data_9FAH
# 
_entry.id   9FAH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9FAH         pdb_00009fah 10.2210/pdb9fah/pdb 
WWPDB D_1292138471 ?            ?                   
# 
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 
1 'Structure model' 1 0 2025-01-22 
2 'Structure model' 1 1 2025-02-12 
# 
_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.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 2 'Structure model' '_citation_author.identifier_ORCID' 
13 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FAH 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              thilo.stehle@uni-tuebingen.de 
_pdbx_contact_author.name_first         Thilo 
_pdbx_contact_author.name_last          Stehle 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4571-8548 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Strebl, M.'  1 0000-0001-9287-5549 
'Liaci, A.M.' 2 0000-0001-5421-6112 
'Stehle, T.'  3 0000-0002-4571-8548 
# 
_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            'Plos Pathog.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1553-7374 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            21 
_citation.language                  ? 
_citation.page_first                e1012892 
_citation.page_last                 e1012892 
_citation.title                     'Extended receptor repertoire of an adenovirus associated with human obesity.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1371/journal.ppat.1012892 
_citation.pdbx_database_id_PubMed   39883726 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liaci, A.M.'   1  ?                   
primary 'Chandra, N.'   2  ?                   
primary 'Vodnala, S.M.' 3  ?                   
primary 'Strebl, M.'    4  ?                   
primary 'Kumar, P.'     5  ?                   
primary 'Pfenning, V.'  6  ?                   
primary 'Bachmann, P.'  7  ?                   
primary 'Caraballo, R.' 8  ?                   
primary 'Chai, W.'      9  ?                   
primary 'Johansson, E.' 10 ?                   
primary 'Elofsson, M.'  11 ?                   
primary 'Feizi, T.'     12 ?                   
primary 'Liu, Y.'       13 ?                   
primary 'Stehle, T.'    14 ?                   
primary 'Arnberg, N.'   15 0000-0002-7069-6678 
# 
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 Fiber                                                                                             40086.266 3   
? ? ? ? 
2 non-polymer syn 'methyl 4-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid' 365.333   3   
? ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                        65.409    5   
? ? ? ? 
4 non-polymer syn 'ACETATE ION'                                                                                     59.044    8   
? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                                                    35.453    1   
? ? ? ? 
6 water       nat water                                                                                             18.015    272 
? ? ? ? 
# 
_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       
;MSKRLRVEDDFNPVYPYGYARNQNIPFLTPPFVSSDGFKNFPPGVLSLKLADPITITNGDVSLKVGGGLTLQDGSLTVNP
KAPLQVNTDKKLELAYDNPFESSANKLSLKVGHGLKVLDEKSAAGLKDLIGKLVVLTGKGIGTENLENTDGSSRGIGINV
RAREGLTFDNDGYLVAWNPKNDTRTLWTTPDTSPNCTIAQDKDSKLTLVLTKCGSQILANVSLIVVAGKYHIINNKTNPK
IKSFTIKLLFNKNGVLLDNSNLGKAYWNFRSGNSNVSTAYEKAIGFMPNLVAYPKPSNSKKYARDIVYGTIYLGGKPDQP
AVIKTTFNQETGCEYSITFNFSWSKTYENVEFETTSFTFSYIAQE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKRLRVEDDFNPVYPYGYARNQNIPFLTPPFVSSDGFKNFPPGVLSLKLADPITITNGDVSLKVGGGLTLQDGSLTVNP
KAPLQVNTDKKLELAYDNPFESSANKLSLKVGHGLKVLDEKSAAGLKDLIGKLVVLTGKGIGTENLENTDGSSRGIGINV
RAREGLTFDNDGYLVAWNPKNDTRTLWTTPDTSPNCTIAQDKDSKLTLVLTKCGSQILANVSLIVVAGKYHIINNKTNPK
IKSFTIKLLFNKNGVLLDNSNLGKAYWNFRSGNSNVSTAYEKAIGFMPNLVAYPKPSNSKKYARDIVYGTIYLGGKPDQP
AVIKTTFNQETGCEYSITFNFSWSKTYENVEFETTSFTFSYIAQE
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'methyl 4-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid' ANA 
3 'ZINC ION'                                                                                        ZN  
4 'ACETATE ION'                                                                                     ACT 
5 'CHLORIDE ION'                                                                                    CL  
6 water                                                                                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   ARG n 
1 5   LEU n 
1 6   ARG n 
1 7   VAL n 
1 8   GLU n 
1 9   ASP n 
1 10  ASP n 
1 11  PHE n 
1 12  ASN n 
1 13  PRO n 
1 14  VAL n 
1 15  TYR n 
1 16  PRO n 
1 17  TYR n 
1 18  GLY n 
1 19  TYR n 
1 20  ALA n 
1 21  ARG n 
1 22  ASN n 
1 23  GLN n 
1 24  ASN n 
1 25  ILE n 
1 26  PRO n 
1 27  PHE n 
1 28  LEU n 
1 29  THR n 
1 30  PRO n 
1 31  PRO n 
1 32  PHE n 
1 33  VAL n 
1 34  SER n 
1 35  SER n 
1 36  ASP n 
1 37  GLY n 
1 38  PHE n 
1 39  LYS n 
1 40  ASN n 
1 41  PHE n 
1 42  PRO n 
1 43  PRO n 
1 44  GLY n 
1 45  VAL n 
1 46  LEU n 
1 47  SER n 
1 48  LEU n 
1 49  LYS n 
1 50  LEU n 
1 51  ALA n 
1 52  ASP n 
1 53  PRO n 
1 54  ILE n 
1 55  THR n 
1 56  ILE n 
1 57  THR n 
1 58  ASN n 
1 59  GLY n 
1 60  ASP n 
1 61  VAL n 
1 62  SER n 
1 63  LEU n 
1 64  LYS n 
1 65  VAL n 
1 66  GLY n 
1 67  GLY n 
1 68  GLY n 
1 69  LEU n 
1 70  THR n 
1 71  LEU n 
1 72  GLN n 
1 73  ASP n 
1 74  GLY n 
1 75  SER n 
1 76  LEU n 
1 77  THR n 
1 78  VAL n 
1 79  ASN n 
1 80  PRO n 
1 81  LYS n 
1 82  ALA n 
1 83  PRO n 
1 84  LEU n 
1 85  GLN n 
1 86  VAL n 
1 87  ASN n 
1 88  THR n 
1 89  ASP n 
1 90  LYS n 
1 91  LYS n 
1 92  LEU n 
1 93  GLU n 
1 94  LEU n 
1 95  ALA n 
1 96  TYR n 
1 97  ASP n 
1 98  ASN n 
1 99  PRO n 
1 100 PHE n 
1 101 GLU n 
1 102 SER n 
1 103 SER n 
1 104 ALA n 
1 105 ASN n 
1 106 LYS n 
1 107 LEU n 
1 108 SER n 
1 109 LEU n 
1 110 LYS n 
1 111 VAL n 
1 112 GLY n 
1 113 HIS n 
1 114 GLY n 
1 115 LEU n 
1 116 LYS n 
1 117 VAL n 
1 118 LEU n 
1 119 ASP n 
1 120 GLU n 
1 121 LYS n 
1 122 SER n 
1 123 ALA n 
1 124 ALA n 
1 125 GLY n 
1 126 LEU n 
1 127 LYS n 
1 128 ASP n 
1 129 LEU n 
1 130 ILE n 
1 131 GLY n 
1 132 LYS n 
1 133 LEU n 
1 134 VAL n 
1 135 VAL n 
1 136 LEU n 
1 137 THR n 
1 138 GLY n 
1 139 LYS n 
1 140 GLY n 
1 141 ILE n 
1 142 GLY n 
1 143 THR n 
1 144 GLU n 
1 145 ASN n 
1 146 LEU n 
1 147 GLU n 
1 148 ASN n 
1 149 THR n 
1 150 ASP n 
1 151 GLY n 
1 152 SER n 
1 153 SER n 
1 154 ARG n 
1 155 GLY n 
1 156 ILE n 
1 157 GLY n 
1 158 ILE n 
1 159 ASN n 
1 160 VAL n 
1 161 ARG n 
1 162 ALA n 
1 163 ARG n 
1 164 GLU n 
1 165 GLY n 
1 166 LEU n 
1 167 THR n 
1 168 PHE n 
1 169 ASP n 
1 170 ASN n 
1 171 ASP n 
1 172 GLY n 
1 173 TYR n 
1 174 LEU n 
1 175 VAL n 
1 176 ALA n 
1 177 TRP n 
1 178 ASN n 
1 179 PRO n 
1 180 LYS n 
1 181 ASN n 
1 182 ASP n 
1 183 THR n 
1 184 ARG n 
1 185 THR n 
1 186 LEU n 
1 187 TRP n 
1 188 THR n 
1 189 THR n 
1 190 PRO n 
1 191 ASP n 
1 192 THR n 
1 193 SER n 
1 194 PRO n 
1 195 ASN n 
1 196 CYS n 
1 197 THR n 
1 198 ILE n 
1 199 ALA n 
1 200 GLN n 
1 201 ASP n 
1 202 LYS n 
1 203 ASP n 
1 204 SER n 
1 205 LYS n 
1 206 LEU n 
1 207 THR n 
1 208 LEU n 
1 209 VAL n 
1 210 LEU n 
1 211 THR n 
1 212 LYS n 
1 213 CYS n 
1 214 GLY n 
1 215 SER n 
1 216 GLN n 
1 217 ILE n 
1 218 LEU n 
1 219 ALA n 
1 220 ASN n 
1 221 VAL n 
1 222 SER n 
1 223 LEU n 
1 224 ILE n 
1 225 VAL n 
1 226 VAL n 
1 227 ALA n 
1 228 GLY n 
1 229 LYS n 
1 230 TYR n 
1 231 HIS n 
1 232 ILE n 
1 233 ILE n 
1 234 ASN n 
1 235 ASN n 
1 236 LYS n 
1 237 THR n 
1 238 ASN n 
1 239 PRO n 
1 240 LYS n 
1 241 ILE n 
1 242 LYS n 
1 243 SER n 
1 244 PHE n 
1 245 THR n 
1 246 ILE n 
1 247 LYS n 
1 248 LEU n 
1 249 LEU n 
1 250 PHE n 
1 251 ASN n 
1 252 LYS n 
1 253 ASN n 
1 254 GLY n 
1 255 VAL n 
1 256 LEU n 
1 257 LEU n 
1 258 ASP n 
1 259 ASN n 
1 260 SER n 
1 261 ASN n 
1 262 LEU n 
1 263 GLY n 
1 264 LYS n 
1 265 ALA n 
1 266 TYR n 
1 267 TRP n 
1 268 ASN n 
1 269 PHE n 
1 270 ARG n 
1 271 SER n 
1 272 GLY n 
1 273 ASN n 
1 274 SER n 
1 275 ASN n 
1 276 VAL n 
1 277 SER n 
1 278 THR n 
1 279 ALA n 
1 280 TYR n 
1 281 GLU n 
1 282 LYS n 
1 283 ALA n 
1 284 ILE n 
1 285 GLY n 
1 286 PHE n 
1 287 MET n 
1 288 PRO n 
1 289 ASN n 
1 290 LEU n 
1 291 VAL n 
1 292 ALA n 
1 293 TYR n 
1 294 PRO n 
1 295 LYS n 
1 296 PRO n 
1 297 SER n 
1 298 ASN n 
1 299 SER n 
1 300 LYS n 
1 301 LYS n 
1 302 TYR n 
1 303 ALA n 
1 304 ARG n 
1 305 ASP n 
1 306 ILE n 
1 307 VAL n 
1 308 TYR n 
1 309 GLY n 
1 310 THR n 
1 311 ILE n 
1 312 TYR n 
1 313 LEU n 
1 314 GLY n 
1 315 GLY n 
1 316 LYS n 
1 317 PRO n 
1 318 ASP n 
1 319 GLN n 
1 320 PRO n 
1 321 ALA n 
1 322 VAL n 
1 323 ILE n 
1 324 LYS n 
1 325 THR n 
1 326 THR n 
1 327 PHE n 
1 328 ASN n 
1 329 GLN n 
1 330 GLU n 
1 331 THR n 
1 332 GLY n 
1 333 CYS n 
1 334 GLU n 
1 335 TYR n 
1 336 SER n 
1 337 ILE n 
1 338 THR n 
1 339 PHE n 
1 340 ASN n 
1 341 PHE n 
1 342 SER n 
1 343 TRP n 
1 344 SER n 
1 345 LYS n 
1 346 THR n 
1 347 TYR n 
1 348 GLU n 
1 349 ASN n 
1 350 VAL n 
1 351 GLU n 
1 352 PHE n 
1 353 GLU n 
1 354 THR n 
1 355 THR n 
1 356 SER n 
1 357 PHE n 
1 358 THR n 
1 359 PHE n 
1 360 SER n 
1 361 TYR n 
1 362 ILE n 
1 363 ALA n 
1 364 GLN n 
1 365 GLU 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                   365 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 L5 
_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      'Human adenovirus D37' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     52275 
_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 
ACT non-polymer         . 'ACETATE ION'                                                                                     ? 
'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE                                                                                           ? 
'C3 H7 N O2'     89.093  
ANA D-saccharide        n 'methyl 4-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid' 
;4-O-ACETYL-ALPHA-2-OMETHYL-5-N-ACETYL-ALPHA-D-NEURAMINIC ACID; methyl 4-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulosidonic acid; methyl 4-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-D-galacto-non-2-ulosidonic acid; methyl 4-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-galacto-non-2-ulosidonic acid
;
'C14 H23 N O10'  365.333 
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 
CL  non-polymer         . 'CHLORIDE ION'                                                                                    ? 
'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                                                                                          ? 
'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                         ? 
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                   ? 
'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                                                           ? 
'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                         ? 
'C6 H10 N3 O2 1' 156.162 
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 
ZN  non-polymer         . 'ZINC ION'                                                                                        ? 
'Zn 2'           65.409  
# 
_pdbx_chem_comp_identifier.comp_id           ANA 
_pdbx_chem_comp_identifier.type              'IUPAC CARBOHYDRATE SYMBOL' 
_pdbx_chem_comp_identifier.program           PDB-CARE 
_pdbx_chem_comp_identifier.program_version   1.0 
_pdbx_chem_comp_identifier.identifier        '4-O-acetyl-2-O-methyl-5-N-acetyl-a-D-neuraminic acid' 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   ARG 6   6   ?   ?   ?   A . n 
A 1 7   VAL 7   7   ?   ?   ?   A . n 
A 1 8   GLU 8   8   ?   ?   ?   A . n 
A 1 9   ASP 9   9   ?   ?   ?   A . n 
A 1 10  ASP 10  10  ?   ?   ?   A . n 
A 1 11  PHE 11  11  ?   ?   ?   A . n 
A 1 12  ASN 12  12  ?   ?   ?   A . n 
A 1 13  PRO 13  13  ?   ?   ?   A . n 
A 1 14  VAL 14  14  ?   ?   ?   A . n 
A 1 15  TYR 15  15  ?   ?   ?   A . n 
A 1 16  PRO 16  16  ?   ?   ?   A . n 
A 1 17  TYR 17  17  ?   ?   ?   A . n 
A 1 18  GLY 18  18  ?   ?   ?   A . n 
A 1 19  TYR 19  19  ?   ?   ?   A . n 
A 1 20  ALA 20  20  ?   ?   ?   A . n 
A 1 21  ARG 21  21  ?   ?   ?   A . n 
A 1 22  ASN 22  22  ?   ?   ?   A . n 
A 1 23  GLN 23  23  ?   ?   ?   A . n 
A 1 24  ASN 24  24  ?   ?   ?   A . n 
A 1 25  ILE 25  25  ?   ?   ?   A . n 
A 1 26  PRO 26  26  ?   ?   ?   A . n 
A 1 27  PHE 27  27  ?   ?   ?   A . n 
A 1 28  LEU 28  28  ?   ?   ?   A . n 
A 1 29  THR 29  29  ?   ?   ?   A . n 
A 1 30  PRO 30  30  ?   ?   ?   A . n 
A 1 31  PRO 31  31  ?   ?   ?   A . n 
A 1 32  PHE 32  32  ?   ?   ?   A . n 
A 1 33  VAL 33  33  ?   ?   ?   A . n 
A 1 34  SER 34  34  ?   ?   ?   A . n 
A 1 35  SER 35  35  ?   ?   ?   A . n 
A 1 36  ASP 36  36  ?   ?   ?   A . n 
A 1 37  GLY 37  37  ?   ?   ?   A . n 
A 1 38  PHE 38  38  ?   ?   ?   A . n 
A 1 39  LYS 39  39  ?   ?   ?   A . n 
A 1 40  ASN 40  40  ?   ?   ?   A . n 
A 1 41  PHE 41  41  ?   ?   ?   A . n 
A 1 42  PRO 42  42  ?   ?   ?   A . n 
A 1 43  PRO 43  43  ?   ?   ?   A . n 
A 1 44  GLY 44  44  ?   ?   ?   A . n 
A 1 45  VAL 45  45  ?   ?   ?   A . n 
A 1 46  LEU 46  46  ?   ?   ?   A . n 
A 1 47  SER 47  47  ?   ?   ?   A . n 
A 1 48  LEU 48  48  ?   ?   ?   A . n 
A 1 49  LYS 49  49  ?   ?   ?   A . n 
A 1 50  LEU 50  50  ?   ?   ?   A . n 
A 1 51  ALA 51  51  ?   ?   ?   A . n 
A 1 52  ASP 52  52  ?   ?   ?   A . n 
A 1 53  PRO 53  53  ?   ?   ?   A . n 
A 1 54  ILE 54  54  ?   ?   ?   A . n 
A 1 55  THR 55  55  ?   ?   ?   A . n 
A 1 56  ILE 56  56  ?   ?   ?   A . n 
A 1 57  THR 57  57  ?   ?   ?   A . n 
A 1 58  ASN 58  58  ?   ?   ?   A . n 
A 1 59  GLY 59  59  ?   ?   ?   A . n 
A 1 60  ASP 60  60  ?   ?   ?   A . n 
A 1 61  VAL 61  61  ?   ?   ?   A . n 
A 1 62  SER 62  62  ?   ?   ?   A . n 
A 1 63  LEU 63  63  ?   ?   ?   A . n 
A 1 64  LYS 64  64  ?   ?   ?   A . n 
A 1 65  VAL 65  65  ?   ?   ?   A . n 
A 1 66  GLY 66  66  ?   ?   ?   A . n 
A 1 67  GLY 67  67  ?   ?   ?   A . n 
A 1 68  GLY 68  68  ?   ?   ?   A . n 
A 1 69  LEU 69  69  ?   ?   ?   A . n 
A 1 70  THR 70  70  ?   ?   ?   A . n 
A 1 71  LEU 71  71  ?   ?   ?   A . n 
A 1 72  GLN 72  72  ?   ?   ?   A . n 
A 1 73  ASP 73  73  ?   ?   ?   A . n 
A 1 74  GLY 74  74  ?   ?   ?   A . n 
A 1 75  SER 75  75  ?   ?   ?   A . n 
A 1 76  LEU 76  76  ?   ?   ?   A . n 
A 1 77  THR 77  77  ?   ?   ?   A . n 
A 1 78  VAL 78  78  ?   ?   ?   A . n 
A 1 79  ASN 79  79  ?   ?   ?   A . n 
A 1 80  PRO 80  80  ?   ?   ?   A . n 
A 1 81  LYS 81  81  ?   ?   ?   A . n 
A 1 82  ALA 82  82  ?   ?   ?   A . n 
A 1 83  PRO 83  83  ?   ?   ?   A . n 
A 1 84  LEU 84  84  ?   ?   ?   A . n 
A 1 85  GLN 85  85  ?   ?   ?   A . n 
A 1 86  VAL 86  86  ?   ?   ?   A . n 
A 1 87  ASN 87  87  ?   ?   ?   A . n 
A 1 88  THR 88  88  ?   ?   ?   A . n 
A 1 89  ASP 89  89  ?   ?   ?   A . n 
A 1 90  LYS 90  90  ?   ?   ?   A . n 
A 1 91  LYS 91  91  ?   ?   ?   A . n 
A 1 92  LEU 92  92  ?   ?   ?   A . n 
A 1 93  GLU 93  93  ?   ?   ?   A . n 
A 1 94  LEU 94  94  ?   ?   ?   A . n 
A 1 95  ALA 95  95  ?   ?   ?   A . n 
A 1 96  TYR 96  96  ?   ?   ?   A . n 
A 1 97  ASP 97  97  ?   ?   ?   A . n 
A 1 98  ASN 98  98  ?   ?   ?   A . n 
A 1 99  PRO 99  99  ?   ?   ?   A . n 
A 1 100 PHE 100 100 ?   ?   ?   A . n 
A 1 101 GLU 101 101 ?   ?   ?   A . n 
A 1 102 SER 102 102 ?   ?   ?   A . n 
A 1 103 SER 103 103 ?   ?   ?   A . n 
A 1 104 ALA 104 104 ?   ?   ?   A . n 
A 1 105 ASN 105 105 ?   ?   ?   A . n 
A 1 106 LYS 106 106 ?   ?   ?   A . n 
A 1 107 LEU 107 107 ?   ?   ?   A . n 
A 1 108 SER 108 108 ?   ?   ?   A . n 
A 1 109 LEU 109 109 ?   ?   ?   A . n 
A 1 110 LYS 110 110 ?   ?   ?   A . n 
A 1 111 VAL 111 111 ?   ?   ?   A . n 
A 1 112 GLY 112 112 ?   ?   ?   A . n 
A 1 113 HIS 113 113 ?   ?   ?   A . n 
A 1 114 GLY 114 114 ?   ?   ?   A . n 
A 1 115 LEU 115 115 ?   ?   ?   A . n 
A 1 116 LYS 116 116 ?   ?   ?   A . n 
A 1 117 VAL 117 117 ?   ?   ?   A . n 
A 1 118 LEU 118 118 ?   ?   ?   A . n 
A 1 119 ASP 119 119 ?   ?   ?   A . n 
A 1 120 GLU 120 120 ?   ?   ?   A . n 
A 1 121 LYS 121 121 ?   ?   ?   A . n 
A 1 122 SER 122 122 ?   ?   ?   A . n 
A 1 123 ALA 123 123 ?   ?   ?   A . n 
A 1 124 ALA 124 124 ?   ?   ?   A . n 
A 1 125 GLY 125 125 ?   ?   ?   A . n 
A 1 126 LEU 126 126 ?   ?   ?   A . n 
A 1 127 LYS 127 127 ?   ?   ?   A . n 
A 1 128 ASP 128 128 ?   ?   ?   A . n 
A 1 129 LEU 129 129 ?   ?   ?   A . n 
A 1 130 ILE 130 130 ?   ?   ?   A . n 
A 1 131 GLY 131 131 ?   ?   ?   A . n 
A 1 132 LYS 132 132 ?   ?   ?   A . n 
A 1 133 LEU 133 133 ?   ?   ?   A . n 
A 1 134 VAL 134 134 ?   ?   ?   A . n 
A 1 135 VAL 135 135 ?   ?   ?   A . n 
A 1 136 LEU 136 136 ?   ?   ?   A . n 
A 1 137 THR 137 137 ?   ?   ?   A . n 
A 1 138 GLY 138 138 ?   ?   ?   A . n 
A 1 139 LYS 139 139 ?   ?   ?   A . n 
A 1 140 GLY 140 140 ?   ?   ?   A . n 
A 1 141 ILE 141 141 ?   ?   ?   A . n 
A 1 142 GLY 142 142 ?   ?   ?   A . n 
A 1 143 THR 143 143 ?   ?   ?   A . n 
A 1 144 GLU 144 144 ?   ?   ?   A . n 
A 1 145 ASN 145 145 ?   ?   ?   A . n 
A 1 146 LEU 146 146 ?   ?   ?   A . n 
A 1 147 GLU 147 147 ?   ?   ?   A . n 
A 1 148 ASN 148 148 ?   ?   ?   A . n 
A 1 149 THR 149 149 ?   ?   ?   A . n 
A 1 150 ASP 150 150 ?   ?   ?   A . n 
A 1 151 GLY 151 151 ?   ?   ?   A . n 
A 1 152 SER 152 152 ?   ?   ?   A . n 
A 1 153 SER 153 153 ?   ?   ?   A . n 
A 1 154 ARG 154 154 ?   ?   ?   A . n 
A 1 155 GLY 155 155 ?   ?   ?   A . n 
A 1 156 ILE 156 156 ?   ?   ?   A . n 
A 1 157 GLY 157 157 ?   ?   ?   A . n 
A 1 158 ILE 158 158 ?   ?   ?   A . n 
A 1 159 ASN 159 159 ?   ?   ?   A . n 
A 1 160 VAL 160 160 ?   ?   ?   A . n 
A 1 161 ARG 161 161 ?   ?   ?   A . n 
A 1 162 ALA 162 162 ?   ?   ?   A . n 
A 1 163 ARG 163 163 ?   ?   ?   A . n 
A 1 164 GLU 164 164 ?   ?   ?   A . n 
A 1 165 GLY 165 165 ?   ?   ?   A . n 
A 1 166 LEU 166 166 ?   ?   ?   A . n 
A 1 167 THR 167 167 ?   ?   ?   A . n 
A 1 168 PHE 168 168 ?   ?   ?   A . n 
A 1 169 ASP 169 169 ?   ?   ?   A . n 
A 1 170 ASN 170 170 ?   ?   ?   A . n 
A 1 171 ASP 171 171 ?   ?   ?   A . n 
A 1 172 GLY 172 172 ?   ?   ?   A . n 
A 1 173 TYR 173 173 ?   ?   ?   A . n 
A 1 174 LEU 174 174 ?   ?   ?   A . n 
A 1 175 VAL 175 175 ?   ?   ?   A . n 
A 1 176 ALA 176 176 ?   ?   ?   A . n 
A 1 177 TRP 177 177 ?   ?   ?   A . n 
A 1 178 ASN 178 178 ?   ?   ?   A . n 
A 1 179 PRO 179 179 ?   ?   ?   A . n 
A 1 180 LYS 180 180 ?   ?   ?   A . n 
A 1 181 ASN 181 181 181 ASN ASN A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 THR 183 183 183 THR THR A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 THR 185 185 185 THR THR A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 TRP 187 187 187 TRP TRP A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 ASN 195 195 195 ASN ASN A . n 
A 1 196 CYS 196 196 196 CYS CYS A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 GLN 200 200 200 GLN GLN A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 LYS 202 202 202 LYS LYS A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 CYS 213 213 213 CYS CYS A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 ASN 220 220 220 ASN ASN A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 LYS 229 229 229 LYS LYS A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 HIS 231 231 231 HIS HIS A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 ILE 233 233 233 ILE ILE A . n 
A 1 234 ASN 234 234 234 ASN ASN A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 THR 245 245 245 THR THR A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 PHE 250 250 250 PHE PHE A . n 
A 1 251 ASN 251 251 251 ASN ASN A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 ASP 258 258 258 ASP ASP A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 ASN 261 261 261 ASN ASN A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 TYR 266 266 266 TYR TYR A . n 
A 1 267 TRP 267 267 267 TRP TRP A . n 
A 1 268 ASN 268 268 268 ASN ASN A . n 
A 1 269 PHE 269 269 269 PHE PHE A . n 
A 1 270 ARG 270 270 270 ARG ARG A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 ASN 275 275 275 ASN ASN A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 TYR 280 280 280 TYR TYR A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 GLY 285 285 285 GLY GLY A . n 
A 1 286 PHE 286 286 286 PHE PHE A . n 
A 1 287 MET 287 287 287 MET MET A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 VAL 291 291 291 VAL VAL A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 PRO 294 294 294 PRO PRO A . n 
A 1 295 LYS 295 295 295 LYS LYS A . n 
A 1 296 PRO 296 296 296 PRO PRO A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 SER 299 299 299 SER SER A . n 
A 1 300 LYS 300 300 300 LYS LYS A . n 
A 1 301 LYS 301 301 301 LYS LYS A . n 
A 1 302 TYR 302 302 302 TYR TYR A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 ARG 304 304 304 ARG ARG A . n 
A 1 305 ASP 305 305 305 ASP ASP A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 VAL 307 307 307 VAL VAL A . n 
A 1 308 TYR 308 308 308 TYR TYR A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 THR 310 310 310 THR THR A . n 
A 1 311 ILE 311 311 311 ILE ILE A . n 
A 1 312 TYR 312 312 312 TYR TYR A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 LYS 316 316 316 LYS LYS A . n 
A 1 317 PRO 317 317 317 PRO PRO A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 GLN 319 319 319 GLN GLN A . n 
A 1 320 PRO 320 320 320 PRO PRO A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 ILE 323 323 323 ILE ILE A . n 
A 1 324 LYS 324 324 324 LYS LYS A . n 
A 1 325 THR 325 325 325 THR THR A . n 
A 1 326 THR 326 326 326 THR THR A . n 
A 1 327 PHE 327 327 327 PHE PHE A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 GLN 329 329 329 GLN GLN A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 THR 331 331 331 THR THR A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 CYS 333 333 333 CYS CYS A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 TYR 335 335 335 TYR TYR A . n 
A 1 336 SER 336 336 336 SER SER A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 THR 338 338 338 THR THR A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 ASN 340 340 340 ASN ASN A . n 
A 1 341 PHE 341 341 341 PHE PHE A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 TRP 343 343 343 TRP TRP A . n 
A 1 344 SER 344 344 344 SER SER A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 THR 346 346 346 THR THR A . n 
A 1 347 TYR 347 347 347 TYR TYR A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 ASN 349 349 349 ASN ASN A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 PHE 352 352 352 PHE PHE A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 THR 354 354 354 THR THR A . n 
A 1 355 THR 355 355 355 THR THR A . n 
A 1 356 SER 356 356 356 SER SER A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 PHE 359 359 359 PHE PHE A . n 
A 1 360 SER 360 360 360 SER SER A . n 
A 1 361 TYR 361 361 361 TYR TYR A . n 
A 1 362 ILE 362 362 362 ILE ILE A . n 
A 1 363 ALA 363 363 363 ALA ALA A . n 
A 1 364 GLN 364 364 364 GLN GLN A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   ?   ?   ?   B . n 
B 1 4   ARG 4   4   ?   ?   ?   B . n 
B 1 5   LEU 5   5   ?   ?   ?   B . n 
B 1 6   ARG 6   6   ?   ?   ?   B . n 
B 1 7   VAL 7   7   ?   ?   ?   B . n 
B 1 8   GLU 8   8   ?   ?   ?   B . n 
B 1 9   ASP 9   9   ?   ?   ?   B . n 
B 1 10  ASP 10  10  ?   ?   ?   B . n 
B 1 11  PHE 11  11  ?   ?   ?   B . n 
B 1 12  ASN 12  12  ?   ?   ?   B . n 
B 1 13  PRO 13  13  ?   ?   ?   B . n 
B 1 14  VAL 14  14  ?   ?   ?   B . n 
B 1 15  TYR 15  15  ?   ?   ?   B . n 
B 1 16  PRO 16  16  ?   ?   ?   B . n 
B 1 17  TYR 17  17  ?   ?   ?   B . n 
B 1 18  GLY 18  18  ?   ?   ?   B . n 
B 1 19  TYR 19  19  ?   ?   ?   B . n 
B 1 20  ALA 20  20  ?   ?   ?   B . n 
B 1 21  ARG 21  21  ?   ?   ?   B . n 
B 1 22  ASN 22  22  ?   ?   ?   B . n 
B 1 23  GLN 23  23  ?   ?   ?   B . n 
B 1 24  ASN 24  24  ?   ?   ?   B . n 
B 1 25  ILE 25  25  ?   ?   ?   B . n 
B 1 26  PRO 26  26  ?   ?   ?   B . n 
B 1 27  PHE 27  27  ?   ?   ?   B . n 
B 1 28  LEU 28  28  ?   ?   ?   B . n 
B 1 29  THR 29  29  ?   ?   ?   B . n 
B 1 30  PRO 30  30  ?   ?   ?   B . n 
B 1 31  PRO 31  31  ?   ?   ?   B . n 
B 1 32  PHE 32  32  ?   ?   ?   B . n 
B 1 33  VAL 33  33  ?   ?   ?   B . n 
B 1 34  SER 34  34  ?   ?   ?   B . n 
B 1 35  SER 35  35  ?   ?   ?   B . n 
B 1 36  ASP 36  36  ?   ?   ?   B . n 
B 1 37  GLY 37  37  ?   ?   ?   B . n 
B 1 38  PHE 38  38  ?   ?   ?   B . n 
B 1 39  LYS 39  39  ?   ?   ?   B . n 
B 1 40  ASN 40  40  ?   ?   ?   B . n 
B 1 41  PHE 41  41  ?   ?   ?   B . n 
B 1 42  PRO 42  42  ?   ?   ?   B . n 
B 1 43  PRO 43  43  ?   ?   ?   B . n 
B 1 44  GLY 44  44  ?   ?   ?   B . n 
B 1 45  VAL 45  45  ?   ?   ?   B . n 
B 1 46  LEU 46  46  ?   ?   ?   B . n 
B 1 47  SER 47  47  ?   ?   ?   B . n 
B 1 48  LEU 48  48  ?   ?   ?   B . n 
B 1 49  LYS 49  49  ?   ?   ?   B . n 
B 1 50  LEU 50  50  ?   ?   ?   B . n 
B 1 51  ALA 51  51  ?   ?   ?   B . n 
B 1 52  ASP 52  52  ?   ?   ?   B . n 
B 1 53  PRO 53  53  ?   ?   ?   B . n 
B 1 54  ILE 54  54  ?   ?   ?   B . n 
B 1 55  THR 55  55  ?   ?   ?   B . n 
B 1 56  ILE 56  56  ?   ?   ?   B . n 
B 1 57  THR 57  57  ?   ?   ?   B . n 
B 1 58  ASN 58  58  ?   ?   ?   B . n 
B 1 59  GLY 59  59  ?   ?   ?   B . n 
B 1 60  ASP 60  60  ?   ?   ?   B . n 
B 1 61  VAL 61  61  ?   ?   ?   B . n 
B 1 62  SER 62  62  ?   ?   ?   B . n 
B 1 63  LEU 63  63  ?   ?   ?   B . n 
B 1 64  LYS 64  64  ?   ?   ?   B . n 
B 1 65  VAL 65  65  ?   ?   ?   B . n 
B 1 66  GLY 66  66  ?   ?   ?   B . n 
B 1 67  GLY 67  67  ?   ?   ?   B . n 
B 1 68  GLY 68  68  ?   ?   ?   B . n 
B 1 69  LEU 69  69  ?   ?   ?   B . n 
B 1 70  THR 70  70  ?   ?   ?   B . n 
B 1 71  LEU 71  71  ?   ?   ?   B . n 
B 1 72  GLN 72  72  ?   ?   ?   B . n 
B 1 73  ASP 73  73  ?   ?   ?   B . n 
B 1 74  GLY 74  74  ?   ?   ?   B . n 
B 1 75  SER 75  75  ?   ?   ?   B . n 
B 1 76  LEU 76  76  ?   ?   ?   B . n 
B 1 77  THR 77  77  ?   ?   ?   B . n 
B 1 78  VAL 78  78  ?   ?   ?   B . n 
B 1 79  ASN 79  79  ?   ?   ?   B . n 
B 1 80  PRO 80  80  ?   ?   ?   B . n 
B 1 81  LYS 81  81  ?   ?   ?   B . n 
B 1 82  ALA 82  82  ?   ?   ?   B . n 
B 1 83  PRO 83  83  ?   ?   ?   B . n 
B 1 84  LEU 84  84  ?   ?   ?   B . n 
B 1 85  GLN 85  85  ?   ?   ?   B . n 
B 1 86  VAL 86  86  ?   ?   ?   B . n 
B 1 87  ASN 87  87  ?   ?   ?   B . n 
B 1 88  THR 88  88  ?   ?   ?   B . n 
B 1 89  ASP 89  89  ?   ?   ?   B . n 
B 1 90  LYS 90  90  ?   ?   ?   B . n 
B 1 91  LYS 91  91  ?   ?   ?   B . n 
B 1 92  LEU 92  92  ?   ?   ?   B . n 
B 1 93  GLU 93  93  ?   ?   ?   B . n 
B 1 94  LEU 94  94  ?   ?   ?   B . n 
B 1 95  ALA 95  95  ?   ?   ?   B . n 
B 1 96  TYR 96  96  ?   ?   ?   B . n 
B 1 97  ASP 97  97  ?   ?   ?   B . n 
B 1 98  ASN 98  98  ?   ?   ?   B . n 
B 1 99  PRO 99  99  ?   ?   ?   B . n 
B 1 100 PHE 100 100 ?   ?   ?   B . n 
B 1 101 GLU 101 101 ?   ?   ?   B . n 
B 1 102 SER 102 102 ?   ?   ?   B . n 
B 1 103 SER 103 103 ?   ?   ?   B . n 
B 1 104 ALA 104 104 ?   ?   ?   B . n 
B 1 105 ASN 105 105 ?   ?   ?   B . n 
B 1 106 LYS 106 106 ?   ?   ?   B . n 
B 1 107 LEU 107 107 ?   ?   ?   B . n 
B 1 108 SER 108 108 ?   ?   ?   B . n 
B 1 109 LEU 109 109 ?   ?   ?   B . n 
B 1 110 LYS 110 110 ?   ?   ?   B . n 
B 1 111 VAL 111 111 ?   ?   ?   B . n 
B 1 112 GLY 112 112 ?   ?   ?   B . n 
B 1 113 HIS 113 113 ?   ?   ?   B . n 
B 1 114 GLY 114 114 ?   ?   ?   B . n 
B 1 115 LEU 115 115 ?   ?   ?   B . n 
B 1 116 LYS 116 116 ?   ?   ?   B . n 
B 1 117 VAL 117 117 ?   ?   ?   B . n 
B 1 118 LEU 118 118 ?   ?   ?   B . n 
B 1 119 ASP 119 119 ?   ?   ?   B . n 
B 1 120 GLU 120 120 ?   ?   ?   B . n 
B 1 121 LYS 121 121 ?   ?   ?   B . n 
B 1 122 SER 122 122 ?   ?   ?   B . n 
B 1 123 ALA 123 123 ?   ?   ?   B . n 
B 1 124 ALA 124 124 ?   ?   ?   B . n 
B 1 125 GLY 125 125 ?   ?   ?   B . n 
B 1 126 LEU 126 126 ?   ?   ?   B . n 
B 1 127 LYS 127 127 ?   ?   ?   B . n 
B 1 128 ASP 128 128 ?   ?   ?   B . n 
B 1 129 LEU 129 129 ?   ?   ?   B . n 
B 1 130 ILE 130 130 ?   ?   ?   B . n 
B 1 131 GLY 131 131 ?   ?   ?   B . n 
B 1 132 LYS 132 132 ?   ?   ?   B . n 
B 1 133 LEU 133 133 ?   ?   ?   B . n 
B 1 134 VAL 134 134 ?   ?   ?   B . n 
B 1 135 VAL 135 135 ?   ?   ?   B . n 
B 1 136 LEU 136 136 ?   ?   ?   B . n 
B 1 137 THR 137 137 ?   ?   ?   B . n 
B 1 138 GLY 138 138 ?   ?   ?   B . n 
B 1 139 LYS 139 139 ?   ?   ?   B . n 
B 1 140 GLY 140 140 ?   ?   ?   B . n 
B 1 141 ILE 141 141 ?   ?   ?   B . n 
B 1 142 GLY 142 142 ?   ?   ?   B . n 
B 1 143 THR 143 143 ?   ?   ?   B . n 
B 1 144 GLU 144 144 ?   ?   ?   B . n 
B 1 145 ASN 145 145 ?   ?   ?   B . n 
B 1 146 LEU 146 146 ?   ?   ?   B . n 
B 1 147 GLU 147 147 ?   ?   ?   B . n 
B 1 148 ASN 148 148 ?   ?   ?   B . n 
B 1 149 THR 149 149 ?   ?   ?   B . n 
B 1 150 ASP 150 150 ?   ?   ?   B . n 
B 1 151 GLY 151 151 ?   ?   ?   B . n 
B 1 152 SER 152 152 ?   ?   ?   B . n 
B 1 153 SER 153 153 ?   ?   ?   B . n 
B 1 154 ARG 154 154 ?   ?   ?   B . n 
B 1 155 GLY 155 155 ?   ?   ?   B . n 
B 1 156 ILE 156 156 ?   ?   ?   B . n 
B 1 157 GLY 157 157 ?   ?   ?   B . n 
B 1 158 ILE 158 158 ?   ?   ?   B . n 
B 1 159 ASN 159 159 ?   ?   ?   B . n 
B 1 160 VAL 160 160 ?   ?   ?   B . n 
B 1 161 ARG 161 161 ?   ?   ?   B . n 
B 1 162 ALA 162 162 ?   ?   ?   B . n 
B 1 163 ARG 163 163 ?   ?   ?   B . n 
B 1 164 GLU 164 164 ?   ?   ?   B . n 
B 1 165 GLY 165 165 ?   ?   ?   B . n 
B 1 166 LEU 166 166 ?   ?   ?   B . n 
B 1 167 THR 167 167 ?   ?   ?   B . n 
B 1 168 PHE 168 168 ?   ?   ?   B . n 
B 1 169 ASP 169 169 ?   ?   ?   B . n 
B 1 170 ASN 170 170 ?   ?   ?   B . n 
B 1 171 ASP 171 171 ?   ?   ?   B . n 
B 1 172 GLY 172 172 ?   ?   ?   B . n 
B 1 173 TYR 173 173 ?   ?   ?   B . n 
B 1 174 LEU 174 174 ?   ?   ?   B . n 
B 1 175 VAL 175 175 ?   ?   ?   B . n 
B 1 176 ALA 176 176 ?   ?   ?   B . n 
B 1 177 TRP 177 177 ?   ?   ?   B . n 
B 1 178 ASN 178 178 ?   ?   ?   B . n 
B 1 179 PRO 179 179 ?   ?   ?   B . n 
B 1 180 LYS 180 180 ?   ?   ?   B . n 
B 1 181 ASN 181 181 ?   ?   ?   B . n 
B 1 182 ASP 182 182 ?   ?   ?   B . n 
B 1 183 THR 183 183 183 THR THR B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 THR 185 185 185 THR THR B . n 
B 1 186 LEU 186 186 186 LEU LEU B . n 
B 1 187 TRP 187 187 187 TRP TRP B . n 
B 1 188 THR 188 188 188 THR THR B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 PRO 190 190 190 PRO PRO B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 PRO 194 194 194 PRO PRO B . n 
B 1 195 ASN 195 195 195 ASN ASN B . n 
B 1 196 CYS 196 196 196 CYS CYS B . n 
B 1 197 THR 197 197 197 THR THR B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 GLN 200 200 200 GLN GLN B . n 
B 1 201 ASP 201 201 201 ASP ASP B . n 
B 1 202 LYS 202 202 202 LYS LYS B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 THR 207 207 207 THR THR B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 THR 211 211 211 THR THR B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 CYS 213 213 213 CYS CYS B . n 
B 1 214 GLY 214 214 214 GLY GLY B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 ASN 220 220 220 ASN ASN B . n 
B 1 221 VAL 221 221 221 VAL VAL B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ILE 224 224 224 ILE ILE B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 ALA 227 227 227 ALA ALA B . n 
B 1 228 GLY 228 228 228 GLY GLY B . n 
B 1 229 LYS 229 229 229 LYS LYS B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 HIS 231 231 231 HIS HIS B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 ILE 233 233 233 ILE ILE B . n 
B 1 234 ASN 234 234 234 ASN ASN B . n 
B 1 235 ASN 235 235 235 ASN ASN B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 THR 237 237 237 THR THR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 LYS 242 242 242 LYS LYS B . n 
B 1 243 SER 243 243 243 SER SER B . n 
B 1 244 PHE 244 244 244 PHE PHE B . n 
B 1 245 THR 245 245 245 THR THR B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 LYS 247 247 247 LYS LYS B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 LEU 249 249 249 LEU LEU B . n 
B 1 250 PHE 250 250 250 PHE PHE B . n 
B 1 251 ASN 251 251 251 ASN ASN B . n 
B 1 252 LYS 252 252 252 LYS LYS B . n 
B 1 253 ASN 253 253 253 ASN ASN B . n 
B 1 254 GLY 254 254 254 GLY GLY B . n 
B 1 255 VAL 255 255 255 VAL VAL B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 LEU 257 257 257 LEU LEU B . n 
B 1 258 ASP 258 258 258 ASP ASP B . n 
B 1 259 ASN 259 259 259 ASN ASN B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 ASN 261 261 261 ASN ASN B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 ALA 265 265 265 ALA ALA B . n 
B 1 266 TYR 266 266 266 TYR TYR B . n 
B 1 267 TRP 267 267 267 TRP TRP B . n 
B 1 268 ASN 268 268 268 ASN ASN B . n 
B 1 269 PHE 269 269 269 PHE PHE B . n 
B 1 270 ARG 270 270 270 ARG ARG B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 GLY 272 272 ?   ?   ?   B . n 
B 1 273 ASN 273 273 ?   ?   ?   B . n 
B 1 274 SER 274 274 ?   ?   ?   B . n 
B 1 275 ASN 275 275 ?   ?   ?   B . n 
B 1 276 VAL 276 276 ?   ?   ?   B . n 
B 1 277 SER 277 277 ?   ?   ?   B . n 
B 1 278 THR 278 278 ?   ?   ?   B . n 
B 1 279 ALA 279 279 ?   ?   ?   B . n 
B 1 280 TYR 280 280 ?   ?   ?   B . n 
B 1 281 GLU 281 281 281 GLU GLU B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 ALA 283 283 283 ALA ALA B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 GLY 285 285 285 GLY GLY B . n 
B 1 286 PHE 286 286 286 PHE PHE B . n 
B 1 287 MET 287 287 287 MET MET B . n 
B 1 288 PRO 288 288 288 PRO PRO B . n 
B 1 289 ASN 289 289 289 ASN ASN B . n 
B 1 290 LEU 290 290 290 LEU LEU B . n 
B 1 291 VAL 291 291 291 VAL VAL B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 TYR 293 293 293 TYR TYR B . n 
B 1 294 PRO 294 294 294 PRO PRO B . n 
B 1 295 LYS 295 295 295 LYS LYS B . n 
B 1 296 PRO 296 296 296 PRO PRO B . n 
B 1 297 SER 297 297 297 SER SER B . n 
B 1 298 ASN 298 298 ?   ?   ?   B . n 
B 1 299 SER 299 299 ?   ?   ?   B . n 
B 1 300 LYS 300 300 300 LYS LYS B . n 
B 1 301 LYS 301 301 301 LYS LYS B . n 
B 1 302 TYR 302 302 302 TYR TYR B . n 
B 1 303 ALA 303 303 303 ALA ALA B . n 
B 1 304 ARG 304 304 304 ARG ARG B . n 
B 1 305 ASP 305 305 305 ASP ASP B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 VAL 307 307 307 VAL VAL B . n 
B 1 308 TYR 308 308 308 TYR TYR B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 THR 310 310 310 THR THR B . n 
B 1 311 ILE 311 311 311 ILE ILE B . n 
B 1 312 TYR 312 312 312 TYR TYR B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 GLY 314 314 314 GLY GLY B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 LYS 316 316 316 LYS LYS B . n 
B 1 317 PRO 317 317 317 PRO PRO B . n 
B 1 318 ASP 318 318 318 ASP ASP B . n 
B 1 319 GLN 319 319 319 GLN GLN B . n 
B 1 320 PRO 320 320 320 PRO PRO B . n 
B 1 321 ALA 321 321 321 ALA ALA B . n 
B 1 322 VAL 322 322 322 VAL VAL B . n 
B 1 323 ILE 323 323 323 ILE ILE B . n 
B 1 324 LYS 324 324 324 LYS LYS B . n 
B 1 325 THR 325 325 325 THR THR B . n 
B 1 326 THR 326 326 326 THR THR B . n 
B 1 327 PHE 327 327 327 PHE PHE B . n 
B 1 328 ASN 328 328 328 ASN ASN B . n 
B 1 329 GLN 329 329 329 GLN GLN B . n 
B 1 330 GLU 330 330 330 GLU GLU B . n 
B 1 331 THR 331 331 331 THR THR B . n 
B 1 332 GLY 332 332 332 GLY GLY B . n 
B 1 333 CYS 333 333 333 CYS CYS B . n 
B 1 334 GLU 334 334 334 GLU GLU B . n 
B 1 335 TYR 335 335 335 TYR TYR B . n 
B 1 336 SER 336 336 336 SER SER B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 THR 338 338 338 THR THR B . n 
B 1 339 PHE 339 339 339 PHE PHE B . n 
B 1 340 ASN 340 340 340 ASN ASN B . n 
B 1 341 PHE 341 341 341 PHE PHE B . n 
B 1 342 SER 342 342 342 SER SER B . n 
B 1 343 TRP 343 343 343 TRP TRP B . n 
B 1 344 SER 344 344 344 SER SER B . n 
B 1 345 LYS 345 345 345 LYS LYS B . n 
B 1 346 THR 346 346 346 THR THR B . n 
B 1 347 TYR 347 347 347 TYR TYR B . n 
B 1 348 GLU 348 348 348 GLU GLU B . n 
B 1 349 ASN 349 349 349 ASN ASN B . n 
B 1 350 VAL 350 350 350 VAL VAL B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 PHE 352 352 352 PHE PHE B . n 
B 1 353 GLU 353 353 353 GLU GLU B . n 
B 1 354 THR 354 354 354 THR THR B . n 
B 1 355 THR 355 355 355 THR THR B . n 
B 1 356 SER 356 356 356 SER SER B . n 
B 1 357 PHE 357 357 357 PHE PHE B . n 
B 1 358 THR 358 358 358 THR THR B . n 
B 1 359 PHE 359 359 359 PHE PHE B . n 
B 1 360 SER 360 360 360 SER SER B . n 
B 1 361 TYR 361 361 361 TYR TYR B . n 
B 1 362 ILE 362 362 362 ILE ILE B . n 
B 1 363 ALA 363 363 363 ALA ALA B . n 
B 1 364 GLN 364 364 364 GLN GLN B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   ?   ?   ?   C . n 
C 1 4   ARG 4   4   ?   ?   ?   C . n 
C 1 5   LEU 5   5   ?   ?   ?   C . n 
C 1 6   ARG 6   6   ?   ?   ?   C . n 
C 1 7   VAL 7   7   ?   ?   ?   C . n 
C 1 8   GLU 8   8   ?   ?   ?   C . n 
C 1 9   ASP 9   9   ?   ?   ?   C . n 
C 1 10  ASP 10  10  ?   ?   ?   C . n 
C 1 11  PHE 11  11  ?   ?   ?   C . n 
C 1 12  ASN 12  12  ?   ?   ?   C . n 
C 1 13  PRO 13  13  ?   ?   ?   C . n 
C 1 14  VAL 14  14  ?   ?   ?   C . n 
C 1 15  TYR 15  15  ?   ?   ?   C . n 
C 1 16  PRO 16  16  ?   ?   ?   C . n 
C 1 17  TYR 17  17  ?   ?   ?   C . n 
C 1 18  GLY 18  18  ?   ?   ?   C . n 
C 1 19  TYR 19  19  ?   ?   ?   C . n 
C 1 20  ALA 20  20  ?   ?   ?   C . n 
C 1 21  ARG 21  21  ?   ?   ?   C . n 
C 1 22  ASN 22  22  ?   ?   ?   C . n 
C 1 23  GLN 23  23  ?   ?   ?   C . n 
C 1 24  ASN 24  24  ?   ?   ?   C . n 
C 1 25  ILE 25  25  ?   ?   ?   C . n 
C 1 26  PRO 26  26  ?   ?   ?   C . n 
C 1 27  PHE 27  27  ?   ?   ?   C . n 
C 1 28  LEU 28  28  ?   ?   ?   C . n 
C 1 29  THR 29  29  ?   ?   ?   C . n 
C 1 30  PRO 30  30  ?   ?   ?   C . n 
C 1 31  PRO 31  31  ?   ?   ?   C . n 
C 1 32  PHE 32  32  ?   ?   ?   C . n 
C 1 33  VAL 33  33  ?   ?   ?   C . n 
C 1 34  SER 34  34  ?   ?   ?   C . n 
C 1 35  SER 35  35  ?   ?   ?   C . n 
C 1 36  ASP 36  36  ?   ?   ?   C . n 
C 1 37  GLY 37  37  ?   ?   ?   C . n 
C 1 38  PHE 38  38  ?   ?   ?   C . n 
C 1 39  LYS 39  39  ?   ?   ?   C . n 
C 1 40  ASN 40  40  ?   ?   ?   C . n 
C 1 41  PHE 41  41  ?   ?   ?   C . n 
C 1 42  PRO 42  42  ?   ?   ?   C . n 
C 1 43  PRO 43  43  ?   ?   ?   C . n 
C 1 44  GLY 44  44  ?   ?   ?   C . n 
C 1 45  VAL 45  45  ?   ?   ?   C . n 
C 1 46  LEU 46  46  ?   ?   ?   C . n 
C 1 47  SER 47  47  ?   ?   ?   C . n 
C 1 48  LEU 48  48  ?   ?   ?   C . n 
C 1 49  LYS 49  49  ?   ?   ?   C . n 
C 1 50  LEU 50  50  ?   ?   ?   C . n 
C 1 51  ALA 51  51  ?   ?   ?   C . n 
C 1 52  ASP 52  52  ?   ?   ?   C . n 
C 1 53  PRO 53  53  ?   ?   ?   C . n 
C 1 54  ILE 54  54  ?   ?   ?   C . n 
C 1 55  THR 55  55  ?   ?   ?   C . n 
C 1 56  ILE 56  56  ?   ?   ?   C . n 
C 1 57  THR 57  57  ?   ?   ?   C . n 
C 1 58  ASN 58  58  ?   ?   ?   C . n 
C 1 59  GLY 59  59  ?   ?   ?   C . n 
C 1 60  ASP 60  60  ?   ?   ?   C . n 
C 1 61  VAL 61  61  ?   ?   ?   C . n 
C 1 62  SER 62  62  ?   ?   ?   C . n 
C 1 63  LEU 63  63  ?   ?   ?   C . n 
C 1 64  LYS 64  64  ?   ?   ?   C . n 
C 1 65  VAL 65  65  ?   ?   ?   C . n 
C 1 66  GLY 66  66  ?   ?   ?   C . n 
C 1 67  GLY 67  67  ?   ?   ?   C . n 
C 1 68  GLY 68  68  ?   ?   ?   C . n 
C 1 69  LEU 69  69  ?   ?   ?   C . n 
C 1 70  THR 70  70  ?   ?   ?   C . n 
C 1 71  LEU 71  71  ?   ?   ?   C . n 
C 1 72  GLN 72  72  ?   ?   ?   C . n 
C 1 73  ASP 73  73  ?   ?   ?   C . n 
C 1 74  GLY 74  74  ?   ?   ?   C . n 
C 1 75  SER 75  75  ?   ?   ?   C . n 
C 1 76  LEU 76  76  ?   ?   ?   C . n 
C 1 77  THR 77  77  ?   ?   ?   C . n 
C 1 78  VAL 78  78  ?   ?   ?   C . n 
C 1 79  ASN 79  79  ?   ?   ?   C . n 
C 1 80  PRO 80  80  ?   ?   ?   C . n 
C 1 81  LYS 81  81  ?   ?   ?   C . n 
C 1 82  ALA 82  82  ?   ?   ?   C . n 
C 1 83  PRO 83  83  ?   ?   ?   C . n 
C 1 84  LEU 84  84  ?   ?   ?   C . n 
C 1 85  GLN 85  85  ?   ?   ?   C . n 
C 1 86  VAL 86  86  ?   ?   ?   C . n 
C 1 87  ASN 87  87  ?   ?   ?   C . n 
C 1 88  THR 88  88  ?   ?   ?   C . n 
C 1 89  ASP 89  89  ?   ?   ?   C . n 
C 1 90  LYS 90  90  ?   ?   ?   C . n 
C 1 91  LYS 91  91  ?   ?   ?   C . n 
C 1 92  LEU 92  92  ?   ?   ?   C . n 
C 1 93  GLU 93  93  ?   ?   ?   C . n 
C 1 94  LEU 94  94  ?   ?   ?   C . n 
C 1 95  ALA 95  95  ?   ?   ?   C . n 
C 1 96  TYR 96  96  ?   ?   ?   C . n 
C 1 97  ASP 97  97  ?   ?   ?   C . n 
C 1 98  ASN 98  98  ?   ?   ?   C . n 
C 1 99  PRO 99  99  ?   ?   ?   C . n 
C 1 100 PHE 100 100 ?   ?   ?   C . n 
C 1 101 GLU 101 101 ?   ?   ?   C . n 
C 1 102 SER 102 102 ?   ?   ?   C . n 
C 1 103 SER 103 103 ?   ?   ?   C . n 
C 1 104 ALA 104 104 ?   ?   ?   C . n 
C 1 105 ASN 105 105 ?   ?   ?   C . n 
C 1 106 LYS 106 106 ?   ?   ?   C . n 
C 1 107 LEU 107 107 ?   ?   ?   C . n 
C 1 108 SER 108 108 ?   ?   ?   C . n 
C 1 109 LEU 109 109 ?   ?   ?   C . n 
C 1 110 LYS 110 110 ?   ?   ?   C . n 
C 1 111 VAL 111 111 ?   ?   ?   C . n 
C 1 112 GLY 112 112 ?   ?   ?   C . n 
C 1 113 HIS 113 113 ?   ?   ?   C . n 
C 1 114 GLY 114 114 ?   ?   ?   C . n 
C 1 115 LEU 115 115 ?   ?   ?   C . n 
C 1 116 LYS 116 116 ?   ?   ?   C . n 
C 1 117 VAL 117 117 ?   ?   ?   C . n 
C 1 118 LEU 118 118 ?   ?   ?   C . n 
C 1 119 ASP 119 119 ?   ?   ?   C . n 
C 1 120 GLU 120 120 ?   ?   ?   C . n 
C 1 121 LYS 121 121 ?   ?   ?   C . n 
C 1 122 SER 122 122 ?   ?   ?   C . n 
C 1 123 ALA 123 123 ?   ?   ?   C . n 
C 1 124 ALA 124 124 ?   ?   ?   C . n 
C 1 125 GLY 125 125 ?   ?   ?   C . n 
C 1 126 LEU 126 126 ?   ?   ?   C . n 
C 1 127 LYS 127 127 ?   ?   ?   C . n 
C 1 128 ASP 128 128 ?   ?   ?   C . n 
C 1 129 LEU 129 129 ?   ?   ?   C . n 
C 1 130 ILE 130 130 ?   ?   ?   C . n 
C 1 131 GLY 131 131 ?   ?   ?   C . n 
C 1 132 LYS 132 132 ?   ?   ?   C . n 
C 1 133 LEU 133 133 ?   ?   ?   C . n 
C 1 134 VAL 134 134 ?   ?   ?   C . n 
C 1 135 VAL 135 135 ?   ?   ?   C . n 
C 1 136 LEU 136 136 ?   ?   ?   C . n 
C 1 137 THR 137 137 ?   ?   ?   C . n 
C 1 138 GLY 138 138 ?   ?   ?   C . n 
C 1 139 LYS 139 139 ?   ?   ?   C . n 
C 1 140 GLY 140 140 ?   ?   ?   C . n 
C 1 141 ILE 141 141 ?   ?   ?   C . n 
C 1 142 GLY 142 142 ?   ?   ?   C . n 
C 1 143 THR 143 143 ?   ?   ?   C . n 
C 1 144 GLU 144 144 ?   ?   ?   C . n 
C 1 145 ASN 145 145 ?   ?   ?   C . n 
C 1 146 LEU 146 146 ?   ?   ?   C . n 
C 1 147 GLU 147 147 ?   ?   ?   C . n 
C 1 148 ASN 148 148 ?   ?   ?   C . n 
C 1 149 THR 149 149 ?   ?   ?   C . n 
C 1 150 ASP 150 150 ?   ?   ?   C . n 
C 1 151 GLY 151 151 ?   ?   ?   C . n 
C 1 152 SER 152 152 ?   ?   ?   C . n 
C 1 153 SER 153 153 ?   ?   ?   C . n 
C 1 154 ARG 154 154 ?   ?   ?   C . n 
C 1 155 GLY 155 155 ?   ?   ?   C . n 
C 1 156 ILE 156 156 ?   ?   ?   C . n 
C 1 157 GLY 157 157 ?   ?   ?   C . n 
C 1 158 ILE 158 158 ?   ?   ?   C . n 
C 1 159 ASN 159 159 ?   ?   ?   C . n 
C 1 160 VAL 160 160 ?   ?   ?   C . n 
C 1 161 ARG 161 161 ?   ?   ?   C . n 
C 1 162 ALA 162 162 ?   ?   ?   C . n 
C 1 163 ARG 163 163 ?   ?   ?   C . n 
C 1 164 GLU 164 164 ?   ?   ?   C . n 
C 1 165 GLY 165 165 ?   ?   ?   C . n 
C 1 166 LEU 166 166 ?   ?   ?   C . n 
C 1 167 THR 167 167 ?   ?   ?   C . n 
C 1 168 PHE 168 168 ?   ?   ?   C . n 
C 1 169 ASP 169 169 ?   ?   ?   C . n 
C 1 170 ASN 170 170 ?   ?   ?   C . n 
C 1 171 ASP 171 171 ?   ?   ?   C . n 
C 1 172 GLY 172 172 ?   ?   ?   C . n 
C 1 173 TYR 173 173 ?   ?   ?   C . n 
C 1 174 LEU 174 174 ?   ?   ?   C . n 
C 1 175 VAL 175 175 ?   ?   ?   C . n 
C 1 176 ALA 176 176 ?   ?   ?   C . n 
C 1 177 TRP 177 177 ?   ?   ?   C . n 
C 1 178 ASN 178 178 ?   ?   ?   C . n 
C 1 179 PRO 179 179 ?   ?   ?   C . n 
C 1 180 LYS 180 180 180 LYS LYS C . n 
C 1 181 ASN 181 181 181 ASN ASN C . n 
C 1 182 ASP 182 182 182 ASP ASP C . n 
C 1 183 THR 183 183 183 THR THR C . n 
C 1 184 ARG 184 184 184 ARG ARG C . n 
C 1 185 THR 185 185 185 THR THR C . n 
C 1 186 LEU 186 186 186 LEU LEU C . n 
C 1 187 TRP 187 187 187 TRP TRP C . n 
C 1 188 THR 188 188 188 THR THR C . n 
C 1 189 THR 189 189 189 THR THR C . n 
C 1 190 PRO 190 190 190 PRO PRO C . n 
C 1 191 ASP 191 191 191 ASP ASP C . n 
C 1 192 THR 192 192 192 THR THR C . n 
C 1 193 SER 193 193 193 SER SER C . n 
C 1 194 PRO 194 194 194 PRO PRO C . n 
C 1 195 ASN 195 195 195 ASN ASN C . n 
C 1 196 CYS 196 196 196 CYS CYS C . n 
C 1 197 THR 197 197 197 THR THR C . n 
C 1 198 ILE 198 198 198 ILE ILE C . n 
C 1 199 ALA 199 199 199 ALA ALA C . n 
C 1 200 GLN 200 200 200 GLN GLN C . n 
C 1 201 ASP 201 201 201 ASP ASP C . n 
C 1 202 LYS 202 202 202 LYS LYS C . n 
C 1 203 ASP 203 203 203 ASP ASP C . n 
C 1 204 SER 204 204 204 SER SER C . n 
C 1 205 LYS 205 205 205 LYS LYS C . n 
C 1 206 LEU 206 206 206 LEU LEU C . n 
C 1 207 THR 207 207 207 THR THR C . n 
C 1 208 LEU 208 208 208 LEU LEU C . n 
C 1 209 VAL 209 209 209 VAL VAL C . n 
C 1 210 LEU 210 210 210 LEU LEU C . n 
C 1 211 THR 211 211 211 THR THR C . n 
C 1 212 LYS 212 212 212 LYS LYS C . n 
C 1 213 CYS 213 213 213 CYS CYS C . n 
C 1 214 GLY 214 214 214 GLY GLY C . n 
C 1 215 SER 215 215 215 SER SER C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 LEU 218 218 218 LEU LEU C . n 
C 1 219 ALA 219 219 219 ALA ALA C . n 
C 1 220 ASN 220 220 220 ASN ASN C . n 
C 1 221 VAL 221 221 221 VAL VAL C . n 
C 1 222 SER 222 222 222 SER SER C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ILE 224 224 224 ILE ILE C . n 
C 1 225 VAL 225 225 225 VAL VAL C . n 
C 1 226 VAL 226 226 226 VAL VAL C . n 
C 1 227 ALA 227 227 227 ALA ALA C . n 
C 1 228 GLY 228 228 228 GLY GLY C . n 
C 1 229 LYS 229 229 229 LYS LYS C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 HIS 231 231 231 HIS HIS C . n 
C 1 232 ILE 232 232 232 ILE ILE C . n 
C 1 233 ILE 233 233 233 ILE ILE C . n 
C 1 234 ASN 234 234 234 ASN ASN C . n 
C 1 235 ASN 235 235 235 ASN ASN C . n 
C 1 236 LYS 236 236 236 LYS LYS C . n 
C 1 237 THR 237 237 237 THR THR C . n 
C 1 238 ASN 238 238 238 ASN ASN C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 LYS 240 240 240 LYS LYS C . n 
C 1 241 ILE 241 241 241 ILE ILE C . n 
C 1 242 LYS 242 242 242 LYS LYS C . n 
C 1 243 SER 243 243 243 SER SER C . n 
C 1 244 PHE 244 244 244 PHE PHE C . n 
C 1 245 THR 245 245 245 THR THR C . n 
C 1 246 ILE 246 246 246 ILE ILE C . n 
C 1 247 LYS 247 247 247 LYS LYS C . n 
C 1 248 LEU 248 248 248 LEU LEU C . n 
C 1 249 LEU 249 249 249 LEU LEU C . n 
C 1 250 PHE 250 250 250 PHE PHE C . n 
C 1 251 ASN 251 251 251 ASN ASN C . n 
C 1 252 LYS 252 252 252 LYS LYS C . n 
C 1 253 ASN 253 253 253 ASN ASN C . n 
C 1 254 GLY 254 254 254 GLY GLY C . n 
C 1 255 VAL 255 255 255 VAL VAL C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 LEU 257 257 257 LEU LEU C . n 
C 1 258 ASP 258 258 258 ASP ASP C . n 
C 1 259 ASN 259 259 259 ASN ASN C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 ASN 261 261 261 ASN ASN C . n 
C 1 262 LEU 262 262 262 LEU LEU C . n 
C 1 263 GLY 263 263 263 GLY GLY C . n 
C 1 264 LYS 264 264 264 LYS LYS C . n 
C 1 265 ALA 265 265 265 ALA ALA C . n 
C 1 266 TYR 266 266 266 TYR TYR C . n 
C 1 267 TRP 267 267 267 TRP TRP C . n 
C 1 268 ASN 268 268 268 ASN ASN C . n 
C 1 269 PHE 269 269 269 PHE PHE C . n 
C 1 270 ARG 270 270 270 ARG ARG C . n 
C 1 271 SER 271 271 271 SER SER C . n 
C 1 272 GLY 272 272 272 GLY GLY C . n 
C 1 273 ASN 273 273 273 ASN ASN C . n 
C 1 274 SER 274 274 274 SER SER C . n 
C 1 275 ASN 275 275 275 ASN ASN C . n 
C 1 276 VAL 276 276 276 VAL VAL C . n 
C 1 277 SER 277 277 277 SER SER C . n 
C 1 278 THR 278 278 278 THR THR C . n 
C 1 279 ALA 279 279 279 ALA ALA C . n 
C 1 280 TYR 280 280 280 TYR TYR C . n 
C 1 281 GLU 281 281 281 GLU GLU C . n 
C 1 282 LYS 282 282 282 LYS LYS C . n 
C 1 283 ALA 283 283 283 ALA ALA C . n 
C 1 284 ILE 284 284 284 ILE ILE C . n 
C 1 285 GLY 285 285 285 GLY GLY C . n 
C 1 286 PHE 286 286 286 PHE PHE C . n 
C 1 287 MET 287 287 287 MET MET C . n 
C 1 288 PRO 288 288 288 PRO PRO C . n 
C 1 289 ASN 289 289 289 ASN ASN C . n 
C 1 290 LEU 290 290 290 LEU LEU C . n 
C 1 291 VAL 291 291 291 VAL VAL C . n 
C 1 292 ALA 292 292 292 ALA ALA C . n 
C 1 293 TYR 293 293 293 TYR TYR C . n 
C 1 294 PRO 294 294 294 PRO PRO C . n 
C 1 295 LYS 295 295 295 LYS LYS C . n 
C 1 296 PRO 296 296 296 PRO PRO C . n 
C 1 297 SER 297 297 297 SER SER C . n 
C 1 298 ASN 298 298 298 ASN ASN C . n 
C 1 299 SER 299 299 299 SER SER C . n 
C 1 300 LYS 300 300 300 LYS LYS C . n 
C 1 301 LYS 301 301 301 LYS LYS C . n 
C 1 302 TYR 302 302 302 TYR TYR C . n 
C 1 303 ALA 303 303 303 ALA ALA C . n 
C 1 304 ARG 304 304 304 ARG ARG C . n 
C 1 305 ASP 305 305 305 ASP ASP C . n 
C 1 306 ILE 306 306 306 ILE ILE C . n 
C 1 307 VAL 307 307 307 VAL VAL C . n 
C 1 308 TYR 308 308 308 TYR TYR C . n 
C 1 309 GLY 309 309 309 GLY GLY C . n 
C 1 310 THR 310 310 310 THR THR C . n 
C 1 311 ILE 311 311 311 ILE ILE C . n 
C 1 312 TYR 312 312 312 TYR TYR C . n 
C 1 313 LEU 313 313 313 LEU LEU C . n 
C 1 314 GLY 314 314 314 GLY GLY C . n 
C 1 315 GLY 315 315 315 GLY GLY C . n 
C 1 316 LYS 316 316 316 LYS LYS C . n 
C 1 317 PRO 317 317 317 PRO PRO C . n 
C 1 318 ASP 318 318 318 ASP ASP C . n 
C 1 319 GLN 319 319 319 GLN GLN C . n 
C 1 320 PRO 320 320 320 PRO PRO C . n 
C 1 321 ALA 321 321 321 ALA ALA C . n 
C 1 322 VAL 322 322 322 VAL VAL C . n 
C 1 323 ILE 323 323 323 ILE ILE C . n 
C 1 324 LYS 324 324 324 LYS LYS C . n 
C 1 325 THR 325 325 325 THR THR C . n 
C 1 326 THR 326 326 326 THR THR C . n 
C 1 327 PHE 327 327 327 PHE PHE C . n 
C 1 328 ASN 328 328 328 ASN ASN C . n 
C 1 329 GLN 329 329 329 GLN GLN C . n 
C 1 330 GLU 330 330 330 GLU GLU C . n 
C 1 331 THR 331 331 331 THR THR C . n 
C 1 332 GLY 332 332 332 GLY GLY C . n 
C 1 333 CYS 333 333 333 CYS CYS C . n 
C 1 334 GLU 334 334 334 GLU GLU C . n 
C 1 335 TYR 335 335 335 TYR TYR C . n 
C 1 336 SER 336 336 336 SER SER C . n 
C 1 337 ILE 337 337 337 ILE ILE C . n 
C 1 338 THR 338 338 338 THR THR C . n 
C 1 339 PHE 339 339 339 PHE PHE C . n 
C 1 340 ASN 340 340 340 ASN ASN C . n 
C 1 341 PHE 341 341 341 PHE PHE C . n 
C 1 342 SER 342 342 342 SER SER C . n 
C 1 343 TRP 343 343 343 TRP TRP C . n 
C 1 344 SER 344 344 344 SER SER C . n 
C 1 345 LYS 345 345 345 LYS LYS C . n 
C 1 346 THR 346 346 346 THR THR C . n 
C 1 347 TYR 347 347 347 TYR TYR C . n 
C 1 348 GLU 348 348 348 GLU GLU C . n 
C 1 349 ASN 349 349 349 ASN ASN C . n 
C 1 350 VAL 350 350 350 VAL VAL C . n 
C 1 351 GLU 351 351 351 GLU GLU C . n 
C 1 352 PHE 352 352 352 PHE PHE C . n 
C 1 353 GLU 353 353 353 GLU GLU C . n 
C 1 354 THR 354 354 354 THR THR C . n 
C 1 355 THR 355 355 355 THR THR C . n 
C 1 356 SER 356 356 356 SER SER C . n 
C 1 357 PHE 357 357 357 PHE PHE C . n 
C 1 358 THR 358 358 358 THR THR C . n 
C 1 359 PHE 359 359 359 PHE PHE C . n 
C 1 360 SER 360 360 360 SER SER C . n 
C 1 361 TYR 361 361 361 TYR TYR C . n 
C 1 362 ILE 362 362 362 ILE ILE C . n 
C 1 363 ALA 363 363 363 ALA ALA C . n 
C 1 364 GLN 364 364 364 GLN GLN C . n 
C 1 365 GLU 365 365 365 GLU GLU C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ANA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ANA 
_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 
D 2 ANA 1   401 3   ANA ANA A . 
E 3 ZN  1   402 6   ZN  ZN  A . 
F 3 ZN  1   403 7   ZN  ZN  A . 
G 3 ZN  1   404 8   ZN  ZN  A . 
H 4 ACT 1   405 1   ACT ACT A . 
I 4 ACT 1   406 4   ACT ACT A . 
J 4 ACT 1   407 7   ACT ACT A . 
K 4 ACT 1   408 9   ACT ACT A . 
L 2 ANA 1   401 1   ANA ANA B . 
M 3 ZN  1   402 4   ZN  ZN  B . 
N 4 ACT 1   403 6   ACT ACT B . 
O 5 CL  1   404 1   CL  CL  B . 
P 2 ANA 1   401 2   ANA ANA C . 
Q 3 ZN  1   402 5   ZN  ZN  C . 
R 4 ACT 1   403 2   ACT ACT C . 
S 4 ACT 1   404 5   ACT ACT C . 
T 4 ACT 1   405 8   ACT ACT C . 
U 6 HOH 1   501 211 HOH HOH A . 
U 6 HOH 2   502 170 HOH HOH A . 
U 6 HOH 3   503 60  HOH HOH A . 
U 6 HOH 4   504 188 HOH HOH A . 
U 6 HOH 5   505 67  HOH HOH A . 
U 6 HOH 6   506 254 HOH HOH A . 
U 6 HOH 7   507 56  HOH HOH A . 
U 6 HOH 8   508 12  HOH HOH A . 
U 6 HOH 9   509 270 HOH HOH A . 
U 6 HOH 10  510 295 HOH HOH A . 
U 6 HOH 11  511 217 HOH HOH A . 
U 6 HOH 12  512 165 HOH HOH A . 
U 6 HOH 13  513 78  HOH HOH A . 
U 6 HOH 14  514 43  HOH HOH A . 
U 6 HOH 15  515 118 HOH HOH A . 
U 6 HOH 16  516 298 HOH HOH A . 
U 6 HOH 17  517 66  HOH HOH A . 
U 6 HOH 18  518 297 HOH HOH A . 
U 6 HOH 19  519 64  HOH HOH A . 
U 6 HOH 20  520 94  HOH HOH A . 
U 6 HOH 21  521 277 HOH HOH A . 
U 6 HOH 22  522 113 HOH HOH A . 
U 6 HOH 23  523 68  HOH HOH A . 
U 6 HOH 24  524 63  HOH HOH A . 
U 6 HOH 25  525 52  HOH HOH A . 
U 6 HOH 26  526 172 HOH HOH A . 
U 6 HOH 27  527 185 HOH HOH A . 
U 6 HOH 28  528 59  HOH HOH A . 
U 6 HOH 29  529 123 HOH HOH A . 
U 6 HOH 30  530 155 HOH HOH A . 
U 6 HOH 31  531 223 HOH HOH A . 
U 6 HOH 32  532 34  HOH HOH A . 
U 6 HOH 33  533 231 HOH HOH A . 
U 6 HOH 34  534 11  HOH HOH A . 
U 6 HOH 35  535 6   HOH HOH A . 
U 6 HOH 36  536 171 HOH HOH A . 
U 6 HOH 37  537 266 HOH HOH A . 
U 6 HOH 38  538 139 HOH HOH A . 
U 6 HOH 39  539 126 HOH HOH A . 
U 6 HOH 40  540 17  HOH HOH A . 
U 6 HOH 41  541 76  HOH HOH A . 
U 6 HOH 42  542 252 HOH HOH A . 
U 6 HOH 43  543 97  HOH HOH A . 
U 6 HOH 44  544 110 HOH HOH A . 
U 6 HOH 45  545 13  HOH HOH A . 
U 6 HOH 46  546 19  HOH HOH A . 
U 6 HOH 47  547 61  HOH HOH A . 
U 6 HOH 48  548 85  HOH HOH A . 
U 6 HOH 49  549 51  HOH HOH A . 
U 6 HOH 50  550 37  HOH HOH A . 
U 6 HOH 51  551 91  HOH HOH A . 
U 6 HOH 52  552 71  HOH HOH A . 
U 6 HOH 53  553 169 HOH HOH A . 
U 6 HOH 54  554 41  HOH HOH A . 
U 6 HOH 55  555 230 HOH HOH A . 
U 6 HOH 56  556 149 HOH HOH A . 
U 6 HOH 57  557 189 HOH HOH A . 
U 6 HOH 58  558 137 HOH HOH A . 
U 6 HOH 59  559 81  HOH HOH A . 
U 6 HOH 60  560 202 HOH HOH A . 
U 6 HOH 61  561 107 HOH HOH A . 
U 6 HOH 62  562 195 HOH HOH A . 
U 6 HOH 63  563 267 HOH HOH A . 
U 6 HOH 64  564 79  HOH HOH A . 
U 6 HOH 65  565 100 HOH HOH A . 
U 6 HOH 66  566 103 HOH HOH A . 
U 6 HOH 67  567 122 HOH HOH A . 
U 6 HOH 68  568 48  HOH HOH A . 
U 6 HOH 69  569 88  HOH HOH A . 
U 6 HOH 70  570 83  HOH HOH A . 
U 6 HOH 71  571 196 HOH HOH A . 
U 6 HOH 72  572 46  HOH HOH A . 
U 6 HOH 73  573 14  HOH HOH A . 
U 6 HOH 74  574 279 HOH HOH A . 
U 6 HOH 75  575 167 HOH HOH A . 
U 6 HOH 76  576 140 HOH HOH A . 
U 6 HOH 77  577 58  HOH HOH A . 
U 6 HOH 78  578 218 HOH HOH A . 
U 6 HOH 79  579 250 HOH HOH A . 
U 6 HOH 80  580 289 HOH HOH A . 
U 6 HOH 81  581 70  HOH HOH A . 
U 6 HOH 82  582 104 HOH HOH A . 
U 6 HOH 83  583 194 HOH HOH A . 
U 6 HOH 84  584 255 HOH HOH A . 
U 6 HOH 85  585 271 HOH HOH A . 
U 6 HOH 86  586 146 HOH HOH A . 
U 6 HOH 87  587 296 HOH HOH A . 
U 6 HOH 88  588 275 HOH HOH A . 
U 6 HOH 89  589 214 HOH HOH A . 
U 6 HOH 90  590 294 HOH HOH A . 
U 6 HOH 91  591 173 HOH HOH A . 
U 6 HOH 92  592 95  HOH HOH A . 
U 6 HOH 93  593 115 HOH HOH A . 
U 6 HOH 94  594 249 HOH HOH A . 
U 6 HOH 95  595 262 HOH HOH A . 
U 6 HOH 96  596 278 HOH HOH A . 
U 6 HOH 97  597 232 HOH HOH A . 
U 6 HOH 98  598 268 HOH HOH A . 
U 6 HOH 99  599 253 HOH HOH A . 
U 6 HOH 100 600 49  HOH HOH A . 
U 6 HOH 101 601 168 HOH HOH A . 
U 6 HOH 102 602 238 HOH HOH A . 
V 6 HOH 1   501 145 HOH HOH B . 
V 6 HOH 2   502 166 HOH HOH B . 
V 6 HOH 3   503 285 HOH HOH B . 
V 6 HOH 4   504 282 HOH HOH B . 
V 6 HOH 5   505 105 HOH HOH B . 
V 6 HOH 6   506 134 HOH HOH B . 
V 6 HOH 7   507 178 HOH HOH B . 
V 6 HOH 8   508 187 HOH HOH B . 
V 6 HOH 9   509 150 HOH HOH B . 
V 6 HOH 10  510 226 HOH HOH B . 
V 6 HOH 11  511 96  HOH HOH B . 
V 6 HOH 12  512 251 HOH HOH B . 
V 6 HOH 13  513 21  HOH HOH B . 
V 6 HOH 14  514 280 HOH HOH B . 
V 6 HOH 15  515 198 HOH HOH B . 
V 6 HOH 16  516 136 HOH HOH B . 
V 6 HOH 17  517 109 HOH HOH B . 
V 6 HOH 18  518 73  HOH HOH B . 
V 6 HOH 19  519 20  HOH HOH B . 
V 6 HOH 20  520 29  HOH HOH B . 
V 6 HOH 21  521 106 HOH HOH B . 
V 6 HOH 22  522 222 HOH HOH B . 
V 6 HOH 23  523 42  HOH HOH B . 
V 6 HOH 24  524 89  HOH HOH B . 
V 6 HOH 25  525 157 HOH HOH B . 
V 6 HOH 26  526 101 HOH HOH B . 
V 6 HOH 27  527 274 HOH HOH B . 
V 6 HOH 28  528 228 HOH HOH B . 
V 6 HOH 29  529 192 HOH HOH B . 
V 6 HOH 30  530 33  HOH HOH B . 
V 6 HOH 31  531 90  HOH HOH B . 
V 6 HOH 32  532 75  HOH HOH B . 
V 6 HOH 33  533 80  HOH HOH B . 
V 6 HOH 34  534 69  HOH HOH B . 
V 6 HOH 35  535 23  HOH HOH B . 
V 6 HOH 36  536 221 HOH HOH B . 
V 6 HOH 37  537 156 HOH HOH B . 
V 6 HOH 38  538 247 HOH HOH B . 
V 6 HOH 39  539 44  HOH HOH B . 
V 6 HOH 40  540 193 HOH HOH B . 
V 6 HOH 41  541 10  HOH HOH B . 
V 6 HOH 42  542 16  HOH HOH B . 
V 6 HOH 43  543 286 HOH HOH B . 
V 6 HOH 44  544 45  HOH HOH B . 
V 6 HOH 45  545 142 HOH HOH B . 
V 6 HOH 46  546 32  HOH HOH B . 
V 6 HOH 47  547 121 HOH HOH B . 
V 6 HOH 48  548 119 HOH HOH B . 
V 6 HOH 49  549 129 HOH HOH B . 
V 6 HOH 50  550 179 HOH HOH B . 
V 6 HOH 51  551 24  HOH HOH B . 
V 6 HOH 52  552 125 HOH HOH B . 
V 6 HOH 53  553 288 HOH HOH B . 
V 6 HOH 54  554 3   HOH HOH B . 
V 6 HOH 55  555 205 HOH HOH B . 
V 6 HOH 56  556 128 HOH HOH B . 
V 6 HOH 57  557 272 HOH HOH B . 
V 6 HOH 58  558 15  HOH HOH B . 
V 6 HOH 59  559 40  HOH HOH B . 
V 6 HOH 60  560 98  HOH HOH B . 
V 6 HOH 61  561 22  HOH HOH B . 
V 6 HOH 62  562 216 HOH HOH B . 
V 6 HOH 63  563 284 HOH HOH B . 
V 6 HOH 64  564 227 HOH HOH B . 
V 6 HOH 65  565 92  HOH HOH B . 
V 6 HOH 66  566 144 HOH HOH B . 
V 6 HOH 67  567 281 HOH HOH B . 
V 6 HOH 68  568 143 HOH HOH B . 
V 6 HOH 69  569 299 HOH HOH B . 
V 6 HOH 70  570 186 HOH HOH B . 
V 6 HOH 71  571 287 HOH HOH B . 
V 6 HOH 72  572 147 HOH HOH B . 
V 6 HOH 73  573 191 HOH HOH B . 
V 6 HOH 74  574 273 HOH HOH B . 
V 6 HOH 75  575 233 HOH HOH B . 
V 6 HOH 76  576 300 HOH HOH B . 
V 6 HOH 77  577 283 HOH HOH B . 
V 6 HOH 78  578 131 HOH HOH B . 
V 6 HOH 79  579 234 HOH HOH B . 
V 6 HOH 80  580 248 HOH HOH B . 
W 6 HOH 1   501 163 HOH HOH C . 
W 6 HOH 2   502 158 HOH HOH C . 
W 6 HOH 3   503 210 HOH HOH C . 
W 6 HOH 4   504 154 HOH HOH C . 
W 6 HOH 5   505 35  HOH HOH C . 
W 6 HOH 6   506 183 HOH HOH C . 
W 6 HOH 7   507 290 HOH HOH C . 
W 6 HOH 8   508 175 HOH HOH C . 
W 6 HOH 9   509 301 HOH HOH C . 
W 6 HOH 10  510 87  HOH HOH C . 
W 6 HOH 11  511 213 HOH HOH C . 
W 6 HOH 12  512 62  HOH HOH C . 
W 6 HOH 13  513 28  HOH HOH C . 
W 6 HOH 14  514 164 HOH HOH C . 
W 6 HOH 15  515 258 HOH HOH C . 
W 6 HOH 16  516 181 HOH HOH C . 
W 6 HOH 17  517 219 HOH HOH C . 
W 6 HOH 18  518 77  HOH HOH C . 
W 6 HOH 19  519 27  HOH HOH C . 
W 6 HOH 20  520 72  HOH HOH C . 
W 6 HOH 21  521 184 HOH HOH C . 
W 6 HOH 22  522 50  HOH HOH C . 
W 6 HOH 23  523 127 HOH HOH C . 
W 6 HOH 24  524 84  HOH HOH C . 
W 6 HOH 25  525 117 HOH HOH C . 
W 6 HOH 26  526 130 HOH HOH C . 
W 6 HOH 27  527 36  HOH HOH C . 
W 6 HOH 28  528 31  HOH HOH C . 
W 6 HOH 29  529 53  HOH HOH C . 
W 6 HOH 30  530 82  HOH HOH C . 
W 6 HOH 31  531 276 HOH HOH C . 
W 6 HOH 32  532 148 HOH HOH C . 
W 6 HOH 33  533 54  HOH HOH C . 
W 6 HOH 34  534 220 HOH HOH C . 
W 6 HOH 35  535 8   HOH HOH C . 
W 6 HOH 36  536 39  HOH HOH C . 
W 6 HOH 37  537 74  HOH HOH C . 
W 6 HOH 38  538 116 HOH HOH C . 
W 6 HOH 39  539 18  HOH HOH C . 
W 6 HOH 40  540 174 HOH HOH C . 
W 6 HOH 41  541 246 HOH HOH C . 
W 6 HOH 42  542 141 HOH HOH C . 
W 6 HOH 43  543 291 HOH HOH C . 
W 6 HOH 44  544 111 HOH HOH C . 
W 6 HOH 45  545 162 HOH HOH C . 
W 6 HOH 46  546 26  HOH HOH C . 
W 6 HOH 47  547 224 HOH HOH C . 
W 6 HOH 48  548 108 HOH HOH C . 
W 6 HOH 49  549 99  HOH HOH C . 
W 6 HOH 50  550 225 HOH HOH C . 
W 6 HOH 51  551 160 HOH HOH C . 
W 6 HOH 52  552 65  HOH HOH C . 
W 6 HOH 53  553 180 HOH HOH C . 
W 6 HOH 54  554 229 HOH HOH C . 
W 6 HOH 55  555 265 HOH HOH C . 
W 6 HOH 56  556 204 HOH HOH C . 
W 6 HOH 57  557 264 HOH HOH C . 
W 6 HOH 58  558 257 HOH HOH C . 
W 6 HOH 59  559 206 HOH HOH C . 
W 6 HOH 60  560 292 HOH HOH C . 
W 6 HOH 61  561 30  HOH HOH C . 
W 6 HOH 62  562 201 HOH HOH C . 
W 6 HOH 63  563 199 HOH HOH C . 
W 6 HOH 64  564 256 HOH HOH C . 
W 6 HOH 65  565 207 HOH HOH C . 
W 6 HOH 66  566 138 HOH HOH C . 
W 6 HOH 67  567 159 HOH HOH C . 
W 6 HOH 68  568 245 HOH HOH C . 
W 6 HOH 69  569 55  HOH HOH C . 
W 6 HOH 70  570 132 HOH HOH C . 
W 6 HOH 71  571 86  HOH HOH C . 
W 6 HOH 72  572 177 HOH HOH C . 
W 6 HOH 73  573 203 HOH HOH C . 
W 6 HOH 74  574 259 HOH HOH C . 
W 6 HOH 75  575 135 HOH HOH C . 
W 6 HOH 76  576 236 HOH HOH C . 
W 6 HOH 77  577 269 HOH HOH C . 
W 6 HOH 78  578 153 HOH HOH C . 
W 6 HOH 79  579 190 HOH HOH C . 
W 6 HOH 80  580 102 HOH HOH C . 
W 6 HOH 81  581 93  HOH HOH C . 
W 6 HOH 82  582 260 HOH HOH C . 
W 6 HOH 83  583 241 HOH HOH C . 
W 6 HOH 84  584 237 HOH HOH C . 
W 6 HOH 85  585 261 HOH HOH C . 
W 6 HOH 86  586 182 HOH HOH C . 
W 6 HOH 87  587 152 HOH HOH C . 
W 6 HOH 88  588 161 HOH HOH C . 
W 6 HOH 89  589 235 HOH HOH C . 
