data_9MTW
# 
_entry.id   9MTW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9MTW         pdb_00009mtw 10.2210/pdb9mtw/pdb 
WWPDB D_1000291830 ?            ?                   
# 
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 2025-04-23 ? 
2 'Structure model' 1 1 2025-05-14 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_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_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.page_first'              
6  2 'Structure model' '_citation.page_last'               
7  2 'Structure model' '_citation.pdbx_database_id_DOI'    
8  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
9  2 'Structure model' '_citation.title'                   
10 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                        9MTW 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-12 
_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              csmith@slac.stanford.edu 
_pdbx_contact_author.name_first         Clyde 
_pdbx_contact_author.name_last          Smith 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1885-1511 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smith, C.A.'     1 ? 
'Stewart, N.K.'   2 ? 
'Vakulenko, S.B.' 3 ? 
# 
_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            Mbio 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2150-7511 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                e0018525 
_citation.page_last                 e0018525 
_citation.title                     'Evolution of carbapenemase activity in the class C beta-lactamase ADC-1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1128/mbio.00185-25 
_citation.pdbx_database_id_PubMed   40293226 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Stewart, N.K.'    1 0009-0008-2856-420X 
primary 'Toth, M.'         2 ?                   
primary 'Bhattacharya, M.' 3 ?                   
primary 'Smith, C.A.'      4 0000-0002-1885-1511 
primary 'Vakulenko, S.B.'  5 0000-0002-5327-8124 
# 
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 Beta-lactamase 40594.305 2   3.5.2.6 ? ? 'ADC-1 beta-lactamase' 
2 non-polymer syn 
;(4R,5S)-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
;
477.531   1   ?       ? ? ?                      
3 non-polymer syn 1,2-ETHANEDIOL 62.068    2   ?       ? ? ?                      
4 non-polymer syn 
;(2S,3R,4R)-4-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-2-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-3-methyl-3,4-dihydro-2H-pyrrole-5-carboxylic acid
;
477.531   1   ?       ? ? ?                      
5 water       nat water 18.015    395 ?       ? ? ?                      
# 
_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       
;GNTPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKAVNSSTIFELGSVSKLFTATAGGYAKN
KGKISFDDTPGKYWKELKNTPIDQVNLLQLATYTSGNLALQFPDEVKTDQQVLTFFKDWKPKNSIGEYRQYSNPSIGLFG
KVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGYNQENQPIRVNPGPLGAPAYGVKSTLPDMLSFIHANL
NPQKYPADIQRAINETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAISKEPSVKMYHKTGSTNRF
GTYVVFIPKENIGLVMLTNKRIPNEERIKAAYAVLNAIKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GNTPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKAVNSSTIFELGSVSKLFTATAGGYAKN
KGKISFDDTPGKYWKELKNTPIDQVNLLQLATYTSGNLALQFPDEVKTDQQVLTFFKDWKPKNSIGEYRQYSNPSIGLFG
KVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGYNQENQPIRVNPGPLGAPAYGVKSTLPDMLSFIHANL
NPQKYPADIQRAINETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAISKEPSVKMYHKTGSTNRF
GTYVVFIPKENIGLVMLTNKRIPNEERIKAAYAVLNAIKK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(4R,5S)-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
;
1RG   
3 1,2-ETHANEDIOL EDO   
4 
;(2S,3R,4R)-4-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-2-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-3-methyl-3,4-dihydro-2H-pyrrole-5-carboxylic acid
;
A1B93 
5 water HOH   
# 
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   ASN n 
1 3   THR n 
1 4   PRO n 
1 5   LYS n 
1 6   ASP n 
1 7   GLN n 
1 8   GLU n 
1 9   ILE n 
1 10  LYS n 
1 11  LYS n 
1 12  LEU n 
1 13  VAL n 
1 14  ASP n 
1 15  GLN n 
1 16  ASN n 
1 17  PHE n 
1 18  LYS n 
1 19  PRO n 
1 20  LEU n 
1 21  LEU n 
1 22  GLU n 
1 23  LYS n 
1 24  TYR n 
1 25  ASP n 
1 26  VAL n 
1 27  PRO n 
1 28  GLY n 
1 29  MET n 
1 30  ALA n 
1 31  VAL n 
1 32  GLY n 
1 33  VAL n 
1 34  ILE n 
1 35  GLN n 
1 36  ASN n 
1 37  ASN n 
1 38  LYS n 
1 39  LYS n 
1 40  TYR n 
1 41  GLU n 
1 42  MET n 
1 43  TYR n 
1 44  TYR n 
1 45  GLY n 
1 46  LEU n 
1 47  GLN n 
1 48  SER n 
1 49  VAL n 
1 50  GLN n 
1 51  ASP n 
1 52  LYS n 
1 53  LYS n 
1 54  ALA n 
1 55  VAL n 
1 56  ASN n 
1 57  SER n 
1 58  SER n 
1 59  THR n 
1 60  ILE n 
1 61  PHE n 
1 62  GLU n 
1 63  LEU n 
1 64  GLY n 
1 65  SER n 
1 66  VAL n 
1 67  SER n 
1 68  LYS n 
1 69  LEU n 
1 70  PHE n 
1 71  THR n 
1 72  ALA n 
1 73  THR n 
1 74  ALA n 
1 75  GLY n 
1 76  GLY n 
1 77  TYR n 
1 78  ALA n 
1 79  LYS n 
1 80  ASN n 
1 81  LYS n 
1 82  GLY n 
1 83  LYS n 
1 84  ILE n 
1 85  SER n 
1 86  PHE n 
1 87  ASP n 
1 88  ASP n 
1 89  THR n 
1 90  PRO n 
1 91  GLY n 
1 92  LYS n 
1 93  TYR n 
1 94  TRP n 
1 95  LYS n 
1 96  GLU n 
1 97  LEU n 
1 98  LYS n 
1 99  ASN n 
1 100 THR n 
1 101 PRO n 
1 102 ILE n 
1 103 ASP n 
1 104 GLN n 
1 105 VAL n 
1 106 ASN n 
1 107 LEU n 
1 108 LEU n 
1 109 GLN n 
1 110 LEU n 
1 111 ALA n 
1 112 THR n 
1 113 TYR n 
1 114 THR n 
1 115 SER n 
1 116 GLY n 
1 117 ASN n 
1 118 LEU n 
1 119 ALA n 
1 120 LEU n 
1 121 GLN n 
1 122 PHE n 
1 123 PRO n 
1 124 ASP n 
1 125 GLU n 
1 126 VAL n 
1 127 LYS n 
1 128 THR n 
1 129 ASP n 
1 130 GLN n 
1 131 GLN n 
1 132 VAL n 
1 133 LEU n 
1 134 THR n 
1 135 PHE n 
1 136 PHE n 
1 137 LYS n 
1 138 ASP n 
1 139 TRP n 
1 140 LYS n 
1 141 PRO n 
1 142 LYS n 
1 143 ASN n 
1 144 SER n 
1 145 ILE n 
1 146 GLY n 
1 147 GLU n 
1 148 TYR n 
1 149 ARG n 
1 150 GLN n 
1 151 TYR n 
1 152 SER n 
1 153 ASN n 
1 154 PRO n 
1 155 SER n 
1 156 ILE n 
1 157 GLY n 
1 158 LEU n 
1 159 PHE n 
1 160 GLY n 
1 161 LYS n 
1 162 VAL n 
1 163 VAL n 
1 164 ALA n 
1 165 LEU n 
1 166 SER n 
1 167 MET n 
1 168 ASN n 
1 169 LYS n 
1 170 PRO n 
1 171 PHE n 
1 172 ASP n 
1 173 GLN n 
1 174 VAL n 
1 175 LEU n 
1 176 GLU n 
1 177 LYS n 
1 178 THR n 
1 179 ILE n 
1 180 PHE n 
1 181 PRO n 
1 182 ALA n 
1 183 LEU n 
1 184 GLY n 
1 185 LEU n 
1 186 LYS n 
1 187 HIS n 
1 188 SER n 
1 189 TYR n 
1 190 VAL n 
1 191 ASN n 
1 192 VAL n 
1 193 PRO n 
1 194 LYS n 
1 195 THR n 
1 196 GLN n 
1 197 MET n 
1 198 GLN n 
1 199 ASN n 
1 200 TYR n 
1 201 ALA n 
1 202 PHE n 
1 203 GLY n 
1 204 TYR n 
1 205 ASN n 
1 206 GLN n 
1 207 GLU n 
1 208 ASN n 
1 209 GLN n 
1 210 PRO n 
1 211 ILE n 
1 212 ARG n 
1 213 VAL n 
1 214 ASN n 
1 215 PRO n 
1 216 GLY n 
1 217 PRO n 
1 218 LEU n 
1 219 GLY n 
1 220 ALA n 
1 221 PRO n 
1 222 ALA n 
1 223 TYR n 
1 224 GLY n 
1 225 VAL n 
1 226 LYS n 
1 227 SER n 
1 228 THR n 
1 229 LEU n 
1 230 PRO n 
1 231 ASP n 
1 232 MET n 
1 233 LEU n 
1 234 SER n 
1 235 PHE n 
1 236 ILE n 
1 237 HIS n 
1 238 ALA n 
1 239 ASN n 
1 240 LEU n 
1 241 ASN n 
1 242 PRO n 
1 243 GLN n 
1 244 LYS n 
1 245 TYR n 
1 246 PRO n 
1 247 ALA n 
1 248 ASP n 
1 249 ILE n 
1 250 GLN n 
1 251 ARG n 
1 252 ALA n 
1 253 ILE n 
1 254 ASN n 
1 255 GLU n 
1 256 THR n 
1 257 HIS n 
1 258 GLN n 
1 259 GLY n 
1 260 ARG n 
1 261 TYR n 
1 262 GLN n 
1 263 VAL n 
1 264 ASN n 
1 265 THR n 
1 266 MET n 
1 267 TYR n 
1 268 GLN n 
1 269 ALA n 
1 270 LEU n 
1 271 GLY n 
1 272 TRP n 
1 273 GLU n 
1 274 GLU n 
1 275 PHE n 
1 276 SER n 
1 277 TYR n 
1 278 PRO n 
1 279 ALA n 
1 280 THR n 
1 281 LEU n 
1 282 GLN n 
1 283 THR n 
1 284 LEU n 
1 285 LEU n 
1 286 ASP n 
1 287 SER n 
1 288 ASN n 
1 289 SER n 
1 290 GLU n 
1 291 GLN n 
1 292 ILE n 
1 293 VAL n 
1 294 MET n 
1 295 LYS n 
1 296 PRO n 
1 297 ASN n 
1 298 LYS n 
1 299 VAL n 
1 300 THR n 
1 301 ALA n 
1 302 ILE n 
1 303 SER n 
1 304 LYS n 
1 305 GLU n 
1 306 PRO n 
1 307 SER n 
1 308 VAL n 
1 309 LYS n 
1 310 MET n 
1 311 TYR n 
1 312 HIS n 
1 313 LYS n 
1 314 THR n 
1 315 GLY n 
1 316 SER n 
1 317 THR n 
1 318 ASN n 
1 319 ARG n 
1 320 PHE n 
1 321 GLY n 
1 322 THR n 
1 323 TYR n 
1 324 VAL n 
1 325 VAL n 
1 326 PHE n 
1 327 ILE n 
1 328 PRO n 
1 329 LYS n 
1 330 GLU n 
1 331 ASN n 
1 332 ILE n 
1 333 GLY n 
1 334 LEU n 
1 335 VAL n 
1 336 MET n 
1 337 LEU n 
1 338 THR n 
1 339 ASN n 
1 340 LYS n 
1 341 ARG n 
1 342 ILE n 
1 343 PRO n 
1 344 ASN n 
1 345 GLU n 
1 346 GLU n 
1 347 ARG n 
1 348 ILE n 
1 349 LYS n 
1 350 ALA n 
1 351 ALA n 
1 352 TYR n 
1 353 ALA n 
1 354 VAL n 
1 355 LEU n 
1 356 ASN n 
1 357 ALA n 
1 358 ILE n 
1 359 LYS n 
1 360 LYS 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                   360 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ampC 
_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      'Acinetobacter baumannii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     470 
_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 
1RG   non-polymer         . 
;(4R,5S)-3-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
;
'ERTAPENEM, bound form PRE-ISOMERIZED'                      'C22 H27 N3 O7 S' 477.531 
A1B93 non-polymer         . 
;(2S,3R,4R)-4-({(3S,5S)-5-[(3-carboxyphenyl)carbamoyl]pyrrolidin-3-yl}sulfanyl)-2-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-3-methyl-3,4-dihydro-2H-pyrrole-5-carboxylic acid
;
'ertapenem, bound form, post-isomerized, delta-1(R) isomer' 'C22 H27 N3 O7 S' 477.531 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL'                                           'C2 H6 O2'        62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                                                           'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                                                           'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ?                                                           'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ?                                                           'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ?                                                           'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                                                           'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ?                                                           'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ?                                                           'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ?                                                           'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                                                           'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ?                                                           'C5 H9 N O2'      115.130 
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   2   ?   ?   ?   A . n 
A 1 2   ASN 2   3   3   ASN ASN A . n 
A 1 3   THR 3   4   4   THR THR A . n 
A 1 4   PRO 4   5   5   PRO PRO A . n 
A 1 5   LYS 5   6   6   LYS LYS A . n 
A 1 6   ASP 6   7   7   ASP ASP A . n 
A 1 7   GLN 7   8   8   GLN GLN A . n 
A 1 8   GLU 8   9   9   GLU GLU A . n 
A 1 9   ILE 9   10  10  ILE ILE A . n 
A 1 10  LYS 10  11  11  LYS LYS A . n 
A 1 11  LYS 11  12  12  LYS LYS A . n 
A 1 12  LEU 12  13  13  LEU LEU A . n 
A 1 13  VAL 13  14  14  VAL VAL A . n 
A 1 14  ASP 14  15  15  ASP ASP A . n 
A 1 15  GLN 15  16  16  GLN GLN A . n 
A 1 16  ASN 16  17  17  ASN ASN A . n 
A 1 17  PHE 17  18  18  PHE PHE A . n 
A 1 18  LYS 18  19  19  LYS LYS A . n 
A 1 19  PRO 19  20  20  PRO PRO A . n 
A 1 20  LEU 20  21  21  LEU LEU A . n 
A 1 21  LEU 21  22  22  LEU LEU A . n 
A 1 22  GLU 22  23  23  GLU GLU A . n 
A 1 23  LYS 23  24  24  LYS LYS A . n 
A 1 24  TYR 24  25  25  TYR TYR A . n 
A 1 25  ASP 25  26  26  ASP ASP A . n 
A 1 26  VAL 26  27  27  VAL VAL A . n 
A 1 27  PRO 27  28  28  PRO PRO A . n 
A 1 28  GLY 28  29  29  GLY GLY A . n 
A 1 29  MET 29  30  30  MET MET A . n 
A 1 30  ALA 30  31  31  ALA ALA A . n 
A 1 31  VAL 31  32  32  VAL VAL A . n 
A 1 32  GLY 32  33  33  GLY GLY A . n 
A 1 33  VAL 33  34  34  VAL VAL A . n 
A 1 34  ILE 34  35  35  ILE ILE A . n 
A 1 35  GLN 35  36  36  GLN GLN A . n 
A 1 36  ASN 36  37  37  ASN ASN A . n 
A 1 37  ASN 37  38  38  ASN ASN A . n 
A 1 38  LYS 38  39  39  LYS LYS A . n 
A 1 39  LYS 39  40  40  LYS LYS A . n 
A 1 40  TYR 40  41  41  TYR TYR A . n 
A 1 41  GLU 41  42  42  GLU GLU A . n 
A 1 42  MET 42  43  43  MET MET A . n 
A 1 43  TYR 43  44  44  TYR TYR A . n 
A 1 44  TYR 44  45  45  TYR TYR A . n 
A 1 45  GLY 45  46  46  GLY GLY A . n 
A 1 46  LEU 46  47  47  LEU LEU A . n 
A 1 47  GLN 47  48  48  GLN GLN A . n 
A 1 48  SER 48  49  49  SER SER A . n 
A 1 49  VAL 49  50  50  VAL VAL A . n 
A 1 50  GLN 50  51  51  GLN GLN A . n 
A 1 51  ASP 51  52  52  ASP ASP A . n 
A 1 52  LYS 52  53  53  LYS LYS A . n 
A 1 53  LYS 53  54  54  LYS LYS A . n 
A 1 54  ALA 54  55  55  ALA ALA A . n 
A 1 55  VAL 55  56  56  VAL VAL A . n 
A 1 56  ASN 56  57  57  ASN ASN A . n 
A 1 57  SER 57  58  58  SER SER A . n 
A 1 58  SER 58  59  59  SER SER A . n 
A 1 59  THR 59  60  60  THR THR A . n 
A 1 60  ILE 60  61  61  ILE ILE A . n 
A 1 61  PHE 61  62  62  PHE PHE A . n 
A 1 62  GLU 62  63  63  GLU GLU A . n 
A 1 63  LEU 63  64  64  LEU LEU A . n 
A 1 64  GLY 64  65  65  GLY GLY A . n 
A 1 65  SER 65  66  66  SER SER A . n 
A 1 66  VAL 66  67  67  VAL VAL A . n 
A 1 67  SER 67  68  68  SER SER A . n 
A 1 68  LYS 68  69  69  LYS LYS A . n 
A 1 69  LEU 69  70  70  LEU LEU A . n 
A 1 70  PHE 70  71  71  PHE PHE A . n 
A 1 71  THR 71  72  72  THR THR A . n 
A 1 72  ALA 72  73  73  ALA ALA A . n 
A 1 73  THR 73  74  74  THR THR A . n 
A 1 74  ALA 74  75  75  ALA ALA A . n 
A 1 75  GLY 75  76  76  GLY GLY A . n 
A 1 76  GLY 76  77  77  GLY GLY A . n 
A 1 77  TYR 77  78  78  TYR TYR A . n 
A 1 78  ALA 78  79  79  ALA ALA A . n 
A 1 79  LYS 79  80  80  LYS LYS A . n 
A 1 80  ASN 80  81  81  ASN ASN A . n 
A 1 81  LYS 81  82  82  LYS LYS A . n 
A 1 82  GLY 82  83  83  GLY GLY A . n 
A 1 83  LYS 83  84  84  LYS LYS A . n 
A 1 84  ILE 84  85  85  ILE ILE A . n 
A 1 85  SER 85  86  86  SER SER A . n 
A 1 86  PHE 86  87  87  PHE PHE A . n 
A 1 87  ASP 87  88  88  ASP ASP A . n 
A 1 88  ASP 88  89  89  ASP ASP A . n 
A 1 89  THR 89  90  90  THR THR A . n 
A 1 90  PRO 90  91  91  PRO PRO A . n 
A 1 91  GLY 91  92  92  GLY GLY A . n 
A 1 92  LYS 92  93  93  LYS LYS A . n 
A 1 93  TYR 93  94  94  TYR TYR A . n 
A 1 94  TRP 94  95  95  TRP TRP A . n 
A 1 95  LYS 95  96  96  LYS LYS A . n 
A 1 96  GLU 96  97  97  GLU GLU A . n 
A 1 97  LEU 97  98  98  LEU LEU A . n 
A 1 98  LYS 98  99  99  LYS LYS A . n 
A 1 99  ASN 99  100 100 ASN ASN A . n 
A 1 100 THR 100 101 101 THR THR A . n 
A 1 101 PRO 101 102 102 PRO PRO A . n 
A 1 102 ILE 102 103 103 ILE ILE A . n 
A 1 103 ASP 103 104 104 ASP ASP A . n 
A 1 104 GLN 104 105 105 GLN GLN A . n 
A 1 105 VAL 105 106 106 VAL VAL A . n 
A 1 106 ASN 106 107 107 ASN ASN A . n 
A 1 107 LEU 107 108 108 LEU LEU A . n 
A 1 108 LEU 108 109 109 LEU LEU A . n 
A 1 109 GLN 109 110 110 GLN GLN A . n 
A 1 110 LEU 110 111 111 LEU LEU A . n 
A 1 111 ALA 111 112 112 ALA ALA A . n 
A 1 112 THR 112 113 113 THR THR A . n 
A 1 113 TYR 113 114 114 TYR TYR A . n 
A 1 114 THR 114 115 115 THR THR A . n 
A 1 115 SER 115 116 116 SER SER A . n 
A 1 116 GLY 116 117 117 GLY GLY A . n 
A 1 117 ASN 117 118 118 ASN ASN A . n 
A 1 118 LEU 118 119 119 LEU LEU A . n 
A 1 119 ALA 119 120 120 ALA ALA A . n 
A 1 120 LEU 120 121 121 LEU LEU A . n 
A 1 121 GLN 121 122 122 GLN GLN A . n 
A 1 122 PHE 122 123 123 PHE PHE A . n 
A 1 123 PRO 123 124 124 PRO PRO A . n 
A 1 124 ASP 124 125 125 ASP ASP A . n 
A 1 125 GLU 125 126 126 GLU GLU A . n 
A 1 126 VAL 126 127 127 VAL VAL A . n 
A 1 127 LYS 127 128 128 LYS LYS A . n 
A 1 128 THR 128 129 129 THR THR A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 GLN 130 131 131 GLN GLN A . n 
A 1 131 GLN 131 132 132 GLN GLN A . n 
A 1 132 VAL 132 133 133 VAL VAL A . n 
A 1 133 LEU 133 134 134 LEU LEU A . n 
A 1 134 THR 134 135 135 THR THR A . n 
A 1 135 PHE 135 136 136 PHE PHE A . n 
A 1 136 PHE 136 137 137 PHE PHE A . n 
A 1 137 LYS 137 138 138 LYS LYS A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 TRP 139 140 140 TRP TRP A . n 
A 1 140 LYS 140 141 141 LYS LYS A . n 
A 1 141 PRO 141 142 142 PRO PRO A . n 
A 1 142 LYS 142 143 143 LYS LYS A . n 
A 1 143 ASN 143 144 144 ASN ASN A . n 
A 1 144 SER 144 145 145 SER SER A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 GLY 146 147 147 GLY GLY A . n 
A 1 147 GLU 147 148 148 GLU GLU A . n 
A 1 148 TYR 148 149 149 TYR TYR A . n 
A 1 149 ARG 149 150 150 ARG ARG A . n 
A 1 150 GLN 150 151 151 GLN GLN A . n 
A 1 151 TYR 151 152 152 TYR TYR A . n 
A 1 152 SER 152 153 153 SER SER A . n 
A 1 153 ASN 153 154 154 ASN ASN A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 SER 155 156 156 SER SER A . n 
A 1 156 ILE 156 157 157 ILE ILE A . n 
A 1 157 GLY 157 158 158 GLY GLY A . n 
A 1 158 LEU 158 159 159 LEU LEU A . n 
A 1 159 PHE 159 160 160 PHE PHE A . n 
A 1 160 GLY 160 161 161 GLY GLY A . n 
A 1 161 LYS 161 162 162 LYS LYS A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 VAL 163 164 164 VAL VAL A . n 
A 1 164 ALA 164 165 165 ALA ALA A . n 
A 1 165 LEU 165 166 166 LEU LEU A . n 
A 1 166 SER 166 167 167 SER SER A . n 
A 1 167 MET 167 168 168 MET MET A . n 
A 1 168 ASN 168 169 169 ASN ASN A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 PRO 170 171 171 PRO PRO A . n 
A 1 171 PHE 171 172 172 PHE PHE A . n 
A 1 172 ASP 172 173 173 ASP ASP A . n 
A 1 173 GLN 173 174 174 GLN GLN A . n 
A 1 174 VAL 174 175 175 VAL VAL A . n 
A 1 175 LEU 175 176 176 LEU LEU A . n 
A 1 176 GLU 176 177 177 GLU GLU A . n 
A 1 177 LYS 177 178 178 LYS LYS A . n 
A 1 178 THR 178 179 179 THR THR A . n 
A 1 179 ILE 179 180 180 ILE ILE A . n 
A 1 180 PHE 180 181 181 PHE PHE A . n 
A 1 181 PRO 181 182 182 PRO PRO A . n 
A 1 182 ALA 182 183 183 ALA ALA A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 GLY 184 185 185 GLY GLY A . n 
A 1 185 LEU 185 186 186 LEU LEU A . n 
A 1 186 LYS 186 187 187 LYS LYS A . n 
A 1 187 HIS 187 188 188 HIS HIS A . n 
A 1 188 SER 188 189 189 SER SER A . n 
A 1 189 TYR 189 190 190 TYR TYR A . n 
A 1 190 VAL 190 191 191 VAL VAL A . n 
A 1 191 ASN 191 192 192 ASN ASN A . n 
A 1 192 VAL 192 193 193 VAL VAL A . n 
A 1 193 PRO 193 194 194 PRO PRO A . n 
A 1 194 LYS 194 195 195 LYS LYS A . n 
A 1 195 THR 195 196 196 THR THR A . n 
A 1 196 GLN 196 197 197 GLN GLN A . n 
A 1 197 MET 197 198 198 MET MET A . n 
A 1 198 GLN 198 199 199 GLN GLN A . n 
A 1 199 ASN 199 200 200 ASN ASN A . n 
A 1 200 TYR 200 201 201 TYR TYR A . n 
A 1 201 ALA 201 202 202 ALA ALA A . n 
A 1 202 PHE 202 203 203 PHE PHE A . n 
A 1 203 GLY 203 204 204 GLY GLY A . n 
A 1 204 TYR 204 205 205 TYR TYR A . n 
A 1 205 ASN 205 206 206 ASN ASN A . n 
A 1 206 GLN 206 207 207 GLN GLN A . n 
A 1 207 GLU 207 208 208 GLU GLU A . n 
A 1 208 ASN 208 209 209 ASN ASN A . n 
A 1 209 GLN 209 210 210 GLN GLN A . n 
A 1 210 PRO 210 211 211 PRO PRO A . n 
A 1 211 ILE 211 212 212 ILE ILE A . n 
A 1 212 ARG 212 213 213 ARG ARG A . n 
A 1 213 VAL 213 214 ?   ?   ?   A . n 
A 1 214 ASN 214 215 ?   ?   ?   A . n 
A 1 215 PRO 215 216 216 PRO PRO A . n 
A 1 216 GLY 216 217 217 GLY GLY A . n 
A 1 217 PRO 217 218 218 PRO PRO A . n 
A 1 218 LEU 218 219 219 LEU LEU A . n 
A 1 219 GLY 219 220 220 GLY GLY A . n 
A 1 220 ALA 220 221 221 ALA ALA A . n 
A 1 221 PRO 221 222 222 PRO PRO A . n 
A 1 222 ALA 222 223 223 ALA ALA A . n 
A 1 223 TYR 223 224 224 TYR TYR A . n 
A 1 224 GLY 224 225 225 GLY GLY A . n 
A 1 225 VAL 225 226 226 VAL VAL A . n 
A 1 226 LYS 226 227 227 LYS LYS A . n 
A 1 227 SER 227 228 228 SER SER A . n 
A 1 228 THR 228 229 229 THR THR A . n 
A 1 229 LEU 229 230 230 LEU LEU A . n 
A 1 230 PRO 230 231 231 PRO PRO A . n 
A 1 231 ASP 231 232 232 ASP ASP A . n 
A 1 232 MET 232 233 233 MET MET A . n 
A 1 233 LEU 233 234 234 LEU LEU A . n 
A 1 234 SER 234 235 235 SER SER A . n 
A 1 235 PHE 235 236 236 PHE PHE A . n 
A 1 236 ILE 236 237 237 ILE ILE A . n 
A 1 237 HIS 237 238 238 HIS HIS A . n 
A 1 238 ALA 238 239 239 ALA ALA A . n 
A 1 239 ASN 239 240 240 ASN ASN A . n 
A 1 240 LEU 240 241 241 LEU LEU A . n 
A 1 241 ASN 241 242 242 ASN ASN A . n 
A 1 242 PRO 242 243 243 PRO PRO A . n 
A 1 243 GLN 243 244 244 GLN GLN A . n 
A 1 244 LYS 244 245 245 LYS LYS A . n 
A 1 245 TYR 245 246 246 TYR TYR A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 ASP 248 249 249 ASP ASP A . n 
A 1 249 ILE 249 250 250 ILE ILE A . n 
A 1 250 GLN 250 251 251 GLN GLN A . n 
A 1 251 ARG 251 252 252 ARG ARG A . n 
A 1 252 ALA 252 253 253 ALA ALA A . n 
A 1 253 ILE 253 254 254 ILE ILE A . n 
A 1 254 ASN 254 255 255 ASN ASN A . n 
A 1 255 GLU 255 256 256 GLU GLU A . n 
A 1 256 THR 256 257 257 THR THR A . n 
A 1 257 HIS 257 258 258 HIS HIS A . n 
A 1 258 GLN 258 259 259 GLN GLN A . n 
A 1 259 GLY 259 260 260 GLY GLY A . n 
A 1 260 ARG 260 261 261 ARG ARG A . n 
A 1 261 TYR 261 262 262 TYR TYR A . n 
A 1 262 GLN 262 263 263 GLN GLN A . n 
A 1 263 VAL 263 264 264 VAL VAL A . n 
A 1 264 ASN 264 265 265 ASN ASN A . n 
A 1 265 THR 265 266 266 THR THR A . n 
A 1 266 MET 266 267 267 MET MET A . n 
A 1 267 TYR 267 268 268 TYR TYR A . n 
A 1 268 GLN 268 269 269 GLN GLN A . n 
A 1 269 ALA 269 270 270 ALA ALA A . n 
A 1 270 LEU 270 271 271 LEU LEU A . n 
A 1 271 GLY 271 272 272 GLY GLY A . n 
A 1 272 TRP 272 273 273 TRP TRP A . n 
A 1 273 GLU 273 274 274 GLU GLU A . n 
A 1 274 GLU 274 275 275 GLU GLU A . n 
A 1 275 PHE 275 276 276 PHE PHE A . n 
A 1 276 SER 276 277 277 SER SER A . n 
A 1 277 TYR 277 278 278 TYR TYR A . n 
A 1 278 PRO 278 279 279 PRO PRO A . n 
A 1 279 ALA 279 280 280 ALA ALA A . n 
A 1 280 THR 280 281 281 THR THR A . n 
A 1 281 LEU 281 282 282 LEU LEU A . n 
A 1 282 GLN 282 283 283 GLN GLN A . n 
A 1 283 THR 283 284 284 THR THR A . n 
A 1 284 LEU 284 285 285 LEU LEU A . n 
A 1 285 LEU 285 286 286 LEU LEU A . n 
A 1 286 ASP 286 287 287 ASP ASP A . n 
A 1 287 SER 287 288 288 SER SER A . n 
A 1 288 ASN 288 289 289 ASN ASN A . n 
A 1 289 SER 289 290 290 SER SER A . n 
A 1 290 GLU 290 291 291 GLU GLU A . n 
A 1 291 GLN 291 292 292 GLN GLN A . n 
A 1 292 ILE 292 293 293 ILE ILE A . n 
A 1 293 VAL 293 294 294 VAL VAL A . n 
A 1 294 MET 294 295 295 MET MET A . n 
A 1 295 LYS 295 296 296 LYS LYS A . n 
A 1 296 PRO 296 297 297 PRO PRO A . n 
A 1 297 ASN 297 298 298 ASN ASN A . n 
A 1 298 LYS 298 299 299 LYS LYS A . n 
A 1 299 VAL 299 300 300 VAL VAL A . n 
A 1 300 THR 300 301 301 THR THR A . n 
A 1 301 ALA 301 302 302 ALA ALA A . n 
A 1 302 ILE 302 303 303 ILE ILE A . n 
A 1 303 SER 303 304 304 SER SER A . n 
A 1 304 LYS 304 305 305 LYS LYS A . n 
A 1 305 GLU 305 306 306 GLU GLU A . n 
A 1 306 PRO 306 307 307 PRO PRO A . n 
A 1 307 SER 307 308 308 SER SER A . n 
A 1 308 VAL 308 309 309 VAL VAL A . n 
A 1 309 LYS 309 310 310 LYS LYS A . n 
A 1 310 MET 310 311 311 MET MET A . n 
A 1 311 TYR 311 312 312 TYR TYR A . n 
A 1 312 HIS 312 313 313 HIS HIS A . n 
A 1 313 LYS 313 314 314 LYS LYS A . n 
A 1 314 THR 314 315 315 THR THR A . n 
A 1 315 GLY 315 316 316 GLY GLY A . n 
A 1 316 SER 316 317 317 SER SER A . n 
A 1 317 THR 317 318 318 THR THR A . n 
A 1 318 ASN 318 319 319 ASN ASN A . n 
A 1 319 ARG 319 320 320 ARG ARG A . n 
A 1 320 PHE 320 321 321 PHE PHE A . n 
A 1 321 GLY 321 322 322 GLY GLY A . n 
A 1 322 THR 322 323 323 THR THR A . n 
A 1 323 TYR 323 324 324 TYR TYR A . n 
A 1 324 VAL 324 325 325 VAL VAL A . n 
A 1 325 VAL 325 326 326 VAL VAL A . n 
A 1 326 PHE 326 327 327 PHE PHE A . n 
A 1 327 ILE 327 328 328 ILE ILE A . n 
A 1 328 PRO 328 329 329 PRO PRO A . n 
A 1 329 LYS 329 330 330 LYS LYS A . n 
A 1 330 GLU 330 331 331 GLU GLU A . n 
A 1 331 ASN 331 332 332 ASN ASN A . n 
A 1 332 ILE 332 333 333 ILE ILE A . n 
A 1 333 GLY 333 334 334 GLY GLY A . n 
A 1 334 LEU 334 335 335 LEU LEU A . n 
A 1 335 VAL 335 336 336 VAL VAL A . n 
A 1 336 MET 336 337 337 MET MET A . n 
A 1 337 LEU 337 338 338 LEU LEU A . n 
A 1 338 THR 338 339 339 THR THR A . n 
A 1 339 ASN 339 340 340 ASN ASN A . n 
A 1 340 LYS 340 341 341 LYS LYS A . n 
A 1 341 ARG 341 342 342 ARG ARG A . n 
A 1 342 ILE 342 343 343 ILE ILE A . n 
A 1 343 PRO 343 344 344 PRO PRO A . n 
A 1 344 ASN 344 345 345 ASN ASN A . n 
A 1 345 GLU 345 346 346 GLU GLU A . n 
A 1 346 GLU 346 347 347 GLU GLU A . n 
A 1 347 ARG 347 348 348 ARG ARG A . n 
A 1 348 ILE 348 349 349 ILE ILE A . n 
A 1 349 LYS 349 350 350 LYS LYS A . n 
A 1 350 ALA 350 351 351 ALA ALA A . n 
A 1 351 ALA 351 352 352 ALA ALA A . n 
A 1 352 TYR 352 353 353 TYR TYR A . n 
A 1 353 ALA 353 354 354 ALA ALA A . n 
A 1 354 VAL 354 355 355 VAL VAL A . n 
A 1 355 LEU 355 356 356 LEU LEU A . n 
A 1 356 ASN 356 357 357 ASN ASN A . n 
A 1 357 ALA 357 358 358 ALA ALA A . n 
A 1 358 ILE 358 359 359 ILE ILE A . n 
A 1 359 LYS 359 360 360 LYS LYS A . n 
A 1 360 LYS 360 361 361 LYS LYS A . n 
B 1 1   GLY 1   2   ?   ?   ?   B . n 
B 1 2   ASN 2   3   3   ASN ASN B . n 
B 1 3   THR 3   4   4   THR THR B . n 
B 1 4   PRO 4   5   5   PRO PRO B . n 
B 1 5   LYS 5   6   6   LYS LYS B . n 
B 1 6   ASP 6   7   7   ASP ASP B . n 
B 1 7   GLN 7   8   8   GLN GLN B . n 
B 1 8   GLU 8   9   9   GLU GLU B . n 
B 1 9   ILE 9   10  10  ILE ILE B . n 
B 1 10  LYS 10  11  11  LYS LYS B . n 
B 1 11  LYS 11  12  12  LYS LYS B . n 
B 1 12  LEU 12  13  13  LEU LEU B . n 
B 1 13  VAL 13  14  14  VAL VAL B . n 
B 1 14  ASP 14  15  15  ASP ASP B . n 
B 1 15  GLN 15  16  16  GLN GLN B . n 
B 1 16  ASN 16  17  17  ASN ASN B . n 
B 1 17  PHE 17  18  18  PHE PHE B . n 
B 1 18  LYS 18  19  19  LYS LYS B . n 
B 1 19  PRO 19  20  20  PRO PRO B . n 
B 1 20  LEU 20  21  21  LEU LEU B . n 
B 1 21  LEU 21  22  22  LEU LEU B . n 
B 1 22  GLU 22  23  23  GLU GLU B . n 
B 1 23  LYS 23  24  24  LYS LYS B . n 
B 1 24  TYR 24  25  25  TYR TYR B . n 
B 1 25  ASP 25  26  26  ASP ASP B . n 
B 1 26  VAL 26  27  27  VAL VAL B . n 
B 1 27  PRO 27  28  28  PRO PRO B . n 
B 1 28  GLY 28  29  29  GLY GLY B . n 
B 1 29  MET 29  30  30  MET MET B . n 
B 1 30  ALA 30  31  31  ALA ALA B . n 
B 1 31  VAL 31  32  32  VAL VAL B . n 
B 1 32  GLY 32  33  33  GLY GLY B . n 
B 1 33  VAL 33  34  34  VAL VAL B . n 
B 1 34  ILE 34  35  35  ILE ILE B . n 
B 1 35  GLN 35  36  36  GLN GLN B . n 
B 1 36  ASN 36  37  37  ASN ASN B . n 
B 1 37  ASN 37  38  38  ASN ASN B . n 
B 1 38  LYS 38  39  39  LYS LYS B . n 
B 1 39  LYS 39  40  40  LYS LYS B . n 
B 1 40  TYR 40  41  41  TYR TYR B . n 
B 1 41  GLU 41  42  42  GLU GLU B . n 
B 1 42  MET 42  43  43  MET MET B . n 
B 1 43  TYR 43  44  44  TYR TYR B . n 
B 1 44  TYR 44  45  45  TYR TYR B . n 
B 1 45  GLY 45  46  46  GLY GLY B . n 
B 1 46  LEU 46  47  47  LEU LEU B . n 
B 1 47  GLN 47  48  48  GLN GLN B . n 
B 1 48  SER 48  49  49  SER SER B . n 
B 1 49  VAL 49  50  50  VAL VAL B . n 
B 1 50  GLN 50  51  51  GLN GLN B . n 
B 1 51  ASP 51  52  52  ASP ASP B . n 
B 1 52  LYS 52  53  53  LYS LYS B . n 
B 1 53  LYS 53  54  54  LYS LYS B . n 
B 1 54  ALA 54  55  55  ALA ALA B . n 
B 1 55  VAL 55  56  56  VAL VAL B . n 
B 1 56  ASN 56  57  57  ASN ASN B . n 
B 1 57  SER 57  58  58  SER SER B . n 
B 1 58  SER 58  59  59  SER SER B . n 
B 1 59  THR 59  60  60  THR THR B . n 
B 1 60  ILE 60  61  61  ILE ILE B . n 
B 1 61  PHE 61  62  62  PHE PHE B . n 
B 1 62  GLU 62  63  63  GLU GLU B . n 
B 1 63  LEU 63  64  64  LEU LEU B . n 
B 1 64  GLY 64  65  65  GLY GLY B . n 
B 1 65  SER 65  66  66  SER SER B . n 
B 1 66  VAL 66  67  67  VAL VAL B . n 
B 1 67  SER 67  68  68  SER SER B . n 
B 1 68  LYS 68  69  69  LYS LYS B . n 
B 1 69  LEU 69  70  70  LEU LEU B . n 
B 1 70  PHE 70  71  71  PHE PHE B . n 
B 1 71  THR 71  72  72  THR THR B . n 
B 1 72  ALA 72  73  73  ALA ALA B . n 
B 1 73  THR 73  74  74  THR THR B . n 
B 1 74  ALA 74  75  75  ALA ALA B . n 
B 1 75  GLY 75  76  76  GLY GLY B . n 
B 1 76  GLY 76  77  77  GLY GLY B . n 
B 1 77  TYR 77  78  78  TYR TYR B . n 
B 1 78  ALA 78  79  79  ALA ALA B . n 
B 1 79  LYS 79  80  80  LYS LYS B . n 
B 1 80  ASN 80  81  81  ASN ASN B . n 
B 1 81  LYS 81  82  82  LYS LYS B . n 
B 1 82  GLY 82  83  83  GLY GLY B . n 
B 1 83  LYS 83  84  84  LYS LYS B . n 
B 1 84  ILE 84  85  85  ILE ILE B . n 
B 1 85  SER 85  86  86  SER SER B . n 
B 1 86  PHE 86  87  87  PHE PHE B . n 
B 1 87  ASP 87  88  88  ASP ASP B . n 
B 1 88  ASP 88  89  89  ASP ASP B . n 
B 1 89  THR 89  90  90  THR THR B . n 
B 1 90  PRO 90  91  91  PRO PRO B . n 
B 1 91  GLY 91  92  92  GLY GLY B . n 
B 1 92  LYS 92  93  93  LYS LYS B . n 
B 1 93  TYR 93  94  94  TYR TYR B . n 
B 1 94  TRP 94  95  95  TRP TRP B . n 
B 1 95  LYS 95  96  96  LYS LYS B . n 
B 1 96  GLU 96  97  97  GLU GLU B . n 
B 1 97  LEU 97  98  98  LEU LEU B . n 
B 1 98  LYS 98  99  99  LYS LYS B . n 
B 1 99  ASN 99  100 100 ASN ASN B . n 
B 1 100 THR 100 101 101 THR THR B . n 
B 1 101 PRO 101 102 102 PRO PRO B . n 
B 1 102 ILE 102 103 103 ILE ILE B . n 
B 1 103 ASP 103 104 104 ASP ASP B . n 
B 1 104 GLN 104 105 105 GLN GLN B . n 
B 1 105 VAL 105 106 106 VAL VAL B . n 
B 1 106 ASN 106 107 107 ASN ASN B . n 
B 1 107 LEU 107 108 108 LEU LEU B . n 
B 1 108 LEU 108 109 109 LEU LEU B . n 
B 1 109 GLN 109 110 110 GLN GLN B . n 
B 1 110 LEU 110 111 111 LEU LEU B . n 
B 1 111 ALA 111 112 112 ALA ALA B . n 
B 1 112 THR 112 113 113 THR THR B . n 
B 1 113 TYR 113 114 114 TYR TYR B . n 
B 1 114 THR 114 115 115 THR THR B . n 
B 1 115 SER 115 116 116 SER SER B . n 
B 1 116 GLY 116 117 117 GLY GLY B . n 
B 1 117 ASN 117 118 118 ASN ASN B . n 
B 1 118 LEU 118 119 119 LEU LEU B . n 
B 1 119 ALA 119 120 120 ALA ALA B . n 
B 1 120 LEU 120 121 121 LEU LEU B . n 
B 1 121 GLN 121 122 122 GLN GLN B . n 
B 1 122 PHE 122 123 123 PHE PHE B . n 
B 1 123 PRO 123 124 124 PRO PRO B . n 
B 1 124 ASP 124 125 125 ASP ASP B . n 
B 1 125 GLU 125 126 126 GLU GLU B . n 
B 1 126 VAL 126 127 127 VAL VAL B . n 
B 1 127 LYS 127 128 128 LYS LYS B . n 
B 1 128 THR 128 129 129 THR THR B . n 
B 1 129 ASP 129 130 130 ASP ASP B . n 
B 1 130 GLN 130 131 131 GLN GLN B . n 
B 1 131 GLN 131 132 132 GLN GLN B . n 
B 1 132 VAL 132 133 133 VAL VAL B . n 
B 1 133 LEU 133 134 134 LEU LEU B . n 
B 1 134 THR 134 135 135 THR THR B . n 
B 1 135 PHE 135 136 136 PHE PHE B . n 
B 1 136 PHE 136 137 137 PHE PHE B . n 
B 1 137 LYS 137 138 138 LYS LYS B . n 
B 1 138 ASP 138 139 139 ASP ASP B . n 
B 1 139 TRP 139 140 140 TRP TRP B . n 
B 1 140 LYS 140 141 141 LYS LYS B . n 
B 1 141 PRO 141 142 142 PRO PRO B . n 
B 1 142 LYS 142 143 143 LYS LYS B . n 
B 1 143 ASN 143 144 144 ASN ASN B . n 
B 1 144 SER 144 145 145 SER SER B . n 
B 1 145 ILE 145 146 146 ILE ILE B . n 
B 1 146 GLY 146 147 147 GLY GLY B . n 
B 1 147 GLU 147 148 148 GLU GLU B . n 
B 1 148 TYR 148 149 149 TYR TYR B . n 
B 1 149 ARG 149 150 150 ARG ARG B . n 
B 1 150 GLN 150 151 151 GLN GLN B . n 
B 1 151 TYR 151 152 152 TYR TYR B . n 
B 1 152 SER 152 153 153 SER SER B . n 
B 1 153 ASN 153 154 154 ASN ASN B . n 
B 1 154 PRO 154 155 155 PRO PRO B . n 
B 1 155 SER 155 156 156 SER SER B . n 
B 1 156 ILE 156 157 157 ILE ILE B . n 
B 1 157 GLY 157 158 158 GLY GLY B . n 
B 1 158 LEU 158 159 159 LEU LEU B . n 
B 1 159 PHE 159 160 160 PHE PHE B . n 
B 1 160 GLY 160 161 161 GLY GLY B . n 
B 1 161 LYS 161 162 162 LYS LYS B . n 
B 1 162 VAL 162 163 163 VAL VAL B . n 
B 1 163 VAL 163 164 164 VAL VAL B . n 
B 1 164 ALA 164 165 165 ALA ALA B . n 
B 1 165 LEU 165 166 166 LEU LEU B . n 
B 1 166 SER 166 167 167 SER SER B . n 
B 1 167 MET 167 168 168 MET MET B . n 
B 1 168 ASN 168 169 169 ASN ASN B . n 
B 1 169 LYS 169 170 170 LYS LYS B . n 
B 1 170 PRO 170 171 171 PRO PRO B . n 
B 1 171 PHE 171 172 172 PHE PHE B . n 
B 1 172 ASP 172 173 173 ASP ASP B . n 
B 1 173 GLN 173 174 174 GLN GLN B . n 
B 1 174 VAL 174 175 175 VAL VAL B . n 
B 1 175 LEU 175 176 176 LEU LEU B . n 
B 1 176 GLU 176 177 177 GLU GLU B . n 
B 1 177 LYS 177 178 178 LYS LYS B . n 
B 1 178 THR 178 179 179 THR THR B . n 
B 1 179 ILE 179 180 180 ILE ILE B . n 
B 1 180 PHE 180 181 181 PHE PHE B . n 
B 1 181 PRO 181 182 182 PRO PRO B . n 
B 1 182 ALA 182 183 183 ALA ALA B . n 
B 1 183 LEU 183 184 184 LEU LEU B . n 
B 1 184 GLY 184 185 185 GLY GLY B . n 
B 1 185 LEU 185 186 186 LEU LEU B . n 
B 1 186 LYS 186 187 187 LYS LYS B . n 
B 1 187 HIS 187 188 188 HIS HIS B . n 
B 1 188 SER 188 189 189 SER SER B . n 
B 1 189 TYR 189 190 190 TYR TYR B . n 
B 1 190 VAL 190 191 191 VAL VAL B . n 
B 1 191 ASN 191 192 192 ASN ASN B . n 
B 1 192 VAL 192 193 193 VAL VAL B . n 
B 1 193 PRO 193 194 194 PRO PRO B . n 
B 1 194 LYS 194 195 195 LYS LYS B . n 
B 1 195 THR 195 196 196 THR THR B . n 
B 1 196 GLN 196 197 197 GLN GLN B . n 
B 1 197 MET 197 198 198 MET MET B . n 
B 1 198 GLN 198 199 199 GLN GLN B . n 
B 1 199 ASN 199 200 200 ASN ASN B . n 
B 1 200 TYR 200 201 201 TYR TYR B . n 
B 1 201 ALA 201 202 202 ALA ALA B . n 
B 1 202 PHE 202 203 ?   ?   ?   B . n 
B 1 203 GLY 203 204 ?   ?   ?   B . n 
B 1 204 TYR 204 205 ?   ?   ?   B . n 
B 1 205 ASN 205 206 ?   ?   ?   B . n 
B 1 206 GLN 206 207 ?   ?   ?   B . n 
B 1 207 GLU 207 208 ?   ?   ?   B . n 
B 1 208 ASN 208 209 ?   ?   ?   B . n 
B 1 209 GLN 209 210 ?   ?   ?   B . n 
B 1 210 PRO 210 211 ?   ?   ?   B . n 
B 1 211 ILE 211 212 ?   ?   ?   B . n 
B 1 212 ARG 212 213 ?   ?   ?   B . n 
B 1 213 VAL 213 214 ?   ?   ?   B . n 
B 1 214 ASN 214 215 ?   ?   ?   B . n 
B 1 215 PRO 215 216 ?   ?   ?   B . n 
B 1 216 GLY 216 217 217 GLY GLY B . n 
B 1 217 PRO 217 218 218 PRO PRO B . n 
B 1 218 LEU 218 219 219 LEU LEU B . n 
B 1 219 GLY 219 220 220 GLY GLY B . n 
B 1 220 ALA 220 221 221 ALA ALA B . n 
B 1 221 PRO 221 222 222 PRO PRO B . n 
B 1 222 ALA 222 223 223 ALA ALA B . n 
B 1 223 TYR 223 224 224 TYR TYR B . n 
B 1 224 GLY 224 225 225 GLY GLY B . n 
B 1 225 VAL 225 226 226 VAL VAL B . n 
B 1 226 LYS 226 227 227 LYS LYS B . n 
B 1 227 SER 227 228 228 SER SER B . n 
B 1 228 THR 228 229 229 THR THR B . n 
B 1 229 LEU 229 230 230 LEU LEU B . n 
B 1 230 PRO 230 231 231 PRO PRO B . n 
B 1 231 ASP 231 232 232 ASP ASP B . n 
B 1 232 MET 232 233 233 MET MET B . n 
B 1 233 LEU 233 234 234 LEU LEU B . n 
B 1 234 SER 234 235 235 SER SER B . n 
B 1 235 PHE 235 236 236 PHE PHE B . n 
B 1 236 ILE 236 237 237 ILE ILE B . n 
B 1 237 HIS 237 238 238 HIS HIS B . n 
B 1 238 ALA 238 239 239 ALA ALA B . n 
B 1 239 ASN 239 240 240 ASN ASN B . n 
B 1 240 LEU 240 241 241 LEU LEU B . n 
B 1 241 ASN 241 242 242 ASN ASN B . n 
B 1 242 PRO 242 243 243 PRO PRO B . n 
B 1 243 GLN 243 244 244 GLN GLN B . n 
B 1 244 LYS 244 245 245 LYS LYS B . n 
B 1 245 TYR 245 246 246 TYR TYR B . n 
B 1 246 PRO 246 247 247 PRO PRO B . n 
B 1 247 ALA 247 248 248 ALA ALA B . n 
B 1 248 ASP 248 249 249 ASP ASP B . n 
B 1 249 ILE 249 250 250 ILE ILE B . n 
B 1 250 GLN 250 251 251 GLN GLN B . n 
B 1 251 ARG 251 252 252 ARG ARG B . n 
B 1 252 ALA 252 253 253 ALA ALA B . n 
B 1 253 ILE 253 254 254 ILE ILE B . n 
B 1 254 ASN 254 255 255 ASN ASN B . n 
B 1 255 GLU 255 256 256 GLU GLU B . n 
B 1 256 THR 256 257 257 THR THR B . n 
B 1 257 HIS 257 258 258 HIS HIS B . n 
B 1 258 GLN 258 259 259 GLN GLN B . n 
B 1 259 GLY 259 260 260 GLY GLY B . n 
B 1 260 ARG 260 261 261 ARG ARG B . n 
B 1 261 TYR 261 262 262 TYR TYR B . n 
B 1 262 GLN 262 263 263 GLN GLN B . n 
B 1 263 VAL 263 264 264 VAL VAL B . n 
B 1 264 ASN 264 265 265 ASN ASN B . n 
B 1 265 THR 265 266 266 THR THR B . n 
B 1 266 MET 266 267 267 MET MET B . n 
B 1 267 TYR 267 268 268 TYR TYR B . n 
B 1 268 GLN 268 269 269 GLN GLN B . n 
B 1 269 ALA 269 270 270 ALA ALA B . n 
B 1 270 LEU 270 271 271 LEU LEU B . n 
B 1 271 GLY 271 272 272 GLY GLY B . n 
B 1 272 TRP 272 273 273 TRP TRP B . n 
B 1 273 GLU 273 274 274 GLU GLU B . n 
B 1 274 GLU 274 275 275 GLU GLU B . n 
B 1 275 PHE 275 276 276 PHE PHE B . n 
B 1 276 SER 276 277 277 SER SER B . n 
B 1 277 TYR 277 278 278 TYR TYR B . n 
B 1 278 PRO 278 279 279 PRO PRO B . n 
B 1 279 ALA 279 280 280 ALA ALA B . n 
B 1 280 THR 280 281 281 THR THR B . n 
B 1 281 LEU 281 282 282 LEU LEU B . n 
B 1 282 GLN 282 283 283 GLN GLN B . n 
B 1 283 THR 283 284 284 THR THR B . n 
B 1 284 LEU 284 285 285 LEU LEU B . n 
B 1 285 LEU 285 286 286 LEU LEU B . n 
B 1 286 ASP 286 287 287 ASP ASP B . n 
B 1 287 SER 287 288 288 SER SER B . n 
B 1 288 ASN 288 289 289 ASN ASN B . n 
B 1 289 SER 289 290 290 SER SER B . n 
B 1 290 GLU 290 291 291 GLU GLU B . n 
B 1 291 GLN 291 292 292 GLN GLN B . n 
B 1 292 ILE 292 293 293 ILE ILE B . n 
B 1 293 VAL 293 294 294 VAL VAL B . n 
B 1 294 MET 294 295 295 MET MET B . n 
B 1 295 LYS 295 296 296 LYS LYS B . n 
B 1 296 PRO 296 297 297 PRO PRO B . n 
B 1 297 ASN 297 298 298 ASN ASN B . n 
B 1 298 LYS 298 299 299 LYS LYS B . n 
B 1 299 VAL 299 300 300 VAL VAL B . n 
B 1 300 THR 300 301 301 THR THR B . n 
B 1 301 ALA 301 302 302 ALA ALA B . n 
B 1 302 ILE 302 303 303 ILE ILE B . n 
B 1 303 SER 303 304 304 SER SER B . n 
B 1 304 LYS 304 305 305 LYS LYS B . n 
B 1 305 GLU 305 306 306 GLU GLU B . n 
B 1 306 PRO 306 307 307 PRO PRO B . n 
B 1 307 SER 307 308 308 SER SER B . n 
B 1 308 VAL 308 309 309 VAL VAL B . n 
B 1 309 LYS 309 310 310 LYS LYS B . n 
B 1 310 MET 310 311 311 MET MET B . n 
B 1 311 TYR 311 312 312 TYR TYR B . n 
B 1 312 HIS 312 313 313 HIS HIS B . n 
B 1 313 LYS 313 314 314 LYS LYS B . n 
B 1 314 THR 314 315 315 THR THR B . n 
B 1 315 GLY 315 316 316 GLY GLY B . n 
B 1 316 SER 316 317 317 SER SER B . n 
B 1 317 THR 317 318 318 THR THR B . n 
B 1 318 ASN 318 319 319 ASN ASN B . n 
B 1 319 ARG 319 320 320 ARG ARG B . n 
B 1 320 PHE 320 321 321 PHE PHE B . n 
B 1 321 GLY 321 322 322 GLY GLY B . n 
B 1 322 THR 322 323 323 THR THR B . n 
B 1 323 TYR 323 324 324 TYR TYR B . n 
B 1 324 VAL 324 325 325 VAL VAL B . n 
B 1 325 VAL 325 326 326 VAL VAL B . n 
B 1 326 PHE 326 327 327 PHE PHE B . n 
B 1 327 ILE 327 328 328 ILE ILE B . n 
B 1 328 PRO 328 329 329 PRO PRO B . n 
B 1 329 LYS 329 330 330 LYS LYS B . n 
B 1 330 GLU 330 331 331 GLU GLU B . n 
B 1 331 ASN 331 332 332 ASN ASN B . n 
B 1 332 ILE 332 333 333 ILE ILE B . n 
B 1 333 GLY 333 334 334 GLY GLY B . n 
B 1 334 LEU 334 335 335 LEU LEU B . n 
B 1 335 VAL 335 336 336 VAL VAL B . n 
B 1 336 MET 336 337 337 MET MET B . n 
B 1 337 LEU 337 338 338 LEU LEU B . n 
B 1 338 THR 338 339 339 THR THR B . n 
B 1 339 ASN 339 340 340 ASN ASN B . n 
B 1 340 LYS 340 341 341 LYS LYS B . n 
B 1 341 ARG 341 342 342 ARG ARG B . n 
B 1 342 ILE 342 343 343 ILE ILE B . n 
B 1 343 PRO 343 344 344 PRO PRO B . n 
B 1 344 ASN 344 345 345 ASN ASN B . n 
B 1 345 GLU 345 346 346 GLU GLU B . n 
B 1 346 GLU 346 347 347 GLU GLU B . n 
B 1 347 ARG 347 348 348 ARG ARG B . n 
B 1 348 ILE 348 349 349 ILE ILE B . n 
B 1 349 LYS 349 350 350 LYS LYS B . n 
B 1 350 ALA 350 351 351 ALA ALA B . n 
B 1 351 ALA 351 352 352 ALA ALA B . n 
B 1 352 TYR 352 353 353 TYR TYR B . n 
B 1 353 ALA 353 354 354 ALA ALA B . n 
B 1 354 VAL 354 355 355 VAL VAL B . n 
B 1 355 LEU 355 356 356 LEU LEU B . n 
B 1 356 ASN 356 357 357 ASN ASN B . n 
B 1 357 ALA 357 358 358 ALA ALA B . n 
B 1 358 ILE 358 359 359 ILE ILE B . n 
B 1 359 LYS 359 360 360 LYS LYS B . n 
B 1 360 LYS 360 361 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B93 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B93 
_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 1RG   1   401 401 1RG   1RG A . 
D 3 EDO   1   402 402 EDO   EDO A . 
E 4 A1B93 1   401 401 A1B93 N9X B . 
F 3 EDO   1   402 402 EDO   EDO B . 
G 5 HOH   1   501 327 HOH   HOH A . 
G 5 HOH   2   502 320 HOH   HOH A . 
G 5 HOH   3   503 323 HOH   HOH A . 
G 5 HOH   4   504 355 HOH   HOH A . 
G 5 HOH   5   505 266 HOH   HOH A . 
G 5 HOH   6   506 197 HOH   HOH A . 
G 5 HOH   7   507 318 HOH   HOH A . 
G 5 HOH   8   508 280 HOH   HOH A . 
G 5 HOH   9   509 294 HOH   HOH A . 
G 5 HOH   10  510 188 HOH   HOH A . 
G 5 HOH   11  511 236 HOH   HOH A . 
G 5 HOH   12  512 305 HOH   HOH A . 
G 5 HOH   13  513 268 HOH   HOH A . 
G 5 HOH   14  514 269 HOH   HOH A . 
G 5 HOH   15  515 69  HOH   HOH A . 
G 5 HOH   16  516 35  HOH   HOH A . 
G 5 HOH   17  517 208 HOH   HOH A . 
G 5 HOH   18  518 127 HOH   HOH A . 
G 5 HOH   19  519 220 HOH   HOH A . 
G 5 HOH   20  520 256 HOH   HOH A . 
G 5 HOH   21  521 299 HOH   HOH A . 
G 5 HOH   22  522 158 HOH   HOH A . 
G 5 HOH   23  523 282 HOH   HOH A . 
G 5 HOH   24  524 61  HOH   HOH A . 
G 5 HOH   25  525 340 HOH   HOH A . 
G 5 HOH   26  526 55  HOH   HOH A . 
G 5 HOH   27  527 247 HOH   HOH A . 
G 5 HOH   28  528 341 HOH   HOH A . 
G 5 HOH   29  529 177 HOH   HOH A . 
G 5 HOH   30  530 182 HOH   HOH A . 
G 5 HOH   31  531 102 HOH   HOH A . 
G 5 HOH   32  532 213 HOH   HOH A . 
G 5 HOH   33  533 348 HOH   HOH A . 
G 5 HOH   34  534 83  HOH   HOH A . 
G 5 HOH   35  535 56  HOH   HOH A . 
G 5 HOH   36  536 22  HOH   HOH A . 
G 5 HOH   37  537 155 HOH   HOH A . 
G 5 HOH   38  538 29  HOH   HOH A . 
G 5 HOH   39  539 162 HOH   HOH A . 
G 5 HOH   40  540 41  HOH   HOH A . 
G 5 HOH   41  541 140 HOH   HOH A . 
G 5 HOH   42  542 228 HOH   HOH A . 
G 5 HOH   43  543 206 HOH   HOH A . 
G 5 HOH   44  544 262 HOH   HOH A . 
G 5 HOH   45  545 53  HOH   HOH A . 
G 5 HOH   46  546 109 HOH   HOH A . 
G 5 HOH   47  547 156 HOH   HOH A . 
G 5 HOH   48  548 159 HOH   HOH A . 
G 5 HOH   49  549 15  HOH   HOH A . 
G 5 HOH   50  550 136 HOH   HOH A . 
G 5 HOH   51  551 244 HOH   HOH A . 
G 5 HOH   52  552 50  HOH   HOH A . 
G 5 HOH   53  553 120 HOH   HOH A . 
G 5 HOH   54  554 36  HOH   HOH A . 
G 5 HOH   55  555 117 HOH   HOH A . 
G 5 HOH   56  556 51  HOH   HOH A . 
G 5 HOH   57  557 24  HOH   HOH A . 
G 5 HOH   58  558 259 HOH   HOH A . 
G 5 HOH   59  559 207 HOH   HOH A . 
G 5 HOH   60  560 279 HOH   HOH A . 
G 5 HOH   61  561 175 HOH   HOH A . 
G 5 HOH   62  562 65  HOH   HOH A . 
G 5 HOH   63  563 27  HOH   HOH A . 
G 5 HOH   64  564 180 HOH   HOH A . 
G 5 HOH   65  565 353 HOH   HOH A . 
G 5 HOH   66  566 74  HOH   HOH A . 
G 5 HOH   67  567 240 HOH   HOH A . 
G 5 HOH   68  568 174 HOH   HOH A . 
G 5 HOH   69  569 47  HOH   HOH A . 
G 5 HOH   70  570 187 HOH   HOH A . 
G 5 HOH   71  571 325 HOH   HOH A . 
G 5 HOH   72  572 111 HOH   HOH A . 
G 5 HOH   73  573 198 HOH   HOH A . 
G 5 HOH   74  574 60  HOH   HOH A . 
G 5 HOH   75  575 126 HOH   HOH A . 
G 5 HOH   76  576 121 HOH   HOH A . 
G 5 HOH   77  577 303 HOH   HOH A . 
G 5 HOH   78  578 309 HOH   HOH A . 
G 5 HOH   79  579 71  HOH   HOH A . 
G 5 HOH   80  580 34  HOH   HOH A . 
G 5 HOH   81  581 173 HOH   HOH A . 
G 5 HOH   82  582 77  HOH   HOH A . 
G 5 HOH   83  583 44  HOH   HOH A . 
G 5 HOH   84  584 209 HOH   HOH A . 
G 5 HOH   85  585 201 HOH   HOH A . 
G 5 HOH   86  586 16  HOH   HOH A . 
G 5 HOH   87  587 293 HOH   HOH A . 
G 5 HOH   88  588 31  HOH   HOH A . 
G 5 HOH   89  589 43  HOH   HOH A . 
G 5 HOH   90  590 257 HOH   HOH A . 
G 5 HOH   91  591 191 HOH   HOH A . 
G 5 HOH   92  592 37  HOH   HOH A . 
G 5 HOH   93  593 40  HOH   HOH A . 
G 5 HOH   94  594 230 HOH   HOH A . 
G 5 HOH   95  595 330 HOH   HOH A . 
G 5 HOH   96  596 170 HOH   HOH A . 
G 5 HOH   97  597 66  HOH   HOH A . 
G 5 HOH   98  598 308 HOH   HOH A . 
G 5 HOH   99  599 285 HOH   HOH A . 
G 5 HOH   100 600 184 HOH   HOH A . 
G 5 HOH   101 601 189 HOH   HOH A . 
G 5 HOH   102 602 143 HOH   HOH A . 
G 5 HOH   103 603 119 HOH   HOH A . 
G 5 HOH   104 604 286 HOH   HOH A . 
G 5 HOH   105 605 116 HOH   HOH A . 
G 5 HOH   106 606 84  HOH   HOH A . 
G 5 HOH   107 607 304 HOH   HOH A . 
G 5 HOH   108 608 183 HOH   HOH A . 
G 5 HOH   109 609 278 HOH   HOH A . 
G 5 HOH   110 610 85  HOH   HOH A . 
G 5 HOH   111 611 226 HOH   HOH A . 
G 5 HOH   112 612 42  HOH   HOH A . 
G 5 HOH   113 613 80  HOH   HOH A . 
G 5 HOH   114 614 210 HOH   HOH A . 
G 5 HOH   115 615 45  HOH   HOH A . 
G 5 HOH   116 616 129 HOH   HOH A . 
G 5 HOH   117 617 222 HOH   HOH A . 
G 5 HOH   118 618 21  HOH   HOH A . 
G 5 HOH   119 619 142 HOH   HOH A . 
G 5 HOH   120 620 217 HOH   HOH A . 
G 5 HOH   121 621 171 HOH   HOH A . 
G 5 HOH   122 622 272 HOH   HOH A . 
G 5 HOH   123 623 25  HOH   HOH A . 
G 5 HOH   124 624 284 HOH   HOH A . 
G 5 HOH   125 625 30  HOH   HOH A . 
G 5 HOH   126 626 167 HOH   HOH A . 
G 5 HOH   127 627 168 HOH   HOH A . 
G 5 HOH   128 628 405 HOH   HOH A . 
G 5 HOH   129 629 91  HOH   HOH A . 
G 5 HOH   130 630 78  HOH   HOH A . 
G 5 HOH   131 631 73  HOH   HOH A . 
G 5 HOH   132 632 281 HOH   HOH A . 
G 5 HOH   133 633 62  HOH   HOH A . 
G 5 HOH   134 634 82  HOH   HOH A . 
G 5 HOH   135 635 276 HOH   HOH A . 
G 5 HOH   136 636 132 HOH   HOH A . 
G 5 HOH   137 637 332 HOH   HOH A . 
G 5 HOH   138 638 70  HOH   HOH A . 
G 5 HOH   139 639 87  HOH   HOH A . 
G 5 HOH   140 640 32  HOH   HOH A . 
G 5 HOH   141 641 311 HOH   HOH A . 
G 5 HOH   142 642 319 HOH   HOH A . 
G 5 HOH   143 643 216 HOH   HOH A . 
G 5 HOH   144 644 176 HOH   HOH A . 
G 5 HOH   145 645 110 HOH   HOH A . 
G 5 HOH   146 646 270 HOH   HOH A . 
G 5 HOH   147 647 122 HOH   HOH A . 
G 5 HOH   148 648 64  HOH   HOH A . 
G 5 HOH   149 649 310 HOH   HOH A . 
G 5 HOH   150 650 261 HOH   HOH A . 
G 5 HOH   151 651 231 HOH   HOH A . 
G 5 HOH   152 652 46  HOH   HOH A . 
G 5 HOH   153 653 95  HOH   HOH A . 
G 5 HOH   154 654 106 HOH   HOH A . 
G 5 HOH   155 655 337 HOH   HOH A . 
G 5 HOH   156 656 199 HOH   HOH A . 
G 5 HOH   157 657 26  HOH   HOH A . 
G 5 HOH   158 658 345 HOH   HOH A . 
G 5 HOH   159 659 48  HOH   HOH A . 
G 5 HOH   160 660 193 HOH   HOH A . 
G 5 HOH   161 661 115 HOH   HOH A . 
G 5 HOH   162 662 38  HOH   HOH A . 
G 5 HOH   163 663 17  HOH   HOH A . 
G 5 HOH   164 664 75  HOH   HOH A . 
G 5 HOH   165 665 196 HOH   HOH A . 
G 5 HOH   166 666 141 HOH   HOH A . 
G 5 HOH   167 667 313 HOH   HOH A . 
G 5 HOH   168 668 383 HOH   HOH A . 
G 5 HOH   169 669 194 HOH   HOH A . 
G 5 HOH   170 670 88  HOH   HOH A . 
G 5 HOH   171 671 342 HOH   HOH A . 
G 5 HOH   172 672 406 HOH   HOH A . 
G 5 HOH   173 673 52  HOH   HOH A . 
G 5 HOH   174 674 72  HOH   HOH A . 
G 5 HOH   175 675 291 HOH   HOH A . 
G 5 HOH   176 676 315 HOH   HOH A . 
G 5 HOH   177 677 157 HOH   HOH A . 
G 5 HOH   178 678 411 HOH   HOH A . 
G 5 HOH   179 679 354 HOH   HOH A . 
G 5 HOH   180 680 93  HOH   HOH A . 
G 5 HOH   181 681 130 HOH   HOH A . 
G 5 HOH   182 682 255 HOH   HOH A . 
G 5 HOH   183 683 103 HOH   HOH A . 
G 5 HOH   184 684 57  HOH   HOH A . 
G 5 HOH   185 685 114 HOH   HOH A . 
G 5 HOH   186 686 329 HOH   HOH A . 
G 5 HOH   187 687 101 HOH   HOH A . 
G 5 HOH   188 688 138 HOH   HOH A . 
G 5 HOH   189 689 227 HOH   HOH A . 
G 5 HOH   190 690 277 HOH   HOH A . 
G 5 HOH   191 691 212 HOH   HOH A . 
G 5 HOH   192 692 307 HOH   HOH A . 
G 5 HOH   193 693 147 HOH   HOH A . 
G 5 HOH   194 694 352 HOH   HOH A . 
G 5 HOH   195 695 160 HOH   HOH A . 
G 5 HOH   196 696 118 HOH   HOH A . 
G 5 HOH   197 697 100 HOH   HOH A . 
G 5 HOH   198 698 163 HOH   HOH A . 
G 5 HOH   199 699 339 HOH   HOH A . 
G 5 HOH   200 700 334 HOH   HOH A . 
G 5 HOH   201 701 331 HOH   HOH A . 
G 5 HOH   202 702 322 HOH   HOH A . 
G 5 HOH   203 703 356 HOH   HOH A . 
G 5 HOH   204 704 224 HOH   HOH A . 
G 5 HOH   205 705 333 HOH   HOH A . 
G 5 HOH   206 706 161 HOH   HOH A . 
G 5 HOH   207 707 312 HOH   HOH A . 
G 5 HOH   208 708 344 HOH   HOH A . 
G 5 HOH   209 709 253 HOH   HOH A . 
G 5 HOH   210 710 343 HOH   HOH A . 
G 5 HOH   211 711 384 HOH   HOH A . 
G 5 HOH   212 712 39  HOH   HOH A . 
G 5 HOH   213 713 338 HOH   HOH A . 
G 5 HOH   214 714 99  HOH   HOH A . 
G 5 HOH   215 715 125 HOH   HOH A . 
G 5 HOH   216 716 328 HOH   HOH A . 
G 5 HOH   217 717 233 HOH   HOH A . 
G 5 HOH   218 718 335 HOH   HOH A . 
G 5 HOH   219 719 89  HOH   HOH A . 
G 5 HOH   220 720 238 HOH   HOH A . 
G 5 HOH   221 721 409 HOH   HOH A . 
G 5 HOH   222 722 412 HOH   HOH A . 
G 5 HOH   223 723 172 HOH   HOH A . 
G 5 HOH   224 724 321 HOH   HOH A . 
G 5 HOH   225 725 336 HOH   HOH A . 
G 5 HOH   226 726 166 HOH   HOH A . 
G 5 HOH   227 727 81  HOH   HOH A . 
G 5 HOH   228 728 185 HOH   HOH A . 
G 5 HOH   229 729 351 HOH   HOH A . 
G 5 HOH   230 730 237 HOH   HOH A . 
G 5 HOH   231 731 181 HOH   HOH A . 
G 5 HOH   232 732 410 HOH   HOH A . 
G 5 HOH   233 733 408 HOH   HOH A . 
G 5 HOH   234 734 317 HOH   HOH A . 
G 5 HOH   235 735 300 HOH   HOH A . 
G 5 HOH   236 736 218 HOH   HOH A . 
G 5 HOH   237 737 346 HOH   HOH A . 
G 5 HOH   238 738 326 HOH   HOH A . 
G 5 HOH   239 739 252 HOH   HOH A . 
G 5 HOH   240 740 165 HOH   HOH A . 
G 5 HOH   241 741 350 HOH   HOH A . 
G 5 HOH   242 742 137 HOH   HOH A . 
G 5 HOH   243 743 249 HOH   HOH A . 
G 5 HOH   244 744 324 HOH   HOH A . 
G 5 HOH   245 745 382 HOH   HOH A . 
G 5 HOH   246 746 59  HOH   HOH A . 
G 5 HOH   247 747 145 HOH   HOH A . 
G 5 HOH   248 748 96  HOH   HOH A . 
G 5 HOH   249 749 316 HOH   HOH A . 
G 5 HOH   250 750 179 HOH   HOH A . 
G 5 HOH   251 751 144 HOH   HOH A . 
G 5 HOH   252 752 349 HOH   HOH A . 
G 5 HOH   253 753 104 HOH   HOH A . 
G 5 HOH   254 754 90  HOH   HOH A . 
G 5 HOH   255 755 407 HOH   HOH A . 
G 5 HOH   256 756 347 HOH   HOH A . 
G 5 HOH   257 757 146 HOH   HOH A . 
G 5 HOH   258 758 164 HOH   HOH A . 
G 5 HOH   259 759 250 HOH   HOH A . 
G 5 HOH   260 760 124 HOH   HOH A . 
H 5 HOH   1   501 152 HOH   HOH B . 
H 5 HOH   2   502 221 HOH   HOH B . 
H 5 HOH   3   503 389 HOH   HOH B . 
H 5 HOH   4   504 375 HOH   HOH B . 
H 5 HOH   5   505 390 HOH   HOH B . 
H 5 HOH   6   506 215 HOH   HOH B . 
H 5 HOH   7   507 359 HOH   HOH B . 
H 5 HOH   8   508 2   HOH   HOH B . 
H 5 HOH   9   509 258 HOH   HOH B . 
H 5 HOH   10  510 260 HOH   HOH B . 
H 5 HOH   11  511 267 HOH   HOH B . 
H 5 HOH   12  512 10  HOH   HOH B . 
H 5 HOH   13  513 387 HOH   HOH B . 
H 5 HOH   14  514 398 HOH   HOH B . 
H 5 HOH   15  515 5   HOH   HOH B . 
H 5 HOH   16  516 271 HOH   HOH B . 
H 5 HOH   17  517 370 HOH   HOH B . 
H 5 HOH   18  518 400 HOH   HOH B . 
H 5 HOH   19  519 296 HOH   HOH B . 
H 5 HOH   20  520 28  HOH   HOH B . 
H 5 HOH   21  521 86  HOH   HOH B . 
H 5 HOH   22  522 150 HOH   HOH B . 
H 5 HOH   23  523 360 HOH   HOH B . 
H 5 HOH   24  524 190 HOH   HOH B . 
H 5 HOH   25  525 23  HOH   HOH B . 
H 5 HOH   26  526 79  HOH   HOH B . 
H 5 HOH   27  527 378 HOH   HOH B . 
H 5 HOH   28  528 385 HOH   HOH B . 
H 5 HOH   29  529 11  HOH   HOH B . 
H 5 HOH   30  530 49  HOH   HOH B . 
H 5 HOH   31  531 365 HOH   HOH B . 
H 5 HOH   32  532 367 HOH   HOH B . 
H 5 HOH   33  533 200 HOH   HOH B . 
H 5 HOH   34  534 301 HOH   HOH B . 
H 5 HOH   35  535 358 HOH   HOH B . 
H 5 HOH   36  536 397 HOH   HOH B . 
H 5 HOH   37  537 8   HOH   HOH B . 
H 5 HOH   38  538 265 HOH   HOH B . 
H 5 HOH   39  539 399 HOH   HOH B . 
H 5 HOH   40  540 371 HOH   HOH B . 
H 5 HOH   41  541 391 HOH   HOH B . 
H 5 HOH   42  542 372 HOH   HOH B . 
H 5 HOH   43  543 7   HOH   HOH B . 
H 5 HOH   44  544 151 HOH   HOH B . 
H 5 HOH   45  545 402 HOH   HOH B . 
H 5 HOH   46  546 13  HOH   HOH B . 
H 5 HOH   47  547 245 HOH   HOH B . 
H 5 HOH   48  548 1   HOH   HOH B . 
H 5 HOH   49  549 386 HOH   HOH B . 
H 5 HOH   50  550 292 HOH   HOH B . 
H 5 HOH   51  551 58  HOH   HOH B . 
H 5 HOH   52  552 12  HOH   HOH B . 
H 5 HOH   53  553 396 HOH   HOH B . 
H 5 HOH   54  554 105 HOH   HOH B . 
H 5 HOH   55  555 302 HOH   HOH B . 
H 5 HOH   56  556 204 HOH   HOH B . 
H 5 HOH   57  557 235 HOH   HOH B . 
H 5 HOH   58  558 19  HOH   HOH B . 
H 5 HOH   59  559 379 HOH   HOH B . 
H 5 HOH   60  560 248 HOH   HOH B . 
H 5 HOH   61  561 394 HOH   HOH B . 
H 5 HOH   62  562 20  HOH   HOH B . 
H 5 HOH   63  563 134 HOH   HOH B . 
H 5 HOH   64  564 393 HOH   HOH B . 
H 5 HOH   65  565 54  HOH   HOH B . 
H 5 HOH   66  566 392 HOH   HOH B . 
H 5 HOH   67  567 76  HOH   HOH B . 
H 5 HOH   68  568 287 HOH   HOH B . 
H 5 HOH   69  569 149 HOH   HOH B . 
H 5 HOH   70  570 112 HOH   HOH B . 
H 5 HOH   71  571 107 HOH   HOH B . 
H 5 HOH   72  572 264 HOH   HOH B . 
H 5 HOH   73  573 401 HOH   HOH B . 
H 5 HOH   74  574 148 HOH   HOH B . 
H 5 HOH   75  575 241 HOH   HOH B . 
H 5 HOH   76  576 113 HOH   HOH B . 
H 5 HOH   77  577 135 HOH   HOH B . 
H 5 HOH   78  578 388 HOH   HOH B . 
H 5 HOH   79  579 376 HOH   HOH B . 
H 5 HOH   80  580 131 HOH   HOH B . 
H 5 HOH   81  581 203 HOH   HOH B . 
H 5 HOH   82  582 404 HOH   HOH B . 
H 5 HOH   83  583 9   HOH   HOH B . 
H 5 HOH   84  584 381 HOH   HOH B . 
H 5 HOH   85  585 67  HOH   HOH B . 
H 5 HOH   86  586 274 HOH   HOH B . 
H 5 HOH   87  587 94  HOH   HOH B . 
H 5 HOH   88  588 63  HOH   HOH B . 
H 5 HOH   89  589 6   HOH   HOH B . 
H 5 HOH   90  590 97  HOH   HOH B . 
H 5 HOH   91  591 123 HOH   HOH B . 
H 5 HOH   92  592 273 HOH   HOH B . 
H 5 HOH   93  593 92  HOH   HOH B . 
H 5 HOH   94  594 214 HOH   HOH B . 
H 5 HOH   95  595 202 HOH   HOH B . 
H 5 HOH   96  596 68  HOH   HOH B . 
H 5 HOH   97  597 225 HOH   HOH B . 
H 5 HOH   98  598 154 HOH   HOH B . 
H 5 HOH   99  599 254 HOH   HOH B . 
H 5 HOH   100 600 178 HOH   HOH B . 
H 5 HOH   101 601 364 HOH   HOH B . 
H 5 HOH   102 602 108 HOH   HOH B . 
H 5 HOH   103 603 290 HOH   HOH B . 
H 5 HOH   104 604 242 HOH   HOH B . 
H 5 HOH   105 605 289 HOH   HOH B . 
H 5 HOH   106 606 14  HOH   HOH B . 
H 5 HOH   107 607 4   HOH   HOH B . 
H 5 HOH   108 608 239 HOH   HOH B . 
H 5 HOH   109 609 229 HOH   HOH B . 
H 5 HOH   110 610 153 HOH   HOH B . 
H 5 HOH   111 611 263 HOH   HOH B . 
H 5 HOH   112 612 377 HOH   HOH B . 
H 5 HOH   113 613 195 HOH   HOH B . 
H 5 HOH   114 614 374 HOH   HOH B . 
H 5 HOH   115 615 211 HOH   HOH B . 
H 5 HOH   116 616 380 HOH   HOH B . 
H 5 HOH   117 617 373 HOH   HOH B . 
H 5 HOH   118 618 298 HOH   HOH B . 
H 5 HOH   119 619 205 HOH   HOH B . 
H 5 HOH   120 620 283 HOH   HOH B . 
H 5 HOH   121 621 306 HOH   HOH B . 
H 5 HOH   122 622 363 HOH   HOH B . 
H 5 HOH   123 623 357 HOH   HOH B . 
H 5 HOH   124 624 403 HOH   HOH B . 
H 5 HOH   125 625 361 HOH   HOH B . 
H 5 HOH   126 626 395 HOH   HOH B . 
H 5 HOH   127 627 368 HOH   HOH B . 
H 5 HOH   128 628 3   HOH   HOH B . 
H 5 HOH   129 629 366 HOH   HOH B . 
H 5 HOH   130 630 314 HOH   HOH B . 
H 5 HOH   131 631 369 HOH   HOH B . 
H 5 HOH   132 632 275 HOH   HOH B . 
H 5 HOH   133 633 251 HOH   HOH B . 
H 5 HOH   134 634 362 HOH   HOH B . 
H 5 HOH   135 635 223 HOH   HOH 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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21.2_5419 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .           ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.48 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MTW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.994 
_cell.length_a_esd                 ? 
_cell.length_b                     183.065 
_cell.length_b_esd                 ? 
_cell.length_c                     50.451 
_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                         9MTW 
_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                   9MTW 
_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             2.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.81 
_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, SITTING 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    '0.2 M lithium chloride, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2023-11-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97946 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MTW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.6 
_reflns.d_resolution_low                               38.63 
_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                                     99666 
_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                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.080 
_reflns.pdbx_Rpim_I_all                                0.039 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.6 
_reflns_shell.d_res_low                                     1.63 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4852 
_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                               0.577 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.491 
_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                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MTW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             38.63 
_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                     99491 
_refine.ls_number_reflns_R_free                  4946 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.43 
_refine.ls_percent_reflns_R_free                 4.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1837 
_refine.ls_R_factor_R_free                       0.2069 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1825 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 19.87 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        38.63 
_refine_hist.number_atoms_solvent             395 
_refine_hist.number_atoms_total               6042 
_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        5573 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         74 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 5835 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.982  ? 7914 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 16.761 ? 2235 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.062  ? 868  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 1020 ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.60 1.62  . . 152 3024 94.00  . . . . 0.2745 . . . . . . . . . . . . . . . 0.2815 
'X-RAY DIFFRACTION' 1.62 1.64  . . 162 3156 99.00  . . . . 0.2456 . . . . . . . . . . . . . . . 0.2756 
'X-RAY DIFFRACTION' 1.64 1.66  . . 160 3214 99.00  . . . . 0.2328 . . . . . . . . . . . . . . . 0.2316 
'X-RAY DIFFRACTION' 1.66 1.68  . . 161 3136 99.00  . . . . 0.2266 . . . . . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 1.68 1.70  . . 173 3155 99.00  . . . . 0.2294 . . . . . . . . . . . . . . . 0.2437 
'X-RAY DIFFRACTION' 1.70 1.72  . . 172 3156 98.00  . . . . 0.2226 . . . . . . . . . . . . . . . 0.2334 
'X-RAY DIFFRACTION' 1.72 1.75  . . 151 3124 98.00  . . . . 0.2292 . . . . . . . . . . . . . . . 0.2780 
'X-RAY DIFFRACTION' 1.75 1.77  . . 172 3113 97.00  . . . . 0.2448 . . . . . . . . . . . . . . . 0.2809 
'X-RAY DIFFRACTION' 1.77 1.80  . . 191 3097 97.00  . . . . 0.2516 . . . . . . . . . . . . . . . 0.2755 
'X-RAY DIFFRACTION' 1.80 1.83  . . 188 2907 94.00  . . . . 0.2324 . . . . . . . . . . . . . . . 0.2464 
'X-RAY DIFFRACTION' 1.83 1.86  . . 173 3241 100.00 . . . . 0.2174 . . . . . . . . . . . . . . . 0.2484 
'X-RAY DIFFRACTION' 1.86 1.90  . . 180 3096 99.00  . . . . 0.2349 . . . . . . . . . . . . . . . 0.2950 
'X-RAY DIFFRACTION' 1.90 1.93  . . 160 3208 99.00  . . . . 0.1992 . . . . . . . . . . . . . . . 0.2405 
'X-RAY DIFFRACTION' 1.93 1.97  . . 169 3155 99.00  . . . . 0.1936 . . . . . . . . . . . . . . . 0.2268 
'X-RAY DIFFRACTION' 1.97 2.02  . . 146 3217 99.00  . . . . 0.1861 . . . . . . . . . . . . . . . 0.2178 
'X-RAY DIFFRACTION' 2.02 2.06  . . 169 3153 99.00  . . . . 0.1938 . . . . . . . . . . . . . . . 0.2138 
'X-RAY DIFFRACTION' 2.06 2.11  . . 139 3153 98.00  . . . . 0.1955 . . . . . . . . . . . . . . . 0.2257 
'X-RAY DIFFRACTION' 2.11 2.17  . . 153 3097 97.00  . . . . 0.1972 . . . . . . . . . . . . . . . 0.2560 
'X-RAY DIFFRACTION' 2.17 2.24  . . 167 3097 97.00  . . . . 0.1930 . . . . . . . . . . . . . . . 0.2085 
'X-RAY DIFFRACTION' 2.24 2.31  . . 144 3224 99.00  . . . . 0.1937 . . . . . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 2.31 2.39  . . 173 3196 99.00  . . . . 0.1898 . . . . . . . . . . . . . . . 0.2158 
'X-RAY DIFFRACTION' 2.39 2.49  . . 166 3149 100.00 . . . . 0.1814 . . . . . . . . . . . . . . . 0.1987 
'X-RAY DIFFRACTION' 2.49 2.60  . . 147 3198 99.00  . . . . 0.1847 . . . . . . . . . . . . . . . 0.2119 
'X-RAY DIFFRACTION' 2.60 2.74  . . 171 3182 99.00  . . . . 0.1931 . . . . . . . . . . . . . . . 0.2301 
'X-RAY DIFFRACTION' 2.74 2.91  . . 173 3118 98.00  . . . . 0.1905 . . . . . . . . . . . . . . . 0.2430 
'X-RAY DIFFRACTION' 2.91 3.13  . . 187 3188 100.00 . . . . 0.1882 . . . . . . . . . . . . . . . 0.2194 
'X-RAY DIFFRACTION' 3.13 3.45  . . 164 3197 99.00  . . . . 0.1831 . . . . . . . . . . . . . . . 0.2034 
'X-RAY DIFFRACTION' 3.45 3.94  . . 170 3191 99.00  . . . . 0.1666 . . . . . . . . . . . . . . . 0.1735 
'X-RAY DIFFRACTION' 3.95 4.97  . . 139 3171 98.00  . . . . 0.1339 . . . . . . . . . . . . . . . 0.1400 
'X-RAY DIFFRACTION' 4.97 38.63 . . 174 3232 99.00  . . . . 0.1445 . . . . . . . . . . . . . . . 0.1599 
# 
_struct.entry_id                     9MTW 
_struct.title                        'Crystal structure of ADC-1-ertapenem complex' 
_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        9MTW 
_struct_keywords.text            
'beta-lactamase, class C, ertapenem, acyl-enzyme complex, HYDROLASE, HYDROLASE-INHIBITOR, ANTIBIOTIC complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/INHIBITOR,ANTIBIOTIC 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 5 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9L4R5_ACIBA 
_struct_ref.pdbx_db_accession          Q9L4R5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GNTPKDQEIKKLVDQNFKPLLEKYDVPGMAVGVIQNNKKYEMYYGLQSVQDKKAVNSSTIFELGSVSKLFTATAGGYAKN
KGKISFDDTPGKYWKELKNTPIDQVNLLQLATYTSGNLALQFPDEVKTDQQVLTFFKDWKPKNSIGEYRQYSNPSIGLFG
KVVALSMNKPFDQVLEKTIFPALGLKHSYVNVPKTQMQNYAFGYNQENQPIRVNPGPLGAPAYGVKSTLPDMLSFIHANL
NPQKYPADIQRAINETHQGRYQVNTMYQALGWEEFSYPATLQTLLDSNSEQIVMKPNKVTAISKEPSVKMYHKTGSTNRF
GTYVVFIPKENIGLVMLTNKRIPNEERIKAAYAVLNAIKK
;
_struct_ref.pdbx_align_begin           24 
# 
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 9MTW A 1 ? 360 ? Q9L4R5 24 ? 383 ? 2 361 
2 1 9MTW B 1 ? 360 ? Q9L4R5 24 ? 383 ? 2 361 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 THR A 3   ? PHE A 17  ? THR A 4   PHE A 18  1 ? 15 
HELX_P HELX_P2  AA2 LYS A 18  ? ASP A 25  ? LYS A 19  ASP A 26  1 ? 8  
HELX_P HELX_P3  AA3 GLY A 64  ? VAL A 66  ? GLY A 65  VAL A 67  5 ? 3  
HELX_P HELX_P4  AA4 SER A 67  ? LYS A 81  ? SER A 68  LYS A 82  1 ? 15 
HELX_P HELX_P5  AA5 THR A 89  ? TYR A 93  ? THR A 90  TYR A 94  5 ? 5  
HELX_P HELX_P6  AA6 TRP A 94  ? LYS A 98  ? TRP A 95  LYS A 99  5 ? 5  
HELX_P HELX_P7  AA7 THR A 100 ? VAL A 105 ? THR A 101 VAL A 106 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 106 ? THR A 112 ? ASN A 107 THR A 113 1 ? 7  
HELX_P HELX_P9  AA9 THR A 128 ? TRP A 139 ? THR A 129 TRP A 140 1 ? 12 
HELX_P HELX_P10 AB1 SER A 152 ? MET A 167 ? SER A 153 MET A 168 1 ? 16 
HELX_P HELX_P11 AB2 PRO A 170 ? THR A 178 ? PRO A 171 THR A 179 1 ? 9  
HELX_P HELX_P12 AB3 THR A 178 ? LEU A 183 ? THR A 179 LEU A 184 1 ? 6  
HELX_P HELX_P13 AB4 PRO A 193 ? TYR A 200 ? PRO A 194 TYR A 201 5 ? 8  
HELX_P HELX_P14 AB5 GLY A 219 ? GLY A 224 ? GLY A 220 GLY A 225 1 ? 6  
HELX_P HELX_P15 AB6 THR A 228 ? ASN A 241 ? THR A 229 ASN A 242 1 ? 14 
HELX_P HELX_P16 AB7 PRO A 242 ? TYR A 245 ? PRO A 243 TYR A 246 5 ? 4  
HELX_P HELX_P17 AB8 PRO A 246 ? HIS A 257 ? PRO A 247 HIS A 258 1 ? 12 
HELX_P HELX_P18 AB9 THR A 280 ? SER A 287 ? THR A 281 SER A 288 1 ? 8  
HELX_P HELX_P19 AC1 SER A 289 ? LYS A 295 ? SER A 290 LYS A 296 1 ? 7  
HELX_P HELX_P20 AC2 PRO A 328 ? GLU A 330 ? PRO A 329 GLU A 331 5 ? 3  
HELX_P HELX_P21 AC3 PRO A 343 ? ILE A 358 ? PRO A 344 ILE A 359 1 ? 16 
HELX_P HELX_P22 AC4 THR B 3   ? PHE B 17  ? THR B 4   PHE B 18  1 ? 15 
HELX_P HELX_P23 AC5 PHE B 17  ? ASP B 25  ? PHE B 18  ASP B 26  1 ? 9  
HELX_P HELX_P24 AC6 VAL B 66  ? LYS B 81  ? VAL B 67  LYS B 82  1 ? 16 
HELX_P HELX_P25 AC7 THR B 89  ? TYR B 93  ? THR B 90  TYR B 94  5 ? 5  
HELX_P HELX_P26 AC8 TRP B 94  ? LYS B 98  ? TRP B 95  LYS B 99  5 ? 5  
HELX_P HELX_P27 AC9 THR B 100 ? VAL B 105 ? THR B 101 VAL B 106 5 ? 6  
HELX_P HELX_P28 AD1 ASN B 106 ? THR B 112 ? ASN B 107 THR B 113 1 ? 7  
HELX_P HELX_P29 AD2 THR B 128 ? TRP B 139 ? THR B 129 TRP B 140 1 ? 12 
HELX_P HELX_P30 AD3 SER B 152 ? MET B 167 ? SER B 153 MET B 168 1 ? 16 
HELX_P HELX_P31 AD4 PRO B 170 ? THR B 178 ? PRO B 171 THR B 179 1 ? 9  
HELX_P HELX_P32 AD5 THR B 178 ? LEU B 183 ? THR B 179 LEU B 184 1 ? 6  
HELX_P HELX_P33 AD6 PRO B 193 ? TYR B 200 ? PRO B 194 TYR B 201 5 ? 8  
HELX_P HELX_P34 AD7 GLY B 219 ? GLY B 224 ? GLY B 220 GLY B 225 1 ? 6  
HELX_P HELX_P35 AD8 THR B 228 ? ASN B 241 ? THR B 229 ASN B 242 1 ? 14 
HELX_P HELX_P36 AD9 PRO B 242 ? TYR B 245 ? PRO B 243 TYR B 246 5 ? 4  
HELX_P HELX_P37 AE1 PRO B 246 ? HIS B 257 ? PRO B 247 HIS B 258 1 ? 12 
HELX_P HELX_P38 AE2 THR B 280 ? SER B 287 ? THR B 281 SER B 288 1 ? 8  
HELX_P HELX_P39 AE3 SER B 289 ? LYS B 295 ? SER B 290 LYS B 296 1 ? 7  
HELX_P HELX_P40 AE4 PRO B 328 ? GLU B 330 ? PRO B 329 GLU B 331 5 ? 3  
HELX_P HELX_P41 AE5 PRO B 343 ? ILE B 358 ? PRO B 344 ILE B 359 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A SER 65 OG ? ? ? 1_555 C 1RG   . CAA ? ? A SER 66 A 1RG   401 1_555 ? ? ? ? ? ? ? 1.421 ? ? 
covale2 covale one  ? B SER 65 OG ? ? ? 1_555 E A1B93 . C7  ? ? B SER 66 B A1B93 401 1_555 ? ? ? ? ? ? ? 1.414 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 1RG   C . ? SER A 65 ? 1RG   A 401 ? 1_555 SER A 66 ? 1_555 CAA OG SER 2 1RG   None 'Covalent chemical modification' 
2 A1B93 E . ? SER B 65 ? A1B93 B 401 ? 1_555 SER B 66 ? 1_555 C7  OG SER 1 A1B93 None 'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 277 A . ? TYR 278 A PRO 278 A ? PRO 279 A 1 0.18 
2 TYR 277 B . ? TYR 278 B PRO 278 B ? PRO 279 B 1 0.43 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 8 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA5 7 8 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 53  ? ALA A 54  ? LYS A 54  ALA A 55  
AA1 2 LYS A 38  ? SER A 48  ? LYS A 39  SER A 49  
AA1 3 GLY A 28  ? GLN A 35  ? GLY A 29  GLN A 36  
AA1 4 ILE A 332 ? THR A 338 ? ILE A 333 THR A 339 
AA1 5 GLY A 321 ? ILE A 327 ? GLY A 322 ILE A 328 
AA1 6 LYS A 309 ? SER A 316 ? LYS A 310 SER A 317 
AA1 7 GLU A 273 ? SER A 276 ? GLU A 274 SER A 277 
AA1 8 MET A 266 ? GLN A 268 ? MET A 267 GLN A 269 
AA1 9 TYR A 261 ? VAL A 263 ? TYR A 262 VAL A 264 
AA2 1 PHE A 61  ? GLU A 62  ? PHE A 62  GLU A 63  
AA2 2 LYS A 226 ? SER A 227 ? LYS A 227 SER A 228 
AA3 1 TYR A 148 ? ARG A 149 ? TYR A 149 ARG A 150 
AA3 2 ASN A 297 ? LYS A 298 ? ASN A 298 LYS A 299 
AA4 1 GLY A 203 ? TYR A 204 ? GLY A 204 TYR A 205 
AA4 2 PRO A 210 ? ILE A 211 ? PRO A 211 ILE A 212 
AA5 1 LYS B 38  ? GLY B 45  ? LYS B 39  GLY B 46  
AA5 2 GLY B 28  ? GLN B 35  ? GLY B 29  GLN B 36  
AA5 3 ILE B 332 ? THR B 338 ? ILE B 333 THR B 339 
AA5 4 GLY B 321 ? ILE B 327 ? GLY B 322 ILE B 328 
AA5 5 LYS B 309 ? SER B 316 ? LYS B 310 SER B 317 
AA5 6 GLU B 273 ? SER B 276 ? GLU B 274 SER B 277 
AA5 7 MET B 266 ? GLN B 268 ? MET B 267 GLN B 269 
AA5 8 TYR B 261 ? VAL B 263 ? TYR B 262 VAL B 264 
AA6 1 PHE B 61  ? GLU B 62  ? PHE B 62  GLU B 63  
AA6 2 LYS B 226 ? SER B 227 ? LYS B 227 SER B 228 
AA7 1 TYR B 148 ? ARG B 149 ? TYR B 149 ARG B 150 
AA7 2 ASN B 297 ? LYS B 298 ? ASN B 298 LYS B 299 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LYS A 53  ? O LYS A 54  N GLN A 47  ? N GLN A 48  
AA1 2 3 O TYR A 44  ? O TYR A 45  N MET A 29  ? N MET A 30  
AA1 3 4 N ALA A 30  ? N ALA A 31  O LEU A 337 ? O LEU A 338 
AA1 4 5 O ILE A 332 ? O ILE A 333 N ILE A 327 ? N ILE A 328 
AA1 5 6 O PHE A 326 ? O PHE A 327 N TYR A 311 ? N TYR A 312 
AA1 6 7 O MET A 310 ? O MET A 311 N PHE A 275 ? N PHE A 276 
AA1 7 8 O GLU A 274 ? O GLU A 275 N TYR A 267 ? N TYR A 268 
AA1 8 9 O MET A 266 ? O MET A 267 N VAL A 263 ? N VAL A 264 
AA2 1 2 N PHE A 61  ? N PHE A 62  O SER A 227 ? O SER A 228 
AA3 1 2 N ARG A 149 ? N ARG A 150 O ASN A 297 ? O ASN A 298 
AA4 1 2 N GLY A 203 ? N GLY A 204 O ILE A 211 ? O ILE A 212 
AA5 1 2 O MET B 42  ? O MET B 43  N VAL B 31  ? N VAL B 32  
AA5 2 3 N ALA B 30  ? N ALA B 31  O LEU B 337 ? O LEU B 338 
AA5 3 4 O ILE B 332 ? O ILE B 333 N ILE B 327 ? N ILE B 328 
AA5 4 5 O THR B 322 ? O THR B 323 N GLY B 315 ? N GLY B 316 
AA5 5 6 O MET B 310 ? O MET B 311 N PHE B 275 ? N PHE B 276 
AA5 6 7 O GLU B 274 ? O GLU B 275 N TYR B 267 ? N TYR B 268 
AA5 7 8 O MET B 266 ? O MET B 267 N VAL B 263 ? N VAL B 264 
AA6 1 2 N PHE B 61  ? N PHE B 62  O SER B 227 ? O SER B 228 
AA7 1 2 N ARG B 149 ? N ARG B 150 O ASN B 297 ? O ASN B 298 
# 
_pdbx_entry_details.entry_id                   9MTW 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    66 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OAC 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   1RG 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.67 
# 
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 118 ? ? -162.36 51.10   
2  1 LYS A 143 ? ? -127.96 -82.12  
3  1 HIS A 188 ? ? -140.72 45.38   
4  1 TYR A 224 ? ? -155.88 14.38   
5  1 ASN A 265 ? ? 54.29   -118.21 
6  1 SER A 304 ? ? -66.74  -71.76  
7  1 ASN B 118 ? ? -159.51 51.46   
8  1 LYS B 128 ? ? -122.35 -60.58  
9  1 LYS B 143 ? ? -122.39 -75.75  
10 1 HIS B 188 ? ? -142.68 46.23   
11 1 TYR B 224 ? ? -159.63 17.87   
12 1 ASN B 265 ? ? 54.65   -127.57 
13 1 THR B 318 ? ? -119.64 -166.26 
# 
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 13.2780 -8.4235  11.6112 0.2600 ? 0.0316  ? 0.0329  ? 0.1976 ? 0.0139  ? 0.2223 ? 0.8978 ? -0.6115 
? 0.4422  ? 1.0757 ? -0.0009 ? 0.6808 ? -0.0959 ? -0.1438 ? 0.1826  ? 0.3132  ? 0.0078  ? 0.1786  ? -0.3585 ? -0.0990 ? -0.0065 ? 
2 'X-RAY DIFFRACTION' ? refined 23.5278 -28.3548 -8.1662 0.1289 ? -0.0010 ? -0.0166 ? 0.1621 ? 0.0194  ? 0.1132 ? 1.2963 ? -0.1755 
? -0.0641 ? 0.7869 ? -0.0238 ? 0.9174 ? -0.0107 ? 0.0688  ? 0.0050  ? -0.1141 ? 0.0347  ? 0.0389  ? -0.0313 ? -0.0517 ? 0.0007  ? 
3 'X-RAY DIFFRACTION' ? refined 21.3284 -24.9703 8.9669  0.1339 ? -0.0075 ? 0.0064  ? 0.1801 ? 0.0231  ? 0.1285 ? 1.0339 ? -0.1401 
? 0.2214  ? 0.9766 ? -0.0636 ? 1.2025 ? 0.0080  ? -0.0617 ? 0.0281  ? 0.0749  ? -0.0056 ? -0.0188 ? -0.0729 ? 0.0016  ? -0.0005 ? 
4 'X-RAY DIFFRACTION' ? refined 6.4379  9.6770   -5.1117 0.3638 ? 0.0299  ? -0.0098 ? 0.2823 ? -0.0260 ? 0.4135 ? 0.5352 ? -0.1695 
? -0.1950 ? 0.2268 ? -0.1306 ? 0.2870 ? 0.2538  ? 0.4005  ? -0.5572 ? -0.4904 ? -0.1612 ? -0.3853 ? 0.4595  ? 0.0137  ? 0.0030  ? 
5 'X-RAY DIFFRACTION' ? refined 2.6381  7.9744   5.7822  0.2330 ? 0.0009  ? -0.0487 ? 0.1899 ? 0.0126  ? 0.3525 ? 0.3479 ? -0.1668 
? -0.3994 ? 0.9404 ? 0.2399  ? 0.5827 ? -0.0486 ? 0.0170  ? -0.2969 ? 0.0089  ? 0.0162  ? 0.1771  ? 0.1208  ? -0.0061 ? 0.0002  ? 
6 'X-RAY DIFFRACTION' ? refined -5.1250 36.3644  21.5875 0.6430 ? -0.0871 ? 0.1204  ? 0.2440 ? -0.0088 ? 0.2288 ? 0.0750 ? 0.2008  
? -0.0946 ? 1.6739 ? -0.1790 ? 0.1503 ? 0.1298  ? -0.3228 ? 0.0137  ? 1.4387  ? -0.2064 ? 0.1925  ? -0.0246 ? -0.0119 ? -0.0702 ? 
7 'X-RAY DIFFRACTION' ? refined -5.3339 15.4802  17.4124 0.4585 ? -0.0220 ? 0.0570  ? 0.2325 ? 0.0472  ? 0.3108 ? 0.6807 ? -0.1562 
? -0.3478 ? 1.1585 ? 0.3853  ? 0.2852 ? -0.1472 ? -0.1878 ? -0.2434 ? 0.9290  ? -0.0041 ? 0.3154  ? 0.0895  ? 0.0941  ? -0.0109 ? 
8 'X-RAY DIFFRACTION' ? refined -6.8940 32.2071  2.7631  0.1898 ? 0.0108  ? -0.0067 ? 0.2074 ? -0.0073 ? 0.2650 ? 0.4976 ? -0.9421 
? -0.2146 ? 2.1041 ? 0.3442  ? 0.5156 ? 0.0668  ? 0.0315  ? 0.0081  ? -0.1701 ? -0.1153 ? 0.2495  ? -0.1012 ? -0.1017 ? -0.0036 ? 
9 'X-RAY DIFFRACTION' ? refined 1.9653  20.8046  0.4391  0.1744 ? 0.0067  ? -0.0134 ? 0.1818 ? 0.0095  ? 0.2362 ? 0.8208 ? -0.0466 
? -0.6780 ? 1.9514 ? 0.3126  ? 0.7570 ? 0.0829  ? 0.1050  ? -0.0464 ? -0.2517 ? -0.0853 ? -0.1177 ? 0.0065  ? -0.0173 ? 0.0000  ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 64 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 65 through 210 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 211 through 361 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 3 through 28 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 29 through 64 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 65 through 168 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 169 through 241 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 242 through 309 )
;
9 'X-RAY DIFFRACTION' 9 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 310 through 360 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       760 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.90 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 2   ? A GLY 1   
2  1 Y 1 A VAL 214 ? A VAL 213 
3  1 Y 1 A ASN 215 ? A ASN 214 
4  1 Y 1 B GLY 2   ? B GLY 1   
5  1 Y 1 B PHE 203 ? B PHE 202 
6  1 Y 1 B GLY 204 ? B GLY 203 
7  1 Y 1 B TYR 205 ? B TYR 204 
8  1 Y 1 B ASN 206 ? B ASN 205 
9  1 Y 1 B GLN 207 ? B GLN 206 
10 1 Y 1 B GLU 208 ? B GLU 207 
11 1 Y 1 B ASN 209 ? B ASN 208 
12 1 Y 1 B GLN 210 ? B GLN 209 
13 1 Y 1 B PRO 211 ? B PRO 210 
14 1 Y 1 B ILE 212 ? B ILE 211 
15 1 Y 1 B ARG 213 ? B ARG 212 
16 1 Y 1 B VAL 214 ? B VAL 213 
17 1 Y 1 B ASN 215 ? B ASN 214 
18 1 Y 1 B PRO 216 ? B PRO 215 
19 1 Y 1 B LYS 361 ? B LYS 360 
# 
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 
1RG   C    C N N 1   
1RG   N    N N N 2   
1RG   O    O N N 3   
1RG   CA   C N S 4   
1RG   CB   C N N 5   
1RG   CD   C N N 6   
1RG   CG   C N S 7   
1RG   CAA  C N N 8   
1RG   CAB  C N S 9   
1RG   OAC  O N N 10  
1RG   CAD  C N S 11  
1RG   CAE  C N R 12  
1RG   CAF  C N N 13  
1RG   OAG  O N N 14  
1RG   CAH  C N R 15  
1RG   CAI  C N N 16  
1RG   NAJ  N N N 17  
1RG   SAK  S N N 18  
1RG   CAL  C N N 19  
1RG   CAM  C N N 20  
1RG   CAS  C N N 21  
1RG   OAT  O N N 22  
1RG   OAU  O N N 23  
1RG   NAX  N N N 24  
1RG   CAY  C Y N 25  
1RG   CAZ  C Y N 26  
1RG   CBA  C Y N 27  
1RG   CBB  C Y N 28  
1RG   CBC  C Y N 29  
1RG   CBD  C Y N 30  
1RG   CBE  C N N 31  
1RG   OBF  O N N 32  
1RG   OBG  O N N 33  
1RG   HN   H N N 34  
1RG   HA   H N N 35  
1RG   HB   H N N 36  
1RG   HBA  H N N 37  
1RG   HD   H N N 38  
1RG   HDA  H N N 39  
1RG   HG   H N N 40  
1RG   HAA  H N N 41  
1RG   HAB  H N N 42  
1RG   HAD  H N N 43  
1RG   HAE  H N N 44  
1RG   HAF  H N N 45  
1RG   HAFA H N N 46  
1RG   HAFB H N N 47  
1RG   HOAG H N N 48  
1RG   HAH  H N N 49  
1RG   HNAJ H N N 50  
1RG   HAS  H N N 51  
1RG   HASA H N N 52  
1RG   HASB H N N 53  
1RG   HNAX H N N 54  
1RG   HAZ  H N N 55  
1RG   HBB  H N N 56  
1RG   HBC  H N N 57  
1RG   HBD  H N N 58  
1RG   HOAU H N N 59  
1RG   HOBF H N N 60  
A1B93 C2   C N R 61  
A1B93 C5   C N S 62  
A1B93 C6   C N S 63  
A1B93 C1   C N R 64  
A1B93 C11  C N N 65  
A1B93 C3   C N N 66  
A1B93 C7   C N N 67  
A1B93 CD2  C Y N 68  
A1B93 CE2  C Y N 69  
A1B93 CE3  C Y N 70  
A1B93 CZ2  C Y N 71  
A1B93 CZ3  C Y N 72  
A1B93 CH2  C Y N 73  
A1B93 C1A  C N S 74  
A1B93 C2A  C N N 75  
A1B93 C31  C N N 76  
A1B93 C41  C N N 77  
A1B93 C4A  C N N 78  
A1B93 C5A  C N S 79  
A1B93 C61  C N R 80  
A1B93 C62  C N N 81  
A1B93 C6A  C N N 82  
A1B93 N3A  N N N 83  
A1B93 N4   N N N 84  
A1B93 N7A  N N N 85  
A1B93 O31  O N N 86  
A1B93 O32  O N N 87  
A1B93 O42  O N N 88  
A1B93 O43  O N N 89  
A1B93 O62  O N N 90  
A1B93 O6A  O N N 91  
A1B93 O7   O N N 92  
A1B93 S21  S N N 93  
A1B93 H1   H N N 94  
A1B93 H2   H N N 95  
A1B93 H3   H N N 96  
A1B93 H4   H N N 97  
A1B93 H5   H N N 98  
A1B93 H6   H N N 99  
A1B93 H7   H N N 100 
A1B93 H8   H N N 101 
A1B93 H10  H N N 102 
A1B93 H11  H N N 103 
A1B93 H12  H N N 104 
A1B93 H13  H N N 105 
A1B93 H14  H N N 106 
A1B93 H15  H N N 107 
A1B93 H16  H N N 108 
A1B93 H17  H N N 109 
A1B93 H18  H N N 110 
A1B93 H19  H N N 111 
A1B93 H20  H N N 112 
A1B93 H21  H N N 113 
A1B93 H22  H N N 114 
A1B93 H23  H N N 115 
A1B93 H24  H N N 116 
A1B93 H26  H N N 117 
A1B93 H27  H N N 118 
A1B93 H28  H N N 119 
A1B93 H29  H N N 120 
ALA   N    N N N 121 
ALA   CA   C N S 122 
ALA   C    C N N 123 
ALA   O    O N N 124 
ALA   CB   C N N 125 
ALA   OXT  O N N 126 
ALA   H    H N N 127 
ALA   H2   H N N 128 
ALA   HA   H N N 129 
ALA   HB1  H N N 130 
ALA   HB2  H N N 131 
ALA   HB3  H N N 132 
ALA   HXT  H N N 133 
ARG   N    N N N 134 
ARG   CA   C N S 135 
ARG   C    C N N 136 
ARG   O    O N N 137 
ARG   CB   C N N 138 
ARG   CG   C N N 139 
ARG   CD   C N N 140 
ARG   NE   N N N 141 
ARG   CZ   C N N 142 
ARG   NH1  N N N 143 
ARG   NH2  N N N 144 
ARG   OXT  O N N 145 
ARG   H    H N N 146 
ARG   H2   H N N 147 
ARG   HA   H N N 148 
ARG   HB2  H N N 149 
ARG   HB3  H N N 150 
ARG   HG2  H N N 151 
ARG   HG3  H N N 152 
ARG   HD2  H N N 153 
ARG   HD3  H N N 154 
ARG   HE   H N N 155 
ARG   HH11 H N N 156 
ARG   HH12 H N N 157 
ARG   HH21 H N N 158 
ARG   HH22 H N N 159 
ARG   HXT  H N N 160 
ASN   N    N N N 161 
ASN   CA   C N S 162 
ASN   C    C N N 163 
ASN   O    O N N 164 
ASN   CB   C N N 165 
ASN   CG   C N N 166 
ASN   OD1  O N N 167 
ASN   ND2  N N N 168 
ASN   OXT  O N N 169 
ASN   H    H N N 170 
ASN   H2   H N N 171 
ASN   HA   H N N 172 
ASN   HB2  H N N 173 
ASN   HB3  H N N 174 
ASN   HD21 H N N 175 
ASN   HD22 H N N 176 
ASN   HXT  H N N 177 
ASP   N    N N N 178 
ASP   CA   C N S 179 
ASP   C    C N N 180 
ASP   O    O N N 181 
ASP   CB   C N N 182 
ASP   CG   C N N 183 
ASP   OD1  O N N 184 
ASP   OD2  O N N 185 
ASP   OXT  O N N 186 
ASP   H    H N N 187 
ASP   H2   H N N 188 
ASP   HA   H N N 189 
ASP   HB2  H N N 190 
ASP   HB3  H N N 191 
ASP   HD2  H N N 192 
ASP   HXT  H N N 193 
EDO   C1   C N N 194 
EDO   O1   O N N 195 
EDO   C2   C N N 196 
EDO   O2   O N N 197 
EDO   H11  H N N 198 
EDO   H12  H N N 199 
EDO   HO1  H N N 200 
EDO   H21  H N N 201 
EDO   H22  H N N 202 
EDO   HO2  H N N 203 
GLN   N    N N N 204 
GLN   CA   C N S 205 
GLN   C    C N N 206 
GLN   O    O N N 207 
GLN   CB   C N N 208 
GLN   CG   C N N 209 
GLN   CD   C N N 210 
GLN   OE1  O N N 211 
GLN   NE2  N N N 212 
GLN   OXT  O N N 213 
GLN   H    H N N 214 
GLN   H2   H N N 215 
GLN   HA   H N N 216 
GLN   HB2  H N N 217 
GLN   HB3  H N N 218 
GLN   HG2  H N N 219 
GLN   HG3  H N N 220 
GLN   HE21 H N N 221 
GLN   HE22 H N N 222 
GLN   HXT  H N N 223 
GLU   N    N N N 224 
GLU   CA   C N S 225 
GLU   C    C N N 226 
GLU   O    O N N 227 
GLU   CB   C N N 228 
GLU   CG   C N N 229 
GLU   CD   C N N 230 
GLU   OE1  O N N 231 
GLU   OE2  O N N 232 
GLU   OXT  O N N 233 
GLU   H    H N N 234 
GLU   H2   H N N 235 
GLU   HA   H N N 236 
GLU   HB2  H N N 237 
GLU   HB3  H N N 238 
GLU   HG2  H N N 239 
GLU   HG3  H N N 240 
GLU   HE2  H N N 241 
GLU   HXT  H N N 242 
GLY   N    N N N 243 
GLY   CA   C N N 244 
GLY   C    C N N 245 
GLY   O    O N N 246 
GLY   OXT  O N N 247 
GLY   H    H N N 248 
GLY   H2   H N N 249 
GLY   HA2  H N N 250 
GLY   HA3  H N N 251 
GLY   HXT  H N N 252 
HIS   N    N N N 253 
HIS   CA   C N S 254 
HIS   C    C N N 255 
HIS   O    O N N 256 
HIS   CB   C N N 257 
HIS   CG   C Y N 258 
HIS   ND1  N Y N 259 
HIS   CD2  C Y N 260 
HIS   CE1  C Y N 261 
HIS   NE2  N Y N 262 
HIS   OXT  O N N 263 
HIS   H    H N N 264 
HIS   H2   H N N 265 
HIS   HA   H N N 266 
HIS   HB2  H N N 267 
HIS   HB3  H N N 268 
HIS   HD1  H N N 269 
HIS   HD2  H N N 270 
HIS   HE1  H N N 271 
HIS   HE2  H N N 272 
HIS   HXT  H N N 273 
HOH   O    O N N 274 
HOH   H1   H N N 275 
HOH   H2   H N N 276 
ILE   N    N N N 277 
ILE   CA   C N S 278 
ILE   C    C N N 279 
ILE   O    O N N 280 
ILE   CB   C N S 281 
ILE   CG1  C N N 282 
ILE   CG2  C N N 283 
ILE   CD1  C N N 284 
ILE   OXT  O N N 285 
ILE   H    H N N 286 
ILE   H2   H N N 287 
ILE   HA   H N N 288 
ILE   HB   H N N 289 
ILE   HG12 H N N 290 
ILE   HG13 H N N 291 
ILE   HG21 H N N 292 
ILE   HG22 H N N 293 
ILE   HG23 H N N 294 
ILE   HD11 H N N 295 
ILE   HD12 H N N 296 
ILE   HD13 H N N 297 
ILE   HXT  H N N 298 
LEU   N    N N N 299 
LEU   CA   C N S 300 
LEU   C    C N N 301 
LEU   O    O N N 302 
LEU   CB   C N N 303 
LEU   CG   C N N 304 
LEU   CD1  C N N 305 
LEU   CD2  C N N 306 
LEU   OXT  O N N 307 
LEU   H    H N N 308 
LEU   H2   H N N 309 
LEU   HA   H N N 310 
LEU   HB2  H N N 311 
LEU   HB3  H N N 312 
LEU   HG   H N N 313 
LEU   HD11 H N N 314 
LEU   HD12 H N N 315 
LEU   HD13 H N N 316 
LEU   HD21 H N N 317 
LEU   HD22 H N N 318 
LEU   HD23 H N N 319 
LEU   HXT  H N N 320 
LYS   N    N N N 321 
LYS   CA   C N S 322 
LYS   C    C N N 323 
LYS   O    O N N 324 
LYS   CB   C N N 325 
LYS   CG   C N N 326 
LYS   CD   C N N 327 
LYS   CE   C N N 328 
LYS   NZ   N N N 329 
LYS   OXT  O N N 330 
LYS   H    H N N 331 
LYS   H2   H N N 332 
LYS   HA   H N N 333 
LYS   HB2  H N N 334 
LYS   HB3  H N N 335 
LYS   HG2  H N N 336 
LYS   HG3  H N N 337 
LYS   HD2  H N N 338 
LYS   HD3  H N N 339 
LYS   HE2  H N N 340 
LYS   HE3  H N N 341 
LYS   HZ1  H N N 342 
LYS   HZ2  H N N 343 
LYS   HZ3  H N N 344 
LYS   HXT  H N N 345 
MET   N    N N N 346 
MET   CA   C N S 347 
MET   C    C N N 348 
MET   O    O N N 349 
MET   CB   C N N 350 
MET   CG   C N N 351 
MET   SD   S N N 352 
MET   CE   C N N 353 
MET   OXT  O N N 354 
MET   H    H N N 355 
MET   H2   H N N 356 
MET   HA   H N N 357 
MET   HB2  H N N 358 
MET   HB3  H N N 359 
MET   HG2  H N N 360 
MET   HG3  H N N 361 
MET   HE1  H N N 362 
MET   HE2  H N N 363 
MET   HE3  H N N 364 
MET   HXT  H N N 365 
PHE   N    N N N 366 
PHE   CA   C N S 367 
PHE   C    C N N 368 
PHE   O    O N N 369 
PHE   CB   C N N 370 
PHE   CG   C Y N 371 
PHE   CD1  C Y N 372 
PHE   CD2  C Y N 373 
PHE   CE1  C Y N 374 
PHE   CE2  C Y N 375 
PHE   CZ   C Y N 376 
PHE   OXT  O N N 377 
PHE   H    H N N 378 
PHE   H2   H N N 379 
PHE   HA   H N N 380 
PHE   HB2  H N N 381 
PHE   HB3  H N N 382 
PHE   HD1  H N N 383 
PHE   HD2  H N N 384 
PHE   HE1  H N N 385 
PHE   HE2  H N N 386 
PHE   HZ   H N N 387 
PHE   HXT  H N N 388 
PRO   N    N N N 389 
PRO   CA   C N S 390 
PRO   C    C N N 391 
PRO   O    O N N 392 
PRO   CB   C N N 393 
PRO   CG   C N N 394 
PRO   CD   C N N 395 
PRO   OXT  O N N 396 
PRO   H    H N N 397 
PRO   HA   H N N 398 
PRO   HB2  H N N 399 
PRO   HB3  H N N 400 
PRO   HG2  H N N 401 
PRO   HG3  H N N 402 
PRO   HD2  H N N 403 
PRO   HD3  H N N 404 
PRO   HXT  H N N 405 
SER   N    N N N 406 
SER   CA   C N S 407 
SER   C    C N N 408 
SER   O    O N N 409 
SER   CB   C N N 410 
SER   OG   O N N 411 
SER   OXT  O N N 412 
SER   H    H N N 413 
SER   H2   H N N 414 
SER   HA   H N N 415 
SER   HB2  H N N 416 
SER   HB3  H N N 417 
SER   HG   H N N 418 
SER   HXT  H N N 419 
THR   N    N N N 420 
THR   CA   C N S 421 
THR   C    C N N 422 
THR   O    O N N 423 
THR   CB   C N R 424 
THR   OG1  O N N 425 
THR   CG2  C N N 426 
THR   OXT  O N N 427 
THR   H    H N N 428 
THR   H2   H N N 429 
THR   HA   H N N 430 
THR   HB   H N N 431 
THR   HG1  H N N 432 
THR   HG21 H N N 433 
THR   HG22 H N N 434 
THR   HG23 H N N 435 
THR   HXT  H N N 436 
TRP   N    N N N 437 
TRP   CA   C N S 438 
TRP   C    C N N 439 
TRP   O    O N N 440 
TRP   CB   C N N 441 
TRP   CG   C Y N 442 
TRP   CD1  C Y N 443 
TRP   CD2  C Y N 444 
TRP   NE1  N Y N 445 
TRP   CE2  C Y N 446 
TRP   CE3  C Y N 447 
TRP   CZ2  C Y N 448 
TRP   CZ3  C Y N 449 
TRP   CH2  C Y N 450 
TRP   OXT  O N N 451 
TRP   H    H N N 452 
TRP   H2   H N N 453 
TRP   HA   H N N 454 
TRP   HB2  H N N 455 
TRP   HB3  H N N 456 
TRP   HD1  H N N 457 
TRP   HE1  H N N 458 
TRP   HE3  H N N 459 
TRP   HZ2  H N N 460 
TRP   HZ3  H N N 461 
TRP   HH2  H N N 462 
TRP   HXT  H N N 463 
TYR   N    N N N 464 
TYR   CA   C N S 465 
TYR   C    C N N 466 
TYR   O    O N N 467 
TYR   CB   C N N 468 
TYR   CG   C Y N 469 
TYR   CD1  C Y N 470 
TYR   CD2  C Y N 471 
TYR   CE1  C Y N 472 
TYR   CE2  C Y N 473 
TYR   CZ   C Y N 474 
TYR   OH   O N N 475 
TYR   OXT  O N N 476 
TYR   H    H N N 477 
TYR   H2   H N N 478 
TYR   HA   H N N 479 
TYR   HB2  H N N 480 
TYR   HB3  H N N 481 
TYR   HD1  H N N 482 
TYR   HD2  H N N 483 
TYR   HE1  H N N 484 
TYR   HE2  H N N 485 
TYR   HH   H N N 486 
TYR   HXT  H N N 487 
VAL   N    N N N 488 
VAL   CA   C N S 489 
VAL   C    C N N 490 
VAL   O    O N N 491 
VAL   CB   C N N 492 
VAL   CG1  C N N 493 
VAL   CG2  C N N 494 
VAL   OXT  O N N 495 
VAL   H    H N N 496 
VAL   H2   H N N 497 
VAL   HA   H N N 498 
VAL   HB   H N N 499 
VAL   HG11 H N N 500 
VAL   HG12 H N N 501 
VAL   HG13 H N N 502 
VAL   HG21 H N N 503 
VAL   HG22 H N N 504 
VAL   HG23 H N N 505 
VAL   HXT  H N N 506 
# 
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 
1RG   C   O    doub N N 1   
1RG   C   CA   sing N N 2   
1RG   C   NAX  sing N N 3   
1RG   N   CA   sing N N 4   
1RG   N   CD   sing N N 5   
1RG   CA  CB   sing N N 6   
1RG   CB  CG   sing N N 7   
1RG   CD  CG   sing N N 8   
1RG   CG  SAK  sing N N 9   
1RG   CAA CAB  sing N N 10  
1RG   CAA OAC  doub N N 11  
1RG   CAB CAD  sing N N 12  
1RG   CAB CAE  sing N N 13  
1RG   CAD CAH  sing N N 14  
1RG   CAD NAJ  sing N N 15  
1RG   CAE CAF  sing N N 16  
1RG   CAE OAG  sing N N 17  
1RG   CAH CAI  sing N N 18  
1RG   CAH CAS  sing N N 19  
1RG   CAI SAK  sing N N 20  
1RG   CAI CAL  doub N N 21  
1RG   NAJ CAL  sing N N 22  
1RG   CAL CAM  sing N N 23  
1RG   CAM OAT  doub N N 24  
1RG   CAM OAU  sing N N 25  
1RG   NAX CAY  sing N N 26  
1RG   CAY CAZ  doub Y N 27  
1RG   CAY CBD  sing Y N 28  
1RG   CAZ CBA  sing Y N 29  
1RG   CBA CBB  doub Y N 30  
1RG   CBA CBE  sing N N 31  
1RG   CBB CBC  sing Y N 32  
1RG   CBC CBD  doub Y N 33  
1RG   CBE OBF  sing N N 34  
1RG   CBE OBG  doub N N 35  
1RG   N   HN   sing N N 36  
1RG   CA  HA   sing N N 37  
1RG   CB  HB   sing N N 38  
1RG   CB  HBA  sing N N 39  
1RG   CD  HD   sing N N 40  
1RG   CD  HDA  sing N N 41  
1RG   CG  HG   sing N N 42  
1RG   CAA HAA  sing N N 43  
1RG   CAB HAB  sing N N 44  
1RG   CAD HAD  sing N N 45  
1RG   CAE HAE  sing N N 46  
1RG   CAF HAF  sing N N 47  
1RG   CAF HAFA sing N N 48  
1RG   CAF HAFB sing N N 49  
1RG   OAG HOAG sing N N 50  
1RG   CAH HAH  sing N N 51  
1RG   NAJ HNAJ sing N N 52  
1RG   CAS HAS  sing N N 53  
1RG   CAS HASA sing N N 54  
1RG   CAS HASB sing N N 55  
1RG   NAX HNAX sing N N 56  
1RG   CAZ HAZ  sing N N 57  
1RG   CBB HBB  sing N N 58  
1RG   CBC HBC  sing N N 59  
1RG   CBD HBD  sing N N 60  
1RG   OAU HOAU sing N N 61  
1RG   OBF HOBF sing N N 62  
A1B93 O32 C31  doub N N 63  
A1B93 O31 C31  sing N N 64  
A1B93 C31 C3   sing N N 65  
A1B93 C2A C1A  sing N N 66  
A1B93 C2A N3A  sing N N 67  
A1B93 C1A C4A  sing N N 68  
A1B93 C1A S21  sing N N 69  
A1B93 N3A C5A  sing N N 70  
A1B93 C4A C5A  sing N N 71  
A1B93 C3  C2   sing N N 72  
A1B93 C3  N4   doub N N 73  
A1B93 C5A C6A  sing N N 74  
A1B93 S21 C2   sing N N 75  
A1B93 C2  C1   sing N N 76  
A1B93 N4  C5   sing N N 77  
A1B93 O7  C7   doub N N 78  
A1B93 C6A N7A  sing N N 79  
A1B93 C6A O6A  doub N N 80  
A1B93 C1  C5   sing N N 81  
A1B93 C1  C11  sing N N 82  
A1B93 C5  C6   sing N N 83  
A1B93 N7A CD2  sing N N 84  
A1B93 C7  C6   sing N N 85  
A1B93 C6  C61  sing N N 86  
A1B93 CD2 CE2  doub Y N 87  
A1B93 CD2 CE3  sing Y N 88  
A1B93 CE2 CZ2  sing Y N 89  
A1B93 C61 O62  sing N N 90  
A1B93 C61 C62  sing N N 91  
A1B93 CE3 CZ3  doub Y N 92  
A1B93 CZ2 CH2  doub Y N 93  
A1B93 CZ3 CH2  sing Y N 94  
A1B93 CZ3 C41  sing N N 95  
A1B93 O43 C41  doub N N 96  
A1B93 C41 O42  sing N N 97  
A1B93 C2  H1   sing N N 98  
A1B93 C5  H2   sing N N 99  
A1B93 C6  H3   sing N N 100 
A1B93 C1  H4   sing N N 101 
A1B93 C11 H5   sing N N 102 
A1B93 C11 H6   sing N N 103 
A1B93 C11 H7   sing N N 104 
A1B93 C7  H8   sing N N 105 
A1B93 CE2 H10  sing N N 106 
A1B93 CE3 H11  sing N N 107 
A1B93 CZ2 H12  sing N N 108 
A1B93 CH2 H13  sing N N 109 
A1B93 C1A H14  sing N N 110 
A1B93 C2A H15  sing N N 111 
A1B93 C2A H16  sing N N 112 
A1B93 C4A H17  sing N N 113 
A1B93 C4A H18  sing N N 114 
A1B93 C5A H19  sing N N 115 
A1B93 C61 H20  sing N N 116 
A1B93 C62 H21  sing N N 117 
A1B93 C62 H22  sing N N 118 
A1B93 C62 H23  sing N N 119 
A1B93 N3A H24  sing N N 120 
A1B93 N7A H26  sing N N 121 
A1B93 O31 H27  sing N N 122 
A1B93 O42 H28  sing N N 123 
A1B93 O62 H29  sing N N 124 
ALA   N   CA   sing N N 125 
ALA   N   H    sing N N 126 
ALA   N   H2   sing N N 127 
ALA   CA  C    sing N N 128 
ALA   CA  CB   sing N N 129 
ALA   CA  HA   sing N N 130 
ALA   C   O    doub N N 131 
ALA   C   OXT  sing N N 132 
ALA   CB  HB1  sing N N 133 
ALA   CB  HB2  sing N N 134 
ALA   CB  HB3  sing N N 135 
ALA   OXT HXT  sing N N 136 
ARG   N   CA   sing N N 137 
ARG   N   H    sing N N 138 
ARG   N   H2   sing N N 139 
ARG   CA  C    sing N N 140 
ARG   CA  CB   sing N N 141 
ARG   CA  HA   sing N N 142 
ARG   C   O    doub N N 143 
ARG   C   OXT  sing N N 144 
ARG   CB  CG   sing N N 145 
ARG   CB  HB2  sing N N 146 
ARG   CB  HB3  sing N N 147 
ARG   CG  CD   sing N N 148 
ARG   CG  HG2  sing N N 149 
ARG   CG  HG3  sing N N 150 
ARG   CD  NE   sing N N 151 
ARG   CD  HD2  sing N N 152 
ARG   CD  HD3  sing N N 153 
ARG   NE  CZ   sing N N 154 
ARG   NE  HE   sing N N 155 
ARG   CZ  NH1  sing N N 156 
ARG   CZ  NH2  doub N N 157 
ARG   NH1 HH11 sing N N 158 
ARG   NH1 HH12 sing N N 159 
ARG   NH2 HH21 sing N N 160 
ARG   NH2 HH22 sing N N 161 
ARG   OXT HXT  sing N N 162 
ASN   N   CA   sing N N 163 
ASN   N   H    sing N N 164 
ASN   N   H2   sing N N 165 
ASN   CA  C    sing N N 166 
ASN   CA  CB   sing N N 167 
ASN   CA  HA   sing N N 168 
ASN   C   O    doub N N 169 
ASN   C   OXT  sing N N 170 
ASN   CB  CG   sing N N 171 
ASN   CB  HB2  sing N N 172 
ASN   CB  HB3  sing N N 173 
ASN   CG  OD1  doub N N 174 
ASN   CG  ND2  sing N N 175 
ASN   ND2 HD21 sing N N 176 
ASN   ND2 HD22 sing N N 177 
ASN   OXT HXT  sing N N 178 
ASP   N   CA   sing N N 179 
ASP   N   H    sing N N 180 
ASP   N   H2   sing N N 181 
ASP   CA  C    sing N N 182 
ASP   CA  CB   sing N N 183 
ASP   CA  HA   sing N N 184 
ASP   C   O    doub N N 185 
ASP   C   OXT  sing N N 186 
ASP   CB  CG   sing N N 187 
ASP   CB  HB2  sing N N 188 
ASP   CB  HB3  sing N N 189 
ASP   CG  OD1  doub N N 190 
ASP   CG  OD2  sing N N 191 
ASP   OD2 HD2  sing N N 192 
ASP   OXT HXT  sing N N 193 
EDO   C1  O1   sing N N 194 
EDO   C1  C2   sing N N 195 
EDO   C1  H11  sing N N 196 
EDO   C1  H12  sing N N 197 
EDO   O1  HO1  sing N N 198 
EDO   C2  O2   sing N N 199 
EDO   C2  H21  sing N N 200 
EDO   C2  H22  sing N N 201 
EDO   O2  HO2  sing N N 202 
GLN   N   CA   sing N N 203 
GLN   N   H    sing N N 204 
GLN   N   H2   sing N N 205 
GLN   CA  C    sing N N 206 
GLN   CA  CB   sing N N 207 
GLN   CA  HA   sing N N 208 
GLN   C   O    doub N N 209 
GLN   C   OXT  sing N N 210 
GLN   CB  CG   sing N N 211 
GLN   CB  HB2  sing N N 212 
GLN   CB  HB3  sing N N 213 
GLN   CG  CD   sing N N 214 
GLN   CG  HG2  sing N N 215 
GLN   CG  HG3  sing N N 216 
GLN   CD  OE1  doub N N 217 
GLN   CD  NE2  sing N N 218 
GLN   NE2 HE21 sing N N 219 
GLN   NE2 HE22 sing N N 220 
GLN   OXT HXT  sing N N 221 
GLU   N   CA   sing N N 222 
GLU   N   H    sing N N 223 
GLU   N   H2   sing N N 224 
GLU   CA  C    sing N N 225 
GLU   CA  CB   sing N N 226 
GLU   CA  HA   sing N N 227 
GLU   C   O    doub N N 228 
GLU   C   OXT  sing N N 229 
GLU   CB  CG   sing N N 230 
GLU   CB  HB2  sing N N 231 
GLU   CB  HB3  sing N N 232 
GLU   CG  CD   sing N N 233 
GLU   CG  HG2  sing N N 234 
GLU   CG  HG3  sing N N 235 
GLU   CD  OE1  doub N N 236 
GLU   CD  OE2  sing N N 237 
GLU   OE2 HE2  sing N N 238 
GLU   OXT HXT  sing N N 239 
GLY   N   CA   sing N N 240 
GLY   N   H    sing N N 241 
GLY   N   H2   sing N N 242 
GLY   CA  C    sing N N 243 
GLY   CA  HA2  sing N N 244 
GLY   CA  HA3  sing N N 245 
GLY   C   O    doub N N 246 
GLY   C   OXT  sing N N 247 
GLY   OXT HXT  sing N N 248 
HIS   N   CA   sing N N 249 
HIS   N   H    sing N N 250 
HIS   N   H2   sing N N 251 
HIS   CA  C    sing N N 252 
HIS   CA  CB   sing N N 253 
HIS   CA  HA   sing N N 254 
HIS   C   O    doub N N 255 
HIS   C   OXT  sing N N 256 
HIS   CB  CG   sing N N 257 
HIS   CB  HB2  sing N N 258 
HIS   CB  HB3  sing N N 259 
HIS   CG  ND1  sing Y N 260 
HIS   CG  CD2  doub Y N 261 
HIS   ND1 CE1  doub Y N 262 
HIS   ND1 HD1  sing N N 263 
HIS   CD2 NE2  sing Y N 264 
HIS   CD2 HD2  sing N N 265 
HIS   CE1 NE2  sing Y N 266 
HIS   CE1 HE1  sing N N 267 
HIS   NE2 HE2  sing N N 268 
HIS   OXT HXT  sing N N 269 
HOH   O   H1   sing N N 270 
HOH   O   H2   sing N N 271 
ILE   N   CA   sing N N 272 
ILE   N   H    sing N N 273 
ILE   N   H2   sing N N 274 
ILE   CA  C    sing N N 275 
ILE   CA  CB   sing N N 276 
ILE   CA  HA   sing N N 277 
ILE   C   O    doub N N 278 
ILE   C   OXT  sing N N 279 
ILE   CB  CG1  sing N N 280 
ILE   CB  CG2  sing N N 281 
ILE   CB  HB   sing N N 282 
ILE   CG1 CD1  sing N N 283 
ILE   CG1 HG12 sing N N 284 
ILE   CG1 HG13 sing N N 285 
ILE   CG2 HG21 sing N N 286 
ILE   CG2 HG22 sing N N 287 
ILE   CG2 HG23 sing N N 288 
ILE   CD1 HD11 sing N N 289 
ILE   CD1 HD12 sing N N 290 
ILE   CD1 HD13 sing N N 291 
ILE   OXT HXT  sing N N 292 
LEU   N   CA   sing N N 293 
LEU   N   H    sing N N 294 
LEU   N   H2   sing N N 295 
LEU   CA  C    sing N N 296 
LEU   CA  CB   sing N N 297 
LEU   CA  HA   sing N N 298 
LEU   C   O    doub N N 299 
LEU   C   OXT  sing N N 300 
LEU   CB  CG   sing N N 301 
LEU   CB  HB2  sing N N 302 
LEU   CB  HB3  sing N N 303 
LEU   CG  CD1  sing N N 304 
LEU   CG  CD2  sing N N 305 
LEU   CG  HG   sing N N 306 
LEU   CD1 HD11 sing N N 307 
LEU   CD1 HD12 sing N N 308 
LEU   CD1 HD13 sing N N 309 
LEU   CD2 HD21 sing N N 310 
LEU   CD2 HD22 sing N N 311 
LEU   CD2 HD23 sing N N 312 
LEU   OXT HXT  sing N N 313 
LYS   N   CA   sing N N 314 
LYS   N   H    sing N N 315 
LYS   N   H2   sing N N 316 
LYS   CA  C    sing N N 317 
LYS   CA  CB   sing N N 318 
LYS   CA  HA   sing N N 319 
LYS   C   O    doub N N 320 
LYS   C   OXT  sing N N 321 
LYS   CB  CG   sing N N 322 
LYS   CB  HB2  sing N N 323 
LYS   CB  HB3  sing N N 324 
LYS   CG  CD   sing N N 325 
LYS   CG  HG2  sing N N 326 
LYS   CG  HG3  sing N N 327 
LYS   CD  CE   sing N N 328 
LYS   CD  HD2  sing N N 329 
LYS   CD  HD3  sing N N 330 
LYS   CE  NZ   sing N N 331 
LYS   CE  HE2  sing N N 332 
LYS   CE  HE3  sing N N 333 
LYS   NZ  HZ1  sing N N 334 
LYS   NZ  HZ2  sing N N 335 
LYS   NZ  HZ3  sing N N 336 
LYS   OXT HXT  sing N N 337 
MET   N   CA   sing N N 338 
MET   N   H    sing N N 339 
MET   N   H2   sing N N 340 
MET   CA  C    sing N N 341 
MET   CA  CB   sing N N 342 
MET   CA  HA   sing N N 343 
MET   C   O    doub N N 344 
MET   C   OXT  sing N N 345 
MET   CB  CG   sing N N 346 
MET   CB  HB2  sing N N 347 
MET   CB  HB3  sing N N 348 
MET   CG  SD   sing N N 349 
MET   CG  HG2  sing N N 350 
MET   CG  HG3  sing N N 351 
MET   SD  CE   sing N N 352 
MET   CE  HE1  sing N N 353 
MET   CE  HE2  sing N N 354 
MET   CE  HE3  sing N N 355 
MET   OXT HXT  sing N N 356 
PHE   N   CA   sing N N 357 
PHE   N   H    sing N N 358 
PHE   N   H2   sing N N 359 
PHE   CA  C    sing N N 360 
PHE   CA  CB   sing N N 361 
PHE   CA  HA   sing N N 362 
PHE   C   O    doub N N 363 
PHE   C   OXT  sing N N 364 
PHE   CB  CG   sing N N 365 
PHE   CB  HB2  sing N N 366 
PHE   CB  HB3  sing N N 367 
PHE   CG  CD1  doub Y N 368 
PHE   CG  CD2  sing Y N 369 
PHE   CD1 CE1  sing Y N 370 
PHE   CD1 HD1  sing N N 371 
PHE   CD2 CE2  doub Y N 372 
PHE   CD2 HD2  sing N N 373 
PHE   CE1 CZ   doub Y N 374 
PHE   CE1 HE1  sing N N 375 
PHE   CE2 CZ   sing Y N 376 
PHE   CE2 HE2  sing N N 377 
PHE   CZ  HZ   sing N N 378 
PHE   OXT HXT  sing N N 379 
PRO   N   CA   sing N N 380 
PRO   N   CD   sing N N 381 
PRO   N   H    sing N N 382 
PRO   CA  C    sing N N 383 
PRO   CA  CB   sing N N 384 
PRO   CA  HA   sing N N 385 
PRO   C   O    doub N N 386 
PRO   C   OXT  sing N N 387 
PRO   CB  CG   sing N N 388 
PRO   CB  HB2  sing N N 389 
PRO   CB  HB3  sing N N 390 
PRO   CG  CD   sing N N 391 
PRO   CG  HG2  sing N N 392 
PRO   CG  HG3  sing N N 393 
PRO   CD  HD2  sing N N 394 
PRO   CD  HD3  sing N N 395 
PRO   OXT HXT  sing N N 396 
SER   N   CA   sing N N 397 
SER   N   H    sing N N 398 
SER   N   H2   sing N N 399 
SER   CA  C    sing N N 400 
SER   CA  CB   sing N N 401 
SER   CA  HA   sing N N 402 
SER   C   O    doub N N 403 
SER   C   OXT  sing N N 404 
SER   CB  OG   sing N N 405 
SER   CB  HB2  sing N N 406 
SER   CB  HB3  sing N N 407 
SER   OG  HG   sing N N 408 
SER   OXT HXT  sing N N 409 
THR   N   CA   sing N N 410 
THR   N   H    sing N N 411 
THR   N   H2   sing N N 412 
THR   CA  C    sing N N 413 
THR   CA  CB   sing N N 414 
THR   CA  HA   sing N N 415 
THR   C   O    doub N N 416 
THR   C   OXT  sing N N 417 
THR   CB  OG1  sing N N 418 
THR   CB  CG2  sing N N 419 
THR   CB  HB   sing N N 420 
THR   OG1 HG1  sing N N 421 
THR   CG2 HG21 sing N N 422 
THR   CG2 HG22 sing N N 423 
THR   CG2 HG23 sing N N 424 
THR   OXT HXT  sing N N 425 
TRP   N   CA   sing N N 426 
TRP   N   H    sing N N 427 
TRP   N   H2   sing N N 428 
TRP   CA  C    sing N N 429 
TRP   CA  CB   sing N N 430 
TRP   CA  HA   sing N N 431 
TRP   C   O    doub N N 432 
TRP   C   OXT  sing N N 433 
TRP   CB  CG   sing N N 434 
TRP   CB  HB2  sing N N 435 
TRP   CB  HB3  sing N N 436 
TRP   CG  CD1  doub Y N 437 
TRP   CG  CD2  sing Y N 438 
TRP   CD1 NE1  sing Y N 439 
TRP   CD1 HD1  sing N N 440 
TRP   CD2 CE2  doub Y N 441 
TRP   CD2 CE3  sing Y N 442 
TRP   NE1 CE2  sing Y N 443 
TRP   NE1 HE1  sing N N 444 
TRP   CE2 CZ2  sing Y N 445 
TRP   CE3 CZ3  doub Y N 446 
TRP   CE3 HE3  sing N N 447 
TRP   CZ2 CH2  doub Y N 448 
TRP   CZ2 HZ2  sing N N 449 
TRP   CZ3 CH2  sing Y N 450 
TRP   CZ3 HZ3  sing N N 451 
TRP   CH2 HH2  sing N N 452 
TRP   OXT HXT  sing N N 453 
TYR   N   CA   sing N N 454 
TYR   N   H    sing N N 455 
TYR   N   H2   sing N N 456 
TYR   CA  C    sing N N 457 
TYR   CA  CB   sing N N 458 
TYR   CA  HA   sing N N 459 
TYR   C   O    doub N N 460 
TYR   C   OXT  sing N N 461 
TYR   CB  CG   sing N N 462 
TYR   CB  HB2  sing N N 463 
TYR   CB  HB3  sing N N 464 
TYR   CG  CD1  doub Y N 465 
TYR   CG  CD2  sing Y N 466 
TYR   CD1 CE1  sing Y N 467 
TYR   CD1 HD1  sing N N 468 
TYR   CD2 CE2  doub Y N 469 
TYR   CD2 HD2  sing N N 470 
TYR   CE1 CZ   doub Y N 471 
TYR   CE1 HE1  sing N N 472 
TYR   CE2 CZ   sing Y N 473 
TYR   CE2 HE2  sing N N 474 
TYR   CZ  OH   sing N N 475 
TYR   OH  HH   sing N N 476 
TYR   OXT HXT  sing N N 477 
VAL   N   CA   sing N N 478 
VAL   N   H    sing N N 479 
VAL   N   H2   sing N N 480 
VAL   CA  C    sing N N 481 
VAL   CA  CB   sing N N 482 
VAL   CA  HA   sing N N 483 
VAL   C   O    doub N N 484 
VAL   C   OXT  sing N N 485 
VAL   CB  CG1  sing N N 486 
VAL   CB  CG2  sing N N 487 
VAL   CB  HB   sing N N 488 
VAL   CG1 HG11 sing N N 489 
VAL   CG1 HG12 sing N N 490 
VAL   CG1 HG13 sing N N 491 
VAL   CG2 HG21 sing N N 492 
VAL   CG2 HG22 sing N N 493 
VAL   CG2 HG23 sing N N 494 
VAL   OXT HXT  sing N N 495 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1R01AI155723 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   9MTU 
_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                    9MTW 
_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]   0.023259 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003468 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005463 
_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]   0.020040 
_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 
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   . ASN   A 1 2   ? -0.216  -6.664  21.570  1.00 64.78 ? 3   ASN   A N   1 
ATOM   2    C CA  . ASN   A 1 2   ? 0.333   -7.946  21.141  1.00 56.43 ? 3   ASN   A CA  1 
ATOM   3    C C   . ASN   A 1 2   ? 0.480   -8.909  22.316  1.00 56.92 ? 3   ASN   A C   1 
ATOM   4    O O   . ASN   A 1 2   ? 0.545   -8.488  23.472  1.00 56.81 ? 3   ASN   A O   1 
ATOM   5    C CB  . ASN   A 1 2   ? 1.680   -7.741  20.450  1.00 56.42 ? 3   ASN   A CB  1 
ATOM   6    C CG  . ASN   A 1 2   ? 1.671   -8.218  19.014  1.00 55.05 ? 3   ASN   A CG  1 
ATOM   7    O OD1 . ASN   A 1 2   ? 0.979   -9.177  18.675  1.00 60.37 ? 3   ASN   A OD1 1 
ATOM   8    N ND2 . ASN   A 1 2   ? 2.439   -7.552  18.162  1.00 46.61 ? 3   ASN   A ND2 1 
ATOM   9    N N   . THR   A 1 3   ? 0.539   -10.203 22.010  1.00 55.01 ? 4   THR   A N   1 
ATOM   10   C CA  . THR   A 1 3   ? 0.587   -11.219 23.050  1.00 55.89 ? 4   THR   A CA  1 
ATOM   11   C C   . THR   A 1 3   ? 1.909   -11.143 23.818  1.00 51.79 ? 4   THR   A C   1 
ATOM   12   O O   . THR   A 1 3   ? 2.911   -10.647 23.293  1.00 49.29 ? 4   THR   A O   1 
ATOM   13   C CB  . THR   A 1 3   ? 0.420   -12.608 22.440  1.00 55.07 ? 4   THR   A CB  1 
ATOM   14   O OG1 . THR   A 1 3   ? 1.623   -12.978 21.755  1.00 49.65 ? 4   THR   A OG1 1 
ATOM   15   C CG2 . THR   A 1 3   ? -0.738  -12.611 21.446  1.00 55.78 ? 4   THR   A CG2 1 
ATOM   16   N N   . PRO   A 1 4   ? 1.932   -11.616 25.074  1.00 51.60 ? 5   PRO   A N   1 
ATOM   17   C CA  . PRO   A 1 4   ? 3.195   -11.620 25.837  1.00 48.99 ? 5   PRO   A CA  1 
ATOM   18   C C   . PRO   A 1 4   ? 4.354   -12.277 25.105  1.00 44.39 ? 5   PRO   A C   1 
ATOM   19   O O   . PRO   A 1 4   ? 5.494   -11.807 25.213  1.00 41.46 ? 5   PRO   A O   1 
ATOM   20   C CB  . PRO   A 1 4   ? 2.822   -12.390 27.111  1.00 51.04 ? 5   PRO   A CB  1 
ATOM   21   C CG  . PRO   A 1 4   ? 1.368   -12.111 27.292  1.00 57.05 ? 5   PRO   A CG  1 
ATOM   22   C CD  . PRO   A 1 4   ? 0.785   -12.034 25.903  1.00 55.66 ? 5   PRO   A CD  1 
ATOM   23   N N   . LYS   A 1 5   ? 4.090   -13.353 24.361  1.00 44.61 ? 6   LYS   A N   1 
ATOM   24   C CA  . LYS   A 1 5   ? 5.143   -13.995 23.581  1.00 42.24 ? 6   LYS   A CA  1 
ATOM   25   C C   . LYS   A 1 5   ? 5.611   -13.097 22.440  1.00 40.89 ? 6   LYS   A C   1 
ATOM   26   O O   . LYS   A 1 5   ? 6.819   -12.955 22.215  1.00 36.54 ? 6   LYS   A O   1 
ATOM   27   C CB  . LYS   A 1 5   ? 4.651   -15.343 23.053  1.00 39.46 ? 6   LYS   A CB  1 
ATOM   28   C CG  . LYS   A 1 5   ? 5.659   -16.088 22.197  1.00 40.32 ? 6   LYS   A CG  1 
ATOM   29   C CD  . LYS   A 1 5   ? 6.855   -16.562 22.997  1.00 39.58 ? 6   LYS   A CD  1 
ATOM   30   C CE  . LYS   A 1 5   ? 6.463   -17.635 23.992  1.00 37.18 ? 6   LYS   A CE  1 
ATOM   31   N NZ  . LYS   A 1 5   ? 7.676   -18.335 24.502  1.00 36.86 ? 6   LYS   A NZ  1 
ATOM   32   N N   . ASP   A 1 6   ? 4.671   -12.478 21.714  1.00 40.13 ? 7   ASP   A N   1 
ATOM   33   C CA  . ASP   A 1 6   ? 5.035   -11.492 20.696  1.00 41.00 ? 7   ASP   A CA  1 
ATOM   34   C C   . ASP   A 1 6   ? 6.009   -10.461 21.251  1.00 38.86 ? 7   ASP   A C   1 
ATOM   35   O O   . ASP   A 1 6   ? 7.019   -10.132 20.620  1.00 36.27 ? 7   ASP   A O   1 
ATOM   36   C CB  . ASP   A 1 6   ? 3.786   -10.780 20.170  1.00 46.73 ? 7   ASP   A CB  1 
ATOM   37   C CG  . ASP   A 1 6   ? 3.007   -11.613 19.185  1.00 50.90 ? 7   ASP   A CG  1 
ATOM   38   O OD1 . ASP   A 1 6   ? 3.582   -11.993 18.141  1.00 45.21 ? 7   ASP   A OD1 1 
ATOM   39   O OD2 . ASP   A 1 6   ? 1.816   -11.882 19.459  1.00 52.81 ? 7   ASP   A OD2 1 
ATOM   40   N N   . GLN   A 1 7   ? 5.709   -9.931  22.436  1.00 37.02 ? 8   GLN   A N   1 
ATOM   41   C CA  . GLN   A 1 7   ? 6.545   -8.886  23.010  1.00 38.29 ? 8   GLN   A CA  1 
ATOM   42   C C   . GLN   A 1 7   ? 7.880   -9.438  23.493  1.00 33.20 ? 8   GLN   A C   1 
ATOM   43   O O   . GLN   A 1 7   ? 8.910   -8.765  23.370  1.00 33.26 ? 8   GLN   A O   1 
ATOM   44   C CB  . GLN   A 1 7   ? 5.790   -8.196  24.148  1.00 43.34 ? 8   GLN   A CB  1 
ATOM   45   C CG  . GLN   A 1 7   ? 4.373   -7.816  23.753  1.00 48.22 ? 8   GLN   A CG  1 
ATOM   46   C CD  . GLN   A 1 7   ? 3.654   -7.005  24.808  1.00 56.24 ? 8   GLN   A CD  1 
ATOM   47   O OE1 . GLN   A 1 7   ? 3.322   -7.510  25.883  1.00 54.61 ? 8   GLN   A OE1 1 
ATOM   48   N NE2 . GLN   A 1 7   ? 3.401   -5.738  24.503  1.00 60.46 ? 8   GLN   A NE2 1 
ATOM   49   N N   . GLU   A 1 8   ? 7.883   -10.651 24.059  1.00 31.98 ? 9   GLU   A N   1 
ATOM   50   C CA  . GLU   A 1 8   ? 9.138   -11.255 24.504  1.00 35.02 ? 9   GLU   A CA  1 
ATOM   51   C C   . GLU   A 1 8   ? 10.091  -11.457 23.333  1.00 33.02 ? 9   GLU   A C   1 
ATOM   52   O O   . GLU   A 1 8   ? 11.264  -11.070 23.393  1.00 32.94 ? 9   GLU   A O   1 
ATOM   53   C CB  . GLU   A 1 8   ? 8.887   -12.596 25.196  1.00 37.10 ? 9   GLU   A CB  1 
ATOM   54   C CG  . GLU   A 1 8   ? 10.193  -13.326 25.513  1.00 37.36 ? 9   GLU   A CG  1 
ATOM   55   C CD  . GLU   A 1 8   ? 10.032  -14.823 25.743  1.00 38.20 ? 9   GLU   A CD  1 
ATOM   56   O OE1 . GLU   A 1 8   ? 8.916   -15.359 25.556  1.00 40.94 ? 9   GLU   A OE1 1 
ATOM   57   O OE2 . GLU   A 1 8   ? 11.035  -15.468 26.113  1.00 36.19 ? 9   GLU   A OE2 1 
ATOM   58   N N   . ILE   A 1 9   ? 9.600   -12.080 22.260  1.00 32.95 ? 10  ILE   A N   1 
ATOM   59   C CA  . ILE   A 1 9   ? 10.444  -12.361 21.103  1.00 30.82 ? 10  ILE   A CA  1 
ATOM   60   C C   . ILE   A 1 9   ? 10.899  -11.063 20.453  1.00 29.90 ? 10  ILE   A C   1 
ATOM   61   O O   . ILE   A 1 9   ? 12.044  -10.946 19.996  1.00 28.16 ? 10  ILE   A O   1 
ATOM   62   C CB  . ILE   A 1 9   ? 9.686   -13.266 20.114  1.00 29.57 ? 10  ILE   A CB  1 
ATOM   63   C CG1 . ILE   A 1 9   ? 9.387   -14.615 20.759  1.00 35.21 ? 10  ILE   A CG1 1 
ATOM   64   C CG2 . ILE   A 1 9   ? 10.469  -13.452 18.817  1.00 31.18 ? 10  ILE   A CG2 1 
ATOM   65   C CD1 . ILE   A 1 9   ? 8.581   -15.533 19.878  1.00 35.49 ? 10  ILE   A CD1 1 
ATOM   66   N N   . LYS   A 1 10  ? 10.012  -10.065 20.396  1.00 30.15 ? 11  LYS   A N   1 
ATOM   67   C CA  . LYS   A 1 10  ? 10.416  -8.762  19.881  1.00 31.29 ? 11  LYS   A CA  1 
ATOM   68   C C   . LYS   A 1 10  ? 11.568  -8.183  20.694  1.00 29.58 ? 11  LYS   A C   1 
ATOM   69   O O   . LYS   A 1 10  ? 12.525  -7.642  20.127  1.00 30.00 ? 11  LYS   A O   1 
ATOM   70   C CB  . LYS   A 1 10  ? 9.226   -7.797  19.874  1.00 34.78 ? 11  LYS   A CB  1 
ATOM   71   C CG  . LYS   A 1 10  ? 9.642   -6.339  20.023  1.00 41.99 ? 11  LYS   A CG  1 
ATOM   72   C CD  . LYS   A 1 10  ? 8.556   -5.372  19.596  1.00 44.00 ? 11  LYS   A CD  1 
ATOM   73   C CE  . LYS   A 1 10  ? 9.083   -3.945  19.593  1.00 46.67 ? 11  LYS   A CE  1 
ATOM   74   N NZ  . LYS   A 1 10  ? 10.261  -3.806  18.682  1.00 45.26 ? 11  LYS   A NZ  1 
ATOM   75   N N   . LYS   A 1 11  ? 11.506  -8.297  22.025  1.00 30.90 ? 12  LYS   A N   1 
ATOM   76   C CA  . LYS   A 1 11  ? 12.594  -7.767  22.842  1.00 30.71 ? 12  LYS   A CA  1 
ATOM   77   C C   . LYS   A 1 11  ? 13.900  -8.510  22.576  1.00 31.51 ? 12  LYS   A C   1 
ATOM   78   O O   . LYS   A 1 11  ? 14.962  -7.888  22.451  1.00 31.01 ? 12  LYS   A O   1 
ATOM   79   C CB  . LYS   A 1 11  ? 12.249  -7.828  24.331  1.00 31.67 ? 12  LYS   A CB  1 
ATOM   80   C CG  . LYS   A 1 11  ? 13.423  -7.364  25.192  1.00 37.09 ? 12  LYS   A CG  1 
ATOM   81   C CD  . LYS   A 1 11  ? 13.229  -7.618  26.679  1.00 46.68 ? 12  LYS   A CD  1 
ATOM   82   C CE  . LYS   A 1 11  ? 14.413  -8.402  27.252  1.00 47.92 ? 12  LYS   A CE  1 
ATOM   83   N NZ  . LYS   A 1 11  ? 14.432  -9.816  26.767  1.00 47.38 ? 12  LYS   A NZ  1 
ATOM   84   N N   . LEU   A 1 12  ? 13.844  -9.841  22.477  1.00 27.92 ? 13  LEU   A N   1 
ATOM   85   C CA  . LEU   A 1 12  ? 15.065  -10.611 22.249  1.00 28.70 ? 13  LEU   A CA  1 
ATOM   86   C C   . LEU   A 1 12  ? 15.684  -10.301 20.891  1.00 26.52 ? 13  LEU   A C   1 
ATOM   87   O O   . LEU   A 1 12  ? 16.913  -10.230 20.761  1.00 26.08 ? 13  LEU   A O   1 
ATOM   88   C CB  . LEU   A 1 12  ? 14.771  -12.102 22.377  1.00 28.79 ? 13  LEU   A CB  1 
ATOM   89   C CG  . LEU   A 1 12  ? 14.541  -12.544 23.817  1.00 34.21 ? 13  LEU   A CG  1 
ATOM   90   C CD1 . LEU   A 1 12  ? 14.149  -14.001 23.844  1.00 31.20 ? 13  LEU   A CD1 1 
ATOM   91   C CD2 . LEU   A 1 12  ? 15.787  -12.304 24.674  1.00 34.85 ? 13  LEU   A CD2 1 
ATOM   92   N N   . VAL   A 1 13  ? 14.853  -10.102 19.865  1.00 26.59 ? 14  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 13  ? 15.396  -9.795  18.543  1.00 27.31 ? 14  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 13  ? 15.913  -8.359  18.486  1.00 28.06 ? 14  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 13  ? 16.965  -8.091  17.891  1.00 25.27 ? 14  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 13  ? 14.344  -10.082 17.457  1.00 28.11 ? 14  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 13  ? 14.847  -9.624  16.084  1.00 25.86 ? 14  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 13  ? 13.994  -11.580 17.451  1.00 28.44 ? 14  VAL   A CG2 1 
ATOM   99   N N   . ASP   A 1 14  ? 15.210  -7.438  19.133  1.00 26.10 ? 15  ASP   A N   1 
ATOM   100  C CA  . ASP   A 1 14  ? 15.719  -6.049  19.211  1.00 29.11 ? 15  ASP   A CA  1 
ATOM   101  C C   . ASP   A 1 14  ? 17.059  -6.033  19.950  1.00 27.52 ? 15  ASP   A C   1 
ATOM   102  O O   . ASP   A 1 14  ? 17.918  -5.227  19.604  1.00 32.22 ? 15  ASP   A O   1 
ATOM   103  C CB  . ASP   A 1 14  ? 14.741  -5.132  19.948  1.00 30.19 ? 15  ASP   A CB  1 
ATOM   104  C CG  . ASP   A 1 14  ? 13.505  -4.722  19.169  1.00 35.93 ? 15  ASP   A CG  1 
ATOM   105  O OD1 . ASP   A 1 14  ? 13.516  -4.842  17.944  1.00 36.02 ? 15  ASP   A OD1 1 
ATOM   106  O OD2 . ASP   A 1 14  ? 12.542  -4.270  19.809  1.00 38.10 ? 15  ASP   A OD2 1 
ATOM   107  N N   . GLN   A 1 15  ? 17.210  -6.889  20.953  1.00 29.51 ? 16  GLN   A N   1 
ATOM   108  C CA  . GLN   A 1 15  ? 18.425  -6.883  21.755  1.00 26.61 ? 16  GLN   A CA  1 
ATOM   109  C C   . GLN   A 1 15  ? 19.596  -7.511  21.012  1.00 28.19 ? 16  GLN   A C   1 
ATOM   110  O O   . GLN   A 1 15  ? 20.738  -7.059  21.145  1.00 26.90 ? 16  GLN   A O   1 
ATOM   111  C CB  . GLN   A 1 15  ? 18.164  -7.610  23.072  1.00 29.66 ? 16  GLN   A CB  1 
ATOM   112  C CG  . GLN   A 1 15  ? 19.401  -7.923  23.886  1.00 35.06 ? 16  GLN   A CG  1 
ATOM   113  C CD  . GLN   A 1 15  ? 19.052  -8.392  25.282  1.00 43.67 ? 16  GLN   A CD  1 
ATOM   114  O OE1 . GLN   A 1 15  ? 17.900  -8.281  25.714  1.00 47.09 ? 16  GLN   A OE1 1 
ATOM   115  N NE2 . GLN   A 1 15  ? 20.045  -8.913  26.000  1.00 44.28 ? 16  GLN   A NE2 1 
ATOM   116  N N   . ASN   A 1 16  ? 19.340  -8.551  20.225  1.00 27.18 ? 17  ASN   A N   1 
ATOM   117  C CA  . ASN   A 1 16  ? 20.420  -9.352  19.666  1.00 23.97 ? 17  ASN   A CA  1 
ATOM   118  C C   . ASN   A 1 16  ? 20.641  -9.157  18.172  1.00 24.31 ? 17  ASN   A C   1 
ATOM   119  O O   . ASN   A 1 16  ? 21.778  -9.287  17.716  1.00 25.57 ? 17  ASN   A O   1 
ATOM   120  C CB  . ASN   A 1 16  ? 20.175  -10.837 19.972  1.00 22.24 ? 17  ASN   A CB  1 
ATOM   121  C CG  . ASN   A 1 16  ? 20.321  -11.145 21.462  1.00 25.65 ? 17  ASN   A CG  1 
ATOM   122  O OD1 . ASN   A 1 16  ? 21.434  -11.174 21.993  1.00 24.41 ? 17  ASN   A OD1 1 
ATOM   123  N ND2 . ASN   A 1 16  ? 19.197  -11.357 22.144  1.00 26.35 ? 17  ASN   A ND2 1 
ATOM   124  N N   . PHE   A 1 17  ? 19.604  -8.835  17.399  1.00 22.22 ? 18  PHE   A N   1 
ATOM   125  C CA  . PHE   A 1 17  ? 19.763  -8.660  15.957  1.00 20.79 ? 18  PHE   A CA  1 
ATOM   126  C C   . PHE   A 1 17  ? 19.751  -7.201  15.520  1.00 24.74 ? 18  PHE   A C   1 
ATOM   127  O O   . PHE   A 1 17  ? 20.560  -6.815  14.668  1.00 25.36 ? 18  PHE   A O   1 
ATOM   128  C CB  . PHE   A 1 17  ? 18.678  -9.440  15.201  1.00 21.21 ? 18  PHE   A CB  1 
ATOM   129  C CG  . PHE   A 1 17  ? 18.976  -10.913 15.071  1.00 18.97 ? 18  PHE   A CG  1 
ATOM   130  C CD1 . PHE   A 1 17  ? 19.699  -11.401 13.982  1.00 19.45 ? 18  PHE   A CD1 1 
ATOM   131  C CD2 . PHE   A 1 17  ? 18.545  -11.806 16.038  1.00 21.67 ? 18  PHE   A CD2 1 
ATOM   132  C CE1 . PHE   A 1 17  ? 19.988  -12.766 13.872  1.00 21.14 ? 18  PHE   A CE1 1 
ATOM   133  C CE2 . PHE   A 1 17  ? 18.829  -13.170 15.937  1.00 20.28 ? 18  PHE   A CE2 1 
ATOM   134  C CZ  . PHE   A 1 17  ? 19.544  -13.650 14.846  1.00 19.36 ? 18  PHE   A CZ  1 
ATOM   135  N N   . LYS   A 1 18  ? 18.872  -6.377  16.098  1.00 24.50 ? 19  LYS   A N   1 
ATOM   136  C CA  . LYS   A 1 18  ? 18.753  -4.987  15.660  1.00 26.13 ? 19  LYS   A CA  1 
ATOM   137  C C   . LYS   A 1 18  ? 20.062  -4.204  15.727  1.00 24.34 ? 19  LYS   A C   1 
ATOM   138  O O   . LYS   A 1 18  ? 20.316  -3.411  14.800  1.00 27.72 ? 19  LYS   A O   1 
ATOM   139  C CB  . LYS   A 1 18  ? 17.662  -4.288  16.483  1.00 26.80 ? 19  LYS   A CB  1 
ATOM   140  C CG  . LYS   A 1 18  ? 17.438  -2.826  16.161  1.00 31.07 ? 19  LYS   A CG  1 
ATOM   141  C CD  . LYS   A 1 18  ? 16.412  -2.260  17.125  1.00 33.53 ? 19  LYS   A CD  1 
ATOM   142  C CE  . LYS   A 1 18  ? 16.144  -0.790  16.874  1.00 39.44 ? 19  LYS   A CE  1 
ATOM   143  N NZ  . LYS   A 1 18  ? 15.207  -0.263  17.901  1.00 43.98 ? 19  LYS   A NZ  1 
ATOM   144  N N   . PRO   A 1 19  ? 20.912  -4.341  16.755  1.00 26.35 ? 20  PRO   A N   1 
ATOM   145  C CA  . PRO   A 1 19  ? 22.160  -3.557  16.761  1.00 27.76 ? 20  PRO   A CA  1 
ATOM   146  C C   . PRO   A 1 19  ? 23.060  -3.843  15.577  1.00 27.90 ? 20  PRO   A C   1 
ATOM   147  O O   . PRO   A 1 19  ? 23.902  -2.998  15.243  1.00 31.58 ? 20  PRO   A O   1 
ATOM   148  C CB  . PRO   A 1 19  ? 22.830  -3.969  18.078  1.00 30.88 ? 20  PRO   A CB  1 
ATOM   149  C CG  . PRO   A 1 19  ? 21.706  -4.420  18.940  1.00 30.10 ? 20  PRO   A CG  1 
ATOM   150  C CD  . PRO   A 1 19  ? 20.756  -5.099  18.013  1.00 27.21 ? 20  PRO   A CD  1 
ATOM   151  N N   . LEU   A 1 20  ? 22.901  -4.999  14.928  1.00 25.76 ? 21  LEU   A N   1 
ATOM   152  C CA  . LEU   A 1 20  ? 23.758  -5.355  13.804  1.00 27.84 ? 21  LEU   A CA  1 
ATOM   153  C C   . LEU   A 1 20  ? 23.554  -4.447  12.603  1.00 27.03 ? 21  LEU   A C   1 
ATOM   154  O O   . LEU   A 1 20  ? 24.476  -4.310  11.790  1.00 26.62 ? 21  LEU   A O   1 
ATOM   155  C CB  . LEU   A 1 20  ? 23.514  -6.806  13.391  1.00 24.37 ? 21  LEU   A CB  1 
ATOM   156  C CG  . LEU   A 1 20  ? 23.858  -7.856  14.444  1.00 22.74 ? 21  LEU   A CG  1 
ATOM   157  C CD1 . LEU   A 1 20  ? 23.401  -9.260  14.009  1.00 21.17 ? 21  LEU   A CD1 1 
ATOM   158  C CD2 . LEU   A 1 20  ? 25.346  -7.840  14.728  1.00 26.95 ? 21  LEU   A CD2 1 
ATOM   159  N N   . LEU   A 1 21  ? 22.376  -3.824  12.475  1.00 26.98 ? 22  LEU   A N   1 
ATOM   160  C CA  . LEU   A 1 21  ? 22.126  -2.939  11.342  1.00 26.78 ? 22  LEU   A CA  1 
ATOM   161  C C   . LEU   A 1 21  ? 23.055  -1.733  11.381  1.00 28.83 ? 22  LEU   A C   1 
ATOM   162  O O   . LEU   A 1 21  ? 23.728  -1.419  10.392  1.00 29.21 ? 22  LEU   A O   1 
ATOM   163  C CB  . LEU   A 1 21  ? 20.662  -2.491  11.325  1.00 29.27 ? 22  LEU   A CB  1 
ATOM   164  C CG  . LEU   A 1 21  ? 19.554  -3.471  10.907  1.00 31.41 ? 22  LEU   A CG  1 
ATOM   165  C CD1 . LEU   A 1 21  ? 19.986  -4.353  9.764   1.00 32.98 ? 22  LEU   A CD1 1 
ATOM   166  C CD2 . LEU   A 1 21  ? 19.064  -4.328  12.059  1.00 31.84 ? 22  LEU   A CD2 1 
ATOM   167  N N   . GLU   A 1 22  ? 23.111  -1.045  12.524  1.00 29.10 ? 23  GLU   A N   1 
ATOM   168  C CA  . GLU   A 1 22  ? 24.025  0.085   12.644  1.00 31.00 ? 23  GLU   A CA  1 
ATOM   169  C C   . GLU   A 1 22  ? 25.477  -0.378  12.631  1.00 30.91 ? 23  GLU   A C   1 
ATOM   170  O O   . GLU   A 1 22  ? 26.329  0.254   11.994  1.00 29.22 ? 23  GLU   A O   1 
ATOM   171  C CB  . GLU   A 1 22  ? 23.712  0.879   13.915  1.00 36.41 ? 23  GLU   A CB  1 
ATOM   172  C CG  . GLU   A 1 22  ? 24.372  2.247   13.965  1.00 41.34 ? 23  GLU   A CG  1 
ATOM   173  C CD  . GLU   A 1 22  ? 25.421  2.333   15.048  1.00 46.65 ? 23  GLU   A CD  1 
ATOM   174  O OE1 . GLU   A 1 22  ? 25.582  3.427   15.631  1.00 52.42 ? 23  GLU   A OE1 1 
ATOM   175  O OE2 . GLU   A 1 22  ? 26.075  1.303   15.328  1.00 46.96 ? 23  GLU   A OE2 1 
ATOM   176  N N   . LYS   A 1 23  ? 25.774  -1.496  13.298  1.00 30.55 ? 24  LYS   A N   1 
ATOM   177  C CA  . LYS   A 1 23  ? 27.158  -1.945  13.399  1.00 28.01 ? 24  LYS   A CA  1 
ATOM   178  C C   . LYS   A 1 23  ? 27.776  -2.191  12.025  1.00 29.53 ? 24  LYS   A C   1 
ATOM   179  O O   . LYS   A 1 23  ? 28.931  -1.827  11.790  1.00 31.79 ? 24  LYS   A O   1 
ATOM   180  C CB  . LYS   A 1 23  ? 27.249  -3.209  14.254  1.00 30.28 ? 24  LYS   A CB  1 
ATOM   181  C CG  . LYS   A 1 23  ? 28.664  -3.743  14.363  1.00 29.19 ? 24  LYS   A CG  1 
ATOM   182  C CD  . LYS   A 1 23  ? 28.774  -4.816  15.435  1.00 26.94 ? 24  LYS   A CD  1 
ATOM   183  C CE  . LYS   A 1 23  ? 30.225  -5.178  15.704  1.00 31.16 ? 24  LYS   A CE  1 
ATOM   184  N NZ  . LYS   A 1 23  ? 30.337  -6.285  16.688  1.00 32.80 ? 24  LYS   A NZ  1 
ATOM   185  N N   . TYR   A 1 24  ? 27.026  -2.796  11.101  1.00 28.95 ? 25  TYR   A N   1 
ATOM   186  C CA  . TYR   A 1 24  ? 27.567  -3.162  9.797   1.00 27.19 ? 25  TYR   A CA  1 
ATOM   187  C C   . TYR   A 1 24  ? 26.961  -2.367  8.644   1.00 31.26 ? 25  TYR   A C   1 
ATOM   188  O O   . TYR   A 1 24  ? 27.169  -2.737  7.483   1.00 30.95 ? 25  TYR   A O   1 
ATOM   189  C CB  . TYR   A 1 24  ? 27.390  -4.665  9.553   1.00 25.25 ? 25  TYR   A CB  1 
ATOM   190  C CG  . TYR   A 1 24  ? 28.247  -5.485  10.486  1.00 26.62 ? 25  TYR   A CG  1 
ATOM   191  C CD1 . TYR   A 1 24  ? 29.618  -5.580  10.285  1.00 26.65 ? 25  TYR   A CD1 1 
ATOM   192  C CD2 . TYR   A 1 24  ? 27.698  -6.132  11.591  1.00 28.25 ? 25  TYR   A CD2 1 
ATOM   193  C CE1 . TYR   A 1 24  ? 30.421  -6.307  11.154  1.00 28.19 ? 25  TYR   A CE1 1 
ATOM   194  C CE2 . TYR   A 1 24  ? 28.499  -6.863  12.466  1.00 28.73 ? 25  TYR   A CE2 1 
ATOM   195  C CZ  . TYR   A 1 24  ? 29.858  -6.947  12.235  1.00 26.93 ? 25  TYR   A CZ  1 
ATOM   196  O OH  . TYR   A 1 24  ? 30.667  -7.665  13.083  1.00 29.35 ? 25  TYR   A OH  1 
ATOM   197  N N   . ASP   A 1 25  ? 26.234  -1.287  8.936   1.00 27.69 ? 26  ASP   A N   1 
ATOM   198  C CA  . ASP   A 1 25  ? 25.563  -0.447  7.933   1.00 29.38 ? 26  ASP   A CA  1 
ATOM   199  C C   . ASP   A 1 25  ? 24.682  -1.270  6.984   1.00 31.00 ? 26  ASP   A C   1 
ATOM   200  O O   . ASP   A 1 25  ? 24.707  -1.099  5.762   1.00 30.68 ? 26  ASP   A O   1 
ATOM   201  C CB  . ASP   A 1 25  ? 26.574  0.389   7.143   1.00 32.73 ? 26  ASP   A CB  1 
ATOM   202  C CG  . ASP   A 1 25  ? 25.917  1.520   6.376   1.00 43.28 ? 26  ASP   A CG  1 
ATOM   203  O OD1 . ASP   A 1 25  ? 24.696  1.725   6.556   1.00 42.71 ? 26  ASP   A OD1 1 
ATOM   204  O OD2 . ASP   A 1 25  ? 26.620  2.219   5.610   1.00 45.46 ? 26  ASP   A OD2 1 
ATOM   205  N N   . VAL   A 1 26  ? 23.870  -2.146  7.564   1.00 29.24 ? 27  VAL   A N   1 
ATOM   206  C CA  . VAL   A 1 26  ? 22.972  -3.011  6.793   1.00 23.50 ? 27  VAL   A CA  1 
ATOM   207  C C   . VAL   A 1 26  ? 21.668  -2.248  6.555   1.00 25.60 ? 27  VAL   A C   1 
ATOM   208  O O   . VAL   A 1 26  ? 21.031  -1.822  7.525   1.00 25.39 ? 27  VAL   A O   1 
ATOM   209  C CB  . VAL   A 1 26  ? 22.692  -4.323  7.532   1.00 22.93 ? 27  VAL   A CB  1 
ATOM   210  C CG1 . VAL   A 1 26  ? 21.738  -5.185  6.709   1.00 22.42 ? 27  VAL   A CG1 1 
ATOM   211  C CG2 . VAL   A 1 26  ? 23.989  -5.046  7.850   1.00 25.61 ? 27  VAL   A CG2 1 
ATOM   212  N N   . PRO   A 1 27  ? 21.237  -2.076  5.299   1.00 23.98 ? 28  PRO   A N   1 
ATOM   213  C CA  . PRO   A 1 27  ? 20.001  -1.307  5.074   1.00 22.49 ? 28  PRO   A CA  1 
ATOM   214  C C   . PRO   A 1 27  ? 18.757  -1.967  5.654   1.00 23.07 ? 28  PRO   A C   1 
ATOM   215  O O   . PRO   A 1 27  ? 17.932  -1.275  6.271   1.00 23.50 ? 28  PRO   A O   1 
ATOM   216  C CB  . PRO   A 1 27  ? 19.938  -1.200  3.542   1.00 26.04 ? 28  PRO   A CB  1 
ATOM   217  C CG  . PRO   A 1 27  ? 21.373  -1.322  3.108   1.00 27.02 ? 28  PRO   A CG  1 
ATOM   218  C CD  . PRO   A 1 27  ? 21.930  -2.374  4.035   1.00 25.10 ? 28  PRO   A CD  1 
ATOM   219  N N   . GLY   A 1 28  ? 18.601  -3.276  5.496   1.00 24.70 ? 29  GLY   A N   1 
ATOM   220  C CA  . GLY   A 1 28  ? 17.372  -3.935  5.909   1.00 22.95 ? 29  GLY   A CA  1 
ATOM   221  C C   . GLY   A 1 28  ? 17.591  -5.348  6.402   1.00 22.62 ? 29  GLY   A C   1 
ATOM   222  O O   . GLY   A 1 28  ? 18.529  -6.038  5.987   1.00 21.10 ? 29  GLY   A O   1 
ATOM   223  N N   . MET   A 1 29  ? 16.684  -5.791  7.267   1.00 18.04 ? 30  MET   A N   1 
ATOM   224  C CA  . MET   A 1 29  ? 16.775  -7.115  7.876   1.00 20.76 ? 30  MET   A CA  1 
ATOM   225  C C   . MET   A 1 29  ? 15.375  -7.637  8.174   1.00 19.96 ? 30  MET   A C   1 
ATOM   226  O O   . MET   A 1 29  ? 14.477  -6.875  8.538   1.00 19.83 ? 30  MET   A O   1 
ATOM   227  C CB  . MET   A 1 29  ? 17.607  -7.070  9.164   1.00 19.23 ? 30  MET   A CB  1 
ATOM   228  C CG  . MET   A 1 29  ? 17.734  -8.423  9.864   1.00 19.79 ? 30  MET   A CG  1 
ATOM   229  S SD  . MET   A 1 29  ? 18.512  -8.269  11.475  1.00 23.32 ? 30  MET   A SD  1 
ATOM   230  C CE  . MET   A 1 29  ? 20.209  -7.975  11.039  1.00 25.25 ? 30  MET   A CE  1 
ATOM   231  N N   . ALA   A 1 30  ? 15.204  -8.949  8.032   1.00 18.78 ? 31  ALA   A N   1 
ATOM   232  C CA  . ALA   A 1 30  ? 13.996  -9.634  8.469   1.00 18.28 ? 31  ALA   A CA  1 
ATOM   233  C C   . ALA   A 1 30  ? 14.411  -10.802 9.353   1.00 20.43 ? 31  ALA   A C   1 
ATOM   234  O O   . ALA   A 1 30  ? 15.303  -11.566 8.979   1.00 19.27 ? 31  ALA   A O   1 
ATOM   235  C CB  . ALA   A 1 30  ? 13.176  -10.142 7.273   1.00 19.09 ? 31  ALA   A CB  1 
ATOM   236  N N   . VAL   A 1 31  ? 13.796  -10.922 10.532  1.00 18.62 ? 32  VAL   A N   1 
ATOM   237  C CA  . VAL   A 1 31  ? 14.106  -12.010 11.461  1.00 16.90 ? 32  VAL   A CA  1 
ATOM   238  C C   . VAL   A 1 31  ? 12.804  -12.691 11.834  1.00 18.23 ? 32  VAL   A C   1 
ATOM   239  O O   . VAL   A 1 31  ? 11.849  -12.029 12.252  1.00 20.05 ? 32  VAL   A O   1 
ATOM   240  C CB  . VAL   A 1 31  ? 14.825  -11.515 12.729  1.00 19.61 ? 32  VAL   A CB  1 
ATOM   241  C CG1 . VAL   A 1 31  ? 15.081  -12.703 13.694  1.00 19.66 ? 32  VAL   A CG1 1 
ATOM   242  C CG2 . VAL   A 1 31  ? 16.130  -10.842 12.357  1.00 19.79 ? 32  VAL   A CG2 1 
ATOM   243  N N   . GLY   A 1 32  ? 12.769  -14.008 11.717  1.00 19.27 ? 33  GLY   A N   1 
ATOM   244  C CA  . GLY   A 1 32  ? 11.587  -14.779 12.057  1.00 19.11 ? 33  GLY   A CA  1 
ATOM   245  C C   . GLY   A 1 32  ? 11.905  -15.846 13.086  1.00 20.50 ? 33  GLY   A C   1 
ATOM   246  O O   . GLY   A 1 32  ? 12.971  -16.464 13.048  1.00 19.68 ? 33  GLY   A O   1 
ATOM   247  N N   . VAL   A 1 33  ? 10.969  -16.060 13.998  1.00 20.69 ? 34  VAL   A N   1 
ATOM   248  C CA  . VAL   A 1 33  ? 11.035  -17.166 14.941  1.00 19.70 ? 34  VAL   A CA  1 
ATOM   249  C C   . VAL   A 1 33  ? 9.757   -17.970 14.783  1.00 22.71 ? 34  VAL   A C   1 
ATOM   250  O O   . VAL   A 1 33  ? 8.669   -17.395 14.662  1.00 21.64 ? 34  VAL   A O   1 
ATOM   251  C CB  . VAL   A 1 33  ? 11.200  -16.661 16.392  1.00 21.51 ? 34  VAL   A CB  1 
ATOM   252  C CG1 . VAL   A 1 33  ? 11.042  -17.810 17.386  1.00 24.42 ? 34  VAL   A CG1 1 
ATOM   253  C CG2 . VAL   A 1 33  ? 12.550  -16.005 16.559  1.00 20.98 ? 34  VAL   A CG2 1 
ATOM   254  N N   . ILE   A 1 34  ? 9.875   -19.295 14.762  1.00 21.01 ? 35  ILE   A N   1 
ATOM   255  C CA  . ILE   A 1 34  ? 8.707   -20.154 14.888  1.00 24.42 ? 35  ILE   A CA  1 
ATOM   256  C C   . ILE   A 1 34  ? 8.880   -20.983 16.146  1.00 23.74 ? 35  ILE   A C   1 
ATOM   257  O O   . ILE   A 1 34  ? 9.938   -21.586 16.351  1.00 21.48 ? 35  ILE   A O   1 
ATOM   258  C CB  . ILE   A 1 34  ? 8.484   -21.048 13.652  1.00 24.90 ? 35  ILE   A CB  1 
ATOM   259  C CG1 . ILE   A 1 34  ? 7.331   -22.029 13.928  1.00 29.20 ? 35  ILE   A CG1 1 
ATOM   260  C CG2 . ILE   A 1 34  ? 9.774   -21.746 13.226  1.00 22.27 ? 35  ILE   A CG2 1 
ATOM   261  C CD1 . ILE   A 1 34  ? 6.825   -22.727 12.700  1.00 25.58 ? 35  ILE   A CD1 1 
ATOM   262  N N   . GLN   A 1 35  ? 7.853   -20.992 16.991  1.00 24.17 ? 36  GLN   A N   1 
ATOM   263  C CA  . GLN   A 1 35  ? 7.879   -21.766 18.222  1.00 25.62 ? 36  GLN   A CA  1 
ATOM   264  C C   . GLN   A 1 35  ? 6.498   -22.344 18.467  1.00 28.98 ? 36  GLN   A C   1 
ATOM   265  O O   . GLN   A 1 35  ? 5.517   -21.597 18.490  1.00 28.55 ? 36  GLN   A O   1 
ATOM   266  C CB  . GLN   A 1 35  ? 8.301   -20.909 19.421  1.00 27.91 ? 36  GLN   A CB  1 
ATOM   267  C CG  . GLN   A 1 35  ? 8.365   -21.704 20.717  1.00 28.03 ? 36  GLN   A CG  1 
ATOM   268  C CD  . GLN   A 1 35  ? 8.566   -20.844 21.963  1.00 34.50 ? 36  GLN   A CD  1 
ATOM   269  O OE1 . GLN   A 1 35  ? 8.075   -19.718 22.051  1.00 32.29 ? 36  GLN   A OE1 1 
ATOM   270  N NE2 . GLN   A 1 35  ? 9.297   -21.384 22.936  1.00 31.05 ? 36  GLN   A NE2 1 
ATOM   271  N N   . ASN   A 1 36  ? 6.430   -23.664 18.653  1.00 31.85 ? 37  ASN   A N   1 
ATOM   272  C CA  . ASN   A 1 36  ? 5.167   -24.378 18.894  1.00 29.38 ? 37  ASN   A CA  1 
ATOM   273  C C   . ASN   A 1 36  ? 4.106   -24.006 17.861  1.00 30.43 ? 37  ASN   A C   1 
ATOM   274  O O   . ASN   A 1 36  ? 2.952   -23.716 18.191  1.00 32.31 ? 37  ASN   A O   1 
ATOM   275  C CB  . ASN   A 1 36  ? 4.650   -24.130 20.312  1.00 33.35 ? 37  ASN   A CB  1 
ATOM   276  C CG  . ASN   A 1 36  ? 5.574   -24.678 21.370  1.00 35.77 ? 37  ASN   A CG  1 
ATOM   277  O OD1 . ASN   A 1 36  ? 6.177   -25.737 21.200  1.00 37.30 ? 37  ASN   A OD1 1 
ATOM   278  N ND2 . ASN   A 1 36  ? 5.698   -23.951 22.474  1.00 37.49 ? 37  ASN   A ND2 1 
ATOM   279  N N   . ASN   A 1 37  ? 4.525   -24.014 16.594  1.00 30.55 ? 38  ASN   A N   1 
ATOM   280  C CA  . ASN   A 1 37  ? 3.683   -23.766 15.423  1.00 32.21 ? 38  ASN   A CA  1 
ATOM   281  C C   . ASN   A 1 37  ? 3.103   -22.353 15.390  1.00 31.93 ? 38  ASN   A C   1 
ATOM   282  O O   . ASN   A 1 37  ? 2.171   -22.084 14.625  1.00 34.49 ? 38  ASN   A O   1 
ATOM   283  C CB  . ASN   A 1 37  ? 2.569   -24.814 15.299  1.00 37.22 ? 38  ASN   A CB  1 
ATOM   284  C CG  . ASN   A 1 37  ? 2.988   -25.998 14.446  1.00 40.49 ? 38  ASN   A CG  1 
ATOM   285  O OD1 . ASN   A 1 37  ? 4.165   -26.373 14.419  1.00 44.84 ? 38  ASN   A OD1 1 
ATOM   286  N ND2 . ASN   A 1 37  ? 2.034   -26.579 13.722  1.00 46.97 ? 38  ASN   A ND2 1 
ATOM   287  N N   . LYS   A 1 38  ? 3.658   -21.427 16.168  1.00 29.45 ? 39  LYS   A N   1 
ATOM   288  C CA  . LYS   A 1 38  ? 3.316   -20.015 16.052  1.00 31.49 ? 39  LYS   A CA  1 
ATOM   289  C C   . LYS   A 1 38  ? 4.492   -19.271 15.433  1.00 26.44 ? 39  LYS   A C   1 
ATOM   290  O O   . LYS   A 1 38  ? 5.645   -19.469 15.839  1.00 27.51 ? 39  LYS   A O   1 
ATOM   291  C CB  . LYS   A 1 38  ? 2.946   -19.409 17.408  1.00 31.81 ? 39  LYS   A CB  1 
ATOM   292  C CG  . LYS   A 1 38  ? 1.651   -19.958 18.009  1.00 34.47 ? 39  LYS   A CG  1 
ATOM   293  C CD  . LYS   A 1 38  ? 1.160   -19.084 19.163  1.00 46.26 ? 39  LYS   A CD  1 
ATOM   294  C CE  . LYS   A 1 38  ? 0.458   -17.820 18.658  1.00 53.24 ? 39  LYS   A CE  1 
ATOM   295  N NZ  . LYS   A 1 38  ? 0.672   -16.637 19.558  1.00 52.60 ? 39  LYS   A NZ  1 
ATOM   296  N N   . LYS   A 1 39  ? 4.201   -18.428 14.448  1.00 24.89 ? 40  LYS   A N   1 
ATOM   297  C CA  . LYS   A 1 39  ? 5.226   -17.693 13.715  1.00 25.35 ? 40  LYS   A CA  1 
ATOM   298  C C   . LYS   A 1 39  ? 5.269   -16.241 14.173  1.00 23.46 ? 40  LYS   A C   1 
ATOM   299  O O   . LYS   A 1 39  ? 4.228   -15.630 14.430  1.00 27.19 ? 40  LYS   A O   1 
ATOM   300  C CB  . LYS   A 1 39  ? 4.968   -17.763 12.208  1.00 29.03 ? 40  LYS   A CB  1 
ATOM   301  C CG  . LYS   A 1 39  ? 5.012   -19.182 11.634  1.00 29.38 ? 40  LYS   A CG  1 
ATOM   302  C CD  . LYS   A 1 39  ? 4.432   -19.211 10.229  1.00 29.68 ? 40  LYS   A CD  1 
ATOM   303  C CE  . LYS   A 1 39  ? 4.492   -20.610 9.625   1.00 31.25 ? 40  LYS   A CE  1 
ATOM   304  N NZ  . LYS   A 1 39  ? 3.740   -20.678 8.336   1.00 29.62 ? 40  LYS   A NZ  1 
ATOM   305  N N   . TYR   A 1 40  ? 6.481   -15.689 14.254  1.00 25.71 ? 41  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 40  ? 6.704   -14.316 14.691  1.00 26.95 ? 41  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 40  ? 7.648   -13.641 13.703  1.00 24.01 ? 41  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 40  ? 8.773   -14.114 13.494  1.00 21.62 ? 41  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 40  ? 7.276   -14.290 16.113  1.00 24.36 ? 41  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 40  ? 6.429   -15.076 17.086  1.00 28.20 ? 41  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 40  ? 6.585   -16.454 17.226  1.00 27.73 ? 41  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 40  ? 5.459   -14.443 17.848  1.00 32.32 ? 41  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 40  ? 5.804   -17.171 18.108  1.00 28.02 ? 41  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 40  ? 4.671   -15.150 18.727  1.00 34.58 ? 41  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 40  ? 4.850   -16.509 18.854  1.00 31.16 ? 41  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 40  ? 4.067   -17.214 19.730  1.00 36.97 ? 41  TYR   A OH  1 
ATOM   317  N N   . GLU   A 1 41  ? 7.188   -12.552 13.085  1.00 22.81 ? 42  GLU   A N   1 
ATOM   318  C CA  . GLU   A 1 41  ? 7.951   -11.855 12.053  1.00 23.01 ? 42  GLU   A CA  1 
ATOM   319  C C   . GLU   A 1 41  ? 8.365   -10.475 12.547  1.00 26.13 ? 42  GLU   A C   1 
ATOM   320  O O   . GLU   A 1 41  ? 7.537   -9.722  13.074  1.00 25.62 ? 42  GLU   A O   1 
ATOM   321  C CB  . GLU   A 1 41  ? 7.139   -11.704 10.763  1.00 24.84 ? 42  GLU   A CB  1 
ATOM   322  C CG  . GLU   A 1 41  ? 6.615   -13.013 10.167  1.00 26.58 ? 42  GLU   A CG  1 
ATOM   323  C CD  . GLU   A 1 41  ? 5.634   -12.766 9.028   1.00 28.47 ? 42  GLU   A CD  1 
ATOM   324  O OE1 . GLU   A 1 41  ? 4.922   -13.715 8.632   1.00 36.24 ? 42  GLU   A OE1 1 
ATOM   325  O OE2 . GLU   A 1 41  ? 5.563   -11.622 8.533   1.00 31.04 ? 42  GLU   A OE2 1 
ATOM   326  N N   . MET   A 1 42  ? 9.633   -10.129 12.336  1.00 22.53 ? 43  MET   A N   1 
ATOM   327  C CA  . MET   A 1 42  ? 10.160  -8.820  12.700  1.00 23.76 ? 43  MET   A CA  1 
ATOM   328  C C   . MET   A 1 42  ? 10.927  -8.234  11.522  1.00 23.34 ? 43  MET   A C   1 
ATOM   329  O O   . MET   A 1 42  ? 11.759  -8.916  10.915  1.00 21.45 ? 43  MET   A O   1 
ATOM   330  C CB  . MET   A 1 42  ? 11.042  -8.937  13.948  1.00 24.99 ? 43  MET   A CB  1 
ATOM   331  C CG  . MET   A 1 42  ? 10.209  -9.159  15.213  1.00 33.02 ? 43  MET   A CG  1 
ATOM   332  S SD  . MET   A 1 42  ? 10.703  -10.484 16.341  1.00 41.05 ? 43  MET   A SD  1 
ATOM   333  C CE  . MET   A 1 42  ? 10.814  -11.925 15.263  1.00 26.92 ? 43  MET   A CE  1 
ATOM   334  N N   . TYR   A 1 43  ? 10.635  -6.978  11.182  1.00 23.86 ? 44  TYR   A N   1 
ATOM   335  C CA  . TYR   A 1 43  ? 11.222  -6.318  10.023  1.00 21.79 ? 44  TYR   A CA  1 
ATOM   336  C C   . TYR   A 1 43  ? 11.893  -5.023  10.448  1.00 23.69 ? 44  TYR   A C   1 
ATOM   337  O O   . TYR   A 1 43  ? 11.343  -4.266  11.254  1.00 26.16 ? 44  TYR   A O   1 
ATOM   338  C CB  . TYR   A 1 43  ? 10.157  -6.030  8.954   1.00 21.10 ? 44  TYR   A CB  1 
ATOM   339  C CG  . TYR   A 1 43  ? 9.485   -7.287  8.496   1.00 24.08 ? 44  TYR   A CG  1 
ATOM   340  C CD1 . TYR   A 1 43  ? 10.170  -8.198  7.701   1.00 21.77 ? 44  TYR   A CD1 1 
ATOM   341  C CD2 . TYR   A 1 43  ? 8.181   -7.582  8.874   1.00 23.73 ? 44  TYR   A CD2 1 
ATOM   342  C CE1 . TYR   A 1 43  ? 9.579   -9.364  7.290   1.00 20.68 ? 44  TYR   A CE1 1 
ATOM   343  C CE2 . TYR   A 1 43  ? 7.569   -8.753  8.456   1.00 22.38 ? 44  TYR   A CE2 1 
ATOM   344  C CZ  . TYR   A 1 43  ? 8.284   -9.640  7.658   1.00 22.03 ? 44  TYR   A CZ  1 
ATOM   345  O OH  . TYR   A 1 43  ? 7.712   -10.822 7.245   1.00 26.10 ? 44  TYR   A OH  1 
ATOM   346  N N   . TYR   A 1 44  ? 13.073  -4.800  9.890   1.00 19.71 ? 45  TYR   A N   1 
ATOM   347  C CA  . TYR   A 1 44  ? 13.803  -3.555  10.180  1.00 22.50 ? 45  TYR   A CA  1 
ATOM   348  C C   . TYR   A 1 44  ? 14.396  -2.951  8.922   1.00 22.65 ? 45  TYR   A C   1 
ATOM   349  O O   . TYR   A 1 44  ? 14.854  -3.683  8.049   1.00 22.47 ? 45  TYR   A O   1 
ATOM   350  C CB  . TYR   A 1 44  ? 15.029  -3.812  11.057  1.00 24.49 ? 45  TYR   A CB  1 
ATOM   351  C CG  . TYR   A 1 44  ? 14.808  -4.460  12.413  1.00 24.40 ? 45  TYR   A CG  1 
ATOM   352  C CD1 . TYR   A 1 44  ? 14.245  -3.754  13.464  1.00 30.44 ? 45  TYR   A CD1 1 
ATOM   353  C CD2 . TYR   A 1 44  ? 15.200  -5.770  12.641  1.00 26.63 ? 45  TYR   A CD2 1 
ATOM   354  C CE1 . TYR   A 1 44  ? 14.058  -4.342  14.703  1.00 29.86 ? 45  TYR   A CE1 1 
ATOM   355  C CE2 . TYR   A 1 44  ? 15.020  -6.370  13.874  1.00 31.93 ? 45  TYR   A CE2 1 
ATOM   356  C CZ  . TYR   A 1 44  ? 14.448  -5.653  14.906  1.00 30.43 ? 45  TYR   A CZ  1 
ATOM   357  O OH  . TYR   A 1 44  ? 14.278  -6.252  16.115  1.00 31.15 ? 45  TYR   A OH  1 
ATOM   358  N N   . GLY   A 1 45  ? 14.289  -1.635  8.795   1.00 22.00 ? 46  GLY   A N   1 
ATOM   359  C CA  . GLY   A 1 45  ? 15.042  -0.943  7.760   1.00 24.47 ? 46  GLY   A CA  1 
ATOM   360  C C   . GLY   A 1 45  ? 14.454  -1.050  6.360   1.00 23.20 ? 46  GLY   A C   1 
ATOM   361  O O   . GLY   A 1 45  ? 13.245  -1.228  6.171   1.00 21.72 ? 46  GLY   A O   1 
ATOM   362  N N   . LEU   A 1 46  ? 15.339  -0.932  5.367   1.00 24.45 ? 47  LEU   A N   1 
ATOM   363  C CA  . LEU   A 1 46  ? 14.968  -0.670  3.979   1.00 23.22 ? 47  LEU   A CA  1 
ATOM   364  C C   . LEU   A 1 46  ? 15.301  -1.840  3.058   1.00 22.34 ? 47  LEU   A C   1 
ATOM   365  O O   . LEU   A 1 46  ? 16.424  -2.364  3.072   1.00 23.95 ? 47  LEU   A O   1 
ATOM   366  C CB  . LEU   A 1 46  ? 15.671  0.589   3.461   1.00 24.69 ? 47  LEU   A CB  1 
ATOM   367  C CG  . LEU   A 1 46  ? 15.302  1.901   4.153   1.00 25.35 ? 47  LEU   A CG  1 
ATOM   368  C CD1 . LEU   A 1 46  ? 16.061  3.091   3.548   1.00 29.55 ? 47  LEU   A CD1 1 
ATOM   369  C CD2 . LEU   A 1 46  ? 13.796  2.142   4.085   1.00 24.35 ? 47  LEU   A CD2 1 
ATOM   370  N N   . GLN   A 1 47  ? 14.327  -2.206  2.229   1.00 23.26 ? 48  GLN   A N   1 
ATOM   371  C CA  . GLN   A 1 47  ? 14.553  -3.166  1.156   1.00 22.02 ? 48  GLN   A CA  1 
ATOM   372  C C   . GLN   A 1 47  ? 15.327  -2.526  0.009   1.00 25.94 ? 48  GLN   A C   1 
ATOM   373  O O   . GLN   A 1 47  ? 16.177  -3.173  -0.614  1.00 28.06 ? 48  GLN   A O   1 
ATOM   374  C CB  . GLN   A 1 47  ? 13.191  -3.713  0.704   1.00 27.50 ? 48  GLN   A CB  1 
ATOM   375  C CG  . GLN   A 1 47  ? 13.052  -4.133  -0.743  1.00 29.53 ? 48  GLN   A CG  1 
ATOM   376  C CD  . GLN   A 1 47  ? 11.597  -4.388  -1.140  1.00 27.38 ? 48  GLN   A CD  1 
ATOM   377  O OE1 . GLN   A 1 47  ? 10.776  -4.851  -0.329  1.00 24.99 ? 48  GLN   A OE1 1 
ATOM   378  N NE2 . GLN   A 1 47  ? 11.270  -4.083  -2.393  1.00 28.15 ? 48  GLN   A NE2 1 
ATOM   379  N N   . SER   A 1 48  ? 15.070  -1.245  -0.253  1.00 24.86 ? 49  SER   A N   1 
ATOM   380  C CA  . SER   A 1 48  ? 15.782  -0.469  -1.260  1.00 29.23 ? 49  SER   A CA  1 
ATOM   381  C C   . SER   A 1 48  ? 16.056  0.910   -0.686  1.00 29.50 ? 49  SER   A C   1 
ATOM   382  O O   . SER   A 1 48  ? 15.118  1.626   -0.320  1.00 28.79 ? 49  SER   A O   1 
ATOM   383  C CB  . SER   A 1 48  ? 14.971  -0.356  -2.554  1.00 33.00 ? 49  SER   A CB  1 
ATOM   384  O OG  . SER   A 1 48  ? 15.385  0.777   -3.297  1.00 33.19 ? 49  SER   A OG  1 
ATOM   385  N N   . VAL   A 1 49  ? 17.334  1.288   -0.621  1.00 26.44 ? 50  VAL   A N   1 
ATOM   386  C CA  . VAL   A 1 49  ? 17.693  2.593   -0.074  1.00 28.40 ? 50  VAL   A CA  1 
ATOM   387  C C   . VAL   A 1 49  ? 17.255  3.713   -1.013  1.00 32.20 ? 50  VAL   A C   1 
ATOM   388  O O   . VAL   A 1 49  ? 16.739  4.745   -0.568  1.00 31.98 ? 50  VAL   A O   1 
ATOM   389  C CB  . VAL   A 1 49  ? 19.202  2.655   0.211   1.00 33.40 ? 50  VAL   A CB  1 
ATOM   390  C CG1 . VAL   A 1 49  ? 19.611  4.066   0.609   1.00 35.89 ? 50  VAL   A CG1 1 
ATOM   391  C CG2 . VAL   A 1 49  ? 19.568  1.668   1.298   1.00 29.40 ? 50  VAL   A CG2 1 
ATOM   392  N N   . GLN   A 1 50  ? 17.442  3.528   -2.322  1.00 32.27 ? 51  GLN   A N   1 
ATOM   393  C CA  . GLN   A 1 50  ? 17.111  4.603   -3.254  1.00 33.39 ? 51  GLN   A CA  1 
ATOM   394  C C   . GLN   A 1 50  ? 15.607  4.820   -3.359  1.00 34.72 ? 51  GLN   A C   1 
ATOM   395  O O   . GLN   A 1 50  ? 15.163  5.935   -3.656  1.00 36.06 ? 51  GLN   A O   1 
ATOM   396  C CB  . GLN   A 1 50  ? 17.704  4.314   -4.634  1.00 35.07 ? 51  GLN   A CB  1 
ATOM   397  C CG  . GLN   A 1 50  ? 17.101  3.113   -5.344  1.00 38.39 ? 51  GLN   A CG  1 
ATOM   398  C CD  . GLN   A 1 50  ? 17.950  2.646   -6.511  1.00 45.41 ? 51  GLN   A CD  1 
ATOM   399  O OE1 . GLN   A 1 50  ? 18.911  1.894   -6.332  1.00 48.04 ? 51  GLN   A OE1 1 
ATOM   400  N NE2 . GLN   A 1 50  ? 17.602  3.091   -7.713  1.00 47.19 ? 51  GLN   A NE2 1 
ATOM   401  N N   . ASP   A 1 51  ? 14.810  3.783   -3.121  1.00 34.31 ? 52  ASP   A N   1 
ATOM   402  C CA  . ASP   A 1 51  ? 13.364  3.913   -3.184  1.00 36.43 ? 52  ASP   A CA  1 
ATOM   403  C C   . ASP   A 1 51  ? 12.729  4.148   -1.825  1.00 32.12 ? 52  ASP   A C   1 
ATOM   404  O O   . ASP   A 1 51  ? 11.518  4.370   -1.760  1.00 30.94 ? 52  ASP   A O   1 
ATOM   405  C CB  . ASP   A 1 51  ? 12.749  2.672   -3.831  1.00 36.28 ? 52  ASP   A CB  1 
ATOM   406  C CG  . ASP   A 1 51  ? 13.182  2.499   -5.268  1.00 39.45 ? 52  ASP   A CG  1 
ATOM   407  O OD1 . ASP   A 1 51  ? 12.888  3.407   -6.081  1.00 42.04 ? 52  ASP   A OD1 1 
ATOM   408  O OD2 . ASP   A 1 51  ? 13.825  1.472   -5.572  1.00 39.53 ? 52  ASP   A OD2 1 
ATOM   409  N N   . LYS   A 1 52  ? 13.512  4.107   -0.749  1.00 31.30 ? 53  LYS   A N   1 
ATOM   410  C CA  . LYS   A 1 52  ? 12.993  4.249   0.613   1.00 27.70 ? 53  LYS   A CA  1 
ATOM   411  C C   . LYS   A 1 52  ? 11.810  3.309   0.844   1.00 26.82 ? 53  LYS   A C   1 
ATOM   412  O O   . LYS   A 1 52  ? 10.808  3.662   1.469   1.00 23.88 ? 53  LYS   A O   1 
ATOM   413  C CB  . LYS   A 1 52  ? 12.618  5.699   0.909   1.00 31.27 ? 53  LYS   A CB  1 
ATOM   414  C CG  . LYS   A 1 52  ? 13.823  6.630   1.084   1.00 32.05 ? 53  LYS   A CG  1 
ATOM   415  C CD  . LYS   A 1 52  ? 14.362  6.555   2.508   1.00 33.43 ? 53  LYS   A CD  1 
ATOM   416  C CE  . LYS   A 1 52  ? 15.572  7.466   2.714   1.00 38.89 ? 53  LYS   A CE  1 
ATOM   417  N NZ  . LYS   A 1 52  ? 16.133  7.350   4.098   1.00 37.26 ? 53  LYS   A NZ  1 
ATOM   418  N N   . LYS   A 1 53  ? 11.925  2.101   0.308   1.00 25.99 ? 54  LYS   A N   1 
ATOM   419  C CA  . LYS   A 1 53  ? 10.911  1.072   0.483   1.00 23.60 ? 54  LYS   A CA  1 
ATOM   420  C C   . LYS   A 1 53  ? 11.300  0.219   1.683   1.00 22.96 ? 54  LYS   A C   1 
ATOM   421  O O   . LYS   A 1 53  ? 12.374  -0.388  1.689   1.00 24.96 ? 54  LYS   A O   1 
ATOM   422  C CB  . LYS   A 1 53  ? 10.802  0.214   -0.776  1.00 26.77 ? 54  LYS   A CB  1 
ATOM   423  C CG  . LYS   A 1 53  ? 9.888   -0.987  -0.649  1.00 29.59 ? 54  LYS   A CG  1 
ATOM   424  C CD  . LYS   A 1 53  ? 8.432   -0.610  -0.817  1.00 30.71 ? 54  LYS   A CD  1 
ATOM   425  C CE  . LYS   A 1 53  ? 7.566   -1.850  -0.979  1.00 37.03 ? 54  LYS   A CE  1 
ATOM   426  N NZ  . LYS   A 1 53  ? 6.204   -1.630  -0.432  1.00 43.82 ? 54  LYS   A NZ  1 
ATOM   427  N N   . ALA   A 1 54  ? 10.443  0.178   2.695   1.00 21.04 ? 55  ALA   A N   1 
ATOM   428  C CA  . ALA   A 1 54  ? 10.786  -0.539  3.916   1.00 23.39 ? 55  ALA   A CA  1 
ATOM   429  C C   . ALA   A 1 54  ? 10.654  -2.050  3.742   1.00 20.40 ? 55  ALA   A C   1 
ATOM   430  O O   . ALA   A 1 54  ? 9.787   -2.540  3.016   1.00 21.60 ? 55  ALA   A O   1 
ATOM   431  C CB  . ALA   A 1 54  ? 9.891   -0.091  5.066   1.00 22.71 ? 55  ALA   A CB  1 
ATOM   432  N N   . VAL   A 1 55  ? 11.522  -2.793  4.432   1.00 21.43 ? 56  VAL   A N   1 
ATOM   433  C CA  . VAL   A 1 55  ? 11.392  -4.247  4.453   1.00 19.55 ? 56  VAL   A CA  1 
ATOM   434  C C   . VAL   A 1 55  ? 10.039  -4.645  5.033   1.00 21.53 ? 56  VAL   A C   1 
ATOM   435  O O   . VAL   A 1 55  ? 9.584   -4.088  6.039   1.00 23.08 ? 56  VAL   A O   1 
ATOM   436  C CB  . VAL   A 1 55  ? 12.539  -4.879  5.261   1.00 18.77 ? 56  VAL   A CB  1 
ATOM   437  C CG1 . VAL   A 1 55  ? 12.349  -6.403  5.378   1.00 20.64 ? 56  VAL   A CG1 1 
ATOM   438  C CG2 . VAL   A 1 55  ? 13.880  -4.571  4.610   1.00 21.96 ? 56  VAL   A CG2 1 
ATOM   439  N N   . ASN   A 1 56  ? 9.396   -5.640  4.418   1.00 20.53 ? 57  ASN   A N   1 
ATOM   440  C CA  . ASN   A 1 56  ? 8.082   -6.082  4.865   1.00 18.71 ? 57  ASN   A CA  1 
ATOM   441  C C   . ASN   A 1 56  ? 7.910   -7.564  4.543   1.00 22.25 ? 57  ASN   A C   1 
ATOM   442  O O   . ASN   A 1 56  ? 8.813   -8.220  4.010   1.00 22.00 ? 57  ASN   A O   1 
ATOM   443  C CB  . ASN   A 1 56  ? 6.978   -5.242  4.215   1.00 24.68 ? 57  ASN   A CB  1 
ATOM   444  C CG  . ASN   A 1 56  ? 7.007   -5.333  2.697   1.00 27.94 ? 57  ASN   A CG  1 
ATOM   445  O OD1 . ASN   A 1 56  ? 6.399   -6.226  2.107   1.00 32.44 ? 57  ASN   A OD1 1 
ATOM   446  N ND2 . ASN   A 1 56  ? 7.755   -4.436  2.062   1.00 31.55 ? 57  ASN   A ND2 1 
ATOM   447  N N   . SER   A 1 57  ? 6.723   -8.090  4.861   1.00 22.26 ? 58  SER   A N   1 
ATOM   448  C CA  . SER   A 1 57  ? 6.461   -9.517  4.679   1.00 23.80 ? 58  SER   A CA  1 
ATOM   449  C C   . SER   A 1 57  ? 6.482   -9.958  3.220   1.00 23.89 ? 58  SER   A C   1 
ATOM   450  O O   . SER   A 1 57  ? 6.524   -11.168 2.966   1.00 23.42 ? 58  SER   A O   1 
ATOM   451  C CB  . SER   A 1 57  ? 5.120   -9.897  5.313   1.00 26.29 ? 58  SER   A CB  1 
ATOM   452  O OG  . SER   A 1 57  ? 4.061   -9.117  4.795   1.00 32.11 ? 58  SER   A OG  1 
ATOM   453  N N   . SER   A 1 58  ? 6.431   -9.024  2.263   1.00 22.66 ? 59  SER   A N   1 
ATOM   454  C CA  . SER   A 1 58  ? 6.533   -9.358  0.849   1.00 22.19 ? 59  SER   A CA  1 
ATOM   455  C C   . SER   A 1 58  ? 7.946   -9.229  0.305   1.00 20.87 ? 59  SER   A C   1 
ATOM   456  O O   . SER   A 1 58  ? 8.174   -9.589  -0.855  1.00 23.66 ? 59  SER   A O   1 
ATOM   457  C CB  . SER   A 1 58  ? 5.617   -8.455  0.004   1.00 25.59 ? 59  SER   A CB  1 
ATOM   458  O OG  . SER   A 1 58  ? 4.249   -8.737  0.227   1.00 29.39 ? 59  SER   A OG  1 
ATOM   459  N N   . THR   A 1 59  ? 8.886   -8.720  1.099   1.00 22.00 ? 60  THR   A N   1 
ATOM   460  C CA  . THR   A 1 59  ? 10.241  -8.490  0.602   1.00 22.36 ? 60  THR   A CA  1 
ATOM   461  C C   . THR   A 1 59  ? 10.911  -9.814  0.259   1.00 19.69 ? 60  THR   A C   1 
ATOM   462  O O   . THR   A 1 59  ? 10.936  -10.739 1.077   1.00 18.11 ? 60  THR   A O   1 
ATOM   463  C CB  . THR   A 1 59  ? 11.074  -7.726  1.633   1.00 21.60 ? 60  THR   A CB  1 
ATOM   464  O OG1 . THR   A 1 59  ? 10.483  -6.440  1.862   1.00 19.36 ? 60  THR   A OG1 1 
ATOM   465  C CG2 . THR   A 1 59  ? 12.512  -7.521  1.134   1.00 20.74 ? 60  THR   A CG2 1 
ATOM   466  N N   . ILE   A 1 60  ? 11.457  -9.898  -0.956  1.00 19.43 ? 61  ILE   A N   1 
ATOM   467  C CA  . ILE   A 1 60  ? 12.176  -11.080 -1.438  1.00 18.88 ? 61  ILE   A CA  1 
ATOM   468  C C   . ILE   A 1 60  ? 13.673  -10.842 -1.268  1.00 18.02 ? 61  ILE   A C   1 
ATOM   469  O O   . ILE   A 1 60  ? 14.210  -9.840  -1.757  1.00 20.32 ? 61  ILE   A O   1 
ATOM   470  C CB  . ILE   A 1 60  ? 11.818  -11.372 -2.912  1.00 20.50 ? 61  ILE   A CB  1 
ATOM   471  C CG1 . ILE   A 1 60  ? 10.332  -11.708 -3.039  1.00 22.82 ? 61  ILE   A CG1 1 
ATOM   472  C CG2 . ILE   A 1 60  ? 12.631  -12.532 -3.468  1.00 19.17 ? 61  ILE   A CG2 1 
