00 52.60  ? 1268 SER   B O   1 
ATOM   3911 C CB  . SER   B 1 231 ? -24.727 5.939   2.862   1.00 55.11  ? 1268 SER   B CB  1 
ATOM   3912 O OG  . SER   B 1 231 ? -23.768 5.748   1.832   1.00 55.62  ? 1268 SER   B OG  1 
ATOM   3913 N N   . PHE   B 1 232 ? -27.618 5.076   4.018   1.00 56.42  ? 1269 PHE   B N   1 
ATOM   3914 C CA  . PHE   B 1 232 ? -28.707 5.218   4.972   1.00 57.20  ? 1269 PHE   B CA  1 
ATOM   3915 C C   . PHE   B 1 232 ? -28.973 3.883   5.667   1.00 56.41  ? 1269 PHE   B C   1 
ATOM   3916 O O   . PHE   B 1 232 ? -29.305 3.858   6.850   1.00 56.23  ? 1269 PHE   B O   1 
ATOM   3917 C CB  . PHE   B 1 232 ? -29.972 5.734   4.281   1.00 60.13  ? 1269 PHE   B CB  1 
ATOM   3918 C CG  . PHE   B 1 232 ? -31.174 5.845   5.185   1.00 61.44  ? 1269 PHE   B CG  1 
ATOM   3919 C CD1 . PHE   B 1 232 ? -31.188 6.746   6.239   1.00 61.26  ? 1269 PHE   B CD1 1 
ATOM   3920 C CD2 . PHE   B 1 232 ? -32.282 5.033   4.996   1.00 63.42  ? 1269 PHE   B CD2 1 
ATOM   3921 C CE1 . PHE   B 1 232 ? -32.291 6.841   7.074   1.00 63.02  ? 1269 PHE   B CE1 1 
ATOM   3922 C CE2 . PHE   B 1 232 ? -33.384 5.129   5.832   1.00 65.13  ? 1269 PHE   B CE2 1 
ATOM   3923 C CZ  . PHE   B 1 232 ? -33.386 6.033   6.870   1.00 64.96  ? 1269 PHE   B CZ  1 
ATOM   3924 N N   . GLY   B 1 233 ? -28.841 2.781   4.920   1.00 56.52  ? 1270 GLY   B N   1 
ATOM   3925 C CA  . GLY   B 1 233 ? -28.936 1.448   5.491   1.00 56.08  ? 1270 GLY   B CA  1 
ATOM   3926 C C   . GLY   B 1 233 ? -27.963 1.259   6.653   1.00 53.85  ? 1270 GLY   B C   1 
ATOM   3927 O O   . GLY   B 1 233 ? -28.333 0.720   7.694   1.00 53.68  ? 1270 GLY   B O   1 
ATOM   3928 N N   . VAL   B 1 234 ? -26.724 1.729   6.462   1.00 52.47  ? 1271 VAL   B N   1 
ATOM   3929 C CA  . VAL   B 1 234 ? -25.676 1.614   7.465   1.00 50.66  ? 1271 VAL   B CA  1 
ATOM   3930 C C   . VAL   B 1 234 ? -26.011 2.515   8.653   1.00 50.76  ? 1271 VAL   B C   1 
ATOM   3931 O O   . VAL   B 1 234 ? -25.727 2.164   9.796   1.00 50.16  ? 1271 VAL   B O   1 
ATOM   3932 C CB  . VAL   B 1 234 ? -24.293 1.954   6.872   1.00 49.78  ? 1271 VAL   B CB  1 
ATOM   3933 C CG1 . VAL   B 1 234 ? -23.194 1.891   7.925   1.00 48.44  ? 1271 VAL   B CG1 1 
ATOM   3934 C CG2 . VAL   B 1 234 ? -23.951 1.062   5.687   1.00 50.19  ? 1271 VAL   B CG2 1 
ATOM   3935 N N   . LEU   B 1 235 ? -26.612 3.678   8.369   1.00 51.85  ? 1272 LEU   B N   1 
ATOM   3936 C CA  . LEU   B 1 235 ? -26.994 4.633   9.398   1.00 52.49  ? 1272 LEU   B CA  1 
ATOM   3937 C C   . LEU   B 1 235 ? -28.049 4.015   10.316  1.00 53.56  ? 1272 LEU   B C   1 
ATOM   3938 O O   . LEU   B 1 235 ? -27.994 4.200   11.530  1.00 53.75  ? 1272 LEU   B O   1 
ATOM   3939 C CB  . LEU   B 1 235 ? -27.501 5.910   8.718   1.00 53.96  ? 1272 LEU   B CB  1 
ATOM   3940 C CG  . LEU   B 1 235 ? -27.696 7.129   9.621   1.00 55.07  ? 1272 LEU   B CG  1 
ATOM   3941 C CD1 . LEU   B 1 235 ? -27.744 8.403   8.791   1.00 56.45  ? 1272 LEU   B CD1 1 
ATOM   3942 C CD2 . LEU   B 1 235 ? -28.956 7.001   10.470  1.00 56.71  ? 1272 LEU   B CD2 1 
ATOM   3943 N N   . LEU   B 1 236 ? -29.000 3.275   9.731   1.00 54.60  ? 1273 LEU   B N   1 
ATOM   3944 C CA  . LEU   B 1 236 ? -30.033 2.595   10.499  1.00 56.12  ? 1273 LEU   B CA  1 
ATOM   3945 C C   . LEU   B 1 236 ? -29.404 1.549   11.418  1.00 54.98  ? 1273 LEU   B C   1 
ATOM   3946 O O   . LEU   B 1 236 ? -29.855 1.370   12.547  1.00 56.12  ? 1273 LEU   B O   1 
ATOM   3947 C CB  . LEU   B 1 236 ? -31.039 1.946   9.542   1.00 57.96  ? 1273 LEU   B CB  1 
ATOM   3948 C CG  . LEU   B 1 236 ? -32.015 2.896   8.848   1.00 60.16  ? 1273 LEU   B CG  1 
ATOM   3949 C CD1 . LEU   B 1 236 ? -32.956 2.127   7.933   1.00 62.41  ? 1273 LEU   B CD1 1 
ATOM   3950 C CD2 . LEU   B 1 236 ? -32.809 3.705   9.865   1.00 61.95  ? 1273 LEU   B CD2 1 
ATOM   3951 N N   . TRP   B 1 237 ? -28.369 0.861   10.920  1.00 53.11  ? 1274 TRP   B N   1 
ATOM   3952 C CA  . TRP   B 1 237 ? -27.673 -0.160  11.688  1.00 52.23  ? 1274 TRP   B CA  1 
ATOM   3953 C C   . TRP   B 1 237 ? -27.016 0.461   12.919  1.00 51.93  ? 1274 TRP   B C   1 
ATOM   3954 O O   . TRP   B 1 237 ? -27.033 -0.134  13.995  1.00 52.54  ? 1274 TRP   B O   1 
ATOM   3955 C CB  . TRP   B 1 237 ? -26.642 -0.887  10.816  1.00 50.49  ? 1274 TRP   B CB  1 
ATOM   3956 C CG  . TRP   B 1 237 ? -26.050 -2.099  11.467  1.00 50.03  ? 1274 TRP   B CG  1 
ATOM   3957 C CD1 . TRP   B 1 237 ? -26.588 -3.353  11.516  1.00 51.28  ? 1274 TRP   B CD1 1 
ATOM   3958 C CD2 . TRP   B 1 237 ? -24.815 -2.164  12.203  1.00 48.73  ? 1274 TRP   B CD2 1 
ATOM   3959 N NE1 . TRP   B 1 237 ? -25.763 -4.197  12.210  1.00 50.80  ? 1274 TRP   B NE1 1 
ATOM   3960 C CE2 . TRP   B 1 237 ? -24.669 -3.497  12.645  1.00 49.24  ? 1274 TRP   B CE2 1 
ATOM   3961 C CE3 . TRP   B 1 237 ? -23.817 -1.236  12.521  1.00 47.60  ? 1274 TRP   B CE3 1 
ATOM   3962 C CZ2 . TRP   B 1 237 ? -23.567 -3.918  13.388  1.00 48.61  ? 1274 TRP   B CZ2 1 
ATOM   3963 C CZ3 . TRP   B 1 237 ? -22.729 -1.652  13.257  1.00 47.08  ? 1274 TRP   B CZ3 1 
ATOM   3964 C CH2 . TRP   B 1 237 ? -22.607 -2.976  13.682  1.00 47.56  ? 1274 TRP   B CH2 1 
ATOM   3965 N N   . GLU   B 1 238 ? -26.432 1.654   12.743  1.00 51.37  ? 1275 GLU   B N   1 
ATOM   3966 C CA  . GLU   B 1 238 ? -25.786 2.376   13.829  1.00 51.64  ? 1275 GLU   B CA  1 
ATOM   3967 C C   . GLU   B 1 238 ? -26.800 2.686   14.928  1.00 54.07  ? 1275 GLU   B C   1 
ATOM   3968 O O   . GLU   B 1 238 ? -26.535 2.440   16.103  1.00 54.73  ? 1275 GLU   B O   1 
ATOM   3969 C CB  . GLU   B 1 238 ? -25.152 3.672   13.319  1.00 51.24  ? 1275 GLU   B CB  1 
ATOM   3970 C CG  . GLU   B 1 238 ? -23.918 3.461   12.460  1.00 49.52  ? 1275 GLU   B CG  1 
ATOM   3971 C CD  . GLU   B 1 238 ? -23.274 4.749   11.975  1.00 49.55  ? 1275 GLU   B CD  1 
ATOM   3972 O OE1 . GLU   B 1 238 ? -22.125 5.022   12.375  1.00 49.02  ? 1275 GLU   B OE1 1 
ATOM   3973 O OE2 . GLU   B 1 238 ? -23.926 5.479   11.202  1.00 50.34  ? 1275 GLU   B OE2 1 
ATOM   3974 N N   . LEU   B 1 239 ? -27.956 3.230   14.530  1.00 55.76  ? 1276 LEU   B N   1 
ATOM   3975 C CA  . LEU   B 1 239 ? -29.001 3.622   15.464  1.00 58.65  ? 1276 LEU   B CA  1 
ATOM   3976 C C   . LEU   B 1 239 ? -29.402 2.438   16.341  1.00 60.16  ? 1276 LEU   B C   1 
ATOM   3977 O O   . LEU   B 1 239 ? -29.479 2.571   17.561  1.00 62.18  ? 1276 LEU   B O   1 
ATOM   3978 C CB  . LEU   B 1 239 ? -30.204 4.150   14.676  1.00 60.28  ? 1276 LEU   B CB  1 
ATOM   3979 C CG  . LEU   B 1 239 ? -30.015 5.511   14.007  1.00 60.22  ? 1276 LEU   B CG  1 
ATOM   3980 C CD1 . LEU   B 1 239 ? -31.254 5.907   13.218  1.00 62.19  ? 1276 LEU   B CD1 1 
ATOM   3981 C CD2 . LEU   B 1 239 ? -29.677 6.581   15.036  1.00 61.34  ? 1276 LEU   B CD2 1 
ATOM   3982 N N   . MET   B 1 240 ? -29.639 1.282   15.708  1.00 59.77  ? 1277 MET   B N   1 
ATOM   3983 C CA  . MET   B 1 240 ? -30.178 0.114   16.389  1.00 61.55  ? 1277 MET   B CA  1 
ATOM   3984 C C   . MET   B 1 240 ? -29.129 -0.509  17.311  1.00 60.73  ? 1277 MET   B C   1 
ATOM   3985 O O   . MET   B 1 240 ? -29.486 -1.197  18.265  1.00 62.89  ? 1277 MET   B O   1 
ATOM   3986 C CB  . MET   B 1 240 ? -30.644 -0.936  15.375  1.00 61.80  ? 1277 MET   B CB  1 
ATOM   3987 C CG  . MET   B 1 240 ? -31.920 -0.558  14.636  1.00 63.80  ? 1277 MET   B CG  1 
ATOM   3988 S SD  . MET   B 1 240 ? -33.344 -0.296  15.728  1.00 68.19  ? 1277 MET   B SD  1 
ATOM   3989 C CE  . MET   B 1 240 ? -33.329 1.491   15.873  1.00 67.97  ? 1277 MET   B CE  1 
ATOM   3990 N N   . THR   B 1 241 ? -27.843 -0.266  17.019  1.00 57.99  ? 1278 THR   B N   1 
ATOM   3991 C CA  . THR   B 1 241 ? -26.744 -0.813  17.801  1.00 57.25  ? 1278 THR   B CA  1 
ATOM   3992 C C   . THR   B 1 241 ? -26.204 0.227   18.785  1.00 57.74  ? 1278 THR   B C   1 
ATOM   3993 O O   . THR   B 1 241 ? -25.210 -0.029  19.461  1.00 57.35  ? 1278 THR   B O   1 
ATOM   3994 C CB  . THR   B 1 241 ? -25.625 -1.314  16.878  1.00 54.54  ? 1278 THR   B CB  1 
ATOM   3995 O OG1 . THR   B 1 241 ? -25.211 -0.225  16.053  1.00 52.83  ? 1278 THR   B OG1 1 
ATOM   3996 C CG2 . THR   B 1 241 ? -26.051 -2.478  16.010  1.00 54.44  ? 1278 THR   B CG2 1 
ATOM   3997 N N   . ARG   B 1 242 ? -26.876 1.384   18.871  1.00 58.98  ? 1279 ARG   B N   1 
ATOM   3998 C CA  . ARG   B 1 242 ? -26.424 2.516   19.667  1.00 60.06  ? 1279 ARG   B CA  1 
ATOM   3999 C C   . ARG   B 1 242 ? -24.992 2.885   19.278  1.00 57.47  ? 1279 ARG   B C   1 
ATOM   4000 O O   . ARG   B 1 242 ? -24.106 2.957   20.128  1.00 57.84  ? 1279 ARG   B O   1 
ATOM   4001 C CB  . ARG   B 1 242 ? -26.568 2.233   21.167  1.00 63.42  ? 1279 ARG   B CB  1 
ATOM   4002 C CG  . ARG   B 1 242 ? -28.006 2.271   21.667  1.00 66.94  ? 1279 ARG   B CG  1 
ATOM   4003 C CD  . ARG   B 1 242 ? -28.092 2.247   23.183  1.00 70.86  ? 1279 ARG   B CD  1 
ATOM   4004 N NE  . ARG   B 1 242 ? -29.435 2.527   23.676  1.00 74.76  ? 1279 ARG   B NE  1 
ATOM   4005 C CZ  . ARG   B 1 242 ? -30.484 1.724   23.524  1.00 76.44  ? 1279 ARG   B CZ  1 
ATOM   4006 N NH1 . ARG   B 1 242 ? -31.677 2.110   23.943  1.00 79.92  ? 1279 ARG   B NH1 1 
ATOM   4007 N NH2 . ARG   B 1 242 ? -30.341 0.539   22.956  1.00 74.89  ? 1279 ARG   B NH2 1 
ATOM   4008 N N   . GLY   B 1 243 ? -24.788 3.112   17.975  1.00 55.04  ? 1280 GLY   B N   1 
ATOM   4009 C CA  . GLY   B 1 243 ? -23.563 3.697   17.458  1.00 53.34  ? 1280 GLY   B CA  1 
ATOM   4010 C C   . GLY   B 1 243 ? -22.380 2.734   17.497  1.00 51.74  ? 1280 GLY   B C   1 
ATOM   4011 O O   . GLY   B 1 243 ? -21.284 3.117   17.899  1.00 52.14  ? 1280 GLY   B O   1 
ATOM   4012 N N   . ALA   B 1 244 ? -22.609 1.489   17.064  1.00 50.40  ? 1281 ALA   B N   1 
ATOM   4013 C CA  . ALA   B 1 244 ? -21.536 0.518   16.925  1.00 49.13  ? 1281 ALA   B CA  1 
ATOM   4014 C C   . ALA   B 1 244 ? -20.809 0.764   15.605  1.00 47.23  ? 1281 ALA   B C   1 
ATOM   4015 O O   . ALA   B 1 244 ? -21.410 1.257   14.652  1.00 46.81  ? 1281 ALA   B O   1 
ATOM   4016 C CB  . ALA   B 1 244 ? -22.092 -0.883  16.997  1.00 49.46  ? 1281 ALA   B CB  1 
ATOM   4017 N N   . PRO   B 1 245 ? -19.499 0.440   15.506  1.00 46.35  ? 1282 PRO   B N   1 
ATOM   4018 C CA  . PRO   B 1 245 ? -18.758 0.606   14.255  1.00 45.16  ? 1282 PRO   B CA  1 
ATOM   4019 C C   . PRO   B 1 245 ? -19.176 -0.436  13.220  1.00 44.32  ? 1282 PRO   B C   1 
ATOM   4020 O O   . PRO   B 1 245 ? -19.046 -1.633  13.469  1.00 44.18  ? 1282 PRO   B O   1 
ATOM   4021 C CB  . PRO   B 1 245 ? -17.294 0.415   14.675  1.00 45.42  ? 1282 PRO   B CB  1 
ATOM   4022 C CG  . PRO   B 1 245 ? -17.371 -0.485  15.890  1.00 46.27  ? 1282 PRO   B CG  1 
ATOM   4023 C CD  . PRO   B 1 245 ? -18.661 -0.103  16.586  1.00 47.12  ? 1282 PRO   B CD  1 
ATOM   4024 N N   . PRO   B 1 246 ? -19.701 -0.025  12.041  1.00 44.25  ? 1283 PRO   B N   1 
ATOM   4025 C CA  . PRO   B 1 246 ? -20.116 -0.976  11.007  1.00 44.33  ? 1283 PRO   B CA  1 
ATOM   4026 C C   . PRO   B 1 246 ? -19.026 -1.985  10.650  1.00 44.23  ? 1283 PRO   B C   1 
ATOM   4027 O O   . PRO   B 1 246 ? -17.842 -1.653  10.669  1.00 43.94  ? 1283 PRO   B O   1 
ATOM   4028 C CB  . PRO   B 1 246 ? -20.434 -0.085  9.797   1.00 44.45  ? 1283 PRO   B CB  1 
ATOM   4029 C CG  . PRO   B 1 246 ? -20.809 1.247   10.408  1.00 44.80  ? 1283 PRO   B CG  1 
ATOM   4030 C CD  . PRO   B 1 246 ? -19.939 1.371   11.641  1.00 44.61  ? 1283 PRO   B CD  1 
ATOM   4031 N N   . TYR   B 1 247 ? -19.451 -3.215  10.335  1.00 44.93  ? 1284 TYR   B N   1 
ATOM   4032 C CA  . TYR   B 1 247 ? -18.548 -4.298  9.981   1.00 45.44  ? 1284 TYR   B CA  1 
ATOM   4033 C C   . TYR   B 1 247 ? -17.489 -4.444  11.074  1.00 45.32  ? 1284 TYR   B C   1 
ATOM   4034 O O   . TYR   B 1 247 ? -16.292 -4.382  10.799  1.00 45.19  ? 1284 TYR   B O   1 
ATOM   4035 C CB  . TYR   B 1 247 ? -17.948 -4.047  8.594   1.00 45.88  ? 1284 TYR   B CB  1 
ATOM   4036 C CG  . TYR   B 1 247 ? -18.972 -3.814  7.511   1.00 46.68  ? 1284 TYR   B CG  1 
ATOM   4037 C CD1 . TYR   B 1 247 ? -19.639 -4.871  6.910   1.00 47.93  ? 1284 TYR   B CD1 1 
ATOM   4038 C CD2 . TYR   B 1 247 ? -19.304 -2.530  7.111   1.00 46.79  ? 1284 TYR   B CD2 1 
ATOM   4039 C CE1 . TYR   B 1 247 ? -20.590 -4.658  5.924   1.00 49.22  ? 1284 TYR   B CE1 1 
ATOM   4040 C CE2 . TYR   B 1 247 ? -20.253 -2.300  6.128   1.00 47.90  ? 1284 TYR   B CE2 1 
ATOM   4041 C CZ  . TYR   B 1 247 ? -20.900 -3.367  5.531   1.00 49.22  ? 1284 TYR   B CZ  1 
ATOM   4042 O OH  . TYR   B 1 247 ? -21.843 -3.135  4.558   1.00 50.78  ? 1284 TYR   B OH  1 
ATOM   4043 N N   . PRO   B 1 248 ? -17.908 -4.645  12.346  1.00 45.83  ? 1285 PRO   B N   1 
ATOM   4044 C CA  . PRO   B 1 248 ? -16.978 -4.675  13.479  1.00 46.39  ? 1285 PRO   B CA  1 
ATOM   4045 C C   . PRO   B 1 248 ? -16.145 -5.949  13.609  1.00 47.37  ? 1285 PRO   B C   1 
ATOM   4046 O O   . PRO   B 1 248 ? -15.216 -5.994  14.414  1.00 48.02  ? 1285 PRO   B O   1 
ATOM   4047 C CB  . PRO   B 1 248 ? -17.911 -4.526  14.692  1.00 47.02  ? 1285 PRO   B CB  1 
ATOM   4048 C CG  . PRO   B 1 248 ? -19.214 -5.152  14.240  1.00 47.30  ? 1285 PRO   B CG  1 
ATOM   4049 C CD  . PRO   B 1 248 ? -19.305 -4.852  12.759  1.00 46.43  ? 1285 PRO   B CD  1 
ATOM   4050 N N   . ASP   B 1 249 ? -16.485 -6.977  12.819  1.00 47.95  ? 1286 ASP   B N   1 
ATOM   4051 C CA  . ASP   B 1 249 ? -15.742 -8.228  12.798  1.00 49.14  ? 1286 ASP   B CA  1 
ATOM   4052 C C   . ASP   B 1 249 ? -15.065 -8.407  11.439  1.00 48.98  ? 1286 ASP   B C   1 
ATOM   4053 O O   . ASP   B 1 249 ? -14.730 -9.528  11.059  1.00 50.18  ? 1286 ASP   B O   1 
ATOM   4054 C CB  . ASP   B 1 249 ? -16.654 -9.416  13.126  1.00 50.66  ? 1286 ASP   B CB  1 
ATOM   4055 C CG  . ASP   B 1 249 ? -17.888 -9.533  12.244  1.00 51.00  ? 1286 ASP   B CG  1 
ATOM   4056 O OD1 . ASP   B 1 249 ? -18.218 -8.545  11.556  1.00 50.16  ? 1286 ASP   B OD1 1 
ATOM   4057 O OD2 . ASP   B 1 249 ? -18.505 -10.616 12.242  1.00 52.65  ? 1286 ASP   B OD2 1 
ATOM   4058 N N   . VAL   B 1 250 ? -14.856 -7.296  10.718  1.00 48.03  ? 1287 VAL   B N   1 
ATOM   4059 C CA  . VAL   B 1 250 ? -14.301 -7.332  9.373   1.00 48.51  ? 1287 VAL   B CA  1 
ATOM   4060 C C   . VAL   B 1 250 ? -13.292 -6.196  9.226   1.00 48.36  ? 1287 VAL   B C   1 
ATOM   4061 O O   . VAL   B 1 250 ? -13.544 -5.076  9.671   1.00 47.33  ? 1287 VAL   B O   1 
ATOM   4062 C CB  . VAL   B 1 250 ? -15.409 -7.236  8.304   1.00 48.44  ? 1287 VAL   B CB  1 
ATOM   4063 C CG1 . VAL   B 1 250 ? -14.836 -7.206  6.893   1.00 49.34  ? 1287 VAL   B CG1 1 
ATOM   4064 C CG2 . VAL   B 1 250 ? -16.435 -8.352  8.442   1.00 49.20  ? 1287 VAL   B CG2 1 
ATOM   4065 N N   . ASN   B 1 251 ? -12.153 -6.502  8.590   1.00 49.69  ? 1288 ASN   B N   1 
ATOM   4066 C CA  . ASN   B 1 251 ? -11.131 -5.510  8.292   1.00 50.31  ? 1288 ASN   B CA  1 
ATOM   4067 C C   . ASN   B 1 251 ? -11.674 -4.518  7.269   1.00 50.30  ? 1288 ASN   B C   1 
ATOM   4068 O O   . ASN   B 1 251 ? -12.549 -4.852  6.473   1.00 50.35  ? 1288 ASN   B O   1 
ATOM   4069 C CB  . ASN   B 1 251 ? -9.838  -6.151  7.779   1.00 52.08  ? 1288 ASN   B CB  1 
ATOM   4070 C CG  . ASN   B 1 251 ? -9.017  -6.794  8.875   1.00 52.67  ? 1288 ASN   B CG  1 
ATOM   4071 O OD1 . ASN   B 1 251 ? -8.495  -6.106  9.749   1.00 52.55  ? 1288 ASN   B OD1 1 
ATOM   4072 N ND2 . ASN   B 1 251 ? -8.884  -8.109  8.830   1.00 53.64  ? 1288 ASN   B ND2 1 
ATOM   4073 N N   . THR   B 1 252 ? -11.118 -3.302  7.289   1.00 50.82  ? 1289 THR   B N   1 
ATOM   4074 C CA  . THR   B 1 252 ? -11.585 -2.216  6.443   1.00 51.16  ? 1289 THR   B CA  1 
ATOM   4075 C C   . THR   B 1 252 ? -11.250 -2.503  4.980   1.00 53.06  ? 1289 THR   B C   1 
ATOM   4076 O O   . THR   B 1 252 ? -11.951 -2.040  4.084   1.00 53.60  ? 1289 THR   B O   1 
ATOM   4077 C CB  . THR   B 1 252 ? -10.990 -0.878  6.903   1.00 51.64  ? 1289 THR   B CB  1 
ATOM   4078 O OG1 . THR   B 1 252 ? -11.166 -0.769  8.316   1.00 50.57  ? 1289 THR   B OG1 1 
ATOM   4079 C CG2 . THR   B 1 252 ? -11.622 0.315   6.220   1.00 51.94  ? 1289 THR   B CG2 1 
ATOM   4080 N N   . PHE   B 1 253 ? -10.185 -3.285  4.754   1.00 54.63  ? 1290 PHE   B N   1 
ATOM   4081 C CA  . PHE   B 1 253 ? -9.676  -3.554  3.417   1.00 57.10  ? 1290 PHE   B CA  1 
ATOM   4082 C C   . PHE   B 1 253 ? -10.221 -4.878  2.877   1.00 57.35  ? 1290 PHE   B C   1 
ATOM   4083 O O   . PHE   B 1 253 ? -9.805  -5.320  1.808   1.00 59.54  ? 1290 PHE   B O   1 
ATOM   4084 C CB  . PHE   B 1 253 ? -8.143  -3.531  3.429   1.00 59.39  ? 1290 PHE   B CB  1 
ATOM   4085 C CG  . PHE   B 1 253 ? -7.494  -4.410  4.470   1.00 59.29  ? 1290 PHE   B CG  1 
ATOM   4086 C CD1 . PHE   B 1 253 ? -7.394  -5.781  4.286   1.00 59.99  ? 1290 PHE   B CD1 1 
ATOM   4087 C CD2 . PHE   B 1 253 ? -6.998  -3.867  5.647   1.00 58.83  ? 1290 PHE   B CD2 1 
ATOM   4088 C CE1 . PHE   B 1 253 ? -6.801  -6.586  5.247   1.00 60.13  ? 1290 PHE   B CE1 1 
ATOM   4089 C CE2 . PHE   B 1 253 ? -6.408  -4.674  6.609   1.00 58.96  ? 1290 PHE   B CE2 1 
ATOM   4090 C CZ  . PHE   B 1 253 ? -6.310  -6.031  6.407   1.00 59.62  ? 1290 PHE   B CZ  1 
ATOM   4091 N N   . ASP   B 1 254 ? -11.153 -5.503  3.612   1.00 55.45  ? 1291 ASP   B N   1 
ATOM   4092 C CA  . ASP   B 1 254 ? -11.798 -6.732  3.174   1.00 56.03  ? 1291 ASP   B CA  1 
ATOM   4093 C C   . ASP   B 1 254 ? -13.302 -6.509  3.012   1.00 54.80  ? 1291 ASP   B C   1 
ATOM   4094 O O   . ASP   B 1 254 ? -14.058 -7.471  2.902   1.00 54.94  ? 1291 ASP   B O   1 
ATOM   4095 C CB  . ASP   B 1 254 ? -11.515 -7.876  4.154   1.00 55.82  ? 1291 ASP   B CB  1 
ATOM   4096 C CG  . ASP   B 1 254 ? -10.087 -8.397  4.115   1.00 57.66  ? 1291 ASP   B CG  1 
ATOM   4097 O OD1 . ASP   B 1 254 ? -9.352  -8.033  3.176   1.00 59.63  ? 1291 ASP   B OD1 1 
ATOM   4098 O OD2 . ASP   B 1 254 ? -9.721  -9.165  5.027   1.00 57.40  ? 1291 ASP   B OD2 1 
ATOM   4099 N N   . ILE   B 1 255 ? -13.724 -5.238  2.971   1.00 53.83  ? 1292 ILE   B N   1 
ATOM   4100 C CA  . ILE   B 1 255 ? -15.133 -4.889  2.877   1.00 53.08  ? 1292 ILE   B CA  1 
ATOM   4101 C C   . ILE   B 1 255 ? -15.634 -5.189  1.465   1.00 55.18  ? 1292 ILE   B C   1 
ATOM   4102 O O   . ILE   B 1 255 ? -16.751 -5.672  1.296   1.00 55.66  ? 1292 ILE   B O   1 
ATOM   4103 C CB  . ILE   B 1 255 ? -15.364 -3.413  3.265   1.00 52.00  ? 1292 ILE   B CB  1 
ATOM   4104 C CG1 . ILE   B 1 255 ? -14.942 -3.125  4.710   1.00 50.47  ? 1292 ILE   B CG1 1 
ATOM   4105 C CG2 . ILE   B 1 255 ? -16.809 -3.001  3.014   1.00 51.84  ? 1292 ILE   B CG2 1 
ATOM   4106 C CD1 . ILE   B 1 255 ? -15.831 -3.757  5.762   1.00 49.32  ? 1292 ILE   B CD1 1 
ATOM   4107 N N   . THR   B 1 256 ? -14.801 -4.891  0.460   1.00 56.86  ? 1293 THR   B N   1 
ATOM   4108 C CA  . THR   B 1 256 ? -15.150 -5.128  -0.932  1.00 59.36  ? 1293 THR   B CA  1 
ATOM   4109 C C   . THR   B 1 256 ? -15.458 -6.610  -1.141  1.00 60.26  ? 1293 THR   B C   1 
ATOM   4110 O O   . THR   B 1 256 ? -16.473 -6.952  -1.744  1.00 61.45  ? 1293 THR   B O   1 
ATOM   4111 C CB  . THR   B 1 256 ? -14.035 -4.643  -1.868  1.00 61.85  ? 1293 THR   B CB  1 
ATOM   4112 O OG1 . THR   B 1 256 ? -13.775 -3.269  -1.579  1.00 60.84  ? 1293 THR   B OG1 1 
ATOM   4113 C CG2 . THR   B 1 256 ? -14.383 -4.796  -3.333  1.00 65.36  ? 1293 THR   B CG2 1 
ATOM   4114 N N   . VAL   B 1 257 ? -14.579 -7.475  -0.621  1.00 59.76  ? 1294 VAL   B N   1 
ATOM   4115 C CA  . VAL   B 1 257 ? -14.726 -8.917  -0.755  1.00 61.14  ? 1294 VAL   B CA  1 
ATOM   4116 C C   . VAL   B 1 257 ? -15.963 -9.376  0.016   1.00 59.54  ? 1294 VAL   B C   1 
ATOM   4117 O O   . VAL   B 1 257 ? -16.711 -10.225 -0.464  1.00 61.42  ? 1294 VAL   B O   1 
ATOM   4118 C CB  . VAL   B 1 257 ? -13.459 -9.655  -0.275  1.00 61.47  ? 1294 VAL   B CB  1 
ATOM   4119 C CG1 . VAL   B 1 257 ? -13.638 -11.167 -0.303  1.00 63.38  ? 1294 VAL   B CG1 1 
ATOM   4120 C CG2 . VAL   B 1 257 ? -12.229 -9.247  -1.074  1.00 63.46  ? 1294 VAL   B CG2 1 
ATOM   4121 N N   . TYR   B 1 258 ? -16.160 -8.807  1.213   1.00 56.35  ? 1295 TYR   B N   1 
ATOM   4122 C CA  . TYR   B 1 258 ? -17.284 -9.140  2.075   1.00 55.07  ? 1295 TYR   B CA  1 
ATOM   4123 C C   . TYR   B 1 258 ? -18.600 -8.942  1.326   1.00 56.15  ? 1295 TYR   B C   1 
ATOM   4124 O O   . TYR   B 1 258 ? -19.458 -9.823  1.327   1.00 57.52  ? 1295 TYR   B O   1 
ATOM   4125 C CB  . TYR   B 1 258 ? -17.245 -8.278  3.341   1.00 52.23  ? 1295 TYR   B CB  1 
ATOM   4126 C CG  . TYR   B 1 258 ? -18.233 -8.654  4.418   1.00 51.39  ? 1295 TYR   B CG  1 
ATOM   4127 C CD1 . TYR   B 1 258 ? -18.050 -9.787  5.195   1.00 51.74  ? 1295 TYR   B CD1 1 
ATOM   4128 C CD2 . TYR   B 1 258 ? -19.349 -7.870  4.672   1.00 50.59  ? 1295 TYR   B CD2 1 
ATOM   4129 C CE1 . TYR   B 1 258 ? -18.947 -10.134 6.193   1.00 51.54  ? 1295 TYR   B CE1 1 
ATOM   4130 C CE2 . TYR   B 1 258 ? -20.257 -8.204  5.664   1.00 50.29  ? 1295 TYR   B CE2 1 
ATOM   4131 C CZ  . TYR   B 1 258 ? -20.055 -9.339  6.429   1.00 50.86  ? 1295 TYR   B CZ  1 
ATOM   4132 O OH  . TYR   B 1 258 ? -20.955 -9.674  7.412   1.00 51.24  ? 1295 TYR   B OH  1 
ATOM   4133 N N   . LEU   B 1 259 ? -18.737 -7.776  0.682   1.00 55.80  ? 1296 LEU   B N   1 
ATOM   4134 C CA  . LEU   B 1 259 ? -19.973 -7.383  0.023   1.00 56.97  ? 1296 LEU   B CA  1 
ATOM   4135 C C   . LEU   B 1 259 ? -20.133 -8.121  -1.305  1.00 60.47  ? 1296 LEU   B C   1 
ATOM   4136 O O   . LEU   B 1 259 ? -21.255 -8.422  -1.707  1.00 62.31  ? 1296 LEU   B O   1 
ATOM   4137 C CB  . LEU   B 1 259 ? -19.957 -5.865  -0.185  1.00 56.10  ? 1296 LEU   B CB  1 
ATOM   4138 C CG  . LEU   B 1 259 ? -19.984 -5.023  1.091   1.00 53.12  ? 1296 LEU   B CG  1 
ATOM   4139 C CD1 . LEU   B 1 259 ? -19.897 -3.540  0.763   1.00 52.94  ? 1296 LEU   B CD1 1 
ATOM   4140 C CD2 . LEU   B 1 259 ? -21.232 -5.316  1.910   1.00 52.60  ? 1296 LEU   B CD2 1 
ATOM   4141 N N   . LEU   B 1 260 ? -19.011 -8.403  -1.982  1.00 61.74  ? 1297 LEU   B N   1 
ATOM   4142 C CA  . LEU   B 1 260 ? -19.024 -9.151  -3.232  1.00 65.62  ? 1297 LEU   B CA  1 
ATOM   4143 C C   . LEU   B 1 260 ? -19.582 -10.556 -3.007  1.00 67.26  ? 1297 LEU   B C   1 
ATOM   4144 O O   . LEU   B 1 260 ? -20.273 -11.091 -3.872  1.00 70.79  ? 1297 LEU   B O   1 
ATOM   4145 C CB  . LEU   B 1 260 ? -17.603 -9.220  -3.807  1.00 66.75  ? 1297 LEU   B CB  1 
ATOM   4146 C CG  . LEU   B 1 260 ? -17.170 -8.033  -4.666  1.00 67.63  ? 1297 LEU   B CG  1 
ATOM   4147 C CD1 . LEU   B 1 260 ? -15.734 -8.207  -5.138  1.00 69.22  ? 1297 LEU   B CD1 1 
ATOM   4148 C CD2 . LEU   B 1 260 ? -18.099 -7.850  -5.858  1.00 71.02  ? 1297 LEU   B CD2 1 
ATOM   4149 N N   . GLN   B 1 261 ? -19.277 -11.141 -1.842  1.00 65.25  ? 1298 GLN   B N   1 
ATOM   4150 C CA  . GLN   B 1 261 ? -19.710 -12.490 -1.512  1.00 67.08  ? 1298 GLN   B CA  1 
ATOM   4151 C C   . GLN   B 1 261 ? -21.150 -12.484 -0.998  1.00 66.94  ? 1298 GLN   B C   1 
ATOM   4152 O O   . GLN   B 1 261 ? -21.707 -13.544 -0.717  1.00 68.96  ? 1298 GLN   B O   1 
ATOM   4153 C CB  . GLN   B 1 261 ? -18.747 -13.109 -0.496  1.00 65.51  ? 1298 GLN   B CB  1 
ATOM   4154 C CG  . GLN   B 1 261 ? -17.383 -13.437 -1.089  1.00 66.91  ? 1298 GLN   B CG  1 
ATOM   4155 C CD  . GLN   B 1 261 ? -16.384 -13.905 -0.060  1.00 65.47  ? 1298 GLN   B CD  1 
ATOM   4156 O OE1 . GLN   B 1 261 ? -16.636 -13.880 1.143   1.00 63.15  ? 1298 GLN   B OE1 1 
ATOM   4157 N NE2 . GLN   B 1 261 ? -15.223 -14.330 -0.532  1.00 67.25  ? 1298 GLN   B NE2 1 
ATOM   4158 N N   . GLY   B 1 262 ? -21.744 -11.291 -0.869  1.00 65.04  ? 1299 GLY   B N   1 
ATOM   4159 C CA  . GLY   B 1 262 ? -23.163 -11.154 -0.583  1.00 65.61  ? 1299 GLY   B CA  1 
ATOM   4160 C C   . GLY   B 1 262 ? -23.461 -11.106 0.914   1.00 62.98  ? 1299 GLY   B C   1 
ATOM   4161 O O   . GLY   B 1 262 ? -24.622 -11.169 1.313   1.00 63.84  ? 1299 GLY   B O   1 
ATOM   4162 N N   . ARG   B 1 263 ? -22.408 -10.989 1.731   1.00 60.22  ? 1300 ARG   B N   1 
ATOM   4163 C CA  . ARG   B 1 263 ? -22.558 -10.889 3.173   1.00 57.89  ? 1300 ARG   B CA  1 
ATOM   4164 C C   . ARG   B 1 263 ? -22.821 -9.433  3.544   1.00 55.45  ? 1300 ARG   B C   1 
ATOM   4165 O O   . ARG   B 1 263 ? -22.131 -8.536  3.064   1.00 53.95  ? 1300 ARG   B O   1 
ATOM   4166 C CB  . ARG   B 1 263 ? -21.306 -11.424 3.876   1.00 56.66  ? 1300 ARG   B CB  1 
ATOM   4167 C CG  . ARG   B 1 263 ? -21.092 -12.921 3.705   1.00 59.34  ? 1300 ARG   B CG  1 
ATOM   4168 C CD  . ARG   B 1 263 ? -19.805 -13.399 4.349   1.00 58.44  ? 1300 ARG   B CD  1 
ATOM   4169 N NE  . ARG   B 1 263 ? -19.751 -14.854 4.427   1.00 61.18  ? 1300 ARG   B NE  1 
ATOM   4170 C CZ  . ARG   B 1 263 ? -18.925 -15.627 3.728   1.00 63.18  ? 1300 ARG   B CZ  1 
ATOM   4171 N NH1 . ARG   B 1 263 ? -18.091 -15.093 2.853   1.00 62.82  ? 1300 ARG   B NH1 1 
ATOM   4172 N NH2 . ARG   B 1 263 ? -18.942 -16.937 3.901   1.00 65.88  ? 1300 ARG   B NH2 1 
ATOM   4173 N N   . ARG   B 1 264 ? -23.831 -9.220  4.397   1.00 55.40  ? 1301 ARG   B N   1 
ATOM   4174 C CA  . ARG   B 1 264 ? -24.199 -7.896  4.872   1.00 53.84  ? 1301 ARG   B CA  1 
ATOM   4175 C C   . ARG   B 1 264 ? -24.121 -7.877  6.398   1.00 52.51  ? 1301 ARG   B C   1 
ATOM   4176 O O   . ARG   B 1 264 ? -23.759 -8.876  7.016   1.00 52.75  ? 1301 ARG   B O   1 
ATOM   4177 C CB  . ARG   B 1 264 ? -25.606 -7.532  4.385   1.00 55.76  ? 1301 ARG   B CB  1 
ATOM   4178 C CG  . ARG   B 1 264 ? -25.784 -7.579  2.873   1.00 58.03  ? 1301 ARG   B CG  1 
ATOM   4179 C CD  . ARG   B 1 264 ? -24.885 -6.601  2.139   1.00 56.83  ? 1301 ARG   B CD  1 
ATOM   4180 N NE  . ARG   B 1 264 ? -25.190 -6.544  0.715   1.00 59.49  ? 1301 ARG   B NE  1 
ATOM   4181 C CZ  . ARG   B 1 264 ? -24.403 -7.009  -0.251  1.00 60.98  ? 1301 ARG   B CZ  1 
ATOM   4182 N NH1 . ARG   B 1 264 ? -23.332 -7.725  0.045   1.00 59.95  ? 1301 ARG   B NH1 1 
ATOM   4183 N NH2 . ARG   B 1 264 ? -24.702 -6.769  -1.516  1.00 63.84  ? 1301 ARG   B NH2 1 
ATOM   4184 N N   . LEU   B 1 265 ? -24.459 -6.726  6.990   1.00 51.52  ? 1302 LEU   B N   1 
ATOM   4185 C CA  . LEU   B 1 265 ? -24.489 -6.574  8.436   1.00 50.80  ? 1302 LEU   B CA  1 
ATOM   4186 C C   . LEU   B 1 265 ? -25.583 -7.467  9.015   1.00 53.09  ? 1302 LEU   B C   1 
ATOM   4187 O O   . LEU   B 1 265 ? -26.645 -7.619  8.414   1.00 54.88  ? 1302 LEU   B O   1 
ATOM   4188 C CB  . LEU   B 1 265 ? -24.747 -5.104  8.786   1.00 49.75  ? 1302 LEU   B CB  1 
ATOM   4189 C CG  . LEU   B 1 265 ? -23.717 -4.099  8.269   1.00 48.12  ? 1302 LEU   B CG  1 
ATOM   4190 C CD1 . LEU   B 1 265 ? -24.075 -2.684  8.700   1.00 47.65  ? 1302 LEU   B CD1 1 
ATOM   4191 C CD2 . LEU   B 1 265 ? -22.318 -4.456  8.744   1.00 46.96  ? 1302 LEU   B CD2 1 
ATOM   4192 N N   . LEU   B 1 266 ? -25.309 -8.045  10.191  1.00 53.41  ? 1303 LEU   B N   1 
ATOM   4193 C CA  . LEU   B 1 266 ? -26.249 -8.931  10.858  1.00 56.18  ? 1303 LEU   B CA  1 
ATOM   4194 C C   . LEU   B 1 266 ? -27.329 -8.098  11.542  1.00 57.05  ? 1303 LEU   B C   1 
ATOM   4195 O O   . LEU   B 1 266 ? -27.182 -6.888  11.697  1.00 55.23  ? 1303 LEU   B O   1 
ATOM   4196 C CB  . LEU   B 1 266 ? -25.501 -9.804  11.873  1.00 56.46  ? 1303 LEU   B CB  1 
ATOM   4197 C CG  . LEU   B 1 266 ? -24.588 -10.879 11.281  1.00 56.69  ? 1303 LEU   B CG  1 
ATOM   4198 C CD1 . LEU   B 1 266 ? -23.227 -10.307 10.905  1.00 54.16  ? 1303 LEU   B CD1 1 
ATOM   4199 C CD2 . LEU   B 1 266 ? -24.428 -12.043 12.248  1.00 58.64  ? 1303 LEU   B CD2 1 
ATOM   4200 N N   . GLN   B 1 267 ? -28.416 -8.765  11.944  1.00 60.29  ? 1304 GLN   B N   1 
ATOM   4201 C CA  . GLN   B 1 267 ? -29.528 -8.104  12.606  1.00 62.04  ? 1304 GLN   B CA  1 
ATOM   4202 C C   . GLN   B 1 267 ? -29.143 -7.820  14.056  1.00 61.98  ? 1304 GLN   B C   1 
ATOM   4203 O O   . GLN   B 1 267 ? -28.757 -8.737  14.778  1.00 62.96  ? 1304 GLN   B O   1 
ATOM   4204 C CB  . GLN   B 1 267 ? -30.783 -8.975  12.521  1.00 65.91  ? 1304 GLN   B CB  1 
ATOM   4205 C CG  . GLN   B 1 267 ? -32.045 -8.281  13.014  1.00 68.07  ? 1304 GLN   B CG  1 
ATOM   4206 C CD  . GLN   B 1 267 ? -33.296 -9.078  12.737  1.00 72.41  ? 1304 GLN   B CD  1 
ATOM   4207 O OE1 . GLN   B 1 267 ? -33.256 -10.156 12.147  1.00 73.90  ? 1304 GLN   B OE1 1 
ATOM   4208 N NE2 . GLN   B 1 267 ? -34.429 -8.545  13.163  1.00 74.93  ? 1304 GLN   B NE2 1 
ATOM   4209 N N   . PRO   B 1 268 ? -29.209 -6.550  14.525  1.00 61.39  ? 1305 PRO   B N   1 
ATOM   4210 C CA  . PRO   B 1 268 ? -28.975 -6.233  15.936  1.00 62.19  ? 1305 PRO   B CA  1 
ATOM   4211 C C   . PRO   B 1 268 ? -29.931 -6.961  16.878  1.00 66.38  ? 1305 PRO   B C   1 
ATOM   4212 O O   . PRO   B 1 268 ? -30.957 -7.485  16.448  1.00 68.72  ? 1305 PRO   B O   1 
ATOM   4213 C CB  . PRO   B 1 268 ? -29.197 -4.715  16.025  1.00 61.24  ? 1305 PRO   B CB  1 
ATOM   4214 C CG  . PRO   B 1 268 ? -28.981 -4.218  14.610  1.00 59.05  ? 1305 PRO   B CG  1 
ATOM   4215 C CD  . PRO   B 1 268 ? -29.465 -5.344  13.720  1.00 60.23  ? 1305 PRO   B CD  1 
ATOM   4216 N N   . GLU   B 1 269 ? -29.579 -6.969  18.169  1.00 68.01  ? 1306 GLU   B N   1 
ATOM   4217 C CA  . GLU   B 1 269 ? -30.295 -7.737  19.175  1.00 72.52  ? 1306 GLU   B CA  1 
ATOM   4218 C C   . GLU   B 1 269 ? -31.726 -7.220  19.303  1.00 75.73  ? 1306 GLU   B C   1 
ATOM   4219 O O   . GLU   B 1 269 ? -32.675 -7.996  19.207  1.00 79.21  ? 1306 GLU   B O   1 
ATOM   4220 C CB  . GLU   B 1 269 ? -29.559 -7.664  20.516  1.00 73.31  ? 1306 GLU   B CB  1 
ATOM   4221 C CG  . GLU   B 1 269 ? -30.096 -8.623  21.563  1.00 77.84  ? 1306 GLU   B CG  1 
ATOM   4222 C CD  . GLU   B 1 269 ? -29.329 -8.612  22.875  1.00 79.08  ? 1306 GLU   B CD  1 
ATOM   4223 O OE1 . GLU   B 1 269 ? -29.953 -8.343  23.921  1.00 82.66  ? 1306 GLU   B OE1 1 
ATOM   4224 O OE2 . GLU   B 1 269 ? -28.109 -8.871  22.846  1.00 76.91  ? 1306 GLU   B OE2 1 
ATOM   4225 N N   . TYR   B 1 270 ? -31.863 -5.905  19.519  1.00 75.07  ? 1307 TYR   B N   1 
ATOM   4226 C CA  . TYR   B 1 270 ? -33.163 -5.270  19.670  1.00 78.01  ? 1307 TYR   B CA  1 
ATOM   4227 C C   . TYR   B 1 270 ? -33.485 -4.472  18.408  1.00 76.00  ? 1307 TYR   B C   1 
ATOM   4228 O O   . TYR   B 1 270 ? -33.612 -3.249  18.452  1.00 75.43  ? 1307 TYR   B O   1 
ATOM   4229 C CB  . TYR   B 1 270 ? -33.184 -4.406  20.934  1.00 79.67  ? 1307 TYR   B CB  1 
ATOM   4230 C CG  . TYR   B 1 270 ? -32.995 -5.180  22.215  1.00 82.60  ? 1307 TYR   B CG  1 
ATOM   4231 C CD1 . TYR   B 1 270 ? -33.908 -6.147  22.605  1.00 86.95  ? 1307 TYR   B CD1 1 
ATOM   4232 C CD2 . TYR   B 1 270 ? -31.899 -4.958  23.034  1.00 81.54  ? 1307 TYR   B CD2 1 
ATOM   4233 C CE1 . TYR   B 1 270 ? -33.744 -6.867  23.777  1.00 90.16  ? 1307 TYR   B CE1 1 
ATOM   4234 C CE2 . TYR   B 1 270 ? -31.719 -5.669  24.210  1.00 84.65  ? 1307 TYR   B CE2 1 
ATOM   4235 C CZ  . TYR   B 1 270 ? -32.645 -6.628  24.583  1.00 88.99  ? 1307 TYR   B CZ  1 
ATOM   4236 O OH  . TYR   B 1 270 ? -32.478 -7.340  25.746  1.00 92.62  ? 1307 TYR   B OH  1 
ATOM   4237 N N   . CYS   B 1 271 ? -33.613 -5.194  17.288  1.00 75.37  ? 1308 CYS   B N   1 
ATOM   4238 C CA  . CYS   B 1 271 ? -33.986 -4.613  16.009  1.00 74.28  ? 1308 CYS   B CA  1 
ATOM   4239 C C   . CYS   B 1 271 ? -35.167 -5.387  15.430  1.00 77.97  ? 1308 CYS   B C   1 
ATOM   4240 O O   . CYS   B 1 271 ? -35.046 -6.582  15.165  1.00 79.07  ? 1308 CYS   B O   1 
ATOM   4241 C CB  . CYS   B 1 271 ? -32.817 -4.647  15.032  1.00 70.27  ? 1308 CYS   B CB  1 
ATOM   4242 S SG  . CYS   B 1 271 ? -33.259 -4.118  13.356  1.00 69.67  ? 1308 CYS   B SG  1 
ATOM   4243 N N   . PRO   B 1 272 ? -36.345 -4.747  15.233  1.00 80.65  ? 1309 PRO   B N   1 
ATOM   4244 C CA  . PRO   B 1 272 ? -37.483 -5.402  14.583  1.00 84.38  ? 1309 PRO   B CA  1 
ATOM   4245 C C   . PRO   B 1 272 ? -37.135 -5.985  13.214  1.00 82.86  ? 1309 PRO   B C   1 
ATOM   4246 O O   . PRO   B 1 272 ? -36.319 -5.422  12.486  1.00 79.03  ? 1309 PRO   B O   1 
ATOM   4247 C CB  . PRO   B 1 272 ? -38.517 -4.275  14.431  1.00 86.51  ? 1309 PRO   B CB  1 
ATOM   4248 C CG  . PRO   B 1 272 ? -38.166 -3.293  15.528  1.00 85.38  ? 1309 PRO   B CG  1 
ATOM   4249 C CD  . PRO   B 1 272 ? -36.660 -3.374  15.660  1.00 80.75  ? 1309 PRO   B CD  1 
ATOM   4250 N N   . ASP   B 1 273 ? -37.771 -7.116  12.879  1.00 86.13  ? 1310 ASP   B N   1 
ATOM   4251 C CA  . ASP   B 1 273 ? -37.539 -7.795  11.614  1.00 85.76  ? 1310 ASP   B CA  1 
ATOM   4252 C C   . ASP   B 1 273 ? -37.956 -6.894  10.452  1.00 85.53  ? 1310 ASP   B C   1 
ATOM   4253 O O   . ASP   B 1 273 ? -37.241 -6.822  9.453   1.00 82.87  ? 1310 ASP   B O   1 
ATOM   4254 C CB  . ASP   B 1 273 ? -38.257 -9.148  11.559  1.00 90.37  ? 1310 ASP   B CB  1 
ATOM   4255 C CG  . ASP   B 1 273 ? -37.758 -10.165 12.572  1.00 90.74  ? 1310 ASP   B CG  1 
ATOM   4256 O OD1 . ASP   B 1 273 ? -36.883 -9.807  13.386  1.00 87.57  ? 1310 ASP   B OD1 1 
ATOM   4257 O OD2 . ASP   B 1 273 ? -38.247 -11.310 12.537  1.00 94.60  ? 1310 ASP   B OD2 1 
ATOM   4258 N N   . PRO   B 1 274 ? -39.112 -6.190  10.524  1.00 88.55  ? 1311 PRO   B N   1 
ATOM   4259 C CA  . PRO   B 1 274 ? -39.508 -5.252  9.469   1.00 88.66  ? 1311 PRO   B CA  1 
ATOM   4260 C C   . PRO   B 1 274 ? -38.472 -4.165  9.182   1.00 83.96  ? 1311 PRO   B C   1 
ATOM   4261 O O   . PRO   B 1 274 ? -38.287 -3.778  8.030   1.00 83.28  ? 1311 PRO   B O   1 
ATOM   4262 C CB  . PRO   B 1 274 ? -40.800 -4.618  10.010  1.00 92.46  ? 1311 PRO   B CB  1 
ATOM   4263 C CG  . PRO   B 1 274 ? -41.351 -5.657  10.960  1.00 96.02  ? 1311 PRO   B CG  1 
ATOM   4264 C CD  . PRO   B 1 274 ? -40.123 -6.278  11.592  1.00 92.47  ? 1311 PRO   B CD  1 
ATOM   4265 N N   . LEU   B 1 275 ? -37.805 -3.681  10.239  1.00 81.29  ? 1312 LEU   B N   1 
ATOM   4266 C CA  . LEU   B 1 275 ? -36.813 -2.624  10.120  1.00 77.05  ? 1312 LEU   B CA  1 
ATOM   4267 C C   . LEU   B 1 275 ? -35.535 -3.176  9.490   1.00 73.58  ? 1312 LEU   B C   1 
ATOM   4268 O O   . LEU   B 1 275 ? -34.927 -2.516  8.650   1.00 71.37  ? 1312 LEU   B O   1 
ATOM   4269 C CB  . LEU   B 1 275 ? -36.535 -2.036  11.508  1.00 76.05  ? 1312 LEU   B CB  1 
ATOM   4270 C CG  . LEU   B 1 275 ? -35.644 -0.794  11.533  1.00 72.78  ? 1312 LEU   B CG  1 
ATOM   4271 C CD1 . LEU   B 1 275 ? -36.389 0.423   11.004  1.00 74.19  ? 1312 LEU   B CD1 1 
ATOM   4272 C CD2 . LEU   B 1 275 ? -35.123 -0.528  12.937  1.00 71.83  ? 1312 LEU   B CD2 1 
ATOM   4273 N N   . TYR   B 1 276 ? -35.130 -4.380  9.912   1.00 73.46  ? 1313 TYR   B N   1 
ATOM   4274 C CA  . TYR   B 1 276 ? -33.951 -5.033  9.363   1.00 71.01  ? 1313 TYR   B CA  1 
ATOM   4275 C C   . TYR   B 1 276 ? -34.192 -5.403  7.900   1.00 72.55  ? 1313 TYR   B C   1 
ATOM   4276 O O   . TYR   B 1 276 ? -33.264 -5.377  7.096   1.00 70.26  ? 1313 TYR   B O   1 
ATOM   4277 C CB  . TYR   B 1 276 ? -33.578 -6.272  10.182  1.00 71.43  ? 1313 TYR   B CB  1 
ATOM   4278 C CG  . TYR   B 1 276 ? -32.351 -6.997  9.688   1.00 69.19  ? 1313 TYR   B CG  1 
ATOM   4279 C CD1 . TYR   B 1 276 ? -31.121 -6.361  9.629   1.00 65.47  ? 1313 TYR   B CD1 1 
ATOM   4280 C CD2 . TYR   B 1 276 ? -32.417 -8.316  9.265   1.00 71.20  ? 1313 TYR   B CD2 1 
ATOM   4281 C CE1 . TYR   B 1 276 ? -29.988 -7.016  9.172   1.00 63.76  ? 1313 TYR   B CE1 1 
ATOM   4282 C CE2 . TYR   B 1 276 ? -31.295 -8.985  8.804   1.00 69.55  ? 1313 TYR   B CE2 1 
ATOM   4283 C CZ  . TYR   B 1 276 ? -30.075 -8.333  8.758   1.00 65.76  ? 1313 TYR   B CZ  1 
ATOM   4284 O OH  . TYR   B 1 276 ? -28.956 -8.987  8.304   1.00 64.52  ? 1313 TYR   B OH  1 
ATOM   4285 N N   . GLU   B 1 277 ? -35.441 -5.754  7.568   1.00 76.85  ? 1314 GLU   B N   1 
ATOM   4286 C CA  . GLU   B 1 277 ? -35.811 -6.080  6.200   1.00 79.35  ? 1314 GLU   B CA  1 
ATOM   4287 C C   . GLU   B 1 277 ? -35.557 -4.869  5.303   1.00 77.88  ? 1314 GLU   B C   1 
ATOM   4288 O O   . GLU   B 1 277 ? -35.093 -5.022  4.176   1.00 77.85  ? 1314 GLU   B O   1 
ATOM   4289 C CB  . GLU   B 1 277 ? -37.275 -6.522  6.132   1.00 84.63  ? 1314 GLU   B CB  1 
ATOM   4290 C CG  . GLU   B 1 277 ? -37.671 -7.156  4.808   1.00 88.06  ? 1314 GLU   B CG  1 
ATOM   4291 C CD  . GLU   B 1 277 ? -37.192 -8.585  4.606   1.00 89.10  ? 1314 GLU   B CD  1 
ATOM   4292 O OE1 . GLU   B 1 277 ? -38.052 -9.482  4.492   1.00 93.78  ? 1314 GLU   B OE1 1 
ATOM   4293 O OE2 . GLU   B 1 277 ? -35.964 -8.799  4.555   1.00 85.54  ? 1314 GLU   B OE2 1 
ATOM   4294 N N   . VAL   B 1 278 ? -35.859 -3.672  5.823   1.00 77.08  ? 1315 VAL   B N   1 
ATOM   4295 C CA  . VAL   B 1 278 ? -35.648 -2.426  5.100   1.00 76.07  ? 1315 VAL   B CA  1 
ATOM   4296 C C   . VAL   B 1 278 ? -34.151 -2.216  4.878   1.00 71.97  ? 1315 VAL   B C   1 
ATOM   4297 O O   . VAL   B 1 278 ? -33.742 -1.763  3.812   1.00 71.72  ? 1315 VAL   B O   1 
ATOM   4298 C CB  . VAL   B 1 278 ? -36.281 -1.231  5.844   1.00 76.59  ? 1315 VAL   B CB  1 
ATOM   4299 C CG1 . VAL   B 1 278 ? -35.904 0.102   5.211   1.00 75.45  ? 1315 VAL   B CG1 1 
ATOM   4300 C CG2 . VAL   B 1 278 ? -37.795 -1.364  5.947   1.00 81.14  ? 1315 VAL   B CG2 1 
ATOM   4301 N N   . MET   B 1 279 ? -33.345 -2.541  5.898   1.00 69.19  ? 1316 MET   B N   1 
ATOM   4302 C CA  . MET   B 1 279 ? -31.899 -2.405  5.822   1.00 65.67  ? 1316 MET   B CA  1 
ATOM   4303 C C   . MET   B 1 279 ? -31.352 -3.264  4.682   1.00 66.22  ? 1316 MET   B C   1 
ATOM   4304 O O   . MET   B 1 279 ? -30.470 -2.826  3.948   1.00 64.91  ? 1316 MET   B O   1 
ATOM   4305 C CB  . MET   B 1 279 ? -31.236 -2.834  7.135   1.00 63.49  ? 1316 MET   B CB  1 
ATOM   4306 C CG  . MET   B 1 279 ? -31.341 -1.804  8.244   1.00 62.44  ? 1316 MET   B CG  1 
ATOM   4307 S SD  . MET   B 1 279 ? -30.572 -2.378  9.783   1.00 60.62  ? 1316 MET   B SD  1 
ATOM   4308 C CE  . MET   B 1 279 ? -31.622 -1.594  11.006  1.00 62.40  ? 1316 MET   B CE  1 
ATOM   4309 N N   . LEU   B 1 280 ? -31.882 -4.487  4.548   1.00 68.68  ? 1317 LEU   B N   1 
ATOM   4310 C CA  . LEU   B 1 280 ? -31.426 -5.427  3.534   1.00 69.91  ? 1317 LEU   B CA  1 
ATOM   4311 C C   . LEU   B 1 280 ? -31.787 -4.926  2.136   1.00 72.21  ? 1317 LEU   B C   1 
ATOM   4312 O O   . LEU   B 1 280 ? -31.042 -5.164  1.188   1.00 72.22  ? 1317 LEU   B O   1 
ATOM   4313 C CB  . LEU   B 1 280 ? -32.048 -6.803  3.803   1.00 72.66  ? 1317 LEU   B CB  1 
ATOM   4314 C CG  . LEU   B 1 280 ? -31.554 -7.527  5.056   1.00 71.13  ? 1317 LEU   B CG  1 
ATOM   4315 C CD1 . LEU   B 1 280 ? -32.169 -8.915  5.154   1.00 74.60  ? 1317 LEU   B CD1 1 
ATOM   4316 C CD2 . LEU   B 1 280 ? -30.035 -7.620  5.079   1.00 67.88  ? 1317 LEU   B CD2 1 
ATOM   4317 N N   . LYS   B 1 281 ? -32.932 -4.240  2.016   1.00 74.56  ? 1318 LYS   B N   1 
ATOM   4318 C CA  . LYS   B 1 281 ? -33.356 -3.662  0.750   1.00 77.24  ? 1318 LYS   B CA  1 
ATOM   4319 C C   . LYS   B 1 281 ? -32.380 -2.566  0.327   1.00 74.89  ? 1318 LYS   B C   1 
ATOM   4320 O O   . LYS   B 1 281 ? -32.066 -2.439  -0.855  1.00 76.48  ? 1318 LYS   B O   1 
ATOM   4321 C CB  . LYS   B 1 281 ? -34.779 -3.103  0.856   1.00 80.25  ? 1318 LYS   B CB  1 
ATOM   4322 C CG  . LYS   B 1 281 ? -35.870 -4.144  1.071   1.00 83.95  ? 1318 LYS   B CG  1 
ATOM   4323 C CD  . LYS   B 1 281 ? -37.249 -3.547  1.266   1.00 87.13  ? 1318 LYS   B CD  1 
ATOM   4324 C CE  . LYS   B 1 281 ? -38.280 -4.562  1.710   1.00 90.85  ? 1318 LYS   B CE  1 
ATOM   4325 N NZ  . LYS   B 1 281 ? -38.407 -5.681  0.746   1.00 94.31  ? 1318 LYS   B NZ  1 
ATOM   4326 N N   . CYS   B 1 282 ? -31.909 -1.779  1.304   1.00 71.64  ? 1319 CYS   B N   1 
ATOM   4327 C CA  . CYS   B 1 282 ? -30.947 -0.718  1.052   1.00 69.48  ? 1319 CYS   B CA  1 
ATOM   4328 C C   . CYS   B 1 282 ? -29.620 -1.302  0.570   1.00 68.29  ? 1319 CYS   B C   1 
ATOM   4329 O O   . CYS   B 1 282 ? -28.947 -0.694  -0.261  1.00 68.18  ? 1319 CYS   B O   1 
ATOM   4330 C CB  . CYS   B 1 282 ? -30.717 0.127   2.301   1.00 66.66  ? 1319 CYS   B CB  1 
ATOM   4331 S SG  . CYS   B 1 282 ? -32.181 1.056   2.830   1.00 68.28  ? 1319 CYS   B SG  1 
ATOM   4332 N N   . TRP   B 1 283 ? -29.258 -2.483  1.093   1.00 67.71  ? 1320 TRP   B N   1 
ATOM   4333 C CA  . TRP   B 1 283 ? -28.006 -3.137  0.746   1.00 66.90  ? 1320 TRP   B CA  1 
ATOM   4334 C C   . TRP   B 1 283 ? -28.224 -4.160  -0.368  1.00 70.34  ? 1320 TRP   B C   1 
ATOM   4335 O O   . TRP   B 1 283 ? -27.855 -5.325  -0.222  1.00 70.55  ? 1320 TRP   B O   1 
ATOM   4336 C CB  . TRP   B 1 283 ? -27.378 -3.802  1.978   1.00 64.47  ? 1320 TRP   B CB  1 
ATOM   4337 C CG  . TRP   B 1 283 ? -27.182 -2.897  3.154   1.00 61.97  ? 1320 TRP   B CG  1 
ATOM   4338 C CD1 . TRP   B 1 283 ? -26.762 -1.598  3.141   1.00 60.83  ? 1320 TRP   B CD1 1 
ATOM   4339 C CD2 . TRP   B 1 283 ? -27.356 -3.247  4.538   1.00 60.85  ? 1320 TRP   B CD2 1 
ATOM   4340 N NE1 . TRP   B 1 283 ? -26.688 -1.109  4.417   1.00 59.12  ? 1320 TRP   B NE1 1 
ATOM   4341 C CE2 . TRP   B 1 283 ? -27.044 -2.098  5.297   1.00 59.13  ? 1320 TRP   B CE2 1 
ATOM   4342 C CE3 . TRP   B 1 283 ? -27.756 -4.410  5.207   1.00 61.62  ? 1320 TRP   B CE3 1 
ATOM   4343 C CZ2 . TRP   B 1 283 ? -27.119 -2.086  6.689   1.00 58.15  ? 1320 TRP   B CZ2 1 
ATOM   4344 C CZ3 . TRP   B 1 283 ? -27.830 -4.396  6.583   1.00 60.70  ? 1320 TRP   B CZ3 1 
ATOM   4345 C CH2 . TRP   B 1 283 ? -27.516 -3.248  7.312   1.00 58.96  ? 1320 TRP   B CH2 1 
ATOM   4346 N N   . HIS   B 1 284 ? -28.812 -3.713  -1.485  1.00 73.61  ? 1321 HIS   B N   1 
ATOM   4347 C CA  . HIS   B 1 284 ? -29.011 -4.567  -2.645  1.00 77.55  ? 1321 HIS   B CA  1 
ATOM   4348 C C   . HIS   B 1 284 ? -27.857 -4.348  -3.621  1.00 77.96  ? 1321 HIS   B C   1 
ATOM   4349 O O   . HIS   B 1 284 ? -27.497 -3.205  -3.896  1.00 77.21  ? 1321 HIS   B O   1 
ATOM   4350 C CB  . HIS   B 1 284 ? -30.373 -4.276  -3.289  1.00 81.48  ? 1321 HIS   B CB  1 
ATOM   4351 C CG  . HIS   B 1 284 ? -30.850 -5.318  -4.256  1.00 86.05  ? 1321 HIS   B CG  1 
ATOM   4352 N ND1 . HIS   B 1 284 ? -30.278 -5.543  -5.484  1.00 88.64  ? 1321 HIS   B ND1 1 
ATOM   4353 C CD2 . HIS   B 1 284 ? -31.889 -6.193  -4.137  1.00 88.98  ? 1321 HIS   B CD2 1 
ATOM   4354 C CE1 . HIS   B 1 284 ? -30.933 -6.526  -6.099  1.00 92.89  ? 1321 HIS   B CE1 1 
ATOM   4355 N NE2 . HIS   B 1 284 ? -31.938 -6.945  -5.279  1.00 93.26  ? 1321 HIS   B NE2 1 
ATOM   4356 N N   . PRO   B 1 285 ? -27.231 -5.420  -4.166  1.00 79.67  ? 1322 PRO   B N   1 
ATOM   4357 C CA  . PRO   B 1 285 ? -26.064 -5.273  -5.039  1.00 80.45  ? 1322 PRO   B CA  1 
ATOM   4358 C C   . PRO   B 1 285 ? -26.325 -4.399  -6.266  1.00 83.73  ? 1322 PRO   B C   1 
ATOM   4359 O O   . PRO   B 1 285 ? -25.505 -3.550  -6.605  1.00 82.97  ? 1322 PRO   B O   1 
ATOM   4360 C CB  . PRO   B 1 285 ? -25.712 -6.711  -5.458  1.00 82.70  ? 1322 PRO   B CB  1 
ATOM   4361 C CG  . PRO   B 1 285 ? -26.956 -7.523  -5.152  1.00 84.50  ? 1322 PRO   B CG  1 
ATOM   4362 C CD  . PRO   B 1 285 ? -27.607 -6.830  -3.974  1.00 81.33  ? 1322 PRO   B CD  1 
ATOM   4363 N N   . LYS   B 1 286 ? -27.469 -4.624  -6.925  1.00 87.91  ? 1323 LYS   B N   1 
ATOM   4364 C CA  . LYS   B 1 286 ? -27.905 -3.792  -8.034  1.00 91.77  ? 1323 LYS   B CA  1 
ATOM   4365 C C   . LYS   B 1 286 ? -28.482 -2.490  -7.480  1.00 90.25  ? 1323 LYS   B C   1 
ATOM   4366 O O   . LYS   B 1 286 ? -29.200 -2.502  -6.482  1.00 88.49  ? 1323 LYS   B O   1 
ATOM   4367 C CB  . LYS   B 1 286 ? -28.921 -4.550  -8.895  1.00 97.01  ? 1323 LYS   B CB  1 
ATOM   4368 C CG  . LYS   B 1 286 ? -28.396 -5.842  -9.511  1.00 99.67  ? 1323 LYS   B CG  1 
ATOM   4369 C CD  . LYS   B 1 286 ? -29.399 -6.559  -10.388 1.00 105.47 ? 1323 LYS   B CD  1 
ATOM   4370 C CE  . LYS   B 1 286 ? -28.849 -7.840  -10.980 1.00 108.42 ? 1323 LYS   B CE  1 
ATOM   4371 N NZ  . LYS   B 1 286 ? -29.843 -8.516  -11.847 1.00 114.79 ? 1323 LYS   B NZ  1 
ATOM   4372 N N   . ALA   B 1 287 ? -28.164 -1.374  -8.150  1.00 91.57  ? 1324 ALA   B N   1 
ATOM   4373 C CA  . ALA   B 1 287 ? -28.428 -0.042  -7.627  1.00 89.92  ? 1324 ALA   B CA  1 
ATOM   4374 C C   . ALA   B 1 287 ? -29.908 0.312   -7.752  1.00 92.72  ? 1324 ALA   B C   1 
ATOM   4375 O O   . ALA   B 1 287 ? -30.513 0.792   -6.795  1.00 90.50  ? 1324 ALA   B O   1 
ATOM   4376 C CB  . ALA   B 1 287 ? -27.565 0.966   -8.346  1.00 90.92  ? 1324 ALA   B CB  1 
ATOM   4377 N N   . GLU   B 1 288 ? -30.478 0.072   -8.940  1.00 97.96  ? 1325 GLU   B N   1 
ATOM   4378 C CA  . GLU   B 1 288 ? -31.836 0.494   -9.256  1.00 101.56 ? 1325 GLU   B CA  1 
ATOM   4379 C C   . GLU   B 1 288 ? -32.861 -0.251  -8.399  1.00 100.99 ? 1325 GLU   B C   1 
ATOM   4380 O O   . GLU   B 1 288 ? -33.971 0.243   -8.207  1.00 103.00 ? 1325 GLU   B O   1 
ATOM   4381 C CB  . GLU   B 1 288 ? -32.140 0.310   -10.748 1.00 107.68 ? 1325 GLU   B CB  1 
ATOM   4382 C CG  . GLU   B 1 288 ? -32.087 -1.131  -11.243 1.00 110.17 ? 1325 GLU   B CG  1 
ATOM   4383 C CD  . GLU   B 1 288 ? -30.703 -1.687  -11.537 1.00 109.01 ? 1325 GLU   B CD  1 
ATOM   4384 O OE1 . GLU   B 1 288 ? -30.614 -2.877  -11.901 1.00 111.12 ? 1325 GLU   B OE1 1 
ATOM   4385 O OE2 . GLU   B 1 288 ? -29.716 -0.933  -11.403 1.00 106.34 ? 1325 GLU   B OE2 1 
ATOM   4386 N N   . MET   B 1 289 ? -32.489 -1.431  -7.883  1.00 98.73  ? 1326 MET   B N   1 
ATOM   4387 C CA  . MET   B 1 289 ? -33.403 -2.270  -7.123  1.00 98.60  ? 1326 MET   B CA  1 
ATOM   4388 C C   . MET   B 1 289 ? -33.627 -1.706  -5.719  1.00 94.21  ? 1326 MET   B C   1 
ATOM   4389 O O   . MET   B 1 289 ? -34.586 -2.091  -5.052  1.00 94.87  ? 1326 MET   B O   1 
ATOM   4390 C CB  . MET   B 1 289 ? -32.860 -3.699  -7.009  1.00 98.16  ? 1326 MET   B CB  1 
ATOM   4391 C CG  . MET   B 1 289 ? -33.057 -4.535  -8.264  1.00 103.55 ? 1326 MET   B CG  1 
ATOM   4392 S SD  . MET   B 1 289 ? -34.799 -4.858  -8.654  1.00 109.50 ? 1326 MET   B SD  1 
ATOM   4393 C CE  . MET   B 1 289 ? -35.088 -3.661  -9.956  1.00 113.51 ? 1326 MET   B CE  1 
ATOM   4394 N N   . ARG   B 1 290 ? -32.743 -0.804  -5.272  1.00 90.09  ? 1327 ARG   B N   1 
ATOM   4395 C CA  . ARG   B 1 290 ? -32.847 -0.203  -3.950  1.00 86.42  ? 1327 ARG   B CA  1 
ATOM   4396 C C   . ARG   B 1 290 ? -34.033 0.759   -3.912  1.00 88.90  ? 1327 ARG   B C   1 
ATOM   4397 O O   . ARG   B 1 290 ? -34.381 1.354   -4.929  1.00 92.23  ? 1327 ARG   B O   1 
ATOM   4398 C CB  . ARG   B 1 290 ? -31.553 0.536   -3.598  1.00 82.27  ? 1327 ARG   B CB  1 
ATOM   4399 C CG  . ARG   B 1 290 ? -30.325 -0.360  -3.524  1.00 79.75  ? 1327 ARG   B CG  1 
ATOM   4400 C CD  . ARG   B 1 290 ? -29.036 0.436   -3.541  1.00 77.11  ? 1327 ARG   B CD  1 
ATOM   4401 N NE  . ARG   B 1 290 ? -27.878 -0.419  -3.752  1.00 75.87  ? 1327 ARG   B NE  1 
ATOM   4402 C CZ  . ARG   B 1 290 ? -26.653 0.020   -4.014  1.00 74.73  ? 1327 ARG   B CZ  1 
ATOM   4403 N NH1 . ARG   B 1 290 ? -26.416 1.317   -4.108  1.00 74.44  ? 1327 ARG   B NH1 1 
ATOM   4404 N NH2 . ARG   B 1 290 ? -25.667 -0.843  -4.184  1.00 74.24  ? 1327 ARG   B NH2 1 
ATOM   4405 N N   . PRO   B 1 291 ? -34.679 0.951   -2.737  1.00 87.90  ? 1328 PRO   B N   1 
ATOM   4406 C CA  . PRO   B 1 291 ? -35.857 1.814   -2.633  1.00 90.83  ? 1328 PRO   B CA  1 
ATOM   4407 C C   . PRO   B 1 291 ? -35.523 3.304   -2.604  1.00 90.33  ? 1328 PRO   B C   1 
ATOM   4408 O O   . PRO   B 1 291 ? -34.397 3.688   -2.296  1.00 86.88  ? 1328 PRO   B O   1 
ATOM   4409 C CB  . PRO   B 1 291 ? -36.477 1.376   -1.298  1.00 89.55  ? 1328 PRO   B CB  1 
ATOM   4410 C CG  . PRO   B 1 291 ? -35.285 0.962   -0.462  1.00 84.69  ? 1328 PRO   B CG  1 
ATOM   4411 C CD  . PRO   B 1 291 ? -34.314 0.343   -1.447  1.00 84.33  ? 1328 PRO   B CD  1 
ATOM   4412 N N   . SER   B 1 292 ? -36.525 4.130   -2.931  1.00 94.49  ? 1329 SER   B N   1 
ATOM   4413 C CA  . SER   B 1 292 ? -36.396 5.578   -2.878  1.00 94.95  ? 1329 SER   B CA  1 
ATOM   4414 C C   . SER   B 1 292 ? -36.605 6.058   -1.444  1.00 93.51  ? 1329 SER   B C   1 
ATOM   4415 O O   . SER   B 1 292 ? -37.173 5.339   -0.626  1.00 93.23  ? 1329 SER   B O   1 
ATOM   4416 C CB  . SER   B 1 292 ? -37.367 6.238   -3.822  1.00 99.78  ? 1329 SER   B CB  1 
ATOM   4417 O OG  . SER   B 1 292 ? -38.703 5.876   -3.509  1.00 102.43 ? 1329 SER   B OG  1 
ATOM   4418 N N   . PHE   B 1 293 ? -36.152 7.286   -1.163  1.00 74.74  ? 1330 PHE   B N   1 
ATOM   4419 C CA  . PHE   B 1 293 ? -36.246 7.868   0.169   1.00 73.37  ? 1330 PHE   B CA  1 
ATOM   4420 C C   . PHE   B 1 293 ? -37.700 8.177   0.521   1.00 73.95  ? 1330 PHE   B C   1 
ATOM   4421 O O   . PHE   B 1 293 ? -38.052 8.213   1.699   1.00 72.73  ? 1330 PHE   B O   1 
ATOM   4422 C CB  . PHE   B 1 293 ? -35.362 9.115   0.275   1.00 72.88  ? 1330 PHE   B CB  1 
ATOM   4423 C CG  . PHE   B 1 293 ? -33.906 8.827   0.540   1.00 73.58  ? 1330 PHE   B CG  1 
ATOM   4424 C CD1 . PHE   B 1 293 ? -33.494 8.345   1.774   1.00 73.20  ? 1330 PHE   B CD1 1 
ATOM   4425 C CD2 . PHE   B 1 293 ? -32.947 9.020   -0.445  1.00 75.27  ? 1330 PHE   B CD2 1 
ATOM   4426 C CE1 . PHE   B 1 293 ? -32.157 8.074   2.021   1.00 75.05  ? 1330 PHE   B CE1 1 
ATOM   4427 C CE2 . PHE   B 1 293 ? -31.610 8.748   -0.196  1.00 76.99  ? 1330 PHE   B CE2 1 
ATOM   4428 C CZ  . PHE   B 1 293 ? -31.217 8.275   1.036   1.00 77.07  ? 1330 PHE   B CZ  1 
ATOM   4429 N N   . SER   B 1 294 ? -38.535 8.405   -0.502  1.00 77.24  ? 1331 SER   B N   1 
ATOM   4430 C CA  . SER   B 1 294 ? -39.962 8.609   -0.308  1.00 79.12  ? 1331 SER   B CA  1 
ATOM   4431 C C   . SER   B 1 294 ? -40.602 7.355   0.286   1.00 80.50  ? 1331 SER   B C   1 
ATOM   4432 O O   . SER   B 1 294 ? -41.479 7.453   1.142   1.00 80.26  ? 1331 SER   B O   1 
ATOM   4433 C CB  . SER   B 1 294 ? -40.631 9.002   -1.601  1.00 81.68  ? 1331 SER   B CB  1 
ATOM   4434 O OG  . SER   B 1 294 ? -42.013 9.259   -1.401  1.00 82.93  ? 1331 SER   B OG  1 
ATOM   4435 N N   . GLU   B 1 295 ? -40.150 6.183   -0.181  1.00 83.03  ? 1332 GLU   B N   1 
ATOM   4436 C CA  . GLU   B 1 295 ? -40.680 4.903   0.263   1.00 84.51  ? 1332 GLU   B CA  1 
ATOM   4437 C C   . GLU   B 1 295 ? -40.252 4.625   1.704   1.00 82.50  ? 1332 GLU   B C   1 
ATOM   4438 O O   . GLU   B 1 295 ? -41.020 4.052   2.475   1.00 81.96  ? 1332 GLU   B O   1 
ATOM   4439 C CB  . GLU   B 1 295 ? -40.203 3.784   -0.667  1.00 87.64  ? 1332 GLU   B CB  1 
ATOM   4440 C CG  . GLU   B 1 295 ? -40.845 2.436   -0.384  1.00 89.41  ? 1332 GLU   B CG  1 
ATOM   4441 C CD  . GLU   B 1 295 ? -40.388 1.305   -1.291  1.00 93.78  ? 1332 GLU   B CD  1 
ATOM   4442 O OE1 . GLU   B 1 295 ? -39.536 1.556   -2.168  1.00 95.70  ? 1332 GLU   B OE1 1 
ATOM   4443 O OE2 . GLU   B 1 295 ? -40.887 0.174   -1.117  1.00 95.83  ? 1332 GLU   B OE2 1 
ATOM   4444 N N   . LEU   B 1 296 ? -39.023 5.030   2.052   1.00 82.28  ? 1333 LEU   B N   1 
ATOM   4445 C CA  . LEU   B 1 296 ? -38.457 4.761   3.365   1.00 81.84  ? 1333 LEU   B CA  1 
ATOM   4446 C C   . LEU   B 1 296 ? -39.184 5.570   4.439   1.00 81.39  ? 1333 LEU   B C   1 
ATOM   4447 O O   . LEU   B 1 296 ? -39.229 5.154   5.595   1.00 80.77  ? 1333 LEU   B O   1 
ATOM   4448 C CB  . LEU   B 1 296 ? -36.960 5.092   3.349   1.00 82.28  ? 1333 LEU   B CB  1 
ATOM   4449 C CG  . LEU   B 1 296 ? -36.100 4.262   2.395   1.00 84.56  ? 1333 LEU   B CG  1 
ATOM   4450 C CD1 . LEU   B 1 296 ? -34.621 4.551   2.607   1.00 85.40  ? 1333 LEU   B CD1 1 
ATOM   4451 C CD2 . LEU   B 1 296 ? -36.376 2.773   2.553   1.00 86.14  ? 1333 LEU   B CD2 1 
ATOM   4452 N N   . VAL   B 1 297 ? -39.741 6.725   4.054   1.00 82.75  ? 1334 VAL   B N   1 
ATOM   4453 C CA  . VAL   B 1 297 ? -40.479 7.575   4.975   1.00 83.91  ? 1334 VAL   B CA  1 
ATOM   4454 C C   . VAL   B 1 297 ? -41.752 6.857   5.424   1.00 85.41  ? 1334 VAL   B C   1 
ATOM   4455 O O   . VAL   B 1 297 ? -42.055 6.825   6.614   1.00 85.24  ? 1334 VAL   B O   1 
ATOM   4456 C CB  . VAL   B 1 297 ? -40.792 8.947   4.342   1.00 84.87  ? 1334 VAL   B CB  1 
ATOM   4457 C CG1 . VAL   B 1 297 ? -41.753 9.766   5.193   1.00 86.63  ? 1334 VAL   B CG1 1 
ATOM   4458 C CG2 . VAL   B 1 297 ? -39.523 9.737   4.056   1.00 84.40  ? 1334 VAL   B CG2 1 
ATOM   4459 N N   . SER   B 1 298 ? -42.486 6.282   4.462   1.00 87.43  ? 1335 SER   B N   1 
ATOM   4460 C CA  . SER   B 1 298 ? -43.762 5.636   4.734   1.00 89.10  ? 1335 SER   B CA  1 
ATOM   4461 C C   . SER   B 1 298 ? -43.565 4.362   5.554   1.00 88.31  ? 1335 SER   B C   1 
ATOM   4462 O O   . SER   B 1 298 ? -44.339 4.093   6.471   1.00 88.17  ? 1335 SER   B O   1 
ATOM   4463 C CB  . SER   B 1 298 ? -44.504 5.347   3.452   1.00 91.61  ? 1335 SER   B CB  1 
ATOM   4464 O OG  . SER   B 1 298 ? -43.761 4.469   2.618   1.00 91.54  ? 1335 SER   B OG  1 
ATOM   4465 N N   . ARG   B 1 299 ? -42.531 3.583   5.210   1.00 88.22  ? 1336 ARG   B N   1 
ATOM   4466 C CA  . ARG   B 1 299 ? -42.264 2.308   5.858   1.00 88.38  ? 1336 ARG   B CA  1 
ATOM   4467 C C   . ARG   B 1 299 ? -41.878 2.523   7.320   1.00 87.56  ? 1336 ARG   B C   1 
ATOM   4468 O O   . ARG   B 1 299 ? -42.415 1.860   8.204   1.00 87.73  ? 1336 ARG   B O   1 
ATOM   4469 C CB  . ARG   B 1 299 ? -41.157 1.545   5.121   1.00 89.13  ? 1336 ARG   B CB  1 
ATOM   4470 C CG  . ARG   B 1 299 ? -41.605 0.892   3.822   1.00 92.06  ? 1336 ARG   B CG  1 
ATOM   4471 C CD  . ARG   B 1 299 ? -40.484 0.102   3.171   1.00 94.30  ? 1336 ARG   B CD  1 
ATOM   4472 N NE  . ARG   B 1 299 ? -40.939 -0.733  2.065   1.00 98.51  ? 1336 ARG   B NE  1 
ATOM   4473 C CZ  . ARG   B 1 299 ? -41.665 -1.839  2.198   1.00 100.73 ? 1336 ARG   B CZ  1 
ATOM   4474 N NH1 . ARG   B 1 299 ? -41.976 -2.292  3.399   1.00 98.66  ? 1336 ARG   B NH1 1 
ATOM   4475 N NH2 . ARG   B 1 299 ? -42.072 -2.494  1.124   1.00 105.29 ? 1336 ARG   B NH2 1 
ATOM   4476 N N   . ILE   B 1 300 ? -40.940 3.448   7.562   1.00 87.38  ? 1337 ILE   B N   1 
ATOM   4477 C CA  . ILE   B 1 300 ? -40.415 3.688   8.898   1.00 87.53  ? 1337 ILE   B CA  1 
ATOM   4478 C C   . ILE   B 1 300 ? -41.478 4.384   9.750   1.00 88.07  ? 1337 ILE   B C   1 
ATOM   4479 O O   . ILE   B 1 300 ? -41.509 4.201   10.966  1.00 88.59  ? 1337 ILE   B O   1 
ATOM   4480 C CB  . ILE   B 1 300 ? -39.091 4.481   8.834   1.00 88.11  ? 1337 ILE   B CB  1 
ATOM   4481 C CG1 . ILE   B 1 300 ? -38.004 3.700   8.089   1.00 88.32  ? 1337 ILE   B CG1 1 
ATOM   4482 C CG2 . ILE   B 1 300 ? -38.628 4.884   10.228  1.00 89.32  ? 1337 ILE   B CG2 1 
ATOM   4483 C CD1 . ILE   B 1 300 ? -36.762 4.506   7.780   1.00 88.99  ? 1337 ILE   B CD1 1 
ATOM   4484 N N   . SER   B 1 301 ? -42.348 5.174   9.106   1.00 88.62  ? 1338 SER   B N   1 
ATOM   4485 C CA  . SER   B 1 301 ? -43.471 5.803   9.785   1.00 90.33  ? 1338 SER   B CA  1 
ATOM   4486 C C   . SER   B 1 301 ? -44.416 4.739   10.339  1.00 90.25  ? 1338 SER   B C   1 
ATOM   4487 O O   . SER   B 1 301 ? -44.945 4.888   11.440  1.00 91.37  ? 1338 SER   B O   1 
ATOM   4488 C CB  . SER   B 1 301 ? -44.195 6.756   8.866   1.00 91.95  ? 1338 SER   B CB  1 
ATOM   4489 O OG  . SER   B 1 301 ? -45.302 7.355   9.522   1.00 95.07  ? 1338 SER   B OG  1 
ATOM   4490 N N   . ALA   B 1 302 ? -44.622 3.669   9.561   1.00 89.10  ? 1339 ALA   B N   1 
ATOM   4491 C CA  . ALA   B 1 302 ? -45.438 2.541   9.981   1.00 89.34  ? 1339 ALA   B CA  1 
ATOM   4492 C C   . ALA   B 1 302 ? -44.812 1.864   11.197  1.00 88.30  ? 1339 ALA   B C   1 
ATOM   4493 O O   . ALA   B 1 302 ? -45.493 1.618   12.190  1.00 89.30  ? 1339 ALA   B O   1 
ATOM   4494 C CB  . ALA   B 1 302 ? -45.591 1.566   8.840   1.00 89.65  ? 1339 ALA   B CB  1 
ATOM   4495 N N   . ILE   B 1 303 ? -43.507 1.579   11.100  1.00 86.79  ? 1340 ILE   B N   1 
ATOM   4496 C CA  . ILE   B 1 303 ? -42.779 0.848   12.126  1.00 86.55  ? 1340 ILE   B CA  1 
ATOM   4497 C C   . ILE   B 1 303 ? -42.685 1.698   13.394  1.00 88.46  ? 1340 ILE   B C   1 
ATOM   4498 O O   . ILE   B 1 303 ? -42.643 1.156   14.498  1.00 89.65  ? 1340 ILE   B O   1 
ATOM   4499 C CB  . ILE   B 1 303 ? -41.389 0.423   11.606  1.00 85.40  ? 1340 ILE   B CB  1 
ATOM   4500 C CG1 . ILE   B 1 303 ? -41.497 -0.508  10.394  1.00 84.96  ? 1340 ILE   B CG1 1 
ATOM   4501 C CG2 . ILE   B 1 303 ? -40.558 -0.205  12.718  1.00 86.35  ? 1340 ILE   B CG2 1 
ATOM   4502 C CD1 . ILE   B 1 303 ? -40.197 -0.708  9.649   1.00 85.43  ? 1340 ILE   B CD1 1 
ATOM   4503 N N   . PHE   B 1 304 ? -42.650 3.026   13.227  1.00 89.73  ? 1341 PHE   B N   1 
ATOM   4504 C CA  . PHE   B 1 304 ? -42.604 3.950   14.349  1.00 92.78  ? 1341 PHE   B CA  1 
ATOM   4505 C C   . PHE   B 1 304 ? -43.909 3.886   15.142  1.00 95.29  ? 1341 PHE   B C   1 
ATOM   4506 O O   . PHE   B 1 304 ? -43.892 3.982   16.367  1.00 97.23  ? 1341 PHE   B O   1 
ATOM   4507 C CB  . PHE   B 1 304 ? -42.331 5.375   13.855  1.00 93.81  ? 1341 PHE   B CB  1 
ATOM   4508 C CG  . PHE   B 1 304 ? -42.283 6.420   14.942  1.00 97.57  ? 1341 PHE   B CG  1 
ATOM   4509 C CD1 . PHE   B 1 304 ? -41.352 6.335   15.967  1.00 99.50  ? 1341 PHE   B CD1 1 
ATOM   4510 C CD2 . PHE   B 1 304 ? -43.172 7.485   14.945  1.00 100.24 ? 1341 PHE   B CD2 1 
ATOM   4511 C CE1 . PHE   B 1 304 ? -41.309 7.294   16.968  1.00 104.12 ? 1341 PHE   B CE1 1 
ATOM   4512 C CE2 . PHE   B 1 304 ? -43.128 8.442   15.947  1.00 104.99 ? 1341 PHE   B CE2 1 
ATOM   4513 C CZ  . PHE   B 1 304 ? -42.197 8.346   16.956  1.00 106.96 ? 1341 PHE   B CZ  1 
ATOM   4514 N N   . SER   B 1 305 ? -45.031 3.723   14.430  1.00 96.13  ? 1342 SER   B N   1 
ATOM   4515 C CA  . SER   B 1 305 ? -46.354 3.740   15.035  1.00 99.59  ? 1342 SER   B CA  1 
ATOM   4516 C C   . SER   B 1 305 ? -46.644 2.425   15.759  1.00 100.12 ? 1342 SER   B C   1 
ATOM   4517 O O   . SER   B 1 305 ? -47.146 2.438   16.881  1.00 102.40 ? 1342 SER   B O   1 
ATOM   4518 C CB  . SER   B 1 305 ? -47.407 4.031   13.998  1.00 100.23 ? 1342 SER   B CB  1 