W 6 HOH 90  590 293 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASN 181 ? CG  ? A ASN 181 CG  
2  1 Y 1 A ASN 181 ? OD1 ? A ASN 181 OD1 
3  1 Y 1 A ASN 181 ? ND2 ? A ASN 181 ND2 
4  1 Y 1 A THR 183 ? OG1 ? A THR 183 OG1 
5  1 Y 1 A THR 183 ? CG2 ? A THR 183 CG2 
6  1 Y 1 A ARG 184 ? NE  ? A ARG 184 NE  
7  1 Y 1 A ARG 184 ? CZ  ? A ARG 184 CZ  
8  1 Y 1 A ARG 184 ? NH1 ? A ARG 184 NH1 
9  1 Y 1 A ARG 184 ? NH2 ? A ARG 184 NH2 
10 1 Y 1 A LYS 236 ? CG  ? A LYS 236 CG  
11 1 Y 1 A LYS 236 ? CD  ? A LYS 236 CD  
12 1 Y 1 A LYS 236 ? CE  ? A LYS 236 CE  
13 1 Y 1 A LYS 236 ? NZ  ? A LYS 236 NZ  
14 1 Y 1 A THR 237 ? OG1 ? A THR 237 OG1 
15 1 Y 1 A THR 237 ? CG2 ? A THR 237 CG2 
16 1 Y 1 A ASN 238 ? CG  ? A ASN 238 CG  
17 1 Y 1 A ASN 238 ? OD1 ? A ASN 238 OD1 
18 1 Y 1 A ASN 238 ? ND2 ? A ASN 238 ND2 
19 1 Y 1 A LYS 252 ? CD  ? A LYS 252 CD  
20 1 Y 1 A LYS 252 ? CE  ? A LYS 252 CE  
21 1 Y 1 A LYS 252 ? NZ  ? A LYS 252 NZ  
22 1 Y 1 A LYS 282 ? CE  ? A LYS 282 CE  
23 1 Y 1 A LYS 282 ? NZ  ? A LYS 282 NZ  
24 1 Y 1 A SER 299 ? OG  ? A SER 299 OG  
25 1 Y 1 A LYS 301 ? CG  ? A LYS 301 CG  
26 1 Y 1 A LYS 301 ? CD  ? A LYS 301 CD  
27 1 Y 1 A LYS 301 ? CE  ? A LYS 301 CE  
28 1 Y 1 A LYS 301 ? NZ  ? A LYS 301 NZ  
29 1 Y 1 B THR 183 ? OG1 ? B THR 183 OG1 
30 1 Y 1 B THR 183 ? CG2 ? B THR 183 CG2 
31 1 Y 1 B ARG 184 ? NE  ? B ARG 184 NE  
32 1 Y 1 B ARG 184 ? CZ  ? B ARG 184 CZ  
33 1 Y 1 B ARG 184 ? NH1 ? B ARG 184 NH1 
34 1 Y 1 B ARG 184 ? NH2 ? B ARG 184 NH2 
35 1 Y 1 B LYS 202 ? CE  ? B LYS 202 CE  
36 1 Y 1 B LYS 202 ? NZ  ? B LYS 202 NZ  
37 1 Y 1 B LYS 240 ? CD  ? B LYS 240 CD  
38 1 Y 1 B LYS 240 ? CE  ? B LYS 240 CE  
39 1 Y 1 B LYS 240 ? NZ  ? B LYS 240 NZ  
40 1 Y 1 B ASN 268 ? CG  ? B ASN 268 CG  
41 1 Y 1 B ASN 268 ? OD1 ? B ASN 268 OD1 
42 1 Y 1 B ASN 268 ? ND2 ? B ASN 268 ND2 
43 1 Y 1 B LYS 282 ? CG  ? B LYS 282 CG  
44 1 Y 1 B LYS 282 ? CD  ? B LYS 282 CD  
45 1 Y 1 B LYS 282 ? CE  ? B LYS 282 CE  
46 1 Y 1 B LYS 282 ? NZ  ? B LYS 282 NZ  
47 1 Y 1 B LYS 300 ? CG  ? B LYS 300 CG  
48 1 Y 1 B LYS 300 ? CD  ? B LYS 300 CD  
49 1 Y 1 B LYS 300 ? CE  ? B LYS 300 CE  
50 1 Y 1 B LYS 300 ? NZ  ? B LYS 300 NZ  
51 1 Y 1 B LYS 316 ? CE  ? B LYS 316 CE  
52 1 Y 1 B LYS 316 ? NZ  ? B LYS 316 NZ  
53 1 Y 1 C LYS 202 ? CD  ? C LYS 202 CD  
54 1 Y 1 C LYS 202 ? CE  ? C LYS 202 CE  
55 1 Y 1 C LYS 202 ? NZ  ? C LYS 202 NZ  
56 1 Y 1 C LYS 236 ? CG  ? C LYS 236 CG  
57 1 Y 1 C LYS 236 ? CD  ? C LYS 236 CD  
58 1 Y 1 C LYS 236 ? CE  ? C LYS 236 CE  
59 1 Y 1 C LYS 236 ? NZ  ? C LYS 236 NZ  
60 1 Y 1 C LYS 240 ? CG  ? C LYS 240 CG  
61 1 Y 1 C LYS 240 ? CD  ? C LYS 240 CD  
62 1 Y 1 C LYS 240 ? CE  ? C LYS 240 CE  
63 1 Y 1 C LYS 240 ? NZ  ? C LYS 240 NZ  
64 1 Y 1 C LYS 252 ? CG  ? C LYS 252 CG  
65 1 Y 1 C LYS 252 ? CD  ? C LYS 252 CD  
66 1 Y 1 C LYS 252 ? CE  ? C LYS 252 CE  
67 1 Y 1 C LYS 252 ? NZ  ? C LYS 252 NZ  
68 1 Y 1 C GLU 281 ? CG  ? C GLU 281 CG  
69 1 Y 1 C GLU 281 ? CD  ? C GLU 281 CD  
70 1 Y 1 C GLU 281 ? OE1 ? C GLU 281 OE1 
71 1 Y 1 C GLU 281 ? OE2 ? C GLU 281 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.10.1_2155 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.747 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FAH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.881 
_cell.length_a_esd                 ? 
_cell.length_b                     66.726 
_cell.length_b_esd                 ? 
_cell.length_c                     73.949 
_cell.length_c_esd                 ? 
_cell.volume                       278107.432 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9FAH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_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                   9FAH 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '26% PEG 8000, 0.1 M HEPES pH 6.9, 0.05 M zinc acetate' 
_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 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-03-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          26.331140676 
_reflns.entry_id                                       9FAH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.65 
_reflns.d_resolution_low                               50 
_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                                     65451 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.8 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_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                                    1.65 
_reflns_shell.d_res_low                                     1.74 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10438 
_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                               6.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.495 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.7 
_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                               34.7471423124 
_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                                 9FAH 
_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                            1.65336537283 
_refine.ls_d_res_low                             47.9040909403 
_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                     65451 
_refine.ls_number_reflns_R_free                  3273 
_refine.ls_number_reflns_R_work                  62178 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7227004708 
_refine.ls_percent_reflns_R_free                 5.00068753724 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.159336092102 
_refine.ls_R_factor_R_free                       0.190329875849 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.157671212129 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36673149348 
_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          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.4086590016 
_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                            0.199489811402 
_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                       1.65336537283 
_refine_hist.d_res_low                        47.9040909403 
_refine_hist.number_atoms_solvent             272 
_refine_hist.number_atoms_total               4619 
_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        4234 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         113 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0100001870461  ? 4442 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.05571063329    ? 6051 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0708199743502  ? 699  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.00736903992421 ? 764  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.100127176     ? 2613 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.6534 1.678         . . 135 2576 95.323488045  . . . . 0.303221697635 . . . . . . . . . . . 0.31856752426  
'X-RAY DIFFRACTION' 1.678  1.7043        . . 141 2683 100.0         . . . . 0.283407068928 . . . . . . . . . . . 0.350584221616 
'X-RAY DIFFRACTION' 1.7043 1.7322        . . 143 2702 100.0         . . . . 0.262273124867 . . . . . . . . . . . 0.296885511166 
'X-RAY DIFFRACTION' 1.7322 1.7621        . . 141 2697 99.9647763297 . . . . 0.250448841836 . . . . . . . . . . . 0.302561914542 
'X-RAY DIFFRACTION' 1.7621 1.7941        . . 142 2693 99.9647390691 . . . . 0.236021376969 . . . . . . . . . . . 0.310964014891 
'X-RAY DIFFRACTION' 1.7941 1.8286        . . 141 2679 100.0         . . . . 0.212033006186 . . . . . . . . . . . 0.263387016866 
'X-RAY DIFFRACTION' 1.8286 1.866         . . 143 2712 99.9299964998 . . . . 0.203121111992 . . . . . . . . . . . 0.252495576626 
'X-RAY DIFFRACTION' 1.866  1.9065        . . 144 2731 99.9652294854 . . . . 0.188405889606 . . . . . . . . . . . 0.22187999733  
'X-RAY DIFFRACTION' 1.9065 1.9509        . . 141 2677 99.8936547324 . . . . 0.195691649159 . . . . . . . . . . . 0.22915678898  
'X-RAY DIFFRACTION' 1.9509 1.9997        . . 140 2672 99.9644507643 . . . . 0.161501975627 . . . . . . . . . . . 0.1943678153   
'X-RAY DIFFRACTION' 1.9997 2.0537        . . 143 2714 99.9300454704 . . . . 0.147544327064 . . . . . . . . . . . 0.199549395915 
'X-RAY DIFFRACTION' 2.0537 2.1142        . . 143 2714 99.9650104969 . . . . 0.156610276447 . . . . . . . . . . . 0.21371038664  
'X-RAY DIFFRACTION' 2.1142 2.1824        . . 142 2700 100.0         . . . . 0.155092252263 . . . . . . . . . . . 0.190139520244 
'X-RAY DIFFRACTION' 2.1824 2.2604        . . 142 2692 99.6483825598 . . . . 0.153620834852 . . . . . . . . . . . 0.204406864603 
'X-RAY DIFFRACTION' 2.2604 2.3509        . . 143 2707 99.9298737728 . . . . 0.155147844783 . . . . . . . . . . . 0.2003081953   
'X-RAY DIFFRACTION' 2.3509 2.4579        . . 142 2697 100.0         . . . . 0.157597165251 . . . . . . . . . . . 0.196443924422 
'X-RAY DIFFRACTION' 2.4579 2.5875        . . 144 2735 100.0         . . . . 0.160586086917 . . . . . . . . . . . 0.195781126883 
'X-RAY DIFFRACTION' 2.5875 2.7496        . . 142 2700 100.0         . . . . 0.156453753522 . . . . . . . . . . . 0.201742675589 
'X-RAY DIFFRACTION' 2.7496 2.9618        . . 142 2710 99.9299229152 . . . . 0.160167777336 . . . . . . . . . . . 0.199450725492 
'X-RAY DIFFRACTION' 2.9618 3.2599        . . 144 2724 99.9303135889 . . . . 0.155537797019 . . . . . . . . . . . 0.200907803207 
'X-RAY DIFFRACTION' 3.2599 3.7314        . . 143 2724 99.6870653686 . . . . 0.137627302183 . . . . . . . . . . . 0.158300982912 
'X-RAY DIFFRACTION' 3.7314 4.7005        . . 144 2742 99.6546961326 . . . . 0.1226454525   . . . . . . . . . . . 0.130293378626 
'X-RAY DIFFRACTION' 4.7005 47.9040909403 . . 148 2797 99.9321343739 . . . . 0.156376883875 . . . . . . . . . . . 0.186203836794 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 ? 
2 1 ? 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 1 A ASN 181 . A THR 185 . A ASN 181 A THR 185 ? 
;(chain A and ((resid 181 and (name O or name N or name CA or name C )) or resseq 182:185 or (resid 186 and (name N or name C or name O or name CB or name CG or name CD2)) or resseq 187:201 or (resid 202 and (name N or name CA or name C or name O or name CB or name CG )) or resseq 203:239 or (resid 240 and (name N or name CA or name C or name O or name CB )) or resseq 241:251 or (resid 252 and (name N or name CA or name C or name O or name CB )) or resseq 253:280 or (resid 281 and (name N or name CA or name C or name O or name CB )) or resseq 282:296 or resseq 299:337 or resseq 339:352 or (resid 353 and (name N or name C or name O or name CB or name CG or name CD or name OE1 or name OE2)) or resseq 354:360 or (resid 361 and (name N or name CA or name C or name O or name CB or name CG or name CD1 or name CE1 or name CZ or name OH )) or resseq 362:365))
;
1 1 2 A TRP 187 . A PRO 296 . A TRP 187 A PRO 296 ? 
;(chain A and ((resid 181 and (name O or name N or name CA or name C )) or resseq 182:185 or (resid 186 and (name N or name C or name O or name CB or name CG or name CD2)) or resseq 187:201 or (resid 202 and (name N or name CA or name C or name O or name CB or name CG )) or resseq 203:239 or (resid 240 and (name N or name CA or name C or name O or name CB )) or resseq 241:251 or (resid 252 and (name N or name CA or name C or name O or name CB )) or resseq 253:280 or (resid 281 and (name N or name CA or name C or name O or name CB )) or resseq 282:296 or resseq 299:337 or resseq 339:352 or (resid 353 and (name N or name C or name O or name CB or name CG or name CD or name OE1 or name OE2)) or resseq 354:360 or (resid 361 and (name N or name CA or name C or name O or name CB or name CG or name CD1 or name CE1 or name CZ or name OH )) or resseq 362:365))
;
1 1 3 A SER 299 . A ILE 337 . A SER 299 A ILE 337 ? 
;(chain A and ((resid 181 and (name O or name N or name CA or name C )) or resseq 182:185 or (resid 186 and (name N or name C or name O or name CB or name CG or name CD2)) or resseq 187:201 or (resid 202 and (name N or name CA or name C or name O or name CB or name CG )) or resseq 203:239 or (resid 240 and (name N or name CA or name C or name O or name CB )) or resseq 241:251 or (resid 252 and (name N or name CA or name C or name O or name CB )) or resseq 253:280 or (resid 281 and (name N or name CA or name C or name O or name CB )) or resseq 282:296 or resseq 299:337 or resseq 339:352 or (resid 353 and (name N or name C or name O or name CB or name CG or name CD or name OE1 or name OE2)) or resseq 354:360 or (resid 361 and (name N or name CA or name C or name O or name CB or name CG or name CD1 or name CE1 or name CZ or name OH )) or resseq 362:365))
;
1 1 4 A PHE 339 . A GLU 365 . A PHE 339 A GLU 365 ? 
;(chain A and ((resid 181 and (name O or name N or name CA or name C )) or resseq 182:185 or (resid 186 and (name N or name C or name O or name CB or name CG or name CD2)) or resseq 187:201 or (resid 202 and (name N or name CA or name C or name O or name CB or name CG )) or resseq 203:239 or (resid 240 and (name N or name CA or name C or name O or name CB )) or resseq 241:251 or (resid 252 and (name N or name CA or name C or name O or name CB )) or resseq 253:280 or (resid 281 and (name N or name CA or name C or name O or name CB )) or resseq 282:296 or resseq 299:337 or resseq 339:352 or (resid 353 and (name N or name C or name O or name CB or name CG or name CD or name OE1 or name OE2)) or resseq 354:360 or (resid 361 and (name N or name CA or name C or name O or name CB or name CG or name CD1 or name CE1 or name CZ or name OH )) or resseq 362:365))
;
1 2 1 C ASN 181 . C THR 185 . C ASN 181 C THR 185 ? 
;(chain C and ((resid 181 and (name N or name CA or name C or name CB )) or resseq 182 or (resid 183 and (name N or name CA or name C or name O or name CB )) or (resid 184 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resseq 185 or (resid 186 and (name N or name C or name O or name CB or name CG or name CD2)) or resseq 187:236 or (resid 237 and (name N or name CA or name C or name O or name CB )) or (resid 238 and (name N or name CA or name C or name O or name CB )) or resseq 239:281 or (resid 282 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resseq 283:296 or (resid 299 and (name N or name CA or name C or name O or name CB )) or resseq 300 or (resid 301 and (name N or name CA or name C or name O or name CB )) or resseq 302:337 or resseq 339:352 or (resid 353 and (name N or name C or name O or name CB or name CG or name CD or name OE1 or name OE2)) or resseq 354:360 or (resid 361 and (name N or name CA or name C or name O or name CB or name CG or name CD1 or name CE1 or name CZ or name OH )) or resseq 362:365))
;
1 2 2 C TRP 187 . C PRO 296 . C TRP 187 C PRO 296 ? 
;(chain C and ((resid 181 and (name N or name CA or name C or name CB )) or resseq 182 or (resid 183 and (name N or name CA or name C or name O or name CB )) or (resid 184 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resseq 185 or (resid 186 and (name N or name C or name O or name CB or name CG or name CD2)) or resseq 187:236 or (resid 237 and (name N or name CA or name C or name O or name CB )) or (resid 238 and (name N or name CA or name C or name O or name CB )) or resseq 239:281 or (resid 282 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resseq 283:296 or (resid 299 and (name N or name CA or name C or name O or name CB )) or resseq 300 or (resid 301 and (name N or name CA or name C or name O or name CB )) or resseq 302:337 or resseq 339:352 or (resid 353 and (name N or name C or name O or name CB or name CG or name CD or name OE1 or name OE2)) or resseq 354:360 or (resid 361 and (name N or name CA or name C or name O or name CB or name CG or name CD1 or name CE1 or name CZ or name OH )) or resseq 362:365))
;
1 2 3 C SER 299 . C ILE 337 . C SER 299 C ILE 337 ? 
;(chain C and ((resid 181 and (name N or name CA or name C or name CB )) or resseq 182 or (resid 183 and (name N or name CA or name C or name O or name CB )) or (resid 184 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resseq 185 or (resid 186 and (name N or name C or name O or name CB or name CG or name CD2)) or resseq 187:236 or (resid 237 and (name N or name CA or name C or name O or name CB )) or (resid 238 and (name N or name CA or name C or name O or name CB )) or resseq 239:281 or (resid 282 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resseq 283:296 or (resid 299 and (name N or name CA or name C or name O or name CB )) or resseq 300 or (resid 301 and (name N or name CA or name C or name O or name CB )) or resseq 302:337 or resseq 339:352 or (resid 353 and (name N or name C or name O or name CB or name CG or name CD or name OE1 or name OE2)) or resseq 354:360 or (resid 361 and (name N or name CA or name C or name O or name CB or name CG or name CD1 or name CE1 or name CZ or name OH )) or resseq 362:365))
;
1 2 4 C PHE 339 . C GLU 365 . C PHE 339 C GLU 365 ? 
;(chain C and ((resid 181 and (name N or name CA or name C or name CB )) or resseq 182 or (resid 183 and (name N or name CA or name C or name O or name CB )) or (resid 184 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resseq 185 or (resid 186 and (name N or name C or name O or name CB or name CG or name CD2)) or resseq 187:236 or (resid 237 and (name N or name CA or name C or name O or name CB )) or (resid 238 and (name N or name CA or name C or name O or name CB )) or resseq 239:281 or (resid 282 and (name N or name CA or name C or name O or name CB or name CG or name CD )) or resseq 283:296 or (resid 299 and (name N or name CA or name C or name O or name CB )) or resseq 300 or (resid 301 and (name N or name CA or name C or name O or name CB )) or resseq 302:337 or resseq 339:352 or (resid 353 and (name N or name C or name O or name CB or name CG or name CD or name OE1 or name OE2)) or resseq 354:360 or (resid 361 and (name N or name CA or name C or name O or name CB or name CG or name CD1 or name CE1 or name CZ or name OH )) or resseq 362:365))
;
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     9FAH 
_struct.title                        'Human adenovirus type 37 fiber knob in complex with 4-O,5-N-diacetylneuraminic acid' 
_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        9FAH 
_struct_keywords.text            'fiber knob, complex, sialic acid, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 2 ? 
M N N 3 ? 
N N N 4 ? 
O N N 5 ? 
P N N 2 ? 
Q N N 3 ? 
R N N 4 ? 
S N N 4 ? 
T N N 4 ? 
U N N 6 ? 
V N N 6 ? 
W N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q64823_9ADEN 
_struct_ref.pdbx_db_accession          Q64823 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSKRLRVEDDFNPVYPYGYARNQNIPFLTPPFVSSDGFKNFPPGVLSLKLADPITITNGDVSLKVGGGLTLQDGSLTVNP
KAPLQVNTDKKLELAYDNPFESSANKLSLKVGHGLKVLDEKSAAGLKDLIGKLVVLTGKGIGTENLENTDGSSRGIGINV
RAREGLTFDNDGYLVAWNPKYDTRTLWTTPDTSPNCTIAQDKDSKLTLVLTKCGSQILANVSLIVVAGKYHIINNKTNPK
IKSFTIKLLFNKNGVLLDNSNLGKAYWNFRSGNSNVSTAYEKAIGFMPNLVAYPKPSNSKKYARDIVYGTIYLGGKPDQP
AVIKTTFNQETGCEYSITFNFSWSKTYENVEFETTSFTFSYIAQE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FAH A 1 ? 365 ? Q64823 1 ? 365 ? 1 365 
2 1 9FAH B 1 ? 365 ? Q64823 1 ? 365 ? 1 365 
3 1 9FAH C 1 ? 365 ? Q64823 1 ? 365 ? 1 365 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9FAH ASN A 181 ? UNP Q64823 TYR 181 conflict 181 1 
2 9FAH ASN B 181 ? UNP Q64823 TYR 181 conflict 181 2 
3 9FAH ASN C 181 ? UNP Q64823 TYR 181 conflict 181 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9820  ? 
1 MORE         -178  ? 
1 'SSA (A^2)'  19930 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 GLY A 263 ? TRP A 267 ? GLY A 263 TRP A 267 5 ? 5 
HELX_P HELX_P2  AA2 ALA A 283 ? MET A 287 ? ALA A 283 MET A 287 5 ? 5 
HELX_P HELX_P3  AA3 TYR A 302 ? ARG A 304 ? TYR A 302 ARG A 304 5 ? 3 
HELX_P HELX_P4  AA4 GLY A 314 ? LYS A 316 ? GLY A 314 LYS A 316 5 ? 3 
HELX_P HELX_P5  AA5 GLY B 263 ? TRP B 267 ? GLY B 263 TRP B 267 5 ? 5 
HELX_P HELX_P6  AA6 ALA B 283 ? MET B 287 ? ALA B 283 MET B 287 5 ? 5 
HELX_P HELX_P7  AA7 TYR B 302 ? ARG B 304 ? TYR B 302 ARG B 304 5 ? 3 
HELX_P HELX_P8  AA8 GLY B 314 ? LYS B 316 ? GLY B 314 LYS B 316 5 ? 3 
HELX_P HELX_P9  AA9 GLY C 263 ? TRP C 267 ? GLY C 263 TRP C 267 5 ? 5 
HELX_P HELX_P10 AB1 ALA C 283 ? MET C 287 ? ALA C 283 MET C 287 5 ? 5 
HELX_P HELX_P11 AB2 TYR C 302 ? ARG C 304 ? TYR C 302 ARG C 304 5 ? 3 
HELX_P HELX_P12 AB3 GLY C 314 ? LYS C 316 ? GLY C 314 LYS C 316 5 ? 3 
# 
_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 
metalc1  metalc ? ? A LYS 212 NZ  ? ? ? 1_555 F ZN  .   ZN  ? ? A LYS 212 A ZN  403 1_555 ? ? ? ? ? ? ? 2.412 ? ? 
metalc2  metalc ? ? A HIS 231 NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 231 A ZN  402 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc3  metalc ? ? A ASP 258 OD1 ? ? ? 1_555 Q ZN  .   ZN  ? ? A ASP 258 C ZN  402 2_546 ? ? ? ? ? ? ? 2.338 ? ? 
metalc4  metalc ? ? A ASP 258 OD2 ? ? ? 1_555 Q ZN  .   ZN  ? ? A ASP 258 C ZN  402 2_546 ? ? ? ? ? ? ? 2.000 ? ? 
metalc5  metalc ? ? A GLU 351 OE2 ? ? ? 1_555 G ZN  .   ZN  ? ? A GLU 351 A ZN  404 1_555 ? ? ? ? ? ? ? 1.947 ? ? 
metalc6  metalc ? ? A GLU 365 O   ? ? ? 1_555 F ZN  .   ZN  ? ? A GLU 365 A ZN  403 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc7  metalc ? ? A GLU 365 OXT ? ? ? 1_555 F ZN  .   ZN  ? ? A GLU 365 A ZN  403 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc8  metalc ? ? E ZN  .   ZN  ? ? ? 2_555 B GLU 348 OE1 ? ? A ZN  402 B GLU 348 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc9  metalc ? ? E ZN  .   ZN  ? ? ? 2_555 B GLU 348 OE2 ? ? A ZN  402 B GLU 348 1_555 ? ? ? ? ? ? ? 2.608 ? ? 
metalc10 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 V HOH .   O   ? ? A ZN  402 B HOH 556 2_545 ? ? ? ? ? ? ? 2.108 ? ? 
metalc11 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 V HOH .   O   ? ? A ZN  402 B HOH 569 2_545 ? ? ? ? ? ? ? 2.510 ? ? 
metalc12 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 V HOH .   O   ? ? A ZN  402 B HOH 576 2_545 ? ? ? ? ? ? ? 2.150 ? ? 
metalc13 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 R ACT .   O   ? ? A ZN  403 C ACT 403 1_555 ? ? ? ? ? ? ? 2.185 ? ? 
metalc14 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 R ACT .   OXT ? ? A ZN  403 C ACT 403 1_555 ? ? ? ? ? ? ? 2.695 ? ? 
metalc15 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 H ACT .   O   ? ? A ZN  404 A ACT 405 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc16 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 U HOH .   O   ? ? A ZN  404 A HOH 590 1_555 ? ? ? ? ? ? ? 2.185 ? ? 
metalc17 metalc ? ? G ZN  .   ZN  ? ? ? 2_555 B LYS 236 NZ  ? ? A ZN  404 B LYS 236 1_555 ? ? ? ? ? ? ? 1.925 ? ? 
metalc18 metalc ? ? B HIS 231 NE2 ? ? ? 1_555 M ZN  .   ZN  ? ? B HIS 231 B ZN  402 1_555 ? ? ? ? ? ? ? 2.564 ? ? 
metalc19 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 W HOH .   O   ? ? B ZN  402 C HOH 579 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc20 metalc ? ? C HIS 231 NE2 ? ? ? 1_555 Q ZN  .   ZN  ? ? C HIS 231 C ZN  402 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
metalc21 metalc ? ? C GLU 351 OE1 ? ? ? 1_555 Q ZN  .   ZN  ? ? C GLU 351 C ZN  402 1_555 ? ? ? ? ? ? ? 1.876 ? ? 
metalc22 metalc ? ? Q ZN  .   ZN  ? ? ? 1_555 W HOH .   O   ? ? C ZN  402 C HOH 502 1_555 ? ? ? ? ? ? ? 1.922 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NZ  ? A LYS 212 ? A LYS 212 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 O   ? A GLU 365 ? A GLU 365 ? 1_555 77.9  ? 
2  NZ  ? A LYS 212 ? A LYS 212 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 OXT ? A GLU 365 ? A GLU 365 ? 1_555 134.6 ? 
3  O   ? A GLU 365 ? A GLU 365 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 OXT ? A GLU 365 ? A GLU 365 ? 1_555 57.5  ? 
4  NZ  ? A LYS 212 ? A LYS 212 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 O   ? R ACT .   ? C ACT 403 ? 1_555 117.8 ? 
5  O   ? A GLU 365 ? A GLU 365 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 O   ? R ACT .   ? C ACT 403 ? 1_555 132.7 ? 
6  OXT ? A GLU 365 ? A GLU 365 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 O   ? R ACT .   ? C ACT 403 ? 1_555 90.2  ? 
7  NZ  ? A LYS 212 ? A LYS 212 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 OXT ? R ACT .   ? C ACT 403 ? 1_555 98.6  ? 
8  O   ? A GLU 365 ? A GLU 365 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 OXT ? R ACT .   ? C ACT 403 ? 1_555 176.2 ? 
9  OXT ? A GLU 365 ? A GLU 365 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 OXT ? R ACT .   ? C ACT 403 ? 1_555 126.1 ? 
10 O   ? R ACT .   ? C ACT 403 ? 1_555 ZN ? F ZN . ? A ZN 403 ? 1_555 OXT ? R ACT .   ? C ACT 403 ? 1_555 50.2  ? 
11 NE2 ? A HIS 231 ? A HIS 231 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 OE1 ? B GLU 348 ? B GLU 348 ? 1_555 81.7  ? 
12 NE2 ? A HIS 231 ? A HIS 231 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 OE2 ? B GLU 348 ? B GLU 348 ? 1_555 83.7  ? 
13 OE1 ? B GLU 348 ? B GLU 348 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 OE2 ? B GLU 348 ? B GLU 348 ? 1_555 2.2   ? 
14 NE2 ? A HIS 231 ? A HIS 231 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 556 ? 2_545 92.2  ? 
15 OE1 ? B GLU 348 ? B GLU 348 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 556 ? 2_545 55.0  ? 
16 OE2 ? B GLU 348 ? B GLU 348 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 556 ? 2_545 54.0  ? 
17 NE2 ? A HIS 231 ? A HIS 231 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 569 ? 2_545 100.2 ? 
18 OE1 ? B GLU 348 ? B GLU 348 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 569 ? 2_545 108.9 ? 
19 OE2 ? B GLU 348 ? B GLU 348 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 569 ? 2_545 109.3 ? 
20 O   ? V HOH .   ? B HOH 556 ? 2_545 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 569 ? 2_545 158.2 ? 
21 NE2 ? A HIS 231 ? A HIS 231 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 576 ? 2_545 115.4 ? 
22 OE1 ? B GLU 348 ? B GLU 348 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 576 ? 2_545 66.5  ? 
23 OE2 ? B GLU 348 ? B GLU 348 ? 1_555 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 576 ? 2_545 66.0  ? 
24 O   ? V HOH .   ? B HOH 556 ? 2_545 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 576 ? 2_545 109.7 ? 
25 O   ? V HOH .   ? B HOH 569 ? 2_545 ZN ? E ZN . ? A ZN 402 ? 1_555 O   ? V HOH .   ? B HOH 576 ? 2_545 48.7  ? 
26 OD1 ? A ASP 258 ? A ASP 258 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 OD2 ? A ASP 258 ? A ASP 258 ? 1_555 59.5  ? 
27 OD1 ? A ASP 258 ? A ASP 258 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 NE2 ? C HIS 231 ? C HIS 231 ? 1_555 52.7  ? 
28 OD2 ? A ASP 258 ? A ASP 258 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 NE2 ? C HIS 231 ? C HIS 231 ? 1_555 111.6 ? 
29 OD1 ? A ASP 258 ? A ASP 258 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 OE1 ? C GLU 351 ? C GLU 351 ? 1_555 52.7  ? 
30 OD2 ? A ASP 258 ? A ASP 258 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 OE1 ? C GLU 351 ? C GLU 351 ? 1_555 111.9 ? 
31 NE2 ? C HIS 231 ? C HIS 231 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 OE1 ? C GLU 351 ? C GLU 351 ? 1_555 2.1   ? 
32 OD1 ? A ASP 258 ? A ASP 258 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 O   ? W HOH .   ? C HOH 502 ? 1_555 52.0  ? 
33 OD2 ? A ASP 258 ? A ASP 258 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 O   ? W HOH .   ? C HOH 502 ? 1_555 110.5 ? 
34 NE2 ? C HIS 231 ? C HIS 231 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 O   ? W HOH .   ? C HOH 502 ? 1_555 2.4   ? 
35 OE1 ? C GLU 351 ? C GLU 351 ? 1_555 ZN ? Q ZN . ? C ZN 402 ? 2_546 O   ? W HOH .   ? C HOH 502 ? 1_555 4.5   ? 
36 OE2 ? A GLU 351 ? A GLU 351 ? 1_555 ZN ? G ZN . ? A ZN 404 ? 1_555 O   ? H ACT .   ? A ACT 405 ? 1_555 112.7 ? 
37 OE2 ? A GLU 351 ? A GLU 351 ? 1_555 ZN ? G ZN . ? A ZN 404 ? 1_555 O   ? U HOH .   ? A HOH 590 ? 1_555 118.1 ? 
38 O   ? H ACT .   ? A ACT 405 ? 1_555 ZN ? G ZN . ? A ZN 404 ? 1_555 O   ? U HOH .   ? A HOH 590 ? 1_555 105.8 ? 
39 OE2 ? A GLU 351 ? A GLU 351 ? 1_555 ZN ? G ZN . ? A ZN 404 ? 1_555 NZ  ? B LYS 236 ? B LYS 236 ? 1_555 67.6  ? 
40 O   ? H ACT .   ? A ACT 405 ? 1_555 ZN ? G ZN . ? A ZN 404 ? 1_555 NZ  ? B LYS 236 ? B LYS 236 ? 1_555 58.7  ? 
41 O   ? U HOH .   ? A HOH 590 ? 1_555 ZN ? G ZN . ? A ZN 404 ? 1_555 NZ  ? B LYS 236 ? B LYS 236 ? 1_555 96.4  ? 
42 NE2 ? B HIS 231 ? B HIS 231 ? 1_555 ZN ? M ZN . ? B ZN 402 ? 1_555 O   ? W HOH .   ? C HOH 579 ? 1_555 121.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 6 ? 
AA8 ? 2 ? 
AA9 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 274 ? ASN A 275 ? SER A 274 ASN A 275 
AA1 2 ASN A 268 ? SER A 271 ? ASN A 268 SER A 271 
AA1 3 ASP A 182 ? TRP A 187 ? ASP A 182 TRP A 187 
AA1 4 SER A 204 ? CYS A 213 ? SER A 204 CYS A 213 
AA1 5 GLN A 216 ? VAL A 225 ? GLN A 216 VAL A 225 
AA1 6 PHE A 357 ? ILE A 362 ? PHE A 357 ILE A 362 
AA2 1 ILE A 232 ? ASN A 234 ? ILE A 232 ASN A 234 
AA2 2 GLU A 348 ? GLU A 351 ? GLU A 348 GLU A 351 
AA3 1 SER A 243 ? PHE A 250 ? SER A 243 PHE A 250 
AA3 2 TYR A 335 ? SER A 342 ? TYR A 335 SER A 342 
AA3 3 PRO A 320 ? PHE A 327 ? PRO A 320 PHE A 327 
AA3 4 ILE A 306 ? TYR A 312 ? ILE A 306 TYR A 312 
AA4 1 ASN B 268 ? PHE B 269 ? ASN B 268 PHE B 269 
AA4 2 THR B 185 ? TRP B 187 ? THR B 185 TRP B 187 
AA4 3 SER B 204 ? CYS B 213 ? SER B 204 CYS B 213 
AA4 4 GLN B 216 ? VAL B 225 ? GLN B 216 VAL B 225 
AA4 5 PHE B 357 ? ILE B 362 ? PHE B 357 ILE B 362 
AA5 1 ILE B 232 ? ASN B 234 ? ILE B 232 ASN B 234 
AA5 2 GLU B 348 ? GLU B 351 ? GLU B 348 GLU B 351 
AA6 1 SER B 243 ? PHE B 250 ? SER B 243 PHE B 250 
AA6 2 TYR B 335 ? SER B 342 ? TYR B 335 SER B 342 
AA6 3 PRO B 320 ? PHE B 327 ? PRO B 320 PHE B 327 
AA6 4 ILE B 306 ? TYR B 312 ? ILE B 306 TYR B 312 
AA7 1 SER C 274 ? ASN C 275 ? SER C 274 ASN C 275 
AA7 2 ASN C 268 ? SER C 271 ? ASN C 268 SER C 271 
AA7 3 ASP C 182 ? TRP C 187 ? ASP C 182 TRP C 187 
AA7 4 SER C 204 ? CYS C 213 ? SER C 204 CYS C 213 
AA7 5 GLN C 216 ? VAL C 225 ? GLN C 216 VAL C 225 
AA7 6 PHE C 357 ? ILE C 362 ? PHE C 357 ILE C 362 
AA8 1 ILE C 232 ? ASN C 234 ? ILE C 232 ASN C 234 
AA8 2 GLU C 348 ? GLU C 351 ? GLU C 348 GLU C 351 
AA9 1 SER C 243 ? PHE C 250 ? SER C 243 PHE C 250 
AA9 2 TYR C 335 ? SER C 342 ? TYR C 335 SER C 342 
AA9 3 PRO C 320 ? PHE C 327 ? PRO C 320 PHE C 327 
AA9 4 ILE C 306 ? TYR C 312 ? ILE C 306 TYR C 312 
# 
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 SER A 274 ? O SER A 274 N SER A 271 ? N SER A 271 
AA1 2 3 O ASN A 268 ? O ASN A 268 N TRP A 187 ? N TRP A 187 
AA1 3 4 N LEU A 186 ? N LEU A 186 O LEU A 210 ? O LEU A 210 
AA1 4 5 N LYS A 205 ? N LYS A 205 O ILE A 224 ? O ILE A 224 
AA1 5 6 N ALA A 219 ? N ALA A 219 O PHE A 359 ? O PHE A 359 
AA2 1 2 N ILE A 233 ? N ILE A 233 O VAL A 350 ? O VAL A 350 
AA3 1 2 N ILE A 246 ? N ILE A 246 O PHE A 339 ? O PHE A 339 
AA3 2 3 O ASN A 340 ? O ASN A 340 N LYS A 324 ? N LYS A 324 
AA3 3 4 O THR A 325 ? O THR A 325 N VAL A 307 ? N VAL A 307 
AA4 1 2 O ASN B 268 ? O ASN B 268 N TRP B 187 ? N TRP B 187 
AA4 2 3 N LEU B 186 ? N LEU B 186 O LEU B 210 ? O LEU B 210 
AA4 3 4 N LYS B 205 ? N LYS B 205 O ILE B 224 ? O ILE B 224 
AA4 4 5 N ALA B 219 ? N ALA B 219 O PHE B 359 ? O PHE B 359 
AA5 1 2 N ILE B 233 ? N ILE B 233 O VAL B 350 ? O VAL B 350 
AA6 1 2 N ILE B 246 ? N ILE B 246 O PHE B 339 ? O PHE B 339 
AA6 2 3 O ASN B 340 ? O ASN B 340 N LYS B 324 ? N LYS B 324 
AA6 3 4 O THR B 325 ? O THR B 325 N VAL B 307 ? N VAL B 307 
AA7 1 2 O SER C 274 ? O SER C 274 N SER C 271 ? N SER C 271 
AA7 2 3 O ASN C 268 ? O ASN C 268 N TRP C 187 ? N TRP C 187 
AA7 3 4 N ARG C 184 ? N ARG C 184 O LYS C 212 ? O LYS C 212 
AA7 4 5 N LYS C 205 ? N LYS C 205 O ILE C 224 ? O ILE C 224 
AA7 5 6 N ALA C 219 ? N ALA C 219 O PHE C 359 ? O PHE C 359 
AA8 1 2 N ILE C 233 ? N ILE C 233 O VAL C 350 ? O VAL C 350 
AA9 1 2 N ILE C 246 ? N ILE C 246 O PHE C 339 ? O PHE C 339 
AA9 2 3 O SER C 342 ? O SER C 342 N VAL C 322 ? N VAL C 322 
AA9 3 4 O THR C 325 ? O THR C 325 N VAL C 307 ? N VAL C 307 
# 
_pdbx_entry_details.entry_id                   9FAH 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    569 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    576 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.95 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     590 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     556 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_545 
_pdbx_validate_symm_contact.dist              2.03 
# 
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 THR A 189 ? ? 67.75   155.74  
2  1 CYS A 213 ? ? -110.10 70.06   
3  1 SER A 274 ? ? -124.41 -155.97 
4  1 ALA A 283 ? ? -150.49 41.07   
5  1 ASP B 191 ? ? -78.79  -162.97 
6  1 ILE B 198 ? ? -99.53  -62.49  
7  1 CYS B 213 ? ? -110.09 74.26   
8  1 ALA B 283 ? ? -159.44 52.43   
9  1 ASN C 181 ? ? -154.02 80.19   
10 1 THR C 189 ? ? 68.51   159.93  
11 1 CYS C 213 ? ? -110.77 74.58   
12 1 SER C 274 ? ? -124.60 -158.49 
13 1 ALA C 283 ? ? -147.27 40.26   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 -3.67471963417 -10.3057996084 19.5790499211 0.215870173284 ? -0.0151165036113  ? -0.0165803789588 
? 0.193173390514 ? -0.00607906104602  ? 0.215038841364 ? 0.378358577824  ? 0.51925840009    ? -0.267850530942  ? 0.941397557982 ? 
-0.248538712853  ? 0.946668171681  ? -0.0487708806405  ? 0.140321338948   ? -0.105864028107   ? -0.0165166927773 ? 0.041474424684 
? 0.0672735281398  ? 0.369578134335   ? -0.0610545866233  ? -0.0114679347959   ? 
2  'X-RAY DIFFRACTION' ? refined -10.133994904  -4.42284104514 25.6048013373 0.205193075547 ? 0.000187267869527 ? 0.0242500381816 
? 0.24840906726  ? 0.0602935592113    ? 0.281276027866 ? 0.6088819286    ? 0.108820455203   ? -0.56709044329   ? 0.524893335419 ? 
0.0428638886623  ? 0.317299353087  ? 0.0740649509945   ? 0.248738571017   ? 0.109367129115    ? 0.343794291242   ? 
-0.0233643331435  ? 0.343733472009   ? -0.0814800401026 ? -0.139606669393   ? 0.0121389109773    ? 
3  'X-RAY DIFFRACTION' ? refined 1.82750090096  -16.4651819285 30.1760915087 0.33778357414  ? 0.0172065855424   ? 0.0185393156706 
? 0.190846176835 ? 0.0400134132518    ? 0.28220087927  ? 0.753690721418  ? 0.152880678441   ? -0.408625843862  ? 0.234319965792 ? 
-0.0428177527309 ? 0.177708056428  ? -0.135589057807   ? -0.150303640544  ? -0.276989653844   ? -0.0344301932934 ? 0.0509686788768 
? -0.077521613314  ? 0.0920484167618  ? 0.0789555949169   ? 0.00010987766503   ? 
4  'X-RAY DIFFRACTION' ? refined -2.60334145844 2.97151743943  24.3363708326 0.201285902551 ? 0.0220730243329   ? 0.0240886513642 
? 0.164914191119 ? 0.0149972487486    ? 0.198892971361 ? 0.919015520124  ? 0.220721463524   ? -0.0395064425862 ? 1.00213438306  ? 
-0.0103027679807 ? 0.24012537444   ? 0.0360461716952   ? -0.0266211324522 ? 0.104908792824    ? 0.146788531469   ? 0.0807939971465 
? 0.211399511917   ? -0.11585144419   ? -0.0512220275728  ? 0.000139558420828  ? 
5  'X-RAY DIFFRACTION' ? refined -7.92479127248 -2.56715684684 7.80819296695 0.188610703644 ? -0.0933468185044  ? -0.0772744880905 
? 0.332523446715 ? 0.0921007547364    ? 0.198702454999 ? 0.0609733588611 ? 0.143453465457   ? 0.116290552286   ? 0.294620593914 ? 
0.274165930093   ? 0.467348023695  ? -0.119695641535   ? 0.471431508325   ? 0.0102940540122   ? -0.320962082357  ? 0.180453897746 
? 0.0479732336453  ? 0.358435975952   ? -0.316564522539   ? -0.0843575275323   ? 
6  'X-RAY DIFFRACTION' ? refined 7.43054933644  -3.85117945396 28.7275599292 0.224018476482 ? 0.0219037282205   ? -0.0186311051327 
? 0.199713947873 ? -0.00632638950122  ? 0.207242532032 ? 0.184307735898  ? 0.0667587818291  ? 0.00205112534348 ? 0.130515914076 ? 
0.0527589623863  ? 0.0339908973821 ? 0.14041363927     ? -0.128367559003  ? -0.0715857674937  ? 0.104498216888   ? 
-0.0307153441348  ? 0.215675811149   ? 0.247014572787   ? -0.00252951738741 ? 0.00080635618016   ? 
7  'X-RAY DIFFRACTION' ? refined 26.7035822254  -4.49637200252 4.03343090517 0.288049136649 ? 0.154077584072    ? 0.051800878177 ? 
0.528878887006 ? -0.000272259644179 ? 0.336171158866 ? 0.270881178484  ? 0.165806039159   ? 0.373224475768   ? 0.327247512716 ? 
0.166386851879   ? 0.968518290268  ? -0.348427519588   ? 0.172223216716   ? -0.110667867095   ? -0.133335105711  ? 0.217625311107 
? -0.460034781644  ? -0.0719272095623 ? 0.885946327067    ? 0.0423373503877    ? 
8  'X-RAY DIFFRACTION' ? refined 18.4106784029  -3.30322917565 2.22342140081 0.256166645055 ? 0.0553257188047   ? 0.0248497366454 
? 0.270681237733 ? 0.00521259077447   ? 0.205633834176 ? 1.05521363444   ? -0.0354826169628 ? -0.244269554721  ? 0.712035892628 ? 
0.659917540097   ? 0.920220046094  ? -0.0552853139461  ? 0.220111628919   ? -0.103009422253   ? -0.175655354686  ? 
-0.0931138053024  ? -0.101686436207  ? 0.14446503299    ? 0.330331107886    ? -0.0225587984136   ? 
9  'X-RAY DIFFRACTION' ? refined 25.3732463626  -14.6071971047 10.0986672752 0.36076364542  ? 0.199657800472    ? 0.069263290494 ? 
0.466268503337 ? 0.00607498530133   ? 0.41530124746  ? 0.113478550001  ? 0.0953235624449  ? -0.0548110510663 ? 0.266884643679 ? 
0.122426892761   ? 0.144453602769  ? -0.0881370834137  ? 0.0184120234088  ? -0.350721282732   ? 0.268048337414   ? 0.0662468897517 
? -0.327686215902  ? 0.350970988002   ? 0.481505471198    ? 0.01249644729      ? 
10 'X-RAY DIFFRACTION' ? refined 10.6598829775  -2.88672485268 5.69637309313 0.246185518638 ? 0.0120553709824   ? 
-0.00963722742481 ? 0.204003987396 ? -0.00345964233754  ? 0.210563879823 ? 0.687129777663  ? 0.313980139829   ? -0.451582489339  ? 
0.35314816864  ? -0.0556098040665 ? 1.11934958562   ? -0.0953304577372  ? 0.210083700369   ? -0.0275846135831  ? -0.14931571034   
? 0.00514545455904  ? 0.00274838227482 ? 0.181477169087   ? 0.0621062000233   ? -0.000691495473959 ? 
11 'X-RAY DIFFRACTION' ? refined 17.6760167343  2.88195758158  37.3866519572 0.293726837517 ? 0.0503486184675   ? -0.046692050568 
? 0.384138638452 ? -0.0330425475737   ? 0.259464046551 ? 0.207809653632  ? 0.0937450520207  ? -0.109194667882  ? 0.193169756023 ? 
0.0435275072372  ? 0.0858111421603 ? -0.0415292429541  ? -0.462323498395  ? -0.0544852274673  ? 0.366530338807   ? 
-0.0342153001939  ? 0.226690869815   ? 0.177149916499   ? 0.334320670167    ? 0.000829417914015  ? 
12 'X-RAY DIFFRACTION' ? refined 17.3638282085  14.4400776714  29.9073042431 0.215889107281 ? -0.034851295593   ? -0.0212364784775 
? 0.22779727     ? -0.0478715078443   ? 0.215288833726 ? 1.30557148037   ? 0.0208499085552  ? -0.435468240882  ? 0.385476371923 ? 
-0.28645871477   ? 1.42616088047   ? 0.0824236166252   ? -0.186018349856  ? 0.130486979182    ? 0.226352583735   ? 
-0.00231656767676 ? -0.131164394027  ? -0.218255487547  ? 0.333130165073    ? 0.000759301608836  ? 
13 'X-RAY DIFFRACTION' ? refined 23.6886591095  1.69420276005  39.5715340214 0.394713970814 ? 0.0554426723372   ? -0.0903526995905 
? 0.587210841407 ? -0.00956714149169  ? 0.335661326152 ? 0.136900710111  ? 0.0674858663978  ? -0.0176733392199 ? 0.103660130718 ? 
0.00153943702038 ? 0.161513660058  ? -0.0644776878473  ? -0.550348961803  ? -0.126452796391   ? 0.373364074238   ? 0.0694702350149 
? -0.188090729035  ? 0.0444132438431  ? 0.185455395882    ? -2.07806105175e-05 ? 
14 'X-RAY DIFFRACTION' ? refined 23.6047878758  8.34017516268  17.1025454788 0.122516633436 ? 0.0168247341837   ? 
-0.00154911953823 ? 0.313411977924 ? 0.029313619861     ? 0.223093322496 ? 0.343072494517  ? 0.264161747482   ? 0.457349780102   ? 
0.30378544119  ? 0.349375310432   ? 0.491705021275  ? -0.0812759119695  ? 0.0683377240462  ? 0.0489876531794   ? 0.0742784688955  
? 0.110107964692    ? -0.0629596074334 ? -0.0976500136489 ? 0.326316350397    ? 0.004254697699     ? 
15 'X-RAY DIFFRACTION' ? refined 16.011511652   14.9171782937  21.6158467875 0.200033494417 ? -0.00754897945716 ? 0.00125932378693 
? 0.222444799636 ? 0.0163378940609    ? 0.267699418018 ? 0.0316416796879 ? -0.257045010782  ? -0.199545126942  ? 0.677398378412 ? 
0.00899908172886 ? 0.843160529834  ? 0.0652001411286   ? 0.0921693462425  ? 0.109082766309    ? 0.0879809738024  ? 
-0.0231465485063  ? -0.143987224544  ? -0.241786005669  ? 0.210795256779    ? -2.79870662944e-05 ? 
16 'X-RAY DIFFRACTION' ? refined 12.9310257785  9.15402035695  25.1561920745 0.200791485017 ? 0.0117132362797   ? 0.007905325887 ? 
0.196106888115 ? -0.00897617899624  ? 0.213877345878 ? 0.119156827967  ? 0.223420738447   ? 0.105855943362   ? 0.281591081449 ? 
-0.0396198796131 ? 0.814617621325  ? -0.00475487910161 ? -0.0749838488257 ? -0.00954774762338 ? 0.138350293326   ? 
0.00601948455242  ? 0.0837725868498  ? -0.147228006077  ? 0.238153602427    ? 0.00187343561337   ? 
# 
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 182 through 234 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 235 through 263 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 264 through 291 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 292 through 347 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 348 through 356 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 357 through 365 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 183 through 203 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 204 through 263 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 264 through 286 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 287 through 365 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 180 through 197 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 198 through 263 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 264 through 283 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 284 through 315 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 316 through 347 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 348 through 365 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A SER 2   ? A SER 2   
3   1 Y 1 A LYS 3   ? A LYS 3   
4   1 Y 1 A ARG 4   ? A ARG 4   
5   1 Y 1 A LEU 5   ? A LEU 5   
6   1 Y 1 A ARG 6   ? A ARG 6   
7   1 Y 1 A VAL 7   ? A VAL 7   
8   1 Y 1 A GLU 8   ? A GLU 8   
9   1 Y 1 A ASP 9   ? A ASP 9   
10  1 Y 1 A ASP 10  ? A ASP 10  
11  1 Y 1 A PHE 11  ? A PHE 11  
12  1 Y 1 A ASN 12  ? A ASN 12  
13  1 Y 1 A PRO 13  ? A PRO 13  
14  1 Y 1 A VAL 14  ? A VAL 14  
15  1 Y 1 A TYR 15  ? A TYR 15  
16  1 Y 1 A PRO 16  ? A PRO 16  
17  1 Y 1 A TYR 17  ? A TYR 17  
18  1 Y 1 A GLY 18  ? A GLY 18  
19  1 Y 1 A TYR 19  ? A TYR 19  
20  1 Y 1 A ALA 20  ? A ALA 20  
21  1 Y 1 A ARG 21  ? A ARG 21  
22  1 Y 1 A ASN 22  ? A ASN 22  
23  1 Y 1 A GLN 23  ? A GLN 23  
24  1 Y 1 A ASN 24  ? A ASN 24  
25  1 Y 1 A ILE 25  ? A ILE 25  
26  1 Y 1 A PRO 26  ? A PRO 26  
27  1 Y 1 A PHE 27  ? A PHE 27  
28  1 Y 1 A LEU 28  ? A LEU 28  
29  1 Y 1 A THR 29  ? A THR 29  
30  1 Y 1 A PRO 30  ? A PRO 30  
31  1 Y 1 A PRO 31  ? A PRO 31  
32  1 Y 1 A PHE 32  ? A PHE 32  
33  1 Y 1 A VAL 33  ? A VAL 33  
34  1 Y 1 A SER 34  ? A SER 34  
35  1 Y 1 A SER 35  ? A SER 35  
36  1 Y 1 A ASP 36  ? A ASP 36  
37  1 Y 1 A GLY 37  ? A GLY 37  
38  1 Y 1 A PHE 38  ? A PHE 38  
39  1 Y 1 A LYS 39  ? A LYS 39  
40  1 Y 1 A ASN 40  ? A ASN 40  
41  1 Y 1 A PHE 41  ? A PHE 41  
42  1 Y 1 A PRO 42  ? A PRO 42  
43  1 Y 1 A PRO 43  ? A PRO 43  
44  1 Y 1 A GLY 44  ? A GLY 44  
45  1 Y 1 A VAL 45  ? A VAL 45  
46  1 Y 1 A LEU 46  ? A LEU 46  
47  1 Y 1 A SER 47  ? A SER 47  
48  1 Y 1 A LEU 48  ? A LEU 48  
49  1 Y 1 A LYS 49  ? A LYS 49  
50  1 Y 1 A LEU 50  ? A LEU 50  
51  1 Y 1 A ALA 51  ? A ALA 51  
52  1 Y 1 A ASP 52  ? A ASP 52  
53  1 Y 1 A PRO 53  ? A PRO 53  
54  1 Y 1 A ILE 54  ? A ILE 54  
55  1 Y 1 A THR 55  ? A THR 55  
56  1 Y 1 A ILE 56  ? A ILE 56  
57  1 Y 1 A THR 57  ? A THR 57  
58  1 Y 1 A ASN 58  ? A ASN 58  
59  1 Y 1 A GLY 59  ? A GLY 59  
60  1 Y 1 A ASP 60  ? A ASP 60  
61  1 Y 1 A VAL 61  ? A VAL 61  
62  1 Y 1 A SER 62  ? A SER 62  
63  1 Y 1 A LEU 63  ? A LEU 63  
64  1 Y 1 A LYS 64  ? A LYS 64  
65  1 Y 1 A VAL 65  ? A VAL 65  
66  1 Y 1 A GLY 66  ? A GLY 66  
67  1 Y 1 A GLY 67  ? A GLY 67  
68  1 Y 1 A GLY 68  ? A GLY 68  
69  1 Y 1 A LEU 69  ? A LEU 69  
70  1 Y 1 A THR 70  ? A THR 70  
71  1 Y 1 A LEU 71  ? A LEU 71  
72  1 Y 1 A GLN 72  ? A GLN 72  
73  1 Y 1 A ASP 73  ? A ASP 73  
74  1 Y 1 A GLY 74  ? A GLY 74  
75  1 Y 1 A SER 75  ? A SER 75  
76  1 Y 1 A LEU 76  ? A LEU 76  
77  1 Y 1 A THR 77  ? A THR 77  
78  1 Y 1 A VAL 78  ? A VAL 78  
79  1 Y 1 A ASN 79  ? A ASN 79  
80  1 Y 1 A PRO 80  ? A PRO 80  
81  1 Y 1 A LYS 81  ? A LYS 81  
82  1 Y 1 A ALA 82  ? A ALA 82  
83  1 Y 1 A PRO 83  ? A PRO 83  
84  1 Y 1 A LEU 84  ? A LEU 84  
85  1 Y 1 A GLN 85  ? A GLN 85  
86  1 Y 1 A VAL 86  ? A VAL 86  
87  1 Y 1 A ASN 87  ? A ASN 87  
88  1 Y 1 A THR 88  ? A THR 88  
89  1 Y 1 A ASP 89  ? A ASP 89  
90  1 Y 1 A LYS 90  ? A LYS 90  
91  1 Y 1 A LYS 91  ? A LYS 91  
92  1 Y 1 A LEU 92  ? A LEU 92  
93  1 Y 1 A GLU 93  ? A GLU 93  
94  1 Y 1 A LEU 94  ? A LEU 94  
95  1 Y 1 A ALA 95  ? A ALA 95  
96  1 Y 1 A TYR 96  ? A TYR 96  
97  1 Y 1 A ASP 97  ? A ASP 97  
98  1 Y 1 A ASN 98  ? A ASN 98  
99  1 Y 1 A PRO 99  ? A PRO 99  
100 1 Y 1 A PHE 100 ? A PHE 100 
101 1 Y 1 A GLU 101 ? A GLU 101 
102 1 Y 1 A SER 102 ? A SER 102 
103 1 Y 1 A SER 103 ? A SER 103 
104 1 Y 1 A ALA 104 ? A ALA 104 
105 1 Y 1 A ASN 105 ? A ASN 105 
106 1 Y 1 A LYS 106 ? A LYS 106 
107 1 Y 1 A LEU 107 ? A LEU 107 
108 1 Y 1 A SER 108 ? A SER 108 
109 1 Y 1 A LEU 109 ? A LEU 109 
110 1 Y 1 A LYS 110 ? A LYS 110 
111 1 Y 1 A VAL 111 ? A VAL 111 
112 1 Y 1 A GLY 112 ? A GLY 112 
113 1 Y 1 A HIS 113 ? A HIS 113 
114 1 Y 1 A GLY 114 ? A GLY 114 
115 1 Y 1 A LEU 115 ? A LEU 115 
116 1 Y 1 A LYS 116 ? A LYS 116 
117 1 Y 1 A VAL 117 ? A VAL 117 
118 1 Y 1 A LEU 118 ? A LEU 118 
119 1 Y 1 A ASP 119 ? A ASP 119 
120 1 Y 1 A GLU 120 ? A GLU 120 
121 1 Y 1 A LYS 121 ? A LYS 121 
122 1 Y 1 A SER 122 ? A SER 122 
123 1 Y 1 A ALA 123 ? A ALA 123 
124 1 Y 1 A ALA 124 ? A ALA 124 
125 1 Y 1 A GLY 125 ? A GLY 125 
126 1 Y 1 A LEU 126 ? A LEU 126 
127 1 Y 1 A LYS 127 ? A LYS 127 
128 1 Y 1 A ASP 128 ? A ASP 128 
129 1 Y 1 A LEU 129 ? A LEU 129 
130 1 Y 1 A ILE 130 ? A ILE 130 
131 1 Y 1 A GLY 131 ? A GLY 131 
132 1 Y 1 A LYS 132 ? A LYS 132 
133 1 Y 1 A LEU 133 ? A LEU 133 
134 1 Y 1 A VAL 134 ? A VAL 134 
135 1 Y 1 A VAL 135 ? A VAL 135 
136 1 Y 1 A LEU 136 ? A LEU 136 
137 1 Y 1 A THR 137 ? A THR 137 
138 1 Y 1 A GLY 138 ? A GLY 138 
139 1 Y 1 A LYS 139 ? A LYS 139 
140 1 Y 1 A GLY 140 ? A GLY 140 
141 1 Y 1 A ILE 141 ? A ILE 141 
142 1 Y 1 A GLY 142 ? A GLY 142 
143 1 Y 1 A THR 143 ? A THR 143 
144 1 Y 1 A GLU 144 ? A GLU 144 
145 1 Y 1 A ASN 145 ? A ASN 145 
146 1 Y 1 A LEU 146 ? A LEU 146 
147 1 Y 1 A GLU 147 ? A GLU 147 
148 1 Y 1 A ASN 148 ? A ASN 148 
149 1 Y 1 A THR 149 ? A THR 149 
150 1 Y 1 A ASP 150 ? A ASP 150 
151 1 Y 1 A GLY 151 ? A GLY 151 
152 1 Y 1 A SER 152 ? A SER 152 
153 1 Y 1 A SER 153 ? A SER 153 
154 1 Y 1 A ARG 154 ? A ARG 154 
155 1 Y 1 A GLY 155 ? A GLY 155 
156 1 Y 1 A ILE 156 ? A ILE 156 
157 1 Y 1 A GLY 157 ? A GLY 157 
158 1 Y 1 A ILE 158 ? A ILE 158 
159 1 Y 1 A ASN 159 ? A ASN 159 
160 1 Y 1 A VAL 160 ? A VAL 160 
161 1 Y 1 A ARG 161 ? A ARG 161 
162 1 Y 1 A ALA 162 ? A ALA 162 
163 1 Y 1 A ARG 163 ? A ARG 163 
164 1 Y 1 A GLU 164 ? A GLU 164 
165 1 Y 1 A GLY 165 ? A GLY 165 
166 1 Y 1 A LEU 166 ? A LEU 166 
167 1 Y 1 A THR 167 ? A THR 167 
168 1 Y 1 A PHE 168 ? A PHE 168 
169 1 Y 1 A ASP 169 ? A ASP 169 
170 1 Y 1 A ASN 170 ? A ASN 170 
171 1 Y 1 A ASP 171 ? A ASP 171 
172 1 Y 1 A GLY 172 ? A GLY 172 
173 1 Y 1 A TYR 173 ? A TYR 173 
174 1 Y 1 A LEU 174 ? A LEU 174 
175 1 Y 1 A VAL 175 ? A VAL 175 
176 1 Y 1 A ALA 176 ? A ALA 176 
177 1 Y 1 A TRP 177 ? A TRP 177 
178 1 Y 1 A ASN 178 ? A ASN 178 
179 1 Y 1 A PRO 179 ? A PRO 179 
180 1 Y 1 A LYS 180 ? A LYS 180 
181 1 Y 1 B MET 1   ? B MET 1   
182 1 Y 1 B SER 2   ? B SER 2   
183 1 Y 1 B LYS 3   ? B LYS 3   
184 1 Y 1 B ARG 4   ? B ARG 4   
185 1 Y 1 B LEU 5   ? B LEU 5   
186 1 Y 1 B ARG 6   ? B ARG 6   
187 1 Y 1 B VAL 7   ? B VAL 7   
188 1 Y 1 B GLU 8   ? B GLU 8   
189 1 Y 1 B ASP 9   ? B ASP 9   
190 1 Y 1 B ASP 10  ? B ASP 10  
191 1 Y 1 B PHE 11  ? B PHE 11  
192 1 Y 1 B ASN 12  ? B ASN 12  
193 1 Y 1 B PRO 13  ? B PRO 13  
194 1 Y 1 B VAL 14  ? B VAL 14  
195 1 Y 1 B TYR 15  ? B TYR 15  
196 1 Y 1 B PRO 16  ? B PRO 16  
197 1 Y 1 B TYR 17  ? B TYR 17  
198 1 Y 1 B GLY 18  ? B GLY 18  
199 1 Y 1 B TYR 19  ? B TYR 19  
200 1 Y 1 B ALA 20  ? B ALA 20  
201 1 Y 1 B ARG 21  ? B ARG 21  
202 1 Y 1 B ASN 22  ? B ASN 22  
203 1 Y 1 B GLN 23  ? B GLN 23  
204 1 Y 1 B ASN 24  ? B ASN 24  
205 1 Y 1 B ILE 25  ? B ILE 25  
206 1 Y 1 B PRO 26  ? B PRO 26  
207 1 Y 1 B PHE 27  ? B PHE 27  
208 1 Y 1 B LEU 28  ? B LEU 28  
209 1 Y 1 B THR 29  ? B THR 29  
210 1 Y 1 B PRO 30  ? B PRO 30  
211 1 Y 1 B PRO 31  ? B PRO 31  
212 1 Y 1 B PHE 32  ? B PHE 32  
213 1 Y 1 B VAL 33  ? B VAL 33  
214 1 Y 1 B SER 34  ? B SER 34  
215 1 Y 1 B SER 35  ? B SER 35  
216 1 Y 1 B ASP 36  ? B ASP 36  
217 1 Y 1 B GLY 37  ? B GLY 37  
218 1 Y 1 B PHE 38  ? B PHE 38  
219 1 Y 1 B LYS 39  ? B LYS 39  
220 1 Y 1 B ASN 40  ? B ASN 40  
221 1 Y 1 B PHE 41  ? B PHE 41  
222 1 Y 1 B PRO 42  ? B PRO 42  
223 1 Y 1 B PRO 43  ? B PRO 43  
224 1 Y 1 B GLY 44  ? B GLY 44  
225 1 Y 1 B VAL 45  ? B VAL 45  
226 1 Y 1 B LEU 46  ? B LEU 46  
227 1 Y 1 B SER 47  ? B SER 47  
228 1 Y 1 B LEU 48  ? B LEU 48  
229 1 Y 1 B LYS 49  ? B LYS 49  
230 1 Y 1 B LEU 50  ? B LEU 50  
231 1 Y 1 B ALA 51  ? B ALA 51  
232 1 Y 1 B ASP 52  ? B ASP 52  
233 1 Y 1 B PRO 53  ? B PRO 53  
234 1 Y 1 B ILE 54  ? B ILE 54  
235 1 Y 1 B THR 55  ? B THR 55  
236 1 Y 1 B ILE 56  ? B ILE 56  
237 1 Y 1 B THR 57  ? B THR 57  
238 1 Y 1 B ASN 58  ? B ASN 58  
239 1 Y 1 B GLY 59  ? B GLY 59  
240 1 Y 1 B ASP 60  ? B ASP 60  
241 1 Y 1 B VAL 61  ? B VAL 61  
242 1 Y 1 B SER 62  ? B SER 62  
243 1 Y 1 B LEU 63  ? B LEU 63  
244 1 Y 1 B LYS 64  ? B LYS 64  
245 1 Y 1 B VAL 65  ? B VAL 65  
246 1 Y 1 B GLY 66  ? B GLY 66  
247 1 Y 1 B GLY 67  ? B GLY 67  
248 1 Y 1 B GLY 68  ? B GLY 68  
249 1 Y 1 B LEU 69  ? B LEU 69  
250 1 Y 1 B THR 70  ? B THR 70  
251 1 Y 1 B LEU 71  ? B LEU 71  
252 1 Y 1 B GLN 72  ? B GLN 72  
253 1 Y 1 B ASP 73  ? B ASP 73  
254 1 Y 1 B GLY 74  ? B GLY 74  
255 1 Y 1 B SER 75  ? B SER 75  
256 1 Y 1 B LEU 76  ? B LEU 76  
257 1 Y 1 B THR 77  ? B THR 77  
258 1 Y 1 B VAL 78  ? B VAL 78  
259 1 Y 1 B ASN 79  ? B ASN 79  
260 1 Y 1 B PRO 80  ? B PRO 80  
261 1 Y 1 B LYS 81  ? B LYS 81  
262 1 Y 1 B ALA 82  ? B ALA 82  
263 1 Y 1 B PRO 83  ? B PRO 83  
264 1 Y 1 B LEU 84  ? B LEU 84  
265 1 Y 1 B GLN 85  ? B GLN 85  
266 1 Y 1 B VAL 86  ? B VAL 86  
267 1 Y 1 B ASN 87  ? B ASN 87  
268 1 Y 1 B THR 88  ? B THR 88  
269 1 Y 1 B ASP 89  ? B ASP 89  
270 1 Y 1 B LYS 90  ? B LYS 90  
271 1 Y 1 B LYS 91  ? B LYS 91  
272 1 Y 1 B LEU 92  ? B LEU 92  
273 1 Y 1 B GLU 93  ? B GLU 93  
274 1 Y 1 B LEU 94  ? B LEU 94  
275 1 Y 1 B ALA 95  ? B ALA 95  
276 1 Y 1 B TYR 96  ? B TYR 96  
277 1 Y 1 B ASP 97  ? B ASP 97  
278 1 Y 1 B ASN 98  ? B ASN 98  
279 1 Y 1 B PRO 99  ? B PRO 99  
280 1 Y 1 B PHE 100 ? B PHE 100 
281 1 Y 1 B GLU 101 ? B GLU 101 
282 1 Y 1 B SER 102 ? B SER 102 
283 1 Y 1 B SER 103 ? B SER 103 
284 1 Y 1 B ALA 104 ? B ALA 104 
285 1 Y 1 B ASN 105 ? B ASN 105 
286 1 Y 1 B LYS 106 ? B LYS 106 
287 1 Y 1 B LEU 107 ? B LEU 107 
288 1 Y 1 B SER 108 ? B SER 108 
289 1 Y 1 B LEU 109 ? B LEU 109 
290 1 Y 1 B LYS 110 ? B LYS 110 
291 1 Y 1 B VAL 111 ? B VAL 111 
292 1 Y 1 B GLY 112 ? B GLY 112 
293 1 Y 1 B HIS 113 ? B HIS 113 
294 1 Y 1 B GLY 114 ? B GLY 114 
295 1 Y 1 B LEU 115 ? B LEU 115 
296 1 Y 1 B LYS 116 ? B LYS 116 
297 1 Y 1 B VAL 117 ? B VAL 117 
298 1 Y 1 B LEU 118 ? B LEU 118 
299 1 Y 1 B ASP 119 ? B ASP 119 
300 1 Y 1 B GLU 120 ? B GLU 120 
301 1 Y 1 B LYS 121 ? B LYS 121 
302 1 Y 1 B SER 122 ? B SER 122 
303 1 Y 1 B ALA 123 ? B ALA 123 
304 1 Y 1 B ALA 124 ? B ALA 124 
305 1 Y 1 B GLY 125 ? B GLY 125 
306 1 Y 1 B LEU 126 ? B LEU 126 
307 1 Y 1 B LYS 127 ? B LYS 127 
308 1 Y 1 B ASP 128 ? B ASP 128 
309 1 Y 1 B LEU 129 ? B LEU 129 
310 1 Y 1 B ILE 130 ? B ILE 130 
311 1 Y 1 B GLY 131 ? B GLY 131 
312 1 Y 1 B LYS 132 ? B LYS 132 
313 1 Y 1 B LEU 133 ? B LEU 133 
314 1 Y 1 B VAL 134 ? B VAL 134 
315 1 Y 1 B VAL 135 ? B VAL 135 
316 1 Y 1 B LEU 136 ? B LEU 136 
317 1 Y 1 B THR 137 ? B THR 137 
318 1 Y 1 B GLY 138 ? B GLY 138 
319 1 Y 1 B LYS 139 ? B LYS 139 
320 1 Y 1 B GLY 140 ? B GLY 140 
321 1 Y 1 B ILE 141 ? B ILE 141 
322 1 Y 1 B GLY 142 ? B GLY 142 
323 1 Y 1 B THR 143 ? B THR 143 
324 1 Y 1 B GLU 144 ? B GLU 144 
325 1 Y 1 B ASN 145 ? B ASN 145 
326 1 Y 1 B LEU 146 ? B LEU 146 
327 1 Y 1 B GLU 147 ? B GLU 147 
328 1 Y 1 B ASN 148 ? B ASN 148 
329 1 Y 1 B THR 149 ? B THR 149 
330 1 Y 1 B ASP 150 ? B ASP 150 
331 1 Y 1 B GLY 151 ? B GLY 151 
332 1 Y 1 B SER 152 ? B SER 152 
333 1 Y 1 B SER 153 ? B SER 153 
334 1 Y 1 B ARG 154 ? B ARG 154 
335 1 Y 1 B GLY 155 ? B GLY 155 
336 1 Y 1 B ILE 156 ? B ILE 156 
337 1 Y 1 B GLY 157 ? B GLY 157 
338 1 Y 1 B ILE 158 ? B ILE 158 
339 1 Y 1 B ASN 159 ? B ASN 159 
340 1 Y 1 B VAL 160 ? B VAL 160 
341 1 Y 1 B ARG 161 ? B ARG 161 
342 1 Y 1 B ALA 162 ? B ALA 162 
343 1 Y 1 B ARG 163 ? B ARG 163 
344 1 Y 1 B GLU 164 ? B GLU 164 
345 1 Y 1 B GLY 165 ? B GLY 165 
346 1 Y 1 B LEU 166 ? B LEU 166 
347 1 Y 1 B THR 167 ? B THR 167 
348 1 Y 1 B PHE 168 ? B PHE 168 
349 1 Y 1 B ASP 169 ? B ASP 169 
350 1 Y 1 B ASN 170 ? B ASN 170 
351 1 Y 1 B ASP 171 ? B ASP 171 
352 1 Y 1 B GLY 172 ? B GLY 172 
353 1 Y 1 B TYR 173 ? B TYR 173 
354 1 Y 1 B LEU 174 ? B LEU 174 
355 1 Y 1 B VAL 175 ? B VAL 175 
356 1 Y 1 B ALA 176 ? B ALA 176 
357 1 Y 1 B TRP 177 ? B TRP 177 
358 1 Y 1 B ASN 178 ? B ASN 178 
359 1 Y 1 B PRO 179 ? B PRO 179 
360 1 Y 1 B LYS 180 ? B LYS 180 
361 1 Y 1 B ASN 181 ? B ASN 181 
362 1 Y 1 B ASP 182 ? B ASP 182 
363 1 Y 1 B GLY 272 ? B GLY 272 
364 1 Y 1 B ASN 273 ? B ASN 273 
365 1 Y 1 B SER 274 ? B SER 274 
366 1 Y 1 B ASN 275 ? B ASN 275 
367 1 Y 1 B VAL 276 ? B VAL 276 
368 1 Y 1 B SER 277 ? B SER 277 
369 1 Y 1 B THR 278 ? B THR 278 
370 1 Y 1 B ALA 279 ? B ALA 279 
371 1 Y 1 B TYR 280 ? B TYR 280 
372 1 Y 1 B ASN 298 ? B ASN 298 
373 1 Y 1 B SER 299 ? B SER 299 
374 1 Y 1 C MET 1   ? C MET 1   
375 1 Y 1 C SER 2   ? C SER 2   
376 1 Y 1 C LYS 3   ? C LYS 3   
377 1 Y 1 C ARG 4   ? C ARG 4   
378 1 Y 1 C LEU 5   ? C LEU 5   
379 1 Y 1 C ARG 6   ? C ARG 6   
380 1 Y 1 C VAL 7   ? C VAL 7   
381 1 Y 1 C GLU 8   ? C GLU 8   
382 1 Y 1 C ASP 9   ? C ASP 9   
383 1 Y 1 C ASP 10  ? C ASP 10  
384 1 Y 1 C PHE 11  ? C PHE 11  
385 1 Y 1 C ASN 12  ? C ASN 12  
386 1 Y 1 C PRO 13  ? C PRO 13  
387 1 Y 1 C VAL 14  ? C VAL 14  
388 1 Y 1 C TYR 15  ? C TYR 15  
389 1 Y 1 C PRO 16  ? C PRO 16  
390 1 Y 1 C TYR 17  ? C TYR 17  
391 1 Y 1 C GLY 18  ? C GLY 18  
392 1 Y 1 C TYR 19  ? C TYR 19  
393 1 Y 1 C ALA 20  ? C ALA 20  
394 1 Y 1 C ARG 21  ? C ARG 21  
395 1 Y 1 C ASN 22  ? C ASN 22  
396 1 Y 1 C GLN 23  ? C GLN 23  
397 1 Y 1 C ASN 24  ? C ASN 24  
398 1 Y 1 C ILE 25  ? C ILE 25  
399 1 Y 1 C PRO 26  ? C PRO 26  
400 1 Y 1 C PHE 27  ? C PHE 27  
401 1 Y 1 C LEU 28  ? C LEU 28  
402 1 Y 1 C THR 29  ? C THR 29  
403 1 Y 1 C PRO 30  ? C PRO 30  
404 1 Y 1 C PRO 31  ? C PRO 31  
405 1 Y 1 C PHE 32  ? C PHE 32  
406 1 Y 1 C VAL 33  ? C VAL 33  
407 1 Y 1 C SER 34  ? C SER 34  
408 1 Y 1 C SER 35  ? C SER 35  
409 1 Y 1 C ASP 36  ? C ASP 36  
410 1 Y 1 C GLY 37  ? C GLY 37  
411 1 Y 1 C PHE 38  ? C PHE 38  
412 1 Y 1 C LYS 39  ? C LYS 39  
413 1 Y 1 C ASN 40  ? C ASN 40  
414 1 Y 1 C PHE 41  ? C PHE 41  
415 1 Y 1 C PRO 42  ? C PRO 42  
416 1 Y 1 C PRO 43  ? C PRO 43  
417 1 Y 1 C GLY 44  ? C GLY 44  
418 1 Y 1 C VAL 45  ? C VAL 45  
419 1 Y 1 C LEU 46  ? C LEU 46  
420 1 Y 1 C SER 47  ? C SER 47  
421 1 Y 1 C LEU 48  ? C LEU 48  
422 1 Y 1 C LYS 49  ? C LYS 49  
423 1 Y 1 C LEU 50  ? C LEU 50  
424 1 Y 1 C ALA 51  ? C ALA 51  
425 1 Y 1 C ASP 52  ? C ASP 52  
426 1 Y 1 C PRO 53  ? C PRO 53  
427 1 Y 1 C ILE 54  ? C ILE 54  
428 1 Y 1 C THR 55  ? C THR 55  
429 1 Y 1 C ILE 56  ? C ILE 56  
430 1 Y 1 C THR 57  ? C THR 57  
431 1 Y 1 C ASN 58  ? C ASN 58  
432 1 Y 1 C GLY 59  ? C GLY 59  
433 1 Y 1 C ASP 60  ? C ASP 60  
434 1 Y 1 C VAL 61  ? C VAL 61  
435 1 Y 1 C SER 62  ? C SER 62  
436 1 Y 1 C LEU 63  ? C LEU 63  
437 1 Y 1 C LYS 64  ? C LYS 64  
438 1 Y 1 C VAL 65  ? C VAL 65  
439 1 Y 1 C GLY 66  ? C GLY 66  
440 1 Y 1 C GLY 67  ? C GLY 67  
441 1 Y 1 C GLY 68  ? C GLY 68  
442 1 Y 1 C LEU 69  ? C LEU 69  
443 1 Y 1 C THR 70  ? C THR 70  
444 1 Y 1 C LEU 71  ? C LEU 71  
445 1 Y 1 C GLN 72  ? C GLN 72  
446 1 Y 1 C ASP 73  ? C ASP 73  
447 1 Y 1 C GLY 74  ? C GLY 74  
448 1 Y 1 C SER 75  ? C SER 75  
449 1 Y 1 C LEU 76  ? C LEU 76  
450 1 Y 1 C THR 77  ? C THR 77  
451 1 Y 1 C VAL 78  ? C VAL 78  
452 1 Y 1 C ASN 79  ? C ASN 79  
453 1 Y 1 C PRO 80  ? C PRO 80  
454 1 Y 1 C LYS 81  ? C LYS 81  
455 1 Y 1 C ALA 82  ? C ALA 82  
456 1 Y 1 C PRO 83  ? C PRO 83  
457 1 Y 1 C LEU 84  ? C LEU 84  
458 1 Y 1 C GLN 85  ? C GLN 85  
459 1 Y 1 C VAL 86  ? C VAL 86  
460 1 Y 1 C ASN 87  ? C ASN 87  
461 1 Y 1 C THR 88  ? C THR 88  
462 1 Y 1 C ASP 89  ? C ASP 89  
463 1 Y 1 C LYS 90  ? C LYS 90  
464 1 Y 1 C LYS 91  ? C LYS 91  
465 1 Y 1 C LEU 92  ? C LEU 92  
466 1 Y 1 C GLU 93  ? C GLU 93  
467 1 Y 1 C LEU 94  ? C LEU 94  
468 1 Y 1 C ALA 95  ? C ALA 95  
469 1 Y 1 C TYR 96  ? C TYR 96  
470 1 Y 1 C ASP 97  ? C ASP 97  
471 1 Y 1 C ASN 98  ? C ASN 98  
472 1 Y 1 C PRO 99  ? C PRO 99  
473 1 Y 1 C PHE 100 ? C PHE 100 
474 1 Y 1 C GLU 101 ? C GLU 101 
475 1 Y 1 C SER 102 ? C SER 102 
476 1 Y 1 C SER 103 ? C SER 103 
477 1 Y 1 C ALA 104 ? C ALA 104 
478 1 Y 1 C ASN 105 ? C ASN 105 
479 1 Y 1 C LYS 106 ? C LYS 106 
480 1 Y 1 C LEU 107 ? C LEU 107 
481 1 Y 1 C SER 108 ? C SER 108 
482 1 Y 1 C LEU 109 ? C LEU 109 
483 1 Y 1 C LYS 110 ? C LYS 110 
484 1 Y 1 C VAL 111 ? C VAL 111 
485 1 Y 1 C GLY 112 ? C GLY 112 
486 1 Y 1 C HIS 113 ? C HIS 113 
487 1 Y 1 C GLY 114 ? C GLY 114 
488 1 Y 1 C LEU 115 ? C LEU 115 
489 1 Y 1 C LYS 116 ? C LYS 116 
490 1 Y 1 C VAL 117 ? C VAL 117 
491 1 Y 1 C LEU 118 ? C LEU 118 
492 1 Y 1 C ASP 119 ? C ASP 119 
493 1 Y 1 C GLU 120 ? C GLU 120 
494 1 Y 1 C LYS 121 ? C LYS 121 
495 1 Y 1 C SER 122 ? C SER 122 
496 1 Y 1 C ALA 123 ? C ALA 123 
497 1 Y 1 C ALA 124 ? C ALA 124 
498 1 Y 1 C GLY 125 ? C GLY 125 
499 1 Y 1 C LEU 126 ? C LEU 126 
500 1 Y 1 C LYS 127 ? C LYS 127 
501 1 Y 1 C ASP 128 ? C ASP 128 
502 1 Y 1 C LEU 129 ? C LEU 129 
503 1 Y 1 C ILE 130 ? C ILE 130 
504 1 Y 1 C GLY 131 ? C GLY 131 
505 1 Y 1 C LYS 132 ? C LYS 132 
506 1 Y 1 C LEU 133 ? C LEU 133 
507 1 Y 1 C VAL 134 ? C VAL 134 
508 1 Y 1 C VAL 135 ? C VAL 135 
509 1 Y 1 C LEU 136 ? C LEU 136 
510 1 Y 1 C THR 137 ? C THR 137 
511 1 Y 1 C GLY 138 ? C GLY 138 
512 1 Y 1 C LYS 139 ? C LYS 139 
513 1 Y 1 C GLY 140 ? C GLY 140 
514 1 Y 1 C ILE 141 ? C ILE 141 
515 1 Y 1 C GLY 142 ? C GLY 142 
516 1 Y 1 C THR 143 ? C THR 143 
517 1 Y 1 C GLU 144 ? C GLU 144 
518 1 Y 1 C ASN 145 ? C ASN 145 
519 1 Y 1 C LEU 146 ? C LEU 146 
520 1 Y 1 C GLU 147 ? C GLU 147 
521 1 Y 1 C ASN 148 ? C ASN 148 
522 1 Y 1 C THR 149 ? C THR 149 
523 1 Y 1 C ASP 150 ? C ASP 150 
524 1 Y 1 C GLY 151 ? C GLY 151 