ATOM   473  C CD1 . ILE   A 1 60  ? 9.752   -11.486 -4.469  1.00 22.28 ? 61  ILE   A CD1 1 
ATOM   474  N N   . PHE   A 1 61  ? 14.347  -11.763 -0.570  1.00 19.16 ? 62  PHE   A N   1 
ATOM   475  C CA  . PHE   A 1 61  ? 15.790  -11.738 -0.364  1.00 19.05 ? 62  PHE   A CA  1 
ATOM   476  C C   . PHE   A 1 61  ? 16.440  -12.890 -1.121  1.00 18.55 ? 62  PHE   A C   1 
ATOM   477  O O   . PHE   A 1 61  ? 15.834  -13.949 -1.288  1.00 20.15 ? 62  PHE   A O   1 
ATOM   478  C CB  . PHE   A 1 61  ? 16.166  -11.904 1.112   1.00 19.03 ? 62  PHE   A CB  1 
ATOM   479  C CG  . PHE   A 1 61  ? 15.688  -10.801 2.021   1.00 18.72 ? 62  PHE   A CG  1 
ATOM   480  C CD1 . PHE   A 1 61  ? 14.386  -10.781 2.493   1.00 19.54 ? 62  PHE   A CD1 1 
ATOM   481  C CD2 . PHE   A 1 61  ? 16.582  -9.851  2.490   1.00 18.93 ? 62  PHE   A CD2 1 
ATOM   482  C CE1 . PHE   A 1 61  ? 13.955  -9.789  3.365   1.00 18.99 ? 62  PHE   A CE1 1 
ATOM   483  C CE2 . PHE   A 1 61  ? 16.163  -8.858  3.365   1.00 22.00 ? 62  PHE   A CE2 1 
ATOM   484  C CZ  . PHE   A 1 61  ? 14.844  -8.829  3.803   1.00 19.08 ? 62  PHE   A CZ  1 
ATOM   485  N N   . GLU   A 1 62  ? 17.679  -12.680 -1.559  1.00 18.96 ? 63  GLU   A N   1 
ATOM   486  C CA  . GLU   A 1 62  ? 18.501  -13.784 -2.050  1.00 17.42 ? 63  GLU   A CA  1 
ATOM   487  C C   . GLU   A 1 62  ? 18.997  -14.625 -0.879  1.00 19.22 ? 63  GLU   A C   1 
ATOM   488  O O   . GLU   A 1 62  ? 19.589  -14.105 0.072   1.00 19.84 ? 63  GLU   A O   1 
ATOM   489  C CB  . GLU   A 1 62  ? 19.680  -13.260 -2.865  1.00 16.26 ? 63  GLU   A CB  1 
ATOM   490  C CG  . GLU   A 1 62  ? 19.244  -12.531 -4.116  1.00 18.65 ? 63  GLU   A CG  1 
ATOM   491  C CD  . GLU   A 1 62  ? 20.389  -11.926 -4.907  1.00 28.98 ? 63  GLU   A CD  1 
ATOM   492  O OE1 . GLU   A 1 62  ? 21.554  -12.293 -4.675  1.00 29.74 ? 63  GLU   A OE1 1 
ATOM   493  O OE2 . GLU   A 1 62  ? 20.109  -11.073 -5.770  1.00 30.85 ? 63  GLU   A OE2 1 
ATOM   494  N N   . LEU   A 1 63  ? 18.774  -15.936 -0.955  1.00 15.97 ? 64  LEU   A N   1 
ATOM   495  C CA  . LEU   A 1 63  ? 19.226  -16.813 0.117   1.00 15.15 ? 64  LEU   A CA  1 
ATOM   496  C C   . LEU   A 1 63  ? 20.675  -17.245 -0.023  1.00 15.59 ? 64  LEU   A C   1 
ATOM   497  O O   . LEU   A 1 63  ? 21.213  -17.833 0.923   1.00 16.01 ? 64  LEU   A O   1 
ATOM   498  C CB  . LEU   A 1 63  ? 18.354  -18.072 0.178   1.00 15.73 ? 64  LEU   A CB  1 
ATOM   499  C CG  . LEU   A 1 63  ? 16.845  -17.893 0.263   1.00 15.56 ? 64  LEU   A CG  1 
ATOM   500  C CD1 . LEU   A 1 63  ? 16.198  -19.286 0.324   1.00 15.22 ? 64  LEU   A CD1 1 
ATOM   501  C CD2 . LEU   A 1 63  ? 16.452  -17.045 1.497   1.00 20.31 ? 64  LEU   A CD2 1 
ATOM   502  N N   . GLY   A 1 64  ? 21.303  -17.025 -1.177  1.00 16.32 ? 65  GLY   A N   1 
ATOM   503  C CA  . GLY   A 1 64  ? 22.706  -17.398 -1.281  1.00 17.49 ? 65  GLY   A CA  1 
ATOM   504  C C   . GLY   A 1 64  ? 22.905  -18.883 -1.037  1.00 15.06 ? 65  GLY   A C   1 
ATOM   505  O O   . GLY   A 1 64  ? 22.118  -19.722 -1.475  1.00 15.72 ? 65  GLY   A O   1 
ATOM   506  N N   . SER   A 1 65  ? 23.963  -19.215 -0.298  1.00 15.52 ? 66  SER   A N   1 
ATOM   507  C CA  . SER   A 1 65  ? 24.309  -20.620 -0.115  1.00 17.35 ? 66  SER   A CA  1 
ATOM   508  C C   . SER   A 1 65  ? 23.238  -21.409 0.633   1.00 15.89 ? 66  SER   A C   1 
ATOM   509  O O   . SER   A 1 65  ? 23.270  -22.642 0.606   1.00 17.33 ? 66  SER   A O   1 
ATOM   510  C CB  . SER   A 1 65  ? 25.652  -20.719 0.606   1.00 19.18 ? 66  SER   A CB  1 
ATOM   511  O OG  . SER   A 1 65  ? 26.534  -19.726 0.093   1.00 23.65 ? 66  SER   A OG  1 
ATOM   512  N N   . VAL   A 1 66  ? 22.302  -20.744 1.325   1.00 14.47 ? 67  VAL   A N   1 
ATOM   513  C CA  . VAL   A 1 66  ? 21.183  -21.454 1.953   1.00 14.60 ? 67  VAL   A CA  1 
ATOM   514  C C   . VAL   A 1 66  ? 20.279  -22.098 0.910   1.00 16.60 ? 67  VAL   A C   1 
ATOM   515  O O   . VAL   A 1 66  ? 19.520  -23.027 1.221   1.00 17.14 ? 67  VAL   A O   1 
ATOM   516  C CB  . VAL   A 1 66  ? 20.456  -20.479 2.912   1.00 16.02 ? 67  VAL   A CB  1 
ATOM   517  C CG1 . VAL   A 1 66  ? 19.068  -20.962 3.326   1.00 17.34 ? 67  VAL   A CG1 1 
ATOM   518  C CG2 . VAL   A 1 66  ? 21.301  -20.245 4.163   1.00 16.42 ? 67  VAL   A CG2 1 
ATOM   519  N N   . SER   A 1 67  ? 20.417  -21.697 -0.354  1.00 16.11 ? 68  SER   A N   1 
ATOM   520  C CA  . SER   A 1 67  ? 19.690  -22.360 -1.437  1.00 13.14 ? 68  SER   A CA  1 
ATOM   521  C C   . SER   A 1 67  ? 19.956  -23.862 -1.471  1.00 13.40 ? 68  SER   A C   1 
ATOM   522  O O   . SER   A 1 67  ? 19.119  -24.625 -1.963  1.00 15.33 ? 68  SER   A O   1 
ATOM   523  C CB  . SER   A 1 67  ? 20.091  -21.758 -2.781  1.00 12.76 ? 68  SER   A CB  1 
ATOM   524  O OG  . SER   A 1 67  ? 19.869  -20.361 -2.827  1.00 15.96 ? 68  SER   A OG  1 
ATOM   525  N N   . LYS   A 1 68  ? 21.133  -24.292 -1.000  1.00 12.62 ? 69  LYS   A N   1 
ATOM   526  C CA  . LYS   A 1 68  ? 21.477  -25.715 -1.011  1.00 10.71 ? 69  LYS   A CA  1 
ATOM   527  C C   . LYS   A 1 68  ? 20.478  -26.557 -0.231  1.00 13.50 ? 69  LYS   A C   1 
ATOM   528  O O   . LYS   A 1 68  ? 20.355  -27.760 -0.495  1.00 14.34 ? 69  LYS   A O   1 
ATOM   529  C CB  . LYS   A 1 68  ? 22.880  -25.922 -0.450  1.00 14.72 ? 69  LYS   A CB  1 
ATOM   530  C CG  . LYS   A 1 68  ? 23.975  -25.322 -1.321  1.00 12.96 ? 69  LYS   A CG  1 
ATOM   531  C CD  . LYS   A 1 68  ? 25.380  -25.644 -0.799  1.00 13.59 ? 69  LYS   A CD  1 
ATOM   532  C CE  . LYS   A 1 68  ? 26.431  -24.985 -1.696  1.00 15.07 ? 69  LYS   A CE  1 
ATOM   533  N NZ  . LYS   A 1 68  ? 26.504  -23.498 -1.514  1.00 16.64 ? 69  LYS   A NZ  1 
ATOM   534  N N   . LEU   A 1 69  ? 19.787  -25.959 0.749   1.00 12.74 ? 70  LEU   A N   1 
ATOM   535  C CA  . LEU   A 1 69  ? 18.787  -26.717 1.499   1.00 12.30 ? 70  LEU   A CA  1 
ATOM   536  C C   . LEU   A 1 69  ? 17.626  -27.127 0.603   1.00 13.40 ? 70  LEU   A C   1 
ATOM   537  O O   . LEU   A 1 69  ? 17.032  -28.191 0.805   1.00 15.10 ? 70  LEU   A O   1 
ATOM   538  C CB  . LEU   A 1 69  ? 18.256  -25.895 2.684   1.00 13.42 ? 70  LEU   A CB  1 
ATOM   539  C CG  . LEU   A 1 69  ? 19.299  -25.383 3.687   1.00 13.16 ? 70  LEU   A CG  1 
ATOM   540  C CD1 . LEU   A 1 69  ? 18.586  -24.639 4.843   1.00 13.64 ? 70  LEU   A CD1 1 
ATOM   541  C CD2 . LEU   A 1 69  ? 20.100  -26.539 4.227   1.00 13.09 ? 70  LEU   A CD2 1 
ATOM   542  N N   . PHE   A 1 70  ? 17.288  -26.303 -0.383  1.00 14.36 ? 71  PHE   A N   1 
ATOM   543  C CA  . PHE   A 1 70  ? 16.215  -26.683 -1.299  1.00 14.34 ? 71  PHE   A CA  1 
ATOM   544  C C   . PHE   A 1 70  ? 16.692  -27.711 -2.312  1.00 13.94 ? 71  PHE   A C   1 
ATOM   545  O O   . PHE   A 1 70  ? 15.936  -28.607 -2.698  1.00 14.96 ? 71  PHE   A O   1 
ATOM   546  C CB  . PHE   A 1 70  ? 15.657  -25.430 -1.974  1.00 15.11 ? 71  PHE   A CB  1 
ATOM   547  C CG  . PHE   A 1 70  ? 14.913  -24.552 -1.016  1.00 15.03 ? 71  PHE   A CG  1 
ATOM   548  C CD1 . PHE   A 1 70  ? 13.667  -24.931 -0.567  1.00 16.01 ? 71  PHE   A CD1 1 
ATOM   549  C CD2 . PHE   A 1 70  ? 15.485  -23.407 -0.501  1.00 18.68 ? 71  PHE   A CD2 1 
ATOM   550  C CE1 . PHE   A 1 70  ? 12.970  -24.158 0.344   1.00 17.19 ? 71  PHE   A CE1 1 
ATOM   551  C CE2 . PHE   A 1 70  ? 14.798  -22.623 0.413   1.00 19.96 ? 71  PHE   A CE2 1 
ATOM   552  C CZ  . PHE   A 1 70  ? 13.543  -23.000 0.843   1.00 20.55 ? 71  PHE   A CZ  1 
ATOM   553  N N   . THR   A 1 71  ? 17.939  -27.592 -2.763  1.00 15.03 ? 72  THR   A N   1 
ATOM   554  C CA  . THR   A 1 71  ? 18.515  -28.633 -3.606  1.00 14.19 ? 72  THR   A CA  1 
ATOM   555  C C   . THR   A 1 71  ? 18.521  -29.964 -2.875  1.00 14.16 ? 72  THR   A C   1 
ATOM   556  O O   . THR   A 1 71  ? 18.192  -31.007 -3.455  1.00 13.62 ? 72  THR   A O   1 
ATOM   557  C CB  . THR   A 1 71  ? 19.934  -28.233 -3.999  1.00 14.62 ? 72  THR   A CB  1 
ATOM   558  O OG1 . THR   A 1 71  ? 19.887  -26.939 -4.603  1.00 14.04 ? 72  THR   A OG1 1 
ATOM   559  C CG2 . THR   A 1 71  ? 20.540  -29.242 -4.976  1.00 14.25 ? 72  THR   A CG2 1 
ATOM   560  N N   . ALA   A 1 72  ? 18.895  -29.939 -1.598  1.00 13.81 ? 73  ALA   A N   1 
ATOM   561  C CA  . ALA   A 1 72  ? 18.886  -31.153 -0.794  1.00 13.20 ? 73  ALA   A CA  1 
ATOM   562  C C   . ALA   A 1 72  ? 17.491  -31.753 -0.726  1.00 14.71 ? 73  ALA   A C   1 
ATOM   563  O O   . ALA   A 1 72  ? 17.318  -32.969 -0.858  1.00 14.30 ? 73  ALA   A O   1 
ATOM   564  C CB  . ALA   A 1 72  ? 19.401  -30.836 0.607   1.00 15.47 ? 73  ALA   A CB  1 
ATOM   565  N N   . THR   A 1 73  ? 16.487  -30.915 -0.483  1.00 14.47 ? 74  THR   A N   1 
ATOM   566  C CA  . THR   A 1 73  ? 15.115  -31.399 -0.390  1.00 13.42 ? 74  THR   A CA  1 
ATOM   567  C C   . THR   A 1 73  ? 14.657  -31.985 -1.724  1.00 14.47 ? 74  THR   A C   1 
ATOM   568  O O   . THR   A 1 73  ? 13.974  -33.016 -1.765  1.00 14.35 ? 74  THR   A O   1 
ATOM   569  C CB  . THR   A 1 73  ? 14.213  -30.240 0.050   1.00 15.37 ? 74  THR   A CB  1 
ATOM   570  O OG1 . THR   A 1 73  ? 14.726  -29.672 1.269   1.00 15.74 ? 74  THR   A OG1 1 
ATOM   571  C CG2 . THR   A 1 73  ? 12.783  -30.691 0.258   1.00 15.87 ? 74  THR   A CG2 1 
ATOM   572  N N   . ALA   A 1 74  ? 15.018  -31.328 -2.828  1.00 14.57 ? 75  ALA   A N   1 
ATOM   573  C CA  . ALA   A 1 74  ? 14.693  -31.859 -4.153  1.00 15.70 ? 75  ALA   A CA  1 
ATOM   574  C C   . ALA   A 1 74  ? 15.341  -33.220 -4.373  1.00 16.76 ? 75  ALA   A C   1 
ATOM   575  O O   . ALA   A 1 74  ? 14.715  -34.143 -4.910  1.00 15.37 ? 75  ALA   A O   1 
ATOM   576  C CB  . ALA   A 1 74  ? 15.150  -30.875 -5.234  1.00 15.49 ? 75  ALA   A CB  1 
ATOM   577  N N   . GLY   A 1 75  ? 16.591  -33.376 -3.939  1.00 14.40 ? 76  GLY   A N   1 
ATOM   578  C CA  . GLY   A 1 75  ? 17.247  -34.673 -4.073  1.00 15.66 ? 76  GLY   A CA  1 
ATOM   579  C C   . GLY   A 1 75  ? 16.602  -35.737 -3.208  1.00 15.81 ? 76  GLY   A C   1 
ATOM   580  O O   . GLY   A 1 75  ? 16.457  -36.891 -3.635  1.00 15.52 ? 76  GLY   A O   1 
ATOM   581  N N   . GLY   A 1 76  ? 16.236  -35.376 -1.974  1.00 14.85 ? 77  GLY   A N   1 
ATOM   582  C CA  . GLY   A 1 76  ? 15.532  -36.324 -1.120  1.00 15.58 ? 77  GLY   A CA  1 
ATOM   583  C C   . GLY   A 1 76  ? 14.198  -36.717 -1.712  1.00 16.46 ? 77  GLY   A C   1 
ATOM   584  O O   . GLY   A 1 76  ? 13.772  -37.873 -1.614  1.00 17.71 ? 77  GLY   A O   1 
ATOM   585  N N   . TYR   A 1 77  ? 13.544  -35.767 -2.379  1.00 14.58 ? 78  TYR   A N   1 
ATOM   586  C CA  . TYR   A 1 77  ? 12.276  -36.040 -3.035  1.00 14.89 ? 78  TYR   A CA  1 
ATOM   587  C C   . TYR   A 1 77  ? 12.462  -37.023 -4.181  1.00 17.50 ? 78  TYR   A C   1 
ATOM   588  O O   . TYR   A 1 77  ? 11.748  -38.032 -4.270  1.00 17.08 ? 78  TYR   A O   1 
ATOM   589  C CB  . TYR   A 1 77  ? 11.687  -34.710 -3.516  1.00 13.77 ? 78  TYR   A CB  1 
ATOM   590  C CG  . TYR   A 1 77  ? 10.363  -34.801 -4.210  1.00 16.19 ? 78  TYR   A CG  1 
ATOM   591  C CD1 . TYR   A 1 77  ? 10.288  -35.058 -5.569  1.00 20.51 ? 78  TYR   A CD1 1 
ATOM   592  C CD2 . TYR   A 1 77  ? 9.183   -34.605 -3.507  1.00 16.01 ? 78  TYR   A CD2 1 
ATOM   593  C CE1 . TYR   A 1 77  ? 9.054   -35.149 -6.213  1.00 21.40 ? 78  TYR   A CE1 1 
ATOM   594  C CE2 . TYR   A 1 77  ? 7.957   -34.661 -4.153  1.00 20.58 ? 78  TYR   A CE2 1 
ATOM   595  C CZ  . TYR   A 1 77  ? 7.907   -34.947 -5.496  1.00 19.81 ? 78  TYR   A CZ  1 
ATOM   596  O OH  . TYR   A 1 77  ? 6.689   -35.017 -6.129  1.00 22.72 ? 78  TYR   A OH  1 
ATOM   597  N N   . ALA   A 1 78  ? 13.415  -36.738 -5.078  1.00 14.34 ? 79  ALA   A N   1 
ATOM   598  C CA  . ALA   A 1 78  ? 13.667  -37.650 -6.193  1.00 16.60 ? 79  ALA   A CA  1 
ATOM   599  C C   . ALA   A 1 78  ? 14.090  -39.043 -5.709  1.00 17.10 ? 79  ALA   A C   1 
ATOM   600  O O   . ALA   A 1 78  ? 13.663  -40.061 -6.269  1.00 18.16 ? 79  ALA   A O   1 
ATOM   601  C CB  . ALA   A 1 78  ? 14.719  -37.051 -7.125  1.00 17.68 ? 79  ALA   A CB  1 
ATOM   602  N N   . LYS   A 1 79  ? 14.946  -39.115 -4.685  1.00 15.19 ? 80  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 79  ? 15.378  -40.426 -4.201  1.00 16.19 ? 80  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 79  ? 14.206  -41.224 -3.645  1.00 17.33 ? 80  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 79  ? 14.073  -42.423 -3.918  1.00 19.10 ? 80  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 79  ? 16.475  -40.256 -3.139  1.00 16.21 ? 80  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 79  ? 16.994  -41.557 -2.538  1.00 17.31 ? 80  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 79  ? 16.317  -41.837 -1.206  1.00 20.10 ? 80  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 79  ? 16.937  -43.007 -0.479  1.00 23.07 ? 80  LYS   A CE  1 
ATOM   610  N NZ  . LYS   A 1 79  ? 16.088  -43.390 0.692   1.00 25.38 ? 80  LYS   A NZ  1 
ATOM   611  N N   . ASN   A 1 80  ? 13.330  -40.579 -2.883  1.00 15.97 ? 81  ASN   A N   1 
ATOM   612  C CA  . ASN   A 1 80  ? 12.246  -41.325 -2.262  1.00 19.55 ? 81  ASN   A CA  1 
ATOM   613  C C   . ASN   A 1 80  ? 11.073  -41.579 -3.201  1.00 19.92 ? 81  ASN   A C   1 
ATOM   614  O O   . ASN   A 1 80  ? 10.159  -42.323 -2.828  1.00 23.21 ? 81  ASN   A O   1 
ATOM   615  C CB  . ASN   A 1 80  ? 11.807  -40.615 -0.985  1.00 20.31 ? 81  ASN   A CB  1 
ATOM   616  C CG  . ASN   A 1 80  ? 12.767  -40.897 0.168   1.00 21.61 ? 81  ASN   A CG  1 
ATOM   617  O OD1 . ASN   A 1 80  ? 12.792  -42.012 0.701   1.00 24.27 ? 81  ASN   A OD1 1 
ATOM   618  N ND2 . ASN   A 1 80  ? 13.595  -39.909 0.523   1.00 19.13 ? 81  ASN   A ND2 1 
ATOM   619  N N   . LYS   A 1 81  ? 11.094  -41.024 -4.409  1.00 19.64 ? 82  LYS   A N   1 
ATOM   620  C CA  . LYS   A 1 81  ? 10.179  -41.433 -5.469  1.00 22.38 ? 82  LYS   A CA  1 
ATOM   621  C C   . LYS   A 1 81  ? 10.821  -42.441 -6.418  1.00 22.26 ? 82  LYS   A C   1 
ATOM   622  O O   . LYS   A 1 81  ? 10.209  -42.817 -7.428  1.00 25.01 ? 82  LYS   A O   1 
ATOM   623  C CB  . LYS   A 1 81  ? 9.664   -40.210 -6.239  1.00 24.15 ? 82  LYS   A CB  1 
ATOM   624  C CG  . LYS   A 1 81  ? 8.641   -39.396 -5.440  1.00 25.32 ? 82  LYS   A CG  1 
ATOM   625  C CD  . LYS   A 1 81  ? 7.689   -38.596 -6.308  1.00 29.34 ? 82  LYS   A CD  1 
ATOM   626  C CE  . LYS   A 1 81  ? 6.662   -39.494 -7.010  1.00 30.83 ? 82  LYS   A CE  1 
ATOM   627  N NZ  . LYS   A 1 81  ? 5.720   -40.211 -6.085  1.00 35.55 ? 82  LYS   A NZ  1 
ATOM   628  N N   . GLY   A 1 82  ? 12.022  -42.915 -6.092  1.00 24.28 ? 83  GLY   A N   1 
ATOM   629  C CA  . GLY   A 1 82  ? 12.709  -43.888 -6.915  1.00 23.93 ? 83  GLY   A CA  1 
ATOM   630  C C   . GLY   A 1 82  ? 13.295  -43.339 -8.193  1.00 23.69 ? 83  GLY   A C   1 
ATOM   631  O O   . GLY   A 1 82  ? 13.693  -44.129 -9.052  1.00 23.00 ? 83  GLY   A O   1 
ATOM   632  N N   . LYS   A 1 83  ? 13.368  -42.004 -8.345  1.00 20.59 ? 84  LYS   A N   1 
ATOM   633  C CA  . LYS   A 1 83  ? 13.916  -41.407 -9.560  1.00 17.58 ? 84  LYS   A CA  1 
ATOM   634  C C   . LYS   A 1 83  ? 15.435  -41.468 -9.608  1.00 19.80 ? 84  LYS   A C   1 
ATOM   635  O O   . LYS   A 1 83  ? 16.013  -41.480 -10.701 1.00 19.88 ? 84  LYS   A O   1 
ATOM   636  C CB  . LYS   A 1 83  ? 13.467  -39.951 -9.691  1.00 17.88 ? 84  LYS   A CB  1 
ATOM   637  C CG  . LYS   A 1 83  ? 11.966  -39.774 -9.640  1.00 22.77 ? 84  LYS   A CG  1 
ATOM   638  C CD  . LYS   A 1 83  ? 11.303  -40.406 -10.849 1.00 27.31 ? 84  LYS   A CD  1 
ATOM   639  C CE  . LYS   A 1 83  ? 9.794   -40.147 -10.859 1.00 32.55 ? 84  LYS   A CE  1 
ATOM   640  N NZ  . LYS   A 1 83  ? 9.116   -40.863 -11.985 1.00 36.34 ? 84  LYS   A NZ  1 
ATOM   641  N N   . ILE   A 1 84  ? 16.091  -41.479 -8.443  1.00 18.66 ? 85  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 84  ? 17.530  -41.680 -8.331  1.00 18.33 ? 85  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 84  ? 17.764  -42.602 -7.149  1.00 19.00 ? 85  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 84  ? 16.896  -42.781 -6.287  1.00 19.87 ? 85  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 84  ? 18.351  -40.382 -8.112  1.00 16.88 ? 85  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 84  ? 17.899  -39.671 -6.835  1.00 16.62 ? 85  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 84  ? 18.277  -39.465 -9.309  1.00 18.88 ? 85  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 84  ? 18.727  -38.431 -6.498  1.00 17.67 ? 85  ILE   A CD1 1 
ATOM   649  N N   . SER   A 1 85  ? 18.951  -43.202 -7.138  1.00 17.31 ? 86  SER   A N   1 
ATOM   650  C CA  . SER   A 1 85  ? 19.549  -43.800 -5.958  1.00 17.55 ? 86  SER   A CA  1 
ATOM   651  C C   . SER   A 1 85  ? 20.788  -42.988 -5.627  1.00 17.08 ? 86  SER   A C   1 
ATOM   652  O O   . SER   A 1 85  ? 21.478  -42.512 -6.534  1.00 16.70 ? 86  SER   A O   1 
ATOM   653  C CB  . SER   A 1 85  ? 19.938  -45.259 -6.208  1.00 19.14 ? 86  SER   A CB  1 
ATOM   654  O OG  . SER   A 1 85  ? 20.886  -45.686 -5.249  1.00 24.39 ? 86  SER   A OG  1 
ATOM   655  N N   . PHE   A 1 86  ? 21.065  -42.826 -4.331  1.00 18.43 ? 87  PHE   A N   1 
ATOM   656  C CA  . PHE   A 1 86  ? 22.258  -42.077 -3.954  1.00 20.41 ? 87  PHE   A CA  1 
ATOM   657  C C   . PHE   A 1 86  ? 23.538  -42.830 -4.301  1.00 17.91 ? 87  PHE   A C   1 
ATOM   658  O O   . PHE   A 1 86  ? 24.615  -42.210 -4.319  1.00 18.63 ? 87  PHE   A O   1 
ATOM   659  C CB  . PHE   A 1 86  ? 22.214  -41.727 -2.459  1.00 18.47 ? 87  PHE   A CB  1 
ATOM   660  C CG  . PHE   A 1 86  ? 21.209  -40.646 -2.107  1.00 19.42 ? 87  PHE   A CG  1 
ATOM   661  C CD1 . PHE   A 1 86  ? 20.780  -39.723 -3.063  1.00 21.00 ? 87  PHE   A CD1 1 
ATOM   662  C CD2 . PHE   A 1 86  ? 20.668  -40.573 -0.825  1.00 19.19 ? 87  PHE   A CD2 1 
ATOM   663  C CE1 . PHE   A 1 86  ? 19.854  -38.731 -2.744  1.00 22.18 ? 87  PHE   A CE1 1 
ATOM   664  C CE2 . PHE   A 1 86  ? 19.744  -39.574 -0.500  1.00 19.75 ? 87  PHE   A CE2 1 
ATOM   665  C CZ  . PHE   A 1 86  ? 19.336  -38.665 -1.444  1.00 20.29 ? 87  PHE   A CZ  1 
ATOM   666  N N   . ASP   A 1 87  ? 23.448  -44.128 -4.622  1.00 18.46 ? 88  ASP   A N   1 
ATOM   667  C CA  . ASP   A 1 87  ? 24.618  -44.848 -5.111  1.00 19.87 ? 88  ASP   A CA  1 
ATOM   668  C C   . ASP   A 1 87  ? 24.817  -44.706 -6.615  1.00 18.18 ? 88  ASP   A C   1 
ATOM   669  O O   . ASP   A 1 87  ? 25.815  -45.222 -7.130  1.00 21.22 ? 88  ASP   A O   1 
ATOM   670  C CB  . ASP   A 1 87  ? 24.532  -46.342 -4.785  1.00 23.74 ? 88  ASP   A CB  1 
ATOM   671  C CG  . ASP   A 1 87  ? 24.626  -46.629 -3.305  1.00 30.46 ? 88  ASP   A CG  1 
ATOM   672  O OD1 . ASP   A 1 87  ? 25.437  -45.960 -2.623  1.00 31.13 ? 88  ASP   A OD1 1 
ATOM   673  O OD2 . ASP   A 1 87  ? 23.901  -47.536 -2.831  1.00 40.91 ? 88  ASP   A OD2 1 
ATOM   674  N N   . ASP   A 1 88  ? 23.885  -44.069 -7.334  1.00 16.54 ? 89  ASP   A N   1 
ATOM   675  C CA  . ASP   A 1 88  ? 24.077  -43.868 -8.769  1.00 17.84 ? 89  ASP   A CA  1 
ATOM   676  C C   . ASP   A 1 88  ? 25.218  -42.890 -9.018  1.00 18.62 ? 89  ASP   A C   1 
ATOM   677  O O   . ASP   A 1 88  ? 25.630  -42.147 -8.133  1.00 16.17 ? 89  ASP   A O   1 
ATOM   678  C CB  . ASP   A 1 88  ? 22.821  -43.308 -9.439  1.00 19.28 ? 89  ASP   A CB  1 
ATOM   679  C CG  . ASP   A 1 88  ? 21.655  -44.259 -9.405  1.00 20.02 ? 89  ASP   A CG  1 
ATOM   680  O OD1 . ASP   A 1 88  ? 21.867  -45.474 -9.210  1.00 22.78 ? 89  ASP   A OD1 1 
ATOM   681  O OD2 . ASP   A 1 88  ? 20.519  -43.764 -9.580  1.00 22.88 ? 89  ASP   A OD2 1 
ATOM   682  N N   . THR   A 1 89  ? 25.720  -42.885 -10.251 1.00 20.46 ? 90  THR   A N   1 
ATOM   683  C CA  . THR   A 1 89  ? 26.734  -41.918 -10.651 1.00 19.06 ? 90  THR   A CA  1 
ATOM   684  C C   . THR   A 1 89  ? 26.156  -40.986 -11.718 1.00 18.16 ? 90  THR   A C   1 
ATOM   685  O O   . THR   A 1 89  ? 25.120  -41.293 -12.315 1.00 18.39 ? 90  THR   A O   1 
ATOM   686  C CB  . THR   A 1 89  ? 27.983  -42.651 -11.159 1.00 22.34 ? 90  THR   A CB  1 
ATOM   687  O OG1 . THR   A 1 89  ? 27.631  -43.521 -12.244 1.00 21.80 ? 90  THR   A OG1 1 
ATOM   688  C CG2 . THR   A 1 89  ? 28.605  -43.490 -10.020 1.00 22.66 ? 90  THR   A CG2 1 
ATOM   689  N N   . PRO   A 1 90  ? 26.745  -39.803 -11.927 1.00 17.31 ? 91  PRO   A N   1 
ATOM   690  C CA  . PRO   A 1 90  ? 26.035  -38.784 -12.725 1.00 18.10 ? 91  PRO   A CA  1 
ATOM   691  C C   . PRO   A 1 90  ? 25.846  -39.167 -14.181 1.00 16.57 ? 91  PRO   A C   1 
ATOM   692  O O   . PRO   A 1 90  ? 24.871  -38.717 -14.795 1.00 17.58 ? 91  PRO   A O   1 
ATOM   693  C CB  . PRO   A 1 90  ? 26.918  -37.535 -12.575 1.00 17.98 ? 91  PRO   A CB  1 
ATOM   694  C CG  . PRO   A 1 90  ? 28.294  -38.078 -12.212 1.00 20.37 ? 91  PRO   A CG  1 
ATOM   695  C CD  . PRO   A 1 90  ? 27.996  -39.278 -11.351 1.00 18.01 ? 91  PRO   A CD  1 
ATOM   696  N N   . GLY   A 1 91  ? 26.723  -40.001 -14.743 1.00 17.55 ? 92  GLY   A N   1 
ATOM   697  C CA  . GLY   A 1 91  ? 26.597  -40.420 -16.135 1.00 21.38 ? 92  GLY   A CA  1 
ATOM   698  C C   . GLY   A 1 91  ? 25.396  -41.298 -16.428 1.00 20.16 ? 92  GLY   A C   1 
ATOM   699  O O   . GLY   A 1 91  ? 25.059  -41.488 -17.606 1.00 21.19 ? 92  GLY   A O   1 
ATOM   700  N N   . LYS   A 1 92  ? 24.743  -41.832 -15.395 1.00 18.72 ? 93  LYS   A N   1 
ATOM   701  C CA  . LYS   A 1 92  ? 23.486  -42.539 -15.604 1.00 22.96 ? 93  LYS   A CA  1 
ATOM   702  C C   . LYS   A 1 92  ? 22.400  -41.604 -16.117 1.00 19.20 ? 93  LYS   A C   1 
ATOM   703  O O   . LYS   A 1 92  ? 21.455  -42.048 -16.781 1.00 22.58 ? 93  LYS   A O   1 
ATOM   704  C CB  . LYS   A 1 92  ? 23.051  -43.200 -14.299 1.00 21.73 ? 93  LYS   A CB  1 
ATOM   705  C CG  . LYS   A 1 92  ? 21.802  -44.055 -14.410 1.00 23.26 ? 93  LYS   A CG  1 
ATOM   706  C CD  . LYS   A 1 92  ? 21.451  -44.635 -13.048 1.00 23.99 ? 93  LYS   A CD  1 
ATOM   707  C CE  . LYS   A 1 92  ? 20.158  -45.439 -13.091 1.00 28.31 ? 93  LYS   A CE  1 
ATOM   708  N NZ  . LYS   A 1 92  ? 20.429  -46.790 -13.627 1.00 39.80 ? 93  LYS   A NZ  1 
ATOM   709  N N   . TYR   A 1 93  ? 22.520  -40.316 -15.815 1.00 20.02 ? 94  TYR   A N   1 
ATOM   710  C CA  . TYR   A 1 93  ? 21.502  -39.325 -16.131 1.00 17.84 ? 94  TYR   A CA  1 
ATOM   711  C C   . TYR   A 1 93  ? 21.999  -38.299 -17.133 1.00 20.09 ? 94  TYR   A C   1 
ATOM   712  O O   . TYR   A 1 93  ? 21.293  -37.999 -18.099 1.00 21.66 ? 94  TYR   A O   1 
ATOM   713  C CB  . TYR   A 1 93  ? 21.030  -38.650 -14.834 1.00 18.50 ? 94  TYR   A CB  1 
ATOM   714  C CG  . TYR   A 1 93  ? 20.488  -39.679 -13.874 1.00 17.60 ? 94  TYR   A CG  1 
ATOM   715  C CD1 . TYR   A 1 93  ? 19.201  -40.161 -14.016 1.00 20.19 ? 94  TYR   A CD1 1 
ATOM   716  C CD2 . TYR   A 1 93  ? 21.283  -40.196 -12.858 1.00 17.78 ? 94  TYR   A CD2 1 
ATOM   717  C CE1 . TYR   A 1 93  ? 18.700  -41.126 -13.154 1.00 19.75 ? 94  TYR   A CE1 1 
ATOM   718  C CE2 . TYR   A 1 93  ? 20.797  -41.169 -12.003 1.00 20.66 ? 94  TYR   A CE2 1 
ATOM   719  C CZ  . TYR   A 1 93  ? 19.497  -41.620 -12.156 1.00 22.57 ? 94  TYR   A CZ  1 
ATOM   720  O OH  . TYR   A 1 93  ? 18.988  -42.581 -11.320 1.00 21.86 ? 94  TYR   A OH  1 
ATOM   721  N N   . TRP   A 1 94  ? 23.199  -37.760 -16.928 1.00 22.24 ? 95  TRP   A N   1 
ATOM   722  C CA  . TRP   A 1 94  ? 23.843  -36.854 -17.884 1.00 17.97 ? 95  TRP   A CA  1 
ATOM   723  C C   . TRP   A 1 94  ? 24.766  -37.720 -18.738 1.00 19.86 ? 95  TRP   A C   1 
ATOM   724  O O   . TRP   A 1 94  ? 25.924  -37.947 -18.392 1.00 19.86 ? 95  TRP   A O   1 
ATOM   725  C CB  . TRP   A 1 94  ? 24.601  -35.760 -17.143 1.00 18.74 ? 95  TRP   A CB  1 
ATOM   726  C CG  . TRP   A 1 94  ? 24.786  -34.495 -17.930 1.00 19.10 ? 95  TRP   A CG  1 
ATOM   727  C CD1 . TRP   A 1 94  ? 24.448  -34.281 -19.241 1.00 20.28 ? 95  TRP   A CD1 1 
ATOM   728  C CD2 . TRP   A 1 94  ? 25.343  -33.272 -17.451 1.00 19.69 ? 95  TRP   A CD2 1 
ATOM   729  N NE1 . TRP   A 1 94  ? 24.771  -32.990 -19.607 1.00 24.10 ? 95  TRP   A NE1 1 
ATOM   730  C CE2 . TRP   A 1 94  ? 25.316  -32.349 -18.524 1.00 21.92 ? 95  TRP   A CE2 1 
ATOM   731  C CE3 . TRP   A 1 94  ? 25.863  -32.865 -16.223 1.00 18.08 ? 95  TRP   A CE3 1 
ATOM   732  C CZ2 . TRP   A 1 94  ? 25.792  -31.046 -18.396 1.00 23.11 ? 95  TRP   A CZ2 1 
ATOM   733  C CZ3 . TRP   A 1 94  ? 26.333  -31.558 -16.100 1.00 20.03 ? 95  TRP   A CZ3 1 
ATOM   734  C CH2 . TRP   A 1 94  ? 26.293  -30.673 -17.178 1.00 18.98 ? 95  TRP   A CH2 1 
ATOM   735  N N   . LYS   A 1 95  ? 24.246  -38.189 -19.879 1.00 23.67 ? 96  LYS   A N   1 
ATOM   736  C CA  . LYS   A 1 95  ? 24.899  -39.265 -20.619 1.00 24.09 ? 96  LYS   A CA  1 
ATOM   737  C C   . LYS   A 1 95  ? 26.272  -38.868 -21.149 1.00 19.23 ? 96  LYS   A C   1 
ATOM   738  O O   . LYS   A 1 95  ? 27.127  -39.739 -21.364 1.00 20.54 ? 96  LYS   A O   1 
ATOM   739  C CB  . LYS   A 1 95  ? 23.995  -39.715 -21.765 1.00 24.34 ? 96  LYS   A CB  1 
ATOM   740  C CG  . LYS   A 1 95  ? 22.601  -40.070 -21.296 1.00 31.23 ? 96  LYS   A CG  1 
ATOM   741  C CD  . LYS   A 1 95  ? 22.630  -41.196 -20.271 1.00 33.55 ? 96  LYS   A CD  1 
ATOM   742  C CE  . LYS   A 1 95  ? 21.210  -41.623 -19.898 1.00 35.87 ? 96  LYS   A CE  1 
ATOM   743  N NZ  . LYS   A 1 95  ? 20.497  -42.289 -21.021 1.00 46.38 ? 96  LYS   A NZ  1 
ATOM   744  N N   . GLU   A 1 96  ? 26.508  -37.570 -21.368 1.00 18.92 ? 97  GLU   A N   1 
ATOM   745  C CA  . GLU   A 1 96  ? 27.808  -37.110 -21.838 1.00 20.98 ? 97  GLU   A CA  1 
ATOM   746  C C   . GLU   A 1 96  ? 28.911  -37.258 -20.791 1.00 20.18 ? 97  GLU   A C   1 
ATOM   747  O O   . GLU   A 1 96  ? 30.087  -37.116 -21.136 1.00 21.52 ? 97  GLU   A O   1 
ATOM   748  C CB  . GLU   A 1 96  ? 27.706  -35.647 -22.292 1.00 22.68 ? 97  GLU   A CB  1 
ATOM   749  C CG  . GLU   A 1 96  ? 26.882  -35.463 -23.572 1.00 24.67 ? 97  GLU   A CG  1 
ATOM   750  C CD  . GLU   A 1 96  ? 25.433  -35.052 -23.322 1.00 32.33 ? 97  GLU   A CD  1 
ATOM   751  O OE1 . GLU   A 1 96  ? 24.862  -35.398 -22.256 1.00 27.55 ? 97  GLU   A OE1 1 
ATOM   752  O OE2 . GLU   A 1 96  ? 24.853  -34.385 -24.213 1.00 35.34 ? 97  GLU   A OE2 1 
ATOM   753  N N   . LEU   A 1 97  ? 28.575  -37.571 -19.540 1.00 20.21 ? 98  LEU   A N   1 
ATOM   754  C CA  . LEU   A 1 97  ? 29.577  -37.848 -18.517 1.00 18.13 ? 98  LEU   A CA  1 
ATOM   755  C C   . LEU   A 1 97  ? 29.851  -39.339 -18.353 1.00 19.30 ? 98  LEU   A C   1 
ATOM   756  O O   . LEU   A 1 97  ? 30.740  -39.714 -17.580 1.00 19.79 ? 98  LEU   A O   1 
ATOM   757  C CB  . LEU   A 1 97  ? 29.145  -37.252 -17.166 1.00 16.05 ? 98  LEU   A CB  1 
ATOM   758  C CG  . LEU   A 1 97  ? 28.935  -35.730 -17.146 1.00 15.94 ? 98  LEU   A CG  1 
ATOM   759  C CD1 . LEU   A 1 97  ? 28.568  -35.294 -15.739 1.00 15.04 ? 98  LEU   A CD1 1 
ATOM   760  C CD2 . LEU   A 1 97  ? 30.188  -35.044 -17.611 1.00 16.44 ? 98  LEU   A CD2 1 
ATOM   761  N N   . LYS   A 1 98  ? 29.126  -40.200 -19.068 1.00 20.50 ? 99  LYS   A N   1 
ATOM   762  C CA  . LYS   A 1 98  ? 29.393  -41.630 -18.989 1.00 23.46 ? 99  LYS   A CA  1 
ATOM   763  C C   . LYS   A 1 98  ? 30.811  -41.916 -19.475 1.00 20.85 ? 99  LYS   A C   1 
ATOM   764  O O   . LYS   A 1 98  ? 31.283  -41.326 -20.450 1.00 25.04 ? 99  LYS   A O   1 
ATOM   765  C CB  . LYS   A 1 98  ? 28.363  -42.403 -19.825 1.00 25.00 ? 99  LYS   A CB  1 
ATOM   766  C CG  . LYS   A 1 98  ? 27.988  -43.797 -19.297 1.00 31.97 ? 99  LYS   A CG  1 
ATOM   767  C CD  . LYS   A 1 98  ? 26.834  -44.422 -20.113 1.00 36.92 ? 99  LYS   A CD  1 
ATOM   768  C CE  . LYS   A 1 98  ? 25.445  -43.911 -19.685 1.00 35.23 ? 99  LYS   A CE  1 
ATOM   769  N NZ  . LYS   A 1 98  ? 24.978  -44.509 -18.395 1.00 33.70 ? 99  LYS   A NZ  1 
ATOM   770  N N   . ASN   A 1 99  ? 31.502  -42.808 -18.767 1.00 27.96 ? 100 ASN   A N   1 
ATOM   771  C CA  . ASN   A 1 99  ? 32.869  -43.201 -19.123 1.00 28.80 ? 100 ASN   A CA  1 
ATOM   772  C C   . ASN   A 1 99  ? 33.846  -42.036 -18.994 1.00 26.95 ? 100 ASN   A C   1 
ATOM   773  O O   . ASN   A 1 99  ? 34.845  -41.962 -19.718 1.00 29.07 ? 100 ASN   A O   1 
ATOM   774  C CB  . ASN   A 1 99  ? 32.939  -43.794 -20.538 1.00 37.04 ? 100 ASN   A CB  1 
ATOM   775  C CG  . ASN   A 1 99  ? 31.943  -44.911 -20.751 1.00 44.37 ? 100 ASN   A CG  1 
ATOM   776  O OD1 . ASN   A 1 99  ? 31.781  -45.781 -19.896 1.00 44.97 ? 100 ASN   A OD1 1 
ATOM   777  N ND2 . ASN   A 1 99  ? 31.254  -44.885 -21.892 1.00 46.65 ? 100 ASN   A ND2 1 
ATOM   778  N N   . THR   A 1 100 ? 33.556  -41.094 -18.100 1.00 21.40 ? 101 THR   A N   1 
ATOM   779  C CA  . THR   A 1 100 ? 34.543  -40.101 -17.714 1.00 20.98 ? 101 THR   A CA  1 
ATOM   780  C C   . THR   A 1 100 ? 34.896  -40.288 -16.241 1.00 18.79 ? 101 THR   A C   1 
ATOM   781  O O   . THR   A 1 100 ? 34.173  -40.966 -15.505 1.00 18.21 ? 101 THR   A O   1 
ATOM   782  C CB  . THR   A 1 100 ? 34.024  -38.675 -17.950 1.00 21.25 ? 101 THR   A CB  1 
ATOM   783  O OG1 . THR   A 1 100 ? 33.007  -38.380 -16.997 1.00 18.83 ? 101 THR   A OG1 1 
ATOM   784  C CG2 . THR   A 1 100 ? 33.470  -38.531 -19.366 1.00 19.95 ? 101 THR   A CG2 1 
ATOM   785  N N   . PRO   A 1 101 ? 36.011  -39.724 -15.773 1.00 17.79 ? 102 PRO   A N   1 
ATOM   786  C CA  . PRO   A 1 101 ? 36.378  -39.943 -14.367 1.00 16.87 ? 102 PRO   A CA  1 
ATOM   787  C C   . PRO   A 1 101 ? 35.331  -39.463 -13.366 1.00 17.63 ? 102 PRO   A C   1 
ATOM   788  O O   . PRO   A 1 101 ? 35.183  -40.088 -12.312 1.00 16.69 ? 102 PRO   A O   1 
ATOM   789  C CB  . PRO   A 1 101 ? 37.699  -39.172 -14.226 1.00 17.11 ? 102 PRO   A CB  1 
ATOM   790  C CG  . PRO   A 1 101 ? 38.306  -39.277 -15.614 1.00 18.84 ? 102 PRO   A CG  1 
ATOM   791  C CD  . PRO   A 1 101 ? 37.109  -39.108 -16.539 1.00 19.22 ? 102 PRO   A CD  1 
ATOM   792  N N   . ILE   A 1 102 ? 34.576  -38.399 -13.658 1.00 16.01 ? 103 ILE   A N   1 
ATOM   793  C CA  . ILE   A 1 102 ? 33.594  -37.937 -12.672 1.00 15.72 ? 103 ILE   A CA  1 
ATOM   794  C C   . ILE   A 1 102 ? 32.452  -38.945 -12.510 1.00 16.57 ? 103 ILE   A C   1 
ATOM   795  O O   . ILE   A 1 102 ? 31.730  -38.911 -11.499 1.00 16.67 ? 103 ILE   A O   1 
ATOM   796  C CB  . ILE   A 1 102 ? 33.073  -36.524 -13.043 1.00 16.07 ? 103 ILE   A CB  1 
ATOM   797  C CG1 . ILE   A 1 102 ? 32.294  -35.884 -11.885 1.00 16.22 ? 103 ILE   A CG1 1 
ATOM   798  C CG2 . ILE   A 1 102 ? 32.154  -36.578 -14.257 1.00 16.45 ? 103 ILE   A CG2 1 
ATOM   799  C CD1 . ILE   A 1 102 ? 33.118  -35.518 -10.706 1.00 21.26 ? 103 ILE   A CD1 1 
ATOM   800  N N   . ASP   A 1 103 ? 32.270  -39.845 -13.479 1.00 16.49 ? 104 ASP   A N   1 
ATOM   801  C CA  . ASP   A 1 103 ? 31.273  -40.904 -13.345 1.00 16.28 ? 104 ASP   A CA  1 
ATOM   802  C C   . ASP   A 1 103 ? 31.695  -41.963 -12.336 1.00 16.99 ? 104 ASP   A C   1 
ATOM   803  O O   . ASP   A 1 103 ? 30.994  -42.970 -12.189 1.00 21.52 ? 104 ASP   A O   1 
ATOM   804  C CB  . ASP   A 1 103 ? 31.001  -41.538 -14.708 1.00 18.79 ? 104 ASP   A CB  1 
ATOM   805  C CG  . ASP   A 1 103 ? 29.613  -42.153 -14.815 1.00 20.70 ? 104 ASP   A CG  1 
ATOM   806  O OD1 . ASP   A 1 103 ? 28.681  -41.719 -14.096 1.00 20.76 ? 104 ASP   A OD1 1 
ATOM   807  O OD2 . ASP   A 1 103 ? 29.470  -43.101 -15.618 1.00 24.36 ? 104 ASP   A OD2 1 
ATOM   808  N N   . GLN   A 1 104 ? 32.830  -41.788 -11.656 1.00 16.79 ? 105 GLN   A N   1 
ATOM   809  C CA  A GLN   A 1 104 ? 33.216  -42.656 -10.556 0.48 16.16 ? 105 GLN   A CA  1 
ATOM   810  C CA  B GLN   A 1 104 ? 33.214  -42.655 -10.551 0.52 16.12 ? 105 GLN   A CA  1 
ATOM   811  C C   . GLN   A 1 104 ? 32.803  -42.097 -9.197  1.00 19.01 ? 105 GLN   A C   1 
ATOM   812  O O   . GLN   A 1 104 ? 33.027  -42.760 -8.173  1.00 20.32 ? 105 GLN   A O   1 
ATOM   813  C CB  A GLN   A 1 104 ? 34.731  -42.902 -10.595 0.48 18.51 ? 105 GLN   A CB  1 
ATOM   814  C CB  B GLN   A 1 104 ? 34.727  -42.900 -10.561 0.52 18.51 ? 105 GLN   A CB  1 
ATOM   815  C CG  A GLN   A 1 104 ? 35.190  -43.515 -11.912 0.48 19.38 ? 105 GLN   A CG  1 
ATOM   816  C CG  B GLN   A 1 104 ? 35.180  -43.810 -11.671 0.52 19.59 ? 105 GLN   A CG  1 
ATOM   817  C CD  A GLN   A 1 104 ? 36.688  -43.392 -12.138 0.48 20.40 ? 105 GLN   A CD  1 
ATOM   818  C CD  B GLN   A 1 104 ? 36.677  -43.735 -11.905 0.52 20.86 ? 105 GLN   A CD  1 
ATOM   819  O OE1 A GLN   A 1 104 ? 37.278  -42.326 -11.934 0.48 19.36 ? 105 GLN   A OE1 1 
ATOM   820  O OE1 B GLN   A 1 104 ? 37.472  -43.661 -10.959 0.52 20.95 ? 105 GLN   A OE1 1 
ATOM   821  N NE2 A GLN   A 1 104 ? 37.311  -44.486 -12.560 0.48 22.08 ? 105 GLN   A NE2 1 
ATOM   822  N NE2 B GLN   A 1 104 ? 37.069  -43.742 -13.173 0.52 20.47 ? 105 GLN   A NE2 1 
ATOM   823  N N   . VAL   A 1 105 ? 32.211  -40.896 -9.169  1.00 14.89 ? 106 VAL   A N   1 
ATOM   824  C CA  . VAL   A 1 105 ? 31.701  -40.260 -7.954  1.00 15.51 ? 106 VAL   A CA  1 
ATOM   825  C C   . VAL   A 1 105 ? 30.192  -40.471 -7.901  1.00 17.38 ? 106 VAL   A C   1 
ATOM   826  O O   . VAL   A 1 105 ? 29.505  -40.268 -8.910  1.00 16.77 ? 106 VAL   A O   1 
ATOM   827  C CB  . VAL   A 1 105 ? 32.035  -38.757 -7.943  1.00 16.72 ? 106 VAL   A CB  1 
ATOM   828  C CG1 . VAL   A 1 105 ? 31.569  -38.097 -6.634  1.00 15.02 ? 106 VAL   A CG1 1 
ATOM   829  C CG2 . VAL   A 1 105 ? 33.541  -38.526 -8.170  1.00 15.27 ? 106 VAL   A CG2 1 
ATOM   830  N N   . ASN   A 1 106 ? 29.666  -40.878 -6.734  1.00 15.86 ? 107 ASN   A N   1 
ATOM   831  C CA  . ASN   A 1 106 ? 28.228  -41.123 -6.659  1.00 16.43 ? 107 ASN   A CA  1 
ATOM   832  C C   . ASN   A 1 106 ? 27.481  -39.858 -6.207  1.00 14.50 ? 107 ASN   A C   1 
ATOM   833  O O   . ASN   A 1 106 ? 28.078  -38.842 -5.847  1.00 14.81 ? 107 ASN   A O   1 
ATOM   834  C CB  . ASN   A 1 106 ? 27.934  -42.371 -5.786  1.00 14.72 ? 107 ASN   A CB  1 
ATOM   835  C CG  . ASN   A 1 106 ? 28.117  -42.158 -4.287  1.00 15.26 ? 107 ASN   A CG  1 
ATOM   836  O OD1 . ASN   A 1 106 ? 27.889  -41.077 -3.749  1.00 15.34 ? 107 ASN   A OD1 1 
ATOM   837  N ND2 . ASN   A 1 106 ? 28.508  -43.230 -3.597  1.00 16.73 ? 107 ASN   A ND2 1 
ATOM   838  N N   . LEU   A 1 107 ? 26.152  -39.912 -6.299  1.00 15.04 ? 108 LEU   A N   1 
ATOM   839  C CA  . LEU   A 1 107 ? 25.353  -38.711 -6.102  1.00 14.64 ? 108 LEU   A CA  1 
ATOM   840  C C   . LEU   A 1 107 ? 25.422  -38.216 -4.663  1.00 13.30 ? 108 LEU   A C   1 
ATOM   841  O O   . LEU   A 1 107 ? 25.415  -37.002 -4.426  1.00 13.71 ? 108 LEU   A O   1 
ATOM   842  C CB  . LEU   A 1 107 ? 23.902  -38.976 -6.509  1.00 14.72 ? 108 LEU   A CB  1 
ATOM   843  C CG  . LEU   A 1 107 ? 23.680  -39.449 -7.948  1.00 15.78 ? 108 LEU   A CG  1 
ATOM   844  C CD1 . LEU   A 1 107 ? 22.193  -39.480 -8.237  1.00 17.87 ? 108 LEU   A CD1 1 
ATOM   845  C CD2 . LEU   A 1 107 ? 24.397  -38.544 -8.929  1.00 18.68 ? 108 LEU   A CD2 1 
ATOM   846  N N   . LEU   A 1 108 ? 25.462  -39.135 -3.691  1.00 14.12 ? 109 LEU   A N   1 
ATOM   847  C CA  . LEU   A 1 108 ? 25.595  -38.719 -2.295  1.00 14.39 ? 109 LEU   A CA  1 
ATOM   848  C C   . LEU   A 1 108 ? 26.918  -37.993 -2.075  1.00 15.54 ? 109 LEU   A C   1 
ATOM   849  O O   . LEU   A 1 108 ? 26.971  -36.970 -1.370  1.00 13.47 ? 109 LEU   A O   1 
ATOM   850  C CB  . LEU   A 1 108 ? 25.480  -39.936 -1.372  1.00 13.36 ? 109 LEU   A CB  1 
ATOM   851  C CG  . LEU   A 1 108 ? 25.441  -39.557 0.108   1.00 15.71 ? 109 LEU   A CG  1 
ATOM   852  C CD1 . LEU   A 1 108 ? 24.282  -38.603 0.364   1.00 17.59 ? 109 LEU   A CD1 1 
ATOM   853  C CD2 . LEU   A 1 108 ? 25.320  -40.807 0.974   1.00 24.34 ? 109 LEU   A CD2 1 
ATOM   854  N N   . GLN   A 1 109 ? 27.990  -38.493 -2.695  1.00 16.50 ? 110 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 109 ? 29.291  -37.839 -2.588  1.00 15.14 ? 110 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 109 ? 29.273  -36.446 -3.214  1.00 12.26 ? 110 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 109 ? 29.896  -35.517 -2.680  1.00 13.95 ? 110 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 109 ? 30.372  -38.723 -3.218  1.00 14.21 ? 110 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 109 ? 30.611  -39.980 -2.369  1.00 14.72 ? 110 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 109 ? 31.348  -41.098 -3.099  1.00 17.20 ? 110 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 109 ? 31.404  -41.128 -4.328  1.00 15.14 ? 110 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 109 ? 31.921  -42.030 -2.336  1.00 18.43 ? 110 GLN   A NE2 1 
ATOM   863  N N   . LEU   A 1 110 ? 28.551  -36.274 -4.333  1.00 12.70 ? 111 LEU   A N   1 
ATOM   864  C CA  . LEU   A 1 110 ? 28.413  -34.946 -4.923  1.00 11.94 ? 111 LEU   A CA  1 
ATOM   865  C C   . LEU   A 1 110 ? 27.610  -34.031 -4.003  1.00 13.42 ? 111 LEU   A C   1 
ATOM   866  O O   . LEU   A 1 110 ? 27.997  -32.879 -3.773  1.00 12.98 ? 111 LEU   A O   1 
ATOM   867  C CB  . LEU   A 1 110 ? 27.748  -35.037 -6.302  1.00 12.15 ? 111 LEU   A CB  1 
ATOM   868  C CG  . LEU   A 1 110 ? 28.636  -35.700 -7.364  1.00 13.22 ? 111 LEU   A CG  1 
ATOM   869  C CD1 . LEU   A 1 110 ? 27.836  -36.020 -8.613  1.00 16.89 ? 111 LEU   A CD1 1 
ATOM   870  C CD2 . LEU   A 1 110 ? 29.878  -34.821 -7.655  1.00 14.11 ? 111 LEU   A CD2 1 
ATOM   871  N N   . ALA   A 1 111 ? 26.497  -34.543 -3.459  1.00 12.90 ? 112 ALA   A N   1 
ATOM   872  C CA  . ALA   A 1 111 ? 25.627  -33.721 -2.629  1.00 14.93 ? 112 ALA   A CA  1 
ATOM   873  C C   . ALA   A 1 111 ? 26.303  -33.298 -1.336  1.00 14.23 ? 112 ALA   A C   1 
ATOM   874  O O   . ALA   A 1 111 ? 25.943  -32.251 -0.783  1.00 15.90 ? 112 ALA   A O   1 
ATOM   875  C CB  . ALA   A 1 111 ? 24.334  -34.467 -2.300  1.00 15.51 ? 112 ALA   A CB  1 
ATOM   876  N N   . THR   A 1 112 ? 27.245  -34.102 -0.821  1.00 13.02 ? 113 THR   A N   1 
ATOM   877  C CA  . THR   A 1 112 ? 27.905  -33.825 0.455   1.00 13.35 ? 113 THR   A CA  1 
ATOM   878  C C   . THR   A 1 112 ? 29.390  -33.500 0.291   1.00 13.89 ? 113 THR   A C   1 
ATOM   879  O O   . THR   A 1 112 ? 30.163  -33.600 1.261   1.00 15.34 ? 113 THR   A O   1 
ATOM   880  C CB  . THR   A 1 112 ? 27.700  -34.984 1.440   1.00 13.65 ? 113 THR   A CB  1 
ATOM   881  O OG1 . THR   A 1 112 ? 28.228  -36.209 0.908   1.00 13.69 ? 113 THR   A OG1 1 
ATOM   882  C CG2 . THR   A 1 112 ? 26.206  -35.175 1.738   1.00 16.57 ? 113 THR   A CG2 1 
ATOM   883  N N   . TYR   A 1 113 ? 29.795  -33.076 -0.915  1.00 13.56 ? 114 TYR   A N   1 
ATOM   884  C CA  . TYR   A 1 113 ? 31.072  -32.390 -1.148  1.00 13.03 ? 114 TYR   A CA  1 
ATOM   885  C C   . TYR   A 1 113 ? 32.295  -33.288 -0.956  1.00 13.23 ? 114 TYR   A C   1 
ATOM   886  O O   . TYR   A 1 113 ? 33.358  -32.793 -0.557  1.00 12.70 ? 114 TYR   A O   1 
ATOM   887  C CB  . TYR   A 1 113 ? 31.230  -31.142 -0.254  1.00 14.07 ? 114 TYR   A CB  1 
ATOM   888  C CG  . TYR   A 1 113 ? 29.946  -30.388 0.030   1.00 13.05 ? 114 TYR   A CG  1 
ATOM   889  C CD1 . TYR   A 1 113 ? 29.279  -29.694 -0.986  1.00 14.33 ? 114 TYR   A CD1 1 
ATOM   890  C CD2 . TYR   A 1 113 ? 29.411  -30.353 1.330   1.00 14.37 ? 114 TYR   A CD2 1 
ATOM   891  C CE1 . TYR   A 1 113 ? 28.085  -29.008 -0.721  1.00 15.02 ? 114 TYR   A CE1 1 
ATOM   892  C CE2 . TYR   A 1 113 ? 28.238  -29.670 1.601   1.00 15.72 ? 114 TYR   A CE2 1 
ATOM   893  C CZ  . TYR   A 1 113 ? 27.578  -29.002 0.578   1.00 15.45 ? 114 TYR   A CZ  1 
ATOM   894  O OH  . TYR   A 1 113 ? 26.399  -28.323 0.853   1.00 18.47 ? 114 TYR   A OH  1 
ATOM   895  N N   . THR   A 1 114 ? 32.217  -34.589 -1.279  1.00 14.62 ? 115 THR   A N   1 
ATOM   896  C CA  . THR   A 1 114 ? 33.368  -35.463 -1.044  1.00 13.95 ? 115 THR   A CA  1 
ATOM   897  C C   . THR   A 1 114 ? 33.980  -36.045 -2.321  1.00 14.51 ? 115 THR   A C   1 
ATOM   898  O O   . THR   A 1 114 ? 34.652  -37.082 -2.245  1.00 15.95 ? 115 THR   A O   1 
ATOM   899  C CB  . THR   A 1 114 ? 33.035  -36.615 -0.082  1.00 15.02 ? 115 THR   A CB  1 
ATOM   900  O OG1 . THR   A 1 114 ? 31.964  -37.427 -0.597  1.00 15.80 ? 115 THR   A OG1 1 
ATOM   901  C CG2 . THR   A 1 114 ? 32.687  -36.085 1.313   1.00 14.21 ? 115 THR   A CG2 1 
ATOM   902  N N   . SER   A 1 115 ? 33.823  -35.386 -3.476  1.00 14.29 ? 116 SER   A N   1 
ATOM   903  C CA  . SER   A 1 115 ? 34.422  -35.922 -4.705  1.00 13.96 ? 116 SER   A CA  1 
ATOM   904  C C   . SER   A 1 115 ? 35.939  -36.015 -4.627  1.00 14.38 ? 116 SER   A C   1 
ATOM   905  O O   . SER   A 1 115 ? 36.539  -36.812 -5.357  1.00 14.04 ? 116 SER   A O   1 
ATOM   906  C CB  . SER   A 1 115 ? 34.049  -35.053 -5.925  1.00 13.96 ? 116 SER   A CB  1 
ATOM   907  O OG  . SER   A 1 115 ? 34.754  -33.816 -5.906  1.00 14.38 ? 116 SER   A OG  1 
ATOM   908  N N   . GLY   A 1 116 ? 36.575  -35.209 -3.783  1.00 14.11 ? 117 GLY   A N   1 
ATOM   909  C CA  . GLY   A 1 116 ? 38.018  -35.204 -3.687  1.00 14.06 ? 117 GLY   A CA  1 
ATOM   910  C C   . GLY   A 1 116 ? 38.733  -34.238 -4.614  1.00 14.49 ? 117 GLY   A C   1 
ATOM   911  O O   . GLY   A 1 116 ? 39.960  -34.143 -4.548  1.00 13.66 ? 117 GLY   A O   1 
ATOM   912  N N   . ASN   A 1 117 ? 38.016  -33.510 -5.466  1.00 13.05 ? 118 ASN   A N   1 
ATOM   913  C CA  . ASN   A 1 117 ? 38.691  -32.510 -6.289  1.00 14.59 ? 118 ASN   A CA  1 
ATOM   914  C C   . ASN   A 1 117 ? 37.691  -31.509 -6.857  1.00 15.83 ? 118 ASN   A C   1 
ATOM   915  O O   . ASN   A 1 117 ? 37.684  -31.235 -8.067  1.00 14.30 ? 118 ASN   A O   1 
ATOM   916  C CB  . ASN   A 1 117 ? 39.492  -33.152 -7.429  1.00 15.13 ? 118 ASN   A CB  1 
ATOM   917  C CG  . ASN   A 1 117 ? 40.415  -32.150 -8.122  1.00 14.64 ? 118 ASN   A CG  1 
ATOM   918  O OD1 . ASN   A 1 117 ? 40.879  -31.183 -7.507  1.00 18.79 ? 118 ASN   A OD1 1 
ATOM   919  N ND2 . ASN   A 1 117 ? 40.702  -32.386 -9.409  1.00 16.82 ? 118 ASN   A ND2 1 
ATOM   920  N N   . LEU   A 1 118 ? 36.854  -30.938 -5.990  1.00 15.24 ? 119 LEU   A N   1 
ATOM   921  C CA  . LEU   A 1 118 ? 35.981  -29.837 -6.398  1.00 12.58 ? 119 LEU   A CA  1 
ATOM   922  C C   . LEU   A 1 118 ? 36.066  -28.740 -5.342  1.00 13.90 ? 119 LEU   A C   1 
ATOM   923  O O   . LEU   A 1 118 ? 35.834  -28.984 -4.154  1.00 13.28 ? 119 LEU   A O   1 
ATOM   924  C CB  . LEU   A 1 118 ? 34.538  -30.300 -6.623  1.00 12.81 ? 119 LEU   A CB  1 
ATOM   925  C CG  . LEU   A 1 118 ? 34.295  -31.148 -7.895  1.00 11.86 ? 119 LEU   A CG  1 
ATOM   926  C CD1 . LEU   A 1 118 ? 32.877  -31.709 -7.931  1.00 13.79 ? 119 LEU   A CD1 1 
ATOM   927  C CD2 . LEU   A 1 118 ? 34.576  -30.371 -9.174  1.00 13.30 ? 119 LEU   A CD2 1 
ATOM   928  N N   . ALA   A 1 119 ? 36.418  -27.541 -5.777  1.00 14.96 ? 120 ALA   A N   1 
ATOM   929  C CA  . ALA   A 1 119 ? 36.651  -26.434 -4.865  1.00 16.71 ? 120 ALA   A CA  1 
ATOM   930  C C   . ALA   A 1 119 ? 35.364  -25.640 -4.661  1.00 14.56 ? 120 ALA   A C   1 
ATOM   931  O O   . ALA   A 1 119 ? 34.297  -25.988 -5.180  1.00 14.56 ? 120 ALA   A O   1 
ATOM   932  C CB  . ALA   A 1 119 ? 37.766  -25.537 -5.396  1.00 17.85 ? 120 ALA   A CB  1 
ATOM   933  N N   . LEU   A 1 120 ? 35.490  -24.527 -3.926  1.00 13.24 ? 121 LEU   A N   1 
ATOM   934  C CA  . LEU   A 1 120 ? 34.324  -23.706 -3.605  1.00 14.53 ? 121 LEU   A CA  1 
ATOM   935  C C   . LEU   A 1 120 ? 33.594  -23.244 -4.857  1.00 15.88 ? 121 LEU   A C   1 
ATOM   936  O O   . LEU   A 1 120 ? 32.360  -23.261 -4.899  1.00 15.70 ? 121 LEU   A O   1 
ATOM   937  C CB  . LEU   A 1 120 ? 34.743  -22.493 -2.775  1.00 15.13 ? 121 LEU   A CB  1 
ATOM   938  C CG  . LEU   A 1 120 ? 33.604  -21.642 -2.235  1.00 22.74 ? 121 LEU   A CG  1 
ATOM   939  C CD1 . LEU   A 1 120 ? 32.773  -22.451 -1.252  1.00 20.61 ? 121 LEU   A CD1 1 
ATOM   940  C CD2 . LEU   A 1 120 ? 34.184  -20.429 -1.535  1.00 25.33 ? 121 LEU   A CD2 1 
ATOM   941  N N   . GLN   A 1 121 ? 34.329  -22.778 -5.867  1.00 16.64 ? 122 GLN   A N   1 
ATOM   942  C CA  . GLN   A 1 121 ? 33.718  -22.267 -7.089  1.00 15.76 ? 122 GLN   A CA  1 
ATOM   943  C C   . GLN   A 1 121 ? 34.348  -22.927 -8.307  1.00 14.62 ? 122 GLN   A C   1 
ATOM   944  O O   . GLN   A 1 121 ? 35.440  -23.486 -8.236  1.00 16.85 ? 122 GLN   A O   1 
ATOM   945  C CB  . GLN   A 1 121 ? 33.882  -20.738 -7.210  1.00 19.68 ? 122 GLN   A CB  1 
ATOM   946  C CG  . GLN   A 1 121 ? 33.427  -19.957 -5.963  1.00 18.50 ? 122 GLN   A CG  1 
ATOM   947  C CD  . GLN   A 1 121 ? 31.929  -19.740 -5.892  1.00 23.71 ? 122 GLN   A CD  1 
ATOM   948  O OE1 . GLN   A 1 121 ? 31.153  -20.341 -6.638  1.00 20.88 ? 122 GLN   A OE1 1 
ATOM   949  N NE2 . GLN   A 1 121 ? 31.510  -18.862 -4.977  1.00 28.31 ? 122 GLN   A NE2 1 
ATOM   950  N N   . PHE   A 1 122 ? 33.634  -22.839 -9.438  1.00 16.40 ? 123 PHE   A N   1 
ATOM   951  C CA  . PHE   A 1 122 ? 34.224  -23.199 -10.717 1.00 16.78 ? 123 PHE   A CA  1 
ATOM   952  C C   . PHE   A 1 122 ? 35.457  -22.340 -10.974 1.00 21.10 ? 123 PHE   A C   1 
ATOM   953  O O   . PHE   A 1 122 ? 35.564  -21.221 -10.464 1.00 19.32 ? 123 PHE   A O   1 
ATOM   954  C CB  . PHE   A 1 122 ? 33.230  -22.972 -11.862 1.00 17.61 ? 123 PHE   A CB  1 
ATOM   955  C CG  . PHE   A 1 122 ? 32.152  -24.023 -11.967 1.00 17.56 ? 123 PHE   A CG  1 
ATOM   956  C CD1 . PHE   A 1 122 ? 32.467  -25.326 -12.319 1.00 16.80 ? 123 PHE   A CD1 1 
ATOM   957  C CD2 . PHE   A 1 122 ? 30.819  -23.693 -11.762 1.00 17.36 ? 123 PHE   A CD2 1 
ATOM   958  C CE1 . PHE   A 1 122 ? 31.470  -26.307 -12.420 1.00 16.91 ? 123 PHE   A CE1 1 
ATOM   959  C CE2 . PHE   A 1 122 ? 29.813  -24.667 -11.868 1.00 20.47 ? 123 PHE   A CE2 1 
ATOM   960  C CZ  . PHE   A 1 122 ? 30.139  -25.976 -12.209 1.00 19.67 ? 123 PHE   A CZ  1 
ATOM   961  N N   . PRO   A 1 123 ? 36.378  -22.821 -11.805 1.00 19.39 ? 124 PRO   A N   1 
ATOM   962  C CA  . PRO   A 1 123 ? 37.427  -21.937 -12.318 1.00 22.66 ? 124 PRO   A CA  1 
ATOM   963  C C   . PRO   A 1 123 ? 36.803  -20.714 -12.977 1.00 22.92 ? 124 PRO   A C   1 
ATOM   964  O O   . PRO   A 1 123 ? 35.680  -20.767 -13.482 1.00 21.12 ? 124 PRO   A O   1 
ATOM   965  C CB  . PRO   A 1 123 ? 38.173  -22.813 -13.334 1.00 23.38 ? 124 PRO   A CB  1 
ATOM   966  C CG  . PRO   A 1 123 ? 37.827  -24.224 -12.955 1.00 22.86 ? 124 PRO   A CG  1 
ATOM   967  C CD  . PRO   A 1 123 ? 36.434  -24.169 -12.398 1.00 19.95 ? 124 PRO   A CD  1 
ATOM   968  N N   . ASP   A 1 124 ? 37.536  -19.596 -12.948 1.00 22.70 ? 125 ASP   A N   1 
ATOM   969  C CA  . ASP   A 1 124 ? 36.979  -18.347 -13.455 1.00 22.93 ? 125 ASP   A CA  1 
ATOM   970  C C   . ASP   A 1 124 ? 36.592  -18.453 -14.925 1.00 25.66 ? 125 ASP   A C   1 
ATOM   971  O O   . ASP   A 1 124 ? 35.648  -17.783 -15.368 1.00 25.43 ? 125 ASP   A O   1 
ATOM   972  C CB  . ASP   A 1 124 ? 37.971  -17.200 -13.247 1.00 28.07 ? 125 ASP   A CB  1 
ATOM   973  C CG  . ASP   A 1 124 ? 38.046  -16.752 -11.800 1.00 36.31 ? 125 ASP   A CG  1 
ATOM   974  O OD1 . ASP   A 1 124 ? 37.138  -17.120 -11.018 1.00 37.07 ? 125 ASP   A OD1 1 
ATOM   975  O OD2 . ASP   A 1 124 ? 39.020  -16.053 -11.440 1.00 38.23 ? 125 ASP   A OD2 1 
ATOM   976  N N   . GLU   A 1 125 ? 37.284  -19.290 -15.692 1.00 23.83 ? 126 GLU   A N   1 
ATOM   977  C CA  . GLU   A 1 125 ? 36.997  -19.336 -17.123 1.00 24.76 ? 126 GLU   A CA  1 
ATOM   978  C C   . GLU   A 1 125 ? 35.773  -20.183 -17.464 1.00 21.79 ? 126 GLU   A C   1 
ATOM   979  O O   . GLU   A 1 125 ? 35.364  -20.201 -18.635 1.00 24.60 ? 126 GLU   A O   1 
ATOM   980  C CB  . GLU   A 1 125 ? 38.221  -19.851 -17.889 1.00 26.12 ? 126 GLU   A CB  1 
ATOM   981  C CG  . GLU   A 1 125 ? 38.523  -21.316 -17.663 1.00 30.78 ? 126 GLU   A CG  1 
ATOM   982  C CD  . GLU   A 1 125 ? 39.439  -21.585 -16.476 1.00 34.12 ? 126 GLU   A CD  1 
ATOM   983  O OE1 . GLU   A 1 125 ? 39.855  -22.756 -16.321 1.00 43.23 ? 126 GLU   A OE1 1 
ATOM   984  O OE2 . GLU   A 1 125 ? 39.741  -20.643 -15.701 1.00 33.02 ? 126 GLU   A OE2 1 
ATOM   985  N N   . VAL   A 1 126 ? 35.172  -20.865 -16.488 1.00 20.32 ? 127 VAL   A N   1 
ATOM   986  C CA  . VAL   A 1 126 ? 33.963  -21.653 -16.712 1.00 20.62 ? 127 VAL   A CA  1 
ATOM   987  C C   . VAL   A 1 126 ? 32.770  -20.719 -16.512 1.00 22.14 ? 127 VAL   A C   1 
ATOM   988  O O   . VAL   A 1 126 ? 32.337  -20.464 -15.387 1.00 21.60 ? 127 VAL   A O   1 
ATOM   989  C CB  . VAL   A 1 126 ? 33.907  -22.873 -15.790 1.00 20.31 ? 127 VAL   A CB  1 
ATOM   990  C CG1 . VAL   A 1 126 ? 32.595  -23.606 -15.963 1.00 20.71 ? 127 VAL   A CG1 1 
ATOM   991  C CG2 . VAL   A 1 126 ? 35.067  -23.801 -16.100 1.00 21.31 ? 127 VAL   A CG2 1 
ATOM   992  N N   . LYS   A 1 127 ? 32.237  -20.197 -17.616 1.00 21.96 ? 128 LYS   A N   1 
ATOM   993  C CA  . LYS   A 1 127 ? 31.234  -19.146 -17.566 1.00 18.52 ? 128 LYS   A CA  1 
ATOM   994  C C   . LYS   A 1 127 ? 29.906  -19.524 -18.195 1.00 24.69 ? 128 LYS   A C   1 
ATOM   995  O O   . LYS   A 1 127 ? 28.921  -18.812 -17.976 1.00 24.68 ? 128 LYS   A O   1 
ATOM   996  C CB  . LYS   A 1 127 ? 31.748  -17.870 -18.257 1.00 22.68 ? 128 LYS   A CB  1 
ATOM   997  C CG  . LYS   A 1 127 ? 32.984  -17.258 -17.603 1.00 23.39 ? 128 LYS   A CG  1 
ATOM   998  C CD  . LYS   A 1 127 ? 33.346  -15.940 -18.273 1.00 30.09 ? 128 LYS   A CD  1 
ATOM   999  C CE  . LYS   A 1 127 ? 34.619  -15.346 -17.687 1.00 34.35 ? 128 LYS   A CE  1 
ATOM   1000 N NZ  . LYS   A 1 127 ? 34.435  -14.928 -16.273 1.00 38.04 ? 128 LYS   A NZ  1 
ATOM   1001 N N   . THR   A 1 128 ? 29.844  -20.597 -18.978 1.00 19.58 ? 129 THR   A N   1 
ATOM   1002 C CA  . THR   A 1 128 ? 28.626  -20.958 -19.692 1.00 17.28 ? 129 THR   A CA  1 
ATOM   1003 C C   . THR   A 1 128 ? 28.273  -22.416 -19.410 1.00 19.66 ? 129 THR   A C   1 
ATOM   1004 O O   . THR   A 1 128 ? 29.098  -23.206 -18.931 1.00 17.35 ? 129 THR   A O   1 
ATOM   1005 C CB  . THR   A 1 128 ? 28.752  -20.761 -21.206 1.00 18.61 ? 129 THR   A CB  1 
ATOM   1006 O OG1 . THR   A 1 128 ? 29.608  -21.782 -21.728 1.00 19.54 ? 129 THR   A OG1 1 
ATOM   1007 C CG2 . THR   A 1 128 ? 29.323  -19.382 -21.560 1.00 19.58 ? 129 THR   A CG2 1 
ATOM   1008 N N   . ASP   A 1 129 ? 27.024  -22.768 -19.728 1.00 20.86 ? 130 ASP   A N   1 
ATOM   1009 C CA  . ASP   A 1 129 ? 26.581  -24.151 -19.557 1.00 18.97 ? 130 ASP   A CA  1 
ATOM   1010 C C   . ASP   A 1 129 ? 27.413  -25.113 -20.396 1.00 18.56 ? 130 ASP   A C   1 
ATOM   1011 O O   . ASP   A 1 129 ? 27.761  -26.205 -19.927 1.00 17.64 ? 130 ASP   A O   1 
ATOM   1012 C CB  . ASP   A 1 129 ? 25.110  -24.305 -19.928 1.00 20.38 ? 130 ASP   A CB  1 
ATOM   1013 C CG  . ASP   A 1 129 ? 24.174  -23.649 -18.929 1.00 29.95 ? 130 ASP   A CG  1 
ATOM   1014 O OD1 . ASP   A 1 129 ? 24.568  -23.454 -17.756 1.00 28.68 ? 130 ASP   A OD1 1 
ATOM   1015 O OD2 . ASP   A 1 129 ? 23.035  -23.340 -19.330 1.00 32.17 ? 130 ASP   A OD2 1 
ATOM   1016 N N   . GLN   A 1 130 ? 27.735  -24.734 -21.635 1.00 17.67 ? 131 GLN   A N   1 
ATOM   1017 C CA  . GLN   A 1 130 ? 28.593  -25.591 -22.447 1.00 16.82 ? 131 GLN   A CA  1 
ATOM   1018 C C   . GLN   A 1 130 ? 29.909  -25.838 -21.736 1.00 16.39 ? 131 GLN   A C   1 
ATOM   1019 O O   . GLN   A 1 130 ? 30.412  -26.968 -21.707 1.00 18.62 ? 131 GLN   A O   1 
ATOM   1020 C CB  . GLN   A 1 130 ? 28.867  -24.967 -23.813 1.00 18.37 ? 131 GLN   A CB  1 
ATOM   1021 C CG  . GLN   A 1 130 ? 27.744  -25.035 -24.827 1.00 19.81 ? 131 GLN   A CG  1 
ATOM   1022 C CD  . GLN   A 1 130 ? 28.189  -24.472 -26.177 1.00 19.33 ? 131 GLN   A CD  1 
ATOM   1023 O OE1 . GLN   A 1 130 ? 29.386  -24.482 -26.503 1.00 21.29 ? 131 GLN   A OE1 1 
ATOM   1024 N NE2 . GLN   A 1 130 ? 27.234  -23.982 -26.974 1.00 20.01 ? 131 GLN   A NE2 1 
ATOM   1025 N N   . GLN   A 1 131 ? 30.462  -24.789 -21.123 1.00 16.43 ? 132 GLN   A N   1 
ATOM   1026 C CA  . GLN   A 1 131 ? 31.770  -24.898 -20.497 1.00 16.38 ? 132 GLN   A CA  1 
ATOM   1027 C C   . GLN   A 1 131 ? 31.713  -25.695 -19.197 1.00 16.54 ? 132 GLN   A C   1 
ATOM   1028 O O   . GLN   A 1 131 ? 32.696  -26.346 -18.836 1.00 17.61 ? 132 GLN   A O   1 
ATOM   1029 C CB  . GLN   A 1 131 ? 32.336  -23.493 -20.280 1.00 16.77 ? 132 GLN   A CB  1 
ATOM   1030 C CG  . GLN   A 1 131 ? 32.643  -22.811 -21.612 1.00 18.95 ? 132 GLN   A CG  1 
ATOM   1031 C CD  . GLN   A 1 131 ? 32.793  -21.309 -21.500 1.00 21.00 ? 132 GLN   A CD  1 
ATOM   1032 O OE1 . GLN   A 1 131 ? 32.744  -20.745 -20.410 1.00 20.51 ? 132 GLN   A OE1 1 
ATOM   1033 N NE2 . GLN   A 1 131 ? 32.974  -20.649 -22.639 1.00 19.37 ? 132 GLN   A NE2 1 
ATOM   1034 N N   . VAL   A 1 132 ? 30.562  -25.692 -18.514 1.00 15.27 ? 133 VAL   A N   1 
ATOM   1035 C CA  . VAL   A 1 132 ? 30.373  -26.531 -17.338 1.00 17.43 ? 133 VAL   A CA  1 
ATOM   1036 C C   . VAL   A 1 132 ? 30.425  -27.998 -17.724 1.00 17.64 ? 133 VAL   A C   1 
ATOM   1037 O O   . VAL   A 1 132 ? 31.071  -28.807 -17.052 1.00 16.08 ? 133 VAL   A O   1 
ATOM   1038 C CB  . VAL   A 1 132 ? 29.045  -26.187 -16.637 1.00 17.73 ? 133 VAL   A CB  1 
ATOM   1039 C CG1 . VAL   A 1 132 ? 28.678  -27.274 -15.621 1.00 15.69 ? 133 VAL   A CG1 1 
ATOM   1040 C CG2 . VAL   A 1 132 ? 29.142  -24.838 -15.955 1.00 18.63 ? 133 VAL   A CG2 1 
ATOM   1041 N N   . LEU   A 1 133 ? 29.734  -28.369 -18.806 1.00 16.09 ? 134 LEU   A N   1 
ATOM   1042 C CA  . LEU   A 1 133 ? 29.778  -29.762 -19.242 1.00 17.50 ? 134 LEU   A CA  1 
ATOM   1043 C C   . LEU   A 1 133 ? 31.204  -30.153 -19.603 1.00 18.26 ? 134 LEU   A C   1 
ATOM   1044 O O   . LEU   A 1 133 ? 31.702  -31.197 -19.168 1.00 16.90 ? 134 LEU   A O   1 
ATOM   1045 C CB  . LEU   A 1 133 ? 28.822  -29.986 -20.421 1.00 18.97 ? 134 LEU   A CB  1 
ATOM   1046 C CG  . LEU   A 1 133 ? 28.907  -31.342 -21.130 1.00 18.67 ? 134 LEU   A CG  1 
ATOM   1047 C CD1 . LEU   A 1 133 ? 28.742  -32.494 -20.113 1.00 18.49 ? 134 LEU   A CD1 1 
ATOM   1048 C CD2 . LEU   A 1 133 ? 27.865  -31.402 -22.253 1.00 19.31 ? 134 LEU   A CD2 1 
ATOM   1049 N N   . THR   A 1 134 ? 31.892  -29.289 -20.355 1.00 17.87 ? 135 THR   A N   1 
ATOM   1050 C CA  . THR   A 1 134 ? 33.284  -29.554 -20.710 1.00 16.42 ? 135 THR   A CA  1 
ATOM   1051 C C   . THR   A 1 134 ? 34.143  -29.709 -19.460 1.00 17.68 ? 135 THR   A C   1 
ATOM   1052 O O   . THR   A 1 134 ? 34.974  -30.622 -19.375 1.00 15.86 ? 135 THR   A O   1 
ATOM   1053 C CB  . THR   A 1 134 ? 33.811  -28.426 -21.590 1.00 17.49 ? 135 THR   A CB  1 
ATOM   1054 O OG1 . THR   A 1 134 ? 33.068  -28.409 -22.815 1.00 18.27 ? 135 THR   A OG1 1 
ATOM   1055 C CG2 . THR   A 1 134 ? 35.303  -28.618 -21.902 1.00 21.65 ? 135 THR   A CG2 1 
ATOM   1056 N N   . PHE   A 1 135 ? 33.944  -28.833 -18.474 1.00 15.12 ? 136 PHE   A N   1 
ATOM   1057 C CA  . PHE   A 1 135 ? 34.691  -28.935 -17.225 1.00 15.40 ? 136 PHE   A CA  1 
ATOM   1058 C C   . PHE   A 1 135 ? 34.496  -30.304 -16.580 1.00 16.68 ? 136 PHE   A C   1 
ATOM   1059 O O   . PHE   A 1 135 ? 35.464  -30.933 -16.127 1.00 15.03 ? 136 PHE   A O   1 
ATOM   1060 C CB  . PHE   A 1 135 ? 34.258  -27.802 -16.280 1.00 16.72 ? 136 PHE   A CB  1 
ATOM   1061 C CG  . PHE   A 1 135 ? 34.775  -27.952 -14.876 1.00 16.77 ? 136 PHE   A CG  1 
ATOM   1062 C CD1 . PHE   A 1 135 ? 36.036  -27.475 -14.536 1.00 17.58 ? 136 PHE   A CD1 1 
ATOM   1063 C CD2 . PHE   A 1 135 ? 33.996  -28.553 -13.901 1.00 14.74 ? 136 PHE   A CD2 1 
ATOM   1064 C CE1 . PHE   A 1 135 ? 36.513  -27.617 -13.258 1.00 18.69 ? 136 PHE   A CE1 1 
ATOM   1065 C CE2 . PHE   A 1 135 ? 34.467  -28.702 -12.620 1.00 17.11 ? 136 PHE   A CE2 1 
ATOM   1066 C CZ  . PHE   A 1 135 ? 35.728  -28.232 -12.291 1.00 17.11 ? 136 PHE   A CZ  1 
ATOM   1067 N N   . PHE   A 1 136 ? 33.259  -30.805 -16.549 1.00 14.42 ? 137 PHE   A N   1 
ATOM   1068 C CA  . PHE   A 1 136 ? 33.068  -32.086 -15.870 1.00 15.24 ? 137 PHE   A CA  1 
ATOM   1069 C C   . PHE   A 1 136 ? 33.588  -33.266 -16.687 1.00 17.32 ? 137 PHE   A C   1 
ATOM   1070 O O   . PHE   A 1 136 ? 34.039  -34.259 -16.103 1.00 16.19 ? 137 PHE   A O   1 
ATOM   1071 C CB  . PHE   A 1 136 ? 31.596  -32.285 -15.486 1.00 16.21 ? 137 PHE   A CB  1 
ATOM   1072 C CG  . PHE   A 1 136 ? 31.166  -31.481 -14.266 1.00 16.13 ? 137 PHE   A CG  1 
ATOM   1073 C CD1 . PHE   A 1 136 ? 31.811  -31.633 -13.035 1.00 15.99 ? 137 PHE   A CD1 1 
ATOM   1074 C CD2 . PHE   A 1 136 ? 30.114  -30.585 -14.358 1.00 13.12 ? 137 PHE   A CD2 1 
ATOM   1075 C CE1 . PHE   A 1 136 ? 31.398  -30.888 -11.911 1.00 15.64 ? 137 PHE   A CE1 1 
ATOM   1076 C CE2 . PHE   A 1 136 ? 29.696  -29.848 -13.260 1.00 17.54 ? 137 PHE   A CE2 1 
ATOM   1077 C CZ  . PHE   A 1 136 ? 30.343  -29.985 -12.038 1.00 15.54 ? 137 PHE   A CZ  1 
ATOM   1078 N N   . LYS   A 1 137 ? 33.564  -33.175 -18.016 1.00 15.64 ? 138 LYS   A N   1 
ATOM   1079 C CA  . LYS   A 1 137 ? 34.176  -34.215 -18.850 1.00 15.56 ? 138 LYS   A CA  1 
ATOM   1080 C C   . LYS   A 1 137 ? 35.691  -34.254 -18.681 1.00 18.09 ? 138 LYS   A C   1 
ATOM   1081 O O   . LYS   A 1 137 ? 36.308  -35.330 -18.785 1.00 20.05 ? 138 LYS   A O   1 
ATOM   1082 C CB  . LYS   A 1 137 ? 33.838  -33.984 -20.327 1.00 17.26 ? 138 LYS   A CB  1 
ATOM   1083 C CG  . LYS   A 1 137 ? 32.357  -34.168 -20.692 1.00 19.79 ? 138 LYS   A CG  1 
ATOM   1084 C CD  . LYS   A 1 137 ? 32.118  -34.241 -22.209 1.00 21.61 ? 138 LYS   A CD  1 
ATOM   1085 C CE  . LYS   A 1 137 ? 32.720  -33.066 -22.998 1.00 25.49 ? 138 LYS   A CE  1 
ATOM   1086 N NZ  . LYS   A 1 137 ? 32.601  -33.279 -24.495 1.00 25.21 ? 138 LYS   A NZ  1 
ATOM   1087 N N   . ASP   A 1 138 ? 36.309  -33.102 -18.459 1.00 16.35 ? 139 ASP   A N   1 
ATOM   1088 C CA  . ASP   A 1 138 ? 37.762  -33.012 -18.364 1.00 17.47 ? 139 ASP   A CA  1 
ATOM   1089 C C   . ASP   A 1 138 ? 38.262  -33.271 -16.951 1.00 16.97 ? 139 ASP   A C   1 
ATOM   1090 O O   . ASP   A 1 138 ? 39.480  -33.377 -16.754 1.00 18.42 ? 139 ASP   A O   1 
ATOM   1091 C CB  . ASP   A 1 138 ? 38.244  -31.634 -18.841 1.00 19.08 ? 139 ASP   A CB  1 
ATOM   1092 C CG  . ASP   A 1 138 ? 38.081  -31.436 -20.347 1.00 19.33 ? 139 ASP   A CG  1 
ATOM   1093 O OD1 . ASP   A 1 138 ? 37.770  -32.409 -21.073 1.00 22.86 ? 139 ASP   A OD1 1 
ATOM   1094 O OD2 . ASP   A 1 138 ? 38.276  -30.283 -20.814 1.00 23.76 ? 139 ASP   A OD2 1 
ATOM   1095 N N   . TRP   A 1 139 ? 37.339  -33.389 -15.991 1.00 16.43 ? 140 TRP   A N   1 
ATOM   1096 C CA  . TRP   A 1 139 ? 37.684  -33.521 -14.584 1.00 15.62 ? 140 TRP   A CA  1 
ATOM   1097 C C   . TRP   A 1 139 ? 38.442  -34.817 -14.321 1.00 15.78 ? 140 TRP   A C   1 
ATOM   1098 O O   . TRP   A 1 139 ? 38.141  -35.863 -14.901 1.00 16.46 ? 140 TRP   A O   1 
ATOM   1099 C CB  . TRP   A 1 139 ? 36.394  -33.482 -13.765 1.00 15.56 ? 140 TRP   A CB  1 
ATOM   1100 C CG  . TRP   A 1 139 ? 36.549  -33.562 -12.273 1.00 15.64 ? 140 TRP   A CG  1 
ATOM   1101 C CD1 . TRP   A 1 139 ? 36.666  -32.511 -11.414 1.00 14.66 ? 140 TRP   A CD1 1 
ATOM   1102 C CD2 . TRP   A 1 139 ? 36.561  -34.751 -11.458 1.00 13.27 ? 140 TRP   A CD2 1 
ATOM   1103 N NE1 . TRP   A 1 139 ? 36.753  -32.967 -10.115 1.00 14.82 ? 140 TRP   A NE1 1 
ATOM   1104 C CE2 . TRP   A 1 139 ? 36.675  -34.335 -10.119 1.00 15.04 ? 140 TRP   A CE2 1 
ATOM   1105 C CE3 . TRP   A 1 139 ? 36.463  -36.120 -11.736 1.00 15.85 ? 140 TRP   A CE3 1 
ATOM   1106 C CZ2 . TRP   A 1 139 ? 36.717  -35.230 -9.056  1.00 14.69 ? 140 TRP   A CZ2 1 
ATOM   1107 C CZ3 . TRP   A 1 139 ? 36.500  -37.017 -10.675 1.00 16.89 ? 140 TRP   A CZ3 1 
ATOM   1108 C CH2 . TRP   A 1 139 ? 36.625  -36.563 -9.350  1.00 14.97 ? 140 TRP   A CH2 1 
ATOM   1109 N N   . LYS   A 1 140 ? 39.443  -34.734 -13.448 1.00 15.62 ? 141 LYS   A N   1 
ATOM   1110 C CA  . LYS   A 1 140 ? 40.190  -35.875 -12.947 1.00 19.47 ? 141 LYS   A CA  1 
ATOM   1111 C C   . LYS   A 1 140 ? 40.155  -35.850 -11.428 1.00 18.25 ? 141 LYS   A C   1 
ATOM   1112 O O   . LYS   A 1 140 ? 40.152  -34.774 -10.824 1.00 16.70 ? 141 LYS   A O   1 
ATOM   1113 C CB  . LYS   A 1 140 ? 41.648  -35.856 -13.418 1.00 20.37 ? 141 LYS   A CB  1 
ATOM   1114 C CG  . LYS   A 1 140 ? 41.839  -35.693 -14.922 1.00 26.41 ? 141 LYS   A CG  1 
ATOM   1115 C CD  . LYS   A 1 140 ? 41.769  -37.015 -15.616 1.00 28.58 ? 141 LYS   A CD  1 
ATOM   1116 C CE  . LYS   A 1 140 ? 43.062  -37.804 -15.444 1.00 30.45 ? 141 LYS   A CE  1 
ATOM   1117 N NZ  . LYS   A 1 140 ? 44.190  -37.279 -16.261 1.00 38.31 ? 141 LYS   A NZ  1 
ATOM   1118 N N   . PRO   A 1 141 ? 40.134  -37.019 -10.783 1.00 15.66 ? 142 PRO   A N   1 
ATOM   1119 C CA  . PRO   A 1 141 ? 40.150  -37.051 -9.320  1.00 13.88 ? 142 PRO   A CA  1 
ATOM   1120 C C   . PRO   A 1 141 ? 41.509  -36.647 -8.772  1.00 16.06 ? 142 PRO   A C   1 
ATOM   1121 O O   . PRO   A 1 141 ? 42.519  -36.649 -9.474  1.00 19.01 ? 142 PRO   A O   1 
ATOM   1122 C CB  . PRO   A 1 141 ? 39.832  -38.520 -8.981  1.00 17.63 ? 142 PRO   A CB  1 
ATOM   1123 C CG  . PRO   A 1 141 ? 40.262  -39.293 -10.194 1.00 16.51 ? 142 PRO   A CG  1 
ATOM   1124 C CD  . PRO   A 1 141 ? 39.989  -38.364 -11.375 1.00 18.21 ? 142 PRO   A CD  1 
ATOM   1125 N N   . LYS   A 1 142 ? 41.504  -36.277 -7.495  1.00 16.73 ? 143 LYS   A N   1 
ATOM   1126 C CA  . LYS   A 1 142 ? 42.728  -35.966 -6.780  1.00 17.93 ? 143 LYS   A CA  1 
ATOM   1127 C C   . LYS   A 1 142 ? 42.750  -36.783 -5.494  1.00 18.48 ? 143 LYS   A C   1 
ATOM   1128 O O   . LYS   A 1 142 ? 43.355  -37.863 -5.441  1.00 19.22 ? 143 LYS   A O   1 
ATOM   1129 C CB  . LYS   A 1 142 ? 42.816  -34.458 -6.511  1.00 19.27 ? 143 LYS   A CB  1 
ATOM   1130 C CG  . LYS   A 1 142 ? 44.125  -34.007 -5.909  1.00 23.49 ? 143 LYS   A CG  1 
ATOM   1131 C CD  . LYS   A 1 142 ? 44.397  -32.518 -6.201  1.00 30.87 ? 143 LYS   A CD  1 
ATOM   1132 C CE  . LYS   A 1 142 ? 44.787  -32.304 -7.673  1.00 33.12 ? 143 LYS   A CE  1 
ATOM   1133 N NZ  . LYS   A 1 142 ? 45.678  -31.111 -7.921  1.00 36.37 ? 143 LYS   A NZ  1 
ATOM   1134 N N   . ASN   A 1 143 ? 42.067  -36.299 -4.469  1.00 16.54 ? 144 ASN   A N   1 
ATOM   1135 C CA  . ASN   A 1 143 ? 42.035  -37.013 -3.199  1.00 15.25 ? 144 ASN   A CA  1 
ATOM   1136 C C   . ASN   A 1 143 ? 41.062  -38.182 -3.286  1.00 15.75 ? 144 ASN   A C   1 
ATOM   1137 O O   . ASN   A 1 143 ? 40.144  -38.183 -4.105  1.00 17.61 ? 144 ASN   A O   1 
ATOM   1138 C CB  . ASN   A 1 143 ? 41.664  -36.035 -2.084  1.00 18.33 ? 144 ASN   A CB  1 
ATOM   1139 C CG  . ASN   A 1 143 ? 42.672  -34.889 -1.993  1.00 20.21 ? 144 ASN   A CG  1 
ATOM   1140 O OD1 . ASN   A 1 143 ? 42.314  -33.721 -1.959  1.00 31.05 ? 144 ASN   A OD1 1 
ATOM   1141 N ND2 . ASN   A 1 143 ? 43.938  -35.242 -1.979  1.00 23.20 ? 144 ASN   A ND2 1 
ATOM   1142 N N   . SER   A 1 144 ? 41.297  -39.211 -2.462  1.00 17.06 ? 145 SER   A N   1 
ATOM   1143 C CA  . SER   A 1 144 ? 40.466  -40.410 -2.530  1.00 15.53 ? 145 SER   A CA  1 
ATOM   1144 C C   . SER   A 1 144 ? 38.980  -40.059 -2.499  1.00 15.65 ? 145 SER   A C   1 
ATOM   1145 O O   . SER   A 1 144 ? 38.513  -39.364 -1.594  1.00 15.92 ? 145 SER   A O   1 
ATOM   1146 C CB  . SER   A 1 144 ? 40.809  -41.353 -1.378  1.00 20.68 ? 145 SER   A CB  1 
ATOM   1147 O OG  . SER   A 1 144 ? 42.088  -41.915 -1.556  1.00 25.25 ? 145 SER   A OG  1 
ATOM   1148 N N   . ILE   A 1 145 ? 38.244  -40.542 -3.508  1.00 16.72 ? 146 ILE   A N   1 
ATOM   1149 C CA  . ILE   A 1 145 ? 36.832  -40.213 -3.629  1.00 16.13 ? 146 ILE   A CA  1 
ATOM   1150 C C   . ILE   A 1 145 ? 36.088  -40.672 -2.386  1.00 16.60 ? 146 ILE   A C   1 
ATOM   1151 O O   . ILE   A 1 145 ? 36.268  -41.804 -1.916  1.00 16.88 ? 146 ILE   A O   1 
ATOM   1152 C CB  . ILE   A 1 145 ? 36.250  -40.856 -4.893  1.00 14.72 ? 146 ILE   A CB  1 
ATOM   1153 C CG1 . ILE   A 1 145 ? 36.868  -40.205 -6.142  1.00 16.02 ? 146 ILE   A CG1 1 
ATOM   1154 C CG2 . ILE   A 1 145 ? 34.698  -40.802 -4.860  1.00 16.41 ? 146 ILE   A CG2 1 
ATOM   1155 C CD1 . ILE   A 1 145 ? 36.608  -40.985 -7.432  1.00 19.40 ? 146 ILE   A CD1 1 
ATOM   1156 N N   . GLY   A 1 146 ? 35.244  -39.788 -1.847  1.00 15.99 ? 147 GLY   A N   1 
ATOM   1157 C CA  . GLY   A 1 146 ? 34.450  -40.084 -0.672  1.00 16.94 ? 147 GLY   A CA  1 
ATOM   1158 C C   . GLY   A 1 146 ? 35.101  -39.740 0.655   1.00 18.58 ? 147 GLY   A C   1 
ATOM   1159 O O   . GLY   A 1 146 ? 34.401  -39.704 1.674   1.00 18.63 ? 147 GLY   A O   1 
ATOM   1160 N N   A GLU   A 1 147 ? 36.406  -39.467 0.680   0.22 16.74 ? 148 GLU   A N   1 
ATOM   1161 N N   B GLU   A 1 147 ? 36.409  -39.474 0.682   0.78 16.32 ? 148 GLU   A N   1 
ATOM   1162 C CA  A GLU   A 1 147 ? 37.132  -39.397 1.943   0.22 17.77 ? 148 GLU   A CA  1 
ATOM   1163 C CA  B GLU   A 1 147 ? 37.124  -39.404 1.951   0.78 17.74 ? 148 GLU   A CA  1 
ATOM   1164 C C   A GLU   A 1 147 ? 37.302  -37.990 2.503   0.22 16.85 ? 148 GLU   A C   1 
ATOM   1165 C C   B GLU   A 1 147 ? 37.328  -37.995 2.502   0.78 16.93 ? 148 GLU   A C   1 
ATOM   1166 O O   A GLU   A 1 147 ? 37.498  -37.852 3.716   0.22 15.52 ? 148 GLU   A O   1 
ATOM   1167 O O   B GLU   A 1 147 ? 37.589  -37.865 3.706   0.78 15.25 ? 148 GLU   A O   1 
ATOM   1168 C CB  A GLU   A 1 147 ? 38.517  -40.036 1.791   0.22 19.50 ? 148 GLU   A CB  1 
ATOM   1169 C CB  B GLU   A 1 147 ? 38.497  -40.079 1.831   0.78 19.47 ? 148 GLU   A CB  1 
ATOM   1170 C CG  A GLU   A 1 147 ? 38.468  -41.528 1.507   0.22 20.34 ? 148 GLU   A CG  1 
ATOM   1171 C CG  B GLU   A 1 147 ? 38.410  -41.590 1.620   0.78 20.26 ? 148 GLU   A CG  1 
ATOM   1172 C CD  A GLU   A 1 147 ? 37.763  -42.305 2.602   0.22 21.89 ? 148 GLU   A CD  1 
ATOM   1173 C CD  B GLU   A 1 147 ? 39.746  -42.310 1.773   0.78 25.57 ? 148 GLU   A CD  1 
ATOM   1174 O OE1 A GLU   A 1 147 ? 38.089  -42.094 3.788   0.22 23.50 ? 148 GLU   A OE1 1 
ATOM   1175 O OE1 B GLU   A 1 147 ? 40.714  -41.701 2.275   0.78 24.19 ? 148 GLU   A OE1 1 
ATOM   1176 O OE2 A GLU   A 1 147 ? 36.878  -43.122 2.277   0.22 23.71 ? 148 GLU   A OE2 1 
ATOM   1177 O OE2 B GLU   A 1 147 ? 39.827  -43.503 1.393   0.78 26.97 ? 148 GLU   A OE2 1 
ATOM   1178 N N   . TYR   A 1 148 ? 37.248  -36.949 1.674   1.00 16.10 ? 149 TYR   A N   1 
ATOM   1179 C CA  . TYR   A 1 148 ? 37.497  -35.588 2.141   1.00 15.17 ? 149 TYR   A CA  1 
ATOM   1180 C C   . TYR   A 1 148 ? 36.363  -34.655 1.758   1.00 15.62 ? 149 TYR   A C   1 
ATOM   1181 O O   . TYR   A 1 148 ? 35.984  -34.577 0.583   1.00 16.00 ? 149 TYR   A O   1 
ATOM   1182 C CB  . TYR   A 1 148 ? 38.817  -35.048 1.573   1.00 16.62 ? 149 TYR   A CB  1 
ATOM   1183 C CG  . TYR   A 1 148 ? 39.991  -35.919 1.916   1.00 19.29 ? 149 TYR   A CG  1 
ATOM   1184 C CD1 . TYR   A 1 148 ? 40.350  -36.980 1.086   1.00 22.65 ? 149 TYR   A CD1 1 
ATOM   1185 C CD2 . TYR   A 1 148 ? 40.747  -35.682 3.051   1.00 21.80 ? 149 TYR   A CD2 1 
ATOM   1186 C CE1 . TYR   A 1 148 ? 41.422  -37.784 1.382   1.00 24.28 ? 149 TYR   A CE1 1 
ATOM   1187 C CE2 . TYR   A 1 148 ? 41.833  -36.510 3.376   1.00 20.98 ? 149 TYR   A CE2 1 
ATOM   1188 C CZ  . TYR   A 1 148 ? 42.163  -37.547 2.530   1.00 23.94 ? 149 TYR   A CZ  1 
ATOM   1189 O OH  . TYR   A 1 148 ? 43.240  -38.354 2.811   1.00 27.27 ? 149 TYR   A OH  1 
ATOM   1190 N N   . ARG   A 1 149 ? 35.866  -33.917 2.747   1.00 14.42 ? 150 ARG   A N   1 
ATOM   1191 C CA  . ARG   A 1 149 ? 34.861  -32.886 2.518   1.00 14.95 ? 150 ARG   A CA  1 
ATOM   1192 C C   . ARG   A 1 149 ? 35.522  -31.572 2.123   1.00 14.47 ? 150 ARG   A C   1 
ATOM   1193 O O   . ARG   A 1 149 ? 36.380  -31.060 2.849   1.00 14.11 ? 150 ARG   A O   1 
ATOM   1194 C CB  . ARG   A 1 149 ? 34.042  -32.655 3.785   1.00 13.69 ? 150 ARG   A CB  1 
ATOM   1195 C CG  . ARG   A 1 149 ? 32.982  -31.584 3.620   1.00 14.73 ? 150 ARG   A CG  1 
ATOM   1196 C CD  . ARG   A 1 149 ? 32.392  -31.260 4.991   1.00 12.39 ? 150 ARG   A CD  1 
ATOM   1197 N NE  . ARG   A 1 149 ? 31.270  -30.337 4.870   1.00 12.55 ? 150 ARG   A NE  1 
ATOM   1198 C CZ  . ARG   A 1 149 ? 31.379  -29.016 4.831   1.00 15.67 ? 150 ARG   A CZ  1 
ATOM   1199 N NH1 . ARG   A 1 149 ? 32.559  -28.417 4.906   1.00 14.00 ? 150 ARG   A NH1 1 
ATOM   1200 N NH2 . ARG   A 1 149 ? 30.270  -28.276 4.695   1.00 16.69 ? 150 ARG   A NH2 1 
ATOM   1201 N N   . GLN   A 1 150 ? 35.099  -31.005 0.998   1.00 13.07 ? 151 GLN   A N   1 
ATOM   1202 C CA  . GLN   A 1 150 ? 35.476  -29.634 0.653   1.00 12.71 ? 151 GLN   A CA  1 
ATOM   1203 C C   . GLN   A 1 150 ? 34.226  -28.941 0.129   1.00 12.20 ? 151 GLN   A C   1 
ATOM   1204 O O   . GLN   A 1 150 ? 33.699  -29.325 -0.918  1.00 13.58 ? 151 GLN   A O   1 
ATOM   1205 C CB  . GLN   A 1 150 ? 36.604  -29.582 -0.385  1.00 14.92 ? 151 GLN   A CB  1 
ATOM   1206 C CG  . GLN   A 1 150 ? 37.007  -28.147 -0.692  1.00 16.65 ? 151 GLN   A CG  1 
ATOM   1207 C CD  . GLN   A 1 150 ? 38.337  -28.020 -1.408  1.00 20.82 ? 151 GLN   A CD  1 
ATOM   1208 O OE1 . GLN   A 1 150 ? 38.721  -28.885 -2.185  1.00 22.79 ? 151 GLN   A OE1 1 
ATOM   1209 N NE2 . GLN   A 1 150 ? 39.055  -26.938 -1.130  1.00 23.39 ? 151 GLN   A NE2 1 
ATOM   1210 N N   . TYR   A 1 151 ? 33.725  -27.969 0.899   1.00 13.88 ? 152 TYR   A N   1 
ATOM   1211 C CA  . TYR   A 1 151 ? 32.497  -27.270 0.547   1.00 12.92 ? 152 TYR   A CA  1 
ATOM   1212 C C   . TYR   A 1 151 ? 32.602  -26.733 -0.877  1.00 13.69 ? 152 TYR   A C   1 
ATOM   1213 O O   . TYR   A 1 151 ? 33.587  -26.077 -1.223  1.00 14.30 ? 152 TYR   A O   1 
ATOM   1214 C CB  . TYR   A 1 151 ? 32.269  -26.132 1.548   1.00 12.71 ? 152 TYR   A CB  1 
ATOM   1215 C CG  . TYR   A 1 151 ? 30.928  -25.436 1.425   1.00 13.56 ? 152 TYR   A CG  1 
ATOM   1216 C CD1 . TYR   A 1 151 ? 29.742  -26.120 1.682   1.00 14.09 ? 152 TYR   A CD1 1 
ATOM   1217 C CD2 . TYR   A 1 151 ? 30.857  -24.089 1.096   1.00 16.33 ? 152 TYR   A CD2 1 
ATOM   1218 C CE1 . TYR   A 1 151 ? 28.527  -25.497 1.590   1.00 15.76 ? 152 TYR   A CE1 1 
ATOM   1219 C CE2 . TYR   A 1 151 ? 29.628  -23.450 0.990   1.00 18.40 ? 152 TYR   A CE2 1 
ATOM   1220 C CZ  . TYR   A 1 151 ? 28.474  -24.161 1.241   1.00 16.93 ? 152 TYR   A CZ  1 
ATOM   1221 O OH  . TYR   A 1 151 ? 27.249  -23.550 1.160   1.00 16.65 ? 152 TYR   A OH  1 
ATOM   1222 N N   . SER   A 1 152 ? 31.587  -27.005 -1.702  1.00 11.74 ? 153 SER   A N   1 
ATOM   1223 C CA  . SER   A 1 152 ? 31.762  -26.837 -3.148  1.00 12.74 ? 153 SER   A CA  1 
ATOM   1224 C C   . SER   A 1 152 ? 30.452  -26.523 -3.870  1.00 13.10 ? 153 SER   A C   1 
ATOM   1225 O O   . SER   A 1 152 ? 29.527  -27.344 -3.877  1.00 13.41 ? 153 SER   A O   1 
ATOM   1226 C CB  . SER   A 1 152 ? 32.399  -28.105 -3.732  1.00 12.23 ? 153 SER   A CB  1 
ATOM   1227 O OG  . SER   A 1 152 ? 32.460  -28.012 -5.151  1.00 12.37 ? 153 SER   A OG  1 
ATOM   1228 N N   . ASN   A 1 153 ? 30.387  -25.355 -4.518  1.00 11.46 ? 154 ASN   A N   1 
ATOM   1229 C CA  . ASN   A 1 153 ? 29.231  -25.067 -5.369  1.00 12.34 ? 154 ASN   A CA  1 
ATOM   1230 C C   . ASN   A 1 153 ? 29.172  -25.969 -6.601  1.00 15.14 ? 154 ASN   A C   1 
ATOM   1231 O O   . ASN   A 1 153 ? 28.077  -26.483 -6.906  1.00 14.25 ? 154 ASN   A O   1 
ATOM   1232 C CB  . ASN   A 1 153 ? 29.223  -23.578 -5.738  1.00 12.91 ? 154 ASN   A CB  1 
ATOM   1233 C CG  . ASN   A 1 153 ? 28.853  -22.712 -4.569  1.00 16.17 ? 154 ASN   A CG  1 
ATOM   1234 O OD1 . ASN   A 1 153 ? 28.276  -23.187 -3.599  1.00 16.50 ? 154 ASN   A OD1 1 
ATOM   1235 N ND2 . ASN   A 1 153 ? 29.169  -21.426 -4.658  1.00 22.21 ? 154 ASN   A ND2 1 
ATOM   1236 N N   . PRO   A 1 154 ? 30.267  -26.193 -7.351  1.00 13.55 ? 155 PRO   A N   1 
ATOM   1237 C CA  . PRO   A 1 154 ? 30.208  -27.154 -8.472  1.00 14.13 ? 155 PRO   A CA  1 
ATOM   1238 C C   . PRO   A 1 154 ? 29.688  -28.524 -8.072  1.00 13.64 ? 155 PRO   A C   1 
ATOM   1239 O O   . PRO   A 1 154 ? 28.933  -29.151 -8.829  1.00 13.96 ? 155 PRO   A O   1 
ATOM   1240 C CB  . PRO   A 1 154 ? 31.670  -27.217 -8.946  1.00 15.56 ? 155 PRO   A CB  1 
ATOM   1241 C CG  . PRO   A 1 154 ? 32.233  -25.873 -8.591  1.00 16.87 ? 155 PRO   A CG  1 
ATOM   1242 C CD  . PRO   A 1 154 ? 31.555  -25.467 -7.310  1.00 14.31 ? 155 PRO   A CD  1 
ATOM   1243 N N   . SER   A 1 155 ? 30.070  -29.004 -6.891  1.00 13.73 ? 156 SER   A N   1 
ATOM   1244 C CA  . SER   A 1 155 ? 29.696  -30.351 -6.471  1.00 14.34 ? 156 SER   A CA  1 
ATOM   1245 C C   . SER   A 1 155 ? 28.182  -30.481 -6.319  1.00 12.31 ? 156 SER   A C   1 
ATOM   1246 O O   . SER   A 1 155 ? 27.552  -31.386 -6.892  1.00 13.58 ? 156 SER   A O   1 
ATOM   1247 C CB  . SER   A 1 155 ? 30.405  -30.694 -5.154  1.00 13.47 ? 156 SER   A CB  1 
ATOM   1248 O OG  . SER   A 1 155 ? 30.273  -32.087 -4.837  1.00 12.74 ? 156 SER   A OG  1 
ATOM   1249 N N   . ILE   A 1 156 ? 27.572  -29.573 -5.555  1.00 13.08 ? 157 ILE   A N   1 
ATOM   1250 C CA  . ILE   A 1 156 ? 26.132  -29.709 -5.361  1.00 14.51 ? 157 ILE   A CA  1 
ATOM   1251 C C   . ILE   A 1 156 ? 25.372  -29.198 -6.588  1.00 12.97 ? 157 ILE   A C   1 
ATOM   1252 O O   . ILE   A 1 156 ? 24.221  -29.606 -6.817  1.00 14.50 ? 157 ILE   A O   1 
ATOM   1253 C CB  . ILE   A 1 156 ? 25.714  -29.027 -4.048  1.00 17.40 ? 157 ILE   A CB  1 
ATOM   1254 C CG1 . ILE   A 1 156 ? 24.300  -29.498 -3.639  1.00 18.18 ? 157 ILE   A CG1 1 
ATOM   1255 C CG2 . ILE   A 1 156 ? 25.790  -27.535 -4.213  1.00 17.41 ? 157 ILE   A CG2 1 
ATOM   1256 C CD1 . ILE   A 1 156 ? 23.894  -29.133 -2.236  1.00 17.07 ? 157 ILE   A CD1 1 
ATOM   1257 N N   . GLY   A 1 157 ? 25.995  -28.344 -7.411  1.00 13.80 ? 158 GLY   A N   1 
ATOM   1258 C CA  . GLY   A 1 157 ? 25.383  -27.989 -8.682  1.00 14.41 ? 158 GLY   A CA  1 
ATOM   1259 C C   . GLY   A 1 157 ? 25.210  -29.186 -9.603  1.00 11.97 ? 158 GLY   A C   1 
ATOM   1260 O O   . GLY   A 1 157 ? 24.150  -29.364 -10.219 1.00 14.43 ? 158 GLY   A O   1 
ATOM   1261 N N   . LEU   A 1 158 ? 26.240  -30.034 -9.696  1.00 14.17 ? 159 LEU   A N   1 
ATOM   1262 C CA  . LEU   A 1 158 ? 26.117  -31.251 -10.497 1.00 13.73 ? 159 LEU   A CA  1 
ATOM   1263 C C   . LEU   A 1 158 ? 25.045  -32.162 -9.921  1.00 14.90 ? 159 LEU   A C   1 
ATOM   1264 O O   . LEU   A 1 158 ? 24.212  -32.704 -10.662 1.00 14.31 ? 159 LEU   A O   1 
ATOM   1265 C CB  . LEU   A 1 158 ? 27.467  -31.979 -10.588 1.00 14.18 ? 159 LEU   A CB  1 
ATOM   1266 C CG  . LEU   A 1 158 ? 27.493  -33.264 -11.442 1.00 14.98 ? 159 LEU   A CG  1 
ATOM   1267 C CD1 . LEU   A 1 158 ? 26.974  -33.072 -12.858 1.00 18.89 ? 159 LEU   A CD1 1 
ATOM   1268 C CD2 . LEU   A 1 158 ? 28.896  -33.874 -11.460 1.00 17.12 ? 159 LEU   A CD2 1 
ATOM   1269 N N   . PHE   A 1 159 ? 25.005  -32.291 -8.595  1.00 13.73 ? 160 PHE   A N   1 
ATOM   1270 C CA  . PHE   A 1 159 ? 23.946  -33.074 -7.974  1.00 14.99 ? 160 PHE   A CA  1 
ATOM   1271 C C   . PHE   A 1 159 ? 22.568  -32.546 -8.370  1.00 14.34 ? 160 PHE   A C   1 
ATOM   1272 O O   . PHE   A 1 159 ? 21.668  -33.318 -8.736  1.00 13.98 ? 160 PHE   A O   1 
ATOM   1273 C CB  . PHE   A 1 159 ? 24.136  -33.056 -6.456  1.00 15.21 ? 160 PHE   A CB  1 
ATOM   1274 C CG  . PHE   A 1 159 ? 23.048  -33.767 -5.680  1.00 11.45 ? 160 PHE   A CG  1 
ATOM   1275 C CD1 . PHE   A 1 159 ? 22.986  -35.150 -5.630  1.00 13.74 ? 160 PHE   A CD1 1 
ATOM   1276 C CD2 . PHE   A 1 159 ? 22.095  -33.028 -4.978  1.00 13.09 ? 160 PHE   A CD2 1 
ATOM   1277 C CE1 . PHE   A 1 159 ? 21.985  -35.778 -4.915  1.00 15.42 ? 160 PHE   A CE1 1 
ATOM   1278 C CE2 . PHE   A 1 159 ? 21.091  -33.658 -4.240  1.00 14.10 ? 160 PHE   A CE2 1 
ATOM   1279 C CZ  . PHE   A 1 159 ? 21.040  -35.040 -4.214  1.00 15.31 ? 160 PHE   A CZ  1 
ATOM   1280 N N   . GLY   A 1 160 ? 22.386  -31.226 -8.292  1.00 12.98 ? 161 GLY   A N   1 
ATOM   1281 C CA  . GLY   A 1 160 ? 21.113  -30.637 -8.679  1.00 12.84 ? 161 GLY   A CA  1 
ATOM   1282 C C   . GLY   A 1 160 ? 20.760  -30.850 -10.139 1.00 14.60 ? 161 GLY   A C   1 
ATOM   1283 O O   . GLY   A 1 160 ? 19.606  -31.120 -10.461 1.00 15.90 ? 161 GLY   A O   1 
ATOM   1284 N N   . LYS   A 1 161 ? 21.743  -30.707 -11.042 1.00 12.80 ? 162 LYS   A N   1 
ATOM   1285 C CA  . LYS   A 1 161 ? 21.512  -30.980 -12.458 1.00 17.03 ? 162 LYS   A CA  1 
ATOM   1286 C C   . LYS   A 1 161 ? 21.048  -32.420 -12.678 1.00 16.69 ? 162 LYS   A C   1 
ATOM   1287 O O   . LYS   A 1 161 ? 20.126  -32.668 -13.467 1.00 17.02 ? 162 LYS   A O   1 
ATOM   1288 C CB  . LYS   A 1 161 ? 22.800  -30.690 -13.238 1.00 14.78 ? 162 LYS   A CB  1 
ATOM   1289 C CG  . LYS   A 1 161 ? 22.812  -31.155 -14.687 1.00 21.08 ? 162 LYS   A CG  1 
ATOM   1290 C CD  . LYS   A 1 161 ? 21.947  -30.314 -15.554 1.00 23.87 ? 162 LYS   A CD  1 
ATOM   1291 C CE  . LYS   A 1 161 ? 22.109  -30.729 -17.014 1.00 22.52 ? 162 LYS   A CE  1 
ATOM   1292 N NZ  . LYS   A 1 161 ? 21.166  -29.951 -17.852 1.00 27.02 ? 162 LYS   A NZ  1 
ATOM   1293 N N   . VAL   A 1 162 ? 21.664  -33.374 -11.973 1.00 14.85 ? 163 VAL   A N   1 
ATOM   1294 C CA  . VAL   A 1 162 ? 21.276  -34.780 -12.112 1.00 16.29 ? 163 VAL   A CA  1 
ATOM   1295 C C   . VAL   A 1 162 ? 19.873  -35.013 -11.561 1.00 15.60 ? 163 VAL   A C   1 
ATOM   1296 O O   . VAL   A 1 162 ? 19.057  -35.720 -12.178 1.00 14.96 ? 163 VAL   A O   1 
ATOM   1297 C CB  . VAL   A 1 162 ? 22.320  -35.684 -11.433 1.00 16.65 ? 163 VAL   A CB  1 
ATOM   1298 C CG1 . VAL   A 1 162 ? 21.772  -37.117 -11.277 1.00 19.23 ? 163 VAL   A CG1 1 
ATOM   1299 C CG2 . VAL   A 1 162 ? 23.609  -35.665 -12.253 1.00 17.94 ? 163 VAL   A CG2 1 
ATOM   1300 N N   . VAL   A 1 163 ? 19.559  -34.420 -10.405 1.00 15.05 ? 164 VAL   A N   1 
ATOM   1301 C CA  . VAL   A 1 163 ? 18.209  -34.531 -9.852  1.00 15.48 ? 164 VAL   A CA  1 
ATOM   1302 C C   . VAL   A 1 163 ? 17.181  -34.047 -10.866 1.00 17.75 ? 164 VAL   A C   1 
ATOM   1303 O O   . VAL   A 1 163 ? 16.167  -34.707 -11.110 1.00 18.90 ? 164 VAL   A O   1 
ATOM   1304 C CB  . VAL   A 1 163 ? 18.106  -33.759 -8.524  1.00 16.12 ? 164 VAL   A CB  1 
ATOM   1305 C CG1 . VAL   A 1 163 ? 16.653  -33.618 -8.101  1.00 17.90 ? 164 VAL   A CG1 1 
ATOM   1306 C CG2 . VAL   A 1 163 ? 18.892  -34.455 -7.430  1.00 15.02 ? 164 VAL   A CG2 1 
ATOM   1307 N N   . ALA   A 1 164 ? 17.450  -32.901 -11.500 1.00 16.26 ? 165 ALA   A N   1 
ATOM   1308 C CA  . ALA   A 1 164 ? 16.534  -32.374 -12.506 1.00 16.08 ? 165 ALA   A CA  1 
ATOM   1309 C C   . ALA   A 1 164 ? 16.381  -33.337 -13.684 1.00 19.14 ? 165 ALA   A C   1 
ATOM   1310 O O   . ALA   A 1 164 ? 15.260  -33.599 -14.147 1.00 18.59 ? 165 ALA   A O   1 
ATOM   1311 C CB  . ALA   A 1 164 ? 17.020  -31.004 -12.977 1.00 17.58 ? 165 ALA   A CB  1 
ATOM   1312 N N   . LEU   A 1 165 ? 17.499  -33.861 -14.201 1.00 16.69 ? 166 LEU   A N   1 
ATOM   1313 C CA  . LEU   A 1 165 ? 17.415  -34.815 -15.308 1.00 18.00 ? 166 LEU   A CA  1 
ATOM   1314 C C   . LEU   A 1 165 ? 16.590  -36.039 -14.924 1.00 19.79 ? 166 LEU   A C   1 
ATOM   1315 O O   . LEU   A 1 165 ? 15.816  -36.557 -15.742 1.00 18.81 ? 166 LEU   A O   1 
ATOM   1316 C CB  . LEU   A 1 165 ? 18.815  -35.233 -15.762 1.00 17.18 ? 166 LEU   A CB  1 
ATOM   1317 C CG  . LEU   A 1 165 ? 19.637  -34.130 -16.428 1.00 18.18 ? 166 LEU   A CG  1 
ATOM   1318 C CD1 . LEU   A 1 165 ? 21.113  -34.517 -16.496 1.00 18.28 ? 166 LEU   A CD1 1 
ATOM   1319 C CD2 . LEU   A 1 165 ? 19.072  -33.838 -17.836 1.00 20.67 ? 166 LEU   A CD2 1 
ATOM   1320 N N   . SER   A 1 166 ? 16.749  -36.521 -13.688 1.00 19.01 ? 167 SER   A N   1 
ATOM   1321 C CA  . SER   A 1 166 ? 15.994  -37.698 -13.252 1.00 16.40 ? 167 SER   A CA  1 
ATOM   1322 C C   . SER   A 1 166 ? 14.495  -37.433 -13.190 1.00 18.72 ? 167 SER   A C   1 
ATOM   1323 O O   . SER   A 1 166 ? 13.706  -38.389 -13.246 1.00 20.35 ? 167 SER   A O   1 
ATOM   1324 C CB  . SER   A 1 166 ? 16.476  -38.162 -11.881 1.00 17.46 ? 167 SER   A CB  1 
ATOM   1325 O OG  . SER   A 1 166 ? 15.929  -37.365 -10.845 1.00 18.38 ? 167 SER   A OG  1 
ATOM   1326 N N   . MET   A 1 167 ? 14.096  -36.169 -13.061 1.00 17.35 ? 168 MET   A N   1 
ATOM   1327 C CA  . MET   A 1 167 ? 12.700  -35.764 -12.978 1.00 21.47 ? 168 MET   A CA  1 
ATOM   1328 C C   . MET   A 1 167 ? 12.179  -35.191 -14.299 1.00 23.47 ? 168 MET   A C   1 
ATOM   1329 O O   . MET   A 1 167 ? 11.038  -34.711 -14.354 1.00 22.33 ? 168 MET   A O   1 
ATOM   1330 C CB  . MET   A 1 167 ? 12.524  -34.752 -11.834 1.00 20.33 ? 168 MET   A CB  1 
ATOM   1331 C CG  . MET   A 1 167 ? 12.815  -35.349 -10.442 1.00 23.19 ? 168 MET   A CG  1 
ATOM   1332 S SD  . MET   A 1 167 ? 12.903  -34.160 -9.073  1.00 26.99 ? 168 MET   A SD  1 
ATOM   1333 C CE  . MET   A 1 167 ? 11.189  -33.629 -8.969  1.00 27.76 ? 168 MET   A CE  1 
ATOM   1334 N N   . ASN   A 1 168 ? 12.994  -35.236 -15.359 1.00 20.74 ? 169 ASN   A N   1 
ATOM   1335 C CA  . ASN   A 1 168 ? 12.604  -34.822 -16.712 1.00 22.11 ? 169 ASN   A CA  1 
ATOM   1336 C C   . ASN   A 1 168 ? 12.077  -33.391 -16.761 1.00 23.73 ? 169 ASN   A C   1 
ATOM   1337 O O   . ASN   A 1 168 ? 11.137  -33.085 -17.497 1.00 22.16 ? 169 ASN   A O   1 
ATOM   1338 C CB  . ASN   A 1 168 ? 11.584  -35.792 -17.307 1.00 22.98 ? 169 ASN   A CB  1 
ATOM   1339 C CG  . ASN   A 1 168 ? 12.114  -37.211 -17.376 1.00 31.13 ? 169 ASN   A CG  1 
ATOM   1340 O OD1 . ASN   A 1 168 ? 11.561  -38.122 -16.761 1.00 37.98 ? 169 ASN   A OD1 1 
ATOM   1341 N ND2 . ASN   A 1 168 ? 13.196  -37.405 -18.128 1.00 34.49 ? 169 ASN   A ND2 1 
ATOM   1342 N N   . LYS   A 1 169 ? 12.693  -32.500 -15.988 1.00 20.13 ? 170 LYS   A N   1 
ATOM   1343 C CA  . LYS   A 1 169 ? 12.380  -31.077 -16.073 1.00 22.84 ? 170 LYS   A CA  1 
ATOM   1344 C C   . LYS   A 1 169 ? 13.587  -30.262 -15.632 1.00 21.86 ? 170 LYS   A C   1 
ATOM   1345 O O   . LYS   A 1 169 ? 14.438  -30.771 -14.893 1.00 20.47 ? 170 LYS   A O   1 
ATOM   1346 C CB  . LYS   A 1 169 ? 11.139  -30.720 -15.229 1.00 25.69 ? 170 LYS   A CB  1 
ATOM   1347 C CG  . LYS   A 1 169 ? 11.191  -31.119 -13.782 1.00 29.67 ? 170 LYS   A CG  1 
ATOM   1348 C CD  . LYS   A 1 169 ? 9.876   -30.770 -13.056 1.00 29.82 ? 170 LYS   A CD  1 
ATOM   1349 C CE  . LYS   A 1 169 ? 8.697   -31.636 -13.508 1.00 37.59 ? 170 LYS   A CE  1 
ATOM   1350 N NZ  . LYS   A 1 169 ? 8.757   -33.011 -12.916 1.00 32.78 ? 170 LYS   A NZ  1 
ATOM   1351 N N   . PRO   A 1 170 ? 13.716  -29.020 -16.097 1.00 19.11 ? 171 PRO   A N   1 
ATOM   1352 C CA  . PRO   A 1 170 ? 14.866  -28.206 -15.683 1.00 20.30 ? 171 PRO   A CA  1 
ATOM   1353 C C   . PRO   A 1 170 ? 14.811  -27.897 -14.194 1.00 19.36 ? 171 PRO   A C   1 
ATOM   1354 O O   . PRO   A 1 170 ? 13.752  -27.925 -13.564 1.00 18.92 ? 171 PRO   A O   1 
ATOM   1355 C CB  . PRO   A 1 170 ? 14.753  -26.933 -16.525 1.00 21.23 ? 171 PRO   A CB  1 
ATOM   1356 C CG  . PRO   A 1 170 ? 13.385  -26.985 -17.173 1.00 24.46 ? 171 PRO   A CG  1 
ATOM   1357 C CD  . PRO   A 1 170 ? 12.901  -28.386 -17.156 1.00 21.11 ? 171 PRO   A CD  1 
ATOM   1358 N N   . PHE   A 1 171 ? 15.989  -27.615 -13.624 1.00 16.06 ? 172 PHE   A N   1 
ATOM   1359 C CA  . PHE   A 1 171 ? 16.076  -27.474 -12.176 1.00 16.84 ? 172 PHE   A CA  1 
ATOM   1360 C C   . PHE   A 1 171 ? 15.140  -26.385 -11.664 1.00 17.53 ? 172 PHE   A C   1 
ATOM   1361 O O   . PHE   A 1 171 ? 14.501  -26.555 -10.619 1.00 17.52 ? 172 PHE   A O   1 
ATOM   1362 C CB  . PHE   A 1 171 ? 17.512  -27.184 -11.762 1.00 18.23 ? 172 PHE   A CB  1 
ATOM   1363 C CG  . PHE   A 1 171 ? 17.684  -27.060 -10.287 1.00 16.74 ? 172 PHE   A CG  1 
ATOM   1364 C CD1 . PHE   A 1 171 ? 17.825  -28.182 -9.501  1.00 17.24 ? 172 PHE   A CD1 1 
ATOM   1365 C CD2 . PHE   A 1 171 ? 17.677  -25.818 -9.682  1.00 17.64 ? 172 PHE   A CD2 1 
ATOM   1366 C CE1 . PHE   A 1 171 ? 17.971  -28.075 -8.124  1.00 16.16 ? 172 PHE   A CE1 1 
ATOM   1367 C CE2 . PHE   A 1 171 ? 17.827  -25.702 -8.317  1.00 15.69 ? 172 PHE   A CE2 1 
ATOM   1368 C CZ  . PHE   A 1 171 ? 17.974  -26.830 -7.532  1.00 15.27 ? 172 PHE   A CZ  1 
ATOM   1369 N N   . ASP   A 1 172 ? 15.022  -25.273 -12.396 1.00 17.89 ? 173 ASP   A N   1 
ATOM   1370 C CA  . ASP   A 1 172 ? 14.151  -24.201 -11.915 1.00 17.96 ? 173 ASP   A CA  1 
ATOM   1371 C C   . ASP   A 1 172 ? 12.714  -24.682 -11.798 1.00 19.50 ? 173 ASP   A C   1 
ATOM   1372 O O   . ASP   A 1 172 ? 11.987  -24.256 -10.890 1.00 18.68 ? 173 ASP   A O   1 
ATOM   1373 C CB  . ASP   A 1 172 ? 14.228  -22.969 -12.828 1.00 20.51 ? 173 ASP   A CB  1 
ATOM   1374 C CG  . ASP   A 1 172 ? 13.628  -23.215 -14.205 1.00 25.51 ? 173 ASP   A CG  1 
ATOM   1375 O OD1 . ASP   A 1 172 ? 14.155  -24.076 -14.939 1.00 23.90 ? 173 ASP   A OD1 1 
ATOM   1376 O OD2 . ASP   A 1 172 ? 12.620  -22.552 -14.552 1.00 25.70 ? 173 ASP   A OD2 1 
ATOM   1377 N N   . GLN   A 1 173 ? 12.297  -25.577 -12.701 1.00 16.59 ? 174 GLN   A N   1 
ATOM   1378 C CA  . GLN   A 1 173 ? 10.955  -26.127 -12.652 1.00 19.20 ? 174 GLN   A CA  1 
ATOM   1379 C C   . GLN   A 1 173 ? 10.823  -27.171 -11.554 1.00 19.01 ? 174 GLN   A C   1 
ATOM   1380 O O   . GLN   A 1 173 ? 9.760   -27.267 -10.931 1.00 19.87 ? 174 GLN   A O   1 
ATOM   1381 C CB  . GLN   A 1 173 ? 10.583  -26.691 -14.026 1.00 17.98 ? 174 GLN   A CB  1 
ATOM   1382 C CG  . GLN   A 1 173 ? 10.457  -25.599 -15.087 1.00 21.27 ? 174 GLN   A CG  1 
ATOM   1383 C CD  . GLN   A 1 173 ? 9.389   -24.582 -14.723 1.00 26.01 ? 174 GLN   A CD  1 
ATOM   1384 O OE1 . GLN   A 1 173 ? 8.196   -24.883 -14.747 1.00 30.20 ? 174 GLN   A OE1 1 
ATOM   1385 N NE2 . GLN   A 1 173 ? 9.815   -23.377 -14.364 1.00 28.95 ? 174 GLN   A NE2 1 
ATOM   1386 N N   . VAL   A 1 174 ? 11.886  -27.929 -11.273 1.00 15.96 ? 175 VAL   A N   1 
ATOM   1387 C CA  . VAL   A 1 174 ? 11.843  -28.840 -10.130 1.00 16.77 ? 175 VAL   A CA  1 
ATOM   1388 C C   . VAL   A 1 174 ? 11.441  -28.082 -8.871  1.00 17.84 ? 175 VAL   A C   1 
ATOM   1389 O O   . VAL   A 1 174 ? 10.552  -28.509 -8.122  1.00 17.76 ? 175 VAL   A O   1 
ATOM   1390 C CB  . VAL   A 1 174 ? 13.191  -29.559 -9.944  1.00 19.36 ? 175 VAL   A CB  1 
ATOM   1391 C CG1 . VAL   A 1 174 ? 13.202  -30.284 -8.608  1.00 19.28 ? 175 VAL   A CG1 1 
ATOM   1392 C CG2 . VAL   A 1 174 ? 13.413  -30.537 -11.095 1.00 20.35 ? 175 VAL   A CG2 1 
ATOM   1393 N N   . LEU   A 1 175 ? 12.062  -26.922 -8.639  1.00 16.51 ? 176 LEU   A N   1 
ATOM   1394 C CA  . LEU   A 1 175 ? 11.750  -26.140 -7.444  1.00 16.84 ? 176 LEU   A CA  1 
ATOM   1395 C C   . LEU   A 1 175 ? 10.425  -25.395 -7.581  1.00 17.82 ? 176 LEU   A C   1 
ATOM   1396 O O   . LEU   A 1 175 ? 9.560   -25.480 -6.701  1.00 17.97 ? 176 LEU   A O   1 
ATOM   1397 C CB  . LEU   A 1 175 ? 12.884  -25.151 -7.131  1.00 14.46 ? 176 LEU   A CB  1 
ATOM   1398 C CG  . LEU   A 1 175 ? 14.199  -25.796 -6.683  1.00 14.56 ? 176 LEU   A CG  1 
ATOM   1399 C CD1 . LEU   A 1 175 ? 15.182  -24.752 -6.143  1.00 16.01 ? 176 LEU   A CD1 1 
ATOM   1400 C CD2 . LEU   A 1 175 ? 14.011  -26.905 -5.654  1.00 15.58 ? 176 LEU   A CD2 1 
ATOM   1401 N N   . GLU   A 1 176 ? 10.223  -24.676 -8.687  1.00 18.81 ? 177 GLU   A N   1 
ATOM   1402 C CA  . GLU   A 1 176 ? 9.047   -23.809 -8.745  1.00 19.89 ? 177 GLU   A CA  1 
ATOM   1403 C C   . GLU   A 1 176 ? 7.745   -24.568 -9.006  1.00 20.06 ? 177 GLU   A C   1 
ATOM   1404 O O   . GLU   A 1 176 ? 6.667   -24.086 -8.621  1.00 21.78 ? 177 GLU   A O   1 
ATOM   1405 C CB  . GLU   A 1 176 ? 9.261   -22.714 -9.796  1.00 20.88 ? 177 GLU   A CB  1 
ATOM   1406 C CG  . GLU   A 1 176 ? 10.395  -21.779 -9.403  1.00 19.62 ? 177 GLU   A CG  1 
ATOM   1407 C CD  . GLU   A 1 176 ? 10.611  -20.632 -10.379 1.00 21.95 ? 177 GLU   A CD  1 
ATOM   1408 O OE1 . GLU   A 1 176 ? 9.963   -20.592 -11.450 1.00 23.71 ? 177 GLU   A OE1 1 
ATOM   1409 O OE2 . GLU   A 1 176 ? 11.452  -19.765 -10.072 1.00 20.66 ? 177 GLU   A OE2 1 
ATOM   1410 N N   . LYS   A 1 177 ? 7.801   -25.739 -9.642  1.00 18.06 ? 178 LYS   A N   1 
ATOM   1411 C CA  . LYS   A 1 177 ? 6.586   -26.492 -9.915  1.00 21.45 ? 178 LYS   A CA  1 
ATOM   1412 C C   . LYS   A 1 177 ? 6.344   -27.644 -8.953  1.00 19.08 ? 178 LYS   A C   1 
ATOM   1413 O O   . LYS   A 1 177 ? 5.175   -27.997 -8.727  1.00 22.72 ? 178 LYS   A O   1 
ATOM   1414 C CB  . LYS   A 1 177 ? 6.610   -27.035 -11.348 1.00 24.32 ? 178 LYS   A CB  1 
ATOM   1415 C CG  . LYS   A 1 177 ? 6.435   -25.954 -12.392 1.00 30.01 ? 178 LYS   A CG  1 
ATOM   1416 C CD  . LYS   A 1 177 ? 5.010   -25.431 -12.367 1.00 37.09 ? 178 LYS   A CD  1 
ATOM   1417 C CE  . LYS   A 1 177 ? 4.947   -23.975 -12.798 1.00 39.74 ? 178 LYS   A CE  1 
ATOM   1418 N NZ  . LYS   A 1 177 ? 5.560   -23.786 -14.140 1.00 38.59 ? 178 LYS   A NZ  1 
ATOM   1419 N N   . THR   A 1 178 ? 7.395   -28.244 -8.384  1.00 19.51 ? 179 THR   A N   1 
ATOM   1420 C CA  . THR   A 1 178 ? 7.233   -29.412 -7.522  1.00 18.58 ? 179 THR   A CA  1 
ATOM   1421 C C   . THR   A 1 178 ? 7.573   -29.132 -6.062  1.00 18.29 ? 179 THR   A C   1 
ATOM   1422 O O   . THR   A 1 178 ? 6.735   -29.345 -5.178  1.00 20.28 ? 179 THR   A O   1 
ATOM   1423 C CB  . THR   A 1 178 ? 8.081   -30.580 -8.052  1.00 21.84 ? 179 THR   A CB  1 
ATOM   1424 O OG1 . THR   A 1 178 ? 7.805   -30.789 -9.449  1.00 24.21 ? 179 THR   A OG1 1 
ATOM   1425 C CG2 . THR   A 1 178 ? 7.749   -31.865 -7.285  1.00 20.12 ? 179 THR   A CG2 1 
ATOM   1426 N N   . ILE   A 1 179 ? 8.794   -28.680 -5.774  1.00 17.35 ? 180 ILE   A N   1 
ATOM   1427 C CA  . ILE   A 1 179 ? 9.253   -28.649 -4.389  1.00 17.97 ? 180 ILE   A CA  1 
ATOM   1428 C C   . ILE   A 1 179 ? 8.650   -27.468 -3.625  1.00 18.04 ? 180 ILE   A C   1 
ATOM   1429 O O   . ILE   A 1 179 ? 8.107   -27.645 -2.530  1.00 16.71 ? 180 ILE   A O   1 
ATOM   1430 C CB  . ILE   A 1 179 ? 10.794  -28.647 -4.342  1.00 18.13 ? 180 ILE   A CB  1 
ATOM   1431 C CG1 . ILE   A 1 179 ? 11.343  -29.935 -4.972  1.00 18.39 ? 180 ILE   A CG1 1 
ATOM   1432 C CG2 . ILE   A 1 179 ? 11.277  -28.515 -2.912  1.00 17.19 ? 180 ILE   A CG2 1 
ATOM   1433 C CD1 . ILE   A 1 179 ? 10.811  -31.235 -4.303  1.00 18.47 ? 180 ILE   A CD1 1 
ATOM   1434 N N   . PHE   A 1 180 ? 8.757   -26.244 -4.153  1.00 17.55 ? 181 PHE   A N   1 
ATOM   1435 C CA  . PHE   A 1 180 ? 8.150   -25.114 -3.453  1.00 20.37 ? 181 PHE   A CA  1 
ATOM   1436 C C   . PHE   A 1 180 ? 6.651   -25.308 -3.228  1.00 20.42 ? 181 PHE   A C   1 
ATOM   1437 O O   . PHE   A 1 180 ? 6.185   -25.037 -2.104  1.00 24.06 ? 181 PHE   A O   1 
ATOM   1438 C CB  . PHE   A 1 180 ? 8.400   -23.798 -4.209  1.00 17.48 ? 181 PHE   A CB  1 
ATOM   1439 C CG  . PHE   A 1 180 ? 9.840   -23.368 -4.284  1.00 18.18 ? 181 PHE   A CG  1 
ATOM   1440 C CD1 . PHE   A 1 180 ? 10.795  -23.828 -3.390  1.00 17.29 ? 181 PHE   A CD1 1 
ATOM   1441 C CD2 . PHE   A 1 180 ? 10.229  -22.473 -5.281  1.00 19.05 ? 181 PHE   A CD2 1 
ATOM   1442 C CE1 . PHE   A 1 180 ? 12.123  -23.396 -3.463  1.00 17.41 ? 181 PHE   A CE1 1 
ATOM   1443 C CE2 . PHE   A 1 180 ? 11.549  -22.029 -5.369  1.00 19.03 ? 181 PHE   A CE2 1 
ATOM   1444 C CZ  . PHE   A 1 180 ? 12.499  -22.507 -4.471  1.00 19.01 ? 181 PHE   A CZ  1 
ATOM   1445 N N   . PRO   A 1 181 ? 5.858   -25.770 -4.205  1.00 17.83 ? 182 PRO   A N   1 
ATOM   1446 C CA  . PRO   A 1 181 ? 4.434   -25.998 -3.919  1.00 20.82 ? 182 PRO   A CA  1 
ATOM   1447 C C   . PRO   A 1 181 ? 4.198   -27.081 -2.885  1.00 22.97 ? 182 PRO   A C   1 
ATOM   1448 O O   . PRO   A 1 181 ? 3.271   -26.958 -2.071  1.00 24.76 ? 182 PRO   A O   1 
ATOM   1449 C CB  . PRO   A 1 181 ? 3.866   -26.387 -5.290  1.00 21.70 ? 182 PRO   A CB  1 
ATOM   1450 C CG  . PRO   A 1 181 ? 4.775   -25.741 -6.268  1.00 18.53 ? 182 PRO   A CG  1 
ATOM   1451 C CD  . PRO   A 1 181 ? 6.131   -25.863 -5.655  1.00 18.77 ? 182 PRO   A CD  1 
ATOM   1452 N N   . ALA   A 1 182 ? 4.999   -28.148 -2.902  1.00 19.22 ? 183 ALA   A N   1 
ATOM   1453 C CA  . ALA   A 1 182 ? 4.805   -29.212 -1.918  1.00 19.35 ? 183 ALA   A CA  1 
ATOM   1454 C C   . ALA   A 1 182 ? 5.046   -28.718 -0.496  1.00 22.71 ? 183 ALA   A C   1 
ATOM   1455 O O   . ALA   A 1 182 ? 4.423   -29.225 0.446   1.00 21.95 ? 183 ALA   A O   1 
ATOM   1456 C CB  . ALA   A 1 182 ? 5.721   -30.391 -2.225  1.00 19.73 ? 183 ALA   A CB  1 
ATOM   1457 N N   . LEU   A 1 183 ? 5.952   -27.748 -0.320  1.00 19.34 ? 184 LEU   A N   1 
ATOM   1458 C CA  . LEU   A 1 183 ? 6.282   -27.156 0.973   1.00 22.64 ? 184 LEU   A CA  1 
ATOM   1459 C C   . LEU   A 1 183 ? 5.355   -26.003 1.346   1.00 24.60 ? 184 LEU   A C   1 
ATOM   1460 O O   . LEU   A 1 183 ? 5.519   -25.413 2.418   1.00 27.42 ? 184 LEU   A O   1 
ATOM   1461 C CB  . LEU   A 1 183 ? 7.743   -26.673 0.976   1.00 23.07 ? 184 LEU   A CB  1 
ATOM   1462 C CG  . LEU   A 1 183 ? 8.850   -27.729 0.822   1.00 18.45 ? 184 LEU   A CG  1 
ATOM   1463 C CD1 . LEU   A 1 183 ? 10.190  -27.098 0.456   1.00 18.89 ? 184 LEU   A CD1 1 
ATOM   1464 C CD2 . LEU   A 1 183 ? 8.982   -28.563 2.115   1.00 20.41 ? 184 LEU   A CD2 1 
ATOM   1465 N N   . GLY   A 1 184 ? 4.410   -25.661 0.483   1.00 21.33 ? 185 GLY   A N   1 
ATOM   1466 C CA  . GLY   A 1 184 ? 3.481   -24.581 0.757   1.00 28.91 ? 185 GLY   A CA  1 
ATOM   1467 C C   . GLY   A 1 184 ? 4.050   -23.188 0.608   1.00 31.07 ? 185 GLY   A C   1 
ATOM   1468 O O   . GLY   A 1 184 ? 3.526   -22.248 1.214   1.00 31.59 ? 185 GLY   A O   1 
ATOM   1469 N N   . LEU   A 1 185 ? 5.094   -23.015 -0.198  1.00 22.59 ? 186 LEU   A N   1 
ATOM   1470 C CA  . LEU   A 1 185 ? 5.731   -21.713 -0.350  1.00 24.09 ? 186 LEU   A CA  1 
ATOM   1471 C C   . LEU   A 1 185 ? 5.070   -20.955 -1.491  1.00 26.23 ? 186 LEU   A C   1 
ATOM   1472 O O   . LEU   A 1 185 ? 4.786   -21.523 -2.548  1.00 32.39 ? 186 LEU   A O   1 
ATOM   1473 C CB  . LEU   A 1 185 ? 7.227   -21.857 -0.628  1.00 21.21 ? 186 LEU   A CB  1 
ATOM   1474 C CG  . LEU   A 1 185 ? 8.010   -22.757 0.324   1.00 23.50 ? 186 LEU   A CG  1 
ATOM   1475 C CD1 . LEU   A 1 185 ? 9.493   -22.661 0.022   1.00 25.17 ? 186 LEU   A CD1 1 
ATOM   1476 C CD2 . LEU   A 1 185 ? 7.719   -22.420 1.786   1.00 24.98 ? 186 LEU   A CD2 1 
ATOM   1477 N N   . LYS   A 1 186 ? 4.834   -19.666 -1.272  1.00 24.58 ? 187 LYS   A N   1 
ATOM   1478 C CA  . LYS   A 1 186 ? 4.075   -18.848 -2.208  1.00 27.26 ? 187 LYS   A CA  1 
ATOM   1479 C C   . LYS   A 1 186 ? 4.915   -17.858 -2.991  1.00 26.73 ? 187 LYS   A C   1 
ATOM   1480 O O   . LYS   A 1 186 ? 4.510   -17.450 -4.083  1.00 24.56 ? 187 LYS   A O   1 
ATOM   1481 C CB  . LYS   A 1 186 ? 2.986   -18.072 -1.457  1.00 33.62 ? 187 LYS   A CB  1 
ATOM   1482 C CG  . LYS   A 1 186 ? 1.969   -18.970 -0.779  1.00 40.58 ? 187 LYS   A CG  1 
ATOM   1483 C CD  . LYS   A 1 186 ? 1.381   -19.961 -1.777  1.00 41.68 ? 187 LYS   A CD  1 
ATOM   1484 C CE  . LYS   A 1 186 ? 0.161   -20.675 -1.206  1.00 46.98 ? 187 LYS   A CE  1 
ATOM   1485 N NZ  . LYS   A 1 186 ? -0.567  -21.442 -2.258  1.00 52.74 ? 187 LYS   A NZ  1 
ATOM   1486 N N   . HIS   A 1 187 ? 6.061   -17.452 -2.455  1.00 21.63 ? 188 HIS   A N   1 
ATOM   1487 C CA  . HIS   A 1 187 ? 6.867   -16.393 -3.048  1.00 21.74 ? 188 HIS   A CA  1 
ATOM   1488 C C   . HIS   A 1 187 ? 8.340   -16.761 -2.925  1.00 24.91 ? 188 HIS   A C   1 
ATOM   1489 O O   . HIS   A 1 187 ? 9.186   -15.955 -2.532  1.00 21.78 ? 188 HIS   A O   1 
ATOM   1490 C CB  . HIS   A 1 187 ? 6.541   -15.044 -2.404  1.00 24.65 ? 188 HIS   A CB  1 
ATOM   1491 C CG  . HIS   A 1 187 ? 5.121   -14.608 -2.615  1.00 29.57 ? 188 HIS   A CG  1 
ATOM   1492 N ND1 . HIS   A 1 187 ? 4.675   -14.089 -3.811  1.00 32.58 ? 188 HIS   A ND1 1 
ATOM   1493 C CD2 . HIS   A 1 187 ? 4.049   -14.624 -1.787  1.00 30.74 ? 188 HIS   A CD2 1 
ATOM   1494 C CE1 . HIS   A 1 187 ? 3.389   -13.797 -3.709  1.00 29.49 ? 188 HIS   A CE1 1 
ATOM   1495 N NE2 . HIS   A 1 187 ? 2.985   -14.111 -2.491  1.00 32.41 ? 188 HIS   A NE2 1 
ATOM   1496 N N   . SER   A 1 188 ? 8.642   -18.014 -3.249  1.00 21.82 ? 189 SER   A N   1 
ATOM   1497 C CA  . SER   A 1 188 ? 10.006  -18.502 -3.373  1.00 18.60 ? 189 SER   A CA  1 
ATOM   1498 C C   . SER   A 1 188 ? 10.282  -18.787 -4.844  1.00 20.10 ? 189 SER   A C   1 
ATOM   1499 O O   . SER   A 1 188 ? 9.434   -19.348 -5.544  1.00 21.78 ? 189 SER   A O   1 
ATOM   1500 C CB  . SER   A 1 188 ? 10.210  -19.752 -2.514  1.00 18.55 ? 189 SER   A CB  1 
ATOM   1501 O OG  . SER   A 1 188 ? 9.928   -19.431 -1.155  1.00 19.45 ? 189 SER   A OG  1 
ATOM   1502 N N   . TYR   A 1 189 ? 11.462  -18.390 -5.311  1.00 19.28 ? 190 TYR   A N   1 
ATOM   1503 C CA  . TYR   A 1 189 ? 11.738  -18.355 -6.740  1.00 19.64 ? 190 TYR   A CA  1 
ATOM   1504 C C   . TYR   A 1 189 ? 13.173  -18.744 -7.038  1.00 18.90 ? 190 TYR   A C   1 
ATOM   1505 O O   . TYR   A 1 189 ? 14.091  -18.454 -6.264  1.00 20.31 ? 190 TYR   A O   1 
ATOM   1506 C CB  . TYR   A 1 189 ? 11.527  -16.957 -7.329  1.00 18.68 ? 190 TYR   A CB  1 
ATOM   1507 C CG  . TYR   A 1 189 ? 10.172  -16.391 -7.057  1.00 19.53 ? 190 TYR   A CG  1 
ATOM   1508 C CD1 . TYR   A 1 189 ? 9.090   -16.743 -7.854  1.00 23.10 ? 190 TYR   A CD1 1 
ATOM   1509 C CD2 . TYR   A 1 189 ? 9.967   -15.517 -6.001  1.00 21.74 ? 190 TYR   A CD2 1 
ATOM   1510 C CE1 . TYR   A 1 189 ? 7.835   -16.243 -7.607  1.00 23.17 ? 190 TYR   A CE1 1 
ATOM   1511 C CE2 . TYR   A 1 189 ? 8.704   -14.989 -5.756  1.00 22.61 ? 190 TYR   A CE2 1 
ATOM   1512 C CZ  . TYR   A 1 189 ? 7.648   -15.367 -6.554  1.00 24.58 ? 190 TYR   A CZ  1 
ATOM   1513 O OH  . TYR   A 1 189 ? 6.388   -14.856 -6.323  1.00 27.64 ? 190 TYR   A OH  1 
ATOM   1514 N N   . VAL   A 1 190 ? 13.362  -19.376 -8.195  1.00 17.55 ? 191 VAL   A N   1 
ATOM   1515 C CA  . VAL   A 1 190 ? 14.675  -19.369 -8.828  1.00 18.94 ? 191 VAL   A CA  1 
ATOM   1516 C C   . VAL   A 1 190 ? 14.808  -18.164 -9.746  1.00 20.08 ? 191 VAL   A C   1 
ATOM   1517 O O   . VAL   A 1 190 ? 15.844  -17.496 -9.757  1.00 21.84 ? 191 VAL   A O   1 
ATOM   1518 C CB  . VAL   A 1 190 ? 14.917  -20.695 -9.580  1.00 16.27 ? 191 VAL   A CB  1 
ATOM   1519 C CG1 . VAL   A 1 190 ? 16.205  -20.639 -10.391 1.00 18.68 ? 191 VAL   A CG1 1 
ATOM   1520 C CG2 . VAL   A 1 190 ? 14.983  -21.842 -8.561  1.00 19.11 ? 191 VAL   A CG2 1 
ATOM   1521 N N   . ASN   A 1 191 ? 13.745  -17.861 -10.487 1.00 19.79 ? 192 ASN   A N   1 
ATOM   1522 C CA  . ASN   A 1 191 ? 13.656  -16.661 -11.311 1.00 20.53 ? 192 ASN   A CA  1 
ATOM   1523 C C   . ASN   A 1 191 ? 12.500  -15.812 -10.793 1.00 22.25 ? 192 ASN   A C   1 
ATOM   1524 O O   . ASN   A 1 191 ? 11.349  -16.249 -10.818 1.00 24.72 ? 192 ASN   A O   1 
ATOM   1525 C CB  . ASN   A 1 191 ? 13.458  -17.045 -12.778 1.00 22.45 ? 192 ASN   A CB  1 
ATOM   1526 C CG  . ASN   A 1 191 ? 14.590  -17.915 -13.301 1.00 24.41 ? 192 ASN   A CG  1 
ATOM   1527 O OD1 . ASN   A 1 191 ? 14.397  -19.099 -13.598 1.00 27.71 ? 192 ASN   A OD1 1 
ATOM   1528 N ND2 . ASN   A 1 191 ? 15.786  -17.345 -13.377 1.00 22.33 ? 192 ASN   A ND2 1 
ATOM   1529 N N   . VAL   A 1 192 ? 12.808  -14.618 -10.289 1.00 21.32 ? 193 VAL   A N   1 
ATOM   1530 C CA  . VAL   A 1 192 ? 11.776  -13.729 -9.749  1.00 20.74 ? 193 VAL   A CA  1 
ATOM   1531 C C   . VAL   A 1 192 ? 10.998  -13.141 -10.922 1.00 23.89 ? 193 VAL   A C   1 
ATOM   1532 O O   . VAL   A 1 192 ? 11.602  -12.507 -11.799 1.00 25.94 ? 193 VAL   A O   1 
ATOM   1533 C CB  . VAL   A 1 192 ? 12.394  -12.624 -8.874  1.00 23.03 ? 193 VAL   A CB  1 
ATOM   1534 C CG1 . VAL   A 1 192 ? 11.322  -11.680 -8.340  1.00 22.77 ? 193 VAL   A CG1 1 
ATOM   1535 C CG2 . VAL   A 1 192 ? 13.208  -13.233 -7.724  1.00 22.77 ? 193 VAL   A CG2 1 
ATOM   1536 N N   . PRO   A 1 193 ? 9.681   -13.326 -10.993 1.00 26.16 ? 194 PRO   A N   1 
ATOM   1537 C CA  . PRO   A 1 193 ? 8.924   -12.793 -12.131 1.00 27.02 ? 194 PRO   A CA  1 
ATOM   1538 C C   . PRO   A 1 193 ? 8.833   -11.273 -12.081 1.00 30.91 ? 194 PRO   A C   1 
ATOM   1539 O O   . PRO   A 1 193 ? 9.016   -10.639 -11.037 1.00 29.87 ? 194 PRO   A O   1 
ATOM   1540 C CB  . PRO   A 1 193 ? 7.544   -13.437 -11.971 1.00 28.12 ? 194 PRO   A CB  1 
ATOM   1541 C CG  . PRO   A 1 193 ? 7.401   -13.593 -10.510 1.00 29.45 ? 194 PRO   A CG  1 
ATOM   1542 C CD  . PRO   A 1 193 ? 8.792   -13.966 -10.005 1.00 24.85 ? 194 PRO   A CD  1 
ATOM   1543 N N   . LYS   A 1 194 ? 8.532   -10.688 -13.245 1.00 30.39 ? 195 LYS   A N   1 
ATOM   1544 C CA  . LYS   A 1 194 ? 8.419   -9.235  -13.326 1.00 29.84 ? 195 LYS   A CA  1 
ATOM   1545 C C   . LYS   A 1 194 ? 7.355   -8.693  -12.376 1.00 30.76 ? 195 LYS   A C   1 
ATOM   1546 O O   . LYS   A 1 194 ? 7.510   -7.589  -11.839 1.00 31.51 ? 195 LYS   A O   1 
ATOM   1547 C CB  . LYS   A 1 194 ? 8.107   -8.812  -14.765 1.00 31.83 ? 195 LYS   A CB  1 
ATOM   1548 C CG  . LYS   A 1 194 ? 8.570   -7.400  -15.091 1.00 46.46 ? 195 LYS   A CG  1 
ATOM   1549 C CD  . LYS   A 1 194 ? 10.092  -7.304  -15.039 1.00 46.25 ? 195 LYS   A CD  1 
ATOM   1550 C CE  . LYS   A 1 194 ? 10.546  -5.954  -14.488 1.00 49.07 ? 195 LYS   A CE  1 
ATOM   1551 N NZ  . LYS   A 1 194 ? 12.033  -5.824  -14.520 1.00 52.85 ? 195 LYS   A NZ  1 
ATOM   1552 N N   . THR   A 1 195 ? 6.273   -9.449  -12.159 1.00 29.97 ? 196 THR   A N   1 
ATOM   1553 C CA  . THR   A 1 195 ? 5.190   -9.042  -11.268 1.00 35.85 ? 196 THR   A CA  1 
ATOM   1554 C C   . THR   A 1 195 ? 5.625   -8.915  -9.812  1.00 34.60 ? 196 THR   A C   1 
ATOM   1555 O O   . THR   A 1 195 ? 4.876   -8.345  -9.009  1.00 32.20 ? 196 THR   A O   1 
ATOM   1556 C CB  . THR   A 1 195 ? 4.029   -10.040 -11.353 1.00 33.47 ? 196 THR   A CB  1 
ATOM   1557 O OG1 . THR   A 1 195 ? 4.541   -11.376 -11.205 1.00 37.64 ? 196 THR   A OG1 1 
ATOM   1558 C CG2 . THR   A 1 195 ? 3.290   -9.909  -12.688 1.00 40.68 ? 196 THR   A CG2 1 
ATOM   1559 N N   . GLN   A 1 196 ? 6.799   -9.433  -9.455  1.00 29.95 ? 197 GLN   A N   1 
ATOM   1560 C CA  . GLN   A 1 196 ? 7.329   -9.341  -8.101  1.00 29.76 ? 197 GLN   A CA  1 
ATOM   1561 C C   . GLN   A 1 196 ? 8.528   -8.411  -7.982  1.00 32.43 ? 197 GLN   A C   1 
ATOM   1562 O O   . GLN   A 1 196 ? 9.072   -8.273  -6.881  1.00 28.61 ? 197 GLN   A O   1 
ATOM   1563 C CB  . GLN   A 1 196 ? 7.734   -10.733 -7.591  1.00 23.13 ? 197 GLN   A CB  1 
ATOM   1564 C CG  . GLN   A 1 196 ? 6.556   -11.630 -7.236  1.00 27.49 ? 197 GLN   A CG  1 
ATOM   1565 C CD  . GLN   A 1 196 ? 5.750   -11.097 -6.060  1.00 28.96 ? 197 GLN   A CD  1 
ATOM   1566 O OE1 . GLN   A 1 196 ? 6.313   -10.658 -5.051  1.00 26.50 ? 197 GLN   A OE1 1 
ATOM   1567 N NE2 . GLN   A 1 196 ? 4.424   -11.123 -6.188  1.00 28.17 ? 197 GLN   A NE2 1 
ATOM   1568 N N   . MET   A 1 197 ? 8.968   -7.776  -9.076  1.00 31.79 ? 198 MET   A N   1 
ATOM   1569 C CA  . MET   A 1 197 ? 10.227  -7.033  -9.030  1.00 34.28 ? 198 MET   A CA  1 
ATOM   1570 C C   . MET   A 1 197 ? 10.186  -5.895  -8.014  1.00 31.13 ? 198 MET   A C   1 
ATOM   1571 O O   . MET   A 1 197 ? 11.219  -5.554  -7.428  1.00 31.52 ? 198 MET   A O   1 
ATOM   1572 C CB  . MET   A 1 197 ? 10.589  -6.498  -10.417 1.00 38.94 ? 198 MET   A CB  1 
ATOM   1573 C CG  . MET   A 1 197 ? 11.259  -7.536  -11.326 1.00 42.57 ? 198 MET   A CG  1 
ATOM   1574 S SD  . MET   A 1 197 ? 12.806  -8.242  -10.674 1.00 53.64 ? 198 MET   A SD  1 
ATOM   1575 C CE  . MET   A 1 197 ? 13.076  -9.610  -11.804 1.00 42.16 ? 198 MET   A CE  1 
ATOM   1576 N N   . GLN   A 1 198 ? 9.010   -5.321  -7.765  1.00 29.87 ? 199 GLN   A N   1 
ATOM   1577 C CA  . GLN   A 1 198 ? 8.893   -4.264  -6.770  1.00 31.22 ? 199 GLN   A CA  1 
ATOM   1578 C C   . GLN   A 1 198 ? 9.109   -4.775  -5.351  1.00 29.84 ? 199 GLN   A C   1 
ATOM   1579 O O   . GLN   A 1 198 ? 9.322   -3.963  -4.440  1.00 32.97 ? 199 GLN   A O   1 
ATOM   1580 C CB  . GLN   A 1 198 ? 7.521   -3.596  -6.877  1.00 35.22 ? 199 GLN   A CB  1 
ATOM   1581 C CG  . GLN   A 1 198 ? 6.351   -4.503  -6.484  1.00 39.71 ? 199 GLN   A CG  1 
ATOM   1582 C CD  . GLN   A 1 198 ? 5.967   -5.528  -7.552  1.00 41.40 ? 199 GLN   A CD  1 
ATOM   1583 O OE1 . GLN   A 1 198 ? 6.729   -5.806  -8.484  1.00 42.27 ? 199 GLN   A OE1 1 
ATOM   1584 N NE2 . GLN   A 1 198 ? 4.767   -6.087  -7.420  1.00 46.07 ? 199 GLN   A NE2 1 
ATOM   1585 N N   . ASN   A 1 199 ? 9.034   -6.091  -5.143  1.00 26.55 ? 200 ASN   A N   1 
ATOM   1586 C CA  . ASN   A 1 199 ? 9.286   -6.714  -3.850  1.00 26.37 ? 200 ASN   A CA  1 
ATOM   1587 C C   . ASN   A 1 199 ? 10.677  -7.310  -3.739  1.00 25.13 ? 200 ASN   A C   1 
ATOM   1588 O O   . ASN   A 1 199 ? 11.035  -7.803  -2.669  1.00 23.03 ? 200 ASN   A O   1 
ATOM   1589 C CB  . ASN   A 1 199 ? 8.276   -7.827  -3.581  1.00 24.95 ? 200 ASN   A CB  1 
ATOM   1590 C CG  . ASN   A 1 199 ? 6.876   -7.314  -3.487  1.00 29.67 ? 200 ASN   A CG  1 
ATOM   1591 O OD1 . ASN   A 1 199 ? 6.642   -6.236  -2.939  1.00 29.09 ? 200 ASN   A OD1 1 
ATOM   1592 N ND2 . ASN   A 1 199 ? 5.926   -8.070  -4.032  1.00 29.62 ? 200 ASN   A ND2 1 
ATOM   1593 N N   . TYR   A 1 200 ? 11.448  -7.298  -4.817  1.00 24.38 ? 201 TYR   A N   1 
ATOM   1594 C CA  . TYR   A 1 200 ? 12.750  -7.947  -4.857  1.00 25.33 ? 201 TYR   A CA  1 
ATOM   1595 C C   . TYR   A 1 200 ? 13.786  -6.981  -4.295  1.00 26.20 ? 201 TYR   A C   1 
ATOM   1596 O O   . TYR   A 1 200 ? 14.081  -5.951  -4.909  1.00 27.57 ? 201 TYR   A O   1 
ATOM   1597 C CB  . TYR   A 1 200 ? 13.059  -8.351  -6.295  1.00 27.58 ? 201 TYR   A CB  1 
ATOM   1598 C CG  . TYR   A 1 200 ? 14.267  -9.230  -6.494  1.00 25.37 ? 201 TYR   A CG  1 
ATOM   1599 C CD1 . TYR   A 1 200 ? 15.068  -9.630  -5.426  1.00 28.04 ? 201 TYR   A CD1 1 
ATOM   1600 C CD2 . TYR   A 1 200 ? 14.614  -9.651  -7.759  1.00 30.14 ? 201 TYR   A CD2 1 
ATOM   1601 C CE1 . TYR   A 1 200 ? 16.183  -10.430 -5.634  1.00 28.72 ? 201 TYR   A CE1 1 
ATOM   1602 C CE2 . TYR   A 1 200 ? 15.708  -10.436 -7.975  1.00 30.20 ? 201 TYR   A CE2 1 
ATOM   1603 C CZ  . TYR   A 1 200 ? 16.493  -10.828 -6.915  1.00 30.05 ? 201 TYR   A CZ  1 
ATOM   1604 O OH  . TYR   A 1 200 ? 17.589  -11.614 -7.158  1.00 25.71 ? 201 TYR   A OH  1 
ATOM   1605 N N   . ALA   A 1 201 ? 14.340  -7.309  -3.125  1.00 22.25 ? 202 ALA   A N   1 
ATOM   1606 C CA  . ALA   A 1 201 ? 15.226  -6.375  -2.442  1.00 26.99 ? 202 ALA   A CA  1 
ATOM   1607 C C   . ALA   A 1 201 ? 16.498  -6.136  -3.252  1.00 27.67 ? 202 ALA   A C   1 
ATOM   1608 O O   . ALA   A 1 201 ? 16.973  -7.011  -3.972  1.00 27.19 ? 202 ALA   A O   1 
ATOM   1609 C CB  . ALA   A 1 201 ? 15.588  -6.902  -1.056  1.00 25.69 ? 202 ALA   A CB  1 
ATOM   1610 N N   . PHE   A 1 202 ? 17.043  -4.928  -3.141  1.00 31.70 ? 203 PHE   A N   1 
ATOM   1611 C CA  . PHE   A 1 202 ? 18.388  -4.681  -3.648  1.00 30.39 ? 203 PHE   A CA  1 
ATOM   1612 C C   . PHE   A 1 202 ? 19.401  -5.176  -2.627  1.00 31.46 ? 203 PHE   A C   1 
ATOM   1613 O O   . PHE   A 1 202 ? 19.185  -5.052  -1.417  1.00 32.51 ? 203 PHE   A O   1 
ATOM   1614 C CB  . PHE   A 1 202 ? 18.617  -3.193  -3.931  1.00 33.64 ? 203 PHE   A CB  1 
ATOM   1615 C CG  . PHE   A 1 202 ? 17.695  -2.615  -4.980  1.00 37.02 ? 203 PHE   A CG  1 
ATOM   1616 C CD1 . PHE   A 1 202 ? 17.050  -3.438  -5.893  1.00 43.16 ? 203 PHE   A CD1 1 
ATOM   1617 C CD2 . PHE   A 1 202 ? 17.481  -1.248  -5.048  1.00 43.67 ? 203 PHE   A CD2 1 
ATOM   1618 C CE1 . PHE   A 1 202 ? 16.201  -2.906  -6.852  1.00 45.13 ? 203 PHE   A CE1 1 
ATOM   1619 C CE2 . PHE   A 1 202 ? 16.632  -0.709  -6.006  1.00 46.94 ? 203 PHE   A CE2 1 
ATOM   1620 C CZ  . PHE   A 1 202 ? 15.994  -1.544  -6.908  1.00 46.87 ? 203 PHE   A CZ  1 
ATOM   1621 N N   . GLY   A 1 203 ? 20.492  -5.761  -3.119  1.00 29.03 ? 204 GLY   A N   1 
ATOM   1622 C CA  . GLY   A 1 203 ? 21.619  -6.141  -2.290  1.00 33.21 ? 204 GLY   A CA  1 
ATOM   1623 C C   . GLY   A 1 203 ? 22.714  -5.092  -2.345  1.00 36.15 ? 204 GLY   A C   1 
ATOM   1624 O O   . GLY   A 1 203 ? 22.901  -4.420  -3.358  1.00 36.94 ? 204 GLY   A O   1 
ATOM   1625 N N   . TYR   A 1 204 ? 23.447  -4.958  -1.241  1.00 32.13 ? 205 TYR   A N   1 
ATOM   1626 C CA  . TYR   A 1 204 ? 24.390  -3.863  -1.065  1.00 34.61 ? 205 TYR   A CA  1 
ATOM   1627 C C   . TYR   A 1 204 ? 25.776  -4.400  -0.743  1.00 40.11 ? 205 TYR   A C   1 
ATOM   1628 O O   . TYR   A 1 204 ? 25.931  -5.245  0.147   1.00 35.71 ? 205 TYR   A O   1 
ATOM   1629 C CB  . TYR   A 1 204 ? 23.894  -2.906  0.023   1.00 37.27 ? 205 TYR   A CB  1 
ATOM   1630 C CG  . TYR   A 1 204 ? 22.650  -2.170  -0.416  1.00 34.91 ? 205 TYR   A CG  1 
ATOM   1631 C CD1 . TYR   A 1 204 ? 21.386  -2.731  -0.243  1.00 31.02 ? 205 TYR   A CD1 1 
ATOM   1632 C CD2 . TYR   A 1 204 ? 22.743  -0.940  -1.046  1.00 38.63 ? 205 TYR   A CD2 1 
ATOM   1633 C CE1 . TYR   A 1 204 ? 20.247  -2.063  -0.665  1.00 32.09 ? 205 TYR   A CE1 1 
ATOM   1634 C CE2 . TYR   A 1 204 ? 21.618  -0.270  -1.468  1.00 37.76 ? 205 TYR   A CE2 1 
ATOM   1635 C CZ  . TYR   A 1 204 ? 20.376  -0.835  -1.280  1.00 33.81 ? 205 TYR   A CZ  1 
ATOM   1636 O OH  . TYR   A 1 204 ? 19.259  -0.153  -1.705  1.00 33.99 ? 205 TYR   A OH  1 
ATOM   1637 N N   . ASN   A 1 205 ? 26.777  -3.917  -1.479  1.00 46.36 ? 206 ASN   A N   1 
ATOM   1638 C CA  . ASN   A 1 205 ? 28.152  -4.375  -1.319  1.00 52.08 ? 206 ASN   A CA  1 
ATOM   1639 C C   . ASN   A 1 205 ? 28.788  -3.664  -0.125  1.00 55.90 ? 206 ASN   A C   1 
ATOM   1640 O O   . ASN   A 1 205 ? 28.119  -2.976  0.652   1.00 55.51 ? 206 ASN   A O   1 
ATOM   1641 C CB  . ASN   A 1 205 ? 28.940  -4.160  -2.612  1.00 53.72 ? 206 ASN   A CB  1 
ATOM   1642 C CG  . ASN   A 1 205 ? 28.970  -2.702  -3.054  1.00 60.18 ? 206 ASN   A CG  1 
ATOM   1643 O OD1 . ASN   A 1 205 ? 28.637  -1.794  -2.288  1.00 60.00 ? 206 ASN   A OD1 1 
ATOM   1644 N ND2 . ASN   A 1 205 ? 29.382  -2.472  -4.298  1.00 60.49 ? 206 ASN   A ND2 1 
ATOM   1645 N N   . GLN   A 1 206 ? 30.106  -3.813  0.029   1.00 62.28 ? 207 GLN   A N   1 
ATOM   1646 C CA  . GLN   A 1 206 ? 30.787  -3.206  1.167   1.00 64.05 ? 207 GLN   A CA  1 
ATOM   1647 C C   . GLN   A 1 206 ? 30.873  -1.689  1.053   1.00 65.12 ? 207 GLN   A C   1 
ATOM   1648 O O   . GLN   A 1 206 ? 31.080  -1.014  2.067   1.00 62.45 ? 207 GLN   A O   1 
ATOM   1649 C CB  . GLN   A 1 206 ? 32.179  -3.820  1.330   1.00 67.47 ? 207 GLN   A CB  1 
ATOM   1650 C CG  . GLN   A 1 206 ? 32.137  -5.315  1.629   1.00 68.76 ? 207 GLN   A CG  1 
ATOM   1651 C CD  . GLN   A 1 206 ? 31.189  -5.658  2.775   1.00 69.58 ? 207 GLN   A CD  1 
ATOM   1652 O OE1 . GLN   A 1 206 ? 30.338  -6.546  2.654   1.00 58.47 ? 207 GLN   A OE1 1 
ATOM   1653 N NE2 . GLN   A 1 206 ? 31.332  -4.952  3.894   1.00 71.60 ? 207 GLN   A NE2 1 
ATOM   1654 N N   . GLU   A 1 207 ? 30.710  -1.139  -0.148  1.00 65.25 ? 208 GLU   A N   1 
ATOM   1655 C CA  . GLU   A 1 207 ? 30.608  0.300   -0.335  1.00 64.30 ? 208 GLU   A CA  1 
ATOM   1656 C C   . GLU   A 1 207 ? 29.162  0.783   -0.319  1.00 60.12 ? 208 GLU   A C   1 
ATOM   1657 O O   . GLU   A 1 207 ? 28.905  1.946   -0.649  1.00 62.13 ? 208 GLU   A O   1 
ATOM   1658 C CB  . GLU   A 1 207 ? 31.290  0.715   -1.644  1.00 66.90 ? 208 GLU   A CB  1 
ATOM   1659 C CG  . GLU   A 1 207 ? 32.634  0.044   -1.890  1.00 67.81 ? 208 GLU   A CG  1 
ATOM   1660 C CD  . GLU   A 1 207 ? 32.505  -1.231  -2.709  1.00 72.66 ? 208 GLU   A CD  1 
ATOM   1661 O OE1 . GLU   A 1 207 ? 31.591  -1.295  -3.560  1.00 71.59 ? 208 GLU   A OE1 1 
ATOM   1662 O OE2 . GLU   A 1 207 ? 33.310  -2.167  -2.499  1.00 69.43 ? 208 GLU   A OE2 1 
ATOM   1663 N N   . ASN   A 1 208 ? 28.220  -0.091  0.050   1.00 57.67 ? 209 ASN   A N   1 
ATOM   1664 C CA  . ASN   A 1 208 ? 26.798  0.245   0.166   1.00 54.58 ? 209 ASN   A CA  1 
ATOM   1665 C C   . ASN   A 1 208 ? 26.228  0.763   -1.154  1.00 52.14 ? 209 ASN   A C   1 
ATOM   1666 O O   . ASN   A 1 208 ? 25.477  1.743   -1.198  1.00 53.42 ? 209 ASN   A O   1 
ATOM   1667 C CB  . ASN   A 1 208 ? 26.557  1.238   1.304   1.00 55.19 ? 209 ASN   A CB  1 
ATOM   1668 C CG  . ASN   A 1 208 ? 26.328  0.544   2.633   1.00 51.24 ? 209 ASN   A CG  1 
ATOM   1669 O OD1 . ASN   A 1 208 ? 27.254  -0.016  3.222   1.00 51.65 ? 209 ASN   A OD1 1 
ATOM   1670 N ND2 . ASN   A 1 208 ? 25.087  0.570   3.108   1.00 48.65 ? 209 ASN   A ND2 1 
ATOM   1671 N N   . GLN   A 1 209 ? 26.586  0.081   -2.241  1.00 54.04 ? 210 GLN   A N   1 
ATOM   1672 C CA  . GLN   A 1 209 ? 26.032  0.333   -3.558  1.00 53.71 ? 210 GLN   A CA  1 
ATOM   1673 C C   . GLN   A 1 209 ? 25.224  -0.874  -4.017  1.00 52.93 ? 210 GLN   A C   1 
ATOM   1674 O O   . GLN   A 1 209 ? 25.602  -2.017  -3.732  1.00 51.92 ? 210 GLN   A O   1 
ATOM   1675 C CB  . GLN   A 1 209 ? 27.136  0.630   -4.585  1.00 57.99 ? 210 GLN   A CB  1 
ATOM   1676 C CG  . GLN   A 1 209 ? 28.001  1.835   -4.239  1.00 55.87 ? 210 GLN   A CG  1 
ATOM   1677 C CD  . GLN   A 1 209 ? 27.200  3.123   -4.104  1.00 60.52 ? 210 GLN   A CD  1 
ATOM   1678 O OE1 . GLN   A 1 209 ? 26.195  3.327   -4.790  1.00 58.43 ? 210 GLN   A OE1 1 
ATOM   1679 N NE2 . GLN   A 1 209 ? 27.647  4.002   -3.213  1.00 64.87 ? 210 GLN   A NE2 1 
ATOM   1680 N N   . PRO   A 1 210 ? 24.106  -0.658  -4.713  1.00 54.50 ? 211 PRO   A N   1 
ATOM   1681 C CA  . PRO   A 1 210 ? 23.294  -1.791  -5.182  1.00 54.14 ? 211 PRO   A CA  1 
ATOM   1682 C C   . PRO   A 1 210 ? 23.866  -2.393  -6.460  1.00 62.53 ? 211 PRO   A C   1 
ATOM   1683 O O   . PRO   A 1 210 ? 24.121  -1.687  -7.440  1.00 63.28 ? 211 PRO   A O   1 
ATOM   1684 C CB  . PRO   A 1 210 ? 21.917  -1.163  -5.427  1.00 51.17 ? 211 PRO   A CB  1 
ATOM   1685 C CG  . PRO   A 1 210 ? 22.224  0.261   -5.774  1.00 46.75 ? 211 PRO   A CG  1 
ATOM   1686 C CD  . PRO   A 1 210 ? 23.452  0.639   -4.971  1.00 50.05 ? 211 PRO   A CD  1 
ATOM   1687 N N   . ILE   A 1 211 ? 24.071  -3.707  -6.437  1.00 65.89 ? 212 ILE   A N   1 
ATOM   1688 C CA  . ILE   A 1 211 ? 24.496  -4.472  -7.601  1.00 73.52 ? 212 ILE   A CA  1 
ATOM   1689 C C   . ILE   A 1 211 ? 23.407  -5.491  -7.906  1.00 75.14 ? 212 ILE   A C   1 
ATOM   1690 O O   . ILE   A 1 211 ? 22.548  -5.774  -7.062  1.00 69.97 ? 212 ILE   A O   1 
ATOM   1691 C CB  . ILE   A 1 211 ? 25.858  -5.169  -7.368  1.00 73.73 ? 212 ILE   A CB  1 
ATOM   1692 C CG1 . ILE   A 1 211 ? 26.736  -4.331  -6.432  1.00 65.68 ? 212 ILE   A CG1 1 
ATOM   1693 C CG2 . ILE   A 1 211 ? 26.578  -5.410  -8.692  1.00 74.91 ? 212 ILE   A CG2 1 
ATOM   1694 C CD1 . ILE   A 1 211 ? 28.073  -4.968  -6.097  1.00 68.15 ? 212 ILE   A CD1 1 
ATOM   1695 N N   . ARG   A 1 212 ? 23.428  -6.019  -9.130  1.00 74.34 ? 213 ARG   A N   1 
ATOM   1696 C CA  . ARG   A 1 212 ? 22.608  -7.186  -9.476  1.00 75.75 ? 213 ARG   A CA  1 
ATOM   1697 C C   . ARG   A 1 212 ? 23.128  -7.840  -10.758 1.00 77.74 ? 213 ARG   A C   1 
ATOM   1698 O O   . ARG   A 1 212 ? 22.656  -7.542  -11.856 1.00 81.80 ? 213 ARG   A O   1 
ATOM   1699 C CB  . ARG   A 1 212 ? 21.130  -6.820  -9.635  1.00 73.52 ? 213 ARG   A CB  1 
ATOM   1700 C CG  . ARG   A 1 212 ? 20.225  -8.045  -9.845  1.00 72.34 ? 213 ARG   A CG  1 
ATOM   1701 C CD  . ARG   A 1 212 ? 18.740  -7.697  -9.891  1.00 65.15 ? 213 ARG   A CD  1 
ATOM   1702 N NE  . ARG   A 1 212 ? 18.195  -7.384  -8.574  1.00 55.98 ? 213 ARG   A NE  1 
ATOM   1703 C CZ  . ARG   A 1 212 ? 16.969  -6.922  -8.360  1.00 59.56 ? 213 ARG   A CZ  1 
ATOM   1704 N NH1 . ARG   A 1 212 ? 16.118  -6.729  -9.357  1.00 56.33 ? 213 ARG   A NH1 1 
ATOM   1705 N NH2 . ARG   A 1 212 ? 16.591  -6.638  -7.117  1.00 47.92 ? 213 ARG   A NH2 1 
ATOM   1706 N N   . PRO   A 1 215 ? 24.531  -14.112 -12.480 1.00 49.88 ? 216 PRO   A N   1 
ATOM   1707 C CA  . PRO   A 1 215 ? 25.148  -15.248 -11.782 1.00 50.21 ? 216 PRO   A CA  1 
ATOM   1708 C C   . PRO   A 1 215 ? 25.960  -16.162 -12.712 1.00 51.09 ? 216 PRO   A C   1 
ATOM   1709 O O   . PRO   A 1 215 ? 25.827  -16.079 -13.934 1.00 45.69 ? 216 PRO   A O   1 
ATOM   1710 C CB  . PRO   A 1 215 ? 23.942  -15.997 -11.200 1.00 45.75 ? 216 PRO   A CB  1 
ATOM   1711 C CG  . PRO   A 1 215 ? 22.792  -15.605 -12.079 1.00 50.44 ? 216 PRO   A CG  1 
ATOM   1712 C CD  . PRO   A 1 215 ? 23.060  -14.177 -12.451 1.00 49.95 ? 216 PRO   A CD  1 
ATOM   1713 N N   . GLY   A 1 216 ? 26.795  -17.032 -12.122 1.00 44.32 ? 217 GLY   A N   1 
ATOM   1714 C CA  . GLY   A 1 216 ? 27.545  -17.987 -12.893 1.00 41.27 ? 217 GLY   A CA  1 
ATOM   1715 C C   . GLY   A 1 216 ? 26.668  -19.126 -13.394 1.00 38.91 ? 217 GLY   A C   1 
ATOM   1716 O O   . GLY   A 1 216 ? 25.455  -19.157 -13.154 1.00 36.97 ? 217 GLY   A O   1 
ATOM   1717 N N   . PRO   A 1 217 ? 27.273  -20.063 -14.123 1.00 33.50 ? 218 PRO   A N   1 
ATOM   1718 C CA  . PRO   A 1 217 ? 26.504  -21.185 -14.671 1.00 25.78 ? 218 PRO   A CA  1 
ATOM   1719 C C   . PRO   A 1 217 ? 26.355  -22.311 -13.660 1.00 25.81 ? 218 PRO   A C   1 
ATOM   1720 O O   . PRO   A 1 217 ? 27.208  -22.516 -12.794 1.00 27.45 ? 218 PRO   A O   1 
ATOM   1721 C CB  . PRO   A 1 217 ? 27.347  -21.629 -15.874 1.00 25.97 ? 218 PRO   A CB  1 
ATOM   1722 C CG  . PRO   A 1 217 ? 28.749  -21.322 -15.445 1.00 26.40 ? 218 PRO   A CG  1 
ATOM   1723 C CD  . PRO   A 1 217 ? 28.660  -20.043 -14.626 1.00 29.74 ? 218 PRO   A CD  1 
ATOM   1724 N N   . LEU   A 1 218 ? 25.241  -23.041 -13.784 1.00 26.07 ? 219 LEU   A N   1 
ATOM   1725 C CA  . LEU   A 1 218 ? 24.871  -24.088 -12.829 1.00 23.04 ? 219 LEU   A CA  1 
ATOM   1726 C C   . LEU   A 1 218 ? 24.771  -23.523 -11.411 1.00 19.69 ? 219 LEU   A C   1 
ATOM   1727 O O   . LEU   A 1 218 ? 25.017  -24.215 -10.408 1.00 21.46 ? 219 LEU   A O   1 
ATOM   1728 C CB  . LEU   A 1 218 ? 25.855  -25.264 -12.904 1.00 23.75 ? 219 LEU   A CB  1 
ATOM   1729 C CG  . LEU   A 1 218 ? 25.393  -26.595 -12.328 1.00 22.36 ? 219 LEU   A CG  1 
ATOM   1730 C CD1 . LEU   A 1 218 ? 23.916  -26.782 -12.561 1.00 26.06 ? 219 LEU   A CD1 1 
ATOM   1731 C CD2 . LEU   A 1 218 ? 26.166  -27.766 -12.918 1.00 24.23 ? 219 LEU   A CD2 1 
ATOM   1732 N N   . GLY   A 1 219 ? 24.425  -22.238 -11.312 1.00 19.40 ? 220 GLY   A N   1 
ATOM   1733 C CA  . GLY   A 1 219 ? 24.416  -21.591 -10.012 1.00 18.59 ? 220 GLY   A CA  1 
ATOM   1734 C C   . GLY   A 1 219 ? 23.180  -21.857 -9.183  1.00 18.95 ? 220 GLY   A C   1 
ATOM   1735 O O   . GLY   A 1 219 ? 23.250  -21.847 -7.949  1.00 16.43 ? 220 GLY   A O   1 
ATOM   1736 N N   . ALA   A 1 220 ? 22.035  -22.097 -9.828  1.00 18.08 ? 221 ALA   A N   1 
ATOM   1737 C CA  . ALA   A 1 220 ? 20.791  -22.190 -9.055  1.00 16.74 ? 221 ALA   A CA  1 
ATOM   1738 C C   . ALA   A 1 220 ? 20.847  -23.207 -7.919  1.00 17.35 ? 221 ALA   A C   1 
ATOM   1739 O O   . ALA   A 1 220 ? 20.439  -22.860 -6.799  1.00 16.17 ? 221 ALA   A O   1 
ATOM   1740 C CB  . ALA   A 1 220 ? 19.613  -22.476 -10.000 1.00 18.56 ? 221 ALA   A CB  1 
ATOM   1741 N N   . PRO   A 1 221 ? 21.320  -24.451 -8.112  1.00 15.85 ? 222 PRO   A N   1 
ATOM   1742 C CA  . PRO   A 1 221 ? 21.302  -25.401 -6.990  1.00 14.91 ? 222 PRO   A CA  1 
ATOM   1743 C C   . PRO   A 1 221 ? 22.239  -25.018 -5.865  1.00 14.64 ? 222 PRO   A C   1 
ATOM   1744 O O   . PRO   A 1 221 ? 22.069  -25.502 -4.737  1.00 16.29 ? 222 PRO   A O   1 
ATOM   1745 C CB  . PRO   A 1 221 ? 21.740  -26.732 -7.634  1.00 15.19 ? 222 PRO   A CB  1 
ATOM   1746 C CG  . PRO   A 1 221 ? 21.548  -26.555 -9.088  1.00 16.61 ? 222 PRO   A CG  1 
ATOM   1747 C CD  . PRO   A 1 221 ? 21.801  -25.089 -9.350  1.00 17.49 ? 222 PRO   A CD  1 
ATOM   1748 N N   . ALA   A 1 222 ? 23.225  -24.163 -6.145  1.00 15.50 ? 223 ALA   A N   1 
ATOM   1749 C CA  . ALA   A 1 222 ? 24.224  -23.812 -5.143  1.00 13.85 ? 223 ALA   A CA  1 
ATOM   1750 C C   . ALA   A 1 222 ? 23.873  -22.529 -4.394  1.00 16.16 ? 223 ALA   A C   1 
ATOM   1751 O O   . ALA   A 1 222 ? 24.130  -22.433 -3.183  1.00 15.96 ? 223 ALA   A O   1 
ATOM   1752 C CB  . ALA   A 1 222 ? 25.600  -23.657 -5.806  1.00 16.59 ? 223 ALA   A CB  1 
ATOM   1753 N N   . TYR   A 1 223 ? 23.300  -21.535 -5.086  1.00 15.89 ? 224 TYR   A N   1 
ATOM   1754 C CA  . TYR   A 1 223 ? 23.106  -20.234 -4.445  1.00 17.01 ? 224 TYR   A CA  1 
ATOM   1755 C C   . TYR   A 1 223 ? 21.982  -19.418 -5.066  1.00 17.85 ? 224 TYR   A C   1 
ATOM   1756 O O   . TYR   A 1 223 ? 21.876  -18.221 -4.782  1.00 21.01 ? 224 TYR   A O   1 
ATOM   1757 C CB  . TYR   A 1 223 ? 24.421  -19.431 -4.468  1.00 19.60 ? 224 TYR   A CB  1 
ATOM   1758 C CG  . TYR   A 1 223 ? 25.011  -19.258 -5.860  1.00 20.73 ? 224 TYR   A CG  1 
ATOM   1759 C CD1 . TYR   A 1 223 ? 24.505  -18.303 -6.724  1.00 21.82 ? 224 TYR   A CD1 1 
ATOM   1760 C CD2 . TYR   A 1 223 ? 26.051  -20.068 -6.313  1.00 17.98 ? 224 TYR   A CD2 1 
ATOM   1761 C CE1 . TYR   A 1 223 ? 25.020  -18.133 -8.006  1.00 23.72 ? 224 TYR   A CE1 1 
ATOM   1762 C CE2 . TYR   A 1 223 ? 26.580  -19.902 -7.602  1.00 21.39 ? 224 TYR   A CE2 1 
ATOM   1763 C CZ  . TYR   A 1 223 ? 26.047  -18.937 -8.441  1.00 22.10 ? 224 TYR   A CZ  1 
ATOM   1764 O OH  . TYR   A 1 223 ? 26.531  -18.748 -9.717  1.00 28.74 ? 224 TYR   A OH  1 
ATOM   1765 N N   . GLY   A 1 224 ? 21.122  -20.031 -5.883  1.00 16.79 ? 225 GLY   A N   1 
ATOM   1766 C CA  . GLY   A 1 224 ? 20.211  -19.241 -6.710  1.00 17.86 ? 225 GLY   A CA  1 
ATOM   1767 C C   . GLY   A 1 224 ? 18.758  -19.072 -6.300  1.00 18.33 ? 225 GLY   A C   1 
ATOM   1768 O O   . GLY   A 1 224 ? 17.938  -18.645 -7.125  1.00 19.19 ? 225 GLY   A O   1 
ATOM   1769 N N   . VAL   A 1 225 ? 18.405  -19.357 -5.054  1.00 17.53 ? 226 VAL   A N   1 
ATOM   1770 C CA  . VAL   A 1 225 ? 17.014  -19.271 -4.614  1.00 18.18 ? 226 VAL   A CA  1 
ATOM   1771 C C   . VAL   A 1 225 ? 16.787  -17.935 -3.922  1.00 17.14 ? 226 VAL   A C   1 
ATOM   1772 O O   . VAL   A 1 225 ? 17.670  -17.435 -3.215  1.00 14.93 ? 226 VAL   A O   1 
ATOM   1773 C CB  . VAL   A 1 225 ? 16.649  -20.448 -3.688  1.00 17.67 ? 226 VAL   A CB  1 
ATOM   1774 C CG1 . VAL   A 1 225 ? 15.244  -20.279 -3.062  1.00 17.89 ? 226 VAL   A CG1 1 
ATOM   1775 C CG2 . VAL   A 1 225 ? 16.710  -21.759 -4.480  1.00 18.82 ? 226 VAL   A CG2 1 
ATOM   1776 N N   . LYS   A 1 226 ? 15.586  -17.379 -4.107  1.00 15.62 ? 227 LYS   A N   1 
ATOM   1777 C CA  . LYS   A 1 226 ? 15.118  -16.159 -3.456  1.00 16.09 ? 227 LYS   A CA  1 
ATOM   1778 C C   . LYS   A 1 226 ? 13.812  -16.448 -2.715  1.00 19.73 ? 227 LYS   A C   1 
ATOM   1779 O O   . LYS   A 1 226 ? 13.007  -17.271 -3.163  1.00 21.39 ? 227 LYS   A O   1 
ATOM   1780 C CB  . LYS   A 1 226 ? 14.916  -15.031 -4.507  1.00 18.61 ? 227 LYS   A CB  1 
ATOM   1781 C CG  . LYS   A 1 226 ? 16.180  -14.672 -5.328  1.00 19.89 ? 227 LYS   A CG  1 
ATOM   1782 C CD  . LYS   A 1 226 ? 16.353  -15.522 -6.591  1.00 22.05 ? 227 LYS   A CD  1 
ATOM   1783 C CE  . LYS   A 1 226 ? 17.684  -15.213 -7.261  1.00 25.68 ? 227 LYS   A CE  1 
ATOM   1784 N NZ  . LYS   A 1 226 ? 17.902  -15.927 -8.550  1.00 23.90 ? 227 LYS   A NZ  1 
ATOM   1785 N N   . SER   A 1 227 ? 13.599  -15.793 -1.568  1.00 18.00 ? 228 SER   A N   1 
ATOM   1786 C CA  . SER   A 1 227 ? 12.411  -16.106 -0.777  1.00 16.38 ? 228 SER   A CA  1 
ATOM   1787 C C   . SER   A 1 227 ? 12.078  -14.947 0.156   1.00 21.32 ? 228 SER   A C   1 
ATOM   1788 O O   . SER   A 1 227 ? 12.836  -13.985 0.292   1.00 19.08 ? 228 SER   A O   1 
ATOM   1789 C CB  . SER   A 1 227 ? 12.623  -17.417 -0.000  1.00 20.34 ? 228 SER   A CB  1 
ATOM   1790 O OG  . SER   A 1 227 ? 11.426  -17.888 0.599   1.00 20.97 ? 228 SER   A OG  1 
ATOM   1791 N N   . THR   A 1 228 ? 10.923  -15.055 0.802   1.00 19.63 ? 229 THR   A N   1 
ATOM   1792 C CA  . THR   A 1 228 ? 10.440  -14.071 1.768   1.00 18.96 ? 229 THR   A CA  1 
ATOM   1793 C C   . THR   A 1 228 ? 10.579  -14.633 3.179   1.00 20.06 ? 229 THR   A C   1 
ATOM   1794 O O   . THR   A 1 228 ? 10.783  -15.831 3.371   1.00 19.09 ? 229 THR   A O   1 
ATOM   1795 C CB  . THR   A 1 228 ? 8.978   -13.727 1.499   1.00 22.59 ? 229 THR   A CB  1 
ATOM   1796 O OG1 . THR   A 1 228 ? 8.206   -14.908 1.752   1.00 19.77 ? 229 THR   A OG1 1 
ATOM   1797 C CG2 . THR   A 1 228 ? 8.797   -13.255 0.041   1.00 19.22 ? 229 THR   A CG2 1 
ATOM   1798 N N   . LEU   A 1 229 ? 10.468  -13.761 4.183   1.00 19.10 ? 230 LEU   A N   1 
ATOM   1799 C CA  . LEU   A 1 229 ? 10.501  -14.262 5.555   1.00 18.28 ? 230 LEU   A CA  1 
ATOM   1800 C C   . LEU   A 1 229 ? 9.328   -15.190 5.866   1.00 19.76 ? 230 LEU   A C   1 
ATOM   1801 O O   . LEU   A 1 229 ? 9.562   -16.239 6.495   1.00 19.53 ? 230 LEU   A O   1 
ATOM   1802 C CB  . LEU   A 1 229 ? 10.561  -13.099 6.565   1.00 17.41 ? 230 LEU   A CB  1 
ATOM   1803 C CG  . LEU   A 1 229 ? 10.764  -13.599 8.012   1.00 18.85 ? 230 LEU   A CG  1 
ATOM   1804 C CD1 . LEU   A 1 229 ? 12.178  -14.119 8.215   1.00 20.42 ? 230 LEU   A CD1 1 
ATOM   1805 C CD2 . LEU   A 1 229 ? 10.439  -12.541 9.077   1.00 19.37 ? 230 LEU   A CD2 1 
ATOM   1806 N N   . PRO   A 1 230 ? 8.079   -14.890 5.479   1.00 20.89 ? 231 PRO   A N   1 
ATOM   1807 C CA  . PRO   A 1 230 ? 7.004   -15.863 5.733   1.00 19.60 ? 231 PRO   A CA  1 
ATOM   1808 C C   . PRO   A 1 230 ? 7.256   -17.219 5.090   1.00 20.45 ? 231 PRO   A C   1 
ATOM   1809 O O   . PRO   A 1 230 ? 6.952   -18.250 5.709   1.00 23.04 ? 231 PRO   A O   1 
ATOM   1810 C CB  . PRO   A 1 230 ? 5.759   -15.163 5.159   1.00 21.31 ? 231 PRO   A CB  1 
ATOM   1811 C CG  . PRO   A 1 230 ? 6.065   -13.715 5.307   1.00 23.92 ? 231 PRO   A CG  1 
ATOM   1812 C CD  . PRO   A 1 230 ? 7.537   -13.600 5.002   1.00 21.08 ? 231 PRO   A CD  1 
ATOM   1813 N N   . ASP   A 1 231 ? 7.787   -17.257 3.858   1.00 18.80 ? 232 ASP   A N   1 
ATOM   1814 C CA  . ASP   A 1 231 ? 8.076   -18.555 3.248   1.00 17.70 ? 232 ASP   A CA  1 
ATOM   1815 C C   . ASP   A 1 231 ? 9.183   -19.285 4.000   1.00 19.60 ? 232 ASP   A C   1 
ATOM   1816 O O   . ASP   A 1 231 ? 9.128   -20.510 4.157   1.00 17.33 ? 232 ASP   A O   1 
ATOM   1817 C CB  . ASP   A 1 231 ? 8.478   -18.405 1.782   1.00 17.37 ? 232 ASP   A CB  1 
ATOM   1818 C CG  . ASP   A 1 231 ? 7.279   -18.335 0.828   1.00 20.31 ? 232 ASP   A CG  1 
ATOM   1819 O OD1 . ASP   A 1 231 ? 6.124   -18.391 1.279   1.00 23.22 ? 232 ASP   A OD1 1 
ATOM   1820 O OD2 . ASP   A 1 231 ? 7.528   -18.214 -0.384  1.00 22.68 ? 232 ASP   A OD2 1 
ATOM   1821 N N   . MET   A 1 232 ? 10.217  -18.566 4.442   1.00 16.50 ? 233 MET   A N   1 
ATOM   1822 C CA  . MET   A 1 232 ? 11.285  -19.264 5.156   1.00 15.90 ? 233 MET   A CA  1 
ATOM   1823 C C   . MET   A 1 232 ? 10.809  -19.790 6.511   1.00 17.40 ? 233 MET   A C   1 
ATOM   1824 O O   . MET   A 1 232 ? 11.258  -20.858 6.950   1.00 16.76 ? 233 MET   A O   1 
ATOM   1825 C CB  . MET   A 1 232 ? 12.510  -18.355 5.288   1.00 17.69 ? 233 MET   A CB  1 
ATOM   1826 C CG  . MET   A 1 232 ? 13.222  -18.119 3.945   1.00 17.91 ? 233 MET   A CG  1 
ATOM   1827 S SD  . MET   A 1 232 ? 13.724  -19.631 3.106   1.00 19.59 ? 233 MET   A SD  1 
ATOM   1828 C CE  . MET   A 1 232 ? 15.102  -20.115 4.140   1.00 19.56 ? 233 MET   A CE  1 
ATOM   1829 N N   . LEU   A 1 233 ? 9.883   -19.091 7.174   1.00 17.96 ? 234 LEU   A N   1 
ATOM   1830 C CA  . LEU   A 1 233 ? 9.297   -19.660 8.385   1.00 17.35 ? 234 LEU   A CA  1 
ATOM   1831 C C   . LEU   A 1 233 ? 8.465   -20.897 8.068   1.00 19.33 ? 234 LEU   A C   1 
ATOM   1832 O O   . LEU   A 1 233 ? 8.464   -21.859 8.846   1.00 19.05 ? 234 LEU   A O   1 
ATOM   1833 C CB  . LEU   A 1 233 ? 8.446   -18.619 9.115   1.00 21.42 ? 234 LEU   A CB  1 
ATOM   1834 C CG  . LEU   A 1 233 ? 9.235   -17.486 9.776   1.00 21.18 ? 234 LEU   A CG  1 
ATOM   1835 C CD1 . LEU   A 1 233 ? 8.320   -16.338 10.190  1.00 24.06 ? 234 LEU   A CD1 1 
ATOM   1836 C CD2 . LEU   A 1 233 ? 10.020  -18.003 10.981  1.00 22.69 ? 234 LEU   A CD2 1 
ATOM   1837 N N   . SER   A 1 234 ? 7.745   -20.887 6.941   1.00 19.72 ? 235 SER   A N   1 
ATOM   1838 C CA  . SER   A 1 234 ? 7.028   -22.084 6.501   1.00 21.58 ? 235 SER   A CA  1 
ATOM   1839 C C   . SER   A 1 234 ? 7.989   -23.236 6.229   1.00 20.94 ? 235 SER   A C   1 
ATOM   1840 O O   . SER   A 1 234 ? 7.694   -24.392 6.550   1.00 20.24 ? 235 SER   A O   1 
ATOM   1841 C CB  . SER   A 1 234 ? 6.205   -21.794 5.239   1.00 23.63 ? 235 SER   A CB  1 
ATOM   1842 O OG  . SER   A 1 234 ? 5.153   -20.877 5.490   1.00 26.43 ? 235 SER   A OG  1 
ATOM   1843 N N   . PHE   A 1 235 ? 9.131   -22.941 5.608   1.00 18.88 ? 236 PHE   A N   1 
ATOM   1844 C CA  . PHE   A 1 235 ? 10.122  -23.982 5.371   1.00 17.39 ? 236 PHE   A CA  1 
ATOM   1845 C C   . PHE   A 1 235 ? 10.637  -24.546 6.689   1.00 17.43 ? 236 PHE   A C   1 
ATOM   1846 O O   . PHE   A 1 235 ? 10.797  -25.761 6.830   1.00 16.28 ? 236 PHE   A O   1 
ATOM   1847 C CB  . PHE   A 1 235 ? 11.270  -23.425 4.522   1.00 16.75 ? 236 PHE   A CB  1 
ATOM   1848 C CG  . PHE   A 1 235 ? 12.337  -24.439 4.191   1.00 17.38 ? 236 PHE   A CG  1 
ATOM   1849 C CD1 . PHE   A 1 235 ? 12.027  -25.602 3.486   1.00 14.96 ? 236 PHE   A CD1 1 
ATOM   1850 C CD2 . PHE   A 1 235 ? 13.647  -24.221 4.570   1.00 17.97 ? 236 PHE   A CD2 1 
ATOM   1851 C CE1 . PHE   A 1 235 ? 13.011  -26.532 3.173   1.00 17.42 ? 236 PHE   A CE1 1 
ATOM   1852 C CE2 . PHE   A 1 235 ? 14.636  -25.151 4.261   1.00 17.29 ? 236 PHE   A CE2 1 
ATOM   1853 C CZ  . PHE   A 1 235 ? 14.318  -26.297 3.568   1.00 18.63 ? 236 PHE   A CZ  1 
ATOM   1854 N N   . ILE   A 1 236 ? 10.886  -23.682 7.679   1.00 15.96 ? 237 ILE   A N   1 
ATOM   1855 C CA  . ILE   A 1 236 ? 11.298  -24.191 8.986   1.00 18.53 ? 237 ILE   A CA  1 
ATOM   1856 C C   . ILE   A 1 236 ? 10.184  -25.020 9.603   1.00 17.95 ? 237 ILE   A C   1 
ATOM   1857 O O   . ILE   A 1 236 ? 10.437  -26.061 10.221  1.00 17.37 ? 237 ILE   A O   1 
ATOM   1858 C CB  . ILE   A 1 236 ? 11.726  -23.045 9.922   1.00 21.11 ? 237 ILE   A CB  1 
ATOM   1859 C CG1 . ILE   A 1 236 ? 12.881  -22.289 9.304   1.00 19.55 ? 237 ILE   A CG1 1 
ATOM   1860 C CG2 . ILE   A 1 236 ? 12.170  -23.596 11.279  1.00 21.17 ? 237 ILE   A CG2 1 
ATOM   1861 C CD1 . ILE   A 1 236 ? 13.878  -23.224 8.687   1.00 26.76 ? 237 ILE   A CD1 1 
ATOM   1862 N N   . HIS   A 1 237 ? 8.937   -24.569 9.462   1.00 17.51 ? 238 HIS   A N   1 
ATOM   1863 C CA  . HIS   A 1 237 ? 7.824   -25.360 9.986   1.00 20.60 ? 238 HIS   A CA  1 
ATOM   1864 C C   . HIS   A 1 237 ? 7.829   -26.764 9.395   1.00 21.60 ? 238 HIS   A C   1 
ATOM   1865 O O   . HIS   A 1 237 ? 7.633   -27.746 10.124  1.00 20.44 ? 238 HIS   A O   1 
ATOM   1866 C CB  . HIS   A 1 237 ? 6.488   -24.667 9.697   1.00 21.84 ? 238 HIS   A CB  1 
ATOM   1867 C CG  . HIS   A 1 237 ? 5.282   -25.490 10.058  1.00 26.42 ? 238 HIS   A CG  1 
ATOM   1868 N ND1 . HIS   A 1 237 ? 4.663   -26.336 9.160   1.00 26.37 ? 238 HIS   A ND1 1 
ATOM   1869 C CD2 . HIS   A 1 237 ? 4.583   -25.594 11.214  1.00 30.06 ? 238 HIS   A CD2 1 
ATOM   1870 C CE1 . HIS   A 1 237 ? 3.636   -26.926 9.749   1.00 31.71 ? 238 HIS   A CE1 1 
ATOM   1871 N NE2 . HIS   A 1 237 ? 3.567   -26.495 10.995  1.00 33.08 ? 238 HIS   A NE2 1 
ATOM   1872 N N   . ALA   A 1 238 ? 8.083   -26.876 8.083   1.00 17.69 ? 239 ALA   A N   1 
ATOM   1873 C CA  . ALA   A 1 238 ? 8.106   -28.183 7.432   1.00 17.72 ? 239 ALA   A CA  1 
ATOM   1874 C C   . ALA   A 1 238 ? 9.218   -29.053 7.996   1.00 18.38 ? 239 ALA   A C   1 
ATOM   1875 O O   . ALA   A 1 238 ? 9.054   -30.268 8.154   1.00 17.96 ? 239 ALA   A O   1 
ATOM   1876 C CB  . ALA   A 1 238 ? 8.280   -28.021 5.923   1.00 16.59 ? 239 ALA   A CB  1 
ATOM   1877 N N   . ASN   A 1 239 ? 10.366  -28.446 8.291   1.00 16.30 ? 240 ASN   A N   1 
ATOM   1878 C CA  . ASN   A 1 239 ? 11.484  -29.204 8.844   1.00 16.08 ? 240 ASN   A CA  1 
ATOM   1879 C C   . ASN   A 1 239 ? 11.240  -29.622 10.294  1.00 15.18 ? 240 ASN   A C   1 
ATOM   1880 O O   . ASN   A 1 239 ? 11.754  -30.660 10.727  1.00 17.63 ? 240 ASN   A O   1 
ATOM   1881 C CB  . ASN   A 1 239 ? 12.765  -28.371 8.718   1.00 12.93 ? 240 ASN   A CB  1 
ATOM   1882 C CG  . ASN   A 1 239 ? 13.423  -28.528 7.349   1.00 14.13 ? 240 ASN   A CG  1 
ATOM   1883 O OD1 . ASN   A 1 239 ? 14.241  -29.428 7.144   1.00 19.75 ? 240 ASN   A OD1 1 
ATOM   1884 N ND2 . ASN   A 1 239 ? 13.042  -27.675 6.404   1.00 15.33 ? 240 ASN   A ND2 1 
ATOM   1885 N N   . LEU   A 1 240 ? 10.491  -28.822 11.057  1.00 16.22 ? 241 LEU   A N   1 
ATOM   1886 C CA  . LEU   A 1 240 ? 10.123  -29.184 12.421  1.00 18.13 ? 241 LEU   A CA  1 
ATOM   1887 C C   . LEU   A 1 240 ? 8.968   -30.174 12.487  1.00 19.57 ? 241 LEU   A C   1 
ATOM   1888 O O   . LEU   A 1 240 ? 8.849   -30.904 13.484  1.00 22.06 ? 241 LEU   A O   1 
ATOM   1889 C CB  . LEU   A 1 240 ? 9.760   -27.927 13.222  1.00 18.68 ? 241 LEU   A CB  1 
ATOM   1890 C CG  . LEU   A 1 240 ? 10.953  -27.043 13.618  1.00 18.97 ? 241 LEU   A CG  1 
ATOM   1891 C CD1 . LEU   A 1 240 ? 10.487  -25.639 14.040  1.00 21.01 ? 241 LEU   A CD1 1 
ATOM   1892 C CD2 . LEU   A 1 240 ? 11.764  -27.711 14.734  1.00 16.88 ? 241 LEU   A CD2 1 
ATOM   1893 N N   . ASN   A 1 241 ? 8.107   -30.218 11.464  1.00 19.63 ? 242 ASN   A N   1 
ATOM   1894 C CA  . ASN   A 1 241 ? 6.910   -31.063 11.493  1.00 21.90 ? 242 ASN   A CA  1 
ATOM   1895 C C   . ASN   A 1 241 ? 6.731   -31.831 10.188  1.00 21.15 ? 242 ASN   A C   1 
ATOM   1896 O O   . ASN   A 1 241 ? 5.662   -31.787 9.572   1.00 20.39 ? 242 ASN   A O   1 
ATOM   1897 C CB  . ASN   A 1 241 ? 5.676   -30.210 11.772  1.00 25.11 ? 242 ASN   A CB  1 
ATOM   1898 C CG  . ASN   A 1 241 ? 5.789   -29.404 13.046  1.00 31.41 ? 242 ASN   A CG  1 
ATOM   1899 O OD1 . ASN   A 1 241 ? 5.488   -29.901 14.135  1.00 35.02 ? 242 ASN   A OD1 1 
ATOM   1900 N ND2 . ASN   A 1 241 ? 6.217   -28.149 12.919  1.00 31.99 ? 242 ASN   A ND2 1 
ATOM   1901 N N   . PRO   A 1 242 ? 7.739   -32.576 9.741   1.00 18.03 ? 243 PRO   A N   1 
ATOM   1902 C CA  . PRO   A 1 242 ? 7.585   -33.290 8.467   1.00 19.33 ? 243 PRO   A CA  1 
ATOM   1903 C C   . PRO   A 1 242 ? 6.418   -34.260 8.467   1.00 20.80 ? 243 PRO   A C   1 
ATOM   1904 O O   . PRO   A 1 242 ? 5.838   -34.509 7.407   1.00 20.65 ? 243 PRO   A O   1 
ATOM   1905 C CB  . PRO   A 1 242 ? 8.937   -34.003 8.295   1.00 19.46 ? 243 PRO   A CB  1 
ATOM   1906 C CG  . PRO   A 1 242 ? 9.499   -34.091 9.664   1.00 22.67 ? 243 PRO   A CG  1 
ATOM   1907 C CD  . PRO   A 1 242 ? 9.035   -32.865 10.385  1.00 18.89 ? 243 PRO   A CD  1 
ATOM   1908 N N   . GLN   A 1 243 ? 6.034   -34.790 9.632   1.00 20.57 ? 244 GLN   A N   1 
ATOM   1909 C CA  . GLN   A 1 243 ? 4.930   -35.743 9.693   1.00 20.94 ? 244 GLN   A CA  1 
ATOM   1910 C C   . GLN   A 1 243 ? 3.586   -35.128 9.318   1.00 24.00 ? 244 GLN   A C   1 
ATOM   1911 O O   . GLN   A 1 243 ? 2.651   -35.875 9.009   1.00 24.36 ? 244 GLN   A O   1 
ATOM   1912 C CB  . GLN   A 1 243 ? 4.852   -36.363 11.092  1.00 25.50 ? 244 GLN   A CB  1 
ATOM   1913 C CG  . GLN   A 1 243 ? 4.344   -35.435 12.195  1.00 24.96 ? 244 GLN   A CG  1 
ATOM   1914 C CD  . GLN   A 1 243 ? 5.388   -34.443 12.714  1.00 26.34 ? 244 GLN   A CD  1 
ATOM   1915 O OE1 . GLN   A 1 243 ? 6.524   -34.388 12.242  1.00 24.20 ? 244 GLN   A OE1 1 
ATOM   1916 N NE2 . GLN   A 1 243 ? 4.989   -33.651 13.697  1.00 32.33 ? 244 GLN   A NE2 1 
ATOM   1917 N N   . LYS   A 1 244 ? 3.459   -33.796 9.342   1.00 20.77 ? 245 LYS   A N   1 
ATOM   1918 C CA  . LYS   A 1 244 ? 2.214   -33.133 8.959   1.00 22.61 ? 245 LYS   A CA  1 
ATOM   1919 C C   . LYS   A 1 244 ? 2.074   -32.948 7.451   1.00 25.33 ? 245 LYS   A C   1 
ATOM   1920 O O   . LYS   A 1 244 ? 1.012   -32.508 6.989   1.00 27.75 ? 245 LYS   A O   1 
ATOM   1921 C CB  . LYS   A 1 244 ? 2.102   -31.763 9.631   1.00 26.38 ? 245 LYS   A CB  1 
ATOM   1922 C CG  . LYS   A 1 244 ? 1.968   -31.788 11.148  1.00 30.90 ? 245 LYS   A CG  1 
ATOM   1923 C CD  . LYS   A 1 244 ? 1.835   -30.368 11.698  1.00 38.53 ? 245 LYS   A CD  1 
ATOM   1924 C CE  . LYS   A 1 244 ? 1.484   -30.373 13.178  1.00 41.35 ? 245 LYS   A CE  1 
ATOM   1925 N NZ  . LYS   A 1 244 ? 2.498   -31.115 13.978  1.00 38.06 ? 245 LYS   A NZ  1 
ATOM   1926 N N   . TYR   A 1 245 ? 3.086   -33.274 6.681   1.00 19.31 ? 246 TYR   A N   1 
ATOM   1927 C CA  . TYR   A 1 245 ? 3.077   -33.055 5.239   1.00 19.78 ? 246 TYR   A CA  1 
ATOM   1928 C C   . TYR   A 1 245 ? 2.847   -34.360 4.492   1.00 20.52 ? 246 TYR   A C   1 
ATOM   1929 O O   . TYR   A 1 245 ? 3.103   -35.441 5.023   1.00 21.84 ? 246 TYR   A O   1 
ATOM   1930 C CB  . TYR   A 1 245 ? 4.400   -32.420 4.801   1.00 17.92 ? 246 TYR   A CB  1 
ATOM   1931 C CG  . TYR   A 1 245 ? 4.521   -30.985 5.249   1.00 22.10 ? 246 TYR   A CG  1 
ATOM   1932 C CD1 . TYR   A 1 245 ? 4.697   -30.671 6.597   1.00 20.14 ? 246 TYR   A CD1 1 
ATOM   1933 C CD2 . TYR   A 1 245 ? 4.432   -29.936 4.332   1.00 20.79 ? 246 TYR   A CD2 1 
ATOM   1934 C CE1 . TYR   A 1 245 ? 4.799   -29.355 7.019   1.00 21.34 ? 246 TYR   A CE1 1 
ATOM   1935 C CE2 . TYR   A 1 245 ? 4.533   -28.621 4.748   1.00 22.44 ? 246 TYR   A CE2 1 
ATOM   1936 C CZ  . TYR   A 1 245 ? 4.711   -28.337 6.093   1.00 24.66 ? 246 TYR   A CZ  1 
ATOM   1937 O OH  . TYR   A 1 245 ? 4.816   -27.028 6.511   1.00 25.34 ? 246 TYR   A OH  1 
ATOM   1938 N N   . PRO   A 1 246 ? 2.335   -34.304 3.258   1.00 18.17 ? 247 PRO   A N   1 
ATOM   1939 C CA  . PRO   A 1 246 ? 2.111   -35.539 2.493   1.00 20.58 ? 247 PRO   A CA  1 
ATOM   1940 C C   . PRO   A 1 246 ? 3.396   -36.329 2.271   1.00 18.36 ? 247 PRO   A C   1 
ATOM   1941 O O   . PRO   A 1 246 ? 4.508   -35.795 2.322   1.00 20.22 ? 247 PRO   A O   1 
ATOM   1942 C CB  . PRO   A 1 246 ? 1.535   -35.030 1.160   1.00 21.88 ? 247 PRO   A CB  1 
ATOM   1943 C CG  . PRO   A 1 246 ? 0.874   -33.747 1.527   1.00 19.03 ? 247 PRO   A CG  1 
ATOM   1944 C CD  . PRO   A 1 246 ? 1.758   -33.125 2.577   1.00 20.56 ? 247 PRO   A CD  1 
ATOM   1945 N N   . ALA   A 1 247 ? 3.217   -37.627 2.000   1.00 20.21 ? 248 ALA   A N   1 
ATOM   1946 C CA  . ALA   A 1 247 ? 4.314   -38.588 2.095   1.00 21.35 ? 248 ALA   A CA  1 
ATOM   1947 C C   . ALA   A 1 247 ? 5.517   -38.205 1.240   1.00 19.50 ? 248 ALA   A C   1 
ATOM   1948 O O   . ALA   A 1 247 ? 6.663   -38.339 1.682   1.00 18.80 ? 248 ALA   A O   1 
ATOM   1949 C CB  . ALA   A 1 247 ? 3.815   -39.977 1.706   1.00 22.94 ? 248 ALA   A CB  1 
ATOM   1950 N N   . ASP   A 1 248 ? 5.293   -37.736 0.011   1.00 19.95 ? 249 ASP   A N   1 
ATOM   1951 C CA  . ASP   A 1 248 ? 6.435   -37.524 -0.879  1.00 20.25 ? 249 ASP   A CA  1 
ATOM   1952 C C   . ASP   A 1 248 ? 7.362   -36.419 -0.370  1.00 18.99 ? 249 ASP   A C   1 
ATOM   1953 O O   . ASP   A 1 248 ? 8.586   -36.588 -0.379  1.00 18.44 ? 249 ASP   A O   1 
ATOM   1954 C CB  . ASP   A 1 248 ? 5.961   -37.220 -2.304  1.00 21.70 ? 249 ASP   A CB  1 
ATOM   1955 C CG  . ASP   A 1 248 ? 5.344   -38.436 -3.003  1.00 24.90 ? 249 ASP   A CG  1 
ATOM   1956 O OD1 . ASP   A 1 248 ? 5.581   -39.587 -2.567  1.00 26.10 ? 249 ASP   A OD1 1 
ATOM   1957 O OD2 . ASP   A 1 248 ? 4.606   -38.249 -4.001  1.00 28.67 ? 249 ASP   A OD2 1 
ATOM   1958 N N   . ILE   A 1 249 ? 6.814   -35.285 0.081   1.00 17.45 ? 250 ILE   A N   1 
ATOM   1959 C CA  . ILE   A 1 249 ? 7.700   -34.239 0.592   1.00 15.35 ? 250 ILE   A CA  1 
ATOM   1960 C C   . ILE   A 1 249 ? 8.124   -34.545 2.030   1.00 16.00 ? 250 ILE   A C   1 
ATOM   1961 O O   . ILE   A 1 249 ? 9.216   -34.154 2.456   1.00 17.47 ? 250 ILE   A O   1 
ATOM   1962 C CB  . ILE   A 1 249 ? 7.032   -32.856 0.455   1.00 18.51 ? 250 ILE   A CB  1 
ATOM   1963 C CG1 . ILE   A 1 249 ? 8.046   -31.715 0.618   1.00 18.71 ? 250 ILE   A CG1 1 
ATOM   1964 C CG2 . ILE   A 1 249 ? 5.855   -32.697 1.426   1.00 20.27 ? 250 ILE   A CG2 1 
ATOM   1965 C CD1 . ILE   A 1 249 ? 9.042   -31.590 -0.542  1.00 17.76 ? 250 ILE   A CD1 1 
ATOM   1966 N N   . GLN   A 1 250 ? 7.285   -35.254 2.791   1.00 19.49 ? 251 GLN   A N   1 
ATOM   1967 C CA  A GLN   A 1 250 ? 7.688   -35.673 4.129   0.56 18.27 ? 251 GLN   A CA  1 
ATOM   1968 C CA  B GLN   A 1 250 ? 7.675   -35.698 4.129   0.44 18.29 ? 251 GLN   A CA  1 
ATOM   1969 C C   . GLN   A 1 250 ? 8.953   -36.520 4.071   1.00 18.03 ? 251 GLN   A C   1 
ATOM   1970 O O   . GLN   A 1 250 ? 9.908   -36.274 4.819   1.00 17.96 ? 251 GLN   A O   1 
ATOM   1971 C CB  A GLN   A 1 250 ? 6.545   -36.437 4.807   0.56 18.84 ? 251 GLN   A CB  1 
ATOM   1972 C CB  B GLN   A 1 250 ? 6.546   -36.527 4.754   0.44 18.85 ? 251 GLN   A CB  1 
ATOM   1973 C CG  A GLN   A 1 250 ? 6.955   -37.112 6.118   0.56 20.00 ? 251 GLN   A CG  1 
ATOM   1974 C CG  B GLN   A 1 250 ? 6.988   -37.373 5.961   0.44 20.04 ? 251 GLN   A CG  1 
ATOM   1975 C CD  A GLN   A 1 250 ? 5.783   -37.660 6.913   0.56 21.88 ? 251 GLN   A CD  1 
ATOM   1976 C CD  B GLN   A 1 250 ? 6.203   -38.674 6.124   0.44 23.07 ? 251 GLN   A CD  1 
ATOM   1977 O OE1 A GLN   A 1 250 ? 4.616   -37.442 6.574   0.56 23.34 ? 251 GLN   A OE1 1 
ATOM   1978 O OE1 B GLN   A 1 250 ? 5.654   -38.948 7.191   0.44 23.78 ? 251 GLN   A OE1 1 
ATOM   1979 N NE2 A GLN   A 1 250 ? 6.095   -38.388 7.981   0.56 23.29 ? 251 GLN   A NE2 1 
ATOM   1980 N NE2 B GLN   A 1 250 ? 6.178   -39.492 5.078   0.44 20.68 ? 251 GLN   A NE2 1 
ATOM   1981 N N   . ARG   A 1 251 ? 8.984   -37.504 3.170   1.00 17.48 ? 252 ARG   A N   1 
ATOM   1982 C CA  . ARG   A 1 251 ? 10.160  -38.359 3.040   1.00 15.59 ? 252 ARG   A CA  1 
ATOM   1983 C C   . ARG   A 1 251 ? 11.362  -37.561 2.563   1.00 18.62 ? 252 ARG   A C   1 
ATOM   1984 O O   . ARG   A 1 251 ? 12.481  -37.772 3.037   1.00 16.70 ? 252 ARG   A O   1 
ATOM   1985 C CB  . ARG   A 1 251 ? 9.858   -39.515 2.086   1.00 16.66 ? 252 ARG   A CB  1 
ATOM   1986 C CG  . ARG   A 1 251 ? 8.902   -40.583 2.679   1.00 17.93 ? 252 ARG   A CG  1 
ATOM   1987 C CD  . ARG   A 1 251 ? 8.161   -41.388 1.611   1.00 22.15 ? 252 ARG   A CD  1 
ATOM   1988 N NE  . ARG   A 1 251 ? 8.997   -42.064 0.627   1.00 32.54 ? 252 ARG   A NE  1 
ATOM   1989 C CZ  . ARG   A 1 251 ? 9.238   -43.369 0.620   1.00 31.99 ? 252 ARG   A CZ  1 
ATOM   1990 N NH1 . ARG   A 1 251 ? 8.836   -44.153 1.611   1.00 36.76 ? 252 ARG   A NH1 1 
ATOM   1991 N NH2 . ARG   A 1 251 ? 9.893   -43.904 -0.407  1.00 34.52 ? 252 ARG   A NH2 1 
ATOM   1992 N N   . ALA   A 1 252 ? 11.139  -36.624 1.639   1.00 16.33 ? 253 ALA   A N   1 
ATOM   1993 C CA  . ALA   A 1 252 ? 12.206  -35.726 1.191   1.00 14.35 ? 253 ALA   A CA  1 
ATOM   1994 C C   . ALA   A 1 252 ? 12.833  -34.967 2.355   1.00 16.01 ? 253 ALA   A C   1 
ATOM   1995 O O   . ALA   A 1 252 ? 14.066  -34.881 2.471   1.00 16.33 ? 253 ALA   A O   1 
ATOM   1996 C CB  . ALA   A 1 252 ? 11.638  -34.744 0.169   1.00 15.16 ? 253 ALA   A CB  1 
ATOM   1997 N N   . ILE   A 1 253 ? 11.996  -34.356 3.196   1.00 14.95 ? 254 ILE   A N   1 
ATOM   1998 C CA  . ILE   A 1 253 ? 12.505  -33.572 4.319   1.00 15.63 ? 254 ILE   A CA  1 
ATOM   1999 C C   . ILE   A 1 253 ? 13.287  -34.456 5.275   1.00 16.97 ? 254 ILE   A C   1 
ATOM   2000 O O   . ILE   A 1 253 ? 14.401  -34.114 5.688   1.00 15.41 ? 254 ILE   A O   1 
ATOM   2001 C CB  . ILE   A 1 253 ? 11.348  -32.867 5.038   1.00 17.21 ? 254 ILE   A CB  1 
ATOM   2002 C CG1 . ILE   A 1 253 ? 10.717  -31.827 4.117   1.00 16.07 ? 254 ILE   A CG1 1 
ATOM   2003 C CG2 . ILE   A 1 253 ? 11.850  -32.217 6.316   1.00 17.40 ? 254 ILE   A CG2 1 
ATOM   2004 C CD1 . ILE   A 1 253 ? 9.381   -31.365 4.591   1.00 18.89 ? 254 ILE   A CD1 1 
ATOM   2005 N N   . ASN   A 1 254 ? 12.714  -35.608 5.641   1.00 14.86 ? 255 ASN   A N   1 
ATOM   2006 C CA  . ASN   A 1 254 ? 13.395  -36.513 6.559   1.00 18.58 ? 255 ASN   A CA  1 
ATOM   2007 C C   . ASN   A 1 254 ? 14.752  -36.924 6.004   1.00 16.19 ? 255 ASN   A C   1 
ATOM   2008 O O   . ASN   A 1 254 ? 15.723  -37.078 6.757   1.00 16.98 ? 255 ASN   A O   1 
ATOM   2009 C CB  . ASN   A 1 254 ? 12.517  -37.737 6.835   1.00 17.55 ? 255 ASN   A CB  1 
ATOM   2010 C CG  . ASN   A 1 254 ? 11.425  -37.443 7.840   1.00 19.57 ? 255 ASN   A CG  1 
ATOM   2011 O OD1 . ASN   A 1 254 ? 11.611  -36.626 8.743   1.00 25.74 ? 255 ASN   A OD1 1 
ATOM   2012 N ND2 . ASN   A 1 254 ? 10.283  -38.097 7.694   1.00 23.54 ? 255 ASN   A ND2 1 
ATOM   2013 N N   . GLU   A 1 255 ? 14.840  -37.097 4.684   1.00 16.86 ? 256 GLU   A N   1 
ATOM   2014 C CA  . GLU   A 1 255 ? 16.106  -37.462 4.055   1.00 17.22 ? 256 GLU   A CA  1 
ATOM   2015 C C   . GLU   A 1 255 ? 17.175  -36.400 4.286   1.00 18.77 ? 256 GLU   A C   1 
ATOM   2016 O O   . GLU   A 1 255 ? 18.360  -36.734 4.411   1.00 16.96 ? 256 GLU   A O   1 