ATOM   4519 O OG  . SER   B 1 305 ? -47.212 5.315   13.424  1.00 101.22 ? 1342 SER   B OG  1 
ATOM   4520 N N   . THR   B 1 306 ? -46.332 1.299   15.104  1.00 98.80  ? 1343 THR   B N   1 
ATOM   4521 C CA  . THR   B 1 306 ? -46.679 -0.022  15.610  1.00 99.36  ? 1343 THR   B CA  1 
ATOM   4522 C C   . THR   B 1 306 ? -45.874 -0.361  16.863  1.00 100.67 ? 1343 THR   B C   1 
ATOM   4523 O O   . THR   B 1 306 ? -46.413 -0.953  17.796  1.00 102.12 ? 1343 THR   B O   1 
ATOM   4524 C CB  . THR   B 1 306 ? -46.461 -1.109  14.548  1.00 97.53  ? 1343 THR   B CB  1 
ATOM   4525 O OG1 . THR   B 1 306 ? -45.116 -1.015  14.076  1.00 95.98  ? 1343 THR   B OG1 1 
ATOM   4526 C CG2 . THR   B 1 306 ? -47.418 -1.000  13.381  1.00 98.00  ? 1343 THR   B CG2 1 
ATOM   4527 N N   . PHE   B 1 307 ? -44.586 0.008   16.873  1.00 101.17 ? 1344 PHE   B N   1 
ATOM   4528 C CA  . PHE   B 1 307 ? -43.668 -0.410  17.921  1.00 103.34 ? 1344 PHE   B CA  1 
ATOM   4529 C C   . PHE   B 1 307 ? -44.186 0.029   19.290  1.00 106.77 ? 1344 PHE   B C   1 
ATOM   4530 O O   . PHE   B 1 307 ? -44.760 1.108   19.429  1.00 108.17 ? 1344 PHE   B O   1 
ATOM   4531 C CB  . PHE   B 1 307 ? -42.264 0.146   17.669  1.00 104.06 ? 1344 PHE   B CB  1 
ATOM   4532 C CG  . PHE   B 1 307 ? -41.225 -0.318  18.659  1.00 106.77 ? 1344 PHE   B CG  1 
ATOM   4533 C CD1 . PHE   B 1 307 ? -40.873 -1.658  18.741  1.00 106.61 ? 1344 PHE   B CD1 1 
ATOM   4534 C CD2 . PHE   B 1 307 ? -40.614 0.578   19.525  1.00 110.25 ? 1344 PHE   B CD2 1 
ATOM   4535 C CE1 . PHE   B 1 307 ? -39.924 -2.088  19.656  1.00 109.70 ? 1344 PHE   B CE1 1 
ATOM   4536 C CE2 . PHE   B 1 307 ? -39.665 0.145   20.440  1.00 113.35 ? 1344 PHE   B CE2 1 
ATOM   4537 C CZ  . PHE   B 1 307 ? -39.322 -1.186  20.504  1.00 113.11 ? 1344 PHE   B CZ  1 
ATOM   4538 N N   . ILE   B 1 308 ? -43.959 -0.827  20.295  1.00 108.58 ? 1345 ILE   B N   1 
ATOM   4539 C CA  . ILE   B 1 308 ? -44.404 -0.583  21.658  1.00 112.50 ? 1345 ILE   B CA  1 
ATOM   4540 C C   . ILE   B 1 308 ? -43.508 0.494   22.281  1.00 116.02 ? 1345 ILE   B C   1 
ATOM   4541 O O   . ILE   B 1 308 ? -42.319 0.189   22.500  1.00 116.76 ? 1345 ILE   B O   1 
ATOM   4542 C CB  . ILE   B 1 308 ? -44.391 -1.891  22.478  1.00 113.36 ? 1345 ILE   B CB  1 
ATOM   4543 C CG1 . ILE   B 1 308 ? -45.330 -2.947  21.884  1.00 110.93 ? 1345 ILE   B CG1 1 
ATOM   4544 C CG2 . ILE   B 1 308 ? -44.707 -1.618  23.941  1.00 117.95 ? 1345 ILE   B CG2 1 
ATOM   4545 C CD1 . ILE   B 1 308 ? -45.197 -4.318  22.510  1.00 111.36 ? 1345 ILE   B CD1 1 
HETATM 4546 C C4  . A1AB1 C 2 .   ? 8.348   -4.217  20.969  1.00 55.12  ? 1401 A1AB1 A C4  1 
HETATM 4547 C C5  . A1AB1 C 2 .   ? 7.325   -4.283  21.917  1.00 55.14  ? 1401 A1AB1 A C5  1 
HETATM 4548 C C6  . A1AB1 C 2 .   ? 7.046   -5.499  22.540  1.00 54.86  ? 1401 A1AB1 A C6  1 
HETATM 4549 C C8  . A1AB1 C 2 .   ? 10.563  -8.058  21.727  1.00 53.70  ? 1401 A1AB1 A C8  1 
HETATM 4550 C C10 . A1AB1 C 2 .   ? 12.404  -9.595  22.228  1.00 53.29  ? 1401 A1AB1 A C10 1 
HETATM 4551 C C13 . A1AB1 C 2 .   ? 10.955  -7.344  22.858  1.00 53.90  ? 1401 A1AB1 A C13 1 
HETATM 4552 C C15 . A1AB1 C 2 .   ? 11.739  -11.138 19.997  1.00 53.15  ? 1401 A1AB1 A C15 1 
HETATM 4553 C C17 . A1AB1 C 2 .   ? 13.148  -10.746 21.910  1.00 53.01  ? 1401 A1AB1 A C17 1 
HETATM 4554 C C20 . A1AB1 C 2 .   ? 5.204   -1.142  21.815  1.00 56.76  ? 1401 A1AB1 A C20 1 
HETATM 4555 C C21 . A1AB1 C 2 .   ? 4.862   -0.923  23.174  1.00 57.36  ? 1401 A1AB1 A C21 1 
HETATM 4556 C C22 . A1AB1 C 2 .   ? 4.083   0.196   23.488  1.00 57.74  ? 1401 A1AB1 A C22 1 
HETATM 4557 C C1  . A1AB1 C 2 .   ? 7.770   -6.637  22.219  1.00 54.59  ? 1401 A1AB1 A C1  1 
HETATM 4558 C C2  . A1AB1 C 2 .   ? 8.784   -6.567  21.270  1.00 54.48  ? 1401 A1AB1 A C2  1 
HETATM 4559 C C3  . A1AB1 C 2 .   ? 9.070   -5.357  20.648  1.00 55.07  ? 1401 A1AB1 A C3  1 
HETATM 4560 O O7  . A1AB1 C 2 .   ? 9.505   -7.678  20.953  1.00 53.91  ? 1401 A1AB1 A O7  1 
HETATM 4561 C C9  . A1AB1 C 2 .   ? 11.310  -9.223  21.400  1.00 53.44  ? 1401 A1AB1 A C9  1 
HETATM 4562 N N11 . A1AB1 C 2 .   ? 12.721  -8.854  23.299  1.00 53.63  ? 1401 A1AB1 A N11 1 
HETATM 4563 C C12 . A1AB1 C 2 .   ? 12.038  -7.776  23.614  1.00 53.79  ? 1401 A1AB1 A C12 1 
HETATM 4564 C C14 . A1AB1 C 2 .   ? 10.997  -10.018 20.280  1.00 53.39  ? 1401 A1AB1 A C14 1 
HETATM 4565 C C16 . A1AB1 C 2 .   ? 12.825  -11.500 20.817  1.00 52.89  ? 1401 A1AB1 A C16 1 
HETATM 4566 N N18 . A1AB1 C 2 .   ? 6.566   -3.156  22.281  1.00 55.47  ? 1401 A1AB1 A N18 1 
HETATM 4567 C C19 . A1AB1 C 2 .   ? 6.014   -2.307  21.378  1.00 55.99  ? 1401 A1AB1 A C19 1 
HETATM 4568 C C23 . A1AB1 C 2 .   ? 3.673   1.045   22.479  1.00 57.78  ? 1401 A1AB1 A C23 1 
HETATM 4569 N N24 . A1AB1 C 2 .   ? 4.002   0.815   21.219  1.00 57.50  ? 1401 A1AB1 A N24 1 
HETATM 4570 C C25 . A1AB1 C 2 .   ? 4.735   -0.222  20.864  1.00 56.98  ? 1401 A1AB1 A C25 1 
HETATM 4571 F F26 . A1AB1 C 2 .   ? 7.491   -7.811  22.828  1.00 54.28  ? 1401 A1AB1 A F26 1 
HETATM 4572 F F27 . A1AB1 C 2 .   ? 10.057  -5.295  19.728  1.00 56.00  ? 1401 A1AB1 A F27 1 
HETATM 4573 O O28 . A1AB1 C 2 .   ? 11.436  -11.903 18.911  1.00 53.20  ? 1401 A1AB1 A O28 1 
HETATM 4574 C C29 . A1AB1 C 2 .   ? 10.074  -12.293 18.706  1.00 53.36  ? 1401 A1AB1 A C29 1 
HETATM 4575 C C30 . A1AB1 C 2 .   ? 10.034  -13.496 17.764  1.00 53.68  ? 1401 A1AB1 A C30 1 
HETATM 4576 O O31 . A1AB1 C 2 .   ? 10.820  -14.558 18.310  1.00 54.19  ? 1401 A1AB1 A O31 1 
HETATM 4577 O O32 . A1AB1 C 2 .   ? 13.558  -12.615 20.541  1.00 52.45  ? 1401 A1AB1 A O32 1 
HETATM 4578 C C33 . A1AB1 C 2 .   ? 14.680  -12.515 19.656  1.00 52.35  ? 1401 A1AB1 A C33 1 
HETATM 4579 O O34 . A1AB1 C 2 .   ? 6.162   -2.502  20.185  1.00 55.67  ? 1401 A1AB1 A O34 1 
HETATM 4580 O O35 . A1AB1 C 2 .   ? 5.276   -1.774  24.152  1.00 57.18  ? 1401 A1AB1 A O35 1 
HETATM 4581 C C36 . A1AB1 C 2 .   ? 5.899   -1.232  25.322  1.00 57.09  ? 1401 A1AB1 A C36 1 
HETATM 4582 C C4  . A1AB1 D 2 .   ? -19.479 22.591  9.343   1.00 41.24  ? 1401 A1AB1 B C4  1 
HETATM 4583 C C5  . A1AB1 D 2 .   ? -20.316 21.856  8.501   1.00 41.09  ? 1401 A1AB1 B C5  1 
HETATM 4584 C C6  . A1AB1 D 2 .   ? -21.155 20.886  9.046   1.00 41.08  ? 1401 A1AB1 B C6  1 
HETATM 4585 C C8  . A1AB1 D 2 .   ? -21.360 21.555  13.411  1.00 42.09  ? 1401 A1AB1 B C8  1 
HETATM 4586 C C10 . A1AB1 D 2 .   ? -22.465 21.491  15.595  1.00 42.25  ? 1401 A1AB1 B C10 1 
HETATM 4587 C C13 . A1AB1 D 2 .   ? -22.353 22.441  13.008  1.00 42.09  ? 1401 A1AB1 B C13 1 
HETATM 4588 C C15 . A1AB1 D 2 .   ? -20.531 19.705  16.524  1.00 42.56  ? 1401 A1AB1 B C15 1 
HETATM 4589 C C17 . A1AB1 D 2 .   ? -22.521 21.005  16.916  1.00 42.40  ? 1401 A1AB1 B C17 1 
HETATM 4590 C C20 . A1AB1 D 2 .   ? -19.352 22.264  4.866   1.00 40.82  ? 1401 A1AB1 B C20 1 
HETATM 4591 C C21 . A1AB1 D 2 .   ? -20.596 22.399  4.204   1.00 41.08  ? 1401 A1AB1 B C21 1 
HETATM 4592 C C22 . A1AB1 D 2 .   ? -20.596 22.460  2.810   1.00 41.08  ? 1401 A1AB1 B C22 1 
HETATM 4593 C C1  . A1AB1 D 2 .   ? -21.175 20.653  10.408  1.00 41.17  ? 1401 A1AB1 B C1  1 
HETATM 4594 C C2  . A1AB1 D 2 .   ? -20.349 21.389  11.247  1.00 41.43  ? 1401 A1AB1 B C2  1 
HETATM 4595 C C3  . A1AB1 D 2 .   ? -19.499 22.353  10.710  1.00 41.43  ? 1401 A1AB1 B C3  1 
HETATM 4596 O O7  . A1AB1 D 2 .   ? -20.354 21.155  12.588  1.00 41.83  ? 1401 A1AB1 B O7  1 
HETATM 4597 C C9  . A1AB1 D 2 .   ? -21.411 21.062  14.742  1.00 42.16  ? 1401 A1AB1 B C9  1 
HETATM 4598 N N11 . A1AB1 D 2 .   ? -23.389 22.348  15.137  1.00 42.20  ? 1401 A1AB1 B N11 1 
HETATM 4599 C C12 . A1AB1 D 2 .   ? -23.349 22.809  13.905  1.00 42.15  ? 1401 A1AB1 B C12 1 
HETATM 4600 C C14 . A1AB1 D 2 .   ? -20.447 20.162  15.236  1.00 42.26  ? 1401 A1AB1 B C14 1 
HETATM 4601 C C16 . A1AB1 D 2 .   ? -21.572 20.131  17.369  1.00 42.63  ? 1401 A1AB1 B C16 1 
HETATM 4602 N N18 . A1AB1 D 2 .   ? -20.356 22.011  7.105   1.00 40.89  ? 1401 A1AB1 B N18 1 
HETATM 4603 C C19 . A1AB1 D 2 .   ? -19.243 22.164  6.340   1.00 40.70  ? 1401 A1AB1 B C19 1 
HETATM 4604 C C23 . A1AB1 D 2 .   ? -19.402 22.380  2.123   1.00 41.14  ? 1401 A1AB1 B C23 1 
HETATM 4605 N N24 . A1AB1 D 2 .   ? -18.255 22.245  2.765   1.00 41.09  ? 1401 A1AB1 B N24 1 
HETATM 4606 C C25 . A1AB1 D 2 .   ? -18.194 22.179  4.080   1.00 40.89  ? 1401 A1AB1 B C25 1 
HETATM 4607 F F26 . A1AB1 D 2 .   ? -21.999 19.713  10.915  1.00 41.16  ? 1401 A1AB1 B F26 1 
HETATM 4608 F F27 . A1AB1 D 2 .   ? -18.696 23.066  11.528  1.00 41.58  ? 1401 A1AB1 B F27 1 
HETATM 4609 O O28 . A1AB1 D 2 .   ? -19.591 18.838  16.991  1.00 42.88  ? 1401 A1AB1 B O28 1 
HETATM 4610 C C29 . A1AB1 D 2 .   ? -19.585 17.503  16.481  1.00 43.07  ? 1401 A1AB1 B C29 1 
HETATM 4611 C C30 . A1AB1 D 2 .   ? -18.420 16.733  17.107  1.00 43.30  ? 1401 A1AB1 B C30 1 
HETATM 4612 O O31 . A1AB1 D 2 .   ? -18.387 16.971  18.517  1.00 43.60  ? 1401 A1AB1 B O31 1 
HETATM 4613 O O32 . A1AB1 D 2 .   ? -21.643 19.670  18.648  1.00 42.96  ? 1401 A1AB1 B O32 1 
HETATM 4614 C C33 . A1AB1 D 2 .   ? -20.812 20.301  19.625  1.00 43.16  ? 1401 A1AB1 B C33 1 
HETATM 4615 O O34 . A1AB1 D 2 .   ? -18.138 22.196  6.848   1.00 40.59  ? 1401 A1AB1 B O34 1 
HETATM 4616 O O35 . A1AB1 D 2 .   ? -21.762 22.472  4.897   1.00 41.37  ? 1401 A1AB1 B O35 1 
HETATM 4617 C C36 . A1AB1 D 2 .   ? -22.603 23.611  4.694   1.00 41.38  ? 1401 A1AB1 B C36 1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ILE A 16  ? 2.2350 1.8657 1.6135 0.0830  0.0724  -0.0021 1053 ILE A N   
2    C CA  . ILE A 16  ? 2.1681 1.8611 1.6103 0.0504  0.0328  -0.0153 1053 ILE A CA  
3    C C   . ILE A 16  ? 2.0850 1.8608 1.6267 0.0300  0.0536  -0.0061 1053 ILE A C   
4    O O   . ILE A 16  ? 2.0603 1.8600 1.6391 0.0277  0.0771  0.0039  1053 ILE A O   
5    C CB  . ILE A 16  ? 2.1612 1.8533 1.6027 0.0318  -0.0119 -0.0306 1053 ILE A CB  
6    C CG1 . ILE A 16  ? 2.2628 1.8615 1.6005 0.0489  -0.0436 -0.0404 1053 ILE A CG1 
7    C CG2 . ILE A 16  ? 2.0825 1.8431 1.6006 0.0026  -0.0414 -0.0365 1053 ILE A CG2 
8    C CD1 . ILE A 16  ? 2.3402 1.8630 1.5959 0.0757  -0.0207 -0.0369 1053 ILE A CD1 
9    N N   . ASP A 17  ? 2.0492 1.8626 1.6292 0.0163  0.0422  -0.0090 1054 ASP A N   
10   C CA  . ASP A 17  ? 1.9750 1.8506 1.6329 -0.0023 0.0550  -0.0025 1054 ASP A CA  
11   C C   . ASP A 17  ? 1.9211 1.8414 1.6273 -0.0263 0.0329  -0.0112 1054 ASP A C   
12   O O   . ASP A 17  ? 1.9119 1.8387 1.6180 -0.0352 0.0037  -0.0214 1054 ASP A O   
13   C CB  . ASP A 17  ? 1.9599 1.8451 1.6257 -0.0039 0.0529  -0.0024 1054 ASP A CB  
14   C CG  . ASP A 17  ? 1.9039 1.8335 1.6329 -0.0201 0.0659  0.0049  1054 ASP A CG  
15   O OD1 . ASP A 17  ? 1.8921 1.8271 1.6254 -0.0223 0.0635  0.0041  1054 ASP A OD1 
16   O OD2 . ASP A 17  ? 1.8728 1.8262 1.6430 -0.0299 0.0760  0.0119  1054 ASP A OD2 
17   N N   . LEU A 18  ? 1.8844 1.8347 1.6354 -0.0355 0.0476  -0.0040 1055 LEU A N   
18   C CA  . LEU A 18  ? 1.8389 1.8226 1.6259 -0.0537 0.0315  -0.0107 1055 LEU A CA  
19   C C   . LEU A 18  ? 1.7906 1.8108 1.6181 -0.0705 0.0211  -0.0139 1055 LEU A C   
20   O O   . LEU A 18  ? 1.7662 1.8084 1.6160 -0.0824 0.0081  -0.0192 1055 LEU A O   
21   C CB  . LEU A 18  ? 1.8285 1.8214 1.6384 -0.0532 0.0493  -0.0007 1055 LEU A CB  
22   C CG  . LEU A 18  ? 1.7940 1.8185 1.6599 -0.0623 0.0637  0.0133  1055 LEU A CG  
23   C CD1 . LEU A 18  ? 1.8070 1.8220 1.6753 -0.0548 0.0807  0.0247  1055 LEU A CD1 
24   C CD2 . LEU A 18  ? 1.7478 1.8053 1.6498 -0.0838 0.0430  0.0055  1055 LEU A CD2 
25   N N   . SER A 19  ? 1.7773 1.7969 1.6077 -0.0688 0.0290  -0.0097 1056 SER A N   
26   C CA  . SER A 19  ? 1.7360 1.7747 1.5878 -0.0799 0.0211  -0.0126 1056 SER A CA  
27   C C   . SER A 19  ? 1.7394 1.7643 1.5687 -0.0710 0.0206  -0.0133 1056 SER A C   
28   O O   . SER A 19  ? 1.7448 1.7659 1.5781 -0.0716 0.0300  -0.0087 1056 SER A O   
29   C CB  . SER A 19  ? 1.7201 1.7693 1.6031 -0.0907 0.0281  -0.0054 1056 SER A CB  
30   O OG  . SER A 19  ? 1.7379 1.7756 1.6256 -0.0845 0.0460  0.0069  1056 SER A OG  
31   N N   . ALA A 20  ? 1.7336 1.7489 1.5408 -0.0637 0.0061  -0.0180 1057 ALA A N   
32   C CA  . ALA A 20  ? 1.7380 1.7393 1.5233 -0.0535 0.0012  -0.0174 1057 ALA A CA  
33   C C   . ALA A 20  ? 1.7014 1.7272 1.5125 -0.0587 -0.0096 -0.0167 1057 ALA A C   
34   O O   . ALA A 20  ? 1.7092 1.7348 1.5197 -0.0549 -0.0010 -0.0133 1057 ALA A O   
35   C CB  . ALA A 20  ? 1.7776 1.7461 1.5212 -0.0415 -0.0134 -0.0203 1057 ALA A CB  
36   N N   . LEU A 21  ? 1.6633 1.7074 1.4976 -0.0655 -0.0253 -0.0173 1058 LEU A N   
37   C CA  . LEU A 21  ? 1.6287 1.6963 1.4943 -0.0660 -0.0321 -0.0101 1058 LEU A CA  
38   C C   . LEU A 21  ? 1.5963 1.6776 1.4791 -0.0706 -0.0153 -0.0081 1058 LEU A C   
39   O O   . LEU A 21  ? 1.5907 1.6619 1.4608 -0.0753 -0.0045 -0.0132 1058 LEU A O   
40   C CB  . LEU A 21  ? 1.6177 1.6954 1.5061 -0.0712 -0.0575 -0.0074 1058 LEU A CB  
41   C CG  . LEU A 21  ? 1.6507 1.6974 1.5058 -0.0670 -0.0826 -0.0117 1058 LEU A CG  
42   C CD1 . LEU A 21  ? 1.6540 1.7092 1.5405 -0.0754 -0.1163 -0.0061 1058 LEU A CD1 
43   C CD2 . LEU A 21  ? 1.6742 1.7031 1.5024 -0.0538 -0.0829 -0.0093 1058 LEU A CD2 
44   N N   . ASN A 22  ? 1.5729 1.6729 1.4842 -0.0675 -0.0138 0.0019  1059 ASN A N   
45   C CA  . ASN A 22  ? 1.5582 1.6578 1.4712 -0.0651 0.0038  0.0058  1059 ASN A CA  
46   C C   . ASN A 22  ? 1.5535 1.6413 1.4499 -0.0753 0.0058  -0.0049 1059 ASN A C   
47   O O   . ASN A 22  ? 1.5401 1.6387 1.4502 -0.0834 -0.0022 -0.0083 1059 ASN A O   
48   C CB  . ASN A 22  ? 1.5372 1.6605 1.4911 -0.0607 0.0063  0.0210  1059 ASN A CB  
49   C CG  . ASN A 22  ? 1.5436 1.6541 1.4855 -0.0506 0.0301  0.0279  1059 ASN A CG  
50   O OD1 . ASN A 22  ? 1.5282 1.6442 1.4827 -0.0521 0.0349  0.0311  1059 ASN A OD1 
51   N ND2 . ASN A 22  ? 1.5655 1.6510 1.4751 -0.0380 0.0456  0.0304  1059 ASN A ND2 
52   N N   . PRO A 23  ? 1.5648 1.6279 1.4331 -0.0758 0.0137  -0.0091 1060 PRO A N   
53   C CA  . PRO A 23  ? 1.5583 1.6108 1.4191 -0.0873 0.0092  -0.0162 1060 PRO A CA  
54   C C   . PRO A 23  ? 1.5647 1.6073 1.4172 -0.0871 0.0106  -0.0160 1060 PRO A C   
55   O O   . PRO A 23  ? 1.5650 1.5919 1.4065 -0.0959 0.0026  -0.0208 1060 PRO A O   
56   C CB  . PRO A 23  ? 1.5793 1.6046 1.4173 -0.0893 0.0107  -0.0177 1060 PRO A CB  
57   C CG  . PRO A 23  ? 1.6034 1.6125 1.4198 -0.0750 0.0212  -0.0128 1060 PRO A CG  
58   C CD  . PRO A 23  ? 1.5867 1.6270 1.4301 -0.0662 0.0237  -0.0058 1060 PRO A CD  
59   N N   . GLU A 24  ? 1.5693 1.6193 1.4291 -0.0756 0.0208  -0.0076 1061 GLU A N   
60   C CA  . GLU A 24  ? 1.5832 1.6206 1.4318 -0.0703 0.0276  -0.0046 1061 GLU A CA  
61   C C   . GLU A 24  ? 1.5495 1.6150 1.4303 -0.0801 0.0199  -0.0063 1061 GLU A C   
62   O O   . GLU A 24  ? 1.5574 1.6109 1.4259 -0.0807 0.0201  -0.0081 1061 GLU A O   
63   C CB  . GLU A 24  ? 1.6048 1.6369 1.4524 -0.0497 0.0497  0.0112  1061 GLU A CB  
64   C CG  . GLU A 24  ? 1.6363 1.6387 1.4546 -0.0367 0.0645  0.0169  1061 GLU A CG  
65   C CD  . GLU A 24  ? 1.6821 1.6236 1.4297 -0.0351 0.0576  0.0055  1061 GLU A CD  
66   O OE1 . GLU A 24  ? 1.6832 1.6124 1.4170 -0.0439 0.0441  -0.0027 1061 GLU A OE1 
67   O OE2 . GLU A 24  ? 1.7141 1.6167 1.4191 -0.0253 0.0628  0.0056  1061 GLU A OE2 
68   N N   . LEU A 25  ? 1.5130 1.6080 1.4273 -0.0864 0.0116  -0.0058 1062 LEU A N   
69   C CA  . LEU A 25  ? 1.4872 1.6007 1.4252 -0.0953 0.0026  -0.0080 1062 LEU A CA  
70   C C   . LEU A 25  ? 1.4961 1.6002 1.4189 -0.1043 -0.0033 -0.0178 1062 LEU A C   
71   O O   . LEU A 25  ? 1.4959 1.5993 1.4196 -0.1064 -0.0029 -0.0183 1062 LEU A O   
72   C CB  . LEU A 25  ? 1.4630 1.5912 1.4208 -0.0992 -0.0109 -0.0076 1062 LEU A CB  
73   C CG  . LEU A 25  ? 1.4524 1.6000 1.4486 -0.0957 -0.0146 0.0064  1062 LEU A CG  
74   C CD1 . LEU A 25  ? 1.4430 1.6036 1.4692 -0.0974 -0.0096 0.0154  1062 LEU A CD1 
75   C CD2 . LEU A 25  ? 1.4582 1.6059 1.4563 -0.0826 -0.0009 0.0176  1062 LEU A CD2 
76   N N   . VAL A 26  ? 1.5135 1.6110 1.4269 -0.1083 -0.0072 -0.0223 1063 VAL A N   
77   C CA  . VAL A 26  ? 1.5260 1.6211 1.4410 -0.1162 -0.0114 -0.0249 1063 VAL A CA  
78   C C   . VAL A 26  ? 1.5428 1.6240 1.4477 -0.1195 -0.0161 -0.0255 1063 VAL A C   
79   O O   . VAL A 26  ? 1.5326 1.6190 1.4480 -0.1251 -0.0216 -0.0253 1063 VAL A O   
80   C CB  . VAL A 26  ? 1.5389 1.6275 1.4523 -0.1175 -0.0096 -0.0233 1063 VAL A CB  
81   C CG1 . VAL A 26  ? 1.5586 1.6281 1.4554 -0.1167 -0.0097 -0.0229 1063 VAL A CG1 
82   C CG2 . VAL A 26  ? 1.5351 1.6280 1.4667 -0.1240 -0.0103 -0.0185 1063 VAL A CG2 
83   N N   . GLN A 27  ? 1.5719 1.6286 1.4499 -0.1137 -0.0146 -0.0255 1064 GLN A N   
84   C CA  . GLN A 27  ? 1.6017 1.6272 1.4503 -0.1130 -0.0222 -0.0271 1064 GLN A CA  
85   C C   . GLN A 27  ? 1.5993 1.6303 1.4481 -0.1063 -0.0149 -0.0252 1064 GLN A C   
86   O O   . GLN A 27  ? 1.6091 1.6300 1.4502 -0.1099 -0.0248 -0.0270 1064 GLN A O   
87   C CB  . GLN A 27  ? 1.6405 1.6242 1.4443 -0.1031 -0.0189 -0.0271 1064 GLN A CB  
88   C CG  . GLN A 27  ? 1.6901 1.6201 1.4428 -0.1010 -0.0331 -0.0304 1064 GLN A CG  
89   C CD  . GLN A 27  ? 1.6963 1.6129 1.4554 -0.1198 -0.0625 -0.0333 1064 GLN A CD  
90   O OE1 . GLN A 27  ? 1.6587 1.6073 1.4614 -0.1326 -0.0728 -0.0310 1064 GLN A OE1 
91   N NE2 . GLN A 27  ? 1.7427 1.6092 1.4606 -0.1212 -0.0766 -0.0358 1064 GLN A NE2 
92   N N   . ALA A 28  ? 1.5835 1.6309 1.4463 -0.0967 0.0014  -0.0191 1065 ALA A N   
93   C CA  . ALA A 28  ? 1.5731 1.6266 1.4443 -0.0894 0.0125  -0.0127 1065 ALA A CA  
94   C C   . ALA A 28  ? 1.5296 1.6115 1.4333 -0.1008 0.0045  -0.0156 1065 ALA A C   
95   O O   . ALA A 28  ? 1.5309 1.6110 1.4348 -0.0984 0.0084  -0.0133 1065 ALA A O   
96   C CB  . ALA A 28  ? 1.5723 1.6385 1.4642 -0.0773 0.0308  0.0005  1065 ALA A CB  
97   N N   . VAL A 29  ? 1.4898 1.5908 1.4133 -0.1103 -0.0042 -0.0198 1066 VAL A N   
98   C CA  . VAL A 29  ? 1.4559 1.5730 1.3987 -0.1173 -0.0094 -0.0220 1066 VAL A CA  
99   C C   . VAL A 29  ? 1.4454 1.5598 1.3845 -0.1231 -0.0159 -0.0253 1066 VAL A C   
100  O O   . VAL A 29  ? 1.4302 1.5508 1.3769 -0.1249 -0.0161 -0.0257 1066 VAL A O   
101  C CB  . VAL A 29  ? 1.4399 1.5682 1.3985 -0.1191 -0.0139 -0.0214 1066 VAL A CB  
102  C CG1 . VAL A 29  ? 1.4357 1.5734 1.4156 -0.1149 -0.0105 -0.0120 1066 VAL A CG1 
103  C CG2 . VAL A 29  ? 1.4419 1.5647 1.3890 -0.1189 -0.0169 -0.0248 1066 VAL A CG2 
104  N N   . GLN A 30  ? 1.4527 1.5534 1.3795 -0.1241 -0.0214 -0.0252 1067 GLN A N   
105  C CA  . GLN A 30  ? 1.4448 1.5473 1.3830 -0.1310 -0.0311 -0.0228 1067 GLN A CA  
106  C C   . GLN A 30  ? 1.4195 1.5344 1.3717 -0.1310 -0.0291 -0.0205 1067 GLN A C   
107  O O   . GLN A 30  ? 1.4097 1.5369 1.3823 -0.1322 -0.0261 -0.0149 1067 GLN A O   
108  C CB  . GLN A 30  ? 1.4774 1.5532 1.3953 -0.1340 -0.0471 -0.0230 1067 GLN A CB  
109  C CG  . GLN A 30  ? 1.4816 1.5622 1.4263 -0.1445 -0.0641 -0.0156 1067 GLN A CG  
110  C CD  . GLN A 30  ? 1.5235 1.5671 1.4428 -0.1500 -0.0905 -0.0165 1067 GLN A CD  
111  O OE1 . GLN A 30  ? 1.5379 1.5714 1.4679 -0.1597 -0.1060 -0.0123 1067 GLN A OE1 
112  N NE2 . GLN A 30  ? 1.5486 1.5644 1.4292 -0.1432 -0.0973 -0.0213 1067 GLN A NE2 
113  N N   . HIS A 31  ? 1.4045 1.5125 1.3437 -0.1268 -0.0270 -0.0225 1068 HIS A N   
114  C CA  . HIS A 31  ? 1.3815 1.4960 1.3284 -0.1258 -0.0249 -0.0205 1068 HIS A CA  
115  C C   . HIS A 31  ? 1.3576 1.4848 1.3182 -0.1256 -0.0163 -0.0202 1068 HIS A C   
116  O O   . HIS A 31  ? 1.3534 1.4850 1.3224 -0.1243 -0.0137 -0.0161 1068 HIS A O   
117  C CB  . HIS A 31  ? 1.3887 1.4898 1.3171 -0.1190 -0.0192 -0.0211 1068 HIS A CB  
118  C CG  . HIS A 31  ? 1.3807 1.4857 1.3143 -0.1152 -0.0067 -0.0196 1068 HIS A CG  
119  N ND1 . HIS A 31  ? 1.3769 1.4812 1.3095 -0.1136 -0.0041 -0.0190 1068 HIS A ND1 
120  C CD2 . HIS A 31  ? 1.3762 1.4875 1.3241 -0.1134 0.0026  -0.0152 1068 HIS A CD2 
121  C CE1 . HIS A 31  ? 1.3732 1.4869 1.3246 -0.1106 0.0055  -0.0126 1068 HIS A CE1 
122  N NE2 . HIS A 31  ? 1.3716 1.4896 1.3351 -0.1117 0.0089  -0.0098 1068 HIS A NE2 
123  N N   . VAL A 32  ? 1.3452 1.4722 1.3037 -0.1255 -0.0134 -0.0234 1069 VAL A N   
124  C CA  . VAL A 32  ? 1.3390 1.4615 1.2950 -0.1248 -0.0121 -0.0250 1069 VAL A CA  
125  C C   . VAL A 32  ? 1.3354 1.4521 1.2846 -0.1204 -0.0074 -0.0226 1069 VAL A C   
126  O O   . VAL A 32  ? 1.3458 1.4495 1.2829 -0.1145 -0.0013 -0.0208 1069 VAL A O   
127  C CB  . VAL A 32  ? 1.3431 1.4637 1.3023 -0.1274 -0.0182 -0.0268 1069 VAL A CB  
128  C CG1 . VAL A 32  ? 1.3419 1.4637 1.2986 -0.1264 -0.0207 -0.0275 1069 VAL A CG1 
129  C CG2 . VAL A 32  ? 1.3630 1.4665 1.3124 -0.1290 -0.0262 -0.0293 1069 VAL A CG2 
130  N N   . VAL A 33  ? 1.3210 1.4421 1.2746 -0.1210 -0.0072 -0.0207 1070 VAL A N   
131  C CA  . VAL A 33  ? 1.3233 1.4381 1.2742 -0.1146 0.0021  -0.0145 1070 VAL A CA  
132  C C   . VAL A 33  ? 1.3114 1.4362 1.2857 -0.1119 0.0108  -0.0018 1070 VAL A C   
133  O O   . VAL A 33  ? 1.2985 1.4371 1.2943 -0.1191 0.0017  0.0011  1070 VAL A O   
134  C CB  . VAL A 33  ? 1.3210 1.4377 1.2747 -0.1169 0.0001  -0.0143 1070 VAL A CB  
135  C CG1 . VAL A 33  ? 1.3321 1.4443 1.2916 -0.1095 0.0141  -0.0032 1070 VAL A CG1 
136  C CG2 . VAL A 33  ? 1.3274 1.4361 1.2629 -0.1165 -0.0067 -0.0228 1070 VAL A CG2 
137  N N   . ILE A 34  ? 1.3212 1.4340 1.2887 -0.0991 0.0286  0.0079  1071 ILE A N   
138  C CA  . ILE A 34  ? 1.3184 1.4434 1.3175 -0.0925 0.0428  0.0269  1071 ILE A CA  
139  C C   . ILE A 34  ? 1.3302 1.4514 1.3419 -0.0813 0.0635  0.0442  1071 ILE A C   
140  O O   . ILE A 34  ? 1.3503 1.4437 1.3220 -0.0707 0.0731  0.0393  1071 ILE A O   
141  C CB  . ILE A 34  ? 1.3356 1.4446 1.3131 -0.0811 0.0539  0.0282  1071 ILE A CB  
142  C CG1 . ILE A 34  ? 1.3332 1.4624 1.3538 -0.0743 0.0675  0.0509  1071 ILE A CG1 
143  C CG2 . ILE A 34  ? 1.3762 1.4408 1.2970 -0.0643 0.0679  0.0243  1071 ILE A CG2 
144  C CD1 . ILE A 34  ? 1.3032 1.4644 1.3686 -0.0907 0.0449  0.0533  1071 ILE A CD1 
145  N N   . GLY A 35  ? 1.3171 1.4647 1.3872 -0.0834 0.0691  0.0667  1072 GLY A N   
146  C CA  . GLY A 35  ? 1.3267 1.4770 1.4266 -0.0737 0.0916  0.0899  1072 GLY A CA  
147  C C   . GLY A 35  ? 1.3634 1.4892 1.4419 -0.0445 0.1310  0.1079  1072 GLY A C   
148  O O   . GLY A 35  ? 1.3683 1.4904 1.4410 -0.0352 0.1396  0.1126  1072 GLY A O   
149  N N   . PRO A 36  ? 1.1833 1.2809 1.3235 -0.1117 -0.0304 -0.0106 1073 PRO A N   
150  C CA  . PRO A 36  ? 1.1680 1.2813 1.3077 -0.1254 -0.0161 0.0106  1073 PRO A CA  
151  C C   . PRO A 36  ? 1.1570 1.2999 1.3151 -0.1313 -0.0143 0.0065  1073 PRO A C   
152  O O   . PRO A 36  ? 1.1429 1.3101 1.3003 -0.1322 0.0001  0.0124  1073 PRO A O   
153  C CB  . PRO A 36  ? 1.1944 1.2787 1.3403 -0.1462 -0.0233 0.0277  1073 PRO A CB  
154  C CG  . PRO A 36  ? 1.2137 1.2641 1.3639 -0.1342 -0.0451 0.0159  1073 PRO A CG  
155  C CD  . PRO A 36  ? 1.2080 1.2732 1.3663 -0.1172 -0.0495 -0.0116 1073 PRO A CD  
156  N N   . SER A 37  ? 1.1665 1.3082 1.3483 -0.1335 -0.0327 -0.0082 1074 SER A N   
157  C CA  . SER A 37  ? 1.1600 1.3319 1.3757 -0.1372 -0.0390 -0.0196 1074 SER A CA  
158  C C   . SER A 37  ? 1.1512 1.3345 1.3440 -0.1136 -0.0440 -0.0297 1074 SER A C   
159  O O   . SER A 37  ? 1.1418 1.3553 1.3630 -0.1122 -0.0453 -0.0366 1074 SER A O   
160  C CB  . SER A 37  ? 1.1818 1.3440 1.4281 -0.1426 -0.0641 -0.0360 1074 SER A CB  
161  O OG  . SER A 37  ? 1.1984 1.3339 1.4108 -0.1209 -0.0821 -0.0516 1074 SER A OG  
162  N N   . SER A 38  ? 1.1596 1.3159 1.3008 -0.0966 -0.0469 -0.0326 1075 SER A N   
163  C CA  . SER A 38  ? 1.1717 1.3186 1.2701 -0.0788 -0.0543 -0.0379 1075 SER A CA  
164  C C   . SER A 38  ? 1.1504 1.2963 1.2189 -0.0765 -0.0309 -0.0217 1075 SER A C   
165  O O   . SER A 38  ? 1.1724 1.2934 1.1879 -0.0694 -0.0254 -0.0212 1075 SER A O   
166  C CB  . SER A 38  ? 1.2155 1.3281 1.2649 -0.0684 -0.0686 -0.0528 1075 SER A CB  
167  O OG  . SER A 38  ? 1.2156 1.3165 1.2483 -0.0717 -0.0492 -0.0532 1075 SER A OG  
168  N N   . LEU A 39  ? 1.1124 1.2837 1.2122 -0.0855 -0.0157 -0.0099 1076 LEU A N   
169  C CA  . LEU A 39  ? 1.0912 1.2625 1.1693 -0.0830 0.0024  0.0032  1076 LEU A CA  
170  C C   . LEU A 39  ? 1.0661 1.2682 1.1789 -0.0924 0.0146  0.0089  1076 LEU A C   
171  O O   . LEU A 39  ? 1.0581 1.2649 1.1879 -0.1098 0.0254  0.0169  1076 LEU A O   
172  C CB  . LEU A 39  ? 1.0900 1.2439 1.1503 -0.0868 0.0162  0.0100  1076 LEU A CB  
173  C CG  . LEU A 39  ? 1.0754 1.2293 1.1226 -0.0860 0.0323  0.0217  1076 LEU A CG  
174  C CD1 . LEU A 39  ? 1.0889 1.2306 1.0992 -0.0768 0.0337  0.0214  1076 LEU A CD1 
175  C CD2 . LEU A 39  ? 1.0728 1.2155 1.1241 -0.0888 0.0388  0.0218  1076 LEU A CD2 
176  N N   . ILE A 40  ? 1.0640 1.2815 1.1815 -0.0816 0.0120  0.0034  1077 ILE A N   
177  C CA  . ILE A 40  ? 1.0506 1.3014 1.1974 -0.0885 0.0287  0.0021  1077 ILE A CA  
178  C C   . ILE A 40  ? 1.0398 1.2763 1.1515 -0.0816 0.0394  0.0138  1077 ILE A C   
179  O O   . ILE A 40  ? 1.0458 1.2611 1.1302 -0.0660 0.0275  0.0136  1077 ILE A O   
180  C CB  . ILE A 40  ? 1.0565 1.3427 1.2523 -0.0783 0.0151  -0.0223 1077 ILE A CB  
181  C CG1 . ILE A 40  ? 1.0656 1.3712 1.3096 -0.0876 0.0032  -0.0376 1077 ILE A CG1 
182  C CG2 . ILE A 40  ? 1.0448 1.3706 1.2702 -0.0833 0.0380  -0.0309 1077 ILE A CG2 
183  C CD1 . ILE A 40  ? 1.0875 1.3558 1.3032 -0.0754 -0.0273 -0.0396 1077 ILE A CD1 
184  N N   . VAL A 41  ? 1.0306 1.2718 1.1375 -0.0955 0.0596  0.0243  1078 VAL A N   
185  C CA  . VAL A 41  ? 1.0279 1.2548 1.1053 -0.0898 0.0666  0.0333  1078 VAL A CA  
186  C C   . VAL A 41  ? 1.0337 1.2905 1.1250 -0.0899 0.0798  0.0230  1078 VAL A C   
187  O O   . VAL A 41  ? 1.0430 1.3179 1.1422 -0.1091 0.0988  0.0224  1078 VAL A O   
188  C CB  . VAL A 41  ? 1.0312 1.2310 1.0851 -0.1012 0.0709  0.0495  1078 VAL A CB  
189  C CG1 . VAL A 41  ? 1.0336 1.2202 1.0635 -0.0955 0.0739  0.0554  1078 VAL A CG1 
190  C CG2 . VAL A 41  ? 1.0259 1.2042 1.0775 -0.0981 0.0597  0.0504  1078 VAL A CG2 
191  N N   . HIS A 42  ? 1.0386 1.2964 1.1290 -0.0703 0.0704  0.0134  1079 HIS A N   
192  C CA  . HIS A 42  ? 1.0509 1.3375 1.1578 -0.0648 0.0806  -0.0034 1079 HIS A CA  
193  C C   . HIS A 42  ? 1.0689 1.3369 1.1361 -0.0708 0.0935  0.0087  1079 HIS A C   
194  O O   . HIS A 42  ? 1.0726 1.3175 1.1206 -0.0568 0.0819  0.0116  1079 HIS A O   
195  C CB  . HIS A 42  ? 1.0560 1.3407 1.1782 -0.0380 0.0556  -0.0204 1079 HIS A CB  
196  C CG  . HIS A 42  ? 1.0639 1.3524 1.2144 -0.0279 0.0310  -0.0325 1079 HIS A CG  
197  N ND1 . HIS A 42  ? 1.0638 1.3954 1.2681 -0.0353 0.0356  -0.0512 1079 HIS A ND1 
198  C CD2 . HIS A 42  ? 1.0871 1.3338 1.2120 -0.0126 -0.0010 -0.0282 1079 HIS A CD2 
199  C CE1 . HIS A 42  ? 1.0784 1.3970 1.2955 -0.0204 0.0019  -0.0606 1079 HIS A CE1 
200  N NE2 . HIS A 42  ? 1.0981 1.3594 1.2578 -0.0064 -0.0215 -0.0449 1079 HIS A NE2 
201  N N   . PHE A 43  ? 1.0981 1.3694 1.1487 -0.0935 0.1145  0.0162  1080 PHE A N   
202  C CA  . PHE A 43  ? 1.1334 1.3756 1.1350 -0.1001 0.1197  0.0287  1080 PHE A CA  
203  C C   . PHE A 43  ? 1.1337 1.3941 1.1306 -0.0893 0.1288  0.0092  1080 PHE A C   
204  O O   . PHE A 43  ? 1.1489 1.3812 1.1084 -0.0839 0.1222  0.0148  1080 PHE A O   
205  C CB  . PHE A 43  ? 1.1938 1.4180 1.1624 -0.1297 0.1338  0.0447  1080 PHE A CB  
206  C CG  . PHE A 43  ? 1.2462 1.5087 1.2306 -0.1535 0.1652  0.0320  1080 PHE A CG  
207  C CD1 . PHE A 43  ? 1.2905 1.5796 1.2628 -0.1602 0.1925  0.0136  1080 PHE A CD1 
208  C CD2 . PHE A 43  ? 1.2572 1.5322 1.2730 -0.1714 0.1697  0.0344  1080 PHE A CD2 
209  C CE1 . PHE A 43  ? 1.3205 1.6536 1.3158 -0.1871 0.2295  -0.0036 1080 PHE A CE1 
210  C CE2 . PHE A 43  ? 1.2873 1.6029 1.3285 -0.1985 0.2024  0.0197  1080 PHE A CE2 
211  C CZ  . PHE A 43  ? 1.3164 1.6640 1.3493 -0.2078 0.2351  -0.0001 1080 PHE A CZ  
212  N N   . ASN A 44  ? 1.1155 1.4246 1.1570 -0.0843 0.1412  -0.0184 1081 ASN A N   
213  C CA  . ASN A 44  ? 1.1185 1.4522 1.1681 -0.0704 0.1493  -0.0463 1081 ASN A CA  
214  C C   . ASN A 44  ? 1.0900 1.3968 1.1411 -0.0403 0.1164  -0.0479 1081 ASN A C   
215  O O   . ASN A 44  ? 1.1045 1.3983 1.1315 -0.0307 0.1139  -0.0553 1081 ASN A O   
216  C CB  . ASN A 44  ? 1.1193 1.5191 1.2345 -0.0705 0.1686  -0.0840 1081 ASN A CB  
217  C CG  . ASN A 44  ? 1.0879 1.5044 1.2651 -0.0550 0.1429  -0.0935 1081 ASN A CG  
218  O OD1 . ASN A 44  ? 1.0724 1.4487 1.2322 -0.0491 0.1165  -0.0687 1081 ASN A OD1 
219  N ND2 . ASN A 44  ? 1.0846 1.5607 1.3349 -0.0488 0.1499  -0.1330 1081 ASN A ND2 
220  N N   . GLU A 45  ? 1.0550 1.3475 1.1275 -0.0282 0.0909  -0.0408 1082 GLU A N   
221  C CA  . GLU A 45  ? 1.0483 1.3036 1.1120 -0.0076 0.0610  -0.0371 1082 GLU A CA  
222  C C   . GLU A 45  ? 1.0396 1.2510 1.0621 -0.0180 0.0576  -0.0079 1082 GLU A C   
223  O O   . GLU A 45  ? 1.0315 1.2305 1.0481 -0.0290 0.0578  0.0095  1082 GLU A O   
224  C CB  . GLU A 45  ? 1.0441 1.2925 1.1325 0.0055  0.0350  -0.0417 1082 GLU A CB  
225  C CG  . GLU A 45  ? 1.0455 1.3396 1.1924 0.0212  0.0287  -0.0782 1082 GLU A CG  
226  C CD  . GLU A 45  ? 1.0549 1.3316 1.2211 0.0374  -0.0083 -0.0838 1082 GLU A CD  
227  O OE1 . GLU A 45  ? 1.0788 1.2997 1.2124 0.0512  -0.0408 -0.0736 1082 GLU A OE1 
228  O OE2 . GLU A 45  ? 1.0460 1.3588 1.2549 0.0342  -0.0067 -0.0979 1082 GLU A OE2 
229  N N   . VAL A 46  ? 1.0388 1.2299 1.0403 -0.0131 0.0530  -0.0082 1083 VAL A N   
230  C CA  . VAL A 46  ? 1.0273 1.1852 1.0051 -0.0220 0.0485  0.0111  1083 VAL A CA  
231  C C   . VAL A 46  ? 1.0339 1.1594 1.0119 -0.0129 0.0289  0.0123  1083 VAL A C   
232  O O   . VAL A 46  ? 1.0493 1.1700 1.0312 0.0022  0.0165  -0.0028 1083 VAL A O   
233  C CB  . VAL A 46  ? 1.0423 1.1963 0.9915 -0.0286 0.0558  0.0108  1083 VAL A CB  
234  C CG1 . VAL A 46  ? 1.0668 1.2333 1.0075 -0.0167 0.0589  -0.0124 1083 VAL A CG1 
235  C CG2 . VAL A 46  ? 1.0445 1.1647 0.9831 -0.0318 0.0409  0.0230  1083 VAL A CG2 
236  N N   . ILE A 47  ? 1.0295 1.1323 1.0051 -0.0244 0.0276  0.0280  1084 ILE A N   
237  C CA  . ILE A 47  ? 1.0498 1.1180 1.0212 -0.0263 0.0162  0.0330  1084 ILE A CA  
238  C C   . ILE A 47  ? 1.0586 1.1124 1.0364 -0.0302 0.0112  0.0313  1084 ILE A C   
239  O O   . ILE A 47  ? 1.0460 1.1101 1.0331 -0.0364 0.0160  0.0322  1084 ILE A O   
240  C CB  . ILE A 47  ? 1.0485 1.1038 1.0120 -0.0417 0.0252  0.0463  1084 ILE A CB  
241  C CG1 . ILE A 47  ? 1.0495 1.1123 1.0048 -0.0353 0.0217  0.0457  1084 ILE A CG1 
242  C CG2 . ILE A 47  ? 1.0826 1.0959 1.0308 -0.0539 0.0214  0.0539  1084 ILE A CG2 
243  C CD1 . ILE A 47  ? 1.0603 1.1080 0.9964 -0.0497 0.0302  0.0562  1084 ILE A CD1 
244  N N   . GLY A 48  ? 1.0858 1.1107 1.0608 -0.0256 -0.0043 0.0273  1085 GLY A N   
245  C CA  . GLY A 48  ? 1.1005 1.1085 1.0887 -0.0304 -0.0133 0.0232  1085 GLY A CA  
246  C C   . GLY A 48  ? 1.1058 1.1261 1.0910 -0.0158 -0.0230 0.0085  1085 GLY A C   
247  O O   . GLY A 48  ? 1.1211 1.1300 1.1186 -0.0180 -0.0347 0.0030  1085 GLY A O   
248  N N   . ARG A 49  ? 1.1028 1.1452 1.0704 -0.0028 -0.0176 0.0000  1086 ARG A N   
249  C CA  . ARG A 49  ? 1.1171 1.1681 1.0625 0.0059  -0.0192 -0.0136 1086 ARG A CA  
250  C C   . ARG A 49  ? 1.1164 1.1587 1.0530 -0.0042 -0.0228 -0.0049 1086 ARG A C   
251  O O   . ARG A 49  ? 1.1429 1.1679 1.0574 0.0016  -0.0385 -0.0142 1086 ARG A O   
252  C CB  . ARG A 49  ? 1.1512 1.1830 1.0935 0.0219  -0.0395 -0.0335 1086 ARG A CB  
253  C CG  . ARG A 49  ? 1.1626 1.1984 1.1167 0.0380  -0.0449 -0.0483 1086 ARG A CG  
254  C CD  . ARG A 49  ? 1.2044 1.2212 1.1567 0.0572  -0.0674 -0.0736 1086 ARG A CD  
255  N NE  . ARG A 49  ? 1.2316 1.2613 1.1527 0.0630  -0.0606 -0.0918 1086 ARG A NE  
256  C CZ  . ARG A 49  ? 1.2535 1.3135 1.1616 0.0758  -0.0460 -0.1198 1086 ARG A CZ  
257  N NH1 . ARG A 49  ? 1.2877 1.3504 1.1488 0.0739  -0.0353 -0.1320 1086 ARG A NH1 
258  N NH2 . ARG A 49  ? 1.2480 1.3343 1.1890 0.0896  -0.0426 -0.1382 1086 ARG A NH2 
259  N N   . GLY A 50  ? 1.0911 1.1414 1.0436 -0.0172 -0.0132 0.0099  1087 GLY A N   
260  C CA  . GLY A 50  ? 1.0944 1.1350 1.0458 -0.0234 -0.0228 0.0151  1087 GLY A CA  
261  C C   . GLY A 50  ? 1.0959 1.1185 1.0809 -0.0224 -0.0464 0.0064  1087 GLY A C   
262  O O   . GLY A 50  ? 1.1179 1.1238 1.0990 -0.0198 -0.0684 0.0029  1087 GLY A O   
263  N N   . HIS A 51  ? 1.0785 1.1002 1.0968 -0.0260 -0.0449 0.0020  1088 HIS A N   
264  C CA  . HIS A 51  ? 1.0790 1.0909 1.1441 -0.0308 -0.0619 -0.0092 1088 HIS A CA  
265  C C   . HIS A 51  ? 1.0491 1.0812 1.1670 -0.0468 -0.0478 -0.0095 1088 HIS A C   
266  O O   . HIS A 51  ? 1.0496 1.0854 1.2188 -0.0489 -0.0636 -0.0251 1088 HIS A O   
267  C CB  . HIS A 51  ? 1.0930 1.0882 1.1670 -0.0332 -0.0653 -0.0137 1088 HIS A CB  
268  C CG  . HIS A 51  ? 1.1245 1.1001 1.1633 -0.0141 -0.0868 -0.0249 1088 HIS A CG  
269  N ND1 . HIS A 51  ? 1.1520 1.1137 1.1758 -0.0018 -0.1135 -0.0383 1088 HIS A ND1 
270  C CD2 . HIS A 51  ? 1.1391 1.1047 1.1531 -0.0037 -0.0872 -0.0283 1088 HIS A CD2 
271  C CE1 . HIS A 51  ? 1.1824 1.1292 1.1697 0.0136  -0.1241 -0.0502 1088 HIS A CE1 
272  N NE2 . HIS A 51  ? 1.1718 1.1243 1.1597 0.0140  -0.1082 -0.0463 1088 HIS A NE2 
273  N N   . PHE A 52  ? 1.0249 1.0716 1.1335 -0.0566 -0.0196 0.0028  1089 PHE A N   
274  C CA  . PHE A 52  ? 1.0044 1.0726 1.1549 -0.0718 -0.0001 -0.0010 1089 PHE A CA  
275  C C   . PHE A 52  ? 0.9739 1.0533 1.1140 -0.0642 -0.0018 0.0025  1089 PHE A C   
276  O O   . PHE A 52  ? 0.9642 1.0582 1.1056 -0.0725 0.0198  0.0067  1089 PHE A O   
277  C CB  . PHE A 52  ? 1.0216 1.0868 1.1579 -0.0906 0.0296  0.0092  1089 PHE A CB  
278  C CG  . PHE A 52  ? 1.0627 1.1061 1.2084 -0.1056 0.0313  0.0079  1089 PHE A CG  
279  C CD1 . PHE A 52  ? 1.0756 1.1311 1.2827 -0.1255 0.0404  -0.0087 1089 PHE A CD1 
280  C CD2 . PHE A 52  ? 1.0933 1.1034 1.1930 -0.1005 0.0218  0.0200  1089 PHE A CD2 
281  C CE1 . PHE A 52  ? 1.1101 1.1410 1.3257 -0.1453 0.0435  -0.0086 1089 PHE A CE1 
282  C CE2 . PHE A 52  ? 1.1327 1.1113 1.2368 -0.1160 0.0185  0.0207  1089 PHE A CE2 
283  C CZ  . PHE A 52  ? 1.1418 1.1289 1.3006 -0.1409 0.0310  0.0086  1089 PHE A CZ  
284  N N   . GLY A 53  ? 0.9639 1.0284 1.0867 -0.0499 -0.0300 0.0011  1090 GLY A N   
285  C CA  . GLY A 53  ? 0.9464 1.0065 1.0498 -0.0456 -0.0376 0.0077  1090 GLY A CA  
286  C C   . GLY A 53  ? 0.9238 0.9856 0.9718 -0.0479 -0.0183 0.0260  1090 GLY A C   
287  O O   . GLY A 53  ? 0.9196 0.9849 0.9438 -0.0470 -0.0063 0.0301  1090 GLY A O   
288  N N   . CYS A 54  ? 0.9028 0.9620 0.9384 -0.0504 -0.0188 0.0336  1091 CYS A N   
289  C CA  . CYS A 54  ? 0.8840 0.9490 0.8796 -0.0560 -0.0011 0.0474  1091 CYS A CA  
290  C C   . CYS A 54  ? 0.8316 0.9229 0.8483 -0.0610 0.0226  0.0476  1091 CYS A C   
291  O O   . CYS A 54  ? 0.8212 0.9188 0.8511 -0.0657 0.0271  0.0484  1091 CYS A O   
292  C CB  . CYS A 54  ? 0.9132 0.9556 0.8840 -0.0611 -0.0137 0.0569  1091 CYS A CB  
293  S SG  . CYS A 54  ? 0.9857 0.9755 0.8987 -0.0584 -0.0469 0.0619  1091 CYS A SG  
294  N N   . VAL A 55  ? 1.0988 1.4049 1.4404 -0.2279 -0.0649 0.1557  1092 VAL A N   
295  C CA  . VAL A 55  ? 1.0522 1.3512 1.4376 -0.2428 -0.0822 0.1441  1092 VAL A CA  
296  C C   . VAL A 55  ? 1.0294 1.3245 1.4695 -0.2651 -0.0698 0.1430  1092 VAL A C   
297  O O   . VAL A 55  ? 1.0149 1.3346 1.4704 -0.2715 -0.0558 0.1374  1092 VAL A O   
298  C CB  . VAL A 55  ? 1.0116 1.3451 1.3969 -0.2416 -0.1015 0.1249  1092 VAL A CB  
299  C CG1 . VAL A 55  ? 0.9877 1.3096 1.4087 -0.2554 -0.1205 0.1157  1092 VAL A CG1 
300  C CG2 . VAL A 55  ? 1.0201 1.3668 1.3598 -0.2199 -0.1120 0.1236  1092 VAL A CG2 
301  N N   . TYR A 56  ? 1.0241 1.2901 1.4959 -0.2777 -0.0738 0.1467  1093 TYR A N   
302  C CA  . TYR A 56  ? 1.0051 1.2730 1.5385 -0.2986 -0.0640 0.1458  1093 TYR A CA  
303  C C   . TYR A 56  ? 0.9720 1.2463 1.5484 -0.3117 -0.0925 0.1362  1093 TYR A C   
304  O O   . TYR A 56  ? 0.9668 1.2321 1.5176 -0.3068 -0.1155 0.1311  1093 TYR A O   
305  C CB  . TYR A 56  ? 1.0462 1.2770 1.5828 -0.3063 -0.0392 0.1584  1093 TYR A CB  
306  C CG  . TYR A 56  ? 1.0866 1.2976 1.5642 -0.2898 -0.0139 0.1730  1093 TYR A CG  
307  C CD1 . TYR A 56  ? 1.1022 1.3175 1.5805 -0.2937 0.0162  0.1781  1093 TYR A CD1 
308  C CD2 . TYR A 56  ? 1.1166 1.3024 1.5362 -0.2692 -0.0190 0.1832  1093 TYR A CD2 
309  C CE1 . TYR A 56  ? 1.1496 1.3453 1.5653 -0.2783 0.0377  0.1933  1093 TYR A CE1 
310  C CE2 . TYR A 56  ? 1.1623 1.3317 1.5252 -0.2501 0.0011  0.2005  1093 TYR A CE2 
311  C CZ  . TYR A 56  ? 1.1802 1.3545 1.5377 -0.2551 0.0282  0.2060  1093 TYR A CZ  
312  O OH  . TYR A 56  ? 1.2339 1.3909 1.5271 -0.2359 0.0465  0.2249  1093 TYR A OH  
313  N N   . HIS A 57  ? 0.9507 1.2419 1.5926 -0.3278 -0.0904 0.1343  1094 HIS A N   
314  C CA  . HIS A 57  ? 0.9334 1.2337 1.6204 -0.3415 -0.1189 0.1283  1094 HIS A CA  
315  C C   . HIS A 57  ? 0.9668 1.2348 1.6539 -0.3562 -0.1224 0.1291  1094 HIS A C   
316  O O   . HIS A 57  ? 1.0031 1.2393 1.6630 -0.3549 -0.0975 0.1363  1094 HIS A O   
317  C CB  . HIS A 57  ? 0.9099 1.2450 1.6733 -0.3508 -0.1149 0.1280  1094 HIS A CB  
318  C CG  . HIS A 57  ? 0.8796 1.2408 1.6472 -0.3386 -0.1106 0.1253  1094 HIS A CG  
319  N ND1 . HIS A 57  ? 0.8559 1.2403 1.6584 -0.3368 -0.1325 0.1230  1094 HIS A ND1 
320  C CD2 . HIS A 57  ? 0.8768 1.2413 1.6136 -0.3287 -0.0841 0.1241  1094 HIS A CD2 
321  C CE1 . HIS A 57  ? 0.8395 1.2359 1.6346 -0.3262 -0.1160 0.1201  1094 HIS A CE1 
322  N NE2 . HIS A 57  ? 0.8510 1.2376 1.6060 -0.3232 -0.0865 0.1187  1094 HIS A NE2 
323  N N   . GLY A 58  ? 0.9629 1.2366 1.6771 -0.3710 -0.1523 0.1216  1095 GLY A N   
324  C CA  . GLY A 58  ? 0.9987 1.2425 1.7144 -0.3909 -0.1559 0.1174  1095 GLY A CA  
325  C C   . GLY A 58  ? 0.9929 1.2609 1.7555 -0.4121 -0.1908 0.1077  1095 GLY A C   
326  O O   . GLY A 58  ? 0.9637 1.2670 1.7488 -0.4061 -0.2151 0.1074  1095 GLY A O   
327  N N   . THR A 59  ? 1.0263 1.2737 1.8010 -0.4373 -0.1918 0.1000  1096 THR A N   
328  C CA  . THR A 59  ? 1.0314 1.3021 1.8437 -0.4618 -0.2273 0.0884  1096 THR A CA  
329  C C   . THR A 59  ? 1.0787 1.2997 1.8435 -0.4811 -0.2304 0.0763  1096 THR A C   
330  O O   . THR A 59  ? 1.1143 1.3014 1.8794 -0.4964 -0.2015 0.0731  1096 THR A O   
331  C CB  . THR A 59  ? 1.0267 1.3414 1.9313 -0.4821 -0.2238 0.0865  1096 THR A CB  
332  O OG1 . THR A 59  ? 0.9859 1.3400 1.9309 -0.4620 -0.2157 0.0978  1096 THR A OG1 
333  C CG2 . THR A 59  ? 1.0364 1.3871 1.9851 -0.5077 -0.2654 0.0746  1096 THR A CG2 
334  N N   . LEU A 60  ? 1.0849 1.2967 1.8063 -0.4807 -0.2616 0.0690  1097 LEU A N   
335  C CA  . LEU A 60  ? 1.1361 1.2957 1.8044 -0.4979 -0.2628 0.0558  1097 LEU A CA  
336  C C   . LEU A 60  ? 1.1644 1.3449 1.8665 -0.5358 -0.2942 0.0388  1097 LEU A C   
337  O O   . LEU A 60  ? 1.1485 1.3688 1.8644 -0.5376 -0.3343 0.0373  1097 LEU A O   
338  C CB  . LEU A 60  ? 1.1319 1.2669 1.7291 -0.4762 -0.2742 0.0561  1097 LEU A CB  
339  C CG  . LEU A 60  ? 1.1858 1.2604 1.7211 -0.4894 -0.2704 0.0425  1097 LEU A CG  
340  C CD1 . LEU A 60  ? 1.2180 1.2391 1.7262 -0.4803 -0.2257 0.0483  1097 LEU A CD1 
341  C CD2 . LEU A 60  ? 1.1794 1.2419 1.6575 -0.4730 -0.2881 0.0397  1097 LEU A CD2 
342  N N   . LEU A 61  ? 1.2131 1.3654 1.9257 -0.5663 -0.2750 0.0260  1098 LEU A N   
343  C CA  . LEU A 61  ? 1.2502 1.4216 1.9920 -0.6085 -0.3022 0.0050  1098 LEU A CA  
344  C C   . LEU A 61  ? 1.2902 1.4181 1.9565 -0.6206 -0.3214 -0.0098 1098 LEU A C   
345  O O   . LEU A 61  ? 1.3333 1.3921 1.9447 -0.6257 -0.2910 -0.0172 1098 LEU A O   
346  C CB  . LEU A 61  ? 1.2930 1.4448 2.0717 -0.6399 -0.2672 -0.0064 1098 LEU A CB  
347  C CG  . LEU A 61  ? 1.2657 1.4778 2.1405 -0.6467 -0.2599 -0.0016 1098 LEU A CG  
348  C CD1 . LEU A 61  ? 1.2519 1.5451 2.1957 -0.6683 -0.3107 -0.0117 1098 LEU A CD1 
349  C CD2 . LEU A 61  ? 1.2136 1.4399 2.0977 -0.6046 -0.2408 0.0236  1098 LEU A CD2 
350  N N   . ASP A 62  ? 1.2797 1.4455 1.9420 -0.6238 -0.3696 -0.0130 1099 ASP A N   
351  C CA  . ASP A 62  ? 1.3241 1.4529 1.9151 -0.6404 -0.3913 -0.0291 1099 ASP A CA  
352  C C   . ASP A 62  ? 1.3853 1.5082 1.9884 -0.6925 -0.3985 -0.0561 1099 ASP A C   
353  O O   . ASP A 62  ? 1.3812 1.5555 2.0607 -0.7145 -0.4058 -0.0610 1099 ASP A O   
354  C CB  . ASP A 62  ? 1.3016 1.4699 1.8796 -0.6259 -0.4387 -0.0211 1099 ASP A CB  
355  C CG  . ASP A 62  ? 1.3472 1.4672 1.8359 -0.6347 -0.4546 -0.0341 1099 ASP A CG  
356  O OD1 . ASP A 62  ? 1.3912 1.4449 1.8278 -0.6486 -0.4259 -0.0491 1099 ASP A OD1 
357  O OD2 . ASP A 62  ? 1.3429 1.4880 1.8132 -0.6269 -0.4929 -0.0284 1099 ASP A OD2 
358  N N   . ASN A 63  ? 1.4441 1.5048 1.9730 -0.7138 -0.3942 -0.0756 1100 ASN A N   
359  C CA  . ASN A 63  ? 1.5114 1.5553 2.0387 -0.7677 -0.3958 -0.1061 1100 ASN A CA  
360  C C   . ASN A 63  ? 1.5200 1.6356 2.0747 -0.7965 -0.4577 -0.1176 1100 ASN A C   
361  O O   . ASN A 63  ? 1.5688 1.6998 2.1468 -0.8449 -0.4682 -0.1435 1100 ASN A O   
362  C CB  . ASN A 63  ? 1.5791 1.5285 2.0156 -0.7816 -0.3671 -0.1243 1100 ASN A CB  
363  C CG  . ASN A 63  ? 1.5886 1.5174 1.9489 -0.7680 -0.3931 -0.1241 1100 ASN A CG  
364  O OD1 . ASN A 63  ? 1.5415 1.5206 1.9106 -0.7433 -0.4298 -0.1074 1100 ASN A OD1 
365  N ND2 . ASN A 63  ? 1.6535 1.5031 1.9377 -0.7838 -0.3698 -0.1430 1100 ASN A ND2 
366  N N   . ASP A 64  ? 1.4756 1.6341 2.0258 -0.7668 -0.4978 -0.0984 1101 ASP A N   
367  C CA  . ASP A 64  ? 1.4793 1.7124 2.0589 -0.7833 -0.5595 -0.1007 1101 ASP A CA  
368  C C   . ASP A 64  ? 1.4457 1.7618 2.1407 -0.7947 -0.5692 -0.0985 1101 ASP A C   
369  O O   . ASP A 64  ? 1.4864 1.8444 2.2172 -0.8385 -0.5956 -0.1206 1101 ASP A O   
370  C CB  . ASP A 64  ? 1.4444 1.6969 1.9955 -0.7420 -0.5911 -0.0754 1101 ASP A CB  
371  C CG  . ASP A 64  ? 1.4768 1.6529 1.9172 -0.7331 -0.5833 -0.0796 1101 ASP A CG  
372  O OD1 . ASP A 64  ? 1.4532 1.6358 1.8642 -0.7015 -0.6027 -0.0609 1101 ASP A OD1 
373  O OD2 . ASP A 64  ? 1.5282 1.6361 1.9138 -0.7581 -0.5545 -0.1020 1101 ASP A OD2 
374  N N   . GLY A 65  ? 1.3724 1.7129 2.1254 -0.7569 -0.5461 -0.0737 1102 GLY A N   
375  C CA  . GLY A 65  ? 1.3365 1.7514 2.2024 -0.7633 -0.5466 -0.0701 1102 GLY A CA  
376  C C   . GLY A 65  ? 1.2583 1.7031 2.1720 -0.7138 -0.5327 -0.0385 1102 GLY A C   
377  O O   . GLY A 65  ? 1.2306 1.6744 2.1943 -0.7075 -0.4907 -0.0335 1102 GLY A O   
378  N N   . LYS A 66  ? 1.2282 1.6945 2.1212 -0.6805 -0.5655 -0.0182 1103 LYS A N   
379  C CA  . LYS A 66  ? 1.1613 1.6614 2.1019 -0.6367 -0.5567 0.0096  1103 LYS A CA  
380  C C   . LYS A 66  ? 1.1274 1.5619 2.0185 -0.6083 -0.5045 0.0189  1103 LYS A C   
381  O O   . LYS A 66  ? 1.1539 1.5196 1.9614 -0.6117 -0.4876 0.0098  1103 LYS A O   
382  C CB  . LYS A 66  ? 1.1559 1.6898 2.0820 -0.6117 -0.6046 0.0277  1103 LYS A CB  
383  C CG  . LYS A 66  ? 1.1871 1.7961 2.1632 -0.6329 -0.6631 0.0240  1103 LYS A CG  
384  C CD  . LYS A 66  ? 1.1592 1.8527 2.2646 -0.6365 -0.6653 0.0283  1103 LYS A CD  
385  C CE  . LYS A 66  ? 1.1943 1.9718 2.3544 -0.6589 -0.7269 0.0231  1103 LYS A CE  
386  N NZ  . LYS A 66  ? 1.2057 2.0058 2.3350 -0.6279 -0.7759 0.0474  1103 LYS A NZ  
387  N N   . LYS A 67  ? 1.0701 1.5298 2.0153 -0.5801 -0.4798 0.0369  1104 LYS A N   
388  C CA  . LYS A 67  ? 1.0391 1.4503 1.9508 -0.5558 -0.4303 0.0454  1104 LYS A CA  
389  C C   . LYS A 67  ? 1.0058 1.4024 1.8645 -0.5189 -0.4356 0.0606  1104 LYS A C   
390  O O   . LYS A 67  ? 1.0001 1.4303 1.8680 -0.5077 -0.4710 0.0695  1104 LYS A O   
391  C CB  . LYS A 67  ? 1.0091 1.4525 2.0032 -0.5508 -0.3971 0.0533  1104 LYS A CB  
392  C CG  . LYS A 67  ? 1.0389 1.4946 2.0897 -0.5890 -0.3840 0.0367  1104 LYS A CG  
393  C CD  . LYS A 67  ? 1.0130 1.5044 2.1509 -0.5856 -0.3514 0.0438  1104 LYS A CD  
394  C CE  . LYS A 67  ? 1.0482 1.5487 2.2423 -0.6269 -0.3344 0.0247  1104 LYS A CE  
395  N NZ  . LYS A 67  ? 1.0709 1.6300 2.3140 -0.6582 -0.3836 0.0087  1104 LYS A NZ  
396  N N   . ILE A 68  ? 0.9871 1.3339 1.7910 -0.5003 -0.3991 0.0636  1105 ILE A N   
397  C CA  . ILE A 68  ? 0.9595 1.2890 1.7101 -0.4696 -0.3976 0.0729  1105 ILE A CA  
398  C C   . ILE A 68  ? 0.9165 1.2458 1.6803 -0.4452 -0.3570 0.0837  1105 ILE A C   
399  O O   . ILE A 68  ? 0.9228 1.2282 1.6832 -0.4492 -0.3242 0.0819  1105 ILE A O   
400  C CB  . ILE A 68  ? 0.9921 1.2625 1.6513 -0.4729 -0.3984 0.0617  1105 ILE A CB  
401  C CG1 . ILE A 68  ? 1.0406 1.3054 1.6779 -0.5020 -0.4361 0.0480  1105 ILE A CG1 
402  C CG2 . ILE A 68  ? 0.9689 1.2249 1.5784 -0.4433 -0.3935 0.0686  1105 ILE A CG2 
403  C CD1 . ILE A 68  ? 1.0811 1.2818 1.6311 -0.5096 -0.4304 0.0340  1105 ILE A CD1 
404  N N   . HIS A 69  ? 0.8776 1.2301 1.6514 -0.4208 -0.3581 0.0949  1106 HIS A N   
405  C CA  . HIS A 69  ? 0.8418 1.1944 1.6178 -0.3994 -0.3213 0.1023  1106 HIS A CA  
406  C C   . HIS A 69  ? 0.8420 1.1522 1.5370 -0.3861 -0.3062 0.0977  1106 HIS A C   
407  O O   . HIS A 69  ? 0.8462 1.1427 1.4952 -0.3795 -0.3235 0.0940  1106 HIS A O   
408  C CB  . HIS A 69  ? 0.8112 1.2010 1.6280 -0.3812 -0.3250 0.1131  1106 HIS A CB  
409  C CG  . HIS A 69  ? 0.7820 1.1779 1.6122 -0.3652 -0.2856 0.1182  1106 HIS A CG  
410  N ND1 . HIS A 69  ? 0.7592 1.1763 1.6140 -0.3480 -0.2776 0.1254  1106 HIS A ND1 
411  C CD2 . HIS A 69  ? 0.7793 1.1589 1.5956 -0.3649 -0.2506 0.1167  1106 HIS A CD2 
412  C CE1 . HIS A 69  ? 0.7438 1.1594 1.5997 -0.3408 -0.2390 0.1253  1106 HIS A CE1 
413  N NE2 . HIS A 69  ? 0.7564 1.1504 1.5869 -0.3504 -0.2236 0.1210  1106 HIS A NE2 
414  N N   . CYS A 70  ? 0.8405 1.1310 1.5192 -0.3816 -0.2735 0.0985  1107 CYS A N   
415  C CA  . CYS A 70  ? 0.8431 1.1004 1.4531 -0.3670 -0.2593 0.0956  1107 CYS A CA  
416  C C   . CYS A 70  ? 0.8231 1.0877 1.4304 -0.3501 -0.2257 0.1029  1107 CYS A C   
417  O O   . CYS A 70  ? 0.8125 1.0979 1.4666 -0.3532 -0.2096 0.1092  1107 CYS A O   
418  C CB  . CYS A 70  ? 0.8846 1.0983 1.4599 -0.3795 -0.2576 0.0895  1107 CYS A CB  
419  S SG  . CYS A 70  ? 0.9123 1.1135 1.5255 -0.3963 -0.2313 0.0938  1107 CYS A SG  
420  N N   . ALA A 71  ? 0.8200 1.0696 1.3720 -0.3328 -0.2157 0.1011  1108 ALA A N   
421  C CA  . ALA A 71  ? 0.8121 1.0694 1.3484 -0.3166 -0.1879 0.1074  1108 ALA A CA  
422  C C   . ALA A 71  ? 0.8445 1.0668 1.3353 -0.3073 -0.1751 0.1121  1108 ALA A C   
423  O O   . ALA A 71  ? 0.8565 1.0581 1.3102 -0.3020 -0.1855 0.1063  1108 ALA A O   
424  C CB  . ALA A 71  ? 0.7838 1.0661 1.3009 -0.3026 -0.1881 0.1010  1108 ALA A CB  
425  N N   . VAL A 72  ? 0.8636 1.0765 1.3566 -0.3042 -0.1496 0.1237  1109 VAL A N   
426  C CA  . VAL A 72  ? 0.9059 1.0792 1.3584 -0.2933 -0.1334 0.1332  1109 VAL A CA  
427  C C   . VAL A 72  ? 0.9090 1.0972 1.3254 -0.2678 -0.1168 0.1433  1109 VAL A C   
428  O O   . VAL A 72  ? 0.8912 1.1094 1.3219 -0.2677 -0.1067 0.1449  1109 VAL A O   
429  C CB  . VAL A 72  ? 0.9416 1.0826 1.4183 -0.3112 -0.1151 0.1399  1109 VAL A CB  
430  C CG1 . VAL A 72  ? 0.9961 1.0851 1.4271 -0.2986 -0.0938 0.1517  1109 VAL A CG1 
431  C CG2 . VAL A 72  ? 0.9391 1.0786 1.4581 -0.3402 -0.1351 0.1273  1109 VAL A CG2 
432  N N   . LYS A 73  ? 0.9370 1.1052 1.3069 -0.2463 -0.1140 0.1498  1110 LYS A N   
433  C CA  . LYS A 73  ? 0.9497 1.1359 1.2820 -0.2196 -0.1028 0.1613  1110 LYS A CA  
434  C C   . LYS A 73  ? 1.0121 1.1512 1.3082 -0.2011 -0.0846 0.1814  1110 LYS A C   
435  O O   . LYS A 73  ? 1.0360 1.1350 1.3240 -0.2009 -0.0858 0.1806  1110 LYS A O   
436  C CB  . LYS A 73  ? 0.9193 1.1441 1.2334 -0.2047 -0.1207 0.1490  1110 LYS A CB  
437  C CG  . LYS A 73  ? 0.9305 1.1879 1.2089 -0.1781 -0.1148 0.1578  1110 LYS A CG  
438  C CD  . LYS A 73  ? 0.9021 1.2027 1.1699 -0.1667 -0.1313 0.1419  1110 LYS A CD  
439  C CE  . LYS A 73  ? 0.9173 1.2592 1.1528 -0.1410 -0.1294 0.1499  1110 LYS A CE  
440  N NZ  . LYS A 73  ? 0.8905 1.2801 1.1234 -0.1328 -0.1444 0.1308  1110 LYS A NZ  
441  N N   . SER A 74  ? 1.0454 1.1864 1.3156 -0.1852 -0.0658 0.1996  1111 SER A N   
442  C CA  . SER A 74  ? 1.1144 1.2099 1.3431 -0.1615 -0.0459 0.2240  1111 SER A CA  
443  C C   . SER A 74  ? 1.1271 1.2526 1.3162 -0.1246 -0.0570 0.2325  1111 SER A C   
444  O O   . SER A 74  ? 1.1070 1.2867 1.2847 -0.1156 -0.0651 0.2308  1111 SER A O   
445  C CB  . SER A 74  ? 1.1529 1.2272 1.3709 -0.1651 -0.0178 0.2413  1111 SER A CB  
446  O OG  . SER A 74  ? 1.2262 1.2478 1.3986 -0.1404 0.0042  0.2679  1111 SER A OG  
447  N N   . LEU A 75  ? 1.1669 1.2583 1.3377 -0.1043 -0.0559 0.2404  1112 LEU A N   
448  C CA  . LEU A 75  ? 1.1831 1.3052 1.3262 -0.0667 -0.0668 0.2487  1112 LEU A CA  
449  C C   . LEU A 75  ? 1.2627 1.3546 1.3609 -0.0317 -0.0470 0.2840  1112 LEU A C   
450  O O   . LEU A 75  ? 1.3188 1.3472 1.4017 -0.0174 -0.0286 0.3000  1112 LEU A O   
451  C CB  . LEU A 75  ? 1.1785 1.2804 1.3317 -0.0638 -0.0747 0.2358  1112 LEU A CB  
452  C CG  . LEU A 75  ? 1.1130 1.2548 1.2971 -0.0876 -0.0982 0.2035  1112 LEU A CG  
453  C CD1 . LEU A 75  ? 1.0865 1.2116 1.3020 -0.1290 -0.0997 0.1886  1112 LEU A CD1 
454  C CD2 . LEU A 75  ? 1.1206 1.2436 1.3028 -0.0781 -0.1026 0.1933  1112 LEU A CD2 
455  N N   . ASN A 76  ? 1.2771 1.4124 1.3501 -0.0182 -0.0497 0.2959  1113 ASN A N   
456  C CA  . ASN A 76  ? 1.3597 1.4697 1.3816 0.0157  -0.0328 0.3323  1113 ASN A CA  
457  C C   . ASN A 76  ? 1.3754 1.5393 1.3743 0.0599  -0.0535 0.3442  1113 ASN A C   
458  O O   . ASN A 76  ? 1.3936 1.6057 1.3602 0.0781  -0.0626 0.3569  1113 ASN A O   
459  C CB  . ASN A 76  ? 1.3773 1.4947 1.3786 0.0013  -0.0202 0.3395  1113 ASN A CB  
460  C CG  . ASN A 76  ? 1.3655 1.4383 1.4003 -0.0414 0.0007  0.3267  1113 ASN A CG  
461  O OD1 . ASN A 76  ? 1.4085 1.4093 1.4455 -0.0476 0.0245  0.3364  1113 ASN A OD1 
462  N ND2 . ASN A 76  ? 1.3116 1.4279 1.3755 -0.0714 -0.0062 0.3039  1113 ASN A ND2 
463  N N   . ARG A 77  ? 1.3729 1.5303 1.3899 0.0756  -0.0605 0.3388  1114 ARG A N   
464  C CA  . ARG A 77  ? 1.3874 1.5975 1.3956 0.1187  -0.0788 0.3486  1114 ARG A CA  
465  C C   . ARG A 77  ? 1.4295 1.5792 1.4407 0.1445  -0.0634 0.3617  1114 ARG A C   
466  O O   . ARG A 77  ? 1.4034 1.5850 1.4399 0.1566  -0.0766 0.3471  1114 ARG A O   
467  C CB  . ARG A 77  ? 1.3108 1.6091 1.3541 0.1037  -0.1085 0.3125  1114 ARG A CB  
468  C CG  . ARG A 77  ? 1.2712 1.6284 1.3138 0.0757  -0.1204 0.2947  1114 ARG A CG  
469  C CD  . ARG A 77  ? 1.2088 1.6504 1.2812 0.0657  -0.1455 0.2608  1114 ARG A CD  
470  N NE  . ARG A 77  ? 1.1736 1.6637 1.2471 0.0349  -0.1517 0.2396  1114 ARG A NE  
471  C CZ  . ARG A 77  ? 1.1254 1.6879 1.2195 0.0202  -0.1684 0.2081  1114 ARG A CZ  
472  N NH1 . ARG A 77  ? 1.1063 1.7083 1.2218 0.0353  -0.1825 0.1950  1114 ARG A NH1 
473  N NH2 . ARG A 77  ? 1.0994 1.6918 1.1934 -0.0105 -0.1671 0.1885  1114 ARG A NH2 
474  N N   . ILE A 78  ? 1.4988 1.5575 1.4837 0.1514  -0.0312 0.3879  1115 ILE A N   
475  C CA  . ILE A 78  ? 1.5453 1.5297 1.5312 0.1683  -0.0081 0.3973  1115 ILE A CA  
476  C C   . ILE A 78  ? 1.6451 1.5483 1.5840 0.1973  0.0265  0.4402  1115 ILE A C   
477  O O   . ILE A 78  ? 1.6694 1.5446 1.5842 0.1808  0.0411  0.4512  1115 ILE A O   
478  C CB  . ILE A 78  ? 1.5077 1.4459 1.5270 0.1184  0.0000  0.3629  1115 ILE A CB  
479  C CG1 . ILE A 78  ? 1.5479 1.4236 1.5713 0.1319  0.0195  0.3625  1115 ILE A CG1 
480  C CG2 . ILE A 78  ? 1.5217 1.4045 1.5363 0.0795  0.0207  0.3620  1115 ILE A CG2 
481  C CD1 . ILE A 78  ? 1.5136 1.3533 1.5642 0.0824  0.0218  0.3258  1115 ILE A CD1 
482  N N   . THR A 79  ? 1.7067 1.5688 1.6330 0.2413  0.0431  0.4642  1116 THR A N   
483  C CA  . THR A 79  ? 1.8143 1.5893 1.6932 0.2748  0.0808  0.5078  1116 THR A CA  
484  C C   . THR A 79  ? 1.8482 1.5117 1.7296 0.2366  0.1223  0.4964  1116 THR A C   
485  O O   . THR A 79  ? 1.9445 1.5186 1.7862 0.2569  0.1624  0.5291  1116 THR A O   
486  C CB  . THR A 79  ? 1.8727 1.6516 1.7401 0.3419  0.0828  0.5405  1116 THR A CB  
487  O OG1 . THR A 79  ? 1.8564 1.6084 1.7605 0.3368  0.0921  0.5177  1116 THR A OG1 
488  C CG2 . THR A 79  ? 1.8399 1.7393 1.7102 0.3776  0.0388  0.5489  1116 THR A CG2 
489  N N   . GLU A 83  ? 1.7031 1.4891 1.7546 0.3257  0.0872  0.4084  1120 GLU A N   
490  C CA  . GLU A 83  ? 1.6269 1.4899 1.6803 0.2936  0.0496  0.3948  1120 GLU A CA  
491  C C   . GLU A 83  ? 1.5874 1.4069 1.6426 0.2247  0.0522  0.3594  1120 GLU A C   
492  O O   . GLU A 83  ? 1.5061 1.3828 1.5857 0.1894  0.0245  0.3250  1120 GLU A O   
493  C CB  . GLU A 83  ? 1.6706 1.5403 1.6877 0.3226  0.0485  0.4364  1120 GLU A CB  
494  C CG  . GLU A 83  ? 1.6036 1.5455 1.6187 0.2912  0.0160  0.4237  1120 GLU A CG  
495  C CD  . GLU A 83  ? 1.5205 1.5835 1.5693 0.2901  -0.0255 0.3987  1120 GLU A CD  
496  O OE1 . GLU A 83  ? 1.4447 1.5363 1.5151 0.2413  -0.0417 0.3609  1120 GLU A OE1 
497  O OE2 . GLU A 83  ? 1.5353 1.6641 1.5892 0.3384  -0.0410 0.4173  1120 GLU A OE2 
498  N N   . VAL A 84  ? 1.6497 1.3682 1.6796 0.2067  0.0866  0.3687  1121 VAL A N   
499  C CA  . VAL A 84  ? 1.6242 1.2999 1.6584 0.1428  0.0903  0.3371  1121 VAL A CA  
500  C C   . VAL A 84  ? 1.6121 1.2609 1.6622 0.1179  0.0948  0.3022  1121 VAL A C   
501  O O   . VAL A 84  ? 1.5561 1.2185 1.6203 0.0684  0.0765  0.2682  1121 VAL A O   
502  C CB  . VAL A 84  ? 1.7000 1.2785 1.7053 0.1291  0.1285  0.3549  1121 VAL A CB  
503  C CG1 . VAL A 84  ? 1.7191 1.3180 1.7017 0.1514  0.1271  0.3892  1121 VAL A CG1 
504  C CG2 . VAL A 84  ? 1.7980 1.2757 1.7823 0.1529  0.1752  0.3701  1121 VAL A CG2 
505  N N   . SER A 85  ? 1.6696 1.2789 1.7157 0.1541  0.1204  0.3123  1122 SER A N   
506  C CA  . SER A 85  ? 1.6747 1.2480 1.7291 0.1341  0.1322  0.2809  1122 SER A CA  
507  C C   . SER A 85  ? 1.5842 1.2467 1.6670 0.1171  0.0932  0.2492  1122 SER A C   
508  O O   . SER A 85  ? 1.5634 1.2061 1.6471 0.0727  0.0890  0.2141  1122 SER A O   
509  C CB  . SER A 85  ? 1.7529 1.2770 1.8027 0.1840  0.1685  0.3012  1122 SER A CB  
510  O OG  . SER A 85  ? 1.8457 1.2821 1.8655 0.2032  0.2084  0.3337  1122 SER A OG  
511  N N   . GLN A 86  ? 1.5378 1.2968 1.6400 0.1516  0.0657  0.2618  1123 GLN A N   
512  C CA  . GLN A 86  ? 1.4581 1.3038 1.5882 0.1407  0.0338  0.2333  1123 GLN A CA  
513  C C   . GLN A 86  ? 1.3892 1.2598 1.5204 0.0864  0.0068  0.2082  1123 GLN A C   
514  O O   . GLN A 86  ? 1.3410 1.2396 1.4844 0.0583  -0.0091 0.1763  1123 GLN A O   
515  C CB  . GLN A 86  ? 1.4377 1.3806 1.5880 0.1905  0.0137  0.2534  1123 GLN A CB  
516  C CG  . GLN A 86  ? 1.3757 1.4030 1.5599 0.1882  -0.0084 0.2239  1123 GLN A CG  
517  C CD  . GLN A 86  ? 1.2959 1.3924 1.4881 0.1506  -0.0420 0.2004  1123 GLN A CD  
518  O OE1 . GLN A 86  ? 1.2832 1.3754 1.4598 0.1293  -0.0518 0.2077  1123 GLN A OE1 
519  N NE2 . GLN A 86  ? 1.2459 1.4055 1.4644 0.1425  -0.0562 0.1715  1123 GLN A NE2 
520  N N   . PHE A 87  ? 1.3891 1.2466 1.5074 0.0731  0.0046  0.2238  1124 PHE A N   
521  C CA  . PHE A 87  ? 1.3285 1.2117 1.4538 0.0269  -0.0187 0.2048  1124 PHE A CA  
522  C C   . PHE A 87  ? 1.3326 1.1542 1.4530 -0.0218 -0.0132 0.1767  1124 PHE A C   
523  O O   . PHE A 87  ? 1.2783 1.1316 1.4097 -0.0538 -0.0363 0.1503  1124 PHE A O   
524  C CB  . PHE A 87  ? 1.3401 1.2209 1.4553 0.0278  -0.0164 0.2297  1124 PHE A CB  
525  C CG  . PHE A 87  ? 1.2855 1.1902 1.4139 -0.0168 -0.0359 0.2128  1124 PHE A CG  
526  C CD1 . PHE A 87  ? 1.2122 1.1924 1.3607 -0.0303 -0.0654 0.1924  1124 PHE A CD1 
527  C CD2 . PHE A 87  ? 1.3105 1.1622 1.4344 -0.0451 -0.0219 0.2171  1124 PHE A CD2 
528  C CE1 . PHE A 87  ? 1.1674 1.1670 1.3309 -0.0673 -0.0805 0.1794  1124 PHE A CE1 
529  C CE2 . PHE A 87  ? 1.2614 1.1403 1.4056 -0.0830 -0.0393 0.2027  1124 PHE A CE2 
530  C CZ  . PHE A 87  ? 1.1908 1.1424 1.3545 -0.0921 -0.0686 0.1853  1124 PHE A CZ  
531  N N   . LEU A 88  ? 1.4022 1.1346 1.5031 -0.0276 0.0181  0.1829  1125 LEU A N   
532  C CA  . LEU A 88  ? 1.4198 1.0915 1.5114 -0.0768 0.0239  0.1561  1125 LEU A CA  
533  C C   . LEU A 88  ? 1.4128 1.0794 1.5001 -0.0853 0.0213  0.1285  1125 LEU A C   
534  O O   . LEU A 88  ? 1.4019 1.0519 1.4823 -0.1292 0.0092  0.1011  1125 LEU A O   
535  C CB  . LEU A 88  ? 1.5070 1.0829 1.5770 -0.0807 0.0638  0.1681  1125 LEU A CB  
536  C CG  . LEU A 88  ? 1.5159 1.0768 1.5883 -0.1009 0.0681  0.1805  1125 LEU A CG  
537  C CD1 . LEU A 88  ? 1.5238 1.1105 1.5935 -0.0553 0.0750  0.2185  1125 LEU A CD1 
538  C CD2 . LEU A 88  ? 1.5953 1.0575 1.6490 -0.1307 0.1041  0.1732  1125 LEU A CD2 
539  N N   . THR A 89  ? 1.4227 1.1046 1.5138 -0.0428 0.0330  0.1364  1126 THR A N   
540  C CA  . THR A 89  ? 1.4195 1.0991 1.5090 -0.0473 0.0355  0.1105  1126 THR A CA  
541  C C   . THR A 89  ? 1.3429 1.0884 1.4435 -0.0750 -0.0009 0.0862  1126 THR A C   
542  O O   . THR A 89  ? 1.3449 1.0653 1.4302 -0.1071 -0.0037 0.0583  1126 THR A O   
543  C CB  . THR A 89  ? 1.4389 1.1410 1.5433 0.0079  0.0527  0.1257  1126 THR A CB  
544  O OG1 . THR A 89  ? 1.5202 1.1504 1.6108 0.0349  0.0899  0.1509  1126 THR A OG1 
545  C CG2 . THR A 89  ? 1.4387 1.1390 1.5458 0.0038  0.0603  0.0976  1126 THR A CG2 
546  N N   . GLU A 90  ? 1.2832 1.1084 1.4059 -0.0625 -0.0262 0.0974  1127 GLU A N   
547  C CA  . GLU A 90  ? 1.2148 1.1018 1.3492 -0.0853 -0.0566 0.0773  1127 GLU A CA  
548  C C   . GLU A 90  ? 1.2025 1.0634 1.3273 -0.1330 -0.0724 0.0655  1127 GLU A C   
549  O O   . GLU A 90  ? 1.1695 1.0488 1.2922 -0.1594 -0.0914 0.0444  1127 GLU A O   
550  C CB  . GLU A 90  ? 1.1653 1.1395 1.3238 -0.0593 -0.0741 0.0920  1127 GLU A CB  
551  C CG  . GLU A 90  ? 1.1704 1.1908 1.3444 -0.0139 -0.0666 0.0998  1127 GLU A CG  
552  C CD  . GLU A 90  ? 1.1302 1.2409 1.3236 0.0097  -0.0854 0.1127  1127 GLU A CD  
553  O OE1 . GLU A 90  ? 1.1314 1.2942 1.3422 0.0455  -0.0847 0.1172  1127 GLU A OE1 
554  O OE2 . GLU A 90  ? 1.1023 1.2329 1.2944 -0.0082 -0.1003 0.1171  1127 GLU A OE2 
555  N N   . GLY A 91  ? 1.2330 1.0522 1.3533 -0.1428 -0.0636 0.0801  1128 GLY A N   
556  C CA  . GLY A 91  ? 1.2292 1.0265 1.3479 -0.1873 -0.0775 0.0695  1128 GLY A CA  