525 1 Y 1 C SER 152 ? C SER 152 
526 1 Y 1 C SER 153 ? C SER 153 
527 1 Y 1 C ARG 154 ? C ARG 154 
528 1 Y 1 C GLY 155 ? C GLY 155 
529 1 Y 1 C ILE 156 ? C ILE 156 
530 1 Y 1 C GLY 157 ? C GLY 157 
531 1 Y 1 C ILE 158 ? C ILE 158 
532 1 Y 1 C ASN 159 ? C ASN 159 
533 1 Y 1 C VAL 160 ? C VAL 160 
534 1 Y 1 C ARG 161 ? C ARG 161 
535 1 Y 1 C ALA 162 ? C ALA 162 
536 1 Y 1 C ARG 163 ? C ARG 163 
537 1 Y 1 C GLU 164 ? C GLU 164 
538 1 Y 1 C GLY 165 ? C GLY 165 
539 1 Y 1 C LEU 166 ? C LEU 166 
540 1 Y 1 C THR 167 ? C THR 167 
541 1 Y 1 C PHE 168 ? C PHE 168 
542 1 Y 1 C ASP 169 ? C ASP 169 
543 1 Y 1 C ASN 170 ? C ASN 170 
544 1 Y 1 C ASP 171 ? C ASP 171 
545 1 Y 1 C GLY 172 ? C GLY 172 
546 1 Y 1 C TYR 173 ? C TYR 173 
547 1 Y 1 C LEU 174 ? C LEU 174 
548 1 Y 1 C VAL 175 ? C VAL 175 
549 1 Y 1 C ALA 176 ? C ALA 176 
550 1 Y 1 C TRP 177 ? C TRP 177 
551 1 Y 1 C ASN 178 ? C ASN 178 
552 1 Y 1 C PRO 179 ? C PRO 179 
# 
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 
ACT C    C  N N 1   
ACT O    O  N N 2   
ACT OXT  O  N N 3   
ACT CH3  C  N N 4   
ACT H1   H  N N 5   
ACT H2   H  N N 6   
ACT H3   H  N N 7   
ALA N    N  N N 8   
ALA CA   C  N S 9   
ALA C    C  N N 10  
ALA O    O  N N 11  
ALA CB   C  N N 12  
ALA OXT  O  N N 13  
ALA H    H  N N 14  
ALA H2   H  N N 15  
ALA HA   H  N N 16  
ALA HB1  H  N N 17  
ALA HB2  H  N N 18  
ALA HB3  H  N N 19  
ALA HXT  H  N N 20  
ANA C1   C  N N 21  
ANA C2   C  N R 22  
ANA C3   C  N N 23  
ANA C4   C  N S 24  
ANA C5   C  N R 25  
ANA C6   C  N R 26  
ANA C7   C  N R 27  
ANA C8   C  N R 28  
ANA C9   C  N N 29  
ANA C10  C  N N 30  
ANA C11  C  N N 31  
ANA C12  C  N N 32  
ANA CA4  C  N N 33  
ANA CM4  C  N N 34  
ANA N5   N  N N 35  
ANA O1A  O  N N 36  
ANA O1B  O  N N 37  
ANA O2   O  N N 38  
ANA O4   O  N N 39  
ANA O6   O  N N 40  
ANA O7   O  N N 41  
ANA O8   O  N N 42  
ANA O9   O  N N 43  
ANA O10  O  N N 44  
ANA OA4  O  N N 45  
ANA H32  H  N N 46  
ANA H31  H  N N 47  
ANA H4   H  N N 48  
ANA H5   H  N N 49  
ANA H6   H  N N 50  
ANA H7   H  N N 51  
ANA H8   H  N N 52  
ANA H92  H  N N 53  
ANA H91  H  N N 54  
ANA H111 H  N N 55  
ANA H113 H  N N 56  
ANA H112 H  N N 57  
ANA H121 H  N N 58  
ANA H122 H  N N 59  
ANA H123 H  N N 60  
ANA HM41 H  N N 61  
ANA HM42 H  N N 62  
ANA HM43 H  N N 63  
ANA HN5  H  N N 64  
ANA HO1B H  N N 65  
ANA HO7  H  N N 66  
ANA HO8  H  N N 67  
ANA HO9  H  N N 68  
ARG N    N  N N 69  
ARG CA   C  N S 70  
ARG C    C  N N 71  
ARG O    O  N N 72  
ARG CB   C  N N 73  
ARG CG   C  N N 74  
ARG CD   C  N N 75  
ARG NE   N  N N 76  
ARG CZ   C  N N 77  
ARG NH1  N  N N 78  
ARG NH2  N  N N 79  
ARG OXT  O  N N 80  
ARG H    H  N N 81  
ARG H2   H  N N 82  
ARG HA   H  N N 83  
ARG HB2  H  N N 84  
ARG HB3  H  N N 85  
ARG HG2  H  N N 86  
ARG HG3  H  N N 87  
ARG HD2  H  N N 88  
ARG HD3  H  N N 89  
ARG HE   H  N N 90  
ARG HH11 H  N N 91  
ARG HH12 H  N N 92  
ARG HH21 H  N N 93  
ARG HH22 H  N N 94  
ARG HXT  H  N N 95  
ASN N    N  N N 96  
ASN CA   C  N S 97  
ASN C    C  N N 98  
ASN O    O  N N 99  
ASN CB   C  N N 100 
ASN CG   C  N N 101 
ASN OD1  O  N N 102 
ASN ND2  N  N N 103 
ASN OXT  O  N N 104 
ASN H    H  N N 105 
ASN H2   H  N N 106 
ASN HA   H  N N 107 
ASN HB2  H  N N 108 
ASN HB3  H  N N 109 
ASN HD21 H  N N 110 
ASN HD22 H  N N 111 
ASN HXT  H  N N 112 
ASP N    N  N N 113 
ASP CA   C  N S 114 
ASP C    C  N N 115 
ASP O    O  N N 116 
ASP CB   C  N N 117 
ASP CG   C  N N 118 
ASP OD1  O  N N 119 
ASP OD2  O  N N 120 
ASP OXT  O  N N 121 
ASP H    H  N N 122 
ASP H2   H  N N 123 
ASP HA   H  N N 124 
ASP HB2  H  N N 125 
ASP HB3  H  N N 126 
ASP HD2  H  N N 127 
ASP HXT  H  N N 128 
CL  CL   CL N N 129 
CYS N    N  N N 130 
CYS CA   C  N R 131 
CYS C    C  N N 132 
CYS O    O  N N 133 
CYS CB   C  N N 134 
CYS SG   S  N N 135 
CYS OXT  O  N N 136 
CYS H    H  N N 137 
CYS H2   H  N N 138 
CYS HA   H  N N 139 
CYS HB2  H  N N 140 
CYS HB3  H  N N 141 
CYS HG   H  N N 142 
CYS HXT  H  N N 143 
GLN N    N  N N 144 
GLN CA   C  N S 145 
GLN C    C  N N 146 
GLN O    O  N N 147 
GLN CB   C  N N 148 
GLN CG   C  N N 149 
GLN CD   C  N N 150 
GLN OE1  O  N N 151 
GLN NE2  N  N N 152 
GLN OXT  O  N N 153 
GLN H    H  N N 154 
GLN H2   H  N N 155 
GLN HA   H  N N 156 
GLN HB2  H  N N 157 
GLN HB3  H  N N 158 
GLN HG2  H  N N 159 
GLN HG3  H  N N 160 
GLN HE21 H  N N 161 
GLN HE22 H  N N 162 
GLN HXT  H  N N 163 
GLU N    N  N N 164 
GLU CA   C  N S 165 
GLU C    C  N N 166 
GLU O    O  N N 167 
GLU CB   C  N N 168 
GLU CG   C  N N 169 
GLU CD   C  N N 170 
GLU OE1  O  N N 171 
GLU OE2  O  N N 172 
GLU OXT  O  N N 173 
GLU H    H  N N 174 
GLU H2   H  N N 175 
GLU HA   H  N N 176 
GLU HB2  H  N N 177 
GLU HB3  H  N N 178 
GLU HG2  H  N N 179 
GLU HG3  H  N N 180 
GLU HE2  H  N N 181 
GLU HXT  H  N N 182 
GLY N    N  N N 183 
GLY CA   C  N N 184 
GLY C    C  N N 185 
GLY O    O  N N 186 
GLY OXT  O  N N 187 
GLY H    H  N N 188 
GLY H2   H  N N 189 
GLY HA2  H  N N 190 
GLY HA3  H  N N 191 
GLY HXT  H  N N 192 
HIS N    N  N N 193 
HIS CA   C  N S 194 
HIS C    C  N N 195 
HIS O    O  N N 196 
HIS CB   C  N N 197 
HIS CG   C  Y N 198 
HIS ND1  N  Y N 199 
HIS CD2  C  Y N 200 
HIS CE1  C  Y N 201 
HIS NE2  N  Y N 202 
HIS OXT  O  N N 203 
HIS H    H  N N 204 
HIS H2   H  N N 205 
HIS HA   H  N N 206 
HIS HB2  H  N N 207 
HIS HB3  H  N N 208 
HIS HD1  H  N N 209 
HIS HD2  H  N N 210 
HIS HE1  H  N N 211 
HIS HE2  H  N N 212 
HIS HXT  H  N N 213 
HOH O    O  N N 214 
HOH H1   H  N N 215 
HOH H2   H  N N 216 
ILE N    N  N N 217 
ILE CA   C  N S 218 
ILE C    C  N N 219 
ILE O    O  N N 220 
ILE CB   C  N S 221 
ILE CG1  C  N N 222 
ILE CG2  C  N N 223 
ILE CD1  C  N N 224 
ILE OXT  O  N N 225 
ILE H    H  N N 226 
ILE H2   H  N N 227 
ILE HA   H  N N 228 
ILE HB   H  N N 229 
ILE HG12 H  N N 230 
ILE HG13 H  N N 231 
ILE HG21 H  N N 232 
ILE HG22 H  N N 233 
ILE HG23 H  N N 234 
ILE HD11 H  N N 235 
ILE HD12 H  N N 236 
ILE HD13 H  N N 237 
ILE HXT  H  N N 238 
LEU N    N  N N 239 
LEU CA   C  N S 240 
LEU C    C  N N 241 
LEU O    O  N N 242 
LEU CB   C  N N 243 
LEU CG   C  N N 244 
LEU CD1  C  N N 245 
LEU CD2  C  N N 246 
LEU OXT  O  N N 247 
LEU H    H  N N 248 
LEU H2   H  N N 249 
LEU HA   H  N N 250 
LEU HB2  H  N N 251 
LEU HB3  H  N N 252 
LEU HG   H  N N 253 
LEU HD11 H  N N 254 
LEU HD12 H  N N 255 
LEU HD13 H  N N 256 
LEU HD21 H  N N 257 
LEU HD22 H  N N 258 
LEU HD23 H  N N 259 
LEU HXT  H  N N 260 
LYS N    N  N N 261 
LYS CA   C  N S 262 
LYS C    C  N N 263 
LYS O    O  N N 264 
LYS CB   C  N N 265 
LYS CG   C  N N 266 
LYS CD   C  N N 267 
LYS CE   C  N N 268 
LYS NZ   N  N N 269 
LYS OXT  O  N N 270 
LYS H    H  N N 271 
LYS H2   H  N N 272 
LYS HA   H  N N 273 
LYS HB2  H  N N 274 
LYS HB3  H  N N 275 
LYS HG2  H  N N 276 
LYS HG3  H  N N 277 
LYS HD2  H  N N 278 
LYS HD3  H  N N 279 
LYS HE2  H  N N 280 
LYS HE3  H  N N 281 
LYS HZ1  H  N N 282 
LYS HZ2  H  N N 283 
LYS HZ3  H  N N 284 
LYS HXT  H  N N 285 
MET N    N  N N 286 
MET CA   C  N S 287 
MET C    C  N N 288 
MET O    O  N N 289 
MET CB   C  N N 290 
MET CG   C  N N 291 
MET SD   S  N N 292 
MET CE   C  N N 293 
MET OXT  O  N N 294 
MET H    H  N N 295 
MET H2   H  N N 296 
MET HA   H  N N 297 
MET HB2  H  N N 298 
MET HB3  H  N N 299 
MET HG2  H  N N 300 
MET HG3  H  N N 301 
MET HE1  H  N N 302 
MET HE2  H  N N 303 
MET HE3  H  N N 304 
MET HXT  H  N N 305 
PHE N    N  N N 306 
PHE CA   C  N S 307 
PHE C    C  N N 308 
PHE O    O  N N 309 
PHE CB   C  N N 310 
PHE CG   C  Y N 311 
PHE CD1  C  Y N 312 
PHE CD2  C  Y N 313 
PHE CE1  C  Y N 314 
PHE CE2  C  Y N 315 
PHE CZ   C  Y N 316 
PHE OXT  O  N N 317 
PHE H    H  N N 318 
PHE H2   H  N N 319 
PHE HA   H  N N 320 
PHE HB2  H  N N 321 
PHE HB3  H  N N 322 
PHE HD1  H  N N 323 
PHE HD2  H  N N 324 
PHE HE1  H  N N 325 
PHE HE2  H  N N 326 
PHE HZ   H  N N 327 
PHE HXT  H  N N 328 
PRO N    N  N N 329 
PRO CA   C  N S 330 
PRO C    C  N N 331 
PRO O    O  N N 332 
PRO CB   C  N N 333 
PRO CG   C  N N 334 
PRO CD   C  N N 335 
PRO OXT  O  N N 336 
PRO H    H  N N 337 
PRO HA   H  N N 338 
PRO HB2  H  N N 339 
PRO HB3  H  N N 340 
PRO HG2  H  N N 341 
PRO HG3  H  N N 342 
PRO HD2  H  N N 343 
PRO HD3  H  N N 344 
PRO HXT  H  N N 345 
SER N    N  N N 346 
SER CA   C  N S 347 
SER C    C  N N 348 
SER O    O  N N 349 
SER CB   C  N N 350 
SER OG   O  N N 351 
SER OXT  O  N N 352 
SER H    H  N N 353 
SER H2   H  N N 354 
SER HA   H  N N 355 
SER HB2  H  N N 356 
SER HB3  H  N N 357 
SER HG   H  N N 358 
SER HXT  H  N N 359 
THR N    N  N N 360 
THR CA   C  N S 361 
THR C    C  N N 362 
THR O    O  N N 363 
THR CB   C  N R 364 
THR OG1  O  N N 365 
THR CG2  C  N N 366 
THR OXT  O  N N 367 
THR H    H  N N 368 
THR H2   H  N N 369 
THR HA   H  N N 370 
THR HB   H  N N 371 
THR HG1  H  N N 372 
THR HG21 H  N N 373 
THR HG22 H  N N 374 
THR HG23 H  N N 375 
THR HXT  H  N N 376 
TRP N    N  N N 377 
TRP CA   C  N S 378 
TRP C    C  N N 379 
TRP O    O  N N 380 
TRP CB   C  N N 381 
TRP CG   C  Y N 382 
TRP CD1  C  Y N 383 
TRP CD2  C  Y N 384 
TRP NE1  N  Y N 385 
TRP CE2  C  Y N 386 
TRP CE3  C  Y N 387 
TRP CZ2  C  Y N 388 
TRP CZ3  C  Y N 389 
TRP CH2  C  Y N 390 
TRP OXT  O  N N 391 
TRP H    H  N N 392 
TRP H2   H  N N 393 
TRP HA   H  N N 394 
TRP HB2  H  N N 395 
TRP HB3  H  N N 396 
TRP HD1  H  N N 397 
TRP HE1  H  N N 398 
TRP HE3  H  N N 399 
TRP HZ2  H  N N 400 
TRP HZ3  H  N N 401 
TRP HH2  H  N N 402 
TRP HXT  H  N N 403 
TYR N    N  N N 404 
TYR CA   C  N S 405 
TYR C    C  N N 406 
TYR O    O  N N 407 
TYR CB   C  N N 408 
TYR CG   C  Y N 409 
TYR CD1  C  Y N 410 
TYR CD2  C  Y N 411 
TYR CE1  C  Y N 412 
TYR CE2  C  Y N 413 
TYR CZ   C  Y N 414 
TYR OH   O  N N 415 
TYR OXT  O  N N 416 
TYR H    H  N N 417 
TYR H2   H  N N 418 
TYR HA   H  N N 419 
TYR HB2  H  N N 420 
TYR HB3  H  N N 421 
TYR HD1  H  N N 422 
TYR HD2  H  N N 423 
TYR HE1  H  N N 424 
TYR HE2  H  N N 425 
TYR HH   H  N N 426 
TYR HXT  H  N N 427 
VAL N    N  N N 428 
VAL CA   C  N S 429 
VAL C    C  N N 430 
VAL O    O  N N 431 
VAL CB   C  N N 432 
VAL CG1  C  N N 433 
VAL CG2  C  N N 434 
VAL OXT  O  N N 435 
VAL H    H  N N 436 
VAL H2   H  N N 437 
VAL HA   H  N N 438 
VAL HB   H  N N 439 
VAL HG11 H  N N 440 
VAL HG12 H  N N 441 
VAL HG13 H  N N 442 
VAL HG21 H  N N 443 
VAL HG22 H  N N 444 
VAL HG23 H  N N 445 
VAL HXT  H  N N 446 
ZN  ZN   ZN N N 447 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ANA C1  C2   sing N N 19  
ANA C1  O1A  doub N N 20  
ANA C1  O1B  sing N N 21  
ANA C2  C3   sing N N 22  
ANA C2  O2   sing N N 23  
ANA C2  O6   sing N N 24  
ANA C3  C4   sing N N 25  
ANA C3  H32  sing N N 26  
ANA C3  H31  sing N N 27  
ANA C4  C5   sing N N 28  
ANA C4  O4   sing N N 29  
ANA C4  H4   sing N N 30  
ANA C5  C6   sing N N 31  
ANA C5  N5   sing N N 32  
ANA C5  H5   sing N N 33  
ANA C6  C7   sing N N 34  
ANA C6  O6   sing N N 35  
ANA C6  H6   sing N N 36  
ANA C7  C8   sing N N 37  
ANA C7  O7   sing N N 38  
ANA C7  H7   sing N N 39  
ANA C8  C9   sing N N 40  
ANA C8  O8   sing N N 41  
ANA C8  H8   sing N N 42  
ANA C9  O9   sing N N 43  
ANA C9  H92  sing N N 44  
ANA C9  H91  sing N N 45  
ANA C10 C11  sing N N 46  
ANA C10 N5   sing N N 47  
ANA C10 O10  doub N N 48  
ANA C11 H111 sing N N 49  
ANA C11 H113 sing N N 50  
ANA C11 H112 sing N N 51  
ANA C12 O2   sing N N 52  
ANA C12 H121 sing N N 53  
ANA C12 H122 sing N N 54  
ANA C12 H123 sing N N 55  
ANA CA4 CM4  sing N N 56  
ANA CA4 O4   sing N N 57  
ANA CA4 OA4  doub N N 58  
ANA CM4 HM41 sing N N 59  
ANA CM4 HM42 sing N N 60  
ANA CM4 HM43 sing N N 61  
ANA N5  HN5  sing N N 62  
ANA O1B HO1B sing N N 63  
ANA O7  HO7  sing N N 64  
ANA O8  HO8  sing N N 65  
ANA O9  HO9  sing N N 66  
ARG N   CA   sing N N 67  
ARG N   H    sing N N 68  
ARG N   H2   sing N N 69  
ARG CA  C    sing N N 70  
ARG CA  CB   sing N N 71  
ARG CA  HA   sing N N 72  
ARG C   O    doub N N 73  
ARG C   OXT  sing N N 74  
ARG CB  CG   sing N N 75  
ARG CB  HB2  sing N N 76  
ARG CB  HB3  sing N N 77  
ARG CG  CD   sing N N 78  
ARG CG  HG2  sing N N 79  
ARG CG  HG3  sing N N 80  
ARG CD  NE   sing N N 81  
ARG CD  HD2  sing N N 82  
ARG CD  HD3  sing N N 83  
ARG NE  CZ   sing N N 84  
ARG NE  HE   sing N N 85  
ARG CZ  NH1  sing N N 86  
ARG CZ  NH2  doub N N 87  
ARG NH1 HH11 sing N N 88  
ARG NH1 HH12 sing N N 89  
ARG NH2 HH21 sing N N 90  
ARG NH2 HH22 sing N N 91  
ARG OXT HXT  sing N N 92  
ASN N   CA   sing N N 93  
ASN N   H    sing N N 94  
ASN N   H2   sing N N 95  
ASN CA  C    sing N N 96  
ASN CA  CB   sing N N 97  
ASN CA  HA   sing N N 98  
ASN C   O    doub N N 99  
ASN C   OXT  sing N N 100 
ASN CB  CG   sing N N 101 
ASN CB  HB2  sing N N 102 
ASN CB  HB3  sing N N 103 
ASN CG  OD1  doub N N 104 
ASN CG  ND2  sing N N 105 
ASN ND2 HD21 sing N N 106 
ASN ND2 HD22 sing N N 107 
ASN OXT HXT  sing N N 108 
ASP N   CA   sing N N 109 
ASP N   H    sing N N 110 
ASP N   H2   sing N N 111 
ASP CA  C    sing N N 112 
ASP CA  CB   sing N N 113 
ASP CA  HA   sing N N 114 
ASP C   O    doub N N 115 
ASP C   OXT  sing N N 116 
ASP CB  CG   sing N N 117 
ASP CB  HB2  sing N N 118 
ASP CB  HB3  sing N N 119 
ASP CG  OD1  doub N N 120 
ASP CG  OD2  sing N N 121 
ASP OD2 HD2  sing N N 122 
ASP OXT HXT  sing N N 123 
CYS N   CA   sing N N 124 
CYS N   H    sing N N 125 
CYS N   H2   sing N N 126 
CYS CA  C    sing N N 127 
CYS CA  CB   sing N N 128 
CYS CA  HA   sing N N 129 
CYS C   O    doub N N 130 
CYS C   OXT  sing N N 131 
CYS CB  SG   sing N N 132 
CYS CB  HB2  sing N N 133 
CYS CB  HB3  sing N N 134 
CYS SG  HG   sing N N 135 
CYS OXT HXT  sing N N 136 
GLN N   CA   sing N N 137 
GLN N   H    sing N N 138 
GLN N   H2   sing N N 139 
GLN CA  C    sing N N 140 
GLN CA  CB   sing N N 141 
GLN CA  HA   sing N N 142 
GLN C   O    doub N N 143 
GLN C   OXT  sing N N 144 
GLN CB  CG   sing N N 145 
GLN CB  HB2  sing N N 146 
GLN CB  HB3  sing N N 147 
GLN CG  CD   sing N N 148 
GLN CG  HG2  sing N N 149 
GLN CG  HG3  sing N N 150 
GLN CD  OE1  doub N N 151 
GLN CD  NE2  sing N N 152 
GLN NE2 HE21 sing N N 153 
GLN NE2 HE22 sing N N 154 
GLN OXT HXT  sing N N 155 
GLU N   CA   sing N N 156 
GLU N   H    sing N N 157 
GLU N   H2   sing N N 158 
GLU CA  C    sing N N 159 
GLU CA  CB   sing N N 160 
GLU CA  HA   sing N N 161 
GLU C   O    doub N N 162 
GLU C   OXT  sing N N 163 
GLU CB  CG   sing N N 164 
GLU CB  HB2  sing N N 165 
GLU CB  HB3  sing N N 166 
GLU CG  CD   sing N N 167 
GLU CG  HG2  sing N N 168 
GLU CG  HG3  sing N N 169 
GLU CD  OE1  doub N N 170 
GLU CD  OE2  sing N N 171 
GLU OE2 HE2  sing N N 172 
GLU OXT HXT  sing N N 173 
GLY N   CA   sing N N 174 
GLY N   H    sing N N 175 
GLY N   H2   sing N N 176 
GLY CA  C    sing N N 177 
GLY CA  HA2  sing N N 178 
GLY CA  HA3  sing N N 179 
GLY C   O    doub N N 180 
GLY C   OXT  sing N N 181 
GLY OXT HXT  sing N N 182 
HIS N   CA   sing N N 183 
HIS N   H    sing N N 184 
HIS N   H2   sing N N 185 
HIS CA  C    sing N N 186 
HIS CA  CB   sing N N 187 
HIS CA  HA   sing N N 188 
HIS C   O    doub N N 189 
HIS C   OXT  sing N N 190 
HIS CB  CG   sing N N 191 
HIS CB  HB2  sing N N 192 
HIS CB  HB3  sing N N 193 
HIS CG  ND1  sing Y N 194 
HIS CG  CD2  doub Y N 195 
HIS ND1 CE1  doub Y N 196 
HIS ND1 HD1  sing N N 197 
HIS CD2 NE2  sing Y N 198 
HIS CD2 HD2  sing N N 199 
HIS CE1 NE2  sing Y N 200 
HIS CE1 HE1  sing N N 201 
HIS NE2 HE2  sing N N 202 
HIS OXT HXT  sing N N 203 
HOH O   H1   sing N N 204 
HOH O   H2   sing N N 205 
ILE N   CA   sing N N 206 
ILE N   H    sing N N 207 
ILE N   H2   sing N N 208 
ILE CA  C    sing N N 209 
ILE CA  CB   sing N N 210 
ILE CA  HA   sing N N 211 
ILE C   O    doub N N 212 
ILE C   OXT  sing N N 213 
ILE CB  CG1  sing N N 214 
ILE CB  CG2  sing N N 215 
ILE CB  HB   sing N N 216 
ILE CG1 CD1  sing N N 217 
ILE CG1 HG12 sing N N 218 
ILE CG1 HG13 sing N N 219 
ILE CG2 HG21 sing N N 220 
ILE CG2 HG22 sing N N 221 
ILE CG2 HG23 sing N N 222 
ILE CD1 HD11 sing N N 223 
ILE CD1 HD12 sing N N 224 
ILE CD1 HD13 sing N N 225 
ILE OXT HXT  sing N N 226 
LEU N   CA   sing N N 227 
LEU N   H    sing N N 228 
LEU N   H2   sing N N 229 
LEU CA  C    sing N N 230 
LEU CA  CB   sing N N 231 
LEU CA  HA   sing N N 232 
LEU C   O    doub N N 233 
LEU C   OXT  sing N N 234 
LEU CB  CG   sing N N 235 
LEU CB  HB2  sing N N 236 
LEU CB  HB3  sing N N 237 
LEU CG  CD1  sing N N 238 
LEU CG  CD2  sing N N 239 
LEU CG  HG   sing N N 240 
LEU CD1 HD11 sing N N 241 
LEU CD1 HD12 sing N N 242 
LEU CD1 HD13 sing N N 243 
LEU CD2 HD21 sing N N 244 
LEU CD2 HD22 sing N N 245 
LEU CD2 HD23 sing N N 246 
LEU OXT HXT  sing N N 247 
LYS N   CA   sing N N 248 
LYS N   H    sing N N 249 
LYS N   H2   sing N N 250 
LYS CA  C    sing N N 251 
LYS CA  CB   sing N N 252 
LYS CA  HA   sing N N 253 
LYS C   O    doub N N 254 
LYS C   OXT  sing N N 255 
LYS CB  CG   sing N N 256 
LYS CB  HB2  sing N N 257 
LYS CB  HB3  sing N N 258 
LYS CG  CD   sing N N 259 
LYS CG  HG2  sing N N 260 
LYS CG  HG3  sing N N 261 
LYS CD  CE   sing N N 262 
LYS CD  HD2  sing N N 263 
LYS CD  HD3  sing N N 264 
LYS CE  NZ   sing N N 265 
LYS CE  HE2  sing N N 266 
LYS CE  HE3  sing N N 267 
LYS NZ  HZ1  sing N N 268 
LYS NZ  HZ2  sing N N 269 
LYS NZ  HZ3  sing N N 270 
LYS OXT HXT  sing N N 271 
MET N   CA   sing N N 272 
MET N   H    sing N N 273 
MET N   H2   sing N N 274 
MET CA  C    sing N N 275 
MET CA  CB   sing N N 276 
MET CA  HA   sing N N 277 
MET C   O    doub N N 278 
MET C   OXT  sing N N 279 
MET CB  CG   sing N N 280 
MET CB  HB2  sing N N 281 
MET CB  HB3  sing N N 282 
MET CG  SD   sing N N 283 
MET CG  HG2  sing N N 284 
MET CG  HG3  sing N N 285 
MET SD  CE   sing N N 286 
MET CE  HE1  sing N N 287 
MET CE  HE2  sing N N 288 
MET CE  HE3  sing N N 289 
MET OXT HXT  sing N N 290 
PHE N   CA   sing N N 291 
PHE N   H    sing N N 292 
PHE N   H2   sing N N 293 
PHE CA  C    sing N N 294 
PHE CA  CB   sing N N 295 
PHE CA  HA   sing N N 296 
PHE C   O    doub N N 297 
PHE C   OXT  sing N N 298 
PHE CB  CG   sing N N 299 
PHE CB  HB2  sing N N 300 
PHE CB  HB3  sing N N 301 
PHE CG  CD1  doub Y N 302 
PHE CG  CD2  sing Y N 303 
PHE CD1 CE1  sing Y N 304 
PHE CD1 HD1  sing N N 305 
PHE CD2 CE2  doub Y N 306 
PHE CD2 HD2  sing N N 307 
PHE CE1 CZ   doub Y N 308 
PHE CE1 HE1  sing N N 309 
PHE CE2 CZ   sing Y N 310 
PHE CE2 HE2  sing N N 311 
PHE CZ  HZ   sing N N 312 
PHE OXT HXT  sing N N 313 
PRO N   CA   sing N N 314 
PRO N   CD   sing N N 315 
PRO N   H    sing N N 316 
PRO CA  C    sing N N 317 
PRO CA  CB   sing N N 318 
PRO CA  HA   sing N N 319 
PRO C   O    doub N N 320 
PRO C   OXT  sing N N 321 
PRO CB  CG   sing N N 322 
PRO CB  HB2  sing N N 323 
PRO CB  HB3  sing N N 324 
PRO CG  CD   sing N N 325 
PRO CG  HG2  sing N N 326 
PRO CG  HG3  sing N N 327 
PRO CD  HD2  sing N N 328 
PRO CD  HD3  sing N N 329 
PRO OXT HXT  sing N N 330 
SER N   CA   sing N N 331 
SER N   H    sing N N 332 
SER N   H2   sing N N 333 
SER CA  C    sing N N 334 
SER CA  CB   sing N N 335 
SER CA  HA   sing N N 336 
SER C   O    doub N N 337 
SER C   OXT  sing N N 338 
SER CB  OG   sing N N 339 
SER CB  HB2  sing N N 340 
SER CB  HB3  sing N N 341 
SER OG  HG   sing N N 342 
SER OXT HXT  sing N N 343 
THR N   CA   sing N N 344 
THR N   H    sing N N 345 
THR N   H2   sing N N 346 
THR CA  C    sing N N 347 
THR CA  CB   sing N N 348 
THR CA  HA   sing N N 349 
THR C   O    doub N N 350 
THR C   OXT  sing N N 351 
THR CB  OG1  sing N N 352 
THR CB  CG2  sing N N 353 
THR CB  HB   sing N N 354 
THR OG1 HG1  sing N N 355 
THR CG2 HG21 sing N N 356 
THR CG2 HG22 sing N N 357 
THR CG2 HG23 sing N N 358 
THR OXT HXT  sing N N 359 
TRP N   CA   sing N N 360 
TRP N   H    sing N N 361 
TRP N   H2   sing N N 362 
TRP CA  C    sing N N 363 
TRP CA  CB   sing N N 364 
TRP CA  HA   sing N N 365 
TRP C   O    doub N N 366 
TRP C   OXT  sing N N 367 
TRP CB  CG   sing N N 368 
TRP CB  HB2  sing N N 369 
TRP CB  HB3  sing N N 370 
TRP CG  CD1  doub Y N 371 
TRP CG  CD2  sing Y N 372 
TRP CD1 NE1  sing Y N 373 
TRP CD1 HD1  sing N N 374 
TRP CD2 CE2  doub Y N 375 
TRP CD2 CE3  sing Y N 376 
TRP NE1 CE2  sing Y N 377 
TRP NE1 HE1  sing N N 378 
TRP CE2 CZ2  sing Y N 379 
TRP CE3 CZ3  doub Y N 380 
TRP CE3 HE3  sing N N 381 
TRP CZ2 CH2  doub Y N 382 
TRP CZ2 HZ2  sing N N 383 
TRP CZ3 CH2  sing Y N 384 
TRP CZ3 HZ3  sing N N 385 
TRP CH2 HH2  sing N N 386 
TRP OXT HXT  sing N N 387 
TYR N   CA   sing N N 388 
TYR N   H    sing N N 389 
TYR N   H2   sing N N 390 
TYR CA  C    sing N N 391 
TYR CA  CB   sing N N 392 
TYR CA  HA   sing N N 393 
TYR C   O    doub N N 394 
TYR C   OXT  sing N N 395 
TYR CB  CG   sing N N 396 
TYR CB  HB2  sing N N 397 
TYR CB  HB3  sing N N 398 
TYR CG  CD1  doub Y N 399 
TYR CG  CD2  sing Y N 400 
TYR CD1 CE1  sing Y N 401 
TYR CD1 HD1  sing N N 402 
TYR CD2 CE2  doub Y N 403 
TYR CD2 HD2  sing N N 404 
TYR CE1 CZ   doub Y N 405 
TYR CE1 HE1  sing N N 406 
TYR CE2 CZ   sing Y N 407 
TYR CE2 HE2  sing N N 408 
TYR CZ  OH   sing N N 409 
TYR OH  HH   sing N N 410 
TYR OXT HXT  sing N N 411 
VAL N   CA   sing N N 412 
VAL N   H    sing N N 413 
VAL N   H2   sing N N 414 
VAL CA  C    sing N N 415 
VAL CA  CB   sing N N 416 
VAL CA  HA   sing N N 417 
VAL C   O    doub N N 418 
VAL C   OXT  sing N N 419 
VAL CB  CG1  sing N N 420 
VAL CB  CG2  sing N N 421 
VAL CB  HB   sing N N 422 
VAL CG1 HG11 sing N N 423 
VAL CG1 HG12 sing N N 424 
VAL CG1 HG13 sing N N 425 
VAL CG2 HG21 sing N N 426 
VAL CG2 HG22 sing N N 427 
VAL CG2 HG23 sing N N 428 
VAL OXT HXT  sing N N 429 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1uxa 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FAH 
_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]   0.017581 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002392 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014987 
_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]   0.013647 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 25.62398 1.50364  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 1.04373  23.83732 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 19.97189 1.75589  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 15.80542 1.70748  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 1.23737  29.19336 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 2.14387  29.76375 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASN A 1 181 ? 9.55162   -25.32333 25.08237  1.000 62.23559  ? 181 ASN A N   1 
ATOM   2    C  CA  . ASN A 1 181 ? 9.06613   -24.73445 26.33195  1.000 62.45150  ? 181 ASN A CA  1 
ATOM   3    C  C   . ASN A 1 181 ? 9.80290   -23.43237 26.67798  1.000 62.64081  ? 181 ASN A C   1 
ATOM   4    O  O   . ASN A 1 181 ? 10.68408  -23.41584 27.54477  1.000 61.11954  ? 181 ASN A O   1 
ATOM   5    C  CB  . ASN A 1 181 ? 9.21070   -25.73409 27.48146  1.000 62.53614  ? 181 ASN A CB  1 
ATOM   6    N  N   . ASP A 1 182 ? 9.41723   -22.34616 26.00830  1.000 88.29110  ? 182 ASP A N   1 
ATOM   7    C  CA  . ASP A 1 182 ? 10.07721  -21.04434 26.13420  1.000 68.21654  ? 182 ASP A CA  1 
ATOM   8    C  C   . ASP A 1 182 ? 9.47699   -20.29688 27.32127  1.000 64.44682  ? 182 ASP A C   1 
ATOM   9    O  O   . ASP A 1 182 ? 8.43060   -19.65247 27.19872  1.000 43.60239  ? 182 ASP A O   1 
ATOM   10   C  CB  . ASP A 1 182 ? 9.93617   -20.25313 24.83400  1.000 54.50931  ? 182 ASP A CB  1 
ATOM   11   C  CG  . ASP A 1 182 ? 10.68114  -18.92525 24.85502  1.000 50.52194  ? 182 ASP A CG  1 
ATOM   12   O  OD1 . ASP A 1 182 ? 11.34785  -18.59170 25.85737  1.000 55.01168  ? 182 ASP A OD1 1 
ATOM   13   O  OD2 . ASP A 1 182 ? 10.62086  -18.21489 23.83822  1.000 63.42953  ? 182 ASP A OD2 1 
ATOM   14   N  N   . THR A 1 183 ? 10.14771  -20.37590 28.47639  1.000 42.95614  ? 183 THR A N   1 
ATOM   15   C  CA  . THR A 1 183 ? 9.68768   -19.69684 29.68534  1.000 54.90745  ? 183 THR A CA  1 
ATOM   16   C  C   . THR A 1 183 ? 9.92803   -18.19326 29.64191  1.000 46.05205  ? 183 THR A C   1 
ATOM   17   O  O   . THR A 1 183 ? 9.54341   -17.49321 30.58544  1.000 45.87545  ? 183 THR A O   1 
ATOM   18   C  CB  . THR A 1 183 ? 10.36871  -20.28403 30.93341  1.000 59.08810  ? 183 THR A CB  1 
ATOM   19   N  N   . ARG A 1 184 ? 10.55275  -17.67874 28.58567  1.000 34.34825  ? 184 ARG A N   1 
ATOM   20   C  CA  . ARG A 1 184 ? 10.80994  -16.25178 28.46961  1.000 30.23818  ? 184 ARG A CA  1 
ATOM   21   C  C   . ARG A 1 184 ? 9.82029   -15.54005 27.55589  1.000 32.11204  ? 184 ARG A C   1 
ATOM   22   O  O   . ARG A 1 184 ? 9.98405   -14.34829 27.32259  1.000 27.20092  ? 184 ARG A O   1 
ATOM   23   C  CB  . ARG A 1 184 ? 12.23665  -16.01027 27.95702  1.000 44.37234  ? 184 ARG A CB  1 
ATOM   24   C  CG  . ARG A 1 184 ? 13.32510  -16.40079 28.95183  1.000 55.22690  ? 184 ARG A CG  1 
ATOM   25   C  CD  . ARG A 1 184 ? 14.70674  -16.09571 28.39281  1.000 57.94825  ? 184 ARG A CD  1 
ATOM   26   N  N   . THR A 1 185 ? 8.81512   -16.24296 27.02577  1.000 26.89047  ? 185 THR A N   1 
ATOM   27   C  CA  . THR A 1 185 ? 7.82899   -15.66499 26.11558  1.000 26.76917  ? 185 THR A CA  1 
ATOM   28   C  C   . THR A 1 185 ? 6.43687   -16.07347 26.54874  1.000 28.32572  ? 185 THR A C   1 
ATOM   29   O  O   . THR A 1 185 ? 6.12871   -17.26827 26.59387  1.000 29.04036  ? 185 THR A O   1 
ATOM   30   C  CB  . THR A 1 185 ? 8.05333   -16.12193 24.67187  1.000 33.61796  ? 185 THR A CB  1 
ATOM   31   O  OG1 . THR A 1 185 ? 9.26146   -15.53835 24.18205  1.000 41.98420  ? 185 THR A OG1 1 
ATOM   32   C  CG2 . THR A 1 185 ? 6.86672   -15.69826 23.79459  1.000 29.79156  ? 185 THR A CG2 1 
ATOM   33   N  N   . LEU A 1 186 ? 5.59698   -15.07848 26.82706  1.000 23.78403  ? 186 LEU A N   1 
ATOM   34   C  CA  . LEU A 1 186 ? 4.15770   -15.23789 26.94664  1.000 24.78125  ? 186 LEU A CA  1 
ATOM   35   C  C   . LEU A 1 186 ? 3.54921   -14.75266 25.64370  1.000 28.73381  ? 186 LEU A C   1 
ATOM   36   O  O   . LEU A 1 186 ? 3.87395   -13.64691 25.19682  1.000 26.82711  ? 186 LEU A O   1 
ATOM   37   C  CB  . LEU A 1 186 ? 3.62908   -14.37368 28.09216  1.000 26.31814  ? 186 LEU A CB  1 
ATOM   38   C  CG  . LEU A 1 186 ? 3.27351   -14.90446 29.44304  1.000 52.59014  ? 186 LEU A CG  1 
ATOM   39   C  CD1 . LEU A 1 186 ? 2.74769   -13.71098 30.17718  1.000 26.95277  ? 186 LEU A CD1 1 
ATOM   40   C  CD2 . LEU A 1 186 ? 2.21021   -15.99233 29.26702  1.000 38.13331  ? 186 LEU A CD2 1 
ATOM   41   N  N   . TRP A 1 187 ? 2.65420   -15.53579 25.05179  1.000 21.04983  ? 187 TRP A N   1 
ATOM   42   C  CA  . TRP A 1 187 ? 2.08640   -15.09653 23.78439  1.000 20.82496  ? 187 TRP A CA  1 
ATOM   43   C  C   . TRP A 1 187 ? 0.69066   -15.66556 23.54673  1.000 23.28522  ? 187 TRP A C   1 
ATOM   44   O  O   . TRP A 1 187 ? 0.16959   -16.47722 24.31710  1.000 25.54167  ? 187 TRP A O   1 
ATOM   45   C  CB  . TRP A 1 187 ? 3.04016   -15.41926 22.61350  1.000 22.80432  ? 187 TRP A CB  1 
ATOM   46   C  CG  . TRP A 1 187 ? 3.15378   -16.87141 22.21224  1.000 22.06038  ? 187 TRP A CG  1 
ATOM   47   C  CD1 . TRP A 1 187 ? 2.64387   -17.97639 22.85672  1.000 23.97159  ? 187 TRP A CD1 1 
ATOM   48   C  CD2 . TRP A 1 187 ? 3.81339   -17.35560 21.03754  1.000 22.60757  ? 187 TRP A CD2 1 
ATOM   49   N  NE1 . TRP A 1 187 ? 2.96980   -19.11982 22.13066  1.000 23.80156  ? 187 TRP A NE1 1 
ATOM   50   C  CE2 . TRP A 1 187 ? 3.68727   -18.75623 21.02089  1.000 24.40130  ? 187 TRP A CE2 1 
ATOM   51   C  CE3 . TRP A 1 187 ? 4.51193   -16.72830 19.99819  1.000 27.50717  ? 187 TRP A CE3 1 
ATOM   52   C  CZ2 . TRP A 1 187 ? 4.23242   -19.54187 20.00473  1.000 26.23588  ? 187 TRP A CZ2 1 
ATOM   53   C  CZ3 . TRP A 1 187 ? 5.04666   -17.50785 18.99917  1.000 26.94644  ? 187 TRP A CZ3 1 
ATOM   54   C  CH2 . TRP A 1 187 ? 4.90975   -18.90332 19.01063  1.000 31.54065  ? 187 TRP A CH2 1 
ATOM   55   N  N   . THR A 1 188 ? 0.06945   -15.17394 22.47808  1.000 24.58079  ? 188 THR A N   1 
ATOM   56   C  CA  . THR A 1 188 ? -1.23834  -15.61509 22.00303  1.000 19.80002  ? 188 THR A CA  1 
ATOM   57   C  C   . THR A 1 188 ? -1.19688  -16.75330 20.98630  1.000 37.44910  ? 188 THR A C   1 
ATOM   58   O  O   . THR A 1 188 ? -2.26358  -17.13290 20.48277  1.000 38.44861  ? 188 THR A O   1 
ATOM   59   C  CB  . THR A 1 188 ? -1.94696  -14.45299 21.32228  1.000 23.09002  ? 188 THR A CB  1 
ATOM   60   O  OG1 . THR A 1 188 ? -1.07722  -13.95793 20.28190  1.000 22.56725  ? 188 THR A OG1 1 
ATOM   61   C  CG2 . THR A 1 188 ? -2.22513  -13.33838 22.32406  1.000 20.33102  ? 188 THR A CG2 1 
ATOM   62   N  N   . THR A 1 189 ? -0.01616  -17.25576 20.63373  1.000 29.17817  ? 189 THR A N   1 
ATOM   63   C  CA  . THR A 1 189 ? 0.29847   -18.07619 19.44733  1.000 29.40514  ? 189 THR A CA  1 
ATOM   64   C  C   . THR A 1 189 ? 0.14410   -17.21547 18.20253  1.000 30.59971  ? 189 THR A C   1 
ATOM   65   O  O   . THR A 1 189 ? -0.58061  -16.21174 18.19941  1.000 30.80639  ? 189 THR A O   1 
ATOM   66   C  CB  . THR A 1 189 ? -0.56245  -19.33682 19.28919  1.000 31.67414  ? 189 THR A CB  1 
ATOM   67   O  OG1 . THR A 1 189 ? -1.82808  -18.97970 18.73604  1.000 37.35940  ? 189 THR A OG1 1 
ATOM   68   C  CG2 . THR A 1 189 ? -0.74491  -20.06107 20.61223  1.000 33.07478  ? 189 THR A CG2 1 
ATOM   69   N  N   . PRO A 1 190 ? 0.82573   -17.57130 17.11402  1.000 27.16734  ? 190 PRO A N   1 
ATOM   70   C  CA  . PRO A 1 190 ? 0.79613   -16.72757 15.91281  1.000 31.40634  ? 190 PRO A CA  1 
ATOM   71   C  C   . PRO A 1 190 ? -0.22671  -17.12957 14.85526  1.000 30.68479  ? 190 PRO A C   1 
ATOM   72   O  O   . PRO A 1 190 ? -0.13017  -16.61993 13.73838  1.000 36.34081  ? 190 PRO A O   1 
ATOM   73   C  CB  . PRO A 1 190 ? 2.22607   -16.89907 15.37973  1.000 31.80725  ? 190 PRO A CB  1 
ATOM   74   C  CG  . PRO A 1 190 ? 2.61113   -18.27885 15.75075  1.000 43.68888  ? 190 PRO A CG  1 
ATOM   75   C  CD  . PRO A 1 190 ? 1.96360   -18.51247 17.10582  1.000 32.13670  ? 190 PRO A CD  1 
ATOM   76   N  N   . ASP A 1 191 ? -1.19929  -17.99986 15.16097  1.000 28.62635  ? 191 ASP A N   1 
ATOM   77   C  CA  . ASP A 1 191 ? -2.18983  -18.40229 14.15871  1.000 29.85068  ? 191 ASP A CA  1 
ATOM   78   C  C   . ASP A 1 191 ? -3.24144  -17.30570 13.99855  1.000 42.28938  ? 191 ASP A C   1 
ATOM   79   O  O   . ASP A 1 191 ? -3.12214  -16.22401 14.57797  1.000 37.37642  ? 191 ASP A O   1 
ATOM   80   C  CB  . ASP A 1 191 ? -2.80721  -19.75825 14.50442  1.000 34.61505  ? 191 ASP A CB  1 
ATOM   81   C  CG  . ASP A 1 191 ? -3.56259  -19.76025 15.81941  1.000 50.79737  ? 191 ASP A CG  1 
ATOM   82   O  OD1 . ASP A 1 191 ? -3.97401  -18.68542 16.28890  1.000 37.82904  ? 191 ASP A OD1 1 
ATOM   83   O  OD2 . ASP A 1 191 ? -3.77577  -20.85975 16.37786  1.000 57.36045  ? 191 ASP A OD2 1 
ATOM   84   N  N   . THR A 1 192 ? -4.30251  -17.56981 13.22116  1.000 32.22146  ? 192 THR A N   1 
ATOM   85   C  CA  . THR A 1 192 ? -5.33089  -16.55679 12.98841  1.000 32.85006  ? 192 THR A CA  1 
ATOM   86   C  C   . THR A 1 192 ? -6.66429  -16.89396 13.63973  1.000 36.47891  ? 192 THR A C   1 
ATOM   87   O  O   . THR A 1 192 ? -7.66455  -16.22430 13.34857  1.000 34.58647  ? 192 THR A O   1 
ATOM   88   C  CB  . THR A 1 192 ? -5.54205  -16.34363 11.47996  1.000 36.89078  ? 192 THR A CB  1 
ATOM   89   O  OG1 . THR A 1 192 ? -5.79949  -17.60748 10.85931  1.000 37.18001  ? 192 THR A OG1 1 
ATOM   90   C  CG2 . THR A 1 192 ? -4.29972  -15.70291 10.83971  1.000 39.96498  ? 192 THR A CG2 1 
ATOM   91   N  N   . SER A 1 193 ? -6.69857  -17.88232 14.53219  1.000 35.15745  ? 193 SER A N   1 
ATOM   92   C  CA  . SER A 1 193 ? -7.92143  -18.25021 15.24264  1.000 32.56164  ? 193 SER A CA  1 
ATOM   93   C  C   . SER A 1 193 ? -8.35961  -17.12305 16.16098  1.000 27.97346  ? 193 SER A C   1 
ATOM   94   O  O   . SER A 1 193 ? -7.57615  -16.71666 17.01977  1.000 28.21149  ? 193 SER A O   1 
ATOM   95   C  CB  . SER A 1 193 ? -7.69451  -19.51313 16.05632  1.000 40.76206  ? 193 SER A CB  1 
ATOM   96   O  OG  . SER A 1 193 ? -7.22746  -20.55328 15.21901  1.000 52.56026  ? 193 SER A OG  1 
ATOM   97   N  N   . PRO A 1 194 ? -9.59203  -16.61917 16.04251  1.000 30.39717  ? 194 PRO A N   1 
ATOM   98   C  CA  . PRO A 1 194 ? -10.03083 -15.50352 16.89576  1.000 23.80857  ? 194 PRO A CA  1 
ATOM   99   C  C   . PRO A 1 194 ? -9.89304  -15.84664 18.36307  1.000 25.56173  ? 194 PRO A C   1 
ATOM   100  O  O   . PRO A 1 194 ? -10.16849 -16.97186 18.79475  1.000 26.95525  ? 194 PRO A O   1 
ATOM   101  C  CB  . PRO A 1 194 ? -11.50375 -15.31064 16.51238  1.000 33.75669  ? 194 PRO A CB  1 
ATOM   102  C  CG  . PRO A 1 194 ? -11.60084 -15.85280 15.12081  1.000 38.52176  ? 194 PRO A CG  1 
ATOM   103  C  CD  . PRO A 1 194 ? -10.61827 -16.99511 15.05299  1.000 31.20959  ? 194 PRO A CD  1 
ATOM   104  N  N   . ASN A 1 195 ? -9.43254  -14.87101 19.11358  1.000 22.37029  ? 195 ASN A N   1 
ATOM   105  C  CA  . ASN A 1 195 ? -9.12500  -15.08058 20.52680  1.000 19.64712  ? 195 ASN A CA  1 
ATOM   106  C  C   . ASN A 1 195 ? -9.56327  -13.91129 21.37620  1.000 23.00882  ? 195 ASN A C   1 
ATOM   107  O  O   . ASN A 1 195 ? -9.27299  -13.89666 22.58072  1.000 27.89525  ? 195 ASN A O   1 
ATOM   108  C  CB  . ASN A 1 195 ? -7.60494  -15.30911 20.71348  1.000 22.54159  ? 195 ASN A CB  1 
ATOM   109  C  CG  . ASN A 1 195 ? -6.75390  -14.08914 20.30116  1.000 23.26502  ? 195 ASN A CG  1 
ATOM   110  O  OD1 . ASN A 1 195 ? -7.27449  -13.03920 19.91740  1.000 21.68397  ? 195 ASN A OD1 1 
ATOM   111  N  ND2 . ASN A 1 195 ? -5.43188  -14.22831 20.43026  1.000 23.00652  ? 195 ASN A ND2 1 
ATOM   112  N  N   . CYS A 1 196 ? -10.27749 -12.95022 20.80363  1.000 23.39620  ? 196 CYS A N   1 
ATOM   113  C  CA  . CYS A 1 196 ? -10.49058 -11.66982 21.43934  1.000 18.38842  ? 196 CYS A CA  1 
ATOM   114  C  C   . CYS A 1 196 ? -11.90435 -11.17887 21.15481  1.000 25.17819  ? 196 CYS A C   1 
ATOM   115  O  O   . CYS A 1 196 ? -12.44857 -11.42379 20.07709  1.000 30.26437  ? 196 CYS A O   1 
ATOM   116  C  CB  . CYS A 1 196 ? -9.44141  -10.69099 20.93564  1.000 26.84571  ? 196 CYS A CB  1 
ATOM   117  S  SG  . CYS A 1 196 ? -9.33989  -9.11501  21.77868  1.000 29.63554  ? 196 CYS A SG  1 
ATOM   118  N  N   . THR A 1 197 ? -12.49978 -10.49471 22.13308  1.000 26.94811  ? 197 THR A N   1 
ATOM   119  C  CA  . THR A 1 197 ? -13.87509 -10.01541 22.03416  1.000 24.36975  ? 197 THR A CA  1 
ATOM   120  C  C   . THR A 1 197 ? -13.84281 -8.50531  22.18925  1.000 33.09815  ? 197 THR A C   1 
ATOM   121  O  O   . THR A 1 197 ? -13.53314 -7.99817  23.26885  1.000 36.51708  ? 197 THR A O   1 
ATOM   122  C  CB  . THR A 1 197 ? -14.75315 -10.66734 23.10983  1.000 27.26906  ? 197 THR A CB  1 
ATOM   123  O  OG1 . THR A 1 197 ? -14.84833 -12.07605 22.85464  1.000 29.55309  ? 197 THR A OG1 1 
ATOM   124  C  CG2 . THR A 1 197 ? -16.15165 -10.06889 23.10145  1.000 31.50068  ? 197 THR A CG2 1 
ATOM   125  N  N   . ILE A 1 198 ? -14.15347 -7.79068  21.11834  1.000 26.73780  ? 198 ILE A N   1 
ATOM   126  C  CA  . ILE A 1 198 ? -14.17070 -6.33469  21.14538  1.000 21.99900  ? 198 ILE A CA  1 
ATOM   127  C  C   . ILE A 1 198 ? -15.61320 -5.88126  21.28023  1.000 30.24777  ? 198 ILE A C   1 
ATOM   128  O  O   . ILE A 1 198 ? -15.96492 -5.15510  22.21213  1.000 38.03511  ? 198 ILE A O   1 
ATOM   129  C  CB  . ILE A 1 198 ? -13.54004 -5.71879  19.88312  1.000 32.35229  ? 198 ILE A CB  1 
ATOM   130  C  CG1 . ILE A 1 198 ? -12.08938 -6.19143  19.68733  1.000 30.16070  ? 198 ILE A CG1 1 
ATOM   131  C  CG2 . ILE A 1 198 ? -13.63963 -4.18181  19.91094  1.000 30.80116  ? 198 ILE A CG2 1 
ATOM   132  C  CD1 . ILE A 1 198 ? -11.50414 -5.76442  18.36519  1.000 32.72392  ? 198 ILE A CD1 1 
ATOM   133  N  N   . ALA A 1 199 ? -16.44249 -6.29471  20.34823  1.000 30.10737  ? 199 ALA A N   1 
ATOM   134  C  CA  . ALA A 1 199 ? -17.84661 -5.92239  20.37402  1.000 35.55598  ? 199 ALA A CA  1 
ATOM   135  C  C   . ALA A 1 199 ? -18.76476 -7.12215  20.45221  1.000 48.06123  ? 199 ALA A C   1 
ATOM   136  O  O   . ALA A 1 199 ? -19.83690 -7.02528  21.05680  1.000 47.95832  ? 199 ALA A O   1 
ATOM   137  C  CB  . ALA A 1 199 ? -18.20113 -5.09301  19.12913  1.000 36.99583  ? 199 ALA A CB  1 
ATOM   138  N  N   . GLN A 1 200 ? -18.36647 -8.24943  19.87104  1.000 32.66343  ? 200 GLN A N   1 
ATOM   139  C  CA  . GLN A 1 200 ? -19.09547 -9.50364  19.96963  1.000 35.76257  ? 200 GLN A CA  1 
ATOM   140  C  C   . GLN A 1 200 ? -18.07667 -10.61273 20.19105  1.000 40.69376  ? 200 GLN A C   1 
ATOM   141  O  O   . GLN A 1 200 ? -16.88379 -10.43768 19.93868  1.000 31.65709  ? 200 GLN A O   1 
ATOM   142  C  CB  . GLN A 1 200 ? -19.95188 -9.76463  18.72269  1.000 38.32971  ? 200 GLN A CB  1 
ATOM   143  C  CG  . GLN A 1 200 ? -19.14476 -9.99904  17.46232  1.000 38.71868  ? 200 GLN A CG  1 
ATOM   144  C  CD  . GLN A 1 200 ? -20.02961 -10.04934 16.22101  1.000 42.39216  ? 200 GLN A CD  1 
ATOM   145  O  OE1 . GLN A 1 200 ? -20.84038 -9.14907  15.99096  1.000 39.98457  ? 200 GLN A OE1 1 
ATOM   146  N  NE2 . GLN A 1 200 ? -19.88185 -11.09759 15.42608  1.000 38.47758  ? 200 GLN A NE2 1 
ATOM   147  N  N   . ASP A 1 201 ? -18.55744 -11.75981 20.66453  1.000 30.68524  ? 201 ASP A N   1 
ATOM   148  C  CA  . ASP A 1 201 ? -17.67709 -12.86116 21.04029  1.000 30.43935  ? 201 ASP A CA  1 
ATOM   149  C  C   . ASP A 1 201 ? -16.74690 -13.28733 19.91188  1.000 35.28509  ? 201 ASP A C   1 
ATOM   150  O  O   . ASP A 1 201 ? -17.19078 -13.57235 18.79858  1.000 33.72870  ? 201 ASP A O   1 
ATOM   151  C  CB  . ASP A 1 201 ? -18.52299 -14.06570 21.48031  1.000 37.95287  ? 201 ASP A CB  1 
ATOM   152  C  CG  . ASP A 1 201 ? -17.67704 -15.19252 22.06033  1.000 56.26867  ? 201 ASP A CG  1 
ATOM   153  O  OD1 . ASP A 1 201 ? -16.91998 -14.93992 23.02600  1.000 65.36447  ? 201 ASP A OD1 1 
ATOM   154  O  OD2 . ASP A 1 201 ? -17.77328 -16.33175 21.55751  1.000 63.54992  ? 201 ASP A OD2 1 
ATOM   155  N  N   . LYS A 1 202 ? -15.44546 -13.33366 20.21825  1.000 35.36009  ? 202 LYS A N   1 
ATOM   156  C  CA  . LYS A 1 202 ? -14.41680 -13.85244 19.31465  1.000 26.61730  ? 202 LYS A CA  1 
ATOM   157  C  C   . LYS A 1 202 ? -14.45485 -13.17045 17.95304  1.000 29.84774  ? 202 LYS A C   1 
ATOM   158  O  O   . LYS A 1 202 ? -14.35991 -13.82272 16.90636  1.000 31.69020  ? 202 LYS A O   1 
ATOM   159  C  CB  . LYS A 1 202 ? -14.53925 -15.36192 19.14424  1.000 29.01066  ? 202 LYS A CB  1 
ATOM   160  C  CG  . LYS A 1 202 ? -14.42963 -16.15339 20.41253  1.000 52.49023  ? 202 LYS A CG  1 
ATOM   161  C  CD  . LYS A 1 202 ? -13.07326 -15.98748 21.04678  1.000 53.89403  ? 202 LYS A CD  1 
ATOM   162  C  CE  . LYS A 1 202 ? -13.03303 -16.75492 22.36260  1.000 62.11582  ? 202 LYS A CE  1 
ATOM   163  N  NZ  . LYS A 1 202 ? -12.11621 -16.12239 23.32546  1.000 68.00372  ? 202 LYS A NZ  1 
ATOM   164  N  N   . ASP A 1 203 ? -14.56129 -11.84156 17.97075  1.000 26.20743  ? 203 ASP A N   1 
ATOM   165  C  CA  . ASP A 1 203 ? -14.61039 -11.08510 16.72157  1.000 28.18968  ? 203 ASP A CA  1 
ATOM   166  C  C   . ASP A 1 203 ? -13.24168 -10.62470 16.24718  1.000 24.49953  ? 203 ASP A C   1 
ATOM   167  O  O   . ASP A 1 203 ? -13.15840 -9.94961  15.21202  1.000 25.03564  ? 203 ASP A O   1 
ATOM   168  C  CB  . ASP A 1 203 ? -15.54658 -9.87692  16.84206  1.000 33.94775  ? 203 ASP A CB  1 
ATOM   169  C  CG  . ASP A 1 203 ? -15.11464 -8.88020  17.91113  1.000 33.12274  ? 203 ASP A CG  1 
ATOM   170  O  OD1 . ASP A 1 203 ? -14.04648 -9.06019  18.53932  1.000 32.43072  ? 203 ASP A OD1 1 
ATOM   171  O  OD2 . ASP A 1 203 ? -15.86279 -7.89212  18.13244  1.000 36.86095  ? 203 ASP A OD2 1 
ATOM   172  N  N   . SER A 1 204 ? -12.16321 -10.99435 16.93911  1.000 22.99327  ? 204 SER A N   1 
ATOM   173  C  CA  . SER A 1 204 ? -10.84753 -10.53777 16.50963  1.000 21.19802  ? 204 SER A CA  1 
ATOM   174  C  C   . SER A 1 204 ? -9.76740  -11.50976 16.95908  1.000 26.05595  ? 204 SER A C   1 
ATOM   175  O  O   . SER A 1 204 ? -9.96645  -12.31953 17.86611  1.000 26.68173  ? 204 SER A O   1 
ATOM   176  C  CB  . SER A 1 204 ? -10.55220 -9.14305  17.04997  1.000 26.00398  ? 204 SER A CB  1 
ATOM   177  O  OG  . SER A 1 204 ? -10.80377 -9.14002  18.43878  1.000 27.87867  ? 204 SER A OG  1 
ATOM   178  N  N   . LYS A 1 205 ? -8.62149  -11.42278 16.28785  1.000 25.79991  ? 205 LYS A N   1 
ATOM   179  C  CA  . LYS A 1 205 ? -7.38262  -12.07751 16.69820  1.000 24.71264  ? 205 LYS A CA  1 
ATOM   180  C  C   . LYS A 1 205 ? -6.37504  -10.99697 17.07612  1.000 22.97606  ? 205 LYS A C   1 
ATOM   181  O  O   . LYS A 1 205 ? -5.86422  -10.25771 16.21299  1.000 20.62714  ? 205 LYS A O   1 
ATOM   182  C  CB  . LYS A 1 205 ? -6.83353  -12.98456 15.60409  1.000 26.95391  ? 205 LYS A CB  1 
ATOM   183  C  CG  . LYS A 1 205 ? -5.37197  -13.38162 15.77348  1.000 27.97004  ? 205 LYS A CG  1 
ATOM   184  C  CD  . LYS A 1 205 ? -5.17335  -14.41578 16.84536  1.000 24.94129  ? 205 LYS A CD  1 
ATOM   185  C  CE  . LYS A 1 205 ? -3.66643  -14.59835 17.15794  1.000 33.38051  ? 205 LYS A CE  1 
ATOM   186  N  NZ  . LYS A 1 205 ? -3.41249  -15.97300 17.64541  1.000 42.62620  ? 205 LYS A NZ  1 
ATOM   187  N  N   . LEU A 1 206 ? -6.07425  -10.91832 18.36555  1.000 21.75022  ? 206 LEU A N   1 
ATOM   188  C  CA  . LEU A 1 206 ? -4.96951  -10.11145 18.85224  1.000 21.40476  ? 206 LEU A CA  1 
ATOM   189  C  C   . LEU A 1 206 ? -3.72820  -11.00270 18.85761  1.000 21.45577  ? 206 LEU A C   1 
ATOM   190  O  O   . LEU A 1 206 ? -3.71647  -12.05237 19.50503  1.000 23.41881  ? 206 LEU A O   1 
ATOM   191  C  CB  . LEU A 1 206 ? -5.26804  -9.58889  20.26206  1.000 21.10286  ? 206 LEU A CB  1 
ATOM   192  C  CG  . LEU A 1 206 ? -4.15353  -8.74411  20.89533  1.000 22.52387  ? 206 LEU A CG  1 
ATOM   193  C  CD1 . LEU A 1 206 ? -4.10780  -7.38070  20.24785  1.000 24.03560  ? 206 LEU A CD1 1 
ATOM   194  C  CD2 . LEU A 1 206 ? -4.35627  -8.61241  22.42559  1.000 22.48415  ? 206 LEU A CD2 1 
ATOM   195  N  N   . THR A 1 207 ? -2.70100  -10.62818 18.09057  1.000 21.45819  ? 207 THR A N   1 
ATOM   196  C  CA  . THR A 1 207 ? -1.43626  -11.34654 18.14257  1.000 20.44684  ? 207 THR A CA  1 
ATOM   197  C  C   . THR A 1 207 ? -0.51702  -10.52214 19.02870  1.000 25.32536  ? 207 THR A C   1 
ATOM   198  O  O   . THR A 1 207 ? -0.14158  -9.40819  18.66271  1.000 22.34729  ? 207 THR A O   1 
ATOM   199  C  CB  . THR A 1 207 ? -0.81940  -11.54430 16.75572  1.000 20.65738  ? 207 THR A CB  1 
ATOM   200  O  OG1 . THR A 1 207 ? -1.79062  -12.15237 15.89033  1.000 24.39617  ? 207 THR A OG1 1 
ATOM   201  C  CG2 . THR A 1 207 ? 0.41745   -12.45079 16.85430  1.000 26.06750  ? 207 THR A CG2 1 
ATOM   202  N  N   . LEU A 1 208 ? -0.16718  -11.05718 20.19454  1.000 19.69427  ? 208 LEU A N   1 
ATOM   203  C  CA  . LEU A 1 208 ? 0.63599   -10.32938 21.16311  1.000 18.41620  ? 208 LEU A CA  1 
ATOM   204  C  C   . LEU A 1 208 ? 1.72070   -11.26421 21.64983  1.000 20.93782  ? 208 LEU A C   1 
ATOM   205  O  O   . LEU A 1 208 ? 1.41849   -12.37680 22.09569  1.000 21.38416  ? 208 LEU A O   1 
ATOM   206  C  CB  . LEU A 1 208 ? -0.23070  -9.83087  22.33470  1.000 18.50170  ? 208 LEU A CB  1 
ATOM   207  C  CG  . LEU A 1 208 ? 0.55484   -9.13716  23.44579  1.000 19.76792  ? 208 LEU A CG  1 
ATOM   208  C  CD1 . LEU A 1 208 ? 1.29272   -7.87747  22.90796  1.000 18.04871  ? 208 LEU A CD1 1 
ATOM   209  C  CD2 . LEU A 1 208 ? -0.39253  -8.78109  24.62743  1.000 21.01862  ? 208 LEU A CD2 1 
ATOM   210  N  N   . VAL A 1 209 ? 2.97612   -10.83610 21.52940  1.000 18.53805  ? 209 VAL A N   1 
ATOM   211  C  CA  . VAL A 1 209 ? 4.11688   -11.61454 22.00713  1.000 20.05518  ? 209 VAL A CA  1 
ATOM   212  C  C   . VAL A 1 209 ? 4.86842   -10.76650 23.01526  1.000 22.93020  ? 209 VAL A C   1 
ATOM   213  O  O   . VAL A 1 209 ? 5.29166   -9.64626  22.69028  1.000 20.88222  ? 209 VAL A O   1 
ATOM   214  C  CB  . VAL A 1 209 ? 5.03780   -12.03849 20.85579  1.000 20.04318  ? 209 VAL A CB  1 
ATOM   215  C  CG1 . VAL A 1 209 ? 6.16822   -12.96772 21.35908  1.000 21.42279  ? 209 VAL A CG1 1 
ATOM   216  C  CG2 . VAL A 1 209 ? 4.20532   -12.70360 19.74363  1.000 22.60971  ? 209 VAL A CG2 1 
ATOM   217  N  N   . LEU A 1 210 ? 5.01969   -11.28877 24.24323  1.000 21.31523  ? 210 LEU A N   1 
ATOM   218  C  CA  . LEU A 1 210 ? 5.77778   -10.61945 25.29243  1.000 22.38286  ? 210 LEU A CA  1 
ATOM   219  C  C   . LEU A 1 210 ? 7.03885   -11.43152 25.57533  1.000 28.67897  ? 210 LEU A C   1 
ATOM   220  O  O   . LEU A 1 210 ? 6.94665   -12.57715 26.02566  1.000 27.22665  ? 210 LEU A O   1 
ATOM   221  C  CB  . LEU A 1 210 ? 4.93845   -10.48148 26.56907  1.000 20.93335  ? 210 LEU A CB  1 
ATOM   222  C  CG  . LEU A 1 210 ? 3.63083   -9.71956  26.40893  1.000 21.66834  ? 210 LEU A CG  1 
ATOM   223  C  CD1 . LEU A 1 210 ? 2.90957   -9.65754  27.77754  1.000 22.18257  ? 210 LEU A CD1 1 
ATOM   224  C  CD2 . LEU A 1 210 ? 3.85921   -8.29982  25.86940  1.000 24.42247  ? 210 LEU A CD2 1 
ATOM   225  N  N   . THR A 1 211 ? 8.20627   -10.86341 25.29260  1.000 21.32583  ? 211 THR A N   1 
ATOM   226  C  CA  . THR A 1 211 ? 9.46024   -11.58010 25.50631  1.000 19.73416  ? 211 THR A CA  1 
ATOM   227  C  C   . THR A 1 211 ? 10.26351  -10.91103 26.60608  1.000 25.23508  ? 211 THR A C   1 
ATOM   228  O  O   . THR A 1 211 ? 10.48840  -9.69735  26.57815  1.000 25.02522  ? 211 THR A O   1 
ATOM   229  C  CB  . THR A 1 211 ? 10.26799  -11.65128 24.21708  1.000 27.16612  ? 211 THR A CB  1 
ATOM   230  O  OG1 . THR A 1 211 ? 9.47419   -12.36164 23.26023  1.000 29.46025  ? 211 THR A OG1 1 
ATOM   231  C  CG2 . THR A 1 211 ? 11.53210  -12.40808 24.47394  1.000 32.16503  ? 211 THR A CG2 1 
ATOM   232  N  N   . LYS A 1 212 ? 10.64740  -11.68318 27.60934  1.000 24.14603  ? 212 LYS A N   1 
ATOM   233  C  CA  . LYS A 1 212 ? 11.30409  -11.07062 28.74416  1.000 24.16668  ? 212 LYS A CA  1 
ATOM   234  C  C   . LYS A 1 212 ? 12.78718  -10.92544 28.43460  1.000 29.85813  ? 212 LYS A C   1 
ATOM   235  O  O   . LYS A 1 212 ? 13.48104  -11.92135 28.22137  1.000 35.91232  ? 212 LYS A O   1 
ATOM   236  C  CB  . LYS A 1 212 ? 11.07232  -11.90352 30.00122  1.000 27.24107  ? 212 LYS A CB  1 
ATOM   237  C  CG  . LYS A 1 212 ? 11.67140  -11.29845 31.25350  1.000 33.66000  ? 212 LYS A CG  1 
ATOM   238  C  CD  . LYS A 1 212 ? 11.13436  -11.99284 32.49414  1.000 28.49332  ? 212 LYS A CD  1 
ATOM   239  C  CE  . LYS A 1 212 ? 11.80721  -11.45130 33.75311  1.000 28.94534  ? 212 LYS A CE  1 
ATOM   240  N  NZ  . LYS A 1 212 ? 11.57337  -10.01493 33.90663  1.000 31.98597  ? 212 LYS A NZ  1 
ATOM   241  N  N   . CYS A 1 213 ? 13.26329  -9.68686  28.35994  1.000 29.84903  ? 213 CYS A N   1 
ATOM   242  C  CA  . CYS A 1 213 ? 14.69395  -9.40124  28.28830  1.000 28.68413  ? 213 CYS A CA  1 
ATOM   243  C  C   . CYS A 1 213 ? 15.10346  -8.76088  29.61093  1.000 33.25628  ? 213 CYS A C   1 
ATOM   244  O  O   . CYS A 1 213 ? 15.37512  -7.56096  29.68952  1.000 50.43850  ? 213 CYS A O   1 
ATOM   245  C  CB  . CYS A 1 213 ? 15.00213  -8.46629  27.12954  1.000 36.47140  ? 213 CYS A CB  1 
ATOM   246  S  SG  . CYS A 1 213 ? 14.20400  -8.83897  25.57293  1.000 43.08889  ? 213 CYS A SG  1 
ATOM   247  N  N   . GLY A 1 214 ? 15.09839  -9.55715  30.65760  1.000 36.17422  ? 214 GLY A N   1 
ATOM   248  C  CA  . GLY A 1 214 ? 15.45681  -9.04639  31.97204  1.000 37.62237  ? 214 GLY A CA  1 
ATOM   249  C  C   . GLY A 1 214 ? 14.49214  -7.98386  32.46880  1.000 36.18801  ? 214 GLY A C   1 
ATOM   250  O  O   . GLY A 1 214 ? 13.28752  -8.22045  32.64635  1.000 33.52525  ? 214 GLY A O   1 
ATOM   251  N  N   . SER A 1 215 ? 15.01346  -6.76749  32.67162  1.000 30.25548  ? 215 SER A N   1 
ATOM   252  C  CA  . SER A 1 215 ? 14.23131  -5.68354  33.26297  1.000 30.41316  ? 215 SER A CA  1 
ATOM   253  C  C   . SER A 1 215 ? 13.22007  -5.08204  32.30169  1.000 30.54655  ? 215 SER A C   1 
ATOM   254  O  O   . SER A 1 215 ? 12.38107  -4.28129  32.72470  1.000 25.09739  ? 215 SER A O   1 
ATOM   255  C  CB  . SER A 1 215 ? 15.17783  -4.56886  33.72809  1.000 45.28535  ? 215 SER A CB  1 
ATOM   256  O  OG  . SER A 1 215 ? 15.95344  -4.11312  32.60671  1.000 39.76864  ? 215 SER A OG  1 
ATOM   257  N  N   . GLN A 1 216 ? 13.28131  -5.42381  31.02053  1.000 26.13720  ? 216 GLN A N   1 
ATOM   258  C  CA  . GLN A 1 216 ? 12.31421  -4.91598  30.06724  1.000 22.67333  ? 216 GLN A CA  1 
ATOM   259  C  C   . GLN A 1 216 ? 11.62804  -6.08643  29.38065  1.000 19.77851  ? 216 GLN A C   1 
ATOM   260  O  O   . GLN A 1 216 ? 12.24833  -7.13070  29.13667  1.000 24.97956  ? 216 GLN A O   1 
ATOM   261  C  CB  . GLN A 1 216 ? 12.96197  -4.02116  29.00029  1.000 26.38038  ? 216 GLN A CB  1 
ATOM   262  C  CG  . GLN A 1 216 ? 13.24306  -2.61802  29.44479  1.000 35.07446  ? 216 GLN A CG  1 
ATOM   263  C  CD  . GLN A 1 216 ? 13.85692  -1.78559  28.31448  1.000 22.50193  ? 216 GLN A CD  1 
ATOM   264  O  OE1 . GLN A 1 216 ? 13.17328  -1.40549  27.34225  1.000 26.44552  ? 216 GLN A OE1 1 
ATOM   265  N  NE2 . GLN A 1 216 ? 15.14042  -1.51443  28.43717  1.000 22.96056  ? 216 GLN A NE2 1 
ATOM   266  N  N   . ILE A 1 217 ? 10.35232  -5.88525  29.09746  1.000 18.97540  ? 217 ILE A N   1 
ATOM   267  C  CA  . ILE A 1 217 ? 9.55418   -6.77315  28.26604  1.000 17.90171  ? 217 ILE A CA  1 
ATOM   268  C  C   . ILE A 1 217 ? 9.54203   -6.17500  26.86961  1.000 20.23843  ? 217 ILE A C   1 
ATOM   269  O  O   . ILE A 1 217 ? 9.15513   -5.01694  26.68777  1.000 21.87242  ? 217 ILE A O   1 
ATOM   270  C  CB  . ILE A 1 217 ? 8.12558   -6.93004  28.79648  1.000 21.51982  ? 217 ILE A CB  1 
ATOM   271  C  CG1 . ILE A 1 217 ? 8.12738   -7.40566  30.25913  1.000 20.45208  ? 217 ILE A CG1 1 
ATOM   272  C  CG2 . ILE A 1 217 ? 7.33568   -7.89448  27.87380  1.000 21.97999  ? 217 ILE A CG2 1 
ATOM   273  C  CD1 . ILE A 1 217 ? 8.97881   -8.63044  30.50070  1.000 22.84150  ? 217 ILE A CD1 1 
ATOM   274  N  N   . LEU A 1 218 ? 9.97680   -6.96247  25.89499  1.000 18.06498  ? 218 LEU A N   1 
ATOM   275  C  CA  . LEU A 1 218 ? 9.87892   -6.59235  24.48399  1.000 21.36333  ? 218 LEU A CA  1 
ATOM   276  C  C   . LEU A 1 218 ? 8.55002   -7.11209  23.94948  1.000 19.38805  ? 218 LEU A C   1 
ATOM   277  O  O   . LEU A 1 218 ? 8.26100   -8.30641  24.03896  1.000 21.74211  ? 218 LEU A O   1 
ATOM   278  C  CB  . LEU A 1 218 ? 11.06577  -7.17459  23.70108  1.000 20.58776  ? 218 LEU A CB  1 
ATOM   279  C  CG  . LEU A 1 218 ? 11.13797  -6.85943  22.18614  1.000 23.35507  ? 218 LEU A CG  1 
ATOM   280  C  CD1 . LEU A 1 218 ? 11.37367  -5.37299  21.94277  1.000 23.64456  ? 218 LEU A CD1 1 
ATOM   281  C  CD2 . LEU A 1 218 ? 12.30149  -7.66183  21.61417  1.000 21.49155  ? 218 LEU A CD2 1 
ATOM   282  N  N   . ALA A 1 219 ? 7.73286   -6.21819  23.40413  1.000 18.39519  ? 219 ALA A N   1 
ATOM   283  C  CA  . ALA A 1 219 ? 6.37752   -6.57502  23.02435  1.000 20.74888  ? 219 ALA A CA  1 
ATOM   284  C  C   . ALA A 1 219 ? 6.17223   -6.35459  21.53813  1.000 23.98234  ? 219 ALA A C   1 
ATOM   285  O  O   . ALA A 1 219 ? 6.60116   -5.34164  20.99624  1.000 21.57215  ? 219 ALA A O   1 
ATOM   286  C  CB  . ALA A 1 219 ? 5.32797   -5.73741  23.79545  1.000 21.12636  ? 219 ALA A CB  1 
ATOM   287  N  N   . ASN A 1 220 ? 5.45920   -7.27862  20.90432  1.000 18.95211  ? 220 ASN A N   1 
ATOM   288  C  CA  . ASN A 1 220 ? 5.12454   -7.17807  19.49083  1.000 17.21551  ? 220 ASN A CA  1 
ATOM   289  C  C   . ASN A 1 220 ? 3.62241   -7.41043  19.35391  1.000 20.29511  ? 220 ASN A C   1 
ATOM   290  O  O   . ASN A 1 220 ? 3.11717   -8.41644  19.86011  1.000 19.43777  ? 220 ASN A O   1 
ATOM   291  C  CB  . ASN A 1 220 ? 5.89742   -8.24130  18.72276  1.000 16.56948  ? 220 ASN A CB  1 
ATOM   292  C  CG  . ASN A 1 220 ? 5.70134   -8.13669  17.23828  1.000 24.85730  ? 220 ASN A CG  1 
ATOM   293  O  OD1 . ASN A 1 220 ? 4.86208   -8.82271  16.65086  1.000 27.45137  ? 220 ASN A OD1 1 
ATOM   294  N  ND2 . ASN A 1 220 ? 6.49115   -7.27866  16.60974  1.000 31.36070  ? 220 ASN A ND2 1 
ATOM   295  N  N   . VAL A 1 221 ? 2.89929   -6.51430  18.65368  1.000 17.84997  ? 221 VAL A N   1 
ATOM   296  C  CA  . VAL A 1 221 ? 1.43508   -6.60674  18.60909  1.000 16.57246  ? 221 VAL A CA  1 
ATOM   297  C  C   . VAL A 1 221 ? 0.90542   -6.33022  17.19706  1.000 18.72935  ? 221 VAL A C   1 
ATOM   298  O  O   . VAL A 1 221 ? 1.47030   -5.53275  16.44895  1.000 20.54203  ? 221 VAL A O   1 
ATOM   299  C  CB  . VAL A 1 221 ? 0.80759   -5.63834  19.65639  1.000 20.14354  ? 221 VAL A CB  1 
ATOM   300  C  CG1 . VAL A 1 221 ? 1.10077   -4.15881  19.30495  1.000 20.61043  ? 221 VAL A CG1 1 
ATOM   301  C  CG2 . VAL A 1 221 ? -0.67690  -5.89793  19.83518  1.000 20.60713  ? 221 VAL A CG2 1 
ATOM   302  N  N   . SER A 1 222 ? -0.18293  -7.02454  16.82459  1.000 17.98135  ? 222 SER A N   1 
ATOM   303  C  CA  . SER A 1 222 ? -0.98114  -6.70015  15.64120  1.000 20.19858  ? 222 SER A CA  1 
ATOM   304  C  C   . SER A 1 222 ? -2.42318  -7.13050  15.91332  1.000 24.06852  ? 222 SER A C   1 
ATOM   305  O  O   . SER A 1 222 ? -2.70058  -7.87143  16.85873  1.000 20.83015  ? 222 SER A O   1 
ATOM   306  C  CB  . SER A 1 222 ? -0.43402  -7.38083  14.37964  1.000 28.02115  ? 222 SER A CB  1 
ATOM   307  O  OG  . SER A 1 222 ? -0.65656  -8.78631  14.44670  1.000 24.75495  ? 222 SER A OG  1 
ATOM   308  N  N   . LEU A 1 223 ? -3.35377  -6.66755  15.08384  1.000 19.89900  ? 223 LEU A N   1 
ATOM   309  C  CA  . LEU A 1 223 ? -4.76577  -6.99207  15.30315  1.000 21.20811  ? 223 LEU A CA  1 
ATOM   310  C  C   . LEU A 1 223 ? -5.44972  -7.32160  13.98655  1.000 22.41065  ? 223 LEU A C   1 
ATOM   311  O  O   . LEU A 1 223 ? -5.23459  -6.63444  12.98833  1.000 23.25061  ? 223 LEU A O   1 
ATOM   312  C  CB  . LEU A 1 223 ? -5.52048  -5.82797  15.97112  1.000 22.99745  ? 223 LEU A CB  1 
ATOM   313  C  CG  . LEU A 1 223 ? -7.00944  -6.02054  16.28615  1.000 22.33845  ? 223 LEU A CG  1 
ATOM   314  C  CD1 . LEU A 1 223 ? -7.22665  -7.13703  17.34814  1.000 22.81356  ? 223 LEU A CD1 1 
ATOM   315  C  CD2 . LEU A 1 223 ? -7.60063  -4.69213  16.76279  1.000 25.15925  ? 223 LEU A CD2 1 
ATOM   316  N  N   . ILE A 1 224 ? -6.27155  -8.36493  13.99224  1.000 22.04296  ? 224 ILE A N   1 
ATOM   317  C  CA  . ILE A 1 224 ? -7.15159  -8.70802  12.86438  1.000 22.52888  ? 224 ILE A CA  1 
ATOM   318  C  C   . ILE A 1 224 ? -8.57326  -8.74894  13.39716  1.000 25.80293  ? 224 ILE A C   1 
ATOM   319  O  O   . ILE A 1 224 ? -8.87756  -9.56893  14.26793  1.000 23.53542  ? 224 ILE A O   1 
ATOM   320  C  CB  . ILE A 1 224 ? -6.80186  -10.06112 12.23035  1.000 23.59850  ? 224 ILE A CB  1 
ATOM   321  C  CG1 . ILE A 1 224 ? -5.35394  -10.08382 11.70082  1.000 28.45381  ? 224 ILE A CG1 1 
ATOM   322  C  CG2 . ILE A 1 224 ? -7.82122  -10.40199 11.12326  1.000 22.43960  ? 224 ILE A CG2 1 
ATOM   323  C  CD1 . ILE A 1 224 ? -4.86809  -11.48982 11.42611  1.000 27.94437  ? 224 ILE A CD1 1 
ATOM   324  N  N   . VAL A 1 225 ? -9.43665  -7.85391  12.93632  1.000 20.63107  ? 225 VAL A N   1 
ATOM   325  C  CA  . VAL A 1 225 ? -10.83308 -7.92649  13.34028  1.000 22.71394  ? 225 VAL A CA  1 
ATOM   326  C  C   . VAL A 1 225 ? -11.51365 -8.74818  12.26210  1.000 28.05824  ? 225 VAL A C   1 
ATOM   327  O  O   . VAL A 1 225 ? -11.46128 -8.37130  11.08522  1.000 28.62773  ? 225 VAL A O   1 
ATOM   328  C  CB  . VAL A 1 225 ? -11.47232 -6.53457  13.49431  1.000 24.29290  ? 225 VAL A CB  1 
ATOM   329  C  CG1 . VAL A 1 225 ? -12.92993 -6.67003  14.02306  1.000 23.05890  ? 225 VAL A CG1 1 
ATOM   330  C  CG2 . VAL A 1 225 ? -10.64225 -5.65454  14.45900  1.000 26.69947  ? 225 VAL A CG2 1 
ATOM   331  N  N   . VAL A 1 226 ? -12.15601 -9.85288  12.65312  1.000 25.18969  ? 226 VAL A N   1 
ATOM   332  C  CA  . VAL A 1 226 ? -12.67227 -10.81361 11.67823  1.000 29.31856  ? 226 VAL A CA  1 
ATOM   333  C  C   . VAL A 1 226 ? -14.17813 -10.73325 11.50039  1.000 29.20511  ? 226 VAL A C   1 
ATOM   334  O  O   . VAL A 1 226 ? -14.70548 -11.29623 10.52593  1.000 32.97843  ? 226 VAL A O   1 
ATOM   335  C  CB  . VAL A 1 226 ? -12.29023 -12.26505 12.05212  1.000 26.61071  ? 226 VAL A CB  1 
ATOM   336  C  CG1 . VAL A 1 226 ? -10.76126 -12.41072 12.09680  1.000 34.81995  ? 226 VAL A CG1 1 
ATOM   337  C  CG2 . VAL A 1 226 ? -12.90812 -12.68782 13.38231  1.000 31.43658  ? 226 VAL A CG2 1 
ATOM   338  N  N   . ALA A 1 227 ? -14.88772 -10.08064 12.40734  1.000 26.29976  ? 227 ALA A N   1 
ATOM   339  C  CA  . ALA A 1 227 ? -16.34125 -10.05374 12.34462  1.000 27.28956  ? 227 ALA A CA  1 
ATOM   340  C  C   . ALA A 1 227 ? -16.84430 -8.86420  13.15505  1.000 27.77232  ? 227 ALA A C   1 
ATOM   341  O  O   . ALA A 1 227 ? -16.09640 -8.23730  13.91067  1.000 27.03856  ? 227 ALA A O   1 
ATOM   342  C  CB  . ALA A 1 227 ? -16.92532 -11.36324 12.87787  1.000 33.61817  ? 227 ALA A CB  1 
ATOM   343  N  N   . GLY A 1 228 ? -18.13445 -8.56399  12.98430  1.000 32.48661  ? 228 GLY A N   1 
ATOM   344  C  CA  . GLY A 1 228 ? -18.76447 -7.59816  13.84848  1.000 38.96137  ? 228 GLY A CA  1 
ATOM   345  C  C   . GLY A 1 228 ? -18.53999 -6.15298  13.44771  1.000 34.13969  ? 228 GLY A C   1 
ATOM   346  O  O   . GLY A 1 228 ? -18.05180 -5.81021  12.36504  1.000 29.90464  ? 228 GLY A O   1 
ATOM   347  N  N   . LYS A 1 229 ? -18.86414 -5.28705  14.41030  1.000 30.08612  ? 229 LYS A N   1 
ATOM   348  C  CA  . LYS A 1 229 ? -18.97238 -3.84795  14.17422  1.000 33.23841  ? 229 LYS A CA  1 
ATOM   349  C  C   . LYS A 1 229 ? -17.66572 -3.22236  13.69283  1.000 37.67629  ? 229 LYS A C   1 
ATOM   350  O  O   . LYS A 1 229 ? -17.68556 -2.25688  12.91363  1.000 33.66819  ? 229 LYS A O   1 
ATOM   351  C  CB  . LYS A 1 229 ? -19.43500 -3.20898  15.49294  1.000 37.60862  ? 229 LYS A CB  1 
ATOM   352  C  CG  . LYS A 1 229 ? -19.05310 -1.77626  15.75504  1.000 37.70970  ? 229 LYS A CG  1 
ATOM   353  C  CD  . LYS A 1 229 ? -19.64161 -1.28868  17.10780  1.000 41.15166  ? 229 LYS A CD  1 
ATOM   354  C  CE  . LYS A 1 229 ? -19.42630 0.22708   17.27272  1.000 43.43314  ? 229 LYS A CE  1 
ATOM   355  N  NZ  . LYS A 1 229 ? -20.07797 0.80532   18.49210  1.000 52.77051  ? 229 LYS A NZ  1 
ATOM   356  N  N   . TYR A 1 230 ? -16.51479 -3.77609  14.07474  1.000 26.31771  ? 230 TYR A N   1 
ATOM   357  C  CA  . TYR A 1 230 ? -15.25897 -3.15885  13.68903  1.000 24.05313  ? 230 TYR A CA  1 
ATOM   358  C  C   . TYR A 1 230 ? -14.54420 -3.88650  12.54856  1.000 27.66505  ? 230 TYR A C   1 
ATOM   359  O  O   . TYR A 1 230 ? -13.40781 -3.52994  12.21765  1.000 28.29884  ? 230 TYR A O   1 
ATOM   360  C  CB  . TYR A 1 230 ? -14.33145 -3.02984  14.91142  1.000 24.78608  ? 230 TYR A CB  1 
ATOM   361  C  CG  . TYR A 1 230 ? -14.89489 -2.08734  15.96382  1.000 35.62294  ? 230 TYR A CG  1 
ATOM   362  C  CD1 . TYR A 1 230 ? -14.99036 -0.72094  15.71411  1.000 37.84552  ? 230 TYR A CD1 1 
ATOM   363  C  CD2 . TYR A 1 230 ? -15.35078 -2.57796  17.19263  1.000 28.26664  ? 230 TYR A CD2 1 
ATOM   364  C  CE1 . TYR A 1 230 ? -15.53165 0.14998   16.66636  1.000 31.21075  ? 230 TYR A CE1 1 
ATOM   365  C  CE2 . TYR A 1 230 ? -15.88076 -1.72488  18.14954  1.000 30.68251  ? 230 TYR A CE2 1 
ATOM   366  C  CZ  . TYR A 1 230 ? -15.96850 -0.35945  17.87161  1.000 31.15713  ? 230 TYR A CZ  1 