ATOM   2017 C CB  . GLU   A 1 255 ? 15.888  -37.704 2.555   1.00 18.40 ? 256 GLU   A CB  1 
ATOM   2018 C CG  . GLU   A 1 255 ? 16.979  -38.538 1.877   1.00 18.53 ? 256 GLU   A CG  1 
ATOM   2019 C CD  . GLU   A 1 255 ? 16.948  -40.017 2.265   1.00 19.64 ? 256 GLU   A CD  1 
ATOM   2020 O OE1 . GLU   A 1 255 ? 15.865  -40.651 2.223   1.00 21.59 ? 256 GLU   A OE1 1 
ATOM   2021 O OE2 . GLU   A 1 255 ? 18.022  -40.560 2.599   1.00 21.94 ? 256 GLU   A OE2 1 
ATOM   2022 N N   . THR   A 1 256 ? 16.792  -35.119 4.370   1.00 14.45 ? 257 THR   A N   1 
ATOM   2023 C CA  . THR   A 1 256 ? 17.810  -34.083 4.542   1.00 15.60 ? 257 THR   A CA  1 
ATOM   2024 C C   . THR   A 1 256 ? 18.296  -33.971 5.980   1.00 18.10 ? 257 THR   A C   1 
ATOM   2025 O O   . THR   A 1 256 ? 19.247  -33.229 6.243   1.00 18.65 ? 257 THR   A O   1 
ATOM   2026 C CB  . THR   A 1 256 ? 17.294  -32.712 4.100   1.00 19.39 ? 257 THR   A CB  1 
ATOM   2027 O OG1 . THR   A 1 256 ? 16.304  -32.239 5.033   1.00 17.00 ? 257 THR   A OG1 1 
ATOM   2028 C CG2 . THR   A 1 256 ? 16.733  -32.786 2.696   1.00 17.18 ? 257 THR   A CG2 1 
ATOM   2029 N N   . HIS   A 1 257 ? 17.666  -34.664 6.910   1.00 15.90 ? 258 HIS   A N   1 
ATOM   2030 C CA  . HIS   A 1 257 ? 18.073  -34.625 8.302   1.00 16.60 ? 258 HIS   A CA  1 
ATOM   2031 C C   . HIS   A 1 257 ? 19.040  -35.736 8.670   1.00 20.53 ? 258 HIS   A C   1 
ATOM   2032 O O   . HIS   A 1 257 ? 19.542  -35.734 9.796   1.00 21.22 ? 258 HIS   A O   1 
ATOM   2033 C CB  . HIS   A 1 257 ? 16.845  -34.710 9.207   1.00 18.25 ? 258 HIS   A CB  1 
ATOM   2034 C CG  . HIS   A 1 257 ? 15.911  -33.562 9.035   1.00 16.51 ? 258 HIS   A CG  1 
ATOM   2035 N ND1 . HIS   A 1 257 ? 14.665  -33.517 9.625   1.00 18.89 ? 258 HIS   A ND1 1 
ATOM   2036 C CD2 . HIS   A 1 257 ? 16.042  -32.414 8.330   1.00 17.02 ? 258 HIS   A CD2 1 
ATOM   2037 C CE1 . HIS   A 1 257 ? 14.075  -32.380 9.295   1.00 17.05 ? 258 HIS   A CE1 1 
ATOM   2038 N NE2 . HIS   A 1 257 ? 14.890  -31.691 8.515   1.00 16.32 ? 258 HIS   A NE2 1 
ATOM   2039 N N   . GLN   A 1 258 ? 19.292  -36.686 7.767   1.00 18.03 ? 259 GLN   A N   1 
ATOM   2040 C CA  . GLN   A 1 258 ? 20.124  -37.836 8.102   1.00 19.13 ? 259 GLN   A CA  1 
ATOM   2041 C C   . GLN   A 1 258 ? 21.603  -37.487 7.943   1.00 18.86 ? 259 GLN   A C   1 
ATOM   2042 O O   . GLN   A 1 258 ? 22.067  -37.195 6.834   1.00 17.21 ? 259 GLN   A O   1 
ATOM   2043 C CB  . GLN   A 1 258 ? 19.769  -39.039 7.233   1.00 20.37 ? 259 GLN   A CB  1 
ATOM   2044 C CG  . GLN   A 1 258 ? 20.579  -40.271 7.589   1.00 25.15 ? 259 GLN   A CG  1 
ATOM   2045 C CD  . GLN   A 1 258 ? 20.329  -41.424 6.639   1.00 33.03 ? 259 GLN   A CD  1 
ATOM   2046 O OE1 . GLN   A 1 258 ? 19.309  -41.459 5.945   1.00 37.75 ? 259 GLN   A OE1 1 
ATOM   2047 N NE2 . GLN   A 1 258 ? 21.266  -42.370 6.589   1.00 35.31 ? 259 GLN   A NE2 1 
ATOM   2048 N N   . GLY   A 1 259 ? 22.333  -37.523 9.052   1.00 19.60 ? 260 GLY   A N   1 
ATOM   2049 C CA  . GLY   A 1 259 ? 23.775  -37.336 8.983   1.00 19.73 ? 260 GLY   A CA  1 
ATOM   2050 C C   . GLY   A 1 259 ? 24.431  -38.432 8.163   1.00 18.18 ? 260 GLY   A C   1 
ATOM   2051 O O   . GLY   A 1 259 ? 24.083  -39.614 8.264   1.00 19.38 ? 260 GLY   A O   1 
ATOM   2052 N N   . ARG   A 1 260 ? 25.393  -38.025 7.337   1.00 14.36 ? 261 ARG   A N   1 
ATOM   2053 C CA  . ARG   A 1 260 ? 26.047  -38.932 6.408   1.00 15.70 ? 261 ARG   A CA  1 
ATOM   2054 C C   . ARG   A 1 260 ? 27.486  -39.240 6.786   1.00 17.67 ? 261 ARG   A C   1 
ATOM   2055 O O   . ARG   A 1 260 ? 27.987  -40.325 6.456   1.00 20.25 ? 261 ARG   A O   1 
ATOM   2056 C CB  . ARG   A 1 260 ? 25.998  -38.340 4.995   1.00 15.63 ? 261 ARG   A CB  1 
ATOM   2057 C CG  . ARG   A 1 260 ? 24.572  -37.912 4.585   1.00 15.43 ? 261 ARG   A CG  1 
ATOM   2058 C CD  . ARG   A 1 260 ? 23.637  -39.120 4.501   1.00 15.32 ? 261 ARG   A CD  1 
ATOM   2059 N NE  . ARG   A 1 260 ? 22.273  -38.702 4.168   1.00 14.42 ? 261 ARG   A NE  1 
ATOM   2060 C CZ  . ARG   A 1 260 ? 21.370  -39.484 3.585   1.00 19.88 ? 261 ARG   A CZ  1 
ATOM   2061 N NH1 . ARG   A 1 260 ? 21.682  -40.699 3.156   1.00 19.57 ? 261 ARG   A NH1 1 
ATOM   2062 N NH2 . ARG   A 1 260 ? 20.125  -39.031 3.428   1.00 18.92 ? 261 ARG   A NH2 1 
ATOM   2063 N N   . TYR   A 1 261 ? 28.150  -38.319 7.471   1.00 14.53 ? 262 TYR   A N   1 
ATOM   2064 C CA  . TYR   A 1 261 ? 29.486  -38.540 8.020   1.00 14.85 ? 262 TYR   A CA  1 
ATOM   2065 C C   . TYR   A 1 261 ? 29.742  -37.416 9.015   1.00 14.43 ? 262 TYR   A C   1 
ATOM   2066 O O   . TYR   A 1 261 ? 28.939  -36.487 9.151   1.00 14.18 ? 262 TYR   A O   1 
ATOM   2067 C CB  . TYR   A 1 261 ? 30.545  -38.586 6.914   1.00 14.99 ? 262 TYR   A CB  1 
ATOM   2068 C CG  . TYR   A 1 261 ? 30.608  -37.325 6.063   1.00 15.80 ? 262 TYR   A CG  1 
ATOM   2069 C CD1 . TYR   A 1 261 ? 31.170  -36.155 6.561   1.00 14.38 ? 262 TYR   A CD1 1 
ATOM   2070 C CD2 . TYR   A 1 261 ? 30.094  -37.310 4.762   1.00 14.44 ? 262 TYR   A CD2 1 
ATOM   2071 C CE1 . TYR   A 1 261 ? 31.215  -34.997 5.804   1.00 14.10 ? 262 TYR   A CE1 1 
ATOM   2072 C CE2 . TYR   A 1 261 ? 30.145  -36.138 3.982   1.00 14.35 ? 262 TYR   A CE2 1 
ATOM   2073 C CZ  . TYR   A 1 261 ? 30.703  -34.997 4.513   1.00 14.78 ? 262 TYR   A CZ  1 
ATOM   2074 O OH  . TYR   A 1 261 ? 30.781  -33.840 3.775   1.00 13.90 ? 262 TYR   A OH  1 
ATOM   2075 N N   . GLN   A 1 262 ? 30.893  -37.488 9.682   1.00 15.49 ? 263 GLN   A N   1 
ATOM   2076 C CA  . GLN   A 1 262 ? 31.265  -36.555 10.731  1.00 17.57 ? 263 GLN   A CA  1 
ATOM   2077 C C   . GLN   A 1 262 ? 32.558  -35.845 10.358  1.00 17.14 ? 263 GLN   A C   1 
ATOM   2078 O O   . GLN   A 1 262 ? 33.456  -36.466 9.795   1.00 17.31 ? 263 GLN   A O   1 
ATOM   2079 C CB  . GLN   A 1 262 ? 31.445  -37.319 12.044  1.00 23.39 ? 263 GLN   A CB  1 
ATOM   2080 C CG  . GLN   A 1 262 ? 31.652  -36.454 13.227  1.00 20.64 ? 263 GLN   A CG  1 
ATOM   2081 C CD  . GLN   A 1 262 ? 31.538  -37.250 14.510  1.00 24.82 ? 263 GLN   A CD  1 
ATOM   2082 O OE1 . GLN   A 1 262 ? 31.385  -38.482 14.487  1.00 26.44 ? 263 GLN   A OE1 1 
ATOM   2083 N NE2 . GLN   A 1 262 ? 31.608  -36.558 15.633  1.00 27.45 ? 263 GLN   A NE2 1 
ATOM   2084 N N   . VAL   A 1 263 ? 32.647  -34.543 10.663  1.00 15.66 ? 264 VAL   A N   1 
ATOM   2085 C CA  . VAL   A 1 263 ? 33.911  -33.800 10.632  1.00 16.76 ? 264 VAL   A CA  1 
ATOM   2086 C C   . VAL   A 1 263 ? 34.037  -33.060 11.956  1.00 20.12 ? 264 VAL   A C   1 
ATOM   2087 O O   . VAL   A 1 263 ? 33.365  -32.042 12.167  1.00 17.40 ? 264 VAL   A O   1 
ATOM   2088 C CB  . VAL   A 1 263 ? 34.001  -32.816 9.458   1.00 17.61 ? 264 VAL   A CB  1 
ATOM   2089 C CG1 . VAL   A 1 263 ? 35.289  -32.038 9.568   1.00 18.16 ? 264 VAL   A CG1 1 
ATOM   2090 C CG2 . VAL   A 1 263 ? 33.969  -33.570 8.139   1.00 19.92 ? 264 VAL   A CG2 1 
ATOM   2091 N N   . ASN   A 1 264 ? 34.912  -33.553 12.834  1.00 21.16 ? 265 ASN   A N   1 
ATOM   2092 C CA  . ASN   A 1 264 ? 35.033  -33.021 14.187  1.00 23.83 ? 265 ASN   A CA  1 
ATOM   2093 C C   . ASN   A 1 264 ? 33.662  -33.044 14.860  1.00 23.62 ? 265 ASN   A C   1 
ATOM   2094 O O   . ASN   A 1 264 ? 33.068  -34.117 15.001  1.00 24.71 ? 265 ASN   A O   1 
ATOM   2095 C CB  . ASN   A 1 264 ? 35.659  -31.620 14.161  1.00 24.04 ? 265 ASN   A CB  1 
ATOM   2096 C CG  . ASN   A 1 264 ? 37.035  -31.613 13.492  1.00 23.34 ? 265 ASN   A CG  1 
ATOM   2097 O OD1 . ASN   A 1 264 ? 37.705  -32.632 13.442  1.00 26.52 ? 265 ASN   A OD1 1 
ATOM   2098 N ND2 . ASN   A 1 264 ? 37.446  -30.462 12.968  1.00 24.15 ? 265 ASN   A ND2 1 
ATOM   2099 N N   . THR   A 1 265 ? 33.126  -31.883 15.241  1.00 20.43 ? 266 THR   A N   1 
ATOM   2100 C CA  . THR   A 1 265 ? 31.865  -31.831 15.974  1.00 21.33 ? 266 THR   A CA  1 
ATOM   2101 C C   . THR   A 1 265 ? 30.654  -31.656 15.066  1.00 19.44 ? 266 THR   A C   1 
ATOM   2102 O O   . THR   A 1 265 ? 29.524  -31.562 15.566  1.00 21.45 ? 266 THR   A O   1 
ATOM   2103 C CB  . THR   A 1 265 ? 31.898  -30.690 16.993  1.00 20.57 ? 266 THR   A CB  1 
ATOM   2104 O OG1 . THR   A 1 265 ? 32.317  -29.500 16.321  1.00 22.15 ? 266 THR   A OG1 1 
ATOM   2105 C CG2 . THR   A 1 265 ? 32.878  -30.996 18.134  1.00 21.62 ? 266 THR   A CG2 1 
ATOM   2106 N N   . MET   A 1 266 ? 30.855  -31.612 13.750  1.00 16.95 ? 267 MET   A N   1 
ATOM   2107 C CA  . MET   A 1 266 ? 29.776  -31.394 12.795  1.00 15.21 ? 267 MET   A CA  1 
ATOM   2108 C C   . MET   A 1 266 ? 29.445  -32.683 12.062  1.00 16.83 ? 267 MET   A C   1 
ATOM   2109 O O   . MET   A 1 266 ? 30.341  -33.457 11.722  1.00 18.51 ? 267 MET   A O   1 
ATOM   2110 C CB  . MET   A 1 266 ? 30.174  -30.310 11.787  1.00 16.04 ? 267 MET   A CB  1 
ATOM   2111 C CG  . MET   A 1 266 ? 29.150  -30.045 10.705  1.00 21.51 ? 267 MET   A CG  1 
ATOM   2112 S SD  . MET   A 1 266 ? 29.695  -28.716 9.592   1.00 24.11 ? 267 MET   A SD  1 
ATOM   2113 C CE  . MET   A 1 266 ? 30.866  -29.618 8.567   1.00 23.81 ? 267 MET   A CE  1 
ATOM   2114 N N   . TYR   A 1 267 ? 28.152  -32.935 11.859  1.00 15.29 ? 268 TYR   A N   1 
ATOM   2115 C CA  . TYR   A 1 267 ? 27.678  -34.016 11.003  1.00 14.84 ? 268 TYR   A CA  1 
ATOM   2116 C C   . TYR   A 1 267 ? 27.124  -33.408 9.723   1.00 15.10 ? 268 TYR   A C   1 
ATOM   2117 O O   . TYR   A 1 267 ? 26.332  -32.471 9.784   1.00 16.31 ? 268 TYR   A O   1 
ATOM   2118 C CB  . TYR   A 1 267 ? 26.589  -34.832 11.703  1.00 17.33 ? 268 TYR   A CB  1 
ATOM   2119 C CG  . TYR   A 1 267 ? 27.052  -35.485 12.986  1.00 18.70 ? 268 TYR   A CG  1 
ATOM   2120 C CD1 . TYR   A 1 267 ? 27.024  -34.795 14.191  1.00 19.40 ? 268 TYR   A CD1 1 
ATOM   2121 C CD2 . TYR   A 1 267 ? 27.503  -36.806 12.992  1.00 24.05 ? 268 TYR   A CD2 1 
ATOM   2122 C CE1 . TYR   A 1 267 ? 27.443  -35.400 15.378  1.00 22.32 ? 268 TYR   A CE1 1 
ATOM   2123 C CE2 . TYR   A 1 267 ? 27.919  -37.417 14.172  1.00 28.48 ? 268 TYR   A CE2 1 
ATOM   2124 C CZ  . TYR   A 1 267 ? 27.885  -36.701 15.361  1.00 23.89 ? 268 TYR   A CZ  1 
ATOM   2125 O OH  . TYR   A 1 267 ? 28.298  -37.307 16.531  1.00 25.89 ? 268 TYR   A OH  1 
ATOM   2126 N N   . GLN   A 1 268 ? 27.573  -33.895 8.571   1.00 13.00 ? 269 GLN   A N   1 
ATOM   2127 C CA  . GLN   A 1 268 ? 27.081  -33.391 7.293   1.00 13.49 ? 269 GLN   A CA  1 
ATOM   2128 C C   . GLN   A 1 268 ? 25.836  -34.190 6.922   1.00 15.75 ? 269 GLN   A C   1 
ATOM   2129 O O   . GLN   A 1 268 ? 25.920  -35.391 6.664   1.00 15.75 ? 269 GLN   A O   1 
ATOM   2130 C CB  . GLN   A 1 268 ? 28.140  -33.522 6.204   1.00 13.57 ? 269 GLN   A CB  1 
ATOM   2131 C CG  . GLN   A 1 268 ? 27.705  -32.960 4.832   1.00 13.11 ? 269 GLN   A CG  1 
ATOM   2132 C CD  . GLN   A 1 268 ? 27.433  -31.471 4.904   1.00 16.18 ? 269 GLN   A CD  1 
ATOM   2133 O OE1 . GLN   A 1 268 ? 28.339  -30.692 5.138   1.00 14.74 ? 269 GLN   A OE1 1 
ATOM   2134 N NE2 . GLN   A 1 268 ? 26.178  -31.070 4.711   1.00 13.62 ? 269 GLN   A NE2 1 
ATOM   2135 N N   . ALA   A 1 269 ? 24.691  -33.536 6.924   1.00 13.85 ? 270 ALA   A N   1 
ATOM   2136 C CA  . ALA   A 1 269 ? 23.470  -34.107 6.370   1.00 13.56 ? 270 ALA   A CA  1 
ATOM   2137 C C   . ALA   A 1 269 ? 23.338  -33.596 4.937   1.00 15.17 ? 270 ALA   A C   1 
ATOM   2138 O O   . ALA   A 1 269 ? 24.282  -33.042 4.371   1.00 15.57 ? 270 ALA   A O   1 
ATOM   2139 C CB  . ALA   A 1 269 ? 22.265  -33.760 7.253   1.00 17.30 ? 270 ALA   A CB  1 
ATOM   2140 N N   . LEU   A 1 270 ? 22.172  -33.779 4.317   1.00 16.76 ? 271 LEU   A N   1 
ATOM   2141 C CA  . LEU   A 1 270 ? 21.972  -33.215 2.976   1.00 17.72 ? 271 LEU   A CA  1 
ATOM   2142 C C   . LEU   A 1 270 ? 21.582  -31.749 3.108   1.00 16.56 ? 271 LEU   A C   1 
ATOM   2143 O O   . LEU   A 1 270 ? 20.483  -31.443 3.584   1.00 16.70 ? 271 LEU   A O   1 
ATOM   2144 C CB  . LEU   A 1 270 ? 20.892  -33.965 2.213   1.00 18.71 ? 271 LEU   A CB  1 
ATOM   2145 C CG  . LEU   A 1 270 ? 21.083  -35.457 2.114   1.00 20.32 ? 271 LEU   A CG  1 
ATOM   2146 C CD1 . LEU   A 1 270 ? 19.897  -36.018 1.312   1.00 20.03 ? 271 LEU   A CD1 1 
ATOM   2147 C CD2 . LEU   A 1 270 ? 22.395  -35.730 1.411   1.00 23.63 ? 271 LEU   A CD2 1 
ATOM   2148 N N   . GLY   A 1 271 ? 22.452  -30.851 2.648   1.00 15.55 ? 272 GLY   A N   1 
ATOM   2149 C CA  . GLY   A 1 271 ? 22.245  -29.420 2.787   1.00 15.04 ? 272 GLY   A CA  1 
ATOM   2150 C C   . GLY   A 1 271 ? 22.520  -28.935 4.196   1.00 13.00 ? 272 GLY   A C   1 
ATOM   2151 O O   . GLY   A 1 271 ? 23.463  -28.165 4.432   1.00 14.80 ? 272 GLY   A O   1 
ATOM   2152 N N   . TRP   A 1 272 ? 21.696  -29.396 5.134   1.00 14.56 ? 273 TRP   A N   1 
ATOM   2153 C CA  . TRP   A 1 272 ? 21.843  -29.026 6.539   1.00 14.53 ? 273 TRP   A CA  1 
ATOM   2154 C C   . TRP   A 1 272 ? 23.148  -29.532 7.151   1.00 14.32 ? 273 TRP   A C   1 
ATOM   2155 O O   . TRP   A 1 272 ? 23.634  -30.617 6.831   1.00 14.39 ? 273 TRP   A O   1 
ATOM   2156 C CB  . TRP   A 1 272 ? 20.698  -29.611 7.370   1.00 13.88 ? 273 TRP   A CB  1 
ATOM   2157 C CG  . TRP   A 1 272 ? 19.347  -29.105 7.041   1.00 15.63 ? 273 TRP   A CG  1 
ATOM   2158 C CD1 . TRP   A 1 272 ? 18.380  -29.757 6.333   1.00 15.73 ? 273 TRP   A CD1 1 
ATOM   2159 C CD2 . TRP   A 1 272 ? 18.765  -27.858 7.466   1.00 15.61 ? 273 TRP   A CD2 1 
ATOM   2160 N NE1 . TRP   A 1 272 ? 17.253  -28.970 6.250   1.00 18.44 ? 273 TRP   A NE1 1 
ATOM   2161 C CE2 . TRP   A 1 272 ? 17.466  -27.804 6.935   1.00 16.04 ? 273 TRP   A CE2 1 
ATOM   2162 C CE3 . TRP   A 1 272 ? 19.232  -26.772 8.216   1.00 14.16 ? 273 TRP   A CE3 1 
ATOM   2163 C CZ2 . TRP   A 1 272 ? 16.610  -26.719 7.155   1.00 15.45 ? 273 TRP   A CZ2 1 
ATOM   2164 C CZ3 . TRP   A 1 272 ? 18.389  -25.694 8.425   1.00 12.74 ? 273 TRP   A CZ3 1 
ATOM   2165 C CH2 . TRP   A 1 272 ? 17.082  -25.679 7.902   1.00 16.47 ? 273 TRP   A CH2 1 
ATOM   2166 N N   . GLU   A 1 273 ? 23.675  -28.746 8.088   1.00 13.26 ? 274 GLU   A N   1 
ATOM   2167 C CA  . GLU   A 1 273 ? 24.695  -29.189 9.035   1.00 14.49 ? 274 GLU   A CA  1 
ATOM   2168 C C   . GLU   A 1 273 ? 24.008  -29.601 10.329  1.00 15.77 ? 274 GLU   A C   1 
ATOM   2169 O O   . GLU   A 1 273 ? 23.079  -28.933 10.789  1.00 16.19 ? 274 GLU   A O   1 
ATOM   2170 C CB  . GLU   A 1 273 ? 25.709  -28.072 9.302   1.00 15.66 ? 274 GLU   A CB  1 
ATOM   2171 C CG  . GLU   A 1 273 ? 26.441  -27.702 8.033   1.00 16.58 ? 274 GLU   A CG  1 
ATOM   2172 C CD  . GLU   A 1 273 ? 27.164  -26.383 8.118   1.00 21.18 ? 274 GLU   A CD  1 
ATOM   2173 O OE1 . GLU   A 1 273 ? 27.107  -25.705 9.165   1.00 23.95 ? 274 GLU   A OE1 1 
ATOM   2174 O OE2 . GLU   A 1 273 ? 27.821  -26.029 7.117   1.00 22.97 ? 274 GLU   A OE2 1 
ATOM   2175 N N   . GLU   A 1 274 ? 24.447  -30.726 10.894  1.00 13.74 ? 275 GLU   A N   1 
ATOM   2176 C CA  . GLU   A 1 274 ? 23.791  -31.363 12.023  1.00 14.14 ? 275 GLU   A CA  1 
ATOM   2177 C C   . GLU   A 1 274 ? 24.743  -31.397 13.209  1.00 15.40 ? 275 GLU   A C   1 
ATOM   2178 O O   . GLU   A 1 274 ? 25.950  -31.594 13.035  1.00 15.22 ? 275 GLU   A O   1 
ATOM   2179 C CB  . GLU   A 1 274 ? 23.353  -32.782 11.625  1.00 15.68 ? 275 GLU   A CB  1 
ATOM   2180 C CG  . GLU   A 1 274 ? 22.796  -33.652 12.717  1.00 17.92 ? 275 GLU   A CG  1 
ATOM   2181 C CD  . GLU   A 1 274 ? 22.380  -35.001 12.171  1.00 24.79 ? 275 GLU   A CD  1 
ATOM   2182 O OE1 . GLU   A 1 274 ? 22.759  -35.314 11.032  1.00 29.25 ? 275 GLU   A OE1 1 
ATOM   2183 O OE2 . GLU   A 1 274 ? 21.660  -35.739 12.857  1.00 30.41 ? 275 GLU   A OE2 1 
ATOM   2184 N N   . PHE   A 1 275 ? 24.201  -31.205 14.414  1.00 14.79 ? 276 PHE   A N   1 
ATOM   2185 C CA  . PHE   A 1 275 ? 25.003  -31.186 15.631  1.00 14.98 ? 276 PHE   A CA  1 
ATOM   2186 C C   . PHE   A 1 275 ? 24.248  -31.900 16.739  1.00 13.84 ? 276 PHE   A C   1 
ATOM   2187 O O   . PHE   A 1 275 ? 23.019  -31.862 16.798  1.00 16.83 ? 276 PHE   A O   1 
ATOM   2188 C CB  . PHE   A 1 275 ? 25.310  -29.744 16.097  1.00 15.36 ? 276 PHE   A CB  1 
ATOM   2189 C CG  . PHE   A 1 275 ? 25.870  -28.877 15.013  1.00 15.71 ? 276 PHE   A CG  1 
ATOM   2190 C CD1 . PHE   A 1 275 ? 25.014  -28.177 14.172  1.00 17.24 ? 276 PHE   A CD1 1 
ATOM   2191 C CD2 . PHE   A 1 275 ? 27.241  -28.779 14.820  1.00 17.20 ? 276 PHE   A CD2 1 
ATOM   2192 C CE1 . PHE   A 1 275 ? 25.519  -27.394 13.145  1.00 15.67 ? 276 PHE   A CE1 1 
ATOM   2193 C CE2 . PHE   A 1 275 ? 27.767  -27.989 13.793  1.00 14.90 ? 276 PHE   A CE2 1 
ATOM   2194 C CZ  . PHE   A 1 275 ? 26.896  -27.293 12.962  1.00 15.77 ? 276 PHE   A CZ  1 
ATOM   2195 N N   . SER   A 1 276 ? 24.998  -32.529 17.641  1.00 15.67 ? 277 SER   A N   1 
ATOM   2196 C CA  . SER   A 1 276 ? 24.379  -33.032 18.856  1.00 16.21 ? 277 SER   A CA  1 
ATOM   2197 C C   . SER   A 1 276 ? 23.844  -31.857 19.672  1.00 18.50 ? 277 SER   A C   1 
ATOM   2198 O O   . SER   A 1 276 ? 24.494  -30.812 19.789  1.00 17.98 ? 277 SER   A O   1 
ATOM   2199 C CB  . SER   A 1 276 ? 25.395  -33.834 19.661  1.00 20.04 ? 277 SER   A CB  1 
ATOM   2200 O OG  . SER   A 1 276 ? 24.848  -34.264 20.899  1.00 22.45 ? 277 SER   A OG  1 
ATOM   2201 N N   . TYR   A 1 277 ? 22.636  -32.022 20.221  1.00 17.60 ? 278 TYR   A N   1 
ATOM   2202 C CA  . TYR   A 1 277 ? 21.973  -30.951 20.947  1.00 18.96 ? 278 TYR   A CA  1 
ATOM   2203 C C   . TYR   A 1 277 ? 22.031  -31.222 22.440  1.00 17.91 ? 278 TYR   A C   1 
ATOM   2204 O O   . TYR   A 1 277 ? 21.713  -32.341 22.863  1.00 22.95 ? 278 TYR   A O   1 
ATOM   2205 C CB  . TYR   A 1 277 ? 20.512  -30.812 20.508  1.00 17.60 ? 278 TYR   A CB  1 
ATOM   2206 C CG  . TYR   A 1 277 ? 19.792  -29.729 21.284  1.00 20.76 ? 278 TYR   A CG  1 
ATOM   2207 C CD1 . TYR   A 1 277 ? 20.006  -28.385 20.987  1.00 23.46 ? 278 TYR   A CD1 1 
ATOM   2208 C CD2 . TYR   A 1 277 ? 18.899  -30.047 22.287  1.00 26.50 ? 278 TYR   A CD2 1 
ATOM   2209 C CE1 . TYR   A 1 277 ? 19.376  -27.392 21.710  1.00 23.14 ? 278 TYR   A CE1 1 
ATOM   2210 C CE2 . TYR   A 1 277 ? 18.259  -29.056 23.008  1.00 25.79 ? 278 TYR   A CE2 1 
ATOM   2211 C CZ  . TYR   A 1 277 ? 18.498  -27.728 22.700  1.00 24.29 ? 278 TYR   A CZ  1 
ATOM   2212 O OH  . TYR   A 1 277 ? 17.854  -26.735 23.417  1.00 34.46 ? 278 TYR   A OH  1 
ATOM   2213 N N   . PRO   A 1 278 ? 22.418  -30.232 23.275  1.00 18.22 ? 279 PRO   A N   1 
ATOM   2214 C CA  . PRO   A 1 278 ? 22.805  -28.861 22.907  1.00 19.06 ? 279 PRO   A CA  1 
ATOM   2215 C C   . PRO   A 1 278 ? 24.173  -28.789 22.256  1.00 17.81 ? 279 PRO   A C   1 
ATOM   2216 O O   . PRO   A 1 278 ? 25.115  -29.483 22.654  1.00 19.20 ? 279 PRO   A O   1 
ATOM   2217 C CB  . PRO   A 1 278 ? 22.813  -28.108 24.255  1.00 19.10 ? 279 PRO   A CB  1 
ATOM   2218 C CG  . PRO   A 1 278 ? 22.018  -28.962 25.205  1.00 21.32 ? 279 PRO   A CG  1 
ATOM   2219 C CD  . PRO   A 1 278 ? 22.262  -30.381 24.735  1.00 19.47 ? 279 PRO   A CD  1 
ATOM   2220 N N   . ALA   A 1 279 ? 24.304  -27.943 21.241  1.00 18.74 ? 280 ALA   A N   1 
ATOM   2221 C CA  . ALA   A 1 279 ? 25.611  -27.616 20.696  1.00 19.55 ? 280 ALA   A CA  1 
ATOM   2222 C C   . ALA   A 1 279 ? 26.201  -26.434 21.459  1.00 18.30 ? 280 ALA   A C   1 
ATOM   2223 O O   . ALA   A 1 279 ? 25.504  -25.445 21.722  1.00 19.54 ? 280 ALA   A O   1 
ATOM   2224 C CB  . ALA   A 1 279 ? 25.505  -27.294 19.206  1.00 17.56 ? 280 ALA   A CB  1 
ATOM   2225 N N   . THR   A 1 280 ? 27.474  -26.528 21.821  1.00 17.22 ? 281 THR   A N   1 
ATOM   2226 C CA  . THR   A 1 280 ? 28.101  -25.348 22.402  1.00 16.80 ? 281 THR   A CA  1 
ATOM   2227 C C   . THR   A 1 280 ? 28.175  -24.256 21.348  1.00 17.04 ? 281 THR   A C   1 
ATOM   2228 O O   . THR   A 1 280 ? 28.164  -24.529 20.147  1.00 17.77 ? 281 THR   A O   1 
ATOM   2229 C CB  . THR   A 1 280 ? 29.508  -25.646 22.906  1.00 18.78 ? 281 THR   A CB  1 
ATOM   2230 O OG1 . THR   A 1 280 ? 30.351  -25.956 21.788  1.00 20.05 ? 281 THR   A OG1 1 
ATOM   2231 C CG2 . THR   A 1 280 ? 29.495  -26.809 23.909  1.00 20.07 ? 281 THR   A CG2 1 
ATOM   2232 N N   . LEU   A 1 281 ? 28.242  -22.999 21.798  1.00 17.27 ? 282 LEU   A N   1 
ATOM   2233 C CA  . LEU   A 1 281 ? 28.402  -21.920 20.822  1.00 16.64 ? 282 LEU   A CA  1 
ATOM   2234 C C   . LEU   A 1 281 ? 29.664  -22.126 19.996  1.00 16.65 ? 282 LEU   A C   1 
ATOM   2235 O O   . LEU   A 1 281 ? 29.655  -21.934 18.777  1.00 17.66 ? 282 LEU   A O   1 
ATOM   2236 C CB  . LEU   A 1 281 ? 28.425  -20.562 21.524  1.00 20.16 ? 282 LEU   A CB  1 
ATOM   2237 C CG  . LEU   A 1 281 ? 28.684  -19.345 20.635  1.00 17.33 ? 282 LEU   A CG  1 
ATOM   2238 C CD1 . LEU   A 1 281 ? 27.678  -19.244 19.483  1.00 18.29 ? 282 LEU   A CD1 1 
ATOM   2239 C CD2 . LEU   A 1 281 ? 28.686  -18.073 21.486  1.00 22.44 ? 282 LEU   A CD2 1 
ATOM   2240 N N   . GLN   A 1 282 ? 30.751  -22.569 20.633  1.00 19.02 ? 283 GLN   A N   1 
ATOM   2241 C CA  . GLN   A 1 282 ? 31.985  -22.795 19.886  1.00 20.98 ? 283 GLN   A CA  1 
ATOM   2242 C C   . GLN   A 1 282 ? 31.802  -23.834 18.787  1.00 19.08 ? 283 GLN   A C   1 
ATOM   2243 O O   . GLN   A 1 282 ? 32.341  -23.676 17.686  1.00 19.28 ? 283 GLN   A O   1 
ATOM   2244 C CB  . GLN   A 1 282 ? 33.108  -23.234 20.823  1.00 21.29 ? 283 GLN   A CB  1 
ATOM   2245 C CG  . GLN   A 1 282 ? 34.491  -23.152 20.171  1.00 23.80 ? 283 GLN   A CG  1 
ATOM   2246 C CD  . GLN   A 1 282 ? 34.795  -21.743 19.681  1.00 27.82 ? 283 GLN   A CD  1 
ATOM   2247 O OE1 . GLN   A 1 282 ? 34.857  -20.801 20.477  1.00 30.34 ? 283 GLN   A OE1 1 
ATOM   2248 N NE2 . GLN   A 1 282 ? 34.951  -21.583 18.365  1.00 25.23 ? 283 GLN   A NE2 1 
ATOM   2249 N N   . THR   A 1 283 ? 31.101  -24.934 19.080  1.00 17.34 ? 284 THR   A N   1 
ATOM   2250 C CA  . THR   A 1 283 ? 30.817  -25.919 18.032  1.00 19.12 ? 284 THR   A CA  1 
ATOM   2251 C C   . THR   A 1 283 ? 30.108  -25.286 16.846  1.00 17.59 ? 284 THR   A C   1 
ATOM   2252 O O   . THR   A 1 283 ? 30.469  -25.544 15.690  1.00 18.12 ? 284 THR   A O   1 
ATOM   2253 C CB  . THR   A 1 283 ? 29.990  -27.074 18.602  1.00 18.89 ? 284 THR   A CB  1 
ATOM   2254 O OG1 . THR   A 1 283 ? 30.851  -27.876 19.411  1.00 19.19 ? 284 THR   A OG1 1 
ATOM   2255 C CG2 . THR   A 1 283 ? 29.371  -27.950 17.490  1.00 16.94 ? 284 THR   A CG2 1 
ATOM   2256 N N   . LEU   A 1 284 ? 29.117  -24.427 17.102  1.00 16.54 ? 285 LEU   A N   1 
ATOM   2257 C CA  . LEU   A 1 284 ? 28.387  -23.819 15.996  1.00 16.68 ? 285 LEU   A CA  1 
ATOM   2258 C C   . LEU   A 1 284 ? 29.278  -22.856 15.218  1.00 16.63 ? 285 LEU   A C   1 
ATOM   2259 O O   . LEU   A 1 284 ? 29.198  -22.792 13.981  1.00 17.45 ? 285 LEU   A O   1 
ATOM   2260 C CB  . LEU   A 1 284 ? 27.133  -23.116 16.529  1.00 17.64 ? 285 LEU   A CB  1 
ATOM   2261 C CG  . LEU   A 1 284 ? 26.125  -24.059 17.199  1.00 16.96 ? 285 LEU   A CG  1 
ATOM   2262 C CD1 . LEU   A 1 284 ? 24.966  -23.278 17.836  1.00 18.77 ? 285 LEU   A CD1 1 
ATOM   2263 C CD2 . LEU   A 1 284 ? 25.611  -25.104 16.201  1.00 17.61 ? 285 LEU   A CD2 1 
ATOM   2264 N N   . LEU   A 1 285 ? 30.148  -22.114 15.924  1.00 17.59 ? 286 LEU   A N   1 
ATOM   2265 C CA  . LEU   A 1 285 ? 31.101  -21.217 15.266  1.00 17.23 ? 286 LEU   A CA  1 
ATOM   2266 C C   . LEU   A 1 285 ? 32.141  -21.988 14.456  1.00 19.70 ? 286 LEU   A C   1 
ATOM   2267 O O   . LEU   A 1 285 ? 32.489  -21.577 13.335  1.00 18.96 ? 286 LEU   A O   1 
ATOM   2268 C CB  . LEU   A 1 285 ? 31.801  -20.339 16.307  1.00 18.62 ? 286 LEU   A CB  1 
ATOM   2269 C CG  . LEU   A 1 285 ? 30.885  -19.342 17.019  1.00 19.82 ? 286 LEU   A CG  1 
ATOM   2270 C CD1 . LEU   A 1 285 ? 31.616  -18.599 18.115  1.00 20.61 ? 286 LEU   A CD1 1 
ATOM   2271 C CD2 . LEU   A 1 285 ? 30.292  -18.353 16.024  1.00 19.19 ? 286 LEU   A CD2 1 
ATOM   2272 N N   . ASP   A 1 286 ? 32.651  -23.097 15.013  1.00 20.41 ? 287 ASP   A N   1 
ATOM   2273 C CA  . ASP   A 1 286 ? 33.639  -23.923 14.321  1.00 21.08 ? 287 ASP   A CA  1 
ATOM   2274 C C   . ASP   A 1 286 ? 33.138  -24.385 12.961  1.00 19.56 ? 287 ASP   A C   1 
ATOM   2275 O O   . ASP   A 1 286 ? 33.934  -24.527 12.019  1.00 19.94 ? 287 ASP   A O   1 
ATOM   2276 C CB  . ASP   A 1 286 ? 33.999  -25.154 15.166  1.00 21.41 ? 287 ASP   A CB  1 
ATOM   2277 C CG  . ASP   A 1 286 ? 34.820  -24.818 16.410  1.00 23.73 ? 287 ASP   A CG  1 
ATOM   2278 O OD1 . ASP   A 1 286 ? 35.348  -23.685 16.536  1.00 26.82 ? 287 ASP   A OD1 1 
ATOM   2279 O OD2 . ASP   A 1 286 ? 34.934  -25.716 17.279  1.00 26.56 ? 287 ASP   A OD2 1 
ATOM   2280 N N   . SER   A 1 287 ? 31.835  -24.643 12.836  1.00 19.58 ? 288 SER   A N   1 
ATOM   2281 C CA  . SER   A 1 287 ? 31.304  -25.141 11.576  1.00 19.64 ? 288 SER   A CA  1 
ATOM   2282 C C   . SER   A 1 287 ? 31.527  -24.153 10.443  1.00 20.49 ? 288 SER   A C   1 
ATOM   2283 O O   . SER   A 1 287 ? 31.485  -24.548 9.272   1.00 20.66 ? 288 SER   A O   1 
ATOM   2284 C CB  . SER   A 1 287 ? 29.809  -25.445 11.714  1.00 19.67 ? 288 SER   A CB  1 
ATOM   2285 O OG  . SER   A 1 287 ? 29.050  -24.234 11.734  1.00 19.51 ? 288 SER   A OG  1 
ATOM   2286 N N   . ASN   A 1 288 ? 31.789  -22.886 10.764  1.00 20.55 ? 289 ASN   A N   1 
ATOM   2287 C CA  . ASN   A 1 288 ? 32.010  -21.865 9.752   1.00 22.67 ? 289 ASN   A CA  1 
ATOM   2288 C C   . ASN   A 1 288 ? 33.427  -21.304 9.783   1.00 21.63 ? 289 ASN   A C   1 
ATOM   2289 O O   . ASN   A 1 288 ? 33.683  -20.241 9.206   1.00 22.44 ? 289 ASN   A O   1 
ATOM   2290 C CB  . ASN   A 1 288 ? 30.968  -20.755 9.903   1.00 24.63 ? 289 ASN   A CB  1 
ATOM   2291 C CG  . ASN   A 1 288 ? 29.698  -21.053 9.116   1.00 30.63 ? 289 ASN   A CG  1 
ATOM   2292 O OD1 . ASN   A 1 288 ? 29.418  -20.388 8.116   1.00 33.29 ? 289 ASN   A OD1 1 
ATOM   2293 N ND2 . ASN   A 1 288 ? 28.934  -22.077 9.550   1.00 25.00 ? 289 ASN   A ND2 1 
ATOM   2294 N N   . SER   A 1 289 ? 34.362  -22.021 10.404  1.00 19.38 ? 290 SER   A N   1 
ATOM   2295 C CA  . SER   A 1 289 ? 35.766  -21.656 10.397  1.00 22.14 ? 290 SER   A CA  1 
ATOM   2296 C C   . SER   A 1 289 ? 36.345  -21.755 8.987   1.00 21.36 ? 290 SER   A C   1 
ATOM   2297 O O   . SER   A 1 289 ? 35.820  -22.468 8.126   1.00 19.28 ? 290 SER   A O   1 
ATOM   2298 C CB  . SER   A 1 289 ? 36.550  -22.566 11.340  1.00 22.09 ? 290 SER   A CB  1 
ATOM   2299 O OG  . SER   A 1 289 ? 36.677  -23.874 10.805  1.00 21.56 ? 290 SER   A OG  1 
ATOM   2300 N N   . GLU   A 1 290 ? 37.448  -21.028 8.759   1.00 22.51 ? 291 GLU   A N   1 
ATOM   2301 C CA  . GLU   A 1 290 ? 38.135  -21.116 7.469   1.00 21.56 ? 291 GLU   A CA  1 
ATOM   2302 C C   . GLU   A 1 290 ? 38.552  -22.550 7.173   1.00 24.28 ? 291 GLU   A C   1 
ATOM   2303 O O   . GLU   A 1 290 ? 38.411  -23.026 6.039   1.00 19.57 ? 291 GLU   A O   1 
ATOM   2304 C CB  . GLU   A 1 290 ? 39.357  -20.196 7.455   1.00 27.09 ? 291 GLU   A CB  1 
ATOM   2305 C CG  . GLU   A 1 290 ? 40.015  -20.060 6.082   1.00 31.68 ? 291 GLU   A CG  1 
ATOM   2306 C CD  . GLU   A 1 290 ? 41.333  -19.309 6.140   1.00 40.45 ? 291 GLU   A CD  1 
ATOM   2307 O OE1 . GLU   A 1 290 ? 41.646  -18.576 5.178   1.00 46.92 ? 291 GLU   A OE1 1 
ATOM   2308 O OE2 . GLU   A 1 290 ? 42.057  -19.458 7.147   1.00 44.04 ? 291 GLU   A OE2 1 
ATOM   2309 N N   . GLN   A 1 291 ? 39.046  -23.263 8.188   1.00 20.70 ? 292 GLN   A N   1 
ATOM   2310 C CA  . GLN   A 1 291 ? 39.465  -24.647 7.987   1.00 21.19 ? 292 GLN   A CA  1 
ATOM   2311 C C   . GLN   A 1 291 ? 38.318  -25.499 7.458   1.00 20.50 ? 292 GLN   A C   1 
ATOM   2312 O O   . GLN   A 1 291 ? 38.497  -26.278 6.514   1.00 20.89 ? 292 GLN   A O   1 
ATOM   2313 C CB  . GLN   A 1 291 ? 40.008  -25.234 9.294   1.00 22.79 ? 292 GLN   A CB  1 
ATOM   2314 C CG  . GLN   A 1 291 ? 40.395  -26.721 9.208   1.00 23.47 ? 292 GLN   A CG  1 
ATOM   2315 C CD  . GLN   A 1 291 ? 41.566  -26.978 8.289   1.00 27.10 ? 292 GLN   A CD  1 
ATOM   2316 O OE1 . GLN   A 1 291 ? 42.534  -26.214 8.267   1.00 32.07 ? 292 GLN   A OE1 1 
ATOM   2317 N NE2 . GLN   A 1 291 ? 41.494  -28.066 7.522   1.00 25.40 ? 292 GLN   A NE2 1 
ATOM   2318 N N   . ILE   A 1 292 ? 37.128  -25.369 8.054   1.00 17.91 ? 293 ILE   A N   1 
ATOM   2319 C CA  . ILE   A 1 292 ? 36.007  -26.210 7.623   1.00 16.14 ? 293 ILE   A CA  1 
ATOM   2320 C C   . ILE   A 1 292 ? 35.455  -25.740 6.278   1.00 21.15 ? 293 ILE   A C   1 
ATOM   2321 O O   . ILE   A 1 292 ? 35.089  -26.561 5.423   1.00 18.83 ? 293 ILE   A O   1 
ATOM   2322 C CB  . ILE   A 1 292 ? 34.907  -26.242 8.702   1.00 17.83 ? 293 ILE   A CB  1 
ATOM   2323 C CG1 . ILE   A 1 292 ? 35.428  -26.926 9.968   1.00 21.50 ? 293 ILE   A CG1 1 
ATOM   2324 C CG2 . ILE   A 1 292 ? 33.638  -26.936 8.190   1.00 17.70 ? 293 ILE   A CG2 1 
ATOM   2325 C CD1 . ILE   A 1 292 ? 35.838  -28.397 9.767   1.00 23.52 ? 293 ILE   A CD1 1 
ATOM   2326 N N   . VAL   A 1 293 ? 35.394  -24.422 6.054   1.00 17.73 ? 294 VAL   A N   1 
ATOM   2327 C CA  . VAL   A 1 293 ? 34.668  -23.912 4.890   1.00 19.46 ? 294 VAL   A CA  1 
ATOM   2328 C C   . VAL   A 1 293 ? 35.525  -23.938 3.629   1.00 17.93 ? 294 VAL   A C   1 
ATOM   2329 O O   . VAL   A 1 293 ? 35.004  -24.174 2.529   1.00 19.56 ? 294 VAL   A O   1 
ATOM   2330 C CB  . VAL   A 1 293 ? 34.139  -22.489 5.164   1.00 18.43 ? 294 VAL   A CB  1 
ATOM   2331 C CG1 . VAL   A 1 293 ? 33.520  -21.875 3.889   1.00 27.18 ? 294 VAL   A CG1 1 
ATOM   2332 C CG2 . VAL   A 1 293 ? 33.121  -22.508 6.293   1.00 20.27 ? 294 VAL   A CG2 1 
ATOM   2333 N N   . MET   A 1 294 ? 36.840  -23.695 3.748   1.00 17.31 ? 295 MET   A N   1 
ATOM   2334 C CA  . MET   A 1 294 ? 37.686  -23.497 2.572   1.00 18.71 ? 295 MET   A CA  1 
ATOM   2335 C C   . MET   A 1 294 ? 38.618  -24.656 2.241   1.00 19.51 ? 295 MET   A C   1 
ATOM   2336 O O   . MET   A 1 294 ? 39.130  -24.711 1.116   1.00 22.13 ? 295 MET   A O   1 
ATOM   2337 C CB  . MET   A 1 294 ? 38.540  -22.229 2.754   1.00 24.71 ? 295 MET   A CB  1 
ATOM   2338 C CG  . MET   A 1 294 ? 37.718  -20.979 2.982   1.00 26.27 ? 295 MET   A CG  1 
ATOM   2339 S SD  . MET   A 1 294 ? 36.658  -20.573 1.569   1.00 36.75 ? 295 MET   A SD  1 
ATOM   2340 C CE  . MET   A 1 294 ? 37.866  -20.259 0.296   1.00 30.36 ? 295 MET   A CE  1 
ATOM   2341 N N   . LYS   A 1 295 ? 38.896  -25.549 3.186   1.00 17.72 ? 296 LYS   A N   1 
ATOM   2342 C CA  . LYS   A 1 295 ? 39.909  -26.576 2.991   1.00 18.88 ? 296 LYS   A CA  1 
ATOM   2343 C C   . LYS   A 1 295 ? 39.282  -27.965 2.972   1.00 17.60 ? 296 LYS   A C   1 
ATOM   2344 O O   . LYS   A 1 295 ? 38.167  -28.154 3.469   1.00 18.17 ? 296 LYS   A O   1 
ATOM   2345 C CB  . LYS   A 1 295 ? 40.956  -26.510 4.111   1.00 20.35 ? 296 LYS   A CB  1 
ATOM   2346 C CG  . LYS   A 1 295 ? 41.534  -25.123 4.319   1.00 27.60 ? 296 LYS   A CG  1 
ATOM   2347 C CD  . LYS   A 1 295 ? 43.042  -25.183 4.417   1.00 37.17 ? 296 LYS   A CD  1 
ATOM   2348 C CE  . LYS   A 1 295 ? 43.656  -23.786 4.418   1.00 36.42 ? 296 LYS   A CE  1 
ATOM   2349 N NZ  . LYS   A 1 295 ? 45.136  -23.862 4.561   1.00 42.89 ? 296 LYS   A NZ  1 
ATOM   2350 N N   . PRO   A 1 296 ? 39.961  -28.961 2.395   1.00 18.14 ? 297 PRO   A N   1 
ATOM   2351 C CA  . PRO   A 1 296 ? 39.479  -30.339 2.535   1.00 18.46 ? 297 PRO   A CA  1 
ATOM   2352 C C   . PRO   A 1 296 ? 39.717  -30.853 3.946   1.00 21.39 ? 297 PRO   A C   1 
ATOM   2353 O O   . PRO   A 1 296 ? 40.742  -30.570 4.572   1.00 22.87 ? 297 PRO   A O   1 
ATOM   2354 C CB  . PRO   A 1 296 ? 40.298  -31.118 1.497   1.00 19.87 ? 297 PRO   A CB  1 
ATOM   2355 C CG  . PRO   A 1 296 ? 41.549  -30.347 1.349   1.00 25.67 ? 297 PRO   A CG  1 
ATOM   2356 C CD  . PRO   A 1 296 ? 41.135  -28.884 1.506   1.00 22.18 ? 297 PRO   A CD  1 
ATOM   2357 N N   . ASN   A 1 297 ? 38.728  -31.566 4.472   1.00 18.67 ? 298 ASN   A N   1 
ATOM   2358 C CA  . ASN   A 1 297 ? 38.847  -32.175 5.789   1.00 18.98 ? 298 ASN   A CA  1 
ATOM   2359 C C   . ASN   A 1 297 ? 38.447  -33.636 5.707   1.00 17.29 ? 298 ASN   A C   1 
ATOM   2360 O O   . ASN   A 1 297 ? 37.436  -33.974 5.091   1.00 16.79 ? 298 ASN   A O   1 
ATOM   2361 C CB  . ASN   A 1 297 ? 37.992  -31.457 6.824   1.00 16.67 ? 298 ASN   A CB  1 
ATOM   2362 C CG  . ASN   A 1 297 ? 38.509  -30.071 7.127   1.00 18.62 ? 298 ASN   A CG  1 
ATOM   2363 O OD1 . ASN   A 1 297 ? 39.418  -29.891 7.951   1.00 19.45 ? 298 ASN   A OD1 1 
ATOM   2364 N ND2 . ASN   A 1 297 ? 37.965  -29.082 6.428   1.00 19.56 ? 298 ASN   A ND2 1 
ATOM   2365 N N   . LYS   A 1 298 ? 39.251  -34.495 6.323   1.00 17.93 ? 299 LYS   A N   1 
ATOM   2366 C CA  . LYS   A 1 298 ? 38.963  -35.921 6.296   1.00 18.09 ? 299 LYS   A CA  1 
ATOM   2367 C C   . LYS   A 1 298 ? 37.659  -36.200 7.027   1.00 17.37 ? 299 LYS   A C   1 
ATOM   2368 O O   . LYS   A 1 298 ? 37.437  -35.694 8.135   1.00 20.28 ? 299 LYS   A O   1 
ATOM   2369 C CB  . LYS   A 1 298 ? 40.101  -36.690 6.949   1.00 21.23 ? 299 LYS   A CB  1 
ATOM   2370 C CG  . LYS   A 1 298 ? 39.914  -38.193 6.954   1.00 23.74 ? 299 LYS   A CG  1 
ATOM   2371 C CD  . LYS   A 1 298 ? 40.154  -38.774 5.585   1.00 28.45 ? 299 LYS   A CD  1 
ATOM   2372 C CE  . LYS   A 1 298 ? 40.756  -40.182 5.673   1.00 33.99 ? 299 LYS   A CE  1 
ATOM   2373 N NZ  . LYS   A 1 298 ? 39.796  -41.152 6.278   1.00 38.32 ? 299 LYS   A NZ  1 
ATOM   2374 N N   . VAL   A 1 299 ? 36.792  -37.016 6.403   1.00 17.14 ? 300 VAL   A N   1 
ATOM   2375 C CA  . VAL   A 1 299 ? 35.534  -37.391 7.037   1.00 16.59 ? 300 VAL   A CA  1 
ATOM   2376 C C   . VAL   A 1 299 ? 35.734  -38.671 7.838   1.00 17.14 ? 300 VAL   A C   1 
ATOM   2377 O O   . VAL   A 1 299 ? 36.624  -39.493 7.568   1.00 18.60 ? 300 VAL   A O   1 
ATOM   2378 C CB  . VAL   A 1 299 ? 34.396  -37.542 6.003   1.00 16.12 ? 300 VAL   A CB  1 
ATOM   2379 C CG1 . VAL   A 1 299 ? 34.393  -36.347 5.045   1.00 15.79 ? 300 VAL   A CG1 1 
ATOM   2380 C CG2 . VAL   A 1 299 ? 34.495  -38.861 5.246   1.00 17.29 ? 300 VAL   A CG2 1 
ATOM   2381 N N   . THR   A 1 300 ? 34.906  -38.831 8.868   1.00 16.85 ? 301 THR   A N   1 
ATOM   2382 C CA  . THR   A 1 300 ? 34.858  -40.078 9.622   1.00 18.54 ? 301 THR   A CA  1 
ATOM   2383 C C   . THR   A 1 300 ? 33.429  -40.613 9.599   1.00 22.51 ? 301 THR   A C   1 
ATOM   2384 O O   . THR   A 1 300 ? 32.466  -39.847 9.642   1.00 19.16 ? 301 THR   A O   1 
ATOM   2385 C CB  . THR   A 1 300 ? 35.360  -39.901 11.062  1.00 23.16 ? 301 THR   A CB  1 
ATOM   2386 O OG1 . THR   A 1 300 ? 34.639  -38.857 11.716  1.00 27.80 ? 301 THR   A OG1 1 
ATOM   2387 C CG2 . THR   A 1 300 ? 36.825  -39.552 11.071  1.00 20.54 ? 301 THR   A CG2 1 
ATOM   2388 N N   . ALA   A 1 301 ? 33.296  -41.932 9.502   1.00 28.64 ? 302 ALA   A N   1 
ATOM   2389 C CA  . ALA   A 1 301 ? 31.970  -42.528 9.429   1.00 30.99 ? 302 ALA   A CA  1 
ATOM   2390 C C   . ALA   A 1 301 ? 31.253  -42.371 10.764  1.00 31.04 ? 302 ALA   A C   1 
ATOM   2391 O O   . ALA   A 1 301 ? 31.876  -42.318 11.826  1.00 31.65 ? 302 ALA   A O   1 
ATOM   2392 C CB  . ALA   A 1 301 ? 32.065  -44.007 9.046   1.00 37.48 ? 302 ALA   A CB  1 
ATOM   2393 N N   . ILE   A 1 302 ? 29.928  -42.270 10.703  1.00 32.84 ? 303 ILE   A N   1 
ATOM   2394 C CA  . ILE   A 1 302 ? 29.132  -42.104 11.914  1.00 39.17 ? 303 ILE   A CA  1 
ATOM   2395 C C   . ILE   A 1 302 ? 28.937  -43.459 12.581  1.00 48.05 ? 303 ILE   A C   1 
ATOM   2396 O O   . ILE   A 1 302 ? 28.461  -44.412 11.952  1.00 46.87 ? 303 ILE   A O   1 
ATOM   2397 C CB  . ILE   A 1 302 ? 27.782  -41.453 11.589  1.00 38.38 ? 303 ILE   A CB  1 
ATOM   2398 C CG1 . ILE   A 1 302 ? 27.985  -40.066 10.982  1.00 28.70 ? 303 ILE   A CG1 1 
ATOM   2399 C CG2 . ILE   A 1 302 ? 26.920  -41.366 12.840  1.00 46.16 ? 303 ILE   A CG2 1 
ATOM   2400 C CD1 . ILE   A 1 302 ? 26.703  -39.473 10.459  1.00 28.01 ? 303 ILE   A CD1 1 
ATOM   2401 N N   . SER   A 1 303 ? 29.304  -43.549 13.860  1.00 60.76 ? 304 SER   A N   1 
ATOM   2402 C CA  . SER   A 1 303 ? 29.042  -44.751 14.644  1.00 73.09 ? 304 SER   A CA  1 
ATOM   2403 C C   . SER   A 1 303 ? 27.539  -44.918 14.837  1.00 71.35 ? 304 SER   A C   1 
ATOM   2404 O O   . SER   A 1 303 ? 26.920  -45.809 14.244  1.00 69.00 ? 304 SER   A O   1 
ATOM   2405 C CB  . SER   A 1 303 ? 29.765  -44.683 15.994  1.00 68.90 ? 304 SER   A CB  1 
ATOM   2406 O OG  . SER   A 1 303 ? 29.543  -43.436 16.632  1.00 69.71 ? 304 SER   A OG  1 
ATOM   2407 N N   . LYS   A 1 304 ? 26.948  -44.064 15.667  1.00 62.54 ? 305 LYS   A N   1 
ATOM   2408 C CA  . LYS   A 1 304 ? 25.504  -43.910 15.748  1.00 61.81 ? 305 LYS   A CA  1 
ATOM   2409 C C   . LYS   A 1 304 ? 25.191  -42.422 15.714  1.00 57.07 ? 305 LYS   A C   1 
ATOM   2410 O O   . LYS   A 1 304 ? 25.932  -41.616 16.287  1.00 57.43 ? 305 LYS   A O   1 
ATOM   2411 C CB  . LYS   A 1 304 ? 24.927  -44.559 17.019  1.00 65.92 ? 305 LYS   A CB  1 
ATOM   2412 C CG  . LYS   A 1 304 ? 25.511  -44.028 18.320  1.00 64.29 ? 305 LYS   A CG  1 
ATOM   2413 C CD  . LYS   A 1 304 ? 24.701  -44.496 19.517  1.00 69.53 ? 305 LYS   A CD  1 
ATOM   2414 C CE  . LYS   A 1 304 ? 25.118  -43.773 20.792  1.00 74.70 ? 305 LYS   A CE  1 
ATOM   2415 N NZ  . LYS   A 1 304 ? 26.543  -44.018 21.148  1.00 76.09 ? 305 LYS   A NZ  1 
ATOM   2416 N N   . GLU   A 1 305 ? 24.117  -42.056 15.013  1.00 50.82 ? 306 GLU   A N   1 
ATOM   2417 C CA  . GLU   A 1 305 ? 23.746  -40.653 14.916  1.00 42.99 ? 306 GLU   A CA  1 
ATOM   2418 C C   . GLU   A 1 305 ? 23.415  -40.119 16.312  1.00 41.10 ? 306 GLU   A C   1 
ATOM   2419 O O   . GLU   A 1 305 ? 23.001  -40.885 17.190  1.00 39.99 ? 306 GLU   A O   1 
ATOM   2420 C CB  . GLU   A 1 305 ? 22.557  -40.474 13.969  1.00 45.33 ? 306 GLU   A CB  1 
ATOM   2421 C CG  . GLU   A 1 305 ? 22.822  -39.509 12.800  1.00 38.50 ? 306 GLU   A CG  1 
ATOM   2422 C CD  . GLU   A 1 305 ? 21.584  -39.230 11.959  1.00 37.07 ? 306 GLU   A CD  1 
ATOM   2423 O OE1 . GLU   A 1 305 ? 20.908  -40.197 11.534  1.00 44.46 ? 306 GLU   A OE1 1 
ATOM   2424 O OE2 . GLU   A 1 305 ? 21.271  -38.042 11.728  1.00 29.29 ? 306 GLU   A OE2 1 
ATOM   2425 N N   . PRO   A 1 306 ? 23.616  -38.819 16.560  1.00 35.67 ? 307 PRO   A N   1 
ATOM   2426 C CA  . PRO   A 1 306 ? 23.349  -38.289 17.904  1.00 33.79 ? 307 PRO   A CA  1 
ATOM   2427 C C   . PRO   A 1 306 ? 21.907  -38.548 18.303  1.00 27.62 ? 307 PRO   A C   1 
ATOM   2428 O O   . PRO   A 1 306 ? 20.996  -38.521 17.469  1.00 30.56 ? 307 PRO   A O   1 
ATOM   2429 C CB  . PRO   A 1 306 ? 23.631  -36.787 17.768  1.00 30.59 ? 307 PRO   A CB  1 
ATOM   2430 C CG  . PRO   A 1 306 ? 24.450  -36.650 16.547  1.00 33.89 ? 307 PRO   A CG  1 
ATOM   2431 C CD  . PRO   A 1 306 ? 24.032  -37.754 15.629  1.00 36.58 ? 307 PRO   A CD  1 
ATOM   2432 N N   . SER   A 1 307 ? 21.712  -38.824 19.593  1.00 27.29 ? 308 SER   A N   1 
ATOM   2433 C CA  . SER   A 1 307 ? 20.373  -39.095 20.101  1.00 25.92 ? 308 SER   A CA  1 
ATOM   2434 C C   . SER   A 1 307 ? 19.450  -37.886 19.932  1.00 29.76 ? 308 SER   A C   1 
ATOM   2435 O O   . SER   A 1 307 ? 18.279  -38.037 19.561  1.00 30.18 ? 308 SER   A O   1 
ATOM   2436 C CB  . SER   A 1 307 ? 20.471  -39.517 21.569  1.00 32.31 ? 308 SER   A CB  1 
ATOM   2437 O OG  . SER   A 1 307 ? 19.226  -39.414 22.229  1.00 42.53 ? 308 SER   A OG  1 
ATOM   2438 N N   . VAL   A 1 308 ? 19.944  -36.685 20.230  1.00 23.58 ? 309 VAL   A N   1 
ATOM   2439 C CA  . VAL   A 1 308 ? 19.167  -35.451 20.120  1.00 19.53 ? 309 VAL   A CA  1 
ATOM   2440 C C   . VAL   A 1 308 ? 19.959  -34.507 19.232  1.00 19.40 ? 309 VAL   A C   1 
ATOM   2441 O O   . VAL   A 1 308 ? 21.163  -34.329 19.447  1.00 17.35 ? 309 VAL   A O   1 
ATOM   2442 C CB  . VAL   A 1 308 ? 18.897  -34.798 21.496  1.00 20.90 ? 309 VAL   A CB  1 
ATOM   2443 C CG1 . VAL   A 1 308 ? 17.871  -33.681 21.356  1.00 23.65 ? 309 VAL   A CG1 1 
ATOM   2444 C CG2 . VAL   A 1 308 ? 18.426  -35.825 22.524  1.00 25.85 ? 309 VAL   A CG2 1 
ATOM   2445 N N   . LYS   A 1 309 ? 19.294  -33.908 18.233  1.00 17.40 ? 310 LYS   A N   1 
ATOM   2446 C CA  . LYS   A 1 309 ? 19.991  -33.200 17.165  1.00 16.78 ? 310 LYS   A CA  1 
ATOM   2447 C C   . LYS   A 1 309 ? 19.450  -31.786 16.984  1.00 17.95 ? 310 LYS   A C   1 
ATOM   2448 O O   . LYS   A 1 309 ? 18.305  -31.485 17.329  1.00 18.21 ? 310 LYS   A O   1 
ATOM   2449 C CB  . LYS   A 1 309 ? 19.852  -33.964 15.832  1.00 22.44 ? 310 LYS   A CB  1 
ATOM   2450 C CG  . LYS   A 1 309 ? 20.327  -35.422 15.915  1.00 26.22 ? 310 LYS   A CG  1 
ATOM   2451 C CD  . LYS   A 1 309 ? 19.631  -36.301 14.881  1.00 32.97 ? 310 LYS   A CD  1 
ATOM   2452 C CE  . LYS   A 1 309 ? 18.771  -37.381 15.507  1.00 37.46 ? 310 LYS   A CE  1 
ATOM   2453 N NZ  . LYS   A 1 309 ? 18.378  -38.383 14.469  1.00 38.63 ? 310 LYS   A NZ  1 
ATOM   2454 N N   . MET   A 1 310 ? 20.302  -30.914 16.429  1.00 17.23 ? 311 MET   A N   1 
ATOM   2455 C CA  . MET   A 1 310 ? 19.880  -29.622 15.895  1.00 15.28 ? 311 MET   A CA  1 
ATOM   2456 C C   . MET   A 1 310 ? 20.616  -29.381 14.586  1.00 16.45 ? 311 MET   A C   1 
ATOM   2457 O O   . MET   A 1 310 ? 21.592  -30.067 14.263  1.00 16.26 ? 311 MET   A O   1 
ATOM   2458 C CB  . MET   A 1 310 ? 20.148  -28.462 16.874  1.00 17.51 ? 311 MET   A CB  1 
ATOM   2459 C CG  . MET   A 1 310 ? 21.632  -28.161 17.071  1.00 17.24 ? 311 MET   A CG  1 
ATOM   2460 S SD  . MET   A 1 310 ? 21.943  -26.802 18.245  1.00 24.16 ? 311 MET   A SD  1 
ATOM   2461 C CE  . MET   A 1 310 ? 21.416  -25.405 17.276  1.00 24.30 ? 311 MET   A CE  1 
ATOM   2462 N N   . TYR   A 1 311 ? 20.149  -28.378 13.833  1.00 13.63 ? 312 TYR   A N   1 
ATOM   2463 C CA  . TYR   A 1 311 ? 20.587  -28.174 12.455  1.00 14.17 ? 312 TYR   A CA  1 
ATOM   2464 C C   . TYR   A 1 311 ? 20.729  -26.688 12.164  1.00 15.24 ? 312 TYR   A C   1 
ATOM   2465 O O   . TYR   A 1 311 ? 19.940  -25.874 12.651  1.00 14.98 ? 312 TYR   A O   1 
ATOM   2466 C CB  . TYR   A 1 311 ? 19.582  -28.768 11.448  1.00 15.86 ? 312 TYR   A CB  1 
ATOM   2467 C CG  . TYR   A 1 311 ? 19.319  -30.236 11.645  1.00 14.77 ? 312 TYR   A CG  1 
ATOM   2468 C CD1 . TYR   A 1 311 ? 18.393  -30.670 12.588  1.00 15.00 ? 312 TYR   A CD1 1 
ATOM   2469 C CD2 . TYR   A 1 311 ? 20.007  -31.187 10.897  1.00 15.05 ? 312 TYR   A CD2 1 
ATOM   2470 C CE1 . TYR   A 1 311 ? 18.163  -32.039 12.786  1.00 16.24 ? 312 TYR   A CE1 1 
ATOM   2471 C CE2 . TYR   A 1 311 ? 19.774  -32.547 11.077  1.00 14.67 ? 312 TYR   A CE2 1 
ATOM   2472 C CZ  . TYR   A 1 311 ? 18.856  -32.963 12.022  1.00 17.94 ? 312 TYR   A CZ  1 
ATOM   2473 O OH  . TYR   A 1 311 ? 18.634  -34.314 12.209  1.00 20.54 ? 312 TYR   A OH  1 
ATOM   2474 N N   . HIS   A 1 312 ? 21.691  -26.330 11.311  1.00 15.12 ? 313 HIS   A N   1 
ATOM   2475 C CA  . HIS   A 1 312 ? 21.714  -24.945 10.839  1.00 13.65 ? 313 HIS   A CA  1 
ATOM   2476 C C   . HIS   A 1 312 ? 22.360  -24.864 9.462   1.00 13.68 ? 313 HIS   A C   1 
ATOM   2477 O O   . HIS   A 1 312 ? 22.886  -25.845 8.933   1.00 14.94 ? 313 HIS   A O   1 
ATOM   2478 C CB  . HIS   A 1 312 ? 22.376  -23.991 11.875  1.00 15.04 ? 313 HIS   A CB  1 
ATOM   2479 C CG  . HIS   A 1 312 ? 23.885  -23.929 11.865  1.00 14.26 ? 313 HIS   A CG  1 
ATOM   2480 N ND1 . HIS   A 1 312 ? 24.578  -23.158 12.778  1.00 15.19 ? 313 HIS   A ND1 1 
ATOM   2481 C CD2 . HIS   A 1 312 ? 24.826  -24.485 11.058  1.00 16.06 ? 313 HIS   A CD2 1 
ATOM   2482 C CE1 . HIS   A 1 312 ? 25.876  -23.256 12.550  1.00 14.61 ? 313 HIS   A CE1 1 
ATOM   2483 N NE2 . HIS   A 1 312 ? 26.055  -24.060 11.512  1.00 16.40 ? 313 HIS   A NE2 1 
ATOM   2484 N N   . LYS   A 1 313 ? 22.286  -23.669 8.875   1.00 13.49 ? 314 LYS   A N   1 
ATOM   2485 C CA  . LYS   A 1 313 ? 22.987  -23.380 7.625   1.00 13.16 ? 314 LYS   A CA  1 
ATOM   2486 C C   . LYS   A 1 313 ? 23.159  -21.877 7.503   1.00 13.60 ? 314 LYS   A C   1 
ATOM   2487 O O   . LYS   A 1 313 ? 22.188  -21.134 7.686   1.00 15.27 ? 314 LYS   A O   1 
ATOM   2488 C CB  . LYS   A 1 313 ? 22.206  -23.911 6.406   1.00 13.63 ? 314 LYS   A CB  1 
ATOM   2489 C CG  . LYS   A 1 313 ? 22.913  -23.688 5.070   1.00 13.10 ? 314 LYS   A CG  1 
ATOM   2490 C CD  . LYS   A 1 313 ? 24.126  -24.643 4.902   1.00 14.57 ? 314 LYS   A CD  1 
ATOM   2491 C CE  . LYS   A 1 313 ? 24.751  -24.542 3.498   1.00 17.73 ? 314 LYS   A CE  1 
ATOM   2492 N NZ  . LYS   A 1 313 ? 25.872  -23.570 3.497   1.00 21.74 ? 314 LYS   A NZ  1 
ATOM   2493 N N   . THR   A 1 314 ? 24.388  -21.439 7.215   1.00 15.85 ? 315 THR   A N   1 
ATOM   2494 C CA  . THR   A 1 314 ? 24.675  -20.066 6.802   1.00 15.26 ? 315 THR   A CA  1 
ATOM   2495 C C   . THR   A 1 314 ? 24.676  -19.956 5.286   1.00 18.27 ? 315 THR   A C   1 
ATOM   2496 O O   . THR   A 1 314 ? 24.880  -20.927 4.565   1.00 20.38 ? 315 THR   A O   1 
ATOM   2497 C CB  . THR   A 1 314 ? 26.045  -19.589 7.297   1.00 20.08 ? 315 THR   A CB  1 
ATOM   2498 O OG1 . THR   A 1 314 ? 27.068  -20.420 6.735   1.00 21.09 ? 315 THR   A OG1 1 
ATOM   2499 C CG2 . THR   A 1 314 ? 26.129  -19.638 8.791   1.00 22.28 ? 315 THR   A CG2 1 
ATOM   2500 N N   . GLY   A 1 315 ? 24.488  -18.740 4.802   1.00 17.03 ? 316 GLY   A N   1 
ATOM   2501 C CA  . GLY   A 1 315 ? 24.707  -18.536 3.385   1.00 17.35 ? 316 GLY   A CA  1 
ATOM   2502 C C   . GLY   A 1 315 ? 24.698  -17.074 3.026   1.00 19.39 ? 316 GLY   A C   1 
ATOM   2503 O O   . GLY   A 1 315 ? 24.036  -16.276 3.693   1.00 21.08 ? 316 GLY   A O   1 
ATOM   2504 N N   . SER   A 1 316 ? 25.421  -16.703 1.974   1.00 18.87 ? 317 SER   A N   1 
ATOM   2505 C CA  . SER   A 1 316 ? 25.450  -15.325 1.518   1.00 21.08 ? 317 SER   A CA  1 
ATOM   2506 C C   . SER   A 1 316 ? 25.536  -15.286 -0.001  1.00 22.25 ? 317 SER   A C   1 
ATOM   2507 O O   . SER   A 1 316 ? 25.803  -16.291 -0.662  1.00 19.61 ? 317 SER   A O   1 
ATOM   2508 C CB  . SER   A 1 316 ? 26.653  -14.561 2.101   1.00 23.27 ? 317 SER   A CB  1 
ATOM   2509 O OG  . SER   A 1 316 ? 26.694  -14.676 3.515   1.00 24.57 ? 317 SER   A OG  1 
ATOM   2510 N N   . THR   A 1 317 ? 25.314  -14.103 -0.543  1.00 22.91 ? 318 THR   A N   1 
ATOM   2511 C CA  . THR   A 1 317 ? 25.862  -13.694 -1.829  1.00 21.68 ? 318 THR   A CA  1 
ATOM   2512 C C   . THR   A 1 317 ? 26.821  -12.547 -1.540  1.00 26.26 ? 318 THR   A C   1 
ATOM   2513 O O   . THR   A 1 317 ? 27.069  -12.214 -0.382  1.00 30.92 ? 318 THR   A O   1 
ATOM   2514 C CB  . THR   A 1 317 ? 24.762  -13.285 -2.811  1.00 25.12 ? 318 THR   A CB  1 
ATOM   2515 O OG1 . THR   A 1 317 ? 24.166  -12.054 -2.376  1.00 27.57 ? 318 THR   A OG1 1 
ATOM   2516 C CG2 . THR   A 1 317 ? 23.696  -14.375 -2.916  1.00 21.59 ? 318 THR   A CG2 1 
ATOM   2517 N N   . ASN   A 1 318 ? 27.355  -11.920 -2.583  1.00 30.73 ? 319 ASN   A N   1 
ATOM   2518 C CA  . ASN   A 1 318 ? 28.211  -10.776 -2.300  1.00 31.87 ? 319 ASN   A CA  1 
ATOM   2519 C C   . ASN   A 1 318 ? 27.448  -9.642  -1.628  1.00 33.02 ? 319 ASN   A C   1 
ATOM   2520 O O   . ASN   A 1 318 ? 28.081  -8.743  -1.062  1.00 34.51 ? 319 ASN   A O   1 
ATOM   2521 C CB  . ASN   A 1 318 ? 28.878  -10.284 -3.583  1.00 37.50 ? 319 ASN   A CB  1 
ATOM   2522 C CG  . ASN   A 1 318 ? 29.903  -11.265 -4.114  1.00 45.08 ? 319 ASN   A CG  1 
ATOM   2523 O OD1 . ASN   A 1 318 ? 30.615  -11.916 -3.344  1.00 48.00 ? 319 ASN   A OD1 1 
ATOM   2524 N ND2 . ASN   A 1 318 ? 29.979  -11.385 -5.434  1.00 48.22 ? 319 ASN   A ND2 1 
ATOM   2525 N N   . ARG   A 1 319 ? 26.113  -9.692  -1.628  1.00 30.23 ? 320 ARG   A N   1 
ATOM   2526 C CA  . ARG   A 1 319 ? 25.309  -8.566  -1.174  1.00 31.43 ? 320 ARG   A CA  1 
ATOM   2527 C C   . ARG   A 1 319 ? 24.106  -8.953  -0.312  1.00 23.99 ? 320 ARG   A C   1 
ATOM   2528 O O   . ARG   A 1 319 ? 23.300  -8.074  0.013   1.00 26.90 ? 320 ARG   A O   1 
ATOM   2529 C CB  . ARG   A 1 319 ? 24.836  -7.796  -2.391  1.00 34.44 ? 320 ARG   A CB  1 
ATOM   2530 C CG  . ARG   A 1 319 ? 24.389  -8.732  -3.489  1.00 41.84 ? 320 ARG   A CG  1 
ATOM   2531 C CD  . ARG   A 1 319 ? 24.720  -8.195  -4.882  1.00 53.56 ? 320 ARG   A CD  1 
ATOM   2532 N NE  . ARG   A 1 319 ? 23.842  -8.822  -5.863  1.00 56.65 ? 320 ARG   A NE  1 
ATOM   2533 C CZ  . ARG   A 1 319 ? 22.571  -8.489  -6.040  1.00 55.70 ? 320 ARG   A CZ  1 
ATOM   2534 N NH1 . ARG   A 1 319 ? 22.019  -7.485  -5.373  1.00 54.76 ? 320 ARG   A NH1 1 
ATOM   2535 N NH2 . ARG   A 1 319 ? 21.830  -9.183  -6.900  1.00 59.34 ? 320 ARG   A NH2 1 
ATOM   2536 N N   . PHE   A 1 320 ? 23.952  -10.224 0.067   1.00 23.99 ? 321 PHE   A N   1 
ATOM   2537 C CA  . PHE   A 1 320 ? 22.878  -10.668 0.950   1.00 18.99 ? 321 PHE   A CA  1 
ATOM   2538 C C   . PHE   A 1 320 ? 23.457  -11.623 1.988   1.00 21.48 ? 321 PHE   A C   1 
ATOM   2539 O O   . PHE   A 1 320 ? 24.464  -12.291 1.733   1.00 22.36 ? 321 PHE   A O   1 
ATOM   2540 C CB  . PHE   A 1 320 ? 21.747  -11.401 0.186   1.00 19.59 ? 321 PHE   A CB  1 
ATOM   2541 C CG  . PHE   A 1 320 ? 20.808  -10.493 -0.552  1.00 20.58 ? 321 PHE   A CG  1 
ATOM   2542 C CD1 . PHE   A 1 320 ? 21.072  -10.108 -1.860  1.00 22.25 ? 321 PHE   A CD1 1 
ATOM   2543 C CD2 . PHE   A 1 320 ? 19.638  -10.069 0.043   1.00 21.72 ? 321 PHE   A CD2 1 
ATOM   2544 C CE1 . PHE   A 1 320 ? 20.195  -9.285  -2.549  1.00 24.65 ? 321 PHE   A CE1 1 
ATOM   2545 C CE2 . PHE   A 1 320 ? 18.757  -9.243  -0.638  1.00 21.83 ? 321 PHE   A CE2 1 
ATOM   2546 C CZ  . PHE   A 1 320 ? 19.037  -8.857  -1.942  1.00 24.01 ? 321 PHE   A CZ  1 
ATOM   2547 N N   . GLY   A 1 321 ? 22.812  -11.699 3.150   1.00 19.74 ? 322 GLY   A N   1 
ATOM   2548 C CA  . GLY   A 1 321 ? 23.175  -12.677 4.163   1.00 20.20 ? 322 GLY   A CA  1 
ATOM   2549 C C   . GLY   A 1 321 ? 21.955  -13.436 4.652   1.00 18.09 ? 322 GLY   A C   1 
ATOM   2550 O O   . GLY   A 1 321 ? 20.841  -12.913 4.672   1.00 20.29 ? 322 GLY   A O   1 
ATOM   2551 N N   . THR   A 1 322 ? 22.180  -14.699 5.038   1.00 16.95 ? 323 THR   A N   1 
ATOM   2552 C CA  . THR   A 1 322 ? 21.104  -15.578 5.499   1.00 14.26 ? 323 THR   A CA  1 
ATOM   2553 C C   . THR   A 1 322 ? 21.631  -16.474 6.610   1.00 16.33 ? 323 THR   A C   1 
ATOM   2554 O O   . THR   A 1 322 ? 22.802  -16.869 6.607   1.00 17.66 ? 323 THR   A O   1 
ATOM   2555 C CB  . THR   A 1 322 ? 20.526  -16.478 4.360   1.00 16.09 ? 323 THR   A CB  1 
ATOM   2556 O OG1 . THR   A 1 322 ? 20.161  -15.660 3.243   1.00 19.92 ? 323 THR   A OG1 1 
ATOM   2557 C CG2 . THR   A 1 322 ? 19.283  -17.244 4.824   1.00 17.91 ? 323 THR   A CG2 1 
ATOM   2558 N N   . TYR   A 1 323 ? 20.746  -16.811 7.552   1.00 14.46 ? 324 TYR   A N   1 
ATOM   2559 C CA  . TYR   A 1 323 ? 21.040  -17.845 8.535   1.00 15.23 ? 324 TYR   A CA  1 
ATOM   2560 C C   . TYR   A 1 323 ? 19.744  -18.520 8.946   1.00 15.10 ? 324 TYR   A C   1 
ATOM   2561 O O   . TYR   A 1 323 ? 18.727  -17.852 9.152   1.00 16.83 ? 324 TYR   A O   1 
ATOM   2562 C CB  . TYR   A 1 323 ? 21.739  -17.271 9.776   1.00 15.27 ? 324 TYR   A CB  1 
ATOM   2563 C CG  . TYR   A 1 323 ? 22.118  -18.308 10.820  1.00 14.59 ? 324 TYR   A CG  1 
ATOM   2564 C CD1 . TYR   A 1 323 ? 23.081  -19.276 10.556  1.00 20.68 ? 324 TYR   A CD1 1 
ATOM   2565 C CD2 . TYR   A 1 323 ? 21.520  -18.303 12.071  1.00 15.10 ? 324 TYR   A CD2 1 
ATOM   2566 C CE1 . TYR   A 1 323 ? 23.436  -20.228 11.522  1.00 16.18 ? 324 TYR   A CE1 1 
ATOM   2567 C CE2 . TYR   A 1 323 ? 21.869  -19.230 13.040  1.00 16.61 ? 324 TYR   A CE2 1 
ATOM   2568 C CZ  . TYR   A 1 323 ? 22.813  -20.191 12.766  1.00 14.88 ? 324 TYR   A CZ  1 
ATOM   2569 O OH  . TYR   A 1 323 ? 23.133  -21.097 13.758  1.00 15.26 ? 324 TYR   A OH  1 
ATOM   2570 N N   . VAL   A 1 324 ? 19.782  -19.845 9.058   1.00 14.39 ? 325 VAL   A N   1 
ATOM   2571 C CA  A VAL   A 1 324 ? 18.621  -20.615 9.499   0.62 15.62 ? 325 VAL   A CA  1 
ATOM   2572 C CA  B VAL   A 1 324 ? 18.631  -20.652 9.445   0.38 15.59 ? 325 VAL   A CA  1 
ATOM   2573 C C   . VAL   A 1 324 ? 19.081  -21.692 10.462  1.00 15.52 ? 325 VAL   A C   1 
ATOM   2574 O O   . VAL   A 1 324 ? 20.132  -22.318 10.281  1.00 16.62 ? 325 VAL   A O   1 
ATOM   2575 C CB  A VAL   A 1 324 ? 17.833  -21.247 8.327   0.62 15.36 ? 325 VAL   A CB  1 
ATOM   2576 C CB  B VAL   A 1 324 ? 18.012  -21.349 8.217   0.38 15.50 ? 325 VAL   A CB  1 
ATOM   2577 C CG1 A VAL   A 1 324 ? 17.166  -20.174 7.481   0.62 16.93 ? 325 VAL   A CG1 1 
ATOM   2578 C CG1 B VAL   A 1 324 ? 16.860  -22.138 8.643   0.38 15.27 ? 325 VAL   A CG1 1 
ATOM   2579 C CG2 A VAL   A 1 324 ? 18.745  -22.123 7.483   0.62 15.31 ? 325 VAL   A CG2 1 
ATOM   2580 C CG2 B VAL   A 1 324 ? 17.605  -20.346 7.152   0.38 16.92 ? 325 VAL   A CG2 1 
ATOM   2581 N N   . VAL   A 1 325 ? 18.281  -21.903 11.507  1.00 14.78 ? 326 VAL   A N   1 
ATOM   2582 C CA  . VAL   A 1 325 ? 18.618  -22.874 12.545  1.00 14.50 ? 326 VAL   A CA  1 
ATOM   2583 C C   . VAL   A 1 325 ? 17.321  -23.411 13.138  1.00 15.91 ? 326 VAL   A C   1 
ATOM   2584 O O   . VAL   A 1 325 ? 16.331  -22.686 13.259  1.00 16.90 ? 326 VAL   A O   1 
ATOM   2585 C CB  . VAL   A 1 325 ? 19.531  -22.229 13.626  1.00 13.67 ? 326 VAL   A CB  1 
ATOM   2586 C CG1 . VAL   A 1 325 ? 18.876  -20.960 14.229  1.00 15.71 ? 326 VAL   A CG1 1 
ATOM   2587 C CG2 . VAL   A 1 325 ? 19.922  -23.239 14.729  1.00 15.71 ? 326 VAL   A CG2 1 
ATOM   2588 N N   . PHE   A 1 326 ? 17.320  -24.695 13.514  1.00 15.53 ? 327 PHE   A N   1 
ATOM   2589 C CA  . PHE   A 1 326 ? 16.143  -25.235 14.189  1.00 14.72 ? 327 PHE   A CA  1 
ATOM   2590 C C   . PHE   A 1 326 ? 16.541  -26.363 15.133  1.00 17.56 ? 327 PHE   A C   1 
ATOM   2591 O O   . PHE   A 1 326 ? 17.579  -27.019 14.964  1.00 16.73 ? 327 PHE   A O   1 
ATOM   2592 C CB  . PHE   A 1 326 ? 15.043  -25.685 13.191  1.00 15.94 ? 327 PHE   A CB  1 
ATOM   2593 C CG  . PHE   A 1 326 ? 15.356  -26.945 12.389  1.00 14.79 ? 327 PHE   A CG  1 
ATOM   2594 C CD1 . PHE   A 1 326 ? 16.093  -26.873 11.205  1.00 15.36 ? 327 PHE   A CD1 1 
ATOM   2595 C CD2 . PHE   A 1 326 ? 14.849  -28.179 12.779  1.00 15.30 ? 327 PHE   A CD2 1 
ATOM   2596 C CE1 . PHE   A 1 326 ? 16.340  -28.021 10.437  1.00 16.40 ? 327 PHE   A CE1 1 
ATOM   2597 C CE2 . PHE   A 1 326 ? 15.111  -29.344 12.030  1.00 16.27 ? 327 PHE   A CE2 1 
ATOM   2598 C CZ  . PHE   A 1 326 ? 15.849  -29.263 10.866  1.00 14.82 ? 327 PHE   A CZ  1 
ATOM   2599 N N   . ILE   A 1 327 ? 15.694  -26.563 16.144  1.00 15.99 ? 328 ILE   A N   1 
ATOM   2600 C CA  . ILE   A 1 327 ? 15.919  -27.515 17.234  1.00 17.05 ? 328 ILE   A CA  1 
ATOM   2601 C C   . ILE   A 1 327 ? 14.664  -28.369 17.408  1.00 17.48 ? 328 ILE   A C   1 
ATOM   2602 O O   . ILE   A 1 327 ? 13.687  -27.927 18.034  1.00 19.94 ? 328 ILE   A O   1 
ATOM   2603 C CB  . ILE   A 1 327 ? 16.264  -26.801 18.549  1.00 17.88 ? 328 ILE   A CB  1 
ATOM   2604 C CG1 . ILE   A 1 327 ? 17.429  -25.819 18.376  1.00 17.28 ? 328 ILE   A CG1 1 
ATOM   2605 C CG2 . ILE   A 1 327 ? 16.557  -27.844 19.616  1.00 21.38 ? 328 ILE   A CG2 1 
ATOM   2606 C CD1 . ILE   A 1 327 ? 17.616  -24.857 19.577  1.00 20.98 ? 328 ILE   A CD1 1 
ATOM   2607 N N   . PRO   A 1 328 ? 14.644  -29.578 16.865  1.00 19.47 ? 329 PRO   A N   1 
ATOM   2608 C CA  . PRO   A 1 328 ? 13.416  -30.397 16.907  1.00 20.55 ? 329 PRO   A CA  1 
ATOM   2609 C C   . PRO   A 1 328 ? 12.832  -30.587 18.298  1.00 23.07 ? 329 PRO   A C   1 
ATOM   2610 O O   . PRO   A 1 328 ? 11.606  -30.475 18.464  1.00 24.30 ? 329 PRO   A O   1 
ATOM   2611 C CB  . PRO   A 1 328 ? 13.888  -31.725 16.302  1.00 23.50 ? 329 PRO   A CB  1 
ATOM   2612 C CG  . PRO   A 1 328 ? 14.945  -31.317 15.338  1.00 21.50 ? 329 PRO   A CG  1 
ATOM   2613 C CD  . PRO   A 1 328 ? 15.647  -30.115 15.930  1.00 16.88 ? 329 PRO   A CD  1 
ATOM   2614 N N   . LYS   A 1 329 ? 13.672  -30.850 19.303  1.00 23.54 ? 330 LYS   A N   1 
ATOM   2615 C CA  . LYS   A 1 329 ? 13.163  -31.168 20.633  1.00 26.07 ? 330 LYS   A CA  1 
ATOM   2616 C C   . LYS   A 1 329 ? 12.428  -29.993 21.252  1.00 26.73 ? 330 LYS   A C   1 
ATOM   2617 O O   . LYS   A 1 329 ? 11.504  -30.186 22.054  1.00 26.09 ? 330 LYS   A O   1 
ATOM   2618 C CB  . LYS   A 1 329 ? 14.302  -31.596 21.554  1.00 26.04 ? 330 LYS   A CB  1 
ATOM   2619 C CG  . LYS   A 1 329 ? 13.797  -32.024 22.920  1.00 27.83 ? 330 LYS   A CG  1 
ATOM   2620 C CD  . LYS   A 1 329 ? 14.877  -32.538 23.819  1.00 29.07 ? 330 LYS   A CD  1 
ATOM   2621 C CE  . LYS   A 1 329 ? 14.255  -32.884 25.169  1.00 33.23 ? 330 LYS   A CE  1 
ATOM   2622 N NZ  . LYS   A 1 329 ? 15.128  -33.711 26.025  1.00 36.57 ? 330 LYS   A NZ  1 
ATOM   2623 N N   . GLU   A 1 330 ? 12.828  -28.778 20.905  1.00 23.84 ? 331 GLU   A N   1 
ATOM   2624 C CA  . GLU   A 1 330 ? 12.225  -27.578 21.457  1.00 26.93 ? 331 GLU   A CA  1 
ATOM   2625 C C   . GLU   A 1 330 ? 11.170  -26.993 20.535  1.00 23.97 ? 331 GLU   A C   1 
ATOM   2626 O O   . GLU   A 1 330 ? 10.591  -25.950 20.863  1.00 25.75 ? 331 GLU   A O   1 
ATOM   2627 C CB  . GLU   A 1 330 ? 13.309  -26.536 21.734  1.00 28.26 ? 331 GLU   A CB  1 
ATOM   2628 C CG  . GLU   A 1 330 ? 14.575  -27.105 22.338  1.00 33.95 ? 331 GLU   A CG  1 
ATOM   2629 C CD  . GLU   A 1 330 ? 14.584  -27.082 23.834  1.00 36.75 ? 331 GLU   A CD  1 
ATOM   2630 O OE1 . GLU   A 1 330 ? 13.496  -27.116 24.451  1.00 46.04 ? 331 GLU   A OE1 1 
ATOM   2631 O OE2 . GLU   A 1 330 ? 15.692  -27.024 24.402  1.00 40.29 ? 331 GLU   A OE2 1 
ATOM   2632 N N   . ASN   A 1 331 ? 10.905  -27.649 19.403  1.00 20.09 ? 332 ASN   A N   1 
ATOM   2633 C CA  . ASN   A 1 331 ? 9.905   -27.214 18.430  1.00 21.10 ? 332 ASN   A CA  1 
ATOM   2634 C C   . ASN   A 1 331 ? 10.078  -25.736 18.085  1.00 23.43 ? 332 ASN   A C   1 
ATOM   2635 O O   . ASN   A 1 331 ? 9.124   -24.950 18.085  1.00 24.47 ? 332 ASN   A O   1 
ATOM   2636 C CB  . ASN   A 1 331 ? 8.491   -27.488 18.948  1.00 30.13 ? 332 ASN   A CB  1 
ATOM   2637 C CG  . ASN   A 1 331 ? 8.240   -28.959 19.200  1.00 29.10 ? 332 ASN   A CG  1 
ATOM   2638 O OD1 . ASN   A 1 331 ? 8.088   -29.387 20.346  1.00 40.31 ? 332 ASN   A OD1 1 
ATOM   2639 N ND2 . ASN   A 1 331 ? 8.171   -29.740 18.126  1.00 37.76 ? 332 ASN   A ND2 1 
ATOM   2640 N N   . ILE   A 1 332 ? 11.321  -25.353 17.805  1.00 20.18 ? 333 ILE   A N   1 
ATOM   2641 C CA  . ILE   A 1 332 ? 11.674  -23.952 17.600  1.00 21.40 ? 333 ILE   A CA  1 
ATOM   2642 C C   . ILE   A 1 332 ? 12.698  -23.806 16.480  1.00 21.14 ? 333 ILE   A C   1 
ATOM   2643 O O   . ILE   A 1 332 ? 13.528  -24.688 16.236  1.00 18.61 ? 333 ILE   A O   1 
ATOM   2644 C CB  . ILE   A 1 332 ? 12.190  -23.313 18.912  1.00 21.09 ? 333 ILE   A CB  1 
ATOM   2645 C CG1 . ILE   A 1 332 ? 12.172  -21.787 18.812  1.00 22.39 ? 333 ILE   A CG1 1 
ATOM   2646 C CG2 . ILE   A 1 332 ? 13.599  -23.827 19.274  1.00 19.98 ? 333 ILE   A CG2 1 
ATOM   2647 C CD1 . ILE   A 1 332 ? 12.263  -21.088 20.164  1.00 24.46 ? 333 ILE   A CD1 1 
ATOM   2648 N N   . GLY   A 1 333 ? 12.642  -22.664 15.798  1.00 18.89 ? 334 GLY   A N   1 
ATOM   2649 C CA  . GLY   A 1 333 ? 13.622  -22.361 14.768  1.00 16.35 ? 334 GLY   A CA  1 
ATOM   2650 C C   . GLY   A 1 333 ? 13.650  -20.871 14.516  1.00 17.38 ? 334 GLY   A C   1 
ATOM   2651 O O   . GLY   A 1 333 ? 12.767  -20.133 14.952  1.00 18.73 ? 334 GLY   A O   1 
ATOM   2652 N N   . LEU   A 1 334 ? 14.686  -20.433 13.793  1.00 17.49 ? 335 LEU   A N   1 
ATOM   2653 C CA  . LEU   A 1 334 ? 14.894  -19.011 13.551  1.00 17.49 ? 335 LEU   A CA  1 
ATOM   2654 C C   . LEU   A 1 334 ? 15.485  -18.807 12.159  1.00 16.91 ? 335 LEU   A C   1 
ATOM   2655 O O   . LEU   A 1 334 ? 16.280  -19.621 11.684  1.00 16.34 ? 335 LEU   A O   1 
ATOM   2656 C CB  . LEU   A 1 334 ? 15.815  -18.414 14.618  1.00 19.00 ? 335 LEU   A CB  1 
ATOM   2657 C CG  . LEU   A 1 334 ? 16.154  -16.920 14.514  1.00 19.99 ? 335 LEU   A CG  1 
ATOM   2658 C CD1 . LEU   A 1 334 ? 16.358  -16.336 15.899  1.00 19.88 ? 335 LEU   A CD1 1 
ATOM   2659 C CD2 . LEU   A 1 334 ? 17.428  -16.717 13.669  1.00 18.94 ? 335 LEU   A CD2 1 
ATOM   2660 N N   . VAL   A 1 335 ? 15.102  -17.689 11.521  1.00 14.97 ? 336 VAL   A N   1 
ATOM   2661 C CA  A VAL   A 1 335 ? 15.566  -17.298 10.189  0.71 17.32 ? 336 VAL   A CA  1 
ATOM   2662 C CA  B VAL   A 1 335 ? 15.622  -17.312 10.216  0.29 17.06 ? 336 VAL   A CA  1 
ATOM   2663 C C   . VAL   A 1 335 ? 16.002  -15.843 10.254  1.00 17.01 ? 336 VAL   A C   1 
ATOM   2664 O O   . VAL   A 1 335 ? 15.262  -15.006 10.784  1.00 17.32 ? 336 VAL   A O   1 
ATOM   2665 C CB  A VAL   A 1 335 ? 14.473  -17.436 9.111   0.71 18.84 ? 336 VAL   A CB  1 
ATOM   2666 C CB  B VAL   A 1 335 ? 14.616  -17.582 9.077   0.29 18.64 ? 336 VAL   A CB  1 
ATOM   2667 C CG1 A VAL   A 1 335 ? 15.056  -17.107 7.715   0.71 15.55 ? 336 VAL   A CG1 1 
ATOM   2668 C CG1 B VAL   A 1 335 ? 14.648  -19.038 8.683   0.29 18.94 ? 336 VAL   A CG1 1 
ATOM   2669 C CG2 A VAL   A 1 335 ? 13.811  -18.813 9.150   0.71 19.34 ? 336 VAL   A CG2 1 
ATOM   2670 C CG2 B VAL   A 1 335 ? 13.219  -17.189 9.493   0.29 15.67 ? 336 VAL   A CG2 1 
ATOM   2671 N N   . MET   A 1 336 ? 17.177  -15.537 9.703   1.00 16.10 ? 337 MET   A N   1 
ATOM   2672 C CA  . MET   A 1 336 ? 17.637  -14.163 9.535   1.00 16.63 ? 337 MET   A CA  1 
ATOM   2673 C C   . MET   A 1 336 ? 17.929  -13.927 8.060   1.00 18.23 ? 337 MET   A C   1 
ATOM   2674 O O   . MET   A 1 336 ? 18.634  -14.723 7.432   1.00 17.28 ? 337 MET   A O   1 
ATOM   2675 C CB  . MET   A 1 336 ? 18.895  -13.870 10.375  1.00 18.24 ? 337 MET   A CB  1 
ATOM   2676 C CG  . MET   A 1 336 ? 19.346  -12.397 10.318  1.00 17.98 ? 337 MET   A CG  1 
ATOM   2677 S SD  . MET   A 1 336 ? 21.136  -12.145 10.240  1.00 23.21 ? 337 MET   A SD  1 
ATOM   2678 C CE  . MET   A 1 336 ? 21.555  -12.795 8.574   1.00 18.59 ? 337 MET   A CE  1 
ATOM   2679 N N   . LEU   A 1 337 ? 17.380  -12.839 7.510   1.00 16.98 ? 338 LEU   A N   1 
ATOM   2680 C CA  . LEU   A 1 337 ? 17.661  -12.392 6.147   1.00 17.36 ? 338 LEU   A CA  1 
ATOM   2681 C C   . LEU   A 1 337 ? 18.148  -10.946 6.188   1.00 19.51 ? 338 LEU   A C   1 
ATOM   2682 O O   . LEU   A 1 337 ? 17.543  -10.113 6.869   1.00 20.22 ? 338 LEU   A O   1 
ATOM   2683 C CB  . LEU   A 1 337 ? 16.407  -12.483 5.270   1.00 17.30 ? 338 LEU   A CB  1 
ATOM   2684 C CG  . LEU   A 1 337 ? 15.659  -13.809 5.376   1.00 17.15 ? 338 LEU   A CG  1 
ATOM   2685 C CD1 . LEU   A 1 337 ? 14.348  -13.699 4.598   1.00 20.52 ? 338 LEU   A CD1 1 
ATOM   2686 C CD2 . LEU   A 1 337 ? 16.496  -14.936 4.830   1.00 18.31 ? 338 LEU   A CD2 1 
ATOM   2687 N N   . THR   A 1 338 ? 19.233  -10.640 5.466   1.00 19.52 ? 339 THR   A N   1 
ATOM   2688 C CA  . THR   A 1 338 ? 19.731  -9.265  5.359   1.00 18.44 ? 339 THR   A CA  1 
ATOM   2689 C C   . THR   A 1 338 ? 20.096  -8.960  3.916   1.00 20.34 ? 339 THR   A C   1 
ATOM   2690 O O   . THR   A 1 338 ? 20.490  -9.855  3.172   1.00 19.95 ? 339 THR   A O   1 
ATOM   2691 C CB  . THR   A 1 338 ? 20.973  -9.001  6.237   1.00 22.83 ? 339 THR   A CB  1 
ATOM   2692 O OG1 . THR   A 1 338 ? 22.040  -9.886  5.850   1.00 23.12 ? 339 THR   A OG1 1 
ATOM   2693 C CG2 . THR   A 1 338 ? 20.655  -9.205  7.705   1.00 21.52 ? 339 THR   A CG2 1 
ATOM   2694 N N   . ASN   A 1 339 ? 19.994  -7.681  3.522   1.00 19.64 ? 340 ASN   A N   1 
ATOM   2695 C CA  . ASN   A 1 339 ? 20.410  -7.279  2.178   1.00 21.40 ? 340 ASN   A CA  1 
ATOM   2696 C C   . ASN   A 1 339 ? 21.780  -6.605  2.186   1.00 23.12 ? 340 ASN   A C   1 
ATOM   2697 O O   . ASN   A 1 339 ? 22.053  -5.715  1.377   1.00 24.54 ? 340 ASN   A O   1 
ATOM   2698 C CB  . ASN   A 1 339 ? 19.357  -6.403  1.487   1.00 22.71 ? 340 ASN   A CB  1 
ATOM   2699 C CG  . ASN   A 1 339 ? 19.038  -5.135  2.244   1.00 20.49 ? 340 ASN   A CG  1 
ATOM   2700 O OD1 . ASN   A 1 339 ? 19.574  -4.879  3.321   1.00 22.56 ? 340 ASN   A OD1 1 
ATOM   2701 N ND2 . ASN   A 1 339 ? 18.169  -4.305  1.660   1.00 23.48 ? 340 ASN   A ND2 1 
ATOM   2702 N N   . LYS   A 1 340 ? 22.642  -7.045  3.102   1.00 21.43 ? 341 LYS   A N   1 
ATOM   2703 C CA  . LYS   A 1 340 ? 24.071  -6.778  3.104   1.00 22.39 ? 341 LYS   A CA  1 
ATOM   2704 C C   . LYS   A 1 340 ? 24.711  -7.908  3.899   1.00 23.92 ? 341 LYS   A C   1 
ATOM   2705 O O   . LYS   A 1 340 ? 24.118  -8.394  4.868   1.00 24.82 ? 341 LYS   A O   1 
ATOM   2706 C CB  . LYS   A 1 340 ? 24.393  -5.408  3.722   1.00 24.94 ? 341 LYS   A CB  1 
ATOM   2707 C CG  . LYS   A 1 340 ? 25.849  -5.001  3.552   1.00 27.07 ? 341 LYS   A CG  1 
ATOM   2708 C CD  . LYS   A 1 340 ? 26.153  -3.686  4.238   1.00 31.91 ? 341 LYS   A CD  1 
ATOM   2709 C CE  . LYS   A 1 340 ? 27.631  -3.353  4.106   1.00 40.04 ? 341 LYS   A CE  1 
ATOM   2710 N NZ  . LYS   A 1 340 ? 27.975  -2.074  4.789   1.00 44.00 ? 341 LYS   A NZ  1 
ATOM   2711 N N   . ARG   A 1 341 ? 25.894  -8.352  3.478   1.00 25.30 ? 342 ARG   A N   1 
ATOM   2712 C CA  . ARG   A 1 341 ? 26.575  -9.398  4.235   1.00 25.25 ? 342 ARG   A CA  1 
ATOM   2713 C C   . ARG   A 1 341 ? 26.970  -8.898  5.614   1.00 27.71 ? 342 ARG   A C   1 
ATOM   2714 O O   . ARG   A 1 341 ? 27.403  -7.757  5.779   1.00 30.27 ? 342 ARG   A O   1 
ATOM   2715 C CB  . ARG   A 1 341 ? 27.828  -9.888  3.515   1.00 30.24 ? 342 ARG   A CB  1 
ATOM   2716 C CG  . ARG   A 1 341 ? 27.548  -10.796 2.356   1.00 31.98 ? 342 ARG   A CG  1 
ATOM   2717 C CD  . ARG   A 1 341 ? 28.736  -11.698 1.979   1.00 38.81 ? 342 ARG   A CD  1 
ATOM   2718 N NE  . ARG   A 1 341 ? 30.045  -11.263 2.447   1.00 42.99 ? 342 ARG   A NE  1 
ATOM   2719 C CZ  . ARG   A 1 341 ? 30.715  -10.229 1.959   1.00 47.21 ? 342 ARG   A CZ  1 
ATOM   2720 N NH1 . ARG   A 1 341 ? 30.163  -9.394  1.091   1.00 50.40 ? 342 ARG   A NH1 1 
ATOM   2721 N NH2 . ARG   A 1 341 ? 31.971  -10.030 2.350   1.00 47.99 ? 342 ARG   A NH2 1 
ATOM   2722 N N   . ILE   A 1 342 ? 26.824  -9.765  6.609   1.00 24.12 ? 343 ILE   A N   1 
ATOM   2723 C CA  . ILE   A 1 342 ? 27.474  -9.541  7.895   1.00 24.86 ? 343 ILE   A CA  1 
ATOM   2724 C C   . ILE   A 1 342 ? 28.216  -10.820 8.262   1.00 20.96 ? 343 ILE   A C   1 
ATOM   2725 O O   . ILE   A 1 342 ? 27.898  -11.901 7.747   1.00 23.39 ? 343 ILE   A O   1 
ATOM   2726 C CB  . ILE   A 1 342 ? 26.465  -9.140  8.996   1.00 29.90 ? 343 ILE   A CB  1 
ATOM   2727 C CG1 . ILE   A 1 342 ? 25.452  -10.246 9.248   1.00 27.43 ? 343 ILE   A CG1 1 
ATOM   2728 C CG2 . ILE   A 1 342 ? 25.775  -7.838  8.643   1.00 29.24 ? 343 ILE   A CG2 1 
ATOM   2729 C CD1 . ILE   A 1 342 ? 24.721  -10.067 10.565  1.00 27.01 ? 343 ILE   A CD1 1 
ATOM   2730 N N   . PRO   A 1 343 ? 29.224  -10.717 9.121   1.00 21.76 ? 344 PRO   A N   1 
ATOM   2731 C CA  . PRO   A 1 343 ? 30.014  -11.904 9.467   1.00 24.87 ? 344 PRO   A CA  1 
ATOM   2732 C C   . PRO   A 1 343 ? 29.138  -13.061 9.932   1.00 21.69 ? 344 PRO   A C   1 
ATOM   2733 O O   . PRO   A 1 343 ? 28.154  -12.882 10.657  1.00 22.06 ? 344 PRO   A O   1 
ATOM   2734 C CB  . PRO   A 1 343 ? 30.928  -11.399 10.588  1.00 23.65 ? 344 PRO   A CB  1 
ATOM   2735 C CG  . PRO   A 1 343 ? 31.087  -9.931  10.305  1.00 20.63 ? 344 PRO   A CG  1 
ATOM   2736 C CD  . PRO   A 1 343 ? 29.734  -9.501  9.784   1.00 23.04 ? 344 PRO   A CD  1 
ATOM   2737 N N   . ASN   A 1 344 ? 29.497  -14.267 9.493   1.00 21.70 ? 345 ASN   A N   1 
ATOM   2738 C CA  . ASN   A 1 344 ? 28.726  -15.435 9.902   1.00 22.07 ? 345 ASN   A CA  1 
ATOM   2739 C C   . ASN   A 1 344 ? 28.736  -15.619 11.414  1.00 21.85 ? 345 ASN   A C   1 
ATOM   2740 O O   . ASN   A 1 344 ? 27.720  -16.038 11.984  1.00 18.67 ? 345 ASN   A O   1 
ATOM   2741 C CB  . ASN   A 1 344 ? 29.250  -16.680 9.188   1.00 22.01 ? 345 ASN   A CB  1 
ATOM   2742 C CG  . ASN   A 1 344 ? 28.860  -16.691 7.727   1.00 28.66 ? 345 ASN   A CG  1 
ATOM   2743 O OD1 . ASN   A 1 344 ? 27.751  -16.290 7.383   1.00 29.04 ? 345 ASN   A OD1 1 
ATOM   2744 N ND2 . ASN   A 1 344 ? 29.776  -17.111 6.855   1.00 31.93 ? 345 ASN   A ND2 1 
ATOM   2745 N N   . GLU   A 1 345 ? 29.845  -15.280 12.086  1.00 23.28 ? 346 GLU   A N   1 
ATOM   2746 C CA  . GLU   A 1 345 ? 29.889  -15.442 13.539  1.00 21.37 ? 346 GLU   A CA  1 
ATOM   2747 C C   . GLU   A 1 345 ? 28.853  -14.565 14.224  1.00 21.91 ? 346 GLU   A C   1 
ATOM   2748 O O   . GLU   A 1 345 ? 28.270  -14.966 15.237  1.00 20.26 ? 346 GLU   A O   1 
ATOM   2749 C CB  . GLU   A 1 345 ? 31.287  -15.117 14.078  1.00 29.11 ? 346 GLU   A CB  1 
ATOM   2750 C CG  . GLU   A 1 345 ? 32.437  -15.650 13.225  1.00 33.51 ? 346 GLU   A CG  1 
ATOM   2751 C CD  . GLU   A 1 345 ? 32.825  -14.685 12.099  1.00 36.69 ? 346 GLU   A CD  1 
ATOM   2752 O OE1 . GLU   A 1 345 ? 32.335  -14.858 10.956  1.00 36.25 ? 346 GLU   A OE1 1 
ATOM   2753 O OE2 . GLU   A 1 345 ? 33.610  -13.741 12.368  1.00 46.48 ? 346 GLU   A OE2 1 
ATOM   2754 N N   . GLU   A 1 346 ? 28.597  -13.377 13.675  1.00 20.50 ? 347 GLU   A N   1 
ATOM   2755 C CA  . GLU   A 1 346 ? 27.572  -12.506 14.241  1.00 21.40 ? 347 GLU   A CA  1 
ATOM   2756 C C   . GLU   A 1 346 ? 26.182  -13.117 14.096  1.00 19.68 ? 347 GLU   A C   1 
ATOM   2757 O O   . GLU   A 1 346 ? 25.352  -12.995 15.003  1.00 19.85 ? 347 GLU   A O   1 
ATOM   2758 C CB  . GLU   A 1 346 ? 27.625  -11.135 13.569  1.00 23.10 ? 347 GLU   A CB  1 
ATOM   2759 C CG  . GLU   A 1 346 ? 28.914  -10.369 13.824  1.00 24.87 ? 347 GLU   A CG  1 
ATOM   2760 C CD  . GLU   A 1 346 ? 28.871  -9.543  15.103  1.00 30.10 ? 347 GLU   A CD  1 
ATOM   2761 O OE1 . GLU   A 1 346 ? 28.158  -9.930  16.050  1.00 28.74 ? 347 GLU   A OE1 1 
ATOM   2762 O OE2 . GLU   A 1 346 ? 29.547  -8.494  15.160  1.00 30.71 ? 347 GLU   A OE2 1 
ATOM   2763 N N   . ARG   A 1 347 ? 25.901  -13.760 12.957  1.00 16.68 ? 348 ARG   A N   1 
ATOM   2764 C CA  . ARG   A 1 347 ? 24.596  -14.384 12.770  1.00 15.67 ? 348 ARG   A CA  1 
ATOM   2765 C C   . ARG   A 1 347 ? 24.422  -15.539 13.740  1.00 17.82 ? 348 ARG   A C   1 
ATOM   2766 O O   . ARG   A 1 347 ? 23.381  -15.668 14.397  1.00 17.71 ? 348 ARG   A O   1 
ATOM   2767 C CB  . ARG   A 1 347 ? 24.442  -14.893 11.332  1.00 18.61 ? 348 ARG   A CB  1 
ATOM   2768 C CG  . ARG   A 1 347 ? 24.782  -13.881 10.257  1.00 17.80 ? 348 ARG   A CG  1 
ATOM   2769 C CD  . ARG   A 1 347 ? 24.846  -14.594 8.911   1.00 18.70 ? 348 ARG   A CD  1 
ATOM   2770 N NE  . ARG   A 1 347 ? 25.680  -13.855 7.976   1.00 22.32 ? 348 ARG   A NE  1 
ATOM   2771 C CZ  . ARG   A 1 347 ? 25.788  -14.156 6.691   1.00 23.77 ? 348 ARG   A CZ  1 
ATOM   2772 N NH1 . ARG   A 1 347 ? 25.197  -15.228 6.187   1.00 23.93 ? 348 ARG   A NH1 1 
ATOM   2773 N NH2 . ARG   A 1 347 ? 26.485  -13.345 5.888   1.00 24.27 ? 348 ARG   A NH2 1 
ATOM   2774 N N   . ILE   A 1 348 ? 25.453  -16.383 13.849  1.00 17.93 ? 349 ILE   A N   1 
ATOM   2775 C CA  . ILE   A 1 348 ? 25.382  -17.547 14.725  1.00 16.55 ? 349 ILE   A CA  1 
ATOM   2776 C C   . ILE   A 1 348 ? 25.269  -17.137 16.191  1.00 18.56 ? 349 ILE   A C   1 
ATOM   2777 O O   . ILE   A 1 348 ? 24.474  -17.712 16.939  1.00 19.73 ? 349 ILE   A O   1 
ATOM   2778 C CB  . ILE   A 1 348 ? 26.602  -18.449 14.482  1.00 17.71 ? 349 ILE   A CB  1 
ATOM   2779 C CG1 . ILE   A 1 348 ? 26.537  -19.033 13.070  1.00 16.84 ? 349 ILE   A CG1 1 
ATOM   2780 C CG2 . ILE   A 1 348 ? 26.702  -19.529 15.561  1.00 17.12 ? 349 ILE   A CG2 1 
ATOM   2781 C CD1 . ILE   A 1 348 ? 27.841  -19.617 12.604  1.00 17.04 ? 349 ILE   A CD1 1 
ATOM   2782 N N   . LYS   A 1 349 ? 26.063  -16.149 16.629  1.00 17.31 ? 350 LYS   A N   1 
ATOM   2783 C CA  . LYS   A 1 349 ? 25.988  -15.704 18.022  1.00 17.09 ? 350 LYS   A CA  1 
ATOM   2784 C C   . LYS   A 1 349 ? 24.621  -15.105 18.348  1.00 21.32 ? 350 LYS   A C   1 
ATOM   2785 O O   . LYS   A 1 349 ? 24.059  -15.363 19.420  1.00 20.38 ? 350 LYS   A O   1 
ATOM   2786 C CB  . LYS   A 1 349 ? 27.099  -14.683 18.304  1.00 19.90 ? 350 LYS   A CB  1 
ATOM   2787 C CG  . LYS   A 1 349 ? 28.494  -15.282 18.465  1.00 23.49 ? 350 LYS   A CG  1 
ATOM   2788 C CD  . LYS   A 1 349 ? 29.575  -14.185 18.371  1.00 28.19 ? 350 LYS   A CD  1 
ATOM   2789 C CE  . LYS   A 1 349 ? 30.985  -14.776 18.374  1.00 32.93 ? 350 LYS   A CE  1 
ATOM   2790 N NZ  . LYS   A 1 349 ? 32.044  -13.751 18.078  1.00 44.06 ? 350 LYS   A NZ  1 
ATOM   2791 N N   . ALA   A 1 350 ? 24.081  -14.271 17.452  1.00 18.05 ? 351 ALA   A N   1 
ATOM   2792 C CA  . ALA   A 1 350 ? 22.791  -13.638 17.737  1.00 20.12 ? 351 ALA   A CA  1 
ATOM   2793 C C   . ALA   A 1 350 ? 21.675  -14.676 17.856  1.00 18.39 ? 351 ALA   A C   1 
ATOM   2794 O O   . ALA   A 1 350 ? 20.828  -14.592 18.758  1.00 19.71 ? 351 ALA   A O   1 
ATOM   2795 C CB  . ALA   A 1 350 ? 22.464  -12.596 16.660  1.00 19.03 ? 351 ALA   A CB  1 
ATOM   2796 N N   . ALA   A 1 351 ? 21.670  -15.677 16.974  1.00 18.69 ? 352 ALA   A N   1 
ATOM   2797 C CA  . ALA   A 1 351 ? 20.633  -16.705 17.041  1.00 18.98 ? 352 ALA   A CA  1 
ATOM   2798 C C   . ALA   A 1 351 ? 20.818  -17.608 18.261  1.00 19.94 ? 352 ALA   A C   1 
ATOM   2799 O O   . ALA   A 1 351 ? 19.836  -18.078 18.837  1.00 19.65 ? 352 ALA   A O   1 
ATOM   2800 C CB  . ALA   A 1 351 ? 20.637  -17.531 15.750  1.00 19.32 ? 352 ALA   A CB  1 
ATOM   2801 N N   . TYR   A 1 352 ? 22.063  -17.879 18.646  1.00 16.56 ? 353 TYR   A N   1 
ATOM   2802 C CA  . TYR   A 1 352 ? 22.324  -18.650 19.860  1.00 16.31 ? 353 TYR   A CA  1 
ATOM   2803 C C   . TYR   A 1 352 ? 21.757  -17.929 21.076  1.00 17.99 ? 353 TYR   A C   1 
ATOM   2804 O O   . TYR   A 1 352 ? 21.082  -18.533 21.919  1.00 19.56 ? 353 TYR   A O   1 
ATOM   2805 C CB  . TYR   A 1 352 ? 23.833  -18.885 19.995  1.00 18.56 ? 353 TYR   A CB  1 
ATOM   2806 C CG  . TYR   A 1 352 ? 24.225  -19.717 21.198  1.00 18.88 ? 353 TYR   A CG  1 
ATOM   2807 C CD1 . TYR   A 1 352 ? 24.477  -19.121 22.426  1.00 21.07 ? 353 TYR   A CD1 1 
ATOM   2808 C CD2 . TYR   A 1 352 ? 24.334  -21.098 21.104  1.00 18.66 ? 353 TYR   A CD2 1 
ATOM   2809 C CE1 . TYR   A 1 352 ? 24.830  -19.874 23.531  1.00 21.01 ? 353 TYR   A CE1 1 
ATOM   2810 C CE2 . TYR   A 1 352 ? 24.695  -21.862 22.201  1.00 19.75 ? 353 TYR   A CE2 1 
ATOM   2811 C CZ  . TYR   A 1 352 ? 24.934  -21.246 23.413  1.00 19.07 ? 353 TYR   A CZ  1 
ATOM   2812 O OH  . TYR   A 1 352 ? 25.291  -22.006 24.521  1.00 18.17 ? 353 TYR   A OH  1 
ATOM   2813 N N   . ALA   A 1 353 ? 21.992  -16.619 21.155  1.00 18.96 ? 354 ALA   A N   1 
ATOM   2814 C CA  . ALA   A 1 353 ? 21.485  -15.843 22.281  1.00 20.72 ? 354 ALA   A CA  1 
ATOM   2815 C C   . ALA   A 1 353 ? 19.964  -15.894 22.339  1.00 19.03 ? 354 ALA   A C   1 
ATOM   2816 O O   . ALA   A 1 353 ? 19.375  -16.086 23.413  1.00 21.12 ? 354 ALA   A O   1 
ATOM   2817 C CB  . ALA   A 1 353 ? 21.967  -14.394 22.183  1.00 20.96 ? 354 ALA   A CB  1 
ATOM   2818 N N   . VAL   A 1 354 ? 19.307  -15.708 21.194  1.00 21.01 ? 355 VAL   A N   1 
ATOM   2819 C CA  . VAL   A 1 354 ? 17.846  -15.667 21.173  1.00 20.66 ? 355 VAL   A CA  1 
ATOM   2820 C C   . VAL   A 1 354 ? 17.262  -17.022 21.555  1.00 20.25 ? 355 VAL   A C   1 
ATOM   2821 O O   . VAL   A 1 354 ? 16.399  -17.116 22.435  1.00 20.62 ? 355 VAL   A O   1 
ATOM   2822 C CB  . VAL   A 1 354 ? 17.342  -15.204 19.797  1.00 23.00 ? 355 VAL   A CB  1 
ATOM   2823 C CG1 . VAL   A 1 354 ? 15.837  -15.461 19.652  1.00 22.10 ? 355 VAL   A CG1 1 
ATOM   2824 C CG2 . VAL   A 1 354 ? 17.681  -13.740 19.594  1.00 18.94 ? 355 VAL   A CG2 1 
ATOM   2825 N N   . LEU   A 1 355 ? 17.719  -18.092 20.904  1.00 19.36 ? 356 LEU   A N   1 
ATOM   2826 C CA  . LEU   A 1 355 ? 17.144  -19.403 21.183  1.00 20.56 ? 356 LEU   A CA  1 
ATOM   2827 C C   . LEU   A 1 355 ? 17.467  -19.907 22.585  1.00 21.85 ? 356 LEU   A C   1 
ATOM   2828 O O   . LEU   A 1 355 ? 16.719  -20.742 23.109  1.00 24.38 ? 356 LEU   A O   1 
ATOM   2829 C CB  . LEU   A 1 355 ? 17.615  -20.424 20.148  1.00 18.64 ? 356 LEU   A CB  1 
ATOM   2830 C CG  . LEU   A 1 355 ? 17.113  -20.224 18.712  1.00 22.46 ? 356 LEU   A CG  1 
ATOM   2831 C CD1 . LEU   A 1 355 ? 17.391  -21.463 17.868  1.00 25.49 ? 356 LEU   A CD1 1 
ATOM   2832 C CD2 . LEU   A 1 355 ? 15.630  -19.880 18.651  1.00 23.01 ? 356 LEU   A CD2 1 
ATOM   2833 N N   . ASN   A 1 356 ? 18.557  -19.435 23.202  1.00 19.49 ? 357 ASN   A N   1 
ATOM   2834 C CA  . ASN   A 1 356 ? 18.852  -19.813 24.579  1.00 20.50 ? 357 ASN   A CA  1 
ATOM   2835 C C   . ASN   A 1 356 ? 18.055  -18.999 25.587  1.00 24.00 ? 357 ASN   A C   1 
ATOM   2836 O O   . ASN   A 1 356 ? 17.921  -19.424 26.742  1.00 27.64 ? 357 ASN   A O   1 
ATOM   2837 C CB  . ASN   A 1 356 ? 20.348  -19.660 24.871  1.00 20.54 ? 357 ASN   A CB  1 
ATOM   2838 C CG  . ASN   A 1 356 ? 21.144  -20.899 24.495  1.00 22.49 ? 357 ASN   A CG  1 
ATOM   2839 O OD1 . ASN   A 1 356 ? 21.397  -21.762 25.338  1.00 23.76 ? 357 ASN   A OD1 1 
ATOM   2840 N ND2 . ASN   A 1 356 ? 21.539  -20.993 23.230  1.00 21.68 ? 357 ASN   A ND2 1 
ATOM   2841 N N   . ALA   A 1 357 ? 17.512  -17.852 25.181  1.00 23.79 ? 358 ALA   A N   1 
ATOM   2842 C CA  . ALA   A 1 357 ? 16.814  -16.984 26.116  1.00 25.32 ? 358 ALA   A CA  1 
ATOM   2843 C C   . ALA   A 1 357 ? 15.295  -17.093 26.054  1.00 28.66 ? 358 ALA   A C   1 
ATOM   2844 O O   . ALA   A 1 357 ? 14.635  -16.748 27.044  1.00 27.89 ? 358 ALA   A O   1 
ATOM   2845 C CB  . ALA   A 1 357 ? 17.219  -15.523 25.884  1.00 25.65 ? 358 ALA   A CB  1 
ATOM   2846 N N   . ILE   A 1 358 ? 14.725  -17.550 24.932  1.00 26.91 ? 359 ILE   A N   1 
ATOM   2847 C CA  . ILE   A 1 358 ? 13.273  -17.612 24.798  1.00 28.81 ? 359 ILE   A CA  1 
ATOM   2848 C C   . ILE   A 1 358 ? 12.706  -18.582 25.826  1.00 34.83 ? 359 ILE   A C   1 
ATOM   2849 O O   . ILE   A 1 358 ? 13.280  -19.647 26.093  1.00 31.65 ? 359 ILE   A O   1 
ATOM   2850 C CB  . ILE   A 1 358 ? 12.866  -18.015 23.367  1.00 31.42 ? 359 ILE   A CB  1 
ATOM   2851 C CG1 . ILE   A 1 358 ? 13.096  -16.869 22.381  1.00 34.51 ? 359 ILE   A CG1 1 
ATOM   2852 C CG2 . ILE   A 1 358 ? 11.398  -18.403 23.294  1.00 29.30 ? 359 ILE   A CG2 1 
ATOM   2853 C CD1 . ILE   A 1 358 ? 12.561  -17.141 20.989  1.00 37.52 ? 359 ILE   A CD1 1 
ATOM   2854 N N   . LYS   A 1 359 ? 11.582  -18.200 26.430  1.00 33.01 ? 360 LYS   A N   1 
ATOM   2855 C CA  . LYS   A 1 359 ? 10.913  -19.060 27.394  1.00 38.15 ? 360 LYS   A CA  1 
ATOM   2856 C C   . LYS   A 1 359 ? 10.162  -20.178 26.678  1.00 39.66 ? 360 LYS   A C   1 
ATOM   2857 O O   . LYS   A 1 359 ? 9.588   -19.974 25.604  1.00 35.35 ? 360 LYS   A O   1 
ATOM   2858 C CB  . LYS   A 1 359 ? 9.957   -18.237 28.257  1.00 39.17 ? 360 LYS   A CB  1 
ATOM   2859 C CG  . LYS   A 1 359 ? 10.664  -17.261 29.191  1.00 42.00 ? 360 LYS   A CG  1 
ATOM   2860 C CD  . LYS   A 1 359 ? 9.785   -16.053 29.499  1.00 45.77 ? 360 LYS   A CD  1 
ATOM   2861 C CE  . LYS   A 1 359 ? 10.316  -15.257 30.688  1.00 52.01 ? 360 LYS   A CE  1 
ATOM   2862 N NZ  . LYS   A 1 359 ? 11.709  -14.758 30.479  1.00 55.41 ? 360 LYS   A NZ  1 
ATOM   2863 N N   . LYS   A 1 360 ? 10.181  -21.368 27.276  1.00 40.98 ? 361 LYS   A N   1 
ATOM   2864 C CA  . LYS   A 1 360 ? 9.505   -22.531 26.703  1.00 46.46 ? 361 LYS   A CA  1 
ATOM   2865 C C   . LYS   A 1 360 ? 7.982   -22.383 26.800  1.00 53.42 ? 361 LYS   A C   1 
ATOM   2866 O O   . LYS   A 1 360 ? 7.460   -21.910 27.810  1.00 51.03 ? 361 LYS   A O   1 
ATOM   2867 C CB  . LYS   A 1 360 ? 9.947   -23.819 27.411  1.00 52.86 ? 361 LYS   A CB  1 
ATOM   2868 C CG  . LYS   A 1 360 ? 11.391  -23.826 27.909  1.00 52.33 ? 361 LYS   A CG  1 
ATOM   2869 C CD  . LYS   A 1 360 ? 12.386  -23.800 26.762  1.00 52.00 ? 361 LYS   A CD  1 
ATOM   2870 C CE  . LYS   A 1 360 ? 13.496  -24.827 26.963  1.00 56.44 ? 361 LYS   A CE  1 
ATOM   2871 N NZ  . LYS   A 1 360 ? 14.226  -24.652 28.255  1.00 55.45 ? 361 LYS   A NZ  1 
ATOM   2872 O OXT . LYS   A 1 360 ? 7.233   -22.738 25.883  1.00 49.71 ? 361 LYS   A OXT 1 
ATOM   2873 N N   . ASN   B 1 2   ? -3.554  -2.576  -8.261  1.00 70.69 ? 3   ASN   B N   1 
ATOM   2874 C CA  . ASN   B 1 2   ? -4.425  -1.480  -7.850  1.00 66.18 ? 3   ASN   B CA  1 
ATOM   2875 C C   . ASN   B 1 2   ? -5.013  -0.749  -9.060  1.00 62.52 ? 3   ASN   B C   1 
ATOM   2876 O O   . ASN   B 1 2   ? -4.591  -0.981  -10.194 1.00 61.12 ? 3   ASN   B O   1 
ATOM   2877 C CB  . ASN   B 1 2   ? -3.660  -0.509  -6.956  1.00 67.68 ? 3   ASN   B CB  1 
ATOM   2878 C CG  . ASN   B 1 2   ? -3.693  -0.914  -5.493  1.00 73.85 ? 3   ASN   B CG  1 
ATOM   2879 O OD1 . ASN   B 1 2   ? -4.442  -0.346  -4.698  1.00 72.85 ? 3   ASN   B OD1 1 
ATOM   2880 N ND2 . ASN   B 1 2   ? -2.883  -1.905  -5.133  1.00 81.97 ? 3   ASN   B ND2 1 
ATOM   2881 N N   . THR   B 1 3   ? -5.990  0.131   -8.808  1.00 58.93 ? 4   THR   B N   1 
ATOM   2882 C CA  . THR   B 1 3   ? -6.705  0.821   -9.877  1.00 57.59 ? 4   THR   B CA  1 
ATOM   2883 C C   . THR   B 1 3   ? -5.742  1.676   -10.704 1.00 56.67 ? 4   THR   B C   1 
ATOM   2884 O O   . THR   B 1 3   ? -4.648  2.012   -10.242 1.00 55.40 ? 4   THR   B O   1 
ATOM   2885 C CB  . THR   B 1 3   ? -7.814  1.701   -9.291  1.00 56.90 ? 4   THR   B CB  1 
ATOM   2886 O OG1 . THR   B 1 3   ? -7.236  2.848   -8.648  1.00 53.52 ? 4   THR   B OG1 1 
ATOM   2887 C CG2 . THR   B 1 3   ? -8.638  0.920   -8.277  1.00 58.28 ? 4   THR   B CG2 1 
ATOM   2888 N N   . PRO   B 1 4   ? -6.120  2.034   -11.939 1.00 56.12 ? 5   PRO   B N   1 
ATOM   2889 C CA  . PRO   B 1 4   ? -5.262  2.949   -12.715 1.00 53.92 ? 5   PRO   B CA  1 
ATOM   2890 C C   . PRO   B 1 4   ? -5.030  4.275   -12.017 1.00 50.24 ? 5   PRO   B C   1 
ATOM   2891 O O   . PRO   B 1 4   ? -3.945  4.857   -12.151 1.00 47.72 ? 5   PRO   B O   1 
ATOM   2892 C CB  . PRO   B 1 4   ? -6.026  3.124   -14.038 1.00 52.71 ? 5   PRO   B CB  1 
ATOM   2893 C CG  . PRO   B 1 4   ? -7.427  2.677   -13.748 1.00 58.13 ? 5   PRO   B CG  1 
ATOM   2894 C CD  . PRO   B 1 4   ? -7.291  1.595   -12.718 1.00 57.57 ? 5   PRO   B CD  1 
ATOM   2895 N N   . LYS   B 1 5   ? -6.018  4.765   -11.265 1.00 48.13 ? 6   LYS   B N   1 
ATOM   2896 C CA  . LYS   B 1 5   ? -5.819  5.967   -10.465 1.00 47.09 ? 6   LYS   B CA  1 
ATOM   2897 C C   . LYS   B 1 5   ? -4.746  5.746   -9.408  1.00 46.33 ? 6   LYS   B C   1 
ATOM   2898 O O   . LYS   B 1 5   ? -3.870  6.595   -9.213  1.00 41.41 ? 6   LYS   B O   1 
ATOM   2899 C CB  . LYS   B 1 5   ? -7.138  6.389   -9.818  1.00 47.13 ? 6   LYS   B CB  1 
ATOM   2900 C CG  . LYS   B 1 5   ? -7.859  7.494   -10.566 1.00 49.40 ? 6   LYS   B CG  1 
ATOM   2901 C CD  . LYS   B 1 5   ? -7.072  8.795   -10.498 1.00 47.52 ? 6   LYS   B CD  1 
ATOM   2902 C CE  . LYS   B 1 5   ? -7.633  9.812   -11.479 1.00 49.07 ? 6   LYS   B CE  1 
ATOM   2903 N NZ  . LYS   B 1 5   ? -6.832  11.069  -11.480 1.00 45.73 ? 6   LYS   B NZ  1 
ATOM   2904 N N   . ASP   B 1 6   ? -4.801  4.602   -8.715  1.00 46.47 ? 7   ASP   B N   1 
ATOM   2905 C CA  . ASP   B 1 6   ? -3.801  4.285   -7.698  1.00 47.32 ? 7   ASP   B CA  1 
ATOM   2906 C C   . ASP   B 1 6   ? -2.393  4.359   -8.273  1.00 45.21 ? 7   ASP   B C   1 
ATOM   2907 O O   . ASP   B 1 6   ? -1.488  4.951   -7.673  1.00 36.79 ? 7   ASP   B O   1 
ATOM   2908 C CB  . ASP   B 1 6   ? -4.053  2.888   -7.125  1.00 52.14 ? 7   ASP   B CB  1 
ATOM   2909 C CG  . ASP   B 1 6   ? -5.292  2.814   -6.255  1.00 53.01 ? 7   ASP   B CG  1 
ATOM   2910 O OD1 . ASP   B 1 6   ? -5.396  3.596   -5.291  1.00 49.22 ? 7   ASP   B OD1 1 
ATOM   2911 O OD2 . ASP   B 1 6   ? -6.159  1.957   -6.528  1.00 58.08 ? 7   ASP   B OD2 1 
ATOM   2912 N N   . GLN   B 1 7   ? -2.192  3.743   -9.441  1.00 44.55 ? 8   GLN   B N   1 
ATOM   2913 C CA  . GLN   B 1 7   ? -0.871  3.717   -10.053 1.00 41.62 ? 8   GLN   B CA  1 
ATOM   2914 C C   . GLN   B 1 7   ? -0.501  5.082   -10.620 1.00 38.64 ? 8   GLN   B C   1 
ATOM   2915 O O   . GLN   B 1 7   ? 0.668   5.481   -10.569 1.00 38.32 ? 8   GLN   B O   1 
ATOM   2916 C CB  . GLN   B 1 7   ? -0.823  2.641   -11.133 1.00 48.19 ? 8   GLN   B CB  1 
ATOM   2917 C CG  . GLN   B 1 7   ? -1.210  1.261   -10.622 1.00 53.69 ? 8   GLN   B CG  1 
ATOM   2918 C CD  . GLN   B 1 7   ? -1.432  0.265   -11.744 1.00 61.39 ? 8   GLN   B CD  1 
ATOM   2919 O OE1 . GLN   B 1 7   ? -0.536  0.005   -12.548 1.00 61.79 ? 8   GLN   B OE1 1 
ATOM   2920 N NE2 . GLN   B 1 7   ? -2.636  -0.295  -11.807 1.00 64.39 ? 8   GLN   B NE2 1 
ATOM   2921 N N   . GLU   B 1 8   ? -1.482  5.812   -11.159 1.00 39.96 ? 9   GLU   B N   1 
ATOM   2922 C CA  . GLU   B 1 8   ? -1.218  7.176   -11.610 1.00 39.49 ? 9   GLU   B CA  1 
ATOM   2923 C C   . GLU   B 1 8   ? -0.742  8.052   -10.456 1.00 37.06 ? 9   GLU   B C   1 
ATOM   2924 O O   . GLU   B 1 8   ? 0.259   8.765   -10.582 1.00 34.19 ? 9   GLU   B O   1 
ATOM   2925 C CB  . GLU   B 1 8   ? -2.464  7.785   -12.256 1.00 46.47 ? 9   GLU   B CB  1 
ATOM   2926 C CG  . GLU   B 1 8   ? -2.206  9.167   -12.878 1.00 50.14 ? 9   GLU   B CG  1 
ATOM   2927 C CD  . GLU   B 1 8   ? -3.431  10.079  -12.888 1.00 50.14 ? 9   GLU   B CD  1 
ATOM   2928 O OE1 . GLU   B 1 8   ? -4.526  9.629   -12.484 1.00 46.91 ? 9   GLU   B OE1 1 
ATOM   2929 O OE2 . GLU   B 1 8   ? -3.286  11.255  -13.297 1.00 48.01 ? 9   GLU   B OE2 1 
ATOM   2930 N N   . ILE   B 1 9   ? -1.455  8.013   -9.321  1.00 38.57 ? 10  ILE   B N   1 
ATOM   2931 C CA  . ILE   B 1 9   ? -1.079  8.822   -8.159  1.00 35.36 ? 10  ILE   B CA  1 
ATOM   2932 C C   . ILE   B 1 9   ? 0.287   8.403   -7.637  1.00 32.95 ? 10  ILE   B C   1 
ATOM   2933 O O   . ILE   B 1 9   ? 1.124   9.244   -7.285  1.00 28.31 ? 10  ILE   B O   1 
ATOM   2934 C CB  . ILE   B 1 9   ? -2.139  8.714   -7.044  1.00 35.33 ? 10  ILE   B CB  1 
ATOM   2935 C CG1 . ILE   B 1 9   ? -3.530  9.096   -7.545  1.00 41.79 ? 10  ILE   B CG1 1 
ATOM   2936 C CG2 . ILE   B 1 9   ? -1.757  9.591   -5.852  1.00 30.90 ? 10  ILE   B CG2 1 
ATOM   2937 C CD1 . ILE   B 1 9   ? -3.581  10.414  -8.174  1.00 42.13 ? 10  ILE   B CD1 1 
ATOM   2938 N N   . LYS   B 1 10  ? 0.523   7.094   -7.549  1.00 32.70 ? 11  LYS   B N   1 
ATOM   2939 C CA  . LYS   B 1 10  ? 1.790   6.607   -7.022  1.00 30.87 ? 11  LYS   B CA  1 
ATOM   2940 C C   . LYS   B 1 10  ? 2.960   7.074   -7.876  1.00 31.52 ? 11  LYS   B C   1 
ATOM   2941 O O   . LYS   B 1 10  ? 3.991   7.500   -7.342  1.00 30.98 ? 11  LYS   B O   1 
ATOM   2942 C CB  . LYS   B 1 10  ? 1.761   5.083   -6.934  1.00 36.70 ? 11  LYS   B CB  1 
ATOM   2943 C CG  . LYS   B 1 10  ? 3.078   4.470   -6.514  1.00 43.04 ? 11  LYS   B CG  1 
ATOM   2944 C CD  . LYS   B 1 10  ? 3.335   4.649   -5.026  1.00 43.61 ? 11  LYS   B CD  1 
ATOM   2945 C CE  . LYS   B 1 10  ? 4.396   3.664   -4.557  1.00 46.87 ? 11  LYS   B CE  1 
ATOM   2946 N NZ  . LYS   B 1 10  ? 4.066   2.283   -5.009  1.00 46.57 ? 11  LYS   B NZ  1 
ATOM   2947 N N   . LYS   B 1 11  ? 2.821   6.993   -9.203  1.00 32.72 ? 12  LYS   B N   1 
ATOM   2948 C CA  . LYS   B 1 11  ? 3.876   7.466   -10.093 1.00 33.38 ? 12  LYS   B CA  1 
ATOM   2949 C C   . LYS   B 1 11  ? 4.196   8.933   -9.835  1.00 33.87 ? 12  LYS   B C   1 
ATOM   2950 O O   . LYS   B 1 11  ? 5.363   9.308   -9.662  1.00 31.72 ? 12  LYS   B O   1 
ATOM   2951 C CB  . LYS   B 1 11  ? 3.466   7.260   -11.552 1.00 36.67 ? 12  LYS   B CB  1 
ATOM   2952 C CG  . LYS   B 1 11  ? 4.406   7.939   -12.540 1.00 43.33 ? 12  LYS   B CG  1 
ATOM   2953 C CD  . LYS   B 1 11  ? 3.702   8.304   -13.845 1.00 49.07 ? 12  LYS   B CD  1 
ATOM   2954 C CE  . LYS   B 1 11  ? 3.665   7.137   -14.816 1.00 51.74 ? 12  LYS   B CE  1 
ATOM   2955 N NZ  . LYS   B 1 11  ? 5.036   6.760   -15.265 1.00 57.71 ? 12  LYS   B NZ  1 
ATOM   2956 N N   . LEU   B 1 12  ? 3.160   9.778   -9.803  1.00 32.18 ? 13  LEU   B N   1 
ATOM   2957 C CA  . LEU   B 1 12  ? 3.366   11.211  -9.635  1.00 30.58 ? 13  LEU   B CA  1 
ATOM   2958 C C   . LEU   B 1 12  ? 4.034   11.521  -8.304  1.00 28.01 ? 13  LEU   B C   1 
ATOM   2959 O O   . LEU   B 1 12  ? 4.917   12.383  -8.231  1.00 27.46 ? 13  LEU   B O   1 
ATOM   2960 C CB  . LEU   B 1 12  ? 2.031   11.947  -9.743  1.00 31.80 ? 13  LEU   B CB  1 
ATOM   2961 C CG  . LEU   B 1 12  ? 1.370   11.936  -11.122 1.00 37.33 ? 13  LEU   B CG  1 
ATOM   2962 C CD1 . LEU   B 1 12  ? -0.062  12.427  -11.032 1.00 36.69 ? 13  LEU   B CD1 1 
ATOM   2963 C CD2 . LEU   B 1 12  ? 2.175   12.791  -12.089 1.00 35.99 ? 13  LEU   B CD2 1 
ATOM   2964 N N   . VAL   B 1 13  ? 3.638   10.821  -7.240  1.00 27.61 ? 14  VAL   B N   1 
ATOM   2965 C CA  . VAL   B 1 13  ? 4.236   11.089  -5.936  1.00 26.47 ? 14  VAL   B CA  1 
ATOM   2966 C C   . VAL   B 1 13  ? 5.657   10.538  -5.884  1.00 27.44 ? 14  VAL   B C   1 
ATOM   2967 O O   . VAL   B 1 13  ? 6.556   11.152  -5.297  1.00 26.82 ? 14  VAL   B O   1 
ATOM   2968 C CB  . VAL   B 1 13  ? 3.346   10.522  -4.816  1.00 25.76 ? 14  VAL   B CB  1 
ATOM   2969 C CG1 . VAL   B 1 13  ? 4.030   10.639  -3.474  1.00 25.44 ? 14  VAL   B CG1 1 
ATOM   2970 C CG2 . VAL   B 1 13  ? 2.005   11.254  -4.785  1.00 24.60 ? 14  VAL   B CG2 1 
ATOM   2971 N N   . ASP   B 1 14  ? 5.890   9.387   -6.519  1.00 29.13 ? 15  ASP   B N   1 
ATOM   2972 C CA  . ASP   B 1 14  ? 7.257   8.887   -6.633  1.00 30.19 ? 15  ASP   B CA  1 
ATOM   2973 C C   . ASP   B 1 14  ? 8.133   9.869   -7.404  1.00 30.25 ? 15  ASP   B C   1 
ATOM   2974 O O   . ASP   B 1 14  ? 9.308   10.062  -7.066  1.00 31.94 ? 15  ASP   B O   1 
ATOM   2975 C CB  . ASP   B 1 14  ? 7.273   7.521   -7.325  1.00 32.08 ? 15  ASP   B CB  1 
ATOM   2976 C CG  . ASP   B 1 14  ? 6.844   6.371   -6.411  1.00 37.02 ? 15  ASP   B CG  1 
ATOM   2977 O OD1 . ASP   B 1 14  ? 6.724   6.547   -5.179  1.00 34.02 ? 15  ASP   B OD1 1 
ATOM   2978 O OD2 . ASP   B 1 14  ? 6.626   5.272   -6.950  1.00 36.56 ? 15  ASP   B OD2 1 
ATOM   2979 N N   . GLN   B 1 15  ? 7.583   10.481  -8.459  1.00 30.36 ? 16  GLN   B N   1 
ATOM   2980 C CA  . GLN   B 1 15  ? 8.372   11.386  -9.290  1.00 30.53 ? 16  GLN   B CA  1 
ATOM   2981 C C   . GLN   B 1 15  ? 8.764   12.641  -8.528  1.00 29.89 ? 16  GLN   B C   1 
ATOM   2982 O O   . GLN   B 1 15  ? 9.879   13.154  -8.693  1.00 31.04 ? 16  GLN   B O   1 
ATOM   2983 C CB  . GLN   B 1 15  ? 7.596   11.776  -10.554 1.00 31.83 ? 16  GLN   B CB  1 
ATOM   2984 C CG  . GLN   B 1 15  ? 7.351   10.649  -11.544 1.00 41.74 ? 16  GLN   B CG  1 
ATOM   2985 C CD  . GLN   B 1 15  ? 6.809   11.164  -12.861 1.00 47.87 ? 16  GLN   B CD  1 
ATOM   2986 O OE1 . GLN   B 1 15  ? 7.566   11.631  -13.707 1.00 53.05 ? 16  GLN   B OE1 1 
ATOM   2987 N NE2 . GLN   B 1 15  ? 5.487   11.089  -13.038 1.00 46.73 ? 16  GLN   B NE2 1 
ATOM   2988 N N   . ASN   B 1 16  ? 7.866   13.151  -7.685  1.00 27.39 ? 17  ASN   B N   1 
ATOM   2989 C CA  . ASN   B 1 16  ? 8.037   14.485  -7.130  1.00 29.73 ? 17  ASN   B CA  1 
ATOM   2990 C C   . ASN   B 1 16  ? 8.415   14.511  -5.662  1.00 28.01 ? 17  ASN   B C   1 
ATOM   2991 O O   . ASN   B 1 16  ? 9.145   15.417  -5.247  1.00 30.03 ? 17  ASN   B O   1 
ATOM   2992 C CB  . ASN   B 1 16  ? 6.755   15.302  -7.328  1.00 24.78 ? 17  ASN   B CB  1 
ATOM   2993 C CG  . ASN   B 1 16  ? 6.513   15.642  -8.784  1.00 29.97 ? 17  ASN   B CG  1 
ATOM   2994 O OD1 . ASN   B 1 16  ? 7.180   16.515  -9.349  1.00 29.71 ? 17  ASN   B OD1 1 
ATOM   2995 N ND2 . ASN   B 1 16  ? 5.555   14.958  -9.403  1.00 27.78 ? 17  ASN   B ND2 1 
ATOM   2996 N N   . PHE   B 1 17  ? 7.939   13.557  -4.869  1.00 25.45 ? 18  PHE   B N   1 
ATOM   2997 C CA  . PHE   B 1 17  ? 8.242   13.547  -3.444  1.00 28.58 ? 18  PHE   B CA  1 
ATOM   2998 C C   . PHE   B 1 17  ? 9.371   12.597  -3.077  1.00 28.50 ? 18  PHE   B C   1 
ATOM   2999 O O   . PHE   B 1 17  ? 10.208  12.952  -2.248  1.00 25.90 ? 18  PHE   B O   1 
ATOM   3000 C CB  . PHE   B 1 17  ? 6.981   13.213  -2.636  1.00 23.06 ? 18  PHE   B CB  1 
ATOM   3001 C CG  . PHE   B 1 17  ? 6.035   14.380  -2.503  1.00 21.42 ? 18  PHE   B CG  1 
ATOM   3002 C CD1 . PHE   B 1 17  ? 5.055   14.610  -3.453  1.00 24.86 ? 18  PHE   B CD1 1 
ATOM   3003 C CD2 . PHE   B 1 17  ? 6.148   15.257  -1.440  1.00 24.80 ? 18  PHE   B CD2 1 
ATOM   3004 C CE1 . PHE   B 1 17  ? 4.193   15.693  -3.344  1.00 23.70 ? 18  PHE   B CE1 1 
ATOM   3005 C CE2 . PHE   B 1 17  ? 5.292   16.341  -1.318  1.00 22.44 ? 18  PHE   B CE2 1 
ATOM   3006 C CZ  . PHE   B 1 17  ? 4.312   16.560  -2.264  1.00 20.60 ? 18  PHE   B CZ  1 
ATOM   3007 N N   . LYS   B 1 18  ? 9.427   11.409  -3.683  1.00 29.84 ? 19  LYS   B N   1 
ATOM   3008 C CA  . LYS   B 1 18  ? 10.473  10.438  -3.350  1.00 29.24 ? 19  LYS   B CA  1 
ATOM   3009 C C   . LYS   B 1 18  ? 11.889  11.005  -3.434  1.00 27.99 ? 19  LYS   B C   1 
ATOM   3010 O O   . LYS   B 1 18  ? 12.668  10.777  -2.496  1.00 30.61 ? 19  LYS   B O   1 
ATOM   3011 C CB  . LYS   B 1 18  ? 10.331  9.190   -4.234  1.00 29.27 ? 19  LYS   B CB  1 
ATOM   3012 C CG  . LYS   B 1 18  ? 11.289  8.064   -3.844  1.00 31.74 ? 19  LYS   B CG  1 
ATOM   3013 C CD  . LYS   B 1 18  ? 11.467  7.020   -4.943  1.00 37.15 ? 19  LYS   B CD  1 
ATOM   3014 C CE  . LYS   B 1 18  ? 10.206  6.227   -5.186  1.00 36.46 ? 19  LYS   B CE  1 
ATOM   3015 N NZ  . LYS   B 1 18  ? 10.491  5.008   -5.981  1.00 37.83 ? 19  LYS   B NZ  1 
ATOM   3016 N N   . PRO   B 1 19  ? 12.282  11.756  -4.477  1.00 29.30 ? 20  PRO   B N   1 
ATOM   3017 C CA  . PRO   B 1 19  ? 13.662  12.283  -4.515  1.00 34.23 ? 20  PRO   B CA  1 
ATOM   3018 C C   . PRO   B 1 19  ? 14.018  13.173  -3.338  1.00 28.87 ? 20  PRO   B C   1 
ATOM   3019 O O   . PRO   B 1 19  ? 15.201  13.278  -2.992  1.00 32.40 ? 20  PRO   B O   1 
ATOM   3020 C CB  . PRO   B 1 19  ? 13.701  13.075  -5.831  1.00 31.23 ? 20  PRO   B CB  1 
ATOM   3021 C CG  . PRO   B 1 19  ? 12.590  12.496  -6.655  1.00 30.89 ? 20  PRO   B CG  1 
ATOM   3022 C CD  . PRO   B 1 19  ? 11.518  12.172  -5.668  1.00 31.55 ? 20  PRO   B CD  1 
ATOM   3023 N N   . LEU   B 1 20  ? 13.029  13.814  -2.710  1.00 28.19 ? 21  LEU   B N   1 
ATOM   3024 C CA  . LEU   B 1 20  ? 13.307  14.699  -1.581  1.00 27.11 ? 21  LEU   B CA  1 
ATOM   3025 C C   . LEU   B 1 20  ? 13.882  13.943  -0.391  1.00 26.69 ? 21  LEU   B C   1 
ATOM   3026 O O   . LEU   B 1 20  ? 14.667  14.508  0.377   1.00 27.58 ? 21  LEU   B O   1 
ATOM   3027 C CB  . LEU   B 1 20  ? 12.029  15.438  -1.168  1.00 26.31 ? 21  LEU   B CB  1 
ATOM   3028 C CG  . LEU   B 1 20  ? 11.432  16.385  -2.215  1.00 27.08 ? 21  LEU   B CG  1 
ATOM   3029 C CD1 . LEU   B 1 20  ? 10.040  16.860  -1.817  1.00 28.87 ? 21  LEU   B CD1 1 
ATOM   3030 C CD2 . LEU   B 1 20  ? 12.329  17.584  -2.439  1.00 28.07 ? 21  LEU   B CD2 1 
ATOM   3031 N N   . LEU   B 1 21  ? 13.520  12.668  -0.215  1.00 26.40 ? 22  LEU   B N   1 
ATOM   3032 C CA  . LEU   B 1 21  ? 14.065  11.924  0.910   1.00 26.69 ? 22  LEU   B CA  1 
ATOM   3033 C C   . LEU   B 1 21  ? 15.567  11.712  0.756   1.00 28.67 ? 22  LEU   B C   1 
ATOM   3034 O O   . LEU   B 1 21  ? 16.310  11.790  1.741   1.00 27.88 ? 22  LEU   B O   1 
ATOM   3035 C CB  . LEU   B 1 21  ? 13.355  10.578  1.064   1.00 27.95 ? 22  LEU   B CB  1 
ATOM   3036 C CG  . LEU   B 1 21  ? 11.884  10.626  1.483   1.00 28.57 ? 22  LEU   B CG  1 
ATOM   3037 C CD1 . LEU   B 1 21  ? 11.007  10.209  0.315   1.00 33.97 ? 22  LEU   B CD1 1 
ATOM   3038 C CD2 . LEU   B 1 21  ? 11.664  9.701   2.698   1.00 29.53 ? 22  LEU   B CD2 1 
ATOM   3039 N N   . GLU   B 1 22  ? 16.030  11.434  -0.466  1.00 29.01 ? 23  GLU   B N   1 
ATOM   3040 C CA  . GLU   B 1 22  ? 17.463  11.301  -0.700  1.00 29.84 ? 23  GLU   B CA  1 
ATOM   3041 C C   . GLU   B 1 22  ? 18.160  12.648  -0.587  1.00 31.88 ? 23  GLU   B C   1 
ATOM   3042 O O   . GLU   B 1 22  ? 19.275  12.738  -0.058  1.00 31.96 ? 23  GLU   B O   1 
ATOM   3043 C CB  . GLU   B 1 22  ? 17.719  10.687  -2.076  1.00 34.29 ? 23  GLU   B CB  1 
ATOM   3044 C CG  . GLU   B 1 22  ? 19.169  10.277  -2.332  1.00 39.59 ? 23  GLU   B CG  1 
ATOM   3045 C CD  . GLU   B 1 22  ? 20.027  11.392  -2.930  1.00 38.63 ? 23  GLU   B CD  1 
ATOM   3046 O OE1 . GLU   B 1 22  ? 19.529  12.522  -3.103  1.00 44.11 ? 23  GLU   B OE1 1 
ATOM   3047 O OE2 . GLU   B 1 22  ? 21.213  11.140  -3.226  1.00 45.82 ? 23  GLU   B OE2 1 
ATOM   3048 N N   . LYS   B 1 23  ? 17.517  13.704  -1.082  1.00 29.50 ? 24  LYS   B N   1 
ATOM   3049 C CA  . LYS   B 1 23  ? 18.166  15.010  -1.148  1.00 32.34 ? 24  LYS   B CA  1 
ATOM   3050 C C   . LYS   B 1 23  ? 18.471  15.556  0.242   1.00 31.39 ? 24  LYS   B C   1 
ATOM   3051 O O   . LYS   B 1 23  ? 19.529  16.167  0.453   1.00 32.50 ? 24  LYS   B O   1 
ATOM   3052 C CB  . LYS   B 1 23  ? 17.288  15.981  -1.936  1.00 31.96 ? 24  LYS   B CB  1 
ATOM   3053 C CG  . LYS   B 1 23  ? 17.861  17.387  -2.081  1.00 31.29 ? 24  LYS   B CG  1 
ATOM   3054 C CD  . LYS   B 1 23  ? 17.128  18.160  -3.158  1.00 34.23 ? 24  LYS   B CD  1 
ATOM   3055 C CE  . LYS   B 1 23  ? 17.507  19.631  -3.118  1.00 35.11 ? 24  LYS   B CE  1 
ATOM   3056 N NZ  . LYS   B 1 23  ? 16.789  20.412  -4.162  1.00 32.30 ? 24  LYS   B NZ  1 
ATOM   3057 N N   . TYR   B 1 24  ? 17.569  15.333  1.202   1.00 28.31 ? 25  TYR   B N   1 
ATOM   3058 C CA  . TYR   B 1 24  ? 17.703  15.865  2.551   1.00 26.91 ? 25  TYR   B CA  1 
ATOM   3059 C C   . TYR   B 1 24  ? 17.940  14.781  3.594   1.00 28.22 ? 25  TYR   B C   1 
ATOM   3060 O O   . TYR   B 1 24  ? 17.918  15.076  4.796   1.00 27.58 ? 25  TYR   B O   1 
ATOM   3061 C CB  . TYR   B 1 24  ? 16.467  16.704  2.905   1.00 27.69 ? 25  TYR   B CB  1 
ATOM   3062 C CG  . TYR   B 1 24  ? 16.316  17.895  1.986   1.00 26.80 ? 25  TYR   B CG  1 
ATOM   3063 C CD1 . TYR   B 1 24  ? 17.080  19.044  2.179   1.00 28.65 ? 25  TYR   B CD1 1 
ATOM   3064 C CD2 . TYR   B 1 24  ? 15.443  17.863  0.904   1.00 27.20 ? 25  TYR   B CD2 1 
ATOM   3065 C CE1 . TYR   B 1 24  ? 16.964  20.127  1.334   1.00 27.30 ? 25  TYR   B CE1 1 
ATOM   3066 C CE2 . TYR   B 1 24  ? 15.309  18.955  0.058   1.00 26.87 ? 25  TYR   B CE2 1 
ATOM   3067 C CZ  . TYR   B 1 24  ? 16.091  20.079  0.273   1.00 27.17 ? 25  TYR   B CZ  1 
ATOM   3068 O OH  . TYR   B 1 24  ? 15.973  21.161  -0.574  1.00 29.68 ? 25  TYR   B OH  1 
ATOM   3069 N N   . ASP   B 1 25  ? 18.202  13.545  3.165   1.00 30.64 ? 26  ASP   B N   1 
ATOM   3070 C CA  . ASP   B 1 25  ? 18.364  12.397  4.060   1.00 29.79 ? 26  ASP   B CA  1 
ATOM   3071 C C   . ASP   B 1 25  ? 17.217  12.325  5.074   1.00 29.80 ? 26  ASP   B C   1 
ATOM   3072 O O   . ASP   B 1 25  ? 17.413  12.298  6.291   1.00 27.00 ? 26  ASP   B O   1 
ATOM   3073 C CB  . ASP   B 1 25  ? 19.723  12.434  4.762   1.00 32.21 ? 26  ASP   B CB  1 
ATOM   3074 C CG  . ASP   B 1 25  ? 20.116  11.085  5.336   1.00 42.63 ? 26  ASP   B CG  1 
ATOM   3075 O OD1 . ASP   B 1 25  ? 19.541  10.064  4.895   1.00 38.03 ? 26  ASP   B OD1 1 
ATOM   3076 O OD2 . ASP   B 1 25  ? 21.020  11.041  6.198   1.00 46.13 ? 26  ASP   B OD2 1 
ATOM   3077 N N   . VAL   B 1 26  ? 16.002  12.307  4.545   1.00 28.62 ? 27  VAL   B N   1 
ATOM   3078 C CA  . VAL   B 1 26  ? 14.802  12.236  5.379   1.00 24.79 ? 27  VAL   B CA  1 
ATOM   3079 C C   . VAL   B 1 26  ? 14.572  10.777  5.772   1.00 27.56 ? 27  VAL   B C   1 
ATOM   3080 O O   . VAL   B 1 26  ? 14.550  9.914   4.886   1.00 28.25 ? 27  VAL   B O   1 
ATOM   3081 C CB  . VAL   B 1 26  ? 13.590  12.776  4.628   1.00 27.49 ? 27  VAL   B CB  1 
ATOM   3082 C CG1 . VAL   B 1 26  ? 12.339  12.709  5.511   1.00 24.33 ? 27  VAL   B CG1 1 
ATOM   3083 C CG2 . VAL   B 1 26  ? 13.850  14.187  4.132   1.00 25.10 ? 27  VAL   B CG2 1 
ATOM   3084 N N   . PRO   B 1 27  ? 14.379  10.469  7.055   1.00 26.84 ? 28  PRO   B N   1 
ATOM   3085 C CA  . PRO   B 1 27  ? 14.145  9.057   7.414   1.00 25.42 ? 28  PRO   B CA  1 
ATOM   3086 C C   . PRO   B 1 27  ? 12.856  8.503   6.838   1.00 24.22 ? 28  PRO   B C   1 
ATOM   3087 O O   . PRO   B 1 27  ? 12.853  7.381   6.315   1.00 24.39 ? 28  PRO   B O   1 
ATOM   3088 C CB  . PRO   B 1 27  ? 14.117  9.083   8.950   1.00 28.36 ? 28  PRO   B CB  1 
ATOM   3089 C CG  . PRO   B 1 27  ? 14.874  10.312  9.323   1.00 28.97 ? 28  PRO   B CG  1 
ATOM   3090 C CD  . PRO   B 1 27  ? 14.575  11.318  8.240   1.00 27.29 ? 28  PRO   B CD  1 
ATOM   3091 N N   . GLY   B 1 28  ? 11.766  9.261   6.903   1.00 20.44 ? 29  GLY   B N   1 
ATOM   3092 C CA  . GLY   B 1 28  ? 10.479  8.752   6.467   1.00 20.29 ? 29  GLY   B CA  1 
ATOM   3093 C C   . GLY   B 1 28  ? 9.518   9.863   6.104   1.00 23.16 ? 29  GLY   B C   1 
ATOM   3094 O O   . GLY   B 1 28  ? 9.686   11.024  6.496   1.00 21.43 ? 29  GLY   B O   1 
ATOM   3095 N N   . MET   B 1 29  ? 8.497   9.486   5.345   1.00 20.95 ? 30  MET   B N   1 
ATOM   3096 C CA  . MET   B 1 29  ? 7.557   10.450  4.798   1.00 21.58 ? 30  MET   B CA  1 
ATOM   3097 C C   . MET   B 1 29  ? 6.227   9.752   4.548   1.00 23.12 ? 30  MET   B C   1 
ATOM   3098 O O   . MET   B 1 29  ? 6.188   8.568   4.212   1.00 22.14 ? 30  MET   B O   1 
ATOM   3099 C CB  . MET   B 1 29  ? 8.096   11.065  3.500   1.00 19.23 ? 30  MET   B CB  1 
ATOM   3100 C CG  . MET   B 1 29  ? 7.161   12.085  2.861   1.00 19.28 ? 30  MET   B CG  1 
ATOM   3101 S SD  . MET   B 1 29  ? 7.731   12.697  1.237   1.00 24.33 ? 30  MET   B SD  1 
ATOM   3102 C CE  . MET   B 1 29  ? 9.126   13.710  1.672   1.00 28.95 ? 30  MET   B CE  1 
ATOM   3103 N N   . ALA   B 1 30  ? 5.132   10.487  4.727   1.00 19.18 ? 31  ALA   B N   1 
ATOM   3104 C CA  . ALA   B 1 30  ? 3.811   10.013  4.321   1.00 19.52 ? 31  ALA   B CA  1 
ATOM   3105 C C   . ALA   B 1 30  ? 3.180   11.067  3.429   1.00 19.95 ? 31  ALA   B C   1 
ATOM   3106 O O   . ALA   B 1 30  ? 3.179   12.252  3.780   1.00 20.55 ? 31  ALA   B O   1 
ATOM   3107 C CB  . ALA   B 1 30  ? 2.904   9.735   5.531   1.00 19.72 ? 31  ALA   B CB  1 
ATOM   3108 N N   . VAL   B 1 31  ? 2.673   10.652  2.269   1.00 19.62 ? 32  VAL   B N   1 
ATOM   3109 C CA  . VAL   B 1 31  ? 2.018   11.555  1.327   1.00 19.55 ? 32  VAL   B CA  1 
ATOM   3110 C C   . VAL   B 1 31  ? 0.637   10.997  1.028   1.00 20.91 ? 32  VAL   B C   1 
ATOM   3111 O O   . VAL   B 1 31  ? 0.502   9.824   0.666   1.00 21.14 ? 32  VAL   B O   1 
ATOM   3112 C CB  . VAL   B 1 31  ? 2.831   11.734  0.025   1.00 19.50 ? 32  VAL   B CB  1 
ATOM   3113 C CG1 . VAL   B 1 31  ? 2.083   12.640  -0.960  1.00 22.56 ? 32  VAL   B CG1 1 
ATOM   3114 C CG2 . VAL   B 1 31  ? 4.214   12.288  0.321   1.00 21.44 ? 32  VAL   B CG2 1 
ATOM   3115 N N   . GLY   B 1 32  ? -0.381  11.818  1.214   1.00 20.38 ? 33  GLY   B N   1 
ATOM   3116 C CA  . GLY   B 1 32  ? -1.751  11.436  0.909   1.00 20.95 ? 33  GLY   B CA  1 
ATOM   3117 C C   . GLY   B 1 32  ? -2.336  12.368  -0.132  1.00 21.48 ? 33  GLY   B C   1 
ATOM   3118 O O   . GLY   B 1 32  ? -2.080  13.572  -0.108  1.00 20.20 ? 33  GLY   B O   1 
ATOM   3119 N N   . VAL   B 1 33  ? -3.114  11.799  -1.048  1.00 21.25 ? 34  VAL   B N   1 
ATOM   3120 C CA  . VAL   B 1 33  ? -3.872  12.556  -2.036  1.00 21.86 ? 34  VAL   B CA  1 
ATOM   3121 C C   . VAL   B 1 33  ? -5.332  12.147  -1.926  1.00 23.01 ? 34  VAL   B C   1 
ATOM   3122 O O   . VAL   B 1 33  ? -5.650  10.956  -1.811  1.00 23.24 ? 34  VAL   B O   1 
ATOM   3123 C CB  . VAL   B 1 33  ? -3.346  12.319  -3.469  1.00 24.53 ? 34  VAL   B CB  1 
ATOM   3124 C CG1 . VAL   B 1 33  ? -4.220  13.046  -4.500  1.00 22.85 ? 34  VAL   B CG1 1 
ATOM   3125 C CG2 . VAL   B 1 33  ? -1.894  12.777  -3.580  1.00 21.11 ? 34  VAL   B CG2 1 
ATOM   3126 N N   . ILE   B 1 34  ? -6.228  13.124  -1.961  1.00 23.82 ? 35  ILE   B N   1 
ATOM   3127 C CA  . ILE   B 1 34  ? -7.647  12.833  -2.092  1.00 25.25 ? 35  ILE   B CA  1 
ATOM   3128 C C   . ILE   B 1 34  ? -8.138  13.478  -3.378  1.00 25.70 ? 35  ILE   B C   1 
ATOM   3129 O O   . ILE   B 1 34  ? -7.831  14.642  -3.655  1.00 26.43 ? 35  ILE   B O   1 
ATOM   3130 C CB  . ILE   B 1 34  ? -8.458  13.294  -0.866  1.00 25.96 ? 35  ILE   B CB  1 
ATOM   3131 C CG1 . ILE   B 1 34  ? -9.935  12.878  -1.042  1.00 29.02 ? 35  ILE   B CG1 1 
ATOM   3132 C CG2 . ILE   B 1 34  ? -8.285  14.787  -0.617  1.00 29.72 ? 35  ILE   B CG2 1 
ATOM   3133 C CD1 . ILE   B 1 34  ? -10.832 13.236  0.120   1.00 32.35 ? 35  ILE   B CD1 1 
ATOM   3134 N N   . GLN   B 1 35  ? -8.852  12.704  -4.190  1.00 26.52 ? 36  GLN   B N   1 
ATOM   3135 C CA  . GLN   B 1 35  ? -9.437  13.218  -5.420  1.00 30.27 ? 36  GLN   B CA  1 
ATOM   3136 C C   . GLN   B 1 35  ? -10.780 12.544  -5.627  1.00 34.95 ? 36  GLN   B C   1 
ATOM   3137 O O   . GLN   B 1 35  ? -10.856 11.312  -5.639  1.00 32.91 ? 36  GLN   B O   1 
ATOM   3138 C CB  . GLN   B 1 35  ? -8.535  12.982  -6.633  1.00 32.38 ? 36  GLN   B CB  1 
ATOM   3139 C CG  . GLN   B 1 35  ? -9.106  13.627  -7.894  1.00 36.62 ? 36  GLN   B CG  1 
ATOM   3140 C CD  . GLN   B 1 35  ? -8.389  13.219  -9.162  1.00 40.73 ? 36  GLN   B CD  1 
ATOM   3141 O OE1 . GLN   B 1 35  ? -8.015  12.061  -9.335  1.00 35.75 ? 36  GLN   B OE1 1 
ATOM   3142 N NE2 . GLN   B 1 35  ? -8.192  14.177  -10.060 1.00 41.56 ? 36  GLN   B NE2 1 
ATOM   3143 N N   . ASN   B 1 36  ? -11.827 13.354  -5.783  1.00 33.27 ? 37  ASN   B N   1 
ATOM   3144 C CA  . ASN   B 1 36  ? -13.176 12.854  -6.036  1.00 39.54 ? 37  ASN   B CA  1 
ATOM   3145 C C   . ASN   B 1 36  ? -13.611 11.877  -4.947  1.00 39.76 ? 37  ASN   B C   1 
ATOM   3146 O O   . ASN   B 1 36  ? -14.127 10.792  -5.220  1.00 37.87 ? 37  ASN   B O   1 
ATOM   3147 C CB  . ASN   B 1 36  ? -13.268 12.212  -7.421  1.00 37.01 ? 37  ASN   B CB  1 
ATOM   3148 C CG  . ASN   B 1 36  ? -12.989 13.194  -8.533  1.00 38.00 ? 37  ASN   B CG  1 
ATOM   3149 O OD1 . ASN   B 1 36  ? -13.387 14.357  -8.461  1.00 43.17 ? 37  ASN   B OD1 1 
ATOM   3150 N ND2 . ASN   B 1 36  ? -12.291 12.737  -9.565  1.00 37.88 ? 37  ASN   B ND2 1 
ATOM   3151 N N   . ASN   B 1 37  ? -13.371 12.265  -3.697  1.00 35.83 ? 38  ASN   B N   1 
ATOM   3152 C CA  . ASN   B 1 37  ? -13.774 11.508  -2.515  1.00 40.69 ? 38  ASN   B CA  1 
ATOM   3153 C C   . ASN   B 1 37  ? -13.074 10.152  -2.401  1.00 38.57 ? 38  ASN   B C   1 
ATOM   3154 O O   . ASN   B 1 37  ? -13.506 9.303   -1.611  1.00 47.21 ? 38  ASN   B O   1 
ATOM   3155 C CB  . ASN   B 1 37  ? -15.302 11.317  -2.470  1.00 40.79 ? 38  ASN   B CB  1 
ATOM   3156 C CG  . ASN   B 1 37  ? -16.066 12.636  -2.595  1.00 49.31 ? 38  ASN   B CG  1 
ATOM   3157 O OD1 . ASN   B 1 37  ? -16.219 13.177  -3.694  1.00 51.22 ? 38  ASN   B OD1 1 
ATOM   3158 N ND2 . ASN   B 1 37  ? -16.553 13.153  -1.470  1.00 43.72 ? 38  ASN   B ND2 1 
ATOM   3159 N N   . LYS   B 1 38  ? -12.010 9.915   -3.165  1.00 36.39 ? 39  LYS   B N   1 
ATOM   3160 C CA  . LYS   B 1 38  ? -11.190 8.715   -3.025  1.00 33.18 ? 39  LYS   B CA  1 
ATOM   3161 C C   . LYS   B 1 38  ? -9.818  9.094   -2.478  1.00 32.36 ? 39  LYS   B C   1 
ATOM   3162 O O   . LYS   B 1 38  ? -9.185  10.028  -2.979  1.00 30.42 ? 39  LYS   B O   1 
ATOM   3163 C CB  . LYS   B 1 38  ? -11.036 7.988   -4.362  1.00 37.86 ? 39  LYS   B CB  1 
ATOM   3164 C CG  . LYS   B 1 38  ? -12.250 7.144   -4.763  1.00 41.40 ? 39  LYS   B CG  1 
ATOM   3165 C CD  . LYS   B 1 38  ? -11.817 5.896   -5.538  1.00 49.68 ? 39  LYS   B CD  1 
ATOM   3166 C CE  . LYS   B 1 38  ? -10.490 5.348   -4.994  1.00 50.79 ? 39  LYS   B CE  1 
ATOM   3167 N NZ  . LYS   B 1 38  ? -10.123 4.006   -5.541  1.00 50.50 ? 39  LYS   B NZ  1 
ATOM   3168 N N   . LYS   B 1 39  ? -9.351  8.347   -1.479  1.00 26.72 ? 40  LYS   B N   1 
ATOM   3169 C CA  . LYS   B 1 39  ? -8.106  8.635   -0.782  1.00 26.57 ? 40  LYS   B CA  1 
ATOM   3170 C C   . LYS   B 1 39  ? -6.993  7.694   -1.233  1.00 27.26 ? 40  LYS   B C   1 
ATOM   3171 O O   . LYS   B 1 39  ? -7.225  6.517   -1.525  1.00 27.25 ? 40  LYS   B O   1 
ATOM   3172 C CB  . LYS   B 1 39  ? -8.298  8.517   0.734   1.00 27.07 ? 40  LYS   B CB  1 
ATOM   3173 C CG  . LYS   B 1 39  ? -9.326  9.484   1.308   1.00 26.75 ? 40  LYS   B CG  1 
ATOM   3174 C CD  . LYS   B 1 39  ? -9.586  9.190   2.782   1.00 29.34 ? 40  LYS   B CD  1 
ATOM   3175 C CE  . LYS   B 1 39  ? -10.677 10.096  3.358   1.00 28.35 ? 40  LYS   B CE  1 
ATOM   3176 N NZ  . LYS   B 1 39  ? -10.960 9.777   4.788   1.00 29.06 ? 40  LYS   B NZ  1 
ATOM   3177 N N   . TYR   B 1 40  ? -5.769  8.222   -1.256  1.00 23.71 ? 41  TYR   B N   1 
ATOM   3178 C CA  . TYR   B 1 40  ? -4.593  7.470   -1.689  1.00 26.72 ? 41  TYR   B CA  1 
ATOM   3179 C C   . TYR   B 1 40  ? -3.474  7.735   -0.691  1.00 24.35 ? 41  TYR   B C   1 
ATOM   3180 O O   . TYR   B 1 40  ? -3.099  8.892   -0.478  1.00 25.46 ? 41  TYR   B O   1 
ATOM   3181 C CB  . TYR   B 1 40  ? -4.177  7.886   -3.107  1.00 28.22 ? 41  TYR   B CB  1 
ATOM   3182 C CG  . TYR   B 1 40  ? -5.302  7.759   -4.115  1.00 30.49 ? 41  TYR   B CG  1 
ATOM   3183 C CD1 . TYR   B 1 40  ? -5.501  6.573   -4.807  1.00 33.67 ? 41  TYR   B CD1 1 
ATOM   3184 C CD2 . TYR   B 1 40  ? -6.175  8.814   -4.360  1.00 28.46 ? 41  TYR   B CD2 1 
ATOM   3185 C CE1 . TYR   B 1 40  ? -6.525  6.442   -5.718  1.00 36.04 ? 41  TYR   B CE1 1 
ATOM   3186 C CE2 . TYR   B 1 40  ? -7.214  8.688   -5.271  1.00 34.26 ? 41  TYR   B CE2 1 
ATOM   3187 C CZ  . TYR   B 1 40  ? -7.377  7.497   -5.947  1.00 36.93 ? 41  TYR   B CZ  1 
ATOM   3188 O OH  . TYR   B 1 40  ? -8.398  7.353   -6.857  1.00 39.05 ? 41  TYR   B OH  1 
ATOM   3189 N N   . GLU   B 1 41  ? -2.962  6.674   -0.067  1.00 27.46 ? 42  GLU   B N   1 
ATOM   3190 C CA  . GLU   B 1 41  ? -1.936  6.775   0.962   1.00 23.60 ? 42  GLU   B CA  1 
ATOM   3191 C C   . GLU   B 1 41  ? -0.626  6.212   0.432   1.00 24.85 ? 42  GLU   B C   1 
ATOM   3192 O O   . GLU   B 1 41  ? -0.606  5.118   -0.144  1.00 22.73 ? 42  GLU   B O   1 
ATOM   3193 C CB  . GLU   B 1 41  ? -2.349  6.013   2.226   1.00 26.91 ? 42  GLU   B CB  1 
ATOM   3194 C CG  . GLU   B 1 41  ? -3.624  6.530   2.887   1.00 25.74 ? 42  GLU   B CG  1 
ATOM   3195 C CD  . GLU   B 1 41  ? -4.069  5.640   4.036   1.00 29.07 ? 42  GLU   B CD  1 
ATOM   3196 O OE1 . GLU   B 1 41  ? -3.260  4.802   4.488   1.00 31.08 ? 42  GLU   B OE1 1 
ATOM   3197 O OE2 . GLU   B 1 41  ? -5.240  5.757   4.469   1.00 36.38 ? 42  GLU   B OE2 1 
ATOM   3198 N N   . MET   B 1 42  ? 0.461   6.946   0.640   1.00 22.96 ? 43  MET   B N   1 
ATOM   3199 C CA  . MET   B 1 42  ? 1.781   6.513   0.202   1.00 25.03 ? 43  MET   B CA  1 
ATOM   3200 C C   . MET   B 1 42  ? 2.792   6.761   1.312   1.00 22.92 ? 43  MET   B C   1 
ATOM   3201 O O   . MET   B 1 42  ? 2.910   7.884   1.809   1.00 22.73 ? 43  MET   B O   1 
ATOM   3202 C CB  . MET   B 1 42  ? 2.179   7.241   -1.088  1.00 24.31 ? 43  MET   B CB  1 
ATOM   3203 C CG  . MET   B 1 42  ? 1.447   6.673   -2.296  1.00 31.27 ? 43  MET   B CG  1 
ATOM   3204 S SD  . MET   B 1 42  ? 0.804   7.890   -3.462  1.00 40.36 ? 43  MET   B SD  1 
ATOM   3205 C CE  . MET   B 1 42  ? -0.223  8.964   -2.429  1.00 27.04 ? 43  MET   B CE  1 
ATOM   3206 N N   . TYR   B 1 43  ? 3.515   5.709   1.699   1.00 21.32 ? 44  TYR   B N   1 
ATOM   3207 C CA  . TYR   B 1 43  ? 4.463   5.760   2.804   1.00 21.07 ? 44  TYR   B CA  1 
ATOM   3208 C C   . TYR   B 1 43  ? 5.863   5.438   2.300   1.00 22.77 ? 44  TYR   B C   1 
ATOM   3209 O O   . TYR   B 1 43  ? 6.038   4.587   1.423   1.00 23.29 ? 44  TYR   B O   1 
ATOM   3210 C CB  . TYR   B 1 43  ? 4.048   4.776   3.934   1.00 21.50 ? 44  TYR   B CB  1 
ATOM   3211 C CG  . TYR   B 1 43  ? 2.656   5.069   4.436   1.00 22.48 ? 44  TYR   B CG  1 
ATOM   3212 C CD1 . TYR   B 1 43  ? 2.415   6.152   5.276   1.00 23.45 ? 44  TYR   B CD1 1 
ATOM   3213 C CD2 . TYR   B 1 43  ? 1.572   4.300   4.036   1.00 22.67 ? 44  TYR   B CD2 1 
ATOM   3214 C CE1 . TYR   B 1 43  ? 1.128   6.447   5.717   1.00 21.40 ? 44  TYR   B CE1 1 
ATOM   3215 C CE2 . TYR   B 1 43  ? 0.283   4.587   4.480   1.00 25.39 ? 44  TYR   B CE2 1 
ATOM   3216 C CZ  . TYR   B 1 43  ? 0.075   5.666   5.317   1.00 24.61 ? 44  TYR   B CZ  1 
ATOM   3217 O OH  . TYR   B 1 43  ? -1.198  5.972   5.752   1.00 23.83 ? 44  TYR   B OH  1 
ATOM   3218 N N   . TYR   B 1 44  ? 6.854   6.152   2.846   1.00 22.26 ? 45  TYR   B N   1 
ATOM   3219 C CA  . TYR   B 1 44  ? 8.258   5.947   2.525   1.00 22.07 ? 45  TYR   B CA  1 
ATOM   3220 C C   . TYR   B 1 44  ? 9.090   5.876   3.795   1.00 22.61 ? 45  TYR   B C   1 
ATOM   3221 O O   . TYR   B 1 44  ? 8.866   6.628   4.750   1.00 21.79 ? 45  TYR   B O   1 
ATOM   3222 C CB  . TYR   B 1 44  ? 8.825   7.095   1.668   1.00 23.78 ? 45  TYR   B CB  1 
ATOM   3223 C CG  . TYR   B 1 44  ? 8.137   7.331   0.349   1.00 24.02 ? 45  TYR   B CG  1 
ATOM   3224 C CD1 . TYR   B 1 44  ? 8.447   6.572   -0.768  1.00 24.63 ? 45  TYR   B CD1 1 
ATOM   3225 C CD2 . TYR   B 1 44  ? 7.215   8.361   0.207   1.00 27.63 ? 45  TYR   B CD2 1 
ATOM   3226 C CE1 . TYR   B 1 44  ? 7.832   6.804   -1.974  1.00 29.13 ? 45  TYR   B CE1 1 
ATOM   3227 C CE2 . TYR   B 1 44  ? 6.596   8.602   -0.999  1.00 27.85 ? 45  TYR   B CE2 1 
ATOM   3228 C CZ  . TYR   B 1 44  ? 6.909   7.823   -2.087  1.00 30.25 ? 45  TYR   B CZ  1 
ATOM   3229 O OH  . TYR   B 1 44  ? 6.291   8.065   -3.286  1.00 30.96 ? 45  TYR   B OH  1 
ATOM   3230 N N   . GLY   B 1 45  ? 10.082  4.996   3.788   1.00 21.71 ? 46  GLY   B N   1 
ATOM   3231 C CA  . GLY   B 1 45  ? 11.098  5.133   4.807   1.00 23.62 ? 46  GLY   B CA  1 
ATOM   3232 C C   . GLY   B 1 45  ? 10.677  4.652   6.186   1.00 23.29 ? 46  GLY   B C   1 
ATOM   3233 O O   . GLY   B 1 45  ? 9.777   3.813   6.350   1.00 21.99 ? 46  GLY   B O   1 
ATOM   3234 N N   . LEU   B 1 46  ? 11.349  5.218   7.195   1.00 21.65 ? 47  LEU   B N   1 
ATOM   3235 C CA  . LEU   B 1 46  ? 11.358  4.733   8.566   1.00 25.46 ? 47  LEU   B CA  1 
ATOM   3236 C C   . LEU   B 1 46  ? 10.943  5.836   9.532   1.00 23.28 ? 47  LEU   B C   1 
ATOM   3237 O O   . LEU   B 1 46  ? 11.107  7.028   9.251   1.00 26.57 ? 47  LEU   B O   1 
ATOM   3238 C CB  . LEU   B 1 46  ? 12.753  4.225   8.956   1.00 26.00 ? 47  LEU   B CB  1 
ATOM   3239 C CG  . LEU   B 1 46  ? 13.390  3.224   7.989   1.00 23.30 ? 47  LEU   B CG  1 
ATOM   3240 C CD1 . LEU   B 1 46  ? 14.807  2.913   8.416   1.00 27.29 ? 47  LEU   B CD1 1 
ATOM   3241 C CD2 . LEU   B 1 46  ? 12.552  1.951   7.887   1.00 22.57 ? 47  LEU   B CD2 1 
ATOM   3242 N N   . GLN   B 1 47  ? 10.412  5.425   10.687  1.00 24.49 ? 48  GLN   B N   1 
ATOM   3243 C CA  . GLN   B 1 47  ? 9.977   6.393   11.690  1.00 28.22 ? 48  GLN   B CA  1 
ATOM   3244 C C   . GLN   B 1 47  ? 11.153  7.137   12.309  1.00 31.95 ? 48  GLN   B C   1 
ATOM   3245 O O   . GLN   B 1 47  ? 11.018  8.311   12.674  1.00 30.72 ? 48  GLN   B O   1 
ATOM   3246 C CB  . GLN   B 1 47  ? 9.153   5.694   12.771  1.00 27.98 ? 48  GLN   B CB  1 
ATOM   3247 C CG  . GLN   B 1 47  ? 7.850   5.116   12.234  1.00 26.09 ? 48  GLN   B CG  1 
ATOM   3248 C CD  . GLN   B 1 47  ? 6.920   4.599   13.319  1.00 33.33 ? 48  GLN   B CD  1 
ATOM   3249 O OE1 . GLN   B 1 47  ? 5.708   4.489   13.109  1.00 33.34 ? 48  GLN   B OE1 1 
ATOM   3250 N NE2 . GLN   B 1 47  ? 7.478   4.271   14.476  1.00 36.06 ? 48  GLN   B NE2 1 
ATOM   3251 N N   . SER   B 1 48  ? 12.301  6.475   12.429  1.00 32.08 ? 49  SER   B N   1 
ATOM   3252 C CA  . SER   B 1 48  ? 13.523  7.077   12.945  1.00 40.12 ? 49  SER   B CA  1 
ATOM   3253 C C   . SER   B 1 48  ? 14.689  6.191   12.538  1.00 39.94 ? 49  SER   B C   1 
ATOM   3254 O O   . SER   B 1 48  ? 14.527  4.988   12.317  1.00 35.75 ? 49  SER   B O   1 
ATOM   3255 C CB  . SER   B 1 48  ? 13.485  7.234   14.471  1.00 38.29 ? 49  SER   B CB  1 
ATOM   3256 O OG  . SER   B 1 48  ? 13.556  5.968   15.114  1.00 42.60 ? 49  SER   B OG  1 
ATOM   3257 N N   . VAL   B 1 49  ? 15.877  6.797   12.447  1.00 43.18 ? 50  VAL   B N   1 
ATOM   3258 C CA  . VAL   B 1 49  ? 17.068  5.980   12.251  1.00 43.95 ? 50  VAL   B CA  1 
ATOM   3259 C C   . VAL   B 1 49  ? 17.346  5.122   13.479  1.00 43.76 ? 50  VAL   B C   1 
ATOM   3260 O O   . VAL   B 1 49  ? 18.050  4.113   13.375  1.00 43.70 ? 50  VAL   B O   1 
ATOM   3261 C CB  . VAL   B 1 49  ? 18.293  6.847   11.893  1.00 46.92 ? 50  VAL   B CB  1 
ATOM   3262 C CG1 . VAL   B 1 49  ? 17.915  7.897   10.858  1.00 42.96 ? 50  VAL   B CG1 1 
ATOM   3263 C CG2 . VAL   B 1 49  ? 18.892  7.488   13.134  1.00 49.23 ? 50  VAL   B CG2 1 
ATOM   3264 N N   . GLN   B 1 50  ? 16.779  5.473   14.637  1.00 44.78 ? 51  GLN   B N   1 
ATOM   3265 C CA  . GLN   B 1 50  ? 16.999  4.673   15.837  1.00 48.92 ? 51  GLN   B CA  1 
ATOM   3266 C C   . GLN   B 1 50  ? 16.138  3.411   15.856  1.00 41.74 ? 51  GLN   B C   1 
ATOM   3267 O O   . GLN   B 1 50  ? 16.642  2.322   16.150  1.00 45.30 ? 51  GLN   B O   1 
ATOM   3268 C CB  . GLN   B 1 50  ? 16.746  5.511   17.095  1.00 52.86 ? 51  GLN   B CB  1 
ATOM   3269 C CG  . GLN   B 1 50  ? 16.835  4.700   18.388  1.00 60.18 ? 51  GLN   B CG  1 
ATOM   3270 C CD  . GLN   B 1 50  ? 16.866  5.564   19.636  1.00 70.59 ? 51  GLN   B CD  1 
ATOM   3271 O OE1 . GLN   B 1 50  ? 17.172  5.084   20.729  1.00 74.60 ? 51  GLN   B OE1 1 
ATOM   3272 N NE2 . GLN   B 1 50  ? 16.551  6.846   19.479  1.00 74.74 ? 51  GLN   B NE2 1 
ATOM   3273 N N   . ASP   B 1 51  ? 14.836  3.524   15.568  1.00 43.35 ? 52  ASP   B N   1 
ATOM   3274 C CA  . ASP   B 1 51  ? 13.987  2.337   15.655  1.00 40.07 ? 52  ASP   B CA  1 
ATOM   3275 C C   . ASP   B 1 51  ? 13.962  1.525   14.361  1.00 34.59 ? 52  ASP   B C   1 
ATOM   3276 O O   . ASP   B 1 51  ? 13.723  0.313   14.409  1.00 35.54 ? 52  ASP   B O   1 
ATOM   3277 C CB  . ASP   B 1 51  ? 12.555  2.711   16.100  1.00 42.00 ? 52  ASP   B CB  1 
ATOM   3278 C CG  . ASP   B 1 51  ? 11.733  3.499   15.042  1.00 40.51 ? 52  ASP   B CG  1 
ATOM   3279 O OD1 . ASP   B 1 51  ? 12.178  3.743   13.896  1.00 35.49 ? 52  ASP   B OD1 1 
ATOM   3280 O OD2 . ASP   B 1 51  ? 10.585  3.878   15.389  1.00 38.14 ? 52  ASP   B OD2 1 
ATOM   3281 N N   . LYS   B 1 52  ? 14.231  2.160   13.219  1.00 34.37 ? 53  LYS   B N   1 
ATOM   3282 C CA  . LYS   B 1 52  ? 14.225  1.513   11.904  1.00 31.11 ? 53  LYS   B CA  1 
ATOM   3283 C C   . LYS   B 1 52  ? 12.904  0.793   11.620  1.00 30.91 ? 53  LYS   B C   1 
ATOM   3284 O O   . LYS   B 1 52  ? 12.872  -0.252  10.955  1.00 26.01 ? 53  LYS   B O   1 
ATOM   3285 C CB  . LYS   B 1 52  ? 15.428  0.575   11.746  1.00 36.00 ? 53  LYS   B CB  1 
ATOM   3286 C CG  . LYS   B 1 52  ? 16.756  1.335   11.881  1.00 38.52 ? 53  LYS   B CG  1 
ATOM   3287 C CD  . LYS   B 1 52  ? 17.938  0.606   11.272  1.00 41.51 ? 53  LYS   B CD  1 
ATOM   3288 C CE  . LYS   B 1 52  ? 19.182  1.483   11.273  1.00 37.60 ? 53  LYS   B CE  1 
ATOM   3289 N NZ  . LYS   B 1 52  ? 19.684  1.742   12.649  1.00 44.63 ? 53  LYS   B NZ  1 
ATOM   3290 N N   . LYS   B 1 53  ? 11.806  1.365   12.108  1.00 30.36 ? 54  LYS   B N   1 
ATOM   3291 C CA  . LYS   B 1 53  ? 10.467  0.854   11.859  1.00 25.96 ? 54  LYS   B CA  1 
ATOM   3292 C C   . LYS   B 1 53  ? 9.844   1.550   10.660  1.00 24.01 ? 54  LYS   B C   1 
ATOM   3293 O O   . LYS   B 1 53  ? 9.946   2.768   10.516  1.00 24.05 ? 54  LYS   B O   1 
ATOM   3294 C CB  . LYS   B 1 53  ? 9.572   1.055   13.084  1.00 32.72 ? 54  LYS   B CB  1 
ATOM   3295 C CG  . LYS   B 1 53  ? 9.414   -0.193  13.940  1.00 39.33 ? 54  LYS   B CG  1 
ATOM   3296 C CD  . LYS   B 1 53  ? 10.745  -0.640  14.515  1.00 43.81 ? 54  LYS   B CD  1 
ATOM   3297 C CE  . LYS   B 1 53  ? 10.703  -2.088  14.963  1.00 45.21 ? 54  LYS   B CE  1 
ATOM   3298 N NZ  . LYS   B 1 53  ? 10.690  -3.040  13.797  1.00 39.93 ? 54  LYS   B NZ  1 
ATOM   3299 N N   . ALA   B 1 54  ? 9.171   0.768   9.821   1.00 23.28 ? 55  ALA   B N   1 
ATOM   3300 C CA  . ALA   B 1 54  ? 8.545   1.310   8.624   1.00 22.87 ? 55  ALA   B CA  1 
ATOM   3301 C C   . ALA   B 1 54  ? 7.520   2.378   8.979   1.00 23.49 ? 55  ALA   B C   1 
ATOM   3302 O O   . ALA   B 1 54  ? 6.718   2.203   9.901   1.00 24.54 ? 55  ALA   B O   1 
ATOM   3303 C CB  . ALA   B 1 54  ? 7.851   0.196   7.845   1.00 23.35 ? 55  ALA   B CB  1 
ATOM   3304 N N   . VAL   B 1 55  ? 7.545   3.488   8.233   1.00 22.02 ? 56  VAL   B N   1 
ATOM   3305 C CA  . VAL   B 1 55  ? 6.438   4.431   8.282   1.00 23.26 ? 56  VAL   B CA  1 
ATOM   3306 C C   . VAL   B 1 55  ? 5.198   3.756   7.714   1.00 22.35 ? 56  VAL   B C   1 
ATOM   3307 O O   . VAL   B 1 55  ? 5.261   3.049   6.696   1.00 23.86 ? 56  VAL   B O   1 
ATOM   3308 C CB  . VAL   B 1 55  ? 6.773   5.722   7.516   1.00 22.00 ? 56  VAL   B CB  1 
ATOM   3309 C CG1 . VAL   B 1 55  ? 5.518   6.604   7.368   1.00 22.08 ? 56  VAL   B CG1 1 
ATOM   3310 C CG2 . VAL   B 1 55  ? 7.871   6.458   8.242   1.00 22.18 ? 56  VAL   B CG2 1 
ATOM   3311 N N   . ASN   B 1 56  ? 4.068   3.949   8.390   1.00 23.76 ? 57  ASN   B N   1 
ATOM   3312 C CA  . ASN   B 1 56  ? 2.839   3.257   8.043   1.00 24.56 ? 57  ASN   B CA  1 
ATOM   3313 C C   . ASN   B 1 56  ? 1.643   4.124   8.432   1.00 23.73 ? 57  ASN   B C   1 
ATOM   3314 O O   . ASN   B 1 56  ? 1.789   5.256   8.910   1.00 23.99 ? 57  ASN   B O   1 
ATOM   3315 C CB  . ASN   B 1 56  ? 2.802   1.895   8.741   1.00 25.44 ? 57  ASN   B CB  1 
ATOM   3316 C CG  . ASN   B 1 56  ? 2.791   2.032   10.245  1.00 29.15 ? 57  ASN   B CG  1 
ATOM   3317 O OD1 . ASN   B 1 56  ? 1.729   2.121   10.853  1.00 32.72 ? 57  ASN   B OD1 1 
ATOM   3318 N ND2 . ASN   B 1 56  ? 3.977   2.079   10.855  1.00 32.16 ? 57  ASN   B ND2 1 
ATOM   3319 N N   . SER   B 1 57  ? 0.442   3.577   8.226   1.00 25.83 ? 58  SER   B N   1 
ATOM   3320 C CA  . SER   B 1 57  ? -0.786  4.331   8.456   1.00 23.93 ? 58  SER   B CA  1 
ATOM   3321 C C   . SER   B 1 57  ? -1.034  4.642   9.926   1.00 26.44 ? 58  SER   B C   1 
ATOM   3322 O O   . SER   B 1 57  ? -1.930  5.448   10.222  1.00 25.95 ? 58  SER   B O   1 
ATOM   3323 C CB  . SER   B 1 57  ? -1.988  3.574   7.887   1.00 25.69 ? 58  SER   B CB  1 
ATOM   3324 O OG  . SER   B 1 57  ? -2.103  2.312   8.511   1.00 27.95 ? 58  SER   B OG  1 
ATOM   3325 N N   . SER   B 1 58  ? -0.284  4.026   10.843  1.00 23.91 ? 59  SER   B N   1 
ATOM   3326 C CA  . SER   B 1 58  ? -0.350  4.364   12.260  1.00 25.67 ? 59  SER   B CA  1 
ATOM   3327 C C   . SER   B 1 58  ? 0.738   5.332   12.714  1.00 26.33 ? 59  SER   B C   1 
ATOM   3328 O O   . SER   B 1 58  ? 0.680   5.804   13.857  1.00 26.43 ? 59  SER   B O   1 
ATOM   3329 C CB  . SER   B 1 58  ? -0.262  3.093   13.116  1.00 29.56 ? 59  SER   B CB  1 
ATOM   3330 O OG  . SER   B 1 58  ? -1.396  2.273   12.910  1.00 31.58 ? 59  SER   B OG  1 
ATOM   3331 N N   . THR   B 1 59  ? 1.719   5.645   11.864  1.00 24.12 ? 60  THR   B N   1 
ATOM   3332 C CA  . THR   B 1 59  ? 2.797   6.540   12.275  1.00 23.18 ? 60  THR   B CA  1 
ATOM   3333 C C   . THR   B 1 59  ? 2.252   7.921   12.627  1.00 24.58 ? 60  THR   B C   1 
ATOM   3334 O O   . THR   B 1 59  ? 1.430   8.479   11.899  1.00 22.80 ? 60  THR   B O   1 
ATOM   3335 C CB  . THR   B 1 59  ? 3.841   6.651   11.167  1.00 24.29 ? 60  THR   B CB  1 
ATOM   3336 O OG1 . THR   B 1 59  ? 4.373   5.345   10.909  1.00 25.40 ? 60  THR   B OG1 1 
ATOM   3337 C CG2 . THR   B 1 59  ? 4.980   7.587   11.594  1.00 24.71 ? 60  THR   B CG2 1 
ATOM   3338 N N   . ILE   B 1 60  ? 2.719   8.473   13.747  1.00 22.40 ? 61  ILE   B N   1 
ATOM   3339 C CA  . ILE   B 1 60  ? 2.246   9.763   14.253  1.00 25.75 ? 61  ILE   B CA  1 
ATOM   3340 C C   . ILE   B 1 60  ? 3.292   10.831  13.952  1.00 21.51 ? 61  ILE   B C   1 
ATOM   3341 O O   . ILE   B 1 60  ? 4.475   10.660  14.269  1.00 24.48 ? 61  ILE   B O   1 
ATOM   3342 C CB  . ILE   B 1 60  ? 1.945   9.686   15.762  1.00 25.99 ? 61  ILE   B CB  1 
ATOM   3343 C CG1 . ILE   B 1 60  ? 0.726   8.795   16.007  1.00 27.30 ? 61  ILE   B CG1 1 
ATOM   3344 C CG2 . ILE   B 1 60  ? 1.701   11.072  16.340  1.00 27.24 ? 61  ILE   B CG2 1 
ATOM   3345 C CD1 . ILE   B 1 60  ? 0.463   8.503   17.484  1.00 32.85 ? 61  ILE   B CD1 1 
ATOM   3346 N N   . PHE   B 1 61  ? 2.850   11.935  13.342  1.00 24.73 ? 62  PHE   B N   1 
ATOM   3347 C CA  . PHE   B 1 61  ? 3.701   13.058  12.968  1.00 23.02 ? 62  PHE   B CA  1 
ATOM   3348 C C   . PHE   B 1 61  ? 3.255   14.302  13.724  1.00 24.98 ? 62  PHE   B C   1 
ATOM   3349 O O   . PHE   B 1 61  ? 2.062   14.503  13.943  1.00 24.06 ? 62  PHE   B O   1 
ATOM   3350 C CB  . PHE   B 1 61  ? 3.627   13.363  11.465  1.00 24.38 ? 62  PHE   B CB  1 
ATOM   3351 C CG  . PHE   B 1 61  ? 4.127   12.256  10.569  1.00 20.36 ? 62  PHE   B CG  1 
ATOM   3352 C CD1 . PHE   B 1 61  ? 3.337   11.162  10.275  1.00 24.18 ? 62  PHE   B CD1 1 
ATOM   3353 C CD2 . PHE   B 1 61  ? 5.377   12.344  9.988   1.00 23.29 ? 62  PHE   B CD2 1 
ATOM   3354 C CE1 . PHE   B 1 61  ? 3.798   10.165  9.424   1.00 22.86 ? 62  PHE   B CE1 1 
ATOM   3355 C CE2 . PHE   B 1 61  ? 5.851   11.356  9.135   1.00 21.62 ? 62  PHE   B CE2 1 
ATOM   3356 C CZ  . PHE   B 1 61  ? 5.063   10.258  8.860   1.00 23.25 ? 62  PHE   B CZ  1 
ATOM   3357 N N   . GLU   B 1 62  ? 4.210   15.152  14.093  1.00 21.89 ? 63  GLU   B N   1 
ATOM   3358 C CA  . GLU   B 1 62  ? 3.876   16.445  14.676  1.00 23.35 ? 63  GLU   B CA  1 
ATOM   3359 C C   . GLU   B 1 62  ? 3.519   17.419  13.559  1.00 23.30 ? 63  GLU   B C   1 
ATOM   3360 O O   . GLU   B 1 62  ? 4.245   17.509  12.564  1.00 23.61 ? 63  GLU   B O   1 
ATOM   3361 C CB  . GLU   B 1 62  ? 5.050   16.985  15.493  1.00 25.70 ? 63  GLU   B CB  1 
ATOM   3362 C CG  . GLU   B 1 62  ? 5.382   16.115  16.708  1.00 26.20 ? 63  GLU   B CG  1 
ATOM   3363 C CD  . GLU   B 1 62  ? 6.668   16.528  17.411  1.00 32.67 ? 63  GLU   B CD  1 
ATOM   3364 O OE1 . GLU   B 1 62  ? 7.281   17.529  16.999  1.00 30.25 ? 63  GLU   B OE1 1 
ATOM   3365 O OE2 . GLU   B 1 62  ? 7.072   15.844  18.380  1.00 32.58 ? 63  GLU   B OE2 1 
ATOM   3366 N N   . LEU   B 1 63  ? 2.412   18.149  13.727  1.00 20.56 ? 64  LEU   B N   1 
ATOM   3367 C CA  . LEU   B 1 63  ? 1.919   19.063  12.695  1.00 21.23 ? 64  LEU   B CA  1 
ATOM   3368 C C   . LEU   B 1 63  ? 2.538   20.457  12.746  1.00 22.22 ? 64  LEU   B C   1 
ATOM   3369 O O   . LEU   B 1 63  ? 2.397   21.213  11.773  1.00 21.99 ? 64  LEU   B O   1 
ATOM   3370 C CB  . LEU   B 1 63  ? 0.393   19.209  12.777  1.00 21.43 ? 64  LEU   B CB  1 
ATOM   3371 C CG  . LEU   B 1 63  ? -0.389  17.903  12.586  1.00 21.90 ? 64  LEU   B CG  1 
ATOM   3372 C CD1 . LEU   B 1 63  ? -1.868  18.167  12.477  1.00 21.78 ? 64  LEU   B CD1 1 
ATOM   3373 C CD2 . LEU   B 1 63  ? 0.126   17.118  11.374  1.00 24.14 ? 64  LEU   B CD2 1 
ATOM   3374 N N   . GLY   B 1 64  ? 3.206   20.826  13.836  1.00 23.22 ? 65  GLY   B N   1 
ATOM   3375 C CA  . GLY   B 1 64  ? 3.765   22.171  13.893  1.00 22.72 ? 65  GLY   B CA  1 
ATOM   3376 C C   . GLY   B 1 64  ? 2.686   23.219  13.710  1.00 21.21 ? 65  GLY   B C   1 
ATOM   3377 O O   . GLY   B 1 64  ? 1.585   23.097  14.252  1.00 24.24 ? 65  GLY   B O   1 
ATOM   3378 N N   . SER   B 1 65  ? 2.989   24.251  12.905  1.00 19.24 ? 66  SER   B N   1 
ATOM   3379 C CA  . SER   B 1 65  ? 2.070   25.377  12.733  1.00 20.48 ? 66  SER   B CA  1 
ATOM   3380 C C   . SER   B 1 65  ? 0.773   24.969  12.060  1.00 21.75 ? 66  SER   B C   1 
ATOM   3381 O O   . SER   B 1 65  ? -0.201  25.729  12.097  1.00 21.57 ? 66  SER   B O   1 
ATOM   3382 C CB  . SER   B 1 65  ? 2.719   26.496  11.911  1.00 21.96 ? 66  SER   B CB  1 
ATOM   3383 O OG  . SER   B 1 65  ? 3.710   27.163  12.657  1.00 28.70 ? 66  SER   B OG  1 
ATOM   3384 N N   . VAL   B 1 66  ? 0.724   23.784  11.443  1.00 19.29 ? 67  VAL   B N   1 
ATOM   3385 C CA  . VAL   B 1 66  ? -0.532  23.344  10.852  1.00 19.03 ? 67  VAL   B CA  1 
ATOM   3386 C C   . VAL   B 1 66  ? -1.548  23.071  11.957  1.00 20.89 ? 67  VAL   B C   1 
ATOM   3387 O O   . VAL   B 1 66  ? -2.754  23.061  11.703  1.00 23.09 ? 67  VAL   B O   1 
ATOM   3388 C CB  . VAL   B 1 66  ? -0.266  22.138  9.918   1.00 18.62 ? 67  VAL   B CB  1 
ATOM   3389 C CG1 . VAL   B 1 66  ? -1.563  21.403  9.541   1.00 20.68 ? 67  VAL   B CG1 1 
ATOM   3390 C CG2 . VAL   B 1 66  ? 0.472   22.611  8.644   1.00 19.45 ? 67  VAL   B CG2 1 
ATOM   3391 N N   . SER   B 1 67  ? -1.082  22.924  13.204  1.00 19.89 ? 68  SER   B N   1 
ATOM   3392 C CA  . SER   B 1 67  ? -1.996  22.822  14.338  1.00 20.08 ? 68  SER   B CA  1 
ATOM   3393 C C   . SER   B 1 67  ? -2.980  23.986  14.381  1.00 21.46 ? 68  SER   B C   1 
ATOM   3394 O O   . SER   B 1 67  ? -4.093  23.839  14.911  1.00 23.55 ? 68  SER   B O   1 
ATOM   3395 C CB  . SER   B 1 67  ? -1.210  22.776  15.650  1.00 21.99 ? 68  SER   B CB  1 
ATOM   3396 O OG  . SER   B 1 67  ? -0.222  21.757  15.652  1.00 24.02 ? 68  SER   B OG  1 
ATOM   3397 N N   . LYS   B 1 68  ? -2.579  25.154  13.866  1.00 23.74 ? 69  LYS   B N   1 
ATOM   3398 C CA  . LYS   B 1 68  ? -3.444  26.332  13.878  1.00 21.14 ? 69  LYS   B CA  1 
ATOM   3399 C C   . LYS   B 1 68  ? -4.729  26.125  13.082  1.00 21.91 ? 69  LYS   B C   1 
ATOM   3400 O O   . LYS   B 1 68  ? -5.722  26.818  13.339  1.00 20.40 ? 69  LYS   B O   1 
ATOM   3401 C CB  . LYS   B 1 68  ? -2.698  27.557  13.332  1.00 21.65 ? 69  LYS   B CB  1 
ATOM   3402 C CG  . LYS   B 1 68  ? -1.554  28.032  14.204  1.00 21.55 ? 69  LYS   B CG  1 
ATOM   3403 C CD  . LYS   B 1 68  ? -0.922  29.306  13.629  1.00 21.16 ? 69  LYS   B CD  1 
ATOM   3404 C CE  . LYS   B 1 68  ? 0.244   29.767  14.491  1.00 22.93 ? 69  LYS   B CE  1 
ATOM   3405 N NZ  . LYS   B 1 68  ? 1.428   28.872  14.373  1.00 22.81 ? 69  LYS   B NZ  1 
ATOM   3406 N N   . LEU   B 1 69  ? -4.734  25.201  12.119  1.00 19.83 ? 70  LEU   B N   1 
ATOM   3407 C CA  . LEU   B 1 69  ? -5.975  24.888  11.412  1.00 20.37 ? 70  LEU   B CA  1 
ATOM   3408 C C   . LEU   B 1 69  ? -7.003  24.267  12.347  1.00 20.07 ? 70  LEU   B C   1 
ATOM   3409 O O   . LEU   B 1 69  ? -8.208  24.524  12.222  1.00 20.44 ? 70  LEU   B O   1 
ATOM   3410 C CB  . LEU   B 1 69  ? -5.695  23.945  10.243  1.00 17.98 ? 70  LEU   B CB  1 
ATOM   3411 C CG  . LEU   B 1 69  ? -4.624  24.431  9.265   1.00 19.36 ? 70  LEU   B CG  1 
ATOM   3412 C CD1 . LEU   B 1 69  ? -4.443  23.411  8.154   1.00 16.41 ? 70  LEU   B CD1 1 
ATOM   3413 C CD2 . LEU   B 1 69  ? -4.993  25.799  8.715   1.00 18.56 ? 70  LEU   B CD2 1 
ATOM   3414 N N   . PHE   B 1 70  ? -6.554  23.445  13.296  1.00 22.44 ? 71  PHE   B N   1 
ATOM   3415 C CA  . PHE   B 1 70  ? -7.504  22.883  14.244  1.00 23.58 ? 71  PHE   B CA  1 
ATOM   3416 C C   . PHE   B 1 70  ? -7.961  23.931  15.248  1.00 26.05 ? 71  PHE   B C   1 
ATOM   3417 O O   . PHE   B 1 70  ? -9.131  23.944  15.645  1.00 24.56 ? 71  PHE   B O   1 
ATOM   3418 C CB  . PHE   B 1 70  ? -6.896  21.664  14.927  1.00 22.40 ? 71  PHE   B CB  1 
ATOM   3419 C CG  . PHE   B 1 70  ? -6.643  20.543  13.970  1.00 24.03 ? 71  PHE   B CG  1 
ATOM   3420 C CD1 . PHE   B 1 70  ? -7.675  19.699  13.602  1.00 25.32 ? 71  PHE   B CD1 1 
ATOM   3421 C CD2 . PHE   B 1 70  ? -5.397  20.369  13.392  1.00 25.54 ? 71  PHE   B CD2 1 
ATOM   3422 C CE1 . PHE   B 1 70  ? -7.458  18.671  12.694  1.00 22.41 ? 71  PHE   B CE1 1 
ATOM   3423 C CE2 . PHE   B 1 70  ? -5.173  19.351  12.488  1.00 27.73 ? 71  PHE   B CE2 1 
ATOM   3424 C CZ  . PHE   B 1 70  ? -6.202  18.503  12.135  1.00 22.06 ? 71  PHE   B CZ  1 
ATOM   3425 N N   . THR   B 1 71  ? -7.065  24.839  15.646  1.00 23.61 ? 72  THR   B N   1 
ATOM   3426 C CA  . THR   B 1 71  ? -7.478  25.939  16.511  1.00 24.53 ? 72  THR   B CA  1 
ATOM   3427 C C   . THR   B 1 71  ? -8.527  26.802  15.824  1.00 24.72 ? 72  THR   B C   1 
ATOM   3428 O O   . THR   B 1 71  ? -9.517  27.212  16.442  1.00 27.55 ? 72  THR   B O   1 
ATOM   3429 C CB  . THR   B 1 71  ? -6.259  26.780  16.883  1.00 26.50 ? 72  THR   B CB  1 
ATOM   3430 O OG1 . THR   B 1 71  ? -5.295  25.941  17.529  1.00 28.04 ? 72  THR   B OG1 1 
ATOM   3431 C CG2 . THR   B 1 71  ? -6.642  27.946  17.797  1.00 26.39 ? 72  THR   B CG2 1 
ATOM   3432 N N   . ALA   B 1 72  ? -8.319  27.088  14.539  1.00 23.83 ? 73  ALA   B N   1 
ATOM   3433 C CA  . ALA   B 1 72  ? -9.280  27.881  13.784  1.00 26.45 ? 73  ALA   B CA  1 
ATOM   3434 C C   . ALA   B 1 72  ? -10.619 27.166  13.690  1.00 25.40 ? 73  ALA   B C   1 
ATOM   3435 O O   . ALA   B 1 72  ? -11.674 27.790  13.856  1.00 27.60 ? 73  ALA   B O   1 
ATOM   3436 C CB  . ALA   B 1 72  ? -8.725  28.181  12.392  1.00 21.68 ? 73  ALA   B CB  1 
ATOM   3437 N N   . THR   B 1 73  ? -10.596 25.851  13.440  1.00 22.48 ? 74  THR   B N   1 
ATOM   3438 C CA  . THR   B 1 73  ? -11.840 25.095  13.369  1.00 24.09 ? 74  THR   B CA  1 
ATOM   3439 C C   . THR   B 1 73  ? -12.557 25.119  14.710  1.00 26.01 ? 74  THR   B C   1 
ATOM   3440 O O   . THR   B 1 73  ? -13.782 25.267  14.763  1.00 28.02 ? 74  THR   B O   1 
ATOM   3441 C CB  . THR   B 1 73  ? -11.562 23.659  12.915  1.00 22.11 ? 74  THR   B CB  1 
ATOM   3442 O OG1 . THR   B 1 73  ? -10.908 23.677  11.638  1.00 23.52 ? 74  THR   B OG1 1 
ATOM   3443 C CG2 . THR   B 1 73  ? -12.863 22.871  12.783  1.00 25.79 ? 74  THR   B CG2 1 
ATOM   3444 N N   . ALA   B 1 74  ? -11.800 25.031  15.806  1.00 26.41 ? 75  ALA   B N   1 
ATOM   3445 C CA  . ALA   B 1 74  ? -12.405 25.124  17.131  1.00 26.86 ? 75  ALA   B CA  1 
ATOM   3446 C C   . ALA   B 1 74  ? -13.066 26.478  17.340  1.00 28.64 ? 75  ALA   B C   1 
ATOM   3447 O O   . ALA   B 1 74  ? -14.173 26.560  17.888  1.00 29.80 ? 75  ALA   B O   1 
ATOM   3448 C CB  . ALA   B 1 74  ? -11.352 24.864  18.205  1.00 29.02 ? 75  ALA   B CB  1 
ATOM   3449 N N   . GLY   B 1 75  ? -12.406 27.555  16.908  1.00 28.17 ? 76  GLY   B N   1 
ATOM   3450 C CA  . GLY   B 1 75  ? -12.996 28.872  17.069  1.00 27.59 ? 76  GLY   B CA  1 
ATOM   3451 C C   . GLY   B 1 75  ? -14.236 29.054  16.218  1.00 28.94 ? 76  GLY   B C   1 
ATOM   3452 O O   . GLY   B 1 75  ? -15.217 29.657  16.661  1.00 30.10 ? 76  GLY   B O   1 
ATOM   3453 N N   . GLY   B 1 76  ? -14.212 28.539  14.985  1.00 29.15 ? 77  GLY   B N   1 
ATOM   3454 C CA  . GLY   B 1 76  ? -15.408 28.574  14.161  1.00 28.54 ? 77  GLY   B CA  1 
ATOM   3455 C C   . GLY   B 1 76  ? -16.538 27.765  14.763  1.00 33.53 ? 77  GLY   B C   1 
ATOM   3456 O O   . GLY   B 1 76  ? -17.711 28.131  14.637  1.00 32.13 ? 77  GLY   B O   1 
ATOM   3457 N N   . TYR   B 1 77  ? -16.196 26.667  15.440  1.00 27.60 ? 78  TYR   B N   1 
ATOM   3458 C CA  . TYR   B 1 77  ? -17.190 25.851  16.128  1.00 30.48 ? 78  TYR   B CA  1 
ATOM   3459 C C   . TYR   B 1 77  ? -17.833 26.633  17.264  1.00 34.52 ? 78  TYR   B C   1 
ATOM   3460 O O   . TYR   B 1 77  ? -19.062 26.755  17.336  1.00 36.91 ? 78  TYR   B O   1 
ATOM   3461 C CB  . TYR   B 1 77  ? -16.518 24.582  16.647  1.00 33.83 ? 78  TYR   B CB  1 
ATOM   3462 C CG  . TYR   B 1 77  ? -17.430 23.581  17.330  1.00 33.75 ? 78  TYR   B CG  1 
ATOM   3463 C CD1 . TYR   B 1 77  ? -18.060 22.580  16.605  1.00 35.49 ? 78  TYR   B CD1 1 
ATOM   3464 C CD2 . TYR   B 1 77  ? -17.634 23.628  18.705  1.00 33.63 ? 78  TYR   B CD2 1 
ATOM   3465 C CE1 . TYR   B 1 77  ? -18.883 21.650  17.235  1.00 39.72 ? 78  TYR   B CE1 1 
ATOM   3466 C CE2 . TYR   B 1 77  ? -18.451 22.710  19.339  1.00 39.47 ? 78  TYR   B CE2 1 
ATOM   3467 C CZ  . TYR   B 1 77  ? -19.074 21.726  18.601  1.00 39.71 ? 78  TYR   B CZ  1 
ATOM   3468 O OH  . TYR   B 1 77  ? -19.891 20.815  19.242  1.00 46.38 ? 78  TYR   B OH  1 
ATOM   3469 N N   . ALA   B 1 78  ? -17.003 27.189  18.152  1.00 32.99 ? 79  ALA   B N   1 
ATOM   3470 C CA  . ALA   B 1 78  ? -17.515 27.958  19.281  1.00 35.34 ? 79  ALA   B CA  1 
ATOM   3471 C C   . ALA   B 1 78  ? -18.305 29.174  18.815  1.00 39.66 ? 79  ALA   B C   1 
ATOM   3472 O O   . ALA   B 1 78  ? -19.334 29.523  19.408  1.00 39.82 ? 79  ALA   B O   1 
ATOM   3473 C CB  . ALA   B 1 78  ? -16.355 28.386  20.181  1.00 38.22 ? 79  ALA   B CB  1 
ATOM   3474 N N   . LYS   B 1 79  ? -17.830 29.841  17.763  1.00 34.78 ? 80  LYS   B N   1 
ATOM   3475 C CA  . LYS   B 1 79  ? -18.538 30.999  17.225  1.00 38.13 ? 80  LYS   B CA  1 
ATOM   3476 C C   . LYS   B 1 79  ? -19.943 30.617  16.781  1.00 39.36 ? 80  LYS   B C   1 
ATOM   3477 O O   . LYS   B 1 79  ? -20.927 31.266  17.157  1.00 42.01 ? 80  LYS   B O   1 
ATOM   3478 C CB  . LYS   B 1 79  ? -17.739 31.601  16.061  1.00 37.69 ? 80  LYS   B CB  1 
ATOM   3479 C CG  . LYS   B 1 79  ? -18.311 32.900  15.488  1.00 36.33 ? 80  LYS   B CG  1 
ATOM   3480 C CD  . LYS   B 1 79  ? -19.056 32.658  14.181  1.00 40.21 ? 80  LYS   B CD  1 
ATOM   3481 C CE  . LYS   B 1 79  ? -19.353 33.957  13.453  1.00 41.73 ? 80  LYS   B CE  1 
ATOM   3482 N NZ  . LYS   B 1 79  ? -20.200 33.737  12.251  1.00 46.42 ? 80  LYS   B NZ  1 
ATOM   3483 N N   . ASN   B 1 80  ? -20.061 29.549  16.004  1.00 38.22 ? 81  ASN   B N   1 
ATOM   3484 C CA  . ASN   B 1 80  ? -21.341 29.195  15.415  1.00 41.85 ? 81  ASN   B CA  1 
ATOM   3485 C C   . ASN   B 1 80  ? -22.258 28.449  16.378  1.00 42.61 ? 81  ASN   B C   1 
ATOM   3486 O O   . ASN   B 1 80  ? -23.392 28.131  16.004  1.00 51.65 ? 81  ASN   B O   1 
ATOM   3487 C CB  . ASN   B 1 80  ? -21.110 28.393  14.136  1.00 44.01 ? 81  ASN   B CB  1 
ATOM   3488 C CG  . ASN   B 1 80  ? -20.721 29.284  12.966  1.00 45.36 ? 81  ASN   B CG  1 
ATOM   3489 O OD1 . ASN   B 1 80  ? -21.555 30.023  12.434  1.00 50.42 ? 81  ASN   B OD1 1 
ATOM   3490 N ND2 . ASN   B 1 80  ? -19.450 29.233  12.569  1.00 39.88 ? 81  ASN   B ND2 1 
ATOM   3491 N N   . LYS   B 1 81  ? -21.807 28.175  17.602  1.00 40.11 ? 82  LYS   B N   1 
ATOM   3492 C CA  . LYS   B 1 81  ? -22.688 27.762  18.686  1.00 43.55 ? 82  LYS   B CA  1 
ATOM   3493 C C   . LYS   B 1 81  ? -22.953 28.895  19.672  1.00 44.29 ? 82  LYS   B C   1 
ATOM   3494 O O   . LYS   B 1 81  ? -23.502 28.653  20.753  1.00 46.45 ? 82  LYS   B O   1 
ATOM   3495 C CB  . LYS   B 1 81  ? -22.109 26.551  19.418  1.00 42.41 ? 82  LYS   B CB  1 
ATOM   3496 C CG  . LYS   B 1 81  ? -22.088 25.279  18.583  1.00 46.70 ? 82  LYS   B CG  1 
ATOM   3497 C CD  . LYS   B 1 81  ? -21.662 24.083  19.416  1.00 48.60 ? 82  LYS   B CD  1 
ATOM   3498 C CE  . LYS   B 1 81  ? -22.775 23.605  20.331  1.00 52.45 ? 82  LYS   B CE  1 
ATOM   3499 N NZ  . LYS   B 1 81  ? -23.841 22.873  19.583  1.00 54.07 ? 82  LYS   B NZ  1 
ATOM   3500 N N   . GLY   B 1 82  ? -22.568 30.123  19.325  1.00 43.14 ? 83  GLY   B N   1 
ATOM   3501 C CA  . GLY   B 1 82  ? -22.814 31.265  20.182  1.00 43.28 ? 83  GLY   B CA  1 
ATOM   3502 C C   . GLY   B 1 82  ? -21.988 31.312  21.445  1.00 41.53 ? 83  GLY   B C   1 
ATOM   3503 O O   . GLY   B 1 82  ? -22.270 32.138  22.318  1.00 44.52 ? 83  GLY   B O   1 
ATOM   3504 N N   . LYS   B 1 83  ? -20.981 30.446  21.581  1.00 37.39 ? 84  LYS   B N   1 
ATOM   3505 C CA  . LYS   B 1 83  ? -20.121 30.514  22.755  1.00 41.37 ? 84  LYS   B CA  1 
ATOM   3506 C C   . LYS   B 1 83  ? -19.225 31.745  22.711  1.00 44.17 ? 84  LYS   B C   1 
ATOM   3507 O O   . LYS   B 1 83  ? -18.831 32.256  23.764  1.00 45.07 ? 84  LYS   B O   1 
ATOM   3508 C CB  . LYS   B 1 83  ? -19.284 29.240  22.875  1.00 43.01 ? 84  LYS   B CB  1 
ATOM   3509 C CG  . LYS   B 1 83  ? -20.105 27.968  23.077  1.00 43.46 ? 84  LYS   B CG  1 
ATOM   3510 C CD  . LYS   B 1 83  ? -21.096 28.122  24.227  1.00 51.47 ? 84  LYS   B CD  1 
ATOM   3511 C CE  . LYS   B 1 83  ? -21.850 26.824  24.489  1.00 57.09 ? 84  LYS   B CE  1 
ATOM   3512 N NZ  . LYS   B 1 83  ? -22.973 27.009  25.455  1.00 57.26 ? 84  LYS   B NZ  1 
ATOM   3513 N N   . ILE   B 1 84  ? -18.895 32.228  21.511  1.00 40.51 ? 85  ILE   B N   1 
ATOM   3514 C CA  . ILE   B 1 84  ? -18.143 33.464  21.333  1.00 37.79 ? 85  ILE   B CA  1 
ATOM   3515 C C   . ILE   B 1 84  ? -18.718 34.234  20.156  1.00 37.21 ? 85  ILE   B C   1 
ATOM   3516 O O   . ILE   B 1 84  ? -19.429 33.690  19.309  1.00 37.77 ? 85  ILE   B O   1 
ATOM   3517 C CB  . ILE   B 1 84  ? -16.633 33.243  21.083  1.00 38.78 ? 85  ILE   B CB  1 
ATOM   3518 C CG1 . ILE   B 1 84  ? -16.415 32.237  19.946  1.00 40.73 ? 85  ILE   B CG1 1 
ATOM   3519 C CG2 . ILE   B 1 84  ? -15.914 32.845  22.352  1.00 42.74 ? 85  ILE   B CG2 1 
ATOM   3520 C CD1 . ILE   B 1 84  ? -15.003 32.229  19.408  1.00 38.52 ? 85  ILE   B CD1 1 
ATOM   3521 N N   . SER   B 1 85  ? -18.380 35.521  20.110  1.00 36.03 ? 86  SER   B N   1 
ATOM   3522 C CA  . SER   B 1 85  ? -18.503 36.337  18.913  1.00 39.36 ? 86  SER   B CA  1 
ATOM   3523 C C   . SER   B 1 85  ? -17.110 36.803  18.523  1.00 34.16 ? 86  SER   B C   1 
ATOM   3524 O O   . SER   B 1 85  ? -16.284 37.092  19.394  1.00 35.54 ? 86  SER   B O   1 
ATOM   3525 C CB  . SER   B 1 85  ? -19.412 37.551  19.133  1.00 42.97 ? 86  SER   B CB  1 
ATOM   3526 O OG  . SER   B 1 85  ? -19.224 38.512  18.105  1.00 42.33 ? 86  SER   B OG  1 
ATOM   3527 N N   . PHE   B 1 86  ? -16.844 36.865  17.218  1.00 34.93 ? 87  PHE   B N   1 
ATOM   3528 C CA  . PHE   B 1 86  ? -15.538 37.330  16.768  1.00 36.07 ? 87  PHE   B CA  1 
ATOM   3529 C C   . PHE   B 1 86  ? -15.310 38.809  17.064  1.00 34.58 ? 87  PHE   B C   1 
ATOM   3530 O O   . PHE   B 1 86  ? -14.167 39.272  16.989  1.00 30.69 ? 87  PHE   B O   1 
ATOM   3531 C CB  . PHE   B 1 86  ? -15.364 37.047  15.268  1.00 33.18 ? 87  PHE   B CB  1 
ATOM   3532 C CG  . PHE   B 1 86  ? -15.105 35.591  14.946  1.00 34.05 ? 87  PHE   B CG  1 
ATOM   3533 C CD1 . PHE   B 1 86  ? -14.623 34.721  15.916  1.00 35.64 ? 87  PHE   B CD1 1 
ATOM   3534 C CD2 . PHE   B 1 86  ? -15.336 35.096  13.673  1.00 34.46 ? 87  PHE   B CD2 1 
ATOM   3535 C CE1 . PHE   B 1 86  ? -14.381 33.382  15.619  1.00 36.32 ? 87  PHE   B CE1 1 
ATOM   3536 C CE2 . PHE   B 1 86  ? -15.087 33.757  13.364  1.00 35.03 ? 87  PHE   B CE2 1 
ATOM   3537 C CZ  . PHE   B 1 86  ? -14.610 32.905  14.338  1.00 31.90 ? 87  PHE   B CZ  1 
ATOM   3538 N N   . ASP   B 1 87  ? -16.354 39.551  17.416  1.00 37.27 ? 88  ASP   B N   1 
ATOM   3539 C CA  . ASP   B 1 87  ? -16.194 40.938  17.834  1.00 37.04 ? 88  ASP   B CA  1 
ATOM   3540 C C   . ASP   B 1 87  ? -15.942 41.074  19.333  1.00 37.59 ? 88  ASP   B C   1 
ATOM   3541 O O   . ASP   B 1 87  ? -15.671 42.185  19.804  1.00 37.33 ? 88  ASP   B O   1 
ATOM   3542 C CB  . ASP   B 1 87  ? -17.423 41.760  17.424  1.00 39.73 ? 88  ASP   B CB  1 
ATOM   3543 C CG  . ASP   B 1 87  ? -17.519 41.957  15.916  1.00 46.44 ? 88  ASP   B CG  1 
ATOM   3544 O OD1 . ASP   B 1 87  ? -16.465 42.072  15.253  1.00 46.57 ? 88  ASP   B OD1 1 
ATOM   3545 O OD2 . ASP   B 1 87  ? -18.652 41.996  15.390  1.00 53.15 ? 88  ASP   B OD2 1 
ATOM   3546 N N   . ASP   B 1 88  ? -16.010 39.977  20.085  1.00 37.26 ? 89  ASP   B N   1 
ATOM   3547 C CA  . ASP   B 1 88  ? -15.680 40.001  21.503  1.00 38.43 ? 89  ASP   B CA  1 
ATOM   3548 C C   . ASP   B 1 88  ? -14.189 40.265  21.703  1.00 35.64 ? 89  ASP   B C   1 
ATOM   3549 O O   . ASP   B 1 88  ? -13.375 40.108  20.790  1.00 36.22 ? 89  ASP   B O   1 
ATOM   3550 C CB  . ASP   B 1 88  ? -16.053 38.679  22.175  1.00 37.65 ? 89  ASP   B CB  1 
ATOM   3551 C CG  . ASP   B 1 88  ? -17.550 38.442  22.220  1.00 38.15 ? 89  ASP   B CG  1 
ATOM   3552 O OD1 . ASP   B 1 88  ? -18.312 39.427  22.181  1.00 45.13 ? 89  ASP   B OD1 1 
ATOM   3553 O OD2 . ASP   B 1 88  ? -17.961 37.261  22.298  1.00 45.29 ? 89  ASP   B OD2 1 
ATOM   3554 N N   . THR   B 1 89  ? -13.835 40.672  22.919  1.00 38.63 ? 90  THR   B N   1 
ATOM   3555 C CA  . THR   B 1 89  ? -12.448 40.849  23.320  1.00 37.44 ? 90  THR   B CA  1 
ATOM   3556 C C   . THR   B 1 89  ? -12.068 39.823  24.386  1.00 39.26 ? 90  THR   B C   1 
ATOM   3557 O O   . THR   B 1 89  ? -12.944 39.208  25.006  1.00 40.62 ? 90  THR   B O   1 
ATOM   3558 C CB  . THR   B 1 89  ? -12.208 42.280  23.828  1.00 39.89 ? 90  THR   B CB  1 
ATOM   3559 O OG1 . THR   B 1 89  ? -12.984 42.525  25.005  1.00 43.60 ? 90  THR   B OG1 1 
ATOM   3560 C CG2 . THR   B 1 89  ? -12.587 43.291  22.753  1.00 36.81 ? 90  THR   B CG2 1 
ATOM   3561 N N   . PRO   B 1 90  ? -10.767 39.574  24.594  1.00 39.11 ? 91  PRO   B N   1 