557  C C   . GLY A 91  ? 1.2594 1.0074 1.3524 -0.2224 -0.0791 0.0423  1128 GLY A C   
558  O O   . GLY A 91  ? 1.2381 0.9965 1.3312 -0.2566 -0.1038 0.0281  1128 GLY A O   
559  N N   . ILE A 92  ? 1.3151 1.0087 1.3847 -0.2125 -0.0518 0.0359  1129 ILE A N   
560  C CA  . ILE A 92  ? 1.3556 0.9950 1.3918 -0.2453 -0.0479 0.0087  1129 ILE A CA  
561  C C   . ILE A 92  ? 1.3083 0.9901 1.3400 -0.2518 -0.0703 -0.0090 1129 ILE A C   
562  O O   . ILE A 92  ? 1.3162 0.9800 1.3238 -0.2886 -0.0873 -0.0285 1129 ILE A O   
563  C CB  . ILE A 92  ? 1.4316 1.0005 1.4454 -0.2292 -0.0063 0.0066  1129 ILE A CB  
564  C CG1 . ILE A 92  ? 1.4887 1.0039 1.5019 -0.2231 0.0218  0.0249  1129 ILE A CG1 
565  C CG2 . ILE A 92  ? 1.4781 0.9901 1.4509 -0.2652 -0.0001 -0.0246 1129 ILE A CG2 
566  C CD1 . ILE A 92  ? 1.5634 1.0110 1.5600 -0.1968 0.0677  0.0293  1129 ILE A CD1 
567  N N   . ILE A 93  ? 1.2633 1.0010 1.3165 -0.2163 -0.0694 -0.0023 1130 ILE A N   
568  C CA  . ILE A 93  ? 1.2234 0.9995 1.2742 -0.2199 -0.0827 -0.0201 1130 ILE A CA  
569  C C   . ILE A 93  ? 1.1669 0.9882 1.2282 -0.2417 -0.1166 -0.0207 1130 ILE A C   
570  O O   . ILE A 93  ? 1.1627 0.9787 1.2029 -0.2663 -0.1307 -0.0380 1130 ILE A O   
571  C CB  . ILE A 93  ? 1.1963 1.0266 1.2743 -0.1774 -0.0710 -0.0144 1130 ILE A CB  
572  C CG1 . ILE A 93  ? 1.2516 1.0399 1.3267 -0.1495 -0.0361 -0.0098 1130 ILE A CG1 
573  C CG2 . ILE A 93  ? 1.1609 1.0308 1.2387 -0.1851 -0.0805 -0.0359 1130 ILE A CG2 
574  C CD1 . ILE A 93  ? 1.3102 1.0231 1.3477 -0.1729 -0.0149 -0.0339 1130 ILE A CD1 
575  N N   . MET A 94  ? 1.1293 0.9908 1.2210 -0.2310 -0.1268 -0.0005 1131 MET A N   
576  C CA  . MET A 94  ? 1.0757 0.9844 1.1859 -0.2454 -0.1538 0.0016  1131 MET A CA  
577  C C   . MET A 94  ? 1.0895 0.9637 1.1860 -0.2845 -0.1720 -0.0055 1131 MET A C   
578  O O   . MET A 94  ? 1.0631 0.9578 1.1583 -0.3016 -0.1941 -0.0128 1131 MET A O   
579  C CB  . MET A 94  ? 1.0489 1.0004 1.1920 -0.2257 -0.1545 0.0245  1131 MET A CB  
580  C CG  . MET A 94  ? 1.0187 1.0290 1.1781 -0.1911 -0.1487 0.0304  1131 MET A CG  
581  S SD  . MET A 94  ? 0.9646 1.0368 1.1343 -0.1994 -0.1655 0.0127  1131 MET A SD  
582  C CE  . MET A 94  ? 0.9304 1.0788 1.1264 -0.1652 -0.1619 0.0257  1131 MET A CE  
583  N N   . LYS A 95  ? 1.1319 0.9547 1.2187 -0.2980 -0.1619 -0.0030 1132 LYS A N   
584  C CA  . LYS A 95  ? 1.1514 0.9482 1.2302 -0.3369 -0.1802 -0.0107 1132 LYS A CA  
585  C C   . LYS A 95  ? 1.1738 0.9420 1.2102 -0.3617 -0.1927 -0.0327 1132 LYS A C   
586  O O   . LYS A 95  ? 1.1711 0.9490 1.2041 -0.3878 -0.2214 -0.0375 1132 LYS A O   
587  C CB  . LYS A 95  ? 1.2074 0.9510 1.2821 -0.3479 -0.1596 -0.0078 1132 LYS A CB  
588  C CG  . LYS A 95  ? 1.2451 0.9609 1.3111 -0.3929 -0.1763 -0.0210 1132 LYS A CG  
589  C CD  . LYS A 95  ? 1.1997 0.9709 1.3049 -0.4076 -0.2091 -0.0143 1132 LYS A CD  
590  C CE  . LYS A 95  ? 1.2396 0.9928 1.3426 -0.4518 -0.2282 -0.0279 1132 LYS A CE  
591  N NZ  . LYS A 95  ? 1.1957 1.0093 1.3467 -0.4619 -0.2596 -0.0195 1132 LYS A NZ  
592  N N   . ASP A 96  ? 1.1980 0.9315 1.2020 -0.3520 -0.1704 -0.0448 1133 ASP A N   
593  C CA  . ASP A 96  ? 1.2331 0.9273 1.1870 -0.3761 -0.1751 -0.0668 1133 ASP A CA  
594  C C   . ASP A 96  ? 1.1874 0.9196 1.1382 -0.3650 -0.1844 -0.0712 1133 ASP A C   
595  O O   . ASP A 96  ? 1.2183 0.9193 1.1300 -0.3702 -0.1726 -0.0884 1133 ASP A O   
596  C CB  . ASP A 96  ? 1.2991 0.9257 1.2181 -0.3759 -0.1399 -0.0805 1133 ASP A CB  
597  C CG  . ASP A 96  ? 1.3557 0.9294 1.2663 -0.3963 -0.1274 -0.0816 1133 ASP A CG  
598  O OD1 . ASP A 96  ? 1.4234 0.9357 1.2863 -0.4276 -0.1203 -0.1023 1133 ASP A OD1 
599  O OD2 . ASP A 96  ? 1.3373 0.9288 1.2857 -0.3829 -0.1226 -0.0633 1133 ASP A OD2 
600  N N   . PHE A 97  ? 1.1175 0.9129 1.1080 -0.3518 -0.2014 -0.0572 1134 PHE A N   
601  C CA  . PHE A 97  ? 1.0784 0.9067 1.0658 -0.3483 -0.2116 -0.0618 1134 PHE A CA  
602  C C   . PHE A 97  ? 1.0690 0.9079 1.0548 -0.3704 -0.2451 -0.0564 1134 PHE A C   
603  O O   . PHE A 97  ? 1.0580 0.9122 1.0732 -0.3779 -0.2610 -0.0440 1134 PHE A O   
604  C CB  . PHE A 97  ? 1.0156 0.9073 1.0473 -0.3172 -0.2023 -0.0525 1134 PHE A CB  
605  C CG  . PHE A 97  ? 1.0151 0.9133 1.0507 -0.2916 -0.1739 -0.0593 1134 PHE A CG  
606  C CD1 . PHE A 97  ? 1.0666 0.9124 1.0689 -0.2948 -0.1532 -0.0740 1134 PHE A CD1 
607  C CD2 . PHE A 97  ? 0.9657 0.9263 1.0403 -0.2640 -0.1677 -0.0514 1134 PHE A CD2 
608  C CE1 . PHE A 97  ? 1.0661 0.9249 1.0816 -0.2678 -0.1269 -0.0791 1134 PHE A CE1 
609  C CE2 . PHE A 97  ? 0.9666 0.9444 1.0513 -0.2383 -0.1456 -0.0567 1134 PHE A CE2 
610  C CZ  . PHE A 97  ? 1.0151 0.9437 1.0741 -0.2387 -0.1252 -0.0697 1134 PHE A CZ  
611  N N   . SER A 98  ? 1.0758 0.9058 1.0282 -0.3796 -0.2541 -0.0650 1135 SER A N   
612  C CA  . SER A 98  ? 1.0752 0.9145 1.0226 -0.3953 -0.2861 -0.0571 1135 SER A CA  
613  C C   . SER A 98  ? 1.0722 0.9092 0.9903 -0.3921 -0.2837 -0.0629 1135 SER A C   
614  O O   . SER A 98  ? 1.1217 0.9111 0.9824 -0.4040 -0.2756 -0.0778 1135 SER A O   
615  C CB  . SER A 98  ? 1.1367 0.9340 1.0475 -0.4256 -0.3073 -0.0619 1135 SER A CB  
616  O OG  . SER A 98  ? 1.1409 0.9561 1.0521 -0.4372 -0.3427 -0.0513 1135 SER A OG  
617  N N   . HIS A 99  ? 1.0183 0.9023 0.9741 -0.3773 -0.2864 -0.0521 1136 HIS A N   
618  C CA  . HIS A 99  ? 1.0183 0.8993 0.9508 -0.3744 -0.2801 -0.0565 1136 HIS A CA  
619  C C   . HIS A 99  ? 0.9781 0.9024 0.9533 -0.3655 -0.2937 -0.0387 1136 HIS A C   
620  O O   . HIS A 99  ? 0.9308 0.8994 0.9614 -0.3546 -0.2932 -0.0291 1136 HIS A O   
621  C CB  . HIS A 99  ? 0.9986 0.8877 0.9313 -0.3613 -0.2446 -0.0740 1136 HIS A CB  
622  C CG  . HIS A 99  ? 1.0138 0.8860 0.9126 -0.3640 -0.2297 -0.0853 1136 HIS A CG  
623  N ND1 . HIS A 99  ? 1.0779 0.8898 0.9093 -0.3803 -0.2276 -0.0952 1136 HIS A ND1 
624  C CD2 . HIS A 99  ? 0.9776 0.8833 0.8993 -0.3541 -0.2124 -0.0895 1136 HIS A CD2 
625  C CE1 . HIS A 99  ? 1.0821 0.8878 0.8958 -0.3791 -0.2083 -0.1037 1136 HIS A CE1 
626  N NE2 . HIS A 99  ? 1.0192 0.8834 0.8902 -0.3639 -0.1981 -0.1014 1136 HIS A NE2 
627  N N   . PRO A 100 ? 1.0016 0.9104 0.9506 -0.3689 -0.3037 -0.0327 1137 PRO A N   
628  C CA  . PRO A 100 ? 0.9693 0.9138 0.9599 -0.3582 -0.3121 -0.0151 1137 PRO A CA  
629  C C   . PRO A 100 ? 0.9086 0.8989 0.9475 -0.3425 -0.2849 -0.0190 1137 PRO A C   
630  O O   . PRO A 100 ? 0.8731 0.9006 0.9616 -0.3343 -0.2897 -0.0050 1137 PRO A O   
631  C CB  . PRO A 100 ? 1.0173 0.9227 0.9558 -0.3610 -0.3141 -0.0123 1137 PRO A CB  
632  C CG  . PRO A 100 ? 1.0835 0.9345 0.9532 -0.3792 -0.3259 -0.0213 1137 PRO A CG  
633  C CD  . PRO A 100 ? 1.0679 0.9187 0.9427 -0.3823 -0.3054 -0.0408 1137 PRO A CD  
634  N N   . ASN A 101 ? 0.9000 0.8893 0.9246 -0.3395 -0.2561 -0.0394 1138 ASN A N   
635  C CA  . ASN A 101 ? 0.8512 0.8871 0.9141 -0.3278 -0.2312 -0.0475 1138 ASN A CA  
636  C C   . ASN A 101 ? 0.8265 0.8909 0.9123 -0.3196 -0.2232 -0.0541 1138 ASN A C   
637  O O   . ASN A 101 ? 0.8068 0.8982 0.9008 -0.3125 -0.2006 -0.0700 1138 ASN A O   
638  C CB  . ASN A 101 ? 0.8627 0.8853 0.8976 -0.3306 -0.2033 -0.0665 1138 ASN A CB  
639  C CG  . ASN A 101 ? 0.9013 0.8837 0.9037 -0.3361 -0.2080 -0.0571 1138 ASN A CG  
640  O OD1 . ASN A 101 ? 0.9506 0.8828 0.8971 -0.3451 -0.2025 -0.0651 1138 ASN A OD1 
641  N ND2 . ASN A 101 ? 0.8841 0.8856 0.9197 -0.3293 -0.2164 -0.0387 1138 ASN A ND2 
642  N N   . VAL A 102 ? 0.8322 0.8912 0.9289 -0.3205 -0.2413 -0.0416 1139 VAL A N   
643  C CA  . VAL A 102 ? 0.8158 0.8965 0.9349 -0.3093 -0.2337 -0.0412 1139 VAL A CA  
644  C C   . VAL A 102 ? 0.8098 0.8993 0.9605 -0.3106 -0.2513 -0.0214 1139 VAL A C   
645  O O   . VAL A 102 ? 0.8391 0.8991 0.9784 -0.3248 -0.2714 -0.0148 1139 VAL A O   
646  C CB  . VAL A 102 ? 0.8520 0.8952 0.9365 -0.3108 -0.2248 -0.0537 1139 VAL A CB  
647  C CG1 . VAL A 102 ? 0.8439 0.9013 0.9508 -0.2959 -0.2174 -0.0475 1139 VAL A CG1 
648  C CG2 . VAL A 102 ? 0.8605 0.8994 0.9209 -0.3098 -0.2028 -0.0755 1139 VAL A CG2 
649  N N   . LEU A 103 ? 0.7778 0.9092 0.9669 -0.2973 -0.2429 -0.0134 1140 LEU A N   
650  C CA  . LEU A 103 ? 0.7737 0.9139 0.9953 -0.2987 -0.2528 0.0039  1140 LEU A CA  
651  C C   . LEU A 103 ? 0.8094 0.9168 1.0171 -0.3004 -0.2525 0.0059  1140 LEU A C   
652  O O   . LEU A 103 ? 0.8102 0.9216 1.0135 -0.2848 -0.2361 0.0045  1140 LEU A O   
653  C CB  . LEU A 103 ? 0.7347 0.9234 0.9911 -0.2847 -0.2392 0.0106  1140 LEU A CB  
654  C CG  . LEU A 103 ? 0.7266 0.9259 1.0194 -0.2866 -0.2435 0.0281  1140 LEU A CG  
655  C CD1 . LEU A 103 ? 0.7226 0.9233 1.0406 -0.2999 -0.2595 0.0351  1140 LEU A CD1 
656  C CD2 . LEU A 103 ? 0.7003 0.9403 1.0130 -0.2723 -0.2260 0.0331  1140 LEU A CD2 
657  N N   . SER A 104 ? 0.8456 0.9213 1.0469 -0.3195 -0.2703 0.0090  1141 SER A N   
658  C CA  . SER A 104 ? 0.8905 0.9251 1.0732 -0.3275 -0.2674 0.0069  1141 SER A CA  
659  C C   . SER A 104 ? 0.8859 0.9314 1.1021 -0.3209 -0.2576 0.0210  1141 SER A C   
660  O O   . SER A 104 ? 0.8560 0.9345 1.1110 -0.3210 -0.2626 0.0322  1141 SER A O   
661  C CB  . SER A 104 ? 0.9322 0.9323 1.0929 -0.3547 -0.2902 0.0016  1141 SER A CB  
662  O OG  . SER A 104 ? 0.9191 0.9455 1.1188 -0.3658 -0.3112 0.0130  1141 SER A OG  
663  N N   . LEU A 105 ? 0.9222 0.9346 1.1211 -0.3146 -0.2401 0.0207  1142 LEU A N   
664  C CA  . LEU A 105 ? 0.9358 0.9424 1.1551 -0.3087 -0.2260 0.0347  1142 LEU A CA  
665  C C   . LEU A 105 ? 0.9780 0.9490 1.2000 -0.3389 -0.2348 0.0317  1142 LEU A C   
666  O O   . LEU A 105 ? 1.0246 0.9495 1.2129 -0.3545 -0.2348 0.0188  1142 LEU A O   
667  C CB  . LEU A 105 ? 0.9584 0.9445 1.1563 -0.2833 -0.2005 0.0376  1142 LEU A CB  
668  C CG  . LEU A 105 ? 0.9847 0.9501 1.1908 -0.2721 -0.1797 0.0546  1142 LEU A CG  
669  C CD1 . LEU A 105 ? 1.0427 0.9448 1.2341 -0.2963 -0.1723 0.0490  1142 LEU A CD1 
670  C CD2 . LEU A 105 ? 0.9532 0.9577 1.1947 -0.2702 -0.1819 0.0697  1142 LEU A CD2 
671  N N   . LEU A 106 ? 0.9668 0.9608 1.2299 -0.3492 -0.2411 0.0414  1143 LEU A N   
672  C CA  . LEU A 106 ? 1.0029 0.9762 1.2796 -0.3809 -0.2512 0.0365  1143 LEU A CA  
673  C C   . LEU A 106 ? 1.0594 0.9799 1.3198 -0.3839 -0.2230 0.0368  1143 LEU A C   
674  O O   . LEU A 106 ? 1.1104 0.9851 1.3432 -0.4065 -0.2227 0.0225  1143 LEU A O   
675  C CB  . LEU A 106 ? 0.9678 0.9872 1.3023 -0.3886 -0.2618 0.0464  1143 LEU A CB  
676  C CG  . LEU A 106 ? 0.9247 0.9911 1.2803 -0.3865 -0.2876 0.0477  1143 LEU A CG  
677  C CD1 . LEU A 106 ? 0.9036 1.0101 1.3225 -0.3976 -0.2969 0.0560  1143 LEU A CD1 
678  C CD2 . LEU A 106 ? 0.9475 0.9978 1.2683 -0.4019 -0.3142 0.0348  1143 LEU A CD2 
679  N N   . GLY A 107 ? 1.0600 0.9835 1.3333 -0.3613 -0.1975 0.0535  1144 GLY A N   
680  C CA  . GLY A 107 ? 1.1204 0.9886 1.3758 -0.3580 -0.1656 0.0586  1144 GLY A CA  
681  C C   . GLY A 107 ? 1.1179 0.9962 1.3824 -0.3271 -0.1409 0.0819  1144 GLY A C   
682  O O   . GLY A 107 ? 1.0693 0.9997 1.3589 -0.3156 -0.1490 0.0913  1144 GLY A O   
683  N N   . ILE A 108 ? 1.1804 1.0045 1.4200 -0.3138 -0.1090 0.0913  1145 ILE A N   
684  C CA  . ILE A 108 ? 1.1990 1.0206 1.4366 -0.2839 -0.0833 0.1164  1145 ILE A CA  
685  C C   . ILE A 108 ? 1.2600 1.0301 1.5048 -0.3050 -0.0563 0.1209  1145 ILE A C   
686  O O   . ILE A 108 ? 1.3161 1.0280 1.5451 -0.3257 -0.0423 0.1088  1145 ILE A O   
687  C CB  . ILE A 108 ? 1.2240 1.0271 1.4252 -0.2424 -0.0667 0.1287  1145 ILE A CB  
688  C CG1 . ILE A 108 ? 1.1775 1.0269 1.3737 -0.2291 -0.0907 0.1170  1145 ILE A CG1 
689  C CG2 . ILE A 108 ? 1.2383 1.0475 1.4325 -0.2078 -0.0461 0.1580  1145 ILE A CG2 
690  C CD1 . ILE A 108 ? 1.2013 1.0400 1.3715 -0.1900 -0.0758 0.1256  1145 ILE A CD1 
691  N N   . CYS A 109 ? 1.2574 1.0467 1.5244 -0.3019 -0.0456 0.1364  1146 CYS A N   
692  C CA  . CYS A 109 ? 1.3134 1.0578 1.5923 -0.3242 -0.0166 0.1399  1146 CYS A CA  
693  C C   . CYS A 109 ? 1.3739 1.0714 1.6169 -0.2897 0.0225  0.1683  1146 CYS A C   
694  O O   . CYS A 109 ? 1.3549 1.0838 1.5949 -0.2639 0.0256  0.1886  1146 CYS A O   
695  C CB  . CYS A 109 ? 1.2735 1.0667 1.6051 -0.3483 -0.0275 0.1365  1146 CYS A CB  
696  S SG  . CYS A 109 ? 1.3364 1.0802 1.6933 -0.3838 0.0094  0.1345  1146 CYS A SG  
697  N N   . LEU A 110 ? 1.4552 1.0748 1.6673 -0.2894 0.0534  0.1699  1147 LEU A N   
698  C CA  . LEU A 110 ? 1.5295 1.0912 1.7041 -0.2562 0.0948  0.1995  1147 LEU A CA  
699  C C   . LEU A 110 ? 1.5859 1.1018 1.7729 -0.2846 0.1293  0.2021  1147 LEU A C   
700  O O   . LEU A 110 ? 1.5829 1.0982 1.8055 -0.3327 0.1250  0.1763  1147 LEU A O   
701  C CB  . LEU A 110 ? 1.5903 1.0853 1.7259 -0.2382 0.1158  0.2007  1147 LEU A CB  
702  C CG  . LEU A 110 ? 1.5554 1.0878 1.6754 -0.2001 0.0929  0.2040  1147 LEU A CG  
703  C CD1 . LEU A 110 ? 1.5198 1.1124 1.6342 -0.1561 0.0806  0.2311  1147 LEU A CD1 
704  C CD2 . LEU A 110 ? 1.4923 1.0727 1.6349 -0.2293 0.0530  0.1716  1147 LEU A CD2 
705  N N   . ARG A 111 ? 1.6449 1.1242 1.8013 -0.2543 0.1636  0.2337  1148 ARG A N   
706  C CA  . ARG A 111 ? 1.7087 1.1361 1.8693 -0.2769 0.2045  0.2398  1148 ARG A CA  
707  C C   . ARG A 111 ? 1.8096 1.1515 1.9110 -0.2381 0.2526  0.2741  1148 ARG A C   
708  O O   . ARG A 111 ? 1.8238 1.1618 1.8880 -0.1906 0.2482  0.2949  1148 ARG A O   
709  C CB  . ARG A 111 ? 1.6609 1.1499 1.8529 -0.2842 0.1938  0.2448  1148 ARG A CB  
710  C CG  . ARG A 111 ? 1.5746 1.1433 1.8304 -0.3212 0.1516  0.2142  1148 ARG A CG  
711  C CD  . ARG A 111 ? 1.5342 1.1573 1.8221 -0.3258 0.1481  0.2201  1148 ARG A CD  
712  N NE  . ARG A 111 ? 1.5091 1.1708 1.7640 -0.2820 0.1363  0.2432  1148 ARG A NE  
713  C CZ  . ARG A 111 ? 1.4828 1.1860 1.7490 -0.2783 0.1372  0.2517  1148 ARG A CZ  
714  N NH1 . ARG A 111 ? 1.4657 1.2033 1.6958 -0.2410 0.1257  0.2698  1148 ARG A NH1 
715  N NH2 . ARG A 111 ? 1.4762 1.1883 1.7912 -0.3135 0.1508  0.2404  1148 ARG A NH2 
716  N N   . SER A 112 ? 1.8850 1.1588 1.9801 -0.2584 0.2996  0.2801  1149 SER A N   
717  C CA  . SER A 112 ? 1.9920 1.1754 2.0276 -0.2224 0.3510  0.3162  1149 SER A CA  
718  C C   . SER A 112 ? 1.9887 1.2068 1.9906 -0.1735 0.3447  0.3546  1149 SER A C   
719  O O   . SER A 112 ? 2.0531 1.2292 1.9994 -0.1219 0.3635  0.3908  1149 SER A O   
720  C CB  . SER A 112 ? 2.0734 1.1736 2.1119 -0.2626 0.4055  0.3087  1149 SER A CB  
721  O OG  . SER A 112 ? 2.0363 1.1807 2.1157 -0.2951 0.4027  0.2992  1149 SER A OG  
722  N N   . GLU A 113 ? 1.9196 1.2147 1.9549 -0.1900 0.3185  0.3464  1150 GLU A N   
723  C CA  . GLU A 113 ? 1.9120 1.2482 1.9159 -0.1524 0.3096  0.3763  1150 GLU A CA  
724  C C   . GLU A 113 ? 1.7961 1.2453 1.8416 -0.1588 0.2541  0.3565  1150 GLU A C   
725  O O   . GLU A 113 ? 1.7312 1.2202 1.8351 -0.2002 0.2316  0.3223  1150 GLU A O   
726  C CB  . GLU A 113 ? 1.9727 1.2645 1.9623 -0.1672 0.3532  0.3907  1150 GLU A CB  
727  C CG  . GLU A 113 ? 1.9142 1.2505 1.9722 -0.2226 0.3477  0.3585  1150 GLU A CG  
728  C CD  . GLU A 113 ? 1.9084 1.2235 2.0233 -0.2762 0.3545  0.3214  1150 GLU A CD  
729  O OE1 . GLU A 113 ? 1.9974 1.2222 2.0946 -0.2911 0.4025  0.3235  1150 GLU A OE1 
730  O OE2 . GLU A 113 ? 1.8205 1.2086 1.9949 -0.3035 0.3123  0.2905  1150 GLU A OE2 
731  N N   . GLY A 114 ? 1.7769 1.2763 1.7896 -0.1174 0.2334  0.3786  1151 GLY A N   
732  C CA  . GLY A 114 ? 1.6761 1.2772 1.7199 -0.1203 0.1865  0.3615  1151 GLY A CA  
733  C C   . GLY A 114 ? 1.6279 1.2709 1.6755 -0.0984 0.1495  0.3521  1151 GLY A C   
734  O O   . GLY A 114 ? 1.6660 1.2600 1.7014 -0.0871 0.1595  0.3541  1151 GLY A O   
735  N N   . SER A 115 ? 1.5478 1.2789 1.6129 -0.0943 0.1109  0.3403  1152 SER A N   
736  C CA  . SER A 115 ? 1.4992 1.2787 1.5702 -0.0753 0.0767  0.3292  1152 SER A CA  
737  C C   . SER A 115 ? 1.4469 1.2317 1.5658 -0.1137 0.0594  0.2940  1152 SER A C   
738  O O   . SER A 115 ? 1.4350 1.2050 1.5880 -0.1542 0.0665  0.2780  1152 SER A O   
739  C CB  . SER A 115 ? 1.4454 1.3122 1.5129 -0.0592 0.0473  0.3287  1152 SER A CB  
740  O OG  . SER A 115 ? 1.5020 1.3671 1.5171 -0.0210 0.0588  0.3620  1152 SER A OG  
741  N N   . PRO A 116 ? 1.3477 0.9372 1.2554 -0.2781 0.3749  0.3225  1153 PRO A N   
742  C CA  . PRO A 116 ? 1.2840 0.9144 1.2473 -0.2903 0.3532  0.2857  1153 PRO A CA  
743  C C   . PRO A 116 ? 1.2041 0.9241 1.2031 -0.2843 0.3362  0.2648  1153 PRO A C   
744  O O   . PRO A 116 ? 1.1804 0.9248 1.1535 -0.2561 0.3278  0.2730  1153 PRO A O   
745  C CB  . PRO A 116 ? 1.2727 0.8671 1.2177 -0.2613 0.3272  0.2828  1153 PRO A CB  
746  C CG  . PRO A 116 ? 1.3447 0.8685 1.2338 -0.2385 0.3400  0.3201  1153 PRO A CG  
747  C CD  . PRO A 116 ? 1.3676 0.9112 1.2284 -0.2389 0.3579  0.3436  1153 PRO A CD  
748  N N   . LEU A 117 ? 1.1679 0.9351 1.2263 -0.3111 0.3307  0.2380  1154 LEU A N   
749  C CA  . LEU A 117 ? 1.0983 0.9483 1.1999 -0.3050 0.3146  0.2188  1154 LEU A CA  
750  C C   . LEU A 117 ? 1.0407 0.9107 1.1635 -0.2966 0.2768  0.1956  1154 LEU A C   
751  O O   . LEU A 117 ? 1.0480 0.9102 1.1959 -0.3224 0.2696  0.1802  1154 LEU A O   
752  C CB  . LEU A 117 ? 1.1067 1.0053 1.2659 -0.3408 0.3365  0.2094  1154 LEU A CB  
753  C CG  . LEU A 117 ? 1.1449 1.0518 1.2915 -0.3456 0.3742  0.2268  1154 LEU A CG  
754  C CD1 . LEU A 117 ? 1.2295 1.0541 1.3184 -0.3561 0.4027  0.2548  1154 LEU A CD1 
755  C CD2 . LEU A 117 ? 1.1365 1.1119 1.3563 -0.3768 0.3926  0.2118  1154 LEU A CD2 
756  N N   . VAL A 118 ? 0.9894 0.8831 1.0975 -0.2632 0.2540  0.1927  1155 VAL A N   
757  C CA  . VAL A 118 ? 0.9373 0.8536 1.0613 -0.2543 0.2196  0.1724  1155 VAL A CA  
758  C C   . VAL A 118 ? 0.8906 0.8820 1.0700 -0.2592 0.2090  0.1575  1155 VAL A C   
759  O O   . VAL A 118 ? 0.8832 0.9086 1.0739 -0.2500 0.2237  0.1627  1155 VAL A O   
760  C CB  . VAL A 118 ? 0.9159 0.8151 0.9956 -0.2179 0.2022  0.1774  1155 VAL A CB  
761  C CG1 . VAL A 118 ? 0.8663 0.7917 0.9598 -0.2097 0.1697  0.1572  1155 VAL A CG1 
762  C CG2 . VAL A 118 ? 0.9614 0.7925 0.9965 -0.2090 0.2097  0.1931  1155 VAL A CG2 
763  N N   . VAL A 119 ? 0.8645 0.8802 1.0767 -0.2730 0.1835  0.1392  1156 VAL A N   
764  C CA  . VAL A 119 ? 0.8262 0.9146 1.0978 -0.2776 0.1691  0.1276  1156 VAL A CA  
765  C C   . VAL A 119 ? 0.7851 0.8869 1.0519 -0.2609 0.1315  0.1164  1156 VAL A C   
766  O O   . VAL A 119 ? 0.7917 0.8591 1.0323 -0.2691 0.1154  0.1087  1156 VAL A O   
767  C CB  . VAL A 119 ? 0.8476 0.9638 1.1717 -0.3187 0.1739  0.1187  1156 VAL A CB  
768  C CG1 . VAL A 119 ? 0.8135 1.0151 1.2090 -0.3203 0.1582  0.1099  1156 VAL A CG1 
769  C CG2 . VAL A 119 ? 0.8966 0.9865 1.2175 -0.3405 0.2144  0.1302  1156 VAL A CG2 
770  N N   . LEU A 120 ? 0.7479 0.8960 1.0384 -0.2382 0.1208  0.1154  1157 LEU A N   
771  C CA  . LEU A 120 ? 0.7164 0.8763 1.0016 -0.2217 0.0871  0.1079  1157 LEU A CA  
772  C C   . LEU A 120 ? 0.6917 0.9204 1.0408 -0.2171 0.0730  0.1048  1157 LEU A C   
773  O O   . LEU A 120 ? 0.6922 0.9591 1.0857 -0.2176 0.0943  0.1080  1157 LEU A O   
774  C CB  . LEU A 120 ? 0.7035 0.8335 0.9385 -0.1897 0.0887  0.1128  1157 LEU A CB  
775  C CG  . LEU A 120 ? 0.7266 0.7981 0.9055 -0.1870 0.1033  0.1200  1157 LEU A CG  
776  C CD1 . LEU A 120 ? 0.7473 0.8122 0.9152 -0.1816 0.1353  0.1335  1157 LEU A CD1 
777  C CD2 . LEU A 120 ? 0.7108 0.7583 0.8458 -0.1646 0.0869  0.1175  1157 LEU A CD2 
778  N N   . PRO A 121 ? 0.6730 0.9194 1.0289 -0.2112 0.0377  0.0998  1158 PRO A N   
779  C CA  . PRO A 121 ? 0.6553 0.9662 1.0734 -0.2007 0.0204  0.1009  1158 PRO A CA  
780  C C   . PRO A 121 ? 0.6380 0.9595 1.0652 -0.1654 0.0375  0.1060  1158 PRO A C   
781  O O   . PRO A 121 ? 0.6338 0.9122 1.0071 -0.1458 0.0425  0.1068  1158 PRO A O   
782  C CB  . PRO A 121 ? 0.6528 0.9606 1.0525 -0.2002 -0.0212 0.0982  1158 PRO A CB  
783  C CG  . PRO A 121 ? 0.6706 0.9196 1.0083 -0.2214 -0.0226 0.0908  1158 PRO A CG  
784  C CD  . PRO A 121 ? 0.6745 0.8800 0.9789 -0.2137 0.0136  0.0942  1158 PRO A CD  
785  N N   . TYR A 122 ? 0.6311 1.0118 1.1289 -0.1587 0.0472  0.1075  1159 TYR A N   
786  C CA  . TYR A 122 ? 0.6243 1.0149 1.1355 -0.1278 0.0709  0.1088  1159 TYR A CA  
787  C C   . TYR A 122 ? 0.6119 0.9855 1.1017 -0.0975 0.0475  0.1100  1159 TYR A C   
788  O O   . TYR A 122 ? 0.6104 1.0154 1.1370 -0.0904 0.0162  0.1138  1159 TYR A O   
789  C CB  . TYR A 122 ? 0.6260 1.0889 1.2274 -0.1267 0.0867  0.1084  1159 TYR A CB  
790  C CG  . TYR A 122 ? 0.6295 1.1011 1.2469 -0.0959 0.1182  0.1063  1159 TYR A CG  
791  C CD1 . TYR A 122 ? 0.6448 1.0783 1.2125 -0.0955 0.1573  0.1037  1159 TYR A CD1 
792  C CD2 . TYR A 122 ? 0.6244 1.1390 1.3030 -0.0667 0.1091  0.1069  1159 TYR A CD2 
793  C CE1 . TYR A 122 ? 0.6565 1.0943 1.2312 -0.0708 0.1886  0.0981  1159 TYR A CE1 
794  C CE2 . TYR A 122 ? 0.6350 1.1514 1.3271 -0.0385 0.1423  0.1016  1159 TYR A CE2 
795  C CZ  . TYR A 122 ? 0.6514 1.1289 1.2891 -0.0424 0.1831  0.0952  1159 TYR A CZ  
796  O OH  . TYR A 122 ? 0.6699 1.1458 1.3137 -0.0181 0.2183  0.0865  1159 TYR A OH  
797  N N   . MET A 123 ? 0.6083 0.9318 1.0369 -0.0816 0.0624  0.1078  1160 MET A N   
798  C CA  . MET A 123 ? 0.6019 0.9002 1.0032 -0.0559 0.0472  0.1074  1160 MET A CA  
799  C C   . MET A 123 ? 0.6074 0.9244 1.0440 -0.0281 0.0715  0.1044  1160 MET A C   
800  O O   . MET A 123 ? 0.6189 0.9140 1.0250 -0.0225 0.1037  0.0980  1160 MET A O   
801  C CB  . MET A 123 ? 0.6023 0.8398 0.9205 -0.0575 0.0503  0.1038  1160 MET A CB  
802  C CG  . MET A 123 ? 0.5987 0.8121 0.8815 -0.0794 0.0272  0.1047  1160 MET A CG  
803  S SD  . MET A 123 ? 0.5965 0.8145 0.8836 -0.0794 -0.0172 0.1076  1160 MET A SD  
804  C CE  . MET A 123 ? 0.5999 0.8714 0.9490 -0.1051 -0.0320 0.1100  1160 MET A CE  
805  N N   . LYS A 124 ? 0.6051 0.9615 1.1045 -0.0103 0.0552  0.1092  1161 LYS A N   
806  C CA  . LYS A 124 ? 0.6141 0.9999 1.1694 0.0167  0.0805  0.1061  1161 LYS A CA  
807  C C   . LYS A 124 ? 0.6290 0.9626 1.1291 0.0345  0.1087  0.0956  1161 LYS A C   
808  O O   . LYS A 124 ? 0.6409 0.9773 1.1408 0.0352  0.1485  0.0863  1161 LYS A O   
809  C CB  . LYS A 124 ? 0.6178 1.0395 1.2362 0.0400  0.0500  0.1165  1161 LYS A CB  
810  C CG  . LYS A 124 ? 0.6336 1.0913 1.3255 0.0729  0.0754  0.1142  1161 LYS A CG  
811  C CD  . LYS A 124 ? 0.6435 1.1329 1.3969 0.1011  0.0416  0.1291  1161 LYS A CD  
812  C CE  . LYS A 124 ? 0.6641 1.1842 1.4937 0.1393  0.0704  0.1263  1161 LYS A CE  
813  N NZ  . LYS A 124 ? 0.6807 1.2269 1.5690 0.1718  0.0343  0.1453  1161 LYS A NZ  
814  N N   . HIS A 125 ? 0.6318 0.9173 1.0814 0.0451  0.0886  0.0963  1162 HIS A N   
815  C CA  . HIS A 125 ? 0.6526 0.8921 1.0603 0.0634  0.1111  0.0850  1162 HIS A CA  
816  C C   . HIS A 125 ? 0.6516 0.8502 0.9785 0.0446  0.1274  0.0754  1162 HIS A C   
817  O O   . HIS A 125 ? 0.6732 0.8311 0.9528 0.0525  0.1414  0.0642  1162 HIS A O   
818  C CB  . HIS A 125 ? 0.6651 0.8711 1.0585 0.0816  0.0838  0.0908  1162 HIS A CB  
819  C CG  . HIS A 125 ? 0.6770 0.9176 1.1476 0.1086  0.0703  0.1024  1162 HIS A CG  
820  N ND1 . HIS A 125 ? 0.6930 0.9670 1.2315 0.1323  0.0991  0.0978  1162 HIS A ND1 
821  C CD2 . HIS A 125 ? 0.6798 0.9285 1.1700 0.1161  0.0291  0.1200  1162 HIS A CD2 
822  C CE1 . HIS A 125 ? 0.7028 1.0073 1.3071 0.1567  0.0751  0.1133  1162 HIS A CE1 
823  N NE2 . HIS A 125 ? 0.6967 0.9853 1.2688 0.1464  0.0296  0.1285  1162 HIS A NE2 
824  N N   . GLY A 126 ? 0.6308 0.8397 0.9425 0.0196  0.1249  0.0801  1163 GLY A N   
825  C CA  . GLY A 126 ? 0.6338 0.8128 0.8790 0.0050  0.1416  0.0752  1163 GLY A CA  
826  C C   . GLY A 126 ? 0.6260 0.7610 0.8060 0.0011  0.1199  0.0734  1163 GLY A C   
827  O O   . GLY A 126 ? 0.6119 0.7398 0.7946 0.0011  0.0900  0.0784  1163 GLY A O   
828  N N   . ASP A 127 ? 0.6388 0.7475 0.7601 -0.0034 0.1354  0.0661  1164 ASP A N   
829  C CA  . ASP A 127 ? 0.6327 0.7088 0.6964 -0.0101 0.1175  0.0638  1164 ASP A CA  
830  C C   . ASP A 127 ? 0.6429 0.6930 0.6929 0.0019  0.1113  0.0535  1164 ASP A C   
831  O O   . ASP A 127 ? 0.6630 0.7121 0.7351 0.0170  0.1282  0.0461  1164 ASP A O   
832  C CB  . ASP A 127 ? 0.6484 0.7138 0.6585 -0.0198 0.1322  0.0620  1164 ASP A CB  
833  C CG  . ASP A 127 ? 0.6835 0.7404 0.6666 -0.0143 0.1599  0.0480  1164 ASP A CG  
834  O OD1 . ASP A 127 ? 0.6992 0.7724 0.7149 -0.0075 0.1849  0.0445  1164 ASP A OD1 
835  O OD2 . ASP A 127 ? 0.6983 0.7344 0.6286 -0.0186 0.1574  0.0390  1164 ASP A OD2 
836  N N   . LEU A 128 ? 0.6343 0.6607 0.6479 -0.0053 0.0897  0.0527  1165 LEU A N   
837  C CA  . LEU A 128 ? 0.6508 0.6467 0.6477 0.0011  0.0813  0.0454  1165 LEU A CA  
838  C C   . LEU A 128 ? 0.6823 0.6546 0.6380 0.0013  0.1031  0.0278  1165 LEU A C   
839  O O   . LEU A 128 ? 0.7075 0.6528 0.6607 0.0110  0.1100  0.0187  1165 LEU A O   
840  C CB  . LEU A 128 ? 0.6353 0.6171 0.6060 -0.0116 0.0548  0.0496  1165 LEU A CB  
841  C CG  . LEU A 128 ? 0.6559 0.6014 0.6005 -0.0108 0.0458  0.0436  1165 LEU A CG  
842  C CD1 . LEU A 128 ? 0.6699 0.6090 0.6499 0.0046  0.0354  0.0536  1165 LEU A CD1 
843  C CD2 . LEU A 128 ? 0.6428 0.5783 0.5541 -0.0279 0.0277  0.0437  1165 LEU A CD2 
844  N N   . ARG A 129 ? 0.6872 0.6677 0.6084 -0.0100 0.1132  0.0234  1166 ARG A N   
845  C CA  . ARG A 129 ? 0.7230 0.6855 0.5960 -0.0161 0.1293  0.0055  1166 ARG A CA  
846  C C   . ARG A 129 ? 0.7617 0.7166 0.6480 -0.0040 0.1602  -0.0067 1166 ARG A C   
847  O O   . ARG A 129 ? 0.7966 0.7197 0.6631 -0.0016 0.1714  -0.0239 1166 ARG A O   
848  C CB  . ARG A 129 ? 0.7228 0.7025 0.5586 -0.0294 0.1293  0.0088  1166 ARG A CB  
849  C CG  . ARG A 129 ? 0.7485 0.7162 0.5281 -0.0427 0.1281  -0.0068 1166 ARG A CG  
850  C CD  . ARG A 129 ? 0.7985 0.7495 0.5490 -0.0446 0.1551  -0.0281 1166 ARG A CD  
851  N NE  . ARG A 129 ? 0.8198 0.7876 0.5630 -0.0438 0.1775  -0.0251 1166 ARG A NE  
852  C CZ  . ARG A 129 ? 0.8608 0.8312 0.5503 -0.0565 0.1896  -0.0350 1166 ARG A CZ  
853  N NH1 . ARG A 129 ? 0.8838 0.8677 0.5646 -0.0568 0.2106  -0.0289 1166 ARG A NH1 
854  N NH2 . ARG A 129 ? 0.8843 0.8450 0.5268 -0.0714 0.1806  -0.0512 1166 ARG A NH2 
855  N N   . ASN A 130 ? 0.7610 0.7434 0.6826 0.0027  0.1765  0.0007  1167 ASN A N   
856  C CA  . ASN A 130 ? 0.7986 0.7802 0.7397 0.0149  0.2108  -0.0117 1167 ASN A CA  
857  C C   . ASN A 130 ? 0.8061 0.7769 0.8000 0.0373  0.2095  -0.0117 1167 ASN A C   
858  O O   . ASN A 130 ? 0.8471 0.7996 0.8493 0.0508  0.2370  -0.0272 1167 ASN A O   
859  C CB  . ASN A 130 ? 0.7948 0.8128 0.7626 0.0135  0.2307  -0.0031 1167 ASN A CB  
860  C CG  . ASN A 130 ? 0.8138 0.8340 0.7212 -0.0051 0.2406  -0.0035 1167 ASN A CG  
861  O OD1 . ASN A 130 ? 0.8534 0.8753 0.7416 -0.0080 0.2732  -0.0140 1167 ASN A OD1 
862  N ND2 . ASN A 130 ? 0.7920 0.8121 0.6683 -0.0171 0.2132  0.0082  1167 ASN A ND2 
863  N N   . PHE A 131 ? 0.7751 0.7555 0.8026 0.0417  0.1779  0.0061  1168 PHE A N   
864  C CA  . PHE A 131 ? 0.7842 0.7591 0.8626 0.0641  0.1694  0.0129  1168 PHE A CA  
865  C C   . PHE A 131 ? 0.8275 0.7467 0.8713 0.0703  0.1731  0.0001  1168 PHE A C   
866  O O   . PHE A 131 ? 0.8641 0.7650 0.9373 0.0929  0.1906  -0.0052 1168 PHE A O   
867  C CB  . PHE A 131 ? 0.7457 0.7426 0.8528 0.0611  0.1315  0.0348  1168 PHE A CB  
868  C CG  . PHE A 131 ? 0.7549 0.7547 0.9154 0.0839  0.1158  0.0477  1168 PHE A CG  
869  C CD1 . PHE A 131 ? 0.7419 0.7921 0.9764 0.0964  0.1135  0.0595  1168 PHE A CD1 
870  C CD2 . PHE A 131 ? 0.7813 0.7355 0.9189 0.0917  0.1016  0.0499  1168 PHE A CD2 
871  C CE1 . PHE A 131 ? 0.7536 0.8130 1.0403 0.1193  0.0944  0.0743  1168 PHE A CE1 
872  C CE2 . PHE A 131 ? 0.7969 0.7521 0.9807 0.1149  0.0843  0.0664  1168 PHE A CE2 
873  C CZ  . PHE A 131 ? 0.7823 0.7926 1.0417 0.1300  0.0788  0.0793  1168 PHE A CZ  
874  N N   . ILE A 132 ? 0.8286 0.7207 0.8133 0.0502  0.1579  -0.0047 1169 ILE A N   
875  C CA  . ILE A 132 ? 0.8717 0.7085 0.8186 0.0491  0.1610  -0.0175 1169 ILE A CA  
876  C C   . ILE A 132 ? 0.9240 0.7357 0.8377 0.0460  0.1978  -0.0450 1169 ILE A C   
877  O O   . ILE A 132 ? 0.9745 0.7375 0.8775 0.0543  0.2136  -0.0582 1169 ILE A O   
878  C CB  . ILE A 132 ? 0.8543 0.6773 0.7537 0.0253  0.1350  -0.0156 1169 ILE A CB  
879  C CG1 . ILE A 132 ? 0.8381 0.6834 0.6955 0.0018  0.1369  -0.0255 1169 ILE A CG1 
880  C CG2 . ILE A 132 ? 0.8187 0.6589 0.7454 0.0276  0.1022  0.0085  1169 ILE A CG2 
881  C CD1 . ILE A 132 ? 0.8218 0.6613 0.6425 -0.0192 0.1140  -0.0250 1169 ILE A CD1 
882  N N   . ARG A 133 ? 0.9215 0.7624 0.8142 0.0327  0.2121  -0.0532 1170 ARG A N   
883  C CA  . ARG A 133 ? 0.9759 0.7979 0.8302 0.0259  0.2474  -0.0801 1170 ARG A CA  
884  C C   . ARG A 133 ? 1.0118 0.8302 0.9142 0.0521  0.2816  -0.0871 1170 ARG A C   
885  O O   . ARG A 133 ? 1.0715 0.8515 0.9498 0.0539  0.3138  -0.1125 1170 ARG A O   
886  C CB  . ARG A 133 ? 0.9659 0.8222 0.7818 0.0051  0.2505  -0.0818 1170 ARG A CB  
887  C CG  . ARG A 133 ? 0.9531 0.8102 0.7141 -0.0203 0.2248  -0.0827 1170 ARG A CG  
888  C CD  . ARG A 133 ? 0.9555 0.8445 0.6780 -0.0365 0.2277  -0.0814 1170 ARG A CD  
889  N NE  . ARG A 133 ? 1.0181 0.8919 0.6967 -0.0453 0.2607  -0.1064 1170 ARG A NE  
890  C CZ  . ARG A 133 ? 1.0419 0.9299 0.7247 -0.0404 0.2899  -0.1080 1170 ARG A CZ  
891  N NH1 . ARG A 133 ? 1.1064 0.9772 0.7384 -0.0523 0.3204  -0.1336 1170 ARG A NH1 
892  N NH2 . ARG A 133 ? 1.0058 0.9247 0.7414 -0.0266 0.2904  -0.0858 1170 ARG A NH2 
893  N N   . ASN A 134 ? 0.9816 0.8419 0.9536 0.0709  0.2760  -0.0663 1171 ASN A N   
894  C CA  . ASN A 134 ? 1.0109 0.8823 1.0437 0.0977  0.3074  -0.0705 1171 ASN A CA  
895  C C   . ASN A 134 ? 1.0689 0.8843 1.1111 0.1198  0.3205  -0.0818 1171 ASN A C   
896  O O   . ASN A 134 ? 1.0619 0.8577 1.1208 0.1309  0.2920  -0.0654 1171 ASN A O   
897  C CB  . ASN A 134 ? 0.9607 0.8895 1.0740 0.1127  0.2899  -0.0441 1171 ASN A CB  
898  C CG  . ASN A 134 ? 0.9797 0.9388 1.1621 0.1362  0.3256  -0.0493 1171 ASN A CG  
899  O OD1 . ASN A 134 ? 1.0321 0.9659 1.2008 0.1430  0.3673  -0.0736 1171 ASN A OD1 
900  N ND2 . ASN A 134 ? 0.9408 0.9562 1.1988 0.1470  0.3111  -0.0284 1171 ASN A ND2 
901  N N   . GLU A 135 ? 1.1364 0.9220 1.1631 0.1252  0.3655  -0.1101 1172 GLU A N   
902  C CA  . GLU A 135 ? 1.2066 0.9249 1.2284 0.1426  0.3857  -0.1267 1172 GLU A CA  
903  C C   . GLU A 135 ? 1.2130 0.9390 1.3276 0.1867  0.3861  -0.1082 1172 GLU A C   
904  O O   . GLU A 135 ? 1.2548 0.9249 1.3754 0.2062  0.3853  -0.1067 1172 GLU A O   
905  C CB  . GLU A 135 ? 1.2816 0.9642 1.2543 0.1321  0.4366  -0.1661 1172 GLU A CB  
906  C CG  . GLU A 135 ? 1.3027 1.0209 1.3235 0.1495  0.4797  -0.1763 1172 GLU A CG  
907  C CD  . GLU A 135 ? 1.2570 1.0444 1.2773 0.1306  0.4762  -0.1659 1172 GLU A CD  
908  O OE1 . GLU A 135 ? 1.2290 1.0700 1.3273 0.1503  0.4817  -0.1501 1172 GLU A OE1 
909  O OE2 . GLU A 135 ? 1.2543 1.0425 1.1976 0.0959  0.4672  -0.1725 1172 GLU A OE2 
910  N N   . THR A 136 ? 1.1760 0.9715 1.3636 0.2019  0.3872  -0.0931 1173 THR A N   
911  C CA  . THR A 136 ? 1.1767 0.9972 1.4629 0.2437  0.3832  -0.0733 1173 THR A CA  
912  C C   . THR A 136 ? 1.1488 0.9642 1.4476 0.2506  0.3289  -0.0406 1173 THR A C   
913  O O   . THR A 136 ? 1.1837 0.9660 1.5174 0.2824  0.3230  -0.0288 1173 THR A O   
914  C CB  . THR A 136 ? 1.1384 1.0437 1.4990 0.2505  0.3945  -0.0658 1173 THR A CB  
915  O OG1 . THR A 136 ? 1.0716 1.0223 1.4124 0.2200  0.3595  -0.0486 1173 THR A OG1 
916  C CG2 . THR A 136 ? 1.1785 1.0869 1.5297 0.2463  0.4534  -0.0974 1173 THR A CG2 
917  N N   . HIS A 137 ? 1.0924 0.9379 1.3604 0.2210  0.2909  -0.0256 1174 HIS A N   
918  C CA  . HIS A 137 ? 1.0694 0.9061 1.3309 0.2190  0.2415  0.0013  1174 HIS A CA  
919  C C   . HIS A 137 ? 1.1119 0.8646 1.3004 0.2097  0.2408  -0.0084 1174 HIS A C   
920  O O   . HIS A 137 ? 1.1341 0.8524 1.2577 0.1864  0.2649  -0.0357 1174 HIS A O   
921  C CB  . HIS A 137 ? 1.0055 0.8904 1.2477 0.1876  0.2091  0.0138  1174 HIS A CB  
922  C CG  . HIS A 137 ? 0.9666 0.9303 1.2776 0.1909  0.2068  0.0248  1174 HIS A CG  
923  N ND1 . HIS A 137 ? 0.9348 0.9353 1.2289 0.1650  0.2171  0.0176  1174 HIS A ND1 
924  C CD2 . HIS A 137 ? 0.9588 0.9719 1.3582 0.2165  0.1941  0.0440  1174 HIS A CD2 
925  C CE1 . HIS A 137 ? 0.9076 0.9735 1.2750 0.1716  0.2142  0.0299  1174 HIS A CE1 
926  N NE2 . HIS A 137 ? 0.9201 0.9997 1.3564 0.2029  0.1990  0.0454  1174 HIS A NE2 
927  N N   . ASN A 138 ? 1.1268 0.8481 1.3248 0.2258  0.2125  0.0145  1175 ASN A N   
928  C CA  . ASN A 138 ? 1.1742 0.8126 1.3065 0.2161  0.2116  0.0087  1175 ASN A CA  
929  C C   . ASN A 138 ? 1.1523 0.7866 1.2707 0.2091  0.1635  0.0395  1175 ASN A C   
930  O O   . ASN A 138 ? 1.1943 0.7938 1.3317 0.2344  0.1492  0.0617  1175 ASN A O   
931  C CB  . ASN A 138 ? 1.2571 0.8307 1.4080 0.2495  0.2447  -0.0002 1175 ASN A CB  
932  C CG  . ASN A 138 ? 1.3196 0.7992 1.3978 0.2348  0.2500  -0.0098 1175 ASN A CG  
933  O OD1 . ASN A 138 ? 1.3211 0.7783 1.3289 0.1967  0.2604  -0.0352 1175 ASN A OD1 
934  N ND2 . ASN A 138 ? 1.3753 0.8006 1.4708 0.2638  0.2419  0.0117  1175 ASN A ND2 
935  N N   . PRO A 139 ? 1.0910 0.7588 1.1739 0.1751  0.1381  0.0424  1176 PRO A N   
936  C CA  . PRO A 139 ? 1.0731 0.7340 1.1325 0.1631  0.0969  0.0669  1176 PRO A CA  
937  C C   . PRO A 139 ? 1.1140 0.6963 1.1010 0.1446  0.1003  0.0595  1176 PRO A C   
938  O O   . PRO A 139 ? 1.1232 0.6798 1.0627 0.1215  0.1246  0.0311  1176 PRO A O   
939  C CB  . PRO A 139 ? 1.0034 0.7248 1.0520 0.1335  0.0801  0.0650  1176 PRO A CB  
940  C CG  . PRO A 139 ? 0.9966 0.7241 1.0216 0.1183  0.1142  0.0345  1176 PRO A CG  
941  C CD  . PRO A 139 ? 1.0429 0.7541 1.1048 0.1476  0.1493  0.0229  1176 PRO A CD  
942  N N   . THR A 140 ? 1.1397 0.6856 1.1171 0.1527  0.0749  0.0857  1177 THR A N   
943  C CA  . THR A 140 ? 1.1875 0.6552 1.0975 0.1340  0.0782  0.0825  1177 THR A CA  
944  C C   . THR A 140 ? 1.1379 0.6224 0.9928 0.0894  0.0674  0.0706  1177 THR A C   
945  O O   . THR A 140 ? 1.0689 0.6199 0.9393 0.0781  0.0538  0.0700  1177 THR A O   
946  C CB  . THR A 140 ? 1.2419 0.6667 1.1543 0.1554  0.0532  0.1185  1177 THR A CB  
947  O OG1 . THR A 140 ? 1.1970 0.6777 1.1227 0.1499  0.0123  0.1438  1177 THR A OG1 
948  C CG2 . THR A 140 ? 1.2928 0.6978 1.2646 0.2042  0.0645  0.1318  1177 THR A CG2 
949  N N   . VAL A 141 ? 1.1757 0.5983 0.9689 0.0645  0.0754  0.0610  1178 VAL A N   
950  C CA  . VAL A 141 ? 1.1391 0.5765 0.8843 0.0232  0.0681  0.0485  1178 VAL A CA  
951  C C   . VAL A 141 ? 1.1025 0.5743 0.8498 0.0175  0.0321  0.0747  1178 VAL A C   
952  O O   . VAL A 141 ? 1.0473 0.5653 0.7848 -0.0057 0.0230  0.0668  1178 VAL A O   
953  C CB  . VAL A 141 ? 1.1996 0.5635 0.8838 -0.0033 0.0856  0.0334  1178 VAL A CB  
954  C CG1 . VAL A 141 ? 1.1657 0.5525 0.8089 -0.0451 0.0778  0.0215  1178 VAL A CG1 
955  C CG2 . VAL A 141 ? 1.2411 0.5685 0.9175 -0.0026 0.1224  0.0030  1178 VAL A CG2 
956  N N   . LYS A 142 ? 1.1376 0.5853 0.8966 0.0395  0.0119  0.1058  1179 LYS A N   
957  C CA  . LYS A 142 ? 1.1150 0.5916 0.8714 0.0339  -0.0236 0.1312  1179 LYS A CA  
958  C C   . LYS A 142 ? 1.0391 0.6000 0.8470 0.0400  -0.0371 0.1310  1179 LYS A C   
959  O O   . LYS A 142 ? 1.0021 0.5980 0.7973 0.0192  -0.0560 0.1338  1179 LYS A O   
960  C CB  . LYS A 142 ? 1.1797 0.6150 0.9403 0.0601  -0.0440 0.1667  1179 LYS A CB  
961  C CG  . LYS A 142 ? 1.1839 0.6332 0.9210 0.0482  -0.0817 0.1937  1179 LYS A CG  
962  C CD  . LYS A 142 ? 1.2620 0.6646 0.9937 0.0734  -0.1037 0.2320  1179 LYS A CD  
963  C CE  . LYS A 142 ? 1.2801 0.6890 0.9716 0.0556  -0.1409 0.2580  1179 LYS A CE  
964  N NZ  . LYS A 142 ? 1.2201 0.7154 0.9555 0.0565  -0.1688 0.2622  1179 LYS A NZ  
965  N N   . ASP A 143 ? 1.0206 0.6106 0.8857 0.0672  -0.0243 0.1265  1180 ASP A N   
966  C CA  . ASP A 143 ? 0.9541 0.6205 0.8692 0.0708  -0.0308 0.1242  1180 ASP A CA  
967  C C   . ASP A 143 ? 0.9011 0.5929 0.7898 0.0410  -0.0177 0.0992  1180 ASP A C   
968  O O   . ASP A 143 ? 0.8546 0.5931 0.7523 0.0280  -0.0326 0.1014  1180 ASP A O   
969  C CB  . ASP A 143 ? 0.9563 0.6453 0.9361 0.1040  -0.0126 0.1219  1180 ASP A CB  
970  C CG  . ASP A 143 ? 1.0021 0.6806 1.0259 0.1402  -0.0277 0.1494  1180 ASP A CG  
971  O OD1 . ASP A 143 ? 0.9960 0.7056 1.0375 0.1427  -0.0636 0.1745  1180 ASP A OD1 
972  O OD2 . ASP A 143 ? 1.0484 0.6885 1.0892 0.1661  -0.0037 0.1453  1180 ASP A OD2 
973  N N   . LEU A 144 ? 0.9129 0.5726 0.7691 0.0306  0.0096  0.0757  1181 LEU A N   
974  C CA  . LEU A 144 ? 0.8708 0.5558 0.7036 0.0056  0.0212  0.0533  1181 LEU A CA  
975  C C   . LEU A 144 ? 0.8496 0.5387 0.6459 -0.0219 0.0033  0.0557  1181 LEU A C   
976  O O   . LEU A 144 ? 0.8033 0.5346 0.6026 -0.0348 -0.0004 0.0497  1181 LEU A O   
977  C CB  . LEU A 144 ? 0.9050 0.5521 0.7071 -0.0016 0.0506  0.0282  1181 LEU A CB  
978  C CG  . LEU A 144 ? 0.9246 0.5689 0.7574 0.0221  0.0761  0.0184  1181 LEU A CG  
979  C CD1 . LEU A 144 ? 0.9736 0.5693 0.7651 0.0099  0.1047  -0.0087 1181 LEU A CD1 
980  C CD2 . LEU A 144 ? 0.8734 0.5812 0.7389 0.0257  0.0807  0.0146  1181 LEU A CD2 
981  N N   . ILE A 145 ? 0.8875 0.5291 0.6486 -0.0305 -0.0050 0.0647  1182 ILE A N   
982  C CA  . ILE A 145 ? 0.8754 0.5173 0.6012 -0.0565 -0.0194 0.0676  1182 ILE A CA  
983  C C   . ILE A 145 ? 0.8438 0.5234 0.5932 -0.0517 -0.0456 0.0863  1182 ILE A C   
984  O O   . ILE A 145 ? 0.8137 0.5169 0.5495 -0.0713 -0.0530 0.0820  1182 ILE A O   
985  C CB  . ILE A 145 ? 0.9385 0.5146 0.6161 -0.0686 -0.0182 0.0734  1182 ILE A CB  
986  C CG1 . ILE A 145 ? 0.9665 0.5069 0.6171 -0.0824 0.0091  0.0496  1182 ILE A CG1 
987  C CG2 . ILE A 145 ? 0.9391 0.5160 0.5809 -0.0943 -0.0327 0.0793  1182 ILE A CG2 
988  C CD1 . ILE A 145 ? 1.0401 0.5057 0.6460 -0.0930 0.0155  0.0556  1182 ILE A CD1 
989  N N   . GLY A 146 ? 0.8526 0.5386 0.6392 -0.0259 -0.0587 0.1058  1183 GLY A N   
990  C CA  . GLY A 146 ? 0.8270 0.5565 0.6436 -0.0222 -0.0844 0.1216  1183 GLY A CA  
991  C C   . GLY A 146 ? 0.7647 0.5494 0.6112 -0.0284 -0.0780 0.1083  1183 GLY A C   
992  O O   . GLY A 146 ? 0.7415 0.5513 0.5848 -0.0439 -0.0925 0.1101  1183 GLY A O   
993  N N   . PHE A 147 ? 0.7434 0.5415 0.6142 -0.0173 -0.0547 0.0948  1184 PHE A N   
994  C CA  . PHE A 147 ? 0.6950 0.5386 0.5899 -0.0218 -0.0459 0.0850  1184 PHE A CA  
995  C C   . PHE A 147 ? 0.6728 0.5166 0.5298 -0.0461 -0.0414 0.0713  1184 PHE A C   
996  O O   . PHE A 147 ? 0.6415 0.5159 0.5096 -0.0543 -0.0443 0.0699  1184 PHE A O   
997  C CB  . PHE A 147 ? 0.6929 0.5457 0.6132 -0.0055 -0.0204 0.0747  1184 PHE A CB  
998  C CG  . PHE A 147 ? 0.7144 0.5732 0.6830 0.0218  -0.0189 0.0856  1184 PHE A CG  
999  C CD1 . PHE A 147 ? 0.7069 0.5997 0.7200 0.0307  -0.0409 0.1039  1184 PHE A CD1 
1000 C CD2 . PHE A 147 ? 0.7457 0.5789 0.7184 0.0385  0.0054  0.0760  1184 PHE A CD2 
1001 C CE1 . PHE A 147 ? 0.7254 0.6321 0.7927 0.0586  -0.0402 0.1147  1184 PHE A CE1 
1002 C CE2 . PHE A 147 ? 0.7670 0.6068 0.7911 0.0675  0.0100  0.0853  1184 PHE A CE2 
1003 C CZ  . PHE A 147 ? 0.7549 0.6347 0.8299 0.0790  -0.0135 0.1058  1184 PHE A CZ  
1004 N N   . GLY A 148 ? 0.6930 0.5023 0.5085 -0.0572 -0.0329 0.0610  1185 GLY A N   
1005 C CA  . GLY A 148 ? 0.6762 0.4902 0.4622 -0.0787 -0.0282 0.0477  1185 GLY A CA  
1006 C C   . GLY A 148 ? 0.6736 0.4885 0.4441 -0.0943 -0.0442 0.0536  1185 GLY A C   
1007 O O   . GLY A 148 ? 0.6470 0.4832 0.4157 -0.1054 -0.0418 0.0457  1185 GLY A O   
1008 N N   . LEU A 149 ? 0.7070 0.4967 0.4646 -0.0944 -0.0599 0.0679  1186 LEU A N   
1009 C CA  . LEU A 149 ? 0.7177 0.5027 0.4504 -0.1122 -0.0752 0.0731  1186 LEU A CA  
1010 C C   . LEU A 149 ? 0.6848 0.5079 0.4473 -0.1122 -0.0856 0.0758  1186 LEU A C   
1011 O O   . LEU A 149 ? 0.6773 0.5067 0.4244 -0.1295 -0.0857 0.0678  1186 LEU A O   
1012 C CB  . LEU A 149 ? 0.7706 0.5195 0.4800 -0.1100 -0.0923 0.0921  1186 LEU A CB  
1013 C CG  . LEU A 149 ? 0.7972 0.5388 0.4726 -0.1297 -0.1113 0.1001  1186 LEU A CG  
1014 C CD1 . LEU A 149 ? 0.8069 0.5304 0.4366 -0.1565 -0.0962 0.0839  1186 LEU A CD1 
1015 C CD2 . LEU A 149 ? 0.8530 0.5641 0.5098 -0.1222 -0.1336 0.1253  1186 LEU A CD2 
1016 N N   . GLN A 150 ? 0.6692 0.5163 0.4758 -0.0939 -0.0919 0.0856  1187 GLN A N   
1017 C CA  . GLN A 150 ? 0.6460 0.5291 0.4848 -0.0963 -0.1009 0.0883  1187 GLN A CA  
1018 C C   . GLN A 150 ? 0.6137 0.5117 0.4549 -0.1047 -0.0835 0.0734  1187 GLN A C   
1019 O O   . GLN A 150 ? 0.6074 0.5153 0.4489 -0.1183 -0.0880 0.0701  1187 GLN A O   
1020 C CB  . GLN A 150 ? 0.6372 0.5478 0.5295 -0.0749 -0.1042 0.0991  1187 GLN A CB  
1021 C CG  . GLN A 150 ? 0.6721 0.5771 0.5735 -0.0636 -0.1275 0.1181  1187 GLN A CG  
1022 C CD  . GLN A 150 ? 0.6640 0.6013 0.6278 -0.0390 -0.1270 0.1273  1187 GLN A CD  
1023 O OE1 . GLN A 150 ? 0.6389 0.6187 0.6448 -0.0409 -0.1283 0.1268  1187 GLN A OE1 
1024 N NE2 . GLN A 150 ? 0.6889 0.6048 0.6607 -0.0162 -0.1223 0.1346  1187 GLN A NE2 
1025 N N   . VAL A 151 ? 0.6003 0.4979 0.4416 -0.0965 -0.0640 0.0648  1188 VAL A N   
1026 C CA  . VAL A 151 ? 0.5770 0.4894 0.4210 -0.0999 -0.0495 0.0550  1188 VAL A CA  
1027 C C   . VAL A 151 ? 0.5844 0.4847 0.3984 -0.1172 -0.0490 0.0455  1188 VAL A C   
1028 O O   . VAL A 151 ? 0.5729 0.4828 0.3940 -0.1223 -0.0444 0.0413  1188 VAL A O   
1029 C CB  . VAL A 151 ? 0.5685 0.4850 0.4121 -0.0894 -0.0329 0.0487  1188 VAL A CB  
1030 C CG1 . VAL A 151 ? 0.5507 0.4826 0.3913 -0.0921 -0.0223 0.0417  1188 VAL A CG1 
1031 C CG2 . VAL A 151 ? 0.5653 0.4948 0.4391 -0.0729 -0.0270 0.0551  1188 VAL A CG2 
1032 N N   . ALA A 152 ? 0.6079 0.4844 0.3890 -0.1264 -0.0508 0.0418  1189 ALA A N   
1033 C CA  . ALA A 152 ? 0.6199 0.4857 0.3723 -0.1443 -0.0461 0.0309  1189 ALA A CA  
1034 C C   . ALA A 152 ? 0.6339 0.4958 0.3792 -0.1571 -0.0560 0.0320  1189 ALA A C   
1035 O O   . ALA A 152 ? 0.6332 0.4966 0.3729 -0.1668 -0.0464 0.0207  1189 ALA A O   
1036 C CB  . ALA A 152 ? 0.6499 0.4877 0.3667 -0.1545 -0.0449 0.0286  1189 ALA A CB  
1037 N N   . LYS A 153 ? 0.6517 0.5095 0.3985 -0.1570 -0.0752 0.0451  1190 LYS A N   
1038 C CA  . LYS A 153 ? 0.6725 0.5298 0.4104 -0.1726 -0.0887 0.0459  1190 LYS A CA  
1039 C C   . LYS A 153 ? 0.6497 0.5290 0.4224 -0.1707 -0.0822 0.0411  1190 LYS A C   
1040 O O   . LYS A 153 ? 0.6644 0.5378 0.4256 -0.1875 -0.0810 0.0317  1190 LYS A O   
1041 C CB  . LYS A 153 ? 0.6979 0.5545 0.4353 -0.1707 -0.1150 0.0638  1190 LYS A CB  
1042 C CG  . LYS A 153 ? 0.7386 0.5629 0.4326 -0.1750 -0.1234 0.0725  1190 LYS A CG  
1043 C CD  . LYS A 153 ? 0.7684 0.5932 0.4671 -0.1668 -0.1519 0.0951  1190 LYS A CD  
1044 C CE  . LYS A 153 ? 0.8219 0.6054 0.4693 -0.1722 -0.1605 0.1072  1190 LYS A CE  
1045 N NZ  . LYS A 153 ? 0.8557 0.6410 0.5121 -0.1589 -0.1909 0.1337  1190 LYS A NZ  
1046 N N   . GLY A 154 ? 0.6205 0.5204 0.4318 -0.1518 -0.0757 0.0470  1191 GLY A N   
1047 C CA  . GLY A 154 ? 0.6017 0.5175 0.4436 -0.1494 -0.0659 0.0453  1191 GLY A CA  
1048 C C   . GLY A 154 ? 0.5962 0.5032 0.4292 -0.1502 -0.0464 0.0336  1191 GLY A C   
1049 O O   . GLY A 154 ? 0.5983 0.5004 0.4381 -0.1577 -0.0395 0.0284  1191 GLY A O   
1050 N N   . MET A 155 ? 0.5909 0.4963 0.4114 -0.1424 -0.0373 0.0294  1192 MET A N   
1051 C CA  . MET A 155 ? 0.5872 0.4939 0.4077 -0.1388 -0.0209 0.0204  1192 MET A CA  
1052 C C   . MET A 155 ? 0.6136 0.5017 0.4099 -0.1559 -0.0158 0.0062  1192 MET A C   
1053 O O   . MET A 155 ? 0.6160 0.5022 0.4199 -0.1535 -0.0012 -0.0019 1192 MET A O   
1054 C CB  . MET A 155 ? 0.5740 0.4929 0.3912 -0.1287 -0.0154 0.0188  1192 MET A CB  
1055 C CG  . MET A 155 ? 0.5559 0.4930 0.3930 -0.1118 -0.0134 0.0287  1192 MET A CG  
1056 S SD  . MET A 155 ? 0.5496 0.4962 0.4120 -0.1000 -0.0038 0.0372  1192 MET A SD  
1057 C CE  . MET A 155 ? 0.5589 0.5009 0.4187 -0.1015 0.0058  0.0264  1192 MET A CE  
1058 N N   . LYS A 156 ? 0.6410 0.5138 0.4067 -0.1723 -0.0268 0.0042  1193 LYS A N   
1059 C CA  . LYS A 156 ? 0.6774 0.5296 0.4108 -0.1931 -0.0212 -0.0099 1193 LYS A CA  
1060 C C   . LYS A 156 ? 0.6969 0.5395 0.4357 -0.2026 -0.0188 -0.0163 1193 LYS A C   
1061 O O   . LYS A 156 ? 0.7172 0.5454 0.4463 -0.2109 -0.0015 -0.0323 1193 LYS A O   
1062 C CB  . LYS A 156 ? 0.7086 0.5437 0.4019 -0.2091 -0.0370 -0.0054 1193 LYS A CB  
1063 C CG  . LYS A 156 ? 0.7544 0.5652 0.4021 -0.2349 -0.0311 -0.0196 1193 LYS A CG  
1064 C CD  . LYS A 156 ? 0.7945 0.5855 0.3963 -0.2505 -0.0498 -0.0096 1193 LYS A CD  
1065 C CE  . LYS A 156 ? 0.8487 0.6137 0.3959 -0.2797 -0.0432 -0.0236 1193 LYS A CE  
1066 N NZ  . LYS A 156 ? 0.8961 0.6390 0.3924 -0.2944 -0.0639 -0.0089 1193 LYS A NZ  
1067 N N   . TYR A 157 ? 0.6946 0.5452 0.4511 -0.2025 -0.0342 -0.0051 1194 TYR A N   
1068 C CA  . TYR A 157 ? 0.7148 0.5568 0.4783 -0.2157 -0.0329 -0.0114 1194 TYR A CA  
1069 C C   . TYR A 157 ? 0.7056 0.5434 0.4968 -0.2016 -0.0097 -0.0152 1194 TYR A C   
1070 O O   . TYR A 157 ? 0.7339 0.5482 0.5170 -0.2117 0.0055  -0.0300 1194 TYR A O   
1071 C CB  . TYR A 157 ? 0.7103 0.5715 0.4949 -0.2187 -0.0549 0.0023  1194 TYR A CB  
1072 C CG  . TYR A 157 ? 0.7307 0.5876 0.5281 -0.2358 -0.0540 -0.0041 1194 TYR A CG  
1073 C CD1 . TYR A 157 ? 0.7706 0.6221 0.5435 -0.2645 -0.0708 -0.0119 1194 TYR A CD1 
1074 C CD2 . TYR A 157 ? 0.7171 0.5739 0.5479 -0.2258 -0.0369 -0.0018 1194 TYR A CD2 
1075 C CE1 . TYR A 157 ? 0.7938 0.6410 0.5774 -0.2853 -0.0696 -0.0210 1194 TYR A CE1 
1076 C CE2 . TYR A 157 ? 0.7421 0.5894 0.5836 -0.2449 -0.0333 -0.0086 1194 TYR A CE2 
1077 C CZ  . TYR A 157 ? 0.7796 0.6228 0.5989 -0.2759 -0.0493 -0.0199 1194 TYR A CZ  
1078 O OH  . TYR A 157 ? 0.8096 0.6432 0.6386 -0.2995 -0.0454 -0.0295 1194 TYR A OH  
1079 N N   . LEU A 158 ? 0.6742 0.5318 0.4952 -0.1780 -0.0069 -0.0012 1195 LEU A N   
1080 C CA  . LEU A 158 ? 0.6703 0.5248 0.5155 -0.1615 0.0113  0.0018  1195 LEU A CA  
1081 C C   . LEU A 158 ? 0.6825 0.5270 0.5209 -0.1549 0.0289  -0.0107 1195 LEU A C   
1082 O O   . LEU A 158 ? 0.7031 0.5277 0.5514 -0.1509 0.0460  -0.0162 1195 LEU A O   
1083 C CB  . LEU A 158 ? 0.6395 0.5196 0.5067 -0.1399 0.0085  0.0195  1195 LEU A CB  
1084 C CG  . LEU A 158 ? 0.6315 0.5249 0.5165 -0.1424 -0.0016 0.0317  1195 LEU A CG  
1085 C CD1 . LEU A 158 ? 0.6083 0.5228 0.5082 -0.1219 0.0015  0.0458  1195 LEU A CD1 
1086 C CD2 . LEU A 158 ? 0.6533 0.5313 0.5516 -0.1551 0.0048  0.0311  1195 LEU A CD2 
1087 N N   . ALA A 159 ? 0.6742 0.5319 0.4984 -0.1539 0.0264  -0.0154 1196 ALA A N   
1088 C CA  . ALA A 159 ? 0.6834 0.5425 0.5080 -0.1484 0.0434  -0.0283 1196 ALA A CA  
1089 C C   . ALA A 159 ? 0.7275 0.5553 0.5341 -0.1659 0.0587  -0.0483 1196 ALA A C   
1090 O O   . ALA A 159 ? 0.7415 0.5621 0.5643 -0.1554 0.0797  -0.0578 1196 ALA A O   
1091 C CB  . ALA A 159 ? 0.6707 0.5480 0.4799 -0.1524 0.0380  -0.0313 1196 ALA A CB  
1092 N N   . SER A 160 ? 0.7549 0.5644 0.5277 -0.1922 0.0478  -0.0548 1197 SER A N   
1093 C CA  . SER A 160 ? 0.8056 0.5832 0.5490 -0.2155 0.0610  -0.0767 1197 SER A CA  
1094 C C   . SER A 160 ? 0.8309 0.5829 0.5928 -0.2131 0.0763  -0.0825 1197 SER A C   
1095 O O   . SER A 160 ? 0.8742 0.5970 0.6238 -0.2224 0.0991  -0.1039 1197 SER A O   
1096 C CB  . SER A 160 ? 0.8300 0.5981 0.5297 -0.2447 0.0402  -0.0784 1197 SER A CB  
1097 O OG  . SER A 160 ? 0.8191 0.5946 0.5320 -0.2475 0.0186  -0.0641 1197 SER A OG  
1098 N N   . LYS A 161 ? 0.8131 0.5723 0.6031 -0.2016 0.0669  -0.0644 1198 LYS A N   
1099 C CA  . LYS A 161 ? 0.8412 0.5717 0.6489 -0.1998 0.0823  -0.0661 1198 LYS A CA  
1100 C C   . LYS A 161 ? 0.8249 0.5597 0.6696 -0.1645 0.0983  -0.0534 1198 LYS A C   
1101 O O   . LYS A 161 ? 0.8399 0.5524 0.7032 -0.1562 0.1087  -0.0452 1198 LYS A O   
1102 C CB  . LYS A 161 ? 0.8388 0.5741 0.6539 -0.2128 0.0643  -0.0537 1198 LYS A CB  
1103 C CG  . LYS A 161 ? 0.8586 0.5987 0.6435 -0.2454 0.0421  -0.0619 1198 LYS A CG  
1104 C CD  . LYS A 161 ? 0.9218 0.6246 0.6695 -0.2759 0.0531  -0.0895 1198 LYS A CD  
1105 C CE  . LYS A 161 ? 0.9451 0.6575 0.6566 -0.3087 0.0259  -0.0948 1198 LYS A CE  
1106 N NZ  . LYS A 161 ? 0.9393 0.6723 0.6736 -0.3207 0.0042  -0.0830 1198 LYS A NZ  
1107 N N   . LYS A 162 ? 0.7982 0.5615 0.6522 -0.1455 0.0998  -0.0512 1199 LYS A N   
1108 C CA  . LYS A 162 ? 0.7838 0.5623 0.6730 -0.1114 0.1094  -0.0376 1199 LYS A CA  
1109 C C   . LYS A 162 ? 0.7660 0.5509 0.6721 -0.0971 0.0990  -0.0110 1199 LYS A C   
1110 O O   . LYS A 162 ? 0.7922 0.5500 0.7138 -0.0849 0.1120  -0.0019 1199 LYS A O   
1111 C CB  . LYS A 162 ? 0.8262 0.5726 0.7303 -0.1001 0.1383  -0.0511 1199 LYS A CB  
1112 C CG  . LYS A 162 ? 0.8411 0.5928 0.7381 -0.1061 0.1543  -0.0762 1199 LYS A CG  
1113 C CD  . LYS A 162 ? 0.8882 0.6083 0.8059 -0.0916 0.1872  -0.0913 1199 LYS A CD  
1114 C CE  . LYS A 162 ? 0.8815 0.6184 0.8495 -0.0485 0.1927  -0.0699 1199 LYS A CE  
1115 N NZ  . LYS A 162 ? 0.9305 0.6375 0.9243 -0.0304 0.2266  -0.0854 1199 LYS A NZ  
1116 N N   . PHE A 163 ? 0.7284 0.5453 0.6292 -0.0993 0.0782  0.0010  1200 PHE A N   
1117 C CA  . PHE A 163 ? 0.7123 0.5412 0.6256 -0.0867 0.0703  0.0247  1200 PHE A CA  
1118 C C   . PHE A 163 ? 0.6764 0.5479 0.5931 -0.0707 0.0584  0.0348  1200 PHE A C   
1119 O O   . PHE A 163 ? 0.6545 0.5452 0.5575 -0.0816 0.0460  0.0288  1200 PHE A O   
1120 C CB  . PHE A 163 ? 0.7121 0.5357 0.6174 -0.1088 0.0600  0.0266  1200 PHE A CB  
1121 C CG  . PHE A 163 ? 0.7048 0.5392 0.6230 -0.0997 0.0572  0.0485  1200 PHE A CG  
1122 C CD1 . PHE A 163 ? 0.7359 0.5423 0.6635 -0.1033 0.0694  0.0572  1200 PHE A CD1 
1123 C CD2 . PHE A 163 ? 0.6742 0.5432 0.5922 -0.0905 0.0454  0.0589  1200 PHE A CD2 
1124 C CE1 . PHE A 163 ? 0.7329 0.5487 0.6692 -0.0978 0.0703  0.0773  1200 PHE A CE1 
1125 C CE2 . PHE A 163 ? 0.6724 0.5503 0.5982 -0.0841 0.0468  0.0769  1200 PHE A CE2 
1126 C CZ  . PHE A 163 ? 0.7011 0.5539 0.6358 -0.0879 0.0594  0.0867  1200 PHE A CZ  
1127 N N   . VAL A 164 ? 0.6767 0.5604 0.6097 -0.0455 0.0619  0.0503  1201 VAL A N   
1128 C CA  . VAL A 164 ? 0.6515 0.5771 0.5856 -0.0323 0.0498  0.0598  1201 VAL A CA  
1129 C C   . VAL A 164 ? 0.6446 0.5749 0.5703 -0.0313 0.0429  0.0781  1201 VAL A C   
1130 O O   . VAL A 164 ? 0.6674 0.5803 0.5977 -0.0215 0.0496  0.0957  1201 VAL A O   
1131 C CB  . VAL A 164 ? 0.6624 0.6067 0.6183 -0.0061 0.0534  0.0681  1201 VAL A CB  
1132 C CG1 . VAL A 164 ? 0.6429 0.6360 0.5973 0.0025  0.0379  0.0754  1201 VAL A CG1 
1133 C CG2 . VAL A 164 ? 0.6727 0.6120 0.6437 -0.0060 0.0665  0.0481  1201 VAL A CG2 
1134 N N   . HIS A 165 ? 0.6193 0.5697 0.5317 -0.0416 0.0321  0.0735  1202 HIS A N   
1135 C CA  . HIS A 165 ? 0.6161 0.5715 0.5217 -0.0428 0.0295  0.0858  1202 HIS A CA  
1136 C C   . HIS A 165 ? 0.6248 0.6010 0.5243 -0.0253 0.0276  0.1028  1202 HIS A C   
1137 O O   . HIS A 165 ? 0.6371 0.6061 0.5317 -0.0217 0.0330  0.1193  1202 HIS A O   
1138 C CB  . HIS A 165 ? 0.5957 0.5621 0.4912 -0.0561 0.0209  0.0743  1202 HIS A CB  
1139 C CG  . HIS A 165 ? 0.5947 0.5631 0.4915 -0.0591 0.0223  0.0826  1202 HIS A CG  
1140 N ND1 . HIS A 165 ? 0.6026 0.5834 0.4925 -0.0497 0.0269  0.0951  1202 HIS A ND1 
1141 C CD2 . HIS A 165 ? 0.5908 0.5533 0.4971 -0.0710 0.0203  0.0794  1202 HIS A CD2 
1142 C CE1 . HIS A 165 ? 0.6021 0.5834 0.4992 -0.0555 0.0316  0.0977  1202 HIS A CE1 
1143 N NE2 . HIS A 165 ? 0.5926 0.5656 0.5042 -0.0674 0.0263  0.0887  1202 HIS A NE2 
1144 N N   . ARG A 166 ? 0.6203 0.6246 0.5183 -0.0175 0.0197  0.0982  1203 ARG A N   
1145 C CA  . ARG A 166 ? 0.6330 0.6643 0.5242 -0.0017 0.0129  0.1135  1203 ARG A CA  
1146 C C   . ARG A 166 ? 0.6288 0.6775 0.4945 -0.0097 0.0079  0.1124  1203 ARG A C   
1147 O O   . ARG A 166 ? 0.6329 0.7132 0.4879 -0.0100 -0.0020 0.1066  1203 ARG A O   
1148 C CB  . ARG A 166 ? 0.6654 0.6776 0.5612 0.0154  0.0191  0.1390  1203 ARG A CB  
1149 C CG  . ARG A 166 ? 0.6796 0.6742 0.6018 0.0282  0.0259  0.1394  1203 ARG A CG  
1150 C CD  . ARG A 166 ? 0.7234 0.6946 0.6494 0.0492  0.0320  0.1676  1203 ARG A CD  
1151 N NE  . ARG A 166 ? 0.7426 0.7136 0.6977 0.0704  0.0347  0.1693  1203 ARG A NE  
1152 C CZ  . ARG A 166 ? 0.7668 0.6943 0.7395 0.0742  0.0520  0.1652  1203 ARG A CZ  
1153 N NH1 . ARG A 166 ? 0.7860 0.7155 0.7883 0.0980  0.0566  0.1677  1203 ARG A NH1 
1154 N NH2 . ARG A 166 ? 0.7738 0.6578 0.7367 0.0535  0.0654  0.1572  1203 ARG A NH2 
1155 N N   . ASP A 167 ? 0.6259 0.6553 0.4837 -0.0173 0.0165  0.1161  1204 ASP A N   
1156 C CA  . ASP A 167 ? 0.6243 0.6651 0.4599 -0.0238 0.0176  0.1129  1204 ASP A CA  
1157 C C   . ASP A 167 ? 0.5995 0.6300 0.4418 -0.0371 0.0203  0.0952  1204 ASP A C   
1158 O O   . ASP A 167 ? 0.5998 0.6196 0.4479 -0.0409 0.0292  0.0979  1204 ASP A O   
1159 C CB  . ASP A 167 ? 0.6513 0.6836 0.4736 -0.0195 0.0282  0.1330  1204 ASP A CB  
1160 C CG  . ASP A 167 ? 0.6618 0.7048 0.4583 -0.0261 0.0343  0.1279  1204 ASP A CG  
1161 O OD1 . ASP A 167 ? 0.6664 0.7301 0.4417 -0.0284 0.0259  0.1176  1204 ASP A OD1 
1162 O OD2 . ASP A 167 ? 0.6694 0.7005 0.4679 -0.0304 0.0494  0.1327  1204 ASP A OD2 
1163 N N   . LEU A 168 ? 0.5807 0.6158 0.4237 -0.0437 0.0125  0.0785  1205 LEU A N   
1164 C CA  . LEU A 168 ? 0.5664 0.5888 0.4107 -0.0544 0.0123  0.0648  1205 LEU A CA  
1165 C C   . LEU A 168 ? 0.5709 0.6001 0.3944 -0.0575 0.0147  0.0558  1205 LEU A C   
1166 O O   . LEU A 168 ? 0.5755 0.6204 0.3817 -0.0606 0.0103  0.0478  1205 LEU A O   
1167 C CB  . LEU A 168 ? 0.5568 0.5738 0.4045 -0.0624 0.0058  0.0525  1205 LEU A CB  
1168 C CG  . LEU A 168 ? 0.5530 0.5522 0.3956 -0.0733 0.0030  0.0420  1205 LEU A CG  
1169 C CD1 . LEU A 168 ? 0.5507 0.5354 0.4095 -0.0740 0.0028  0.0494  1205 LEU A CD1 
1170 C CD2 . LEU A 168 ? 0.5518 0.5455 0.3879 -0.0841 -0.0008 0.0302  1205 LEU A CD2 
1171 N N   . ALA A 169 ? 0.5710 0.5893 0.3990 -0.0572 0.0228  0.0557  1206 ALA A N   
1172 C CA  . ALA A 169 ? 0.5858 0.6022 0.3956 -0.0590 0.0304  0.0449  1206 ALA A CA  
1173 C C   . ALA A 169 ? 0.5847 0.5872 0.4153 -0.0554 0.0382  0.0447  1206 ALA A C   
1174 O O   . ALA A 169 ? 0.5716 0.5739 0.4299 -0.0531 0.0363  0.0545  1206 ALA A O   
1175 C CB  . ALA A 169 ? 0.6077 0.6396 0.3946 -0.0564 0.0379  0.0495  1206 ALA A CB  
1176 N N   . ALA A 170 ? 0.6029 0.5949 0.4221 -0.0549 0.0472  0.0326  1207 ALA A N   
1177 C CA  . ALA A 170 ? 0.6081 0.5894 0.4524 -0.0468 0.0556  0.0324  1207 ALA A CA  
1178 C C   . ALA A 170 ? 0.6081 0.6068 0.4759 -0.0403 0.0692  0.0429  1207 ALA A C   
1179 O O   . ALA A 170 ? 0.5990 0.6029 0.5052 -0.0345 0.0696  0.0494  1207 ALA A O   
1180 C CB  . ALA A 170 ? 0.6378 0.5991 0.4626 -0.0461 0.0673  0.0161  1207 ALA A CB  
1181 N N   . ARG A 171 ? 0.6233 0.6329 0.4671 -0.0427 0.0795  0.0454  1208 ARG A N   
1182 C CA  . ARG A 171 ? 0.6340 0.6565 0.4910 -0.0401 0.0967  0.0557  1208 ARG A CA  
1183 C C   . ARG A 171 ? 0.6122 0.6420 0.5018 -0.0419 0.0887  0.0717  1208 ARG A C   
1184 O O   . ARG A 171 ? 0.6178 0.6582 0.5341 -0.0419 0.1024  0.0792  1208 ARG A O   
1185 C CB  . ARG A 171 ? 0.6637 0.6919 0.4764 -0.0443 0.1063  0.0581  1208 ARG A CB  
1186 C CG  . ARG A 171 ? 0.6589 0.6920 0.4495 -0.0473 0.0877  0.0684  1208 ARG A CG  
1187 C CD  . ARG A 171 ? 0.6951 0.7373 0.4418 -0.0498 0.0933  0.0758  1208 ARG A CD  
1188 N NE  . ARG A 171 ? 0.6931 0.7448 0.4246 -0.0484 0.0729  0.0865  1208 ARG A NE  
1189 C CZ  . ARG A 171 ? 0.6842 0.7448 0.4061 -0.0515 0.0559  0.0750  1208 ARG A CZ  
1190 N NH1 . ARG A 171 ? 0.6850 0.7402 0.3987 -0.0591 0.0582  0.0523  1208 ARG A NH1 
1191 N NH2 . ARG A 171 ? 0.6785 0.7530 0.4013 -0.0470 0.0385  0.0860  1208 ARG A NH2 
1192 N N   . ASN A 172 ? 0.5920 0.6156 0.4795 -0.0456 0.0691  0.0748  1209 ASN A N   
1193 C CA  . ASN A 172 ? 0.5772 0.6006 0.4891 -0.0502 0.0626  0.0861  1209 ASN A CA  
1194 C C   . ASN A 172 ? 0.5582 0.5791 0.4979 -0.0534 0.0480  0.0814  1209 ASN A C   
1195 O O   . ASN A 172 ? 0.5484 0.5637 0.4969 -0.0610 0.0375  0.0847  1209 ASN A O   
1196 C CB  . ASN A 172 ? 0.5780 0.5941 0.4688 -0.0513 0.0544  0.0927  1209 ASN A CB  
1197 C CG  . ASN A 172 ? 0.6014 0.6227 0.4605 -0.0466 0.0627  0.1008  1209 ASN A CG  
1198 O OD1 . ASN A 172 ? 0.6206 0.6440 0.4771 -0.0468 0.0785  0.1109  1209 ASN A OD1 
1199 N ND2 . ASN A 172 ? 0.6047 0.6306 0.4387 -0.0440 0.0519  0.0970  1209 ASN A ND2 
1200 N N   . CYS A 173 ? 0.5595 0.5817 0.5101 -0.0476 0.0476  0.0740  1210 CYS A N   
1201 C CA  . CYS A 173 ? 0.5528 0.5751 0.5297 -0.0483 0.0319  0.0741  1210 CYS A CA  
1202 C C   . CYS A 173 ? 0.5605 0.6028 0.5801 -0.0394 0.0411  0.0768  1210 CYS A C   
1203 O O   . CYS A 173 ? 0.5744 0.6188 0.5923 -0.0298 0.0603  0.0718  1210 CYS A O   
1204 C CB  . CYS A 173 ? 0.5561 0.5571 0.5079 -0.0470 0.0201  0.0659  1210 CYS A CB  
1205 S SG  . CYS A 173 ? 0.5472 0.5334 0.4596 -0.0586 0.0107  0.0607  1210 CYS A SG  
1206 N N   . MET A 174 ? 0.5561 0.6156 0.6147 -0.0433 0.0278  0.0834  1211 MET A N   
1207 C CA  . MET A 174 ? 0.5609 0.6521 0.6733 -0.0362 0.0361  0.0875  1211 MET A CA  
1208 C C   . MET A 174 ? 0.5648 0.6652 0.7078 -0.0277 0.0137  0.0916  1211 MET A C   
1209 O O   . MET A 174 ? 0.5653 0.6491 0.6865 -0.0346 -0.0101 0.0935  1211 MET A O   
1210 C CB  . MET A 174 ? 0.5568 0.6710 0.6968 -0.0520 0.0407  0.0936  1211 MET A CB  
1211 C CG  . MET A 174 ? 0.5657 0.6685 0.6770 -0.0584 0.0636  0.0949  1211 MET A CG  
1212 S SD  . MET A 174 ? 0.5859 0.6968 0.6945 -0.0452 0.0976  0.0911  1211 MET A SD  
1213 C CE  . MET A 174 ? 0.6030 0.7043 0.6816 -0.0591 0.1173  0.1007  1211 MET A CE  
1214 N N   . LEU A 175 ? 0.5739 0.7018 0.7677 -0.0119 0.0225  0.0940  1212 LEU A N   
1215 C CA  . LEU A 175 ? 0.5846 0.7259 0.8158 0.0024  0.0013  0.1020  1212 LEU A CA  
1216 C C   . LEU A 175 ? 0.5782 0.7766 0.8823 0.0006  -0.0036 0.1095  1212 LEU A C   
1217 O O   . LEU A 175 ? 0.5751 0.8008 0.9137 0.0021  0.0233  0.1058  1212 LEU A O   
1218 C CB  . LEU A 175 ? 0.6086 0.7301 0.8415 0.0285  0.0177  0.0974  1212 LEU A CB  
1219 C CG  . LEU A 175 ? 0.6259 0.6924 0.7957 0.0301  0.0139  0.0915  1212 LEU A CG  
1220 C CD1 . LEU A 175 ? 0.6317 0.6827 0.7835 0.0236  -0.0211 0.1024  1212 LEU A CD1 
1221 C CD2 . LEU A 175 ? 0.6174 0.6625 0.7312 0.0135  0.0291  0.0795  1212 LEU A CD2 