ATOM   367  O  OH  . TYR A 1 230 ? -16.47763 0.49519   18.81970  1.000 39.10591  ? 230 TYR A OH  1 
ATOM   368  N  N   . HIS A 1 231 ? -15.18497 -4.87264  11.92454  1.000 29.76461  ? 231 HIS A N   1 
ATOM   369  C  CA  . HIS A 1 231 ? -14.50659 -5.63951  10.88195  1.000 27.14346  ? 231 HIS A CA  1 
ATOM   370  C  C   . HIS A 1 231 ? -14.22590 -4.76550  9.66234   1.000 32.91464  ? 231 HIS A C   1 
ATOM   371  O  O   . HIS A 1 231 ? -13.14352 -4.83185  9.07316   1.000 31.51450  ? 231 HIS A O   1 
ATOM   372  C  CB  . HIS A 1 231 ? -15.34194 -6.87255  10.53031  1.000 25.96319  ? 231 HIS A CB  1 
ATOM   373  C  CG  . HIS A 1 231 ? -14.83812 -7.64369  9.34800   1.000 29.35104  ? 231 HIS A CG  1 
ATOM   374  N  ND1 . HIS A 1 231 ? -13.54120 -8.11173  9.24857   1.000 26.49579  ? 231 HIS A ND1 1 
ATOM   375  C  CD2 . HIS A 1 231 ? -15.46052 -8.01058  8.19898   1.000 33.63734  ? 231 HIS A CD2 1 
ATOM   376  C  CE1 . HIS A 1 231 ? -13.39060 -8.73882  8.09382   1.000 32.92618  ? 231 HIS A CE1 1 
ATOM   377  N  NE2 . HIS A 1 231 ? -14.53908 -8.69487  7.44306   1.000 31.60239  ? 231 HIS A NE2 1 
ATOM   378  N  N   . ILE A 1 232 ? -15.22092 -3.99591  9.23286   1.000 31.45999  ? 232 ILE A N   1 
ATOM   379  C  CA  . ILE A 1 232 ? -15.10922 -3.08533  8.09461   1.000 29.38372  ? 232 ILE A CA  1 
ATOM   380  C  C   . ILE A 1 232 ? -15.40736 -1.68395  8.58626   1.000 41.74323  ? 232 ILE A C   1 
ATOM   381  O  O   . ILE A 1 232 ? -16.46649 -1.44631  9.17847   1.000 42.29217  ? 232 ILE A O   1 
ATOM   382  C  CB  . ILE A 1 232 ? -16.06716 -3.45237  6.95457   1.000 36.02835  ? 232 ILE A CB  1 
ATOM   383  C  CG1 . ILE A 1 232 ? -15.80604 -4.88305  6.47405   1.000 38.05599  ? 232 ILE A CG1 1 
ATOM   384  C  CG2 . ILE A 1 232 ? -15.93436 -2.40106  5.83635   1.000 29.92266  ? 232 ILE A CG2 1 
ATOM   385  C  CD1 . ILE A 1 232 ? -14.46122 -5.06716  5.82226   1.000 39.19791  ? 232 ILE A CD1 1 
ATOM   386  N  N   . ILE A 1 233 ? -14.47289 -0.77404  8.39737   1.000 33.59993  ? 233 ILE A N   1 
ATOM   387  C  CA  . ILE A 1 233 ? -14.67956 0.60132   8.82098   1.000 34.41139  ? 233 ILE A CA  1 
ATOM   388  C  C   . ILE A 1 233 ? -15.33658 1.34925   7.67997   1.000 41.90761  ? 233 ILE A C   1 
ATOM   389  O  O   . ILE A 1 233 ? -14.87513 1.26188   6.53899   1.000 42.13750  ? 233 ILE A O   1 
ATOM   390  C  CB  . ILE A 1 233 ? -13.36185 1.26854   9.22502   1.000 30.60443  ? 233 ILE A CB  1 
ATOM   391  C  CG1 . ILE A 1 233 ? -12.68995 0.42833   10.31491  1.000 33.18350  ? 233 ILE A CG1 1 
ATOM   392  C  CG2 . ILE A 1 233 ? -13.61381 2.71681   9.62255   1.000 38.72040  ? 233 ILE A CG2 1 
ATOM   393  C  CD1 . ILE A 1 233 ? -13.65515 0.07869   11.46460  1.000 33.26724  ? 233 ILE A CD1 1 
ATOM   394  N  N   . ASN A 1 234 ? -16.42451 2.05840   7.97345   1.000 39.02839  ? 234 ASN A N   1 
ATOM   395  C  CA  . ASN A 1 234 ? -17.00885 2.96017   6.97590   1.000 47.72950  ? 234 ASN A CA  1 
ATOM   396  C  C   . ASN A 1 234 ? -17.44920 4.22681   7.69941   1.000 48.85707  ? 234 ASN A C   1 
ATOM   397  O  O   . ASN A 1 234 ? -18.54051 4.27863   8.27091   1.000 53.82388  ? 234 ASN A O   1 
ATOM   398  C  CB  . ASN A 1 234 ? -18.16325 2.31066   6.22954   1.000 50.90588  ? 234 ASN A CB  1 
ATOM   399  C  CG  . ASN A 1 234 ? -18.51404 3.05600   4.94539   1.000 52.08022  ? 234 ASN A CG  1 
ATOM   400  O  OD1 . ASN A 1 234 ? -18.42283 4.28104   4.87003   1.000 49.15676  ? 234 ASN A OD1 1 
ATOM   401  N  ND2 . ASN A 1 234 ? -18.86807 2.30721   3.91726   1.000 63.38116  ? 234 ASN A ND2 1 
ATOM   402  N  N   . ASN A 1 235 ? -16.60554 5.24869   7.65954   1.000 39.24156  ? 235 ASN A N   1 
ATOM   403  C  CA  . ASN A 1 235 ? -16.91176 6.50838   8.32492   1.000 48.32328  ? 235 ASN A CA  1 
ATOM   404  C  C   . ASN A 1 235 ? -17.79184 7.42289   7.49595   1.000 44.80060  ? 235 ASN A C   1 
ATOM   405  O  O   . ASN A 1 235 ? -18.15791 8.49402   7.97917   1.000 48.93432  ? 235 ASN A O   1 
ATOM   406  C  CB  . ASN A 1 235 ? -15.63307 7.24266   8.69539   1.000 47.07590  ? 235 ASN A CB  1 
ATOM   407  C  CG  . ASN A 1 235 ? -14.85494 6.51997   9.75421   1.000 53.64984  ? 235 ASN A CG  1 
ATOM   408  O  OD1 . ASN A 1 235 ? -13.64987 6.34332   9.62437   1.000 42.56849  ? 235 ASN A OD1 1 
ATOM   409  N  ND2 . ASN A 1 235 ? -15.54384 6.07436   10.80395  1.000 46.43460  ? 235 ASN A ND2 1 
ATOM   410  N  N   . LYS A 1 236 ? -18.12162 7.03739   6.26821   1.000 49.47428  ? 236 LYS A N   1 
ATOM   411  C  CA  . LYS A 1 236 ? -19.15734 7.76194   5.54332   1.000 70.25892  ? 236 LYS A CA  1 
ATOM   412  C  C   . LYS A 1 236 ? -20.51801 7.53087   6.18603   1.000 76.06574  ? 236 LYS A C   1 
ATOM   413  O  O   . LYS A 1 236 ? -21.31333 8.46584   6.32420   1.000 91.45125  ? 236 LYS A O   1 
ATOM   414  C  CB  . LYS A 1 236 ? -19.16390 7.34012   4.07377   1.000 62.04177  ? 236 LYS A CB  1 
ATOM   415  N  N   . THR A 1 237 ? -20.78929 6.29807   6.61455   1.000 89.82363  ? 237 THR A N   1 
ATOM   416  C  CA  . THR A 1 237 ? -22.05608 5.99393   7.26845   1.000 99.18215  ? 237 THR A CA  1 
ATOM   417  C  C   . THR A 1 237 ? -22.04929 6.39270   8.74243   1.000 101.65085 ? 237 THR A C   1 
ATOM   418  O  O   . THR A 1 237 ? -22.97249 7.06516   9.21387   1.000 102.43090 ? 237 THR A O   1 
ATOM   419  C  CB  . THR A 1 237 ? -22.35557 4.50062   7.13538   1.000 95.36714  ? 237 THR A CB  1 
ATOM   420  N  N   . ASN A 1 238 ? -21.00824 6.00576   9.48395   1.000 74.20800  ? 238 ASN A N   1 
ATOM   421  C  CA  . ASN A 1 238 ? -20.90826 6.26641   10.91944  1.000 62.34534  ? 238 ASN A CA  1 
ATOM   422  C  C   . ASN A 1 238 ? -19.61499 7.02888   11.18412  1.000 69.39679  ? 238 ASN A C   1 
ATOM   423  O  O   . ASN A 1 238 ? -18.58971 6.43485   11.55174  1.000 52.96734  ? 238 ASN A O   1 
ATOM   424  C  CB  . ASN A 1 238 ? -20.97152 4.96967   11.72500  1.000 59.65941  ? 238 ASN A CB  1 
ATOM   425  N  N   . PRO A 1 239 ? -19.62661 8.35271   11.01346  1.000 65.26028  ? 239 PRO A N   1 
ATOM   426  C  CA  . PRO A 1 239 ? -18.39580 9.13939   11.20224  1.000 67.10351  ? 239 PRO A CA  1 
ATOM   427  C  C   . PRO A 1 239 ? -17.90367 9.20410   12.63852  1.000 73.11666  ? 239 PRO A C   1 
ATOM   428  O  O   . PRO A 1 239 ? -16.79396 9.70865   12.86351  1.000 60.52915  ? 239 PRO A O   1 
ATOM   429  C  CB  . PRO A 1 239 ? -18.79426 10.53076  10.69925  1.000 72.52469  ? 239 PRO A CB  1 
ATOM   430  C  CG  . PRO A 1 239 ? -20.26478 10.56564  10.88178  1.000 73.59022  ? 239 PRO A CG  1 
ATOM   431  C  CD  . PRO A 1 239 ? -20.76539 9.19055   10.60561  1.000 67.27785  ? 239 PRO A CD  1 
ATOM   432  N  N   . LYS A 1 240 ? -18.68862 8.73579   13.60977  1.000 61.50551  ? 240 LYS A N   1 
ATOM   433  C  CA  . LYS A 1 240 ? -18.32859 8.79331   15.02185  1.000 72.75138  ? 240 LYS A CA  1 
ATOM   434  C  C   . LYS A 1 240 ? -17.67161 7.51595   15.53305  1.000 56.77968  ? 240 LYS A C   1 
ATOM   435  O  O   . LYS A 1 240 ? -17.21192 7.48771   16.68229  1.000 50.33470  ? 240 LYS A O   1 
ATOM   436  C  CB  . LYS A 1 240 ? -19.57233 9.10739   15.85585  1.000 70.09302  ? 240 LYS A CB  1 
ATOM   437  C  CG  . LYS A 1 240 ? -19.95494 10.56862  15.79497  1.000 81.18933  ? 240 LYS A CG  1 
ATOM   438  C  CD  . LYS A 1 240 ? -19.00006 11.38444  16.63732  1.000 81.44005  ? 240 LYS A CD  1 
ATOM   439  C  CE  . LYS A 1 240 ? -18.85005 12.78326  16.09619  1.000 87.71755  ? 240 LYS A CE  1 
ATOM   440  N  NZ  . LYS A 1 240 ? -18.37388 12.75101  14.69003  1.000 98.27561  ? 240 LYS A NZ  1 
ATOM   441  N  N   . ILE A 1 241 ? -17.68190 6.44917   14.74028  1.000 42.67021  ? 241 ILE A N   1 
ATOM   442  C  CA  . ILE A 1 241 ? -17.02536 5.20352   15.10313  1.000 41.69903  ? 241 ILE A CA  1 
ATOM   443  C  C   . ILE A 1 241 ? -15.56765 5.33033   14.68354  1.000 47.21638  ? 241 ILE A C   1 
ATOM   444  O  O   . ILE A 1 241 ? -15.21017 5.01334   13.53916  1.000 38.09208  ? 241 ILE A O   1 
ATOM   445  C  CB  . ILE A 1 241 ? -17.69617 3.99349   14.43217  1.000 63.53554  ? 241 ILE A CB  1 
ATOM   446  C  CG1 . ILE A 1 241 ? -19.15497 3.87814   14.87799  1.000 63.45941  ? 241 ILE A CG1 1 
ATOM   447  C  CG2 . ILE A 1 241 ? -16.93825 2.71097   14.74476  1.000 55.37654  ? 241 ILE A CG2 1 
ATOM   448  C  CD1 . ILE A 1 241 ? -19.86263 2.69442   14.27375  1.000 73.95218  ? 241 ILE A CD1 1 
ATOM   449  N  N   . LYS A 1 242 ? -14.71955 5.78255   15.61296  1.000 34.44772  ? 242 LYS A N   1 
ATOM   450  C  CA  . LYS A 1 242 ? -13.33281 6.10991   15.31542  1.000 29.80209  ? 242 LYS A CA  1 
ATOM   451  C  C   . LYS A 1 242 ? -12.35767 5.46970   16.28741  1.000 27.82779  ? 242 LYS A C   1 
ATOM   452  O  O   . LYS A 1 242 ? -11.18113 5.82695   16.26526  1.000 28.47735  ? 242 LYS A O   1 
ATOM   453  C  CB  . LYS A 1 242 ? -13.11370 7.62385   15.33371  1.000 43.62452  ? 242 LYS A CB  1 
ATOM   454  C  CG  . LYS A 1 242 ? -14.01398 8.40216   14.38326  1.000 45.88295  ? 242 LYS A CG  1 
ATOM   455  C  CD  . LYS A 1 242 ? -13.68137 8.06592   12.93404  1.000 64.19755  ? 242 LYS A CD  1 
ATOM   456  C  CE  . LYS A 1 242 ? -12.88853 9.17753   12.26197  1.000 55.86248  ? 242 LYS A CE  1 
ATOM   457  N  NZ  . LYS A 1 242 ? -12.90456 8.99198   10.79008  1.000 53.13175  ? 242 LYS A NZ  1 
ATOM   458  N  N   . SER A 1 243 ? -12.82183 4.58495   17.17505  1.000 30.91462  ? 243 SER A N   1 
ATOM   459  C  CA  . SER A 1 243 ? -11.90392 4.01030   18.15570  1.000 34.86145  ? 243 SER A CA  1 
ATOM   460  C  C   . SER A 1 243 ? -12.54393 2.82771   18.86155  1.000 26.17313  ? 243 SER A C   1 
ATOM   461  O  O   . SER A 1 243 ? -13.77504 2.67774   18.89317  1.000 28.44290  ? 243 SER A O   1 
ATOM   462  C  CB  . SER A 1 243 ? -11.46606 5.03643   19.19829  1.000 34.77140  ? 243 SER A CB  1 
ATOM   463  O  OG  . SER A 1 243 ? -12.58262 5.40626   19.98135  1.000 42.41050  ? 243 SER A OG  1 
ATOM   464  N  N   . PHE A 1 244 ? -11.68240 1.98009   19.43147  1.000 25.08577  ? 244 PHE A N   1 
ATOM   465  C  CA  . PHE A 1 244 ? -12.12934 0.90930   20.30569  1.000 25.17116  ? 244 PHE A CA  1 
ATOM   466  C  C   . PHE A 1 244 ? -10.97141 0.48167   21.19242  1.000 22.21192  ? 244 PHE A C   1 
ATOM   467  O  O   . PHE A 1 244 ? -9.81414  0.82221   20.93616  1.000 24.85072  ? 244 PHE A O   1 
ATOM   468  C  CB  . PHE A 1 244 ? -12.67513 -0.29612  19.51853  1.000 26.86033  ? 244 PHE A CB  1 
ATOM   469  C  CG  . PHE A 1 244 ? -11.70496 -0.89336  18.53931  1.000 27.47239  ? 244 PHE A CG  1 
ATOM   470  C  CD1 . PHE A 1 244 ? -10.83170 -1.89288  18.93557  1.000 26.10566  ? 244 PHE A CD1 1 
ATOM   471  C  CD2 . PHE A 1 244 ? -11.69657 -0.47639  17.20173  1.000 26.01001  ? 244 PHE A CD2 1 
ATOM   472  C  CE1 . PHE A 1 244 ? -9.93009  -2.45945  18.03208  1.000 27.67342  ? 244 PHE A CE1 1 
ATOM   473  C  CE2 . PHE A 1 244 ? -10.82231 -1.05304  16.29345  1.000 23.66757  ? 244 PHE A CE2 1 
ATOM   474  C  CZ  . PHE A 1 244 ? -9.94226  -2.04698  16.71180  1.000 27.60177  ? 244 PHE A CZ  1 
ATOM   475  N  N   . THR A 1 245 ? -11.29870 -0.26744  22.25053  1.000 21.40772  ? 245 THR A N   1 
ATOM   476  C  CA  . THR A 1 245 ? -10.27405 -0.62999  23.22441  1.000 20.95637  ? 245 THR A CA  1 
ATOM   477  C  C   . THR A 1 245 ? -10.25179 -2.12893  23.47967  1.000 25.21721  ? 245 THR A C   1 
ATOM   478  O  O   . THR A 1 245 ? -11.30584 -2.77473  23.50635  1.000 28.56090  ? 245 THR A O   1 
ATOM   479  C  CB  . THR A 1 245 ? -10.53577 0.11778   24.54893  1.000 33.06832  ? 245 THR A CB  1 
ATOM   480  O  OG1 . THR A 1 245 ? -10.51049 1.52088   24.29821  1.000 34.19389  ? 245 THR A OG1 1 
ATOM   481  C  CG2 . THR A 1 245 ? -9.48768  -0.20439  25.57981  1.000 31.34039  ? 245 THR A CG2 1 
ATOM   482  N  N   . ILE A 1 246 ? -9.05130  -2.67431  23.66430  1.000 22.26212  ? 246 ILE A N   1 
ATOM   483  C  CA  . ILE A 1 246 ? -8.84789  -4.06213  24.08180  1.000 23.82704  ? 246 ILE A CA  1 
ATOM   484  C  C   . ILE A 1 246 ? -8.09114  -4.04353  25.39892  1.000 24.73969  ? 246 ILE A C   1 
ATOM   485  O  O   . ILE A 1 246 ? -6.99193  -3.48053  25.47803  1.000 25.07214  ? 246 ILE A O   1 
ATOM   486  C  CB  . ILE A 1 246 ? -8.07484  -4.85844  23.02048  1.000 20.95888  ? 246 ILE A CB  1 
ATOM   487  C  CG1 . ILE A 1 246 ? -8.93630  -5.00862  21.75063  1.000 26.14154  ? 246 ILE A CG1 1 
ATOM   488  C  CG2 . ILE A 1 246 ? -7.55539  -6.20738  23.59465  1.000 22.21861  ? 246 ILE A CG2 1 
ATOM   489  C  CD1 . ILE A 1 246 ? -8.19081  -5.56580  20.55439  1.000 28.41725  ? 246 ILE A CD1 1 
ATOM   490  N  N   . LYS A 1 247 ? -8.65322  -4.67736  26.42763  1.000 22.71446  ? 247 LYS A N   1 
ATOM   491  C  CA  . LYS A 1 247 ? -8.04337  -4.67022  27.76375  1.000 22.50585  ? 247 LYS A CA  1 
ATOM   492  C  C   . LYS A 1 247 ? -7.52133  -6.05051  28.14001  1.000 24.81687  ? 247 LYS A C   1 
ATOM   493  O  O   . LYS A 1 247 ? -8.23214  -7.04678  27.99322  1.000 23.61590  ? 247 LYS A O   1 
ATOM   494  C  CB  . LYS A 1 247 ? -9.04504  -4.21470  28.83149  1.000 23.86563  ? 247 LYS A CB  1 
ATOM   495  C  CG  . LYS A 1 247 ? -9.57710  -2.82762  28.56200  1.000 24.69977  ? 247 LYS A CG  1 
ATOM   496  C  CD  . LYS A 1 247 ? -10.45819 -2.31247  29.68566  1.000 37.03911  ? 247 LYS A CD  1 
ATOM   497  C  CE  . LYS A 1 247 ? -10.88382 -0.89197  29.35334  1.000 45.21235  ? 247 LYS A CE  1 
ATOM   498  N  NZ  . LYS A 1 247 ? -11.66166 -0.26138  30.45194  1.000 48.89599  ? 247 LYS A NZ  1 
ATOM   499  N  N   . LEU A 1 248 ? -6.29436  -6.09566  28.65106  1.000 20.66846  ? 248 LEU A N   1 
ATOM   500  C  CA  . LEU A 1 248 ? -5.74671  -7.27702  29.30887  1.000 23.26734  ? 248 LEU A CA  1 
ATOM   501  C  C   . LEU A 1 248 ? -5.59134  -6.94699  30.79620  1.000 20.39121  ? 248 LEU A C   1 
ATOM   502  O  O   . LEU A 1 248 ? -4.81965  -6.04855  31.14724  1.000 23.05930  ? 248 LEU A O   1 
ATOM   503  C  CB  . LEU A 1 248 ? -4.38962  -7.67114  28.72259  1.000 22.70863  ? 248 LEU A CB  1 
ATOM   504  C  CG  . LEU A 1 248 ? -4.36779  -8.40544  27.37906  1.000 25.02758  ? 248 LEU A CG  1 
ATOM   505  C  CD1 . LEU A 1 248 ? -4.96619  -7.59488  26.26721  1.000 31.09235  ? 248 LEU A CD1 1 
ATOM   506  C  CD2 . LEU A 1 248 ? -2.92631  -8.82374  27.03182  1.000 29.51595  ? 248 LEU A CD2 1 
ATOM   507  N  N   . LEU A 1 249 ? -6.29789  -7.68315  31.64651  1.000 21.27641  ? 249 LEU A N   1 
ATOM   508  C  CA  . LEU A 1 249 ? -6.33612  -7.44044  33.09030  1.000 23.10428  ? 249 LEU A CA  1 
ATOM   509  C  C   . LEU A 1 249 ? -5.69829  -8.63805  33.78381  1.000 23.00773  ? 249 LEU A C   1 
ATOM   510  O  O   . LEU A 1 249 ? -5.96267  -9.78595  33.41395  1.000 22.28784  ? 249 LEU A O   1 
ATOM   511  C  CB  . LEU A 1 249 ? -7.77883  -7.23129  33.60876  1.000 22.73607  ? 249 LEU A CB  1 
ATOM   512  C  CG  . LEU A 1 249 ? -8.68023  -6.28720  32.77831  1.000 30.04916  ? 249 LEU A CG  1 
ATOM   513  C  CD1 . LEU A 1 249 ? -10.13648 -6.32470  33.26236  1.000 36.29854  ? 249 LEU A CD1 1 
ATOM   514  C  CD2 . LEU A 1 249 ? -8.15861  -4.88145  32.82101  1.000 33.40811  ? 249 LEU A CD2 1 
ATOM   515  N  N   . PHE A 1 250 ? -4.82709  -8.37833  34.75079  1.000 24.00468  ? 250 PHE A N   1 
ATOM   516  C  CA  . PHE A 1 250 ? -4.09724  -9.46074  35.39483  1.000 23.06014  ? 250 PHE A CA  1 
ATOM   517  C  C   . PHE A 1 250 ? -4.28267  -9.38010  36.90330  1.000 23.71504  ? 250 PHE A C   1 
ATOM   518  O  O   . PHE A 1 250 ? -4.35847  -8.29160  37.48394  1.000 24.42959  ? 250 PHE A O   1 
ATOM   519  C  CB  . PHE A 1 250 ? -2.59087  -9.41793  35.07269  1.000 21.10361  ? 250 PHE A CB  1 
ATOM   520  C  CG  . PHE A 1 250 ? -2.28867  -9.44360  33.58954  1.000 19.82206  ? 250 PHE A CG  1 
ATOM   521  C  CD1 . PHE A 1 250 ? -2.15711  -10.65544 32.91607  1.000 23.14663  ? 250 PHE A CD1 1 
ATOM   522  C  CD2 . PHE A 1 250 ? -2.11219  -8.26220  32.89920  1.000 19.72432  ? 250 PHE A CD2 1 
ATOM   523  C  CE1 . PHE A 1 250 ? -1.89138  -10.68029 31.53999  1.000 19.43227  ? 250 PHE A CE1 1 
ATOM   524  C  CE2 . PHE A 1 250 ? -1.81049  -8.28503  31.52689  1.000 21.55110  ? 250 PHE A CE2 1 
ATOM   525  C  CZ  . PHE A 1 250 ? -1.70209  -9.50815  30.87045  1.000 21.94692  ? 250 PHE A CZ  1 
ATOM   526  N  N   . ASN A 1 251 ? -4.29673  -10.53614 37.53634  1.000 25.16755  ? 251 ASN A N   1 
ATOM   527  C  CA  . ASN A 1 251 ? -4.41468  -10.53309 38.98215  1.000 27.13584  ? 251 ASN A CA  1 
ATOM   528  C  C   . ASN A 1 251 ? -3.02394  -10.44661 39.62396  1.000 27.24973  ? 251 ASN A C   1 
ATOM   529  O  O   . ASN A 1 251 ? -2.00965  -10.21747 38.95726  1.000 27.64631  ? 251 ASN A O   1 
ATOM   530  C  CB  . ASN A 1 251 ? -5.24691  -11.74803 39.43139  1.000 30.47081  ? 251 ASN A CB  1 
ATOM   531  C  CG  . ASN A 1 251 ? -4.53496  -13.07707 39.22702  1.000 34.82337  ? 251 ASN A CG  1 
ATOM   532  O  OD1 . ASN A 1 251 ? -3.32124  -13.13847 39.05250  1.000 27.65385  ? 251 ASN A OD1 1 
ATOM   533  N  ND2 . ASN A 1 251 ? -5.30780  -14.16239 39.26170  1.000 33.36317  ? 251 ASN A ND2 1 
ATOM   534  N  N   . LYS A 1 252 ? -2.95641  -10.64125 40.95455  1.000 31.65505  ? 252 LYS A N   1 
ATOM   535  C  CA  . LYS A 1 252 ? -1.68547  -10.45045 41.65758  1.000 28.96245  ? 252 LYS A CA  1 
ATOM   536  C  C   . LYS A 1 252 ? -0.61040  -11.46319 41.26208  1.000 29.41338  ? 252 LYS A C   1 
ATOM   537  O  O   . LYS A 1 252 ? 0.58022   -11.19667 41.48250  1.000 37.88546  ? 252 LYS A O   1 
ATOM   538  C  CB  . LYS A 1 252 ? -1.88977  -10.49940 43.17697  1.000 30.56343  ? 252 LYS A CB  1 
ATOM   539  C  CG  . LYS A 1 252 ? -3.06459  -9.71395  43.66163  1.000 47.86861  ? 252 LYS A CG  1 
ATOM   540  N  N   . ASN A 1 253 ? -0.98317  -12.60075 40.68292  1.000 26.81172  ? 253 ASN A N   1 
ATOM   541  C  CA  . ASN A 1 253 ? 0.00128   -13.55892 40.18794  1.000 29.52318  ? 253 ASN A CA  1 
ATOM   542  C  C   . ASN A 1 253 ? 0.36190   -13.35679 38.70892  1.000 31.44160  ? 253 ASN A C   1 
ATOM   543  O  O   . ASN A 1 253 ? 1.12024   -14.15689 38.15289  1.000 31.39129  ? 253 ASN A O   1 
ATOM   544  C  CB  . ASN A 1 253 ? -0.50542  -14.98107 40.37114  1.000 29.25138  ? 253 ASN A CB  1 
ATOM   545  C  CG  . ASN A 1 253 ? -0.54690  -15.39140 41.83794  1.000 42.85656  ? 253 ASN A CG  1 
ATOM   546  O  OD1 . ASN A 1 253 ? 0.28450   -14.95655 42.62811  1.000 41.63228  ? 253 ASN A OD1 1 
ATOM   547  N  ND2 . ASN A 1 253 ? -1.50398  -16.23194 42.19670  1.000 44.95877  ? 253 ASN A ND2 1 
ATOM   548  N  N   . GLY A 1 254 ? -0.14424  -12.31280 38.07341  1.000 26.55747  ? 254 GLY A N   1 
ATOM   549  C  CA  . GLY A 1 254 ? 0.07560   -12.12616 36.64565  1.000 24.87055  ? 254 GLY A CA  1 
ATOM   550  C  C   . GLY A 1 254 ? -0.77323  -12.98163 35.74175  1.000 22.85426  ? 254 GLY A C   1 
ATOM   551  O  O   . GLY A 1 254 ? -0.46679  -13.09496 34.53846  1.000 24.96468  ? 254 GLY A O   1 
ATOM   552  N  N   . VAL A 1 255 ? -1.84343  -13.58085 36.27215  1.000 26.24248  ? 255 VAL A N   1 
ATOM   553  C  CA  . VAL A 1 255 ? -2.73540  -14.44662 35.50728  1.000 23.38255  ? 255 VAL A CA  1 
ATOM   554  C  C   . VAL A 1 255 ? -3.82269  -13.58923 34.87803  1.000 22.29548  ? 255 VAL A C   1 
ATOM   555  O  O   . VAL A 1 255 ? -4.37746  -12.69201 35.52215  1.000 23.90393  ? 255 VAL A O   1 
ATOM   556  C  CB  . VAL A 1 255 ? -3.32916  -15.53876 36.43155  1.000 28.01662  ? 255 VAL A CB  1 
ATOM   557  C  CG1 . VAL A 1 255 ? -4.42715  -16.38809 35.73476  1.000 28.13635  ? 255 VAL A CG1 1 
ATOM   558  C  CG2 . VAL A 1 255 ? -2.20811  -16.42414 36.94308  1.000 32.25269  ? 255 VAL A CG2 1 
ATOM   559  N  N   . LEU A 1 256 ? -4.11390  -13.85441 33.60754  1.000 24.75229  ? 256 LEU A N   1 
ATOM   560  C  CA  . LEU A 1 256 ? -5.10575  -13.08542 32.87216  1.000 25.87915  ? 256 LEU A CA  1 
ATOM   561  C  C   . LEU A 1 256 ? -6.49737  -13.28665 33.46217  1.000 27.15416  ? 256 LEU A C   1 
ATOM   562  O  O   . LEU A 1 256 ? -6.93028  -14.42645 33.67719  1.000 27.95407  ? 256 LEU A O   1 
ATOM   563  C  CB  . LEU A 1 256 ? -5.08673  -13.53010 31.41065  1.000 24.06997  ? 256 LEU A CB  1 
ATOM   564  C  CG  . LEU A 1 256 ? -5.83187  -12.63752 30.43664  1.000 23.05073  ? 256 LEU A CG  1 
ATOM   565  C  CD1 . LEU A 1 256 ? -5.11699  -11.23882 30.28098  1.000 23.25639  ? 256 LEU A CD1 1 
ATOM   566  C  CD2 . LEU A 1 256 ? -5.99951  -13.33546 29.03885  1.000 21.40214  ? 256 LEU A CD2 1 
ATOM   567  N  N   . LEU A 1 257 ? -7.21696  -12.18941 33.69249  1.000 24.79491  ? 257 LEU A N   1 
ATOM   568  C  CA  . LEU A 1 257 ? -8.57207  -12.26092 34.25009  1.000 25.99044  ? 257 LEU A CA  1 
ATOM   569  C  C   . LEU A 1 257 ? -9.61053  -12.42068 33.14554  1.000 28.08638  ? 257 LEU A C   1 
ATOM   570  O  O   . LEU A 1 257 ? -9.46290  -11.89362 32.03256  1.000 28.27682  ? 257 LEU A O   1 
ATOM   571  C  CB  . LEU A 1 257 ? -8.87619  -11.00663 35.06162  1.000 25.17589  ? 257 LEU A CB  1 
ATOM   572  C  CG  . LEU A 1 257 ? -8.02448  -10.83129 36.31451  1.000 31.10023  ? 257 LEU A CG  1 
ATOM   573  C  CD1 . LEU A 1 257 ? -8.22181  -9.42872  36.84771  1.000 31.79503  ? 257 LEU A CD1 1 
ATOM   574  C  CD2 . LEU A 1 257 ? -8.47551  -11.84710 37.37893  1.000 34.72025  ? 257 LEU A CD2 1 
ATOM   575  N  N   . ASP A 1 258 ? -10.69467 -13.13331 33.48236  1.000 27.78671  ? 258 ASP A N   1 
ATOM   576  C  CA  . ASP A 1 258 ? -11.68678 -13.50569 32.48306  1.000 27.30171  ? 258 ASP A CA  1 
ATOM   577  C  C   . ASP A 1 258 ? -12.48991 -12.32705 31.95429  1.000 38.82263  ? 258 ASP A C   1 
ATOM   578  O  O   . ASP A 1 258 ? -13.14804 -12.47083 30.92162  1.000 36.15179  ? 258 ASP A O   1 
ATOM   579  C  CB  . ASP A 1 258 ? -12.65337 -14.56148 33.02515  1.000 30.67576  ? 258 ASP A CB  1 
ATOM   580  C  CG  . ASP A 1 258 ? -13.31150 -14.15714 34.35918  1.000 24.15622  ? 258 ASP A CG  1 
ATOM   581  O  OD1 . ASP A 1 258 ? -13.18301 -13.01279 34.81714  1.000 34.04384  ? 258 ASP A OD1 1 
ATOM   582  O  OD2 . ASP A 1 258 ? -13.97801 -15.03317 34.92508  1.000 38.77085  ? 258 ASP A OD2 1 
ATOM   583  N  N   . ASN A 1 259 ? -12.49452 -11.18145 32.62669  1.000 27.00701  ? 259 ASN A N   1 
ATOM   584  C  CA  . ASN A 1 259 ? -13.16989 -10.03606 32.03390  1.000 32.30313  ? 259 ASN A CA  1 
ATOM   585  C  C   . ASN A 1 259 ? -12.26707 -9.23676  31.09937  1.000 29.13638  ? 259 ASN A C   1 
ATOM   586  O  O   . ASN A 1 259 ? -12.69890 -8.19290  30.60171  1.000 30.09902  ? 259 ASN A O   1 
ATOM   587  C  CB  . ASN A 1 259 ? -13.77823 -9.12293  33.10802  1.000 43.17104  ? 259 ASN A CB  1 
ATOM   588  C  CG  . ASN A 1 259 ? -12.79747 -8.72313  34.17103  1.000 46.13596  ? 259 ASN A CG  1 
ATOM   589  O  OD1 . ASN A 1 259 ? -11.85279 -9.44796  34.46997  1.000 46.02527  ? 259 ASN A OD1 1 
ATOM   590  N  ND2 . ASN A 1 259 ? -13.03375 -7.56261  34.77615  1.000 44.31995  ? 259 ASN A ND2 1 
ATOM   591  N  N   . SER A 1 260 ? -11.05120 -9.71922  30.82046  1.000 22.56938  ? 260 SER A N   1 
ATOM   592  C  CA  . SER A 1 260 ? -10.24173 -9.14791  29.73753  1.000 19.33976  ? 260 SER A CA  1 
ATOM   593  C  C   . SER A 1 260 ? -10.91469 -9.39787  28.39437  1.000 32.84861  ? 260 SER A C   1 
ATOM   594  O  O   . SER A 1 260 ? -11.69657 -10.33101 28.23499  1.000 26.84666  ? 260 SER A O   1 
ATOM   595  C  CB  . SER A 1 260 ? -8.84361  -9.76613  29.69208  1.000 24.89505  ? 260 SER A CB  1 
ATOM   596  O  OG  . SER A 1 260 ? -8.19007  -9.68887  30.92901  1.000 24.34397  ? 260 SER A OG  1 
ATOM   597  N  N   . ASN A 1 261 ? -10.60043 -8.54493  27.41076  1.000 23.46179  ? 261 ASN A N   1 
ATOM   598  C  CA  . ASN A 1 261 ? -11.13552 -8.77921  26.07245  1.000 22.74375  ? 261 ASN A CA  1 
ATOM   599  C  C   . ASN A 1 261 ? -10.48699 -10.00081 25.44155  1.000 26.68323  ? 261 ASN A C   1 
ATOM   600  O  O   . ASN A 1 261 ? -11.13964 -10.74036 24.69488  1.000 24.08663  ? 261 ASN A O   1 
ATOM   601  C  CB  . ASN A 1 261 ? -10.94653 -7.52857  25.19103  1.000 21.08062  ? 261 ASN A CB  1 
ATOM   602  C  CG  . ASN A 1 261 ? -11.75467 -6.35991  25.66485  1.000 27.18994  ? 261 ASN A CG  1 
ATOM   603  O  OD1 . ASN A 1 261 ? -11.30202 -5.57864  26.49820  1.000 26.17892  ? 261 ASN A OD1 1 
ATOM   604  N  ND2 . ASN A 1 261 ? -12.98843 -6.23969  25.17236  1.000 30.20506  ? 261 ASN A ND2 1 
ATOM   605  N  N   . LEU A 1 262 ? -9.23271  -10.25167 25.77625  1.000 24.40783  ? 262 LEU A N   1 
ATOM   606  C  CA  . LEU A 1 262 ? -8.50677  -11.42927 25.32169  1.000 20.32578  ? 262 LEU A CA  1 
ATOM   607  C  C   . LEU A 1 262 ? -8.95738  -12.66213 26.08546  1.000 25.25309  ? 262 LEU A C   1 
ATOM   608  O  O   . LEU A 1 262 ? -9.07967  -12.63112 27.31324  1.000 22.75656  ? 262 LEU A O   1 
ATOM   609  C  CB  . LEU A 1 262 ? -7.00711  -11.23945 25.50565  1.000 19.84596  ? 262 LEU A CB  1 
ATOM   610  C  CG  . LEU A 1 262 ? -6.10130  -12.43893 25.16949  1.000 21.27495  ? 262 LEU A CG  1 
ATOM   611  C  CD1 . LEU A 1 262 ? -6.14535  -12.73480 23.66437  1.000 24.29030  ? 262 LEU A CD1 1 
ATOM   612  C  CD2 . LEU A 1 262 ? -4.65466  -12.17933 25.58849  1.000 22.10246  ? 262 LEU A CD2 1 
ATOM   613  N  N   . GLY A 1 263 ? -9.19325  -13.75244 25.35551  1.000 24.73874  ? 263 GLY A N   1 
ATOM   614  C  CA  . GLY A 1 263 ? -9.59900  -14.99354 25.98868  1.000 26.55813  ? 263 GLY A CA  1 
ATOM   615  C  C   . GLY A 1 263 ? -8.44870  -15.70607 26.67375  1.000 24.36183  ? 263 GLY A C   1 
ATOM   616  O  O   . GLY A 1 263 ? -7.29189  -15.68515 26.24572  1.000 25.19057  ? 263 GLY A O   1 
ATOM   617  N  N   . LYS A 1 264 ? -8.77842  -16.38703 27.76308  1.000 26.57250  ? 264 LYS A N   1 
ATOM   618  C  CA  . LYS A 1 264 ? -7.74280  -17.06047 28.53175  1.000 28.24151  ? 264 LYS A CA  1 
ATOM   619  C  C   . LYS A 1 264 ? -7.23080  -18.33287 27.87207  1.000 31.36294  ? 264 LYS A C   1 
ATOM   620  O  O   . LYS A 1 264 ? -6.11090  -18.74948 28.17101  1.000 33.44163  ? 264 LYS A O   1 
ATOM   621  C  CB  . LYS A 1 264 ? -8.27529  -17.38352 29.93052  1.000 28.41222  ? 264 LYS A CB  1 
ATOM   622  C  CG  . LYS A 1 264 ? -8.38014  -16.12371 30.78922  1.000 34.64315  ? 264 LYS A CG  1 
ATOM   623  C  CD  . LYS A 1 264 ? -9.05283  -16.35648 32.12571  1.000 40.15041  ? 264 LYS A CD  1 
ATOM   624  C  CE  . LYS A 1 264 ? -8.40961  -17.46973 32.93431  1.000 33.89015  ? 264 LYS A CE  1 
ATOM   625  N  NZ  . LYS A 1 264 ? -7.00953  -17.19257 33.30902  1.000 33.81091  ? 264 LYS A NZ  1 
ATOM   626  N  N   . ALA A 1 265 ? -8.00623  -18.95765 26.98393  1.000 27.81322  ? 265 ALA A N   1 
ATOM   627  C  CA  . ALA A 1 265 ? -7.58995  -20.25681 26.45868  1.000 29.91638  ? 265 ALA A CA  1 
ATOM   628  C  C   . ALA A 1 265 ? -6.32179  -20.17437 25.64414  1.000 35.28084  ? 265 ALA A C   1 
ATOM   629  O  O   . ALA A 1 265 ? -5.59835  -21.16907 25.55226  1.000 38.05373  ? 265 ALA A O   1 
ATOM   630  C  CB  . ALA A 1 265 ? -8.68070  -20.85710 25.57044  1.000 41.23308  ? 265 ALA A CB  1 
ATOM   631  N  N   . TYR A 1 266 ? -6.03516  -18.99469 25.10519  1.000 38.25247  ? 266 TYR A N   1 
ATOM   632  C  CA  . TYR A 1 266 ? -5.06834  -18.75041 24.05011  1.000 47.44136  ? 266 TYR A CA  1 
ATOM   633  C  C   . TYR A 1 266 ? -3.77787  -18.11092 24.54205  1.000 36.67899  ? 266 TYR A C   1 
ATOM   634  O  O   . TYR A 1 266 ? -2.85986  -17.89625 23.74234  1.000 45.99584  ? 266 TYR A O   1 
ATOM   635  C  CB  . TYR A 1 266 ? -5.72759  -17.83258 23.01323  1.000 61.69485  ? 266 TYR A CB  1 
ATOM   636  C  CG  . TYR A 1 266 ? -7.12765  -18.28875 22.64845  1.000 53.59625  ? 266 TYR A CG  1 
ATOM   637  C  CD1 . TYR A 1 266 ? -7.32917  -19.25812 21.66949  1.000 49.80448  ? 266 TYR A CD1 1 
ATOM   638  C  CD2 . TYR A 1 266 ? -8.25190  -17.74076 23.28084  1.000 54.74221  ? 266 TYR A CD2 1 
ATOM   639  C  CE1 . TYR A 1 266 ? -8.60432  -19.68437 21.33558  1.000 58.33931  ? 266 TYR A CE1 1 
ATOM   640  C  CE2 . TYR A 1 266 ? -9.53495  -18.15811 22.95417  1.000 43.41612  ? 266 TYR A CE2 1 
ATOM   641  C  CZ  . TYR A 1 266 ? -9.70216  -19.13676 21.97516  1.000 68.21035  ? 266 TYR A CZ  1 
ATOM   642  O  OH  . TYR A 1 266 ? -10.96256 -19.57758 21.62700  1.000 62.93807  ? 266 TYR A OH  1 
ATOM   643  N  N   . TRP A 1 267 ? -3.68135  -17.81948 25.83231  1.000 25.02028  ? 267 TRP A N   1 
ATOM   644  C  CA  . TRP A 1 267 ? -2.66005  -16.94916 26.40127  1.000 23.86186  ? 267 TRP A CA  1 
ATOM   645  C  C   . TRP A 1 267 ? -1.81176  -17.75839 27.37354  1.000 26.79546  ? 267 TRP A C   1 
ATOM   646  O  O   . TRP A 1 267 ? -2.30374  -18.18349 28.43421  1.000 25.55808  ? 267 TRP A O   1 
ATOM   647  C  CB  . TRP A 1 267 ? -3.32868  -15.77775 27.10022  1.000 25.30302  ? 267 TRP A CB  1 
ATOM   648  C  CG  . TRP A 1 267 ? -2.40528  -14.87510 27.82662  1.000 23.51503  ? 267 TRP A CG  1 
ATOM   649  C  CD1 . TRP A 1 267 ? -2.24446  -14.76959 29.18800  1.000 26.37143  ? 267 TRP A CD1 1 
ATOM   650  C  CD2 . TRP A 1 267 ? -1.52434  -13.91774 27.24050  1.000 24.45684  ? 267 TRP A CD2 1 
ATOM   651  N  NE1 . TRP A 1 267 ? -1.30220  -13.79754 29.48003  1.000 25.49186  ? 267 TRP A NE1 1 
ATOM   652  C  CE2 . TRP A 1 267 ? -0.84713  -13.25982 28.29576  1.000 23.34076  ? 267 TRP A CE2 1 
ATOM   653  C  CE3 . TRP A 1 267 ? -1.22958  -13.56576 25.91881  1.000 21.66865  ? 267 TRP A CE3 1 
ATOM   654  C  CZ2 . TRP A 1 267 ? 0.10391   -12.25636 28.07085  1.000 24.62029  ? 267 TRP A CZ2 1 
ATOM   655  C  CZ3 . TRP A 1 267 ? -0.26579  -12.56767 25.68818  1.000 23.45212  ? 267 TRP A CZ3 1 
ATOM   656  C  CH2 . TRP A 1 267 ? 0.37112   -11.91478 26.76124  1.000 24.83661  ? 267 TRP A CH2 1 
ATOM   657  N  N   . ASN A 1 268 ? -0.55479  -18.00222 27.00867  1.000 24.92645  ? 268 ASN A N   1 
ATOM   658  C  CA  . ASN A 1 268 ? 0.27963   -18.89858 27.79824  1.000 24.70996  ? 268 ASN A CA  1 
ATOM   659  C  C   . ASN A 1 268 ? 1.73127   -18.77041 27.37119  1.000 24.81004  ? 268 ASN A C   1 
ATOM   660  O  O   . ASN A 1 268 ? 2.06679   -18.11279 26.37820  1.000 24.20354  ? 268 ASN A O   1 
ATOM   661  C  CB  . ASN A 1 268 ? -0.18658  -20.36080 27.66814  1.000 29.61031  ? 268 ASN A CB  1 
ATOM   662  C  CG  . ASN A 1 268 ? 0.15780   -21.20785 28.89185  1.000 28.27702  ? 268 ASN A CG  1 
ATOM   663  O  OD1 . ASN A 1 268 ? 0.95142   -20.81539 29.75527  1.000 28.94398  ? 268 ASN A OD1 1 
ATOM   664  N  ND2 . ASN A 1 268 ? -0.44331  -22.39161 28.96616  1.000 28.35826  ? 268 ASN A ND2 1 
ATOM   665  N  N   . PHE A 1 269 ? 2.59828   -19.45315 28.11304  1.000 26.14069  ? 269 PHE A N   1 
ATOM   666  C  CA  . PHE A 1 269 ? 3.98745   -19.54587 27.67452  1.000 27.14219  ? 269 PHE A CA  1 
ATOM   667  C  C   . PHE A 1 269 ? 4.10351   -20.34889 26.38723  1.000 26.99366  ? 269 PHE A C   1 
ATOM   668  O  O   . PHE A 1 269 ? 3.31000   -21.24187 26.11261  1.000 27.71407  ? 269 PHE A O   1 
ATOM   669  C  CB  . PHE A 1 269 ? 4.86377   -20.18481 28.76703  1.000 25.33625  ? 269 PHE A CB  1 
ATOM   670  C  CG  . PHE A 1 269 ? 5.05567   -19.27528 29.94340  1.000 35.30916  ? 269 PHE A CG  1 
ATOM   671  C  CD1 . PHE A 1 269 ? 5.96351   -18.22716 29.87252  1.000 41.13204  ? 269 PHE A CD1 1 
ATOM   672  C  CD2 . PHE A 1 269 ? 4.31769   -19.44525 31.09575  1.000 38.31548  ? 269 PHE A CD2 1 
ATOM   673  C  CE1 . PHE A 1 269 ? 6.11037   -17.34899 30.93609  1.000 41.25974  ? 269 PHE A CE1 1 
ATOM   674  C  CE2 . PHE A 1 269 ? 4.47097   -18.58060 32.16587  1.000 44.98626  ? 269 PHE A CE2 1 
ATOM   675  C  CZ  . PHE A 1 269 ? 5.37479   -17.53698 32.08516  1.000 36.14430  ? 269 PHE A CZ  1 
ATOM   676  N  N   . ARG A 1 270 ? 5.13386   -20.03220 25.60304  1.000 28.04022  ? 270 ARG A N   1 
ATOM   677  C  CA  . ARG A 1 270 ? 5.28234   -20.58150 24.26198  1.000 25.32056  ? 270 ARG A CA  1 
ATOM   678  C  C   . ARG A 1 270 ? 5.87040   -21.99122 24.33131  1.000 42.83694  ? 270 ARG A C   1 
ATOM   679  O  O   . ARG A 1 270 ? 6.72778   -22.27805 25.16795  1.000 31.52012  ? 270 ARG A O   1 
ATOM   680  C  CB  . ARG A 1 270 ? 6.19369   -19.64330 23.44809  1.000 26.10681  ? 270 ARG A CB  1 
ATOM   681  C  CG  . ARG A 1 270 ? 6.80289   -20.27642 22.24056  1.000 28.92570  ? 270 ARG A CG  1 
ATOM   682  C  CD  . ARG A 1 270 ? 7.54822   -19.24767 21.40483  1.000 35.40295  ? 270 ARG A CD  1 
ATOM   683  N  NE  . ARG A 1 270 ? 8.05871   -19.88724 20.20135  1.000 38.75362  ? 270 ARG A NE  1 
ATOM   684  C  CZ  . ARG A 1 270 ? 9.34122   -20.17207 20.00699  1.000 72.46020  ? 270 ARG A CZ  1 
ATOM   685  N  NH1 . ARG A 1 270 ? 10.24247  -19.85597 20.93616  1.000 64.79134  ? 270 ARG A NH1 1 
ATOM   686  N  NH2 . ARG A 1 270 ? 9.72284   -20.76080 18.88101  1.000 74.82934  ? 270 ARG A NH2 1 
ATOM   687  N  N   . SER A 1 271 ? 5.37384   -22.87847 23.46966  1.000 31.49544  ? 271 SER A N   1 
ATOM   688  C  CA  . SER A 1 271 ? 6.03681   -24.14717 23.18511  1.000 34.19584  ? 271 SER A CA  1 
ATOM   689  C  C   . SER A 1 271 ? 5.95128   -24.35474 21.68015  1.000 35.69845  ? 271 SER A C   1 
ATOM   690  O  O   . SER A 1 271 ? 4.86894   -24.63268 21.15093  1.000 35.63353  ? 271 SER A O   1 
ATOM   691  C  CB  . SER A 1 271 ? 5.39558   -25.30565 23.94588  1.000 45.00056  ? 271 SER A CB  1 
ATOM   692  O  OG  . SER A 1 271 ? 6.03388   -26.51847 23.59068  1.000 40.14570  ? 271 SER A OG  1 
ATOM   693  N  N   . GLY A 1 272 ? 7.07542   -24.19203 20.98772  1.000 41.61995  ? 272 GLY A N   1 
ATOM   694  C  CA  . GLY A 1 272 ? 7.04301   -24.30570 19.53617  1.000 35.86530  ? 272 GLY A CA  1 
ATOM   695  C  C   . GLY A 1 272 ? 6.20524   -23.18798 18.95131  1.000 38.53153  ? 272 GLY A C   1 
ATOM   696  O  O   . GLY A 1 272 ? 6.36380   -22.01993 19.31590  1.000 38.19828  ? 272 GLY A O   1 
ATOM   697  N  N   . ASN A 1 273 ? 5.28929   -23.53083 18.04489  1.000 36.69660  ? 273 ASN A N   1 
ATOM   698  C  CA  . ASN A 1 273 ? 4.33081   -22.56163 17.52565  1.000 34.90797  ? 273 ASN A CA  1 
ATOM   699  C  C   . ASN A 1 273 ? 3.00915   -22.60151 18.26652  1.000 48.88654  ? 273 ASN A C   1 
ATOM   700  O  O   . ASN A 1 273 ? 2.03319   -21.98569 17.82242  1.000 41.90335  ? 273 ASN A O   1 
ATOM   701  C  CB  . ASN A 1 273 ? 4.09833   -22.77432 16.03044  1.000 43.68795  ? 273 ASN A CB  1 
ATOM   702  C  CG  . ASN A 1 273 ? 5.18487   -22.14982 15.18908  1.000 41.73738  ? 273 ASN A CG  1 
ATOM   703  O  OD1 . ASN A 1 273 ? 5.90052   -21.25944 15.64399  1.000 40.76466  ? 273 ASN A OD1 1 
ATOM   704  N  ND2 . ASN A 1 273 ? 5.30066   -22.59703 13.94953  1.000 62.38852  ? 273 ASN A ND2 1 
ATOM   705  N  N   . SER A 1 274 ? 2.97132   -23.28732 19.40285  1.000 38.28062  ? 274 SER A N   1 
ATOM   706  C  CA  . SER A 1 274 ? 1.78134   -23.39211 20.22958  1.000 33.61617  ? 274 SER A CA  1 
ATOM   707  C  C   . SER A 1 274 ? 2.12094   -22.91828 21.63522  1.000 34.15091  ? 274 SER A C   1 
ATOM   708  O  O   . SER A 1 274 ? 3.08129   -22.16278 21.83071  1.000 32.50719  ? 274 SER A O   1 
ATOM   709  C  CB  . SER A 1 274 ? 1.25521   -24.83570 20.26081  1.000 40.33970  ? 274 SER A CB  1 
ATOM   710  O  OG  . SER A 1 274 ? -0.00102  -24.88670 20.91069  1.000 52.40421  ? 274 SER A OG  1 
ATOM   711  N  N   . ASN A 1 275 ? 1.35310   -23.38633 22.61120  1.000 32.67776  ? 275 ASN A N   1 
ATOM   712  C  CA  . ASN A 1 275 ? 1.51006   -23.05454 24.01900  1.000 37.69916  ? 275 ASN A CA  1 
ATOM   713  C  C   . ASN A 1 275 ? 1.89907   -24.28757 24.81195  1.000 30.98847  ? 275 ASN A C   1 
ATOM   714  O  O   . ASN A 1 275 ? 1.61721   -25.42658 24.41839  1.000 35.61699  ? 275 ASN A O   1 
ATOM   715  C  CB  . ASN A 1 275 ? 0.20397   -22.50663 24.61919  1.000 34.77713  ? 275 ASN A CB  1 
ATOM   716  C  CG  . ASN A 1 275 ? -0.14033  -21.14017 24.11362  1.000 37.43280  ? 275 ASN A CG  1 
ATOM   717  O  OD1 . ASN A 1 275 ? 0.73063   -20.40281 23.65522  1.000 39.31525  ? 275 ASN A OD1 1 
ATOM   718  N  ND2 . ASN A 1 275 ? -1.42375  -20.78560 24.19214  1.000 35.70080  ? 275 ASN A ND2 1 
ATOM   719  N  N   . VAL A 1 276 ? 2.49810   -24.04526 25.98117  1.000 32.06465  ? 276 VAL A N   1 
ATOM   720  C  CA  . VAL A 1 276 ? 2.68181   -25.14774 26.91001  1.000 31.48516  ? 276 VAL A CA  1 
ATOM   721  C  C   . VAL A 1 276 ? 1.30683   -25.72207 27.27851  1.000 30.27104  ? 276 VAL A C   1 
ATOM   722  O  O   . VAL A 1 276 ? 0.26744   -25.06240 27.15697  1.000 38.13248  ? 276 VAL A O   1 
ATOM   723  C  CB  . VAL A 1 276 ? 3.46207   -24.69982 28.15321  1.000 34.42349  ? 276 VAL A CB  1 
ATOM   724  C  CG1 . VAL A 1 276 ? 4.85327   -24.15407 27.74203  1.000 34.83848  ? 276 VAL A CG1 1 
ATOM   725  C  CG2 . VAL A 1 276 ? 2.69697   -23.65396 28.90852  1.000 36.65551  ? 276 VAL A CG2 1 
ATOM   726  N  N   . SER A 1 277 ? 1.31432   -26.97577 27.73032  1.000 34.14961  ? 277 SER A N   1 
ATOM   727  C  CA  . SER A 1 277 ? 0.07236   -27.73915 27.81525  1.000 48.09311  ? 277 SER A CA  1 
ATOM   728  C  C   . SER A 1 277 ? -0.82892  -27.28276 28.95804  1.000 46.97732  ? 277 SER A C   1 
ATOM   729  O  O   . SER A 1 277 ? -2.05279  -27.33656 28.82391  1.000 61.66669  ? 277 SER A O   1 
ATOM   730  C  CB  . SER A 1 277 ? 0.38946   -29.23019 27.94876  1.000 53.33105  ? 277 SER A CB  1 
ATOM   731  O  OG  . SER A 1 277 ? 1.32104   -29.47958 28.99444  1.000 72.83854  ? 277 SER A OG  1 
ATOM   732  N  N   . THR A 1 278 ? -0.26611  -26.82024 30.06834  1.000 35.99986  ? 278 THR A N   1 
ATOM   733  C  CA  . THR A 1 278 ? -1.05390  -26.43174 31.22883  1.000 35.42409  ? 278 THR A CA  1 
ATOM   734  C  C   . THR A 1 278 ? -1.01566  -24.91942 31.42898  1.000 35.83479  ? 278 THR A C   1 
ATOM   735  O  O   . THR A 1 278 ? -0.00403  -24.26660 31.15599  1.000 29.23888  ? 278 THR A O   1 
ATOM   736  C  CB  . THR A 1 278 ? -0.55555  -27.14831 32.47721  1.000 39.52475  ? 278 THR A CB  1 
ATOM   737  O  OG1 . THR A 1 278 ? 0.80817   -26.79752 32.70434  1.000 52.54941  ? 278 THR A OG1 1 
ATOM   738  C  CG2 . THR A 1 278 ? -0.65718  -28.65353 32.27223  1.000 41.71133  ? 278 THR A CG2 1 
ATOM   739  N  N   . ALA A 1 279 ? -2.13177  -24.36576 31.89778  1.000 30.84387  ? 279 ALA A N   1 
ATOM   740  C  CA  . ALA A 1 279 ? -2.22234  -22.92507 32.09187  1.000 30.84715  ? 279 ALA A CA  1 
ATOM   741  C  C   . ALA A 1 279 ? -1.24701  -22.47551 33.17086  1.000 33.54921  ? 279 ALA A C   1 
ATOM   742  O  O   . ALA A 1 279 ? -1.10878  -23.11764 34.20601  1.000 37.19850  ? 279 ALA A O   1 
ATOM   743  C  CB  . ALA A 1 279 ? -3.65332  -22.53352 32.46076  1.000 41.29340  ? 279 ALA A CB  1 
ATOM   744  N  N   . TYR A 1 280 ? -0.55325  -21.37081 32.93010  1.000 30.04424  ? 280 TYR A N   1 
ATOM   745  C  CA  . TYR A 1 280 ? 0.46945   -20.95029 33.87587  1.000 28.48201  ? 280 TYR A CA  1 
ATOM   746  C  C   . TYR A 1 280 ? -0.14199  -20.45805 35.18491  1.000 29.31899  ? 280 TYR A C   1 
ATOM   747  O  O   . TYR A 1 280 ? -1.27939  -19.97722 35.22990  1.000 33.45988  ? 280 TYR A O   1 
ATOM   748  C  CB  . TYR A 1 280 ? 1.35133   -19.85583 33.26870  1.000 33.07509  ? 280 TYR A CB  1 
ATOM   749  C  CG  . TYR A 1 280 ? 0.74109   -18.45827 33.06872  1.000 32.35296  ? 280 TYR A CG  1 
ATOM   750  C  CD1 . TYR A 1 280 ? 0.75356   -17.50587 34.08132  1.000 30.36541  ? 280 TYR A CD1 1 
ATOM   751  C  CD2 . TYR A 1 280 ? 0.25552   -18.06139 31.81828  1.000 25.35089  ? 280 TYR A CD2 1 
ATOM   752  C  CE1 . TYR A 1 280 ? 0.23909   -16.20364 33.87391  1.000 27.90153  ? 280 TYR A CE1 1 
ATOM   753  C  CE2 . TYR A 1 280 ? -0.26059  -16.76838 31.59503  1.000 32.60676  ? 280 TYR A CE2 1 
ATOM   754  C  CZ  . TYR A 1 280 ? -0.26235  -15.83665 32.61378  1.000 32.03815  ? 280 TYR A CZ  1 
ATOM   755  O  OH  . TYR A 1 280 ? -0.76679  -14.54147 32.37182  1.000 25.73207  ? 280 TYR A OH  1 
ATOM   756  N  N   . GLU A 1 281 ? 0.63989   -20.57068 36.25936  1.000 35.80611  ? 281 GLU A N   1 
ATOM   757  C  CA  . GLU A 1 281 ? 0.16118   -20.11229 37.55793  1.000 41.80662  ? 281 GLU A CA  1 
ATOM   758  C  C   . GLU A 1 281 ? 0.76273   -18.77960 37.99568  1.000 37.90513  ? 281 GLU A C   1 
ATOM   759  O  O   . GLU A 1 281 ? 0.13381   -18.07476 38.79272  1.000 38.22357  ? 281 GLU A O   1 
ATOM   760  C  CB  . GLU A 1 281 ? 0.42760   -21.18106 38.62962  1.000 43.04967  ? 281 GLU A CB  1 
ATOM   761  C  CG  . GLU A 1 281 ? -0.42891  -22.44328 38.45254  1.000 53.87232  ? 281 GLU A CG  1 
ATOM   762  C  CD  . GLU A 1 281 ? -0.12138  -23.54117 39.47007  1.000 73.34680  ? 281 GLU A CD  1 
ATOM   763  O  OE1 . GLU A 1 281 ? 1.03348   -23.62436 39.94735  1.000 68.60753  ? 281 GLU A OE1 1 
ATOM   764  O  OE2 . GLU A 1 281 ? -1.04316  -24.32379 39.79012  1.000 78.48331  ? 281 GLU A OE2 1 
ATOM   765  N  N   . LYS A 1 282 ? 1.94163   -18.40929 37.48841  1.000 34.83316  ? 282 LYS A N   1 
ATOM   766  C  CA  . LYS A 1 282 ? 2.62503   -17.17483 37.86999  1.000 44.03616  ? 282 LYS A CA  1 
ATOM   767  C  C   . LYS A 1 282 ? 3.32157   -16.56391 36.66491  1.000 37.85319  ? 282 LYS A C   1 
ATOM   768  O  O   . LYS A 1 282 ? 3.95876   -17.28310 35.89295  1.000 33.44890  ? 282 LYS A O   1 
ATOM   769  C  CB  . LYS A 1 282 ? 3.67965   -17.41955 38.95482  1.000 35.62548  ? 282 LYS A CB  1 
ATOM   770  C  CG  . LYS A 1 282 ? 3.11198   -17.70518 40.34406  1.000 54.22839  ? 282 LYS A CG  1 
ATOM   771  C  CD  . LYS A 1 282 ? 2.97855   -16.43691 41.17219  1.000 72.12895  ? 282 LYS A CD  1 
ATOM   772  N  N   . ALA A 1 283 ? 3.20310   -15.23821 36.50552  1.000 29.86278  ? 283 ALA A N   1 
ATOM   773  C  CA  . ALA A 1 283 ? 3.94313   -14.54593 35.44741  1.000 29.25995  ? 283 ALA A CA  1 
ATOM   774  C  C   . ALA A 1 283 ? 4.24572   -13.11866 35.87111  1.000 29.05273  ? 283 ALA A C   1 
ATOM   775  O  O   . ALA A 1 283 ? 4.09824   -12.18118 35.08310  1.000 27.13765  ? 283 ALA A O   1 
ATOM   776  C  CB  . ALA A 1 283 ? 3.17832   -14.55016 34.12299  1.000 28.70620  ? 283 ALA A CB  1 
ATOM   777  N  N   . ILE A 1 284 ? 4.62418   -12.93038 37.14016  1.000 26.80250  ? 284 ILE A N   1 
ATOM   778  C  CA  . ILE A 1 284 ? 4.85323   -11.57143 37.63721  1.000 26.36875  ? 284 ILE A CA  1 
ATOM   779  C  C   . ILE A 1 284 ? 6.00668   -10.90494 36.89766  1.000 27.20093  ? 284 ILE A C   1 
ATOM   780  O  O   . ILE A 1 284 ? 6.04566   -9.67758  36.76552  1.000 28.71236  ? 284 ILE A O   1 
ATOM   781  C  CB  . ILE A 1 284 ? 5.07033   -11.60213 39.17155  1.000 33.14424  ? 284 ILE A CB  1 
ATOM   782  C  CG1 . ILE A 1 284 ? 3.78826   -12.06094 39.86511  1.000 31.65289  ? 284 ILE A CG1 1 
ATOM   783  C  CG2 . ILE A 1 284 ? 5.45146   -10.24676 39.71734  1.000 37.67083  ? 284 ILE A CG2 1 
ATOM   784  C  CD1 . ILE A 1 284 ? 3.90542   -12.22289 41.39769  1.000 35.78717  ? 284 ILE A CD1 1 
ATOM   785  N  N   . GLY A 1 285 ? 6.96454   -11.69058 36.41700  1.000 28.67925  ? 285 GLY A N   1 
ATOM   786  C  CA  . GLY A 1 285 ? 8.08517   -11.14093 35.69840  1.000 28.44076  ? 285 GLY A CA  1 
ATOM   787  C  C   . GLY A 1 285 ? 7.72377   -10.50706 34.37369  1.000 28.57650  ? 285 GLY A C   1 
ATOM   788  O  O   . GLY A 1 285 ? 8.57561   -9.83610  33.78851  1.000 24.83163  ? 285 GLY A O   1 
ATOM   789  N  N   . PHE A 1 286 ? 6.49941   -10.71008 33.89287  1.000 22.80347  ? 286 PHE A N   1 
ATOM   790  C  CA  . PHE A 1 286 ? 6.03055   -10.10544 32.63811  1.000 24.45755  ? 286 PHE A CA  1 
ATOM   791  C  C   . PHE A 1 286 ? 5.08674   -8.92826  32.86128  1.000 20.80277  ? 286 PHE A C   1 
ATOM   792  O  O   . PHE A 1 286 ? 4.59742   -8.34645  31.89249  1.000 20.81158  ? 286 PHE A O   1 
ATOM   793  C  CB  . PHE A 1 286 ? 5.30132   -11.16089 31.79827  1.000 23.48605  ? 286 PHE A CB  1 
ATOM   794  C  CG  . PHE A 1 286 ? 6.19656   -12.20722 31.25652  1.000 23.70512  ? 286 PHE A CG  1 
ATOM   795  C  CD1 . PHE A 1 286 ? 6.63366   -13.25926 32.05309  1.000 28.46492  ? 286 PHE A CD1 1 
ATOM   796  C  CD2 . PHE A 1 286 ? 6.61072   -12.13249 29.93953  1.000 27.22989  ? 286 PHE A CD2 1 
ATOM   797  C  CE1 . PHE A 1 286 ? 7.48434   -14.23557 31.53039  1.000 28.80140  ? 286 PHE A CE1 1 
ATOM   798  C  CE2 . PHE A 1 286 ? 7.44891   -13.10596 29.41707  1.000 26.34499  ? 286 PHE A CE2 1 
ATOM   799  C  CZ  . PHE A 1 286 ? 7.88264   -14.15059 30.19774  1.000 25.27609  ? 286 PHE A CZ  1 
ATOM   800  N  N   . MET A 1 287 ? 4.76501   -8.60964  34.11376  1.000 22.50756  ? 287 MET A N   1 
ATOM   801  C  CA  . MET A 1 287 ? 3.80073   -7.55172  34.39594  1.000 19.83562  ? 287 MET A CA  1 
ATOM   802  C  C   . MET A 1 287 ? 4.44821   -6.17241  34.32402  1.000 23.32392  ? 287 MET A C   1 
ATOM   803  O  O   . MET A 1 287 ? 5.65799   -6.03267  34.53879  1.000 23.44841  ? 287 MET A O   1 
ATOM   804  C  CB  . MET A 1 287 ? 3.20044   -7.76365  35.78957  1.000 22.35117  ? 287 MET A CB  1 
ATOM   805  C  CG  . MET A 1 287 ? 2.37531   -9.06222  35.88135  1.000 24.85882  ? 287 MET A CG  1 
ATOM   806  S  SD  . MET A 1 287 ? 0.94913   -9.03222  34.80609  1.000 24.58051  ? 287 MET A SD  1 
ATOM   807  C  CE  . MET A 1 287 ? 1.41204   -10.17680 33.49111  1.000 27.46833  ? 287 MET A CE  1 
ATOM   808  N  N   . PRO A 1 288 ? 3.68298   -5.13775  33.95271  1.000 21.01040  ? 288 PRO A N   1 
ATOM   809  C  CA  . PRO A 1 288 ? 4.24073   -3.76958  33.94742  1.000 19.13725  ? 288 PRO A CA  1 
ATOM   810  C  C   . PRO A 1 288 ? 4.53985   -3.29569  35.36823  1.000 22.10776  ? 288 PRO A C   1 
ATOM   811  O  O   . PRO A 1 288 ? 3.73304   -3.45966  36.28249  1.000 24.82825  ? 288 PRO A O   1 
ATOM   812  C  CB  . PRO A 1 288 ? 3.13660   -2.91969  33.28696  1.000 23.38133  ? 288 PRO A CB  1 
ATOM   813  C  CG  . PRO A 1 288 ? 2.19196   -3.91965  32.64525  1.000 26.70903  ? 288 PRO A CG  1 
ATOM   814  C  CD  . PRO A 1 288 ? 2.29168   -5.18388  33.46460  1.000 21.56858  ? 288 PRO A CD  1 
ATOM   815  N  N   . ASN A 1 289 ? 5.73113   -2.73534  35.53511  1.000 24.09719  ? 289 ASN A N   1 
ATOM   816  C  CA  . ASN A 1 289 ? 6.24896   -2.34084  36.84110  1.000 24.50970  ? 289 ASN A CA  1 
ATOM   817  C  C   . ASN A 1 289 ? 5.34790   -1.29106  37.49546  1.000 20.68190  ? 289 ASN A C   1 
ATOM   818  O  O   . ASN A 1 289 ? 5.03229   -0.25541  36.88878  1.000 24.68935  ? 289 ASN A O   1 
ATOM   819  C  CB  . ASN A 1 289 ? 7.67187   -1.79889  36.62908  1.000 23.28153  ? 289 ASN A CB  1 
ATOM   820  C  CG  . ASN A 1 289 ? 8.37752   -1.46892  37.91701  1.000 29.68927  ? 289 ASN A CG  1 
ATOM   821  O  OD1 . ASN A 1 289 ? 8.10572   -0.43492  38.50961  1.000 26.32583  ? 289 ASN A OD1 1 
ATOM   822  N  ND2 . ASN A 1 289 ? 9.31077   -2.32997  38.33391  1.000 27.45334  ? 289 ASN A ND2 1 
ATOM   823  N  N   . LEU A 1 290 ? 4.96600   -1.54793  38.75906  1.000 20.55957  ? 290 LEU A N   1 
ATOM   824  C  CA  . LEU A 1 290 ? 4.00341   -0.69349  39.43759  1.000 29.74917  ? 290 LEU A CA  1 
ATOM   825  C  C   . LEU A 1 290 ? 4.62171   0.60125   39.95577  1.000 27.73295  ? 290 LEU A C   1 
ATOM   826  O  O   . LEU A 1 290 ? 3.89251   1.57382   40.15239  1.000 30.99987  ? 290 LEU A O   1 
ATOM   827  C  CB  . LEU A 1 290 ? 3.35464   -1.47766  40.58724  1.000 28.90911  ? 290 LEU A CB  1 
ATOM   828  C  CG  . LEU A 1 290 ? 2.23905   -2.44902  40.15796  1.000 26.70876  ? 290 LEU A CG  1 
ATOM   829  C  CD1 . LEU A 1 290 ? 1.92500   -3.45084  41.27297  1.000 35.45806  ? 290 LEU A CD1 1 
ATOM   830  C  CD2 . LEU A 1 290 ? 0.94732   -1.68538  39.78163  1.000 25.86462  ? 290 LEU A CD2 1 
ATOM   831  N  N   . VAL A 1 291 ? 5.94502   0.65475   40.14263  1.000 27.46601  ? 291 VAL A N   1 
ATOM   832  C  CA  . VAL A 1 291 ? 6.56271   1.93903   40.46004  1.000 26.50456  ? 291 VAL A CA  1 
ATOM   833  C  C   . VAL A 1 291 ? 6.67237   2.80133   39.20895  1.000 29.62474  ? 291 VAL A C   1 
ATOM   834  O  O   . VAL A 1 291 ? 6.38509   4.00492   39.24882  1.000 28.64980  ? 291 VAL A O   1 
ATOM   835  C  CB  . VAL A 1 291 ? 7.92107   1.72359   41.15789  1.000 36.61518  ? 291 VAL A CB  1 
ATOM   836  C  CG1 . VAL A 1 291 ? 8.63416   3.05728   41.36443  1.000 33.08712  ? 291 VAL A CG1 1 
ATOM   837  C  CG2 . VAL A 1 291 ? 7.70812   1.02997   42.48697  1.000 35.43458  ? 291 VAL A CG2 1 
ATOM   838  N  N   . ALA A 1 292 ? 7.06527   2.20926   38.06875  1.000 26.75701  ? 292 ALA A N   1 
ATOM   839  C  CA  . ALA A 1 292 ? 7.11874   2.98093   36.82211  1.000 27.19958  ? 292 ALA A CA  1 
ATOM   840  C  C   . ALA A 1 292 ? 5.72840   3.40962   36.38355  1.000 24.81100  ? 292 ALA A C   1 
ATOM   841  O  O   . ALA A 1 292 ? 5.53079   4.54356   35.92369  1.000 24.62635  ? 292 ALA A O   1 
ATOM   842  C  CB  . ALA A 1 292 ? 7.78294   2.16290   35.71280  1.000 26.60982  ? 292 ALA A CB  1 
ATOM   843  N  N   . TYR A 1 293 ? 4.74370   2.52807   36.56431  1.000 22.57800  ? 293 TYR A N   1 
ATOM   844  C  CA  . TYR A 1 293 ? 3.39054   2.71394   36.04650  1.000 20.58348  ? 293 TYR A CA  1 
ATOM   845  C  C   . TYR A 1 293 ? 2.41426   2.44003   37.18463  1.000 21.33879  ? 293 TYR A C   1 
ATOM   846  O  O   . TYR A 1 293 ? 1.89314   1.31929   37.32204  1.000 24.49820  ? 293 TYR A O   1 
ATOM   847  C  CB  . TYR A 1 293 ? 3.11224   1.77129   34.87245  1.000 20.17729  ? 293 TYR A CB  1 
ATOM   848  C  CG  . TYR A 1 293 ? 4.27319   1.59654   33.90171  1.000 19.19016  ? 293 TYR A CG  1 
ATOM   849  C  CD1 . TYR A 1 293 ? 4.79513   2.68167   33.19894  1.000 20.54410  ? 293 TYR A CD1 1 
ATOM   850  C  CD2 . TYR A 1 293 ? 4.84368   0.33992   33.69905  1.000 20.42292  ? 293 TYR A CD2 1 
ATOM   851  C  CE1 . TYR A 1 293 ? 5.87582   2.53670   32.32207  1.000 21.64605  ? 293 TYR A CE1 1 
ATOM   852  C  CE2 . TYR A 1 293 ? 5.90853   0.17154   32.83037  1.000 22.47937  ? 293 TYR A CE2 1 
ATOM   853  C  CZ  . TYR A 1 293 ? 6.42138   1.26691   32.14275  1.000 23.07364  ? 293 TYR A CZ  1 
ATOM   854  O  OH  . TYR A 1 293 ? 7.48564   1.05677   31.26076  1.000 22.16482  ? 293 TYR A OH  1 
ATOM   855  N  N   . PRO A 1 294 ? 2.15556   3.43348   38.03038  1.000 25.44596  ? 294 PRO A N   1 
ATOM   856  C  CA  . PRO A 1 294 ? 1.30779   3.20801   39.21239  1.000 29.09011  ? 294 PRO A CA  1 
ATOM   857  C  C   . PRO A 1 294 ? -0.17151  3.04012   38.87653  1.000 24.34995  ? 294 PRO A C   1 
ATOM   858  O  O   . PRO A 1 294 ? -0.66579  3.54862   37.87474  1.000 27.69191  ? 294 PRO A O   1 
ATOM   859  C  CB  . PRO A 1 294 ? 1.51961   4.46958   40.05462  1.000 34.00145  ? 294 PRO A CB  1 
ATOM   860  C  CG  . PRO A 1 294 ? 2.79114   5.07755   39.53994  1.000 31.34315  ? 294 PRO A CG  1 
ATOM   861  C  CD  . PRO A 1 294 ? 2.86067   4.72791   38.07689  1.000 25.54371  ? 294 PRO A CD  1 
ATOM   862  N  N   . LYS A 1 295 ? -0.87868  2.34243   39.77479  1.000 28.65525  ? 295 LYS A N   1 
ATOM   863  C  CA  . LYS A 1 295 ? -2.33987  2.16808   39.63085  1.000 35.18520  ? 295 LYS A CA  1 
ATOM   864  C  C   . LYS A 1 295 ? -3.09989  3.49566   39.69165  1.000 34.07636  ? 295 LYS A C   1 
ATOM   865  O  O   . LYS A 1 295 ? -2.56635  4.51601   40.13445  1.000 35.11564  ? 295 LYS A O   1 
ATOM   866  C  CB  . LYS A 1 295 ? -2.88109  1.20941   40.69240  1.000 33.68909  ? 295 LYS A CB  1 
ATOM   867  C  CG  . LYS A 1 295 ? -2.42722  -0.22393  40.51080  1.000 34.28116  ? 295 LYS A CG  1 
ATOM   868  C  CD  . LYS A 1 295 ? -2.75175  -0.70309  39.07941  1.000 55.26159  ? 295 LYS A CD  1 
ATOM   869  C  CE  . LYS A 1 295 ? -3.80142  -1.83432  38.99524  1.000 62.20627  ? 295 LYS A CE  1 
ATOM   870  N  NZ  . LYS A 1 295 ? -5.21058  -1.53431  39.43059  1.000 47.87186  ? 295 LYS A NZ  1 
ATOM   871  N  N   . PRO A 1 296 ? -4.34779  3.51698   39.19677  1.000 36.04771  ? 296 PRO A N   1 
ATOM   872  C  CA  . PRO A 1 296 ? -5.10732  4.78355   39.15898  1.000 34.99774  ? 296 PRO A CA  1 
ATOM   873  C  C   . PRO A 1 296 ? -5.33948  5.40856   40.52050  1.000 55.17734  ? 296 PRO A C   1 
ATOM   874  O  O   . PRO A 1 296 ? -5.73883  6.57801   40.58735  1.000 41.21016  ? 296 PRO A O   1 
ATOM   875  C  CB  . PRO A 1 296 ? -6.44063  4.38486   38.50520  1.000 44.98556  ? 296 PRO A CB  1 
ATOM   876  C  CG  . PRO A 1 296 ? -6.11856  3.16185   37.72945  1.000 41.79548  ? 296 PRO A CG  1 
ATOM   877  C  CD  . PRO A 1 296 ? -5.06364  2.43197   38.49635  1.000 34.09211  ? 296 PRO A CD  1 
ATOM   878  N  N   . SER A 1 297 ? -5.09911  4.68658   41.60555  1.000 30.21282  ? 297 SER A N   1 
ATOM   879  C  CA  . SER A 1 297 ? -5.28147  5.31897   42.90724  1.000 35.41460  ? 297 SER A CA  1 
ATOM   880  C  C   . SER A 1 297 ? -4.16397  6.31005   43.20879  1.000 40.74881  ? 297 SER A C   1 
ATOM   881  O  O   . SER A 1 297 ? -4.29797  7.11755   44.13353  1.000 44.08099  ? 297 SER A O   1 
ATOM   882  C  CB  . SER A 1 297 ? -5.37579  4.24443   43.98980  1.000 41.32616  ? 297 SER A CB  1 
ATOM   883  O  OG  . SER A 1 297 ? -4.34023  3.29703   43.82901  1.000 54.99089  ? 297 SER A OG  1 
ATOM   884  N  N   . ASN A 1 298 ? -3.09204  6.28751   42.41309  1.000 43.39545  ? 298 ASN A N   1 
ATOM   885  C  CA  . ASN A 1 298 ? -1.91606  7.12749   42.62963  1.000 55.30524  ? 298 ASN A CA  1 
ATOM   886  C  C   . ASN A 1 298 ? -2.28470  8.60753   42.68678  1.000 63.70506  ? 298 ASN A C   1 
ATOM   887  O  O   . ASN A 1 298 ? -3.21340  9.06340   42.01285  1.000 64.49337  ? 298 ASN A O   1 
ATOM   888  C  CB  . ASN A 1 298 ? -0.89700  6.89666   41.49940  1.000 37.68795  ? 298 ASN A CB  1 
ATOM   889  C  CG  . ASN A 1 298 ? 0.53265   7.21785   41.92270  1.000 56.49864  ? 298 ASN A CG  1 
ATOM   890  O  OD1 . ASN A 1 298 ? 0.98845   6.80039   42.99423  1.000 57.66406  ? 298 ASN A OD1 1 
ATOM   891  N  ND2 . ASN A 1 298 ? 1.24262   7.96906   41.08789  1.000 41.43599  ? 298 ASN A ND2 1 
ATOM   892  N  N   . SER A 1 299 ? -1.52652  9.35777   43.49910  1.000 56.14093  ? 299 SER A N   1 
ATOM   893  C  CA  . SER A 1 299 ? -1.67935  10.80910  43.58144  1.000 48.76973  ? 299 SER A CA  1 
ATOM   894  C  C   . SER A 1 299 ? -1.71234  11.45864  42.20032  1.000 61.15111  ? 299 SER A C   1 
ATOM   895  O  O   . SER A 1 299 ? -2.62554  12.22840  41.87323  1.000 52.24690  ? 299 SER A O   1 
ATOM   896  C  CB  . SER A 1 299 ? -0.52257  11.39839  44.39099  1.000 60.19403  ? 299 SER A CB  1 
ATOM   897  N  N   . LYS A 1 300 ? -0.70332  11.16571  41.39096  1.000 32.73494  ? 300 LYS A N   1 
ATOM   898  C  CA  . LYS A 1 300 ? -0.48348  11.77823  40.08473  1.000 44.32924  ? 300 LYS A CA  1 
ATOM   899  C  C   . LYS A 1 300 ? -0.43148  10.69081  39.02328  1.000 52.84560  ? 300 LYS A C   1 
ATOM   900  O  O   . LYS A 1 300 ? 0.15970   9.62972   39.24928  1.000 39.85497  ? 300 LYS A O   1 
ATOM   901  C  CB  . LYS A 1 300 ? 0.81724   12.59381  40.07402  1.000 46.36364  ? 300 LYS A CB  1 
ATOM   902  C  CG  . LYS A 1 300 ? 1.20209   13.22528  38.72369  1.000 51.17549  ? 300 LYS A CG  1 
ATOM   903  C  CD  . LYS A 1 300 ? 0.05365   13.93298  38.03054  1.000 65.95071  ? 300 LYS A CD  1 
ATOM   904  C  CE  . LYS A 1 300 ? 0.55579   15.06303  37.12922  1.000 70.31493  ? 300 LYS A CE  1 
ATOM   905  N  NZ  . LYS A 1 300 ? 1.52053   14.60507  36.11202  1.000 57.37553  ? 300 LYS A NZ  1 
ATOM   906  N  N   . LYS A 1 301 ? -1.10849  10.92630  37.90246  1.000 36.58322  ? 301 LYS A N   1 
ATOM   907  C  CA  . LYS A 1 301 ? -1.03547  10.03960  36.75314  1.000 30.85342  ? 301 LYS A CA  1 
ATOM   908  C  C   . LYS A 1 301 ? 0.04191   10.58506  35.81973  1.000 37.27170  ? 301 LYS A C   1 
ATOM   909  O  O   . LYS A 1 301 ? 0.04271   11.78077  35.52108  1.000 45.09997  ? 301 LYS A O   1 
ATOM   910  C  CB  . LYS A 1 301 ? -2.38727  9.96593   36.04205  1.000 42.72410  ? 301 LYS A CB  1 
ATOM   911  N  N   . TYR A 1 302 ? 1.00033   9.74877   35.42184  1.000 31.61759  ? 302 TYR A N   1 
ATOM   912  C  CA  . TYR A 1 302 ? 2.10513   10.23307  34.60035  1.000 26.48657  ? 302 TYR A CA  1 
ATOM   913  C  C   . TYR A 1 302 ? 1.95916   9.72594   33.17773  1.000 22.28930  ? 302 TYR A C   1 
ATOM   914  O  O   . TYR A 1 302 ? 1.59999   8.56355   32.96569  1.000 27.09294  ? 302 TYR A O   1 
ATOM   915  C  CB  . TYR A 1 302 ? 3.46781   9.80249   35.17640  1.000 46.97847  ? 302 TYR A CB  1 
ATOM   916  C  CG  . TYR A 1 302 ? 3.89633   10.62829  36.38419  1.000 39.37104  ? 302 TYR A CG  1 
ATOM   917  C  CD1 . TYR A 1 302 ? 4.24439   11.97164  36.24462  1.000 47.03745  ? 302 TYR A CD1 1 
ATOM   918  C  CD2 . TYR A 1 302 ? 3.92036   10.07383  37.65311  1.000 63.55521  ? 302 TYR A CD2 1 
ATOM   919  C  CE1 . TYR A 1 302 ? 4.61108   12.73553  37.34142  1.000 55.62059  ? 302 TYR A CE1 1 
ATOM   920  C  CE2 . TYR A 1 302 ? 4.28504   10.83022  38.75478  1.000 39.52572  ? 302 TYR A CE2 1 
ATOM   921  C  CZ  . TYR A 1 302 ? 4.63729   12.15684  38.58752  1.000 54.80085  ? 302 TYR A CZ  1 
ATOM   922  O  OH  . TYR A 1 302 ? 5.00627   12.91940  39.67871  1.000 64.67922  ? 302 TYR A OH  1 
ATOM   923  N  N   . ALA A 1 303 ? 2.34469   10.56354  32.20897  1.000 22.74602  ? 303 ALA A N   1 
ATOM   924  C  CA  . ALA A 1 303 ? 2.19091   10.11757  30.82642  1.000 23.11134  ? 303 ALA A CA  1 
ATOM   925  C  C   . ALA A 1 303 ? 3.16061   9.01104   30.45758  1.000 22.93567  ? 303 ALA A C   1 
ATOM   926  O  O   . ALA A 1 303 ? 2.97387   8.37602   29.41329  1.000 20.13852  ? 303 ALA A O   1 
ATOM   927  C  CB  . ALA A 1 303 ? 2.36363   11.29488  29.86966  1.000 28.46871  ? 303 ALA A CB  1 
ATOM   928  N  N   . ARG A 1 304 ? 4.18710   8.73688   31.27724  1.000 21.61587  ? 304 ARG A N   1 
ATOM   929  C  CA  . ARG A 1 304 ? 5.13149   7.70340   30.86152  1.000 19.56407  ? 304 ARG A CA  1 
ATOM   930  C  C   . ARG A 1 304 ? 4.49490   6.30822   30.88320  1.000 19.14188  ? 304 ARG A C   1 
ATOM   931  O  O   . ARG A 1 304 ? 5.10261   5.37298   30.36741  1.000 20.58144  ? 304 ARG A O   1 
ATOM   932  C  CB  . ARG A 1 304 ? 6.39141   7.73458   31.75033  1.000 27.08495  ? 304 ARG A CB  1 
ATOM   933  C  CG  . ARG A 1 304 ? 6.14937   7.38129   33.17440  1.000 26.18822  ? 304 ARG A CG  1 
ATOM   934  C  CD  . ARG A 1 304 ? 7.43795   7.46947   34.03912  1.000 41.25425  ? 304 ARG A CD  1 
ATOM   935  N  NE  . ARG A 1 304 ? 7.15644   7.00842   35.40179  1.000 33.01835  ? 304 ARG A NE  1 
ATOM   936  C  CZ  . ARG A 1 304 ? 8.04215   6.94466   36.39242  1.000 28.49547  ? 304 ARG A CZ  1 
ATOM   937  N  NH1 . ARG A 1 304 ? 9.31012   7.32097   36.21161  1.000 29.12918  ? 304 ARG A NH1 1 
ATOM   938  N  NH2 . ARG A 1 304 ? 7.63324   6.52912   37.57954  1.000 28.13719  ? 304 ARG A NH2 1 
ATOM   939  N  N   . ASP A 1 305 ? 3.29322   6.15292   31.46165  1.000 19.70605  ? 305 ASP A N   1 
ATOM   940  C  CA  . ASP A 1 305 ? 2.61856   4.84979   31.39849  1.000 21.17279  ? 305 ASP A CA  1 
ATOM   941  C  C   . ASP A 1 305 ? 1.92497   4.61898   30.07349  1.000 21.66938  ? 305 ASP A C   1 
ATOM   942  O  O   . ASP A 1 305 ? 1.21703   3.62055   29.91730  1.000 21.16481  ? 305 ASP A O   1 
ATOM   943  C  CB  . ASP A 1 305 ? 1.62181   4.66921   32.57618  1.000 24.69921  ? 305 ASP A CB  1 
ATOM   944  C  CG  . ASP A 1 305 ? 0.46099   5.65529   32.57249  1.000 29.38398  ? 305 ASP A CG  1 
ATOM   945  O  OD1 . ASP A 1 305 ? 0.24500   6.37514   31.58505  1.000 30.47244  ? 305 ASP A OD1 1 
ATOM   946  O  OD2 . ASP A 1 305 ? -0.26434  5.71768   33.60797  1.000 32.22609  ? 305 ASP A OD2 1 
ATOM   947  N  N   . ILE A 1 306 ? 2.17138   5.48200   29.08574  1.000 19.54758  ? 306 ILE A N   1 
ATOM   948  C  CA  . ILE A 1 306 ? 1.58373   5.36704   27.75797  1.000 20.24548  ? 306 ILE A CA  1 
ATOM   949  C  C   . ILE A 1 306 ? 2.68799   5.22200   26.71912  1.000 18.60910  ? 306 ILE A C   1 
ATOM   950  O  O   . ILE A 1 306 ? 3.70711   5.91415   26.78986  1.000 18.28664  ? 306 ILE A O   1 
ATOM   951  C  CB  . ILE A 1 306 ? 0.73990   6.61811   27.43829  1.000 16.31977  ? 306 ILE A CB  1 
ATOM   952  C  CG1 . ILE A 1 306 ? -0.46702  6.69057   28.37744  1.000 20.88270  ? 306 ILE A CG1 1 
ATOM   953  C  CG2 . ILE A 1 306 ? 0.29778   6.57911   25.95674  1.000 19.63812  ? 306 ILE A CG2 1 
ATOM   954  C  CD1 . ILE A 1 306 ? -1.12645  8.07564   28.32360  1.000 25.42180  ? 306 ILE A CD1 1 
ATOM   955  N  N   . VAL A 1 307 ? 2.46642   4.35484   25.72582  1.000 16.93325  ? 307 VAL A N   1 