ATOM   3562 C CA  . PRO   B 1 90  ? -10.373 38.455  25.467  1.00 41.16 ? 91  PRO   B CA  1 
ATOM   3563 C C   . PRO   B 1 90  ? -10.759 38.634  26.925  1.00 44.83 ? 91  PRO   B C   1 
ATOM   3564 O O   . PRO   B 1 90  ? -10.967 37.632  27.622  1.00 45.86 ? 91  PRO   B O   1 
ATOM   3565 C CB  . PRO   B 1 90  ? -8.847  38.399  25.296  1.00 39.37 ? 91  PRO   B CB  1 
ATOM   3566 C CG  . PRO   B 1 90  ? -8.463  39.755  24.808  1.00 38.72 ? 91  PRO   B CG  1 
ATOM   3567 C CD  . PRO   B 1 90  ? -9.595  40.167  23.924  1.00 38.37 ? 91  PRO   B CD  1 
ATOM   3568 N N   . GLY   B 1 91  ? -10.848 39.874  27.412  1.00 43.49 ? 92  GLY   B N   1 
ATOM   3569 C CA  . GLY   B 1 91  ? -11.207 40.112  28.801  1.00 48.85 ? 92  GLY   B CA  1 
ATOM   3570 C C   . GLY   B 1 91  ? -12.615 39.684  29.152  1.00 51.72 ? 92  GLY   B C   1 
ATOM   3571 O O   . GLY   B 1 91  ? -12.942 39.570  30.338  1.00 52.78 ? 92  GLY   B O   1 
ATOM   3572 N N   . LYS   B 1 92  ? -13.460 39.449  28.148  1.00 46.09 ? 93  LYS   B N   1 
ATOM   3573 C CA  . LYS   B 1 92  ? -14.798 38.940  28.407  1.00 50.35 ? 93  LYS   B CA  1 
ATOM   3574 C C   . LYS   B 1 92  ? -14.774 37.501  28.915  1.00 49.11 ? 93  LYS   B C   1 
ATOM   3575 O O   . LYS   B 1 92  ? -15.721 37.076  29.589  1.00 49.99 ? 93  LYS   B O   1 
ATOM   3576 C CB  . LYS   B 1 92  ? -15.635 39.072  27.135  1.00 46.67 ? 93  LYS   B CB  1 
ATOM   3577 C CG  . LYS   B 1 92  ? -17.062 38.562  27.215  1.00 48.98 ? 93  LYS   B CG  1 
ATOM   3578 C CD  . LYS   B 1 92  ? -17.819 38.972  25.962  1.00 47.80 ? 93  LYS   B CD  1 
ATOM   3579 C CE  . LYS   B 1 92  ? -19.200 38.356  25.895  1.00 52.45 ? 93  LYS   B CE  1 
ATOM   3580 N NZ  . LYS   B 1 92  ? -19.880 38.775  24.639  1.00 57.34 ? 93  LYS   B NZ  1 
ATOM   3581 N N   . TYR   B 1 93  ? -13.698 36.759  28.652  1.00 46.64 ? 94  TYR   B N   1 
ATOM   3582 C CA  . TYR   B 1 93  ? -13.581 35.364  29.067  1.00 45.31 ? 94  TYR   B CA  1 
ATOM   3583 C C   . TYR   B 1 93  ? -12.454 35.124  30.058  1.00 50.48 ? 94  TYR   B C   1 
ATOM   3584 O O   . TYR   B 1 93  ? -12.633 34.360  31.009  1.00 49.88 ? 94  TYR   B O   1 
ATOM   3585 C CB  . TYR   B 1 93  ? -13.404 34.469  27.826  1.00 44.73 ? 94  TYR   B CB  1 
ATOM   3586 C CG  . TYR   B 1 93  ? -14.539 34.660  26.849  1.00 43.29 ? 94  TYR   B CG  1 
ATOM   3587 C CD1 . TYR   B 1 93  ? -15.709 33.932  26.972  1.00 44.77 ? 94  TYR   B CD1 1 
ATOM   3588 C CD2 . TYR   B 1 93  ? -14.462 35.609  25.831  1.00 44.01 ? 94  TYR   B CD2 1 
ATOM   3589 C CE1 . TYR   B 1 93  ? -16.763 34.117  26.100  1.00 47.13 ? 94  TYR   B CE1 1 
ATOM   3590 C CE2 . TYR   B 1 93  ? -15.515 35.801  24.951  1.00 42.75 ? 94  TYR   B CE2 1 
ATOM   3591 C CZ  . TYR   B 1 93  ? -16.666 35.050  25.096  1.00 48.28 ? 94  TYR   B CZ  1 
ATOM   3592 O OH  . TYR   B 1 93  ? -17.726 35.227  24.233  1.00 46.98 ? 94  TYR   B OH  1 
ATOM   3593 N N   . TRP   B 1 94  ? -11.302 35.765  29.878  1.00 48.71 ? 95  TRP   B N   1 
ATOM   3594 C CA  . TRP   B 1 94  ? -10.197 35.692  30.828  1.00 51.01 ? 95  TRP   B CA  1 
ATOM   3595 C C   . TRP   B 1 94  ? -10.234 36.972  31.655  1.00 53.37 ? 95  TRP   B C   1 
ATOM   3596 O O   . TRP   B 1 94  ? -9.862  38.045  31.167  1.00 52.08 ? 95  TRP   B O   1 
ATOM   3597 C CB  . TRP   B 1 94  ? -8.866  35.521  30.098  1.00 45.99 ? 95  TRP   B CB  1 
ATOM   3598 C CG  . TRP   B 1 94  ? -7.721  35.117  30.977  1.00 49.07 ? 95  TRP   B CG  1 
ATOM   3599 C CD1 . TRP   B 1 94  ? -7.753  34.901  32.328  1.00 48.81 ? 95  TRP   B CD1 1 
ATOM   3600 C CD2 . TRP   B 1 94  ? -6.371  34.876  30.565  1.00 48.76 ? 95  TRP   B CD2 1 
ATOM   3601 N NE1 . TRP   B 1 94  ? -6.505  34.538  32.776  1.00 53.24 ? 95  TRP   B NE1 1 
ATOM   3602 C CE2 . TRP   B 1 94  ? -5.639  34.518  31.714  1.00 51.60 ? 95  TRP   B CE2 1 
ATOM   3603 C CE3 . TRP   B 1 94  ? -5.709  34.931  29.333  1.00 46.07 ? 95  TRP   B CE3 1 
ATOM   3604 C CZ2 . TRP   B 1 94  ? -4.279  34.215  31.668  1.00 54.65 ? 95  TRP   B CZ2 1 
ATOM   3605 C CZ3 . TRP   B 1 94  ? -4.360  34.629  29.290  1.00 49.94 ? 95  TRP   B CZ3 1 
ATOM   3606 C CH2 . TRP   B 1 94  ? -3.660  34.277  30.449  1.00 53.03 ? 95  TRP   B CH2 1 
ATOM   3607 N N   . LYS   B 1 95  ? -10.682 36.858  32.908  1.00 52.75 ? 96  LYS   B N   1 
ATOM   3608 C CA  . LYS   B 1 95  ? -11.083 38.041  33.663  1.00 52.66 ? 96  LYS   B CA  1 
ATOM   3609 C C   . LYS   B 1 95  ? -9.897  38.910  34.064  1.00 53.11 ? 96  LYS   B C   1 
ATOM   3610 O O   . LYS   B 1 95  ? -10.042 40.131  34.188  1.00 55.15 ? 96  LYS   B O   1 
ATOM   3611 C CB  . LYS   B 1 95  ? -11.867 37.619  34.906  1.00 59.59 ? 96  LYS   B CB  1 
ATOM   3612 C CG  . LYS   B 1 95  ? -13.275 38.182  34.941  1.00 66.76 ? 96  LYS   B CG  1 
ATOM   3613 C CD  . LYS   B 1 95  ? -14.031 37.854  33.660  1.00 62.22 ? 96  LYS   B CD  1 
ATOM   3614 C CE  . LYS   B 1 95  ? -14.392 36.380  33.583  1.00 63.55 ? 96  LYS   B CE  1 
ATOM   3615 N NZ  . LYS   B 1 95  ? -15.118 36.054  32.324  1.00 67.95 ? 96  LYS   B NZ  1 
ATOM   3616 N N   . GLU   B 1 96  ? -8.720  38.316  34.259  1.00 53.75 ? 97  GLU   B N   1 
ATOM   3617 C CA  . GLU   B 1 96  ? -7.551  39.078  34.681  1.00 53.71 ? 97  GLU   B CA  1 
ATOM   3618 C C   . GLU   B 1 96  ? -7.074  40.022  33.582  1.00 53.08 ? 97  GLU   B C   1 
ATOM   3619 O O   . GLU   B 1 96  ? -6.122  40.778  33.784  1.00 53.73 ? 97  GLU   B O   1 
ATOM   3620 C CB  . GLU   B 1 96  ? -6.424  38.131  35.096  1.00 57.65 ? 97  GLU   B CB  1 
ATOM   3621 C CG  . GLU   B 1 96  ? -6.487  37.656  36.541  1.00 59.00 ? 97  GLU   B CG  1 
ATOM   3622 C CD  . GLU   B 1 96  ? -7.239  36.347  36.708  1.00 57.45 ? 97  GLU   B CD  1 
ATOM   3623 O OE1 . GLU   B 1 96  ? -7.755  35.808  35.701  1.00 59.77 ? 97  GLU   B OE1 1 
ATOM   3624 O OE2 . GLU   B 1 96  ? -7.308  35.847  37.850  1.00 59.77 ? 97  GLU   B OE2 1 
ATOM   3625 N N   . LEU   B 1 97  ? -7.723  39.978  32.416  1.00 53.14 ? 98  LEU   B N   1 
ATOM   3626 C CA  . LEU   B 1 97  ? -7.399  40.843  31.289  1.00 51.19 ? 98  LEU   B CA  1 
ATOM   3627 C C   . LEU   B 1 97  ? -8.386  41.992  31.113  1.00 52.83 ? 98  LEU   B C   1 
ATOM   3628 O O   . LEU   B 1 97  ? -8.194  42.826  30.218  1.00 46.56 ? 98  LEU   B O   1 
ATOM   3629 C CB  . LEU   B 1 97  ? -7.335  40.025  29.992  1.00 47.24 ? 98  LEU   B CB  1 
ATOM   3630 C CG  . LEU   B 1 97  ? -6.244  38.961  29.877  1.00 44.14 ? 98  LEU   B CG  1 
ATOM   3631 C CD1 . LEU   B 1 97  ? -6.190  38.450  28.443  1.00 44.71 ? 98  LEU   B CD1 1 
ATOM   3632 C CD2 . LEU   B 1 97  ? -4.893  39.504  30.298  1.00 44.69 ? 98  LEU   B CD2 1 
ATOM   3633 N N   . LYS   B 1 98  ? -9.429  42.065  31.939  1.00 54.09 ? 99  LYS   B N   1 
ATOM   3634 C CA  . LYS   B 1 98  ? -10.372 43.172  31.845  1.00 60.80 ? 99  LYS   B CA  1 
ATOM   3635 C C   . LYS   B 1 98  ? -9.660  44.493  32.119  1.00 56.28 ? 99  LYS   B C   1 
ATOM   3636 O O   . LYS   B 1 98  ? -8.763  44.570  32.964  1.00 59.81 ? 99  LYS   B O   1 
ATOM   3637 C CB  . LYS   B 1 98  ? -11.523 42.971  32.834  1.00 61.58 ? 99  LYS   B CB  1 
ATOM   3638 C CG  . LYS   B 1 98  ? -12.884 43.454  32.336  1.00 61.97 ? 99  LYS   B CG  1 
ATOM   3639 C CD  . LYS   B 1 98  ? -13.351 42.650  31.130  1.00 63.33 ? 99  LYS   B CD  1 
ATOM   3640 C CE  . LYS   B 1 98  ? -14.858 42.418  31.150  1.00 64.06 ? 99  LYS   B CE  1 
ATOM   3641 N NZ  . LYS   B 1 98  ? -15.270 41.489  32.238  1.00 67.75 ? 99  LYS   B NZ  1 
ATOM   3642 N N   . ASN   B 1 99  ? -10.045 45.530  31.372  1.00 64.21 ? 100 ASN   B N   1 
ATOM   3643 C CA  . ASN   B 1 99  ? -9.530  46.889  31.563  1.00 65.47 ? 100 ASN   B CA  1 
ATOM   3644 C C   . ASN   B 1 99  ? -8.022  46.984  31.334  1.00 62.26 ? 100 ASN   B C   1 
ATOM   3645 O O   . ASN   B 1 99  ? -7.342  47.814  31.944  1.00 60.55 ? 100 ASN   B O   1 
ATOM   3646 C CB  . ASN   B 1 99  ? -9.889  47.434  32.949  1.00 73.65 ? 100 ASN   B CB  1 
ATOM   3647 C CG  . ASN   B 1 99  ? -11.329 47.886  33.038  1.00 75.55 ? 100 ASN   B CG  1 
ATOM   3648 O OD1 . ASN   B 1 99  ? -12.178 47.445  32.261  1.00 76.56 ? 100 ASN   B OD1 1 
ATOM   3649 N ND2 . ASN   B 1 99  ? -11.613 48.776  33.983  1.00 78.15 ? 100 ASN   B ND2 1 
ATOM   3650 N N   . THR   B 1 100 ? -7.484  46.150  30.456  1.00 51.45 ? 101 THR   B N   1 
ATOM   3651 C CA  . THR   B 1 100 ? -6.099  46.237  30.027  1.00 50.41 ? 101 THR   B CA  1 
ATOM   3652 C C   . THR   B 1 100 ? -6.060  46.556  28.539  1.00 45.40 ? 101 THR   B C   1 
ATOM   3653 O O   . THR   B 1 100 ? -7.058  46.375  27.832  1.00 42.16 ? 101 THR   B O   1 
ATOM   3654 C CB  . THR   B 1 100 ? -5.341  44.928  30.293  1.00 50.53 ? 101 THR   B CB  1 
ATOM   3655 O OG1 . THR   B 1 100 ? -5.871  43.893  29.457  1.00 46.92 ? 101 THR   B OG1 1 
ATOM   3656 C CG2 . THR   B 1 100 ? -5.458  44.518  31.760  1.00 52.10 ? 101 THR   B CG2 1 
ATOM   3657 N N   . PRO   B 1 101 ? -4.931  47.053  28.031  1.00 43.57 ? 102 PRO   B N   1 
ATOM   3658 C CA  . PRO   B 1 101 ? -4.875  47.389  26.597  1.00 42.89 ? 102 PRO   B CA  1 
ATOM   3659 C C   . PRO   B 1 101 ? -5.113  46.204  25.669  1.00 39.46 ? 102 PRO   B C   1 
ATOM   3660 O O   . PRO   B 1 101 ? -5.693  46.397  24.594  1.00 37.02 ? 102 PRO   B O   1 
ATOM   3661 C CB  . PRO   B 1 101 ? -3.467  47.975  26.435  1.00 39.95 ? 102 PRO   B CB  1 
ATOM   3662 C CG  . PRO   B 1 101 ? -3.173  48.577  27.785  1.00 40.65 ? 102 PRO   B CG  1 
ATOM   3663 C CD  . PRO   B 1 101 ? -3.801  47.634  28.782  1.00 45.90 ? 102 PRO   B CD  1 
ATOM   3664 N N   . ILE   B 1 102 ? -4.703  44.988  26.041  1.00 39.85 ? 103 ILE   B N   1 
ATOM   3665 C CA  . ILE   B 1 102 ? -4.935  43.842  25.161  1.00 37.34 ? 103 ILE   B CA  1 
ATOM   3666 C C   . ILE   B 1 102 ? -6.426  43.571  24.999  1.00 35.86 ? 103 ILE   B C   1 
ATOM   3667 O O   . ILE   B 1 102 ? -6.842  42.959  24.005  1.00 37.83 ? 103 ILE   B O   1 
ATOM   3668 C CB  . ILE   B 1 102 ? -4.188  42.585  25.669  1.00 40.70 ? 103 ILE   B CB  1 
ATOM   3669 C CG1 . ILE   B 1 102 ? -4.102  41.511  24.575  1.00 37.65 ? 103 ILE   B CG1 1 
ATOM   3670 C CG2 . ILE   B 1 102 ? -4.879  41.983  26.893  1.00 40.77 ? 103 ILE   B CG2 1 
ATOM   3671 C CD1 . ILE   B 1 102 ? -3.298  41.917  23.364  1.00 37.59 ? 103 ILE   B CD1 1 
ATOM   3672 N N   . ASP   B 1 103 ? -7.247  44.030  25.947  1.00 38.54 ? 104 ASP   B N   1 
ATOM   3673 C CA  . ASP   B 1 103 ? -8.696  43.911  25.858  1.00 37.92 ? 104 ASP   B CA  1 
ATOM   3674 C C   . ASP   B 1 103 ? -9.309  44.866  24.835  1.00 39.95 ? 104 ASP   B C   1 
ATOM   3675 O O   . ASP   B 1 103 ? -10.538 44.903  24.714  1.00 40.14 ? 104 ASP   B O   1 
ATOM   3676 C CB  . ASP   B 1 103 ? -9.312  44.144  27.241  1.00 42.54 ? 104 ASP   B CB  1 
ATOM   3677 C CG  . ASP   B 1 103 ? -10.626 43.415  27.438  1.00 46.31 ? 104 ASP   B CG  1 
ATOM   3678 O OD1 . ASP   B 1 103 ? -10.900 42.427  26.722  1.00 43.69 ? 104 ASP   B OD1 1 
ATOM   3679 O OD2 . ASP   B 1 103 ? -11.388 43.829  28.334  1.00 49.21 ? 104 ASP   B OD2 1 
ATOM   3680 N N   . GLN   B 1 104 ? -8.501  45.633  24.101  1.00 34.96 ? 105 GLN   B N   1 
ATOM   3681 C CA  . GLN   B 1 104 ? -8.975  46.409  22.964  1.00 38.77 ? 105 GLN   B CA  1 
ATOM   3682 C C   . GLN   B 1 104 ? -8.860  45.655  21.642  1.00 31.64 ? 105 GLN   B C   1 
ATOM   3683 O O   . GLN   B 1 104 ? -9.271  46.183  20.603  1.00 34.64 ? 105 GLN   B O   1 
ATOM   3684 C CB  . GLN   B 1 104 ? -8.196  47.723  22.858  1.00 36.99 ? 105 GLN   B CB  1 
ATOM   3685 C CG  . GLN   B 1 104 ? -8.350  48.629  24.058  1.00 44.29 ? 105 GLN   B CG  1 
ATOM   3686 C CD  . GLN   B 1 104 ? -9.794  48.991  24.313  1.00 46.67 ? 105 GLN   B CD  1 
ATOM   3687 O OE1 . GLN   B 1 104 ? -10.411 49.719  23.531  1.00 51.30 ? 105 GLN   B OE1 1 
ATOM   3688 N NE2 . GLN   B 1 104 ? -10.350 48.468  25.397  1.00 45.12 ? 105 GLN   B NE2 1 
ATOM   3689 N N   . VAL   B 1 105 ? -8.298  44.455  21.655  1.00 31.85 ? 106 VAL   B N   1 
ATOM   3690 C CA  . VAL   B 1 105 ? -8.134  43.623  20.463  1.00 29.40 ? 106 VAL   B CA  1 
ATOM   3691 C C   . VAL   B 1 105 ? -9.244  42.581  20.467  1.00 33.15 ? 106 VAL   B C   1 
ATOM   3692 O O   . VAL   B 1 105 ? -9.541  41.994  21.513  1.00 35.61 ? 106 VAL   B O   1 
ATOM   3693 C CB  . VAL   B 1 105 ? -6.741  42.958  20.463  1.00 30.58 ? 106 VAL   B CB  1 
ATOM   3694 C CG1 . VAL   B 1 105 ? -6.517  42.116  19.198  1.00 27.36 ? 106 VAL   B CG1 1 
ATOM   3695 C CG2 . VAL   B 1 105 ? -5.641  44.017  20.620  1.00 30.70 ? 106 VAL   B CG2 1 
ATOM   3696 N N   . ASN   B 1 106 ? -9.883  42.361  19.321  1.00 31.13 ? 107 ASN   B N   1 
ATOM   3697 C CA  . ASN   B 1 106 ? -10.975 41.396  19.328  1.00 30.33 ? 107 ASN   B CA  1 
ATOM   3698 C C   . ASN   B 1 106 ? -10.473 40.008  18.927  1.00 30.89 ? 107 ASN   B C   1 
ATOM   3699 O O   . ASN   B 1 106 ? -9.322  39.819  18.530  1.00 28.93 ? 107 ASN   B O   1 
ATOM   3700 C CB  . ASN   B 1 106 ? -12.147 41.864  18.443  1.00 29.48 ? 107 ASN   B CB  1 
ATOM   3701 C CG  . ASN   B 1 106 ? -11.843 41.847  16.940  1.00 30.32 ? 107 ASN   B CG  1 
ATOM   3702 O OD1 . ASN   B 1 106 ? -11.118 40.993  16.421  1.00 29.94 ? 107 ASN   B OD1 1 
ATOM   3703 N ND2 . ASN   B 1 106 ? -12.430 42.804  16.228  1.00 32.02 ? 107 ASN   B ND2 1 
ATOM   3704 N N   . LEU   B 1 107 ? -11.357 39.016  19.065  1.00 29.81 ? 108 LEU   B N   1 
ATOM   3705 C CA  . LEU   B 1 107 ? -10.928 37.634  18.879  1.00 29.06 ? 108 LEU   B CA  1 
ATOM   3706 C C   . LEU   B 1 107 ? -10.504 37.365  17.443  1.00 27.48 ? 108 LEU   B C   1 
ATOM   3707 O O   . LEU   B 1 107 ? -9.554  36.604  17.203  1.00 27.74 ? 108 LEU   B O   1 
ATOM   3708 C CB  . LEU   B 1 107 ? -12.042 36.677  19.296  1.00 32.62 ? 108 LEU   B CB  1 
ATOM   3709 C CG  . LEU   B 1 107 ? -12.514 36.847  20.736  1.00 32.12 ? 108 LEU   B CG  1 
ATOM   3710 C CD1 . LEU   B 1 107 ? -13.493 35.741  21.082  1.00 31.12 ? 108 LEU   B CD1 1 
ATOM   3711 C CD2 . LEU   B 1 107 ? -11.341 36.869  21.711  1.00 36.39 ? 108 LEU   B CD2 1 
ATOM   3712 N N   . LEU   B 1 108 ? -11.186 37.973  16.468  1.00 26.87 ? 109 LEU   B N   1 
ATOM   3713 C CA  . LEU   B 1 108 ? -10.778 37.765  15.081  1.00 27.89 ? 109 LEU   B CA  1 
ATOM   3714 C C   . LEU   B 1 108 ? -9.376  38.317  14.841  1.00 25.15 ? 109 LEU   B C   1 
ATOM   3715 O O   . LEU   B 1 108 ? -8.551  37.681  14.168  1.00 26.24 ? 109 LEU   B O   1 
ATOM   3716 C CB  . LEU   B 1 108 ? -11.789 38.406  14.127  1.00 28.11 ? 109 LEU   B CB  1 
ATOM   3717 C CG  . LEU   B 1 108 ? -11.511 38.192  12.631  1.00 26.63 ? 109 LEU   B CG  1 
ATOM   3718 C CD1 . LEU   B 1 108 ? -11.587 36.728  12.274  1.00 26.79 ? 109 LEU   B CD1 1 
ATOM   3719 C CD2 . LEU   B 1 108 ? -12.496 38.985  11.784  1.00 33.36 ? 109 LEU   B CD2 1 
ATOM   3720 N N   . GLN   B 1 109 ? -9.081  39.485  15.416  1.00 26.37 ? 110 GLN   B N   1 
ATOM   3721 C CA  . GLN   B 1 109 ? -7.760  40.084  15.251  1.00 24.61 ? 110 GLN   B CA  1 
ATOM   3722 C C   . GLN   B 1 109 ? -6.678  39.219  15.894  1.00 24.47 ? 110 GLN   B C   1 
ATOM   3723 O O   . GLN   B 1 109 ? -5.589  39.064  15.335  1.00 24.59 ? 110 GLN   B O   1 
ATOM   3724 C CB  . GLN   B 1 109 ? -7.774  41.511  15.817  1.00 24.34 ? 110 GLN   B CB  1 
ATOM   3725 C CG  . GLN   B 1 109 ? -8.677  42.413  14.989  1.00 26.53 ? 110 GLN   B CG  1 
ATOM   3726 C CD  . GLN   B 1 109 ? -9.047  43.719  15.655  1.00 27.67 ? 110 GLN   B CD  1 
ATOM   3727 O OE1 . GLN   B 1 109 ? -9.080  43.831  16.885  1.00 28.30 ? 110 GLN   B OE1 1 
ATOM   3728 N NE2 . GLN   B 1 109 ? -9.364  44.715  14.836  1.00 29.71 ? 110 GLN   B NE2 1 
ATOM   3729 N N   . LEU   B 1 110 ? -6.967  38.624  17.055  1.00 26.27 ? 111 LEU   B N   1 
ATOM   3730 C CA  . LEU   B 1 110 ? -6.021  37.680  17.643  1.00 24.13 ? 111 LEU   B CA  1 
ATOM   3731 C C   . LEU   B 1 110 ? -5.827  36.467  16.740  1.00 25.22 ? 111 LEU   B C   1 
ATOM   3732 O O   . LEU   B 1 110 ? -4.694  36.034  16.500  1.00 26.06 ? 111 LEU   B O   1 
ATOM   3733 C CB  . LEU   B 1 110 ? -6.503  37.244  19.027  1.00 25.64 ? 111 LEU   B CB  1 
ATOM   3734 C CG  . LEU   B 1 110 ? -6.463  38.317  20.119  1.00 27.38 ? 111 LEU   B CG  1 
ATOM   3735 C CD1 . LEU   B 1 110 ? -7.111  37.761  21.390  1.00 29.54 ? 111 LEU   B CD1 1 
ATOM   3736 C CD2 . LEU   B 1 110 ? -5.044  38.744  20.405  1.00 28.83 ? 111 LEU   B CD2 1 
ATOM   3737 N N   . ALA   B 1 111 ? -6.930  35.905  16.225  1.00 24.71 ? 112 ALA   B N   1 
ATOM   3738 C CA  . ALA   B 1 111 ? -6.841  34.681  15.429  1.00 21.03 ? 112 ALA   B CA  1 
ATOM   3739 C C   . ALA   B 1 111 ? -6.123  34.896  14.102  1.00 20.75 ? 112 ALA   B C   1 
ATOM   3740 O O   . ALA   B 1 111 ? -5.565  33.934  13.551  1.00 21.17 ? 112 ALA   B O   1 
ATOM   3741 C CB  . ALA   B 1 111 ? -8.239  34.116  15.171  1.00 22.09 ? 112 ALA   B CB  1 
ATOM   3742 N N   . THR   B 1 112 ? -6.153  36.122  13.556  1.00 21.80 ? 113 THR   B N   1 
ATOM   3743 C CA  . THR   B 1 112 ? -5.522  36.428  12.274  1.00 19.56 ? 113 THR   B CA  1 
ATOM   3744 C C   . THR   B 1 112 ? -4.328  37.375  12.405  1.00 20.25 ? 113 THR   B C   1 
ATOM   3745 O O   . THR   B 1 112 ? -3.918  37.995  11.412  1.00 18.83 ? 113 THR   B O   1 
ATOM   3746 C CB  . THR   B 1 112 ? -6.547  36.989  11.284  1.00 19.88 ? 113 THR   B CB  1 
ATOM   3747 O OG1 . THR   B 1 112 ? -7.154  38.175  11.816  1.00 21.28 ? 113 THR   B OG1 1 
ATOM   3748 C CG2 . THR   B 1 112 ? -7.630  35.945  10.983  1.00 21.00 ? 113 THR   B CG2 1 
ATOM   3749 N N   . TYR   B 1 113 ? -3.747  37.476  13.608  1.00 19.51 ? 114 TYR   B N   1 
ATOM   3750 C CA  . TYR   B 1 113 ? -2.412  38.048  13.827  1.00 20.11 ? 114 TYR   B CA  1 
ATOM   3751 C C   . TYR   B 1 113 ? -2.354  39.559  13.584  1.00 19.92 ? 114 TYR   B C   1 
ATOM   3752 O O   . TYR   B 1 113 ? -1.320  40.068  13.165  1.00 19.65 ? 114 TYR   B O   1 
ATOM   3753 C CB  . TYR   B 1 113 ? -1.338  37.348  12.970  1.00 18.45 ? 114 TYR   B CB  1 
ATOM   3754 C CG  . TYR   B 1 113 ? -1.598  35.872  12.664  1.00 19.98 ? 114 TYR   B CG  1 
ATOM   3755 C CD1 . TYR   B 1 113 ? -1.526  34.902  13.659  1.00 19.45 ? 114 TYR   B CD1 1 
ATOM   3756 C CD2 . TYR   B 1 113 ? -1.910  35.463  11.375  1.00 17.05 ? 114 TYR   B CD2 1 
ATOM   3757 C CE1 . TYR   B 1 113 ? -1.766  33.564  13.373  1.00 21.89 ? 114 TYR   B CE1 1 
ATOM   3758 C CE2 . TYR   B 1 113 ? -2.158  34.126  11.075  1.00 18.29 ? 114 TYR   B CE2 1 
ATOM   3759 C CZ  . TYR   B 1 113 ? -2.073  33.182  12.075  1.00 20.13 ? 114 TYR   B CZ  1 
ATOM   3760 O OH  . TYR   B 1 113 ? -2.328  31.851  11.783  1.00 20.94 ? 114 TYR   B OH  1 
ATOM   3761 N N   . THR   B 1 114 ? -3.412  40.307  13.914  1.00 19.83 ? 115 THR   B N   1 
ATOM   3762 C CA  . THR   B 1 114 ? -3.386  41.747  13.642  1.00 20.10 ? 115 THR   B CA  1 
ATOM   3763 C C   . THR   B 1 114 ? -3.496  42.607  14.904  1.00 21.36 ? 115 THR   B C   1 
ATOM   3764 O O   . THR   B 1 114 ? -3.898  43.778  14.824  1.00 20.93 ? 115 THR   B O   1 
ATOM   3765 C CB  . THR   B 1 114 ? -4.482  42.152  12.647  1.00 21.61 ? 115 THR   B CB  1 
ATOM   3766 O OG1 . THR   B 1 114 ? -5.773  41.854  13.187  1.00 22.01 ? 115 THR   B OG1 1 
ATOM   3767 C CG2 . THR   B 1 114 ? -4.290  41.449  11.314  1.00 19.32 ? 115 THR   B CG2 1 
ATOM   3768 N N   . SER   B 1 115 ? -3.090  42.087  16.063  1.00 20.76 ? 116 SER   B N   1 
ATOM   3769 C CA  . SER   B 1 115 ? -3.111  42.903  17.276  1.00 23.13 ? 116 SER   B CA  1 
ATOM   3770 C C   . SER   B 1 115 ? -2.206  44.121  17.163  1.00 22.72 ? 116 SER   B C   1 
ATOM   3771 O O   . SER   B 1 115 ? -2.446  45.134  17.832  1.00 24.03 ? 116 SER   B O   1 
ATOM   3772 C CB  . SER   B 1 115 ? -2.677  42.076  18.485  1.00 26.27 ? 116 SER   B CB  1 
ATOM   3773 O OG  . SER   B 1 115 ? -1.276  41.864  18.448  1.00 26.11 ? 116 SER   B OG  1 
ATOM   3774 N N   . GLY   B 1 116 ? -1.163  44.041  16.338  1.00 21.64 ? 117 GLY   B N   1 
ATOM   3775 C CA  . GLY   B 1 116 ? -0.261  45.161  16.149  1.00 22.44 ? 117 GLY   B CA  1 
ATOM   3776 C C   . GLY   B 1 116 ? 0.965   45.165  17.038  1.00 24.30 ? 117 GLY   B C   1 
ATOM   3777 O O   . GLY   B 1 116 ? 1.820   46.047  16.877  1.00 24.93 ? 117 GLY   B O   1 
ATOM   3778 N N   . ASN   B 1 117 ? 1.095   44.201  17.953  1.00 26.11 ? 118 ASN   B N   1 
ATOM   3779 C CA  . ASN   B 1 117 ? 2.307   44.094  18.754  1.00 24.41 ? 118 ASN   B CA  1 
ATOM   3780 C C   . ASN   B 1 117 ? 2.484   42.702  19.353  1.00 25.31 ? 118 ASN   B C   1 
ATOM   3781 O O   . ASN   B 1 117 ? 2.701   42.566  20.562  1.00 29.73 ? 118 ASN   B O   1 
ATOM   3782 C CB  . ASN   B 1 117 ? 2.311   45.138  19.868  1.00 28.25 ? 118 ASN   B CB  1 
ATOM   3783 C CG  . ASN   B 1 117 ? 3.691   45.342  20.448  1.00 29.41 ? 118 ASN   B CG  1 
ATOM   3784 O OD1 . ASN   B 1 117 ? 4.690   44.988  19.817  1.00 31.60 ? 118 ASN   B OD1 1 
ATOM   3785 N ND2 . ASN   B 1 117 ? 3.759   45.911  21.644  1.00 32.96 ? 118 ASN   B ND2 1 
ATOM   3786 N N   . LEU   B 1 118 ? 2.399   41.667  18.518  1.00 27.65 ? 119 LEU   B N   1 
ATOM   3787 C CA  . LEU   B 1 118 ? 2.727   40.315  18.954  1.00 29.55 ? 119 LEU   B CA  1 
ATOM   3788 C C   . LEU   B 1 118 ? 3.592   39.657  17.892  1.00 27.53 ? 119 LEU   B C   1 
ATOM   3789 O O   . LEU   B 1 118 ? 3.211   39.602  16.715  1.00 27.65 ? 119 LEU   B O   1 
ATOM   3790 C CB  . LEU   B 1 118 ? 1.468   39.478  19.223  1.00 26.45 ? 119 LEU   B CB  1 
ATOM   3791 C CG  . LEU   B 1 118 ? 0.662   39.870  20.470  1.00 28.38 ? 119 LEU   B CG  1 
ATOM   3792 C CD1 . LEU   B 1 118 ? -0.589  39.017  20.567  1.00 28.59 ? 119 LEU   B CD1 1 
ATOM   3793 C CD2 . LEU   B 1 118 ? 1.485   39.769  21.777  1.00 29.51 ? 119 LEU   B CD2 1 
ATOM   3794 N N   . ALA   B 1 119 ? 4.753   39.167  18.314  1.00 30.08 ? 120 ALA   B N   1 
ATOM   3795 C CA  . ALA   B 1 119 ? 5.749   38.630  17.402  1.00 31.79 ? 120 ALA   B CA  1 
ATOM   3796 C C   . ALA   B 1 119 ? 5.550   37.126  17.262  1.00 29.34 ? 120 ALA   B C   1 
ATOM   3797 O O   . ALA   B 1 119 ? 4.592   36.555  17.786  1.00 29.41 ? 120 ALA   B O   1 
ATOM   3798 C CB  . ALA   B 1 119 ? 7.156   38.958  17.894  1.00 31.88 ? 120 ALA   B CB  1 
ATOM   3799 N N   . LEU   B 1 120 ? 6.476   36.471  16.562  1.00 30.61 ? 121 LEU   B N   1 
ATOM   3800 C CA  . LEU   B 1 120 ? 6.347   35.038  16.319  1.00 29.70 ? 121 LEU   B CA  1 
ATOM   3801 C C   . LEU   B 1 120 ? 6.229   34.261  17.621  1.00 32.91 ? 121 LEU   B C   1 
ATOM   3802 O O   . LEU   B 1 120 ? 5.374   33.374  17.750  1.00 31.36 ? 121 LEU   B O   1 
ATOM   3803 C CB  . LEU   B 1 120 ? 7.541   34.544  15.509  1.00 31.83 ? 121 LEU   B CB  1 
ATOM   3804 C CG  . LEU   B 1 120 ? 7.531   33.062  15.134  1.00 36.45 ? 121 LEU   B CG  1 
ATOM   3805 C CD1 . LEU   B 1 120 ? 6.271   32.735  14.340  1.00 31.75 ? 121 LEU   B CD1 1 
ATOM   3806 C CD2 . LEU   B 1 120 ? 8.787   32.747  14.339  1.00 35.62 ? 121 LEU   B CD2 1 
ATOM   3807 N N   . GLN   B 1 121 ? 7.067   34.587  18.604  1.00 33.39 ? 122 GLN   B N   1 
ATOM   3808 C CA  . GLN   B 1 121 ? 7.125   33.860  19.860  1.00 36.76 ? 122 GLN   B CA  1 
ATOM   3809 C C   . GLN   B 1 121 ? 6.905   34.796  21.039  1.00 38.73 ? 122 GLN   B C   1 
ATOM   3810 O O   . GLN   B 1 121 ? 7.045   36.018  20.932  1.00 38.63 ? 122 GLN   B O   1 
ATOM   3811 C CB  . GLN   B 1 121 ? 8.480   33.157  20.046  1.00 37.59 ? 122 GLN   B CB  1 
ATOM   3812 C CG  . GLN   B 1 121 ? 8.975   32.389  18.835  1.00 40.06 ? 122 GLN   B CG  1 
ATOM   3813 C CD  . GLN   B 1 121 ? 8.272   31.062  18.663  1.00 37.83 ? 122 GLN   B CD  1 
ATOM   3814 O OE1 . GLN   B 1 121 ? 7.416   30.687  19.468  1.00 36.91 ? 122 GLN   B OE1 1 
ATOM   3815 N NE2 . GLN   B 1 121 ? 8.633   30.337  17.611  1.00 43.65 ? 122 GLN   B NE2 1 
ATOM   3816 N N   . PHE   B 1 122 ? 6.550   34.195  22.168  1.00 40.29 ? 123 PHE   B N   1 
ATOM   3817 C CA  . PHE   B 1 122 ? 6.739   34.854  23.446  1.00 44.58 ? 123 PHE   B CA  1 
ATOM   3818 C C   . PHE   B 1 122 ? 8.222   35.164  23.634  1.00 50.29 ? 123 PHE   B C   1 
ATOM   3819 O O   . PHE   B 1 122 ? 9.083   34.434  23.129  1.00 49.27 ? 123 PHE   B O   1 
ATOM   3820 C CB  . PHE   B 1 122 ? 6.260   33.966  24.587  1.00 45.89 ? 123 PHE   B CB  1 
ATOM   3821 C CG  . PHE   B 1 122 ? 4.775   33.928  24.751  1.00 42.58 ? 123 PHE   B CG  1 
ATOM   3822 C CD1 . PHE   B 1 122 ? 4.102   35.006  25.306  1.00 42.74 ? 123 PHE   B CD1 1 
ATOM   3823 C CD2 . PHE   B 1 122 ? 4.049   32.808  24.372  1.00 44.16 ? 123 PHE   B CD2 1 
ATOM   3824 C CE1 . PHE   B 1 122 ? 2.732   34.969  25.479  1.00 43.60 ? 123 PHE   B CE1 1 
ATOM   3825 C CE2 . PHE   B 1 122 ? 2.676   32.765  24.536  1.00 43.02 ? 123 PHE   B CE2 1 
ATOM   3826 C CZ  . PHE   B 1 122 ? 2.016   33.849  25.092  1.00 43.32 ? 123 PHE   B CZ  1 
ATOM   3827 N N   . PRO   B 1 123 ? 8.553   36.235  24.351  1.00 54.54 ? 124 PRO   B N   1 
ATOM   3828 C CA  . PRO   B 1 123 ? 9.964   36.486  24.662  1.00 56.61 ? 124 PRO   B CA  1 
ATOM   3829 C C   . PRO   B 1 123 ? 10.556  35.335  25.464  1.00 58.24 ? 124 PRO   B C   1 
ATOM   3830 O O   . PRO   B 1 123 ? 9.845   34.596  26.151  1.00 57.74 ? 124 PRO   B O   1 
ATOM   3831 C CB  . PRO   B 1 123 ? 9.937   37.796  25.464  1.00 56.79 ? 124 PRO   B CB  1 
ATOM   3832 C CG  . PRO   B 1 123 ? 8.502   38.048  25.800  1.00 56.54 ? 124 PRO   B CG  1 
ATOM   3833 C CD  . PRO   B 1 123 ? 7.673   37.330  24.789  1.00 50.82 ? 124 PRO   B CD  1 
ATOM   3834 N N   . ASP   B 1 124 ? 11.879  35.183  25.347  1.00 59.52 ? 125 ASP   B N   1 
ATOM   3835 C CA  . ASP   B 1 124 ? 12.559  33.996  25.863  1.00 64.26 ? 125 ASP   B CA  1 
ATOM   3836 C C   . ASP   B 1 124 ? 12.226  33.726  27.325  1.00 64.08 ? 125 ASP   B C   1 
ATOM   3837 O O   . ASP   B 1 124 ? 12.071  32.568  27.728  1.00 65.18 ? 125 ASP   B O   1 
ATOM   3838 C CB  . ASP   B 1 124 ? 14.071  34.147  25.682  1.00 68.24 ? 125 ASP   B CB  1 
ATOM   3839 C CG  . ASP   B 1 124 ? 14.571  33.535  24.388  1.00 71.64 ? 125 ASP   B CG  1 
ATOM   3840 O OD1 . ASP   B 1 124 ? 14.561  32.291  24.278  1.00 75.25 ? 125 ASP   B OD1 1 
ATOM   3841 O OD2 . ASP   B 1 124 ? 14.963  34.297  23.479  1.00 73.26 ? 125 ASP   B OD2 1 
ATOM   3842 N N   . GLU   B 1 125 ? 12.094  34.780  28.132  1.00 65.71 ? 126 GLU   B N   1 
ATOM   3843 C CA  . GLU   B 1 125 ? 11.951  34.613  29.575  1.00 67.39 ? 126 GLU   B CA  1 
ATOM   3844 C C   . GLU   B 1 125 ? 10.520  34.327  30.018  1.00 65.49 ? 126 GLU   B C   1 
ATOM   3845 O O   . GLU   B 1 125 ? 10.275  34.234  31.227  1.00 65.35 ? 126 GLU   B O   1 
ATOM   3846 C CB  . GLU   B 1 125 ? 12.477  35.854  30.311  1.00 67.00 ? 126 GLU   B CB  1 
ATOM   3847 C CG  . GLU   B 1 125 ? 11.524  37.045  30.332  1.00 71.16 ? 126 GLU   B CG  1 
ATOM   3848 C CD  . GLU   B 1 125 ? 11.524  37.832  29.034  1.00 68.69 ? 126 GLU   B CD  1 
ATOM   3849 O OE1 . GLU   B 1 125 ? 12.256  37.442  28.100  1.00 68.34 ? 126 GLU   B OE1 1 
ATOM   3850 O OE2 . GLU   B 1 125 ? 10.794  38.846  28.953  1.00 66.86 ? 126 GLU   B OE2 1 
ATOM   3851 N N   . VAL   B 1 126 ? 9.576   34.177  29.095  1.00 64.98 ? 127 VAL   B N   1 
ATOM   3852 C CA  . VAL   B 1 126 ? 8.189   33.880  29.438  1.00 63.57 ? 127 VAL   B CA  1 
ATOM   3853 C C   . VAL   B 1 126 ? 8.018   32.369  29.342  1.00 64.79 ? 127 VAL   B C   1 
ATOM   3854 O O   . VAL   B 1 126 ? 7.896   31.811  28.247  1.00 64.73 ? 127 VAL   B O   1 
ATOM   3855 C CB  . VAL   B 1 126 ? 7.204   34.626  28.536  1.00 62.07 ? 127 VAL   B CB  1 
ATOM   3856 C CG1 . VAL   B 1 126 ? 5.771   34.366  28.987  1.00 59.42 ? 127 VAL   B CG1 1 
ATOM   3857 C CG2 . VAL   B 1 126 ? 7.502   36.107  28.558  1.00 59.39 ? 127 VAL   B CG2 1 
ATOM   3858 N N   . LYS   B 1 127 ? 8.007   31.702  30.497  1.00 65.08 ? 128 LYS   B N   1 
ATOM   3859 C CA  . LYS   B 1 127 ? 7.916   30.247  30.557  1.00 65.84 ? 128 LYS   B CA  1 
ATOM   3860 C C   . LYS   B 1 127 ? 6.712   29.787  31.368  1.00 63.43 ? 128 LYS   B C   1 
ATOM   3861 O O   . LYS   B 1 127 ? 5.836   29.108  30.824  1.00 69.99 ? 128 LYS   B O   1 
ATOM   3862 C CB  . LYS   B 1 127 ? 9.216   29.667  31.132  1.00 63.94 ? 128 LYS   B CB  1 
ATOM   3863 C CG  . LYS   B 1 127 ? 10.460  30.067  30.352  1.00 65.53 ? 128 LYS   B CG  1 
ATOM   3864 C CD  . LYS   B 1 127 ? 11.735  29.670  31.078  1.00 66.16 ? 128 LYS   B CD  1 
ATOM   3865 C CE  . LYS   B 1 127 ? 12.964  30.198  30.354  1.00 66.80 ? 128 LYS   B CE  1 
ATOM   3866 N NZ  . LYS   B 1 127 ? 13.021  29.712  28.944  1.00 67.21 ? 128 LYS   B NZ  1 
ATOM   3867 N N   . THR   B 1 128 ? 6.634   30.141  32.648  1.00 68.09 ? 129 THR   B N   1 
ATOM   3868 C CA  . THR   B 1 128 ? 5.555   29.661  33.500  1.00 68.16 ? 129 THR   B CA  1 
ATOM   3869 C C   . THR   B 1 128 ? 4.229   30.316  33.118  1.00 65.57 ? 129 THR   B C   1 
ATOM   3870 O O   . THR   B 1 128 ? 4.171   31.249  32.311  1.00 65.54 ? 129 THR   B O   1 
ATOM   3871 C CB  . THR   B 1 128 ? 5.864   29.936  34.972  1.00 65.08 ? 129 THR   B CB  1 
ATOM   3872 O OG1 . THR   B 1 128 ? 4.849   29.343  35.790  1.00 70.41 ? 129 THR   B OG1 1 
ATOM   3873 C CG2 . THR   B 1 128 ? 5.890   31.425  35.238  1.00 65.78 ? 129 THR   B CG2 1 
ATOM   3874 N N   . ASP   B 1 129 ? 3.149   29.811  33.723  1.00 63.68 ? 130 ASP   B N   1 
ATOM   3875 C CA  . ASP   B 1 129 ? 1.827   30.373  33.466  1.00 63.01 ? 130 ASP   B CA  1 
ATOM   3876 C C   . ASP   B 1 129 ? 1.719   31.801  33.982  1.00 67.12 ? 130 ASP   B C   1 
ATOM   3877 O O   . ASP   B 1 129 ? 1.134   32.663  33.315  1.00 61.47 ? 130 ASP   B O   1 
ATOM   3878 C CB  . ASP   B 1 129 ? 0.746   29.503  34.102  1.00 60.73 ? 130 ASP   B CB  1 
ATOM   3879 C CG  . ASP   B 1 129 ? 0.465   28.245  33.305  1.00 67.71 ? 130 ASP   B CG  1 
ATOM   3880 O OD1 . ASP   B 1 129 ? 0.987   28.121  32.174  1.00 69.52 ? 130 ASP   B OD1 1 
ATOM   3881 O OD2 . ASP   B 1 129 ? -0.280  27.381  33.815  1.00 72.59 ? 130 ASP   B OD2 1 
ATOM   3882 N N   . GLN   B 1 130 ? 2.266   32.073  35.170  1.00 61.90 ? 131 GLN   B N   1 
ATOM   3883 C CA  . GLN   B 1 130 ? 2.169   33.421  35.718  1.00 61.70 ? 131 GLN   B CA  1 
ATOM   3884 C C   . GLN   B 1 130 ? 2.919   34.424  34.853  1.00 61.94 ? 131 GLN   B C   1 
ATOM   3885 O O   . GLN   B 1 130 ? 2.493   35.576  34.720  1.00 60.73 ? 131 GLN   B O   1 
ATOM   3886 C CB  . GLN   B 1 130 ? 2.685   33.449  37.156  1.00 64.24 ? 131 GLN   B CB  1 
ATOM   3887 C CG  . GLN   B 1 130 ? 1.625   33.076  38.183  1.00 62.42 ? 131 GLN   B CG  1 
ATOM   3888 C CD  . GLN   B 1 130 ? 0.366   33.921  38.052  1.00 61.28 ? 131 GLN   B CD  1 
ATOM   3889 O OE1 . GLN   B 1 130 ? -0.674  33.436  37.607  1.00 66.58 ? 131 GLN   B OE1 1 
ATOM   3890 N NE2 . GLN   B 1 130 ? 0.455   35.185  38.442  1.00 60.10 ? 131 GLN   B NE2 1 
ATOM   3891 N N   . GLN   B 1 131 ? 4.037   34.008  34.254  1.00 65.13 ? 132 GLN   B N   1 
ATOM   3892 C CA  . GLN   B 1 131 ? 4.732   34.888  33.320  1.00 61.16 ? 132 GLN   B CA  1 
ATOM   3893 C C   . GLN   B 1 131 ? 3.875   35.179  32.095  1.00 63.36 ? 132 GLN   B C   1 
ATOM   3894 O O   . GLN   B 1 131 ? 4.009   36.243  31.482  1.00 59.09 ? 132 GLN   B O   1 
ATOM   3895 C CB  . GLN   B 1 131 ? 6.070   34.272  32.904  1.00 63.56 ? 132 GLN   B CB  1 
ATOM   3896 C CG  . GLN   B 1 131 ? 7.180   34.402  33.946  1.00 66.16 ? 132 GLN   B CG  1 
ATOM   3897 C CD  . GLN   B 1 131 ? 8.320   33.427  33.708  1.00 66.66 ? 132 GLN   B CD  1 
ATOM   3898 O OE1 . GLN   B 1 131 ? 8.186   32.475  32.939  1.00 67.57 ? 132 GLN   B OE1 1 
ATOM   3899 N NE2 . GLN   B 1 131 ? 9.447   33.658  34.370  1.00 72.83 ? 132 GLN   B NE2 1 
ATOM   3900 N N   . VAL   B 1 132 ? 2.986   34.254  31.732  1.00 60.16 ? 133 VAL   B N   1 
ATOM   3901 C CA  . VAL   B 1 132 ? 2.081   34.471  30.607  1.00 60.04 ? 133 VAL   B CA  1 
ATOM   3902 C C   . VAL   B 1 132 ? 0.957   35.427  30.990  1.00 59.43 ? 133 VAL   B C   1 
ATOM   3903 O O   . VAL   B 1 132 ? 0.555   36.283  30.191  1.00 55.28 ? 133 VAL   B O   1 
ATOM   3904 C CB  . VAL   B 1 132 ? 1.545   33.117  30.108  1.00 61.20 ? 133 VAL   B CB  1 
ATOM   3905 C CG1 . VAL   B 1 132 ? 0.170   33.272  29.474  1.00 61.26 ? 133 VAL   B CG1 1 
ATOM   3906 C CG2 . VAL   B 1 132 ? 2.525   32.508  29.123  1.00 61.20 ? 133 VAL   B CG2 1 
ATOM   3907 N N   . LEU   B 1 133 ? 0.441   35.304  32.215  1.00 61.86 ? 134 LEU   B N   1 
ATOM   3908 C CA  . LEU   B 1 133 ? -0.607  36.205  32.681  1.00 62.04 ? 134 LEU   B CA  1 
ATOM   3909 C C   . LEU   B 1 133 ? -0.116  37.648  32.717  1.00 58.98 ? 134 LEU   B C   1 
ATOM   3910 O O   . LEU   B 1 133 ? -0.797  38.561  32.233  1.00 56.23 ? 134 LEU   B O   1 
ATOM   3911 C CB  . LEU   B 1 133 ? -1.094  35.769  34.063  1.00 60.01 ? 134 LEU   B CB  1 
ATOM   3912 C CG  . LEU   B 1 133 ? -2.043  36.749  34.755  1.00 63.54 ? 134 LEU   B CG  1 
ATOM   3913 C CD1 . LEU   B 1 133 ? -3.328  36.892  33.955  1.00 59.55 ? 134 LEU   B CD1 1 
ATOM   3914 C CD2 . LEU   B 1 133 ? -2.327  36.327  36.193  1.00 62.51 ? 134 LEU   B CD2 1 
ATOM   3915 N N   . THR   B 1 134 ? 1.072   37.870  33.283  1.00 59.24 ? 135 THR   B N   1 
ATOM   3916 C CA  . THR   B 1 134 ? 1.621   39.217  33.389  1.00 56.11 ? 135 THR   B CA  1 
ATOM   3917 C C   . THR   B 1 134 ? 2.136   39.749  32.058  1.00 54.15 ? 135 THR   B C   1 
ATOM   3918 O O   . THR   B 1 134 ? 2.264   40.969  31.904  1.00 51.32 ? 135 THR   B O   1 
ATOM   3919 C CB  . THR   B 1 134 ? 2.747   39.256  34.429  1.00 63.54 ? 135 THR   B CB  1 
ATOM   3920 O OG1 . THR   B 1 134 ? 3.886   38.538  33.935  1.00 70.85 ? 135 THR   B OG1 1 
ATOM   3921 C CG2 . THR   B 1 134 ? 2.288   38.614  35.727  1.00 58.17 ? 135 THR   B CG2 1 
ATOM   3922 N N   . PHE   B 1 135 ? 2.449   38.869  31.102  1.00 53.68 ? 136 PHE   B N   1 
ATOM   3923 C CA  . PHE   B 1 135 ? 2.806   39.340  29.766  1.00 51.68 ? 136 PHE   B CA  1 
ATOM   3924 C C   . PHE   B 1 135 ? 1.627   40.040  29.107  1.00 49.38 ? 136 PHE   B C   1 
ATOM   3925 O O   . PHE   B 1 135 ? 1.779   41.121  28.528  1.00 46.64 ? 136 PHE   B O   1 
ATOM   3926 C CB  . PHE   B 1 135 ? 3.291   38.180  28.892  1.00 46.97 ? 136 PHE   B CB  1 
ATOM   3927 C CG  . PHE   B 1 135 ? 3.573   38.576  27.462  1.00 46.80 ? 136 PHE   B CG  1 
ATOM   3928 C CD1 . PHE   B 1 135 ? 4.767   39.194  27.122  1.00 45.27 ? 136 PHE   B CD1 1 
ATOM   3929 C CD2 . PHE   B 1 135 ? 2.642   38.331  26.459  1.00 45.26 ? 136 PHE   B CD2 1 
ATOM   3930 C CE1 . PHE   B 1 135 ? 5.027   39.565  25.813  1.00 42.25 ? 136 PHE   B CE1 1 
ATOM   3931 C CE2 . PHE   B 1 135 ? 2.898   38.696  25.146  1.00 40.92 ? 136 PHE   B CE2 1 
ATOM   3932 C CZ  . PHE   B 1 135 ? 4.091   39.310  24.823  1.00 40.30 ? 136 PHE   B CZ  1 
ATOM   3933 N N   . PHE   B 1 136 ? 0.438   39.441  29.183  1.00 47.71 ? 137 PHE   B N   1 
ATOM   3934 C CA  . PHE   B 1 136 ? -0.714  40.052  28.530  1.00 48.45 ? 137 PHE   B CA  1 
ATOM   3935 C C   . PHE   B 1 136 ? -1.257  41.242  29.311  1.00 46.09 ? 137 PHE   B C   1 
ATOM   3936 O O   . PHE   B 1 136 ? -1.823  42.159  28.707  1.00 43.92 ? 137 PHE   B O   1 
ATOM   3937 C CB  . PHE   B 1 136 ? -1.809  39.009  28.300  1.00 44.12 ? 137 PHE   B CB  1 
ATOM   3938 C CG  . PHE   B 1 136 ? -1.528  38.094  27.143  1.00 38.68 ? 137 PHE   B CG  1 
ATOM   3939 C CD1 . PHE   B 1 136 ? -1.454  38.593  25.850  1.00 39.97 ? 137 PHE   B CD1 1 
ATOM   3940 C CD2 . PHE   B 1 136 ? -1.334  36.735  27.341  1.00 40.61 ? 137 PHE   B CD2 1 
ATOM   3941 C CE1 . PHE   B 1 136 ? -1.190  37.754  24.782  1.00 38.50 ? 137 PHE   B CE1 1 
ATOM   3942 C CE2 . PHE   B 1 136 ? -1.076  35.891  26.270  1.00 38.19 ? 137 PHE   B CE2 1 
ATOM   3943 C CZ  . PHE   B 1 136 ? -1.002  36.401  24.993  1.00 39.00 ? 137 PHE   B CZ  1 
ATOM   3944 N N   . LYS   B 1 137 ? -1.092  41.255  30.637  1.00 45.52 ? 138 LYS   B N   1 
ATOM   3945 C CA  . LYS   B 1 137 ? -1.455  42.441  31.409  1.00 49.21 ? 138 LYS   B CA  1 
ATOM   3946 C C   . LYS   B 1 137 ? -0.523  43.612  31.114  1.00 46.01 ? 138 LYS   B C   1 
ATOM   3947 O O   . LYS   B 1 137 ? -0.965  44.767  31.065  1.00 46.03 ? 138 LYS   B O   1 
ATOM   3948 C CB  . LYS   B 1 137 ? -1.441  42.121  32.903  1.00 49.43 ? 138 LYS   B CB  1 
ATOM   3949 C CG  . LYS   B 1 137 ? -2.653  41.363  33.411  1.00 53.44 ? 138 LYS   B CG  1 
ATOM   3950 C CD  . LYS   B 1 137 ? -2.424  40.939  34.864  1.00 61.68 ? 138 LYS   B CD  1 
ATOM   3951 C CE  . LYS   B 1 137 ? -3.723  40.810  35.639  1.00 66.85 ? 138 LYS   B CE  1 
ATOM   3952 N NZ  . LYS   B 1 137 ? -4.495  42.091  35.644  1.00 63.58 ? 138 LYS   B NZ  1 
ATOM   3953 N N   . ASP   B 1 138 ? 0.770   43.340  30.934  1.00 45.59 ? 139 ASP   B N   1 
ATOM   3954 C CA  . ASP   B 1 138 ? 1.744   44.392  30.667  1.00 48.56 ? 139 ASP   B CA  1 
ATOM   3955 C C   . ASP   B 1 138 ? 1.772   44.812  29.203  1.00 45.48 ? 139 ASP   B C   1 
ATOM   3956 O O   . ASP   B 1 138 ? 2.441   45.798  28.864  1.00 46.77 ? 139 ASP   B O   1 
ATOM   3957 C CB  . ASP   B 1 138 ? 3.145   43.937  31.091  1.00 52.94 ? 139 ASP   B CB  1 
ATOM   3958 C CG  . ASP   B 1 138 ? 3.273   43.742  32.594  1.00 54.35 ? 139 ASP   B CG  1 
ATOM   3959 O OD1 . ASP   B 1 138 ? 2.375   44.182  33.345  1.00 50.34 ? 139 ASP   B OD1 1 
ATOM   3960 O OD2 . ASP   B 1 138 ? 4.279   43.137  33.021  1.00 57.50 ? 139 ASP   B OD2 1 
ATOM   3961 N N   . TRP   B 1 139 ? 1.060   44.091  28.339  1.00 41.11 ? 140 TRP   B N   1 
ATOM   3962 C CA  . TRP   B 1 139 ? 1.080   44.365  26.906  1.00 38.20 ? 140 TRP   B CA  1 
ATOM   3963 C C   . TRP   B 1 139 ? 0.531   45.754  26.598  1.00 38.47 ? 140 TRP   B C   1 
ATOM   3964 O O   . TRP   B 1 139 ? -0.435  46.213  27.217  1.00 41.39 ? 140 TRP   B O   1 
ATOM   3965 C CB  . TRP   B 1 139 ? 0.258   43.293  26.182  1.00 38.24 ? 140 TRP   B CB  1 
ATOM   3966 C CG  . TRP   B 1 139 ? 0.258   43.366  24.680  1.00 34.22 ? 140 TRP   B CG  1 
ATOM   3967 C CD1 . TRP   B 1 139 ? 1.078   42.681  23.823  1.00 32.68 ? 140 TRP   B CD1 1 
ATOM   3968 C CD2 . TRP   B 1 139 ? -0.620  44.145  23.853  1.00 34.55 ? 140 TRP   B CD2 1 
ATOM   3969 N NE1 . TRP   B 1 139 ? 0.773   42.999  22.520  1.00 32.02 ? 140 TRP   B NE1 1 
ATOM   3970 C CE2 . TRP   B 1 139 ? -0.272  43.883  22.510  1.00 30.58 ? 140 TRP   B CE2 1 
ATOM   3971 C CE3 . TRP   B 1 139 ? -1.662  45.040  24.117  1.00 36.69 ? 140 TRP   B CE3 1 
ATOM   3972 C CZ2 . TRP   B 1 139 ? -0.921  44.497  21.434  1.00 30.39 ? 140 TRP   B CZ2 1 
ATOM   3973 C CZ3 . TRP   B 1 139 ? -2.309  45.645  23.049  1.00 34.87 ? 140 TRP   B CZ3 1 
ATOM   3974 C CH2 . TRP   B 1 139 ? -1.940  45.364  21.722  1.00 31.51 ? 140 TRP   B CH2 1 
ATOM   3975 N N   . LYS   B 1 140 ? 1.167   46.431  25.645  1.00 36.47 ? 141 LYS   B N   1 
ATOM   3976 C CA  . LYS   B 1 140 ? 0.716   47.716  25.134  1.00 35.25 ? 141 LYS   B CA  1 
ATOM   3977 C C   . LYS   B 1 140 ? 0.701   47.683  23.613  1.00 32.98 ? 141 LYS   B C   1 
ATOM   3978 O O   . LYS   B 1 140 ? 1.464   46.932  22.997  1.00 33.18 ? 141 LYS   B O   1 
ATOM   3979 C CB  . LYS   B 1 140 ? 1.623   48.869  25.602  1.00 36.12 ? 141 LYS   B CB  1 
ATOM   3980 C CG  . LYS   B 1 140 ? 1.726   49.029  27.118  1.00 40.86 ? 141 LYS   B CG  1 
ATOM   3981 C CD  . LYS   B 1 140 ? 2.575   50.242  27.492  1.00 49.00 ? 141 LYS   B CD  1 
ATOM   3982 C CE  . LYS   B 1 140 ? 2.682   50.404  29.003  1.00 54.07 ? 141 LYS   B CE  1 
ATOM   3983 N NZ  . LYS   B 1 140 ? 3.292   49.205  29.656  1.00 60.32 ? 141 LYS   B NZ  1 
ATOM   3984 N N   . PRO   B 1 141 ? -0.130  48.507  22.979  1.00 32.05 ? 142 PRO   B N   1 
ATOM   3985 C CA  . PRO   B 1 141 ? -0.174  48.519  21.513  1.00 31.52 ? 142 PRO   B CA  1 
ATOM   3986 C C   . PRO   B 1 141 ? 1.076   49.140  20.902  1.00 29.36 ? 142 PRO   B C   1 
ATOM   3987 O O   . PRO   B 1 141 ? 1.788   49.935  21.524  1.00 33.56 ? 142 PRO   B O   1 
ATOM   3988 C CB  . PRO   B 1 141 ? -1.419  49.357  21.203  1.00 33.31 ? 142 PRO   B CB  1 
ATOM   3989 C CG  . PRO   B 1 141 ? -1.576  50.247  22.412  1.00 34.20 ? 142 PRO   B CG  1 
ATOM   3990 C CD  . PRO   B 1 141 ? -1.176  49.363  23.569  1.00 33.68 ? 142 PRO   B CD  1 
ATOM   3991 N N   . LYS   B 1 142 ? 1.345   48.732  19.658  1.00 27.82 ? 143 LYS   B N   1 
ATOM   3992 C CA  . LYS   B 1 142 ? 2.380   49.357  18.833  1.00 28.97 ? 143 LYS   B CA  1 
ATOM   3993 C C   . LYS   B 1 142 ? 1.779   49.877  17.534  1.00 26.70 ? 143 LYS   B C   1 
ATOM   3994 O O   . LYS   B 1 142 ? 1.587   51.090  17.396  1.00 24.97 ? 143 LYS   B O   1 
ATOM   3995 C CB  . LYS   B 1 142 ? 3.528   48.378  18.562  1.00 29.80 ? 143 LYS   B CB  1 
ATOM   3996 C CG  . LYS   B 1 142 ? 4.728   49.034  17.884  1.00 30.23 ? 143 LYS   B CG  1 
ATOM   3997 C CD  . LYS   B 1 142 ? 5.922   48.103  17.791  1.00 30.14 ? 143 LYS   B CD  1 
ATOM   3998 C CE  . LYS   B 1 142 ? 5.781   47.107  16.670  1.00 29.90 ? 143 LYS   B CE  1 
ATOM   3999 N NZ  . LYS   B 1 142 ? 6.941   46.182  16.674  1.00 33.29 ? 143 LYS   B NZ  1 
ATOM   4000 N N   . ASN   B 1 143 ? 1.472   49.011  16.570  1.00 26.20 ? 144 ASN   B N   1 
ATOM   4001 C CA  . ASN   B 1 143 ? 0.749   49.449  15.385  1.00 24.73 ? 144 ASN   B CA  1 
ATOM   4002 C C   . ASN   B 1 143 ? -0.739  49.596  15.700  1.00 27.80 ? 144 ASN   B C   1 
ATOM   4003 O O   . ASN   B 1 143 ? -1.237  49.098  16.716  1.00 31.28 ? 144 ASN   B O   1 
ATOM   4004 C CB  . ASN   B 1 143 ? 0.962   48.478  14.218  1.00 23.58 ? 144 ASN   B CB  1 
ATOM   4005 C CG  . ASN   B 1 143 ? 2.371   48.571  13.639  1.00 27.50 ? 144 ASN   B CG  1 
ATOM   4006 O OD1 . ASN   B 1 143 ? 2.746   49.591  13.064  1.00 25.76 ? 144 ASN   B OD1 1 
ATOM   4007 N ND2 . ASN   B 1 143 ? 3.152   47.512  13.799  1.00 28.20 ? 144 ASN   B ND2 1 
ATOM   4008 N N   . SER   B 1 144 ? -1.443  50.326  14.834  1.00 27.49 ? 145 SER   B N   1 
ATOM   4009 C CA  . SER   B 1 144 ? -2.890  50.446  14.972  1.00 23.96 ? 145 SER   B CA  1 
ATOM   4010 C C   . SER   B 1 144 ? -3.521  49.063  14.927  1.00 21.60 ? 145 SER   B C   1 
ATOM   4011 O O   . SER   B 1 144 ? -3.198  48.254  14.052  1.00 21.54 ? 145 SER   B O   1 
ATOM   4012 C CB  . SER   B 1 144 ? -3.471  51.315  13.862  1.00 27.50 ? 145 SER   B CB  1 
ATOM   4013 O OG  . SER   B 1 144 ? -2.950  52.623  13.926  1.00 31.05 ? 145 SER   B OG  1 
ATOM   4014 N N   . ILE   B 1 145 ? -4.421  48.795  15.878  1.00 25.11 ? 146 ILE   B N   1 
ATOM   4015 C CA  . ILE   B 1 145 ? -5.008  47.462  16.004  1.00 25.88 ? 146 ILE   B CA  1 
ATOM   4016 C C   . ILE   B 1 145 ? -5.781  47.118  14.739  1.00 26.57 ? 146 ILE   B C   1 
ATOM   4017 O O   . ILE   B 1 145 ? -6.588  47.918  14.245  1.00 26.20 ? 146 ILE   B O   1 
ATOM   4018 C CB  . ILE   B 1 145 ? -5.896  47.395  17.257  1.00 26.36 ? 146 ILE   B CB  1 
ATOM   4019 C CG1 . ILE   B 1 145 ? -5.029  47.449  18.513  1.00 27.71 ? 146 ILE   B CG1 1 
ATOM   4020 C CG2 . ILE   B 1 145 ? -6.767  46.144  17.262  1.00 29.02 ? 146 ILE   B CG2 1 
ATOM   4021 C CD1 . ILE   B 1 145 ? -5.825  47.478  19.809  1.00 30.35 ? 146 ILE   B CD1 1 
ATOM   4022 N N   . GLY   B 1 146 ? -5.511  45.931  14.190  1.00 21.14 ? 147 GLY   B N   1 
ATOM   4023 C CA  . GLY   B 1 146 ? -6.192  45.439  13.013  1.00 23.55 ? 147 GLY   B CA  1 
ATOM   4024 C C   . GLY   B 1 146 ? -5.525  45.758  11.686  1.00 21.53 ? 147 GLY   B C   1 
ATOM   4025 O O   . GLY   B 1 146 ? -5.896  45.157  10.668  1.00 22.43 ? 147 GLY   B O   1 
ATOM   4026 N N   . GLU   B 1 147 ? -4.537  46.655  11.661  1.00 24.45 ? 148 GLU   B N   1 
ATOM   4027 C CA  A GLU   B 1 147 ? -3.974  47.137  10.405  0.44 21.30 ? 148 GLU   B CA  1 
ATOM   4028 C CA  B GLU   B 1 147 ? -3.985  47.122  10.397  0.56 21.28 ? 148 GLU   B CA  1 
ATOM   4029 C C   . GLU   B 1 147 ? -2.710  46.400  9.965   1.00 23.53 ? 148 GLU   B C   1 
ATOM   4030 O O   . GLU   B 1 147 ? -2.360  46.451  8.775   1.00 18.56 ? 148 GLU   B O   1 
ATOM   4031 C CB  A GLU   B 1 147 ? -3.677  48.644  10.510  0.44 21.87 ? 148 GLU   B CB  1 
ATOM   4032 C CB  B GLU   B 1 147 ? -3.730  48.635  10.478  0.56 21.87 ? 148 GLU   B CB  1 
ATOM   4033 C CG  A GLU   B 1 147 ? -3.054  49.249  9.258   0.44 23.04 ? 148 GLU   B CG  1 
ATOM   4034 C CG  B GLU   B 1 147 ? -5.018  49.434  10.718  0.56 24.24 ? 148 GLU   B CG  1 
ATOM   4035 C CD  A GLU   B 1 147 ? -3.691  50.550  8.818   0.44 26.90 ? 148 GLU   B CD  1 
ATOM   4036 C CD  B GLU   B 1 147 ? -4.824  50.939  10.633  0.56 26.48 ? 148 GLU   B CD  1 
ATOM   4037 O OE1 A GLU   B 1 147 ? -4.751  50.922  9.373   0.44 25.80 ? 148 GLU   B OE1 1 
ATOM   4038 O OE1 B GLU   B 1 147 ? -3.730  51.382  10.219  0.56 27.71 ? 148 GLU   B OE1 1 
ATOM   4039 O OE2 A GLU   B 1 147 ? -3.117  51.201  7.914   0.44 25.53 ? 148 GLU   B OE2 1 
ATOM   4040 O OE2 B GLU   B 1 147 ? -5.773  51.679  10.989  0.56 28.77 ? 148 GLU   B OE2 1 
ATOM   4041 N N   . TYR   B 1 148 ? -2.021  45.704  10.871  1.00 18.72 ? 149 TYR   B N   1 
ATOM   4042 C CA  . TYR   B 1 148 ? -0.744  45.080  10.548  1.00 16.92 ? 149 TYR   B CA  1 
ATOM   4043 C C   . TYR   B 1 148 ? -0.744  43.612  10.950  1.00 17.74 ? 149 TYR   B C   1 
ATOM   4044 O O   . TYR   B 1 148 ? -1.027  43.287  12.106  1.00 21.90 ? 149 TYR   B O   1 
ATOM   4045 C CB  . TYR   B 1 148 ? 0.409   45.836  11.223  1.00 19.28 ? 149 TYR   B CB  1 
ATOM   4046 C CG  . TYR   B 1 148 ? 0.793   47.025  10.376  1.00 18.65 ? 149 TYR   B CG  1 
ATOM   4047 C CD1 . TYR   B 1 148 ? 0.029   48.187  10.386  1.00 21.30 ? 149 TYR   B CD1 1 
ATOM   4048 C CD2 . TYR   B 1 148 ? 1.880   46.949  9.514   1.00 20.04 ? 149 TYR   B CD2 1 
ATOM   4049 C CE1 . TYR   B 1 148 ? 0.365   49.253  9.555   1.00 21.78 ? 149 TYR   B CE1 1 
ATOM   4050 C CE2 . TYR   B 1 148 ? 2.227   48.002  8.699   1.00 21.74 ? 149 TYR   B CE2 1 
ATOM   4051 C CZ  . TYR   B 1 148 ? 1.464   49.142  8.718   1.00 18.39 ? 149 TYR   B CZ  1 
ATOM   4052 O OH  . TYR   B 1 148 ? 1.808   50.181  7.877   1.00 22.70 ? 149 TYR   B OH  1 
ATOM   4053 N N   . ARG   B 1 149 ? -0.420  42.741  9.992   1.00 16.41 ? 150 ARG   B N   1 
ATOM   4054 C CA  . ARG   B 1 149 ? -0.322  41.298  10.225  1.00 16.74 ? 150 ARG   B CA  1 
ATOM   4055 C C   . ARG   B 1 149 ? 1.105   40.926  10.608  1.00 21.59 ? 150 ARG   B C   1 
ATOM   4056 O O   . ARG   B 1 149 ? 2.058   41.245  9.891   1.00 20.03 ? 150 ARG   B O   1 
ATOM   4057 C CB  . ARG   B 1 149 ? -0.743  40.513  8.976   1.00 17.83 ? 150 ARG   B CB  1 
ATOM   4058 C CG  . ARG   B 1 149 ? -0.561  38.977  9.082   1.00 17.38 ? 150 ARG   B CG  1 
ATOM   4059 C CD  . ARG   B 1 149 ? -0.663  38.329  7.685   1.00 17.26 ? 150 ARG   B CD  1 
ATOM   4060 N NE  . ARG   B 1 149 ? -0.756  36.875  7.783   1.00 16.53 ? 150 ARG   B NE  1 
ATOM   4061 C CZ  . ARG   B 1 149 ? 0.273   36.047  7.831   1.00 16.95 ? 150 ARG   B CZ  1 
ATOM   4062 N NH1 . ARG   B 1 149 ? 1.523   36.489  7.825   1.00 19.61 ? 150 ARG   B NH1 1 
ATOM   4063 N NH2 . ARG   B 1 149 ? 0.046   34.737  7.911   1.00 17.69 ? 150 ARG   B NH2 1 
ATOM   4064 N N   . GLN   B 1 150 ? 1.251   40.217  11.723  1.00 20.02 ? 151 GLN   B N   1 
ATOM   4065 C CA  . GLN   B 1 150 ? 2.540   39.638  12.082  1.00 20.10 ? 151 GLN   B CA  1 
ATOM   4066 C C   . GLN   B 1 150 ? 2.276   38.223  12.564  1.00 20.63 ? 151 GLN   B C   1 
ATOM   4067 O O   . GLN   B 1 150 ? 1.690   38.035  13.634  1.00 22.38 ? 151 GLN   B O   1 
ATOM   4068 C CB  . GLN   B 1 150 ? 3.254   40.471  13.146  1.00 24.36 ? 151 GLN   B CB  1 
ATOM   4069 C CG  . GLN   B 1 150 ? 4.596   39.916  13.562  1.00 26.45 ? 151 GLN   B CG  1 
ATOM   4070 C CD  . GLN   B 1 150 ? 5.519   40.977  14.149  1.00 34.42 ? 151 GLN   B CD  1 
ATOM   4071 O OE1 . GLN   B 1 150 ? 5.074   41.935  14.798  1.00 36.22 ? 151 GLN   B OE1 1 
ATOM   4072 N NE2 . GLN   B 1 150 ? 6.816   40.813  13.914  1.00 37.52 ? 151 GLN   B NE2 1 
ATOM   4073 N N   . TYR   B 1 151 ? 2.661   37.234  11.758  1.00 19.09 ? 152 TYR   B N   1 
ATOM   4074 C CA  . TYR   B 1 151 ? 2.393   35.844  12.127  1.00 21.09 ? 152 TYR   B CA  1 
ATOM   4075 C C   . TYR   B 1 151 ? 2.901   35.583  13.541  1.00 23.15 ? 152 TYR   B C   1 
ATOM   4076 O O   . TYR   B 1 151 ? 4.047   35.903  13.864  1.00 23.97 ? 152 TYR   B O   1 
ATOM   4077 C CB  . TYR   B 1 151 ? 3.070   34.903  11.126  1.00 21.03 ? 152 TYR   B CB  1 
ATOM   4078 C CG  . TYR   B 1 151 ? 2.682   33.451  11.275  1.00 20.46 ? 152 TYR   B CG  1 
ATOM   4079 C CD1 . TYR   B 1 151 ? 1.404   33.016  10.949  1.00 20.69 ? 152 TYR   B CD1 1 
ATOM   4080 C CD2 . TYR   B 1 151 ? 3.603   32.522  11.716  1.00 23.13 ? 152 TYR   B CD2 1 
ATOM   4081 C CE1 . TYR   B 1 151 ? 1.050   31.681  11.079  1.00 21.19 ? 152 TYR   B CE1 1 
ATOM   4082 C CE2 . TYR   B 1 151 ? 3.262   31.189  11.845  1.00 23.49 ? 152 TYR   B CE2 1 
ATOM   4083 C CZ  . TYR   B 1 151 ? 1.985   30.782  11.522  1.00 22.16 ? 152 TYR   B CZ  1 
ATOM   4084 O OH  . TYR   B 1 151 ? 1.680   29.452  11.659  1.00 25.43 ? 152 TYR   B OH  1 
ATOM   4085 N N   . SER   B 1 152 ? 2.041   35.022  14.397  1.00 21.79 ? 153 SER   B N   1 
ATOM   4086 C CA  . SER   B 1 152 ? 2.309   35.081  15.838  1.00 24.50 ? 153 SER   B CA  1 
ATOM   4087 C C   . SER   B 1 152 ? 1.693   33.914  16.593  1.00 27.02 ? 153 SER   B C   1 
ATOM   4088 O O   . SER   B 1 152 ? 0.469   33.757  16.617  1.00 25.07 ? 153 SER   B O   1 
ATOM   4089 C CB  . SER   B 1 152 ? 1.783   36.388  16.420  1.00 25.96 ? 153 SER   B CB  1 
ATOM   4090 O OG  . SER   B 1 152 ? 1.873   36.377  17.840  1.00 25.84 ? 153 SER   B OG  1 
ATOM   4091 N N   . ASN   B 1 153 ? 2.542   33.141  17.278  1.00 24.96 ? 154 ASN   B N   1 
ATOM   4092 C CA  . ASN   B 1 153 ? 2.024   32.069  18.125  1.00 27.48 ? 154 ASN   B CA  1 
ATOM   4093 C C   . ASN   B 1 153 ? 1.297   32.594  19.356  1.00 27.97 ? 154 ASN   B C   1 
ATOM   4094 O O   . ASN   B 1 153 ? 0.208   32.079  19.667  1.00 30.04 ? 154 ASN   B O   1 
ATOM   4095 C CB  . ASN   B 1 153 ? 3.157   31.115  18.502  1.00 29.17 ? 154 ASN   B CB  1 
ATOM   4096 C CG  . ASN   B 1 153 ? 3.717   30.403  17.299  1.00 32.66 ? 154 ASN   B CG  1 
ATOM   4097 O OD1 . ASN   B 1 153 ? 2.969   30.029  16.390  1.00 27.52 ? 154 ASN   B OD1 1 
ATOM   4098 N ND2 . ASN   B 1 153 ? 5.031   30.230  17.267  1.00 31.30 ? 154 ASN   B ND2 1 
ATOM   4099 N N   . PRO   B 1 154 ? 1.821   33.571  20.108  1.00 29.65 ? 155 PRO   B N   1 
ATOM   4100 C CA  . PRO   B 1 154 ? 1.048   34.065  21.263  1.00 33.03 ? 155 PRO   B CA  1 
ATOM   4101 C C   . PRO   B 1 154 ? -0.312  34.613  20.873  1.00 28.68 ? 155 PRO   B C   1 
ATOM   4102 O O   . PRO   B 1 154 ? -1.269  34.495  21.650  1.00 31.57 ? 155 PRO   B O   1 
ATOM   4103 C CB  . PRO   B 1 154 ? 1.949   35.158  21.862  1.00 31.08 ? 155 PRO   B CB  1 
ATOM   4104 C CG  . PRO   B 1 154 ? 2.986   35.446  20.839  1.00 31.09 ? 155 PRO   B CG  1 
ATOM   4105 C CD  . PRO   B 1 154 ? 3.155   34.191  20.040  1.00 30.79 ? 155 PRO   B CD  1 
ATOM   4106 N N   . SER   B 1 155 ? -0.419  35.215  19.689  1.00 28.30 ? 156 SER   B N   1 
ATOM   4107 C CA  . SER   B 1 155 ? -1.688  35.773  19.231  1.00 27.39 ? 156 SER   B CA  1 
ATOM   4108 C C   . SER   B 1 155 ? -2.755  34.688  19.105  1.00 27.43 ? 156 SER   B C   1 
ATOM   4109 O O   . SER   B 1 155 ? -3.834  34.779  19.700  1.00 27.37 ? 156 SER   B O   1 
ATOM   4110 C CB  . SER   B 1 155 ? -1.479  36.481  17.892  1.00 24.59 ? 156 SER   B CB  1 
ATOM   4111 O OG  . SER   B 1 155 ? -2.591  37.275  17.534  1.00 24.84 ? 156 SER   B OG  1 
ATOM   4112 N N   . ILE   B 1 156 ? -2.482  33.655  18.313  1.00 26.84 ? 157 ILE   B N   1 
ATOM   4113 C CA  . ILE   B 1 156 ? -3.481  32.601  18.193  1.00 28.29 ? 157 ILE   B CA  1 
ATOM   4114 C C   . ILE   B 1 156 ? -3.505  31.711  19.431  1.00 28.04 ? 157 ILE   B C   1 
ATOM   4115 O O   . ILE   B 1 156 ? -4.495  31.013  19.656  1.00 28.04 ? 157 ILE   B O   1 
ATOM   4116 C CB  . ILE   B 1 156 ? -3.272  31.767  16.918  1.00 27.07 ? 157 ILE   B CB  1 
ATOM   4117 C CG1 . ILE   B 1 156 ? -4.609  31.144  16.490  1.00 26.43 ? 157 ILE   B CG1 1 
ATOM   4118 C CG2 . ILE   B 1 156 ? -2.203  30.704  17.141  1.00 31.33 ? 157 ILE   B CG2 1 
ATOM   4119 C CD1 . ILE   B 1 156 ? -4.553  30.361  15.180  1.00 25.47 ? 157 ILE   B CD1 1 
ATOM   4120 N N   . GLY   B 1 157 ? -2.450  31.719  20.248  1.00 29.27 ? 158 GLY   B N   1 
ATOM   4121 C CA  . GLY   B 1 157 ? -2.508  31.003  21.515  1.00 31.06 ? 158 GLY   B CA  1 
ATOM   4122 C C   . GLY   B 1 157 ? -3.515  31.612  22.471  1.00 32.01 ? 158 GLY   B C   1 
ATOM   4123 O O   . GLY   B 1 157 ? -4.291  30.896  23.114  1.00 33.08 ? 158 GLY   B O   1 
ATOM   4124 N N   . LEU   B 1 158 ? -3.521  32.943  22.579  1.00 31.97 ? 159 LEU   B N   1 
ATOM   4125 C CA  . LEU   B 1 158 ? -4.537  33.614  23.386  1.00 33.78 ? 159 LEU   B CA  1 
ATOM   4126 C C   . LEU   B 1 158 ? -5.925  33.385  22.801  1.00 33.03 ? 159 LEU   B C   1 
ATOM   4127 O O   . LEU   B 1 158 ? -6.890  33.159  23.541  1.00 34.52 ? 159 LEU   B O   1 
ATOM   4128 C CB  . LEU   B 1 158 ? -4.229  35.112  23.501  1.00 32.32 ? 159 LEU   B CB  1 
ATOM   4129 C CG  . LEU   B 1 158 ? -5.242  35.980  24.258  1.00 33.79 ? 159 LEU   B CG  1 
ATOM   4130 C CD1 . LEU   B 1 158 ? -5.557  35.423  25.652  1.00 36.21 ? 159 LEU   B CD1 1 
ATOM   4131 C CD2 . LEU   B 1 158 ? -4.743  37.412  24.377  1.00 33.97 ? 159 LEU   B CD2 1 
ATOM   4132 N N   . PHE   B 1 159 ? -6.040  33.415  21.471  1.00 31.71 ? 160 PHE   B N   1 
ATOM   4133 C CA  . PHE   B 1 159 ? -7.304  33.065  20.835  1.00 28.74 ? 160 PHE   B CA  1 
ATOM   4134 C C   . PHE   B 1 159 ? -7.756  31.677  21.271  1.00 30.31 ? 160 PHE   B C   1 
ATOM   4135 O O   . PHE   B 1 159 ? -8.908  31.482  21.677  1.00 32.02 ? 160 PHE   B O   1 
ATOM   4136 C CB  . PHE   B 1 159 ? -7.162  33.134  19.314  1.00 28.29 ? 160 PHE   B CB  1 
ATOM   4137 C CG  . PHE   B 1 159 ? -8.408  32.742  18.573  1.00 30.43 ? 160 PHE   B CG  1 
ATOM   4138 C CD1 . PHE   B 1 159 ? -9.500  33.601  18.521  1.00 29.07 ? 160 PHE   B CD1 1 
ATOM   4139 C CD2 . PHE   B 1 159 ? -8.487  31.528  17.922  1.00 27.48 ? 160 PHE   B CD2 1 
ATOM   4140 C CE1 . PHE   B 1 159 ? -10.653 33.249  17.841  1.00 27.61 ? 160 PHE   B CE1 1 
ATOM   4141 C CE2 . PHE   B 1 159 ? -9.636  31.167  17.241  1.00 29.25 ? 160 PHE   B CE2 1 
ATOM   4142 C CZ  . PHE   B 1 159 ? -10.715 32.033  17.194  1.00 28.91 ? 160 PHE   B CZ  1 
ATOM   4143 N N   . GLY   B 1 160 ? -6.843  30.703  21.219  1.00 30.66 ? 161 GLY   B N   1 
ATOM   4144 C CA  . GLY   B 1 160 ? -7.205  29.339  21.583  1.00 31.86 ? 161 GLY   B CA  1 
ATOM   4145 C C   . GLY   B 1 160 ? -7.601  29.203  23.040  1.00 35.47 ? 161 GLY   B C   1 
ATOM   4146 O O   . GLY   B 1 160 ? -8.548  28.485  23.371  1.00 34.07 ? 161 GLY   B O   1 
ATOM   4147 N N   . LYS   B 1 161 ? -6.882  29.888  23.932  1.00 35.36 ? 162 LYS   B N   1 
ATOM   4148 C CA  . LYS   B 1 161 ? -7.243  29.842  25.344  1.00 37.96 ? 162 LYS   B CA  1 
ATOM   4149 C C   . LYS   B 1 161 ? -8.650  30.379  25.563  1.00 36.56 ? 162 LYS   B C   1 
ATOM   4150 O O   . LYS   B 1 161 ? -9.419  29.819  26.357  1.00 40.20 ? 162 LYS   B O   1 
ATOM   4151 C CB  . LYS   B 1 161 ? -6.239  30.638  26.177  1.00 38.53 ? 162 LYS   B CB  1 
ATOM   4152 C CG  . LYS   B 1 161 ? -6.494  30.542  27.682  1.00 46.27 ? 162 LYS   B CG  1 
ATOM   4153 C CD  . LYS   B 1 161 ? -5.648  31.536  28.456  1.00 49.70 ? 162 LYS   B CD  1 
ATOM   4154 C CE  . LYS   B 1 161 ? -5.850  31.399  29.961  1.00 54.00 ? 162 LYS   B CE  1 
ATOM   4155 N NZ  . LYS   B 1 161 ? -5.079  30.262  30.529  1.00 49.82 ? 162 LYS   B NZ  1 
ATOM   4156 N N   . VAL   B 1 162 ? -9.005  31.457  24.860  1.00 37.30 ? 163 VAL   B N   1 
ATOM   4157 C CA  . VAL   B 1 162 ? -10.320 32.071  25.017  1.00 38.26 ? 163 VAL   B CA  1 
ATOM   4158 C C   . VAL   B 1 162 ? -11.410 31.145  24.492  1.00 35.63 ? 163 VAL   B C   1 
ATOM   4159 O O   . VAL   B 1 162 ? -12.454 30.969  25.131  1.00 39.78 ? 163 VAL   B O   1 
ATOM   4160 C CB  . VAL   B 1 162 ? -10.365 33.439  24.313  1.00 36.41 ? 163 VAL   B CB  1 
ATOM   4161 C CG1 . VAL   B 1 162 ? -11.805 33.921  24.185  1.00 37.71 ? 163 VAL   B CG1 1 
ATOM   4162 C CG2 . VAL   B 1 162 ? -9.513  34.468  25.056  1.00 37.88 ? 163 VAL   B CG2 1 
ATOM   4163 N N   . VAL   B 1 163 ? -11.192 30.557  23.311  1.00 33.58 ? 164 VAL   B N   1 
ATOM   4164 C CA  . VAL   B 1 163 ? -12.157 29.602  22.767  1.00 33.12 ? 164 VAL   B CA  1 
ATOM   4165 C C   . VAL   B 1 163 ? -12.417 28.495  23.779  1.00 37.52 ? 164 VAL   B C   1 
ATOM   4166 O O   . VAL   B 1 163 ? -13.570 28.124  24.040  1.00 39.75 ? 164 VAL   B O   1 
ATOM   4167 C CB  . VAL   B 1 163 ? -11.661 29.038  21.420  1.00 32.78 ? 164 VAL   B CB  1 
ATOM   4168 C CG1 . VAL   B 1 163 ? -12.614 27.969  20.904  1.00 32.74 ? 164 VAL   B CG1 1 
ATOM   4169 C CG2 . VAL   B 1 163 ? -11.543 30.141  20.396  1.00 32.43 ? 164 VAL   B CG2 1 
ATOM   4170 N N   . ALA   B 1 164 ? -11.347 27.979  24.389  1.00 36.00 ? 165 ALA   B N   1 
ATOM   4171 C CA  . ALA   B 1 164 ? -11.481 26.925  25.390  1.00 37.08 ? 165 ALA   B CA  1 
ATOM   4172 C C   . ALA   B 1 164 ? -12.291 27.397  26.590  1.00 41.71 ? 165 ALA   B C   1 
ATOM   4173 O O   . ALA   B 1 164 ? -13.122 26.648  27.119  1.00 41.41 ? 165 ALA   B O   1 
ATOM   4174 C CB  . ALA   B 1 164 ? -10.097 26.445  25.827  1.00 37.31 ? 165 ALA   B CB  1 
ATOM   4175 N N   . LEU   B 1 165 ? -12.065 28.637  27.035  1.00 40.09 ? 166 LEU   B N   1 
ATOM   4176 C CA  . LEU   B 1 165 ? -12.851 29.183  28.137  1.00 42.34 ? 166 LEU   B CA  1 
ATOM   4177 C C   . LEU   B 1 165 ? -14.327 29.258  27.777  1.00 43.40 ? 166 LEU   B C   1 
ATOM   4178 O O   . LEU   B 1 165 ? -15.189 28.913  28.592  1.00 44.97 ? 166 LEU   B O   1 
ATOM   4179 C CB  . LEU   B 1 165 ? -12.333 30.565  28.524  1.00 42.91 ? 166 LEU   B CB  1 
ATOM   4180 C CG  . LEU   B 1 165 ? -11.082 30.615  29.398  1.00 44.05 ? 166 LEU   B CG  1 
ATOM   4181 C CD1 . LEU   B 1 165 ? -10.620 32.049  29.546  1.00 49.76 ? 166 LEU   B CD1 1 
ATOM   4182 C CD2 . LEU   B 1 165 ? -11.364 29.994  30.761  1.00 46.60 ? 166 LEU   B CD2 1 
ATOM   4183 N N   . SER   B 1 166 ? -14.638 29.703  26.559  1.00 41.98 ? 167 SER   B N   1 
ATOM   4184 C CA  . SER   B 1 166 ? -16.033 29.819  26.153  1.00 44.19 ? 167 SER   B CA  1 
ATOM   4185 C C   . SER   B 1 166 ? -16.743 28.473  26.114  1.00 45.46 ? 167 SER   B C   1 
ATOM   4186 O O   . SER   B 1 166 ? -17.971 28.438  26.240  1.00 45.69 ? 167 SER   B O   1 
ATOM   4187 C CB  . SER   B 1 166 ? -16.134 30.481  24.785  1.00 41.16 ? 167 SER   B CB  1 
ATOM   4188 O OG  . SER   B 1 166 ? -15.709 29.601  23.754  1.00 39.05 ? 167 SER   B OG  1 
ATOM   4189 N N   . MET   B 1 167 ? -16.005 27.375  25.937  1.00 44.03 ? 168 MET   B N   1 
ATOM   4190 C CA  . MET   B 1 167 ? -16.574 26.037  25.843  1.00 47.04 ? 168 MET   B CA  1 
ATOM   4191 C C   . MET   B 1 167 ? -16.463 25.253  27.146  1.00 53.73 ? 168 MET   B C   1 
ATOM   4192 O O   . MET   B 1 167 ? -16.840 24.077  27.176  1.00 53.81 ? 168 MET   B O   1 
ATOM   4193 C CB  . MET   B 1 167 ? -15.904 25.257  24.705  1.00 47.47 ? 168 MET   B CB  1 
ATOM   4194 C CG  . MET   B 1 167 ? -16.194 25.819  23.311  1.00 39.97 ? 168 MET   B CG  1 
ATOM   4195 S SD  . MET   B 1 167 ? -15.177 25.116  21.992  1.00 44.23 ? 168 MET   B SD  1 
ATOM   4196 C CE  . MET   B 1 167 ? -15.801 23.437  21.929  1.00 44.20 ? 168 MET   B CE  1 
ATOM   4197 N N   . ASN   B 1 168 ? -15.938 25.873  28.208  1.00 48.40 ? 169 ASN   B N   1 
ATOM   4198 C CA  . ASN   B 1 168 ? -15.920 25.298  29.557  1.00 49.78 ? 169 ASN   B CA  1 
ATOM   4199 C C   . ASN   B 1 168 ? -15.107 24.007  29.618  1.00 53.51 ? 169 ASN   B C   1 
ATOM   4200 O O   . ASN   B 1 168 ? -15.463 23.063  30.324  1.00 47.75 ? 169 ASN   B O   1 
ATOM   4201 C CB  . ASN   B 1 168 ? -17.341 25.068  30.076  1.00 54.54 ? 169 ASN   B CB  1 
ATOM   4202 C CG  . ASN   B 1 168 ? -18.197 26.314  29.994  1.00 58.06 ? 169 ASN   B CG  1 
ATOM   4203 O OD1 . ASN   B 1 168 ? -19.110 26.398  29.170  1.00 59.63 ? 169 ASN   B OD1 1 
ATOM   4204 N ND2 . ASN   B 1 168 ? -17.908 27.293  30.848  1.00 59.42 ? 169 ASN   B ND2 1 
ATOM   4205 N N   . LYS   B 1 169 ? -14.000 23.971  28.882  1.00 47.02 ? 170 LYS   B N   1 
ATOM   4206 C CA  . LYS   B 1 169 ? -13.103 22.826  28.850  1.00 48.66 ? 170 LYS   B CA  1 
ATOM   4207 C C   . LYS   B 1 169 ? -11.697 23.326  28.559  1.00 47.00 ? 170 LYS   B C   1 
ATOM   4208 O O   . LYS   B 1 169 ? -11.535 24.354  27.890  1.00 44.75 ? 170 LYS   B O   1 
ATOM   4209 C CB  . LYS   B 1 169 ? -13.528 21.798  27.786  1.00 48.79 ? 170 LYS   B CB  1 
ATOM   4210 C CG  . LYS   B 1 169 ? -14.683 20.891  28.203  1.00 54.29 ? 170 LYS   B CG  1 
ATOM   4211 C CD  . LYS   B 1 169 ? -15.291 20.181  27.000  1.00 58.07 ? 170 LYS   B CD  1 
ATOM   4212 C CE  . LYS   B 1 169 ? -16.189 21.114  26.207  1.00 57.29 ? 170 LYS   B CE  1 
ATOM   4213 N NZ  . LYS   B 1 169 ? -15.930 21.011  24.742  1.00 57.68 ? 170 LYS   B NZ  1 
ATOM   4214 N N   . PRO   B 1 170 ? -10.667 22.646  29.064  1.00 44.67 ? 171 PRO   B N   1 
ATOM   4215 C CA  . PRO   B 1 170 ? -9.299  22.960  28.636  1.00 44.93 ? 171 PRO   B CA  1 
ATOM   4216 C C   . PRO   B 1 170 ? -9.128  22.740  27.138  1.00 40.22 ? 171 PRO   B C   1 
ATOM   4217 O O   . PRO   B 1 170 ? -9.844  21.956  26.513  1.00 39.94 ? 171 PRO   B O   1 
ATOM   4218 C CB  . PRO   B 1 170 ? -8.433  21.989  29.450  1.00 43.17 ? 171 PRO   B CB  1 
ATOM   4219 C CG  . PRO   B 1 170 ? -9.391  20.948  29.978  1.00 46.87 ? 171 PRO   B CG  1 
ATOM   4220 C CD  . PRO   B 1 170 ? -10.701 21.642  30.142  1.00 45.26 ? 171 PRO   B CD  1 
ATOM   4221 N N   . PHE   B 1 171 ? -8.156  23.453  26.559  1.00 39.66 ? 172 PHE   B N   1 
ATOM   4222 C CA  . PHE   B 1 171 ? -8.005  23.436  25.106  1.00 38.41 ? 172 PHE   B CA  1 
ATOM   4223 C C   . PHE   B 1 171 ? -7.755  22.027  24.578  1.00 36.51 ? 172 PHE   B C   1 
ATOM   4224 O O   . PHE   B 1 171 ? -8.309  21.644  23.541  1.00 35.25 ? 172 PHE   B O   1 
ATOM   4225 C CB  . PHE   B 1 171 ? -6.878  24.375  24.670  1.00 33.69 ? 172 PHE   B CB  1 
ATOM   4226 C CG  . PHE   B 1 171 ? -6.696  24.433  23.178  1.00 32.63 ? 172 PHE   B CG  1 
ATOM   4227 C CD1 . PHE   B 1 171 ? -7.507  25.244  22.403  1.00 32.80 ? 172 PHE   B CD1 1 
ATOM   4228 C CD2 . PHE   B 1 171 ? -5.741  23.648  22.550  1.00 33.50 ? 172 PHE   B CD2 1 
ATOM   4229 C CE1 . PHE   B 1 171 ? -7.358  25.289  21.020  1.00 31.24 ? 172 PHE   B CE1 1 
ATOM   4230 C CE2 . PHE   B 1 171 ? -5.585  23.690  21.171  1.00 30.02 ? 172 PHE   B CE2 1 
ATOM   4231 C CZ  . PHE   B 1 171 ? -6.395  24.512  20.409  1.00 30.29 ? 172 PHE   B CZ  1 
ATOM   4232 N N   . ASP   B 1 172 ? -6.931  21.239  25.275  1.00 36.51 ? 173 ASP   B N   1 
ATOM   4233 C CA  . ASP   B 1 172 ? -6.634  19.890  24.798  1.00 38.98 ? 173 ASP   B CA  1 
ATOM   4234 C C   . ASP   B 1 172 ? -7.887  19.026  24.733  1.00 39.52 ? 173 ASP   B C   1 
ATOM   4235 O O   . ASP   B 1 172 ? -7.990  18.147  23.869  1.00 35.92 ? 173 ASP   B O   1 
ATOM   4236 C CB  . ASP   B 1 172 ? -5.574  19.224  25.682  1.00 40.15 ? 173 ASP   B CB  1 
ATOM   4237 C CG  . ASP   B 1 172 ? -6.072  18.936  27.089  1.00 41.01 ? 173 ASP   B CG  1 
ATOM   4238 O OD1 . ASP   B 1 172 ? -6.562  19.874  27.756  1.00 43.14 ? 173 ASP   B OD1 1 
ATOM   4239 O OD2 . ASP   B 1 172 ? -5.974  17.766  27.532  1.00 48.90 ? 173 ASP   B OD2 1 
ATOM   4240 N N   . GLN   B 1 173 ? -8.854  19.262  25.623  1.00 40.26 ? 174 GLN   B N   1 
ATOM   4241 C CA  . GLN   B 1 173 ? -10.090 18.491  25.569  1.00 42.00 ? 174 GLN   B CA  1 
ATOM   4242 C C   . GLN   B 1 173 ? -11.073 19.055  24.548  1.00 37.22 ? 174 GLN   B C   1 
ATOM   4243 O O   . GLN   B 1 173 ? -11.885 18.296  24.000  1.00 36.81 ? 174 GLN   B O   1 
ATOM   4244 C CB  . GLN   B 1 173 ? -10.732 18.415  26.956  1.00 42.57 ? 174 GLN   B CB  1 
ATOM   4245 C CG  . GLN   B 1 173 ? -9.906  17.631  27.962  1.00 44.23 ? 174 GLN   B CG  1 
ATOM   4246 C CD  . GLN   B 1 173 ? -10.724 17.177  29.154  1.00 57.12 ? 174 GLN   B CD  1 
ATOM   4247 O OE1 . GLN   B 1 173 ? -11.308 17.994  29.871  1.00 55.22 ? 174 GLN   B OE1 1 
ATOM   4248 N NE2 . GLN   B 1 173 ? -10.781 15.866  29.368  1.00 64.20 ? 174 GLN   B NE2 1 
ATOM   4249 N N   . VAL   B 1 174 ? -11.013 20.361  24.264  1.00 35.68 ? 175 VAL   B N   1 
ATOM   4250 C CA  . VAL   B 1 174 ? -11.789 20.903  23.151  1.00 33.69 ? 175 VAL   B CA  1 
ATOM   4251 C C   . VAL   B 1 174 ? -11.452 20.146  21.873  1.00 32.36 ? 175 VAL   B C   1 
ATOM   4252 O O   . VAL   B 1 174 ? -12.339 19.702  21.136  1.00 33.31 ? 175 VAL   B O   1 
ATOM   4253 C CB  . VAL   B 1 174 ? -11.539 22.415  22.993  1.00 38.20 ? 175 VAL   B CB  1 
ATOM   4254 C CG1 . VAL   B 1 174 ? -12.188 22.921  21.724  1.00 30.87 ? 175 VAL   B CG1 1 
ATOM   4255 C CG2 . VAL   B 1 174 ? -12.080 23.167  24.199  1.00 37.42 ? 175 VAL   B CG2 1 
ATOM   4256 N N   . LEU   B 1 175 ? -10.160 19.945  21.617  1.00 33.61 ? 176 LEU   B N   1 
ATOM   4257 C CA  . LEU   B 1 175 ? -9.766  19.221  20.412  1.00 31.48 ? 176 LEU   B CA  1 
ATOM   4258 C C   . LEU   B 1 175 ? -10.032 17.726  20.541  1.00 32.06 ? 176 LEU   B C   1 
ATOM   4259 O O   . LEU   B 1 175 ? -10.702 17.137  19.688  1.00 31.09 ? 176 LEU   B O   1 
ATOM   4260 C CB  . LEU   B 1 175 ? -8.292  19.468  20.097  1.00 28.70 ? 176 LEU   B CB  1 
ATOM   4261 C CG  . LEU   B 1 175 ? -7.922  20.861  19.593  1.00 27.72 ? 176 LEU   B CG  1 
ATOM   4262 C CD1 . LEU   B 1 175 ? -6.508  20.840  19.046  1.00 29.79 ? 176 LEU   B CD1 1 
ATOM   4263 C CD2 . LEU   B 1 175 ? -8.907  21.311  18.533  1.00 26.78 ? 176 LEU   B CD2 1 
ATOM   4264 N N   . GLU   B 1 176 ? -9.524  17.104  21.613  1.00 32.27 ? 177 GLU   B N   1 
ATOM   4265 C CA  . GLU   B 1 176 ? -9.519  15.645  21.719  1.00 34.41 ? 177 GLU   B CA  1 
ATOM   4266 C C   . GLU   B 1 176 ? -10.903 15.077  22.005  1.00 36.00 ? 177 GLU   B C   1 
ATOM   4267 O O   . GLU   B 1 176 ? -11.174 13.914  21.666  1.00 36.01 ? 177 GLU   B O   1 
ATOM   4268 C CB  . GLU   B 1 176 ? -8.533  15.200  22.805  1.00 38.14 ? 177 GLU   B CB  1 
ATOM   4269 C CG  . GLU   B 1 176 ? -7.070  15.331  22.401  1.00 35.66 ? 177 GLU   B CG  1 
ATOM   4270 C CD  . GLU   B 1 176 ? -6.100  14.815  23.448  1.00 39.07 ? 177 GLU   B CD  1 
ATOM   4271 O OE1 . GLU   B 1 176 ? -4.879  14.836  23.186  1.00 36.47 ? 177 GLU   B OE1 1 
ATOM   4272 O OE2 . GLU   B 1 176 ? -6.548  14.373  24.532  1.00 40.16 ? 177 GLU   B OE2 1 
ATOM   4273 N N   . LYS   B 1 177 ? -11.788 15.851  22.640  1.00 35.20 ? 178 LYS   B N   1 
ATOM   4274 C CA  . LYS   B 1 177 ? -13.114 15.335  22.951  1.00 37.34 ? 178 LYS   B CA  1 
ATOM   4275 C C   . LYS   B 1 177 ? -14.222 15.902  22.072  1.00 38.55 ? 178 LYS   B C   1 
ATOM   4276 O O   . LYS   B 1 177 ? -15.282 15.276  21.973  1.00 38.80 ? 178 LYS   B O   1 
ATOM   4277 C CB  . LYS   B 1 177 ? -13.476 15.590  24.424  1.00 39.53 ? 178 LYS   B CB  1 
ATOM   4278 C CG  . LYS   B 1 177 ? -12.718 14.734  25.449  1.00 44.89 ? 178 LYS   B CG  1 
ATOM   4279 C CD  . LYS   B 1 177 ? -12.047 13.484  24.847  1.00 48.53 ? 178 LYS   B CD  1 
ATOM   4280 C CE  . LYS   B 1 177 ? -13.036 12.399  24.420  1.00 53.69 ? 178 LYS   B CE  1 
ATOM   4281 N NZ  . LYS   B 1 177 ? -12.434 11.585  23.308  1.00 53.38 ? 178 LYS   B NZ  1 
ATOM   4282 N N   . THR   B 1 178 ? -14.013 17.046  21.417  1.00 35.72 ? 179 THR   B N   1 
ATOM   4283 C CA  . THR   B 1 178 ? -15.085 17.666  20.645  1.00 33.96 ? 179 THR   B CA  1 
ATOM   4284 C C   . THR   B 1 178 ? -14.753 17.806  19.168  1.00 33.48 ? 179 THR   B C   1 
ATOM   4285 O O   . THR   B 1 178 ? -15.507 17.309  18.324  1.00 34.48 ? 179 THR   B O   1 
ATOM   4286 C CB  . THR   B 1 178 ? -15.430 19.036  21.251  1.00 41.04 ? 179 THR   B CB  1 
ATOM   4287 O OG1 . THR   B 1 178 ? -15.890 18.851  22.598  1.00 42.43 ? 179 THR   B OG1 1 
ATOM   4288 C CG2 . THR   B 1 178 ? -16.514 19.744  20.441  1.00 39.23 ? 179 THR   B CG2 1 
ATOM   4289 N N   . ILE   B 1 179 ? -13.634 18.449  18.830  1.00 33.86 ? 180 ILE   B N   1 
ATOM   4290 C CA  . ILE   B 1 179 ? -13.354 18.782  17.436  1.00 32.27 ? 180 ILE   B CA  1 
ATOM   4291 C C   . ILE   B 1 179 ? -12.813 17.580  16.666  1.00 31.60 ? 180 ILE   B C   1 
ATOM   4292 O O   . ILE   B 1 179 ? -13.262 17.298  15.548  1.00 30.75 ? 180 ILE   B O   1 
ATOM   4293 C CB  . ILE   B 1 179 ? -12.396 19.986  17.370  1.00 28.85 ? 180 ILE   B CB  1 
ATOM   4294 C CG1 . ILE   B 1 179 ? -13.044 21.195  18.049  1.00 30.11 ? 180 ILE   B CG1 1 
ATOM   4295 C CG2 . ILE   B 1 179 ? -11.994 20.302  15.916  1.00 28.76 ? 180 ILE   B CG2 1 
ATOM   4296 C CD1 . ILE   B 1 179 ? -14.321 21.664  17.385  1.00 30.07 ? 180 ILE   B CD1 1 
ATOM   4297 N N   . PHE   B 1 180 ? -11.822 16.869  17.218  1.00 28.43 ? 181 PHE   B N   1 
ATOM   4298 C CA  . PHE   B 1 180 ? -11.293 15.707  16.502  1.00 28.89 ? 181 PHE   B CA  1 
ATOM   4299 C C   . PHE   B 1 180 ? -12.374 14.675  16.224  1.00 32.85 ? 181 PHE   B C   1 
ATOM   4300 O O   . PHE   B 1 180 ? -12.460 14.195  15.080  1.00 30.95 ? 181 PHE   B O   1 
ATOM   4301 C CB  . PHE   B 1 180 ? -10.123 15.075  17.266  1.00 30.55 ? 181 PHE   B CB  1 
ATOM   4302 C CG  . PHE   B 1 180 ? -8.885  15.924  17.316  1.00 27.00 ? 181 PHE   B CG  1 
ATOM   4303 C CD1 . PHE   B 1 180 ? -8.716  17.003  16.450  1.00 27.81 ? 181 PHE   B CD1 1 
ATOM   4304 C CD2 . PHE   B 1 180 ? -7.883  15.639  18.230  1.00 30.04 ? 181 PHE   B CD2 1 
ATOM   4305 C CE1 . PHE   B 1 180 ? -7.567  17.785  16.505  1.00 28.63 ? 181 PHE   B CE1 1 
ATOM   4306 C CE2 . PHE   B 1 180 ? -6.734  16.409  18.290  1.00 28.75 ? 181 PHE   B CE2 1 
ATOM   4307 C CZ  . PHE   B 1 180 ? -6.576  17.489  17.420  1.00 27.51 ? 181 PHE   B CZ  1 
ATOM   4308 N N   . PRO   B 1 181 ? -13.228 14.299  17.182  1.00 33.69 ? 182 PRO   B N   1 
ATOM   4309 C CA  . PRO   B 1 181 ? -14.256 13.294  16.855  1.00 32.84 ? 182 PRO   B CA  1 
ATOM   4310 C C   . PRO   B 1 181 ? -15.289 13.805  15.867  1.00 36.92 ? 182 PRO   B C   1 
ATOM   4311 O O   . PRO   B 1 181 ? -15.753 13.037  15.015  1.00 37.96 ? 182 PRO   B O   1 
ATOM   4312 C CB  . PRO   B 1 181 ? -14.880 12.968  18.219  1.00 37.47 ? 182 PRO   B CB  1 
ATOM   4313 C CG  . PRO   B 1 181 ? -13.891 13.451  19.237  1.00 35.33 ? 182 PRO   B CG  1 
ATOM   4314 C CD  . PRO   B 1 181 ? -13.250 14.653  18.611  1.00 32.62 ? 182 PRO   B CD  1 
ATOM   4315 N N   . ALA   B 1 182 ? -15.654 15.089  15.949  1.00 36.84 ? 183 ALA   B N   1 
ATOM   4316 C CA  . ALA   B 1 182 ? -16.563 15.660  14.963  1.00 31.09 ? 183 ALA   B CA  1 
ATOM   4317 C C   . ALA   B 1 182 ? -16.001 15.545  13.553  1.00 34.66 ? 183 ALA   B C   1 
ATOM   4318 O O   . ALA   B 1 182 ? -16.762 15.404  12.590  1.00 35.84 ? 183 ALA   B O   1 
ATOM   4319 C CB  . ALA   B 1 182 ? -16.865 17.116  15.308  1.00 36.90 ? 183 ALA   B CB  1 
ATOM   4320 N N   . LEU   B 1 183 ? -14.679 15.591  13.408  1.00 30.76 ? 184 LEU   B N   1 
ATOM   4321 C CA  . LEU   B 1 183 ? -14.038 15.506  12.105  1.00 30.96 ? 184 LEU   B CA  1 
ATOM   4322 C C   . LEU   B 1 183 ? -13.745 14.072  11.687  1.00 33.47 ? 184 LEU   B C   1 
ATOM   4323 O O   . LEU   B 1 183 ? -13.193 13.859  10.602  1.00 33.24 ? 184 LEU   B O   1 
ATOM   4324 C CB  . LEU   B 1 183 ? -12.739 16.317  12.102  1.00 30.81 ? 184 LEU   B CB  1 
ATOM   4325 C CG  . LEU   B 1 183 ? -12.868 17.839  12.183  1.00 29.60 ? 184 LEU   B CG  1 
ATOM   4326 C CD1 . LEU   B 1 183 ? -11.517 18.461  12.461  1.00 28.42 ? 184 LEU   B CD1 1 
ATOM   4327 C CD2 . LEU   B 1 183 ? -13.446 18.406  10.894  1.00 30.37 ? 184 LEU   B CD2 1 
ATOM   4328 N N   . GLY   B 1 184 ? -14.084 13.097  12.525  1.00 32.64 ? 185 GLY   B N   1 
ATOM   4329 C CA  . GLY   B 1 184 ? -13.833 11.706  12.215  1.00 33.26 ? 185 GLY   B CA  1 
ATOM   4330 C C   . GLY   B 1 184 ? -12.403 11.266  12.403  1.00 34.55 ? 185 GLY   B C   1 
ATOM   4331 O O   . GLY   B 1 184 ? -11.996 10.262  11.812  1.00 36.00 ? 185 GLY   B O   1 
ATOM   4332 N N   . LEU   B 1 185 ? -11.627 11.976  13.215  1.00 30.58 ? 186 LEU   B N   1 
ATOM   4333 C CA  . LEU   B 1 185 ? -10.230 11.630  13.433  1.00 29.58 ? 186 LEU   B CA  1 
ATOM   4334 C C   . LEU   B 1 185 ? -10.103 10.624  14.571  1.00 34.60 ? 186 LEU   B C   1 
ATOM   4335 O O   . LEU   B 1 185 ? -10.730 10.776  15.624  1.00 39.10 ? 186 LEU   B O   1 
ATOM   4336 C CB  . LEU   B 1 185 ? -9.406  12.885  13.733  1.00 29.98 ? 186 LEU   B CB  1 
ATOM   4337 C CG  . LEU   B 1 185 ? -9.734  14.083  12.834  1.00 30.69 ? 186 LEU   B CG  1 
ATOM   4338 C CD1 . LEU   B 1 185 ? -8.815  15.276  13.147  1.00 27.76 ? 186 LEU   B CD1 1 
ATOM   4339 C CD2 . LEU   B 1 185 ? -9.683  13.728  11.351  1.00 31.52 ? 186 LEU   B CD2 1 
ATOM   4340 N N   . LYS   B 1 186 ? -9.278  9.596   14.352  1.00 32.22 ? 187 LYS   B N   1 
ATOM   4341 C CA  . LYS   B 1 186 ? -9.147  8.502   15.309  1.00 33.31 ? 187 LYS   B CA  1 
ATOM   4342 C C   . LYS   B 1 186 ? -7.844  8.516   16.090  1.00 30.87 ? 187 LYS   B C   1 
ATOM   4343 O O   . LYS   B 1 186 ? -7.785  7.906   17.166  1.00 32.31 ? 187 LYS   B O   1 
ATOM   4344 C CB  . LYS   B 1 186 ? -9.251  7.142   14.601  1.00 38.30 ? 187 LYS   B CB  1 
ATOM   4345 C CG  . LYS   B 1 186 ? -10.286 7.067   13.493  1.00 43.92 ? 187 LYS   B CG  1 
ATOM   4346 C CD  . LYS   B 1 186 ? -11.703 6.980   14.024  1.00 41.07 ? 187 LYS   B CD  1 
ATOM   4347 C CE  . LYS   B 1 186 ? -12.545 6.086   13.122  1.00 47.14 ? 187 LYS   B CE  1 
ATOM   4348 N NZ  . LYS   B 1 186 ? -12.069 6.134   11.703  1.00 57.36 ? 187 LYS   B NZ  1 
ATOM   4349 N N   . HIS   B 1 187 ? -6.800  9.161   15.572  1.00 31.56 ? 188 HIS   B N   1 
ATOM   4350 C CA  . HIS   B 1 187 ? -5.478  9.116   16.186  1.00 28.11 ? 188 HIS   B CA  1 
ATOM   4351 C C   . HIS   B 1 187 ? -4.799  10.467  16.057  1.00 28.10 ? 188 HIS   B C   1 
ATOM   4352 O O   . HIS   B 1 187 ? -3.631  10.574  15.688  1.00 27.40 ? 188 HIS   B O   1 
ATOM   4353 C CB  . HIS   B 1 187 ? -4.637  8.002   15.574  1.00 28.89 ? 188 HIS   B CB  1 
ATOM   4354 C CG  . HIS   B 1 187 ? -5.196  6.641   15.832  1.00 30.71 ? 188 HIS   B CG  1 
ATOM   4355 N ND1 . HIS   B 1 187 ? -5.953  5.959   14.904  1.00 35.40 ? 188 HIS   B ND1 1 
ATOM   4356 C CD2 . HIS   B 1 187 ? -5.159  5.860   16.937  1.00 34.41 ? 188 HIS   B CD2 1 
ATOM   4357 C CE1 . HIS   B 1 187 ? -6.331  4.800   15.414  1.00 34.30 ? 188 HIS   B CE1 1 
ATOM   4358 N NE2 . HIS   B 1 187 ? -5.862  4.715   16.647  1.00 35.32 ? 188 HIS   B NE2 1 
ATOM   4359 N N   . SER   B 1 188 ? -5.546  11.519  16.366  1.00 29.98 ? 189 SER   B N   1 
ATOM   4360 C CA  . SER   B 1 188 ? -5.019  12.870  16.441  1.00 27.54 ? 189 SER   B CA  1 
ATOM   4361 C C   . SER   B 1 188 ? -5.069  13.325  17.891  1.00 31.08 ? 189 SER   B C   1 
ATOM   4362 O O   . SER   B 1 188 ? -6.043  13.054  18.604  1.00 34.36 ? 189 SER   B O   1 
ATOM   4363 C CB  . SER   B 1 188 ? -5.813  13.806  15.535  1.00 28.01 ? 189 SER   B CB  1 
ATOM   4364 O OG  . SER   B 1 188 ? -5.698  13.355  14.194  1.00 25.32 ? 189 SER   B OG  1 
ATOM   4365 N N   . TYR   B 1 189 ? -3.998  13.973  18.340  1.00 29.43 ? 190 TYR   B N   1 
ATOM   4366 C CA  . TYR   B 1 189 ? -3.801  14.203  19.761  1.00 31.94 ? 190 TYR   B CA  1 
ATOM   4367 C C   . TYR   B 1 189 ? -3.166  15.559  20.002  1.00 31.43 ? 190 TYR   B C   1 
ATOM   4368 O O   . TYR   B 1 189 ? -2.435  16.085  19.157  1.00 31.55 ? 190 TYR   B O   1 
ATOM   4369 C CB  . TYR   B 1 189 ? -2.890  13.150  20.400  1.00 32.47 ? 190 TYR   B CB  1 
ATOM   4370 C CG  . TYR   B 1 189 ? -3.287  11.727  20.129  1.00 31.87 ? 190 TYR   B CG  1 
ATOM   4371 C CD1 . TYR   B 1 189 ? -4.248  11.099  20.901  1.00 33.59 ? 190 TYR   B CD1 1 
ATOM   4372 C CD2 . TYR   B 1 189 ? -2.689  11.006  19.103  1.00 34.08 ? 190 TYR   B CD2 1 
ATOM   4373 C CE1 . TYR   B 1 189 ? -4.611  9.787   20.660  1.00 35.04 ? 190 TYR   B CE1 1 
ATOM   4374 C CE2 . TYR   B 1 189 ? -3.045  9.696   18.847  1.00 30.45 ? 190 TYR   B CE2 1 
ATOM   4375 C CZ  . TYR   B 1 189 ? -4.007  9.090   19.630  1.00 35.62 ? 190 TYR   B CZ  1 
ATOM   4376 O OH  . TYR   B 1 189 ? -4.369  7.782   19.388  1.00 34.90 ? 190 TYR   B OH  1 
ATOM   4377 N N   . VAL   B 1 190 ? -3.463  16.119  21.168  1.00 32.70 ? 191 VAL   B N   1 
ATOM   4378 C CA  . VAL   B 1 190 ? -2.597  17.137  21.746  1.00 33.08 ? 191 VAL   B CA  1 
ATOM   4379 C C   . VAL   B 1 190 ? -1.554  16.491  22.649  1.00 35.17 ? 191 VAL   B C   1 
ATOM   4380 O O   . VAL   B 1 190 ? -0.388  16.895  22.653  1.00 36.79 ? 191 VAL   B O   1 
ATOM   4381 C CB  . VAL   B 1 190 ? -3.434  18.196  22.493  1.00 36.39 ? 191 VAL   B CB  1 
ATOM   4382 C CG1 . VAL   B 1 190 ? -2.530  19.183  23.207  1.00 32.44 ? 191 VAL   B CG1 1 
ATOM   4383 C CG2 . VAL   B 1 190 ? -4.346  18.932  21.512  1.00 31.15 ? 191 VAL   B CG2 1 
ATOM   4384 N N   . ASN   B 1 191 ? -1.948  15.466  23.400  1.00 35.45 ? 192 ASN   B N   1 
ATOM   4385 C CA  . ASN   B 1 191 ? -1.025  14.662  24.194  1.00 35.79 ? 192 ASN   B CA  1 
ATOM   4386 C C   . ASN   B 1 191 ? -1.147  13.214  23.740  1.00 34.07 ? 192 ASN   B C   1 
ATOM   4387 O O   . ASN   B 1 191 ? -2.189  12.578  23.939  1.00 38.48 ? 192 ASN   B O   1 
ATOM   4388 C CB  . ASN   B 1 191 ? -1.314  14.808  25.685  1.00 37.36 ? 192 ASN   B CB  1 
ATOM   4389 C CG  . ASN   B 1 191 ? -1.285  16.253  26.133  1.00 38.73 ? 192 ASN   B CG  1 
ATOM   4390 O OD1 . ASN   B 1 191 ? -0.223  16.873  26.199  1.00 44.32 ? 192 ASN   B OD1 1 
ATOM   4391 N ND2 . ASN   B 1 191 ? -2.456  16.805  26.426  1.00 42.89 ? 192 ASN   B ND2 1 
ATOM   4392 N N   . VAL   B 1 192 ? -0.089  12.700  23.121  1.00 36.64 ? 193 VAL   B N   1 
ATOM   4393 C CA  . VAL   B 1 192 ? -0.067  11.324  22.630  1.00 35.65 ? 193 VAL   B CA  1 
ATOM   4394 C C   . VAL   B 1 192 ? -0.015  10.373  23.820  1.00 40.33 ? 193 VAL   B C   1 
ATOM   4395 O O   . VAL   B 1 192 ? 0.894   10.480  24.656  1.00 38.93 ? 193 VAL   B O   1 
ATOM   4396 C CB  . VAL   B 1 192 ? 1.119   11.098  21.682  1.00 38.70 ? 193 VAL   B CB  1 
ATOM   4397 C CG1 . VAL   B 1 192 ? 1.263   9.629   21.352  1.00 37.67 ? 193 VAL   B CG1 1 
ATOM   4398 C CG2 . VAL   B 1 192 ? 0.938   11.929  20.411  1.00 32.23 ? 193 VAL   B CG2 1 
ATOM   4399 N N   . PRO   B 1 193 ? -0.958  9.443   23.943  1.00 41.62 ? 194 PRO   B N   1 
ATOM   4400 C CA  . PRO   B 1 193 ? -0.943  8.524   25.087  1.00 40.59 ? 194 PRO   B CA  1 
ATOM   4401 C C   . PRO   B 1 193 ? 0.147   7.467   24.953  1.00 42.80 ? 194 PRO   B C   1 
ATOM   4402 O O   . PRO   B 1 193 ? 0.650   7.175   23.866  1.00 42.63 ? 194 PRO   B O   1 
ATOM   4403 C CB  . PRO   B 1 193 ? -2.340  7.892   25.055  1.00 45.05 ? 194 PRO   B CB  1 
ATOM   4404 C CG  . PRO   B 1 193 ? -2.769  8.001   23.622  1.00 37.89 ? 194 PRO   B CG  1 
ATOM   4405 C CD  . PRO   B 1 193 ? -2.147  9.262   23.089  1.00 37.80 ? 194 PRO   B CD  1 
ATOM   4406 N N   . LYS   B 1 194 ? 0.509   6.881   26.100  1.00 43.90 ? 195 LYS   B N   1 
ATOM   4407 C CA  . LYS   B 1 194 ? 1.600   5.910   26.120  1.00 46.14 ? 195 LYS   B CA  1 
ATOM   4408 C C   . LYS   B 1 194 ? 1.296   4.696   25.251  1.00 47.70 ? 195 LYS   B C   1 
ATOM   4409 O O   . LYS   B 1 194 ? 2.217   4.085   24.695  1.00 48.97 ? 195 LYS   B O   1 
ATOM   4410 C CB  . LYS   B 1 194 ? 1.893   5.481   27.559  1.00 47.23 ? 195 LYS   B CB  1 
ATOM   4411 C CG  . LYS   B 1 194 ? 2.481   6.607   28.397  1.00 57.60 ? 195 LYS   B CG  1 
ATOM   4412 C CD  . LYS   B 1 194 ? 3.791   7.138   27.790  1.00 59.92 ? 195 LYS   B CD  1 
ATOM   4413 C CE  . LYS   B 1 194 ? 4.883   6.062   27.720  1.00 64.24 ? 195 LYS   B CE  1 
ATOM   4414 N NZ  . LYS   B 1 194 ? 6.247   6.679   27.658  1.00 67.11 ? 195 LYS   B NZ  1 
ATOM   4415 N N   . THR   B 1 195 ? 0.015   4.347   25.096  1.00 44.84 ? 196 THR   B N   1 
ATOM   4416 C CA  . THR   B 1 195 ? -0.358  3.228   24.237  1.00 44.74 ? 196 THR   B CA  1 
ATOM   4417 C C   . THR   B 1 195 ? -0.043  3.481   22.767  1.00 45.14 ? 196 THR   B C   1 
ATOM   4418 O O   . THR   B 1 195 ? -0.184  2.564   21.952  1.00 41.56 ? 196 THR   B O   1 
ATOM   4419 C CB  . THR   B 1 195 ? -1.846  2.921   24.409  1.00 47.51 ? 196 THR   B CB  1 
ATOM   4420 O OG1 . THR   B 1 195 ? -2.620  3.982   23.840  1.00 47.01 ? 196 THR   B OG1 1 
ATOM   4421 C CG2 . THR   B 1 195 ? -2.194  2.800   25.885  1.00 50.30 ? 196 THR   B CG2 1 
ATOM   4422 N N   . GLN   B 1 196 ? 0.380   4.693   22.412  1.00 42.63 ? 197 GLN   B N   1 
ATOM   4423 C CA  . GLN   B 1 196 ? 0.715   5.050   21.041  1.00 44.75 ? 197 GLN   B CA  1 
ATOM   4424 C C   . GLN   B 1 196 ? 2.210   5.256   20.834  1.00 44.55 ? 197 GLN   B C   1 
ATOM   4425 O O   . GLN   B 1 196 ? 2.620   5.675   19.750  1.00 40.58 ? 197 GLN   B O   1 
ATOM   4426 C CB  . GLN   B 1 196 ? -0.038  6.320   20.632  1.00 38.08 ? 197 GLN   B CB  1 
ATOM   4427 C CG  . GLN   B 1 196 ? -1.500  6.112   20.309  1.00 35.63 ? 197 GLN   B CG  1 
ATOM   4428 C CD  . GLN   B 1 196 ? -1.698  5.169   19.141  1.00 39.42 ? 197 GLN   B CD  1 
ATOM   4429 O OE1 . GLN   B 1 196 ? -1.028  5.285   18.114  1.00 37.31 ? 197 GLN   B OE1 1 
ATOM   4430 N NE2 . GLN   B 1 196 ? -2.615  4.221   19.294  1.00 39.98 ? 197 GLN   B NE2 1 
ATOM   4431 N N   . MET   B 1 197 ? 3.039   4.966   21.841  1.00 51.77 ? 198 MET   B N   1 
ATOM   4432 C CA  . MET   B 1 197 ? 4.433   5.396   21.776  1.00 54.03 ? 198 MET   B CA  1 
ATOM   4433 C C   . MET   B 1 197 ? 5.260   4.588   20.780  1.00 48.73 ? 198 MET   B C   1 
ATOM   4434 O O   . MET   B 1 197 ? 6.290   5.085   20.310  1.00 50.42 ? 198 MET   B O   1 
ATOM   4435 C CB  . MET   B 1 197 ? 5.065   5.358   23.172  1.00 55.85 ? 198 MET   B CB  1 
ATOM   4436 C CG  . MET   B 1 197 ? 4.620   6.514   24.088  1.00 60.84 ? 198 MET   B CG  1 
ATOM   4437 S SD  . MET   B 1 197 ? 4.894   8.173   23.397  1.00 61.25 ? 198 MET   B SD  1 
ATOM   4438 C CE  . MET   B 1 197 ? 4.080   9.203   24.620  1.00 55.86 ? 198 MET   B CE  1 
ATOM   4439 N N   . GLN   B 1 198 ? 4.826   3.384   20.407  1.00 39.73 ? 199 GLN   B N   1 
ATOM   4440 C CA  . GLN   B 1 198 ? 5.501   2.704   19.304  1.00 40.91 ? 199 GLN   B CA  1 
ATOM   4441 C C   . GLN   B 1 198 ? 5.262   3.392   17.962  1.00 40.28 ? 199 GLN   B C   1 
ATOM   4442 O O   . GLN   B 1 198 ? 5.991   3.118   17.001  1.00 37.06 ? 199 GLN   B O   1 
ATOM   4443 C CB  . GLN   B 1 198 ? 5.063   1.239   19.217  1.00 43.28 ? 199 GLN   B CB  1 
ATOM   4444 C CG  . GLN   B 1 198 ? 3.659   1.016   18.663  1.00 45.70 ? 199 GLN   B CG  1 
ATOM   4445 C CD  . GLN   B 1 198 ? 2.559   1.107   19.723  1.00 51.82 ? 199 GLN   B CD  1 
ATOM   4446 O OE1 . GLN   B 1 198 ? 2.698   1.800   20.739  1.00 48.32 ? 199 GLN   B OE1 1 
ATOM   4447 N NE2 . GLN   B 1 198 ? 1.459   0.392   19.488  1.00 53.24 ? 199 GLN   B NE2 1 
ATOM   4448 N N   . ASN   B 1 199 ? 4.276   4.281   17.873  1.00 37.71 ? 200 ASN   B N   1 
ATOM   4449 C CA  . ASN   B 1 199 ? 3.943   4.958   16.628  1.00 33.53 ? 200 ASN   B CA  1 
ATOM   4450 C C   . ASN   B 1 199 ? 4.491   6.376   16.562  1.00 34.34 ? 200 ASN   B C   1 
ATOM   4451 O O   . ASN   B 1 199 ? 4.345   7.032   15.525  1.00 29.91 ? 200 ASN   B O   1 
ATOM   4452 C CB  . ASN   B 1 199 ? 2.421   4.989   16.435  1.00 31.55 ? 200 ASN   B CB  1 
ATOM   4453 C CG  . ASN   B 1 199 ? 1.828   3.597   16.252  1.00 37.14 ? 200 ASN   B CG  1 
ATOM   4454 O OD1 . ASN   B 1 199 ? 2.411   2.743   15.581  1.00 33.70 ? 200 ASN   B OD1 1 
ATOM   4455 N ND2 . ASN   B 1 199 ? 0.667   3.361   16.858  1.00 36.54 ? 200 ASN   B ND2 1 
ATOM   4456 N N   . TYR   B 1 200 ? 5.133   6.851   17.629  1.00 37.53 ? 201 TYR   B N   1 
ATOM   4457 C CA  . TYR   B 1 200 ? 5.471   8.266   17.780  1.00 39.21 ? 201 TYR   B CA  1 
ATOM   4458 C C   . TYR   B 1 200 ? 6.910   8.386   18.264  1.00 47.18 ? 201 TYR   B C   1 
ATOM   4459 O O   . TYR   B 1 200 ? 7.205   8.050   19.414  1.00 50.74 ? 201 TYR   B O   1 
ATOM   4460 C CB  . TYR   B 1 200 ? 4.505   8.939   18.756  1.00 36.61 ? 201 TYR   B CB  1 
ATOM   4461 C CG  . TYR   B 1 200 ? 4.793   10.400  19.029  1.00 42.08 ? 201 TYR   B CG  1 
ATOM   4462 C CD1 . TYR   B 1 200 ? 5.193   11.255  18.008  1.00 40.53 ? 201 TYR   B CD1 1 
ATOM   4463 C CD2 . TYR   B 1 200 ? 4.638   10.926  20.305  1.00 40.39 ? 201 TYR   B CD2 1 
ATOM   4464 C CE1 . TYR   B 1 200 ? 5.448   12.589  18.259  1.00 40.48 ? 201 TYR   B CE1 1 
ATOM   4465 C CE2 . TYR   B 1 200 ? 4.886   12.260  20.563  1.00 39.24 ? 201 TYR   B CE2 1 
ATOM   4466 C CZ  . TYR   B 1 200 ? 5.293   13.083  19.537  1.00 38.41 ? 201 TYR   B CZ  1 
ATOM   4467 O OH  . TYR   B 1 200 ? 5.542   14.410  19.790  1.00 36.92 ? 201 TYR   B OH  1 
ATOM   4468 N N   . ALA   B 1 201 ? 7.795   8.869   17.392  1.00 59.17 ? 202 ALA   B N   1 
ATOM   4469 C CA  . ALA   B 1 201 ? 9.207   9.087   17.724  1.00 68.61 ? 202 ALA   B CA  1 
ATOM   4470 C C   . ALA   B 1 201 ? 9.399   9.844   19.044  1.00 65.00 ? 202 ALA   B C   1 
ATOM   4471 O O   . ALA   B 1 201 ? 9.507   11.073  19.066  1.00 64.28 ? 202 ALA   B O   1 
ATOM   4472 C CB  . ALA   B 1 201 ? 9.902   9.835   16.582  1.00 66.94 ? 202 ALA   B CB  1 
ATOM   4473 N N   . GLY   B 1 216 ? 6.752   25.210  24.753  1.00 67.54 ? 217 GLY   B N   1 
ATOM   4474 C CA  . GLY   B 1 216 ? 6.574   26.569  25.232  1.00 62.41 ? 217 GLY   B CA  1 
ATOM   4475 C C   . GLY   B 1 216 ? 5.222   26.827  25.873  1.00 58.78 ? 217 GLY   B C   1 
ATOM   4476 O O   . GLY   B 1 216 ? 4.348   25.956  25.879  1.00 57.36 ? 217 GLY   B O   1 
ATOM   4477 N N   . PRO   B 1 217 ? 5.041   28.027  26.415  1.00 60.42 ? 218 PRO   B N   1 
ATOM   4478 C CA  . PRO   B 1 217 ? 3.766   28.365  27.051  1.00 55.76 ? 218 PRO   B CA  1 
ATOM   4479 C C   . PRO   B 1 217 ? 2.692   28.667  26.020  1.00 53.93 ? 218 PRO   B C   1 
ATOM   4480 O O   . PRO   B 1 217 ? 2.962   29.212  24.947  1.00 53.14 ? 218 PRO   B O   1 
ATOM   4481 C CB  . PRO   B 1 217 ? 4.109   29.614  27.868  1.00 60.92 ? 218 PRO   B CB  1 
ATOM   4482 C CG  . PRO   B 1 217 ? 5.186   30.278  27.061  1.00 58.69 ? 218 PRO   B CG  1 
ATOM   4483 C CD  . PRO   B 1 217 ? 5.993   29.153  26.446  1.00 62.43 ? 218 PRO   B CD  1 
ATOM   4484 N N   . LEU   B 1 218 ? 1.456   28.294  26.365  1.00 51.22 ? 219 LEU   B N   1 
ATOM   4485 C CA  . LEU   B 1 218 ? 0.292   28.501  25.499  1.00 50.32 ? 219 LEU   B CA  1 
ATOM   4486 C C   . LEU   B 1 218 ? 0.536   27.965  24.086  1.00 46.94 ? 219 LEU   B C   1 
ATOM   4487 O O   . LEU   B 1 218 ? 0.013   28.492  23.095  1.00 41.84 ? 219 LEU   B O   1 
ATOM   4488 C CB  . LEU   B 1 218 ? -0.101  29.979  25.460  1.00 51.53 ? 219 LEU   B CB  1 
ATOM   4489 C CG  . LEU   B 1 218 ? -1.495  30.238  26.026  1.00 52.07 ? 219 LEU   B CG  1 
ATOM   4490 C CD1 . LEU   B 1 218 ? -1.870  31.707  25.966  1.00 43.47 ? 219 LEU   B CD1 1 
ATOM   4491 C CD2 . LEU   B 1 218 ? -2.492  29.385  25.264  1.00 46.04 ? 219 LEU   B CD2 1 
ATOM   4492 N N   . GLY   B 1 219 ? 1.322   26.898  23.987  1.00 43.24 ? 220 GLY   B N   1 
ATOM   4493 C CA  . GLY   B 1 219 ? 1.783   26.402  22.707  1.00 41.03 ? 220 GLY   B CA  1 
ATOM   4494 C C   . GLY   B 1 219 ? 0.818   25.528  21.933  1.00 36.63 ? 220 GLY   B C   1 
ATOM   4495 O O   . GLY   B 1 219 ? 0.850   25.547  20.702  1.00 33.10 ? 220 GLY   B O   1 
ATOM   4496 N N   . ALA   B 1 220 ? -0.024  24.751  22.622  1.00 32.59 ? 221 ALA   B N   1 
ATOM   4497 C CA  . ALA   B 1 220 ? -0.907  23.796  21.946  1.00 31.03 ? 221 ALA   B CA  1 
ATOM   4498 C C   . ALA   B 1 220 ? -1.737  24.406  20.815  1.00 31.53 ? 221 ALA   B C   1 
ATOM   4499 O O   . ALA   B 1 220 ? -1.782  23.806  19.729  1.00 28.46 ? 221 ALA   B O   1 
ATOM   4500 C CB  . ALA   B 1 220 ? -1.805  23.110  22.987  1.00 30.00 ? 221 ALA   B CB  1 
ATOM   4501 N N   . PRO   B 1 221 ? -2.392  25.569  20.972  1.00 29.48 ? 222 PRO   B N   1 
ATOM   4502 C CA  . PRO   B 1 221 ? -3.140  26.129  19.830  1.00 29.71 ? 222 PRO   B CA  1 
ATOM   4503 C C   . PRO   B 1 221 ? -2.261  26.593  18.682  1.00 26.37 ? 222 PRO   B C   1 
ATOM   4504 O O   . PRO   B 1 221 ? -2.764  26.719  17.559  1.00 26.12 ? 222 PRO   B O   1 
ATOM   4505 C CB  . PRO   B 1 221 ? -3.901  27.314  20.445  1.00 31.05 ? 222 PRO   B CB  1 
ATOM   4506 C CG  . PRO   B 1 221 ? -3.919  27.045  21.900  1.00 30.62 ? 222 PRO   B CG  1 
ATOM   4507 C CD  . PRO   B 1 221 ? -2.608  26.373  22.188  1.00 32.10 ? 222 PRO   B CD  1 
ATOM   4508 N N   . ALA   B 1 222 ? -0.977  26.856  18.919  1.00 25.67 ? 223 ALA   B N   1 
ATOM   4509 C CA  . ALA   B 1 222 ? -0.105  27.328  17.850  1.00 26.22 ? 223 ALA   B CA  1 
ATOM   4510 C C   . ALA   B 1 222 ? 0.671   26.201  17.177  1.00 25.96 ? 223 ALA   B C   1 
ATOM   4511 O O   . ALA   B 1 222 ? 0.950   26.283  15.974  1.00 23.80 ? 223 ALA   B O   1 
ATOM   4512 C CB  . ALA   B 1 222 ? 0.877   28.369  18.398  1.00 29.14 ? 223 ALA   B CB  1 
ATOM   4513 N N   . TYR   B 1 223 ? 1.009   25.127  17.916  1.00 29.84 ? 224 TYR   B N   1 
ATOM   4514 C CA  . TYR   B 1 223 ? 1.874   24.114  17.301  1.00 28.94 ? 224 TYR   B CA  1 
ATOM   4515 C C   . TYR   B 1 223 ? 1.819   22.744  17.972  1.00 29.11 ? 224 TYR   B C   1 
ATOM   4516 O O   . TYR   B 1 223 ? 2.729   21.951  17.719  1.00 32.09 ? 224 TYR   B O   1 
ATOM   4517 C CB  . TYR   B 1 223 ? 3.335   24.600  17.297  1.00 28.17 ? 224 TYR   B CB  1 
ATOM   4518 C CG  . TYR   B 1 223 ? 3.820   25.171  18.619  1.00 29.93 ? 224 TYR   B CG  1 
ATOM   4519 C CD1 . TYR   B 1 223 ? 4.115   24.345  19.698  1.00 36.44 ? 224 TYR   B CD1 1 
ATOM   4520 C CD2 . TYR   B 1 223 ? 3.989   26.545  18.780  1.00 34.93 ? 224 TYR   B CD2 1 
ATOM   4521 C CE1 . TYR   B 1 223 ? 4.560   24.875  20.907  1.00 40.58 ? 224 TYR   B CE1 1 
ATOM   4522 C CE2 . TYR   B 1 223 ? 4.430   27.080  19.981  1.00 39.31 ? 224 TYR   B CE2 1 
ATOM   4523 C CZ  . TYR   B 1 223 ? 4.715   26.244  21.038  1.00 45.85 ? 224 TYR   B CZ  1 
ATOM   4524 O OH  . TYR   B 1 223 ? 5.152   26.781  22.232  1.00 48.35 ? 224 TYR   B OH  1 
ATOM   4525 N N   . GLY   B 1 224 ? 0.809   22.420  18.777  1.00 28.99 ? 225 GLY   B N   1 
ATOM   4526 C CA  . GLY   B 1 224 ? 0.849   21.228  19.604  1.00 29.17 ? 225 GLY   B CA  1 
ATOM   4527 C C   . GLY   B 1 224 ? 0.087   19.995  19.152  1.00 28.75 ? 225 GLY   B C   1 
ATOM   4528 O O   . GLY   B 1 224 ? -0.046  19.059  19.951  1.00 30.22 ? 225 GLY   B O   1 
ATOM   4529 N N   . VAL   B 1 225 ? -0.396  19.934  17.903  1.00 25.51 ? 226 VAL   B N   1 
ATOM   4530 C CA  . VAL   B 1 225 ? -1.189  18.796  17.444  1.00 26.36 ? 226 VAL   B CA  1 
ATOM   4531 C C   . VAL   B 1 225 ? -0.288  17.762  16.773  1.00 25.18 ? 226 VAL   B C   1 
ATOM   4532 O O   . VAL   B 1 225 ? 0.663   18.108  16.058  1.00 26.74 ? 226 VAL   B O   1 
ATOM   4533 C CB  . VAL   B 1 225 ? -2.319  19.261  16.504  1.00 26.19 ? 226 VAL   B CB  1 
ATOM   4534 C CG1 . VAL   B 1 225 ? -3.084  18.071  15.935  1.00 24.86 ? 226 VAL   B CG1 1 
ATOM   4535 C CG2 . VAL   B 1 225 ? -3.271  20.182  17.256  1.00 25.80 ? 226 VAL   B CG2 1 
ATOM   4536 N N   . LYS   B 1 226 ? -0.591  16.483  17.017  1.00 24.97 ? 227 LYS   B N   1 
ATOM   4537 C CA  . LYS   B 1 226 ? 0.039   15.329  16.375  1.00 25.47 ? 227 LYS   B CA  1 
ATOM   4538 C C   . LYS   B 1 226 ? -1.027  14.525  15.634  1.00 25.27 ? 227 LYS   B C   1 
ATOM   4539 O O   . LYS   B 1 226 ? -2.163  14.416  16.106  1.00 27.56 ? 227 LYS   B O   1 
ATOM   4540 C CB  . LYS   B 1 226 ? 0.733   14.437  17.421  1.00 27.26 ? 227 LYS   B CB  1 
ATOM   4541 C CG  . LYS   B 1 226 ? 2.152   14.869  17.824  1.00 29.97 ? 227 LYS   B CG  1 
ATOM   4542 C CD  . LYS   B 1 226 ? 2.206   16.183  18.598  1.00 34.92 ? 227 LYS   B CD  1 
ATOM   4543 C CE  . LYS   B 1 226 ? 1.580   16.063  19.971  1.00 32.68 ? 227 LYS   B CE  1 
ATOM   4544 N NZ  . LYS   B 1 226 ? 1.943   17.186  20.904  1.00 32.53 ? 227 LYS   B NZ  1 
ATOM   4545 N N   . SER   B 1 227 ? -0.680  13.938  14.488  1.00 25.27 ? 228 SER   B N   1 
ATOM   4546 C CA  . SER   B 1 227 ? -1.705  13.222  13.725  1.00 24.53 ? 228 SER   B CA  1 
ATOM   4547 C C   . SER   B 1 227 ? -1.072  12.171  12.811  1.00 24.22 ? 228 SER   B C   1 
ATOM   4548 O O   . SER   B 1 227 ? 0.151   12.032  12.728  1.00 23.52 ? 228 SER   B O   1 
ATOM   4549 C CB  . SER   B 1 227 ? -2.561  14.217  12.922  1.00 23.67 ? 228 SER   B CB  1 
ATOM   4550 O OG  . SER   B 1 227 ? -3.673  13.565  12.338  1.00 26.40 ? 228 SER   B OG  1 
ATOM   4551 N N   . THR   B 1 228 ? -1.936  11.416  12.126  1.00 22.58 ? 229 THR   B N   1 
ATOM   4552 C CA  . THR   B 1 228 ? -1.546  10.379  11.177  1.00 21.32 ? 229 THR   B CA  1 
ATOM   4553 C C   . THR   B 1 228 ? -1.979  10.775  9.772   1.00 20.83 ? 229 THR   B C   1 
ATOM   4554 O O   . THR   B 1 228 ? -2.854  11.631  9.587   1.00 22.43 ? 229 THR   B O   1 
ATOM   4555 C CB  . THR   B 1 228 ? -2.192  9.026   11.508  1.00 23.38 ? 229 THR   B CB  1 
ATOM   4556 O OG1 . THR   B 1 228 ? -3.612  9.130   11.340  1.00 23.84 ? 229 THR   B OG1 1 
ATOM   4557 C CG2 . THR   B 1 228 ? -1.874  8.568   12.933  1.00 23.80 ? 229 THR   B CG2 1 
ATOM   4558 N N   . LEU   B 1 229 ? -1.398  10.103  8.770   1.00 19.54 ? 230 LEU   B N   1 
ATOM   4559 C CA  . LEU   B 1 229 ? -1.819  10.386  7.401   1.00 23.21 ? 230 LEU   B CA  1 
ATOM   4560 C C   . LEU   B 1 229 ? -3.293  10.068  7.170   1.00 22.39 ? 230 LEU   B C   1 
ATOM   4561 O O   . LEU   B 1 229 ? -3.979  10.905  6.558   1.00 22.89 ? 230 LEU   B O   1 
ATOM   4562 C CB  . LEU   B 1 229 ? -0.928  9.658   6.380   1.00 17.56 ? 230 LEU   B CB  1 
ATOM   4563 C CG  . LEU   B 1 229 ? -1.250  10.067  4.936   1.00 22.89 ? 230 LEU   B CG  1 
ATOM   4564 C CD1 . LEU   B 1 229 ? -0.792  11.509  4.633   1.00 23.55 ? 230 LEU   B CD1 1 
ATOM   4565 C CD2 . LEU   B 1 229 ? -0.683  9.098   3.898   1.00 21.61 ? 230 LEU   B CD2 1 
ATOM   4566 N N   . PRO   B 1 230 ? -3.854  8.940   7.636   1.00 22.14 ? 231 PRO   B N   1 
ATOM   4567 C CA  . PRO   B 1 230 ? -5.306  8.759   7.457   1.00 21.12 ? 231 PRO   B CA  1 
ATOM   4568 C C   . PRO   B 1 230 ? -6.136  9.870   8.082   1.00 23.90 ? 231 PRO   B C   1 
ATOM   4569 O O   . PRO   B 1 230 ? -7.104  10.327  7.465   1.00 21.78 ? 231 PRO   B O   1 
ATOM   4570 C CB  . PRO   B 1 230 ? -5.574  7.397   8.117   1.00 23.82 ? 231 PRO   B CB  1 
ATOM   4571 C CG  . PRO   B 1 230 ? -4.282  6.666   7.986   1.00 23.81 ? 231 PRO   B CG  1 
ATOM   4572 C CD  . PRO   B 1 230 ? -3.213  7.704   8.145   1.00 21.48 ? 231 PRO   B CD  1 
ATOM   4573 N N   . ASP   B 1 231 ? -5.772  10.340  9.278   1.00 22.45 ? 232 ASP   B N   1 
ATOM   4574 C CA  . ASP   B 1 231 ? -6.530  11.428  9.896   1.00 23.75 ? 232 ASP   B CA  1 
ATOM   4575 C C   . ASP   B 1 231 ? -6.401  12.718  9.097   1.00 22.16 ? 232 ASP   B C   1 
ATOM   4576 O O   . ASP   B 1 231 ? -7.383  13.452  8.928   1.00 24.71 ? 232 ASP   B O   1 
ATOM   4577 C CB  . ASP   B 1 231 ? -6.070  11.653  11.335  1.00 24.30 ? 232 ASP   B CB  1 
ATOM   4578 C CG  . ASP   B 1 231 ? -6.729  10.699  12.318  1.00 28.94 ? 232 ASP   B CG  1 
ATOM   4579 O OD1 . ASP   B 1 231 ? -7.496  9.811   11.884  1.00 29.73 ? 232 ASP   B OD1 1 
ATOM   4580 O OD2 . ASP   B 1 231 ? -6.475  10.847  13.528  1.00 30.23 ? 232 ASP   B OD2 1 
ATOM   4581 N N   . MET   B 1 232 ? -5.205  13.024  8.601   1.00 20.88 ? 233 MET   B N   1 
ATOM   4582 C CA  . MET   B 1 232 ? -5.069  14.261  7.840   1.00 20.01 ? 233 MET   B CA  1 
ATOM   4583 C C   . MET   B 1 232 ? -5.821  14.185  6.516   1.00 21.88 ? 233 MET   B C   1 
ATOM   4584 O O   . MET   B 1 232 ? -6.399  15.181  6.078   1.00 20.41 ? 233 MET   B O   1 
ATOM   4585 C CB  . MET   B 1 232 ? -3.596  14.592  7.636   1.00 19.37 ? 233 MET   B CB  1 
ATOM   4586 C CG  . MET   B 1 232 ? -2.913  14.969  8.950   1.00 20.01 ? 233 MET   B CG  1 
ATOM   4587 S SD  . MET   B 1 232 ? -3.650  16.345  9.847   1.00 22.67 ? 233 MET   B SD  1 
ATOM   4588 C CE  . MET   B 1 232 ? -3.319  17.709  8.714   1.00 22.27 ? 233 MET   B CE  1 
ATOM   4589 N N   . LEU   B 1 233 ? -5.879  13.008  5.895   1.00 21.41 ? 234 LEU   B N   1 
ATOM   4590 C CA  . LEU   B 1 233 ? -6.730  12.856  4.718   1.00 24.35 ? 234 LEU   B CA  1 
ATOM   4591 C C   . LEU   B 1 233 ? -8.200  13.038  5.065   1.00 23.01 ? 234 LEU   B C   1 
ATOM   4592 O O   . LEU   B 1 233 ? -8.962  13.622  4.282   1.00 22.79 ? 234 LEU   B O   1 
ATOM   4593 C CB  . LEU   B 1 233 ? -6.493  11.493  4.079   1.00 23.74 ? 234 LEU   B CB  1 
ATOM   4594 C CG  . LEU   B 1 233 ? -5.228  11.424  3.239   1.00 22.13 ? 234 LEU   B CG  1 
ATOM   4595 C CD1 . LEU   B 1 233 ? -4.901  9.973   2.873   1.00 23.55 ? 234 LEU   B CD1 1 
ATOM   4596 C CD2 . LEU   B 1 233 ? -5.366  12.290  1.986   1.00 27.31 ? 234 LEU   B CD2 1 
ATOM   4597 N N   . SER   B 1 234 ? -8.625  12.533  6.227   1.00 23.68 ? 235 SER   B N   1 
ATOM   4598 C CA  . SER   B 1 234 ? -9.992  12.774  6.679   1.00 23.60 ? 235 SER   B CA  1 
ATOM   4599 C C   . SER   B 1 234 ? -10.245 14.260  6.889   1.00 24.23 ? 235 SER   B C   1 
ATOM   4600 O O   . SER   B 1 234 ? -11.316 14.767  6.538   1.00 23.18 ? 235 SER   B O   1 
ATOM   4601 C CB  . SER   B 1 234 ? -10.268 12.000  7.964   1.00 25.66 ? 235 SER   B CB  1 
ATOM   4602 O OG  . SER   B 1 234 ? -10.243 10.604  7.731   1.00 27.49 ? 235 SER   B OG  1 
ATOM   4603 N N   . PHE   B 1 235 ? -9.269  14.968  7.466   1.00 20.00 ? 236 PHE   B N   1 
ATOM   4604 C CA  . PHE   B 1 235 ? -9.390  16.413  7.652   1.00 21.97 ? 236 PHE   B CA  1 
ATOM   4605 C C   . PHE   B 1 235 ? -9.490  17.139  6.316   1.00 23.30 ? 236 PHE   B C   1 
ATOM   4606 O O   . PHE   B 1 235 ? -10.295 18.069  6.163   1.00 22.22 ? 236 PHE   B O   1 
ATOM   4607 C CB  . PHE   B 1 235 ? -8.202  16.935  8.457   1.00 20.71 ? 236 PHE   B CB  1 
ATOM   4608 C CG  . PHE   B 1 235 ? -8.298  18.394  8.797   1.00 20.91 ? 236 PHE   B CG  1 
ATOM   4609 C CD1 . PHE   B 1 235 ? -9.356  18.872  9.557   1.00 23.72 ? 236 PHE   B CD1 1 
ATOM   4610 C CD2 . PHE   B 1 235 ? -7.326  19.290  8.359   1.00 21.25 ? 236 PHE   B CD2 1 
ATOM   4611 C CE1 . PHE   B 1 235 ? -9.452  20.229  9.870   1.00 24.03 ? 236 PHE   B CE1 1 
ATOM   4612 C CE2 . PHE   B 1 235 ? -7.405  20.631  8.668   1.00 22.74 ? 236 PHE   B CE2 1 
ATOM   4613 C CZ  . PHE   B 1 235 ? -8.474  21.106  9.434   1.00 26.04 ? 236 PHE   B CZ  1 
ATOM   4614 N N   . ILE   B 1 236 ? -8.699  16.721  5.326   1.00 20.49 ? 237 ILE   B N   1 
ATOM   4615 C CA  . ILE   B 1 236 ? -8.822  17.349  4.016   1.00 23.06 ? 237 ILE   B CA  1 
ATOM   4616 C C   . ILE   B 1 236 ? -10.180 17.031  3.405   1.00 21.76 ? 237 ILE   B C   1 
ATOM   4617 O O   . ILE   B 1 236 ? -10.810 17.894  2.785   1.00 21.86 ? 237 ILE   B O   1 
ATOM   4618 C CB  . ILE   B 1 236 ? -7.666  16.933  3.086   1.00 25.22 ? 237 ILE   B CB  1 
ATOM   4619 C CG1 . ILE   B 1 236 ? -6.312  17.362  3.659   1.00 21.17 ? 237 ILE   B CG1 1 
ATOM   4620 C CG2 . ILE   B 1 236 ? -7.864  17.534  1.691   1.00 25.37 ? 237 ILE   B CG2 1 
ATOM   4621 C CD1 . ILE   B 1 236 ? -6.130  18.869  3.939   1.00 23.95 ? 237 ILE   B CD1 1 
ATOM   4622 N N   . HIS   B 1 237 ? -10.664 15.797  3.584   1.00 20.03 ? 238 HIS   B N   1 
ATOM   4623 C CA  . HIS   B 1 237 ? -11.998 15.456  3.093   1.00 21.97 ? 238 HIS   B CA  1 
ATOM   4624 C C   . HIS   B 1 237 ? -13.054 16.371  3.694   1.00 23.74 ? 238 HIS   B C   1 
ATOM   4625 O O   . HIS   B 1 237 ? -13.968 16.822  2.992   1.00 23.67 ? 238 HIS   B O   1 
ATOM   4626 C CB  . HIS   B 1 237 ? -12.338 14.001  3.407   1.00 23.76 ? 238 HIS   B CB  1 
ATOM   4627 C CG  . HIS   B 1 237 ? -13.750 13.638  3.063   1.00 26.29 ? 238 HIS   B CG  1 
ATOM   4628 N ND1 . HIS   B 1 237 ? -14.790 13.784  3.955   1.00 29.59 ? 238 HIS   B ND1 1 
ATOM   4629 C CD2 . HIS   B 1 237 ? -14.296 13.163  1.919   1.00 31.83 ? 238 HIS   B CD2 1 
ATOM   4630 C CE1 . HIS   B 1 237 ? -15.917 13.402  3.379   1.00 29.01 ? 238 HIS   B CE1 1 
ATOM   4631 N NE2 . HIS   B 1 237 ? -15.645 13.022  2.144   1.00 29.15 ? 238 HIS   B NE2 1 
ATOM   4632 N N   . ALA   B 1 238 ? -12.948 16.653  4.994   1.00 22.77 ? 239 ALA   B N   1 
ATOM   4633 C CA  . ALA   B 1 238 ? -13.928 17.522  5.636   1.00 24.52 ? 239 ALA   B CA  1 
ATOM   4634 C C   . ALA   B 1 238 ? -13.861 18.938  5.077   1.00 24.72 ? 239 ALA   B C   1 
ATOM   4635 O O   . ALA   B 1 238 ? -14.892 19.613  4.959   1.00 24.94 ? 239 ALA   B O   1 
ATOM   4636 C CB  . ALA   B 1 238 ? -13.715 17.526  7.148   1.00 25.97 ? 239 ALA   B CB  1 
ATOM   4637 N N   . ASN   B 1 239 ? -12.659 19.412  4.737   1.00 21.47 ? 240 ASN   B N   1 
ATOM   4638 C CA  . ASN   B 1 239 ? -12.562 20.752  4.177   1.00 21.33 ? 240 ASN   B CA  1 
ATOM   4639 C C   . ASN   B 1 239 ? -13.083 20.801  2.750   1.00 25.24 ? 240 ASN   B C   1 
ATOM   4640 O O   . ASN   B 1 239 ? -13.624 21.830  2.325   1.00 24.17 ? 240 ASN   B O   1 
ATOM   4641 C CB  . ASN   B 1 239 ? -11.124 21.246  4.241   1.00 21.17 ? 240 ASN   B CB  1 
ATOM   4642 C CG  . ASN   B 1 239 ? -10.785 21.820  5.592   1.00 25.71 ? 240 ASN   B CG  1 
ATOM   4643 O OD1 . ASN   B 1 239 ? -10.936 23.014  5.816   1.00 23.27 ? 240 ASN   B OD1 1 
ATOM   4644 N ND2 . ASN   B 1 239 ? -10.347 20.971  6.509   1.00 22.22 ? 240 ASN   B ND2 1 
ATOM   4645 N N   . LEU   B 1 240 ? -12.917 19.711  2.000   1.00 21.92 ? 241 LEU   B N   1 
ATOM   4646 C CA  . LEU   B 1 240 ? -13.447 19.630  0.644   1.00 24.49 ? 241 LEU   B CA  1 
ATOM   4647 C C   . LEU   B 1 240 ? -14.948 19.382  0.605   1.00 25.14 ? 241 LEU   B C   1 
ATOM   4648 O O   . LEU   B 1 240 ? -15.575 19.670  -0.419  1.00 27.29 ? 241 LEU   B O   1 
ATOM   4649 C CB  . LEU   B 1 240 ? -12.750 18.511  -0.130  1.00 22.92 ? 241 LEU   B CB  1 
ATOM   4650 C CG  . LEU   B 1 240 ? -11.374 18.843  -0.707  1.00 23.16 ? 241 LEU   B CG  1 
ATOM   4651 C CD1 . LEU   B 1 240 ? -10.675 17.571  -1.194  1.00 21.40 ? 241 LEU   B CD1 1 
ATOM   4652 C CD2 . LEU   B 1 240 ? -11.467 19.862  -1.844  1.00 25.20 ? 241 LEU   B CD2 1 
ATOM   4653 N N   . ASN   B 1 241 ? -15.526 18.827  1.677   1.00 25.90 ? 242 ASN   B N   1 
ATOM   4654 C CA  . ASN   B 1 241 ? -16.927 18.395  1.684   1.00 27.70 ? 242 ASN   B CA  1 
ATOM   4655 C C   . ASN   B 1 241 ? -17.608 18.754  2.999   1.00 27.78 ? 242 ASN   B C   1 
ATOM   4656 O O   . ASN   B 1 241 ? -18.215 17.879  3.633   1.00 26.34 ? 242 ASN   B O   1 
ATOM   4657 C CB  . ASN   B 1 241 ? -17.033 16.881  1.474   1.00 27.19 ? 242 ASN   B CB  1 
ATOM   4658 C CG  . ASN   B 1 241 ? -16.396 16.419  0.185   1.00 30.17 ? 242 ASN   B CG  1 
ATOM   4659 O OD1 . ASN   B 1 241 ? -17.015 16.476  -0.873  1.00 34.48 ? 242 ASN   B OD1 1 
ATOM   4660 N ND2 . ASN   B 1 241 ? -15.151 15.950  0.268   1.00 28.74 ? 242 ASN   B ND2 1 
ATOM   4661 N N   . PRO   B 1 242 ? -17.548 20.015  3.438   1.00 25.47 ? 243 PRO   B N   1 
ATOM   4662 C CA  . PRO   B 1 242 ? -18.168 20.355  4.726   1.00 28.21 ? 243 PRO   B CA  1 
ATOM   4663 C C   . PRO   B 1 242 ? -19.654 20.055  4.777   1.00 28.87 ? 243 PRO   B C   1 
ATOM   4664 O O   . PRO   B 1 242 ? -20.171 19.764  5.862   1.00 28.95 ? 243 PRO   B O   1 
ATOM   4665 C CB  . PRO   B 1 242 ? -17.886 21.858  4.862   1.00 28.61 ? 243 PRO   B CB  1 
ATOM   4666 C CG  . PRO   B 1 242 ? -17.730 22.340  3.468   1.00 31.32 ? 243 PRO   B CG  1 
ATOM   4667 C CD  . PRO   B 1 242 ? -17.105 21.210  2.701   1.00 24.50 ? 243 PRO   B CD  1 
ATOM   4668 N N   . GLN   B 1 243 ? -20.356 20.091  3.637   1.00 27.89 ? 244 GLN   B N   1 
ATOM   4669 C CA  A GLN   B 1 243 ? -21.794 19.853  3.673   0.35 30.61 ? 244 GLN   B CA  1 
ATOM   4670 C CA  B GLN   B 1 243 ? -21.793 19.832  3.595   0.65 30.60 ? 244 GLN   B CA  1 
ATOM   4671 C C   . GLN   B 1 243 ? -22.147 18.403  3.985   1.00 30.45 ? 244 GLN   B C   1 
ATOM   4672 O O   . GLN   B 1 243 ? -23.325 18.117  4.239   1.00 31.90 ? 244 GLN   B O   1 
ATOM   4673 C CB  A GLN   B 1 243 ? -22.443 20.286  2.355   0.35 33.63 ? 244 GLN   B CB  1 
ATOM   4674 C CB  B GLN   B 1 243 ? -22.346 20.122  2.196   0.65 33.85 ? 244 GLN   B CB  1 
ATOM   4675 C CG  A GLN   B 1 243 ? -21.815 19.712  1.097   0.35 33.32 ? 244 GLN   B CG  1 
ATOM   4676 C CG  B GLN   B 1 243 ? -21.907 19.136  1.109   0.65 33.02 ? 244 GLN   B CG  1 
ATOM   4677 C CD  A GLN   B 1 243 ? -22.269 20.449  -0.152  0.35 32.28 ? 244 GLN   B CD  1 
ATOM   4678 C CD  B GLN   B 1 243 ? -20.477 19.366  0.630   0.65 33.28 ? 244 GLN   B CD  1 
ATOM   4679 O OE1 A GLN   B 1 243 ? -22.733 21.586  -0.079  0.35 31.68 ? 244 GLN   B OE1 1 
ATOM   4680 O OE1 B GLN   B 1 243 ? -19.816 20.323  1.034   0.65 29.67 ? 244 GLN   B OE1 1 
ATOM   4681 N NE2 A GLN   B 1 243 ? -22.133 19.805  -1.305  0.35 35.52 ? 244 GLN   B NE2 1 
ATOM   4682 N NE2 B GLN   B 1 243 ? -19.998 18.482  -0.242  0.65 35.97 ? 244 GLN   B NE2 1 
ATOM   4683 N N   . LYS   B 1 244 ? -21.171 17.501  4.013   1.00 29.61 ? 245 LYS   B N   1 
ATOM   4684 C CA  . LYS   B 1 244 ? -21.414 16.112  4.381   1.00 30.38 ? 245 LYS   B CA  1 
ATOM   4685 C C   . LYS   B 1 244 ? -21.277 15.877  5.880   1.00 30.53 ? 245 LYS   B C   1 
ATOM   4686 O O   . LYS   B 1 244 ? -21.376 14.732  6.327   1.00 33.30 ? 245 LYS   B O   1 
ATOM   4687 C CB  . LYS   B 1 244 ? -20.469 15.191  3.601   1.00 30.19 ? 245 LYS   B CB  1 
ATOM   4688 C CG  . LYS   B 1 244 ? -20.680 15.257  2.091   1.00 35.29 ? 245 LYS   B CG  1 
ATOM   4689 C CD  . LYS   B 1 244 ? -19.854 14.240  1.315   1.00 34.97 ? 245 LYS   B CD  1 
ATOM   4690 C CE  . LYS   B 1 244 ? -20.384 14.124  -0.112  1.00 42.44 ? 245 LYS   B CE  1 
ATOM   4691 N NZ  . LYS   B 1 244 ? -19.774 13.012  -0.889  1.00 43.31 ? 245 LYS   B NZ  1 
ATOM   4692 N N   . TYR   B 1 245 ? -21.073 16.929  6.665   1.00 31.35 ? 246 TYR   B N   1 
ATOM   4693 C CA  . TYR   B 1 245 ? -20.817 16.805  8.091   1.00 30.98 ? 246 TYR   B CA  1 
ATOM   4694 C C   . TYR   B 1 245 ? -21.940 17.440  8.902   1.00 34.78 ? 246 TYR   B C   1 
ATOM   4695 O O   . TYR   B 1 245 ? -22.739 18.219  8.366   1.00 34.49 ? 246 TYR   B O   1 
ATOM   4696 C CB  . TYR   B 1 245 ? -19.460 17.447  8.434   1.00 33.84 ? 246 TYR   B CB  1 
ATOM   4697 C CG  . TYR   B 1 245 ? -18.286 16.618  7.945   1.00 31.90 ? 246 TYR   B CG  1 
ATOM   4698 C CD1 . TYR   B 1 245 ? -17.966 16.562  6.595   1.00 30.07 ? 246 TYR   B CD1 1 
ATOM   4699 C CD2 . TYR   B 1 245 ? -17.523 15.866  8.827   1.00 32.61 ? 246 TYR   B CD2 1 
ATOM   4700 C CE1 . TYR   B 1 245 ? -16.916 15.792  6.138   1.00 31.19 ? 246 TYR   B CE1 1 
ATOM   4701 C CE2 . TYR   B 1 245 ? -16.461 15.089  8.378   1.00 29.11 ? 246 TYR   B CE2 1 
ATOM   4702 C CZ  . TYR   B 1 245 ? -16.166 15.056  7.032   1.00 29.09 ? 246 TYR   B CZ  1 
ATOM   4703 O OH  . TYR   B 1 245 ? -15.114 14.294  6.578   1.00 29.23 ? 246 TYR   B OH  1 
ATOM   4704 N N   . PRO   B 1 246 ? -22.046 17.123  10.197  1.00 36.73 ? 247 PRO   B N   1 
ATOM   4705 C CA  . PRO   B 1 246 ? -23.097 17.742  11.014  1.00 39.05 ? 247 PRO   B CA  1 
ATOM   4706 C C   . PRO   B 1 246 ? -22.960 19.258  11.065  1.00 36.01 ? 247 PRO   B C   1 
ATOM   4707 O O   . PRO   B 1 246 ? -21.885 19.824  10.860  1.00 35.31 ? 247 PRO   B O   1 
ATOM   4708 C CB  . PRO   B 1 246 ? -22.892 17.113  12.397  1.00 40.60 ? 247 PRO   B CB  1 
ATOM   4709 C CG  . PRO   B 1 246 ? -22.231 15.813  12.112  1.00 39.62 ? 247 PRO   B CG  1 
ATOM   4710 C CD  . PRO   B 1 246 ? -21.315 16.087  10.951  1.00 34.64 ? 247 PRO   B CD  1 
ATOM   4711 N N   . ALA   B 1 247 ? -24.083 19.910  11.377  1.00 40.60 ? 248 ALA   B N   1 
ATOM   4712 C CA  . ALA   B 1 247 ? -24.212 21.351  11.187  1.00 34.93 ? 248 ALA   B CA  1 
ATOM   4713 C C   . ALA   B 1 247 ? -23.146 22.137  11.945  1.00 35.77 ? 248 ALA   B C   1 
ATOM   4714 O O   . ALA   B 1 247 ? -22.621 23.133  11.431  1.00 34.83 ? 248 ALA   B O   1 
ATOM   4715 C CB  . ALA   B 1 247 ? -25.611 21.798  11.615  1.00 35.47 ? 248 ALA   B CB  1 
ATOM   4716 N N   . ASP   B 1 248 ? -22.810 21.706  13.166  1.00 37.80 ? 249 ASP   B N   1 
ATOM   4717 C CA  . ASP   B 1 248 ? -21.922 22.503  14.011  1.00 39.52 ? 249 ASP   B CA  1 
ATOM   4718 C C   . ASP   B 1 248 ? -20.486 22.468  13.500  1.00 32.13 ? 249 ASP   B C   1 
ATOM   4719 O O   . ASP   B 1 248 ? -19.787 23.489  13.531  1.00 34.61 ? 249 ASP   B O   1 
ATOM   4720 C CB  . ASP   B 1 248 ? -21.987 22.015  15.459  1.00 43.05 ? 249 ASP   B CB  1 
ATOM   4721 C CG  . ASP   B 1 248 ? -23.281 22.419  16.162  1.00 54.39 ? 249 ASP   B CG  1 
ATOM   4722 O OD1 . ASP   B 1 248 ? -24.075 23.188  15.576  1.00 49.26 ? 249 ASP   B OD1 1 
ATOM   4723 O OD2 . ASP   B 1 248 ? -23.503 21.965  17.306  1.00 56.10 ? 249 ASP   B OD2 1 
ATOM   4724 N N   . ILE   B 1 249 ? -20.022 21.307  13.036  1.00 35.69 ? 250 ILE   B N   1 
ATOM   4725 C CA  . ILE   B 1 249 ? -18.675 21.251  12.479  1.00 31.78 ? 250 ILE   B CA  1 
ATOM   4726 C C   . ILE   B 1 249 ? -18.667 21.755  11.035  1.00 30.96 ? 250 ILE   B C   1 
ATOM   4727 O O   . ILE   B 1 249 ? -17.654 22.292  10.571  1.00 31.02 ? 250 ILE   B O   1 
ATOM   4728 C CB  . ILE   B 1 249 ? -18.095 19.826  12.612  1.00 29.87 ? 250 ILE   B CB  1 
ATOM   4729 C CG1 . ILE   B 1 249 ? -16.572 19.820  12.424  1.00 28.44 ? 250 ILE   B CG1 1 
ATOM   4730 C CG2 . ILE   B 1 249 ? -18.753 18.859  11.644  1.00 34.77 ? 250 ILE   B CG2 1 
ATOM   4731 C CD1 . ILE   B 1 249 ? -15.806 20.538  13.528  1.00 31.10 ? 250 ILE   B CD1 1 
ATOM   4732 N N   . GLN   B 1 250 ? -19.783 21.612  10.313  1.00 30.48 ? 251 GLN   B N   1 
ATOM   4733 C CA  . GLN   B 1 250 ? -19.885 22.163  8.963   1.00 29.72 ? 251 GLN   B CA  1 
ATOM   4734 C C   . GLN   B 1 250 ? -19.685 23.672  8.970   1.00 30.65 ? 251 GLN   B C   1 
ATOM   4735 O O   . GLN   B 1 250 ? -18.860 24.209  8.220   1.00 29.95 ? 251 GLN   B O   1 
ATOM   4736 C CB  . GLN   B 1 250 ? -21.248 21.810  8.353   1.00 32.98 ? 251 GLN   B CB  1 
ATOM   4737 C CG  . GLN   B 1 250 ? -21.526 22.496  7.018   1.00 32.11 ? 251 GLN   B CG  1 
ATOM   4738 C CD  . GLN   B 1 250 ? -22.900 22.161  6.441   1.00 39.03 ? 251 GLN   B CD  1 
ATOM   4739 O OE1 . GLN   B 1 250 ? -23.300 22.709  5.409   1.00 41.87 ? 251 GLN   B OE1 1 
ATOM   4740 N NE2 . GLN   B 1 250 ? -23.623 21.252  7.099   1.00 45.56 ? 251 GLN   B NE2 1 
ATOM   4741 N N   . ARG   B 1 251 ? -20.437 24.381  9.807   1.00 32.66 ? 252 ARG   B N   1 
ATOM   4742 C CA  . ARG   B 1 251 ? -20.284 25.831  9.817   1.00 33.72 ? 252 ARG   B CA  1 
ATOM   4743 C C   . ARG   B 1 251 ? -18.930 26.239  10.384  1.00 29.07 ? 252 ARG   B C   1 
ATOM   4744 O O   . ARG   B 1 251 ? -18.373 27.264  9.971   1.00 29.02 ? 252 ARG   B O   1 
ATOM   4745 C CB  . ARG   B 1 251 ? -21.455 26.473  10.564  1.00 41.10 ? 252 ARG   B CB  1 
ATOM   4746 C CG  . ARG   B 1 251 ? -22.690 26.593  9.665   1.00 40.02 ? 252 ARG   B CG  1 
ATOM   4747 C CD  . ARG   B 1 251 ? -23.988 26.701  10.436  1.00 51.92 ? 252 ARG   B CD  1 
ATOM   4748 N NE  . ARG   B 1 251 ? -24.386 28.085  10.667  1.00 60.46 ? 252 ARG   B NE  1 
ATOM   4749 C CZ  . ARG   B 1 251 ? -24.380 28.674  11.855  1.00 64.23 ? 252 ARG   B CZ  1 
ATOM   4750 N NH1 . ARG   B 1 251 ? -24.016 28.019  12.947  1.00 61.96 ? 252 ARG   B NH1 1 
ATOM   4751 N NH2 . ARG   B 1 251 ? -24.756 29.947  11.952  1.00 57.95 ? 252 ARG   B NH2 1 
ATOM   4752 N N   . ALA   B 1 252 ? -18.363 25.430  11.283  1.00 30.12 ? 253 ALA   B N   1 
ATOM   4753 C CA  . ALA   B 1 252 ? -17.006 25.681  11.769  1.00 28.64 ? 253 ALA   B CA  1 
ATOM   4754 C C   . ALA   B 1 252 ? -15.990 25.641  10.633  1.00 27.31 ? 253 ALA   B C   1 
ATOM   4755 O O   . ALA   B 1 252 ? -15.109 26.505  10.542  1.00 24.57 ? 253 ALA   B O   1 
ATOM   4756 C CB  . ALA   B 1 252 ? -16.643 24.658  12.845  1.00 28.19 ? 253 ALA   B CB  1 
ATOM   4757 N N   . ILE   B 1 253 ? -16.075 24.617  9.779   1.00 25.41 ? 254 ILE   B N   1 
ATOM   4758 C CA  . ILE   B 1 253 ? -15.163 24.507  8.640   1.00 25.39 ? 254 ILE   B CA  1 
ATOM   4759 C C   . ILE   B 1 253 ? -15.370 25.672  7.687   1.00 25.40 ? 254 ILE   B C   1 
ATOM   4760 O O   . ILE   B 1 253 ? -14.411 26.295  7.216   1.00 25.35 ? 254 ILE   B O   1 
ATOM   4761 C CB  . ILE   B 1 253 ? -15.367 23.160  7.922   1.00 25.86 ? 254 ILE   B CB  1 
ATOM   4762 C CG1 . ILE   B 1 253 ? -15.025 22.008  8.863   1.00 27.99 ? 254 ILE   B CG1 1 
ATOM   4763 C CG2 . ILE   B 1 253 ? -14.546 23.103  6.631   1.00 25.15 ? 254 ILE   B CG2 1 
ATOM   4764 C CD1 . ILE   B 1 253 ? -15.515 20.660  8.384   1.00 27.46 ? 254 ILE   B CD1 1 
ATOM   4765 N N   . ASN   B 1 254 ? -16.636 25.973  7.378   1.00 26.35 ? 255 ASN   B N   1 
ATOM   4766 C CA  . ASN   B 1 254 ? -16.939 27.114  6.518   1.00 26.98 ? 255 ASN   B CA  1 
ATOM   4767 C C   . ASN   B 1 254 ? -16.310 28.394  7.053   1.00 27.29 ? 255 ASN   B C   1 
ATOM   4768 O O   . ASN   B 1 254 ? -15.785 29.203  6.281   1.00 28.04 ? 255 ASN   B O   1 
ATOM   4769 C CB  . ASN   B 1 254 ? -18.454 27.290  6.389   1.00 27.90 ? 255 ASN   B CB  1 
ATOM   4770 C CG  . ASN   B 1 254 ? -19.091 26.276  5.457   1.00 34.36 ? 255 ASN   B CG  1 
ATOM   4771 O OD1 . ASN   B 1 254 ? -18.425 25.674  4.614   1.00 35.38 ? 255 ASN   B OD1 1 
ATOM   4772 N ND2 . ASN   B 1 254 ? -20.404 26.105  5.590   1.00 38.68 ? 255 ASN   B ND2 1 
ATOM   4773 N N   . GLU   B 1 255 ? -16.353 28.589  8.375   1.00 30.25 ? 256 GLU   B N   1 
ATOM   4774 C CA  . GLU   B 1 255 ? -15.781 29.788  8.989   1.00 26.21 ? 256 GLU   B CA  1 
ATOM   4775 C C   . GLU   B 1 255 ? -14.292 29.917  8.679   1.00 28.90 ? 256 GLU   B C   1 
ATOM   4776 O O   . GLU   B 1 255 ? -13.791 31.023  8.437   1.00 26.72 ? 256 GLU   B O   1 
ATOM   4777 C CB  . GLU   B 1 255 ? -16.025 29.736  10.501  1.00 30.23 ? 256 GLU   B CB  1 
ATOM   4778 C CG  . GLU   B 1 255 ? -16.102 31.070  11.228  1.00 35.70 ? 256 GLU   B CG  1 
ATOM   4779 C CD  . GLU   B 1 255 ? -17.258 31.939  10.764  1.00 34.02 ? 256 GLU   B CD  1 
ATOM   4780 O OE1 . GLU   B 1 255 ? -16.989 33.036  10.246  1.00 31.95 ? 256 GLU   B OE1 1 
ATOM   4781 O OE2 . GLU   B 1 255 ? -18.434 31.537  10.914  1.00 33.60 ? 256 GLU   B OE2 1 
ATOM   4782 N N   . THR   B 1 256 ? -13.565 28.794  8.667   1.00 23.40 ? 257 THR   B N   1 
ATOM   4783 C CA  . THR   B 1 256 ? -12.131 28.816  8.406   1.00 23.05 ? 257 THR   B CA  1 
ATOM   4784 C C   . THR   B 1 256 ? -11.792 29.087  6.946   1.00 23.20 ? 257 THR   B C   1 
ATOM   4785 O O   . THR   B 1 256 ? -10.622 29.347  6.645   1.00 24.54 ? 257 THR   B O   1 
ATOM   4786 C CB  . THR   B 1 256 ? -11.477 27.488  8.827   1.00 23.54 ? 257 THR   B CB  1 
ATOM   4787 O OG1 . THR   B 1 256 ? -11.811 26.446  7.900   1.00 23.76 ? 257 THR   B OG1 1 
ATOM   4788 C CG2 . THR   B 1 256 ? -11.923 27.082  10.220  1.00 23.51 ? 257 THR   B CG2 1 
ATOM   4789 N N   . HIS   B 1 257 ? -12.757 29.000  6.032   1.00 22.82 ? 258 HIS   B N   1 
ATOM   4790 C CA  . HIS   B 1 257 ? -12.489 29.237  4.618   1.00 19.87 ? 258 HIS   B CA  1 
ATOM   4791 C C   . HIS   B 1 257 ? -12.747 30.675  4.200   1.00 22.84 ? 258 HIS   B C   1 
ATOM   4792 O O   . HIS   B 1 257 ? -12.472 31.029  3.044   1.00 21.96 ? 258 HIS   B O   1 
ATOM   4793 C CB  . HIS   B 1 257 ? -13.339 28.315  3.746   1.00 24.13 ? 258 HIS   B CB  1 
ATOM   4794 C CG  . HIS   B 1 257 ? -13.040 26.866  3.939   1.00 22.22 ? 258 HIS   B CG  1 
ATOM   4795 N ND1 . HIS   B 1 257 ? -13.807 25.864  3.379   1.00 26.66 ? 258 HIS   B ND1 1 
ATOM   4796 C CD2 . HIS   B 1 257 ? -12.048 26.250  4.621   1.00 23.45 ? 258 HIS   B CD2 1 
ATOM   4797 C CE1 . HIS   B 1 257 ? -13.298 24.691  3.713   1.00 24.65 ? 258 HIS   B CE1 1 
ATOM   4798 N NE2 . HIS   B 1 257 ? -12.229 24.897  4.463   1.00 24.52 ? 258 HIS   B NE2 1 
ATOM   4799 N N   . GLN   B 1 258 ? -13.270 31.499  5.102   1.00 21.09 ? 259 GLN   B N   1 
ATOM   4800 C CA  . GLN   B 1 258 ? -13.637 32.878  4.779   1.00 22.03 ? 259 GLN   B CA  1 
ATOM   4801 C C   . GLN   B 1 258 ? -12.414 33.780  4.908   1.00 21.67 ? 259 GLN   B C   1 
ATOM   4802 O O   . GLN   B 1 258 ? -11.898 33.988  6.011   1.00 22.37 ? 259 GLN   B O   1 
ATOM   4803 C CB  . GLN   B 1 258 ? -14.756 33.362  5.693   1.00 24.46 ? 259 GLN   B CB  1 
ATOM   4804 C CG  . GLN   B 1 258 ? -15.084 34.827  5.498   1.00 25.41 ? 259 GLN   B CG  1 
ATOM   4805 C CD  . GLN   B 1 258 ? -16.281 35.262  6.309   1.00 30.99 ? 259 GLN   B CD  1 
ATOM   4806 O OE1 . GLN   B 1 258 ? -17.007 34.432  6.854   1.00 35.24 ? 259 GLN   B OE1 1 
ATOM   4807 N NE2 . GLN   B 1 258 ? -16.493 36.571  6.394   1.00 33.47 ? 259 GLN   B NE2 1 
ATOM   4808 N N   . GLY   B 1 259 ? -11.958 34.325  3.782   1.00 24.40 ? 260 GLY   B N   1 
ATOM   4809 C CA  . GLY   B 1 259 ? -10.892 35.309  3.833   1.00 23.87 ? 260 GLY   B CA  1 
ATOM   4810 C C   . GLY   B 1 259 ? -11.319 36.541  4.614   1.00 21.09 ? 260 GLY   B C   1 
ATOM   4811 O O   . GLY   B 1 259 ? -12.449 37.019  4.491   1.00 22.78 ? 260 GLY   B O   1 
ATOM   4812 N N   . ARG   B 1 260 ? -10.388 37.065  5.420   1.00 22.00 ? 261 ARG   B N   1 
ATOM   4813 C CA  . ARG   B 1 260 ? -10.651 38.193  6.303   1.00 19.40 ? 261 ARG   B CA  1 
ATOM   4814 C C   . ARG   B 1 260 ? -9.939  39.474  5.890   1.00 21.91 ? 261 ARG   B C   1 
ATOM   4815 O O   . ARG   B 1 260 ? -10.397 40.556  6.255   1.00 25.64 ? 261 ARG   B O   1 
ATOM   4816 C CB  . ARG   B 1 260 ? -10.247 37.837  7.739   1.00 20.66 ? 261 ARG   B CB  1 
ATOM   4817 C CG  . ARG   B 1 260 ? -10.839 36.505  8.230   1.00 18.78 ? 261 ARG   B CG  1 
ATOM   4818 C CD  . ARG   B 1 260 ? -12.369 36.549  8.302   1.00 22.41 ? 261 ARG   B CD  1 
ATOM   4819 N NE  . ARG   B 1 260 ? -12.923 35.225  8.595   1.00 22.68 ? 261 ARG   B NE  1 
ATOM   4820 C CZ  . ARG   B 1 260 ? -14.072 35.010  9.224   1.00 26.83 ? 261 ARG   B CZ  1 
ATOM   4821 N NH1 . ARG   B 1 260 ? -14.813 36.010  9.672   1.00 26.85 ? 261 ARG   B NH1 1 
ATOM   4822 N NH2 . ARG   B 1 260 ? -14.486 33.758  9.407   1.00 27.44 ? 261 ARG   B NH2 1 
ATOM   4823 N N   . TYR   B 1 261 ? -8.812  39.371  5.183   1.00 18.61 ? 262 TYR   B N   1 
ATOM   4824 C CA  . TYR   B 1 261 ? -8.104  40.500  4.579   1.00 19.82 ? 262 TYR   B CA  1 
ATOM   4825 C C   . TYR   B 1 261 ? -7.082  39.890  3.631   1.00 18.69 ? 262 TYR   B C   1 
ATOM   4826 O O   . TYR   B 1 261 ? -6.939  38.666  3.558   1.00 18.26 ? 262 TYR   B O   1 
ATOM   4827 C CB  . TYR   B 1 261 ? -7.422  41.412  5.615   1.00 19.02 ? 262 TYR   B CB  1 
ATOM   4828 C CG  . TYR   B 1 261 ? -6.419  40.685  6.498   1.00 18.20 ? 262 TYR   B CG  1 
ATOM   4829 C CD1 . TYR   B 1 261 ? -5.125  40.426  6.055   1.00 18.00 ? 262 TYR   B CD1 1 
ATOM   4830 C CD2 . TYR   B 1 261 ? -6.770  40.254  7.775   1.00 18.11 ? 262 TYR   B CD2 1 
ATOM   4831 C CE1 . TYR   B 1 261 ? -4.212  39.732  6.862   1.00 18.79 ? 262 TYR   B CE1 1 
ATOM   4832 C CE2 . TYR   B 1 261 ? -5.861  39.582  8.588   1.00 17.83 ? 262 TYR   B CE2 1 
ATOM   4833 C CZ  . TYR   B 1 261 ? -4.591  39.318  8.129   1.00 18.47 ? 262 TYR   B CZ  1 
ATOM   4834 O OH  . TYR   B 1 261 ? -3.674  38.647  8.912   1.00 17.84 ? 262 TYR   B OH  1 
ATOM   4835 N N   . GLN   B 1 262 ? -6.337  40.738  2.930   1.00 18.74 ? 263 GLN   B N   1 
ATOM   4836 C CA  . GLN   B 1 262 ? -5.271  40.214  2.086   1.00 20.27 ? 263 GLN   B CA  1 
ATOM   4837 C C   . GLN   B 1 262 ? -3.975  40.971  2.317   1.00 18.66 ? 263 GLN   B C   1 
ATOM   4838 O O   . GLN   B 1 262 ? -3.969  42.113  2.786   1.00 19.61 ? 263 GLN   B O   1 
ATOM   4839 C CB  . GLN   B 1 262 ? -5.650  40.240  0.595   1.00 23.31 ? 263 GLN   B CB  1 
ATOM   4840 C CG  . GLN   B 1 262 ? -5.689  41.598  -0.036  1.00 23.30 ? 263 GLN   B CG  1 
ATOM   4841 C CD  . GLN   B 1 262 ? -6.224  41.553  -1.472  1.00 27.43 ? 263 GLN   B CD  1 
ATOM   4842 O OE1 . GLN   B 1 262 ? -7.265  42.142  -1.774  1.00 26.41 ? 263 GLN   B OE1 1 
ATOM   4843 N NE2 . GLN   B 1 262 ? -5.515  40.846  -2.355  1.00 28.03 ? 263 GLN   B NE2 1 
ATOM   4844 N N   . VAL   B 1 263 ? -2.872  40.283  2.034   1.00 18.47 ? 264 VAL   B N   1 
ATOM   4845 C CA  . VAL   B 1 263 ? -1.539  40.873  1.969   1.00 18.80 ? 264 VAL   B CA  1 
ATOM   4846 C C   . VAL   B 1 263 ? -0.978  40.454  0.621   1.00 20.12 ? 264 VAL   B C   1 
ATOM   4847 O O   . VAL   B 1 263 ? -0.660  39.274  0.427   1.00 21.51 ? 264 VAL   B O   1 
ATOM   4848 C CB  . VAL   B 1 263 ? -0.623  40.403  3.106   1.00 19.22 ? 264 VAL   B CB  1 
ATOM   4849 C CG1 . VAL   B 1 263 ? 0.770   41.025  2.939   1.00 22.25 ? 264 VAL   B CG1 1 
ATOM   4850 C CG2 . VAL   B 1 263 ? -1.219  40.787  4.461   1.00 18.17 ? 264 VAL   B CG2 1 
ATOM   4851 N N   . ASN   B 1 264 ? -0.879  41.400  -0.316  1.00 20.81 ? 265 ASN   B N   1 
ATOM   4852 C CA  . ASN   B 1 264 ? -0.474  41.080  -1.698  1.00 24.58 ? 265 ASN   B CA  1 
ATOM   4853 C C   . ASN   B 1 264 ? -1.417  39.993  -2.218  1.00 25.49 ? 265 ASN   B C   1 
ATOM   4854 O O   . ASN   B 1 264 ? -2.640  40.150  -2.122  1.00 27.96 ? 265 ASN   B O   1 
ATOM   4855 C CB  . ASN   B 1 264 ? 1.009   40.721  -1.723  1.00 25.23 ? 265 ASN   B CB  1 
ATOM   4856 C CG  . ASN   B 1 264 ? 1.894   41.811  -1.159  1.00 27.36 ? 265 ASN   B CG  1 
ATOM   4857 O OD1 . ASN   B 1 264 ? 1.576   42.999  -1.245  1.00 30.37 ? 265 ASN   B OD1 1 
ATOM   4858 N ND2 . ASN   B 1 264 ? 3.019   41.410  -0.575  1.00 33.17 ? 265 ASN   B ND2 1 
ATOM   4859 N N   . THR   B 1 265 ? -0.913  38.876  -2.744  1.00 21.14 ? 266 THR   B N   1 
ATOM   4860 C CA  . THR   B 1 265 ? -1.772  37.857  -3.343  1.00 20.98 ? 266 THR   B CA  1 
ATOM   4861 C C   . THR   B 1 265 ? -2.290  36.828  -2.345  1.00 21.02 ? 266 THR   B C   1 
ATOM   4862 O O   . THR   B 1 265 ? -3.005  35.900  -2.748  1.00 22.11 ? 266 THR   B O   1 
ATOM   4863 C CB  . THR   B 1 265 ? -1.022  37.139  -4.470  1.00 24.35 ? 266 THR   B CB  1 
ATOM   4864 O OG1 . THR   B 1 265 ? 0.268   36.739  -3.989  1.00 22.78 ? 266 THR   B OG1 1 
ATOM   4865 C CG2 . THR   B 1 265 ? -0.854  38.065  -5.667  1.00 25.23 ? 266 THR   B CG2 1 
ATOM   4866 N N   . MET   B 1 266 ? -1.948  36.948  -1.065  1.00 18.46 ? 267 MET   B N   1 
ATOM   4867 C CA  . MET   B 1 266 ? -2.390  35.991  -0.055  1.00 19.39 ? 267 MET   B CA  1 
ATOM   4868 C C   . MET   B 1 266 ? -3.551  36.581  0.730   1.00 21.83 ? 267 MET   B C   1 
ATOM   4869 O O   . MET   B 1 266 ? -3.456  37.710  1.228   1.00 21.29 ? 267 MET   B O   1 
ATOM   4870 C CB  . MET   B 1 266 ? -1.245  35.630  0.896   1.00 19.01 ? 267 MET   B CB  1 
ATOM   4871 C CG  . MET   B 1 266 ? -1.634  34.609  1.967   1.00 19.51 ? 267 MET   B CG  1 
ATOM   4872 S SD  . MET   B 1 266 ? -0.321  34.365  3.178   1.00 26.15 ? 267 MET   B SD  1 
ATOM   4873 C CE  . MET   B 1 266 ? -0.516  35.829  4.194   1.00 21.00 ? 267 MET   B CE  1 
ATOM   4874 N N   . TYR   B 1 267 ? -4.639  35.822  0.834   1.00 17.86 ? 268 TYR   B N   1 
ATOM   4875 C CA  . TYR   B 1 267 ? -5.767  36.182  1.684   1.00 17.93 ? 268 TYR   B CA  1 
ATOM   4876 C C   . TYR   B 1 267 ? -5.648  35.404  2.983   1.00 17.48 ? 268 TYR   B C   1 
ATOM   4877 O O   . TYR   B 1 267 ? -5.364  34.201  2.969   1.00 17.89 ? 268 TYR   B O   1 
ATOM   4878 C CB  . TYR   B 1 267 ? -7.106  35.857  1.006   1.00 18.39 ? 268 TYR   B CB  1 
ATOM   4879 C CG  . TYR   B 1 267 ? -7.400  36.669  -0.235  1.00 21.69 ? 268 TYR   B CG  1 
ATOM   4880 C CD1 . TYR   B 1 267 ? -6.812  36.359  -1.451  1.00 23.57 ? 268 TYR   B CD1 1 
ATOM   4881 C CD2 . TYR   B 1 267 ? -8.265  37.754  -0.184  1.00 23.66 ? 268 TYR   B CD2 1 
ATOM   4882 C CE1 . TYR   B 1 267 ? -7.071  37.118  -2.580  1.00 26.88 ? 268 TYR   B CE1 1 
ATOM   4883 C CE2 . TYR   B 1 267 ? -8.533  38.511  -1.306  1.00 26.34 ? 268 TYR   B CE2 1 
ATOM   4884 C CZ  . TYR   B 1 267 ? -7.942  38.190  -2.500  1.00 25.42 ? 268 TYR   B CZ  1 
ATOM   4885 O OH  . TYR   B 1 267 ? -8.214  38.942  -3.624  1.00 34.03 ? 268 TYR   B OH  1 
ATOM   4886 N N   . GLN   B 1 268 ? -5.876  36.075  4.107   1.00 17.45 ? 269 GLN   B N   1 
ATOM   4887 C CA  . GLN   B 1 268 ? -5.761  35.410  5.404   1.00 17.17 ? 269 GLN   B CA  1 
ATOM   4888 C C   . GLN   B 1 268 ? -7.141  34.919  5.812   1.00 18.17 ? 269 GLN   B C   1 
ATOM   4889 O O   . GLN   B 1 268 ? -8.015  35.725  6.134   1.00 18.18 ? 269 GLN   B O   1 
ATOM   4890 C CB  . GLN   B 1 268 ? -5.199  36.359  6.460   1.00 17.14 ? 269 GLN   B CB  1 
ATOM   4891 C CG  . GLN   B 1 268 ? -5.059  35.718  7.836   1.00 16.99 ? 269 GLN   B CG  1 
ATOM   4892 C CD  . GLN   B 1 268 ? -4.022  34.612  7.848   1.00 16.65 ? 269 GLN   B CD  1 
ATOM   4893 O OE1 . GLN   B 1 268 ? -2.833  34.867  7.673   1.00 16.87 ? 269 GLN   B OE1 1 
ATOM   4894 N NE2 . GLN   B 1 268 ? -4.463  33.381  8.053   1.00 16.87 ? 269 GLN   B NE2 1 
ATOM   4895 N N   . ALA   B 1 269 ? -7.347  33.607  5.784   1.00 18.72 ? 270 ALA   B N   1 
ATOM   4896 C CA  . ALA   B 1 269 ? -8.566  33.043  6.341   1.00 20.12 ? 270 ALA   B CA  1 
ATOM   4897 C C   . ALA   B 1 269 ? -8.283  32.693  7.805   1.00 19.64 ? 270 ALA   B C   1 
ATOM   4898 O O   . ALA   B 1 269 ? -7.308  33.169  8.388   1.00 21.38 ? 270 ALA   B O   1 
ATOM   4899 C CB  . ALA   B 1 269 ? -9.037  31.854  5.483   1.00 19.47 ? 270 ALA   B CB  1 
ATOM   4900 N N   . LEU   B 1 270 ? -9.120  31.877  8.434   1.00 20.50 ? 271 LEU   B N   1 
ATOM   4901 C CA  . LEU   B 1 270 ? -8.857  31.454  9.807   1.00 22.87 ? 271 LEU   B CA  1 
ATOM   4902 C C   . LEU   B 1 270 ? -7.969  30.226  9.748   1.00 21.05 ? 271 LEU   B C   1 
ATOM   4903 O O   . LEU   B 1 270 ? -8.418  29.144  9.337   1.00 23.47 ? 271 LEU   B O   1 
ATOM   4904 C CB  . LEU   B 1 270 ? -10.139 31.145  10.575  1.00 23.17 ? 271 LEU   B CB  1 
ATOM   4905 C CG  . LEU   B 1 270 ? -11.180 32.204  10.868  1.00 30.03 ? 271 LEU   B CG  1 
ATOM   4906 C CD1 . LEU   B 1 270 ? -12.230 31.587  11.791  1.00 29.93 ? 271 LEU   B CD1 1 
ATOM   4907 C CD2 . LEU   B 1 270 ? -10.540 33.425  11.504  1.00 26.88 ? 271 LEU   B CD2 1 
ATOM   4908 N N   . GLY   B 1 271 ? -6.716  30.384  10.164  1.00 17.72 ? 272 GLY   B N   1 
ATOM   4909 C CA  . GLY   B 1 271 ? -5.736  29.326  10.042  1.00 20.50 ? 272 GLY   B CA  1 
ATOM   4910 C C   . GLY   B 1 271 ? -5.239  29.181  8.616   1.00 18.52 ? 272 GLY   B C   1 
ATOM   4911 O O   . GLY   B 1 271 ? -4.059  29.405  8.350   1.00 18.14 ? 272 GLY   B O   1 
ATOM   4912 N N   . TRP   B 1 272 ? -6.140  28.833  7.689   1.00 17.78 ? 273 TRP   B N   1 
ATOM   4913 C CA  . TRP   B 1 272 ? -5.753  28.662  6.289   1.00 18.99 ? 273 TRP   B CA  1 
ATOM   4914 C C   . TRP   B 1 272 ? -5.282  29.971  5.651   1.00 18.28 ? 273 TRP   B C   1 
ATOM   4915 O O   . TRP   B 1 272 ? -5.786  31.055  5.952   1.00 18.93 ? 273 TRP   B O   1 
ATOM   4916 C CB  . TRP   B 1 272 ? -6.928  28.132  5.475   1.00 18.38 ? 273 TRP   B CB  1 
ATOM   4917 C CG  . TRP   B 1 272 ? -7.387  26.737  5.820   1.00 19.58 ? 273 TRP   B CG  1 
ATOM   4918 C CD1 . TRP   B 1 272 ? -8.474  26.391  6.572   1.00 22.43 ? 273 TRP   B CD1 1 
ATOM   4919 C CD2 . TRP   B 1 272 ? -6.796  25.510  5.377   1.00 19.21 ? 273 TRP   B CD2 1 
ATOM   4920 N NE1 . TRP   B 1 272 ? -8.579  25.021  6.649   1.00 21.52 ? 273 TRP   B NE1 1 
ATOM   4921 C CE2 . TRP   B 1 272 ? -7.566  24.455  5.919   1.00 21.09 ? 273 TRP   B CE2 1 
ATOM   4922 C CE3 . TRP   B 1 272 ? -5.681  25.202  4.593   1.00 18.54 ? 273 TRP   B CE3 1 
ATOM   4923 C CZ2 . TRP   B 1 272 ? -7.262  23.106  5.689   1.00 18.21 ? 273 TRP   B CZ2 1 
ATOM   4924 C CZ3 . TRP   B 1 272 ? -5.379  23.867  4.362   1.00 16.63 ? 273 TRP   B CZ3 1 
ATOM   4925 C CH2 . TRP   B 1 272 ? -6.168  22.836  4.911   1.00 18.02 ? 273 TRP   B CH2 1 
ATOM   4926 N N   . GLU   B 1 273 ? -4.320  29.844  4.735   1.00 16.23 ? 274 GLU   B N   1 
ATOM   4927 C CA  . GLU   B 1 273 ? -4.016  30.882  3.755   1.00 17.53 ? 274 GLU   B CA  1 
ATOM   4928 C C   . GLU   B 1 273 ? -4.801  30.591  2.484   1.00 16.70 ? 274 GLU   B C   1 
ATOM   4929 O O   . GLU   B 1 273 ? -4.947  29.432  2.090   1.00 16.70 ? 274 GLU   B O   1 
ATOM   4930 C CB  . GLU   B 1 273 ? -2.521  30.922  3.444   1.00 18.12 ? 274 GLU   B CB  1 
ATOM   4931 C CG  . GLU   B 1 273 ? -1.656  31.103  4.680   1.00 20.88 ? 274 GLU   B CG  1 
ATOM   4932 C CD  . GLU   B 1 273 ? -0.174  30.876  4.414   1.00 25.30 ? 274 GLU   B CD  1 
ATOM   4933 O OE1 . GLU   B 1 273 ? 0.193   30.548  3.262   1.00 25.43 ? 274 GLU   B OE1 1 
ATOM   4934 O OE2 . GLU   B 1 273 ? 0.629   31.015  5.365   1.00 23.23 ? 274 GLU   B OE2 1 
ATOM   4935 N N   . GLU   B 1 274 ? -5.319  31.652  1.860   1.00 17.08 ? 275 GLU   B N   1 
ATOM   4936 C CA  . GLU   B 1 274 ? -6.280  31.553  0.772   1.00 18.22 ? 275 GLU   B CA  1 
ATOM   4937 C C   . GLU   B 1 274 ? -5.743  32.280  -0.454  1.00 17.89 ? 275 GLU   B C   1 
ATOM   4938 O O   . GLU   B 1 274 ? -5.115  33.332  -0.333  1.00 17.85 ? 275 GLU   B O   1 
ATOM   4939 C CB  . GLU   B 1 274 ? -7.621  32.153  1.195   1.00 18.84 ? 275 GLU   B CB  1 
ATOM   4940 C CG  . GLU   B 1 274 ? -8.635  32.331  0.077   1.00 19.31 ? 275 GLU   B CG  1 
ATOM   4941 C CD  . GLU   B 1 274 ? -9.961  32.826  0.603   1.00 30.00 ? 275 GLU   B CD  1 
ATOM   4942 O OE1 . GLU   B 1 274 ? -10.028 33.167  1.798   1.00 27.47 ? 275 GLU   B OE1 1 
ATOM   4943 O OE2 . GLU   B 1 274 ? -10.934 32.876  -0.171  1.00 33.59 ? 275 GLU   B OE2 1 
ATOM   4944 N N   . PHE   B 1 275 ? -5.982  31.709  -1.635  1.00 19.79 ? 276 PHE   B N   1 
ATOM   4945 C CA  . PHE   B 1 275 ? -5.500  32.285  -2.881  1.00 20.49 ? 276 PHE   B CA  1 
ATOM   4946 C C   . PHE   B 1 275 ? -6.587  32.194  -3.942  1.00 24.06 ? 276 PHE   B C   1 
ATOM   4947 O O   . PHE   B 1 275 ? -7.403  31.269  -3.940  1.00 21.66 ? 276 PHE   B O   1 
ATOM   4948 C CB  . PHE   B 1 275 ? -4.227  31.565  -3.360  1.00 19.39 ? 276 PHE   B CB  1 
ATOM   4949 C CG  . PHE   B 1 275 ? -3.173  31.464  -2.301  1.00 17.92 ? 276 PHE   B CG  1 
ATOM   4950 C CD1 . PHE   B 1 275 ? -3.155  30.381  -1.432  1.00 17.30 ? 276 PHE   B CD1 1 
ATOM   4951 C CD2 . PHE   B 1 275 ? -2.247  32.485  -2.125  1.00 18.87 ? 276 PHE   B CD2 1 
ATOM   4952 C CE1 . PHE   B 1 275 ? -2.201  30.296  -0.425  1.00 18.28 ? 276 PHE   B CE1 1 
ATOM   4953 C CE2 . PHE   B 1 275 ? -1.289  32.410  -1.127  1.00 17.62 ? 276 PHE   B CE2 1 
ATOM   4954 C CZ  . PHE   B 1 275 ? -1.267  31.313  -0.272  1.00 18.86 ? 276 PHE   B CZ  1 
ATOM   4955 N N   . SER   B 1 276 ? -6.594  33.158  -4.858  1.00 22.15 ? 277 SER   B N   1 
ATOM   4956 C CA  . SER   B 1 276 ? -7.411  32.995  -6.057  1.00 24.87 ? 277 SER   B CA  1 
ATOM   4957 C C   . SER   B 1 276 ? -6.905  31.809  -6.875  1.00 27.49 ? 277 SER   B C   1 
ATOM   4958 O O   . SER   B 1 276 ? -5.696  31.645  -7.073  1.00 23.23 ? 277 SER   B O   1 
ATOM   4959 C CB  . SER   B 1 276 ? -7.379  34.268  -6.898  1.00 25.86 ? 277 SER   B CB  1 
ATOM   4960 O OG  . SER   B 1 276 ? -8.226  34.140  -8.039  1.00 31.47 ? 277 SER   B OG  1 
ATOM   4961 N N   . TYR   B 1 277 ? -7.845  30.962  -7.351  1.00 27.75 ? 278 TYR   B N   1 
ATOM   4962 C CA  . TYR   B 1 277 ? -7.474  29.806  -8.156  1.00 28.41 ? 278 TYR   B CA  1 
ATOM   4963 C C   . TYR   B 1 277 ? -7.899  30.004  -9.611  1.00 30.17 ? 278 TYR   B C   1 
ATOM   4964 O O   . TYR   B 1 277 ? -9.004  30.492  -9.870  1.00 31.64 ? 278 TYR   B O   1 
ATOM   4965 C CB  . TYR   B 1 277 ? -8.109  28.523  -7.603  1.00 26.51 ? 278 TYR   B CB  1 
ATOM   4966 C CG  . TYR   B 1 277 ? -7.717  27.272  -8.360  1.00 31.16 ? 278 TYR   B CG  1 
ATOM   4967 C CD1 . TYR   B 1 277 ? -6.530  26.610  -8.078  1.00 28.33 ? 278 TYR   B CD1 1 
ATOM   4968 C CD2 . TYR   B 1 277 ? -8.528  26.767  -9.363  1.00 35.38 ? 278 TYR   B CD2 1 
ATOM   4969 C CE1 . TYR   B 1 277 ? -6.162  25.478  -8.773  1.00 33.91 ? 278 TYR   B CE1 1 
ATOM   4970 C CE2 . TYR   B 1 277 ? -8.173  25.641  -10.062 1.00 30.86 ? 278 TYR   B CE2 1 
ATOM   4971 C CZ  . TYR   B 1 277 ? -6.989  24.994  -9.764  1.00 35.88 ? 278 TYR   B CZ  1 
ATOM   4972 O OH  . TYR   B 1 277 ? -6.631  23.856  -10.459 1.00 38.77 ? 278 TYR   B OH  1 
ATOM   4973 N N   . PRO   B 1 278 ? -7.045  29.646  -10.581 1.00 30.32 ? 279 PRO   B N   1 
ATOM   4974 C CA  . PRO   B 1 278 ? -5.706  29.058  -10.428 1.00 29.01 ? 279 PRO   B CA  1 
ATOM   4975 C C   . PRO   B 1 278 ? -4.699  30.031  -9.826  1.00 27.49 ? 279 PRO   B C   1 
ATOM   4976 O O   . PRO   B 1 278 ? -4.721  31.235  -10.084 1.00 27.62 ? 279 PRO   B O   1 
ATOM   4977 C CB  . PRO   B 1 278 ? -5.333  28.667  -11.867 1.00 32.74 ? 279 PRO   B CB  1 
ATOM   4978 C CG  . PRO   B 1 278 ? -6.078  29.662  -12.714 1.00 31.42 ? 279 PRO   B CG  1 
ATOM   4979 C CD  . PRO   B 1 278 ? -7.390  29.852  -12.000 1.00 35.44 ? 279 PRO   B CD  1 
ATOM   4980 N N   . ALA   B 1 279 ? -3.828  29.514  -8.968  1.00 25.99 ? 280 ALA   B N   1 
ATOM   4981 C CA  . ALA   B 1 279 ? -2.727  30.276  -8.405  1.00 26.13 ? 280 ALA   B CA  1 
ATOM   4982 C C   . ALA   B 1 279 ? -1.425  29.822  -9.051  1.00 29.26 ? 280 ALA   B C   1 
ATOM   4983 O O   . ALA   B 1 279 ? -1.205  28.621  -9.256  1.00 28.45 ? 280 ALA   B O   1 
ATOM   4984 C CB  . ALA   B 1 279 ? -2.656  30.098  -6.885  1.00 27.52 ? 280 ALA   B CB  1 
ATOM   4985 N N   . THR   B 1 280 ? -0.574  30.781  -9.394  1.00 29.31 ? 281 THR   B N   1 
ATOM   4986 C CA  . THR   B 1 280 ? 0.737   30.420  -9.912  1.00 28.84 ? 281 THR   B CA  1 
ATOM   4987 C C   . THR   B 1 280 ? 1.590   29.842  -8.793  1.00 24.41 ? 281 THR   B C   1 
ATOM   4988 O O   . THR   B 1 280 ? 1.368   30.121  -7.611  1.00 23.52 ? 281 THR   B O   1 
ATOM   4989 C CB  . THR   B 1 280 ? 1.430   31.638  -10.520 1.00 30.06 ? 281 THR   B CB  1 
ATOM   4990 O OG1 . THR   B 1 280 ? 1.817   32.543  -9.473  1.00 27.95 ? 281 THR   B OG1 1 
ATOM   4991 C CG2 . THR   B 1 280 ? 0.489   32.362  -11.487 1.00 32.91 ? 281 THR   B CG2 1 
ATOM   4992 N N   . LEU   B 1 281 ? 2.568   29.009  -9.175  1.00 24.97 ? 282 LEU   B N   1 
ATOM   4993 C CA  . LEU   B 1 281 ? 3.519   28.493  -8.197  1.00 22.53 ? 282 LEU   B CA  1 
ATOM   4994 C C   . LEU   B 1 281 ? 4.219   29.631  -7.456  1.00 24.80 ? 282 LEU   B C   1 
ATOM   4995 O O   . LEU   B 1 281 ? 4.390   29.567  -6.233  1.00 23.21 ? 282 LEU   B O   1 
ATOM   4996 C CB  . LEU   B 1 281 ? 4.534   27.562  -8.879  1.00 24.17 ? 282 LEU   B CB  1 
ATOM   4997 C CG  . LEU   B 1 281 ? 5.722   27.129  -8.016  1.00 24.73 ? 282 LEU   B CG  1 
ATOM   4998 C CD1 . LEU   B 1 281 ? 5.277   26.283  -6.824  1.00 23.75 ? 282 LEU   B CD1 1 
ATOM   4999 C CD2 . LEU   B 1 281 ? 6.756   26.378  -8.852  1.00 32.30 ? 282 LEU   B CD2 1 
ATOM   5000 N N   . GLN   B 1 282 ? 4.573   30.709  -8.167  1.00 23.64 ? 283 GLN   B N   1 
ATOM   5001 C CA  . GLN   B 1 282 ? 5.271   31.817  -7.520  1.00 24.20 ? 283 GLN   B CA  1 
ATOM   5002 C C   . GLN   B 1 282 ? 4.407   32.469  -6.448  1.00 25.51 ? 283 GLN   B C   1 
ATOM   5003 O O   . GLN   B 1 282 ? 4.908   32.860  -5.385  1.00 23.85 ? 283 GLN   B O   1 
ATOM   5004 C CB  . GLN   B 1 282 ? 5.692   32.859  -8.564  1.00 29.23 ? 283 GLN   B CB  1 
ATOM   5005 C CG  . GLN   B 1 282 ? 6.667   33.878  -8.013  1.00 33.53 ? 283 GLN   B CG  1 
ATOM   5006 C CD  . GLN   B 1 282 ? 7.910   33.204  -7.487  1.00 36.97 ? 283 GLN   B CD  1 
ATOM   5007 O OE1 . GLN   B 1 282 ? 8.618   32.531  -8.229  1.00 37.46 ? 283 GLN   B OE1 1 
ATOM   5008 N NE2 . GLN   B 1 282 ? 8.168   33.359  -6.195  1.00 31.01 ? 283 GLN   B NE2 1 
ATOM   5009 N N   . THR   B 1 283 ? 3.111   32.616  -6.718  1.00 23.69 ? 284 THR   B N   1 
ATOM   5010 C CA  . THR   B 1 283 ? 2.198   33.124  -5.697  1.00 20.90 ? 284 THR   B CA  1 
ATOM   5011 C C   . THR   B 1 283 ? 2.239   32.253  -4.447  1.00 20.21 ? 284 THR   B C   1 
ATOM   5012 O O   . THR   B 1 283 ? 2.326   32.768  -3.327  1.00 21.66 ? 284 THR   B O   1 
ATOM   5013 C CB  . THR   B 1 283 ? 0.778   33.199  -6.258  1.00 21.52 ? 284 THR   B CB  1 
ATOM   5014 O OG1 . THR   B 1 283 ? 0.698   34.275  -7.201  1.00 22.97 ? 284 THR   B OG1 1 
ATOM   5015 C CG2 . THR   B 1 283 ? -0.249  33.417  -5.141  1.00 20.62 ? 284 THR   B CG2 1 
ATOM   5016 N N   . LEU   B 1 284 ? 2.225   30.930  -4.618  1.00 21.73 ? 285 LEU   B N   1 
ATOM   5017 C CA  . LEU   B 1 284 ? 2.212   30.056  -3.449  1.00 19.19 ? 285 LEU   B CA  1 
ATOM   5018 C C   . LEU   B 1 284 ? 3.543   30.111  -2.711  1.00 21.88 ? 285 LEU   B C   1 
ATOM   5019 O O   . LEU   B 1 284 ? 3.574   30.079  -1.477  1.00 21.14 ? 285 LEU   B O   1 
ATOM   5020 C CB  . LEU   B 1 284 ? 1.873   28.621  -3.867  1.00 19.16 ? 285 LEU   B CB  1 
ATOM   5021 C CG  . LEU   B 1 284 ? 0.504   28.491  -4.551  1.00 17.65 ? 285 LEU   B CG  1 
ATOM   5022 C CD1 . LEU   B 1 284 ? 0.272   27.048  -4.979  1.00 23.47 ? 285 LEU   B CD1 1 
ATOM   5023 C CD2 . LEU   B 1 284 ? -0.595  28.931  -3.580  1.00 19.04 ? 285 LEU   B CD2 1 
ATOM   5024 N N   . LEU   B 1 285 ? 4.650   30.218  -3.449  1.00 21.34 ? 286 LEU   B N   1 
ATOM   5025 C CA  . LEU   B 1 285 ? 5.958   30.375  -2.819  1.00 22.14 ? 286 LEU   B CA  1 
ATOM   5026 C C   . LEU   B 1 285 ? 6.081   31.715  -2.098  1.00 22.73 ? 286 LEU   B C   1 
ATOM   5027 O O   . LEU   B 1 285 ? 6.673   31.791  -1.012  1.00 24.25 ? 286 LEU   B O   1 
ATOM   5028 C CB  . LEU   B 1 285 ? 7.057   30.241  -3.871  1.00 23.16 ? 286 LEU   B CB  1 
ATOM   5029 C CG  . LEU   B 1 285 ? 7.127   28.873  -4.557  1.00 24.05 ? 286 LEU   B CG  1 
ATOM   5030 C CD1 . LEU   B 1 285 ? 8.126   28.931  -5.704  1.00 27.39 ? 286 LEU   B CD1 1 
ATOM   5031 C CD2 . LEU   B 1 285 ? 7.513   27.768  -3.570  1.00 23.28 ? 286 LEU   B CD2 1 
ATOM   5032 N N   . ASP   B 1 286 ? 5.535   32.782  -2.692  1.00 23.26 ? 287 ASP   B N   1 
ATOM   5033 C CA  . ASP   B 1 286 ? 5.624   34.105  -2.075  1.00 21.85 ? 287 ASP   B CA  1 
ATOM   5034 C C   . ASP   B 1 286 ? 4.945   34.130  -0.715  1.00 23.86 ? 287 ASP   B C   1 
ATOM   5035 O O   . ASP   B 1 286 ? 5.331   34.916  0.163   1.00 25.62 ? 287 ASP   B O   1 
ATOM   5036 C CB  . ASP   B 1 286 ? 4.994   35.167  -2.983  1.00 23.57 ? 287 ASP   B CB  1 
ATOM   5037 C CG  . ASP   B 1 286 ? 5.818   35.450  -4.237  1.00 30.11 ? 287 ASP   B CG  1 
ATOM   5038 O OD1 . ASP   B 1 286 ? 6.988   35.023  -4.308  1.00 31.04 ? 287 ASP   B OD1 1 
ATOM   5039 O OD2 . ASP   B 1 286 ? 5.285   36.111  -5.158  1.00 32.15 ? 287 ASP   B OD2 1 
ATOM   5040 N N   . SER   B 1 287 ? 3.930   33.281  -0.525  1.00 21.43 ? 288 SER   B N   1 
ATOM   5041 C CA  . SER   B 1 287 ? 3.217   33.246  0.743   1.00 22.27 ? 288 SER   B CA  1 
ATOM   5042 C C   . SER   B 1 287 ? 4.118   32.823  1.894   1.00 23.35 ? 288 SER   B C   1 
ATOM   5043 O O   . SER   B 1 287 ? 3.803   33.129  3.047   1.00 24.89 ? 288 SER   B O   1 
ATOM   5044 C CB  . SER   B 1 287 ? 2.010   32.307  0.649   1.00 19.50 ? 288 SER   B CB  1 
ATOM   5045 O OG  . SER   B 1 287 ? 2.416   30.943  0.654   1.00 20.39 ? 288 SER   B OG  1 
ATOM   5046 N N   . ASN   B 1 288 ? 5.235   32.144  1.615   1.00 21.04 ? 289 ASN   B N   1 
ATOM   5047 C CA  . ASN   B 1 288 ? 6.152   31.715  2.662   1.00 22.31 ? 289 ASN   B CA  1 
ATOM   5048 C C   . ASN   B 1 288 ? 7.436   32.540  2.678   1.00 25.16 ? 289 ASN   B C   1 
ATOM   5049 O O   . ASN   B 1 288 ? 8.444   32.109  3.246   1.00 26.85 ? 289 ASN   B O   1 
ATOM   5050 C CB  . ASN   B 1 288 ? 6.468   30.223  2.513   1.00 24.11 ? 289 ASN   B CB  1 
ATOM   5051 C CG  . ASN   B 1 288 ? 7.140   29.643  3.748   1.00 28.17 ? 289 ASN   B CG  1 
ATOM   5052 O OD1 . ASN   B 1 288 ? 8.317   29.284  3.716   1.00 29.07 ? 289 ASN   B OD1 1 
ATOM   5053 N ND2 . ASN   B 1 288 ? 6.400   29.583  4.854   1.00 29.11 ? 289 ASN   B ND2 1 
ATOM   5054 N N   . SER   B 1 289 ? 7.418   33.725  2.079   1.00 24.64 ? 290 SER   B N   1 
ATOM   5055 C CA  . SER   B 1 289 ? 8.610   34.557  2.075   1.00 25.28 ? 290 SER   B CA  1 
ATOM   5056 C C   . SER   B 1 289 ? 8.948   35.026  3.491   1.00 22.33 ? 290 SER   B C   1 
ATOM   5057 O O   . SER   B 1 289 ? 8.091   35.123  4.367   1.00 25.02 ? 290 SER   B O   1 
ATOM   5058 C CB  . SER   B 1 289 ? 8.408   35.756  1.157   1.00 26.15 ? 290 SER   B CB  1 
ATOM   5059 O OG  . SER   B 1 289 ? 7.493   36.679  1.723   1.00 27.17 ? 290 SER   B OG  1 
ATOM   5060 N N   . GLU   B 1 290 ? 10.230  35.348  3.705   1.00 26.85 ? 291 GLU   B N   1 
ATOM   5061 C CA  . GLU   B 1 290 ? 10.635  35.859  5.011   1.00 26.02 ? 291 GLU   B CA  1 
ATOM   5062 C C   . GLU   B 1 290 ? 9.880   37.137  5.356   1.00 24.52 ? 291 GLU   B C   1 
ATOM   5063 O O   . GLU   B 1 290 ? 9.523   37.368  6.519   1.00 23.80 ? 291 GLU   B O   1 
ATOM   5064 C CB  . GLU   B 1 290 ? 12.144  36.103  5.042   1.00 35.63 ? 291 GLU   B CB  1 
ATOM   5065 C CG  . GLU   B 1 290 ? 12.698  36.158  6.452   1.00 39.86 ? 291 GLU   B CG  1 
ATOM   5066 C CD  . GLU   B 1 290 ? 13.758  37.225  6.639   1.00 49.64 ? 291 GLU   B CD  1 
ATOM   5067 O OE1 . GLU   B 1 290 ? 14.377  37.650  5.634   1.00 54.58 ? 291 GLU   B OE1 1 
ATOM   5068 O OE2 . GLU   B 1 290 ? 13.972  37.640  7.801   1.00 53.42 ? 291 GLU   B OE2 1 
ATOM   5069 N N   . GLN   B 1 291 ? 9.620   37.977  4.353   1.00 26.66 ? 292 GLN   B N   1 
ATOM   5070 C CA  . GLN   B 1 291 ? 8.850   39.195  4.597   1.00 25.89 ? 292 GLN   B CA  1 
ATOM   5071 C C   . GLN   B 1 291 ? 7.461   38.871  5.138   1.00 24.30 ? 292 GLN   B C   1 
ATOM   5072 O O   . GLN   B 1 291 ? 7.012   39.481  6.113   1.00 25.81 ? 292 GLN   B O   1 
ATOM   5073 C CB  . GLN   B 1 291 ? 8.754   40.029  3.318   1.00 28.20 ? 292 GLN   B CB  1 
ATOM   5074 C CG  . GLN   B 1 291 ? 7.951   41.330  3.455   1.00 25.66 ? 292 GLN   B CG  1 
ATOM   5075 C CD  . GLN   B 1 291 ? 8.562   42.333  4.418   1.00 34.00 ? 292 GLN   B CD  1 
ATOM   5076 O OE1 . GLN   B 1 291 ? 9.784   42.403  4.576   1.00 34.90 ? 292 GLN   B OE1 1 
ATOM   5077 N NE2 . GLN   B 1 291 ? 7.709   43.124  5.066   1.00 30.10 ? 292 GLN   B NE2 1 
ATOM   5078 N N   . ILE   B 1 292 ? 6.781   37.879  4.551   1.00 24.98 ? 293 ILE   B N   1 
ATOM   5079 C CA  . ILE   B 1 292 ? 5.418   37.585  4.988   1.00 23.45 ? 293 ILE   B CA  1 
ATOM   5080 C C   . ILE   B 1 292 ? 5.420   36.890  6.344   1.00 20.76 ? 293 ILE   B C   1 
ATOM   5081 O O   . ILE   B 1 292 ? 4.573   37.171  7.197   1.00 21.75 ? 293 ILE   B O   1 
ATOM   5082 C CB  . ILE   B 1 292 ? 4.670   36.738  3.938   1.00 24.13 ? 293 ILE   B CB  1 
ATOM   5083 C CG1 . ILE   B 1 292 ? 4.423   37.543  2.663   1.00 28.37 ? 293 ILE   B CG1 1 
ATOM   5084 C CG2 . ILE   B 1 292 ? 3.330   36.234  4.507   1.00 21.44 ? 293 ILE   B CG2 1 
ATOM   5085 C CD1 . ILE   B 1 292 ? 3.509   38.746  2.852   1.00 29.42 ? 293 ILE   B CD1 1 
ATOM   5086 N N   . VAL   B 1 293 ? 6.342   35.945  6.548   1.00 21.96 ? 294 VAL   B N   1 
ATOM   5087 C CA  . VAL   B 1 293 ? 6.299   35.075  7.723   1.00 22.05 ? 294 VAL   B CA  1 
ATOM   5088 C C   . VAL   B 1 293 ? 6.902   35.751  8.946   1.00 24.72 ? 294 VAL   B C   1 
ATOM   5089 O O   . VAL   B 1 293 ? 6.432   35.549  10.072  1.00 25.65 ? 294 VAL   B O   1 
ATOM   5090 C CB  . VAL   B 1 293 ? 7.013   33.744  7.418   1.00 22.62 ? 294 VAL   B CB  1 
ATOM   5091 C CG1 . VAL   B 1 293 ? 7.046   32.861  8.665   1.00 27.26 ? 294 VAL   B CG1 1 
ATOM   5092 C CG2 . VAL   B 1 293 ? 6.342   33.034  6.248   1.00 22.03 ? 294 VAL   B CG2 1 
ATOM   5093 N N   . MET   B 1 294 ? 7.965   36.539  8.760   1.00 26.98 ? 295 MET   B N   1 
ATOM   5094 C CA  . MET   B 1 294 ? 8.752   37.027  9.882   1.00 29.71 ? 295 MET   B CA  1 
ATOM   5095 C C   . MET   B 1 294 ? 8.584   38.515  10.180  1.00 30.05 ? 295 MET   B C   1 
ATOM   5096 O O   . MET   B 1 294 ? 9.038   38.965  11.239  1.00 32.40 ? 295 MET   B O   1 
ATOM   5097 C CB  . MET   B 1 294 ? 10.242  36.723  9.639   1.00 33.69 ? 295 MET   B CB  1 
ATOM   5098 C CG  . MET   B 1 294 ? 10.560  35.233  9.523   1.00 34.32 ? 295 MET   B CG  1 
ATOM   5099 S SD  . MET   B 1 294 ? 10.017  34.284  10.964  1.00 44.10 ? 295 MET   B SD  1 
ATOM   5100 C CE  . MET   B 1 294 ? 10.976  35.034  12.279  1.00 39.75 ? 295 MET   B CE  1 
ATOM   5101 N N   . LYS   B 1 295 ? 7.951   39.287  9.304   1.00 28.26 ? 296 LYS   B N   1 
ATOM   5102 C CA  . LYS   B 1 295 ? 7.869   40.732  9.464   1.00 28.73 ? 296 LYS   B CA  1 
ATOM   5103 C C   . LYS   B 1 295 ? 6.416   41.196  9.529   1.00 28.26 ? 296 LYS   B C   1 
ATOM   5104 O O   . LYS   B 1 295 ? 5.502   40.491  9.069   1.00 24.97 ? 296 LYS   B O   1 
ATOM   5105 C CB  . LYS   B 1 295 ? 8.590   41.457  8.312   1.00 29.87 ? 296 LYS   B CB  1 
ATOM   5106 C CG  . LYS   B 1 295 ? 10.049  41.027  8.081   1.00 36.49 ? 296 LYS   B CG  1 
ATOM   5107 C CD  . LYS   B 1 295 ? 10.938  41.402  9.265   1.00 40.26 ? 296 LYS   B CD  1 