1222 N N   . ASP A 176 ? 0.5807 0.7987 0.9064 -0.0045 -0.0381 0.1198  1213 ASP A N   
1223 C CA  . ASP A 176 ? 0.5774 0.8576 0.9773 -0.0077 -0.0497 0.1271  1213 ASP A CA  
1224 C C   . ASP A 176 ? 0.5925 0.8978 1.0489 0.0255  -0.0556 0.1366  1213 ASP A C   
1225 O O   . ASP A 176 ? 0.6068 0.8751 1.0423 0.0492  -0.0420 0.1346  1213 ASP A O   
1226 C CB  . ASP A 176 ? 0.5777 0.8692 0.9679 -0.0354 -0.0848 0.1316  1213 ASP A CB  
1227 C CG  . ASP A 176 ? 0.5979 0.8688 0.9582 -0.0303 -0.1218 0.1418  1213 ASP A CG  
1228 O OD1 . ASP A 176 ? 0.6118 0.8532 0.9566 -0.0046 -0.1201 0.1467  1213 ASP A OD1 
1229 O OD2 . ASP A 176 ? 0.6062 0.8874 0.9550 -0.0541 -0.1510 0.1444  1213 ASP A OD2 
1230 N N   . GLU A 177 ? 0.5931 0.9619 1.1231 0.0269  -0.0759 0.1467  1214 GLU A N   
1231 C CA  . GLU A 177 ? 0.6109 1.0137 1.2096 0.0622  -0.0821 0.1582  1214 GLU A CA  
1232 C C   . GLU A 177 ? 0.6393 1.0084 1.2071 0.0787  -0.1186 0.1745  1214 GLU A C   
1233 O O   . GLU A 177 ? 0.6630 1.0312 1.2657 0.1147  -0.1188 0.1848  1214 GLU A O   
1234 C CB  . GLU A 177 ? 0.6035 1.0953 1.2988 0.0579  -0.0930 0.1643  1214 GLU A CB  
1235 C CG  . GLU A 177 ? 0.6054 1.1309 1.3048 0.0311  -0.1414 0.1744  1214 GLU A CG  
1236 C CD  . GLU A 177 ? 0.5903 1.1056 1.2460 -0.0151 -0.1395 0.1616  1214 GLU A CD  
1237 O OE1 . GLU A 177 ? 0.5967 1.1439 1.2607 -0.0414 -0.1744 0.1654  1214 GLU A OE1 
1238 O OE2 . GLU A 177 ? 0.5785 1.0521 1.1904 -0.0248 -0.1036 0.1480  1214 GLU A OE2 
1239 N N   . LYS A 178 ? 0.6432 0.9812 1.1443 0.0527  -0.1466 0.1770  1215 LYS A N   
1240 C CA  . LYS A 178 ? 0.6769 0.9733 1.1322 0.0625  -0.1778 0.1923  1215 LYS A CA  
1241 C C   . LYS A 178 ? 0.6852 0.9016 1.0643 0.0674  -0.1540 0.1824  1215 LYS A C   
1242 O O   . LYS A 178 ? 0.7128 0.8827 1.0379 0.0681  -0.1735 0.1918  1215 LYS A O   
1243 C CB  . LYS A 178 ? 0.6855 0.9873 1.1018 0.0290  -0.2174 0.1978  1215 LYS A CB  
1244 C CG  . LYS A 178 ? 0.6887 1.0697 1.1720 0.0180  -0.2497 0.2077  1215 LYS A CG  
1245 C CD  . LYS A 178 ? 0.6596 1.0763 1.1620 -0.0167 -0.2353 0.1897  1215 LYS A CD  
1246 C CE  . LYS A 178 ? 0.6674 1.1629 1.2321 -0.0347 -0.2698 0.1969  1215 LYS A CE  
1247 N NZ  . LYS A 178 ? 0.6484 1.1635 1.2165 -0.0758 -0.2556 0.1779  1215 LYS A NZ  
1248 N N   . PHE A 179 ? 0.6658 0.8682 1.0392 0.0687  -0.1122 0.1638  1216 PHE A N   
1249 C CA  . PHE A 179 ? 0.6721 0.8083 0.9771 0.0690  -0.0888 0.1511  1216 PHE A CA  
1250 C C   . PHE A 179 ? 0.6651 0.7659 0.8957 0.0394  -0.1057 0.1482  1216 PHE A C   
1251 O O   . PHE A 179 ? 0.6880 0.7371 0.8650 0.0405  -0.1101 0.1494  1216 PHE A O   
1252 C CB  . PHE A 179 ? 0.7147 0.8117 1.0194 0.1010  -0.0843 0.1582  1216 PHE A CB  
1253 C CG  . PHE A 179 ? 0.7285 0.8557 1.1087 0.1340  -0.0630 0.1590  1216 PHE A CG  
1254 C CD1 . PHE A 179 ? 0.7396 0.8393 1.1128 0.1464  -0.0202 0.1404  1216 PHE A CD1 
1255 C CD2 . PHE A 179 ? 0.7363 0.9216 1.1957 0.1526  -0.0851 0.1772  1216 PHE A CD2 
1256 C CE1 . PHE A 179 ? 0.7565 0.8819 1.1989 0.1770  0.0044  0.1382  1216 PHE A CE1 
1257 C CE2 . PHE A 179 ? 0.7492 0.9663 1.2858 0.1854  -0.0623 0.1769  1216 PHE A CE2 
1258 C CZ  . PHE A 179 ? 0.7596 0.9442 1.2871 0.1980  -0.0153 0.1566  1216 PHE A CZ  
1259 N N   . THR A 180 ? 0.6364 0.7638 0.8657 0.0124  -0.1118 0.1431  1217 THR A N   
1260 C CA  . THR A 180 ? 0.6315 0.7298 0.7980 -0.0154 -0.1236 0.1376  1217 THR A CA  
1261 C C   . THR A 180 ? 0.6018 0.6847 0.7400 -0.0278 -0.0939 0.1206  1217 THR A C   
1262 O O   . THR A 180 ? 0.5812 0.6936 0.7502 -0.0339 -0.0789 0.1161  1217 THR A O   
1263 C CB  . THR A 180 ? 0.6349 0.7669 0.8150 -0.0380 -0.1535 0.1436  1217 THR A CB  
1264 O OG1 . THR A 180 ? 0.6616 0.8190 0.8766 -0.0231 -0.1836 0.1626  1217 THR A OG1 
1265 C CG2 . THR A 180 ? 0.6444 0.7416 0.7571 -0.0656 -0.1646 0.1368  1217 THR A CG2 
1266 N N   . VAL A 181 ? 1.1358 1.1592 0.8087 -0.0158 -0.0611 0.0393  1218 VAL A N   
1267 C CA  . VAL A 181 ? 1.0975 1.1502 0.8010 -0.0297 -0.0424 0.0500  1218 VAL A CA  
1268 C C   . VAL A 181 ? 1.1835 1.1631 0.8079 0.0081  -0.0730 0.0372  1218 VAL A C   
1269 O O   . VAL A 181 ? 1.2749 1.1980 0.8046 0.0724  -0.0713 0.0350  1218 VAL A O   
1270 C CB  . VAL A 181 ? 1.0565 1.1655 0.7939 -0.0182 0.0160  0.0800  1218 VAL A CB  
1271 C CG1 . VAL A 181 ? 1.0311 1.1626 0.7983 -0.0285 0.0301  0.0918  1218 VAL A CG1 
1272 C CG2 . VAL A 181 ? 0.9812 1.1489 0.7943 -0.0539 0.0328  0.0887  1218 VAL A CG2 
1273 N N   . LYS A 182 ? 1.1616 1.1397 0.8200 -0.0255 -0.1009 0.0308  1219 LYS A N   
1274 C CA  . LYS A 182 ? 1.2423 1.1495 0.8351 0.0041  -0.1375 0.0175  1219 LYS A CA  
1275 C C   . LYS A 182 ? 1.1915 1.1421 0.8236 -0.0147 -0.1086 0.0311  1219 LYS A C   
1276 O O   . LYS A 182 ? 1.1060 1.1168 0.8243 -0.0675 -0.0998 0.0396  1219 LYS A O   
1277 C CB  . LYS A 182 ? 1.2812 1.1318 0.8873 -0.0194 -0.2164 -0.0006 1219 LYS A CB  
1278 C CG  . LYS A 182 ? 1.3511 1.1393 0.9140 0.0024  -0.2626 -0.0171 1219 LYS A CG  
1279 C CD  . LYS A 182 ? 1.4044 1.1263 0.9961 -0.0195 -0.3551 -0.0284 1219 LYS A CD  
1280 C CE  . LYS A 182 ? 1.4723 1.1313 1.0355 -0.0032 -0.4094 -0.0434 1219 LYS A CE  
1281 N NZ  . LYS A 182 ? 1.6090 1.1650 1.0126 0.0828  -0.4267 -0.0718 1219 LYS A NZ  
1282 N N   . VAL A 183 ? 1.2552 1.1713 0.8158 0.0362  -0.0936 0.0346  1220 VAL A N   
1283 C CA  . VAL A 183 ? 1.2189 1.1692 0.8103 0.0246  -0.0678 0.0485  1220 VAL A CA  
1284 C C   . VAL A 183 ? 1.2368 1.1500 0.8367 -0.0030 -0.1230 0.0301  1220 VAL A C   
1285 O O   . VAL A 183 ? 1.3357 1.1620 0.8567 0.0333  -0.1723 0.0106  1220 VAL A O   
1286 C CB  . VAL A 183 ? 1.2845 1.2152 0.8019 0.0949  -0.0282 0.0678  1220 VAL A CB  
1287 C CG1 . VAL A 183 ? 1.2484 1.2121 0.8024 0.0822  -0.0057 0.0835  1220 VAL A CG1 
1288 C CG2 . VAL A 183 ? 1.2707 1.2465 0.8010 0.1244  0.0286  0.1005  1220 VAL A CG2 
1289 N N   . ALA A 184 ? 1.1523 1.1272 0.8461 -0.0618 -0.1172 0.0387  1221 ALA A N   
1290 C CA  . ALA A 184 ? 1.1574 1.1158 0.8859 -0.0932 -0.1620 0.0340  1221 ALA A CA  
1291 C C   . ALA A 184 ? 1.1355 1.1183 0.8755 -0.0982 -0.1376 0.0422  1221 ALA A C   
1292 O O   . ALA A 184 ? 1.0804 1.1182 0.8452 -0.1018 -0.0873 0.0560  1221 ALA A O   
1293 C CB  . ALA A 184 ? 1.0890 1.0995 0.9110 -0.1445 -0.1696 0.0465  1221 ALA A CB  
1294 N N   . ASP A 185 ? 1.1860 1.1230 0.9143 -0.0995 -0.1810 0.0348  1222 ASP A N   
1295 C CA  . ASP A 185 ? 1.1716 1.1264 0.9111 -0.1062 -0.1648 0.0413  1222 ASP A CA  
1296 C C   . ASP A 185 ? 1.1337 1.1166 0.9580 -0.1553 -0.1907 0.0530  1222 ASP A C   
1297 O O   . ASP A 185 ? 1.1704 1.1162 1.0200 -0.1677 -0.2470 0.0536  1222 ASP A O   
1298 C CB  . ASP A 185 ? 1.2716 1.1461 0.9145 -0.0542 -0.1881 0.0267  1222 ASP A CB  
1299 C CG  . ASP A 185 ? 1.2531 1.1462 0.9018 -0.0560 -0.1662 0.0345  1222 ASP A CG  
1300 O OD1 . ASP A 185 ? 1.1644 1.1325 0.8876 -0.0944 -0.1295 0.0506  1222 ASP A OD1 
1301 O OD2 . ASP A 185 ? 1.3379 1.1629 0.9089 -0.0143 -0.1901 0.0230  1222 ASP A OD2 
1302 N N   . PHE A 186 ? 1.0713 1.1182 0.9439 -0.1789 -0.1517 0.0675  1223 PHE A N   
1303 C CA  . PHE A 186 ? 1.0411 1.1226 0.9878 -0.2138 -0.1627 0.0872  1223 PHE A CA  
1304 C C   . PHE A 186 ? 1.0750 1.1286 1.0090 -0.2110 -0.1805 0.0852  1223 PHE A C   
1305 O O   . PHE A 186 ? 1.0652 1.1328 1.0599 -0.2349 -0.2013 0.1048  1223 PHE A O   
1306 C CB  . PHE A 186 ? 0.9682 1.1244 0.9576 -0.2301 -0.1148 0.1020  1223 PHE A CB  
1307 C CG  . PHE A 186 ? 0.9433 1.1296 0.9620 -0.2378 -0.1063 0.1109  1223 PHE A CG  
1308 C CD1 . PHE A 186 ? 0.9366 1.1454 1.0211 -0.2557 -0.1236 0.1386  1223 PHE A CD1 
1309 C CD2 . PHE A 186 ? 0.9300 1.1248 0.9202 -0.2257 -0.0811 0.0984  1223 PHE A CD2 
1310 C CE1 . PHE A 186 ? 0.9177 1.1564 1.0287 -0.2588 -0.1125 0.1506  1223 PHE A CE1 
1311 C CE2 . PHE A 186 ? 0.9115 1.1311 0.9245 -0.2313 -0.0747 0.1050  1223 PHE A CE2 
1312 C CZ  . PHE A 186 ? 0.9058 1.1468 0.9740 -0.2465 -0.0889 0.1295  1223 PHE A CZ  
1313 N N   . GLY A 187 ? 1.1204 1.1392 0.9811 -0.1783 -0.1686 0.0681  1224 GLY A N   
1314 C CA  . GLY A 187 ? 1.1678 1.1479 0.9999 -0.1671 -0.1886 0.0626  1224 GLY A CA  
1315 C C   . GLY A 187 ? 1.1133 1.1503 0.9938 -0.1916 -0.1570 0.0773  1224 GLY A C   
1316 O O   . GLY A 187 ? 1.1301 1.1503 1.0231 -0.1999 -0.1809 0.0808  1224 GLY A O   
1317 N N   . LEU A 188 ? 1.0620 1.1581 0.9663 -0.2000 -0.1096 0.0848  1225 LEU A N   
1318 C CA  . LEU A 188 ? 1.0244 1.1631 0.9601 -0.2146 -0.0844 0.0944  1225 LEU A CA  
1319 C C   . LEU A 188 ? 1.0399 1.1709 0.9430 -0.1938 -0.0617 0.0905  1225 LEU A C   
1320 O O   . LEU A 188 ? 1.0150 1.1687 0.9382 -0.2026 -0.0485 0.0958  1225 LEU A O   
1321 C CB  . LEU A 188 ? 0.9756 1.1658 0.9478 -0.2275 -0.0598 0.1027  1225 LEU A CB  
1322 C CG  . LEU A 188 ? 0.9615 1.1801 0.9806 -0.2440 -0.0675 0.1224  1225 LEU A CG  
1323 C CD1 . LEU A 188 ? 0.9843 1.1819 1.0192 -0.2493 -0.0976 0.1272  1225 LEU A CD1 
1324 C CD2 . LEU A 188 ? 0.9335 1.1929 0.9619 -0.2402 -0.0402 0.1283  1225 LEU A CD2 
1325 N N   . ALA A 189 ? 1.0904 1.1893 0.9439 -0.1607 -0.0564 0.0864  1226 ALA A N   
1326 C CA  . ALA A 189 ? 1.1076 1.2090 0.9426 -0.1327 -0.0262 0.0979  1226 ALA A CA  
1327 C C   . ALA A 189 ? 1.1569 1.2216 0.9526 -0.1158 -0.0387 0.0942  1226 ALA A C   
1328 O O   . ALA A 189 ? 1.1696 1.2409 0.9568 -0.0921 -0.0116 0.1097  1226 ALA A O   
1329 C CB  . ALA A 189 ? 1.1460 1.2322 0.9414 -0.0921 -0.0076 0.1058  1226 ALA A CB  
1330 N N   . ARG A 190 ? 1.1896 1.2165 0.9714 -0.1277 -0.0820 0.0791  1227 ARG A N   
1331 C CA  . ARG A 190 ? 1.2445 1.2258 0.9863 -0.1115 -0.1047 0.0724  1227 ARG A CA  
1332 C C   . ARG A 190 ? 1.1920 1.2130 0.9943 -0.1502 -0.1019 0.0799  1227 ARG A C   
1333 O O   . ARG A 190 ? 1.2247 1.2157 1.0089 -0.1457 -0.1220 0.0760  1227 ARG A O   
1334 C CB  . ARG A 190 ? 1.3247 1.2284 1.0221 -0.0990 -0.1679 0.0535  1227 ARG A CB  
1335 C CG  . ARG A 190 ? 1.4391 1.2561 1.0253 -0.0360 -0.1897 0.0384  1227 ARG A CG  
1336 C CD  . ARG A 190 ? 1.4525 1.2696 1.0134 -0.0163 -0.1666 0.0452  1227 ARG A CD  
1337 N NE  . ARG A 190 ? 1.4188 1.2475 1.0377 -0.0607 -0.1930 0.0449  1227 ARG A NE  
1338 C CZ  . ARG A 190 ? 1.4177 1.2512 1.0292 -0.0548 -0.1783 0.0499  1227 ARG A CZ  
1339 N NH1 . ARG A 190 ? 1.3868 1.2321 1.0541 -0.0949 -0.2027 0.0519  1227 ARG A NH1 
1340 N NH2 . ARG A 190 ? 1.4487 1.2795 1.0035 -0.0063 -0.1361 0.0597  1227 ARG A NH2 
1341 N N   . ASN A 191 ? 1.1232 1.2049 0.9878 -0.1815 -0.0794 0.0899  1228 ASN A N   
1342 C CA  . ASN A 191 ? 1.0820 1.1982 0.9907 -0.2073 -0.0740 0.0980  1228 ASN A CA  
1343 C C   . ASN A 191 ? 1.0699 1.1989 0.9756 -0.1976 -0.0482 0.1022  1228 ASN A C   
1344 O O   . ASN A 191 ? 1.0709 1.1962 0.9787 -0.2026 -0.0529 0.1034  1228 ASN A O   
1345 C CB  . ASN A 191 ? 1.0362 1.1989 0.9908 -0.2283 -0.0632 0.1065  1228 ASN A CB  
1346 C CG  . ASN A 191 ? 1.0436 1.2055 1.0231 -0.2401 -0.0858 0.1147  1228 ASN A CG  
1347 O OD1 . ASN A 191 ? 1.0652 1.2110 1.0667 -0.2499 -0.1151 0.1245  1228 ASN A OD1 
1348 N ND2 . ASN A 191 ? 1.0281 1.2072 1.0151 -0.2403 -0.0764 0.1151  1228 ASN A ND2 
1349 N N   . MET A 192 ? 1.0565 1.2029 0.9699 -0.1853 -0.0234 0.1095  1229 MET A N   
1350 C CA  . MET A 192 ? 1.0434 1.2063 0.9795 -0.1774 -0.0030 0.1246  1229 MET A CA  
1351 C C   . MET A 192 ? 1.0871 1.2196 0.9789 -0.1460 0.0035  0.1311  1229 MET A C   
1352 O O   . MET A 192 ? 1.0743 1.2221 0.9908 -0.1397 0.0201  0.1489  1229 MET A O   
1353 C CB  . MET A 192 ? 1.0287 1.2163 1.0027 -0.1693 0.0162  0.1428  1229 MET A CB  
1354 C CG  . MET A 192 ? 1.0638 1.2374 1.0031 -0.1385 0.0302  0.1502  1229 MET A CG  
1355 S SD  . MET A 192 ? 1.0428 1.2548 1.0494 -0.1298 0.0552  0.1844  1229 MET A SD  
1356 C CE  . MET A 192 ? 1.0171 1.2320 1.0240 -0.1552 0.0357  0.1585  1229 MET A CE  
1357 N N   . GLU A 196 ? 1.0215 1.1800 0.9715 -0.2024 -0.0189 0.1232  1233 GLU A N   
1358 C CA  . GLU A 196 ? 1.0116 1.1718 0.9658 -0.2184 -0.0308 0.1182  1233 GLU A CA  
1359 C C   . GLU A 196 ? 0.9998 1.1671 0.9741 -0.2165 -0.0235 0.1261  1233 GLU A C   
1360 O O   . GLU A 196 ? 0.9893 1.1702 0.9989 -0.2147 -0.0180 0.1361  1233 GLU A O   
1361 C CB  . GLU A 196 ? 0.9933 1.1746 0.9640 -0.2333 -0.0368 0.1155  1233 GLU A CB  
1362 C CG  . GLU A 196 ? 0.9812 1.1767 0.9686 -0.2314 -0.0338 0.1133  1233 GLU A CG  
1363 C CD  . GLU A 196 ? 0.9782 1.1775 0.9714 -0.2280 -0.0298 0.1128  1233 GLU A CD  
1364 O OE1 . GLU A 196 ? 0.9897 1.1804 0.9672 -0.2250 -0.0273 0.1131  1233 GLU A OE1 
1365 O OE2 . GLU A 196 ? 0.9723 1.1761 0.9839 -0.2261 -0.0352 0.1112  1233 GLU A OE2 
1366 N N   . TYR A 197 ? 1.0033 1.1593 0.9641 -0.2183 -0.0288 0.1246  1234 TYR A N   
1367 C CA  . TYR A 197 ? 0.9933 1.1538 0.9733 -0.2172 -0.0243 0.1327  1234 TYR A CA  
1368 C C   . TYR A 197 ? 0.9722 1.1411 0.9617 -0.2317 -0.0367 0.1248  1234 TYR A C   
1369 O O   . TYR A 197 ? 0.9654 1.1379 0.9792 -0.2325 -0.0446 0.1254  1234 TYR A O   
1370 C CB  . TYR A 197 ? 1.0257 1.1634 0.9741 -0.2014 -0.0203 0.1365  1234 TYR A CB  
1371 C CG  . TYR A 197 ? 1.0680 1.1848 0.9794 -0.1685 -0.0074 0.1443  1234 TYR A CG  
1372 C CD1 . TYR A 197 ? 1.1204 1.1921 0.9693 -0.1506 -0.0251 0.1305  1234 TYR A CD1 
1373 C CD2 . TYR A 197 ? 1.0679 1.2048 1.0065 -0.1492 0.0180  0.1691  1234 TYR A CD2 
1374 C CE1 . TYR A 197 ? 1.1809 1.2188 0.9715 -0.1060 -0.0171 0.1344  1234 TYR A CE1 
1375 C CE2 . TYR A 197 ? 1.1177 1.2362 1.0117 -0.1060 0.0372  0.1826  1234 TYR A CE2 
1376 C CZ  . TYR A 197 ? 1.1799 1.2444 0.9876 -0.0800 0.0200  0.1618  1234 TYR A CZ  
1377 O OH  . TYR A 197 ? 1.2506 1.2827 0.9907 -0.0234 0.0353  0.1718  1234 TYR A OH  
1378 N N   . TYR A 198 ? 0.9684 1.1361 0.9407 -0.2383 -0.0425 0.1214  1235 TYR A N   
1379 C CA  . TYR A 198 ? 0.9620 1.1407 0.9346 -0.2404 -0.0458 0.1225  1235 TYR A CA  
1380 C C   . TYR A 198 ? 0.9626 1.1582 0.9334 -0.2364 -0.0425 0.1273  1235 TYR A C   
1381 O O   . TYR A 198 ? 0.9610 1.1654 0.9437 -0.2432 -0.0428 0.1391  1235 TYR A O   
1382 C CB  . TYR A 198 ? 0.9642 1.1390 0.9353 -0.2463 -0.0493 0.1297  1235 TYR A CB  
1383 C CG  . TYR A 198 ? 0.9671 1.1237 0.9322 -0.2448 -0.0504 0.1263  1235 TYR A CG  
1384 C CD1 . TYR A 198 ? 0.9822 1.1170 0.9307 -0.2361 -0.0505 0.1250  1235 TYR A CD1 
1385 C CD2 . TYR A 198 ? 0.9636 1.1212 0.9319 -0.2444 -0.0508 0.1265  1235 TYR A CD2 
1386 C CE1 . TYR A 198 ? 0.9958 1.1152 0.9319 -0.2242 -0.0454 0.1281  1235 TYR A CE1 
1387 C CE2 . TYR A 198 ? 0.9673 1.1123 0.9353 -0.2414 -0.0491 0.1283  1235 TYR A CE2 
1388 C CZ  . TYR A 198 ? 0.9833 1.1116 0.9357 -0.2299 -0.0436 0.1312  1235 TYR A CZ  
1389 O OH  . TYR A 198 ? 0.9971 1.1141 0.9426 -0.2168 -0.0360 0.1389  1235 TYR A OH  
1390 N N   . SER A 199 ? 0.9743 1.1694 0.9320 -0.2219 -0.0448 0.1201  1236 SER A N   
1391 C CA  . SER A 199 ? 0.9872 1.1955 0.9311 -0.2068 -0.0381 0.1257  1236 SER A CA  
1392 C C   . SER A 199 ? 1.0238 1.2374 0.9369 -0.1782 -0.0309 0.1364  1236 SER A C   
1393 O O   . SER A 199 ? 1.0408 1.2367 0.9355 -0.1693 -0.0399 0.1286  1236 SER A O   
1394 C CB  . SER A 199 ? 0.9912 1.1851 0.9288 -0.2001 -0.0496 0.1099  1236 SER A CB  
1395 O OG  . SER A 199 ? 0.9635 1.1595 0.9285 -0.2185 -0.0477 0.1090  1236 SER A OG  
1396 N N   . VAL A 200 ? 1.0436 1.2821 0.9504 -0.1582 -0.0124 0.1587  1237 VAL A N   
1397 C CA  . VAL A 200 ? 1.0915 1.3421 0.9634 -0.1159 0.0061  0.1818  1237 VAL A CA  
1398 C C   . VAL A 200 ? 1.1454 1.3805 0.9572 -0.0702 0.0076  0.1745  1237 VAL A C   
1399 O O   . VAL A 200 ? 1.1487 1.4143 0.9725 -0.0585 0.0293  0.1998  1237 VAL A O   
1400 C CB  . VAL A 200 ? 1.0753 1.3768 1.0049 -0.1221 0.0323  0.2332  1237 VAL A CB  
1401 C CG1 . VAL A 200 ? 1.0438 1.3709 1.0309 -0.1468 0.0340  0.2517  1237 VAL A CG1 
1402 C CG2 . VAL A 200 ? 1.1263 1.4529 1.0255 -0.0663 0.0645  0.2732  1237 VAL A CG2 
1403 N N   . HIS A 201 ? 1.1968 1.3779 0.9452 -0.0427 -0.0220 0.1400  1238 HIS A N   
1404 C CA  . HIS A 201 ? 1.2672 1.4100 0.9410 0.0082  -0.0369 0.1235  1238 HIS A CA  
1405 C C   . HIS A 201 ? 1.2309 1.3841 0.9373 -0.0158 -0.0399 0.1168  1238 HIS A C   
1406 O O   . HIS A 201 ? 1.2864 1.4065 0.9339 0.0244  -0.0548 0.1023  1238 HIS A O   
1407 C CB  . HIS A 201 ? 1.3372 1.4954 0.9445 0.0787  -0.0003 0.1579  1238 HIS A CB  
1408 C CG  . HIS A 201 ? 1.3788 1.5302 0.9496 0.1103  0.0085  0.1703  1238 HIS A CG  
1409 N ND1 . HIS A 201 ? 1.4388 1.5205 0.9449 0.1331  -0.0353 0.1313  1238 HIS A ND1 
1410 C CD2 . HIS A 201 ? 1.3698 1.5778 0.9700 0.1224  0.0551  0.2232  1238 HIS A CD2 
1411 C CE1 . HIS A 201 ? 1.4653 1.5588 0.9484 0.1609  -0.0129 0.1546  1238 HIS A CE1 
1412 N NE2 . HIS A 201 ? 1.4216 1.5963 0.9654 0.1547  0.0455  0.2140  1238 HIS A NE2 
1413 N N   . ALA A 206 ? 0.9010 0.8908 0.7709 0.0359  0.2676  0.2355  1243 ALA A N   
1414 C CA  . ALA A 206 ? 0.9518 0.9078 0.7310 0.0932  0.2682  0.2398  1243 ALA A CA  
1415 C C   . ALA A 206 ? 0.9097 0.8551 0.6493 0.1106  0.2178  0.1831  1243 ALA A C   
1416 O O   . ALA A 206 ? 0.9211 0.8237 0.6325 0.1182  0.1985  0.1676  1243 ALA A O   
1417 C CB  . ALA A 206 ? 1.0059 0.9985 0.7380 0.1482  0.3039  0.2766  1243 ALA A CB  
1418 N N   . LYS A 207 ? 0.8653 0.8509 0.6094 0.1167  0.1978  0.1547  1244 LYS A N   
1419 C CA  . LYS A 207 ? 0.8332 0.8115 0.5523 0.1321  0.1524  0.1060  1244 LYS A CA  
1420 C C   . LYS A 207 ? 0.7725 0.7338 0.5403 0.0846  0.1276  0.0799  1244 LYS A C   
1421 O O   . LYS A 207 ? 0.7430 0.7151 0.5652 0.0420  0.1358  0.0855  1244 LYS A O   
1422 C CB  . LYS A 207 ? 0.8196 0.8367 0.5325 0.1523  0.1405  0.0871  1244 LYS A CB  
1423 C CG  . LYS A 207 ? 0.8860 0.9115 0.5240 0.2207  0.1441  0.0904  1244 LYS A CG  
1424 C CD  . LYS A 207 ? 0.9474 0.9904 0.5615 0.2466  0.1963  0.1448  1244 LYS A CD  
1425 C CE  . LYS A 207 ? 1.0230 1.0768 0.5479 0.3273  0.1995  0.1464  1244 LYS A CE  
1426 N NZ  . LYS A 207 ? 1.0924 1.1658 0.5921 0.3575  0.2589  0.2097  1244 LYS A NZ  
1427 N N   . LEU A 208 ? 0.7588 0.6982 0.5073 0.0969  0.0963  0.0511  1245 LEU A N   
1428 C CA  . LEU A 208 ? 0.7040 0.6376 0.4925 0.0640  0.0733  0.0265  1245 LEU A CA  
1429 C C   . LEU A 208 ? 0.6584 0.6201 0.4704 0.0588  0.0524  0.0023  1245 LEU A C   
1430 O O   . LEU A 208 ? 0.6736 0.6422 0.4610 0.0897  0.0368  -0.0116 1245 LEU A O   
1431 C CB  . LEU A 208 ? 0.7189 0.6269 0.4858 0.0822  0.0529  0.0120  1245 LEU A CB  
1432 C CG  . LEU A 208 ? 0.7700 0.6405 0.5084 0.0916  0.0710  0.0348  1245 LEU A CG  
1433 C CD1 . LEU A 208 ? 0.7767 0.6316 0.5012 0.1100  0.0471  0.0161  1245 LEU A CD1 
1434 C CD2 . LEU A 208 ? 0.7686 0.6210 0.5423 0.0506  0.0916  0.0521  1245 LEU A CD2 
1435 N N   . PRO A 209 ? 0.6096 0.5837 0.4659 0.0242  0.0495  -0.0042 1246 PRO A N   
1436 C CA  . PRO A 209 ? 0.5755 0.5698 0.4534 0.0210  0.0326  -0.0217 1246 PRO A CA  
1437 C C   . PRO A 209 ? 0.5604 0.5438 0.4509 0.0245  0.0067  -0.0415 1246 PRO A C   
1438 O O   . PRO A 209 ? 0.5355 0.5241 0.4584 0.0044  0.0030  -0.0446 1246 PRO A O   
1439 C CB  . PRO A 209 ? 0.5464 0.5576 0.4598 -0.0112 0.0424  -0.0164 1246 PRO A CB  
1440 C CG  . PRO A 209 ? 0.5552 0.5424 0.4715 -0.0272 0.0481  -0.0112 1246 PRO A CG  
1441 C CD  . PRO A 209 ? 0.5977 0.5626 0.4808 -0.0080 0.0598  0.0035  1246 PRO A CD  
1442 N N   . VAL A 210 ? 0.5830 0.5554 0.4502 0.0534  -0.0115 -0.0541 1247 VAL A N   
1443 C CA  . VAL A 210 ? 0.5748 0.5419 0.4657 0.0561  -0.0377 -0.0718 1247 VAL A CA  
1444 C C   . VAL A 210 ? 0.5463 0.5220 0.4852 0.0418  -0.0545 -0.0835 1247 VAL A C   
1445 O O   . VAL A 210 ? 0.5271 0.5086 0.5114 0.0281  -0.0643 -0.0862 1247 VAL A O   
1446 C CB  . VAL A 210 ? 0.6218 0.5778 0.4764 0.0949  -0.0598 -0.0875 1247 VAL A CB  
1447 C CG1 . VAL A 210 ? 0.6564 0.5990 0.4598 0.1134  -0.0381 -0.0683 1247 VAL A CG1 
1448 C CG2 . VAL A 210 ? 0.6546 0.6085 0.4848 0.1236  -0.0786 -0.1056 1247 VAL A CG2 
1449 N N   . LYS A 211 ? 0.5476 0.5246 0.4781 0.0475  -0.0549 -0.0865 1248 LYS A N   
1450 C CA  . LYS A 211 ? 0.5372 0.5113 0.5078 0.0386  -0.0707 -0.0956 1248 LYS A CA  
1451 C C   . LYS A 211 ? 0.4975 0.4866 0.4966 0.0113  -0.0484 -0.0756 1248 LYS A C   
1452 O O   . LYS A 211 ? 0.4902 0.4764 0.5281 0.0014  -0.0544 -0.0735 1248 LYS A O   
1453 C CB  . LYS A 211 ? 0.5727 0.5363 0.5122 0.0658  -0.0834 -0.1101 1248 LYS A CB  
1454 C CG  . LYS A 211 ? 0.6263 0.5745 0.5254 0.1044  -0.1096 -0.1342 1248 LYS A CG  
1455 C CD  . LYS A 211 ? 0.6734 0.6042 0.5444 0.1381  -0.1326 -0.1575 1248 LYS A CD  
1456 C CE  . LYS A 211 ? 0.7369 0.6511 0.5611 0.1849  -0.1659 -0.1879 1248 LYS A CE  
1457 N NZ  . LYS A 211 ? 0.7958 0.6861 0.5892 0.2234  -0.1951 -0.2177 1248 LYS A NZ  
1458 N N   . TRP A 212 ? 0.4792 0.4816 0.4592 0.0018  -0.0243 -0.0610 1249 TRP A N   
1459 C CA  . TRP A 212 ? 0.4506 0.4681 0.4480 -0.0166 -0.0087 -0.0481 1249 TRP A CA  
1460 C C   . TRP A 212 ? 0.4422 0.4597 0.4501 -0.0254 -0.0031 -0.0427 1249 TRP A C   
1461 O O   . TRP A 212 ? 0.4327 0.4616 0.4526 -0.0324 0.0063  -0.0340 1249 TRP A O   
1462 C CB  . TRP A 212 ? 0.4462 0.4801 0.4241 -0.0206 0.0067  -0.0420 1249 TRP A CB  
1463 C CG  . TRP A 212 ? 0.4519 0.4975 0.4240 -0.0088 0.0054  -0.0437 1249 TRP A CG  
1464 C CD1 . TRP A 212 ? 0.4410 0.5043 0.4236 -0.0103 0.0086  -0.0399 1249 TRP A CD1 
1465 C CD2 . TRP A 212 ? 0.4782 0.5201 0.4252 0.0142  0.0008  -0.0497 1249 TRP A CD2 
1466 N NE1 . TRP A 212 ? 0.4563 0.5267 0.4261 0.0081  0.0063  -0.0433 1249 TRP A NE1 
1467 C CE2 . TRP A 212 ? 0.4799 0.5377 0.4262 0.0246  0.0019  -0.0497 1249 TRP A CE2 
1468 C CE3 . TRP A 212 ? 0.5074 0.5351 0.4252 0.0345  -0.0044 -0.0554 1249 TRP A CE3 
1469 C CZ2 . TRP A 212 ? 0.5095 0.5695 0.4275 0.0548  -0.0012 -0.0558 1249 TRP A CZ2 
1470 C CZ3 . TRP A 212 ? 0.5395 0.5694 0.4251 0.0664  -0.0078 -0.0614 1249 TRP A CZ3 
1471 C CH2 . TRP A 212 ? 0.5407 0.5867 0.4267 0.0765  -0.0058 -0.0619 1249 TRP A CH2 
1472 N N   . MET A 213 ? 0.4546 0.4602 0.4511 -0.0180 -0.0091 -0.0480 1250 MET A N   
1473 C CA  . MET A 213 ? 0.4533 0.4572 0.4510 -0.0196 -0.0035 -0.0440 1250 MET A CA  
1474 C C   . MET A 213 ? 0.4391 0.4595 0.4826 -0.0208 -0.0083 -0.0398 1250 MET A C   
1475 O O   . MET A 213 ? 0.4368 0.4607 0.5155 -0.0213 -0.0232 -0.0442 1250 MET A O   
1476 C CB  . MET A 213 ? 0.4776 0.4633 0.4465 -0.0053 -0.0084 -0.0487 1250 MET A CB  
1477 C CG  . MET A 213 ? 0.4959 0.4625 0.4296 -0.0087 0.0075  -0.0409 1250 MET A CG  
1478 S SD  . MET A 213 ? 0.5387 0.4803 0.4291 0.0157  0.0078  -0.0373 1250 MET A SD  
1479 C CE  . MET A 213 ? 0.5556 0.4813 0.4413 0.0254  0.0039  -0.0391 1250 MET A CE  
1480 N N   . ALA A 214 ? 0.4351 0.4653 0.4808 -0.0197 0.0044  -0.0306 1251 ALA A N   
1481 C CA  . ALA A 214 ? 0.4261 0.4822 0.5189 -0.0177 0.0089  -0.0179 1251 ALA A CA  
1482 C C   . ALA A 214 ? 0.4309 0.4940 0.5484 -0.0099 -0.0061 -0.0254 1251 ALA A C   
1483 O O   . ALA A 214 ? 0.4432 0.4861 0.5246 -0.0002 -0.0169 -0.0393 1251 ALA A O   
1484 C CB  . ALA A 214 ? 0.4307 0.4982 0.5051 -0.0083 0.0290  -0.0062 1251 ALA A CB  
1485 N N   . LEU A 215 ? 0.4239 0.5192 0.6067 -0.0121 -0.0053 -0.0130 1252 LEU A N   
1486 C CA  . LEU A 215 ? 0.4300 0.5440 0.6561 -0.0063 -0.0253 -0.0221 1252 LEU A CA  
1487 C C   . LEU A 215 ? 0.4446 0.5576 0.6268 0.0156  -0.0204 -0.0261 1252 LEU A C   
1488 O O   . LEU A 215 ? 0.4624 0.5658 0.6280 0.0291  -0.0409 -0.0435 1252 LEU A O   
1489 C CB  . LEU A 215 ? 0.4212 0.5787 0.7432 -0.0177 -0.0193 -0.0006 1252 LEU A CB  
1490 C CG  . LEU A 215 ? 0.4288 0.6042 0.8306 -0.0257 -0.0538 -0.0161 1252 LEU A CG  
1491 C CD1 . LEU A 215 ? 0.4231 0.6518 0.9342 -0.0388 -0.0403 0.0135  1252 LEU A CD1 
1492 C CD2 . LEU A 215 ? 0.4437 0.6190 0.8135 -0.0032 -0.0785 -0.0426 1252 LEU A CD2 
1493 N N   . GLU A 216 ? 0.4469 0.5659 0.6040 0.0247  0.0053  -0.0110 1253 GLU A N   
1494 C CA  . GLU A 216 ? 0.4688 0.5791 0.5820 0.0490  0.0100  -0.0151 1253 GLU A CA  
1495 C C   . GLU A 216 ? 0.4889 0.5427 0.5279 0.0512  0.0038  -0.0308 1253 GLU A C   
1496 O O   . GLU A 216 ? 0.5169 0.5501 0.5217 0.0704  -0.0011 -0.0374 1253 GLU A O   
1497 C CB  . GLU A 216 ? 0.4795 0.6089 0.5819 0.0652  0.0359  0.0015  1253 GLU A CB  
1498 C CG  . GLU A 216 ? 0.4875 0.5895 0.5404 0.0611  0.0473  0.0008  1253 GLU A CG  
1499 C CD  . GLU A 216 ? 0.4657 0.5879 0.5521 0.0446  0.0570  0.0165  1253 GLU A CD  
1500 O OE1 . GLU A 216 ? 0.4459 0.5951 0.5996 0.0304  0.0546  0.0287  1253 GLU A OE1 
1501 O OE2 . GLU A 216 ? 0.4750 0.5836 0.5218 0.0473  0.0644  0.0152  1253 GLU A OE2 
1502 N N   . SER A 217 ? 0.4798 0.5109 0.4989 0.0327  0.0061  -0.0329 1254 SER A N   
1503 C CA  . SER A 217 ? 0.5015 0.4873 0.4672 0.0299  0.0053  -0.0404 1254 SER A CA  
1504 C C   . SER A 217 ? 0.5136 0.4877 0.4682 0.0389  -0.0094 -0.0472 1254 SER A C   
1505 O O   . SER A 217 ? 0.5429 0.4815 0.4525 0.0486  -0.0062 -0.0462 1254 SER A O   
1506 C CB  . SER A 217 ? 0.4900 0.4696 0.4499 0.0097  0.0118  -0.0394 1254 SER A CB  
1507 O OG  . SER A 217 ? 0.4942 0.4780 0.4468 0.0102  0.0216  -0.0377 1254 SER A OG  
1508 N N   . LEU A 218 ? 0.4977 0.4993 0.4935 0.0386  -0.0264 -0.0537 1255 LEU A N   
1509 C CA  . LEU A 218 ? 0.5221 0.5162 0.5030 0.0564  -0.0478 -0.0668 1255 LEU A CA  
1510 C C   . LEU A 218 ? 0.5508 0.5487 0.5222 0.0837  -0.0581 -0.0715 1255 LEU A C   
1511 O O   . LEU A 218 ? 0.5909 0.5733 0.5243 0.1092  -0.0717 -0.0800 1255 LEU A O   
1512 C CB  . LEU A 218 ? 0.5062 0.5236 0.5400 0.0486  -0.0710 -0.0795 1255 LEU A CB  
1513 C CG  . LEU A 218 ? 0.4928 0.4997 0.5221 0.0328  -0.0661 -0.0785 1255 LEU A CG  
1514 C CD1 . LEU A 218 ? 0.4872 0.5070 0.5744 0.0256  -0.0918 -0.0919 1255 LEU A CD1 
1515 C CD2 . LEU A 218 ? 0.5211 0.5010 0.4844 0.0489  -0.0619 -0.0805 1255 LEU A CD2 
1516 N N   . GLN A 219 ? 0.5390 0.5606 0.5405 0.0846  -0.0505 -0.0647 1256 GLN A N   
1517 C CA  . GLN A 219 ? 0.5624 0.5979 0.5636 0.1134  -0.0605 -0.0689 1256 GLN A CA  
1518 C C   . GLN A 219 ? 0.5975 0.5905 0.5336 0.1308  -0.0414 -0.0599 1256 GLN A C   
1519 O O   . GLN A 219 ? 0.6348 0.6143 0.5377 0.1619  -0.0492 -0.0629 1256 GLN A O   
1520 C CB  . GLN A 219 ? 0.5356 0.6321 0.6187 0.1088  -0.0628 -0.0642 1256 GLN A CB  
1521 C CG  . GLN A 219 ? 0.5107 0.6433 0.6746 0.0881  -0.0849 -0.0723 1256 GLN A CG  
1522 C CD  . GLN A 219 ? 0.4879 0.6843 0.7480 0.0795  -0.0804 -0.0584 1256 GLN A CD  
1523 O OE1 . GLN A 219 ? 0.4623 0.6762 0.7687 0.0560  -0.0614 -0.0389 1256 GLN A OE1 
1524 N NE2 . GLN A 219 ? 0.5026 0.7381 0.7950 0.1018  -0.0953 -0.0644 1256 GLN A NE2 
1525 N N   . THR A 220 ? 0.5923 0.5619 0.5108 0.1136  -0.0200 -0.0510 1257 THR A N   
1526 C CA  . THR A 220 ? 0.6320 0.5579 0.5005 0.1285  -0.0071 -0.0474 1257 THR A CA  
1527 C C   . THR A 220 ? 0.6552 0.5212 0.4808 0.1107  0.0031  -0.0436 1257 THR A C   
1528 O O   . THR A 220 ? 0.7027 0.5158 0.4864 0.1217  0.0090  -0.0414 1257 THR A O   
1529 C CB  . THR A 220 ? 0.6223 0.5740 0.5090 0.1325  0.0039  -0.0451 1257 THR A CB  
1530 O OG1 . THR A 220 ? 0.5911 0.5511 0.4943 0.1048  0.0120  -0.0427 1257 THR A OG1 
1531 C CG2 . THR A 220 ? 0.6014 0.6218 0.5449 0.1487  0.0005  -0.0407 1257 THR A CG2 
1532 N N   . GLN A 221 ? 0.6249 0.4996 0.4674 0.0835  0.0049  -0.0420 1258 GLN A N   
1533 C CA  . GLN A 221 ? 0.6381 0.4751 0.4626 0.0606  0.0159  -0.0369 1258 GLN A CA  
1534 C C   . GLN A 221 ? 0.6518 0.4681 0.4705 0.0539  0.0190  -0.0442 1258 GLN A C   
1535 O O   . GLN A 221 ? 0.6907 0.4560 0.4890 0.0448  0.0224  -0.0439 1258 GLN A O   
1536 C CB  . GLN A 221 ? 0.6897 0.4785 0.4752 0.0698  0.0237  -0.0237 1258 GLN A CB  
1537 C CG  . GLN A 221 ? 0.6886 0.4966 0.4658 0.0840  0.0200  -0.0184 1258 GLN A CG  
1538 C CD  . GLN A 221 ? 0.7445 0.5092 0.4802 0.0947  0.0371  0.0038  1258 GLN A CD  
1539 O OE1 . GLN A 221 ? 0.7840 0.4994 0.5065 0.0861  0.0518  0.0175  1258 GLN A OE1 
1540 N NE2 . GLN A 221 ? 0.7555 0.5363 0.4707 0.1165  0.0353  0.0087  1258 GLN A NE2 
1541 N N   . LYS A 222 ? 0.6269 0.4825 0.4655 0.0607  0.0173  -0.0503 1259 LYS A N   
1542 C CA  . LYS A 222 ? 0.6483 0.4923 0.4728 0.0645  0.0177  -0.0607 1259 LYS A CA  
1543 C C   . LYS A 222 ? 0.6080 0.4906 0.4587 0.0466  0.0196  -0.0610 1259 LYS A C   
1544 O O   . LYS A 222 ? 0.5646 0.4955 0.4490 0.0458  0.0242  -0.0509 1259 LYS A O   
1545 C CB  . LYS A 222 ? 0.6705 0.5300 0.4831 0.1006  0.0197  -0.0625 1259 LYS A CB  
1546 C CG  . LYS A 222 ? 0.7252 0.5396 0.5020 0.1257  0.0163  -0.0647 1259 LYS A CG  
1547 C CD  . LYS A 222 ? 0.7572 0.5834 0.5143 0.1669  0.0186  -0.0694 1259 LYS A CD  
1548 C CE  . LYS A 222 ? 0.8237 0.5923 0.5357 0.1956  0.0136  -0.0740 1259 LYS A CE  
1549 N NZ  . LYS A 222 ? 0.8637 0.6416 0.5490 0.2418  0.0158  -0.0811 1259 LYS A NZ  
1550 N N   . PHE A 223 ? 0.6285 0.4872 0.4674 0.0329  0.0138  -0.0732 1260 PHE A N   
1551 C CA  . PHE A 223 ? 0.6003 0.4919 0.4581 0.0185  0.0132  -0.0749 1260 PHE A CA  
1552 C C   . PHE A 223 ? 0.6296 0.5234 0.4618 0.0401  0.0069  -0.0905 1260 PHE A C   
1553 O O   . PHE A 223 ? 0.6843 0.5346 0.4855 0.0520  -0.0053 -0.1097 1260 PHE A O   
1554 C CB  . PHE A 223 ? 0.6003 0.4763 0.4730 -0.0130 0.0091  -0.0767 1260 PHE A CB  
1555 C CG  . PHE A 223 ? 0.5893 0.4615 0.4728 -0.0236 0.0174  -0.0604 1260 PHE A CG  
1556 C CD1 . PHE A 223 ? 0.6258 0.4563 0.4898 -0.0172 0.0205  -0.0545 1260 PHE A CD1 
1557 C CD2 . PHE A 223 ? 0.5524 0.4600 0.4580 -0.0327 0.0215  -0.0514 1260 PHE A CD2 
1558 C CE1 . PHE A 223 ? 0.6240 0.4531 0.4863 -0.0165 0.0285  -0.0389 1260 PHE A CE1 
1559 C CE2 . PHE A 223 ? 0.5512 0.4552 0.4553 -0.0322 0.0265  -0.0402 1260 PHE A CE2 
1560 C CZ  . PHE A 223 ? 0.5880 0.4553 0.4683 -0.0224 0.0305  -0.0335 1260 PHE A CZ  
1561 N N   . THR A 224 ? 0.6032 0.5441 0.4449 0.0496  0.0145  -0.0820 1261 THR A N   
1562 C CA  . THR A 224 ? 0.6365 0.5888 0.4452 0.0801  0.0110  -0.0932 1261 THR A CA  
1563 C C   . THR A 224 ? 0.6118 0.5974 0.4335 0.0718  0.0109  -0.0896 1261 THR A C   
1564 O O   . THR A 224 ? 0.5717 0.5655 0.4272 0.0411  0.0117  -0.0817 1261 THR A O   
1565 C CB  . THR A 224 ? 0.6465 0.6292 0.4440 0.1191  0.0306  -0.0753 1261 THR A CB  
1566 O OG1 . THR A 224 ? 0.5966 0.6276 0.4420 0.1095  0.0512  -0.0433 1261 THR A OG1 
1567 C CG2 . THR A 224 ? 0.6691 0.6255 0.4553 0.1318  0.0305  -0.0782 1261 THR A CG2 
1568 N N   . THR A 225 ? 0.6446 0.6494 0.4320 0.1064  0.0098  -0.0953 1262 THR A N   
1569 C CA  . THR A 225 ? 0.6320 0.6721 0.4235 0.1103  0.0129  -0.0869 1262 THR A CA  
1570 C C   . THR A 225 ? 0.5863 0.6617 0.4166 0.1054  0.0424  -0.0457 1262 THR A C   
1571 O O   . THR A 225 ? 0.5595 0.6520 0.4111 0.0923  0.0455  -0.0345 1262 THR A O   
1572 C CB  . THR A 225 ? 0.6946 0.7458 0.4283 0.1600  0.0048  -0.1021 1262 THR A CB  
1573 O OG1 . THR A 225 ? 0.7477 0.7565 0.4530 0.1622  -0.0300 -0.1469 1262 THR A OG1 
1574 C CG2 . THR A 225 ? 0.6929 0.7778 0.4216 0.1703  0.0044  -0.0962 1262 THR A CG2 
1575 N N   . LYS A 226 ? 0.5814 0.6670 0.4260 0.1165  0.0618  -0.0245 1263 LYS A N   
1576 C CA  . LYS A 226 ? 0.5476 0.6654 0.4452 0.1087  0.0861  0.0133  1263 LYS A CA  
1577 C C   . LYS A 226 ? 0.5010 0.6040 0.4458 0.0662  0.0755  0.0107  1263 LYS A C   
1578 O O   . LYS A 226 ? 0.4753 0.5939 0.4655 0.0526  0.0842  0.0320  1263 LYS A O   
1579 C CB  . LYS A 226 ? 0.5631 0.7057 0.4727 0.1340  0.1075  0.0350  1263 LYS A CB  
1580 C CG  . LYS A 226 ? 0.6189 0.7833 0.4759 0.1881  0.1241  0.0434  1263 LYS A CG  
1581 C CD  . LYS A 226 ? 0.6337 0.8296 0.4868 0.2090  0.1464  0.0741  1263 LYS A CD  
1582 C CE  . LYS A 226 ? 0.6989 0.9225 0.4924 0.2740  0.1679  0.0881  1263 LYS A CE  
1583 N NZ  . LYS A 226 ? 0.7227 0.9745 0.5046 0.2999  0.1923  0.1227  1263 LYS A NZ  
1584 N N   . SER A 227 ? 0.4986 0.5681 0.4305 0.0493  0.0568  -0.0144 1264 SER A N   
1585 C CA  . SER A 227 ? 0.4691 0.5245 0.4292 0.0196  0.0472  -0.0180 1264 SER A CA  
1586 C C   . SER A 227 ? 0.4565 0.5115 0.4164 0.0038  0.0402  -0.0239 1264 SER A C   
1587 O O   . SER A 227 ? 0.4378 0.4931 0.4223 -0.0114 0.0373  -0.0198 1264 SER A O   
1588 C CB  . SER A 227 ? 0.4827 0.5043 0.4251 0.0138  0.0366  -0.0339 1264 SER A CB  
1589 O OG  . SER A 227 ? 0.5102 0.5041 0.4210 0.0093  0.0261  -0.0533 1264 SER A OG  
1590 N N   . ASP A 228 ? 0.4755 0.5317 0.4066 0.0119  0.0343  -0.0366 1265 ASP A N   
1591 C CA  . ASP A 228 ? 0.4667 0.5340 0.4009 0.0021  0.0271  -0.0424 1265 ASP A CA  
1592 C C   . ASP A 228 ? 0.4553 0.5474 0.4018 0.0142  0.0397  -0.0202 1265 ASP A C   
1593 O O   . ASP A 228 ? 0.4384 0.5379 0.3968 0.0058  0.0367  -0.0185 1265 ASP A O   
1594 C CB  . ASP A 228 ? 0.5004 0.5661 0.4080 0.0090  0.0104  -0.0672 1265 ASP A CB  
1595 C CG  . ASP A 228 ? 0.5195 0.5528 0.4290 -0.0113 -0.0039 -0.0877 1265 ASP A CG  
1596 O OD1 . ASP A 228 ? 0.5089 0.5225 0.4317 -0.0270 0.0030  -0.0790 1265 ASP A OD1 
1597 O OD2 . ASP A 228 ? 0.5521 0.5782 0.4511 -0.0098 -0.0237 -0.1124 1265 ASP A OD2 
1598 N N   . VAL A 229 ? 0.4700 0.5749 0.4143 0.0368  0.0563  0.0000  1266 VAL A N   
1599 C CA  . VAL A 229 ? 0.4725 0.5956 0.4355 0.0484  0.0743  0.0305  1266 VAL A CA  
1600 C C   . VAL A 229 ? 0.4453 0.5573 0.4602 0.0228  0.0736  0.0410  1266 VAL A C   
1601 O O   . VAL A 229 ? 0.4451 0.5549 0.4737 0.0205  0.0746  0.0511  1266 VAL A O   
1602 C CB  . VAL A 229 ? 0.4993 0.6432 0.4560 0.0793  0.0990  0.0578  1266 VAL A CB  
1603 C CG1 . VAL A 229 ? 0.5049 0.6633 0.5003 0.0848  0.1242  0.1005  1266 VAL A CG1 
1604 C CG2 . VAL A 229 ? 0.5411 0.6941 0.4326 0.1171  0.0956  0.0434  1266 VAL A CG2 
1605 N N   . TRP A 230 ? 0.4303 0.5329 0.4702 0.0083  0.0682  0.0355  1267 TRP A N   
1606 C CA  . TRP A 230 ? 0.4146 0.5044 0.4989 -0.0111 0.0579  0.0353  1267 TRP A CA  
1607 C C   . TRP A 230 ? 0.4047 0.4786 0.4713 -0.0199 0.0424  0.0167  1267 TRP A C   
1608 O O   . TRP A 230 ? 0.4053 0.4696 0.4941 -0.0234 0.0372  0.0210  1267 TRP A O   
1609 C CB  . TRP A 230 ? 0.4113 0.4974 0.5122 -0.0173 0.0492  0.0255  1267 TRP A CB  
1610 C CG  . TRP A 230 ? 0.4093 0.4844 0.5540 -0.0308 0.0312  0.0188  1267 TRP A CG  
1611 C CD1 . TRP A 230 ? 0.4110 0.4641 0.5423 -0.0359 0.0120  -0.0009 1267 TRP A CD1 
1612 C CD2 . TRP A 230 ? 0.4124 0.5007 0.6240 -0.0369 0.0273  0.0292  1267 TRP A CD2 
1613 N NE1 . TRP A 230 ? 0.4185 0.4639 0.5939 -0.0410 -0.0079 -0.0088 1267 TRP A NE1 
1614 C CE2 . TRP A 230 ? 0.4173 0.4844 0.6497 -0.0456 -0.0012 0.0082  1267 TRP A CE2 
1615 C CE3 . TRP A 230 ? 0.4156 0.5360 0.6753 -0.0337 0.0449  0.0545  1267 TRP A CE3 
1616 C CZ2 . TRP A 230 ? 0.4250 0.4988 0.7301 -0.0548 -0.0196 0.0059  1267 TRP A CZ2 
1617 C CZ3 . TRP A 230 ? 0.4170 0.5513 0.7581 -0.0465 0.0326  0.0589  1267 TRP A CZ3 
1618 C CH2 . TRP A 230 ? 0.4220 0.5315 0.7881 -0.0588 -0.0026 0.0321  1267 TRP A CH2 
1619 N N   . SER A 231 ? 0.4007 0.4715 0.4313 -0.0222 0.0358  -0.0022 1268 SER A N   
1620 C CA  . SER A 231 ? 0.3950 0.4623 0.4130 -0.0283 0.0269  -0.0149 1268 SER A CA  
1621 C C   . SER A 231 ? 0.3992 0.4812 0.4136 -0.0193 0.0296  -0.0087 1268 SER A C   
1622 O O   . SER A 231 ? 0.3988 0.4786 0.4154 -0.0182 0.0240  -0.0120 1268 SER A O   
1623 C CB  . SER A 231 ? 0.3973 0.4626 0.3932 -0.0357 0.0241  -0.0287 1268 SER A CB  
1624 O OG  . SER A 231 ? 0.4016 0.4476 0.3944 -0.0389 0.0227  -0.0318 1268 SER A OG  
1625 N N   . PHE A 232 ? 0.4097 0.5069 0.4115 -0.0060 0.0378  -0.0001 1269 PHE A N   
1626 C CA  . PHE A 232 ? 0.4205 0.5329 0.4114 0.0103  0.0407  0.0075  1269 PHE A CA  
1627 C C   . PHE A 232 ? 0.4294 0.5252 0.4458 0.0140  0.0475  0.0288  1269 PHE A C   
1628 O O   . PHE A 232 ? 0.4414 0.5363 0.4529 0.0229  0.0441  0.0299  1269 PHE A O   
1629 C CB  . PHE A 232 ? 0.4434 0.5741 0.4056 0.0337  0.0474  0.0126  1269 PHE A CB  
1630 C CG  . PHE A 232 ? 0.4665 0.6139 0.4100 0.0596  0.0513  0.0240  1269 PHE A CG  
1631 C CD1 . PHE A 232 ? 0.4662 0.6338 0.3987 0.0628  0.0356  0.0051  1269 PHE A CD1 
1632 C CD2 . PHE A 232 ? 0.4931 0.6389 0.4339 0.0830  0.0729  0.0577  1269 PHE A CD2 
1633 C CE1 . PHE A 232 ? 0.4922 0.6771 0.4036 0.0925  0.0372  0.0148  1269 PHE A CE1 
1634 C CE2 . PHE A 232 ? 0.5241 0.6810 0.4403 0.1129  0.0784  0.0720  1269 PHE A CE2 
1635 C CZ  . PHE A 232 ? 0.5236 0.6994 0.4214 0.1193  0.0586  0.0483  1269 PHE A CZ  
1636 N N   . GLY A 233 ? 0.4299 0.5127 0.4792 0.0076  0.0558  0.0455  1270 GLY A N   
1637 C CA  . GLY A 233 ? 0.4416 0.5013 0.5333 0.0036  0.0578  0.0640  1270 GLY A CA  
1638 C C   . GLY A 233 ? 0.4391 0.4743 0.5342 -0.0030 0.0358  0.0421  1270 GLY A C   
1639 O O   . GLY A 233 ? 0.4618 0.4757 0.5659 0.0045  0.0329  0.0495  1270 GLY A O   
1640 N N   . VAL A 234 ? 0.4191 0.4552 0.5014 -0.0117 0.0216  0.0166  1271 VAL A N   
1641 C CA  . VAL A 234 ? 0.4268 0.4454 0.4994 -0.0083 0.0028  -0.0044 1271 VAL A CA  
1642 C C   . VAL A 234 ? 0.4291 0.4645 0.4680 0.0065  0.0060  -0.0080 1271 VAL A C   
1643 O O   . VAL A 234 ? 0.4485 0.4682 0.4804 0.0202  -0.0041 -0.0155 1271 VAL A O   
1644 C CB  . VAL A 234 ? 0.4172 0.4366 0.4773 -0.0139 -0.0067 -0.0233 1271 VAL A CB  
1645 C CG1 . VAL A 234 ? 0.4360 0.4429 0.4726 0.0007  -0.0221 -0.0425 1271 VAL A CG1 
1646 C CG2 . VAL A 234 ? 0.4156 0.4256 0.5115 -0.0244 -0.0133 -0.0223 1271 VAL A CG2 
1647 N N   . LEU A 235 ? 0.4130 0.4818 0.4333 0.0063  0.0167  -0.0054 1272 LEU A N   
1648 C CA  . LEU A 235 ? 0.4138 0.5119 0.4141 0.0187  0.0173  -0.0101 1272 LEU A CA  
1649 C C   . LEU A 235 ? 0.4392 0.5283 0.4362 0.0397  0.0191  0.0029  1272 LEU A C   
1650 O O   . LEU A 235 ? 0.4498 0.5473 0.4345 0.0561  0.0143  -0.0028 1272 LEU A O   
1651 C CB  . LEU A 235 ? 0.4010 0.5325 0.3929 0.0126  0.0208  -0.0143 1272 LEU A CB  
1652 C CG  . LEU A 235 ? 0.3996 0.5733 0.3883 0.0166  0.0161  -0.0250 1272 LEU A CG  
1653 C CD1 . LEU A 235 ? 0.3947 0.5897 0.3884 0.0016  0.0111  -0.0373 1272 LEU A CD1 
1654 C CD2 . LEU A 235 ? 0.4182 0.6100 0.3953 0.0428  0.0149  -0.0190 1272 LEU A CD2 
1655 N N   . LEU A 236 ? 0.4549 0.5274 0.4631 0.0426  0.0291  0.0244  1273 LEU A N   
1656 C CA  . LEU A 236 ? 0.4918 0.5444 0.4998 0.0630  0.0351  0.0449  1273 LEU A CA  
1657 C C   . LEU A 236 ? 0.5150 0.5217 0.5407 0.0630  0.0210  0.0380  1273 LEU A C   
1658 O O   . LEU A 236 ? 0.5437 0.5359 0.5547 0.0851  0.0172  0.0398  1273 LEU A O   
1659 C CB  . LEU A 236 ? 0.5103 0.5538 0.5349 0.0646  0.0551  0.0775  1273 LEU A CB  
1660 C CG  . LEU A 236 ? 0.5108 0.5944 0.5025 0.0808  0.0676  0.0843  1273 LEU A CG  
1661 C CD1 . LEU A 236 ? 0.5379 0.6148 0.5428 0.0911  0.0938  0.1237  1273 LEU A CD1 
1662 C CD2 . LEU A 236 ? 0.5276 0.6389 0.4786 0.1101  0.0623  0.0776  1273 LEU A CD2 
1663 N N   . TRP A 237 ? 0.5096 0.4926 0.5642 0.0425  0.0097  0.0270  1274 TRP A N   
1664 C CA  . TRP A 237 ? 0.5433 0.4786 0.6151 0.0446  -0.0126 0.0117  1274 TRP A CA  
1665 C C   . TRP A 237 ? 0.5514 0.4951 0.5798 0.0673  -0.0255 -0.0140 1274 TRP A C   
1666 O O   . TRP A 237 ? 0.5937 0.4990 0.6153 0.0868  -0.0418 -0.0250 1274 TRP A O   
1667 C CB  . TRP A 237 ? 0.5368 0.4559 0.6485 0.0216  -0.0265 0.0009  1274 TRP A CB  
1668 C CG  . TRP A 237 ? 0.5804 0.4484 0.7138 0.0252  -0.0588 -0.0225 1274 TRP A CG  
1669 C CD1 . TRP A 237 ? 0.6183 0.4399 0.8136 0.0126  -0.0722 -0.0153 1274 TRP A CD1 
1670 C CD2 . TRP A 237 ? 0.5996 0.4567 0.6949 0.0452  -0.0844 -0.0589 1274 TRP A CD2 
1671 N NE1 . TRP A 237 ? 0.6614 0.4392 0.8594 0.0228  -0.1116 -0.0519 1274 TRP A NE1 
1672 C CE2 . TRP A 237 ? 0.6516 0.4512 0.7809 0.0475  -0.1189 -0.0793 1274 TRP A CE2 
1673 C CE3 . TRP A 237 ? 0.5844 0.4753 0.6228 0.0637  -0.0805 -0.0739 1274 TRP A CE3 
1674 C CZ2 . TRP A 237 ? 0.6923 0.4664 0.7864 0.0752  -0.1528 -0.1195 1274 TRP A CZ2 
1675 C CZ3 . TRP A 237 ? 0.6217 0.4925 0.6269 0.0910  -0.1056 -0.1047 1274 TRP A CZ3 
1676 C CH2 . TRP A 237 ? 0.6772 0.4898 0.7030 0.1004  -0.1431 -0.1299 1274 TRP A CH2 
1677 N N   . GLU A 238 ? 0.5182 0.5114 0.5206 0.0663  -0.0172 -0.0219 1275 GLU A N   
1678 C CA  . GLU A 238 ? 0.5260 0.5441 0.4948 0.0888  -0.0199 -0.0365 1275 GLU A CA  
1679 C C   . GLU A 238 ? 0.5468 0.5768 0.4999 0.1146  -0.0154 -0.0284 1275 GLU A C   
1680 O O   . GLU A 238 ? 0.5807 0.5966 0.5120 0.1438  -0.0250 -0.0392 1275 GLU A O   
1681 C CB  . GLU A 238 ? 0.4897 0.5613 0.4521 0.0760  -0.0071 -0.0376 1275 GLU A CB  
1682 C CG  . GLU A 238 ? 0.4820 0.5419 0.4456 0.0618  -0.0109 -0.0463 1275 GLU A CG  
1683 C CD  . GLU A 238 ? 0.4598 0.5625 0.4203 0.0492  0.0041  -0.0426 1275 GLU A CD  
1684 O OE1 . GLU A 238 ? 0.4734 0.5846 0.4158 0.0614  0.0075  -0.0461 1275 GLU A OE1 
1685 O OE2 . GLU A 238 ? 0.4396 0.5647 0.4156 0.0298  0.0121  -0.0354 1275 GLU A OE2 
1686 N N   . LEU A 239 ? 0.5337 0.5904 0.4919 0.1102  -0.0022 -0.0109 1276 LEU A N   
1687 C CA  . LEU A 239 ? 0.5567 0.6326 0.4966 0.1388  0.0016  -0.0022 1276 LEU A CA  
1688 C C   . LEU A 239 ? 0.6147 0.6268 0.5497 0.1611  -0.0057 0.0048  1276 LEU A C   
1689 O O   . LEU A 239 ? 0.6472 0.6607 0.5576 0.1942  -0.0107 -0.0004 1276 LEU A O   
1690 C CB  . LEU A 239 ? 0.5431 0.6491 0.4836 0.1349  0.0131  0.0138  1276 LEU A CB  
1691 C CG  . LEU A 239 ? 0.5043 0.6737 0.4487 0.1201  0.0132  0.0011  1276 LEU A CG  
1692 C CD1 . LEU A 239 ? 0.5066 0.6936 0.4428 0.1233  0.0179  0.0105  1276 LEU A CD1 
1693 C CD2 . LEU A 239 ? 0.5011 0.7266 0.4429 0.1367  0.0083  -0.0111 1276 LEU A CD2 
1694 N N   . MET A 240 ? 0.6327 0.5890 0.5969 0.1430  -0.0067 0.0173  1277 MET A N   
1695 C CA  . MET A 240 ? 0.6943 0.5812 0.6699 0.1567  -0.0127 0.0298  1277 MET A CA  
1696 C C   . MET A 240 ? 0.7305 0.5691 0.7000 0.1694  -0.0409 -0.0009 1277 MET A C   
1697 O O   . MET A 240 ? 0.7938 0.5692 0.7651 0.1881  -0.0529 0.0005  1277 MET A O   
1698 C CB  . MET A 240 ? 0.7053 0.5558 0.7322 0.1284  -0.0028 0.0571  1277 MET A CB  
1699 C CG  . MET A 240 ? 0.6993 0.5838 0.7207 0.1323  0.0273  0.0939  1277 MET A CG  
1700 S SD  . MET A 240 ? 0.7581 0.6380 0.7348 0.1804  0.0401  0.1188  1277 MET A SD  
1701 C CE  . MET A 240 ? 0.7068 0.6812 0.6339 0.1976  0.0378  0.0945  1277 MET A CE  
1702 N N   . THR A 241 ? 0.7005 0.5647 0.6589 0.1639  -0.0520 -0.0286 1278 THR A N   
1703 C CA  . THR A 241 ? 0.7432 0.5697 0.6805 0.1871  -0.0798 -0.0617 1278 THR A CA  
1704 C C   . THR A 241 ? 0.7393 0.6212 0.6246 0.2226  -0.0735 -0.0742 1278 THR A C   
1705 O O   . THR A 241 ? 0.7696 0.6411 0.6246 0.2483  -0.0899 -0.1004 1278 THR A O   
1706 C CB  . THR A 241 ? 0.7310 0.5414 0.6913 0.1633  -0.0979 -0.0817 1278 THR A CB  
1707 O OG1 . THR A 241 ? 0.6666 0.5441 0.6178 0.1473  -0.0783 -0.0768 1278 THR A OG1 
1708 C CG2 . THR A 241 ? 0.7394 0.5036 0.7659 0.1281  -0.1056 -0.0695 1278 THR A CG2 
1709 N N   . ARG A 242 ? 0.6577 0.7672 0.6116 0.1356  0.0257  -0.1302 1279 ARG A N   
1710 C CA  . ARG A 242 ? 0.6499 0.8412 0.6149 0.1512  0.0380  -0.1372 1279 ARG A CA  
1711 C C   . ARG A 242 ? 0.6313 0.8596 0.5871 0.1290  0.0512  -0.1414 1279 ARG A C   
1712 O O   . ARG A 242 ? 0.6516 0.9143 0.5973 0.1482  0.0606  -0.1590 1279 ARG A O   
1713 C CB  . ARG A 242 ? 0.7026 0.8967 0.6640 0.2006  0.0351  -0.1586 1279 ARG A CB  
1714 C CG  . ARG A 242 ? 0.7265 0.9023 0.6995 0.2266  0.0220  -0.1505 1279 ARG A CG  
1715 C CD  . ARG A 242 ? 0.7828 0.9695 0.7543 0.2815  0.0191  -0.1730 1279 ARG A CD  
1716 N NE  . ARG A 242 ? 0.8043 0.9933 0.7912 0.3094  0.0065  -0.1628 1279 ARG A NE  
1717 C CZ  . ARG A 242 ? 0.8387 0.9468 0.8123 0.3120  -0.0119 -0.1496 1279 ARG A CZ  
1718 N NH1 . ARG A 242 ? 0.8569 0.9739 0.8417 0.3373  -0.0241 -0.1379 1279 ARG A NH1 
1719 N NH2 . ARG A 242 ? 0.8573 0.8787 0.8070 0.2881  -0.0188 -0.1466 1279 ARG A NH2 
1720 N N   . GLY A 243 ? 0.5980 0.8163 0.5538 0.0904  0.0518  -0.1248 1280 GLY A N   
1721 C CA  . GLY A 243 ? 0.5820 0.8316 0.5277 0.0654  0.0618  -0.1220 1280 GLY A CA  
1722 C C   . GLY A 243 ? 0.6116 0.8297 0.5285 0.0705  0.0597  -0.1392 1280 GLY A C   
1723 O O   . GLY A 243 ? 0.6264 0.8846 0.5274 0.0760  0.0708  -0.1485 1280 GLY A O   
1724 N N   . ALA A 244 ? 0.6246 0.7736 0.5343 0.0668  0.0449  -0.1425 1281 ALA A N   
1725 C CA  . ALA A 244 ? 0.6577 0.7719 0.5408 0.0664  0.0369  -0.1582 1281 ALA A CA  
1726 C C   . ALA A 244 ? 0.6359 0.7545 0.5131 0.0336  0.0369  -0.1443 1281 ALA A C   
1727 O O   . ALA A 244 ? 0.5975 0.7232 0.4929 0.0121  0.0392  -0.1241 1281 ALA A O   
1728 C CB  . ALA A 244 ? 0.6863 0.7286 0.5693 0.0729  0.0186  -0.1666 1281 ALA A CB  
1729 N N   . PRO A 245 ? 0.6675 0.7791 0.5148 0.0312  0.0329  -0.1554 1282 PRO A N   
1730 C CA  . PRO A 245 ? 0.6574 0.7643 0.4963 0.0039  0.0281  -0.1419 1282 PRO A CA  
1731 C C   . PRO A 245 ? 0.6537 0.7104 0.5103 -0.0088 0.0098  -0.1377 1282 PRO A C   
1732 O O   . PRO A 245 ? 0.6843 0.7026 0.5359 -0.0007 -0.0050 -0.1536 1282 PRO A O   
1733 C CB  . PRO A 245 ? 0.6994 0.8143 0.4954 0.0113  0.0278  -0.1571 1282 PRO A CB  
1734 C CG  . PRO A 245 ? 0.7425 0.8349 0.5260 0.0423  0.0225  -0.1852 1282 PRO A CG  
1735 C CD  . PRO A 245 ? 0.7213 0.8269 0.5367 0.0576  0.0313  -0.1823 1282 PRO A CD  
1736 N N   . PRO A 246 ? 0.6228 0.6794 0.5014 -0.0290 0.0103  -0.1172 1283 PRO A N   
1737 C CA  . PRO A 246 ? 0.6176 0.6399 0.5187 -0.0403 -0.0032 -0.1121 1283 PRO A CA  
1738 C C   . PRO A 246 ? 0.6483 0.6516 0.5350 -0.0451 -0.0216 -0.1214 1283 PRO A C   
1739 O O   . PRO A 246 ? 0.6623 0.6795 0.5190 -0.0466 -0.0224 -0.1225 1283 PRO A O   
1740 C CB  . PRO A 246 ? 0.5820 0.6170 0.4988 -0.0560 0.0038  -0.0911 1283 PRO A CB  
1741 C CG  . PRO A 246 ? 0.5697 0.6380 0.4791 -0.0539 0.0197  -0.0853 1283 PRO A CG  
1742 C CD  . PRO A 246 ? 0.5955 0.6852 0.4786 -0.0417 0.0236  -0.0991 1283 PRO A CD  
1743 N N   . TYR A 247 ? 0.6659 0.6386 0.5735 -0.0493 -0.0373 -0.1266 1284 TYR A N   
1744 C CA  . TYR A 247 ? 0.6989 0.6555 0.6012 -0.0566 -0.0597 -0.1350 1284 TYR A CA  
1745 C C   . TYR A 247 ? 0.7467 0.7013 0.5995 -0.0442 -0.0658 -0.1546 1284 TYR A C   
1746 O O   . TYR A 247 ? 0.7581 0.7242 0.5852 -0.0481 -0.0716 -0.1520 1284 TYR A O   
1747 C CB  . TYR A 247 ? 0.6769 0.6494 0.5945 -0.0697 -0.0633 -0.1175 1284 TYR A CB  
1748 C CG  . TYR A 247 ? 0.6403 0.6197 0.6005 -0.0775 -0.0532 -0.1001 1284 TYR A CG  
1749 C CD1 . TYR A 247 ? 0.6393 0.6090 0.6392 -0.0862 -0.0611 -0.0983 1284 TYR A CD1 
1750 C CD2 . TYR A 247 ? 0.6129 0.6091 0.5717 -0.0776 -0.0354 -0.0856 1284 TYR A CD2 
1751 C CE1 . TYR A 247 ? 0.6118 0.5928 0.6467 -0.0919 -0.0482 -0.0822 1284 TYR A CE1 
1752 C CE2 . TYR A 247 ? 0.5871 0.5877 0.5770 -0.0819 -0.0256 -0.0725 1284 TYR A CE2 
1753 C CZ  . TYR A 247 ? 0.5865 0.5817 0.6135 -0.0875 -0.0302 -0.0707 1284 TYR A CZ  
1754 O OH  . TYR A 247 ? 0.5665 0.5709 0.6203 -0.0903 -0.0170 -0.0576 1284 TYR A OH  
1755 N N   . PRO A 248 ? 0.7851 0.7227 0.6192 -0.0266 -0.0647 -0.1749 1285 PRO A N   
1756 C CA  . PRO A 248 ? 0.8336 0.7760 0.6159 -0.0090 -0.0640 -0.1956 1285 PRO A CA  
1757 C C   . PRO A 248 ? 0.8866 0.8006 0.6389 -0.0118 -0.0914 -0.2137 1285 PRO A C   
1758 O O   . PRO A 248 ? 0.9260 0.8483 0.6275 -0.0002 -0.0909 -0.2275 1285 PRO A O   
1759 C CB  . PRO A 248 ? 0.8578 0.7849 0.6363 0.0150  -0.0566 -0.2130 1285 PRO A CB  
1760 C CG  . PRO A 248 ? 0.8494 0.7360 0.6682 0.0042  -0.0694 -0.2076 1285 PRO A CG  
1761 C CD  . PRO A 248 ? 0.7904 0.7003 0.6481 -0.0204 -0.0644 -0.1789 1285 PRO A CD  
1762 N N   . ASP A 249 ? 0.8922 0.7764 0.6757 -0.0283 -0.1153 -0.2131 1286 ASP A N   
1763 C CA  . ASP A 249 ? 0.9459 0.8040 0.7088 -0.0350 -0.1471 -0.2299 1286 ASP A CA  
1764 C C   . ASP A 249 ? 0.9142 0.7887 0.7151 -0.0576 -0.1619 -0.2093 1286 ASP A C   
1765 O O   . ASP A 249 ? 0.9317 0.7876 0.7548 -0.0719 -0.1901 -0.2155 1286 ASP A O   
1766 C CB  . ASP A 249 ? 0.9992 0.8036 0.7626 -0.0325 -0.1675 -0.2542 1286 ASP A CB  
1767 C CG  . ASP A 249 ? 0.9724 0.7603 0.7911 -0.0442 -0.1628 -0.2404 1286 ASP A CG  
1768 O OD1 . ASP A 249 ? 0.9153 0.7363 0.7764 -0.0565 -0.1472 -0.2129 1286 ASP A OD1 
1769 O OD2 . ASP A 249 ? 1.0165 0.7548 0.8304 -0.0399 -0.1747 -0.2571 1286 ASP A OD2 
1770 N N   . VAL A 250 ? 0.8731 0.7832 0.6818 -0.0602 -0.1438 -0.1853 1287 VAL A N   
1771 C CA  . VAL A 250 ? 0.8492 0.7764 0.6895 -0.0739 -0.1552 -0.1658 1287 VAL A CA  
1772 C C   . VAL A 250 ? 0.8514 0.7983 0.6524 -0.0698 -0.1468 -0.1521 1287 VAL A C   
1773 O O   . VAL A 250 ? 0.8384 0.7992 0.6187 -0.0641 -0.1207 -0.1452 1287 VAL A O   
1774 C CB  . VAL A 250 ? 0.7939 0.7341 0.6964 -0.0831 -0.1409 -0.1467 1287 VAL A CB  
1775 C CG1 . VAL A 250 ? 0.7690 0.7309 0.7035 -0.0906 -0.1498 -0.1284 1287 VAL A CG1 
1776 C CG2 . VAL A 250 ? 0.8010 0.7196 0.7397 -0.0915 -0.1479 -0.1551 1287 VAL A CG2 
1777 N N   . ASN A 251 ? 0.8721 0.8201 0.6646 -0.0741 -0.1710 -0.1465 1288 ASN A N   
1778 C CA  . ASN A 251 ? 0.8909 0.8467 0.6377 -0.0718 -0.1689 -0.1317 1288 ASN A CA  
1779 C C   . ASN A 251 ? 0.8442 0.8128 0.6185 -0.0760 -0.1499 -0.1058 1288 ASN A C   
1780 O O   . ASN A 251 ? 0.8044 0.7785 0.6349 -0.0791 -0.1475 -0.0996 1288 ASN A O   
1781 C CB  . ASN A 251 ? 0.9363 0.8841 0.6629 -0.0725 -0.2051 -0.1332 1288 ASN A CB  
1782 C CG  . ASN A 251 ? 0.9762 0.9226 0.6383 -0.0697 -0.2056 -0.1186 1288 ASN A CG  
1783 O OD1 . ASN A 251 ? 0.9725 0.9262 0.6040 -0.0701 -0.1775 -0.1081 1288 ASN A OD1 
1784 N ND2 . ASN A 251 ? 1.0201 0.9585 0.6612 -0.0685 -0.2388 -0.1162 1288 ASN A ND2 
1785 N N   . THR A 252 ? 0.8565 0.8283 0.5871 -0.0771 -0.1365 -0.0909 1289 THR A N   
1786 C CA  . THR A 252 ? 0.8281 0.8017 0.5716 -0.0828 -0.1225 -0.0673 1289 THR A CA  
1787 C C   . THR A 252 ? 0.8252 0.7889 0.5976 -0.0802 -0.1452 -0.0561 1289 THR A C   
1788 O O   . THR A 252 ? 0.7909 0.7557 0.6022 -0.0796 -0.1367 -0.0464 1289 THR A O   
1789 C CB  . THR A 252 ? 0.8604 0.8346 0.5456 -0.0897 -0.1095 -0.0521 1289 THR A CB  
1790 O OG1 . THR A 252 ? 0.8691 0.8635 0.5304 -0.0877 -0.0896 -0.0657 1289 THR A OG1 
1791 C CG2 . THR A 252 ? 0.8395 0.8091 0.5340 -0.0995 -0.0947 -0.0299 1289 THR A CG2 
1792 N N   . PHE A 253 ? 0.8661 0.8223 0.6178 -0.0761 -0.1747 -0.0586 1290 PHE A N   
1793 C CA  . PHE A 253 ? 0.8739 0.8254 0.6490 -0.0693 -0.1999 -0.0472 1290 PHE A CA  
1794 C C   . PHE A 253 ? 0.8334 0.8061 0.6844 -0.0666 -0.2080 -0.0572 1290 PHE A C   
1795 O O   . PHE A 253 ? 0.8147 0.7953 0.7073 -0.0590 -0.2113 -0.0468 1290 PHE A O   
1796 C CB  . PHE A 253 ? 0.9378 0.8775 0.6630 -0.0654 -0.2316 -0.0461 1290 PHE A CB  
1797 C CG  . PHE A 253 ? 0.9877 0.9078 0.6337 -0.0701 -0.2240 -0.0312 1290 PHE A CG  
1798 C CD1 . PHE A 253 ? 0.9745 0.8887 0.6046 -0.0791 -0.1939 -0.0156 1290 PHE A CD1 
1799 C CD2 . PHE A 253 ? 1.0534 0.9627 0.6388 -0.0678 -0.2478 -0.0319 1290 PHE A CD2 
1800 C CE1 . PHE A 253 ? 1.0243 0.9254 0.5847 -0.0887 -0.1859 0.0012  1290 PHE A CE1 
1801 C CE2 . PHE A 253 ? 1.1048 0.9992 0.6143 -0.0745 -0.2382 -0.0149 1290 PHE A CE2 
1802 C CZ  . PHE A 253 ? 1.0898 0.9817 0.5893 -0.0864 -0.2063 0.0026  1290 PHE A CZ  
1803 N N   . ASP A 254 ? 0.8242 0.8052 0.6918 -0.0729 -0.2104 -0.0770 1291 ASP A N   
1804 C CA  . ASP A 254 ? 0.7945 0.7961 0.7320 -0.0771 -0.2200 -0.0847 1291 ASP A CA  
1805 C C   . ASP A 254 ? 0.7399 0.7492 0.7166 -0.0815 -0.1880 -0.0827 1291 ASP A C   
1806 O O   . ASP A 254 ? 0.7238 0.7440 0.7466 -0.0902 -0.1890 -0.0903 1291 ASP A O   
1807 C CB  . ASP A 254 ? 0.8278 0.8244 0.7599 -0.0852 -0.2448 -0.1064 1291 ASP A CB  
1808 C CG  . ASP A 254 ? 0.8866 0.8749 0.7735 -0.0808 -0.2798 -0.1107 1291 ASP A CG  
1809 O OD1 . ASP A 254 ? 0.8951 0.8988 0.8047 -0.0747 -0.3019 -0.0990 1291 ASP A OD1 
1810 O OD2 . ASP A 254 ? 0.9295 0.8967 0.7570 -0.0811 -0.2852 -0.1262 1291 ASP A OD2 
1811 N N   . ILE A 255 ? 0.7157 0.7176 0.6724 -0.0777 -0.1616 -0.0712 1292 ILE A N   
1812 C CA  . ILE A 255 ? 0.6713 0.6781 0.6536 -0.0808 -0.1327 -0.0692 1292 ILE A CA  
1813 C C   . ILE A 255 ? 0.6389 0.6648 0.6759 -0.0765 -0.1270 -0.0589 1292 ILE A C   
1814 O O   . ILE A 255 ? 0.6094 0.6463 0.6820 -0.0810 -0.1101 -0.0588 1292 ILE A O   
1815 C CB  . ILE A 255 ? 0.6679 0.6631 0.6059 -0.0804 -0.1098 -0.0630 1292 ILE A CB  
1816 C CG1 . ILE A 255 ? 0.6356 0.6350 0.5896 -0.0833 -0.0850 -0.0661 1292 ILE A CG1 
1817 C CG2 . ILE A 255 ? 0.6741 0.6608 0.5997 -0.0762 -0.1074 -0.0460 1292 ILE A CG2 
1818 C CD1 . ILE A 255 ? 0.6469 0.6415 0.5964 -0.0847 -0.0870 -0.0829 1292 ILE A CD1 
1819 N N   . THR A 256 ? 0.6477 0.6767 0.6880 -0.0657 -0.1409 -0.0499 1293 THR A N   
1820 C CA  . THR A 256 ? 0.6264 0.6760 0.7150 -0.0549 -0.1347 -0.0421 1293 THR A CA  
1821 C C   . THR A 256 ? 0.6135 0.7021 0.7677 -0.0597 -0.1458 -0.0469 1293 THR A C   
1822 O O   . THR A 256 ? 0.5867 0.7010 0.7876 -0.0603 -0.1275 -0.0435 1293 THR A O   
1823 C CB  . THR A 256 ? 0.6539 0.6893 0.7228 -0.0373 -0.1488 -0.0321 1293 THR A CB  
1824 O OG1 . THR A 256 ? 0.6686 0.6659 0.6768 -0.0405 -0.1381 -0.0256 1293 THR A OG1 
1825 C CG2 . THR A 256 ? 0.6426 0.6979 0.7573 -0.0190 -0.1413 -0.0272 1293 THR A CG2 
1826 N N   . VAL A 257 ? 0.6368 0.7308 0.7921 -0.0652 -0.1764 -0.0541 1294 VAL A N   
1827 C CA  . VAL A 257 ? 0.6319 0.7643 0.8505 -0.0754 -0.1933 -0.0587 1294 VAL A CA  
1828 C C   . VAL A 257 ? 0.6119 0.7435 0.8516 -0.0962 -0.1755 -0.0635 1294 VAL A C   
1829 O O   . VAL A 257 ? 0.5933 0.7605 0.8952 -0.1060 -0.1691 -0.0588 1294 VAL A O   
1830 C CB  . VAL A 257 ? 0.6716 0.8015 0.8749 -0.0793 -0.2340 -0.0679 1294 VAL A CB  
1831 C CG1 . VAL A 257 ? 0.6744 0.8425 0.9441 -0.0970 -0.2549 -0.0741 1294 VAL A CG1 
1832 C CG2 . VAL A 257 ? 0.6967 0.8257 0.8792 -0.0575 -0.2550 -0.0596 1294 VAL A CG2 
1833 N N   . TYR A 258 ? 0.6196 0.7113 0.8064 -0.1019 -0.1674 -0.0717 1295 TYR A N   
1834 C CA  . TYR A 258 ? 0.6144 0.6919 0.8086 -0.1175 -0.1540 -0.0768 1295 TYR A CA  
1835 C C   . TYR A 258 ? 0.5795 0.6762 0.8110 -0.1184 -0.1228 -0.0629 1295 TYR A C   
1836 O O   . TYR A 258 ? 0.5765 0.6828 0.8471 -0.1351 -0.1177 -0.0598 1295 TYR A O   
1837 C CB  . TYR A 258 ? 0.6306 0.6673 0.7583 -0.1133 -0.1475 -0.0874 1295 TYR A CB  
1838 C CG  . TYR A 258 ? 0.6353 0.6483 0.7608 -0.1225 -0.1360 -0.0940 1295 TYR A CG  
1839 C CD1 . TYR A 258 ? 0.6744 0.6598 0.7856 -0.1312 -0.1570 -0.1116 1295 TYR A CD1 
1840 C CD2 . TYR A 258 ? 0.6086 0.6204 0.7393 -0.1202 -0.1067 -0.0837 1295 TYR A CD2 
1841 C CE1 . TYR A 258 ? 0.6881 0.6421 0.7929 -0.1361 -0.1492 -0.1179 1295 TYR A CE1 
1842 C CE2 . TYR A 258 ? 0.6183 0.6040 0.7435 -0.1255 -0.0988 -0.0879 1295 TYR A CE2 
1843 C CZ  . TYR A 258 ? 0.6591 0.6138 0.7718 -0.1326 -0.1200 -0.1047 1295 TYR A CZ  
1844 O OH  . TYR A 258 ? 0.6824 0.6023 0.7864 -0.1347 -0.1147 -0.1089 1295 TYR A OH  
1845 N N   . LEU A 259 ? 0.5617 0.6604 0.7763 -0.1019 -0.1031 -0.0543 1296 LEU A N   
1846 C CA  . LEU A 259 ? 0.5383 0.6521 0.7758 -0.0989 -0.0734 -0.0432 1296 LEU A CA  
1847 C C   . LEU A 259 ? 0.5316 0.6950 0.8337 -0.0969 -0.0728 -0.0354 1296 LEU A C   
1848 O O   . LEU A 259 ? 0.5181 0.7044 0.8550 -0.1043 -0.0517 -0.0268 1296 LEU A O   
1849 C CB  . LEU A 259 ? 0.5316 0.6259 0.7248 -0.0826 -0.0579 -0.0398 1296 LEU A CB  
1850 C CG  . LEU A 259 ? 0.5351 0.5948 0.6730 -0.0853 -0.0528 -0.0450 1296 LEU A CG  
1851 C CD1 . LEU A 259 ? 0.5324 0.5777 0.6340 -0.0749 -0.0402 -0.0396 1296 LEU A CD1 
1852 C CD2 . LEU A 259 ? 0.5286 0.5805 0.6714 -0.0956 -0.0388 -0.0457 1296 LEU A CD2 
1853 N N   . LEU A 260 ? 0.5455 0.7286 0.8629 -0.0857 -0.0956 -0.0373 1297 LEU A N   
1854 C CA  . LEU A 260 ? 0.5432 0.7838 0.9284 -0.0797 -0.0982 -0.0313 1297 LEU A CA  
1855 C C   . LEU A 260 ? 0.5463 0.8200 0.9888 -0.1081 -0.1067 -0.0301 1297 LEU A C   
1856 O O   . LEU A 260 ? 0.5374 0.8659 1.0429 -0.1122 -0.0937 -0.0208 1297 LEU A O   
1857 C CB  . LEU A 260 ? 0.5632 0.8119 0.9468 -0.0594 -0.1272 -0.0340 1297 LEU A CB  
1858 C CG  . LEU A 260 ? 0.5706 0.7952 0.9156 -0.0297 -0.1188 -0.0309 1297 LEU A CG  
1859 C CD1 . LEU A 260 ? 0.6001 0.8236 0.9380 -0.0109 -0.1526 -0.0312 1297 LEU A CD1 
1860 C CD2 . LEU A 260 ? 0.5565 0.8131 0.9368 -0.0127 -0.0893 -0.0256 1297 LEU A CD2 
1861 N N   . GLN A 261 ? 0.5672 0.8070 0.9860 -0.1282 -0.1283 -0.0397 1298 GLN A N   
1862 C CA  . GLN A 261 ? 0.5824 0.8363 1.0456 -0.1597 -0.1409 -0.0400 1298 GLN A CA  
1863 C C   . GLN A 261 ? 0.5749 0.8209 1.0477 -0.1763 -0.1094 -0.0287 1298 GLN A C   
1864 O O   . GLN A 261 ? 0.5884 0.8542 1.1090 -0.2048 -0.1121 -0.0217 1298 GLN A O   
1865 C CB  . GLN A 261 ? 0.6172 0.8238 1.0388 -0.1719 -0.1738 -0.0572 1298 GLN A CB  
1866 C CG  . GLN A 261 ? 0.6384 0.8615 1.0619 -0.1639 -0.2119 -0.0662 1298 GLN A CG  
1867 C CD  . GLN A 261 ? 0.6811 0.8527 1.0473 -0.1711 -0.2415 -0.0855 1298 GLN A CD  
1868 O OE1 . GLN A 261 ? 0.6957 0.8181 1.0196 -0.1780 -0.2327 -0.0941 1298 GLN A OE1 
1869 N NE2 . GLN A 261 ? 0.7094 0.8923 1.0712 -0.1663 -0.2779 -0.0935 1298 GLN A NE2 
1870 N N   . GLY A 262 ? 0.5599 0.7755 0.9854 -0.1605 -0.0817 -0.0258 1299 GLY A N   
1871 C CA  . GLY A 262 ? 0.5554 0.7625 0.9815 -0.1710 -0.0516 -0.0133 1299 GLY A CA  
1872 C C   . GLY A 262 ? 0.5742 0.7164 0.9462 -0.1777 -0.0537 -0.0201 1299 GLY A C   
1873 O O   . GLY A 262 ? 0.5736 0.6988 0.9368 -0.1845 -0.0328 -0.0095 1299 GLY A O   
1874 N N   . ARG A 263 ? 0.5958 0.7037 0.9296 -0.1730 -0.0789 -0.0377 1300 ARG A N   
1875 C CA  . ARG A 263 ? 0.6230 0.6741 0.9069 -0.1737 -0.0829 -0.0482 1300 ARG A CA  
1876 C C   . ARG A 263 ? 0.6015 0.6379 0.8381 -0.1516 -0.0599 -0.0469 1300 ARG A C   
1877 O O   . ARG A 263 ? 0.5795 0.6349 0.8051 -0.1356 -0.0533 -0.0456 1300 ARG A O   
1878 C CB  . ARG A 263 ? 0.6592 0.6851 0.9159 -0.1736 -0.1158 -0.0694 1300 ARG A CB  
1879 C CG  . ARG A 263 ? 0.6908 0.7311 0.9921 -0.1970 -0.1455 -0.0735 1300 ARG A CG  
1880 C CD  . ARG A 263 ? 0.7330 0.7443 0.9957 -0.1942 -0.1795 -0.0969 1300 ARG A CD  
1881 N NE  . ARG A 263 ? 0.7637 0.7948 1.0698 -0.2163 -0.2128 -0.1016 1300 ARG A NE  
1882 C CZ  . ARG A 263 ? 0.8095 0.8189 1.0878 -0.2183 -0.2485 -0.1224 1300 ARG A CZ  
1883 N NH1 . ARG A 263 ? 0.8322 0.8019 1.0376 -0.1977 -0.2516 -0.1398 1300 ARG A NH1 
1884 N NH2 . ARG A 263 ? 0.8348 0.8667 1.1585 -0.2413 -0.2810 -0.1257 1300 ARG A NH2 
1885 N N   . ARG A 264 ? 0.6135 0.6141 0.8231 -0.1515 -0.0505 -0.0469 1301 ARG A N   
1886 C CA  . ARG A 264 ? 0.5965 0.5871 0.7665 -0.1335 -0.0312 -0.0452 1301 ARG A CA  