ATOM   956  C  CA  . VAL A 1 307 ? 3.28966   4.32333   24.51024  1.000 16.38360  ? 307 VAL A CA  1 
ATOM   957  C  C   . VAL A 1 307 ? 2.37135   4.50227   23.30199  1.000 20.00263  ? 307 VAL A C   1 
ATOM   958  O  O   . VAL A 1 307 ? 1.34959   3.81959   23.19748  1.000 21.63541  ? 307 VAL A O   1 
ATOM   959  C  CB  . VAL A 1 307 ? 4.07661   3.00650   24.37563  1.000 20.62627  ? 307 VAL A CB  1 
ATOM   960  C  CG1 . VAL A 1 307 ? 4.82173   3.00281   23.01209  1.000 23.64083  ? 307 VAL A CG1 1 
ATOM   961  C  CG2 . VAL A 1 307 ? 5.04439   2.85264   25.48551  1.000 31.33733  ? 307 VAL A CG2 1 
ATOM   962  N  N   . TYR A 1 308 ? 2.73841   5.39149   22.38018  1.000 18.20237  ? 308 TYR A N   1 
ATOM   963  C  CA  . TYR A 1 308 ? 1.98831   5.55058   21.13011  1.000 19.52406  ? 308 TYR A CA  1 
ATOM   964  C  C   . TYR A 1 308 ? 2.74417   4.94326   19.95279  1.000 19.75964  ? 308 TYR A C   1 
ATOM   965  O  O   . TYR A 1 308 ? 3.96609   5.10306   19.83169  1.000 21.56172  ? 308 TYR A O   1 
ATOM   966  C  CB  . TYR A 1 308 ? 1.73991   7.03665   20.79672  1.000 17.90689  ? 308 TYR A CB  1 
ATOM   967  C  CG  . TYR A 1 308 ? 0.56371   7.69165   21.47969  1.000 20.51045  ? 308 TYR A CG  1 
ATOM   968  C  CD1 . TYR A 1 308 ? -0.73036  7.54676   20.97263  1.000 28.04114  ? 308 TYR A CD1 1 
ATOM   969  C  CD2 . TYR A 1 308 ? 0.73611   8.44961   22.62905  1.000 21.47461  ? 308 TYR A CD2 1 
ATOM   970  C  CE1 . TYR A 1 308 ? -1.81862  8.17008   21.57852  1.000 27.26357  ? 308 TYR A CE1 1 
ATOM   971  C  CE2 . TYR A 1 308 ? -0.35259  9.08071   23.24650  1.000 20.63991  ? 308 TYR A CE2 1 
ATOM   972  C  CZ  . TYR A 1 308 ? -1.61190  8.94234   22.69985  1.000 26.22549  ? 308 TYR A CZ  1 
ATOM   973  O  OH  . TYR A 1 308 ? -2.68162  9.53301   23.32923  1.000 24.97048  ? 308 TYR A OH  1 
ATOM   974  N  N   . GLY A 1 309 ? 2.00054   4.33068   19.02783  1.000 16.91289  ? 309 GLY A N   1 
ATOM   975  C  CA  . GLY A 1 309 ? 2.60417   3.91132   17.76672  1.000 17.61304  ? 309 GLY A CA  1 
ATOM   976  C  C   . GLY A 1 309 ? 1.56311   4.05912   16.68099  1.000 23.00878  ? 309 GLY A C   1 
ATOM   977  O  O   . GLY A 1 309 ? 0.41093   4.37850   16.95774  1.000 22.62089  ? 309 GLY A O   1 
ATOM   978  N  N   . THR A 1 310 ? 1.98221   3.90054   15.42669  1.000 19.56054  ? 310 THR A N   1 
ATOM   979  C  CA  . THR A 1 310 ? 1.05497   3.92727   14.29585  1.000 18.07971  ? 310 THR A CA  1 
ATOM   980  C  C   . THR A 1 310 ? 1.15295   2.60303   13.55905  1.000 22.00679  ? 310 THR A C   1 
ATOM   981  O  O   . THR A 1 310 ? 2.25597   2.11075   13.32590  1.000 23.04732  ? 310 THR A O   1 
ATOM   982  C  CB  . THR A 1 310 ? 1.37623   5.05475   13.31962  1.000 26.44498  ? 310 THR A CB  1 
ATOM   983  O  OG1 . THR A 1 310 ? 1.33470   6.30065   14.00889  1.000 27.75049  ? 310 THR A OG1 1 
ATOM   984  C  CG2 . THR A 1 310 ? 0.31697   5.10402   12.17582  1.000 25.02323  ? 310 THR A CG2 1 
ATOM   985  N  N   . ILE A 1 311 ? 0.00996   1.99630   13.24498  1.000 19.64727  ? 311 ILE A N   1 
ATOM   986  C  CA  . ILE A 1 311 ? 0.02292   0.82929   12.36562  1.000 20.06745  ? 311 ILE A CA  1 
ATOM   987  C  C   . ILE A 1 311 ? -0.81537  1.15939   11.13912  1.000 20.06959  ? 311 ILE A C   1 
ATOM   988  O  O   . ILE A 1 311 ? -1.39995  2.24334   11.06656  1.000 21.64527  ? 311 ILE A O   1 
ATOM   989  C  CB  . ILE A 1 311 ? -0.46342  -0.43666  13.09241  1.000 20.79228  ? 311 ILE A CB  1 
ATOM   990  C  CG1 . ILE A 1 311 ? -1.75680  -0.19600  13.88095  1.000 24.86281  ? 311 ILE A CG1 1 
ATOM   991  C  CG2 . ILE A 1 311 ? 0.64831   -0.86244  14.08747  1.000 20.14731  ? 311 ILE A CG2 1 
ATOM   992  C  CD1 . ILE A 1 311 ? -3.02472  -0.00811  13.04989  1.000 28.74135  ? 311 ILE A CD1 1 
ATOM   993  N  N   . TYR A 1 312 ? -0.87004  0.25751   10.16569  1.000 21.22534  ? 312 TYR A N   1 
ATOM   994  C  CA  . TYR A 1 312 ? -1.45911  0.57335   8.86877   1.000 17.79098  ? 312 TYR A CA  1 
ATOM   995  C  C   . TYR A 1 312 ? -2.45728  -0.51032  8.48761   1.000 19.32731  ? 312 TYR A C   1 
ATOM   996  O  O   . TYR A 1 312 ? -2.12171  -1.70298  8.47324   1.000 22.84310  ? 312 TYR A O   1 
ATOM   997  C  CB  . TYR A 1 312 ? -0.36197  0.72393   7.81350   1.000 19.91868  ? 312 TYR A CB  1 
ATOM   998  C  CG  . TYR A 1 312 ? 0.45236   1.94801   8.18738   1.000 20.32287  ? 312 TYR A CG  1 
ATOM   999  C  CD1 . TYR A 1 312 ? 1.49160   1.86255   9.10218   1.000 21.26488  ? 312 TYR A CD1 1 
ATOM   1000 C  CD2 . TYR A 1 312 ? 0.09296   3.19422   7.71707   1.000 21.44593  ? 312 TYR A CD2 1 
ATOM   1001 C  CE1 . TYR A 1 312 ? 2.19471   3.00566   9.49833   1.000 21.35734  ? 312 TYR A CE1 1 
ATOM   1002 C  CE2 . TYR A 1 312 ? 0.78814   4.32729   8.09823   1.000 21.51712  ? 312 TYR A CE2 1 
ATOM   1003 C  CZ  . TYR A 1 312 ? 1.82453   4.22545   8.98381   1.000 24.52099  ? 312 TYR A CZ  1 
ATOM   1004 O  OH  . TYR A 1 312 ? 2.49835   5.35315   9.38652   1.000 26.18713  ? 312 TYR A OH  1 
ATOM   1005 N  N   . LEU A 1 313 ? -3.67650  -0.08639  8.20135   1.000 20.29717  ? 313 LEU A N   1 
ATOM   1006 C  CA  . LEU A 1 313 ? -4.75552  -1.02266  7.89960   1.000 21.84631  ? 313 LEU A CA  1 
ATOM   1007 C  C   . LEU A 1 313 ? -4.54191  -1.60458  6.50938   1.000 22.64218  ? 313 LEU A C   1 
ATOM   1008 O  O   . LEU A 1 313 ? -4.31412  -0.86072  5.55649   1.000 25.64993  ? 313 LEU A O   1 
ATOM   1009 C  CB  . LEU A 1 313 ? -6.10767  -0.32001  7.96139   1.000 22.69967  ? 313 LEU A CB  1 
ATOM   1010 C  CG  . LEU A 1 313 ? -6.39559  0.40123   9.29046   1.000 25.38567  ? 313 LEU A CG  1 
ATOM   1011 C  CD1 . LEU A 1 313 ? -7.84758  0.92744   9.28767   1.000 24.80667  ? 313 LEU A CD1 1 
ATOM   1012 C  CD2 . LEU A 1 313 ? -6.12489  -0.51353  10.54179  1.000 25.80726  ? 313 LEU A CD2 1 
ATOM   1013 N  N   . GLY A 1 314 ? -4.60799  -2.93062  6.40333   1.000 24.77133  ? 314 GLY A N   1 
ATOM   1014 C  CA  . GLY A 1 314 ? -4.38481  -3.60426  5.13594   1.000 24.47907  ? 314 GLY A CA  1 
ATOM   1015 C  C   . GLY A 1 314 ? -2.96625  -3.44268  4.62647   1.000 25.66096  ? 314 GLY A C   1 
ATOM   1016 O  O   . GLY A 1 314 ? -2.67291  -3.75034  3.46782   1.000 27.80695  ? 314 GLY A O   1 
ATOM   1017 N  N   . GLY A 1 315 ? -2.07076  -2.96578  5.48560   1.000 25.81931  ? 315 GLY A N   1 
ATOM   1018 C  CA  . GLY A 1 315 ? -0.71520  -2.73620  5.04341   1.000 25.95696  ? 315 GLY A CA  1 
ATOM   1019 C  C   . GLY A 1 315 ? -0.56710  -1.57873  4.09089   1.000 24.41803  ? 315 GLY A C   1 
ATOM   1020 O  O   . GLY A 1 315 ? 0.48813   -1.44526  3.46917   1.000 26.19306  ? 315 GLY A O   1 
ATOM   1021 N  N   . LYS A 1 316 ? -1.58925  -0.72531  3.96388   1.000 25.39375  ? 316 LYS A N   1 
ATOM   1022 C  CA  . LYS A 1 316 ? -1.51621  0.39152   3.02201   1.000 24.96181  ? 316 LYS A CA  1 
ATOM   1023 C  C   . LYS A 1 316 ? -0.94089  1.61984   3.71674   1.000 26.74449  ? 316 LYS A C   1 
ATOM   1024 O  O   . LYS A 1 316 ? -1.41452  1.98797   4.80559   1.000 21.32009  ? 316 LYS A O   1 
ATOM   1025 C  CB  . LYS A 1 316 ? -2.88581  0.71454   2.45675   1.000 23.39508  ? 316 LYS A CB  1 
ATOM   1026 C  CG  . LYS A 1 316 ? -3.46326  -0.38138  1.59571   1.000 30.07324  ? 316 LYS A CG  1 
ATOM   1027 C  CD  . LYS A 1 316 ? -4.63354  0.19843   0.81426   1.000 45.68525  ? 316 LYS A CD  1 
ATOM   1028 C  CE  . LYS A 1 316 ? -5.25644  -0.79098  -0.13626  1.000 61.26705  ? 316 LYS A CE  1 
ATOM   1029 N  NZ  . LYS A 1 316 ? -6.45068  -0.15021  -0.78252  1.000 64.25102  ? 316 LYS A NZ  1 
ATOM   1030 N  N   . PRO A 1 317 ? 0.05203   2.28986   3.12367   1.000 24.47143  ? 317 PRO A N   1 
ATOM   1031 C  CA  . PRO A 1 317 ? 0.72768   3.37369   3.85046   1.000 22.51475  ? 317 PRO A CA  1 
ATOM   1032 C  C   . PRO A 1 317 ? -0.14175  4.60962   4.05538   1.000 23.48556  ? 317 PRO A C   1 
ATOM   1033 O  O   . PRO A 1 317 ? 0.16993   5.41593   4.94709   1.000 25.40738  ? 317 PRO A O   1 
ATOM   1034 C  CB  . PRO A 1 317 ? 1.96767   3.66363   2.98895   1.000 31.03447  ? 317 PRO A CB  1 
ATOM   1035 C  CG  . PRO A 1 317 ? 1.59953   3.19090   1.62213   1.000 31.96233  ? 317 PRO A CG  1 
ATOM   1036 C  CD  . PRO A 1 317 ? 0.67007   2.01656   1.80734   1.000 25.17775  ? 317 PRO A CD  1 
ATOM   1037 N  N   . ASP A 1 318 ? -1.24878  4.75303   3.31288   1.000 23.78387  ? 318 ASP A N   1 
ATOM   1038 C  CA  . ASP A 1 318 ? -2.14244  5.87900   3.51905   1.000 27.21596  ? 318 ASP A CA  1 
ATOM   1039 C  C   . ASP A 1 318 ? -3.36039  5.50060   4.36601   1.000 26.81302  ? 318 ASP A C   1 
ATOM   1040 O  O   . ASP A 1 318 ? -4.36119  6.22948   4.36260   1.000 25.42701  ? 318 ASP A O   1 
ATOM   1041 C  CB  . ASP A 1 318 ? -2.56250  6.48931   2.17647   1.000 31.73791  ? 318 ASP A CB  1 
ATOM   1042 C  CG  . ASP A 1 318 ? -3.48917  5.60176   1.37949   1.000 44.14500  ? 318 ASP A CG  1 
ATOM   1043 O  OD1 . ASP A 1 318 ? -3.49449  4.37207   1.56664   1.000 34.55678  ? 318 ASP A OD1 1 
ATOM   1044 O  OD2 . ASP A 1 318 ? -4.21299  6.15672   0.53890   1.000 46.89683  ? 318 ASP A OD2 1 
ATOM   1045 N  N   . GLN A 1 319 ? -3.28911  4.38954   5.10547   1.000 24.87530  ? 319 GLN A N   1 
ATOM   1046 C  CA  . GLN A 1 319 ? -4.35090  4.00687   6.04141   1.000 21.47283  ? 319 GLN A CA  1 
ATOM   1047 C  C   . GLN A 1 319 ? -3.79563  3.81548   7.44816   1.000 20.76048  ? 319 GLN A C   1 
ATOM   1048 O  O   . GLN A 1 319 ? -3.90193  2.73108   8.02909   1.000 21.52640  ? 319 GLN A O   1 
ATOM   1049 C  CB  . GLN A 1 319 ? -5.07672  2.75478   5.55150   1.000 23.02122  ? 319 GLN A CB  1 
ATOM   1050 C  CG  . GLN A 1 319 ? -5.70740  3.02983   4.16877   1.000 25.63118  ? 319 GLN A CG  1 
ATOM   1051 C  CD  . GLN A 1 319 ? -6.43977  1.84363   3.57258   1.000 26.99444  ? 319 GLN A CD  1 
ATOM   1052 O  OE1 . GLN A 1 319 ? -6.26184  0.67286   3.98874   1.000 28.93585  ? 319 GLN A OE1 1 
ATOM   1053 N  NE2 . GLN A 1 319 ? -7.27176  2.13125   2.60863   1.000 25.85565  ? 319 GLN A NE2 1 
ATOM   1054 N  N   . PRO A 1 320 ? -3.23650  4.86329   8.02982   1.000 22.21185  ? 320 PRO A N   1 
ATOM   1055 C  CA  . PRO A 1 320 ? -2.75599  4.75876   9.40126   1.000 19.83088  ? 320 PRO A CA  1 
ATOM   1056 C  C   . PRO A 1 320 ? -3.89022  4.67720   10.41489  1.000 21.44744  ? 320 PRO A C   1 
ATOM   1057 O  O   . PRO A 1 320 ? -4.99768  5.20135   10.21899  1.000 23.74705  ? 320 PRO A O   1 
ATOM   1058 C  CB  . PRO A 1 320 ? -1.95039  6.04872   9.58748   1.000 21.99755  ? 320 PRO A CB  1 
ATOM   1059 C  CG  . PRO A 1 320 ? -2.65466  7.05487   8.66053   1.000 24.61256  ? 320 PRO A CG  1 
ATOM   1060 C  CD  . PRO A 1 320 ? -3.01114  6.21076   7.45775   1.000 25.33600  ? 320 PRO A CD  1 
ATOM   1061 N  N   . ALA A 1 321 ? -3.59039  3.99564   11.51944  1.000 19.55610  ? 321 ALA A N   1 
ATOM   1062 C  CA  . ALA A 1 321 ? -4.41257  4.06603   12.72384  1.000 18.74644  ? 321 ALA A CA  1 
ATOM   1063 C  C   . ALA A 1 321 ? -3.45521  4.09991   13.90491  1.000 21.68084  ? 321 ALA A C   1 
ATOM   1064 O  O   . ALA A 1 321 ? -2.33731  3.58000   13.83177  1.000 22.78886  ? 321 ALA A O   1 
ATOM   1065 C  CB  . ALA A 1 321 ? -5.39014  2.89144   12.85160  1.000 22.37360  ? 321 ALA A CB  1 
ATOM   1066 N  N   . VAL A 1 322 ? -3.87909  4.73243   14.98014  1.000 19.69502  ? 322 VAL A N   1 
ATOM   1067 C  CA  . VAL A 1 322 ? -3.02334  4.90120   16.14859  1.000 20.17620  ? 322 VAL A CA  1 
ATOM   1068 C  C   . VAL A 1 322 ? -3.26719  3.75286   17.11264  1.000 19.67239  ? 322 VAL A C   1 
ATOM   1069 O  O   . VAL A 1 322 ? -4.42131  3.42314   17.40010  1.000 22.26007  ? 322 VAL A O   1 
ATOM   1070 C  CB  . VAL A 1 322 ? -3.32069  6.24952   16.82161  1.000 20.85353  ? 322 VAL A CB  1 
ATOM   1071 C  CG1 . VAL A 1 322 ? -2.56919  6.35581   18.14872  1.000 24.08828  ? 322 VAL A CG1 1 
ATOM   1072 C  CG2 . VAL A 1 322 ? -2.97976  7.37187   15.84418  1.000 27.93430  ? 322 VAL A CG2 1 
ATOM   1073 N  N   . ILE A 1 323 ? -2.19386  3.14346   17.62728  1.000 17.88881  ? 323 ILE A N   1 
ATOM   1074 C  CA  . ILE A 1 323 ? -2.32100  2.20799   18.73454  1.000 18.98357  ? 323 ILE A CA  1 
ATOM   1075 C  C   . ILE A 1 323 ? -1.74599  2.88209   19.96597  1.000 21.79496  ? 323 ILE A C   1 
ATOM   1076 O  O   . ILE A 1 323 ? -0.57105  3.26993   19.98182  1.000 21.67738  ? 323 ILE A O   1 
ATOM   1077 C  CB  . ILE A 1 323 ? -1.64987  0.84962   18.44977  1.000 18.57809  ? 323 ILE A CB  1 
ATOM   1078 C  CG1 . ILE A 1 323 ? -1.76296  -0.04169  19.70761  1.000 24.29652  ? 323 ILE A CG1 1 
ATOM   1079 C  CG2 . ILE A 1 323 ? -0.16889  1.01399   17.86871  1.000 24.84814  ? 323 ILE A CG2 1 
ATOM   1080 C  CD1 . ILE A 1 323 ? -1.36851  -1.54705  19.41277  1.000 34.57971  ? 323 ILE A CD1 1 
ATOM   1081 N  N   . LYS A 1 324 ? -2.58369  3.05722   20.97901  1.000 18.38277  ? 324 LYS A N   1 
ATOM   1082 C  CA  . LYS A 1 324 ? -2.17469  3.68199   22.22264  1.000 16.72605  ? 324 LYS A CA  1 
ATOM   1083 C  C   . LYS A 1 324 ? -2.18234  2.58585   23.27204  1.000 20.65299  ? 324 LYS A C   1 
ATOM   1084 O  O   . LYS A 1 324 ? -3.22626  1.96126   23.50621  1.000 22.08913  ? 324 LYS A O   1 
ATOM   1085 C  CB  . LYS A 1 324 ? -3.12710  4.82102   22.59604  1.000 19.66590  ? 324 LYS A CB  1 
ATOM   1086 C  CG  . LYS A 1 324 ? -2.81349  5.44244   23.97054  1.000 19.11117  ? 324 LYS A CG  1 
ATOM   1087 C  CD  . LYS A 1 324 ? -3.92540  6.37956   24.35789  1.000 21.91397  ? 324 LYS A CD  1 
ATOM   1088 C  CE  . LYS A 1 324 ? -3.60528  7.19921   25.58429  1.000 38.66612  ? 324 LYS A CE  1 
ATOM   1089 N  NZ  . LYS A 1 324 ? -4.85557  7.90204   26.02571  1.000 38.69505  ? 324 LYS A NZ  1 
ATOM   1090 N  N   . THR A 1 325 ? -1.01649  2.30126   23.84623  1.000 18.20569  ? 325 THR A N   1 
ATOM   1091 C  CA  . THR A 1 325 ? -0.88538  1.25357   24.85121  1.000 19.03863  ? 325 THR A CA  1 
ATOM   1092 C  C   . THR A 1 325 ? -0.68290  1.90119   26.20503  1.000 20.40464  ? 325 THR A C   1 
ATOM   1093 O  O   . THR A 1 325 ? 0.18605   2.75596   26.34457  1.000 19.04958  ? 325 THR A O   1 
ATOM   1094 C  CB  . THR A 1 325 ? 0.30062   0.34363   24.52597  1.000 20.22761  ? 325 THR A CB  1 
ATOM   1095 O  OG1 . THR A 1 325 ? 0.12961   -0.20396  23.20579  1.000 22.97178  ? 325 THR A OG1 1 
ATOM   1096 C  CG2 . THR A 1 325 ? 0.40710   -0.81306  25.56522  1.000 20.17396  ? 325 THR A CG2 1 
ATOM   1097 N  N   . THR A 1 326 ? -1.48131  1.51445   27.20469  1.000 17.71157  ? 326 THR A N   1 
ATOM   1098 C  CA  . THR A 1 326 ? -1.39111  2.13729   28.52857  1.000 16.13906  ? 326 THR A CA  1 
ATOM   1099 C  C   . THR A 1 326 ? -1.19029  1.04293   29.57341  1.000 19.11079  ? 326 THR A C   1 
ATOM   1100 O  O   . THR A 1 326 ? -1.87360  0.02755   29.53732  1.000 20.27950  ? 326 THR A O   1 
ATOM   1101 C  CB  . THR A 1 326 ? -2.67720  2.96444   28.86085  1.000 23.59998  ? 326 THR A CB  1 
ATOM   1102 O  OG1 . THR A 1 326 ? -2.96451  3.90451   27.80363  1.000 23.72305  ? 326 THR A OG1 1 
ATOM   1103 C  CG2 . THR A 1 326 ? -2.54333  3.71262   30.16484  1.000 22.73195  ? 326 THR A CG2 1 
ATOM   1104 N  N   . PHE A 1 327 ? -0.29074  1.27087   30.52246  1.000 18.75389  ? 327 PHE A N   1 
ATOM   1105 C  CA  . PHE A 1 327 ? 0.02423   0.28738   31.56224  1.000 22.30846  ? 327 PHE A CA  1 
ATOM   1106 C  C   . PHE A 1 327 ? -0.61909  0.62757   32.89908  1.000 24.19178  ? 327 PHE A C   1 
ATOM   1107 O  O   . PHE A 1 327 ? -0.47625  1.75061   33.39673  1.000 21.73025  ? 327 PHE A O   1 
ATOM   1108 C  CB  . PHE A 1 327 ? 1.54712   0.18141   31.72240  1.000 17.83334  ? 327 PHE A CB  1 
ATOM   1109 C  CG  . PHE A 1 327 ? 2.23724   -0.10189  30.41443  1.000 17.65689  ? 327 PHE A CG  1 
ATOM   1110 C  CD1 . PHE A 1 327 ? 1.99900   -1.29047  29.74164  1.000 22.95899  ? 327 PHE A CD1 1 
ATOM   1111 C  CD2 . PHE A 1 327 ? 3.06384   0.83773   29.83443  1.000 21.44643  ? 327 PHE A CD2 1 
ATOM   1112 C  CE1 . PHE A 1 327 ? 2.60271   -1.54782  28.51468  1.000 22.43888  ? 327 PHE A CE1 1 
ATOM   1113 C  CE2 . PHE A 1 327 ? 3.67537   0.58629   28.60773  1.000 24.01576  ? 327 PHE A CE2 1 
ATOM   1114 C  CZ  . PHE A 1 327 ? 3.41691   -0.60492  27.93306  1.000 18.67174  ? 327 PHE A CZ  1 
ATOM   1115 N  N   . ASN A 1 328 ? -1.28657  -0.37640  33.49721  1.000 21.46072  ? 328 ASN A N   1 
ATOM   1116 C  CA  . ASN A 1 328 ? -1.74034  -0.33708  34.89686  1.000 17.74420  ? 328 ASN A CA  1 
ATOM   1117 C  C   . ASN A 1 328 ? -2.73114  0.79443   35.16899  1.000 22.37760  ? 328 ASN A C   1 
ATOM   1118 O  O   . ASN A 1 328 ? -2.71586  1.41339   36.23864  1.000 25.40456  ? 328 ASN A O   1 
ATOM   1119 C  CB  . ASN A 1 328 ? -0.55833  -0.26275  35.87749  1.000 26.32272  ? 328 ASN A CB  1 
ATOM   1120 C  CG  . ASN A 1 328 ? 0.33290   -1.52244  35.83715  1.000 25.59707  ? 328 ASN A CG  1 
ATOM   1121 O  OD1 . ASN A 1 328 ? -0.09016  -2.59971  35.39184  1.000 24.95786  ? 328 ASN A OD1 1 
ATOM   1122 N  ND2 . ASN A 1 328 ? 1.58054   -1.37801  36.28655  1.000 22.04568  ? 328 ASN A ND2 1 
ATOM   1123 N  N   . GLN A 1 329 ? -3.61975  1.08158   34.21557  1.000 20.50712  ? 329 GLN A N   1 
ATOM   1124 C  CA  . GLN A 1 329 ? -4.60048  2.13354   34.45003  1.000 21.94926  ? 329 GLN A CA  1 
ATOM   1125 C  C   . GLN A 1 329 ? -6.02968  1.60748   34.58383  1.000 29.35019  ? 329 GLN A C   1 
ATOM   1126 O  O   . GLN A 1 329 ? -6.97514  2.40880   34.68623  1.000 29.45316  ? 329 GLN A O   1 
ATOM   1127 C  CB  . GLN A 1 329 ? -4.50700  3.19184   33.34904  1.000 26.23934  ? 329 GLN A CB  1 
ATOM   1128 C  CG  . GLN A 1 329 ? -3.30416  4.14510   33.53790  1.000 32.64422  ? 329 GLN A CG  1 
ATOM   1129 C  CD  . GLN A 1 329 ? -3.42570  4.99999   34.77602  1.000 45.64718  ? 329 GLN A CD  1 
ATOM   1130 O  OE1 . GLN A 1 329 ? -2.67372  4.83384   35.74235  1.000 41.02044  ? 329 GLN A OE1 1 
ATOM   1131 N  NE2 . GLN A 1 329 ? -4.38981  5.91376   34.76499  1.000 40.67274  ? 329 GLN A NE2 1 
ATOM   1132 N  N   . GLU A 1 330 ? -6.21432  0.29363   34.64083  1.000 23.17896  ? 330 GLU A N   1 
ATOM   1133 C  CA  . GLU A 1 330 ? -7.53532  -0.28214  34.88989  1.000 25.65842  ? 330 GLU A CA  1 
ATOM   1134 C  C   . GLU A 1 330 ? -7.70832  -0.58898  36.37073  1.000 26.64566  ? 330 GLU A C   1 
ATOM   1135 O  O   . GLU A 1 330 ? -6.73305  -0.82473  37.08608  1.000 33.06438  ? 330 GLU A O   1 
ATOM   1136 C  CB  . GLU A 1 330 ? -7.74410  -1.57149  34.08872  1.000 26.48786  ? 330 GLU A CB  1 
ATOM   1137 C  CG  . GLU A 1 330 ? -7.54434  -1.37771  32.58820  1.000 27.90329  ? 330 GLU A CG  1 
ATOM   1138 C  CD  . GLU A 1 330 ? -8.56306  -0.42013  31.99017  1.000 34.46302  ? 330 GLU A CD  1 
ATOM   1139 O  OE1 . GLU A 1 330 ? -9.71509  -0.38620  32.47347  1.000 33.76482  ? 330 GLU A OE1 1 
ATOM   1140 O  OE2 . GLU A 1 330 ? -8.22462  0.29266   31.02670  1.000 36.31311  ? 330 GLU A OE2 1 
ATOM   1141 N  N   . THR A 1 331 ? -8.95506  -0.57565  36.82863  1.000 27.38677  ? 331 THR A N   1 
ATOM   1142 C  CA  . THR A 1 331 ? -9.23874  -1.00178  38.19692  1.000 26.83941  ? 331 THR A CA  1 
ATOM   1143 C  C   . THR A 1 331 ? -9.78313  -2.42599  38.20499  1.000 28.78080  ? 331 THR A C   1 
ATOM   1144 O  O   . THR A 1 331 ? -10.02197 -3.03663  37.16527  1.000 35.56497  ? 331 THR A O   1 
ATOM   1145 C  CB  . THR A 1 331 ? -10.21661 -0.05600  38.87751  1.000 32.70486  ? 331 THR A CB  1 
ATOM   1146 O  OG1 . THR A 1 331 ? -11.39945 0.03602   38.08082  1.000 41.48974  ? 331 THR A OG1 1 
ATOM   1147 C  CG2 . THR A 1 331 ? -9.58517  1.31821   39.01871  1.000 36.81792  ? 331 THR A CG2 1 
ATOM   1148 N  N   . GLY A 1 332 ? -9.93607  -2.97536  39.40384  1.000 31.29871  ? 332 GLY A N   1 
ATOM   1149 C  CA  . GLY A 1 332 ? -10.40530 -4.34330  39.50795  1.000 31.70177  ? 332 GLY A CA  1 
ATOM   1150 C  C   . GLY A 1 332 ? -9.36464  -5.37587  39.14513  1.000 34.86114  ? 332 GLY A C   1 
ATOM   1151 O  O   . GLY A 1 332 ? -9.71960  -6.50676  38.80943  1.000 38.34798  ? 332 GLY A O   1 
ATOM   1152 N  N   . CYS A 1 333 ? -8.08133  -5.02628  39.23141  1.000 28.13906  ? 333 CYS A N   1 
ATOM   1153 C  CA  . CYS A 1 333 ? -6.97920  -5.91509  38.86942  1.000 22.44485  ? 333 CYS A CA  1 
ATOM   1154 C  C   . CYS A 1 333 ? -5.70278  -5.41053  39.54282  1.000 31.82438  ? 333 CYS A C   1 
ATOM   1155 O  O   . CYS A 1 333 ? -5.69026  -4.33470  40.14705  1.000 33.22452  ? 333 CYS A O   1 
ATOM   1156 C  CB  . CYS A 1 333 ? -6.79830  -5.97539  37.33994  1.000 27.79416  ? 333 CYS A CB  1 
ATOM   1157 S  SG  . CYS A 1 333 ? -6.49165  -4.33900  36.61241  1.000 30.55574  ? 333 CYS A SG  1 
ATOM   1158 N  N   . GLU A 1 334 ? -4.63933  -6.22540  39.50150  1.000 24.80013  ? 334 GLU A N   1 
ATOM   1159 C  CA  . GLU A 1 334 ? -3.35020  -5.72808  40.00156  1.000 28.23596  ? 334 GLU A CA  1 
ATOM   1160 C  C   . GLU A 1 334 ? -2.53825  -5.04641  38.91511  1.000 26.22494  ? 334 GLU A C   1 
ATOM   1161 O  O   . GLU A 1 334 ? -1.81799  -4.07038  39.17922  1.000 24.54370  ? 334 GLU A O   1 
ATOM   1162 C  CB  . GLU A 1 334 ? -2.48015  -6.84148  40.57738  1.000 26.91154  ? 334 GLU A CB  1 
ATOM   1163 C  CG  . GLU A 1 334 ? -2.64271  -7.00931  42.03531  1.000 73.24840  ? 334 GLU A CG  1 
ATOM   1164 C  CD  . GLU A 1 334 ? -2.37697  -5.76316  42.84675  1.000 54.45640  ? 334 GLU A CD  1 
ATOM   1165 O  OE1 . GLU A 1 334 ? -1.19839  -5.39802  43.09890  1.000 40.53348  ? 334 GLU A OE1 1 
ATOM   1166 O  OE2 . GLU A 1 334 ? -3.37880  -5.12626  43.18901  1.000 44.66913  ? 334 GLU A OE2 1 
ATOM   1167 N  N   . TYR A 1 335 ? -2.62144  -5.57913  37.70398  1.000 21.46341  ? 335 TYR A N   1 
ATOM   1168 C  CA  . TYR A 1 335 ? -1.84418  -5.08525  36.56248  1.000 23.54387  ? 335 TYR A CA  1 
ATOM   1169 C  C   . TYR A 1 335 ? -2.74567  -5.03984  35.34909  1.000 23.53069  ? 335 TYR A C   1 
ATOM   1170 O  O   . TYR A 1 335 ? -3.71223  -5.78740  35.25980  1.000 23.12594  ? 335 TYR A O   1 
ATOM   1171 C  CB  . TYR A 1 335 ? -0.64355  -5.98987  36.19292  1.000 25.62728  ? 335 TYR A CB  1 
ATOM   1172 C  CG  . TYR A 1 335 ? 0.24289   -6.33952  37.36070  1.000 25.53252  ? 335 TYR A CG  1 
ATOM   1173 C  CD1 . TYR A 1 335 ? 1.27872   -5.50139  37.72901  1.000 23.36348  ? 335 TYR A CD1 1 
ATOM   1174 C  CD2 . TYR A 1 335 ? 0.04197   -7.52403  38.09451  1.000 21.27185  ? 335 TYR A CD2 1 
ATOM   1175 C  CE1 . TYR A 1 335 ? 2.09123   -5.81092  38.82716  1.000 30.71798  ? 335 TYR A CE1 1 
ATOM   1176 C  CE2 . TYR A 1 335 ? 0.83077   -7.82901  39.15979  1.000 26.31195  ? 335 TYR A CE2 1 
ATOM   1177 C  CZ  . TYR A 1 335 ? 1.85207   -6.97529  39.52752  1.000 23.80609  ? 335 TYR A CZ  1 
ATOM   1178 O  OH  . TYR A 1 335 ? 2.65648   -7.31472  40.58731  1.000 29.72542  ? 335 TYR A OH  1 
ATOM   1179 N  N   . SER A 1 336 ? -2.39218  -4.20248  34.37002  1.000 21.63829  ? 336 SER A N   1 
ATOM   1180 C  CA  . SER A 1 336 ? -3.17816  -4.23240  33.14223  1.000 20.55212  ? 336 SER A CA  1 
ATOM   1181 C  C   . SER A 1 336 ? -2.35726  -3.68622  31.98222  1.000 21.72541  ? 336 SER A C   1 
ATOM   1182 O  O   . SER A 1 336 ? -1.42914  -2.90749  32.17557  1.000 21.37674  ? 336 SER A O   1 
ATOM   1183 C  CB  . SER A 1 336 ? -4.47430  -3.42173  33.28532  1.000 27.29586  ? 336 SER A CB  1 
ATOM   1184 O  OG  . SER A 1 336 ? -4.19338  -2.05008  33.60041  1.000 25.03325  ? 336 SER A OG  1 
ATOM   1185 N  N   . ILE A 1 337 ? -2.68909  -4.14785  30.78142  1.000 19.86908  ? 337 ILE A N   1 
ATOM   1186 C  CA  . ILE A 1 337 ? -2.19982  -3.56976  29.52453  1.000 20.09578  ? 337 ILE A CA  1 
ATOM   1187 C  C   . ILE A 1 337 ? -3.44143  -3.28021  28.70050  1.000 21.96702  ? 337 ILE A C   1 
ATOM   1188 O  O   . ILE A 1 337 ? -4.24800  -4.18461  28.46469  1.000 21.72315  ? 337 ILE A O   1 
ATOM   1189 C  CB  . ILE A 1 337 ? -1.25187  -4.52377  28.76110  1.000 17.61756  ? 337 ILE A CB  1 
ATOM   1190 C  CG1 . ILE A 1 337 ? -0.01637  -4.85150  29.58935  1.000 21.07462  ? 337 ILE A CG1 1 
ATOM   1191 C  CG2 . ILE A 1 337 ? -0.85716  -3.88776  27.38401  1.000 21.67685  ? 337 ILE A CG2 1 
ATOM   1192 C  CD1 . ILE A 1 337 ? 0.82079   -6.05647  29.04183  1.000 26.63488  ? 337 ILE A CD1 1 
ATOM   1193 N  N   . THR A 1 338 ? -3.64341  -2.02279  28.29440  1.000 20.52841  ? 338 THR A N   1 
ATOM   1194 C  CA  A THR A 1 338 ? -4.81711  -1.62098  27.51486  0.664 19.63474  ? 338 THR A CA  1 
ATOM   1195 C  CA  B THR A 1 338 ? -4.80366  -1.72076  27.46304  0.336 18.75011  ? 338 THR A CA  1 
ATOM   1196 C  C   . THR A 1 338 ? -4.35121  -1.14461  26.13621  1.000 22.69693  ? 338 THR A C   1 
ATOM   1197 O  O   . THR A 1 338 ? -3.42827  -0.33864  26.07404  1.000 24.40727  ? 338 THR A O   1 
ATOM   1198 C  CB  A THR A 1 338 ? -5.54329  -0.49704  28.26653  0.664 27.79498  ? 338 THR A CB  1 
ATOM   1199 C  CB  B THR A 1 338 ? -5.76556  -0.75844  28.13444  0.336 22.76557  ? 338 THR A CB  1 
ATOM   1200 O  OG1 A THR A 1 338 ? -5.97529  -0.98057  29.55642  0.664 27.24966  ? 338 THR A OG1 1 
ATOM   1201 O  OG1 B THR A 1 338 ? -5.16318  0.53350   28.20596  0.336 17.98875  ? 338 THR A OG1 1 
ATOM   1202 C  CG2 A THR A 1 338 ? -6.71262  0.02145   27.50181  0.664 26.19753  ? 338 THR A CG2 1 
ATOM   1203 C  CG2 B THR A 1 338 ? -6.07897  -1.25369  29.52141  0.336 19.79855  ? 338 THR A CG2 1 
ATOM   1204 N  N   . PHE A 1 339 ? -4.98123  -1.61856  25.05512  1.000 19.67328  ? 339 PHE A N   1 
ATOM   1205 C  CA  . PHE A 1 339 ? -4.69336  -1.15800  23.69576  1.000 18.69246  ? 339 PHE A CA  1 
ATOM   1206 C  C   . PHE A 1 339 ? -5.89914  -0.36443  23.20594  1.000 27.51516  ? 339 PHE A C   1 
ATOM   1207 O  O   . PHE A 1 339 ? -7.00161  -0.91124  23.10482  1.000 26.40067  ? 339 PHE A O   1 
ATOM   1208 C  CB  . PHE A 1 339 ? -4.41504  -2.31348  22.72642  1.000 18.29978  ? 339 PHE A CB  1 
ATOM   1209 C  CG  . PHE A 1 339 ? -3.26710  -3.17462  23.10502  1.000 20.89370  ? 339 PHE A CG  1 
ATOM   1210 C  CD1 . PHE A 1 339 ? -1.95353  -2.73542  22.94256  1.000 19.80742  ? 339 PHE A CD1 1 
ATOM   1211 C  CD2 . PHE A 1 339 ? -3.48476  -4.43624  23.65839  1.000 22.68974  ? 339 PHE A CD2 1 
ATOM   1212 C  CE1 . PHE A 1 339 ? -0.86754  -3.54051  23.30836  1.000 20.83891  ? 339 PHE A CE1 1 
ATOM   1213 C  CE2 . PHE A 1 339 ? -2.40860  -5.24265  23.99451  1.000 24.39520  ? 339 PHE A CE2 1 
ATOM   1214 C  CZ  . PHE A 1 339 ? -1.10446  -4.79355  23.82619  1.000 21.97744  ? 339 PHE A CZ  1 
ATOM   1215 N  N   . ASN A 1 340 ? -5.70292  0.90913   22.88483  1.000 18.87485  ? 340 ASN A N   1 
ATOM   1216 C  CA  . ASN A 1 340 ? -6.77531  1.68626   22.26723  1.000 19.24775  ? 340 ASN A CA  1 
ATOM   1217 C  C   . ASN A 1 340 ? -6.39654  1.93280   20.81576  1.000 23.12331  ? 340 ASN A C   1 
ATOM   1218 O  O   . ASN A 1 340 ? -5.32070  2.46686   20.54926  1.000 21.84311  ? 340 ASN A O   1 
ATOM   1219 C  CB  . ASN A 1 340 ? -7.00995  3.02040   22.98584  1.000 18.20898  ? 340 ASN A CB  1 
ATOM   1220 C  CG  . ASN A 1 340 ? -8.03185  3.87005   22.27150  1.000 37.22772  ? 340 ASN A CG  1 
ATOM   1221 O  OD1 . ASN A 1 340 ? -7.67647  4.78098   21.51760  1.000 32.66593  ? 340 ASN A OD1 1 
ATOM   1222 N  ND2 . ASN A 1 340 ? -9.31613  3.55445   22.46373  1.000 35.50069  ? 340 ASN A ND2 1 
ATOM   1223 N  N   . PHE A 1 341 ? -7.27402  1.55535   19.89380  1.000 19.31527  ? 341 PHE A N   1 
ATOM   1224 C  CA  . PHE A 1 341 ? -7.04596  1.73921   18.46366  1.000 21.14152  ? 341 PHE A CA  1 
ATOM   1225 C  C   . PHE A 1 341 ? -7.95494  2.86917   18.02900  1.000 24.85859  ? 341 PHE A C   1 
ATOM   1226 O  O   . PHE A 1 341 ? -9.14021  2.87881   18.38399  1.000 24.04542  ? 341 PHE A O   1 
ATOM   1227 C  CB  . PHE A 1 341 ? -7.36392  0.44903   17.68405  1.000 22.76069  ? 341 PHE A CB  1 
ATOM   1228 C  CG  . PHE A 1 341 ? -6.46811  -0.70642  18.02852  1.000 25.50536  ? 341 PHE A CG  1 
ATOM   1229 C  CD1 . PHE A 1 341 ? -6.69638  -1.47828  19.16903  1.000 24.09830  ? 341 PHE A CD1 1 
ATOM   1230 C  CD2 . PHE A 1 341 ? -5.39363  -1.03196  17.21317  1.000 24.21528  ? 341 PHE A CD2 1 
ATOM   1231 C  CE1 . PHE A 1 341 ? -5.85662  -2.55425  19.47904  1.000 22.74835  ? 341 PHE A CE1 1 
ATOM   1232 C  CE2 . PHE A 1 341 ? -4.54680  -2.14084  17.54265  1.000 22.43522  ? 341 PHE A CE2 1 
ATOM   1233 C  CZ  . PHE A 1 341 ? -4.78511  -2.85590  18.67246  1.000 26.04736  ? 341 PHE A CZ  1 
ATOM   1234 N  N   . SER A 1 342 ? -7.41319  3.83099   17.28699  1.000 19.24325  ? 342 SER A N   1 
ATOM   1235 C  CA  . SER A 1 342 ? -8.24676  4.93176   16.84635  1.000 18.70742  ? 342 SER A CA  1 
ATOM   1236 C  C   . SER A 1 342 ? -7.70659  5.44078   15.52175  1.000 24.45735  ? 342 SER A C   1 
ATOM   1237 O  O   . SER A 1 342 ? -6.57315  5.14327   15.13657  1.000 24.20055  ? 342 SER A O   1 
ATOM   1238 C  CB  . SER A 1 342 ? -8.26353  6.06834   17.88176  1.000 26.53626  ? 342 SER A CB  1 
ATOM   1239 O  OG  . SER A 1 342 ? -6.98253  6.64414   17.99562  1.000 25.88784  ? 342 SER A OG  1 
ATOM   1240 N  N   . TRP A 1 343 ? -8.52634  6.20742   14.81658  1.000 24.77316  ? 343 TRP A N   1 
ATOM   1241 C  CA  . TRP A 1 343 ? -8.06413  6.77991   13.56105  1.000 23.58761  ? 343 TRP A CA  1 
ATOM   1242 C  C   . TRP A 1 343 ? -8.80625  8.08430   13.32385  1.000 31.20229  ? 343 TRP A C   1 
ATOM   1243 O  O   . TRP A 1 343 ? -9.89396  8.30514   13.85910  1.000 29.49036  ? 343 TRP A O   1 
ATOM   1244 C  CB  . TRP A 1 343 ? -8.28072  5.82414   12.38855  1.000 26.15377  ? 343 TRP A CB  1 
ATOM   1245 C  CG  . TRP A 1 343 ? -9.66453  5.37529   12.29392  1.000 26.84787  ? 343 TRP A CG  1 
ATOM   1246 C  CD1 . TRP A 1 343 ? -10.63999 5.87068   11.46908  1.000 29.32487  ? 343 TRP A CD1 1 
ATOM   1247 C  CD2 . TRP A 1 343 ? -10.26979 4.32572   13.05611  1.000 27.28035  ? 343 TRP A CD2 1 
ATOM   1248 N  NE1 . TRP A 1 343 ? -11.81871 5.18807   11.67917  1.000 29.33848  ? 343 TRP A NE1 1 
ATOM   1249 C  CE2 . TRP A 1 343 ? -11.61942 4.23817   12.64732  1.000 30.93374  ? 343 TRP A CE2 1 
ATOM   1250 C  CE3 . TRP A 1 343 ? -9.80830  3.46771   14.06540  1.000 28.95138  ? 343 TRP A CE3 1 
ATOM   1251 C  CZ2 . TRP A 1 343 ? -12.51017 3.30755   13.20120  1.000 29.01752  ? 343 TRP A CZ2 1 
ATOM   1252 C  CZ3 . TRP A 1 343 ? -10.68415 2.54940   14.61518  1.000 30.82024  ? 343 TRP A CZ3 1 
ATOM   1253 C  CH2 . TRP A 1 343 ? -12.02289 2.47258   14.18152  1.000 34.56054  ? 343 TRP A CH2 1 
ATOM   1254 N  N   . SER A 1 344 ? -8.21310  8.94757   12.51580  1.000 33.74783  ? 344 SER A N   1 
ATOM   1255 C  CA  . SER A 1 344 ? -8.79762  10.25992  12.28136  1.000 27.76725  ? 344 SER A CA  1 
ATOM   1256 C  C   . SER A 1 344 ? -9.19461  10.49142  10.83547  1.000 38.10849  ? 344 SER A C   1 
ATOM   1257 O  O   . SER A 1 344 ? -9.92773  11.44863  10.56462  1.000 41.63418  ? 344 SER A O   1 
ATOM   1258 C  CB  . SER A 1 344 ? -7.83781  11.36808  12.74684  1.000 33.84177  ? 344 SER A CB  1 
ATOM   1259 O  OG  . SER A 1 344 ? -6.52141  11.15626  12.28400  1.000 36.53675  ? 344 SER A OG  1 
ATOM   1260 N  N   . LYS A 1 345 ? -8.76759  9.63295   9.91292   1.000 30.95232  ? 345 LYS A N   1 
ATOM   1261 C  CA  . LYS A 1 345 ? -9.18689  9.70829   8.52105   1.000 29.70985  ? 345 LYS A CA  1 
ATOM   1262 C  C   . LYS A 1 345 ? -10.58229 9.13263   8.30793   1.000 52.27045  ? 345 LYS A C   1 
ATOM   1263 O  O   . LYS A 1 345 ? -11.07110 8.29970   9.07024   1.000 33.19097  ? 345 LYS A O   1 
ATOM   1264 C  CB  . LYS A 1 345 ? -8.19704  8.96921   7.63227   1.000 35.07675  ? 345 LYS A CB  1 
ATOM   1265 C  CG  . LYS A 1 345 ? -6.83438  9.62852   7.59007   1.000 32.78929  ? 345 LYS A CG  1 
ATOM   1266 C  CD  . LYS A 1 345 ? -5.97639  8.93859   6.54147   1.000 44.55920  ? 345 LYS A CD  1 
ATOM   1267 C  CE  . LYS A 1 345 ? -4.81638  9.79204   6.10999   1.000 59.23352  ? 345 LYS A CE  1 
ATOM   1268 N  NZ  . LYS A 1 345 ? -4.11921  9.13585   4.97573   1.000 41.02241  ? 345 LYS A NZ  1 
ATOM   1269 N  N   . THR A 1 346 ? -11.21624 9.56953   7.22424   1.000 36.42418  ? 346 THR A N   1 
ATOM   1270 C  CA  . THR A 1 346 ? -12.52548 9.05260   6.84445   1.000 32.98804  ? 346 THR A CA  1 
ATOM   1271 C  C   . THR A 1 346 ? -12.29932 7.84928   5.93999   1.000 39.22770  ? 346 THR A C   1 
ATOM   1272 O  O   . THR A 1 346 ? -12.07420 7.99969   4.73696   1.000 50.77844  ? 346 THR A O   1 
ATOM   1273 C  CB  . THR A 1 346 ? -13.34821 10.12586  6.14305   1.000 31.92569  ? 346 THR A CB  1 
ATOM   1274 O  OG1 . THR A 1 346 ? -13.37316 11.30037  6.96400   1.000 48.30877  ? 346 THR A OG1 1 
ATOM   1275 C  CG2 . THR A 1 346 ? -14.76819 9.62437   5.95839   1.000 42.43599  ? 346 THR A CG2 1 
ATOM   1276 N  N   . TYR A 1 347 ? -12.35245 6.65067   6.51310   1.000 33.02098  ? 347 TYR A N   1 
ATOM   1277 C  CA  . TYR A 1 347 ? -12.15416 5.42445   5.75205   1.000 32.31642  ? 347 TYR A CA  1 
ATOM   1278 C  C   . TYR A 1 347 ? -13.49065 4.91478   5.22479   1.000 41.90588  ? 347 TYR A C   1 
ATOM   1279 O  O   . TYR A 1 347 ? -14.51913 5.02396   5.89027   1.000 42.55067  ? 347 TYR A O   1 
ATOM   1280 C  CB  . TYR A 1 347 ? -11.47782 4.33640   6.60579   1.000 31.16179  ? 347 TYR A CB  1 
ATOM   1281 C  CG  . TYR A 1 347 ? -10.04076 4.68436   6.97548   1.000 30.45704  ? 347 TYR A CG  1 
ATOM   1282 C  CD1 . TYR A 1 347 ? -9.15114  5.15598   6.00804   1.000 29.46266  ? 347 TYR A CD1 1 
ATOM   1283 C  CD2 . TYR A 1 347 ? -9.57210  4.53963   8.28868   1.000 26.62463  ? 347 TYR A CD2 1 
ATOM   1284 C  CE1 . TYR A 1 347 ? -7.83740  5.50754   6.33731   1.000 25.96130  ? 347 TYR A CE1 1 
ATOM   1285 C  CE2 . TYR A 1 347 ? -8.25139  4.87710   8.62720   1.000 25.81376  ? 347 TYR A CE2 1 
ATOM   1286 C  CZ  . TYR A 1 347 ? -7.39457  5.36525   7.65456   1.000 22.32342  ? 347 TYR A CZ  1 
ATOM   1287 O  OH  . TYR A 1 347 ? -6.11058  5.71798   7.98464   1.000 24.57865  ? 347 TYR A OH  1 
ATOM   1288 N  N   . GLU A 1 348 ? -13.45697 4.33447   4.02511   1.000 41.00204  ? 348 GLU A N   1 
ATOM   1289 C  CA  . GLU A 1 348 ? -14.65821 3.84632   3.35033   1.000 44.73685  ? 348 GLU A CA  1 
ATOM   1290 C  C   . GLU A 1 348 ? -14.44814 2.38991   2.97897   1.000 32.75709  ? 348 GLU A C   1 
ATOM   1291 O  O   . GLU A 1 348 ? -13.69318 2.08848   2.04934   1.000 52.63076  ? 348 GLU A O   1 
ATOM   1292 C  CB  . GLU A 1 348 ? -14.97624 4.66847   2.10142   1.000 41.49458  ? 348 GLU A CB  1 
ATOM   1293 C  CG  . GLU A 1 348 ? -16.21944 4.17067   1.37940   1.000 53.47252  ? 348 GLU A CG  1 
ATOM   1294 C  CD  . GLU A 1 348 ? -16.55480 4.99009   0.13693   1.000 66.08477  ? 348 GLU A CD  1 
ATOM   1295 O  OE1 . GLU A 1 348 ? -15.75061 4.98950   -0.82464  1.000 79.76715  ? 348 GLU A OE1 1 
ATOM   1296 O  OE2 . GLU A 1 348 ? -17.62485 5.63489   0.12772   1.000 80.37608  ? 348 GLU A OE2 1 
ATOM   1297 N  N   . ASN A 1 349 ? -15.10290 1.48922   3.71311   1.000 38.33457  ? 349 ASN A N   1 
ATOM   1298 C  CA  . ASN A 1 349 ? -14.98739 0.05623   3.46966   1.000 36.70961  ? 349 ASN A CA  1 
ATOM   1299 C  C   . ASN A 1 349 ? -13.54178 -0.42103  3.58446   1.000 44.52594  ? 349 ASN A C   1 
ATOM   1300 O  O   . ASN A 1 349 ? -13.00397 -1.08221  2.69485   1.000 42.06292  ? 349 ASN A O   1 
ATOM   1301 C  CB  . ASN A 1 349 ? -15.59661 -0.32413  2.12256   1.000 47.71425  ? 349 ASN A CB  1 
ATOM   1302 C  CG  . ASN A 1 349 ? -17.08162 -0.02784  2.07137   1.000 71.65759  ? 349 ASN A CG  1 
ATOM   1303 O  OD1 . ASN A 1 349 ? -17.74446 0.00971   3.11213   1.000 66.58164  ? 349 ASN A OD1 1 
ATOM   1304 N  ND2 . ASN A 1 349 ? -17.61524 0.18219   0.86673   1.000 72.43666  ? 349 ASN A ND2 1 
ATOM   1305 N  N   . VAL A 1 350 ? -12.91424 -0.09409  4.71248   1.000 34.96007  ? 350 VAL A N   1 
ATOM   1306 C  CA  . VAL A 1 350 ? -11.54990 -0.51813  4.99551   1.000 32.08450  ? 350 VAL A CA  1 
ATOM   1307 C  C   . VAL A 1 350 ? -11.59132 -1.61180  6.05113   1.000 38.61650  ? 350 VAL A C   1 
ATOM   1308 O  O   . VAL A 1 350 ? -12.14577 -1.42019  7.14207   1.000 34.99602  ? 350 VAL A O   1 
ATOM   1309 C  CB  . VAL A 1 350 ? -10.67023 0.65329   5.45069   1.000 29.84618  ? 350 VAL A CB  1 
ATOM   1310 C  CG1 . VAL A 1 350 ? -9.31445  0.12352   5.91975   1.000 28.80150  ? 350 VAL A CG1 1 
ATOM   1311 C  CG2 . VAL A 1 350 ? -10.48918 1.66533   4.30143   1.000 31.78171  ? 350 VAL A CG2 1 
ATOM   1312 N  N   . GLU A 1 351 ? -11.01374 -2.75929  5.72320   1.000 33.64305  ? 351 GLU A N   1 
ATOM   1313 C  CA  . GLU A 1 351 ? -10.95299 -3.86994  6.66368   1.000 31.34720  ? 351 GLU A CA  1 
ATOM   1314 C  C   . GLU A 1 351 ? -9.94939  -3.59534  7.77831   1.000 26.53850  ? 351 GLU A C   1 
ATOM   1315 O  O   . GLU A 1 351 ? -8.82158  -3.16345  7.52353   1.000 27.70197  ? 351 GLU A O   1 
ATOM   1316 C  CB  . GLU A 1 351 ? -10.55957 -5.14388  5.94640   1.000 30.67295  ? 351 GLU A CB  1 
ATOM   1317 C  CG  . GLU A 1 351 ? -10.83026 -6.37014  6.75549   1.000 34.37273  ? 351 GLU A CG  1 
ATOM   1318 C  CD  . GLU A 1 351 ? -10.45219 -7.61591  6.01223   1.000 58.60165  ? 351 GLU A CD  1 
ATOM   1319 O  OE1 . GLU A 1 351 ? -10.09592 -7.51143  4.81391   1.000 53.00962  ? 351 GLU A OE1 1 
ATOM   1320 O  OE2 . GLU A 1 351 ? -10.46072 -8.68533  6.64270   1.000 57.20393  ? 351 GLU A OE2 1 
ATOM   1321 N  N   . PHE A 1 352 ? -10.34936 -3.84677  9.02248   1.000 26.19135  ? 352 PHE A N   1 
ATOM   1322 C  CA  . PHE A 1 352 ? -9.46551  -3.55077  10.14750  1.000 30.38202  ? 352 PHE A CA  1 
ATOM   1323 C  C   . PHE A 1 352 ? -8.54947  -4.74644  10.44199  1.000 29.72480  ? 352 PHE A C   1 
ATOM   1324 O  O   . PHE A 1 352 ? -8.79077  -5.56042  11.34538  1.000 28.81229  ? 352 PHE A O   1 
ATOM   1325 C  CB  . PHE A 1 352 ? -10.24787 -3.12546  11.38712  1.000 24.43284  ? 352 PHE A CB  1 
ATOM   1326 C  CG  . PHE A 1 352 ? -9.42826  -2.23832  12.30136  1.000 22.18182  ? 352 PHE A CG  1 
ATOM   1327 C  CD1 . PHE A 1 352 ? -8.41794  -2.77709  13.08376  1.000 23.91912  ? 352 PHE A CD1 1 
ATOM   1328 C  CD2 . PHE A 1 352 ? -9.62840  -0.86689  12.33593  1.000 29.38349  ? 352 PHE A CD2 1 
ATOM   1329 C  CE1 . PHE A 1 352 ? -7.60186  -1.97698  13.88789  1.000 23.91771  ? 352 PHE A CE1 1 
ATOM   1330 C  CE2 . PHE A 1 352 ? -8.81546  -0.05402  13.16090  1.000 25.45901  ? 352 PHE A CE2 1 
ATOM   1331 C  CZ  . PHE A 1 352 ? -7.80712  -0.61021  13.92443  1.000 24.60668  ? 352 PHE A CZ  1 
ATOM   1332 N  N   . GLU A 1 353 ? -7.43301  -4.80714  9.70298   1.000 22.32860  ? 353 GLU A N   1 
ATOM   1333 C  CA  . GLU A 1 353 ? -6.38045  -5.78566  9.96695   1.000 25.51132  ? 353 GLU A CA  1 
ATOM   1334 C  C   . GLU A 1 353 ? -5.03840  -5.08933  9.74405   1.000 23.91587  ? 353 GLU A C   1 
ATOM   1335 O  O   . GLU A 1 353 ? -4.85564  -4.39476  8.73754   1.000 27.03259  ? 353 GLU A O   1 
ATOM   1336 C  CB  . GLU A 1 353 ? -6.56302  -7.04159  9.10181   1.000 31.29149  ? 353 GLU A CB  1 
ATOM   1337 C  CG  . GLU A 1 353 ? -6.67933  -6.78384  7.60333   1.000 36.87690  ? 353 GLU A CG  1 
ATOM   1338 C  CD  . GLU A 1 353 ? -5.36029  -7.05037  6.89033   1.000 39.73189  ? 353 GLU A CD  1 
ATOM   1339 O  OE1 . GLU A 1 353 ? -5.18752  -6.68426  5.70103   1.000 36.59022  ? 353 GLU A OE1 1 
ATOM   1340 O  OE2 . GLU A 1 353 ? -4.47735  -7.63711  7.53932   1.000 37.11119  ? 353 GLU A OE2 1 
ATOM   1341 N  N   . THR A 1 354 ? -4.16137  -5.16741  10.74943  1.000 21.62203  ? 354 THR A N   1 
ATOM   1342 C  CA  . THR A 1 354 ? -3.08303  -4.19426  10.91612  1.000 22.33048  ? 354 THR A CA  1 
ATOM   1343 C  C   . THR A 1 354 ? -1.70830  -4.77196  10.62997  1.000 23.09154  ? 354 THR A C   1 
ATOM   1344 O  O   . THR A 1 354 ? -1.48184  -5.97989  10.72867  1.000 22.28508  ? 354 THR A O   1 
ATOM   1345 C  CB  . THR A 1 354 ? -3.04465  -3.60396  12.34211  1.000 23.02797  ? 354 THR A CB  1 
ATOM   1346 O  OG1 . THR A 1 354 ? -2.44959  -4.52340  13.26138  1.000 23.29600  ? 354 THR A OG1 1 
ATOM   1347 C  CG2 . THR A 1 354 ? -4.45083  -3.26689  12.81912  1.000 28.08653  ? 354 THR A CG2 1 
ATOM   1348 N  N   . THR A 1 355 ? -0.76987  -3.86691  10.32317  1.000 20.01859  ? 355 THR A N   1 
ATOM   1349 C  CA  . THR A 1 355 ? 0.65174   -4.20116  10.39798  1.000 15.97683  ? 355 THR A CA  1 
ATOM   1350 C  C   . THR A 1 355 ? 1.05477   -4.37506  11.85959  1.000 20.65208  ? 355 THR A C   1 
ATOM   1351 O  O   . THR A 1 355 ? 0.23515   -4.22366  12.76949  1.000 19.48868  ? 355 THR A O   1 
ATOM   1352 C  CB  . THR A 1 355 ? 1.49907   -3.12215  9.71859   1.000 19.12979  ? 355 THR A CB  1 
ATOM   1353 O  OG1 . THR A 1 355 ? 1.26189   -1.85975  10.34597  1.000 21.28864  ? 355 THR A OG1 1 
ATOM   1354 C  CG2 . THR A 1 355 ? 1.13370   -3.04228  8.23825   1.000 19.10184  ? 355 THR A CG2 1 
ATOM   1355 N  N   . SER A 1 356 ? 2.31342   -4.76689  12.08360  1.000 18.52541  ? 356 SER A N   1 
ATOM   1356 C  CA  . SER A 1 356 ? 2.79141   -5.09653  13.42942  1.000 17.73794  ? 356 SER A CA  1 
ATOM   1357 C  C   . SER A 1 356 ? 3.55697   -3.92594  14.02102  1.000 20.28218  ? 356 SER A C   1 
ATOM   1358 O  O   . SER A 1 356 ? 4.15433   -3.13239  13.30532  1.000 20.59792  ? 356 SER A O   1 
ATOM   1359 C  CB  . SER A 1 356 ? 3.69852   -6.33889  13.42274  1.000 22.44068  ? 356 SER A CB  1 
ATOM   1360 O  OG  . SER A 1 356 ? 2.93070   -7.51082  13.13291  1.000 23.42557  ? 356 SER A OG  1 
ATOM   1361 N  N   . PHE A 1 357 ? 3.54035   -3.83417  15.35479  1.000 20.85679  ? 357 PHE A N   1 
ATOM   1362 C  CA  . PHE A 1 357 ? 4.20481   -2.75760  16.07748  1.000 17.79064  ? 357 PHE A CA  1 
ATOM   1363 C  C   . PHE A 1 357 ? 4.95740   -3.36245  17.25498  1.000 20.30333  ? 357 PHE A C   1 
ATOM   1364 O  O   . PHE A 1 357 ? 4.44947   -4.27248  17.92055  1.000 21.62432  ? 357 PHE A O   1 
ATOM   1365 C  CB  . PHE A 1 357 ? 3.17611   -1.70486  16.56341  1.000 18.29436  ? 357 PHE A CB  1 
ATOM   1366 C  CG  . PHE A 1 357 ? 3.76377   -0.61849  17.42787  1.000 19.50094  ? 357 PHE A CG  1 
ATOM   1367 C  CD1 . PHE A 1 357 ? 4.73765   0.23900   16.92118  1.000 27.91755  ? 357 PHE A CD1 1 
ATOM   1368 C  CD2 . PHE A 1 357 ? 3.33147   -0.45558  18.77457  1.000 19.51680  ? 357 PHE A CD2 1 
ATOM   1369 C  CE1 . PHE A 1 357 ? 5.29445   1.25162   17.71654  1.000 25.23911  ? 357 PHE A CE1 1 
ATOM   1370 C  CE2 . PHE A 1 357 ? 3.87283   0.55225   19.59218  1.000 21.01111  ? 357 PHE A CE2 1 
ATOM   1371 C  CZ  . PHE A 1 357 ? 4.86816   1.42115   19.05725  1.000 23.19335  ? 357 PHE A CZ  1 
ATOM   1372 N  N   . THR A 1 358 ? 6.17074   -2.86333  17.51138  1.000 16.73359  ? 358 THR A N   1 
ATOM   1373 C  CA  . THR A 1 358 ? 7.00367   -3.30327  18.62708  1.000 16.06653  ? 358 THR A CA  1 
ATOM   1374 C  C   . THR A 1 358 ? 7.20691   -2.17471  19.61353  1.000 22.81801  ? 358 THR A C   1 
ATOM   1375 O  O   . THR A 1 358 ? 7.42667   -1.02622  19.21480  1.000 20.07563  ? 358 THR A O   1 
ATOM   1376 C  CB  . THR A 1 358 ? 8.36909   -3.76241  18.10628  1.000 24.21337  ? 358 THR A CB  1 
ATOM   1377 O  OG1 . THR A 1 358 ? 8.16519   -4.93183  17.31314  1.000 24.88625  ? 358 THR A OG1 1 
ATOM   1378 C  CG2 . THR A 1 358 ? 9.36184   -4.06297  19.22809  1.000 21.85094  ? 358 THR A CG2 1 
ATOM   1379 N  N   . PHE A 1 359 ? 7.15300   -2.51177  20.89896  1.000 18.49055  ? 359 PHE A N   1 
ATOM   1380 C  CA  . PHE A 1 359 ? 7.43857   -1.54951  21.94966  1.000 17.54364  ? 359 PHE A CA  1 
ATOM   1381 C  C   . PHE A 1 359 ? 8.06963   -2.31521  23.10393  1.000 19.98549  ? 359 PHE A C   1 
ATOM   1382 O  O   . PHE A 1 359 ? 8.26453   -3.52476  23.03013  1.000 18.93579  ? 359 PHE A O   1 
ATOM   1383 C  CB  . PHE A 1 359 ? 6.16833   -0.77529  22.36348  1.000 20.05486  ? 359 PHE A CB  1 
ATOM   1384 C  CG  . PHE A 1 359 ? 5.05200   -1.66055  22.90742  1.000 20.79509  ? 359 PHE A CG  1 
ATOM   1385 C  CD1 . PHE A 1 359 ? 4.15972   -2.30184  22.05904  1.000 21.24789  ? 359 PHE A CD1 1 
ATOM   1386 C  CD2 . PHE A 1 359 ? 4.91045   -1.84061  24.27471  1.000 18.96180  ? 359 PHE A CD2 1 
ATOM   1387 C  CE1 . PHE A 1 359 ? 3.14145   -3.10608  22.55007  1.000 21.54987  ? 359 PHE A CE1 1 
ATOM   1388 C  CE2 . PHE A 1 359 ? 3.89029   -2.66625  24.80612  1.000 22.32487  ? 359 PHE A CE2 1 
ATOM   1389 C  CZ  . PHE A 1 359 ? 2.99606   -3.29475  23.95800  1.000 20.29295  ? 359 PHE A CZ  1 
ATOM   1390 N  N   . SER A 1 360 ? 8.43351   -1.60706  24.16804  1.000 19.64087  ? 360 SER A N   1 
ATOM   1391 C  CA  . SER A 1 360 ? 8.87419   -2.30904  25.36660  1.000 18.75055  ? 360 SER A CA  1 
ATOM   1392 C  C   . SER A 1 360 ? 8.31049   -1.60466  26.58085  1.000 18.34090  ? 360 SER A C   1 
ATOM   1393 O  O   . SER A 1 360 ? 7.77374   -0.49439  26.49644  1.000 20.20362  ? 360 SER A O   1 
ATOM   1394 C  CB  . SER A 1 360 ? 10.40092  -2.40582  25.46498  1.000 23.88376  ? 360 SER A CB  1 
ATOM   1395 O  OG  . SER A 1 360 ? 10.97240  -1.14674  25.81990  1.000 21.49817  ? 360 SER A OG  1 
ATOM   1396 N  N   . TYR A 1 361 ? 8.41909   -2.27605  27.72248  1.000 17.53046  ? 361 TYR A N   1 
ATOM   1397 C  CA  . TYR A 1 361 ? 8.06290   -1.63730  28.98475  1.000 17.34450  ? 361 TYR A CA  1 
ATOM   1398 C  C   . TYR A 1 361 ? 8.86908   -2.25746  30.12425  1.000 19.40486  ? 361 TYR A C   1 
ATOM   1399 O  O   . TYR A 1 361 ? 9.49877   -3.30371  29.97702  1.000 20.50409  ? 361 TYR A O   1 
ATOM   1400 C  CB  . TYR A 1 361 ? 6.56424   -1.71464  29.29796  1.000 20.28565  ? 361 TYR A CB  1 
ATOM   1401 C  CG  . TYR A 1 361 ? 5.99782   -3.12531  29.37553  1.000 20.47093  ? 361 TYR A CG  1 
ATOM   1402 C  CD1 . TYR A 1 361 ? 5.97987   -3.84661  30.59044  1.000 20.07172  ? 361 TYR A CD1 1 
ATOM   1403 C  CD2 . TYR A 1 361 ? 5.47078   -3.73199  28.23701  1.000 20.72051  ? 361 TYR A CD2 1 
ATOM   1404 C  CE1 . TYR A 1 361 ? 5.42475   -5.13110  30.64774  1.000 18.83676  ? 361 TYR A CE1 1 
ATOM   1405 C  CE2 . TYR A 1 361 ? 4.92941   -5.04116  28.28900  1.000 20.47585  ? 361 TYR A CE2 1 
ATOM   1406 C  CZ  . TYR A 1 361 ? 4.91304   -5.72233  29.50144  1.000 21.08519  ? 361 TYR A CZ  1 
ATOM   1407 O  OH  . TYR A 1 361 ? 4.35506   -6.98053  29.53367  1.000 20.16201  ? 361 TYR A OH  1 
ATOM   1408 N  N   . ILE A 1 362 ? 8.89843   -1.54293  31.24927  1.000 21.40994  ? 362 ILE A N   1 
ATOM   1409 C  CA  . ILE A 1 362 ? 9.67740   -1.94934  32.41464  1.000 21.62666  ? 362 ILE A CA  1 
ATOM   1410 C  C   . ILE A 1 362 ? 8.91140   -3.02639  33.18165  1.000 19.22795  ? 362 ILE A C   1 
ATOM   1411 O  O   . ILE A 1 362 ? 7.70776   -2.87673  33.46168  1.000 21.40637  ? 362 ILE A O   1 
ATOM   1412 C  CB  . ILE A 1 362 ? 9.97202   -0.72985  33.30379  1.000 22.89113  ? 362 ILE A CB  1 
ATOM   1413 C  CG1 . ILE A 1 362 ? 10.72684  0.34948   32.48826  1.000 21.64686  ? 362 ILE A CG1 1 
ATOM   1414 C  CG2 . ILE A 1 362 ? 10.74118  -1.18226  34.54891  1.000 26.81283  ? 362 ILE A CG2 1 
ATOM   1415 C  CD1 . ILE A 1 362 ? 10.73369  1.75235   33.21469  1.000 24.74911  ? 362 ILE A CD1 1 
ATOM   1416 N  N   . ALA A 1 363 ? 9.59749   -4.14077  33.48612  1.000 22.08599  ? 363 ALA A N   1 
ATOM   1417 C  CA  . ALA A 1 363 ? 8.97596   -5.30588  34.10271  1.000 24.05315  ? 363 ALA A CA  1 
ATOM   1418 C  C   . ALA A 1 363 ? 8.90314   -5.13645  35.62107  1.000 25.57222  ? 363 ALA A C   1 
ATOM   1419 O  O   . ALA A 1 363 ? 9.74146   -4.46625  36.23097  1.000 24.97209  ? 363 ALA A O   1 
ATOM   1420 C  CB  . ALA A 1 363 ? 9.74882   -6.57905  33.75337  1.000 26.55603  ? 363 ALA A CB  1 
ATOM   1421 N  N   . GLN A 1 364 ? 7.86851   -5.74052  36.20787  1.000 26.45273  ? 364 GLN A N   1 
ATOM   1422 C  CA  . GLN A 1 364 ? 7.63600   -5.64475  37.65183  1.000 24.03664  ? 364 GLN A CA  1 
ATOM   1423 C  C   . GLN A 1 364 ? 8.76201   -6.29241  38.44752  1.000 33.63793  ? 364 GLN A C   1 
ATOM   1424 O  O   . GLN A 1 364 ? 9.21383   -5.74678  39.46179  1.000 32.57454  ? 364 GLN A O   1 
ATOM   1425 C  CB  . GLN A 1 364 ? 6.29619   -6.28849  38.00319  1.000 24.35731  ? 364 GLN A CB  1 
ATOM   1426 C  CG  . GLN A 1 364 ? 6.07467   -6.48440  39.52473  1.000 24.47551  ? 364 GLN A CG  1 
ATOM   1427 C  CD  . GLN A 1 364 ? 5.84803   -5.17705  40.27581  1.000 30.48145  ? 364 GLN A CD  1 
ATOM   1428 O  OE1 . GLN A 1 364 ? 5.79648   -4.10520  39.69013  1.000 29.36870  ? 364 GLN A OE1 1 
ATOM   1429 N  NE2 . GLN A 1 364 ? 5.71132   -5.27228  41.60571  1.000 33.91517  ? 364 GLN A NE2 1 
ATOM   1430 N  N   . GLU A 1 365 ? 9.21801   -7.45423  38.02573  1.000 31.90523  ? 365 GLU A N   1 
ATOM   1431 C  CA  . GLU A 1 365 ? 10.37492  -8.02757  38.69116  1.000 53.57093  ? 365 GLU A CA  1 
ATOM   1432 C  C   . GLU A 1 365 ? 11.23672  -8.70617  37.65387  1.000 51.60218  ? 365 GLU A C   1 
ATOM   1433 O  O   . GLU A 1 365 ? 10.74536  -8.98697  36.55474  1.000 38.68198  ? 365 GLU A O   1 
ATOM   1434 C  CB  . GLU A 1 365 ? 9.96192   -9.00522  39.78567  1.000 47.53555  ? 365 GLU A CB  1 
ATOM   1435 C  CG  . GLU A 1 365 ? 9.16604   -10.18349 39.29117  1.000 57.07120  ? 365 GLU A CG  1 
ATOM   1436 C  CD  . GLU A 1 365 ? 8.96035   -11.23064 40.37603  1.000 78.92762  ? 365 GLU A CD  1 
ATOM   1437 O  OE1 . GLU A 1 365 ? 9.31411   -12.40710 40.13844  1.000 81.71406  ? 365 GLU A OE1 1 
ATOM   1438 O  OE2 . GLU A 1 365 ? 8.45745   -10.87183 41.46554  1.000 73.95146  ? 365 GLU A OE2 1 
ATOM   1439 O  OXT . GLU A 1 365 ? 12.40973  -8.97582  37.90797  1.000 52.78080  ? 365 GLU A OXT 1 
ATOM   1440 N  N   . THR B 1 183 ? 26.86013  -16.49842 19.07766  1.000 87.75522  ? 183 THR B N   1 
ATOM   1441 C  CA  . THR B 1 183 ? 25.68942  -16.83575 18.28162  1.000 79.47586  ? 183 THR B CA  1 
ATOM   1442 C  C   . THR B 1 183 ? 24.41307  -16.28454 18.91773  1.000 81.26242  ? 183 THR B C   1 
ATOM   1443 O  O   . THR B 1 183 ? 23.40349  -16.99191 19.02037  1.000 84.52723  ? 183 THR B O   1 
ATOM   1444 C  CB  . THR B 1 183 ? 25.54400  -18.35916 18.09260  1.000 80.13388  ? 183 THR B CB  1 
ATOM   1445 N  N   . ARG B 1 184 ? 24.46127  -15.02432 19.36731  1.000 69.88658  ? 184 ARG B N   1 
ATOM   1446 C  CA  . ARG B 1 184 ? 23.24137  -14.28112 19.63387  1.000 37.49749  ? 184 ARG B CA  1 
ATOM   1447 C  C   . ARG B 1 184 ? 23.03071  -13.09766 18.69730  1.000 32.32843  ? 184 ARG B C   1 
ATOM   1448 O  O   . ARG B 1 184 ? 21.90069  -12.62923 18.60675  1.000 32.42545  ? 184 ARG B O   1 
ATOM   1449 C  CB  . ARG B 1 184 ? 23.17284  -13.78299 21.09098  1.000 43.05921  ? 184 ARG B CB  1 
ATOM   1450 C  CG  . ARG B 1 184 ? 22.05368  -14.43175 21.90701  1.000 65.23440  ? 184 ARG B CG  1 
ATOM   1451 C  CD  . ARG B 1 184 ? 22.09609  -14.00410 23.37335  1.000 57.37428  ? 184 ARG B CD  1 
ATOM   1452 N  N   . THR B 1 185 ? 24.05933  -12.61604 17.99228  1.000 34.21771  ? 185 THR B N   1 
ATOM   1453 C  CA  . THR B 1 185 ? 23.87569  -11.54512 17.01877  1.000 32.01138  ? 185 THR B CA  1 
ATOM   1454 C  C   . THR B 1 185 ? 24.35539  -11.98982 15.64383  1.000 35.40172  ? 185 THR B C   1 
ATOM   1455 O  O   . THR B 1 185 ? 25.47489  -12.49759 15.49525  1.000 35.98868  ? 185 THR B O   1 
ATOM   1456 C  CB  . THR B 1 185 ? 24.59801  -10.25854 17.42913  1.000 37.90467  ? 185 THR B CB  1 
ATOM   1457 O  OG1 . THR B 1 185 ? 23.86933  -9.64146  18.49503  1.000 41.76479  ? 185 THR B OG1 1 
ATOM   1458 C  CG2 . THR B 1 185 ? 24.61663  -9.26692  16.24747  1.000 34.56806  ? 185 THR B CG2 1 
ATOM   1459 N  N   . LEU B 1 186 ? 23.49102  -11.78915 14.65617  1.000 31.60292  ? 186 LEU B N   1 
ATOM   1460 C  CA  . LEU B 1 186 ? 23.81108  -11.91814 13.24094  1.000 32.85093  ? 186 LEU B CA  1 
ATOM   1461 C  C   . LEU B 1 186 ? 23.81997  -10.51429 12.65482  1.000 30.99638  ? 186 LEU B C   1 
ATOM   1462 O  O   . LEU B 1 186 ? 22.86698  -9.74937  12.87124  1.000 28.79652  ? 186 LEU B O   1 
ATOM   1463 C  CB  . LEU B 1 186 ? 22.74936  -12.79332 12.58192  1.000 37.96801  ? 186 LEU B CB  1 
ATOM   1464 C  CG  . LEU B 1 186 ? 22.80104  -13.46695 11.23459  1.000 50.17171  ? 186 LEU B CG  1 
ATOM   1465 C  CD1 . LEU B 1 186 ? 24.09284  -14.26714 11.08375  1.000 37.28564  ? 186 LEU B CD1 1 
ATOM   1466 C  CD2 . LEU B 1 186 ? 21.55576  -14.34771 11.16701  1.000 36.73362  ? 186 LEU B CD2 1 
ATOM   1467 N  N   . TRP B 1 187 ? 24.88867  -10.14636 11.94857  1.000 34.83153  ? 187 TRP B N   1 
ATOM   1468 C  CA  . TRP B 1 187 ? 24.96864  -8.75341  11.52219  1.000 32.92813  ? 187 TRP B CA  1 
ATOM   1469 C  C   . TRP B 1 187 ? 25.84333  -8.59721  10.28548  1.000 33.39669  ? 187 TRP B C   1 
ATOM   1470 O  O   . TRP B 1 187 ? 26.59979  -9.48944  9.89798   1.000 32.76019  ? 187 TRP B O   1 
ATOM   1471 C  CB  . TRP B 1 187 ? 25.49090  -7.83335  12.64292  1.000 30.42351  ? 187 TRP B CB  1 
ATOM   1472 C  CG  . TRP B 1 187 ? 26.97782  -7.96053  12.98847  1.000 31.56690  ? 187 TRP B CG  1 
ATOM   1473 C  CD1 . TRP B 1 187 ? 27.85276  -8.96892  12.63149  1.000 36.65135  ? 187 TRP B CD1 1 
ATOM   1474 C  CD2 . TRP B 1 187 ? 27.74018  -7.03695  13.77928  1.000 44.10355  ? 187 TRP B CD2 1 
ATOM   1475 N  NE1 . TRP B 1 187 ? 29.10593  -8.71266  13.14616  1.000 38.48774  ? 187 TRP B NE1 1 
ATOM   1476 C  CE2 . TRP B 1 187 ? 29.06059  -7.53962  13.86111  1.000 42.19617  ? 187 TRP B CE2 1 
ATOM   1477 C  CE3 . TRP B 1 187 ? 27.42989  -5.84067  14.44063  1.000 37.07049  ? 187 TRP B CE3 1 
ATOM   1478 C  CZ2 . TRP B 1 187 ? 30.06752  -6.87133  14.55863  1.000 40.40871  ? 187 TRP B CZ2 1 
ATOM   1479 C  CZ3 . TRP B 1 187 ? 28.43539  -5.17681  15.13670  1.000 60.78567  ? 187 TRP B CZ3 1 
ATOM   1480 C  CH2 . TRP B 1 187 ? 29.73638  -5.69751  15.19349  1.000 47.56039  ? 187 TRP B CH2 1 
ATOM   1481 N  N   . THR B 1 188 ? 25.69777  -7.43722  9.66342   1.000 37.37037  ? 188 THR B N   1 
ATOM   1482 C  CA  . THR B 1 188 ? 26.72915  -6.82578  8.83564   1.000 42.43277  ? 188 THR B CA  1 
ATOM   1483 C  C   . THR B 1 188 ? 27.77333  -6.17546  9.74796   1.000 43.58708  ? 188 THR B C   1 
ATOM   1484 O  O   . THR B 1 188 ? 27.48835  -5.84600  10.90019  1.000 70.24222  ? 188 THR B O   1 
ATOM   1485 C  CB  . THR B 1 188 ? 26.08340  -5.76094  7.94062   1.000 35.02352  ? 188 THR B CB  1 
ATOM   1486 O  OG1 . THR B 1 188 ? 25.49735  -4.75296  8.77911   1.000 32.19747  ? 188 THR B OG1 1 
ATOM   1487 C  CG2 . THR B 1 188 ? 24.93530  -6.33935  7.12986   1.000 36.30469  ? 188 THR B CG2 1 
ATOM   1488 N  N   . THR B 1 189 ? 28.98922  -5.97467  9.23369   1.000 80.97466  ? 189 THR B N   1 
ATOM   1489 C  CA  . THR B 1 189 ? 29.95785  -5.18531  9.99356   1.000 84.31344  ? 189 THR B CA  1 
ATOM   1490 C  C   . THR B 1 189 ? 29.47836  -3.73529  10.10554  1.000 93.16670  ? 189 THR B C   1 
ATOM   1491 O  O   . THR B 1 189 ? 28.82255  -3.21426  9.19886   1.000 92.73649  ? 189 THR B O   1 
ATOM   1492 C  CB  . THR B 1 189 ? 31.33716  -5.21318  9.34319   1.000 98.35373  ? 189 THR B CB  1 
ATOM   1493 O  OG1 . THR B 1 189 ? 31.22357  -4.83630  7.96565   1.000 113.40599 ? 189 THR B OG1 1 
ATOM   1494 C  CG2 . THR B 1 189 ? 31.95663  -6.59530  9.45850   1.000 108.00905 ? 189 THR B CG2 1 
ATOM   1495 N  N   . PRO B 1 190 ? 29.79758  -3.05198  11.21039  1.000 62.24366  ? 190 PRO B N   1 
ATOM   1496 C  CA  . PRO B 1 190 ? 29.22931  -1.71950  11.45535  1.000 67.01440  ? 190 PRO B CA  1 
ATOM   1497 C  C   . PRO B 1 190 ? 29.95456  -0.56506  10.77778  1.000 71.36087  ? 190 PRO B C   1 
ATOM   1498 O  O   . PRO B 1 190 ? 29.61098  0.58979   11.04265  1.000 58.16901  ? 190 PRO B O   1 
ATOM   1499 C  CB  . PRO B 1 190 ? 29.32264  -1.59799  12.98364  1.000 59.10013  ? 190 PRO B CB  1 
ATOM   1500 C  CG  . PRO B 1 190 ? 30.51638  -2.41220  13.34547  1.000 73.49793  ? 190 PRO B CG  1 
ATOM   1501 C  CD  . PRO B 1 190 ? 30.54676  -3.56229  12.37192  1.000 78.77616  ? 190 PRO B CD  1 
ATOM   1502 N  N   . ASP B 1 191 ? 30.92609  -0.81252  9.89808   1.000 74.70298  ? 191 ASP B N   1 
ATOM   1503 C  CA  . ASP B 1 191 ? 31.56904  0.28199   9.17383   1.000 85.93332  ? 191 ASP B CA  1 
ATOM   1504 C  C   . ASP B 1 191 ? 30.70119  0.76682   8.01102   1.000 86.54790  ? 191 ASP B C   1 
ATOM   1505 O  O   . ASP B 1 191 ? 29.49978  0.47968   7.96825   1.000 75.87470  ? 191 ASP B O   1 
ATOM   1506 C  CB  . ASP B 1 191 ? 32.94468  -0.15168  8.66620   1.000 90.35027  ? 191 ASP B CB  1 
ATOM   1507 C  CG  . ASP B 1 191 ? 32.86355  -1.28468  7.67039   1.000 93.44078  ? 191 ASP B CG  1 
ATOM   1508 O  OD1 . ASP B 1 191 ? 32.10395  -2.24468  7.91116   1.000 89.64145  ? 191 ASP B OD1 1 
ATOM   1509 O  OD2 . ASP B 1 191 ? 33.56016  -1.21189  6.64010   1.000 99.80756  ? 191 ASP B OD2 1 
ATOM   1510 N  N   . THR B 1 192 ? 31.28631  1.50546   7.06044   1.000 77.86435  ? 192 THR B N   1 
ATOM   1511 C  CA  . THR B 1 192 ? 30.52574  2.05143   5.93865   1.000 84.99773  ? 192 THR B CA  1 
ATOM   1512 C  C   . THR B 1 192 ? 31.05082  1.56248   4.58481   1.000 80.57742  ? 192 THR B C   1 
ATOM   1513 O  O   . THR B 1 192 ? 30.87208  2.23445   3.56620   1.000 72.92045  ? 192 THR B O   1 
ATOM   1514 C  CB  . THR B 1 192 ? 30.50323  3.58290   5.98795   1.000 80.37476  ? 192 THR B CB  1 
ATOM   1515 O  OG1 . THR B 1 192 ? 31.82575  4.09861   5.80533   1.000 92.03504  ? 192 THR B OG1 1 
ATOM   1516 C  CG2 . THR B 1 192 ? 29.96208  4.07745   7.32004   1.000 70.32419  ? 192 THR B CG2 1 
ATOM   1517 N  N   . SER B 1 193 ? 31.69496  0.36522   4.55368   1.000 86.56364  ? 193 SER B N   1 
ATOM   1518 C  CA  . SER B 1 193 ? 32.18058  -0.22694  3.30718   1.000 77.50605  ? 193 SER B CA  1 
ATOM   1519 C  C   . SER B 1 193 ? 31.05222  -0.97274  2.58835   1.000 69.77890  ? 193 SER B C   1 
ATOM   1520 O  O   . SER B 1 193 ? 30.28778  -1.70453  3.22317   1.000 68.67912  ? 193 SER B O   1 
ATOM   1521 C  CB  . SER B 1 193 ? 33.33489  -1.18155  3.57859   1.000 70.95063  ? 193 SER B CB  1 
ATOM   1522 O  OG  . SER B 1 193 ? 32.99150  -2.08947  4.60594   1.000 71.80311  ? 193 SER B OG  1 
ATOM   1523 N  N   . PRO B 1 194 ? 30.95229  -0.83062  1.26416   1.000 65.28994  ? 194 PRO B N   1 
ATOM   1524 C  CA  . PRO B 1 194 ? 29.75790  -1.30715  0.54627   1.000 48.76752  ? 194 PRO B CA  1 
ATOM   1525 C  C   . PRO B 1 194 ? 29.61230  -2.82155  0.58898   1.000 53.12788  ? 194 PRO B C   1 
ATOM   1526 O  O   . PRO B 1 194 ? 30.55898  -3.56505  0.31891   1.000 54.85189  ? 194 PRO B O   1 
ATOM   1527 C  CB  . PRO B 1 194 ? 29.98325  -0.81483  -0.88904  1.000 49.53038  ? 194 PRO B CB  1 
ATOM   1528 C  CG  . PRO B 1 194 ? 30.97712  0.27713   -0.77173  1.000 64.49394  ? 194 PRO B CG  1 
ATOM   1529 C  CD  . PRO B 1 194 ? 31.86537  -0.09065  0.38059   1.000 64.78661  ? 194 PRO B CD  1 
ATOM   1530 N  N   . ASN B 1 195 ? 28.38765  -3.27354  0.88076   1.000 38.63802  ? 195 ASN B N   1 
ATOM   1531 C  CA  . ASN B 1 195 ? 28.10016  -4.69559  0.98396   1.000 33.02837  ? 195 ASN B CA  1 
ATOM   1532 C  C   . ASN B 1 195 ? 26.85527  -5.10261  0.21250   1.000 35.01856  ? 195 ASN B C   1 
ATOM   1533 O  O   . ASN B 1 195 ? 26.42336  -6.25427  0.31960   1.000 39.39320  ? 195 ASN B O   1 
ATOM   1534 C  CB  . ASN B 1 195 ? 27.94323  -5.09627  2.46513   1.000 32.38537  ? 195 ASN B CB  1 
ATOM   1535 C  CG  . ASN B 1 195 ? 26.88658  -4.28173  3.19865   1.000 32.25036  ? 195 ASN B CG  1 
ATOM   1536 O  OD1 . ASN B 1 195 ? 26.05645  -3.57870  2.59012   1.000 31.94692  ? 195 ASN B OD1 1 
ATOM   1537 N  ND2 . ASN B 1 195 ? 26.88811  -4.40218  4.53353   1.000 31.81684  ? 195 ASN B ND2 1 
ATOM   1538 N  N   . CYS B 1 196 ? 26.27013  -4.20107  -0.56596  1.000 33.70003  ? 196 CYS B N   1 
ATOM   1539 C  CA  . CYS B 1 196 ? 24.91746  -4.39687  -1.03515  1.000 29.97166  ? 196 CYS B CA  1 
ATOM   1540 C  C   . CYS B 1 196 ? 24.80562  -3.82207  -2.43483  1.000 36.00391  ? 196 CYS B C   1 
ATOM   1541 O  O   . CYS B 1 196 ? 25.48371  -2.84791  -2.77209  1.000 37.22362  ? 196 CYS B O   1 
ATOM   1542 C  CB  . CYS B 1 196 ? 23.92823  -3.73838  -0.02870  1.000 38.61852  ? 196 CYS B CB  1 
ATOM   1543 S  SG  . CYS B 1 196 ? 22.17317  -3.87168  -0.40406  1.000 39.05142  ? 196 CYS B SG  1 
ATOM   1544 N  N   . THR B 1 197 ? 23.96942  -4.45525  -3.25782  1.000 36.66514  ? 197 THR B N   1 
ATOM   1545 C  CA  . THR B 1 197 ? 23.78880  -4.07790  -4.65878  1.000 32.67647  ? 197 THR B CA  1 