ATOM   5108 C CE  . LYS   B 1 295 ? 12.386  40.965  9.049   1.00 41.22 ? 296 LYS   B CE  1 
ATOM   5109 N NZ  . LYS   B 1 295 ? 13.029  41.662  7.897   1.00 44.18 ? 296 LYS   B NZ  1 
ATOM   5110 N N   . PRO   B 1 296 ? 6.161   42.357  10.139  1.00 26.92 ? 297 PRO   B N   1 
ATOM   5111 C CA  . PRO   B 1 296 ? 4.821   42.953  10.048  1.00 23.87 ? 297 PRO   B CA  1 
ATOM   5112 C C   . PRO   B 1 296 ? 4.552   43.460  8.642   1.00 25.24 ? 297 PRO   B C   1 
ATOM   5113 O O   . PRO   B 1 296 ? 5.430   44.029  7.990   1.00 26.62 ? 297 PRO   B O   1 
ATOM   5114 C CB  . PRO   B 1 296 ? 4.862   44.117  11.050  1.00 28.68 ? 297 PRO   B CB  1 
ATOM   5115 C CG  . PRO   B 1 296 ? 6.088   43.907  11.875  1.00 31.24 ? 297 PRO   B CG  1 
ATOM   5116 C CD  . PRO   B 1 296 ? 7.051   43.111  11.038  1.00 29.76 ? 297 PRO   B CD  1 
ATOM   5117 N N   . ASN   B 1 297 ? 3.310   43.289  8.192   1.00 20.56 ? 298 ASN   B N   1 
ATOM   5118 C CA  . ASN   B 1 297 ? 2.888   43.757  6.877   1.00 20.29 ? 298 ASN   B CA  1 
ATOM   5119 C C   . ASN   B 1 297 ? 1.516   44.402  6.975   1.00 19.61 ? 298 ASN   B C   1 
ATOM   5120 O O   . ASN   B 1 297 ? 0.594   43.819  7.556   1.00 19.39 ? 298 ASN   B O   1 
ATOM   5121 C CB  . ASN   B 1 297 ? 2.841   42.610  5.858   1.00 20.52 ? 298 ASN   B CB  1 
ATOM   5122 C CG  . ASN   B 1 297 ? 4.202   42.021  5.589   1.00 25.63 ? 298 ASN   B CG  1 
ATOM   5123 O OD1 . ASN   B 1 297 ? 4.959   42.534  4.758   1.00 27.09 ? 298 ASN   B OD1 1 
ATOM   5124 N ND2 . ASN   B 1 297 ? 4.531   40.951  6.298   1.00 23.30 ? 298 ASN   B ND2 1 
ATOM   5125 N N   . LYS   B 1 298 ? 1.387   45.597  6.386   1.00 20.11 ? 299 LYS   B N   1 
ATOM   5126 C CA  . LYS   B 1 298 ? 0.104   46.287  6.312   1.00 20.12 ? 299 LYS   B CA  1 
ATOM   5127 C C   . LYS   B 1 298 ? -0.917  45.426  5.578   1.00 19.90 ? 299 LYS   B C   1 
ATOM   5128 O O   . LYS   B 1 298 ? -0.621  44.861  4.524   1.00 20.37 ? 299 LYS   B O   1 
ATOM   5129 C CB  . LYS   B 1 298 ? 0.274   47.630  5.597   1.00 20.81 ? 299 LYS   B CB  1 
ATOM   5130 C CG  . LYS   B 1 298 ? -0.948  48.522  5.690   1.00 21.49 ? 299 LYS   B CG  1 
ATOM   5131 C CD  . LYS   B 1 298 ? -0.782  49.774  4.827   1.00 21.68 ? 299 LYS   B CD  1 
ATOM   5132 C CE  . LYS   B 1 298 ? -2.047  50.628  4.805   1.00 27.71 ? 299 LYS   B CE  1 
ATOM   5133 N NZ  . LYS   B 1 298 ? -1.914  51.869  3.973   1.00 29.10 ? 299 LYS   B NZ  1 
ATOM   5134 N N   . VAL   B 1 299 ? -2.112  45.301  6.146   1.00 19.44 ? 300 VAL   B N   1 
ATOM   5135 C CA  . VAL   B 1 299 ? -3.150  44.502  5.515   1.00 19.50 ? 300 VAL   B CA  1 
ATOM   5136 C C   . VAL   B 1 299 ? -4.019  45.389  4.634   1.00 19.59 ? 300 VAL   B C   1 
ATOM   5137 O O   . VAL   B 1 299 ? -4.121  46.614  4.817   1.00 20.41 ? 300 VAL   B O   1 
ATOM   5138 C CB  . VAL   B 1 299 ? -4.014  43.740  6.546   1.00 18.81 ? 300 VAL   B CB  1 
ATOM   5139 C CG1 . VAL   B 1 299 ? -3.133  42.981  7.530   1.00 20.12 ? 300 VAL   B CG1 1 
ATOM   5140 C CG2 . VAL   B 1 299 ? -4.929  44.695  7.285   1.00 20.28 ? 300 VAL   B CG2 1 
ATOM   5141 N N   . THR   B 1 300 ? -4.649  44.745  3.654   1.00 19.85 ? 301 THR   B N   1 
ATOM   5142 C CA  . THR   B 1 300 ? -5.639  45.357  2.774   1.00 22.97 ? 301 THR   B CA  1 
ATOM   5143 C C   . THR   B 1 300 ? -6.997  44.746  3.095   1.00 20.94 ? 301 THR   B C   1 
ATOM   5144 O O   . THR   B 1 300 ? -7.182  43.527  2.963   1.00 19.75 ? 301 THR   B O   1 
ATOM   5145 C CB  . THR   B 1 300 ? -5.277  45.129  1.303   1.00 23.34 ? 301 THR   B CB  1 
ATOM   5146 O OG1 . THR   B 1 300 ? -4.006  45.730  1.026   1.00 31.19 ? 301 THR   B OG1 1 
ATOM   5147 C CG2 . THR   B 1 300 ? -6.312  45.746  0.387   1.00 27.37 ? 301 THR   B CG2 1 
ATOM   5148 N N   . ALA   B 1 301 ? -7.930  45.582  3.551   1.00 21.20 ? 302 ALA   B N   1 
ATOM   5149 C CA  . ALA   B 1 301 ? -9.295  45.123  3.755   1.00 23.05 ? 302 ALA   B CA  1 
ATOM   5150 C C   . ALA   B 1 301 ? -9.873  44.679  2.420   1.00 25.85 ? 302 ALA   B C   1 
ATOM   5151 O O   . ALA   B 1 301 ? -9.583  45.266  1.376   1.00 27.30 ? 302 ALA   B O   1 
ATOM   5152 C CB  . ALA   B 1 301 ? -10.146 46.241  4.369   1.00 23.83 ? 302 ALA   B CB  1 
ATOM   5153 N N   . ILE   B 1 302 ? -10.670 43.623  2.441   1.00 27.77 ? 303 ILE   B N   1 
ATOM   5154 C CA  . ILE   B 1 302 ? -11.190 43.056  1.206   1.00 31.37 ? 303 ILE   B CA  1 
ATOM   5155 C C   . ILE   B 1 302 ? -12.681 43.332  1.113   1.00 34.99 ? 303 ILE   B C   1 
ATOM   5156 O O   . ILE   B 1 302 ? -13.411 43.241  2.109   1.00 36.32 ? 303 ILE   B O   1 
ATOM   5157 C CB  . ILE   B 1 302 ? -10.875 41.553  1.094   1.00 28.90 ? 303 ILE   B CB  1 
ATOM   5158 C CG1 . ILE   B 1 302 ? -11.362 40.781  2.325   1.00 30.11 ? 303 ILE   B CG1 1 
ATOM   5159 C CG2 . ILE   B 1 302 ? -9.370  41.373  0.906   1.00 26.90 ? 303 ILE   B CG2 1 
ATOM   5160 C CD1 . ILE   B 1 302 ? -11.059 39.281  2.244   1.00 28.02 ? 303 ILE   B CD1 1 
ATOM   5161 N N   . SER   B 1 303 ? -13.115 43.723  -0.084  1.00 38.11 ? 304 SER   B N   1 
ATOM   5162 C CA  . SER   B 1 303 ? -14.529 43.874  -0.387  1.00 45.66 ? 304 SER   B CA  1 
ATOM   5163 C C   . SER   B 1 303 ? -15.151 42.572  -0.857  1.00 47.33 ? 304 SER   B C   1 
ATOM   5164 O O   . SER   B 1 303 ? -16.366 42.386  -0.719  1.00 49.45 ? 304 SER   B O   1 
ATOM   5165 C CB  . SER   B 1 303 ? -14.726 44.945  -1.464  1.00 49.08 ? 304 SER   B CB  1 
ATOM   5166 O OG  . SER   B 1 303 ? -14.049 44.580  -2.654  1.00 52.96 ? 304 SER   B OG  1 
ATOM   5167 N N   . LYS   B 1 304 ? -14.338 41.667  -1.395  1.00 42.18 ? 305 LYS   B N   1 
ATOM   5168 C CA  . LYS   B 1 304 ? -14.811 40.370  -1.846  1.00 45.80 ? 305 LYS   B CA  1 
ATOM   5169 C C   . LYS   B 1 304 ? -13.675 39.373  -1.683  1.00 37.40 ? 305 LYS   B C   1 
ATOM   5170 O O   . LYS   B 1 304 ? -12.507 39.750  -1.566  1.00 36.64 ? 305 LYS   B O   1 
ATOM   5171 C CB  . LYS   B 1 304 ? -15.297 40.428  -3.305  1.00 45.37 ? 305 LYS   B CB  1 
ATOM   5172 C CG  . LYS   B 1 304 ? -14.323 41.093  -4.302  1.00 46.97 ? 305 LYS   B CG  1 
ATOM   5173 C CD  . LYS   B 1 304 ? -13.256 40.112  -4.785  1.00 51.79 ? 305 LYS   B CD  1 
ATOM   5174 C CE  . LYS   B 1 304 ? -12.357 40.694  -5.867  1.00 58.14 ? 305 LYS   B CE  1 
ATOM   5175 N NZ  . LYS   B 1 304 ? -11.393 39.643  -6.332  1.00 53.68 ? 305 LYS   B NZ  1 
ATOM   5176 N N   . GLU   B 1 305 ? -14.031 38.112  -1.643  1.00 42.25 ? 306 GLU   B N   1 
ATOM   5177 C CA  . GLU   B 1 305 ? -13.024 37.085  -1.822  1.00 37.27 ? 306 GLU   B CA  1 
ATOM   5178 C C   . GLU   B 1 305 ? -12.896 36.767  -3.304  1.00 37.76 ? 306 GLU   B C   1 
ATOM   5179 O O   . GLU   B 1 305 ? -13.738 37.178  -4.110  1.00 35.40 ? 306 GLU   B O   1 
ATOM   5180 C CB  . GLU   B 1 305 ? -13.405 35.833  -1.032  1.00 33.01 ? 306 GLU   B CB  1 
ATOM   5181 C CG  . GLU   B 1 305 ? -13.509 36.051  0.462   1.00 30.71 ? 306 GLU   B CG  1 
ATOM   5182 C CD  . GLU   B 1 305 ? -13.960 34.802  1.192   1.00 34.84 ? 306 GLU   B CD  1 
ATOM   5183 O OE1 . GLU   B 1 305 ? -13.225 33.792  1.161   1.00 32.87 ? 306 GLU   B OE1 1 
ATOM   5184 O OE2 . GLU   B 1 305 ? -15.059 34.828  1.784   1.00 35.66 ? 306 GLU   B OE2 1 
ATOM   5185 N N   . PRO   B 1 306 ? -11.847 36.057  -3.713  1.00 35.60 ? 307 PRO   B N   1 
ATOM   5186 C CA  . PRO   B 1 306 ? -11.822 35.544  -5.087  1.00 34.97 ? 307 PRO   B CA  1 
ATOM   5187 C C   . PRO   B 1 306 ? -13.043 34.678  -5.354  1.00 34.88 ? 307 PRO   B C   1 
ATOM   5188 O O   . PRO   B 1 306 ? -13.571 34.014  -4.457  1.00 37.94 ? 307 PRO   B O   1 
ATOM   5189 C CB  . PRO   B 1 306 ? -10.529 34.722  -5.141  1.00 32.78 ? 307 PRO   B CB  1 
ATOM   5190 C CG  . PRO   B 1 306 ? -9.669  35.301  -4.060  1.00 31.96 ? 307 PRO   B CG  1 
ATOM   5191 C CD  . PRO   B 1 306 ? -10.611 35.728  -2.975  1.00 32.45 ? 307 PRO   B CD  1 
ATOM   5192 N N   . SER   B 1 307 ? -13.493 34.692  -6.610  1.00 35.84 ? 308 SER   B N   1 
ATOM   5193 C CA  . SER   B 1 307 ? -14.626 33.858  -6.997  1.00 34.95 ? 308 SER   B CA  1 
ATOM   5194 C C   . SER   B 1 307 ? -14.297 32.376  -6.855  1.00 35.74 ? 308 SER   B C   1 
ATOM   5195 O O   . SER   B 1 307 ? -15.154 31.577  -6.460  1.00 37.27 ? 308 SER   B O   1 
ATOM   5196 C CB  . SER   B 1 307 ? -15.036 34.169  -8.435  1.00 37.43 ? 308 SER   B CB  1 
ATOM   5197 O OG  . SER   B 1 307 ? -14.971 35.562  -8.680  1.00 48.25 ? 308 SER   B OG  1 
ATOM   5198 N N   . VAL   B 1 308 ? -13.069 31.989  -7.194  1.00 33.05 ? 309 VAL   B N   1 
ATOM   5199 C CA  . VAL   B 1 308 ? -12.609 30.606  -7.131  1.00 31.16 ? 309 VAL   B CA  1 
ATOM   5200 C C   . VAL   B 1 308 ? -11.331 30.591  -6.300  1.00 29.00 ? 309 VAL   B C   1 
ATOM   5201 O O   . VAL   B 1 308 ? -10.429 31.405  -6.530  1.00 27.94 ? 309 VAL   B O   1 
ATOM   5202 C CB  . VAL   B 1 308 ? -12.365 30.024  -8.540  1.00 32.75 ? 309 VAL   B CB  1 
ATOM   5203 C CG1 . VAL   B 1 308 ? -12.085 28.527  -8.471  1.00 32.54 ? 309 VAL   B CG1 1 
ATOM   5204 C CG2 . VAL   B 1 308 ? -13.552 30.304  -9.455  1.00 37.07 ? 309 VAL   B CG2 1 
ATOM   5205 N N   . LYS   B 1 309 ? -11.254 29.679  -5.334  1.00 28.23 ? 310 LYS   B N   1 
ATOM   5206 C CA  . LYS   B 1 309 ? -10.248 29.765  -4.280  1.00 24.04 ? 310 LYS   B CA  1 
ATOM   5207 C C   . LYS   B 1 309 ? -9.515  28.444  -4.109  1.00 24.44 ? 310 LYS   B C   1 
ATOM   5208 O O   . LYS   B 1 309 ? -10.024 27.374  -4.453  1.00 25.48 ? 310 LYS   B O   1 
ATOM   5209 C CB  . LYS   B 1 309 ? -10.882 30.157  -2.941  1.00 27.75 ? 310 LYS   B CB  1 
ATOM   5210 C CG  . LYS   B 1 309 ? -11.576 31.511  -2.986  1.00 29.85 ? 310 LYS   B CG  1 
ATOM   5211 C CD  . LYS   B 1 309 ? -12.816 31.545  -2.105  1.00 33.59 ? 310 LYS   B CD  1 
ATOM   5212 C CE  . LYS   B 1 309 ? -13.971 30.794  -2.740  1.00 37.84 ? 310 LYS   B CE  1 
ATOM   5213 N NZ  . LYS   B 1 309 ? -15.274 31.240  -2.181  1.00 38.92 ? 310 LYS   B NZ  1 
ATOM   5214 N N   . MET   B 1 310 ? -8.313  28.542  -3.544  1.00 21.45 ? 311 MET   B N   1 
ATOM   5215 C CA  . MET   B 1 310 ? -7.572  27.396  -3.032  1.00 23.24 ? 311 MET   B CA  1 
ATOM   5216 C C   . MET   B 1 310 ? -6.912  27.810  -1.721  1.00 20.27 ? 311 MET   B C   1 
ATOM   5217 O O   . MET   B 1 310 ? -6.829  29.000  -1.395  1.00 18.72 ? 311 MET   B O   1 
ATOM   5218 C CB  . MET   B 1 310 ? -6.517  26.881  -4.028  1.00 22.57 ? 311 MET   B CB  1 
ATOM   5219 C CG  . MET   B 1 310 ? -5.214  27.718  -4.093  1.00 22.93 ? 311 MET   B CG  1 
ATOM   5220 S SD  . MET   B 1 310 ? -3.975  26.984  -5.202  1.00 29.37 ? 311 MET   B SD  1 
ATOM   5221 C CE  . MET   B 1 310 ? -3.267  25.746  -4.115  1.00 23.65 ? 311 MET   B CE  1 
ATOM   5222 N N   . TYR   B 1 311 ? -6.462  26.816  -0.958  1.00 17.16 ? 312 TYR   B N   1 
ATOM   5223 C CA  . TYR   B 1 311 ? -6.023  27.033  0.411   1.00 16.40 ? 312 TYR   B CA  1 
ATOM   5224 C C   . TYR   B 1 311 ? -4.817  26.158  0.692   1.00 17.71 ? 312 TYR   B C   1 
ATOM   5225 O O   . TYR   B 1 311 ? -4.753  25.026  0.208   1.00 18.84 ? 312 TYR   B O   1 
ATOM   5226 C CB  . TYR   B 1 311 ? -7.125  26.667  1.416   1.00 17.78 ? 312 TYR   B CB  1 
ATOM   5227 C CG  . TYR   B 1 311 ? -8.409  27.434  1.225   1.00 20.02 ? 312 TYR   B CG  1 
ATOM   5228 C CD1 . TYR   B 1 311 ? -9.349  27.025  0.289   1.00 19.06 ? 312 TYR   B CD1 1 
ATOM   5229 C CD2 . TYR   B 1 311 ? -8.679  28.569  1.982   1.00 20.27 ? 312 TYR   B CD2 1 
ATOM   5230 C CE1 . TYR   B 1 311 ? -10.522 27.731  0.099   1.00 22.05 ? 312 TYR   B CE1 1 
ATOM   5231 C CE2 . TYR   B 1 311 ? -9.857  29.284  1.800   1.00 22.37 ? 312 TYR   B CE2 1 
ATOM   5232 C CZ  . TYR   B 1 311 ? -10.779 28.851  0.863   1.00 23.45 ? 312 TYR   B CZ  1 
ATOM   5233 O OH  . TYR   B 1 311 ? -11.955 29.541  0.662   1.00 25.01 ? 312 TYR   B OH  1 
ATOM   5234 N N   . HIS   B 1 312 ? -3.880  26.658  1.505   1.00 15.50 ? 313 HIS   B N   1 
ATOM   5235 C CA  . HIS   B 1 312 ? -2.800  25.785  1.960   1.00 15.14 ? 313 HIS   B CA  1 
ATOM   5236 C C   . HIS   B 1 312 ? -2.286  26.253  3.313   1.00 16.11 ? 313 HIS   B C   1 
ATOM   5237 O O   . HIS   B 1 312 ? -2.659  27.323  3.811   1.00 16.32 ? 313 HIS   B O   1 
ATOM   5238 C CB  . HIS   B 1 312 ? -1.673  25.649  0.894   1.00 16.25 ? 313 HIS   B CB  1 
ATOM   5239 C CG  . HIS   B 1 312 ? -0.698  26.798  0.802   1.00 15.72 ? 313 HIS   B CG  1 
ATOM   5240 N ND1 . HIS   B 1 312 ? 0.320   26.805  -0.128  1.00 16.93 ? 313 HIS   B ND1 1 
ATOM   5241 C CD2 . HIS   B 1 312 ? -0.576  27.960  1.494   1.00 17.59 ? 313 HIS   B CD2 1 
ATOM   5242 C CE1 . HIS   B 1 312 ? 1.032   27.913  -0.006  1.00 16.08 ? 313 HIS   B CE1 1 
ATOM   5243 N NE2 . HIS   B 1 312 ? 0.514   28.629  0.979   1.00 18.22 ? 313 HIS   B NE2 1 
ATOM   5244 N N   . LYS   B 1 313 ? -1.446  25.410  3.922   1.00 14.48 ? 314 LYS   B N   1 
ATOM   5245 C CA  . LYS   B 1 313 ? -0.763  25.757  5.164   1.00 14.59 ? 314 LYS   B CA  1 
ATOM   5246 C C   . LYS   B 1 313 ? 0.516   24.942  5.278   1.00 19.24 ? 314 LYS   B C   1 
ATOM   5247 O O   . LYS   B 1 313 ? 0.504   23.730  5.037   1.00 16.62 ? 314 LYS   B O   1 
ATOM   5248 C CB  . LYS   B 1 313 ? -1.652  25.500  6.396   1.00 16.36 ? 314 LYS   B CB  1 
ATOM   5249 C CG  . LYS   B 1 313 ? -1.023  25.965  7.722   1.00 16.08 ? 314 LYS   B CG  1 
ATOM   5250 C CD  . LYS   B 1 313 ? -1.123  27.498  7.880   1.00 18.75 ? 314 LYS   B CD  1 
ATOM   5251 C CE  . LYS   B 1 313 ? -0.491  27.968  9.190   1.00 21.13 ? 314 LYS   B CE  1 
ATOM   5252 N NZ  . LYS   B 1 313 ? 0.995   28.017  9.132   1.00 24.30 ? 314 LYS   B NZ  1 
ATOM   5253 N N   . THR   B 1 314 ? 1.599   25.607  5.677   1.00 18.03 ? 315 THR   B N   1 
ATOM   5254 C CA  . THR   B 1 314 ? 2.858   24.956  6.032   1.00 15.71 ? 315 THR   B CA  1 
ATOM   5255 C C   . THR   B 1 314 ? 3.023   24.900  7.543   1.00 18.23 ? 315 THR   B C   1 
ATOM   5256 O O   . THR   B 1 314 ? 2.478   25.719  8.286   1.00 19.29 ? 315 THR   B O   1 
ATOM   5257 C CB  . THR   B 1 314 ? 4.070   25.686  5.436   1.00 20.77 ? 315 THR   B CB  1 
ATOM   5258 O OG1 . THR   B 1 314 ? 4.146   27.007  5.994   1.00 23.82 ? 315 THR   B OG1 1 
ATOM   5259 C CG2 . THR   B 1 314 ? 3.978   25.743  3.920   1.00 22.23 ? 315 THR   B CG2 1 
ATOM   5260 N N   . GLY   B 1 315 ? 3.824   23.944  8.001   1.00 19.62 ? 316 GLY   B N   1 
ATOM   5261 C CA  . GLY   B 1 315 ? 4.167   23.910  9.408   1.00 20.84 ? 316 GLY   B CA  1 
ATOM   5262 C C   . GLY   B 1 315 ? 5.360   23.022  9.643   1.00 23.24 ? 316 GLY   B C   1 
ATOM   5263 O O   . GLY   B 1 315 ? 5.624   22.099  8.869   1.00 21.53 ? 316 GLY   B O   1 
ATOM   5264 N N   . SER   B 1 316 ? 6.100   23.321  10.707  1.00 21.56 ? 317 SER   B N   1 
ATOM   5265 C CA  . SER   B 1 316 ? 7.240   22.506  11.099  1.00 26.32 ? 317 SER   B CA  1 
ATOM   5266 C C   . SER   B 1 316 ? 7.345   22.489  12.613  1.00 28.22 ? 317 SER   B C   1 
ATOM   5267 O O   . SER   B 1 316 ? 6.860   23.388  13.306  1.00 23.86 ? 317 SER   B O   1 
ATOM   5268 C CB  . SER   B 1 316 ? 8.554   23.025  10.499  1.00 24.05 ? 317 SER   B CB  1 
ATOM   5269 O OG  . SER   B 1 316 ? 8.500   23.061  9.092   1.00 23.87 ? 317 SER   B OG  1 
ATOM   5270 N N   . THR   B 1 317 ? 7.978   21.439  13.118  1.00 24.02 ? 318 THR   B N   1 
ATOM   5271 C CA  . THR   B 1 317 ? 8.497   21.430  14.476  1.00 32.87 ? 318 THR   B CA  1 
ATOM   5272 C C   . THR   B 1 317 ? 10.002  21.221  14.398  1.00 32.68 ? 318 THR   B C   1 
ATOM   5273 O O   . THR   B 1 317 ? 10.609  21.337  13.331  1.00 32.71 ? 318 THR   B O   1 
ATOM   5274 C CB  . THR   B 1 317 ? 7.843   20.349  15.332  1.00 28.96 ? 318 THR   B CB  1 
ATOM   5275 O OG1 . THR   B 1 317 ? 8.126   19.062  14.769  1.00 31.78 ? 318 THR   B OG1 1 
ATOM   5276 C CG2 . THR   B 1 317 ? 6.342   20.554  15.406  1.00 25.04 ? 318 THR   B CG2 1 
ATOM   5277 N N   . ASN   B 1 318 ? 10.606  20.903  15.543  1.00 33.30 ? 319 ASN   B N   1 
ATOM   5278 C CA  . ASN   B 1 318 ? 12.039  20.655  15.558  1.00 41.02 ? 319 ASN   B CA  1 
ATOM   5279 C C   . ASN   B 1 318 ? 12.418  19.547  14.581  1.00 37.63 ? 319 ASN   B C   1 
ATOM   5280 O O   . ASN   B 1 318 ? 13.416  19.659  13.858  1.00 38.35 ? 319 ASN   B O   1 
ATOM   5281 C CB  . ASN   B 1 318 ? 12.491  20.305  16.974  1.00 40.33 ? 319 ASN   B CB  1 
ATOM   5282 C CG  . ASN   B 1 318 ? 13.968  20.036  17.052  1.00 48.03 ? 319 ASN   B CG  1 
ATOM   5283 O OD1 . ASN   B 1 318 ? 14.772  20.728  16.418  1.00 52.03 ? 319 ASN   B OD1 1 
ATOM   5284 N ND2 . ASN   B 1 318 ? 14.342  19.019  17.819  1.00 45.66 ? 319 ASN   B ND2 1 
ATOM   5285 N N   . ARG   B 1 319 ? 11.622  18.480  14.522  1.00 37.90 ? 320 ARG   B N   1 
ATOM   5286 C CA  . ARG   B 1 319 ? 11.975  17.327  13.713  1.00 35.52 ? 320 ARG   B CA  1 
ATOM   5287 C C   . ARG   B 1 319 ? 10.983  16.995  12.606  1.00 32.65 ? 320 ARG   B C   1 
ATOM   5288 O O   . ARG   B 1 319 ? 11.290  16.132  11.779  1.00 34.16 ? 320 ARG   B O   1 
ATOM   5289 C CB  . ARG   B 1 319 ? 12.147  16.088  14.607  1.00 43.91 ? 320 ARG   B CB  1 
ATOM   5290 C CG  . ARG   B 1 319 ? 13.155  15.092  14.071  1.00 51.79 ? 320 ARG   B CG  1 
ATOM   5291 C CD  . ARG   B 1 319 ? 14.103  14.648  15.162  1.00 61.54 ? 320 ARG   B CD  1 
ATOM   5292 N NE  . ARG   B 1 319 ? 15.225  13.886  14.627  0.91 71.33 ? 320 ARG   B NE  1 
ATOM   5293 C CZ  . ARG   B 1 319 ? 16.154  13.301  15.371  0.93 76.34 ? 320 ARG   B CZ  1 
ATOM   5294 N NH1 . ARG   B 1 319 ? 16.120  13.360  16.693  0.97 75.46 ? 320 ARG   B NH1 1 
ATOM   5295 N NH2 . ARG   B 1 319 ? 17.143  12.641  14.774  0.94 80.12 ? 320 ARG   B NH2 1 
ATOM   5296 N N   . PHE   B 1 320 ? 9.822   17.640  12.547  1.00 27.55 ? 321 PHE   B N   1 
ATOM   5297 C CA  . PHE   B 1 320 ? 8.779   17.250  11.608  1.00 24.91 ? 321 PHE   B CA  1 
ATOM   5298 C C   . PHE   B 1 320 ? 8.468   18.383  10.633  1.00 24.87 ? 321 PHE   B C   1 
ATOM   5299 O O   . PHE   B 1 320 ? 8.680   19.559  10.936  1.00 26.40 ? 321 PHE   B O   1 
ATOM   5300 C CB  . PHE   B 1 320 ? 7.504   16.836  12.349  1.00 24.84 ? 321 PHE   B CB  1 
ATOM   5301 C CG  . PHE   B 1 320 ? 7.642   15.552  13.118  1.00 26.52 ? 321 PHE   B CG  1 
ATOM   5302 C CD1 . PHE   B 1 320 ? 8.166   15.551  14.400  1.00 29.30 ? 321 PHE   B CD1 1 
ATOM   5303 C CD2 . PHE   B 1 320 ? 7.232   14.348  12.554  1.00 26.32 ? 321 PHE   B CD2 1 
ATOM   5304 C CE1 . PHE   B 1 320 ? 8.284   14.365  15.112  1.00 33.80 ? 321 PHE   B CE1 1 
ATOM   5305 C CE2 . PHE   B 1 320 ? 7.348   13.161  13.253  1.00 25.61 ? 321 PHE   B CE2 1 
ATOM   5306 C CZ  . PHE   B 1 320 ? 7.873   13.163  14.537  1.00 32.66 ? 321 PHE   B CZ  1 
ATOM   5307 N N   . GLY   B 1 321 ? 7.990   18.012  9.453   1.00 22.87 ? 322 GLY   B N   1 
ATOM   5308 C CA  . GLY   B 1 321 ? 7.524   18.983  8.475   1.00 20.48 ? 322 GLY   B CA  1 
ATOM   5309 C C   . GLY   B 1 321 ? 6.156   18.591  7.956   1.00 21.77 ? 322 GLY   B C   1 
ATOM   5310 O O   . GLY   B 1 321 ? 5.862   17.409  7.793   1.00 19.19 ? 322 GLY   B O   1 
ATOM   5311 N N   . THR   B 1 322 ? 5.311   19.596  7.722   1.00 17.66 ? 323 THR   B N   1 
ATOM   5312 C CA  . THR   B 1 322 ? 3.950   19.373  7.249   1.00 18.77 ? 323 THR   B CA  1 
ATOM   5313 C C   . THR   B 1 322 ? 3.617   20.329  6.110   1.00 17.71 ? 323 THR   B C   1 
ATOM   5314 O O   . THR   B 1 322 ? 4.058   21.481  6.100   1.00 18.07 ? 323 THR   B O   1 
ATOM   5315 C CB  . THR   B 1 322 ? 2.916   19.577  8.382   1.00 20.46 ? 323 THR   B CB  1 
ATOM   5316 O OG1 . THR   B 1 322 ? 3.320   18.843  9.542   1.00 24.98 ? 323 THR   B OG1 1 
ATOM   5317 C CG2 . THR   B 1 322 ? 1.554   19.086  7.948   1.00 19.81 ? 323 THR   B CG2 1 
ATOM   5318 N N   . TYR   B 1 323 ? 2.806   19.853  5.161   1.00 15.59 ? 324 TYR   B N   1 
ATOM   5319 C CA  . TYR   B 1 323 ? 2.178   20.733  4.184   1.00 17.01 ? 324 TYR   B CA  1 
ATOM   5320 C C   . TYR   B 1 323 ? 0.822   20.157  3.830   1.00 16.04 ? 324 TYR   B C   1 
ATOM   5321 O O   . TYR   B 1 323 ? 0.696   18.941  3.653   1.00 17.45 ? 324 TYR   B O   1 
ATOM   5322 C CB  . TYR   B 1 323 ? 3.020   20.875  2.913   1.00 16.02 ? 324 TYR   B CB  1 
ATOM   5323 C CG  . TYR   B 1 323 ? 2.449   21.805  1.860   1.00 17.65 ? 324 TYR   B CG  1 
ATOM   5324 C CD1 . TYR   B 1 323 ? 2.256   23.153  2.131   1.00 18.39 ? 324 TYR   B CD1 1 
ATOM   5325 C CD2 . TYR   B 1 323 ? 2.119   21.338  0.588   1.00 18.17 ? 324 TYR   B CD2 1 
ATOM   5326 C CE1 . TYR   B 1 323 ? 1.755   24.020  1.165   1.00 17.38 ? 324 TYR   B CE1 1 
ATOM   5327 C CE2 . TYR   B 1 323 ? 1.617   22.207  -0.393  1.00 17.54 ? 324 TYR   B CE2 1 
ATOM   5328 C CZ  . TYR   B 1 323 ? 1.433   23.536  -0.098  1.00 17.57 ? 324 TYR   B CZ  1 
ATOM   5329 O OH  . TYR   B 1 323 ? 0.940   24.396  -1.061  1.00 18.76 ? 324 TYR   B OH  1 
ATOM   5330 N N   . VAL   B 1 324 ? -0.188  21.029  3.758   1.00 15.08 ? 325 VAL   B N   1 
ATOM   5331 C CA  . VAL   B 1 324 ? -1.538  20.626  3.388   1.00 16.10 ? 325 VAL   B CA  1 
ATOM   5332 C C   . VAL   B 1 324 ? -2.090  21.667  2.426   1.00 16.84 ? 325 VAL   B C   1 
ATOM   5333 O O   . VAL   B 1 324 ? -1.876  22.868  2.610   1.00 15.67 ? 325 VAL   B O   1 
ATOM   5334 C CB  . VAL   B 1 324 ? -2.459  20.470  4.621   1.00 18.89 ? 325 VAL   B CB  1 
ATOM   5335 C CG1 . VAL   B 1 324 ? -2.051  19.278  5.447   1.00 22.54 ? 325 VAL   B CG1 1 
ATOM   5336 C CG2 . VAL   B 1 324 ? -2.425  21.717  5.482   1.00 20.83 ? 325 VAL   B CG2 1 
ATOM   5337 N N   . VAL   B 1 325 ? -2.789  21.205  1.396   1.00 16.12 ? 326 VAL   B N   1 
ATOM   5338 C CA  . VAL   B 1 325 ? -3.303  22.073  0.339   1.00 16.28 ? 326 VAL   B CA  1 
ATOM   5339 C C   . VAL   B 1 325 ? -4.569  21.436  -0.217  1.00 19.24 ? 326 VAL   B C   1 
ATOM   5340 O O   . VAL   B 1 325 ? -4.649  20.213  -0.350  1.00 18.26 ? 326 VAL   B O   1 
ATOM   5341 C CB  . VAL   B 1 325 ? -2.230  22.294  -0.760  1.00 16.07 ? 326 VAL   B CB  1 
ATOM   5342 C CG1 . VAL   B 1 325 ? -1.723  20.966  -1.313  1.00 16.49 ? 326 VAL   B CG1 1 
ATOM   5343 C CG2 . VAL   B 1 325 ? -2.770  23.137  -1.892  1.00 18.18 ? 326 VAL   B CG2 1 
ATOM   5344 N N   . PHE   B 1 326 ? -5.568  22.253  -0.539  1.00 19.27 ? 327 PHE   B N   1 
ATOM   5345 C CA  . PHE   B 1 326 ? -6.733  21.681  -1.197  1.00 18.77 ? 327 PHE   B CA  1 
ATOM   5346 C C   . PHE   B 1 326 ? -7.365  22.704  -2.132  1.00 21.12 ? 327 PHE   B C   1 
ATOM   5347 O O   . PHE   B 1 326 ? -7.213  23.919  -1.953  1.00 22.03 ? 327 PHE   B O   1 
ATOM   5348 C CB  . PHE   B 1 326 ? -7.748  21.121  -0.174  1.00 19.35 ? 327 PHE   B CB  1 
ATOM   5349 C CG  . PHE   B 1 326 ? -8.497  22.169  0.612   1.00 20.54 ? 327 PHE   B CG  1 
ATOM   5350 C CD1 . PHE   B 1 326 ? -7.956  22.710  1.774   1.00 19.70 ? 327 PHE   B CD1 1 
ATOM   5351 C CD2 . PHE   B 1 326 ? -9.753  22.583  0.207   1.00 21.37 ? 327 PHE   B CD2 1 
ATOM   5352 C CE1 . PHE   B 1 326 ? -8.646  23.674  2.502   1.00 21.03 ? 327 PHE   B CE1 1 
ATOM   5353 C CE2 . PHE   B 1 326 ? -10.451 23.529  0.925   1.00 22.97 ? 327 PHE   B CE2 1 
ATOM   5354 C CZ  . PHE   B 1 326 ? -9.902  24.074  2.078   1.00 19.19 ? 327 PHE   B CZ  1 
ATOM   5355 N N   . ILE   B 1 327 ? -8.043  22.191  -3.158  1.00 21.07 ? 328 ILE   B N   1 
ATOM   5356 C CA  . ILE   B 1 327 ? -8.617  23.013  -4.224  1.00 23.48 ? 328 ILE   B CA  1 
ATOM   5357 C C   . ILE   B 1 327 ? -10.068 22.597  -4.435  1.00 26.60 ? 328 ILE   B C   1 
ATOM   5358 O O   . ILE   B 1 327 ? -10.340 21.611  -5.136  1.00 24.29 ? 328 ILE   B O   1 
ATOM   5359 C CB  . ILE   B 1 327 ? -7.815  22.895  -5.529  1.00 24.92 ? 328 ILE   B CB  1 
ATOM   5360 C CG1 . ILE   B 1 327 ? -6.332  23.226  -5.301  1.00 24.45 ? 328 ILE   B CG1 1 
ATOM   5361 C CG2 . ILE   B 1 327 ? -8.420  23.792  -6.602  1.00 28.51 ? 328 ILE   B CG2 1 
ATOM   5362 C CD1 . ILE   B 1 327 ? -5.409  22.695  -6.408  1.00 27.94 ? 328 ILE   B CD1 1 
ATOM   5363 N N   . PRO   B 1 328 ? -11.023 23.321  -3.851  1.00 23.42 ? 329 PRO   B N   1 
ATOM   5364 C CA  . PRO   B 1 328 ? -12.433 22.886  -3.913  1.00 29.07 ? 329 PRO   B CA  1 
ATOM   5365 C C   . PRO   B 1 328 ? -12.974 22.673  -5.318  1.00 29.77 ? 329 PRO   B C   1 
ATOM   5366 O O   . PRO   B 1 328 ? -13.693 21.693  -5.540  1.00 32.51 ? 329 PRO   B O   1 
ATOM   5367 C CB  . PRO   B 1 328 ? -13.169 24.020  -3.189  1.00 31.58 ? 329 PRO   B CB  1 
ATOM   5368 C CG  . PRO   B 1 328 ? -12.144 24.600  -2.274  1.00 26.49 ? 329 PRO   B CG  1 
ATOM   5369 C CD  . PRO   B 1 328 ? -10.839 24.501  -2.989  1.00 25.21 ? 329 PRO   B CD  1 
ATOM   5370 N N   . LYS   B 1 329 ? -12.650 23.549  -6.276  1.00 30.36 ? 330 LYS   B N   1 
ATOM   5371 C CA  . LYS   B 1 329 ? -13.216 23.424  -7.620  1.00 35.53 ? 330 LYS   B CA  1 
ATOM   5372 C C   . LYS   B 1 329 ? -12.751 22.149  -8.312  1.00 34.16 ? 330 LYS   B C   1 
ATOM   5373 O O   . LYS   B 1 329 ? -13.496 21.571  -9.119  1.00 31.50 ? 330 LYS   B O   1 
ATOM   5374 C CB  . LYS   B 1 329 ? -12.845 24.643  -8.468  1.00 34.48 ? 330 LYS   B CB  1 
ATOM   5375 C CG  . LYS   B 1 329 ? -13.213 24.525  -9.948  1.00 40.55 ? 330 LYS   B CG  1 
ATOM   5376 C CD  . LYS   B 1 329 ? -12.114 25.101  -10.829 1.00 41.34 ? 330 LYS   B CD  1 
ATOM   5377 C CE  . LYS   B 1 329 ? -12.361 24.792  -12.295 1.00 48.14 ? 330 LYS   B CE  1 
ATOM   5378 N NZ  . LYS   B 1 329 ? -13.654 25.380  -12.757 1.00 42.90 ? 330 LYS   B NZ  1 
ATOM   5379 N N   . GLU   B 1 330 ? -11.536 21.697  -8.008  1.00 31.85 ? 331 GLU   B N   1 
ATOM   5380 C CA  . GLU   B 1 330 ? -10.974 20.496  -8.608  1.00 31.90 ? 331 GLU   B CA  1 
ATOM   5381 C C   . GLU   B 1 330 ? -11.195 19.255  -7.758  1.00 31.05 ? 331 GLU   B C   1 
ATOM   5382 O O   . GLU   B 1 330 ? -10.727 18.172  -8.138  1.00 29.94 ? 331 GLU   B O   1 
ATOM   5383 C CB  . GLU   B 1 330 ? -9.474  20.688  -8.865  1.00 34.52 ? 331 GLU   B CB  1 
ATOM   5384 C CG  . GLU   B 1 330 ? -9.152  21.895  -9.748  1.00 38.37 ? 331 GLU   B CG  1 
ATOM   5385 C CD  . GLU   B 1 330 ? -9.543  21.674  -11.195 1.00 41.16 ? 331 GLU   B CD  1 
ATOM   5386 O OE1 . GLU   B 1 330 ? -9.727  20.500  -11.584 1.00 44.58 ? 331 GLU   B OE1 1 
ATOM   5387 O OE2 . GLU   B 1 330 ? -9.663  22.668  -11.947 1.00 43.92 ? 331 GLU   B OE2 1 
ATOM   5388 N N   . ASN   B 1 331 ? -11.888 19.386  -6.625  1.00 27.90 ? 332 ASN   B N   1 
ATOM   5389 C CA  . ASN   B 1 331 ? -12.212 18.259  -5.745  1.00 29.50 ? 332 ASN   B CA  1 
ATOM   5390 C C   . ASN   B 1 331 ? -10.971 17.451  -5.376  1.00 28.85 ? 332 ASN   B C   1 
ATOM   5391 O O   . ASN   B 1 331 ? -10.976 16.219  -5.405  1.00 28.16 ? 332 ASN   B O   1 
ATOM   5392 C CB  . ASN   B 1 331 ? -13.257 17.344  -6.385  1.00 32.37 ? 332 ASN   B CB  1 
ATOM   5393 C CG  . ASN   B 1 331 ? -14.528 18.074  -6.741  1.00 36.12 ? 332 ASN   B CG  1 
ATOM   5394 O OD1 . ASN   B 1 331 ? -15.066 18.833  -5.936  1.00 39.41 ? 332 ASN   B OD1 1 
ATOM   5395 N ND2 . ASN   B 1 331 ? -15.016 17.854  -7.959  1.00 42.57 ? 332 ASN   B ND2 1 
ATOM   5396 N N   . ILE   B 1 332 ? -9.899  18.150  -5.007  1.00 26.50 ? 333 ILE   B N   1 
ATOM   5397 C CA  . ILE   B 1 332 ? -8.614  17.492  -4.803  1.00 24.97 ? 333 ILE   B CA  1 
ATOM   5398 C C   . ILE   B 1 332 ? -7.860  18.159  -3.660  1.00 25.25 ? 333 ILE   B C   1 
ATOM   5399 O O   . ILE   B 1 332 ? -8.060  19.337  -3.360  1.00 23.97 ? 333 ILE   B O   1 
ATOM   5400 C CB  . ILE   B 1 332 ? -7.782  17.505  -6.107  1.00 25.58 ? 333 ILE   B CB  1 
ATOM   5401 C CG1 . ILE   B 1 332 ? -6.564  16.593  -5.995  1.00 29.24 ? 333 ILE   B CG1 1 
ATOM   5402 C CG2 . ILE   B 1 332 ? -7.355  18.926  -6.489  1.00 25.62 ? 333 ILE   B CG2 1 
ATOM   5403 C CD1 . ILE   B 1 332 ? -5.941  16.320  -7.339  1.00 34.20 ? 333 ILE   B CD1 1 
ATOM   5404 N N   . GLY   B 1 333 ? -6.999  17.387  -2.997  1.00 22.00 ? 334 GLY   B N   1 
ATOM   5405 C CA  . GLY   B 1 333 ? -6.185  17.937  -1.927  1.00 18.39 ? 334 GLY   B CA  1 
ATOM   5406 C C   . GLY   B 1 333 ? -5.009  17.022  -1.679  1.00 21.08 ? 334 GLY   B C   1 
ATOM   5407 O O   . GLY   B 1 333 ? -4.988  15.878  -2.130  1.00 21.60 ? 334 GLY   B O   1 
ATOM   5408 N N   . LEU   B 1 334 ? -4.022  17.539  -0.951  1.00 16.69 ? 335 LEU   B N   1 
ATOM   5409 C CA  . LEU   B 1 334 ? -2.807  16.766  -0.716  1.00 18.82 ? 335 LEU   B CA  1 
ATOM   5410 C C   . LEU   B 1 334 ? -2.254  17.062  0.673   1.00 18.33 ? 335 LEU   B C   1 
ATOM   5411 O O   . LEU   B 1 334 ? -2.369  18.180  1.177   1.00 18.10 ? 335 LEU   B O   1 
ATOM   5412 C CB  . LEU   B 1 334 ? -1.755  17.056  -1.798  1.00 21.34 ? 335 LEU   B CB  1 
ATOM   5413 C CG  . LEU   B 1 334 ? -0.415  16.319  -1.718  1.00 20.10 ? 335 LEU   B CG  1 
ATOM   5414 C CD1 . LEU   B 1 334 ? 0.182   16.035  -3.099  1.00 20.78 ? 335 LEU   B CD1 1 
ATOM   5415 C CD2 . LEU   B 1 334 ? 0.577   17.104  -0.868  1.00 18.16 ? 335 LEU   B CD2 1 
ATOM   5416 N N   . VAL   B 1 335 ? -1.641  16.042  1.285   1.00 17.74 ? 336 VAL   B N   1 
ATOM   5417 C CA  . VAL   B 1 335 ? -0.971  16.159  2.580   1.00 18.02 ? 336 VAL   B CA  1 
ATOM   5418 C C   . VAL   B 1 335 ? 0.415   15.542  2.457   1.00 18.50 ? 336 VAL   B C   1 
ATOM   5419 O O   . VAL   B 1 335 ? 0.540   14.410  1.979   1.00 19.10 ? 336 VAL   B O   1 
ATOM   5420 C CB  . VAL   B 1 335 ? -1.730  15.427  3.708   1.00 25.21 ? 336 VAL   B CB  1 
ATOM   5421 C CG1 . VAL   B 1 335 ? -1.062  15.705  5.066   1.00 21.03 ? 336 VAL   B CG1 1 
ATOM   5422 C CG2 . VAL   B 1 335 ? -3.202  15.762  3.715   1.00 31.64 ? 336 VAL   B CG2 1 
ATOM   5423 N N   . MET   B 1 336 ? 1.444   16.261  2.918   1.00 16.82 ? 337 MET   B N   1 
ATOM   5424 C CA  . MET   B 1 336 ? 2.793   15.713  3.068   1.00 16.81 ? 337 MET   B CA  1 
ATOM   5425 C C   . MET   B 1 336 ? 3.189   15.790  4.538   1.00 18.67 ? 337 MET   B C   1 
ATOM   5426 O O   . MET   B 1 336 ? 3.067   16.855  5.160   1.00 18.11 ? 337 MET   B O   1 
ATOM   5427 C CB  . MET   B 1 336 ? 3.827   16.476  2.215   1.00 16.26 ? 337 MET   B CB  1 
ATOM   5428 C CG  . MET   B 1 336 ? 5.238   15.910  2.298   1.00 18.03 ? 337 MET   B CG  1 
ATOM   5429 S SD  . MET   B 1 336 ? 6.513   17.195  2.295   1.00 24.21 ? 337 MET   B SD  1 
ATOM   5430 C CE  . MET   B 1 336 ? 6.378   17.864  3.978   1.00 20.59 ? 337 MET   B CE  1 
ATOM   5431 N N   . LEU   B 1 337 ? 3.646   14.662  5.093   1.00 16.09 ? 338 LEU   B N   1 
ATOM   5432 C CA  . LEU   B 1 337 ? 4.190   14.603  6.449   1.00 17.38 ? 338 LEU   B CA  1 
ATOM   5433 C C   . LEU   B 1 337 ? 5.608   14.036  6.400   1.00 19.92 ? 338 LEU   B C   1 
ATOM   5434 O O   . LEU   B 1 337 ? 5.828   12.968  5.820   1.00 18.35 ? 338 LEU   B O   1 
ATOM   5435 C CB  . LEU   B 1 337 ? 3.308   13.728  7.369   1.00 18.70 ? 338 LEU   B CB  1 
ATOM   5436 C CG  . LEU   B 1 337 ? 1.802   14.024  7.354   1.00 18.45 ? 338 LEU   B CG  1 
ATOM   5437 C CD1 . LEU   B 1 337 ? 0.982   12.984  8.134   1.00 19.78 ? 338 LEU   B CD1 1 
ATOM   5438 C CD2 . LEU   B 1 337 ? 1.510   15.443  7.876   1.00 20.50 ? 338 LEU   B CD2 1 
ATOM   5439 N N   . THR   B 1 338 ? 6.578   14.750  6.987   1.00 19.73 ? 339 THR   B N   1 
ATOM   5440 C CA  . THR   B 1 338 ? 7.950   14.251  7.059   1.00 21.18 ? 339 THR   B CA  1 
ATOM   5441 C C   . THR   B 1 338 ? 8.441   14.262  8.496   1.00 21.64 ? 339 THR   B C   1 
ATOM   5442 O O   . THR   B 1 338 ? 8.008   15.083  9.308   1.00 21.42 ? 339 THR   B O   1 
ATOM   5443 C CB  . THR   B 1 338 ? 8.923   15.083  6.214   1.00 23.09 ? 339 THR   B CB  1 
ATOM   5444 O OG1 . THR   B 1 338 ? 8.911   16.441  6.685   1.00 23.84 ? 339 THR   B OG1 1 
ATOM   5445 C CG2 . THR   B 1 338 ? 8.518   15.049  4.774   1.00 23.63 ? 339 THR   B CG2 1 
ATOM   5446 N N   . ASN   B 1 339 ? 9.351   13.333  8.805   1.00 21.48 ? 340 ASN   B N   1 
ATOM   5447 C CA  . ASN   B 1 339 ? 10.011  13.317  10.100  1.00 21.20 ? 340 ASN   B CA  1 
ATOM   5448 C C   . ASN   B 1 339 ? 11.416  13.898  10.028  1.00 26.13 ? 340 ASN   B C   1 
ATOM   5449 O O   . ASN   B 1 339 ? 12.262  13.591  10.876  1.00 26.47 ? 340 ASN   B O   1 
ATOM   5450 C CB  . ASN   B 1 339 ? 10.016  11.903  10.691  1.00 23.51 ? 340 ASN   B CB  1 
ATOM   5451 C CG  . ASN   B 1 339 ? 10.599  10.867  9.749   1.00 25.45 ? 340 ASN   B CG  1 
ATOM   5452 O OD1 . ASN   B 1 339 ? 11.464  11.165  8.925   1.00 22.17 ? 340 ASN   B OD1 1 
ATOM   5453 N ND2 . ASN   B 1 339 ? 10.124  9.627   9.874   1.00 28.02 ? 340 ASN   B ND2 1 
ATOM   5454 N N   . LYS   B 1 340 ? 11.673  14.724  9.017   1.00 22.68 ? 341 LYS   B N   1 
ATOM   5455 C CA  . LYS   B 1 340 ? 12.756  15.695  9.029   1.00 25.68 ? 341 LYS   B CA  1 
ATOM   5456 C C   . LYS   B 1 340 ? 12.229  16.953  8.365   1.00 25.61 ? 341 LYS   B C   1 
ATOM   5457 O O   . LYS   B 1 340 ? 11.501  16.865  7.374   1.00 27.48 ? 341 LYS   B O   1 
ATOM   5458 C CB  . LYS   B 1 340 ? 13.984  15.198  8.277   1.00 24.82 ? 341 LYS   B CB  1 
ATOM   5459 C CG  . LYS   B 1 340 ? 15.242  16.030  8.563   1.00 29.89 ? 341 LYS   B CG  1 
ATOM   5460 C CD  . LYS   B 1 340 ? 16.113  16.153  7.341   1.00 29.76 ? 341 LYS   B CD  1 
ATOM   5461 C CE  . LYS   B 1 340 ? 17.301  17.066  7.625   1.00 33.58 ? 341 LYS   B CE  1 
ATOM   5462 N NZ  . LYS   B 1 340 ? 18.227  17.167  6.459   1.00 30.63 ? 341 LYS   B NZ  1 
ATOM   5463 N N   . ARG   B 1 341 ? 12.584  18.116  8.911   1.00 26.90 ? 342 ARG   B N   1 
ATOM   5464 C CA  . ARG   B 1 341 ? 12.264  19.373  8.237   1.00 26.26 ? 342 ARG   B CA  1 
ATOM   5465 C C   . ARG   B 1 341 ? 12.971  19.436  6.887   1.00 28.59 ? 342 ARG   B C   1 
ATOM   5466 O O   . ARG   B 1 341 ? 14.170  19.161  6.791   1.00 30.54 ? 342 ARG   B O   1 
ATOM   5467 C CB  . ARG   B 1 341 ? 12.695  20.562  9.096   1.00 30.70 ? 342 ARG   B CB  1 
ATOM   5468 C CG  . ARG   B 1 341 ? 11.681  21.032  10.107  1.00 33.03 ? 342 ARG   B CG  1 
ATOM   5469 C CD  . ARG   B 1 341 ? 12.278  22.187  10.908  1.00 37.42 ? 342 ARG   B CD  1 
ATOM   5470 N NE  . ARG   B 1 341 ? 13.129  21.694  11.988  1.00 41.65 ? 342 ARG   B NE  1 
ATOM   5471 C CZ  . ARG   B 1 341 ? 14.084  22.396  12.586  1.00 42.18 ? 342 ARG   B CZ  1 
ATOM   5472 N NH1 . ARG   B 1 341 ? 14.392  23.623  12.195  1.00 41.61 ? 342 ARG   B NH1 1 
ATOM   5473 N NH2 . ARG   B 1 341 ? 14.752  21.849  13.600  1.00 43.37 ? 342 ARG   B NH2 1 
ATOM   5474 N N   . ILE   B 1 342 ? 12.217  19.765  5.842   1.00 29.44 ? 343 ILE   B N   1 
ATOM   5475 C CA  . ILE   B 1 342 ? 12.774  20.106  4.535   1.00 24.76 ? 343 ILE   B CA  1 
ATOM   5476 C C   . ILE   B 1 342 ? 12.218  21.473  4.150   1.00 23.91 ? 343 ILE   B C   1 
ATOM   5477 O O   . ILE   B 1 342 ? 11.180  21.896  4.675   1.00 24.73 ? 343 ILE   B O   1 
ATOM   5478 C CB  . ILE   B 1 342 ? 12.441  19.039  3.466   1.00 27.07 ? 343 ILE   B CB  1 
ATOM   5479 C CG1 . ILE   B 1 342 ? 10.953  19.058  3.123   1.00 28.29 ? 343 ILE   B CG1 1 
ATOM   5480 C CG2 . ILE   B 1 342 ? 12.894  17.654  3.927   1.00 26.15 ? 343 ILE   B CG2 1 
ATOM   5481 C CD1 . ILE   B 1 342 ? 10.572  18.195  1.924   1.00 26.38 ? 343 ILE   B CD1 1 
ATOM   5482 N N   . PRO   B 1 343 ? 12.896  22.196  3.264   1.00 25.34 ? 344 PRO   B N   1 
ATOM   5483 C CA  . PRO   B 1 343 ? 12.464  23.573  2.969   1.00 22.77 ? 344 PRO   B CA  1 
ATOM   5484 C C   . PRO   B 1 343 ? 11.015  23.644  2.497   1.00 23.41 ? 344 PRO   B C   1 
ATOM   5485 O O   . PRO   B 1 343 ? 10.549  22.810  1.716   1.00 22.36 ? 344 PRO   B O   1 
ATOM   5486 C CB  . PRO   B 1 343 ? 13.439  24.016  1.870   1.00 26.27 ? 344 PRO   B CB  1 
ATOM   5487 C CG  . PRO   B 1 343 ? 14.675  23.210  2.137   1.00 27.01 ? 344 PRO   B CG  1 
ATOM   5488 C CD  . PRO   B 1 343 ? 14.156  21.861  2.574   1.00 24.51 ? 344 PRO   B CD  1 
ATOM   5489 N N   . ASN   B 1 344 ? 10.301  24.661  2.992   1.00 22.77 ? 345 ASN   B N   1 
ATOM   5490 C CA  . ASN   B 1 344 ? 8.905   24.855  2.609   1.00 19.49 ? 345 ASN   B CA  1 
ATOM   5491 C C   . ASN   B 1 344 ? 8.746   24.944  1.098   1.00 20.09 ? 345 ASN   B C   1 
ATOM   5492 O O   . ASN   B 1 344 ? 7.769   24.436  0.544   1.00 20.76 ? 345 ASN   B O   1 
ATOM   5493 C CB  . ASN   B 1 344 ? 8.351   26.118  3.270   1.00 21.67 ? 345 ASN   B CB  1 
ATOM   5494 C CG  . ASN   B 1 344 ? 8.071   25.931  4.746   1.00 21.53 ? 345 ASN   B CG  1 
ATOM   5495 O OD1 . ASN   B 1 344 ? 7.662   24.857  5.181   1.00 24.84 ? 345 ASN   B OD1 1 
ATOM   5496 N ND2 . ASN   B 1 344 ? 8.263   26.988  5.520   1.00 28.06 ? 345 ASN   B ND2 1 
ATOM   5497 N N   A GLU   B 1 345 ? 9.703   25.583  0.417   0.52 22.57 ? 346 GLU   B N   1 
ATOM   5498 N N   B GLU   B 1 345 ? 9.701   25.586  0.413   0.48 22.57 ? 346 GLU   B N   1 
ATOM   5499 C CA  A GLU   B 1 345 ? 9.624   25.726  -1.032  0.52 24.19 ? 346 GLU   B CA  1 
ATOM   5500 C CA  B GLU   B 1 345 ? 9.605   25.725  -1.037  0.48 24.19 ? 346 GLU   B CA  1 
ATOM   5501 C C   A GLU   B 1 345 ? 9.564   24.368  -1.719  0.52 22.97 ? 346 GLU   B C   1 
ATOM   5502 C C   B GLU   B 1 345 ? 9.560   24.364  -1.722  0.48 22.97 ? 346 GLU   B C   1 
ATOM   5503 O O   A GLU   B 1 345 ? 8.854   24.199  -2.717  0.52 21.45 ? 346 GLU   B O   1 
ATOM   5504 O O   B GLU   B 1 345 ? 8.847   24.185  -2.717  0.48 21.46 ? 346 GLU   B O   1 
ATOM   5505 C CB  A GLU   B 1 345 ? 10.825  26.524  -1.540  0.52 24.83 ? 346 GLU   B CB  1 
ATOM   5506 C CB  B GLU   B 1 345 ? 10.778  26.557  -1.564  0.48 24.83 ? 346 GLU   B CB  1 
ATOM   5507 C CG  A GLU   B 1 345 ? 11.950  26.671  -0.509  0.52 28.29 ? 346 GLU   B CG  1 
ATOM   5508 C CG  B GLU   B 1 345 ? 11.451  26.010  -2.817  0.48 29.01 ? 346 GLU   B CG  1 
ATOM   5509 C CD  A GLU   B 1 345 ? 11.634  27.720  0.551   0.52 26.15 ? 346 GLU   B CD  1 
ATOM   5510 C CD  B GLU   B 1 345 ? 12.739  25.256  -2.521  0.48 27.72 ? 346 GLU   B CD  1 
ATOM   5511 O OE1 A GLU   B 1 345 ? 11.392  28.889  0.176   0.52 33.65 ? 346 GLU   B OE1 1 
ATOM   5512 O OE1 B GLU   B 1 345 ? 13.376  25.524  -1.479  0.48 33.84 ? 346 GLU   B OE1 1 
ATOM   5513 O OE2 A GLU   B 1 345 ? 11.594  27.382  1.757   0.52 22.66 ? 346 GLU   B OE2 1 
ATOM   5514 O OE2 B GLU   B 1 345 ? 13.121  24.389  -3.331  0.48 33.42 ? 346 GLU   B OE2 1 
ATOM   5515 N N   . GLU   B 1 346 ? 10.310  23.389  -1.196  1.00 21.59 ? 347 GLU   B N   1 
ATOM   5516 C CA  . GLU   B 1 346 ? 10.293  22.046  -1.773  1.00 23.60 ? 347 GLU   B CA  1 
ATOM   5517 C C   . GLU   B 1 346 ? 8.931   21.386  -1.592  1.00 21.91 ? 347 GLU   B C   1 
ATOM   5518 O O   . GLU   B 1 346 ? 8.446   20.693  -2.496  1.00 20.82 ? 347 GLU   B O   1 
ATOM   5519 C CB  . GLU   B 1 346 ? 11.384  21.181  -1.134  1.00 24.95 ? 347 GLU   B CB  1 
ATOM   5520 C CG  . GLU   B 1 346 ? 12.819  21.688  -1.350  1.00 27.62 ? 347 GLU   B CG  1 
ATOM   5521 C CD  . GLU   B 1 346 ? 13.447  21.181  -2.638  1.00 31.96 ? 347 GLU   B CD  1 
ATOM   5522 O OE1 . GLU   B 1 346 ? 12.716  20.961  -3.631  1.00 32.46 ? 347 GLU   B OE1 1 
ATOM   5523 O OE2 . GLU   B 1 346 ? 14.686  20.985  -2.649  1.00 34.14 ? 347 GLU   B OE2 1 
ATOM   5524 N N   . ARG   B 1 347 ? 8.303   21.589  -0.431  1.00 18.25 ? 348 ARG   B N   1 
ATOM   5525 C CA  . ARG   B 1 347 ? 6.986   21.009  -0.192  1.00 17.07 ? 348 ARG   B CA  1 
ATOM   5526 C C   . ARG   B 1 347 ? 5.962   21.596  -1.151  1.00 19.96 ? 348 ARG   B C   1 
ATOM   5527 O O   . ARG   B 1 347 ? 5.165   20.871  -1.755  1.00 21.87 ? 348 ARG   B O   1 
ATOM   5528 C CB  . ARG   B 1 347 ? 6.551   21.258  1.258   1.00 19.38 ? 348 ARG   B CB  1 
ATOM   5529 C CG  . ARG   B 1 347 ? 7.621   21.016  2.304   1.00 19.66 ? 348 ARG   B CG  1 
ATOM   5530 C CD  . ARG   B 1 347 ? 7.132   21.433  3.682   1.00 19.36 ? 348 ARG   B CD  1 
ATOM   5531 N NE  . ARG   B 1 347 ? 8.247   21.548  4.620   1.00 20.52 ? 348 ARG   B NE  1 
ATOM   5532 C CZ  . ARG   B 1 347 ? 8.135   21.886  5.900   1.00 21.48 ? 348 ARG   B CZ  1 
ATOM   5533 N NH1 . ARG   B 1 347 ? 6.954   22.051  6.475   1.00 20.48 ? 348 ARG   B NH1 1 
ATOM   5534 N NH2 . ARG   B 1 347 ? 9.240   22.052  6.626   1.00 21.76 ? 348 ARG   B NH2 1 
ATOM   5535 N N   . ILE   B 1 348 ? 5.971   22.925  -1.291  1.00 19.41 ? 349 ILE   B N   1 
ATOM   5536 C CA  . ILE   B 1 348 ? 5.011   23.605  -2.153  1.00 19.39 ? 349 ILE   B CA  1 
ATOM   5537 C C   . ILE   B 1 348 ? 5.220   23.214  -3.614  1.00 19.59 ? 349 ILE   B C   1 
ATOM   5538 O O   . ILE   B 1 348 ? 4.256   22.956  -4.337  1.00 20.52 ? 349 ILE   B O   1 
ATOM   5539 C CB  . ILE   B 1 348 ? 5.114   25.129  -1.946  1.00 18.17 ? 349 ILE   B CB  1 
ATOM   5540 C CG1 . ILE   B 1 348 ? 4.673   25.509  -0.529  1.00 18.77 ? 349 ILE   B CG1 1 
ATOM   5541 C CG2 . ILE   B 1 348 ? 4.296   25.859  -2.986  1.00 20.83 ? 349 ILE   B CG2 1 
ATOM   5542 C CD1 . ILE   B 1 348 ? 5.168   26.909  -0.113  1.00 20.25 ? 349 ILE   B CD1 1 
ATOM   5543 N N   . LYS   B 1 349 ? 6.477   23.134  -4.062  1.00 23.02 ? 350 LYS   B N   1 
ATOM   5544 C CA  . LYS   B 1 349 ? 6.751   22.810  -5.460  1.00 22.31 ? 350 LYS   B CA  1 
ATOM   5545 C C   . LYS   B 1 349 ? 6.312   21.391  -5.795  1.00 21.97 ? 350 LYS   B C   1 
ATOM   5546 O O   . LYS   B 1 349 ? 5.676   21.154  -6.830  1.00 24.06 ? 350 LYS   B O   1 
ATOM   5547 C CB  . LYS   B 1 349 ? 8.242   22.979  -5.766  1.00 23.48 ? 350 LYS   B CB  1 
ATOM   5548 C CG  . LYS   B 1 349 ? 8.748   24.411  -5.849  1.00 29.48 ? 350 LYS   B CG  1 
ATOM   5549 C CD  . LYS   B 1 349 ? 10.273  24.389  -6.019  1.00 32.44 ? 350 LYS   B CD  1 
ATOM   5550 C CE  . LYS   B 1 349 ? 10.849  25.753  -6.350  1.00 37.82 ? 350 LYS   B CE  1 
ATOM   5551 N NZ  . LYS   B 1 349 ? 12.315  25.648  -6.644  1.00 45.64 ? 350 LYS   B NZ  1 
ATOM   5552 N N   . ALA   B 1 350 ? 6.659   20.431  -4.935  1.00 20.42 ? 351 ALA   B N   1 
ATOM   5553 C CA  . ALA   B 1 350 ? 6.307   19.039  -5.203  1.00 21.92 ? 351 ALA   B CA  1 
ATOM   5554 C C   . ALA   B 1 350 ? 4.796   18.843  -5.246  1.00 21.30 ? 351 ALA   B C   1 
ATOM   5555 O O   . ALA   B 1 350 ? 4.278   18.171  -6.143  1.00 22.09 ? 351 ALA   B O   1 
ATOM   5556 C CB  . ALA   B 1 350 ? 6.937   18.133  -4.150  1.00 22.43 ? 351 ALA   B CB  1 
ATOM   5557 N N   . ALA   B 1 351 ? 4.073   19.434  -4.289  1.00 19.54 ? 352 ALA   B N   1 
ATOM   5558 C CA  . ALA   B 1 351 ? 2.619   19.312  -4.274  1.00 22.48 ? 352 ALA   B CA  1 
ATOM   5559 C C   . ALA   B 1 351 ? 2.001   19.975  -5.498  1.00 20.57 ? 352 ALA   B C   1 
ATOM   5560 O O   . ALA   B 1 351 ? 1.030   19.465  -6.070  1.00 22.69 ? 352 ALA   B O   1 
ATOM   5561 C CB  . ALA   B 1 351 ? 2.056   19.926  -2.986  1.00 19.42 ? 352 ALA   B CB  1 
ATOM   5562 N N   . TYR   B 1 352 ? 2.550   21.120  -5.909  1.00 21.84 ? 353 TYR   B N   1 
ATOM   5563 C CA  . TYR   B 1 352 ? 2.050   21.801  -7.099  1.00 21.88 ? 353 TYR   B CA  1 
ATOM   5564 C C   . TYR   B 1 352 ? 2.222   20.928  -8.341  1.00 23.81 ? 353 TYR   B C   1 
ATOM   5565 O O   . TYR   B 1 352 ? 1.327   20.853  -9.193  1.00 25.40 ? 353 TYR   B O   1 
ATOM   5566 C CB  . TYR   B 1 352 ? 2.778   23.140  -7.261  1.00 24.13 ? 353 TYR   B CB  1 
ATOM   5567 C CG  . TYR   B 1 352 ? 2.226   24.043  -8.342  1.00 23.31 ? 353 TYR   B CG  1 
ATOM   5568 C CD1 . TYR   B 1 352 ? 2.687   23.956  -9.649  1.00 23.07 ? 353 TYR   B CD1 1 
ATOM   5569 C CD2 . TYR   B 1 352 ? 1.246   24.981  -8.052  1.00 24.24 ? 353 TYR   B CD2 1 
ATOM   5570 C CE1 . TYR   B 1 352 ? 2.187   24.786  -10.641 1.00 29.32 ? 353 TYR   B CE1 1 
ATOM   5571 C CE2 . TYR   B 1 352 ? 0.735   25.810  -9.036  1.00 27.56 ? 353 TYR   B CE2 1 
ATOM   5572 C CZ  . TYR   B 1 352 ? 1.209   25.706  -10.328 1.00 31.21 ? 353 TYR   B CZ  1 
ATOM   5573 O OH  . TYR   B 1 352 ? 0.704   26.529  -11.307 1.00 35.34 ? 353 TYR   B OH  1 
ATOM   5574 N N   . ALA   B 1 353 ? 3.373   20.269  -8.470  1.00 24.68 ? 354 ALA   B N   1 
ATOM   5575 C CA  . ALA   B 1 353 ? 3.595   19.415  -9.634  1.00 23.79 ? 354 ALA   B CA  1 
ATOM   5576 C C   . ALA   B 1 353 ? 2.595   18.264  -9.670  1.00 25.92 ? 354 ALA   B C   1 
ATOM   5577 O O   . ALA   B 1 353 ? 2.029   17.953  -10.723 1.00 28.11 ? 354 ALA   B O   1 
ATOM   5578 C CB  . ALA   B 1 353 ? 5.031   18.887  -9.626  1.00 23.87 ? 354 ALA   B CB  1 
ATOM   5579 N N   . VAL   B 1 354 ? 2.355   17.625  -8.525  1.00 26.25 ? 355 VAL   B N   1 
ATOM   5580 C CA  . VAL   B 1 354 ? 1.434   16.489  -8.483  1.00 24.35 ? 355 VAL   B CA  1 
ATOM   5581 C C   . VAL   B 1 354 ? 0.013   16.936  -8.803  1.00 25.58 ? 355 VAL   B C   1 
ATOM   5582 O O   . VAL   B 1 354 ? -0.690  16.310  -9.607  1.00 28.10 ? 355 VAL   B O   1 
ATOM   5583 C CB  . VAL   B 1 354 ? 1.500   15.798  -7.109  1.00 23.40 ? 355 VAL   B CB  1 
ATOM   5584 C CG1 . VAL   B 1 354 ? 0.363   14.777  -6.963  1.00 22.63 ? 355 VAL   B CG1 1 
ATOM   5585 C CG2 . VAL   B 1 354 ? 2.850   15.121  -6.925  1.00 24.86 ? 355 VAL   B CG2 1 
ATOM   5586 N N   . LEU   B 1 355 ? -0.442  18.009  -8.151  1.00 26.32 ? 356 LEU   B N   1 
ATOM   5587 C CA  . LEU   B 1 355 ? -1.832  18.429  -8.300  1.00 24.51 ? 356 LEU   B CA  1 
ATOM   5588 C C   . LEU   B 1 355 ? -2.135  18.917  -9.709  1.00 26.79 ? 356 LEU   B C   1 
ATOM   5589 O O   . LEU   B 1 355 ? -3.269  18.784  -10.181 1.00 29.82 ? 356 LEU   B O   1 
ATOM   5590 C CB  . LEU   B 1 355 ? -2.163  19.520  -7.283  1.00 23.78 ? 356 LEU   B CB  1 
ATOM   5591 C CG  . LEU   B 1 355 ? -2.239  19.074  -5.821  1.00 24.37 ? 356 LEU   B CG  1 
ATOM   5592 C CD1 . LEU   B 1 355 ? -2.573  20.239  -4.907  1.00 28.67 ? 356 LEU   B CD1 1 
ATOM   5593 C CD2 . LEU   B 1 355 ? -3.233  17.945  -5.633  1.00 27.77 ? 356 LEU   B CD2 1 
ATOM   5594 N N   . ASN   B 1 356 ? -1.151  19.476  -10.397 1.00 26.15 ? 357 ASN   B N   1 
ATOM   5595 C CA  . ASN   B 1 356 ? -1.423  19.986  -11.726 1.00 28.91 ? 357 ASN   B CA  1 
ATOM   5596 C C   . ASN   B 1 356 ? -1.231  18.939  -12.812 1.00 32.65 ? 357 ASN   B C   1 
ATOM   5597 O O   . ASN   B 1 356 ? -1.794  19.091  -13.903 1.00 36.26 ? 357 ASN   B O   1 
ATOM   5598 C CB  . ASN   B 1 356 ? -0.563  21.220  -11.991 1.00 29.38 ? 357 ASN   B CB  1 
ATOM   5599 C CG  . ASN   B 1 356 ? -1.154  22.469  -11.354 1.00 29.60 ? 357 ASN   B CG  1 
ATOM   5600 O OD1 . ASN   B 1 356 ? -2.116  23.041  -11.871 1.00 33.72 ? 357 ASN   B OD1 1 
ATOM   5601 N ND2 . ASN   B 1 356 ? -0.600  22.882  -10.215 1.00 29.95 ? 357 ASN   B ND2 1 
ATOM   5602 N N   . ALA   B 1 357 ? -0.500  17.861  -12.530 1.00 31.84 ? 358 ALA   B N   1 
ATOM   5603 C CA  . ALA   B 1 357 ? -0.305  16.811  -13.521 1.00 31.24 ? 358 ALA   B CA  1 
ATOM   5604 C C   . ALA   B 1 357 ? -1.337  15.699  -13.422 1.00 38.57 ? 358 ALA   B C   1 
ATOM   5605 O O   . ALA   B 1 357 ? -1.513  14.948  -14.387 1.00 39.43 ? 358 ALA   B O   1 
ATOM   5606 C CB  . ALA   B 1 357 ? 1.097   16.209  -13.391 1.00 32.42 ? 358 ALA   B CB  1 
ATOM   5607 N N   . ILE   B 1 358 ? -2.023  15.575  -12.288 1.00 34.69 ? 359 ILE   B N   1 
ATOM   5608 C CA  . ILE   B 1 358 ? -2.996  14.505  -12.119 1.00 39.89 ? 359 ILE   B CA  1 
ATOM   5609 C C   . ILE   B 1 358 ? -4.161  14.712  -13.083 1.00 43.87 ? 359 ILE   B C   1 
ATOM   5610 O O   . ILE   B 1 358 ? -4.651  15.835  -13.271 1.00 40.35 ? 359 ILE   B O   1 
ATOM   5611 C CB  . ILE   B 1 358 ? -3.456  14.456  -10.652 1.00 39.91 ? 359 ILE   B CB  1 
ATOM   5612 C CG1 . ILE   B 1 358 ? -4.445  13.323  -10.411 1.00 41.25 ? 359 ILE   B CG1 1 
ATOM   5613 C CG2 . ILE   B 1 358 ? -4.062  15.781  -10.241 1.00 37.90 ? 359 ILE   B CG2 1 
ATOM   5614 C CD1 . ILE   B 1 358 ? -5.029  13.356  -9.029  1.00 40.41 ? 359 ILE   B CD1 1 
ATOM   5615 N N   . LYS   B 1 359 ? -4.594  13.628  -13.723 1.00 44.70 ? 360 LYS   B N   1 
ATOM   5616 C CA  . LYS   B 1 359 ? -5.634  13.705  -14.749 1.00 45.94 ? 360 LYS   B CA  1 
ATOM   5617 C C   . LYS   B 1 359 ? -7.005  13.945  -14.129 1.00 44.68 ? 360 LYS   B C   1 
ATOM   5618 O O   . LYS   B 1 359 ? -7.218  13.662  -12.951 1.00 42.33 ? 360 LYS   B O   1 
ATOM   5619 C CB  . LYS   B 1 359 ? -5.644  12.426  -15.595 1.00 46.17 ? 360 LYS   B CB  1 
ATOM   5620 C CG  . LYS   B 1 359 ? -4.315  12.150  -16.291 1.00 49.50 ? 360 LYS   B CG  1 
ATOM   5621 C CD  . LYS   B 1 359 ? -4.083  10.658  -16.495 1.00 58.44 ? 360 LYS   B CD  1 
ATOM   5622 C CE  . LYS   B 1 359 ? -2.595  10.307  -16.448 1.00 58.20 ? 360 LYS   B CE  1 
ATOM   5623 N NZ  . LYS   B 1 359 ? -1.852  10.746  -17.662 1.00 61.80 ? 360 LYS   B NZ  1 
HETATM 5624 C C   . 1RG   C 2 .   ? 33.876  -16.320 -2.615  0.66 44.58 ? 401 1RG   A C   1 
HETATM 5625 N N   . 1RG   C 2 .   ? 32.601  -14.200 -2.209  0.66 46.21 ? 401 1RG   A N   1 
HETATM 5626 O O   . 1RG   C 2 .   ? 32.975  -16.799 -3.293  0.66 39.33 ? 401 1RG   A O   1 
HETATM 5627 C CA  . 1RG   C 2 .   ? 33.688  -15.069 -1.802  0.66 44.99 ? 401 1RG   A CA  1 
HETATM 5628 C CB  . 1RG   C 2 .   ? 33.432  -15.373 -0.329  0.66 44.26 ? 401 1RG   A CB  1 
HETATM 5629 C CD  . 1RG   C 2 .   ? 31.932  -13.582 -1.082  0.66 44.75 ? 401 1RG   A CD  1 
HETATM 5630 C CG  . 1RG   C 2 .   ? 32.587  -14.195 0.153   0.66 42.60 ? 401 1RG   A CG  1 
HETATM 5631 C CAA . 1RG   C 2 .   ? 27.920  -19.674 -0.216  0.66 25.34 ? 401 1RG   A CAA 1 
HETATM 5632 C CAB . 1RG   C 2 .   ? 28.562  -18.477 -0.877  0.66 22.86 ? 401 1RG   A CAB 1 
HETATM 5633 O OAC . 1RG   C 2 .   ? 27.541  -20.645 -0.872  0.66 25.95 ? 401 1RG   A OAC 1 
HETATM 5634 C CAD . 1RG   C 2 .   ? 29.675  -17.923 -0.001  0.66 26.82 ? 401 1RG   A CAD 1 
HETATM 5635 C CAE . 1RG   C 2 .   ? 29.158  -18.885 -2.214  0.66 25.12 ? 401 1RG   A CAE 1 
HETATM 5636 C CAF . 1RG   C 2 .   ? 30.281  -19.899 -2.031  0.66 26.46 ? 401 1RG   A CAF 1 
HETATM 5637 O OAG . 1RG   C 2 .   ? 28.116  -19.425 -3.017  0.66 23.30 ? 401 1RG   A OAG 1 
HETATM 5638 C CAH . 1RG   C 2 .   ? 30.146  -16.509 -0.345  0.66 29.23 ? 401 1RG   A CAH 1 
HETATM 5639 C CAI . 1RG   C 2 .   ? 30.430  -15.988 1.022   0.66 33.98 ? 401 1RG   A CAI 1 
HETATM 5640 N NAJ . 1RG   C 2 .   ? 29.272  -17.812 1.381   0.66 29.29 ? 401 1RG   A NAJ 1 
HETATM 5641 S SAK . 1RG   C 2 .   ? 31.375  -14.645 1.360   0.66 39.79 ? 401 1RG   A SAK 1 
HETATM 5642 C CAL . 1RG   C 2 .   ? 29.801  -16.732 1.927   0.66 23.28 ? 401 1RG   A CAL 1 
HETATM 5643 C CAM . 1RG   C 2 .   ? 29.669  -16.442 3.346   0.66 32.15 ? 401 1RG   A CAM 1 
HETATM 5644 C CAS . 1RG   C 2 .   ? 29.064  -15.612 -0.932  0.66 26.59 ? 401 1RG   A CAS 1 
HETATM 5645 O OAT . 1RG   C 2 .   ? 28.716  -16.964 3.974   0.66 30.14 ? 401 1RG   A OAT 1 
HETATM 5646 O OAU . 1RG   C 2 .   ? 30.515  -15.702 3.894   0.66 32.05 ? 401 1RG   A OAU 1 
HETATM 5647 N NAX . 1RG   C 2 .   ? 35.102  -16.831 -2.505  0.66 42.83 ? 401 1RG   A NAX 1 
HETATM 5648 C CAY . 1RG   C 2 .   ? 35.728  -17.516 -3.488  0.66 37.02 ? 401 1RG   A CAY 1 
HETATM 5649 C CAZ . 1RG   C 2 .   ? 35.611  -17.134 -4.820  0.66 38.20 ? 401 1RG   A CAZ 1 
HETATM 5650 C CBA . 1RG   C 2 .   ? 36.282  -17.854 -5.804  0.66 38.56 ? 401 1RG   A CBA 1 
HETATM 5651 C CBB . 1RG   C 2 .   ? 37.067  -18.944 -5.447  0.66 33.35 ? 401 1RG   A CBB 1 
HETATM 5652 C CBC . 1RG   C 2 .   ? 37.191  -19.327 -4.117  0.66 29.42 ? 401 1RG   A CBC 1 
HETATM 5653 C CBD . 1RG   C 2 .   ? 36.527  -18.600 -3.140  0.66 38.48 ? 401 1RG   A CBD 1 
HETATM 5654 C CBE . 1RG   C 2 .   ? 36.167  -17.476 -7.252  0.66 36.97 ? 401 1RG   A CBE 1 
HETATM 5655 O OBF . 1RG   C 2 .   ? 37.022  -17.920 -8.059  0.66 33.98 ? 401 1RG   A OBF 1 
HETATM 5656 O OBG . 1RG   C 2 .   ? 35.219  -16.739 -7.615  0.66 39.95 ? 401 1RG   A OBG 1 
HETATM 5657 C C1  . EDO   D 3 .   ? 20.671  -25.876 -12.625 1.00 30.11 ? 402 EDO   A C1  1 
HETATM 5658 O O1  . EDO   D 3 .   ? 20.595  -26.809 -13.712 1.00 32.28 ? 402 EDO   A O1  1 
HETATM 5659 C C2  . EDO   D 3 .   ? 20.352  -24.450 -13.017 1.00 27.57 ? 402 EDO   A C2  1 
HETATM 5660 O O2  . EDO   D 3 .   ? 21.394  -23.517 -12.729 1.00 29.19 ? 402 EDO   A O2  1 
HETATM 5661 C C2  . A1B93 E 4 .   ? 8.145   28.684  10.467  0.80 24.68 ? 401 A1B93 B C2  1 
HETATM 5662 C C5  . A1B93 E 4 .   ? 6.456   28.825  12.218  0.80 24.70 ? 401 A1B93 B C5  1 
HETATM 5663 C C6  . A1B93 E 4 .   ? 6.225   27.589  13.065  0.80 24.32 ? 401 A1B93 B C6  1 
HETATM 5664 C C1  . A1B93 E 4 .   ? 7.932   29.082  11.912  0.80 26.56 ? 401 A1B93 B C1  1 
HETATM 5665 C C11 . A1B93 E 4 .   ? 8.900   28.358  12.839  0.80 31.91 ? 401 A1B93 B C11 1 
HETATM 5666 C C3  . A1B93 E 4 .   ? 6.764   28.483  9.972   0.80 25.43 ? 401 A1B93 B C3  1 
HETATM 5667 C C7  . A1B93 E 4 .   ? 5.033   26.704  12.463  0.80 24.14 ? 401 A1B93 B C7  1 
HETATM 5668 C CD2 . A1B93 E 4 .   ? 11.211  25.003  13.603  0.80 38.78 ? 401 A1B93 B CD2 1 
HETATM 5669 C CE2 . A1B93 E 4 .   ? 9.906   24.952  14.061  0.80 37.00 ? 401 A1B93 B CE2 1 
HETATM 5670 C CE3 . A1B93 E 4 .   ? 12.258  24.751  14.481  0.80 39.72 ? 401 A1B93 B CE3 1 
HETATM 5671 C CZ2 . A1B93 E 4 .   ? 9.644   24.657  15.388  0.80 37.70 ? 401 A1B93 B CZ2 1 
HETATM 5672 C CZ3 . A1B93 E 4 .   ? 11.993  24.459  15.808  0.80 42.03 ? 401 A1B93 B CZ3 1 
HETATM 5673 C CH2 . A1B93 E 4 .   ? 10.686  24.407  16.263  0.80 43.51 ? 401 A1B93 B CH2 1 
HETATM 5674 C C1A . A1B93 E 4 .   ? 10.147  27.166  9.226   0.80 31.96 ? 401 A1B93 B C1A 1 
HETATM 5675 C C2A . A1B93 E 4 .   ? 10.563  25.786  8.787   0.80 31.95 ? 401 A1B93 B C2A 1 
HETATM 5676 C C31 . A1B93 E 4 .   ? 6.487   28.204  8.566   0.80 27.53 ? 401 A1B93 B C31 1 
HETATM 5677 C C41 . A1B93 E 4 .   ? 13.110  24.184  16.761  0.80 47.97 ? 401 A1B93 B C41 1 
HETATM 5678 C C4A . A1B93 E 4 .   ? 11.361  27.756  9.904   0.80 35.46 ? 401 A1B93 B C4A 1 
HETATM 5679 C C5A . A1B93 E 4 .   ? 12.157  26.563  10.400  0.80 38.31 ? 401 A1B93 B C5A 1 
HETATM 5680 C C61 . A1B93 E 4 .   ? 5.788   27.987  14.473  0.80 27.63 ? 401 A1B93 B C61 1 
HETATM 5681 C C62 . A1B93 E 4 .   ? 5.652   26.746  15.355  0.80 27.32 ? 401 A1B93 B C62 1 
HETATM 5682 C C6A . A1B93 E 4 .   ? 11.976  26.433  11.882  0.80 39.84 ? 401 A1B93 B C6A 1 
HETATM 5683 N N3A . A1B93 E 4 .   ? 11.642  25.371  9.700   0.80 34.23 ? 401 A1B93 B N3A 1 
HETATM 5684 N N4  . A1B93 E 4 .   ? 5.905   28.549  10.885  0.80 24.11 ? 401 A1B93 B N4  1 
HETATM 5685 N N7A . A1B93 E 4 .   ? 11.445  25.286  12.308  0.80 37.08 ? 401 A1B93 B N7A 1 
HETATM 5686 O O31 . A1B93 E 4 .   ? 5.673   27.314  8.264   0.80 23.82 ? 401 A1B93 B O31 1 
HETATM 5687 O O32 . A1B93 E 4 .   ? 7.103   28.859  7.700   0.80 27.52 ? 401 A1B93 B O32 1 
HETATM 5688 O O42 . A1B93 E 4 .   ? 12.824  23.815  17.917  0.80 51.91 ? 401 A1B93 B O42 1 
HETATM 5689 O O43 . A1B93 E 4 .   ? 14.288  24.330  16.376  0.80 48.50 ? 401 A1B93 B O43 1 
HETATM 5690 O O62 . A1B93 E 4 .   ? 6.671   28.951  15.061  0.80 27.30 ? 401 A1B93 B O62 1 
HETATM 5691 O O6A . A1B93 E 4 .   ? 12.309  27.358  12.603  0.80 42.66 ? 401 A1B93 B O6A 1 
HETATM 5692 O O7  . A1B93 E 4 .   ? 5.482   25.754  11.820  0.80 23.55 ? 401 A1B93 B O7  1 
HETATM 5693 S S21 . A1B93 E 4 .   ? 8.851   27.076  10.402  0.80 27.17 ? 401 A1B93 B S21 1 
HETATM 5694 C C1  . EDO   F 3 .   ? 16.391  18.217  11.967  1.00 34.83 ? 402 EDO   B C1  1 
HETATM 5695 O O1  . EDO   F 3 .   ? 16.775  16.891  11.691  1.00 48.74 ? 402 EDO   B O1  1 
HETATM 5696 C C2  . EDO   F 3 .   ? 15.422  18.681  10.911  1.00 36.53 ? 402 EDO   B C2  1 
HETATM 5697 O O2  . EDO   F 3 .   ? 14.162  18.140  11.232  1.00 35.48 ? 402 EDO   B O2  1 
HETATM 5698 O O   . HOH   G 5 .   ? 37.530  -40.470 5.199   1.00 30.71 ? 501 HOH   A O   1 
HETATM 5699 O O   . HOH   G 5 .   ? 4.650   -15.908 9.019   1.00 35.34 ? 502 HOH   A O   1 
HETATM 5700 O O   . HOH   G 5 .   ? 27.787  -26.231 4.786   1.00 28.72 ? 503 HOH   A O   1 
HETATM 5701 O O   . HOH   G 5 .   ? 12.926  -14.692 27.442  1.00 36.27 ? 504 HOH   A O   1 
HETATM 5702 O O   A HOH   G 5 .   ? 27.924  -36.409 18.773  0.52 23.99 ? 505 HOH   A O   1 
HETATM 5703 O O   B HOH   G 5 .   ? 29.070  -34.196 19.191  0.48 20.87 ? 505 HOH   A O   1 
HETATM 5704 O O   . HOH   G 5 .   ? 14.983  5.806   5.647   1.00 31.75 ? 506 HOH   A O   1 
HETATM 5705 O O   . HOH   G 5 .   ? 3.101   -8.413  2.411   1.00 35.55 ? 507 HOH   A O   1 
HETATM 5706 O O   . HOH   G 5 .   ? 8.096   -21.374 -12.909 1.00 29.86 ? 508 HOH   A O   1 
HETATM 5707 O O   . HOH   G 5 .   ? 37.914  -44.980 0.699   1.00 30.25 ? 509 HOH   A O   1 
HETATM 5708 O O   . HOH   G 5 .   ? 8.078   -38.122 9.513   1.00 28.46 ? 510 HOH   A O   1 
HETATM 5709 O O   . HOH   G 5 .   ? 19.449  1.595   -3.537  1.00 36.88 ? 511 HOH   A O   1 
HETATM 5710 O O   . HOH   G 5 .   ? 6.785   -14.829 26.863  1.00 44.48 ? 512 HOH   A O   1 
HETATM 5711 O O   . HOH   G 5 .   ? 9.302   3.105   -1.973  1.00 30.49 ? 513 HOH   A O   1 
HETATM 5712 O O   . HOH   G 5 .   ? 4.673   -22.295 -4.989  1.00 31.41 ? 514 HOH   A O   1 
HETATM 5713 O O   . HOH   G 5 .   ? 26.060  -11.021 17.060  1.00 22.90 ? 515 HOH   A O   1 
HETATM 5714 O O   . HOH   G 5 .   ? 20.170  -16.526 -3.864  1.00 17.08 ? 516 HOH   A O   1 
HETATM 5715 O O   . HOH   G 5 .   ? 27.385  -7.155  1.120   1.00 28.35 ? 517 HOH   A O   1 
HETATM 5716 O O   . HOH   G 5 .   ? 22.589  -33.719 24.882  1.00 23.73 ? 518 HOH   A O   1 
HETATM 5717 O O   . HOH   G 5 .   ? 30.409  -26.155 7.349   1.00 28.67 ? 519 HOH   A O   1 
HETATM 5718 O O   . HOH   G 5 .   ? 27.761  -24.030 5.226   1.00 28.73 ? 520 HOH   A O   1 
HETATM 5719 O O   . HOH   G 5 .   ? 26.065  -32.400 -25.393 1.00 30.76 ? 521 HOH   A O   1 
HETATM 5720 O O   . HOH   G 5 .   ? 36.616  -32.739 -23.389 1.00 31.43 ? 522 HOH   A O   1 
HETATM 5721 O O   . HOH   G 5 .   ? 26.049  -27.516 -18.451 1.00 29.30 ? 523 HOH   A O   1 
HETATM 5722 O O   . HOH   G 5 .   ? 16.254  -31.811 18.915  1.00 23.49 ? 524 HOH   A O   1 
HETATM 5723 O O   . HOH   G 5 .   ? 4.693   -19.167 3.329   1.00 31.08 ? 525 HOH   A O   1 
HETATM 5724 O O   . HOH   G 5 .   ? 31.140  -21.550 -8.971  1.00 20.91 ? 526 HOH   A O   1 
HETATM 5725 O O   . HOH   G 5 .   ? 0.647   -36.018 7.303   1.00 32.02 ? 527 HOH   A O   1 
HETATM 5726 O O   . HOH   G 5 .   ? 6.762   -31.891 15.309  1.00 37.51 ? 528 HOH   A O   1 
HETATM 5727 O O   . HOH   G 5 .   ? 15.880  -44.755 -4.843  1.00 29.13 ? 529 HOH   A O   1 
HETATM 5728 O O   . HOH   G 5 .   ? 25.510  -43.493 -1.655  1.00 24.18 ? 530 HOH   A O   1 
HETATM 5729 O O   . HOH   G 5 .   ? 7.900   -40.592 -1.764  1.00 26.00 ? 531 HOH   A O   1 
HETATM 5730 O O   . HOH   G 5 .   ? 28.949  -42.458 7.705   1.00 30.36 ? 532 HOH   A O   1 
HETATM 5731 O O   . HOH   G 5 .   ? 35.886  -21.006 22.914  1.00 37.74 ? 533 HOH   A O   1 
HETATM 5732 O O   . HOH   G 5 .   ? 25.975  -27.987 3.586   1.00 22.45 ? 534 HOH   A O   1 
HETATM 5733 O O   . HOH   G 5 .   ? 11.708  -20.238 -13.612 1.00 25.23 ? 535 HOH   A O   1 
HETATM 5734 O O   . HOH   G 5 .   ? 39.107  -37.009 -6.258  1.00 15.90 ? 536 HOH   A O   1 
HETATM 5735 O O   . HOH   G 5 .   ? 34.030  -43.622 -15.324 1.00 26.42 ? 537 HOH   A O   1 
HETATM 5736 O O   . HOH   G 5 .   ? 34.409  -31.019 -2.851  1.00 15.70 ? 538 HOH   A O   1 
HETATM 5737 O O   . HOH   G 5 .   ? 35.915  -18.326 -20.455 1.00 28.96 ? 539 HOH   A O   1 
HETATM 5738 O O   . HOH   G 5 .   ? 35.712  -27.202 2.903   1.00 17.73 ? 540 HOH   A O   1 
HETATM 5739 O O   . HOH   G 5 .   ? 41.493  -32.109 -15.525 1.00 25.40 ? 541 HOH   A O   1 
HETATM 5740 O O   . HOH   G 5 .   ? 20.959  -0.839  14.400  1.00 33.15 ? 542 HOH   A O   1 
HETATM 5741 O O   . HOH   G 5 .   ? 32.693  -19.329 -12.981 1.00 29.46 ? 543 HOH   A O   1 
HETATM 5742 O O   . HOH   G 5 .   ? 27.984  -20.674 -10.896 1.00 29.01 ? 544 HOH   A O   1 
HETATM 5743 O O   . HOH   G 5 .   ? 9.359   -17.779 -11.774 1.00 21.83 ? 545 HOH   A O   1 
HETATM 5744 O O   . HOH   G 5 .   ? 36.531  -37.056 -20.835 1.00 24.30 ? 546 HOH   A O   1 
HETATM 5745 O O   . HOH   G 5 .   ? 32.032  -37.943 -22.802 1.00 29.48 ? 547 HOH   A O   1 
HETATM 5746 O O   . HOH   G 5 .   ? 38.293  -29.109 -23.236 1.00 24.53 ? 548 HOH   A O   1 
HETATM 5747 O O   . HOH   G 5 .   ? 35.441  -36.511 -15.638 1.00 16.63 ? 549 HOH   A O   1 
HETATM 5748 O O   . HOH   G 5 .   ? 27.344  -24.845 -9.206  1.00 23.16 ? 550 HOH   A O   1 
HETATM 5749 O O   . HOH   G 5 .   ? 3.490   -12.361 -8.928  1.00 34.92 ? 551 HOH   A O   1 
HETATM 5750 O O   . HOH   G 5 .   ? 24.577  -24.586 24.207  1.00 17.54 ? 552 HOH   A O   1 
HETATM 5751 O O   . HOH   G 5 .   ? 25.071  -31.079 1.483   1.00 22.45 ? 553 HOH   A O   1 
HETATM 5752 O O   . HOH   G 5 .   ? 27.969  -32.450 17.591  1.00 18.87 ? 554 HOH   A O   1 
HETATM 5753 O O   . HOH   G 5 .   ? 26.412  -17.233 -3.122  1.00 26.54 ? 555 HOH   A O   1 
HETATM 5754 O O   . HOH   G 5 .   ? 31.325  -27.916 14.365  1.00 17.81 ? 556 HOH   A O   1 
HETATM 5755 O O   . HOH   G 5 .   ? 37.347  -36.960 -1.160  1.00 14.51 ? 557 HOH   A O   1 
HETATM 5756 O O   . HOH   G 5 .   ? 43.723  -38.440 -11.108 1.00 25.99 ? 558 HOH   A O   1 
HETATM 5757 O O   . HOH   G 5 .   ? 10.601  -23.919 22.653  1.00 27.23 ? 559 HOH   A O   1 
HETATM 5758 O O   . HOH   G 5 .   ? 8.041   -5.156  -0.885  1.00 33.93 ? 560 HOH   A O   1 
HETATM 5759 O O   . HOH   G 5 .   ? 16.826  -44.141 -11.817 1.00 36.21 ? 561 HOH   A O   1 
HETATM 5760 O O   . HOH   G 5 .   ? 4.624   -18.159 7.099   1.00 25.68 ? 562 HOH   A O   1 
HETATM 5761 O O   . HOH   G 5 .   ? 22.940  -25.066 20.915  1.00 20.67 ? 563 HOH   A O   1 
HETATM 5762 O O   . HOH   G 5 .   ? 19.768  -42.624 2.312   1.00 31.29 ? 564 HOH   A O   1 
HETATM 5763 O O   . HOH   G 5 .   ? 43.418  -30.644 5.050   1.00 30.86 ? 565 HOH   A O   1 
HETATM 5764 O O   . HOH   G 5 .   ? 25.706  -32.344 22.625  1.00 22.94 ? 566 HOH   A O   1 
HETATM 5765 O O   . HOH   G 5 .   ? 12.288  -42.632 3.304   1.00 34.25 ? 567 HOH   A O   1 
HETATM 5766 O O   . HOH   G 5 .   ? 18.756  -42.324 -17.076 1.00 31.14 ? 568 HOH   A O   1 
HETATM 5767 O O   . HOH   G 5 .   ? 30.010  -38.349 1.073   1.00 19.12 ? 569 HOH   A O   1 
HETATM 5768 O O   . HOH   G 5 .   ? 20.566  -16.182 25.870  1.00 28.25 ? 570 HOH   A O   1 
HETATM 5769 O O   . HOH   G 5 .   ? 43.212  -40.831 1.588   1.00 29.12 ? 571 HOH   A O   1 
HETATM 5770 O O   . HOH   G 5 .   ? 33.568  -30.304 -24.724 1.00 23.42 ? 572 HOH   A O   1 
HETATM 5771 O O   . HOH   G 5 .   ? 16.397  -38.542 8.968   1.00 28.19 ? 573 HOH   A O   1 
HETATM 5772 O O   . HOH   G 5 .   ? 33.372  -25.810 -23.618 1.00 18.89 ? 574 HOH   A O   1 
HETATM 5773 O O   . HOH   G 5 .   ? 31.798  -39.921 2.497   1.00 22.22 ? 575 HOH   A O   1 
HETATM 5774 O O   . HOH   G 5 .   ? 7.160   -3.544  7.195   1.00 32.25 ? 576 HOH   A O   1 
HETATM 5775 O O   . HOH   G 5 .   ? 34.289  -18.813 -10.754 1.00 30.26 ? 577 HOH   A O   1 
HETATM 5776 O O   . HOH   G 5 .   ? 21.080  0.616   8.778   1.00 32.66 ? 578 HOH   A O   1 
HETATM 5777 O O   . HOH   G 5 .   ? 38.623  -36.345 -17.723 1.00 20.72 ? 579 HOH   A O   1 
HETATM 5778 O O   . HOH   G 5 .   ? 35.809  -24.967 -0.056  1.00 19.08 ? 580 HOH   A O   1 
HETATM 5779 O O   . HOH   G 5 .   ? 18.643  -38.466 -18.648 1.00 28.74 ? 581 HOH   A O   1 
HETATM 5780 O O   . HOH   G 5 .   ? 12.223  -32.146 12.993  1.00 22.56 ? 582 HOH   A O   1 
HETATM 5781 O O   . HOH   G 5 .   ? 28.876  -28.937 21.004  1.00 20.10 ? 583 HOH   A O   1 
HETATM 5782 O O   . HOH   G 5 .   ? 16.320  -35.196 13.409  1.00 29.63 ? 584 HOH   A O   1 
HETATM 5783 O O   . HOH   G 5 .   ? 37.299  -25.073 -9.508  1.00 25.30 ? 585 HOH   A O   1 
HETATM 5784 O O   . HOH   G 5 .   ? 32.872  -32.738 -4.167  1.00 14.53 ? 586 HOH   A O   1 
HETATM 5785 O O   . HOH   G 5 .   ? 5.212   -18.323 -6.610  1.00 31.65 ? 587 HOH   A O   1 
HETATM 5786 O O   . HOH   G 5 .   ? 18.905  -13.274 2.634   1.00 21.21 ? 588 HOH   A O   1 
HETATM 5787 O O   . HOH   G 5 .   ? 31.995  -43.492 -5.711  1.00 19.59 ? 589 HOH   A O   1 
HETATM 5788 O O   . HOH   G 5 .   ? 3.761   -23.333 7.549   1.00 33.51 ? 590 HOH   A O   1 
HETATM 5789 O O   . HOH   G 5 .   ? 39.996  -19.705 -11.680 1.00 32.00 ? 591 HOH   A O   1 
HETATM 5790 O O   . HOH   G 5 .   ? 37.966  -31.335 -3.234  1.00 18.53 ? 592 HOH   A O   1 
HETATM 5791 O O   . HOH   G 5 .   ? 27.193  -30.390 19.311  1.00 19.23 ? 593 HOH   A O   1 
HETATM 5792 O O   . HOH   G 5 .   ? 26.962  -44.181 -16.123 1.00 31.79 ? 594 HOH   A O   1 
HETATM 5793 O O   . HOH   G 5 .   ? 2.711   -26.926 -9.437  1.00 35.11 ? 595 HOH   A O   1 
HETATM 5794 O O   . HOH   G 5 .   ? 18.497  -29.688 -17.110 1.00 33.98 ? 596 HOH   A O   1 
HETATM 5795 O O   . HOH   G 5 .   ? 4.300   -30.634 -5.573  1.00 23.66 ? 597 HOH   A O   1 
HETATM 5796 O O   . HOH   G 5 .   ? 18.428  1.162   7.537   1.00 35.63 ? 598 HOH   A O   1 
HETATM 5797 O O   . HOH   G 5 .   ? 40.342  -31.750 -2.078  1.00 30.09 ? 599 HOH   A O   1 
HETATM 5798 O O   . HOH   G 5 .   ? 26.140  -46.860 -9.367  1.00 32.17 ? 600 HOH   A O   1 
HETATM 5799 O O   . HOH   G 5 .   ? 34.923  -28.493 16.214  1.00 28.75 ? 601 HOH   A O   1 
HETATM 5800 O O   . HOH   G 5 .   ? -1.415  -33.532 7.926   1.00 25.66 ? 602 HOH   A O   1 
HETATM 5801 O O   . HOH   G 5 .   ? 35.352  -25.730 -19.464 1.00 21.89 ? 603 HOH   A O   1 
HETATM 5802 O O   . HOH   G 5 .   ? 40.165  -28.436 -4.543  1.00 27.82 ? 604 HOH   A O   1 
HETATM 5803 O O   . HOH   G 5 .   ? 14.743  -41.289 -13.200 1.00 26.75 ? 605 HOH   A O   1 
HETATM 5804 O O   . HOH   G 5 .   ? 6.555   -22.032 -6.707  1.00 26.23 ? 606 HOH   A O   1 
HETATM 5805 O O   . HOH   G 5 .   ? 24.054  -31.404 -21.814 1.00 34.76 ? 607 HOH   A O   1 
HETATM 5806 O O   . HOH   G 5 .   ? 28.076  -45.875 -5.593  1.00 33.08 ? 608 HOH   A O   1 
HETATM 5807 O O   . HOH   G 5 .   ? 24.384  -9.703  18.684  1.00 29.74 ? 609 HOH   A O   1 
HETATM 5808 O O   . HOH   G 5 .   ? 41.071  -34.395 -18.838 1.00 29.33 ? 610 HOH   A O   1 
HETATM 5809 O O   . HOH   G 5 .   ? 37.467  -20.785 -8.437  1.00 28.33 ? 611 HOH   A O   1 
HETATM 5810 O O   . HOH   G 5 .   ? 36.008  -33.145 -1.841  1.00 14.57 ? 612 HOH   A O   1 
HETATM 5811 O O   . HOH   G 5 .   ? 39.624  -41.997 -5.485  1.00 22.19 ? 613 HOH   A O   1 
HETATM 5812 O O   . HOH   G 5 .   ? 32.932  -26.888 22.458  1.00 32.53 ? 614 HOH   A O   1 
HETATM 5813 O O   . HOH   G 5 .   ? 38.401  -29.366 -10.063 1.00 20.74 ? 615 HOH   A O   1 
HETATM 5814 O O   . HOH   G 5 .   ? 6.499   -11.353 -2.296  1.00 26.17 ? 616 HOH   A O   1 
HETATM 5815 O O   . HOH   G 5 .   ? 36.096  -36.086 12.408  1.00 26.54 ? 617 HOH   A O   1 
HETATM 5816 O O   . HOH   G 5 .   ? 10.253  -10.804 3.821   1.00 20.42 ? 618 HOH   A O   1 
HETATM 5817 O O   . HOH   G 5 .   ? 4.160   -11.107 -1.318  1.00 31.94 ? 619 HOH   A O   1 
HETATM 5818 O O   . HOH   G 5 .   ? 25.744  -15.375 21.699  1.00 28.63 ? 620 HOH   A O   1 
HETATM 5819 O O   . HOH   G 5 .   ? 15.680  -35.784 -18.471 1.00 33.76 ? 621 HOH   A O   1 
HETATM 5820 O O   . HOH   G 5 .   ? 37.410  -22.839 14.776  1.00 36.64 ? 622 HOH   A O   1 
HETATM 5821 O O   . HOH   G 5 .   ? 23.015  -20.258 16.470  1.00 17.07 ? 623 HOH   A O   1 
HETATM 5822 O O   . HOH   G 5 .   ? 17.020  -24.024 23.686  1.00 32.82 ? 624 HOH   A O   1 
HETATM 5823 O O   . HOH   G 5 .   ? 38.060  -30.165 -15.239 1.00 18.26 ? 625 HOH   A O   1 
HETATM 5824 O O   . HOH   G 5 .   ? 24.990  -25.965 -16.476 1.00 33.24 ? 626 HOH   A O   1 
HETATM 5825 O O   . HOH   G 5 .   ? 22.128  -26.479 -16.094 1.00 33.58 ? 627 HOH   A O   1 
HETATM 5826 O O   . HOH   G 5 .   ? 21.516  -31.615 -20.145 1.00 35.22 ? 628 HOH   A O   1 
HETATM 5827 O O   . HOH   G 5 .   ? 5.051   -31.317 -9.997  1.00 33.65 ? 629 HOH   A O   1 
HETATM 5828 O O   . HOH   G 5 .   ? 7.026   -20.195 -4.161  1.00 24.63 ? 630 HOH   A O   1 
HETATM 5829 O O   . HOH   G 5 .   ? 11.098  -2.367  7.760   1.00 22.14 ? 631 HOH   A O   1 
HETATM 5830 O O   . HOH   G 5 .   ? 37.203  -25.794 12.869  1.00 29.94 ? 632 HOH   A O   1 
HETATM 5831 O O   . HOH   G 5 .   ? 7.916   1.541   2.567   1.00 21.85 ? 633 HOH   A O   1 
HETATM 5832 O O   . HOH   G 5 .   ? 19.565  -44.244 -2.321  1.00 21.03 ? 634 HOH   A O   1 
HETATM 5833 O O   . HOH   G 5 .   ? 4.651   -11.464 13.915  1.00 27.27 ? 635 HOH   A O   1 
HETATM 5834 O O   . HOH   G 5 .   ? 37.670  -24.171 -2.073  1.00 23.14 ? 636 HOH   A O   1 
HETATM 5835 O O   . HOH   G 5 .   ? 0.972   -28.152 -0.805  1.00 30.69 ? 637 HOH   A O   1 
HETATM 5836 O O   . HOH   G 5 .   ? 7.614   -19.917 -7.708  1.00 25.10 ? 638 HOH   A O   1 
HETATM 5837 O O   . HOH   G 5 .   ? 23.850  -42.526 3.708   1.00 24.05 ? 639 HOH   A O   1 
HETATM 5838 O O   . HOH   G 5 .   ? 35.348  -29.415 5.040   1.00 15.29 ? 640 HOH   A O   1 
HETATM 5839 O O   . HOH   G 5 .   ? 13.676  -3.284  -3.867  1.00 34.98 ? 641 HOH   A O   1 
HETATM 5840 O O   . HOH   G 5 .   ? 2.778   -13.161 6.766   1.00 35.15 ? 642 HOH   A O   1 
HETATM 5841 O O   . HOH   G 5 .   ? 1.489   -18.427 13.432  1.00 34.76 ? 643 HOH   A O   1 
HETATM 5842 O O   . HOH   G 5 .   ? 18.705  -46.010 -9.825  1.00 33.08 ? 644 HOH   A O   1 
HETATM 5843 O O   . HOH   G 5 .   ? 26.649  -23.256 7.683   1.00 23.47 ? 645 HOH   A O   1 
HETATM 5844 O O   . HOH   G 5 .   ? 37.855  -18.889 10.673  1.00 32.02 ? 646 HOH   A O   1 
HETATM 5845 O O   . HOH   G 5 .   ? 9.566   -38.537 -2.293  1.00 21.38 ? 647 HOH   A O   1 
HETATM 5846 O O   . HOH   G 5 .   ? 16.537  -31.564 -16.735 1.00 23.27 ? 648 HOH   A O   1 
HETATM 5847 O O   . HOH   G 5 .   ? -0.735  -22.114 14.667  1.00 37.93 ? 649 HOH   A O   1 
HETATM 5848 O O   . HOH   G 5 .   ? 44.084  -34.504 -10.660 1.00 30.18 ? 650 HOH   A O   1 
HETATM 5849 O O   . HOH   G 5 .   ? 19.010  -11.638 25.033  1.00 40.50 ? 651 HOH   A O   1 
HETATM 5850 O O   . HOH   G 5 .   ? 18.408  -28.211 -15.128 1.00 22.09 ? 652 HOH   A O   1 
HETATM 5851 O O   . HOH   G 5 .   ? 37.590  -27.378 -8.437  1.00 22.25 ? 653 HOH   A O   1 
HETATM 5852 O O   . HOH   G 5 .   ? 25.365  -20.482 -20.434 1.00 26.06 ? 654 HOH   A O   1 
HETATM 5853 O O   . HOH   G 5 .   ? 3.979   -23.430 -9.532  1.00 37.78 ? 655 HOH   A O   1 
HETATM 5854 O O   . HOH   G 5 .   ? 22.522  -36.098 21.463  1.00 26.62 ? 656 HOH   A O   1 
HETATM 5855 O O   . HOH   G 5 .   ? 22.234  -14.760 1.392   1.00 21.82 ? 657 HOH   A O   1 
HETATM 5856 O O   . HOH   G 5 .   ? 34.934  -42.017 4.163   1.00 34.01 ? 658 HOH   A O   1 
HETATM 5857 O O   . HOH   G 5 .   ? 31.395  -25.587 4.981   1.00 18.13 ? 659 HOH   A O   1 
HETATM 5858 O O   . HOH   G 5 .   ? 33.719  -27.291 19.674  1.00 31.62 ? 660 HOH   A O   1 
HETATM 5859 O O   . HOH   G 5 .   ? 25.026  -45.296 -11.782 1.00 25.68 ? 661 HOH   A O   1 
HETATM 5860 O O   . HOH   G 5 .   ? 40.703  -32.127 -12.940 1.00 20.68 ? 662 HOH   A O   1 
HETATM 5861 O O   . HOH   G 5 .   ? 14.545  -29.757 4.225   1.00 21.15 ? 663 HOH   A O   1 
HETATM 5862 O O   . HOH   G 5 .   ? 28.322  -22.376 24.685  1.00 25.85 ? 664 HOH   A O   1 
HETATM 5863 O O   . HOH   G 5 .   ? 4.485   -33.406 -4.993  1.00 27.12 ? 665 HOH   A O   1 
HETATM 5864 O O   . HOH   G 5 .   ? 42.935  -31.966 -11.302 1.00 24.57 ? 666 HOH   A O   1 
HETATM 5865 O O   . HOH   G 5 .   ? 16.824  7.673   -0.143  1.00 39.45 ? 667 HOH   A O   1 
HETATM 5866 O O   . HOH   G 5 .   ? 5.085   -6.393  6.651   1.00 29.93 ? 668 HOH   A O   1 
HETATM 5867 O O   . HOH   G 5 .   ? 7.122   -25.129 15.711  1.00 32.74 ? 669 HOH   A O   1 
HETATM 5868 O O   . HOH   G 5 .   ? 2.660   -37.768 -1.346  1.00 23.37 ? 670 HOH   A O   1 
HETATM 5869 O O   . HOH   G 5 .   ? 4.851   -42.179 -3.813  1.00 32.99 ? 671 HOH   A O   1 
HETATM 5870 O O   . HOH   G 5 .   ? 13.690  -34.079 28.597  1.00 38.47 ? 672 HOH   A O   1 
HETATM 5871 O O   . HOH   G 5 .   ? 31.660  -42.166 0.620   1.00 22.32 ? 673 HOH   A O   1 
HETATM 5872 O O   . HOH   G 5 .   ? 26.220  -22.509 -22.908 1.00 19.24 ? 674 HOH   A O   1 
HETATM 5873 O O   . HOH   G 5 .   ? 14.618  -33.437 12.604  1.00 30.14 ? 675 HOH   A O   1 
HETATM 5874 O O   . HOH   G 5 .   ? 7.123   -1.222  2.779   1.00 32.82 ? 676 HOH   A O   1 
HETATM 5875 O O   . HOH   G 5 .   ? 35.289  -34.575 -24.373 1.00 31.42 ? 677 HOH   A O   1 
HETATM 5876 O O   . HOH   G 5 .   ? 20.558  -38.454 24.732  1.00 31.04 ? 678 HOH   A O   1 
HETATM 5877 O O   . HOH   G 5 .   ? 28.613  -40.268 16.195  1.00 48.33 ? 679 HOH   A O   1 
HETATM 5878 O O   . HOH   G 5 .   ? 31.068  -22.490 23.615  1.00 21.89 ? 680 HOH   A O   1 
HETATM 5879 O O   . HOH   G 5 .   ? 35.644  -28.130 13.538  1.00 27.19 ? 681 HOH   A O   1 
HETATM 5880 O O   . HOH   G 5 .   ? 27.669  -21.178 3.123   1.00 28.96 ? 682 HOH   A O   1 
HETATM 5881 O O   . HOH   G 5 .   ? 28.109  -42.891 -0.615  1.00 25.40 ? 683 HOH   A O   1 
HETATM 5882 O O   . HOH   G 5 .   ? 37.199  -21.822 -5.653  1.00 20.07 ? 684 HOH   A O   1 
HETATM 5883 O O   . HOH   G 5 .   ? 40.190  -22.043 10.734  1.00 26.88 ? 685 HOH   A O   1 
HETATM 5884 O O   . HOH   G 5 .   ? 17.186  -24.519 -14.403 1.00 30.72 ? 686 HOH   A O   1 
HETATM 5885 O O   . HOH   G 5 .   ? 13.023  -40.464 4.363   1.00 24.01 ? 687 HOH   A O   1 
HETATM 5886 O O   . HOH   G 5 .   ? 43.552  -39.019 -0.415  1.00 28.45 ? 688 HOH   A O   1 
HETATM 5887 O O   . HOH   G 5 .   ? 8.136   -12.616 -15.595 1.00 31.15 ? 689 HOH   A O   1 
HETATM 5888 O O   . HOH   G 5 .   ? 22.145  -36.397 -21.217 1.00 31.78 ? 690 HOH   A O   1 
HETATM 5889 O O   . HOH   G 5 .   ? 8.080   -5.744  12.360  1.00 29.40 ? 691 HOH   A O   1 
HETATM 5890 O O   . HOH   G 5 .   ? 15.385  -5.161  23.808  1.00 40.70 ? 692 HOH   A O   1 
HETATM 5891 O O   . HOH   G 5 .   ? 28.563  -22.883 -29.525 1.00 21.19 ? 693 HOH   A O   1 
HETATM 5892 O O   . HOH   G 5 .   ? 42.444  -21.885 9.021   1.00 37.81 ? 694 HOH   A O   1 
HETATM 5893 O O   . HOH   G 5 .   ? 37.666  -27.791 -19.077 1.00 27.56 ? 695 HOH   A O   1 
HETATM 5894 O O   . HOH   G 5 .   ? 16.308  -34.683 17.943  1.00 26.65 ? 696 HOH   A O   1 
HETATM 5895 O O   . HOH   G 5 .   ? 10.600  -40.768 6.140   1.00 28.07 ? 697 HOH   A O   1 
HETATM 5896 O O   . HOH   G 5 .   ? 33.516  -17.616 -22.112 1.00 27.44 ? 698 HOH   A O   1 
HETATM 5897 O O   . HOH   G 5 .   ? 19.350  -18.667 -9.922  1.00 30.31 ? 699 HOH   A O   1 
HETATM 5898 O O   . HOH   G 5 .   ? 2.649   -31.580 -0.633  1.00 37.96 ? 700 HOH   A O   1 
HETATM 5899 O O   . HOH   G 5 .   ? 1.326   -24.524 -2.583  1.00 39.37 ? 701 HOH   A O   1 
HETATM 5900 O O   . HOH   G 5 .   ? 13.361  -44.661 -0.934  1.00 31.96 ? 702 HOH   A O   1 
HETATM 5901 O O   . HOH   G 5 .   ? 10.812  -20.830 30.335  1.00 45.17 ? 703 HOH   A O   1 
HETATM 5902 O O   . HOH   G 5 .   ? 15.897  -13.658 -10.386 1.00 29.57 ? 704 HOH   A O   1 
HETATM 5903 O O   . HOH   G 5 .   ? 4.243   -34.051 -1.518  1.00 27.89 ? 705 HOH   A O   1 
HETATM 5904 O O   . HOH   G 5 .   ? 35.883  -22.969 -20.329 1.00 31.57 ? 706 HOH   A O   1 
HETATM 5905 O O   . HOH   G 5 .   ? 10.392  -0.878  -3.999  1.00 43.90 ? 707 HOH   A O   1 
HETATM 5906 O O   . HOH   G 5 .   ? 28.249  -41.540 3.402   1.00 36.49 ? 708 HOH   A O   1 
HETATM 5907 O O   . HOH   G 5 .   ? -0.608  -35.871 9.646   1.00 32.70 ? 709 HOH   A O   1 
HETATM 5908 O O   . HOH   G 5 .   ? 26.380  -42.476 4.483   1.00 32.51 ? 710 HOH   A O   1 
HETATM 5909 O O   . HOH   G 5 .   ? 4.958   1.488   -0.635  1.00 39.85 ? 711 HOH   A O   1 
HETATM 5910 O O   . HOH   G 5 .   ? 20.967  -21.191 18.036  1.00 21.37 ? 712 HOH   A O   1 
HETATM 5911 O O   . HOH   G 5 .   ? 21.798  -18.698 -9.915  1.00 30.57 ? 713 HOH   A O   1 
HETATM 5912 O O   . HOH   G 5 .   ? 2.096   -29.655 -4.068  1.00 29.37 ? 714 HOH   A O   1 
HETATM 5913 O O   . HOH   G 5 .   ? 37.420  -39.534 -20.083 1.00 22.63 ? 715 HOH   A O   1 
HETATM 5914 O O   . HOH   G 5 .   ? 13.904  -30.826 -19.179 1.00 38.05 ? 716 HOH   A O   1 
HETATM 5915 O O   . HOH   G 5 .   ? 13.169  -23.594 23.690  1.00 34.36 ? 717 HOH   A O   1 
HETATM 5916 O O   . HOH   G 5 .   ? 7.111   -18.803 -10.056 1.00 30.72 ? 718 HOH   A O   1 
HETATM 5917 O O   . HOH   G 5 .   ? 33.154  -28.403 12.464  1.00 26.92 ? 719 HOH   A O   1 
HETATM 5918 O O   . HOH   G 5 .   ? 38.702  -23.483 -19.737 1.00 33.69 ? 720 HOH   A O   1 
HETATM 5919 O O   . HOH   G 5 .   ? 25.909  -27.872 -22.829 1.00 30.43 ? 721 HOH   A O   1 
HETATM 5920 O O   . HOH   G 5 .   ? 28.272  -32.920 21.998  1.00 30.46 ? 722 HOH   A O   1 
HETATM 5921 O O   . HOH   G 5 .   ? 15.258  -33.352 -18.736 1.00 32.09 ? 723 HOH   A O   1 
HETATM 5922 O O   . HOH   G 5 .   ? 2.113   -15.992 10.104  1.00 38.07 ? 724 HOH   A O   1 
HETATM 5923 O O   . HOH   G 5 .   ? 5.607   -21.124 -11.284 1.00 40.51 ? 725 HOH   A O   1 
HETATM 5924 O O   . HOH   G 5 .   ? 29.435  -15.524 -20.019 1.00 36.26 ? 726 HOH   A O   1 
HETATM 5925 O O   . HOH   G 5 .   ? 28.576  -22.561 -9.136  1.00 22.70 ? 727 HOH   A O   1 
HETATM 5926 O O   . HOH   G 5 .   ? 25.220  -45.864 -14.688 1.00 37.05 ? 728 HOH   A O   1 
HETATM 5927 O O   . HOH   G 5 .   ? 36.145  -19.615 -24.766 1.00 31.45 ? 729 HOH   A O   1 
HETATM 5928 O O   . HOH   G 5 .   ? 39.623  -23.646 -9.603  1.00 32.75 ? 730 HOH   A O   1 
HETATM 5929 O O   . HOH   G 5 .   ? 23.686  -44.022 0.433   1.00 34.62 ? 731 HOH   A O   1 
HETATM 5930 O O   . HOH   G 5 .   ? 17.369  -30.315 26.026  1.00 35.11 ? 732 HOH   A O   1 
HETATM 5931 O O   . HOH   G 5 .   ? 24.399  -28.476 -20.384 1.00 38.13 ? 733 HOH   A O   1 
HETATM 5932 O O   . HOH   G 5 .   ? 4.028   -3.131  3.342   1.00 38.52 ? 734 HOH   A O   1 
HETATM 5933 O O   . HOH   G 5 .   ? 29.904  -23.259 4.408   1.00 27.98 ? 735 HOH   A O   1 
HETATM 5934 O O   . HOH   G 5 .   ? 19.744  -16.052 28.328  1.00 30.12 ? 736 HOH   A O   1 
HETATM 5935 O O   . HOH   G 5 .   ? 32.366  -24.634 25.167  1.00 29.10 ? 737 HOH   A O   1 
HETATM 5936 O O   . HOH   G 5 .   ? 31.538  -41.462 4.593   1.00 30.33 ? 738 HOH   A O   1 
HETATM 5937 O O   . HOH   G 5 .   ? -3.195  -22.830 -5.195  1.00 30.51 ? 739 HOH   A O   1 
HETATM 5938 O O   . HOH   G 5 .   ? 34.662  -17.313 -24.518 1.00 26.67 ? 740 HOH   A O   1 
HETATM 5939 O O   . HOH   G 5 .   ? 32.008  -20.128 23.891  1.00 33.37 ? 741 HOH   A O   1 
HETATM 5940 O O   . HOH   G 5 .   ? 21.982  -36.392 24.246  1.00 31.19 ? 742 HOH   A O   1 
HETATM 5941 O O   . HOH   G 5 .   ? 25.051  -16.015 24.130  1.00 24.33 ? 743 HOH   A O   1 
HETATM 5942 O O   . HOH   G 5 .   ? 30.970  -19.736 -11.004 1.00 32.18 ? 744 HOH   A O   1 
HETATM 5943 O O   . HOH   G 5 .   ? 7.281   -3.401  9.784   1.00 36.44 ? 745 HOH   A O   1 
HETATM 5944 O O   . HOH   G 5 .   ? 39.094  -29.894 -12.673 1.00 19.28 ? 746 HOH   A O   1 
HETATM 5945 O O   . HOH   G 5 .   ? 36.460  -30.438 -24.848 1.00 26.49 ? 747 HOH   A O   1 
HETATM 5946 O O   . HOH   G 5 .   ? 28.786  -40.853 0.973   1.00 26.92 ? 748 HOH   A O   1 
HETATM 5947 O O   . HOH   G 5 .   ? 5.874   -1.482  4.867   1.00 35.86 ? 749 HOH   A O   1 
HETATM 5948 O O   . HOH   G 5 .   ? 20.474  -44.187 0.359   1.00 31.30 ? 750 HOH   A O   1 
HETATM 5949 O O   . HOH   G 5 .   ? 38.232  -26.293 -22.836 1.00 25.66 ? 751 HOH   A O   1 
HETATM 5950 O O   . HOH   G 5 .   ? 36.204  -24.071 23.220  1.00 35.30 ? 752 HOH   A O   1 
HETATM 5951 O O   . HOH   G 5 .   ? 30.151  -30.922 22.657  1.00 22.64 ? 753 HOH   A O   1 
HETATM 5952 O O   . HOH   G 5 .   ? 35.796  -24.806 -22.932 1.00 29.62 ? 754 HOH   A O   1 
HETATM 5953 O O   . HOH   G 5 .   ? 11.099  -34.332 28.260  1.00 39.72 ? 755 HOH   A O   1 
HETATM 5954 O O   . HOH   G 5 .   ? 34.730  -20.759 25.177  1.00 36.96 ? 756 HOH   A O   1 
HETATM 5955 O O   . HOH   G 5 .   ? 34.693  -37.198 -22.901 1.00 25.65 ? 757 HOH   A O   1 
HETATM 5956 O O   . HOH   G 5 .   ? 31.451  -15.976 -21.610 1.00 32.33 ? 758 HOH   A O   1 
HETATM 5957 O O   . HOH   G 5 .   ? 40.822  -24.444 -7.233  1.00 30.79 ? 759 HOH   A O   1 
HETATM 5958 O O   . HOH   G 5 .   ? 40.478  -27.617 -13.032 1.00 31.13 ? 760 HOH   A O   1 
HETATM 5959 O O   . HOH   H 5 .   ? 10.061  29.702  1.877   1.00 30.71 ? 501 HOH   B O   1 
HETATM 5960 O O   . HOH   H 5 .   ? -7.137  7.236   4.077   1.00 28.88 ? 502 HOH   B O   1 
HETATM 5961 O O   . HOH   H 5 .   ? 3.947   2.469   13.695  1.00 37.88 ? 503 HOH   B O   1 
HETATM 5962 O O   . HOH   H 5 .   ? -16.551 26.232  3.100   1.00 35.69 ? 504 HOH   B O   1 
HETATM 5963 O O   . HOH   H 5 .   ? -4.182  4.324   21.947  1.00 41.60 ? 505 HOH   B O   1 
HETATM 5964 O O   . HOH   H 5 .   ? 2.952   19.689  16.631  1.00 26.09 ? 506 HOH   B O   1 
HETATM 5965 O O   . HOH   H 5 .   ? 6.377   31.314  21.695  1.00 37.54 ? 507 HOH   B O   1 
HETATM 5966 O O   . HOH   H 5 .   ? 3.449   28.603  9.406   1.00 28.84 ? 508 HOH   B O   1 
HETATM 5967 O O   . HOH   H 5 .   ? -11.694 26.137  -5.921  1.00 32.57 ? 509 HOH   B O   1 
HETATM 5968 O O   . HOH   H 5 .   ? -1.440  44.779  2.098   1.00 30.53 ? 510 HOH   B O   1 
HETATM 5969 O O   . HOH   H 5 .   ? -2.865  26.679  -9.039  1.00 30.40 ? 511 HOH   B O   1 
HETATM 5970 O O   . HOH   H 5 .   ? 2.847   42.815  15.723  1.00 27.41 ? 512 HOH   B O   1 
HETATM 5971 O O   . HOH   H 5 .   ? -4.042  5.205   11.664  1.00 33.48 ? 513 HOH   B O   1 
HETATM 5972 O O   . HOH   H 5 .   ? -8.613  14.095  26.043  1.00 48.46 ? 514 HOH   B O   1 
HETATM 5973 O O   . HOH   H 5 .   ? -0.038  31.417  7.849   1.00 24.67 ? 515 HOH   B O   1 
HETATM 5974 O O   . HOH   H 5 .   ? -3.221  32.907  37.347  1.00 34.04 ? 516 HOH   B O   1 
HETATM 5975 O O   . HOH   H 5 .   ? -10.537 40.631  -3.047  1.00 43.84 ? 517 HOH   B O   1 
HETATM 5976 O O   . HOH   H 5 .   ? -17.816 16.196  18.860  1.00 39.41 ? 518 HOH   B O   1 
HETATM 5977 O O   . HOH   H 5 .   ? 5.820   46.617  8.113   1.00 29.06 ? 519 HOH   B O   1 
HETATM 5978 O O   . HOH   H 5 .   ? -5.309  32.573  11.323  1.00 23.88 ? 520 HOH   B O   1 
HETATM 5979 O O   . HOH   H 5 .   ? 7.449   2.709   0.254   1.00 23.30 ? 521 HOH   B O   1 
HETATM 5980 O O   . HOH   H 5 .   ? 2.201   33.117  5.128   1.00 29.37 ? 522 HOH   B O   1 
HETATM 5981 O O   . HOH   H 5 .   ? 1.430   30.229  21.705  1.00 36.79 ? 523 HOH   B O   1 
HETATM 5982 O O   . HOH   H 5 .   ? 20.511  10.868  1.336   1.00 34.88 ? 524 HOH   B O   1 
HETATM 5983 O O   . HOH   H 5 .   ? -2.096  45.878  13.713  1.00 20.10 ? 525 HOH   B O   1 
HETATM 5984 O O   . HOH   H 5 .   ? -2.353  31.285  9.083   1.00 19.35 ? 526 HOH   B O   1 
HETATM 5985 O O   . HOH   H 5 .   ? -25.715 21.824  4.787   1.00 38.42 ? 527 HOH   B O   1 
HETATM 5986 O O   . HOH   H 5 .   ? -2.511  2.345   3.826   1.00 41.29 ? 528 HOH   B O   1 
HETATM 5987 O O   . HOH   H 5 .   ? -0.967  47.301  18.657  1.00 23.70 ? 529 HOH   B O   1 
HETATM 5988 O O   . HOH   H 5 .   ? -3.730  33.427  -6.855  1.00 26.31 ? 530 HOH   B O   1 
HETATM 5989 O O   . HOH   H 5 .   ? 9.107   35.382  -2.735  1.00 36.60 ? 531 HOH   B O   1 
HETATM 5990 O O   . HOH   H 5 .   ? 6.338   38.131  -0.189  1.00 35.05 ? 532 HOH   B O   1 
HETATM 5991 O O   . HOH   H 5 .   ? -13.956 12.521  8.203   1.00 31.49 ? 533 HOH   B O   1 
HETATM 5992 O O   . HOH   H 5 .   ? 2.839   19.155  -12.968 1.00 34.15 ? 534 HOH   B O   1 
HETATM 5993 O O   . HOH   H 5 .   ? 8.394   27.508  16.508  1.00 37.80 ? 535 HOH   B O   1 
HETATM 5994 O O   . HOH   H 5 .   ? -4.815  15.547  26.417  1.00 43.75 ? 536 HOH   B O   1 
HETATM 5995 O O   . HOH   H 5 .   ? 6.292   36.747  12.679  1.00 26.37 ? 537 HOH   B O   1 
HETATM 5996 O O   . HOH   H 5 .   ? -6.442  33.286  -10.188 1.00 29.89 ? 538 HOH   B O   1 
HETATM 5997 O O   . HOH   H 5 .   ? -11.187 11.428  18.185  1.00 40.97 ? 539 HOH   B O   1 
HETATM 5998 O O   . HOH   H 5 .   ? -8.047  38.092  -6.164  1.00 38.32 ? 540 HOH   B O   1 
HETATM 5999 O O   . HOH   H 5 .   ? -9.200  5.775   18.007  1.00 36.51 ? 541 HOH   B O   1 
HETATM 6000 O O   . HOH   H 5 .   ? -10.758 33.484  -8.692  1.00 34.11 ? 542 HOH   B O   1 
HETATM 6001 O O   . HOH   H 5 .   ? 4.533   38.074  9.773   1.00 23.40 ? 543 HOH   B O   1 
HETATM 6002 O O   . HOH   H 5 .   ? 3.964   30.507  5.569   1.00 30.90 ? 544 HOH   B O   1 
HETATM 6003 O O   . HOH   H 5 .   ? -12.968 11.329  5.715   1.00 27.55 ? 545 HOH   B O   1 
HETATM 6004 O O   . HOH   H 5 .   ? -1.567  39.671  16.806  1.00 22.41 ? 546 HOH   B O   1 
HETATM 6005 O O   . HOH   H 5 .   ? -9.860  12.622  19.681  1.00 36.38 ? 547 HOH   B O   1 
HETATM 6006 O O   . HOH   H 5 .   ? 6.919   24.839  7.795   1.00 24.65 ? 548 HOH   B O   1 
HETATM 6007 O O   . HOH   H 5 .   ? -5.982  4.077   6.468   1.00 36.65 ? 549 HOH   B O   1 
HETATM 6008 O O   . HOH   H 5 .   ? 4.250   1.009   5.213   1.00 32.81 ? 550 HOH   B O   1 
HETATM 6009 O O   . HOH   H 5 .   ? -4.409  35.204  -4.971  1.00 23.06 ? 551 HOH   B O   1 
HETATM 6010 O O   . HOH   H 5 .   ? 0.750   39.724  15.552  1.00 24.45 ? 552 HOH   B O   1 
HETATM 6011 O O   . HOH   H 5 .   ? -4.974  12.150  24.559  1.00 39.98 ? 553 HOH   B O   1 
HETATM 6012 O O   . HOH   H 5 .   ? -11.108 43.027  5.348   1.00 29.09 ? 554 HOH   B O   1 
HETATM 6013 O O   . HOH   H 5 .   ? -15.606 41.765  24.797  1.00 39.73 ? 555 HOH   B O   1 
HETATM 6014 O O   . HOH   H 5 .   ? -8.626  8.578   6.004   1.00 27.15 ? 556 HOH   B O   1 
HETATM 6015 O O   . HOH   H 5 .   ? -16.454 30.492  3.951   1.00 31.06 ? 557 HOH   B O   1 
HETATM 6016 O O   . HOH   H 5 .   ? 5.354   19.661  11.268  1.00 23.63 ? 558 HOH   B O   1 
HETATM 6017 O O   . HOH   H 5 .   ? 8.649   29.903  -0.739  1.00 33.41 ? 559 HOH   B O   1 
HETATM 6018 O O   . HOH   H 5 .   ? -7.783  43.266  9.976   1.00 26.68 ? 560 HOH   B O   1 
HETATM 6019 O O   . HOH   H 5 .   ? -7.500  8.887   19.733  1.00 37.18 ? 561 HOH   B O   1 
HETATM 6020 O O   . HOH   H 5 .   ? 0.690   8.027   9.273   1.00 21.42 ? 562 HOH   B O   1 
HETATM 6021 O O   . HOH   H 5 .   ? -0.286  51.974  7.639   1.00 22.81 ? 563 HOH   B O   1 
HETATM 6022 O O   . HOH   H 5 .   ? -7.341  11.781  20.696  1.00 35.71 ? 564 HOH   B O   1 
HETATM 6023 O O   . HOH   H 5 .   ? 1.141   34.994  -2.011  1.00 21.59 ? 565 HOH   B O   1 
HETATM 6024 O O   . HOH   H 5 .   ? -8.172  11.631  17.304  1.00 34.07 ? 566 HOH   B O   1 
HETATM 6025 O O   . HOH   H 5 .   ? -1.480  33.431  -8.731  1.00 25.44 ? 567 HOH   B O   1 
HETATM 6026 O O   . HOH   H 5 .   ? -9.682  34.759  38.842  1.00 30.84 ? 568 HOH   B O   1 
HETATM 6027 O O   . HOH   H 5 .   ? 2.903   29.739  3.128   1.00 30.30 ? 569 HOH   B O   1 
HETATM 6028 O O   . HOH   H 5 .   ? 0.238   51.425  12.891  1.00 25.64 ? 570 HOH   B O   1 
HETATM 6029 O O   . HOH   H 5 .   ? 10.133  19.959  -4.601  1.00 28.71 ? 571 HOH   B O   1 
HETATM 6030 O O   . HOH   H 5 .   ? -9.726  9.445   10.234  1.00 33.61 ? 572 HOH   B O   1 
HETATM 6031 O O   . HOH   H 5 .   ? -15.843 12.640  22.726  1.00 44.67 ? 573 HOH   B O   1 
HETATM 6032 O O   . HOH   H 5 .   ? 1.703   28.559  6.186   1.00 25.98 ? 574 HOH   B O   1 
HETATM 6033 O O   . HOH   H 5 .   ? -2.118  43.921  -0.369  1.00 30.68 ? 575 HOH   B O   1 
HETATM 6034 O O   . HOH   H 5 .   ? 6.773   9.051   14.520  1.00 31.12 ? 576 HOH   B O   1 
HETATM 6035 O O   . HOH   H 5 .   ? -1.729  5.716   15.419  1.00 27.63 ? 577 HOH   B O   1 
HETATM 6036 O O   . HOH   H 5 .   ? -3.586  3.753   13.888  1.00 38.88 ? 578 HOH   B O   1 
HETATM 6037 O O   . HOH   H 5 .   ? -21.441 24.057  3.755   1.00 43.93 ? 579 HOH   B O   1 
HETATM 6038 O O   . HOH   H 5 .   ? -7.405  48.364  3.606   1.00 23.59 ? 580 HOH   B O   1 
HETATM 6039 O O   . HOH   H 5 .   ? -14.565 23.191  0.013   1.00 29.42 ? 581 HOH   B O   1 
HETATM 6040 O O   . HOH   H 5 .   ? -19.445 12.657  6.553   1.00 41.34 ? 582 HOH   B O   1 
HETATM 6041 O O   . HOH   H 5 .   ? 0.153   42.279  14.498  1.00 19.99 ? 583 HOH   B O   1 
HETATM 6042 O O   . HOH   H 5 .   ? 10.018  32.398  5.612   1.00 32.70 ? 584 HOH   B O   1 
HETATM 6043 O O   . HOH   H 5 .   ? 1.328   23.523  -3.756  1.00 20.58 ? 585 HOH   B O   1 
HETATM 6044 O O   . HOH   H 5 .   ? -4.652  48.799  23.444  1.00 30.52 ? 586 HOH   B O   1 
HETATM 6045 O O   . HOH   H 5 .   ? -7.843  40.914  11.322  1.00 23.80 ? 587 HOH   B O   1 
HETATM 6046 O O   . HOH   H 5 .   ? 7.440   3.165   4.815   1.00 20.65 ? 588 HOH   B O   1 
HETATM 6047 O O   . HOH   H 5 .   ? 2.647   39.341  7.806   1.00 21.40 ? 589 HOH   B O   1 
HETATM 6048 O O   . HOH   H 5 .   ? 4.531   16.108  9.999   1.00 27.99 ? 590 HOH   B O   1 
HETATM 6049 O O   . HOH   H 5 .   ? -4.027  4.068   -0.717  1.00 27.50 ? 591 HOH   B O   1 
HETATM 6050 O O   . HOH   H 5 .   ? 0.072   1.237   6.572   1.00 27.69 ? 592 HOH   B O   1 
HETATM 6051 O O   . HOH   H 5 .   ? 3.097   53.093  18.836  1.00 23.90 ? 593 HOH   B O   1 
HETATM 6052 O O   . HOH   H 5 .   ? -15.093 38.827  9.052   1.00 28.98 ? 594 HOH   B O   1 
HETATM 6053 O O   . HOH   H 5 .   ? 2.845   3.060   0.684   1.00 27.68 ? 595 HOH   B O   1 
HETATM 6054 O O   . HOH   H 5 .   ? -10.810 23.542  8.697   1.00 27.99 ? 596 HOH   B O   1 
HETATM 6055 O O   . HOH   H 5 .   ? 3.837   47.072  5.689   1.00 27.18 ? 597 HOH   B O   1 
HETATM 6056 O O   . HOH   H 5 .   ? 12.145  35.177  1.473   1.00 39.37 ? 598 HOH   B O   1 
HETATM 6057 O O   . HOH   H 5 .   ? -9.420  44.506  11.894  1.00 29.16 ? 599 HOH   B O   1 
HETATM 6058 O O   . HOH   H 5 .   ? -13.660 44.804  4.599   1.00 40.18 ? 600 HOH   B O   1 
HETATM 6059 O O   . HOH   H 5 .   ? 11.743  26.616  4.667   1.00 33.45 ? 601 HOH   B O   1 
HETATM 6060 O O   . HOH   H 5 .   ? 9.693   -2.144  9.946   1.00 22.84 ? 602 HOH   B O   1 
HETATM 6061 O O   . HOH   H 5 .   ? -12.438 42.283  13.305  1.00 34.18 ? 603 HOH   B O   1 
HETATM 6062 O O   . HOH   H 5 .   ? -5.173  50.958  17.769  1.00 36.08 ? 604 HOH   B O   1 
HETATM 6063 O O   . HOH   H 5 .   ? -12.958 15.070  -2.801  1.00 37.75 ? 605 HOH   B O   1 
HETATM 6064 O O   . HOH   H 5 .   ? 8.016   37.914  14.443  1.00 34.35 ? 606 HOH   B O   1 
HETATM 6065 O O   . HOH   H 5 .   ? 2.875   33.745  7.710   1.00 20.91 ? 607 HOH   B O   1 
HETATM 6066 O O   . HOH   H 5 .   ? -13.698 25.783  0.373   1.00 35.32 ? 608 HOH   B O   1 
HETATM 6067 O O   . HOH   H 5 .   ? 8.198   9.326   12.244  1.00 31.71 ? 609 HOH   B O   1 
HETATM 6068 O O   . HOH   H 5 .   ? 11.203  38.130  1.766   1.00 31.24 ? 610 HOH   B O   1 
HETATM 6069 O O   . HOH   H 5 .   ? -2.318  24.075  -7.989  1.00 30.71 ? 611 HOH   B O   1 
HETATM 6070 O O   . HOH   H 5 .   ? -24.897 23.204  2.845   1.00 39.55 ? 612 HOH   B O   1 
HETATM 6071 O O   . HOH   H 5 .   ? -11.324 41.483  9.024   1.00 33.51 ? 613 HOH   B O   1 
HETATM 6072 O O   . HOH   H 5 .   ? -14.154 28.023  -0.891  1.00 37.78 ? 614 HOH   B O   1 
HETATM 6073 O O   . HOH   H 5 .   ? 14.494  22.822  5.853   1.00 34.09 ? 615 HOH   B O   1 
HETATM 6074 O O   . HOH   H 5 .   ? 10.712  30.203  -2.575  1.00 32.90 ? 616 HOH   B O   1 
HETATM 6075 O O   . HOH   H 5 .   ? -13.881 28.052  -4.861  1.00 39.87 ? 617 HOH   B O   1 
HETATM 6076 O O   . HOH   H 5 .   ? -3.118  54.348  7.584   1.00 30.91 ? 618 HOH   B O   1 
HETATM 6077 O O   . HOH   H 5 .   ? 4.799   30.644  -11.327 1.00 28.76 ? 619 HOH   B O   1 
HETATM 6078 O O   . HOH   H 5 .   ? 3.845   38.408  -1.179  1.00 31.04 ? 620 HOH   B O   1 
HETATM 6079 O O   . HOH   H 5 .   ? 10.827  -6.010  15.107  1.00 35.18 ? 621 HOH   B O   1 
HETATM 6080 O O   . HOH   H 5 .   ? 11.048  28.727  5.387   1.00 33.50 ? 622 HOH   B O   1 
HETATM 6081 O O   . HOH   H 5 .   ? 4.372   4.893   -1.601  1.00 31.75 ? 623 HOH   B O   1 
HETATM 6082 O O   . HOH   H 5 .   ? -15.293 10.401  4.919   1.00 38.97 ? 624 HOH   B O   1 
HETATM 6083 O O   . HOH   H 5 .   ? -2.112  25.106  25.498  1.00 38.41 ? 625 HOH   B O   1 
HETATM 6084 O O   . HOH   H 5 .   ? -6.868  10.953  23.215  1.00 40.11 ? 626 HOH   B O   1 
HETATM 6085 O O   . HOH   H 5 .   ? 2.069   36.886  -0.379  1.00 32.02 ? 627 HOH   B O   1 
HETATM 6086 O O   . HOH   H 5 .   ? 3.053   31.168  8.268   1.00 27.76 ? 628 HOH   B O   1 
HETATM 6087 O O   . HOH   H 5 .   ? 8.222   37.859  -1.932  1.00 38.25 ? 629 HOH   B O   1 
HETATM 6088 O O   . HOH   H 5 .   ? 19.029  8.588   1.129   1.00 37.62 ? 630 HOH   B O   1 
HETATM 6089 O O   . HOH   H 5 .   ? -5.301  37.463  -6.112  1.00 30.47 ? 631 HOH   B O   1 
HETATM 6090 O O   . HOH   H 5 .   ? -0.914  23.342  -5.449  1.00 28.86 ? 632 HOH   B O   1 
HETATM 6091 O O   . HOH   H 5 .   ? -8.938  44.390  7.603   1.00 33.92 ? 633 HOH   B O   1 
HETATM 6092 O O   . HOH   H 5 .   ? -4.655  26.951  26.220  1.00 43.24 ? 634 HOH   B O   1 
HETATM 6093 O O   . HOH   H 5 .   ? -10.490 41.557  11.576  1.00 31.98 ? 635 HOH   B O   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   . ASN A 2   ? 0.8475 0.8196 0.7942 0.1593  0.1686  -0.0237 3   ASN A N   
2    C CA  . ASN A 2   ? 0.7339 0.7171 0.6931 0.1479  0.1695  -0.0147 3   ASN A CA  
3    C C   . ASN A 2   ? 0.7417 0.7313 0.6898 0.1451  0.1781  -0.0089 3   ASN A C   
4    O O   . ASN A 2   ? 0.7518 0.7317 0.6750 0.1520  0.1814  -0.0125 3   ASN A O   
5    C CB  . ASN A 2   ? 0.7421 0.7102 0.6915 0.1384  0.1540  -0.0158 3   ASN A CB  
6    C CG  . ASN A 2   ? 0.7114 0.6909 0.6892 0.1289  0.1466  -0.0111 3   ASN A CG  
7    O OD1 . ASN A 2   ? 0.7637 0.7634 0.7668 0.1267  0.1539  -0.0050 3   ASN A OD1 
8    N ND2 . ASN A 2   ? 0.6102 0.5766 0.5841 0.1235  0.1318  -0.0139 3   ASN A ND2 
9    N N   . THR A 3   ? 0.7061 0.7112 0.6727 0.1351  0.1805  0.0002  4   THR A N   
10   C CA  . THR A 3   ? 0.7174 0.7292 0.6769 0.1318  0.1881  0.0070  4   THR A CA  
11   C C   . THR A 3   ? 0.6832 0.6766 0.6081 0.1318  0.1850  0.0050  4   THR A C   
12   O O   . THR A 3   ? 0.6605 0.6393 0.5731 0.1305  0.1764  0.0006  4   THR A O   
13   C CB  . THR A 3   ? 0.6917 0.7216 0.6792 0.1206  0.1887  0.0165  4   THR A CB  
14   O OG1 . THR A 3   ? 0.6260 0.6500 0.6105 0.1129  0.1808  0.0181  4   THR A OG1 
15   C CG2 . THR A 3   ? 0.6840 0.7295 0.7058 0.1199  0.1878  0.0169  4   THR A CG2 
16   N N   . PRO A 4   ? 0.6864 0.6795 0.5947 0.1334  0.1913  0.0081  5   PRO A N   
17   C CA  . PRO A 4   ? 0.6702 0.6459 0.5455 0.1331  0.1868  0.0061  5   PRO A CA  
18   C C   . PRO A 4   ? 0.6121 0.5853 0.4890 0.1225  0.1794  0.0094  5   PRO A C   
19   O O   . PRO A 4   ? 0.5891 0.5442 0.4418 0.1219  0.1704  0.0040  5   PRO A O   
20   C CB  . PRO A 4   ? 0.6964 0.6788 0.5640 0.1344  0.1958  0.0121  5   PRO A CB  
21   C CG  . PRO A 4   ? 0.7627 0.7580 0.6468 0.1410  0.2048  0.0123  5   PRO A CG  
22   C CD  . PRO A 4   ? 0.7304 0.7372 0.6470 0.1369  0.2022  0.0126  5   PRO A CD  
23   N N   . LYS A 5   ? 0.5995 0.5904 0.5052 0.1133  0.1809  0.0177  6   LYS A N   
24   C CA  . LYS A 5   ? 0.5681 0.5586 0.4782 0.1029  0.1727  0.0209  6   LYS A CA  
25   C C   . LYS A 5   ? 0.5517 0.5340 0.4678 0.0987  0.1572  0.0146  6   LYS A C   
26   O O   . LYS A 5   ? 0.5047 0.4754 0.4083 0.0918  0.1444  0.0123  6   LYS A O   
27   C CB  . LYS A 5   ? 0.5157 0.5267 0.4570 0.0943  0.1757  0.0305  6   LYS A CB  
28   C CG  . LYS A 5   ? 0.5233 0.5361 0.4724 0.0830  0.1657  0.0339  6   LYS A CG  
29   C CD  . LYS A 5   ? 0.5264 0.5283 0.4492 0.0792  0.1619  0.0351  6   LYS A CD  
30   C CE  . LYS A 5   ? 0.4937 0.5028 0.4161 0.0788  0.1707  0.0424  6   LYS A CE  
31   N NZ  . LYS A 5   ? 0.4989 0.5000 0.4017 0.0733  0.1653  0.0447  6   LYS A NZ  
32   N N   . ASP A 6   ? 0.5337 0.5220 0.4691 0.1030  0.1583  0.0120  7   ASP A N   
33   C CA  . ASP A 6   ? 0.5468 0.5255 0.4853 0.1007  0.1445  0.0061  7   ASP A CA  
34   C C   . ASP A 6   ? 0.5380 0.4932 0.4454 0.1026  0.1352  -0.0014 7   ASP A C   
35   O O   . ASP A 6   ? 0.5095 0.4552 0.4133 0.0949  0.1216  -0.0031 7   ASP A O   
36   C CB  . ASP A 6   ? 0.6113 0.5961 0.5680 0.1087  0.1486  0.0030  7   ASP A CB  
37   C CG  . ASP A 6   ? 0.6454 0.6513 0.6372 0.1047  0.1515  0.0090  7   ASP A CG  
38   O OD1 . ASP A 6   ? 0.5683 0.5771 0.5722 0.0956  0.1410  0.0114  7   ASP A OD1 
39   O OD2 . ASP A 6   ? 0.6596 0.6794 0.6673 0.1112  0.1640  0.0111  7   ASP A OD2 
40   N N   . GLN A 7   ? 0.5251 0.4709 0.4104 0.1132  0.1424  -0.0061 8   GLN A N   
41   C CA  . GLN A 7   ? 0.5589 0.4811 0.4149 0.1164  0.1328  -0.0145 8   GLN A CA  
42   C C   . GLN A 7   ? 0.5032 0.4174 0.3409 0.1087  0.1258  -0.0130 8   GLN A C   
43   O O   . GLN A 7   ? 0.5138 0.4116 0.3385 0.1045  0.1120  -0.0179 8   GLN A O   
44   C CB  . GLN A 7   ? 0.6317 0.5466 0.4685 0.1316  0.1424  -0.0206 8   GLN A CB  
45   C CG  . GLN A 7   ? 0.6829 0.6094 0.5400 0.1399  0.1514  -0.0213 8   GLN A CG  
46   C CD  . GLN A 7   ? 0.7935 0.7122 0.6312 0.1560  0.1599  -0.0284 8   GLN A CD  
47   O OE1 . GLN A 7   ? 0.7738 0.6990 0.6024 0.1597  0.1693  -0.0254 8   GLN A OE1 
48   N NE2 . GLN A 7   ? 0.8523 0.7582 0.6868 0.1625  0.1527  -0.0370 8   GLN A NE2 
49   N N   . GLU A 8   ? 0.4842 0.4094 0.3213 0.1067  0.1348  -0.0060 9   GLU A N   
50   C CA  . GLU A 8   ? 0.5305 0.4489 0.3511 0.0996  0.1280  -0.0043 9   GLU A CA  
51   C C   . GLU A 8   ? 0.4998 0.4199 0.3350 0.0863  0.1142  -0.0023 9   GLU A C   
52   O O   . GLU A 8   ? 0.5082 0.4145 0.3289 0.0815  0.1017  -0.0061 9   GLU A O   
53   C CB  . GLU A 8   ? 0.5526 0.4837 0.3733 0.0994  0.1404  0.0041  9   GLU A CB  
54   C CG  . GLU A 8   ? 0.5625 0.4880 0.3692 0.0913  0.1323  0.0063  9   GLU A CG  
55   C CD  . GLU A 8   ? 0.5650 0.5057 0.3809 0.0871  0.1416  0.0165  9   GLU A CD  
56   O OE1 . GLU A 8   ? 0.5874 0.5443 0.4240 0.0891  0.1539  0.0227  9   GLU A OE1 
57   O OE2 . GLU A 8   ? 0.5454 0.4813 0.3484 0.0818  0.1359  0.0184  9   GLU A OE2 
58   N N   . ILE A 9   ? 0.4833 0.4208 0.3478 0.0807  0.1162  0.0038  10  ILE A N   
59   C CA  . ILE A 9   ? 0.4502 0.3916 0.3290 0.0691  0.1043  0.0063  10  ILE A CA  
60   C C   . ILE A 9   ? 0.4442 0.3719 0.3200 0.0680  0.0922  0.0002  10  ILE A C   
61   O O   . ILE A 9   ? 0.4250 0.3469 0.2979 0.0597  0.0803  0.0000  10  ILE A O   
62   C CB  . ILE A 9   ? 0.4170 0.3795 0.3271 0.0654  0.1091  0.0133  10  ILE A CB  
63   C CG1 . ILE A 9   ? 0.4832 0.4579 0.3969 0.0648  0.1196  0.0202  10  ILE A CG1 
64   C CG2 . ILE A 9   ? 0.4312 0.3979 0.3557 0.0554  0.0968  0.0152  10  ILE A CG2 
65   C CD1 . ILE A 9   ? 0.4694 0.4642 0.4149 0.0616  0.1240  0.0267  10  ILE A CD1 
66   N N   . LYS A 10  ? 0.4486 0.3713 0.3257 0.0764  0.0951  -0.0045 11  LYS A N   
67   C CA  . LYS A 10  ? 0.4697 0.3769 0.3422 0.0760  0.0836  -0.0103 11  LYS A CA  
68   C C   . LYS A 10  ? 0.4636 0.3507 0.3096 0.0749  0.0744  -0.0158 11  LYS A C   
69   O O   . LYS A 10  ? 0.4723 0.3501 0.3176 0.0676  0.0618  -0.0169 11  LYS A O   
70   C CB  . LYS A 10  ? 0.5142 0.4177 0.3897 0.0869  0.0887  -0.0152 11  LYS A CB  
71   C CG  . LYS A 10  ? 0.6186 0.4992 0.4775 0.0903  0.0784  -0.0233 11  LYS A CG  
72   C CD  . LYS A 10  ? 0.6421 0.5200 0.5095 0.0990  0.0803  -0.0274 11  LYS A CD  
73   C CE  . LYS A 10  ? 0.6888 0.5426 0.5417 0.1006  0.0679  -0.0347 11  LYS A CE  
74   N NZ  . LYS A 10  ? 0.6708 0.5197 0.5291 0.0879  0.0546  -0.0312 11  LYS A NZ  
75   N N   . LYS A 11  ? 0.4898 0.3701 0.3140 0.0822  0.0804  -0.0190 12  LYS A N   
76   C CA  . LYS A 11  ? 0.5026 0.3632 0.3011 0.0819  0.0706  -0.0251 12  LYS A CA  
77   C C   . LYS A 11  ? 0.5114 0.3748 0.3112 0.0697  0.0619  -0.0209 12  LYS A C   
78   O O   . LYS A 11  ? 0.5117 0.3619 0.3045 0.0641  0.0486  -0.0245 12  LYS A O   
79   C CB  . LYS A 11  ? 0.5255 0.3789 0.2987 0.0934  0.0791  -0.0293 12  LYS A CB  
80   C CG  . LYS A 11  ? 0.6102 0.4429 0.3563 0.0933  0.0675  -0.0361 12  LYS A CG  
81   C CD  . LYS A 11  ? 0.7429 0.5692 0.4615 0.1045  0.0754  -0.0394 12  LYS A CD  
82   C CE  . LYS A 11  ? 0.7644 0.5876 0.4688 0.0984  0.0695  -0.0378 12  LYS A CE  
83   N NZ  . LYS A 11  ? 0.7444 0.5886 0.4671 0.0897  0.0762  -0.0270 12  LYS A NZ  
84   N N   . LEU A 12  ? 0.4567 0.3374 0.2667 0.0653  0.0688  -0.0134 13  LEU A N   
85   C CA  . LEU A 12  ? 0.4650 0.3494 0.2762 0.0546  0.0607  -0.0097 13  LEU A CA  
86   C C   . LEU A 12  ? 0.4301 0.3178 0.2598 0.0447  0.0501  -0.0076 13  LEU A C   
87   O O   . LEU A 12  ? 0.4278 0.3099 0.2532 0.0370  0.0391  -0.0082 13  LEU A O   
88   C CB  . LEU A 12  ? 0.4574 0.3593 0.2770 0.0528  0.0704  -0.0019 13  LEU A CB  
89   C CG  . LEU A 12  ? 0.5351 0.4323 0.3323 0.0607  0.0793  -0.0027 13  LEU A CG  
90   C CD1 . LEU A 12  ? 0.4873 0.4021 0.2962 0.0583  0.0892  0.0062  13  LEU A CD1 
91   C CD2 . LEU A 12  ? 0.5575 0.4379 0.3287 0.0598  0.0690  -0.0080 13  LEU A CD2 
92   N N   . VAL A 13  ? 0.4209 0.3180 0.2712 0.0451  0.0533  -0.0049 14  VAL A N   
93   C CA  . VAL A 13  ? 0.4236 0.3241 0.2902 0.0368  0.0440  -0.0023 14  VAL A CA  
94   C C   . VAL A 13  ? 0.4427 0.3237 0.2999 0.0365  0.0337  -0.0079 14  VAL A C   
95   O O   . VAL A 13  ? 0.4072 0.2852 0.2679 0.0278  0.0232  -0.0065 14  VAL A O   
96   C CB  . VAL A 13  ? 0.4203 0.3366 0.3110 0.0381  0.0500  0.0022  14  VAL A CB  
97   C CG1 . VAL A 13  ? 0.3866 0.3046 0.2913 0.0312  0.0406  0.0048  14  VAL A CG1 
98   C CG2 . VAL A 13  ? 0.4144 0.3496 0.3167 0.0366  0.0580  0.0082  14  VAL A CG2 
99   N N   . ASP A 14  ? 0.4260 0.2937 0.2719 0.0460  0.0363  -0.0143 15  ASP A N   
100  C CA  . ASP A 14  ? 0.4751 0.3214 0.3097 0.0464  0.0256  -0.0206 15  ASP A CA  
101  C C   . ASP A 14  ? 0.4641 0.2989 0.2827 0.0410  0.0158  -0.0235 15  ASP A C   
102  O O   . ASP A 14  ? 0.5275 0.3506 0.3460 0.0347  0.0038  -0.0250 15  ASP A O   
103  C CB  . ASP A 14  ? 0.4973 0.3308 0.3189 0.0593  0.0304  -0.0281 15  ASP A CB  
104  C CG  . ASP A 14  ? 0.5624 0.4023 0.4005 0.0645  0.0360  -0.0269 15  ASP A CG  
105  O OD1 . ASP A 14  ? 0.5529 0.4042 0.4113 0.0581  0.0344  -0.0208 15  ASP A OD1 
106  O OD2 . ASP A 14  ? 0.5949 0.4282 0.4248 0.0760  0.0419  -0.0325 15  ASP A OD2 
107  N N   . GLN A 15  ? 0.4928 0.3305 0.2980 0.0435  0.0205  -0.0241 16  GLN A N   
108  C CA  . GLN A 15  ? 0.4657 0.2916 0.2536 0.0400  0.0111  -0.0280 16  GLN A CA  
109  C C   . GLN A 15  ? 0.4780 0.3141 0.2790 0.0270  0.0035  -0.0221 16  GLN A C   
110  O O   . GLN A 15  ? 0.4671 0.2925 0.2627 0.0211  -0.0086 -0.0248 16  GLN A O   
111  C CB  . GLN A 15  ? 0.5113 0.3367 0.2792 0.0480  0.0191  -0.0302 16  GLN A CB  
112  C CG  . GLN A 15  ? 0.5881 0.4050 0.3391 0.0446  0.0102  -0.0331 16  GLN A CG  
113  C CD  . GLN A 15  ? 0.7069 0.5189 0.4334 0.0551  0.0179  -0.0364 16  GLN A CD  
114  O OE1 . GLN A 15  ? 0.7520 0.5646 0.4726 0.0656  0.0294  -0.0375 16  GLN A OE1 
115  N NE2 . GLN A 15  ? 0.7211 0.5284 0.4329 0.0527  0.0117  -0.0379 16  GLN A NE2 
116  N N   . ASN A 16  ? 0.4524 0.3093 0.2711 0.0228  0.0101  -0.0142 17  ASN A N   
117  C CA  . ASN A 16  ? 0.4046 0.2729 0.2332 0.0123  0.0043  -0.0089 17  ASN A CA  
118  C C   . ASN A 16  ? 0.3981 0.2765 0.2491 0.0046  0.0004  -0.0032 17  ASN A C   
119  O O   . ASN A 16  ? 0.4110 0.2928 0.2677 -0.0043 -0.0079 -0.0006 17  ASN A O   
120  C CB  . ASN A 16  ? 0.3772 0.2611 0.2068 0.0131  0.0131  -0.0044 17  ASN A CB  
121  C CG  . ASN A 16  ? 0.4318 0.3057 0.2371 0.0191  0.0151  -0.0089 17  ASN A CG  
122  O OD1 . ASN A 16  ? 0.4227 0.2887 0.2162 0.0154  0.0060  -0.0118 17  ASN A OD1 
123  N ND2 . ASN A 16  ? 0.4431 0.3174 0.2407 0.0286  0.0269  -0.0095 17  ASN A ND2 
124  N N   . PHE A 17  ? 0.3659 0.2492 0.2293 0.0082  0.0061  -0.0011 18  PHE A N   
125  C CA  . PHE A 17  ? 0.3381 0.2307 0.2210 0.0022  0.0027  0.0046  18  PHE A CA  
126  C C   . PHE A 17  ? 0.3929 0.2705 0.2765 0.0021  -0.0036 0.0025  18  PHE A C   
127  O O   . PHE A 17  ? 0.3976 0.2758 0.2901 -0.0057 -0.0111 0.0065  18  PHE A O   
128  C CB  . PHE A 17  ? 0.3321 0.2425 0.2312 0.0056  0.0120  0.0093  18  PHE A CB  
129  C CG  . PHE A 17  ? 0.2955 0.2236 0.2017 0.0019  0.0148  0.0139  18  PHE A CG  
130  C CD1 . PHE A 17  ? 0.2927 0.2337 0.2125 -0.0054 0.0099  0.0194  18  PHE A CD1 
131  C CD2 . PHE A 17  ? 0.3310 0.2626 0.2297 0.0061  0.0223  0.0131  18  PHE A CD2 
132  C CE1 . PHE A 17  ? 0.3070 0.2634 0.2329 -0.0081 0.0115  0.0230  18  PHE A CE1 
133  C CE2 . PHE A 17  ? 0.3063 0.2528 0.2116 0.0027  0.0242  0.0174  18  PHE A CE2 
134  C CZ  . PHE A 17  ? 0.2859 0.2446 0.2050 -0.0043 0.0183  0.0220  18  PHE A CZ  
135  N N   . LYS A 18  ? 0.3977 0.2616 0.2717 0.0108  -0.0008 -0.0033 19  LYS A N   
136  C CA  . LYS A 18  ? 0.4230 0.2716 0.2981 0.0116  -0.0069 -0.0053 19  LYS A CA  
137  C C   . LYS A 18  ? 0.4066 0.2410 0.2771 0.0034  -0.0197 -0.0063 19  LYS A C   
138  O O   . LYS A 18  ? 0.4475 0.2777 0.3281 -0.0013 -0.0255 -0.0027 19  LYS A O   
139  C CB  . LYS A 18  ? 0.4401 0.2753 0.3028 0.0235  -0.0023 -0.0129 19  LYS A CB  
140  C CG  . LYS A 18  ? 0.5005 0.3176 0.3624 0.0259  -0.0088 -0.0161 19  LYS A CG  
141  C CD  . LYS A 18  ? 0.5405 0.3454 0.3882 0.0388  -0.0040 -0.0246 19  LYS A CD  
142  C CE  . LYS A 18  ? 0.6226 0.4077 0.4683 0.0424  -0.0112 -0.0288 19  LYS A CE  
143  N NZ  . LYS A 18  ? 0.6894 0.4625 0.5193 0.0560  -0.0068 -0.0381 19  LYS A NZ  
144  N N   . PRO A 19  ? 0.4394 0.2657 0.2960 0.0015  -0.0250 -0.0109 20  PRO A N   
145  C CA  . PRO A 19  ? 0.4620 0.2752 0.3176 -0.0069 -0.0381 -0.0118 20  PRO A CA  
146  C C   . PRO A 19  ? 0.4529 0.2801 0.3271 -0.0185 -0.0419 -0.0026 20  PRO A C   
147  O O   . PRO A 19  ? 0.5010 0.3187 0.3802 -0.0258 -0.0516 -0.0011 20  PRO A O   
148  C CB  . PRO A 19  ? 0.5096 0.3161 0.3477 -0.0060 -0.0418 -0.0181 20  PRO A CB  
149  C CG  . PRO A 19  ? 0.5041 0.3110 0.3285 0.0060  -0.0311 -0.0226 20  PRO A CG  
150  C CD  . PRO A 19  ? 0.4557 0.2821 0.2959 0.0075  -0.0199 -0.0157 20  PRO A CD  
151  N N   . LEU A 20  ? 0.4148 0.2643 0.2997 -0.0200 -0.0346 0.0037  21  LEU A N   
152  C CA  . LEU A 20  ? 0.4307 0.2951 0.3319 -0.0296 -0.0375 0.0122  21  LEU A CA  
153  C C   . LEU A 20  ? 0.4170 0.2793 0.3306 -0.0318 -0.0392 0.0177  21  LEU A C   
154  O O   . LEU A 20  ? 0.4061 0.2744 0.3308 -0.0405 -0.0441 0.0244  21  LEU A O   
155  C CB  . LEU A 20  ? 0.3765 0.2641 0.2853 -0.0289 -0.0296 0.0166  21  LEU A CB  
156  C CG  . LEU A 20  ? 0.3579 0.2498 0.2562 -0.0280 -0.0281 0.0131  21  LEU A CG  
157  C CD1 . LEU A 20  ? 0.3281 0.2413 0.2349 -0.0263 -0.0200 0.0175  21  LEU A CD1 
158  C CD2 . LEU A 20  ? 0.4125 0.3021 0.3092 -0.0367 -0.0380 0.0129  21  LEU A CD2 
159  N N   . LEU A 21  ? 0.4198 0.2739 0.3316 -0.0238 -0.0351 0.0155  22  LEU A N   
160  C CA  . LEU A 21  ? 0.4150 0.2656 0.3371 -0.0250 -0.0370 0.0208  22  LEU A CA  
161  C C   . LEU A 21  ? 0.4471 0.2797 0.3686 -0.0322 -0.0478 0.0213  22  LEU A C   
162  O O   . LEU A 21  ? 0.4466 0.2834 0.3799 -0.0400 -0.0514 0.0295  22  LEU A O   
163  C CB  . LEU A 21  ? 0.4495 0.2936 0.3690 -0.0142 -0.0312 0.0171  22  LEU A CB  
164  C CG  . LEU A 21  ? 0.4682 0.3305 0.3946 -0.0072 -0.0207 0.0185  22  LEU A CG  
165  C CD1 . LEU A 21  ? 0.4763 0.3598 0.4169 -0.0127 -0.0194 0.0271  22  LEU A CD1 
166  C CD2 . LEU A 21  ? 0.4754 0.3418 0.3925 -0.0014 -0.0140 0.0126  22  LEU A CD2 
167  N N   . GLU A 22  ? 0.4619 0.2741 0.3697 -0.0295 -0.0533 0.0126  23  GLU A N   
168  C CA  . GLU A 22  ? 0.4920 0.2858 0.4002 -0.0367 -0.0650 0.0122  23  GLU A CA  
169  C C   . GLU A 22  ? 0.4855 0.2883 0.4006 -0.0481 -0.0708 0.0163  23  GLU A C   
170  O O   . GLU A 22  ? 0.4613 0.2612 0.3877 -0.0574 -0.0776 0.0227  23  GLU A O   
171  C CB  . GLU A 22  ? 0.5745 0.3438 0.4653 -0.0297 -0.0704 0.0006  23  GLU A CB  
172  C CG  . GLU A 22  ? 0.6442 0.3905 0.5362 -0.0353 -0.0833 -0.0006 23  GLU A CG  
173  C CD  . GLU A 22  ? 0.7178 0.4532 0.6016 -0.0395 -0.0935 -0.0073 23  GLU A CD  
174  O OE1 . GLU A 22  ? 0.8012 0.5123 0.6781 -0.0385 -0.1040 -0.0139 23  GLU A OE1 
175  O OE2 . GLU A 22  ? 0.7166 0.4671 0.6006 -0.0433 -0.0918 -0.0063 23  GLU A OE2 
176  N N   . LYS A 23  ? 0.4791 0.2935 0.3883 -0.0474 -0.0680 0.0133  24  LYS A N   
177  C CA  . LYS A 23  ? 0.4423 0.2647 0.3572 -0.0573 -0.0742 0.0158  24  LYS A CA  
178  C C   . LYS A 23  ? 0.4489 0.2899 0.3831 -0.0660 -0.0728 0.0277  24  LYS A C   
179  O O   . LYS A 23  ? 0.4744 0.3153 0.4183 -0.0759 -0.0803 0.0319  24  LYS A O   
180  C CB  . LYS A 23  ? 0.4708 0.3038 0.3758 -0.0540 -0.0704 0.0112  24  LYS A CB  
181  C CG  . LYS A 23  ? 0.4519 0.2942 0.3629 -0.0634 -0.0769 0.0133  24  LYS A CG  
182  C CD  . LYS A 23  ? 0.4266 0.2732 0.3239 -0.0593 -0.0753 0.0072  24  LYS A CD  
183  C CE  . LYS A 23  ? 0.4767 0.3287 0.3786 -0.0680 -0.0841 0.0074  24  LYS A CE  
184  N NZ  . LYS A 23  ? 0.5005 0.3570 0.3887 -0.0636 -0.0825 0.0022  24  LYS A NZ  
185  N N   . TYR A 24  ? 0.4341 0.2913 0.3746 -0.0620 -0.0634 0.0333  25  TYR A N   
186  C CA  . TYR A 24  ? 0.4000 0.2766 0.3565 -0.0683 -0.0613 0.0442  25  TYR A CA  
187  C C   . TYR A 24  ? 0.4500 0.3237 0.4141 -0.0669 -0.0589 0.0511  25  TYR A C   
188  O O   . TYR A 24  ? 0.4367 0.3274 0.4120 -0.0693 -0.0554 0.0601  25  TYR A O   
189  C CB  . TYR A 24  ? 0.3670 0.2670 0.3254 -0.0652 -0.0537 0.0456  25  TYR A CB  
190  C CG  . TYR A 24  ? 0.3844 0.2893 0.3377 -0.0684 -0.0569 0.0412  25  TYR A CG  
191  C CD1 . TYR A 24  ? 0.3791 0.2920 0.3414 -0.0780 -0.0630 0.0453  25  TYR A CD1 
192  C CD2 . TYR A 24  ? 0.4109 0.3122 0.3503 -0.0616 -0.0540 0.0330  25  TYR A CD2 
193  C CE1 . TYR A 24  ? 0.3990 0.3157 0.3566 -0.0805 -0.0669 0.0408  25  TYR A CE1 
194  C CE2 . TYR A 24  ? 0.4180 0.3225 0.3513 -0.0640 -0.0575 0.0291  25  TYR A CE2 
195  C CZ  . TYR A 24  ? 0.3897 0.3016 0.3321 -0.0734 -0.0644 0.0327  25  TYR A CZ  
196  O OH  . TYR A 24  ? 0.4212 0.3361 0.3578 -0.0754 -0.0687 0.0285  25  TYR A OH  
197  N N   . ASP A 25  ? 0.4140 0.2665 0.3715 -0.0624 -0.0612 0.0469  26  ASP A N   
198  C CA  . ASP A 25  ? 0.4356 0.2822 0.3984 -0.0599 -0.0597 0.0525  26  ASP A CA  
199  C C   . ASP A 25  ? 0.4483 0.3138 0.4157 -0.0532 -0.0503 0.0566  26  ASP A C   
200  O O   . ASP A 25  ? 0.4387 0.3119 0.4151 -0.0546 -0.0487 0.0657  26  ASP A O   
201  C CB  . ASP A 25  ? 0.4753 0.3186 0.4497 -0.0703 -0.0657 0.0624  26  ASP A CB  
202  C CG  . ASP A 25  ? 0.6128 0.4422 0.5893 -0.0677 -0.0664 0.0669  26  ASP A CG  
203  O OD1 . ASP A 25  ? 0.6112 0.4320 0.5796 -0.0576 -0.0633 0.0610  26  ASP A OD1 
204  O OD2 . ASP A 25  ? 0.6380 0.4648 0.6244 -0.0757 -0.0701 0.0766  26  ASP A OD2 
205  N N   . VAL A 26  ? 0.4261 0.2982 0.3869 -0.0453 -0.0443 0.0498  27  VAL A N   
206  C CA  . VAL A 26  ? 0.3458 0.2354 0.3118 -0.0385 -0.0363 0.0522  27  VAL A CA  
207  C C   . VAL A 26  ? 0.3770 0.2549 0.3409 -0.0296 -0.0340 0.0497  27  VAL A C   
208  O O   . VAL A 26  ? 0.3823 0.2457 0.3366 -0.0240 -0.0339 0.0414  27  VAL A O   
209  C CB  . VAL A 26  ? 0.3356 0.2378 0.2977 -0.0348 -0.0310 0.0468  27  VAL A CB  
210  C CG1 . VAL A 26  ? 0.3209 0.2403 0.2907 -0.0280 -0.0239 0.0491  27  VAL A CG1 
211  C CG2 . VAL A 26  ? 0.3660 0.2780 0.3291 -0.0430 -0.0342 0.0483  27  VAL A CG2 
212  N N   . PRO A 27  ? 0.3516 0.2358 0.3236 -0.0271 -0.0322 0.0564  28  PRO A N   
213  C CA  . PRO A 27  ? 0.3373 0.2097 0.3075 -0.0182 -0.0309 0.0537  28  PRO A CA  
214  C C   . PRO A 27  ? 0.3437 0.2212 0.3115 -0.0082 -0.0241 0.0458  28  PRO A C   
215  O O   . PRO A 27  ? 0.3563 0.2190 0.3177 -0.0016 -0.0238 0.0391  28  PRO A O   
216  C CB  . PRO A 27  ? 0.3763 0.2575 0.3556 -0.0179 -0.0304 0.0633  28  PRO A CB  
217  C CG  . PRO A 27  ? 0.3846 0.2734 0.3685 -0.0288 -0.0337 0.0717  28  PRO A CG  
218  C CD  . PRO A 27  ? 0.3575 0.2568 0.3393 -0.0321 -0.0324 0.0668  28  PRO A CD  
219  N N   . GLY A 28  ? 0.3556 0.2537 0.3291 -0.0068 -0.0189 0.0463  29  GLY A N   
220  C CA  . GLY A 28  ? 0.3309 0.2357 0.3055 0.0022  -0.0120 0.0404  29  GLY A CA  
221  C C   . GLY A 28  ? 0.3206 0.2421 0.2969 0.0006  -0.0077 0.0392  29  GLY A C   
222  O O   . GLY A 28  ? 0.2959 0.2296 0.2761 -0.0058 -0.0096 0.0441  29  GLY A O   
223  N N   . MET A 29  ? 0.2630 0.1855 0.2369 0.0071  -0.0017 0.0330  30  MET A N   
224  C CA  . MET A 29  ? 0.2927 0.2289 0.2673 0.0062  0.0029  0.0319  30  MET A CA  
225  C C   . MET A 29  ? 0.2784 0.2213 0.2587 0.0151  0.0109  0.0282  30  MET A C   
226  O O   . MET A 29  ? 0.2812 0.2138 0.2584 0.0219  0.0135  0.0238  30  MET A O   
227  C CB  . MET A 29  ? 0.2813 0.2075 0.2416 0.0019  0.0011  0.0281  30  MET A CB  
228  C CG  . MET A 29  ? 0.2847 0.2233 0.2439 0.0011  0.0056  0.0272  30  MET A CG  
229  S SD  . MET A 29  ? 0.3407 0.2650 0.2803 -0.0013 0.0036  0.0216  30  MET A SD  
230  C CE  . MET A 29  ? 0.3658 0.2882 0.3053 -0.0127 -0.0069 0.0256  30  MET A CE  
231  N N   . ALA A 30  ? 0.2545 0.2150 0.2439 0.0150  0.0147  0.0300  31  ALA A N   
232  C CA  . ALA A 30  ? 0.2432 0.2119 0.2396 0.0219  0.0229  0.0273  31  ALA A CA  
233  C C   . ALA A 30  ? 0.2691 0.2454 0.2618 0.0185  0.0263  0.0273  31  ALA A C   
234  O O   . ALA A 30  ? 0.2505 0.2358 0.2456 0.0125  0.0226  0.0309  31  ALA A O   
235  C CB  . ALA A 30  ? 0.2422 0.2256 0.2573 0.0259  0.0235  0.0298  31  ALA A CB  
236  N N   . VAL A 31  ? 0.2497 0.2220 0.2356 0.0229  0.0335  0.0236  32  VAL A N   
237  C CA  . VAL A 31  ? 0.2277 0.2057 0.2085 0.0206  0.0376  0.0241  32  VAL A CA  
238  C C   . VAL A 31  ? 0.2380 0.2257 0.2291 0.0270  0.0476  0.0238  32  VAL A C   
239  O O   . VAL A 31  ? 0.2634 0.2452 0.2531 0.0342  0.0532  0.0204  32  VAL A O   
240  C CB  . VAL A 31  ? 0.2747 0.2370 0.2334 0.0193  0.0366  0.0203  32  VAL A CB  
241  C CG1 . VAL A 31  ? 0.2754 0.2437 0.2280 0.0179  0.0412  0.0213  32  VAL A CG1 
242  C CG2 . VAL A 31  ? 0.2823 0.2358 0.2339 0.0122  0.0262  0.0208  32  VAL A CG2 
243  N N   . GLY A 32  ? 0.2428 0.2450 0.2446 0.0247  0.0498  0.0275  33  GLY A N   
244  C CA  . GLY A 32  ? 0.2330 0.2457 0.2475 0.0294  0.0592  0.0285  33  GLY A CA  
245  C C   . GLY A 32  ? 0.2517 0.2677 0.2595 0.0268  0.0641  0.0307  33  GLY A C   
246  O O   . GLY A 32  ? 0.2426 0.2600 0.2451 0.0205  0.0584  0.0327  33  GLY A O   
247  N N   . VAL A 33  ? 0.2537 0.2709 0.2616 0.0321  0.0748  0.0307  34  VAL A N   
248  C CA  . VAL A 33  ? 0.2410 0.2627 0.2450 0.0306  0.0811  0.0341  34  VAL A CA  
249  C C   . VAL A 33  ? 0.2662 0.3029 0.2938 0.0337  0.0897  0.0378  34  VAL A C   
250  O O   . VAL A 33  ? 0.2486 0.2874 0.2861 0.0399  0.0952  0.0360  34  VAL A O   
251  C CB  . VAL A 33  ? 0.2769 0.2848 0.2554 0.0344  0.0870  0.0314  34  VAL A CB  
252  C CG1 . VAL A 33  ? 0.3132 0.3263 0.2884 0.0344  0.0957  0.0360  34  VAL A CG1 
253  C CG2 . VAL A 33  ? 0.2821 0.2757 0.2395 0.0304  0.0770  0.0279  34  VAL A CG2 
254  N N   . ILE A 34  ? 0.2378 0.2848 0.2758 0.0294  0.0902  0.0428  35  ILE A N   
255  C CA  . ILE A 34  ? 0.2694 0.3295 0.3289 0.0316  0.0993  0.0471  35  ILE A CA  
256  C C   . ILE A 34  ? 0.2651 0.3238 0.3130 0.0303  0.1072  0.0516  35  ILE A C   
257  O O   . ILE A 34  ? 0.2414 0.2968 0.2778 0.0250  0.1016  0.0531  35  ILE A O   
258  C CB  . ILE A 34  ? 0.2617 0.3359 0.3484 0.0282  0.0925  0.0494  35  ILE A CB  
259  C CG1 . ILE A 34  ? 0.3041 0.3912 0.4140 0.0295  0.1017  0.0545  35  ILE A CG1 
260  C CG2 . ILE A 34  ? 0.2305 0.3046 0.3112 0.0213  0.0818  0.0506  35  ILE A CG2 
261  C CD1 . ILE A 34  ? 0.2446 0.3442 0.3831 0.0280  0.0943  0.0549  35  ILE A CD1 
262  N N   . GLN A 35  ? 0.2687 0.3302 0.3193 0.0357  0.1205  0.0539  36  GLN A N   
263  C CA  . GLN A 35  ? 0.2911 0.3517 0.3307 0.0356  0.1299  0.0593  36  GLN A CA  
264  C C   . GLN A 35  ? 0.3231 0.3941 0.3837 0.0375  0.1376  0.0628  36  GLN A C   
265  O O   . GLN A 35  ? 0.3149 0.3879 0.3819 0.0434  0.1431  0.0601  36  GLN A O   
266  C CB  . GLN A 35  ? 0.3364 0.3813 0.3427 0.0406  0.1344  0.0557  36  GLN A CB  
267  C CG  . GLN A 35  ? 0.3436 0.3862 0.3354 0.0412  0.1430  0.0611  36  GLN A CG  
268  C CD  . GLN A 35  ? 0.4412 0.4691 0.4005 0.0486  0.1489  0.0573  36  GLN A CD  
269  O OE1 . GLN A 35  ? 0.4168 0.4399 0.3703 0.0558  0.1527  0.0520  36  GLN A OE1 
270  N NE2 . GLN A 35  ? 0.4074 0.4272 0.3452 0.0471  0.1480  0.0591  36  GLN A NE2 
271  N N   . ASN A 36  ? 0.3546 0.4309 0.4248 0.0321  0.1360  0.0681  37  ASN A N   
272  C CA  . ASN A 36  ? 0.3138 0.3987 0.4038 0.0323  0.1411  0.0718  37  ASN A CA  
273  C C   . ASN A 36  ? 0.3154 0.4094 0.4315 0.0342  0.1387  0.0689  37  ASN A C   
274  O O   . ASN A 36  ? 0.3349 0.4330 0.4596 0.0384  0.1460  0.0689  37  ASN A O   
275  C CB  . ASN A 36  ? 0.3708 0.4514 0.4448 0.0375  0.1533  0.0738  37  ASN A CB  
276  C CG  . ASN A 36  ? 0.4127 0.4843 0.4620 0.0356  0.1548  0.0771  37  ASN A CG  
277  O OD1 . ASN A 36  ? 0.4305 0.5031 0.4835 0.0293  0.1488  0.0806  37  ASN A OD1 
278  N ND2 . ASN A 36  ? 0.4463 0.5085 0.4695 0.0418  0.1621  0.0754  37  ASN A ND2 
279  N N   . ASN A 37  ? 0.3121 0.4090 0.4398 0.0314  0.1278  0.0660  38  ASN A N   
280  C CA  . ASN A 37  ? 0.3228 0.4271 0.4739 0.0327  0.1219  0.0625  38  ASN A CA  
281  C C   . ASN A 37  ? 0.3209 0.4233 0.4690 0.0401  0.1269  0.0576  38  ASN A C   
282  O O   . ASN A 37  ? 0.3453 0.4535 0.5118 0.0423  0.1238  0.0547  38  ASN A O   
283  C CB  . ASN A 37  ? 0.3757 0.4884 0.5502 0.0304  0.1217  0.0657  38  ASN A CB  
284  C CG  . ASN A 37  ? 0.4118 0.5275 0.5989 0.0243  0.1101  0.0669  38  ASN A CG  
285  O OD1 . ASN A 37  ? 0.4721 0.5840 0.6477 0.0209  0.1052  0.0678  38  ASN A OD1 
286  N ND2 . ASN A 37  ? 0.4843 0.6063 0.6942 0.0234  0.1052  0.0664  38  ASN A ND2 
287  N N   . LYS A 38  ? 0.3007 0.3938 0.4245 0.0443  0.1335  0.0560  39  LYS A N   
288  C CA  . LYS A 38  ? 0.3298 0.4185 0.4481 0.0520  0.1366  0.0504  39  LYS A CA  
289  C C   . LYS A 38  ? 0.2726 0.3536 0.3784 0.0521  0.1305  0.0471  39  LYS A C   
290  O O   . LYS A 38  ? 0.2964 0.3681 0.3806 0.0475  0.1260  0.0477  39  LYS A O   
291  C CB  . LYS A 38  ? 0.3426 0.4247 0.4414 0.0585  0.1486  0.0498  39  LYS A CB  
292  C CG  . LYS A 38  ? 0.3687 0.4597 0.4813 0.0595  0.1561  0.0531  39  LYS A CG  
293  C CD  . LYS A 38  ? 0.5258 0.6113 0.6205 0.0681  0.1671  0.0510  39  LYS A CD  
294  C CE  . LYS A 38  ? 0.6125 0.6977 0.7128 0.0757  0.1671  0.0441  39  LYS A CE  
295  N NZ  . LYS A 38  ? 0.6180 0.6904 0.6903 0.0847  0.1733  0.0390  39  LYS A NZ  
296  N N   . LYS A 39  ? 0.2505 0.3307 0.3646 0.0551  0.1237  0.0421  40  LYS A N   
297  C CA  . LYS A 39  ? 0.2648 0.3337 0.3645 0.0525  0.1108  0.0378  40  LYS A CA  
298  C C   . LYS A 39  ? 0.2530 0.3068 0.3315 0.0584  0.1119  0.0319  40  LYS A C   
299  O O   . LYS A 39  ? 0.2980 0.3530 0.3821 0.0661  0.1194  0.0295  40  LYS A O   
300  C CB  . LYS A 39  ? 0.3012 0.3784 0.4234 0.0518  0.1010  0.0368  40  LYS A CB  
301  C CG  . LYS A 39  ? 0.2942 0.3851 0.4371 0.0463  0.0972  0.0414  40  LYS A CG  
302  C CD  . LYS A 39  ? 0.2875 0.3867 0.4533 0.0480  0.0884  0.0393  40  LYS A CD  
303  C CE  . LYS A 39  ? 0.3012 0.4075 0.4788 0.0414  0.0792  0.0411  40  LYS A CE  
304  N NZ  . LYS A 39  ? 0.2745 0.3844 0.4666 0.0428  0.0689  0.0370  40  LYS A NZ  
305  N N   . TYR A 40  ? 0.2940 0.3335 0.3492 0.0548  0.1039  0.0295  41  TYR A N   
306  C CA  . TYR A 40  ? 0.3226 0.3451 0.3562 0.0594  0.1026  0.0237  41  TYR A CA  
307  C C   . TYR A 40  ? 0.2900 0.3039 0.3183 0.0548  0.0891  0.0216  41  TYR A C   
308  O O   . TYR A 40  ? 0.2623 0.2751 0.2842 0.0473  0.0820  0.0239  41  TYR A O   
309  C CB  . TYR A 40  ? 0.3023 0.3139 0.3094 0.0601  0.1077  0.0229  41  TYR A CB  
310  C CG  . TYR A 40  ? 0.3463 0.3675 0.3578 0.0641  0.1218  0.0267  41  TYR A CG  
311  C CD1 . TYR A 40  ? 0.3335 0.3659 0.3541 0.0584  0.1247  0.0334  41  TYR A CD1 
312  C CD2 . TYR A 40  ? 0.4005 0.4198 0.4076 0.0739  0.1325  0.0239  41  TYR A CD2 
313  C CE1 . TYR A 40  ? 0.3327 0.3737 0.3582 0.0617  0.1382  0.0381  41  TYR A CE1 
314  C CE2 . TYR A 40  ? 0.4242 0.4535 0.4360 0.0777  0.1466  0.0284  41  TYR A CE2 
315  C CZ  . TYR A 40  ? 0.3743 0.4142 0.3954 0.0712  0.1496  0.0359  41  TYR A CZ  
316  O OH  . TYR A 40  ? 0.4431 0.4921 0.4693 0.0739  0.1624  0.0412  41  TYR A OH  
317  N N   . GLU A 41  ? 0.2757 0.2837 0.3072 0.0596  0.0858  0.0178  42  GLU A N   
318  C CA  . GLU A 41  ? 0.2818 0.2822 0.3104 0.0558  0.0738  0.0170  42  GLU A CA  
319  C C   . GLU A 41  ? 0.3352 0.3153 0.3422 0.0583  0.0705  0.0120  42  GLU A C   
320  O O   . GLU A 41  ? 0.3322 0.3059 0.3353 0.0665  0.0759  0.0076  42  GLU A O   
321  C CB  . GLU A 41  ? 0.2948 0.3038 0.3451 0.0591  0.0706  0.0173  42  GLU A CB  
322  C CG  . GLU A 41  ? 0.3022 0.3310 0.3767 0.0577  0.0723  0.0213  42  GLU A CG  
323  C CD  . GLU A 41  ? 0.3167 0.3529 0.4122 0.0631  0.0694  0.0201  42  GLU A CD  
324  O OE1 . GLU A 41  ? 0.4025 0.4542 0.5202 0.0639  0.0714  0.0220  42  GLU A OE1 
325  O OE2 . GLU A 41  ? 0.3545 0.3803 0.4445 0.0667  0.0647  0.0172  42  GLU A OE2 
326  N N   . MET A 42  ? 0.2972 0.2673 0.2915 0.0514  0.0612  0.0125  43  MET A N   
327  C CA  . MET A 42  ? 0.3259 0.2756 0.3015 0.0523  0.0558  0.0080  43  MET A CA  
328  C C   . MET A 42  ? 0.3211 0.2661 0.2996 0.0466  0.0448  0.0104  43  MET A C   
329  O O   . MET A 42  ? 0.2928 0.2461 0.2762 0.0390  0.0401  0.0151  43  MET A O   
330  C CB  . MET A 42  ? 0.3518 0.2918 0.3060 0.0495  0.0559  0.0061  43  MET A CB  
331  C CG  . MET A 42  ? 0.4561 0.3963 0.4024 0.0576  0.0673  0.0031  43  MET A CG  
332  S SD  . MET A 42  ? 0.5587 0.5056 0.4952 0.0545  0.0735  0.0061  43  MET A SD  
333  C CE  . MET A 42  ? 0.3644 0.3332 0.3253 0.0465  0.0726  0.0140  43  MET A CE  
334  N N   . TYR A 43  ? 0.3330 0.2649 0.3086 0.0506  0.0408  0.0074  44  TYR A N   
335  C CA  . TYR A 43  ? 0.3075 0.2342 0.2864 0.0461  0.0314  0.0106  44  TYR A CA  
336  C C   . TYR A 43  ? 0.3446 0.2488 0.3066 0.0447  0.0246  0.0073  44  TYR A C   
337  O O   . TYR A 43  ? 0.3834 0.2748 0.3355 0.0517  0.0267  0.0011  44  TYR A O   
338  C CB  . TYR A 43  ? 0.2915 0.2239 0.2862 0.0525  0.0317  0.0112  44  TYR A CB  
339  C CG  . TYR A 43  ? 0.3160 0.2699 0.3291 0.0539  0.0369  0.0139  44  TYR A CG  
340  C CD1 . TYR A 43  ? 0.2799 0.2465 0.3009 0.0472  0.0331  0.0194  44  TYR A CD1 
341  C CD2 . TYR A 43  ? 0.3055 0.2674 0.3288 0.0620  0.0453  0.0109  44  TYR A CD2 
342  C CE1 . TYR A 43  ? 0.2542 0.2392 0.2923 0.0486  0.0365  0.0213  44  TYR A CE1 
343  C CE2 . TYR A 43  ? 0.2754 0.2568 0.3180 0.0626  0.0492  0.0135  44  TYR A CE2 
344  C CZ  . TYR A 43  ? 0.2652 0.2573 0.3147 0.0559  0.0442  0.0184  44  TYR A CZ  
345  O OH  . TYR A 43  ? 0.3042 0.3145 0.3729 0.0566  0.0467  0.0205  44  TYR A OH  
346  N N   . TYR A 44  ? 0.2966 0.1964 0.2559 0.0358  0.0162  0.0115  45  TYR A N   
347  C CA  . TYR A 44  ? 0.3433 0.2218 0.2899 0.0328  0.0081  0.0095  45  TYR A CA  
348  C C   . TYR A 44  ? 0.3435 0.2196 0.2975 0.0276  0.0007  0.0158  45  TYR A C   
349  O O   . TYR A 44  ? 0.3329 0.2239 0.2968 0.0224  0.0000  0.0224  45  TYR A O   
350  C CB  . TYR A 44  ? 0.3743 0.2477 0.3085 0.0253  0.0045  0.0086  45  TYR A CB  
351  C CG  . TYR A 44  ? 0.3764 0.2509 0.2998 0.0295  0.0110  0.0033  45  TYR A CG  
352  C CD1 . TYR A 44  ? 0.4626 0.3217 0.3720 0.0376  0.0128  -0.0045 45  TYR A CD1 
353  C CD2 . TYR A 44  ? 0.3985 0.2888 0.3245 0.0257  0.0150  0.0062  45  TYR A CD2 
354  C CE1 . TYR A 44  ? 0.4589 0.3190 0.3565 0.0422  0.0193  -0.0087 45  TYR A CE1 
355  C CE2 . TYR A 44  ? 0.4692 0.3598 0.3842 0.0295  0.0212  0.0023  45  TYR A CE2 
356  C CZ  . TYR A 44  ? 0.4599 0.3358 0.3604 0.0378  0.0237  -0.0048 45  TYR A CZ  
357  O OH  . TYR A 44  ? 0.4731 0.3495 0.3609 0.0423  0.0306  -0.0080 45  TYR A OH  
358  N N   . GLY A 45  ? 0.3435 0.2003 0.2920 0.0294  -0.0049 0.0140  46  GLY A N   
359  C CA  . GLY A 45  ? 0.3756 0.2263 0.3279 0.0227  -0.0127 0.0208  46  GLY A CA  
360  C C   . GLY A 45  ? 0.3515 0.2130 0.3169 0.0256  -0.0117 0.0267  46  GLY A C   
361  O O   . GLY A 45  ? 0.3288 0.1962 0.3003 0.0347  -0.0068 0.0238  46  GLY A O   
362  N N   . LEU A 46  ? 0.3649 0.2291 0.3348 0.0181  -0.0165 0.0352  47  LEU A N   
363  C CA  . LEU A 46  ? 0.3452 0.2135 0.3236 0.0208  -0.0179 0.0415  47  LEU A CA  
364  C C   . LEU A 46  ? 0.3231 0.2145 0.3112 0.0181  -0.0157 0.0479  47  LEU A C   
365  O O   . LEU A 46  ? 0.3410 0.2401 0.3288 0.0096  -0.0169 0.0521  47  LEU A O   
366  C CB  . LEU A 46  ? 0.3709 0.2216 0.3456 0.0155  -0.0254 0.0473  47  LEU A CB  
367  C CG  . LEU A 46  ? 0.3907 0.2160 0.3566 0.0189  -0.0297 0.0413  47  LEU A CG  
368  C CD1 . LEU A 46  ? 0.4500 0.2583 0.4145 0.0124  -0.0377 0.0485  47  LEU A CD1 
369  C CD2 . LEU A 46  ? 0.3783 0.2013 0.3458 0.0317  -0.0263 0.0353  47  LEU A CD2 
370  N N   . GLN A 47  ? 0.3284 0.2301 0.3251 0.0260  -0.0132 0.0484  48  GLN A N   
371  C CA  . GLN A 47  ? 0.3032 0.2247 0.3087 0.0253  -0.0127 0.0543  48  GLN A CA  
372  C C   . GLN A 47  ? 0.3544 0.2725 0.3588 0.0213  -0.0176 0.0638  48  GLN A C   
373  O O   . GLN A 47  ? 0.3759 0.3075 0.3829 0.0164  -0.0181 0.0700  48  GLN A O   
374  C CB  . GLN A 47  ? 0.3657 0.2979 0.3813 0.0359  -0.0095 0.0506  48  GLN A CB  
375  C CG  . GLN A 47  ? 0.3846 0.3296 0.4080 0.0395  -0.0117 0.0561  48  GLN A CG  
376  C CD  . GLN A 47  ? 0.3520 0.3029 0.3856 0.0508  -0.0103 0.0513  48  GLN A CD  
377  O OE1 . GLN A 47  ? 0.3184 0.2734 0.3578 0.0545  -0.0057 0.0444  48  GLN A OE1 
378  N NE2 . GLN A 47  ? 0.3605 0.3123 0.3969 0.0565  -0.0142 0.0551  48  GLN A NE2 
379  N N   . SER A 48  ? 0.3482 0.2480 0.3482 0.0234  -0.0211 0.0652  49  SER A N   
380  C CA  . SER A 48  ? 0.4064 0.2998 0.4044 0.0193  -0.0254 0.0752  49  SER A CA  
381  C C   . SER A 48  ? 0.4206 0.2891 0.4112 0.0154  -0.0298 0.0749  49  SER A C   
382  O O   . SER A 48  ? 0.4174 0.2714 0.4051 0.0224  -0.0307 0.0687  49  SER A O   
383  C CB  . SER A 48  ? 0.4517 0.3489 0.4534 0.0285  -0.0261 0.0788  49  SER A CB  
384  O OG  . SER A 48  ? 0.4602 0.3433 0.4574 0.0262  -0.0302 0.0873  49  SER A OG  
385  N N   . VAL A 49  ? 0.3842 0.2477 0.3727 0.0046  -0.0329 0.0813  50  VAL A N   
386  C CA  . VAL A 49  ? 0.4190 0.2580 0.4018 -0.0001 -0.0385 0.0811  50  VAL A CA  
387  C C   . VAL A 49  ? 0.4725 0.2968 0.4543 0.0039  -0.0420 0.0870  50  VAL A C   
388  O O   . VAL A 49  ? 0.4784 0.2812 0.4554 0.0072  -0.0460 0.0824  50  VAL A O   
389  C CB  . VAL A 49  ? 0.4821 0.3211 0.4657 -0.0134 -0.0415 0.0867  50  VAL A CB  
390  C CG1 . VAL A 49  ? 0.5237 0.3364 0.5035 -0.0187 -0.0487 0.0878  50  VAL A CG1 
391  C CG2 . VAL A 49  ? 0.4284 0.2778 0.4109 -0.0163 -0.0391 0.0794  50  VAL A CG2 
392  N N   . GLN A 50  ? 0.4685 0.3036 0.4539 0.0044  -0.0409 0.0972  51  GLN A N   
393  C CA  . GLN A 50  ? 0.4883 0.3088 0.4716 0.0080  -0.0444 0.1043  51  GLN A CA  
394  C C   . GLN A 50  ? 0.5077 0.3221 0.4894 0.0215  -0.0443 0.0966  51  GLN A C   
395  O O   . GLN A 50  ? 0.5324 0.3272 0.5103 0.0253  -0.0486 0.0982  51  GLN A O   
396  C CB  . GLN A 50  ? 0.5041 0.3386 0.4900 0.0061  -0.0426 0.1175  51  GLN A CB  
397  C CG  . GLN A 50  ? 0.5373 0.3949 0.5263 0.0150  -0.0382 0.1159  51  GLN A CG  
398  C CD  . GLN A 50  ? 0.6203 0.4946 0.6107 0.0121  -0.0361 0.1281  51  GLN A CD  
399  O OE1 . GLN A 50  ? 0.6473 0.5368 0.6410 0.0047  -0.0337 0.1304  51  GLN A OE1 
400  N NE2 . GLN A 50  ? 0.6448 0.5163 0.6319 0.0187  -0.0370 0.1358  51  GLN A NE2 
401  N N   . ASP A 51  ? 0.4958 0.3264 0.4813 0.0288  -0.0398 0.0883  52  ASP A N   
402  C CA  . ASP A 51  ? 0.5233 0.3507 0.5100 0.0416  -0.0394 0.0805  52  ASP A CA  
403  C C   . ASP A 51  ? 0.4730 0.2902 0.4574 0.0447  -0.0386 0.0683  52  ASP A C   
404  O O   . ASP A 51  ? 0.4588 0.2722 0.4447 0.0554  -0.0381 0.0613  52  ASP A O   
405  C CB  . ASP A 51  ? 0.5109 0.3622 0.5052 0.0487  -0.0353 0.0791  52  ASP A CB  
406  C CG  . ASP A 51  ? 0.5479 0.4084 0.5426 0.0490  -0.0365 0.0902  52  ASP A CG  
407  O OD1 . ASP A 51  ? 0.5863 0.4340 0.5769 0.0535  -0.0402 0.0954  52  ASP A OD1 
408  O OD2 . ASP A 51  ? 0.5414 0.4212 0.5394 0.0451  -0.0339 0.0936  52  ASP A OD2 
409  N N   . LYS A 52  ? 0.4652 0.2782 0.4457 0.0364  -0.0385 0.0655  53  LYS A N   
410  C CA  . LYS A 52  ? 0.4240 0.2284 0.4003 0.0399  -0.0372 0.0538  53  LYS A CA  
411  C C   . LYS A 52  ? 0.4051 0.2260 0.3877 0.0497  -0.0305 0.0460  53  LYS A C   
412  O O   . LYS A 52  ? 0.3708 0.1844 0.3521 0.0584  -0.0291 0.0373  53  LYS A O   
413  C CB  . LYS A 52  ? 0.4806 0.2577 0.4497 0.0437  -0.0432 0.0504  53  LYS A CB  
414  C CG  . LYS A 52  ? 0.4987 0.2569 0.4622 0.0327  -0.0504 0.0560  53  LYS A CG  
415  C CD  . LYS A 52  ? 0.5203 0.2724 0.4776 0.0279  -0.0511 0.0482  53  LYS A CD  
416  C CE  . LYS A 52  ? 0.5967 0.3302 0.5506 0.0167  -0.0594 0.0530  53  LYS A CE  
417  N NZ  . LYS A 52  ? 0.5803 0.3079 0.5276 0.0126  -0.0612 0.0448  53  LYS A NZ  
418  N N   . LYS A 53  ? 0.3844 0.2282 0.3750 0.0485  -0.0265 0.0494  54  LYS A N   
419  C CA  . LYS A 53  ? 0.3453 0.2068 0.3447 0.0562  -0.0204 0.0432  54  LYS A CA  
420  C C   . LYS A 53  ? 0.3350 0.2047 0.3327 0.0513  -0.0155 0.0386  54  LYS A C   
421  O O   . LYS A 53  ? 0.3579 0.2358 0.3546 0.0423  -0.0157 0.0433  54  LYS A O   
422  C CB  . LYS A 53  ? 0.3759 0.2564 0.3848 0.0582  -0.0201 0.0489  54  LYS A CB  
423  C CG  . LYS A 53  ? 0.4010 0.3014 0.4217 0.0644  -0.0148 0.0434  54  LYS A CG  
424  C CD  . LYS A 53  ? 0.4138 0.3115 0.4413 0.0764  -0.0143 0.0374  54  LYS A CD  
425  C CE  . LYS A 53  ? 0.4815 0.4009 0.5244 0.0821  -0.0102 0.0338  54  LYS A CE  
426  N NZ  . LYS A 53  ? 0.5654 0.4836 0.6158 0.0917  -0.0067 0.0254  54  LYS A NZ  
427  N N   . ALA A 54  ? 0.3115 0.1792 0.3086 0.0576  -0.0110 0.0298  55  ALA A N   
428  C CA  . ALA A 54  ? 0.3409 0.2139 0.3339 0.0538  -0.0062 0.0256  55  ALA A CA  
429  C C   . ALA A 54  ? 0.2912 0.1887 0.2952 0.0530  -0.0007 0.0270  55  ALA A C   
430  O O   . ALA A 54  ? 0.2981 0.2082 0.3145 0.0592  0.0012  0.0272  55  ALA A O   
431  C CB  . ALA A 54  ? 0.3372 0.2007 0.3249 0.0618  -0.0022 0.0161  55  ALA A CB  
432  N N   . VAL A 55  ? 0.3036 0.2071 0.3034 0.0455  0.0011  0.0276  56  VAL A N   
433  C CA  . VAL A 55  ? 0.2695 0.1944 0.2789 0.0448  0.0063  0.0282  56  VAL A CA  
434  C C   . VAL A 55  ? 0.2898 0.2214 0.3068 0.0537  0.0137  0.0221  56  VAL A C   
435  O O   . VAL A 55  ? 0.3156 0.2364 0.3249 0.0580  0.0170  0.0163  56  VAL A O   
436  C CB  . VAL A 55  ? 0.2615 0.1889 0.2629 0.0359  0.0067  0.0292  56  VAL A CB  
437  C CG1 . VAL A 55  ? 0.2750 0.2231 0.2860 0.0355  0.0119  0.0296  56  VAL A CG1 
438  C CG2 . VAL A 55  ? 0.3042 0.2284 0.3016 0.0268  -0.0002 0.0359  56  VAL A CG2 
439  N N   . ASN A 56  ? 0.2658 0.2157 0.2984 0.0568  0.0163  0.0233  57  ASN A N   
440  C CA  . ASN A 56  ? 0.2362 0.1948 0.2800 0.0648  0.0234  0.0184  57  ASN A CA  
441  C C   . ASN A 56  ? 0.2687 0.2487 0.3279 0.0633  0.0260  0.0208  57  ASN A C   
442  O O   . ASN A 56  ? 0.2631 0.2504 0.3224 0.0569  0.0221  0.0254  57  ASN A O   
443  C CB  . ASN A 56  ? 0.3109 0.2648 0.3621 0.0743  0.0218  0.0158  57  ASN A CB  
444  C CG  . ASN A 56  ? 0.3471 0.3072 0.4073 0.0751  0.0150  0.0203  57  ASN A CG  
445  O OD1 . ASN A 56  ? 0.3933 0.3696 0.4695 0.0784  0.0156  0.0206  57  ASN A OD1 
446  N ND2 . ASN A 56  ? 0.4006 0.3478 0.4503 0.0722  0.0082  0.0243  57  ASN A ND2 
447  N N   . SER A 57  ? 0.2606 0.2511 0.3339 0.0696  0.0325  0.0175  58  SER A N   
448  C CA  . SER A 57  ? 0.2682 0.2781 0.3579 0.0682  0.0350  0.0194  58  SER A CA  
449  C C   . SER A 57  ? 0.2620 0.2818 0.3640 0.0690  0.0274  0.0223  58  SER A C   
450  O O   . SER A 57  ? 0.2473 0.2818 0.3609 0.0667  0.0271  0.0241  58  SER A O   
451  C CB  . SER A 57  ? 0.2919 0.3107 0.3964 0.0748  0.0437  0.0158  58  SER A CB  
452  O OG  . SER A 57  ? 0.3633 0.3798 0.4769 0.0837  0.0427  0.0124  58  SER A OG  
453  N N   . SER A 58  ? 0.2501 0.2618 0.3493 0.0726  0.0210  0.0228  59  SER A N   
454  C CA  . SER A 58  ? 0.2387 0.2584 0.3459 0.0743  0.0134  0.0257  59  SER A CA  
455  C C   . SER A 58  ? 0.2281 0.2437 0.3213 0.0672  0.0078  0.0314  59  SER A C   
456  O O   . SER A 58  ? 0.2595 0.2825 0.3570 0.0686  0.0019  0.0344  59  SER A O   
457  C CB  . SER A 58  ? 0.2820 0.2960 0.3943 0.0835  0.0095  0.0237  59  SER A CB  
458  O OG  . SER A 58  ? 0.3213 0.3435 0.4517 0.0910  0.0134  0.0187  59  SER A OG  
459  N N   . THR A 59  ? 0.2516 0.2557 0.3286 0.0603  0.0093  0.0328  60  THR A N   
460  C CA  . THR A 59  ? 0.2612 0.2616 0.3267 0.0532  0.0043  0.0385  60  THR A CA  
461  C C   . THR A 59  ? 0.2202 0.2371 0.2909 0.0489  0.0029  0.0414  60  THR A C   
462  O O   . THR A 59  ? 0.1966 0.2209 0.2707 0.0460  0.0069  0.0395  60  THR A O   
463  C CB  . THR A 59  ? 0.2621 0.2471 0.3114 0.0465  0.0056  0.0385  60  THR A CB  
464  O OG1 . THR A 59  ? 0.2411 0.2095 0.2849 0.0511  0.0055  0.0356  60  THR A OG1 
465  C CG2 . THR A 59  ? 0.2550 0.2377 0.2952 0.0383  0.0005  0.0450  60  THR A CG2 
466  N N   . ILE A 60  ? 0.2151 0.2373 0.2857 0.0490  -0.0029 0.0462  61  ILE A N   
467  C CA  . ILE A 60  ? 0.2018 0.2393 0.2762 0.0461  -0.0054 0.0489  61  ILE A CA  
468  C C   . ILE A 60  ? 0.1965 0.2303 0.2578 0.0369  -0.0066 0.0539  61  ILE A C   
469  O O   . ILE A 60  ? 0.2316 0.2561 0.2843 0.0352  -0.0091 0.0584  61  ILE A O   
470  C CB  . ILE A 60  ? 0.2166 0.2635 0.2987 0.0535  -0.0110 0.0505  61  ILE A CB  
471  C CG1 . ILE A 60  ? 0.2392 0.2909 0.3370 0.0623  -0.0107 0.0449  61  ILE A CG1 
472  C CG2 . ILE A 60  ? 0.1940 0.2560 0.2782 0.0514  -0.0144 0.0530  61  ILE A CG2 
473  C CD1 . ILE A 60  ? 0.2298 0.2843 0.3327 0.0718  -0.0172 0.0454  61  ILE A CD1 
474  N N   . PHE A 61  ? 0.2088 0.2499 0.2693 0.0309  -0.0050 0.0535  62  PHE A N   
475  C CA  . PHE A 61  ? 0.2108 0.2514 0.2615 0.0223  -0.0066 0.0576  62  PHE A CA  
476  C C   . PHE A 61  ? 0.1971 0.2550 0.2526 0.0218  -0.0098 0.0602  62  PHE A C   
477  O O   . PHE A 61  ? 0.2102 0.2793 0.2759 0.0262  -0.0101 0.0573  62  PHE A O   
478  C CB  . PHE A 61  ? 0.2147 0.2494 0.2589 0.0161  -0.0030 0.0545  62  PHE A CB  
479  C CG  . PHE A 61  ? 0.2191 0.2361 0.2559 0.0164  0.0000  0.0512  62  PHE A CG  
480  C CD1 . PHE A 61  ? 0.2286 0.2431 0.2707 0.0230  0.0045  0.0461  62  PHE A CD1 
481  C CD2 . PHE A 61  ? 0.2304 0.2338 0.2553 0.0102  -0.0019 0.0526  62  PHE A CD2 
482  C CE1 . PHE A 61  ? 0.2295 0.2281 0.2638 0.0244  0.0073  0.0424  62  PHE A CE1 
483  C CE2 . PHE A 61  ? 0.2776 0.2638 0.2947 0.0113  -0.0001 0.0486  62  PHE A CE2 
484  C CZ  . PHE A 61  ? 0.2400 0.2239 0.2611 0.0189  0.0047  0.0434  62  PHE A CZ  
485  N N   . GLU A 62  ? 0.2038 0.2638 0.2526 0.0166  -0.0125 0.0657  63  GLU A N   
486  C CA  . GLU A 62  ? 0.1781 0.2543 0.2294 0.0154  -0.0152 0.0678  63  GLU A CA  
487  C C   . GLU A 62  ? 0.2004 0.2793 0.2506 0.0094  -0.0136 0.0647  63  GLU A C   
488  O O   . GLU A 62  ? 0.2142 0.2833 0.2564 0.0025  -0.0120 0.0646  63  GLU A O   
489  C CB  . GLU A 62  ? 0.1646 0.2434 0.2097 0.0119  -0.0175 0.0752  63  GLU A CB  
490  C CG  . GLU A 62  ? 0.1956 0.2727 0.2405 0.0186  -0.0191 0.0793  63  GLU A CG  
491  C CD  . GLU A 62  ? 0.3277 0.4070 0.3665 0.0150  -0.0202 0.0881  63  GLU A CD  
492  O OE1 . GLU A 62  ? 0.3354 0.4221 0.3726 0.0082  -0.0203 0.0907  63  GLU A OE1 
493  O OE2 . GLU A 62  ? 0.3541 0.4278 0.3901 0.0191  -0.0207 0.0927  63  GLU A OE2 
494  N N   . LEU A 63  ? 0.1525 0.2439 0.2105 0.0122  -0.0148 0.0620  64  LEU A N   
495  C CA  . LEU A 63  ? 0.1417 0.2356 0.1984 0.0070  -0.0136 0.0596  64  LEU A CA  
496  C C   . LEU A 63  ? 0.1461 0.2483 0.1980 0.0016  -0.0169 0.0627  64  LEU A C   
497  O O   . LEU A 63  ? 0.1524 0.2548 0.2011 -0.0033 -0.0165 0.0610  64  LEU A O   
498  C CB  . LEU A 63  ? 0.1421 0.2450 0.2105 0.0118  -0.0136 0.0558  64  LEU A CB  
499  C CG  . LEU A 63  ? 0.1383 0.2371 0.2159 0.0178  -0.0104 0.0525  64  LEU A CG  
500  C CD1 . LEU A 63  ? 0.1259 0.2353 0.2171 0.0210  -0.0113 0.0496  64  LEU A CD1 
501  C CD2 . LEU A 63  ? 0.2057 0.2898 0.2762 0.0150  -0.0040 0.0507  64  LEU A CD2 
502  N N   . GLY A 64  ? 0.2026 0.2097 0.2078 0.0242  -0.0114 0.0048  65  GLY A N   
503  C CA  . GLY A 64  ? 0.2183 0.2245 0.2217 0.0184  -0.0113 0.0035  65  GLY A CA  
504  C C   . GLY A 64  ? 0.1846 0.2016 0.1861 0.0166  -0.0115 0.0045  65  GLY A C   
505  O O   . GLY A 64  ? 0.1913 0.2136 0.1925 0.0176  -0.0121 0.0086  65  GLY A O   
506  N N   . SER A 65  ? 0.1896 0.2098 0.1905 0.0140  -0.0113 0.0006  66  SER A N   
507  C CA  . SER A 65  ? 0.2102 0.2391 0.2097 0.0124  -0.0115 0.0022  66  SER A CA  
508  C C   . SER A 65  ? 0.1890 0.2266 0.1883 0.0159  -0.0113 0.0033  66  SER A C   
509  O O   . SER A 65  ? 0.2055 0.2488 0.2043 0.0148  -0.0113 0.0061  66  SER A O   
510  C CB  . SER A 65  ? 0.2326 0.2641 0.2321 0.0098  -0.0116 -0.0021 66  SER A CB  
511  O OG  . SER A 65  ? 0.2912 0.3149 0.2926 0.0065  -0.0115 -0.0039 66  SER A OG  
512  N N   . VAL A 66  ? 0.1703 0.2090 0.1705 0.0201  -0.0107 0.0013  67  VAL A N   
513  C CA  . VAL A 66  ? 0.1685 0.2166 0.1695 0.0233  -0.0098 0.0033  67  VAL A CA  
514  C C   . VAL A 66  ? 0.1926 0.2419 0.1960 0.0228  -0.0105 0.0091  67  VAL A C   
515  O O   . VAL A 66  ? 0.1961 0.2536 0.2014 0.0234  -0.0099 0.0119  67  VAL A O   
516  C CB  . VAL A 66  ? 0.1860 0.2353 0.1875 0.0284  -0.0085 -0.0010 67  VAL A CB  
517  C CG1 . VAL A 66  ? 0.1986 0.2575 0.2026 0.0322  -0.0069 0.0018  67  VAL A CG1 
518  C CG2 . VAL A 66  ? 0.1913 0.2432 0.1893 0.0287  -0.0081 -0.0073 67  VAL A CG2 
519  N N   . SER A 67  ? 0.1889 0.2308 0.1923 0.0211  -0.0119 0.0112  68  SER A N   
520  C CA  . SER A 67  ? 0.1503 0.1940 0.1549 0.0201  -0.0134 0.0160  68  SER A CA  
521  C C   . SER A 67  ? 0.1520 0.2008 0.1563 0.0168  -0.0135 0.0177  68  SER A C   
522  O O   . SER A 67  ? 0.1743 0.2273 0.1809 0.0161  -0.0146 0.0207  68  SER A O   
523  C CB  . SER A 67  ? 0.1492 0.1842 0.1515 0.0184  -0.0147 0.0179  68  SER A CB  
524  O OG  . SER A 67  ? 0.1915 0.2199 0.1948 0.0214  -0.0145 0.0172  68  SER A OG  
525  N N   . LYS A 68  ? 0.1431 0.1913 0.1450 0.0147  -0.0126 0.0158  69  LYS A N   
526  C CA  . LYS A 68  ? 0.1178 0.1694 0.1197 0.0121  -0.0125 0.0175  69  LYS A CA  
527  C C   . LYS A 68  ? 0.1494 0.2090 0.1545 0.0134  -0.0117 0.0198  69  LYS A C   
528  O O   . LYS A 68  ? 0.1590 0.2202 0.1657 0.0111  -0.0120 0.0223  69  LYS A O   
529  C CB  . LYS A 68  ? 0.1694 0.2205 0.1692 0.0109  -0.0118 0.0152  69  LYS A CB  
530  C CG  . LYS A 68  ? 0.1500 0.1945 0.1480 0.0086  -0.0120 0.0136  69  LYS A CG  
531  C CD  . LYS A 68  ? 0.1576 0.2037 0.1552 0.0073  -0.0115 0.0114  69  LYS A CD  
532  C CE  . LYS A 68  ? 0.1784 0.2189 0.1755 0.0045  -0.0111 0.0102  69  LYS A CE  
533  N NZ  . LYS A 68  ? 0.1995 0.2356 0.1972 0.0046  -0.0111 0.0076  69  LYS A NZ  
534  N N   . LEU A 69  ? 0.1378 0.2022 0.1442 0.0168  -0.0104 0.0190  70  LEU A N   
535  C CA  . LEU A 69  ? 0.1280 0.2012 0.1380 0.0179  -0.0088 0.0219  70  LEU A CA  
536  C C   . LEU A 69  ? 0.1395 0.2149 0.1548 0.0166  -0.0102 0.0251  70  LEU A C   
537  O O   . LEU A 69  ? 0.1578 0.2387 0.1772 0.0148  -0.0095 0.0284  70  LEU A O   
538  C CB  . LEU A 69  ? 0.1405 0.2193 0.1503 0.0225  -0.0067 0.0198  70  LEU A CB  
539  C CG  . LEU A 69  ? 0.1391 0.2173 0.1435 0.0241  -0.0059 0.0154  70  LEU A CG  
540  C CD1 . LEU A 69  ? 0.1433 0.2280 0.1470 0.0291  -0.0035 0.0127  70  LEU A CD1 
541  C CD2 . LEU A 69  ? 0.1381 0.2193 0.1402 0.0221  -0.0055 0.0176  70  LEU A CD2 
542  N N   . PHE A 70  ? 0.1529 0.2243 0.1685 0.0173  -0.0123 0.0244  71  PHE A N   
543  C CA  . PHE A 70  ? 0.1498 0.2246 0.1703 0.0160  -0.0145 0.0271  71  PHE A CA  
544  C C   . PHE A 70  ? 0.1467 0.2174 0.1656 0.0112  -0.0166 0.0278  71  PHE A C   
545  O O   . PHE A 70  ? 0.1567 0.2316 0.1802 0.0086  -0.0180 0.0296  71  PHE A O   
546  C CB  . PHE A 70  ? 0.1602 0.2328 0.1811 0.0193  -0.0163 0.0268  71  PHE A CB  
547  C CG  . PHE A 70  ? 0.1564 0.2341 0.1807 0.0246  -0.0142 0.0259  71  PHE A CG  
548  C CD1 . PHE A 70  ? 0.1626 0.2514 0.1943 0.0261  -0.0132 0.0281  71  PHE A CD1 
549  C CD2 . PHE A 70  ? 0.2058 0.2776 0.2265 0.0279  -0.0127 0.0225  71  PHE A CD2 
550  C CE1 . PHE A 70  ? 0.1746 0.2691 0.2094 0.0315  -0.0106 0.0269  71  PHE A CE1 
551  C CE2 . PHE A 70  ? 0.2196 0.2957 0.2430 0.0332  -0.0105 0.0206  71  PHE A CE2 
552  C CZ  . PHE A 70  ? 0.2209 0.3087 0.2511 0.0354  -0.0092 0.0228  71  PHE A CZ  
553  N N   . THR A 71  ? 0.1651 0.2280 0.1779 0.0099  -0.0168 0.0259  72  THR A N   
554  C CA  . THR A 71  ? 0.1564 0.2155 0.1672 0.0060  -0.0180 0.0257  72  THR A CA  
555  C C   . THR A 71  ? 0.1539 0.2160 0.1682 0.0041  -0.0165 0.0270  72  THR A C   
556  O O   . THR A 71  ? 0.1462 0.2080 0.1630 0.0009  -0.0179 0.0275  72  THR A O   
557  C CB  . THR A 71  ? 0.1663 0.2181 0.1709 0.0055  -0.0173 0.0236  72  THR A CB  
558  O OG1 . THR A 71  ? 0.1611 0.2094 0.1630 0.0072  -0.0182 0.0234  72  THR A OG1 
559  C CG2 . THR A 71  ? 0.1638 0.2119 0.1659 0.0023  -0.0181 0.0228  72  THR A CG2 
560  N N   . ALA A 72  ? 0.1486 0.2132 0.1628 0.0060  -0.0139 0.0274  73  ALA A N   
561  C CA  . ALA A 72  ? 0.1390 0.2065 0.1563 0.0048  -0.0121 0.0301  73  ALA A CA  
562  C C   . ALA A 72  ? 0.1535 0.2272 0.1781 0.0032  -0.0122 0.0331  73  ALA A C   
563  O O   . ALA A 72  ? 0.1473 0.2202 0.1759 -0.0001 -0.0122 0.0351  73  ALA A O   
564  C CB  . ALA A 72  ? 0.1672 0.2383 0.1822 0.0079  -0.0095 0.0304  73  ALA A CB  
565  N N   . THR A 73  ? 0.1474 0.2275 0.1749 0.0055  -0.0120 0.0336  74  THR A N   
566  C CA  . THR A 73  ? 0.1285 0.2169 0.1647 0.0040  -0.0118 0.0366  74  THR A CA  
567  C C   . THR A 73  ? 0.1413 0.2275 0.1809 -0.0002 -0.0158 0.0358  74  THR A C   
568  O O   . THR A 73  ? 0.1363 0.2258 0.1832 -0.0041 -0.0160 0.0379  74  THR A O   
569  C CB  . THR A 73  ? 0.1499 0.2459 0.1884 0.0085  -0.0109 0.0365  74  THR A CB  
570  O OG1 . THR A 73  ? 0.1556 0.2529 0.1895 0.0125  -0.0075 0.0357  74  THR A OG1 
571  C CG2 . THR A 73  ? 0.1491 0.2560 0.1979 0.0073  -0.0101 0.0399  74  THR A CG2 
572  N N   . ALA A 74  ? 0.1461 0.2270 0.1805 0.0003  -0.0189 0.0328  75  ALA A N   
573  C CA  . ALA A 74  ? 0.1608 0.2397 0.1961 -0.0034 -0.0230 0.0313  75  ALA A CA  
574  C C   . ALA A 74  ? 0.1764 0.2491 0.2113 -0.0077 -0.0229 0.0303  75  ALA A C   
575  O O   . ALA A 74  ? 0.1566 0.2303 0.1969 -0.0119 -0.0251 0.0298  75  ALA A O   
576  C CB  . ALA A 74  ? 0.1624 0.2364 0.1899 -0.0015 -0.0256 0.0291  75  ALA A CB  
577  N N   . GLY A 75  ? 0.1505 0.2167 0.1799 -0.0065 -0.0203 0.0298  76  GLY A N   
578  C CA  . GLY A 75  ? 0.1685 0.2282 0.1982 -0.0095 -0.0198 0.0290  76  GLY A CA  
579  C C   . GLY A 75  ? 0.1667 0.2294 0.2048 -0.0120 -0.0179 0.0329  76  GLY A C   
580  O O   . GLY A 75  ? 0.1629 0.2215 0.2053 -0.0160 -0.0189 0.0322  76  GLY A O   
581  N N   . GLY A 76  ? 0.1513 0.2210 0.1920 -0.0095 -0.0148 0.0369  77  GLY A N   
582  C CA  . GLY A 76  ? 0.1564 0.2303 0.2054 -0.0119 -0.0123 0.0418  77  GLY A CA  
583  C C   . GLY A 76  ? 0.1626 0.2416 0.2211 -0.0164 -0.0146 0.0420  77  GLY A C   
584  O O   . GLY A 76  ? 0.1763 0.2542 0.2425 -0.0210 -0.0140 0.0443  77  GLY A O   
585  N N   . TYR A 77  ? 0.1369 0.2214 0.1954 -0.0153 -0.0176 0.0396  78  TYR A N   
586  C CA  . TYR A 77  ? 0.1355 0.2268 0.2033 -0.0193 -0.0208 0.0392  78  TYR A CA  
587  C C   . TYR A 77  ? 0.1711 0.2545 0.2393 -0.0246 -0.0248 0.0350  78  TYR A C   
588  O O   . TYR A 77  ? 0.1621 0.2470 0.2400 -0.0302 -0.0256 0.0357  78  TYR A O   
589  C CB  . TYR A 77  ? 0.1195 0.2178 0.1858 -0.0155 -0.0235 0.0377  78  TYR A CB  
590  C CG  . TYR A 77  ? 0.1438 0.2516 0.2198 -0.0185 -0.0276 0.0373  78  TYR A CG  
591  C CD1 . TYR A 77  ? 0.2001 0.3049 0.2742 -0.0216 -0.0334 0.0330  78  TYR A CD1 
592  C CD2 . TYR A 77  ? 0.1336 0.2546 0.2203 -0.0179 -0.0258 0.0410  78  TYR A CD2 
593  C CE1 . TYR A 77  ? 0.2048 0.3200 0.2882 -0.0245 -0.0380 0.0323  78  TYR A CE1 
594  C CE2 . TYR A 77  ? 0.1844 0.3160 0.2814 -0.0206 -0.0300 0.0406  78  TYR A CE2 
595  C CZ  . TYR A 77  ? 0.1762 0.3048 0.2715 -0.0240 -0.0364 0.0362  78  TYR A CZ  
596  O OH  . TYR A 77  ? 0.2057 0.3461 0.3114 -0.0268 -0.0413 0.0356  78  TYR A OH  
597  N N   . ALA A 78  ? 0.1373 0.2123 0.1951 -0.0230 -0.0270 0.0304  79  ALA A N   
598  C CA  . ALA A 78  ? 0.1690 0.2364 0.2255 -0.0273 -0.0304 0.0254  79  ALA A CA  
599  C C   . ALA A 78  ? 0.1766 0.2357 0.2376 -0.0307 -0.0278 0.0263  79  ALA A C   
600  O O   . ALA A 78  ? 0.1890 0.2448 0.2560 -0.0362 -0.0302 0.0235  79  ALA A O   
601  C CB  . ALA A 78  ? 0.1890 0.2497 0.2329 -0.0243 -0.0319 0.0211  79  ALA A CB  
602  N N   . LYS A 79  ? 0.1545 0.2099 0.2128 -0.0275 -0.0231 0.0301  80  LYS A N   
603  C CA  . LYS A 79  ? 0.1685 0.2156 0.2310 -0.0298 -0.0205 0.0321  80  LYS A CA  
604  C C   . LYS A 79  ? 0.1771 0.2287 0.2527 -0.0349 -0.0195 0.0367  80  LYS A C   
605  O O   . LYS A 79  ? 0.1998 0.2439 0.2819 -0.0399 -0.0201 0.0357  80  LYS A O   