1887 C C   . ARG A 264 ? 0.6247 0.5740 0.7555 -0.1262 -0.0392 -0.0589 1301 ARG A C   
1888 O O   . ARG A 264 ? 0.6601 0.5826 0.7900 -0.1339 -0.0595 -0.0709 1301 ARG A O   
1889 C CB  . ARG A 264 ? 0.5822 0.5841 0.7668 -0.1361 -0.0058 -0.0261 1301 ARG A CB  
1890 C CG  . ARG A 264 ? 0.5593 0.6057 0.7799 -0.1370 0.0064  -0.0149 1301 ARG A CG  
1891 C CD  . ARG A 264 ? 0.5369 0.5965 0.7361 -0.1179 0.0103  -0.0198 1301 ARG A CD  
1892 N NE  . ARG A 264 ? 0.5227 0.6191 0.7520 -0.1120 0.0224  -0.0117 1301 ARG A NE  
1893 C CZ  . ARG A 264 ? 0.5209 0.6498 0.7924 -0.1139 0.0116  -0.0119 1301 ARG A CZ  
1894 N NH1 . ARG A 264 ? 0.5325 0.6586 0.8178 -0.1245 -0.0142 -0.0198 1301 ARG A NH1 
1895 N NH2 . ARG A 264 ? 0.5121 0.6777 0.8111 -0.1028 0.0256  -0.0056 1301 ARG A NH2 
1896 N N   . LEU A 265 ? 0.6143 0.5599 0.7132 -0.1102 -0.0245 -0.0585 1302 LEU A N   
1897 C CA  . LEU A 265 ? 0.6415 0.5570 0.7072 -0.0972 -0.0286 -0.0710 1302 LEU A CA  
1898 C C   . LEU A 265 ? 0.6784 0.5561 0.7536 -0.1045 -0.0318 -0.0654 1302 LEU A C   
1899 O O   . LEU A 265 ? 0.6716 0.5538 0.7679 -0.1153 -0.0194 -0.0458 1302 LEU A O   
1900 C CB  . LEU A 265 ? 0.6174 0.5501 0.6585 -0.0809 -0.0115 -0.0679 1302 LEU A CB  
1901 C CG  . LEU A 265 ? 0.5964 0.5574 0.6203 -0.0762 -0.0093 -0.0722 1302 LEU A CG  
1902 C CD1 . LEU A 265 ? 0.5771 0.5569 0.5838 -0.0673 0.0063  -0.0662 1302 LEU A CD1 
1903 C CD2 . LEU A 265 ? 0.6233 0.5773 0.6225 -0.0699 -0.0236 -0.0910 1302 LEU A CD2 
1904 N N   . LEU A 266 ? 0.7277 0.5646 0.7822 -0.0978 -0.0486 -0.0827 1303 LEU A N   
1905 C CA  . LEU A 266 ? 0.7797 0.5655 0.8356 -0.1039 -0.0566 -0.0787 1303 LEU A CA  
1906 C C   . LEU A 266 ? 0.7846 0.5595 0.8195 -0.0833 -0.0427 -0.0705 1303 LEU A C   
1907 O O   . LEU A 266 ? 0.7546 0.5604 0.7722 -0.0632 -0.0314 -0.0751 1303 LEU A O   
1908 C CB  . LEU A 266 ? 0.8383 0.5769 0.8731 -0.1001 -0.0828 -0.1045 1303 LEU A CB  
1909 C CG  . LEU A 266 ? 0.8457 0.5933 0.8967 -0.1197 -0.1028 -0.1153 1303 LEU A CG  
1910 C CD1 . LEU A 266 ? 0.9168 0.6053 0.9408 -0.1175 -0.1315 -0.1419 1303 LEU A CD1 
1911 C CD2 . LEU A 266 ? 0.8297 0.5988 0.9333 -0.1527 -0.1018 -0.0926 1303 LEU A CD2 
1912 N N   . GLN A 267 ? 0.8295 0.5602 0.8663 -0.0903 -0.0455 -0.0569 1304 GLN A N   
1913 C CA  . GLN A 267 ? 0.8450 0.5613 0.8619 -0.0709 -0.0362 -0.0458 1304 GLN A CA  
1914 C C   . GLN A 267 ? 0.8815 0.5729 0.8659 -0.0368 -0.0471 -0.0699 1304 GLN A C   
1915 O O   . GLN A 267 ? 0.9376 0.5769 0.9091 -0.0332 -0.0667 -0.0870 1304 GLN A O   
1916 C CB  . GLN A 267 ? 0.8905 0.5597 0.9137 -0.0894 -0.0382 -0.0216 1304 GLN A CB  
1917 C CG  . GLN A 267 ? 0.9043 0.5600 0.9049 -0.0703 -0.0294 -0.0049 1304 GLN A CG  
1918 C CD  . GLN A 267 ? 0.9550 0.5639 0.9565 -0.0917 -0.0296 0.0241  1304 GLN A CD  
1919 O OE1 . GLN A 267 ? 0.9797 0.5690 1.0034 -0.1241 -0.0349 0.0329  1304 GLN A OE1 
1920 N NE2 . GLN A 267 ? 0.9756 0.5684 0.9527 -0.0752 -0.0245 0.0411  1304 GLN A NE2 
1921 N N   . PRO A 268 ? 0.8566 0.5869 0.8278 -0.0106 -0.0352 -0.0734 1305 PRO A N   
1922 C CA  . PRO A 268 ? 0.8912 0.6097 0.8369 0.0260  -0.0419 -0.0945 1305 PRO A CA  
1923 C C   . PRO A 268 ? 0.9650 0.6120 0.8944 0.0421  -0.0567 -0.0927 1305 PRO A C   
1924 O O   . PRO A 268 ? 0.9860 0.5959 0.9217 0.0230  -0.0588 -0.0688 1305 PRO A O   
1925 C CB  . PRO A 268 ? 0.8428 0.6246 0.7894 0.0423  -0.0251 -0.0882 1305 PRO A CB  
1926 C CG  . PRO A 268 ? 0.7822 0.6087 0.7476 0.0137  -0.0116 -0.0737 1305 PRO A CG  
1927 C CD  . PRO A 268 ? 0.7954 0.5858 0.7766 -0.0150 -0.0158 -0.0590 1305 PRO A CD  
1928 N N   . GLU A 269 ? 1.0099 0.6378 0.9160 0.0790  -0.0660 -0.1175 1306 GLU A N   
1929 C CA  . GLU A 269 ? 1.0942 0.6442 0.9787 0.1019  -0.0839 -0.1211 1306 GLU A CA  
1930 C C   . GLU A 269 ? 1.0970 0.6461 0.9830 0.1113  -0.0790 -0.0929 1306 GLU A C   
1931 O O   . GLU A 269 ? 1.1510 0.6328 1.0291 0.1001  -0.0899 -0.0732 1306 GLU A O   
1932 C CB  . GLU A 269 ? 1.1367 0.6806 0.9959 0.1478  -0.0912 -0.1569 1306 GLU A CB  
1933 C CG  . GLU A 269 ? 1.2354 0.6887 1.0675 0.1784  -0.1130 -0.1655 1306 GLU A CG  
1934 C CD  . GLU A 269 ? 1.2879 0.7329 1.0922 0.2289  -0.1197 -0.2055 1306 GLU A CD  
1935 O OE1 . GLU A 269 ? 1.3708 0.7309 1.1465 0.2369  -0.1418 -0.2278 1306 GLU A OE1 
1936 O OE2 . GLU A 269 ? 1.2498 0.7745 1.0609 0.2596  -0.1026 -0.2147 1306 GLU A OE2 
1937 N N   . TYR A 270 ? 1.0443 0.6679 0.9387 0.1292  -0.0638 -0.0898 1307 TYR A N   
1938 C CA  . TYR A 270 ? 1.0480 0.6785 0.9402 0.1435  -0.0623 -0.0668 1307 TYR A CA  
1939 C C   . TYR A 270 ? 0.9826 0.6608 0.8906 0.1103  -0.0454 -0.0403 1307 TYR A C   
1940 O O   . TYR A 270 ? 0.9644 0.6811 0.8724 0.1216  -0.0404 -0.0275 1307 TYR A O   
1941 C CB  . TYR A 270 ? 1.0471 0.7279 0.9384 0.1897  -0.0616 -0.0834 1307 TYR A CB  
1942 C CG  . TYR A 270 ? 1.1246 0.7555 0.9961 0.2333  -0.0779 -0.1092 1307 TYR A CG  
1943 C CD1 . TYR A 270 ? 1.2087 0.7481 1.0579 0.2495  -0.0984 -0.1005 1307 TYR A CD1 
1944 C CD2 . TYR A 270 ? 1.1222 0.7940 0.9931 0.2600  -0.0727 -0.1422 1307 TYR A CD2 
1945 C CE1 . TYR A 270 ? 1.2892 0.7735 1.1160 0.2938  -0.1155 -0.1267 1307 TYR A CE1 
1946 C CE2 . TYR A 270 ? 1.1988 0.8246 1.0474 0.3053  -0.0866 -0.1697 1307 TYR A CE2 
1947 C CZ  . TYR A 270 ? 1.2839 0.8127 1.1104 0.3239  -0.1092 -0.1634 1307 TYR A CZ  
1948 O OH  . TYR A 270 ? 1.3704 0.8444 1.1708 0.3728  -0.1250 -0.1931 1307 TYR A OH  
1949 N N   . CYS A 271 ? 0.9527 0.6284 0.8734 0.0714  -0.0384 -0.0335 1308 CYS A N   
1950 C CA  . CYS A 271 ? 0.9024 0.6151 0.8352 0.0428  -0.0220 -0.0104 1308 CYS A CA  
1951 C C   . CYS A 271 ? 0.9445 0.6037 0.8702 0.0224  -0.0233 0.0186  1308 CYS A C   
1952 O O   . CYS A 271 ? 0.9809 0.5909 0.9115 0.0025  -0.0310 0.0209  1308 CYS A O   
1953 C CB  . CYS A 271 ? 0.8507 0.5999 0.8041 0.0162  -0.0122 -0.0187 1308 CYS A CB  
1954 S SG  . CYS A 271 ? 0.7982 0.5880 0.7647 -0.0131 0.0081  0.0056  1308 CYS A SG  
1955 N N   . PRO A 272 ? 0.9460 0.6134 0.8582 0.0247  -0.0166 0.0427  1309 PRO A N   
1956 C CA  . PRO A 272 ? 0.9891 0.6134 0.8904 0.0020  -0.0130 0.0746  1309 PRO A CA  
1957 C C   . PRO A 272 ? 0.9599 0.6044 0.8858 -0.0376 0.0035  0.0840  1309 PRO A C   
1958 O O   . PRO A 272 ? 0.8980 0.5991 0.8435 -0.0440 0.0149  0.0708  1309 PRO A O   
1959 C CB  . PRO A 272 ? 0.9866 0.6349 0.8650 0.0151  -0.0070 0.0932  1309 PRO A CB  
1960 C CG  . PRO A 272 ? 0.9640 0.6492 0.8421 0.0515  -0.0168 0.0706  1309 PRO A CG  
1961 C CD  . PRO A 272 ? 0.9161 0.6347 0.8203 0.0479  -0.0134 0.0413  1309 PRO A CD  
1962 N N   . ASP A 273 ? 1.0112 0.6099 0.9368 -0.0639 0.0043  0.1082  1310 ASP A N   
1963 C CA  . ASP A 273 ? 0.9921 0.6153 0.9477 -0.1017 0.0202  0.1197  1310 ASP A CA  
1964 C C   . ASP A 273 ? 0.9449 0.6324 0.9007 -0.1047 0.0456  0.1298  1310 ASP A C   
1965 O O   . ASP A 273 ? 0.8954 0.6322 0.8799 -0.1169 0.0577  0.1203  1310 ASP A O   
1966 C CB  . ASP A 273 ? 1.0636 0.6286 1.0191 -0.1321 0.0170  0.1480  1310 ASP A CB  
1967 C CG  . ASP A 273 ? 1.1211 0.6126 1.0756 -0.1336 -0.0110 0.1354  1310 ASP A CG  
1968 O OD1 . ASP A 273 ? 1.1068 0.5955 1.0584 -0.1068 -0.0264 0.1027  1310 ASP A OD1 
1969 O OD2 . ASP A 273 ? 1.1857 0.6217 1.1400 -0.1626 -0.0172 0.1585  1310 ASP A OD2 
1970 N N   . PRO A 274 ? 0.9654 0.6514 0.8859 -0.0918 0.0523  0.1478  1311 PRO A N   
1971 C CA  . PRO A 274 ? 0.9302 0.6705 0.8421 -0.0918 0.0739  0.1531  1311 PRO A CA  
1972 C C   . PRO A 274 ? 0.8640 0.6564 0.7891 -0.0779 0.0745  0.1239  1311 PRO A C   
1973 O O   . PRO A 274 ? 0.8288 0.6632 0.7646 -0.0865 0.0916  0.1211  1311 PRO A O   
1974 C CB  . PRO A 274 ? 0.9722 0.6908 0.8365 -0.0736 0.0699  0.1712  1311 PRO A CB  
1975 C CG  . PRO A 274 ? 1.0450 0.6913 0.8962 -0.0758 0.0536  0.1891  1311 PRO A CG  
1976 C CD  . PRO A 274 ? 1.0315 0.6597 0.9147 -0.0749 0.0370  0.1636  1311 PRO A CD  
1977 N N   . LEU A 275 ? 0.8531 0.6416 0.7761 -0.0557 0.0562  0.1031  1312 LEU A N   
1978 C CA  . LEU A 275 ? 0.7971 0.6318 0.7296 -0.0453 0.0556  0.0787  1312 LEU A CA  
1979 C C   . LEU A 275 ? 0.7620 0.6127 0.7279 -0.0602 0.0581  0.0636  1312 LEU A C   
1980 O O   . LEU A 275 ? 0.7161 0.6051 0.6901 -0.0617 0.0647  0.0521  1312 LEU A O   
1981 C CB  . LEU A 275 ? 0.8026 0.6346 0.7261 -0.0182 0.0378  0.0637  1312 LEU A CB  
1982 C CG  . LEU A 275 ? 0.7539 0.6368 0.6852 -0.0098 0.0373  0.0424  1312 LEU A CG  
1983 C CD1 . LEU A 275 ? 0.7379 0.6530 0.6523 -0.0112 0.0444  0.0488  1312 LEU A CD1 
1984 C CD2 . LEU A 275 ? 0.7627 0.6499 0.6945 0.0160  0.0226  0.0267  1312 LEU A CD2 
1985 N N   . TYR A 276 ? 0.7876 0.6045 0.7701 -0.0714 0.0497  0.0640  1313 TYR A N   
1986 C CA  . TYR A 276 ? 0.7648 0.5951 0.7786 -0.0862 0.0474  0.0505  1313 TYR A CA  
1987 C C   . TYR A 276 ? 0.7499 0.6120 0.7865 -0.1074 0.0659  0.0639  1313 TYR A C   
1988 O O   . TYR A 276 ? 0.7156 0.6099 0.7753 -0.1123 0.0676  0.0521  1313 TYR A O   
1989 C CB  . TYR A 276 ? 0.8064 0.5878 0.8288 -0.0939 0.0294  0.0458  1313 TYR A CB  
1990 C CG  . TYR A 276 ? 0.7882 0.5824 0.8398 -0.1086 0.0215  0.0300  1313 TYR A CG  
1991 C CD1 . TYR A 276 ? 0.7491 0.5730 0.8002 -0.0960 0.0170  0.0070  1313 TYR A CD1 
1992 C CD2 . TYR A 276 ? 0.8136 0.5926 0.8934 -0.1372 0.0172  0.0397  1313 TYR A CD2 
1993 C CE1 . TYR A 276 ? 0.7378 0.5721 0.8103 -0.1079 0.0071  -0.0064 1313 TYR A CE1 
1994 C CE2 . TYR A 276 ? 0.7997 0.5940 0.9076 -0.1504 0.0059  0.0249  1313 TYR A CE2 
1995 C CZ  . TYR A 276 ? 0.7621 0.5824 0.8638 -0.1340 0.0001  0.0014  1313 TYR A CZ  
1996 O OH  . TYR A 276 ? 0.7548 0.5885 0.8789 -0.1455 -0.0137 -0.0121 1313 TYR A OH  
1997 N N   . GLU A 277 ? 0.7829 0.6373 0.8118 -0.1178 0.0799  0.0891  1314 GLU A N   
1998 C CA  . GLU A 277 ? 0.7747 0.6674 0.8230 -0.1333 0.1023  0.1021  1314 GLU A CA  
1999 C C   . GLU A 277 ? 0.7310 0.6636 0.7674 -0.1170 0.1129  0.0897  1314 GLU A C   
2000 O O   . GLU A 277 ? 0.7059 0.6746 0.7671 -0.1212 0.1232  0.0847  1314 GLU A O   
2001 C CB  . GLU A 277 ? 0.8292 0.7064 0.8615 -0.1459 0.1179  0.1331  1314 GLU A CB  
2002 C CG  . GLU A 277 ? 0.8843 0.7191 0.9321 -0.1702 0.1085  0.1499  1314 GLU A CG  
2003 C CD  . GLU A 277 ? 0.8772 0.7336 0.9792 -0.1955 0.1057  0.1455  1314 GLU A CD  
2004 O OE1 . GLU A 277 ? 0.8607 0.7717 0.9927 -0.2068 0.1265  0.1526  1314 GLU A OE1 
2005 O OE2 . GLU A 277 ? 0.8965 0.7167 1.0102 -0.2022 0.0814  0.1335  1314 GLU A OE2 
2006 N N   . VAL A 278 ? 0.7274 0.6516 0.7266 -0.0984 0.1080  0.0846  1315 VAL A N   
2007 C CA  . VAL A 278 ? 0.6966 0.6483 0.6791 -0.0860 0.1130  0.0722  1315 VAL A CA  
2008 C C   . VAL A 278 ? 0.6533 0.6216 0.6576 -0.0843 0.1031  0.0507  1315 VAL A C   
2009 O O   . VAL A 278 ? 0.6334 0.6238 0.6396 -0.0818 0.1098  0.0429  1315 VAL A O   
2010 C CB  . VAL A 278 ? 0.7108 0.6521 0.6540 -0.0705 0.1047  0.0718  1315 VAL A CB  
2011 C CG1 . VAL A 278 ? 0.6880 0.6527 0.6158 -0.0626 0.1037  0.0563  1315 VAL A CG1 
2012 C CG2 . VAL A 278 ? 0.7561 0.6805 0.6687 -0.0705 0.1137  0.0947  1315 VAL A CG2 
2013 N N   . MET A 279 ? 0.6453 0.5984 0.6608 -0.0838 0.0864  0.0411  1316 MET A N   
2014 C CA  . MET A 279 ? 0.6132 0.5791 0.6435 -0.0831 0.0762  0.0228  1316 MET A CA  
2015 C C   . MET A 279 ? 0.5956 0.5791 0.6591 -0.0950 0.0811  0.0238  1316 MET A C   
2016 O O   . MET A 279 ? 0.5714 0.5749 0.6392 -0.0915 0.0817  0.0152  1316 MET A O   
2017 C CB  . MET A 279 ? 0.6278 0.5719 0.6594 -0.0792 0.0589  0.0119  1316 MET A CB  
2018 C CG  . MET A 279 ? 0.6311 0.5757 0.6378 -0.0618 0.0525  0.0038  1316 MET A CG  
2019 S SD  . MET A 279 ? 0.6595 0.5794 0.6645 -0.0500 0.0351  -0.0125 1316 MET A SD  
2020 C CE  . MET A 279 ? 0.6812 0.5958 0.6636 -0.0269 0.0323  -0.0088 1316 MET A CE  
2021 N N   . LEU A 280 ? 0.6099 0.5860 0.6981 -0.1096 0.0831  0.0354  1317 LEU A N   
2022 C CA  . LEU A 280 ? 0.5991 0.6022 0.7283 -0.1226 0.0873  0.0386  1317 LEU A CA  
2023 C C   . LEU A 280 ? 0.5862 0.6229 0.7169 -0.1159 0.1090  0.0447  1317 LEU A C   
2024 O O   . LEU A 280 ? 0.5700 0.6365 0.7271 -0.1135 0.1103  0.0387  1317 LEU A O   
2025 C CB  . LEU A 280 ? 0.6309 0.6201 0.7855 -0.1446 0.0864  0.0539  1317 LEU A CB  
2026 C CG  . LEU A 280 ? 0.6532 0.6034 0.8098 -0.1520 0.0614  0.0440  1317 LEU A CG  
2027 C CD1 . LEU A 280 ? 0.6950 0.6257 0.8765 -0.1791 0.0592  0.0614  1317 LEU A CD1 
2028 C CD2 . LEU A 280 ? 0.6321 0.5966 0.8044 -0.1497 0.0436  0.0230  1317 LEU A CD2 
2029 N N   . LYS A 281 ? 0.6003 0.6303 0.6996 -0.1102 0.1244  0.0554  1318 LYS A N   
2030 C CA  . LYS A 281 ? 0.6021 0.6571 0.6907 -0.1005 0.1455  0.0584  1318 LYS A CA  
2031 C C   . LYS A 281 ? 0.5767 0.6361 0.6516 -0.0843 0.1383  0.0390  1318 LYS A C   
2032 O O   . LYS A 281 ? 0.5747 0.6565 0.6581 -0.0746 0.1491  0.0347  1318 LYS A O   
2033 C CB  . LYS A 281 ? 0.6341 0.6727 0.6791 -0.0966 0.1577  0.0713  1318 LYS A CB  
2034 C CG  . LYS A 281 ? 0.6571 0.7207 0.6895 -0.0903 0.1846  0.0793  1318 LYS A CG  
2035 C CD  . LYS A 281 ? 0.6794 0.7683 0.7440 -0.1070 0.2050  0.1010  1318 LYS A CD  
2036 C CE  . LYS A 281 ? 0.7091 0.8266 0.7538 -0.0981 0.2359  0.1095  1318 LYS A CE  
2037 N NZ  . LYS A 281 ? 0.7338 0.8843 0.8130 -0.1184 0.2588  0.1344  1318 LYS A NZ  
2038 N N   . CYS A 282 ? 0.5589 0.5962 0.6121 -0.0810 0.1201  0.0281  1319 CYS A N   
2039 C CA  . CYS A 282 ? 0.5388 0.5739 0.5757 -0.0716 0.1110  0.0132  1319 CYS A CA  
2040 C C   . CYS A 282 ? 0.5214 0.5694 0.5900 -0.0718 0.1018  0.0058  1319 CYS A C   
2041 O O   . CYS A 282 ? 0.5210 0.5704 0.5828 -0.0620 0.1002  -0.0017 1319 CYS A O   
2042 C CB  . CYS A 282 ? 0.5296 0.5481 0.5412 -0.0719 0.0962  0.0067  1319 CYS A CB  
2043 S SG  . CYS A 282 ? 0.5445 0.5524 0.5183 -0.0680 0.1006  0.0139  1319 CYS A SG  
2044 N N   . TRP A 283 ? 0.5117 0.5643 0.6116 -0.0825 0.0927  0.0078  1320 TRP A N   
2045 C CA  . TRP A 283 ? 0.5012 0.5664 0.6295 -0.0835 0.0788  0.0007  1320 TRP A CA  
2046 C C   . TRP A 283 ? 0.5042 0.6042 0.6784 -0.0856 0.0886  0.0079  1320 TRP A C   
2047 O O   . TRP A 283 ? 0.5036 0.6183 0.7154 -0.0963 0.0767  0.0081  1320 TRP A O   
2048 C CB  . TRP A 283 ? 0.5000 0.5502 0.6324 -0.0935 0.0595  -0.0050 1320 TRP A CB  
2049 C CG  . TRP A 283 ? 0.4992 0.5262 0.5933 -0.0898 0.0535  -0.0116 1320 TRP A CG  
2050 C CD1 . TRP A 283 ? 0.4928 0.5159 0.5553 -0.0823 0.0533  -0.0165 1320 TRP A CD1 
2051 C CD2 . TRP A 283 ? 0.5110 0.5180 0.5971 -0.0930 0.0458  -0.0144 1320 TRP A CD2 
2052 N NE1 . TRP A 283 ? 0.4956 0.5088 0.5366 -0.0812 0.0484  -0.0211 1320 TRP A NE1 
2053 C CE2 . TRP A 283 ? 0.5073 0.5093 0.5608 -0.0842 0.0439  -0.0212 1320 TRP A CE2 
2054 C CE3 . TRP A 283 ? 0.5307 0.5217 0.6340 -0.1024 0.0396  -0.0119 1320 TRP A CE3 
2055 C CZ2 . TRP A 283 ? 0.5203 0.5078 0.5599 -0.0788 0.0377  -0.0272 1320 TRP A CZ2 
2056 C CZ3 . TRP A 283 ? 0.5492 0.5132 0.6324 -0.0974 0.0311  -0.0186 1320 TRP A CZ3 
2057 C CH2 . TRP A 283 ? 0.5433 0.5085 0.5959 -0.0830 0.0310  -0.0268 1320 TRP A CH2 
2058 N N   . HIS A 284 ? 0.5116 0.6284 0.6830 -0.0750 0.1099  0.0128  1321 HIS A N   
2059 C CA  . HIS A 284 ? 0.5139 0.6759 0.7310 -0.0719 0.1233  0.0186  1321 HIS A CA  
2060 C C   . HIS A 284 ? 0.5093 0.6837 0.7408 -0.0541 0.1102  0.0068  1321 HIS A C   
2061 O O   . HIS A 284 ? 0.5149 0.6613 0.7074 -0.0385 0.1048  -0.0028 1321 HIS A O   
2062 C CB  . HIS A 284 ? 0.5317 0.7073 0.7327 -0.0627 0.1532  0.0264  1321 HIS A CB  
2063 C CG  . HIS A 284 ? 0.5394 0.7716 0.7904 -0.0636 0.1744  0.0369  1321 HIS A CG  
2064 N ND1 . HIS A 284 ? 0.5353 0.8091 0.8260 -0.0467 0.1751  0.0299  1321 HIS A ND1 
2065 C CD2 . HIS A 284 ? 0.5549 0.8120 0.8229 -0.0801 0.1968  0.0560  1321 HIS A CD2 
2066 C CE1 . HIS A 284 ? 0.5432 0.8746 0.8796 -0.0522 0.1986  0.0431  1321 HIS A CE1 
2067 N NE2 . HIS A 284 ? 0.5570 0.8779 0.8785 -0.0754 0.2133  0.0606  1321 HIS A NE2 
2068 N N   . PRO A 285 ? 0.5046 0.7187 0.7915 -0.0569 0.1018  0.0082  1322 PRO A N   
2069 C CA  . PRO A 285 ? 0.5062 0.7307 0.8065 -0.0370 0.0853  -0.0014 1322 PRO A CA  
2070 C C   . PRO A 285 ? 0.5243 0.7527 0.8086 -0.0064 0.1015  -0.0071 1322 PRO A C   
2071 O O   . PRO A 285 ? 0.5366 0.7334 0.7907 0.0116  0.0873  -0.0167 1322 PRO A O   
2072 C CB  . PRO A 285 ? 0.5000 0.7795 0.8715 -0.0471 0.0765  0.0036  1322 PRO A CB  
2073 C CG  . PRO A 285 ? 0.5008 0.8065 0.8994 -0.0705 0.0988  0.0183  1322 PRO A CG  
2074 C CD  . PRO A 285 ? 0.5034 0.7536 0.8435 -0.0805 0.1048  0.0203  1322 PRO A CD  
2075 N N   . LYS A 286 ? 0.5348 0.7987 0.8356 -0.0012 0.1312  -0.0009 1323 LYS A N   
2076 C CA  . LYS A 286 ? 0.5625 0.8251 0.8377 0.0294  0.1505  -0.0090 1323 LYS A CA  
2077 C C   . LYS A 286 ? 0.5748 0.7755 0.7760 0.0280  0.1522  -0.0142 1323 LYS A C   
2078 O O   . LYS A 286 ? 0.5677 0.7587 0.7506 0.0079  0.1616  -0.0052 1323 LYS A O   
2079 C CB  . LYS A 286 ? 0.5734 0.8994 0.8865 0.0336  0.1846  0.0000  1323 LYS A CB  
2080 C CG  . LYS A 286 ? 0.6060 0.9541 0.9160 0.0743  0.2033  -0.0118 1323 LYS A CG  
2081 C CD  . LYS A 286 ? 0.6071 0.9956 0.9717 0.0985  0.1891  -0.0187 1323 LYS A CD  
2082 C CE  . LYS A 286 ? 0.6461 1.0597 1.0105 0.1447  0.2095  -0.0320 1323 LYS A CE  
2083 N NZ  . LYS A 286 ? 0.6488 1.1042 1.0703 0.1722  0.1927  -0.0380 1323 LYS A NZ  
2084 N N   . ALA A 287 ? 0.5994 0.7571 0.7590 0.0486  0.1407  -0.0279 1324 ALA A N   
2085 C CA  . ALA A 287 ? 0.6161 0.7153 0.7097 0.0429  0.1350  -0.0334 1324 ALA A CA  
2086 C C   . ALA A 287 ? 0.6445 0.7428 0.7047 0.0506  0.1608  -0.0350 1324 ALA A C   
2087 O O   . ALA A 287 ? 0.6409 0.7148 0.6640 0.0347  0.1614  -0.0316 1324 ALA A O   
2088 C CB  . ALA A 287 ? 0.6426 0.6940 0.7037 0.0585  0.1137  -0.0454 1324 ALA A CB  
2089 N N   . GLU A 288 ? 0.6762 0.8045 0.7489 0.0773  0.1817  -0.0406 1325 GLU A N   
2090 C CA  . GLU A 288 ? 0.7136 0.8432 0.7486 0.0897  0.2082  -0.0442 1325 GLU A CA  
2091 C C   . GLU A 288 ? 0.6946 0.8536 0.7387 0.0641  0.2269  -0.0244 1325 GLU A C   
2092 O O   . GLU A 288 ? 0.7224 0.8651 0.7181 0.0637  0.2403  -0.0235 1325 GLU A O   
2093 C CB  . GLU A 288 ? 0.7504 0.9179 0.8052 0.1267  0.2295  -0.0544 1325 GLU A CB  
2094 C CG  . GLU A 288 ? 0.7280 0.9791 0.8620 0.1232  0.2478  -0.0396 1325 GLU A CG  
2095 C CD  . GLU A 288 ? 0.7584 1.0586 0.9297 0.1630  0.2625  -0.0505 1325 GLU A CD  
2096 O OE1 . GLU A 288 ? 0.8079 1.0680 0.9379 0.1984  0.2578  -0.0719 1325 GLU A OE1 
2097 O OE2 . GLU A 288 ? 0.7419 1.1209 0.9851 0.1589  0.2774  -0.0380 1325 GLU A OE2 
2098 N N   . MET A 289 ? 0.6547 0.8521 0.7574 0.0426  0.2250  -0.0085 1326 MET A N   
2099 C CA  . MET A 289 ? 0.6456 0.8667 0.7621 0.0171  0.2410  0.0128  1326 MET A CA  
2100 C C   . MET A 289 ? 0.6293 0.8011 0.7062 -0.0043 0.2237  0.0179  1326 MET A C   
2101 O O   . MET A 289 ? 0.6331 0.8063 0.7009 -0.0209 0.2347  0.0347  1326 MET A O   
2102 C CB  . MET A 289 ? 0.6223 0.8933 0.8146 -0.0012 0.2394  0.0262  1326 MET A CB  
2103 C CG  . MET A 289 ? 0.6363 0.9781 0.8806 0.0153  0.2634  0.0279  1326 MET A CG  
2104 S SD  . MET A 289 ? 0.6831 1.0649 0.9076 0.0214  0.3110  0.0409  1326 MET A SD  
2105 C CE  . MET A 289 ? 0.6839 1.0317 0.8821 -0.0202 0.3099  0.0665  1326 MET A CE  
2106 N N   . ARG A 290 ? 0.6128 0.7431 0.6670 -0.0033 0.1968  0.0049  1327 ARG A N   
2107 C CA  . ARG A 290 ? 0.6016 0.6952 0.6247 -0.0199 0.1802  0.0076  1327 ARG A CA  
2108 C C   . ARG A 290 ? 0.6324 0.7031 0.5967 -0.0143 0.1889  0.0066  1327 ARG A C   
2109 O O   . ARG A 290 ? 0.6653 0.7306 0.6002 0.0046  0.1990  -0.0045 1327 ARG A O   
2110 C CB  . ARG A 290 ? 0.5842 0.6496 0.6003 -0.0209 0.1529  -0.0047 1327 ARG A CB  
2111 C CG  . ARG A 290 ? 0.5585 0.6418 0.6233 -0.0259 0.1397  -0.0045 1327 ARG A CG  
2112 C CD  . ARG A 290 ? 0.5544 0.6103 0.6039 -0.0225 0.1165  -0.0157 1327 ARG A CD  
2113 N NE  . ARG A 290 ? 0.5393 0.6133 0.6299 -0.0223 0.1034  -0.0162 1327 ARG A NE  
2114 C CZ  . ARG A 290 ? 0.5463 0.6018 0.6288 -0.0160 0.0843  -0.0230 1327 ARG A CZ  
2115 N NH1 . ARG A 290 ? 0.5665 0.5826 0.6029 -0.0130 0.0766  -0.0290 1327 ARG A NH1 
2116 N NH2 . ARG A 290 ? 0.5382 0.6134 0.6574 -0.0145 0.0711  -0.0225 1327 ARG A NH2 
2117 N N   . PRO A 291 ? 0.6290 0.6835 0.5719 -0.0283 0.1829  0.0167  1328 PRO A N   
2118 C CA  . PRO A 291 ? 0.6622 0.6972 0.5486 -0.0237 0.1870  0.0171  1328 PRO A CA  
2119 C C   . PRO A 291 ? 0.6693 0.6725 0.5173 -0.0200 0.1659  -0.0004 1328 PRO A C   
2120 O O   . PRO A 291 ? 0.6425 0.6370 0.5065 -0.0273 0.1466  -0.0068 1328 PRO A O   
2121 C CB  . PRO A 291 ? 0.6574 0.6881 0.5447 -0.0390 0.1829  0.0357  1328 PRO A CB  
2122 C CG  . PRO A 291 ? 0.6168 0.6471 0.5459 -0.0500 0.1647  0.0342  1328 PRO A CG  
2123 C CD  . PRO A 291 ? 0.6009 0.6530 0.5703 -0.0463 0.1696  0.0269  1328 PRO A CD  
2124 N N   . SER A 292 ? 0.7123 0.6984 0.5075 -0.0107 0.1695  -0.0076 1329 SER A N   
2125 C CA  . SER A 292 ? 0.7304 0.6845 0.4863 -0.0123 0.1475  -0.0231 1329 SER A CA  
2126 C C   . SER A 292 ? 0.7170 0.6702 0.4669 -0.0279 0.1294  -0.0146 1329 SER A C   
2127 O O   . SER A 292 ? 0.7078 0.6756 0.4699 -0.0317 0.1353  0.0019  1329 SER A O   
2128 C CB  . SER A 292 ? 0.7902 0.7233 0.4892 0.0029  0.1546  -0.0364 1329 SER A CB  
2129 O OG  . SER A 292 ? 0.8176 0.7600 0.4863 0.0048  0.1677  -0.0243 1329 SER A OG  
2130 N N   . PHE A 293 ? 0.7234 0.6595 0.4552 -0.0367 0.1066  -0.0257 1330 PHE A N   
2131 C CA  . PHE A 293 ? 0.7135 0.6590 0.4452 -0.0492 0.0884  -0.0198 1330 PHE A CA  
2132 C C   . PHE A 293 ? 0.7519 0.6961 0.4439 -0.0440 0.0885  -0.0132 1330 PHE A C   
2133 O O   . PHE A 293 ? 0.7417 0.7005 0.4414 -0.0466 0.0805  -0.0012 1330 PHE A O   
2134 C CB  . PHE A 293 ? 0.7157 0.6506 0.4409 -0.0635 0.0658  -0.0316 1330 PHE A CB  
2135 C CG  . PHE A 293 ? 0.6807 0.6207 0.4436 -0.0713 0.0627  -0.0323 1330 PHE A CG  
2136 C CD1 . PHE A 293 ? 0.6387 0.6062 0.4394 -0.0759 0.0618  -0.0231 1330 PHE A CD1 
2137 C CD2 . PHE A 293 ? 0.6972 0.6102 0.4527 -0.0717 0.0596  -0.0426 1330 PHE A CD2 
2138 C CE1 . PHE A 293 ? 0.6129 0.5846 0.4405 -0.0823 0.0587  -0.0243 1330 PHE A CE1 
2139 C CE2 . PHE A 293 ? 0.6707 0.5864 0.4547 -0.0786 0.0552  -0.0408 1330 PHE A CE2 
2140 C CZ  . PHE A 293 ? 0.6282 0.5751 0.4469 -0.0846 0.0553  -0.0317 1330 PHE A CZ  
2141 N N   . SER A 294 ? 0.8040 0.7289 0.4498 -0.0340 0.0967  -0.0217 1331 SER A N   
2142 C CA  . SER A 294 ? 0.8524 0.7741 0.4514 -0.0269 0.0998  -0.0145 1331 SER A CA  
2143 C C   . SER A 294 ? 0.8482 0.7874 0.4653 -0.0224 0.1207  0.0092  1331 SER A C   
2144 O O   . SER A 294 ? 0.8665 0.8075 0.4648 -0.0223 0.1148  0.0243  1331 SER A O   
2145 C CB  . SER A 294 ? 0.9122 0.8088 0.4552 -0.0143 0.1079  -0.0310 1331 SER A CB  
2146 O OG  . SER A 294 ? 0.9628 0.8560 0.4526 -0.0071 0.1110  -0.0237 1331 SER A OG  
2147 N N   . GLU A 295 ? 0.8298 0.7807 0.4839 -0.0198 0.1430  0.0133  1332 GLU A N   
2148 C CA  . GLU A 295 ? 0.8280 0.7943 0.5048 -0.0215 0.1631  0.0367  1332 GLU A CA  
2149 C C   . GLU A 295 ? 0.7914 0.7601 0.5047 -0.0319 0.1472  0.0491  1332 GLU A C   
2150 O O   . GLU A 295 ? 0.8082 0.7731 0.5170 -0.0340 0.1508  0.0701  1332 GLU A O   
2151 C CB  . GLU A 295 ? 0.8162 0.8017 0.5309 -0.0183 0.1873  0.0355  1332 GLU A CB  
2152 C CG  . GLU A 295 ? 0.8327 0.8379 0.5642 -0.0234 0.2127  0.0604  1332 GLU A CG  
2153 C CD  . GLU A 295 ? 0.8240 0.8612 0.5988 -0.0205 0.2369  0.0595  1332 GLU A CD  
2154 O OE1 . GLU A 295 ? 0.8450 0.8894 0.6022 -0.0032 0.2495  0.0430  1332 GLU A OE1 
2155 O OE2 . GLU A 295 ? 0.8028 0.8576 0.6293 -0.0346 0.2415  0.0744  1332 GLU A OE2 
2156 N N   . LEU A 296 ? 0.7506 0.7224 0.4959 -0.0372 0.1298  0.0362  1333 LEU A N   
2157 C CA  . LEU A 296 ? 0.7232 0.6988 0.5017 -0.0426 0.1158  0.0429  1333 LEU A CA  
2158 C C   . LEU A 296 ? 0.7442 0.7162 0.4961 -0.0383 0.0978  0.0492  1333 LEU A C   
2159 O O   . LEU A 296 ? 0.7521 0.7188 0.5139 -0.0356 0.0934  0.0635  1333 LEU A O   
2160 C CB  . LEU A 296 ? 0.6825 0.6664 0.4929 -0.0481 0.1041  0.0269  1333 LEU A CB  
2161 C CG  . LEU A 296 ? 0.6596 0.6488 0.5064 -0.0509 0.1156  0.0235  1333 LEU A CG  
2162 C CD1 . LEU A 296 ? 0.6264 0.6203 0.4966 -0.0564 0.1011  0.0112  1333 LEU A CD1 
2163 C CD2 . LEU A 296 ? 0.6591 0.6508 0.5339 -0.0544 0.1265  0.0394  1333 LEU A CD2 
2164 N N   . VAL A 297 ? 0.7606 0.7336 0.4793 -0.0374 0.0847  0.0380  1334 VAL A N   
2165 C CA  . VAL A 297 ? 0.7823 0.7600 0.4784 -0.0329 0.0639  0.0427  1334 VAL A CA  
2166 C C   . VAL A 297 ? 0.8265 0.7888 0.4937 -0.0240 0.0710  0.0651  1334 VAL A C   
2167 O O   . VAL A 297 ? 0.8338 0.7959 0.5043 -0.0166 0.0568  0.0770  1334 VAL A O   
2168 C CB  . VAL A 297 ? 0.8051 0.7835 0.4650 -0.0373 0.0482  0.0270  1334 VAL A CB  
2169 C CG1 . VAL A 297 ? 0.8388 0.8248 0.4695 -0.0317 0.0260  0.0338  1334 VAL A CG1 
2170 C CG2 . VAL A 297 ? 0.7694 0.7604 0.4575 -0.0505 0.0368  0.0099  1334 VAL A CG2 
2171 N N   . SER A 298 ? 0.8607 0.8105 0.4989 -0.0235 0.0936  0.0715  1335 SER A N   
2172 C CA  . SER A 298 ? 0.9130 0.8475 0.5164 -0.0188 0.1045  0.0963  1335 SER A CA  
2173 C C   . SER A 298 ? 0.9069 0.8314 0.5463 -0.0220 0.1079  0.1168  1335 SER A C   
2174 O O   . SER A 298 ? 0.9440 0.8497 0.5613 -0.0163 0.0991  0.1374  1335 SER A O   
2175 C CB  . SER A 298 ? 0.9441 0.8770 0.5165 -0.0186 0.1335  0.0980  1335 SER A CB  
2176 O OG  . SER A 298 ? 0.9632 0.8953 0.4961 -0.0132 0.1279  0.0754  1335 SER A OG  
2177 N N   . ARG A 299 ? 0.8677 0.7997 0.5588 -0.0307 0.1179  0.1106  1336 ARG A N   
2178 C CA  . ARG A 299 ? 0.8672 0.7843 0.5923 -0.0368 0.1197  0.1263  1336 ARG A CA  
2179 C C   . ARG A 299 ? 0.8560 0.7630 0.5925 -0.0263 0.0926  0.1240  1336 ARG A C   
2180 O O   . ARG A 299 ? 0.8944 0.7728 0.6218 -0.0218 0.0855  0.1433  1336 ARG A O   
2181 C CB  . ARG A 299 ? 0.8308 0.7619 0.6075 -0.0482 0.1317  0.1158  1336 ARG A CB  
2182 C CG  . ARG A 299 ? 0.8469 0.7951 0.6249 -0.0557 0.1603  0.1198  1336 ARG A CG  
2183 C CD  . ARG A 299 ? 0.8094 0.7767 0.6423 -0.0641 0.1664  0.1081  1336 ARG A CD  
2184 N NE  . ARG A 299 ? 0.8210 0.8148 0.6610 -0.0654 0.1925  0.1078  1336 ARG A NE  
2185 C CZ  . ARG A 299 ? 0.8587 0.8640 0.6996 -0.0741 0.2170  0.1293  1336 ARG A CZ  
2186 N NH1 . ARG A 299 ? 0.8661 0.9049 0.7147 -0.0700 0.2420  0.1256  1336 ARG A NH1 
2187 N NH2 . ARG A 299 ? 0.8922 0.8758 0.7261 -0.0865 0.2168  0.1552  1336 ARG A NH2 
2188 N N   . ILE A 300 ? 0.8096 0.7401 0.5652 -0.0217 0.0779  0.1011  1337 ILE A N   
2189 C CA  . ILE A 300 ? 0.7935 0.7280 0.5701 -0.0097 0.0564  0.0949  1337 ILE A CA  
2190 C C   . ILE A 300 ? 0.8297 0.7625 0.5734 0.0064  0.0375  0.1046  1337 ILE A C   
2191 O O   . ILE A 300 ? 0.8401 0.7669 0.5945 0.0225  0.0210  0.1077  1337 ILE A O   
2192 C CB  . ILE A 300 ? 0.7418 0.7098 0.5488 -0.0131 0.0504  0.0703  1337 ILE A CB  
2193 C CG1 . ILE A 300 ? 0.7087 0.6757 0.5457 -0.0263 0.0653  0.0621  1337 ILE A CG1 
2194 C CG2 . ILE A 300 ? 0.7323 0.7162 0.5599 0.0019  0.0316  0.0631  1337 ILE A CG2 
2195 C CD1 . ILE A 300 ? 0.6685 0.6624 0.5253 -0.0320 0.0609  0.0418  1337 ILE A CD1 
2196 N N   . SER A 301 ? 0.8535 0.7911 0.5554 0.0046  0.0382  0.1080  1338 SER A N   
2197 C CA  . SER A 301 ? 0.8988 0.8342 0.5631 0.0191  0.0182  0.1191  1338 SER A CA  
2198 C C   . SER A 301 ? 0.9504 0.8436 0.5946 0.0287  0.0177  0.1473  1338 SER A C   
2199 O O   . SER A 301 ? 0.9778 0.8645 0.6143 0.0483  -0.0051 0.1558  1338 SER A O   
2200 C CB  . SER A 301 ? 0.9276 0.8686 0.5432 0.0136  0.0197  0.1160  1338 SER A CB  
2201 O OG  . SER A 301 ? 0.8921 0.8636 0.5226 0.0045  0.0130  0.0906  1338 SER A OG  
2202 N N   . ALA A 302 ? 0.9660 0.8314 0.6033 0.0145  0.0423  0.1627  1339 ALA A N   
2203 C CA  . ALA A 302 ? 1.0224 0.8411 0.6395 0.0157  0.0444  0.1933  1339 ALA A CA  
2204 C C   . ALA A 302 ? 1.0123 0.8073 0.6691 0.0240  0.0309  0.1916  1339 ALA A C   
2205 O O   . ALA A 302 ? 1.0694 0.8233 0.7076 0.0376  0.0156  0.2110  1339 ALA A O   
2206 C CB  . ALA A 302 ? 1.0397 0.8473 0.6470 -0.0067 0.0765  0.2095  1339 ALA A CB  
2207 N N   . ILE A 303 ? 0.9486 0.7651 0.6551 0.0174  0.0356  0.1679  1340 ILE A N   
2208 C CA  . ILE A 303 ? 0.9415 0.7366 0.6824 0.0260  0.0240  0.1602  1340 ILE A CA  
2209 C C   . ILE A 303 ? 0.9431 0.7537 0.6872 0.0568  -0.0023 0.1487  1340 ILE A C   
2210 O O   . ILE A 303 ? 0.9813 0.7555 0.7261 0.0764  -0.0182 0.1542  1340 ILE A O   
2211 C CB  . ILE A 303 ? 0.8810 0.6985 0.6671 0.0103  0.0362  0.1378  1340 ILE A CB  
2212 C CG1 . ILE A 303 ? 0.8824 0.6909 0.6740 -0.0174 0.0606  0.1500  1340 ILE A CG1 
2213 C CG2 . ILE A 303 ? 0.8791 0.6773 0.6938 0.0229  0.0219  0.1242  1340 ILE A CG2 
2214 C CD1 . ILE A 303 ? 0.8239 0.6619 0.6565 -0.0311 0.0709  0.1286  1340 ILE A CD1 
2215 N N   . PHE A 304 ? 0.9066 0.7719 0.6543 0.0610  -0.0075 0.1326  1341 PHE A N   
2216 C CA  . PHE A 304 ? 0.9026 0.8024 0.6628 0.0872  -0.0308 0.1211  1341 PHE A CA  
2217 C C   . PHE A 304 ? 0.9747 0.8468 0.6996 0.1113  -0.0516 0.1430  1341 PHE A C   
2218 O O   . PHE A 304 ? 0.9944 0.8683 0.7329 0.1413  -0.0716 0.1395  1341 PHE A O   
2219 C CB  . PHE A 304 ? 0.8551 0.8174 0.6236 0.0775  -0.0323 0.1038  1341 PHE A CB  
2220 C CG  . PHE A 304 ? 0.8486 0.8617 0.6352 0.0993  -0.0558 0.0941  1341 PHE A CG  
2221 C CD1 . PHE A 304 ? 0.8272 0.8651 0.6548 0.1184  -0.0614 0.0794  1341 PHE A CD1 
2222 C CD2 . PHE A 304 ? 0.8681 0.9088 0.6312 0.1013  -0.0727 0.0986  1341 PHE A CD2 
2223 C CE1 . PHE A 304 ? 0.8220 0.9192 0.6730 0.1395  -0.0806 0.0710  1341 PHE A CE1 
2224 C CE2 . PHE A 304 ? 0.8627 0.9605 0.6506 0.1196  -0.0958 0.0904  1341 PHE A CE2 
2225 C CZ  . PHE A 304 ? 0.8373 0.9673 0.6723 0.1389  -0.0984 0.0773  1341 PHE A CZ  
2226 N N   . SER A 305 ? 1.0200 0.8666 0.6969 0.1003  -0.0465 0.1656  1342 SER A N   
2227 C CA  . SER A 305 ? 1.0932 0.9133 0.7261 0.1210  -0.0672 0.1894  1342 SER A CA  
2228 C C   . SER A 305 ? 1.1588 0.9047 0.7777 0.1316  -0.0716 0.2129  1342 SER A C   
2229 O O   . SER A 305 ? 1.2273 0.9408 0.8108 0.1539  -0.0929 0.2343  1342 SER A O   
2230 C CB  . SER A 305 ? 1.1227 0.9425 0.7018 0.1053  -0.0593 0.2041  1342 SER A CB  
2231 O OG  . SER A 305 ? 1.1275 0.9181 0.6934 0.0780  -0.0282 0.2156  1342 SER A OG  
2232 N N   . THR A 306 ? 1.1454 0.8607 0.7900 0.1149  -0.0545 0.2094  1343 THR A N   
2233 C CA  . THR A 306 ? 1.2137 0.8515 0.8479 0.1197  -0.0607 0.2290  1343 THR A CA  
2234 C C   . THR A 306 ? 1.2072 0.8386 0.8804 0.1469  -0.0772 0.2048  1343 THR A C   
2235 O O   . THR A 306 ? 1.2314 0.8079 0.9144 0.1407  -0.0758 0.2052  1343 THR A O   
2236 C CB  . THR A 306 ? 1.2179 0.8221 0.8514 0.0801  -0.0334 0.2438  1343 THR A CB  
2237 O OG1 . THR A 306 ? 1.1375 0.7843 0.8196 0.0637  -0.0174 0.2148  1343 THR A OG1 
2238 C CG2 . THR A 306 ? 1.2425 0.8510 0.8324 0.0577  -0.0141 0.2697  1343 THR A CG2 
2239 N N   . PHE A 307 ? 1.1808 0.8705 0.8754 0.1767  -0.0931 0.1834  1344 PHE A N   
2240 C CA  . PHE A 307 ? 1.1816 0.8764 0.9095 0.2104  -0.1079 0.1596  1344 PHE A CA  
2241 C C   . PHE A 307 ? 1.2216 0.9405 0.9437 0.2548  -0.1364 0.1618  1344 PHE A C   
2242 O O   . PHE A 307 ? 1.2080 0.9787 0.9208 0.2539  -0.1426 0.1674  1344 PHE A O   
2243 C CB  . PHE A 307 ? 1.0938 0.8573 0.8695 0.1998  -0.0926 0.1259  1344 PHE A CB  
2244 C CG  . PHE A 307 ? 1.0768 0.8048 0.8688 0.1781  -0.0769 0.1148  1344 PHE A CG  
2245 C CD1 . PHE A 307 ? 1.0677 0.7697 0.8499 0.1375  -0.0575 0.1290  1344 PHE A CD1 
2246 C CD2 . PHE A 307 ? 1.0750 0.7983 0.8916 0.1999  -0.0825 0.0893  1344 PHE A CD2 
2247 C CE1 . PHE A 307 ? 1.0557 0.7305 0.8571 0.1169  -0.0469 0.1189  1344 PHE A CE1 
2248 C CE2 . PHE A 307 ? 1.0669 0.7558 0.8947 0.1793  -0.0722 0.0779  1344 PHE A CE2 
2249 C CZ  . PHE A 307 ? 1.0565 0.7221 0.8788 0.1368  -0.0560 0.0933  1344 PHE A CZ  
2250 N N   . ILE A 308 ? 1.2781 0.9589 1.0059 0.2950  -0.1555 0.1556  1345 ILE A N   
2251 C CA  . ILE A 308 ? 1.3274 1.0256 1.0525 0.3445  -0.1853 0.1586  1345 ILE A CA  
2252 C C   . ILE A 308 ? 1.2629 1.0674 1.0440 0.3663  -0.1857 0.1251  1345 ILE A C   
2253 O O   . ILE A 308 ? 1.2246 1.0468 1.0389 0.3670  -0.1717 0.0982  1345 ILE A O   
2254 C CB  . ILE A 308 ? 1.4269 1.0270 1.1280 0.3820  -0.2070 0.1682  1345 ILE A CB  
2255 C CG1 . ILE A 308 ? 1.5019 0.9956 1.1464 0.3545  -0.2065 0.2068  1345 ILE A CG1 
2256 C CG2 . ILE A 308 ? 1.4720 1.0983 1.1773 0.4414  -0.2393 0.1676  1345 ILE A CG2 
2257 C CD1 . ILE A 308 ? 1.4818 0.9300 1.1295 0.3076  -0.1807 0.2053  1345 ILE A CD1 
2258 N N   . GLY A 309 ? 1.2559 1.1327 1.0460 0.3823  -0.2025 0.1282  1346 GLY A N   
2259 C CA  . GLY A 309 ? 1.1975 1.1863 1.0443 0.3991  -0.2040 0.1015  1346 GLY A CA  
2260 C C   . GLY A 309 ? 1.1699 1.2368 1.0208 0.3842  -0.2152 0.1089  1346 GLY A C   
2261 O O   . GLY A 309 ? 1.2238 1.2971 1.0612 0.4156  -0.2448 0.1237  1346 GLY A O   
2262 O OXT . GLY A 309 ? 1.1008 1.2157 0.9659 0.3421  -0.1965 0.0993  1346 GLY A OXT 
2263 N N   . THR B 13  ? 1.1537 2.0021 2.0782 0.0889  -0.2989 0.0064  1050 THR B N   
2264 C CA  . THR B 13  ? 1.1387 1.9305 1.9165 0.0813  -0.2487 0.0250  1050 THR B CA  
2265 C C   . THR B 13  ? 1.0947 1.9057 1.9159 0.0599  -0.1686 0.0424  1050 THR B C   
2266 O O   . THR B 13  ? 1.0779 1.9379 2.0333 0.0477  -0.1460 0.0402  1050 THR B O   
2267 C CB  . THR B 13  ? 1.1641 1.9033 1.8454 0.0680  -0.2785 0.0146  1050 THR B CB  
2268 O OG1 . THR B 13  ? 1.1496 1.9190 1.9245 0.0377  -0.2817 0.0020  1050 THR B OG1 
2269 C CG2 . THR B 13  ? 1.2348 1.9274 1.8387 0.0949  -0.3523 -0.0008 1050 THR B CG2 
2270 N N   . VAL B 14  ? 1.0871 1.8509 1.7930 0.0573  -0.1264 0.0591  1051 VAL B N   
2271 C CA  . VAL B 14  ? 1.0656 1.8227 1.7743 0.0449  -0.0562 0.0760  1051 VAL B CA  
2272 C C   . VAL B 14  ? 1.0552 1.7944 1.7487 0.0150  -0.0409 0.0730  1051 VAL B C   
2273 O O   . VAL B 14  ? 1.0566 1.7538 1.6513 0.0093  -0.0516 0.0733  1051 VAL B O   
2274 C CB  . VAL B 14  ? 1.0705 1.7813 1.6674 0.0615  -0.0285 0.0932  1051 VAL B CB  
2275 C CG1 . VAL B 14  ? 1.0692 1.7540 1.6482 0.0538  0.0354  0.1088  1051 VAL B CG1 
2276 C CG2 . VAL B 14  ? 1.0852 1.8075 1.6871 0.0922  -0.0435 0.0964  1051 VAL B CG2 
2277 N N   . HIS B 15  ? 1.0467 1.8154 1.8441 -0.0030 -0.0111 0.0709  1052 HIS B N   
2278 C CA  . HIS B 15  ? 1.0419 1.7908 1.8300 -0.0305 0.0110  0.0693  1052 HIS B CA  
2279 C C   . HIS B 15  ? 1.0496 1.7490 1.7631 -0.0303 0.0750  0.0890  1052 HIS B C   
2280 O O   . HIS B 15  ? 1.0618 1.7604 1.8223 -0.0264 0.1287  0.0999  1052 HIS B O   
2281 C CB  . HIS B 15  ? 1.0392 1.8350 1.9760 -0.0502 0.0152  0.0570  1052 HIS B CB  
2282 C CG  . HIS B 15  ? 1.0428 1.8775 2.0521 -0.0515 -0.0603 0.0330  1052 HIS B CG  
2283 N ND1 . HIS B 15  ? 1.0561 1.8627 1.9870 -0.0558 -0.1171 0.0191  1052 HIS B ND1 
2284 C CD2 . HIS B 15  ? 1.0454 1.9379 2.2002 -0.0462 -0.0900 0.0197  1052 HIS B CD2 
2285 C CE1 . HIS B 15  ? 1.0779 1.9143 2.0861 -0.0518 -0.1840 -0.0028 1052 HIS B CE1 
2286 N NE2 . HIS B 15  ? 1.0678 1.9628 2.2238 -0.0465 -0.1727 -0.0039 1052 HIS B NE2 
2287 N N   . ILE B 16  ? 1.0534 1.7043 1.6500 -0.0321 0.0681  0.0931  1053 ILE B N   
2288 C CA  . ILE B 16  ? 1.0763 1.6695 1.5894 -0.0290 0.1116  0.1082  1053 ILE B CA  
2289 C C   . ILE B 16  ? 1.0879 1.6559 1.5937 -0.0513 0.1324  0.1066  1053 ILE B C   
2290 O O   . ILE B 16  ? 1.0737 1.6476 1.5731 -0.0666 0.1009  0.0959  1053 ILE B O   
2291 C CB  . ILE B 16  ? 1.0765 1.6327 1.4838 -0.0160 0.0884  0.1126  1053 ILE B CB  
2292 C CG1 . ILE B 16  ? 1.0731 1.6494 1.4825 0.0060  0.0679  0.1137  1053 ILE B CG1 
2293 C CG2 . ILE B 16  ? 1.1050 1.5962 1.4298 -0.0108 0.1203  0.1246  1053 ILE B CG2 
2294 C CD1 . ILE B 16  ? 1.0725 1.6140 1.3937 0.0165  0.0473  0.1167  1053 ILE B CD1 
2295 N N   . ASP B 17  ? 1.1254 1.6546 1.6217 -0.0501 0.1887  0.1180  1054 ASP B N   
2296 C CA  . ASP B 17  ? 1.1512 1.6394 1.6208 -0.0663 0.2155  0.1191  1054 ASP B CA  
2297 C C   . ASP B 17  ? 1.1610 1.5889 1.5069 -0.0598 0.1987  0.1234  1054 ASP B C   
2298 O O   . ASP B 17  ? 1.2048 1.5675 1.4712 -0.0434 0.2241  0.1346  1054 ASP B O   
2299 C CB  . ASP B 17  ? 1.2060 1.6594 1.7012 -0.0631 0.2876  0.1308  1054 ASP B CB  
2300 C CG  . ASP B 17  ? 1.2434 1.6490 1.7145 -0.0790 0.3212  0.1321  1054 ASP B CG  
2301 O OD1 . ASP B 17  ? 1.2156 1.6622 1.7598 -0.1035 0.3053  0.1197  1054 ASP B OD1 
2302 O OD2 . ASP B 17  ? 1.3104 1.6298 1.6819 -0.0648 0.3608  0.1449  1054 ASP B OD2 
2303 N N   . LEU B 18  ? 1.1275 1.5717 1.4600 -0.0710 0.1546  0.1137  1055 LEU B N   
2304 C CA  . LEU B 18  ? 1.1282 1.5295 1.3728 -0.0649 0.1324  0.1160  1055 LEU B CA  
2305 C C   . LEU B 18  ? 1.1614 1.5005 1.3495 -0.0688 0.1546  0.1203  1055 LEU B C   
2306 O O   . LEU B 18  ? 1.1752 1.4716 1.2966 -0.0609 0.1364  0.1222  1055 LEU B O   
2307 C CB  . LEU B 18  ? 1.0933 1.5255 1.3472 -0.0733 0.0893  0.1060  1055 LEU B CB  
2308 C CG  . LEU B 18  ? 1.0905 1.5288 1.3632 -0.0947 0.0813  0.0969  1055 LEU B CG  
2309 C CD1 . LEU B 18  ? 1.0986 1.5643 1.4472 -0.1103 0.1013  0.0912  1055 LEU B CD1 
2310 C CD2 . LEU B 18  ? 1.1070 1.4941 1.3199 -0.0979 0.0881  0.1010  1055 LEU B CD2 
2311 N N   . SER B 19  ? 1.1758 1.5058 1.3946 -0.0794 0.1941  0.1217  1056 SER B N   
2312 C CA  . SER B 19  ? 1.2168 1.4772 1.3733 -0.0804 0.2201  0.1266  1056 SER B CA  
2313 C C   . SER B 19  ? 1.2829 1.4623 1.3602 -0.0560 0.2578  0.1395  1056 SER B C   
2314 O O   . SER B 19  ? 1.3471 1.4495 1.3555 -0.0504 0.2850  0.1450  1056 SER B O   
2315 C CB  . SER B 19  ? 1.2193 1.4976 1.4407 -0.1037 0.2482  0.1217  1056 SER B CB  
2316 O OG  . SER B 19  ? 1.2269 1.5342 1.5315 -0.1065 0.2878  0.1240  1056 SER B OG  
2317 N N   . ALA B 20  ? 1.2735 1.4591 1.3480 -0.0387 0.2592  0.1445  1057 ALA B N   
2318 C CA  . ALA B 20  ? 1.3520 1.4521 1.3443 -0.0126 0.2978  0.1569  1057 ALA B CA  
2319 C C   . ALA B 20  ? 1.3840 1.4137 1.2626 0.0086  0.2570  0.1570  1057 ALA B C   
2320 O O   . ALA B 20  ? 1.4740 1.4069 1.2526 0.0338  0.2781  0.1652  1057 ALA B O   
2321 C CB  . ALA B 20  ? 1.3409 1.4801 1.3934 -0.0042 0.3235  0.1622  1057 ALA B CB  
2322 N N   . LEU B 21  ? 1.3159 1.3868 1.2108 -0.0001 0.1994  0.1474  1058 LEU B N   
2323 C CA  . LEU B 21  ? 1.3389 1.3584 1.1603 0.0168  0.1541  0.1447  1058 LEU B CA  
2324 C C   . LEU B 21  ? 1.4181 1.3413 1.1466 0.0281  0.1476  0.1448  1058 LEU B C   
2325 O O   . LEU B 21  ? 1.4281 1.3434 1.1612 0.0167  0.1703  0.1454  1058 LEU B O   
2326 C CB  . LEU B 21  ? 1.2520 1.3438 1.1365 0.0030  0.1062  0.1357  1058 LEU B CB  
2327 C CG  . LEU B 21  ? 1.2032 1.3531 1.1348 0.0050  0.0973  0.1355  1058 LEU B CG  
2328 C CD1 . LEU B 21  ? 1.1675 1.3841 1.1734 -0.0060 0.1279  0.1370  1058 LEU B CD1 
2329 C CD2 . LEU B 21  ? 1.1465 1.3354 1.1142 -0.0026 0.0563  0.1285  1058 LEU B CD2 
2330 N N   . ASN B 22  ? 1.4818 1.3272 1.1247 0.0518  0.1118  0.1427  1059 ASN B N   
2331 C CA  . ASN B 22  ? 1.5801 1.3176 1.1196 0.0705  0.0913  0.1407  1059 ASN B CA  
2332 C C   . ASN B 22  ? 1.5236 1.3016 1.1156 0.0543  0.0504  0.1316  1059 ASN B C   
2333 O O   . ASN B 22  ? 1.4483 1.2899 1.1118 0.0443  0.0103  0.1244  1059 ASN B O   
2334 C CB  . ASN B 22  ? 1.6682 1.3121 1.1101 0.1012  0.0514  0.1374  1059 ASN B CB  
2335 C CG  . ASN B 22  ? 1.7956 1.3065 1.1107 0.1282  0.0211  0.1335  1059 ASN B CG  
2336 O OD1 . ASN B 22  ? 1.8300 1.3070 1.1151 0.1269  0.0411  0.1361  1059 ASN B OD1 
2337 N ND2 . ASN B 22  ? 1.8746 1.3012 1.1091 0.1547  -0.0307 0.1261  1059 ASN B ND2 
2338 N N   . PRO B 23  ? 1.5616 1.3004 1.1215 0.0521  0.0649  0.1328  1060 PRO B N   
2339 C CA  . PRO B 23  ? 1.5173 1.2853 1.1216 0.0401  0.0287  0.1252  1060 PRO B CA  
2340 C C   . PRO B 23  ? 1.5215 1.2687 1.1271 0.0539  -0.0422 0.1151  1060 PRO B C   
2341 O O   . PRO B 23  ? 1.4445 1.2588 1.1396 0.0385  -0.0680 0.1095  1060 PRO B O   
2342 C CB  . PRO B 23  ? 1.6017 1.2884 1.1280 0.0477  0.0540  0.1291  1060 PRO B CB  
2343 C CG  . PRO B 23  ? 1.7080 1.3031 1.1325 0.0686  0.1030  0.1390  1060 PRO B CG  
2344 C CD  . PRO B 23  ? 1.6511 1.3141 1.1354 0.0608  0.1245  0.1425  1060 PRO B CD  
2345 N N   . GLU B 24  ? 1.6198 1.2674 1.1279 0.0840  -0.0725 0.1124  1061 GLU B N   
2346 C CA  . GLU B 24  ? 1.6340 1.2553 1.1517 0.0982  -0.1473 0.0998  1061 GLU B CA  
2347 C C   . GLU B 24  ? 1.5306 1.2471 1.1569 0.0816  -0.1594 0.0967  1061 GLU B C   
2348 O O   . GLU B 24  ? 1.4785 1.2361 1.1921 0.0743  -0.2008 0.0882  1061 GLU B O   
2349 C CB  . GLU B 24  ? 1.7805 1.2614 1.1557 0.1361  -0.1806 0.0958  1061 GLU B CB  
2350 C CG  . GLU B 24  ? 1.8988 1.2640 1.1650 0.1609  -0.2014 0.0932  1061 GLU B CG  
2351 C CD  . GLU B 24  ? 1.9410 1.2715 1.1396 0.1589  -0.1260 0.1072  1061 GLU B CD  
2352 O OE1 . GLU B 24  ? 2.0342 1.2736 1.1469 0.1777  -0.1372 0.1061  1061 GLU B OE1 
2353 O OE2 . GLU B 24  ? 1.8853 1.2763 1.1209 0.1397  -0.0571 0.1185  1061 GLU B OE2 
2354 N N   . LEU B 25  ? 1.5065 1.2520 1.1287 0.0775  -0.1196 0.1043  1062 LEU B N   
2355 C CA  . LEU B 25  ? 1.4177 1.2470 1.1294 0.0637  -0.1226 0.1032  1062 LEU B CA  
2356 C C   . LEU B 25  ? 1.3084 1.2401 1.1297 0.0357  -0.1046 0.1045  1062 LEU B C   
2357 O O   . LEU B 25  ? 1.2520 1.2320 1.1532 0.0270  -0.1250 0.1001  1062 LEU B O   
2358 C CB  . LEU B 25  ? 1.4278 1.2604 1.1046 0.0685  -0.0804 0.1120  1062 LEU B CB  
2359 C CG  . LEU B 25  ? 1.3485 1.2603 1.1030 0.0576  -0.0784 0.1123  1062 LEU B CG  
2360 C CD1 . LEU B 25  ? 1.3757 1.2512 1.1264 0.0702  -0.1299 0.1032  1062 LEU B CD1 
2361 C CD2 . LEU B 25  ? 1.3477 1.2790 1.0861 0.0600  -0.0288 0.1224  1062 LEU B CD2 
2362 N N   . VAL B 26  ? 1.2902 1.2443 1.1103 0.0230  -0.0640 0.1103  1063 VAL B N   
2363 C CA  . VAL B 26  ? 1.2071 1.2423 1.1097 -0.0012 -0.0462 0.1109  1063 VAL B CA  
2364 C C   . VAL B 26  ? 1.1890 1.2263 1.1382 -0.0042 -0.0788 0.1050  1063 VAL B C   
2365 O O   . VAL B 26  ? 1.1277 1.2207 1.1516 -0.0168 -0.0772 0.1044  1063 VAL B O   
2366 C CB  . VAL B 26  ? 1.2093 1.2550 1.0989 -0.0136 -0.0025 0.1158  1063 VAL B CB  
2367 C CG1 . VAL B 26  ? 1.1448 1.2529 1.1016 -0.0362 0.0060  0.1138  1063 VAL B CG1 
2368 C CG2 . VAL B 26  ? 1.2151 1.2758 1.0952 -0.0132 0.0345  0.1216  1063 VAL B CG2 
2369 N N   . GLN B 27  ? 1.2524 1.2212 1.1548 0.0101  -0.1064 0.1012  1064 GLN B N   
2370 C CA  . GLN B 27  ? 1.2412 1.2088 1.1960 0.0100  -0.1386 0.0955  1064 GLN B CA  
2371 C C   . GLN B 27  ? 1.2206 1.1974 1.2434 0.0161  -0.1810 0.0881  1064 GLN B C   
2372 O O   . GLN B 27  ? 1.1870 1.1924 1.2984 0.0101  -0.1942 0.0851  1064 GLN B O   
2373 C CB  . GLN B 27  ? 1.3274 1.2111 1.2058 0.0279  -0.1609 0.0927  1064 GLN B CB  
2374 C CG  . GLN B 27  ? 1.3166 1.2043 1.2558 0.0275  -0.1884 0.0878  1064 GLN B CG  
2375 C CD  . GLN B 27  ? 1.4051 1.2094 1.2590 0.0455  -0.2039 0.0864  1064 GLN B CD  
2376 O OE1 . GLN B 27  ? 1.4660 1.2135 1.3118 0.0672  -0.2612 0.0773  1064 GLN B OE1 
2377 N NE2 . GLN B 27  ? 1.4206 1.2124 1.2124 0.0376  -0.1546 0.0944  1064 GLN B NE2 
2378 N N   . ALA B 28  ? 1.2427 1.1921 1.2286 0.0281  -0.1979 0.0856  1065 ALA B N   
2379 C CA  . ALA B 28  ? 1.2255 1.1787 1.2756 0.0328  -0.2377 0.0774  1065 ALA B CA  
2380 C C   . ALA B 28  ? 1.1380 1.1660 1.2584 0.0161  -0.2022 0.0831  1065 ALA B C   
2381 O O   . ALA B 28  ? 1.1249 1.1601 1.3023 0.0174  -0.2227 0.0781  1065 ALA B O   
2382 C CB  . ALA B 28  ? 1.3124 1.1847 1.2733 0.0560  -0.2756 0.0709  1065 ALA B CB  
2383 N N   . VAL B 29  ? 1.0829 1.1592 1.1969 0.0018  -0.1516 0.0926  1066 VAL B N   
2384 C CA  . VAL B 29  ? 1.0215 1.1534 1.1726 -0.0085 -0.1194 0.0981  1066 VAL B CA  
2385 C C   . VAL B 29  ? 0.9697 1.1448 1.1654 -0.0241 -0.0873 0.1028  1066 VAL B C   
2386 O O   . VAL B 29  ? 0.9394 1.1501 1.1436 -0.0309 -0.0585 0.1074  1066 VAL B O   
2387 C CB  . VAL B 29  ? 1.0338 1.1667 1.1165 -0.0042 -0.0980 0.1031  1066 VAL B CB  
2388 C CG1 . VAL B 29  ? 0.9860 1.1764 1.0923 -0.0139 -0.0637 0.1088  1066 VAL B CG1 
2389 C CG2 . VAL B 29  ? 1.0798 1.1663 1.1220 0.0128  -0.1245 0.0995  1066 VAL B CG2 
2390 N N   . GLN B 30  ? 0.9682 1.1310 1.1873 -0.0268 -0.0952 0.1009  1067 GLN B N   
2391 C CA  . GLN B 30  ? 0.9359 1.1245 1.1804 -0.0394 -0.0641 0.1052  1067 GLN B CA  
2392 C C   . GLN B 30  ? 0.9018 1.1106 1.2197 -0.0426 -0.0454 0.1083  1067 GLN B C   
2393 O O   . GLN B 30  ? 0.8866 1.1105 1.1999 -0.0497 -0.0111 0.1135  1067 GLN B O   
2394 C CB  . GLN B 30  ? 0.9589 1.1220 1.2059 -0.0386 -0.0766 0.1030  1067 GLN B CB  
2395 C CG  . GLN B 30  ? 0.9970 1.1313 1.1603 -0.0368 -0.0776 0.1026  1067 GLN B CG  
2396 C CD  . GLN B 30  ? 0.9796 1.1409 1.1128 -0.0519 -0.0393 0.1066  1067 GLN B CD  
2397 O OE1 . GLN B 30  ? 1.0074 1.1500 1.0864 -0.0534 -0.0293 0.1070  1067 GLN B OE1 
2398 N NE2 . GLN B 30  ? 0.9424 1.1402 1.1098 -0.0621 -0.0175 0.1088  1067 GLN B NE2 
2399 N N   . HIS B 31  ? 0.8973 1.0968 1.2802 -0.0359 -0.0673 0.1047  1068 HIS B N   
2400 C CA  . HIS B 31  ? 0.8750 1.0845 1.3419 -0.0381 -0.0420 0.1086  1068 HIS B CA  
2401 C C   . HIS B 31  ? 0.8589 1.0799 1.3004 -0.0376 -0.0148 0.1137  1068 HIS B C   
2402 O O   . HIS B 31  ? 0.8559 1.0752 1.3289 -0.0384 0.0244  0.1205  1068 HIS B O   
2403 C CB  . HIS B 31  ? 0.8839 1.0810 1.4510 -0.0327 -0.0769 0.1011  1068 HIS B CB  
2404 C CG  . HIS B 31  ? 0.9056 1.0855 1.4577 -0.0246 -0.1236 0.0918  1068 HIS B CG  
2405 N ND1 . HIS B 31  ? 0.9419 1.0913 1.4137 -0.0153 -0.1662 0.0849  1068 HIS B ND1 
2406 C CD2 . HIS B 31  ? 0.9067 1.0856 1.5111 -0.0230 -0.1309 0.0886  1068 HIS B CD2 
2407 C CE1 . HIS B 31  ? 0.9676 1.0941 1.4334 -0.0070 -0.2008 0.0774  1068 HIS B CE1 
2408 N NE2 . HIS B 31  ? 0.9425 1.0911 1.4949 -0.0131 -0.1818 0.0788  1068 HIS B NE2 
2409 N N   . VAL B 32  ? 0.8549 1.0789 1.2337 -0.0334 -0.0323 0.1113  1069 VAL B N   
2410 C CA  . VAL B 32  ? 0.8447 1.0774 1.1994 -0.0296 -0.0134 0.1153  1069 VAL B CA  
2411 C C   . VAL B 32  ? 0.8350 1.0840 1.1202 -0.0316 0.0089  0.1194  1069 VAL B C   
2412 O O   . VAL B 32  ? 0.8398 1.0907 1.1044 -0.0265 0.0292  0.1235  1069 VAL B O   
2413 C CB  . VAL B 32  ? 0.8569 1.0800 1.1922 -0.0214 -0.0441 0.1104  1069 VAL B CB  
2414 C CG1 . VAL B 32  ? 0.8711 1.0723 1.2805 -0.0190 -0.0761 0.1028  1069 VAL B CG1 
2415 C CG2 . VAL B 32  ? 0.8719 1.0888 1.1316 -0.0179 -0.0630 0.1080  1069 VAL B CG2 
2416 N N   . VAL B 33  ? 0.8261 1.0820 1.0764 -0.0377 0.0026  0.1173  1070 VAL B N   
2417 C CA  . VAL B 33  ? 0.8201 1.0929 1.0222 -0.0416 0.0162  0.1180  1070 VAL B CA  
2418 C C   . VAL B 33  ? 0.8270 1.0874 1.0288 -0.0441 0.0418  0.1210  1070 VAL B C   
2419 O O   . VAL B 33  ? 0.8332 1.0747 1.0753 -0.0450 0.0550  0.1238  1070 VAL B O   
2420 C CB  . VAL B 33  ? 0.8209 1.1010 0.9946 -0.0490 0.0068  0.1145  1070 VAL B CB  
2421 C CG1 . VAL B 33  ? 0.8295 1.1060 0.9805 -0.0418 -0.0075 0.1137  1070 VAL B CG1 
2422 C CG2 . VAL B 33  ? 0.8266 1.0888 1.0149 -0.0556 0.0043  0.1134  1070 VAL B CG2 
2423 N N   . ILE B 34  ? 0.8353 1.1003 0.9910 -0.0432 0.0474  0.1196  1071 ILE B N   
2424 C CA  . ILE B 34  ? 0.8670 1.1014 0.9927 -0.0407 0.0685  0.1213  1071 ILE B CA  
2425 C C   . ILE B 34  ? 0.8741 1.1123 0.9726 -0.0521 0.0602  0.1149  1071 ILE B C   
2426 O O   . ILE B 34  ? 0.8899 1.1031 0.9869 -0.0571 0.0748  0.1163  1071 ILE B O   
2427 C CB  . ILE B 34  ? 0.8983 1.1152 0.9801 -0.0252 0.0745  0.1229  1071 ILE B CB  
2428 C CG1 . ILE B 34  ? 0.9166 1.0983 1.0172 -0.0140 0.1053  0.1319  1071 ILE B CG1 
2429 C CG2 . ILE B 34  ? 0.9485 1.1358 0.9639 -0.0209 0.0726  0.1182  1071 ILE B CG2 
2430 C CD1 . ILE B 34  ? 0.8775 1.0819 1.0486 -0.0176 0.0984  0.1334  1071 ILE B CD1 
2431 N N   . GLY B 35  ? 0.8646 1.1332 0.9496 -0.0563 0.0388  0.1079  1072 GLY B N   
2432 C CA  . GLY B 35  ? 0.8785 1.1500 0.9449 -0.0676 0.0288  0.0995  1072 GLY B CA  
2433 C C   . GLY B 35  ? 0.9282 1.1708 0.9428 -0.0579 0.0201  0.0939  1072 GLY B C   
2434 O O   . GLY B 35  ? 0.9703 1.1602 0.9438 -0.0481 0.0385  0.0982  1072 GLY B O   
2435 N N   . PRO B 36  ? 0.9352 1.2031 0.9491 -0.0576 -0.0083 0.0838  1073 PRO B N   
2436 C CA  . PRO B 36  ? 0.9981 1.2308 0.9558 -0.0426 -0.0300 0.0759  1073 PRO B CA  
2437 C C   . PRO B 36  ? 1.0709 1.2325 0.9576 -0.0389 -0.0263 0.0724  1073 PRO B C   
2438 O O   . PRO B 36  ? 1.1443 1.2469 0.9561 -0.0180 -0.0352 0.0699  1073 PRO B O   
2439 C CB  . PRO B 36  ? 0.9863 1.2681 0.9873 -0.0513 -0.0666 0.0621  1073 PRO B CB  
2440 C CG  . PRO B 36  ? 0.9187 1.2591 0.9889 -0.0604 -0.0521 0.0689  1073 PRO B CG  
2441 C CD  . PRO B 36  ? 0.8947 1.2196 0.9643 -0.0689 -0.0206 0.0794  1073 PRO B CD  
2442 N N   . SER B 37  ? 1.0631 1.2199 0.9623 -0.0564 -0.0125 0.0723  1074 SER B N   
2443 C CA  . SER B 37  ? 1.1360 1.2204 0.9654 -0.0535 -0.0050 0.0694  1074 SER B CA  
2444 C C   . SER B 37  ? 1.1827 1.1996 0.9619 -0.0339 0.0388  0.0843  1074 SER B C   
2445 O O   . SER B 37  ? 1.2741 1.2061 0.9630 -0.0182 0.0470  0.0833  1074 SER B O   
2446 C CB  . SER B 37  ? 1.1107 1.2091 0.9712 -0.0765 0.0021  0.0668  1074 SER B CB  
2447 O OG  . SER B 37  ? 1.0503 1.1769 0.9653 -0.0831 0.0333  0.0798  1074 SER B OG  
2448 N N   . SER B 38  ? 1.1310 1.1785 0.9694 -0.0338 0.0678  0.0975  1075 SER B N   
2449 C CA  . SER B 38  ? 1.1652 1.1589 0.9915 -0.0195 0.1168  0.1122  1075 SER B CA  
2450 C C   . SER B 38  ? 1.2223 1.1722 0.9947 0.0050  0.1264  0.1168  1075 SER B C   
2451 O O   . SER B 38  ? 1.2777 1.1587 1.0176 0.0211  0.1738  0.1287  1075 SER B O   
2452 C CB  . SER B 38  ? 1.0887 1.1308 1.0135 -0.0304 0.1357  0.1212  1075 SER B CB  
2453 O OG  . SER B 38  ? 1.0581 1.1225 1.0173 -0.0480 0.1309  0.1183  1075 SER B OG  
2454 N N   . LEU B 39  ? 1.0641 0.7392 0.9087 -0.1431 -0.1129 -0.0871 1076 LEU B N   
2455 C CA  . LEU B 39  ? 1.0090 0.7427 0.9136 -0.1512 -0.0935 -0.0847 1076 LEU B CA  
2456 C C   . LEU B 39  ? 1.0241 0.7381 0.8975 -0.1760 -0.0950 -0.0728 1076 LEU B C   
2457 O O   . LEU B 39  ? 1.0381 0.7353 0.8889 -0.2028 -0.1116 -0.0627 1076 LEU B O   
2458 C CB  . LEU B 39  ? 0.9566 0.7436 0.9152 -0.1594 -0.0953 -0.0843 1076 LEU B CB  
2459 C CG  . LEU B 39  ? 0.8996 0.7447 0.9205 -0.1668 -0.0778 -0.0827 1076 LEU B CG  
2460 C CD1 . LEU B 39  ? 0.8940 0.7397 0.8982 -0.1928 -0.0753 -0.0685 1076 LEU B CD1 
2461 C CD2 . LEU B 39  ? 0.8918 0.7552 0.9531 -0.1467 -0.0558 -0.0916 1076 LEU B CD2 
2462 N N   . ILE B 40  ? 1.0296 0.7443 0.9043 -0.1655 -0.0773 -0.0740 1077 ILE B N   
2463 C CA  . ILE B 40  ? 1.0578 0.7465 0.8963 -0.1806 -0.0839 -0.0665 1077 ILE B CA  
2464 C C   . ILE B 40  ? 1.0082 0.7511 0.8983 -0.1859 -0.0658 -0.0626 1077 ILE B C   
2465 O O   . ILE B 40  ? 0.9892 0.7544 0.9113 -0.1670 -0.0373 -0.0664 1077 ILE B O   
2466 C CB  . ILE B 40  ? 1.1358 0.7531 0.9012 -0.1565 -0.0801 -0.0708 1077 ILE B CB  
2467 C CG1 . ILE B 40  ? 1.2004 0.7556 0.9069 -0.1469 -0.0989 -0.0758 1077 ILE B CG1 
2468 C CG2 . ILE B 40  ? 1.1747 0.7542 0.8928 -0.1671 -0.0949 -0.0661 1077 ILE B CG2 
2469 C CD1 . ILE B 40  ? 1.2840 0.7670 0.9152 -0.1123 -0.0899 -0.0816 1077 ILE B CD1 
2470 N N   . VAL B 41  ? 0.9944 0.7577 0.8957 -0.2115 -0.0815 -0.0544 1078 VAL B N   
2471 C CA  . VAL B 41  ? 0.9574 0.7642 0.8966 -0.2150 -0.0692 -0.0506 1078 VAL B CA  
2472 C C   . VAL B 41  ? 1.0127 0.7769 0.9007 -0.2120 -0.0779 -0.0488 1078 VAL B C   
2473 O O   . VAL B 41  ? 1.0715 0.7856 0.9087 -0.2191 -0.1055 -0.0492 1078 VAL B O   
2474 C CB  . VAL B 41  ? 0.9069 0.7663 0.8923 -0.2372 -0.0792 -0.0432 1078 VAL B CB  
2475 C CG1 . VAL B 41  ? 0.8697 0.7695 0.8883 -0.2362 -0.0677 -0.0401 1078 VAL B CG1 
2476 C CG2 . VAL B 41  ? 0.8792 0.7607 0.8921 -0.2349 -0.0754 -0.0456 1078 VAL B CG2 
2477 N N   . HIS B 42  ? 1.0089 0.7849 0.9050 -0.2004 -0.0571 -0.0475 1079 HIS B N   
2478 C CA  . HIS B 42  ? 1.0684 0.7992 0.9081 -0.1921 -0.0669 -0.0463 1079 HIS B CA  
2479 C C   . HIS B 42  ? 1.0324 0.8098 0.9097 -0.2041 -0.0764 -0.0416 1079 HIS B C   
2480 O O   . HIS B 42  ? 1.0123 0.8099 0.9094 -0.1940 -0.0500 -0.0395 1079 HIS B O   
2481 C CB  . HIS B 42  ? 1.1182 0.8026 0.9139 -0.1607 -0.0289 -0.0470 1079 HIS B CB  
2482 C CG  . HIS B 42  ? 1.1537 0.8044 0.9256 -0.1426 -0.0107 -0.0510 1079 HIS B CG  
2483 N ND1 . HIS B 42  ? 1.1444 0.8108 0.9499 -0.1238 0.0355  -0.0505 1079 HIS B ND1 
2484 C CD2 . HIS B 42  ? 1.2044 0.8048 0.9236 -0.1395 -0.0346 -0.0557 1079 HIS B CD2 
2485 C CE1 . HIS B 42  ? 1.1838 0.8169 0.9608 -0.1060 0.0411  -0.0550 1079 HIS B CE1 
2486 N NE2 . HIS B 42  ? 1.2245 0.8107 0.9399 -0.1144 -0.0025 -0.0584 1079 HIS B NE2 
2487 N N   . PHE B 43  ? 1.0316 0.8256 0.9225 -0.2256 -0.1136 -0.0395 1080 PHE B N   
2488 C CA  . PHE B 43  ? 0.9968 0.8436 0.9324 -0.2351 -0.1245 -0.0347 1080 PHE B CA  
2489 C C   . PHE B 43  ? 1.0478 0.8563 0.9341 -0.2153 -0.1341 -0.0376 1080 PHE B C   
2490 O O   . PHE B 43  ? 1.0251 0.8685 0.9368 -0.2106 -0.1313 -0.0349 1080 PHE B O   
2491 C CB  . PHE B 43  ? 0.9869 0.8671 0.9638 -0.2641 -0.1569 -0.0299 1080 PHE B CB  
2492 C CG  . PHE B 43  ? 0.9475 0.8605 0.9646 -0.2806 -0.1431 -0.0241 1080 PHE B CG  
2493 C CD1 . PHE B 43  ? 0.8880 0.8528 0.9489 -0.2765 -0.1163 -0.0200 1080 PHE B CD1 
2494 C CD2 . PHE B 43  ? 0.9826 0.8627 0.9823 -0.2974 -0.1592 -0.0233 1080 PHE B CD2 
2495 C CE1 . PHE B 43  ? 0.8679 0.8488 0.9492 -0.2854 -0.1064 -0.0156 1080 PHE B CE1 
2496 C CE2 . PHE B 43  ? 0.9592 0.8568 0.9815 -0.3083 -0.1457 -0.0173 1080 PHE B CE2 
2497 C CZ  . PHE B 43  ? 0.9043 0.8512 0.9647 -0.3005 -0.1195 -0.0137 1080 PHE B CZ  
2498 N N   . ASN B 44  ? 1.1284 0.8557 0.9334 -0.1993 -0.1465 -0.0435 1081 ASN B N   
2499 C CA  . ASN B 44  ? 1.1990 0.8664 0.9316 -0.1724 -0.1537 -0.0468 1081 ASN B CA  
2500 C C   . ASN B 44  ? 1.1912 0.8509 0.9114 -0.1504 -0.0993 -0.0417 1081 ASN B C   
2501 O O   . ASN B 44  ? 1.2077 0.8584 0.9086 -0.1358 -0.0958 -0.0399 1081 ASN B O   
2502 C CB  . ASN B 44  ? 1.3070 0.8738 0.9390 -0.1553 -0.1788 -0.0546 1081 ASN B CB  
2503 C CG  . ASN B 44  ? 1.3295 0.8935 0.9738 -0.1806 -0.2384 -0.0607 1081 ASN B CG  
2504 O OD1 . ASN B 44  ? 1.2852 0.8905 0.9859 -0.2086 -0.2398 -0.0576 1081 ASN B OD1 
2505 N ND2 . ASN B 44  ? 1.4093 0.9191 1.0002 -0.1709 -0.2895 -0.0697 1081 ASN B ND2 
2506 N N   . GLU B 45  ? 1.1694 0.8322 0.9052 -0.1484 -0.0584 -0.0394 1082 GLU B N   
2507 C CA  . GLU B 45  ? 1.1708 0.8250 0.9075 -0.1317 -0.0038 -0.0339 1082 GLU B CA  
2508 C C   . GLU B 45  ? 1.0774 0.8142 0.9084 -0.1498 0.0111  -0.0312 1082 GLU B C   
2509 O O   . GLU B 45  ? 1.0173 0.7992 0.9104 -0.1620 0.0227  -0.0329 1082 GLU B O   
2510 C CB  . GLU B 45  ? 1.2008 0.8227 0.9200 -0.1184 0.0307  -0.0338 1082 GLU B CB  
2511 C CG  . GLU B 45  ? 1.3051 0.8337 0.9175 -0.0955 0.0159  -0.0371 1082 GLU B CG  
2512 C CD  . GLU B 45  ? 1.3411 0.8369 0.9328 -0.0756 0.0545  -0.0362 1082 GLU B CD  
2513 O OE1 . GLU B 45  ? 1.3579 0.8354 0.9294 -0.0776 0.0289  -0.0428 1082 GLU B OE1 
2514 O OE2 . GLU B 45  ? 1.3566 0.8446 0.9552 -0.0579 0.1117  -0.0283 1082 GLU B OE2 
2515 N N   . VAL B 46  ? 1.0735 0.8213 0.9060 -0.1472 0.0071  -0.0283 1083 VAL B N   
2516 C CA  . VAL B 46  ? 1.0063 0.8154 0.9098 -0.1586 0.0199  -0.0263 1083 VAL B CA  
2517 C C   . VAL B 46  ? 1.0270 0.8095 0.9294 -0.1482 0.0690  -0.0215 1083 VAL B C   
2518 O O   . VAL B 46  ? 1.0977 0.8173 0.9326 -0.1289 0.0867  -0.0163 1083 VAL B O   
2519 C CB  . VAL B 46  ? 0.9960 0.8310 0.9029 -0.1586 -0.0101 -0.0256 1083 VAL B CB  
2520 C CG1 . VAL B 46  ? 0.9387 0.8261 0.9049 -0.1652 0.0022  -0.0240 1083 VAL B CG1 
2521 C CG2 . VAL B 46  ? 0.9837 0.8481 0.9053 -0.1719 -0.0551 -0.0281 1083 VAL B CG2 
2522 N N   . ILE B 47  ? 0.9732 0.7997 0.9507 -0.1609 0.0897  -0.0233 1084 ILE B N   
2523 C CA  . ILE B 47  ? 0.9896 0.8005 0.9914 -0.1582 0.1369  -0.0187 1084 ILE B CA  
2524 C C   . ILE B 47  ? 0.9713 0.7951 0.9961 -0.1637 0.1395  -0.0169 1084 ILE B C   
2525 O O   . ILE B 47  ? 1.0071 0.7967 1.0277 -0.1605 0.1773  -0.0098 1084 ILE B O   
2526 C CB  . ILE B 47  ? 0.9518 0.8011 1.0305 -0.1674 0.1525  -0.0243 1084 ILE B CB  
2527 C CG1 . ILE B 47  ? 0.8781 0.7917 1.0349 -0.1845 0.1271  -0.0337 1084 ILE B CG1 
2528 C CG2 . ILE B 47  ? 0.9714 0.8054 1.0188 -0.1590 0.1433  -0.0272 1084 ILE B CG2 
2529 C CD1 . ILE B 47  ? 0.8498 0.7977 1.0825 -0.1894 0.1344  -0.0422 1084 ILE B CD1 
2530 N N   . GLY B 48  ? 0.9221 0.7903 0.9687 -0.1709 0.1029  -0.0220 1085 GLY B N   
2531 C CA  . GLY B 48  ? 0.9132 0.7885 0.9712 -0.1712 0.1011  -0.0214 1085 GLY B CA  
2532 C C   . GLY B 48  ? 0.8689 0.7916 0.9395 -0.1720 0.0627  -0.0251 1085 GLY B C   
2533 O O   . GLY B 48  ? 0.8327 0.7894 0.9196 -0.1785 0.0411  -0.0277 1085 GLY B O   
2534 N N   . ARG B 49  ? 0.8798 0.7994 0.9396 -0.1638 0.0586  -0.0238 1086 ARG B N   
2535 C CA  . ARG B 49  ? 0.8501 0.8135 0.9226 -0.1589 0.0314  -0.0252 1086 ARG B CA  
2536 C C   . ARG B 49  ? 0.8527 0.8053 0.9294 -0.1524 0.0369  -0.0273 1086 ARG B C   
2537 O O   . ARG B 49  ? 0.8976 0.8013 0.9480 -0.1485 0.0566  -0.0248 1086 ARG B O   
2538 C CB  . ARG B 49  ? 0.8767 0.8430 0.9112 -0.1453 0.0100  -0.0209 1086 ARG B CB  
2539 C CG  . ARG B 49  ? 0.8513 0.8737 0.9117 -0.1391 -0.0121 -0.0195 1086 ARG B CG  
2540 C CD  . ARG B 49  ? 0.8776 0.9121 0.9205 -0.1271 -0.0369 -0.0166 1086 ARG B CD  
2541 N NE  . ARG B 49  ? 0.8886 0.9203 0.9300 -0.1403 -0.0519 -0.0172 1086 ARG B NE  
2542 C CZ  . ARG B 49  ? 0.9452 0.9261 0.9339 -0.1315 -0.0626 -0.0193 1086 ARG B CZ  
2543 N NH1 . ARG B 49  ? 1.0026 0.9297 0.9330 -0.1089 -0.0561 -0.0196 1086 ARG B NH1 
2544 N NH2 . ARG B 49  ? 0.9552 0.9283 0.9391 -0.1430 -0.0806 -0.0213 1086 ARG B NH2 
2545 N N   . GLY B 50  ? 0.8138 0.8028 0.9157 -0.1498 0.0208  -0.0312 1087 GLY B N   
2546 C CA  . GLY B 50  ? 0.8252 0.7961 0.9241 -0.1414 0.0201  -0.0355 1087 GLY B CA  
2547 C C   . GLY B 50  ? 0.8037 0.8094 0.9041 -0.1263 0.0018  -0.0365 1087 GLY B C   
2548 O O   . GLY B 50  ? 0.7869 0.8321 0.8868 -0.1191 -0.0056 -0.0297 1087 GLY B O   
2549 N N   . HIS B 51  ? 0.8116 0.7978 0.9139 -0.1211 -0.0044 -0.0448 1088 HIS B N   
2550 C CA  . HIS B 51  ? 0.8129 0.8134 0.8983 -0.0991 -0.0172 -0.0455 1088 HIS B CA  
2551 C C   . HIS B 51  ? 0.7803 0.8190 0.8875 -0.1036 -0.0228 -0.0445 1088 HIS B C   