ATOM   1546 C  C   . THR B 1 197 ? 22.30918  -3.80091  -4.88119  1.000 41.60347  ? 197 THR B C   1 
ATOM   1547 O  O   . THR B 1 197 ? 21.48540  -4.71471  -4.79240  1.000 36.42547  ? 197 THR B O   1 
ATOM   1548 C  CB  . THR B 1 197 ? 24.30095  -5.17724  -5.58597  1.000 36.89713  ? 197 THR B CB  1 
ATOM   1549 O  OG1 . THR B 1 197 ? 25.70759  -5.34808  -5.36609  1.000 38.36632  ? 197 THR B OG1 1 
ATOM   1550 C  CG2 . THR B 1 197 ? 24.07637  -4.80480  -7.04406  1.000 39.05431  ? 197 THR B CG2 1 
ATOM   1551 N  N   . ILE B 1 198 ? 21.96626  -2.54032  -5.13629  1.000 38.74690  ? 198 ILE B N   1 
ATOM   1552 C  CA  . ILE B 1 198 ? 20.57365  -2.18292  -5.39459  1.000 32.01280  ? 198 ILE B CA  1 
ATOM   1553 C  C   . ILE B 1 198 ? 20.39168  -2.06679  -6.90503  1.000 32.14643  ? 198 ILE B C   1 
ATOM   1554 O  O   . ILE B 1 198 ? 19.59383  -2.79334  -7.50326  1.000 48.71367  ? 198 ILE B O   1 
ATOM   1555 C  CB  . ILE B 1 198 ? 20.18051  -0.86759  -4.70672  1.000 26.47285  ? 198 ILE B CB  1 
ATOM   1556 C  CG1 . ILE B 1 198 ? 20.45104  -0.93150  -3.19179  1.000 30.39921  ? 198 ILE B CG1 1 
ATOM   1557 C  CG2 . ILE B 1 198 ? 18.69767  -0.50303  -5.00245  1.000 34.16607  ? 198 ILE B CG2 1 
ATOM   1558 C  CD1 . ILE B 1 198 ? 20.27071  0.40443   -2.51565  1.000 34.31931  ? 198 ILE B CD1 1 
ATOM   1559 N  N   . ALA B 1 199 ? 21.10447  -1.12687  -7.51209  1.000 34.10793  ? 199 ALA B N   1 
ATOM   1560 C  CA  . ALA B 1 199 ? 21.03601  -0.85923  -8.94848  1.000 34.24270  ? 199 ALA B CA  1 
ATOM   1561 C  C   . ALA B 1 199 ? 22.34332  -1.11332  -9.68022  1.000 43.64833  ? 199 ALA B C   1 
ATOM   1562 O  O   . ALA B 1 199 ? 22.31883  -1.39639  -10.88175 1.000 44.21261  ? 199 ALA B O   1 
ATOM   1563 C  CB  . ALA B 1 199 ? 20.60289  0.59849   -9.18668  1.000 36.35670  ? 199 ALA B CB  1 
ATOM   1564 N  N   . GLN B 1 200 ? 23.48293  -1.00631  -9.00612  1.000 38.26892  ? 200 GLN B N   1 
ATOM   1565 C  CA  . GLN B 1 200 ? 24.76568  -1.39448  -9.57412  1.000 39.37767  ? 200 GLN B CA  1 
ATOM   1566 C  C   . GLN B 1 200 ? 25.60582  -2.01330  -8.46442  1.000 42.94129  ? 200 GLN B C   1 
ATOM   1567 O  O   . GLN B 1 200 ? 25.30069  -1.87957  -7.28008  1.000 40.71228  ? 200 GLN B O   1 
ATOM   1568 C  CB  . GLN B 1 200 ? 25.48860  -0.20437  -10.22306 1.000 42.15454  ? 200 GLN B CB  1 
ATOM   1569 C  CG  . GLN B 1 200 ? 26.14476  0.73867   -9.22866  1.000 49.87553  ? 200 GLN B CG  1 
ATOM   1570 C  CD  . GLN B 1 200 ? 26.64338  2.02797   -9.85754  1.000 48.83224  ? 200 GLN B CD  1 
ATOM   1571 O  OE1 . GLN B 1 200 ? 26.05667  2.53978   -10.81300 1.000 49.81213  ? 200 GLN B OE1 1 
ATOM   1572 N  NE2 . GLN B 1 200 ? 27.72122  2.56725   -9.31078  1.000 53.12220  ? 200 GLN B NE2 1 
ATOM   1573 N  N   . ASP B 1 201 ? 26.68703  -2.68538  -8.84971  1.000 44.73545  ? 201 ASP B N   1 
ATOM   1574 C  CA  . ASP B 1 201 ? 27.38934  -3.54544  -7.90474  1.000 37.64405  ? 201 ASP B CA  1 
ATOM   1575 C  C   . ASP B 1 201 ? 27.99585  -2.73493  -6.76338  1.000 38.73365  ? 201 ASP B C   1 
ATOM   1576 O  O   . ASP B 1 201 ? 28.66587  -1.72435  -6.98887  1.000 42.11494  ? 201 ASP B O   1 
ATOM   1577 C  CB  . ASP B 1 201 ? 28.47944  -4.33960  -8.63279  1.000 56.96761  ? 201 ASP B CB  1 
ATOM   1578 C  CG  . ASP B 1 201 ? 29.09879  -5.41225  -7.76122  1.000 68.56471  ? 201 ASP B CG  1 
ATOM   1579 O  OD1 . ASP B 1 201 ? 28.36601  -6.04000  -6.96367  1.000 78.97368  ? 201 ASP B OD1 1 
ATOM   1580 O  OD2 . ASP B 1 201 ? 30.32104  -5.62862  -7.87192  1.000 85.99880  ? 201 ASP B OD2 1 
ATOM   1581 N  N   . LYS B 1 202 ? 27.73162  -3.16918  -5.52611  1.000 36.39211  ? 202 LYS B N   1 
ATOM   1582 C  CA  . LYS B 1 202 ? 28.34474  -2.57588  -4.33871  1.000 38.54524  ? 202 LYS B CA  1 
ATOM   1583 C  C   . LYS B 1 202 ? 28.06933  -1.07326  -4.24124  1.000 51.39630  ? 202 LYS B C   1 
ATOM   1584 O  O   . LYS B 1 202 ? 28.94106  -0.28145  -3.87374  1.000 41.43523  ? 202 LYS B O   1 
ATOM   1585 C  CB  . LYS B 1 202 ? 29.85105  -2.85901  -4.30831  1.000 50.96112  ? 202 LYS B CB  1 
ATOM   1586 C  CG  . LYS B 1 202 ? 30.19001  -4.33893  -4.15037  1.000 60.70743  ? 202 LYS B CG  1 
ATOM   1587 C  CD  . LYS B 1 202 ? 29.42457  -4.95086  -2.97643  1.000 58.12864  ? 202 LYS B CD  1 
ATOM   1588 N  N   . ASP B 1 203 ? 26.84852  -0.66797  -4.56773  1.000 34.39283  ? 203 ASP B N   1 
ATOM   1589 C  CA  . ASP B 1 203 ? 26.48213  0.74175   -4.50633  1.000 33.43867  ? 203 ASP B CA  1 
ATOM   1590 C  C   . ASP B 1 203 ? 25.95396  1.16919   -3.14643  1.000 31.89495  ? 203 ASP B C   1 
ATOM   1591 O  O   . ASP B 1 203 ? 25.62009  2.34476   -2.96246  1.000 31.76733  ? 203 ASP B O   1 
ATOM   1592 C  CB  . ASP B 1 203 ? 25.44370  1.07802   -5.58728  1.000 33.73822  ? 203 ASP B CB  1 
ATOM   1593 C  CG  . ASP B 1 203 ? 24.11516  0.31174   -5.42545  1.000 51.52572  ? 203 ASP B CG  1 
ATOM   1594 O  OD1 . ASP B 1 203 ? 23.87506  -0.38377  -4.40415  1.000 43.81657  ? 203 ASP B OD1 1 
ATOM   1595 O  OD2 . ASP B 1 203 ? 23.28053  0.43464   -6.34419  1.000 41.27838  ? 203 ASP B OD2 1 
ATOM   1596 N  N   . SER B 1 204 ? 25.86400  0.25905   -2.18448  1.000 29.07912  ? 204 SER B N   1 
ATOM   1597 C  CA  . SER B 1 204 ? 25.26150  0.64192   -0.92382  1.000 27.42340  ? 204 SER B CA  1 
ATOM   1598 C  C   . SER B 1 204 ? 25.87140  -0.15817  0.21543   1.000 27.26775  ? 204 SER B C   1 
ATOM   1599 O  O   . SER B 1 204 ? 26.43539  -1.24103  0.02991   1.000 29.04528  ? 204 SER B O   1 
ATOM   1600 C  CB  . SER B 1 204 ? 23.73541  0.46403   -0.96565  1.000 40.79832  ? 204 SER B CB  1 
ATOM   1601 O  OG  . SER B 1 204 ? 23.36892  -0.80661  -1.48672  1.000 37.88563  ? 204 SER B OG  1 
ATOM   1602 N  N   . LYS B 1 205 ? 25.73129  0.39694   1.40583   1.000 27.32361  ? 205 LYS B N   1 
ATOM   1603 C  CA  . LYS B 1 205 ? 26.11576  -0.26092  2.65459   1.000 26.75871  ? 205 LYS B CA  1 
ATOM   1604 C  C   . LYS B 1 205 ? 24.86229  -0.37425  3.52442   1.000 30.23321  ? 205 LYS B C   1 
ATOM   1605 O  O   . LYS B 1 205 ? 24.40246  0.61699   4.10037   1.000 25.59609  ? 205 LYS B O   1 
ATOM   1606 C  CB  . LYS B 1 205 ? 27.22862  0.52073   3.34890   1.000 32.10102  ? 205 LYS B CB  1 
ATOM   1607 C  CG  . LYS B 1 205 ? 27.49508  0.14935   4.81136   1.000 46.38477  ? 205 LYS B CG  1 
ATOM   1608 C  CD  . LYS B 1 205 ? 27.57102  -1.35537  5.01470   1.000 60.99352  ? 205 LYS B CD  1 
ATOM   1609 C  CE  . LYS B 1 205 ? 27.80066  -1.73677  6.46987   1.000 51.03753  ? 205 LYS B CE  1 
ATOM   1610 N  NZ  . LYS B 1 205 ? 29.26891  -1.69136  6.76009   1.000 57.59852  ? 205 LYS B NZ  1 
ATOM   1611 N  N   . LEU B 1 206 ? 24.31362  -1.58269  3.61239   1.000 29.52772  ? 206 LEU B N   1 
ATOM   1612 C  CA  . LEU B 1 206 ? 23.24529  -1.86765  4.56509   1.000 27.06556  ? 206 LEU B CA  1 
ATOM   1613 C  C   . LEU B 1 206 ? 23.85425  -2.20325  5.91857   1.000 24.49715  ? 206 LEU B C   1 
ATOM   1614 O  O   . LEU B 1 206 ? 24.74994  -3.04843  6.00490   1.000 27.81594  ? 206 LEU B O   1 
ATOM   1615 C  CB  . LEU B 1 206 ? 22.39364  -3.03870  4.07011   1.000 28.30306  ? 206 LEU B CB  1 
ATOM   1616 C  CG  . LEU B 1 206 ? 21.25964  -3.44516  5.01775   1.000 26.88414  ? 206 LEU B CG  1 
ATOM   1617 C  CD1 . LEU B 1 206 ? 20.09365  -2.45057  4.89150   1.000 26.80338  ? 206 LEU B CD1 1 
ATOM   1618 C  CD2 . LEU B 1 206 ? 20.80773  -4.86443  4.72137   1.000 30.93732  ? 206 LEU B CD2 1 
ATOM   1619 N  N   . THR B 1 207 ? 23.42349  -1.52070  6.97900   1.000 22.43502  ? 207 THR B N   1 
ATOM   1620 C  CA  . THR B 1 207 ? 23.79912  -1.94703  8.33522   1.000 23.12752  ? 207 THR B CA  1 
ATOM   1621 C  C   . THR B 1 207 ? 22.57636  -2.59572  8.95837   1.000 30.16445  ? 207 THR B C   1 
ATOM   1622 O  O   . THR B 1 207 ? 21.54663  -1.93962  9.13183   1.000 26.35692  ? 207 THR B O   1 
ATOM   1623 C  CB  . THR B 1 207 ? 24.30508  -0.79706  9.19850   1.000 28.58736  ? 207 THR B CB  1 
ATOM   1624 O  OG1 . THR B 1 207 ? 25.37827  -0.13353  8.53116   1.000 33.11310  ? 207 THR B OG1 1 
ATOM   1625 C  CG2 . THR B 1 207 ? 24.82119  -1.34048  10.57851  1.000 32.94922  ? 207 THR B CG2 1 
ATOM   1626 N  N   . LEU B 1 208 ? 22.67130  -3.88774  9.25053   1.000 26.28428  ? 208 LEU B N   1 
ATOM   1627 C  CA  . LEU B 1 208 ? 21.55799  -4.64818  9.80466   1.000 28.45336  ? 208 LEU B CA  1 
ATOM   1628 C  C   . LEU B 1 208 ? 22.11440  -5.49726  10.93390  1.000 29.56190  ? 208 LEU B C   1 
ATOM   1629 O  O   . LEU B 1 208 ? 23.06258  -6.26312  10.72050  1.000 25.74423  ? 208 LEU B O   1 
ATOM   1630 C  CB  . LEU B 1 208 ? 20.90024  -5.52525  8.72105   1.000 26.43359  ? 208 LEU B CB  1 
ATOM   1631 C  CG  . LEU B 1 208 ? 19.74404  -6.38729  9.23850   1.000 26.28261  ? 208 LEU B CG  1 
ATOM   1632 C  CD1 . LEU B 1 208 ? 18.60093  -5.52560  9.83389   1.000 24.70748  ? 208 LEU B CD1 1 
ATOM   1633 C  CD2 . LEU B 1 208 ? 19.21653  -7.30964  8.13547   1.000 26.30364  ? 208 LEU B CD2 1 
ATOM   1634 N  N   . VAL B 1 209 ? 21.56468  -5.32605  12.13614  1.000 21.09277  ? 209 VAL B N   1 
ATOM   1635 C  CA  . VAL B 1 209 ? 21.96062  -6.08757  13.31511  1.000 22.60091  ? 209 VAL B CA  1 
ATOM   1636 C  C   . VAL B 1 209 ? 20.73292  -6.82781  13.80080  1.000 21.22232  ? 209 VAL B C   1 
ATOM   1637 O  O   . VAL B 1 209 ? 19.70729  -6.20488  14.10956  1.000 25.00492  ? 209 VAL B O   1 
ATOM   1638 C  CB  . VAL B 1 209 ? 22.54044  -5.18271  14.41336  1.000 23.42902  ? 209 VAL B CB  1 
ATOM   1639 C  CG1 . VAL B 1 209 ? 23.12197  -6.02386  15.54134  1.000 25.87794  ? 209 VAL B CG1 1 
ATOM   1640 C  CG2 . VAL B 1 209 ? 23.61159  -4.27493  13.84077  1.000 27.20906  ? 209 VAL B CG2 1 
ATOM   1641 N  N   . LEU B 1 210 ? 20.83032  -8.15388  13.84155  1.000 25.16834  ? 210 LEU B N   1 
ATOM   1642 C  CA  . LEU B 1 210 ? 19.77053  -9.02020  14.34509  1.000 22.26171  ? 210 LEU B CA  1 
ATOM   1643 C  C   . LEU B 1 210 ? 20.25583  -9.67323  15.62361  1.000 29.32998  ? 210 LEU B C   1 
ATOM   1644 O  O   . LEU B 1 210 ? 21.25387  -10.40346 15.60394  1.000 29.60244  ? 210 LEU B O   1 
ATOM   1645 C  CB  . LEU B 1 210 ? 19.39106  -10.07928 13.30601  1.000 24.84371  ? 210 LEU B CB  1 
ATOM   1646 C  CG  . LEU B 1 210 ? 18.94696  -9.60318  11.92383  1.000 30.39561  ? 210 LEU B CG  1 
ATOM   1647 C  CD1 . LEU B 1 210 ? 18.54575  -10.81093 11.07179  1.000 28.47501  ? 210 LEU B CD1 1 
ATOM   1648 C  CD2 . LEU B 1 210 ? 17.79045  -8.60959  12.06467  1.000 25.07558  ? 210 LEU B CD2 1 
ATOM   1649 N  N   . THR B 1 211 ? 19.55478  -9.43448  16.72673  1.000 24.85612  ? 211 THR B N   1 
ATOM   1650 C  CA  . THR B 1 211 ? 19.89584  -10.05738 17.99818  1.000 25.11190  ? 211 THR B CA  1 
ATOM   1651 C  C   . THR B 1 211 ? 18.74275  -10.91377 18.48865  1.000 29.88701  ? 211 THR B C   1 
ATOM   1652 O  O   . THR B 1 211 ? 17.60175  -10.44774 18.54835  1.000 26.46211  ? 211 THR B O   1 
ATOM   1653 C  CB  . THR B 1 211 ? 20.24794  -9.00617  19.04356  1.000 33.57850  ? 211 THR B CB  1 
ATOM   1654 O  OG1 . THR B 1 211 ? 21.33041  -8.21812  18.53571  1.000 34.15199  ? 211 THR B OG1 1 
ATOM   1655 C  CG2 . THR B 1 211 ? 20.65978  -9.69982  20.34357  1.000 36.89091  ? 211 THR B CG2 1 
ATOM   1656 N  N   . LYS B 1 212 ? 19.04659  -12.15421 18.87324  1.000 29.41931  ? 212 LYS B N   1 
ATOM   1657 C  CA  . LYS B 1 212 ? 18.01024  -13.11362 19.23564  1.000 27.68053  ? 212 LYS B CA  1 
ATOM   1658 C  C   . LYS B 1 212 ? 17.70620  -12.94644 20.71038  1.000 34.45342  ? 212 LYS B C   1 
ATOM   1659 O  O   . LYS B 1 212 ? 18.56414  -13.20588 21.55784  1.000 37.35714  ? 212 LYS B O   1 
ATOM   1660 C  CB  . LYS B 1 212 ? 18.43316  -14.54801 18.90741  1.000 32.18959  ? 212 LYS B CB  1 
ATOM   1661 C  CG  . LYS B 1 212 ? 17.31088  -15.54590 19.14093  1.000 29.23305  ? 212 LYS B CG  1 
ATOM   1662 C  CD  . LYS B 1 212 ? 17.66919  -16.94226 18.65042  1.000 34.86516  ? 212 LYS B CD  1 
ATOM   1663 C  CE  . LYS B 1 212 ? 16.55000  -17.91604 18.97954  1.000 40.24102  ? 212 LYS B CE  1 
ATOM   1664 N  NZ  . LYS B 1 212 ? 15.24440  -17.52110 18.37624  1.000 36.34356  ? 212 LYS B NZ  1 
ATOM   1665 N  N   . CYS B 1 213 ? 16.49858  -12.47163 21.01308  1.000 29.73619  ? 213 CYS B N   1 
ATOM   1666 C  CA  . CYS B 1 213 ? 15.98949  -12.36283 22.38118  1.000 36.82558  ? 213 CYS B CA  1 
ATOM   1667 C  C   . CYS B 1 213 ? 14.88124  -13.40363 22.53817  1.000 41.97285  ? 213 CYS B C   1 
ATOM   1668 O  O   . CYS B 1 213 ? 13.69493  -13.08295 22.51866  1.000 41.79519  ? 213 CYS B O   1 
ATOM   1669 C  CB  . CYS B 1 213 ? 15.47172  -10.95016 22.65177  1.000 36.42146  ? 213 CYS B CB  1 
ATOM   1670 S  SG  . CYS B 1 213 ? 16.60044  -9.61122  22.17195  1.000 51.65256  ? 213 CYS B SG  1 
ATOM   1671 N  N   . GLY B 1 214 ? 15.27186  -14.65949 22.64090  1.000 46.33661  ? 214 GLY B N   1 
ATOM   1672 C  CA  . GLY B 1 214 ? 14.29548  -15.73148 22.73765  1.000 35.20464  ? 214 GLY B CA  1 
ATOM   1673 C  C   . GLY B 1 214 ? 13.42636  -15.79108 21.49280  1.000 39.65485  ? 214 GLY B C   1 
ATOM   1674 O  O   . GLY B 1 214 ? 13.90770  -15.94852 20.36815  1.000 42.41169  ? 214 GLY B O   1 
ATOM   1675 N  N   . SER B 1 215 ? 12.11867  -15.65703 21.68386  1.000 35.85348  ? 215 SER B N   1 
ATOM   1676 C  CA  . SER B 1 215 ? 11.16860  -15.87971 20.60705  1.000 35.30828  ? 215 SER B CA  1 
ATOM   1677 C  C   . SER B 1 215 ? 11.04685  -14.68718 19.67496  1.000 28.73707  ? 215 SER B C   1 
ATOM   1678 O  O   . SER B 1 215 ? 10.26252  -14.75031 18.72147  1.000 30.36281  ? 215 SER B O   1 
ATOM   1679 C  CB  . SER B 1 215 ? 9.79586   -16.22367 21.19592  1.000 60.29891  ? 215 SER B CB  1 
ATOM   1680 O  OG  . SER B 1 215 ? 8.84061   -16.48779 20.18552  1.000 77.27996  ? 215 SER B OG  1 
ATOM   1681 N  N   . GLN B 1 216 ? 11.76579  -13.59568 19.94312  1.000 26.93197  ? 216 GLN B N   1 
ATOM   1682 C  CA  . GLN B 1 216 ? 11.71482  -12.41180 19.09464  1.000 25.32878  ? 216 GLN B CA  1 
ATOM   1683 C  C   . GLN B 1 216 ? 13.11669  -12.02630 18.67180  1.000 27.35422  ? 216 GLN B C   1 
ATOM   1684 O  O   . GLN B 1 216 ? 14.06830  -12.16391 19.44700  1.000 28.39928  ? 216 GLN B O   1 
ATOM   1685 C  CB  . GLN B 1 216 ? 11.07637  -11.17903 19.81004  1.000 28.97797  ? 216 GLN B CB  1 
ATOM   1686 C  CG  . GLN B 1 216 ? 9.59080   -11.03397 19.65683  1.000 31.91295  ? 216 GLN B CG  1 
ATOM   1687 C  CD  . GLN B 1 216 ? 9.06963   -9.80493  20.41795  1.000 24.23299  ? 216 GLN B CD  1 
ATOM   1688 O  OE1 . GLN B 1 216 ? 9.18427   -8.67206  19.95396  1.000 26.42737  ? 216 GLN B OE1 1 
ATOM   1689 N  NE2 . GLN B 1 216 ? 8.53383   -10.03548 21.59971  1.000 24.38798  ? 216 GLN B NE2 1 
ATOM   1690 N  N   . ILE B 1 217 ? 13.23610  -11.51400 17.45264  1.000 23.61257  ? 217 ILE B N   1 
ATOM   1691 C  CA  . ILE B 1 217 ? 14.49418  -10.97349 16.95888  1.000 22.79014  ? 217 ILE B CA  1 
ATOM   1692 C  C   . ILE B 1 217 ? 14.40186  -9.46170  17.05669  1.000 22.48875  ? 217 ILE B C   1 
ATOM   1693 O  O   . ILE B 1 217 ? 13.44107  -8.85907  16.55640  1.000 23.71011  ? 217 ILE B O   1 
ATOM   1694 C  CB  . ILE B 1 217 ? 14.76404  -11.39798 15.50658  1.000 22.76299  ? 217 ILE B CB  1 
ATOM   1695 C  CG1 . ILE B 1 217 ? 14.68933  -12.92935 15.36845  1.000 26.46040  ? 217 ILE B CG1 1 
ATOM   1696 C  CG2 . ILE B 1 217 ? 16.08097  -10.79565 15.05940  1.000 22.62437  ? 217 ILE B CG2 1 
ATOM   1697 C  CD1 . ILE B 1 217 ? 15.59605  -13.73460 16.29087  1.000 29.63352  ? 217 ILE B CD1 1 
ATOM   1698 N  N   . LEU B 1 218 ? 15.35583  -8.85748  17.76189  1.000 22.56377  ? 218 LEU B N   1 
ATOM   1699 C  CA  . LEU B 1 218 ? 15.47478  -7.41619  17.85382  1.000 22.21658  ? 218 LEU B CA  1 
ATOM   1700 C  C   . LEU B 1 218 ? 16.36224  -6.94902  16.70875  1.000 23.86668  ? 218 LEU B C   1 
ATOM   1701 O  O   . LEU B 1 218 ? 17.50073  -7.40516  16.57820  1.000 21.00375  ? 218 LEU B O   1 
ATOM   1702 C  CB  . LEU B 1 218 ? 16.05932  -6.99858  19.20443  1.000 21.83034  ? 218 LEU B CB  1 
ATOM   1703 C  CG  . LEU B 1 218 ? 16.23586  -5.48767  19.44756  1.000 21.47411  ? 218 LEU B CG  1 
ATOM   1704 C  CD1 . LEU B 1 218 ? 14.87630  -4.80563  19.53140  1.000 23.04472  ? 218 LEU B CD1 1 
ATOM   1705 C  CD2 . LEU B 1 218 ? 17.00310  -5.27438  20.77494  1.000 25.24038  ? 218 LEU B CD2 1 
ATOM   1706 N  N   . ALA B 1 219 ? 15.83976  -6.06925  15.86442  1.000 19.02623  ? 219 ALA B N   1 
ATOM   1707 C  CA  . ALA B 1 219 ? 16.50777  -5.68729  14.63244  1.000 22.19038  ? 219 ALA B CA  1 
ATOM   1708 C  C   . ALA B 1 219 ? 16.80403  -4.19552  14.62701  1.000 28.00054  ? 219 ALA B C   1 
ATOM   1709 O  O   . ALA B 1 219 ? 15.96710  -3.38119  15.04145  1.000 23.03289  ? 219 ALA B O   1 
ATOM   1710 C  CB  . ALA B 1 219 ? 15.61527  -6.05487  13.42760  1.000 21.42934  ? 219 ALA B CB  1 
ATOM   1711 N  N   . ASN B 1 220 ? 17.96941  -3.82812  14.11810  1.000 22.11708  ? 220 ASN B N   1 
ATOM   1712 C  CA  . ASN B 1 220 ? 18.35409  -2.42646  14.00661  1.000 19.49576  ? 220 ASN B CA  1 
ATOM   1713 C  C   . ASN B 1 220 ? 18.88714  -2.23417  12.59545  1.000 20.34753  ? 220 ASN B C   1 
ATOM   1714 O  O   . ASN B 1 220 ? 19.73011  -3.01914  12.15435  1.000 22.54889  ? 220 ASN B O   1 
ATOM   1715 C  CB  . ASN B 1 220 ? 19.40911  -2.08940  15.07823  1.000 20.62311  ? 220 ASN B CB  1 
ATOM   1716 C  CG  . ASN B 1 220 ? 19.81854  -0.64022  15.05310  1.000 35.93747  ? 220 ASN B CG  1 
ATOM   1717 O  OD1 . ASN B 1 220 ? 20.71816  -0.24766  14.30007  1.000 34.41668  ? 220 ASN B OD1 1 
ATOM   1718 N  ND2 . ASN B 1 220 ? 19.16764  0.17589   15.87804  1.000 34.66474  ? 220 ASN B ND2 1 
ATOM   1719 N  N   . VAL B 1 221 ? 18.37138  -1.24475  11.86184  1.000 20.61943  ? 221 VAL B N   1 
ATOM   1720 C  CA  . VAL B 1 221 ? 18.70840  -1.13567  10.43571  1.000 22.46774  ? 221 VAL B CA  1 
ATOM   1721 C  C   . VAL B 1 221 ? 18.97362  0.32419   10.05343  1.000 23.98151  ? 221 VAL B C   1 
ATOM   1722 O  O   . VAL B 1 221 ? 18.33630  1.24788   10.56929  1.000 22.45822  ? 221 VAL B O   1 
ATOM   1723 C  CB  . VAL B 1 221 ? 17.58769  -1.73790  9.55565   1.000 19.14232  ? 221 VAL B CB  1 
ATOM   1724 C  CG1 . VAL B 1 221 ? 16.32120  -0.90578  9.67549   1.000 21.98904  ? 221 VAL B CG1 1 
ATOM   1725 C  CG2 . VAL B 1 221 ? 18.02203  -1.84589  8.05518   1.000 20.96501  ? 221 VAL B CG2 1 
ATOM   1726 N  N   . SER B 1 222 ? 19.94412  0.52899   9.15080   1.000 20.92709  ? 222 SER B N   1 
ATOM   1727 C  CA  . SER B 1 222 ? 20.15301  1.81766   8.50032   1.000 19.72911  ? 222 SER B CA  1 
ATOM   1728 C  C   . SER B 1 222 ? 20.80608  1.56018   7.14695   1.000 22.45695  ? 222 SER B C   1 
ATOM   1729 O  O   . SER B 1 222 ? 21.28702  0.45739   6.86956   1.000 26.31218  ? 222 SER B O   1 
ATOM   1730 C  CB  . SER B 1 222 ? 21.02910  2.75242   9.33780   1.000 28.91926  ? 222 SER B CB  1 
ATOM   1731 O  OG  . SER B 1 222 ? 22.36327  2.26624   9.40549   1.000 32.13417  ? 222 SER B OG  1 
ATOM   1732 N  N   . LEU B 1 223 ? 20.82011  2.58560   6.30251   1.000 24.56201  ? 223 LEU B N   1 
ATOM   1733 C  CA  . LEU B 1 223 ? 21.32550  2.41894   4.94457   1.000 21.74080  ? 223 LEU B CA  1 
ATOM   1734 C  C   . LEU B 1 223 ? 22.09327  3.65128   4.48629   1.000 20.31351  ? 223 LEU B C   1 
ATOM   1735 O  O   . LEU B 1 223 ? 21.68134  4.79147   4.72671   1.000 24.74706  ? 223 LEU B O   1 
ATOM   1736 C  CB  . LEU B 1 223 ? 20.16161  2.13627   3.97804   1.000 22.45467  ? 223 LEU B CB  1 
ATOM   1737 C  CG  . LEU B 1 223 ? 20.52608  1.95826   2.50502   1.000 22.79454  ? 223 LEU B CG  1 
ATOM   1738 C  CD1 . LEU B 1 223 ? 21.31332  0.66623   2.27862   1.000 28.60338  ? 223 LEU B CD1 1 
ATOM   1739 C  CD2 . LEU B 1 223 ? 19.25281  2.01787   1.62235   1.000 28.90374  ? 223 LEU B CD2 1 
ATOM   1740 N  N   . ILE B 1 224 ? 23.22465  3.40452   3.81885   1.000 23.81002  ? 224 ILE B N   1 
ATOM   1741 C  CA  . ILE B 1 224 ? 23.97524  4.43337   3.10953   1.000 25.69508  ? 224 ILE B CA  1 
ATOM   1742 C  C   . ILE B 1 224 ? 24.07542  3.96390   1.66530   1.000 24.63805  ? 224 ILE B C   1 
ATOM   1743 O  O   . ILE B 1 224 ? 24.54951  2.84908   1.41407   1.000 32.52248  ? 224 ILE B O   1 
ATOM   1744 C  CB  . ILE B 1 224 ? 25.38363  4.63313   3.70810   1.000 24.65743  ? 224 ILE B CB  1 
ATOM   1745 C  CG1 . ILE B 1 224 ? 25.30682  5.08480   5.16972   1.000 29.30846  ? 224 ILE B CG1 1 
ATOM   1746 C  CG2 . ILE B 1 224 ? 26.20137  5.62327   2.83187   1.000 31.00942  ? 224 ILE B CG2 1 
ATOM   1747 C  CD1 . ILE B 1 224 ? 26.62903  4.91890   5.92274   1.000 41.58219  ? 224 ILE B CD1 1 
ATOM   1748 N  N   . VAL B 1 225 ? 23.58712  4.77099   0.73298   1.000 23.54277  ? 225 VAL B N   1 
ATOM   1749 C  CA  . VAL B 1 225 ? 23.84676  4.53383   -0.68321  1.000 22.48748  ? 225 VAL B CA  1 
ATOM   1750 C  C   . VAL B 1 225 ? 25.06125  5.37534   -1.04986  1.000 31.21913  ? 225 VAL B C   1 
ATOM   1751 O  O   . VAL B 1 225 ? 25.06417  6.58926   -0.83121  1.000 31.17224  ? 225 VAL B O   1 
ATOM   1752 C  CB  . VAL B 1 225 ? 22.63647  4.87115   -1.55618  1.000 23.83802  ? 225 VAL B CB  1 
ATOM   1753 C  CG1 . VAL B 1 225 ? 22.93151  4.48092   -3.00178  1.000 28.03315  ? 225 VAL B CG1 1 
ATOM   1754 C  CG2 . VAL B 1 225 ? 21.39780  4.11130   -1.01833  1.000 25.94961  ? 225 VAL B CG2 1 
ATOM   1755 N  N   . VAL B 1 226 ? 26.09913  4.72808   -1.59167  1.000 33.26360  ? 226 VAL B N   1 
ATOM   1756 C  CA  . VAL B 1 226 ? 27.35980  5.41752   -1.85851  1.000 38.74829  ? 226 VAL B CA  1 
ATOM   1757 C  C   . VAL B 1 226 ? 27.56706  5.75942   -3.33520  1.000 42.17974  ? 226 VAL B C   1 
ATOM   1758 O  O   . VAL B 1 226 ? 28.39199  6.63583   -3.63923  1.000 40.56258  ? 226 VAL B O   1 
ATOM   1759 C  CB  . VAL B 1 226 ? 28.56122  4.59287   -1.33745  1.000 31.40338  ? 226 VAL B CB  1 
ATOM   1760 C  CG1 . VAL B 1 226 ? 28.43334  4.33483   0.15327   1.000 30.65485  ? 226 VAL B CG1 1 
ATOM   1761 C  CG2 . VAL B 1 226 ? 28.68325  3.28819   -2.09136  1.000 43.38736  ? 226 VAL B CG2 1 
ATOM   1762 N  N   . ALA B 1 227 ? 26.84295  5.11940   -4.25450  1.000 30.08271  ? 227 ALA B N   1 
ATOM   1763 C  CA  . ALA B 1 227 ? 27.04196  5.38353   -5.67471  1.000 36.98615  ? 227 ALA B CA  1 
ATOM   1764 C  C   . ALA B 1 227 ? 25.80386  4.96553   -6.46133  1.000 40.74299  ? 227 ALA B C   1 
ATOM   1765 O  O   . ALA B 1 227 ? 24.90662  4.29400   -5.94505  1.000 37.38063  ? 227 ALA B O   1 
ATOM   1766 C  CB  . ALA B 1 227 ? 28.28297  4.65701   -6.18548  1.000 38.05563  ? 227 ALA B CB  1 
ATOM   1767 N  N   . GLY B 1 228 ? 25.77423  5.36709   -7.73552  1.000 33.53053  ? 228 GLY B N   1 
ATOM   1768 C  CA  . GLY B 1 228 ? 24.73843  4.90916   -8.64200  1.000 43.81346  ? 228 GLY B CA  1 
ATOM   1769 C  C   . GLY B 1 228 ? 23.41918  5.66396   -8.53133  1.000 42.63394  ? 228 GLY B C   1 
ATOM   1770 O  O   . GLY B 1 228 ? 23.32198  6.76696   -7.96512  1.000 34.23240  ? 228 GLY B O   1 
ATOM   1771 N  N   . LYS B 1 229 ? 22.38173  5.02561   -9.09838  1.000 34.11810  ? 229 LYS B N   1 
ATOM   1772 C  CA  . LYS B 1 229 ? 21.07764  5.64427   -9.32588  1.000 37.12441  ? 229 LYS B CA  1 
ATOM   1773 C  C   . LYS B 1 229 ? 20.50930  6.30473   -8.07409  1.000 40.64737  ? 229 LYS B C   1 
ATOM   1774 O  O   . LYS B 1 229 ? 19.94176  7.40381   -8.14094  1.000 37.17324  ? 229 LYS B O   1 
ATOM   1775 C  CB  . LYS B 1 229 ? 20.11086  4.57650   -9.84211  1.000 36.41793  ? 229 LYS B CB  1 
ATOM   1776 C  CG  . LYS B 1 229 ? 18.70680  5.04462   -10.13889 1.000 40.04743  ? 229 LYS B CG  1 
ATOM   1777 C  CD  . LYS B 1 229 ? 17.95493  3.96141   -10.88681 1.000 42.26153  ? 229 LYS B CD  1 
ATOM   1778 C  CE  . LYS B 1 229 ? 16.46885  4.25182   -10.95271 1.000 54.29970  ? 229 LYS B CE  1 
ATOM   1779 N  NZ  . LYS B 1 229 ? 15.70855  3.12619   -11.56993 1.000 48.96374  ? 229 LYS B NZ  1 
ATOM   1780 N  N   . TYR B 1 230 ? 20.64428  5.65408   -6.92175  1.000 31.23737  ? 230 TYR B N   1 
ATOM   1781 C  CA  . TYR B 1 230 ? 19.94771  6.08997   -5.70982  1.000 26.43385  ? 230 TYR B CA  1 
ATOM   1782 C  C   . TYR B 1 230 ? 20.84732  6.86455   -4.77662  1.000 28.97587  ? 230 TYR B C   1 
ATOM   1783 O  O   . TYR B 1 230 ? 20.43988  7.21976   -3.66928  1.000 30.58529  ? 230 TYR B O   1 
ATOM   1784 C  CB  . TYR B 1 230 ? 19.34286  4.89304   -4.99327  1.000 30.47974  ? 230 TYR B CB  1 
ATOM   1785 C  CG  . TYR B 1 230 ? 18.28293  4.26771   -5.84609  1.000 31.17485  ? 230 TYR B CG  1 
ATOM   1786 C  CD1 . TYR B 1 230 ? 17.09161  4.94301   -6.10921  1.000 31.75838  ? 230 TYR B CD1 1 
ATOM   1787 C  CD2 . TYR B 1 230 ? 18.48845  3.02895   -6.44112  1.000 30.00554  ? 230 TYR B CD2 1 
ATOM   1788 C  CE1 . TYR B 1 230 ? 16.11875  4.37643   -6.93232  1.000 29.29364  ? 230 TYR B CE1 1 
ATOM   1789 C  CE2 . TYR B 1 230 ? 17.52865  2.45350   -7.26002  1.000 33.54698  ? 230 TYR B CE2 1 
ATOM   1790 C  CZ  . TYR B 1 230 ? 16.35009  3.12746   -7.50063  1.000 34.18320  ? 230 TYR B CZ  1 
ATOM   1791 O  OH  . TYR B 1 230 ? 15.40199  2.54098   -8.31034  1.000 38.76959  ? 230 TYR B OH  1 
ATOM   1792 N  N   . HIS B 1 231 ? 22.04543  7.17997   -5.22911  1.000 31.24671  ? 231 HIS B N   1 
ATOM   1793 C  CA  . HIS B 1 231 ? 23.00839  7.83812   -4.37050  1.000 34.18888  ? 231 HIS B CA  1 
ATOM   1794 C  C   . HIS B 1 231 ? 22.54860  9.24067   -3.98205  1.000 28.83410  ? 231 HIS B C   1 
ATOM   1795 O  O   . HIS B 1 231 ? 22.51988  9.59608   -2.79426  1.000 32.25750  ? 231 HIS B O   1 
ATOM   1796 C  CB  . HIS B 1 231 ? 24.32279  7.88701   -5.11645  1.000 40.80333  ? 231 HIS B CB  1 
ATOM   1797 C  CG  . HIS B 1 231 ? 25.37894  8.58295   -4.36556  1.000 29.85888  ? 231 HIS B CG  1 
ATOM   1798 N  ND1 . HIS B 1 231 ? 25.54902  8.38293   -3.01899  1.000 40.36117  ? 231 HIS B ND1 1 
ATOM   1799 C  CD2 . HIS B 1 231 ? 26.31925  9.47194   -4.75154  1.000 41.19578  ? 231 HIS B CD2 1 
ATOM   1800 C  CE1 . HIS B 1 231 ? 26.56056  9.10999   -2.61364  1.000 39.12167  ? 231 HIS B CE1 1 
ATOM   1801 N  NE2 . HIS B 1 231 ? 27.03754  9.79449   -3.63549  1.000 41.29563  ? 231 HIS B NE2 1 
ATOM   1802 N  N   . ILE B 1 232 ? 22.20536  10.05391  -4.97967  1.000 30.46976  ? 232 ILE B N   1 
ATOM   1803 C  CA  . ILE B 1 232 ? 21.68061  11.39924  -4.78437  1.000 29.36004  ? 232 ILE B CA  1 
ATOM   1804 C  C   . ILE B 1 232 ? 20.26699  11.42665  -5.35396  1.000 42.12928  ? 232 ILE B C   1 
ATOM   1805 O  O   . ILE B 1 232 ? 20.07304  11.16540  -6.54750  1.000 37.05479  ? 232 ILE B O   1 
ATOM   1806 C  CB  . ILE B 1 232 ? 22.55852  12.45312  -5.48031  1.000 34.61068  ? 232 ILE B CB  1 
ATOM   1807 C  CG1 . ILE B 1 232 ? 24.02882  12.27943  -5.08071  1.000 40.14273  ? 232 ILE B CG1 1 
ATOM   1808 C  CG2 . ILE B 1 232 ? 22.05551  13.85016  -5.15843  1.000 39.04074  ? 232 ILE B CG2 1 
ATOM   1809 C  CD1 . ILE B 1 232 ? 24.29267  12.54615  -3.63149  1.000 47.02046  ? 232 ILE B CD1 1 
ATOM   1810 N  N   . ILE B 1 233 ? 19.29027  11.76872  -4.52604  1.000 32.91547  ? 233 ILE B N   1 
ATOM   1811 C  CA  . ILE B 1 233 ? 17.89223  11.82231  -4.96487  1.000 25.20555  ? 233 ILE B CA  1 
ATOM   1812 C  C   . ILE B 1 233 ? 17.56761  13.21759  -5.49008  1.000 34.98345  ? 233 ILE B C   1 
ATOM   1813 O  O   . ILE B 1 233 ? 17.78909  14.22143  -4.80505  1.000 30.64628  ? 233 ILE B O   1 
ATOM   1814 C  CB  . ILE B 1 233 ? 16.94033  11.44612  -3.81589  1.000 32.34905  ? 233 ILE B CB  1 
ATOM   1815 C  CG1 . ILE B 1 233 ? 17.28706  10.06602  -3.26224  1.000 40.27640  ? 233 ILE B CG1 1 
ATOM   1816 C  CG2 . ILE B 1 233 ? 15.47811  11.53676  -4.28902  1.000 43.51613  ? 233 ILE B CG2 1 
ATOM   1817 C  CD1 . ILE B 1 233 ? 17.36678  8.99343   -4.33657  1.000 42.17182  ? 233 ILE B CD1 1 
ATOM   1818 N  N   . ASN B 1 234 ? 17.02274  13.29251  -6.70087  1.000 35.25689  ? 234 ASN B N   1 
ATOM   1819 C  CA  . ASN B 1 234 ? 16.45842  14.55286  -7.18519  1.000 35.66683  ? 234 ASN B CA  1 
ATOM   1820 C  C   . ASN B 1 234 ? 15.12459  14.23495  -7.84375  1.000 44.57066  ? 234 ASN B C   1 
ATOM   1821 O  O   . ASN B 1 234 ? 15.08795  13.80171  -8.99745  1.000 38.48978  ? 234 ASN B O   1 
ATOM   1822 C  CB  . ASN B 1 234 ? 17.37646  15.28030  -8.15036  1.000 36.61983  ? 234 ASN B CB  1 
ATOM   1823 C  CG  . ASN B 1 234 ? 16.90684  16.68971  -8.39978  1.000 40.12705  ? 234 ASN B CG  1 
ATOM   1824 O  OD1 . ASN B 1 234 ? 15.71388  16.96694  -8.32865  1.000 40.34018  ? 234 ASN B OD1 1 
ATOM   1825 N  ND2 . ASN B 1 234 ? 17.83652  17.59444  -8.62735  1.000 40.22091  ? 234 ASN B ND2 1 
ATOM   1826 N  N   . ASN B 1 235 ? 14.04184  14.45741  -7.10730  1.000 35.11124  ? 235 ASN B N   1 
ATOM   1827 C  CA  . ASN B 1 235 ? 12.70282  14.29557  -7.64725  1.000 31.99341  ? 235 ASN B CA  1 
ATOM   1828 C  C   . ASN B 1 235 ? 12.19231  15.53119  -8.36352  1.000 35.28131  ? 235 ASN B C   1 
ATOM   1829 O  O   . ASN B 1 235 ? 11.09128  15.48569  -8.91876  1.000 47.69440  ? 235 ASN B O   1 
ATOM   1830 C  CB  . ASN B 1 235 ? 11.72644  13.94316  -6.54622  1.000 40.20996  ? 235 ASN B CB  1 
ATOM   1831 C  CG  . ASN B 1 235 ? 12.09166  12.67754  -5.88066  1.000 36.75028  ? 235 ASN B CG  1 
ATOM   1832 O  OD1 . ASN B 1 235 ? 12.32237  12.64794  -4.67940  1.000 42.69766  ? 235 ASN B OD1 1 
ATOM   1833 N  ND2 . ASN B 1 235 ? 12.21069  11.62015  -6.66735  1.000 45.56197  ? 235 ASN B ND2 1 
ATOM   1834 N  N   . LYS B 1 236 ? 12.93755  16.63502  -8.33140  1.000 37.96912  ? 236 LYS B N   1 
ATOM   1835 C  CA  . LYS B 1 236 ? 12.61690  17.74768  -9.22099  1.000 47.87138  ? 236 LYS B CA  1 
ATOM   1836 C  C   . LYS B 1 236 ? 12.80008  17.32075  -10.66526 1.000 51.97455  ? 236 LYS B C   1 
ATOM   1837 O  O   . LYS B 1 236 ? 11.91703  17.51220  -11.51164 1.000 58.48409  ? 236 LYS B O   1 
ATOM   1838 C  CB  . LYS B 1 236 ? 13.50529  18.95172  -8.91077  1.000 49.16891  ? 236 LYS B CB  1 
ATOM   1839 C  CG  . LYS B 1 236 ? 13.22846  19.61826  -7.59559  1.000 61.31218  ? 236 LYS B CG  1 
ATOM   1840 C  CD  . LYS B 1 236 ? 11.86173  20.22086  -7.63670  1.000 66.74064  ? 236 LYS B CD  1 
ATOM   1841 C  CE  . LYS B 1 236 ? 11.71646  21.31908  -6.63625  1.000 54.12038  ? 236 LYS B CE  1 
ATOM   1842 N  NZ  . LYS B 1 236 ? 10.49854  22.08038  -6.99338  1.000 63.86578  ? 236 LYS B NZ  1 
ATOM   1843 N  N   . THR B 1 237 ? 13.94335  16.71493  -10.95716 1.000 42.98837  ? 237 THR B N   1 
ATOM   1844 C  CA  . THR B 1 237 ? 14.24673  16.27175  -12.30144 1.000 43.83676  ? 237 THR B CA  1 
ATOM   1845 C  C   . THR B 1 237 ? 13.77861  14.84648  -12.57846 1.000 34.97518  ? 237 THR B C   1 
ATOM   1846 O  O   . THR B 1 237 ? 13.53228  14.51133  -13.74505 1.000 37.15064  ? 237 THR B O   1 
ATOM   1847 C  CB  . THR B 1 237 ? 15.74724  16.41475  -12.54138 1.000 52.03192  ? 237 THR B CB  1 
ATOM   1848 O  OG1 . THR B 1 237 ? 16.45115  15.60051  -11.60291 1.000 43.20599  ? 237 THR B OG1 1 
ATOM   1849 C  CG2 . THR B 1 237 ? 16.16238  17.87328  -12.33468 1.000 45.20782  ? 237 THR B CG2 1 
ATOM   1850 N  N   . ASN B 1 238 ? 13.60909  14.01004  -11.55051 1.000 34.53758  ? 238 ASN B N   1 
ATOM   1851 C  CA  . ASN B 1 238 ? 13.12536  12.63815  -11.73694 1.000 36.21382  ? 238 ASN B CA  1 
ATOM   1852 C  C   . ASN B 1 238 ? 12.03826  12.29236  -10.73438 1.000 34.95016  ? 238 ASN B C   1 
ATOM   1853 O  O   . ASN B 1 238 ? 12.25026  11.48804  -9.81322  1.000 34.91219  ? 238 ASN B O   1 
ATOM   1854 C  CB  . ASN B 1 238 ? 14.27275  11.63649  -11.64326 1.000 30.36240  ? 238 ASN B CB  1 
ATOM   1855 C  CG  . ASN B 1 238 ? 15.25069  11.78858  -12.76214 1.000 43.83622  ? 238 ASN B CG  1 
ATOM   1856 O  OD1 . ASN B 1 238 ? 16.14264  12.62800  -12.70064 1.000 57.32913  ? 238 ASN B OD1 1 
ATOM   1857 N  ND2 . ASN B 1 238 ? 15.08351  10.98984  -13.80857 1.000 56.91873  ? 238 ASN B ND2 1 
ATOM   1858 N  N   . PRO B 1 239 ? 10.82925  12.83134  -10.92397 1.000 35.39542  ? 239 PRO B N   1 
ATOM   1859 C  CA  . PRO B 1 239 ? 9.77807   12.64950  -9.91202  1.000 35.13823  ? 239 PRO B CA  1 
ATOM   1860 C  C   . PRO B 1 239 ? 9.32728   11.22037  -9.76836  1.000 44.02128  ? 239 PRO B C   1 
ATOM   1861 O  O   . PRO B 1 239 ? 8.75882   10.88247  -8.72705  1.000 45.15659  ? 239 PRO B O   1 
ATOM   1862 C  CB  . PRO B 1 239 ? 8.62369   13.53295  -10.41466 1.000 49.50421  ? 239 PRO B CB  1 
ATOM   1863 C  CG  . PRO B 1 239 ? 9.11229   14.19648  -11.65307 1.000 38.67475  ? 239 PRO B CG  1 
ATOM   1864 C  CD  . PRO B 1 239 ? 10.33680  13.52318  -12.12976 1.000 43.42663  ? 239 PRO B CD  1 
ATOM   1865 N  N   . LYS B 1 240 ? 9.56105   10.36851  -10.76843 1.000 39.87700  ? 240 LYS B N   1 
ATOM   1866 C  CA  . LYS B 1 240 ? 9.08475   8.99300   -10.71083 1.000 41.76563  ? 240 LYS B CA  1 
ATOM   1867 C  C   . LYS B 1 240 ? 10.03800  8.04959   -9.98592  1.000 48.51993  ? 240 LYS B C   1 
ATOM   1868 O  O   . LYS B 1 240 ? 9.67885   6.88904   -9.76091  1.000 54.43311  ? 240 LYS B O   1 
ATOM   1869 C  CB  . LYS B 1 240 ? 8.81796   8.47669   -12.12688 1.000 36.65857  ? 240 LYS B CB  1 
ATOM   1870 C  CG  . LYS B 1 240 ? 7.71847   9.25431   -12.82839 1.000 40.70670  ? 240 LYS B CG  1 
ATOM   1871 N  N   . ILE B 1 241 ? 11.22868  8.51658   -9.61465  1.000 33.09602  ? 241 ILE B N   1 
ATOM   1872 C  CA  . ILE B 1 241 ? 12.20005  7.70304   -8.87684  1.000 31.35401  ? 241 ILE B CA  1 
ATOM   1873 C  C   . ILE B 1 241 ? 11.90824  7.94599   -7.39722  1.000 34.27287  ? 241 ILE B C   1 
ATOM   1874 O  O   . ILE B 1 241 ? 12.38235  8.91321   -6.79499  1.000 35.79947  ? 241 ILE B O   1 
ATOM   1875 C  CB  . ILE B 1 241 ? 13.63348  8.04899   -9.24812  1.000 50.34634  ? 241 ILE B CB  1 
ATOM   1876 C  CG1 . ILE B 1 241 ? 13.89929  7.69980   -10.71335 1.000 40.22273  ? 241 ILE B CG1 1 
ATOM   1877 C  CG2 . ILE B 1 241 ? 14.61052  7.32377   -8.34281  1.000 40.29703  ? 241 ILE B CG2 1 
ATOM   1878 C  CD1 . ILE B 1 241 ? 15.29612  8.02138   -11.14277 1.000 51.63963  ? 241 ILE B CD1 1 
ATOM   1879 N  N   . LYS B 1 242 ? 11.11987  7.04000   -6.80595  1.000 32.52872  ? 242 LYS B N   1 
ATOM   1880 C  CA  . LYS B 1 242 ? 10.51097  7.24899   -5.49814  1.000 33.22687  ? 242 LYS B CA  1 
ATOM   1881 C  C   . LYS B 1 242 ? 10.68882  6.08758   -4.54039  1.000 27.55059  ? 242 LYS B C   1 
ATOM   1882 O  O   . LYS B 1 242 ? 10.21872  6.18427   -3.40019  1.000 27.72720  ? 242 LYS B O   1 
ATOM   1883 C  CB  . LYS B 1 242 ? 8.99901   7.49956   -5.63933  1.000 37.99803  ? 242 LYS B CB  1 
ATOM   1884 C  CG  . LYS B 1 242 ? 8.64895   8.86170   -6.17393  1.000 64.60954  ? 242 LYS B CG  1 
ATOM   1885 C  CD  . LYS B 1 242 ? 9.37290   9.92986   -5.36758  1.000 54.38548  ? 242 LYS B CD  1 
ATOM   1886 C  CE  . LYS B 1 242 ? 8.52108   11.17987  -5.24595  1.000 72.91105  ? 242 LYS B CE  1 
ATOM   1887 N  NZ  . LYS B 1 242 ? 8.98484   12.06987  -4.15407  1.000 54.22605  ? 242 LYS B NZ  1 
ATOM   1888 N  N   . SER B 1 243 ? 11.32036  4.99428   -4.96845  1.000 26.36939  ? 243 SER B N   1 
ATOM   1889 C  CA  . SER B 1 243 ? 11.43020  3.81645   -4.11248  1.000 25.79021  ? 243 SER B CA  1 
ATOM   1890 C  C   . SER B 1 243 ? 12.44586  2.84277   -4.69005  1.000 28.80420  ? 243 SER B C   1 
ATOM   1891 O  O   . SER B 1 243 ? 12.72170  2.84938   -5.89647  1.000 28.62254  ? 243 SER B O   1 
ATOM   1892 C  CB  . SER B 1 243 ? 10.08062  3.10937   -3.95289  1.000 28.93036  ? 243 SER B CB  1 
ATOM   1893 O  OG  . SER B 1 243 ? 9.66495   2.54813   -5.17120  1.000 41.71981  ? 243 SER B OG  1 
ATOM   1894 N  N   . PHE B 1 244 ? 12.95991  1.96862   -3.82161  1.000 22.96881  ? 244 PHE B N   1 
ATOM   1895 C  CA  . PHE B 1 244 ? 13.78876  0.83197   -4.20722  1.000 28.60596  ? 244 PHE B CA  1 
ATOM   1896 C  C   . PHE B 1 244 ? 13.69674  -0.22148  -3.11240  1.000 26.20471  ? 244 PHE B C   1 
ATOM   1897 O  O   . PHE B 1 244 ? 13.24292  0.04366   -1.99939  1.000 25.75070  ? 244 PHE B O   1 
ATOM   1898 C  CB  . PHE B 1 244 ? 15.26328  1.22509   -4.46259  1.000 26.71535  ? 244 PHE B CB  1 
ATOM   1899 C  CG  . PHE B 1 244 ? 15.94759  1.85771   -3.27803  1.000 24.26936  ? 244 PHE B CG  1 
ATOM   1900 C  CD1 . PHE B 1 244 ? 16.54802  1.06800   -2.29667  1.000 26.22490  ? 244 PHE B CD1 1 
ATOM   1901 C  CD2 . PHE B 1 244 ? 15.98856  3.23776   -3.14364  1.000 27.81577  ? 244 PHE B CD2 1 
ATOM   1902 C  CE1 . PHE B 1 244 ? 17.16706  1.65081   -1.21160  1.000 28.23329  ? 244 PHE B CE1 1 
ATOM   1903 C  CE2 . PHE B 1 244 ? 16.63088  3.81729   -2.05496  1.000 26.08933  ? 244 PHE B CE2 1 
ATOM   1904 C  CZ  . PHE B 1 244 ? 17.20900  3.00949   -1.10290  1.000 27.93936  ? 244 PHE B CZ  1 
ATOM   1905 N  N   . THR B 1 245 ? 14.16103  -1.41119  -3.43440  1.000 25.30538  ? 245 THR B N   1 
ATOM   1906 C  CA  . THR B 1 245 ? 13.96620  -2.56509  -2.57089  1.000 23.57564  ? 245 THR B CA  1 
ATOM   1907 C  C   . THR B 1 245 ? 15.28592  -3.29003  -2.34792  1.000 29.08698  ? 245 THR B C   1 
ATOM   1908 O  O   . THR B 1 245 ? 16.05480  -3.49847  -3.28858  1.000 30.78841  ? 245 THR B O   1 
ATOM   1909 C  CB  . THR B 1 245 ? 12.94375  -3.52588  -3.18697  1.000 37.11273  ? 245 THR B CB  1 
ATOM   1910 O  OG1 . THR B 1 245 ? 11.68014  -2.86569  -3.25903  1.000 35.65329  ? 245 THR B OG1 1 
ATOM   1911 C  CG2 . THR B 1 245 ? 12.81320  -4.78618  -2.36167  1.000 32.19909  ? 245 THR B CG2 1 
ATOM   1912 N  N   . ILE B 1 246 ? 15.54295  -3.68827  -1.10244  1.000 23.35418  ? 246 ILE B N   1 
ATOM   1913 C  CA  . ILE B 1 246 ? 16.66616  -4.56345  -0.77502  1.000 26.26861  ? 246 ILE B CA  1 
ATOM   1914 C  C   . ILE B 1 246 ? 16.10590  -5.87072  -0.22940  1.000 22.20351  ? 246 ILE B C   1 
ATOM   1915 O  O   . ILE B 1 246 ? 15.33212  -5.86231  0.73518   1.000 26.36701  ? 246 ILE B O   1 
ATOM   1916 C  CB  . ILE B 1 246 ? 17.59978  -3.89810  0.25415   1.000 26.92360  ? 246 ILE B CB  1 
ATOM   1917 C  CG1 . ILE B 1 246 ? 18.33973  -2.73605  -0.41550  1.000 27.59956  ? 246 ILE B CG1 1 
ATOM   1918 C  CG2 . ILE B 1 246 ? 18.54849  -4.94389  0.90109   1.000 27.85372  ? 246 ILE B CG2 1 
ATOM   1919 C  CD1 . ILE B 1 246 ? 19.03565  -1.78906  0.57278   1.000 37.57886  ? 246 ILE B CD1 1 
ATOM   1920 N  N   . LYS B 1 247 ? 16.49933  -6.99287  -0.81890  1.000 26.20195  ? 247 LYS B N   1 
ATOM   1921 C  CA  . LYS B 1 247 ? 15.97342  -8.27943  -0.37044  1.000 27.68131  ? 247 LYS B CA  1 
ATOM   1922 C  C   . LYS B 1 247 ? 17.05521  -9.13780  0.26520   1.000 31.31030  ? 247 LYS B C   1 
ATOM   1923 O  O   . LYS B 1 247 ? 18.17473  -9.23667  -0.25310  1.000 29.60705  ? 247 LYS B O   1 
ATOM   1924 C  CB  . LYS B 1 247 ? 15.36058  -9.06649  -1.54225  1.000 34.46359  ? 247 LYS B CB  1 
ATOM   1925 C  CG  . LYS B 1 247 ? 14.23462  -8.35293  -2.25233  1.000 30.73293  ? 247 LYS B CG  1 
ATOM   1926 C  CD  . LYS B 1 247 ? 13.85198  -9.11882  -3.51960  1.000 35.63044  ? 247 LYS B CD  1 
ATOM   1927 C  CE  . LYS B 1 247 ? 12.73768  -8.40497  -4.23754  1.000 37.85835  ? 247 LYS B CE  1 
ATOM   1928 N  NZ  . LYS B 1 247 ? 11.90720  -9.34760  -5.03632  1.000 43.88880  ? 247 LYS B NZ  1 
ATOM   1929 N  N   . LEU B 1 248 ? 16.69744  -9.79193  1.36554   1.000 26.67326  ? 248 LEU B N   1 
ATOM   1930 C  CA  . LEU B 1 248 ? 17.49317  -10.84315 1.98164   1.000 27.38145  ? 248 LEU B CA  1 
ATOM   1931 C  C   . LEU B 1 248 ? 16.70663  -12.14178 1.88419   1.000 26.42795  ? 248 LEU B C   1 
ATOM   1932 O  O   . LEU B 1 248 ? 15.60665  -12.24043 2.43132   1.000 26.04624  ? 248 LEU B O   1 
ATOM   1933 C  CB  . LEU B 1 248 ? 17.79296  -10.51469 3.44592   1.000 24.20426  ? 248 LEU B CB  1 
ATOM   1934 C  CG  . LEU B 1 248 ? 18.88915  -9.49728  3.74829   1.000 36.62168  ? 248 LEU B CG  1 
ATOM   1935 C  CD1 . LEU B 1 248 ? 18.53083  -8.14062  3.23540   1.000 46.39637  ? 248 LEU B CD1 1 
ATOM   1936 C  CD2 . LEU B 1 248 ? 19.08713  -9.43247  5.27062   1.000 33.23798  ? 248 LEU B CD2 1 
ATOM   1937 N  N   . LEU B 1 249 ? 17.24168  -13.11721 1.15399   1.000 28.28197  ? 249 LEU B N   1 
ATOM   1938 C  CA  . LEU B 1 249 ? 16.59821  -14.41482 0.97503   1.000 25.25887  ? 249 LEU B CA  1 
ATOM   1939 C  C   . LEU B 1 249 ? 17.41096  -15.47773 1.69285   1.000 32.82017  ? 249 LEU B C   1 
ATOM   1940 O  O   . LEU B 1 249 ? 18.64393  -15.45750 1.64438   1.000 33.95348  ? 249 LEU B O   1 
ATOM   1941 C  CB  . LEU B 1 249 ? 16.52426  -14.79089 -0.52639  1.000 29.70771  ? 249 LEU B CB  1 
ATOM   1942 C  CG  . LEU B 1 249 ? 16.16222  -13.58685 -1.39125  1.000 32.15762  ? 249 LEU B CG  1 
ATOM   1943 C  CD1 . LEU B 1 249 ? 16.40980  -13.89072 -2.86596  1.000 43.15717  ? 249 LEU B CD1 1 
ATOM   1944 C  CD2 . LEU B 1 249 ? 14.73849  -13.18974 -1.17136  1.000 31.68219  ? 249 LEU B CD2 1 
ATOM   1945 N  N   . PHE B 1 250 ? 16.72742  -16.43584 2.31994   1.000 30.61254  ? 250 PHE B N   1 
ATOM   1946 C  CA  . PHE B 1 250 ? 17.40638  -17.45018 3.11484   1.000 33.29004  ? 250 PHE B CA  1 
ATOM   1947 C  C   . PHE B 1 250 ? 16.92387  -18.84651 2.73684   1.000 27.60252  ? 250 PHE B C   1 
ATOM   1948 O  O   . PHE B 1 250 ? 15.75346  -19.04795 2.39297   1.000 38.67209  ? 250 PHE B O   1 
ATOM   1949 C  CB  . PHE B 1 250 ? 17.18340  -17.22410 4.61322   1.000 29.34900  ? 250 PHE B CB  1 
ATOM   1950 C  CG  . PHE B 1 250 ? 17.57791  -15.84669 5.09385   1.000 26.12176  ? 250 PHE B CG  1 
ATOM   1951 C  CD1 . PHE B 1 250 ? 18.89050  -15.59350 5.49638   1.000 31.30774  ? 250 PHE B CD1 1 
ATOM   1952 C  CD2 . PHE B 1 250 ? 16.63159  -14.82923 5.18860   1.000 28.72013  ? 250 PHE B CD2 1 
ATOM   1953 C  CE1 . PHE B 1 250 ? 19.25468  -14.33093 5.97183   1.000 31.48296  ? 250 PHE B CE1 1 
ATOM   1954 C  CE2 . PHE B 1 250 ? 16.98545  -13.56605 5.64574   1.000 25.81698  ? 250 PHE B CE2 1 
ATOM   1955 C  CZ  . PHE B 1 250 ? 18.28782  -13.30878 6.04046   1.000 33.10678  ? 250 PHE B CZ  1 
ATOM   1956 N  N   . ASN B 1 251 ? 17.83683  -19.81719 2.80508   1.000 30.40058  ? 251 ASN B N   1 
ATOM   1957 C  CA  . ASN B 1 251 ? 17.45822  -21.20343 2.56326   1.000 44.05490  ? 251 ASN B CA  1 
ATOM   1958 C  C   . ASN B 1 251 ? 16.83033  -21.81499 3.82507   1.000 37.53462  ? 251 ASN B C   1 
ATOM   1959 O  O   . ASN B 1 251 ? 16.56259  -21.13256 4.82478   1.000 35.93391  ? 251 ASN B O   1 
ATOM   1960 C  CB  . ASN B 1 251 ? 18.66346  -21.99673 2.04718   1.000 38.86172  ? 251 ASN B CB  1 
ATOM   1961 C  CG  . ASN B 1 251 ? 19.73420  -22.25122 3.12009   1.000 44.39890  ? 251 ASN B CG  1 
ATOM   1962 O  OD1 . ASN B 1 251 ? 19.50118  -22.11176 4.31859   1.000 40.49871  ? 251 ASN B OD1 1 
ATOM   1963 N  ND2 . ASN B 1 251 ? 20.91564  -22.65731 2.67257   1.000 48.70957  ? 251 ASN B ND2 1 
ATOM   1964 N  N   . LYS B 1 252 ? 16.59758  -23.13355 3.78724   1.000 43.86638  ? 252 LYS B N   1 
ATOM   1965 C  CA  . LYS B 1 252 ? 15.87282  -23.81794 4.85744   1.000 41.56316  ? 252 LYS B CA  1 
ATOM   1966 C  C   . LYS B 1 252 ? 16.64652  -23.84822 6.17010   1.000 40.02796  ? 252 LYS B C   1 
ATOM   1967 O  O   . LYS B 1 252 ? 16.03719  -24.03919 7.22923   1.000 44.11890  ? 252 LYS B O   1 
ATOM   1968 C  CB  . LYS B 1 252 ? 15.53334  -25.24984 4.43435   1.000 48.88775  ? 252 LYS B CB  1 
ATOM   1969 C  CG  . LYS B 1 252 ? 16.74576  -26.16878 4.37811   1.000 53.62393  ? 252 LYS B CG  1 
ATOM   1970 C  CD  . LYS B 1 252 ? 16.33889  -27.63002 4.25371   1.000 70.06408  ? 252 LYS B CD  1 
ATOM   1971 C  CE  . LYS B 1 252 ? 17.55066  -28.54214 4.33768   1.000 71.28381  ? 252 LYS B CE  1 
ATOM   1972 N  NZ  . LYS B 1 252 ? 18.45963  -28.32645 3.17823   1.000 86.71816  ? 252 LYS B NZ  1 
ATOM   1973 N  N   . ASN B 1 253 ? 17.96350  -23.66743 6.12738   1.000 42.47845  ? 253 ASN B N   1 
ATOM   1974 C  CA  . ASN B 1 253 ? 18.78670  -23.60998 7.32404   1.000 34.22155  ? 253 ASN B CA  1 
ATOM   1975 C  C   . ASN B 1 253 ? 19.03809  -22.18232 7.79196   1.000 38.09989  ? 253 ASN B C   1 
ATOM   1976 O  O   . ASN B 1 253 ? 19.88180  -21.96787 8.66892   1.000 41.17851  ? 253 ASN B O   1 
ATOM   1977 C  CB  . ASN B 1 253 ? 20.12210  -24.30533 7.07865   1.000 46.20232  ? 253 ASN B CB  1 
ATOM   1978 C  CG  . ASN B 1 253 ? 19.97526  -25.79616 6.90536   1.000 50.29723  ? 253 ASN B CG  1 
ATOM   1979 O  OD1 . ASN B 1 253 ? 19.08077  -26.41127 7.48114   1.000 63.86933  ? 253 ASN B OD1 1 
ATOM   1980 N  ND2 . ASN B 1 253 ? 20.85441  -26.38735 6.10594   1.000 52.14714  ? 253 ASN B ND2 1 
ATOM   1981 N  N   . GLY B 1 254 ? 18.35040  -21.20267 7.21416   1.000 37.75095  ? 254 GLY B N   1 
ATOM   1982 C  CA  . GLY B 1 254 ? 18.57399  -19.82553 7.60375   1.000 34.23348  ? 254 GLY B CA  1 
ATOM   1983 C  C   . GLY B 1 254 ? 19.81967  -19.16915 7.04441   1.000 42.63481  ? 254 GLY B C   1 
ATOM   1984 O  O   . GLY B 1 254 ? 20.24936  -18.14502 7.58247   1.000 34.38195  ? 254 GLY B O   1 
ATOM   1985 N  N   . VAL B 1 255 ? 20.41779  -19.71637 5.96636   1.000 39.32005  ? 255 VAL B N   1 
ATOM   1986 C  CA  . VAL B 1 255 ? 21.64065  -19.17198 5.38399   1.000 29.38429  ? 255 VAL B CA  1 
ATOM   1987 C  C   . VAL B 1 255 ? 21.28485  -18.26912 4.20893   1.000 40.42482  ? 255 VAL B C   1 
ATOM   1988 O  O   . VAL B 1 255 ? 20.42833  -18.60866 3.37152   1.000 31.46549  ? 255 VAL B O   1 
ATOM   1989 C  CB  . VAL B 1 255 ? 22.60417  -20.29882 4.95113   1.000 31.14605  ? 255 VAL B CB  1 
ATOM   1990 C  CG1 . VAL B 1 255 ? 23.83225  -19.72419 4.25235   1.000 36.87433  ? 255 VAL B CG1 1 
ATOM   1991 C  CG2 . VAL B 1 255 ? 23.01957  -21.11792 6.16179   1.000 38.26511  ? 255 VAL B CG2 1 
ATOM   1992 N  N   . LEU B 1 256 ? 21.93530  -17.10632 4.15177   1.000 34.68249  ? 256 LEU B N   1 
ATOM   1993 C  CA  . LEU B 1 256 ? 21.66803  -16.11611 3.10618   1.000 32.04137  ? 256 LEU B CA  1 
ATOM   1994 C  C   . LEU B 1 256 ? 21.97716  -16.66449 1.71025   1.000 32.70945  ? 256 LEU B C   1 
ATOM   1995 O  O   . LEU B 1 256 ? 23.04337  -17.23149 1.48166   1.000 33.74988  ? 256 LEU B O   1 
ATOM   1996 C  CB  . LEU B 1 256 ? 22.51572  -14.87382 3.36369   1.000 36.67890  ? 256 LEU B CB  1 
ATOM   1997 C  CG  . LEU B 1 256 ? 22.21570  -13.61123 2.56722   1.000 33.38553  ? 256 LEU B CG  1 
ATOM   1998 C  CD1 . LEU B 1 256 ? 20.83705  -13.00053 2.98875   1.000 25.84685  ? 256 LEU B CD1 1 
ATOM   1999 C  CD2 . LEU B 1 256 ? 23.37180  -12.62267 2.77934   1.000 33.42389  ? 256 LEU B CD2 1 
ATOM   2000 N  N   . LEU B 1 257 ? 21.05215  -16.47550 0.77024   1.000 28.39505  ? 257 LEU B N   1 
ATOM   2001 C  CA  . LEU B 1 257 ? 21.24888  -16.91890 -0.61628  1.000 30.57479  ? 257 LEU B CA  1 
ATOM   2002 C  C   . LEU B 1 257 ? 21.96830  -15.86410 -1.45236  1.000 41.16514  ? 257 LEU B C   1 
ATOM   2003 O  O   . LEU B 1 257 ? 21.85074  -14.66484 -1.21476  1.000 37.38425  ? 257 LEU B O   1 
ATOM   2004 C  CB  . LEU B 1 257 ? 19.90313  -17.24225 -1.27182  1.000 35.58521  ? 257 LEU B CB  1 
ATOM   2005 C  CG  . LEU B 1 257 ? 19.16831  -18.43730 -0.66806  1.000 32.85996  ? 257 LEU B CG  1 
ATOM   2006 C  CD1 . LEU B 1 257 ? 17.71094  -18.49043 -1.12757  1.000 36.84830  ? 257 LEU B CD1 1 
ATOM   2007 C  CD2 . LEU B 1 257 ? 19.90705  -19.72420 -1.01920  1.000 44.42539  ? 257 LEU B CD2 1 
ATOM   2008 N  N   . ASP B 1 258 ? 22.69887  -16.32187 -2.47618  1.000 37.13924  ? 258 ASP B N   1 
ATOM   2009 C  CA  . ASP B 1 258 ? 23.50746  -15.39475 -3.25914  1.000 36.00219  ? 258 ASP B CA  1 
ATOM   2010 C  C   . ASP B 1 258 ? 22.68776  -14.43164 -4.10974  1.000 32.71086  ? 258 ASP B C   1 
ATOM   2011 O  O   . ASP B 1 258 ? 23.22445  -13.40935 -4.54601  1.000 45.53626  ? 258 ASP B O   1 
ATOM   2012 C  CB  . ASP B 1 258 ? 24.47262  -16.17219 -4.17113  1.000 46.43553  ? 258 ASP B CB  1 
ATOM   2013 C  CG  . ASP B 1 258 ? 25.58258  -16.86418 -3.39346  1.000 69.22134  ? 258 ASP B CG  1 
ATOM   2014 O  OD1 . ASP B 1 258 ? 26.49619  -16.16554 -2.90752  1.000 75.12496  ? 258 ASP B OD1 1 
ATOM   2015 O  OD2 . ASP B 1 258 ? 25.54560  -18.10667 -3.26852  1.000 87.95825  ? 258 ASP B OD2 1 
ATOM   2016 N  N   . ASN B 1 259 ? 21.42185  -14.71792 -4.38480  1.000 36.64461  ? 259 ASN B N   1 
ATOM   2017 C  CA  . ASN B 1 259 ? 20.65160  -13.74998 -5.15653  1.000 43.11028  ? 259 ASN B CA  1 
ATOM   2018 C  C   . ASN B 1 259 ? 20.07108  -12.63314 -4.29235  1.000 41.07847  ? 259 ASN B C   1 
ATOM   2019 O  O   . ASN B 1 259 ? 19.29875  -11.81350 -4.80379  1.000 41.60968  ? 259 ASN B O   1 
ATOM   2020 C  CB  . ASN B 1 259 ? 19.52822  -14.43769 -5.93313  1.000 52.28848  ? 259 ASN B CB  1 
ATOM   2021 C  CG  . ASN B 1 259 ? 18.85739  -15.51283 -5.13779  1.000 56.20587  ? 259 ASN B CG  1 
ATOM   2022 O  OD1 . ASN B 1 259 ? 19.48688  -16.16491 -4.31168  1.000 68.91904  ? 259 ASN B OD1 1 
ATOM   2023 N  ND2 . ASN B 1 259 ? 17.57048  -15.71438 -5.38122  1.000 71.66274  ? 259 ASN B ND2 1 
ATOM   2024 N  N   . SER B 1 260 ? 20.44139  -12.57833 -3.01439  1.000 34.05067  ? 260 SER B N   1 
ATOM   2025 C  CA  . SER B 1 260 ? 20.07373  -11.45075 -2.16058  1.000 32.39012  ? 260 SER B CA  1 
ATOM   2026 C  C   . SER B 1 260 ? 20.81458  -10.18401 -2.57969  1.000 33.13972  ? 260 SER B C   1 
ATOM   2027 O  O   . SER B 1 260 ? 21.91956  -10.24142 -3.12185  1.000 32.56268  ? 260 SER B O   1 
ATOM   2028 C  CB  . SER B 1 260 ? 20.41786  -11.76801 -0.70784  1.000 27.39633  ? 260 SER B CB  1 
ATOM   2029 O  OG  . SER B 1 260 ? 19.76667  -12.94666 -0.27800  1.000 35.84916  ? 260 SER B OG  1 
ATOM   2030 N  N   . ASN B 1 261 ? 20.22828  -9.02110  -2.27499  1.000 28.48218  ? 261 ASN B N   1 
ATOM   2031 C  CA  . ASN B 1 261 ? 20.95463  -7.79089  -2.57383  1.000 31.08185  ? 261 ASN B CA  1 
ATOM   2032 C  C   . ASN B 1 261 ? 22.18999  -7.66448  -1.69437  1.000 29.90874  ? 261 ASN B C   1 
ATOM   2033 O  O   . ASN B 1 261 ? 23.18875  -7.07638  -2.11502  1.000 30.99280  ? 261 ASN B O   1 
ATOM   2034 C  CB  . ASN B 1 261 ? 20.05128  -6.56867  -2.42316  1.000 28.38395  ? 261 ASN B CB  1 
ATOM   2035 C  CG  . ASN B 1 261 ? 18.93326  -6.53973  -3.43911  1.000 32.25715  ? 261 ASN B CG  1 
ATOM   2036 O  OD1 . ASN B 1 261 ? 17.87254  -7.11722  -3.22214  1.000 29.59966  ? 261 ASN B OD1 1 
ATOM   2037 N  ND2 . ASN B 1 261 ? 19.16151  -5.85222  -4.56073  1.000 34.13414  ? 261 ASN B ND2 1 
ATOM   2038 N  N   . LEU B 1 262 ? 22.13415  -8.20579  -0.47461  1.000 31.56833  ? 262 LEU B N   1 
ATOM   2039 C  CA  . LEU B 1 262 ? 23.26257  -8.19247  0.44182   1.000 29.65164  ? 262 LEU B CA  1 
ATOM   2040 C  C   . LEU B 1 262 ? 24.20778  -9.32405  0.09679   1.000 36.26639  ? 262 LEU B C   1 
ATOM   2041 O  O   . LEU B 1 262 ? 23.77422  -10.44566 -0.17015  1.000 33.02768  ? 262 LEU B O   1 
ATOM   2042 C  CB  . LEU B 1 262 ? 22.77754  -8.35008  1.88645   1.000 27.56001  ? 262 LEU B CB  1 
ATOM   2043 C  CG  . LEU B 1 262 ? 23.82283  -8.41653  2.99144   1.000 30.39385  ? 262 LEU B CG  1 
ATOM   2044 C  CD1 . LEU B 1 262 ? 24.58854  -7.09408  3.07763   1.000 33.50706  ? 262 LEU B CD1 1 
ATOM   2045 C  CD2 . LEU B 1 262 ? 23.12466  -8.70671  4.34417   1.000 33.20068  ? 262 LEU B CD2 1 
ATOM   2046 N  N   . GLY B 1 263 ? 25.50390  -9.03227  0.09938   1.000 33.70472  ? 263 GLY B N   1 
ATOM   2047 C  CA  . GLY B 1 263 ? 26.48611  -10.05656 -0.24923  1.000 28.23199  ? 263 GLY B CA  1 
ATOM   2048 C  C   . GLY B 1 263 ? 26.76788  -10.97687 0.93299   1.000 35.40802  ? 263 GLY B C   1 
ATOM   2049 O  O   . GLY B 1 263 ? 26.89681  -10.53697 2.07316   1.000 36.17769  ? 263 GLY B O   1 
ATOM   2050 N  N   . LYS B 1 264 ? 26.87862  -12.27770 0.63792   1.000 41.88917  ? 264 LYS B N   1 
ATOM   2051 C  CA  . LYS B 1 264 ? 27.08497  -13.27806 1.68835   1.000 44.33125  ? 264 LYS B CA  1 
ATOM   2052 C  C   . LYS B 1 264 ? 28.37150  -13.04935 2.47254   1.000 51.93522  ? 264 LYS B C   1 
ATOM   2053 O  O   . LYS B 1 264 ? 28.44644  -13.39967 3.65500   1.000 42.75378  ? 264 LYS B O   1 
ATOM   2054 C  CB  . LYS B 1 264 ? 27.12465  -14.68215 1.08838   1.000 49.57181  ? 264 LYS B CB  1 
ATOM   2055 C  CG  . LYS B 1 264 ? 25.79057  -15.25419 0.67875   1.000 61.57551  ? 264 LYS B CG  1 
ATOM   2056 C  CD  . LYS B 1 264 ? 25.97221  -16.68557 0.17087   1.000 66.52629  ? 264 LYS B CD  1 
ATOM   2057 C  CE  . LYS B 1 264 ? 26.72722  -17.54312 1.18337   1.000 66.55836  ? 264 LYS B CE  1 
ATOM   2058 N  NZ  . LYS B 1 264 ? 26.05933  -17.55681 2.51793   1.000 59.77048  ? 264 LYS B NZ  1 
ATOM   2059 N  N   . ALA B 1 265 ? 29.40286  -12.49870 1.83441   1.000 39.69745  ? 265 ALA B N   1 
ATOM   2060 C  CA  . ALA B 1 265 ? 30.68396  -12.32650 2.51268   1.000 38.22026  ? 265 ALA B CA  1 
ATOM   2061 C  C   . ALA B 1 265 ? 30.58906  -11.32376 3.64508   1.000 45.45655  ? 265 ALA B C   1 
ATOM   2062 O  O   . ALA B 1 265 ? 31.49710  -11.25493 4.48886   1.000 44.27228  ? 265 ALA B O   1 
ATOM   2063 C  CB  . ALA B 1 265 ? 31.75273  -11.88655 1.51074   1.000 48.74772  ? 265 ALA B CB  1 
ATOM   2064 N  N   . TYR B 1 266 ? 29.49050  -10.57868 3.69781   1.000 40.82231  ? 266 TYR B N   1 
ATOM   2065 C  CA  . TYR B 1 266 ? 29.31922  -9.46125  4.60771   1.000 47.18871  ? 266 TYR B CA  1 
ATOM   2066 C  C   . TYR B 1 266 ? 28.31657  -9.75000  5.71720   1.000 48.53454  ? 266 TYR B C   1 
ATOM   2067 O  O   . TYR B 1 266 ? 27.99040  -8.84145  6.49482   1.000 45.03578  ? 266 TYR B O   1 
ATOM   2068 C  CB  . TYR B 1 266 ? 28.90405  -8.23174  3.80015   1.000 36.27649  ? 266 TYR B CB  1 
ATOM   2069 C  CG  . TYR B 1 266 ? 29.94487  -7.85478  2.74825   1.000 38.31770  ? 266 TYR B CG  1 
ATOM   2070 C  CD1 . TYR B 1 266 ? 31.13107  -7.23087  3.10703   1.000 46.30628  ? 266 TYR B CD1 1 
ATOM   2071 C  CD2 . TYR B 1 266 ? 29.73110  -8.12778  1.39936   1.000 40.84781  ? 266 TYR B CD2 1 
ATOM   2072 C  CE1 . TYR B 1 266 ? 32.08624  -6.89396  2.14728   1.000 53.31186  ? 266 TYR B CE1 1 
ATOM   2073 C  CE2 . TYR B 1 266 ? 30.66707  -7.79270  0.44576   1.000 50.51832  ? 266 TYR B CE2 1 
ATOM   2074 C  CZ  . TYR B 1 266 ? 31.84240  -7.17224  0.81968   1.000 56.35444  ? 266 TYR B CZ  1 
ATOM   2075 O  OH  . TYR B 1 266 ? 32.77258  -6.83597  -0.15039  1.000 53.02572  ? 266 TYR B OH  1 
ATOM   2076 N  N   . TRP B 1 267 ? 27.84650  -10.99568 5.82740   1.000 34.60628  ? 267 TRP B N   1 
ATOM   2077 C  CA  . TRP B 1 267 ? 26.76627  -11.38790 6.73773   1.000 36.37369  ? 267 TRP B CA  1 
ATOM   2078 C  C   . TRP B 1 267 ? 27.24877  -12.55069 7.60247   1.000 42.00250  ? 267 TRP B C   1 
ATOM   2079 O  O   . TRP B 1 267 ? 27.48529  -13.65046 7.09371   1.000 40.43357  ? 267 TRP B O   1 
ATOM   2080 C  CB  . TRP B 1 267 ? 25.53277  -11.76907 5.92530   1.000 37.58252  ? 267 TRP B CB  1 
ATOM   2081 C  CG  . TRP B 1 267 ? 24.31180  -12.16120 6.66140   1.000 34.01458  ? 267 TRP B CG  1 
ATOM   2082 C  CD1 . TRP B 1 267 ? 23.73431  -13.40276 6.68274   1.000 35.40624  ? 267 TRP B CD1 1 
ATOM   2083 C  CD2 . TRP B 1 267 ? 23.47219  -11.31102 7.45508   1.000 28.63936  ? 267 TRP B CD2 1 
ATOM   2084 N  NE1 . TRP B 1 267 ? 22.59532  -13.37810 7.43666   1.000 36.77493  ? 267 TRP B NE1 1 
ATOM   2085 C  CE2 . TRP B 1 267 ? 22.39825  -12.10498 7.91820   1.000 36.83225  ? 267 TRP B CE2 1 
ATOM   2086 C  CE3 . TRP B 1 267 ? 23.50861  -9.95581  7.79826   1.000 28.48495  ? 267 TRP B CE3 1 
ATOM   2087 C  CZ2 . TRP B 1 267 ? 21.37394  -11.59089 8.72629   1.000 35.53589  ? 267 TRP B CZ2 1 
ATOM   2088 C  CZ3 . TRP B 1 267 ? 22.50373  -9.44873  8.63187   1.000 28.69933  ? 267 TRP B CZ3 1 
ATOM   2089 C  CH2 . TRP B 1 267 ? 21.44087  -10.25819 9.06442   1.000 32.26175  ? 267 TRP B CH2 1 
ATOM   2090 N  N   . ASN B 1 268 ? 27.40041  -12.31931 8.90565   1.000 35.73487  ? 268 ASN B N   1 
ATOM   2091 C  CA  . ASN B 1 268 ? 28.04537  -13.32106 9.74818   1.000 34.17714  ? 268 ASN B CA  1 
ATOM   2092 C  C   . ASN B 1 268 ? 27.58953  -13.13216 11.18271  1.000 34.29655  ? 268 ASN B C   1 
ATOM   2093 O  O   . ASN B 1 268 ? 27.04459  -12.09103 11.53354  1.000 39.08528  ? 268 ASN B O   1 
ATOM   2094 C  CB  . ASN B 1 268 ? 29.57423  -13.21781 9.67085   1.000 35.29203  ? 268 ASN B CB  1 
ATOM   2095 N  N   . PHE B 1 269 ? 27.84065  -14.14014 12.01547  1.000 36.68626  ? 269 PHE B N   1 
ATOM   2096 C  CA  . PHE B 1 269 ? 27.64183  -13.95499 13.44838  1.000 34.78345  ? 269 PHE B CA  1 
ATOM   2097 C  C   . PHE B 1 269 ? 28.75621  -13.07648 14.00685  1.000 49.99589  ? 269 PHE B C   1 
ATOM   2098 O  O   . PHE B 1 269 ? 29.90734  -13.15047 13.56558  1.000 44.00060  ? 269 PHE B O   1 
ATOM   2099 C  CB  . PHE B 1 269 ? 27.61806  -15.30595 14.17715  1.000 36.94502  ? 269 PHE B CB  1 
ATOM   2100 C  CG  . PHE B 1 269 ? 26.37246  -16.12086 13.92088  1.000 46.93080  ? 269 PHE B CG  1 
ATOM   2101 C  CD1 . PHE B 1 269 ? 25.19226  -15.85628 14.61511  1.000 44.62559  ? 269 PHE B CD1 1 
ATOM   2102 C  CD2 . PHE B 1 269 ? 26.37663  -17.15001 12.99300  1.000 49.51948  ? 269 PHE B CD2 1 
ATOM   2103 C  CE1 . PHE B 1 269 ? 24.04216  -16.60738 14.38002  1.000 47.99742  ? 269 PHE B CE1 1 
ATOM   2104 C  CE2 . PHE B 1 269 ? 25.23359  -17.90408 12.75817  1.000 52.78801  ? 269 PHE B CE2 1 
ATOM   2105 C  CZ  . PHE B 1 269 ? 24.06504  -17.63299 13.45066  1.000 44.61714  ? 269 PHE B CZ  1 
ATOM   2106 N  N   . ARG B 1 270 ? 28.40822  -12.22955 14.98028  1.000 37.80775  ? 270 ARG B N   1 
ATOM   2107 C  CA  . ARG B 1 270 ? 29.39717  -11.38792 15.64493  1.000 48.73977  ? 270 ARG B CA  1 
ATOM   2108 C  C   . ARG B 1 270 ? 30.27293  -12.23828 16.56149  1.000 57.14194  ? 270 ARG B C   1 
ATOM   2109 O  O   . ARG B 1 270 ? 29.78715  -13.14912 17.23562  1.000 59.70569  ? 270 ARG B O   1 
ATOM   2110 C  CB  . ARG B 1 270 ? 28.71767  -10.27255 16.45084  1.000 44.99648  ? 270 ARG B CB  1 
ATOM   2111 C  CG  . ARG B 1 270 ? 29.69563  -9.28735  17.08840  1.000 52.90016  ? 270 ARG B CG  1 
ATOM   2112 C  CD  . ARG B 1 270 ? 29.03836  -8.02501  17.70296  1.000 40.76421  ? 270 ARG B CD  1 
ATOM   2113 N  NE  . ARG B 1 270 ? 30.05514  -7.21213  18.38390  1.000 64.69624  ? 270 ARG B NE  1 
ATOM   2114 C  CZ  . ARG B 1 270 ? 29.84119  -6.04040  18.98930  1.000 71.03345  ? 270 ARG B CZ  1 
ATOM   2115 N  NH1 . ARG B 1 270 ? 28.63055  -5.49889  19.01625  1.000 64.54626  ? 270 ARG B NH1 1 
ATOM   2116 N  NH2 . ARG B 1 270 ? 30.84980  -5.40133  19.57487  1.000 63.84800  ? 270 ARG B NH2 1 
ATOM   2117 N  N   . SER B 1 271 ? 31.57095  -11.94493 16.57230  1.000 78.72377  ? 271 SER B N   1 
ATOM   2118 C  CA  . SER B 1 271 ? 32.51816  -12.67077 17.42008  1.000 97.29347  ? 271 SER B CA  1 
ATOM   2119 C  C   . SER B 1 271 ? 32.63376  -12.03660 18.80354  1.000 99.28251  ? 271 SER B C   1 
ATOM   2120 O  O   . SER B 1 271 ? 32.90300  -10.84230 18.92930  1.000 102.24142 ? 271 SER B O   1 
ATOM   2121 C  CB  . SER B 1 271 ? 33.89808  -12.73149 16.75538  1.000 105.50139 ? 271 SER B CB  1 
ATOM   2122 O  OG  . SER B 1 271 ? 34.86873  -13.28142 17.63294  1.000 111.51366 ? 271 SER B OG  1 
ATOM   2123 N  N   . GLU B 1 281 ? 27.20591  -21.47831 10.46365  1.000 73.23893  ? 281 GLU B N   1 
ATOM   2124 C  CA  . GLU B 1 281 ? 26.53963  -20.44665 9.67973   1.000 68.63901  ? 281 GLU B CA  1 
ATOM   2125 C  C   . GLU B 1 281 ? 25.01340  -20.60635 9.68879   1.000 81.17280  ? 281 GLU B C   1 
ATOM   2126 O  O   . GLU B 1 281 ? 24.29298  -19.68899 9.27438   1.000 66.78714  ? 281 GLU B O   1 
ATOM   2127 C  CB  . GLU B 1 281 ? 27.05076  -20.46530 8.23987   1.000 75.11575  ? 281 GLU B CB  1 
ATOM   2128 C  CG  . GLU B 1 281 ? 26.72009  -21.74831 7.50602   1.000 79.01368  ? 281 GLU B CG  1 
ATOM   2129 C  CD  . GLU B 1 281 ? 27.26160  -21.77280 6.08881   1.000 78.91487  ? 281 GLU B CD  1 
ATOM   2130 O  OE1 . GLU B 1 281 ? 27.11007  -22.81172 5.41185   1.000 77.34857  ? 281 GLU B OE1 1 
ATOM   2131 O  OE2 . GLU B 1 281 ? 27.83730  -20.75514 5.65447   1.000 70.24229  ? 281 GLU B OE2 1 
ATOM   2132 N  N   . LYS B 1 282 ? 24.52732  -21.76479 10.14855  1.000 72.83580  ? 282 LYS B N   1 
ATOM   2133 C  CA  . LYS B 1 282 ? 23.08804  -22.00377 10.24233  1.000 62.45426  ? 282 LYS B CA  1 
ATOM   2134 C  C   . LYS B 1 282 ? 22.45121  -21.07785 11.27498  1.000 68.63400  ? 282 LYS B C   1 