606  C CB  . LYS A 79  ? 0.1714 0.2160 0.2283 -0.0246 -0.0162 0.0362  80  LYS A CB  
607  C CG  . LYS A 79  ? 0.1869 0.2230 0.2478 -0.0256 -0.0133 0.0397  80  LYS A CG  
608  C CD  . LYS A 79  ? 0.2178 0.2604 0.2856 -0.0261 -0.0095 0.0482  80  LYS A CD  
609  C CE  . LYS A 79  ? 0.2574 0.2916 0.3277 -0.0258 -0.0063 0.0535  80  LYS A CE  
610  N NZ  . LYS A 79  ? 0.2819 0.3228 0.3599 -0.0275 -0.0024 0.0626  80  LYS A NZ  
611  N N   . ASN A 80  ? 0.1542 0.2180 0.2344 -0.0340 -0.0178 0.0414  81  ASN A N   
612  C CA  . ASN A 80  ? 0.1933 0.2628 0.2867 -0.0389 -0.0158 0.0468  81  ASN A CA  
613  C C   . ASN A 80  ? 0.1929 0.2677 0.2961 -0.0452 -0.0206 0.0430  81  ASN A C   
614  O O   . ASN A 80  ? 0.2289 0.3081 0.3451 -0.0507 -0.0193 0.0468  81  ASN A O   
615  C CB  . ASN A 80  ? 0.1985 0.2800 0.2932 -0.0350 -0.0111 0.0536  81  ASN A CB  
616  C CG  . ASN A 80  ? 0.2185 0.2951 0.3074 -0.0311 -0.0061 0.0590  81  ASN A CG  
617  O OD1 . ASN A 80  ? 0.2520 0.3238 0.3465 -0.0341 -0.0033 0.0641  81  ASN A OD1 
618  N ND2 . ASN A 80  ? 0.1905 0.2680 0.2682 -0.0246 -0.0053 0.0577  81  ASN A ND2 
619  N N   . LYS A 81  ? 0.1913 0.2661 0.2888 -0.0446 -0.0260 0.0360  82  LYS A N   
620  C CA  . LYS A 81  ? 0.2224 0.3005 0.3276 -0.0508 -0.0318 0.0309  82  LYS A CA  
621  C C   . LYS A 81  ? 0.2267 0.2906 0.3286 -0.0546 -0.0348 0.0240  82  LYS A C   
622  O O   . LYS A 81  ? 0.2597 0.3249 0.3656 -0.0597 -0.0404 0.0179  82  LYS A O   
623  C CB  . LYS A 81  ? 0.2426 0.3311 0.3437 -0.0477 -0.0365 0.0279  82  LYS A CB  
624  C CG  . LYS A 81  ? 0.2496 0.3539 0.3586 -0.0453 -0.0344 0.0337  82  LYS A CG  
625  C CD  . LYS A 81  ? 0.2956 0.4120 0.4073 -0.0447 -0.0403 0.0309  82  LYS A CD  
626  C CE  . LYS A 81  ? 0.3083 0.4304 0.4329 -0.0529 -0.0456 0.0278  82  LYS A CE  
627  N NZ  . LYS A 81  ? 0.3595 0.4899 0.5013 -0.0583 -0.0420 0.0332  82  LYS A NZ  
628  N N   . GLY A 82  ? 0.2588 0.3098 0.3539 -0.0520 -0.0312 0.0245  83  GLY A N   
629  C CA  . GLY A 82  ? 0.2601 0.2971 0.3522 -0.0545 -0.0331 0.0177  83  GLY A CA  
630  C C   . GLY A 82  ? 0.2620 0.2965 0.3413 -0.0518 -0.0373 0.0095  83  GLY A C   
631  O O   . GLY A 82  ? 0.2575 0.2820 0.3343 -0.0542 -0.0396 0.0023  83  GLY A O   
632  N N   . LYS A 83  ? 0.2228 0.2658 0.2938 -0.0467 -0.0381 0.0105  84  LYS A N   
633  C CA  . LYS A 83  ? 0.1894 0.2307 0.2477 -0.0440 -0.0415 0.0040  84  LYS A CA  
634  C C   . LYS A 83  ? 0.2247 0.2553 0.2725 -0.0395 -0.0380 0.0024  84  LYS A C   
635  O O   . LYS A 83  ? 0.2303 0.2563 0.2688 -0.0387 -0.0400 -0.0041 84  LYS A O   
636  C CB  . LYS A 83  ? 0.1908 0.2438 0.2448 -0.0401 -0.0432 0.0066  84  LYS A CB  
637  C CG  . LYS A 83  ? 0.2447 0.3105 0.3098 -0.0434 -0.0467 0.0085  84  LYS A CG  
638  C CD  . LYS A 83  ? 0.3009 0.3682 0.3684 -0.0490 -0.0534 0.0014  84  LYS A CD  
639  C CE  . LYS A 83  ? 0.3582 0.4407 0.4377 -0.0520 -0.0575 0.0033  84  LYS A CE  
640  N NZ  . LYS A 83  ? 0.4043 0.4891 0.4874 -0.0584 -0.0648 -0.0043 84  LYS A NZ  
641  N N   . ILE A 84  ? 0.2107 0.2386 0.2596 -0.0363 -0.0327 0.0083  85  ILE A N   
642  C CA  . ILE A 84  ? 0.2120 0.2308 0.2537 -0.0323 -0.0292 0.0074  85  ILE A CA  
643  C C   . ILE A 84  ? 0.2197 0.2332 0.2691 -0.0325 -0.0252 0.0128  85  ILE A C   
644  O O   . ILE A 84  ? 0.2261 0.2445 0.2845 -0.0348 -0.0241 0.0186  85  ILE A O   
645  C CB  . ILE A 84  ? 0.1954 0.2182 0.2278 -0.0264 -0.0272 0.0095  85  ILE A CB  
646  C CG1 . ILE A 84  ? 0.1879 0.2190 0.2246 -0.0244 -0.0249 0.0168  85  ILE A CG1 
647  C CG2 . ILE A 84  ? 0.2223 0.2488 0.2461 -0.0256 -0.0305 0.0053  85  ILE A CG2 
648  C CD1 . ILE A 84  ? 0.2028 0.2368 0.2316 -0.0191 -0.0229 0.0184  85  ILE A CD1 
649  N N   . SER A 85  ? 0.2027 0.2065 0.2487 -0.0297 -0.0227 0.0113  86  SER A N   
650  C CA  . SER A 85  ? 0.2058 0.2052 0.2557 -0.0272 -0.0185 0.0176  86  SER A CA  
651  C C   . SER A 85  ? 0.2019 0.2036 0.2434 -0.0208 -0.0162 0.0188  86  SER A C   
652  O O   . SER A 85  ? 0.2000 0.2008 0.2336 -0.0188 -0.0171 0.0131  86  SER A O   
653  C CB  . SER A 85  ? 0.2289 0.2147 0.2836 -0.0288 -0.0178 0.0150  86  SER A CB  
654  O OG  . SER A 85  ? 0.2967 0.2780 0.3521 -0.0242 -0.0138 0.0206  86  SER A OG  
655  N N   . PHE A 86  ? 0.2172 0.2226 0.2602 -0.0177 -0.0132 0.0260  87  PHE A N   
656  C CA  . PHE A 86  ? 0.2437 0.2521 0.2798 -0.0121 -0.0115 0.0267  87  PHE A CA  
657  C C   . PHE A 86  ? 0.2154 0.2151 0.2498 -0.0091 -0.0103 0.0238  87  PHE A C   
658  O O   . PHE A 86  ? 0.2255 0.2279 0.2545 -0.0050 -0.0094 0.0225  87  PHE A O   
659  C CB  . PHE A 86  ? 0.2163 0.2319 0.2537 -0.0094 -0.0092 0.0344  87  PHE A CB  
660  C CG  . PHE A 86  ? 0.2250 0.2509 0.2620 -0.0105 -0.0099 0.0361  87  PHE A CG  
661  C CD1 . PHE A 86  ? 0.2451 0.2741 0.2786 -0.0118 -0.0125 0.0312  87  PHE A CD1 
662  C CD2 . PHE A 86  ? 0.2188 0.2515 0.2588 -0.0096 -0.0077 0.0430  87  PHE A CD2 
663  C CE1 . PHE A 86  ? 0.2569 0.2949 0.2909 -0.0119 -0.0130 0.0329  87  PHE A CE1 
664  C CE2 . PHE A 86  ? 0.2226 0.2651 0.2626 -0.0098 -0.0078 0.0439  87  PHE A CE2 
665  C CZ  . PHE A 86  ? 0.2295 0.2743 0.2671 -0.0108 -0.0106 0.0389  87  PHE A CZ  
666  N N   . ASP A 87  ? 0.2241 0.2135 0.2638 -0.0110 -0.0101 0.0223  88  ASP A N   
667  C CA  . ASP A 87  ? 0.2453 0.2260 0.2838 -0.0076 -0.0089 0.0183  88  ASP A CA  
668  C C   . ASP A 87  ? 0.2267 0.2045 0.2594 -0.0087 -0.0105 0.0087  88  ASP A C   
669  O O   . ASP A 87  ? 0.2680 0.2396 0.2988 -0.0055 -0.0091 0.0043  88  ASP A O   
670  C CB  . ASP A 87  ? 0.2954 0.2644 0.3422 -0.0083 -0.0076 0.0207  88  ASP A CB  
671  C CG  . ASP A 87  ? 0.3783 0.3493 0.4296 -0.0057 -0.0052 0.0311  88  ASP A CG  
672  O OD1 . ASP A 87  ? 0.3856 0.3644 0.4327 -0.0007 -0.0042 0.0345  88  ASP A OD1 
673  O OD2 . ASP A 87  ? 0.5101 0.4752 0.5692 -0.0088 -0.0045 0.0360  88  ASP A OD2 
674  N N   . ASP A 88  ? 0.2055 0.1878 0.2351 -0.0128 -0.0135 0.0054  89  ASP A N   
675  C CA  . ASP A 88  ? 0.2249 0.2058 0.2470 -0.0136 -0.0152 -0.0032 89  ASP A CA  
676  C C   . ASP A 88  ? 0.2357 0.2220 0.2498 -0.0090 -0.0132 -0.0040 89  ASP A C   
677  O O   . ASP A 88  ? 0.2026 0.1952 0.2168 -0.0065 -0.0117 0.0015  89  ASP A O   
678  C CB  . ASP A 88  ? 0.2419 0.2284 0.2623 -0.0184 -0.0193 -0.0055 89  ASP A CB  
679  C CG  . ASP A 88  ? 0.2498 0.2321 0.2789 -0.0239 -0.0218 -0.0061 89  ASP A CG  
680  O OD1 . ASP A 88  ? 0.2860 0.2581 0.3212 -0.0246 -0.0205 -0.0070 89  ASP A OD1 
681  O OD2 . ASP A 88  ? 0.2830 0.2725 0.3137 -0.0277 -0.0250 -0.0055 89  ASP A OD2 
682  N N   . THR A 89  ? 0.2620 0.2462 0.2691 -0.0084 -0.0132 -0.0112 90  THR A N   
683  C CA  . THR A 89  ? 0.2449 0.2348 0.2445 -0.0051 -0.0110 -0.0119 90  THR A CA  
684  C C   . THR A 89  ? 0.2347 0.2296 0.2258 -0.0075 -0.0135 -0.0147 90  THR A C   
685  O O   . THR A 89  ? 0.2383 0.2318 0.2287 -0.0112 -0.0171 -0.0178 90  THR A O   
686  C CB  . THR A 89  ? 0.2886 0.2733 0.2869 -0.0012 -0.0077 -0.0169 90  THR A CB  
687  O OG1 . THR A 89  ? 0.2852 0.2626 0.2807 -0.0030 -0.0091 -0.0248 90  THR A OG1 
688  C CG2 . THR A 89  ? 0.2911 0.2717 0.2983 0.0023  -0.0055 -0.0127 90  THR A CG2 
689  N N   . PRO A 90  ? 0.2237 0.2250 0.2089 -0.0058 -0.0120 -0.0129 91  PRO A N   
690  C CA  . PRO A 90  ? 0.2345 0.2408 0.2125 -0.0078 -0.0146 -0.0129 91  PRO A CA  
691  C C   . PRO A 90  ? 0.2185 0.2228 0.1882 -0.0090 -0.0163 -0.0198 91  PRO A C   
692  O O   . PRO A 90  ? 0.2316 0.2392 0.1971 -0.0114 -0.0202 -0.0202 91  PRO A O   
693  C CB  . PRO A 90  ? 0.2323 0.2440 0.2069 -0.0056 -0.0117 -0.0092 91  PRO A CB  
694  C CG  . PRO A 90  ? 0.2621 0.2721 0.2397 -0.0024 -0.0074 -0.0102 91  PRO A CG  
695  C CD  . PRO A 90  ? 0.2311 0.2359 0.2172 -0.0022 -0.0082 -0.0099 91  PRO A CD  
696  N N   . GLY A 91  ? 0.2334 0.2329 0.2006 -0.0071 -0.0136 -0.0256 92  GLY A N   
697  C CA  . GLY A 91  ? 0.2856 0.2833 0.2436 -0.0078 -0.0149 -0.0334 92  GLY A CA  
698  C C   . GLY A 91  ? 0.2707 0.2642 0.2311 -0.0118 -0.0201 -0.0382 92  GLY A C   
699  O O   . GLY A 91  ? 0.2864 0.2802 0.2384 -0.0131 -0.0227 -0.0449 92  GLY A O   
700  N N   . LYS A 92  ? 0.2497 0.2400 0.2216 -0.0140 -0.0217 -0.0351 93  LYS A N   
701  C CA  . LYS A 92  ? 0.3028 0.2907 0.2791 -0.0189 -0.0268 -0.0386 93  LYS A CA  
702  C C   . LYS A 92  ? 0.2535 0.2506 0.2254 -0.0216 -0.0318 -0.0370 93  LYS A C   
703  O O   . LYS A 92  ? 0.2962 0.2937 0.2678 -0.0254 -0.0369 -0.0422 93  LYS A O   
704  C CB  . LYS A 92  ? 0.2839 0.2676 0.2740 -0.0208 -0.0265 -0.0336 93  LYS A CB  
705  C CG  . LYS A 92  ? 0.3019 0.2825 0.2995 -0.0266 -0.0311 -0.0369 93  LYS A CG  
706  C CD  . LYS A 92  ? 0.3078 0.2849 0.3189 -0.0282 -0.0296 -0.0301 93  LYS A CD  
707  C CE  . LYS A 92  ? 0.3601 0.3350 0.3806 -0.0350 -0.0338 -0.0324 93  LYS A CE  
708  N NZ  . LYS A 92  ? 0.5091 0.4710 0.5319 -0.0367 -0.0340 -0.0408 93  LYS A NZ  
709  N N   . TYR A 93  ? 0.2624 0.2668 0.2314 -0.0194 -0.0306 -0.0300 94  TYR A N   
710  C CA  . TYR A 93  ? 0.2329 0.2459 0.1991 -0.0207 -0.0349 -0.0268 94  TYR A CA  
711  C C   . TYR A 93  ? 0.2643 0.2817 0.2172 -0.0180 -0.0343 -0.0264 94  TYR A C   
712  O O   . TYR A 93  ? 0.2850 0.3072 0.2309 -0.0191 -0.0388 -0.0284 94  TYR A O   
713  C CB  . TYR A 93  ? 0.2367 0.2538 0.2122 -0.0205 -0.0343 -0.0183 94  TYR A CB  
714  C CG  . TYR A 93  ? 0.2224 0.2359 0.2105 -0.0233 -0.0345 -0.0176 94  TYR A CG  
715  C CD1 . TYR A 93  ? 0.2521 0.2683 0.2467 -0.0279 -0.0393 -0.0193 94  TYR A CD1 
716  C CD2 . TYR A 93  ? 0.2245 0.2325 0.2183 -0.0216 -0.0300 -0.0151 94  TYR A CD2 
717  C CE1 . TYR A 93  ? 0.2436 0.2564 0.2505 -0.0311 -0.0390 -0.0180 94  TYR A CE1 
718  C CE2 . TYR A 93  ? 0.2587 0.2629 0.2635 -0.0241 -0.0298 -0.0134 94  TYR A CE2 
719  C CZ  . TYR A 93  ? 0.2799 0.2863 0.2914 -0.0292 -0.0341 -0.0147 94  TYR A CZ  
720  O OH  . TYR A 93  ? 0.2683 0.2709 0.2915 -0.0323 -0.0334 -0.0123 94  TYR A OH  
721  N N   . TRP A 94  ? 0.2930 0.3094 0.2425 -0.0146 -0.0288 -0.0235 95  TRP A N   
722  C CA  . TRP A 94  ? 0.2419 0.2616 0.1792 -0.0123 -0.0268 -0.0227 95  TRP A CA  
723  C C   . TRP A 94  ? 0.2695 0.2853 0.1997 -0.0111 -0.0238 -0.0303 95  TRP A C   
724  O O   . TRP A 94  ? 0.2698 0.2827 0.2021 -0.0088 -0.0184 -0.0306 95  TRP A O   
725  C CB  . TRP A 94  ? 0.2505 0.2718 0.1899 -0.0101 -0.0224 -0.0154 95  TRP A CB  
726  C CG  . TRP A 94  ? 0.2568 0.2823 0.1864 -0.0088 -0.0216 -0.0113 95  TRP A CG  
727  C CD1 . TRP A 94  ? 0.2748 0.3034 0.1925 -0.0088 -0.0240 -0.0129 95  TRP A CD1 
728  C CD2 . TRP A 94  ? 0.2636 0.2904 0.1943 -0.0075 -0.0183 -0.0045 95  TRP A CD2 
729  N NE1 . TRP A 94  ? 0.3243 0.3556 0.2357 -0.0073 -0.0219 -0.0065 95  TRP A NE1 
730  C CE2 . TRP A 94  ? 0.2944 0.3241 0.2143 -0.0067 -0.0184 -0.0015 95  TRP A CE2 
731  C CE3 . TRP A 94  ? 0.2405 0.2663 0.1801 -0.0069 -0.0154 -0.0008 95  TRP A CE3 
732  C CZ2 . TRP A 94  ? 0.3096 0.3398 0.2286 -0.0058 -0.0154 0.0053  95  TRP A CZ2 
733  C CZ3 . TRP A 94  ? 0.2652 0.2922 0.2038 -0.0062 -0.0129 0.0048  95  TRP A CZ3 
734  C CH2 . TRP A 94  ? 0.2547 0.2831 0.1835 -0.0058 -0.0127 0.0078  95  TRP A CH2 
735  N N   . LYS A 95  ? 0.3204 0.3369 0.2422 -0.0124 -0.0276 -0.0370 96  LYS A N   
736  C CA  . LYS A 95  ? 0.3291 0.3407 0.2455 -0.0115 -0.0256 -0.0464 96  LYS A CA  
737  C C   . LYS A 95  ? 0.2699 0.2832 0.1776 -0.0076 -0.0188 -0.0463 96  LYS A C   
738  O O   . LYS A 95  ? 0.2882 0.2968 0.1953 -0.0055 -0.0149 -0.0527 96  LYS A O   
739  C CB  . LYS A 95  ? 0.3346 0.3480 0.2424 -0.0139 -0.0317 -0.0541 96  LYS A CB  
740  C CG  . LYS A 95  ? 0.4184 0.4322 0.3362 -0.0184 -0.0386 -0.0542 96  LYS A CG  
741  C CD  . LYS A 95  ? 0.4459 0.4507 0.3782 -0.0202 -0.0374 -0.0562 96  LYS A CD  
742  C CE  . LYS A 95  ? 0.4714 0.4772 0.4141 -0.0255 -0.0439 -0.0566 96  LYS A CE  
743  N NZ  . LYS A 95  ? 0.6063 0.6127 0.5433 -0.0288 -0.0500 -0.0667 96  LYS A NZ  
744  N N   . GLU A 96  ? 0.2659 0.2854 0.1676 -0.0065 -0.0170 -0.0389 97  GLU A N   
745  C CA  . GLU A 96  ? 0.2934 0.3155 0.1882 -0.0035 -0.0100 -0.0376 97  GLU A CA  
746  C C   . GLU A 96  ? 0.2804 0.3000 0.1865 -0.0018 -0.0043 -0.0353 97  GLU A C   
747  O O   . GLU A 96  ? 0.2976 0.3197 0.2005 0.0007  0.0019  -0.0356 97  GLU A O   
748  C CB  . GLU A 96  ? 0.3155 0.3440 0.2024 -0.0035 -0.0097 -0.0292 97  GLU A CB  
749  C CG  . GLU A 96  ? 0.3441 0.3768 0.2165 -0.0039 -0.0143 -0.0312 97  GLU A CG  
750  C CD  . GLU A 96  ? 0.4394 0.4740 0.3151 -0.0060 -0.0222 -0.0275 97  GLU A CD  
751  O OE1 . GLU A 96  ? 0.3754 0.4069 0.2645 -0.0078 -0.0249 -0.0272 97  GLU A OE1 
752  O OE2 . GLU A 96  ? 0.4793 0.5194 0.3441 -0.0056 -0.0256 -0.0247 97  GLU A OE2 
753  N N   . LEU A 97  ? 0.2777 0.2936 0.1968 -0.0028 -0.0063 -0.0331 98  LEU A N   
754  C CA  . LEU A 97  ? 0.2484 0.2625 0.1780 -0.0008 -0.0019 -0.0314 98  LEU A CA  
755  C C   . LEU A 97  ? 0.2638 0.2709 0.1987 0.0008  -0.0012 -0.0385 98  LEU A C   
756  O O   . LEU A 97  ? 0.2677 0.2734 0.2110 0.0034  0.0024  -0.0374 98  LEU A O   
757  C CB  . LEU A 97  ? 0.2184 0.2331 0.1582 -0.0021 -0.0038 -0.0240 98  LEU A CB  
758  C CG  . LEU A 97  ? 0.2163 0.2362 0.1530 -0.0032 -0.0042 -0.0168 98  LEU A CG  
759  C CD1 . LEU A 97  ? 0.2015 0.2215 0.1486 -0.0039 -0.0058 -0.0113 98  LEU A CD1 
760  C CD2 . LEU A 97  ? 0.2228 0.2467 0.1554 -0.0017 0.0016  -0.0150 98  LEU A CD2 
761  N N   . LYS A 98  ? 0.2820 0.2846 0.2125 -0.0006 -0.0047 -0.0458 99  LYS A N   
762  C CA  . LYS A 98  ? 0.3206 0.3146 0.2562 0.0009  -0.0038 -0.0532 99  LYS A CA  
763  C C   . LYS A 98  ? 0.2884 0.2832 0.2208 0.0059  0.0029  -0.0572 99  LYS A C   
764  O O   . LYS A 98  ? 0.3430 0.3441 0.2644 0.0071  0.0058  -0.0585 99  LYS A O   
765  C CB  . LYS A 98  ? 0.3434 0.3326 0.2738 -0.0021 -0.0091 -0.0616 99  LYS A CB  
766  C CG  . LYS A 98  ? 0.4319 0.4100 0.3728 -0.0033 -0.0110 -0.0665 99  LYS A CG  
767  C CD  . LYS A 98  ? 0.4972 0.4718 0.4340 -0.0077 -0.0172 -0.0748 99  LYS A CD  
768  C CE  . LYS A 98  ? 0.4727 0.4517 0.4141 -0.0131 -0.0236 -0.0692 99  LYS A CE  
769  N NZ  . LYS A 98  ? 0.4501 0.4231 0.4072 -0.0154 -0.0244 -0.0646 99  LYS A NZ  
770  N N   . ASN A 99  ? 0.3769 0.3661 0.3194 0.0090  0.0057  -0.0585 100 ASN A N   
771  C CA  . ASN A 99  ? 0.3873 0.3776 0.3293 0.0146  0.0122  -0.0625 100 ASN A CA  
772  C C   . ASN A 99  ? 0.3603 0.3618 0.3018 0.0161  0.0169  -0.0557 100 ASN A C   
773  O O   . ASN A 99  ? 0.3870 0.3937 0.3238 0.0194  0.0226  -0.0587 100 ASN A O   
774  C CB  . ASN A 99  ? 0.4963 0.4844 0.4265 0.0160  0.0135  -0.0734 100 ASN A CB  
775  C CG  . ASN A 99  ? 0.5927 0.5695 0.5235 0.0136  0.0084  -0.0814 100 ASN A CG  
776  O OD1 . ASN A 99  ? 0.5996 0.5672 0.5421 0.0137  0.0071  -0.0812 100 ASN A OD1 
777  N ND2 . ASN A 99  ? 0.6255 0.6033 0.5437 0.0111  0.0052  -0.0882 100 ASN A ND2 
778  N N   . THR A 100 ? 0.2870 0.2926 0.2335 0.0134  0.0149  -0.0467 101 THR A N   
779  C CA  . THR A 100 ? 0.2774 0.2923 0.2273 0.0144  0.0190  -0.0404 101 THR A CA  
780  C C   . THR A 100 ? 0.2452 0.2597 0.2089 0.0158  0.0184  -0.0354 101 THR A C   
781  O O   . THR A 100 ? 0.2384 0.2458 0.2076 0.0151  0.0145  -0.0349 101 THR A O   
782  C CB  . THR A 100 ? 0.2811 0.3016 0.2245 0.0104  0.0173  -0.0344 101 THR A CB  
783  O OG1 . THR A 100 ? 0.2497 0.2674 0.1982 0.0074  0.0119  -0.0296 101 THR A OG1 
784  C CG2 . THR A 100 ? 0.2695 0.2903 0.1982 0.0091  0.0166  -0.0384 101 THR A CG2 
785  N N   . PRO A 101 ? 0.2279 0.2504 0.1975 0.0176  0.0221  -0.0316 102 PRO A N   
786  C CA  . PRO A 101 ? 0.2120 0.2353 0.1937 0.0195  0.0210  -0.0272 102 PRO A CA  
787  C C   . PRO A 101 ? 0.2215 0.2427 0.2056 0.0158  0.0158  -0.0215 102 PRO A C   
788  O O   . PRO A 101 ? 0.2081 0.2261 0.1999 0.0173  0.0137  -0.0192 102 PRO A O   
789  C CB  . PRO A 101 ? 0.2096 0.2443 0.1960 0.0208  0.0255  -0.0244 102 PRO A CB  
790  C CG  . PRO A 101 ? 0.2331 0.2706 0.2121 0.0224  0.0308  -0.0297 102 PRO A CG  
791  C CD  . PRO A 101 ? 0.2441 0.2757 0.2104 0.0189  0.0280  -0.0320 102 PRO A CD  
792  N N   . ILE A 102 ? 0.2025 0.2255 0.1802 0.0115  0.0137  -0.0190 103 ILE A N   
793  C CA  . ILE A 102 ? 0.1983 0.2201 0.1790 0.0088  0.0092  -0.0140 103 ILE A CA  
794  C C   . ILE A 102 ? 0.2116 0.2250 0.1930 0.0079  0.0055  -0.0158 103 ILE A C   
795  O O   . ILE A 102 ? 0.2115 0.2240 0.1977 0.0067  0.0025  -0.0116 103 ILE A O   
796  C CB  . ILE A 102 ? 0.2036 0.2289 0.1780 0.0052  0.0081  -0.0108 103 ILE A CB  
797  C CG1 . ILE A 102 ? 0.2039 0.2297 0.1827 0.0033  0.0045  -0.0058 103 ILE A CG1 
798  C CG2 . ILE A 102 ? 0.2130 0.2348 0.1774 0.0032  0.0063  -0.0138 103 ILE A CG2 
799  C CD1 . ILE A 102 ? 0.2634 0.2942 0.2500 0.0046  0.0055  -0.0027 103 ILE A CD1 
800  N N   . ASP A 103 ? 0.2139 0.2217 0.1910 0.0084  0.0057  -0.0220 104 ASP A N   
801  C CA  . ASP A 103 ? 0.2133 0.2124 0.1928 0.0070  0.0023  -0.0243 104 ASP A CA  
802  C C   . ASP A 103 ? 0.2205 0.2147 0.2102 0.0101  0.0032  -0.0229 104 ASP A C   
803  O O   . ASP A 103 ? 0.2796 0.2653 0.2729 0.0090  0.0011  -0.0245 104 ASP A O   
804  C CB  . ASP A 103 ? 0.2493 0.2436 0.2210 0.0063  0.0020  -0.0326 104 ASP A CB  
805  C CG  . ASP A 103 ? 0.2754 0.2633 0.2476 0.0023  -0.0031 -0.0350 104 ASP A CG  
806  O OD1 . ASP A 103 ? 0.2744 0.2641 0.2504 -0.0008 -0.0064 -0.0295 104 ASP A OD1 
807  O OD2 . ASP A 103 ? 0.3249 0.3062 0.2944 0.0022  -0.0036 -0.0428 104 ASP A OD2 
808  N N   . GLN A 104 ? 0.2146 0.2139 0.2094 0.0139  0.0061  -0.0197 105 GLN A N   
809  C CA  A GLN A 104 ? 0.2046 0.2007 0.2089 0.0174  0.0065  -0.0164 105 GLN A CA  
810  C CA  B GLN A 104 ? 0.2041 0.2002 0.2084 0.0174  0.0064  -0.0163 105 GLN A CA  
811  C C   . GLN A 104 ? 0.2376 0.2384 0.2463 0.0162  0.0041  -0.0085 105 GLN A C   
812  O O   . GLN A 104 ? 0.2524 0.2515 0.2681 0.0190  0.0040  -0.0043 105 GLN A O   
813  C CB  A GLN A 104 ? 0.2317 0.2320 0.2397 0.0232  0.0106  -0.0177 105 GLN A CB  
814  C CB  B GLN A 104 ? 0.2315 0.2319 0.2397 0.0232  0.0106  -0.0176 105 GLN A CB  
815  C CG  A GLN A 104 ? 0.2455 0.2418 0.2491 0.0253  0.0137  -0.0261 105 GLN A CG  
816  C CG  B GLN A 104 ? 0.2481 0.2423 0.2540 0.0261  0.0135  -0.0255 105 GLN A CG  
817  C CD  A GLN A 104 ? 0.2548 0.2591 0.2611 0.0304  0.0186  -0.0275 105 GLN A CD  
818  C CD  B GLN A 104 ? 0.2607 0.2627 0.2694 0.0315  0.0183  -0.0271 105 GLN A CD  
819  O OE1 A GLN A 104 ? 0.2378 0.2532 0.2445 0.0297  0.0198  -0.0240 105 GLN A OE1 
820  O OE1 B GLN A 104 ? 0.2570 0.2653 0.2737 0.0349  0.0189  -0.0223 105 GLN A OE1 
821  N NE2 A GLN A 104 ? 0.2769 0.2759 0.2860 0.0357  0.0215  -0.0327 105 GLN A NE2 
822  N NE2 B GLN A 104 ? 0.2577 0.2606 0.2597 0.0323  0.0216  -0.0339 105 GLN A NE2 
823  N N   . VAL A 105 ? 0.1850 0.1914 0.1893 0.0124  0.0024  -0.0063 106 VAL A N   
824  C CA  . VAL A 105 ? 0.1904 0.2014 0.1974 0.0112  0.0002  0.0000  106 VAL A CA  
825  C C   . VAL A 105 ? 0.2158 0.2222 0.2223 0.0073  -0.0028 0.0011  106 VAL A C   
826  O O   . VAL A 105 ? 0.2106 0.2149 0.2119 0.0042  -0.0041 -0.0026 106 VAL A O   
827  C CB  . VAL A 105 ? 0.2040 0.2237 0.2076 0.0099  0.0005  0.0012  106 VAL A CB  
828  C CG1 . VAL A 105 ? 0.1800 0.2044 0.1862 0.0092  -0.0016 0.0066  106 VAL A CG1 
829  C CG2 . VAL A 105 ? 0.1832 0.2085 0.1884 0.0128  0.0037  -0.0004 106 VAL A CG2 
830  N N   . ASN A 106 ? 0.1949 0.2006 0.2069 0.0074  -0.0039 0.0063  107 ASN A N   
831  C CA  . ASN A 106 ? 0.2028 0.2054 0.2160 0.0033  -0.0062 0.0077  107 ASN A CA  
832  C C   . ASN A 106 ? 0.1766 0.1869 0.1875 0.0013  -0.0078 0.0109  107 ASN A C   
833  O O   . ASN A 106 ? 0.1791 0.1958 0.1877 0.0029  -0.0071 0.0121  107 ASN A O   
834  C CB  . ASN A 106 ? 0.1807 0.1774 0.2013 0.0040  -0.0059 0.0118  107 ASN A CB  
835  C CG  . ASN A 106 ? 0.1845 0.1871 0.2082 0.0065  -0.0053 0.0194  107 ASN A CG  
836  O OD1 . ASN A 106 ? 0.1836 0.1945 0.2048 0.0061  -0.0059 0.0217  107 ASN A OD1 
837  N ND2 . ASN A 106 ? 0.2029 0.2008 0.2319 0.0095  -0.0040 0.0233  107 ASN A ND2 
838  N N   . LEU A 107 ? 0.1832 0.1929 0.1954 -0.0023 -0.0100 0.0116  108 LEU A N   
839  C CA  . LEU A 107 ? 0.1765 0.1931 0.1866 -0.0038 -0.0115 0.0136  108 LEU A CA  
840  C C   . LEU A 107 ? 0.1568 0.1794 0.1693 -0.0017 -0.0105 0.0190  108 LEU A C   
841  O O   . LEU A 107 ? 0.1612 0.1893 0.1706 -0.0010 -0.0107 0.0195  108 LEU A O   
842  C CB  . LEU A 107 ? 0.1770 0.1930 0.1895 -0.0079 -0.0142 0.0131  108 LEU A CB  
843  C CG  . LEU A 107 ? 0.1931 0.2041 0.2024 -0.0104 -0.0162 0.0069  108 LEU A CG  
844  C CD1 . LEU A 107 ? 0.2177 0.2312 0.2301 -0.0145 -0.0197 0.0068  108 LEU A CD1 
845  C CD2 . LEU A 107 ? 0.2322 0.2449 0.2326 -0.0089 -0.0159 0.0035  108 LEU A CD2 
846  N N   . LEU A 108 ? 0.1660 0.1872 0.1834 -0.0005 -0.0093 0.0231  109 LEU A N   
847  C CA  . LEU A 108 ? 0.1669 0.1949 0.1851 0.0021  -0.0083 0.0282  109 LEU A CA  
848  C C   . LEU A 108 ? 0.1812 0.2131 0.1960 0.0054  -0.0077 0.0266  109 LEU A C   
849  O O   . LEU A 108 ? 0.1535 0.1922 0.1662 0.0065  -0.0080 0.0275  109 LEU A O   
850  C CB  . LEU A 108 ? 0.1529 0.1784 0.1763 0.0031  -0.0070 0.0337  109 LEU A CB  
851  C CG  . LEU A 108 ? 0.1801 0.2137 0.2031 0.0057  -0.0060 0.0395  109 LEU A CG  
852  C CD1 . LEU A 108 ? 0.2021 0.2422 0.2241 0.0038  -0.0065 0.0399  109 LEU A CD1 
853  C CD2 . LEU A 108 ? 0.2887 0.3196 0.3164 0.0068  -0.0044 0.0464  109 LEU A CD2 
854  N N   . GLN A 109 ? 0.1946 0.2228 0.2095 0.0069  -0.0069 0.0238  110 GLN A N   
855  C CA  . GLN A 109 ? 0.1763 0.2093 0.1896 0.0094  -0.0063 0.0221  110 GLN A CA  
856  C C   . GLN A 109 ? 0.1403 0.1763 0.1492 0.0074  -0.0067 0.0188  110 GLN A C   
857  O O   . GLN A 109 ? 0.1600 0.2018 0.1682 0.0083  -0.0068 0.0186  110 GLN A O   
858  C CB  . GLN A 109 ? 0.1652 0.1941 0.1804 0.0117  -0.0048 0.0197  110 GLN A CB  
859  C CG  . GLN A 109 ? 0.1709 0.1973 0.1912 0.0151  -0.0043 0.0241  110 GLN A CG  
860  C CD  . GLN A 109 ? 0.2037 0.2229 0.2269 0.0174  -0.0027 0.0214  110 GLN A CD  
861  O OE1 . GLN A 109 ? 0.1799 0.1948 0.2007 0.0158  -0.0020 0.0158  110 GLN A OE1 
862  N NE2 . GLN A 109 ? 0.2181 0.2360 0.2460 0.0218  -0.0021 0.0255  110 GLN A NE2 
863  N N   . LEU A 110 ? 0.1483 0.1801 0.1543 0.0045  -0.0073 0.0163  111 LEU A N   
864  C CA  . LEU A 110 ? 0.1393 0.1731 0.1411 0.0028  -0.0078 0.0146  111 LEU A CA  
865  C C   . LEU A 110 ? 0.1566 0.1945 0.1586 0.0027  -0.0090 0.0170  111 LEU A C   
866  O O   . LEU A 110 ? 0.1506 0.1915 0.1512 0.0029  -0.0089 0.0164  111 LEU A O   
867  C CB  . LEU A 110 ? 0.1447 0.1741 0.1427 0.0004  -0.0086 0.0121  111 LEU A CB  
868  C CG  . LEU A 110 ? 0.1602 0.1861 0.1560 0.0008  -0.0069 0.0083  111 LEU A CG  
869  C CD1 . LEU A 110 ? 0.2095 0.2313 0.2009 -0.0014 -0.0084 0.0054  111 LEU A CD1 
870  C CD2 . LEU A 110 ? 0.1710 0.2004 0.1648 0.0016  -0.0046 0.0073  111 LEU A CD2 
871  N N   . ALA A 111 ? 0.1492 0.1874 0.1536 0.0023  -0.0098 0.0197  112 ALA A N   
872  C CA  . ALA A 111 ? 0.1732 0.2160 0.1779 0.0027  -0.0105 0.0217  112 ALA A CA  
873  C C   . ALA A 111 ? 0.1625 0.2107 0.1674 0.0053  -0.0097 0.0227  112 ALA A C   
874  O O   . ALA A 111 ? 0.1829 0.2347 0.1865 0.0060  -0.0101 0.0222  112 ALA A O   
875  C CB  . ALA A 111 ? 0.1791 0.2226 0.1876 0.0016  -0.0109 0.0247  112 ALA A CB  
876  N N   . THR A 112 ? 0.1464 0.1954 0.1528 0.0071  -0.0090 0.0238  113 THR A N   
877  C CA  . THR A 112 ? 0.1485 0.2041 0.1547 0.0098  -0.0091 0.0248  113 THR A CA  
878  C C   . THR A 112 ? 0.1546 0.2121 0.1610 0.0106  -0.0092 0.0219  113 THR A C   
879  O O   . THR A 112 ? 0.1708 0.2342 0.1780 0.0131  -0.0098 0.0227  113 THR A O   
880  C CB  . THR A 112 ? 0.1510 0.2085 0.1592 0.0120  -0.0085 0.0300  113 THR A CB  
881  O OG1 . THR A 112 ? 0.1523 0.2044 0.1634 0.0123  -0.0079 0.0311  113 THR A OG1 
882  C CG2 . THR A 112 ? 0.1876 0.2453 0.1966 0.0107  -0.0078 0.0333  113 THR A CG2 
883  N N   . TYR A 113 ? 0.1520 0.2057 0.1578 0.0085  -0.0087 0.0186  114 TYR A N   
884  C CA  . TYR A 113 ? 0.1440 0.2006 0.1507 0.0081  -0.0084 0.0156  114 TYR A CA  
885  C C   . TYR A 113 ? 0.1442 0.2041 0.1545 0.0106  -0.0079 0.0159  114 TYR A C   
886  O O   . TYR A 113 ? 0.1345 0.2007 0.1473 0.0110  -0.0083 0.0142  114 TYR A O   
887  C CB  . TYR A 113 ? 0.1556 0.2173 0.1617 0.0079  -0.0097 0.0138  114 TYR A CB  
888  C CG  . TYR A 113 ? 0.1442 0.2041 0.1475 0.0073  -0.0103 0.0140  114 TYR A CG  
889  C CD1 . TYR A 113 ? 0.1630 0.2171 0.1644 0.0051  -0.0099 0.0133  114 TYR A CD1 
890  C CD2 . TYR A 113 ? 0.1597 0.2244 0.1618 0.0096  -0.0111 0.0151  114 TYR A CD2 
891  C CE1 . TYR A 113 ? 0.1725 0.2256 0.1724 0.0055  -0.0105 0.0136  114 TYR A CE1 
892  C CE2 . TYR A 113 ? 0.1776 0.2417 0.1779 0.0097  -0.0112 0.0150  114 TYR A CE2 
893  C CZ  . TYR A 113 ? 0.1763 0.2345 0.1760 0.0078  -0.0109 0.0142  114 TYR A CZ  
894  O OH  . TYR A 113 ? 0.2149 0.2731 0.2137 0.0087  -0.0110 0.0143  114 TYR A OH  
895  N N   . THR A 114 ? 0.1626 0.2184 0.1744 0.0122  -0.0070 0.0178  115 THR A N   
896  C CA  . THR A 114 ? 0.1517 0.2104 0.1677 0.0156  -0.0064 0.0185  115 THR A CA  
897  C C   . THR A 114 ? 0.1598 0.2141 0.1772 0.0157  -0.0041 0.0158  115 THR A C   
898  O O   . THR A 114 ? 0.1769 0.2310 0.1982 0.0193  -0.0033 0.0167  115 THR A O   
899  C CB  . THR A 114 ? 0.1649 0.2231 0.1826 0.0189  -0.0071 0.0235  115 THR A CB  
900  O OG1 . THR A 114 ? 0.1781 0.2272 0.1951 0.0175  -0.0063 0.0249  115 THR A OG1 
901  C CG2 . THR A 114 ? 0.1530 0.2182 0.1687 0.0199  -0.0089 0.0262  115 THR A CG2 
902  N N   . SER A 115 ? 0.1592 0.2105 0.1733 0.0124  -0.0029 0.0126  116 SER A N   
903  C CA  . SER A 115 ? 0.1561 0.2042 0.1701 0.0129  -0.0002 0.0096  116 SER A CA  
904  C C   . SER A 115 ? 0.1571 0.2126 0.1767 0.0155  0.0015  0.0085  116 SER A C   
905  O O   . SER A 115 ? 0.1528 0.2066 0.1740 0.0178  0.0040  0.0065  116 SER A O   
906  C CB  . SER A 115 ? 0.1589 0.2043 0.1673 0.0091  0.0009  0.0072  116 SER A CB  
907  O OG  . SER A 115 ? 0.1619 0.2132 0.1711 0.0072  0.0016  0.0068  116 SER A OG  
908  N N   . GLY A 116 ? 0.1496 0.2138 0.1725 0.0153  0.0002  0.0092  117 GLY A N   
909  C CA  . GLY A 116 ? 0.1437 0.2170 0.1733 0.0174  0.0014  0.0080  117 GLY A CA  
910  C C   . GLY A 116 ? 0.1477 0.2248 0.1781 0.0139  0.0042  0.0052  117 GLY A C   
911  O O   . GLY A 116 ? 0.1318 0.2182 0.1692 0.0149  0.0054  0.0042  117 GLY A O   
912  N N   . ASN A 117 ? 0.1336 0.2046 0.1576 0.0098  0.0053  0.0045  118 ASN A N   
913  C CA  . ASN A 117 ? 0.1517 0.2263 0.1764 0.0062  0.0083  0.0032  118 ASN A CA  
914  C C   . ASN A 117 ? 0.1722 0.2396 0.1895 0.0020  0.0081  0.0039  118 ASN A C   
915  O O   . ASN A 117 ? 0.1553 0.2200 0.1681 0.0001  0.0111  0.0037  118 ASN A O   
916  C CB  . ASN A 117 ? 0.1577 0.2339 0.1832 0.0079  0.0130  0.0013  118 ASN A CB  
917  C CG  . ASN A 117 ? 0.1484 0.2311 0.1767 0.0043  0.0168  0.0009  118 ASN A CG  
918  O OD1 . ASN A 117 ? 0.1972 0.2857 0.2310 0.0012  0.0156  0.0014  118 ASN A OD1 
919  N ND2 . ASN A 117 ? 0.1776 0.2595 0.2021 0.0045  0.0215  -0.0003 118 ASN A ND2 
920  N N   . LEU A 118 ? 0.1660 0.2312 0.1819 0.0009  0.0045  0.0051  119 LEU A N   
921  C CA  . LEU A 118 ? 0.1360 0.1953 0.1466 -0.0025 0.0041  0.0060  119 LEU A CA  
922  C C   . LEU A 118 ? 0.1506 0.2126 0.1648 -0.0044 0.0018  0.0056  119 LEU A C   
923  O O   . LEU A 118 ? 0.1414 0.2061 0.1573 -0.0024 -0.0011 0.0053  119 LEU A O   
924  C CB  . LEU A 118 ? 0.1436 0.1954 0.1476 -0.0015 0.0022  0.0072  119 LEU A CB  
925  C CG  . LEU A 118 ? 0.1347 0.1823 0.1336 -0.0008 0.0041  0.0066  119 LEU A CG  
926  C CD1 . LEU A 118 ? 0.1625 0.2043 0.1571 -0.0002 0.0014  0.0072  119 LEU A CD1 
927  C CD2 . LEU A 118 ? 0.1548 0.2013 0.1491 -0.0033 0.0071  0.0069  119 LEU A CD2 
928  N N   . ALA A 119 ? 0.1640 0.2252 0.1793 -0.0083 0.0033  0.0055  120 ALA A N   
929  C CA  . ALA A 119 ? 0.1840 0.2471 0.2037 -0.0107 0.0014  0.0039  120 ALA A CA  
930  C C   . ALA A 119 ? 0.1613 0.2162 0.1758 -0.0111 -0.0005 0.0046  120 ALA A C   
931  O O   . ALA A 119 ? 0.1652 0.2144 0.1735 -0.0094 -0.0007 0.0068  120 ALA A O   
932  C CB  . ALA A 119 ? 0.1956 0.2615 0.2209 -0.0153 0.0043  0.0034  120 ALA A CB  
933  N N   . LEU A 120 ? 0.1436 0.1981 0.1614 -0.0133 -0.0021 0.0024  121 LEU A N   
934  C CA  . LEU A 120 ? 0.1635 0.2107 0.1776 -0.0128 -0.0038 0.0024  121 LEU A CA  
935  C C   . LEU A 120 ? 0.1853 0.2237 0.1944 -0.0136 -0.0019 0.0062  121 LEU A C   
936  O O   . LEU A 120 ? 0.1861 0.2200 0.1905 -0.0112 -0.0032 0.0078  121 LEU A O   
937  C CB  . LEU A 120 ? 0.1696 0.2166 0.1885 -0.0155 -0.0052 -0.0016 121 LEU A CB  
938  C CG  . LEU A 120 ? 0.2694 0.3095 0.2853 -0.0140 -0.0070 -0.0029 121 LEU A CG  
939  C CD1 . LEU A 120 ? 0.2421 0.2865 0.2543 -0.0092 -0.0093 -0.0036 121 LEU A CD1 
940  C CD2 . LEU A 120 ? 0.3009 0.3396 0.3221 -0.0172 -0.0081 -0.0079 121 LEU A CD2 
941  N N   . GLN A 121 ? 0.1951 0.2318 0.2053 -0.0170 0.0013  0.0081  122 GLN A N   
942  C CA  . GLN A 121 ? 0.1883 0.2174 0.1930 -0.0177 0.0032  0.0125  122 GLN A CA  
943  C C   . GLN A 121 ? 0.1739 0.2059 0.1758 -0.0185 0.0067  0.0149  122 GLN A C   
944  O O   . GLN A 121 ? 0.1982 0.2375 0.2046 -0.0194 0.0085  0.0131  122 GLN A O   
945  C CB  . GLN A 121 ? 0.2394 0.2613 0.2470 -0.0213 0.0043  0.0137  122 GLN A CB  
946  C CG  . GLN A 121 ? 0.2245 0.2431 0.2355 -0.0206 0.0011  0.0098  122 GLN A CG  
947  C CD  . GLN A 121 ? 0.2942 0.3067 0.3000 -0.0165 -0.0010 0.0113  122 GLN A CD  
948  O OE1 . GLN A 121 ? 0.2604 0.2724 0.2603 -0.0140 -0.0011 0.0148  122 GLN A OE1 
949  N NE2 . GLN A 121 ? 0.3531 0.3613 0.3615 -0.0157 -0.0028 0.0080  122 GLN A NE2 
950  N N   . PHE A 122 ? 0.2007 0.2275 0.1949 -0.0178 0.0076  0.0189  123 PHE A N   
951  C CA  . PHE A 122 ? 0.2063 0.2352 0.1962 -0.0188 0.0115  0.0213  123 PHE A CA  
952  C C   . PHE A 122 ? 0.2585 0.2890 0.2543 -0.0234 0.0158  0.0227  123 PHE A C   
953  O O   . PHE A 122 ? 0.2356 0.2619 0.2366 -0.0262 0.0154  0.0232  123 PHE A O   
954  C CB  . PHE A 122 ? 0.2219 0.2451 0.2019 -0.0176 0.0113  0.0257  123 PHE A CB  
955  C CG  . PHE A 122 ? 0.2231 0.2467 0.1973 -0.0139 0.0079  0.0242  123 PHE A CG  
956  C CD1 . PHE A 122 ? 0.2127 0.2410 0.1847 -0.0126 0.0087  0.0212  123 PHE A CD1 
957  C CD2 . PHE A 122 ? 0.2228 0.2420 0.1947 -0.0119 0.0039  0.0256  123 PHE A CD2 
958  C CE1 . PHE A 122 ? 0.2156 0.2436 0.1835 -0.0100 0.0053  0.0195  123 PHE A CE1 
959  C CE2 . PHE A 122 ? 0.2630 0.2837 0.2312 -0.0094 0.0007  0.0242  123 PHE A CE2 
960  C CZ  . PHE A 122 ? 0.2522 0.2767 0.2183 -0.0088 0.0013  0.0211  123 PHE A CZ  
961  N N   . PRO A 123 ? 0.2351 0.2714 0.2303 -0.0244 0.0202  0.0234  124 PRO A N   
962  C CA  . PRO A 123 ? 0.2744 0.3122 0.2743 -0.0292 0.0252  0.0265  124 PRO A CA  
963  C C   . PRO A 123 ? 0.2827 0.3106 0.2777 -0.0311 0.0260  0.0326  124 PRO A C   
964  O O   . PRO A 123 ? 0.2650 0.2872 0.2504 -0.0280 0.0239  0.0352  124 PRO A O   
965  C CB  . PRO A 123 ? 0.2821 0.3276 0.2785 -0.0283 0.0301  0.0268  124 PRO A CB  
966  C CG  . PRO A 123 ? 0.2752 0.3241 0.2694 -0.0233 0.0270  0.0219  124 PRO A CG  
967  C CD  . PRO A 123 ? 0.2423 0.2835 0.2321 -0.0210 0.0212  0.0216  124 PRO A CD  
968  N N   . ASP A 124 ? 0.2781 0.3038 0.2805 -0.0363 0.0290  0.0351  125 ASP A N   
969  C CA  . ASP A 124 ? 0.2858 0.3003 0.2850 -0.0381 0.0298  0.0415  125 ASP A CA  
970  C C   . ASP A 124 ? 0.3251 0.3381 0.3118 -0.0363 0.0329  0.0483  125 ASP A C   
971  O O   . ASP A 124 ? 0.3274 0.3313 0.3074 -0.0347 0.0314  0.0536  125 ASP A O   
972  C CB  . ASP A 124 ? 0.3479 0.3602 0.3583 -0.0449 0.0332  0.0431  125 ASP A CB  
973  C CG  . ASP A 124 ? 0.4493 0.4598 0.4703 -0.0465 0.0289  0.0365  125 ASP A CG  
974  O OD1 . ASP A 124 ? 0.4607 0.4692 0.4787 -0.0420 0.0236  0.0323  125 ASP A OD1 
975  O OD2 . ASP A 124 ? 0.4695 0.4812 0.5019 -0.0525 0.0308  0.0352  125 ASP A OD2 
976  N N   . GLU A 125 ? 0.3000 0.3222 0.2830 -0.0361 0.0370  0.0482  126 GLU A N   
977  C CA  . GLU A 125 ? 0.3164 0.3382 0.2863 -0.0346 0.0402  0.0545  126 GLU A CA  
978  C C   . GLU A 125 ? 0.2830 0.3038 0.2409 -0.0287 0.0353  0.0527  126 GLU A C   
979  O O   . GLU A 125 ? 0.3229 0.3432 0.2685 -0.0270 0.0367  0.0574  126 GLU A O   
980  C CB  . GLU A 125 ? 0.3301 0.3625 0.2999 -0.0363 0.0472  0.0548  126 GLU A CB  
981  C CG  . GLU A 125 ? 0.3859 0.4277 0.3558 -0.0327 0.0464  0.0469  126 GLU A CG  
982  C CD  . GLU A 125 ? 0.4210 0.4693 0.4062 -0.0345 0.0459  0.0410  126 GLU A CD  
983  O OE1 . GLU A 125 ? 0.5332 0.5895 0.5198 -0.0315 0.0460  0.0354  126 GLU A OE1 
984  O OE2 . GLU A 125 ? 0.4045 0.4499 0.4003 -0.0388 0.0450  0.0416  126 GLU A OE2 
985  N N   . VAL A 126 ? 0.2633 0.2843 0.2245 -0.0260 0.0297  0.0463  127 VAL A N   
986  C CA  . VAL A 126 ? 0.2705 0.2905 0.2225 -0.0213 0.0248  0.0443  127 VAL A CA  
987  C C   . VAL A 126 ? 0.2932 0.3044 0.2437 -0.0200 0.0205  0.0484  127 VAL A C   
988  O O   . VAL A 126 ? 0.2850 0.2929 0.2429 -0.0195 0.0169  0.0456  127 VAL A O   
989  C CB  . VAL A 126 ? 0.2634 0.2880 0.2203 -0.0192 0.0216  0.0364  127 VAL A CB  
990  C CG1 . VAL A 126 ? 0.2714 0.2945 0.2209 -0.0154 0.0163  0.0346  127 VAL A CG1 
991  C CG2 . VAL A 126 ? 0.2728 0.3057 0.2310 -0.0195 0.0260  0.0328  127 VAL A CG2 
992  N N   . LYS A 127 ? 0.2953 0.3032 0.2358 -0.0189 0.0209  0.0551  128 LYS A N   
993  C CA  . LYS A 127 ? 0.2549 0.2542 0.1945 -0.0173 0.0177  0.0605  128 LYS A CA  
994  C C   . LYS A 127 ? 0.3361 0.3363 0.2657 -0.0127 0.0126  0.0619  128 LYS A C   
995  O O   . LYS A 127 ? 0.3376 0.3320 0.2681 -0.0102 0.0088  0.0652  128 LYS A O   
996  C CB  . LYS A 127 ? 0.3099 0.3031 0.2485 -0.0200 0.0224  0.0695  128 LYS A CB  
997  C CG  . LYS A 127 ? 0.3155 0.3070 0.2662 -0.0255 0.0271  0.0686  128 LYS A CG  
998  C CD  . LYS A 127 ? 0.4030 0.3866 0.3536 -0.0286 0.0316  0.0783  128 LYS A CD  
999  C CE  . LYS A 127 ? 0.4528 0.4355 0.4167 -0.0352 0.0363  0.0771  128 LYS A CE  
1000 N NZ  . LYS A 127 ? 0.4975 0.4747 0.4732 -0.0359 0.0322  0.0708  128 LYS A NZ  
1001 N N   . THR A 128 ? 0.2721 0.2793 0.1926 -0.0113 0.0121  0.0593  129 THR A N   
1002 C CA  . THR A 128 ? 0.2456 0.2548 0.1563 -0.0076 0.0069  0.0603  129 THR A CA  
1003 C C   . THR A 128 ? 0.2736 0.2889 0.1844 -0.0066 0.0035  0.0515  129 THR A C   
1004 O O   . THR A 128 ? 0.2418 0.2599 0.1575 -0.0082 0.0061  0.0456  129 THR A O   
1005 C CB  . THR A 128 ? 0.2664 0.2779 0.1629 -0.0069 0.0092  0.0665  129 THR A CB  
1006 O OG1 . THR A 128 ? 0.2776 0.2960 0.1689 -0.0082 0.0129  0.0613  129 THR A OG1 
1007 C CG2 . THR A 128 ? 0.2807 0.2859 0.1772 -0.0087 0.0142  0.0762  129 THR A CG2 
1008 N N   . ASP A 129 ? 0.2898 0.3071 0.1958 -0.0038 -0.0026 0.0509  130 ASP A N   
1009 C CA  . ASP A 129 ? 0.2641 0.2863 0.1703 -0.0034 -0.0061 0.0429  130 ASP A CA  
1010 C C   . ASP A 129 ? 0.2602 0.2867 0.1585 -0.0043 -0.0028 0.0384  130 ASP A C   
1011 O O   . ASP A 129 ? 0.2465 0.2747 0.1493 -0.0050 -0.0023 0.0313  130 ASP A O   
1012 C CB  . ASP A 129 ? 0.2825 0.3073 0.1848 -0.0009 -0.0132 0.0434  130 ASP A CB  
1013 C CG  . ASP A 129 ? 0.4012 0.4234 0.3134 0.0007  -0.0167 0.0457  130 ASP A CG  
1014 O OD1 . ASP A 129 ? 0.3828 0.4017 0.3052 -0.0003 -0.0145 0.0441  130 ASP A OD1 
1015 O OD2 . ASP A 129 ? 0.4294 0.4538 0.3390 0.0033  -0.0218 0.0488  130 ASP A OD2 
1016 N N   . GLN A 130 ? 0.2523 0.2806 0.1386 -0.0039 -0.0002 0.0427  131 GLN A N   
1017 C CA  . GLN A 130 ? 0.2427 0.2756 0.1210 -0.0043 0.0040  0.0381  131 GLN A CA  
1018 C C   . GLN A 130 ? 0.2341 0.2668 0.1219 -0.0063 0.0101  0.0352  131 GLN A C   
1019 O O   . GLN A 130 ? 0.2611 0.2967 0.1498 -0.0061 0.0116  0.0277  131 GLN A O   
1020 C CB  . GLN A 130 ? 0.2663 0.3016 0.1301 -0.0036 0.0072  0.0446  131 GLN A CB  
1021 C CG  . GLN A 130 ? 0.2878 0.3264 0.1383 -0.0010 0.0012  0.0460  131 GLN A CG  
1022 C CD  . GLN A 130 ? 0.2858 0.3278 0.1207 -0.0001 0.0054  0.0528  131 GLN A CD  
1023 O OE1 . GLN A 130 ? 0.3108 0.3546 0.1434 -0.0014 0.0132  0.0532  131 GLN A OE1 
1024 N NE2 . GLN A 130 ? 0.2975 0.3414 0.1216 0.0025  0.0004  0.0585  131 GLN A NE2 
1025 N N   . GLN A 131 ? 0.2329 0.2623 0.1290 -0.0082 0.0133  0.0406  132 GLN A N   
1026 C CA  . GLN A 131 ? 0.2286 0.2595 0.1343 -0.0104 0.0189  0.0384  132 GLN A CA  
1027 C C   . GLN A 131 ? 0.2268 0.2574 0.1441 -0.0102 0.0160  0.0316  132 GLN A C   
1028 O O   . GLN A 131 ? 0.2373 0.2714 0.1605 -0.0106 0.0194  0.0273  132 GLN A O   
1029 C CB  . GLN A 131 ? 0.2329 0.2602 0.1441 -0.0132 0.0227  0.0460  132 GLN A CB  
1030 C CG  . GLN A 131 ? 0.2639 0.2923 0.1638 -0.0138 0.0273  0.0535  132 GLN A CG  
1031 C CD  . GLN A 131 ? 0.2906 0.3125 0.1948 -0.0163 0.0296  0.0626  132 GLN A CD  
1032 O OE1 . GLN A 131 ? 0.2822 0.2988 0.1982 -0.0178 0.0279  0.0622  132 GLN A OE1 
1033 N NE2 . GLN A 131 ? 0.2732 0.2952 0.1674 -0.0167 0.0336  0.0708  132 GLN A NE2 
1034 N N   . VAL A 132 ? 0.2107 0.2380 0.1313 -0.0091 0.0099  0.0311  133 VAL A N   
1035 C CA  . VAL A 132 ? 0.2350 0.2623 0.1649 -0.0086 0.0072  0.0254  133 VAL A CA  
1036 C C   . VAL A 132 ? 0.2379 0.2681 0.1643 -0.0073 0.0067  0.0188  133 VAL A C   
1037 O O   . VAL A 132 ? 0.2153 0.2468 0.1488 -0.0070 0.0082  0.0144  133 VAL A O   
1038 C CB  . VAL A 132 ? 0.2387 0.2629 0.1720 -0.0076 0.0013  0.0268  133 VAL A CB  
1039 C CG1 . VAL A 132 ? 0.2101 0.2353 0.1506 -0.0069 -0.0015 0.0214  133 VAL A CG1 
1040 C CG2 . VAL A 132 ? 0.2494 0.2698 0.1888 -0.0085 0.0022  0.0316  133 VAL A CG2 
1041 N N   . LEU A 133 ? 0.2216 0.2525 0.1372 -0.0063 0.0044  0.0177  134 LEU A N   
1042 C CA  . LEU A 133 ? 0.2401 0.2725 0.1522 -0.0053 0.0039  0.0103  134 LEU A CA  
1043 C C   . LEU A 133 ? 0.2490 0.2844 0.1604 -0.0048 0.0106  0.0076  134 LEU A C   
1044 O O   . LEU A 133 ? 0.2299 0.2653 0.1470 -0.0038 0.0118  0.0020  134 LEU A O   
1045 C CB  . LEU A 133 ? 0.2626 0.2962 0.1622 -0.0046 -0.0001 0.0090  134 LEU A CB  
1046 C CG  . LEU A 133 ? 0.2603 0.2950 0.1539 -0.0037 -0.0004 0.0004  134 LEU A CG  
1047 C CD1 . LEU A 133 ? 0.2555 0.2867 0.1602 -0.0039 -0.0025 -0.0054 134 LEU A CD1 
1048 C CD2 . LEU A 133 ? 0.2719 0.3087 0.1530 -0.0034 -0.0056 -0.0008 134 LEU A CD2 
1049 N N   . THR A 134 ? 0.2452 0.2832 0.1507 -0.0054 0.0155  0.0124  135 THR A N   
1050 C CA  . THR A 134 ? 0.2251 0.2678 0.1312 -0.0051 0.0227  0.0106  135 THR A CA  
1051 C C   . THR A 134 ? 0.2358 0.2793 0.1568 -0.0056 0.0246  0.0093  135 THR A C   
1052 O O   . THR A 134 ? 0.2103 0.2569 0.1353 -0.0038 0.0278  0.0042  135 THR A O   
1053 C CB  . THR A 134 ? 0.2399 0.2855 0.1390 -0.0065 0.0278  0.0177  135 THR A CB  
1054 O OG1 . THR A 134 ? 0.2549 0.3010 0.1383 -0.0053 0.0259  0.0187  135 THR A OG1 
1055 C CG2 . THR A 134 ? 0.2897 0.3418 0.1912 -0.0065 0.0361  0.0165  135 THR A CG2 
1056 N N   . PHE A 135 ? 0.2012 0.2423 0.1308 -0.0075 0.0226  0.0137  136 PHE A N   
1057 C CA  . PHE A 135 ? 0.1997 0.2425 0.1428 -0.0080 0.0234  0.0124  136 PHE A CA  
1058 C C   . PHE A 135 ? 0.2148 0.2567 0.1623 -0.0053 0.0206  0.0063  136 PHE A C   
1059 O O   . PHE A 135 ? 0.1902 0.2358 0.1451 -0.0039 0.0232  0.0034  136 PHE A O   
1060 C CB  . PHE A 135 ? 0.2155 0.2548 0.1650 -0.0102 0.0205  0.0169  136 PHE A CB  
1061 C CG  . PHE A 135 ? 0.2113 0.2526 0.1734 -0.0104 0.0196  0.0149  136 PHE A CG  
1062 C CD1 . PHE A 135 ? 0.2171 0.2635 0.1874 -0.0123 0.0235  0.0156  136 PHE A CD1 
1063 C CD2 . PHE A 135 ? 0.1852 0.2240 0.1509 -0.0087 0.0147  0.0125  136 PHE A CD2 
1064 C CE1 . PHE A 135 ? 0.2266 0.2759 0.2077 -0.0122 0.0220  0.0135  136 PHE A CE1 
1065 C CE2 . PHE A 135 ? 0.2111 0.2524 0.1867 -0.0084 0.0137  0.0111  136 PHE A CE2 
1066 C CZ  . PHE A 135 ? 0.2068 0.2536 0.1898 -0.0100 0.0170  0.0113  136 PHE A CZ  
1067 N N   . PHE A 136 ? 0.1890 0.2262 0.1327 -0.0046 0.0153  0.0046  137 PHE A N   
1068 C CA  . PHE A 136 ? 0.1982 0.2336 0.1474 -0.0026 0.0129  -0.0003 137 PHE A CA  
1069 C C   . PHE A 136 ? 0.2257 0.2615 0.1707 -0.0002 0.0157  -0.0063 137 PHE A C   
1070 O O   . PHE A 136 ? 0.2094 0.2445 0.1614 0.0020  0.0162  -0.0098 137 PHE A O   
1071 C CB  . PHE A 136 ? 0.2122 0.2430 0.1608 -0.0032 0.0067  -0.0001 137 PHE A CB  
1072 C CG  . PHE A 136 ? 0.2088 0.2393 0.1648 -0.0042 0.0043  0.0042  137 PHE A CG  
1073 C CD1 . PHE A 136 ? 0.2032 0.2354 0.1688 -0.0035 0.0051  0.0043  137 PHE A CD1 
1074 C CD2 . PHE A 136 ? 0.1723 0.2011 0.1251 -0.0053 0.0010  0.0078  137 PHE A CD2 
1075 C CE1 . PHE A 136 ? 0.1969 0.2292 0.1680 -0.0042 0.0028  0.0073  137 PHE A CE1 
1076 C CE2 . PHE A 136 ? 0.2264 0.2547 0.1855 -0.0057 -0.0009 0.0109  137 PHE A CE2 
1077 C CZ  . PHE A 136 ? 0.1976 0.2276 0.1654 -0.0053 0.0001  0.0103  137 PHE A CZ  
1078 N N   . LYS A 137 ? 0.2079 0.2448 0.1415 -0.0002 0.0175  -0.0076 138 LYS A N   
1079 C CA  . LYS A 137 ? 0.2082 0.2461 0.1371 0.0026  0.0210  -0.0142 138 LYS A CA  
1080 C C   . LYS A 137 ? 0.2359 0.2798 0.1717 0.0044  0.0277  -0.0144 138 LYS A C   
1081 O O   . LYS A 137 ? 0.2599 0.3040 0.1981 0.0078  0.0302  -0.0202 138 LYS A O   
1082 C CB  . LYS A 137 ? 0.2343 0.2737 0.1478 0.0023  0.0218  -0.0153 138 LYS A CB  
1083 C CG  . LYS A 137 ? 0.2702 0.3053 0.1765 0.0011  0.0148  -0.0168 138 LYS A CG  
1084 C CD  . LYS A 137 ? 0.2979 0.3354 0.1878 0.0018  0.0152  -0.0199 138 LYS A CD  
1085 C CE  . LYS A 137 ? 0.3478 0.3913 0.2294 0.0015  0.0202  -0.0132 138 LYS A CE  
1086 N NZ  . LYS A 137 ? 0.3488 0.3959 0.2131 0.0029  0.0213  -0.0167 138 LYS A NZ  
1087 N N   . ASP A 138 ? 0.2108 0.2598 0.1504 0.0022  0.0306  -0.0084 139 ASP A N   
1088 C CA  . ASP A 138 ? 0.2200 0.2768 0.1671 0.0031  0.0369  -0.0081 139 ASP A CA  
1089 C C   . ASP A 138 ? 0.2082 0.2666 0.1701 0.0040  0.0354  -0.0080 139 ASP A C   
1090 O O   . ASP A 138 ? 0.2213 0.2871 0.1914 0.0054  0.0398  -0.0085 139 ASP A O   
1091 C CB  . ASP A 138 ? 0.2394 0.3013 0.1844 -0.0004 0.0411  -0.0016 139 ASP A CB  
1092 C CG  . ASP A 138 ? 0.2472 0.3103 0.1770 -0.0004 0.0444  -0.0011 139 ASP A CG  
1093 O OD1 . ASP A 138 ? 0.2954 0.3569 0.2164 0.0027  0.0441  -0.0072 139 ASP A OD1 
1094 O OD2 . ASP A 138 ? 0.3035 0.3692 0.2301 -0.0035 0.0474  0.0055  139 ASP A OD2 
1095 N N   . TRP A 139 ? 0.2024 0.2547 0.1674 0.0034  0.0292  -0.0072 140 TRP A N   
1096 C CA  . TRP A 139 ? 0.1874 0.2415 0.1647 0.0042  0.0271  -0.0061 140 TRP A CA  
1097 C C   . TRP A 139 ? 0.1867 0.2425 0.1704 0.0090  0.0288  -0.0104 140 TRP A C   
1098 O O   . TRP A 139 ? 0.1985 0.2493 0.1775 0.0117  0.0290  -0.0150 140 TRP A O   
1099 C CB  . TRP A 139 ? 0.1889 0.2362 0.1660 0.0030  0.0208  -0.0045 140 TRP A CB  
1100 C CG  . TRP A 139 ? 0.1860 0.2350 0.1733 0.0037  0.0180  -0.0029 140 TRP A CG  
1101 C CD1 . TRP A 139 ? 0.1710 0.2230 0.1632 0.0014  0.0166  0.0005  140 TRP A CD1 
1102 C CD2 . TRP A 139 ? 0.1546 0.2018 0.1477 0.0073  0.0162  -0.0045 140 TRP A CD2 
1103 N NE1 . TRP A 139 ? 0.1699 0.2235 0.1696 0.0033  0.0139  0.0008  140 TRP A NE1 
1104 C CE2 . TRP A 139 ? 0.1736 0.2242 0.1739 0.0070  0.0137  -0.0015 140 TRP A CE2 
1105 C CE3 . TRP A 139 ? 0.1891 0.2314 0.1816 0.0106  0.0164  -0.0082 140 TRP A CE3 
1106 C CZ2 . TRP A 139 ? 0.1671 0.2176 0.1735 0.0102  0.0115  -0.0011 140 TRP A CZ2 
1107 C CZ3 . TRP A 139 ? 0.2003 0.2411 0.2002 0.0137  0.0144  -0.0075 140 TRP A CZ3 
1108 C CH2 . TRP A 139 ? 0.1724 0.2177 0.1787 0.0135  0.0121  -0.0034 140 TRP A CH2 
1109 N N   . LYS A 140 ? 0.1785 0.2416 0.1735 0.0102  0.0299  -0.0091 141 LYS A N   
1110 C CA  . LYS A 140 ? 0.2236 0.2891 0.2269 0.0154  0.0308  -0.0118 141 LYS A CA  
1111 C C   . LYS A 140 ? 0.2047 0.2717 0.2169 0.0159  0.0262  -0.0087 141 LYS A C   
1112 O O   . LYS A 140 ? 0.1830 0.2539 0.1978 0.0122  0.0245  -0.0054 141 LYS A O   
1113 C CB  . LYS A 140 ? 0.2294 0.3058 0.2386 0.0175  0.0370  -0.0132 141 LYS A CB  
1114 C CG  . LYS A 140 ? 0.3086 0.3863 0.3085 0.0169  0.0426  -0.0155 141 LYS A CG  
1115 C CD  . LYS A 140 ? 0.3395 0.4119 0.3347 0.0221  0.0444  -0.0218 141 LYS A CD  
1116 C CE  . LYS A 140 ? 0.3570 0.4372 0.3629 0.0281  0.0486  -0.0245 141 LYS A CE  
1117 N NZ  . LYS A 140 ? 0.4520 0.5445 0.4593 0.0281  0.0561  -0.0247 141 LYS A NZ  
1118 N N   . PRO A 141 ? 0.1716 0.2353 0.1883 0.0205  0.0244  -0.0096 142 PRO A N   
1119 C CA  . PRO A 141 ? 0.1456 0.2119 0.1698 0.0216  0.0203  -0.0061 142 PRO A CA  
1120 C C   . PRO A 141 ? 0.1654 0.2450 0.1999 0.0229  0.0216  -0.0051 142 PRO A C   
1121 O O   . PRO A 141 ? 0.1993 0.2859 0.2372 0.0242  0.0263  -0.0072 142 PRO A O   
1122 C CB  . PRO A 141 ? 0.1951 0.2536 0.2211 0.0265  0.0189  -0.0069 142 PRO A CB  
1123 C CG  . PRO A 141 ? 0.1827 0.2382 0.2063 0.0296  0.0234  -0.0121 142 PRO A CG  
1124 C CD  . PRO A 141 ? 0.2072 0.2633 0.2216 0.0248  0.0258  -0.0139 142 PRO A CD  
1125 N N   . LYS A 142 ? 0.1708 0.2547 0.2102 0.0224  0.0175  -0.0020 143 LYS A N   
1126 C CA  . LYS A 142 ? 0.1780 0.2754 0.2280 0.0237  0.0172  -0.0013 143 LYS A CA  
1127 C C   . LYS A 142 ? 0.1829 0.2817 0.2376 0.0287  0.0130  0.0013  143 LYS A C   
1128 O O   . LYS A 142 ? 0.1900 0.2903 0.2501 0.0349  0.0141  0.0013  143 LYS A O   
1129 C CB  . LYS A 142 ? 0.1928 0.2958 0.2435 0.0173  0.0160  -0.0006 143 LYS A CB  
1130 C CG  . LYS A 142 ? 0.2372 0.3555 0.2997 0.0171  0.0156  -0.0008 143 LYS A CG  
1131 C CD  . LYS A 142 ? 0.3289 0.4513 0.3929 0.0097  0.0169  -0.0013 143 LYS A CD  
1132 C CE  . LYS A 142 ? 0.3579 0.4803 0.4201 0.0076  0.0237  -0.0021 143 LYS A CE  
1133 N NZ  . LYS A 142 ? 0.3934 0.5253 0.4632 0.0016  0.0264  -0.0019 143 LYS A NZ  
1134 N N   . ASN A 143 ? 0.1594 0.2573 0.2117 0.0266  0.0084  0.0038  144 ASN A N   
1135 C CA  . ASN A 143 ? 0.1413 0.2413 0.1966 0.0313  0.0045  0.0073  144 ASN A CA  
1136 C C   . ASN A 143 ? 0.1538 0.2405 0.2042 0.0342  0.0045  0.0091  144 ASN A C   
1137 O O   . ASN A 143 ? 0.1831 0.2594 0.2266 0.0311  0.0060  0.0075  144 ASN A O   
1138 C CB  . ASN A 143 ? 0.1793 0.2840 0.2329 0.0280  0.0001  0.0087  144 ASN A CB  
1139 C CG  . ASN A 143 ? 0.1970 0.3141 0.2568 0.0244  -0.0002 0.0061  144 ASN A CG  
1140 O OD1 . ASN A 143 ? 0.3354 0.4520 0.3923 0.0188  -0.0011 0.0046  144 ASN A OD1 
1141 N ND2 . ASN A 143 ? 0.2279 0.3563 0.2973 0.0278  0.0006  0.0055  144 ASN A ND2 
1142 N N   . SER A 144 ? 0.1688 0.2560 0.2235 0.0401  0.0028  0.0127  145 SER A N   
1143 C CA  . SER A 144 ? 0.1548 0.2287 0.2067 0.0427  0.0032  0.0149  145 SER A CA  
1144 C C   . SER A 144 ? 0.1621 0.2270 0.2058 0.0374  0.0018  0.0158  145 SER A C   
1145 O O   . SER A 144 ? 0.1648 0.2339 0.2060 0.0352  -0.0010 0.0184  145 SER A O   
1146 C CB  . SER A 144 ? 0.2174 0.2936 0.2746 0.0493  0.0009  0.0206  145 SER A CB  
1147 O OG  . SER A 144 ? 0.2703 0.3530 0.3359 0.0554  0.0025  0.0198  145 SER A OG  
1148 N N   . ILE A 145 ? 0.1808 0.2340 0.2204 0.0355  0.0038  0.0131  146 ILE A N   
1149 C CA  . ILE A 145 ? 0.1781 0.2239 0.2110 0.0304  0.0025  0.0135  146 ILE A CA  
1150 C C   . ILE A 145 ? 0.1845 0.2284 0.2179 0.0315  -0.0001 0.0196  146 ILE A C   
1151 O O   . ILE A 145 ? 0.1880 0.2280 0.2256 0.0359  0.0001  0.0231  146 ILE A O   
1152 C CB  . ILE A 145 ? 0.1651 0.1996 0.1946 0.0289  0.0044  0.0093  146 ILE A CB  
1153 C CG1 . ILE A 145 ? 0.1815 0.2193 0.2080 0.0273  0.0073  0.0037  146 ILE A CG1 
1154 C CG2 . ILE A 145 ? 0.1905 0.2177 0.2152 0.0243  0.0024  0.0106  146 ILE A CG2 
1155 C CD1 . ILE A 145 ? 0.2287 0.2571 0.2516 0.0273  0.0095  -0.0016 146 ILE A CD1 
1156 N N   . GLY A 146 ? 0.1772 0.2237 0.2065 0.0277  -0.0020 0.0213  147 GLY A N   
1157 C CA  . GLY A 146 ? 0.1895 0.2358 0.2183 0.0283  -0.0038 0.0272  147 GLY A CA  
1158 C C   . GLY A 146 ? 0.2062 0.2636 0.2362 0.0316  -0.0058 0.0308  147 GLY A C   
1159 O O   . GLY A 146 ? 0.2070 0.2664 0.2346 0.0317  -0.0072 0.0354  147 GLY A O   
1160 N N   A GLU A 147 ? 0.1788 0.2448 0.2125 0.0342  -0.0061 0.0288  148 GLU A N   
1161 N N   B GLU A 147 ? 0.1735 0.2395 0.2072 0.0342  -0.0061 0.0288  148 GLU A N   
1162 C CA  A GLU A 147 ? 0.1874 0.2646 0.2232 0.0382  -0.0088 0.0323  148 GLU A CA  
1163 C CA  B GLU A 147 ? 0.1870 0.2642 0.2228 0.0382  -0.0088 0.0324  148 GLU A CA  
1164 C C   A GLU A 147 ? 0.1730 0.2608 0.2063 0.0353  -0.0111 0.0295  148 GLU A C   
1165 C C   B GLU A 147 ? 0.1740 0.2618 0.2073 0.0354  -0.0111 0.0295  148 GLU A C   
1166 O O   A GLU A 147 ? 0.1536 0.2501 0.1859 0.0378  -0.0140 0.0323  148 GLU A O   
1167 O O   B GLU A 147 ? 0.1499 0.2469 0.1826 0.0380  -0.0140 0.0322  148 GLU A O   
1168 C CB  A GLU A 147 ? 0.2052 0.2874 0.2484 0.0436  -0.0083 0.0321  148 GLU A CB  
1169 C CB  B GLU A 147 ? 0.2048 0.2869 0.2480 0.0437  -0.0084 0.0324  148 GLU A CB  
1170 C CG  A GLU A 147 ? 0.2182 0.2900 0.2648 0.0480  -0.0064 0.0355  148 GLU A CG  
1171 C CG  B GLU A 147 ? 0.2172 0.2889 0.2637 0.0483  -0.0066 0.0362  148 GLU A CG  
1172 C CD  A GLU A 147 ? 0.2396 0.3078 0.2845 0.0507  -0.0077 0.0436  148 GLU A CD  
1173 C CD  B GLU A 147 ? 0.2798 0.3574 0.3342 0.0555  -0.0066 0.0376  148 GLU A CD  
1174 O OE1 A GLU A 147 ? 0.2566 0.3353 0.3008 0.0536  -0.0105 0.0479  148 GLU A OE1 
1175 O OE1 B GLU A 147 ? 0.2566 0.3486 0.3142 0.0572  -0.0088 0.0369  148 GLU A OE1 
1176 O OE2 A GLU A 147 ? 0.2671 0.3224 0.3114 0.0496  -0.0059 0.0457  148 GLU A OE2 
1177 O OE2 B GLU A 147 ? 0.2995 0.3675 0.3577 0.0596  -0.0045 0.0393  148 GLU A OE2 
1178 N N   . TYR A 148 ? 0.1643 0.2511 0.1961 0.0303  -0.0101 0.0240  149 TYR A N   
1179 C CA  . TYR A 148 ? 0.1501 0.2454 0.1808 0.0273  -0.0122 0.0206  149 TYR A CA  
1180 C C   . TYR A 148 ? 0.1599 0.2486 0.1849 0.0223  -0.0116 0.0185  149 TYR A C   
1181 O O   . TYR A 148 ? 0.1678 0.2486 0.1916 0.0195  -0.0092 0.0167  149 TYR A O   
1182 C CB  . TYR A 148 ? 0.1639 0.2666 0.2009 0.0262  -0.0117 0.0163  149 TYR A CB  
1183 C CG  . TYR A 148 ? 0.1927 0.3035 0.2368 0.0317  -0.0124 0.0182  149 TYR A CG  
1184 C CD1 . TYR A 148 ? 0.2357 0.3414 0.2836 0.0349  -0.0094 0.0191  149 TYR A CD1 
1185 C CD2 . TYR A 148 ? 0.2190 0.3430 0.2662 0.0340  -0.0163 0.0187  149 TYR A CD2 
1186 C CE1 . TYR A 148 ? 0.2514 0.3645 0.3066 0.0408  -0.0099 0.0209  149 TYR A CE1 
1187 C CE2 . TYR A 148 ? 0.2033 0.3360 0.2577 0.0399  -0.0174 0.0210  149 TYR A CE2 
1188 C CZ  . TYR A 148 ? 0.2413 0.3683 0.3001 0.0434  -0.0140 0.0223  149 TYR A CZ  
1189 O OH  . TYR A 148 ? 0.2781 0.4134 0.3449 0.0500  -0.0148 0.0247  149 TYR A OH  
1190 N N   . ARG A 149 ? 0.1446 0.2374 0.1659 0.0216  -0.0138 0.0183  150 ARG A N   
1191 C CA  . ARG A 149 ? 0.1545 0.2424 0.1712 0.0177  -0.0135 0.0160  150 ARG A CA  
1192 C C   . ARG A 149 ? 0.1469 0.2372 0.1655 0.0139  -0.0138 0.0106  150 ARG A C   
1193 O O   . ARG A 149 ? 0.1385 0.2378 0.1598 0.0140  -0.0161 0.0081  150 ARG A O   
1194 C CB  . ARG A 149 ? 0.1389 0.2303 0.1509 0.0192  -0.0152 0.0177  150 ARG A CB  
1195 C CG  . ARG A 149 ? 0.1549 0.2417 0.1630 0.0161  -0.0148 0.0151  150 ARG A CG  
1196 C CD  . ARG A 149 ? 0.1248 0.2176 0.1283 0.0183  -0.0163 0.0156  150 ARG A CD  
1197 N NE  . ARG A 149 ? 0.1294 0.2177 0.1298 0.0164  -0.0154 0.0135  150 ARG A NE  
1198 C CZ  . ARG A 149 ? 0.1692 0.2569 0.1692 0.0143  -0.0162 0.0079  150 ARG A CZ  
1199 N NH1 . ARG A 149 ? 0.1459 0.2375 0.1486 0.0128  -0.0180 0.0035  150 ARG A NH1 
1200 N NH2 . ARG A 149 ? 0.1845 0.2675 0.1821 0.0136  -0.0153 0.0068  150 ARG A NH2 
1201 N N   . GLN A 150 ? 0.1321 0.2148 0.1496 0.0103  -0.0117 0.0090  151 GLN A N   
1202 C CA  . GLN A 150 ? 0.1272 0.2099 0.1459 0.0062  -0.0116 0.0050  151 GLN A CA  
1203 C C   . GLN A 150 ? 0.1253 0.1991 0.1391 0.0041  -0.0108 0.0051  151 GLN A C   
1204 O O   . GLN A 150 ? 0.1457 0.2128 0.1574 0.0035  -0.0088 0.0070  151 GLN A O   
1205 C CB  . GLN A 150 ? 0.1530 0.2371 0.1768 0.0041  -0.0093 0.0037  151 GLN A CB  
1206 C CG  . GLN A 150 ? 0.1742 0.2580 0.2003 -0.0008 -0.0089 0.0004  151 GLN A CG  
1207 C CD  . GLN A 150 ? 0.2231 0.3121 0.2561 -0.0032 -0.0066 -0.0007 151 GLN A CD  
1208 O OE1 . GLN A 150 ? 0.2475 0.3369 0.2815 -0.0015 -0.0040 0.0009  151 GLN A OE1 
1209 N NE2 . GLN A 150 ? 0.2524 0.3457 0.2907 -0.0071 -0.0074 -0.0039 151 GLN A NE2 
1210 N N   . TYR A 151 ? 0.1472 0.2212 0.1590 0.0035  -0.0124 0.0030  152 TYR A N   
1211 C CA  . TYR A 151 ? 0.1389 0.2053 0.1468 0.0026  -0.0118 0.0032  152 TYR A CA  
1212 C C   . TYR A 151 ? 0.1508 0.2103 0.1591 -0.0007 -0.0097 0.0035  152 TYR A C   
1213 O O   . TYR A 151 ? 0.1571 0.2175 0.1689 -0.0036 -0.0090 0.0015  152 TYR A O   
1214 C CB  . TYR A 151 ? 0.1360 0.2039 0.1431 0.0025  -0.0136 -0.0006 152 TYR A CB  
1215 C CG  . TYR A 151 ? 0.1500 0.2114 0.1538 0.0030  -0.0132 -0.0004 152 TYR A CG  
1216 C CD1 . TYR A 151 ? 0.1577 0.2193 0.1585 0.0058  -0.0129 0.0029  152 TYR A CD1 
1217 C CD2 . TYR A 151 ? 0.1869 0.2422 0.1915 0.0008  -0.0130 -0.0032 152 TYR A CD2 
1218 C CE1 . TYR A 151 ? 0.1808 0.2382 0.1798 0.0068  -0.0125 0.0031  152 TYR A CE1 
1219 C CE2 . TYR A 151 ? 0.2158 0.2653 0.2179 0.0022  -0.0126 -0.0028 152 TYR A CE2 
1220 C CZ  . TYR A 151 ? 0.1974 0.2489 0.1970 0.0053  -0.0124 0.0003  152 TYR A CZ  
1221 O OH  . TYR A 151 ? 0.1956 0.2432 0.1940 0.0072  -0.0121 0.0008  152 TYR A OH  
1222 N N   . SER A 152 ? 0.1293 0.1827 0.1340 -0.0004 -0.0088 0.0062  153 SER A N   
1223 C CA  . SER A 152 ? 0.1442 0.1925 0.1476 -0.0028 -0.0068 0.0074  153 SER A CA  
1224 C C   . SER A 152 ? 0.1523 0.1942 0.1514 -0.0027 -0.0070 0.0095  153 SER A C   
1225 O O   . SER A 152 ? 0.1569 0.1985 0.1542 -0.0010 -0.0079 0.0112  153 SER A O   
1226 C CB  . SER A 152 ? 0.1367 0.1871 0.1408 -0.0020 -0.0054 0.0082  153 SER A CB  
1227 O OG  . SER A 152 ? 0.1409 0.1871 0.1421 -0.0038 -0.0032 0.0091  153 SER A OG  
1228 N N   . ASN A 153 ? 0.1336 0.1704 0.1315 -0.0046 -0.0063 0.0099  154 ASN A N   
1229 C CA  . ASN A 153 ? 0.1479 0.1794 0.1417 -0.0041 -0.0068 0.0126  154 ASN A CA  
1230 C C   . ASN A 153 ? 0.1848 0.2157 0.1747 -0.0045 -0.0060 0.0144  154 ASN A C   
1231 O O   . ASN A 153 ? 0.1746 0.2048 0.1619 -0.0032 -0.0077 0.0156  154 ASN A O   
1232 C CB  . ASN A 153 ? 0.1571 0.1826 0.1507 -0.0055 -0.0062 0.0135  154 ASN A CB  
1233 C CG  . ASN A 153 ? 0.1978 0.2224 0.1943 -0.0042 -0.0075 0.0110  154 ASN A CG  
1234 O OD1 . ASN A 153 ? 0.2003 0.2291 0.1974 -0.0017 -0.0089 0.0096  154 ASN A OD1 
1235 N ND2 . ASN A 153 ? 0.2756 0.2943 0.2739 -0.0060 -0.0067 0.0104  154 ASN A ND2 
1236 N N   . PRO A 154 ? 0.1647 0.1963 0.1539 -0.0062 -0.0035 0.0141  155 PRO A N   
1237 C CA  . PRO A 154 ? 0.1736 0.2050 0.1583 -0.0060 -0.0027 0.0144  155 PRO A CA  
1238 C C   . PRO A 154 ? 0.1666 0.1996 0.1521 -0.0042 -0.0044 0.0132  155 PRO A C   
1239 O O   . PRO A 154 ? 0.1725 0.2037 0.1541 -0.0040 -0.0056 0.0132  155 PRO A O   
1240 C CB  . PRO A 154 ? 0.1904 0.2244 0.1764 -0.0075 0.0009  0.0135  155 PRO A CB  
1241 C CG  . PRO A 154 ? 0.2059 0.2394 0.1956 -0.0099 0.0019  0.0142  155 PRO A CG  
1242 C CD  . PRO A 154 ? 0.1727 0.2056 0.1656 -0.0087 -0.0011 0.0132  155 PRO A CD  
1243 N N   . SER A 155 ? 0.1649 0.2014 0.1555 -0.0029 -0.0048 0.0121  156 SER A N   
1244 C CA  . SER A 155 ? 0.1718 0.2092 0.1640 -0.0013 -0.0058 0.0118  156 SER A CA  
1245 C C   . SER A 155 ? 0.1470 0.1827 0.1382 -0.0010 -0.0083 0.0134  156 SER A C   
1246 O O   . SER A 155 ? 0.1641 0.1978 0.1542 -0.0014 -0.0092 0.0131  156 SER A O   
1247 C CB  . SER A 155 ? 0.1575 0.1996 0.1548 0.0005  -0.0058 0.0116  156 SER A CB  
1248 O OG  . SER A 155 ? 0.1476 0.1896 0.1468 0.0023  -0.0060 0.0122  156 SER A OG  
1249 N N   . ILE A 156 ? 0.1558 0.1928 0.1482 -0.0005 -0.0093 0.0145  157 ILE A N   
1250 C CA  . ILE A 156 ? 0.1737 0.2110 0.1666 0.0000  -0.0113 0.0161  157 ILE A CA  
1251 C C   . ILE A 156 ? 0.1564 0.1909 0.1454 -0.0010 -0.0126 0.0168  157 ILE A C   
1252 O O   . ILE A 156 ? 0.1752 0.2107 0.1649 -0.0011 -0.0147 0.0177  157 ILE A O   
1253 C CB  . ILE A 156 ? 0.2083 0.2491 0.2038 0.0018  -0.0116 0.0167  157 ILE A CB  
1254 C CG1 . ILE A 156 ? 0.2165 0.2599 0.2142 0.0025  -0.0128 0.0187  157 ILE A CG1 
1255 C CG2 . ILE A 156 ? 0.2097 0.2481 0.2037 0.0018  -0.0115 0.0160  157 ILE A CG2 
1256 C CD1 . ILE A 156 ? 0.2002 0.2484 0.2001 0.0048  -0.0123 0.0193  157 ILE A CD1 
1257 N N   . GLY A 157 ? 0.1690 0.2008 0.1543 -0.0017 -0.0116 0.0168  158 GLY A N   
1258 C CA  . GLY A 157 ? 0.1792 0.2087 0.1595 -0.0023 -0.0129 0.0181  158 GLY A CA  
1259 C C   . GLY A 157 ? 0.1493 0.1789 0.1265 -0.0033 -0.0139 0.0165  158 GLY A C   
1260 O O   . GLY A 157 ? 0.1808 0.2112 0.1562 -0.0035 -0.0168 0.0170  158 GLY A O   
1261 N N   . LEU A 158 ? 0.1773 0.2065 0.1545 -0.0038 -0.0117 0.0141  159 LEU A N   
1262 C CA  . LEU A 158 ? 0.1731 0.2011 0.1476 -0.0046 -0.0124 0.0113  159 LEU A CA  
1263 C C   . LEU A 158 ? 0.1860 0.2147 0.1656 -0.0050 -0.0150 0.0111  159 LEU A C   
1264 O O   . LEU A 158 ? 0.1792 0.2075 0.1570 -0.0063 -0.0177 0.0096  159 LEU A O   
1265 C CB  . LEU A 158 ? 0.1789 0.2061 0.1537 -0.0041 -0.0091 0.0087  159 LEU A CB  
1266 C CG  . LEU A 158 ? 0.1908 0.2156 0.1629 -0.0044 -0.0092 0.0046  159 LEU A CG  
1267 C CD1 . LEU A 158 ? 0.2434 0.2677 0.2068 -0.0055 -0.0108 0.0032  159 LEU A CD1 
1268 C CD2 . LEU A 158 ? 0.2175 0.2421 0.1910 -0.0029 -0.0053 0.0021  159 LEU A CD2 
1269 N N   . PHE A 159 ? 0.1684 0.1988 0.1543 -0.0041 -0.0145 0.0127  160 PHE A N   
1270 C CA  . PHE A 159 ? 0.1822 0.2139 0.1735 -0.0048 -0.0163 0.0137  160 PHE A CA  
1271 C C   . PHE A 159 ? 0.1730 0.2075 0.1644 -0.0056 -0.0194 0.0150  160 PHE A C   
1272 O O   . PHE A 159 ? 0.1675 0.2027 0.1612 -0.0075 -0.0218 0.0141  160 PHE A O   
1273 C CB  . PHE A 159 ? 0.1823 0.2168 0.1787 -0.0031 -0.0147 0.0162  160 PHE A CB  
1274 C CG  . PHE A 159 ? 0.1319 0.1688 0.1343 -0.0038 -0.0156 0.0185  160 PHE A CG  
1275 C CD1 . PHE A 159 ? 0.1607 0.1946 0.1666 -0.0052 -0.0154 0.0184  160 PHE A CD1 
1276 C CD2 . PHE A 159 ? 0.1502 0.1922 0.1550 -0.0029 -0.0161 0.0210  160 PHE A CD2 
1277 C CE1 . PHE A 159 ? 0.1791 0.2154 0.1913 -0.0064 -0.0157 0.0214  160 PHE A CE1 
1278 C CE2 . PHE A 159 ? 0.1597 0.2054 0.1706 -0.0037 -0.0162 0.0237  160 PHE A CE2 
1279 C CZ  . PHE A 159 ? 0.1747 0.2176 0.1894 -0.0058 -0.0159 0.0243  160 PHE A CZ  
1280 N N   . GLY A 160 ? 0.1558 0.1921 0.1455 -0.0040 -0.0195 0.0169  161 GLY A N   
1281 C CA  . GLY A 160 ? 0.1527 0.1922 0.1429 -0.0037 -0.0226 0.0186  161 GLY A CA  
1282 C C   . GLY A 160 ? 0.1771 0.2160 0.1619 -0.0052 -0.0255 0.0171  161 GLY A C   
1283 O O   . GLY A 160 ? 0.1913 0.2342 0.1788 -0.0061 -0.0290 0.0172  161 GLY A O   
1284 N N   . LYS A 161 ? 0.1580 0.1932 0.1353 -0.0053 -0.0242 0.0157  162 LYS A N   
1285 C CA  . LYS A 161 ? 0.2139 0.2491 0.1841 -0.0064 -0.0267 0.0137  162 LYS A CA  
1286 C C   . LYS A 161 ? 0.2087 0.2441 0.1815 -0.0091 -0.0290 0.0095  162 LYS A C   
1287 O O   . LYS A 161 ? 0.2123 0.2507 0.1835 -0.0104 -0.0333 0.0080  162 LYS A O   
1288 C CB  . LYS A 161 ? 0.1894 0.2210 0.1512 -0.0061 -0.0234 0.0129  162 LYS A CB  
1289 C CG  . LYS A 161 ? 0.2721 0.3038 0.2248 -0.0070 -0.0250 0.0099  162 LYS A CG  
1290 C CD  . LYS A 161 ? 0.3084 0.3432 0.2553 -0.0061 -0.0287 0.0129  162 LYS A CD  
1291 C CE  . LYS A 161 ? 0.2947 0.3304 0.2304 -0.0066 -0.0300 0.0098  162 LYS A CE  
1292 N NZ  . LYS A 161 ? 0.3523 0.3923 0.2821 -0.0053 -0.0345 0.0134  162 LYS A NZ  
1293 N N   . VAL A 162 ? 0.1849 0.2171 0.1623 -0.0098 -0.0264 0.0076  163 VAL A N   
1294 C CA  . VAL A 162 ? 0.2025 0.2328 0.1835 -0.0125 -0.0280 0.0036  163 VAL A CA  
1295 C C   . VAL A 162 ? 0.1893 0.2243 0.1791 -0.0144 -0.0312 0.0055  163 VAL A C   
1296 O O   . VAL A 162 ? 0.1802 0.2164 0.1717 -0.0174 -0.0350 0.0024  163 VAL A O   
1297 C CB  . VAL A 162 ? 0.2077 0.2328 0.1920 -0.0119 -0.0242 0.0023  163 VAL A CB  
1298 C CG1 . VAL A 162 ? 0.2394 0.2611 0.2303 -0.0148 -0.0256 -0.0004 163 VAL A CG1 
1299 C CG2 . VAL A 162 ? 0.2279 0.2496 0.2042 -0.0104 -0.0214 -0.0009 163 VAL A CG2 
1300 N N   . VAL A 163 ? 0.1792 0.2177 0.1748 -0.0129 -0.0297 0.0102  164 VAL A N   
1301 C CA  . VAL A 163 ? 0.1797 0.2245 0.1841 -0.0143 -0.0320 0.0126  164 VAL A CA  
1302 C C   . VAL A 163 ? 0.2071 0.2574 0.2098 -0.0149 -0.0369 0.0119  164 VAL A C   
1303 O O   . VAL A 163 ? 0.2183 0.2728 0.2271 -0.0182 -0.0405 0.0105  164 VAL A O   
1304 C CB  . VAL A 163 ? 0.1851 0.2335 0.1938 -0.0114 -0.0291 0.0173  164 VAL A CB  
1305 C CG1 . VAL A 163 ? 0.2021 0.2589 0.2192 -0.0120 -0.0311 0.0199  164 VAL A CG1 
1306 C CG2 . VAL A 163 ? 0.1714 0.2164 0.1830 -0.0111 -0.0252 0.0183  164 VAL A CG2 
1307 N N   . ALA A 164 ? 0.1908 0.2415 0.1856 -0.0120 -0.0375 0.0131  165 ALA A N   
1308 C CA  . ALA A 164 ? 0.1875 0.2438 0.1795 -0.0117 -0.0425 0.0134  165 ALA A CA  
1309 C C   . ALA A 164 ? 0.2278 0.2838 0.2157 -0.0151 -0.0464 0.0080  165 ALA A C   
1310 O O   . ALA A 164 ? 0.2172 0.2800 0.2090 -0.0171 -0.0516 0.0067  165 ALA A O   
1311 C CB  . ALA A 164 ? 0.2099 0.2646 0.1934 -0.0077 -0.0416 0.0166  165 ALA A CB  
1312 N N   . LEU A 165 ? 0.2018 0.2506 0.1819 -0.0157 -0.0441 0.0041  166 LEU A N   
1313 C CA  . LEU A 165 ? 0.2204 0.2681 0.1956 -0.0187 -0.0475 -0.0025 166 LEU A CA  
1314 C C   . LEU A 165 ? 0.2390 0.2875 0.2253 -0.0233 -0.0500 -0.0058 166 LEU A C   
1315 O O   . LEU A 165 ? 0.2254 0.2776 0.2117 -0.0264 -0.0555 -0.0103 166 LEU A O   
1316 C CB  . LEU A 165 ? 0.2155 0.2552 0.1819 -0.0179 -0.0434 -0.0064 166 LEU A CB  
1317 C CG  . LEU A 165 ? 0.2321 0.2716 0.1869 -0.0144 -0.0411 -0.0037 166 LEU A CG  
1318 C CD1 . LEU A 165 ? 0.2372 0.2701 0.1873 -0.0134 -0.0354 -0.0064 166 LEU A CD1 
1319 C CD2 . LEU A 165 ? 0.2655 0.3100 0.2101 -0.0143 -0.0461 -0.0053 166 LEU A CD2 
1320 N N   . SER A 166 ? 0.2271 0.2725 0.2228 -0.0240 -0.0462 -0.0035 167 SER A N   
1321 C CA  . SER A 166 ? 0.1902 0.2354 0.1974 -0.0288 -0.0478 -0.0054 167 SER A CA  
1322 C C   . SER A 166 ? 0.2129 0.2692 0.2290 -0.0310 -0.0524 -0.0032 167 SER A C   
1323 O O   . SER A 166 ? 0.2301 0.2880 0.2552 -0.0362 -0.0554 -0.0061 167 SER A O   
1324 C CB  . SER A 166 ? 0.2027 0.2431 0.2174 -0.0284 -0.0423 -0.0016 167 SER A CB  
1325 O OG  . SER A 166 ? 0.2101 0.2576 0.2308 -0.0265 -0.0407 0.0051  167 SER A OG  
1326 N N   . MET A 167 ? 0.1936 0.2574 0.2084 -0.0272 -0.0530 0.0018  168 MET A N   
1327 C CA  . MET A 167 ? 0.2388 0.3146 0.2625 -0.0278 -0.0571 0.0045  168 MET A CA  
1328 C C   . MET A 167 ? 0.2643 0.3465 0.2808 -0.0268 -0.0635 0.0025  168 MET A C   
1329 O O   . MET A 167 ? 0.2439 0.3375 0.2672 -0.0263 -0.0676 0.0051  168 MET A O   
1330 C CB  . MET A 167 ? 0.2214 0.3013 0.2496 -0.0234 -0.0531 0.0114  168 MET A CB  
1331 C CG  . MET A 167 ? 0.2562 0.3327 0.2922 -0.0244 -0.0474 0.0140  168 MET A CG  
1332 S SD  . MET A 167 ? 0.3027 0.3825 0.3404 -0.0185 -0.0421 0.0204  168 MET A SD  
1333 C CE  . MET A 167 ? 0.3035 0.3987 0.3527 -0.0180 -0.0455 0.0234  168 MET A CE  
1334 N N   . ASN A 168 ? 0.2363 0.3126 0.2393 -0.0262 -0.0645 -0.0016 169 ASN A N   
1335 C CA  . ASN A 168 ? 0.2547 0.3370 0.2485 -0.0252 -0.0707 -0.0037 169 ASN A CA  
1336 C C   . ASN A 168 ? 0.2731 0.3631 0.2656 -0.0198 -0.0722 0.0033  169 ASN A C   
1337 O O   . ASN A 168 ? 0.2498 0.3498 0.2423 -0.0193 -0.0788 0.0036  169 ASN A O   
1338 C CB  . ASN A 168 ? 0.2613 0.3504 0.2614 -0.0309 -0.0777 -0.0098 169 ASN A CB  
1339 C CG  . ASN A 168 ? 0.3675 0.4470 0.3684 -0.0361 -0.0764 -0.0176 169 ASN A CG  
1340 O OD1 . ASN A 168 ? 0.4498 0.5292 0.4640 -0.0412 -0.0767 -0.0192 169 ASN A OD1 
1341 N ND2 . ASN A 168 ? 0.4175 0.4885 0.4044 -0.0347 -0.0746 -0.0221 169 ASN A ND2 
1342 N N   . LYS A 169 ? 0.2294 0.3146 0.2209 -0.0155 -0.0665 0.0089  170 LYS A N   
1343 C CA  . LYS A 169 ? 0.2632 0.3524 0.2523 -0.0098 -0.0671 0.0154  170 LYS A CA  
1344 C C   . LYS A 169 ? 0.2563 0.3356 0.2387 -0.0063 -0.0605 0.0187  170 LYS A C   
1345 O O   . LYS A 169 ? 0.2406 0.3128 0.2245 -0.0080 -0.0554 0.0169  170 LYS A O   
1346 C CB  . LYS A 169 ? 0.2911 0.3902 0.2946 -0.0084 -0.0686 0.0192  170 LYS A CB  
1347 C CG  . LYS A 169 ? 0.3385 0.4358 0.3530 -0.0098 -0.0631 0.0198  170 LYS A CG  
1348 C CD  . LYS A 169 ? 0.3317 0.4410 0.3602 -0.0082 -0.0644 0.0234  170 LYS A CD  
1349 C CE  . LYS A 169 ? 0.4230 0.5438 0.4613 -0.0131 -0.0706 0.0206  170 LYS A CE  
1350 N NZ  . LYS A 169 ? 0.3603 0.4785 0.4065 -0.0198 -0.0684 0.0171  170 LYS A NZ  
1351 N N   . PRO A 170 ? 0.2240 0.3026 0.1994 -0.0016 -0.0606 0.0237  171 PRO A N   
1352 C CA  . PRO A 170 ? 0.2440 0.3130 0.2143 0.0008  -0.0544 0.0267  171 PRO A CA  
1353 C C   . PRO A 170 ? 0.2290 0.2968 0.2099 0.0021  -0.0503 0.0283  171 PRO A C   
1354 O O   . PRO A 170 ? 0.2175 0.2925 0.2087 0.0028  -0.0521 0.0293  171 PRO A O   
1355 C CB  . PRO A 170 ? 0.2584 0.3275 0.2208 0.0054  -0.0562 0.0324  171 PRO A CB  
1356 C CG  . PRO A 170 ? 0.2947 0.3749 0.2598 0.0064  -0.0637 0.0333  171 PRO A CG  
1357 C CD  . PRO A 170 ? 0.2485 0.3345 0.2192 0.0012  -0.0668 0.0267  171 PRO A CD  
1358 N N   . PHE A 171 ? 0.1908 0.2502 0.1690 0.0024  -0.0447 0.0284  172 PHE A N   
1359 C CA  . PHE A 171 ? 0.1984 0.2567 0.1849 0.0032  -0.0409 0.0288  172 PHE A CA  
1360 C C   . PHE A 171 ? 0.2037 0.2660 0.1964 0.0078  -0.0417 0.0327  172 PHE A C   
1361 O O   . PHE A 171 ? 0.1988 0.2661 0.2008 0.0084  -0.0407 0.0325  172 PHE A O   
1362 C CB  . PHE A 171 ? 0.2203 0.2700 0.2025 0.0031  -0.0356 0.0282  172 PHE A CB  
1363 C CG  . PHE A 171 ? 0.1993 0.2485 0.1884 0.0040  -0.0321 0.0280  172 PHE A CG  
1364 C CD1 . PHE A 171 ? 0.2035 0.2543 0.1974 0.0015  -0.0306 0.0255  172 PHE A CD1 
1365 C CD2 . PHE A 171 ? 0.2107 0.2578 0.2015 0.0076  -0.0304 0.0302  172 PHE A CD2 
1366 C CE1 . PHE A 171 ? 0.1879 0.2394 0.1869 0.0028  -0.0275 0.0257  172 PHE A CE1 
1367 C CE2 . PHE A 171 ? 0.1843 0.2317 0.1803 0.0086  -0.0274 0.0291  172 PHE A CE2 
1368 C CZ  . PHE A 171 ? 0.1767 0.2271 0.1763 0.0063  -0.0260 0.0271  172 PHE A CZ  
1369 N N   . ASP A 172 ? 0.2106 0.2710 0.1983 0.0114  -0.0432 0.0365  173 ASP A N   
1370 C CA  . ASP A 172 ? 0.2084 0.2715 0.2024 0.0166  -0.0438 0.0400  173 ASP A CA  
1371 C C   . ASP A 172 ? 0.2206 0.2962 0.2241 0.0171  -0.0479 0.0400  173 ASP A C   
1372 O O   . ASP A 172 ? 0.2057 0.2859 0.2182 0.0204  -0.0467 0.0410  173 ASP A O   
1373 C CB  . ASP A 172 ? 0.2446 0.3027 0.2319 0.0206  -0.0451 0.0450  173 ASP A CB  
1374 C CG  . ASP A 172 ? 0.3078 0.3720 0.2896 0.0206  -0.0510 0.0470  173 ASP A CG  
1375 O OD1 . ASP A 172 ? 0.2899 0.3540 0.2643 0.0164  -0.0519 0.0442  173 ASP A OD1 
1376 O OD2 . ASP A 172 ? 0.3073 0.3771 0.2921 0.0252  -0.0549 0.0511  173 ASP A OD2 
1377 N N   . GLN A 173 ? 0.1822 0.2639 0.1842 0.0137  -0.0525 0.0384  174 GLN A N   
1378 C CA  . GLN A 173 ? 0.2076 0.3022 0.2199 0.0130  -0.0568 0.0380  174 GLN A CA  
1379 C C   . GLN A 173 ? 0.2010 0.2987 0.2226 0.0089  -0.0539 0.0349  174 GLN A C   
1380 O O   . GLN A 173 ? 0.2047 0.3125 0.2379 0.0097  -0.0545 0.0359  174 GLN A O   
1381 C CB  . GLN A 173 ? 0.1920 0.2919 0.1991 0.0104  -0.0634 0.0366  174 GLN A CB  
1382 C CG  . GLN A 173 ? 0.2366 0.3362 0.2353 0.0155  -0.0669 0.0414  174 GLN A CG  
1383 C CD  . GLN A 173 ? 0.2912 0.3979 0.2991 0.0220  -0.0685 0.0463  174 GLN A CD  
1384 O OE1 . GLN A 173 ? 0.3366 0.4566 0.3544 0.0222  -0.0731 0.0463  174 GLN A OE1 
1385 N NE2 . GLN A 173 ? 0.3321 0.4301 0.3376 0.0272  -0.0647 0.0503  174 GLN A NE2 
1386 N N   . VAL A 174 ? 0.1666 0.2562 0.1837 0.0050  -0.0503 0.0318  175 VAL A N   
1387 C CA  . VAL A 174 ? 0.1736 0.2649 0.1989 0.0018  -0.0469 0.0303  175 VAL A CA  
1388 C C   . VAL A 174 ? 0.1836 0.2784 0.2158 0.0062  -0.0431 0.0330  175 VAL A C   
1389 O O   . VAL A 174 ? 0.1760 0.2798 0.2189 0.0054  -0.0423 0.0338  175 VAL A O   
1390 C CB  . VAL A 174 ? 0.2119 0.2929 0.2306 -0.0013 -0.0432 0.0274  175 VAL A CB  
1391 C CG1 . VAL A 174 ? 0.2080 0.2902 0.2344 -0.0031 -0.0391 0.0275  175 VAL A CG1 
1392 C CG2 . VAL A 174 ? 0.2269 0.3057 0.2406 -0.0058 -0.0467 0.0236  175 VAL A CG2 
1393 N N   . LEU A 175 ? 0.1709 0.2589 0.1976 0.0108  -0.0405 0.0342  176 LEU A N   
1394 C CA  . LEU A 175 ? 0.1726 0.2628 0.2046 0.0154  -0.0368 0.0354  176 LEU A CA  
1395 C C   . LEU A 175 ? 0.1792 0.2789 0.2188 0.0202  -0.0394 0.0381  176 LEU A C   
1396 O O   . LEU A 175 ? 0.1747 0.2839 0.2240 0.0218  -0.0376 0.0387  176 LEU A O   
1397 C CB  . LEU A 175 ? 0.1487 0.2276 0.1730 0.0181  -0.0334 0.0349  176 LEU A CB  
1398 C CG  . LEU A 175 ? 0.1541 0.2259 0.1732 0.0144  -0.0301 0.0323  176 LEU A CG  
1399 C CD1 . LEU A 175 ? 0.1769 0.2401 0.1912 0.0170  -0.0269 0.0312  176 LEU A CD1 
1400 C CD2 . LEU A 175 ? 0.1633 0.2407 0.1881 0.0118  -0.0278 0.0315  176 LEU A CD2 
1401 N N   . GLU A 176 ? 0.1936 0.2920 0.2293 0.0229  -0.0435 0.0402  177 GLU A N   
1402 C CA  . GLU A 176 ? 0.2020 0.3086 0.2451 0.0290  -0.0457 0.0432  177 GLU A CA  
1403 C C   . GLU A 176 ? 0.1954 0.3178 0.2491 0.0271  -0.0500 0.0437  177 GLU A C   
1404 O O   . GLU A 176 ? 0.2102 0.3431 0.2742 0.0318  -0.0503 0.0457  177 GLU A O   
1405 C CB  . GLU A 176 ? 0.2194 0.3190 0.2548 0.0332  -0.0487 0.0464  177 GLU A CB  
1406 C CG  . GLU A 176 ? 0.2109 0.2957 0.2389 0.0354  -0.0440 0.0462  177 GLU A CG  
1407 C CD  . GLU A 176 ? 0.2453 0.3219 0.2666 0.0395  -0.0461 0.0505  177 GLU A CD  
1408 O OE1 . GLU A 176 ? 0.2661 0.3484 0.2862 0.0410  -0.0514 0.0540  177 GLU A OE1 
1409 O OE2 . GLU A 176 ? 0.2346 0.2989 0.2516 0.0412  -0.0424 0.0506  177 GLU A OE2 
1410 N N   . LYS A 177 ? 0.1696 0.2944 0.2222 0.0203  -0.0532 0.0417  178 LYS A N   
1411 C CA  . LYS A 177 ? 0.2037 0.3436 0.2675 0.0174  -0.0577 0.0416  178 LYS A CA  
1412 C C   . LYS A 177 ? 0.1688 0.3140 0.2421 0.0118  -0.0543 0.0398  178 LYS A C   
1413 O O   . LYS A 177 ? 0.2057 0.3653 0.2924 0.0107  -0.0558 0.0408  178 LYS A O   
1414 C CB  . LYS A 177 ? 0.2420 0.3825 0.2995 0.0134  -0.0646 0.0399  178 LYS A CB  
1415 C CG  . LYS A 177 ? 0.3164 0.4568 0.3670 0.0193  -0.0693 0.0433  178 LYS A CG  
1416 C CD  . LYS A 177 ? 0.3965 0.5526 0.4599 0.0242  -0.0731 0.0465  178 LYS A CD  
1417 C CE  . LYS A 177 ? 0.4330 0.5856 0.4915 0.0331  -0.0743 0.0516  178 LYS A CE  
1418 N NZ  . LYS A 177 ? 0.4257 0.5713 0.4693 0.0328  -0.0786 0.0528  178 LYS A NZ  
1419 N N   . THR A 178 ? 0.1797 0.3144 0.2472 0.0082  -0.0497 0.0379  179 THR A N   
1420 C CA  . THR A 178 ? 0.1641 0.3024 0.2396 0.0028  -0.0464 0.0372  179 THR A CA  
1421 C C   . THR A 178 ? 0.1607 0.2972 0.2371 0.0057  -0.0391 0.0387  179 THR A C   
1422 O O   . THR A 178 ? 0.1786 0.3259 0.2659 0.0059  -0.0361 0.0408  179 THR A O   
1423 C CB  . THR A 178 ? 0.2106 0.3394 0.2798 -0.0041 -0.0475 0.0338  179 THR A CB  
1424 O OG1 . THR A 178 ? 0.2410 0.3716 0.3074 -0.0064 -0.0545 0.0315  179 THR A OG1 
1425 C CG2 . THR A 178 ? 0.1842 0.3168 0.2635 -0.0101 -0.0449 0.0340  179 THR A CG2 
1426 N N   . ILE A 179 ? 0.1567 0.2807 0.2220 0.0079  -0.0359 0.0376  180 ILE A N   
1427 C CA  . ILE A 179 ? 0.1651 0.2874 0.2301 0.0095  -0.0296 0.0381  180 ILE A CA  
1428 C C   . ILE A 179 ? 0.1628 0.2911 0.2313 0.0167  -0.0268 0.0392  180 ILE A C   
1429 O O   . ILE A 179 ? 0.1409 0.2778 0.2161 0.0178  -0.0226 0.0406  180 ILE A O   
1430 C CB  . ILE A 179 ? 0.1760 0.2841 0.2289 0.0088  -0.0277 0.0359  180 ILE A CB  
1431 C CG1 . ILE A 179 ? 0.1818 0.2846 0.2324 0.0023  -0.0295 0.0345  180 ILE A CG1 
1432 C CG2 . ILE A 179 ? 0.1646 0.2721 0.2163 0.0111  -0.0220 0.0362  180 ILE A CG2 
1433 C CD1 . ILE A 179 ? 0.1777 0.2865 0.2375 -0.0025 -0.0277 0.0361  180 ILE A CD1 
1434 N N   . PHE A 180 ? 0.1598 0.2834 0.2237 0.0220  -0.0287 0.0388  181 PHE A N   
1435 C CA  . PHE A 180 ? 0.1926 0.3209 0.2606 0.0294  -0.0261 0.0392  181 PHE A CA  
1436 C C   . PHE A 180 ? 0.1828 0.3282 0.2647 0.0309  -0.0264 0.0415  181 PHE A C   
1437 O O   . PHE A 180 ? 0.2248 0.3775 0.3118 0.0347  -0.0215 0.0416  181 PHE A O   
1438 C CB  . PHE A 180 ? 0.1607 0.2804 0.2230 0.0347  -0.0287 0.0391  181 PHE A CB  
1439 C CG  . PHE A 180 ? 0.1788 0.2827 0.2292 0.0339  -0.0274 0.0370  181 PHE A CG  
1440 C CD1 . PHE A 180 ? 0.1707 0.2698 0.2164 0.0312  -0.0234 0.0345  181 PHE A CD1 
1441 C CD2 . PHE A 180 ? 0.1950 0.2896 0.2393 0.0361  -0.0302 0.0380  181 PHE A CD2 
1442 C CE1 . PHE A 180 ? 0.1797 0.2659 0.2160 0.0304  -0.0224 0.0324  181 PHE A CE1 
1443 C CE2 . PHE A 180 ? 0.2025 0.2833 0.2372 0.0350  -0.0286 0.0364  181 PHE A CE2 
1444 C CZ  . PHE A 180 ? 0.2046 0.2818 0.2359 0.0319  -0.0249 0.0332  181 PHE A CZ  
1445 N N   . PRO A 181 ? 0.1452 0.2986 0.2338 0.0280  -0.0318 0.0432  182 PRO A N   
1446 C CA  . PRO A 181 ? 0.1719 0.3435 0.2757 0.0289  -0.0318 0.0454  182 PRO A CA  
1447 C C   . PRO A 181 ? 0.1943 0.3735 0.3050 0.0239  -0.0269 0.0463  182 PRO A C   
1448 O O   . PRO A 181 ? 0.2089 0.4016 0.3302 0.0268  -0.0231 0.0481  182 PRO A O   
1449 C CB  . PRO A 181 ? 0.1800 0.3569 0.2875 0.0254  -0.0397 0.0460  182 PRO A CB  
1450 C CG  . PRO A 181 ? 0.1491 0.3117 0.2430 0.0272  -0.0433 0.0451  182 PRO A CG  
1451 C CD  . PRO A 181 ? 0.1609 0.3087 0.2436 0.0254  -0.0384 0.0429  182 PRO A CD  
1452 N N   . ALA A 182 ? 0.1513 0.3224 0.2568 0.0167  -0.0265 0.0456  183 ALA A N   
1453 C CA  . ALA A 182 ? 0.1487 0.3257 0.2606 0.0120  -0.0216 0.0476  183 ALA A CA  
1454 C C   . ALA A 182 ? 0.1920 0.3701 0.3008 0.0172  -0.0142 0.0483  183 ALA A C   
1455 O O   . ALA A 182 ? 0.1759 0.3651 0.2930 0.0161  -0.0093 0.0513  183 ALA A O   
1456 C CB  . ALA A 182 ? 0.1592 0.3251 0.2653 0.0044  -0.0227 0.0467  183 ALA A CB  
1457 N N   . LEU A 183 ? 0.1570 0.3239 0.2540 0.0226  -0.0132 0.0454  184 LEU A N   
1458 C CA  . LEU A 183 ? 0.2004 0.3672 0.2925 0.0279  -0.0071 0.0444  184 LEU A CA  
1459 C C   . LEU A 183 ? 0.2202 0.3963 0.3181 0.0362  -0.0051 0.0437  184 LEU A C   
1460 O O   . LEU A 183 ? 0.2570 0.4339 0.3510 0.0414  0.0000  0.0418  184 LEU A O   
1461 C CB  . LEU A 183 ? 0.2162 0.3664 0.2938 0.0290  -0.0074 0.0408  184 LEU A CB  
1462 C CG  . LEU A 183 ? 0.1632 0.3038 0.2340 0.0224  -0.0082 0.0410  184 LEU A CG  
1463 C CD1 . LEU A 183 ? 0.1779 0.3035 0.2365 0.0235  -0.0099 0.0373  184 LEU A CD1 
1464 C CD2 . LEU A 183 ? 0.1863 0.3318 0.2572 0.0208  -0.0027 0.0435  184 LEU A CD2 
1465 N N   . GLY A 184 ? 0.1735 0.3568 0.2804 0.0379  -0.0093 0.0448  185 GLY A N   
1466 C CA  . GLY A 184 ? 0.2640 0.4565 0.3779 0.0465  -0.0077 0.0444  185 GLY A CA  
1467 C C   . GLY A 184 ? 0.2985 0.4782 0.4037 0.0538  -0.0084 0.0408  185 GLY A C   
1468 O O   . GLY A 184 ? 0.3025 0.4868 0.4110 0.0620  -0.0051 0.0391  185 GLY A O   
1469 N N   . LEU A 185 ? 0.2000 0.3637 0.2946 0.0513  -0.0124 0.0395  186 LEU A N   
1470 C CA  . LEU A 185 ? 0.2263 0.3761 0.3128 0.0572  -0.0129 0.0365  186 LEU A CA  
1471 C C   . LEU A 185 ? 0.2518 0.4020 0.3429 0.0615  -0.0181 0.0389  186 LEU A C   
1472 O O   . LEU A 185 ? 0.3278 0.4815 0.4214 0.0573  -0.0235 0.0419  186 LEU A O   
1473 C CB  . LEU A 185 ? 0.1998 0.3329 0.2732 0.0523  -0.0140 0.0345  186 LEU A CB  
1474 C CG  . LEU A 185 ? 0.2308 0.3632 0.2990 0.0474  -0.0101 0.0330  186 LEU A CG  
1475 C CD1 . LEU A 185 ? 0.2611 0.3776 0.3176 0.0441  -0.0114 0.0307  186 LEU A CD1 
1476 C CD2 . LEU A 185 ? 0.2468 0.3861 0.3161 0.0524  -0.0040 0.0306  186 LEU A CD2 
1477 N N   . LYS A 186 ? 0.2319 0.3782 0.3239 0.0702  -0.0168 0.0374  187 LYS A N   
1478 C CA  . LYS A 186 ? 0.2634 0.4113 0.3611 0.0762  -0.0212 0.0405  187 LYS A CA  
1479 C C   . LYS A 186 ? 0.2662 0.3952 0.3544 0.0784  -0.0239 0.0407  187 LYS A C   
1480 O O   . LYS A 186 ? 0.2382 0.3669 0.3282 0.0810  -0.0291 0.0449  187 LYS A O   
1481 C CB  . LYS A 186 ? 0.3368 0.4953 0.4452 0.0859  -0.0176 0.0396  187 LYS A CB  
1482 C CG  . LYS A 186 ? 0.4139 0.5938 0.5341 0.0844  -0.0147 0.0406  187 LYS A CG  
1483 C CD  . LYS A 186 ? 0.4216 0.6131 0.5490 0.0778  -0.0206 0.0452  187 LYS A CD  
1484 C CE  . LYS A 186 ? 0.4759 0.6903 0.6188 0.0771  -0.0180 0.0471  187 LYS A CE  
1485 N NZ  . LYS A 186 ? 0.5417 0.7682 0.6938 0.0717  -0.0249 0.0509  187 LYS A NZ  
1486 N N   . HIS A 187 ? 0.2097 0.3238 0.2882 0.0774  -0.0207 0.0366  188 HIS A N   
1487 C CA  . HIS A 187 ? 0.2199 0.3155 0.2908 0.0795  -0.0221 0.0367  188 HIS A CA  
1488 C C   . HIS A 187 ? 0.2678 0.3511 0.3274 0.0720  -0.0208 0.0338  188 HIS A C   
1489 O O   . HIS A 187 ? 0.2345 0.3042 0.2888 0.0731  -0.0185 0.0302  188 HIS A O   
1490 C CB  . HIS A 187 ? 0.2574 0.3471 0.3319 0.0890  -0.0189 0.0338  188 HIS A CB  
1491 C CG  . HIS A 187 ? 0.3119 0.4136 0.3982 0.0975  -0.0203 0.0370  188 HIS A CG  
1492 N ND1 . HIS A 187 ? 0.3499 0.4496 0.4385 0.1012  -0.0256 0.0432  188 HIS A ND1 
1493 C CD2 . HIS A 187 ? 0.3182 0.4351 0.4148 0.1032  -0.0171 0.0354  188 HIS A CD2 
1494 C CE1 . HIS A 187 ? 0.3021 0.4155 0.4028 0.1090  -0.0260 0.0450  188 HIS A CE1 
1495 N NE2 . HIS A 187 ? 0.3337 0.4578 0.4398 0.1103  -0.0206 0.0402  188 HIS A NE2 
1496 N N   . SER A 188 ? 0.2277 0.3164 0.2848 0.0642  -0.0224 0.0351  189 SER A N   
1497 C CA  . SER A 188 ? 0.1936 0.2723 0.2409 0.0571  -0.0221 0.0334  189 SER A CA  
1498 C C   . SER A 188 ? 0.2154 0.2903 0.2582 0.0532  -0.0269 0.0377  189 SER A C   
1499 O O   . SER A 188 ? 0.2318 0.3168 0.2788 0.0526  -0.0307 0.0410  189 SER A O   
1500 C CB  . SER A 188 ? 0.1901 0.2770 0.2376 0.0518  -0.0195 0.0313  189 SER A CB  
1501 O OG  . SER A 188 ? 0.1990 0.2905 0.2494 0.0560  -0.0149 0.0276  189 SER A OG  
1502 N N   . TYR A 189 ? 0.2125 0.2735 0.2465 0.0506  -0.0268 0.0375  190 TYR A N   
1503 C CA  . TYR A 189 ? 0.2206 0.2767 0.2490 0.0485  -0.0307 0.0420  190 TYR A CA  
1504 C C   . TYR A 189 ? 0.2173 0.2642 0.2366 0.0420  -0.0294 0.0405  190 TYR A C   
1505 O O   . TYR A 189 ? 0.2384 0.2778 0.2555 0.0407  -0.0259 0.0368  190 TYR A O   
1506 C CB  . TYR A 189 ? 0.2115 0.2587 0.2395 0.0546  -0.0318 0.0458  190 TYR A CB  
1507 C CG  . TYR A 189 ? 0.2164 0.2716 0.2540 0.0625  -0.0328 0.0473  190 TYR A CG  
1508 C CD1 . TYR A 189 ? 0.2561 0.3235 0.2982 0.0644  -0.0377 0.0517  190 TYR A CD1 
1509 C CD2 . TYR A 189 ? 0.2440 0.2955 0.2865 0.0683  -0.0291 0.0439  190 TYR A CD2 
1510 C CE1 . TYR A 189 ? 0.2505 0.3270 0.3027 0.0720  -0.0386 0.0533  190 TYR A CE1 
1511 C CE2 . TYR A 189 ? 0.2492 0.3088 0.3012 0.0764  -0.0296 0.0451  190 TYR A CE2 
1512 C CZ  . TYR A 189 ? 0.2681 0.3406 0.3254 0.0782  -0.0343 0.0501  190 TYR A CZ  
1513 O OH  . TYR A 189 ? 0.2999 0.3822 0.3680 0.0866  -0.0348 0.0516  190 TYR A OH  
1514 N N   . VAL A 190 ? 0.2016 0.2496 0.2157 0.0381  -0.0326 0.0432  191 VAL A N   
1515 C CA  . VAL A 190 ? 0.2256 0.2636 0.2306 0.0337  -0.0315 0.0435  191 VAL A CA  
1516 C C   . VAL A 190 ? 0.2445 0.2731 0.2454 0.0369  -0.0324 0.0486  191 VAL A C   
1517 O O   . VAL A 190 ? 0.2718 0.2891 0.2687 0.0354  -0.0295 0.0487  191 VAL A O   
1518 C CB  . VAL A 190 ? 0.1915 0.2348 0.1920 0.0282  -0.0336 0.0430  191 VAL A CB  
1519 C CG1 . VAL A 190 ? 0.2280 0.2625 0.2191 0.0245  -0.0323 0.0438  191 VAL A CG1 
1520 C CG2 . VAL A 190 ? 0.2239 0.2734 0.2287 0.0248  -0.0318 0.0385  191 VAL A CG2 
1521 N N   . ASN A 191 ? 0.2386 0.2723 0.2410 0.0413  -0.0364 0.0534  192 ASN A N   
1522 C CA  . ASN A 191 ? 0.2517 0.2772 0.2511 0.0457  -0.0376 0.0597  192 ASN A CA  
1523 C C   . ASN A 191 ? 0.2697 0.2975 0.2783 0.0537  -0.0385 0.0611  192 ASN A C   
1524 O O   . ASN A 191 ? 0.2945 0.3355 0.3092 0.0564  -0.0419 0.0616  192 ASN A O   
1525 C CB  . ASN A 191 ? 0.2770 0.3072 0.2688 0.0447  -0.0421 0.0648  192 ASN A CB  
1526 C CG  . ASN A 191 ? 0.3055 0.3338 0.2882 0.0374  -0.0408 0.0627  192 ASN A CG  
1527 O OD1 . ASN A 191 ? 0.3448 0.3823 0.3259 0.0338  -0.0432 0.0598  192 ASN A OD1 
1528 N ND2 . ASN A 191 ? 0.2848 0.3012 0.2624 0.0351  -0.0366 0.0636  192 ASN A ND2 
1529 N N   . VAL A 192 ? 0.2613 0.2768 0.2720 0.0574  -0.0353 0.0611  193 VAL A N   
1530 C CA  . VAL A 192 ? 0.2507 0.2669 0.2704 0.0658  -0.0354 0.0617  193 VAL A CA  
1531 C C   . VAL A 192 ? 0.2905 0.3076 0.3097 0.0716  -0.0400 0.0703  193 VAL A C   
1532 O O   . VAL A 192 ? 0.3226 0.3284 0.3347 0.0713  -0.0401 0.0761  193 VAL A O   
1533 C CB  . VAL A 192 ? 0.2841 0.2850 0.3059 0.0678  -0.0308 0.0581  193 VAL A CB  
1534 C CG1 . VAL A 192 ? 0.2778 0.2785 0.3088 0.0775  -0.0306 0.0581  193 VAL A CG1 
1535 C CG2 . VAL A 192 ? 0.2807 0.2823 0.3020 0.0621  -0.0270 0.0495  193 VAL A CG2 
1536 N N   . PRO A 193 ? 0.3121 0.3432 0.3387 0.0770  -0.0438 0.0720  194 PRO A N   
1537 C CA  . PRO A 193 ? 0.3223 0.3561 0.3483 0.0830  -0.0489 0.0807  194 PRO A CA  
1538 C C   . PRO A 193 ? 0.3754 0.3946 0.4043 0.0912  -0.0472 0.0851  194 PRO A C   
1539 O O   . PRO A 193 ? 0.3635 0.3736 0.3977 0.0936  -0.0426 0.0802  194 PRO A O   
1540 C CB  . PRO A 193 ? 0.3261 0.3804 0.3620 0.0862  -0.0530 0.0797  194 PRO A CB  
1541 C CG  . PRO A 193 ? 0.3392 0.3962 0.3837 0.0865  -0.0481 0.0721  194 PRO A CG  
1542 C CD  . PRO A 193 ? 0.2872 0.3330 0.3238 0.0783  -0.0433 0.0667  194 PRO A CD  
1543 N N   . LYS A 194 ? 0.3710 0.3877 0.3959 0.0957  -0.0512 0.0946  195 LYS A N   
1544 C CA  . LYS A 194 ? 0.3681 0.3697 0.3959 0.1039  -0.0499 0.1004  195 LYS A CA  
1545 C C   . LYS A 194 ? 0.3737 0.3795 0.4154 0.1132  -0.0491 0.0971  195 LYS A C   
1546 O O   . LYS A 194 ? 0.3870 0.3773 0.4330 0.1183  -0.0453 0.0964  195 LYS A O   
1547 C CB  . LYS A 194 ? 0.3956 0.3971 0.4169 0.1081  -0.0551 0.1124  195 LYS A CB  
1548 C CG  . LYS A 194 ? 0.5888 0.5684 0.6080 0.1128  -0.0524 0.1200  195 LYS A CG  
1549 C CD  . LYS A 194 ? 0.5944 0.5576 0.6052 0.1036  -0.0468 0.1181  195 LYS A CD  
1550 C CE  . LYS A 194 ? 0.6361 0.5765 0.6520 0.1069  -0.0417 0.1186  195 LYS A CE  
1551 N NZ  . LYS A 194 ? 0.6913 0.6167 0.7002 0.0974  -0.0366 0.1175  195 LYS A NZ  
1552 N N   . THR A 195 ? 0.3542 0.3810 0.4037 0.1153  -0.0524 0.0948  196 THR A N   
1553 C CA  . THR A 195 ? 0.4214 0.4559 0.4848 0.1242  -0.0513 0.0917  196 THR A CA  
1554 C C   . THR A 195 ? 0.4066 0.4342 0.4739 0.1228  -0.0443 0.0814  196 THR A C   
1555 O O   . THR A 195 ? 0.3719 0.4018 0.4496 0.1311  -0.0420 0.0783  196 THR A O   
1556 C CB  . THR A 195 ? 0.3799 0.4405 0.4512 0.1247  -0.0559 0.0911  196 THR A CB  
1557 O OG1 . THR A 195 ? 0.4317 0.5004 0.4979 0.1135  -0.0556 0.0857  196 THR A OG1 
1558 C CG2 . THR A 195 ? 0.4695 0.5371 0.5391 0.1270  -0.0633 0.0988  196 THR A CG2 
1559 N N   . GLN A 196 ? 0.3530 0.3732 0.4120 0.1131  -0.0409 0.0761  197 GLN A N   
1560 C CA  . GLN A 196 ? 0.3520 0.3659 0.4128 0.1111  -0.0349 0.0663  197 GLN A CA  
1561 C C   . GLN A 196 ? 0.3956 0.3859 0.4505 0.1089  -0.0313 0.0649  197 GLN A C   
1562 O O   . GLN A 196 ? 0.3491 0.3333 0.4045 0.1069  -0.0268 0.0562  197 GLN A O   
1563 C CB  . GLN A 196 ? 0.2652 0.2909 0.3227 0.1016  -0.0338 0.0604  197 GLN A CB  
1564 C CG  . GLN A 196 ? 0.3098 0.3584 0.3761 0.1033  -0.0354 0.0592  197 GLN A CG  
1565 C CD  . GLN A 196 ? 0.3234 0.3768 0.4001 0.1115  -0.0315 0.0541  197 GLN A CD  
1566 O OE1 . GLN A 196 ? 0.2959 0.3396 0.3713 0.1118  -0.0264 0.0472  197 GLN A OE1 
1567 N NE2 . GLN A 196 ? 0.3045 0.3740 0.3919 0.1184  -0.0338 0.0572  197 GLN A NE2 
1568 N N   . MET A 197 ? 0.3937 0.3710 0.4430 0.1088  -0.0331 0.0732  198 MET A N   
1569 C CA  . MET A 197 ? 0.4343 0.3900 0.4783 0.1044  -0.0295 0.0722  198 MET A CA  
1570 C C   . MET A 197 ? 0.3966 0.3382 0.4478 0.1104  -0.0255 0.0660  198 MET A C   
1571 O O   . MET A 197 ? 0.4068 0.3349 0.4558 0.1051  -0.0218 0.0598  198 MET A O   
1572 C CB  . MET A 197 ? 0.4991 0.4441 0.5365 0.1040  -0.0317 0.0837  198 MET A CB  
1573 C CG  . MET A 197 ? 0.5461 0.4985 0.5727 0.0949  -0.0338 0.0873  198 MET A CG  
1574 S SD  . MET A 197 ? 0.6897 0.6380 0.7105 0.0824  -0.0292 0.0783  198 MET A SD  
1575 C CE  . MET A 197 ? 0.5429 0.5055 0.5533 0.0752  -0.0327 0.0825  198 MET A CE  
1576 N N   . GLN A 198 ? 0.3765 0.3216 0.4368 0.1213  -0.0262 0.0666  199 GLN A N   
1577 C CA  . GLN A 198 ? 0.3956 0.3277 0.4629 0.1279  -0.0222 0.0595  199 GLN A CA  
1578 C C   . GLN A 198 ? 0.3755 0.3147 0.4437 0.1248  -0.0184 0.0464  199 GLN A C   
1579 O O   . GLN A 198 ? 0.4181 0.3450 0.4895 0.1279  -0.0147 0.0381  199 GLN A O   
1580 C CB  . GLN A 198 ? 0.4415 0.3778 0.5189 0.1415  -0.0237 0.0635  199 GLN A CB  
1581 C CG  . GLN A 198 ? 0.4874 0.4503 0.5711 0.1453  -0.0252 0.0614  199 GLN A CG  
1582 C CD  . GLN A 198 ? 0.5039 0.4847 0.5844 0.1415  -0.0309 0.0699  199 GLN A CD  
1583 O OE1 . GLN A 198 ? 0.5199 0.4953 0.5910 0.1342  -0.0332 0.0757  199 GLN A OE1 
1584 N NE2 . GLN A 198 ? 0.5529 0.5558 0.6417 0.1465  -0.0331 0.0702  199 GLN A NE2 
1585 N N   . ASN A 199 ? 0.3282 0.2869 0.3937 0.1191  -0.0193 0.0443  200 ASN A N   
1586 C CA  . ASN A 199 ? 0.3234 0.2903 0.3882 0.1155  -0.0158 0.0335  200 ASN A CA  
1587 C C   . ASN A 199 ? 0.3123 0.2745 0.3681 0.1037  -0.0150 0.0302  200 ASN A C   
1588 O O   . ASN A 199 ? 0.2844 0.2522 0.3385 0.1004  -0.0124 0.0216  200 ASN A O   
1589 C CB  . ASN A 199 ? 0.2957 0.2876 0.3646 0.1168  -0.0168 0.0337  200 ASN A CB  
1590 C CG  . ASN A 199 ? 0.3491 0.3494 0.4287 0.1285  -0.0171 0.0355  200 ASN A CG  
1591 O OD1 . ASN A 199 ? 0.3437 0.3334 0.4281 0.1365  -0.0143 0.0313  200 ASN A OD1 
1592 N ND2 . ASN A 199 ? 0.3405 0.3600 0.4248 0.1298  -0.0205 0.0415  200 ASN A ND2 
1593 N N   . TYR A 200 ? 0.3077 0.2609 0.3576 0.0978  -0.0170 0.0371  201 TYR A N   
1594 C CA  . TYR A 200 ? 0.3231 0.2740 0.3653 0.0869  -0.0164 0.0351  201 TYR A CA  
1595 C C   . TYR A 200 ? 0.3406 0.2725 0.3823 0.0843  -0.0133 0.0288  201 TYR A C   
1596 O O   . TYR A 200 ? 0.3634 0.2783 0.4060 0.0854  -0.0131 0.0333  201 TYR A O   
1597 C CB  . TYR A 200 ? 0.3535 0.3046 0.3898 0.0824  -0.0195 0.0452  201 TYR A CB  
1598 C CG  . TYR A 200 ? 0.3275 0.2802 0.3562 0.0718  -0.0190 0.0440  201 TYR A CG  
1599 C CD1 . TYR A 200 ? 0.3613 0.3151 0.3889 0.0665  -0.0164 0.0349  201 TYR A CD1 
1600 C CD2 . TYR A 200 ? 0.3897 0.3434 0.4120 0.0675  -0.0212 0.0520  201 TYR A CD2 
1601 C CE1 . TYR A 200 ? 0.3713 0.3270 0.3930 0.0576  -0.0160 0.0343  201 TYR A CE1 
1602 C CE2 . TYR A 200 ? 0.3922 0.3474 0.4081 0.0587  -0.0204 0.0508  201 TYR A CE2 
1603 C CZ  . TYR A 200 ? 0.3898 0.3461 0.4060 0.0538  -0.0178 0.0421  201 TYR A CZ  
1604 O OH  . TYR A 200 ? 0.3359 0.2943 0.3466 0.0457  -0.0171 0.0414  201 TYR A OH  
1605 N N   . ALA A 201 ? 0.2899 0.2250 0.3305 0.0806  -0.0111 0.0186  202 ALA A N   
1606 C CA  . ALA A 201 ? 0.3552 0.2740 0.3965 0.0785  -0.0087 0.0107  202 ALA A CA  
1607 C C   . ALA A 201 ? 0.3692 0.2752 0.4070 0.0698  -0.0088 0.0150  202 ALA A C   
1608 O O   . ALA A 201 ? 0.3624 0.2757 0.3951 0.0636  -0.0101 0.0206  202 ALA A O   
1609 C CB  . ALA A 201 ? 0.3363 0.2640 0.3757 0.0760  -0.0070 -0.0007 202 ALA A CB  
1610 N N   . PHE A 202 ? 0.4256 0.3121 0.4666 0.0694  -0.0073 0.0123  203 PHE A N   
1611 C CA  . PHE A 202 ? 0.4135 0.2887 0.4526 0.0599  -0.0066 0.0143  203 PHE A CA  
1612 C C   . PHE A 202 ? 0.4257 0.3064 0.4631 0.0526  -0.0058 0.0035  203 PHE A C   
1613 O O   . PHE A 202 ? 0.4376 0.3210 0.4765 0.0556  -0.0053 -0.0072 203 PHE A O   
1614 C CB  . PHE A 202 ? 0.4607 0.3121 0.5052 0.0613  -0.0051 0.0159  203 PHE A CB  
1615 C CG  . PHE A 202 ? 0.5052 0.3498 0.5514 0.0689  -0.0059 0.0278  203 PHE A CG  
1616 C CD1 . PHE A 202 ? 0.5798 0.4386 0.6214 0.0712  -0.0083 0.0377  203 PHE A CD1 
1617 C CD2 . PHE A 202 ? 0.5943 0.4181 0.6468 0.0740  -0.0046 0.0290  203 PHE A CD2 
1618 C CE1 . PHE A 202 ? 0.6059 0.4600 0.6488 0.0786  -0.0098 0.0487  203 PHE A CE1 
1619 C CE2 . PHE A 202 ? 0.6372 0.4549 0.6913 0.0819  -0.0057 0.0408  203 PHE A CE2 
1620 C CZ  . PHE A 202 ? 0.6327 0.4665 0.6818 0.0842  -0.0085 0.0508  203 PHE A CZ  
1621 N N   . GLY A 203 ? 0.3952 0.2787 0.4290 0.0434  -0.0059 0.0064  204 GLY A N   
1622 C CA  . GLY A 203 ? 0.4470 0.3347 0.4800 0.0359  -0.0056 -0.0026 204 GLY A CA  
1623 C C   . GLY A 203 ? 0.4885 0.3589 0.5262 0.0295  -0.0042 -0.0052 204 GLY A C   
1624 O O   . GLY A 203 ? 0.5020 0.3596 0.5418 0.0279  -0.0031 0.0034  204 GLY A O   
1625 N N   . TYR A 204 ? 0.4368 0.3076 0.4765 0.0255  -0.0044 -0.0169 205 TYR A N   
1626 C CA  . TYR A 204 ? 0.4717 0.3258 0.5177 0.0196  -0.0035 -0.0221 205 TYR A CA  
1627 C C   . TYR A 204 ? 0.5385 0.4008 0.5847 0.0095  -0.0042 -0.0269 205 TYR A C   
1628 O O   . TYR A 204 ? 0.4788 0.3566 0.5214 0.0094  -0.0058 -0.0340 205 TYR A O   
1629 C CB  . TYR A 204 ? 0.5074 0.3516 0.5572 0.0251  -0.0036 -0.0338 205 TYR A CB  
1630 C CG  . TYR A 204 ? 0.4805 0.3135 0.5323 0.0349  -0.0026 -0.0282 205 TYR A CG  
1631 C CD1 . TYR A 204 ? 0.4283 0.2738 0.4766 0.0444  -0.0031 -0.0265 205 TYR A CD1 
1632 C CD2 . TYR A 204 ? 0.5329 0.3437 0.5911 0.0347  -0.0012 -0.0238 205 TYR A CD2 
1633 C CE1 . TYR A 204 ? 0.4437 0.2806 0.4950 0.0539  -0.0024 -0.0211 205 TYR A CE1 
1634 C CE2 . TYR A 204 ? 0.5245 0.3253 0.5850 0.0445  -0.0005 -0.0180 205 TYR A CE2 
1635 C CZ  . TYR A 204 ? 0.4710 0.2855 0.5281 0.0542  -0.0013 -0.0168 205 TYR A CZ  
1636 O OH  . TYR A 204 ? 0.4750 0.2808 0.5356 0.0644  -0.0008 -0.0109 205 TYR A OH  
1637 N N   . ASN A 205 ? 0.6193 0.4719 0.6702 0.0014  -0.0027 -0.0223 206 ASN A N   
1638 C CA  . ASN A 205 ? 0.6884 0.5492 0.7414 -0.0084 -0.0031 -0.0257 206 ASN A CA  
1639 C C   . ASN A 205 ? 0.7364 0.5920 0.7955 -0.0123 -0.0047 -0.0400 206 ASN A C   
1640 O O   . ASN A 205 ? 0.7340 0.5814 0.7939 -0.0067 -0.0055 -0.0483 206 ASN A O   
1641 C CB  . ASN A 205 ? 0.7103 0.5646 0.7664 -0.0155 -0.0003 -0.0146 206 ASN A CB  
1642 C CG  . ASN A 205 ? 0.7974 0.6284 0.8609 -0.0172 0.0019  -0.0116 206 ASN A CG  
1643 O OD1 . ASN A 205 ? 0.7977 0.6163 0.8658 -0.0145 0.0010  -0.0202 206 ASN A OD1 
1644 N ND2 . ASN A 205 ? 0.8031 0.6276 0.8678 -0.0215 0.0049  0.0007  206 ASN A ND2 
1645 N N   . GLN A 206 ? 0.8140 0.6748 0.8776 -0.0218 -0.0053 -0.0437 207 GLN A N   
1646 C CA  . GLN A 206 ? 0.8354 0.6935 0.9048 -0.0263 -0.0077 -0.0581 207 GLN A CA  
1647 C C   . GLN A 206 ? 0.8539 0.6878 0.9325 -0.0292 -0.0064 -0.0610 207 GLN A C   
1648 O O   . GLN A 206 ? 0.8207 0.6488 0.9033 -0.0305 -0.0086 -0.0746 207 GLN A O   
1649 C CB  . GLN A 206 ? 0.8728 0.7451 0.9458 -0.0357 -0.0091 -0.0608 207 GLN A CB  
1650 C CG  . GLN A 206 ? 0.8843 0.7795 0.9488 -0.0325 -0.0108 -0.0596 207 GLN A CG  
1651 C CD  . GLN A 206 ? 0.8950 0.7975 0.9514 -0.0237 -0.0132 -0.0677 207 GLN A CD  
1652 O OE1 . GLN A 206 ? 0.7537 0.6655 0.8023 -0.0169 -0.0127 -0.0620 207 GLN A OE1 
1653 N NE2 . GLN A 206 ? 0.9211 0.8197 0.9797 -0.0241 -0.0157 -0.0812 207 GLN A NE2 
1654 N N   . GLU A 207 ? 0.8593 0.6789 0.9410 -0.0299 -0.0029 -0.0487 208 GLU A N   
1655 C CA  . GLU A 207 ? 0.8529 0.6473 0.9430 -0.0310 -0.0012 -0.0493 208 GLU A CA  
1656 C C   . GLU A 207 ? 0.8050 0.5881 0.8912 -0.0190 -0.0007 -0.0477 208 GLU A C   
1657 O O   . GLU A 207 ? 0.8358 0.5965 0.9284 -0.0179 0.0012  -0.0455 208 GLU A O   
1658 C CB  . GLU A 207 ? 0.8872 0.6714 0.9834 -0.0387 0.0027  -0.0358 208 GLU A CB  
1659 C CG  . GLU A 207 ? 0.8927 0.6918 0.9921 -0.0495 0.0031  -0.0343 208 GLU A CG  
1660 C CD  . GLU A 207 ? 0.9512 0.7685 1.0412 -0.0468 0.0043  -0.0230 208 GLU A CD  
1661 O OE1 . GLU A 207 ? 0.9413 0.7541 1.0247 -0.0399 0.0061  -0.0118 208 GLU A OE1 
1662 O OE2 . GLU A 207 ? 0.9043 0.7402 0.9935 -0.0514 0.0032  -0.0255 208 GLU A OE2 
1663 N N   . ASN A 208 ? 0.7721 0.5704 0.8489 -0.0099 -0.0021 -0.0484 209 ASN A N   
1664 C CA  . ASN A 208 ? 0.7360 0.5280 0.8097 0.0023  -0.0017 -0.0476 209 ASN A CA  
1665 C C   . ASN A 208 ? 0.7094 0.4874 0.7844 0.0059  0.0009  -0.0321 209 ASN A C   
1666 O O   . ASN A 208 ? 0.7301 0.4908 0.8089 0.0126  0.0019  -0.0317 209 ASN A O   
1667 C CB  . ASN A 208 ? 0.7466 0.5258 0.8247 0.0056  -0.0026 -0.0629 209 ASN A CB  
1668 C CG  . ASN A 208 ? 0.6928 0.4899 0.7642 0.0094  -0.0051 -0.0761 209 ASN A CG  
1669 O OD1 . ASN A 208 ? 0.6941 0.5041 0.7642 0.0023  -0.0073 -0.0831 209 ASN A OD1 
1670 N ND2 . ASN A 208 ? 0.6607 0.4598 0.7280 0.0208  -0.0047 -0.0790 209 ASN A ND2 
1671 N N   . GLN A 209 ? 0.7318 0.5181 0.8034 0.0018  0.0020  -0.0192 210 GLN A N   
1672 C CA  . GLN A 209 ? 0.7308 0.5089 0.8009 0.0055  0.0039  -0.0033 210 GLN A CA  
1673 C C   . GLN A 209 ? 0.7177 0.5153 0.7780 0.0117  0.0027  0.0040  210 GLN A C   
1674 O O   . GLN A 209 ? 0.7001 0.5168 0.7556 0.0086  0.0014  0.0009  210 GLN A O   
1675 C CB  . GLN A 209 ? 0.7864 0.5569 0.8601 -0.0047 0.0068  0.0066  210 GLN A CB  
1676 C CG  . GLN A 209 ? 0.7623 0.5128 0.8475 -0.0125 0.0083  0.0005  210 GLN A CG  
1677 C CD  . GLN A 209 ? 0.8273 0.5540 0.9181 -0.0055 0.0089  -0.0004 210 GLN A CD  
1678 O OE1 . GLN A 209 ? 0.8038 0.5249 0.8912 0.0036  0.0095  0.0101  210 GLN A OE1 
1679 N NE2 . GLN A 209 ? 0.8841 0.5967 0.9838 -0.0094 0.0086  -0.0133 210 GLN A NE2 
1680 N N   . PRO A 210 ? 0.7811 0.5794 0.7102 -0.0469 -0.0040 0.1148  211 PRO A N   
1681 C CA  . PRO A 210 ? 0.7705 0.5889 0.6977 -0.0370 -0.0022 0.1128  211 PRO A CA  
1682 C C   . PRO A 210 ? 0.8723 0.7068 0.7969 -0.0413 0.0033  0.1218  211 PRO A C   
1683 O O   . PRO A 210 ? 0.8874 0.7120 0.8051 -0.0450 0.0045  0.1330  211 PRO A O   
1684 C CB  . PRO A 210 ? 0.7408 0.5436 0.6600 -0.0247 -0.0067 0.1138  211 PRO A CB  
1685 C CG  . PRO A 210 ? 0.6956 0.4715 0.6091 -0.0297 -0.0089 0.1224  211 PRO A CG  
1686 C CD  . PRO A 210 ? 0.7370 0.5071 0.6577 -0.0428 -0.0084 0.1199  211 PRO A CD  
1687 N N   . ILE A 211 ? 0.9050 0.7639 0.8345 -0.0404 0.0067  0.1169  212 ILE A N   
1688 C CA  . ILE A 211 ? 0.9968 0.8734 0.9232 -0.0421 0.0119  0.1231  212 ILE A CA  
1689 C C   . ILE A 211 ? 1.0142 0.9036 0.9371 -0.0309 0.0108  0.1183  212 ILE A C   
1690 O O   . ILE A 211 ? 0.9477 0.8370 0.8739 -0.0238 0.0072  0.1097  212 ILE A O   
1691 C CB  . ILE A 211 ? 0.9903 0.8849 0.9264 -0.0518 0.0171  0.1215  212 ILE A CB  
1692 C CG1 . ILE A 211 ? 0.8893 0.7726 0.8335 -0.0619 0.0156  0.1204  212 ILE A CG1 
1693 C CG2 . ILE A 211 ? 1.0028 0.9089 0.9344 -0.0564 0.0234  0.1312  212 ILE A CG2 
1694 C CD1 . ILE A 211 ? 0.9105 0.8125 0.8663 -0.0712 0.0196  0.1185  212 ILE A CD1 
1695 N N   . ARG A 212 ? 1.0027 0.9033 0.9185 -0.0294 0.0140  0.1241  213 ARG A N   
1696 C CA  . ARG A 212 ? 1.0162 0.9322 0.9297 -0.0207 0.0133  0.1189  213 ARG A CA  
1697 C C   . ARG A 212 ? 1.0391 0.9692 0.9455 -0.0224 0.0182  0.1245  213 ARG A C   
1698 O O   . ARG A 212 ? 1.0957 1.0219 0.9903 -0.0187 0.0174  0.1317  213 ARG A O   
1699 C CB  . ARG A 212 ? 0.9931 0.8996 0.9007 -0.0101 0.0072  0.1186  213 ARG A CB  
1700 C CG  . ARG A 212 ? 0.9726 0.8955 0.8803 -0.0020 0.0056  0.1122  213 ARG A CG  
1701 C CD  . ARG A 212 ? 0.8848 0.8009 0.7896 0.0084  -0.0008 0.1112  213 ARG A CD  
1702 N NE  . ARG A 212 ? 0.7680 0.6775 0.6816 0.0116  -0.0035 0.1038  213 ARG A NE  
1703 C CZ  . ARG A 212 ? 0.8155 0.7182 0.7293 0.0207  -0.0085 0.1022  213 ARG A CZ  
1704 N NH1 . ARG A 212 ? 0.7773 0.6791 0.6837 0.0277  -0.0122 0.1074  213 ARG A NH1 
1705 N NH2 . ARG A 212 ? 0.6673 0.5648 0.5887 0.0233  -0.0099 0.0951  213 ARG A NH2 
1706 N N   . PRO A 215 ? 0.6573 0.6728 0.5652 -0.0143 0.0330  0.1009  216 PRO A N   
1707 C CA  . PRO A 215 ? 0.6538 0.6817 0.5724 -0.0150 0.0351  0.0927  216 PRO A CA  
1708 C C   . PRO A 215 ? 0.6616 0.7042 0.5756 -0.0143 0.0411  0.0921  216 PRO A C   
1709 O O   . PRO A 215 ? 0.5971 0.6408 0.4979 -0.0121 0.0429  0.0966  216 PRO A O   
1710 C CB  . PRO A 215 ? 0.5968 0.6238 0.5178 -0.0087 0.0288  0.0844  216 PRO A CB  
1711 C CG  . PRO A 215 ? 0.6624 0.6827 0.5715 -0.0035 0.0245  0.0878  216 PRO A CG  
1712 C CD  . PRO A 215 ? 0.6617 0.6708 0.5656 -0.0071 0.0258  0.0978  216 PRO A CD  
1713 N N   . GLY A 216 ? 0.5686 0.6222 0.4931 -0.0157 0.0440  0.0863  217 GLY A N   
1714 C CA  . GLY A 216 ? 0.5264 0.5941 0.4478 -0.0136 0.0495  0.0842  217 GLY A CA  
1715 C C   . GLY A 216 ? 0.4985 0.5682 0.4117 -0.0058 0.0460  0.0770  217 GLY A C   
1716 O O   . GLY A 216 ? 0.4775 0.5389 0.3883 -0.0025 0.0392  0.0742  217 GLY A O   
1717 N N   . PRO A 217 ? 0.4277 0.5087 0.3365 -0.0027 0.0506  0.0736  218 PRO A N   
1718 C CA  . PRO A 217 ? 0.3326 0.4145 0.2326 0.0044  0.0469  0.0661  218 PRO A CA  
1719 C C   . PRO A 217 ? 0.3287 0.4121 0.2399 0.0065  0.0434  0.0568  218 PRO A C   
1720 O O   . PRO A 217 ? 0.3436 0.4319 0.2676 0.0039  0.0460  0.0554  218 PRO A O   
1721 C CB  . PRO A 217 ? 0.3347 0.4274 0.2245 0.0069  0.0542  0.0666  218 PRO A CB  
1722 C CG  . PRO A 217 ? 0.3331 0.4352 0.2349 0.0018  0.0616  0.0702  218 PRO A CG  
1723 C CD  . PRO A 217 ? 0.3755 0.4687 0.2856 -0.0053 0.0595  0.0772  218 PRO A CD  
1724 N N   . LEU A 218 ? 0.3351 0.4140 0.2415 0.0109  0.0371  0.0508  219 LEU A N   
1725 C CA  . LEU A 218 ? 0.2939 0.3718 0.2098 0.0125  0.0328  0.0428  219 LEU A CA  
1726 C C   . LEU A 218 ? 0.2484 0.3219 0.1777 0.0082  0.0307  0.0446  219 LEU A C   
1727 O O   . LEU A 218 ? 0.2670 0.3419 0.2066 0.0078  0.0299  0.0401  219 LEU A O   
1728 C CB  . LEU A 218 ? 0.2992 0.3853 0.2178 0.0152  0.0368  0.0369  219 LEU A CB  
1729 C CG  . LEU A 218 ? 0.2808 0.3645 0.2043 0.0182  0.0320  0.0282  219 LEU A CG  
1730 C CD1 . LEU A 218 ? 0.3322 0.4084 0.2497 0.0196  0.0245  0.0256  219 LEU A CD1 
1731 C CD2 . LEU A 218 ? 0.3037 0.3932 0.2236 0.0232  0.0354  0.0219  219 LEU A CD2 
1732 N N   . GLY A 219 ? 0.2472 0.3144 0.1755 0.0052  0.0299  0.0511  220 GLY A N   
1733 C CA  . GLY A 219 ? 0.2348 0.2972 0.1742 0.0013  0.0284  0.0525  220 GLY A CA  
1734 C C   . GLY A 219 ? 0.2399 0.2967 0.1835 0.0031  0.0221  0.0484  220 GLY A C   
1735 O O   . GLY A 219 ? 0.2053 0.2606 0.1585 0.0010  0.0212  0.0466  220 GLY A O   
1736 N N   . ALA A 220 ? 0.2318 0.2866 0.1684 0.0069  0.0178  0.0470  221 ALA A N   
1737 C CA  . ALA A 220 ? 0.2145 0.2654 0.1563 0.0082  0.0123  0.0442  221 ALA A CA  
1738 C C   . ALA A 220 ? 0.2180 0.2713 0.1698 0.0074  0.0115  0.0384  221 ALA A C   
1739 O O   . ALA A 220 ? 0.2016 0.2520 0.1607 0.0061  0.0101  0.0383  221 ALA A O   
1740 C CB  . ALA A 220 ? 0.2400 0.2910 0.1742 0.0122  0.0073  0.0429  221 ALA A CB  
1741 N N   . PRO A 221 ? 0.1974 0.2554 0.1494 0.0084  0.0124  0.0337  222 PRO A N   
1742 C CA  . PRO A 221 ? 0.1823 0.2409 0.1432 0.0076  0.0112  0.0292  222 PRO A CA  
1743 C C   . PRO A 221 ? 0.1761 0.2352 0.1449 0.0046  0.0141  0.0308  222 PRO A C   
1744 O O   . PRO A 221 ? 0.1949 0.2532 0.1706 0.0037  0.0125  0.0285  222 PRO A O   
1745 C CB  . PRO A 221 ? 0.1858 0.2477 0.1436 0.0101  0.0116  0.0242  222 PRO A CB  
1746 C CG  . PRO A 221 ? 0.2073 0.2701 0.1535 0.0126  0.0115  0.0248  222 PRO A CG  
1747 C CD  . PRO A 221 ? 0.2198 0.2817 0.1629 0.0109  0.0143  0.0319  222 PRO A CD  
1748 N N   . ALA A 222 ? 0.1869 0.2474 0.1546 0.0026  0.0180  0.0350  223 ALA A N   
1749 C CA  . ALA A 222 ? 0.1628 0.2248 0.1385 -0.0009 0.0201  0.0362  223 ALA A CA  
1750 C C   . ALA A 222 ? 0.1937 0.2491 0.1714 -0.0039 0.0189  0.0394  223 ALA A C   
1751 O O   . ALA A 222 ? 0.1893 0.2436 0.1734 -0.0060 0.0180  0.0383  223 ALA A O   
1752 C CB  . ALA A 222 ? 0.1953 0.2642 0.1709 -0.0023 0.0253  0.0387  223 ALA A CB  
1753 N N   . TYR A 223 ? 0.1940 0.2441 0.1655 -0.0036 0.0184  0.0433  224 TYR A N   
1754 C CA  . TYR A 223 ? 0.2104 0.2526 0.1833 -0.0060 0.0175  0.0463  224 TYR A CA  
1755 C C   . TYR A 223 ? 0.2256 0.2607 0.1919 -0.0032 0.0151  0.0492  224 TYR A C   
1756 O O   . TYR A 223 ? 0.2687 0.2953 0.2344 -0.0045 0.0145  0.0524  224 TYR A O   
1757 C CB  . TYR A 223 ? 0.2424 0.2847 0.2174 -0.0112 0.0209  0.0504  224 TYR A CB  
1758 C CG  . TYR A 223 ? 0.2576 0.3037 0.2265 -0.0118 0.0247  0.0551  224 TYR A CG  
1759 C CD1 . TYR A 223 ? 0.2764 0.3155 0.2370 -0.0114 0.0245  0.0605  224 TYR A CD1 
1760 C CD2 . TYR A 223 ? 0.2184 0.2755 0.1892 -0.0122 0.0287  0.0542  224 TYR A CD2 
1761 C CE1 . TYR A 223 ? 0.3018 0.3444 0.2551 -0.0119 0.0283  0.0654  224 TYR A CE1 
1762 C CE2 . TYR A 223 ? 0.2624 0.3240 0.2265 -0.0124 0.0331  0.0585  224 TYR A CE2 
1763 C CZ  . TYR A 223 ? 0.2769 0.3312 0.2317 -0.0125 0.0329  0.0643  224 TYR A CZ  
1764 O OH  . TYR A 223 ? 0.3622 0.4209 0.3089 -0.0128 0.0375  0.0693  224 TYR A OH  
1765 N N   . GLY A 224 ? 0.2129 0.2506 0.1744 0.0009  0.0130  0.0479  225 GLY A N   
1766 C CA  . GLY A 224 ? 0.2305 0.2631 0.1849 0.0039  0.0106  0.0517  225 GLY A CA  
1767 C C   . GLY A 224 ? 0.2366 0.2666 0.1932 0.0079  0.0060  0.0499  225 GLY A C   
1768 O O   . GLY A 224 ? 0.2500 0.2780 0.2010 0.0114  0.0031  0.0525  225 GLY A O   
1769 N N   . VAL A 225 ? 0.2235 0.2542 0.1882 0.0077  0.0052  0.0458  226 VAL A N   
1770 C CA  . VAL A 225 ? 0.2305 0.2614 0.1987 0.0116  0.0017  0.0439  226 VAL A CA  
1771 C C   . VAL A 225 ? 0.2200 0.2419 0.1893 0.0127  0.0016  0.0459  226 VAL A C   
1772 O O   . VAL A 225 ? 0.1935 0.2101 0.1638 0.0092  0.0039  0.0461  226 VAL A O   
1773 C CB  . VAL A 225 ? 0.2193 0.2571 0.1951 0.0109  0.0013  0.0386  226 VAL A CB  
1774 C CG1 . VAL A 225 ? 0.2196 0.2594 0.2009 0.0144  -0.0011 0.0370  226 VAL A CG1 
1775 C CG2 . VAL A 225 ? 0.2322 0.2766 0.2063 0.0105  0.0004  0.0363  226 VAL A CG2 
1776 N N   . LYS A 226 ? 0.2014 0.2216 0.1706 0.0178  -0.0016 0.0467  227 LYS A N   
1777 C CA  . LYS A 226 ? 0.2099 0.2212 0.1802 0.0208  -0.0023 0.0476  227 LYS A CA  
1778 C C   . LYS A 226 ? 0.2513 0.2692 0.2291 0.0255  -0.0039 0.0436  227 LYS A C   
1779 O O   . LYS A 226 ? 0.2680 0.2959 0.2487 0.0272  -0.0061 0.0424  227 LYS A O   
1780 C CB  . LYS A 226 ? 0.2473 0.2496 0.2103 0.0240  -0.0044 0.0536  227 LYS A CB  
1781 C CG  . LYS A 226 ? 0.2680 0.2644 0.2233 0.0189  -0.0020 0.0589  227 LYS A CG  
1782 C CD  . LYS A 226 ? 0.2945 0.2993 0.2441 0.0184  -0.0021 0.0606  227 LYS A CD  
1783 C CE  . LYS A 226 ? 0.3437 0.3450 0.2869 0.0131  0.0017  0.0655  227 LYS A CE  
1784 N NZ  . LYS A 226 ? 0.3213 0.3300 0.2568 0.0133  0.0023  0.0672  227 LYS A NZ  
1785 N N   . SER A 227 ? 0.2300 0.2430 0.2108 0.0272  -0.0028 0.0413  228 SER A N   
1786 C CA  . SER A 227 ? 0.2043 0.2255 0.1926 0.0314  -0.0031 0.0375  228 SER A CA  
1787 C C   . SER A 227 ? 0.2697 0.2822 0.2583 0.0358  -0.0023 0.0358  228 SER A C   
1788 O O   . SER A 227 ? 0.2477 0.2467 0.2308 0.0346  -0.0018 0.0370  228 SER A O   
1789 C CB  . SER A 227 ? 0.2496 0.2805 0.2428 0.0269  -0.0008 0.0339  228 SER A CB  
1790 O OG  . SER A 227 ? 0.2514 0.2928 0.2524 0.0299  -0.0008 0.0313  228 SER A OG  
1791 N N   . THR A 228 ? 0.2434 0.2640 0.2386 0.0409  -0.0020 0.0328  229 THR A N   
1792 C CA  . THR A 228 ? 0.2367 0.2511 0.2325 0.0466  -0.0007 0.0299  229 THR A CA  
1793 C C   . THR A 228 ? 0.2481 0.2677 0.2463 0.0441  0.0032  0.0251  229 THR A C   
1794 O O   . THR A 228 ? 0.2315 0.2611 0.2327 0.0390  0.0045  0.0246  229 THR A O   
1795 C CB  . THR A 228 ? 0.2781 0.2998 0.2802 0.0554  -0.0027 0.0300  229 THR A CB  
1796 O OG1 . THR A 228 ? 0.2333 0.2733 0.2444 0.0545  -0.0016 0.0283  229 THR A OG1 
1797 C CG2 . THR A 228 ? 0.2380 0.2553 0.2368 0.0582  -0.0074 0.0354  229 THR A CG2 
1798 N N   . LEU A 229 ? 0.2393 0.2511 0.2352 0.0481  0.0049  0.0215  230 LEU A N   
1799 C CA  . LEU A 229 ? 0.2268 0.2443 0.2235 0.0466  0.0087  0.0170  230 LEU A CA  
1800 C C   . LEU A 229 ? 0.2364 0.2724 0.2421 0.0488  0.0109  0.0162  230 LEU A C   
1801 O O   . LEU A 229 ? 0.2302 0.2744 0.2374 0.0437  0.0133  0.0155  230 LEU A O   
1802 C CB  . LEU A 229 ? 0.2219 0.2269 0.2129 0.0511  0.0099  0.0124  230 LEU A CB  
1803 C CG  . LEU A 229 ? 0.2393 0.2490 0.2281 0.0489  0.0136  0.0078  230 LEU A CG  
1804 C CD1 . LEU A 229 ? 0.2621 0.2674 0.2462 0.0397  0.0129  0.0085  230 LEU A CD1 
1805 C CD2 . LEU A 229 ? 0.2505 0.2513 0.2340 0.0557  0.0153  0.0018  230 LEU A CD2 
1806 N N   . PRO A 230 ? 0.2458 0.2896 0.2583 0.0561  0.0102  0.0167  231 PRO A N   
1807 C CA  . PRO A 230 ? 0.2194 0.2830 0.2425 0.0566  0.0122  0.0165  231 PRO A CA  
1808 C C   . PRO A 230 ? 0.2262 0.2982 0.2527 0.0486  0.0106  0.0195  231 PRO A C   
1809 O O   . PRO A 230 ? 0.2533 0.3369 0.2850 0.0448  0.0133  0.0190  231 PRO A O   
1810 C CB  . PRO A 230 ? 0.2368 0.3061 0.2670 0.0658  0.0102  0.0171  231 PRO A CB  
1811 C CG  . PRO A 230 ? 0.2783 0.3299 0.3006 0.0721  0.0095  0.0154  231 PRO A CG  
1812 C CD  . PRO A 230 ? 0.2513 0.2865 0.2630 0.0647  0.0078  0.0170  231 PRO A CD  
1813 N N   . ASP A 231 ? 0.2082 0.2744 0.2316 0.0461  0.0063  0.0225  232 ASP A N   
1814 C CA  . ASP A 231 ? 0.1915 0.2642 0.2169 0.0391  0.0046  0.0242  232 ASP A CA  
1815 C C   . ASP A 231 ? 0.2183 0.2872 0.2391 0.0322  0.0073  0.0232  232 ASP A C   
1816 O O   . ASP A 231 ? 0.1856 0.2625 0.2103 0.0274  0.0079  0.0234  232 ASP A O   
1817 C CB  . ASP A 231 ? 0.1907 0.2577 0.2116 0.0385  0.0000  0.0272  232 ASP A CB  
1818 C CG  . ASP A 231 ? 0.2228 0.2991 0.2500 0.0432  -0.0042 0.0288  232 ASP A CG  
1819 O OD1 . ASP A 231 ? 0.2524 0.3406 0.2892 0.0470  -0.0036 0.0276  232 ASP A OD1 
1820 O OD2 . ASP A 231 ? 0.2559 0.3280 0.2780 0.0432  -0.0082 0.0314  232 ASP A OD2 
1821 N N   . MET A 232 ? 0.1860 0.2422 0.1986 0.0315  0.0085  0.0224  233 MET A N   
1822 C CA  . MET A 232 ? 0.1804 0.2342 0.1894 0.0254  0.0103  0.0216  233 MET A CA  
1823 C C   . MET A 232 ? 0.1961 0.2574 0.2077 0.0252  0.0140  0.0195  233 MET A C   
1824 O O   . MET A 232 ? 0.1868 0.2515 0.1985 0.0200  0.0149  0.0200  233 MET A O   
1825 C CB  . MET A 232 ? 0.2105 0.2503 0.2114 0.0241  0.0099  0.0211  233 MET A CB  
1826 C CG  . MET A 232 ? 0.2163 0.2500 0.2142 0.0221  0.0071  0.0243  233 MET A CG  
1827 S SD  . MET A 232 ? 0.2344 0.2758 0.2342 0.0168  0.0062  0.0261  233 MET A SD  
1828 C CE  . MET A 232 ? 0.2358 0.2743 0.2330 0.0113  0.0081  0.0247  233 MET A CE  
1829 N N   . LEU A 233 ? 0.2016 0.2660 0.2150 0.0310  0.0163  0.0174  234 LEU A N   
1830 C CA  . LEU A 233 ? 0.1897 0.2638 0.2058 0.0308  0.0207  0.0161  234 LEU A CA  
1831 C C   . LEU A 233 ? 0.2066 0.2953 0.2325 0.0277  0.0209  0.0188  234 LEU A C   
1832 O O   . LEU A 233 ? 0.2008 0.2952 0.2277 0.0234  0.0235  0.0196  234 LEU A O   
1833 C CB  . LEU A 233 ? 0.2408 0.3162 0.2568 0.0387  0.0237  0.0129  234 LEU A CB  
1834 C CG  . LEU A 233 ? 0.2464 0.3066 0.2516 0.0412  0.0239  0.0092  234 LEU A CG  
1835 C CD1 . LEU A 233 ? 0.2831 0.3425 0.2885 0.0507  0.0260  0.0055  234 LEU A CD1 
1836 C CD2 . LEU A 233 ? 0.2685 0.3270 0.2665 0.0366  0.0262  0.0077  234 LEU A CD2 
1837 N N   . SER A 234 ? 0.2074 0.3015 0.2404 0.0295  0.0177  0.0202  235 SER A N   
1838 C CA  . SER A 234 ? 0.2236 0.3302 0.2660 0.0254  0.0165  0.0223  235 SER A CA  
1839 C C   . SER A 234 ? 0.2183 0.3200 0.2573 0.0178  0.0146  0.0236  235 SER A C   
1840 O O   . SER A 234 ? 0.2055 0.3142 0.2494 0.0128  0.0155  0.0250  235 SER A O   
1841 C CB  . SER A 234 ? 0.2455 0.3577 0.2947 0.0288  0.0119  0.0232  235 SER A CB  
1842 O OG  . SER A 234 ? 0.2766 0.3959 0.3315 0.0365  0.0135  0.0222  235 SER A OG  
1843 N N   . PHE A 235 ? 0.1988 0.2886 0.2298 0.0170  0.0121  0.0235  236 PHE A N   
1844 C CA  . PHE A 235 ? 0.1826 0.2678 0.2103 0.0111  0.0107  0.0242  236 PHE A CA  
1845 C C   . PHE A 235 ? 0.1843 0.2685 0.2093 0.0080  0.0141  0.0243  236 PHE A C   
1846 O O   . PHE A 235 ? 0.1686 0.2545 0.1953 0.0032  0.0137  0.0256  236 PHE A O   
1847 C CB  . PHE A 235 ? 0.1806 0.2551 0.2008 0.0115  0.0084  0.0242  236 PHE A CB  
1848 C CG  . PHE A 235 ? 0.1908 0.2615 0.2081 0.0068  0.0072  0.0246  236 PHE A CG  
1849 C CD1 . PHE A 235 ? 0.1576 0.2324 0.1785 0.0040  0.0048  0.0247  236 PHE A CD1 
1850 C CD2 . PHE A 235 ? 0.2028 0.2659 0.2140 0.0053  0.0082  0.0244  236 PHE A CD2 
1851 C CE1 . PHE A 235 ? 0.1911 0.2616 0.2091 0.0008  0.0037  0.0245  236 PHE A CE1 
1852 C CE2 . PHE A 235 ? 0.1954 0.2563 0.2050 0.0021  0.0072  0.0245  236 PHE A CE2 
1853 C CZ  . PHE A 235 ? 0.2104 0.2745 0.2229 0.0003  0.0052  0.0245  236 PHE A CZ  
1854 N N   . ILE A 236 ? 0.1687 0.2491 0.1885 0.0107  0.0169  0.0229  237 ILE A N   
1855 C CA  . ILE A 236 ? 0.2026 0.2828 0.2185 0.0081  0.0198  0.0231  237 ILE A CA  
1856 C C   . ILE A 236 ? 0.1892 0.2810 0.2117 0.0065  0.0228  0.0250  237 ILE A C   
1857 O O   . ILE A 236 ? 0.1819 0.2745 0.2035 0.0020  0.0238  0.0271  237 ILE A O   
1858 C CB  . ILE A 236 ? 0.2401 0.3139 0.2481 0.0115  0.0217  0.0204  237 ILE A CB  
1859 C CG1 . ILE A 236 ? 0.2258 0.2884 0.2286 0.0115  0.0186  0.0193  237 ILE A CG1 
1860 C CG2 . ILE A 236 ? 0.2426 0.3166 0.2451 0.0090  0.0241  0.0206  237 ILE A CG2 
1861 C CD1 . ILE A 236 ? 0.3178 0.3782 0.3208 0.0067  0.0160  0.0212  237 ILE A CD1 
1862 N N   . HIS A 237 ? 0.1781 0.2793 0.2078 0.0101  0.0244  0.0246  238 HIS A N   
1863 C CA  . HIS A 237 ? 0.2100 0.3246 0.2481 0.0078  0.0276  0.0269  238 HIS A CA  
1864 C C   . HIS A 237 ? 0.2203 0.3365 0.2638 0.0008  0.0246  0.0297  238 HIS A C   
1865 O O   . HIS A 237 ? 0.2037 0.3238 0.2490 -0.0041 0.0270  0.0326  238 HIS A O   
1866 C CB  . HIS A 237 ? 0.2187 0.3450 0.2661 0.0131  0.0289  0.0259  238 HIS A CB  
1867 C CG  . HIS A 237 ? 0.2674 0.4101 0.3264 0.0099  0.0320  0.0287  238 HIS A CG  
1868 N ND1 . HIS A 237 ? 0.2607 0.4108 0.3304 0.0054  0.0283  0.0307  238 HIS A ND1 
1869 C CD2 . HIS A 237 ? 0.3090 0.4626 0.3705 0.0103  0.0385  0.0299  238 HIS A CD2 
1870 C CE1 . HIS A 237 ? 0.3200 0.4850 0.3997 0.0024  0.0322  0.0333  238 HIS A CE1 
1871 N NE2 . HIS A 237 ? 0.3380 0.5059 0.4129 0.0054  0.0388  0.0332  238 HIS A NE2 
1872 N N   . ALA A 238 ? 0.1717 0.2837 0.2167 0.0003  0.0194  0.0289  239 ALA A N   
1873 C CA  . ALA A 238 ? 0.1709 0.2825 0.2200 -0.0058 0.0158  0.0304  239 ALA A CA  
1874 C C   . ALA A 238 ? 0.1847 0.2869 0.2268 -0.0098 0.0160  0.0317  239 ALA A C   
1875 O O   . ALA A 238 ? 0.1781 0.2808 0.2236 -0.0153 0.0154  0.0340  239 ALA A O   
1876 C CB  . ALA A 238 ? 0.1577 0.2657 0.2069 -0.0044 0.0103  0.0285  239 ALA A CB  
1877 N N   . ASN A 239 ? 0.1644 0.2576 0.1972 -0.0072 0.0165  0.0304  240 ASN A N   
1878 C CA  . ASN A 239 ? 0.1664 0.2516 0.1929 -0.0101 0.0161  0.0316  240 ASN A CA  
1879 C C   . ASN A 239 ? 0.1547 0.2429 0.1793 -0.0121 0.0202  0.0345  240 ASN A C   
1880 O O   . ASN A 239 ? 0.1879 0.2716 0.2102 -0.0158 0.0195  0.0371  240 ASN A O   
1881 C CB  . ASN A 239 ? 0.1319 0.2087 0.1505 -0.0071 0.0150  0.0294  240 ASN A CB  
1882 C CG  . ASN A 239 ? 0.1488 0.2206 0.1673 -0.0070 0.0112  0.0280  240 ASN A CG  
1883 O OD1 . ASN A 239 ? 0.2221 0.2892 0.2391 -0.0091 0.0093  0.0284  240 ASN A OD1 
1884 N ND2 . ASN A 239 ? 0.1632 0.2364 0.1830 -0.0042 0.0100  0.0265  240 ASN A ND2 
1885 N N   . LEU A 240 ? 0.1654 0.2608 0.1901 -0.0093 0.0244  0.0342  241 LEU A N   
1886 C CA  . LEU A 240 ? 0.1889 0.2890 0.2111 -0.0110 0.0292  0.0372  241 LEU A CA  
1887 C C   . LEU A 240 ? 0.2006 0.3105 0.2325 -0.0159 0.0311  0.0412  241 LEU A C   
1888 O O   . LEU A 240 ? 0.2324 0.3440 0.2620 -0.0195 0.0342  0.0454  241 LEU A O   
1889 C CB  . LEU A 240 ? 0.1958 0.3002 0.2137 -0.0054 0.0335  0.0345  241 LEU A CB  
1890 C CG  . LEU A 240 ? 0.2068 0.3006 0.2132 -0.0020 0.0321  0.0311  241 LEU A CG  
1891 C CD1 . LEU A 240 ? 0.2331 0.3289 0.2364 0.0044  0.0351  0.0269  241 LEU A CD1 
1892 C CD2 . LEU A 240 ? 0.1849 0.2742 0.1822 -0.0048 0.0326  0.0335  241 LEU A CD2 
1893 N N   . ASN A 241 ? 0.1955 0.3121 0.2382 -0.0165 0.0291  0.0404  242 ASN A N   
1894 C CA  . ASN A 241 ? 0.2167 0.3445 0.2708 -0.0219 0.0306  0.0440  242 ASN A CA  
1895 C C   . ASN A 241 ? 0.2053 0.3311 0.2672 -0.0259 0.0244  0.0433  242 ASN A C   
1896 O O   . ASN A 241 ? 0.1883 0.3250 0.2615 -0.0267 0.0232  0.0429  242 ASN A O   
1897 C CB  . ASN A 241 ? 0.2495 0.3931 0.3113 -0.0180 0.0352  0.0433  242 ASN A CB  
1898 C CG  . ASN A 241 ? 0.3316 0.4771 0.3847 -0.0131 0.0415  0.0427  242 ASN A CG  
1899 O OD1 . ASN A 241 ? 0.3761 0.5271 0.4276 -0.0161 0.0468  0.0466  242 ASN A OD1 
1900 N ND2 . ASN A 241 ? 0.3428 0.4831 0.3894 -0.0058 0.0410  0.0379  242 ASN A ND2 
1901 N N   . PRO A 242 ? 0.1721 0.2846 0.2284 -0.0282 0.0200  0.0430  243 PRO A N   
1902 C CA  . PRO A 242 ? 0.1876 0.2971 0.2496 -0.0314 0.0139  0.0413  243 PRO A CA  
1903 C C   . PRO A 242 ? 0.1995 0.3173 0.2734 -0.0387 0.0134  0.0444  243 PRO A C   
1904 O O   . PRO A 242 ? 0.1941 0.3151 0.2755 -0.0407 0.0086  0.0422  243 PRO A O   
1905 C CB  . PRO A 242 ? 0.1975 0.2913 0.2505 -0.0321 0.0108  0.0407  243 PRO A CB  
1906 C CG  . PRO A 242 ? 0.2417 0.3322 0.2876 -0.0322 0.0150  0.0442  243 PRO A CG  
1907 C CD  . PRO A 242 ? 0.1909 0.2911 0.2359 -0.0279 0.0201  0.0440  243 PRO A CD  
1908 N N   . GLN A 243 ? 0.1946 0.3165 0.2703 -0.0432 0.0183  0.0496  244 GLN A N   
1909 C CA  . GLN A 243 ? 0.1924 0.3226 0.2804 -0.0515 0.0183  0.0535  244 GLN A CA  
1910 C C   . GLN A 243 ? 0.2203 0.3696 0.3220 -0.0509 0.0192  0.0525  244 GLN A C   
1911 O O   . GLN A 243 ? 0.2181 0.3752 0.3324 -0.0581 0.0171  0.0544  244 GLN A O   
1912 C CB  . GLN A 243 ? 0.2508 0.3817 0.3365 -0.0563 0.0242  0.0604  244 GLN A CB  
1913 C CG  . GLN A 243 ? 0.2395 0.3843 0.3244 -0.0523 0.0326  0.0624  244 GLN A CG  
1914 C CD  . GLN A 243 ? 0.2644 0.4019 0.3345 -0.0438 0.0346  0.0594  244 GLN A CD  
1915 O OE1 . GLN A 243 ? 0.2448 0.3683 0.3064 -0.0410 0.0300  0.0562  244 GLN A OE1 
1916 N NE2 . GLN A 243 ? 0.3377 0.4854 0.4053 -0.0399 0.0415  0.0602  244 GLN A NE2 
1917 N N   . LYS A 244 ? 0.1774 0.3343 0.2776 -0.0425 0.0218  0.0496  245 LYS A N   
1918 C CA  . LYS A 244 ? 0.1901 0.3654 0.3035 -0.0401 0.0223  0.0484  245 LYS A CA  
1919 C C   . LYS A 244 ? 0.2237 0.3979 0.3410 -0.0384 0.0141  0.0438  245 LYS A C   
1920 O O   . LYS A 244 ? 0.2451 0.4346 0.3745 -0.0367 0.0128  0.0430  245 LYS A O   
1921 C CB  . LYS A 244 ? 0.2367 0.4192 0.3463 -0.0309 0.0284  0.0469  245 LYS A CB  
1922 C CG  . LYS A 244 ? 0.2932 0.4812 0.3995 -0.0316 0.0372  0.0509  245 LYS A CG  
1923 C CD  . LYS A 244 ? 0.3894 0.5833 0.4913 -0.0214 0.0425  0.0478  245 LYS A CD  
1924 C CE  . LYS A 244 ? 0.4229 0.6258 0.5223 -0.0216 0.0517  0.0513  245 LYS A CE  
1925 N NZ  . LYS A 244 ? 0.3905 0.5793 0.4764 -0.0261 0.0528  0.0546  245 LYS A NZ  
1926 N N   . TYR A 245 ? 0.1561 0.3138 0.2638 -0.0383 0.0087  0.0410  246 TYR A N   
1927 C CA  . TYR A 245 ? 0.1627 0.3181 0.2707 -0.0359 0.0012  0.0366  246 TYR A CA  
1928 C C   . TYR A 245 ? 0.1717 0.3232 0.2849 -0.0442 -0.0054 0.0359  246 TYR A C   
1929 O O   . TYR A 245 ? 0.1910 0.3351 0.3036 -0.0510 -0.0046 0.0385  246 TYR A O   
1930 C CB  . TYR A 245 ? 0.1493 0.2896 0.2421 -0.0295 0.0000  0.0335  246 TYR A CB  
1931 C CG  . TYR A 245 ? 0.2026 0.3460 0.2911 -0.0212 0.0045  0.0330  246 TYR A CG  
1932 C CD1 . TYR A 245 ? 0.1785 0.3230 0.2638 -0.0200 0.0115  0.0353  246 TYR A CD1 
1933 C CD2 . TYR A 245 ? 0.1863 0.3307 0.2731 -0.0146 0.0015  0.0304  246 TYR A CD2 
1934 C CE1 . TYR A 245 ? 0.1948 0.3405 0.2755 -0.0123 0.0152  0.0340  246 TYR A CE1 
1935 C CE2 . TYR A 245 ? 0.2083 0.3533 0.2911 -0.0071 0.0052  0.0299  246 TYR A CE2 
1936 C CZ  . TYR A 245 ? 0.2372 0.3826 0.3171 -0.0060 0.0120  0.0312  246 TYR A CZ  
1937 O OH  . TYR A 245 ? 0.2478 0.3921 0.3230 0.0015  0.0152  0.0298  246 TYR A OH  
1938 N N   . PRO A 246 ? 0.1389 0.2945 0.2568 -0.0438 -0.0124 0.0324  247 PRO A N   
1939 C CA  . PRO A 246 ? 0.1698 0.3204 0.2916 -0.0517 -0.0197 0.0306  247 PRO A CA  
1940 C C   . PRO A 246 ? 0.1533 0.2826 0.2615 -0.0527 -0.0216 0.0285  247 PRO A C   
1941 O O   . PRO A 246 ? 0.1844 0.3038 0.2800 -0.0464 -0.0192 0.0274  247 PRO A O   
1942 C CB  . PRO A 246 ? 0.1829 0.3407 0.3078 -0.0482 -0.0270 0.0263  247 PRO A CB  
1943 C CG  . PRO A 246 ? 0.1394 0.3131 0.2705 -0.0414 -0.0228 0.0282  247 PRO A CG  
1944 C CD  . PRO A 246 ? 0.1646 0.3311 0.2857 -0.0365 -0.0144 0.0303  247 PRO A CD  
1945 N N   . ALA A 247 ? 0.1779 0.3003 0.2896 -0.0609 -0.0265 0.0278  248 ALA A N   
1946 C CA  . ALA A 247 ? 0.2025 0.3050 0.3038 -0.0627 -0.0274 0.0269  248 ALA A CA  
1947 C C   . ALA A 247 ? 0.1879 0.2784 0.2745 -0.0548 -0.0294 0.0218  248 ALA A C   
1948 O O   . ALA A 247 ? 0.1863 0.2650 0.2631 -0.0518 -0.0263 0.0224  248 ALA A O   
1949 C CB  . ALA A 247 ? 0.2226 0.3187 0.3303 -0.0722 -0.0338 0.0258  248 ALA A CB  
1950 N N   . ASP A 248 ? 0.1931 0.2871 0.2778 -0.0513 -0.0346 0.0170  249 ASP A N   
1951 C CA  . ASP A 248 ? 0.2055 0.2879 0.2759 -0.0447 -0.0363 0.0123  249 ASP A CA  
1952 C C   . ASP A 248 ? 0.1923 0.2743 0.2549 -0.0374 -0.0297 0.0145  249 ASP A C   
1953 O O   . ASP A 248 ? 0.1924 0.2630 0.2450 -0.0343 -0.0280 0.0133  249 ASP A O   
1954 C CB  . ASP A 248 ? 0.2231 0.3098 0.2917 -0.0425 -0.0432 0.0073  249 ASP A CB  
1955 C CG  . ASP A 248 ? 0.2636 0.3462 0.3362 -0.0495 -0.0514 0.0031  249 ASP A CG  
1956 O OD1 . ASP A 248 ? 0.2821 0.3537 0.3557 -0.0551 -0.0520 0.0031  249 ASP A OD1 
1957 O OD2 . ASP A 248 ? 0.3082 0.3981 0.3829 -0.0496 -0.0580 -0.0003 249 ASP A OD2 
1958 N N   . ILE A 249 ? 0.1671 0.2614 0.2345 -0.0345 -0.0259 0.0175  250 ILE A N   
1959 C CA  . ILE A 249 ? 0.1438 0.2360 0.2035 -0.0282 -0.0202 0.0192  250 ILE A CA  
1960 C C   . ILE A 249 ? 0.1528 0.2420 0.2129 -0.0304 -0.0145 0.0231  250 ILE A C   
1961 O O   . ILE A 249 ? 0.1765 0.2590 0.2284 -0.0267 -0.0112 0.0236  250 ILE A O   
1962 C CB  . ILE A 249 ? 0.1790 0.2827 0.2418 -0.0231 -0.0190 0.0202  250 ILE A CB  
1963 C CG1 . ILE A 249 ? 0.1864 0.2848 0.2395 -0.0166 -0.0149 0.0207  250 ILE A CG1 
1964 C CG2 . ILE A 249 ? 0.1925 0.3097 0.2679 -0.0255 -0.0159 0.0236  250 ILE A CG2 
1965 C CD1 . ILE A 249 ? 0.1812 0.2705 0.2232 -0.0134 -0.0176 0.0178  250 ILE A CD1 
1966 N N   . GLN A 250 ? 0.1922 0.2866 0.2615 -0.0366 -0.0135 0.0263  251 GLN A N   
1967 C CA  A GLN A 250 ? 0.1786 0.2692 0.2466 -0.0390 -0.0085 0.0305  251 GLN A CA  
1968 C CA  B GLN A 250 ? 0.1787 0.2692 0.2468 -0.0391 -0.0086 0.0306  251 GLN A CA  
1969 C C   . GLN A 250 ? 0.1839 0.2583 0.2428 -0.0390 -0.0101 0.0294  251 GLN A C   
1970 O O   . GLN A 250 ? 0.1871 0.2564 0.2390 -0.0360 -0.0066 0.0311  251 GLN A O   
1971 C CB  A GLN A 250 ? 0.1793 0.2777 0.2587 -0.0467 -0.0075 0.0347  251 GLN A CB  
1972 C CB  B GLN A 250 ? 0.1796 0.2774 0.2591 -0.0471 -0.0079 0.0345  251 GLN A CB  
1973 C CG  A GLN A 250 ? 0.1969 0.2894 0.2735 -0.0503 -0.0031 0.0399  251 GLN A CG  
1974 C CG  B GLN A 250 ? 0.1981 0.2883 0.2749 -0.0513 -0.0044 0.0395  251 GLN A CG  
1975 C CD  A GLN A 250 ? 0.2136 0.3164 0.3014 -0.0579 -0.0002 0.0453  251 GLN A CD  
1976 C CD  B GLN A 250 ? 0.2338 0.3232 0.3195 -0.0610 -0.0065 0.0427  251 GLN A CD  
1977 O OE1 A GLN A 250 ? 0.2234 0.3404 0.3228 -0.0602 -0.0009 0.0451  251 GLN A OE1 
1978 O OE1 B GLN A 250 ? 0.2391 0.3346 0.3298 -0.0658 -0.0018 0.0487  251 GLN A OE1 
1979 N NE2 A GLN A 250 ? 0.2347 0.3311 0.3193 -0.0618 0.0031  0.0506  251 GLN A NE2 
1980 N NE2 B GLN A 250 ? 0.2059 0.2869 0.2929 -0.0642 -0.0136 0.0388  251 GLN A NE2 
1981 N N   . ARG A 251 ? 0.1796 0.2460 0.2384 -0.0418 -0.0158 0.0262  252 ARG A N   
1982 C CA  . ARG A 251 ? 0.1636 0.2145 0.2144 -0.0407 -0.0176 0.0245  252 ARG A CA  
1983 C C   . ARG A 251 ? 0.2061 0.2539 0.2473 -0.0330 -0.0163 0.0215  252 ARG A C   
1984 O O   . ARG A 251 ? 0.1863 0.2265 0.2217 -0.0304 -0.0145 0.0223  252 ARG A O   
1985 C CB  . ARG A 251 ? 0.1793 0.2220 0.2316 -0.0448 -0.0243 0.0204  252 ARG A CB  
1986 C CG  . ARG A 251 ? 0.1927 0.2343 0.2543 -0.0541 -0.0258 0.0241  252 ARG A CG  
1987 C CD  . ARG A 251 ? 0.2456 0.2841 0.3118 -0.0592 -0.0333 0.0194  252 ARG A CD  
1988 N NE  . ARG A 251 ? 0.3853 0.4086 0.4423 -0.0560 -0.0383 0.0128  252 ARG A NE  
1989 C CZ  . ARG A 251 ? 0.3841 0.3915 0.4398 -0.0598 -0.0421 0.0115  252 ARG A CZ  
1990 N NH1 . ARG A 251 ? 0.4438 0.4469 0.5058 -0.0671 -0.0412 0.0175  252 ARG A NH1 
1991 N NH2 . ARG A 251 ? 0.4232 0.4180 0.4704 -0.0559 -0.0469 0.0041  252 ARG A NH2 
1992 N N   . ALA A 252 ? 0.1754 0.2298 0.2154 -0.0294 -0.0173 0.0186  253 ALA A N   
1993 C CA  . ALA A 252 ? 0.1535 0.2065 0.1852 -0.0229 -0.0155 0.0168  253 ALA A CA  
1994 C C   . ALA A 252 ? 0.1745 0.2291 0.2045 -0.0207 -0.0101 0.0205  253 ALA A C   
1995 O O   . ALA A 252 ? 0.1825 0.2316 0.2065 -0.0176 -0.0086 0.0201  253 ALA A O   
1996 C CB  . ALA A 252 ? 0.1614 0.2218 0.1926 -0.0201 -0.0171 0.0149  253 ALA A CB  
1997 N N   . ILE A 253 ? 0.1566 0.2196 0.1917 -0.0221 -0.0072 0.0237  254 ILE A N   
1998 C CA  . ILE A 253 ? 0.1657 0.2301 0.1980 -0.0199 -0.0025 0.0264  254 ILE A CA  
1999 C C   . ILE A 253 ? 0.1860 0.2431 0.2155 -0.0217 -0.0015 0.0288  254 ILE A C   
2000 O O   . ILE A 253 ? 0.1694 0.2229 0.1933 -0.0188 0.0000  0.0289  254 ILE A O   
2001 C CB  . ILE A 253 ? 0.1804 0.2553 0.2184 -0.0206 0.0006  0.0288  254 ILE A CB  
2002 C CG1 . ILE A 253 ? 0.1630 0.2445 0.2030 -0.0171 -0.0007 0.0267  254 ILE A CG1 
2003 C CG2 . ILE A 253 ? 0.1842 0.2591 0.2178 -0.0187 0.0052  0.0309  254 ILE A CG2 
2004 C CD1 . ILE A 253 ? 0.1920 0.2853 0.2403 -0.0174 0.0013  0.0283  254 ILE A CD1 
2005 N N   . ASN A 254 ? 0.1587 0.2136 0.1923 -0.0267 -0.0026 0.0309  255 ASN A N   
2006 C CA  . ASN A 254 ? 0.2094 0.2563 0.2400 -0.0283 -0.0022 0.0341  255 ASN A CA  
2007 C C   . ASN A 254 ? 0.1843 0.2215 0.2093 -0.0245 -0.0047 0.0312  255 ASN A C   
2008 O O   . ASN A 254 ? 0.1972 0.2300 0.2179 -0.0226 -0.0038 0.0331  255 ASN A O   
2009 C CB  . ASN A 254 ? 0.1955 0.2398 0.2317 -0.0350 -0.0036 0.0371  255 ASN A CB  
2010 C CG  . ASN A 254 ? 0.2159 0.2706 0.2572 -0.0388 0.0006  0.0418  255 ASN A CG  
2011 O OD1 . ASN A 254 ? 0.2935 0.3533 0.3311 -0.0361 0.0049  0.0438  255 ASN A OD1 
2012 N ND2 . ASN A 254 ? 0.2620 0.3205 0.3118 -0.0450 -0.0005 0.0435  255 ASN A ND2 
2013 N N   . GLU A 255 ? 0.1938 0.2285 0.2185 -0.0230 -0.0079 0.0265  256 GLU A N   
2014 C CA  . GLU A 255 ? 0.2025 0.2298 0.2221 -0.0186 -0.0095 0.0232  256 GLU A CA  
2015 C C   . GLU A 255 ? 0.2221 0.2534 0.2379 -0.0140 -0.0065 0.0233  256 GLU A C   
2016 O O   . GLU A 255 ? 0.2014 0.2284 0.2146 -0.0109 -0.0067 0.0229  256 GLU A O   
2017 C CB  . GLU A 255 ? 0.2183 0.2438 0.2370 -0.0175 -0.0128 0.0177  256 GLU A CB  
2018 C CG  . GLU A 255 ? 0.2246 0.2408 0.2386 -0.0135 -0.0149 0.0137  256 GLU A CG  
2019 C CD  . GLU A 255 ? 0.2422 0.2465 0.2574 -0.0159 -0.0180 0.0141  256 GLU A CD  
2020 O OE1 . GLU A 255 ? 0.2666 0.2680 0.2857 -0.0216 -0.0208 0.0145  256 GLU A OE1 
2021 O OE2 . GLU A 255 ? 0.2745 0.2720 0.2872 -0.0122 -0.0179 0.0143  256 GLU A OE2 
2022 N N   . THR A 256 ? 0.1646 0.2039 0.1807 -0.0136 -0.0041 0.0239  257 THR A N   
2023 C CA  . THR A 256 ? 0.1794 0.2213 0.1922 -0.0102 -0.0018 0.0239  257 THR A CA  
2024 C C   . THR A 256 ? 0.2114 0.2532 0.2231 -0.0107 -0.0001 0.0272  257 THR A C   
2025 O O   . THR A 256 ? 0.2186 0.2620 0.2280 -0.0086 0.0009  0.0271  257 THR A O   
2026 C CB  . THR A 256 ? 0.2252 0.2734 0.2379 -0.0093 -0.0002 0.0233  257 THR A CB  
2027 O OG1 . THR A 256 ? 0.1928 0.2453 0.2079 -0.0112 0.0016  0.0257  257 THR A OG1 
2028 C CG2 . THR A 256 ? 0.1970 0.2459 0.2098 -0.0087 -0.0024 0.0205  257 THR A CG2 
2029 N N   . HIS A 257 ? 0.1837 0.2240 0.1965 -0.0137 0.0000  0.0304  258 HIS A N   
2030 C CA  . HIS A 257 ? 0.1935 0.2336 0.2035 -0.0141 0.0013  0.0338  258 HIS A CA  
2031 C C   . HIS A 257 ? 0.2463 0.2791 0.2545 -0.0131 -0.0011 0.0354  258 HIS A C   
2032 O O   . HIS A 257 ? 0.2564 0.2887 0.2613 -0.0127 -0.0009 0.0384  258 HIS A O   
2033 C CB  . HIS A 257 ? 0.2130 0.2564 0.2241 -0.0177 0.0036  0.0373  258 HIS A CB  
2034 C CG  . HIS A 257 ? 0.1876 0.2390 0.2008 -0.0175 0.0061  0.0359  258 HIS A CG  
2035 N ND1 . HIS A 257 ? 0.2147 0.2722 0.2309 -0.0201 0.0088  0.0383  258 HIS A ND1 
2036 C CD2 . HIS A 257 ? 0.1932 0.2476 0.2061 -0.0146 0.0064  0.0327  258 HIS A CD2 
2037 C CE1 . HIS A 257 ? 0.1886 0.2526 0.2066 -0.0180 0.0105  0.0360  258 HIS A CE1 
2038 N NE2 . HIS A 257 ? 0.1812 0.2424 0.1967 -0.0147 0.0088  0.0328  258 HIS A NE2 
2039 N N   . GLN A 258 ? 0.2161 0.2428 0.2260 -0.0121 -0.0037 0.0333  259 GLN A N   
2040 C CA  . GLN A 258 ? 0.2331 0.2517 0.2419 -0.0103 -0.0063 0.0348  259 GLN A CA  
2041 C C   . GLN A 258 ? 0.2294 0.2501 0.2373 -0.0051 -0.0069 0.0328  259 GLN A C   
2042 O O   . GLN A 258 ? 0.2073 0.2303 0.2164 -0.0023 -0.0067 0.0286  259 GLN A O   
2043 C CB  . GLN A 258 ? 0.2511 0.2609 0.2618 -0.0111 -0.0092 0.0327  259 GLN A CB  
2044 C CG  . GLN A 258 ? 0.3157 0.3149 0.3250 -0.0085 -0.0122 0.0343  259 GLN A CG  
2045 C CD  . GLN A 258 ? 0.4187 0.4072 0.4291 -0.0085 -0.0154 0.0309  259 GLN A CD  
2046 O OE1 . GLN A 258 ? 0.4778 0.4664 0.4901 -0.0123 -0.0159 0.0286  259 GLN A OE1 
2047 N NE2 . GLN A 258 ? 0.4510 0.4301 0.4603 -0.0038 -0.0182 0.0300  259 GLN A NE2 
2048 N N   . GLY A 259 ? 0.2394 0.2602 0.2452 -0.0039 -0.0076 0.0361  260 GLY A N   
2049 C CA  . GLY A 259 ? 0.2396 0.2635 0.2464 0.0008  -0.0088 0.0347  260 GLY A CA  
2050 C C   . GLY A 259 ? 0.2212 0.2392 0.2303 0.0052  -0.0110 0.0322  260 GLY A C   
2051 O O   . GLY A 259 ? 0.2401 0.2480 0.2484 0.0051  -0.0132 0.0336  260 GLY A O   
2052 N N   . ARG A 260 ? 0.1699 0.1940 0.1819 0.0092  -0.0102 0.0285  261 ARG A N   
2053 C CA  . ARG A 260 ? 0.1875 0.2077 0.2013 0.0145  -0.0113 0.0249  261 ARG A CA  
2054 C C   . ARG A 260 ? 0.2101 0.2338 0.2274 0.0203  -0.0129 0.0254  261 ARG A C   
2055 O O   . ARG A 260 ? 0.2444 0.2619 0.2629 0.0257  -0.0149 0.0238  261 ARG A O   
2056 C CB  . ARG A 260 ? 0.1847 0.2102 0.1989 0.0153  -0.0084 0.0200  261 ARG A CB  
2057 C CG  . ARG A 260 ? 0.1837 0.2075 0.1951 0.0100  -0.0074 0.0195  261 ARG A CG  
2058 C CD  . ARG A 260 ? 0.1866 0.1988 0.1966 0.0083  -0.0102 0.0191  261 ARG A CD  
2059 N NE  . ARG A 260 ? 0.1752 0.1882 0.1845 0.0031  -0.0097 0.0189  261 ARG A NE  
2060 C CZ  . ARG A 260 ? 0.2469 0.2528 0.2558 0.0008  -0.0120 0.0167  261 ARG A CZ  
2061 N NH1 . ARG A 260 ? 0.2467 0.2423 0.2546 0.0035  -0.0149 0.0138  261 ARG A NH1 
2062 N NH2 . ARG A 260 ? 0.2333 0.2424 0.2431 -0.0041 -0.0117 0.0172  261 ARG A NH2 
2063 N N   . TYR A 261 ? 0.1664 0.2000 0.1857 0.0195  -0.0125 0.0275  262 TYR A N   
2064 C CA  . TYR A 261 ? 0.1672 0.2062 0.1910 0.0243  -0.0150 0.0287  262 TYR A CA  
2065 C C   . TYR A 261 ? 0.1591 0.2065 0.1827 0.0204  -0.0154 0.0314  262 TYR A C   
2066 O O   . TYR A 261 ? 0.1569 0.2051 0.1770 0.0150  -0.0133 0.0316  262 TYR A O   
2067 C CB  . TYR A 261 ? 0.1642 0.2111 0.1942 0.0300  -0.0131 0.0244  262 TYR A CB  
2068 C CG  . TYR A 261 ? 0.1705 0.2279 0.2021 0.0270  -0.0086 0.0221  262 TYR A CG  
2069 C CD1 . TYR A 261 ? 0.1478 0.2159 0.1828 0.0237  -0.0081 0.0238  262 TYR A CD1 
2070 C CD2 . TYR A 261 ? 0.1546 0.2102 0.1837 0.0273  -0.0054 0.0183  262 TYR A CD2 
2071 C CE1 . TYR A 261 ? 0.1412 0.2170 0.1775 0.0204  -0.0042 0.0225  262 TYR A CE1 
2072 C CE2 . TYR A 261 ? 0.1505 0.2148 0.1801 0.0245  -0.0013 0.0172  262 TYR A CE2 
2073 C CZ  . TYR A 261 ? 0.1514 0.2253 0.1848 0.0210  -0.0007 0.0197  262 TYR A CZ  
2074 O OH  . TYR A 261 ? 0.1378 0.2186 0.1716 0.0179  0.0031  0.0194  262 TYR A OH  
2075 N N   . GLN A 262 ? 0.1690 0.2228 0.1967 0.0236  -0.0185 0.0330  263 GLN A N   
2076 C CA  . GLN A 262 ? 0.1932 0.2540 0.2203 0.0203  -0.0205 0.0351  263 GLN A CA  
2077 C C   . GLN A 262 ? 0.1799 0.2551 0.2162 0.0217  -0.0203 0.0330  263 GLN A C   
2078 O O   . GLN A 262 ? 0.1780 0.2582 0.2216 0.0274  -0.0206 0.0317  263 GLN A O   
2079 C CB  . GLN A 262 ? 0.2699 0.3257 0.2930 0.0222  -0.0256 0.0396  263 GLN A CB  
2080 C CG  . GLN A 262 ? 0.2346 0.2955 0.2540 0.0187  -0.0282 0.0415  263 GLN A CG  
2081 C CD  . GLN A 262 ? 0.2924 0.3462 0.3044 0.0201  -0.0327 0.0467  263 GLN A CD  
2082 O OE1 . GLN A 262 ? 0.3164 0.3610 0.3272 0.0237  -0.0340 0.0494  263 GLN A OE1 
2083 N NE2 . GLN A 262 ? 0.3265 0.3837 0.3327 0.0171  -0.0352 0.0483  263 GLN A NE2 
2084 N N   . VAL A 263 ? 0.1590 0.2407 0.1954 0.0163  -0.0198 0.0327  264 VAL A N   
2085 C CA  . VAL A 263 ? 0.1651 0.2608 0.2107 0.0157  -0.0209 0.0318  264 VAL A CA  
2086 C C   . VAL A 263 ? 0.2085 0.3057 0.2504 0.0115  -0.0254 0.0332  264 VAL A C   
2087 O O   . VAL A 263 ? 0.1769 0.2709 0.2132 0.0060  -0.0239 0.0323  264 VAL A O   
2088 C CB  . VAL A 263 ? 0.1722 0.2744 0.2223 0.0125  -0.0157 0.0293  264 VAL A CB  
2089 C CG1 . VAL A 263 ? 0.1710 0.2877 0.2313 0.0105  -0.0171 0.0293  264 VAL A CG1 
2090 C CG2 . VAL A 263 ? 0.2009 0.3026 0.2534 0.0174  -0.0115 0.0274  264 VAL A CG2 
2091 N N   . ASN A 264 ? 0.2191 0.3211 0.2639 0.0146  -0.0311 0.0351  265 ASN A N   
2092 C CA  . ASN A 264 ? 0.2547 0.3571 0.2938 0.0114  -0.0364 0.0363  265 ASN A CA  
2093 C C   . ASN A 264 ? 0.2612 0.3503 0.2860 0.0090  -0.0352 0.0377  265 ASN A C   
2094 O O   . ASN A 264 ? 0.2796 0.3600 0.2993 0.0122  -0.0349 0.0404  265 ASN A O   
2095 C CB  . ASN A 264 ? 0.2521 0.3643 0.2969 0.0055  -0.0371 0.0337  265 ASN A CB  
2096 C CG  . ASN A 264 ? 0.2327 0.3606 0.2934 0.0073  -0.0377 0.0331  265 ASN A CG  
2097 O OD1 . ASN A 264 ? 0.2692 0.4022 0.3363 0.0139  -0.0398 0.0344  265 ASN A OD1 
2098 N ND2 . ASN A 264 ? 0.2381 0.3738 0.3056 0.0016  -0.0356 0.0312  265 ASN A ND2 
2099 N N   . THR A 265 ? 0.2234 0.3108 0.2421 0.0034  -0.0342 0.0358  266 THR A N   
2100 C CA  . THR A 265 ? 0.2426 0.3197 0.2482 0.0015  -0.0326 0.0369  266 THR A CA  
2101 C C   . THR A 265 ? 0.2212 0.2921 0.2252 -0.0001 -0.0260 0.0357  266 THR A C   
2102 O O   . THR A 265 ? 0.2520 0.3162 0.2469 -0.0017 -0.0238 0.0364  266 THR A O   
2103 C CB  . THR A 265 ? 0.2350 0.3130 0.2335 -0.0026 -0.0354 0.0348  266 THR A CB  
2104 O OG1 . THR A 265 ? 0.2511 0.3340 0.2565 -0.0064 -0.0343 0.0310  266 THR A OG1 
2105 C CG2 . THR A 265 ? 0.2474 0.3301 0.2440 -0.0009 -0.0431 0.0365  266 THR A CG2 
2106 N N   . MET A 266 ? 0.1859 0.2598 0.1984 0.0005  -0.0228 0.0340  267 MET A N   
2107 C CA  . MET A 266 ? 0.1659 0.2349 0.1771 -0.0008 -0.0174 0.0327  267 MET A CA  
2108 C C   . MET A 266 ? 0.1871 0.2520 0.2003 0.0029  -0.0159 0.0338  267 MET A C   
2109 O O   . MET A 266 ? 0.2054 0.2734 0.2245 0.0069  -0.0176 0.0341  267 MET A O   
2110 C CB  . MET A 266 ? 0.1726 0.2471 0.1899 -0.0032 -0.0149 0.0299  267 MET A CB  
2111 C CG  . MET A 266 ? 0.2437 0.3139 0.2597 -0.0039 -0.0100 0.0288  267 MET A CG  
2112 S SD  . MET A 266 ? 0.2729 0.3486 0.2946 -0.0070 -0.0072 0.0270  267 MET A SD  
2113 C CE  . MET A 266 ? 0.2630 0.3476 0.2942 -0.0030 -0.0063 0.0272  267 MET A CE  
2114 N N   . TYR A 267 ? 0.1717 0.2294 0.1800 0.0017  -0.0131 0.0343  268 TYR A N   
2115 C CA  . TYR A 267 ? 0.1672 0.2196 0.1772 0.0039  -0.0117 0.0343  268 TYR A CA  
2116 C C   . TYR A 267 ? 0.1695 0.2230 0.1814 0.0026  -0.0079 0.0313  268 TYR A C   
2117 O O   . TYR A 267 ? 0.1859 0.2392 0.1947 -0.0006 -0.0058 0.0307  268 TYR A O   
2118 C CB  . TYR A 267 ? 0.2035 0.2475 0.2074 0.0026  -0.0119 0.0376  268 TYR A CB  
2119 C CG  . TYR A 267 ? 0.2229 0.2646 0.2229 0.0040  -0.0157 0.0417  268 TYR A CG  
2120 C CD1 . TYR A 267 ? 0.2331 0.2771 0.2269 0.0019  -0.0167 0.0432  268 TYR A CD1 
2121 C CD2 . TYR A 267 ? 0.2920 0.3282 0.2936 0.0078  -0.0186 0.0439  268 TYR A CD2 
2122 C CE1 . TYR A 267 ? 0.2725 0.3144 0.2611 0.0033  -0.0205 0.0473  268 TYR A CE1 
2123 C CE2 . TYR A 267 ? 0.3505 0.3838 0.3477 0.0094  -0.0225 0.0485  268 TYR A CE2 
2124 C CZ  . TYR A 267 ? 0.2936 0.3303 0.2840 0.0070  -0.0235 0.0504  268 TYR A CZ  
2125 O OH  . TYR A 267 ? 0.3217 0.3557 0.3063 0.0088  -0.0278 0.0553  268 TYR A OH  
2126 N N   . GLN A 268 ? 0.1411 0.1957 0.1573 0.0056  -0.0070 0.0292  269 GLN A N   
2127 C CA  . GLN A 268 ? 0.1468 0.2024 0.1633 0.0048  -0.0037 0.0266  269 GLN A CA  
2128 C C   . GLN A 268 ? 0.1790 0.2267 0.1925 0.0043  -0.0035 0.0263  269 GLN A C   
2129 O O   . GLN A 268 ? 0.1807 0.2231 0.1947 0.0071  -0.0050 0.0258  269 GLN A O   
2130 C CB  . GLN A 268 ? 0.1442 0.2057 0.1657 0.0083  -0.0024 0.0244  269 GLN A CB  
2131 C CG  . GLN A 268 ? 0.1384 0.2012 0.1586 0.0077  0.0011  0.0221  269 GLN A CG  
2132 C CD  . GLN A 268 ? 0.1767 0.2424 0.1957 0.0034  0.0027  0.0232  269 GLN A CD  
2133 O OE1 . GLN A 268 ? 0.1553 0.2272 0.1777 0.0019  0.0031  0.0240  269 GLN A OE1 
2134 N NE2 . GLN A 268 ? 0.1473 0.2083 0.1619 0.0012  0.0034  0.0232  269 GLN A NE2 
2135 N N   . ALA A 269 ? 0.1563 0.2030 0.1671 0.0010  -0.0020 0.0266  270 ALA A N   
2136 C CA  . ALA A 269 ? 0.1547 0.1964 0.1642 -0.0002 -0.0018 0.0258  270 ALA A CA  
2137 C C   . ALA A 269 ? 0.1741 0.2184 0.1838 0.0007  -0.0002 0.0228  270 ALA A C   
2138 O O   . ALA A 269 ? 0.1773 0.2263 0.1879 0.0024  0.0011  0.0216  270 ALA A O   
2139 C CB  . ALA A 269 ? 0.2029 0.2440 0.2105 -0.0039 -0.0011 0.0282  270 ALA A CB  
2140 N N   . LEU A 270 ? 0.1954 0.2373 0.2040 -0.0008 -0.0005 0.0217  271 LEU A N   
2141 C CA  . LEU A 270 ? 0.2072 0.2516 0.2143 0.0002  0.0006  0.0192  271 LEU A CA  
2142 C C   . LEU A 270 ? 0.1915 0.2400 0.1979 -0.0015 0.0024  0.0207  271 LEU A C   
2143 O O   . LEU A 270 ? 0.1931 0.2416 0.1998 -0.0035 0.0023  0.0219  271 LEU A O   
2144 C CB  . LEU A 270 ? 0.2213 0.2619 0.2277 -0.0006 -0.0015 0.0171  271 LEU A CB  
2145 C CG  . LEU A 270 ? 0.2440 0.2775 0.2505 0.0006  -0.0040 0.0152  271 LEU A CG  
2146 C CD1 . LEU A 270 ? 0.2417 0.2717 0.2476 -0.0014 -0.0066 0.0127  271 LEU A CD1 
2147 C CD2 . LEU A 270 ? 0.2862 0.3202 0.2913 0.0055  -0.0031 0.0124  271 LEU A CD2 
2148 N N   . GLY A 271 ? 0.1777 0.2298 0.1835 -0.0005 0.0042  0.0208  272 GLY A N   
2149 C CA  . GLY A 271 ? 0.1710 0.2248 0.1758 -0.0020 0.0057  0.0223  272 GLY A CA  
2150 C C   . GLY A 271 ? 0.1448 0.1985 0.1505 -0.0037 0.0056  0.0238  272 GLY A C   
2151 O O   . GLY A 271 ? 0.1668 0.2223 0.1732 -0.0045 0.0062  0.0243  272 GLY A O   
2152 N N   . TRP A 272 ? 0.1652 0.2171 0.1708 -0.0046 0.0048  0.0244  273 TRP A N   
2153 C CA  . TRP A 272 ? 0.1653 0.2168 0.1698 -0.0058 0.0047  0.0255  273 TRP A CA  
2154 C C   . TRP A 272 ? 0.1620 0.2145 0.1676 -0.0055 0.0032  0.0260  273 TRP A C   
2155 O O   . TRP A 272 ? 0.1624 0.2145 0.1699 -0.0039 0.0021  0.0260  273 TRP A O   
2156 C CB  . TRP A 272 ? 0.1577 0.2082 0.1615 -0.0067 0.0048  0.0267  273 TRP A CB  
2157 C CG  . TRP A 272 ? 0.1792 0.2310 0.1835 -0.0068 0.0061  0.0263  273 TRP A CG  
2158 C CD1 . TRP A 272 ? 0.1793 0.2320 0.1864 -0.0072 0.0056  0.0262  273 TRP A CD1 
2159 C CD2 . TRP A 272 ? 0.1793 0.2320 0.1819 -0.0062 0.0077  0.0259  273 TRP A CD2 
2160 N NE1 . TRP A 272 ? 0.2122 0.2680 0.2203 -0.0067 0.0067  0.0260  273 TRP A NE1 
2161 C CE2 . TRP A 272 ? 0.1829 0.2383 0.1882 -0.0056 0.0083  0.0258  273 TRP A CE2 
2162 C CE3 . TRP A 272 ? 0.1625 0.2136 0.1617 -0.0059 0.0082  0.0251  273 TRP A CE3 
2163 C CZ2 . TRP A 272 ? 0.1750 0.2319 0.1800 -0.0039 0.0098  0.0252  273 TRP A CZ2 
2164 C CZ3 . TRP A 272 ? 0.1452 0.1960 0.1430 -0.0044 0.0097  0.0241  273 TRP A CZ3 
2165 C CH2 . TRP A 272 ? 0.1904 0.2444 0.1913 -0.0029 0.0107  0.0243  273 TRP A CH2 
2166 N N   . GLU A 273 ? 0.1488 0.2020 0.1529 -0.0067 0.0026  0.0263  274 GLU A N   
2167 C CA  . GLU A 273 ? 0.1639 0.2185 0.1683 -0.0065 0.0002  0.0271  274 GLU A CA  
2168 C C   . GLU A 273 ? 0.1826 0.2345 0.1822 -0.0070 -0.0004 0.0287  274 GLU A C   
2169 O O   . GLU A 273 ? 0.1895 0.2402 0.1854 -0.0079 0.0012  0.0283  274 GLU A O   
2170 C CB  . GLU A 273 ? 0.1774 0.2348 0.1828 -0.0082 -0.0008 0.0262  274 GLU A CB  
2171 C CG  . GLU A 273 ? 0.1861 0.2473 0.1966 -0.0083 0.0006  0.0257  274 GLU A CG  
2172 C CD  . GLU A 273 ? 0.2434 0.3062 0.2553 -0.0115 0.0002  0.0253  274 GLU A CD  
2173 O OE1 . GLU A 273 ? 0.2805 0.3406 0.2890 -0.0134 -0.0017 0.0245  274 GLU A OE1 
2174 O OE2 . GLU A 273 ? 0.2633 0.3300 0.2794 -0.0123 0.0019  0.0257  274 GLU A OE2 
2175 N N   . GLU A 274 ? 0.1571 0.2083 0.1567 -0.0059 -0.0026 0.0307  275 GLU A N   
2176 C CA  . GLU A 274 ? 0.1649 0.2131 0.1594 -0.0065 -0.0029 0.0335  275 GLU A CA  
2177 C C   . GLU A 274 ? 0.1816 0.2309 0.1726 -0.0060 -0.0062 0.0348  275 GLU A C   
2178 O O   . GLU A 274 ? 0.1771 0.2291 0.1721 -0.0044 -0.0090 0.0345  275 GLU A O   
2179 C CB  . GLU A 274 ? 0.1849 0.2292 0.1815 -0.0059 -0.0031 0.0356  275 GLU A CB  
2180 C CG  . GLU A 274 ? 0.2161 0.2566 0.2082 -0.0071 -0.0034 0.0399  275 GLU A CG  
2181 C CD  . GLU A 274 ? 0.3040 0.3388 0.2991 -0.0073 -0.0041 0.0417  275 GLU A CD  
2182 O OE1 . GLU A 274 ? 0.3593 0.3930 0.3590 -0.0054 -0.0049 0.0389  275 GLU A OE1 
2183 O OE2 . GLU A 274 ? 0.3774 0.4084 0.3697 -0.0095 -0.0036 0.0457  275 GLU A OE2 
2184 N N   . PHE A 275 ? 0.1768 0.2250 0.1602 -0.0071 -0.0058 0.0363  276 PHE A N   
2185 C CA  . PHE A 275 ? 0.1808 0.2298 0.1586 -0.0066 -0.0094 0.0374  276 PHE A CA  
2186 C C   . PHE A 275 ? 0.1701 0.2161 0.1396 -0.0070 -0.0085 0.0417  276 PHE A C   
2187 O O   . PHE A 275 ? 0.2090 0.2542 0.1762 -0.0083 -0.0043 0.0425  276 PHE A O   
2188 C CB  . PHE A 275 ? 0.1861 0.2372 0.1603 -0.0079 -0.0102 0.0335  276 PHE A CB  
2189 C CG  . PHE A 275 ? 0.1873 0.2407 0.1691 -0.0087 -0.0101 0.0300  276 PHE A CG  
2190 C CD1 . PHE A 275 ? 0.2066 0.2584 0.1901 -0.0094 -0.0062 0.0281  276 PHE A CD1 
2191 C CD2 . PHE A 275 ? 0.2028 0.2605 0.1903 -0.0088 -0.0138 0.0293  276 PHE A CD2 
2192 C CE1 . PHE A 275 ? 0.1843 0.2375 0.1737 -0.0103 -0.0059 0.0260  276 PHE A CE1 
2193 C CE2 . PHE A 275 ? 0.1702 0.2308 0.1650 -0.0102 -0.0130 0.0271  276 PHE A CE2 
2194 C CZ  . PHE A 275 ? 0.1823 0.2398 0.1772 -0.0111 -0.0090 0.0256  276 PHE A CZ  
2195 N N   . SER A 276 ? 0.1951 0.2403 0.1601 -0.0057 -0.0126 0.0449  277 SER A N   
2196 C CA  . SER A 276 ? 0.2062 0.2488 0.1609 -0.0063 -0.0118 0.0494  277 SER A CA  
2197 C C   . SER A 276 ? 0.2374 0.2824 0.1831 -0.0073 -0.0094 0.0464  277 SER A C   
2198 O O   . SER A 276 ? 0.2304 0.2776 0.1752 -0.0071 -0.0118 0.0416  277 SER A O   
2199 C CB  . SER A 276 ? 0.2566 0.2976 0.2072 -0.0041 -0.0176 0.0535  277 SER A CB  
2200 O OG  . SER A 276 ? 0.2920 0.3305 0.2306 -0.0048 -0.0168 0.0586  277 SER A OG  
2201 N N   . TYR A 277 ? 0.2282 0.2729 0.1678 -0.0085 -0.0045 0.0490  278 TYR A N   
2202 C CA  . TYR A 277 ? 0.2474 0.2946 0.1785 -0.0085 -0.0011 0.0457  278 TYR A CA  
2203 C C   . TYR A 277 ? 0.2391 0.2859 0.1557 -0.0079 -0.0019 0.0491  278 TYR A C   
2204 O O   . TYR A 277 ? 0.3044 0.3497 0.2180 -0.0088 -0.0009 0.0561  278 TYR A O   
2205 C CB  . TYR A 277 ? 0.2281 0.2777 0.1630 -0.0095 0.0059  0.0456  278 TYR A CB  
2206 C CG  . TYR A 277 ? 0.2700 0.3226 0.1961 -0.0081 0.0099  0.0419  278 TYR A CG  
2207 C CD1 . TYR A 277 ? 0.3044 0.3562 0.2309 -0.0065 0.0091  0.0347  278 TYR A CD1 
2208 C CD2 . TYR A 277 ? 0.3447 0.4003 0.2621 -0.0083 0.0148  0.0455  278 TYR A CD2 
2209 C CE1 . TYR A 277 ? 0.3028 0.3557 0.2207 -0.0044 0.0125  0.0305  278 TYR A CE1 
2210 C CE2 . TYR A 277 ? 0.3375 0.3962 0.2463 -0.0060 0.0189  0.0414  278 TYR A CE2 
2211 C CZ  . TYR A 277 ? 0.3190 0.3758 0.2281 -0.0037 0.0176  0.0334  278 TYR A CZ  
2212 O OH  . TYR A 277 ? 0.4503 0.5088 0.3504 -0.0006 0.0215  0.0285  278 TYR A OH  
2213 N N   . PRO A 278 ? 0.2460 0.2937 0.1525 -0.0067 -0.0039 0.0445  279 PRO A N   
2214 C CA  . PRO A 278 ? 0.2559 0.3036 0.1648 -0.0063 -0.0056 0.0364  279 PRO A CA  
2215 C C   . PRO A 278 ? 0.2371 0.2846 0.1549 -0.0068 -0.0123 0.0346  279 PRO A C   
2216 O O   . PRO A 278 ? 0.2550 0.3030 0.1717 -0.0064 -0.0177 0.0378  279 PRO A O   
2217 C CB  . PRO A 278 ? 0.2619 0.3092 0.1545 -0.0049 -0.0064 0.0329  279 PRO A CB  
2218 C CG  . PRO A 278 ? 0.2931 0.3419 0.1751 -0.0045 -0.0022 0.0392  279 PRO A CG  
2219 C CD  . PRO A 278 ? 0.2672 0.3151 0.1573 -0.0059 -0.0036 0.0471  279 PRO A CD  
2220 N N   . ALA A 279 ? 0.2459 0.2932 0.1730 -0.0076 -0.0118 0.0299  280 ALA A N   
2221 C CA  . ALA A 279 ? 0.2529 0.3016 0.1882 -0.0087 -0.0174 0.0276  280 ALA A CA  
2222 C C   . ALA A 279 ? 0.2400 0.2875 0.1680 -0.0098 -0.0217 0.0219  280 ALA A C   
2223 O O   . ALA A 279 ? 0.2590 0.3029 0.1806 -0.0096 -0.0189 0.0174  280 ALA A O   
2224 C CB  . ALA A 279 ? 0.2234 0.2723 0.1714 -0.0096 -0.0147 0.0261  280 ALA A CB  
2225 N N   . THR A 280 ? 0.2248 0.2752 0.1541 -0.0107 -0.0288 0.0218  281 THR A N   
2226 C CA  . THR A 280 ? 0.2216 0.2708 0.1461 -0.0128 -0.0338 0.0157  281 THR A CA  
2227 C C   . THR A 280 ? 0.2222 0.2690 0.1562 -0.0155 -0.0322 0.0115  281 THR A C   
2228 O O   . THR A 280 ? 0.2268 0.2757 0.1727 -0.0158 -0.0292 0.0138  281 THR A O   
2229 C CB  . THR A 280 ? 0.2441 0.2987 0.1706 -0.0137 -0.0425 0.0164  281 THR A CB  
2230 O OG1 . THR A 280 ? 0.2527 0.3131 0.1962 -0.0148 -0.0436 0.0184  281 THR A OG1 
2231 C CG2 . THR A 280 ? 0.2633 0.3193 0.1801 -0.0106 -0.0446 0.0219  281 THR A CG2 
2232 N N   . LEU A 281 ? 0.2290 0.2706 0.1567 -0.0174 -0.0345 0.0051  282 LEU A N   
2233 C CA  . LEU A 281 ? 0.2193 0.2573 0.1558 -0.0205 -0.0337 0.0018  282 LEU A CA  
2234 C C   . LEU A 281 ? 0.2120 0.2572 0.1636 -0.0240 -0.0373 0.0042  282 LEU A C   
2235 O O   . LEU A 281 ? 0.2209 0.2668 0.1831 -0.0252 -0.0339 0.0056  282 LEU A O   
2236 C CB  . LEU A 281 ? 0.2699 0.2993 0.1970 -0.0224 -0.0370 -0.0056 282 LEU A CB  
2237 C CG  . LEU A 281 ? 0.2334 0.2567 0.1685 -0.0264 -0.0373 -0.0088 282 LEU A CG  
2238 C CD1 . LEU A 281 ? 0.2447 0.2651 0.1852 -0.0241 -0.0297 -0.0065 282 LEU A CD1 
2239 C CD2 . LEU A 281 ? 0.3054 0.3180 0.2293 -0.0279 -0.0414 -0.0167 282 LEU A CD2 
2240 N N   . GLN A 282 ? 0.2392 0.2912 0.1922 -0.0251 -0.0441 0.0050  283 GLN A N   
2241 C CA  . GLN A 282 ? 0.2556 0.3171 0.2244 -0.0278 -0.0471 0.0073  283 GLN A CA  
2242 C C   . GLN A 282 ? 0.2267 0.2931 0.2052 -0.0247 -0.0417 0.0126  283 GLN A C   
2243 O O   . GLN A 282 ? 0.2234 0.2946 0.2146 -0.0267 -0.0401 0.0137  283 GLN A O   
2244 C CB  . GLN A 282 ? 0.2569 0.3263 0.2258 -0.0282 -0.0556 0.0077  283 GLN A CB  
2245 C CG  . GLN A 282 ? 0.2790 0.3598 0.2654 -0.0319 -0.0596 0.0086  283 GLN A CG  
2246 C CD  . GLN A 282 ? 0.3292 0.4067 0.3212 -0.0388 -0.0601 0.0045  283 GLN A CD  
2247 O OE1 . GLN A 282 ? 0.3659 0.4370 0.3498 -0.0424 -0.0650 -0.0007 283 GLN A OE1 
2248 N NE2 . GLN A 282 ? 0.2911 0.3718 0.2958 -0.0406 -0.0550 0.0068  283 GLN A NE2 
2249 N N   . THR A 283 ? 0.2070 0.2724 0.1795 -0.0200 -0.0391 0.0162  284 THR A N   
2250 C CA  . THR A 283 ? 0.2261 0.2938 0.2066 -0.0172 -0.0343 0.0204  284 THR A CA  
2251 C C   . THR A 283 ? 0.2066 0.2705 0.1912 -0.0184 -0.0282 0.0192  284 THR A C   
2252 O O   . THR A 283 ? 0.2085 0.2766 0.2035 -0.0183 -0.0259 0.0208  284 THR A O   
2253 C CB  . THR A 283 ? 0.2270 0.2916 0.1991 -0.0131 -0.0324 0.0241  284 THR A CB  
2254 O OG1 . THR A 283 ? 0.2297 0.2987 0.2007 -0.0112 -0.0384 0.0268  284 THR A OG1 
2255 C CG2 . THR A 283 ? 0.2005 0.2642 0.1789 -0.0109 -0.0269 0.0273  284 THR A CG2 
2256 N N   . LEU A 284 ? 0.1987 0.2547 0.1749 -0.0190 -0.0255 0.0163  285 LEU A N   
2257 C CA  . LEU A 284 ? 0.2008 0.2528 0.1803 -0.0195 -0.0203 0.0156  285 LEU A CA  
2258 C C   . LEU A 284 ? 0.1968 0.2501 0.1848 -0.0237 -0.0217 0.0143  285 LEU A C   
2259 O O   . LEU A 284 ? 0.2045 0.2589 0.1995 -0.0240 -0.0180 0.0159  285 LEU A O   
2260 C CB  . LEU A 284 ? 0.2191 0.2630 0.1881 -0.0182 -0.0175 0.0128  285 LEU A CB  
2261 C CG  . LEU A 284 ? 0.2130 0.2569 0.1745 -0.0146 -0.0146 0.0150  285 LEU A CG  
2262 C CD1 . LEU A 284 ? 0.2411 0.2793 0.1926 -0.0128 -0.0115 0.0117  285 LEU A CD1 
2263 C CD2 . LEU A 284 ? 0.2179 0.2647 0.1864 -0.0129 -0.0108 0.0192  285 LEU A CD2 
2264 N N   . LEU A 285 ? 0.2091 0.2626 0.1966 -0.0275 -0.0271 0.0114  286 LEU A N   
2265 C CA  . LEU A 285 ? 0.2008 0.2563 0.1975 -0.0329 -0.0288 0.0107  286 LEU A CA  
2266 C C   . LEU A 285 ? 0.2234 0.2914 0.2335 -0.0332 -0.0286 0.0145  286 LEU A C   
2267 O O   . LEU A 285 ? 0.2104 0.2811 0.2290 -0.0358 -0.0257 0.0161  286 LEU A O   
2268 C CB  . LEU A 285 ? 0.2203 0.2734 0.2136 -0.0374 -0.0356 0.0065  286 LEU A CB  
2269 C CG  . LEU A 285 ? 0.2445 0.2840 0.2246 -0.0371 -0.0357 0.0014  286 LEU A CG  
2270 C CD1 . LEU A 285 ? 0.2571 0.2938 0.2324 -0.0413 -0.0434 -0.0036 286 LEU A CD1 
2271 C CD2 . LEU A 285 ? 0.2390 0.2695 0.2208 -0.0385 -0.0314 0.0011  286 LEU A CD2 
2272 N N   . ASP A 286 ? 0.2293 0.3051 0.2410 -0.0302 -0.0316 0.0161  287 ASP A N   
2273 C CA  . ASP A 286 ? 0.2295 0.3177 0.2539 -0.0289 -0.0315 0.0192  287 ASP A CA  
2274 C C   . ASP A 286 ? 0.2089 0.2972 0.2371 -0.0261 -0.0246 0.0216  287 ASP A C   
2275 O O   . ASP A 286 ? 0.2070 0.3044 0.2461 -0.0266 -0.0226 0.0232  287 ASP A O   
2276 C CB  . ASP A 286 ? 0.2323 0.3257 0.2555 -0.0242 -0.0355 0.0209  287 ASP A CB  
2277 C CG  . ASP A 286 ? 0.2610 0.3582 0.2826 -0.0267 -0.0436 0.0190  287 ASP A CG  