2552 O O   . HIS B 51  ? 0.7788 0.8467 0.8743 -0.0870 -0.0218 -0.0361 1088 HIS B O   
2553 C CB  . HIS B 51  ? 0.8494 0.8009 0.9196 -0.0914 -0.0281 -0.0575 1088 HIS B CB  
2554 C CG  . HIS B 51  ? 0.8714 0.8193 0.9066 -0.0620 -0.0410 -0.0597 1088 HIS B CG  
2555 N ND1 . HIS B 51  ? 0.8887 0.8498 0.8864 -0.0315 -0.0351 -0.0498 1088 HIS B ND1 
2556 C CD2 . HIS B 51  ? 0.8886 0.8156 0.9167 -0.0546 -0.0595 -0.0711 1088 HIS B CD2 
2557 C CE1 . HIS B 51  ? 0.9196 0.8669 0.8843 -0.0054 -0.0430 -0.0529 1088 HIS B CE1 
2558 N NE2 . HIS B 51  ? 0.9239 0.8440 0.8998 -0.0185 -0.0604 -0.0667 1088 HIS B NE2 
2559 N N   . PHE B 52  ? 0.7610 0.7973 0.9004 -0.1247 -0.0256 -0.0519 1089 PHE B N   
2560 C CA  . PHE B 52  ? 0.7456 0.8019 0.8958 -0.1273 -0.0330 -0.0530 1089 PHE B CA  
2561 C C   . PHE B 52  ? 0.7227 0.8166 0.8811 -0.1377 -0.0242 -0.0399 1089 PHE B C   
2562 O O   . PHE B 52  ? 0.7214 0.8381 0.8735 -0.1318 -0.0230 -0.0314 1089 PHE B O   
2563 C CB  . PHE B 52  ? 0.7394 0.7781 0.9229 -0.1415 -0.0438 -0.0680 1089 PHE B CB  
2564 C CG  . PHE B 52  ? 0.7712 0.7729 0.9559 -0.1334 -0.0625 -0.0836 1089 PHE B CG  
2565 C CD1 . PHE B 52  ? 0.8019 0.7829 0.9510 -0.1104 -0.0831 -0.0906 1089 PHE B CD1 
2566 C CD2 . PHE B 52  ? 0.7826 0.7624 0.9996 -0.1480 -0.0593 -0.0907 1089 PHE B CD2 
2567 C CE1 . PHE B 52  ? 0.8440 0.7808 0.9879 -0.1016 -0.1089 -0.1078 1089 PHE B CE1 
2568 C CE2 . PHE B 52  ? 0.8186 0.7612 1.0439 -0.1448 -0.0819 -0.1063 1089 PHE B CE2 
2569 C CZ  . PHE B 52  ? 0.8502 0.7700 1.0376 -0.1212 -0.1110 -0.1164 1089 PHE B CZ  
2570 N N   . GLY B 53  ? 0.7169 0.8100 0.8859 -0.1527 -0.0174 -0.0378 1090 GLY B N   
2571 C CA  . GLY B 53  ? 0.7061 0.8237 0.8785 -0.1629 -0.0169 -0.0282 1090 GLY B CA  
2572 C C   . GLY B 53  ? 0.7146 0.8091 0.8840 -0.1751 -0.0114 -0.0302 1090 GLY B C   
2573 O O   . GLY B 53  ? 0.7316 0.7956 0.8971 -0.1743 -0.0003 -0.0350 1090 GLY B O   
2574 N N   . CYS B 54  ? 0.7150 0.8182 0.8825 -0.1857 -0.0174 -0.0254 1091 CYS B N   
2575 C CA  . CYS B 54  ? 0.7385 0.8099 0.8878 -0.1918 -0.0128 -0.0270 1091 CYS B CA  
2576 C C   . CYS B 54  ? 0.7313 0.7917 0.8962 -0.2007 -0.0064 -0.0336 1091 CYS B C   
2577 O O   . CYS B 54  ? 0.7143 0.7924 0.8948 -0.2057 -0.0154 -0.0351 1091 CYS B O   
2578 C CB  . CYS B 54  ? 0.7559 0.8317 0.8888 -0.1964 -0.0303 -0.0213 1091 CYS B CB  
2579 S SG  . CYS B 54  ? 0.7803 0.8746 0.9045 -0.1816 -0.0446 -0.0159 1091 CYS B SG  
2580 N N   . VAL B 55  ? 0.7524 0.7804 0.9104 -0.1994 0.0116  -0.0367 1092 VAL B N   
2581 C CA  . VAL B 55  ? 0.7498 0.7700 0.9273 -0.2032 0.0204  -0.0428 1092 VAL B CA  
2582 C C   . VAL B 55  ? 0.7883 0.7729 0.9224 -0.2005 0.0259  -0.0391 1092 VAL B C   
2583 O O   . VAL B 55  ? 0.8245 0.7770 0.9168 -0.1927 0.0338  -0.0340 1092 VAL B O   
2584 C CB  . VAL B 55  ? 0.7454 0.7617 0.9652 -0.2026 0.0418  -0.0490 1092 VAL B CB  
2585 C CG1 . VAL B 55  ? 0.7388 0.7610 0.9966 -0.2035 0.0473  -0.0570 1092 VAL B CG1 
2586 C CG2 . VAL B 55  ? 0.7247 0.7595 0.9720 -0.2027 0.0302  -0.0541 1092 VAL B CG2 
2587 N N   . TYR B 56  ? 0.7947 0.7754 0.9284 -0.2030 0.0194  -0.0427 1093 TYR B N   
2588 C CA  . TYR B 56  ? 0.8491 0.7873 0.9306 -0.1981 0.0180  -0.0407 1093 TYR B CA  
2589 C C   . TYR B 56  ? 0.8692 0.7891 0.9597 -0.1879 0.0420  -0.0454 1093 TYR B C   
2590 O O   . TYR B 56  ? 0.8351 0.7862 0.9826 -0.1890 0.0475  -0.0521 1093 TYR B O   
2591 C CB  . TYR B 56  ? 0.8548 0.7967 0.9194 -0.2099 -0.0143 -0.0395 1093 TYR B CB  
2592 C CG  . TYR B 56  ? 0.8380 0.8120 0.9138 -0.2205 -0.0348 -0.0335 1093 TYR B CG  
2593 C CD1 . TYR B 56  ? 0.8032 0.8175 0.9142 -0.2308 -0.0435 -0.0309 1093 TYR B CD1 
2594 C CD2 . TYR B 56  ? 0.8654 0.8268 0.9143 -0.2163 -0.0446 -0.0300 1093 TYR B CD2 
2595 C CE1 . TYR B 56  ? 0.7899 0.8388 0.9182 -0.2377 -0.0547 -0.0230 1093 TYR B CE1 
2596 C CE2 . TYR B 56  ? 0.8480 0.8481 0.9197 -0.2231 -0.0632 -0.0248 1093 TYR B CE2 
2597 C CZ  . TYR B 56  ? 0.8084 0.8563 0.9247 -0.2344 -0.0650 -0.0202 1093 TYR B CZ  
2598 O OH  . TYR B 56  ? 0.7966 0.8879 0.9424 -0.2384 -0.0760 -0.0128 1093 TYR B OH  
2599 N N   . HIS B 57  ? 0.9331 0.7998 0.9652 -0.1744 0.0542  -0.0426 1094 HIS B N   
2600 C CA  . HIS B 57  ? 0.9665 0.8123 0.9967 -0.1597 0.0760  -0.0459 1094 HIS B CA  
2601 C C   . HIS B 57  ? 0.9616 0.8119 0.9884 -0.1645 0.0458  -0.0525 1094 HIS B C   
2602 O O   . HIS B 57  ? 0.9569 0.8032 0.9570 -0.1785 0.0122  -0.0511 1094 HIS B O   
2603 C CB  . HIS B 57  ? 1.0504 0.8236 0.9987 -0.1377 0.0984  -0.0400 1094 HIS B CB  
2604 C CG  . HIS B 57  ? 1.0784 0.8354 1.0313 -0.1257 0.1474  -0.0318 1094 HIS B CG  
2605 N ND1 . HIS B 57  ? 1.0531 0.8471 1.0873 -0.1258 0.1867  -0.0310 1094 HIS B ND1 
2606 C CD2 . HIS B 57  ? 1.1399 0.8406 1.0224 -0.1129 0.1626  -0.0233 1094 HIS B CD2 
2607 C CE1 . HIS B 57  ? 1.0966 0.8587 1.1146 -0.1172 0.2305  -0.0200 1094 HIS B CE1 
2608 N NE2 . HIS B 57  ? 1.1537 0.8529 1.0693 -0.1068 0.2169  -0.0149 1094 HIS B NE2 
2609 N N   . GLY B 58  ? 0.9685 0.8266 1.0258 -0.1523 0.0591  -0.0590 1095 GLY B N   
2610 C CA  . GLY B 58  ? 0.9740 0.8278 1.0220 -0.1520 0.0326  -0.0659 1095 GLY B CA  
2611 C C   . GLY B 58  ? 1.0231 0.8487 1.0571 -0.1256 0.0514  -0.0709 1095 GLY B C   
2612 O O   . GLY B 58  ? 1.0432 0.8669 1.0952 -0.1085 0.0909  -0.0684 1095 GLY B O   
2613 N N   . THR B 59  ? 1.0505 0.8510 1.0503 -0.1212 0.0258  -0.0765 1096 THR B N   
2614 C CA  . THR B 59  ? 1.1023 0.8737 1.0830 -0.0917 0.0382  -0.0827 1096 THR B CA  
2615 C C   . THR B 59  ? 1.1016 0.8789 1.0908 -0.0896 0.0073  -0.0925 1096 THR B C   
2616 O O   . THR B 59  ? 1.1302 0.8619 1.0538 -0.0995 -0.0223 -0.0910 1096 THR B O   
2617 C CB  . THR B 59  ? 1.1865 0.8742 1.0611 -0.0773 0.0399  -0.0779 1096 THR B CB  
2618 O OG1 . THR B 59  ? 1.2063 0.8806 1.0659 -0.0709 0.0723  -0.0693 1096 THR B OG1 
2619 C CG2 . THR B 59  ? 1.2470 0.8945 1.0863 -0.0421 0.0508  -0.0841 1096 THR B CG2 
2620 N N   . LEU B 60  ? 1.0820 0.9117 1.1532 -0.0768 0.0129  -0.1029 1097 LEU B N   
2621 C CA  . LEU B 60  ? 1.1035 0.9324 1.1792 -0.0644 -0.0163 -0.1149 1097 LEU B CA  
2622 C C   . LEU B 60  ? 1.1664 0.9759 1.2362 -0.0262 -0.0022 -0.1230 1097 LEU B C   
2623 O O   . LEU B 60  ? 1.1786 1.0036 1.2819 -0.0098 0.0371  -0.1203 1097 LEU B O   
2624 C CB  . LEU B 60  ? 1.0464 0.9402 1.2136 -0.0694 -0.0284 -0.1248 1097 LEU B CB  
2625 C CG  . LEU B 60  ? 1.0598 0.9465 1.2233 -0.0544 -0.0660 -0.1387 1097 LEU B CG  
2626 C CD1 . LEU B 60  ? 1.0772 0.9194 1.1605 -0.0742 -0.0914 -0.1299 1097 LEU B CD1 
2627 C CD2 . LEU B 60  ? 1.0166 0.9641 1.2795 -0.0483 -0.0788 -0.1537 1097 LEU B CD2 
2628 N N   . LEU B 61  ? 1.2208 0.9917 1.2431 -0.0099 -0.0313 -0.1314 1098 LEU B N   
2629 C CA  . LEU B 61  ? 1.2811 1.0348 1.2982 0.0322  -0.0237 -0.1414 1098 LEU B CA  
2630 C C   . LEU B 61  ? 1.2910 1.0573 1.3335 0.0499  -0.0604 -0.1580 1098 LEU B C   
2631 O O   . LEU B 61  ? 1.3255 1.0382 1.2917 0.0426  -0.0937 -0.1578 1098 LEU B O   
2632 C CB  . LEU B 61  ? 1.3663 1.0257 1.2590 0.0432  -0.0244 -0.1348 1098 LEU B CB  
2633 C CG  . LEU B 61  ? 1.3897 0.9854 1.1903 0.0091  -0.0578 -0.1261 1098 LEU B CG  
2634 C CD1 . LEU B 61  ? 1.4902 0.9863 1.1755 0.0276  -0.0734 -0.1270 1098 LEU B CD1 
2635 C CD2 . LEU B 61  ? 1.3611 0.9628 1.1563 -0.0250 -0.0473 -0.1125 1098 LEU B CD2 
2636 N N   . ASP B 62  ? 1.2731 1.1079 1.4248 0.0739  -0.0542 -0.1721 1099 ASP B N   
2637 C CA  . ASP B 62  ? 1.2794 1.1346 1.4710 0.0934  -0.0956 -0.1917 1099 ASP B CA  
2638 C C   . ASP B 62  ? 1.3505 1.1724 1.5106 0.1418  -0.1047 -0.2039 1099 ASP B C   
2639 O O   . ASP B 62  ? 1.3689 1.2096 1.5637 0.1679  -0.0692 -0.2035 1099 ASP B O   
2640 C CB  . ASP B 62  ? 1.2191 1.1686 1.5575 0.0899  -0.0947 -0.2034 1099 ASP B CB  
2641 C CG  . ASP B 62  ? 1.2241 1.1892 1.5995 0.1069  -0.1489 -0.2260 1099 ASP B CG  
2642 O OD1 . ASP B 62  ? 1.2822 1.1809 1.5608 0.1235  -0.1836 -0.2311 1099 ASP B OD1 
2643 O OD2 . ASP B 62  ? 1.1816 1.2176 1.6778 0.1041  -0.1580 -0.2387 1099 ASP B OD2 
2644 N N   . ASN B 63  ? 1.3988 1.1655 1.4866 0.1565  -0.1496 -0.2136 1100 ASN B N   
2645 C CA  . ASN B 63  ? 1.4735 1.1968 1.5165 0.2059  -0.1672 -0.2271 1100 ASN B CA  
2646 C C   . ASN B 63  ? 1.5332 1.1938 1.4888 0.2173  -0.1353 -0.2145 1100 ASN B C   
2647 O O   . ASN B 63  ? 1.5749 1.2362 1.5421 0.2632  -0.1221 -0.2231 1100 ASN B O   
2648 C CB  . ASN B 63  ? 1.4547 1.2616 1.6321 0.2465  -0.1744 -0.2497 1100 ASN B CB  
2649 C CG  . ASN B 63  ? 1.4081 1.2681 1.6688 0.2374  -0.2148 -0.2657 1100 ASN B CG  
2650 O OD1 . ASN B 63  ? 1.3434 1.2947 1.7429 0.2275  -0.2032 -0.2717 1100 ASN B OD1 
2651 N ND2 . ASN B 63  ? 1.4509 1.2455 1.6218 0.2417  -0.2619 -0.2723 1100 ASN B ND2 
2652 N N   . ASP B 64  ? 1.5413 1.1456 1.4090 0.1778  -0.1258 -0.1952 1101 ASP B N   
2653 C CA  . ASP B 64  ? 1.6027 1.1366 1.3776 0.1839  -0.1024 -0.1838 1101 ASP B CA  
2654 C C   . ASP B 64  ? 1.5898 1.1779 1.4390 0.2125  -0.0525 -0.1836 1101 ASP B C   
2655 O O   . ASP B 64  ? 1.6673 1.2100 1.4642 0.2541  -0.0350 -0.1853 1101 ASP B O   
2656 C CB  . ASP B 64  ? 1.7057 1.1351 1.3572 0.2134  -0.1309 -0.1896 1101 ASP B CB  
2657 C CG  . ASP B 64  ? 1.7848 1.1150 1.3127 0.2105  -0.1216 -0.1780 1101 ASP B CG  
2658 O OD1 . ASP B 64  ? 1.8615 1.1424 1.3355 0.2582  -0.1128 -0.1844 1101 ASP B OD1 
2659 O OD2 . ASP B 64  ? 1.7714 1.0725 1.2581 0.1629  -0.1259 -0.1639 1101 ASP B OD2 
2660 N N   . GLY B 65  ? 1.4981 1.1780 1.4655 0.1909  -0.0268 -0.1800 1102 GLY B N   
2661 C CA  . GLY B 65  ? 1.4789 1.2207 1.5385 0.2135  0.0273  -0.1773 1102 GLY B CA  
2662 C C   . GLY B 65  ? 1.4749 1.1960 1.4984 0.1892  0.0695  -0.1571 1102 GLY B C   
2663 O O   . GLY B 65  ? 1.5114 1.1542 1.4188 0.1673  0.0538  -0.1478 1102 GLY B O   
2664 N N   . LYS B 66  ? 1.4355 1.2254 1.5625 0.1936  0.1217  -0.1507 1103 LYS B N   
2665 C CA  . LYS B 66  ? 1.4415 1.2074 1.5332 0.1792  0.1678  -0.1314 1103 LYS B CA  
2666 C C   . LYS B 66  ? 1.3647 1.1463 1.4634 0.1245  0.1442  -0.1256 1103 LYS B C   
2667 O O   . LYS B 66  ? 1.2933 1.1268 1.4594 0.1013  0.1077  -0.1355 1103 LYS B O   
2668 C CB  . LYS B 66  ? 1.4352 1.2683 1.6410 0.2010  0.2365  -0.1243 1103 LYS B CB  
2669 C CG  . LYS B 66  ? 1.4935 1.2740 1.6313 0.2085  0.2977  -0.1030 1103 LYS B CG  
2670 C CD  . LYS B 66  ? 1.6132 1.2827 1.5957 0.2525  0.3091  -0.0989 1103 LYS B CD  
2671 C CE  . LYS B 66  ? 1.6912 1.2998 1.5993 0.2707  0.3732  -0.0785 1103 LYS B CE  
2672 N NZ  . LYS B 66  ? 1.6734 1.2464 1.5226 0.2279  0.3558  -0.0697 1103 LYS B NZ  
2673 N N   . LYS B 67  ? 1.3835 1.1135 1.4042 0.1092  0.1634  -0.1104 1104 LYS B N   
2674 C CA  . LYS B 67  ? 1.3217 1.0657 1.3465 0.0630  0.1456  -0.1038 1104 LYS B CA  
2675 C C   . LYS B 67  ? 1.2368 1.0747 1.4018 0.0463  0.1708  -0.1033 1104 LYS B C   
2676 O O   . LYS B 67  ? 1.2486 1.1145 1.4747 0.0634  0.2250  -0.0967 1104 LYS B O   
2677 C CB  . LYS B 67  ? 1.3826 1.0489 1.2956 0.0582  0.1587  -0.0900 1104 LYS B CB  
2678 C CG  . LYS B 67  ? 1.4474 1.0872 1.3418 0.0901  0.2240  -0.0780 1104 LYS B CG  
2679 C CD  . LYS B 67  ? 1.5007 1.0673 1.2912 0.0831  0.2309  -0.0657 1104 LYS B CD  
2680 C CE  . LYS B 67  ? 1.5722 1.0408 1.2230 0.0839  0.1811  -0.0698 1104 LYS B CE  
2681 N NZ  . LYS B 67  ? 1.6679 1.0663 1.2380 0.1289  0.1884  -0.0743 1104 LYS B NZ  
2682 N N   . ILE B 68  ? 1.1566 1.0372 1.3695 0.0134  0.1321  -0.1096 1105 ILE B N   
2683 C CA  . ILE B 68  ? 1.0819 1.0399 1.4168 -0.0065 0.1433  -0.1114 1105 ILE B CA  
2684 C C   . ILE B 68  ? 1.0539 0.9977 1.3535 -0.0393 0.1451  -0.0990 1105 ILE B C   
2685 O O   . ILE B 68  ? 1.0338 0.9605 1.2832 -0.0600 0.1049  -0.0998 1105 ILE B O   
2686 C CB  . ILE B 68  ? 1.0321 1.0402 1.4401 -0.0109 0.0950  -0.1305 1105 ILE B CB  
2687 C CG1 . ILE B 68  ? 1.0606 1.0772 1.4949 0.0269  0.0852  -0.1450 1105 ILE B CG1 
2688 C CG2 . ILE B 68  ? 0.9734 1.0518 1.5031 -0.0323 0.0990  -0.1346 1105 ILE B CG2 
2689 C CD1 . ILE B 68  ? 1.0333 1.0777 1.5104 0.0300  0.0290  -0.1656 1105 ILE B CD1 
2690 N N   . HIS B 69  ? 1.0573 1.0063 1.3830 -0.0414 0.1949  -0.0864 1106 HIS B N   
2691 C CA  . HIS B 69  ? 1.0412 0.9734 1.3327 -0.0665 0.1991  -0.0751 1106 HIS B CA  
2692 C C   . HIS B 69  ? 0.9613 0.9519 1.3339 -0.0948 0.1695  -0.0832 1106 HIS B C   
2693 O O   . HIS B 69  ? 0.9297 0.9758 1.4136 -0.0982 0.1813  -0.0895 1106 HIS B O   
2694 C CB  . HIS B 69  ? 1.0890 1.0002 1.3795 -0.0565 0.2640  -0.0589 1106 HIS B CB  
2695 C CG  . HIS B 69  ? 1.1104 0.9762 1.3258 -0.0704 0.2686  -0.0466 1106 HIS B CG  
2696 N ND1 . HIS B 69  ? 1.1631 0.9952 1.3582 -0.0624 0.3243  -0.0306 1106 HIS B ND1 
2697 C CD2 . HIS B 69  ? 1.0903 0.9383 1.2462 -0.0895 0.2230  -0.0481 1106 HIS B CD2 
2698 C CE1 . HIS B 69  ? 1.1757 0.9667 1.2949 -0.0735 0.3079  -0.0246 1106 HIS B CE1 
2699 N NE2 . HIS B 69  ? 1.1277 0.9342 1.2294 -0.0908 0.2448  -0.0356 1106 HIS B NE2 
2700 N N   . CYS B 70  ? 0.9320 0.9079 1.2497 -0.1135 0.1301  -0.0830 1107 CYS B N   
2701 C CA  . CYS B 70  ? 0.8699 0.8873 1.2398 -0.1337 0.0984  -0.0908 1107 CYS B CA  
2702 C C   . CYS B 70  ? 0.8558 0.8554 1.1734 -0.1525 0.0911  -0.0805 1107 CYS B C   
2703 O O   . CYS B 70  ? 0.8862 0.8420 1.1274 -0.1505 0.1012  -0.0697 1107 CYS B O   
2704 C CB  . CYS B 70  ? 0.8566 0.8798 1.2189 -0.1291 0.0525  -0.1038 1107 CYS B CB  
2705 S SG  . CYS B 70  ? 0.8931 0.8551 1.1338 -0.1288 0.0294  -0.0968 1107 CYS B SG  
2706 N N   . ALA B 71  ? 0.8130 0.8439 1.1712 -0.1670 0.0706  -0.0853 1108 ALA B N   
2707 C CA  . ALA B 71  ? 0.8002 0.8228 1.1181 -0.1807 0.0607  -0.0771 1108 ALA B CA  
2708 C C   . ALA B 71  ? 0.7751 0.8075 1.0740 -0.1857 0.0209  -0.0816 1108 ALA B C   
2709 O O   . ALA B 71  ? 0.7540 0.8058 1.0920 -0.1813 0.0006  -0.0938 1108 ALA B O   
2710 C CB  . ALA B 71  ? 0.7886 0.8278 1.1576 -0.1893 0.0780  -0.0761 1108 ALA B CB  
2711 N N   . VAL B 72  ? 0.7826 0.7988 1.0220 -0.1932 0.0103  -0.0715 1109 VAL B N   
2712 C CA  . VAL B 72  ? 0.7770 0.7982 0.9941 -0.1984 -0.0169 -0.0704 1109 VAL B CA  
2713 C C   . VAL B 72  ? 0.7619 0.7993 0.9735 -0.2061 -0.0197 -0.0623 1109 VAL B C   
2714 O O   . VAL B 72  ? 0.7631 0.7956 0.9614 -0.2090 -0.0080 -0.0552 1109 VAL B O   
2715 C CB  . VAL B 72  ? 0.8059 0.7971 0.9698 -0.2022 -0.0272 -0.0646 1109 VAL B CB  
2716 C CG1 . VAL B 72  ? 0.8057 0.7988 0.9505 -0.2103 -0.0472 -0.0597 1109 VAL B CG1 
2717 C CG2 . VAL B 72  ? 0.8313 0.7994 0.9902 -0.1886 -0.0229 -0.0727 1109 VAL B CG2 
2718 N N   . LYS B 73  ? 0.7565 0.8071 0.9707 -0.2045 -0.0350 -0.0634 1110 LYS B N   
2719 C CA  . LYS B 73  ? 0.7518 0.8189 0.9606 -0.2055 -0.0357 -0.0559 1110 LYS B CA  
2720 C C   . LYS B 73  ? 0.7640 0.8326 0.9508 -0.2031 -0.0465 -0.0503 1110 LYS B C   
2721 O O   . LYS B 73  ? 0.7775 0.8294 0.9558 -0.1955 -0.0572 -0.0576 1110 LYS B O   
2722 C CB  . LYS B 73  ? 0.7456 0.8188 0.9850 -0.1979 -0.0330 -0.0648 1110 LYS B CB  
2723 C CG  . LYS B 73  ? 0.7479 0.8305 0.9743 -0.1918 -0.0347 -0.0591 1110 LYS B CG  
2724 C CD  . LYS B 73  ? 0.7538 0.8295 1.0033 -0.1858 -0.0354 -0.0690 1110 LYS B CD  
2725 C CE  . LYS B 73  ? 0.7660 0.8418 0.9905 -0.1732 -0.0395 -0.0648 1110 LYS B CE  
2726 N NZ  . LYS B 73  ? 0.7817 0.8542 0.9794 -0.1593 -0.0525 -0.0648 1110 LYS B NZ  
2727 N N   . SER B 74  ? 0.7652 0.8519 0.9424 -0.2069 -0.0417 -0.0367 1111 SER B N   
2728 C CA  . SER B 74  ? 0.7833 0.8725 0.9413 -0.2049 -0.0406 -0.0258 1111 SER B CA  
2729 C C   . SER B 74  ? 0.7937 0.8870 0.9439 -0.1844 -0.0377 -0.0268 1111 SER B C   
2730 O O   . SER B 74  ? 0.7760 0.8787 0.9394 -0.1777 -0.0369 -0.0318 1111 SER B O   
2731 C CB  . SER B 74  ? 0.7834 0.8945 0.9478 -0.2227 -0.0349 -0.0086 1111 SER B CB  
2732 O OG  . SER B 74  ? 0.7670 0.9077 0.9510 -0.2208 -0.0315 -0.0051 1111 SER B OG  
2733 N N   . LEU B 75  ? 0.8341 0.9098 0.9521 -0.1722 -0.0353 -0.0213 1112 LEU B N   
2734 C CA  . LEU B 75  ? 0.8667 0.9317 0.9576 -0.1462 -0.0322 -0.0212 1112 LEU B CA  
2735 C C   . LEU B 75  ? 0.8935 0.9764 0.9708 -0.1439 -0.0060 0.0027  1112 LEU B C   
2736 O O   . LEU B 75  ? 0.9360 0.9924 0.9774 -0.1383 0.0041  0.0125  1112 LEU B O   
2737 C CB  . LEU B 75  ? 0.9074 0.9224 0.9604 -0.1252 -0.0524 -0.0372 1112 LEU B CB  
2738 C CG  . LEU B 75  ? 0.8902 0.8967 0.9760 -0.1271 -0.0784 -0.0614 1112 LEU B CG  
2739 C CD1 . LEU B 75  ? 0.9385 0.8975 0.9912 -0.1018 -0.1070 -0.0796 1112 LEU B CD1 
2740 C CD2 . LEU B 75  ? 0.8630 0.8891 0.9859 -0.1301 -0.0794 -0.0688 1112 LEU B CD2 
2741 N N   . ASN B 76  ? 0.8769 1.0036 0.9846 -0.1464 0.0065  0.0128  1113 ASN B N   
2742 C CA  . ASN B 76  ? 0.8920 1.0550 1.0153 -0.1488 0.0333  0.0369  1113 ASN B CA  
2743 C C   . ASN B 76  ? 0.9505 1.0917 1.0256 -0.1144 0.0549  0.0460  1113 ASN B C   
2744 O O   . ASN B 76  ? 0.9768 1.1368 1.0567 -0.1135 0.0863  0.0691  1113 ASN B O   
2745 C CB  . ASN B 76  ? 0.8559 1.0744 1.0308 -0.1570 0.0340  0.0419  1113 ASN B CB  
2746 C CG  . ASN B 76  ? 0.8240 1.0526 1.0313 -0.1866 0.0141  0.0354  1113 ASN B CG  
2747 O OD1 . ASN B 76  ? 0.8068 1.0322 1.0173 -0.1848 0.0000  0.0229  1113 ASN B OD1 
2748 N ND2 . ASN B 76  ? 0.8292 1.0600 1.0519 -0.2123 0.0139  0.0444  1113 ASN B ND2 
2749 N N   . ARG B 77  ? 0.9832 1.0809 1.0119 -0.0857 0.0388  0.0284  1114 ARG B N   
2750 C CA  . ARG B 77  ? 1.0583 1.1148 1.0196 -0.0457 0.0531  0.0332  1114 ARG B CA  
2751 C C   . ARG B 77  ? 1.1148 1.1261 1.0247 -0.0399 0.0675  0.0441  1114 ARG B C   
2752 O O   . ARG B 77  ? 1.1771 1.1683 1.0396 -0.0134 0.1005  0.0627  1114 ARG B O   
2753 C CB  . ARG B 77  ? 1.0910 1.0963 1.0106 -0.0197 0.0201  0.0071  1114 ARG B CB  
2754 C CG  . ARG B 77  ? 1.0817 1.1082 1.0174 -0.0089 0.0177  0.0026  1114 ARG B CG  
2755 C CD  . ARG B 77  ? 1.1219 1.1678 1.0362 0.0201  0.0536  0.0241  1114 ARG B CD  
2756 N NE  . ARG B 77  ? 1.1476 1.1773 1.0365 0.0484  0.0447  0.0148  1114 ARG B NE  
2757 C CZ  . ARG B 77  ? 1.2150 1.1714 1.0305 0.0820  0.0237  -0.0014 1114 ARG B CZ  
2758 N NH1 . ARG B 77  ? 1.2678 1.1616 1.0261 0.0956  0.0085  -0.0106 1114 ARG B NH1 
2759 N NH2 . ARG B 77  ? 1.2360 1.1743 1.0296 0.1041  0.0140  -0.0098 1114 ARG B NH2 
2760 N N   . ILE B 78  ? 1.1013 1.0910 1.0143 -0.0611 0.0456  0.0333  1115 ILE B N   
2761 C CA  . ILE B 78  ? 1.1611 1.0970 1.0171 -0.0555 0.0550  0.0419  1115 ILE B CA  
2762 C C   . ILE B 78  ? 1.1605 1.1337 1.0498 -0.0819 0.0975  0.0740  1115 ILE B C   
2763 O O   . ILE B 78  ? 1.1051 1.1214 1.0594 -0.1212 0.0921  0.0769  1115 ILE B O   
2764 C CB  . ILE B 78  ? 1.1494 1.0535 1.0028 -0.0674 0.0165  0.0193  1115 ILE B CB  
2765 C CG1 . ILE B 78  ? 1.1484 1.0249 0.9910 -0.0451 -0.0264 -0.0125 1115 ILE B CG1 
2766 C CG2 . ILE B 78  ? 1.2228 1.0640 1.0090 -0.0601 0.0253  0.0288  1115 ILE B CG2 
2767 C CD1 . ILE B 78  ? 1.1259 0.9916 0.9929 -0.0573 -0.0620 -0.0350 1115 ILE B CD1 
2768 N N   . THR B 79  ? 1.2290 1.1806 1.0726 -0.0590 0.1398  0.0981  1116 THR B N   
2769 C CA  . THR B 79  ? 1.2379 1.2294 1.1254 -0.0840 0.1873  0.1321  1116 THR B CA  
2770 C C   . THR B 79  ? 1.3296 1.2440 1.1400 -0.0781 0.2123  0.1486  1116 THR B C   
2771 O O   . THR B 79  ? 1.3289 1.2408 1.1638 -0.1152 0.2130  0.1569  1116 THR B O   
2772 C CB  . THR B 79  ? 1.2454 1.2884 1.1612 -0.0637 0.2288  0.1527  1116 THR B CB  
2773 O OG1 . THR B 79  ? 1.1678 1.2720 1.1460 -0.0683 0.2010  0.1358  1116 THR B OG1 
2774 C CG2 . THR B 79  ? 1.2559 1.3525 1.2394 -0.0911 0.2807  0.1891  1116 THR B CG2 
2775 N N   . ASP B 80  ? 1.4210 1.2616 1.1271 -0.0284 0.2312  0.1527  1117 ASP B N   
2776 C CA  . ASP B 80  ? 1.5284 1.2828 1.1420 -0.0135 0.2643  0.1729  1117 ASP B CA  
2777 C C   . ASP B 80  ? 1.5523 1.2262 1.0964 -0.0074 0.2132  0.1458  1117 ASP B C   
2778 O O   . ASP B 80  ? 1.4829 1.1732 1.0559 -0.0114 0.1572  0.1125  1117 ASP B O   
2779 C CB  . ASP B 80  ? 1.6369 1.3337 1.1526 0.0437  0.3075  0.1895  1117 ASP B CB  
2780 C CG  . ASP B 80  ? 1.6739 1.3076 1.1009 0.0974  0.2614  0.1565  1117 ASP B CG  
2781 O OD1 . ASP B 80  ? 1.6516 1.3234 1.0988 0.1179  0.2640  0.1526  1117 ASP B OD1 
2782 O OD2 . ASP B 80  ? 1.7333 1.2765 1.0709 0.1198  0.2210  0.1345  1117 ASP B OD2 
2783 N N   . ILE B 81  ? 1.0974 1.1174 1.4039 -0.1711 0.3660  0.0992  1118 ILE B N   
2784 C CA  . ILE B 81  ? 1.1097 1.0815 1.3432 -0.1779 0.3325  0.0858  1118 ILE B CA  
2785 C C   . ILE B 81  ? 1.1323 1.0505 1.2743 -0.1603 0.3303  0.0696  1118 ILE B C   
2786 O O   . ILE B 81  ? 1.1171 1.0129 1.2195 -0.1599 0.2919  0.0554  1118 ILE B O   
2787 C CB  . ILE B 81  ? 1.1619 1.1026 1.3777 -0.1958 0.3466  0.1009  1118 ILE B CB  
2788 C CG1 . ILE B 81  ? 1.1689 1.0709 1.3327 -0.2052 0.3047  0.0894  1118 ILE B CG1 
2789 C CG2 . ILE B 81  ? 1.2368 1.1291 1.3955 -0.1884 0.3993  0.1118  1118 ILE B CG2 
2790 C CD1 . ILE B 81  ? 1.1132 1.0515 1.3257 -0.2138 0.2600  0.0802  1118 ILE B CD1 
2791 N N   . GLY B 82  ? 1.1712 1.0653 1.2808 -0.1459 0.3714  0.0734  1119 GLY B N   
2792 C CA  . GLY B 82  ? 1.2092 1.0420 1.2244 -0.1316 0.3682  0.0602  1119 GLY B CA  
2793 C C   . GLY B 82  ? 1.1489 1.0067 1.1768 -0.1207 0.3315  0.0431  1119 GLY B C   
2794 O O   . GLY B 82  ? 1.1612 0.9792 1.1286 -0.1175 0.3009  0.0315  1119 GLY B O   
2795 N N   . GLU B 83  ? 1.0860 1.0099 1.1967 -0.1161 0.3335  0.0440  1120 GLU B N   
2796 C CA  . GLU B 83  ? 1.0331 0.9830 1.1599 -0.1058 0.3046  0.0300  1120 GLU B CA  
2797 C C   . GLU B 83  ? 0.9828 0.9452 1.1176 -0.1148 0.2561  0.0199  1120 GLU B C   
2798 O O   . GLU B 83  ? 0.9518 0.9174 1.0772 -0.1069 0.2298  0.0078  1120 GLU B O   
2799 C CB  . GLU B 83  ? 0.9941 1.0072 1.2070 -0.1000 0.3197  0.0367  1120 GLU B CB  
2800 C CG  . GLU B 83  ? 1.0419 1.0417 1.2502 -0.0849 0.3716  0.0459  1120 GLU B CG  
2801 C CD  . GLU B 83  ? 1.0058 1.0706 1.3128 -0.0786 0.3890  0.0574  1120 GLU B CD  
2802 O OE1 . GLU B 83  ? 1.0430 1.0983 1.3531 -0.0627 0.4349  0.0654  1120 GLU B OE1 
2803 O OE2 . GLU B 83  ? 0.9495 1.0696 1.3279 -0.0893 0.3567  0.0593  1120 GLU B OE2 
2804 N N   . VAL B 84  ? 0.9774 0.9442 1.1300 -0.1309 0.2469  0.0258  1121 VAL B N   
2805 C CA  . VAL B 84  ? 0.9500 0.9166 1.1015 -0.1378 0.2074  0.0166  1121 VAL B CA  
2806 C C   . VAL B 84  ? 0.9830 0.8927 1.0614 -0.1331 0.1916  0.0104  1121 VAL B C   
2807 O O   . VAL B 84  ? 0.9571 0.8667 1.0301 -0.1267 0.1631  0.0003  1121 VAL B O   
2808 C CB  . VAL B 84  ? 0.9492 0.9275 1.1345 -0.1567 0.2023  0.0251  1121 VAL B CB  
2809 C CG1 . VAL B 84  ? 0.9371 0.9009 1.1087 -0.1613 0.1666  0.0150  1121 VAL B CG1 
2810 C CG2 . VAL B 84  ? 0.9175 0.9514 1.1816 -0.1647 0.2080  0.0341  1121 VAL B CG2 
2811 N N   . SER B 85  ? 1.0431 0.9030 1.0674 -0.1369 0.2103  0.0186  1122 SER B N   
2812 C CA  . SER B 85  ? 1.0892 0.8867 1.0401 -0.1357 0.1914  0.0165  1122 SER B CA  
2813 C C   . SER B 85  ? 1.0936 0.8734 1.0112 -0.1221 0.1783  0.0083  1122 SER B C   
2814 O O   . SER B 85  ? 1.1006 0.8521 0.9898 -0.1205 0.1453  0.0050  1122 SER B O   
2815 C CB  . SER B 85  ? 1.1651 0.9067 1.0563 -0.1435 0.2168  0.0280  1122 SER B CB  
2816 O OG  . SER B 85  ? 1.1620 0.9204 1.0881 -0.1580 0.2268  0.0375  1122 SER B OG  
2817 N N   . GLN B 86  ? 1.0930 0.8885 1.0184 -0.1126 0.2037  0.0069  1123 GLN B N   
2818 C CA  . GLN B 86  ? 1.0990 0.8797 0.9969 -0.1004 0.1922  -0.0007 1123 GLN B CA  
2819 C C   . GLN B 86  ? 1.0314 0.8513 0.9747 -0.0975 0.1542  -0.0088 1123 GLN B C   
2820 O O   . GLN B 86  ? 1.0405 0.8320 0.9536 -0.0945 0.1253  -0.0114 1123 GLN B O   
2821 C CB  . GLN B 86  ? 1.1030 0.9044 1.0188 -0.0897 0.2286  -0.0005 1123 GLN B CB  
2822 C CG  . GLN B 86  ? 1.0952 0.8943 0.9994 -0.0770 0.2153  -0.0094 1123 GLN B CG  
2823 C CD  . GLN B 86  ? 1.1716 0.8891 0.9797 -0.0750 0.2017  -0.0115 1123 GLN B CD  
2824 O OE1 . GLN B 86  ? 1.2423 0.8978 0.9823 -0.0818 0.2065  -0.0062 1123 GLN B OE1 
2825 N NE2 . GLN B 86  ? 1.1665 0.8783 0.9642 -0.0670 0.1822  -0.0182 1123 GLN B NE2 
2826 N N   . PHE B 87  ? 0.9677 0.8491 0.9827 -0.0994 0.1544  -0.0111 1124 PHE B N   
2827 C CA  . PHE B 87  ? 0.9116 0.8303 0.9680 -0.0949 0.1283  -0.0188 1124 PHE B CA  
2828 C C   . PHE B 87  ? 0.9076 0.8110 0.9605 -0.0986 0.1005  -0.0194 1124 PHE B C   
2829 O O   . PHE B 87  ? 0.8850 0.7977 0.9526 -0.0921 0.0787  -0.0232 1124 PHE B O   
2830 C CB  . PHE B 87  ? 0.8646 0.8410 0.9851 -0.0973 0.1370  -0.0202 1124 PHE B CB  
2831 C CG  . PHE B 87  ? 0.8196 0.8283 0.9738 -0.0929 0.1151  -0.0281 1124 PHE B CG  
2832 C CD1 . PHE B 87  ? 0.8098 0.8186 0.9568 -0.0824 0.1039  -0.0324 1124 PHE B CD1 
2833 C CD2 . PHE B 87  ? 0.7962 0.8290 0.9839 -0.1002 0.1064  -0.0304 1124 PHE B CD2 
2834 C CE1 . PHE B 87  ? 0.7722 0.8087 0.9490 -0.0785 0.0885  -0.0378 1124 PHE B CE1 
2835 C CE2 . PHE B 87  ? 0.7680 0.8208 0.9753 -0.0956 0.0912  -0.0376 1124 PHE B CE2 
2836 C CZ  . PHE B 87  ? 0.7537 0.8106 0.9578 -0.0843 0.0843  -0.0407 1124 PHE B CZ  
2837 N N   . LEU B 88  ? 0.9309 0.8111 0.9686 -0.1083 0.1032  -0.0141 1125 LEU B N   
2838 C CA  . LEU B 88  ? 0.9299 0.7924 0.9667 -0.1104 0.0793  -0.0133 1125 LEU B CA  
2839 C C   . LEU B 88  ? 0.9582 0.7800 0.9587 -0.1053 0.0550  -0.0095 1125 LEU B C   
2840 O O   . LEU B 88  ? 0.9398 0.7666 0.9645 -0.0999 0.0318  -0.0093 1125 LEU B O   
2841 C CB  . LEU B 88  ? 0.9608 0.8005 0.9827 -0.1229 0.0880  -0.0069 1125 LEU B CB  
2842 C CG  . LEU B 88  ? 0.9303 0.8061 0.9966 -0.1314 0.0980  -0.0087 1125 LEU B CG  
2843 C CD1 . LEU B 88  ? 0.9678 0.8156 1.0170 -0.1455 0.1045  -0.0003 1125 LEU B CD1 
2844 C CD2 . LEU B 88  ? 0.8911 0.7893 0.9913 -0.1261 0.0798  -0.0178 1125 LEU B CD2 
2845 N N   . THR B 89  ? 1.0097 0.7874 0.9518 -0.1072 0.0606  -0.0050 1126 THR B N   
2846 C CA  . THR B 89  ? 1.0526 0.7803 0.9498 -0.1062 0.0317  0.0005  1126 THR B CA  
2847 C C   . THR B 89  ? 1.0145 0.7683 0.9415 -0.0969 0.0144  -0.0031 1126 THR B C   
2848 O O   . THR B 89  ? 1.0214 0.7596 0.9535 -0.0957 -0.0189 0.0032  1126 THR B O   
2849 C CB  . THR B 89  ? 1.1338 0.7951 0.9450 -0.1115 0.0444  0.0051  1126 THR B CB  
2850 O OG1 . THR B 89  ? 1.1267 0.8058 0.9355 -0.1057 0.0776  -0.0008 1126 THR B OG1 
2851 C CG2 . THR B 89  ? 1.1792 0.8058 0.9554 -0.1221 0.0585  0.0120  1126 THR B CG2 
2852 N N   . GLU B 90  ? 0.9745 0.7684 0.9259 -0.0910 0.0361  -0.0110 1127 GLU B N   
2853 C CA  . GLU B 90  ? 0.9366 0.7590 0.9191 -0.0829 0.0230  -0.0144 1127 GLU B CA  
2854 C C   . GLU B 90  ? 0.8793 0.7452 0.9273 -0.0789 0.0093  -0.0148 1127 GLU B C   
2855 O O   . GLU B 90  ? 0.8665 0.7400 0.9384 -0.0741 -0.0124 -0.0110 1127 GLU B O   
2856 C CB  . GLU B 90  ? 0.9139 0.7686 0.9093 -0.0776 0.0505  -0.0218 1127 GLU B CB  
2857 C CG  . GLU B 90  ? 0.9736 0.7832 0.9061 -0.0769 0.0704  -0.0214 1127 GLU B CG  
2858 C CD  . GLU B 90  ? 0.9514 0.7952 0.9072 -0.0693 0.1008  -0.0265 1127 GLU B CD  
2859 O OE1 . GLU B 90  ? 0.8893 0.7924 0.9090 -0.0670 0.1020  -0.0299 1127 GLU B OE1 
2860 O OE2 . GLU B 90  ? 1.0025 0.8089 0.9100 -0.0652 0.1235  -0.0262 1127 GLU B OE2 
2861 N N   . GLY B 91  ? 0.8521 0.7423 0.9273 -0.0810 0.0236  -0.0185 1128 GLY B N   
2862 C CA  . GLY B 91  ? 0.8103 0.7326 0.9362 -0.0758 0.0187  -0.0209 1128 GLY B CA  
2863 C C   . GLY B 91  ? 0.8233 0.7253 0.9621 -0.0721 -0.0056 -0.0117 1128 GLY B C   
2864 O O   . GLY B 91  ? 0.7918 0.7179 0.9757 -0.0635 -0.0090 -0.0110 1128 GLY B O   
2865 N N   . ILE B 92  ? 0.8749 0.7301 0.9745 -0.0784 -0.0213 -0.0029 1129 ILE B N   
2866 C CA  . ILE B 92  ? 0.8984 0.7308 1.0133 -0.0762 -0.0500 0.0096  1129 ILE B CA  
2867 C C   . ILE B 92  ? 0.8833 0.7284 1.0305 -0.0703 -0.0720 0.0175  1129 ILE B C   
2868 O O   . ILE B 92  ? 0.8685 0.7309 1.0720 -0.0622 -0.0839 0.0263  1129 ILE B O   
2869 C CB  . ILE B 92  ? 0.9668 0.7379 1.0212 -0.0869 -0.0663 0.0186  1129 ILE B CB  
2870 C CG1 . ILE B 92  ? 0.9852 0.7446 1.0152 -0.0938 -0.0445 0.0139  1129 ILE B CG1 
2871 C CG2 . ILE B 92  ? 0.9913 0.7368 1.0656 -0.0856 -0.1046 0.0353  1129 ILE B CG2 
2872 C CD1 . ILE B 92  ? 1.0576 0.7536 1.0154 -0.1056 -0.0521 0.0218  1129 ILE B CD1 
2873 N N   . ILE B 93  ? 0.8924 0.7268 1.0054 -0.0741 -0.0757 0.0157  1130 ILE B N   
2874 C CA  . ILE B 93  ? 0.8851 0.7244 1.0208 -0.0720 -0.1004 0.0243  1130 ILE B CA  
2875 C C   . ILE B 93  ? 0.8171 0.7170 1.0171 -0.0616 -0.0828 0.0190  1130 ILE B C   
2876 O O   . ILE B 93  ? 0.8000 0.7185 1.0522 -0.0569 -0.0992 0.0303  1130 ILE B O   
2877 C CB  . ILE B 93  ? 0.9308 0.7291 0.9978 -0.0793 -0.1080 0.0221  1130 ILE B CB  
2878 C CG1 . ILE B 93  ? 1.0090 0.7344 0.9972 -0.0901 -0.1231 0.0276  1130 ILE B CG1 
2879 C CG2 . ILE B 93  ? 0.9289 0.7307 1.0192 -0.0792 -0.1362 0.0311  1130 ILE B CG2 
2880 C CD1 . ILE B 93  ? 1.0667 0.7393 0.9705 -0.0953 -0.1203 0.0229  1130 ILE B CD1 
2881 N N   . MET B 94  ? 0.7833 0.7113 0.9796 -0.0591 -0.0501 0.0039  1131 MET B N   
2882 C CA  . MET B 94  ? 0.7334 0.7090 0.9735 -0.0512 -0.0328 -0.0023 1131 MET B CA  
2883 C C   . MET B 94  ? 0.7148 0.7095 1.0067 -0.0422 -0.0270 0.0016  1131 MET B C   
2884 O O   . MET B 94  ? 0.6856 0.7095 1.0200 -0.0342 -0.0204 0.0040  1131 MET B O   
2885 C CB  . MET B 94  ? 0.7155 0.7088 0.9361 -0.0532 -0.0054 -0.0171 1131 MET B CB  
2886 C CG  . MET B 94  ? 0.7242 0.7096 0.9094 -0.0567 -0.0020 -0.0209 1131 MET B CG  
2887 S SD  . MET B 94  ? 0.7030 0.7152 0.8852 -0.0589 0.0280  -0.0327 1131 MET B SD  
2888 C CE  . MET B 94  ? 0.7488 0.7254 0.8767 -0.0622 0.0366  -0.0321 1131 MET B CE  
2889 N N   . LYS B 95  ? 0.7364 0.7104 1.0213 -0.0429 -0.0264 0.0025  1132 LYS B N   
2890 C CA  . LYS B 95  ? 0.7322 0.7143 1.0597 -0.0323 -0.0173 0.0057  1132 LYS B CA  
2891 C C   . LYS B 95  ? 0.7323 0.7180 1.1146 -0.0250 -0.0386 0.0254  1132 LYS B C   
2892 O O   . LYS B 95  ? 0.7181 0.7265 1.1541 -0.0120 -0.0248 0.0306  1132 LYS B O   
2893 C CB  . LYS B 95  ? 0.7631 0.7163 1.0648 -0.0360 -0.0140 0.0023  1132 LYS B CB  
2894 C CG  . LYS B 95  ? 0.7675 0.7234 1.0887 -0.0263 0.0077  -0.0041 1132 LYS B CG  
2895 C CD  . LYS B 95  ? 0.7750 0.7364 1.1555 -0.0098 0.0079  0.0087  1132 LYS B CD  
2896 C CE  . LYS B 95  ? 0.7976 0.7420 1.1826 0.0006  0.0296  0.0027  1132 LYS B CE  
2897 N NZ  . LYS B 95  ? 0.7956 0.7437 1.1495 0.0000  0.0564  -0.0158 1132 LYS B NZ  
2898 N N   . ASP B 96  ? 0.7546 0.7139 1.1219 -0.0339 -0.0722 0.0379  1133 ASP B N   
2899 C CA  . ASP B 96  ? 0.7593 0.7172 1.1811 -0.0311 -0.1027 0.0610  1133 ASP B CA  
2900 C C   . ASP B 96  ? 0.7230 0.7176 1.1937 -0.0267 -0.1020 0.0680  1133 ASP B C   
2901 O O   . ASP B 96  ? 0.7174 0.7294 1.2615 -0.0199 -0.1139 0.0882  1133 ASP B O   
2902 C CB  . ASP B 96  ? 0.8082 0.7168 1.1855 -0.0457 -0.1446 0.0723  1133 ASP B CB  
2903 C CG  . ASP B 96  ? 0.8459 0.7138 1.1815 -0.0504 -0.1494 0.0712  1133 ASP B CG  
2904 O OD1 . ASP B 96  ? 0.8299 0.7094 1.1728 -0.0429 -0.1206 0.0609  1133 ASP B OD1 
2905 O OD2 . ASP B 96  ? 0.8963 0.7150 1.1865 -0.0627 -0.1832 0.0811  1133 ASP B OD2 
2906 N N   . PHE B 97  ? 0.6973 0.7040 1.1324 -0.0308 -0.0885 0.0535  1134 PHE B N   
2907 C CA  . PHE B 97  ? 0.6643 0.7042 1.1390 -0.0275 -0.0852 0.0586  1134 PHE B CA  
2908 C C   . PHE B 97  ? 0.6366 0.7121 1.1782 -0.0118 -0.0555 0.0631  1134 PHE B C   
2909 O O   . PHE B 97  ? 0.6260 0.7075 1.1496 -0.0049 -0.0222 0.0471  1134 PHE B O   
2910 C CB  . PHE B 97  ? 0.6475 0.6938 1.0714 -0.0322 -0.0697 0.0401  1134 PHE B CB  
2911 C CG  . PHE B 97  ? 0.6750 0.6845 1.0339 -0.0443 -0.0914 0.0364  1134 PHE B CG  
2912 C CD1 . PHE B 97  ? 0.7185 0.6848 1.0562 -0.0533 -0.1279 0.0494  1134 PHE B CD1 
2913 C CD2 . PHE B 97  ? 0.6643 0.6771 0.9798 -0.0463 -0.0744 0.0205  1134 PHE B CD2 
2914 C CE1 . PHE B 97  ? 0.7601 0.6803 1.0232 -0.0635 -0.1432 0.0446  1134 PHE B CE1 
2915 C CE2 . PHE B 97  ? 0.6998 0.6734 0.9527 -0.0543 -0.0869 0.0168  1134 PHE B CE2 
2916 C CZ  . PHE B 97  ? 0.7512 0.6751 0.9723 -0.0627 -0.1194 0.0279  1134 PHE B CZ  
2917 N N   . SER B 98  ? 0.6311 0.7256 1.2488 -0.0068 -0.0682 0.0865  1135 SER B N   
2918 C CA  . SER B 98  ? 0.6145 0.7402 1.3024 0.0103  -0.0356 0.0952  1135 SER B CA  
2919 C C   . SER B 98  ? 0.5956 0.7529 1.3455 0.0100  -0.0416 0.1141  1135 SER B C   
2920 O O   . SER B 98  ? 0.6029 0.7652 1.4150 0.0062  -0.0743 0.1404  1135 SER B O   
2921 C CB  . SER B 98  ? 0.6328 0.7506 1.3723 0.0208  -0.0381 0.1105  1135 SER B CB  
2922 O OG  . SER B 98  ? 0.6256 0.7699 1.4352 0.0405  -0.0003 0.1203  1135 SER B OG  
2923 N N   . HIS B 99  ? 0.5735 0.7498 1.3061 0.0124  -0.0130 0.1021  1136 HIS B N   
2924 C CA  . HIS B 99  ? 0.5557 0.7611 1.3405 0.0113  -0.0143 0.1187  1136 HIS B CA  
2925 C C   . HIS B 99  ? 0.5444 0.7670 1.3186 0.0217  0.0343  0.1067  1136 HIS B C   
2926 O O   . HIS B 99  ? 0.5457 0.7532 1.2486 0.0216  0.0533  0.0814  1136 HIS B O   
2927 C CB  . HIS B 99  ? 0.5553 0.7480 1.3009 -0.0071 -0.0547 0.1176  1136 HIS B CB  
2928 C CG  . HIS B 99  ? 0.5476 0.7630 1.3532 -0.0127 -0.0715 0.1405  1136 HIS B CG  
2929 N ND1 . HIS B 99  ? 0.5569 0.7848 1.4507 -0.0148 -0.0984 0.1727  1136 HIS B ND1 
2930 C CD2 . HIS B 99  ? 0.5353 0.7626 1.3264 -0.0180 -0.0670 0.1367  1136 HIS B CD2 
2931 C CE1 . HIS B 99  ? 0.5487 0.7960 1.4818 -0.0222 -0.1097 0.1887  1136 HIS B CE1 
2932 N NE2 . HIS B 99  ? 0.5360 0.7819 1.4031 -0.0239 -0.0896 0.1658  1136 HIS B NE2 
2933 N N   . PRO B 100 ? 0.5379 0.7894 1.3812 0.0298  0.0552  0.1259  1137 PRO B N   
2934 C CA  . PRO B 100 ? 0.5402 0.7984 1.3643 0.0396  0.1034  0.1159  1137 PRO B CA  
2935 C C   . PRO B 100 ? 0.5284 0.7856 1.2906 0.0274  0.0977  0.1004  1137 PRO B C   
2936 O O   . PRO B 100 ? 0.5400 0.7933 1.2669 0.0325  0.1319  0.0890  1137 PRO B O   
2937 C CB  . PRO B 100 ? 0.5414 0.8304 1.4659 0.0507  0.1256  0.1466  1137 PRO B CB  
2938 C CG  . PRO B 100 ? 0.5392 0.8392 1.5454 0.0488  0.0885  0.1731  1137 PRO B CG  
2939 C CD  . PRO B 100 ? 0.5353 0.8115 1.4802 0.0294  0.0343  0.1608  1137 PRO B CD  
2940 N N   . ASN B 101 ? 0.5130 0.7678 1.2588 0.0117  0.0542  0.1008  1138 ASN B N   
2941 C CA  . ASN B 101 ? 0.5030 0.7540 1.1917 0.0015  0.0463  0.0863  1138 ASN B CA  
2942 C C   . ASN B 101 ? 0.5034 0.7289 1.1237 -0.0074 0.0218  0.0667  1138 ASN B C   
2943 O O   . ASN B 101 ? 0.4981 0.7163 1.0869 -0.0173 -0.0006 0.0621  1138 ASN B O   
2944 C CB  . ASN B 101 ? 0.4946 0.7620 1.2248 -0.0072 0.0237  0.1058  1138 ASN B CB  
2945 C CG  . ASN B 101 ? 0.4926 0.7881 1.2968 0.0010  0.0522  0.1283  1138 ASN B CG  
2946 O OD1 . ASN B 101 ? 0.4913 0.8045 1.3747 -0.0013 0.0346  0.1560  1138 ASN B OD1 
2947 N ND2 . ASN B 101 ? 0.4985 0.7950 1.2772 0.0101  0.0959  0.1184  1138 ASN B ND2 
2948 N N   . VAL B 102 ? 0.5117 0.7213 1.1093 -0.0032 0.0294  0.0560  1139 VAL B N   
2949 C CA  . VAL B 102 ? 0.5156 0.7020 1.0493 -0.0105 0.0164  0.0378  1139 VAL B CA  
2950 C C   . VAL B 102 ? 0.5195 0.6966 1.0231 -0.0045 0.0440  0.0219  1139 VAL B C   
2951 O O   . VAL B 102 ? 0.5304 0.7037 1.0607 0.0045  0.0576  0.0272  1139 VAL B O   
2952 C CB  . VAL B 102 ? 0.5311 0.6957 1.0653 -0.0174 -0.0183 0.0467  1139 VAL B CB  
2953 C CG1 . VAL B 102 ? 0.5439 0.6814 1.0111 -0.0234 -0.0229 0.0291  1139 VAL B CG1 
2954 C CG2 . VAL B 102 ? 0.5361 0.6980 1.0884 -0.0263 -0.0518 0.0621  1139 VAL B CG2 
2955 N N   . LEU B 103 ? 0.5134 0.6848 0.9641 -0.0097 0.0504  0.0039  1140 LEU B N   
2956 C CA  . LEU B 103 ? 0.5253 0.6829 0.9417 -0.0084 0.0694  -0.0108 1140 LEU B CA  
2957 C C   . LEU B 103 ? 0.5335 0.6728 0.9261 -0.0144 0.0557  -0.0163 1140 LEU B C   
2958 O O   . LEU B 103 ? 0.5298 0.6657 0.8892 -0.0228 0.0482  -0.0250 1140 LEU B O   
2959 C CB  . LEU B 103 ? 0.5225 0.6836 0.9022 -0.0135 0.0776  -0.0230 1140 LEU B CB  
2960 C CG  . LEU B 103 ? 0.5443 0.6859 0.8854 -0.0152 0.0927  -0.0366 1140 LEU B CG  
2961 C CD1 . LEU B 103 ? 0.5707 0.6977 0.9150 -0.0044 0.1194  -0.0350 1140 LEU B CD1 
2962 C CD2 . LEU B 103 ? 0.5427 0.6874 0.8512 -0.0246 0.0878  -0.0457 1140 LEU B CD2 
2963 N N   . SER B 104 ? 0.5486 0.6758 0.9620 -0.0093 0.0542  -0.0091 1141 SER B N   
2964 C CA  . SER B 104 ? 0.5641 0.6691 0.9537 -0.0150 0.0423  -0.0124 1141 SER B CA  
2965 C C   . SER B 104 ? 0.5768 0.6677 0.9333 -0.0166 0.0599  -0.0267 1141 SER B C   
2966 O O   . SER B 104 ? 0.5847 0.6729 0.9422 -0.0096 0.0804  -0.0312 1141 SER B O   
2967 C CB  . SER B 104 ? 0.5772 0.6720 1.0032 -0.0099 0.0286  0.0030  1141 SER B CB  
2968 O OG  . SER B 104 ? 0.5837 0.6822 1.0467 0.0035  0.0499  0.0078  1141 SER B OG  
2969 N N   . LEU B 105 ? 0.5838 0.6606 0.9077 -0.0266 0.0519  -0.0329 1142 LEU B N   
2970 C CA  . LEU B 105 ? 0.5980 0.6605 0.8928 -0.0323 0.0624  -0.0442 1142 LEU B CA  
2971 C C   . LEU B 105 ? 0.6210 0.6591 0.9214 -0.0254 0.0687  -0.0427 1142 LEU B C   
2972 O O   . LEU B 105 ? 0.6240 0.6554 0.9482 -0.0197 0.0592  -0.0317 1142 LEU B O   
2973 C CB  . LEU B 105 ? 0.5991 0.6573 0.8677 -0.0451 0.0544  -0.0471 1142 LEU B CB  
2974 C CG  . LEU B 105 ? 0.6133 0.6521 0.8742 -0.0477 0.0412  -0.0390 1142 LEU B CG  
2975 C CD1 . LEU B 105 ? 0.6390 0.6513 0.8932 -0.0486 0.0412  -0.0381 1142 LEU B CD1 
2976 C CD2 . LEU B 105 ? 0.6171 0.6548 0.8521 -0.0570 0.0407  -0.0403 1142 LEU B CD2 
2977 N N   . LEU B 106 ? 0.6415 0.6617 0.9178 -0.0263 0.0825  -0.0531 1143 LEU B N   
2978 C CA  . LEU B 106 ? 0.6738 0.6621 0.9448 -0.0203 0.0902  -0.0544 1143 LEU B CA  
2979 C C   . LEU B 106 ? 0.6851 0.6577 0.9396 -0.0320 0.0755  -0.0534 1143 LEU B C   
2980 O O   . LEU B 106 ? 0.6979 0.6537 0.9652 -0.0267 0.0699  -0.0458 1143 LEU B O   
2981 C CB  . LEU B 106 ? 0.7054 0.6679 0.9402 -0.0203 0.1070  -0.0671 1143 LEU B CB  
2982 C CG  . LEU B 106 ? 0.7082 0.6760 0.9454 -0.0094 0.1261  -0.0685 1143 LEU B CG  
2983 C CD1 . LEU B 106 ? 0.7628 0.6852 0.9475 -0.0091 0.1426  -0.0814 1143 LEU B CD1 
2984 C CD2 . LEU B 106 ? 0.6986 0.6800 0.9888 0.0098  0.1386  -0.0551 1143 LEU B CD2 
2985 N N   . GLY B 107 ? 0.6832 0.6613 0.9128 -0.0480 0.0699  -0.0589 1144 GLY B N   
2986 C CA  . GLY B 107 ? 0.6964 0.6626 0.9111 -0.0604 0.0604  -0.0559 1144 GLY B CA  
2987 C C   . GLY B 107 ? 0.6943 0.6725 0.8944 -0.0767 0.0601  -0.0600 1144 GLY B C   
2988 O O   . GLY B 107 ? 0.6813 0.6747 0.8816 -0.0792 0.0627  -0.0655 1144 GLY B O   
2989 N N   . ILE B 108 ? 0.7113 0.6810 0.9015 -0.0880 0.0570  -0.0550 1145 ILE B N   
2990 C CA  . ILE B 108 ? 0.7123 0.6965 0.9021 -0.1033 0.0592  -0.0538 1145 ILE B CA  
2991 C C   . ILE B 108 ? 0.7455 0.7062 0.9232 -0.1169 0.0559  -0.0555 1145 ILE B C   
2992 O O   . ILE B 108 ? 0.7701 0.6997 0.9336 -0.1163 0.0538  -0.0544 1145 ILE B O   
2993 C CB  . ILE B 108 ? 0.7137 0.7012 0.8994 -0.1063 0.0639  -0.0451 1145 ILE B CB  
2994 C CG1 . ILE B 108 ? 0.6995 0.6941 0.8855 -0.0935 0.0617  -0.0434 1145 ILE B CG1 
2995 C CG2 . ILE B 108 ? 0.7083 0.7178 0.9072 -0.1186 0.0729  -0.0409 1145 ILE B CG2 
2996 C CD1 . ILE B 108 ? 0.7205 0.6972 0.8824 -0.0954 0.0648  -0.0359 1145 ILE B CD1 
2997 N N   . CYS B 109 ? 0.7527 0.7255 0.9372 -0.1302 0.0521  -0.0567 1146 CYS B N   
2998 C CA  . CYS B 109 ? 0.7936 0.7417 0.9669 -0.1472 0.0435  -0.0566 1146 CYS B CA  
2999 C C   . CYS B 109 ? 0.7971 0.7680 0.9966 -0.1653 0.0439  -0.0444 1146 CYS B C   
3000 O O   . CYS B 109 ? 0.7814 0.7824 1.0073 -0.1724 0.0402  -0.0405 1146 CYS B O   
3001 C CB  . CYS B 109 ? 0.8126 0.7442 0.9681 -0.1509 0.0331  -0.0660 1146 CYS B CB  
3002 S SG  . CYS B 109 ? 0.8644 0.7522 0.9958 -0.1747 0.0153  -0.0662 1146 CYS B SG  
3003 N N   . LEU B 110 ? 0.8240 0.7797 1.0194 -0.1723 0.0496  -0.0364 1147 LEU B N   
3004 C CA  . LEU B 110 ? 0.8358 0.8091 1.0588 -0.1898 0.0555  -0.0219 1147 LEU B CA  
3005 C C   . LEU B 110 ? 0.8690 0.8294 1.0997 -0.2119 0.0365  -0.0190 1147 LEU B C   
3006 O O   . LEU B 110 ? 0.8999 0.8201 1.0968 -0.2134 0.0227  -0.0287 1147 LEU B O   
3007 C CB  . LEU B 110 ? 0.8572 0.8101 1.0634 -0.1900 0.0697  -0.0137 1147 LEU B CB  
3008 C CG  . LEU B 110 ? 0.8471 0.8075 1.0428 -0.1744 0.0871  -0.0119 1147 LEU B CG  
3009 C CD1 . LEU B 110 ? 0.8400 0.7847 1.0106 -0.1558 0.0778  -0.0230 1147 LEU B CD1 
3010 C CD2 . LEU B 110 ? 0.8814 0.8184 1.0574 -0.1809 0.1031  0.0001  1147 LEU B CD2 
3011 N N   . ARG B 111 ? 0.8710 0.8628 1.1476 -0.2287 0.0356  -0.0043 1148 ARG B N   
3012 C CA  . ARG B 111 ? 0.9083 0.8883 1.1997 -0.2545 0.0125  0.0034  1148 ARG B CA  
3013 C C   . ARG B 111 ? 0.9072 0.9270 1.2636 -0.2710 0.0224  0.0272  1148 ARG B C   
3014 O O   . ARG B 111 ? 0.8816 0.9397 1.2702 -0.2597 0.0474  0.0348  1148 ARG B O   
3015 C CB  . ARG B 111 ? 0.9162 0.8886 1.1969 -0.2588 -0.0145 -0.0058 1148 ARG B CB  
3016 C CG  . ARG B 111 ? 0.8792 0.9012 1.2047 -0.2555 -0.0150 0.0002  1148 ARG B CG  
3017 C CD  . ARG B 111 ? 0.8974 0.9000 1.1973 -0.2602 -0.0436 -0.0094 1148 ARG B CD  
3018 N NE  . ARG B 111 ? 0.8747 0.9202 1.2275 -0.2676 -0.0563 0.0029  1148 ARG B NE  
3019 C CZ  . ARG B 111 ? 0.8267 0.9172 1.2126 -0.2506 -0.0376 0.0054  1148 ARG B CZ  
3020 N NH1 . ARG B 111 ? 0.7975 0.8918 1.1616 -0.2265 -0.0089 -0.0049 1148 ARG B NH1 
3021 N NH2 . ARG B 111 ? 0.8120 0.9406 1.2535 -0.2584 -0.0506 0.0195  1148 ARG B NH2 
3022 N N   . SER B 112 ? 0.9431 0.9502 1.3188 -0.2975 0.0038  0.0399  1149 SER B N   
3023 C CA  . SER B 112 ? 0.9449 0.9891 1.3922 -0.3157 0.0138  0.0668  1149 SER B CA  
3024 C C   . SER B 112 ? 0.9339 1.0182 1.4469 -0.3295 -0.0088 0.0802  1149 SER B C   
3025 O O   . SER B 112 ? 0.9284 1.0551 1.5199 -0.3421 0.0008  0.1059  1149 SER B O   
3026 C CB  . SER B 112 ? 0.9885 0.9998 1.4303 -0.3390 0.0045  0.0774  1149 SER B CB  
3027 O OG  . SER B 112 ? 1.0036 0.9801 1.3912 -0.3264 0.0262  0.0689  1149 SER B OG  
3028 N N   . GLU B 113 ? 0.9364 1.0054 1.4188 -0.3271 -0.0383 0.0647  1150 GLU B N   
3029 C CA  . GLU B 113 ? 0.9316 1.0290 1.4659 -0.3414 -0.0679 0.0769  1150 GLU B CA  
3030 C C   . GLU B 113 ? 0.8770 1.0373 1.4742 -0.3236 -0.0399 0.0871  1150 GLU B C   
3031 O O   . GLU B 113 ? 0.8685 1.0751 1.5536 -0.3352 -0.0369 0.1135  1150 GLU B O   
3032 C CB  . GLU B 113 ? 0.9594 1.0122 1.4265 -0.3414 -0.1025 0.0559  1150 GLU B CB  
3033 C CG  . GLU B 113 ? 1.0253 1.0068 1.4268 -0.3596 -0.1314 0.0463  1150 GLU B CG  
3034 C CD  . GLU B 113 ? 1.0680 0.9940 1.3924 -0.3590 -0.1603 0.0259  1150 GLU B CD  
3035 O OE1 . GLU B 113 ? 1.0504 0.9683 1.3287 -0.3319 -0.1395 0.0057  1150 GLU B OE1 
3036 O OE2 . GLU B 113 ? 1.1261 1.0129 1.4344 -0.3865 -0.2037 0.0313  1150 GLU B OE2 
3037 N N   . GLY B 114 ? 0.8434 1.0033 1.3979 -0.2951 -0.0191 0.0675  1151 GLY B N   
3038 C CA  . GLY B 114 ? 0.7985 1.0064 1.3965 -0.2755 0.0065  0.0729  1151 GLY B CA  
3039 C C   . GLY B 114 ? 0.7774 0.9753 1.3271 -0.2477 0.0447  0.0577  1151 GLY B C   
3040 O O   . GLY B 114 ? 0.7938 0.9631 1.3061 -0.2465 0.0605  0.0539  1151 GLY B O   
3041 N N   . SER B 115 ? 0.7449 0.9629 1.2947 -0.2271 0.0555  0.0504  1152 SER B N   
3042 C CA  . SER B 115 ? 0.7315 0.9372 1.2359 -0.2025 0.0850  0.0374  1152 SER B CA  
3043 C C   . SER B 115 ? 0.7333 0.8972 1.1643 -0.1955 0.0697  0.0152  1152 SER B C   
3044 O O   . SER B 115 ? 0.7424 0.8900 1.1565 -0.2048 0.0410  0.0077  1152 SER B O   
3045 C CB  . SER B 115 ? 0.7042 0.9421 1.2356 -0.1848 0.0992  0.0388  1152 SER B CB  
3046 O OG  . SER B 115 ? 0.7013 0.9784 1.3087 -0.1883 0.1181  0.0613  1152 SER B OG  
3047 N N   . PRO B 116 ? 0.7296 0.8710 1.1148 -0.1790 0.0882  0.0054  1153 PRO B N   
3048 C CA  . PRO B 116 ? 0.7337 0.8398 1.0639 -0.1709 0.0759  -0.0114 1153 PRO B CA  
3049 C C   . PRO B 116 ? 0.7119 0.8240 1.0331 -0.1618 0.0608  -0.0230 1153 PRO B C   
3050 O O   . PRO B 116 ? 0.6888 0.8313 1.0377 -0.1570 0.0620  -0.0199 1153 PRO B O   
3051 C CB  . PRO B 116 ? 0.7383 0.8271 1.0362 -0.1556 0.0962  -0.0138 1153 PRO B CB  
3052 C CG  . PRO B 116 ? 0.7518 0.8507 1.0716 -0.1606 0.1215  0.0013  1153 PRO B CG  
3053 C CD  . PRO B 116 ? 0.7336 0.8765 1.1161 -0.1678 0.1211  0.0120  1153 PRO B CD  
3054 N N   . LEU B 117 ? 0.7218 0.8021 1.0039 -0.1587 0.0492  -0.0354 1154 LEU B N   
3055 C CA  . LEU B 117 ? 0.7113 0.7892 0.9769 -0.1491 0.0403  -0.0460 1154 LEU B CA  
3056 C C   . LEU B 117 ? 0.7016 0.7681 0.9447 -0.1296 0.0509  -0.0533 1154 LEU B C   
3057 O O   . LEU B 117 ? 0.7114 0.7581 0.9408 -0.1264 0.0569  -0.0525 1154 LEU B O   
3058 C CB  . LEU B 117 ? 0.7458 0.7895 0.9831 -0.1605 0.0221  -0.0528 1154 LEU B CB  
3059 C CG  . LEU B 117 ? 0.7643 0.8116 1.0219 -0.1842 0.0016  -0.0437 1154 LEU B CG  
3060 C CD1 . LEU B 117 ? 0.8136 0.8125 1.0240 -0.1945 -0.0194 -0.0529 1154 LEU B CD1 
3061 C CD2 . LEU B 117 ? 0.7353 0.8273 1.0388 -0.1862 -0.0028 -0.0339 1154 LEU B CD2 
3062 N N   . VAL B 118 ? 0.6837 0.7619 0.9261 -0.1181 0.0505  -0.0582 1155 VAL B N   
3063 C CA  . VAL B 118 ? 0.6739 0.7446 0.9053 -0.1012 0.0567  -0.0622 1155 VAL B CA  
3064 C C   . VAL B 118 ? 0.6836 0.7419 0.8996 -0.0953 0.0548  -0.0699 1155 VAL B C   
3065 O O   . VAL B 118 ? 0.6785 0.7470 0.8943 -0.0993 0.0491  -0.0715 1155 VAL B O   
3066 C CB  . VAL B 118 ? 0.6458 0.7402 0.8919 -0.0921 0.0619  -0.0577 1155 VAL B CB  
3067 C CG1 . VAL B 118 ? 0.6266 0.7494 0.8912 -0.0933 0.0593  -0.0568 1155 VAL B CG1 
3068 C CG2 . VAL B 118 ? 0.6408 0.7270 0.8818 -0.0779 0.0619  -0.0584 1155 VAL B CG2 
3069 N N   . VAL B 119 ? 0.7023 0.7351 0.9048 -0.0854 0.0610  -0.0733 1156 VAL B N   
3070 C CA  . VAL B 119 ? 0.7246 0.7360 0.9074 -0.0775 0.0678  -0.0801 1156 VAL B CA  
3071 C C   . VAL B 119 ? 0.7035 0.7297 0.9079 -0.0598 0.0778  -0.0761 1156 VAL B C   
3072 O O   . VAL B 119 ? 0.6949 0.7238 0.9190 -0.0523 0.0781  -0.0698 1156 VAL B O   
3073 C CB  . VAL B 119 ? 0.7678 0.7342 0.9225 -0.0779 0.0718  -0.0856 1156 VAL B CB  
3074 C CG1 . VAL B 119 ? 0.8052 0.7388 0.9292 -0.0679 0.0855  -0.0934 1156 VAL B CG1 
3075 C CG2 . VAL B 119 ? 0.7903 0.7413 0.9285 -0.0984 0.0576  -0.0867 1156 VAL B CG2 
3076 N N   . LEU B 120 ? 0.7001 0.7333 0.9009 -0.0550 0.0835  -0.0778 1157 LEU B N   
3077 C CA  . LEU B 120 ? 0.6821 0.7302 0.9083 -0.0400 0.0937  -0.0717 1157 LEU B CA  
3078 C C   . LEU B 120 ? 0.7167 0.7390 0.9211 -0.0310 0.1135  -0.0759 1157 LEU B C   
3079 O O   . LEU B 120 ? 0.7516 0.7453 0.9116 -0.0390 0.1139  -0.0847 1157 LEU B O   
3080 C CB  . LEU B 120 ? 0.6457 0.7282 0.8897 -0.0426 0.0844  -0.0672 1157 LEU B CB  
3081 C CG  . LEU B 120 ? 0.6206 0.7209 0.8777 -0.0490 0.0710  -0.0633 1157 LEU B CG  
3082 C CD1 . LEU B 120 ? 0.6237 0.7281 0.8684 -0.0628 0.0640  -0.0672 1157 LEU B CD1 
3083 C CD2 . LEU B 120 ? 0.5943 0.7174 0.8724 -0.0438 0.0657  -0.0566 1157 LEU B CD2 
3084 N N   . PRO B 121 ? 0.7134 0.7409 0.9471 -0.0146 0.1309  -0.0682 1158 PRO B N   
3085 C CA  . PRO B 121 ? 0.7535 0.7548 0.9669 -0.0033 0.1583  -0.0703 1158 PRO B CA  
3086 C C   . PRO B 121 ? 0.7610 0.7619 0.9419 -0.0110 0.1573  -0.0742 1158 PRO B C   
3087 O O   . PRO B 121 ? 0.7223 0.7596 0.9280 -0.0158 0.1433  -0.0684 1158 PRO B O   
3088 C CB  . PRO B 121 ? 0.7345 0.7587 1.0090 0.0140  0.1738  -0.0550 1158 PRO B CB  
3089 C CG  . PRO B 121 ? 0.6986 0.7454 1.0145 0.0114  0.1503  -0.0469 1158 PRO B CG  
3090 C CD  . PRO B 121 ? 0.6783 0.7335 0.9665 -0.0067 0.1248  -0.0548 1158 PRO B CD  
3091 N N   . TYR B 122 ? 0.8206 0.7732 0.9402 -0.0124 0.1709  -0.0838 1159 TYR B N   
3092 C CA  . TYR B 122 ? 0.8427 0.7838 0.9200 -0.0221 0.1654  -0.0872 1159 TYR B CA  
3093 C C   . TYR B 122 ? 0.8275 0.7903 0.9317 -0.0104 0.1853  -0.0768 1159 TYR B C   
3094 O O   . TYR B 122 ? 0.8400 0.7999 0.9698 0.0069  0.2156  -0.0699 1159 TYR B O   
3095 C CB  . TYR B 122 ? 0.9303 0.8002 0.9226 -0.0275 0.1732  -0.0994 1159 TYR B CB  
3096 C CG  . TYR B 122 ? 0.9691 0.8163 0.9086 -0.0384 0.1652  -0.1014 1159 TYR B CG  
3097 C CD1 . TYR B 122 ? 0.9384 0.8148 0.8877 -0.0564 0.1289  -0.0991 1159 TYR B CD1 
3098 C CD2 . TYR B 122 ? 1.0424 0.8368 0.9227 -0.0298 0.1954  -0.1039 1159 TYR B CD2 
3099 C CE1 . TYR B 122 ? 0.9747 0.8295 0.8785 -0.0671 0.1169  -0.0988 1159 TYR B CE1 
3100 C CE2 . TYR B 122 ? 1.0852 0.8520 0.9091 -0.0412 0.1857  -0.1047 1159 TYR B CE2 
3101 C CZ  . TYR B 122 ? 1.0497 0.8477 0.8868 -0.0606 0.1434  -0.1018 1159 TYR B CZ  
3102 O OH  . TYR B 122 ? 1.0946 0.8639 0.8782 -0.0726 0.1291  -0.1007 1159 TYR B OH  
3103 N N   . MET B 123 ? 0.8023 0.7871 0.9053 -0.0203 0.1680  -0.0740 1160 MET B N   
3104 C CA  . MET B 123 ? 0.7825 0.7901 0.9117 -0.0129 0.1812  -0.0630 1160 MET B CA  
3105 C C   . MET B 123 ? 0.8401 0.8062 0.9005 -0.0188 0.1889  -0.0670 1160 MET B C   
3106 O O   . MET B 123 ? 0.8419 0.8022 0.8703 -0.0347 0.1607  -0.0716 1160 MET B O   
3107 C CB  . MET B 123 ? 0.7142 0.7756 0.8944 -0.0192 0.1535  -0.0556 1160 MET B CB  
3108 C CG  . MET B 123 ? 0.6684 0.7609 0.9061 -0.0140 0.1454  -0.0500 1160 MET B CG  
3109 S SD  . MET B 123 ? 0.6582 0.7702 0.9602 0.0029  0.1684  -0.0324 1160 MET B SD  
3110 C CE  . MET B 123 ? 0.6982 0.7751 0.9912 0.0153  0.1947  -0.0366 1160 MET B CE  
3111 N N   . LYS B 124 ? 0.8913 0.8261 0.9304 -0.0056 0.2282  -0.0635 1161 LYS B N   
3112 C CA  . LYS B 124 ? 0.9778 0.8499 0.9287 -0.0096 0.2430  -0.0692 1161 LYS B CA  
3113 C C   . LYS B 124 ? 0.9685 0.8556 0.9080 -0.0228 0.2195  -0.0642 1161 LYS B C   
3114 O O   . LYS B 124 ? 1.0105 0.8621 0.8862 -0.0392 0.1936  -0.0716 1161 LYS B O   
3115 C CB  . LYS B 124 ? 1.0308 0.8718 0.9725 0.0108  0.2986  -0.0630 1161 LYS B CB  
3116 C CG  . LYS B 124 ? 1.1406 0.8966 0.9713 0.0093  0.3232  -0.0706 1161 LYS B CG  
3117 C CD  . LYS B 124 ? 1.2021 0.9216 1.0235 0.0333  0.3875  -0.0647 1161 LYS B CD  
3118 C CE  . LYS B 124 ? 1.3298 0.9479 1.0215 0.0323  0.4157  -0.0743 1161 LYS B CE  
3119 N NZ  . LYS B 124 ? 1.3502 0.9588 0.9986 0.0180  0.4027  -0.0690 1161 LYS B NZ  
3120 N N   . HIS B 125 ? 0.9177 0.8554 0.9215 -0.0166 0.2252  -0.0501 1162 HIS B N   
3121 C CA  . HIS B 125 ? 0.9135 0.8611 0.9071 -0.0261 0.2095  -0.0434 1162 HIS B CA  
3122 C C   . HIS B 125 ? 0.8447 0.8415 0.8815 -0.0375 0.1644  -0.0432 1162 HIS B C   
3123 O O   . HIS B 125 ? 0.8338 0.8453 0.8740 -0.0443 0.1475  -0.0370 1162 HIS B O   
3124 C CB  . HIS B 125 ? 0.9070 0.8751 0.9419 -0.0142 0.2420  -0.0267 1162 HIS B CB  
3125 C CG  . HIS B 125 ? 0.9905 0.9034 0.9738 -0.0028 0.2925  -0.0247 1162 HIS B CG  
3126 N ND1 . HIS B 125 ? 1.0805 0.9219 0.9591 -0.0102 0.3009  -0.0323 1162 HIS B ND1 
3127 C CD2 . HIS B 125 ? 1.0022 0.9183 1.0261 0.0163  0.3393  -0.0145 1162 HIS B CD2 
3128 C CE1 . HIS B 125 ? 1.1494 0.9463 0.9962 0.0050  0.3556  -0.0286 1162 HIS B CE1 
3129 N NE2 . HIS B 125 ? 1.0988 0.9454 1.0419 0.0228  0.3820  -0.0168 1162 HIS B NE2 
3130 N N   . GLY B 126 ? 0.8048 0.8233 0.8727 -0.0387 0.1476  -0.0494 1163 GLY B N   
3131 C CA  . GLY B 126 ? 0.7550 0.8071 0.8502 -0.0490 0.1105  -0.0508 1163 GLY B CA  
3132 C C   . GLY B 126 ? 0.6891 0.7923 0.8499 -0.0438 0.1031  -0.0410 1163 GLY B C   
3133 O O   . GLY B 126 ? 0.6685 0.7876 0.8672 -0.0333 0.1210  -0.0330 1163 GLY B O   
3134 N N   . ASP B 127 ? 0.6597 0.7845 0.8337 -0.0513 0.0755  -0.0403 1164 ASP B N   
3135 C CA  . ASP B 127 ? 0.6078 0.7703 0.8321 -0.0471 0.0651  -0.0335 1164 ASP B CA  
3136 C C   . ASP B 127 ? 0.6078 0.7745 0.8391 -0.0445 0.0714  -0.0228 1164 ASP B C   
3137 O O   . ASP B 127 ? 0.6460 0.7883 0.8396 -0.0477 0.0803  -0.0209 1164 ASP B O   
3138 C CB  . ASP B 127 ? 0.5864 0.7655 0.8219 -0.0530 0.0399  -0.0362 1164 ASP B CB  
3139 C CG  . ASP B 127 ? 0.6075 0.7783 0.8210 -0.0613 0.0231  -0.0338 1164 ASP B CG  
3140 O OD1 . ASP B 127 ? 0.6302 0.7867 0.8221 -0.0708 0.0101  -0.0376 1164 ASP B OD1 
3141 O OD2 . ASP B 127 ? 0.6037 0.7810 0.8236 -0.0594 0.0198  -0.0267 1164 ASP B OD2 
3142 N N   . LEU B 128 ? 0.5702 0.7628 0.8451 -0.0403 0.0650  -0.0152 1165 LEU B N   
3143 C CA  . LEU B 128 ? 0.5705 0.7700 0.8641 -0.0385 0.0706  -0.0021 1165 LEU B CA  
3144 C C   . LEU B 128 ? 0.5759 0.7733 0.8520 -0.0444 0.0541  0.0001  1165 LEU B C   
3145 O O   . LEU B 128 ? 0.5984 0.7882 0.8661 -0.0461 0.0626  0.0094  1165 LEU B O   
3146 C CB  . LEU B 128 ? 0.5384 0.7589 0.8816 -0.0346 0.0623  0.0058  1165 LEU B CB  
3147 C CG  . LEU B 128 ? 0.5364 0.7668 0.9123 -0.0348 0.0644  0.0230  1165 LEU B CG  
3148 C CD1 . LEU B 128 ? 0.5578 0.7847 0.9461 -0.0300 0.0968  0.0331  1165 LEU B CD1 
3149 C CD2 . LEU B 128 ? 0.5126 0.7548 0.9282 -0.0351 0.0437  0.0303  1165 LEU B CD2 
3150 N N   . ARG B 129 ? 0.5590 0.7626 0.8328 -0.0470 0.0322  -0.0067 1166 ARG B N   
3151 C CA  . ARG B 129 ? 0.5616 0.7658 0.8295 -0.0505 0.0141  -0.0030 1166 ARG B CA  
3152 C C   . ARG B 129 ? 0.6049 0.7840 0.8277 -0.0584 0.0136  -0.0024 1166 ARG B C   
3153 O O   . ARG B 129 ? 0.6250 0.7944 0.8340 -0.0614 0.0115  0.0059  1166 ARG B O   
3154 C CB  . ARG B 129 ? 0.5402 0.7573 0.8244 -0.0487 -0.0039 -0.0085 1166 ARG B CB  
3155 C CG  . ARG B 129 ? 0.5407 0.7611 0.8331 -0.0476 -0.0207 -0.0027 1166 ARG B CG  
3156 C CD  . ARG B 129 ? 0.5357 0.7648 0.8415 -0.0459 -0.0347 -0.0056 1166 ARG B CD  
3157 N NE  . ARG B 129 ? 0.5411 0.7699 0.8549 -0.0435 -0.0496 0.0013  1166 ARG B NE  
3158 C CZ  . ARG B 129 ? 0.5443 0.7808 0.8769 -0.0413 -0.0632 0.0037  1166 ARG B CZ  
3159 N NH1 . ARG B 129 ? 0.5418 0.7893 0.8900 -0.0428 -0.0641 0.0008  1166 ARG B NH1 
3160 N NH2 . ARG B 129 ? 0.5521 0.7857 0.8929 -0.0376 -0.0760 0.0108  1166 ARG B NH2 
3161 N N   . ASN B 130 ? 0.6284 0.7912 0.8230 -0.0632 0.0132  -0.0106 1167 ASN B N   
3162 C CA  . ASN B 130 ? 0.6843 0.8109 0.8235 -0.0734 0.0065  -0.0107 1167 ASN B CA  
3163 C C   . ASN B 130 ? 0.7317 0.8273 0.8309 -0.0724 0.0348  -0.0066 1167 ASN B C   
3164 O O   . ASN B 130 ? 0.7866 0.8468 0.8339 -0.0801 0.0315  -0.0027 1167 ASN B O   
3165 C CB  . ASN B 130 ? 0.7030 0.8133 0.8197 -0.0810 -0.0040 -0.0196 1167 ASN B CB  
3166 C CG  . ASN B 130 ? 0.6733 0.8101 0.8282 -0.0845 -0.0324 -0.0188 1167 ASN B CG  
3167 O OD1 . ASN B 130 ? 0.6776 0.8178 0.8389 -0.0888 -0.0548 -0.0114 1167 ASN B OD1 
3168 N ND2 . ASN B 130 ? 0.6460 0.8010 0.8294 -0.0821 -0.0299 -0.0247 1167 ASN B ND2 
3169 N N   . PHE B 131 ? 0.7188 0.8254 0.8431 -0.0626 0.0633  -0.0057 1168 PHE B N   
3170 C CA  . PHE B 131 ? 0.7620 0.8446 0.8634 -0.0581 0.0983  0.0008  1168 PHE B CA  
3171 C C   . PHE B 131 ? 0.7676 0.8537 0.8742 -0.0603 0.0991  0.0150  1168 PHE B C   
3172 O O   . PHE B 131 ? 0.8250 0.8722 0.8767 -0.0646 0.1130  0.0195  1168 PHE B O   
3173 C CB  . PHE B 131 ? 0.7372 0.8409 0.8866 -0.0462 0.1241  0.0028  1168 PHE B CB  
3174 C CG  . PHE B 131 ? 0.7807 0.8623 0.9188 -0.0382 0.1676  0.0113  1168 PHE B CG  
3175 C CD1 . PHE B 131 ? 0.8259 0.8721 0.9265 -0.0321 0.1948  0.0031  1168 PHE B CD1 
3176 C CD2 . PHE B 131 ? 0.7798 0.8745 0.9479 -0.0358 0.1839  0.0287  1168 PHE B CD2 
3177 C CE1 . PHE B 131 ? 0.8733 0.8962 0.9654 -0.0214 0.2419  0.0117  1168 PHE B CE1 
3178 C CE2 . PHE B 131 ? 0.8225 0.8991 0.9887 -0.0269 0.2301  0.0394  1168 PHE B CE2 
3179 C CZ  . PHE B 131 ? 0.8703 0.9108 0.9987 -0.0184 0.2613  0.0307  1168 PHE B CZ  
3180 N N   . ILE B 132 ? 0.7148 0.8412 0.8813 -0.0580 0.0838  0.0221  1169 ILE B N   
3181 C CA  . ILE B 132 ? 0.7170 0.8494 0.8973 -0.0605 0.0822  0.0368  1169 ILE B CA  
3182 C C   . ILE B 132 ? 0.7458 0.8585 0.8849 -0.0698 0.0553  0.0363  1169 ILE B C   
3183 O O   . ILE B 132 ? 0.7761 0.8724 0.8946 -0.0745 0.0591  0.0477  1169 ILE B O   
3184 C CB  . ILE B 132 ? 0.6588 0.8304 0.9087 -0.0567 0.0698  0.0442  1169 ILE B CB  
3185 C CG1 . ILE B 132 ? 0.6203 0.8075 0.8844 -0.0562 0.0375  0.0337  1169 ILE B CG1 
3186 C CG2 . ILE B 132 ? 0.6426 0.8307 0.9369 -0.0493 0.0928  0.0496  1169 ILE B CG2 
3187 C CD1 . ILE B 132 ? 0.5828 0.7925 0.8965 -0.0530 0.0245  0.0389  1169 ILE B CD1 
3188 N N   . ARG B 133 ? 0.7385 0.8535 0.8707 -0.0726 0.0279  0.0255  1170 ARG B N   
3189 C CA  . ARG B 133 ? 0.7637 0.8632 0.8684 -0.0810 -0.0021 0.0271  1170 ARG B CA  
3190 C C   . ARG B 133 ? 0.8454 0.8912 0.8709 -0.0913 0.0018  0.0275  1170 ARG B C   
3191 O O   . ARG B 133 ? 0.8795 0.9012 0.8712 -0.0999 -0.0175 0.0349  1170 ARG B O   
3192 C CB  . ARG B 133 ? 0.7307 0.8510 0.8628 -0.0805 -0.0293 0.0188  1170 ARG B CB  
3193 C CG  . ARG B 133 ? 0.6755 0.8338 0.8682 -0.0711 -0.0382 0.0196  1170 ARG B CG  
3194 C CD  . ARG B 133 ? 0.6525 0.8292 0.8728 -0.0686 -0.0557 0.0129  1170 ARG B CD  
3195 N NE  . ARG B 133 ? 0.6777 0.8447 0.8885 -0.0758 -0.0831 0.0179  1170 ARG B NE  
3196 C CZ  . ARG B 133 ? 0.6847 0.8517 0.9054 -0.0751 -0.1013 0.0270  1170 ARG B CZ  
3197 N NH1 . ARG B 133 ? 0.6691 0.8443 0.9076 -0.0674 -0.0949 0.0306  1170 ARG B NH1 
3198 N NH2 . ARG B 133 ? 0.7135 0.8696 0.9274 -0.0829 -0.1292 0.0338  1170 ARG B NH2 
3199 N N   . ASN B 134 ? 0.8880 0.9088 0.8785 -0.0904 0.0258  0.0195  1171 ASN B N   
3200 C CA  . ASN B 134 ? 0.9837 0.9394 0.8837 -0.1001 0.0304  0.0171  1171 ASN B CA  
3201 C C   . ASN B 134 ? 1.0449 0.9666 0.9002 -0.1029 0.0496  0.0296  1171 ASN B C   
3202 O O   . ASN B 134 ? 1.0212 0.9670 0.9156 -0.0942 0.0790  0.0388  1171 ASN B O   
3203 C CB  . ASN B 134 ? 1.0113 0.9421 0.8822 -0.0952 0.0600  0.0061  1171 ASN B CB  
3204 C CG  . ASN B 134 ? 1.1138 0.9649 0.8783 -0.1066 0.0591  0.0005  1171 ASN B CG  
3205 O OD1 . ASN B 134 ? 1.1657 0.9793 0.8765 -0.1204 0.0307  0.0054  1171 ASN B OD1 
3206 N ND2 . ASN B 134 ? 1.1510 0.9695 0.8798 -0.1013 0.0877  -0.0093 1171 ASN B ND2 
3207 N N   . GLU B 135 ? 1.1329 0.9958 0.9057 -0.1167 0.0308  0.0318  1172 GLU B N   
3208 C CA  . GLU B 135 ? 1.2050 1.0254 0.9214 -0.1219 0.0454  0.0444  1172 GLU B CA  
3209 C C   . GLU B 135 ? 1.2846 1.0524 0.9356 -0.1165 0.1006  0.0434  1172 GLU B C   
3210 O O   . GLU B 135 ? 1.3068 1.0688 0.9560 -0.1117 0.1374  0.0561  1172 GLU B O   
3211 C CB  . GLU B 135 ? 1.2713 1.0423 0.9195 -0.1399 -0.0005 0.0482  1172 GLU B CB  
3212 C CG  . GLU B 135 ? 1.3422 1.0675 0.9300 -0.1471 0.0082  0.0629  1172 GLU B CG  
3213 C CD  . GLU B 135 ? 1.4140 1.0864 0.9335 -0.1661 -0.0430 0.0690  1172 GLU B CD  
3214 O OE1 . GLU B 135 ? 1.4815 1.1084 0.9413 -0.1738 -0.0387 0.0816  1172 GLU B OE1 
3215 O OE2 . GLU B 135 ? 1.4069 1.0830 0.9358 -0.1741 -0.0883 0.0633  1172 GLU B OE2 