ATOM   2135 O  O   . LYS B 1 282 ? 23.05770  -20.73731 12.29462  1.000 54.10946  ? 282 LYS B O   1 
ATOM   2136 C  CB  . LYS B 1 282 ? 22.79616  -23.45561 10.61535  1.000 53.23542  ? 282 LYS B CB  1 
ATOM   2137 N  N   . ALA B 1 283 ? 21.20526  -20.67910 11.00772  1.000 49.08448  ? 283 ALA B N   1 
ATOM   2138 C  CA  . ALA B 1 283 ? 20.56140  -19.68772 11.85973  1.000 36.83423  ? 283 ALA B CA  1 
ATOM   2139 C  C   . ALA B 1 283 ? 19.04053  -19.70816 11.74527  1.000 42.46328  ? 283 ALA B C   1 
ATOM   2140 O  O   . ALA B 1 283 ? 18.41381  -18.66063 11.52748  1.000 36.63504  ? 283 ALA B O   1 
ATOM   2141 C  CB  . ALA B 1 283 ? 21.10773  -18.30391 11.51762  1.000 49.53402  ? 283 ALA B CB  1 
ATOM   2142 N  N   . ILE B 1 284 ? 18.43569  -20.88780 11.91718  1.000 35.21503  ? 284 ILE B N   1 
ATOM   2143 C  CA  . ILE B 1 284 ? 16.97989  -21.00218 11.83960  1.000 37.49732  ? 284 ILE B CA  1 
ATOM   2144 C  C   . ILE B 1 284 ? 16.31888  -20.16592 12.93274  1.000 40.10063  ? 284 ILE B C   1 
ATOM   2145 O  O   . ILE B 1 284 ? 15.20572  -19.65377 12.75398  1.000 43.40763  ? 284 ILE B O   1 
ATOM   2146 C  CB  . ILE B 1 284 ? 16.54015  -22.48187 11.92252  1.000 39.26532  ? 284 ILE B CB  1 
ATOM   2147 C  CG1 . ILE B 1 284 ? 17.21363  -23.31281 10.83408  1.000 65.22484  ? 284 ILE B CG1 1 
ATOM   2148 C  CG2 . ILE B 1 284 ? 15.04005  -22.61401 11.75291  1.000 41.96620  ? 284 ILE B CG2 1 
ATOM   2149 C  CD1 . ILE B 1 284 ? 16.81022  -24.77593 10.84634  1.000 63.95891  ? 284 ILE B CD1 1 
ATOM   2150 N  N   . GLY B 1 285 ? 16.98121  -20.02012 14.07984  1.000 37.16975  ? 285 GLY B N   1 
ATOM   2151 C  CA  . GLY B 1 285 ? 16.42551  -19.23212 15.16659  1.000 33.95985  ? 285 GLY B CA  1 
ATOM   2152 C  C   . GLY B 1 285 ? 16.32589  -17.75308 14.87778  1.000 30.31474  ? 285 GLY B C   1 
ATOM   2153 O  O   . GLY B 1 285 ? 15.69460  -17.02971 15.65685  1.000 33.23993  ? 285 GLY B O   1 
ATOM   2154 N  N   . PHE B 1 286 ? 16.94055  -17.28524 13.79258  1.000 31.27833  ? 286 PHE B N   1 
ATOM   2155 C  CA  . PHE B 1 286 ? 16.84742  -15.89235 13.37823  1.000 32.85107  ? 286 PHE B CA  1 
ATOM   2156 C  C   . PHE B 1 286 ? 15.83567  -15.67600 12.26655  1.000 30.74354  ? 286 PHE B C   1 
ATOM   2157 O  O   . PHE B 1 286 ? 15.65029  -14.53805 11.82992  1.000 32.06848  ? 286 PHE B O   1 
ATOM   2158 C  CB  . PHE B 1 286 ? 18.22956  -15.38944 12.93070  1.000 31.56923  ? 286 PHE B CB  1 
ATOM   2159 C  CG  . PHE B 1 286 ? 19.20050  -15.22238 14.06955  1.000 31.78351  ? 286 PHE B CG  1 
ATOM   2160 C  CD1 . PHE B 1 286 ? 19.93723  -16.29960 14.54425  1.000 32.00499  ? 286 PHE B CD1 1 
ATOM   2161 C  CD2 . PHE B 1 286 ? 19.35032  -13.98747 14.68847  1.000 32.76910  ? 286 PHE B CD2 1 
ATOM   2162 C  CE1 . PHE B 1 286 ? 20.81097  -16.14182 15.62290  1.000 39.09885  ? 286 PHE B CE1 1 
ATOM   2163 C  CE2 . PHE B 1 286 ? 20.23008  -13.82077 15.74155  1.000 35.26695  ? 286 PHE B CE2 1 
ATOM   2164 C  CZ  . PHE B 1 286 ? 20.95677  -14.89699 16.21596  1.000 32.71199  ? 286 PHE B CZ  1 
ATOM   2165 N  N   . MET B 1 287 ? 15.18998  -16.73527 11.79112  1.000 30.08654  ? 287 MET B N   1 
ATOM   2166 C  CA  . MET B 1 287 ? 14.32690  -16.59353 10.63482  1.000 25.89792  ? 287 MET B CA  1 
ATOM   2167 C  C   . MET B 1 287 ? 12.92854  -16.12656 11.04561  1.000 29.13252  ? 287 MET B C   1 
ATOM   2168 O  O   . MET B 1 287 ? 12.46080  -16.43270 12.15348  1.000 26.71929  ? 287 MET B O   1 
ATOM   2169 C  CB  . MET B 1 287 ? 14.24211  -17.91984 9.89647   1.000 28.18468  ? 287 MET B CB  1 
ATOM   2170 C  CG  . MET B 1 287 ? 15.57554  -18.31341 9.17927   1.000 27.86723  ? 287 MET B CG  1 
ATOM   2171 S  SD  . MET B 1 287 ? 16.14835  -17.07102 8.00827   1.000 30.31115  ? 287 MET B SD  1 
ATOM   2172 C  CE  . MET B 1 287 ? 17.44017  -16.21974 8.91339   1.000 28.39445  ? 287 MET B CE  1 
ATOM   2173 N  N   . PRO B 1 288 ? 12.23561  -15.38701 10.17617  1.000 23.62964  ? 288 PRO B N   1 
ATOM   2174 C  CA  . PRO B 1 288 ? 10.88132  -14.94125 10.53136  1.000 22.54467  ? 288 PRO B CA  1 
ATOM   2175 C  C   . PRO B 1 288 ? 9.93323   -16.12584 10.55714  1.000 29.43089  ? 288 PRO B C   1 
ATOM   2176 O  O   . PRO B 1 288 ? 9.94149   -16.96903 9.65861   1.000 29.64707  ? 288 PRO B O   1 
ATOM   2177 C  CB  . PRO B 1 288 ? 10.51602  -13.94888 9.42344   1.000 26.39847  ? 288 PRO B CB  1 
ATOM   2178 C  CG  . PRO B 1 288 ? 11.84360  -13.50393 8.85301   1.000 27.70364  ? 288 PRO B CG  1 
ATOM   2179 C  CD  . PRO B 1 288 ? 12.68502  -14.77708 8.91099   1.000 23.66798  ? 288 PRO B CD  1 
ATOM   2180 N  N   . ASN B 1 289 ? 9.11746   -16.16349 11.60708  1.000 27.19465  ? 289 ASN B N   1 
ATOM   2181 C  CA  . ASN B 1 289 ? 8.21252   -17.27613 11.86414  1.000 29.79857  ? 289 ASN B CA  1 
ATOM   2182 C  C   . ASN B 1 289 ? 7.22783   -17.49994 10.71341  1.000 26.16599  ? 289 ASN B C   1 
ATOM   2183 O  O   . ASN B 1 289 ? 6.49485   -16.59376 10.32265  1.000 27.70488  ? 289 ASN B O   1 
ATOM   2184 C  CB  . ASN B 1 289 ? 7.46707   -16.99088 13.16779  1.000 31.36154  ? 289 ASN B CB  1 
ATOM   2185 C  CG  . ASN B 1 289 ? 6.64262   -18.15471 13.61436  1.000 33.52860  ? 289 ASN B CG  1 
ATOM   2186 O  OD1 . ASN B 1 289 ? 5.55314   -18.39804 13.07952  1.000 32.30745  ? 289 ASN B OD1 1 
ATOM   2187 N  ND2 . ASN B 1 289 ? 7.16561   -18.91117 14.58059  1.000 33.56825  ? 289 ASN B ND2 1 
ATOM   2188 N  N   . LEU B 1 290 ? 7.19547   -18.73760 10.17955  1.000 30.26393  ? 290 LEU B N   1 
ATOM   2189 C  CA  . LEU B 1 290 ? 6.34474   -19.04211 9.02501   1.000 29.27584  ? 290 LEU B CA  1 
ATOM   2190 C  C   . LEU B 1 290 ? 4.85679   -19.13306 9.35308   1.000 31.26641  ? 290 LEU B C   1 
ATOM   2191 O  O   . LEU B 1 290 ? 4.02978   -18.96753 8.45602   1.000 35.46435  ? 290 LEU B O   1 
ATOM   2192 C  CB  . LEU B 1 290 ? 6.78439   -20.34680 8.36309   1.000 33.12013  ? 290 LEU B CB  1 
ATOM   2193 C  CG  . LEU B 1 290 ? 8.01187   -20.14575 7.47469   1.000 30.67452  ? 290 LEU B CG  1 
ATOM   2194 C  CD1 . LEU B 1 290 ? 8.67911   -21.49394 7.13661   1.000 40.39124  ? 290 LEU B CD1 1 
ATOM   2195 C  CD2 . LEU B 1 290 ? 7.63810   -19.38637 6.17187   1.000 32.75402  ? 290 LEU B CD2 1 
ATOM   2196 N  N   . VAL B 1 291 ? 4.48018   -19.41008 10.59288  1.000 34.97410  ? 291 VAL B N   1 
ATOM   2197 C  CA  . VAL B 1 291 ? 3.06189   -19.32712 10.91485  1.000 32.00115  ? 291 VAL B CA  1 
ATOM   2198 C  C   . VAL B 1 291 ? 2.62503   -17.87498 11.10011  1.000 34.35752  ? 291 VAL B C   1 
ATOM   2199 O  O   . VAL B 1 291 ? 1.54401   -17.48319 10.64974  1.000 30.03737  ? 291 VAL B O   1 
ATOM   2200 C  CB  . VAL B 1 291 ? 2.74256   -20.19134 12.14376  1.000 28.41504  ? 291 VAL B CB  1 
ATOM   2201 C  CG1 . VAL B 1 291 ? 1.30663   -19.95160 12.58721  1.000 38.57999  ? 291 VAL B CG1 1 
ATOM   2202 C  CG2 . VAL B 1 291 ? 2.92707   -21.65346 11.79412  1.000 33.24606  ? 291 VAL B CG2 1 
ATOM   2203 N  N   . ALA B 1 292 ? 3.45680   -17.04282 11.73946  1.000 29.43100  ? 292 ALA B N   1 
ATOM   2204 C  CA  . ALA B 1 292 ? 3.11063   -15.62736 11.86264  1.000 24.52915  ? 292 ALA B CA  1 
ATOM   2205 C  C   . ALA B 1 292 ? 3.12539   -14.94033 10.50308  1.000 28.75720  ? 292 ALA B C   1 
ATOM   2206 O  O   . ALA B 1 292 ? 2.28003   -14.07352 10.23386  1.000 26.18471  ? 292 ALA B O   1 
ATOM   2207 C  CB  . ALA B 1 292 ? 4.07397   -14.92280 12.82642  1.000 27.77407  ? 292 ALA B CB  1 
ATOM   2208 N  N   . TYR B 1 293 ? 4.07323   -15.31812 9.64410   1.000 26.62004  ? 293 TYR B N   1 
ATOM   2209 C  CA  . TYR B 1 293 ? 4.32683   -14.65184 8.36042   1.000 23.93957  ? 293 TYR B CA  1 
ATOM   2210 C  C   . TYR B 1 293 ? 4.42284   -15.73014 7.28101   1.000 27.23365  ? 293 TYR B C   1 
ATOM   2211 O  O   . TYR B 1 293 ? 5.52317   -16.17073 6.91507   1.000 26.86554  ? 293 TYR B O   1 
ATOM   2212 C  CB  . TYR B 1 293 ? 5.60978   -13.81087 8.42743   1.000 25.42570  ? 293 TYR B CB  1 
ATOM   2213 C  CG  . TYR B 1 293 ? 5.86503   -13.10425 9.77231   1.000 24.50926  ? 293 TYR B CG  1 
ATOM   2214 C  CD1 . TYR B 1 293 ? 4.97578   -12.13264 10.26922  1.000 24.43212  ? 293 TYR B CD1 1 
ATOM   2215 C  CD2 . TYR B 1 293 ? 7.02235   -13.36043 10.51050  1.000 21.61813  ? 293 TYR B CD2 1 
ATOM   2216 C  CE1 . TYR B 1 293 ? 5.20806   -11.47279 11.47139  1.000 24.64680  ? 293 TYR B CE1 1 
ATOM   2217 C  CE2 . TYR B 1 293 ? 7.25712   -12.70288 11.74356  1.000 22.61688  ? 293 TYR B CE2 1 
ATOM   2218 C  CZ  . TYR B 1 293 ? 6.35192   -11.75682 12.20374  1.000 25.62874  ? 293 TYR B CZ  1 
ATOM   2219 O  OH  . TYR B 1 293 ? 6.60240   -11.10771 13.40662  1.000 22.86968  ? 293 TYR B OH  1 
ATOM   2220 N  N   . PRO B 1 294 ? 3.28929   -16.18088 6.74520   1.000 33.64375  ? 294 PRO B N   1 
ATOM   2221 C  CA  . PRO B 1 294 ? 3.31996   -17.28408 5.77020   1.000 34.66690  ? 294 PRO B CA  1 
ATOM   2222 C  C   . PRO B 1 294 ? 3.84887   -16.86959 4.40481   1.000 30.45111  ? 294 PRO B C   1 
ATOM   2223 O  O   . PRO B 1 294 ? 3.73027   -15.71741 3.98360   1.000 31.29070  ? 294 PRO B O   1 
ATOM   2224 C  CB  . PRO B 1 294 ? 1.84766   -17.70914 5.66960   1.000 32.85110  ? 294 PRO B CB  1 
ATOM   2225 C  CG  . PRO B 1 294 ? 1.20407   -17.21699 6.93594   1.000 35.45607  ? 294 PRO B CG  1 
ATOM   2226 C  CD  . PRO B 1 294 ? 1.93786   -15.94461 7.28904   1.000 29.23331  ? 294 PRO B CD  1 
ATOM   2227 N  N   . LYS B 1 295 ? 4.40519   -17.86044 3.68670   1.000 28.44352  ? 295 LYS B N   1 
ATOM   2228 C  CA  . LYS B 1 295 ? 4.94337   -17.64413 2.35431   1.000 36.36110  ? 295 LYS B CA  1 
ATOM   2229 C  C   . LYS B 1 295 ? 3.82150   -17.27218 1.38400   1.000 31.38471  ? 295 LYS B C   1 
ATOM   2230 O  O   . LYS B 1 295 ? 2.64738   -17.51272 1.66972   1.000 38.28639  ? 295 LYS B O   1 
ATOM   2231 C  CB  . LYS B 1 295 ? 5.67922   -18.90436 1.88882   1.000 37.59501  ? 295 LYS B CB  1 
ATOM   2232 C  CG  . LYS B 1 295 ? 7.01576   -19.12552 2.58477   1.000 55.27406  ? 295 LYS B CG  1 
ATOM   2233 C  CD  . LYS B 1 295 ? 8.14432   -18.34452 1.92429   1.000 61.04363  ? 295 LYS B CD  1 
ATOM   2234 C  CE  . LYS B 1 295 ? 8.46529   -18.98398 0.57103   1.000 56.49117  ? 295 LYS B CE  1 
ATOM   2235 N  NZ  . LYS B 1 295 ? 9.63135   -18.37572 -0.11158  1.000 58.33797  ? 295 LYS B NZ  1 
ATOM   2236 N  N   . PRO B 1 296 ? 4.15402   -16.65665 0.24432   1.000 37.14090  ? 296 PRO B N   1 
ATOM   2237 C  CA  . PRO B 1 296 ? 3.10018   -16.15810 -0.65736  1.000 43.17399  ? 296 PRO B CA  1 
ATOM   2238 C  C   . PRO B 1 296 ? 2.13674   -17.26697 -1.06204  1.000 44.90974  ? 296 PRO B C   1 
ATOM   2239 O  O   . PRO B 1 296 ? 2.55124   -18.39010 -1.34770  1.000 45.69277  ? 296 PRO B O   1 
ATOM   2240 C  CB  . PRO B 1 296 ? 3.88749   -15.62346 -1.85985  1.000 58.35855  ? 296 PRO B CB  1 
ATOM   2241 C  CG  . PRO B 1 296 ? 5.24882   -15.30424 -1.31327  1.000 39.10539  ? 296 PRO B CG  1 
ATOM   2242 C  CD  . PRO B 1 296 ? 5.50237   -16.38534 -0.29547  1.000 48.23291  ? 296 PRO B CD  1 
ATOM   2243 N  N   . SER B 1 297 ? 0.84342   -16.93589 -1.05634  1.000 68.58088  ? 297 SER B N   1 
ATOM   2244 C  CA  . SER B 1 297 ? -0.27519  -17.85416 -1.32212  1.000 74.25954  ? 297 SER B CA  1 
ATOM   2245 C  C   . SER B 1 297 ? -0.03105  -19.30456 -0.90737  1.000 87.89975  ? 297 SER B C   1 
ATOM   2246 O  O   . SER B 1 297 ? 0.05122   -19.61799 0.27885   1.000 90.93825  ? 297 SER B O   1 
ATOM   2247 C  CB  . SER B 1 297 ? -0.64084  -17.81195 -2.80290  1.000 76.48257  ? 297 SER B CB  1 
ATOM   2248 O  OG  . SER B 1 297 ? -0.93945  -16.49052 -3.21355  1.000 78.63706  ? 297 SER B OG  1 
ATOM   2249 N  N   . LYS B 1 300 ? -4.89006  -12.97238 -1.20773  1.000 46.63302  ? 300 LYS B N   1 
ATOM   2250 C  CA  . LYS B 1 300 ? -5.04437  -12.02541 -0.09101  1.000 45.91178  ? 300 LYS B CA  1 
ATOM   2251 C  C   . LYS B 1 300 ? -4.45289  -12.56383 1.20932   1.000 63.29662  ? 300 LYS B C   1 
ATOM   2252 O  O   . LYS B 1 300 ? -4.90707  -13.57745 1.75301   1.000 52.31087  ? 300 LYS B O   1 
ATOM   2253 C  CB  . LYS B 1 300 ? -6.51774  -11.67594 0.12818   1.000 55.98564  ? 300 LYS B CB  1 
ATOM   2254 N  N   . LYS B 1 301 ? -3.44429  -11.86159 1.71579   1.000 46.53436  ? 301 LYS B N   1 
ATOM   2255 C  CA  . LYS B 1 301 ? -2.77407  -12.23622 2.94534   1.000 37.15044  ? 301 LYS B CA  1 
ATOM   2256 C  C   . LYS B 1 301 ? -2.91208  -11.10680 3.96773   1.000 31.71019  ? 301 LYS B C   1 
ATOM   2257 O  O   . LYS B 1 301 ? -3.40444  -10.01613 3.66728   1.000 31.69230  ? 301 LYS B O   1 
ATOM   2258 C  CB  . LYS B 1 301 ? -1.30266  -12.59406 2.68354   1.000 41.58250  ? 301 LYS B CB  1 
ATOM   2259 C  CG  . LYS B 1 301 ? -0.49947  -11.57083 1.86671   1.000 38.94493  ? 301 LYS B CG  1 
ATOM   2260 C  CD  . LYS B 1 301 ? 0.22795   -10.63143 2.80588   1.000 52.62038  ? 301 LYS B CD  1 
ATOM   2261 C  CE  . LYS B 1 301 ? 0.92756   -9.50300  2.09491   1.000 37.41072  ? 301 LYS B CE  1 
ATOM   2262 N  NZ  . LYS B 1 301 ? 1.20709   -8.44399  3.12097   1.000 34.65751  ? 301 LYS B NZ  1 
ATOM   2263 N  N   . TYR B 1 302 ? -2.48693  -11.38390 5.19288   1.000 32.38879  ? 302 TYR B N   1 
ATOM   2264 C  CA  . TYR B 1 302 ? -2.68042  -10.44805 6.29168   1.000 28.06573  ? 302 TYR B CA  1 
ATOM   2265 C  C   . TYR B 1 302 ? -1.48521  -9.49647  6.42704   1.000 27.14216  ? 302 TYR B C   1 
ATOM   2266 O  O   . TYR B 1 302 ? -0.32496  -9.85960  6.21080   1.000 31.56122  ? 302 TYR B O   1 
ATOM   2267 C  CB  . TYR B 1 302 ? -2.91765  -11.20024 7.61376   1.000 29.31802  ? 302 TYR B CB  1 
ATOM   2268 C  CG  . TYR B 1 302 ? -4.32854  -11.75861 7.76672   1.000 30.19080  ? 302 TYR B CG  1 
ATOM   2269 C  CD1 . TYR B 1 302 ? -5.42816  -10.91230 7.83626   1.000 35.31629  ? 302 TYR B CD1 1 
ATOM   2270 C  CD2 . TYR B 1 302 ? -4.55532  -13.13136 7.80491   1.000 33.86926  ? 302 TYR B CD2 1 
ATOM   2271 C  CE1 . TYR B 1 302 ? -6.71621  -11.40602 7.94251   1.000 29.32335  ? 302 TYR B CE1 1 
ATOM   2272 C  CE2 . TYR B 1 302 ? -5.84379  -13.63925 7.92774   1.000 31.54918  ? 302 TYR B CE2 1 
ATOM   2273 C  CZ  . TYR B 1 302 ? -6.91807  -12.78313 7.99825   1.000 40.76088  ? 302 TYR B CZ  1 
ATOM   2274 O  OH  . TYR B 1 302 ? -8.20016  -13.31590 8.11053   1.000 42.17527  ? 302 TYR B OH  1 
ATOM   2275 N  N   . ALA B 1 303 ? -1.79144  -8.27450  6.83523   1.000 22.90342  ? 303 ALA B N   1 
ATOM   2276 C  CA  . ALA B 1 303 ? -0.77389  -7.22974  6.91505   1.000 23.80656  ? 303 ALA B CA  1 
ATOM   2277 C  C   . ALA B 1 303 ? 0.17813   -7.39079  8.09201   1.000 23.03646  ? 303 ALA B C   1 
ATOM   2278 O  O   . ALA B 1 303 ? 1.13751   -6.61535  8.20499   1.000 22.11620  ? 303 ALA B O   1 
ATOM   2279 C  CB  . ALA B 1 303 ? -1.43702  -5.86447  7.01659   1.000 23.32908  ? 303 ALA B CB  1 
ATOM   2280 N  N   . ARG B 1 304 ? -0.04737  -8.35967  8.97996   1.000 23.23629  ? 304 ARG B N   1 
ATOM   2281 C  CA  . ARG B 1 304 ? 0.83999   -8.37279  10.14340  1.000 22.87188  ? 304 ARG B CA  1 
ATOM   2282 C  C   . ARG B 1 304 ? 2.25320   -8.83968  9.77878   1.000 23.05414  ? 304 ARG B C   1 
ATOM   2283 O  O   . ARG B 1 304 ? 3.16801   -8.69587  10.59923  1.000 22.12423  ? 304 ARG B O   1 
ATOM   2284 C  CB  . ARG B 1 304 ? 0.26828   -9.24690  11.25548  1.000 26.19737  ? 304 ARG B CB  1 
ATOM   2285 C  CG  . ARG B 1 304 ? 0.00985   -10.64239 10.82249  1.000 30.45076  ? 304 ARG B CG  1 
ATOM   2286 C  CD  . ARG B 1 304 ? -0.68696  -11.47507 11.93178  1.000 38.07771  ? 304 ARG B CD  1 
ATOM   2287 N  NE  . ARG B 1 304 ? -0.67122  -12.86586 11.48560  1.000 35.83421  ? 304 ARG B NE  1 
ATOM   2288 C  CZ  . ARG B 1 304 ? -0.96265  -13.94284 12.21457  1.000 29.61283  ? 304 ARG B CZ  1 
ATOM   2289 N  NH1 . ARG B 1 304 ? -1.32164  -13.83856 13.49636  1.000 28.56949  ? 304 ARG B NH1 1 
ATOM   2290 N  NH2 . ARG B 1 304 ? -0.88382  -15.14168 11.63699  1.000 31.41035  ? 304 ARG B NH2 1 
ATOM   2291 N  N   . ASP B 1 305 ? 2.46643   -9.31858  8.55549   1.000 21.01441  ? 305 ASP B N   1 
ATOM   2292 C  CA  . ASP B 1 305 ? 3.81553   -9.60949  8.07988   1.000 21.71586  ? 305 ASP B CA  1 
ATOM   2293 C  C   . ASP B 1 305 ? 4.55261   -8.35594  7.59386   1.000 25.32830  ? 305 ASP B C   1 
ATOM   2294 O  O   . ASP B 1 305 ? 5.62032   -8.47283  6.99666   1.000 27.37538  ? 305 ASP B O   1 
ATOM   2295 C  CB  . ASP B 1 305 ? 3.79528   -10.70500 6.97306   1.000 25.61945  ? 305 ASP B CB  1 
ATOM   2296 C  CG  . ASP B 1 305 ? 3.10319   -10.26504 5.67837   1.000 28.48161  ? 305 ASP B CG  1 
ATOM   2297 O  OD1 . ASP B 1 305 ? 2.59629   -9.13996  5.60077   1.000 27.95274  ? 305 ASP B OD1 1 
ATOM   2298 O  OD2 . ASP B 1 305 ? 3.06338   -11.07040 4.71975   1.000 29.34345  ? 305 ASP B OD2 1 
ATOM   2299 N  N   . ILE B 1 306 ? 4.03387   -7.15817  7.88163   1.000 20.46119  ? 306 ILE B N   1 
ATOM   2300 C  CA  . ILE B 1 306 ? 4.68220   -5.90198  7.51534   1.000 19.00907  ? 306 ILE B CA  1 
ATOM   2301 C  C   . ILE B 1 306 ? 4.94359   -5.08961  8.77436   1.000 21.50209  ? 306 ILE B C   1 
ATOM   2302 O  O   . ILE B 1 306 ? 4.08355   -5.03136  9.66228   1.000 20.77773  ? 306 ILE B O   1 
ATOM   2303 C  CB  . ILE B 1 306 ? 3.80589   -5.07516  6.55687   1.000 19.11442  ? 306 ILE B CB  1 
ATOM   2304 C  CG1 . ILE B 1 306 ? 3.64229   -5.80630  5.23176   1.000 24.90264  ? 306 ILE B CG1 1 
ATOM   2305 C  CG2 . ILE B 1 306 ? 4.36196   -3.62812  6.38292   1.000 19.59079  ? 306 ILE B CG2 1 
ATOM   2306 C  CD1 . ILE B 1 306 ? 2.46023   -5.27042  4.47073   1.000 28.45779  ? 306 ILE B CD1 1 
ATOM   2307 N  N   . VAL B 1 307 ? 6.09504   -4.41476  8.82454   1.000 17.95332  ? 307 VAL B N   1 
ATOM   2308 C  CA  . VAL B 1 307 ? 6.34323   -3.33858  9.80291   1.000 18.06578  ? 307 VAL B CA  1 
ATOM   2309 C  C   . VAL B 1 307 ? 6.76521   -2.09515  9.05058   1.000 23.01566  ? 307 VAL B C   1 
ATOM   2310 O  O   . VAL B 1 307 ? 7.64690   -2.17513  8.18760   1.000 22.73392  ? 307 VAL B O   1 
ATOM   2311 C  CB  . VAL B 1 307 ? 7.45889   -3.69936  10.79977  1.000 31.52243  ? 307 VAL B CB  1 
ATOM   2312 C  CG1 . VAL B 1 307 ? 7.70803   -2.53399  11.80208  1.000 24.67688  ? 307 VAL B CG1 1 
ATOM   2313 C  CG2 . VAL B 1 307 ? 7.14855   -4.96120  11.50974  1.000 39.60040  ? 307 VAL B CG2 1 
ATOM   2314 N  N   . TYR B 1 308 ? 6.14987   -0.95227  9.37445   1.000 19.72280  ? 308 TYR B N   1 
ATOM   2315 C  CA  . TYR B 1 308 ? 6.52591   0.34074   8.80535   1.000 19.75804  ? 308 TYR B CA  1 
ATOM   2316 C  C   . TYR B 1 308 ? 7.29535   1.16357   9.81826   1.000 23.22200  ? 308 TYR B C   1 
ATOM   2317 O  O   . TYR B 1 308 ? 6.96393   1.16595   11.00788  1.000 24.86099  ? 308 TYR B O   1 
ATOM   2318 C  CB  . TYR B 1 308 ? 5.30290   1.17076   8.39714   1.000 18.85220  ? 308 TYR B CB  1 
ATOM   2319 C  CG  . TYR B 1 308 ? 4.64768   0.78508   7.08819   1.000 20.25334  ? 308 TYR B CG  1 
ATOM   2320 C  CD1 . TYR B 1 308 ? 5.15827   1.26448   5.87109   1.000 21.10582  ? 308 TYR B CD1 1 
ATOM   2321 C  CD2 . TYR B 1 308 ? 3.51431   -0.00593  7.05191   1.000 17.43550  ? 308 TYR B CD2 1 
ATOM   2322 C  CE1 . TYR B 1 308 ? 4.56239   0.95925   4.67069   1.000 19.48919  ? 308 TYR B CE1 1 
ATOM   2323 C  CE2 . TYR B 1 308 ? 2.91335   -0.32833  5.82849   1.000 21.14217  ? 308 TYR B CE2 1 
ATOM   2324 C  CZ  . TYR B 1 308 ? 3.44993   0.17354   4.64269   1.000 23.49438  ? 308 TYR B CZ  1 
ATOM   2325 O  OH  . TYR B 1 308 ? 2.84712   -0.12708  3.41610   1.000 28.44891  ? 308 TYR B OH  1 
ATOM   2326 N  N   . GLY B 1 309 ? 8.27263   1.91678   9.32883   1.000 21.05231  ? 309 GLY B N   1 
ATOM   2327 C  CA  . GLY B 1 309 ? 8.95138   2.90574   10.14040  1.000 19.18353  ? 309 GLY B CA  1 
ATOM   2328 C  C   . GLY B 1 309 ? 9.33452   4.08186   9.27849   1.000 23.89705  ? 309 GLY B C   1 
ATOM   2329 O  O   . GLY B 1 309 ? 9.24735   4.03261   8.05206   1.000 26.45169  ? 309 GLY B O   1 
ATOM   2330 N  N   . THR B 1 310 ? 9.68727   5.17169   9.93753   1.000 21.34552  ? 310 THR B N   1 
ATOM   2331 C  CA  . THR B 1 310 ? 10.14524  6.35680   9.24390   1.000 20.07320  ? 310 THR B CA  1 
ATOM   2332 C  C   . THR B 1 310 ? 11.59560  6.60368   9.63570   1.000 24.11372  ? 310 THR B C   1 
ATOM   2333 O  O   . THR B 1 310 ? 11.92169  6.63557   10.83219  1.000 22.71545  ? 310 THR B O   1 
ATOM   2334 C  CB  . THR B 1 310 ? 9.25765   7.57245   9.58091   1.000 23.88880  ? 310 THR B CB  1 
ATOM   2335 O  OG1 . THR B 1 310 ? 7.88432   7.25749   9.31469   1.000 27.77443  ? 310 THR B OG1 1 
ATOM   2336 C  CG2 . THR B 1 310 ? 9.64874   8.73662   8.71357   1.000 22.98713  ? 310 THR B CG2 1 
ATOM   2337 N  N   . ILE B 1 311 ? 12.46145  6.77506   8.64132   1.000 20.22528  ? 311 ILE B N   1 
ATOM   2338 C  CA  . ILE B 1 311 ? 13.81164  7.23576   8.89830   1.000 17.44346  ? 311 ILE B CA  1 
ATOM   2339 C  C   . ILE B 1 311 ? 13.98692  8.57975   8.18973   1.000 20.18270  ? 311 ILE B C   1 
ATOM   2340 O  O   . ILE B 1 311 ? 13.09044  9.06599   7.50466   1.000 24.19598  ? 311 ILE B O   1 
ATOM   2341 C  CB  . ILE B 1 311 ? 14.89348  6.20137   8.51206   1.000 21.44317  ? 311 ILE B CB  1 
ATOM   2342 C  CG1 . ILE B 1 311 ? 14.72813  5.61960   7.10303   1.000 23.12528  ? 311 ILE B CG1 1 
ATOM   2343 C  CG2 . ILE B 1 311 ? 14.84793  5.00608   9.50627   1.000 21.41508  ? 311 ILE B CG2 1 
ATOM   2344 C  CD1 . ILE B 1 311 ? 14.90191  6.61724   5.92678   1.000 27.86564  ? 311 ILE B CD1 1 
ATOM   2345 N  N   . TYR B 1 312 ? 15.13226  9.21518   8.42160   1.000 20.29620  ? 312 TYR B N   1 
ATOM   2346 C  CA  . TYR B 1 312 ? 15.30277  10.58962  7.96971   1.000 20.62299  ? 312 TYR B CA  1 
ATOM   2347 C  C   . TYR B 1 312 ? 16.60422  10.72532  7.19933   1.000 22.90098  ? 312 TYR B C   1 
ATOM   2348 O  O   . TYR B 1 312 ? 17.65762  10.30953  7.68233   1.000 22.10573  ? 312 TYR B O   1 
ATOM   2349 C  CB  . TYR B 1 312 ? 15.27166  11.57658  9.14999   1.000 20.36177  ? 312 TYR B CB  1 
ATOM   2350 C  CG  . TYR B 1 312 ? 13.89708  11.56133  9.73551   1.000 24.29463  ? 312 TYR B CG  1 
ATOM   2351 C  CD1 . TYR B 1 312 ? 13.52930  10.57704  10.66638  1.000 21.31613  ? 312 TYR B CD1 1 
ATOM   2352 C  CD2 . TYR B 1 312 ? 12.93212  12.45702  9.29044   1.000 22.47882  ? 312 TYR B CD2 1 
ATOM   2353 C  CE1 . TYR B 1 312 ? 12.22219  10.49053  11.15442  1.000 24.30858  ? 312 TYR B CE1 1 
ATOM   2354 C  CE2 . TYR B 1 312 ? 11.61766  12.39186  9.79373   1.000 26.84338  ? 312 TYR B CE2 1 
ATOM   2355 C  CZ  . TYR B 1 312 ? 11.28094  11.41743  10.72889  1.000 23.83100  ? 312 TYR B CZ  1 
ATOM   2356 O  OH  . TYR B 1 312 ? 9.97052   11.36713  11.22349  1.000 26.75221  ? 312 TYR B OH  1 
ATOM   2357 N  N   . LEU B 1 313 ? 16.53111  11.31403  6.00861   1.000 23.21726  ? 313 LEU B N   1 
ATOM   2358 C  CA  . LEU B 1 313 ? 17.71940  11.37952  5.16399   1.000 24.53715  ? 313 LEU B CA  1 
ATOM   2359 C  C   . LEU B 1 313 ? 18.64827  12.47416  5.66239   1.000 22.29048  ? 313 LEU B C   1 
ATOM   2360 O  O   . LEU B 1 313 ? 18.21139  13.58443  5.97398   1.000 24.84112  ? 313 LEU B O   1 
ATOM   2361 C  CB  . LEU B 1 313 ? 17.33762  11.61941  3.69389   1.000 24.55206  ? 313 LEU B CB  1 
ATOM   2362 C  CG  . LEU B 1 313 ? 16.34103  10.58334  3.14853   1.000 24.15813  ? 313 LEU B CG  1 
ATOM   2363 C  CD1 . LEU B 1 313 ? 16.02387  10.83706  1.66041   1.000 25.13418  ? 313 LEU B CD1 1 
ATOM   2364 C  CD2 . LEU B 1 313 ? 16.83840  9.13814   3.33037   1.000 27.07028  ? 313 LEU B CD2 1 
ATOM   2365 N  N   . GLY B 1 314 ? 19.92696  12.13835  5.77349   1.000 23.63258  ? 314 GLY B N   1 
ATOM   2366 C  CA  . GLY B 1 314 ? 20.92959  13.06387  6.26162   1.000 28.09154  ? 314 GLY B CA  1 
ATOM   2367 C  C   . GLY B 1 314 ? 20.69445  13.48329  7.69281   1.000 35.23321  ? 314 GLY B C   1 
ATOM   2368 O  O   . GLY B 1 314 ? 21.27938  14.46210  8.15571   1.000 32.10714  ? 314 GLY B O   1 
ATOM   2369 N  N   . GLY B 1 315 ? 19.81864  12.76158  8.39577   1.000 25.71912  ? 315 GLY B N   1 
ATOM   2370 C  CA  . GLY B 1 315 ? 19.49866  13.11980  9.76727   1.000 24.20680  ? 315 GLY B CA  1 
ATOM   2371 C  C   . GLY B 1 315 ? 18.65826  14.35889  9.89904   1.000 28.83212  ? 315 GLY B C   1 
ATOM   2372 O  O   . GLY B 1 315 ? 18.49242  14.85451  11.01303  1.000 26.09959  ? 315 GLY B O   1 
ATOM   2373 N  N   . LYS B 1 316 ? 18.10408  14.87174  8.78503   1.000 25.31885  ? 316 LYS B N   1 
ATOM   2374 C  CA  . LYS B 1 316 ? 17.33597  16.10798  8.83335   1.000 26.52320  ? 316 LYS B CA  1 
ATOM   2375 C  C   . LYS B 1 316 ? 15.87523  15.78875  9.12133   1.000 23.32424  ? 316 LYS B C   1 
ATOM   2376 O  O   . LYS B 1 316 ? 15.28578  14.96323  8.42272   1.000 25.66789  ? 316 LYS B O   1 
ATOM   2377 C  CB  . LYS B 1 316 ? 17.46519  16.86831  7.52527   1.000 30.47455  ? 316 LYS B CB  1 
ATOM   2378 C  CG  . LYS B 1 316 ? 18.91989  17.22081  7.21798   1.000 38.11106  ? 316 LYS B CG  1 
ATOM   2379 C  CD  . LYS B 1 316 ? 19.00953  18.10981  6.00394   1.000 45.76270  ? 316 LYS B CD  1 
ATOM   2380 N  N   . PRO B 1 317 ? 15.26020  16.44498  10.11207  1.000 23.17837  ? 317 PRO B N   1 
ATOM   2381 C  CA  . PRO B 1 317 ? 13.91268  16.04735  10.53442  1.000 21.31355  ? 317 PRO B CA  1 
ATOM   2382 C  C   . PRO B 1 317 ? 12.83365  16.37108  9.52263   1.000 23.91802  ? 317 PRO B C   1 
ATOM   2383 O  O   . PRO B 1 317 ? 11.74928  15.79606  9.61591   1.000 26.95466  ? 317 PRO B O   1 
ATOM   2384 C  CB  . PRO B 1 317 ? 13.70576  16.83387  11.84850  1.000 27.53073  ? 317 PRO B CB  1 
ATOM   2385 C  CG  . PRO B 1 317 ? 14.66065  17.98582  11.74416  1.000 28.59115  ? 317 PRO B CG  1 
ATOM   2386 C  CD  . PRO B 1 317 ? 15.86029  17.42621  11.03629  1.000 27.37185  ? 317 PRO B CD  1 
ATOM   2387 N  N   . ASP B 1 318 ? 13.09877  17.23428  8.53459   1.000 26.05356  ? 318 ASP B N   1 
ATOM   2388 C  CA  . ASP B 1 318 ? 12.13258  17.46534  7.46663   1.000 26.69785  ? 318 ASP B CA  1 
ATOM   2389 C  C   . ASP B 1 318 ? 12.46054  16.65848  6.21465   1.000 28.83023  ? 318 ASP B C   1 
ATOM   2390 O  O   . ASP B 1 318 ? 11.95538  16.96949  5.12922   1.000 28.16163  ? 318 ASP B O   1 
ATOM   2391 C  CB  . ASP B 1 318 ? 12.03014  18.96031  7.13367   1.000 28.26554  ? 318 ASP B CB  1 
ATOM   2392 C  CG  . ASP B 1 318 ? 13.29336  19.51993  6.56303   1.000 40.02366  ? 318 ASP B CG  1 
ATOM   2393 O  OD1 . ASP B 1 318 ? 14.35114  18.87465  6.65871   1.000 36.94834  ? 318 ASP B OD1 1 
ATOM   2394 O  OD2 . ASP B 1 318 ? 13.21996  20.62793  6.00617   1.000 44.85587  ? 318 ASP B OD2 1 
ATOM   2395 N  N   . GLN B 1 319 ? 13.25588  15.59520  6.35107   1.000 24.24416  ? 319 GLN B N   1 
ATOM   2396 C  CA  . GLN B 1 319 ? 13.54928  14.70040  5.23788   1.000 23.09982  ? 319 GLN B CA  1 
ATOM   2397 C  C   . GLN B 1 319 ? 13.16485  13.24768  5.53579   1.000 19.10389  ? 319 GLN B C   1 
ATOM   2398 O  O   . GLN B 1 319 ? 13.99891  12.34262  5.40841   1.000 22.71143  ? 319 GLN B O   1 
ATOM   2399 C  CB  . GLN B 1 319 ? 15.02174  14.82568  4.85080   1.000 24.78598  ? 319 GLN B CB  1 
ATOM   2400 C  CG  . GLN B 1 319 ? 15.25978  16.19572  4.18862   1.000 28.00560  ? 319 GLN B CG  1 
ATOM   2401 C  CD  . GLN B 1 319 ? 16.66733  16.41783  3.73615   1.000 27.60211  ? 319 GLN B CD  1 
ATOM   2402 O  OE1 . GLN B 1 319 ? 17.58218  15.62365  4.02264   1.000 34.94143  ? 319 GLN B OE1 1 
ATOM   2403 N  NE2 . GLN B 1 319 ? 16.87214  17.52072  3.02550   1.000 29.20928  ? 319 GLN B NE2 1 
ATOM   2404 N  N   . PRO B 1 320 ? 11.89001  12.97765  5.83856   1.000 23.36778  ? 320 PRO B N   1 
ATOM   2405 C  CA  . PRO B 1 320 ? 11.47976  11.59309  6.09340   1.000 20.48488  ? 320 PRO B CA  1 
ATOM   2406 C  C   . PRO B 1 320 ? 11.49889  10.73122  4.84217   1.000 22.95679  ? 320 PRO B C   1 
ATOM   2407 O  O   . PRO B 1 320 ? 11.18746  11.17240  3.73795   1.000 25.10009  ? 320 PRO B O   1 
ATOM   2408 C  CB  . PRO B 1 320 ? 10.03336  11.72924  6.61802   1.000 23.54372  ? 320 PRO B CB  1 
ATOM   2409 C  CG  . PRO B 1 320 ? 9.55157   13.04498  5.97698   1.000 23.90591  ? 320 PRO B CG  1 
ATOM   2410 C  CD  . PRO B 1 320 ? 10.77542  13.91902  6.07930   1.000 26.85509  ? 320 PRO B CD  1 
ATOM   2411 N  N   . ALA B 1 321 ? 11.79079  9.45587   5.05781   1.000 20.83026  ? 321 ALA B N   1 
ATOM   2412 C  CA  . ALA B 1 321 ? 11.51949  8.40168   4.09582   1.000 25.09209  ? 321 ALA B CA  1 
ATOM   2413 C  C   . ALA B 1 321 ? 10.95188  7.19646   4.85332   1.000 25.81328  ? 321 ALA B C   1 
ATOM   2414 O  O   . ALA B 1 321 ? 11.22768  6.99355   6.04286   1.000 22.28189  ? 321 ALA B O   1 
ATOM   2415 C  CB  . ALA B 1 321 ? 12.80059  8.03282   3.31787   1.000 22.71138  ? 321 ALA B CB  1 
ATOM   2416 N  N   . VAL B 1 322 ? 10.17518  6.38415   4.16048   1.000 22.16308  ? 322 VAL B N   1 
ATOM   2417 C  CA  . VAL B 1 322 ? 9.48598   5.24776   4.77651   1.000 21.08687  ? 322 VAL B CA  1 
ATOM   2418 C  C   . VAL B 1 322 ? 10.32413  3.99273   4.59176   1.000 23.23378  ? 322 VAL B C   1 
ATOM   2419 O  O   . VAL B 1 322 ? 10.71297  3.67020   3.46521   1.000 24.75242  ? 322 VAL B O   1 
ATOM   2420 C  CB  . VAL B 1 322 ? 8.10519   5.05000   4.13250   1.000 20.04481  ? 322 VAL B CB  1 
ATOM   2421 C  CG1 . VAL B 1 322 ? 7.41624   3.75999   4.64960   1.000 22.82612  ? 322 VAL B CG1 1 
ATOM   2422 C  CG2 . VAL B 1 322 ? 7.21918   6.27838   4.39945   1.000 30.26851  ? 322 VAL B CG2 1 
ATOM   2423 N  N   . ILE B 1 323 ? 10.56221  3.23519   5.66562   1.000 17.81185  ? 323 ILE B N   1 
ATOM   2424 C  CA  . ILE B 1 323 ? 11.13282  1.90731   5.48688   1.000 19.28178  ? 323 ILE B CA  1 
ATOM   2425 C  C   . ILE B 1 323 ? 10.03345  0.89723   5.75863   1.000 26.02332  ? 323 ILE B C   1 
ATOM   2426 O  O   . ILE B 1 323 ? 9.43515   0.88283   6.84280   1.000 23.96986  ? 323 ILE B O   1 
ATOM   2427 C  CB  . ILE B 1 323 ? 12.38534  1.69659   6.35713   1.000 19.59006  ? 323 ILE B CB  1 
ATOM   2428 C  CG1 . ILE B 1 323 ? 12.88678  0.25316   6.22441   1.000 31.17426  ? 323 ILE B CG1 1 
ATOM   2429 C  CG2 . ILE B 1 323 ? 12.12988  2.11395   7.84181   1.000 30.38597  ? 323 ILE B CG2 1 
ATOM   2430 C  CD1 . ILE B 1 323 ? 14.19066  0.03444   6.96971   1.000 36.08193  ? 323 ILE B CD1 1 
ATOM   2431 N  N   . LYS B 1 324 ? 9.70946   0.10781   4.74364   1.000 18.66650  ? 324 LYS B N   1 
ATOM   2432 C  CA  . LYS B 1 324 ? 8.68570   -0.92520  4.84577   1.000 21.96963  ? 324 LYS B CA  1 
ATOM   2433 C  C   . LYS B 1 324 ? 9.38495   -2.27145  4.87168   1.000 29.40632  ? 324 LYS B C   1 
ATOM   2434 O  O   . LYS B 1 324 ? 10.05773  -2.63094  3.90293   1.000 26.57198  ? 324 LYS B O   1 
ATOM   2435 C  CB  . LYS B 1 324 ? 7.72678   -0.85324  3.65353   1.000 20.50212  ? 324 LYS B CB  1 
ATOM   2436 C  CG  . LYS B 1 324 ? 6.65002   -1.89140  3.70663   1.000 21.56528  ? 324 LYS B CG  1 
ATOM   2437 C  CD  . LYS B 1 324 ? 5.78915   -1.80847  2.42040   1.000 27.45820  ? 324 LYS B CD  1 
ATOM   2438 C  CE  . LYS B 1 324 ? 4.70705   -2.87102  2.39993   1.000 34.03203  ? 324 LYS B CE  1 
ATOM   2439 N  NZ  . LYS B 1 324 ? 4.07003   -2.95968  1.03419   1.000 40.11422  ? 324 LYS B NZ  1 
ATOM   2440 N  N   . THR B 1 325 ? 9.19159   -3.04048  5.93980   1.000 18.70089  ? 325 THR B N   1 
ATOM   2441 C  CA  . THR B 1 325 ? 9.85139   -4.33966  6.09088   1.000 18.54977  ? 325 THR B CA  1 
ATOM   2442 C  C   . THR B 1 325 ? 8.79325   -5.43247  6.02150   1.000 22.78769  ? 325 THR B C   1 
ATOM   2443 O  O   . THR B 1 325 ? 7.79614   -5.37831  6.75404   1.000 23.00238  ? 325 THR B O   1 
ATOM   2444 C  CB  . THR B 1 325 ? 10.60661  -4.40150  7.43332   1.000 18.06019  ? 325 THR B CB  1 
ATOM   2445 O  OG1 . THR B 1 325 ? 11.57036  -3.35156  7.47038   1.000 21.71720  ? 325 THR B OG1 1 
ATOM   2446 C  CG2 . THR B 1 325 ? 11.35017  -5.74778  7.56880   1.000 20.19106  ? 325 THR B CG2 1 
ATOM   2447 N  N   . THR B 1 326 ? 8.99519   -6.41075  5.13940   1.000 21.61464  ? 326 THR B N   1 
ATOM   2448 C  CA  . THR B 1 326 ? 8.01554   -7.46535  4.91019   1.000 19.97606  ? 326 THR B CA  1 
ATOM   2449 C  C   . THR B 1 326 ? 8.69976   -8.81432  5.11367   1.000 25.83628  ? 326 THR B C   1 
ATOM   2450 O  O   . THR B 1 326 ? 9.80851   -9.02476  4.60880   1.000 22.95700  ? 326 THR B O   1 
ATOM   2451 C  CB  . THR B 1 326 ? 7.42782   -7.37428  3.49316   1.000 25.71756  ? 326 THR B CB  1 
ATOM   2452 O  OG1 . THR B 1 326 ? 6.91842   -6.05747  3.26493   1.000 26.97178  ? 326 THR B OG1 1 
ATOM   2453 C  CG2 . THR B 1 326 ? 6.29263   -8.34841  3.34787   1.000 25.94602  ? 326 THR B CG2 1 
ATOM   2454 N  N   . PHE B 1 327 ? 8.06644   -9.70319  5.87061   1.000 19.82507  ? 327 PHE B N   1 
ATOM   2455 C  CA  . PHE B 1 327 ? 8.62162   -11.03540 6.14536   1.000 25.81993  ? 327 PHE B CA  1 
ATOM   2456 C  C   . PHE B 1 327 ? 8.00055   -12.09852 5.24870   1.000 27.69593  ? 327 PHE B C   1 
ATOM   2457 O  O   . PHE B 1 327 ? 6.77072   -12.16560 5.10956   1.000 26.96333  ? 327 PHE B O   1 
ATOM   2458 C  CB  . PHE B 1 327 ? 8.44329   -11.40413 7.63154   1.000 19.86599  ? 327 PHE B CB  1 
ATOM   2459 C  CG  . PHE B 1 327 ? 8.93992   -10.31686 8.53846   1.000 22.86408  ? 327 PHE B CG  1 
ATOM   2460 C  CD1 . PHE B 1 327 ? 10.30255  -10.06935 8.63288   1.000 24.48058  ? 327 PHE B CD1 1 
ATOM   2461 C  CD2 . PHE B 1 327 ? 8.05803   -9.47124  9.20750   1.000 26.83074  ? 327 PHE B CD2 1 
ATOM   2462 C  CE1 . PHE B 1 327 ? 10.78276  -9.03305  9.39732   1.000 21.30445  ? 327 PHE B CE1 1 
ATOM   2463 C  CE2 . PHE B 1 327 ? 8.53188   -8.44594  9.97917   1.000 24.85751  ? 327 PHE B CE2 1 
ATOM   2464 C  CZ  . PHE B 1 327 ? 9.91595   -8.20319  10.04839  1.000 21.55437  ? 327 PHE B CZ  1 
ATOM   2465 N  N   . ASN B 1 328 ? 8.87160   -12.91759 4.64215   1.000 23.61794  ? 328 ASN B N   1 
ATOM   2466 C  CA  . ASN B 1 328 ? 8.51389   -14.17674 3.98821   1.000 29.25055  ? 328 ASN B CA  1 
ATOM   2467 C  C   . ASN B 1 328 ? 7.56243   -13.96626 2.82164   1.000 31.39398  ? 328 ASN B C   1 
ATOM   2468 O  O   . ASN B 1 328 ? 6.64257   -14.75486 2.61571   1.000 35.00171  ? 328 ASN B O   1 
ATOM   2469 C  CB  . ASN B 1 328 ? 7.91773   -15.18128 4.98599   1.000 25.39627  ? 328 ASN B CB  1 
ATOM   2470 C  CG  . ASN B 1 328 ? 8.91381   -15.59787 6.03973   1.000 28.51400  ? 328 ASN B CG  1 
ATOM   2471 O  OD1 . ASN B 1 328 ? 10.10749  -15.45699 5.82879   1.000 27.51753  ? 328 ASN B OD1 1 
ATOM   2472 N  ND2 . ASN B 1 328 ? 8.43454   -16.08619 7.18290   1.000 25.01921  ? 328 ASN B ND2 1 
ATOM   2473 N  N   . GLN B 1 329 ? 7.74618   -12.88343 2.06752   1.000 28.37405  ? 329 GLN B N   1 
ATOM   2474 C  CA  . GLN B 1 329 ? 6.88804   -12.67641 0.90665   1.000 24.44152  ? 329 GLN B CA  1 
ATOM   2475 C  C   . GLN B 1 329 ? 7.61529   -12.81089 -0.41848  1.000 35.49950  ? 329 GLN B C   1 
ATOM   2476 O  O   . GLN B 1 329 ? 7.07284   -12.39028 -1.43833  1.000 38.38222  ? 329 GLN B O   1 
ATOM   2477 C  CB  . GLN B 1 329 ? 6.19225   -11.30978 0.96436   1.000 25.54488  ? 329 GLN B CB  1 
ATOM   2478 C  CG  . GLN B 1 329 ? 5.01479   -11.31746 1.96616   1.000 29.15210  ? 329 GLN B CG  1 
ATOM   2479 C  CD  . GLN B 1 329 ? 3.81830   -12.18327 1.50561   1.000 36.42148  ? 329 GLN B CD  1 
ATOM   2480 O  OE1 . GLN B 1 329 ? 3.53416   -13.24627 2.06741   1.000 37.19460  ? 329 GLN B OE1 1 
ATOM   2481 N  NE2 . GLN B 1 329 ? 3.10879   -11.70698 0.50416   1.000 35.45898  ? 329 GLN B NE2 1 
ATOM   2482 N  N   . GLU B 1 330 ? 8.82255   -13.34567 -0.42968  1.000 30.76717  ? 330 GLU B N   1 
ATOM   2483 C  CA  . GLU B 1 330 ? 9.53077   -13.60844 -1.67645  1.000 27.66846  ? 330 GLU B CA  1 
ATOM   2484 C  C   . GLU B 1 330 ? 9.39620   -15.07995 -2.00959  1.000 31.33747  ? 330 GLU B C   1 
ATOM   2485 O  O   . GLU B 1 330 ? 9.18699   -15.90336 -1.12248  1.000 34.96748  ? 330 GLU B O   1 
ATOM   2486 C  CB  . GLU B 1 330 ? 11.01456  -13.25142 -1.57230  1.000 29.39600  ? 330 GLU B CB  1 
ATOM   2487 C  CG  . GLU B 1 330 ? 11.22387  -11.80442 -1.14838  1.000 30.11727  ? 330 GLU B CG  1 
ATOM   2488 C  CD  . GLU B 1 330 ? 10.80736  -10.82067 -2.22594  1.000 50.08061  ? 330 GLU B CD  1 
ATOM   2489 O  OE1 . GLU B 1 330 ? 10.96163  -11.14151 -3.42240  1.000 41.14555  ? 330 GLU B OE1 1 
ATOM   2490 O  OE2 . GLU B 1 330 ? 10.32826  -9.72662  -1.88501  1.000 35.03815  ? 330 GLU B OE2 1 
ATOM   2491 N  N   . THR B 1 331 ? 9.50563   -15.40073 -3.30096  1.000 36.40063  ? 331 THR B N   1 
ATOM   2492 C  CA  . THR B 1 331 ? 9.56014   -16.78420 -3.74696  1.000 41.71312  ? 331 THR B CA  1 
ATOM   2493 C  C   . THR B 1 331 ? 11.00652  -17.17707 -4.00344  1.000 35.10581  ? 331 THR B C   1 
ATOM   2494 O  O   . THR B 1 331 ? 11.91470  -16.34275 -4.00871  1.000 48.29135  ? 331 THR B O   1 
ATOM   2495 C  CB  . THR B 1 331 ? 8.72290   -16.98800 -5.01069  1.000 46.01173  ? 331 THR B CB  1 
ATOM   2496 O  OG1 . THR B 1 331 ? 9.11351   -16.02000 -5.99141  1.000 43.88074  ? 331 THR B OG1 1 
ATOM   2497 C  CG2 . THR B 1 331 ? 7.24280   -16.83588 -4.69993  1.000 61.24839  ? 331 THR B CG2 1 
ATOM   2498 N  N   . GLY B 1 332 ? 11.21556  -18.46790 -4.23746  1.000 34.27739  ? 332 GLY B N   1 
ATOM   2499 C  CA  . GLY B 1 332 ? 12.55994  -18.94867 -4.48382  1.000 37.70918  ? 332 GLY B CA  1 
ATOM   2500 C  C   . GLY B 1 332 ? 13.42373  -19.04170 -3.25271  1.000 47.10908  ? 332 GLY B C   1 
ATOM   2501 O  O   . GLY B 1 332 ? 14.65156  -19.04476 -3.36429  1.000 52.55378  ? 332 GLY B O   1 
ATOM   2502 N  N   . CYS B 1 333 ? 12.81924  -19.11230 -2.07498  1.000 41.02241  ? 333 CYS B N   1 
ATOM   2503 C  CA  . CYS B 1 333 ? 13.57515  -19.17893 -0.83129  1.000 42.22188  ? 333 CYS B CA  1 
ATOM   2504 C  C   . CYS B 1 333 ? 12.67292  -19.79782 0.21689   1.000 34.19082  ? 333 CYS B C   1 
ATOM   2505 O  O   . CYS B 1 333 ? 11.47003  -19.94701 0.00573   1.000 42.19187  ? 333 CYS B O   1 
ATOM   2506 C  CB  . CYS B 1 333 ? 14.04908  -17.79695 -0.39789  1.000 36.42615  ? 333 CYS B CB  1 
ATOM   2507 S  SG  . CYS B 1 333 ? 12.67851  -16.64074 -0.22401  1.000 38.52840  ? 333 CYS B SG  1 
ATOM   2508 N  N   . GLU B 1 334 ? 13.26115  -20.14434 1.36502   1.000 31.07923  ? 334 GLU B N   1 
ATOM   2509 C  CA  . GLU B 1 334 ? 12.45327  -20.61693 2.47990   1.000 30.91406  ? 334 GLU B CA  1 
ATOM   2510 C  C   . GLU B 1 334 ? 12.00292  -19.48024 3.39258   1.000 31.27027  ? 334 GLU B C   1 
ATOM   2511 O  O   . GLU B 1 334 ? 10.89075  -19.52763 3.92312   1.000 32.41036  ? 334 GLU B O   1 
ATOM   2512 C  CB  . GLU B 1 334 ? 13.21161  -21.67092 3.29141   1.000 36.87969  ? 334 GLU B CB  1 
ATOM   2513 C  CG  . GLU B 1 334 ? 13.04046  -23.09764 2.74330   1.000 65.28978  ? 334 GLU B CG  1 
ATOM   2514 C  CD  . GLU B 1 334 ? 11.57568  -23.50970 2.64873   1.000 64.60537  ? 334 GLU B CD  1 
ATOM   2515 O  OE1 . GLU B 1 334 ? 11.14868  -23.96119 1.56196   1.000 77.44889  ? 334 GLU B OE1 1 
ATOM   2516 O  OE2 . GLU B 1 334 ? 10.84663  -23.35777 3.65444   1.000 68.24056  ? 334 GLU B OE2 1 
ATOM   2517 N  N   . TYR B 1 335 ? 12.83363  -18.45640 3.56744   1.000 31.20683  ? 335 TYR B N   1 
ATOM   2518 C  CA  . TYR B 1 335 ? 12.51042  -17.29633 4.38476   1.000 28.35996  ? 335 TYR B CA  1 
ATOM   2519 C  C   . TYR B 1 335 ? 13.00941  -16.04862 3.67533   1.000 26.42528  ? 335 TYR B C   1 
ATOM   2520 O  O   . TYR B 1 335 ? 13.92751  -16.11052 2.86320   1.000 27.72789  ? 335 TYR B O   1 
ATOM   2521 C  CB  . TYR B 1 335 ? 13.16855  -17.36535 5.76729   1.000 30.36545  ? 335 TYR B CB  1 
ATOM   2522 C  CG  . TYR B 1 335 ? 12.93173  -18.63474 6.54142   1.000 32.99457  ? 335 TYR B CG  1 
ATOM   2523 C  CD1 . TYR B 1 335 ? 13.80316  -19.71101 6.42628   1.000 35.10201  ? 335 TYR B CD1 1 
ATOM   2524 C  CD2 . TYR B 1 335 ? 11.86175  -18.73909 7.42876   1.000 31.50916  ? 335 TYR B CD2 1 
ATOM   2525 C  CE1 . TYR B 1 335 ? 13.60382  -20.87478 7.15156   1.000 34.12575  ? 335 TYR B CE1 1 
ATOM   2526 C  CE2 . TYR B 1 335 ? 11.64968  -19.91299 8.17842   1.000 29.49899  ? 335 TYR B CE2 1 
ATOM   2527 C  CZ  . TYR B 1 335 ? 12.52931  -20.97167 8.02212   1.000 39.15383  ? 335 TYR B CZ  1 
ATOM   2528 O  OH  . TYR B 1 335 ? 12.33553  -22.12899 8.73892   1.000 40.21086  ? 335 TYR B OH  1 
ATOM   2529 N  N   . SER B 1 336 ? 12.42593  -14.89109 4.00345   1.000 25.11670  ? 336 SER B N   1 
ATOM   2530 C  CA  . SER B 1 336 ? 12.95066  -13.65682 3.44362   1.000 24.86024  ? 336 SER B CA  1 
ATOM   2531 C  C   . SER B 1 336 ? 12.63316  -12.47883 4.35470   1.000 27.26104  ? 336 SER B C   1 
ATOM   2532 O  O   . SER B 1 336 ? 11.66369  -12.50028 5.11018   1.000 25.49557  ? 336 SER B O   1 
ATOM   2533 C  CB  . SER B 1 336 ? 12.36731  -13.38087 2.06488   1.000 24.07804  ? 336 SER B CB  1 
ATOM   2534 O  OG  . SER B 1 336 ? 10.94757  -13.30712 2.15649   1.000 25.60611  ? 336 SER B OG  1 
ATOM   2535 N  N   . ILE B 1 337 ? 13.48337  -11.46122 4.27137   1.000 24.17445  ? 337 ILE B N   1 
ATOM   2536 C  CA  . ILE B 1 337 ? 13.23200  -10.14125 4.82508   1.000 21.03166  ? 337 ILE B CA  1 
ATOM   2537 C  C   . ILE B 1 337 ? 13.47654  -9.15033  3.70636   1.000 28.09575  ? 337 ILE B C   1 
ATOM   2538 O  O   . ILE B 1 337 ? 14.58007  -9.10911  3.15630   1.000 28.15534  ? 337 ILE B O   1 
ATOM   2539 C  CB  . ILE B 1 337 ? 14.17026  -9.83703  6.01158   1.000 25.55316  ? 337 ILE B CB  1 
ATOM   2540 C  CG1 . ILE B 1 337 ? 14.04276  -10.89126 7.08767   1.000 23.77646  ? 337 ILE B CG1 1 
ATOM   2541 C  CG2 . ILE B 1 337 ? 13.88461  -8.46811  6.60690   1.000 23.71639  ? 337 ILE B CG2 1 
ATOM   2542 C  CD1 . ILE B 1 337 ? 15.10058  -10.77682 8.21160   1.000 29.79407  ? 337 ILE B CD1 1 
ATOM   2543 N  N   . THR B 1 338 ? 12.46643  -8.34677  3.37457   1.000 22.67082  ? 338 THR B N   1 
ATOM   2544 C  CA  A THR B 1 338 ? 12.63054  -7.36799  2.31138   0.401 23.27278  ? 338 THR B CA  1 
ATOM   2545 C  CA  B THR B 1 338 ? 12.50591  -7.38013  2.27817   0.599 25.17300  ? 338 THR B CA  1 
ATOM   2546 C  C   . THR B 1 338 ? 12.38957  -5.97545  2.85720   1.000 28.89976  ? 338 THR B C   1 
ATOM   2547 O  O   . THR B 1 338 ? 11.47440  -5.73464  3.65173   1.000 25.64430  ? 338 THR B O   1 
ATOM   2548 C  CB  A THR B 1 338 ? 11.72001  -7.62507  1.10358   0.401 32.33589  ? 338 THR B CB  1 
ATOM   2549 C  CB  B THR B 1 338 ? 11.33512  -7.62069  1.31453   0.599 20.45407  ? 338 THR B CB  1 
ATOM   2550 O  OG1 A THR B 1 338 ? 10.34959  -7.39112  1.44182   0.401 25.60081  ? 338 THR B OG1 1 
ATOM   2551 O  OG1 B THR B 1 338 ? 11.41855  -8.93854  0.74864   0.599 32.85442  ? 338 THR B OG1 1 
ATOM   2552 C  CG2 A THR B 1 338 ? 11.89795  -9.03438  0.63668   0.401 35.44892  ? 338 THR B CG2 1 
ATOM   2553 C  CG2 B THR B 1 338 ? 11.33339  -6.58675  0.22213   0.599 23.83848  ? 338 THR B CG2 1 
ATOM   2554 N  N   . PHE B 1 339 ? 13.28973  -5.06809  2.46879   1.000 23.34962  ? 339 PHE B N   1 
ATOM   2555 C  CA  . PHE B 1 339 ? 13.23009  -3.66997  2.88593   1.000 22.83900  ? 339 PHE B CA  1 
ATOM   2556 C  C   . PHE B 1 339 ? 12.84624  -2.84663  1.67113   1.000 27.62546  ? 339 PHE B C   1 
ATOM   2557 O  O   . PHE B 1 339 ? 13.57936  -2.83325  0.67652   1.000 28.05026  ? 339 PHE B O   1 
ATOM   2558 C  CB  . PHE B 1 339 ? 14.57273  -3.18612  3.43216   1.000 22.76429  ? 339 PHE B CB  1 
ATOM   2559 C  CG  . PHE B 1 339 ? 15.03398  -3.91944  4.63438   1.000 22.82716  ? 339 PHE B CG  1 
ATOM   2560 C  CD1 . PHE B 1 339 ? 14.43923  -3.69920  5.87531   1.000 22.85649  ? 339 PHE B CD1 1 
ATOM   2561 C  CD2 . PHE B 1 339 ? 16.05840  -4.84845  4.53791   1.000 28.76376  ? 339 PHE B CD2 1 
ATOM   2562 C  CE1 . PHE B 1 339 ? 14.87330  -4.38345  6.98385   1.000 21.64275  ? 339 PHE B CE1 1 
ATOM   2563 C  CE2 . PHE B 1 339 ? 16.47584  -5.55738  5.66270   1.000 24.91612  ? 339 PHE B CE2 1 
ATOM   2564 C  CZ  . PHE B 1 339 ? 15.88425  -5.30921  6.89792   1.000 23.52248  ? 339 PHE B CZ  1 
ATOM   2565 N  N   . ASN B 1 340 ? 11.71423  -2.16107  1.73561   1.000 23.23200  ? 340 ASN B N   1 
ATOM   2566 C  CA  . ASN B 1 340 ? 11.37299  -1.20584  0.67461   1.000 21.36243  ? 340 ASN B CA  1 
ATOM   2567 C  C   . ASN B 1 340 ? 11.54355  0.19900   1.23293   1.000 26.92376  ? 340 ASN B C   1 
ATOM   2568 O  O   . ASN B 1 340 ? 10.94756  0.52997   2.26783   1.000 24.72688  ? 340 ASN B O   1 
ATOM   2569 C  CB  . ASN B 1 340 ? 9.94606   -1.40770  0.15748   1.000 25.48000  ? 340 ASN B CB  1 
ATOM   2570 C  CG  . ASN B 1 340 ? 9.56806   -0.36175  -0.91211  1.000 34.04207  ? 340 ASN B CG  1 
ATOM   2571 O  OD1 . ASN B 1 340 ? 8.97185   0.66541   -0.59292  1.000 31.04106  ? 340 ASN B OD1 1 
ATOM   2572 N  ND2 . ASN B 1 340 ? 9.98424   -0.58775  -2.16711  1.000 28.01051  ? 340 ASN B ND2 1 
ATOM   2573 N  N   . PHE B 1 341 ? 12.39046  1.00257   0.58001   1.000 21.36095  ? 341 PHE B N   1 
ATOM   2574 C  CA  . PHE B 1 341 ? 12.60627  2.39525   0.93683   1.000 20.65842  ? 341 PHE B CA  1 
ATOM   2575 C  C   . PHE B 1 341 ? 11.81318  3.24586   -0.04012  1.000 26.14300  ? 341 PHE B C   1 
ATOM   2576 O  O   . PHE B 1 341 ? 11.87487  3.01795   -1.24622  1.000 27.14619  ? 341 PHE B O   1 
ATOM   2577 C  CB  . PHE B 1 341 ? 14.09219  2.76782   0.87523   1.000 22.30514  ? 341 PHE B CB  1 
ATOM   2578 C  CG  . PHE B 1 341 ? 14.92956  2.03140   1.89843   1.000 25.70157  ? 341 PHE B CG  1 
ATOM   2579 C  CD1 . PHE B 1 341 ? 15.35542  0.72487   1.67021   1.000 26.83573  ? 341 PHE B CD1 1 
ATOM   2580 C  CD2 . PHE B 1 341 ? 15.24008  2.63275   3.10968   1.000 28.62851  ? 341 PHE B CD2 1 
ATOM   2581 C  CE1 . PHE B 1 341 ? 16.10756  0.03696   2.65844   1.000 26.51177  ? 341 PHE B CE1 1 
ATOM   2582 C  CE2 . PHE B 1 341 ? 15.98116  1.95499   4.09500   1.000 26.24087  ? 341 PHE B CE2 1 
ATOM   2583 C  CZ  . PHE B 1 341 ? 16.41798  0.67732   3.86951   1.000 22.89382  ? 341 PHE B CZ  1 
ATOM   2584 N  N   . SER B 1 342 ? 11.06695  4.21793   0.46551   1.000 21.40431  ? 342 SER B N   1 
ATOM   2585 C  CA  . SER B 1 342 ? 10.24728  5.01731   -0.44404  1.000 23.14953  ? 342 SER B CA  1 
ATOM   2586 C  C   . SER B 1 342 ? 10.02009  6.37410   0.18640   1.000 27.93115  ? 342 SER B C   1 
ATOM   2587 O  O   . SER B 1 342 ? 10.19866  6.54785   1.38726   1.000 26.47517  ? 342 SER B O   1 
ATOM   2588 C  CB  . SER B 1 342 ? 8.89212   4.35553   -0.75912  1.000 24.78936  ? 342 SER B CB  1 
ATOM   2589 O  OG  . SER B 1 342 ? 8.06262   4.42601   0.37806   1.000 27.59426  ? 342 SER B OG  1 
ATOM   2590 N  N   . TRP B 1 343 ? 9.67086   7.35417   -0.64554  1.000 23.29941  ? 343 TRP B N   1 
ATOM   2591 C  CA  . TRP B 1 343 ? 9.44374   8.68394   -0.10504  1.000 23.11887  ? 343 TRP B CA  1 
ATOM   2592 C  C   . TRP B 1 343 ? 8.45566   9.43130   -0.97500  1.000 28.66319  ? 343 TRP B C   1 
ATOM   2593 O  O   . TRP B 1 343 ? 8.29734   9.14715   -2.16658  1.000 27.87166  ? 343 TRP B O   1 
ATOM   2594 C  CB  . TRP B 1 343 ? 10.75671  9.46507   0.04495   1.000 25.33024  ? 343 TRP B CB  1 
ATOM   2595 C  CG  . TRP B 1 343 ? 11.51826  9.52503   -1.23610  1.000 26.29947  ? 343 TRP B CG  1 
ATOM   2596 C  CD1 . TRP B 1 343 ? 11.51815  10.55370  -2.13480  1.000 32.43187  ? 343 TRP B CD1 1 
ATOM   2597 C  CD2 . TRP B 1 343 ? 12.39468  8.52542   -1.76329  1.000 25.83859  ? 343 TRP B CD2 1 
ATOM   2598 N  NE1 . TRP B 1 343 ? 12.33403  10.25076  -3.19278  1.000 32.37433  ? 343 TRP B NE1 1 
ATOM   2599 C  CE2 . TRP B 1 343 ? 12.87557  9.00421   -2.99333  1.000 33.95808  ? 343 TRP B CE2 1 
ATOM   2600 C  CE3 . TRP B 1 343 ? 12.80945  7.26018   -1.31995  1.000 23.54976  ? 343 TRP B CE3 1 
ATOM   2601 C  CZ2 . TRP B 1 343 ? 13.73569  8.26684   -3.78900  1.000 29.39165  ? 343 TRP B CZ2 1 
ATOM   2602 C  CZ3 . TRP B 1 343 ? 13.66918  6.52232   -2.11067  1.000 26.82972  ? 343 TRP B CZ3 1 
ATOM   2603 C  CH2 . TRP B 1 343 ? 14.13205  7.03320   -3.33716  1.000 35.02531  ? 343 TRP B CH2 1 
ATOM   2604 N  N   . SER B 1 344 ? 7.78543   10.39999  -0.35434  1.000 27.97529  ? 344 SER B N   1 
ATOM   2605 C  CA  . SER B 1 344 ? 6.74809   11.15685  -1.04726  1.000 27.50933  ? 344 SER B CA  1 
ATOM   2606 C  C   . SER B 1 344 ? 7.04029   12.64972  -1.15287  1.000 30.77821  ? 344 SER B C   1 
ATOM   2607 O  O   . SER B 1 344 ? 6.44551   13.32067  -2.00859  1.000 35.32063  ? 344 SER B O   1 
ATOM   2608 C  CB  . SER B 1 344 ? 5.39942   10.94672  -0.34448  1.000 31.63744  ? 344 SER B CB  1 
ATOM   2609 O  OG  . SER B 1 344 ? 5.53018   11.29401  1.02482   1.000 31.22128  ? 344 SER B OG  1 
ATOM   2610 N  N   . LYS B 1 345 ? 7.95261   13.18425  -0.34787  1.000 31.46233  ? 345 LYS B N   1 
ATOM   2611 C  CA  . LYS B 1 345 ? 8.37578   14.56008  -0.53018  1.000 34.58124  ? 345 LYS B CA  1 
ATOM   2612 C  C   . LYS B 1 345 ? 9.22959   14.69619  -1.78684  1.000 41.27524  ? 345 LYS B C   1 
ATOM   2613 O  O   . LYS B 1 345 ? 9.77192   13.72035  -2.31486  1.000 34.48248  ? 345 LYS B O   1 
ATOM   2614 C  CB  . LYS B 1 345 ? 9.15824   15.04136  0.67940   1.000 30.52133  ? 345 LYS B CB  1 
ATOM   2615 C  CG  . LYS B 1 345 ? 8.32360   15.23755  1.88718   1.000 40.26978  ? 345 LYS B CG  1 
ATOM   2616 C  CD  . LYS B 1 345 ? 9.11889   16.09210  2.84497   1.000 49.21691  ? 345 LYS B CD  1 
ATOM   2617 C  CE  . LYS B 1 345 ? 8.30106   16.54113  4.01589   1.000 44.06915  ? 345 LYS B CE  1 
ATOM   2618 N  NZ  . LYS B 1 345 ? 9.13117   17.45286  4.86235   1.000 40.22151  ? 345 LYS B NZ  1 
ATOM   2619 N  N   . THR B 1 346 ? 9.31649   15.92893  -2.28731  1.000 36.75182  ? 346 THR B N   1 
ATOM   2620 C  CA  . THR B 1 346 ? 10.17132  16.24814  -3.42600  1.000 32.47213  ? 346 THR B CA  1 
ATOM   2621 C  C   . THR B 1 346 ? 11.54580  16.62944  -2.89320  1.000 46.47960  ? 346 THR B C   1 
ATOM   2622 O  O   . THR B 1 346 ? 11.72157  17.72391  -2.35694  1.000 61.02994  ? 346 THR B O   1 
ATOM   2623 C  CB  . THR B 1 346 ? 9.57432   17.38367  -4.25432  1.000 39.11838  ? 346 THR B CB  1 
ATOM   2624 O  OG1 . THR B 1 346 ? 8.26167   17.01358  -4.66083  1.000 42.85665  ? 346 THR B OG1 1 
ATOM   2625 C  CG2 . THR B 1 346 ? 10.39487  17.62375  -5.48592  1.000 42.13863  ? 346 THR B CG2 1 
ATOM   2626 N  N   . TYR B 1 347 ? 12.51566  15.73090  -3.01596  1.000 33.30372  ? 347 TYR B N   1 
ATOM   2627 C  CA  . TYR B 1 347 ? 13.86032  16.02180  -2.53391  1.000 30.00790  ? 347 TYR B CA  1 
ATOM   2628 C  C   . TYR B 1 347 ? 14.72572  16.48960  -3.69552  1.000 34.08981  ? 347 TYR B C   1 
ATOM   2629 O  O   . TYR B 1 347 ? 14.60955  15.98131  -4.81337  1.000 37.91650  ? 347 TYR B O   1 
ATOM   2630 C  CB  . TYR B 1 347 ? 14.47618  14.81243  -1.85064  1.000 29.23166  ? 347 TYR B CB  1 
ATOM   2631 C  CG  . TYR B 1 347 ? 13.74432  14.48228  -0.56096  1.000 30.07275  ? 347 TYR B CG  1 
ATOM   2632 C  CD1 . TYR B 1 347 ? 13.46715  15.48369  0.37330   1.000 32.05472  ? 347 TYR B CD1 1 
ATOM   2633 C  CD2 . TYR B 1 347 ? 13.27032  13.19616  -0.31281  1.000 33.81628  ? 347 TYR B CD2 1 
ATOM   2634 C  CE1 . TYR B 1 347 ? 12.77616  15.20151  1.56095   1.000 28.68370  ? 347 TYR B CE1 1 
ATOM   2635 C  CE2 . TYR B 1 347 ? 12.59336  12.89819  0.85650   1.000 27.51467  ? 347 TYR B CE2 1 
ATOM   2636 C  CZ  . TYR B 1 347 ? 12.34931  13.90956  1.79172   1.000 30.11211  ? 347 TYR B CZ  1 
ATOM   2637 O  OH  . TYR B 1 347 ? 11.66024  13.61904  2.94147   1.000 28.37125  ? 347 TYR B OH  1 
ATOM   2638 N  N   . GLU B 1 348 ? 15.58652  17.46465  -3.42010  1.000 36.06370  ? 348 GLU B N   1 
ATOM   2639 C  CA  . GLU B 1 348 ? 16.39267  18.13589  -4.44010  1.000 37.35122  ? 348 GLU B CA  1 
ATOM   2640 C  C   . GLU B 1 348 ? 17.86072  17.94582  -4.07636  1.000 33.74279  ? 348 GLU B C   1 
ATOM   2641 O  O   . GLU B 1 348 ? 18.40801  18.68734  -3.25155  1.000 36.25284  ? 348 GLU B O   1 
ATOM   2642 C  CB  . GLU B 1 348 ? 16.02100  19.61069  -4.53685  1.000 31.89666  ? 348 GLU B CB  1 
ATOM   2643 C  CG  . GLU B 1 348 ? 16.62306  20.31443  -5.72592  1.000 41.24832  ? 348 GLU B CG  1 
ATOM   2644 C  CD  . GLU B 1 348 ? 16.21213  21.77296  -5.82055  1.000 45.15611  ? 348 GLU B CD  1 
ATOM   2645 O  OE1 . GLU B 1 348 ? 15.53042  22.27558  -4.90996  1.000 58.68569  ? 348 GLU B OE1 1 
ATOM   2646 O  OE2 . GLU B 1 348 ? 16.58113  22.41302  -6.81314  1.000 58.06338  ? 348 GLU B OE2 1 
ATOM   2647 N  N   . ASN B 1 349 ? 18.47727  16.92311  -4.66742  1.000 35.96173  ? 349 ASN B N   1 
ATOM   2648 C  CA  . ASN B 1 349 ? 19.89338  16.61230  -4.49486  1.000 31.29353  ? 349 ASN B CA  1 
ATOM   2649 C  C   . ASN B 1 349 ? 20.21341  16.24518  -3.04641  1.000 35.45995  ? 349 ASN B C   1 
ATOM   2650 O  O   . ASN B 1 349 ? 21.09557  16.82055  -2.40600  1.000 39.01644  ? 349 ASN B O   1 
ATOM   2651 C  CB  . ASN B 1 349 ? 20.76520  17.76980  -4.97609  1.000 48.41067  ? 349 ASN B CB  1 
ATOM   2652 C  CG  . ASN B 1 349 ? 20.54829  18.05865  -6.43206  1.000 62.88277  ? 349 ASN B CG  1 
ATOM   2653 O  OD1 . ASN B 1 349 ? 20.37366  17.13567  -7.23198  1.000 51.07256  ? 349 ASN B OD1 1 
ATOM   2654 N  ND2 . ASN B 1 349 ? 20.50297  19.33904  -6.78449  1.000 60.15018  ? 349 ASN B ND2 1 
ATOM   2655 N  N   . VAL B 1 350 ? 19.49734  15.24145  -2.55643  1.000 29.01948  ? 350 VAL B N   1 
ATOM   2656 C  CA  . VAL B 1 350 ? 19.63422  14.76275  -1.18006  1.000 28.34047  ? 350 VAL B CA  1 
ATOM   2657 C  C   . VAL B 1 350 ? 20.36224  13.42807  -1.23528  1.000 35.37365  ? 350 VAL B C   1 
ATOM   2658 O  O   . VAL B 1 350 ? 19.93663  12.50289  -1.93501  1.000 29.30858  ? 350 VAL B O   1 
ATOM   2659 C  CB  . VAL B 1 350 ? 18.26855  14.63151  -0.48199  1.000 28.33394  ? 350 VAL B CB  1 
ATOM   2660 C  CG1 . VAL B 1 350 ? 18.41494  13.96485  0.92973   1.000 26.96316  ? 350 VAL B CG1 1 
ATOM   2661 C  CG2 . VAL B 1 350 ? 17.58239  15.98798  -0.33872  1.000 27.12285  ? 350 VAL B CG2 1 
ATOM   2662 N  N   . GLU B 1 351 ? 21.45256  13.31391  -0.49484  1.000 30.70643  ? 351 GLU B N   1 
ATOM   2663 C  CA  . GLU B 1 351 ? 22.18074  12.05692  -0.47909  1.000 27.86944  ? 351 GLU B CA  1 
ATOM   2664 C  C   . GLU B 1 351 ? 21.39942  11.04971  0.36249   1.000 30.01715  ? 351 GLU B C   1 
ATOM   2665 O  O   . GLU B 1 351 ? 20.86576  11.39635  1.41501   1.000 29.57289  ? 351 GLU B O   1 
ATOM   2666 C  CB  . GLU B 1 351 ? 23.58393  12.30261  0.08165   1.000 31.82532  ? 351 GLU B CB  1 
ATOM   2667 C  CG  . GLU B 1 351 ? 24.43912  11.11634  0.42519   1.000 46.33509  ? 351 GLU B CG  1 
ATOM   2668 C  CD  . GLU B 1 351 ? 25.58439  11.53938  1.34163   1.000 73.46751  ? 351 GLU B CD  1 
ATOM   2669 O  OE1 . GLU B 1 351 ? 25.63368  12.73559  1.70451   1.000 65.01838  ? 351 GLU B OE1 1 
ATOM   2670 O  OE2 . GLU B 1 351 ? 26.42066  10.69223  1.71494   1.000 93.25148  ? 351 GLU B OE2 1 
ATOM   2671 N  N   . PHE B 1 352 ? 21.28898  9.80934   -0.12218  1.000 26.22419  ? 352 PHE B N   1 
ATOM   2672 C  CA  . PHE B 1 352 ? 20.42293  8.82997   0.54456   1.000 26.91967  ? 352 PHE B CA  1 
ATOM   2673 C  C   . PHE B 1 352 ? 21.23666  8.10121   1.61177   1.000 27.02248  ? 352 PHE B C   1 
ATOM   2674 O  O   . PHE B 1 352 ? 21.80749  7.04153   1.38057   1.000 26.35434  ? 352 PHE B O   1 
ATOM   2675 C  CB  . PHE B 1 352 ? 19.79121  7.85934   -0.44955  1.000 24.38394  ? 352 PHE B CB  1 
ATOM   2676 C  CG  . PHE B 1 352 ? 18.57166  7.16396   0.11144   1.000 26.57531  ? 352 PHE B CG  1 
ATOM   2677 C  CD1 . PHE B 1 352 ? 18.71123  6.16522   1.07501   1.000 27.12922  ? 352 PHE B CD1 1 
ATOM   2678 C  CD2 . PHE B 1 352 ? 17.28354  7.55172   -0.26547  1.000 24.84338  ? 352 PHE B CD2 1 
ATOM   2679 C  CE1 . PHE B 1 352 ? 17.60879  5.54788   1.63925   1.000 25.22264  ? 352 PHE B CE1 1 
ATOM   2680 C  CE2 . PHE B 1 352 ? 16.14774  6.94105   0.31055   1.000 31.17289  ? 352 PHE B CE2 1 
ATOM   2681 C  CZ  . PHE B 1 352 ? 16.31506  5.93106   1.26011   1.000 29.64548  ? 352 PHE B CZ  1 
ATOM   2682 N  N   . GLU B 1 353 ? 21.27436  8.67178   2.81477   1.000 25.03041  ? 353 GLU B N   1 
ATOM   2683 C  CA  . GLU B 1 353 ? 21.89793  8.01097   3.95025   1.000 21.13171  ? 353 GLU B CA  1 
ATOM   2684 C  C   . GLU B 1 353 ? 20.99351  8.27128   5.14949   1.000 21.28526  ? 353 GLU B C   1 
ATOM   2685 O  O   . GLU B 1 353 ? 20.55702  9.40734   5.34890   1.000 27.63188  ? 353 GLU B O   1 
ATOM   2686 C  CB  . GLU B 1 353 ? 23.32536  8.52046   4.14189   1.000 30.76289  ? 353 GLU B CB  1 
ATOM   2687 C  CG  . GLU B 1 353 ? 23.45393  10.03212  4.25617   1.000 34.79895  ? 353 GLU B CG  1 
ATOM   2688 C  CD  . GLU B 1 353 ? 23.78191  10.43936  5.69029   1.000 50.95920  ? 353 GLU B CD  1 
ATOM   2689 O  OE1 . GLU B 1 353 ? 24.02996  9.51921   6.49678   1.000 46.60458  ? 353 GLU B OE1 1 
ATOM   2690 O  OE2 . GLU B 1 353 ? 23.80275  11.65237  6.00822   1.000 37.86007  ? 353 GLU B OE2 1 
ATOM   2691 N  N   . THR B 1 354 ? 20.63289  7.21821   5.86974   1.000 23.95991  ? 354 THR B N   1 
ATOM   2692 C  CA  . THR B 1 354 ? 19.48356  7.29112   6.77001   1.000 24.92613  ? 354 THR B CA  1 
ATOM   2693 C  C   . THR B 1 354 ? 19.89482  7.26707   8.22725   1.000 23.90804  ? 354 THR B C   1 
ATOM   2694 O  O   . THR B 1 354 ? 20.96760  6.77005   8.60002   1.000 22.75744  ? 354 THR B O   1 
ATOM   2695 C  CB  . THR B 1 354 ? 18.52263  6.11738   6.57312   1.000 20.26530  ? 354 THR B CB  1 
ATOM   2696 O  OG1 . THR B 1 354 ? 19.09412  4.93768   7.15857   1.000 22.40035  ? 354 THR B OG1 1 
ATOM   2697 C  CG2 . THR B 1 354 ? 18.28216  5.85790   5.04743   1.000 24.87632  ? 354 THR B CG2 1 
ATOM   2698 N  N   . THR B 1 355 ? 18.96312  7.75536   9.04844   1.000 19.15523  ? 355 THR B N   1 
ATOM   2699 C  CA  . THR B 1 355 ? 18.99742  7.48836   10.48965  1.000 18.07742  ? 355 THR B CA  1 
ATOM   2700 C  C   . THR B 1 355 ? 18.69242  6.01107   10.72332  1.000 19.91787  ? 355 THR B C   1 
ATOM   2701 O  O   . THR B 1 355 ? 18.40925  5.25649   9.79174   1.000 21.82280  ? 355 THR B O   1 
ATOM   2702 C  CB  . THR B 1 355 ? 18.01275  8.40427   11.22261  1.000 20.60129  ? 355 THR B CB  1 
ATOM   2703 O  OG1 . THR B 1 355 ? 16.67436  8.19818   10.71964  1.000 20.72017  ? 355 THR B OG1 1 
ATOM   2704 C  CG2 . THR B 1 355 ? 18.41610  9.86763   11.01131  1.000 20.14227  ? 355 THR B CG2 1 
ATOM   2705 N  N   . SER B 1 356 ? 18.74621  5.58622   11.99218  1.000 18.43141  ? 356 SER B N   1 
ATOM   2706 C  CA  . SER B 1 356 ? 18.57792  4.18514   12.34345  1.000 17.03121  ? 356 SER B CA  1 
ATOM   2707 C  C   . SER B 1 356 ? 17.15682  3.88640   12.83427  1.000 20.43255  ? 356 SER B C   1 
ATOM   2708 O  O   . SER B 1 356 ? 16.51845  4.71223   13.48827  1.000 23.72458  ? 356 SER B O   1 
ATOM   2709 C  CB  . SER B 1 356 ? 19.58706  3.77936   13.43320  1.000 25.99678  ? 356 SER B CB  1 
ATOM   2710 O  OG  . SER B 1 356 ? 20.92687  3.80777   12.93502  1.000 26.73450  ? 356 SER B OG  1 
ATOM   2711 N  N   . PHE B 1 357 ? 16.69042  2.67325   12.56542  1.000 20.83591  ? 357 PHE B N   1 
ATOM   2712 C  CA  . PHE B 1 357 ? 15.34048  2.25905   12.97197  1.000 19.88673  ? 357 PHE B CA  1 
ATOM   2713 C  C   . PHE B 1 357 ? 15.40545  0.88270   13.62639  1.000 19.28916  ? 357 PHE B C   1 
ATOM   2714 O  O   . PHE B 1 357 ? 16.16143  0.00875   13.18374  1.000 21.98874  ? 357 PHE B O   1 
ATOM   2715 C  CB  . PHE B 1 357 ? 14.41766  2.24407   11.74379  1.000 21.99349  ? 357 PHE B CB  1 
ATOM   2716 C  CG  . PHE B 1 357 ? 13.02635  1.68820   12.01432  1.000 21.87900  ? 357 PHE B CG  1 
ATOM   2717 C  CD1 . PHE B 1 357 ? 12.15045  2.34978   12.87542  1.000 27.11572  ? 357 PHE B CD1 1 
ATOM   2718 C  CD2 . PHE B 1 357 ? 12.60103  0.53940   11.38163  1.000 21.20898  ? 357 PHE B CD2 1 
ATOM   2719 C  CE1 . PHE B 1 357 ? 10.85372  1.82482   13.12591  1.000 24.56518  ? 357 PHE B CE1 1 
ATOM   2720 C  CE2 . PHE B 1 357 ? 11.30296  0.02234   11.61544  1.000 21.03190  ? 357 PHE B CE2 1 
ATOM   2721 C  CZ  . PHE B 1 357 ? 10.44482  0.67334   12.48789  1.000 22.59112  ? 357 PHE B CZ  1 
ATOM   2722 N  N   . THR B 1 358 ? 14.64269  0.70105   14.72023  1.000 19.17493  ? 358 THR B N   1 
ATOM   2723 C  CA  . THR B 1 358 ? 14.57630  -0.55698  15.43162  1.000 18.38819  ? 358 THR B CA  1 
ATOM   2724 C  C   . THR B 1 358 ? 13.19351  -1.15044  15.28499  1.000 20.38981  ? 358 THR B C   1 