2278 O OD1 . ASP A 286 ? 0.2989 0.3967 0.3234 -0.0327 -0.0466 0.0162  287 ASP A OD1 
2279 O OD2 . ASP A 286 ? 0.2978 0.3966 0.3147 -0.0227 -0.0475 0.0206  287 ASP A OD2 
2280 N N   . SER A 287 ? 0.2151 0.2943 0.2346 -0.0231 -0.0208 0.0216  288 SER A N   
2281 C CA  . SER A 287 ? 0.2151 0.2941 0.2372 -0.0204 -0.0152 0.0234  288 SER A CA  
2282 C C   . SER A 287 ? 0.2239 0.3037 0.2510 -0.0240 -0.0120 0.0236  288 SER A C   
2283 O O   . SER A 287 ? 0.2238 0.3066 0.2546 -0.0221 -0.0079 0.0252  288 SER A O   
2284 C CB  . SER A 287 ? 0.2217 0.2915 0.2342 -0.0177 -0.0125 0.0233  288 SER A CB  
2285 O OG  . SER A 287 ? 0.2240 0.2863 0.2311 -0.0201 -0.0111 0.0213  288 SER A OG  
2286 N N   . ASN A 288 ? 0.2259 0.3024 0.2525 -0.0293 -0.0140 0.0221  289 ASN A N   
2287 C CA  . ASN A 288 ? 0.2518 0.3273 0.2824 -0.0335 -0.0112 0.0233  289 ASN A CA  
2288 C C   . ASN A 288 ? 0.2322 0.3165 0.2732 -0.0394 -0.0139 0.0239  289 ASN A C   
2289 O O   . ASN A 288 ? 0.2422 0.3242 0.2861 -0.0448 -0.0126 0.0250  289 ASN A O   
2290 C CB  . ASN A 288 ? 0.2842 0.3459 0.3058 -0.0349 -0.0106 0.0215  289 ASN A CB  
2291 C CG  . ASN A 288 ? 0.3637 0.4201 0.3801 -0.0303 -0.0060 0.0226  289 ASN A CG  
2292 O OD1 . ASN A 288 ? 0.3986 0.4513 0.4151 -0.0314 -0.0030 0.0243  289 ASN A OD1 
2293 N ND2 . ASN A 288 ? 0.2939 0.3502 0.3059 -0.0254 -0.0056 0.0220  289 ASN A ND2 
2294 N N   . SER A 289 ? 0.1979 0.2930 0.2453 -0.0386 -0.0177 0.0237  290 SER A N   
2295 C CA  . SER A 289 ? 0.2247 0.3319 0.2845 -0.0438 -0.0204 0.0245  290 SER A CA  
2296 C C   . SER A 289 ? 0.2080 0.3255 0.2780 -0.0444 -0.0144 0.0280  290 SER A C   
2297 O O   . SER A 289 ? 0.1826 0.2999 0.2501 -0.0390 -0.0092 0.0293  290 SER A O   
2298 C CB  . SER A 289 ? 0.2191 0.3366 0.2836 -0.0410 -0.0260 0.0238  290 SER A CB  
2299 O OG  . SER A 289 ? 0.2084 0.3338 0.2770 -0.0339 -0.0230 0.0257  290 SER A OG  
2300 N N   . GLU A 290 ? 0.2155 0.3426 0.2970 -0.0514 -0.0152 0.0295  291 GLU A N   
2301 C CA  . GLU A 290 ? 0.1959 0.3355 0.2878 -0.0522 -0.0089 0.0333  291 GLU A CA  
2302 C C   . GLU A 290 ? 0.2242 0.3768 0.3217 -0.0439 -0.0069 0.0336  291 GLU A C   
2303 O O   . GLU A 290 ? 0.1633 0.3194 0.2609 -0.0398 -0.0004 0.0352  291 GLU A O   
2304 C CB  . GLU A 290 ? 0.2578 0.4082 0.3632 -0.0616 -0.0106 0.0352  291 GLU A CB  
2305 C CG  . GLU A 290 ? 0.3084 0.4715 0.4237 -0.0639 -0.0030 0.0400  291 GLU A CG  
2306 C CD  . GLU A 290 ? 0.4093 0.5866 0.5409 -0.0736 -0.0047 0.0423  291 GLU A CD  
2307 O OE1 . GLU A 290 ? 0.4887 0.6692 0.6250 -0.0798 0.0009  0.0468  291 GLU A OE1 
2308 O OE2 . GLU A 290 ? 0.4492 0.6351 0.5890 -0.0753 -0.0117 0.0400  291 GLU A OE2 
2309 N N   . GLN A 291 ? 0.1755 0.3344 0.2768 -0.0408 -0.0128 0.0317  292 GLN A N   
2310 C CA  . GLN A 291 ? 0.1763 0.3459 0.2829 -0.0322 -0.0118 0.0318  292 GLN A CA  
2311 C C   . GLN A 291 ? 0.1753 0.3335 0.2702 -0.0248 -0.0077 0.0312  292 GLN A C   
2312 O O   . GLN A 291 ? 0.1770 0.3416 0.2751 -0.0192 -0.0028 0.0316  292 GLN A O   
2313 C CB  . GLN A 291 ? 0.1938 0.3685 0.3036 -0.0297 -0.0199 0.0304  292 GLN A CB  
2314 C CG  . GLN A 291 ? 0.1981 0.3811 0.3125 -0.0197 -0.0199 0.0306  292 GLN A CG  
2315 C CD  . GLN A 291 ? 0.2320 0.4350 0.3627 -0.0178 -0.0157 0.0320  292 GLN A CD  
2316 O OE1 . GLN A 291 ? 0.2860 0.5029 0.4296 -0.0243 -0.0166 0.0332  292 GLN A OE1 
2317 N NE2 . GLN A 291 ? 0.2097 0.4148 0.3406 -0.0089 -0.0110 0.0317  292 GLN A NE2 
2318 N N   . ILE A 292 ? 0.1524 0.2942 0.2338 -0.0247 -0.0097 0.0297  293 ILE A N   
2319 C CA  . ILE A 292 ? 0.1367 0.2684 0.2082 -0.0186 -0.0065 0.0292  293 ILE A CA  
2320 C C   . ILE A 292 ? 0.2024 0.3306 0.2707 -0.0197 0.0000  0.0301  293 ILE A C   
2321 O O   . ILE A 292 ? 0.1740 0.3016 0.2398 -0.0143 0.0038  0.0298  293 ILE A O   
2322 C CB  . ILE A 292 ? 0.1668 0.2845 0.2263 -0.0183 -0.0102 0.0278  293 ILE A CB  
2323 C CG1 . ILE A 292 ? 0.2117 0.3327 0.2724 -0.0159 -0.0166 0.0275  293 ILE A CG1 
2324 C CG2 . ILE A 292 ? 0.1716 0.2791 0.2219 -0.0138 -0.0068 0.0275  293 ILE A CG2 
2325 C CD1 . ILE A 292 ? 0.2340 0.3606 0.2990 -0.0082 -0.0166 0.0283  293 ILE A CD1 
2326 N N   . VAL A 293 ? 0.1604 0.2854 0.2280 -0.0265 0.0011  0.0313  294 VAL A N   
2327 C CA  . VAL A 293 ? 0.1863 0.3049 0.2480 -0.0273 0.0065  0.0328  294 VAL A CA  
2328 C C   . VAL A 293 ? 0.1603 0.2914 0.2295 -0.0274 0.0122  0.0352  294 VAL A C   
2329 O O   . VAL A 293 ? 0.1836 0.3125 0.2472 -0.0243 0.0169  0.0359  294 VAL A O   
2330 C CB  . VAL A 293 ? 0.1789 0.2862 0.2352 -0.0337 0.0052  0.0334  294 VAL A CB  
2331 C CG1 . VAL A 293 ? 0.2934 0.3950 0.3443 -0.0345 0.0104  0.0359  294 VAL A CG1 
2332 C CG2 . VAL A 293 ? 0.2093 0.3044 0.2565 -0.0321 0.0010  0.0305  294 VAL A CG2 
2333 N N   . MET A 294 ? 0.1436 0.2889 0.2254 -0.0310 0.0119  0.0367  295 MET A N   
2334 C CA  . MET A 294 ? 0.1542 0.3129 0.2437 -0.0325 0.0183  0.0398  295 MET A CA  
2335 C C   . MET A 294 ? 0.1556 0.3310 0.2547 -0.0259 0.0206  0.0388  295 MET A C   
2336 O O   . MET A 294 ? 0.1840 0.3701 0.2868 -0.0248 0.0273  0.0407  295 MET A O   
2337 C CB  . MET A 294 ? 0.2252 0.3897 0.3240 -0.0427 0.0175  0.0430  295 MET A CB  
2338 C CG  . MET A 294 ? 0.2538 0.4008 0.3435 -0.0492 0.0155  0.0439  295 MET A CG  
2339 S SD  . MET A 294 ? 0.3947 0.5304 0.4714 -0.0477 0.0221  0.0470  295 MET A SD  
2340 C CE  . MET A 294 ? 0.3044 0.4578 0.3913 -0.0519 0.0299  0.0527  295 MET A CE  
2341 N N   . LYS A 295 ? 0.1307 0.3090 0.2337 -0.0211 0.0155  0.0361  296 LYS A N   
2342 C CA  . LYS A 295 ? 0.1362 0.3309 0.2501 -0.0144 0.0168  0.0352  296 LYS A CA  
2343 C C   . LYS A 295 ? 0.1253 0.3120 0.2315 -0.0043 0.0160  0.0318  296 LYS A C   
2344 O O   . LYS A 295 ? 0.1418 0.3120 0.2364 -0.0036 0.0127  0.0305  296 LYS A O   
2345 C CB  . LYS A 295 ? 0.1465 0.3531 0.2737 -0.0169 0.0105  0.0353  296 LYS A CB  
2346 C CG  . LYS A 295 ? 0.2337 0.4461 0.3687 -0.0282 0.0094  0.0381  296 LYS A CG  
2347 C CD  . LYS A 295 ? 0.3404 0.5767 0.4952 -0.0295 0.0089  0.0395  296 LYS A CD  
2348 C CE  . LYS A 295 ? 0.3258 0.5686 0.4896 -0.0421 0.0087  0.0427  296 LYS A CE  
2349 N NZ  . LYS A 295 ? 0.3919 0.6604 0.5772 -0.0439 0.0077  0.0441  296 LYS A NZ  
2350 N N   . PRO A 296 ? 0.1263 0.3242 0.2388 0.0037  0.0191  0.0303  297 PRO A N   
2351 C CA  . PRO A 296 ? 0.1354 0.3244 0.2417 0.0131  0.0170  0.0269  297 PRO A CA  
2352 C C   . PRO A 296 ? 0.1718 0.3592 0.2818 0.0149  0.0089  0.0268  297 PRO A C   
2353 O O   . PRO A 296 ? 0.1819 0.3829 0.3041 0.0129  0.0058  0.0282  297 PRO A O   
2354 C CB  . PRO A 296 ? 0.1465 0.3490 0.2595 0.0212  0.0228  0.0251  297 PRO A CB  
2355 C CG  . PRO A 296 ? 0.2077 0.4315 0.3359 0.0168  0.0257  0.0280  297 PRO A CG  
2356 C CD  . PRO A 296 ? 0.1665 0.3849 0.2913 0.0048  0.0254  0.0315  297 PRO A CD  
2357 N N   . ASN A 297 ? 0.1466 0.3172 0.2455 0.0180  0.0052  0.0255  298 ASN A N   
2358 C CA  . ASN A 297 ? 0.1514 0.3185 0.2510 0.0204  -0.0023 0.0260  298 ASN A CA  
2359 C C   . ASN A 297 ? 0.1351 0.2922 0.2294 0.0295  -0.0033 0.0241  298 ASN A C   
2360 O O   . ASN A 297 ? 0.1364 0.2808 0.2206 0.0305  -0.0006 0.0225  298 ASN A O   
2361 C CB  . ASN A 297 ? 0.1291 0.2843 0.2197 0.0134  -0.0066 0.0273  298 ASN A CB  
2362 C CG  . ASN A 297 ? 0.1492 0.3127 0.2455 0.0047  -0.0075 0.0286  298 ASN A CG  
2363 O OD1 . ASN A 297 ? 0.1536 0.3271 0.2585 0.0032  -0.0125 0.0294  298 ASN A OD1 
2364 N ND2 . ASN A 297 ? 0.1640 0.3233 0.2559 -0.0011 -0.0030 0.0289  298 ASN A ND2 
2365 N N   . LYS A 298 ? 0.1391 0.3016 0.2405 0.0360  -0.0077 0.0244  299 LYS A N   
2366 C CA  . LYS A 298 ? 0.1463 0.2978 0.2432 0.0449  -0.0094 0.0230  299 LYS A CA  
2367 C C   . LYS A 298 ? 0.1484 0.2799 0.2316 0.0419  -0.0128 0.0243  299 LYS A C   
2368 O O   . LYS A 298 ? 0.1872 0.3162 0.2673 0.0367  -0.0172 0.0271  299 LYS A O   
2369 C CB  . LYS A 298 ? 0.1794 0.3404 0.2868 0.0525  -0.0144 0.0239  299 LYS A CB  
2370 C CG  . LYS A 298 ? 0.2168 0.3651 0.3201 0.0624  -0.0167 0.0227  299 LYS A CG  
2371 C CD  . LYS A 298 ? 0.2749 0.4257 0.3805 0.0698  -0.0105 0.0180  299 LYS A CD  
2372 C CE  . LYS A 298 ? 0.3447 0.4925 0.4544 0.0823  -0.0137 0.0165  299 LYS A CE  
2373 N NZ  . LYS A 298 ? 0.4115 0.5353 0.5093 0.0837  -0.0188 0.0177  299 LYS A NZ  
2374 N N   . VAL A 299 ? 0.1529 0.2704 0.2278 0.0451  -0.0109 0.0222  300 VAL A N   
2375 C CA  . VAL A 299 ? 0.1558 0.2555 0.2192 0.0421  -0.0137 0.0238  300 VAL A CA  
2376 C C   . VAL A 299 ? 0.1659 0.2570 0.2285 0.0485  -0.0192 0.0257  300 VAL A C   
2377 O O   . VAL A 299 ? 0.1808 0.2759 0.2502 0.0570  -0.0202 0.0243  300 VAL A O   
2378 C CB  . VAL A 299 ? 0.1561 0.2449 0.2113 0.0407  -0.0096 0.0209  300 VAL A CB  
2379 C CG1 . VAL A 299 ? 0.1484 0.2466 0.2048 0.0362  -0.0040 0.0194  300 VAL A CG1 
2380 C CG2 . VAL A 299 ? 0.1735 0.2551 0.2281 0.0490  -0.0092 0.0174  300 VAL A CG2 
2381 N N   . THR A 300 ? 0.1688 0.2483 0.2231 0.0447  -0.0228 0.0293  301 THR A N   
2382 C CA  . THR A 300 ? 0.1953 0.2630 0.2463 0.0496  -0.0279 0.0323  301 THR A CA  
2383 C C   . THR A 300 ? 0.2551 0.3048 0.2955 0.0459  -0.0272 0.0331  301 THR A C   
2384 O O   . THR A 300 ? 0.2149 0.2630 0.2500 0.0385  -0.0246 0.0335  301 THR A O   
2385 C CB  . THR A 300 ? 0.2525 0.3242 0.3033 0.0488  -0.0338 0.0372  301 THR A CB  
2386 O OG1 . THR A 300 ? 0.3134 0.3853 0.3575 0.0400  -0.0331 0.0389  301 THR A OG1 
2387 C CG2 . THR A 300 ? 0.2091 0.2992 0.2723 0.0529  -0.0356 0.0363  301 THR A CG2 
2388 N N   . ALA A 301 ? 0.3379 0.3742 0.3762 0.0512  -0.0295 0.0334  302 ALA A N   
2389 C CA  . ALA A 301 ? 0.3760 0.3954 0.4060 0.0471  -0.0292 0.0343  302 ALA A CA  
2390 C C   . ALA A 301 ? 0.3807 0.3949 0.4036 0.0408  -0.0314 0.0408  302 ALA A C   
2391 O O   . ALA A 301 ? 0.3873 0.4054 0.4100 0.0423  -0.0351 0.0451  302 ALA A O   
2392 C CB  . ALA A 301 ? 0.4633 0.4679 0.4928 0.0541  -0.0318 0.0330  302 ALA A CB  
2393 N N   . ILE A 302 ? 0.4081 0.4146 0.4250 0.0339  -0.0290 0.0416  303 ILE A N   
2394 C CA  . ILE A 302 ? 0.4919 0.4945 0.5017 0.0278  -0.0298 0.0476  303 ILE A CA  
2395 C C   . ILE A 302 ? 0.6110 0.5980 0.6164 0.0295  -0.0338 0.0531  303 ILE A C   
2396 O O   . ILE A 302 ? 0.6004 0.5747 0.6057 0.0301  -0.0341 0.0520  303 ILE A O   
2397 C CB  . ILE A 302 ? 0.4831 0.4855 0.4898 0.0201  -0.0254 0.0464  303 ILE A CB  
2398 C CG1 . ILE A 302 ? 0.3547 0.3708 0.3648 0.0186  -0.0218 0.0418  303 ILE A CG1 
2399 C CG2 . ILE A 302 ? 0.5851 0.5842 0.5845 0.0144  -0.0253 0.0526  303 ILE A CG2 
2400 C CD1 . ILE A 302 ? 0.3467 0.3627 0.3549 0.0127  -0.0179 0.0400  303 ILE A CD1 
2401 N N   . SER A 303 ? 0.7734 0.7606 0.7745 0.0301  -0.0372 0.0593  304 SER A N   
2402 C CA  . SER A 303 ? 0.9368 0.9085 0.9318 0.0307  -0.0408 0.0664  304 SER A CA  
2403 C C   . SER A 303 ? 0.9195 0.8827 0.9088 0.0220  -0.0376 0.0697  304 SER A C   
2404 O O   . SER A 303 ? 0.8938 0.8439 0.8838 0.0206  -0.0376 0.0694  304 SER A O   
2405 C CB  . SER A 303 ? 0.8841 0.8595 0.8743 0.0332  -0.0453 0.0726  304 SER A CB  
2406 O OG  . SER A 303 ? 0.8915 0.8794 0.8779 0.0280  -0.0430 0.0726  304 SER A OG  
2407 N N   . LYS A 304 ? 0.8073 0.7779 0.7910 0.0161  -0.0349 0.0727  305 LYS A N   
2408 C CA  . LYS A 304 ? 0.7999 0.7682 0.7804 0.0078  -0.0304 0.0746  305 LYS A CA  
2409 C C   . LYS A 304 ? 0.7347 0.7181 0.7155 0.0046  -0.0260 0.0705  305 LYS A C   
2410 O O   . LYS A 304 ? 0.7368 0.7295 0.7156 0.0068  -0.0271 0.0699  305 LYS A O   
2411 C CB  . LYS A 304 ? 0.8578 0.8177 0.8292 0.0039  -0.0309 0.0844  305 LYS A CB  
2412 C CG  . LYS A 304 ? 0.8375 0.8045 0.8007 0.0056  -0.0326 0.0887  305 LYS A CG  
2413 C CD  . LYS A 304 ? 0.9094 0.8702 0.8622 0.0005  -0.0313 0.0983  305 LYS A CD  
2414 C CE  . LYS A 304 ? 0.9754 0.9449 0.9180 0.0016  -0.0322 0.1013  305 LYS A CE  
2415 N NZ  . LYS A 304 ? 0.9933 0.9626 0.9350 0.0093  -0.0394 0.1021  305 LYS A NZ  
2416 N N   . GLU A 305 ? 0.6540 0.6393 0.6377 -0.0003 -0.0217 0.0674  306 GLU A N   
2417 C CA  . GLU A 305 ? 0.5505 0.5482 0.5345 -0.0027 -0.0177 0.0635  306 GLU A CA  
2418 C C   . GLU A 305 ? 0.5279 0.5301 0.5034 -0.0054 -0.0162 0.0683  306 GLU A C   
2419 O O   . GLU A 305 ? 0.5182 0.5137 0.4877 -0.0076 -0.0165 0.0752  306 GLU A O   
2420 C CB  . GLU A 305 ? 0.5784 0.5768 0.5670 -0.0071 -0.0140 0.0603  306 GLU A CB  
2421 C CG  . GLU A 305 ? 0.4875 0.4940 0.4815 -0.0052 -0.0126 0.0528  306 GLU A CG  
2422 C CD  . GLU A 305 ? 0.4676 0.4759 0.4651 -0.0093 -0.0096 0.0501  306 GLU A CD  
2423 O OE1 . GLU A 305 ? 0.5630 0.5636 0.5626 -0.0119 -0.0105 0.0510  306 GLU A OE1 
2424 O OE2 . GLU A 305 ? 0.3658 0.3829 0.3640 -0.0101 -0.0068 0.0472  306 GLU A OE2 
2425 N N   . PRO A 306 ? 0.4564 0.4688 0.4302 -0.0052 -0.0146 0.0647  307 PRO A N   
2426 C CA  . PRO A 306 ? 0.4345 0.4506 0.3985 -0.0070 -0.0134 0.0681  307 PRO A CA  
2427 C C   . PRO A 306 ? 0.3580 0.3727 0.3187 -0.0122 -0.0084 0.0723  307 PRO A C   
2428 O O   . PRO A 306 ? 0.3928 0.4084 0.3601 -0.0150 -0.0052 0.0702  307 PRO A O   
2429 C CB  . PRO A 306 ? 0.3907 0.4164 0.3553 -0.0063 -0.0121 0.0618  307 PRO A CB  
2430 C CG  . PRO A 306 ? 0.4287 0.4561 0.4029 -0.0036 -0.0141 0.0567  307 PRO A CG  
2431 C CD  . PRO A 306 ? 0.4633 0.4835 0.4431 -0.0037 -0.0137 0.0576  307 PRO A CD  
2432 N N   . SER A 307 ? 0.3576 0.3710 0.3082 -0.0134 -0.0079 0.0786  308 SER A N   
2433 C CA  . SER A 307 ? 0.3412 0.3551 0.2885 -0.0186 -0.0024 0.0837  308 SER A CA  
2434 C C   . SER A 307 ? 0.3857 0.4101 0.3348 -0.0203 0.0033  0.0787  308 SER A C   
2435 O O   . SER A 307 ? 0.3884 0.4153 0.3431 -0.0243 0.0077  0.0796  308 SER A O   
2436 C CB  . SER A 307 ? 0.4274 0.4388 0.3615 -0.0190 -0.0028 0.0916  308 SER A CB  
2437 O OG  . SER A 307 ? 0.5569 0.5730 0.4862 -0.0236 0.0040  0.0957  308 SER A OG  
2438 N N   . VAL A 308 ? 0.3069 0.3374 0.2517 -0.0172 0.0031  0.0734  309 VAL A N   
2439 C CA  . VAL A 308 ? 0.2525 0.2915 0.1981 -0.0175 0.0080  0.0682  309 VAL A CA  
2440 C C   . VAL A 308 ? 0.2485 0.2890 0.1997 -0.0146 0.0050  0.0606  309 VAL A C   
2441 O O   . VAL A 308 ? 0.2239 0.2629 0.1724 -0.0120 0.0002  0.0591  309 VAL A O   
2442 C CB  . VAL A 308 ? 0.2726 0.3163 0.2051 -0.0169 0.0110  0.0692  309 VAL A CB  
2443 C CG1 . VAL A 308 ? 0.3043 0.3559 0.2385 -0.0168 0.0169  0.0643  309 VAL A CG1 
2444 C CG2 . VAL A 308 ? 0.3388 0.3803 0.2631 -0.0196 0.0132  0.0783  309 VAL A CG2 
2445 N N   . LYS A 309 ? 0.2193 0.2633 0.1786 -0.0151 0.0078  0.0562  310 LYS A N   
2446 C CA  . LYS A 309 ? 0.2091 0.2535 0.1749 -0.0130 0.0053  0.0503  310 LYS A CA  
2447 C C   . LYS A 309 ? 0.2223 0.2715 0.1881 -0.0122 0.0084  0.0452  310 LYS A C   
2448 O O   . LYS A 309 ? 0.2248 0.2780 0.1892 -0.0129 0.0130  0.0456  310 LYS A O   
2449 C CB  . LYS A 309 ? 0.2784 0.3199 0.2541 -0.0138 0.0044  0.0501  310 LYS A CB  
2450 C CG  . LYS A 309 ? 0.3286 0.3630 0.3047 -0.0141 0.0011  0.0548  310 LYS A CG  
2451 C CD  . LYS A 309 ? 0.4127 0.4434 0.3965 -0.0163 0.0014  0.0552  310 LYS A CD  
2452 C CE  . LYS A 309 ? 0.4714 0.4981 0.4538 -0.0204 0.0028  0.0616  310 LYS A CE  
2453 N NZ  . LYS A 309 ? 0.4859 0.5063 0.4757 -0.0226 0.0011  0.0614  310 LYS A NZ  
2454 N N   . MET A 310 ? 0.2127 0.2616 0.1805 -0.0105 0.0059  0.0405  311 MET A N   
2455 C CA  . MET A 310 ? 0.1866 0.2375 0.1564 -0.0096 0.0079  0.0357  311 MET A CA  
2456 C C   . MET A 310 ? 0.1993 0.2492 0.1766 -0.0092 0.0055  0.0332  311 MET A C   
2457 O O   . MET A 310 ? 0.1963 0.2449 0.1765 -0.0091 0.0024  0.0343  311 MET A O   
2458 C CB  . MET A 310 ? 0.2177 0.2685 0.1789 -0.0083 0.0077  0.0323  311 MET A CB  
2459 C CG  . MET A 310 ? 0.2156 0.2643 0.1751 -0.0084 0.0024  0.0305  311 MET A CG  
2460 S SD  . MET A 310 ? 0.3076 0.3544 0.2561 -0.0076 0.0010  0.0256  311 MET A SD  
2461 C CE  . MET A 310 ? 0.3085 0.3531 0.2616 -0.0069 0.0034  0.0206  311 MET A CE  
2462 N N   . TYR A 311 ? 0.1624 0.2130 0.1426 -0.0085 0.0073  0.0301  312 TYR A N   
2463 C CA  . TYR A 311 ? 0.1672 0.2173 0.1538 -0.0084 0.0061  0.0286  312 TYR A CA  
2464 C C   . TYR A 311 ? 0.1816 0.2303 0.1673 -0.0077 0.0064  0.0252  312 TYR A C   
2465 O O   . TYR A 311 ? 0.1796 0.2277 0.1618 -0.0066 0.0084  0.0236  312 TYR A O   
2466 C CB  . TYR A 311 ? 0.1863 0.2378 0.1785 -0.0085 0.0078  0.0295  312 TYR A CB  
2467 C CG  . TYR A 311 ? 0.1722 0.2231 0.1658 -0.0099 0.0073  0.0328  312 TYR A CG  
2468 C CD1 . TYR A 311 ? 0.1754 0.2279 0.1667 -0.0112 0.0095  0.0355  312 TYR A CD1 
2469 C CD2 . TYR A 311 ? 0.1754 0.2238 0.1724 -0.0097 0.0049  0.0332  312 TYR A CD2 
2470 C CE1 . TYR A 311 ? 0.1913 0.2418 0.1839 -0.0134 0.0089  0.0394  312 TYR A CE1 
2471 C CE2 . TYR A 311 ? 0.1714 0.2167 0.1693 -0.0110 0.0039  0.0361  312 TYR A CE2 
2472 C CZ  . TYR A 311 ? 0.2133 0.2592 0.2091 -0.0132 0.0058  0.0395  312 TYR A CZ  
2473 O OH  . TYR A 311 ? 0.2474 0.2889 0.2442 -0.0153 0.0047  0.0432  312 TYR A OH  
2474 N N   . HIS A 312 ? 0.1791 0.2271 0.1683 -0.0083 0.0047  0.0244  313 HIS A N   
2475 C CA  . HIS A 312 ? 0.1615 0.2067 0.1504 -0.0083 0.0051  0.0221  313 HIS A CA  
2476 C C   . HIS A 312 ? 0.1599 0.2059 0.1540 -0.0090 0.0047  0.0228  313 HIS A C   
2477 O O   . HIS A 312 ? 0.1736 0.2227 0.1713 -0.0090 0.0042  0.0241  313 HIS A O   
2478 C CB  . HIS A 312 ? 0.1818 0.2239 0.1657 -0.0095 0.0031  0.0197  313 HIS A CB  
2479 C CG  . HIS A 312 ? 0.1707 0.2140 0.1572 -0.0120 -0.0002 0.0197  313 HIS A CG  
2480 N ND1 . HIS A 312 ? 0.1845 0.2254 0.1673 -0.0139 -0.0031 0.0173  313 HIS A ND1 
2481 C CD2 . HIS A 312 ? 0.1898 0.2374 0.1829 -0.0130 -0.0011 0.0214  313 HIS A CD2 
2482 C CE1 . HIS A 312 ? 0.1741 0.2188 0.1622 -0.0164 -0.0059 0.0180  313 HIS A CE1 
2483 N NE2 . HIS A 312 ? 0.1931 0.2423 0.1877 -0.0155 -0.0043 0.0206  313 HIS A NE2 
2484 N N   . LYS A 313 ? 0.1587 0.2014 0.1524 -0.0092 0.0053  0.0219  314 LYS A N   
2485 C CA  . LYS A 313 ? 0.1532 0.1965 0.1503 -0.0103 0.0055  0.0231  314 LYS A CA  
2486 C C   . LYS A 313 ? 0.1613 0.1987 0.1566 -0.0118 0.0053  0.0226  314 LYS A C   
2487 O O   . LYS A 313 ? 0.1853 0.2176 0.1773 -0.0099 0.0059  0.0215  314 LYS A O   
2488 C CB  . LYS A 313 ? 0.1581 0.2032 0.1567 -0.0083 0.0070  0.0243  314 LYS A CB  
2489 C CG  . LYS A 313 ? 0.1503 0.1967 0.1506 -0.0090 0.0077  0.0257  314 LYS A CG  
2490 C CD  . LYS A 313 ? 0.1658 0.2178 0.1699 -0.0096 0.0075  0.0260  314 LYS A CD  
2491 C CE  . LYS A 313 ? 0.2044 0.2596 0.2097 -0.0096 0.0094  0.0274  314 LYS A CE  
2492 N NZ  . LYS A 313 ? 0.2540 0.3104 0.2617 -0.0131 0.0100  0.0288  314 LYS A NZ  
2493 N N   . THR A 314 ? 0.1887 0.2267 0.1868 -0.0152 0.0044  0.0234  315 THR A N   
2494 C CA  . THR A 314 ? 0.1837 0.2153 0.1809 -0.0178 0.0043  0.0240  315 THR A CA  
2495 C C   . THR A 314 ? 0.2208 0.2536 0.2196 -0.0176 0.0066  0.0274  315 THR A C   
2496 O O   . THR A 314 ? 0.2444 0.2843 0.2456 -0.0164 0.0080  0.0286  315 THR A O   
2497 C CB  . THR A 314 ? 0.2434 0.2758 0.2438 -0.0229 0.0020  0.0237  315 THR A CB  
2498 O OG1 . THR A 314 ? 0.2506 0.2932 0.2576 -0.0242 0.0028  0.0257  315 THR A OG1 
2499 C CG2 . THR A 314 ? 0.2727 0.3038 0.2702 -0.0232 -0.0010 0.0202  315 THR A CG2 
2500 N N   . GLY A 315 ? 0.2086 0.2335 0.2049 -0.0187 0.0068  0.0288  316 GLY A N   
2501 C CA  . GLY A 315 ? 0.2123 0.2383 0.2089 -0.0194 0.0089  0.0329  316 GLY A CA  
2502 C C   . GLY A 315 ? 0.2426 0.2580 0.2363 -0.0216 0.0086  0.0353  316 GLY A C   
2503 O O   . GLY A 315 ? 0.2683 0.2741 0.2587 -0.0202 0.0068  0.0332  316 GLY A O   
2504 N N   . SER A 316 ? 0.2352 0.2518 0.2299 -0.0249 0.0106  0.0399  317 SER A N   
2505 C CA  . SER A 316 ? 0.2680 0.2733 0.2596 -0.0277 0.0104  0.0435  317 SER A CA  
2506 C C   . SER A 316 ? 0.2829 0.2907 0.2719 -0.0276 0.0134  0.0493  317 SER A C   
2507 O O   . SER A 316 ? 0.2452 0.2643 0.2354 -0.0262 0.0158  0.0499  317 SER A O   
2508 C CB  . SER A 316 ? 0.2952 0.2975 0.2913 -0.0354 0.0091  0.0439  317 SER A CB  
2509 O OG  . SER A 316 ? 0.3117 0.3128 0.3091 -0.0355 0.0059  0.0382  317 SER A OG  
2510 N N   . THR A 317 ? 0.2965 0.2929 0.2810 -0.0289 0.0132  0.0537  318 THR A N   
2511 C CA  . THR A 317 ? 0.2815 0.2785 0.2637 -0.0321 0.0162  0.0608  318 THR A CA  
2512 C C   . THR A 317 ? 0.3411 0.3301 0.3265 -0.0403 0.0159  0.0639  318 THR A C   
2513 O O   . THR A 317 ? 0.4005 0.3847 0.3897 -0.0431 0.0129  0.0597  318 THR A O   
2514 C CB  . THR A 317 ? 0.3305 0.3201 0.3039 -0.0267 0.0158  0.0645  318 THR A CB  
2515 O OG1 . THR A 317 ? 0.3682 0.3410 0.3385 -0.0260 0.0126  0.0650  318 THR A OG1 
2516 C CG2 . THR A 317 ? 0.2840 0.2808 0.2555 -0.0191 0.0148  0.0603  318 THR A CG2 
2517 N N   . ASN A 318 ? 0.3991 0.3862 0.3824 -0.0447 0.0188  0.0715  319 ASN A N   
2518 C CA  . ASN A 318 ? 0.4154 0.3934 0.4023 -0.0536 0.0181  0.0749  319 ASN A CA  
2519 C C   . ASN A 318 ? 0.4384 0.3954 0.4207 -0.0525 0.0132  0.0731  319 ASN A C   
2520 O O   . ASN A 318 ? 0.4594 0.4067 0.4451 -0.0597 0.0110  0.0733  319 ASN A O   
2521 C CB  . ASN A 318 ? 0.4867 0.4662 0.4717 -0.0590 0.0227  0.0845  319 ASN A CB  
2522 C CG  . ASN A 318 ? 0.5736 0.5745 0.5649 -0.0614 0.0280  0.0858  319 ASN A CG  
2523 O OD1 . ASN A 318 ? 0.6034 0.6160 0.6043 -0.0633 0.0277  0.0809  319 ASN A OD1 
2524 N ND2 . ASN A 318 ? 0.6135 0.6200 0.5989 -0.0605 0.0330  0.0923  319 ASN A ND2 
2525 N N   . ARG A 319 ? 0.4076 0.3579 0.3831 -0.0434 0.0112  0.0706  320 ARG A N   
2526 C CA  . ARG A 319 ? 0.4312 0.3614 0.4016 -0.0406 0.0072  0.0694  320 ARG A CA  
2527 C C   . ARG A 319 ? 0.3378 0.2672 0.3065 -0.0314 0.0046  0.0616  320 ARG A C   
2528 O O   . ARG A 319 ? 0.3814 0.2952 0.3456 -0.0270 0.0016  0.0601  320 ARG A O   
2529 C CB  . ARG A 319 ? 0.4755 0.3950 0.4381 -0.0387 0.0078  0.0778  320 ARG A CB  
2530 C CG  . ARG A 319 ? 0.5658 0.4991 0.5248 -0.0334 0.0107  0.0807  320 ARG A CG  
2531 C CD  . ARG A 319 ? 0.7176 0.6474 0.6702 -0.0364 0.0134  0.0912  320 ARG A CD  
2532 N NE  . ARG A 319 ? 0.7566 0.6936 0.7022 -0.0286 0.0139  0.0930  320 ARG A NE  
2533 C CZ  . ARG A 319 ? 0.7495 0.6778 0.6892 -0.0202 0.0101  0.0929  320 ARG A CZ  
2534 N NH1 . ARG A 319 ? 0.7435 0.6546 0.6827 -0.0178 0.0062  0.0915  320 ARG A NH1 
2535 N NH2 . ARG A 319 ? 0.7943 0.7316 0.7287 -0.0137 0.0099  0.0937  320 ARG A NH2 
2536 N N   . PHE A 320 ? 0.3313 0.2766 0.3035 -0.0283 0.0057  0.0568  321 PHE A N   
2537 C CA  . PHE A 320 ? 0.2677 0.2144 0.2393 -0.0209 0.0040  0.0499  321 PHE A CA  
2538 C C   . PHE A 320 ? 0.2935 0.2519 0.2706 -0.0233 0.0042  0.0442  321 PHE A C   
2539 O O   . PHE A 320 ? 0.2994 0.2690 0.2811 -0.0282 0.0060  0.0459  321 PHE A O   
2540 C CB  . PHE A 320 ? 0.2734 0.2281 0.2428 -0.0131 0.0048  0.0509  321 PHE A CB  
2541 C CG  . PHE A 320 ? 0.2917 0.2350 0.2553 -0.0078 0.0032  0.0548  321 PHE A CG  
2542 C CD1 . PHE A 320 ? 0.3153 0.2556 0.2745 -0.0095 0.0042  0.0627  321 PHE A CD1 
2543 C CD2 . PHE A 320 ? 0.3088 0.2453 0.2711 -0.0003 0.0009  0.0509  321 PHE A CD2 
2544 C CE1 . PHE A 320 ? 0.3513 0.2807 0.3045 -0.0040 0.0021  0.0669  321 PHE A CE1 
2545 C CE2 . PHE A 320 ? 0.3152 0.2415 0.2728 0.0057  -0.0010 0.0546  321 PHE A CE2 
2546 C CZ  . PHE A 320 ? 0.3457 0.2681 0.2986 0.0038  -0.0008 0.0629  321 PHE A CZ  
2547 N N   . GLY A 321 ? 0.2725 0.2287 0.2487 -0.0192 0.0024  0.0378  322 GLY A N   
2548 C CA  . GLY A 321 ? 0.2736 0.2406 0.2534 -0.0202 0.0023  0.0329  322 GLY A CA  
2549 C C   . GLY A 321 ? 0.2453 0.2181 0.2238 -0.0128 0.0029  0.0291  322 GLY A C   
2550 O O   . GLY A 321 ? 0.2765 0.2427 0.2517 -0.0068 0.0025  0.0280  322 GLY A O   
2551 N N   . THR A 322 ? 0.2254 0.2112 0.2073 -0.0132 0.0039  0.0274  323 THR A N   
2552 C CA  . THR A 322 ? 0.1891 0.1820 0.1709 -0.0076 0.0048  0.0247  323 THR A CA  
2553 C C   . THR A 322 ? 0.2123 0.2125 0.1956 -0.0096 0.0045  0.0216  323 THR A C   
2554 O O   . THR A 322 ? 0.2266 0.2314 0.2131 -0.0144 0.0039  0.0226  323 THR A O   
2555 C CB  . THR A 322 ? 0.2085 0.2103 0.1925 -0.0049 0.0063  0.0279  323 THR A CB  
2556 O OG1 . THR A 322 ? 0.2599 0.2554 0.2415 -0.0033 0.0061  0.0316  323 THR A OG1 
2557 C CG2 . THR A 322 ? 0.2291 0.2374 0.2140 0.0000  0.0070  0.0254  323 THR A CG2 
2558 N N   . TYR A 323 ? 0.1887 0.1908 0.1699 -0.0056 0.0049  0.0182  324 TYR A N   
2559 C CA  . TYR A 323 ? 0.1957 0.2054 0.1774 -0.0067 0.0049  0.0164  324 TYR A CA  
2560 C C   . TYR A 323 ? 0.1923 0.2077 0.1736 -0.0019 0.0070  0.0155  324 TYR A C   
2561 O O   . TYR A 323 ? 0.2162 0.2279 0.1952 0.0024  0.0080  0.0137  324 TYR A O   
2562 C CB  . TYR A 323 ? 0.1994 0.2037 0.1770 -0.0092 0.0026  0.0127  324 TYR A CB  
2563 C CG  . TYR A 323 ? 0.1887 0.2004 0.1654 -0.0101 0.0019  0.0115  324 TYR A CG  
2564 C CD1 . TYR A 323 ? 0.2615 0.2811 0.2432 -0.0133 0.0010  0.0140  324 TYR A CD1 
2565 C CD2 . TYR A 323 ? 0.1976 0.2083 0.1679 -0.0074 0.0022  0.0079  324 TYR A CD2 
2566 C CE1 . TYR A 323 ? 0.2030 0.2283 0.1835 -0.0136 -0.0002 0.0136  324 TYR A CE1 
2567 C CE2 . TYR A 323 ? 0.2154 0.2322 0.1835 -0.0082 0.0014  0.0077  324 TYR A CE2 
2568 C CZ  . TYR A 323 ? 0.1895 0.2131 0.1628 -0.0113 -0.0001 0.0107  324 TYR A CZ  
2569 O OH  . TYR A 323 ? 0.1937 0.2221 0.1641 -0.0116 -0.0014 0.0110  324 TYR A OH  
2570 N N   . VAL A 324 ? 0.1795 0.2037 0.1635 -0.0028 0.0077  0.0168  325 VAL A N   
2571 C CA  A VAL A 324 ? 0.1928 0.2233 0.1774 0.0002  0.0098  0.0167  325 VAL A CA  
2572 C CA  B VAL A 324 ? 0.1923 0.2230 0.1772 0.0001  0.0098  0.0168  325 VAL A CA  
2573 C C   . VAL A 324 ? 0.1903 0.2255 0.1739 -0.0019 0.0096  0.0169  325 VAL A C   
2574 O O   . VAL A 324 ? 0.2031 0.2398 0.1884 -0.0049 0.0079  0.0183  325 VAL A O   
2575 C CB  A VAL A 324 ? 0.1859 0.2218 0.1758 0.0016  0.0106  0.0192  325 VAL A CB  
2576 C CB  B VAL A 324 ? 0.1875 0.2236 0.1777 0.0010  0.0103  0.0195  325 VAL A CB  
2577 C CG1 A VAL A 324 ? 0.2071 0.2389 0.1972 0.0048  0.0105  0.0194  325 VAL A CG1 
2578 C CG1 B VAL A 324 ? 0.1816 0.2246 0.1741 0.0027  0.0122  0.0197  325 VAL A CG1 
2579 C CG2 A VAL A 324 ? 0.1835 0.2221 0.1762 -0.0015 0.0094  0.0214  325 VAL A CG2 
2580 C CG2 B VAL A 324 ? 0.2069 0.2386 0.1974 0.0033  0.0099  0.0202  325 VAL A CG2 
2581 N N   . VAL A 325 ? 0.1811 0.2189 0.1615 0.0000  0.0116  0.0158  326 VAL A N   
2582 C CA  . VAL A 325 ? 0.1773 0.2186 0.1549 -0.0017 0.0115  0.0167  326 VAL A CA  
2583 C C   . VAL A 325 ? 0.1934 0.2407 0.1706 0.0003  0.0152  0.0177  326 VAL A C   
2584 O O   . VAL A 325 ? 0.2058 0.2539 0.1826 0.0038  0.0178  0.0158  326 VAL A O   
2585 C CB  . VAL A 325 ? 0.1710 0.2073 0.1411 -0.0027 0.0092  0.0138  326 VAL A CB  
2586 C CG1 . VAL A 325 ? 0.2006 0.2317 0.1647 0.0007  0.0106  0.0094  326 VAL A CG1 
2587 C CG2 . VAL A 325 ? 0.1971 0.2370 0.1629 -0.0040 0.0085  0.0154  326 VAL A CG2 
2588 N N   . PHE A 326 ? 0.1867 0.2384 0.1648 -0.0018 0.0156  0.0210  327 PHE A N   
2589 C CA  . PHE A 326 ? 0.1744 0.2325 0.1524 -0.0011 0.0195  0.0227  327 PHE A CA  
2590 C C   . PHE A 326 ? 0.2113 0.2706 0.1851 -0.0037 0.0192  0.0262  327 PHE A C   
2591 O O   . PHE A 326 ? 0.2018 0.2579 0.1758 -0.0058 0.0157  0.0278  327 PHE A O   
2592 C CB  . PHE A 326 ? 0.1847 0.2487 0.1722 -0.0011 0.0210  0.0246  327 PHE A CB  
2593 C CG  . PHE A 326 ? 0.1683 0.2324 0.1612 -0.0046 0.0186  0.0277  327 PHE A CG  
2594 C CD1 . PHE A 326 ? 0.1759 0.2361 0.1717 -0.0048 0.0154  0.0268  327 PHE A CD1 
2595 C CD2 . PHE A 326 ? 0.1727 0.2406 0.1680 -0.0074 0.0198  0.0314  327 PHE A CD2 
2596 C CE1 . PHE A 326 ? 0.1878 0.2477 0.1878 -0.0071 0.0133  0.0286  327 PHE A CE1 
2597 C CE2 . PHE A 326 ? 0.1842 0.2501 0.1841 -0.0103 0.0171  0.0336  327 PHE A CE2 
2598 C CZ  . PHE A 326 ? 0.1664 0.2283 0.1684 -0.0097 0.0139  0.0316  327 PHE A CZ  
2599 N N   . ILE A 327 ? 0.1912 0.2553 0.1610 -0.0031 0.0233  0.0275  328 ILE A N   
2600 C CA  . ILE A 327 ? 0.2065 0.2714 0.1699 -0.0052 0.0238  0.0315  328 ILE A CA  
2601 C C   . ILE A 327 ? 0.2079 0.2804 0.1758 -0.0071 0.0284  0.0361  328 ILE A C   
2602 O O   . ILE A 327 ? 0.2376 0.3166 0.2035 -0.0051 0.0336  0.0355  328 ILE A O   
2603 C CB  . ILE A 327 ? 0.2218 0.2849 0.1725 -0.0030 0.0243  0.0288  328 ILE A CB  
2604 C CG1 . ILE A 327 ? 0.2177 0.2736 0.1652 -0.0020 0.0194  0.0238  328 ILE A CG1 
2605 C CG2 . ILE A 327 ? 0.2686 0.3322 0.2116 -0.0052 0.0242  0.0339  328 ILE A CG2 
2606 C CD1 . ILE A 327 ? 0.2698 0.3228 0.2045 0.0005  0.0194  0.0191  328 ILE A CD1 
2607 N N   . PRO A 328 ? 0.2312 0.3032 0.2056 -0.0108 0.0269  0.0405  329 PRO A N   
2608 C CA  . PRO A 328 ? 0.2402 0.3194 0.2210 -0.0139 0.0308  0.0450  329 PRO A CA  
2609 C C   . PRO A 328 ? 0.2728 0.3576 0.2462 -0.0145 0.0362  0.0486  329 PRO A C   
2610 O O   . PRO A 328 ? 0.2834 0.3782 0.2616 -0.0147 0.0416  0.0497  329 PRO A O   
2611 C CB  . PRO A 328 ? 0.2780 0.3514 0.2634 -0.0180 0.0268  0.0487  329 PRO A CB  
2612 C CG  . PRO A 328 ? 0.2544 0.3214 0.2411 -0.0158 0.0218  0.0444  329 PRO A CG  
2613 C CD  . PRO A 328 ? 0.1992 0.2646 0.1775 -0.0121 0.0215  0.0405  329 PRO A CD  
2614 N N   . LYS A 329 ? 0.2844 0.3640 0.2461 -0.0146 0.0349  0.0506  330 LYS A N   
2615 C CA  . LYS A 329 ? 0.3177 0.4022 0.2706 -0.0155 0.0400  0.0551  330 LYS A CA  
2616 C C   . LYS A 329 ? 0.3251 0.4174 0.2731 -0.0110 0.0457  0.0506  330 LYS A C   
2617 O O   . LYS A 329 ? 0.3148 0.4160 0.2603 -0.0116 0.0523  0.0541  330 LYS A O   
2618 C CB  . LYS A 329 ? 0.3242 0.4010 0.2641 -0.0156 0.0362  0.0578  330 LYS A CB  
2619 C CG  . LYS A 329 ? 0.3491 0.4302 0.2780 -0.0168 0.0414  0.0636  330 LYS A CG  
2620 C CD  . LYS A 329 ? 0.3718 0.4454 0.2875 -0.0168 0.0371  0.0672  330 LYS A CD  
2621 C CE  . LYS A 329 ? 0.4268 0.5056 0.3300 -0.0179 0.0431  0.0733  330 LYS A CE  
2622 N NZ  . LYS A 329 ? 0.4758 0.5472 0.3667 -0.0189 0.0389  0.0797  330 LYS A NZ  
2623 N N   . GLU A 330 ? 0.2901 0.3791 0.2367 -0.0063 0.0434  0.0431  331 GLU A N   
2624 C CA  . GLU A 330 ? 0.3295 0.4232 0.2707 -0.0009 0.0480  0.0376  331 GLU A CA  
2625 C C   . GLU A 330 ? 0.2853 0.3861 0.2395 0.0016  0.0508  0.0348  331 GLU A C   
2626 O O   . GLU A 330 ? 0.3075 0.4120 0.2589 0.0072  0.0546  0.0298  331 GLU A O   
2627 C CB  . GLU A 330 ? 0.3531 0.4370 0.2838 0.0027  0.0433  0.0308  331 GLU A CB  
2628 C CG  . GLU A 330 ? 0.4308 0.5072 0.3518 0.0001  0.0379  0.0331  331 GLU A CG  
2629 C CD  . GLU A 330 ? 0.4713 0.5492 0.3759 0.0016  0.0405  0.0337  331 GLU A CD  
2630 O OE1 . GLU A 330 ? 0.5870 0.6736 0.4887 0.0030  0.0480  0.0353  331 GLU A OE1 
2631 O OE2 . GLU A 330 ? 0.5218 0.5929 0.4161 0.0015  0.0350  0.0325  331 GLU A OE2 
2632 N N   . ASN A 331 ? 0.2311 0.3334 0.1987 -0.0020 0.0486  0.0377  332 ASN A N   
2633 C CA  . ASN A 331 ? 0.2370 0.3468 0.2178 -0.0001 0.0500  0.0358  332 ASN A CA  
2634 C C   . ASN A 331 ? 0.2690 0.3739 0.2474 0.0066  0.0486  0.0284  332 ASN A C   
2635 O O   . ASN A 331 ? 0.2784 0.3907 0.2607 0.0116  0.0525  0.0255  332 ASN A O   
2636 C CB  . ASN A 331 ? 0.3443 0.4695 0.3310 -0.0003 0.0576  0.0389  332 ASN A CB  
2637 C CG  . ASN A 331 ? 0.3287 0.4579 0.3191 -0.0080 0.0589  0.0470  332 ASN A CG  
2638 O OD1 . ASN A 331 ? 0.4720 0.6050 0.4546 -0.0096 0.0637  0.0511  332 ASN A OD1 
2639 N ND2 . ASN A 331 ? 0.4349 0.5628 0.4368 -0.0128 0.0547  0.0495  332 ASN A ND2 
2640 N N   . ILE A 332 ? 0.2339 0.3264 0.2064 0.0065  0.0429  0.0256  333 ILE A N   
2641 C CA  . ILE A 332 ? 0.2533 0.3383 0.2216 0.0117  0.0409  0.0191  333 ILE A CA  
2642 C C   . ILE A 332 ? 0.2521 0.3275 0.2236 0.0096  0.0344  0.0184  333 ILE A C   
2643 O O   . ILE A 332 ? 0.2209 0.2932 0.1930 0.0050  0.0311  0.0216  333 ILE A O   
2644 C CB  . ILE A 332 ? 0.2561 0.3359 0.2094 0.0143  0.0418  0.0152  333 ILE A CB  
2645 C CG1 . ILE A 332 ? 0.2761 0.3487 0.2258 0.0204  0.0411  0.0080  333 ILE A CG1 
2646 C CG2 . ILE A 332 ? 0.2473 0.3189 0.1929 0.0099  0.0366  0.0166  333 ILE A CG2 
2647 C CD1 . ILE A 332 ? 0.3083 0.3777 0.2433 0.0244  0.0433  0.0028  333 ILE A CD1 
2648 N N   . GLY A 333 ? 0.2246 0.2951 0.1979 0.0134  0.0329  0.0144  334 GLY A N   
2649 C CA  . GLY A 333 ? 0.1948 0.2565 0.1700 0.0115  0.0276  0.0139  334 GLY A CA  
2650 C C   . GLY A 333 ? 0.2114 0.2649 0.1839 0.0160  0.0265  0.0092  334 GLY A C   
2651 O O   . GLY A 333 ? 0.2284 0.2837 0.1994 0.0215  0.0297  0.0062  334 GLY A O   
2652 N N   . LEU A 334 ? 0.2159 0.2604 0.1881 0.0138  0.0221  0.0088  335 LEU A N   
2653 C CA  . LEU A 334 ? 0.2205 0.2545 0.1895 0.0168  0.0203  0.0049  335 LEU A CA  
2654 C C   . LEU A 334 ? 0.2131 0.2423 0.1872 0.0143  0.0169  0.0074  335 LEU A C   
2655 O O   . LEU A 334 ? 0.2042 0.2355 0.1810 0.0096  0.0151  0.0104  335 LEU A O   
2656 C CB  . LEU A 334 ? 0.2459 0.2712 0.2047 0.0157  0.0184  0.0008  335 LEU A CB  
2657 C CG  . LEU A 334 ? 0.2646 0.2761 0.2189 0.0177  0.0159  -0.0037 335 LEU A CG  
2658 C CD1 . LEU A 334 ? 0.2689 0.2745 0.2119 0.0194  0.0157  -0.0097 335 LEU A CD1 
2659 C CD2 . LEU A 334 ? 0.2526 0.2573 0.2096 0.0118  0.0113  -0.0016 335 LEU A CD2 
2660 N N   . VAL A 335 ? 0.1906 0.2130 0.1653 0.0180  0.0162  0.0062  336 VAL A N   
2661 C CA  A VAL A 335 ? 0.2211 0.2380 0.1989 0.0163  0.0135  0.0089  336 VAL A CA  
2662 C CA  B VAL A 335 ? 0.2178 0.2347 0.1955 0.0161  0.0134  0.0089  336 VAL A CA  
2663 C C   . VAL A 335 ? 0.2238 0.2262 0.1963 0.0175  0.0114  0.0062  336 VAL A C   
2664 O O   . VAL A 335 ? 0.2304 0.2280 0.1997 0.0232  0.0125  0.0025  336 VAL A O   
2665 C CB  A VAL A 335 ? 0.2361 0.2591 0.2206 0.0200  0.0141  0.0116  336 VAL A CB  
2666 C CB  B VAL A 335 ? 0.2334 0.2569 0.2180 0.0190  0.0139  0.0120  336 VAL A CB  
2667 C CG1 A VAL A 335 ? 0.1959 0.2134 0.1816 0.0179  0.0113  0.0151  336 VAL A CG1 
2668 C CG1 B VAL A 335 ? 0.2319 0.2660 0.2217 0.0152  0.0142  0.0151  336 VAL A CG1 
2669 C CG2 A VAL A 335 ? 0.2358 0.2727 0.2262 0.0189  0.0160  0.0136  336 VAL A CG2 
2670 C CG2 B VAL A 335 ? 0.1936 0.2216 0.1801 0.0259  0.0165  0.0099  336 VAL A CG2 
2671 N N   . MET A 336 ? 0.2147 0.2102 0.1867 0.0122  0.0087  0.0080  337 MET A N   
2672 C CA  . MET A 336 ? 0.2278 0.2082 0.1959 0.0118  0.0062  0.0067  337 MET A CA  
2673 C C   . MET A 336 ? 0.2477 0.2256 0.2193 0.0098  0.0051  0.0122  337 MET A C   
2674 O O   . MET A 336 ? 0.2322 0.2171 0.2073 0.0051  0.0052  0.0157  337 MET A O   
2675 C CB  . MET A 336 ? 0.2516 0.2257 0.2155 0.0060  0.0037  0.0038  337 MET A CB  
2676 C CG  . MET A 336 ? 0.2555 0.2122 0.2154 0.0047  0.0007  0.0019  337 MET A CG  
2677 S SD  . MET A 336 ? 0.3229 0.2750 0.2842 -0.0059 -0.0031 0.0033  337 MET A SD  
2678 C CE  . MET A 336 ? 0.2586 0.2198 0.2281 -0.0094 -0.0014 0.0119  337 MET A CE  
2679 N N   . LEU A 337 ? 0.2359 0.2034 0.2058 0.0138  0.0043  0.0129  338 LEU A N   
2680 C CA  . LEU A 337 ? 0.2422 0.2045 0.2130 0.0121  0.0031  0.0186  338 LEU A CA  
2681 C C   . LEU A 337 ? 0.2771 0.2208 0.2433 0.0107  0.0006  0.0182  338 LEU A C   
2682 O O   . LEU A 337 ? 0.2907 0.2244 0.2531 0.0159  -0.0001 0.0139  338 LEU A O   
2683 C CB  . LEU A 337 ? 0.2390 0.2061 0.2122 0.0189  0.0035  0.0213  338 LEU A CB  
2684 C CG  . LEU A 337 ? 0.2297 0.2140 0.2080 0.0209  0.0055  0.0206  338 LEU A CG  
2685 C CD1 . LEU A 337 ? 0.2699 0.2585 0.2512 0.0278  0.0050  0.0225  338 LEU A CD1 
2686 C CD2 . LEU A 337 ? 0.2406 0.2338 0.2213 0.0146  0.0059  0.0234  338 LEU A CD2 
2687 N N   . THR A 338 ? 0.2789 0.2176 0.2453 0.0036  -0.0004 0.0228  339 THR A N   
2688 C CA  . THR A 338 ? 0.2726 0.1926 0.2353 0.0007  -0.0029 0.0238  339 THR A CA  
2689 C C   . THR A 338 ? 0.2976 0.2146 0.2606 -0.0025 -0.0027 0.0321  339 THR A C   
2690 O O   . THR A 338 ? 0.2871 0.2173 0.2534 -0.0054 -0.0007 0.0361  339 THR A O   
2691 C CB  . THR A 338 ? 0.3299 0.2450 0.2924 -0.0074 -0.0049 0.0205  339 THR A CB  
2692 O OG1 . THR A 338 ? 0.3273 0.2557 0.2953 -0.0147 -0.0037 0.0240  339 THR A OG1 
2693 C CG2 . THR A 338 ? 0.3140 0.2303 0.2735 -0.0042 -0.0054 0.0122  339 THR A CG2 
2694 N N   . ASN A 339 ? 0.2962 0.1951 0.2551 -0.0018 -0.0048 0.0349  340 ASN A N   
2695 C CA  . ASN A 339 ? 0.3202 0.2147 0.2780 -0.0055 -0.0045 0.0438  340 ASN A CA  
2696 C C   . ASN A 339 ? 0.3450 0.2301 0.3035 -0.0164 -0.0053 0.0466  340 ASN A C   
2697 O O   . ASN A 339 ? 0.3681 0.2406 0.3237 -0.0196 -0.0060 0.0533  340 ASN A O   
2698 C CB  . ASN A 339 ? 0.3428 0.2245 0.2957 0.0024  -0.0062 0.0474  340 ASN A CB  
2699 C CG  . ASN A 339 ? 0.3232 0.1835 0.2720 0.0057  -0.0093 0.0433  340 ASN A CG  
2700 O OD1 . ASN A 339 ? 0.3513 0.2057 0.3001 0.0019  -0.0105 0.0371  340 ASN A OD1 
2701 N ND2 . ASN A 339 ? 0.3666 0.2143 0.3114 0.0132  -0.0113 0.0466  340 ASN A ND2 
2702 N N   . LYS A 340 ? 0.3198 0.2118 0.2825 -0.0224 -0.0055 0.0418  341 LYS A N   
2703 C CA  . LYS A 340 ? 0.3310 0.2221 0.2977 -0.0338 -0.0059 0.0443  341 LYS A CA  
2704 C C   . LYS A 340 ? 0.3424 0.2513 0.3149 -0.0366 -0.0052 0.0395  341 LYS A C   
2705 O O   . LYS A 340 ? 0.3531 0.2658 0.3241 -0.0311 -0.0060 0.0325  341 LYS A O   
2706 C CB  . LYS A 340 ? 0.3717 0.2405 0.3355 -0.0381 -0.0101 0.0420  341 LYS A CB  
2707 C CG  . LYS A 340 ? 0.3972 0.2647 0.3665 -0.0512 -0.0109 0.0461  341 LYS A CG  
2708 C CD  . LYS A 340 ? 0.4672 0.3116 0.4337 -0.0561 -0.0160 0.0428  341 LYS A CD  
2709 C CE  . LYS A 340 ? 0.5671 0.4128 0.5412 -0.0704 -0.0169 0.0469  341 LYS A CE  
2710 N NZ  . LYS A 340 ? 0.6260 0.4481 0.5978 -0.0765 -0.0227 0.0433  341 LYS A NZ  
2711 N N   . ARG A 341 ? 0.3538 0.2744 0.3329 -0.0447 -0.0035 0.0434  342 ARG A N   
2712 C CA  . ARG A 341 ? 0.3459 0.2827 0.3308 -0.0470 -0.0035 0.0392  342 ARG A CA  
2713 C C   . ARG A 341 ? 0.3798 0.3088 0.3644 -0.0503 -0.0082 0.0322  342 ARG A C   
2714 O O   . ARG A 341 ? 0.4174 0.3314 0.4012 -0.0562 -0.0113 0.0323  342 ARG A O   
2715 C CB  . ARG A 341 ? 0.4016 0.3528 0.3947 -0.0544 -0.0008 0.0447  342 ARG A CB  
2716 C CG  . ARG A 341 ? 0.4194 0.3833 0.4125 -0.0502 0.0040  0.0494  342 ARG A CG  
2717 C CD  . ARG A 341 ? 0.4967 0.4797 0.4984 -0.0548 0.0070  0.0517  342 ARG A CD  
2718 N NE  . ARG A 341 ? 0.5460 0.5316 0.5559 -0.0643 0.0054  0.0521  342 ARG A NE  
2719 C CZ  . ARG A 341 ? 0.6009 0.5797 0.6132 -0.0725 0.0057  0.0575  342 ARG A CZ  
2720 N NH1 . ARG A 341 ? 0.6480 0.6135 0.6534 -0.0720 0.0072  0.0631  342 ARG A NH1 
2721 N NH2 . ARG A 341 ? 0.6053 0.5908 0.6274 -0.0816 0.0044  0.0579  342 ARG A NH2 
2722 N N   . ILE A 342 ? 0.3312 0.2696 0.3158 -0.0469 -0.0091 0.0262  343 ILE A N   
2723 C CA  . ILE A 342 ? 0.3413 0.2772 0.3260 -0.0512 -0.0137 0.0199  343 ILE A CA  
2724 C C   . ILE A 342 ? 0.2831 0.2390 0.2743 -0.0528 -0.0133 0.0194  343 ILE A C   
2725 O O   . ILE A 342 ? 0.3089 0.2776 0.3021 -0.0483 -0.0095 0.0220  343 ILE A O   
2726 C CB  . ILE A 342 ? 0.4123 0.3363 0.3874 -0.0443 -0.0160 0.0121  343 ILE A CB  
2727 C CG1 . ILE A 342 ? 0.3781 0.3134 0.3506 -0.0352 -0.0127 0.0104  343 ILE A CG1 
2728 C CG2 . ILE A 342 ? 0.4129 0.3160 0.3820 -0.0418 -0.0168 0.0124  343 ILE A CG2 
2729 C CD1 . ILE A 342 ? 0.3777 0.3067 0.3417 -0.0295 -0.0145 0.0023  343 ILE A CD1 
2730 N N   . PRO A 343 ? 0.2912 0.2496 0.2859 -0.0591 -0.0177 0.0161  344 PRO A N   
2731 C CA  . PRO A 343 ? 0.3219 0.2993 0.3235 -0.0603 -0.0180 0.0161  344 PRO A CA  
2732 C C   . PRO A 343 ? 0.2809 0.2657 0.2775 -0.0514 -0.0161 0.0137  344 PRO A C   
2733 O O   . PRO A 343 ? 0.2915 0.2678 0.2790 -0.0459 -0.0167 0.0091  344 PRO A O   
2734 C CB  . PRO A 343 ? 0.3070 0.2818 0.3099 -0.0669 -0.0247 0.0112  344 PRO A CB  
2735 C CG  . PRO A 343 ? 0.2749 0.2322 0.2768 -0.0732 -0.0269 0.0116  344 PRO A CG  
2736 C CD  . PRO A 343 ? 0.3129 0.2566 0.3058 -0.0657 -0.0233 0.0124  344 PRO A CD  
2737 N N   . ASN A 344 ? 0.2736 0.2744 0.2765 -0.0500 -0.0135 0.0170  345 ASN A N   
2738 C CA  . ASN A 344 ? 0.2774 0.2847 0.2765 -0.0428 -0.0118 0.0155  345 ASN A CA  
2739 C C   . ASN A 344 ? 0.2768 0.2833 0.2703 -0.0417 -0.0160 0.0100  345 ASN A C   
2740 O O   . ASN A 344 ? 0.2395 0.2441 0.2256 -0.0357 -0.0147 0.0077  345 ASN A O   
2741 C CB  . ASN A 344 ? 0.2689 0.2918 0.2758 -0.0418 -0.0090 0.0195  345 ASN A CB  
2742 C CG  . ASN A 344 ? 0.3523 0.3757 0.3607 -0.0403 -0.0042 0.0241  345 ASN A CG  
2743 O OD1 . ASN A 344 ? 0.3621 0.3767 0.3644 -0.0366 -0.0025 0.0242  345 ASN A OD1 
2744 N ND2 . ASN A 344 ? 0.3876 0.4218 0.4040 -0.0429 -0.0020 0.0280  345 ASN A ND2 
2745 N N   . GLU A 345 ? 0.2933 0.3014 0.2899 -0.0477 -0.0211 0.0079  346 GLU A N   
2746 C CA  . GLU A 345 ? 0.2718 0.2790 0.2613 -0.0466 -0.0258 0.0026  346 GLU A CA  
2747 C C   . GLU A 345 ? 0.2878 0.2796 0.2650 -0.0432 -0.0262 -0.0028 346 GLU A C   
2748 O O   . GLU A 345 ? 0.2700 0.2615 0.2381 -0.0385 -0.0267 -0.0064 346 GLU A O   
2749 C CB  . GLU A 345 ? 0.3663 0.3779 0.3618 -0.0541 -0.0323 0.0010  346 GLU A CB  
2750 C CG  . GLU A 345 ? 0.4120 0.4389 0.4223 -0.0583 -0.0315 0.0064  346 GLU A CG  
2751 C CD  . GLU A 345 ? 0.4512 0.4741 0.4688 -0.0646 -0.0293 0.0100  346 GLU A CD  
2752 O OE1 . GLU A 345 ? 0.4449 0.4683 0.4641 -0.0619 -0.0232 0.0144  346 GLU A OE1 
2753 O OE2 . GLU A 345 ? 0.5752 0.5941 0.5967 -0.0725 -0.0340 0.0084  346 GLU A OE2 
2754 N N   . GLU A 346 ? 0.2747 0.2534 0.2509 -0.0451 -0.0258 -0.0033 347 GLU A N   
2755 C CA  . GLU A 346 ? 0.2950 0.2582 0.2598 -0.0406 -0.0258 -0.0087 347 GLU A CA  
2756 C C   . GLU A 346 ? 0.2739 0.2397 0.2343 -0.0316 -0.0201 -0.0078 347 GLU A C   
2757 O O   . GLU A 346 ? 0.2809 0.2419 0.2315 -0.0261 -0.0196 -0.0128 347 GLU A O   
2758 C CB  . GLU A 346 ? 0.3214 0.2690 0.2871 -0.0443 -0.0268 -0.0084 347 GLU A CB  
2759 C CG  . GLU A 346 ? 0.3441 0.2869 0.3140 -0.0542 -0.0330 -0.0099 347 GLU A CG  
2760 C CD  . GLU A 346 ? 0.4186 0.3474 0.3777 -0.0545 -0.0388 -0.0190 347 GLU A CD  
2761 O OE1 . GLU A 346 ? 0.4045 0.3340 0.3535 -0.0475 -0.0383 -0.0240 347 GLU A OE1 
2762 O OE2 . GLU A 346 ? 0.4298 0.3467 0.3901 -0.0620 -0.0438 -0.0211 347 GLU A OE2 
2763 N N   . ARG A 347 ? 0.2309 0.2046 0.1982 -0.0300 -0.0157 -0.0017 348 ARG A N   
2764 C CA  . ARG A 347 ? 0.2177 0.1952 0.1825 -0.0225 -0.0109 -0.0007 348 ARG A CA  
2765 C C   . ARG A 347 ? 0.2426 0.2303 0.2043 -0.0198 -0.0104 -0.0019 348 ARG A C   
2766 O O   . ARG A 347 ? 0.2437 0.2306 0.1986 -0.0142 -0.0081 -0.0045 348 ARG A O   
2767 C CB  . ARG A 347 ? 0.2502 0.2343 0.2226 -0.0221 -0.0073 0.0057  348 ARG A CB  
2768 C CG  . ARG A 347 ? 0.2416 0.2174 0.2172 -0.0256 -0.0075 0.0088  348 ARG A CG  
2769 C CD  . ARG A 347 ? 0.2478 0.2329 0.2299 -0.0257 -0.0042 0.0150  348 ARG A CD  
2770 N NE  . ARG A 347 ? 0.2936 0.2748 0.2798 -0.0315 -0.0045 0.0191  348 ARG A NE  
2771 C CZ  . ARG A 347 ? 0.3088 0.2956 0.2988 -0.0319 -0.0015 0.0246  348 ARG A CZ  
2772 N NH1 . ARG A 347 ? 0.3075 0.3037 0.2982 -0.0271 0.0012  0.0260  348 ARG A NH1 
2773 N NH2 . ARG A 347 ? 0.3158 0.2980 0.3083 -0.0373 -0.0013 0.0289  348 ARG A NH2 
2774 N N   . ILE A 348 ? 0.2390 0.2365 0.2057 -0.0237 -0.0125 0.0003  349 ILE A N   
2775 C CA  . ILE A 348 ? 0.2196 0.2260 0.1832 -0.0214 -0.0125 0.0004  349 ILE A CA  
2776 C C   . ILE A 348 ? 0.2505 0.2517 0.2029 -0.0203 -0.0153 -0.0053 349 ILE A C   
2777 O O   . ILE A 348 ? 0.2668 0.2708 0.2123 -0.0158 -0.0130 -0.0060 349 ILE A O   
2778 C CB  . ILE A 348 ? 0.2279 0.2450 0.1999 -0.0252 -0.0149 0.0039  349 ILE A CB  
2779 C CG1 . ILE A 348 ? 0.2120 0.2349 0.1929 -0.0247 -0.0111 0.0090  349 ILE A CG1 
2780 C CG2 . ILE A 348 ? 0.2197 0.2436 0.1873 -0.0232 -0.0165 0.0040  349 ILE A CG2 
2781 C CD1 . ILE A 348 ? 0.2082 0.2407 0.1986 -0.0282 -0.0128 0.0119  349 ILE A CD1 
2782 N N   . LYS A 349 ? 0.2381 0.2317 0.1881 -0.0245 -0.0205 -0.0095 350 LYS A N   
2783 C CA  . LYS A 349 ? 0.2413 0.2290 0.1789 -0.0233 -0.0238 -0.0160 350 LYS A CA  
2784 C C   . LYS A 349 ? 0.3010 0.2800 0.2290 -0.0167 -0.0195 -0.0200 350 LYS A C   
2785 O O   . LYS A 349 ? 0.2923 0.2725 0.2097 -0.0125 -0.0184 -0.0232 350 LYS A O   
2786 C CB  . LYS A 349 ? 0.2795 0.2594 0.2172 -0.0299 -0.0308 -0.0202 350 LYS A CB  
2787 C CG  . LYS A 349 ? 0.3188 0.3096 0.2641 -0.0358 -0.0362 -0.0178 350 LYS A CG  
2788 C CD  . LYS A 349 ? 0.3788 0.3631 0.3290 -0.0440 -0.0425 -0.0206 350 LYS A CD  
2789 C CE  . LYS A 349 ? 0.4307 0.4287 0.3918 -0.0499 -0.0475 -0.0176 350 LYS A CE  
2790 N NZ  . LYS A 349 ? 0.5700 0.5643 0.5396 -0.0591 -0.0528 -0.0189 350 LYS A NZ  
2791 N N   . ALA A 350 ? 0.2613 0.2319 0.1927 -0.0154 -0.0172 -0.0199 351 ALA A N   
2792 C CA  . ALA A 350 ? 0.2927 0.2555 0.2163 -0.0081 -0.0134 -0.0240 351 ALA A CA  
2793 C C   . ALA A 350 ? 0.2669 0.2414 0.1902 -0.0022 -0.0072 -0.0211 351 ALA A C   
2794 O O   . ALA A 350 ? 0.2869 0.2611 0.2010 0.0034  -0.0043 -0.0251 351 ALA A O   
2795 C CB  . ALA A 350 ? 0.2810 0.2327 0.2093 -0.0075 -0.0126 -0.0233 351 ALA A CB  
2796 N N   . ALA A 351 ? 0.2639 0.2490 0.1972 -0.0036 -0.0049 -0.0142 352 ALA A N   
2797 C CA  . ALA A 351 ? 0.2636 0.2594 0.1979 0.0007  0.0005  -0.0110 352 ALA A CA  
2798 C C   . ALA A 351 ? 0.2759 0.2788 0.2030 0.0005  0.0002  -0.0110 352 ALA A C   
2799 O O   . ALA A 351 ? 0.2717 0.2802 0.1945 0.0046  0.0048  -0.0107 352 ALA A O   
2800 C CB  . ALA A 351 ? 0.2615 0.2649 0.2075 -0.0011 0.0020  -0.0043 352 ALA A CB  
2801 N N   . TYR A 352 ? 0.2332 0.2367 0.1594 -0.0044 -0.0050 -0.0108 353 TYR A N   
2802 C CA  . TYR A 352 ? 0.2311 0.2399 0.1488 -0.0044 -0.0063 -0.0107 353 TYR A CA  
2803 C C   . TYR A 352 ? 0.2592 0.2623 0.1622 -0.0003 -0.0055 -0.0173 353 TYR A C   
2804 O O   . TYR A 352 ? 0.2798 0.2886 0.1749 0.0030  -0.0018 -0.0164 353 TYR A O   
2805 C CB  . TYR A 352 ? 0.2582 0.2684 0.1785 -0.0099 -0.0133 -0.0099 353 TYR A CB  
2806 C CG  . TYR A 352 ? 0.2634 0.2790 0.1750 -0.0098 -0.0159 -0.0090 353 TYR A CG  
2807 C CD1 . TYR A 352 ? 0.2972 0.3079 0.1953 -0.0094 -0.0197 -0.0148 353 TYR A CD1 
2808 C CD2 . TYR A 352 ? 0.2561 0.2806 0.1722 -0.0098 -0.0149 -0.0023 353 TYR A CD2 
2809 C CE1 . TYR A 352 ? 0.2980 0.3136 0.1867 -0.0090 -0.0225 -0.0135 353 TYR A CE1 
2810 C CE2 . TYR A 352 ? 0.2715 0.2999 0.1789 -0.0095 -0.0177 -0.0005 353 TYR A CE2 
2811 C CZ  . TYR A 352 ? 0.2688 0.2933 0.1623 -0.0090 -0.0214 -0.0058 353 TYR A CZ  
2812 O OH  . TYR A 352 ? 0.2596 0.2879 0.1430 -0.0084 -0.0245 -0.0036 353 TYR A OH  
2813 N N   . ALA A 353 ? 0.2767 0.2682 0.1757 -0.0005 -0.0085 -0.0239 354 ALA A N   
2814 C CA  . ALA A 353 ? 0.3063 0.2907 0.1903 0.0041  -0.0080 -0.0315 354 ALA A CA  
2815 C C   . ALA A 353 ? 0.2843 0.2725 0.1662 0.0115  0.0004  -0.0316 354 ALA A C   
2816 O O   . ALA A 353 ? 0.3135 0.3053 0.1837 0.0158  0.0037  -0.0340 354 ALA A O   
2817 C CB  . ALA A 353 ? 0.3154 0.2842 0.1969 0.0025  -0.0130 -0.0387 354 ALA A CB  
2818 N N   . VAL A 354 ? 0.3056 0.2941 0.1987 0.0133  0.0038  -0.0288 355 VAL A N   
2819 C CA  . VAL A 354 ? 0.2993 0.2927 0.1928 0.0205  0.0112  -0.0290 355 VAL A CA  
2820 C C   . VAL A 354 ? 0.2887 0.2973 0.1832 0.0208  0.0163  -0.0231 355 VAL A C   
2821 O O   . VAL A 354 ? 0.2943 0.3083 0.1808 0.0257  0.0217  -0.0249 355 VAL A O   
2822 C CB  . VAL A 354 ? 0.3257 0.3165 0.2316 0.0220  0.0125  -0.0268 355 VAL A CB  
2823 C CG1 . VAL A 354 ? 0.3097 0.3103 0.2198 0.0287  0.0198  -0.0251 355 VAL A CG1 
2824 C CG2 . VAL A 354 ? 0.2812 0.2549 0.1838 0.0229  0.0084  -0.0329 355 VAL A CG2 
2825 N N   . LEU A 355 ? 0.2720 0.2875 0.1760 0.0156  0.0150  -0.0158 356 LEU A N   
2826 C CA  . LEU A 355 ? 0.2825 0.3105 0.1882 0.0152  0.0195  -0.0096 356 LEU A CA  
2827 C C   . LEU A 355 ? 0.3026 0.3331 0.1947 0.0148  0.0192  -0.0098 356 LEU A C   
2828 O O   . LEU A 355 ? 0.3322 0.3720 0.2221 0.0158  0.0245  -0.0056 356 LEU A O   
2829 C CB  . LEU A 355 ? 0.2525 0.2850 0.1707 0.0102  0.0175  -0.0026 356 LEU A CB  
2830 C CG  . LEU A 355 ? 0.2964 0.3294 0.2277 0.0107  0.0187  -0.0009 356 LEU A CG  
2831 C CD1 . LEU A 355 ? 0.3294 0.3684 0.2707 0.0065  0.0178  0.0058  356 LEU A CD1 
2832 C CD2 . LEU A 355 ? 0.3009 0.3389 0.2345 0.0163  0.0247  -0.0020 356 LEU A CD2 
2833 N N   . ASN A 356 ? 0.2783 0.3010 0.1612 0.0128  0.0129  -0.0140 357 ASN A N   
2834 C CA  . ASN A 356 ? 0.2955 0.3200 0.1633 0.0130  0.0119  -0.0147 357 ASN A CA  
2835 C C   . ASN A 356 ? 0.3455 0.3678 0.1988 0.0192  0.0162  -0.0217 357 ASN A C   
2836 O O   . ASN A 356 ? 0.3946 0.4211 0.2343 0.0207  0.0181  -0.0213 357 ASN A O   
2837 C CB  . ASN A 356 ? 0.2993 0.3178 0.1632 0.0085  0.0026  -0.0168 357 ASN A CB  
2838 C CG  . ASN A 356 ? 0.3192 0.3439 0.1916 0.0038  -0.0007 -0.0088 357 ASN A CG  
2839 O OD1 . ASN A 356 ? 0.3363 0.3655 0.2008 0.0033  -0.0018 -0.0050 357 ASN A OD1 
2840 N ND2 . ASN A 356 ? 0.3038 0.3284 0.1916 0.0009  -0.0023 -0.0061 357 ASN A ND2 
2841 N N   . ALA A 357 ? 0.3443 0.3599 0.1996 0.0234  0.0179  -0.0280 358 ALA A N   
2842 C CA  . ALA A 357 ? 0.3696 0.3816 0.2108 0.0304  0.0217  -0.0360 358 ALA A CA  
2843 C C   . ALA A 357 ? 0.4072 0.4294 0.2523 0.0368  0.0317  -0.0346 358 ALA A C   
2844 O O   . ALA A 357 ? 0.4010 0.4254 0.2332 0.0430  0.0368  -0.0395 358 ALA A O   
2845 C CB  . ALA A 357 ? 0.3801 0.3758 0.2187 0.0320  0.0165  -0.0453 358 ALA A CB  
2846 N N   . ILE A 358 ? 0.3768 0.4063 0.2393 0.0357  0.0347  -0.0284 359 ILE A N   
2847 C CA  . ILE A 358 ? 0.3951 0.4358 0.2639 0.0415  0.0435  -0.0270 359 ILE A CA  
2848 C C   . ILE A 358 ? 0.4692 0.5235 0.3306 0.0417  0.0502  -0.0225 359 ILE A C   
2849 O O   . ILE A 358 ? 0.4284 0.4862 0.2880 0.0355  0.0483  -0.0160 359 ILE A O   
2850 C CB  . ILE A 358 ? 0.4197 0.4657 0.3084 0.0392  0.0438  -0.0209 359 ILE A CB  
2851 C CG1 . ILE A 358 ? 0.4610 0.4945 0.3558 0.0411  0.0393  -0.0254 359 ILE A CG1 
2852 C CG2 . ILE A 358 ? 0.3848 0.4465 0.2820 0.0433  0.0525  -0.0176 359 ILE A CG2 
2853 C CD1 . ILE A 358 ? 0.4914 0.5304 0.4038 0.0403  0.0399  -0.0200 359 ILE A CD1 
2854 N N   . LYS A 359 ? 0.4451 0.5071 0.3020 0.0490  0.0584  -0.0259 360 LYS A N   
2855 C CA  . LYS A 359 ? 0.5075 0.5841 0.3578 0.0493  0.0663  -0.0211 360 LYS A CA  
2856 C C   . LYS A 359 ? 0.5159 0.6072 0.3840 0.0449  0.0707  -0.0109 360 LYS A C   
2857 O O   . LYS A 359 ? 0.4546 0.5491 0.3393 0.0460  0.0712  -0.0102 360 LYS A O   
2858 C CB  . LYS A 359 ? 0.5224 0.6037 0.3624 0.0591  0.0743  -0.0285 360 LYS A CB  
2859 C CG  . LYS A 359 ? 0.5702 0.6369 0.3888 0.0633  0.0702  -0.0390 360 LYS A CG  
2860 C CD  . LYS A 359 ? 0.6201 0.6854 0.4337 0.0747  0.0757  -0.0491 360 LYS A CD  
2861 C CE  . LYS A 359 ? 0.7114 0.7644 0.5003 0.0793  0.0733  -0.0597 360 LYS A CE  
2862 N NZ  . LYS A 359 ? 0.7629 0.7958 0.5466 0.0739  0.0608  -0.0642 360 LYS A NZ  
2863 N N   . LYS A 360 ? 0.5310 0.6306 0.3954 0.0396  0.0734  -0.0028 361 LYS A N   
2864 C CA  . LYS A 360 ? 0.5909 0.7032 0.4711 0.0342  0.0772  0.0072  361 LYS A CA  
2865 C C   . LYS A 360 ? 0.6706 0.7999 0.5591 0.0391  0.0875  0.0076  361 LYS A C   
2866 O O   . LYS A 360 ? 0.6423 0.7775 0.5190 0.0452  0.0943  0.0036  361 LYS A O   
2867 C CB  . LYS A 360 ? 0.6739 0.7884 0.5463 0.0274  0.0771  0.0161  361 LYS A CB  
2868 C CG  . LYS A 360 ? 0.6768 0.7773 0.5343 0.0252  0.0686  0.0144  361 LYS A CG  
2869 C CD  . LYS A 360 ? 0.6728 0.7622 0.5409 0.0214  0.0590  0.0137  361 LYS A CD  
2870 C CE  . LYS A 360 ? 0.7322 0.8163 0.5961 0.0153  0.0526  0.0200  361 LYS A CE  
2871 N NZ  . LYS A 360 ? 0.7282 0.8075 0.5711 0.0167  0.0499  0.0176  361 LYS A NZ  
2872 O OXT . LYS A 360 ? 0.6144 0.7529 0.5215 0.0372  0.0893  0.0116  361 LYS A OXT 
2873 N N   . ASN B 2   ? 1.0170 0.7216 0.9474 -0.0383 -0.1484 -0.1654 3   ASN B N   
2874 C CA  . ASN B 2   ? 0.9551 0.6822 0.8771 -0.0480 -0.1529 -0.1526 3   ASN B CA  
2875 C C   . ASN B 2   ? 0.9158 0.6547 0.8047 -0.0448 -0.1479 -0.1619 3   ASN B C   
2876 O O   . ASN B 2   ? 0.9055 0.6374 0.7793 -0.0336 -0.1391 -0.1770 3   ASN B O   
2877 C CB  . ASN B 2   ? 0.9618 0.7072 0.9027 -0.0460 -0.1456 -0.1333 3   ASN B CB  
2878 C CG  . ASN B 2   ? 1.0316 0.7735 1.0010 -0.0559 -0.1561 -0.1190 3   ASN B CG  
2879 O OD1 . ASN B 2   ? 1.0135 0.7688 0.9856 -0.0671 -0.1642 -0.1059 3   ASN B OD1 
2880 N ND2 . ASN B 2   ? 1.1332 0.8573 1.1239 -0.0514 -0.1558 -0.1213 3   ASN B ND2 
2881 N N   . THR B 3   ? 0.8679 0.6253 0.7459 -0.0544 -0.1534 -0.1526 4   THR B N   
2882 C CA  . THR B 3   ? 0.8573 0.6270 0.7038 -0.0529 -0.1503 -0.1601 4   THR B CA  
2883 C C   . THR B 3   ? 0.8449 0.6265 0.6818 -0.0377 -0.1319 -0.1616 4   THR B C   
2884 O O   . THR B 3   ? 0.8211 0.6070 0.6768 -0.0307 -0.1224 -0.1522 4   THR B O   
2885 C CB  . THR B 3   ? 0.8442 0.6331 0.6846 -0.0657 -0.1585 -0.1466 4   THR B CB  
2886 O OG1 . THR B 3   ? 0.7910 0.5997 0.6429 -0.0634 -0.1499 -0.1290 4   THR B OG1 
2887 C CG2 . THR B 3   ? 0.8563 0.6423 0.7158 -0.0788 -0.1702 -0.1383 4   THR B CG2 
2888 N N   . PRO B 4   ? 0.8456 0.6332 0.6535 -0.0321 -0.1266 -0.1732 5   PRO B N   
2889 C CA  . PRO B 4   ? 0.8165 0.6176 0.6147 -0.0178 -0.1087 -0.1731 5   PRO B CA  
2890 C C   . PRO B 4   ? 0.7591 0.5837 0.5662 -0.0191 -0.1023 -0.1532 5   PRO B C   
2891 O O   . PRO B 4   ? 0.7222 0.5544 0.5365 -0.0080 -0.0879 -0.1485 5   PRO B O   
2892 C CB  . PRO B 4   ? 0.8112 0.6165 0.5751 -0.0148 -0.1075 -0.1875 5   PRO B CB  
2893 C CG  . PRO B 4   ? 0.8836 0.6850 0.6399 -0.0301 -0.1251 -0.1897 5   PRO B CG  
2894 C CD  . PRO B 4   ? 0.8741 0.6563 0.6571 -0.0377 -0.1360 -0.1874 5   PRO B CD  
2895 N N   . LYS B 5   ? 0.7283 0.5645 0.5358 -0.0325 -0.1126 -0.1414 6   LYS B N   
2896 C CA  . LYS B 5   ? 0.7045 0.5617 0.5229 -0.0351 -0.1077 -0.1220 6   LYS B CA  
2897 C C   . LYS B 5   ? 0.6857 0.5381 0.5367 -0.0336 -0.1055 -0.1115 6   LYS B C   
2898 O O   . LYS B 5   ? 0.6158 0.4811 0.4764 -0.0267 -0.0934 -0.1017 6   LYS B O   
2899 C CB  . LYS B 5   ? 0.7032 0.5713 0.5164 -0.0504 -0.1206 -0.1121 6   LYS B CB  
2900 C CG  . LYS B 5   ? 0.7342 0.6223 0.5204 -0.0498 -0.1157 -0.1111 6   LYS B CG  
2901 C CD  . LYS B 5   ? 0.7024 0.6103 0.4928 -0.0420 -0.1003 -0.0987 6   LYS B CD  
2902 C CE  . LYS B 5   ? 0.7256 0.6514 0.4874 -0.0382 -0.0927 -0.1003 6   LYS B CE  
2903 N NZ  . LYS B 5   ? 0.6757 0.6201 0.4416 -0.0299 -0.0767 -0.0889 6   LYS B NZ  
2904 N N   . ASP B 6   ? 0.6878 0.5216 0.5563 -0.0400 -0.1170 -0.1134 7   ASP B N   
2905 C CA  . ASP B 6   ? 0.6899 0.5182 0.5896 -0.0386 -0.1157 -0.1038 7   ASP B CA  
2906 C C   . ASP B 6   ? 0.6620 0.4884 0.5674 -0.0225 -0.0993 -0.1083 7   ASP B C   
2907 O O   . ASP B 6   ? 0.5457 0.3823 0.4697 -0.0185 -0.0912 -0.0962 7   ASP B O   
2908 C CB  . ASP B 6   ? 0.7537 0.5594 0.6681 -0.0457 -0.1294 -0.1088 7   ASP B CB  
2909 C CG  . ASP B 6   ? 0.7631 0.5713 0.6796 -0.0623 -0.1458 -0.1004 7   ASP B CG  
2910 O OD1 . ASP B 6   ? 0.7060 0.5300 0.6341 -0.0687 -0.1475 -0.0834 7   ASP B OD1 
2911 O OD2 . ASP B 6   ? 0.8351 0.6295 0.7421 -0.0688 -0.1569 -0.1110 7   ASP B OD2 
2912 N N   . GLN B 7   ? 0.6632 0.4765 0.5528 -0.0131 -0.0943 -0.1261 8   GLN B N   
2913 C CA  . GLN B 7   ? 0.6258 0.4356 0.5198 0.0027  -0.0788 -0.1316 8   GLN B CA  
2914 C C   . GLN B 7   ? 0.5847 0.4167 0.4666 0.0110  -0.0639 -0.1261 8   GLN B C   
2915 O O   . GLN B 7   ? 0.5744 0.4118 0.4697 0.0209  -0.0512 -0.1208 8   GLN B O   
2916 C CB  . GLN B 7   ? 0.7208 0.5096 0.6006 0.0101  -0.0783 -0.1525 8   GLN B CB  
2917 C CG  . GLN B 7   ? 0.7943 0.5600 0.6858 0.0020  -0.0928 -0.1588 8   GLN B CG  
2918 C CD  . GLN B 7   ? 0.9044 0.6504 0.7775 0.0070  -0.0940 -0.1805 8   GLN B CD  
2919 O OE1 . GLN B 7   ? 0.9133 0.6518 0.7828 0.0207  -0.0824 -0.1907 8   GLN B OE1 
2920 N NE2 . GLN B 7   ? 0.9491 0.6870 0.8103 -0.0040 -0.1081 -0.1878 8   GLN B NE2 
2921 N N   . GLU B 8   ? 0.6053 0.4505 0.4624 0.0070  -0.0652 -0.1269 9   GLU B N   
2922 C CA  . GLU B 8   ? 0.5955 0.4630 0.4419 0.0137  -0.0514 -0.1198 9   GLU B CA  
2923 C C   . GLU B 8   ? 0.5519 0.4350 0.4214 0.0098  -0.0486 -0.0999 9   GLU B C   
2924 O O   . GLU B 8   ? 0.5095 0.4030 0.3865 0.0196  -0.0342 -0.0943 9   GLU B O   
2925 C CB  . GLU B 8   ? 0.6897 0.5691 0.5068 0.0085  -0.0550 -0.1227 9   GLU B CB  
2926 C CG  . GLU B 8   ? 0.7333 0.6350 0.5368 0.0167  -0.0397 -0.1168 9   GLU B CG  
2927 C CD  . GLU B 8   ? 0.7335 0.6530 0.5185 0.0075  -0.0446 -0.1100 9   GLU B CD  
2928 O OE1 . GLU B 8   ? 0.6957 0.6102 0.4765 -0.0052 -0.0600 -0.1106 9   GLU B OE1 
2929 O OE2 . GLU B 8   ? 0.7037 0.6420 0.4787 0.0132  -0.0326 -0.1035 9   GLU B OE2 
2930 N N   . ILE B 9   ? 0.5663 0.4515 0.4477 -0.0045 -0.0622 -0.0892 10  ILE B N   
2931 C CA  . ILE B 9   ? 0.5135 0.4134 0.4167 -0.0093 -0.0608 -0.0703 10  ILE B CA  
2932 C C   . ILE B 9   ? 0.4761 0.3687 0.4071 -0.0020 -0.0547 -0.0671 10  ILE B C   
2933 O O   . ILE B 9   ? 0.4083 0.3148 0.3527 0.0026  -0.0442 -0.0563 10  ILE B O   
2934 C CB  . ILE B 9   ? 0.5102 0.4117 0.4205 -0.0260 -0.0776 -0.0605 10  ILE B CB  
2935 C CG1 . ILE B 9   ? 0.5986 0.5074 0.4816 -0.0336 -0.0843 -0.0635 10  ILE B CG1 
2936 C CG2 . ILE B 9   ? 0.4415 0.3591 0.3734 -0.0308 -0.0760 -0.0413 10  ILE B CG2 
2937 C CD1 . ILE B 9   ? 0.6018 0.5312 0.4676 -0.0284 -0.0722 -0.0594 10  ILE B CD1 
2938 N N   . LYS B 10  ? 0.4768 0.3477 0.4177 -0.0013 -0.0612 -0.0761 11  LYS B N   
2939 C CA  . LYS B 10  ? 0.4473 0.3103 0.4152 0.0054  -0.0563 -0.0730 11  LYS B CA  
2940 C C   . LYS B 10  ? 0.4545 0.3227 0.4203 0.0214  -0.0377 -0.0769 11  LYS B C   
2941 O O   . LYS B 10  ? 0.4380 0.3143 0.4247 0.0262  -0.0295 -0.0670 11  LYS B O   
2942 C CB  . LYS B 10  ? 0.5270 0.3646 0.5027 0.0041  -0.0660 -0.0836 11  LYS B CB  
2943 C CG  . LYS B 10  ? 0.6017 0.4295 0.6040 0.0123  -0.0604 -0.0821 11  LYS B CG  
2944 C CD  . LYS B 10  ? 0.5970 0.4323 0.6278 0.0042  -0.0664 -0.0645 11  LYS B CD  
2945 C CE  . LYS B 10  ? 0.6346 0.4549 0.6914 0.0101  -0.0655 -0.0650 11  LYS B CE  
2946 N NZ  . LYS B 10  ? 0.6411 0.4360 0.6923 0.0104  -0.0729 -0.0802 11  LYS B NZ  
2947 N N   . LYS B 11  ? 0.4795 0.3434 0.4202 0.0299  -0.0311 -0.0915 12  LYS B N   
2948 C CA  . LYS B 11  ? 0.4875 0.3569 0.4239 0.0455  -0.0130 -0.0955 12  LYS B CA  
2949 C C   . LYS B 11  ? 0.4842 0.3784 0.4242 0.0466  -0.0027 -0.0808 12  LYS B C   
2950 O O   . LYS B 11  ? 0.4492 0.3495 0.4064 0.0550  0.0089  -0.0746 12  LYS B O   
2951 C CB  . LYS B 11  ? 0.5414 0.4048 0.4469 0.0531  -0.0086 -0.1127 12  LYS B CB  
2952 C CG  . LYS B 11  ? 0.6255 0.4980 0.5228 0.0689  0.0106  -0.1157 12  LYS B CG  
2953 C CD  . LYS B 11  ? 0.7081 0.5854 0.5711 0.0734  0.0149  -0.1269 12  LYS B CD  
2954 C CE  . LYS B 11  ? 0.7538 0.6101 0.6021 0.0802  0.0133  -0.1469 12  LYS B CE  
2955 N NZ  . LYS B 11  ? 0.8287 0.6764 0.6875 0.0955  0.0267  -0.1525 12  LYS B NZ  
2956 N N   . LEU B 12  ? 0.4633 0.3720 0.3875 0.0381  -0.0068 -0.0751 13  LEU B N   
2957 C CA  . LEU B 12  ? 0.4348 0.3671 0.3601 0.0389  0.0033  -0.0618 13  LEU B CA  
2958 C C   . LEU B 12  ? 0.3894 0.3289 0.3458 0.0342  0.0024  -0.0460 13  LEU B C   
2959 O O   . LEU B 12  ? 0.3744 0.3276 0.3414 0.0408  0.0152  -0.0377 13  LEU B O   
2960 C CB  . LEU B 12  ? 0.4533 0.3981 0.3568 0.0293  -0.0029 -0.0584 13  LEU B CB  
2961 C CG  . LEU B 12  ? 0.5348 0.4782 0.4054 0.0347  0.0002  -0.0724 13  LEU B CG  
2962 C CD1 . LEU B 12  ? 0.5296 0.4828 0.3818 0.0228  -0.0097 -0.0687 13  LEU B CD1 
2963 C CD2 . LEU B 12  ? 0.5169 0.4721 0.3783 0.0492  0.0196  -0.0737 13  LEU B CD2 
2964 N N   . VAL B 13  ? 0.3821 0.3129 0.3540 0.0230  -0.0127 -0.0414 14  VAL B N   
2965 C CA  . VAL B 13  ? 0.3553 0.2936 0.3568 0.0181  -0.0144 -0.0263 14  VAL B CA  
2966 C C   . VAL B 13  ? 0.3632 0.2930 0.3864 0.0291  -0.0061 -0.0283 14  VAL B C   
2967 O O   . VAL B 13  ? 0.3447 0.2862 0.3880 0.0318  0.0015  -0.0173 14  VAL B O   
2968 C CB  . VAL B 13  ? 0.3452 0.2775 0.3560 0.0030  -0.0330 -0.0204 14  VAL B CB  
2969 C CG1 . VAL B 13  ? 0.3288 0.2669 0.3709 -0.0011 -0.0353 -0.0059 14  VAL B CG1 
2970 C CG2 . VAL B 13  ? 0.3331 0.2772 0.3243 -0.0078 -0.0399 -0.0159 14  VAL B CG2 
2971 N N   . ASP B 14  ? 0.3927 0.3022 0.4119 0.0358  -0.0069 -0.0424 15  ASP B N   
2972 C CA  . ASP B 14  ? 0.4028 0.3043 0.4400 0.0478  0.0027  -0.0454 15  ASP B CA  
2973 C C   . ASP B 14  ? 0.4004 0.3159 0.4329 0.0604  0.0215  -0.0445 15  ASP B C   
2974 O O   . ASP B 14  ? 0.4130 0.3334 0.4671 0.0673  0.0306  -0.0382 15  ASP B O   
2975 C CB  . ASP B 14  ? 0.4373 0.3143 0.4673 0.0533  -0.0006 -0.0621 15  ASP B CB  
2976 C CG  . ASP B 14  ? 0.5005 0.3610 0.5451 0.0433  -0.0171 -0.0618 15  ASP B CG  
2977 O OD1 . ASP B 14  ? 0.4538 0.3212 0.5175 0.0335  -0.0252 -0.0482 15  ASP B OD1 
2978 O OD2 . ASP B 14  ? 0.5042 0.3444 0.5406 0.0455  -0.0217 -0.0757 15  ASP B OD2 
2979 N N   . GLN B 15  ? 0.4088 0.3311 0.4136 0.0639  0.0277  -0.0509 16  GLN B N   
2980 C CA  . GLN B 15  ? 0.4088 0.3439 0.4074 0.0766  0.0461  -0.0508 16  GLN B CA  
2981 C C   . GLN B 15  ? 0.3881 0.3453 0.4023 0.0735  0.0523  -0.0338 16  GLN B C   
2982 O O   . GLN B 15  ? 0.3960 0.3614 0.4220 0.0834  0.0665  -0.0300 16  GLN B O   
2983 C CB  . GLN B 15  ? 0.4355 0.3738 0.4001 0.0803  0.0506  -0.0607 16  GLN B CB  
2984 C CG  . GLN B 15  ? 0.5738 0.4919 0.5203 0.0862  0.0479  -0.0793 16  GLN B CG  
2985 C CD  . GLN B 15  ? 0.6602 0.5844 0.5742 0.0925  0.0553  -0.0885 16  GLN B CD  
2986 O OE1 . GLN B 15  ? 0.7258 0.6562 0.6338 0.1057  0.0711  -0.0914 16  GLN B OE1 
2987 N NE2 . GLN B 15  ? 0.6530 0.5765 0.5462 0.0830  0.0441  -0.0928 16  GLN B NE2 
2988 N N   . ASN B 16  ? 0.3529 0.3198 0.3678 0.0597  0.0419  -0.0236 17  ASN B N   
2989 C CA  . ASN B 16  ? 0.3723 0.3614 0.3958 0.0564  0.0483  -0.0087 17  ASN B CA  
2990 C C   . ASN B 16  ? 0.3389 0.3327 0.3926 0.0479  0.0412  0.0049  17  ASN B C   
2991 O O   . ASN B 16  ? 0.3542 0.3635 0.4232 0.0499  0.0504  0.0156  17  ASN B O   
2992 C CB  . ASN B 16  ? 0.3136 0.3142 0.3138 0.0480  0.0443  -0.0059 17  ASN B CB  
2993 C CG  . ASN B 16  ? 0.3883 0.3909 0.3594 0.0576  0.0548  -0.0164 17  ASN B CG  
2994 O OD1 . ASN B 16  ? 0.3817 0.3965 0.3507 0.0672  0.0706  -0.0139 17  ASN B OD1 
2995 N ND2 . ASN B 16  ? 0.3720 0.3630 0.3207 0.0551  0.0461  -0.0280 17  ASN B ND2 
2996 N N   . PHE B 17  ? 0.3077 0.2888 0.3704 0.0386  0.0254  0.0049  18  PHE B N   
2997 C CA  . PHE B 17  ? 0.3364 0.3223 0.4272 0.0304  0.0179  0.0180  18  PHE B CA  
2998 C C   . PHE B 17  ? 0.3312 0.3050 0.4467 0.0368  0.0187  0.0163  18  PHE B C   
2999 O O   . PHE B 17  ? 0.2868 0.2703 0.4269 0.0369  0.0219  0.0270  18  PHE B O   
3000 C CB  . PHE B 17  ? 0.2689 0.2512 0.3563 0.0150  -0.0003 0.0219  18  PHE B CB  
3001 C CG  . PHE B 17  ? 0.2470 0.2467 0.3201 0.0064  -0.0016 0.0300  18  PHE B CG  
3002 C CD1 . PHE B 17  ? 0.3006 0.3002 0.3438 0.0059  -0.0016 0.0222  18  PHE B CD1 
3003 C CD2 . PHE B 17  ? 0.2789 0.2951 0.3682 -0.0007 -0.0023 0.0452  18  PHE B CD2 
3004 C CE1 . PHE B 17  ? 0.2849 0.3007 0.3149 -0.0015 -0.0022 0.0300  18  PHE B CE1 
3005 C CE2 . PHE B 17  ? 0.2482 0.2801 0.3244 -0.0083 -0.0029 0.0527  18  PHE B CE2 
3006 C CZ  . PHE B 17  ? 0.2347 0.2664 0.2815 -0.0087 -0.0028 0.0454  18  PHE B CZ  
3007 N N   . LYS B 18  ? 0.3570 0.3103 0.4666 0.0424  0.0162  0.0030  19  LYS B N   
3008 C CA  . LYS B 18  ? 0.3459 0.2865 0.4787 0.0488  0.0168  0.0012  19  LYS B CA  
3009 C C   . LYS B 18  ? 0.3207 0.2721 0.4706 0.0601  0.0326  0.0061  19  LYS B C   
3010 O O   . LYS B 18  ? 0.3441 0.2972 0.5215 0.0596  0.0311  0.0144  19  LYS B O   
3011 C CB  . LYS B 18  ? 0.3584 0.2757 0.4781 0.0549  0.0145  -0.0156 19  LYS B CB  
3012 C CG  . LYS B 18  ? 0.3869 0.2888 0.5302 0.0606  0.0136  -0.0177 19  LYS B CG  
3013 C CD  . LYS B 18  ? 0.4668 0.3475 0.5971 0.0708  0.0169  -0.0350 19  LYS B CD  
3014 C CE  . LYS B 18  ? 0.4697 0.3346 0.5812 0.0626  0.0033  -0.0450 19  LYS B CE  
3015 N NZ  . LYS B 18  ? 0.4966 0.3383 0.6024 0.0714  0.0046  -0.0609 19  LYS B NZ  
3016 N N   . PRO B 19  ? 0.3392 0.2989 0.4752 0.0704  0.0479  0.0020  20  PRO B N   
3017 C CA  . PRO B 19  ? 0.3922 0.3623 0.5464 0.0810  0.0630  0.0072  20  PRO B CA  
3018 C C   . PRO B 19  ? 0.3102 0.2994 0.4873 0.0739  0.0627  0.0238  20  PRO B C   
3019 O O   . PRO B 19  ? 0.3453 0.3401 0.5456 0.0802  0.0705  0.0293  20  PRO B O   
3020 C CB  . PRO B 19  ? 0.3594 0.3369 0.4902 0.0907  0.0779  0.0008  20  PRO B CB  
3021 C CG  . PRO B 19  ? 0.3693 0.3333 0.4710 0.0889  0.0709  -0.0122 20  PRO B CG  
3022 C CD  . PRO B 19  ? 0.3780 0.3388 0.4818 0.0731  0.0526  -0.0072 20  PRO B CD  
3023 N N   . LEU B 20  ? 0.3000 0.2996 0.4714 0.0610  0.0538  0.0319  21  LEU B N   
3024 C CA  . LEU B 20  ? 0.2734 0.2915 0.4654 0.0538  0.0531  0.0474  21  LEU B CA  
3025 C C   . LEU B 20  ? 0.2597 0.2731 0.4813 0.0501  0.0443  0.0539  21  LEU B C   
3026 O O   . LEU B 20  ? 0.2589 0.2861 0.5032 0.0497  0.0482  0.0647  21  LEU B O   
3027 C CB  . LEU B 20  ? 0.2646 0.2927 0.4426 0.0405  0.0443  0.0538  21  LEU B CB  
3028 C CG  . LEU B 20  ? 0.2806 0.3175 0.4307 0.0431  0.0533  0.0502  21  LEU B CG  
3029 C CD1 . LEU B 20  ? 0.3063 0.3494 0.4413 0.0296  0.0423  0.0551  21  LEU B CD1 
3030 C CD2 . LEU B 20  ? 0.2846 0.3397 0.4422 0.0503  0.0701  0.0567  21  LEU B CD2 
3031 N N   . LEU B 21  ? 0.2622 0.2564 0.4844 0.0476  0.0325  0.0476  22  LEU B N   
3032 C CA  . LEU B 21  ? 0.2580 0.2476 0.5084 0.0446  0.0243  0.0541  22  LEU B CA  
3033 C C   . LEU B 21  ? 0.2764 0.2660 0.5471 0.0574  0.0363  0.0537  22  LEU B C   
3034 O O   . LEU B 21  ? 0.2546 0.2527 0.5521 0.0560  0.0354  0.0640  22  LEU B O   
3035 C CB  . LEU B 21  ? 0.2825 0.2506 0.5289 0.0398  0.0099  0.0471  22  LEU B CB  
3036 C CG  . LEU B 21  ? 0.2954 0.2629 0.5272 0.0255  -0.0048 0.0493  22  LEU B CG  
3037 C CD1 . LEU B 21  ? 0.3784 0.3320 0.5802 0.0272  -0.0059 0.0349  22  LEU B CD1 
3038 C CD2 . LEU B 21  ? 0.3039 0.2628 0.5553 0.0167  -0.0203 0.0553  22  LEU B CD2 
3039 N N   . GLU B 22  ? 0.2877 0.2681 0.5463 0.0701  0.0477  0.0420  23  GLU B N   
3040 C CA  . GLU B 22  ? 0.2920 0.2732 0.5686 0.0830  0.0604  0.0416  23  GLU B CA  
3041 C C   . GLU B 22  ? 0.3070 0.3114 0.5930 0.0855  0.0728  0.0513  23  GLU B C   
3042 O O   . GLU B 22  ? 0.2968 0.3090 0.6085 0.0899  0.0783  0.0583  23  GLU B O   
3043 C CB  . GLU B 22  ? 0.3594 0.3248 0.6186 0.0960  0.0695  0.0262  23  GLU B CB  
3044 C CG  . GLU B 22  ? 0.4214 0.3834 0.6993 0.1099  0.0813  0.0244  23  GLU B CG  
3045 C CD  . GLU B 22  ? 0.4033 0.3823 0.6821 0.1194  0.0992  0.0273  23  GLU B CD  
3046 O OE1 . GLU B 22  ? 0.4719 0.4660 0.7380 0.1152  0.1028  0.0314  23  GLU B OE1 
3047 O OE2 . GLU B 22  ? 0.4917 0.4694 0.7799 0.1292  0.1083  0.0255  23  GLU B OE2 
3048 N N   . LYS B 23  ? 0.2796 0.2956 0.5456 0.0828  0.0775  0.0519  24  LYS B N   
3049 C CA  . LYS B 23  ? 0.3063 0.3434 0.5789 0.0862  0.0910  0.0598  24  LYS B CA  
3050 C C   . LYS B 23  ? 0.2835 0.3343 0.5750 0.0744  0.0842  0.0736  24  LYS B C   
3051 O O   . LYS B 23  ? 0.2961 0.3526 0.5859 0.0722  0.0892  0.0770  24  LYS B O   
3052 C CB  . LYS B 23  ? 0.3082 0.3534 0.5527 0.0844  0.0960  0.0575  24  LYS B CB  
3053 C CG  . LYS B 23  ? 0.2941 0.3580 0.5367 0.0850  0.1080  0.0644  24  LYS B CG  
3054 C CD  . LYS B 23  ? 0.3385 0.4080 0.5541 0.0883  0.1164  0.0599  24  LYS B CD  
3055 C CE  . LYS B 23  ? 0.3515 0.4311 0.5514 0.0803  0.1176  0.0655  24  LYS B CE  
3056 N NZ  . LYS B 23  ? 0.3238 0.4076 0.4960 0.0821  0.1233  0.0612  24  LYS B NZ  
3057 N N   . TYR B 24  ? 0.2412 0.2929 0.5414 0.0637  0.0699  0.0800  25  TYR B N   
3058 C CA  . TYR B 24  ? 0.2196 0.2792 0.5236 0.0485  0.0610  0.0908  25  TYR B CA  
3059 C C   . TYR B 24  ? 0.2330 0.2836 0.5556 0.0432  0.0490  0.0934  25  TYR B C   
3060 O O   . TYR B 24  ? 0.2240 0.2771 0.5468 0.0304  0.0407  0.1015  25  TYR B O   
3061 C CB  . TYR B 24  ? 0.2312 0.2996 0.5215 0.0373  0.0540  0.0966  25  TYR B CB  
3062 C CG  . TYR B 24  ? 0.2246 0.3014 0.4922 0.0406  0.0655  0.0944  25  TYR B CG  
3063 C CD1 . TYR B 24  ? 0.2532 0.3307 0.5049 0.0380  0.0694  0.0968  25  TYR B CD1 
3064 C CD2 . TYR B 24  ? 0.2318 0.3120 0.4897 0.0469  0.0710  0.0886  25  TYR B CD2 
3065 C CE1 . TYR B 24  ? 0.2419 0.3240 0.4713 0.0409  0.0772  0.0939  25  TYR B CE1 
3066 C CE2 . TYR B 24  ? 0.2328 0.3205 0.4676 0.0495  0.0818  0.0866  25  TYR B CE2 
3067 C CZ  . TYR B 24  ? 0.2415 0.3289 0.4618 0.0460  0.0836  0.0890  25  TYR B CZ  
3068 O OH  . TYR B 24  ? 0.2805 0.3711 0.4763 0.0481  0.0903  0.0857  25  TYR B OH  
3069 N N   . ASP B 25  ? 0.2650 0.3011 0.5980 0.0530  0.0483  0.0860  26  ASP B N   
3070 C CA  . ASP B 25  ? 0.2528 0.2784 0.6008 0.0483  0.0366  0.0873  26  ASP B CA  
3071 C C   . ASP B 25  ? 0.2524 0.2794 0.6006 0.0338  0.0204  0.0940  26  ASP B C   
3072 O O   . ASP B 25  ? 0.2132 0.2452 0.5676 0.0219  0.0136  0.1007  26  ASP B O   
3073 C CB  . ASP B 25  ? 0.2783 0.3096 0.6359 0.0458  0.0408  0.0913  26  ASP B CB  
3074 C CG  . ASP B 25  ? 0.4090 0.4292 0.7818 0.0458  0.0331  0.0898  26  ASP B CG  
3075 O OD1 . ASP B 25  ? 0.3561 0.3598 0.7292 0.0511  0.0274  0.0829  26  ASP B OD1 
3076 O OD2 . ASP B 25  ? 0.4483 0.4740 0.8306 0.0407  0.0331  0.0949  26  ASP B OD2 
3077 N N   . VAL B 26  ? 0.2437 0.2644 0.5794 0.0334  0.0147  0.0910  27  VAL B N   
3078 C CA  . VAL B 26  ? 0.1967 0.2175 0.5277 0.0191  -0.0012 0.0966  27  VAL B CA  
3079 C C   . VAL B 26  ? 0.2360 0.2367 0.5743 0.0171  -0.0138 0.0929  27  VAL B C   
3080 O O   . VAL B 26  ? 0.2547 0.2370 0.5816 0.0241  -0.0120 0.0806  27  VAL B O   
3081 C CB  . VAL B 26  ? 0.2413 0.2621 0.5411 0.0143  -0.0021 0.0912  27  VAL B CB  
3082 C CG1 . VAL B 26  ? 0.2027 0.2239 0.4980 -0.0006 -0.0186 0.0974  27  VAL B CG1 
3083 C CG2 . VAL B 26  ? 0.2074 0.2468 0.4994 0.0176  0.0117  0.0942  27  VAL B CG2 
3084 N N   . PRO B 27  ? 0.2219 0.2302 0.5677 0.0043  -0.0246 0.0982  28  PRO B N   
3085 C CA  . PRO B 27  ? 0.2076 0.2004 0.5579 0.0025  -0.0356 0.0935  28  PRO B CA  
3086 C C   . PRO B 27  ? 0.2051 0.1769 0.5383 -0.0001 -0.0456 0.0877  28  PRO B C   
3087 O O   . PRO B 27  ? 0.2152 0.1634 0.5480 0.0055  -0.0482 0.0792  28  PRO B O   
3088 C CB  . PRO B 27  ? 0.2340 0.2489 0.5946 -0.0097 -0.0438 0.0998  28  PRO B CB  
3089 C CG  . PRO B 27  ? 0.2397 0.2686 0.5923 -0.0104 -0.0327 0.1042  28  PRO B CG  
3090 C CD  . PRO B 27  ? 0.2194 0.2500 0.5674 -0.0076 -0.0245 0.1061  28  PRO B CD  
3091 N N   . GLY B 28  ? 0.2402 0.2166 0.3198 0.0201  -0.0505 0.0132  29  GLY B N   
3092 C CA  . GLY B 28  ? 0.2389 0.2089 0.3230 0.0176  -0.0500 0.0130  29  GLY B CA  
3093 C C   . GLY B 28  ? 0.2762 0.2477 0.3561 0.0138  -0.0508 0.0116  29  GLY B C   
3094 O O   . GLY B 28  ? 0.2551 0.2314 0.3279 0.0132  -0.0508 0.0125  29  GLY B O   
3095 N N   . MET B 29  ? 0.2480 0.2154 0.3325 0.0112  -0.0515 0.0091  30  MET B N   
3096 C CA  . MET B 29  ? 0.2566 0.2253 0.3379 0.0082  -0.0529 0.0069  30  MET B CA  
3097 C C   . MET B 29  ? 0.2745 0.2393 0.3646 0.0061  -0.0534 0.0065  30  MET B C   
3098 O O   . MET B 29  ? 0.2612 0.2216 0.3585 0.0061  -0.0532 0.0048  30  MET B O   
3099 C CB  . MET B 29  ? 0.2289 0.1984 0.3034 0.0074  -0.0547 0.0004  30  MET B CB  
3100 C CG  . MET B 29  ? 0.2310 0.2011 0.3005 0.0052  -0.0565 -0.0019 30  MET B CG  
3101 S SD  . MET B 29  ? 0.2990 0.2670 0.3586 0.0047  -0.0581 -0.0095 30  MET B SD  
3102 C CE  . MET B 29  ? 0.3591 0.3312 0.4097 0.0057  -0.0550 -0.0089 30  MET B CE  
3103 N N   . ALA B 30  ? 0.2239 0.1906 0.3141 0.0043  -0.0538 0.0078  31  ALA B N   
3104 C CA  . ALA B 30  ? 0.2257 0.1906 0.3252 0.0019  -0.0550 0.0060  31  ALA B CA  
3105 C C   . ALA B 30  ? 0.2317 0.1997 0.3265 0.0005  -0.0585 0.0021  31  ALA B C   
3106 O O   . ALA B 30  ? 0.2408 0.2121 0.3279 0.0010  -0.0579 0.0043  31  ALA B O   
3107 C CB  . ALA B 30  ? 0.2261 0.1900 0.3330 0.0013  -0.0516 0.0119  31  ALA B CB  
3108 N N   . VAL B 31  ? 0.2268 0.1933 0.3253 -0.0010 -0.0620 -0.0038 32  VAL B N   
3109 C CA  . VAL B 31  ? 0.2268 0.1956 0.3204 -0.0015 -0.0661 -0.0078 32  VAL B CA  
3110 C C   . VAL B 31  ? 0.2395 0.2092 0.3456 -0.0037 -0.0687 -0.0102 32  VAL B C   
3111 O O   . VAL B 31  ? 0.2406 0.2072 0.3553 -0.0052 -0.0694 -0.0134 32  VAL B O   
3112 C CB  . VAL B 31  ? 0.2305 0.1966 0.3139 -0.0007 -0.0687 -0.0138 32  VAL B CB  
3113 C CG1 . VAL B 31  ? 0.2710 0.2381 0.3480 -0.0005 -0.0731 -0.0177 32  VAL B CG1 
3114 C CG2 . VAL B 31  ? 0.2585 0.2245 0.3315 0.0010  -0.0656 -0.0121 32  VAL B CG2 
3115 N N   . GLY B 32  ? 0.2309 0.2049 0.3387 -0.0040 -0.0699 -0.0089 33  GLY B N   
3116 C CA  . GLY B 32  ? 0.2329 0.2096 0.3536 -0.0060 -0.0729 -0.0117 33  GLY B CA  
3117 C C   . GLY B 32  ? 0.2405 0.2204 0.3552 -0.0048 -0.0788 -0.0160 33  GLY B C   
3118 O O   . GLY B 32  ? 0.2279 0.2088 0.3306 -0.0026 -0.0785 -0.0139 33  GLY B O   
3119 N N   . VAL B 33  ? 0.2345 0.2156 0.3572 -0.0062 -0.0841 -0.0223 34  VAL B N   
3120 C CA  . VAL B 33  ? 0.2423 0.2270 0.3612 -0.0047 -0.0908 -0.0267 34  VAL B CA  
3121 C C   . VAL B 33  ? 0.2487 0.2396 0.3860 -0.0069 -0.0935 -0.0287 34  VAL B C   
3122 O O   . VAL B 33  ? 0.2471 0.2375 0.3986 -0.0102 -0.0928 -0.0310 34  VAL B O   
3123 C CB  . VAL B 33  ? 0.2812 0.2613 0.3897 -0.0038 -0.0960 -0.0338 34  VAL B CB  
3124 C CG1 . VAL B 33  ? 0.2602 0.2436 0.3643 -0.0016 -0.1036 -0.0384 34  VAL B CG1 
3125 C CG2 . VAL B 33  ? 0.2456 0.2197 0.3368 -0.0019 -0.0924 -0.0320 34  VAL B CG2 
3126 N N   . ILE B 34  ? 0.2567 0.2536 0.3947 -0.0050 -0.0963 -0.0280 35  ILE B N   
3127 C CA  . ILE B 34  ? 0.2665 0.2707 0.4223 -0.0066 -0.1004 -0.0314 35  ILE B CA  
3128 C C   . ILE B 34  ? 0.2734 0.2809 0.4222 -0.0035 -0.1095 -0.0372 35  ILE B C   
3129 O O   . ILE B 34  ? 0.2884 0.2946 0.4210 0.0006  -0.1105 -0.0352 35  ILE B O   
3130 C CB  . ILE B 34  ? 0.2700 0.2794 0.4368 -0.0070 -0.0953 -0.0252 35  ILE B CB  
3131 C CG1 . ILE B 34  ? 0.2988 0.3167 0.4870 -0.0092 -0.0993 -0.0297 35  ILE B CG1 
3132 C CG2 . ILE B 34  ? 0.3223 0.3323 0.4746 -0.0029 -0.0941 -0.0202 35  ILE B CG2 
3133 C CD1 . ILE B 34  ? 0.3349 0.3578 0.5363 -0.0099 -0.0938 -0.0243 35  ILE B CD1 
3134 N N   . GLN B 35  ? 0.2790 0.2898 0.4388 -0.0053 -0.1162 -0.0448 36  GLN B N   
3135 C CA  . GLN B 35  ? 0.3271 0.3416 0.4813 -0.0020 -0.1260 -0.0509 36  GLN B CA  
3136 C C   . GLN B 35  ? 0.3757 0.3995 0.5525 -0.0048 -0.1315 -0.0569 36  GLN B C   
3137 O O   . GLN B 35  ? 0.3458 0.3688 0.5356 -0.0096 -0.1308 -0.0610 36  GLN B O   
3138 C CB  . GLN B 35  ? 0.3625 0.3687 0.4991 -0.0007 -0.1301 -0.0562 36  GLN B CB  
3139 C CG  . GLN B 35  ? 0.4185 0.4270 0.5457 0.0037  -0.1402 -0.0619 36  GLN B CG  
3140 C CD  . GLN B 35  ? 0.4787 0.4786 0.5902 0.0045  -0.1448 -0.0683 36  GLN B CD  
3141 O OE1 . GLN B 35  ? 0.4149 0.4112 0.5322 0.0004  -0.1437 -0.0722 36  GLN B OE1 
3142 N NE2 . GLN B 35  ? 0.4974 0.4933 0.5884 0.0100  -0.1492 -0.0694 36  GLN B NE2 
3143 N N   . ASN B 36  ? 0.3498 0.3824 0.5318 -0.0017 -0.1368 -0.0576 37  ASN B N   
3144 C CA  . ASN B 36  ? 0.4180 0.4616 0.6226 -0.0038 -0.1431 -0.0639 37  ASN B CA  
3145 C C   . ASN B 36  ? 0.4121 0.4583 0.6403 -0.0101 -0.1355 -0.0624 37  ASN B C   
3146 O O   . ASN B 36  ? 0.3815 0.4308 0.6266 -0.0148 -0.1379 -0.0692 37  ASN B O   
3147 C CB  . ASN B 36  ? 0.3869 0.4303 0.5890 -0.0042 -0.1531 -0.0741 37  ASN B CB  
3148 C CG  . ASN B 36  ? 0.4083 0.4486 0.5869 0.0026  -0.1609 -0.0758 37  ASN B CG  
3149 O OD1 . ASN B 36  ? 0.4745 0.5186 0.6470 0.0079  -0.1626 -0.0721 37  ASN B OD1 
3150 N ND2 . ASN B 36  ? 0.4143 0.4465 0.5784 0.0028  -0.1650 -0.0813 37  ASN B ND2 
3151 N N   . ASN B 37  ? 0.3630 0.4070 0.5914 -0.0103 -0.1258 -0.0536 38  ASN B N   
3152 C CA  . ASN B 37  ? 0.4177 0.4626 0.6659 -0.0154 -0.1171 -0.0504 38  ASN B CA  
3153 C C   . ASN B 37  ? 0.3928 0.4292 0.6436 -0.0202 -0.1125 -0.0521 38  ASN B C   
3154 O O   . ASN B 37  ? 0.4962 0.5326 0.7648 -0.0249 -0.1060 -0.0513 38  ASN B O   
3155 C CB  . ASN B 37  ? 0.4062 0.4634 0.6803 -0.0176 -0.1202 -0.0551 38  ASN B CB  
3156 C CG  . ASN B 37  ? 0.5114 0.5776 0.7845 -0.0123 -0.1250 -0.0535 38  ASN B CG  
3157 O OD1 . ASN B 37  ? 0.5375 0.6073 0.8015 -0.0080 -0.1350 -0.0582 38  ASN B OD1 
3158 N ND2 . ASN B 37  ? 0.4369 0.5058 0.7183 -0.0122 -0.1175 -0.0468 38  ASN B ND2 
3159 N N   . LYS B 38  ? 0.3734 0.4021 0.6072 -0.0191 -0.1152 -0.0544 39  LYS B N   
3160 C CA  . LYS B 38  ? 0.3359 0.3554 0.5695 -0.0227 -0.1101 -0.0550 39  LYS B CA  
3161 C C   . LYS B 38  ? 0.3349 0.3454 0.5491 -0.0200 -0.1038 -0.0473 39  LYS B C   
3162 O O   . LYS B 38  ? 0.3172 0.3260 0.5125 -0.0158 -0.1069 -0.0462 39  LYS B O   
3163 C CB  . LYS B 38  ? 0.3967 0.4141 0.6278 -0.0240 -0.1178 -0.0645 39  LYS B CB  
3164 C CG  . LYS B 38  ? 0.4314 0.4562 0.6854 -0.0287 -0.1223 -0.0731 39  LYS B CG  
3165 C CD  . LYS B 38  ? 0.5384 0.5563 0.7928 -0.0323 -0.1239 -0.0805 39  LYS B CD  
3166 C CE  . LYS B 38  ? 0.5604 0.5658 0.8038 -0.0326 -0.1149 -0.0747 39  LYS B CE  
3167 N NZ  . LYS B 38  ? 0.5580 0.5559 0.8048 -0.0366 -0.1142 -0.0810 39  LYS B NZ  
3168 N N   . LYS B 39  ? 0.2640 0.2684 0.4828 -0.0224 -0.0950 -0.0424 40  LYS B N   
3169 C CA  . LYS B 39  ? 0.2698 0.2669 0.4730 -0.0200 -0.0888 -0.0350 40  LYS B CA  
3170 C C   . LYS B 39  ? 0.2838 0.2722 0.4797 -0.0207 -0.0878 -0.0373 40  LYS B C   
3171 O O   . LYS B 39  ? 0.2809 0.2667 0.4880 -0.0242 -0.0876 -0.0421 40  LYS B O   
3172 C CB  . LYS B 39  ? 0.2739 0.2696 0.4851 -0.0211 -0.0795 -0.0270 40  LYS B CB  
3173 C CG  . LYS B 39  ? 0.2651 0.2684 0.4829 -0.0203 -0.0789 -0.0238 40  LYS B CG  
3174 C CD  . LYS B 39  ? 0.2960 0.2964 0.5225 -0.0219 -0.0691 -0.0166 40  LYS B CD  
3175 C CE  . LYS B 39  ? 0.2783 0.2860 0.5130 -0.0214 -0.0677 -0.0137 40  LYS B CE  
3176 N NZ  . LYS B 39  ? 0.2861 0.2896 0.5286 -0.0231 -0.0574 -0.0069 40  LYS B NZ  
3177 N N   . TYR B 40  ? 0.2464 0.2303 0.4241 -0.0173 -0.0866 -0.0339 41  TYR B N   
3178 C CA  . TYR B 40  ? 0.2900 0.2660 0.4595 -0.0172 -0.0854 -0.0357 41  TYR B CA  
3179 C C   . TYR B 40  ? 0.2644 0.2364 0.4242 -0.0148 -0.0788 -0.0278 41  TYR B C   
3180 O O   . TYR B 40  ? 0.2817 0.2559 0.4297 -0.0119 -0.0788 -0.0242 41  TYR B O   
3181 C CB  . TYR B 40  ? 0.3138 0.2887 0.4696 -0.0153 -0.0924 -0.0420 41  TYR B CB  
3182 C CG  . TYR B 40  ? 0.3384 0.3180 0.5018 -0.0169 -0.1003 -0.0500 41  TYR B CG  
3183 C CD1 . TYR B 40  ? 0.3769 0.3536 0.5487 -0.0202 -0.1026 -0.0572 41  TYR B CD1 
3184 C CD2 . TYR B 40  ? 0.3106 0.2977 0.4732 -0.0150 -0.1055 -0.0506 41  TYR B CD2 
3185 C CE1 . TYR B 40  ? 0.4029 0.3846 0.5820 -0.0218 -0.1105 -0.0651 41  TYR B CE1 
3186 C CE2 . TYR B 40  ? 0.3796 0.3721 0.5500 -0.0159 -0.1136 -0.0582 41  TYR B CE2 
3187 C CZ  . TYR B 40  ? 0.4115 0.4015 0.5901 -0.0195 -0.1163 -0.0656 41  TYR B CZ  
3188 O OH  . TYR B 40  ? 0.4338 0.4297 0.6202 -0.0206 -0.1250 -0.0739 41  TYR B OH  
3189 N N   . GLU B 41  ? 0.3042 0.2703 0.4690 -0.0158 -0.0732 -0.0253 42  GLU B N   
3190 C CA  . GLU B 41  ? 0.2589 0.2216 0.4162 -0.0132 -0.0673 -0.0180 42  GLU B CA  
3191 C C   . GLU B 41  ? 0.2795 0.2364 0.4283 -0.0117 -0.0670 -0.0199 42  GLU B C   
3192 O O   . GLU B 41  ? 0.2522 0.2044 0.4070 -0.0135 -0.0672 -0.0245 42  GLU B O   
3193 C CB  . GLU B 41  ? 0.2980 0.2577 0.4667 -0.0145 -0.0604 -0.0125 42  GLU B CB  
3194 C CG  . GLU B 41  ? 0.2783 0.2432 0.4565 -0.0161 -0.0592 -0.0099 42  GLU B CG  
3195 C CD  . GLU B 41  ? 0.3183 0.2783 0.5079 -0.0177 -0.0516 -0.0053 42  GLU B CD  
3196 O OE1 . GLU B 41  ? 0.3471 0.2996 0.5342 -0.0165 -0.0472 -0.0024 42  GLU B OE1 
3197 O OE2 . GLU B 41  ? 0.4059 0.3692 0.6073 -0.0200 -0.0497 -0.0046 42  GLU B OE2 
3198 N N   . MET B 42  ? 0.2600 0.2170 0.3955 -0.0085 -0.0660 -0.0167 43  MET B N   
3199 C CA  . MET B 42  ? 0.2902 0.2427 0.4181 -0.0067 -0.0652 -0.0183 43  MET B CA  
3200 C C   . MET B 42  ? 0.2653 0.2179 0.3876 -0.0036 -0.0608 -0.0114 43  MET B C   
3201 O O   . MET B 42  ? 0.2638 0.2208 0.3789 -0.0024 -0.0607 -0.0079 43  MET B O   
3202 C CB  . MET B 42  ? 0.2848 0.2379 0.4011 -0.0060 -0.0699 -0.0241 43  MET B CB  
3203 C CG  . MET B 42  ? 0.3722 0.3232 0.4928 -0.0084 -0.0747 -0.0319 43  MET B CG  
3204 S SD  . MET B 42  ? 0.4894 0.4441 0.6002 -0.0080 -0.0818 -0.0371 43  MET B SD  
3205 C CE  . MET B 42  ? 0.3165 0.2793 0.4316 -0.0077 -0.0815 -0.0311 43  MET B CE  
3206 N N   . TYR B 43  ? 0.2456 0.1932 0.3711 -0.0023 -0.0573 -0.0096 44  TYR B N   
3207 C CA  . TYR B 43  ? 0.2439 0.1915 0.3652 0.0011  -0.0536 -0.0032 44  TYR B CA  
3208 C C   . TYR B 43  ? 0.2678 0.2136 0.3835 0.0037  -0.0535 -0.0054 44  TYR B C   
3209 O O   . TYR B 43  ? 0.2750 0.2160 0.3937 0.0029  -0.0539 -0.0103 44  TYR B O   
3210 C CB  . TYR B 43  ? 0.2478 0.1908 0.3781 0.0015  -0.0488 0.0024  44  TYR B CB  
3211 C CG  . TYR B 43  ? 0.2575 0.2021 0.3946 -0.0013 -0.0480 0.0044  44  TYR B CG  
3212 C CD1 . TYR B 43  ? 0.2699 0.2192 0.4020 -0.0005 -0.0473 0.0092  44  TYR B CD1 
3213 C CD2 . TYR B 43  ? 0.2568 0.1987 0.4058 -0.0049 -0.0477 0.0008  44  TYR B CD2 
3214 C CE1 . TYR B 43  ? 0.2411 0.1920 0.3800 -0.0029 -0.0461 0.0109  44  TYR B CE1 
3215 C CE2 . TYR B 43  ? 0.2878 0.2322 0.4448 -0.0075 -0.0467 0.0022  44  TYR B CE2 
3216 C CZ  . TYR B 43  ? 0.2781 0.2269 0.4300 -0.0064 -0.0458 0.0074  44  TYR B CZ  
3217 O OH  . TYR B 43  ? 0.2647 0.2160 0.4249 -0.0088 -0.0444 0.0087  44  TYR B OH  
3218 N N   . TYR B 44  ? 0.2628 0.2125 0.3707 0.0065  -0.0528 -0.0023 45  TYR B N   
3219 C CA  . TYR B 44  ? 0.2618 0.2114 0.3655 0.0093  -0.0522 -0.0040 45  TYR B CA  
3220 C C   . TYR B 44  ? 0.2682 0.2200 0.3710 0.0132  -0.0499 0.0023  45  TYR B C   
3221 O O   . TYR B 44  ? 0.2574 0.2133 0.3570 0.0136  -0.0496 0.0070  45  TYR B O   
3222 C CB  . TYR B 44  ? 0.2853 0.2389 0.3793 0.0087  -0.0544 -0.0085 45  TYR B CB  
3223 C CG  . TYR B 44  ? 0.2901 0.2412 0.3815 0.0058  -0.0573 -0.0148 45  TYR B CG  
3224 C CD1 . TYR B 44  ? 0.2994 0.2451 0.3914 0.0053  -0.0578 -0.0206 45  TYR B CD1 
3225 C CD2 . TYR B 44  ? 0.3360 0.2902 0.4235 0.0039  -0.0597 -0.0151 45  TYR B CD2 
3226 C CE1 . TYR B 44  ? 0.3585 0.3017 0.4466 0.0030  -0.0611 -0.0266 45  TYR B CE1 
3227 C CE2 . TYR B 44  ? 0.3406 0.2927 0.4248 0.0021  -0.0631 -0.0209 45  TYR B CE2 
3228 C CZ  . TYR B 44  ? 0.3729 0.3194 0.4569 0.0016  -0.0640 -0.0267 45  TYR B CZ  
3229 O OH  . TYR B 44  ? 0.3843 0.3284 0.4636 0.0001  -0.0679 -0.0326 45  TYR B OH  
3230 N N   . GLY B 45  ? 0.2568 0.2062 0.3619 0.0163  -0.0484 0.0023  46  GLY B N   
3231 C CA  . GLY B 45  ? 0.2805 0.2340 0.3830 0.0207  -0.0476 0.0069  46  GLY B CA  
3232 C C   . GLY B 45  ? 0.2763 0.2273 0.3812 0.0231  -0.0455 0.0145  46  GLY B C   
3233 O O   . GLY B 45  ? 0.2603 0.2042 0.3710 0.0220  -0.0433 0.0163  46  GLY B O   
3234 N N   . LEU B 46  ? 0.2555 0.2119 0.3553 0.0263  -0.0460 0.0187  47  LEU B N   
3235 C CA  . LEU B 46  ? 0.3048 0.2585 0.4040 0.0304  -0.0442 0.0261  47  LEU B CA  
3236 C C   . LEU B 46  ? 0.2780 0.2361 0.3706 0.0295  -0.0447 0.0301  47  LEU B C   
3237 O O   . LEU B 46  ? 0.3190 0.2840 0.4066 0.0272  -0.0467 0.0273  47  LEU B O   
3238 C CB  . LEU B 46  ? 0.3110 0.2670 0.4098 0.0365  -0.0449 0.0276  47  LEU B CB  
3239 C CG  . LEU B 46  ? 0.2760 0.2285 0.3809 0.0379  -0.0441 0.0233  47  LEU B CG  
3240 C CD1 . LEU B 46  ? 0.3250 0.2819 0.4299 0.0442  -0.0452 0.0246  47  LEU B CD1 
3241 C CD2 . LEU B 46  ? 0.2686 0.2096 0.3795 0.0374  -0.0405 0.0249  47  LEU B CD2 
3242 N N   . GLN B 47  ? 0.2953 0.2481 0.3870 0.0316  -0.0421 0.0368  48  GLN B N   
3243 C CA  . GLN B 47  ? 0.3441 0.2994 0.4287 0.0310  -0.0419 0.0411  48  GLN B CA  
3244 C C   . GLN B 47  ? 0.3912 0.3547 0.4681 0.0343  -0.0448 0.0419  48  GLN B C   
3245 O O   . GLN B 47  ? 0.3760 0.3446 0.4466 0.0322  -0.0457 0.0421  48  GLN B O   
3246 C CB  . GLN B 47  ? 0.3440 0.2902 0.4290 0.0327  -0.0376 0.0481  48  GLN B CB  
3247 C CG  . GLN B 47  ? 0.3194 0.2587 0.4133 0.0283  -0.0344 0.0467  48  GLN B CG  
3248 C CD  . GLN B 47  ? 0.4139 0.3440 0.5083 0.0290  -0.0290 0.0533  48  GLN B CD  
3249 O OE1 . GLN B 47  ? 0.4129 0.3395 0.5142 0.0247  -0.0261 0.0526  48  GLN B OE1 
3250 N NE2 . GLN B 47  ? 0.4522 0.3783 0.5394 0.0346  -0.0274 0.0597  48  GLN B NE2 
3251 N N   . SER B 48  ? 0.3921 0.3570 0.4700 0.0393  -0.0463 0.0421  49  SER B N   
3252 C CA  . SER B 48  ? 0.4925 0.4665 0.5652 0.0427  -0.0496 0.0418  49  SER B CA  
3253 C C   . SER B 48  ? 0.4878 0.4636 0.5660 0.0473  -0.0511 0.0396  49  SER B C   
3254 O O   . SER B 48  ? 0.4357 0.4034 0.5192 0.0496  -0.0489 0.0410  49  SER B O   
3255 C CB  . SER B 48  ? 0.4725 0.4453 0.5371 0.0464  -0.0497 0.0487  49  SER B CB  
3256 O OG  . SER B 48  ? 0.5296 0.4941 0.5949 0.0523  -0.0481 0.0542  49  SER B OG  
3257 N N   . VAL B 49  ? 0.5257 0.5120 0.6031 0.0487  -0.0544 0.0360  50  VAL B N   
3258 C CA  . VAL B 49  ? 0.5325 0.5217 0.6156 0.0541  -0.0559 0.0345  50  VAL B CA  
3259 C C   . VAL B 49  ? 0.5322 0.5176 0.6129 0.0617  -0.0566 0.0417  50  VAL B C   
3260 O O   . VAL B 49  ? 0.5303 0.5141 0.6160 0.0672  -0.0568 0.0422  50  VAL B O   
3261 C CB  . VAL B 49  ? 0.5655 0.5676 0.6498 0.0536  -0.0589 0.0285  50  VAL B CB  
3262 C CG1 . VAL B 49  ? 0.5149 0.5193 0.5982 0.0461  -0.0576 0.0224  50  VAL B CG1 
3263 C CG2 . VAL B 49  ? 0.5939 0.6043 0.6724 0.0567  -0.0625 0.0311  50  VAL B CG2 
3264 N N   . GLN B 50  ? 0.5487 0.5316 0.6210 0.0626  -0.0566 0.0474  51  GLN B N   
3265 C CA  . GLN B 50  ? 0.6045 0.5821 0.6721 0.0703  -0.0570 0.0547  51  GLN B CA  
3266 C C   . GLN B 50  ? 0.5180 0.4804 0.5876 0.0719  -0.0518 0.0594  51  GLN B C   
3267 O O   . GLN B 50  ? 0.5644 0.5216 0.6353 0.0788  -0.0514 0.0627  51  GLN B O   
3268 C CB  . GLN B 50  ? 0.6577 0.6369 0.7139 0.0709  -0.0586 0.0590  51  GLN B CB  
3269 C CG  . GLN B 50  ? 0.7556 0.7270 0.8042 0.0792  -0.0586 0.0672  51  GLN B CG  
3270 C CD  . GLN B 50  ? 0.8905 0.8650 0.9267 0.0806  -0.0613 0.0706  51  GLN B CD  
3271 O OE1 . GLN B 50  ? 0.9454 0.9158 0.9735 0.0881  -0.0628 0.0765  51  GLN B OE1 
3272 N NE2 . GLN B 50  ? 0.9416 0.9228 0.9755 0.0737  -0.0618 0.0669  51  GLN B NE2 
3273 N N   . ASP B 51  ? 0.5406 0.4956 0.6108 0.0657  -0.0476 0.0597  52  ASP B N   
3274 C CA  . ASP B 51  ? 0.5030 0.4436 0.5759 0.0667  -0.0421 0.0639  52  ASP B CA  
3275 C C   . ASP B 51  ? 0.4311 0.3683 0.5147 0.0643  -0.0402 0.0588  52  ASP B C   
3276 O O   . ASP B 51  ? 0.4459 0.3719 0.5326 0.0671  -0.0361 0.0617  52  ASP B O   
3277 C CB  . ASP B 51  ? 0.5308 0.4644 0.6005 0.0617  -0.0379 0.0670  52  ASP B CB  
3278 C CG  . ASP B 51  ? 0.5086 0.4464 0.5840 0.0528  -0.0378 0.0608  52  ASP B CG  
3279 O OD1 . ASP B 51  ? 0.4411 0.3857 0.5219 0.0501  -0.0404 0.0540  52  ASP B OD1 
3280 O OD2 . ASP B 51  ? 0.4805 0.4141 0.5544 0.0489  -0.0347 0.0630  52  ASP B OD2 
3281 N N   . LYS B 52  ? 0.4239 0.3697 0.5122 0.0595  -0.0426 0.0513  53  LYS B N   
3282 C CA  . LYS B 52  ? 0.3808 0.3236 0.4778 0.0568  -0.0412 0.0456  53  LYS B CA  
3283 C C   . LYS B 52  ? 0.3806 0.3116 0.4821 0.0527  -0.0363 0.0463  53  LYS B C   
3284 O O   . LYS B 52  ? 0.3189 0.2427 0.4268 0.0528  -0.0336 0.0443  53  LYS B O   
3285 C CB  . LYS B 52  ? 0.4415 0.3841 0.5422 0.0634  -0.0417 0.0453  53  LYS B CB  
3286 C CG  . LYS B 52  ? 0.4695 0.4258 0.5685 0.0666  -0.0468 0.0430  53  LYS B CG  
3287 C CD  . LYS B 52  ? 0.5044 0.4630 0.6100 0.0712  -0.0474 0.0398  53  LYS B CD  
3288 C CE  . LYS B 52  ? 0.4496 0.4232 0.5556 0.0729  -0.0521 0.0360  53  LYS B CE  
3289 N NZ  . LYS B 52  ? 0.5388 0.5180 0.6389 0.0789  -0.0557 0.0414  53  LYS B NZ  
3290 N N   . LYS B 53  ? 0.3751 0.3045 0.4738 0.0488  -0.0349 0.0487  54  LYS B N   
3291 C CA  . LYS B 53  ? 0.3206 0.2408 0.4249 0.0440  -0.0304 0.0487  54  LYS B CA  
3292 C C   . LYS B 53  ? 0.2927 0.2181 0.4014 0.0367  -0.0325 0.0414  54  LYS B C   
3293 O O   . LYS B 53  ? 0.2916 0.2262 0.3959 0.0345  -0.0360 0.0392  54  LYS B O   
3294 C CB  . LYS B 53  ? 0.4095 0.3245 0.5092 0.0441  -0.0271 0.0554  54  LYS B CB  
3295 C CG  . LYS B 53  ? 0.4978 0.3995 0.5971 0.0489  -0.0214 0.0620  54  LYS B CG  
3296 C CD  . LYS B 53  ? 0.5564 0.4584 0.6496 0.0576  -0.0234 0.0657  54  LYS B CD  
3297 C CE  . LYS B 53  ? 0.5787 0.4661 0.6728 0.0626  -0.0175 0.0706  54  LYS B CE  
3298 N NZ  . LYS B 53  ? 0.5100 0.3927 0.6145 0.0602  -0.0154 0.0653  54  LYS B NZ  
3299 N N   . ALA B 54  ? 0.2828 0.2019 0.3997 0.0331  -0.0303 0.0376  55  ALA B N   
3300 C CA  . ALA B 54  ? 0.2749 0.1981 0.3957 0.0268  -0.0328 0.0304  55  ALA B CA  
3301 C C   . ALA B 54  ? 0.2820 0.2095 0.4010 0.0229  -0.0335 0.0316  55  ALA B C   
3302 O O   . ALA B 54  ? 0.2965 0.2191 0.4166 0.0227  -0.0298 0.0367  55  ALA B O   
3303 C CB  . ALA B 54  ? 0.2807 0.1955 0.4109 0.0235  -0.0300 0.0265  55  ALA B CB  
3304 N N   . VAL B 55  ? 0.2618 0.1974 0.3776 0.0200  -0.0376 0.0268  56  VAL B N   
3305 C CA  . VAL B 55  ? 0.2763 0.2154 0.3920 0.0158  -0.0383 0.0266  56  VAL B CA  
3306 C C   . VAL B 55  ? 0.2629 0.1971 0.3892 0.0115  -0.0368 0.0235  56  VAL B C   
3307 O O   . VAL B 55  ? 0.2813 0.2127 0.4125 0.0100  -0.0378 0.0180  56  VAL B O   
3308 C CB  . VAL B 55  ? 0.2596 0.2073 0.3689 0.0141  -0.0428 0.0220  56  VAL B CB  
3309 C CG1 . VAL B 55  ? 0.2593 0.2099 0.3697 0.0100  -0.0436 0.0211  56  VAL B CG1 
3310 C CG2 . VAL B 55  ? 0.2631 0.2163 0.3634 0.0177  -0.0436 0.0251  56  VAL B CG2 
3311 N N   . ASN B 56  ? 0.2800 0.2129 0.4099 0.0093  -0.0342 0.0268  57  ASN B N   
3312 C CA  . ASN B 56  ? 0.2876 0.2162 0.4294 0.0051  -0.0321 0.0242  57  ASN B CA  
3313 C C   . ASN B 56  ? 0.2748 0.2074 0.4194 0.0021  -0.0316 0.0256  57  ASN B C   
3314 O O   . ASN B 56  ? 0.2790 0.2170 0.4154 0.0033  -0.0328 0.0285  57  ASN B O   
3315 C CB  . ASN B 56  ? 0.3005 0.2184 0.4475 0.0068  -0.0258 0.0282  57  ASN B CB  
3316 C CG  . ASN B 56  ? 0.3506 0.2649 0.4921 0.0101  -0.0212 0.0369  57  ASN B CG  
3317 O OD1 . ASN B 56  ? 0.3951 0.3069 0.5412 0.0077  -0.0173 0.0395  57  ASN B OD1 
3318 N ND2 . ASN B 56  ? 0.3922 0.3061 0.5235 0.0157  -0.0217 0.0412  57  ASN B ND2 
3319 N N   . SER B 57  ? 0.2980 0.2282 0.4551 -0.0019 -0.0295 0.0232  58  SER B N   
3320 C CA  . SER B 57  ? 0.2707 0.2053 0.4331 -0.0050 -0.0292 0.0235  58  SER B CA  
3321 C C   . SER B 57  ? 0.3048 0.2363 0.4635 -0.0032 -0.0234 0.0318  58  SER B C   
3322 O O   . SER B 57  ? 0.2963 0.2320 0.4576 -0.0051 -0.0227 0.0329  58  SER B O   
3323 C CB  . SER B 57  ? 0.2881 0.2214 0.4668 -0.0099 -0.0282 0.0183  58  SER B CB  
3324 O OG  . SER B 57  ? 0.3178 0.2410 0.5031 -0.0101 -0.0212 0.0211  58  SER B OG  
3325 N N   . SER B 58  ? 0.2773 0.2013 0.4298 0.0006  -0.0191 0.0377  59  SER B N   
3326 C CA  . SER B 58  ? 0.3033 0.2234 0.4487 0.0032  -0.0141 0.0457  59  SER B CA  
3327 C C   . SER B 58  ? 0.3152 0.2400 0.4451 0.0073  -0.0174 0.0489  59  SER B C   
3328 O O   . SER B 58  ? 0.3198 0.2424 0.4422 0.0092  -0.0141 0.0551  59  SER B O   
3329 C CB  . SER B 58  ? 0.3564 0.2638 0.5030 0.0056  -0.0069 0.0509  59  SER B CB  
3330 O OG  . SER B 58  ? 0.3787 0.2811 0.5402 0.0012  -0.0021 0.0485  59  SER B OG  
3331 N N   . THR B 59  ? 0.2868 0.2177 0.4118 0.0084  -0.0234 0.0446  60  THR B N   
3332 C CA  . THR B 59  ? 0.2777 0.2136 0.3894 0.0118  -0.0263 0.0468  60  THR B CA  
3333 C C   . THR B 59  ? 0.2953 0.2368 0.4019 0.0100  -0.0267 0.0481  60  THR B C   
3334 O O   . THR B 59  ? 0.2694 0.2153 0.3814 0.0064  -0.0284 0.0441  60  THR B O   
3335 C CB  . THR B 59  ? 0.2907 0.2322 0.4000 0.0125  -0.0318 0.0410  60  THR B CB  
3336 O OG1 . THR B 59  ? 0.3052 0.2408 0.4190 0.0145  -0.0308 0.0402  60  THR B OG1 
3337 C CG2 . THR B 59  ? 0.2982 0.2456 0.3952 0.0155  -0.0344 0.0425  60  THR B CG2 
3338 N N   . ILE B 60  ? 0.2714 0.2125 0.3673 0.0129  -0.0252 0.0536  61  ILE B N   
3339 C CA  . ILE B 60  ? 0.3146 0.2594 0.4043 0.0115  -0.0245 0.0556  61  ILE B CA  
3340 C C   . ILE B 60  ? 0.2617 0.2144 0.3410 0.0124  -0.0292 0.0530  61  ILE B C   
3341 O O   . ILE B 60  ? 0.3012 0.2549 0.3739 0.0158  -0.0310 0.0538  61  ILE B O   
3342 C CB  . ILE B 60  ? 0.3220 0.2597 0.4059 0.0136  -0.0188 0.0633  61  ILE B CB  
3343 C CG1 . ILE B 60  ? 0.3374 0.2671 0.4326 0.0117  -0.0129 0.0653  61  ILE B CG1 
3344 C CG2 . ILE B 60  ? 0.3395 0.2809 0.4146 0.0127  -0.0182 0.0653  61  ILE B CG2 
3345 C CD1 . ILE B 60  ? 0.4131 0.3329 0.5020 0.0142  -0.0061 0.0732  61  ILE B CD1 
3346 N N   . PHE B 61  ? 0.3009 0.2593 0.3794 0.0095  -0.0310 0.0497  62  PHE B N   
3347 C CA  . PHE B 61  ? 0.2802 0.2453 0.3492 0.0096  -0.0344 0.0466  62  PHE B CA  
3348 C C   . PHE B 61  ? 0.3072 0.2736 0.3684 0.0086  -0.0320 0.0497  62  PHE B C   
3349 O O   . PHE B 61  ? 0.2947 0.2590 0.3604 0.0068  -0.0291 0.0517  62  PHE B O   
3350 C CB  . PHE B 61  ? 0.2949 0.2642 0.3673 0.0074  -0.0382 0.0397  62  PHE B CB  
3351 C CG  . PHE B 61  ? 0.2422 0.2103 0.3211 0.0080  -0.0406 0.0356  62  PHE B CG  
3352 C CD1 . PHE B 61  ? 0.2883 0.2519 0.3784 0.0069  -0.0397 0.0350  62  PHE B CD1 
3353 C CD2 . PHE B 61  ? 0.2799 0.2511 0.3539 0.0093  -0.0434 0.0319  62  PHE B CD2 
3354 C CE1 . PHE B 61  ? 0.2704 0.2323 0.3658 0.0073  -0.0416 0.0310  62  PHE B CE1 
3355 C CE2 . PHE B 61  ? 0.2575 0.2270 0.3369 0.0099  -0.0451 0.0281  62  PHE B CE2 
3356 C CZ  . PHE B 61  ? 0.2764 0.2409 0.3661 0.0089  -0.0443 0.0277  62  PHE B CZ  
3357 N N   . GLU B 62  ? 0.2705 0.2406 0.3206 0.0096  -0.0331 0.0497  63  GLU B N   
3358 C CA  . GLU B 62  ? 0.2914 0.2627 0.3331 0.0083  -0.0309 0.0516  63  GLU B CA  
3359 C C   . GLU B 62  ? 0.2894 0.2648 0.3311 0.0057  -0.0324 0.0468  63  GLU B C   
3360 O O   . GLU B 62  ? 0.2924 0.2712 0.3333 0.0055  -0.0357 0.0416  63  GLU B O   
3361 C CB  . GLU B 62  ? 0.3242 0.2980 0.3542 0.0099  -0.0315 0.0527  63  GLU B CB  
3362 C CG  . GLU B 62  ? 0.3329 0.3020 0.3605 0.0134  -0.0303 0.0582  63  GLU B CG  
3363 C CD  . GLU B 62  ? 0.4171 0.3901 0.4342 0.0155  -0.0326 0.0582  63  GLU B CD  
3364 O OE1 . GLU B 62  ? 0.3860 0.3653 0.3983 0.0137  -0.0343 0.0539  63  GLU B OE1 
3365 O OE2 . GLU B 62  ? 0.4182 0.3879 0.4318 0.0192  -0.0326 0.0624  63  GLU B OE2 
3366 N N   . LEU B 63  ? 0.2549 0.2293 0.2969 0.0041  -0.0297 0.0485  64  LEU B N   
3367 C CA  . LEU B 63  ? 0.2626 0.2398 0.3042 0.0025  -0.0310 0.0446  64  LEU B CA  
3368 C C   . LEU B 63  ? 0.2787 0.2581 0.3074 0.0020  -0.0302 0.0433  64  LEU B C   
3369 O O   . LEU B 63  ? 0.2760 0.2571 0.3022 0.0012  -0.0314 0.0396  64  LEU B O   
3370 C CB  . LEU B 63  ? 0.2629 0.2387 0.3124 0.0015  -0.0286 0.0467  64  LEU B CB  
3371 C CG  . LEU B 63  ? 0.2647 0.2386 0.3289 0.0012  -0.0290 0.0468  64  LEU B CG  
3372 C CD1 . LEU B 63  ? 0.2598 0.2344 0.3333 0.0000  -0.0273 0.0475  64  LEU B CD1 
3373 C CD2 . LEU B 63  ? 0.2908 0.2665 0.3599 0.0013  -0.0341 0.0412  64  LEU B CD2 
3374 N N   . GLY B 64  ? 0.3521 0.2372 0.2928 -0.0383 -0.0620 0.0999  65  GLY B N   
3375 C CA  . GLY B 64  ? 0.3460 0.2305 0.2867 -0.0397 -0.0742 0.0969  65  GLY B CA  
3376 C C   . GLY B 64  ? 0.3295 0.2090 0.2673 -0.0415 -0.0600 0.0950  65  GLY B C   
3377 O O   . GLY B 64  ? 0.3842 0.2418 0.2951 -0.0462 -0.0414 0.0953  65  GLY B O   
3378 N N   . SER B 65  ? 0.2870 0.1887 0.2555 -0.0384 -0.0661 0.0913  66  SER B N   
3379 C CA  . SER B 65  ? 0.3038 0.2014 0.2730 -0.0407 -0.0536 0.0890  66  SER B CA  
3380 C C   . SER B 65  ? 0.3056 0.2214 0.2993 -0.0386 -0.0276 0.0847  66  SER B C   
3381 O O   . SER B 65  ? 0.3036 0.2197 0.2961 -0.0392 -0.0089 0.0754  66  SER B O   
3382 C CB  . SER B 65  ? 0.3026 0.2258 0.3061 -0.0360 -0.0656 0.0847  66  SER B CB  
3383 O OG  . SER B 65  ? 0.4018 0.3082 0.3805 -0.0386 -0.0844 0.0836  66  SER B OG  
3384 N N   . VAL B 66  ? 0.2610 0.1945 0.2775 -0.0349 -0.0248 0.0879  67  VAL B N   
3385 C CA  . VAL B 66  ? 0.2457 0.1947 0.2829 -0.0331 -0.0011 0.0831  67  VAL B CA  
3386 C C   . VAL B 66  ? 0.2929 0.2103 0.2903 -0.0402 0.0190  0.0831  67  VAL B C   
3387 O O   . VAL B 66  ? 0.3141 0.2401 0.3230 -0.0397 0.0413  0.0758  67  VAL B O   
3388 C CB  . VAL B 66  ? 0.2222 0.1981 0.2871 -0.0261 -0.0052 0.0815  67  VAL B CB  
3389 C CG1 . VAL B 66  ? 0.2429 0.2273 0.3156 -0.0242 0.0151  0.0750  67  VAL B CG1 
3390 C CG2 . VAL B 66  ? 0.2064 0.2188 0.3139 -0.0183 -0.0183 0.0776  67  VAL B CG2 
3391 N N   . SER B 67  ? 0.3090 0.1904 0.2564 -0.0456 0.0106  0.0867  68  SER B N   
3392 C CA  . SER B 67  ? 0.3375 0.1857 0.2399 -0.0516 0.0301  0.0828  68  SER B CA  
3393 C C   . SER B 67  ? 0.3543 0.2030 0.2581 -0.0520 0.0500  0.0713  68  SER B C   
3394 O O   . SER B 67  ? 0.3910 0.2260 0.2779 -0.0546 0.0734  0.0660  68  SER B O   
3395 C CB  . SER B 67  ? 0.3929 0.2020 0.2406 -0.0570 0.0145  0.0870  68  SER B CB  
3396 O OG  . SER B 67  ? 0.4143 0.2302 0.2682 -0.0539 -0.0051 0.0945  68  SER B OG  
3397 N N   . LYS B 68  ? 0.3707 0.2359 0.2954 -0.0490 0.0406  0.0668  69  LYS B N   
3398 C CA  . LYS B 68  ? 0.3363 0.2029 0.2642 -0.0491 0.0581  0.0559  69  LYS B CA  
3399 C C   . LYS B 68  ? 0.3252 0.2164 0.2911 -0.0461 0.0827  0.0508  69  LYS B C   
3400 O O   . LYS B 68  ? 0.3085 0.1959 0.2710 -0.0464 0.1014  0.0414  69  LYS B O   
3401 C CB  . LYS B 68  ? 0.3302 0.2138 0.2787 -0.0457 0.0416  0.0528  69  LYS B CB  
3402 C CG  . LYS B 68  ? 0.3507 0.2076 0.2605 -0.0493 0.0190  0.0561  69  LYS B CG  
3403 C CD  . LYS B 68  ? 0.3320 0.2069 0.2649 -0.0460 0.0051  0.0521  69  LYS B CD  
3404 C CE  . LYS B 68  ? 0.3757 0.2240 0.2715 -0.0499 -0.0189 0.0558  69  LYS B CE  
3405 N NZ  . LYS B 68  ? 0.3714 0.2226 0.2725 -0.0490 -0.0436 0.0671  69  LYS B NZ  
3406 N N   . LEU B 69  ? 0.2765 0.1975 0.2796 -0.0410 0.0777  0.0541  70  LEU B N   
3407 C CA  . LEU B 69  ? 0.2647 0.2127 0.2967 -0.0339 0.0875  0.0439  70  LEU B CA  
3408 C C   . LEU B 69  ? 0.2765 0.2038 0.2823 -0.0362 0.1042  0.0406  70  LEU B C   
3409 O O   . LEU B 69  ? 0.2756 0.2089 0.2923 -0.0319 0.1153  0.0310  70  LEU B O   
3410 C CB  . LEU B 69  ? 0.2152 0.1909 0.2770 -0.0272 0.0738  0.0451  70  LEU B CB  
3411 C CG  . LEU B 69  ? 0.2179 0.2132 0.3043 -0.0223 0.0558  0.0466  70  LEU B CG  
3412 C CD1 . LEU B 69  ? 0.1694 0.1816 0.2726 -0.0134 0.0447  0.0453  70  LEU B CD1 
3413 C CD2 . LEU B 69  ? 0.1998 0.2057 0.2997 -0.0175 0.0562  0.0374  70  LEU B CD2 
3414 N N   . PHE B 70  ? 0.3275 0.2277 0.2974 -0.0421 0.1034  0.0485  71  PHE B N   
3415 C CA  . PHE B 70  ? 0.3578 0.2368 0.3013 -0.0439 0.1191  0.0443  71  PHE B CA  
3416 C C   . PHE B 70  ? 0.4098 0.2597 0.3203 -0.0477 0.1331  0.0371  71  PHE B C   
3417 O O   . PHE B 70  ? 0.3940 0.2371 0.3022 -0.0462 0.1492  0.0288  71  PHE B O   
3418 C CB  . PHE B 70  ? 0.3592 0.2185 0.2735 -0.0480 0.1120  0.0538  71  PHE B CB  
3419 C CG  . PHE B 70  ? 0.3596 0.2470 0.3066 -0.0442 0.1011  0.0592  71  PHE B CG  
3420 C CD1 . PHE B 70  ? 0.3644 0.2671 0.3306 -0.0401 0.1094  0.0539  71  PHE B CD1 
3421 C CD2 . PHE B 70  ? 0.3715 0.2688 0.3301 -0.0444 0.0814  0.0685  71  PHE B CD2 
3422 C CE1 . PHE B 70  ? 0.3116 0.2372 0.3026 -0.0369 0.0989  0.0570  71  PHE B CE1 
3423 C CE2 . PHE B 70  ? 0.3825 0.3033 0.3677 -0.0411 0.0720  0.0708  71  PHE B CE2 
3424 C CZ  . PHE B 70  ? 0.3015 0.2359 0.3009 -0.0375 0.0812  0.0646  71  PHE B CZ  
3425 N N   . THR B 71  ? 0.3940 0.2246 0.2785 -0.0525 0.1255  0.0400  72  THR B N   
3426 C CA  . THR B 71  ? 0.4253 0.2288 0.2780 -0.0561 0.1378  0.0321  72  THR B CA  
3427 C C   . THR B 71  ? 0.4060 0.2348 0.2984 -0.0502 0.1505  0.0213  72  THR B C   
3428 O O   . THR B 71  ? 0.4508 0.2643 0.3316 -0.0502 0.1667  0.0126  72  THR B O   
3429 C CB  . THR B 71  ? 0.4686 0.2492 0.2889 -0.0618 0.1219  0.0373  72  THR B CB  
3430 O OG1 . THR B 71  ? 0.5080 0.2649 0.2925 -0.0657 0.1037  0.0470  72  THR B OG1 
3431 C CG2 . THR B 71  ? 0.4895 0.2402 0.2731 -0.0658 0.1336  0.0288  72  THR B CG2 
3432 N N   . ALA B 72  ? 0.3664 0.2328 0.3063 -0.0445 0.1408  0.0217  73  ALA B N   
3433 C CA  . ALA B 72  ? 0.3793 0.2694 0.3565 -0.0374 0.1457  0.0119  73  ALA B CA  
3434 C C   . ALA B 72  ? 0.3597 0.2542 0.3512 -0.0329 0.1534  0.0072  73  ALA B C   
3435 O O   . ALA B 72  ? 0.3879 0.2765 0.3841 -0.0314 0.1631  -0.0002 73  ALA B O   
3436 C CB  . ALA B 72  ? 0.2927 0.2190 0.3121 -0.0314 0.1284  0.0135  73  ALA B CB  
3437 N N   . THR B 73  ? 0.3179 0.2206 0.3156 -0.0316 0.1483  0.0123  74  THR B N   
3438 C CA  . THR B 73  ? 0.3343 0.2383 0.3428 -0.0284 0.1546  0.0089  74  THR B CA  
3439 C C   . THR B 73  ? 0.3806 0.2511 0.3567 -0.0332 0.1738  0.0050  74  THR B C   
3440 O O   . THR B 73  ? 0.4037 0.2707 0.3902 -0.0313 0.1826  -0.0007 74  THR B O   
3441 C CB  . THR B 73  ? 0.3022 0.2189 0.3191 -0.0268 0.1456  0.0153  74  THR B CB  
3442 O OG1 . THR B 73  ? 0.3017 0.2462 0.3458 -0.0222 0.1272  0.0180  74  THR B OG1 
3443 C CG2 . THR B 73  ? 0.3449 0.2624 0.3727 -0.0239 0.1510  0.0120  74  THR B CG2 
3444 N N   . ALA B 74  ? 0.4096 0.2514 0.3424 -0.0400 0.1786  0.0083  75  ALA B N   
3445 C CA  . ALA B 74  ? 0.4406 0.2450 0.3351 -0.0448 0.1954  0.0038  75  ALA B CA  
3446 C C   . ALA B 74  ? 0.4653 0.2610 0.3618 -0.0448 0.2055  -0.0044 75  ALA B C   
3447 O O   . ALA B 74  ? 0.4864 0.2662 0.3794 -0.0452 0.2197  -0.0099 75  ALA B O   
3448 C CB  . ALA B 74  ? 0.4971 0.2680 0.3377 -0.0523 0.1925  0.0095  75  ALA B CB  
3449 N N   . GLY B 75  ? 0.4539 0.2594 0.3570 -0.0446 0.1982  -0.0050 76  GLY B N   
3450 C CA  . GLY B 75  ? 0.4479 0.2463 0.3542 -0.0447 0.2066  -0.0125 76  GLY B CA  
3451 C C   . GLY B 75  ? 0.4421 0.2640 0.3936 -0.0386 0.2068  -0.0163 76  GLY B C   
3452 O O   . GLY B 75  ? 0.4619 0.2696 0.4124 -0.0397 0.2188  -0.0216 76  GLY B O   
3453 N N   . GLY B 76  ? 0.4214 0.2765 0.4096 -0.0328 0.1920  -0.0130 77  GLY B N   
3454 C CA  . GLY B 76  ? 0.3969 0.2687 0.4188 -0.0281 0.1884  -0.0152 77  GLY B CA  
3455 C C   . GLY B 76  ? 0.4676 0.3224 0.4841 -0.0293 0.2024  -0.0167 77  GLY B C   
3456 O O   . GLY B 76  ? 0.4475 0.2939 0.4795 -0.0288 0.2121  -0.0210 77  GLY B O   
3457 N N   . TYR B 77  ? 0.4041 0.2467 0.3980 -0.0317 0.2071  -0.0135 78  TYR B N   
3458 C CA  . TYR B 77  ? 0.4495 0.2741 0.4346 -0.0332 0.2208  -0.0148 78  TYR B CA  
3459 C C   . TYR B 77  ? 0.5191 0.3116 0.4808 -0.0377 0.2396  -0.0203 78  TYR B C   
3460 O O   . TYR B 77  ? 0.5468 0.3334 0.5220 -0.0372 0.2494  -0.0236 78  TYR B O   
3461 C CB  . TYR B 77  ? 0.5029 0.3183 0.4640 -0.0354 0.2210  -0.0100 78  TYR B CB  
3462 C CG  . TYR B 77  ? 0.5112 0.3089 0.4623 -0.0368 0.2339  -0.0107 78  TYR B CG  
3463 C CD1 . TYR B 77  ? 0.5191 0.3328 0.4965 -0.0329 0.2303  -0.0091 78  TYR B CD1 
3464 C CD2 . TYR B 77  ? 0.5352 0.2952 0.4473 -0.0423 0.2509  -0.0135 78  TYR B CD2 
3465 C CE1 . TYR B 77  ? 0.5817 0.3774 0.5502 -0.0342 0.2435  -0.0101 78  TYR B CE1 
3466 C CE2 . TYR B 77  ? 0.6182 0.3609 0.5208 -0.0435 0.2630  -0.0143 78  TYR B CE2 
3467 C CZ  . TYR B 77  ? 0.6040 0.3680 0.5366 -0.0393 0.2583  -0.0122 78  TYR B CZ  
3468 O OH  . TYR B 77  ? 0.6975 0.4437 0.6209 -0.0407 0.2711  -0.0131 78  TYR B OH  
3469 N N   . ALA B 78  ? 0.5201 0.2889 0.4446 -0.0426 0.2448  -0.0212 79  ALA B N   
3470 C CA  . ALA B 78  ? 0.5708 0.3049 0.4671 -0.0475 0.2620  -0.0263 79  ALA B CA  
3471 C C   . ALA B 78  ? 0.6127 0.3570 0.5372 -0.0457 0.2642  -0.0305 79  ALA B C   
3472 O O   . ALA B 78  ? 0.6221 0.3471 0.5436 -0.0477 0.2792  -0.0343 79  ALA B O   
3473 C CB  . ALA B 78  ? 0.6328 0.3392 0.4804 -0.0534 0.2624  -0.0258 79  ALA B CB  
3474 N N   . LYS B 79  ? 0.5323 0.3057 0.4834 -0.0421 0.2490  -0.0296 80  LYS B N   
3475 C CA  . LYS B 79  ? 0.5621 0.3468 0.5399 -0.0404 0.2481  -0.0328 80  LYS B CA  
3476 C C   . LYS B 79  ? 0.5675 0.3536 0.5743 -0.0383 0.2553  -0.0344 80  LYS B C   
3477 O O   . LYS B 79  ? 0.6054 0.3751 0.6159 -0.0404 0.2693  -0.0383 80  LYS B O   
3478 C CB  . LYS B 79  ? 0.5384 0.3542 0.5395 -0.0366 0.2286  -0.0310 80  LYS B CB  
3479 C CG  . LYS B 79  ? 0.5113 0.3333 0.5357 -0.0358 0.2282  -0.0346 80  LYS B CG  
3480 C CD  . LYS B 79  ? 0.5421 0.3797 0.6060 -0.0318 0.2219  -0.0345 80  LYS B CD  
3481 C CE  . LYS B 79  ? 0.5517 0.3967 0.6373 -0.0313 0.2178  -0.0373 80  LYS B CE  
3482 N NZ  . LYS B 79  ? 0.5971 0.4508 0.7160 -0.0284 0.2127  -0.0371 80  LYS B NZ  
3483 N N   . ASN B 80  ? 0.5417 0.3425 0.5682 -0.0347 0.2481  -0.0316 81  ASN B N   
3484 C CA  . ASN B 80  ? 0.5779 0.3783 0.6337 -0.0328 0.2542  -0.0330 81  ASN B CA  
3485 C C   . ASN B 80  ? 0.6001 0.3760 0.6427 -0.0353 0.2728  -0.0345 81  ASN B C   
3486 O O   . ASN B 80  ? 0.7079 0.4809 0.7738 -0.0341 0.2799  -0.0357 81  ASN B O   
3487 C CB  . ASN B 80  ? 0.5891 0.4129 0.6700 -0.0280 0.2384  -0.0294 81  ASN B CB  
3488 C CG  . ASN B 80  ? 0.5925 0.4357 0.6953 -0.0253 0.2231  -0.0293 81  ASN B CG  
3489 O OD1 . ASN B 80  ? 0.6500 0.4919 0.7738 -0.0252 0.2253  -0.0319 81  ASN B OD1 
3490 N ND2 . ASN B 80  ? 0.5193 0.3793 0.6167 -0.0236 0.2078  -0.0260 81  ASN B ND2 
3491 N N   . LYS B 81  ? 0.5874 0.3441 0.5925 -0.0390 0.2807  -0.0342 82  LYS B N   
3492 C CA  . LYS B 81  ? 0.6468 0.3739 0.6340 -0.0424 0.3007  -0.0366 82  LYS B CA  
3493 C C   . LYS B 81  ? 0.6719 0.3736 0.6372 -0.0469 0.3145  -0.0405 82  LYS B C   
3494 O O   . LYS B 81  ? 0.7169 0.3891 0.6587 -0.0505 0.3315  -0.0425 82  LYS B O   
3495 C CB  . LYS B 81  ? 0.6457 0.3632 0.6024 -0.0439 0.3009  -0.0334 82  LYS B CB  
3496 C CG  . LYS B 81  ? 0.6865 0.4239 0.6641 -0.0399 0.2916  -0.0298 82  LYS B CG  
3497 C CD  . LYS B 81  ? 0.7252 0.4495 0.6718 -0.0421 0.2943  -0.0268 82  LYS B CD  
3498 C CE  . LYS B 81  ? 0.7877 0.4826 0.7227 -0.0447 0.3151  -0.0298 82  LYS B CE  
3499 N NZ  . LYS B 81  ? 0.7934 0.4975 0.7637 -0.0411 0.3190  -0.0302 82  LYS B NZ  
3500 N N   . GLY B 82  ? 0.6521 0.3633 0.6238 -0.0469 0.3077  -0.0417 83  GLY B N   
3501 C CA  . GLY B 82  ? 0.6678 0.3561 0.6205 -0.0512 0.3202  -0.0453 83  GLY B CA  
3502 C C   . GLY B 82  ? 0.6733 0.3302 0.5745 -0.0565 0.3273  -0.0459 83  GLY B C   
3503 O O   . GLY B 82  ? 0.7282 0.3562 0.6070 -0.0610 0.3415  -0.0493 83  GLY B O   
3504 N N   . LYS B 83  ? 0.6287 0.2844 0.5075 -0.0568 0.3194  -0.0428 84  LYS B N   
3505 C CA  . LYS B 83  ? 0.7097 0.3287 0.5335 -0.0628 0.3252  -0.0433 84  LYS B CA  
3506 C C   . LYS B 83  ? 0.7496 0.3681 0.5604 -0.0648 0.3179  -0.0442 84  LYS B C   
3507 O O   . LYS B 83  ? 0.7883 0.3704 0.5537 -0.0707 0.3254  -0.0460 84  LYS B O   
3508 C CB  . LYS B 83  ? 0.7377 0.3558 0.5407 -0.0629 0.3169  -0.0390 84  LYS B CB  
3509 C CG  . LYS B 83  ? 0.7428 0.3566 0.5519 -0.0618 0.3251  -0.0381 84  LYS B CG  
3510 C CD  . LYS B 83  ? 0.8649 0.4395 0.6510 -0.0661 0.3473  -0.0424 84  LYS B CD  
3511 C CE  . LYS B 83  ? 0.9373 0.5055 0.7265 -0.0653 0.3559  -0.0415 84  LYS B CE  
3512 N NZ  . LYS B 83  ? 0.9555 0.4891 0.7312 -0.0687 0.3785  -0.0458 84  LYS B NZ  
3513 N N   . ILE B 84  ? 0.6781 0.3349 0.5263 -0.0600 0.3028  -0.0430 85  ILE B N   
3514 C CA  . ILE B 84  ? 0.6441 0.3047 0.4871 -0.0612 0.2958  -0.0442 85  ILE B CA  
3515 C C   . ILE B 84  ? 0.6077 0.3041 0.5021 -0.0561 0.2882  -0.0451 85  ILE B C   
3516 O O   . ILE B 84  ? 0.5938 0.3154 0.5260 -0.0513 0.2829  -0.0436 85  ILE B O   
3517 C CB  . ILE B 84  ? 0.6602 0.3284 0.4850 -0.0614 0.2798  -0.0406 85  ILE B CB  
3518 C CG1 . ILE B 84  ? 0.6603 0.3663 0.5211 -0.0554 0.2656  -0.0362 85  ILE B CG1 
3519 C CG2 . ILE B 84  ? 0.7450 0.3707 0.5081 -0.0681 0.2840  -0.0397 85  ILE B CG2 
3520 C CD1 . ILE B 84  ? 0.6285 0.3504 0.4847 -0.0546 0.2489  -0.0323 85  ILE B CD1 
3521 N N   . SER B 85  ? 0.5933 0.2900 0.4857 -0.0576 0.2863  -0.0472 86  SER B N   
3522 C CA  . SER B 85  ? 0.6097 0.3415 0.5445 -0.0530 0.2737  -0.0473 86  SER B CA  
3523 C C   . SER B 85  ? 0.5422 0.2864 0.4693 -0.0526 0.2595  -0.0461 86  SER B C   
3524 O O   . SER B 85  ? 0.5826 0.3002 0.4674 -0.0576 0.2637  -0.0469 86  SER B O   
3525 C CB  . SER B 85  ? 0.6552 0.3788 0.5987 -0.0548 0.2839  -0.0510 86  SER B CB  
3526 O OG  . SER B 85  ? 0.6274 0.3801 0.6008 -0.0514 0.2700  -0.0511 86  SER B OG  
3527 N N   . PHE B 86  ? 0.5270 0.3086 0.4916 -0.0470 0.2419  -0.0441 87  PHE B N   
3528 C CA  . PHE B 86  ? 0.5379 0.3331 0.4996 -0.0463 0.2287  -0.0430 87  PHE B CA  
3529 C C   . PHE B 86  ? 0.5254 0.3117 0.4767 -0.0492 0.2318  -0.0467 87  PHE B C   
3530 O O   . PHE B 86  ? 0.4798 0.2682 0.4180 -0.0502 0.2242  -0.0467 87  PHE B O   
3531 C CB  . PHE B 86  ? 0.4736 0.3093 0.4776 -0.0394 0.2086  -0.0398 87  PHE B CB  
3532 C CG  . PHE B 86  ? 0.4801 0.3253 0.4881 -0.0367 0.2022  -0.0353 87  PHE B CG  
3533 C CD1 . PHE B 86  ? 0.5201 0.3414 0.4928 -0.0407 0.2114  -0.0339 87  PHE B CD1 
3534 C CD2 . PHE B 86  ? 0.4641 0.3393 0.5061 -0.0308 0.1859  -0.0320 87  PHE B CD2 
3535 C CE1 . PHE B 86  ? 0.5239 0.3551 0.5011 -0.0385 0.2054  -0.0292 87  PHE B CE1 
3536 C CE2 . PHE B 86  ? 0.4673 0.3512 0.5125 -0.0285 0.1798  -0.0276 87  PHE B CE2 
3537 C CZ  . PHE B 86  ? 0.4442 0.3080 0.4599 -0.0322 0.1901  -0.0262 87  PHE B CZ  
3538 N N   . ASP B 87  ? 0.5615 0.3372 0.5174 -0.0509 0.2430  -0.0497 88  ASP B N   
3539 C CA  . ASP B 87  ? 0.5669 0.3309 0.5094 -0.0542 0.2478  -0.0531 88  ASP B CA  
3540 C C   . ASP B 87  ? 0.6072 0.3260 0.4949 -0.0615 0.2633  -0.0549 88  ASP B C   
3541 O O   . ASP B 87  ? 0.6155 0.3197 0.4834 -0.0649 0.2669  -0.0573 88  ASP B O   
3542 C CB  . ASP B 87  ? 0.5869 0.3616 0.5610 -0.0525 0.2511  -0.0549 88  ASP B CB  
3543 C CG  . ASP B 87  ? 0.6439 0.4583 0.6623 -0.0462 0.2315  -0.0530 88  ASP B CG  
3544 O OD1 . ASP B 87  ? 0.6373 0.4708 0.6614 -0.0437 0.2163  -0.0517 88  ASP B OD1 
3545 O OD2 . ASP B 87  ? 0.7194 0.5350 0.7652 -0.0459 0.2365  -0.0542 88  ASP B OD2 
3546 N N   . ASP B 88  ? 0.6204 0.3151 0.4803 -0.0640 0.2711  -0.0534 89  ASP B N   
3547 C CA  . ASP B 88  ? 0.6707 0.3182 0.4714 -0.0712 0.2821  -0.0543 89  ASP B CA  
3548 C C   . ASP B 88  ? 0.6513 0.2882 0.4147 -0.0741 0.2696  -0.0531 89  ASP B C   
3549 O O   . ASP B 88  ? 0.6427 0.3082 0.4253 -0.0704 0.2544  -0.0511 89  ASP B O   
3550 C CB  . ASP B 88  ? 0.6749 0.3005 0.4551 -0.0729 0.2905  -0.0527 89  ASP B CB  
3551 C CG  . ASP B 88  ? 0.6720 0.2984 0.4791 -0.0713 0.3049  -0.0543 89  ASP B CG  
3552 O OD1 . ASP B 88  ? 0.7541 0.3821 0.5786 -0.0715 0.3125  -0.0570 89  ASP B OD1 
3553 O OD2 . ASP B 88  ? 0.7619 0.3867 0.5721 -0.0701 0.3083  -0.0528 89  ASP B OD2 
3554 N N   . THR B 89  ? 0.7223 0.3155 0.4300 -0.0809 0.2749  -0.0539 90  THR B N   
3555 C CA  . THR B 89  ? 0.7296 0.3027 0.3902 -0.0849 0.2606  -0.0521 90  THR B CA  
3556 C C   . THR B 89  ? 0.7843 0.3166 0.3907 -0.0903 0.2596  -0.0491 90  THR B C   
3557 O O   . THR B 89  ? 0.8098 0.3237 0.4098 -0.0917 0.2742  -0.0497 90  THR B O   
3558 C CB  . THR B 89  ? 0.7747 0.3295 0.4116 -0.0886 0.2611  -0.0550 90  THR B CB  
3559 O OG1 . THR B 89  ? 0.8450 0.3604 0.4514 -0.0938 0.2782  -0.0566 90  THR B OG1 
3560 C CG2 . THR B 89  ? 0.7035 0.2999 0.3953 -0.0830 0.2608  -0.0579 90  THR B CG2 
3561 N N   . PRO B 90  ? 0.8004 0.3181 0.3676 -0.0933 0.2406  -0.0454 91  PRO B N   
3562 C CA  . PRO B 90  ? 0.8528 0.3369 0.3742 -0.0978 0.2353  -0.0414 91  PRO B CA  
3563 C C   . PRO B 90  ? 0.9332 0.3655 0.4045 -0.1047 0.2461  -0.0430 91  PRO B C   
3564 O O   . PRO B 90  ? 0.9626 0.3707 0.4094 -0.1072 0.2503  -0.0414 91  PRO B O   
3565 C CB  . PRO B 90  ? 0.8402 0.3217 0.3341 -0.0997 0.2076  -0.0363 91  PRO B CB  
3566 C CG  . PRO B 90  ? 0.8230 0.3192 0.3291 -0.0985 0.2013  -0.0394 91  PRO B CG  
3567 C CD  . PRO B 90  ? 0.7850 0.3200 0.3531 -0.0921 0.2203  -0.0442 91  PRO B CD  
3568 N N   . GLY B 91  ? 0.9279 0.3419 0.3827 -0.1079 0.2507  -0.0459 92  GLY B N   
3569 C CA  . GLY B 91  ? 1.0290 0.3918 0.4353 -0.1148 0.2617  -0.0472 92  GLY B CA  
3570 C C   . GLY B 91  ? 1.0624 0.4180 0.4846 -0.1142 0.2876  -0.0502 92  GLY B C   
3571 O O   . GLY B 91  ? 1.1050 0.4154 0.4850 -0.1200 0.2979  -0.0510 92  GLY B O   
3572 N N   . LYS B 92  ? 0.9569 0.3549 0.4393 -0.1075 0.2973  -0.0518 93  LYS B N   
3573 C CA  . LYS B 92  ? 1.0061 0.3995 0.5073 -0.1065 0.3189  -0.0541 93  LYS B CA  
3574 C C   . LYS B 92  ? 1.0044 0.3792 0.4823 -0.1078 0.3191  -0.0519 93  LYS B C   
3575 O O   . LYS B 92  ? 1.0255 0.3777 0.4961 -0.1095 0.3371  -0.0538 93  LYS B O   
3576 C CB  . LYS B 92  ? 0.9185 0.3635 0.4914 -0.0988 0.3238  -0.0557 93  LYS B CB  
3577 C CG  . LYS B 92  ? 0.9379 0.3843 0.5386 -0.0969 0.3429  -0.0576 93  LYS B CG  
3578 C CD  . LYS B 92  ? 0.8844 0.3791 0.5529 -0.0901 0.3429  -0.0588 93  LYS B CD  
3579 C CE  . LYS B 92  ? 0.9313 0.4309 0.6308 -0.0876 0.3577  -0.0599 93  LYS B CE  
3580 N NZ  . LYS B 92  ? 0.9572 0.5020 0.7195 -0.0813 0.3531  -0.0603 93  LYS B NZ  
3581 N N   . TYR B 93  ? 0.9753 0.3573 0.4396 -0.1073 0.2994  -0.0478 94  TYR B N   
3582 C CA  . TYR B 93  ? 0.9700 0.3378 0.4137 -0.1083 0.2971  -0.0450 94  TYR B CA  
3583 C C   . TYR B 93  ? 1.0714 0.3969 0.4498 -0.1151 0.2807  -0.0417 94  TYR B C   
3584 O O   . TYR B 93  ? 1.0872 0.3779 0.4301 -0.1191 0.2859  -0.0413 94  TYR B O   
3585 C CB  . TYR B 93  ? 0.9308 0.3473 0.4214 -0.1012 0.2874  -0.0419 94  TYR B CB  
3586 C CG  . TYR B 93  ? 0.8773 0.3344 0.4330 -0.0945 0.3002  -0.0447 94  TYR B CG  
3587 C CD1 . TYR B 93  ? 0.8891 0.3468 0.4650 -0.0925 0.3163  -0.0463 94  TYR B CD1 
3588 C CD2 . TYR B 93  ? 0.8610 0.3540 0.4574 -0.0904 0.2949  -0.0459 94  TYR B CD2 
3589 C CE1 . TYR B 93  ? 0.8880 0.3805 0.5222 -0.0868 0.3246  -0.0483 94  TYR B CE1 
3590 C CE2 . TYR B 93  ? 0.8134 0.3420 0.4688 -0.0845 0.3032  -0.0481 94  TYR B CE2 
3591 C CZ  . TYR B 93  ? 0.8779 0.4053 0.5512 -0.0829 0.3171  -0.0490 94  TYR B CZ  
3592 O OH  . TYR B 93  ? 0.8319 0.3919 0.5613 -0.0775 0.3221  -0.0506 94  TYR B OH  
3593 N N   . TRP B 94  ? 1.0541 0.3808 0.4159 -0.1168 0.2597  -0.0392 95  TRP B N   
3594 C CA  . TRP B 94  ? 1.1170 0.4028 0.4183 -0.1236 0.2400  -0.0356 95  TRP B CA  
3595 C C   . TRP B 94  ? 1.1695 0.4204 0.4381 -0.1291 0.2449  -0.0385 95  TRP B C   
3596 O O   . TRP B 94  ? 1.1436 0.4105 0.4249 -0.1280 0.2379  -0.0391 95  TRP B O   
3597 C CB  . TRP B 94  ? 1.0440 0.3535 0.3498 -0.1220 0.2104  -0.0299 95  TRP B CB  
3598 C CG  . TRP B 94  ? 1.1128 0.3862 0.3654 -0.1281 0.1858  -0.0247 95  TRP B CG  
3599 C CD1 . TRP B 94  ? 1.1440 0.3661 0.3445 -0.1350 0.1878  -0.0252 95  TRP B CD1 
3600 C CD2 . TRP B 94  ? 1.1059 0.3920 0.3550 -0.1281 0.1539  -0.0180 95  TRP B CD2 
3601 N NE1 . TRP B 94  ? 1.2178 0.4210 0.3843 -0.1391 0.1585  -0.0194 95  TRP B NE1 
3602 C CE2 . TRP B 94  ? 1.1736 0.4163 0.3707 -0.1348 0.1367  -0.0146 95  TRP B CE2 
3603 C CE3 . TRP B 94  ? 1.0445 0.3745 0.3313 -0.1230 0.1376  -0.0140 95  TRP B CE3 
3604 C CZ2 . TRP B 94  ? 1.2154 0.4594 0.4016 -0.1364 0.1029  -0.0075 95  TRP B CZ2 
3605 C CZ3 . TRP B 94  ? 1.0979 0.4278 0.3718 -0.1245 0.1045  -0.0065 95  TRP B CZ3 
3606 C CH2 . TRP B 94  ? 1.1666 0.4552 0.3931 -0.1310 0.0870  -0.0033 95  TRP B CH2 
3607 N N   . LYS B 95  ? 1.1918 0.3945 0.4178 -0.1350 0.2571  -0.0402 96  LYS B N   
3608 C CA  . LYS B 95  ? 1.2090 0.3802 0.4115 -0.1397 0.2697  -0.0435 96  LYS B CA  
3609 C C   . LYS B 95  ? 1.2346 0.3845 0.3989 -0.1445 0.2467  -0.0408 96  LYS B C   
3610 O O   . LYS B 95  ? 1.2630 0.4071 0.4253 -0.1459 0.2525  -0.0429 96  LYS B O   
3611 C CB  . LYS B 95  ? 1.3253 0.4481 0.4907 -0.1450 0.2892  -0.0457 96  LYS B CB  
3612 C CG  . LYS B 95  ? 1.4067 0.5312 0.5986 -0.1436 0.3197  -0.0507 96  LYS B CG  
3613 C CD  . LYS B 95  ? 1.3070 0.4880 0.5692 -0.1349 0.3289  -0.0522 96  LYS B CD  
3614 C CE  . LYS B 95  ? 1.3182 0.5059 0.5906 -0.1323 0.3327  -0.0513 96  LYS B CE  
3615 N NZ  . LYS B 95  ? 1.3327 0.5750 0.6741 -0.1239 0.3397  -0.0522 96  LYS B NZ  
3616 N N   . GLU B 96  ? 1.2554 0.3949 0.3920 -0.1469 0.2195  -0.0358 97  GLU B N   
3617 C CA  . GLU B 96  ? 1.2735 0.3918 0.3752 -0.1516 0.1943  -0.0325 97  GLU B CA  
3618 C C   . GLU B 96  ? 1.2392 0.3996 0.3780 -0.1467 0.1831  -0.0323 97  GLU B C   
3619 O O   . GLU B 96  ? 1.2579 0.4076 0.3762 -0.1495 0.1619  -0.0297 97  GLU B O   
3620 C CB  . GLU B 96  ? 1.3395 0.4405 0.4103 -0.1549 0.1660  -0.0267 97  GLU B CB  
3621 C CG  . GLU B 96  ? 1.3951 0.4378 0.4089 -0.1627 0.1686  -0.0265 97  GLU B CG  
3622 C CD  . GLU B 96  ? 1.3753 0.4153 0.3924 -0.1614 0.1847  -0.0278 97  GLU B CD  
3623 O OE1 . GLU B 96  ? 1.3739 0.4580 0.4390 -0.1543 0.1945  -0.0286 97  GLU B OE1 
3624 O OE2 . GLU B 96  ? 1.4354 0.4288 0.4069 -0.1674 0.1872  -0.0278 97  GLU B OE2 
3625 N N   . LEU B 97  ? 1.2052 0.4138 0.3999 -0.1393 0.1964  -0.0348 98  LEU B N   
3626 C CA  . LEU B 97  ? 1.1532 0.4042 0.3875 -0.1341 0.1888  -0.0356 98  LEU B CA  
3627 C C   . LEU B 97  ? 1.1623 0.4239 0.4212 -0.1322 0.2126  -0.0413 98  LEU B C   
3628 O O   . LEU B 97  ? 1.0603 0.3564 0.3525 -0.1279 0.2080  -0.0429 98  LEU B O   
3629 C CB  . LEU B 97  ? 1.0703 0.3710 0.3535 -0.1269 0.1843  -0.0341 98  LEU B CB  
3630 C CG  . LEU B 97  ? 1.0350 0.3370 0.3050 -0.1274 0.1573  -0.0275 98  LEU B CG  
3631 C CD1 . LEU B 97  ? 1.0069 0.3620 0.3298 -0.1200 0.1542  -0.0261 98  LEU B CD1 
3632 C CD2 . LEU B 97  ? 1.0598 0.3420 0.2963 -0.1318 0.1262  -0.0231 98  LEU B CD2 
3633 N N   . LYS B 98  ? 1.1926 0.4254 0.4372 -0.1354 0.2372  -0.0444 99  LYS B N   
3634 C CA  . LYS B 98  ? 1.2673 0.5079 0.5350 -0.1342 0.2587  -0.0492 99  LYS B CA  
3635 C C   . LYS B 98  ? 1.2220 0.4501 0.4665 -0.1371 0.2465  -0.0492 99  LYS B C   
3636 O O   . LYS B 98  ? 1.2960 0.4869 0.4896 -0.1430 0.2290  -0.0459 99  LYS B O   
3637 C CB  . LYS B 98  ? 1.2954 0.4998 0.5446 -0.1381 0.2851  -0.0518 99  LYS B CB  
3638 C CG  . LYS B 98  ? 1.2752 0.5050 0.5742 -0.1339 0.3111  -0.0563 99  LYS B CG  
3639 C CD  . LYS B 98  ? 1.2555 0.5358 0.6148 -0.1261 0.3134  -0.0566 99  LYS B CD  
3640 C CE  . LYS B 98  ? 1.2526 0.5372 0.6441 -0.1242 0.3399  -0.0598 99  LYS B CE  
3641 N NZ  . LYS B 98  ? 1.3267 0.5679 0.6798 -0.1289 0.3514  -0.0596 99  LYS B NZ  
3642 N N   . ASN B 99  ? 1.2981 0.5591 0.5825 -0.1327 0.2541  -0.0527 100 ASN B N   
3643 C CA  . ASN B 99  ? 1.3217 0.5753 0.5907 -0.1345 0.2457  -0.0537 100 ASN B CA  
3644 C C   . ASN B 99  ? 1.2855 0.5432 0.5370 -0.1347 0.2124  -0.0499 100 ASN B C   
3645 O O   . ASN B 99  ? 1.2836 0.5164 0.5007 -0.1388 0.1996  -0.0489 100 ASN B O   
3646 C CB  . ASN B 99  ? 1.4602 0.6591 0.6789 -0.1423 0.2584  -0.0543 100 ASN B CB  
3647 C CG  . ASN B 99  ? 1.4756 0.6761 0.7190 -0.1415 0.2898  -0.0588 100 ASN B CG  
3648 O OD1 . ASN B 99  ? 1.4602 0.6951 0.7535 -0.1361 0.3032  -0.0607 100 ASN B OD1 
3649 N ND2 . ASN B 99  ? 1.5322 0.6951 0.7422 -0.1470 0.3007  -0.0601 100 ASN B ND2 
3650 N N   . THR B 100 ? 1.1299 0.4189 0.4061 -0.1303 0.1973  -0.0476 101 THR B N   
3651 C CA  . THR B 100 ? 1.1143 0.4153 0.3859 -0.1292 0.1650  -0.0441 101 THR B CA  
3652 C C   . THR B 100 ? 1.0123 0.3703 0.3425 -0.1208 0.1620  -0.0473 101 THR B C   
3653 O O   . THR B 100 ? 0.9465 0.3346 0.3207 -0.1159 0.1831  -0.0509 101 THR B O   
3654 C CB  . THR B 100 ? 1.1287 0.4148 0.3765 -0.1318 0.1456  -0.0378 101 THR B CB  
3655 O OG1 . THR B 100 ? 1.0599 0.3776 0.3453 -0.1267 0.1557  -0.0383 101 THR B OG1 
3656 C CG2 . THR B 100 ? 1.1863 0.4155 0.3779 -0.1399 0.1497  -0.0355 101 THR B CG2 
3657 N N   . PRO B 101 ? 0.9820 0.3562 0.3173 -0.1189 0.1354  -0.0462 102 PRO B N   
3658 C CA  . PRO B 101 ? 0.9371 0.3641 0.3286 -0.1108 0.1322  -0.0503 102 PRO B CA  
3659 C C   . PRO B 101 ? 0.8718 0.3294 0.2983 -0.1062 0.1356  -0.0495 102 PRO B C   
3660 O O   . PRO B 101 ? 0.8098 0.3083 0.2886 -0.0996 0.1475  -0.0543 102 PRO B O   
3661 C CB  . PRO B 101 ? 0.9018 0.3317 0.2845 -0.1109 0.0986  -0.0481 102 PRO B CB  
3662 C CG  . PRO B 101 ? 0.9442 0.3267 0.2739 -0.1183 0.0941  -0.0453 102 PRO B CG  
3663 C CD  . PRO B 101 ? 1.0350 0.3798 0.3293 -0.1239 0.1098  -0.0423 102 PRO B CD  
3664 N N   . ILE B 102 ? 0.8911 0.3306 0.2925 -0.1093 0.1254  -0.0434 103 ILE B N   
3665 C CA  . ILE B 102 ? 0.8388 0.3071 0.2727 -0.1050 0.1292  -0.0423 103 ILE B CA  
3666 C C   . ILE B 102 ? 0.8055 0.2867 0.2704 -0.1023 0.1629  -0.0459 103 ILE B C   
3667 O O   . ILE B 102 ? 0.8035 0.3207 0.3132 -0.0967 0.1705  -0.0466 103 ILE B O   
3668 C CB  . ILE B 102 ? 0.9004 0.3458 0.3002 -0.1091 0.1104  -0.0340 103 ILE B CB  
3669 C CG1 . ILE B 102 ? 0.8385 0.3190 0.2732 -0.1042 0.1069  -0.0315 103 ILE B CG1 
3670 C CG2 . ILE B 102 ? 0.9270 0.3318 0.2903 -0.1146 0.1273  -0.0325 103 ILE B CG2 
3671 C CD1 . ILE B 102 ? 0.8088 0.3314 0.2880 -0.0983 0.0849  -0.0316 103 ILE B CD1 
3672 N N   . ASP B 103 ? 0.8554 0.3083 0.3006 -0.1061 0.1821  -0.0478 104 ASP B N   
3673 C CA  . ASP B 103 ? 0.8329 0.2967 0.3109 -0.1038 0.2112  -0.0511 104 ASP B CA  
3674 C C   . ASP B 103 ? 0.8254 0.3319 0.3608 -0.0976 0.2208  -0.0560 104 ASP B C   
3675 O O   . ASP B 103 ? 0.8132 0.3310 0.3811 -0.0956 0.2415  -0.0581 104 ASP B O   
3676 C CB  . ASP B 103 ? 0.9214 0.3376 0.3573 -0.1105 0.2265  -0.0516 104 ASP B CB  
3677 C CG  . ASP B 103 ? 0.9637 0.3778 0.4182 -0.1099 0.2510  -0.0529 104 ASP B CG  
3678 O OD1 . ASP B 103 ? 0.9103 0.3516 0.3983 -0.1054 0.2526  -0.0518 104 ASP B OD1 
3679 O OD2 . ASP B 103 ? 1.0170 0.4009 0.4520 -0.1139 0.2683  -0.0549 104 ASP B OD2 
3680 N N   . GLN B 104 ? 0.7493 0.2795 0.2995 -0.0943 0.2043  -0.0578 105 GLN B N   
3681 C CA  . GLN B 104 ? 0.7625 0.3381 0.3724 -0.0874 0.2097  -0.0622 105 GLN B CA  
3682 C C   . GLN B 104 ? 0.6410 0.2606 0.3007 -0.0807 0.2037  -0.0616 105 GLN B C   
3683 O O   . GLN B 104 ? 0.6473 0.3072 0.3617 -0.0747 0.2061  -0.0642 105 GLN B O   
3684 C CB  . GLN B 104 ? 0.7415 0.3196 0.3441 -0.0869 0.1954  -0.0655 105 GLN B CB  
3685 C CG  . GLN B 104 ? 0.8615 0.4004 0.4211 -0.0929 0.2018  -0.0662 105 GLN B CG  
3686 C CD  . GLN B 104 ? 0.8849 0.4232 0.4652 -0.0932 0.2288  -0.0681 105 GLN B CD  
3687 O OE1 . GLN B 104 ? 0.9164 0.4881 0.5447 -0.0884 0.2357  -0.0712 105 GLN B OE1 
3688 N NE2 . GLN B 104 ? 0.8898 0.3894 0.4352 -0.0990 0.2425  -0.0660 105 GLN B NE2 
3689 N N   . VAL B 105 ? 0.6519 0.2642 0.2941 -0.0818 0.1946  -0.0576 106 VAL B N   
3690 C CA  . VAL B 105 ? 0.5938 0.2442 0.2789 -0.0760 0.1893  -0.0563 106 VAL B CA  
3691 C C   . VAL B 105 ? 0.6315 0.2885 0.3396 -0.0750 0.2065  -0.0532 106 VAL B C   
3692 O O   . VAL B 105 ? 0.6872 0.3089 0.3570 -0.0801 0.2141  -0.0510 106 VAL B O   
3693 C CB  . VAL B 105 ? 0.6237 0.2620 0.2760 -0.0779 0.1638  -0.0529 106 VAL B CB  
3694 C CG1 . VAL B 105 ? 0.5465 0.2337 0.2592 -0.0711 0.1515  -0.0467 106 VAL B CG1 
3695 C CG2 . VAL B 105 ? 0.6340 0.2641 0.2685 -0.0793 0.1384  -0.0539 106 VAL B CG2 
3696 N N   . ASN B 106 ? 0.5702 0.2710 0.3415 -0.0683 0.2100  -0.0533 107 ASN B N   
3697 C CA  . ASN B 106 ? 0.5510 0.2568 0.3445 -0.0669 0.2216  -0.0511 107 ASN B CA  
3698 C C   . ASN B 106 ? 0.5537 0.2698 0.3503 -0.0652 0.2138  -0.0460 107 ASN B C   
3699 O O   . ASN B 106 ? 0.5299 0.2527 0.3167 -0.0653 0.2002  -0.0434 107 ASN B O   
3700 C CB  . ASN B 106 ? 0.5084 0.2489 0.3628 -0.0612 0.2257  -0.0529 107 ASN B CB  
3701 C CG  . ASN B 106 ? 0.4855 0.2733 0.3931 -0.0540 0.2100  -0.0516 107 ASN B CG  
3702 O OD1 . ASN B 106 ? 0.4740 0.2756 0.3879 -0.0518 0.2004  -0.0483 107 ASN B OD1 
3703 N ND2 . ASN B 106 ? 0.4869 0.2980 0.4318 -0.0506 0.2063  -0.0535 107 ASN B ND2 
3704 N N   . LEU B 107 ? 0.5362 0.2519 0.3446 -0.0640 0.2225  -0.0443 108 LEU B N   
3705 C CA  . LEU B 107 ? 0.5261 0.2467 0.3314 -0.0632 0.2162  -0.0387 108 LEU B CA  
3706 C C   . LEU B 107 ? 0.4737 0.2408 0.3298 -0.0566 0.2028  -0.0358 108 LEU B C   
3707 O O   . LEU B 107 ? 0.4785 0.2501 0.3254 -0.0577 0.1924  -0.0294 108 LEU B O   
3708 C CB  . LEU B 107 ? 0.5723 0.2845 0.3825 -0.0625 0.2282  -0.0385 108 LEU B CB  
3709 C CG  . LEU B 107 ? 0.5979 0.2629 0.3598 -0.0690 0.2426  -0.0411 108 LEU B CG  
3710 C CD1 . LEU B 107 ? 0.5856 0.2438 0.3529 -0.0682 0.2536  -0.0405 108 LEU B CD1 
3711 C CD2 . LEU B 107 ? 0.6870 0.3127 0.3832 -0.0762 0.2347  -0.0387 108 LEU B CD2 
3712 N N   . LEU B 108 ? 0.4372 0.2377 0.3460 -0.0504 0.2001  -0.0387 109 LEU B N   
3713 C CA  . LEU B 108 ? 0.4207 0.2631 0.3762 -0.0438 0.1838  -0.0358 109 LEU B CA  
3714 C C   . LEU B 108 ? 0.3876 0.2347 0.3331 -0.0457 0.1747  -0.0349 109 LEU B C   
3715 O O   . LEU B 108 ? 0.3895 0.2565 0.3510 -0.0444 0.1631  -0.0289 109 LEU B O   
3716 C CB  . LEU B 108 ? 0.3992 0.2683 0.4007 -0.0378 0.1775  -0.0380 109 LEU B CB  
3717 C CG  . LEU B 108 ? 0.3542 0.2611 0.3967 -0.0306 0.1563  -0.0344 109 LEU B CG  
3718 C CD1 . LEU B 108 ? 0.3508 0.2663 0.4010 -0.0278 0.1510  -0.0292 109 LEU B CD1 
3719 C CD2 . LEU B 108 ? 0.4255 0.3473 0.4946 -0.0270 0.1480  -0.0356 109 LEU B CD2 
3720 N N   . GLN B 109 ? 0.4189 0.2463 0.3367 -0.0496 0.1790  -0.0400 110 GLN B N   
3721 C CA  . GLN B 109 ? 0.3997 0.2291 0.3064 -0.0503 0.1597  -0.0390 110 GLN B CA  
3722 C C   . GLN B 109 ? 0.4182 0.2254 0.2861 -0.0542 0.1379  -0.0300 110 GLN B C   
3723 O O   . GLN B 109 ? 0.4085 0.2336 0.2923 -0.0517 0.1113  -0.0242 110 GLN B O   
3724 C CB  . GLN B 109 ? 0.4110 0.2205 0.2933 -0.0524 0.1642  -0.0471 110 GLN B CB  
3725 C CG  . GLN B 109 ? 0.4115 0.2516 0.3448 -0.0473 0.1721  -0.0520 110 GLN B CG  
3726 C CD  . GLN B 109 ? 0.4388 0.2600 0.3526 -0.0502 0.1787  -0.0570 110 GLN B CD  
3727 O OE1 . GLN B 109 ? 0.4776 0.2583 0.3394 -0.0563 0.1874  -0.0582 110 GLN B OE1 
3728 N NE2 . GLN B 109 ? 0.4414 0.2913 0.3963 -0.0460 0.1727  -0.0587 110 GLN B NE2 
3729 N N   . LEU B 110 ? 0.4709 0.2388 0.2885 -0.0605 0.1490  -0.0285 111 LEU B N   
3730 C CA  . LEU B 110 ? 0.4624 0.2094 0.2449 -0.0642 0.1289  -0.0193 111 LEU B CA  
3731 C C   . LEU B 110 ? 0.4523 0.2312 0.2745 -0.0599 0.1201  -0.0115 111 LEU B C   
3732 O O   . LEU B 110 ? 0.4595 0.2459 0.2847 -0.0590 0.0934  -0.0038 111 LEU B O   
3733 C CB  . LEU B 110 ? 0.5183 0.2162 0.2396 -0.0718 0.1454  -0.0196 111 LEU B CB  
3734 C CG  . LEU B 110 ? 0.5719 0.2283 0.2400 -0.0775 0.1500  -0.0257 111 LEU B CG  
3735 C CD1 . LEU B 110 ? 0.6344 0.2429 0.2452 -0.0847 0.1709  -0.0261 111 LEU B CD1 
3736 C CD2 . LEU B 110 ? 0.6026 0.2470 0.2457 -0.0797 0.1167  -0.0215 111 LEU B CD2 
3737 N N   . ALA B 111 ? 0.4291 0.2266 0.2831 -0.0573 0.1425  -0.0132 112 ALA B N   
3738 C CA  . ALA B 111 ? 0.3624 0.1864 0.2502 -0.0539 0.1364  -0.0058 112 ALA B CA  
3739 C C   . ALA B 111 ? 0.3276 0.1937 0.2670 -0.0473 0.1158  -0.0035 112 ALA B C   
3740 O O   . ALA B 111 ? 0.3212 0.2039 0.2792 -0.0450 0.1017  0.0044  112 ALA B O   
3741 C CB  . ALA B 111 ? 0.3638 0.1993 0.2764 -0.0515 0.1621  -0.0095 112 ALA B CB  
3742 N N   . THR B 112 ? 0.3271 0.2105 0.2906 -0.0440 0.1149  -0.0101 113 THR B N   
3743 C CA  . THR B 112 ? 0.2698 0.1917 0.2818 -0.0378 0.0972  -0.0087 113 THR B CA  
3744 C C   . THR B 112 ? 0.2843 0.2013 0.2837 -0.0379 0.0736  -0.0086 113 THR B C   
3745 O O   . THR B 112 ? 0.2440 0.1901 0.2815 -0.0328 0.0626  -0.0100 113 THR B O   
3746 C CB  . THR B 112 ? 0.2476 0.1999 0.3078 -0.0330 0.1143  -0.0157 113 THR B CB  
3747 O OG1 . THR B 112 ? 0.2755 0.2128 0.3202 -0.0345 0.1284  -0.0248 113 THR B OG1 
3748 C CG2 . THR B 112 ? 0.2570 0.2148 0.3260 -0.0266 0.1161  -0.0152 113 THR B CG2 
3749 N N   . TYR B 113 ? 0.3052 0.1849 0.2513 -0.0437 0.0650  -0.0068 114 TYR B N   
3750 C CA  . TYR B 113 ? 0.3206 0.1924 0.2511 -0.0447 0.0375  -0.0038 114 TYR B CA  
3751 C C   . TYR B 113 ? 0.3124 0.1915 0.2530 -0.0430 0.0365  -0.0118 114 TYR B C   
3752 O O   . TYR B 113 ? 0.3003 0.1917 0.2546 -0.0409 0.0141  -0.0097 114 TYR B O   
3753 C CB  . TYR B 113 ? 0.2802 0.1779 0.2428 -0.0406 0.0132  0.0053  114 TYR B CB  
3754 C CG  . TYR B 113 ? 0.2921 0.1992 0.2680 -0.0395 0.0178  0.0122  114 TYR B CG  
3755 C CD1 . TYR B 113 ? 0.3094 0.1860 0.2436 -0.0448 0.0176  0.0179  114 TYR B CD1 
3756 C CD2 . TYR B 113 ? 0.2248 0.1697 0.2535 -0.0335 0.0220  0.0130  114 TYR B CD2 
3757 C CE1 . TYR B 113 ? 0.3333 0.2185 0.2799 -0.0438 0.0221  0.0242  114 TYR B CE1 
3758 C CE2 . TYR B 113 ? 0.2337 0.1868 0.2745 -0.0326 0.0264  0.0192  114 TYR B CE2 
3759 C CZ  . TYR B 113 ? 0.2802 0.2041 0.2806 -0.0376 0.0263  0.0248  114 TYR B CZ  
3760 O OH  . TYR B 113 ? 0.2839 0.2157 0.2962 -0.0368 0.0310  0.0309  114 TYR B OH  
3761 N N   . THR B 114 ? 0.3176 0.1867 0.2493 -0.0443 0.0602  -0.0209 115 THR B N   
3762 C CA  . THR B 114 ? 0.3145 0.1916 0.2577 -0.0424 0.0598  -0.0286 115 THR B CA  
3763 C C   . THR B 114 ? 0.3623 0.1981 0.2513 -0.0487 0.0664  -0.0342 115 THR B C   
3764 O O   . THR B 114 ? 0.3542 0.1921 0.2491 -0.0477 0.0760  -0.0425 115 THR B O   
3765 C CB  . THR B 114 ? 0.3067 0.2156 0.2988 -0.0370 0.0801  -0.0354 115 THR B CB  
3766 O OG1 . THR B 114 ? 0.3213 0.2147 0.3002 -0.0395 0.1090  -0.0394 115 THR B OG1 
3767 C CG2 . THR B 114 ? 0.2465 0.1956 0.2918 -0.0308 0.0713  -0.0303 115 THR B CG2 
3768 N N   . SER B 115 ? 0.3855 0.1826 0.2207 -0.0552 0.0602  -0.0298 116 SER B N   
3769 C CA  . SER B 115 ? 0.4484 0.2027 0.2277 -0.0618 0.0646  -0.0347 116 SER B CA  
3770 C C   . SER B 115 ? 0.4424 0.1990 0.2217 -0.0613 0.0445  -0.0372 116 SER B C   
3771 O O   . SER B 115 ? 0.4776 0.2092 0.2260 -0.0648 0.0527  -0.0442 116 SER B O   
3772 C CB  . SER B 115 ? 0.5220 0.2336 0.2426 -0.0691 0.0568  -0.0283 116 SER B CB  
3773 O OG  . SER B 115 ? 0.5210 0.2336 0.2375 -0.0696 0.0232  -0.0202 116 SER B OG  
3774 N N   . GLY B 116 ? 0.4080 0.1930 0.2211 -0.0572 0.0186  -0.0316 117 GLY B N   
3775 C CA  . GLY B 116 ? 0.4148 0.2049 0.2328 -0.0564 -0.0014 -0.0335 117 GLY B CA  
3776 C C   . GLY B 116 ? 0.4633 0.2223 0.2377 -0.0622 -0.0286 -0.0275 117 GLY B C   
3777 O O   . GLY B 116 ? 0.4680 0.2315 0.2478 -0.0618 -0.0479 -0.0282 117 GLY B O   
3778 N N   . ASN B 117 ? 0.5108 0.2384 0.2430 -0.0678 -0.0318 -0.0214 118 ASN B N   
3779 C CA  . ASN B 117 ? 0.5118 0.2105 0.2050 -0.0734 -0.0605 -0.0144 118 ASN B CA  
3780 C C   . ASN B 117 ? 0.5391 0.2175 0.2052 -0.0771 -0.0659 -0.0054 118 ASN B C   
3781 O O   . ASN B 117 ? 0.6299 0.2630 0.2367 -0.0848 -0.0716 -0.0033 118 ASN B O   
3782 C CB  . ASN B 117 ? 0.5934 0.2493 0.2308 -0.0804 -0.0596 -0.0204 118 ASN B CB  
3783 C CG  . ASN B 117 ? 0.6249 0.2587 0.2338 -0.0852 -0.0939 -0.0140 118 ASN B CG  
3784 O OD1 . ASN B 117 ? 0.6332 0.2918 0.2757 -0.0818 -0.1185 -0.0064 118 ASN B OD1 
3785 N ND2 . ASN B 117 ? 0.7013 0.2937 0.2574 -0.0914 -0.0936 -0.0147 118 ASN B ND2 
3786 N N   . LEU B 118 ? 0.5443 0.2544 0.2520 -0.0719 -0.0645 0.0001  119 LEU B N   
3787 C CA  . LEU B 118 ? 0.5796 0.2752 0.2682 -0.0746 -0.0732 0.0098  119 LEU B CA  
3788 C C   . LEU B 118 ? 0.5236 0.2579 0.2644 -0.0685 -0.0934 0.0182  119 LEU B C   
3789 O O   . LEU B 118 ? 0.4935 0.2686 0.2882 -0.0614 -0.0837 0.0162  119 LEU B O   
3790 C CB  . LEU B 118 ? 0.5473 0.2338 0.2237 -0.0756 -0.0435 0.0078  119 LEU B CB  
3791 C CG  . LEU B 118 ? 0.6076 0.2472 0.2234 -0.0828 -0.0231 0.0012  119 LEU B CG  
3792 C CD1 . LEU B 118 ? 0.6118 0.2486 0.2259 -0.0828 0.0073  -0.0006 119 LEU B CD1 
3793 C CD2 . LEU B 118 ? 0.6607 0.2501 0.2104 -0.0915 -0.0432 0.0064  119 LEU B CD2 
3794 N N   . ALA B 119 ? 0.5661 0.2862 0.2905 -0.0714 -0.1214 0.0277  120 ALA B N   
3795 C CA  . ALA B 119 ? 0.5613 0.3139 0.3325 -0.0662 -0.1431 0.0363  120 ALA B CA  
3796 C C   . ALA B 119 ? 0.5259 0.2841 0.3047 -0.0650 -0.1385 0.0439  120 ALA B C   
3797 O O   . ALA B 119 ? 0.5418 0.2819 0.2937 -0.0679 -0.1175 0.0419  120 ALA B O   
3798 C CB  . ALA B 119 ? 0.5663 0.3091 0.3360 -0.0678 -0.1664 0.0404  120 ALA B CB  
3799 N N   . LEU B 120 ? 0.5194 0.3042 0.3393 -0.0607 -0.1549 0.0513  121 LEU B N   
3800 C CA  . LEU B 120 ? 0.5001 0.2947 0.3334 -0.0590 -0.1503 0.0576  121 LEU B CA  
3801 C C   . LEU B 120 ? 0.5725 0.3266 0.3512 -0.0662 -0.1496 0.0605  121 LEU B C   
3802 O O   . LEU B 120 ? 0.5622 0.3058 0.3235 -0.0672 -0.1351 0.0644  121 LEU B O   
3803 C CB  . LEU B 120 ? 0.4961 0.3267 0.3867 -0.0540 -0.1561 0.0578  121 LEU B CB  
3804 C CG  . LEU B 120 ? 0.5432 0.3888 0.4528 -0.0519 -0.1512 0.0625  121 LEU B CG  
3805 C CD1 . LEU B 120 ? 0.4733 0.3354 0.3975 -0.0478 -0.1368 0.0645  121 LEU B CD1 
3806 C CD2 . LEU B 120 ? 0.5083 0.3810 0.4639 -0.0481 -0.1514 0.0611  121 LEU B CD2 
3807 N N   . GLN B 121 ? 0.5951 0.3250 0.3487 -0.0713 -0.1626 0.0586  122 GLN B N   
3808 C CA  . GLN B 121 ? 0.6656 0.3585 0.3724 -0.0780 -0.1645 0.0605  122 GLN B CA  
3809 C C   . GLN B 121 ? 0.7241 0.3732 0.3742 -0.0852 -0.1636 0.0555  122 GLN B C   
3810 O O   . GLN B 121 ? 0.7223 0.3715 0.3740 -0.0850 -0.1667 0.0513  122 GLN B O   
3811 C CB  . GLN B 121 ? 0.6657 0.3667 0.3958 -0.0782 -0.1815 0.0641  122 GLN B CB  
3812 C CG  . GLN B 121 ? 0.6620 0.4075 0.4527 -0.0712 -0.1813 0.0671  122 GLN B CG  
3813 C CD  . GLN B 121 ? 0.6323 0.3833 0.4217 -0.0697 -0.1711 0.0711  122 GLN B CD  
3814 O OE1 . GLN B 121 ? 0.6460 0.3670 0.3892 -0.0738 -0.1625 0.0720  122 GLN B OE1 
3815 N NE2 . GLN B 121 ? 0.6771 0.4650 0.5164 -0.0639 -0.1687 0.0730  122 GLN B NE2 
3816 N N   . PHE B 122 ? 0.7728 0.3843 0.3736 -0.0914 -0.1579 0.0557  123 PHE B N   
3817 C CA  . PHE B 122 ? 0.8581 0.4262 0.4094 -0.0988 -0.1621 0.0519  123 PHE B CA  
3818 C C   . PHE B 122 ? 0.9217 0.4944 0.4949 -0.0994 -0.1872 0.0547  123 PHE B C   
3819 O O   . PHE B 122 ? 0.8861 0.4856 0.5005 -0.0960 -0.1988 0.0596  123 PHE B O   
3820 C CB  . PHE B 122 ? 0.9038 0.4338 0.4060 -0.1048 -0.1532 0.0521  123 PHE B CB  
3821 C CG  . PHE B 122 ? 0.8782 0.3913 0.3483 -0.1061 -0.1231 0.0473  123 PHE B CG  
3822 C CD1 . PHE B 122 ? 0.9019 0.3867 0.3351 -0.1100 -0.1080 0.0397  123 PHE B CD1 
3823 C CD2 . PHE B 122 ? 0.8909 0.4165 0.3706 -0.1034 -0.1071 0.0501  123 PHE B CD2 
3824 C CE1 . PHE B 122 ? 0.9257 0.3962 0.3349 -0.1111 -0.0759 0.0341  123 PHE B CE1 
3825 C CE2 . PHE B 122 ? 0.8889 0.4003 0.3453 -0.1045 -0.0755 0.0452  123 PHE B CE2 
3826 C CZ  . PHE B 122 ? 0.9130 0.3974 0.3354 -0.1084 -0.0591 0.0368  123 PHE B CZ  
3827 N N   . PRO B 123 ? 0.9927 0.5394 0.5402 -0.1037 -0.1936 0.0518  124 PRO B N   
3828 C CA  . PRO B 123 ? 1.0138 0.5595 0.5777 -0.1050 -0.2155 0.0553  124 PRO B CA  
3829 C C   . PRO B 123 ? 1.0459 0.5725 0.5944 -0.1096 -0.2264 0.0600  124 PRO B C   
3830 O O   . PRO B 123 ? 1.0613 0.5619 0.5705 -0.1136 -0.2175 0.0594  124 PRO B O   
3831 C CB  . PRO B 123 ? 1.0394 0.5523 0.5660 -0.1097 -0.2167 0.0514  124 PRO B CB  
3832 C CG  . PRO B 123 ? 1.0587 0.5483 0.5413 -0.1122 -0.1940 0.0455  124 PRO B CG  
3833 C CD  . PRO B 123 ? 0.9675 0.4881 0.4752 -0.1067 -0.1792 0.0452  124 PRO B CD  
3834 N N   . ASP B 124 ? 1.0467 0.5868 0.6279 -0.1089 -0.2443 0.0643  125 ASP B N   
3835 C CA  . ASP B 124 ? 1.1104 0.6417 0.6894 -0.1121 -0.2554 0.0692  125 ASP B CA  
3836 C C   . ASP B 124 ? 1.1472 0.6261 0.6616 -0.1208 -0.2571 0.0687  125 ASP B C   
3837 O O   . ASP B 124 ? 1.1693 0.6383 0.6689 -0.1229 -0.2563 0.0710  125 ASP B O   
3838 C CB  . ASP B 124 ? 1.1438 0.6891 0.7599 -0.1115 -0.2734 0.0731  125 ASP B CB  
3839 C CG  . ASP B 124 ? 1.1500 0.7438 0.8284 -0.1039 -0.2706 0.0755  125 ASP B CG  
3840 O OD1 . ASP B 124 ? 1.1899 0.7925 0.8767 -0.1033 -0.2693 0.0784  125 ASP B OD1 
3841 O OD2 . ASP B 124 ? 1.1478 0.7699 0.8657 -0.0986 -0.2683 0.0741  125 ASP B OD2 
3842 N N   . GLU B 125 ? 1.1925 0.6368 0.6675 -0.1259 -0.2582 0.0655  126 GLU B N   
3843 C CA  . GLU B 125 ? 1.2518 0.6429 0.6658 -0.1349 -0.2611 0.0650  126 GLU B CA  
3844 C C   . GLU B 125 ? 1.2512 0.6177 0.6196 -0.1370 -0.2381 0.0602  126 GLU B C   
3845 O O   . GLU B 125 ? 1.2828 0.6026 0.5977 -0.1444 -0.2366 0.0588  126 GLU B O   
3846 C CB  . GLU B 125 ? 1.2648 0.6262 0.6546 -0.1398 -0.2717 0.0640  126 GLU B CB  
3847 C CG  . GLU B 125 ? 1.3297 0.6792 0.6949 -0.1397 -0.2551 0.0578  126 GLU B CG  
3848 C CD  . GLU B 125 ? 1.2666 0.6616 0.6819 -0.1314 -0.2509 0.0564  126 GLU B CD  
3849 O OE1 . GLU B 125 ? 1.2304 0.6660 0.7003 -0.1257 -0.2596 0.0600  126 GLU B OE1 
3850 O OE2 . GLU B 125 ? 1.2500 0.6397 0.6504 -0.1307 -0.2377 0.0514  126 GLU B OE2 
3851 N N   . VAL B 126 ? 1.2286 0.6236 0.6165 -0.1311 -0.2193 0.0577  127 VAL B N   
3852 C CA  . VAL B 126 ? 1.2306 0.6048 0.5799 -0.1326 -0.1940 0.0530  127 VAL B CA  
3853 C C   . VAL B 126 ? 1.2403 0.6244 0.5969 -0.1311 -0.1909 0.0567  127 VAL B C   
3854 O O   . VAL B 126 ? 1.2111 0.6369 0.6114 -0.1243 -0.1870 0.0593  127 VAL B O   
3855 C CB  . VAL B 126 ? 1.1992 0.5958 0.5632 -0.1275 -0.1734 0.0481  127 VAL B CB  
3856 C CG1 . VAL B 126 ? 1.1874 0.5591 0.5112 -0.1298 -0.1439 0.0426  127 VAL B CG1 
3857 C CG2 . VAL B 126 ? 1.1676 0.5590 0.5301 -0.1283 -0.1786 0.0451  127 VAL B CG2 
3858 N N   . LYS B 127 ? 1.2714 0.6163 0.5849 -0.1376 -0.1923 0.0573  128 LYS B N   
3859 C CA  . LYS B 127 ? 1.2784 0.6284 0.5947 -0.1368 -0.1907 0.0611  128 LYS B CA  
3860 C C   . LYS B 127 ? 1.2763 0.5909 0.5430 -0.1405 -0.1670 0.0567  128 LYS B C   
3861 O O   . LYS B 127 ? 1.3492 0.6824 0.6278 -0.1361 -0.1477 0.0563  128 LYS B O   
3862 C CB  . LYS B 127 ? 1.2568 0.5970 0.5755 -0.1405 -0.2173 0.0668  128 LYS B CB  
3863 C CG  . LYS B 127 ? 1.2476 0.6230 0.6193 -0.1368 -0.2384 0.0709  128 LYS B CG  
3864 C CD  . LYS B 127 ? 1.2623 0.6206 0.6308 -0.1420 -0.2630 0.0758  128 LYS B CD  
3865 C CE  . LYS B 127 ? 1.2425 0.6327 0.6630 -0.1387 -0.2807 0.0790  128 LYS B CE  
3866 N NZ  . LYS B 127 ? 1.2091 0.6541 0.6903 -0.1296 -0.2751 0.0810  128 LYS B NZ  
3867 N N   . THR B 128 ? 1.3702 0.6338 0.5830 -0.1485 -0.1667 0.0535  129 THR B N   
3868 C CA  . THR B 128 ? 1.3988 0.6259 0.5649 -0.1523 -0.1437 0.0491  129 THR B CA  
3869 C C   . THR B 128 ? 1.3660 0.5969 0.5285 -0.1496 -0.1125 0.0420  129 THR B C   
3870 O O   . THR B 128 ? 1.3484 0.6044 0.5374 -0.1457 -0.1103 0.0403  129 THR B O   
3871 C CB  . THR B 128 ? 1.3978 0.5673 0.5074 -0.1618 -0.1519 0.0475  129 THR B CB  
3872 O OG1 . THR B 128 ? 1.4912 0.6260 0.5582 -0.1653 -0.1294 0.0434  129 THR B OG1 
3873 C CG2 . THR B 128 ? 1.4186 0.5692 0.5114 -0.1648 -0.1517 0.0434  129 THR B CG2 
3874 N N   . ASP B 129 ? 1.3614 0.5665 0.4918 -0.1518 -0.0875 0.0376  130 ASP B N   
3875 C CA  . ASP B 129 ? 1.3535 0.5595 0.4813 -0.1496 -0.0548 0.0303  130 ASP B CA  
3876 C C   . ASP B 129 ? 1.4237 0.6016 0.5250 -0.1538 -0.0507 0.0250  130 ASP B C   
3877 O O   . ASP B 129 ? 1.3394 0.5363 0.4598 -0.1502 -0.0352 0.0208  130 ASP B O   
3878 C CB  . ASP B 129 ? 1.3411 0.5236 0.4427 -0.1513 -0.0289 0.0267  130 ASP B CB  
3879 C CG  . ASP B 129 ? 1.4054 0.6248 0.5425 -0.1452 -0.0232 0.0308  130 ASP B CG  
3880 O OD1 . ASP B 129 ? 1.3976 0.6623 0.5814 -0.1393 -0.0360 0.0361  130 ASP B OD1 
3881 O OD2 . ASP B 129 ? 1.4788 0.6814 0.5980 -0.1463 -0.0056 0.0290  130 ASP B OD2 
3882 N N   . GLN B 130 ? 1.3874 0.5195 0.4448 -0.1615 -0.0639 0.0252  131 GLN B N   
3883 C CA  . GLN B 130 ? 1.4036 0.5066 0.4340 -0.1657 -0.0597 0.0209  131 GLN B CA  
3884 C C   . GLN B 130 ? 1.3840 0.5196 0.4499 -0.1621 -0.0771 0.0231  131 GLN B C   
3885 O O   . GLN B 130 ? 1.3697 0.5036 0.4340 -0.1617 -0.0650 0.0187  131 GLN B O   
3886 C CB  . GLN B 130 ? 1.4726 0.5192 0.4490 -0.1750 -0.0726 0.0219  131 GLN B CB  
3887 C CG  . GLN B 130 ? 1.4799 0.4817 0.4100 -0.1797 -0.0462 0.0166  131 GLN B CG  
3888 C CD  . GLN B 130 ? 1.4669 0.4660 0.3954 -0.1781 -0.0126 0.0092  131 GLN B CD  
3889 O OE1 . GLN B 130 ? 1.5220 0.5391 0.4684 -0.1736 0.0133  0.0056  131 GLN B OE1 
3890 N NE2 . GLN B 130 ? 1.4656 0.4430 0.3751 -0.1815 -0.0126 0.0071  131 GLN B NE2 
3891 N N   . GLN B 131 ? 1.4026 0.5688 0.5031 -0.1592 -0.1050 0.0298  132 GLN B N   
3892 C CA  . GLN B 131 ? 1.3269 0.5288 0.4681 -0.1547 -0.1204 0.0319  132 GLN B CA  
3893 C C   . GLN B 131 ? 1.3288 0.5716 0.5068 -0.1472 -0.0998 0.0284  132 GLN B C   
3894 O O   . GLN B 131 ? 1.2614 0.5233 0.4603 -0.1444 -0.1019 0.0269  132 GLN B O   
3895 C CB  . GLN B 131 ? 1.3366 0.5650 0.5134 -0.1527 -0.1518 0.0398  132 GLN B CB  
3896 C CG  . GLN B 131 ? 1.3898 0.5836 0.5405 -0.1598 -0.1772 0.0435  132 GLN B CG  
3897 C CD  . GLN B 131 ? 1.3785 0.5936 0.5606 -0.1585 -0.2025 0.0508  132 GLN B CD  
3898 O OE1 . GLN B 131 ? 1.3677 0.6169 0.5828 -0.1531 -0.1992 0.0533  132 GLN B OE1 
3899 N NE2 . GLN B 131 ? 1.4665 0.6611 0.6394 -0.1636 -0.2270 0.0546  132 GLN B NE2 
3900 N N   . VAL B 132 ? 1.2810 0.5373 0.4676 -0.1440 -0.0794 0.0272  133 VAL B N   
3901 C CA  . VAL B 132 ? 1.2561 0.5487 0.4764 -0.1374 -0.0575 0.0238  133 VAL B CA  
3902 C C   . VAL B 132 ? 1.2638 0.5342 0.4602 -0.1394 -0.0281 0.0152  133 VAL B C   
3903 O O   . VAL B 132 ? 1.1949 0.4895 0.4159 -0.1354 -0.0172 0.0116  133 VAL B O   
3904 C CB  . VAL B 132 ? 1.2566 0.5716 0.4972 -0.1333 -0.0458 0.0263  133 VAL B CB  
3905 C CG1 . VAL B 132 ? 1.2461 0.5783 0.5029 -0.1292 -0.0115 0.0204  133 VAL B CG1 
3906 C CG2 . VAL B 132 ? 1.2269 0.5843 0.5141 -0.1281 -0.0704 0.0347  133 VAL B CG2 
3907 N N   . LEU B 133 ? 1.3255 0.5496 0.4755 -0.1455 -0.0147 0.0117  134 LEU B N   
3908 C CA  . LEU B 133 ? 1.3427 0.5432 0.4714 -0.1477 0.0137  0.0040  134 LEU B CA  
3909 C C   . LEU B 133 ? 1.3070 0.5025 0.4315 -0.1491 0.0035  0.0030  134 LEU B C   
3910 O O   . LEU B 133 ? 1.2619 0.4720 0.4025 -0.1463 0.0222  -0.0021 134 LEU B O   
3911 C CB  . LEU B 133 ? 1.3511 0.4996 0.4294 -0.1545 0.0262  0.0017  134 LEU B CB  
3912 C CG  . LEU B 133 ? 1.4153 0.5320 0.4671 -0.1579 0.0526  -0.0051 134 LEU B CG  
3913 C CD1 . LEU B 133 ? 1.3426 0.4895 0.4306 -0.1520 0.0852  -0.0109 134 LEU B CD1 
3914 C CD2 . LEU B 133 ? 1.4390 0.4993 0.4369 -0.1655 0.0602  -0.0064 134 LEU B CD2 
3915 N N   . THR B 134 ? 1.3230 0.4993 0.4286 -0.1534 -0.0262 0.0080  135 THR B N   
3916 C CA  . THR B 134 ? 1.2869 0.4571 0.3879 -0.1549 -0.0378 0.0078  135 THR B CA  
3917 C C   . THR B 134 ? 1.2279 0.4492 0.3804 -0.1478 -0.0507 0.0094  135 THR B C   
3918 O O   . THR B 134 ? 1.1892 0.4146 0.3463 -0.1472 -0.0519 0.0073  135 THR B O   
3919 C CB  . THR B 134 ? 1.4044 0.5380 0.4720 -0.1618 -0.0655 0.0129  135 THR B CB  
3920 O OG1 . THR B 134 ? 1.4783 0.6380 0.5757 -0.1594 -0.0951 0.0198  135 THR B OG1 
3921 C CG2 . THR B 134 ? 1.3707 0.4529 0.3866 -0.1689 -0.0546 0.0115  135 THR B CG2 
3922 N N   . PHE B 135 ? 1.1961 0.4560 0.3876 -0.1425 -0.0605 0.0132  136 PHE B N   
3923 C CA  . PHE B 135 ? 1.1376 0.4465 0.3796 -0.1354 -0.0697 0.0142  136 PHE B CA  
3924 C C   . PHE B 135 ? 1.0979 0.4244 0.3538 -0.1316 -0.0398 0.0064  136 PHE B C   
3925 O O   . PHE B 135 ? 1.0499 0.3961 0.3260 -0.1286 -0.0425 0.0038  136 PHE B O   
3926 C CB  . PHE B 135 ? 1.0529 0.3981 0.3337 -0.1306 -0.0837 0.0203  136 PHE B CB  
3927 C CG  . PHE B 135 ? 1.0161 0.4117 0.3503 -0.1231 -0.0913 0.0214  136 PHE B CG  
3928 C CD1 . PHE B 135 ? 0.9821 0.3951 0.3429 -0.1212 -0.1186 0.0253  136 PHE B CD1 
3929 C CD2 . PHE B 135 ? 0.9782 0.4036 0.3379 -0.1179 -0.0703 0.0185  136 PHE B CD2 
3930 C CE1 . PHE B 135 ? 0.9114 0.3704 0.3233 -0.1140 -0.1253 0.0259  136 PHE B CE1 
3931 C CE2 . PHE B 135 ? 0.8928 0.3622 0.2997 -0.1114 -0.0779 0.0194  136 PHE B CE2 
3932 C CZ  . PHE B 135 ? 0.8705 0.3569 0.3038 -0.1093 -0.1060 0.0228  136 PHE B CZ  
3933 N N   . PHE B 136 ? 1.0807 0.4021 0.3300 -0.1313 -0.0103 0.0022  137 PHE B N   
3934 C CA  . PHE B 136 ? 1.0762 0.4178 0.3470 -0.1273 0.0199  -0.0055 137 PHE B CA  
3935 C C   . PHE B 136 ? 1.0646 0.3776 0.3091 -0.1310 0.0364  -0.0116 137 PHE B C   
3936 O O   . PHE B 136 ? 1.0218 0.3564 0.2905 -0.1273 0.0520  -0.0175 137 PHE B O   
3937 C CB  . PHE B 136 ? 1.0145 0.3649 0.2970 -0.1251 0.0465  -0.0076 137 PHE B CB  
3938 C CG  . PHE B 136 ? 0.9186 0.3103 0.2408 -0.1195 0.0373  -0.0024 137 PHE B CG  
3939 C CD1 . PHE B 136 ? 0.9068 0.3406 0.2712 -0.1136 0.0356  -0.0035 137 PHE B CD1 
3940 C CD2 . PHE B 136 ? 0.9453 0.3341 0.2635 -0.1200 0.0305  0.0038  137 PHE B CD2 
3941 C CE1 . PHE B 136 ? 0.8640 0.3341 0.2647 -0.1088 0.0272  0.0033  137 PHE B CE1 
3942 C CE2 . PHE B 136 ? 0.8886 0.3163 0.2461 -0.1147 0.0223  0.0103  137 PHE B CE2 
3943 C CZ  . PHE B 136 ? 0.8718 0.3392 0.2706 -0.1093 0.0207  0.0111  137 PHE B CZ  
3944 N N   . LYS B 137 ? 1.0893 0.3544 0.2859 -0.1381 0.0332  -0.0101 138 LYS B N   
3945 C CA  . LYS B 137 ? 1.1547 0.3909 0.3244 -0.1420 0.0453  -0.0143 138 LYS B CA  
3946 C C   . LYS B 137 ? 1.1071 0.3553 0.2857 -0.1409 0.0232  -0.0130 138 LYS B C   
3947 O O   . LYS B 137 ? 1.1053 0.3561 0.2876 -0.1401 0.0366  -0.0181 138 LYS B O   
3948 C CB  . LYS B 137 ? 1.1948 0.3742 0.3089 -0.1503 0.0457  -0.0126 138 LYS B CB  
3949 C CG  . LYS B 137 ? 1.2567 0.4167 0.3572 -0.1518 0.0758  -0.0164 138 LYS B CG  
3950 C CD  . LYS B 137 ? 1.3989 0.5019 0.4428 -0.1602 0.0705  -0.0142 138 LYS B CD  