3216 N N   . THR B 136 ? 1.3326 1.0596 0.9310 -0.1170 0.1076  0.0292  1173 THR B N   
3217 C CA  . THR B 136 ? 1.4146 1.0808 0.9418 -0.1095 0.1624  0.0261  1173 THR B CA  
3218 C C   . THR B 136 ? 1.3530 1.0752 0.9682 -0.0894 0.2134  0.0328  1173 THR B C   
3219 O O   . THR B 136 ? 1.4014 1.0978 0.9946 -0.0815 0.2646  0.0435  1173 THR B O   
3220 C CB  . THR B 136 ? 1.4714 1.0831 0.9297 -0.1141 0.1538  0.0085  1173 THR B CB  
3221 O OG1 . THR B 136 ? 1.3772 1.0565 0.9262 -0.1069 0.1400  -0.0001 1173 THR B OG1 
3222 C CG2 . THR B 136 ? 1.5449 1.0933 0.9141 -0.1370 0.0995  0.0054  1173 THR B CG2 
3223 N N   . HIS B 137 ? 1.2503 1.0464 0.9653 -0.0818 0.1986  0.0284  1174 HIS B N   
3224 C CA  . HIS B 137 ? 1.1805 1.0378 0.9937 -0.0664 0.2308  0.0383  1174 HIS B CA  
3225 C C   . HIS B 137 ? 1.1395 1.0344 1.0038 -0.0696 0.2234  0.0568  1174 HIS B C   
3226 O O   . HIS B 137 ? 1.1119 1.0219 0.9823 -0.0801 0.1784  0.0569  1174 HIS B O   
3227 C CB  . HIS B 137 ? 1.0957 1.0106 0.9874 -0.0604 0.2097  0.0287  1174 HIS B CB  
3228 C CG  . HIS B 137 ? 1.1255 1.0118 0.9864 -0.0542 0.2262  0.0139  1174 HIS B CG  
3229 N ND1 . HIS B 137 ? 1.1092 0.9959 0.9606 -0.0607 0.1910  -0.0012 1174 HIS B ND1 
3230 C CD2 . HIS B 137 ? 1.1740 1.0289 1.0150 -0.0408 0.2774  0.0138  1174 HIS B CD2 
3231 C CE1 . HIS B 137 ? 1.1462 1.0004 0.9677 -0.0534 0.2161  -0.0113 1174 HIS B CE1 
3232 N NE2 . HIS B 137 ? 1.1882 1.0209 1.0016 -0.0398 0.2707  -0.0028 1174 HIS B NE2 
3233 N N   . ASN B 138 ? 1.1362 1.0451 1.0409 -0.0605 0.2681  0.0739  1175 ASN B N   
3234 C CA  . ASN B 138 ? 1.1029 1.0446 1.0586 -0.0648 0.2636  0.0939  1175 ASN B CA  
3235 C C   . ASN B 138 ? 1.0548 1.0473 1.1116 -0.0529 0.2974  0.1111  1175 ASN B C   
3236 O O   . ASN B 138 ? 1.0942 1.0752 1.1575 -0.0486 0.3435  0.1299  1175 ASN B O   
3237 C CB  . ASN B 138 ? 1.1902 1.0720 1.0602 -0.0739 0.2796  0.1039  1175 ASN B CB  
3238 C CG  . ASN B 138 ? 1.1633 1.0734 1.0750 -0.0824 0.2617  0.1228  1175 ASN B CG  
3239 O OD1 . ASN B 138 ? 1.0794 1.0506 1.0807 -0.0818 0.2349  0.1276  1175 ASN B OD1 
3240 N ND2 . ASN B 138 ? 1.2417 1.1002 1.0812 -0.0910 0.2752  0.1337  1175 ASN B ND2 
3241 N N   . PRO B 139 ? 0.9720 1.0195 1.1115 -0.0479 0.2751  0.1073  1176 PRO B N   
3242 C CA  . PRO B 139 ? 0.9281 1.0242 1.1705 -0.0392 0.2961  0.1262  1176 PRO B CA  
3243 C C   . PRO B 139 ? 0.8945 1.0253 1.1987 -0.0484 0.2775  0.1479  1176 PRO B C   
3244 O O   . PRO B 139 ? 0.8726 1.0076 1.1632 -0.0588 0.2332  0.1424  1176 PRO B O   
3245 C CB  . PRO B 139 ? 0.8653 0.9939 1.1512 -0.0346 0.2675  0.1118  1176 PRO B CB  
3246 C CG  . PRO B 139 ? 0.8492 0.9686 1.0860 -0.0447 0.2185  0.0924  1176 PRO B CG  
3247 C CD  . PRO B 139 ? 0.9237 0.9865 1.0621 -0.0511 0.2281  0.0869  1176 PRO B CD  
3248 N N   . THR B 140 ? 0.8923 1.0467 1.2684 -0.0440 0.3119  0.1742  1177 THR B N   
3249 C CA  . THR B 140 ? 0.8636 1.0495 1.3057 -0.0544 0.2957  0.1989  1177 THR B CA  
3250 C C   . THR B 140 ? 0.7853 1.0148 1.2989 -0.0588 0.2438  0.1978  1177 THR B C   
3251 O O   . THR B 140 ? 0.7536 0.9925 1.2749 -0.0521 0.2301  0.1816  1177 THR B O   
3252 C CB  . THR B 140 ? 0.8926 1.0918 1.3987 -0.0490 0.3500  0.2308  1177 THR B CB  
3253 O OG1 . THR B 140 ? 0.8677 1.0964 1.4473 -0.0356 0.3693  0.2360  1177 THR B OG1 
3254 C CG2 . THR B 140 ? 0.9805 1.1254 1.4032 -0.0447 0.4060  0.2331  1177 THR B CG2 
3255 N N   . VAL B 141 ? 0.7606 1.0096 1.3203 -0.0710 0.2155  0.2158  1178 VAL B N   
3256 C CA  . VAL B 141 ? 0.7053 0.9808 1.3171 -0.0775 0.1636  0.2156  1178 VAL B CA  
3257 C C   . VAL B 141 ? 0.6750 0.9840 1.3752 -0.0716 0.1703  0.2295  1178 VAL B C   
3258 O O   . VAL B 141 ? 0.6354 0.9551 1.3571 -0.0729 0.1325  0.2211  1178 VAL B O   
3259 C CB  . VAL B 141 ? 0.7050 0.9842 1.3411 -0.0929 0.1336  0.2340  1178 VAL B CB  
3260 C CG1 . VAL B 141 ? 0.6658 0.9591 1.3445 -0.1002 0.0797  0.2340  1178 VAL B CG1 
3261 C CG2 . VAL B 141 ? 0.7341 0.9791 1.2860 -0.0980 0.1245  0.2218  1178 VAL B CG2 
3262 N N   . LYS B 142 ? 0.6973 1.0194 1.4480 -0.0648 0.2198  0.2524  1179 LYS B N   
3263 C CA  . LYS B 142 ? 0.6783 1.0328 1.5208 -0.0567 0.2323  0.2690  1179 LYS B CA  
3264 C C   . LYS B 142 ? 0.6616 1.0076 1.4701 -0.0455 0.2246  0.2411  1179 LYS B C   
3265 O O   . LYS B 142 ? 0.6288 0.9958 1.4931 -0.0459 0.1953  0.2448  1179 LYS B O   
3266 C CB  . LYS B 142 ? 0.7165 1.0778 1.6018 -0.0456 0.3008  0.2938  1179 LYS B CB  
3267 C CG  . LYS B 142 ? 0.6981 1.1012 1.7069 -0.0377 0.3160  0.3220  1179 LYS B CG  
3268 C CD  . LYS B 142 ? 0.6716 1.1143 1.7905 -0.0546 0.2780  0.3574  1179 LYS B CD  
3269 C CE  . LYS B 142 ? 0.6598 1.1460 1.9138 -0.0473 0.2948  0.3919  1179 LYS B CE  
3270 N NZ  . LYS B 142 ? 0.6440 1.1659 2.0085 -0.0671 0.2579  0.4316  1179 LYS B NZ  
3271 N N   . ASP B 143 ? 0.6905 1.0012 1.4043 -0.0372 0.2483  0.2146  1180 ASP B N   
3272 C CA  . ASP B 143 ? 0.6815 0.9798 1.3566 -0.0276 0.2447  0.1884  1180 ASP B CA  
3273 C C   . ASP B 143 ? 0.6407 0.9408 1.2937 -0.0366 0.1862  0.1694  1180 ASP B C   
3274 O O   . ASP B 143 ? 0.6143 0.9226 1.2856 -0.0327 0.1688  0.1610  1180 ASP B O   
3275 C CB  . ASP B 143 ? 0.7332 0.9864 1.3085 -0.0202 0.2798  0.1671  1180 ASP B CB  
3276 C CG  . ASP B 143 ? 0.7906 1.0263 1.3664 -0.0088 0.3456  0.1824  1180 ASP B CG  
3277 O OD1 . ASP B 143 ? 0.7864 1.0536 1.4533 -0.0057 0.3676  0.2124  1180 ASP B OD1 
3278 O OD2 . ASP B 143 ? 0.8470 1.0339 1.3309 -0.0033 0.3745  0.1655  1180 ASP B OD2 
3279 N N   . LEU B 144 ? 0.6400 0.9289 1.2522 -0.0476 0.1586  0.1638  1181 LEU B N   
3280 C CA  . LEU B 144 ? 0.6131 0.8963 1.1946 -0.0534 0.1113  0.1451  1181 LEU B CA  
3281 C C   . LEU B 144 ? 0.5842 0.8864 1.2287 -0.0584 0.0760  0.1560  1181 LEU B C   
3282 O O   . LEU B 144 ? 0.5686 0.8638 1.1935 -0.0578 0.0489  0.1396  1181 LEU B O   
3283 C CB  . LEU B 144 ? 0.6242 0.8915 1.1621 -0.0624 0.0935  0.1427  1181 LEU B CB  
3284 C CG  . LEU B 144 ? 0.6612 0.9003 1.1238 -0.0607 0.1162  0.1309  1181 LEU B CG  
3285 C CD1 . LEU B 144 ? 0.6728 0.8975 1.1016 -0.0699 0.0924  0.1316  1181 LEU B CD1 
3286 C CD2 . LEU B 144 ? 0.6604 0.8850 1.0725 -0.0543 0.1151  0.1051  1181 LEU B CD2 
3287 N N   . ILE B 145 ? 0.5860 0.9084 1.3046 -0.0645 0.0756  0.1854  1182 ILE B N   
3288 C CA  . ILE B 145 ? 0.5698 0.9048 1.3512 -0.0723 0.0376  0.2006  1182 ILE B CA  
3289 C C   . ILE B 145 ? 0.5582 0.9059 1.3771 -0.0624 0.0487  0.2012  1182 ILE B C   
3290 O O   . ILE B 145 ? 0.5460 0.8883 1.3741 -0.0662 0.0126  0.1981  1182 ILE B O   
3291 C CB  . ILE B 145 ? 0.5773 0.9310 1.4348 -0.0843 0.0310  0.2358  1182 ILE B CB  
3292 C CG1 . ILE B 145 ? 0.5917 0.9279 1.4082 -0.0951 0.0148  0.2349  1182 ILE B CG1 
3293 C CG2 . ILE B 145 ? 0.5675 0.9312 1.4960 -0.0944 -0.0120 0.2557  1182 ILE B CG2 
3294 C CD1 . ILE B 145 ? 0.6054 0.9592 1.4913 -0.1071 0.0176  0.2703  1182 ILE B CD1 
3295 N N   . GLY B 146 ? 0.5679 0.9258 1.4024 -0.0495 0.0995  0.2053  1183 GLY B N   
3296 C CA  . GLY B 146 ? 0.5612 0.9284 1.4302 -0.0373 0.1167  0.2058  1183 GLY B CA  
3297 C C   . GLY B 146 ? 0.5500 0.8953 1.3510 -0.0332 0.1004  0.1743  1183 GLY B C   
3298 O O   . GLY B 146 ? 0.5395 0.8888 1.3697 -0.0305 0.0852  0.1754  1183 GLY B O   
3299 N N   . PHE B 147 ? 0.5552 0.8774 1.2695 -0.0336 0.1029  0.1486  1184 PHE B N   
3300 C CA  . PHE B 147 ? 0.5446 0.8481 1.1976 -0.0311 0.0891  0.1206  1184 PHE B CA  
3301 C C   . PHE B 147 ? 0.5241 0.8236 1.1823 -0.0396 0.0411  0.1187  1184 PHE B C   
3302 O O   . PHE B 147 ? 0.5154 0.8064 1.1601 -0.0368 0.0304  0.1072  1184 PHE B O   
3303 C CB  . PHE B 147 ? 0.5577 0.8406 1.1311 -0.0323 0.0957  0.0997  1184 PHE B CB  
3304 C CG  . PHE B 147 ? 0.5918 0.8607 1.1316 -0.0255 0.1391  0.0968  1184 PHE B CG  
3305 C CD1 . PHE B 147 ? 0.6117 0.8828 1.1825 -0.0147 0.1780  0.1069  1184 PHE B CD1 
3306 C CD2 . PHE B 147 ? 0.6139 0.8609 1.0868 -0.0298 0.1407  0.0848  1184 PHE B CD2 
3307 C CE1 . PHE B 147 ? 0.6596 0.9041 1.1837 -0.0079 0.2207  0.1028  1184 PHE B CE1 
3308 C CE2 . PHE B 147 ? 0.6607 0.8815 1.0870 -0.0257 0.1772  0.0819  1184 PHE B CE2 
3309 C CZ  . PHE B 147 ? 0.6869 0.9029 1.1332 -0.0146 0.2188  0.0899  1184 PHE B CZ  
3310 N N   . GLY B 148 ? 0.5230 0.8215 1.1933 -0.0505 0.0131  0.1299  1185 GLY B N   
3311 C CA  . GLY B 148 ? 0.5238 0.8047 1.1855 -0.0594 -0.0324 0.1284  1185 GLY B CA  
3312 C C   . GLY B 148 ? 0.5245 0.8095 1.2413 -0.0623 -0.0527 0.1450  1185 GLY B C   
3313 O O   . GLY B 148 ? 0.5332 0.7939 1.2211 -0.0655 -0.0814 0.1359  1185 GLY B O   
3314 N N   . LEU B 149 ? 0.5199 0.8335 1.3169 -0.0609 -0.0368 0.1710  1186 LEU B N   
3315 C CA  . LEU B 149 ? 0.5197 0.8424 1.3867 -0.0636 -0.0575 0.1927  1186 LEU B CA  
3316 C C   . LEU B 149 ? 0.5149 0.8296 1.3595 -0.0528 -0.0471 0.1764  1186 LEU B C   
3317 O O   . LEU B 149 ? 0.5232 0.8211 1.3713 -0.0583 -0.0820 0.1795  1186 LEU B O   
3318 C CB  . LEU B 149 ? 0.5155 0.8765 1.4824 -0.0608 -0.0313 0.2253  1186 LEU B CB  
3319 C CG  . LEU B 149 ? 0.5168 0.8950 1.5805 -0.0641 -0.0545 0.2559  1186 LEU B CG  
3320 C CD1 . LEU B 149 ? 0.5318 0.8944 1.6174 -0.0862 -0.1188 0.2747  1186 LEU B CD1 
3321 C CD2 . LEU B 149 ? 0.5128 0.9331 1.6772 -0.0535 -0.0093 0.2852  1186 LEU B CD2 
3322 N N   . GLN B 150 ? 0.5073 0.8281 1.3234 -0.0387 -0.0008 0.1599  1187 GLN B N   
3323 C CA  . GLN B 150 ? 0.5060 0.8186 1.3020 -0.0282 0.0136  0.1451  1187 GLN B CA  
3324 C C   . GLN B 150 ? 0.5081 0.7902 1.2317 -0.0341 -0.0165 0.1222  1187 GLN B C   
3325 O O   . GLN B 150 ? 0.5143 0.7847 1.2360 -0.0324 -0.0279 0.1193  1187 GLN B O   
3326 C CB  . GLN B 150 ? 0.5112 0.8252 1.2762 -0.0148 0.0657  0.1309  1187 GLN B CB  
3327 C CG  . GLN B 150 ? 0.5212 0.8574 1.3535 -0.0048 0.1062  0.1536  1187 GLN B CG  
3328 C CD  . GLN B 150 ? 0.5448 0.8657 1.3261 0.0077  0.1573  0.1376  1187 GLN B CD  
3329 O OE1 . GLN B 150 ? 0.5557 0.8579 1.2976 0.0156  0.1703  0.1196  1187 GLN B OE1 
3330 N NE2 . GLN B 150 ? 0.5622 0.8848 1.3377 0.0082  0.1853  0.1447  1187 GLN B NE2 
3331 N N   . VAL B 151 ? 0.5073 0.7750 1.1733 -0.0402 -0.0269 0.1075  1188 VAL B N   
3332 C CA  . VAL B 151 ? 0.5142 0.7519 1.1137 -0.0440 -0.0489 0.0876  1188 VAL B CA  
3333 C C   . VAL B 151 ? 0.5357 0.7493 1.1446 -0.0544 -0.0929 0.1001  1188 VAL B C   
3334 O O   . VAL B 151 ? 0.5482 0.7352 1.1200 -0.0552 -0.1064 0.0904  1188 VAL B O   
3335 C CB  . VAL B 151 ? 0.5124 0.7415 1.0602 -0.0460 -0.0480 0.0730  1188 VAL B CB  
3336 C CG1 . VAL B 151 ? 0.5268 0.7230 1.0145 -0.0484 -0.0678 0.0566  1188 VAL B CG1 
3337 C CG2 . VAL B 151 ? 0.5022 0.7457 1.0297 -0.0385 -0.0121 0.0605  1188 VAL B CG2 
3338 N N   . ALA B 152 ? 0.5456 0.7639 1.2005 -0.0638 -0.1167 0.1227  1189 ALA B N   
3339 C CA  . ALA B 152 ? 0.5789 0.7660 1.2391 -0.0774 -0.1664 0.1375  1189 ALA B CA  
3340 C C   . ALA B 152 ? 0.5857 0.7753 1.2906 -0.0767 -0.1777 0.1513  1189 ALA B C   
3341 O O   . ALA B 152 ? 0.6166 0.7654 1.2828 -0.0838 -0.2105 0.1490  1189 ALA B O   
3342 C CB  . ALA B 152 ? 0.5860 0.7813 1.2953 -0.0892 -0.1894 0.1616  1189 ALA B CB  
3343 N N   . LYS B 153 ? 0.5634 0.7964 1.3468 -0.0674 -0.1488 0.1665  1190 LYS B N   
3344 C CA  . LYS B 153 ? 0.5686 0.8092 1.4052 -0.0629 -0.1529 0.1807  1190 LYS B CA  
3345 C C   . LYS B 153 ? 0.5721 0.7894 1.3403 -0.0552 -0.1401 0.1545  1190 LYS B C   
3346 O O   . LYS B 153 ? 0.5917 0.7872 1.3606 -0.0584 -0.1654 0.1602  1190 LYS B O   
3347 C CB  . LYS B 153 ? 0.5481 0.8375 1.4776 -0.0499 -0.1121 0.1998  1190 LYS B CB  
3348 C CG  . LYS B 153 ? 0.5478 0.8655 1.5688 -0.0581 -0.1247 0.2341  1190 LYS B CG  
3349 C CD  . LYS B 153 ? 0.5334 0.8966 1.6478 -0.0425 -0.0757 0.2546  1190 LYS B CD  
3350 C CE  . LYS B 153 ? 0.5354 0.9304 1.7550 -0.0516 -0.0882 0.2939  1190 LYS B CE  
3351 N NZ  . LYS B 153 ? 0.5285 0.9660 1.8414 -0.0335 -0.0318 0.3154  1190 LYS B NZ  
3352 N N   . GLY B 154 ? 0.5563 0.7770 1.2677 -0.0465 -0.1031 0.1281  1191 GLY B N   
3353 C CA  . GLY B 154 ? 0.5594 0.7592 1.2054 -0.0415 -0.0908 0.1036  1191 GLY B CA  
3354 C C   . GLY B 154 ? 0.5884 0.7419 1.1655 -0.0522 -0.1257 0.0942  1191 GLY B C   
3355 O O   . GLY B 154 ? 0.6051 0.7337 1.1538 -0.0527 -0.1341 0.0889  1191 GLY B O   
3356 N N   . MET B 155 ? 0.5981 0.7349 1.1443 -0.0603 -0.1439 0.0925  1192 MET B N   
3357 C CA  . MET B 155 ? 0.6386 0.7218 1.1085 -0.0685 -0.1710 0.0825  1192 MET B CA  
3358 C C   . MET B 155 ? 0.6808 0.7266 1.1588 -0.0812 -0.2192 0.1024  1192 MET B C   
3359 O O   . MET B 155 ? 0.7262 0.7179 1.1347 -0.0870 -0.2390 0.0948  1192 MET B O   
3360 C CB  . MET B 155 ? 0.6468 0.7182 1.0830 -0.0718 -0.1756 0.0762  1192 MET B CB  
3361 C CG  . MET B 155 ? 0.6237 0.7099 1.0228 -0.0615 -0.1382 0.0531  1192 MET B CG  
3362 S SD  . MET B 155 ? 0.6444 0.6997 0.9708 -0.0561 -0.1218 0.0307  1192 MET B SD  
3363 C CE  . MET B 155 ? 0.7158 0.6973 0.9836 -0.0673 -0.1634 0.0367  1192 MET B CE  
3364 N N   . LYS B 156 ? 0.6695 0.7416 1.2326 -0.0862 -0.2382 0.1296  1193 LYS B N   
3365 C CA  . LYS B 156 ? 0.7098 0.7509 1.2969 -0.1002 -0.2904 0.1539  1193 LYS B CA  
3366 C C   . LYS B 156 ? 0.7191 0.7455 1.2972 -0.0965 -0.2916 0.1524  1193 LYS B C   
3367 O O   . LYS B 156 ? 0.7735 0.7436 1.3071 -0.1086 -0.3337 0.1583  1193 LYS B O   
3368 C CB  . LYS B 156 ? 0.6912 0.7766 1.3936 -0.1044 -0.3041 0.1871  1193 LYS B CB  
3369 C CG  . LYS B 156 ? 0.7360 0.7950 1.4824 -0.1209 -0.3646 0.2184  1193 LYS B CG  
3370 C CD  . LYS B 156 ? 0.7149 0.8257 1.5927 -0.1245 -0.3747 0.2555  1193 LYS B CD  
3371 C CE  . LYS B 156 ? 0.7592 0.8465 1.6924 -0.1420 -0.4398 0.2903  1193 LYS B CE  
3372 N NZ  . LYS B 156 ? 0.7356 0.8799 1.8123 -0.1453 -0.4473 0.3305  1193 LYS B NZ  
3373 N N   . TYR B 157 ? 0.6723 0.7429 1.2871 -0.0803 -0.2468 0.1450  1194 TYR B N   
3374 C CA  . TYR B 157 ? 0.6771 0.7370 1.2868 -0.0751 -0.2427 0.1426  1194 TYR B CA  
3375 C C   . TYR B 157 ? 0.7084 0.7142 1.2071 -0.0790 -0.2444 0.1188  1194 TYR B C   
3376 O O   . TYR B 157 ? 0.7495 0.7104 1.2149 -0.0866 -0.2733 0.1240  1194 TYR B O   
3377 C CB  . TYR B 157 ? 0.6303 0.7403 1.2876 -0.0566 -0.1904 0.1358  1194 TYR B CB  
3378 C CG  . TYR B 157 ? 0.6412 0.7398 1.2950 -0.0501 -0.1837 0.1329  1194 TYR B CG  
3379 C CD1 . TYR B 157 ? 0.6609 0.7553 1.3763 -0.0518 -0.2131 0.1585  1194 TYR B CD1 
3380 C CD2 . TYR B 157 ? 0.6365 0.7272 1.2288 -0.0434 -0.1512 0.1067  1194 TYR B CD2 
3381 C CE1 . TYR B 157 ? 0.6734 0.7543 1.3850 -0.0456 -0.2083 0.1565  1194 TYR B CE1 
3382 C CE2 . TYR B 157 ? 0.6486 0.7255 1.2355 -0.0387 -0.1463 0.1044  1194 TYR B CE2 
3383 C CZ  . TYR B 157 ? 0.6676 0.7382 1.3115 -0.0392 -0.1742 0.1286  1194 TYR B CZ  
3384 O OH  . TYR B 157 ? 0.6828 0.7371 1.3209 -0.0341 -0.1703 0.1270  1194 TYR B OH  
3385 N N   . LEU B 158 ? 0.6887 0.6983 1.1334 -0.0737 -0.2124 0.0946  1195 LEU B N   
3386 C CA  . LEU B 158 ? 0.7179 0.6834 1.0673 -0.0749 -0.2038 0.0732  1195 LEU B CA  
3387 C C   . LEU B 158 ? 0.7844 0.6792 1.0648 -0.0890 -0.2461 0.0778  1195 LEU B C   
3388 O O   . LEU B 158 ? 0.8320 0.6724 1.0403 -0.0934 -0.2540 0.0715  1195 LEU B O   
3389 C CB  . LEU B 158 ? 0.6856 0.6778 1.0129 -0.0660 -0.1634 0.0520  1195 LEU B CB  
3390 C CG  . LEU B 158 ? 0.6327 0.6787 1.0040 -0.0543 -0.1232 0.0443  1195 LEU B CG  
3391 C CD1 . LEU B 158 ? 0.6118 0.6749 0.9547 -0.0490 -0.0931 0.0256  1195 LEU B CD1 
3392 C CD2 . LEU B 158 ? 0.6388 0.6769 1.0030 -0.0516 -0.1136 0.0406  1195 LEU B CD2 
3393 N N   . ALA B 159 ? 0.7931 0.6829 1.0906 -0.0967 -0.2730 0.0895  1196 ALA B N   
3394 C CA  . ALA B 159 ? 0.8699 0.6837 1.0955 -0.1114 -0.3167 0.0941  1196 ALA B CA  
3395 C C   . ALA B 159 ? 0.9273 0.6912 1.1407 -0.1247 -0.3637 0.1122  1196 ALA B C   
3396 O O   . ALA B 159 ? 1.0079 0.6889 1.1227 -0.1347 -0.3885 0.1079  1196 ALA B O   
3397 C CB  . ALA B 159 ? 0.8651 0.6894 1.1275 -0.1186 -0.3397 0.1069  1196 ALA B CB  
3398 N N   . SER B 160 ? 0.8910 0.7013 1.2026 -0.1241 -0.3746 0.1334  1197 SER B N   
3399 C CA  . SER B 160 ? 0.9385 0.7097 1.2579 -0.1363 -0.4228 0.1551  1197 SER B CA  
3400 C C   . SER B 160 ? 0.9653 0.6994 1.2131 -0.1325 -0.4068 0.1402  1197 SER B C   
3401 O O   . SER B 160 ? 1.0380 0.7063 1.2379 -0.1457 -0.4494 0.1514  1197 SER B O   
3402 C CB  . SER B 160 ? 0.8889 0.7255 1.3450 -0.1332 -0.4324 0.1833  1197 SER B CB  
3403 O OG  . SER B 160 ? 0.8212 0.7207 1.3279 -0.1130 -0.3768 0.1725  1197 SER B OG  
3404 N N   . LYS B 161 ? 1.2543 0.8465 1.3638 0.1433  -0.2549 0.2287  1198 LYS B N   
3405 C CA  . LYS B 161 ? 1.3134 0.8193 1.3342 0.1471  -0.2382 0.2257  1198 LYS B CA  
3406 C C   . LYS B 161 ? 1.3410 0.7883 1.2888 0.1234  -0.2199 0.2243  1198 LYS B C   
3407 O O   . LYS B 161 ? 1.3893 0.7714 1.2629 0.1178  -0.1988 0.2228  1198 LYS B O   
3408 C CB  . LYS B 161 ? 1.2794 0.8083 1.3192 0.1505  -0.2014 0.2212  1198 LYS B CB  
3409 C CG  . LYS B 161 ? 1.2513 0.8407 1.3600 0.1786  -0.2128 0.2209  1198 LYS B CG  
3410 C CD  . LYS B 161 ? 1.3237 0.8694 1.4009 0.2117  -0.2520 0.2223  1198 LYS B CD  
3411 C CE  . LYS B 161 ? 1.2973 0.9119 1.4448 0.2455  -0.2608 0.2203  1198 LYS B CE  
3412 N NZ  . LYS B 161 ? 1.3748 0.9473 1.4897 0.2836  -0.3024 0.2199  1198 LYS B NZ  
3413 N N   . LYS B 162 ? 1.3165 0.7865 1.2822 0.1096  -0.2282 0.2250  1199 LYS B N   
3414 C CA  . LYS B 162 ? 1.3451 0.7666 1.2443 0.0934  -0.2127 0.2223  1199 LYS B CA  
3415 C C   . LYS B 162 ? 1.3043 0.7453 1.2013 0.0796  -0.1603 0.2160  1199 LYS B C   
3416 O O   . LYS B 162 ? 1.3488 0.7386 1.1742 0.0707  -0.1374 0.2136  1199 LYS B O   
3417 C CB  . LYS B 162 ? 1.4482 0.7688 1.2458 0.0994  -0.2319 0.2249  1199 LYS B CB  
3418 C CG  . LYS B 162 ? 1.4968 0.7919 1.2912 0.1157  -0.2879 0.2306  1199 LYS B CG  
3419 C CD  . LYS B 162 ? 1.4699 0.8074 1.3144 0.1092  -0.3196 0.2332  1199 LYS B CD  
3420 C CE  . LYS B 162 ? 1.4946 0.7922 1.2834 0.0945  -0.3127 0.2306  1199 LYS B CE  
3421 N NZ  . LYS B 162 ? 1.5965 0.7885 1.2725 0.1000  -0.3231 0.2308  1199 LYS B NZ  
3422 N N   . PHE B 163 ? 1.2206 0.7392 1.1971 0.0770  -0.1420 0.2135  1200 PHE B N   
3423 C CA  . PHE B 163 ? 1.1766 0.7232 1.1625 0.0644  -0.0969 0.2070  1200 PHE B CA  
3424 C C   . PHE B 163 ? 1.1305 0.7141 1.1380 0.0539  -0.0852 0.2018  1200 PHE B C   
3425 O O   . PHE B 163 ? 1.0975 0.7181 1.1532 0.0546  -0.1063 0.2040  1200 PHE B O   
3426 C CB  . PHE B 163 ? 1.1277 0.7265 1.1771 0.0708  -0.0851 0.2065  1200 PHE B CB  
3427 C CG  . PHE B 163 ? 1.0938 0.7179 1.1520 0.0574  -0.0428 0.2000  1200 PHE B CG  
3428 C CD1 . PHE B 163 ? 1.1400 0.7164 1.1376 0.0468  -0.0202 0.1988  1200 PHE B CD1 
3429 C CD2 . PHE B 163 ? 1.0212 0.7148 1.1453 0.0527  -0.0270 0.1957  1200 PHE B CD2 
3430 C CE1 . PHE B 163 ? 1.1090 0.7136 1.1183 0.0312  0.0156  0.1932  1200 PHE B CE1 
3431 C CE2 . PHE B 163 ? 0.9908 0.7074 1.1228 0.0411  0.0081  0.1891  1200 PHE B CE2 
3432 C CZ  . PHE B 163 ? 1.0333 0.7086 1.1111 0.0300  0.0287  0.1878  1200 PHE B CZ  
3433 N N   . VAL B 164 ? 1.1323 0.7058 1.1016 0.0439  -0.0522 0.1951  1201 VAL B N   
3434 C CA  . VAL B 164 ? 1.0967 0.7005 1.0771 0.0397  -0.0393 0.1877  1201 VAL B CA  
3435 C C   . VAL B 164 ? 1.0349 0.6946 1.0565 0.0319  -0.0013 0.1806  1201 VAL B C   
3436 O O   . VAL B 164 ? 1.0523 0.7037 1.0445 0.0235  0.0276  0.1774  1201 VAL B O   
3437 C CB  . VAL B 164 ? 1.1599 0.7106 1.0599 0.0407  -0.0351 0.1840  1201 VAL B CB  
3438 C CG1 . VAL B 164 ? 1.1419 0.7139 1.0453 0.0443  -0.0317 0.1757  1201 VAL B CG1 
3439 C CG2 . VAL B 164 ? 1.2324 0.7131 1.0772 0.0478  -0.0721 0.1916  1201 VAL B CG2 
3440 N N   . HIS B 165 ? 0.9675 0.6826 1.0548 0.0325  -0.0030 0.1786  1202 HIS B N   
3441 C CA  . HIS B 165 ? 0.9091 0.6762 1.0403 0.0270  0.0268  0.1724  1202 HIS B CA  
3442 C C   . HIS B 165 ? 0.9059 0.6869 1.0162 0.0237  0.0528  0.1612  1202 HIS B C   
3443 O O   . HIS B 165 ? 0.9000 0.6975 1.0070 0.0154  0.0823  0.1563  1202 HIS B O   
3444 C CB  . HIS B 165 ? 0.8509 0.6673 1.0515 0.0292  0.0155  0.1746  1202 HIS B CB  
3445 C CG  . HIS B 165 ? 0.7981 0.6598 1.0430 0.0262  0.0409  0.1701  1202 HIS B CG  
3446 N ND1 . HIS B 165 ? 0.7758 0.6587 1.0192 0.0204  0.0689  0.1600  1202 HIS B ND1 
3447 C CD2 . HIS B 165 ? 0.7680 0.6573 1.0587 0.0304  0.0404  0.1742  1202 HIS B CD2 
3448 C CE1 . HIS B 165 ? 0.7361 0.6523 1.0199 0.0187  0.0830  0.1584  1202 HIS B CE1 
3449 N NE2 . HIS B 165 ? 0.7320 0.6506 1.0429 0.0259  0.0670  0.1671  1202 HIS B NE2 
3450 N N   . ARG B 166 ? 0.9157 0.6908 1.0119 0.0309  0.0395  0.1572  1203 ARG B N   
3451 C CA  . ARG B 166 ? 0.9245 0.7081 0.9925 0.0366  0.0587  0.1452  1203 ARG B CA  
3452 C C   . ARG B 166 ? 0.8628 0.7055 0.9807 0.0363  0.0782  0.1359  1203 ARG B C   
3453 O O   . ARG B 166 ? 0.8651 0.7281 0.9690 0.0434  0.0969  0.1240  1203 ARG B O   
3454 C CB  . ARG B 166 ? 0.9705 0.7363 0.9874 0.0325  0.0845  0.1426  1203 ARG B CB  
3455 C CG  . ARG B 166 ? 1.0402 0.7390 0.9979 0.0323  0.0671  0.1519  1203 ARG B CG  
3456 C CD  . ARG B 166 ? 1.0867 0.7680 0.9961 0.0213  0.0959  0.1523  1203 ARG B CD  
3457 N NE  . ARG B 166 ? 1.1105 0.8082 0.9860 0.0269  0.1218  0.1418  1203 ARG B NE  
3458 C CZ  . ARG B 166 ? 1.1843 0.8377 0.9865 0.0315  0.1271  0.1420  1203 ARG B CZ  
3459 N NH1 . ARG B 166 ? 1.2419 0.8227 0.9939 0.0335  0.1004  0.1516  1203 ARG B NH1 
3460 N NH2 . ARG B 166 ? 1.2041 0.8879 0.9826 0.0361  0.1588  0.1320  1203 ARG B NH2 
3461 N N   . ASP B 167 ? 0.8112 0.6825 0.9852 0.0306  0.0732  0.1405  1204 ASP B N   
3462 C CA  . ASP B 167 ? 0.7570 0.6775 0.9744 0.0301  0.0896  0.1324  1204 ASP B CA  
3463 C C   . ASP B 167 ? 0.7150 0.6546 0.9843 0.0260  0.0772  0.1403  1204 ASP B C   
3464 O O   . ASP B 167 ? 0.6819 0.6499 0.9854 0.0216  0.0928  0.1398  1204 ASP B O   
3465 C CB  . ASP B 167 ? 0.7455 0.6936 0.9679 0.0220  0.1219  0.1261  1204 ASP B CB  
3466 C CG  . ASP B 167 ? 0.7015 0.6992 0.9606 0.0234  0.1378  0.1150  1204 ASP B CG  
3467 O OD1 . ASP B 167 ? 0.6840 0.6897 0.9570 0.0330  0.1253  0.1111  1204 ASP B OD1 
3468 O OD2 . ASP B 167 ? 0.6899 0.7140 0.9594 0.0131  0.1607  0.1108  1204 ASP B OD2 
3469 N N   . LEU B 168 ? 0.7198 0.6443 0.9926 0.0266  0.0489  0.1478  1205 LEU B N   
3470 C CA  . LEU B 168 ? 0.6844 0.6357 1.0083 0.0213  0.0381  0.1564  1205 LEU B CA  
3471 C C   . LEU B 168 ? 0.6522 0.6278 0.9954 0.0200  0.0431  0.1502  1205 LEU B C   
3472 O O   . LEU B 168 ? 0.6729 0.6275 0.9858 0.0227  0.0317  0.1451  1205 LEU B O   
3473 C CB  . LEU B 168 ? 0.7127 0.6430 1.0339 0.0176  0.0044  0.1685  1205 LEU B CB  
3474 C CG  . LEU B 168 ? 0.6850 0.6541 1.0643 0.0108  -0.0067 0.1794  1205 LEU B CG  
3475 C CD1 . LEU B 168 ? 0.6661 0.6585 1.0759 0.0185  0.0074  0.1821  1205 LEU B CD1 
3476 C CD2 . LEU B 168 ? 0.7164 0.6708 1.0941 0.0028  -0.0433 0.1907  1205 LEU B CD2 
3477 N N   . ALA B 169 ? 0.6072 0.6198 0.9933 0.0178  0.0590  0.1501  1206 ALA B N   
3478 C CA  . ALA B 169 ? 0.5804 0.6126 0.9824 0.0165  0.0646  0.1446  1206 ALA B CA  
3479 C C   . ALA B 169 ? 0.5432 0.6110 0.9928 0.0134  0.0768  0.1496  1206 ALA B C   
3480 O O   . ALA B 169 ? 0.5385 0.6151 1.0056 0.0159  0.0821  0.1552  1206 ALA B O   
3481 C CB  . ALA B 169 ? 0.5789 0.6124 0.9579 0.0252  0.0817  0.1287  1206 ALA B CB  
3482 N N   . ALA B 170 ? 0.5247 0.6072 0.9878 0.0104  0.0804  0.1472  1207 ALA B N   
3483 C CA  . ALA B 170 ? 0.4969 0.6109 0.9985 0.0092  0.0940  0.1511  1207 ALA B CA  
3484 C C   . ALA B 170 ? 0.4816 0.6031 0.9861 0.0175  0.1167  0.1423  1207 ALA B C   
3485 O O   . ALA B 170 ? 0.4726 0.6084 0.9995 0.0215  0.1260  0.1470  1207 ALA B O   
3486 C CB  . ALA B 170 ? 0.4946 0.6116 0.9966 0.0028  0.0924  0.1499  1207 ALA B CB  
3487 N N   . ARG B 171 ? 0.4838 0.5959 0.9635 0.0203  0.1244  0.1295  1208 ARG B N   
3488 C CA  . ARG B 171 ? 0.4729 0.5924 0.9525 0.0218  0.1435  0.1212  1208 ARG B CA  
3489 C C   . ARG B 171 ? 0.4860 0.5932 0.9618 0.0206  0.1466  0.1280  1208 ARG B C   
3490 O O   . ARG B 171 ? 0.4852 0.5924 0.9647 0.0203  0.1588  0.1265  1208 ARG B O   
3491 C CB  . ARG B 171 ? 0.4779 0.5997 0.9351 0.0235  0.1491  0.1073  1208 ARG B CB  
3492 C CG  . ARG B 171 ? 0.5043 0.6091 0.9320 0.0245  0.1423  0.1074  1208 ARG B CG  
3493 C CD  . ARG B 171 ? 0.5122 0.6301 0.9206 0.0305  0.1505  0.0927  1208 ARG B CD  
3494 N NE  . ARG B 171 ? 0.5440 0.6434 0.9185 0.0336  0.1465  0.0932  1208 ARG B NE  
3495 C CZ  . ARG B 171 ? 0.5669 0.6509 0.9123 0.0466  0.1340  0.0877  1208 ARG B CZ  
3496 N NH1 . ARG B 171 ? 0.5626 0.6474 0.9069 0.0573  0.1244  0.0802  1208 ARG B NH1 
3497 N NH2 . ARG B 171 ? 0.6018 0.6617 0.9112 0.0499  0.1299  0.0896  1208 ARG B NH2 
3498 N N   . ASN B 172 ? 0.5074 0.5964 0.9687 0.0204  0.1329  0.1352  1209 ASN B N   
3499 C CA  . ASN B 172 ? 0.5325 0.5998 0.9801 0.0211  0.1316  0.1416  1209 ASN B CA  
3500 C C   . ASN B 172 ? 0.5324 0.6058 1.0054 0.0293  0.1184  0.1532  1209 ASN B C   
3501 O O   . ASN B 172 ? 0.5562 0.6090 1.0164 0.0335  0.1058  0.1600  1209 ASN B O   
3502 C CB  . ASN B 172 ? 0.5651 0.6049 0.9740 0.0175  0.1251  0.1414  1209 ASN B CB  
3503 C CG  . ASN B 172 ? 0.5689 0.6140 0.9560 0.0112  0.1419  0.1299  1209 ASN B CG  
3504 O OD1 . ASN B 172 ? 0.5482 0.6163 0.9500 0.0077  0.1569  0.1221  1209 ASN B OD1 
3505 N ND2 . ASN B 172 ? 0.5998 0.6266 0.9518 0.0104  0.1394  0.1285  1209 ASN B ND2 
3506 N N   . CYS B 173 ? 0.5083 0.6124 1.0165 0.0325  0.1216  0.1551  1210 CYS B N   
3507 C CA  . CYS B 173 ? 0.5080 0.6343 1.0489 0.0420  0.1146  0.1651  1210 CYS B CA  
3508 C C   . CYS B 173 ? 0.4946 0.6385 1.0530 0.0511  0.1332  0.1622  1210 CYS B C   
3509 O O   . CYS B 173 ? 0.4741 0.6285 1.0369 0.0454  0.1445  0.1565  1210 CYS B O   
3510 C CB  . CYS B 173 ? 0.5000 0.6520 1.0667 0.0338  0.0987  0.1735  1210 CYS B CB  
3511 S SG  . CYS B 173 ? 0.5309 0.6525 1.0693 0.0251  0.0714  0.1776  1210 CYS B SG  
3512 N N   . MET B 174 ? 0.5134 0.6548 1.0756 0.0680  0.1345  0.1654  1211 MET B N   
3513 C CA  . MET B 174 ? 0.5192 0.6585 1.0794 0.0802  0.1515  0.1606  1211 MET B CA  
3514 C C   . MET B 174 ? 0.5186 0.6970 1.1153 0.1005  0.1530  0.1676  1211 MET B C   
3515 O O   . MET B 174 ? 0.5272 0.7222 1.1417 0.1111  0.1386  0.1751  1211 MET B O   
3516 C CB  . MET B 174 ? 0.5586 0.6471 1.0749 0.0854  0.1528  0.1563  1211 MET B CB  
3517 C CG  . MET B 174 ? 0.5660 0.6253 1.0486 0.0634  0.1557  0.1499  1211 MET B CG  
3518 S SD  . MET B 174 ? 0.5400 0.6139 1.0264 0.0492  0.1727  0.1387  1211 MET B SD  
3519 C CE  . MET B 174 ? 0.5644 0.6080 1.0103 0.0278  0.1767  0.1324  1211 MET B CE  
3520 N N   . LEU B 175 ? 0.5121 0.7070 1.1188 0.1070  0.1705  0.1645  1212 LEU B N   
3521 C CA  . LEU B 175 ? 0.5158 0.7528 1.1547 0.1286  0.1784  0.1699  1212 LEU B CA  
3522 C C   . LEU B 175 ? 0.5532 0.7567 1.1616 0.1565  0.1865  0.1637  1212 LEU B C   
3523 O O   . LEU B 175 ? 0.5660 0.7276 1.1380 0.1522  0.1956  0.1551  1212 LEU B O   
3524 C CB  . LEU B 175 ? 0.4922 0.7635 1.1531 0.1175  0.1936  0.1712  1212 LEU B CB  
3525 C CG  . LEU B 175 ? 0.4707 0.7725 1.1574 0.0909  0.1839  0.1791  1212 LEU B CG  
3526 C CD1 . LEU B 175 ? 0.4729 0.8143 1.1959 0.0920  0.1667  0.1906  1212 LEU B CD1 
3527 C CD2 . LEU B 175 ? 0.4658 0.7266 1.1210 0.0700  0.1743  0.1723  1212 LEU B CD2 
3528 N N   . ASP B 176 ? 0.5774 0.7988 1.1990 0.1861  0.1810  0.1677  1213 ASP B N   
3529 C CA  . ASP B 176 ? 0.6229 0.8102 1.2107 0.2197  0.1869  0.1617  1213 ASP B CA  
3530 C C   . ASP B 176 ? 0.6180 0.8458 1.2271 0.2368  0.2092  0.1610  1213 ASP B C   
3531 O O   . ASP B 176 ? 0.5797 0.8460 1.2178 0.2154  0.2207  0.1642  1213 ASP B O   
3532 C CB  . ASP B 176 ? 0.6585 0.8384 1.2412 0.2491  0.1683  0.1642  1213 ASP B CB  
3533 C CG  . ASP B 176 ? 0.6409 0.9055 1.2879 0.2690  0.1647  0.1724  1213 ASP B CG  
3534 O OD1 . ASP B 176 ? 0.6007 0.9315 1.2972 0.2545  0.1778  0.1780  1213 ASP B OD1 
3535 O OD2 . ASP B 176 ? 0.6709 0.9350 1.3167 0.2981  0.1475  0.1733  1213 ASP B OD2 
3536 N N   . GLU B 177 ? 0.6645 0.8773 1.2515 0.2767  0.2150  0.1565  1214 GLU B N   
3537 C CA  . GLU B 177 ? 0.6719 0.9160 1.2683 0.2981  0.2385  0.1548  1214 GLU B CA  
3538 C C   . GLU B 177 ? 0.6399 0.9867 1.3098 0.3032  0.2473  0.1654  1214 GLU B C   
3539 O O   . GLU B 177 ? 0.6277 1.0156 1.3171 0.3026  0.2699  0.1676  1214 GLU B O   
3540 C CB  . GLU B 177 ? 0.7404 0.9323 1.2836 0.3437  0.2405  0.1461  1214 GLU B CB  
3541 C CG  . GLU B 177 ? 0.7743 0.9929 1.3313 0.3880  0.2294  0.1477  1214 GLU B CG  
3542 C CD  . GLU B 177 ? 0.7941 0.9712 1.3315 0.3846  0.2003  0.1487  1214 GLU B CD  
3543 O OE1 . GLU B 177 ? 0.8217 1.0219 1.3719 0.4217  0.1874  0.1497  1214 GLU B OE1 
3544 O OE2 . GLU B 177 ? 0.7854 0.9082 1.2931 0.3466  0.1906  0.1483  1214 GLU B OE2 
3545 N N   . LYS B 178 ? 0.6314 1.0186 1.3396 0.3057  0.2287  0.1724  1215 LYS B N   
3546 C CA  . LYS B 178 ? 0.6052 1.0961 1.3881 0.3054  0.2326  0.1837  1215 LYS B CA  
3547 C C   . LYS B 178 ? 0.5596 1.0761 1.3750 0.2535  0.2240  0.1933  1215 LYS B C   
3548 O O   . LYS B 178 ? 0.5412 1.1327 1.4148 0.2427  0.2167  0.2044  1215 LYS B O   
3549 C CB  . LYS B 178 ? 0.6287 1.1515 1.4353 0.3409  0.2130  0.1852  1215 LYS B CB  
3550 C CG  . LYS B 178 ? 0.6870 1.1804 1.4554 0.3994  0.2172  0.1749  1215 LYS B CG  
3551 C CD  . LYS B 178 ? 0.7176 1.2361 1.5036 0.4383  0.1933  0.1748  1215 LYS B CD  
3552 C CE  . LYS B 178 ? 0.6895 1.3401 1.5683 0.4462  0.1963  0.1849  1215 LYS B CE  
3553 N NZ  . LYS B 178 ? 0.7249 1.4010 1.6198 0.4910  0.1705  0.1827  1215 LYS B NZ  
3554 N N   . PHE B 179 ? 0.5467 1.0010 1.3225 0.2225  0.2236  0.1888  1216 PHE B N   
3555 C CA  . PHE B 179 ? 0.5125 0.9747 1.3034 0.1779  0.2148  0.1953  1216 PHE B CA  
3556 C C   . PHE B 179 ? 0.5056 0.9838 1.3204 0.1676  0.1865  0.2025  1216 PHE B C   
3557 O O   . PHE B 179 ? 0.4872 1.0109 1.3396 0.1405  0.1779  0.2131  1216 PHE B O   
3558 C CB  . PHE B 179 ? 0.4956 1.0183 1.3223 0.1593  0.2330  0.2042  1216 PHE B CB  
3559 C CG  . PHE B 179 ? 0.5078 1.0139 1.3077 0.1698  0.2607  0.1979  1216 PHE B CG  
3560 C CD1 . PHE B 179 ? 0.5004 0.9636 1.2675 0.1438  0.2658  0.1937  1216 PHE B CD1 
3561 C CD2 . PHE B 179 ? 0.5325 1.0649 1.3367 0.2087  0.2802  0.1954  1216 PHE B CD2 
3562 C CE1 . PHE B 179 ? 0.5165 0.9598 1.2550 0.1537  0.2884  0.1877  1216 PHE B CE1 
3563 C CE2 . PHE B 179 ? 0.5505 1.0608 1.3228 0.2191  0.3047  0.1895  1216 PHE B CE2 
3564 C CZ  . PHE B 179 ? 0.5422 1.0070 1.2818 0.1901  0.3081  0.1860  1216 PHE B CZ  
3565 N N   . THR B 180 ? 0.5283 0.9610 1.3139 0.1872  0.1703  0.1969  1217 THR B N   
3566 C CA  . THR B 180 ? 0.5331 0.9684 1.3304 0.1818  0.1415  0.2024  1217 THR B CA  
3567 C C   . THR B 180 ? 0.5335 0.8979 1.2835 0.1552  0.1296  0.1982  1217 THR B C   
3568 O O   . THR B 180 ? 0.5529 0.8533 1.2519 0.1614  0.1343  0.1889  1217 THR B O   
3569 C CB  . THR B 180 ? 0.5707 1.0008 1.3622 0.2237  0.1295  0.1996  1217 THR B CB  
3570 O OG1 . THR B 180 ? 0.5729 1.0716 1.4051 0.2544  0.1453  0.2011  1217 THR B OG1 
3571 C CG2 . THR B 180 ? 0.5807 1.0194 1.3876 0.2212  0.0973  0.2059  1217 THR B CG2 
3572 N N   . VAL B 181 ? 0.5188 0.8959 1.2841 0.1252  0.1139  0.2052  1218 VAL B N   
3573 C CA  . VAL B 181 ? 0.5219 0.8401 1.2440 0.1026  0.1038  0.2009  1218 VAL B CA  
3574 C C   . VAL B 181 ? 0.5563 0.8297 1.2465 0.1153  0.0842  0.1993  1218 VAL B C   
3575 O O   . VAL B 181 ? 0.5680 0.8647 1.2810 0.1236  0.0628  0.2063  1218 VAL B O   
3576 C CB  . VAL B 181 ? 0.5070 0.8434 1.2452 0.0705  0.0906  0.2085  1218 VAL B CB  
3577 C CG1 . VAL B 181 ? 0.5166 0.7924 1.2062 0.0544  0.0790  0.2030  1218 VAL B CG1 
3578 C CG2 . VAL B 181 ? 0.4857 0.8545 1.2439 0.0551  0.1088  0.2107  1218 VAL B CG2 
3579 N N   . LYS B 182 ? 0.5766 0.7865 1.2128 0.1148  0.0911  0.1904  1219 LYS B N   
3580 C CA  . LYS B 182 ? 0.6188 0.7737 1.2109 0.1215  0.0755  0.1891  1219 LYS B CA  
3581 C C   . LYS B 182 ? 0.6219 0.7337 1.1734 0.0961  0.0758  0.1850  1219 LYS B C   
3582 O O   . LYS B 182 ? 0.6023 0.7067 1.1417 0.0836  0.0945  0.1780  1219 LYS B O   
3583 C CB  . LYS B 182 ? 0.6548 0.7698 1.2118 0.1449  0.0842  0.1832  1219 LYS B CB  
3584 C CG  . LYS B 182 ? 0.6651 0.8173 1.2530 0.1794  0.0840  0.1850  1219 LYS B CG  
3585 C CD  . LYS B 182 ? 0.7147 0.8108 1.2527 0.2050  0.0890  0.1781  1219 LYS B CD  
3586 C CE  . LYS B 182 ? 0.7294 0.8634 1.2942 0.2461  0.0909  0.1778  1219 LYS B CE  
3587 N NZ  . LYS B 182 ? 0.7410 0.9146 1.3399 0.2678  0.0666  0.1839  1219 LYS B NZ  
3588 N N   . VAL B 183 ? 0.6508 0.7362 1.1807 0.0911  0.0544  0.1888  1220 VAL B N   
3589 C CA  . VAL B 183 ? 0.6648 0.7117 1.1531 0.0716  0.0544  0.1851  1220 VAL B CA  
3590 C C   . VAL B 183 ? 0.7004 0.6954 1.1360 0.0708  0.0685  0.1788  1220 VAL B C   
3591 O O   . VAL B 183 ? 0.7453 0.7022 1.1506 0.0827  0.0590  0.1811  1220 VAL B O   
3592 C CB  . VAL B 183 ? 0.6904 0.7204 1.1658 0.0679  0.0259  0.1916  1220 VAL B CB  
3593 C CG1 . VAL B 183 ? 0.7100 0.6957 1.1334 0.0531  0.0279  0.1868  1220 VAL B CG1 
3594 C CG2 . VAL B 183 ? 0.6669 0.7471 1.1927 0.0616  0.0091  0.1993  1220 VAL B CG2 
3595 N N   . ALA B 184 ? 0.6881 0.6818 1.1116 0.0556  0.0894  0.1709  1221 ALA B N   
3596 C CA  . ALA B 184 ? 0.7205 0.6746 1.0989 0.0466  0.1045  0.1656  1221 ALA B CA  
3597 C C   . ALA B 184 ? 0.7400 0.6751 1.0830 0.0295  0.1078  0.1627  1221 ALA B C   
3598 O O   . ALA B 184 ? 0.7161 0.6735 1.0726 0.0260  0.1043  0.1608  1221 ALA B O   
3599 C CB  . ALA B 184 ? 0.6942 0.6682 1.0884 0.0427  0.1252  0.1586  1221 ALA B CB  
3600 N N   . ASP B 185 ? 0.7913 0.6822 1.0839 0.0193  0.1148  0.1626  1222 ASP B N   
3601 C CA  . ASP B 185 ? 0.8197 0.6946 1.0737 0.0034  0.1228  0.1601  1222 ASP B CA  
3602 C C   . ASP B 185 ? 0.8325 0.7093 1.0696 -0.0173 0.1479  0.1543  1222 ASP B C   
3603 O O   . ASP B 185 ? 0.8582 0.7080 1.0784 -0.0224 0.1514  0.1563  1222 ASP B O   
3604 C CB  . ASP B 185 ? 0.8801 0.6982 1.0822 0.0056  0.1068  0.1677  1222 ASP B CB  
3605 C CG  . ASP B 185 ? 0.9098 0.7105 1.0679 -0.0073 0.1148  0.1660  1222 ASP B CG  
3606 O OD1 . ASP B 185 ? 0.8795 0.7198 1.0547 -0.0123 0.1287  0.1583  1222 ASP B OD1 
3607 O OD2 . ASP B 185 ? 0.9691 0.7147 1.0718 -0.0102 0.1072  0.1719  1222 ASP B OD2 
3608 N N   . PHE B 186 ? 0.8241 0.7328 1.0639 -0.0285 0.1634  0.1468  1223 PHE B N   
3609 C CA  . PHE B 186 ? 0.8345 0.7610 1.0673 -0.0508 0.1868  0.1408  1223 PHE B CA  
3610 C C   . PHE B 186 ? 0.8935 0.8026 1.0775 -0.0687 0.1993  0.1423  1223 PHE B C   
3611 O O   . PHE B 186 ? 0.8975 0.8360 1.0795 -0.0896 0.2207  0.1372  1223 PHE B O   
3612 C CB  . PHE B 186 ? 0.7765 0.7652 1.0559 -0.0473 0.1964  0.1293  1223 PHE B CB  
3613 C CG  . PHE B 186 ? 0.7396 0.7440 1.0562 -0.0412 0.1943  0.1270  1223 PHE B CG  
3614 C CD1 . PHE B 186 ? 0.7547 0.7468 1.0633 -0.0564 0.2028  0.1269  1223 PHE B CD1 
3615 C CD2 . PHE B 186 ? 0.6986 0.7251 1.0520 -0.0220 0.1836  0.1255  1223 PHE B CD2 
3616 C CE1 . PHE B 186 ? 0.7299 0.7307 1.0654 -0.0482 0.2009  0.1241  1223 PHE B CE1 
3617 C CE2 . PHE B 186 ? 0.6725 0.7120 1.0549 -0.0161 0.1844  0.1236  1223 PHE B CE2 
3618 C CZ  . PHE B 186 ? 0.6880 0.7141 1.0607 -0.0270 0.1931  0.1224  1223 PHE B CZ  
3619 N N   . GLY B 187 ? 0.9496 0.8131 1.0942 -0.0613 0.1860  0.1495  1224 GLY B N   
3620 C CA  . GLY B 187 ? 1.0203 0.8562 1.1079 -0.0775 0.1978  0.1526  1224 GLY B CA  
3621 C C   . GLY B 187 ? 1.0191 0.9037 1.1133 -0.0749 0.2138  0.1433  1224 GLY B C   
3622 O O   . GLY B 187 ? 1.0410 0.9490 1.1182 -0.0952 0.2390  0.1405  1224 GLY B O   
3623 N N   . LEU B 188 ? 1.0077 0.9071 1.1242 -0.0495 0.1982  0.1387  1225 LEU B N   
3624 C CA  . LEU B 188 ? 1.0189 0.9500 1.1298 -0.0383 0.2073  0.1290  1225 LEU B CA  
3625 C C   . LEU B 188 ? 1.0994 0.9827 1.1432 -0.0383 0.2077  0.1340  1225 LEU B C   
3626 O O   . LEU B 188 ? 1.1250 1.0311 1.1443 -0.0403 0.2297  0.1278  1225 LEU B O   
3627 C CB  . LEU B 188 ? 0.9791 0.9238 1.1236 -0.0136 0.1855  0.1239  1225 LEU B CB  
3628 C CG  . LEU B 188 ? 0.9686 0.9528 1.1172 0.0029  0.1930  0.1101  1225 LEU B CG  
3629 C CD1 . LEU B 188 ? 1.0261 0.9843 1.1154 0.0122  0.1967  0.1082  1225 LEU B CD1 
3630 C CD2 . LEU B 188 ? 0.9381 0.9885 1.1216 -0.0055 0.2190  0.0993  1225 LEU B CD2 
3631 N N   . ALA B 189 ? 1.1473 0.9661 1.1609 -0.0343 0.1830  0.1450  1226 ALA B N   
3632 C CA  . ALA B 189 ? 1.2295 0.9884 1.1718 -0.0342 0.1783  0.1512  1226 ALA B CA  
3633 C C   . ALA B 189 ? 1.2868 1.0447 1.1859 -0.0601 0.2114  0.1528  1226 ALA B C   
3634 O O   . ALA B 189 ? 1.3351 1.0849 1.1866 -0.0587 0.2255  0.1508  1226 ALA B O   
3635 C CB  . ALA B 189 ? 1.2572 0.9520 1.1806 -0.0293 0.1466  0.1627  1226 ALA B CB  
3636 N N   . ARG B 190 ? 1.2910 1.0556 1.2035 -0.0849 0.2236  0.1570  1227 ARG B N   
3637 C CA  . ARG B 190 ? 1.3485 1.1115 1.2215 -0.1186 0.2538  0.1609  1227 ARG B CA  
3638 C C   . ARG B 190 ? 1.3378 1.1814 1.2308 -0.1226 0.2864  0.1499  1227 ARG B C   
3639 O O   . ARG B 190 ? 1.3887 1.2285 1.2322 -0.1316 0.3076  0.1511  1227 ARG B O   
3640 C CB  . ARG B 190 ? 1.3424 1.1014 1.2325 -0.1442 0.2567  0.1657  1227 ARG B CB  
3641 C CG  . ARG B 190 ? 1.3798 1.0543 1.2364 -0.1398 0.2280  0.1764  1227 ARG B CG  
3642 C CD  . ARG B 190 ? 1.3682 1.0401 1.2452 -0.1560 0.2276  0.1782  1227 ARG B CD  
3643 N NE  . ARG B 190 ? 1.3970 1.0896 1.2577 -0.1980 0.2570  0.1795  1227 ARG B NE  
3644 C CZ  . ARG B 190 ? 1.3457 1.1145 1.2625 -0.2117 0.2748  0.1714  1227 ARG B CZ  
3645 N NH1 . ARG B 190 ? 1.3784 1.1686 1.2792 -0.2539 0.2999  0.1739  1227 ARG B NH1 
3646 N NH2 . ARG B 190 ? 1.2647 1.0881 1.2519 -0.1851 0.2666  0.1612  1227 ARG B NH2 
3647 N N   . ASN B 191 ? 1.2770 1.1937 1.2409 -0.1134 0.2899  0.1386  1228 ASN B N   
3648 C CA  . ASN B 191 ? 1.2626 1.2671 1.2570 -0.1151 0.3188  0.1262  1228 ASN B CA  
3649 C C   . ASN B 191 ? 1.3003 1.3103 1.2594 -0.0889 0.3259  0.1192  1228 ASN B C   
3650 O O   . ASN B 191 ? 1.3230 1.3866 1.2732 -0.0960 0.3571  0.1135  1228 ASN B O   
3651 C CB  . ASN B 191 ? 1.1838 1.2511 1.2537 -0.1007 0.3122  0.1144  1228 ASN B CB  
3652 C CG  . ASN B 191 ? 1.1584 1.2255 1.2604 -0.1254 0.3085  0.1193  1228 ASN B CG  
3653 O OD1 . ASN B 191 ? 1.2024 1.2179 1.2686 -0.1524 0.3088  0.1316  1228 ASN B OD1 
3654 N ND2 . ASN B 191 ? 1.0971 1.2135 1.2586 -0.1148 0.3035  0.1096  1228 ASN B ND2 
3655 N N   . MET B 192 ? 1.3136 1.2698 1.2519 -0.0585 0.2963  0.1196  1229 MET B N   
3656 C CA  . MET B 192 ? 1.3563 1.3015 1.2518 -0.0295 0.2961  0.1125  1229 MET B CA  
3657 C C   . MET B 192 ? 1.4495 1.3544 1.2684 -0.0446 0.3157  0.1207  1229 MET B C   
3658 O O   . MET B 192 ? 1.4830 1.4220 1.2752 -0.0346 0.3415  0.1128  1229 MET B O   
3659 C CB  . MET B 192 ? 1.3493 1.2341 1.2339 -0.0015 0.2548  0.1140  1229 MET B CB  
3660 C CG  . MET B 192 ? 1.2888 1.2143 1.2250 0.0233  0.2404  0.1017  1229 MET B CG  
3661 S SD  . MET B 192 ? 1.3014 1.1551 1.2154 0.0488  0.1922  0.1051  1229 MET B SD  
3662 C CE  . MET B 192 ? 1.3732 1.1998 1.2087 0.0781  0.1971  0.0953  1229 MET B CE  
3663 N N   . TYR B 193 ? 1.5002 1.3309 1.2800 -0.0664 0.3034  0.1361  1230 TYR B N   
3664 C CA  . TYR B 193 ? 1.5997 1.3730 1.2950 -0.0816 0.3170  0.1457  1230 TYR B CA  
3665 C C   . TYR B 193 ? 1.6321 1.4558 1.3223 -0.1211 0.3610  0.1486  1230 TYR B C   
3666 O O   . TYR B 193 ? 1.7047 1.5088 1.3288 -0.1334 0.3848  0.1534  1230 TYR B O   
3667 C CB  . TYR B 193 ? 1.6413 1.3129 1.2925 -0.0884 0.2844  0.1603  1230 TYR B CB  
3668 C CG  . TYR B 193 ? 1.6439 1.2597 1.2806 -0.0540 0.2426  0.1598  1230 TYR B CG  
3669 C CD1 . TYR B 193 ? 1.6918 1.2802 1.2744 -0.0301 0.2394  0.1550  1230 TYR B CD1 
3670 C CD2 . TYR B 193 ? 1.6034 1.1943 1.2782 -0.0460 0.2056  0.1642  1230 TYR B CD2 
3671 C CE1 . TYR B 193 ? 1.7006 1.2341 1.2665 -0.0031 0.1975  0.1553  1230 TYR B CE1 
3672 C CE2 . TYR B 193 ? 1.6078 1.1555 1.2741 -0.0199 0.1662  0.1650  1230 TYR B CE2 
3673 C CZ  . TYR B 193 ? 1.6571 1.1734 1.2681 -0.0004 0.1605  0.1609  1230 TYR B CZ  
3674 O OH  . TYR B 193 ? 1.6667 1.1364 1.2661 0.0210  0.1180  0.1623  1230 TYR B OH  
3675 N N   . ASP B 194 ? 1.5857 1.4731 1.3429 -0.1430 0.3712  0.1465  1231 ASP B N   
3676 C CA  . ASP B 194 ? 1.6118 1.5576 1.3741 -0.1855 0.4103  0.1493  1231 ASP B CA  
3677 C C   . ASP B 194 ? 1.6030 1.6508 1.3907 -0.1702 0.4434  0.1348  1231 ASP B C   
3678 O O   . ASP B 194 ? 1.6638 1.7271 1.4049 -0.1850 0.4759  0.1378  1231 ASP B O   
3679 C CB  . ASP B 194 ? 1.5625 1.5388 1.3847 -0.2132 0.4061  0.1511  1231 ASP B CB  
3680 C CG  . ASP B 194 ? 1.5933 1.4707 1.3801 -0.2313 0.3795  0.1656  1231 ASP B CG  
3681 O OD1 . ASP B 194 ? 1.6774 1.4819 1.3860 -0.2555 0.3841  0.1788  1231 ASP B OD1 
3682 O OD2 . ASP B 194 ? 1.5371 1.4098 1.3709 -0.2197 0.3548  0.1632  1231 ASP B OD2 
3683 N N   . LYS B 195 ? 1.5342 1.6498 1.3924 -0.1385 0.4348  0.1188  1232 LYS B N   
3684 C CA  . LYS B 195 ? 1.5213 1.7410 1.4125 -0.1173 0.4620  0.1021  1232 LYS B CA  
3685 C C   . LYS B 195 ? 1.5510 1.7403 1.4020 -0.0637 0.4497  0.0917  1232 LYS B C   
3686 O O   . LYS B 195 ? 1.5103 1.7037 1.3929 -0.0260 0.4241  0.0800  1232 LYS B O   
3687 C CB  . LYS B 195 ? 1.4340 1.7373 1.4165 -0.1129 0.4569  0.0899  1232 LYS B CB  
3688 C CG  . LYS B 195 ? 1.4095 1.8311 1.4353 -0.0894 0.4825  0.0708  1232 LYS B CG  
3689 C CD  . LYS B 195 ? 1.3282 1.8200 1.4380 -0.0816 0.4710  0.0583  1232 LYS B CD  
3690 C CE  . LYS B 195 ? 1.3103 1.9182 1.4612 -0.0507 0.4918  0.0374  1232 LYS B CE  
3691 N NZ  . LYS B 195 ? 1.2398 1.9059 1.4664 -0.0410 0.4759  0.0249  1232 LYS B NZ  
3692 N N   . GLU B 196 ? 1.6324 1.7840 1.4060 -0.0622 0.4672  0.0967  1233 GLU B N   
3693 C CA  . GLU B 196 ? 1.6702 1.7865 1.3908 -0.0126 0.4579  0.0869  1233 GLU B CA  
3694 C C   . GLU B 196 ? 1.7580 1.8661 1.4007 -0.0202 0.4942  0.0915  1233 GLU B C   
3695 O O   . GLU B 196 ? 1.8050 1.8530 1.3999 -0.0605 0.5001  0.1095  1233 GLU B O   
3696 C CB  . GLU B 196 ? 1.6759 1.6788 1.3644 0.0055  0.4079  0.0934  1233 GLU B CB  
3697 C CG  . GLU B 196 ? 1.7172 1.6742 1.3512 0.0560  0.3891  0.0829  1233 GLU B CG  
3698 C CD  . GLU B 196 ? 1.8201 1.6996 1.3510 0.0608  0.3957  0.0899  1233 GLU B CD  
3699 O OE1 . GLU B 196 ? 1.8652 1.7134 1.3609 0.0227  0.4115  0.1052  1233 GLU B OE1 
3700 O OE2 . GLU B 196 ? 1.8638 1.7063 1.3421 0.1030  0.3830  0.0801  1233 GLU B OE2 
3701 N N   . ALA B 206 ? 0.8860 1.3581 0.9968 0.1041  0.3962  0.0033  1243 ALA B N   
3702 C CA  . ALA B 206 ? 0.8581 1.2516 0.9745 0.0759  0.3689  0.0202  1243 ALA B CA  
3703 C C   . ALA B 206 ? 0.8200 1.1826 0.9549 0.1049  0.3327  0.0126  1243 ALA B C   
3704 O O   . ALA B 206 ? 0.8452 1.1803 0.9448 0.1464  0.3166  0.0019  1243 ALA B O   
3705 C CB  . ALA B 206 ? 0.9108 1.2106 0.9593 0.0650  0.3619  0.0364  1243 ALA B CB  
3706 N N   . LYS B 207 ? 0.7667 1.1285 0.9502 0.0818  0.3200  0.0188  1244 LYS B N   
3707 C CA  . LYS B 207 ? 0.7313 1.0677 0.9349 0.1019  0.2892  0.0137  1244 LYS B CA  
3708 C C   . LYS B 207 ? 0.7333 0.9781 0.9129 0.0917  0.2618  0.0304  1244 LYS B C   
3709 O O   . LYS B 207 ? 0.7143 0.9410 0.9115 0.0599  0.2620  0.0445  1244 LYS B O   
3710 C CB  . LYS B 207 ? 0.6773 1.0729 0.9470 0.0859  0.2931  0.0090  1244 LYS B CB  
3711 C CG  . LYS B 207 ? 0.6704 1.1639 0.9732 0.1022  0.3118  -0.0101 1244 LYS B CG  
3712 C CD  . LYS B 207 ? 0.6218 1.1657 0.9860 0.0873  0.3095  -0.0151 1244 LYS B CD  
3713 C CE  . LYS B 207 ? 0.6152 1.2575 1.0147 0.1106  0.3208  -0.0364 1244 LYS B CE  
3714 N NZ  . LYS B 207 ? 0.6401 1.3586 1.0453 0.0966  0.3555  -0.0381 1244 LYS B NZ  
3715 N N   . LEU B 208 ? 0.7596 0.9477 0.8974 0.1199  0.2367  0.0281  1245 LEU B N   
3716 C CA  . LEU B 208 ? 0.7667 0.8755 0.8827 0.1118  0.2080  0.0432  1245 LEU B CA  
3717 C C   . LEU B 208 ? 0.7380 0.8268 0.8710 0.1246  0.1793  0.0404  1245 LEU B C   
3718 O O   . LEU B 208 ? 0.7376 0.8486 0.8700 0.1504  0.1761  0.0250  1245 LEU B O   
3719 C CB  . LEU B 208 ? 0.8356 0.8862 0.8802 0.1273  0.1995  0.0455  1245 LEU B CB  
3720 C CG  . LEU B 208 ? 0.8741 0.9218 0.8886 0.1096  0.2239  0.0532  1245 LEU B CG  
3721 C CD1 . LEU B 208 ? 0.8837 1.0079 0.9035 0.1157  0.2617  0.0403  1245 LEU B CD1 
3722 C CD2 . LEU B 208 ? 0.9416 0.9090 0.8829 0.1214  0.2052  0.0595  1245 LEU B CD2 
3723 N N   . PRO B 209 ? 0.7180 0.7648 0.8639 0.1074  0.1575  0.0553  1246 PRO B N   
3724 C CA  . PRO B 209 ? 0.7009 0.7258 0.8584 0.1137  0.1311  0.0556  1246 PRO B CA  
3725 C C   . PRO B 209 ? 0.7542 0.7156 0.8528 0.1326  0.1020  0.0547  1246 PRO B C   
3726 O O   . PRO B 209 ? 0.7742 0.6862 0.8555 0.1208  0.0802  0.0685  1246 PRO B O   
3727 C CB  . PRO B 209 ? 0.6669 0.6824 0.8623 0.0864  0.1246  0.0728  1246 PRO B CB  
3728 C CG  . PRO B 209 ? 0.6948 0.6857 0.8661 0.0746  0.1296  0.0833  1246 PRO B CG  
3729 C CD  . PRO B 209 ? 0.7178 0.7379 0.8662 0.0818  0.1571  0.0725  1246 PRO B CD  
3730 N N   . VAL B 210 ? 0.7813 0.7431 0.8473 0.1631  0.0994  0.0378  1247 VAL B N   
3731 C CA  . VAL B 210 ? 0.8490 0.7439 0.8424 0.1862  0.0737  0.0339  1247 VAL B CA  
3732 C C   . VAL B 210 ? 0.8576 0.6955 0.8408 0.1756  0.0365  0.0435  1247 VAL B C   
3733 O O   . VAL B 210 ? 0.9151 0.6843 0.8437 0.1774  0.0083  0.0494  1247 VAL B O   
3734 C CB  . VAL B 210 ? 0.8846 0.7966 0.8418 0.2278  0.0818  0.0110  1247 VAL B CB  
3735 C CG1 . VAL B 210 ? 0.8754 0.8575 0.8488 0.2344  0.1215  0.0025  1247 VAL B CG1 
3736 C CG2 . VAL B 210 ? 0.8631 0.7942 0.8416 0.2412  0.0735  -0.0004 1247 VAL B CG2 
3737 N N   . LYS B 211 ? 0.8061 0.6713 0.8389 0.1622  0.0361  0.0457  1248 LYS B N   
3738 C CA  . LYS B 211 ? 0.8176 0.6363 0.8410 0.1497  0.0047  0.0546  1248 LYS B CA  
3739 C C   . LYS B 211 ? 0.8025 0.6066 0.8515 0.1161  -0.0081 0.0767  1248 LYS B C   
3740 O O   . LYS B 211 ? 0.8331 0.5894 0.8606 0.1025  -0.0390 0.0871  1248 LYS B O   
3741 C CB  . LYS B 211 ? 0.7770 0.6294 0.8381 0.1493  0.0114  0.0484  1248 LYS B CB  
3742 C CG  . LYS B 211 ? 0.7956 0.6640 0.8323 0.1861  0.0187  0.0252  1248 LYS B CG  
3743 C CD  . LYS B 211 ? 0.7862 0.6535 0.8315 0.1894  0.0099  0.0192  1248 LYS B CD  
3744 C CE  . LYS B 211 ? 0.8156 0.6931 0.8299 0.2320  0.0107  -0.0053 1248 LYS B CE  
3745 N NZ  . LYS B 211 ? 0.8210 0.6801 0.8293 0.2365  -0.0040 -0.0108 1248 LYS B NZ  
3746 N N   . TRP B 212 ? 0.7616 0.6062 0.8540 0.1027  0.0137  0.0839  1249 TRP B N   
3747 C CA  . TRP B 212 ? 0.7518 0.5877 0.8686 0.0778  0.0017  0.1028  1249 TRP B CA  
3748 C C   . TRP B 212 ? 0.8065 0.5968 0.8731 0.0821  -0.0112 0.1068  1249 TRP B C   
3749 O O   . TRP B 212 ? 0.8184 0.5865 0.8898 0.0656  -0.0324 0.1215  1249 TRP B O   
3750 C CB  . TRP B 212 ? 0.6890 0.5810 0.8705 0.0640  0.0277  0.1083  1249 TRP B CB  
3751 C CG  . TRP B 212 ? 0.6411 0.5686 0.8705 0.0561  0.0349  0.1085  1249 TRP B CG  
3752 C CD1 . TRP B 212 ? 0.6144 0.5543 0.8848 0.0376  0.0267  0.1221  1249 TRP B CD1 
3753 C CD2 . TRP B 212 ? 0.6181 0.5751 0.8578 0.0677  0.0521  0.0941  1249 TRP B CD2 
3754 N NE1 . TRP B 212 ? 0.5805 0.5492 0.8802 0.0365  0.0390  0.1176  1249 TRP B NE1 
3755 C CE2 . TRP B 212 ? 0.5823 0.5591 0.8633 0.0546  0.0528  0.1004  1249 TRP B CE2 
3756 C CE3 . TRP B 212 ? 0.6270 0.5995 0.8462 0.0892  0.0666  0.0762  1249 TRP B CE3 
3757 C CZ2 . TRP B 212 ? 0.5596 0.5612 0.8557 0.0617  0.0651  0.0895  1249 TRP B CZ2 
3758 C CZ3 . TRP B 212 ? 0.6006 0.6053 0.8416 0.0967  0.0773  0.0650  1249 TRP B CZ3 
3759 C CH2 . TRP B 212 ? 0.5692 0.5832 0.8453 0.0828  0.0754  0.0716  1249 TRP B CH2 
3760 N N   . MET B 213 ? 0.8429 0.6220 0.8613 0.1057  0.0015  0.0932  1250 MET B N   
3761 C CA  . MET B 213 ? 0.8997 0.6331 0.8614 0.1129  -0.0058 0.0953  1250 MET B CA  
3762 C C   . MET B 213 ? 0.9680 0.6252 0.8692 0.1166  -0.0478 0.0988  1250 MET B C   
3763 O O   . MET B 213 ? 0.9836 0.6205 0.8675 0.1231  -0.0647 0.0934  1250 MET B O   
3764 C CB  . MET B 213 ? 0.9205 0.6712 0.8474 0.1382  0.0237  0.0792  1250 MET B CB  
3765 C CG  . MET B 213 ? 0.8851 0.6855 0.8456 0.1260  0.0593  0.0816  1250 MET B CG  
3766 S SD  . MET B 213 ? 0.8854 0.7446 0.8370 0.1486  0.1009  0.0617  1250 MET B SD  
3767 C CE  . MET B 213 ? 0.9748 0.7789 0.8375 0.1656  0.1020  0.0605  1250 MET B CE  
3768 N N   . ALA B 214 ? 1.0161 0.6252 0.8793 0.1115  -0.0665 0.1080  1251 ALA B N   
3769 C CA  . ALA B 214 ? 1.0920 0.6210 0.8903 0.1122  -0.1098 0.1124  1251 ALA B CA  
3770 C C   . ALA B 214 ? 1.1688 0.6479 0.8779 0.1478  -0.1086 0.0958  1251 ALA B C   
3771 O O   . ALA B 214 ? 1.1603 0.6755 0.8644 0.1694  -0.0721 0.0831  1251 ALA B O   
3772 C CB  . ALA B 214 ? 1.1125 0.6127 0.9085 0.0935  -0.1326 0.1284  1251 ALA B CB  
3773 N N   . LEU B 215 ? 1.2500 0.6460 0.8869 0.1531  -0.1495 0.0964  1252 LEU B N   
3774 C CA  . LEU B 215 ? 1.3379 0.6732 0.8782 0.1917  -0.1548 0.0799  1252 LEU B CA  
3775 C C   . LEU B 215 ? 1.3773 0.7008 0.8738 0.2094  -0.1345 0.0763  1252 LEU B C   
3776 O O   . LEU B 215 ? 1.4187 0.7370 0.8615 0.2467  -0.1137 0.0593  1252 LEU B O   
3777 C CB  . LEU B 215 ? 1.4245 0.6596 0.8916 0.1862  -0.2097 0.0850  1252 LEU B CB  
3778 C CG  . LEU B 215 ? 1.5286 0.6841 0.8830 0.2298  -0.2234 0.0669  1252 LEU B CG  
3779 C CD1 . LEU B 215 ? 1.5094 0.7000 0.8703 0.2588  -0.2034 0.0485  1252 LEU B CD1 
3780 C CD2 . LEU B 215 ? 1.6260 0.6681 0.8996 0.2168  -0.2831 0.0754  1252 LEU B CD2 
3781 N N   . GLU B 216 ? 1.3689 0.6888 0.8863 0.1840  -0.1404 0.0921  1253 GLU B N   
3782 C CA  . GLU B 216 ? 1.4069 0.7131 0.8835 0.1947  -0.1203 0.0914  1253 GLU B CA  
3783 C C   . GLU B 216 ? 1.3469 0.7423 0.8735 0.2005  -0.0639 0.0833  1253 GLU B C   
3784 O O   . GLU B 216 ? 1.3864 0.7852 0.8657 0.2254  -0.0351 0.0720  1253 GLU B O   
3785 C CB  . GLU B 216 ? 1.4103 0.6914 0.9007 0.1659  -0.1432 0.1103  1253 GLU B CB  
3786 C CG  . GLU B 216 ? 1.4720 0.6726 0.9210 0.1535  -0.2020 0.1205  1253 GLU B CG  
3787 C CD  . GLU B 216 ? 1.4174 0.6487 0.9397 0.1230  -0.2275 0.1316  1253 GLU B CD  
3788 O OE1 . GLU B 216 ? 1.4559 0.6451 0.9450 0.1231  -0.2566 0.1292  1253 GLU B OE1 
3789 O OE2 . GLU B 216 ? 1.3431 0.6379 0.9508 0.0997  -0.2178 0.1425  1253 GLU B OE2 
3790 N N   . SER B 217 ? 1.2567 0.7246 0.8776 0.1760  -0.0489 0.0898  1254 SER B N   
3791 C CA  . SER B 217 ? 1.1991 0.7486 0.8731 0.1719  -0.0008 0.0855  1254 SER B CA  
3792 C C   . SER B 217 ? 1.2029 0.7948 0.8649 0.2024  0.0284  0.0652  1254 SER B C   
3793 O O   . SER B 217 ? 1.1984 0.8383 0.8631 0.2080  0.0681  0.0588  1254 SER B O   
3794 C CB  . SER B 217 ? 1.1121 0.7184 0.8793 0.1436  0.0028  0.0950  1254 SER B CB  
3795 O OG  . SER B 217 ? 1.1116 0.6888 0.8930 0.1203  -0.0219 0.1124  1254 SER B OG  
3796 N N   . LEU B 218 ? 1.2165 0.7915 0.8642 0.2216  0.0075  0.0554  1255 LEU B N   
3797 C CA  . LEU B 218 ? 1.2267 0.8402 0.8619 0.2571  0.0290  0.0343  1255 LEU B CA  
3798 C C   . LEU B 218 ? 1.3124 0.8977 0.8640 0.2916  0.0429  0.0228  1255 LEU B C   
3799 O O   . LEU B 218 ? 1.3057 0.9576 0.8657 0.3126  0.0815  0.0089  1255 LEU B O   
3800 C CB  . LEU B 218 ? 1.2404 0.8174 0.8600 0.2709  -0.0047 0.0276  1255 LEU B CB  
3801 C CG  . LEU B 218 ? 1.1605 0.7755 0.8611 0.2414  -0.0116 0.0361  1255 LEU B CG  
3802 C CD1 . LEU B 218 ? 1.1912 0.7625 0.8610 0.2561  -0.0431 0.0286  1255 LEU B CD1 
3803 C CD2 . LEU B 218 ? 1.0794 0.7966 0.8598 0.2351  0.0306  0.0307  1255 LEU B CD2 
3804 N N   . GLN B 219 ? 1.3969 0.8861 0.8682 0.2968  0.0113  0.0289  1256 GLN B N   
3805 C CA  . GLN B 219 ? 1.4939 0.9395 0.8708 0.3330  0.0197  0.0181  1256 GLN B CA  
3806 C C   . GLN B 219 ? 1.5067 0.9618 0.8763 0.3146  0.0476  0.0285  1256 GLN B C   
3807 O O   . GLN B 219 ? 1.5095 1.0240 0.8782 0.3275  0.0926  0.0198  1256 GLN B O   
3808 C CB  . GLN B 219 ? 1.5890 0.9136 0.8705 0.3492  -0.0324 0.0185  1256 GLN B CB  
3809 C CG  . GLN B 219 ? 1.6030 0.9023 0.8697 0.3699  -0.0609 0.0072  1256 GLN B CG  
3810 C CD  . GLN B 219 ? 1.7103 0.8804 0.8721 0.3825  -0.1149 0.0083  1256 GLN B CD  
3811 O OE1 . GLN B 219 ? 1.7738 0.8733 0.8758 0.3761  -0.1334 0.0174  1256 GLN B OE1 
3812 N NE2 . GLN B 219 ? 1.7392 0.8702 0.8715 0.3995  -0.1433 -0.0008 1256 GLN B NE2 
3813 N N   . THR B 220 ? 1.5199 0.9175 0.8836 0.2835  0.0195  0.0474  1257 THR B N   
3814 C CA  . THR B 220 ? 1.5602 0.9340 0.8903 0.2696  0.0341  0.0578  1257 THR B CA  
3815 C C   . THR B 220 ? 1.4845 0.9397 0.8970 0.2356  0.0706  0.0667  1257 THR B C   
3816 O O   . THR B 220 ? 1.5109 0.9763 0.8987 0.2289  0.1028  0.0696  1257 THR B O   
3817 C CB  . THR B 220 ? 1.6112 0.8854 0.8961 0.2542  -0.0164 0.0730  1257 THR B CB  
3818 O OG1 . THR B 220 ? 1.5341 0.8322 0.9031 0.2203  -0.0396 0.0864  1257 THR B OG1 
3819 C CG2 . THR B 220 ? 1.7021 0.8826 0.8961 0.2828  -0.0578 0.0657  1257 THR B CG2 
3820 N N   . GLN B 221 ? 1.4016 0.9076 0.9043 0.2134  0.0644  0.0716  1258 GLN B N   
3821 C CA  . GLN B 221 ? 1.3353 0.9029 0.9126 0.1799  0.0892  0.0813  1258 GLN B CA  
3822 C C   . GLN B 221 ? 1.3633 0.8725 0.9221 0.1558  0.0688  0.0994  1258 GLN B C   
3823 O O   . GLN B 221 ? 1.3586 0.8839 0.9245 0.1358  0.0938  0.1067  1258 GLN B O   
3824 C CB  . GLN B 221 ? 1.3266 0.9681 0.9148 0.1807  0.1432  0.0730  1258 GLN B CB  
3825 C CG  . GLN B 221 ? 1.3087 1.0149 0.9155 0.2100  0.1623  0.0531  1258 GLN B CG  
3826 C CD  . GLN B 221 ? 1.2947 1.0903 0.9267 0.2054  0.2150  0.0460  1258 GLN B CD  
3827 O OE1 . GLN B 221 ? 1.3006 1.1063 0.9338 0.1756  0.2386  0.0571  1258 GLN B OE1 
3828 N NE2 . GLN B 221 ? 1.2830 1.1443 0.9338 0.2342  0.2322  0.0275  1258 GLN B NE2 
3829 N N   . LYS B 222 ? 1.3993 0.8389 0.9318 0.1574  0.0207  0.1065  1259 LYS B N   
3830 C CA  . LYS B 222 ? 1.4171 0.8096 0.9476 0.1367  -0.0078 0.1231  1259 LYS B CA  
3831 C C   . LYS B 222 ? 1.3376 0.7731 0.9604 0.1162  -0.0255 0.1314  1259 LYS B C   
3832 O O   . LYS B 222 ? 1.3064 0.7592 0.9607 0.1196  -0.0417 0.1275  1259 LYS B O   
3833 C CB  . LYS B 222 ? 1.5058 0.8019 0.9547 0.1489  -0.0521 0.1262  1259 LYS B CB  
3834 C CG  . LYS B 222 ? 1.6012 0.8426 0.9464 0.1723  -0.0370 0.1185  1259 LYS B CG  
3835 C CD  . LYS B 222 ? 1.6948 0.8329 0.9537 0.1858  -0.0854 0.1206  1259 LYS B CD  
3836 C CE  . LYS B 222 ? 1.7970 0.8767 0.9450 0.2135  -0.0688 0.1118  1259 LYS B CE  
3837 N NZ  . LYS B 222 ? 1.8261 0.8979 0.9455 0.2019  -0.0398 0.1191  1259 LYS B NZ  
3838 N N   . PHE B 223 ? 1.3139 0.7627 0.9734 0.0964  -0.0221 0.1426  1260 PHE B N   
3839 C CA  . PHE B 223 ? 1.2419 0.7382 0.9885 0.0804  -0.0325 0.1498  1260 PHE B CA  
3840 C C   . PHE B 223 ? 1.2664 0.7239 1.0146 0.0711  -0.0684 0.1640  1260 PHE B C   
3841 O O   . PHE B 223 ? 1.3128 0.7321 1.0196 0.0693  -0.0651 0.1691  1260 PHE B O   
3842 C CB  . PHE B 223 ? 1.1819 0.7456 0.9813 0.0698  0.0095  0.1469  1260 PHE B CB  
3843 C CG  . PHE B 223 ? 1.1550 0.7702 0.9657 0.0790  0.0424  0.1324  1260 PHE B CG  
3844 C CD1 . PHE B 223 ? 1.2018 0.8107 0.9553 0.0910  0.0692  0.1232  1260 PHE B CD1 
3845 C CD2 . PHE B 223 ? 1.0868 0.7585 0.9639 0.0777  0.0461  0.1274  1260 PHE B CD2 
3846 C CE1 . PHE B 223 ? 1.1776 0.8435 0.9467 0.1034  0.0978  0.1086  1260 PHE B CE1 
3847 C CE2 . PHE B 223 ? 1.0655 0.7842 0.9521 0.0894  0.0725  0.1129  1260 PHE B CE2 
3848 C CZ  . PHE B 223 ? 1.1094 0.8287 0.9450 0.1033  0.0976  0.1031  1260 PHE B CZ  
3849 N N   . THR B 224 ? 1.2410 0.7105 1.0364 0.0651  -0.1031 0.1703  1261 THR B N   
3850 C CA  . THR B 224 ? 1.2584 0.7068 1.0687 0.0582  -0.1415 0.1831  1261 THR B CA  
3851 C C   . THR B 224 ? 1.1868 0.7026 1.0915 0.0468  -0.1512 0.1888  1261 THR B C   
3852 O O   . THR B 224 ? 1.1273 0.6973 1.0780 0.0439  -0.1249 0.1832  1261 THR B O   
3853 C CB  . THR B 224 ? 1.3370 0.7112 1.0810 0.0626  -0.1850 0.1862  1261 THR B CB  
3854 O OG1 . THR B 224 ? 1.3306 0.7080 1.0771 0.0613  -0.1982 0.1819  1261 THR B OG1 
3855 C CG2 . THR B 224 ? 1.4186 0.7213 1.0628 0.0759  -0.1751 0.1813  1261 THR B CG2 
3856 N N   . THR B 225 ? 1.1768 0.7931 0.9546 0.0318  -0.3504 0.2256  1262 THR B N   
3857 C CA  . THR B 225 ? 1.1085 0.7701 0.9847 0.0178  -0.3641 0.1997  1262 THR B CA  
3858 C C   . THR B 225 ? 1.0717 0.7547 0.9461 -0.0009 -0.3655 0.1680  1262 THR B C   
3859 O O   . THR B 225 ? 0.9983 0.7178 0.9453 -0.0178 -0.3510 0.1484  1262 THR B O   
3860 C CB  . THR B 225 ? 1.1400 0.8121 1.0507 0.0330  -0.4143 0.2052  1262 THR B CB  
3861 O OG1 . THR B 225 ? 1.1873 0.8314 1.0917 0.0532  -0.4116 0.2385  1262 THR B OG1 
3862 C CG2 . THR B 225 ? 1.0698 0.7943 1.0914 0.0212  -0.4228 0.1828  1262 THR B CG2 
3863 N N   . LYS B 226 ? 1.1319 0.7883 0.9189 0.0042  -0.3825 0.1636  1263 LYS B N   
3864 C CA  . LYS B 226 ? 1.1145 0.7798 0.8924 -0.0112 -0.3892 0.1346  1263 LYS B CA  
3865 C C   . LYS B 226 ? 1.0583 0.7324 0.8445 -0.0259 -0.3383 0.1264  1263 LYS B C   
3866 O O   . LYS B 226 ? 1.0075 0.7046 0.8323 -0.0432 -0.3340 0.1047  1263 LYS B O   
3867 C CB  . LYS B 226 ? 1.2036 0.8289 0.8761 0.0026  -0.4197 0.1301  1263 LYS B CB  
3868 C CG  . LYS B 226 ? 1.2759 0.8897 0.9260 0.0202  -0.4777 0.1360  1263 LYS B CG  
3869 C CD  . LYS B 226 ? 1.2391 0.8941 0.9883 0.0065  -0.5183 0.1192  1263 LYS B CD  
3870 C CE  . LYS B 226 ? 1.3165 0.9631 1.0452 0.0249  -0.5823 0.1227  1263 LYS B CE  
3871 N NZ  . LYS B 226 ? 1.2777 0.9729 1.1184 0.0097  -0.6202 0.1070  1263 LYS B NZ  
3872 N N   . SER B 227 ? 1.0713 0.7275 0.8233 -0.0187 -0.3009 0.1459  1264 SER B N   
3873 C CA  . SER B 227 ? 1.0210 0.6894 0.7874 -0.0309 -0.2554 0.1395  1264 SER B CA  
3874 C C   . SER B 227 ? 0.9449 0.6512 0.8089 -0.0453 -0.2402 0.1305  1264 SER B C   
3875 O O   . SER B 227 ? 0.8943 0.6220 0.7842 -0.0582 -0.2170 0.1144  1264 SER B O   
3876 C CB  . SER B 227 ? 1.0593 0.7030 0.7742 -0.0207 -0.2214 0.1641  1264 SER B CB  
3877 O OG  . SER B 227 ? 1.0742 0.7111 0.8194 -0.0147 -0.2161 0.1897  1264 SER B OG  
3878 N N   . ASP B 228 ? 0.9449 0.6579 0.8584 -0.0396 -0.2540 0.1408  1265 ASP B N   
3879 C CA  . ASP B 228 ? 0.8848 0.6311 0.8868 -0.0477 -0.2421 0.1297  1265 ASP B CA  
3880 C C   . ASP B 228 ? 0.8460 0.6284 0.8939 -0.0577 -0.2590 0.1075  1265 ASP B C   