3951 C CE  . LYS B 137 ? 1.4821 0.5541 0.5037 -0.1631 0.1043  -0.0195 138 LYS B CE  
3952 N NZ  . LYS B 137 ? 1.4391 0.5104 0.4664 -0.1628 0.1264  -0.0246 138 LYS B NZ  
3953 N N   . ASP B 138 ? 1.0968 0.3532 0.2821 -0.1408 -0.0106 -0.0062 139 ASP B N   
3954 C CA  . ASP B 138 ? 1.1259 0.3950 0.3242 -0.1395 -0.0337 -0.0043 139 ASP B CA  
3955 C C   . ASP B 138 ? 1.0506 0.3740 0.3033 -0.1312 -0.0352 -0.0071 139 ASP B C   
3956 O O   . ASP B 138 ? 1.0561 0.3950 0.3257 -0.1289 -0.0505 -0.0071 139 ASP B O   
3957 C CB  . ASP B 138 ? 1.1879 0.4451 0.3784 -0.1424 -0.0691 0.0043  139 ASP B CB  
3958 C CG  . ASP B 138 ? 1.2434 0.4438 0.3780 -0.1513 -0.0715 0.0064  139 ASP B CG  
3959 O OD1 . ASP B 138 ? 1.2147 0.3831 0.3148 -0.1553 -0.0476 0.0015  139 ASP B OD1 
3960 O OD2 . ASP B 138 ? 1.2899 0.4779 0.4170 -0.1543 -0.0970 0.0128  139 ASP B OD2 
3961 N N   . TRP B 139 ? 0.9764 0.3283 0.2572 -0.1266 -0.0195 -0.0098 140 TRP B N   
3962 C CA  . TRP B 139 ? 0.9053 0.3078 0.2382 -0.1190 -0.0214 -0.0130 140 TRP B CA  
3963 C C   . TRP B 139 ? 0.9000 0.3149 0.2468 -0.1163 -0.0055 -0.0219 140 TRP B C   
3964 O O   . TRP B 139 ? 0.9510 0.3446 0.2772 -0.1188 0.0209  -0.0270 140 TRP B O   
3965 C CB  . TRP B 139 ? 0.8914 0.3153 0.2461 -0.1155 -0.0030 -0.0149 140 TRP B CB  
3966 C CG  . TRP B 139 ? 0.8061 0.2798 0.2142 -0.1082 -0.0051 -0.0188 140 TRP B CG  
3967 C CD1 . TRP B 139 ? 0.7666 0.2693 0.2058 -0.1048 -0.0292 -0.0128 140 TRP B CD1 
3968 C CD2 . TRP B 139 ? 0.7897 0.2906 0.2323 -0.1032 0.0179  -0.0298 140 TRP B CD2 
3969 N NE1 . TRP B 139 ? 0.7179 0.2733 0.2255 -0.0960 -0.0217 -0.0163 140 TRP B NE1 
3970 C CE2 . TRP B 139 ? 0.6996 0.2538 0.2086 -0.0952 0.0064  -0.0271 140 TRP B CE2 
3971 C CE3 . TRP B 139 ? 0.8189 0.3143 0.2608 -0.1028 0.0468  -0.0377 140 TRP B CE3 
3972 C CZ2 . TRP B 139 ? 0.6643 0.2605 0.2298 -0.0878 0.0222  -0.0339 140 TRP B CZ2 
3973 C CZ3 . TRP B 139 ? 0.7670 0.2998 0.2582 -0.0963 0.0627  -0.0464 140 TRP B CZ3 
3974 C CH2 . TRP B 139 ? 0.6866 0.2700 0.2405 -0.0888 0.0499  -0.0441 140 TRP B CH2 
3975 N N   . LYS B 140 ? 0.8500 0.3003 0.2355 -0.1111 -0.0220 -0.0234 141 LYS B N   
3976 C CA  . LYS B 140 ? 0.8199 0.2903 0.2291 -0.1073 -0.0092 -0.0323 141 LYS B CA  
3977 C C   . LYS B 140 ? 0.7547 0.2755 0.2228 -0.0997 -0.0115 -0.0371 141 LYS B C   
3978 O O   . LYS B 140 ? 0.7435 0.2836 0.2337 -0.0977 -0.0333 -0.0315 141 LYS B O   
3979 C CB  . LYS B 140 ? 0.8385 0.2982 0.2358 -0.1090 -0.0290 -0.0301 141 LYS B CB  
3980 C CG  . LYS B 140 ? 0.9352 0.3424 0.2748 -0.1171 -0.0290 -0.0259 141 LYS B CG  
3981 C CD  . LYS B 140 ? 1.0438 0.4427 0.3755 -0.1183 -0.0469 -0.0245 141 LYS B CD  
3982 C CE  . LYS B 140 ? 1.1456 0.4896 0.4192 -0.1269 -0.0472 -0.0207 141 LYS B CE  
3983 N NZ  . LYS B 140 ? 1.2414 0.5598 0.4905 -0.1315 -0.0637 -0.0120 141 LYS B NZ  
3984 N N   . PRO B 141 ? 0.7254 0.2686 0.2235 -0.0953 0.0099  -0.0468 142 PRO B N   
3985 C CA  . PRO B 141 ? 0.6836 0.2730 0.2411 -0.0883 0.0084  -0.0519 142 PRO B CA  
3986 C C   . PRO B 141 ? 0.6393 0.2522 0.2242 -0.0854 -0.0233 -0.0488 142 PRO B C   
3987 O O   . PRO B 141 ? 0.7040 0.3026 0.2686 -0.0874 -0.0380 -0.0455 142 PRO B O   
3988 C CB  . PRO B 141 ? 0.6941 0.2974 0.2743 -0.0845 0.0404  -0.0616 142 PRO B CB  
3989 C CG  . PRO B 141 ? 0.7313 0.3003 0.2680 -0.0894 0.0475  -0.0614 142 PRO B CG  
3990 C CD  . PRO B 141 ? 0.7564 0.2838 0.2394 -0.0966 0.0386  -0.0529 142 PRO B CD  
3991 N N   . LYS B 142 ? 0.5854 0.2432 0.2286 -0.0785 -0.0321 -0.0463 143 LYS B N   
3992 C CA  . LYS B 142 ? 0.5770 0.2650 0.2587 -0.0742 -0.0573 -0.0445 143 LYS B CA  
3993 C C   . LYS B 142 ? 0.5119 0.2466 0.2560 -0.0656 -0.0429 -0.0504 143 LYS B C   
3994 O O   . LYS B 142 ? 0.4873 0.2248 0.2365 -0.0646 -0.0371 -0.0583 143 LYS B O   
3995 C CB  . LYS B 142 ? 0.5787 0.2784 0.2750 -0.0734 -0.0862 -0.0327 143 LYS B CB  
3996 C CG  . LYS B 142 ? 0.5608 0.2910 0.2970 -0.0680 -0.1108 -0.0279 143 LYS B CG  
3997 C CD  . LYS B 142 ? 0.5503 0.2916 0.3034 -0.0654 -0.1343 -0.0136 143 LYS B CD  
3998 C CE  . LYS B 142 ? 0.5205 0.2962 0.3194 -0.0605 -0.1341 -0.0111 143 LYS B CE  
3999 N NZ  . LYS B 142 ? 0.5558 0.3390 0.3702 -0.0573 -0.1516 0.0030  143 LYS B NZ  
4000 N N   . ASN B 143 ? 0.4781 0.2484 0.2690 -0.0596 -0.0373 -0.0469 144 ASN B N   
4001 C CA  . ASN B 143 ? 0.4276 0.2383 0.2739 -0.0520 -0.0214 -0.0528 144 ASN B CA  
4002 C C   . ASN B 143 ? 0.4733 0.2734 0.3097 -0.0528 0.0131  -0.0607 144 ASN B C   
4003 O O   . ASN B 143 ? 0.5436 0.3092 0.3356 -0.0584 0.0261  -0.0605 144 ASN B O   
4004 C CB  . ASN B 143 ? 0.3821 0.2329 0.2809 -0.0456 -0.0283 -0.0461 144 ASN B CB  
4005 C CG  . ASN B 143 ? 0.4178 0.2869 0.3401 -0.0431 -0.0594 -0.0397 144 ASN B CG  
4006 O OD1 . ASN B 143 ? 0.3822 0.2685 0.3281 -0.0400 -0.0669 -0.0436 144 ASN B OD1 
4007 N ND2 . ASN B 143 ? 0.4300 0.2951 0.3464 -0.0445 -0.0771 -0.0298 144 ASN B ND2 
4008 N N   . SER B 144 ? 0.4459 0.2748 0.3239 -0.0472 0.0280  -0.0678 145 SER B N   
4009 C CA  . SER B 144 ? 0.4020 0.2269 0.2816 -0.0469 0.0610  -0.0749 145 SER B CA  
4010 C C   . SER B 144 ? 0.3686 0.1972 0.2549 -0.0467 0.0734  -0.0700 145 SER B C   
4011 O O   . SER B 144 ? 0.3455 0.2040 0.2689 -0.0424 0.0625  -0.0638 145 SER B O   
4012 C CB  . SER B 144 ? 0.4172 0.2783 0.3495 -0.0401 0.0714  -0.0818 145 SER B CB  
4013 O OG  . SER B 144 ? 0.4659 0.3226 0.3912 -0.0404 0.0617  -0.0868 145 SER B OG  
4014 N N   . ILE B 145 ? 0.4357 0.2328 0.2855 -0.0514 0.0968  -0.0729 146 ILE B N   
4015 C CA  . ILE B 145 ? 0.4465 0.2413 0.2955 -0.0522 0.1091  -0.0681 146 ILE B CA  
4016 C C   . ILE B 145 ? 0.4194 0.2584 0.3319 -0.0451 0.1208  -0.0688 146 ILE B C   
4017 O O   . ILE B 145 ? 0.3986 0.2556 0.3414 -0.0417 0.1359  -0.0748 146 ILE B O   
4018 C CB  . ILE B 145 ? 0.4839 0.2352 0.2823 -0.0586 0.1348  -0.0722 146 ILE B CB  
4019 C CG1 . ILE B 145 ? 0.5390 0.2437 0.2702 -0.0664 0.1195  -0.0693 146 ILE B CG1 
4020 C CG2 . ILE B 145 ? 0.5142 0.2677 0.3207 -0.0586 0.1536  -0.0690 146 ILE B CG2 
4021 C CD1 . ILE B 145 ? 0.6023 0.2659 0.2849 -0.0727 0.1415  -0.0700 146 ILE B CD1 
4022 N N   . GLY B 146 ? 0.3369 0.1950 0.2713 -0.0428 0.1112  -0.0610 147 GLY B N   
4023 C CA  . GLY B 146 ? 0.3356 0.2327 0.3265 -0.0367 0.1203  -0.0605 147 GLY B CA  
4024 C C   . GLY B 146 ? 0.2800 0.2173 0.3207 -0.0302 0.1010  -0.0589 147 GLY B C   
4025 O O   . GLY B 146 ? 0.2663 0.2348 0.3513 -0.0255 0.1037  -0.0566 147 GLY B O   
4026 N N   . GLU B 147 ? 0.3193 0.2559 0.3536 -0.0300 0.0813  -0.0597 148 GLU B N   
4027 C CA  A GLU B 147 ? 0.2516 0.2247 0.3329 -0.0238 0.0658  -0.0595 148 GLU B CA  
4028 C CA  B GLU B 147 ? 0.2512 0.2245 0.3329 -0.0237 0.0660  -0.0594 148 GLU B CA  
4029 C C   . GLU B 147 ? 0.2727 0.2577 0.3636 -0.0223 0.0388  -0.0501 148 GLU B C   
4030 O O   . GLU B 147 ? 0.1840 0.2021 0.3193 -0.0167 0.0289  -0.0485 148 GLU B O   
4031 C CB  A GLU B 147 ? 0.2623 0.2310 0.3376 -0.0237 0.0615  -0.0665 148 GLU B CB  
4032 C CB  B GLU B 147 ? 0.2614 0.2311 0.3384 -0.0235 0.0624  -0.0666 148 GLU B CB  
4033 C CG  A GLU B 147 ? 0.2503 0.2540 0.3713 -0.0175 0.0456  -0.0667 148 GLU B CG  
4034 C CG  B GLU B 147 ? 0.2933 0.2581 0.3695 -0.0242 0.0879  -0.0737 148 GLU B CG  
4035 C CD  A GLU B 147 ? 0.2915 0.3060 0.4247 -0.0175 0.0516  -0.0692 148 GLU B CD  
4036 C CD  B GLU B 147 ? 0.3203 0.2887 0.3972 -0.0235 0.0823  -0.0771 148 GLU B CD  
4037 O OE1 A GLU B 147 ? 0.2876 0.2886 0.4039 -0.0208 0.0685  -0.0700 148 GLU B OE1 
4038 O OE1 B GLU B 147 ? 0.3299 0.3062 0.4166 -0.0210 0.0631  -0.0796 148 GLU B OE1 
4039 O OE2 A GLU B 147 ? 0.2691 0.2910 0.4099 -0.0148 0.0331  -0.0660 148 GLU B OE2 
4040 O OE2 B GLU B 147 ? 0.3541 0.3162 0.4227 -0.0260 0.0949  -0.0765 148 GLU B OE2 
4041 N N   . TYR B 148 ? 0.2338 0.1924 0.2850 -0.0273 0.0269  -0.0436 149 TYR B N   
4042 C CA  . TYR B 148 ? 0.2055 0.1729 0.2646 -0.0262 0.0003  -0.0345 149 TYR B CA  
4043 C C   . TYR B 148 ? 0.2248 0.1812 0.2679 -0.0287 0.0002  -0.0264 149 TYR B C   
4044 O O   . TYR B 148 ? 0.3042 0.2266 0.3013 -0.0346 0.0077  -0.0261 149 TYR B O   
4045 C CB  . TYR B 148 ? 0.2524 0.1991 0.2809 -0.0297 -0.0216 -0.0335 149 TYR B CB  
4046 C CG  . TYR B 148 ? 0.2256 0.1960 0.2870 -0.0251 -0.0296 -0.0382 149 TYR B CG  
4047 C CD1 . TYR B 148 ? 0.2590 0.2288 0.3214 -0.0246 -0.0136 -0.0481 149 TYR B CD1 
4048 C CD2 . TYR B 148 ? 0.2244 0.2189 0.3183 -0.0211 -0.0517 -0.0327 149 TYR B CD2 
4049 C CE1 . TYR B 148 ? 0.2469 0.2396 0.3411 -0.0202 -0.0208 -0.0523 149 TYR B CE1 
4050 C CE2 . TYR B 148 ? 0.2354 0.2474 0.3432 -0.0123 -0.0497 -0.0315 149 TYR B CE2 
4051 C CZ  . TYR B 148 ? 0.1905 0.2040 0.3044 -0.0133 -0.0388 -0.0424 149 TYR B CZ  
4052 O OH  . TYR B 148 ? 0.2413 0.2632 0.3580 -0.0038 -0.0356 -0.0387 149 TYR B OH  
4053 N N   . ARG B 149 ? 0.1865 0.1703 0.2667 -0.0242 -0.0079 -0.0200 150 ARG B N   
4054 C CA  . ARG B 149 ? 0.1960 0.1733 0.2667 -0.0258 -0.0100 -0.0117 150 ARG B CA  
4055 C C   . ARG B 149 ? 0.2670 0.2328 0.3204 -0.0279 -0.0378 -0.0029 150 ARG B C   
4056 O O   . ARG B 149 ? 0.2315 0.2170 0.3124 -0.0243 -0.0566 -0.0001 150 ARG B O   
4057 C CB  . ARG B 149 ? 0.1819 0.1939 0.3017 -0.0201 -0.0037 -0.0092 150 ARG B CB  
4058 C CG  . ARG B 149 ? 0.1789 0.1876 0.2938 -0.0212 -0.0071 0.0000  150 ARG B CG  
4059 C CD  . ARG B 149 ? 0.1589 0.1940 0.3028 -0.0118 -0.0060 0.0029  150 ARG B CD  
4060 N NE  . ARG B 149 ? 0.1494 0.1839 0.2946 -0.0133 -0.0046 0.0098  150 ARG B NE  
4061 C CZ  . ARG B 149 ? 0.1574 0.1885 0.2981 -0.0134 -0.0210 0.0186  150 ARG B CZ  
4062 N NH1 . ARG B 149 ? 0.1974 0.2215 0.3262 -0.0118 -0.0379 0.0210  150 ARG B NH1 
4063 N NH2 . ARG B 149 ? 0.1662 0.1971 0.3089 -0.0148 -0.0177 0.0247  150 ARG B NH2 
4064 N N   . GLN B 150 ? 0.2728 0.2064 0.2815 -0.0337 -0.0404 0.0019  151 GLN B N   
4065 C CA  . GLN B 150 ? 0.2822 0.2048 0.2765 -0.0357 -0.0668 0.0116  151 GLN B CA  
4066 C C   . GLN B 150 ? 0.3001 0.2086 0.2750 -0.0384 -0.0616 0.0183  151 GLN B C   
4067 O O   . GLN B 150 ? 0.3481 0.2241 0.2782 -0.0441 -0.0496 0.0165  151 GLN B O   
4068 C CB  . GLN B 150 ? 0.3617 0.2519 0.3121 -0.0414 -0.0820 0.0107  151 GLN B CB  
4069 C CG  . GLN B 150 ? 0.3971 0.2746 0.3331 -0.0439 -0.1108 0.0211  151 GLN B CG  
4070 C CD  . GLN B 150 ? 0.5121 0.3709 0.4249 -0.0474 -0.1313 0.0202  151 GLN B CD  
4071 O OE1 . GLN B 150 ? 0.5523 0.3897 0.4343 -0.0510 -0.1225 0.0124  151 GLN B OE1 
4072 N NE2 . GLN B 150 ? 0.5410 0.4097 0.4750 -0.0432 -0.1457 0.0280  151 GLN B NE2 
4073 N N   . TYR B 151 ? 0.2616 0.1937 0.2700 -0.0344 -0.0692 0.0257  152 TYR B N   
4074 C CA  . TYR B 151 ? 0.2955 0.2167 0.2892 -0.0365 -0.0638 0.0322  152 TYR B CA  
4075 C C   . TYR B 151 ? 0.3549 0.2336 0.2910 -0.0438 -0.0752 0.0367  152 TYR B C   
4076 O O   . TYR B 151 ? 0.3724 0.2411 0.2971 -0.0455 -0.0997 0.0412  152 TYR B O   
4077 C CB  . TYR B 151 ? 0.2717 0.2211 0.3064 -0.0314 -0.0765 0.0408  152 TYR B CB  
4078 C CG  . TYR B 151 ? 0.2681 0.2127 0.2965 -0.0325 -0.0686 0.0470  152 TYR B CG  
4079 C CD1 . TYR B 151 ? 0.2641 0.2180 0.3040 -0.0313 -0.0433 0.0427  152 TYR B CD1 
4080 C CD2 . TYR B 151 ? 0.3114 0.2428 0.3245 -0.0345 -0.0870 0.0573  152 TYR B CD2 
4081 C CE1 . TYR B 151 ? 0.2736 0.2232 0.3082 -0.0324 -0.0360 0.0484  152 TYR B CE1 
4082 C CE2 . TYR B 151 ? 0.3195 0.2465 0.3267 -0.0354 -0.0799 0.0630  152 TYR B CE2 
4083 C CZ  . TYR B 151 ? 0.2960 0.2322 0.3137 -0.0343 -0.0541 0.0584  152 TYR B CZ  
4084 O OH  . TYR B 151 ? 0.3410 0.2724 0.3527 -0.0354 -0.0477 0.0643  152 TYR B OH  
4085 N N   . SER B 152 ? 0.3588 0.2111 0.2579 -0.0484 -0.0575 0.0356  153 SER B N   
4086 C CA  . SER B 152 ? 0.4294 0.2354 0.2660 -0.0563 -0.0639 0.0370  153 SER B CA  
4087 C C   . SER B 152 ? 0.4807 0.2620 0.2840 -0.0605 -0.0507 0.0405  153 SER B C   
4088 O O   . SER B 152 ? 0.4565 0.2371 0.2588 -0.0606 -0.0232 0.0348  153 SER B O   
4089 C CB  . SER B 152 ? 0.4634 0.2499 0.2729 -0.0594 -0.0522 0.0268  153 SER B CB  
4090 O OG  . SER B 152 ? 0.4997 0.2376 0.2444 -0.0675 -0.0545 0.0276  153 SER B OG  
4091 N N   . ASN B 153 ? 0.4722 0.2304 0.2458 -0.0644 -0.0702 0.0498  154 ASN B N   
4092 C CA  . ASN B 153 ? 0.5267 0.2559 0.2615 -0.0692 -0.0590 0.0533  154 ASN B CA  
4093 C C   . ASN B 153 ? 0.5670 0.2526 0.2433 -0.0762 -0.0423 0.0466  154 ASN B C   
4094 O O   . ASN B 153 ? 0.6016 0.2761 0.2637 -0.0779 -0.0164 0.0435  154 ASN B O   
4095 C CB  . ASN B 153 ? 0.5573 0.2735 0.2773 -0.0713 -0.0856 0.0655  154 ASN B CB  
4096 C CG  . ASN B 153 ? 0.5688 0.3263 0.3460 -0.0644 -0.0968 0.0723  154 ASN B CG  
4097 O OD1 . ASN B 153 ? 0.4806 0.2681 0.2968 -0.0593 -0.0788 0.0698  154 ASN B OD1 
4098 N ND2 . ASN B 153 ? 0.5425 0.3109 0.3358 -0.0629 -0.1219 0.0756  154 ASN B ND2 
4099 N N   . PRO B 154 ? 0.6097 0.2676 0.2494 -0.0808 -0.0548 0.0440  155 PRO B N   
4100 C CA  . PRO B 154 ? 0.6861 0.3004 0.2684 -0.0876 -0.0358 0.0371  155 PRO B CA  
4101 C C   . PRO B 154 ? 0.6195 0.2482 0.2218 -0.0848 -0.0021 0.0263  155 PRO B C   
4102 O O   . PRO B 154 ? 0.6782 0.2774 0.2440 -0.0892 0.0224  0.0218  155 PRO B O   
4103 C CB  . PRO B 154 ? 0.6795 0.2703 0.2309 -0.0917 -0.0579 0.0360  155 PRO B CB  
4104 C CG  . PRO B 154 ? 0.6494 0.2793 0.2526 -0.0858 -0.0830 0.0400  155 PRO B CG  
4105 C CD  . PRO B 154 ? 0.6218 0.2822 0.2659 -0.0807 -0.0869 0.0481  155 PRO B CD  
4106 N N   . SER B 155 ? 0.5810 0.2534 0.2407 -0.0778 -0.0002 0.0221  156 SER B N   
4107 C CA  . SER B 155 ? 0.5557 0.2447 0.2401 -0.0747 0.0300  0.0122  156 SER B CA  
4108 C C   . SER B 155 ? 0.5509 0.2454 0.2457 -0.0739 0.0545  0.0129  156 SER B C   
4109 O O   . SER B 155 ? 0.5652 0.2383 0.2365 -0.0770 0.0818  0.0069  156 SER B O   
4110 C CB  . SER B 155 ? 0.4837 0.2203 0.2303 -0.0671 0.0234  0.0093  156 SER B CB  
4111 O OG  . SER B 155 ? 0.4759 0.2250 0.2428 -0.0647 0.0489  -0.0007 156 SER B OG  
4112 N N   . ILE B 156 ? 0.5217 0.2448 0.2530 -0.0697 0.0461  0.0202  157 ILE B N   
4113 C CA  . ILE B 156 ? 0.5353 0.2633 0.2765 -0.0692 0.0686  0.0210  157 ILE B CA  
4114 C C   . ILE B 156 ? 0.5661 0.2500 0.2493 -0.0761 0.0716  0.0258  157 ILE B C   
4115 O O   . ILE B 156 ? 0.5705 0.2468 0.2480 -0.0775 0.0954  0.0247  157 ILE B O   
4116 C CB  . ILE B 156 ? 0.4862 0.2580 0.2845 -0.0625 0.0607  0.0268  157 ILE B CB  
4117 C CG1 . ILE B 156 ? 0.4644 0.2513 0.2883 -0.0606 0.0894  0.0237  157 ILE B CG1 
4118 C CG2 . ILE B 156 ? 0.5475 0.3111 0.3318 -0.0639 0.0368  0.0381  157 ILE B CG2 
4119 C CD1 . ILE B 156 ? 0.4193 0.2488 0.2999 -0.0543 0.0844  0.0284  157 ILE B CD1 
4120 N N   . GLY B 157 ? 0.6062 0.2599 0.2461 -0.0809 0.0479  0.0313  158 GLY B N   
4121 C CA  . GLY B 157 ? 0.6651 0.2714 0.2435 -0.0883 0.0512  0.0351  158 GLY B CA  
4122 C C   . GLY B 157 ? 0.7037 0.2736 0.2387 -0.0934 0.0784  0.0260  158 GLY B C   
4123 O O   . GLY B 157 ? 0.7266 0.2825 0.2476 -0.0942 0.0957  0.0221  158 GLY B O   
4124 N N   . LEU B 158 ? 0.7075 0.2718 0.2356 -0.0941 0.0799  0.0186  159 LEU B N   
4125 C CA  . LEU B 158 ? 0.7498 0.2858 0.2480 -0.0973 0.1070  0.0080  159 LEU B CA  
4126 C C   . LEU B 158 ? 0.7166 0.2797 0.2586 -0.0923 0.1383  0.0014  159 LEU B C   
4127 O O   . LEU B 158 ? 0.7458 0.2903 0.2756 -0.0930 0.1585  -0.0053 159 LEU B O   
4128 C CB  . LEU B 158 ? 0.7397 0.2655 0.2227 -0.0992 0.1023  0.0025  159 LEU B CB  
4129 C CG  . LEU B 158 ? 0.7723 0.2746 0.2372 -0.1010 0.1279  -0.0096 159 LEU B CG  
4130 C CD1 . LEU B 158 ? 0.8327 0.2908 0.2525 -0.1062 0.1339  -0.0110 159 LEU B CD1 
4131 C CD2 . LEU B 158 ? 0.7831 0.2755 0.2321 -0.1028 0.1184  -0.0141 159 LEU B CD2 
4132 N N   . PHE B 159 ? 0.6661 0.2741 0.2648 -0.0868 0.1403  0.0033  160 PHE B N   
4133 C CA  . PHE B 159 ? 0.6015 0.2405 0.2499 -0.0808 0.1645  -0.0026 160 PHE B CA  
4134 C C   . PHE B 159 ? 0.6255 0.2576 0.2684 -0.0803 0.1698  -0.0002 160 PHE B C   
4135 O O   . PHE B 159 ? 0.6474 0.2733 0.2958 -0.0787 0.1900  -0.0073 160 PHE B O   
4136 C CB  . PHE B 159 ? 0.5575 0.2474 0.2700 -0.0746 0.1589  0.0000  160 PHE B CB  
4137 C CG  . PHE B 159 ? 0.5547 0.2793 0.3222 -0.0673 0.1771  -0.0058 160 PHE B CG  
4138 C CD1 . PHE B 159 ? 0.5276 0.2592 0.3175 -0.0636 0.1932  -0.0165 160 PHE B CD1 
4139 C CD2 . PHE B 159 ? 0.4983 0.2483 0.2974 -0.0633 0.1726  -0.0002 160 PHE B CD2 
4140 C CE1 . PHE B 159 ? 0.4827 0.2432 0.3232 -0.0564 0.2008  -0.0202 160 PHE B CE1 
4141 C CE2 . PHE B 159 ? 0.4945 0.2745 0.3425 -0.0557 0.1824  -0.0055 160 PHE B CE2 
4142 C CZ  . PHE B 159 ? 0.4822 0.2663 0.3499 -0.0524 0.1946  -0.0150 160 PHE B CZ  
4143 N N   . GLY B 160 ? 0.6336 0.2650 0.2664 -0.0817 0.1501  0.0103  161 GLY B N   
4144 C CA  . GLY B 160 ? 0.6516 0.2785 0.2803 -0.0812 0.1542  0.0129  161 GLY B CA  
4145 C C   . GLY B 160 ? 0.7303 0.3111 0.3064 -0.0862 0.1635  0.0079  161 GLY B C   
4146 O O   . GLY B 160 ? 0.7122 0.2892 0.2930 -0.0849 0.1803  0.0044  161 GLY B O   
4147 N N   . LYS B 161 ? 0.7576 0.3020 0.2840 -0.0921 0.1515  0.0077  162 LYS B N   
4148 C CA  . LYS B 161 ? 0.8228 0.3204 0.2989 -0.0974 0.1601  0.0027  162 LYS B CA  
4149 C C   . LYS B 161 ? 0.8023 0.2956 0.2913 -0.0959 0.1899  -0.0077 162 LYS B C   
4150 O O   . LYS B 161 ? 0.8616 0.3319 0.3341 -0.0975 0.2049  -0.0109 162 LYS B O   
4151 C CB  . LYS B 161 ? 0.8588 0.3203 0.2849 -0.1036 0.1406  0.0036  162 LYS B CB  
4152 C CG  . LYS B 161 ? 0.9923 0.4019 0.3640 -0.1100 0.1470  -0.0006 162 LYS B CG  
4153 C CD  . LYS B 161 ? 1.0616 0.4369 0.3898 -0.1159 0.1298  -0.0012 162 LYS B CD  
4154 C CE  . LYS B 161 ? 1.1521 0.4737 0.4259 -0.1228 0.1351  -0.0043 162 LYS B CE  
4155 N NZ  . LYS B 161 ? 1.1133 0.4184 0.3614 -0.1257 0.1152  0.0024  162 LYS B NZ  
4156 N N   . VAL B 162 ? 0.7935 0.3091 0.3144 -0.0928 0.1978  -0.0125 163 VAL B N   
4157 C CA  . VAL B 162 ? 0.8000 0.3139 0.3396 -0.0911 0.2228  -0.0214 163 VAL B CA  
4158 C C   . VAL B 162 ? 0.7429 0.2835 0.3274 -0.0854 0.2372  -0.0224 163 VAL B C   
4159 O O   . VAL B 162 ? 0.8029 0.3252 0.3833 -0.0862 0.2552  -0.0269 163 VAL B O   
4160 C CB  . VAL B 162 ? 0.7602 0.2954 0.3279 -0.0886 0.2243  -0.0256 163 VAL B CB  
4161 C CG1 . VAL B 162 ? 0.7611 0.3065 0.3651 -0.0853 0.2470  -0.0326 163 VAL B CG1 
4162 C CG2 . VAL B 162 ? 0.8064 0.3077 0.3250 -0.0948 0.2132  -0.0261 163 VAL B CG2 
4163 N N   . VAL B 163 ? 0.6879 0.2714 0.3165 -0.0798 0.2285  -0.0179 164 VAL B N   
4164 C CA  . VAL B 163 ? 0.6593 0.2687 0.3303 -0.0744 0.2380  -0.0182 164 VAL B CA  
4165 C C   . VAL B 163 ? 0.7369 0.3154 0.3732 -0.0778 0.2441  -0.0168 164 VAL B C   
4166 O O   . VAL B 163 ? 0.7625 0.3364 0.4112 -0.0763 0.2605  -0.0208 164 VAL B O   
4167 C CB  . VAL B 163 ? 0.6246 0.2801 0.3407 -0.0687 0.2238  -0.0121 164 VAL B CB  
4168 C CG1 . VAL B 163 ? 0.6033 0.2824 0.3584 -0.0634 0.2304  -0.0120 164 VAL B CG1 
4169 C CG2 . VAL B 163 ? 0.5972 0.2836 0.3514 -0.0649 0.2193  -0.0145 164 VAL B CG2 
4170 N N   . ALA B 164 ? 0.7404 0.2954 0.3319 -0.0827 0.2295  -0.0108 165 ALA B N   
4171 C CA  . ALA B 164 ? 0.7764 0.3004 0.3320 -0.0862 0.2329  -0.0093 165 ALA B CA  
4172 C C   . ALA B 164 ? 0.8606 0.3419 0.3822 -0.0906 0.2515  -0.0166 165 ALA B C   
4173 O O   . ALA B 164 ? 0.8631 0.3302 0.3803 -0.0909 0.2656  -0.0186 165 ALA B O   
4174 C CB  . ALA B 164 ? 0.7991 0.3049 0.3134 -0.0908 0.2094  -0.0012 165 ALA B CB  
4175 N N   . LEU B 165 ? 0.8555 0.3149 0.3529 -0.0943 0.2518  -0.0203 166 LEU B N   
4176 C CA  . LEU B 165 ? 0.9075 0.3263 0.3751 -0.0987 0.2701  -0.0267 166 LEU B CA  
4177 C C   . LEU B 165 ? 0.9001 0.3364 0.4126 -0.0941 0.2926  -0.0319 166 LEU B C   
4178 O O   . LEU B 165 ? 0.9342 0.3430 0.4314 -0.0964 0.3095  -0.0350 166 LEU B O   
4179 C CB  . LEU B 165 ? 0.9309 0.3285 0.3711 -0.1029 0.2652  -0.0291 166 LEU B CB  
4180 C CG  . LEU B 165 ? 0.9779 0.3379 0.3578 -0.1098 0.2449  -0.0253 166 LEU B CG  
4181 C CD1 . LEU B 165 ? 1.0598 0.4074 0.4233 -0.1128 0.2390  -0.0276 166 LEU B CD1 
4182 C CD2 . LEU B 165 ? 1.0430 0.3539 0.3738 -0.1156 0.2528  -0.0264 166 LEU B CD2 
4183 N N   . SER B 166 ? 0.8486 0.3296 0.4170 -0.0879 0.2918  -0.0327 167 SER B N   
4184 C CA  . SER B 166 ? 0.8554 0.3543 0.4693 -0.0836 0.3088  -0.0368 167 SER B CA  
4185 C C   . SER B 166 ? 0.8640 0.3696 0.4937 -0.0810 0.3155  -0.0354 167 SER B C   
4186 O O   . SER B 166 ? 0.8611 0.3640 0.5108 -0.0797 0.3318  -0.0389 167 SER B O   
4187 C CB  . SER B 166 ? 0.7821 0.3288 0.4529 -0.0774 0.3017  -0.0371 167 SER B CB  
4188 O OG  . SER B 166 ? 0.7323 0.3168 0.4347 -0.0722 0.2879  -0.0323 167 SER B OG  
4189 N N   . MET B 167 ? 0.8457 0.3598 0.4673 -0.0804 0.3028  -0.0300 168 MET B N   
4190 C CA  . MET B 167 ? 0.8759 0.3986 0.5126 -0.0778 0.3071  -0.0280 168 MET B CA  
4191 C C   . MET B 167 ? 0.9935 0.4715 0.5764 -0.0836 0.3130  -0.0274 168 MET B C   
4192 O O   . MET B 167 ? 0.9912 0.4727 0.5806 -0.0821 0.3162  -0.0254 168 MET B O   
4193 C CB  . MET B 167 ? 0.8568 0.4214 0.5254 -0.0729 0.2893  -0.0216 168 MET B CB  
4194 C CG  . MET B 167 ? 0.7265 0.3377 0.4543 -0.0663 0.2836  -0.0222 168 MET B CG  
4195 S SD  . MET B 167 ? 0.7549 0.4112 0.5145 -0.0615 0.2611  -0.0144 168 MET B SD  
4196 C CE  . MET B 167 ? 0.7477 0.4114 0.5204 -0.0591 0.2642  -0.0113 168 MET B CE  
4197 N N   . ASN B 168 ? 0.9235 0.4013 0.5141 -0.0389 0.2677  0.0109  169 ASN B N   
4198 C CA  . ASN B 168 ? 0.9682 0.4097 0.5136 -0.0347 0.2783  0.0150  169 ASN B CA  
4199 C C   . ASN B 168 ? 1.0205 0.4598 0.5530 -0.0299 0.2687  0.0234  169 ASN B C   
4200 O O   . ASN B 168 ? 0.9569 0.3783 0.4789 -0.0257 0.2808  0.0251  169 ASN B O   
4201 C CB  . ASN B 168 ? 1.0280 0.4562 0.5882 -0.0342 0.3047  0.0085  169 ASN B CB  
4202 C CG  . ASN B 168 ? 1.0662 0.4972 0.6428 -0.0386 0.3146  -0.0001 169 ASN B CG  
4203 O OD1 . ASN B 168 ? 1.0635 0.5154 0.6868 -0.0412 0.3242  -0.0061 169 ASN B OD1 
4204 N ND2 . ASN B 168 ? 1.1023 0.5133 0.6420 -0.0392 0.3113  -0.0012 169 ASN B ND2 
4205 N N   . LYS B 169 ? 0.9312 0.3893 0.4660 -0.0302 0.2458  0.0281  170 LYS B N   
4206 C CA  . LYS B 169 ? 0.9559 0.4138 0.4793 -0.0258 0.2340  0.0364  170 LYS B CA  
4207 C C   . LYS B 169 ? 0.9329 0.4076 0.4452 -0.0243 0.2021  0.0373  170 LYS B C   
4208 O O   . LYS B 169 ? 0.8891 0.3879 0.4231 -0.0276 0.1893  0.0309  170 LYS B O   
4209 C CB  . LYS B 169 ? 0.9327 0.4151 0.5058 -0.0266 0.2391  0.0364  170 LYS B CB  
4210 C CG  . LYS B 169 ? 1.0027 0.4720 0.5879 -0.0250 0.2653  0.0346  170 LYS B CG  
4211 C CD  . LYS B 169 ? 1.0225 0.5200 0.6639 -0.0275 0.2717  0.0318  170 LYS B CD  
4212 C CE  . LYS B 169 ? 0.9921 0.5106 0.6739 -0.0331 0.2781  0.0227  170 LYS B CE  
4213 N NZ  . LYS B 169 ? 0.9675 0.5266 0.6973 -0.0351 0.2621  0.0198  170 LYS B NZ  
4214 N N   . PRO B 170 ? 0.9187 0.3807 0.3977 -0.0193 0.1892  0.0451  171 PRO B N   
4215 C CA  . PRO B 170 ? 0.9160 0.3984 0.3925 -0.0180 0.1582  0.0456  171 PRO B CA  
4216 C C   . PRO B 170 ? 0.8241 0.3483 0.3558 -0.0205 0.1462  0.0428  171 PRO B C   
4217 O O   . PRO B 170 ? 0.8055 0.3406 0.3716 -0.0215 0.1591  0.0428  171 PRO B O   
4218 C CB  . PRO B 170 ? 0.9154 0.3746 0.3503 -0.0115 0.1511  0.0551  171 PRO B CB  
4219 C CG  . PRO B 170 ? 0.9687 0.4083 0.4038 -0.0092 0.1764  0.0580  171 PRO B CG  
4220 C CD  . PRO B 170 ? 0.9466 0.3794 0.3936 -0.0136 0.1993  0.0509  171 PRO B CD  
4221 N N   . PHE B 171 ? 0.8066 0.3541 0.3464 -0.0215 0.1213  0.0398  172 PHE B N   
4222 C CA  . PHE B 171 ? 0.7603 0.3478 0.3514 -0.0242 0.1097  0.0362  172 PHE B CA  
4223 C C   . PHE B 171 ? 0.7265 0.3242 0.3365 -0.0218 0.1081  0.0417  172 PHE B C   
4224 O O   . PHE B 171 ? 0.6875 0.3094 0.3423 -0.0242 0.1133  0.0389  172 PHE B O   
4225 C CB  . PHE B 171 ? 0.6937 0.3010 0.2855 -0.0253 0.0833  0.0330  172 PHE B CB  
4226 C CG  . PHE B 171 ? 0.6503 0.2973 0.2920 -0.0282 0.0715  0.0294  172 PHE B CG  
4227 C CD1 . PHE B 171 ? 0.6349 0.3007 0.3106 -0.0324 0.0779  0.0226  172 PHE B CD1 
4228 C CD2 . PHE B 171 ? 0.6511 0.3161 0.3057 -0.0264 0.0547  0.0329  172 PHE B CD2 
4229 C CE1 . PHE B 171 ? 0.5886 0.2901 0.3083 -0.0345 0.0673  0.0195  172 PHE B CE1 
4230 C CE2 . PHE B 171 ? 0.5803 0.2809 0.2796 -0.0290 0.0447  0.0294  172 PHE B CE2 
4231 C CZ  . PHE B 171 ? 0.5672 0.2857 0.2980 -0.0330 0.0510  0.0229  172 PHE B CZ  
4232 N N   . ASP B 172 ? 0.7436 0.3231 0.3203 -0.0168 0.1008  0.0493  173 ASP B N   
4233 C CA  . ASP B 172 ? 0.7661 0.3546 0.3603 -0.0143 0.0989  0.0547  173 ASP B CA  
4234 C C   . ASP B 172 ? 0.7689 0.3499 0.3830 -0.0151 0.1258  0.0554  173 ASP B C   
4235 O O   . ASP B 172 ? 0.7047 0.3055 0.3545 -0.0156 0.1268  0.0558  173 ASP B O   
4236 C CB  . ASP B 172 ? 0.8025 0.3691 0.3539 -0.0080 0.0875  0.0632  173 ASP B CB  
4237 C CG  . ASP B 172 ? 0.8435 0.3671 0.3477 -0.0044 0.1061  0.0686  173 ASP B CG  
4238 O OD1 . ASP B 172 ? 0.8834 0.3903 0.3654 -0.0060 0.1146  0.0650  173 ASP B OD1 
4239 O OD2 . ASP B 172 ? 0.9544 0.4603 0.4432 0.0003  0.1127  0.0766  173 ASP B OD2 
4240 N N   . GLN B 173 ? 0.7947 0.3476 0.3874 -0.0155 0.1482  0.0550  174 GLN B N   
4241 C CA  . GLN B 173 ? 0.8120 0.3577 0.4259 -0.0167 0.1751  0.0547  174 GLN B CA  
4242 C C   . GLN B 173 ? 0.7256 0.2988 0.3896 -0.0223 0.1829  0.0452  174 GLN B C   
4243 O O   . GLN B 173 ? 0.7056 0.2883 0.4046 -0.0238 0.1978  0.0433  174 GLN B O   
4244 C CB  . GLN B 173 ? 0.8481 0.3507 0.4188 -0.0147 0.1976  0.0584  174 GLN B CB  
4245 C CG  . GLN B 173 ? 0.8945 0.3685 0.4175 -0.0081 0.1928  0.0683  174 GLN B CG  
4246 C CD  . GLN B 173 ? 1.0736 0.5203 0.5764 -0.0044 0.2143  0.0673  174 GLN B CD  
4247 O OE1 . GLN B 173 ? 1.0604 0.4916 0.5460 -0.0054 0.2242  0.0623  174 GLN B OE1 
4248 N NE2 . GLN B 173 ? 1.1647 0.6047 0.6701 -0.0001 0.2220  0.0718  174 GLN B NE2 
4249 N N   . VAL B 174 ? 0.6999 0.2867 0.3692 -0.0252 0.1727  0.0390  175 VAL B N   
4250 C CA  . VAL B 174 ? 0.6481 0.2650 0.3668 -0.0297 0.1756  0.0304  175 VAL B CA  
4251 C C   . VAL B 174 ? 0.6061 0.2567 0.3670 -0.0301 0.1640  0.0299  175 VAL B C   
4252 O O   . VAL B 174 ? 0.5992 0.2658 0.4006 -0.0321 0.1759  0.0255  175 VAL B O   
4253 C CB  . VAL B 174 ? 0.7029 0.3301 0.4186 -0.0321 0.1626  0.0250  175 VAL B CB  
4254 C CG1 . VAL B 174 ? 0.5816 0.2426 0.3489 -0.0357 0.1618  0.0172  175 VAL B CG1 
4255 C CG2 . VAL B 174 ? 0.7159 0.3107 0.3953 -0.0324 0.1775  0.0240  175 VAL B CG2 
4256 N N   . LEU B 175 ? 0.6213 0.2824 0.3732 -0.0280 0.1409  0.0339  176 LEU B N   
4257 C CA  . LEU B 175 ? 0.5712 0.2636 0.3614 -0.0284 0.1295  0.0334  176 LEU B CA  
4258 C C   . LEU B 175 ? 0.5797 0.2628 0.3757 -0.0263 0.1428  0.0381  176 LEU B C   
4259 O O   . LEU B 175 ? 0.5471 0.2495 0.3845 -0.0282 0.1513  0.0342  176 LEU B O   
4260 C CB  . LEU B 175 ? 0.5346 0.2409 0.3148 -0.0272 0.1015  0.0359  176 LEU B CB  
4261 C CG  . LEU B 175 ? 0.5139 0.2387 0.3007 -0.0299 0.0858  0.0303  176 LEU B CG  
4262 C CD1 . LEU B 175 ? 0.5335 0.2770 0.3214 -0.0290 0.0596  0.0322  176 LEU B CD1 
4263 C CD2 . LEU B 175 ? 0.4786 0.2286 0.3102 -0.0336 0.0929  0.0227  176 LEU B CD2 
4264 N N   . GLU B 176 ? 0.6061 0.2592 0.3608 -0.0221 0.1449  0.0464  177 GLU B N   
4265 C CA  . GLU B 176 ? 0.6352 0.2797 0.3928 -0.0193 0.1539  0.0523  177 GLU B CA  
4266 C C   . GLU B 176 ? 0.6561 0.2855 0.4263 -0.0206 0.1840  0.0506  177 GLU B C   
4267 O O   . GLU B 176 ? 0.6476 0.2807 0.4399 -0.0201 0.1936  0.0522  177 GLU B O   
4268 C CB  . GLU B 176 ? 0.7087 0.3244 0.4160 -0.0136 0.1462  0.0622  177 GLU B CB  
4269 C CG  . GLU B 176 ? 0.6730 0.3063 0.3756 -0.0118 0.1165  0.0643  177 GLU B CG  
4270 C CD  . GLU B 176 ? 0.7411 0.3471 0.3962 -0.0054 0.1080  0.0739  177 GLU B CD  
4271 O OE1 . GLU B 176 ? 0.7053 0.3242 0.3563 -0.0035 0.0840  0.0757  177 GLU B OE1 
4272 O OE2 . GLU B 176 ? 0.7776 0.3489 0.3994 -0.0022 0.1253  0.0795  177 GLU B OE2 
4273 N N   . LYS B 177 ? 0.6562 0.2678 0.4133 -0.0223 0.2000  0.0472  178 LYS B N   
4274 C CA  . LYS B 177 ? 0.6843 0.2804 0.4539 -0.0237 0.2297  0.0451  178 LYS B CA  
4275 C C   . LYS B 177 ? 0.6756 0.2964 0.4927 -0.0286 0.2386  0.0342  178 LYS B C   
4276 O O   . LYS B 177 ? 0.6711 0.2895 0.5137 -0.0302 0.2607  0.0308  178 LYS B O   
4277 C CB  . LYS B 177 ? 0.7430 0.2959 0.4631 -0.0217 0.2470  0.0494  178 LYS B CB  
4278 C CG  . LYS B 177 ? 0.8343 0.3607 0.5105 -0.0151 0.2442  0.0588  178 LYS B CG  
4279 C CD  . LYS B 177 ? 0.8712 0.4092 0.5636 -0.0130 0.2360  0.0647  178 LYS B CD  
4280 C CE  . LYS B 177 ? 0.9188 0.4683 0.6529 -0.0134 0.2550  0.0599  178 LYS B CE  
4281 N NZ  . LYS B 177 ? 0.8959 0.4696 0.6626 -0.0145 0.2436  0.0623  178 LYS B NZ  
4282 N N   . THR B 178 ? 0.6271 0.2719 0.4581 -0.0309 0.2222  0.0285  179 THR B N   
4283 C CA  . THR B 178 ? 0.5836 0.2500 0.4568 -0.0348 0.2303  0.0185  179 THR B CA  
4284 C C   . THR B 178 ? 0.5489 0.2580 0.4652 -0.0365 0.2109  0.0133  179 THR B C   
4285 O O   . THR B 178 ? 0.5401 0.2698 0.5003 -0.0382 0.2188  0.0074  179 THR B O   
4286 C CB  . THR B 178 ? 0.6847 0.3379 0.5367 -0.0362 0.2334  0.0153  179 THR B CB  
4287 O OG1 . THR B 178 ? 0.7283 0.3412 0.5425 -0.0350 0.2546  0.0192  179 THR B OG1 
4288 C CG2 . THR B 178 ? 0.6396 0.3156 0.5355 -0.0397 0.2404  0.0051  179 THR B CG2 
4289 N N   . ILE B 179 ? 0.5529 0.2756 0.4580 -0.0359 0.1859  0.0152  180 ILE B N   
4290 C CA  . ILE B 179 ? 0.5069 0.2688 0.4505 -0.0376 0.1680  0.0100  180 ILE B CA  
4291 C C   . ILE B 179 ? 0.4848 0.2653 0.4506 -0.0368 0.1599  0.0120  180 ILE B C   
4292 O O   . ILE B 179 ? 0.4500 0.2588 0.4595 -0.0385 0.1594  0.0060  180 ILE B O   
4293 C CB  . ILE B 179 ? 0.4679 0.2364 0.3921 -0.0377 0.1461  0.0106  180 ILE B CB  
4294 C CG1 . ILE B 179 ? 0.4949 0.2470 0.4022 -0.0389 0.1556  0.0074  180 ILE B CG1 
4295 C CG2 . ILE B 179 ? 0.4413 0.2490 0.4024 -0.0392 0.1271  0.0062  180 ILE B CG2 
4296 C CD1 . ILE B 179 ? 0.4759 0.2440 0.4226 -0.0414 0.1678  -0.0011 180 ILE B CD1 
4297 N N   . PHE B 180 ? 0.4592 0.2249 0.3960 -0.0339 0.1526  0.0202  181 PHE B N   
4298 C CA  . PHE B 180 ? 0.4522 0.2349 0.4104 -0.0331 0.1453  0.0222  181 PHE B CA  
4299 C C   . PHE B 180 ? 0.4908 0.2759 0.4813 -0.0342 0.1665  0.0187  181 PHE B C   
4300 O O   . PHE B 180 ? 0.4434 0.2580 0.4744 -0.0357 0.1616  0.0138  181 PHE B O   
4301 C CB  . PHE B 180 ? 0.4925 0.2554 0.4128 -0.0293 0.1359  0.0320  181 PHE B CB  
4302 C CG  . PHE B 180 ? 0.4541 0.2214 0.3505 -0.0283 0.1114  0.0344  181 PHE B CG  
4303 C CD1 . PHE B 180 ? 0.4492 0.2427 0.3649 -0.0312 0.0971  0.0283  181 PHE B CD1 
4304 C CD2 . PHE B 180 ? 0.5137 0.2587 0.3688 -0.0244 0.1027  0.0426  181 PHE B CD2 
4305 C CE1 . PHE B 180 ? 0.4653 0.2623 0.3603 -0.0306 0.0755  0.0300  181 PHE B CE1 
4306 C CE2 . PHE B 180 ? 0.5027 0.2522 0.3376 -0.0236 0.0800  0.0439  181 PHE B CE2 
4307 C CZ  . PHE B 180 ? 0.4713 0.2470 0.3270 -0.0270 0.0668  0.0373  181 PHE B CZ  
4308 N N   . PRO B 181 ? 0.5159 0.2719 0.4921 -0.0336 0.1904  0.0202  182 PRO B N   
4309 C CA  . PRO B 181 ? 0.4922 0.2523 0.5033 -0.0350 0.2109  0.0159  182 PRO B CA  
4310 C C   . PRO B 181 ? 0.5191 0.3069 0.5767 -0.0385 0.2153  0.0045  182 PRO B C   
4311 O O   . PRO B 181 ? 0.5115 0.3204 0.6102 -0.0399 0.2200  -0.0011 182 PRO B O   
4312 C CB  . PRO B 181 ? 0.5751 0.2941 0.5543 -0.0335 0.2356  0.0205  182 PRO B CB  
4313 C CG  . PRO B 181 ? 0.5749 0.2685 0.4990 -0.0303 0.2245  0.0295  182 PRO B CG  
4314 C CD  . PRO B 181 ? 0.5317 0.2489 0.4587 -0.0315 0.2005  0.0261  182 PRO B CD  
4315 N N   . ALA B 182 ? 0.5194 0.3083 0.5722 -0.0397 0.2134  0.0005  183 ALA B N   
4316 C CA  . ALA B 182 ? 0.4227 0.2395 0.5192 -0.0422 0.2147  -0.0100 183 ALA B CA  
4317 C C   . ALA B 182 ? 0.4440 0.2994 0.5734 -0.0428 0.1937  -0.0135 183 ALA B C   
4318 O O   . ALA B 182 ? 0.4360 0.3167 0.6090 -0.0443 0.1968  -0.0221 183 ALA B O   
4319 C CB  . ALA B 182 ? 0.5032 0.3138 0.5849 -0.0429 0.2135  -0.0124 183 ALA B CB  
4320 N N   . LEU B 183 ? 0.3997 0.2599 0.5091 -0.0415 0.1726  -0.0073 184 LEU B N   
4321 C CA  . LEU B 183 ? 0.3815 0.2765 0.5183 -0.0421 0.1524  -0.0101 184 LEU B CA  
4322 C C   . LEU B 183 ? 0.4046 0.3079 0.5593 -0.0418 0.1534  -0.0088 184 LEU B C   
4323 O O   . LEU B 183 ? 0.3845 0.3160 0.5624 -0.0424 0.1377  -0.0112 184 LEU B O   
4324 C CB  . LEU B 183 ? 0.3879 0.2854 0.4973 -0.0412 0.1291  -0.0049 184 LEU B CB  
4325 C CG  . LEU B 183 ? 0.3761 0.2739 0.4747 -0.0419 0.1232  -0.0073 184 LEU B CG  
4326 C CD1 . LEU B 183 ? 0.3737 0.2668 0.4393 -0.0410 0.1031  -0.0013 184 LEU B CD1 
4327 C CD2 . LEU B 183 ? 0.3612 0.2918 0.5010 -0.0434 0.1177  -0.0159 184 LEU B CD2 
4328 N N   . GLY B 184 ? 0.4059 0.2846 0.5498 -0.0408 0.1718  -0.0051 185 GLY B N   
4329 C CA  . GLY B 184 ? 0.4067 0.2905 0.5667 -0.0405 0.1746  -0.0036 185 GLY B CA  
4330 C C   . GLY B 184 ? 0.4333 0.3121 0.5672 -0.0381 0.1578  0.0055  185 GLY B C   
4331 O O   . GLY B 184 ? 0.4407 0.3330 0.5940 -0.0381 0.1537  0.0057  185 GLY B O   
4332 N N   . LEU B 185 ? 0.4036 0.2634 0.4949 -0.0361 0.1480  0.0125  186 LEU B N   
4333 C CA  . LEU B 185 ? 0.4009 0.2559 0.4669 -0.0335 0.1307  0.0207  186 LEU B CA  
4334 C C   . LEU B 185 ? 0.4855 0.3070 0.5220 -0.0301 0.1437  0.0295  186 LEU B C   
4335 O O   . LEU B 185 ? 0.5608 0.3527 0.5720 -0.0290 0.1606  0.0321  186 LEU B O   
4336 C CB  . LEU B 185 ? 0.4173 0.2692 0.4528 -0.0328 0.1125  0.0233  186 LEU B CB  
4337 C CG  . LEU B 185 ? 0.4099 0.2877 0.4684 -0.0359 0.1039  0.0152  186 LEU B CG  
4338 C CD1 . LEU B 185 ? 0.3842 0.2581 0.4123 -0.0353 0.0858  0.0179  186 LEU B CD1 
4339 C CD2 . LEU B 185 ? 0.3930 0.3081 0.4964 -0.0380 0.0947  0.0089  186 LEU B CD2 
4340 N N   . LYS B 186 ? 0.4532 0.2787 0.4925 -0.0282 0.1360  0.0342  187 LYS B N   
4341 C CA  . LYS B 186 ? 0.4849 0.2804 0.5003 -0.0245 0.1483  0.0428  187 LYS B CA  
4342 C C   . LYS B 186 ? 0.4748 0.2519 0.4463 -0.0198 0.1322  0.0529  187 LYS B C   
4343 O O   . LYS B 186 ? 0.5146 0.2593 0.4538 -0.0157 0.1428  0.0612  187 LYS B O   
4344 C CB  . LYS B 186 ? 0.5315 0.3413 0.5825 -0.0251 0.1546  0.0413  187 LYS B CB  
4345 C CG  . LYS B 186 ? 0.5760 0.4143 0.6785 -0.0298 0.1635  0.0296  187 LYS B CG  
4346 C CD  . LYS B 186 ? 0.5435 0.3645 0.6523 -0.0311 0.1909  0.0259  187 LYS B CD  
4347 C CE  . LYS B 186 ? 0.5964 0.4385 0.7561 -0.0342 0.2037  0.0171  187 LYS B CE  
4348 N NZ  . LYS B 186 ? 0.7005 0.5831 0.8958 -0.0365 0.1840  0.0104  187 LYS B NZ  
4349 N N   . HIS B 187 ? 0.4775 0.2740 0.4475 -0.0201 0.1073  0.0523  188 HIS B N   
4350 C CA  . HIS B 187 ? 0.4502 0.2336 0.3843 -0.0156 0.0897  0.0607  188 HIS B CA  
4351 C C   . HIS B 187 ? 0.4509 0.2450 0.3720 -0.0168 0.0692  0.0582  188 HIS B C   
4352 O O   . HIS B 187 ? 0.4377 0.2456 0.3576 -0.0160 0.0476  0.0595  188 HIS B O   
4353 C CB  . HIS B 187 ? 0.4489 0.2470 0.4018 -0.0142 0.0796  0.0635  188 HIS B CB  
4354 C CG  . HIS B 187 ? 0.4739 0.2577 0.4351 -0.0125 0.0996  0.0671  188 HIS B CG  
4355 N ND1 . HIS B 187 ? 0.5114 0.3156 0.5180 -0.0161 0.1114  0.0604  188 HIS B ND1 
4356 C CD2 . HIS B 187 ? 0.5427 0.2925 0.4722 -0.0074 0.1110  0.0764  188 HIS B CD2 
4357 C CE1 . HIS B 187 ? 0.5051 0.2891 0.5092 -0.0138 0.1294  0.0652  188 HIS B CE1 
4358 N NE2 . HIS B 187 ? 0.5449 0.2952 0.5020 -0.0083 0.1298  0.0754  188 HIS B NE2 
4359 N N   . SER B 188 ? 0.4797 0.2672 0.3921 -0.0189 0.0768  0.0542  189 SER B N   
4360 C CA  . SER B 188 ? 0.4531 0.2449 0.3485 -0.0198 0.0607  0.0520  189 SER B CA  
4361 C C   . SER B 188 ? 0.5267 0.2818 0.3724 -0.0167 0.0669  0.0573  189 SER B C   
4362 O O   . SER B 188 ? 0.5798 0.3114 0.4141 -0.0160 0.0889  0.0587  189 SER B O   
4363 C CB  . SER B 188 ? 0.4403 0.2562 0.3678 -0.0248 0.0630  0.0426  189 SER B CB  
4364 O OG  . SER B 188 ? 0.3807 0.2300 0.3514 -0.0273 0.0560  0.0379  189 SER B OG  
4365 N N   . TYR B 189 ? 0.5177 0.2671 0.3334 -0.0146 0.0479  0.0599  190 TYR B N   
4366 C CA  . TYR B 189 ? 0.5786 0.2921 0.3429 -0.0105 0.0505  0.0659  190 TYR B CA  
4367 C C   . TYR B 189 ? 0.5786 0.2936 0.3220 -0.0113 0.0337  0.0629  190 TYR B C   
4368 O O   . TYR B 189 ? 0.5647 0.3065 0.3276 -0.0136 0.0148  0.0588  190 TYR B O   
4369 C CB  . TYR B 189 ? 0.5997 0.2958 0.3382 -0.0044 0.0436  0.0751  190 TYR B CB  
4370 C CG  . TYR B 189 ? 0.5854 0.2809 0.3447 -0.0031 0.0574  0.0788  190 TYR B CG  
4371 C CD1 . TYR B 189 ? 0.6213 0.2887 0.3664 -0.0013 0.0822  0.0827  190 TYR B CD1 
4372 C CD2 . TYR B 189 ? 0.5930 0.3156 0.3864 -0.0038 0.0462  0.0780  190 TYR B CD2 
4373 C CE1 . TYR B 189 ? 0.6332 0.2996 0.3984 -0.0003 0.0958  0.0857  190 TYR B CE1 
4374 C CE2 . TYR B 189 ? 0.5404 0.2627 0.3540 -0.0028 0.0591  0.0808  190 TYR B CE2 
4375 C CZ  . TYR B 189 ? 0.6198 0.3139 0.4195 -0.0011 0.0839  0.0846  190 TYR B CZ  
4376 O OH  . TYR B 189 ? 0.6040 0.2972 0.4248 -0.0002 0.0978  0.0872  190 TYR B OH  
4377 N N   . VAL B 190 ? 0.6180 0.3032 0.3214 -0.0096 0.0416  0.0647  191 VAL B N   
4378 C CA  . VAL B 190 ? 0.6360 0.3138 0.3071 -0.0085 0.0241  0.0642  191 VAL B CA  
4379 C C   . VAL B 190 ? 0.6824 0.3391 0.3150 -0.0019 0.0125  0.0722  191 VAL B C   
4380 O O   . VAL B 190 ? 0.7039 0.3681 0.3258 -0.0005 -0.0102 0.0718  191 VAL B O   
4381 C CB  . VAL B 190 ? 0.6917 0.3502 0.3406 -0.0103 0.0373  0.0607  191 VAL B CB  
4382 C CG1 . VAL B 190 ? 0.6575 0.3054 0.2698 -0.0089 0.0200  0.0600  191 VAL B CG1 
4383 C CG2 . VAL B 190 ? 0.6038 0.2865 0.2932 -0.0164 0.0451  0.0524  191 VAL B CG2 
4384 N N   . ASN B 191 ? 0.7015 0.3317 0.3138 0.0024  0.0279  0.0796  192 ASN B N   
4385 C CA  . ASN B 191 ? 0.7240 0.3338 0.3021 0.0095  0.0183  0.0883  192 ASN B CA  
4386 C C   . ASN B 191 ? 0.6928 0.3072 0.2944 0.0114  0.0265  0.0935  192 ASN B C   
4387 O O   . ASN B 191 ? 0.7520 0.3522 0.3578 0.0112  0.0505  0.0957  192 ASN B O   
4388 C CB  . ASN B 191 ? 0.7760 0.3442 0.2994 0.0140  0.0291  0.0934  192 ASN B CB  
4389 C CG  . ASN B 191 ? 0.8022 0.3656 0.3039 0.0116  0.0229  0.0873  192 ASN B CG  
4390 O OD1 . ASN B 191 ? 0.8746 0.4456 0.3639 0.0127  -0.0002 0.0853  192 ASN B OD1 
4391 N ND2 . ASN B 191 ? 0.8598 0.4112 0.3586 0.0082  0.0439  0.0838  192 ASN B ND2 
4392 N N   . VAL B 192 ? 0.7131 0.3475 0.3315 0.0130  0.0071  0.0950  193 VAL B N   
4393 C CA  . VAL B 192 ? 0.6903 0.3313 0.3329 0.0148  0.0125  0.0995  193 VAL B CA  
4394 C C   . VAL B 192 ? 0.7758 0.3792 0.3775 0.0225  0.0217  0.1103  193 VAL B C   
4395 O O   . VAL B 192 ? 0.7769 0.3629 0.3393 0.0284  0.0067  0.1153  193 VAL B O   
4396 C CB  . VAL B 192 ? 0.7096 0.3813 0.3794 0.0145  -0.0115 0.0979  193 VAL B CB  
4397 C CG1 . VAL B 192 ? 0.6896 0.3636 0.3779 0.0173  -0.0068 0.1035  193 VAL B CG1 
4398 C CG2 . VAL B 192 ? 0.6012 0.3095 0.3139 0.0068  -0.0171 0.0876  193 VAL B CG2 
4399 N N   . PRO B 193 ? 0.7942 0.3838 0.4033 0.0229  0.0459  0.1139  194 PRO B N   
4400 C CA  . PRO B 193 ? 0.8073 0.3589 0.3762 0.0305  0.0564  0.1249  194 PRO B CA  
4401 C C   . PRO B 193 ? 0.8335 0.3887 0.4039 0.0363  0.0413  0.1320  194 PRO B C   
4402 O O   . PRO B 193 ? 0.8072 0.3946 0.4179 0.0336  0.0291  0.1284  194 PRO B O   
4403 C CB  . PRO B 193 ? 0.8616 0.4025 0.4476 0.0278  0.0881  0.1249  194 PRO B CB  
4404 C CG  . PRO B 193 ? 0.7377 0.3186 0.3833 0.0201  0.0888  0.1152  194 PRO B CG  
4405 C CD  . PRO B 193 ? 0.7255 0.3319 0.3787 0.0165  0.0660  0.1077  194 PRO B CD  
4406 N N   . LYS B 194 ? 0.8670 0.3985 0.4026 0.0438  0.0415  0.1385  195 LYS B N   
4407 C CA  . LYS B 194 ? 0.8934 0.4297 0.4301 0.0499  0.0260  0.1444  195 LYS B CA  
4408 C C   . LYS B 194 ? 0.8989 0.4425 0.4710 0.0490  0.0377  0.1484  195 LYS B C   
4409 O O   . LYS B 194 ? 0.9048 0.4626 0.4930 0.0514  0.0219  0.1513  195 LYS B O   
4410 C CB  . LYS B 194 ? 0.9283 0.4404 0.4259 0.0576  0.0271  0.1490  195 LYS B CB  
4411 C CG  . LYS B 194 ? 1.0716 0.5797 0.5371 0.0592  0.0108  0.1445  195 LYS B CG  
4412 C CD  . LYS B 194 ? 1.0874 0.6229 0.5663 0.0587  -0.0193 0.1405  195 LYS B CD  
4413 C CE  . LYS B 194 ? 1.1367 0.6802 0.6239 0.0646  -0.0337 0.1461  195 LYS B CE  
4414 N NZ  . LYS B 194 ? 1.1650 0.7299 0.6551 0.0655  -0.0622 0.1407  195 LYS B NZ  
4415 N N   . THR B 195 ? 0.8598 0.3959 0.4479 0.0451  0.0653  0.1473  196 THR B N   
4416 C CA  . THR B 195 ? 0.8424 0.3880 0.4695 0.0433  0.0784  0.1490  196 THR B CA  
4417 C C   . THR B 195 ? 0.8142 0.4061 0.4950 0.0364  0.0640  0.1390  196 THR B C   
4418 O O   . THR B 195 ? 0.7501 0.3592 0.4699 0.0343  0.0701  0.1378  196 THR B O   
4419 C CB  . THR B 195 ? 0.8764 0.4122 0.5166 0.0395  0.1102  0.1457  196 THR B CB  
4420 O OG1 . THR B 195 ? 0.8589 0.4090 0.5183 0.0317  0.1159  0.1365  196 THR B OG1 
4421 C CG2 . THR B 195 ? 0.9354 0.4418 0.5340 0.0446  0.1214  0.1486  196 THR B CG2 
4422 N N   . GLN B 196 ? 0.7747 0.3869 0.4581 0.0327  0.0456  0.1318  197 GLN B N   
4423 C CA  . GLN B 196 ? 0.7716 0.4266 0.5022 0.0263  0.0313  0.1224  197 GLN B CA  
4424 C C   . GLN B 196 ? 0.7656 0.4353 0.4918 0.0291  0.0013  0.1232  197 GLN B C   
4425 O O   . GLN B 196 ? 0.6924 0.3963 0.4532 0.0240  -0.0125 0.1155  197 GLN B O   
4426 C CB  . GLN B 196 ? 0.6779 0.3476 0.4215 0.0192  0.0351  0.1124  197 GLN B CB  
4427 C CG  . GLN B 196 ? 0.6379 0.3086 0.4074 0.0143  0.0620  0.1078  197 GLN B CG  
4428 C CD  . GLN B 196 ? 0.6600 0.3576 0.4803 0.0110  0.0667  0.1040  197 GLN B CD  
4429 O OE1 . GLN B 196 ? 0.6127 0.3423 0.4626 0.0082  0.0492  0.0991  197 GLN B OE1 
4430 N NE2 . GLN B 196 ? 0.6680 0.3523 0.4986 0.0111  0.0909  0.1060  197 GLN B NE2 
4431 N N   . MET B 197 ? 0.8793 0.5238 0.5641 0.0373  -0.0092 0.1322  198 MET B N   
4432 C CA  . MET B 197 ? 0.9063 0.5633 0.5832 0.0399  -0.0386 0.1316  198 MET B CA  
4433 C C   . MET B 197 ? 0.8173 0.5016 0.5326 0.0395  -0.0514 0.1309  198 MET B C   
4434 O O   . MET B 197 ? 0.8281 0.5340 0.5535 0.0385  -0.0746 0.1267  198 MET B O   
4435 C CB  . MET B 197 ? 0.9598 0.5819 0.5803 0.0492  -0.0471 0.1407  198 MET B CB  
4436 C CG  . MET B 197 ? 1.0408 0.6455 0.6254 0.0485  -0.0431 0.1378  198 MET B CG  
4437 S SD  . MET B 197 ? 1.0324 0.6643 0.6307 0.0409  -0.0605 0.1261  198 MET B SD  
4438 C CE  . MET B 197 ? 0.9876 0.5916 0.5431 0.0409  -0.0473 0.1243  198 MET B CE  
4439 N N   . GLN B 198 ? 0.6952 0.3802 0.4342 0.0397  -0.0362 0.1341  199 GLN B N   
4440 C CA  . GLN B 198 ? 0.6861 0.4009 0.4673 0.0378  -0.0468 0.1314  199 GLN B CA  
4441 C C   . GLN B 198 ? 0.6503 0.4038 0.4765 0.0283  -0.0502 0.1194  199 GLN B C   
4442 O O   . GLN B 198 ? 0.5893 0.3705 0.4482 0.0261  -0.0634 0.1156  199 GLN B O   
4443 C CB  . GLN B 198 ? 0.7138 0.4199 0.5109 0.0401  -0.0288 0.1372  199 GLN B CB  
4444 C CG  . GLN B 198 ? 0.7322 0.4450 0.5593 0.0335  -0.0029 0.1318  199 GLN B CG  
4445 C CD  . GLN B 198 ? 0.8323 0.5103 0.6264 0.0355  0.0203  0.1362  199 GLN B CD  
4446 O OE1 . GLN B 198 ? 0.8106 0.4648 0.5604 0.0394  0.0160  0.1402  199 GLN B OE1 
4447 N NE2 . GLN B 198 ? 0.8439 0.5186 0.6603 0.0327  0.0454  0.1352  199 GLN B NE2 
4448 N N   . ASN B 199 ? 0.6165 0.3719 0.4444 0.0230  -0.0387 0.1133  200 ASN B N   
4449 C CA  . ASN B 199 ? 0.5386 0.3286 0.4068 0.0146  -0.0405 0.1024  200 ASN B CA  
4450 C C   . ASN B 199 ? 0.5487 0.3496 0.4064 0.0122  -0.0587 0.0970  200 ASN B C   
4451 O O   . ASN B 199 ? 0.4727 0.3022 0.3614 0.0057  -0.0627 0.0883  200 ASN B O   
4452 C CB  . ASN B 199 ? 0.5089 0.2971 0.3927 0.0100  -0.0152 0.0982  200 ASN B CB  
4453 C CG  . ASN B 199 ? 0.5743 0.3581 0.4790 0.0108  0.0036  0.1012  200 ASN B CG  
4454 O OD1 . ASN B 199 ? 0.5166 0.3167 0.4471 0.0110  -0.0029 0.1014  200 ASN B OD1 
4455 N ND2 . ASN B 199 ? 0.5776 0.3389 0.4719 0.0111  0.0276  0.1031  200 ASN B ND2 
4456 N N   . TYR B 200 ? 0.6107 0.3895 0.4257 0.0174  -0.0700 0.1018  201 TYR B N   
4457 C CA  . TYR B 200 ? 0.6357 0.4189 0.4352 0.0152  -0.0835 0.0966  201 TYR B CA  
4458 C C   . TYR B 200 ? 0.7455 0.5248 0.5225 0.0204  -0.1082 0.0996  201 TYR B C   
4459 O O   . TYR B 200 ? 0.8134 0.5636 0.5510 0.0276  -0.1099 0.1073  201 TYR B O   
4460 C CB  . TYR B 200 ? 0.6229 0.3792 0.3890 0.0156  -0.0684 0.0977  201 TYR B CB  
4461 C CG  . TYR B 200 ? 0.6981 0.4555 0.4454 0.0136  -0.0806 0.0925  201 TYR B CG  
4462 C CD1 . TYR B 200 ? 0.6584 0.4470 0.4345 0.0078  -0.0939 0.0840  201 TYR B CD1 
4463 C CD2 . TYR B 200 ? 0.7027 0.4290 0.4031 0.0174  -0.0778 0.0959  201 TYR B CD2 
4464 C CE1 . TYR B 200 ? 0.6630 0.4520 0.4229 0.0058  -0.1040 0.0792  201 TYR B CE1 
4465 C CE2 . TYR B 200 ? 0.6932 0.4204 0.3773 0.0153  -0.0883 0.0906  201 TYR B CE2 
4466 C CZ  . TYR B 200 ? 0.6620 0.4207 0.3766 0.0095  -0.1013 0.0823  201 TYR B CZ  
4467 O OH  . TYR B 200 ? 0.6481 0.4071 0.3475 0.0073  -0.1110 0.0769  201 TYR B OH  
4468 N N   . ALA B 201 ? 0.8794 0.6875 0.6812 0.0168  -0.1271 0.0933  202 ALA B N   
4469 C CA  . ALA B 201 ? 1.0037 0.8127 0.7904 0.0208  -0.1519 0.0941  202 ALA B CA  
4470 C C   . ALA B 201 ? 0.9782 0.7671 0.7245 0.0245  -0.1524 0.0931  202 ALA B C   
4471 O O   . ALA B 201 ? 0.9662 0.7645 0.7115 0.0206  -0.1563 0.0850  202 ALA B O   
4472 C CB  . ALA B 201 ? 0.9566 0.8046 0.7822 0.0140  -0.1628 0.0823  202 ALA B CB  
4473 N N   . GLY B 216 ? 1.0902 0.8132 0.6629 -0.0054 -0.1371 0.0253  217 GLY B N   
4474 C CA  . GLY B 216 ? 1.0308 0.7480 0.5924 -0.0081 -0.1354 0.0192  217 GLY B CA  
4475 C C   . GLY B 216 ? 1.0063 0.6931 0.5340 -0.0091 -0.1192 0.0210  217 GLY B C   
4476 O O   . GLY B 216 ? 0.9983 0.6687 0.5124 -0.0079 -0.1071 0.0273  217 GLY B O   
4477 N N   . PRO B 217 ? 1.0339 0.7130 0.5488 -0.0114 -0.1169 0.0154  218 PRO B N   
4478 C CA  . PRO B 217 ? 0.9948 0.6451 0.4787 -0.0126 -0.0993 0.0161  218 PRO B CA  
4479 C C   . PRO B 217 ? 0.9656 0.6202 0.4634 -0.0185 -0.0883 0.0154  218 PRO B C   
4480 O O   . PRO B 217 ? 0.9364 0.6166 0.4659 -0.0228 -0.0963 0.0114  218 PRO B O   
4481 C CB  . PRO B 217 ? 1.0661 0.7114 0.5371 -0.0135 -0.1030 0.0093  218 PRO B CB  
4482 C CG  . PRO B 217 ? 1.0148 0.6930 0.5221 -0.0160 -0.1189 0.0038  218 PRO B CG  
4483 C CD  . PRO B 217 ? 1.0485 0.7453 0.5785 -0.0130 -0.1287 0.0079  218 PRO B CD  
4484 N N   . LEU B 218 ? 0.9475 0.5767 0.4221 -0.0185 -0.0682 0.0196  219 LEU B N   
4485 C CA  . LEU B 218 ? 0.9256 0.5624 0.4240 -0.0235 -0.0521 0.0186  219 LEU B CA  
4486 C C   . LEU B 218 ? 0.8557 0.5261 0.4017 -0.0251 -0.0592 0.0196  219 LEU B C   
4487 O O   . LEU B 218 ? 0.7718 0.4638 0.3541 -0.0296 -0.0544 0.0157  219 LEU B O   
4488 C CB  . LEU B 218 ? 0.9386 0.5779 0.4412 -0.0285 -0.0484 0.0106  219 LEU B CB  
4489 C CG  . LEU B 218 ? 0.9562 0.5744 0.4481 -0.0297 -0.0227 0.0101  219 LEU B CG  
4490 C CD1 . LEU B 218 ? 0.8443 0.4654 0.3420 -0.0345 -0.0192 0.0022  219 LEU B CD1 
4491 C CD2 . LEU B 218 ? 0.8650 0.4939 0.3905 -0.0302 -0.0063 0.0138  219 LEU B CD2 
4492 N N   . GLY B 219 ? 0.8077 0.4822 0.3532 -0.0213 -0.0705 0.0248  220 GLY B N   
4493 C CA  . GLY B 219 ? 0.7554 0.4614 0.3423 -0.0227 -0.0805 0.0252  220 GLY B CA  
4494 C C   . GLY B 219 ? 0.6854 0.4021 0.3043 -0.0235 -0.0643 0.0284  220 GLY B C   
4495 O O   . GLY B 219 ? 0.6176 0.3632 0.2766 -0.0267 -0.0684 0.0260  220 GLY B O   
4496 N N   . ALA B 220 ? 0.6476 0.3414 0.2494 -0.0208 -0.0459 0.0335  221 ALA B N   
4497 C CA  . ALA B 220 ? 0.6146 0.3176 0.2468 -0.0213 -0.0304 0.0362  221 ALA B CA  
4498 C C   . ALA B 220 ? 0.5985 0.3264 0.2732 -0.0266 -0.0227 0.0303  221 ALA B C   
4499 O O   . ALA B 220 ? 0.5391 0.2914 0.2507 -0.0277 -0.0243 0.0304  221 ALA B O   
4500 C CB  . ALA B 220 ? 0.6215 0.2923 0.2262 -0.0181 -0.0090 0.0413  221 ALA B CB  
4501 N N   . PRO B 221 ? 0.5746 0.2984 0.2470 -0.0296 -0.0148 0.0251  222 PRO B N   
4502 C CA  . PRO B 221 ? 0.5553 0.3041 0.2695 -0.0339 -0.0091 0.0199  222 PRO B CA  
4503 C C   . PRO B 221 ? 0.4934 0.2733 0.2352 -0.0362 -0.0287 0.0166  222 PRO B C   
4504 O O   . PRO B 221 ? 0.4696 0.2734 0.2492 -0.0387 -0.0259 0.0137  222 PRO B O   
4505 C CB  . PRO B 221 ? 0.5826 0.3157 0.2816 -0.0359 0.0024  0.0155  222 PRO B CB  
4506 C CG  . PRO B 221 ? 0.6043 0.3021 0.2568 -0.0328 0.0098  0.0191  222 PRO B CG  
4507 C CD  . PRO B 221 ? 0.6305 0.3259 0.2633 -0.0292 -0.0087 0.0237  222 PRO B CD  
4508 N N   . ALA B 222 ? 0.4901 0.2704 0.2147 -0.0354 -0.0483 0.0168  223 ALA B N   
4509 C CA  . ALA B 222 ? 0.4791 0.2877 0.2296 -0.0378 -0.0661 0.0134  223 ALA B CA  
4510 C C   . ALA B 222 ? 0.4641 0.2896 0.2325 -0.0363 -0.0772 0.0169  223 ALA B C   
4511 O O   . ALA B 222 ? 0.4165 0.2695 0.2183 -0.0387 -0.0849 0.0145  223 ALA B O   
4512 C CB  . ALA B 222 ? 0.5262 0.3283 0.2528 -0.0385 -0.0812 0.0100  223 ALA B CB  
4513 N N   . TYR B 223 ? 0.5260 0.3351 0.2727 -0.0321 -0.0777 0.0225  224 TYR B N   
4514 C CA  . TYR B 223 ? 0.5038 0.3289 0.2670 -0.0306 -0.0900 0.0255  224 TYR B CA  
4515 C C   . TYR B 223 ? 0.5174 0.3247 0.2640 -0.0258 -0.0837 0.0326  224 TYR B C   
4516 O O   . TYR B 223 ? 0.5504 0.3661 0.3026 -0.0237 -0.0962 0.0355  224 TYR B O   
4517 C CB  . TYR B 223 ? 0.4940 0.3267 0.2494 -0.0306 -0.1133 0.0234  224 TYR B CB  
4518 C CG  . TYR B 223 ? 0.5394 0.3464 0.2513 -0.0282 -0.1194 0.0232  224 TYR B CG  
4519 C CD1 . TYR B 223 ? 0.6410 0.4241 0.3194 -0.0227 -0.1203 0.0289  224 TYR B CD1 
4520 C CD2 . TYR B 223 ? 0.6055 0.4122 0.3095 -0.0312 -0.1245 0.0171  224 TYR B CD2 
4521 C CE1 . TYR B 223 ? 0.7112 0.4747 0.3561 -0.0199 -0.1240 0.0275  224 TYR B CE1 
4522 C CE2 . TYR B 223 ? 0.6767 0.4654 0.3514 -0.0284 -0.1264 0.0155  224 TYR B CE2 
4523 C CZ  . TYR B 223 ? 0.7754 0.5441 0.4227 -0.0228 -0.1259 0.0203  224 TYR B CZ  
4524 O OH  . TYR B 223 ? 0.8201 0.5740 0.4429 -0.0199 -0.1273 0.0181  224 TYR B OH  
4525 N N   . GLY B 224 ? 0.5301 0.3134 0.2580 -0.0240 -0.0646 0.0356  225 GLY B N   
4526 C CA  . GLY B 224 ? 0.5476 0.3086 0.2520 -0.0189 -0.0589 0.0429  225 GLY B CA  
4527 C C   . GLY B 224 ? 0.5332 0.2982 0.2611 -0.0183 -0.0436 0.0464  225 GLY B C   
4528 O O   . GLY B 224 ? 0.5668 0.3090 0.2724 -0.0140 -0.0350 0.0528  225 GLY B O   
4529 N N   . VAL B 225 ? 0.4683 0.2610 0.2399 -0.0222 -0.0399 0.0423  226 VAL B N   
4530 C CA  . VAL B 225 ? 0.4691 0.2667 0.2656 -0.0221 -0.0246 0.0442  226 VAL B CA  
4531 C C   . VAL B 225 ? 0.4421 0.2570 0.2576 -0.0207 -0.0372 0.0469  226 VAL B C   
4532 O O   . VAL B 225 ? 0.4500 0.2866 0.2796 -0.0222 -0.0558 0.0443  226 VAL B O   
4533 C CB  . VAL B 225 ? 0.4483 0.2655 0.2815 -0.0267 -0.0126 0.0377  226 VAL B CB  
4534 C CG1 . VAL B 225 ? 0.4187 0.2442 0.2817 -0.0268 0.0016  0.0383  226 VAL B CG1 
4535 C CG2 . VAL B 225 ? 0.4561 0.2537 0.2704 -0.0277 0.0018  0.0353  226 VAL B CG2 
4536 N N   . LYS B 226 ? 0.4428 0.2471 0.2587 -0.0178 -0.0260 0.0521  227 LYS B N   
4537 C CA  . LYS B 226 ? 0.4370 0.2562 0.2744 -0.0165 -0.0332 0.0548  227 LYS B CA  
4538 C C   . LYS B 226 ? 0.4187 0.2497 0.2919 -0.0187 -0.0155 0.0527  227 LYS B C   
4539 O O   . LYS B 226 ? 0.4546 0.2694 0.3232 -0.0188 0.0050  0.0528  227 LYS B O   
4540 C CB  . LYS B 226 ? 0.4797 0.2732 0.2830 -0.0102 -0.0366 0.0634  227 LYS B CB  
4541 C CG  . LYS B 226 ? 0.5227 0.3141 0.3018 -0.0075 -0.0606 0.0650  227 LYS B CG  
4542 C CD  . LYS B 226 ? 0.6007 0.3778 0.3481 -0.0078 -0.0650 0.0625  227 LYS B CD  
4543 C CE  . LYS B 226 ? 0.5989 0.3385 0.3043 -0.0039 -0.0499 0.0677  227 LYS B CE  
4544 N NZ  . LYS B 226 ? 0.6156 0.3378 0.2827 -0.0029 -0.0582 0.0662  227 LYS B NZ  
4545 N N   . SER B 227 ? 0.3974 0.2561 0.3068 -0.0205 -0.0226 0.0504  228 SER B N   
4546 C CA  . SER B 227 ? 0.3714 0.2435 0.3171 -0.0229 -0.0065 0.0470  228 SER B CA  
4547 C C   . SER B 227 ? 0.3506 0.2442 0.3255 -0.0231 -0.0145 0.0472  228 SER B C   
4548 O O   . SER B 227 ? 0.3419 0.2411 0.3106 -0.0215 -0.0325 0.0498  228 SER B O   
4549 C CB  . SER B 227 ? 0.3456 0.2371 0.3165 -0.0276 -0.0023 0.0387  228 SER B CB  
4550 O OG  . SER B 227 ? 0.3662 0.2676 0.3694 -0.0294 0.0146  0.0348  228 SER B OG  
4551 N N   . THR B 228 ? 0.3147 0.2206 0.3228 -0.0251 -0.0006 0.0438  229 THR B N   
4552 C CA  . THR B 228 ? 0.2808 0.2084 0.3211 -0.0259 -0.0049 0.0426  229 THR B CA  
4553 C C   . THR B 228 ? 0.2495 0.2111 0.3309 -0.0308 -0.0072 0.0334  229 THR B C   
4554 O O   . THR B 228 ? 0.2661 0.2319 0.3541 -0.0331 -0.0004 0.0283  229 THR B O   
4555 C CB  . THR B 228 ? 0.3091 0.2232 0.3562 -0.0240 0.0139  0.0458  229 THR B CB  
4556 O OG1 . THR B 228 ? 0.3084 0.2235 0.3737 -0.0267 0.0335  0.0402  229 THR B OG1 
4557 C CG2 . THR B 228 ? 0.3407 0.2183 0.3452 -0.0185 0.0185  0.0556  229 THR B CG2 
4558 N N   . LEU B 229 ? 0.2158 0.2011 0.3254 -0.0321 -0.0160 0.0312  230 LEU B N   
4559 C CA  . LEU B 229 ? 0.2388 0.2562 0.3868 -0.0364 -0.0180 0.0224  230 LEU B CA  
4560 C C   . LEU B 229 ? 0.2200 0.2398 0.3910 -0.0379 0.0022  0.0171  230 LEU B C   
4561 O O   . LEU B 229 ? 0.2161 0.2508 0.4027 -0.0403 0.0034  0.0106  230 LEU B O   
4562 C CB  . LEU B 229 ? 0.1507 0.1922 0.3242 -0.0376 -0.0302 0.0208  230 LEU B CB  
4563 C CG  . LEU B 229 ? 0.1953 0.2698 0.4045 -0.0417 -0.0345 0.0118  230 LEU B CG  
4564 C CD1 . LEU B 229 ? 0.2050 0.2873 0.4024 -0.0426 -0.0481 0.0098  230 LEU B CD1 
4565 C CD2 . LEU B 229 ? 0.1729 0.2603 0.3877 -0.0388 -0.0366 0.0082  230 LEU B CD2 
4566 N N   . PRO B 230 ? 0.2204 0.2262 0.3948 -0.0364 0.0187  0.0193  231 PRO B N   
4567 C CA  . PRO B 230 ? 0.1992 0.2071 0.3963 -0.0382 0.0384  0.0132  231 PRO B CA  
4568 C C   . PRO B 230 ? 0.2449 0.2385 0.4247 -0.0383 0.0466  0.0120  231 PRO B C   
4569 O O   . PRO B 230 ? 0.2048 0.2135 0.4091 -0.0406 0.0530  0.0042  231 PRO B O   
4570 C CB  . PRO B 230 ? 0.2406 0.2288 0.4356 -0.0361 0.0546  0.0177  231 PRO B CB  
4571 C CG  . PRO B 230 ? 0.2408 0.2324 0.4316 -0.0344 0.0406  0.0230  231 PRO B CG  
4572 C CD  . PRO B 230 ? 0.2198 0.2116 0.3849 -0.0335 0.0201  0.0263  231 PRO B CD  
4573 N N   . ASP B 231 ? 0.2497 0.2152 0.3881 -0.0356 0.0459  0.0192  232 ASP B N   
4574 C CA  . ASP B 231 ? 0.2766 0.2279 0.3977 -0.0359 0.0538  0.0179  232 ASP B CA  
4575 C C   . ASP B 231 ? 0.2457 0.2193 0.3768 -0.0383 0.0398  0.0124  232 ASP B C   
4576 O O   . ASP B 231 ? 0.2731 0.2508 0.4150 -0.0398 0.0480  0.0069  232 ASP B O   
4577 C CB  . ASP B 231 ? 0.3114 0.2280 0.3841 -0.0325 0.0546  0.0265  232 ASP B CB  
4578 C CG  . ASP B 231 ? 0.3842 0.2721 0.4434 -0.0301 0.0760  0.0311  232 ASP B CG  
4579 O OD1 . ASP B 231 ? 0.3817 0.2769 0.4708 -0.0314 0.0902  0.0275  232 ASP B OD1 
4580 O OD2 . ASP B 231 ? 0.4244 0.2818 0.4425 -0.0270 0.0787  0.0381  232 ASP B OD2 
4581 N N   . MET B 232 ? 0.2258 0.2135 0.3540 -0.0385 0.0191  0.0138  233 MET B N   
4582 C CA  . MET B 232 ? 0.2054 0.2128 0.3423 -0.0406 0.0068  0.0090  233 MET B CA  
4583 C C   . MET B 232 ? 0.2048 0.2420 0.3845 -0.0431 0.0093  0.0006  233 MET B C   
4584 O O   . MET B 232 ? 0.1797 0.2272 0.3688 -0.0443 0.0090  -0.0043 233 MET B O   
4585 C CB  . MET B 232 ? 0.1991 0.2136 0.3234 -0.0405 -0.0149 0.0121  233 MET B CB  
4586 C CG  . MET B 232 ? 0.2313 0.2173 0.3118 -0.0379 -0.0193 0.0190  233 MET B CG  
4587 S SD  . MET B 232 ? 0.2806 0.2462 0.3346 -0.0379 -0.0114 0.0183  233 MET B SD  
4588 C CE  . MET B 232 ? 0.2605 0.2538 0.3320 -0.0410 -0.0270 0.0123  233 MET B CE  
4589 N N   . LEU B 233 ? 0.1856 0.2363 0.3916 -0.0436 0.0125  -0.0015 234 LEU B N   
4590 C CA  . LEU B 233 ? 0.2040 0.2786 0.4427 -0.0441 0.0162  -0.0100 234 LEU B CA  
4591 C C   . LEU B 233 ? 0.1873 0.2533 0.4339 -0.0438 0.0346  -0.0143 234 LEU B C   
4592 O O   . LEU B 233 ? 0.1824 0.2564 0.4272 -0.0398 0.0322  -0.0199 234 LEU B O   
4593 C CB  . LEU B 233 ? 0.1938 0.2734 0.4350 -0.0404 0.0155  -0.0108 234 LEU B CB  
4594 C CG  . LEU B 233 ? 0.1751 0.2650 0.4009 -0.0383 -0.0017 -0.0092 234 LEU B CG  
4595 C CD1 . LEU B 233 ? 0.1914 0.2822 0.4213 -0.0365 0.0000  -0.0089 234 LEU B CD1 
4596 C CD2 . LEU B 233 ? 0.2437 0.3431 0.4509 -0.0352 -0.0086 -0.0123 234 LEU B CD2 
4597 N N   . SER B 234 ? 0.2075 0.2483 0.4439 -0.0443 0.0516  -0.0105 235 SER B N   
4598 C CA  . SER B 234 ? 0.2083 0.2380 0.4504 -0.0445 0.0707  -0.0144 235 SER B CA  
4599 C C   . SER B 234 ? 0.2224 0.2485 0.4498 -0.0445 0.0670  -0.0154 235 SER B C   
4600 O O   . SER B 234 ? 0.1993 0.2342 0.4471 -0.0453 0.0751  -0.0222 235 SER B O   
4601 C CB  . SER B 234 ? 0.2528 0.2498 0.4724 -0.0428 0.0884  -0.0086 235 SER B CB  
4602 O OG  . SER B 234 ? 0.2685 0.2691 0.5067 -0.0429 0.0950  -0.0087 235 SER B OG  
4603 N N   . PHE B 235 ? 0.1846 0.1978 0.3775 -0.0436 0.0549  -0.0090 236 PHE B N   
4604 C CA  . PHE B 235 ? 0.2156 0.2254 0.3938 -0.0438 0.0503  -0.0099 236 PHE B CA  
4605 C C   . PHE B 235 ? 0.2124 0.2537 0.4193 -0.0451 0.0387  -0.0163 236 PHE B C   
4606 O O   . PHE B 235 ? 0.1949 0.2398 0.4095 -0.0453 0.0429  -0.0207 236 PHE B O   
4607 C CB  . PHE B 235 ? 0.2190 0.2110 0.3569 -0.0427 0.0379  -0.0024 236 PHE B CB  
4608 C CG  . PHE B 235 ? 0.2298 0.2148 0.3497 -0.0430 0.0345  -0.0031 236 PHE B CG  
4609 C CD1 . PHE B 235 ? 0.2746 0.2411 0.3855 -0.0428 0.0510  -0.0046 236 PHE B CD1 
4610 C CD2 . PHE B 235 ? 0.2327 0.2291 0.3455 -0.0437 0.0155  -0.0025 236 PHE B CD2 
4611 C CE1 . PHE B 235 ? 0.2861 0.2459 0.3812 -0.0432 0.0483  -0.0056 236 PHE B CE1 
4612 C CE2 . PHE B 235 ? 0.2590 0.2487 0.3562 -0.0441 0.0129  -0.0034 236 PHE B CE2 
4613 C CZ  . PHE B 235 ? 0.3100 0.2812 0.3980 -0.0438 0.0292  -0.0048 236 PHE B CZ  
4614 N N   . ILE B 236 ? 0.1637 0.2278 0.3870 -0.0458 0.0246  -0.0171 237 ILE B N   
4615 C CA  . ILE B 236 ? 0.1893 0.2727 0.4141 -0.0417 0.0130  -0.0209 237 ILE B CA  
4616 C C   . ILE B 236 ? 0.1699 0.2547 0.4022 -0.0370 0.0221  -0.0262 237 ILE B C   
4617 O O   . ILE B 236 ? 0.1706 0.2598 0.4001 -0.0343 0.0195  -0.0288 237 ILE B O   
4618 C CB  . ILE B 236 ? 0.2182 0.3115 0.4284 -0.0390 -0.0022 -0.0179 237 ILE B CB  
4619 C CG1 . ILE B 236 ? 0.1709 0.2620 0.3714 -0.0427 -0.0143 -0.0134 237 ILE B CG1 
4620 C CG2 . ILE B 236 ? 0.2220 0.3244 0.4175 -0.0345 -0.0084 -0.0187 237 ILE B CG2 
4621 C CD1 . ILE B 236 ? 0.2096 0.2988 0.4015 -0.0447 -0.0211 -0.0131 237 ILE B CD1 
4622 N N   . HIS B 237 ? 0.1465 0.2260 0.3884 -0.0362 0.0325  -0.0279 238 HIS B N   
4623 C CA  . HIS B 237 ? 0.1691 0.2471 0.4188 -0.0325 0.0401  -0.0337 238 HIS B CA  
4624 C C   . HIS B 237 ? 0.1918 0.2621 0.4481 -0.0331 0.0511  -0.0372 238 HIS B C   
4625 O O   . HIS B 237 ? 0.1890 0.2628 0.4473 -0.0301 0.0493  -0.0415 238 HIS B O   
4626 C CB  . HIS B 237 ? 0.1911 0.2613 0.4504 -0.0322 0.0511  -0.0351 238 HIS B CB  
4627 C CG  . HIS B 237 ? 0.2216 0.2873 0.4902 -0.0296 0.0594  -0.0418 238 HIS B CG  
4628 N ND1 . HIS B 237 ? 0.2649 0.3170 0.5425 -0.0305 0.0760  -0.0451 238 HIS B ND1 
4629 C CD2 . HIS B 237 ? 0.2895 0.3612 0.5585 -0.0268 0.0535  -0.0456 238 HIS B CD2 
4630 C CE1 . HIS B 237 ? 0.2553 0.3062 0.5409 -0.0283 0.0784  -0.0514 238 HIS B CE1 
4631 N NE2 . HIS B 237 ? 0.2545 0.3175 0.5354 -0.0263 0.0648  -0.0518 238 HIS B NE2 
4632 N N   . ALA B 238 ? 0.1836 0.2408 0.4407 -0.0378 0.0638  -0.0347 239 ALA B N   
4633 C CA  . ALA B 238 ? 0.2085 0.2551 0.4679 -0.0388 0.0768  -0.0375 239 ALA B CA  
4634 C C   . ALA B 238 ? 0.2087 0.2660 0.4645 -0.0380 0.0645  -0.0386 239 ALA B C   
4635 O O   . ALA B 238 ? 0.2102 0.2660 0.4713 -0.0358 0.0693  -0.0431 239 ALA B O   
4636 C CB  . ALA B 238 ? 0.2389 0.2610 0.4869 -0.0453 0.0948  -0.0320 239 ALA B CB  
4637 N N   . ASN B 239 ? 0.1674 0.2344 0.4139 -0.0395 0.0486  -0.0344 240 ASN B N   
4638 C CA  . ASN B 239 ? 0.1648 0.2404 0.4055 -0.0381 0.0373  -0.0348 240 ASN B CA  
4639 C C   . ASN B 239 ? 0.2114 0.2980 0.4495 -0.0318 0.0281  -0.0369 240 ASN B C   
4640 O O   . ASN B 239 ? 0.1970 0.2866 0.4346 -0.0298 0.0257  -0.0385 240 ASN B O   
4641 C CB  . ASN B 239 ? 0.1655 0.2450 0.3939 -0.0415 0.0230  -0.0297 240 ASN B CB  
4642 C CG  . ASN B 239 ? 0.2378 0.2943 0.4446 -0.0453 0.0283  -0.0259 240 ASN B CG  
4643 O OD1 . ASN B 239 ? 0.2127 0.2632 0.4082 -0.0451 0.0270  -0.0261 240 ASN B OD1 
4644 N ND2 . ASN B 239 ? 0.2074 0.2440 0.3929 -0.0453 0.0331  -0.0209 240 ASN B ND2 
4645 N N   . LEU B 240 ? 0.1690 0.2600 0.4041 -0.0295 0.0239  -0.0362 241 LEU B N   
4646 C CA  . LEU B 240 ? 0.2009 0.2987 0.4309 -0.0254 0.0179  -0.0373 241 LEU B CA  
4647 C C   . LEU B 240 ? 0.2060 0.2989 0.4502 -0.0237 0.0275  -0.0439 241 LEU B C   
4648 O O   . LEU B 240 ? 0.2309 0.3272 0.4789 -0.0210 0.0238  -0.0478 241 LEU B O   
4649 C CB  . LEU B 240 ? 0.1815 0.2827 0.4068 -0.0244 0.0123  -0.0361 241 LEU B CB  
4650 C CG  . LEU B 240 ? 0.1873 0.2937 0.3989 -0.0245 0.0009  -0.0315 241 LEU B CG  
4651 C CD1 . LEU B 240 ? 0.1649 0.2719 0.3764 -0.0240 -0.0015 -0.0314 241 LEU B CD1 
4652 C CD2 . LEU B 240 ? 0.2129 0.3230 0.4216 -0.0219 -0.0054 -0.0332 241 LEU B CD2 
4653 N N   . ASN B 241 ? 0.2012 0.2788 0.5040 -0.0120 -0.0277 -0.0595 242 ASN B N   
4654 C CA  . ASN B 241 ? 0.2065 0.2932 0.5530 -0.0138 -0.0298 -0.0685 242 ASN B CA  
4655 C C   . ASN B 241 ? 0.1981 0.2910 0.5663 -0.0176 -0.0123 -0.0657 242 ASN B C   
4656 O O   . ASN B 241 ? 0.1693 0.2656 0.5659 -0.0229 -0.0007 -0.0670 242 ASN B O   
4657 C CB  . ASN B 241 ? 0.1949 0.2808 0.5574 -0.0182 -0.0297 -0.0723 242 ASN B CB  
4658 C CG  . ASN B 241 ? 0.2424 0.3206 0.5833 -0.0140 -0.0465 -0.0753 242 ASN B CG  
4659 O OD1 . ASN B 241 ? 0.2929 0.3720 0.6450 -0.0088 -0.0647 -0.0848 242 ASN B OD1 
4660 N ND2 . ASN B 241 ? 0.2379 0.3075 0.5468 -0.0153 -0.0407 -0.0675 242 ASN B ND2 
4661 N N   . PRO B 242 ? 0.1728 0.2661 0.5288 -0.0146 -0.0089 -0.0617 243 PRO B N   
4662 C CA  . PRO B 242 ? 0.2004 0.2977 0.5740 -0.0172 0.0087  -0.0586 243 PRO B CA  
4663 C C   . PRO B 242 ? 0.1889 0.2964 0.6115 -0.0189 0.0097  -0.0669 243 PRO B C   
4664 O O   . PRO B 242 ? 0.1829 0.2918 0.6253 -0.0226 0.0283  -0.0642 243 PRO B O   
4665 C CB  . PRO B 242 ? 0.2132 0.3090 0.5650 -0.0124 0.0065  -0.0550 243 PRO B CB  
4666 C CG  . PRO B 242 ? 0.2517 0.3465 0.5918 -0.0068 -0.0144 -0.0599 243 PRO B CG  
4667 C CD  . PRO B 242 ? 0.1701 0.2602 0.5004 -0.0081 -0.0217 -0.0611 243 PRO B CD  
4668 N N   . GLN B 243 ? 0.1675 0.2813 0.6108 -0.0156 -0.0094 -0.0773 244 GLN B N   
4669 C CA  A GLN B 243 ? 0.1858 0.3059 0.6712 -0.0163 -0.0094 -0.0855 244 GLN B CA  
4670 C CA  B GLN B 243 ? 0.1857 0.3058 0.6711 -0.0161 -0.0107 -0.0860 244 GLN B CA  
4671 C C   . GLN B 243 ? 0.1800 0.2950 0.6820 -0.0218 0.0006  -0.0865 244 GLN B C   
4672 O O   . GLN B 243 ? 0.1891 0.3036 0.7192 -0.0224 0.0054  -0.0911 244 GLN B O   
4673 C CB  A GLN B 243 ? 0.2206 0.3431 0.7140 -0.0093 -0.0339 -0.0964 244 GLN B CB  
4674 C CB  B GLN B 243 ? 0.2241 0.3460 0.7161 -0.0093 -0.0361 -0.0970 244 GLN B CB  
4675 C CG  A GLN B 243 ? 0.2227 0.3417 0.7017 -0.0064 -0.0533 -0.1013 244 GLN B CG  
4676 C CG  B GLN B 243 ? 0.2173 0.3348 0.7023 -0.0084 -0.0515 -0.1023 244 GLN B CG  
4677 C CD  A GLN B 243 ? 0.2112 0.3291 0.6863 0.0034  -0.0774 -0.1103 244 GLN B CD  
4678 C CD  B GLN B 243 ? 0.2368 0.3481 0.6796 -0.0060 -0.0578 -0.0962 244 GLN B CD  
4679 O OE1 A GLN B 243 ? 0.2021 0.3230 0.6786 0.0079  -0.0798 -0.1110 244 GLN B OE1 
4680 O OE1 B GLN B 243 ? 0.2025 0.3095 0.6154 -0.0042 -0.0512 -0.0876 244 GLN B OE1 
4681 N NE2 A GLN B 243 ? 0.2567 0.3684 0.7244 0.0076  -0.0951 -0.1172 244 GLN B NE2 
4682 N NE2 B GLN B 243 ? 0.2769 0.3818 0.7081 -0.0051 -0.0689 -0.0992 244 GLN B NE2 
4683 N N   . LYS B 244 ? 0.1759 0.2867 0.6623 -0.0256 0.0046  -0.0821 245 LYS B N   
4684 C CA  . LYS B 244 ? 0.1833 0.2881 0.6828 -0.0304 0.0157  -0.0820 245 LYS B CA  
4685 C C   . LYS B 244 ? 0.1893 0.2874 0.6832 -0.0341 0.0425  -0.0720 245 LYS B C   
4686 O O   . LYS B 244 ? 0.2246 0.3155 0.7251 -0.0376 0.0545  -0.0703 245 LYS B O   
4687 C CB  . LYS B 244 ? 0.1868 0.2887 0.6716 -0.0321 0.0059  -0.0830 245 LYS B CB  
4688 C CG  . LYS B 244 ? 0.2494 0.3538 0.7374 -0.0269 -0.0209 -0.0936 245 LYS B CG  
4689 C CD  . LYS B 244 ? 0.2516 0.3511 0.7260 -0.0281 -0.0305 -0.0952 245 LYS B CD  
4690 C CE  . LYS B 244 ? 0.3444 0.4427 0.8254 -0.0214 -0.0558 -0.1072 245 LYS B CE  
4691 N NZ  . LYS B 244 ? 0.3611 0.4528 0.8317 -0.0218 -0.0655 -0.1101 245 LYS B NZ  
4692 N N   . TYR B 245 ? 0.2040 0.3027 0.6845 -0.0324 0.0519  -0.0655 246 TYR B N   
4693 C CA  . TYR B 245 ? 0.2068 0.2963 0.6740 -0.0338 0.0761  -0.0556 246 TYR B CA  
4694 C C   . TYR B 245 ? 0.2499 0.3377 0.7337 -0.0318 0.0875  -0.0553 246 TYR B C   
4695 O O   . TYR B 245 ? 0.2376 0.3334 0.7394 -0.0293 0.0759  -0.0619 246 TYR B O   
4696 C CB  . TYR B 245 ? 0.2549 0.3436 0.6872 -0.0328 0.0790  -0.0476 246 TYR B CB  
4697 C CG  . TYR B 245 ? 0.2413 0.3239 0.6467 -0.0343 0.0726  -0.0453 246 TYR B CG  
4698 C CD1 . TYR B 245 ? 0.2188 0.3051 0.6187 -0.0331 0.0507  -0.0511 246 TYR B CD1 
4699 C CD2 . TYR B 245 ? 0.2616 0.3326 0.6448 -0.0357 0.0884  -0.0373 246 TYR B CD2 
4700 C CE1 . TYR B 245 ? 0.2438 0.3231 0.6180 -0.0338 0.0455  -0.0487 246 TYR B CE1 
4701 C CE2 . TYR B 245 ? 0.2276 0.2926 0.5858 -0.0365 0.0823  -0.0352 246 TYR B CE2 
4702 C CZ  . TYR B 245 ? 0.2269 0.2966 0.5817 -0.0359 0.0612  -0.0408 246 TYR B CZ  
4703 O OH  . TYR B 245 ? 0.2391 0.3023 0.5692 -0.0363 0.0559  -0.0386 246 TYR B OH  
4704 N N   . PRO B 246 ? 0.2808 0.3568 0.7578 -0.0321 0.1100  -0.0478 247 PRO B N   
4705 C CA  . PRO B 246 ? 0.3066 0.3792 0.7979 -0.0298 0.1218  -0.0469 247 PRO B CA  
4706 C C   . PRO B 246 ? 0.2696 0.3491 0.7497 -0.0260 0.1165  -0.0457 247 PRO B C   
4707 O O   . PRO B 246 ? 0.2679 0.3510 0.7226 -0.0246 0.1100  -0.0426 247 PRO B O   
4708 C CB  . PRO B 246 ? 0.3375 0.3927 0.8122 -0.0294 0.1464  -0.0376 247 PRO B CB  
4709 C CG  . PRO B 246 ? 0.3290 0.3796 0.7968 -0.0326 0.1464  -0.0370 247 PRO B CG  
4710 C CD  . PRO B 246 ? 0.2653 0.3283 0.7224 -0.0337 0.1255  -0.0405 247 PRO B CD  
4711 N N   . ALA B 247 ? 0.3204 0.4012 0.8209 -0.0241 0.1202  -0.0481 248 ALA B N   
4712 C CA  . ALA B 247 ? 0.2467 0.3361 0.7444 -0.0202 0.1116  -0.0494 248 ALA B CA  
4713 C C   . ALA B 247 ? 0.2708 0.3556 0.7326 -0.0171 0.1198  -0.0406 248 ALA B C   
4714 O O   . ALA B 247 ? 0.2598 0.3530 0.7105 -0.0144 0.1076  -0.0418 248 ALA B O   
4715 C CB  . ALA B 247 ? 0.2447 0.3335 0.7695 -0.0189 0.1184  -0.0522 248 ALA B CB  
4716 N N   . ASP B 248 ? 0.3078 0.3780 0.7504 -0.0166 0.1400  -0.0323 249 ASP B N   
4717 C CA  . ASP B 248 ? 0.3433 0.4067 0.7517 -0.0121 0.1485  -0.0247 249 ASP B CA  
4718 C C   . ASP B 248 ? 0.2566 0.3238 0.6403 -0.0126 0.1391  -0.0233 249 ASP B C   
4719 O O   . ASP B 248 ? 0.2977 0.3635 0.6540 -0.0089 0.1319  -0.0212 249 ASP B O   
4720 C CB  . ASP B 248 ? 0.4003 0.4438 0.7918 -0.0097 0.1717  -0.0167 249 ASP B CB  
4721 C CG  . ASP B 248 ? 0.5396 0.5776 0.9495 -0.0076 0.1833  -0.0163 249 ASP B CG  
4722 O OD1 . ASP B 248 ? 0.4624 0.5128 0.8964 -0.0078 0.1733  -0.0222 249 ASP B OD1 
4723 O OD2 . ASP B 248 ? 0.5708 0.5908 0.9700 -0.0053 0.2023  -0.0100 249 ASP B OD2 
4724 N N   . ILE B 249 ? 0.3020 0.3685 0.6856 -0.0168 0.1359  -0.0240 250 ILE B N   
4725 C CA  . ILE B 249 ? 0.2641 0.3287 0.6147 -0.0169 0.1225  -0.0224 250 ILE B CA  
4726 C C   . ILE B 249 ? 0.2474 0.3240 0.6051 -0.0175 0.0983  -0.0294 250 ILE B C   
4727 O O   . ILE B 249 ? 0.2591 0.3334 0.5862 -0.0156 0.0859  -0.0279 250 ILE B O   
4728 C CB  . ILE B 249 ? 0.2450 0.3019 0.5879 -0.0202 0.1293  -0.0196 250 ILE B CB  
4729 C CG1 . ILE B 249 ? 0.2434 0.2935 0.5436 -0.0188 0.1196  -0.0159 250 ILE B CG1 
4730 C CG2 . ILE B 249 ? 0.2918 0.3585 0.6710 -0.0257 0.1223  -0.0268 250 ILE B CG2 
4731 C CD1 . ILE B 249 ? 0.2933 0.3314 0.5572 -0.0133 0.1274  -0.0093 250 ILE B CD1 
4732 N N   . GLN B 250 ? 0.2240 0.3124 0.6217 -0.0193 0.0916  -0.0374 251 GLN B N   
4733 C CA  . GLN B 250 ? 0.2097 0.3071 0.6123 -0.0176 0.0683  -0.0446 251 GLN B CA  
4734 C C   . GLN B 250 ? 0.2283 0.3254 0.6108 -0.0124 0.0620  -0.0430 251 GLN B C   
4735 O O   . GLN B 250 ? 0.2291 0.3240 0.5850 -0.0101 0.0476  -0.0426 251 GLN B O   
4736 C CB  . GLN B 250 ? 0.2306 0.3402 0.6823 -0.0191 0.0625  -0.0544 251 GLN B CB  
4737 C CG  . GLN B 250 ? 0.2150 0.3326 0.6725 -0.0150 0.0382  -0.0627 251 GLN B CG  
4738 C CD  . GLN B 250 ? 0.2896 0.4112 0.7820 -0.0147 0.0295  -0.0725 251 GLN B CD  
4739 O OE1 . GLN B 250 ? 0.3216 0.4485 0.8209 -0.0102 0.0101  -0.0803 251 GLN B OE1 
4740 N NE2 . GLN B 250 ? 0.3679 0.4841 0.8791 -0.0186 0.0436  -0.0723 251 GLN B NE2 
4741 N N   . ARG B 251 ? 0.2492 0.3475 0.6443 -0.0104 0.0734  -0.0418 252 ARG B N   
4742 C CA  . ARG B 251 ? 0.2689 0.3664 0.6457 -0.0054 0.0673  -0.0406 252 ARG B CA  
4743 C C   . ARG B 251 ? 0.2291 0.3146 0.5608 -0.0040 0.0706  -0.0328 252 ARG B C   
4744 O O   . ARG B 251 ? 0.2362 0.3200 0.5463 -0.0009 0.0599  -0.0323 252 ARG B O   
4745 C CB  . ARG B 251 ? 0.3526 0.4540 0.7548 -0.0031 0.0788  -0.0415 252 ARG B CB  
4746 C CG  . ARG B 251 ? 0.3203 0.4358 0.7643 -0.0023 0.0671  -0.0514 252 ARG B CG  
4747 C CD  . ARG B 251 ? 0.4623 0.5776 0.9329 -0.0022 0.0803  -0.0522 252 ARG B CD  
4748 N NE  . ARG B 251 ? 0.5699 0.6879 1.0396 0.0032  0.0796  -0.0522 252 ARG B NE  
4749 C CZ  . ARG B 251 ? 0.6244 0.7347 1.0812 0.0056  0.0966  -0.0456 252 ARG B CZ  
4750 N NH1 . ARG B 251 ? 0.6046 0.7029 1.0466 0.0038  0.1156  -0.0383 252 ARG B NH1 
4751 N NH2 . ARG B 251 ? 0.5440 0.6571 1.0007 0.0108  0.0943  -0.0464 252 ARG B NH2 
4752 N N   . ALA B 252 ? 0.2501 0.3266 0.5678 -0.0059 0.0846  -0.0271 253 ALA B N   
4753 C CA  . ALA B 252 ? 0.2486 0.3142 0.5254 -0.0043 0.0854  -0.0211 253 ALA B CA  
4754 C C   . ALA B 252 ? 0.2373 0.3042 0.4963 -0.0055 0.0683  -0.0223 253 ALA B C   
4755 O O   . ALA B 252 ? 0.2125 0.2753 0.4458 -0.0033 0.0617  -0.0201 253 ALA B O   
4756 C CB  . ALA B 252 ? 0.2499 0.3050 0.5161 -0.0051 0.1022  -0.0158 253 ALA B CB  
4757 N N   . ILE B 253 ? 0.2072 0.2787 0.4796 -0.0088 0.0619  -0.0256 254 ILE B N   
4758 C CA  . ILE B 253 ? 0.2127 0.2840 0.4682 -0.0091 0.0466  -0.0266 254 ILE B CA  
4759 C C   . ILE B 253 ? 0.2117 0.2869 0.4665 -0.0055 0.0321  -0.0302 254 ILE B C   
4760 O O   . ILE B 253 ? 0.2211 0.2916 0.4507 -0.0036 0.0245  -0.0280 254 ILE B O   
4761 C CB  . ILE B 253 ? 0.2121 0.2866 0.4838 -0.0126 0.0426  -0.0302 254 ILE B CB  
4762 C CG1 . ILE B 253 ? 0.2425 0.3108 0.5103 -0.0158 0.0576  -0.0258 254 ILE B CG1 
4763 C CG2 . ILE B 253 ? 0.2093 0.2826 0.4637 -0.0116 0.0263  -0.0316 254 ILE B CG2 
4764 C CD1 . ILE B 253 ? 0.2268 0.2984 0.5182 -0.0197 0.0574  -0.0297 254 ILE B CD1 
4765 N N   . ASN B 254 ? 0.2115 0.2946 0.4950 -0.0040 0.0285  -0.0359 255 ASN B N   
4766 C CA  . ASN B 254 ? 0.2192 0.3046 0.5016 0.0009  0.0150  -0.0396 255 ASN B CA  
4767 C C   . ASN B 254 ? 0.2335 0.3127 0.4907 0.0035  0.0181  -0.0345 255 ASN B C   
4768 O O   . ASN B 254 ? 0.2503 0.3258 0.4894 0.0068  0.0078  -0.0344 255 ASN B O   
4769 C CB  . ASN B 254 ? 0.2152 0.3103 0.5346 0.0026  0.0128  -0.0466 255 ASN B CB  
4770 C CG  . ASN B 254 ? 0.2862 0.3877 0.6315 0.0016  0.0025  -0.0543 255 ASN B CG  
4771 O OD1 . ASN B 254 ? 0.3051 0.4029 0.6364 0.0014  -0.0071 -0.0551 255 ASN B OD1 
4772 N ND2 . ASN B 254 ? 0.3246 0.4357 0.7094 0.0013  0.0041  -0.0607 255 ASN B ND2 
4773 N N   . GLU B 255 ? 0.2726 0.3491 0.5277 0.0027  0.0328  -0.0305 256 GLU B N   
4774 C CA  . GLU B 255 ? 0.2312 0.3012 0.4636 0.0054  0.0357  -0.0265 256 GLU B CA  
4775 C C   . GLU B 255 ? 0.2779 0.3406 0.4796 0.0047  0.0305  -0.0228 256 GLU B C   
4776 O O   . GLU B 255 ? 0.2568 0.3156 0.4428 0.0072  0.0252  -0.0218 256 GLU B O   
4777 C CB  . GLU B 255 ? 0.2834 0.3492 0.5161 0.0054  0.0527  -0.0229 256 GLU B CB  
4778 C CG  . GLU B 255 ? 0.3578 0.4189 0.5796 0.0095  0.0564  -0.0212 256 GLU B CG  
4779 C CD  . GLU B 255 ? 0.3272 0.3955 0.5700 0.0126  0.0514  -0.0256 256 GLU B CD  
4780 O OE1 . GLU B 255 ? 0.3056 0.3722 0.5363 0.0154  0.0420  -0.0262 256 GLU B OE1 
4781 O OE2 . GLU B 255 ? 0.3097 0.3850 0.5820 0.0124  0.0571  -0.0285 256 GLU B OE2 
4782 N N   . THR B 256 ? 0.2113 0.2720 0.4058 0.0014  0.0323  -0.0209 257 THR B N   
4783 C CA  . THR B 256 ? 0.2176 0.2722 0.3862 0.0006  0.0283  -0.0176 257 THR B CA  
4784 C C   . THR B 256 ? 0.2213 0.2759 0.3843 0.0020  0.0151  -0.0193 257 THR B C   
4785 O O   . THR B 256 ? 0.2468 0.2959 0.3898 0.0018  0.0124  -0.0164 257 THR B O   
4786 C CB  . THR B 256 ? 0.2266 0.2787 0.3892 -0.0026 0.0344  -0.0152 257 THR B CB  
4787 O OG1 . THR B 256 ? 0.2235 0.2800 0.3992 -0.0046 0.0291  -0.0179 257 THR B OG1 
4788 C CG2 . THR B 256 ? 0.2256 0.2750 0.3927 -0.0026 0.0487  -0.0134 257 THR B CG2 
4789 N N   . HIS B 257 ? 0.2093 0.2687 0.3891 0.0039  0.0071  -0.0241 258 HIS B N   
4790 C CA  . HIS B 257 ? 0.1760 0.2323 0.3467 0.0072  -0.0056 -0.0258 258 HIS B CA  
4791 C C   . HIS B 257 ? 0.2166 0.2698 0.3816 0.0123  -0.0112 -0.0266 258 HIS B C   
4792 O O   . HIS B 257 ? 0.2114 0.2587 0.3643 0.0165  -0.0205 -0.0272 258 HIS B O   
4793 C CB  . HIS B 257 ? 0.2222 0.2832 0.4115 0.0081  -0.0140 -0.0316 258 HIS B CB  
4794 C CG  . HIS B 257 ? 0.1960 0.2585 0.3898 0.0034  -0.0098 -0.0311 258 HIS B CG  
4795 N ND1 . HIS B 257 ? 0.2438 0.3110 0.4580 0.0028  -0.0155 -0.0367 258 HIS B ND1 
4796 C CD2 . HIS B 257 ? 0.2171 0.2764 0.3975 -0.0007 -0.0009 -0.0260 258 HIS B CD2 
4797 C CE1 . HIS B 257 ? 0.2192 0.2856 0.4318 -0.0017 -0.0093 -0.0345 258 HIS B CE1 
4798 N NE2 . HIS B 257 ? 0.2263 0.2878 0.4176 -0.0036 -0.0005 -0.0279 258 HIS B NE2 
4799 N N   . GLN B 258 ? 0.1914 0.2468 0.3631 0.0128  -0.0051 -0.0263 259 GLN B N   
4800 C CA  . GLN B 258 ? 0.2055 0.2581 0.3734 0.0179  -0.0098 -0.0273 259 GLN B CA  
4801 C C   . GLN B 258 ? 0.2123 0.2557 0.3555 0.0178  -0.0073 -0.0223 259 GLN B C   
4802 O O   . GLN B 258 ? 0.2233 0.2655 0.3610 0.0148  0.0012  -0.0194 259 GLN B O   
4803 C CB  . GLN B 258 ? 0.2279 0.2866 0.4149 0.0187  -0.0039 -0.0294 259 GLN B CB  
4804 C CG  . GLN B 258 ? 0.2429 0.2980 0.4245 0.0239  -0.0077 -0.0300 259 GLN B CG  
4805 C CD  . GLN B 258 ? 0.3046 0.3661 0.5068 0.0255  -0.0023 -0.0325 259 GLN B CD  
4806 O OE1 . GLN B 258 ? 0.3486 0.4177 0.5727 0.0230  0.0037  -0.0344 259 GLN B OE1 
4807 N NE2 . GLN B 258 ? 0.3394 0.3970 0.5353 0.0296  -0.0033 -0.0322 259 GLN B NE2 
4808 N N   . GLY B 259 ? 0.2543 0.2900 0.3829 0.0216  -0.0147 -0.0216 260 GLY B N   
4809 C CA  . GLY B 259 ? 0.2570 0.2837 0.3663 0.0216  -0.0118 -0.0174 260 GLY B CA  
4810 C C   . GLY B 259 ? 0.2212 0.2473 0.3328 0.0231  -0.0082 -0.0175 260 GLY B C   
4811 O O   . GLY B 259 ? 0.2381 0.2671 0.3605 0.0272  -0.0116 -0.0208 260 GLY B O   
4812 N N   . ARG B 260 ? 0.2374 0.2594 0.3392 0.0200  -0.0019 -0.0145 261 ARG B N   
4813 C CA  . ARG B 260 ? 0.2051 0.2252 0.3069 0.0212  0.0019  -0.0147 261 ARG B CA  
4814 C C   . ARG B 260 ? 0.2448 0.2546 0.3329 0.0229  0.0010  -0.0127 261 ARG B C   
4815 O O   . ARG B 260 ? 0.2930 0.3000 0.3813 0.0256  0.0018  -0.0135 261 ARG B O   
4816 C CB  . ARG B 260 ? 0.2204 0.2425 0.3222 0.0174  0.0096  -0.0139 261 ARG B CB  
4817 C CG  . ARG B 260 ? 0.1899 0.2199 0.3039 0.0155  0.0133  -0.0149 261 ARG B CG  
4818 C CD  . ARG B 260 ? 0.2275 0.2639 0.3600 0.0184  0.0139  -0.0179 261 ARG B CD  
4819 N NE  . ARG B 260 ? 0.2237 0.2670 0.3709 0.0161  0.0180  -0.0189 261 ARG B NE  
4820 C CZ  . ARG B 260 ? 0.2685 0.3171 0.4339 0.0170  0.0240  -0.0208 261 ARG B CZ  
4821 N NH1 . ARG B 260 ? 0.2671 0.3154 0.4377 0.0206  0.0265  -0.0218 261 ARG B NH1 
4822 N NH2 . ARG B 260 ? 0.2697 0.3236 0.4494 0.0144  0.0285  -0.0215 261 ARG B NH2 
4823 N N   . TYR B 261 ? 0.2089 0.2124 0.2859 0.0214  0.0004  -0.0100 262 TYR B N   
4824 C CA  . TYR B 261 ? 0.2318 0.2240 0.2972 0.0232  0.0008  -0.0076 262 TYR B CA  
4825 C C   . TYR B 261 ? 0.2221 0.2092 0.2789 0.0220  0.0009  -0.0046 262 TYR B C   
4826 O O   . TYR B 261 ? 0.2137 0.2068 0.2733 0.0197  0.0000  -0.0048 262 TYR B O   
4827 C CB  . TYR B 261 ? 0.2233 0.2121 0.2873 0.0202  0.0056  -0.0075 262 TYR B CB  
4828 C CG  . TYR B 261 ? 0.2111 0.2040 0.2766 0.0146  0.0086  -0.0074 262 TYR B CG  
4829 C CD1 . TYR B 261 ? 0.2111 0.2004 0.2725 0.0115  0.0100  -0.0053 262 TYR B CD1 
4830 C CD2 . TYR B 261 ? 0.2062 0.2054 0.2765 0.0134  0.0105  -0.0096 262 TYR B CD2 
4831 C CE1 . TYR B 261 ? 0.2191 0.2124 0.2824 0.0072  0.0115  -0.0060 262 TYR B CE1 
4832 C CE2 . TYR B 261 ? 0.2025 0.2034 0.2713 0.0099  0.0123  -0.0100 262 TYR B CE2 
4833 C CZ  . TYR B 261 ? 0.2123 0.2111 0.2783 0.0068  0.0120  -0.0086 262 TYR B CZ  
4834 O OH  . TYR B 261 ? 0.2040 0.2048 0.2691 0.0041  0.0126  -0.0096 262 TYR B OH  
4835 N N   . GLN B 262 ? 0.2301 0.2053 0.2765 0.0236  0.0032  -0.0017 263 GLN B N   
4836 C CA  . GLN B 262 ? 0.2542 0.2234 0.2926 0.0226  0.0056  0.0018  263 GLN B CA  
4837 C C   . GLN B 262 ? 0.2364 0.1988 0.2738 0.0188  0.0125  0.0043  263 GLN B C   
4838 O O   . GLN B 262 ? 0.2491 0.2075 0.2884 0.0186  0.0146  0.0036  263 GLN B O   
4839 C CB  . GLN B 262 ? 0.3008 0.2590 0.3259 0.0304  0.0021  0.0035  263 GLN B CB  
4840 C CG  . GLN B 262 ? 0.3094 0.2527 0.3234 0.0361  0.0044  0.0057  263 GLN B CG  
4841 C CD  . GLN B 262 ? 0.3714 0.3021 0.3688 0.0461  -0.0006 0.0067  263 GLN B CD  
4842 O OE1 . GLN B 262 ? 0.3607 0.2879 0.3547 0.0531  -0.0064 0.0043  263 GLN B OE1 
4843 N NE2 . GLN B 262 ? 0.3853 0.3083 0.3716 0.0478  0.0012  0.0098  263 GLN B NE2 
4844 N N   . VAL B 263 ? 0.2344 0.1962 0.2711 0.0155  0.0159  0.0066  264 VAL B N   
4845 C CA  . VAL B 263 ? 0.2404 0.1950 0.2788 0.0122  0.0230  0.0091  264 VAL B CA  
4846 C C   . VAL B 263 ? 0.2641 0.2085 0.2917 0.0153  0.0270  0.0139  264 VAL B C   
4847 O O   . VAL B 263 ? 0.2803 0.2298 0.3073 0.0140  0.0259  0.0144  264 VAL B O   
4848 C CB  . VAL B 263 ? 0.2383 0.2028 0.2891 0.0052  0.0237  0.0065  264 VAL B CB  
4849 C CG1 . VAL B 263 ? 0.2769 0.2345 0.3340 0.0018  0.0305  0.0082  264 VAL B CG1 
4850 C CG2 . VAL B 263 ? 0.2203 0.1922 0.2777 0.0039  0.0199  0.0018  264 VAL B CG2 
4851 N N   . ASN B 264 ? 0.2817 0.2101 0.2988 0.0202  0.0320  0.0175  265 ASN B N   
4852 C CA  . ASN B 264 ? 0.3393 0.2536 0.3409 0.0258  0.0366  0.0227  265 ASN B CA  
4853 C C   . ASN B 264 ? 0.3529 0.2709 0.3448 0.0309  0.0274  0.0211  265 ASN B C   
4854 O O   . ASN B 264 ? 0.3835 0.3048 0.3740 0.0348  0.0193  0.0176  265 ASN B O   
4855 C CB  . ASN B 264 ? 0.3451 0.2589 0.3545 0.0202  0.0455  0.0256  265 ASN B CB  
4856 C CG  . ASN B 264 ? 0.3681 0.2794 0.3919 0.0148  0.0532  0.0256  265 ASN B CG  
4857 O OD1 . ASN B 264 ? 0.4104 0.3121 0.4314 0.0173  0.0558  0.0262  265 ASN B OD1 
4858 N ND2 . ASN B 264 ? 0.4333 0.3531 0.4737 0.0077  0.0563  0.0244  265 ASN B ND2 
4859 N N   . THR B 265 ? 0.2994 0.2174 0.2865 0.0310  0.0280  0.0229  266 THR B N   
4860 C CA  . THR B 265 ? 0.2998 0.2193 0.2779 0.0363  0.0188  0.0208  266 THR B CA  
4861 C C   . THR B 265 ? 0.2885 0.2280 0.2822 0.0303  0.0117  0.0158  266 THR B C   
4862 O O   . THR B 265 ? 0.3022 0.2447 0.2930 0.0336  0.0040  0.0133  266 THR B O   
4863 C CB  . THR B 265 ? 0.3518 0.2591 0.3144 0.0405  0.0229  0.0253  266 THR B CB  
4864 O OG1 . THR B 265 ? 0.3261 0.2395 0.2999 0.0326  0.0312  0.0276  266 THR B OG1 
4865 C CG2 . THR B 265 ? 0.3781 0.2614 0.3192 0.0501  0.0292  0.0303  266 THR B CG2 
4866 N N   . MET B 266 ? 0.2466 0.1983 0.2564 0.0224  0.0141  0.0140  267 MET B N   
4867 C CA  . MET B 266 ? 0.2488 0.2166 0.2711 0.0175  0.0096  0.0100  267 MET B CA  
4868 C C   . MET B 266 ? 0.2748 0.2493 0.3055 0.0179  0.0055  0.0061  267 MET B C   
4869 O O   . MET B 266 ? 0.2679 0.2399 0.3011 0.0171  0.0084  0.0061  267 MET B O   
4870 C CB  . MET B 266 ? 0.2384 0.2137 0.2701 0.0101  0.0145  0.0103  267 MET B CB  
4871 C CG  . MET B 266 ? 0.2372 0.2260 0.2781 0.0062  0.0112  0.0069  267 MET B CG  
4872 S SD  . MET B 266 ? 0.3164 0.3116 0.3656 -0.0002 0.0151  0.0062  267 MET B SD  
4873 C CE  . MET B 266 ? 0.2493 0.2441 0.3047 -0.0010 0.0156  0.0035  267 MET B CE  
4874 N N   . TYR B 267 ? 0.2199 0.2023 0.2562 0.0192  -0.0007 0.0026  268 TYR B N   
4875 C CA  . TYR B 267 ? 0.2143 0.2048 0.2620 0.0191  -0.0032 -0.0012 268 TYR B CA  
4876 C C   . TYR B 267 ? 0.2012 0.2030 0.2598 0.0130  -0.0003 -0.0027 268 TYR B C   
4877 O O   . TYR B 267 ? 0.2046 0.2107 0.2645 0.0105  -0.0003 -0.0025 268 TYR B O   
4878 C CB  . TYR B 267 ? 0.2185 0.2106 0.2694 0.0247  -0.0114 -0.0048 268 TYR B CB  
4879 C CG  . TYR B 267 ? 0.2691 0.2482 0.3066 0.0331  -0.0159 -0.0042 268 TYR B CG  
4880 C CD1 . TYR B 267 ? 0.3024 0.2696 0.3234 0.0376  -0.0170 -0.0015 268 TYR B CD1 
4881 C CD2 . TYR B 267 ? 0.2943 0.2712 0.3335 0.0376  -0.0185 -0.0062 268 TYR B CD2 
4882 C CE1 . TYR B 267 ? 0.3550 0.3069 0.3596 0.0470  -0.0205 -0.0006 268 TYR B CE1 
4883 C CE2 . TYR B 267 ? 0.3377 0.3008 0.3621 0.0466  -0.0226 -0.0056 268 TYR B CE2 
4884 C CZ  . TYR B 267 ? 0.3366 0.2865 0.3427 0.0516  -0.0236 -0.0028 268 TYR B CZ  
4885 O OH  . TYR B 267 ? 0.4576 0.3905 0.4450 0.0622  -0.0273 -0.0020 268 TYR B OH  
4886 N N   . GLN B 268 ? 0.1979 0.2029 0.2624 0.0113  0.0025  -0.0040 269 GLN B N   
4887 C CA  . GLN B 268 ? 0.1897 0.2021 0.2604 0.0073  0.0059  -0.0052 269 GLN B CA  
4888 C C   . GLN B 268 ? 0.1962 0.2158 0.2782 0.0085  0.0053  -0.0080 269 GLN B C   
4889 O O   . GLN B 268 ? 0.1945 0.2147 0.2817 0.0110  0.0052  -0.0097 269 GLN B O   
4890 C CB  . GLN B 268 ? 0.1907 0.2007 0.2599 0.0059  0.0092  -0.0056 269 GLN B CB  
4891 C CG  . GLN B 268 ? 0.1867 0.2010 0.2577 0.0039  0.0124  -0.0070 269 GLN B CG  
4892 C CD  . GLN B 268 ? 0.1830 0.1988 0.2507 0.0009  0.0130  -0.0059 269 GLN B CD  
4893 O OE1 . GLN B 268 ? 0.1881 0.2007 0.2524 -0.0008 0.0127  -0.0051 269 GLN B OE1 
4894 N NE2 . GLN B 268 ? 0.1834 0.2039 0.2538 0.0003  0.0143  -0.0059 269 GLN B NE2 
4895 N N   . ALA B 269 ? 0.1997 0.2246 0.2870 0.0068  0.0053  -0.0085 270 ALA B N   
4896 C CA  . ALA B 269 ? 0.2103 0.2421 0.3119 0.0070  0.0071  -0.0111 270 ALA B CA  
4897 C C   . ALA B 269 ? 0.2043 0.2370 0.3050 0.0046  0.0151  -0.0103 270 ALA B C   
4898 O O   . ALA B 269 ? 0.2314 0.2596 0.3212 0.0039  0.0169  -0.0089 270 ALA B O   
4899 C CB  . ALA B 269 ? 0.1981 0.2339 0.3077 0.0068  0.0028  -0.0128 270 ALA B CB  
4900 N N   . LEU B 270 ? 0.2100 0.2471 0.3219 0.0040  0.0200  -0.0114 271 LEU B N   
4901 C CA  . LEU B 270 ? 0.2424 0.2771 0.3493 0.0035  0.0285  -0.0101 271 LEU B CA  
4902 C C   . LEU B 270 ? 0.2219 0.2559 0.3221 0.0008  0.0292  -0.0085 271 LEU B C   
4903 O O   . LEU B 270 ? 0.2481 0.2860 0.3578 -0.0009 0.0298  -0.0089 271 LEU B O   
4904 C CB  . LEU B 270 ? 0.2407 0.2780 0.3618 0.0047  0.0364  -0.0111 271 LEU B CB  
4905 C CG  . LEU B 270 ? 0.3242 0.3624 0.4545 0.0078  0.0382  -0.0127 271 LEU B CG  
4906 C CD1 . LEU B 270 ? 0.3179 0.3574 0.4619 0.0086  0.0495  -0.0127 271 LEU B CD1 
4907 C CD2 . LEU B 270 ? 0.2920 0.3231 0.4061 0.0102  0.0380  -0.0119 271 LEU B CD2 
4908 N N   . GLY B 271 ? 0.1863 0.2155 0.2716 0.0005  0.0287  -0.0072 272 GLY B N   
4909 C CA  . GLY B 271 ? 0.2240 0.2526 0.3022 -0.0015 0.0284  -0.0058 272 GLY B CA  
4910 C C   . GLY B 271 ? 0.1982 0.2288 0.2767 -0.0033 0.0217  -0.0052 272 GLY B C   
4911 O O   . GLY B 271 ? 0.1970 0.2251 0.2670 -0.0040 0.0192  -0.0041 272 GLY B O   
4912 N N   . TRP B 272 ? 0.1842 0.2184 0.2729 -0.0033 0.0188  -0.0062 273 TRP B N   
4913 C CA  . TRP B 272 ? 0.2009 0.2341 0.2864 -0.0033 0.0123  -0.0057 273 TRP B CA  
4914 C C   . TRP B 272 ? 0.1958 0.2244 0.2743 -0.0013 0.0088  -0.0048 273 TRP B C   
4915 O O   . TRP B 272 ? 0.2035 0.2314 0.2844 0.0004  0.0089  -0.0058 273 TRP B O   
4916 C CB  . TRP B 272 ? 0.1879 0.2247 0.2857 -0.0022 0.0081  -0.0084 273 TRP B CB  
4917 C CG  . TRP B 272 ? 0.1986 0.2392 0.3061 -0.0045 0.0114  -0.0094 273 TRP B CG  
4918 C CD1 . TRP B 272 ? 0.2281 0.2729 0.3513 -0.0053 0.0168  -0.0114 273 TRP B CD1 
4919 C CD2 . TRP B 272 ? 0.1958 0.2354 0.2988 -0.0063 0.0106  -0.0085 273 TRP B CD2 
4920 N NE1 . TRP B 272 ? 0.2141 0.2602 0.3433 -0.0077 0.0198  -0.0116 273 TRP B NE1 
4921 C CE2 . TRP B 272 ? 0.2140 0.2570 0.3304 -0.0084 0.0155  -0.0100 273 TRP B CE2 
4922 C CE3 . TRP B 272 ? 0.1933 0.2288 0.2825 -0.0062 0.0072  -0.0063 273 TRP B CE3 
4923 C CZ2 . TRP B 272 ? 0.1780 0.2203 0.2938 -0.0104 0.0162  -0.0097 273 TRP B CZ2 
4924 C CZ3 . TRP B 272 ? 0.1695 0.2047 0.2575 -0.0079 0.0076  -0.0059 273 TRP B CZ3 
4925 C CH2 . TRP B 272 ? 0.1818 0.2203 0.2826 -0.0100 0.0117  -0.0077 273 TRP B CH2 
4926 N N   . GLU B 273 ? 0.1744 0.1987 0.2438 -0.0013 0.0066  -0.0026 274 GLU B N   
4927 C CA  . GLU B 273 ? 0.1953 0.2128 0.2578 0.0015  0.0040  -0.0012 274 GLU B CA  
4928 C C   . GLU B 273 ? 0.1861 0.2009 0.2475 0.0056  -0.0021 -0.0023 274 GLU B C   
4929 O O   . GLU B 273 ? 0.1851 0.2017 0.2477 0.0053  -0.0045 -0.0032 274 GLU B O   
4930 C CB  . GLU B 273 ? 0.2073 0.2200 0.2612 0.0000  0.0067  0.0020  274 GLU B CB  
4931 C CG  . GLU B 273 ? 0.2407 0.2561 0.2966 -0.0033 0.0105  0.0017  274 GLU B CG  
4932 C CD  . GLU B 273 ? 0.2986 0.3116 0.3510 -0.0052 0.0127  0.0039  274 GLU B CD  
4933 O OE1 . GLU B 273 ? 0.3037 0.3121 0.3506 -0.0039 0.0129  0.0065  274 GLU B OE1 
4934 O OE2 . GLU B 273 ? 0.2708 0.2858 0.3259 -0.0072 0.0141  0.0026  274 GLU B OE2 
4935 N N   . GLU B 274 ? 0.1936 0.2032 0.2522 0.0101  -0.0054 -0.0029 275 GLU B N   
4936 C CA  . GLU B 274 ? 0.2094 0.2157 0.2673 0.0159  -0.0133 -0.0055 275 GLU B CA  
4937 C C   . GLU B 274 ? 0.2158 0.2082 0.2558 0.0217  -0.0148 -0.0026 275 GLU B C   
4938 O O   . GLU B 274 ? 0.2192 0.2057 0.2531 0.0216  -0.0097 0.0004  275 GLU B O   
4939 C CB  . GLU B 274 ? 0.2109 0.2228 0.2821 0.0178  -0.0164 -0.0096 275 GLU B CB  
4940 C CG  . GLU B 274 ? 0.2182 0.2261 0.2893 0.0253  -0.0264 -0.0135 275 GLU B CG  
4941 C CD  . GLU B 274 ? 0.3451 0.3608 0.4339 0.0266  -0.0290 -0.0180 275 GLU B CD  
4942 O OE1 . GLU B 274 ? 0.3081 0.3300 0.4055 0.0222  -0.0218 -0.0172 275 GLU B OE1 
4943 O OE2 . GLU B 274 ? 0.3892 0.4041 0.4830 0.0327  -0.0385 -0.0228 275 GLU B OE2 
4944 N N   . PHE B 275 ? 0.2451 0.2306 0.2762 0.0274  -0.0214 -0.0036 276 PHE B N   
4945 C CA  . PHE B 275 ? 0.2665 0.2353 0.2766 0.0348  -0.0219 -0.0004 276 PHE B CA  
4946 C C   . PHE B 275 ? 0.3160 0.2780 0.3200 0.0442  -0.0337 -0.0050 276 PHE B C   
4947 O O   . PHE B 275 ? 0.2790 0.2491 0.2949 0.0441  -0.0416 -0.0104 276 PHE B O   
4948 C CB  . PHE B 275 ? 0.2588 0.2210 0.2569 0.0335  -0.0164 0.0043  276 PHE B CB  
4949 C CG  . PHE B 275 ? 0.2346 0.2051 0.2414 0.0246  -0.0072 0.0072  276 PHE B CG  
4950 C CD1 . PHE B 275 ? 0.2184 0.2016 0.2374 0.0183  -0.0071 0.0053  276 PHE B CD1 
4951 C CD2 . PHE B 275 ? 0.2494 0.2144 0.2532 0.0230  0.0010  0.0112  276 PHE B CD2 
4952 C CE1 . PHE B 275 ? 0.2266 0.2161 0.2519 0.0116  -0.0001 0.0071  276 PHE B CE1 
4953 C CE2 . PHE B 275 ? 0.2278 0.2005 0.2413 0.0156  0.0074  0.0124  276 PHE B CE2 
4954 C CZ  . PHE B 275 ? 0.2362 0.2211 0.2594 0.0104  0.0062  0.0102  276 PHE B CZ  
4955 N N   . SER B 276 ? 0.3034 0.2494 0.2891 0.0531  -0.0350 -0.0032 277 SER B N   
4956 C CA  . SER B 276 ? 0.3455 0.2806 0.3189 0.0645  -0.0473 -0.0074 277 SER B CA  
4957 C C   . SER B 276 ? 0.3853 0.3132 0.3460 0.0672  -0.0500 -0.0068 277 SER B C   
4958 O O   . SER B 276 ? 0.3382 0.2584 0.2860 0.0652  -0.0402 -0.0004 277 SER B O   
4959 C CB  . SER B 276 ? 0.3721 0.2876 0.3230 0.0748  -0.0466 -0.0045 277 SER B CB  
4960 O OG  . SER B 276 ? 0.4518 0.3552 0.3887 0.0877  -0.0603 -0.0095 277 SER B OG  
4961 N N   . TYR B 277 ? 0.3862 0.3164 0.3520 0.0718  -0.0635 -0.0142 278 TYR B N   
4962 C CA  . TYR B 277 ? 0.4012 0.3237 0.3545 0.0752  -0.0678 -0.0147 278 TYR B CA  
4963 C C   . TYR B 277 ? 0.4394 0.3404 0.3665 0.0911  -0.0795 -0.0176 278 TYR B C   
4964 O O   . TYR B 277 ? 0.4569 0.3572 0.3882 0.0983  -0.0912 -0.0242 278 TYR B O   
4965 C CB  . TYR B 277 ? 0.3628 0.3029 0.3416 0.0683  -0.0743 -0.0212 278 TYR B CB  
4966 C CG  . TYR B 277 ? 0.4280 0.3606 0.3952 0.0711  -0.0787 -0.0221 278 TYR B CG  
4967 C CD1 . TYR B 277 ? 0.3936 0.3271 0.3556 0.0644  -0.0676 -0.0158 278 TYR B CD1 
4968 C CD2 . TYR B 277 ? 0.4862 0.4104 0.4475 0.0812  -0.0948 -0.0298 278 TYR B CD2 
4969 C CE1 . TYR B 277 ? 0.4707 0.3967 0.4211 0.0673  -0.0713 -0.0164 278 TYR B CE1 
4970 C CE2 . TYR B 277 ? 0.4357 0.3519 0.3851 0.0843  -0.0994 -0.0310 278 TYR B CE2 
4971 C CZ  . TYR B 277 ? 0.5009 0.4179 0.4444 0.0772  -0.0870 -0.0239 278 TYR B CZ  
4972 O OH  . TYR B 277 ? 0.5445 0.4530 0.4755 0.0805  -0.0913 -0.0249 278 TYR B OH  
4973 N N   . PRO B 278 ? 0.4571 0.3390 0.3559 0.0980  -0.0767 -0.0131 279 PRO B N   
4974 C CA  . PRO B 278 ? 0.4428 0.3238 0.3355 0.0912  -0.0632 -0.0055 279 PRO B CA  
4975 C C   . PRO B 278 ? 0.4234 0.3047 0.3163 0.0846  -0.0460 0.0031  279 PRO B C   
4976 O O   . PRO B 278 ? 0.4325 0.3025 0.3143 0.0900  -0.0423 0.0059  279 PRO B O   
4977 C CB  . PRO B 278 ? 0.5101 0.3655 0.3683 0.1048  -0.0669 -0.0039 279 PRO B CB  
4978 C CG  . PRO B 278 ? 0.5060 0.3433 0.3444 0.1192  -0.0755 -0.0065 279 PRO B CG  
4979 C CD  . PRO B 278 ? 0.5406 0.3977 0.4085 0.1153  -0.0874 -0.0154 279 PRO B CD  
4980 N N   . ALA B 279 ? 0.3952 0.2897 0.3025 0.0729  -0.0359 0.0067  280 ALA B N   
4981 C CA  . ALA B 279 ? 0.3959 0.2911 0.3058 0.0663  -0.0205 0.0139  280 ALA B CA  
4982 C C   . ALA B 279 ? 0.4453 0.3278 0.3386 0.0680  -0.0103 0.0206  280 ALA B C   
4983 O O   . ALA B 279 ? 0.4350 0.3195 0.3264 0.0673  -0.0131 0.0197  280 ALA B O   
4984 C CB  . ALA B 279 ? 0.3960 0.3149 0.3348 0.0528  -0.0171 0.0123  280 ALA B CB  
4985 N N   . THR B 280 ? 0.4543 0.3230 0.3362 0.0704  0.0022  0.0275  281 THR B N   
4986 C CA  . THR B 280 ? 0.4558 0.3135 0.3263 0.0711  0.0145  0.0344  281 THR B CA  
4987 C C   . THR B 280 ? 0.3848 0.2628 0.2799 0.0578  0.0207  0.0350  281 THR B C   
4988 O O   . THR B 280 ? 0.3599 0.2561 0.2777 0.0487  0.0192  0.0319  281 THR B O   
4989 C CB  . THR B 280 ? 0.4829 0.3204 0.3388 0.0766  0.0282  0.0417  281 THR B CB  
4990 O OG1 . THR B 280 ? 0.4442 0.2944 0.3233 0.0665  0.0358  0.0425  281 THR B OG1 
4991 C CG2 . THR B 280 ? 0.5342 0.3511 0.3649 0.0906  0.0214  0.0406  281 THR B CG2 
4992 N N   . LEU B 281 ? 0.3955 0.2690 0.2843 0.0577  0.0273  0.0389  282 LEU B N   
4993 C CA  . LEU B 281 ? 0.3518 0.2423 0.2621 0.0466  0.0336  0.0397  282 LEU B CA  
4994 C C   . LEU B 281 ? 0.3730 0.2688 0.3003 0.0399  0.0436  0.0420  282 LEU B C   
4995 O O   . LEU B 281 ? 0.3392 0.2537 0.2889 0.0305  0.0424  0.0389  282 LEU B O   
4996 C CB  . LEU B 281 ? 0.3791 0.2610 0.2783 0.0492  0.0407  0.0442  282 LEU B CB  
4997 C CG  . LEU B 281 ? 0.3744 0.2709 0.2943 0.0394  0.0486  0.0457  282 LEU B CG  
4998 C CD1 . LEU B 281 ? 0.3487 0.2671 0.2866 0.0310  0.0390  0.0396  282 LEU B CD1 
4999 C CD2 . LEU B 281 ? 0.4782 0.3632 0.3857 0.0435  0.0575  0.0510  282 LEU B CD2 
5000 N N   . GLN B 282 ? 0.3678 0.2461 0.2843 0.0454  0.0533  0.0470  283 GLN B N   
5001 C CA  . GLN B 282 ? 0.3676 0.2497 0.3022 0.0390  0.0631  0.0488  283 GLN B CA  
5002 C C   . GLN B 282 ? 0.3743 0.2708 0.3242 0.0337  0.0546  0.0431  283 GLN B C   
5003 O O   . GLN B 282 ? 0.3416 0.2512 0.3135 0.0251  0.0571  0.0412  283 GLN B O   
5004 C CB  . GLN B 282 ? 0.4447 0.3024 0.3633 0.0468  0.0759  0.0555  283 GLN B CB  
5005 C CG  . GLN B 282 ? 0.4911 0.3514 0.4314 0.0397  0.0886  0.0578  283 GLN B CG  
5006 C CD  . GLN B 282 ? 0.5234 0.3963 0.4850 0.0316  0.0948  0.0581  283 GLN B CD  
5007 O OE1 . GLN B 282 ? 0.5356 0.3995 0.4883 0.0352  0.1025  0.0627  283 GLN B OE1 
5008 N NE2 . GLN B 282 ? 0.4321 0.3253 0.4210 0.0216  0.0907  0.0530  283 GLN B NE2 
5009 N N   . THR B 283 ? 0.3561 0.2494 0.2946 0.0395  0.0442  0.0399  284 THR B N   
5010 C CA  . THR B 283 ? 0.3113 0.2186 0.2643 0.0350  0.0362  0.0344  284 THR B CA  
5011 C C   . THR B 283 ? 0.2886 0.2178 0.2616 0.0257  0.0314  0.0300  284 THR B C   
5012 O O   . THR B 283 ? 0.2975 0.2381 0.2873 0.0191  0.0319  0.0276  284 THR B O   
5013 C CB  . THR B 283 ? 0.3255 0.2271 0.2651 0.0432  0.0249  0.0310  284 THR B CB  
5014 O OG1 . THR B 283 ? 0.3570 0.2377 0.2781 0.0522  0.0295  0.0347  284 THR B OG1 
5015 C CG2 . THR B 283 ? 0.3024 0.2213 0.2597 0.0381  0.0164  0.0248  284 THR B CG2 
5016 N N   . LEU B 284 ? 0.3075 0.2410 0.2773 0.0257  0.0272  0.0290  285 LEU B N   
5017 C CA  . LEU B 284 ? 0.2638 0.2155 0.2497 0.0180  0.0233  0.0252  285 LEU B CA  
5018 C C   . LEU B 284 ? 0.2914 0.2496 0.2904 0.0114  0.0311  0.0268  285 LEU B C   
5019 O O   . LEU B 284 ? 0.2728 0.2441 0.2863 0.0055  0.0291  0.0234  285 LEU B O   
5020 C CB  . LEU B 284 ? 0.2653 0.2183 0.2443 0.0199  0.0173  0.0238  285 LEU B CB  
5021 C CG  . LEU B 284 ? 0.2508 0.1988 0.2208 0.0266  0.0072  0.0203  285 LEU B CG  
5022 C CD1 . LEU B 284 ? 0.3260 0.2747 0.2911 0.0282  0.0012  0.0183  285 LEU B CD1 
5023 C CD2 . LEU B 284 ? 0.2593 0.2195 0.2447 0.0233  0.0015  0.0153  285 LEU B CD2 
5024 N N   . LEU B 285 ? 0.2895 0.2378 0.2838 0.0130  0.0402  0.0317  286 LEU B N   
5025 C CA  . LEU B 285 ? 0.2921 0.2465 0.3026 0.0071  0.0474  0.0324  286 LEU B CA  
5026 C C   . LEU B 285 ? 0.2941 0.2510 0.3186 0.0035  0.0496  0.0307  286 LEU B C   
5027 O O   . LEU B 285 ? 0.3038 0.2721 0.3457 -0.0024 0.0488  0.0273  286 LEU B O   
5028 C CB  . LEU B 285 ? 0.3112 0.2533 0.3154 0.0102  0.0582  0.0384  286 LEU B CB  
5029 C CG  . LEU B 285 ? 0.3281 0.2670 0.3185 0.0138  0.0566  0.0401  286 LEU B CG  
5030 C CD1 . LEU B 285 ? 0.3789 0.3018 0.3598 0.0186  0.0691  0.0469  286 LEU B CD1 
5031 C CD2 . LEU B 285 ? 0.3087 0.2641 0.3116 0.0078  0.0521  0.0366  286 LEU B CD2 
5032 N N   . ASP B 286 ? 0.3075 0.2528 0.3236 0.0077  0.0518  0.0325  287 ASP B N   
5033 C CA  . ASP B 286 ? 0.2853 0.2311 0.3136 0.0047  0.0542  0.0310  287 ASP B CA  
5034 C C   . ASP B 286 ? 0.3023 0.2631 0.3412 0.0004  0.0449  0.0247  287 ASP B C   
5035 O O   . ASP B 286 ? 0.3182 0.2837 0.3716 -0.0038 0.0455  0.0218  287 ASP B O   
5036 C CB  . ASP B 286 ? 0.3174 0.2468 0.3313 0.0112  0.0575  0.0341  287 ASP B CB  
5037 C CG  . ASP B 286 ? 0.4100 0.3206 0.4134 0.0161  0.0702  0.0411  287 ASP B CG  
5038 O OD1 . ASP B 286 ? 0.4182 0.3300 0.4311 0.0130  0.0779  0.0433  287 ASP B OD1 
5039 O OD2 . ASP B 286 ? 0.4477 0.3412 0.4327 0.0239  0.0729  0.0445  287 ASP B OD2 
5040 N N   . SER B 287 ? 0.2717 0.2388 0.3037 0.0018  0.0366  0.0224  288 SER B N   
5041 C CA  . SER B 287 ? 0.2756 0.2547 0.3159 -0.0013 0.0297  0.0172  288 SER B CA  
5042 C C   . SER B 287 ? 0.2816 0.2710 0.3347 -0.0066 0.0295  0.0143  288 SER B C   
5043 O O   . SER B 287 ? 0.2967 0.2928 0.3564 -0.0086 0.0257  0.0102  288 SER B O   
5044 C CB  . SER B 287 ? 0.2415 0.2247 0.2746 0.0012  0.0228  0.0155  288 SER B CB  
5045 O OG  . SER B 287 ? 0.2516 0.2396 0.2837 -0.0003 0.0221  0.0158  288 SER B OG  
5046 N N   . ASN B 288 ? 0.2512 0.2411 0.3071 -0.0080 0.0331  0.0161  289 ASN B N   
5047 C CA  . ASN B 288 ? 0.2601 0.2593 0.3281 -0.0119 0.0316  0.0126  289 ASN B CA  
5048 C C   . ASN B 288 ? 0.2918 0.2891 0.3750 -0.0145 0.0369  0.0123  289 ASN B C   
5049 O O   . ASN B 288 ? 0.3073 0.3110 0.4018 -0.0169 0.0360  0.0097  289 ASN B O   
5050 C CB  . ASN B 288 ? 0.2833 0.2864 0.3463 -0.0117 0.0308  0.0137  289 ASN B CB  
5051 C CG  . ASN B 288 ? 0.3288 0.3412 0.4003 -0.0141 0.0270  0.0094  289 ASN B CG  
5052 O OD1 . ASN B 288 ? 0.3369 0.3513 0.4163 -0.0153 0.0291  0.0093  289 ASN B OD1 
5053 N ND2 . ASN B 288 ? 0.3398 0.3567 0.4094 -0.0140 0.0216  0.0055  289 ASN B ND2 
5054 N N   . SER B 289 ? 0.2877 0.2760 0.3725 -0.0138 0.0423  0.0146  290 SER B N   
5055 C CA  . SER B 289 ? 0.2907 0.2766 0.3934 -0.0168 0.0486  0.0141  290 SER B CA  
5056 C C   . SER B 289 ? 0.2449 0.2397 0.3638 -0.0203 0.0417  0.0065  290 SER B C   
5057 O O   . SER B 289 ? 0.2796 0.2784 0.3926 -0.0195 0.0341  0.0029  290 SER B O   
5058 C CB  . SER B 289 ? 0.3074 0.2796 0.4066 -0.0148 0.0568  0.0184  290 SER B CB  
5059 O OG  . SER B 289 ? 0.3212 0.2929 0.4182 -0.0144 0.0519  0.0155  290 SER B OG  
5060 N N   . GLU B 290 ? 0.2942 0.2914 0.4344 -0.0235 0.0444  0.0039  291 GLU B N   
5061 C CA  . GLU B 290 ? 0.2761 0.2801 0.4322 -0.0258 0.0363  -0.0045 291 GLU B CA  
5062 C C   . GLU B 290 ? 0.2595 0.2582 0.4140 -0.0256 0.0347  -0.0064 291 GLU B C   
5063 O O   . GLU B 290 ? 0.2492 0.2519 0.4031 -0.0250 0.0256  -0.0125 291 GLU B O   
5064 C CB  . GLU B 290 ? 0.3877 0.3946 0.5713 -0.0293 0.0394  -0.0077 291 GLU B CB  
5065 C CG  . GLU B 290 ? 0.4335 0.4492 0.6317 -0.0301 0.0274  -0.0179 291 GLU B CG  
5066 C CD  . GLU B 290 ? 0.5471 0.5628 0.7763 -0.0339 0.0287  -0.0235 291 GLU B CD  
5067 O OE1 . GLU B 290 ? 0.6066 0.6171 0.8502 -0.0366 0.0412  -0.0188 291 GLU B OE1 
5068 O OE2 . GLU B 290 ? 0.5903 0.6099 0.8294 -0.0337 0.0175  -0.0328 291 GLU B OE2 
5069 N N   . GLN B 291 ? 0.2911 0.2791 0.4427 -0.0252 0.0438  -0.0009 292 GLN B N   
5070 C CA  . GLN B 291 ? 0.2843 0.2664 0.4328 -0.0245 0.0428  -0.0022 292 GLN B CA  
5071 C C   . GLN B 291 ? 0.2697 0.2548 0.3987 -0.0211 0.0350  -0.0030 292 GLN B C   
5072 O O   . GLN B 291 ? 0.2881 0.2747 0.4180 -0.0209 0.0287  -0.0080 292 GLN B O   
5073 C CB  . GLN B 291 ? 0.3197 0.2876 0.4640 -0.0232 0.0547  0.0048  292 GLN B CB  
5074 C CG  . GLN B 291 ? 0.2917 0.2517 0.4316 -0.0219 0.0546  0.0042  292 GLN B CG  
5075 C CD  . GLN B 291 ? 0.3894 0.3514 0.5511 -0.0260 0.0516  -0.0030 292 GLN B CD  
5076 O OE1 . GLN B 291 ? 0.3921 0.3569 0.5768 -0.0301 0.0539  -0.0061 292 GLN B OE1 
5077 N NE2 . GLN B 291 ? 0.3426 0.3029 0.4982 -0.0245 0.0459  -0.0062 292 GLN B NE2 
5078 N N   . ILE B 292 ? 0.2836 0.2694 0.3961 -0.0183 0.0352  0.0014  293 ILE B N   
5079 C CA  . ILE B 292 ? 0.2682 0.2568 0.3662 -0.0153 0.0291  0.0006  293 ILE B CA  
5080 C C   . ILE B 292 ? 0.2304 0.2285 0.3298 -0.0159 0.0214  -0.0049 293 ILE B C   
5081 O O   . ILE B 292 ? 0.2443 0.2436 0.3386 -0.0141 0.0169  -0.0079 293 ILE B O   
5082 C CB  . ILE B 292 ? 0.2827 0.2690 0.3653 -0.0121 0.0308  0.0059  293 ILE B CB  
5083 C CG1 . ILE B 292 ? 0.3431 0.3167 0.4183 -0.0089 0.0373  0.0110  293 ILE B CG1 
5084 C CG2 . ILE B 292 ? 0.2498 0.2415 0.3232 -0.0098 0.0245  0.0040  293 ILE B CG2 
5085 C CD1 . ILE B 292 ? 0.3590 0.3276 0.4312 -0.0069 0.0359  0.0098  293 ILE B CD1 
5086 N N   . VAL B 293 ? 0.2420 0.2456 0.3466 -0.0173 0.0202  -0.0061 294 VAL B N   
5087 C CA  . VAL B 293 ? 0.2422 0.2525 0.3431 -0.0161 0.0135  -0.0104 294 VAL B CA  
5088 C C   . VAL B 293 ? 0.2726 0.2836 0.3829 -0.0161 0.0073  -0.0178 294 VAL B C   
5089 O O   . VAL B 293 ? 0.2870 0.2988 0.3889 -0.0131 0.0018  -0.0216 294 VAL B O   
5090 C CB  . VAL B 293 ? 0.2481 0.2629 0.3486 -0.0166 0.0142  -0.0087 294 VAL B CB  
5091 C CG1 . VAL B 293 ? 0.3071 0.3265 0.4021 -0.0145 0.0078  -0.0131 294 VAL B CG1 
5092 C CG2 . VAL B 293 ? 0.2450 0.2577 0.3342 -0.0158 0.0189  -0.0023 294 VAL B CG2 
5093 N N   . MET B 294 ? 0.2958 0.3056 0.4238 -0.0189 0.0084  -0.0202 295 MET B N   
5094 C CA  . MET B 294 ? 0.3258 0.3371 0.4661 -0.0188 0.0005  -0.0287 295 MET B CA  
5095 C C   . MET B 294 ? 0.3294 0.3350 0.4773 -0.0195 -0.0006 -0.0322 295 MET B C   
5096 O O   . MET B 294 ? 0.3568 0.3623 0.5118 -0.0181 -0.0090 -0.0404 295 MET B O   
5097 C CB  . MET B 294 ? 0.3678 0.3836 0.5286 -0.0215 0.0006  -0.0312 295 MET B CB  
5098 C CG  . MET B 294 ? 0.3762 0.3976 0.5301 -0.0203 0.0002  -0.0291 295 MET B CG  
5099 S SD  . MET B 294 ? 0.5062 0.5292 0.6399 -0.0142 -0.0099 -0.0337 295 MET B SD  
5100 C CE  . MET B 294 ? 0.4465 0.4692 0.5946 -0.0119 -0.0222 -0.0457 295 MET B CE  
5101 N N   . LYS B 295 ? 0.3095 0.3093 0.4548 -0.0207 0.0069  -0.0268 296 LYS B N   
5102 C CA  . LYS B 295 ? 0.3150 0.3083 0.4684 -0.0217 0.0072  -0.0295 296 LYS B CA  
5103 C C   . LYS B 295 ? 0.3166 0.3052 0.4520 -0.0184 0.0078  -0.0268 296 LYS B C   
5104 O O   . LYS B 295 ? 0.2795 0.2694 0.3997 -0.0164 0.0104  -0.0214 296 LYS B O   
5105 C CB  . LYS B 295 ? 0.3258 0.3138 0.4954 -0.0258 0.0172  -0.0257 296 LYS B CB  
5106 C CG  . LYS B 295 ? 0.4007 0.3935 0.5923 -0.0293 0.0192  -0.0276 296 LYS B CG  
5107 C CD  . LYS B 295 ? 0.4404 0.4374 0.6519 -0.0304 0.0088  -0.0386 296 LYS B CD  
5108 C CE  . LYS B 295 ? 0.4420 0.4451 0.6791 -0.0337 0.0100  -0.0414 296 LYS B CE  
5109 N NZ  . LYS B 295 ? 0.4749 0.4723 0.7316 -0.0384 0.0240  -0.0366 296 LYS B NZ  
5110 N N   . PRO B 296 ? 0.3005 0.2839 0.4383 -0.0177 0.0049  -0.0310 297 PRO B N   
5111 C CA  . PRO B 296 ? 0.2684 0.2467 0.3918 -0.0147 0.0069  -0.0279 297 PRO B CA  
5112 C C   . PRO B 296 ? 0.2880 0.2601 0.4107 -0.0157 0.0162  -0.0208 297 PRO B C   
5113 O O   . PRO B 296 ? 0.3027 0.2700 0.4388 -0.0189 0.0219  -0.0196 297 PRO B O   
5114 C CB  . PRO B 296 ? 0.3294 0.3027 0.4576 -0.0137 0.0013  -0.0349 297 PRO B CB  
5115 C CG  . PRO B 296 ? 0.3563 0.3328 0.4981 -0.0149 -0.0062 -0.0428 297 PRO B CG  
5116 C CD  . PRO B 296 ? 0.3317 0.3138 0.4854 -0.0188 -0.0019 -0.0398 297 PRO B CD  
5117 N N   . ASN B 297 ? 0.2343 0.2054 0.3416 -0.0122 0.0179  -0.0162 298 ASN B N   
5118 C CA  . ASN B 297 ? 0.2354 0.1985 0.3369 -0.0108 0.0251  -0.0098 298 ASN B CA  
5119 C C   . ASN B 297 ? 0.2318 0.1914 0.3219 -0.0064 0.0236  -0.0093 298 ASN B C   
5120 O O   . ASN B 297 ? 0.2293 0.1953 0.3121 -0.0040 0.0191  -0.0105 298 ASN B O   
5121 C CB  . ASN B 297 ? 0.2402 0.2054 0.3340 -0.0099 0.0282  -0.0043 298 ASN B CB  
5122 C CG  . ASN B 297 ? 0.3004 0.2679 0.4054 -0.0137 0.0314  -0.0039 298 ASN B CG  
5123 O OD1 . ASN B 297 ? 0.3194 0.2789 0.4311 -0.0151 0.0393  -0.0007 298 ASN B OD1 
5124 N ND2 . ASN B 297 ? 0.2669 0.2443 0.3742 -0.0150 0.0262  -0.0069 298 ASN B ND2 
5125 N N   . LYS B 298 ? 0.2419 0.1907 0.3314 -0.0052 0.0282  -0.0072 299 LYS B N   
5126 C CA  . LYS B 298 ? 0.2472 0.1915 0.3260 -0.0004 0.0271  -0.0064 299 LYS B CA  
5127 C C   . LYS B 298 ? 0.2472 0.1949 0.3141 0.0040  0.0258  -0.0028 299 LYS B C   
5128 O O   . LYS B 298 ? 0.2555 0.2004 0.3180 0.0047  0.0290  0.0014  299 LYS B O   
5129 C CB  . LYS B 298 ? 0.2607 0.1908 0.3393 0.0007  0.0335  -0.0038 299 LYS B CB  
5130 C CG  . LYS B 298 ? 0.2741 0.1991 0.3433 0.0059  0.0317  -0.0041 299 LYS B CG  
5131 C CD  . LYS B 298 ? 0.2831 0.1916 0.3490 0.0080  0.0390  -0.0005 299 LYS B CD  
5132 C CE  . LYS B 298 ? 0.3651 0.2679 0.4200 0.0142  0.0369  -0.0005 299 LYS B CE  
5133 N NZ  . LYS B 298 ? 0.3907 0.2753 0.4398 0.0172  0.0445  0.0032  299 LYS B NZ  
5134 N N   . VAL B 299 ? 0.2409 0.1942 0.3036 0.0071  0.0211  -0.0048 300 VAL B N   
5135 C CA  . VAL B 299 ? 0.2425 0.2000 0.2983 0.0111  0.0188  -0.0028 300 VAL B CA  
5136 C C   . VAL B 299 ? 0.2496 0.1977 0.2970 0.0172  0.0190  -0.0008 300 VAL B C   
5137 O O   . VAL B 299 ? 0.2628 0.2032 0.3094 0.0186  0.0207  -0.0013 300 VAL B O   
5138 C CB  . VAL B 299 ? 0.2290 0.1979 0.2877 0.0114  0.0147  -0.0061 300 VAL B CB  
5139 C CG1 . VAL B 299 ? 0.2418 0.2171 0.3054 0.0068  0.0143  -0.0084 300 VAL B CG1 
5140 C CG2 . VAL B 299 ? 0.2481 0.2156 0.3068 0.0144  0.0137  -0.0086 300 VAL B CG2 
5141 N N   . THR B 300 ? 0.2552 0.2032 0.2957 0.0216  0.0166  0.0012  301 THR B N   
5142 C CA  . THR B 300 ? 0.3006 0.2405 0.3317 0.0293  0.0143  0.0022  301 THR B CA  
5143 C C   . THR B 300 ? 0.2692 0.2207 0.3057 0.0322  0.0075  -0.0013 301 THR B C   
5144 O O   . THR B 300 ? 0.2501 0.2101 0.2902 0.0311  0.0044  -0.0021 301 THR B O   
5145 C CB  . THR B 300 ? 0.3136 0.2417 0.3315 0.0338  0.0159  0.0065  301 THR B CB  
5146 O OG1 . THR B 300 ? 0.4176 0.3344 0.4333 0.0310  0.0247  0.0102  301 THR B OG1 
5147 C CG2 . THR B 300 ? 0.3722 0.2900 0.3776 0.0437  0.0120  0.0068  301 THR B CG2 
5148 N N   . ALA B 301 ? 0.2716 0.2234 0.3106 0.0355  0.0057  -0.0036 302 ALA B N   
5149 C CA  . ALA B 301 ? 0.2890 0.2509 0.3361 0.0389  0.0002  -0.0071 302 ALA B CA  
5150 C C   . ALA B 301 ? 0.3275 0.2861 0.3686 0.0456  -0.0062 -0.0071 302 ALA B C   
5151 O O   . ALA B 301 ? 0.3554 0.2999 0.3819 0.0508  -0.0062 -0.0044 302 ALA B O   
5152 C CB  . ALA B 301 ? 0.2982 0.2591 0.3482 0.0422  0.0001  -0.0092 302 ALA B CB  
5153 N N   . ILE B 302 ? 0.3443 0.3146 0.3962 0.0459  -0.0113 -0.0103 303 ILE B N   
5154 C CA  . ILE B 302 ? 0.3923 0.3599 0.4398 0.0524  -0.0194 -0.0117 303 ILE B CA  
5155 C C   . ILE B 302 ? 0.4329 0.4057 0.4908 0.0591  -0.0270 -0.0168 303 ILE B C   
5156 O O   . ILE B 302 ? 0.4398 0.4248 0.5155 0.0563  -0.0256 -0.0197 303 ILE B O   
5157 C CB  . ILE B 302 ? 0.3565 0.3322 0.4093 0.0481  -0.0207 -0.0121 303 ILE B CB  
5158 C CG1 . ILE B 302 ? 0.3596 0.3517 0.4328 0.0418  -0.0185 -0.0149 303 ILE B CG1 
5159 C CG2 . ILE B 302 ? 0.3377 0.3059 0.3783 0.0435  -0.0141 -0.0070 303 ILE B CG2 
5160 C CD1 . ILE B 302 ? 0.3291 0.3283 0.4075 0.0375  -0.0192 -0.0152 303 ILE B CD1 
5161 N N   . SER B 303 ? 0.4800 0.4420 0.5259 0.0689  -0.0346 -0.0179 304 SER B N   
5162 C CA  . SER B 303 ? 0.5705 0.5372 0.6271 0.0768  -0.0446 -0.0239 304 SER B CA  
5163 C C   . SER B 303 ? 0.5841 0.5604 0.6537 0.0781  -0.0540 -0.0292 304 SER B C   
5164 O O   . SER B 303 ? 0.6005 0.5877 0.6908 0.0811  -0.0610 -0.0355 304 SER B O   
5165 C CB  . SER B 303 ? 0.6270 0.5754 0.6623 0.0885  -0.0499 -0.0234 304 SER B CB  
5166 O OG  . SER B 303 ? 0.6883 0.6221 0.7018 0.0934  -0.0524 -0.0208 304 SER B OG  
5167 N N   . LYS B 304 ? 0.5234 0.4960 0.5834 0.0758  -0.0539 -0.0270 305 LYS B N   
5168 C CA  . LYS B 304 ? 0.5627 0.5432 0.6342 0.0765  -0.0626 -0.0319 305 LYS B CA  
5169 C C   . LYS B 304 ? 0.4576 0.4392 0.5241 0.0682  -0.0558 -0.0276 305 LYS B C   
5170 O O   . LYS B 304 ? 0.4561 0.4293 0.5067 0.0646  -0.0467 -0.0212 305 LYS B O   
5171 C CB  . LYS B 304 ? 0.5664 0.5342 0.6233 0.0896  -0.0766 -0.0359 305 LYS B CB  
5172 C CG  . LYS B 304 ? 0.6065 0.5505 0.6275 0.0965  -0.0740 -0.0297 305 LYS B CG  
5173 C CD  . LYS B 304 ? 0.6739 0.6121 0.6817 0.0933  -0.0707 -0.0258 305 LYS B CD  
5174 C CE  . LYS B 304 ? 0.7743 0.6874 0.7473 0.1013  -0.0671 -0.0196 305 LYS B CE  
5175 N NZ  . LYS B 304 ? 0.7228 0.6314 0.6853 0.0986  -0.0640 -0.0163 305 LYS B NZ  
5176 N N   . GLU B 305 ? 0.5101 0.5026 0.5925 0.0651  -0.0600 -0.0315 306 GLU B N   
5177 C CA  . GLU B 305 ? 0.4503 0.4412 0.5245 0.0600  -0.0564 -0.0282 306 GLU B CA  
5178 C C   . GLU B 305 ? 0.4678 0.4447 0.5224 0.0693  -0.0664 -0.0294 306 GLU B C   
5179 O O   . GLU B 305 ? 0.4413 0.4118 0.4921 0.0796  -0.0776 -0.0342 306 GLU B O   
5180 C CB  . GLU B 305 ? 0.3826 0.3901 0.4816 0.0521  -0.0549 -0.0313 306 GLU B CB  
5181 C CG  . GLU B 305 ? 0.3445 0.3631 0.4593 0.0443  -0.0440 -0.0298 306 GLU B CG  
5182 C CD  . GLU B 305 ? 0.3845 0.4167 0.5225 0.0379  -0.0411 -0.0325 306 GLU B CD  
5183 O OE1 . GLU B 305 ? 0.3611 0.3933 0.4945 0.0334  -0.0386 -0.0304 306 GLU B OE1 
5184 O OE2 . GLU B 305 ? 0.3839 0.4260 0.5451 0.0376  -0.0405 -0.0366 306 GLU B OE2 
5185 N N   . PRO B 306 ? 0.4474 0.4177 0.4874 0.0670  -0.0628 -0.0252 307 PRO B N   
5186 C CA  . PRO B 306 ? 0.4500 0.4069 0.4718 0.0764  -0.0727 -0.0271 307 PRO B CA  
5187 C C   . PRO B 306 ? 0.4391 0.4057 0.4807 0.0797  -0.0869 -0.0367 307 PRO B C   
5188 O O   . PRO B 306 ? 0.4623 0.4469 0.5324 0.0715  -0.0856 -0.0402 307 PRO B O   
5189 C CB  . PRO B 306 ? 0.4271 0.3807 0.4378 0.0705  -0.0643 -0.0213 307 PRO B CB  
5190 C CG  . PRO B 306 ? 0.4138 0.3723 0.4283 0.0610  -0.0500 -0.0151 307 PRO B CG  
5191 C CD  . PRO B 306 ? 0.4073 0.3806 0.4453 0.0569  -0.0500 -0.0189 307 PRO B CD  
5192 N N   . SER B 307 ? 0.4608 0.4139 0.4871 0.0925  -0.1006 -0.0412 308 SER B N   
5193 C CA  . SER B 307 ? 0.4404 0.4013 0.4862 0.0967  -0.1165 -0.0518 308 SER B CA  
5194 C C   . SER B 307 ? 0.4440 0.4131 0.5008 0.0891  -0.1158 -0.0529 308 SER B C   
5195 O O   . SER B 307 ? 0.4478 0.4326 0.5356 0.0848  -0.1215 -0.0602 308 SER B O   
5196 C CB  . SER B 307 ? 0.4864 0.4276 0.5080 0.1138  -0.1325 -0.0567 308 SER B CB  
5197 O OG  . SER B 307 ? 0.6350 0.5625 0.6359 0.1214  -0.1297 -0.0527 308 SER B OG  
5198 N N   . VAL B 308 ? 0.4217 0.3798 0.4544 0.0875  -0.1083 -0.0458 309 VAL B N   
5199 C CA  . VAL B 308 ? 0.3941 0.3574 0.4323 0.0811  -0.1069 -0.0458 309 VAL B CA  
5200 C C   . VAL B 308 ? 0.3678 0.3339 0.4003 0.0703  -0.0889 -0.0359 309 VAL B C   
5201 O O   . VAL B 308 ? 0.3662 0.3198 0.3755 0.0725  -0.0807 -0.0286 309 VAL B O   
5202 C CB  . VAL B 308 ? 0.4291 0.3739 0.4412 0.0922  -0.1180 -0.0480 309 VAL B CB  
5203 C CG1 . VAL B 308 ? 0.4211 0.3725 0.4427 0.0858  -0.1185 -0.0497 309 VAL B CG1 
5204 C CG2 . VAL B 308 ? 0.4864 0.4241 0.4980 0.1059  -0.1375 -0.0580 309 VAL B CG2 
5205 N N   . LYS B 309 ? 0.3452 0.3655 0.3621 0.0702  -0.0867 0.0202  310 LYS B N   
5206 C CA  . LYS B 309 ? 0.2911 0.3077 0.3146 0.0616  -0.0723 0.0216  310 LYS B CA  
5207 C C   . LYS B 309 ? 0.2963 0.3138 0.3184 0.0537  -0.0706 0.0158  310 LYS B C   
5208 O O   . LYS B 309 ? 0.3066 0.3307 0.3306 0.0524  -0.0798 0.0091  310 LYS B O   
5209 C CB  . LYS B 309 ? 0.3263 0.3520 0.3761 0.0565  -0.0685 0.0207  310 LYS B CB  
5210 C CG  . LYS B 309 ? 0.3519 0.3763 0.4061 0.0640  -0.0680 0.0267  310 LYS B CG  
5211 C CD  . LYS B 309 ? 0.3855 0.4231 0.4678 0.0616  -0.0713 0.0228  310 LYS B CD  
5212 C CE  . LYS B 309 ? 0.4323 0.4822 0.5231 0.0654  -0.0870 0.0168  310 LYS B CE  
5213 N NZ  . LYS B 309 ? 0.4332 0.4944 0.5510 0.0671  -0.0902 0.0152  310 LYS B NZ  
5214 N N   . MET B 310 ? 0.2613 0.2724 0.2815 0.0484  -0.0586 0.0183  311 MET B N   
5215 C CA  . MET B 310 ? 0.2819 0.2949 0.3064 0.0403  -0.0553 0.0138  311 MET B CA  
5216 C C   . MET B 310 ? 0.2399 0.2534 0.2768 0.0335  -0.0451 0.0159  311 MET B C   
5217 O O   . MET B 310 ? 0.2210 0.2311 0.2594 0.0348  -0.0391 0.0207  311 MET B O   
5218 C CB  . MET B 310 ? 0.2836 0.2862 0.2877 0.0420  -0.0524 0.0141  311 MET B CB  
5219 C CG  . MET B 310 ? 0.2950 0.2863 0.2898 0.0426  -0.0397 0.0203  311 MET B CG  
5220 S SD  . MET B 310 ? 0.3875 0.3666 0.3618 0.0437  -0.0343 0.0197  311 MET B SD  
5221 C CE  . MET B 310 ? 0.3062 0.2936 0.2989 0.0341  -0.0313 0.0149  311 MET B CE  
5222 N N   . TYR B 311 ? 0.1965 0.2137 0.2416 0.0262  -0.0433 0.0122  312 TYR B N   
5223 C CA  . TYR B 311 ? 0.1823 0.2015 0.2395 0.0193  -0.0365 0.0130  312 TYR B CA  
5224 C C   . TYR B 311 ? 0.1999 0.2174 0.2556 0.0147  -0.0327 0.0120  312 TYR B C   
5225 O O   . TYR B 311 ? 0.2152 0.2331 0.2676 0.0148  -0.0364 0.0086  312 TYR B O   
5226 C CB  . TYR B 311 ? 0.1915 0.2189 0.2651 0.0148  -0.0399 0.0090  312 TYR B CB  
5227 C CG  . TYR B 311 ? 0.2164 0.2476 0.2967 0.0192  -0.0440 0.0092  312 TYR B CG  
5228 C CD1 . TYR B 311 ? 0.2027 0.2387 0.2827 0.0243  -0.0538 0.0061  312 TYR B CD1 
5229 C CD2 . TYR B 311 ? 0.2174 0.2477 0.3052 0.0183  -0.0382 0.0123  312 TYR B CD2 
5230 C CE1 . TYR B 311 ? 0.2362 0.2770 0.3246 0.0292  -0.0586 0.0064  312 TYR B CE1 
5231 C CE2 . TYR B 311 ? 0.2400 0.2739 0.3360 0.0231  -0.0415 0.0128  312 TYR B CE2 
5232 C CZ  . TYR B 311 ? 0.2512 0.2911 0.3485 0.0288  -0.0522 0.0101  312 TYR B CZ  
5233 O OH  . TYR B 311 ? 0.2658 0.3108 0.3737 0.0344  -0.0567 0.0107  312 TYR B OH  
5234 N N   . HIS B 312 ? 0.1711 0.1870 0.2306 0.0107  -0.0256 0.0145  313 HIS B N   
5235 C CA  . HIS B 312 ? 0.1656 0.1819 0.2276 0.0064  -0.0234 0.0136  313 HIS B CA  
5236 C C   . HIS B 312 ? 0.1744 0.1927 0.2451 0.0005  -0.0194 0.0147  313 HIS B C   
5237 O O   . HIS B 312 ? 0.1763 0.1941 0.2497 -0.0007 -0.0166 0.0161  313 HIS B O   
5238 C CB  . HIS B 312 ? 0.1850 0.1953 0.2372 0.0098  -0.0194 0.0151  313 HIS B CB  
5239 C CG  . HIS B 312 ? 0.1804 0.1859 0.2309 0.0103  -0.0110 0.0188  313 HIS B CG  
5240 N ND1 . HIS B 312 ? 0.2005 0.1993 0.2434 0.0130  -0.0050 0.0202  313 HIS B ND1 
5241 C CD2 . HIS B 312 ? 0.2023 0.2079 0.2580 0.0078  -0.0064 0.0209  313 HIS B CD2 
5242 C CE1 . HIS B 312 ? 0.1903 0.1856 0.2350 0.0122  0.0030  0.0229  313 HIS B CE1 
5243 N NE2 . HIS B 312 ? 0.2135 0.2130 0.2659 0.0090  0.0021  0.0232  313 HIS B NE2 
5244 N N   . LYS B 313 ? 0.1519 0.1719 0.2265 -0.0032 -0.0194 0.0139  314 LYS B N   
5245 C CA  . LYS B 313 ? 0.1505 0.1723 0.2314 -0.0086 -0.0170 0.0147  314 LYS B CA  
5246 C C   . LYS B 313 ? 0.2079 0.2313 0.2918 -0.0095 -0.0171 0.0150  314 LYS B C   
5247 O O   . LYS B 313 ? 0.1748 0.1983 0.2582 -0.0082 -0.0200 0.0138  314 LYS B O   
5248 C CB  . LYS B 313 ? 0.1713 0.1945 0.2559 -0.0132 -0.0196 0.0130  314 LYS B CB  
5249 C CG  . LYS B 313 ? 0.1668 0.1902 0.2541 -0.0190 -0.0178 0.0136  314 LYS B CG  
5250 C CD  . LYS B 313 ? 0.2011 0.2227 0.2887 -0.0204 -0.0126 0.0143  314 LYS B CD  
5251 C CE  . LYS B 313 ? 0.2307 0.2522 0.3198 -0.0270 -0.0113 0.0137  314 LYS B CE  
5252 N NZ  . LYS B 313 ? 0.2687 0.2934 0.3612 -0.0278 -0.0112 0.0141  314 LYS B NZ  
5253 N N   . THR B 314 ? 0.1906 0.2153 0.2791 -0.0119 -0.0137 0.0161  315 THR B N   
5254 C CA  . THR B 314 ? 0.1577 0.1860 0.2532 -0.0131 -0.0145 0.0163  315 THR B CA  
5255 C C   . THR B 314 ? 0.1872 0.2189 0.2867 -0.0184 -0.0186 0.0160  315 THR B C   
5256 O O   . THR B 314 ? 0.2016 0.2322 0.2990 -0.0221 -0.0181 0.0154  315 THR B O   
5257 C CB  . THR B 314 ? 0.2200 0.2487 0.3207 -0.0123 -0.0083 0.0170  315 THR B CB  
5258 O OG1 . THR B 314 ? 0.2577 0.2867 0.3607 -0.0162 -0.0050 0.0167  315 THR B OG1 
5259 C CG2 . THR B 314 ? 0.2430 0.2654 0.3360 -0.0068 -0.0032 0.0177  315 THR B CG2 
5260 N N   . GLY B 315 ? 0.2021 0.2370 0.3065 -0.0185 -0.0225 0.0166  316 GLY B N   
5261 C CA  . GLY B 315 ? 0.2161 0.2534 0.3221 -0.0228 -0.0273 0.0167  316 GLY B CA  
5262 C C   . GLY B 315 ? 0.2423 0.2844 0.3565 -0.0211 -0.0314 0.0180  316 GLY B C   
5263 O O   . GLY B 315 ? 0.2198 0.2614 0.3368 -0.0167 -0.0305 0.0189  316 GLY B O   
5264 N N   . SER B 316 ? 0.2180 0.2647 0.3363 -0.0244 -0.0361 0.0179  317 SER B N   
5265 C CA  . SER B 316 ? 0.2734 0.3259 0.4009 -0.0224 -0.0420 0.0195  317 SER B CA  
5266 C C   . SER B 316 ? 0.2992 0.3520 0.4210 -0.0259 -0.0502 0.0200  317 SER B C   
5267 O O   . SER B 316 ? 0.2475 0.2976 0.3614 -0.0312 -0.0500 0.0181  317 SER B O   
5268 C CB  . SER B 316 ? 0.2360 0.2971 0.3806 -0.0217 -0.0393 0.0181  317 SER B CB  
5269 O OG  . SER B 316 ? 0.2341 0.2923 0.3807 -0.0183 -0.0307 0.0179  317 SER B OG  
5270 N N   . THR B 317 ? 0.2445 0.2992 0.3691 -0.0227 -0.0571 0.0228  318 THR B N   
5271 C CA  . THR B 317 ? 0.3569 0.4138 0.4780 -0.0248 -0.0668 0.0236  318 THR B CA  
5272 C C   . THR B 317 ? 0.3440 0.4132 0.4845 -0.0218 -0.0726 0.0240  318 THR B C   
5273 O O   . THR B 317 ? 0.3369 0.4124 0.4937 -0.0195 -0.0670 0.0228  318 THR B O   
5274 C CB  . THR B 317 ? 0.3164 0.3628 0.4211 -0.0230 -0.0710 0.0275  318 THR B CB  
5275 O OG1 . THR B 317 ? 0.3503 0.3960 0.4612 -0.0163 -0.0708 0.0310  318 THR B OG1 
5276 C CG2 . THR B 317 ? 0.2758 0.3107 0.3648 -0.0264 -0.0643 0.0263  318 THR B CG2 
5277 N N   . ASN B 318 ? 0.3514 0.4237 0.4903 -0.0215 -0.0839 0.0256  319 ASN B N   
5278 C CA  . ASN B 318 ? 0.4376 0.5234 0.5977 -0.0180 -0.0911 0.0260  319 ASN B CA  
5279 C C   . ASN B 318 ? 0.3900 0.4768 0.5630 -0.0104 -0.0869 0.0293  319 ASN B C   
5280 O O   . ASN B 318 ? 0.3879 0.4853 0.5838 -0.0084 -0.0844 0.0277  319 ASN B O   
5281 C CB  . ASN B 318 ? 0.4309 0.5181 0.5835 -0.0174 -0.1056 0.0282  319 ASN B CB  
5282 C CG  . ASN B 318 ? 0.5150 0.6179 0.6919 -0.0133 -0.1150 0.0285  319 ASN B CG  
5283 O OD1 . ASN B 318 ? 0.5537 0.6693 0.7540 -0.0152 -0.1118 0.0239  319 ASN B OD1 
5284 N ND2 . ASN B 318 ? 0.4868 0.5887 0.6596 -0.0072 -0.1261 0.0339  319 ASN B ND2 
5285 N N   . ARG B 319 ? 0.4020 0.4770 0.5611 -0.0066 -0.0846 0.0335  320 ARG B N   
5286 C CA  . ARG B 319 ? 0.3686 0.4429 0.5382 0.0005  -0.0808 0.0365  320 ARG B CA  
5287 C C   . ARG B 319 ? 0.3382 0.4024 0.5000 0.0009  -0.0690 0.0356  320 ARG B C   
5288 O O   . ARG B 319 ? 0.3548 0.4179 0.5254 0.0059  -0.0641 0.0369  320 ARG B O   
5289 C CB  . ARG B 319 ? 0.4787 0.5479 0.6420 0.0063  -0.0892 0.0426  320 ARG B CB  
5290 C CG  . ARG B 319 ? 0.5699 0.6445 0.7533 0.0142  -0.0892 0.0458  320 ARG B CG  
5291 C CD  . ARG B 319 ? 0.6891 0.7703 0.8787 0.0190  -0.1032 0.0503  320 ARG B CD  
5292 N NE  . ARG B 319 ? 0.8018 0.8915 1.0168 0.0266  -0.1033 0.0527  320 ARG B NE  
5293 C CZ  . ARG B 319 ? 0.8596 0.9560 1.0852 0.0332  -0.1152 0.0574  320 ARG B CZ  
5294 N NH1 . ARG B 319 ? 0.8541 0.9489 1.0642 0.0333  -0.1287 0.0604  320 ARG B NH1 
5295 N NH2 . ARG B 319 ? 0.8961 1.0004 1.1478 0.0402  -0.1134 0.0592  320 ARG B NH2 
5296 N N   . PHE B 320 ? 0.2810 0.3383 0.4275 -0.0041 -0.0645 0.0330  321 PHE B N   
5297 C CA  . PHE B 320 ? 0.2532 0.3016 0.3915 -0.0036 -0.0558 0.0319  321 PHE B CA  
5298 C C   . PHE B 320 ? 0.2516 0.3020 0.3913 -0.0067 -0.0485 0.0278  321 PHE B C   
5299 O O   . PHE B 320 ? 0.2686 0.3241 0.4105 -0.0109 -0.0494 0.0257  321 PHE B O   
5300 C CB  . PHE B 320 ? 0.2625 0.2995 0.3818 -0.0057 -0.0565 0.0329  321 PHE B CB  
5301 C CG  . PHE B 320 ? 0.2876 0.3180 0.4019 -0.0017 -0.0609 0.0376  321 PHE B CG  
5302 C CD1 . PHE B 320 ? 0.3241 0.3552 0.4340 -0.0015 -0.0701 0.0409  321 PHE B CD1 
5303 C CD2 . PHE B 320 ? 0.2882 0.3106 0.4012 0.0019  -0.0557 0.0386  321 PHE B CD2 
5304 C CE1 . PHE B 320 ? 0.3861 0.4091 0.4891 0.0032  -0.0739 0.0462  321 PHE B CE1 
5305 C CE2 . PHE B 320 ? 0.2836 0.2980 0.3916 0.0060  -0.0583 0.0434  321 PHE B CE2 
5306 C CZ  . PHE B 320 ? 0.3748 0.3890 0.4772 0.0071  -0.0674 0.0477  321 PHE B CZ  
5307 N N   . GLY B 321 ? 0.2286 0.2741 0.3663 -0.0045 -0.0413 0.0265  322 GLY B N   
5308 C CA  . GLY B 321 ? 0.1997 0.2442 0.3344 -0.0063 -0.0347 0.0234  322 GLY B CA  
5309 C C   . GLY B 321 ? 0.2232 0.2593 0.3448 -0.0062 -0.0319 0.0219  322 GLY B C   
5310 O O   . GLY B 321 ? 0.1929 0.2241 0.3120 -0.0038 -0.0317 0.0224  322 GLY B O   
5311 N N   . THR B 322 ? 0.1739 0.2086 0.2884 -0.0089 -0.0298 0.0200  323 THR B N   
5312 C CA  . THR B 322 ? 0.1932 0.2221 0.2978 -0.0089 -0.0284 0.0179  323 THR B CA  
5313 C C   . THR B 322 ? 0.1813 0.2094 0.2823 -0.0078 -0.0240 0.0162  323 THR B C   
5314 O O   . THR B 322 ? 0.1841 0.2149 0.2876 -0.0090 -0.0218 0.0167  323 THR B O   
5315 C CB  . THR B 322 ? 0.2175 0.2441 0.3158 -0.0130 -0.0314 0.0177  323 THR B CB  
5316 O OG1 . THR B 322 ? 0.2752 0.3005 0.3736 -0.0138 -0.0355 0.0200  323 THR B OG1 
5317 C CG2 . THR B 322 ? 0.2127 0.2346 0.3053 -0.0129 -0.0304 0.0149  323 THR B CG2 
5318 N N   . TYR B 323 ? 0.1581 0.1819 0.2524 -0.0056 -0.0229 0.0141  324 TYR B N   
5319 C CA  . TYR B 323 ? 0.1790 0.2009 0.2663 -0.0040 -0.0207 0.0128  324 TYR B CA  
5320 C C   . TYR B 323 ? 0.1695 0.1890 0.2508 -0.0035 -0.0238 0.0097  324 TYR B C   
5321 O O   . TYR B 323 ? 0.1882 0.2056 0.2694 -0.0030 -0.0248 0.0077  324 TYR B O   
5322 C CB  . TYR B 323 ? 0.1684 0.1870 0.2532 -0.0002 -0.0153 0.0131  324 TYR B CB  
5323 C CG  . TYR B 323 ? 0.1941 0.2084 0.2682 0.0025  -0.0130 0.0128  324 TYR B CG  
5324 C CD1 . TYR B 323 ? 0.2033 0.2184 0.2771 0.0016  -0.0115 0.0145  324 TYR B CD1 
5325 C CD2 . TYR B 323 ? 0.2065 0.2146 0.2695 0.0064  -0.0122 0.0108  324 TYR B CD2 
5326 C CE1 . TYR B 323 ? 0.1959 0.2056 0.2590 0.0052  -0.0092 0.0153  324 TYR B CE1 
5327 C CE2 . TYR B 323 ? 0.2044 0.2072 0.2549 0.0099  -0.0111 0.0113  324 TYR B CE2 
5328 C CZ  . TYR B 323 ? 0.2043 0.2080 0.2552 0.0097  -0.0096 0.0139  324 TYR B CZ  
5329 O OH  . TYR B 323 ? 0.2259 0.2231 0.2637 0.0142  -0.0083 0.0153  324 TYR B OH  
5330 N N   . VAL B 324 ? 0.1583 0.1785 0.2364 -0.0038 -0.0252 0.0089  325 VAL B N   
5331 C CA  . VAL B 324 ? 0.1721 0.1920 0.2476 -0.0033 -0.0289 0.0052  325 VAL B CA  
5332 C C   . VAL B 324 ? 0.1839 0.2033 0.2529 0.0004  -0.0295 0.0054  325 VAL B C   
5333 O O   . VAL B 324 ? 0.1691 0.1885 0.2379 0.0007  -0.0268 0.0084  325 VAL B O   
5334 C CB  . VAL B 324 ? 0.2047 0.2266 0.2865 -0.0078 -0.0307 0.0040  325 VAL B CB  
5335 C CG1 . VAL B 324 ? 0.2506 0.2705 0.3354 -0.0103 -0.0304 0.0040  325 VAL B CG1 
5336 C CG2 . VAL B 324 ? 0.2281 0.2513 0.3119 -0.0101 -0.0289 0.0067  325 VAL B CG2 
5337 N N   . VAL B 325 ? 0.1771 0.1953 0.2400 0.0034  -0.0331 0.0020  326 VAL B N   
5338 C CA  . VAL B 325 ? 0.1827 0.1992 0.2365 0.0084  -0.0352 0.0025  326 VAL B CA  
5339 C C   . VAL B 325 ? 0.2194 0.2388 0.2726 0.0095  -0.0427 -0.0030 326 VAL B C   
5340 O O   . VAL B 325 ? 0.2068 0.2260 0.2611 0.0076  -0.0443 -0.0075 326 VAL B O   
5341 C CB  . VAL B 325 ? 0.1868 0.1957 0.2279 0.0125  -0.0304 0.0049  326 VAL B CB  
5342 C CG1 . VAL B 325 ? 0.1946 0.2000 0.2318 0.0123  -0.0297 0.0016  326 VAL B CG1 
5343 C CG2 . VAL B 325 ? 0.2196 0.2240 0.2470 0.0185  -0.0326 0.0060  326 VAL B CG2 
5344 N N   . PHE B 326 ? 0.2190 0.2413 0.2718 0.0127  -0.0474 -0.0030 327 PHE B N   
5345 C CA  . PHE B 326 ? 0.2112 0.2376 0.2645 0.0142  -0.0560 -0.0089 327 PHE B CA  
5346 C C   . PHE B 326 ? 0.2439 0.2701 0.2885 0.0212  -0.0616 -0.0071 327 PHE B C   
5347 O O   . PHE B 326 ? 0.2565 0.2808 0.2998 0.0239  -0.0581 -0.0013 327 PHE B O   
5348 C CB  . PHE B 326 ? 0.2098 0.2439 0.2815 0.0088  -0.0582 -0.0136 327 PHE B CB  
5349 C CG  . PHE B 326 ? 0.2194 0.2584 0.3025 0.0085  -0.0577 -0.0113 327 PHE B CG  
5350 C CD1 . PHE B 326 ? 0.2080 0.2449 0.2956 0.0048  -0.0503 -0.0070 327 PHE B CD1 
5351 C CD2 . PHE B 326 ? 0.2254 0.2710 0.3155 0.0117  -0.0648 -0.0140 327 PHE B CD2 
5352 C CE1 . PHE B 326 ? 0.2208 0.2604 0.3179 0.0041  -0.0485 -0.0054 327 PHE B CE1 
5353 C CE2 . PHE B 326 ? 0.2404 0.2899 0.3426 0.0116  -0.0632 -0.0120 327 PHE B CE2 
5354 C CZ  . PHE B 326 ? 0.1927 0.2384 0.2978 0.0075  -0.0543 -0.0077 327 PHE B CZ  
5355 N N   . ILE B 327 ? 0.2452 0.2726 0.2829 0.0244  -0.0703 -0.0121 328 ILE B N   
5356 C CA  . ILE B 327 ? 0.2803 0.3063 0.3056 0.0323  -0.0776 -0.0103 328 ILE B CA  
5357 C C   . ILE B 327 ? 0.3124 0.3495 0.3491 0.0329  -0.0899 -0.0175 328 ILE B C   
5358 O O   . ILE B 327 ? 0.2845 0.3224 0.3160 0.0321  -0.0964 -0.0245 328 ILE B O   
5359 C CB  . ILE B 327 ? 0.3114 0.3251 0.3104 0.0371  -0.0767 -0.0090 328 ILE B CB  
5360 C CG1 . ILE B 327 ? 0.3111 0.3148 0.3032 0.0358  -0.0635 -0.0030 328 ILE B CG1 
5361 C CG2 . ILE B 327 ? 0.3634 0.3736 0.3464 0.0462  -0.0846 -0.0062 328 ILE B CG2 
5362 C CD1 . ILE B 327 ? 0.3667 0.3578 0.3370 0.0379  -0.0595 -0.0036 328 ILE B CD1 
5363 N N   . PRO B 328 ? 0.2634 0.3093 0.3171 0.0339  -0.0929 -0.0166 329 PRO B N   
5364 C CA  . PRO B 328 ? 0.3250 0.3837 0.3960 0.0335  -0.1039 -0.0244 329 PRO B CA  
5365 C C   . PRO B 328 ? 0.3379 0.3980 0.3953 0.0398  -0.1175 -0.0286 329 PRO B C   
5366 O O   . PRO B 328 ? 0.3668 0.4349 0.4335 0.0364  -0.1254 -0.0381 329 PRO B O   
5367 C CB  . PRO B 328 ? 0.3489 0.4139 0.4370 0.0356  -0.1029 -0.0203 329 PRO B CB  
5368 C CG  . PRO B 328 ? 0.2882 0.3449 0.3736 0.0324  -0.0892 -0.0131 329 PRO B CG  
5369 C CD  . PRO B 328 ? 0.2841 0.3288 0.3449 0.0343  -0.0850 -0.0093 329 PRO B CD  
5370 N N   . LYS B 329 ? 0.3559 0.4073 0.3904 0.0486  -0.1203 -0.0221 330 LYS B N   
5371 C CA  . LYS B 329 ? 0.4267 0.4783 0.4450 0.0555  -0.1346 -0.0256 330 LYS B CA  
5372 C C   . LYS B 329 ? 0.4163 0.4622 0.4193 0.0514  -0.1361 -0.0330 330 LYS B C   
5373 O O   . LYS B 329 ? 0.3822 0.4333 0.3814 0.0528  -0.1493 -0.0410 330 LYS B O   
5374 C CB  . LYS B 329 ? 0.4260 0.4654 0.4187 0.0662  -0.1351 -0.0157 330 LYS B CB  
5375 C CG  . LYS B 329 ? 0.5129 0.5477 0.4800 0.0741  -0.1492 -0.0181 330 LYS B CG  
5376 C CD  . LYS B 329 ? 0.5423 0.5555 0.4730 0.0803  -0.1416 -0.0098 330 LYS B CD  
5377 C CE  . LYS B 329 ? 0.6413 0.6465 0.5414 0.0870  -0.1544 -0.0130 330 LYS B CE  
5378 N NZ  . LYS B 329 ? 0.5704 0.5857 0.4740 0.0961  -0.1726 -0.0129 330 LYS B NZ  
5379 N N   . GLU B 330 ? 0.3932 0.4286 0.3882 0.0464  -0.1228 -0.0309 331 GLU B N   
5380 C CA  . GLU B 330 ? 0.4010 0.4291 0.3821 0.0425  -0.1213 -0.0373 331 GLU B CA  
5381 C C   . GLU B 330 ? 0.3798 0.4161 0.3837 0.0327  -0.1184 -0.0455 331 GLU B C   
5382 O O   . GLU B 330 ? 0.3708 0.4008 0.3661 0.0287  -0.1157 -0.0511 331 GLU B O   
5383 C CB  . GLU B 330 ? 0.4469 0.4581 0.4067 0.0435  -0.1078 -0.0302 331 GLU B CB  
5384 C CG  . GLU B 330 ? 0.5081 0.5074 0.4425 0.0530  -0.1078 -0.0218 331 GLU B CG  
5385 C CD  . GLU B 330 ? 0.5550 0.5470 0.4621 0.0588  -0.1191 -0.0258 331 GLU B CD  
5386 O OE1 . GLU B 330 ? 0.5987 0.5920 0.5033 0.0544  -0.1237 -0.0353 331 GLU B OE1 
5387 O OE2 . GLU B 330 ? 0.5993 0.5833 0.4861 0.0679  -0.1231 -0.0195 331 GLU B OE2 
5388 N N   . ASN B 331 ? 0.3268 0.3750 0.3584 0.0288  -0.1178 -0.0462 332 ASN B N   
5389 C CA  . ASN B 331 ? 0.3376 0.3922 0.3912 0.0198  -0.1141 -0.0536 332 ASN B CA  
5390 C C   . ASN B 331 ? 0.3353 0.3790 0.3820 0.0149  -0.1015 -0.0519 332 ASN B C   
5391 O O   . ASN B 331 ? 0.3258 0.3683 0.3758 0.0094  -0.1000 -0.0594 332 ASN B O   
5392 C CB  . ASN B 331 ? 0.3688 0.4317 0.4292 0.0175  -0.1257 -0.0659 332 ASN B CB  
5393 C CG  . ASN B 331 ? 0.4085 0.4843 0.4794 0.0226  -0.1398 -0.0683 332 ASN B CG  
5394 O OD1 . ASN B 331 ? 0.4412 0.5250 0.5314 0.0234  -0.1386 -0.0645 332 ASN B OD1 
5395 N ND2 . ASN B 331 ? 0.4938 0.5716 0.5519 0.0264  -0.1534 -0.0747 332 ASN B ND2 
5396 N N   . ILE B 332 ? 0.3107 0.3468 0.3493 0.0168  -0.0922 -0.0423 333 ILE B N   
5397 C CA  . ILE B 332 ? 0.2970 0.3232 0.3285 0.0139  -0.0814 -0.0400 333 ILE B CA  
5398 C C   . ILE B 332 ? 0.2983 0.3235 0.3376 0.0126  -0.0720 -0.0315 333 ILE B C   
5399 O O   . ILE B 332 ? 0.2803 0.3084 0.3222 0.0155  -0.0726 -0.0261 333 ILE B O   
5400 C CB  . ILE B 332 ? 0.3176 0.3316 0.3226 0.0186  -0.0803 -0.0387 333 ILE B CB  
5401 C CG1 . ILE B 332 ? 0.3682 0.3731 0.3694 0.0153  -0.0695 -0.0383 333 ILE B CG1 
5402 C CG2 . ILE B 332 ? 0.3244 0.3334 0.3158 0.0255  -0.0789 -0.0298 333 ILE B CG2 
5403 C CD1 . ILE B 332 ? 0.4436 0.4359 0.4200 0.0186  -0.0680 -0.0399 333 ILE B CD1 
5404 N N   . GLY B 333 ? 0.2571 0.2782 0.3006 0.0083  -0.0637 -0.0306 334 GLY B N   
5405 C CA  . GLY B 333 ? 0.2096 0.2298 0.2593 0.0070  -0.0560 -0.0232 334 GLY B CA  
5406 C C   . GLY B 333 ? 0.2461 0.2600 0.2947 0.0047  -0.0484 -0.0221 334 GLY B C   
5407 O O   . GLY B 333 ? 0.2548 0.2651 0.3009 0.0032  -0.0481 -0.0273 334 GLY B O   
5408 N N   . LEU B 334 ? 0.1901 0.2027 0.2414 0.0045  -0.0424 -0.0154 335 LEU B N   
5409 C CA  . LEU B 334 ? 0.2185 0.2261 0.2706 0.0034  -0.0358 -0.0135 335 LEU B CA  
5410 C C   . LEU B 334 ? 0.2077 0.2182 0.2705 0.0008  -0.0327 -0.0083 335 LEU B C   
5411 O O   . LEU B 334 ? 0.2029 0.2169 0.2679 0.0007  -0.0332 -0.0049 335 LEU B O   
5412 C CB  . LEU B 334 ? 0.2570 0.2575 0.2965 0.0076  -0.0313 -0.0112 335 LEU B CB  
5413 C CG  . LEU B 334 ? 0.2418 0.2376 0.2842 0.0075  -0.0238 -0.0093 335 LEU B CG  
5414 C CD1 . LEU B 334 ? 0.2583 0.2446 0.2867 0.0107  -0.0192 -0.0112 335 LEU B CD1 
5415 C CD2 . LEU B 334 ? 0.2133 0.2123 0.2645 0.0072  -0.0199 -0.0029 335 LEU B CD2 
5416 N N   . VAL B 335 ? 0.1991 0.2074 0.2676 -0.0011 -0.0295 -0.0078 336 VAL B N   
5417 C CA  . VAL B 335 ? 0.1995 0.2095 0.2758 -0.0030 -0.0276 -0.0028 336 VAL B CA  
5418 C C   . VAL B 335 ? 0.2059 0.2128 0.2841 -0.0009 -0.0233 -0.0001 336 VAL B C   
5419 O O   . VAL B 335 ? 0.2155 0.2176 0.2928 -0.0002 -0.0211 -0.0027 336 VAL B O   
5420 C CB  . VAL B 335 ? 0.2887 0.2983 0.3710 -0.0069 -0.0286 -0.0042 336 VAL B CB  
5421 C CG1 . VAL B 335 ? 0.2342 0.2444 0.3204 -0.0085 -0.0279 0.0013  336 VAL B CG1 
5422 C CG2 . VAL B 335 ? 0.3686 0.3812 0.4525 -0.0091 -0.0319 -0.0085 336 VAL B CG2 
5423 N N   . MET B 336 ? 0.1822 0.1921 0.2647 -0.0003 -0.0218 0.0047  337 MET B N   
5424 C CA  . MET B 336 ? 0.1800 0.1893 0.2695 0.0016  -0.0185 0.0077  337 MET B CA  
5425 C C   . MET B 336 ? 0.1997 0.2131 0.2967 -0.0004 -0.0216 0.0117  337 MET B C   
5426 O O   . MET B 336 ? 0.1910 0.2086 0.2884 -0.0026 -0.0238 0.0132  337 MET B O   
5427 C CB  . MET B 336 ? 0.1728 0.1824 0.2627 0.0042  -0.0137 0.0091  337 MET B CB  
5428 C CG  . MET B 336 ? 0.1913 0.2016 0.2922 0.0063  -0.0098 0.0116  337 MET B CG  
5429 S SD  . MET B 336 ? 0.2645 0.2806 0.3750 0.0067  -0.0061 0.0144  337 MET B SD  
5430 C CE  . MET B 336 ? 0.2135 0.2383 0.3305 0.0027  -0.0140 0.0170  337 MET B CE  
5431 N N   . LEU B 337 ? 0.1661 0.1772 0.2680 0.0007  -0.0217 0.0135  338 LEU B N   
5432 C CA  . LEU B 337 ? 0.1799 0.1936 0.2870 0.0001  -0.0255 0.0179  338 LEU B CA  
5433 C C   . LEU B 337 ? 0.2078 0.2234 0.3255 0.0041  -0.0244 0.0211  338 LEU B C   
5434 O O   . LEU B 337 ? 0.1889 0.1996 0.3087 0.0070  -0.0205 0.0205  338 LEU B O   
5435 C CB  . LEU B 337 ? 0.2005 0.2077 0.3024 -0.0018 -0.0271 0.0182  338 LEU B CB  
5436 C CG  . LEU B 337 ? 0.2004 0.2053 0.2952 -0.0057 -0.0269 0.0140  338 LEU B CG  
5437 C CD1 . LEU B 337 ? 0.2211 0.2178 0.3126 -0.0076 -0.0258 0.0134  338 LEU B CD1 
5438 C CD2 . LEU B 337 ? 0.2253 0.2352 0.3183 -0.0087 -0.0295 0.0145  338 LEU B CD2 
5439 N N   . THR B 338 ? 0.2000 0.2233 0.3262 0.0043  -0.0276 0.0240  339 THR B N   
5440 C CA  . THR B 338 ? 0.2123 0.2398 0.3526 0.0083  -0.0277 0.0270  339 THR B CA  
5441 C C   . THR B 338 ? 0.2153 0.2475 0.3595 0.0083  -0.0362 0.0312  339 THR B C   
5442 O O   . THR B 338 ? 0.2141 0.2482 0.3515 0.0043  -0.0408 0.0311  339 THR B O   
5443 C CB  . THR B 338 ? 0.2307 0.2646 0.3819 0.0091  -0.0232 0.0257  339 THR B CB  
5444 O OG1 . THR B 338 ? 0.2382 0.2784 0.3892 0.0051  -0.0262 0.0251  339 THR B OG1 
5445 C CG2 . THR B 338 ? 0.2423 0.2694 0.3862 0.0098  -0.0149 0.0221  339 THR B CG2 
5446 N N   . ASN B 339 ? 0.2094 0.2427 0.3639 0.0132  -0.0382 0.0349  340 ASN B N   
5447 C CA  . ASN B 339 ? 0.2028 0.2412 0.3615 0.0145  -0.0478 0.0392  340 ASN B CA  
5448 C C   . ASN B 339 ? 0.2538 0.3058 0.4332 0.0162  -0.0506 0.0393  340 ASN B C   
5449 O O   . ASN B 339 ? 0.2530 0.3110 0.4417 0.0195  -0.0589 0.0431  340 ASN B O   
5450 C CB  . ASN B 339 ? 0.2358 0.2660 0.3913 0.0195  -0.0499 0.0441  340 ASN B CB  
5451 C CG  . ASN B 339 ? 0.2573 0.2850 0.4248 0.0251  -0.0428 0.0447  340 ASN B CG  
5452 O OD1 . ASN B 339 ? 0.2080 0.2432 0.3912 0.0266  -0.0390 0.0429  340 ASN B OD1 
5453 N ND2 . ASN B 339 ? 0.2962 0.3120 0.4563 0.0279  -0.0398 0.0469  340 ASN B ND2 
5454 N N   . LYS B 340 ? 0.2061 0.2625 0.3930 0.0141  -0.0437 0.0353  341 LYS B N   
5455 C CA  . LYS B 340 ? 0.2340 0.3030 0.4386 0.0128  -0.0452 0.0336  341 LYS B CA  
5456 C C   . LYS B 340 ? 0.2358 0.3037 0.4334 0.0075  -0.0387 0.0292  341 LYS B C   
5457 O O   . LYS B 340 ? 0.2660 0.3252 0.4528 0.0075  -0.0306 0.0275  341 LYS B O   
5458 C CB  . LYS B 340 ? 0.2137 0.2881 0.4412 0.0178  -0.0399 0.0338  341 LYS B CB  
5459 C CG  . LYS B 340 ? 0.2650 0.3547 0.5161 0.0167  -0.0434 0.0321  341 LYS B CG  
5460 C CD  . LYS B 340 ? 0.2562 0.3483 0.5263 0.0184  -0.0314 0.0294  341 LYS B CD  
5461 C CE  . LYS B 340 ? 0.2908 0.3985 0.5865 0.0162  -0.0338 0.0266  341 LYS B CE  
5462 N NZ  . LYS B 340 ? 0.2460 0.3552 0.5625 0.0177  -0.0203 0.0237  341 LYS B NZ  
5463 N N   . ARG B 341 ? 0.2477 0.3239 0.4506 0.0031  -0.0423 0.0273  342 ARG B N   
5464 C CA  . ARG B 341 ? 0.2413 0.3161 0.4403 -0.0013 -0.0348 0.0236  342 ARG B CA  
5465 C C   . ARG B 341 ? 0.2671 0.3413 0.4778 0.0012  -0.0233 0.0219  342 ARG B C   
5466 O O   . ARG B 341 ? 0.2821 0.3641 0.5141 0.0037  -0.0225 0.0218  342 ARG B O   
5467 C CB  . ARG B 341 ? 0.2923 0.3762 0.4980 -0.0067 -0.0398 0.0213  342 ARG B CB  
5468 C CG  . ARG B 341 ? 0.3293 0.4092 0.5166 -0.0112 -0.0459 0.0213  342 ARG B CG  
5469 C CD  . ARG B 341 ? 0.3792 0.4679 0.5746 -0.0169 -0.0503 0.0181  342 ARG B CD  
5470 N NE  . ARG B 341 ? 0.4266 0.5244 0.6315 -0.0159 -0.0625 0.0193  342 ARG B NE  
5471 C CZ  . ARG B 341 ? 0.4243 0.5339 0.6442 -0.0195 -0.0683 0.0159  342 ARG B CZ  
5472 N NH1 . ARG B 341 ? 0.4127 0.5262 0.6420 -0.0246 -0.0614 0.0109  342 ARG B NH1 
5473 N NH2 . ARG B 341 ? 0.4350 0.5522 0.6607 -0.0176 -0.0816 0.0175  342 ARG B NH2 
5474 N N   . ILE B 342 ? 0.2859 0.3503 0.4825 0.0010  -0.0146 0.0205  343 ILE B N   
5475 C CA  . ILE B 342 ? 0.2262 0.2866 0.4280 0.0024  -0.0022 0.0186  343 ILE B CA  
5476 C C   . ILE B 342 ? 0.2206 0.2765 0.4111 -0.0011 0.0030  0.0169  343 ILE B C   
5477 O O   . ILE B 342 ? 0.2364 0.2903 0.4128 -0.0037 -0.0022 0.0172  343 ILE B O   
5478 C CB  . ILE B 342 ? 0.2623 0.3119 0.4544 0.0070  0.0040  0.0190  343 ILE B CB  
5479 C CG1 . ILE B 342 ? 0.2894 0.3292 0.4565 0.0063  0.0030  0.0186  343 ILE B CG1 
5480 C CG2 . ILE B 342 ? 0.2461 0.2987 0.4486 0.0107  -0.0007 0.0212  343 ILE B CG2 
5481 C CD1 . ILE B 342 ? 0.2729 0.3014 0.4282 0.0097  0.0094  0.0175  343 ILE B CD1 
5482 N N   . PRO B 343 ? 0.2375 0.2909 0.4346 -0.0012 0.0142  0.0152  344 PRO B N   
5483 C CA  . PRO B 343 ? 0.2098 0.2581 0.3971 -0.0043 0.0199  0.0141  344 PRO B CA  
5484 C C   . PRO B 343 ? 0.2303 0.2677 0.3915 -0.0028 0.0191  0.0154  344 PRO B C   
5485 O O   . PRO B 343 ? 0.2236 0.2533 0.3729 0.0011  0.0204  0.0160  344 PRO B O   
5486 C CB  . PRO B 343 ? 0.2529 0.2963 0.4490 -0.0031 0.0344  0.0126  344 PRO B CB  
5487 C CG  . PRO B 343 ? 0.2504 0.3039 0.4720 -0.0019 0.0335  0.0117  344 PRO B CG  
5488 C CD  . PRO B 343 ? 0.2203 0.2751 0.4359 0.0012  0.0232  0.0141  344 PRO B CD  
5489 N N   . ASN B 344 ? 0.2248 0.2621 0.3784 -0.0060 0.0167  0.0154  345 ASN B N   
5490 C CA  . ASN B 344 ? 0.1932 0.2219 0.3255 -0.0045 0.0153  0.0165  345 ASN B CA  
5491 C C   . ASN B 344 ? 0.2095 0.2259 0.3279 0.0001  0.0244  0.0171  345 ASN B C   
5492 O O   . ASN B 344 ? 0.2254 0.2357 0.3278 0.0032  0.0213  0.0175  345 ASN B O   
5493 C CB  . ASN B 344 ? 0.2214 0.2511 0.3507 -0.0084 0.0144  0.0164  345 ASN B CB  
5494 C CG  . ASN B 344 ? 0.2152 0.2533 0.3494 -0.0127 0.0042  0.0158  345 ASN B CG  
5495 O OD1 . ASN B 344 ? 0.2574 0.2973 0.3892 -0.0118 -0.0032 0.0165  345 ASN B OD1 
5496 N ND2 . ASN B 344 ? 0.2949 0.3365 0.4346 -0.0177 0.0046  0.0145  345 ASN B ND2 
5497 N N   A GLU B 345 ? 0.2406 0.2527 0.3643 0.0005  0.0357  0.0168  346 GLU B N   
5498 N N   B GLU B 345 ? 0.2406 0.2527 0.3643 0.0005  0.0357  0.0168  346 GLU B N   
5499 C CA  A GLU B 345 ? 0.2715 0.2690 0.3787 0.0051  0.0456  0.0177  346 GLU B CA  
5500 C CA  B GLU B 345 ? 0.2716 0.2690 0.3784 0.0051  0.0455  0.0177  346 GLU B CA  
5501 C C   A GLU B 345 ? 0.2599 0.2529 0.3600 0.0088  0.0445  0.0170  346 GLU B C   
5502 C C   B GLU B 345 ? 0.2599 0.2529 0.3600 0.0088  0.0444  0.0170  346 GLU B C   
5503 O O   A GLU B 345 ? 0.2515 0.2332 0.3303 0.0126  0.0458  0.0174  346 GLU B O   
5504 O O   B GLU B 345 ? 0.2516 0.2333 0.3303 0.0126  0.0457  0.0174  346 GLU B O   
5505 C CB  A GLU B 345 ? 0.2778 0.2708 0.3948 0.0042  0.0598  0.0171  346 GLU B CB  
5506 C CB  B GLU B 345 ? 0.2783 0.2708 0.3943 0.0043  0.0598  0.0172  346 GLU B CB  
5507 C CG  A GLU B 345 ? 0.3070 0.3146 0.4532 -0.0009 0.0590  0.0147  346 GLU B CG  
5508 C CG  B GLU B 345 ? 0.3368 0.3178 0.4476 0.0082  0.0712  0.0169  346 GLU B CG  
5509 C CD  A GLU B 345 ? 0.2758 0.2906 0.4272 -0.0060 0.0541  0.0142  346 GLU B CD  
5510 C CD  B GLU B 345 ? 0.3087 0.2989 0.4456 0.0067  0.0741  0.0146  346 GLU B CD  
5511 O OE1 A GLU B 345 ? 0.3766 0.3827 0.5193 -0.0064 0.0622  0.0149  346 GLU B OE1 
5512 O OE1 B GLU B 345 ? 0.3735 0.3781 0.5342 0.0024  0.0702  0.0131  346 GLU B OE1 
5513 O OE2 A GLU B 345 ? 0.2238 0.2512 0.3859 -0.0093 0.0427  0.0131  346 GLU B OE2 
5514 O OE2 B GLU B 345 ? 0.3843 0.3673 0.5181 0.0098  0.0800  0.0140  346 GLU B OE2 
5515 N N   . GLU B 346 ? 0.2336 0.2353 0.3515 0.0078  0.0418  0.0159  347 GLU B N   
5516 C CA  . GLU B 346 ? 0.2622 0.2593 0.3752 0.0110  0.0417  0.0150  347 GLU B CA  
5517 C C   . GLU B 346 ? 0.2460 0.2425 0.3440 0.0116  0.0311  0.0147  347 GLU B C   
5518 O O   . GLU B 346 ? 0.2404 0.2277 0.3230 0.0144  0.0322  0.0132  347 GLU B O   
5519 C CB  . GLU B 346 ? 0.2679 0.2749 0.4053 0.0104  0.0409  0.0145  347 GLU B CB  
5520 C CG  . GLU B 346 ? 0.2941 0.3036 0.4517 0.0097  0.0518  0.0138  347 GLU B CG  
5521 C CD  . GLU B 346 ? 0.3544 0.3515 0.5085 0.0131  0.0653  0.0126  347 GLU B CD  
5522 O OE1 . GLU B 346 ? 0.3739 0.3568 0.5027 0.0157  0.0686  0.0124  347 GLU B OE1 
5523 O OE2 . GLU B 346 ? 0.3729 0.3745 0.5500 0.0132  0.0726  0.0116  347 GLU B OE2 
5524 N N   . ARG B 347 ? 0.1951 0.2008 0.2976 0.0087  0.0212  0.0154  348 ARG B N   
5525 C CA  . ARG B 347 ? 0.1840 0.1895 0.2753 0.0086  0.0122  0.0145  348 ARG B CA  
5526 C C   . ARG B 347 ? 0.2302 0.2270 0.3011 0.0110  0.0127  0.0140  348 ARG B C   
5527 O O   . ARG B 347 ? 0.2601 0.2521 0.3188 0.0129  0.0094  0.0119  348 ARG B O   
5528 C CB  . ARG B 347 ? 0.2073 0.2224 0.3067 0.0047  0.0037  0.0155  348 ARG B CB  
5529 C CG  . ARG B 347 ? 0.2015 0.2257 0.3197 0.0026  0.0017  0.0165  348 ARG B CG  
5530 C CD  . ARG B 347 ? 0.1947 0.2255 0.3154 -0.0015 -0.0061 0.0173  348 ARG B CD  
5531 N NE  . ARG B 347 ? 0.2011 0.2406 0.3381 -0.0036 -0.0085 0.0180  348 ARG B NE  
5532 C CZ  . ARG B 347 ? 0.2104 0.2555 0.3502 -0.0075 -0.0153 0.0184  348 ARG B CZ  
5533 N NH1 . ARG B 347 ? 0.2025 0.2448 0.3308 -0.0097 -0.0192 0.0184  348 ARG B NH1 
5534 N NH2 . ARG B 347 ? 0.2062 0.2598 0.3609 -0.0091 -0.0181 0.0185  348 ARG B NH2 
5535 N N   . ILE B 348 ? 0.2252 0.2198 0.2926 0.0110  0.0166  0.0159  349 ILE B N   
5536 C CA  . ILE B 348 ? 0.2341 0.2204 0.2822 0.0143  0.0165  0.0165  349 ILE B CA  
5537 C C   . ILE B 348 ? 0.2466 0.2200 0.2778 0.0188  0.0225  0.0157  349 ILE B C   
5538 O O   . ILE B 348 ? 0.2659 0.2338 0.2800 0.0219  0.0176  0.0143  349 ILE B O   
5539 C CB  . ILE B 348 ? 0.2187 0.2039 0.2677 0.0137  0.0212  0.0193  349 ILE B CB  
5540 C CG1 . ILE B 348 ? 0.2185 0.2146 0.2800 0.0090  0.0145  0.0194  349 ILE B CG1 
5541 C CG2 . ILE B 348 ? 0.2630 0.2373 0.2910 0.0188  0.0224  0.0211  349 ILE B CG2 
5542 C CD1 . ILE B 348 ? 0.2350 0.2313 0.3031 0.0065  0.0210  0.0210  349 ILE B CD1 
5543 N N   . LYS B 349 ? 0.2902 0.2584 0.3261 0.0192  0.0333  0.0159  350 LYS B N   
5544 C CA  . LYS B 349 ? 0.2922 0.2454 0.3100 0.0232  0.0412  0.0150  350 LYS B CA  
5545 C C   . LYS B 349 ? 0.2904 0.2424 0.3019 0.0238  0.0358  0.0112  350 LYS B C   
5546 O O   . LYS B 349 ? 0.3280 0.2693 0.3170 0.0269  0.0345  0.0094  350 LYS B O   
5547 C CB  . LYS B 349 ? 0.3050 0.2534 0.3335 0.0227  0.0556  0.0155  350 LYS B CB  
5548 C CG  . LYS B 349 ? 0.3820 0.3260 0.4119 0.0225  0.0651  0.0183  350 LYS B CG  
5549 C CD  . LYS B 349 ? 0.4144 0.3565 0.4615 0.0210  0.0791  0.0174  350 LYS B CD  
5550 C CE  . LYS B 349 ? 0.4855 0.4193 0.5321 0.0208  0.0921  0.0194  350 LYS B CE  
5551 N NZ  . LYS B 349 ? 0.5795 0.5107 0.6440 0.0193  0.1071  0.0176  350 LYS B NZ  
5552 N N   . ALA B 350 ? 0.2611 0.2231 0.2918 0.0209  0.0326  0.0098  351 ALA B N   
5553 C CA  . ALA B 350 ? 0.2822 0.2421 0.3087 0.0210  0.0291  0.0060  351 ALA B CA  
5554 C C   . ALA B 350 ? 0.2780 0.2394 0.2918 0.0210  0.0176  0.0035  351 ALA B C   
5555 O O   . ALA B 350 ? 0.2960 0.2494 0.2938 0.0224  0.0162  -0.0004 351 ALA B O   
5556 C CB  . ALA B 350 ? 0.2774 0.2474 0.3273 0.0186  0.0277  0.0062  351 ALA B CB  
5557 N N   . ALA B 351 ? 0.2499 0.2214 0.2712 0.0191  0.0096  0.0051  352 ALA B N   
5558 C CA  . ALA B 351 ? 0.2887 0.2632 0.3022 0.0189  -0.0009 0.0024  352 ALA B CA  
5559 C C   . ALA B 351 ? 0.2752 0.2405 0.2661 0.0233  -0.0020 0.0020  352 ALA B C   
5560 O O   . ALA B 351 ? 0.3063 0.2699 0.2859 0.0244  -0.0093 -0.0022 352 ALA B O   
5561 C CB  . ALA B 351 ? 0.2418 0.2276 0.2686 0.0160  -0.0069 0.0046  352 ALA B CB  
5562 N N   . TYR B 352 ? 0.2957 0.2546 0.2796 0.0261  0.0049  0.0064  353 TYR B N   
5563 C CA  . TYR B 352 ? 0.3082 0.2557 0.2676 0.0314  0.0046  0.0073  353 TYR B CA  
5564 C C   . TYR B 352 ? 0.3435 0.2781 0.2830 0.0336  0.0073  0.0033  353 TYR B C   
5565 O O   . TYR B 352 ? 0.3721 0.3012 0.2916 0.0369  0.0000  0.0009  353 TYR B O   
5566 C CB  . TYR B 352 ? 0.3401 0.2806 0.2962 0.0336  0.0146  0.0130  353 TYR B CB  
5567 C CG  . TYR B 352 ? 0.3426 0.2703 0.2728 0.0400  0.0143  0.0157  353 TYR B CG  
5568 C CD1 . TYR B 352 ? 0.3537 0.2635 0.2595 0.0441  0.0220  0.0158  353 TYR B CD1 
5569 C CD2 . TYR B 352 ? 0.3532 0.2855 0.2825 0.0424  0.0069  0.0186  353 TYR B CD2 
5570 C CE1 . TYR B 352 ? 0.4465 0.3425 0.3252 0.0508  0.0214  0.0191  353 TYR B CE1 
5571 C CE2 . TYR B 352 ? 0.4073 0.3274 0.3126 0.0495  0.0060  0.0220  353 TYR B CE2 
5572 C CZ  . TYR B 352 ? 0.4684 0.3702 0.3474 0.0538  0.0128  0.0224  353 TYR B CZ  
5573 O OH  . TYR B 352 ? 0.5343 0.4222 0.3863 0.0617  0.0115  0.0265  353 TYR B OH  
5574 N N   . ALA B 353 ? 0.3544 0.2839 0.2993 0.0319  0.0177  0.0025  354 ALA B N   
5575 C CA  . ALA B 353 ? 0.3542 0.2698 0.2800 0.0335  0.0222  -0.0017 354 ALA B CA  
5576 C C   . ALA B 353 ? 0.3803 0.3006 0.3038 0.0316  0.0112  -0.0084 354 ALA B C   
5577 O O   . ALA B 353 ? 0.4192 0.3297 0.3192 0.0338  0.0074  -0.0125 354 ALA B O   
5578 C CB  . ALA B 353 ? 0.3528 0.2637 0.2904 0.0318  0.0363  -0.0015 354 ALA B CB  
5579 N N   . VAL B 354 ? 0.3720 0.3065 0.3189 0.0273  0.0059  -0.0098 355 VAL B N   
5580 C CA  . VAL B 354 ? 0.3462 0.2849 0.2940 0.0246  -0.0028 -0.0166 355 VAL B CA  
5581 C C   . VAL B 354 ? 0.3642 0.3069 0.3010 0.0262  -0.0159 -0.0191 355 VAL B C   
5582 O O   . VAL B 354 ? 0.4024 0.3407 0.3247 0.0264  -0.0219 -0.0257 355 VAL B O   
5583 C CB  . VAL B 354 ? 0.3211 0.2723 0.2957 0.0201  -0.0042 -0.0164 355 VAL B CB  
5584 C CG1 . VAL B 354 ? 0.3090 0.2648 0.2860 0.0169  -0.0130 -0.0235 355 VAL B CG1 
5585 C CG2 . VAL B 354 ? 0.3374 0.2846 0.3227 0.0193  0.0071  -0.0149 355 VAL B CG2 
5586 N N   . LEU B 355 ? 0.3679 0.3193 0.3127 0.0273  -0.0206 -0.0145 356 LEU B N   
5587 C CA  . LEU B 355 ? 0.3445 0.3022 0.2846 0.0291  -0.0335 -0.0166 356 LEU B CA  
5588 C C   . LEU B 355 ? 0.3870 0.3328 0.2981 0.0351  -0.0367 -0.0170 356 LEU B C   
5589 O O   . LEU B 355 ? 0.4268 0.3760 0.3302 0.0367  -0.0489 -0.0217 356 LEU B O   
5590 C CB  . LEU B 355 ? 0.3266 0.2947 0.2821 0.0291  -0.0357 -0.0110 356 LEU B CB  
5591 C CG  . LEU B 355 ? 0.3214 0.3017 0.3028 0.0232  -0.0359 -0.0114 356 LEU B CG  
5592 C CD1 . LEU B 355 ? 0.3695 0.3575 0.3623 0.0232  -0.0373 -0.0064 356 LEU B CD1 
5593 C CD2 . LEU B 355 ? 0.3598 0.3465 0.3488 0.0196  -0.0437 -0.0190 356 LEU B CD2 
5594 N N   . ASN B 356 ? 0.3891 0.3207 0.2836 0.0387  -0.0262 -0.0123 357 ASN B N   
5595 C CA  . ASN B 356 ? 0.4394 0.3568 0.3023 0.0451  -0.0287 -0.0117 357 ASN B CA  
5596 C C   . ASN B 356 ? 0.4983 0.4026 0.3397 0.0447  -0.0271 -0.0185 357 ASN B C   
5597 O O   . ASN B 356 ? 0.5565 0.4510 0.3703 0.0493  -0.0340 -0.0205 357 ASN B O   
5598 C CB  . ASN B 356 ? 0.4527 0.3583 0.3053 0.0495  -0.0171 -0.0032 357 ASN B CB  
5599 C CG  . ASN B 356 ? 0.4494 0.3638 0.3117 0.0522  -0.0220 0.0028  357 ASN B CG  
5600 O OD1 . ASN B 356 ? 0.5065 0.4199 0.3547 0.0577  -0.0322 0.0039  357 ASN B OD1 
5601 N ND2 . ASN B 356 ? 0.4425 0.3659 0.3294 0.0483  -0.0154 0.0064  357 ASN B ND2 
5602 N N   . ALA B 357 ? 0.4843 0.3881 0.3374 0.0394  -0.0188 -0.0222 358 ALA B N   
5603 C CA  . ALA B 357 ? 0.4876 0.3780 0.3213 0.0384  -0.0158 -0.0293 358 ALA B CA  
5604 C C   . ALA B 357 ? 0.5751 0.4751 0.4154 0.0340  -0.0278 -0.0389 358 ALA B C   
5605 O O   . ALA B 357 ? 0.5964 0.4857 0.4161 0.0334  -0.0293 -0.0463 358 ALA B O   
5606 C CB  . ALA B 357 ? 0.5022 0.3848 0.3447 0.0356  0.0014  -0.0284 358 ALA B CB  
5607 N N   . ILE B 358 ? 0.5105 0.4292 0.3783 0.0306  -0.0356 -0.0396 359 ILE B N   
5608 C CA  . ILE B 358 ? 0.5702 0.4979 0.4476 0.0257  -0.0452 -0.0492 359 ILE B CA  
5609 C C   . ILE B 358 ? 0.6274 0.5548 0.4847 0.0287  -0.0603 -0.0550 359 ILE B C   
5610 O O   . ILE B 358 ? 0.5844 0.5145 0.4341 0.0343  -0.0679 -0.0501 359 ILE B O   
5611 C CB  . ILE B 358 ? 0.5534 0.4992 0.4638 0.0217  -0.0485 -0.0477 359 ILE B CB  
5612 C CG1 . ILE B 358 ? 0.5634 0.5176 0.4863 0.0160  -0.0562 -0.0579 359 ILE B CG1 
5613 C CG2 . ILE B 358 ? 0.5231 0.4784 0.4386 0.0255  -0.0559 -0.0416 359 ILE B CG2 
5614 C CD1 . ILE B 358 ? 0.5379 0.5077 0.4899 0.0124  -0.0591 -0.0565 359 ILE B CD1 
5615 N N   . LYS B 359 ? 0.6420 0.5659 0.4904 0.0252  -0.0648 -0.0657 360 LYS B N   
5616 C CA  . LYS B 359 ? 0.6651 0.5882 0.4923 0.0278  -0.0801 -0.0726 360 LYS B CA  
5617 C C   . LYS B 359 ? 0.6346 0.5788 0.4844 0.0270  -0.0960 -0.0757 360 LYS B C   
5618 O O   . LYS B 359 ? 0.5899 0.5476 0.4709 0.0222  -0.0939 -0.0757 360 LYS B O   
5619 C CB  . LYS B 359 ? 0.6767 0.5893 0.4883 0.0232  -0.0795 -0.0844 360 LYS B CB  
5620 C CG  . LYS B 359 ? 0.7341 0.6240 0.5227 0.0240  -0.0626 -0.0821 360 LYS B CG  
5621 C CD  . LYS B 359 ? 0.8492 0.7322 0.6392 0.0168  -0.0557 -0.0926 360 LYS B CD  
5622 C CE  . LYS B 359 ? 0.8514 0.7194 0.6408 0.0163  -0.0345 -0.0876 360 LYS B CE  
5623 N NZ  . LYS B 359 ? 0.9168 0.7619 0.6695 0.0211  -0.0262 -0.0852 360 LYS B NZ  
# 