3881 O O   . ASP B 228 ? 0.7905 0.6039 0.8914 -0.0670 -0.2388 0.0924  1265 ASP B O   
3882 C CB  . ASP B 228 ? 0.9054 0.6433 0.9455 -0.0346 -0.2513 0.1473  1265 ASP B CB  
3883 C CG  . ASP B 228 ? 0.9395 0.6425 0.9529 -0.0285 -0.2276 0.1724  1265 ASP B CG  
3884 O OD1 . ASP B 228 ? 0.9428 0.6342 0.9115 -0.0347 -0.2020 0.1760  1265 ASP B OD1 
3885 O OD2 . ASP B 228 ? 0.9632 0.6511 1.0058 -0.0174 -0.2338 0.1897  1265 ASP B OD2 
3886 N N   . VAL B 229 ? 0.8815 0.6594 0.9092 -0.0555 -0.2964 0.1063  1266 VAL B N   
3887 C CA  . VAL B 229 ? 0.8549 0.6649 0.9299 -0.0685 -0.3133 0.0886  1266 VAL B CA  
3888 C C   . VAL B 229 ? 0.8259 0.6386 0.8814 -0.0834 -0.2880 0.0741  1266 VAL B C   
3889 O O   . VAL B 229 ? 0.7803 0.6268 0.8907 -0.0952 -0.2741 0.0633  1266 VAL B O   
3890 C CB  . VAL B 229 ? 0.9072 0.7067 0.9637 -0.0648 -0.3641 0.0885  1266 VAL B CB  
3891 C CG1 . VAL B 229 ? 0.8858 0.7129 0.9900 -0.0837 -0.3802 0.0708  1266 VAL B CG1 
3892 C CG2 . VAL B 229 ? 0.9352 0.7404 1.0240 -0.0482 -0.3931 0.1031  1266 VAL B CG2 
3893 N N   . TRP B 230 ? 0.8596 0.6370 0.8354 -0.0801 -0.2805 0.0758  1267 TRP B N   
3894 C CA  . TRP B 230 ? 0.8386 0.6144 0.7912 -0.0895 -0.2557 0.0642  1267 TRP B CA  
3895 C C   . TRP B 230 ? 0.7794 0.5840 0.7767 -0.0944 -0.2179 0.0614  1267 TRP B C   
3896 O O   . TRP B 230 ? 0.7429 0.5692 0.7656 -0.1046 -0.2043 0.0502  1267 TRP B O   
3897 C CB  . TRP B 230 ? 0.8917 0.6267 0.7535 -0.0789 -0.2497 0.0686  1267 TRP B CB  
3898 C CG  . TRP B 230 ? 0.8797 0.6112 0.7164 -0.0842 -0.2259 0.0573  1267 TRP B CG  
3899 C CD1 . TRP B 230 ? 0.8355 0.5874 0.6938 -0.0883 -0.1900 0.0558  1267 TRP B CD1 
3900 C CD2 . TRP B 230 ? 0.9189 0.6227 0.7044 -0.0839 -0.2395 0.0445  1267 TRP B CD2 
3901 N NE1 . TRP B 230 ? 0.8407 0.5823 0.6660 -0.0891 -0.1797 0.0460  1267 TRP B NE1 
3902 C CE2 . TRP B 230 ? 0.8913 0.6009 0.6717 -0.0864 -0.2080 0.0388  1267 TRP B CE2 
3903 C CE3 . TRP B 230 ? 0.9789 0.6511 0.7226 -0.0806 -0.2780 0.0353  1267 TRP B CE3 
3904 C CZ2 . TRP B 230 ? 0.9210 0.6038 0.6574 -0.0844 -0.2111 0.0263  1267 TRP B CZ2 
3905 C CZ3 . TRP B 230 ? 1.0104 0.6534 0.7093 -0.0804 -0.2823 0.0195  1267 TRP B CZ3 
3906 C CH2 . TRP B 230 ? 0.9821 0.6293 0.6781 -0.0817 -0.2477 0.0161  1267 TRP B CH2 
3907 N N   . SER B 231 ? 0.7766 0.5780 0.7812 -0.0866 -0.2028 0.0720  1268 SER B N   
3908 C CA  . SER B 231 ? 0.7315 0.5549 0.7762 -0.0899 -0.1726 0.0657  1268 SER B CA  
3909 C C   . SER B 231 ? 0.6948 0.5554 0.8093 -0.0935 -0.1734 0.0539  1268 SER B C   
3910 O O   . SER B 231 ? 0.6590 0.5431 0.7962 -0.0976 -0.1516 0.0411  1268 SER B O   
3911 C CB  . SER B 231 ? 0.7477 0.5536 0.7923 -0.0827 -0.1613 0.0798  1268 SER B CB  
3912 O OG  . SER B 231 ? 0.7855 0.5615 0.7661 -0.0781 -0.1541 0.0945  1268 SER B OG  
3913 N N   . PHE B 232 ? 0.7095 0.5773 0.8566 -0.0894 -0.1987 0.0588  1269 PHE B N   
3914 C CA  . PHE B 232 ? 0.6823 0.5903 0.9004 -0.0903 -0.1979 0.0501  1269 PHE B CA  
3915 C C   . PHE B 232 ? 0.6622 0.5926 0.8882 -0.1036 -0.1925 0.0418  1269 PHE B C   
3916 O O   . PHE B 232 ? 0.6343 0.5991 0.9028 -0.1052 -0.1725 0.0338  1269 PHE B O   
3917 C CB  . PHE B 232 ? 0.7050 0.6185 0.9609 -0.0818 -0.2290 0.0594  1269 PHE B CB  
3918 C CG  . PHE B 232 ? 0.6787 0.6398 1.0158 -0.0808 -0.2267 0.0524  1269 PHE B CG  
3919 C CD1 . PHE B 232 ? 0.6555 0.6378 1.0343 -0.0714 -0.2004 0.0429  1269 PHE B CD1 
3920 C CD2 . PHE B 232 ? 0.6831 0.6689 1.0575 -0.0888 -0.2501 0.0541  1269 PHE B CD2 
3921 C CE1 . PHE B 232 ? 0.6383 0.6672 1.0889 -0.0666 -0.1931 0.0369  1269 PHE B CE1 
3922 C CE2 . PHE B 232 ? 0.6606 0.6966 1.1174 -0.0875 -0.2428 0.0509  1269 PHE B CE2 
3923 C CZ  . PHE B 232 ? 0.6392 0.6977 1.1312 -0.0748 -0.2119 0.0430  1269 PHE B CZ  
3924 N N   . GLY B 233 ? 0.6857 0.5933 0.8684 -0.1116 -0.2099 0.0443  1270 GLY B N   
3925 C CA  . GLY B 233 ? 0.6763 0.5934 0.8611 -0.1253 -0.2047 0.0388  1270 GLY B CA  
3926 C C   . GLY B 233 ? 0.6487 0.5763 0.8207 -0.1258 -0.1685 0.0326  1270 GLY B C   
3927 O O   . GLY B 233 ? 0.6271 0.5822 0.8302 -0.1320 -0.1529 0.0307  1270 GLY B O   
3928 N N   . VAL B 234 ? 0.6526 0.5601 0.7807 -0.1185 -0.1555 0.0311  1271 VAL B N   
3929 C CA  . VAL B 234 ? 0.6309 0.5484 0.7454 -0.1172 -0.1274 0.0236  1271 VAL B CA  
3930 C C   . VAL B 234 ? 0.6046 0.5567 0.7670 -0.1119 -0.1104 0.0149  1271 VAL B C   
3931 O O   . VAL B 234 ? 0.5896 0.5625 0.7536 -0.1111 -0.0911 0.0075  1271 VAL B O   
3932 C CB  . VAL B 234 ? 0.6434 0.5359 0.7118 -0.1117 -0.1198 0.0250  1271 VAL B CB  
3933 C CG1 . VAL B 234 ? 0.6228 0.5313 0.6863 -0.1099 -0.0959 0.0154  1271 VAL B CG1 
3934 C CG2 . VAL B 234 ? 0.6789 0.5363 0.6915 -0.1115 -0.1332 0.0316  1271 VAL B CG2 
3935 N N   . LEU B 235 ? 0.6058 0.5613 0.8026 -0.1053 -0.1183 0.0154  1272 LEU B N   
3936 C CA  . LEU B 235 ? 0.5901 0.5729 0.8314 -0.0963 -0.1039 0.0037  1272 LEU B CA  
3937 C C   . LEU B 235 ? 0.5788 0.5994 0.8566 -0.0973 -0.0943 0.0025  1272 LEU B C   
3938 O O   . LEU B 235 ? 0.5696 0.6151 0.8574 -0.0898 -0.0720 -0.0091 1272 LEU B O   
3939 C CB  . LEU B 235 ? 0.6026 0.5738 0.8738 -0.0874 -0.1178 0.0076  1272 LEU B CB  
3940 C CG  . LEU B 235 ? 0.5979 0.5840 0.9103 -0.0744 -0.1045 -0.0080 1272 LEU B CG  
3941 C CD1 . LEU B 235 ? 0.6196 0.5771 0.9481 -0.0664 -0.1178 -0.0011 1272 LEU B CD1 
3942 C CD2 . LEU B 235 ? 0.5886 0.6162 0.9498 -0.0671 -0.0963 -0.0137 1272 LEU B CD2 
3943 N N   . LEU B 236 ? 0.5839 0.6090 0.8815 -0.1062 -0.1113 0.0149  1273 LEU B N   
3944 C CA  . LEU B 236 ? 0.5758 0.6385 0.9180 -0.1112 -0.1007 0.0195  1273 LEU B CA  
3945 C C   . LEU B 236 ? 0.5711 0.6376 0.8803 -0.1168 -0.0779 0.0201  1273 LEU B C   
3946 O O   . LEU B 236 ? 0.5663 0.6667 0.8991 -0.1130 -0.0530 0.0210  1273 LEU B O   
3947 C CB  . LEU B 236 ? 0.5892 0.6509 0.9621 -0.1238 -0.1302 0.0318  1273 LEU B CB  
3948 C CG  . LEU B 236 ? 0.5968 0.6694 1.0194 -0.1154 -0.1534 0.0343  1273 LEU B CG  
3949 C CD1 . LEU B 236 ? 0.6154 0.6888 1.0670 -0.1290 -0.1885 0.0438  1273 LEU B CD1 
3950 C CD2 . LEU B 236 ? 0.5827 0.7016 1.0694 -0.1015 -0.1302 0.0297  1273 LEU B CD2 
3951 N N   . TRP B 237 ? 0.5779 0.6093 0.8306 -0.1232 -0.0852 0.0212  1274 TRP B N   
3952 C CA  . TRP B 237 ? 0.5794 0.6084 0.7968 -0.1260 -0.0674 0.0236  1274 TRP B CA  
3953 C C   . TRP B 237 ? 0.5732 0.6229 0.7767 -0.1112 -0.0422 0.0111  1274 TRP B C   
3954 O O   . TRP B 237 ? 0.5771 0.6458 0.7732 -0.1080 -0.0213 0.0150  1274 TRP B O   
3955 C CB  . TRP B 237 ? 0.5901 0.5768 0.7516 -0.1308 -0.0811 0.0248  1274 TRP B CB  
3956 C CG  . TRP B 237 ? 0.5972 0.5765 0.7271 -0.1330 -0.0675 0.0303  1274 TRP B CG  
3957 C CD1 . TRP B 237 ? 0.6135 0.5835 0.7511 -0.1453 -0.0698 0.0429  1274 TRP B CD1 
3958 C CD2 . TRP B 237 ? 0.5937 0.5738 0.6839 -0.1220 -0.0511 0.0243  1274 TRP B CD2 
3959 N NE1 . TRP B 237 ? 0.6229 0.5836 0.7236 -0.1409 -0.0543 0.0474  1274 TRP B NE1 
3960 C CE2 . TRP B 237 ? 0.6103 0.5797 0.6806 -0.1255 -0.0438 0.0358  1274 TRP B CE2 
3961 C CE3 . TRP B 237 ? 0.5819 0.5703 0.6562 -0.1102 -0.0444 0.0104  1274 TRP B CE3 
3962 C CZ2 . TRP B 237 ? 0.6157 0.5844 0.6468 -0.1142 -0.0307 0.0348  1274 TRP B CZ2 
3963 C CZ3 . TRP B 237 ? 0.5854 0.5769 0.6261 -0.1013 -0.0336 0.0068  1274 TRP B CZ3 
3964 C CH2 . TRP B 237 ? 0.6024 0.5851 0.6195 -0.1017 -0.0271 0.0193  1274 TRP B CH2 
3965 N N   . GLU B 238 ? 0.5698 0.6132 0.7686 -0.1019 -0.0459 -0.0033 1275 GLU B N   
3966 C CA  . GLU B 238 ? 0.5715 0.6305 0.7599 -0.0880 -0.0297 -0.0214 1275 GLU B CA  
3967 C C   . GLU B 238 ? 0.5791 0.6753 0.7997 -0.0768 -0.0103 -0.0263 1275 GLU B C   
3968 O O   . GLU B 238 ? 0.5890 0.7038 0.7866 -0.0665 0.0088  -0.0326 1275 GLU B O   
3969 C CB  . GLU B 238 ? 0.5706 0.6122 0.7640 -0.0838 -0.0402 -0.0351 1275 GLU B CB  
3970 C CG  . GLU B 238 ? 0.5701 0.5824 0.7290 -0.0911 -0.0500 -0.0308 1275 GLU B CG  
3971 C CD  . GLU B 238 ? 0.5719 0.5675 0.7432 -0.0895 -0.0562 -0.0390 1275 GLU B CD  
3972 O OE1 . GLU B 238 ? 0.5687 0.5646 0.7289 -0.0884 -0.0520 -0.0509 1275 GLU B OE1 
3973 O OE2 . GLU B 238 ? 0.5780 0.5605 0.7740 -0.0896 -0.0662 -0.0321 1275 GLU B OE2 
3974 N N   . LEU B 239 ? 0.5795 0.6875 0.8515 -0.0761 -0.0152 -0.0226 1276 LEU B N   
3975 C CA  . LEU B 239 ? 0.5901 0.7371 0.9012 -0.0625 0.0057  -0.0267 1276 LEU B CA  
3976 C C   . LEU B 239 ? 0.6024 0.7758 0.9075 -0.0654 0.0299  -0.0105 1276 LEU B C   
3977 O O   . LEU B 239 ? 0.6234 0.8228 0.9160 -0.0487 0.0567  -0.0180 1276 LEU B O   
3978 C CB  . LEU B 239 ? 0.5863 0.7430 0.9611 -0.0637 -0.0078 -0.0193 1276 LEU B CB  
3979 C CG  . LEU B 239 ? 0.5891 0.7225 0.9764 -0.0546 -0.0260 -0.0327 1276 LEU B CG  
3980 C CD1 . LEU B 239 ? 0.5896 0.7344 1.0389 -0.0533 -0.0425 -0.0216 1276 LEU B CD1 
3981 C CD2 . LEU B 239 ? 0.6031 0.7423 0.9853 -0.0334 -0.0091 -0.0598 1276 LEU B CD2 
3982 N N   . MET B 240 ? 0.5990 0.7619 0.9099 -0.0857 0.0201  0.0117  1277 MET B N   
3983 C CA  . MET B 240 ? 0.6118 0.7953 0.9316 -0.0930 0.0419  0.0336  1277 MET B CA  
3984 C C   . MET B 240 ? 0.6269 0.8011 0.8794 -0.0854 0.0588  0.0340  1277 MET B C   
3985 O O   . MET B 240 ? 0.6481 0.8440 0.8971 -0.0820 0.0866  0.0507  1277 MET B O   
3986 C CB  . MET B 240 ? 0.6123 0.7774 0.9584 -0.1186 0.0202  0.0535  1277 MET B CB  
3987 C CG  . MET B 240 ? 0.6054 0.7908 1.0280 -0.1265 0.0035  0.0581  1277 MET B CG  
3988 S SD  . MET B 240 ? 0.6124 0.8657 1.1129 -0.1172 0.0405  0.0694  1277 MET B SD  
3989 C CE  . MET B 240 ? 0.6038 0.8695 1.1092 -0.0878 0.0417  0.0414  1277 MET B CE  
3990 N N   . THR B 241 ? 0.6189 0.7630 0.8212 -0.0818 0.0425  0.0181  1278 THR B N   
3991 C CA  . THR B 241 ? 0.6326 0.7688 0.7739 -0.0727 0.0516  0.0165  1278 THR B CA  
3992 C C   . THR B 241 ? 0.6417 0.7952 0.7568 -0.0493 0.0604  -0.0102 1278 THR B C   
3993 O O   . THR B 241 ? 0.6548 0.8050 0.7192 -0.0385 0.0621  -0.0170 1278 THR B O   
3994 C CB  . THR B 241 ? 0.6224 0.7191 0.7308 -0.0827 0.0282  0.0162  1278 THR B CB  
3995 O OG1 . THR B 241 ? 0.6017 0.6858 0.7197 -0.0828 0.0090  -0.0024 1278 THR B OG1 
3996 C CG2 . THR B 241 ? 0.6250 0.6973 0.7458 -0.1025 0.0177  0.0380  1278 THR B CG2 
3997 N N   . ARG B 242 ? 0.6397 0.8105 0.7908 -0.0401 0.0635  -0.0268 1279 ARG B N   
3998 C CA  . ARG B 242 ? 0.6568 0.8362 0.7890 -0.0184 0.0662  -0.0589 1279 ARG B CA  
3999 C C   . ARG B 242 ? 0.6426 0.7942 0.7467 -0.0219 0.0415  -0.0774 1279 ARG B C   
4000 O O   . ARG B 242 ? 0.6599 0.8155 0.7220 -0.0087 0.0409  -0.0946 1279 ARG B O   
4001 C CB  . ARG B 242 ? 0.7028 0.9110 0.7957 0.0040  0.0947  -0.0609 1279 ARG B CB  
4002 C CG  . ARG B 242 ? 0.7231 0.9668 0.8532 0.0132  0.1254  -0.0485 1279 ARG B CG  
4003 C CD  . ARG B 242 ? 0.7797 1.0513 0.8610 0.0422  0.1566  -0.0549 1279 ARG B CD  
4004 N NE  . ARG B 242 ? 0.8032 1.1133 0.9240 0.0561  0.1902  -0.0476 1279 ARG B NE  
4005 C CZ  . ARG B 242 ? 0.8004 1.1346 0.9694 0.0427  0.2130  -0.0105 1279 ARG B CZ  
4006 N NH1 . ARG B 242 ? 0.8154 1.1905 1.0307 0.0569  0.2440  -0.0060 1279 ARG B NH1 
4007 N NH2 . ARG B 242 ? 0.7841 1.1018 0.9597 0.0156  0.2047  0.0211  1279 ARG B NH2 
4008 N N   . GLY B 243 ? 0.6121 0.7379 0.7413 -0.0390 0.0209  -0.0723 1280 GLY B N   
4009 C CA  . GLY B 243 ? 0.6012 0.7040 0.7212 -0.0435 0.0015  -0.0873 1280 GLY B CA  
4010 C C   . GLY B 243 ? 0.5973 0.6927 0.6755 -0.0473 -0.0030 -0.0803 1280 GLY B C   
4011 O O   . GLY B 243 ? 0.6074 0.7039 0.6698 -0.0415 -0.0113 -0.0992 1280 GLY B O   
4012 N N   . ALA B 244 ? 0.5874 0.6746 0.6530 -0.0567 0.0002  -0.0542 1281 ALA B N   
4013 C CA  . ALA B 244 ? 0.5874 0.6621 0.6170 -0.0587 -0.0045 -0.0454 1281 ALA B CA  
4014 C C   . ALA B 244 ? 0.5692 0.6185 0.6068 -0.0700 -0.0199 -0.0445 1281 ALA B C   
4015 O O   . ALA B 244 ? 0.5598 0.5953 0.6232 -0.0792 -0.0264 -0.0399 1281 ALA B O   
4016 C CB  . ALA B 244 ? 0.5985 0.6675 0.6130 -0.0633 0.0051  -0.0193 1281 ALA B CB  
4017 N N   . PRO B 245 ? 0.5667 0.6115 0.5826 -0.0674 -0.0250 -0.0471 1282 PRO B N   
4018 C CA  . PRO B 245 ? 0.5569 0.5810 0.5779 -0.0757 -0.0330 -0.0427 1282 PRO B CA  
4019 C C   . PRO B 245 ? 0.5617 0.5577 0.5645 -0.0828 -0.0347 -0.0221 1282 PRO B C   
4020 O O   . PRO B 245 ? 0.5710 0.5603 0.5470 -0.0793 -0.0315 -0.0125 1282 PRO B O   
4021 C CB  . PRO B 245 ? 0.5602 0.5973 0.5683 -0.0677 -0.0349 -0.0511 1282 PRO B CB  
4022 C CG  . PRO B 245 ? 0.5760 0.6281 0.5537 -0.0551 -0.0300 -0.0496 1282 PRO B CG  
4023 C CD  . PRO B 245 ? 0.5809 0.6429 0.5666 -0.0539 -0.0226 -0.0528 1282 PRO B CD  
4024 N N   . PRO B 246 ? 0.5638 0.5391 0.5782 -0.0915 -0.0421 -0.0155 1283 PRO B N   
4025 C CA  . PRO B 246 ? 0.5820 0.5273 0.5747 -0.0970 -0.0495 -0.0013 1283 PRO B CA  
4026 C C   . PRO B 246 ? 0.5992 0.5275 0.5537 -0.0908 -0.0469 0.0027  1283 PRO B C   
4027 O O   . PRO B 246 ? 0.5932 0.5314 0.5447 -0.0841 -0.0407 -0.0022 1283 PRO B O   
4028 C CB  . PRO B 246 ? 0.5858 0.5142 0.5888 -0.1017 -0.0594 0.0020  1283 PRO B CB  
4029 C CG  . PRO B 246 ? 0.5692 0.5197 0.6134 -0.1014 -0.0570 -0.0077 1283 PRO B CG  
4030 C CD  . PRO B 246 ? 0.5576 0.5336 0.6039 -0.0948 -0.0462 -0.0218 1283 PRO B CD  
4031 N N   . TYR B 247 ? 0.6241 0.5272 0.5556 -0.0928 -0.0520 0.0112  1284 TYR B N   
4032 C CA  . TYR B 247 ? 0.6509 0.5311 0.5446 -0.0838 -0.0501 0.0140  1284 TYR B CA  
4033 C C   . TYR B 247 ? 0.6411 0.5477 0.5330 -0.0718 -0.0385 0.0107  1284 TYR B C   
4034 O O   . TYR B 247 ? 0.6408 0.5525 0.5235 -0.0617 -0.0335 0.0075  1284 TYR B O   
4035 C CB  . TYR B 247 ? 0.6717 0.5295 0.5419 -0.0795 -0.0527 0.0137  1284 TYR B CB  
4036 C CG  . TYR B 247 ? 0.6920 0.5245 0.5571 -0.0879 -0.0688 0.0163  1284 TYR B CG  
4037 C CD1 . TYR B 247 ? 0.7281 0.5244 0.5687 -0.0911 -0.0846 0.0168  1284 TYR B CD1 
4038 C CD2 . TYR B 247 ? 0.6825 0.5257 0.5695 -0.0923 -0.0715 0.0176  1284 TYR B CD2 
4039 C CE1 . TYR B 247 ? 0.7528 0.5283 0.5890 -0.0977 -0.1056 0.0169  1284 TYR B CE1 
4040 C CE2 . TYR B 247 ? 0.7057 0.5275 0.5867 -0.0970 -0.0898 0.0213  1284 TYR B CE2 
4041 C CZ  . TYR B 247 ? 0.7416 0.5317 0.5965 -0.0995 -0.1085 0.0201  1284 TYR B CZ  
4042 O OH  . TYR B 247 ? 0.7696 0.5407 0.6187 -0.1030 -0.1325 0.0216  1284 TYR B OH  
4043 N N   . PRO B 248 ? 0.6379 0.5646 0.5386 -0.0708 -0.0338 0.0124  1285 PRO B N   
4044 C CA  . PRO B 248 ? 0.6377 0.5924 0.5324 -0.0569 -0.0276 0.0077  1285 PRO B CA  
4045 C C   . PRO B 248 ? 0.6657 0.6048 0.5292 -0.0429 -0.0259 0.0163  1285 PRO B C   
4046 O O   . PRO B 248 ? 0.6678 0.6309 0.5257 -0.0283 -0.0247 0.0126  1285 PRO B O   
4047 C CB  . PRO B 248 ? 0.6356 0.6113 0.5394 -0.0580 -0.0217 0.0096  1285 PRO B CB  
4048 C CG  . PRO B 248 ? 0.6449 0.5960 0.5560 -0.0720 -0.0218 0.0239  1285 PRO B CG  
4049 C CD  . PRO B 248 ? 0.6402 0.5666 0.5572 -0.0816 -0.0338 0.0202  1285 PRO B CD  
4050 N N   . ASP B 249 ? 0.6934 0.5907 0.5376 -0.0460 -0.0286 0.0261  1286 ASP B N   
4051 C CA  . ASP B 249 ? 0.7266 0.5990 0.5413 -0.0309 -0.0275 0.0335  1286 ASP B CA  
4052 C C   . ASP B 249 ? 0.7386 0.5853 0.5370 -0.0249 -0.0295 0.0271  1286 ASP B C   
4053 O O   . ASP B 249 ? 0.7748 0.5856 0.5459 -0.0138 -0.0304 0.0308  1286 ASP B O   
4054 C CB  . ASP B 249 ? 0.7609 0.5989 0.5647 -0.0369 -0.0280 0.0496  1286 ASP B CB  
4055 C CG  . ASP B 249 ? 0.7715 0.5790 0.5870 -0.0579 -0.0373 0.0503  1286 ASP B CG  
4056 O OD1 . ASP B 249 ? 0.7519 0.5709 0.5829 -0.0672 -0.0429 0.0400  1286 ASP B OD1 
4057 O OD2 . ASP B 249 ? 0.8058 0.5769 0.6176 -0.0649 -0.0410 0.0617  1286 ASP B OD2 
4058 N N   . VAL B 250 ? 0.7162 0.5793 0.5293 -0.0302 -0.0285 0.0185  1287 VAL B N   
4059 C CA  . VAL B 250 ? 0.7363 0.5775 0.5292 -0.0235 -0.0259 0.0154  1287 VAL B CA  
4060 C C   . VAL B 250 ? 0.7123 0.5934 0.5315 -0.0201 -0.0154 0.0114  1287 VAL B C   
4061 O O   . VAL B 250 ? 0.6783 0.5884 0.5313 -0.0321 -0.0168 0.0080  1287 VAL B O   
4062 C CB  . VAL B 250 ? 0.7521 0.5576 0.5305 -0.0369 -0.0372 0.0148  1287 VAL B CB  
4063 C CG1 . VAL B 250 ? 0.7826 0.5647 0.5274 -0.0260 -0.0331 0.0119  1287 VAL B CG1 
4064 C CG2 . VAL B 250 ? 0.7785 0.5462 0.5447 -0.0447 -0.0504 0.0179  1287 VAL B CG2 
4065 N N   . ASN B 251 ? 0.7332 0.6144 0.5404 -0.0033 -0.0038 0.0119  1288 ASN B N   
4066 C CA  . ASN B 251 ? 0.7177 0.6363 0.5573 -0.0015 0.0095  0.0119  1288 ASN B CA  
4067 C C   . ASN B 251 ? 0.7220 0.6280 0.5611 -0.0150 0.0122  0.0163  1288 ASN B C   
4068 O O   . ASN B 251 ? 0.7492 0.6141 0.5497 -0.0174 0.0048  0.0181  1288 ASN B O   
4069 C CB  . ASN B 251 ? 0.7415 0.6656 0.5715 0.0216  0.0256  0.0144  1288 ASN B CB  
4070 C CG  . ASN B 251 ? 0.7336 0.6860 0.5813 0.0369  0.0225  0.0117  1288 ASN B CG  
4071 O OD1 . ASN B 251 ? 0.7009 0.7008 0.5946 0.0326  0.0184  0.0075  1288 ASN B OD1 
4072 N ND2 . ASN B 251 ? 0.7686 0.6898 0.5794 0.0563  0.0220  0.0131  1288 ASN B ND2 
4073 N N   . THR B 252 ? 0.7021 0.6425 0.5862 -0.0232 0.0210  0.0182  1289 THR B N   
4074 C CA  . THR B 252 ? 0.7080 0.6377 0.5980 -0.0357 0.0243  0.0263  1289 THR B CA  
4075 C C   . THR B 252 ? 0.7563 0.6585 0.6009 -0.0228 0.0402  0.0384  1289 THR B C   
4076 O O   . THR B 252 ? 0.7809 0.6556 0.6001 -0.0273 0.0373  0.0465  1289 THR B O   
4077 C CB  . THR B 252 ? 0.6791 0.6483 0.6346 -0.0482 0.0299  0.0258  1289 THR B CB  
4078 O OG1 . THR B 252 ? 0.6472 0.6414 0.6327 -0.0537 0.0144  0.0098  1289 THR B OG1 
4079 C CG2 . THR B 252 ? 0.6843 0.6379 0.6510 -0.0621 0.0305  0.0355  1289 THR B CG2 
4080 N N   . PHE B 253 ? 0.7780 0.6880 0.6094 -0.0033 0.0566  0.0392  1290 PHE B N   
4081 C CA  . PHE B 253 ? 0.8310 0.7208 0.6175 0.0144  0.0780  0.0496  1290 PHE B CA  
4082 C C   . PHE B 253 ? 0.8765 0.7138 0.5885 0.0309  0.0667  0.0400  1290 PHE B C   
4083 O O   . PHE B 253 ? 0.9290 0.7432 0.5899 0.0518  0.0825  0.0430  1290 PHE B O   
4084 C CB  . PHE B 253 ? 0.8327 0.7666 0.6572 0.0280  0.1064  0.0563  1290 PHE B CB  
4085 C CG  . PHE B 253 ? 0.8153 0.7743 0.6632 0.0394  0.1003  0.0442  1290 PHE B CG  
4086 C CD1 . PHE B 253 ? 0.8512 0.7799 0.6481 0.0635  0.0995  0.0369  1290 PHE B CD1 
4087 C CD2 . PHE B 253 ? 0.7691 0.7783 0.6878 0.0278  0.0925  0.0392  1290 PHE B CD2 
4088 C CE1 . PHE B 253 ? 0.8394 0.7882 0.6567 0.0765  0.0932  0.0294  1290 PHE B CE1 
4089 C CE2 . PHE B 253 ? 0.7578 0.7900 0.6922 0.0416  0.0838  0.0299  1290 PHE B CE2 
4090 C CZ  . PHE B 253 ? 0.7929 0.7951 0.6772 0.0663  0.0851  0.0273  1290 PHE B CZ  
4091 N N   . ASP B 254 ? 0.8609 0.6783 0.5676 0.0220  0.0401  0.0285  1291 ASP B N   
4092 C CA  . ASP B 254 ? 0.9060 0.6692 0.5535 0.0317  0.0240  0.0181  1291 ASP B CA  
4093 C C   . ASP B 254 ? 0.9034 0.6382 0.5405 0.0118  -0.0035 0.0153  1291 ASP B C   
4094 O O   . ASP B 254 ? 0.9289 0.6226 0.5359 0.0113  -0.0242 0.0055  1291 ASP B O   
4095 C CB  . ASP B 254 ? 0.9014 0.6628 0.5566 0.0400  0.0188  0.0106  1291 ASP B CB  
4096 C CG  . ASP B 254 ? 0.9186 0.6983 0.5740 0.0669  0.0418  0.0110  1291 ASP B CG  
4097 O OD1 . ASP B 254 ? 0.9452 0.7334 0.5869 0.0808  0.0646  0.0162  1291 ASP B OD1 
4098 O OD2 . ASP B 254 ? 0.9079 0.6947 0.5782 0.0754  0.0381  0.0084  1291 ASP B OD2 
4099 N N   . ILE B 255 ? 0.8737 0.6301 0.5412 -0.0042 -0.0046 0.0242  1292 ILE B N   
4100 C CA  . ILE B 255 ? 0.8689 0.6084 0.5394 -0.0215 -0.0304 0.0230  1292 ILE B CA  
4101 C C   . ILE B 255 ? 0.9334 0.6252 0.5377 -0.0118 -0.0440 0.0210  1292 ILE B C   
4102 O O   . ILE B 255 ? 0.9537 0.6164 0.5447 -0.0200 -0.0730 0.0124  1292 ILE B O   
4103 C CB  . ILE B 255 ? 0.8258 0.6003 0.5496 -0.0372 -0.0269 0.0323  1292 ILE B CB  
4104 C CG1 . ILE B 255 ? 0.7722 0.5906 0.5548 -0.0453 -0.0192 0.0284  1292 ILE B CG1 
4105 C CG2 . ILE B 255 ? 0.8277 0.5862 0.5555 -0.0504 -0.0526 0.0326  1292 ILE B CG2 
4106 C CD1 . ILE B 255 ? 0.7520 0.5714 0.5502 -0.0545 -0.0353 0.0202  1292 ILE B CD1 
4107 N N   . THR B 256 ? 0.9701 0.6560 0.5343 0.0062  -0.0231 0.0293  1293 THR B N   
4108 C CA  . THR B 256 ? 1.0427 0.6829 0.5298 0.0214  -0.0340 0.0271  1293 THR B CA  
4109 C C   . THR B 256 ? 1.0857 0.6792 0.5246 0.0315  -0.0551 0.0045  1293 THR B C   
4110 O O   . THR B 256 ? 1.1255 0.6802 0.5288 0.0286  -0.0884 -0.0066 1293 THR B O   
4111 C CB  . THR B 256 ? 1.0846 0.7305 0.5346 0.0430  0.0014  0.0429  1293 THR B CB  
4112 O OG1 . THR B 256 ? 1.0392 0.7255 0.5469 0.0289  0.0191  0.0646  1293 THR B OG1 
4113 C CG2 . THR B 256 ? 1.1758 0.7743 0.5331 0.0632  -0.0081 0.0422  1293 THR B CG2 
4114 N N   . VAL B 257 ? 1.0768 0.6738 0.5200 0.0432  -0.0381 -0.0024 1294 VAL B N   
4115 C CA  . VAL B 257 ? 1.1243 0.6721 0.5264 0.0546  -0.0549 -0.0234 1294 VAL B CA  
4116 C C   . VAL B 257 ? 1.0952 0.6304 0.5363 0.0280  -0.0889 -0.0307 1294 VAL B C   
4117 O O   . VAL B 257 ? 1.1471 0.6318 0.5547 0.0269  -0.1189 -0.0476 1294 VAL B O   
4118 C CB  . VAL B 257 ? 1.1231 0.6818 0.5304 0.0751  -0.0272 -0.0253 1294 VAL B CB  
4119 C CG1 . VAL B 257 ? 1.1783 0.6800 0.5497 0.0866  -0.0455 -0.0463 1294 VAL B CG1 
4120 C CG2 . VAL B 257 ? 1.1525 0.7291 0.5293 0.1023  0.0102  -0.0166 1294 VAL B CG2 
4121 N N   . TYR B 258 ? 1.0152 0.5972 0.5286 0.0071  -0.0833 -0.0183 1295 TYR B N   
4122 C CA  . TYR B 258 ? 0.9839 0.5655 0.5429 -0.0174 -0.1062 -0.0196 1295 TYR B CA  
4123 C C   . TYR B 258 ? 1.0086 0.5660 0.5589 -0.0312 -0.1403 -0.0255 1295 TYR B C   
4124 O O   . TYR B 258 ? 1.0358 0.5600 0.5894 -0.0424 -0.1676 -0.0361 1295 TYR B O   
4125 C CB  . TYR B 258 ? 0.9057 0.5460 0.5327 -0.0321 -0.0908 -0.0056 1295 TYR B CB  
4126 C CG  . TYR B 258 ? 0.8766 0.5248 0.5509 -0.0530 -0.1034 -0.0028 1295 TYR B CG  
4127 C CD1 . TYR B 258 ? 0.8845 0.5184 0.5627 -0.0510 -0.1004 -0.0023 1295 TYR B CD1 
4128 C CD2 . TYR B 258 ? 0.8447 0.5157 0.5616 -0.0727 -0.1155 0.0019  1295 TYR B CD2 
4129 C CE1 . TYR B 258 ? 0.8650 0.5073 0.5857 -0.0696 -0.1063 0.0056  1295 TYR B CE1 
4130 C CE2 . TYR B 258 ? 0.8213 0.5050 0.5845 -0.0902 -0.1210 0.0071  1295 TYR B CE2 
4131 C CZ  . TYR B 258 ? 0.8329 0.5025 0.5970 -0.0894 -0.1150 0.0104  1295 TYR B CZ  
4132 O OH  . TYR B 258 ? 0.8183 0.5012 0.6272 -0.1063 -0.1154 0.0207  1295 TYR B OH  
4133 N N   . LEU B 259 ? 1.0007 0.5751 0.5441 -0.0302 -0.1397 -0.0175 1296 LEU B N   
4134 C CA  . LEU B 259 ? 1.0204 0.5818 0.5625 -0.0411 -0.1734 -0.0200 1296 LEU B CA  
4135 C C   . LEU B 259 ? 1.1108 0.6138 0.5729 -0.0252 -0.1995 -0.0378 1296 LEU B C   
4136 O O   . LEU B 259 ? 1.1415 0.6211 0.6047 -0.0363 -0.2393 -0.0490 1296 LEU B O   
4137 C CB  . LEU B 259 ? 0.9922 0.5879 0.5512 -0.0415 -0.1620 -0.0025 1296 LEU B CB  
4138 C CG  . LEU B 259 ? 0.9105 0.5593 0.5484 -0.0574 -0.1437 0.0093  1296 LEU B CG  
4139 C CD1 . LEU B 259 ? 0.8963 0.5675 0.5475 -0.0560 -0.1337 0.0249  1296 LEU B CD1 
4140 C CD2 . LEU B 259 ? 0.8808 0.5416 0.5761 -0.0789 -0.1651 0.0055  1296 LEU B CD2 
4141 N N   . LEU B 260 ? 1.1565 0.6381 0.5512 0.0021  -0.1775 -0.0417 1297 LEU B N   
4142 C CA  . LEU B 260 ? 1.2550 0.6776 0.5605 0.0238  -0.1984 -0.0625 1297 LEU B CA  
4143 C C   . LEU B 260 ? 1.2900 0.6671 0.5984 0.0150  -0.2294 -0.0872 1297 LEU B C   
4144 O O   . LEU B 260 ? 1.3662 0.6948 0.6287 0.0181  -0.2692 -0.1091 1297 LEU B O   
4145 C CB  . LEU B 260 ? 1.2926 0.7089 0.5345 0.0572  -0.1587 -0.0600 1297 LEU B CB  
4146 C CG  . LEU B 260 ? 1.3106 0.7452 0.5139 0.0728  -0.1364 -0.0394 1297 LEU B CG  
4147 C CD1 . LEU B 260 ? 1.3473 0.7823 0.5003 0.1050  -0.0912 -0.0349 1297 LEU B CD1 
4148 C CD2 . LEU B 260 ? 1.3887 0.7847 0.5250 0.0802  -0.1751 -0.0475 1297 LEU B CD2 
4149 N N   . GLN B 261 ? 1.2419 0.6329 0.6044 0.0043  -0.2127 -0.0830 1298 GLN B N   
4150 C CA  . GLN B 261 ? 1.2764 0.6225 0.6498 -0.0051 -0.2360 -0.1004 1298 GLN B CA  
4151 C C   . GLN B 261 ? 1.2470 0.6035 0.6926 -0.0411 -0.2691 -0.0976 1298 GLN B C   
4152 O O   . GLN B 261 ? 1.2767 0.5974 0.7458 -0.0559 -0.2915 -0.1085 1298 GLN B O   
4153 C CB  . GLN B 261 ? 1.2454 0.6012 0.6423 0.0020  -0.2027 -0.0921 1298 GLN B CB  
4154 C CG  . GLN B 261 ? 1.2921 0.6290 0.6212 0.0401  -0.1751 -0.1002 1298 GLN B CG  
4155 C CD  . GLN B 261 ? 1.2568 0.6139 0.6165 0.0497  -0.1433 -0.0893 1298 GLN B CD  
4156 O OE1 . GLN B 261 ? 1.1953 0.5836 0.6204 0.0292  -0.1390 -0.0734 1298 GLN B OE1 
4157 N NE2 . GLN B 261 ? 1.3012 0.6425 0.6112 0.0843  -0.1201 -0.0972 1298 GLN B NE2 
4158 N N   . GLY B 262 ? 1.1931 0.5988 0.6792 -0.0548 -0.2705 -0.0816 1299 GLY B N   
4159 C CA  . GLY B 262 ? 1.1726 0.5939 0.7264 -0.0846 -0.3026 -0.0793 1299 GLY B CA  
4160 C C   . GLY B 262 ? 1.0944 0.5616 0.7367 -0.1074 -0.2808 -0.0591 1299 GLY B C   
4161 O O   . GLY B 262 ? 1.0779 0.5608 0.7869 -0.1327 -0.3008 -0.0550 1299 GLY B O   
4162 N N   . ARG B 263 ? 1.0513 0.5425 0.6940 -0.0966 -0.2398 -0.0465 1300 ARG B N   
4163 C CA  . ARG B 263 ? 0.9847 0.5194 0.6952 -0.1118 -0.2166 -0.0277 1300 ARG B CA  
4164 C C   . ARG B 263 ? 0.9208 0.5152 0.6705 -0.1167 -0.2039 -0.0145 1300 ARG B C   
4165 O O   . ARG B 263 ? 0.9078 0.5151 0.6268 -0.1013 -0.1916 -0.0135 1300 ARG B O   
4166 C CB  . ARG B 263 ? 0.9766 0.5095 0.6667 -0.0952 -0.1847 -0.0223 1300 ARG B CB  
4167 C CG  . ARG B 263 ? 1.0406 0.5122 0.7017 -0.0898 -0.1951 -0.0331 1300 ARG B CG  
4168 C CD  . ARG B 263 ? 1.0359 0.5079 0.6766 -0.0684 -0.1648 -0.0267 1300 ARG B CD  
4169 N NE  . ARG B 263 ? 1.0948 0.5077 0.7220 -0.0654 -0.1741 -0.0324 1300 ARG B NE  
4170 C CZ  . ARG B 263 ? 1.1562 0.5190 0.7252 -0.0398 -0.1751 -0.0493 1300 ARG B CZ  
4171 N NH1 . ARG B 263 ? 1.1672 0.5356 0.6842 -0.0149 -0.1650 -0.0606 1300 ARG B NH1 
4172 N NH2 . ARG B 263 ? 1.2112 0.5167 0.7753 -0.0382 -0.1843 -0.0536 1300 ARG B NH2 
4173 N N   . ARG B 264 ? 0.8854 0.5140 0.7054 -0.1376 -0.2053 -0.0038 1301 ARG B N   
4174 C CA  . ARG B 264 ? 0.8332 0.5157 0.6966 -0.1413 -0.1936 0.0062  1301 ARG B CA  
4175 C C   . ARG B 264 ? 0.7888 0.5108 0.6956 -0.1464 -0.1636 0.0193  1301 ARG B C   
4176 O O   . ARG B 264 ? 0.7992 0.5061 0.6990 -0.1465 -0.1526 0.0238  1301 ARG B O   
4177 C CB  . ARG B 264 ? 0.8399 0.5317 0.7470 -0.1565 -0.2248 0.0051  1301 ARG B CB  
4178 C CG  . ARG B 264 ? 0.8986 0.5500 0.7562 -0.1494 -0.2609 -0.0087 1301 ARG B CG  
4179 C CD  . ARG B 264 ? 0.9031 0.5524 0.7036 -0.1273 -0.2497 -0.0078 1301 ARG B CD  
4180 N NE  . ARG B 264 ? 0.9660 0.5799 0.7145 -0.1179 -0.2840 -0.0176 1301 ARG B NE  
4181 C CZ  . ARG B 264 ? 1.0278 0.5967 0.6924 -0.0988 -0.2874 -0.0284 1301 ARG B CZ  
4182 N NH1 . ARG B 264 ? 1.0312 0.5832 0.6634 -0.0889 -0.2614 -0.0322 1301 ARG B NH1 
4183 N NH2 . ARG B 264 ? 1.0912 0.6324 0.7018 -0.0865 -0.3170 -0.0353 1301 ARG B NH2 
4184 N N   . LEU B 265 ? 0.7469 0.5165 0.6938 -0.1479 -0.1511 0.0252  1302 LEU B N   
4185 C CA  . LEU B 265 ? 0.7130 0.5223 0.6946 -0.1494 -0.1238 0.0350  1302 LEU B CA  
4186 C C   . LEU B 265 ? 0.7256 0.5379 0.7533 -0.1674 -0.1259 0.0465  1302 LEU B C   
4187 O O   . LEU B 265 ? 0.7386 0.5453 0.8012 -0.1822 -0.1498 0.0459  1302 LEU B O   
4188 C CB  . LEU B 265 ? 0.6746 0.5273 0.6882 -0.1456 -0.1147 0.0339  1302 LEU B CB  
4189 C CG  . LEU B 265 ? 0.6651 0.5164 0.6469 -0.1316 -0.1106 0.0262  1302 LEU B CG  
4190 C CD1 . LEU B 265 ? 0.6341 0.5215 0.6550 -0.1293 -0.1033 0.0243  1302 LEU B CD1 
4191 C CD2 . LEU B 265 ? 0.6635 0.5119 0.6087 -0.1196 -0.0917 0.0241  1302 LEU B CD2 
4192 N N   . LEU B 266 ? 0.7254 0.5484 0.7555 -0.1656 -0.1009 0.0588  1303 LEU B N   
4193 C CA  . LEU B 266 ? 0.7445 0.5708 0.8190 -0.1825 -0.0947 0.0764  1303 LEU B CA  
4194 C C   . LEU B 266 ? 0.7161 0.5980 0.8534 -0.1890 -0.0812 0.0847  1303 LEU B C   
4195 O O   . LEU B 266 ? 0.6824 0.5960 0.8199 -0.1769 -0.0740 0.0756  1303 LEU B O   
4196 C CB  . LEU B 266 ? 0.7613 0.5771 0.8067 -0.1737 -0.0704 0.0906  1303 LEU B CB  
4197 C CG  . LEU B 266 ? 0.8007 0.5583 0.7950 -0.1671 -0.0825 0.0854  1303 LEU B CG  
4198 C CD1 . LEU B 266 ? 0.7875 0.5434 0.7267 -0.1437 -0.0809 0.0691  1303 LEU B CD1 
4199 C CD2 . LEU B 266 ? 0.8326 0.5724 0.8228 -0.1668 -0.0642 0.1078  1303 LEU B CD2 
4200 N N   . GLN B 267 ? 0.7345 0.6269 0.9292 -0.2079 -0.0768 0.1024  1304 GLN B N   
4201 C CA  . GLN B 267 ? 0.7153 0.6642 0.9776 -0.2131 -0.0599 0.1129  1304 GLN B CA  
4202 C C   . GLN B 267 ? 0.7094 0.6924 0.9529 -0.1958 -0.0179 0.1242  1304 GLN B C   
4203 O O   . GLN B 267 ? 0.7349 0.7030 0.9541 -0.1946 0.0008  0.1415  1304 GLN B O   
4204 C CB  . GLN B 267 ? 0.7383 0.6900 1.0760 -0.2406 -0.0677 0.1304  1304 GLN B CB  
4205 C CG  . GLN B 267 ? 0.7166 0.7321 1.1376 -0.2460 -0.0525 0.1409  1304 GLN B CG  
4206 C CD  . GLN B 267 ? 0.7394 0.7619 1.2497 -0.2763 -0.0666 0.1563  1304 GLN B CD  
4207 O OE1 . GLN B 267 ? 0.7749 0.7487 1.2842 -0.2952 -0.0917 0.1567  1304 GLN B OE1 
4208 N NE2 . GLN B 267 ? 0.7232 0.8069 1.3167 -0.2809 -0.0513 0.1678  1304 GLN B NE2 
4209 N N   . PRO B 268 ? 0.6860 0.7114 0.9351 -0.1796 -0.0038 0.1137  1305 PRO B N   
4210 C CA  . PRO B 268 ? 0.6912 0.7507 0.9208 -0.1610 0.0335  0.1204  1305 PRO B CA  
4211 C C   . PRO B 268 ? 0.7212 0.8074 0.9934 -0.1695 0.0647  0.1510  1305 PRO B C   
4212 O O   . PRO B 268 ? 0.7277 0.8172 1.0659 -0.1925 0.0575  0.1655  1305 PRO B O   
4213 C CB  . PRO B 268 ? 0.6618 0.7573 0.9077 -0.1460 0.0357  0.0998  1305 PRO B CB  
4214 C CG  . PRO B 268 ? 0.6432 0.7112 0.8892 -0.1523 -0.0016 0.0820  1305 PRO B CG  
4215 C CD  . PRO B 268 ? 0.6609 0.6983 0.9290 -0.1756 -0.0247 0.0938  1305 PRO B CD  
4216 N N   . GLU B 269 ? 0.7478 0.8543 0.9820 -0.1502 0.0992  0.1612  1306 GLU B N   
4217 C CA  . GLU B 269 ? 0.7897 0.9178 1.0477 -0.1541 0.1363  0.1964  1306 GLU B CA  
4218 C C   . GLU B 269 ? 0.7842 0.9650 1.1280 -0.1618 0.1535  0.2047  1306 GLU B C   
4219 O O   . GLU B 269 ? 0.8031 0.9915 1.2149 -0.1857 0.1611  0.2319  1306 GLU B O   
4220 C CB  . GLU B 269 ? 0.8198 0.9604 1.0049 -0.1246 0.1673  0.2019  1306 GLU B CB  
4221 C CG  . GLU B 269 ? 0.8714 1.0242 1.0619 -0.1256 0.2082  0.2450  1306 GLU B CG  
4222 C CD  . GLU B 269 ? 0.9128 1.0741 1.0178 -0.0927 0.2351  0.2516  1306 GLU B CD  
4223 O OE1 . GLU B 269 ? 0.9440 1.1482 1.0484 -0.0767 0.2754  0.2671  1306 GLU B OE1 
4224 O OE2 . GLU B 269 ? 0.9188 1.0459 0.9573 -0.0809 0.2153  0.2408  1306 GLU B OE2 
4225 N N   . TYR B 270 ? 0.7632 0.9801 1.1088 -0.1414 0.1589  0.1809  1307 TYR B N   
4226 C CA  . TYR B 270 ? 0.7555 1.0267 1.1816 -0.1416 0.1763  0.1851  1307 TYR B CA  
4227 C C   . TYR B 270 ? 0.7164 0.9837 1.1876 -0.1502 0.1351  0.1602  1307 TYR B C   
4228 O O   . TYR B 270 ? 0.6993 0.9900 1.1767 -0.1309 0.1351  0.1376  1307 TYR B O   
4229 C CB  . TYR B 270 ? 0.7731 1.0864 1.1676 -0.1074 0.2162  0.1775  1307 TYR B CB  
4230 C CG  . TYR B 270 ? 0.8236 1.1449 1.1699 -0.0953 0.2591  0.2062  1307 TYR B CG  
4231 C CD1 . TYR B 270 ? 0.8536 1.1958 1.2543 -0.1121 0.2913  0.2495  1307 TYR B CD1 
4232 C CD2 . TYR B 270 ? 0.8473 1.1552 1.0954 -0.0671 0.2664  0.1921  1307 TYR B CD2 
4233 C CE1 . TYR B 270 ? 0.9088 1.2556 1.2610 -0.0995 0.3335  0.2818  1307 TYR B CE1 
4234 C CE2 . TYR B 270 ? 0.9025 1.2163 1.0975 -0.0522 0.3036  0.2205  1307 TYR B CE2 
4235 C CZ  . TYR B 270 ? 0.9351 1.2669 1.1789 -0.0676 0.3392  0.2674  1307 TYR B CZ  
4236 O OH  . TYR B 270 ? 0.9989 1.3339 1.1862 -0.0515 0.3790  0.3012  1307 TYR B OH  
4237 N N   . CYS B 271 ? 0.7104 0.9440 1.2092 -0.1777 0.0990  0.1646  1308 CYS B N   
4238 C CA  . CYS B 271 ? 0.6861 0.9125 1.2237 -0.1866 0.0563  0.1460  1308 CYS B CA  
4239 C C   . CYS B 271 ? 0.6981 0.9366 1.3279 -0.2166 0.0399  0.1645  1308 CYS B C   
4240 O O   . CYS B 271 ? 0.7244 0.9276 1.3520 -0.2388 0.0287  0.1779  1308 CYS B O   
4241 C CB  . CYS B 271 ? 0.6791 0.8458 1.1448 -0.1869 0.0192  0.1255  1308 CYS B CB  
4242 S SG  . CYS B 271 ? 0.6665 0.8156 1.1650 -0.1971 -0.0350 0.1082  1308 CYS B SG  
4243 N N   . PRO B 272 ? 0.6857 0.9742 1.4043 -0.2179 0.0363  0.1651  1309 PRO B N   
4244 C CA  . PRO B 272 ? 0.6947 0.9991 1.5122 -0.2477 0.0120  0.1790  1309 PRO B CA  
4245 C C   . PRO B 272 ? 0.7035 0.9474 1.4971 -0.2673 -0.0460 0.1646  1309 PRO B C   
4246 O O   . PRO B 272 ? 0.6916 0.8974 1.4135 -0.2534 -0.0729 0.1409  1309 PRO B O   
4247 C CB  . PRO B 272 ? 0.6751 1.0389 1.5729 -0.2353 0.0087  0.1722  1309 PRO B CB  
4248 C CG  . PRO B 272 ? 0.6654 1.0570 1.5214 -0.2005 0.0548  0.1658  1309 PRO B CG  
4249 C CD  . PRO B 272 ? 0.6670 1.0000 1.4010 -0.1897 0.0543  0.1516  1309 PRO B CD  
4250 N N   . ASP B 273 ? 0.7274 0.9623 1.5825 -0.2994 -0.0639 0.1792  1310 ASP B N   
4251 C CA  . ASP B 273 ? 0.7500 0.9250 1.5834 -0.3179 -0.1204 0.1630  1310 ASP B CA  
4252 C C   . ASP B 273 ? 0.7389 0.9212 1.5894 -0.3107 -0.1694 0.1399  1310 ASP B C   
4253 O O   . ASP B 273 ? 0.7484 0.8770 1.5230 -0.3040 -0.2068 0.1181  1310 ASP B O   
4254 C CB  . ASP B 273 ? 0.7861 0.9515 1.6958 -0.3553 -0.1315 0.1815  1310 ASP B CB  
4255 C CG  . ASP B 273 ? 0.8076 0.9501 1.6901 -0.3627 -0.0879 0.2077  1310 ASP B CG  
4256 O OD1 . ASP B 273 ? 0.7940 0.9350 1.5981 -0.3368 -0.0489 0.2112  1310 ASP B OD1 
4257 O OD2 . ASP B 273 ? 0.8428 0.9673 1.7841 -0.3941 -0.0955 0.2246  1310 ASP B OD2 
4258 N N   . PRO B 274 ? 0.7224 0.9710 1.6708 -0.3092 -0.1700 0.1455  1311 PRO B N   
4259 C CA  . PRO B 274 ? 0.7166 0.9731 1.6787 -0.2973 -0.2163 0.1265  1311 PRO B CA  
4260 C C   . PRO B 274 ? 0.7016 0.9277 1.5607 -0.2652 -0.2157 0.1084  1311 PRO B C   
4261 O O   . PRO B 274 ? 0.7166 0.9103 1.5371 -0.2582 -0.2611 0.0922  1311 PRO B O   
4262 C CB  . PRO B 274 ? 0.6955 1.0377 1.7798 -0.2938 -0.1975 0.1406  1311 PRO B CB  
4263 C CG  . PRO B 274 ? 0.7052 1.0790 1.8641 -0.3193 -0.1594 0.1682  1311 PRO B CG  
4264 C CD  . PRO B 274 ? 0.7133 1.0337 1.7663 -0.3170 -0.1260 0.1725  1311 PRO B CD  
4265 N N   . LEU B 275 ? 0.6789 0.9150 1.4946 -0.2460 -0.1646 0.1120  1312 LEU B N   
4266 C CA  . LEU B 275 ? 0.6616 0.8728 1.3930 -0.2184 -0.1597 0.0959  1312 LEU B CA  
4267 C C   . LEU B 275 ? 0.6759 0.8165 1.3032 -0.2208 -0.1767 0.0853  1312 LEU B C   
4268 O O   . LEU B 275 ? 0.6778 0.7861 1.2477 -0.2073 -0.1995 0.0718  1312 LEU B O   
4269 C CB  . LEU B 275 ? 0.6408 0.8852 1.3633 -0.1987 -0.1036 0.0997  1312 LEU B CB  
4270 C CG  . LEU B 275 ? 0.6272 0.8539 1.2841 -0.1711 -0.0972 0.0815  1312 LEU B CG  
4271 C CD1 . LEU B 275 ? 0.6202 0.8709 1.3277 -0.1555 -0.1167 0.0746  1312 LEU B CD1 
4272 C CD2 . LEU B 275 ? 0.6191 0.8643 1.2456 -0.1545 -0.0469 0.0804  1312 LEU B CD2 
4273 N N   . TYR B 276 ? 0.6896 0.8069 1.2944 -0.2364 -0.1627 0.0936  1313 TYR B N   
4274 C CA  . TYR B 276 ? 0.7108 0.7635 1.2238 -0.2371 -0.1764 0.0839  1313 TYR B CA  
4275 C C   . TYR B 276 ? 0.7467 0.7601 1.2499 -0.2474 -0.2320 0.0713  1313 TYR B C   
4276 O O   . TYR B 276 ? 0.7615 0.7261 1.1817 -0.2370 -0.2493 0.0577  1313 TYR B O   
4277 C CB  . TYR B 276 ? 0.7260 0.7623 1.2257 -0.2496 -0.1498 0.0979  1313 TYR B CB  
4278 C CG  . TYR B 276 ? 0.7494 0.7206 1.1589 -0.2469 -0.1610 0.0880  1313 TYR B CG  
4279 C CD1 . TYR B 276 ? 0.7346 0.6879 1.0649 -0.2242 -0.1511 0.0761  1313 TYR B CD1 
4280 C CD2 . TYR B 276 ? 0.7896 0.7172 1.1983 -0.2664 -0.1817 0.0896  1313 TYR B CD2 
4281 C CE1 . TYR B 276 ? 0.7561 0.6562 1.0101 -0.2190 -0.1583 0.0679  1313 TYR B CE1 
4282 C CE2 . TYR B 276 ? 0.8163 0.6836 1.1424 -0.2596 -0.1904 0.0788  1313 TYR B CE2 
4283 C CZ  . TYR B 276 ? 0.7976 0.6543 1.0466 -0.2347 -0.1772 0.0687  1313 TYR B CZ  
4284 O OH  . TYR B 276 ? 0.8248 0.6281 0.9983 -0.2255 -0.1826 0.0590  1313 TYR B OH  
4285 N N   . GLU B 277 ? 0.7648 0.8016 1.3536 -0.2667 -0.2598 0.0754  1314 GLU B N   
4286 C CA  . GLU B 277 ? 0.8090 0.8126 1.3931 -0.2755 -0.3193 0.0604  1314 GLU B CA  
4287 C C   . GLU B 277 ? 0.8089 0.8052 1.3447 -0.2505 -0.3420 0.0488  1314 GLU B C   
4288 O O   . GLU B 277 ? 0.8492 0.7950 1.3135 -0.2443 -0.3777 0.0342  1314 GLU B O   
4289 C CB  . GLU B 277 ? 0.8230 0.8663 1.5259 -0.3007 -0.3454 0.0673  1314 GLU B CB  
4290 C CG  . GLU B 277 ? 0.8808 0.8842 1.5807 -0.3144 -0.4127 0.0484  1314 GLU B CG  
4291 C CD  . GLU B 277 ? 0.9282 0.8680 1.5892 -0.3337 -0.4252 0.0400  1314 GLU B CD  
4292 O OE1 . GLU B 277 ? 0.9605 0.9018 1.7008 -0.3633 -0.4529 0.0402  1314 GLU B OE1 
4293 O OE2 . GLU B 277 ? 0.9348 0.8233 1.4918 -0.3191 -0.4081 0.0331  1314 GLU B OE2 
4294 N N   . VAL B 278 ? 0.7705 0.8147 1.3432 -0.2344 -0.3190 0.0562  1315 VAL B N   
4295 C CA  . VAL B 278 ? 0.7722 0.8098 1.3080 -0.2102 -0.3349 0.0504  1315 VAL B CA  
4296 C C   . VAL B 278 ? 0.7741 0.7615 1.1987 -0.1950 -0.3181 0.0441  1315 VAL B C   
4297 O O   . VAL B 278 ? 0.8029 0.7555 1.1665 -0.1815 -0.3437 0.0386  1315 VAL B O   
4298 C CB  . VAL B 278 ? 0.7362 0.8324 1.3414 -0.1955 -0.3098 0.0586  1315 VAL B CB  
4299 C CG1 . VAL B 278 ? 0.7412 0.8216 1.3038 -0.1695 -0.3199 0.0553  1315 VAL B CG1 
4300 C CG2 . VAL B 278 ? 0.7353 0.8883 1.4593 -0.2075 -0.3274 0.0661  1315 VAL B CG2 
4301 N N   . MET B 279 ? 0.7471 0.7339 1.1476 -0.1961 -0.2745 0.0469  1316 MET B N   
4302 C CA  . MET B 279 ? 0.7457 0.6940 1.0553 -0.1832 -0.2559 0.0415  1316 MET B CA  
4303 C C   . MET B 279 ? 0.7957 0.6865 1.0338 -0.1858 -0.2860 0.0325  1316 MET B C   
4304 O O   . MET B 279 ? 0.8136 0.6723 0.9802 -0.1704 -0.2891 0.0284  1316 MET B O   
4305 C CB  . MET B 279 ? 0.7167 0.6767 1.0190 -0.1850 -0.2113 0.0456  1316 MET B CB  
4306 C CG  . MET B 279 ? 0.6763 0.6818 1.0142 -0.1731 -0.1769 0.0484  1316 MET B CG  
4307 S SD  . MET B 279 ? 0.6562 0.6739 0.9729 -0.1718 -0.1298 0.0526  1316 MET B SD  
4308 C CE  . MET B 279 ? 0.6315 0.7145 1.0248 -0.1644 -0.1000 0.0579  1316 MET B CE  
4309 N N   . LEU B 280 ? 0.8242 0.7012 1.0838 -0.2049 -0.3067 0.0296  1317 LEU B N   
4310 C CA  . LEU B 280 ? 0.8820 0.6998 1.0742 -0.2065 -0.3365 0.0162  1317 LEU B CA  
4311 C C   . LEU B 280 ? 0.9283 0.7260 1.0892 -0.1958 -0.3827 0.0070  1317 LEU B C   
4312 O O   . LEU B 280 ? 0.9743 0.7224 1.0470 -0.1828 -0.3972 -0.0036 1317 LEU B O   
4313 C CB  . LEU B 280 ? 0.9053 0.7125 1.1429 -0.2319 -0.3501 0.0145  1317 LEU B CB  
4314 C CG  . LEU B 280 ? 0.8810 0.6927 1.1287 -0.2399 -0.3064 0.0264  1317 LEU B CG  
4315 C CD1 . LEU B 280 ? 0.9176 0.7077 1.2090 -0.2662 -0.3232 0.0273  1317 LEU B CD1 
4316 C CD2 . LEU B 280 ? 0.8829 0.6589 1.0373 -0.2205 -0.2819 0.0217  1317 LEU B CD2 
4317 N N   . LYS B 281 ? 0.9215 0.7587 1.1527 -0.1984 -0.4051 0.0121  1318 LYS B N   
4318 C CA  . LYS B 281 ? 0.9690 0.7920 1.1735 -0.1850 -0.4511 0.0069  1318 LYS B CA  
4319 C C   . LYS B 281 ? 0.9707 0.7760 1.0985 -0.1584 -0.4314 0.0140  1318 LYS B C   
4320 O O   . LYS B 281 ? 1.0300 0.7955 1.0801 -0.1426 -0.4580 0.0096  1318 LYS B O   
4321 C CB  . LYS B 281 ? 0.9545 0.8316 1.2630 -0.1911 -0.4757 0.0135  1318 LYS B CB  
4322 C CG  . LYS B 281 ? 0.9649 0.8629 1.3620 -0.2196 -0.5026 0.0082  1318 LYS B CG  
4323 C CD  . LYS B 281 ? 0.9448 0.9076 1.4580 -0.2243 -0.5208 0.0171  1318 LYS B CD  
4324 C CE  . LYS B 281 ? 0.9456 0.9400 1.5664 -0.2566 -0.5348 0.0173  1318 LYS B CE  
4325 N NZ  . LYS B 281 ? 1.0156 0.9599 1.6078 -0.2723 -0.5903 -0.0033 1318 LYS B NZ  
4326 N N   . CYS B 282 ? 0.9124 0.7467 1.0628 -0.1534 -0.3846 0.0254  1319 CYS B N   
4327 C CA  . CYS B 282 ? 0.9085 0.7285 1.0029 -0.1329 -0.3617 0.0337  1319 CYS B CA  
4328 C C   . CYS B 282 ? 0.9414 0.7139 0.9393 -0.1259 -0.3482 0.0285  1319 CYS B C   
4329 O O   . CYS B 282 ? 0.9706 0.7165 0.9034 -0.1082 -0.3467 0.0350  1319 CYS B O   
4330 C CB  . CYS B 282 ? 0.8432 0.7020 0.9875 -0.1316 -0.3179 0.0409  1319 CYS B CB  
4331 S SG  . CYS B 282 ? 0.8089 0.7239 1.0616 -0.1306 -0.3264 0.0473  1319 CYS B SG  
4332 N N   . TRP B 283 ? 0.9394 0.7021 0.9312 -0.1383 -0.3364 0.0190  1320 TRP B N   
4333 C CA  . TRP B 283 ? 0.9704 0.6920 0.8795 -0.1297 -0.3210 0.0127  1320 TRP B CA  
4334 C C   . TRP B 283 ? 1.0483 0.7220 0.9020 -0.1282 -0.3614 -0.0029 1320 TRP B C   
4335 O O   . TRP B 283 ? 1.0672 0.7141 0.8991 -0.1341 -0.3594 -0.0147 1320 TRP B O   
4336 C CB  . TRP B 283 ? 0.9289 0.6631 0.8575 -0.1390 -0.2845 0.0120  1320 TRP B CB  
4337 C CG  . TRP B 283 ? 0.8658 0.6452 0.8435 -0.1393 -0.2487 0.0219  1320 TRP B CG  
4338 C CD1 . TRP B 283 ? 0.8469 0.6405 0.8236 -0.1276 -0.2328 0.0294  1320 TRP B CD1 
4339 C CD2 . TRP B 283 ? 0.8231 0.6352 0.8535 -0.1506 -0.2242 0.0244  1320 TRP B CD2 
4340 N NE1 . TRP B 283 ? 0.7963 0.6281 0.8219 -0.1308 -0.2040 0.0313  1320 TRP B NE1 
4341 C CE2 . TRP B 283 ? 0.7822 0.6277 0.8366 -0.1431 -0.1972 0.0288  1320 TRP B CE2 
4342 C CE3 . TRP B 283 ? 0.8230 0.6370 0.8811 -0.1656 -0.2222 0.0245  1320 TRP B CE3 
4343 C CZ2 . TRP B 283 ? 0.7441 0.6256 0.8397 -0.1469 -0.1696 0.0306  1320 TRP B CZ2 
4344 C CZ3 . TRP B 283 ? 0.7848 0.6358 0.8854 -0.1701 -0.1912 0.0320  1320 TRP B CZ3 
4345 C CH2 . TRP B 283 ? 0.7468 0.6318 0.8615 -0.1593 -0.1658 0.0336  1320 TRP B CH2 
4346 N N   . HIS B 284 ? 1.1032 0.7628 0.9306 -0.1181 -0.4000 -0.0041 1321 HIS B N   
4347 C CA  . HIS B 284 ? 1.1911 0.8018 0.9534 -0.1121 -0.4438 -0.0231 1321 HIS B CA  
4348 C C   . HIS B 284 ? 1.2482 0.8177 0.8961 -0.0838 -0.4298 -0.0217 1321 HIS B C   
4349 O O   . HIS B 284 ? 1.2416 0.8221 0.8697 -0.0687 -0.4117 -0.0021 1321 HIS B O   
4350 C CB  . HIS B 284 ? 1.2253 0.8467 1.0239 -0.1155 -0.4993 -0.0265 1321 HIS B CB  
4351 C CG  . HIS B 284 ? 1.3120 0.8890 1.0684 -0.1168 -0.5547 -0.0527 1321 HIS B CG  
4352 N ND1 . HIS B 284 ? 1.4026 0.9246 1.0405 -0.0917 -0.5738 -0.0656 1321 HIS B ND1 
4353 C CD2 . HIS B 284 ? 1.3258 0.9061 1.1489 -0.1409 -0.5963 -0.0696 1321 HIS B CD2 
4354 C CE1 . HIS B 284 ? 1.4716 0.9602 1.0973 -0.0988 -0.6287 -0.0938 1321 HIS B CE1 
4355 N NE2 . HIS B 284 ? 1.4245 0.9487 1.1699 -0.1315 -0.6447 -0.0963 1321 HIS B NE2 
4356 N N   . PRO B 285 ? 1.3116 0.8322 0.8834 -0.0747 -0.4347 -0.0410 1322 PRO B N   
4357 C CA  . PRO B 285 ? 1.3688 0.8550 0.8329 -0.0452 -0.4127 -0.0385 1322 PRO B CA  
4358 C C   . PRO B 285 ? 1.4365 0.9083 0.8363 -0.0226 -0.4363 -0.0283 1322 PRO B C   
4359 O O   . PRO B 285 ? 1.4411 0.9146 0.7966 -0.0039 -0.4019 -0.0062 1322 PRO B O   
4360 C CB  . PRO B 285 ? 1.4358 0.8687 0.8377 -0.0391 -0.4273 -0.0678 1322 PRO B CB  
4361 C CG  . PRO B 285 ? 1.4368 0.8671 0.9067 -0.0662 -0.4747 -0.0869 1322 PRO B CG  
4362 C CD  . PRO B 285 ? 1.3361 0.8302 0.9236 -0.0911 -0.4594 -0.0656 1322 PRO B CD  
4363 N N   . LYS B 286 ? 1.4950 0.9527 0.8925 -0.0245 -0.4961 -0.0430 1323 LYS B N   
4364 C CA  . LYS B 286 ? 1.5659 1.0127 0.9082 -0.0025 -0.5270 -0.0320 1323 LYS B CA  
4365 C C   . LYS B 286 ? 1.5004 0.9984 0.9300 -0.0112 -0.5188 -0.0033 1323 LYS B C   
4366 O O   . LYS B 286 ? 1.4280 0.9671 0.9669 -0.0368 -0.5220 -0.0048 1323 LYS B O   
4367 C CB  . LYS B 286 ? 1.6527 1.0679 0.9653 -0.0009 -0.6000 -0.0619 1323 LYS B CB  
4368 C CG  . LYS B 286 ? 1.7372 1.0925 0.9572 0.0107  -0.6133 -0.0959 1323 LYS B CG  
4369 C CD  . LYS B 286 ? 1.8326 1.1525 1.0222 0.0121  -0.6917 -0.1302 1323 LYS B CD  
4370 C CE  . LYS B 286 ? 1.9238 1.1770 1.0184 0.0258  -0.7048 -0.1684 1323 LYS B CE  
4371 N NZ  . LYS B 286 ? 2.0269 1.2421 1.0923 0.0265  -0.7876 -0.2066 1323 LYS B NZ  
4372 N N   . ALA B 287 ? 1.5358 1.0284 0.9147 0.0121  -0.5066 0.0238  1324 ALA B N   
4373 C CA  . ALA B 287 ? 1.4776 1.0095 0.9295 0.0084  -0.4879 0.0533  1324 ALA B CA  
4374 C C   . ALA B 287 ? 1.4843 1.0390 0.9997 0.0040  -0.5433 0.0520  1324 ALA B C   
4375 O O   . ALA B 287 ? 1.4047 1.0050 1.0288 -0.0131 -0.5365 0.0580  1324 ALA B O   
4376 C CB  . ALA B 287 ? 1.5218 1.0334 0.8992 0.0341  -0.4561 0.0851  1324 ALA B CB  
4377 N N   . GLU B 288 ? 1.5839 1.1082 1.0299 0.0221  -0.5986 0.0432  1325 GLU B N   
4378 C CA  . GLU B 288 ? 1.6052 1.1508 1.1026 0.0241  -0.6568 0.0445  1325 GLU B CA  
4379 C C   . GLU B 288 ? 1.5445 1.1304 1.1621 -0.0082 -0.6842 0.0204  1325 GLU B C   
4380 O O   . GLU B 288 ? 1.5273 1.1530 1.2332 -0.0133 -0.7155 0.0260  1325 GLU B O   
4381 C CB  . GLU B 288 ? 1.7352 1.2364 1.1197 0.0530  -0.7141 0.0372  1325 GLU B CB  
4382 C CG  . GLU B 288 ? 1.8011 1.2633 1.1215 0.0499  -0.7484 -0.0037 1325 GLU B CG  
4383 C CD  . GLU B 288 ? 1.8385 1.2550 1.0481 0.0636  -0.7025 -0.0094 1325 GLU B CD  
4384 O OE1 . GLU B 288 ? 1.8952 1.2748 1.0520 0.0632  -0.7278 -0.0451 1325 GLU B OE1 
4385 O OE2 . GLU B 288 ? 1.8139 1.2316 0.9950 0.0750  -0.6421 0.0211  1325 GLU B OE2 
4386 N N   . MET B 289 ? 1.5170 1.0930 1.1412 -0.0290 -0.6705 -0.0036 1326 MET B N   
4387 C CA  . MET B 289 ? 1.4687 1.0763 1.2014 -0.0612 -0.6936 -0.0236 1326 MET B CA  
4388 C C   . MET B 289 ? 1.3526 1.0205 1.2062 -0.0806 -0.6490 -0.0059 1326 MET B C   
4389 O O   . MET B 289 ? 1.3117 1.0200 1.2728 -0.1046 -0.6648 -0.0129 1326 MET B O   
4390 C CB  . MET B 289 ? 1.4877 1.0577 1.1842 -0.0753 -0.6892 -0.0512 1326 MET B CB  
4391 C CG  . MET B 289 ? 1.6045 1.1190 1.2107 -0.0630 -0.7500 -0.0813 1326 MET B CG  
4392 S SD  . MET B 289 ? 1.6426 1.1809 1.3369 -0.0802 -0.8392 -0.1016 1326 MET B SD  
4393 C CE  . MET B 289 ? 1.7242 1.2539 1.3345 -0.0392 -0.8796 -0.0858 1326 MET B CE  
4394 N N   . ARG B 290 ? 1.3041 0.9779 1.1408 -0.0699 -0.5932 0.0162  1327 ARG B N   
4395 C CA  . ARG B 290 ? 1.2077 0.9326 1.1432 -0.0832 -0.5500 0.0293  1327 ARG B CA  
4396 C C   . ARG B 290 ? 1.1969 0.9646 1.2161 -0.0781 -0.5757 0.0417  1327 ARG B C   
4397 O O   . ARG B 290 ? 1.2572 1.0092 1.2377 -0.0570 -0.6124 0.0502  1327 ARG B O   
4398 C CB  . ARG B 290 ? 1.1733 0.8876 1.0648 -0.0721 -0.4915 0.0458  1327 ARG B CB  
4399 C CG  . ARG B 290 ? 1.1759 0.8570 0.9971 -0.0749 -0.4610 0.0354  1327 ARG B CG  
4400 C CD  . ARG B 290 ? 1.1643 0.8321 0.9333 -0.0601 -0.4134 0.0532  1327 ARG B CD  
4401 N NE  . ARG B 290 ? 1.1850 0.8197 0.8779 -0.0563 -0.3907 0.0439  1327 ARG B NE  
4402 C CZ  . ARG B 290 ? 1.1951 0.8135 0.8306 -0.0422 -0.3526 0.0575  1327 ARG B CZ  
4403 N NH1 . ARG B 290 ? 1.1855 0.8126 0.8300 -0.0331 -0.3337 0.0819  1327 ARG B NH1 
4404 N NH2 . ARG B 290 ? 1.2176 0.8110 0.7922 -0.0371 -0.3330 0.0474  1327 ARG B NH2 
4405 N N   . PRO B 291 ? 1.1277 0.9508 1.2612 -0.0940 -0.5557 0.0442  1328 PRO B N   
4406 C CA  . PRO B 291 ? 1.1192 0.9885 1.3434 -0.0872 -0.5778 0.0543  1328 PRO B CA  
4407 C C   . PRO B 291 ? 1.1161 0.9845 1.3313 -0.0632 -0.5526 0.0758  1328 PRO B C   
4408 O O   . PRO B 291 ? 1.0966 0.9420 1.2623 -0.0590 -0.5072 0.0825  1328 PRO B O   
4409 C CB  . PRO B 291 ? 1.0458 0.9716 1.3848 -0.1114 -0.5528 0.0492  1328 PRO B CB  
4410 C CG  . PRO B 291 ? 1.0040 0.9125 1.3014 -0.1209 -0.4969 0.0464  1328 PRO B CG  
4411 C CD  . PRO B 291 ? 1.0604 0.9051 1.2384 -0.1156 -0.5097 0.0385  1328 PRO B CD  
4412 N N   . SER B 292 ? 1.1421 1.0357 1.4120 -0.0478 -0.5844 0.0864  1329 SER B N   
4413 C CA  . SER B 292 ? 1.1460 1.0379 1.4236 -0.0245 -0.5652 0.1072  1329 SER B CA  
4414 C C   . SER B 292 ? 1.0794 1.0189 1.4545 -0.0315 -0.5198 0.1049  1329 SER B C   
4415 O O   . SER B 292 ? 1.0366 1.0202 1.4852 -0.0508 -0.5127 0.0920  1329 SER B O   
4416 C CB  . SER B 292 ? 1.2009 1.0967 1.4935 -0.0012 -0.6193 0.1201  1329 SER B CB  
4417 O OG  . SER B 292 ? 1.1779 1.1324 1.5812 -0.0104 -0.6523 0.1098  1329 SER B OG  
4418 N N   . PHE B 293 ? 0.8590 0.9872 0.9937 -0.0545 -0.0307 0.0432  1330 PHE B N   
4419 C CA  . PHE B 293 ? 0.8107 0.9698 1.0071 -0.0371 -0.0528 0.0472  1330 PHE B CA  
4420 C C   . PHE B 293 ? 0.8114 0.9848 1.0134 -0.0481 -0.0770 0.0475  1330 PHE B C   
4421 O O   . PHE B 293 ? 0.7876 0.9627 1.0130 -0.0365 -0.0822 0.0422  1330 PHE B O   
4422 C CB  . PHE B 293 ? 0.7797 0.9659 1.0234 -0.0283 -0.0631 0.0650  1330 PHE B CB  
4423 C CG  . PHE B 293 ? 0.7762 0.9708 1.0485 -0.0138 -0.0463 0.0819  1330 PHE B CG  
4424 C CD1 . PHE B 293 ? 0.7601 0.9628 1.0582 -0.0076 -0.0498 0.0885  1330 PHE B CD1 
4425 C CD2 . PHE B 293 ? 0.7921 0.9952 1.0727 -0.0082 -0.0263 0.1018  1330 PHE B CD2 
4426 C CE1 . PHE B 293 ? 0.7585 0.9892 1.1037 0.0022  -0.0381 0.1247  1330 PHE B CE1 
4427 C CE2 . PHE B 293 ? 0.7902 1.0158 1.1193 0.0085  -0.0071 0.1351  1330 PHE B CE2 
4428 C CZ  . PHE B 293 ? 0.7717 1.0168 1.1396 0.0130  -0.0151 0.1515  1330 PHE B CZ  
4429 N N   . SER B 294 ? 0.8547 1.0423 1.0377 -0.0730 -0.0900 0.0620  1331 SER B N   
4430 C CA  . SER B 294 ? 0.8605 1.0781 1.0674 -0.0841 -0.1102 0.0828  1331 SER B CA  
4431 C C   . SER B 294 ? 0.8937 1.0933 1.0715 -0.0923 -0.1095 0.0693  1331 SER B C   
4432 O O   . SER B 294 ? 0.8704 1.0908 1.0881 -0.0811 -0.1151 0.0809  1331 SER B O   
4433 C CB  . SER B 294 ? 0.8845 1.1367 1.0823 -0.1202 -0.1312 0.1177  1331 SER B CB  
4434 O OG  . SER B 294 ? 0.8672 1.1683 1.1154 -0.1286 -0.1506 0.1588  1331 SER B OG  
4435 N N   . GLU B 295 ? 0.9653 1.1177 1.0716 -0.1104 -0.0948 0.0465  1332 GLU B N   
4436 C CA  . GLU B 295 ? 1.0068 1.1288 1.0753 -0.1232 -0.0911 0.0326  1332 GLU B CA  
4437 C C   . GLU B 295 ? 0.9668 1.0874 1.0802 -0.0834 -0.0777 0.0186  1332 GLU B C   
4438 O O   . GLU B 295 ? 0.9554 1.0816 1.0770 -0.0842 -0.0849 0.0191  1332 GLU B O   
4439 C CB  . GLU B 295 ? 1.1060 1.1508 1.0731 -0.1527 -0.0640 0.0094  1332 GLU B CB  
4440 C CG  . GLU B 295 ? 1.1630 1.1597 1.0742 -0.1777 -0.0598 -0.0042 1332 GLU B CG  
4441 C CD  . GLU B 295 ? 1.2960 1.1822 1.0850 -0.2099 -0.0180 -0.0328 1332 GLU B CD  
4442 O OE1 . GLU B 295 ? 1.3469 1.1950 1.0942 -0.2092 0.0130  -0.0412 1332 GLU B OE1 
4443 O OE2 . GLU B 295 ? 1.3608 1.1893 1.0907 -0.2362 -0.0105 -0.0464 1332 GLU B OE2 
4444 N N   . LEU B 296 ? 0.9549 1.0742 1.0968 -0.0554 -0.0619 0.0134  1333 LEU B N   
4445 C CA  . LEU B 296 ? 0.9363 1.0601 1.1130 -0.0315 -0.0556 0.0100  1333 LEU B CA  
4446 C C   . LEU B 296 ? 0.9117 1.0606 1.1200 -0.0253 -0.0740 0.0135  1333 LEU B C   
4447 O O   . LEU B 296 ? 0.9016 1.0501 1.1172 -0.0186 -0.0736 0.0092  1333 LEU B O   
4448 C CB  . LEU B 296 ? 0.9309 1.0608 1.1346 -0.0157 -0.0422 0.0207  1333 LEU B CB  
4449 C CG  . LEU B 296 ? 0.9789 1.0743 1.1596 -0.0097 -0.0032 0.0234  1333 LEU B CG  
4450 C CD1 . LEU B 296 ? 0.9613 1.0844 1.1988 0.0112  0.0106  0.0534  1333 LEU B CD1 
4451 C CD2 . LEU B 296 ? 1.0256 1.0737 1.1735 -0.0091 0.0244  0.0121  1333 LEU B CD2 
4452 N N   . VAL B 297 ? 0.9181 1.0826 1.1432 -0.0272 -0.0831 0.0245  1334 VAL B N   
4453 C CA  . VAL B 297 ? 0.9238 1.0905 1.1737 -0.0160 -0.0809 0.0297  1334 VAL B CA  
4454 C C   . VAL B 297 ? 0.9364 1.1157 1.1929 -0.0159 -0.0804 0.0381  1334 VAL B C   
4455 O O   . VAL B 297 ? 0.9382 1.1048 1.1957 -0.0046 -0.0692 0.0313  1334 VAL B O   
4456 C CB  . VAL B 297 ? 0.9230 1.0988 1.2026 -0.0120 -0.0791 0.0496  1334 VAL B CB  
4457 C CG1 . VAL B 297 ? 0.9410 1.1026 1.2479 0.0063  -0.0571 0.0610  1334 VAL B CG1 
4458 C CG2 . VAL B 297 ? 0.9234 1.0854 1.1978 -0.0140 -0.0811 0.0430  1334 VAL B CG2 
4459 N N   . SER B 298 ? 0.9556 1.1581 1.2082 -0.0360 -0.0941 0.0561  1335 SER B N   
4460 C CA  . SER B 298 ? 0.9638 1.1911 1.2305 -0.0449 -0.1013 0.0777  1335 SER B CA  
4461 C C   . SER B 298 ? 0.9720 1.1748 1.2085 -0.0453 -0.0977 0.0532  1335 SER B C   
4462 O O   . SER B 298 ? 0.9587 1.1748 1.2164 -0.0358 -0.0935 0.0627  1335 SER B O   
4463 C CB  . SER B 298 ? 0.9888 1.2468 1.2450 -0.0851 -0.1272 0.1100  1335 SER B CB  
4464 O OG  . SER B 298 ? 1.0286 1.2424 1.2068 -0.1151 -0.1310 0.0820  1335 SER B OG  
4465 N N   . ARG B 299 ? 0.9971 1.1641 1.1907 -0.0531 -0.0930 0.0281  1336 ARG B N   
4466 C CA  . ARG B 299 ? 1.0138 1.1558 1.1881 -0.0519 -0.0841 0.0132  1336 ARG B CA  
4467 C C   . ARG B 299 ? 0.9905 1.1428 1.1935 -0.0275 -0.0777 0.0087  1336 ARG B C   
4468 O O   . ARG B 299 ? 0.9888 1.1473 1.1972 -0.0257 -0.0780 0.0110  1336 ARG B O   
4469 C CB  . ARG B 299 ? 1.0526 1.1468 1.1872 -0.0565 -0.0636 -0.0026 1336 ARG B CB  
4470 C CG  . ARG B 299 ? 1.1277 1.1783 1.1917 -0.0957 -0.0624 -0.0074 1336 ARG B CG  
4471 C CD  . ARG B 299 ? 1.1972 1.1744 1.2111 -0.0933 -0.0200 -0.0261 1336 ARG B CD  
4472 N NE  . ARG B 299 ? 1.3105 1.2113 1.2208 -0.1418 -0.0093 -0.0400 1336 ARG B NE  
4473 C CZ  . ARG B 299 ? 1.3706 1.2259 1.2305 -0.1723 -0.0102 -0.0468 1336 ARG B CZ  
4474 N NH1 . ARG B 299 ? 1.3148 1.2018 1.2319 -0.1500 -0.0179 -0.0392 1336 ARG B NH1 
4475 N NH2 . ARG B 299 ? 1.4960 1.2675 1.2369 -0.2324 -0.0039 -0.0606 1336 ARG B NH2 
4476 N N   . ILE B 300 ? 0.9851 1.1373 1.1976 -0.0173 -0.0748 0.0050  1337 ILE B N   
4477 C CA  . ILE B 300 ? 0.9857 1.1388 1.2009 -0.0133 -0.0748 0.0029  1337 ILE B CA  
4478 C C   . ILE B 300 ? 0.9966 1.1434 1.2061 -0.0089 -0.0675 0.0010  1337 ILE B C   
4479 O O   . ILE B 300 ? 1.0118 1.1505 1.2035 -0.0126 -0.0640 -0.0028 1337 ILE B O   
4480 C CB  . ILE B 300 ? 0.9926 1.1449 1.2100 -0.0180 -0.0796 0.0067  1337 ILE B CB  
4481 C CG1 . ILE B 300 ? 0.9859 1.1466 1.2231 -0.0130 -0.0723 0.0198  1337 ILE B CG1 
4482 C CG2 . ILE B 300 ? 1.0160 1.1637 1.2140 -0.0343 -0.0886 0.0088  1337 ILE B CG2 
4483 C CD1 . ILE B 300 ? 0.9841 1.1580 1.2390 -0.0165 -0.0772 0.0360  1337 ILE B CD1 
4484 N N   . SER B 301 ? 0.9968 1.1468 1.2234 -0.0010 -0.0600 0.0104  1338 SER B N   
4485 C CA  . SER B 301 ? 1.0173 1.1592 1.2555 0.0137  -0.0361 0.0208  1338 SER B CA  
4486 C C   . SER B 301 ? 1.0040 1.1701 1.2548 0.0159  -0.0359 0.0330  1338 SER B C   
4487 O O   . SER B 301 ? 1.0269 1.1760 1.2685 0.0268  -0.0114 0.0330  1338 SER B O   
4488 C CB  . SER B 301 ? 1.0182 1.1758 1.2994 0.0251  -0.0262 0.0480  1338 SER B CB  
4489 O OG  . SER B 301 ? 1.0512 1.2002 1.3609 0.0491  0.0116  0.0702  1338 SER B OG  
4490 N N   . ALA B 302 ? 0.9762 1.1716 1.2374 0.0013  -0.0596 0.0428  1339 ALA B N   
4491 C CA  . ALA B 302 ? 0.9695 1.1856 1.2392 -0.0048 -0.0660 0.0559  1339 ALA B CA  
4492 C C   . ALA B 302 ? 0.9706 1.1689 1.2152 -0.0025 -0.0615 0.0356  1339 ALA B C   
4493 O O   . ALA B 302 ? 0.9788 1.1853 1.2286 0.0045  -0.0504 0.0439  1339 ALA B O   
4494 C CB  . ALA B 302 ? 0.9754 1.1986 1.2323 -0.0341 -0.0907 0.0631  1339 ALA B CB  
4495 N N   . ILE B 303 ? 0.9638 1.1451 1.1887 -0.0092 -0.0688 0.0183  1340 ILE B N   
4496 C CA  . ILE B 303 ? 0.9633 1.1447 1.1802 -0.0129 -0.0710 0.0159  1340 ILE B CA  
4497 C C   . ILE B 303 ? 1.0012 1.1708 1.1888 -0.0168 -0.0632 0.0102  1340 ILE B C   
4498 O O   . ILE B 303 ? 1.0185 1.1951 1.1926 -0.0259 -0.0652 0.0151  1340 ILE B O   
4499 C CB  . ILE B 303 ? 0.9475 1.1247 1.1723 -0.0156 -0.0745 0.0178  1340 ILE B CB  
4500 C CG1 . ILE B 303 ? 0.9493 1.1055 1.1732 -0.0164 -0.0668 0.0159  1340 ILE B CG1 
4501 C CG2 . ILE B 303 ? 0.9488 1.1454 1.1867 -0.0213 -0.0795 0.0353  1340 ILE B CG2 
4502 C CD1 . ILE B 303 ? 0.9592 1.0970 1.1896 -0.0102 -0.0512 0.0193  1340 ILE B CD1 
4503 N N   . PHE B 304 ? 1.0334 1.1751 1.2006 -0.0152 -0.0516 0.0000  1341 PHE B N   
4504 C CA  . PHE B 304 ? 1.1064 1.2031 1.2156 -0.0273 -0.0336 -0.0129 1341 PHE B CA  
4505 C C   . PHE B 304 ? 1.1456 1.2289 1.2461 -0.0119 -0.0010 -0.0097 1341 PHE B C   
4506 O O   . PHE B 304 ? 1.2024 1.2505 1.2414 -0.0288 0.0136  -0.0196 1341 PHE B O   
4507 C CB  . PHE B 304 ? 1.1409 1.1941 1.2292 -0.0273 -0.0198 -0.0245 1341 PHE B CB  
4508 C CG  . PHE B 304 ? 1.2443 1.2170 1.2457 -0.0477 0.0087  -0.0448 1341 PHE B CG  
4509 C CD1 . PHE B 304 ? 1.3002 1.2516 1.2285 -0.0951 -0.0124 -0.0517 1341 PHE B CD1 
4510 C CD2 . PHE B 304 ? 1.3032 1.2146 1.2905 -0.0245 0.0610  -0.0512 1341 PHE B CD2 
4511 C CE1 . PHE B 304 ? 1.4288 1.2835 1.2438 -0.1299 0.0148  -0.0754 1341 PHE B CE1 
4512 C CE2 . PHE B 304 ? 1.4337 1.2388 1.3167 -0.0464 0.1019  -0.0765 1341 PHE B CE2 
4513 C CZ  . PHE B 304 ? 1.5041 1.2728 1.2869 -0.1046 0.0773  -0.0939 1341 PHE B CZ  
4514 N N   . SER B 305 ? 1.1258 1.2401 1.2864 0.0148  0.0097  0.0108  1342 SER B N   
4515 C CA  . SER B 305 ? 1.1633 1.2792 1.3415 0.0366  0.0463  0.0303  1342 SER B CA  
4516 C C   . SER B 305 ? 1.1567 1.3077 1.3396 0.0286  0.0309  0.0391  1342 SER B C   
4517 O O   . SER B 305 ? 1.2028 1.3325 1.3551 0.0330  0.0616  0.0398  1342 SER B O   
4518 C CB  . SER B 305 ? 1.1312 1.2887 1.3885 0.0599  0.0545  0.0691  1342 SER B CB  
4519 O OG  . SER B 305 ? 1.1533 1.2784 1.4139 0.0711  0.0754  0.0675  1342 SER B OG  
4520 N N   . THR B 306 ? 1.1152 1.3090 1.3297 0.0163  -0.0099 0.0457  1343 THR B N   
4521 C CA  . THR B 306 ? 1.1064 1.3320 1.3365 0.0094  -0.0243 0.0592  1343 THR B CA  
4522 C C   . THR B 306 ? 1.1426 1.3551 1.3271 -0.0067 -0.0273 0.0467  1343 THR B C   
4523 O O   . THR B 306 ? 1.1572 1.3841 1.3385 -0.0078 -0.0204 0.0584  1343 THR B O   
4524 C CB  . THR B 306 ? 1.0681 1.3130 1.3246 -0.0038 -0.0561 0.0649  1343 THR B CB  
4525 O OG1 . THR B 306 ? 1.0619 1.2847 1.3000 -0.0109 -0.0658 0.0451  1343 THR B OG1 
4526 C CG2 . THR B 306 ? 1.0564 1.3224 1.3447 -0.0076 -0.0646 0.0875  1343 THR B CG2 
4527 N N   . PHE B 307 ? 1.1653 1.3597 1.3190 -0.0242 -0.0413 0.0320  1344 PHE B N   
4528 C CA  . PHE B 307 ? 1.2001 1.4027 1.3234 -0.0521 -0.0582 0.0379  1344 PHE B CA  
4529 C C   . PHE B 307 ? 1.2778 1.4493 1.3297 -0.0675 -0.0352 0.0309  1344 PHE B C   
4530 O O   . PHE B 307 ? 1.3295 1.4457 1.3345 -0.0592 0.0020  0.0120  1344 PHE B O   
4531 C CB  . PHE B 307 ? 1.2164 1.4130 1.3244 -0.0741 -0.0782 0.0369  1344 PHE B CB  
4532 C CG  . PHE B 307 ? 1.2445 1.4722 1.3399 -0.1117 -0.1057 0.0644  1344 PHE B CG  
4533 C CD1 . PHE B 307 ? 1.2016 1.4837 1.3652 -0.1059 -0.1201 0.0997  1344 PHE B CD1 
4534 C CD2 . PHE B 307 ? 1.3254 1.5253 1.3380 -0.1593 -0.1167 0.0618  1344 PHE B CD2 
4535 C CE1 . PHE B 307 ? 1.2223 1.5511 1.3946 -0.1412 -0.1472 0.1429  1344 PHE B CE1 
4536 C CE2 . PHE B 307 ? 1.3529 1.5971 1.3564 -0.2072 -0.1522 0.1021  1344 PHE B CE2 
4537 C CZ  . PHE B 307 ? 1.2947 1.6136 1.3894 -0.1953 -0.1685 0.1481  1344 PHE B CZ  
4538 N N   . ILE B 308 ? 1.2943 1.4951 1.3360 -0.0902 -0.0514 0.0494  1345 ILE B N   
4539 C CA  . ILE B 308 ? 1.3822 1.5510 1.3410 -0.1133 -0.0296 0.0442  1345 ILE B CA  
4540 C C   . ILE B 308 ? 1.4845 1.5924 1.3313 -0.1649 -0.0325 0.0259  1345 ILE B C   
4541 O O   . ILE B 308 ? 1.4802 1.6277 1.3283 -0.2066 -0.0791 0.0503  1345 ILE B O   
4542 C CB  . ILE B 308 ? 1.3639 1.5926 1.3507 -0.1276 -0.0530 0.0766  1345 ILE B CB  
4543 C CG1 . ILE B 308 ? 1.2867 1.5596 1.3683 -0.0861 -0.0499 0.0929  1345 ILE B CG1 
4544 C CG2 . ILE B 308 ? 1.4694 1.6615 1.3504 -0.1631 -0.0327 0.0717  1345 ILE B CG2 
4545 C CD1 . ILE B 308 ? 1.2589 1.5887 1.3836 -0.0970 -0.0739 0.1278  1345 ILE B CD1 
# 