ATOM   2725 O  O   . THR B 1 358 ? 12.19043  -0.44359  15.42024  1.000 21.67828  ? 358 THR B O   1 
ATOM   2726 C  CB  . THR B 1 358 ? 14.85253  -0.34739  16.93603  1.000 22.51439  ? 358 THR B CB  1 
ATOM   2727 O  OG1 . THR B 1 358 ? 16.19678  0.13214   17.07506  1.000 27.57504  ? 358 THR B OG1 1 
ATOM   2728 C  CG2 . THR B 1 358 ? 14.67425  -1.65381  17.75408  1.000 28.13970  ? 358 THR B CG2 1 
ATOM   2729 N  N   . PHE B 1 359 ? 13.14847  -2.46013  15.09975  1.000 19.80550  ? 359 PHE B N   1 
ATOM   2730 C  CA  . PHE B 1 359 ? 11.87229  -3.17177  15.08572  1.000 21.57712  ? 359 PHE B CA  1 
ATOM   2731 C  C   . PHE B 1 359 ? 12.14212  -4.55315  15.67287  1.000 24.54204  ? 359 PHE B C   1 
ATOM   2732 O  O   . PHE B 1 359 ? 13.26292  -4.85956  16.07769  1.000 22.61307  ? 359 PHE B O   1 
ATOM   2733 C  CB  . PHE B 1 359 ? 11.26707  -3.21669  13.66123  1.000 20.40003  ? 359 PHE B CB  1 
ATOM   2734 C  CG  . PHE B 1 359 ? 12.14252  -3.88208  12.63792  1.000 24.46414  ? 359 PHE B CG  1 
ATOM   2735 C  CD1 . PHE B 1 359 ? 13.17470  -3.17502  12.01547  1.000 24.00644  ? 359 PHE B CD1 1 
ATOM   2736 C  CD2 . PHE B 1 359 ? 11.92226  -5.20883  12.27143  1.000 23.30905  ? 359 PHE B CD2 1 
ATOM   2737 C  CE1 . PHE B 1 359 ? 13.98713  -3.78573  11.02081  1.000 24.38309  ? 359 PHE B CE1 1 
ATOM   2738 C  CE2 . PHE B 1 359 ? 12.71956  -5.83818  11.32282  1.000 21.06187  ? 359 PHE B CE2 1 
ATOM   2739 C  CZ  . PHE B 1 359 ? 13.76632  -5.12780  10.68039  1.000 25.91273  ? 359 PHE B CZ  1 
ATOM   2740 N  N   . SER B 1 360 ? 11.11524  -5.39869  15.71091  1.000 21.88264  ? 360 SER B N   1 
ATOM   2741 C  CA  . SER B 1 360 ? 11.30377  -6.79380  16.10830  1.000 19.46087  ? 360 SER B CA  1 
ATOM   2742 C  C   . SER B 1 360 ? 10.36835  -7.64972  15.27683  1.000 20.65424  ? 360 SER B C   1 
ATOM   2743 O  O   . SER B 1 360 ? 9.46635   -7.13918  14.59914  1.000 20.49484  ? 360 SER B O   1 
ATOM   2744 C  CB  . SER B 1 360 ? 11.04217  -7.01516  17.62219  1.000 25.61814  ? 360 SER B CB  1 
ATOM   2745 O  OG  . SER B 1 360 ? 9.63861   -7.10838  17.87814  1.000 23.12446  ? 360 SER B OG  1 
ATOM   2746 N  N   . TYR B 1 361 ? 10.64496  -8.94907  15.26016  1.000 21.20030  ? 361 TYR B N   1 
ATOM   2747 C  CA  . TYR B 1 361 ? 9.71433   -9.87964  14.63628  1.000 18.46348  ? 361 TYR B CA  1 
ATOM   2748 C  C   . TYR B 1 361 ? 9.76630   -11.20654 15.36196  1.000 22.28003  ? 361 TYR B C   1 
ATOM   2749 O  O   . TYR B 1 361 ? 10.70458  -11.50140 16.11691  1.000 23.20242  ? 361 TYR B O   1 
ATOM   2750 C  CB  . TYR B 1 361 ? 9.99176   -10.08652 13.13469  1.000 19.24931  ? 361 TYR B CB  1 
ATOM   2751 C  CG  . TYR B 1 361 ? 11.39448  -10.55809 12.78323  1.000 24.46730  ? 361 TYR B CG  1 
ATOM   2752 C  CD1 . TYR B 1 361 ? 12.40510  -9.63745  12.50482  1.000 23.65932  ? 361 TYR B CD1 1 
ATOM   2753 C  CD2 . TYR B 1 361 ? 11.69414  -11.91480 12.68009  1.000 26.58637  ? 361 TYR B CD2 1 
ATOM   2754 C  CE1 . TYR B 1 361 ? 13.69443  -10.05762 12.12972  1.000 25.20862  ? 361 TYR B CE1 1 
ATOM   2755 C  CE2 . TYR B 1 361 ? 12.97295  -12.34288 12.34656  1.000 24.61048  ? 361 TYR B CE2 1 
ATOM   2756 C  CZ  . TYR B 1 361 ? 13.96876  -11.41036 12.07090  1.000 27.92174  ? 361 TYR B CZ  1 
ATOM   2757 O  OH  . TYR B 1 361 ? 15.22386  -11.86808 11.73626  1.000 24.45081  ? 361 TYR B OH  1 
ATOM   2758 N  N   . ILE B 1 362 ? 8.74506   -12.02139 15.09398  1.000 22.58198  ? 362 ILE B N   1 
ATOM   2759 C  CA  . ILE B 1 362 ? 8.60552   -13.31580 15.74862  1.000 21.86940  ? 362 ILE B CA  1 
ATOM   2760 C  C   . ILE B 1 362 ? 9.53199   -14.32656 15.07400  1.000 24.34220  ? 362 ILE B C   1 
ATOM   2761 O  O   . ILE B 1 362 ? 9.54445   -14.44607 13.83797  1.000 26.68801  ? 362 ILE B O   1 
ATOM   2762 C  CB  . ILE B 1 362 ? 7.14038   -13.77965 15.69831  1.000 23.05374  ? 362 ILE B CB  1 
ATOM   2763 C  CG1 . ILE B 1 362 ? 6.24797   -12.76024 16.39997  1.000 25.80991  ? 362 ILE B CG1 1 
ATOM   2764 C  CG2 . ILE B 1 362 ? 6.98829   -15.16581 16.32681  1.000 29.47066  ? 362 ILE B CG2 1 
ATOM   2765 C  CD1 . ILE B 1 362 ? 4.75508   -12.96356 16.10510  1.000 27.24582  ? 362 ILE B CD1 1 
ATOM   2766 N  N   . ALA B 1 363 ? 10.31717  -15.06702 15.88737  1.000 27.04725  ? 363 ALA B N   1 
ATOM   2767 C  CA  . ALA B 1 363 ? 11.31809  -16.00282 15.37122  1.000 26.44465  ? 363 ALA B CA  1 
ATOM   2768 C  C   . ALA B 1 363 ? 10.71427  -17.37044 15.06055  1.000 27.09853  ? 363 ALA B C   1 
ATOM   2769 O  O   . ALA B 1 363 ? 9.79290   -17.83343 15.73569  1.000 29.84404  ? 363 ALA B O   1 
ATOM   2770 C  CB  . ALA B 1 363 ? 12.48219  -16.19402 16.35178  1.000 30.99973  ? 363 ALA B CB  1 
ATOM   2771 N  N   . GLN B 1 364 ? 11.27687  -18.01876 14.03413  1.000 29.36615  ? 364 GLN B N   1 
ATOM   2772 C  CA  . GLN B 1 364 ? 10.80472  -19.33187 13.59519  1.000 30.96375  ? 364 GLN B CA  1 
ATOM   2773 C  C   . GLN B 1 364 ? 10.96260  -20.38476 14.68816  1.000 39.50506  ? 364 GLN B C   1 
ATOM   2774 O  O   . GLN B 1 364 ? 10.10549  -21.26485 14.84626  1.000 35.50671  ? 364 GLN B O   1 
ATOM   2775 C  CB  . GLN B 1 364 ? 11.56397  -19.74835 12.33785  1.000 30.42187  ? 364 GLN B CB  1 
ATOM   2776 C  CG  . GLN B 1 364 ? 11.35568  -21.19301 11.91056  1.000 31.97706  ? 364 GLN B CG  1 
ATOM   2777 C  CD  . GLN B 1 364 ? 9.93502   -21.50920 11.44412  1.000 48.86773  ? 364 GLN B CD  1 
ATOM   2778 O  OE1 . GLN B 1 364 ? 9.11143   -20.62137 11.23159  1.000 39.97904  ? 364 GLN B OE1 1 
ATOM   2779 N  NE2 . GLN B 1 364 ? 9.65107   -22.79457 11.27342  1.000 56.98383  ? 364 GLN B NE2 1 
ATOM   2780 N  N   . GLU B 1 365 ? 12.05737  -20.32724 15.43217  1.000 37.51762  ? 365 GLU B N   1 
ATOM   2781 C  CA  . GLU B 1 365 ? 12.20177  -21.15654 16.62009  1.000 51.34227  ? 365 GLU B CA  1 
ATOM   2782 C  C   . GLU B 1 365 ? 13.08612  -20.46185 17.64439  1.000 55.11194  ? 365 GLU B C   1 
ATOM   2783 O  O   . GLU B 1 365 ? 13.12814  -20.85586 18.81024  1.000 72.63014  ? 365 GLU B O   1 
ATOM   2784 C  CB  . GLU B 1 365 ? 12.76738  -22.53325 16.26176  1.000 50.26024  ? 365 GLU B CB  1 
ATOM   2785 C  CG  . GLU B 1 365 ? 14.10814  -22.50668 15.56581  1.000 56.68799  ? 365 GLU B CG  1 
ATOM   2786 C  CD  . GLU B 1 365 ? 14.56915  -23.89677 15.15761  1.000 77.65407  ? 365 GLU B CD  1 
ATOM   2787 O  OE1 . GLU B 1 365 ? 13.72816  -24.67782 14.65907  1.000 76.44410  ? 365 GLU B OE1 1 
ATOM   2788 O  OE2 . GLU B 1 365 ? 15.76697  -24.21051 15.34260  1.000 73.07097  ? 365 GLU B OE2 1 
ATOM   2789 O  OXT . GLU B 1 365 ? 13.76908  -19.48640 17.33600  1.000 62.28495  ? 365 GLU B OXT 1 
ATOM   2790 N  N   . LYS C 1 180 ? 17.67629  -8.32883  44.37391  1.000 70.28379  ? 180 LYS C N   1 
ATOM   2791 C  CA  . LYS C 1 180 ? 18.43608  -8.96753  43.30794  1.000 76.12502  ? 180 LYS C CA  1 
ATOM   2792 C  C   . LYS C 1 180 ? 19.63835  -8.11155  42.89212  1.000 78.56573  ? 180 LYS C C   1 
ATOM   2793 O  O   . LYS C 1 180 ? 19.97091  -7.13328  43.56283  1.000 66.80307  ? 180 LYS C O   1 
ATOM   2794 C  CB  . LYS C 1 180 ? 17.53108  -9.25210  42.10493  1.000 74.46098  ? 180 LYS C CB  1 
ATOM   2795 C  CG  . LYS C 1 180 ? 17.22597  -8.06822  41.18866  1.000 58.28912  ? 180 LYS C CG  1 
ATOM   2796 C  CD  . LYS C 1 180 ? 16.62855  -8.57178  39.87678  1.000 66.38264  ? 180 LYS C CD  1 
ATOM   2797 C  CE  . LYS C 1 180 ? 17.18289  -9.96237  39.48714  1.000 55.23240  ? 180 LYS C CE  1 
ATOM   2798 N  NZ  . LYS C 1 180 ? 18.66879  -9.98799  39.21550  1.000 41.50266  ? 180 LYS C NZ  1 
ATOM   2799 N  N   . ASN C 1 181 ? 20.29273  -8.48846  41.77872  1.000 62.98021  ? 181 ASN C N   1 
ATOM   2800 C  CA  . ASN C 1 181 ? 21.53869  -7.85118  41.32947  1.000 60.26032  ? 181 ASN C CA  1 
ATOM   2801 C  C   . ASN C 1 181 ? 21.61749  -8.04465  39.80996  1.000 59.53152  ? 181 ASN C C   1 
ATOM   2802 O  O   . ASN C 1 181 ? 22.30276  -8.93605  39.30344  1.000 57.53109  ? 181 ASN C O   1 
ATOM   2803 C  CB  . ASN C 1 181 ? 22.76386  -8.43281  42.03523  1.000 67.34963  ? 181 ASN C CB  1 
ATOM   2804 C  CG  . ASN C 1 181 ? 23.95564  -7.49436  42.01053  1.000 74.09207  ? 181 ASN C CG  1 
ATOM   2805 O  OD1 . ASN C 1 181 ? 24.85466  -7.62440  41.18032  1.000 72.26542  ? 181 ASN C OD1 1 
ATOM   2806 N  ND2 . ASN C 1 181 ? 23.97099  -6.54453  42.93470  1.000 87.95154  ? 181 ASN C ND2 1 
ATOM   2807 N  N   . ASP C 1 182 ? 20.88677  -7.19446  39.08636  1.000 45.00502  ? 182 ASP C N   1 
ATOM   2808 C  CA  . ASP C 1 182 ? 20.71927  -7.30984  37.63572  1.000 53.62372  ? 182 ASP C CA  1 
ATOM   2809 C  C   . ASP C 1 182 ? 21.85693  -6.59938  36.90246  1.000 36.81095  ? 182 ASP C C   1 
ATOM   2810 O  O   . ASP C 1 182 ? 21.79683  -5.39000  36.65261  1.000 36.53056  ? 182 ASP C O   1 
ATOM   2811 C  CB  . ASP C 1 182 ? 19.35464  -6.76625  37.24943  1.000 38.49177  ? 182 ASP C CB  1 
ATOM   2812 C  CG  . ASP C 1 182 ? 19.06192  -6.90604  35.77712  1.000 54.74972  ? 182 ASP C CG  1 
ATOM   2813 O  OD1 . ASP C 1 182 ? 19.90067  -7.45927  35.00888  1.000 38.38028  ? 182 ASP C OD1 1 
ATOM   2814 O  OD2 . ASP C 1 182 ? 17.96321  -6.46102  35.39549  1.000 41.30818  ? 182 ASP C OD2 1 
ATOM   2815 N  N   . THR C 1 183 ? 22.86883  -7.37265  36.50424  1.000 34.11159  ? 183 THR C N   1 
ATOM   2816 C  CA  . THR C 1 183 ? 24.04475  -6.86227  35.80928  1.000 39.84292  ? 183 THR C CA  1 
ATOM   2817 C  C   . THR C 1 183 ? 23.79518  -6.53058  34.34764  1.000 44.27675  ? 183 THR C C   1 
ATOM   2818 O  O   . THR C 1 183 ? 24.70237  -5.98283  33.70551  1.000 37.51090  ? 183 THR C O   1 
ATOM   2819 C  CB  . THR C 1 183 ? 25.18402  -7.88727  35.90799  1.000 44.30753  ? 183 THR C CB  1 
ATOM   2820 O  OG1 . THR C 1 183 ? 24.89992  -9.00082  35.04714  1.000 43.68308  ? 183 THR C OG1 1 
ATOM   2821 C  CG2 . THR C 1 183 ? 25.31497  -8.37790  37.33888  1.000 44.35448  ? 183 THR C CG2 1 
ATOM   2822 N  N   . ARG C 1 184 ? 22.59985  -6.82105  33.81666  1.000 29.85528  ? 184 ARG C N   1 
ATOM   2823 C  CA  . ARG C 1 184 ? 22.24944  -6.56548  32.42831  1.000 28.46689  ? 184 ARG C CA  1 
ATOM   2824 C  C   . ARG C 1 184 ? 21.41277  -5.30715  32.24937  1.000 29.18810  ? 184 ARG C C   1 
ATOM   2825 O  O   . ARG C 1 184 ? 21.00968  -5.00373  31.12992  1.000 31.22754  ? 184 ARG C O   1 
ATOM   2826 C  CB  . ARG C 1 184 ? 21.50507  -7.76662  31.84134  1.000 37.48712  ? 184 ARG C CB  1 
ATOM   2827 C  CG  . ARG C 1 184 ? 22.25090  -9.09498  32.02989  1.000 58.26088  ? 184 ARG C CG  1 
ATOM   2828 C  CD  . ARG C 1 184 ? 22.00662  -10.07182 30.88198  1.000 57.14721  ? 184 ARG C CD  1 
ATOM   2829 N  NE  . ARG C 1 184 ? 22.61924  -9.59950  29.63932  1.000 79.26378  ? 184 ARG C NE  1 
ATOM   2830 C  CZ  . ARG C 1 184 ? 22.66633  -10.29770 28.50640  1.000 80.36900  ? 184 ARG C CZ  1 
ATOM   2831 N  NH1 . ARG C 1 184 ? 23.24670  -9.78705  27.42157  1.000 63.39316  ? 184 ARG C NH1 1 
ATOM   2832 N  NH2 . ARG C 1 184 ? 22.13630  -11.51153 28.45782  1.000 81.93352  ? 184 ARG C NH2 1 
ATOM   2833 N  N   . THR C 1 185 ? 21.18274  -4.54910  33.32118  1.000 27.99651  ? 185 THR C N   1 
ATOM   2834 C  CA  . THR C 1 185 ? 20.36952  -3.33703  33.25496  1.000 28.12320  ? 185 THR C CA  1 
ATOM   2835 C  C   . THR C 1 185 ? 21.08383  -2.18687  33.94457  1.000 30.74094  ? 185 THR C C   1 
ATOM   2836 O  O   . THR C 1 185 ? 21.40095  -2.26785  35.13596  1.000 29.83833  ? 185 THR C O   1 
ATOM   2837 C  CB  . THR C 1 185 ? 19.00307  -3.56485  33.89544  1.000 32.77011  ? 185 THR C CB  1 
ATOM   2838 O  OG1 . THR C 1 185 ? 18.28525  -4.50716  33.09945  1.000 41.48091  ? 185 THR C OG1 1 
ATOM   2839 C  CG2 . THR C 1 185 ? 18.19968  -2.24505  33.94778  1.000 33.97332  ? 185 THR C CG2 1 
ATOM   2840 N  N   . LEU C 1 186 ? 21.31855  -1.11441  33.19524  1.000 26.12325  ? 186 LEU C N   1 
ATOM   2841 C  CA  . LEU C 1 186 ? 21.81906  0.14980   33.72305  1.000 29.44215  ? 186 LEU C CA  1 
ATOM   2842 C  C   . LEU C 1 186 ? 20.65409  1.13267   33.65088  1.000 26.03001  ? 186 LEU C C   1 
ATOM   2843 O  O   . LEU C 1 186 ? 20.04032  1.27509   32.59430  1.000 26.37605  ? 186 LEU C O   1 
ATOM   2844 C  CB  . LEU C 1 186 ? 23.01222  0.61289   32.88128  1.000 29.90317  ? 186 LEU C CB  1 
ATOM   2845 C  CG  . LEU C 1 186 ? 23.92687  1.76112   33.23518  1.000 39.99991  ? 186 LEU C CG  1 
ATOM   2846 C  CD1 . LEU C 1 186 ? 24.49757  1.54907   34.62041  1.000 32.47669  ? 186 LEU C CD1 1 
ATOM   2847 C  CD2 . LEU C 1 186 ? 25.04869  1.76543   32.22212  1.000 34.82212  ? 186 LEU C CD2 1 
ATOM   2848 N  N   . TRP C 1 187 ? 20.28994  1.75497   34.77299  1.000 24.36491  ? 187 TRP C N   1 
ATOM   2849 C  CA  . TRP C 1 187 ? 19.07358  2.55924   34.71006  1.000 22.85949  ? 187 TRP C CA  1 
ATOM   2850 C  C   . TRP C 1 187 ? 19.09408  3.69219   35.73181  1.000 27.07251  ? 187 TRP C C   1 
ATOM   2851 O  O   . TRP C 1 187 ? 19.99616  3.80910   36.56224  1.000 27.47636  ? 187 TRP C O   1 
ATOM   2852 C  CB  . TRP C 1 187 ? 17.81906  1.67088   34.88465  1.000 24.20005  ? 187 TRP C CB  1 
ATOM   2853 C  CG  . TRP C 1 187 ? 17.53543  1.13443   36.29645  1.000 24.20705  ? 187 TRP C CG  1 
ATOM   2854 C  CD1 . TRP C 1 187 ? 18.34611  1.20083   37.40450  1.000 25.11660  ? 187 TRP C CD1 1 
ATOM   2855 C  CD2 . TRP C 1 187 ? 16.35526  0.43003   36.70084  1.000 24.55367  ? 187 TRP C CD2 1 
ATOM   2856 N  NE1 . TRP C 1 187 ? 17.71146  0.60562   38.49175  1.000 27.38324  ? 187 TRP C NE1 1 
ATOM   2857 C  CE2 . TRP C 1 187 ? 16.49433  0.12040   38.07690  1.000 27.93124  ? 187 TRP C CE2 1 
ATOM   2858 C  CE3 . TRP C 1 187 ? 15.19094  0.03376   36.03315  1.000 24.09394  ? 187 TRP C CE3 1 
ATOM   2859 C  CZ2 . TRP C 1 187 ? 15.50666  -0.55921  38.78913  1.000 26.98345  ? 187 TRP C CZ2 1 
ATOM   2860 C  CZ3 . TRP C 1 187 ? 14.19983  -0.63641  36.75153  1.000 27.77577  ? 187 TRP C CZ3 1 
ATOM   2861 C  CH2 . TRP C 1 187 ? 14.36964  -0.93046  38.11561  1.000 26.91826  ? 187 TRP C CH2 1 
ATOM   2862 N  N   . THR C 1 188 ? 18.07310  4.53499   35.64132  1.000 23.80364  ? 188 THR C N   1 
ATOM   2863 C  CA  . THR C 1 188 ? 17.83896  5.63206   36.57917  1.000 27.18772  ? 188 THR C CA  1 
ATOM   2864 C  C   . THR C 1 188 ? 16.98111  5.24488   37.78281  1.000 30.12537  ? 188 THR C C   1 
ATOM   2865 O  O   . THR C 1 188 ? 16.70274  6.11656   38.61502  1.000 31.24231  ? 188 THR C O   1 
ATOM   2866 C  CB  . THR C 1 188 ? 17.12175  6.77917   35.85784  1.000 26.80978  ? 188 THR C CB  1 
ATOM   2867 O  OG1 . THR C 1 188 ? 15.93149  6.26317   35.23757  1.000 25.57903  ? 188 THR C OG1 1 
ATOM   2868 C  CG2 . THR C 1 188 ? 18.02693  7.41878   34.79464  1.000 27.36502  ? 188 THR C CG2 1 
ATOM   2869 N  N   . THR C 1 189 ? 16.53753  3.99240   37.87743  1.000 29.74845  ? 189 THR C N   1 
ATOM   2870 C  CA  . THR C 1 189 ? 15.43463  3.47604   38.70588  1.000 26.15795  ? 189 THR C CA  1 
ATOM   2871 C  C   . THR C 1 189 ? 14.12432  4.03085   38.14909  1.000 36.96084  ? 189 THR C C   1 
ATOM   2872 O  O   . THR C 1 189 ? 14.14062  5.01986   37.40121  1.000 30.68819  ? 189 THR C O   1 
ATOM   2873 C  CB  . THR C 1 189 ? 15.51920  3.83420   40.19719  1.000 35.35028  ? 189 THR C CB  1 
ATOM   2874 O  OG1 . THR C 1 189 ? 15.03811  5.16845   40.39688  1.000 35.58700  ? 189 THR C OG1 1 
ATOM   2875 C  CG2 . THR C 1 189 ? 16.93914  3.69440   40.71570  1.000 35.40368  ? 189 THR C CG2 1 
ATOM   2876 N  N   . PRO C 1 190 ? 12.98745  3.41449   38.45121  1.000 33.56268  ? 190 PRO C N   1 
ATOM   2877 C  CA  . PRO C 1 190 ? 11.70550  3.88164   37.87426  1.000 31.69511  ? 190 PRO C CA  1 
ATOM   2878 C  C   . PRO C 1 190 ? 10.89209  4.82092   38.75377  1.000 31.69904  ? 190 PRO C C   1 
ATOM   2879 O  O   . PRO C 1 190 ? 9.72354   5.05805   38.42019  1.000 35.25738  ? 190 PRO C O   1 
ATOM   2880 C  CB  . PRO C 1 190 ? 10.94657  2.56513   37.67770  1.000 29.61512  ? 190 PRO C CB  1 
ATOM   2881 C  CG  . PRO C 1 190 ? 11.40050  1.70563   38.83466  1.000 34.86925  ? 190 PRO C CG  1 
ATOM   2882 C  CD  . PRO C 1 190 ? 12.87284  2.06131   39.03220  1.000 30.45434  ? 190 PRO C CD  1 
ATOM   2883 N  N   . ASP C 1 191 ? 11.45475  5.37346   39.83430  1.000 29.62494  ? 191 ASP C N   1 
ATOM   2884 C  CA  . ASP C 1 191 ? 10.66762  6.24991   40.69495  1.000 34.86650  ? 191 ASP C CA  1 
ATOM   2885 C  C   . ASP C 1 191 ? 10.48395  7.60950   40.01389  1.000 34.13948  ? 191 ASP C C   1 
ATOM   2886 O  O   . ASP C 1 191 ? 10.83031  7.80230   38.84517  1.000 37.38295  ? 191 ASP C O   1 
ATOM   2887 C  CB  . ASP C 1 191 ? 11.31076  6.37710   42.07476  1.000 37.39011  ? 191 ASP C CB  1 
ATOM   2888 C  CG  . ASP C 1 191 ? 12.68774  7.03491   42.04810  1.000 53.23108  ? 191 ASP C CG  1 
ATOM   2889 O  OD1 . ASP C 1 191 ? 13.02182  7.76731   41.09140  1.000 52.87357  ? 191 ASP C OD1 1 
ATOM   2890 O  OD2 . ASP C 1 191 ? 13.43915  6.84803   43.02933  1.000 48.12185  ? 191 ASP C OD2 1 
ATOM   2891 N  N   . THR C 1 192 ? 9.91374   8.57852   40.73113  1.000 34.62715  ? 192 THR C N   1 
ATOM   2892 C  CA  . THR C 1 192 ? 9.72610   9.91860   40.17914  1.000 41.32685  ? 192 THR C CA  1 
ATOM   2893 C  C   . THR C 1 192 ? 10.61266  10.97149  40.84527  1.000 35.35348  ? 192 THR C C   1 
ATOM   2894 O  O   . THR C 1 192 ? 10.36573  12.16804  40.67625  1.000 41.90844  ? 192 THR C O   1 
ATOM   2895 C  CB  . THR C 1 192 ? 8.26544   10.34081  40.28095  1.000 39.00085  ? 192 THR C CB  1 
ATOM   2896 O  OG1 . THR C 1 192 ? 7.82444   10.15485  41.62639  1.000 42.63249  ? 192 THR C OG1 1 
ATOM   2897 C  CG2 . THR C 1 192 ? 7.40887   9.50264   39.35258  1.000 40.42152  ? 192 THR C CG2 1 
ATOM   2898 N  N   . SER C 1 193 ? 11.63135  10.55868  41.59397  1.000 39.31175  ? 193 SER C N   1 
ATOM   2899 C  CA  . SER C 1 193 ? 12.57128  11.49996  42.21379  1.000 35.36343  ? 193 SER C CA  1 
ATOM   2900 C  C   . SER C 1 193 ? 13.36974  12.25316  41.15774  1.000 31.02555  ? 193 SER C C   1 
ATOM   2901 O  O   . SER C 1 193 ? 14.04698  11.61464  40.33463  1.000 34.29232  ? 193 SER C O   1 
ATOM   2902 C  CB  . SER C 1 193 ? 13.54258  10.74955  43.12272  1.000 43.55776  ? 193 SER C CB  1 
ATOM   2903 O  OG  . SER C 1 193 ? 12.84673  9.96775   44.07308  1.000 64.86916  ? 193 SER C OG  1 
ATOM   2904 N  N   . PRO C 1 194 ? 13.34343  13.58352  41.13987  1.000 36.31330  ? 194 PRO C N   1 
ATOM   2905 C  CA  . PRO C 1 194 ? 14.09583  14.31946  40.11268  1.000 35.50432  ? 194 PRO C CA  1 
ATOM   2906 C  C   . PRO C 1 194 ? 15.58137  13.98294  40.15615  1.000 40.87355  ? 194 PRO C C   1 
ATOM   2907 O  O   . PRO C 1 194 ? 16.19698  13.89617  41.21771  1.000 38.17738  ? 194 PRO C O   1 
ATOM   2908 C  CB  . PRO C 1 194 ? 13.84502  15.79131  40.46801  1.000 41.60513  ? 194 PRO C CB  1 
ATOM   2909 C  CG  . PRO C 1 194 ? 12.57917  15.78230  41.23363  1.000 48.51636  ? 194 PRO C CG  1 
ATOM   2910 C  CD  . PRO C 1 194 ? 12.56713  14.48414  42.00469  1.000 44.78036  ? 194 PRO C CD  1 
ATOM   2911 N  N   . ASN C 1 195 ? 16.15885  13.80966  38.97912  1.000 33.88222  ? 195 ASN C N   1 
ATOM   2912 C  CA  . ASN C 1 195 ? 17.53783  13.37117  38.86371  1.000 29.81975  ? 195 ASN C CA  1 
ATOM   2913 C  C   . ASN C 1 195 ? 18.27070  14.13237  37.77077  1.000 31.49432  ? 195 ASN C C   1 
ATOM   2914 O  O   . ASN C 1 195 ? 19.38992  13.75205  37.41949  1.000 33.36507  ? 195 ASN C O   1 
ATOM   2915 C  CB  . ASN C 1 195 ? 17.59261  11.86102  38.54281  1.000 29.42800  ? 195 ASN C CB  1 
ATOM   2916 C  CG  . ASN C 1 195 ? 16.89035  11.52478  37.22980  1.000 33.32193  ? 195 ASN C CG  1 
ATOM   2917 O  OD1 . ASN C 1 195 ? 16.36737  12.39479  36.56782  1.000 27.51295  ? 195 ASN C OD1 1 
ATOM   2918 N  ND2 . ASN C 1 195 ? 16.91402  10.25602  36.84274  1.000 31.25857  ? 195 ASN C ND2 1 
ATOM   2919 N  N   . CYS C 1 196 ? 17.67452  15.17240  37.21041  1.000 29.76185  ? 196 CYS C N   1 
ATOM   2920 C  CA  . CYS C 1 196 ? 18.17718  15.74129  35.96933  1.000 37.33667  ? 196 CYS C CA  1 
ATOM   2921 C  C   . CYS C 1 196 ? 18.03806  17.25798  36.00118  1.000 42.92143  ? 196 CYS C C   1 
ATOM   2922 O  O   . CYS C 1 196 ? 17.08753  17.80166  36.56990  1.000 38.37148  ? 196 CYS C O   1 
ATOM   2923 C  CB  . CYS C 1 196 ? 17.41636  15.12137  34.78295  1.000 33.20310  ? 196 CYS C CB  1 
ATOM   2924 S  SG  . CYS C 1 196 ? 18.06445  15.48685  33.15057  1.000 35.61304  ? 196 CYS C SG  1 
ATOM   2925 N  N   . THR C 1 197 ? 19.00604  17.93552  35.38765  1.000 38.24246  ? 197 THR C N   1 
ATOM   2926 C  CA  . THR C 1 197 ? 19.07286  19.39646  35.35993  1.000 40.37294  ? 197 THR C CA  1 
ATOM   2927 C  C   . THR C 1 197 ? 19.03643  19.86985  33.90973  1.000 46.19457  ? 197 THR C C   1 
ATOM   2928 O  O   . THR C 1 197 ? 19.96878  19.61229  33.14272  1.000 44.40761  ? 197 THR C O   1 
ATOM   2929 C  CB  . THR C 1 197 ? 20.33335  19.88169  36.07516  1.000 38.16270  ? 197 THR C CB  1 
ATOM   2930 O  OG1 . THR C 1 197 ? 20.20639  19.56467  37.45603  1.000 36.90782  ? 197 THR C OG1 1 
ATOM   2931 C  CG2 . THR C 1 197 ? 20.52872  21.39082  35.89238  1.000 37.63821  ? 197 THR C CG2 1 
ATOM   2932 N  N   . ILE C 1 198 ? 17.95095  20.53881  33.52677  1.000 31.64107  ? 198 ILE C N   1 
ATOM   2933 C  CA  . ILE C 1 198 ? 17.83086  21.07792  32.17399  1.000 41.99208  ? 198 ILE C CA  1 
ATOM   2934 C  C   . ILE C 1 198 ? 18.10137  22.57466  32.23444  1.000 41.64083  ? 198 ILE C C   1 
ATOM   2935 O  O   . ILE C 1 198 ? 18.97335  23.09381  31.52949  1.000 53.76480  ? 198 ILE C O   1 
ATOM   2936 C  CB  . ILE C 1 198 ? 16.44104  20.79199  31.57346  1.000 36.02708  ? 198 ILE C CB  1 
ATOM   2937 C  CG1 . ILE C 1 198 ? 16.12367  19.28958  31.59736  1.000 30.48584  ? 198 ILE C CG1 1 
ATOM   2938 C  CG2 . ILE C 1 198 ? 16.37227  21.28352  30.13055  1.000 37.42115  ? 198 ILE C CG2 1 
ATOM   2939 C  CD1 . ILE C 1 198 ? 14.66909  18.98477  31.30687  1.000 36.22283  ? 198 ILE C CD1 1 
ATOM   2940 N  N   . ALA C 1 199 ? 17.32623  23.27904  33.04936  1.000 37.71887  ? 199 ALA C N   1 
ATOM   2941 C  CA  . ALA C 1 199 ? 17.43444  24.72269  33.22119  1.000 42.20752  ? 199 ALA C CA  1 
ATOM   2942 C  C   . ALA C 1 199 ? 17.62596  25.13290  34.67176  1.000 44.17943  ? 199 ALA C C   1 
ATOM   2943 O  O   . ALA C 1 199 ? 18.18502  26.19809  34.93157  1.000 49.73558  ? 199 ALA C O   1 
ATOM   2944 C  CB  . ALA C 1 199 ? 16.19018  25.43225  32.66114  1.000 39.12154  ? 199 ALA C CB  1 
ATOM   2945 N  N   . GLN C 1 200 ? 17.14146  24.33668  35.61703  1.000 45.58347  ? 200 GLN C N   1 
ATOM   2946 C  CA  . GLN C 1 200 ? 17.38431  24.54713  37.03658  1.000 44.41253  ? 200 GLN C CA  1 
ATOM   2947 C  C   . GLN C 1 200 ? 17.80329  23.22095  37.63961  1.000 42.00598  ? 200 GLN C C   1 
ATOM   2948 O  O   . GLN C 1 200 ? 17.50839  22.15306  37.10105  1.000 40.45802  ? 200 GLN C O   1 
ATOM   2949 C  CB  . GLN C 1 200 ? 16.14494  25.04059  37.78900  1.000 55.29744  ? 200 GLN C CB  1 
ATOM   2950 C  CG  . GLN C 1 200 ? 15.45569  26.24940  37.22201  1.000 66.55361  ? 200 GLN C CG  1 
ATOM   2951 C  CD  . GLN C 1 200 ? 14.20337  26.57734  38.01044  1.000 58.06326  ? 200 GLN C CD  1 
ATOM   2952 O  OE1 . GLN C 1 200 ? 13.78524  25.80141  38.86921  1.000 51.91968  ? 200 GLN C OE1 1 
ATOM   2953 N  NE2 . GLN C 1 200 ? 13.59895  27.72643  37.72515  1.000 75.78514  ? 200 GLN C NE2 1 
ATOM   2954 N  N   . ASP C 1 201 ? 18.47155  23.29449  38.77992  1.000 39.57949  ? 201 ASP C N   1 
ATOM   2955 C  CA  . ASP C 1 201 ? 18.97819  22.09014  39.42114  1.000 43.55969  ? 201 ASP C CA  1 
ATOM   2956 C  C   . ASP C 1 201 ? 17.82860  21.13115  39.73052  1.000 43.96865  ? 201 ASP C C   1 
ATOM   2957 O  O   . ASP C 1 201 ? 16.82963  21.52558  40.33071  1.000 41.10071  ? 201 ASP C O   1 
ATOM   2958 C  CB  . ASP C 1 201 ? 19.73152  22.47789  40.69994  1.000 58.66786  ? 201 ASP C CB  1 
ATOM   2959 C  CG  . ASP C 1 201 ? 20.48396  21.31367  41.31740  1.000 74.35303  ? 201 ASP C CG  1 
ATOM   2960 O  OD1 . ASP C 1 201 ? 21.33310  20.71151  40.62863  1.000 73.91598  ? 201 ASP C OD1 1 
ATOM   2961 O  OD2 . ASP C 1 201 ? 20.22530  21.00269  42.49708  1.000 84.86475  ? 201 ASP C OD2 1 
ATOM   2962 N  N   . LYS C 1 202 ? 17.95783  19.87499  39.28638  1.000 36.39606  ? 202 LYS C N   1 
ATOM   2963 C  CA  . LYS C 1 202 ? 16.99069  18.81491  39.58331  1.000 46.55510  ? 202 LYS C CA  1 
ATOM   2964 C  C   . LYS C 1 202 ? 15.55653  19.22822  39.22706  1.000 38.97893  ? 202 LYS C C   1 
ATOM   2965 O  O   . LYS C 1 202 ? 14.60922  19.04455  40.00065  1.000 38.16426  ? 202 LYS C O   1 
ATOM   2966 C  CB  . LYS C 1 202 ? 17.09638  18.37758  41.04413  1.000 52.28071  ? 202 LYS C CB  1 
ATOM   2967 C  CG  . LYS C 1 202 ? 18.30780  17.48872  41.32440  1.000 55.69590  ? 202 LYS C CG  1 
ATOM   2968 N  N   . ASP C 1 203 ? 15.39599  19.78657  38.03187  1.000 39.01767  ? 203 ASP C N   1 
ATOM   2969 C  CA  . ASP C 1 203 ? 14.08258  20.21834  37.58760  1.000 37.65385  ? 203 ASP C CA  1 
ATOM   2970 C  C   . ASP C 1 203 ? 13.34076  19.14332  36.80061  1.000 36.23161  ? 203 ASP C C   1 
ATOM   2971 O  O   . ASP C 1 203 ? 12.22282  19.39869  36.33709  1.000 30.27349  ? 203 ASP C O   1 
ATOM   2972 C  CB  . ASP C 1 203 ? 14.19594  21.49402  36.75056  1.000 31.25285  ? 203 ASP C CB  1 
ATOM   2973 C  CG  . ASP C 1 203 ? 15.03168  21.31576  35.47644  1.000 35.14915  ? 203 ASP C CG  1 
ATOM   2974 O  OD1 . ASP C 1 203 ? 15.49990  20.19522  35.16789  1.000 37.54797  ? 203 ASP C OD1 1 
ATOM   2975 O  OD2 . ASP C 1 203 ? 15.20652  22.31960  34.75331  1.000 41.04047  ? 203 ASP C OD2 1 
ATOM   2976 N  N   . SER C 1 204 ? 13.91177  17.94663  36.65805  1.000 29.26084  ? 204 SER C N   1 
ATOM   2977 C  CA  . SER C 1 204 ? 13.24343  16.92849  35.85548  1.000 24.10533  ? 204 SER C CA  1 
ATOM   2978 C  C   . SER C 1 204 ? 13.65006  15.52734  36.30052  1.000 30.82812  ? 204 SER C C   1 
ATOM   2979 O  O   . SER C 1 204 ? 14.68756  15.32625  36.94448  1.000 29.09022  ? 204 SER C O   1 
ATOM   2980 C  CB  . SER C 1 204 ? 13.55563  17.12115  34.36319  1.000 32.47636  ? 204 SER C CB  1 
ATOM   2981 O  OG  . SER C 1 204 ? 14.95489  17.21509  34.13764  1.000 37.54052  ? 204 SER C OG  1 
ATOM   2982 N  N   . LYS C 1 205 ? 12.79835  14.55570  35.95882  1.000 24.17776  ? 205 LYS C N   1 
ATOM   2983 C  CA  . LYS C 1 205 ? 13.09899  13.12623  36.09872  1.000 25.20293  ? 205 LYS C CA  1 
ATOM   2984 C  C   . LYS C 1 205 ? 13.24665  12.53815  34.70087  1.000 23.16138  ? 205 LYS C C   1 
ATOM   2985 O  O   . LYS C 1 205 ? 12.26999  12.46795  33.94411  1.000 24.51487  ? 205 LYS C O   1 
ATOM   2986 C  CB  . LYS C 1 205 ? 12.00351  12.37538  36.85760  1.000 27.91604  ? 205 LYS C CB  1 
ATOM   2987 C  CG  . LYS C 1 205 ? 12.09835  10.82948  36.73275  1.000 29.87062  ? 205 LYS C CG  1 
ATOM   2988 C  CD  . LYS C 1 205 ? 13.26858  10.21997  37.55097  1.000 30.12036  ? 205 LYS C CD  1 
ATOM   2989 C  CE  . LYS C 1 205 ? 13.49332  8.72181   37.22644  1.000 27.50645  ? 205 LYS C CE  1 
ATOM   2990 N  NZ  . LYS C 1 205 ? 14.05101  7.97694   38.41400  1.000 37.24011  ? 205 LYS C NZ  1 
ATOM   2991 N  N   . LEU C 1 206 ? 14.46387  12.14146  34.35421  1.000 21.44605  ? 206 LEU C N   1 
ATOM   2992 C  CA  . LEU C 1 206 ? 14.71180  11.34315  33.15677  1.000 25.09032  ? 206 LEU C CA  1 
ATOM   2993 C  C   . LEU C 1 206 ? 14.63294  9.89004   33.57687  1.000 22.61143  ? 206 LEU C C   1 
ATOM   2994 O  O   . LEU C 1 206 ? 15.41821  9.44237   34.42554  1.000 24.77358  ? 206 LEU C O   1 
ATOM   2995 C  CB  . LEU C 1 206 ? 16.08526  11.65009  32.55038  1.000 22.69982  ? 206 LEU C CB  1 
ATOM   2996 C  CG  . LEU C 1 206 ? 16.48357  10.80191  31.32757  1.000 24.55148  ? 206 LEU C CG  1 
ATOM   2997 C  CD1 . LEU C 1 206 ? 15.68943  11.26549  30.11985  1.000 26.73977  ? 206 LEU C CD1 1 
ATOM   2998 C  CD2 . LEU C 1 206 ? 18.00292  10.92916  31.11483  1.000 26.67663  ? 206 LEU C CD2 1 
ATOM   2999 N  N   . THR C 1 207 ? 13.68035  9.15401   33.02317  1.000 19.18145  ? 207 THR C N   1 
ATOM   3000 C  CA  . THR C 1 207 ? 13.60257  7.71613   33.26924  1.000 22.73644  ? 207 THR C CA  1 
ATOM   3001 C  C   . THR C 1 207 ? 14.24257  7.05595   32.05324  1.000 27.65121  ? 207 THR C C   1 
ATOM   3002 O  O   . THR C 1 207 ? 13.72630  7.16835   30.93357  1.000 23.57488  ? 207 THR C O   1 
ATOM   3003 C  CB  . THR C 1 207 ? 12.16494  7.22314   33.50431  1.000 25.18306  ? 207 THR C CB  1 
ATOM   3004 O  OG1 . THR C 1 207 ? 11.52469  7.96670   34.56640  1.000 23.54651  ? 207 THR C OG1 1 
ATOM   3005 C  CG2 . THR C 1 207 ? 12.17234  5.73659   33.94604  1.000 26.99177  ? 207 THR C CG2 1 
ATOM   3006 N  N   . LEU C 1 208 ? 15.39554  6.42044   32.25992  1.000 22.54150  ? 208 LEU C N   1 
ATOM   3007 C  CA  . LEU C 1 208 ? 16.14454  5.79086   31.17549  1.000 21.69668  ? 208 LEU C CA  1 
ATOM   3008 C  C   . LEU C 1 208 ? 16.53993  4.40613   31.64281  1.000 22.77989  ? 208 LEU C C   1 
ATOM   3009 O  O   . LEU C 1 208 ? 17.16846  4.26776   32.69944  1.000 23.93177  ? 208 LEU C O   1 
ATOM   3010 C  CB  . LEU C 1 208 ? 17.39699  6.59577   30.80368  1.000 23.47123  ? 208 LEU C CB  1 
ATOM   3011 C  CG  . LEU C 1 208 ? 18.25168  6.02651   29.65139  1.000 23.46395  ? 208 LEU C CG  1 
ATOM   3012 C  CD1 . LEU C 1 208 ? 17.45017  5.90302   28.33974  1.000 20.74364  ? 208 LEU C CD1 1 
ATOM   3013 C  CD2 . LEU C 1 208 ? 19.54984  6.85960   29.39755  1.000 25.51891  ? 208 LEU C CD2 1 
ATOM   3014 N  N   . VAL C 1 209 ? 16.15906  3.38773   30.87729  1.000 19.78488  ? 209 VAL C N   1 
ATOM   3015 C  CA  . VAL C 1 209 ? 16.52014  2.01483   31.15973  1.000 18.18858  ? 209 VAL C CA  1 
ATOM   3016 C  C   . VAL C 1 209 ? 17.29287  1.47878   29.97479  1.000 24.45806  ? 209 VAL C C   1 
ATOM   3017 O  O   . VAL C 1 209 ? 16.77728  1.49186   28.85953  1.000 22.26934  ? 209 VAL C O   1 
ATOM   3018 C  CB  . VAL C 1 209 ? 15.26798  1.16111   31.41478  1.000 20.34219  ? 209 VAL C CB  1 
ATOM   3019 C  CG1 . VAL C 1 209 ? 15.67147  -0.24307  31.88117  1.000 22.28168  ? 209 VAL C CG1 1 
ATOM   3020 C  CG2 . VAL C 1 209 ? 14.38257  1.86659   32.47681  1.000 25.88147  ? 209 VAL C CG2 1 
ATOM   3021 N  N   . LEU C 1 210 ? 18.51065  0.99493   30.21746  1.000 20.98458  ? 210 LEU C N   1 
ATOM   3022 C  CA  . LEU C 1 210 ? 19.34989  0.38064   29.17736  1.000 18.26852  ? 210 LEU C CA  1 
ATOM   3023 C  C   . LEU C 1 210 ? 19.46511  -1.09030  29.51277  1.000 28.30439  ? 210 LEU C C   1 
ATOM   3024 O  O   . LEU C 1 210 ? 20.07311  -1.44075  30.52757  1.000 29.75586  ? 210 LEU C O   1 
ATOM   3025 C  CB  . LEU C 1 210 ? 20.72847  1.02172   29.12784  1.000 23.80985  ? 210 LEU C CB  1 
ATOM   3026 C  CG  . LEU C 1 210 ? 20.76124  2.53223   28.89458  1.000 21.79830  ? 210 LEU C CG  1 
ATOM   3027 C  CD1 . LEU C 1 210 ? 22.19983  3.00297   28.86280  1.000 22.50092  ? 210 LEU C CD1 1 
ATOM   3028 C  CD2 . LEU C 1 210 ? 20.03380  2.92791   27.58071  1.000 21.85088  ? 210 LEU C CD2 1 
ATOM   3029 N  N   . THR C 1 211 ? 18.91750  -1.95798  28.65987  1.000 22.50128  ? 211 THR C N   1 
ATOM   3030 C  CA  . THR C 1 211 ? 18.94979  -3.39338  28.92359  1.000 23.61919  ? 211 THR C CA  1 
ATOM   3031 C  C   . THR C 1 211 ? 19.81546  -4.06586  27.87215  1.000 30.19857  ? 211 THR C C   1 
ATOM   3032 O  O   . THR C 1 211 ? 19.56214  -3.92985  26.67204  1.000 26.15503  ? 211 THR C O   1 
ATOM   3033 C  CB  . THR C 1 211 ? 17.53263  -3.96997  28.95076  1.000 34.19251  ? 211 THR C CB  1 
ATOM   3034 O  OG1 . THR C 1 211 ? 16.78984  -3.36434  30.03480  1.000 27.36569  ? 211 THR C OG1 1 
ATOM   3035 C  CG2 . THR C 1 211 ? 17.57749  -5.45324  29.15073  1.000 33.13166  ? 211 THR C CG2 1 
ATOM   3036 N  N   . LYS C 1 212 ? 20.83815  -4.78407  28.30919  1.000 25.31552  ? 212 LYS C N   1 
ATOM   3037 C  CA  . LYS C 1 212 ? 21.79877  -5.34215  27.37153  1.000 25.72668  ? 212 LYS C CA  1 
ATOM   3038 C  C   . LYS C 1 212 ? 21.26651  -6.66533  26.85078  1.000 47.39881  ? 212 LYS C C   1 
ATOM   3039 O  O   . LYS C 1 212 ? 21.05027  -7.60129  27.62631  1.000 38.19053  ? 212 LYS C O   1 
ATOM   3040 C  CB  . LYS C 1 212 ? 23.17181  -5.51402  28.01255  1.000 26.09808  ? 212 LYS C CB  1 
ATOM   3041 C  CG  . LYS C 1 212 ? 24.23598  -6.01259  27.06046  1.000 28.59868  ? 212 LYS C CG  1 
ATOM   3042 C  CD  . LYS C 1 212 ? 25.61708  -5.82300  27.66100  1.000 34.92774  ? 212 LYS C CD  1 
ATOM   3043 C  CE  . LYS C 1 212 ? 26.72814  -6.35431  26.77313  1.000 46.26470  ? 212 LYS C CE  1 
ATOM   3044 N  NZ  . LYS C 1 212 ? 26.79813  -5.68549  25.45472  1.000 35.61938  ? 212 LYS C NZ  1 
ATOM   3045 N  N   . CYS C 1 213 ? 21.01375  -6.71687  25.54626  1.000 33.56889  ? 213 CYS C N   1 
ATOM   3046 C  CA  . CYS C 1 213 ? 20.69338  -7.95504  24.85109  1.000 33.78582  ? 213 CYS C CA  1 
ATOM   3047 C  C   . CYS C 1 213 ? 21.86710  -8.29373  23.93847  1.000 38.43132  ? 213 CYS C C   1 
ATOM   3048 O  O   . CYS C 1 213 ? 21.84040  -8.04144  22.73842  1.000 41.79884  ? 213 CYS C O   1 
ATOM   3049 C  CB  . CYS C 1 213 ? 19.40003  -7.81768  24.07904  1.000 32.28864  ? 213 CYS C CB  1 
ATOM   3050 S  SG  . CYS C 1 213 ? 18.03338  -7.05624  25.00531  1.000 50.03180  ? 213 CYS C SG  1 
ATOM   3051 N  N   . GLY C 1 214 ? 22.94559  -8.76339  24.54732  1.000 43.19272  ? 214 GLY C N   1 
ATOM   3052 C  CA  . GLY C 1 214 ? 24.13735  -9.09527  23.78811  1.000 39.43468  ? 214 GLY C CA  1 
ATOM   3053 C  C   . GLY C 1 214 ? 24.69239  -7.86721  23.10005  1.000 37.57182  ? 214 GLY C C   1 
ATOM   3054 O  O   . GLY C 1 214 ? 24.96653  -6.83664  23.72206  1.000 45.35787  ? 214 GLY C O   1 
ATOM   3055 N  N   . SER C 1 215 ? 24.78497  -7.93399  21.78006  1.000 34.93449  ? 215 SER C N   1 
ATOM   3056 C  CA  . SER C 1 215 ? 25.39917  -6.85418  21.02693  1.000 37.42992  ? 215 SER C CA  1 
ATOM   3057 C  C   . SER C 1 215 ? 24.50805  -5.62942  20.84974  1.000 31.65715  ? 215 SER C C   1 
ATOM   3058 O  O   . SER C 1 215 ? 24.96366  -4.63839  20.26068  1.000 34.70345  ? 215 SER C O   1 
ATOM   3059 C  CB  . SER C 1 215 ? 25.84365  -7.37304  19.65772  1.000 55.63531  ? 215 SER C CB  1 
ATOM   3060 O  OG  . SER C 1 215 ? 26.49897  -6.35193  18.93671  1.000 68.65962  ? 215 SER C OG  1 
ATOM   3061 N  N   . GLN C 1 216 ? 23.24196  -5.66809  21.26905  1.000 23.58454  ? 216 GLN C N   1 
ATOM   3062 C  CA  . GLN C 1 216 ? 22.37595  -4.50187  21.17088  1.000 22.42272  ? 216 GLN C CA  1 
ATOM   3063 C  C   . GLN C 1 216 ? 21.88295  -4.09905  22.54497  1.000 26.33433  ? 216 GLN C C   1 
ATOM   3064 O  O   . GLN C 1 216 ? 21.60793  -4.96204  23.38969  1.000 26.55375  ? 216 GLN C O   1 
ATOM   3065 C  CB  . GLN C 1 216 ? 21.12481  -4.72614  20.30299  1.000 31.32060  ? 216 GLN C CB  1 
ATOM   3066 C  CG  . GLN C 1 216 ? 21.31381  -4.59616  18.83555  1.000 48.64872  ? 216 GLN C CG  1 
ATOM   3067 C  CD  . GLN C 1 216 ? 20.00002  -4.79182  18.10628  1.000 25.29178  ? 216 GLN C CD  1 
ATOM   3068 O  OE1 . GLN C 1 216 ? 19.11998  -3.90568  18.05533  1.000 26.47837  ? 216 GLN C OE1 1 
ATOM   3069 N  NE2 . GLN C 1 216 ? 19.84489  -5.98209  17.56281  1.000 28.17970  ? 216 GLN C NE2 1 
ATOM   3070 N  N   . ILE C 1 217 ? 21.74953  -2.79082  22.74411  1.000 21.27368  ? 217 ILE C N   1 
ATOM   3071 C  CA  . ILE C 1 217 ? 21.14555  -2.23658  23.95367  1.000 21.44774  ? 217 ILE C CA  1 
ATOM   3072 C  C   . ILE C 1 217 ? 19.69147  -1.89713  23.63755  1.000 24.57702  ? 217 ILE C C   1 
ATOM   3073 O  O   . ILE C 1 217 ? 19.41511  -1.13136  22.70760  1.000 24.04520  ? 217 ILE C O   1 
ATOM   3074 C  CB  . ILE C 1 217 ? 21.89814  -0.98969  24.43238  1.000 19.39363  ? 217 ILE C CB  1 
ATOM   3075 C  CG1 . ILE C 1 217 ? 23.38206  -1.30324  24.64471  1.000 24.98106  ? 217 ILE C CG1 1 
ATOM   3076 C  CG2 . ILE C 1 217 ? 21.25073  -0.41051  25.72760  1.000 24.21091  ? 217 ILE C CG2 1 
ATOM   3077 C  CD1 . ILE C 1 217 ? 23.62905  -2.55923  25.51906  1.000 28.34001  ? 217 ILE C CD1 1 
ATOM   3078 N  N   . LEU C 1 218 ? 18.76359  -2.45388  24.40803  1.000 20.05592  ? 218 LEU C N   1 
ATOM   3079 C  CA  . LEU C 1 218 ? 17.34919  -2.08570  24.29617  1.000 17.53428  ? 218 LEU C CA  1 
ATOM   3080 C  C   . LEU C 1 218 ? 17.10984  -0.94256  25.26282  1.000 25.28098  ? 218 LEU C C   1 
ATOM   3081 O  O   . LEU C 1 218 ? 17.35068  -1.08864  26.47001  1.000 22.87852  ? 218 LEU C O   1 
ATOM   3082 C  CB  . LEU C 1 218 ? 16.44873  -3.28049  24.62257  1.000 22.10283  ? 218 LEU C CB  1 
ATOM   3083 C  CG  . LEU C 1 218 ? 14.92463  -3.05189  24.57779  1.000 23.59285  ? 218 LEU C CG  1 
ATOM   3084 C  CD1 . LEU C 1 218 ? 14.50196  -2.70386  23.16478  1.000 22.90880  ? 218 LEU C CD1 1 
ATOM   3085 C  CD2 . LEU C 1 218 ? 14.20449  -4.34314  25.04538  1.000 24.91051  ? 218 LEU C CD2 1 
ATOM   3086 N  N   . ALA C 1 219 ? 16.65165  0.19514   24.74868  1.000 19.73382  ? 219 ALA C N   1 
ATOM   3087 C  CA  . ALA C 1 219 ? 16.58072  1.41457   25.54202  1.000 20.79787  ? 219 ALA C CA  1 
ATOM   3088 C  C   . ALA C 1 219 ? 15.13750  1.90451   25.66612  1.000 20.66153  ? 219 ALA C C   1 
ATOM   3089 O  O   . ALA C 1 219 ? 14.37222  1.89347   24.69379  1.000 23.62873  ? 219 ALA C O   1 
ATOM   3090 C  CB  . ALA C 1 219 ? 17.47455  2.49792   24.90825  1.000 21.95518  ? 219 ALA C CB  1 
ATOM   3091 N  N   . ASN C 1 220 ? 14.75917  2.34154   26.86673  1.000 16.91930  ? 220 ASN C N   1 
ATOM   3092 C  CA  . ASN C 1 220 ? 13.41818  2.84893   27.08741  1.000 17.57010  ? 220 ASN C CA  1 
ATOM   3093 C  C   . ASN C 1 220 ? 13.55682  4.19052   27.78184  1.000 21.71565  ? 220 ASN C C   1 
ATOM   3094 O  O   . ASN C 1 220 ? 14.27653  4.27888   28.78430  1.000 21.52620  ? 220 ASN C O   1 
ATOM   3095 C  CB  . ASN C 1 220 ? 12.62008  1.85366   27.95972  1.000 19.64463  ? 220 ASN C CB  1 
ATOM   3096 C  CG  . ASN C 1 220 ? 11.18874  2.28352   28.17507  1.000 26.96735  ? 220 ASN C CG  1 
ATOM   3097 O  OD1 . ASN C 1 220 ? 10.87582  2.90189   29.17788  1.000 25.85740  ? 220 ASN C OD1 1 
ATOM   3098 N  ND2 . ASN C 1 220 ? 10.31616  1.96613   27.24003  1.000 26.58005  ? 220 ASN C ND2 1 
ATOM   3099 N  N   . VAL C 1 221 ? 12.89995  5.23610   27.26689  1.000 16.17361  ? 221 VAL C N   1 
ATOM   3100 C  CA  . VAL C 1 221 ? 13.11150  6.57759   27.81820  1.000 16.77732  ? 221 VAL C CA  1 
ATOM   3101 C  C   . VAL C 1 221 ? 11.80359  7.36019   27.94393  1.000 17.75457  ? 221 VAL C C   1 
ATOM   3102 O  O   . VAL C 1 221 ? 10.89018  7.21989   27.13399  1.000 19.13794  ? 221 VAL C O   1 
ATOM   3103 C  CB  . VAL C 1 221 ? 14.15097  7.35959   26.97856  1.000 19.36838  ? 221 VAL C CB  1 
ATOM   3104 C  CG1 . VAL C 1 221 ? 13.60351  7.62696   25.57314  1.000 20.40895  ? 221 VAL C CG1 1 
ATOM   3105 C  CG2 . VAL C 1 221 ? 14.56096  8.66680   27.66990  1.000 21.86254  ? 221 VAL C CG2 1 
ATOM   3106 N  N   . SER C 1 222 ? 11.70590  8.16788   29.00447  1.000 17.76906  ? 222 SER C N   1 
ATOM   3107 C  CA  . SER C 1 222 ? 10.63235  9.15648   29.14804  1.000 21.23771  ? 222 SER C CA  1 
ATOM   3108 C  C   . SER C 1 222 ? 11.15684  10.31493  29.99620  1.000 22.77294  ? 222 SER C C   1 
ATOM   3109 O  O   . SER C 1 222 ? 12.17573  10.19808  30.65721  1.000 22.34781  ? 222 SER C O   1 
ATOM   3110 C  CB  . SER C 1 222 ? 9.39081   8.55875   29.80052  1.000 24.69044  ? 222 SER C CB  1 
ATOM   3111 O  OG  . SER C 1 222 ? 9.67834   8.29205   31.18219  1.000 27.46708  ? 222 SER C OG  1 
ATOM   3112 N  N   . LEU C 1 223 ? 10.43484  11.43428  29.99395  1.000 19.99471  ? 223 LEU C N   1 
ATOM   3113 C  CA  . LEU C 1 223 ? 10.89140  12.61545  30.73529  1.000 20.46148  ? 223 LEU C CA  1 
ATOM   3114 C  C   . LEU C 1 223 ? 9.71717   13.24898  31.45618  1.000 23.92852  ? 223 LEU C C   1 
ATOM   3115 O  O   . LEU C 1 223 ? 8.64084   13.38590  30.87458  1.000 21.62804  ? 223 LEU C O   1 
ATOM   3116 C  CB  . LEU C 1 223 ? 11.50788  13.63543  29.77698  1.000 20.21984  ? 223 LEU C CB  1 
ATOM   3117 C  CG  . LEU C 1 223 ? 12.06559  14.91320  30.39468  1.000 22.79311  ? 223 LEU C CG  1 
ATOM   3118 C  CD1 . LEU C 1 223 ? 13.27413  14.55817  31.24217  1.000 26.34544  ? 223 LEU C CD1 1 
ATOM   3119 C  CD2 . LEU C 1 223 ? 12.37955  15.90276  29.28530  1.000 25.44783  ? 223 LEU C CD2 1 
ATOM   3120 N  N   . ILE C 1 224 ? 9.91322   13.60349  32.72577  1.000 20.25098  ? 224 ILE C N   1 
ATOM   3121 C  CA  . ILE C 1 224 ? 8.94381   14.38450  33.49377  1.000 22.38467  ? 224 ILE C CA  1 
ATOM   3122 C  C   . ILE C 1 224 ? 9.66429   15.63949  33.94911  1.000 27.52023  ? 224 ILE C C   1 
ATOM   3123 O  O   . ILE C 1 224 ? 10.57475  15.55045  34.77612  1.000 28.18211  ? 224 ILE C O   1 
ATOM   3124 C  CB  . ILE C 1 224 ? 8.42032   13.62689  34.72284  1.000 27.77776  ? 224 ILE C CB  1 
ATOM   3125 C  CG1 . ILE C 1 224 ? 7.77188   12.29351  34.31353  1.000 26.36579  ? 224 ILE C CG1 1 
ATOM   3126 C  CG2 . ILE C 1 224 ? 7.47330   14.53934  35.54622  1.000 29.23901  ? 224 ILE C CG2 1 
ATOM   3127 C  CD1 . ILE C 1 224 ? 7.63891   11.32392  35.49293  1.000 29.49105  ? 224 ILE C CD1 1 
ATOM   3128 N  N   . VAL C 1 225 ? 9.26615   16.80410  33.43300  1.000 25.44858  ? 225 VAL C N   1 
ATOM   3129 C  CA  . VAL C 1 225 ? 9.78812   18.07631  33.93646  1.000 25.68547  ? 225 VAL C CA  1 
ATOM   3130 C  C   . VAL C 1 225 ? 8.86536   18.54660  35.05269  1.000 26.48509  ? 225 VAL C C   1 
ATOM   3131 O  O   . VAL C 1 225 ? 7.63409   18.50207  34.90115  1.000 28.55911  ? 225 VAL C O   1 
ATOM   3132 C  CB  . VAL C 1 225 ? 9.89516   19.12825  32.81982  1.000 26.13629  ? 225 VAL C CB  1 
ATOM   3133 C  CG1 . VAL C 1 225 ? 10.49494  20.39286  33.37025  1.000 30.88654  ? 225 VAL C CG1 1 
ATOM   3134 C  CG2 . VAL C 1 225 ? 10.77574  18.59114  31.66720  1.000 27.56594  ? 225 VAL C CG2 1 
ATOM   3135 N  N   . VAL C 1 226 ? 9.45179   18.88680  36.21368  1.000 27.73870  ? 226 VAL C N   1 
ATOM   3136 C  CA  . VAL C 1 226 ? 8.67678   19.23796  37.40040  1.000 30.80268  ? 226 VAL C CA  1 
ATOM   3137 C  C   . VAL C 1 226 ? 8.80323   20.70355  37.80588  1.000 31.71982  ? 226 VAL C C   1 
ATOM   3138 O  O   . VAL C 1 226 ? 7.98493   21.17719  38.61160  1.000 34.90441  ? 226 VAL C O   1 
ATOM   3139 C  CB  . VAL C 1 226 ? 9.03904   18.32331  38.59452  1.000 35.55770  ? 226 VAL C CB  1 
ATOM   3140 C  CG1 . VAL C 1 226 ? 8.75824   16.86883  38.23677  1.000 38.49945  ? 226 VAL C CG1 1 
ATOM   3141 C  CG2 . VAL C 1 226 ? 10.49488  18.50407  38.99065  1.000 35.47960  ? 226 VAL C CG2 1 
ATOM   3142 N  N   . ALA C 1 227 ? 9.78966   21.43669  37.29979  1.000 28.77582  ? 227 ALA C N   1 
ATOM   3143 C  CA  . ALA C 1 227 ? 10.00055  22.82026  37.70685  1.000 31.14838  ? 227 ALA C CA  1 
ATOM   3144 C  C   . ALA C 1 227 ? 10.77846  23.55519  36.61925  1.000 33.33359  ? 227 ALA C C   1 
ATOM   3145 O  O   . ALA C 1 227 ? 11.28823  22.95435  35.67506  1.000 39.10416  ? 227 ALA C O   1 
ATOM   3146 C  CB  . ALA C 1 227 ? 10.73813  22.89330  39.04582  1.000 36.29542  ? 227 ALA C CB  1 
ATOM   3147 N  N   . GLY C 1 228 ? 10.85420  24.88089  36.75792  1.000 32.41740  ? 228 GLY C N   1 
ATOM   3148 C  CA  . GLY C 1 228 ? 11.70460  25.64967  35.89412  1.000 31.79890  ? 228 GLY C CA  1 
ATOM   3149 C  C   . GLY C 1 228 ? 11.06163  25.98020  34.56181  1.000 47.20091  ? 228 GLY C C   1 
ATOM   3150 O  O   . GLY C 1 228 ? 9.86126   25.75471  34.32390  1.000 33.57440  ? 228 GLY C O   1 
ATOM   3151 N  N   . LYS C 1 229 ? 11.90492  26.51006  33.66263  1.000 35.25797  ? 229 LYS C N   1 
ATOM   3152 C  CA  . LYS C 1 229 ? 11.41230  27.13888  32.43750  1.000 39.46431  ? 229 LYS C CA  1 
ATOM   3153 C  C   . LYS C 1 229 ? 10.76164  26.15142  31.47228  1.000 37.32157  ? 229 LYS C C   1 
ATOM   3154 O  O   . LYS C 1 229 ? 9.96906   26.57029  30.62362  1.000 38.86716  ? 229 LYS C O   1 
ATOM   3155 C  CB  . LYS C 1 229 ? 12.53013  27.91732  31.73420  1.000 41.46949  ? 229 LYS C CB  1 
ATOM   3156 C  CG  . LYS C 1 229 ? 13.46428  27.09093  30.90225  1.000 47.85348  ? 229 LYS C CG  1 
ATOM   3157 C  CD  . LYS C 1 229 ? 14.61364  27.92786  30.32385  1.000 61.19602  ? 229 LYS C CD  1 
ATOM   3158 C  CE  . LYS C 1 229 ? 14.18249  28.77803  29.14257  1.000 64.99959  ? 229 LYS C CE  1 
ATOM   3159 N  NZ  . LYS C 1 229 ? 15.36275  29.17110  28.30516  1.000 76.09439  ? 229 LYS C NZ  1 
ATOM   3160 N  N   . TYR C 1 230 ? 11.08952  24.86560  31.54584  1.000 33.50097  ? 230 TYR C N   1 
ATOM   3161 C  CA  . TYR C 1 230 ? 10.50690  23.89834  30.62580  1.000 27.19884  ? 230 TYR C CA  1 
ATOM   3162 C  C   . TYR C 1 230 ? 9.35948   23.10964  31.26040  1.000 25.17376  ? 230 TYR C C   1 
ATOM   3163 O  O   . TYR C 1 230 ? 8.84433   22.16840  30.63540  1.000 28.61095  ? 230 TYR C O   1 
ATOM   3164 C  CB  . TYR C 1 230 ? 11.58915  22.95183  30.10423  1.000 27.61834  ? 230 TYR C CB  1 
ATOM   3165 C  CG  . TYR C 1 230 ? 12.62520  23.68001  29.25100  1.000 29.19009  ? 230 TYR C CG  1 
ATOM   3166 C  CD1 . TYR C 1 230 ? 12.29105  24.17449  28.00266  1.000 29.74934  ? 230 TYR C CD1 1 
ATOM   3167 C  CD2 . TYR C 1 230 ? 13.91522  23.89520  29.72223  1.000 37.96522  ? 230 TYR C CD2 1 
ATOM   3168 C  CE1 . TYR C 1 230 ? 13.23791  24.85227  27.21795  1.000 31.44894  ? 230 TYR C CE1 1 
ATOM   3169 C  CE2 . TYR C 1 230 ? 14.86235  24.57705  28.95111  1.000 31.57002  ? 230 TYR C CE2 1 
ATOM   3170 C  CZ  . TYR C 1 230 ? 14.51335  25.05573  27.71233  1.000 35.95208  ? 230 TYR C CZ  1 
ATOM   3171 O  OH  . TYR C 1 230 ? 15.45613  25.72567  26.96029  1.000 40.09496  ? 230 TYR C OH  1 
ATOM   3172 N  N   . HIS C 1 231 ? 8.93926   23.48109  32.47413  1.000 28.75967  ? 231 HIS C N   1 
ATOM   3173 C  CA  . HIS C 1 231 ? 7.90264   22.71461  33.16186  1.000 28.40428  ? 231 HIS C CA  1 
ATOM   3174 C  C   . HIS C 1 231 ? 6.53985   22.89515  32.50221  1.000 31.37831  ? 231 HIS C C   1 
ATOM   3175 O  O   . HIS C 1 231 ? 5.89724   21.91347  32.12398  1.000 30.22254  ? 231 HIS C O   1 
ATOM   3176 C  CB  . HIS C 1 231 ? 7.81586   23.12054  34.63566  1.000 28.20883  ? 231 HIS C CB  1 
ATOM   3177 C  CG  . HIS C 1 231 ? 6.72079   22.41791  35.36790  1.000 37.18755  ? 231 HIS C CG  1 
ATOM   3178 N  ND1 . HIS C 1 231 ? 6.09890   22.94216  36.48138  1.000 39.37932  ? 231 HIS C ND1 1 
ATOM   3179 C  CD2 . HIS C 1 231 ? 6.14746   21.21052  35.14711  1.000 29.11572  ? 231 HIS C CD2 1 
ATOM   3180 C  CE1 . HIS C 1 231 ? 5.18090   22.09180  36.90823  1.000 36.46347  ? 231 HIS C CE1 1 
ATOM   3181 N  NE2 . HIS C 1 231 ? 5.19367   21.03093  36.11877  1.000 31.10151  ? 231 HIS C NE2 1 
ATOM   3182 N  N   . ILE C 1 232 ? 6.09151   24.14700  32.35403  1.000 29.33816  ? 232 ILE C N   1 
ATOM   3183 C  CA  . ILE C 1 232 ? 4.80682   24.48637  31.74974  1.000 29.12574  ? 232 ILE C CA  1 
ATOM   3184 C  C   . ILE C 1 232 ? 5.12946   25.31431  30.50370  1.000 35.27774  ? 232 ILE C C   1 
ATOM   3185 O  O   . ILE C 1 232 ? 5.56713   26.46859  30.60871  1.000 37.25802  ? 232 ILE C O   1 
ATOM   3186 C  CB  . ILE C 1 232 ? 3.92295   25.30193  32.70651  1.000 31.15398  ? 232 ILE C CB  1 
ATOM   3187 C  CG1 . ILE C 1 232 ? 3.70747   24.58915  34.04654  1.000 38.79128  ? 232 ILE C CG1 1 
ATOM   3188 C  CG2 . ILE C 1 232 ? 2.57045   25.57600  32.04370  1.000 32.60185  ? 232 ILE C CG2 1 
ATOM   3189 C  CD1 . ILE C 1 232 ? 2.85108   23.37089  33.94257  1.000 45.40875  ? 232 ILE C CD1 1 
ATOM   3190 N  N   . ILE C 1 233 ? 4.86053   24.76862  29.33639  1.000 29.37318  ? 233 ILE C N   1 
ATOM   3191 C  CA  . ILE C 1 233 ? 5.19161   25.42542  28.08516  1.000 27.47843  ? 233 ILE C CA  1 
ATOM   3192 C  C   . ILE C 1 233 ? 4.04443   26.34032  27.71257  1.000 32.64377  ? 233 ILE C C   1 
ATOM   3193 O  O   . ILE C 1 233 ? 2.88550   25.90898  27.68625  1.000 30.35987  ? 233 ILE C O   1 
ATOM   3194 C  CB  . ILE C 1 233 ? 5.43472   24.38791  26.97273  1.000 25.85945  ? 233 ILE C CB  1 
ATOM   3195 C  CG1 . ILE C 1 233 ? 6.52156   23.37629  27.36092  1.000 31.30851  ? 233 ILE C CG1 1 
ATOM   3196 C  CG2 . ILE C 1 233 ? 5.74558   25.08462  25.62736  1.000 32.68482  ? 233 ILE C CG2 1 
ATOM   3197 C  CD1 . ILE C 1 233 ? 7.81874   24.00433  27.78786  1.000 37.24368  ? 233 ILE C CD1 1 
ATOM   3198 N  N   . ASN C 1 234 ? 4.36105   27.60318  27.41399  1.000 30.41452  ? 234 ASN C N   1 
ATOM   3199 C  CA  . ASN C 1 234 ? 3.37096   28.52355  26.85659  1.000 27.68102  ? 234 ASN C CA  1 
ATOM   3200 C  C   . ASN C 1 234 ? 4.05485   29.31620  25.75586  1.000 30.53718  ? 234 ASN C C   1 
ATOM   3201 O  O   . ASN C 1 234 ? 4.78395   30.27114  26.03107  1.000 37.31299  ? 234 ASN C O   1 
ATOM   3202 C  CB  . ASN C 1 234 ? 2.74495   29.43852  27.90356  1.000 32.52918  ? 234 ASN C CB  1 
ATOM   3203 C  CG  . ASN C 1 234 ? 1.58629   30.22923  27.32896  1.000 37.89234  ? 234 ASN C CG  1 
ATOM   3204 O  OD1 . ASN C 1 234 ? 1.63301   30.61624  26.15846  1.000 39.68575  ? 234 ASN C OD1 1 
ATOM   3205 N  ND2 . ASN C 1 234 ? 0.54281   30.45987  28.12351  1.000 37.67701  ? 234 ASN C ND2 1 
ATOM   3206 N  N   . ASN C 1 235 ? 3.83306   28.89643  24.51243  1.000 31.48139  ? 235 ASN C N   1 
ATOM   3207 C  CA  . ASN C 1 235 ? 4.45648   29.57439  23.38193  1.000 29.65981  ? 235 ASN C CA  1 
ATOM   3208 C  C   . ASN C 1 235 ? 3.67661   30.78628  22.89933  1.000 35.64237  ? 235 ASN C C   1 
ATOM   3209 O  O   . ASN C 1 235 ? 4.12434   31.42905  21.95724  1.000 37.76065  ? 235 ASN C O   1 
ATOM   3210 C  CB  . ASN C 1 235 ? 4.65530   28.60535  22.21902  1.000 30.84668  ? 235 ASN C CB  1 
ATOM   3211 C  CG  . ASN C 1 235 ? 5.65396   27.51662  22.53580  1.000 38.02284  ? 235 ASN C CG  1 
ATOM   3212 O  OD1 . ASN C 1 235 ? 5.38403   26.35566  22.27682  1.000 36.45035  ? 235 ASN C OD1 1 
ATOM   3213 N  ND2 . ASN C 1 235 ? 6.81001   27.88506  23.10118  1.000 33.34166  ? 235 ASN C ND2 1 
ATOM   3214 N  N   . LYS C 1 236 ? 2.50134   31.07757  23.45397  1.000 34.17510  ? 236 LYS C N   1 
ATOM   3215 C  CA  . LYS C 1 236 ? 1.91464   32.39570  23.21991  1.000 36.39876  ? 236 LYS C CA  1 
ATOM   3216 C  C   . LYS C 1 236 ? 2.70422   33.46356  23.97035  1.000 49.02029  ? 236 LYS C C   1 
ATOM   3217 O  O   . LYS C 1 236 ? 3.06106   34.50165  23.40026  1.000 48.45339  ? 236 LYS C O   1 
ATOM   3218 C  CB  . LYS C 1 236 ? 0.44080   32.40404  23.63407  1.000 40.34868  ? 236 LYS C CB  1 
ATOM   3219 N  N   . THR C 1 237 ? 3.06579   33.18563  25.22533  1.000 37.77513  ? 237 THR C N   1 
ATOM   3220 C  CA  . THR C 1 237 ? 3.86647   34.12611  26.00509  1.000 43.54428  ? 237 THR C CA  1 
ATOM   3221 C  C   . THR C 1 237 ? 5.35011   34.03928  25.64743  1.000 47.70549  ? 237 THR C C   1 
ATOM   3222 O  O   . THR C 1 237 ? 6.02828   35.06715  25.55738  1.000 51.57300  ? 237 THR C O   1 
ATOM   3223 C  CB  . THR C 1 237 ? 3.65341   33.89999  27.50695  1.000 41.35612  ? 237 THR C CB  1 
ATOM   3224 O  OG1 . THR C 1 237 ? 4.19563   32.63285  27.89077  1.000 59.57134  ? 237 THR C OG1 1 
ATOM   3225 C  CG2 . THR C 1 237 ? 2.17065   33.91340  27.84949  1.000 49.15568  ? 237 THR C CG2 1 
ATOM   3226 N  N   . ASN C 1 238 ? 5.88485   32.82881  25.46677  1.000 40.67320  ? 238 ASN C N   1 
ATOM   3227 C  CA  . ASN C 1 238 ? 7.29867   32.61022  25.16308  1.000 35.09518  ? 238 ASN C CA  1 
ATOM   3228 C  C   . ASN C 1 238 ? 7.38556   31.86431  23.84192  1.000 46.03309  ? 238 ASN C C   1 
ATOM   3229 O  O   . ASN C 1 238 ? 7.58409   30.64089  23.81888  1.000 37.99937  ? 238 ASN C O   1 
ATOM   3230 C  CB  . ASN C 1 238 ? 8.01197   31.79887  26.24326  1.000 48.11560  ? 238 ASN C CB  1 
ATOM   3231 C  CG  . ASN C 1 238 ? 7.71192   32.28366  27.64425  1.000 57.79289  ? 238 ASN C CG  1 
ATOM   3232 O  OD1 . ASN C 1 238 ? 6.80279   31.78039  28.31156  1.000 68.99528  ? 238 ASN C OD1 1 
ATOM   3233 N  ND2 . ASN C 1 238 ? 8.49318   33.24274  28.11177  1.000 63.79414  ? 238 ASN C ND2 1 
ATOM   3234 N  N   . PRO C 1 239 ? 7.29462   32.57123  22.71717  1.000 46.93457  ? 239 PRO C N   1 
ATOM   3235 C  CA  . PRO C 1 239 ? 7.34406   31.88299  21.41787  1.000 37.43831  ? 239 PRO C CA  1 
ATOM   3236 C  C   . PRO C 1 239 ? 8.69669   31.26512  21.07749  1.000 39.78747  ? 239 PRO C C   1 
ATOM   3237 O  O   . PRO C 1 239 ? 8.75641   30.44788  20.14829  1.000 46.00229  ? 239 PRO C O   1 
ATOM   3238 C  CB  . PRO C 1 239 ? 6.97806   32.99901  20.42252  1.000 40.69140  ? 239 PRO C CB  1 
ATOM   3239 C  CG  . PRO C 1 239 ? 7.33996   34.27020  21.13585  1.000 56.35894  ? 239 PRO C CG  1 
ATOM   3240 C  CD  . PRO C 1 239 ? 7.04367   34.01604  22.58478  1.000 38.68775  ? 239 PRO C CD  1 
ATOM   3241 N  N   . LYS C 1 240 ? 9.77332   31.57843  21.79932  1.000 37.32182  ? 240 LYS C N   1 
ATOM   3242 C  CA  . LYS C 1 240 ? 11.07250  31.04552  21.40431  1.000 46.59020  ? 240 LYS C CA  1 
ATOM   3243 C  C   . LYS C 1 240 ? 11.44361  29.75345  22.11748  1.000 48.55162  ? 240 LYS C C   1 
ATOM   3244 O  O   . LYS C 1 240 ? 12.42627  29.11769  21.72527  1.000 51.49275  ? 240 LYS C O   1 
ATOM   3245 C  CB  . LYS C 1 240 ? 12.17557  32.08501  21.64052  1.000 59.86037  ? 240 LYS C CB  1 
ATOM   3246 N  N   . ILE C 1 241 ? 10.68705  29.34218  23.13401  1.000 37.01491  ? 241 ILE C N   1 
ATOM   3247 C  CA  . ILE C 1 241 ? 10.99720  28.13188  23.89631  1.000 45.51307  ? 241 ILE C CA  1 
ATOM   3248 C  C   . ILE C 1 241 ? 10.44417  26.94053  23.11751  1.000 31.21712  ? 241 ILE C C   1 
ATOM   3249 O  O   . ILE C 1 241 ? 9.25932   26.61429  23.23719  1.000 35.13663  ? 241 ILE C O   1 
ATOM   3250 C  CB  . ILE C 1 241 ? 10.43329  28.19760  25.31837  1.000 38.20201  ? 241 ILE C CB  1 
ATOM   3251 C  CG1 . ILE C 1 241 ? 11.03676  29.38632  26.06838  1.000 44.17432  ? 241 ILE C CG1 1 
ATOM   3252 C  CG2 . ILE C 1 241 ? 10.71343  26.90818  26.07879  1.000 52.51541  ? 241 ILE C CG2 1 
ATOM   3253 C  CD1 . ILE C 1 241 ? 10.56839  29.49051  27.49538  1.000 75.54271  ? 241 ILE C CD1 1 
ATOM   3254 N  N   . LYS C 1 242 ? 11.30046  26.29688  22.29930  1.000 31.70620  ? 242 LYS C N   1 
ATOM   3255 C  CA  . LYS C 1 242 ? 10.86574  25.22932  21.41081  1.000 29.15795  ? 242 LYS C CA  1 
ATOM   3256 C  C   . LYS C 1 242 ? 11.73948  23.98584  21.44145  1.000 27.88271  ? 242 LYS C C   1 
ATOM   3257 O  O   . LYS C 1 242 ? 11.48194  23.07533  20.66028  1.000 27.58162  ? 242 LYS C O   1 
ATOM   3258 C  CB  . LYS C 1 242 ? 10.82027  25.73328  19.95660  1.000 31.51628  ? 242 LYS C CB  1 
ATOM   3259 C  CG  . LYS C 1 242 ? 9.96371   26.96912  19.72649  1.000 42.27900  ? 242 LYS C CG  1 
ATOM   3260 C  CD  . LYS C 1 242 ? 8.48928   26.66949  19.99316  1.000 38.22796  ? 242 LYS C CD  1 
ATOM   3261 C  CE  . LYS C 1 242 ? 7.71543   26.52784  18.69599  1.000 58.70935  ? 242 LYS C CE  1 
ATOM   3262 N  NZ  . LYS C 1 242 ? 6.25294   26.62737  18.91314  1.000 51.42638  ? 242 LYS C NZ  1 
ATOM   3263 N  N   . SER C 1 243 ? 12.76652  23.92590  22.29193  1.000 27.15831  ? 243 SER C N   1 
ATOM   3264 C  CA  . SER C 1 243 ? 13.64800  22.76547  22.30230  1.000 25.31200  ? 243 SER C CA  1 
ATOM   3265 C  C   . SER C 1 243 ? 14.60488  22.84884  23.48386  1.000 32.97570  ? 243 SER C C   1 
ATOM   3266 O  O   . SER C 1 243 ? 14.89520  23.93408  23.99267  1.000 31.69857  ? 243 SER C O   1 
ATOM   3267 C  CB  . SER C 1 243 ? 14.45029  22.65863  20.99798  1.000 29.73665  ? 243 SER C CB  1 
ATOM   3268 O  OG  . SER C 1 243 ? 15.38208  23.71712  20.90373  1.000 38.74014  ? 243 SER C OG  1 
ATOM   3269 N  N   . PHE C 1 244 ? 15.11651  21.69097  23.89608  1.000 28.21536  ? 244 PHE C N   1 
ATOM   3270 C  CA  . PHE C 1 244 ? 16.18650  21.63028  24.89037  1.000 27.57588  ? 244 PHE C CA  1 
ATOM   3271 C  C   . PHE C 1 244 ? 16.85854  20.27494  24.75883  1.000 28.55178  ? 244 PHE C C   1 
ATOM   3272 O  O   . PHE C 1 244 ? 16.32618  19.36314  24.13403  1.000 26.27017  ? 244 PHE C O   1 
ATOM   3273 C  CB  . PHE C 1 244 ? 15.67482  21.83775  26.31800  1.000 24.57606  ? 244 PHE C CB  1 
ATOM   3274 C  CG  . PHE C 1 244 ? 14.60603  20.85379  26.72552  1.000 24.87020  ? 244 PHE C CG  1 
ATOM   3275 C  CD1 . PHE C 1 244 ? 14.94108  19.63739  27.28802  1.000 27.16530  ? 244 PHE C CD1 1 
ATOM   3276 C  CD2 . PHE C 1 244 ? 13.25983  21.15349  26.53674  1.000 26.73674  ? 244 PHE C CD2 1 
ATOM   3277 C  CE1 . PHE C 1 244 ? 13.95596  18.72682  27.64340  1.000 27.15784  ? 244 PHE C CE1 1 
ATOM   3278 C  CE2 . PHE C 1 244 ? 12.27056  20.25757  26.90765  1.000 25.31851  ? 244 PHE C CE2 1 
ATOM   3279 C  CZ  . PHE C 1 244 ? 12.61960  19.04404  27.46234  1.000 25.61711  ? 244 PHE C CZ  1 
ATOM   3280 N  N   . THR C 1 245 ? 18.03913  20.15482  25.35511  1.000 25.77518  ? 245 THR C N   1 
ATOM   3281 C  CA  . THR C 1 245 ? 18.82269  18.94404  25.19712  1.000 27.52669  ? 245 THR C CA  1 
ATOM   3282 C  C   . THR C 1 245 ? 19.24191  18.41408  26.56554  1.000 27.09760  ? 245 THR C C   1 
ATOM   3283 O  O   . THR C 1 245 ? 19.58481  19.18754  27.46574  1.000 28.42701  ? 245 THR C O   1 
ATOM   3284 C  CB  . THR C 1 245 ? 20.04518  19.22829  24.33474  1.000 37.32598  ? 245 THR C CB  1 
ATOM   3285 O  OG1 . THR C 1 245 ? 19.60318  19.79297  23.09641  1.000 33.85451  ? 245 THR C OG1 1 
ATOM   3286 C  CG2 . THR C 1 245 ? 20.80754  17.94193  24.02528  1.000 34.56009  ? 245 THR C CG2 1 
ATOM   3287 N  N   . ILE C 1 246 ? 19.23034  17.08831  26.70009  1.000 29.07805  ? 246 ILE C N   1 
ATOM   3288 C  CA  . ILE C 1 246 ? 19.73194  16.38928  27.87723  1.000 28.68544  ? 246 ILE C CA  1 
ATOM   3289 C  C   . ILE C 1 246 ? 20.90026  15.52625  27.40732  1.000 30.20956  ? 246 ILE C C   1 
ATOM   3290 O  O   . ILE C 1 246 ? 20.73770  14.72324  26.48406  1.000 28.10253  ? 246 ILE C O   1 
ATOM   3291 C  CB  . ILE C 1 246 ? 18.63025  15.52754  28.52411  1.000 25.83536  ? 246 ILE C CB  1 
ATOM   3292 C  CG1 . ILE C 1 246 ? 17.54395  16.42316  29.13596  1.000 27.21508  ? 246 ILE C CG1 1 
ATOM   3293 C  CG2 . ILE C 1 246 ? 19.21021  14.53353  29.52297  1.000 25.13645  ? 246 ILE C CG2 1 
ATOM   3294 C  CD1 . ILE C 1 246 ? 16.33494  15.65245  29.61842  1.000 30.75847  ? 246 ILE C CD1 1 
ATOM   3295 N  N   . LYS C 1 247 ? 22.08425  15.71293  28.00640  1.000 29.23289  ? 247 LYS C N   1 
ATOM   3296 C  CA  . LYS C 1 247 ? 23.29915  15.01345  27.57096  1.000 25.05470  ? 247 LYS C CA  1 
ATOM   3297 C  C   . LYS C 1 247 ? 23.80965  14.04676  28.63457  1.000 28.19633  ? 247 LYS C C   1 
ATOM   3298 O  O   . LYS C 1 247 ? 23.94228  14.42477  29.80602  1.000 28.62571  ? 247 LYS C O   1 
ATOM   3299 C  CB  . LYS C 1 247 ? 24.41262  16.00604  27.24374  1.000 30.36428  ? 247 LYS C CB  1 
ATOM   3300 C  CG  . LYS C 1 247 ? 24.04673  16.97394  26.17167  1.000 29.23116  ? 247 LYS C CG  1 
ATOM   3301 C  CD  . LYS C 1 247 ? 25.22680  17.85960  25.77253  1.000 36.74812  ? 247 LYS C CD  1 
ATOM   3302 C  CE  . LYS C 1 247 ? 24.81682  18.80231  24.65083  1.000 49.18829  ? 247 LYS C CE  1 
ATOM   3303 N  NZ  . LYS C 1 247 ? 25.94251  19.63334  24.13562  1.000 44.85923  ? 247 LYS C NZ  1 
ATOM   3304 N  N   . LEU C 1 248 ? 24.11198  12.80715  28.22201  1.000 27.77251  ? 248 LEU C N   1 
ATOM   3305 C  CA  . LEU C 1 248 ? 24.81565  11.84184  29.06340  1.000 24.99857  ? 248 LEU C CA  1 
ATOM   3306 C  C   . LEU C 1 248 ? 26.17736  11.58313  28.42777  1.000 25.21934  ? 248 LEU C C   1 
ATOM   3307 O  O   . LEU C 1 248 ? 26.25707  11.12431  27.27995  1.000 26.24927  ? 248 LEU C O   1 
ATOM   3308 C  CB  . LEU C 1 248 ? 24.04188  10.52714  29.20750  1.000 23.94460  ? 248 LEU C CB  1 
ATOM   3309 C  CG  . LEU C 1 248 ? 22.80975  10.45217  30.12567  1.000 35.81615  ? 248 LEU C CG  1 
ATOM   3310 C  CD1 . LEU C 1 248 ? 21.71562  11.39437  29.66364  1.000 37.88139  ? 248 LEU C CD1 1 
ATOM   3311 C  CD2 . LEU C 1 248 ? 22.26627  9.01843   30.18217  1.000 34.37367  ? 248 LEU C CD2 1 
ATOM   3312 N  N   . LEU C 1 249 ? 27.23350  11.92274  29.15250  1.000 27.03696  ? 249 LEU C N   1 
ATOM   3313 C  CA  . LEU C 1 249 ? 28.60566  11.83929  28.66417  1.000 25.89562  ? 249 LEU C CA  1 
ATOM   3314 C  C   . LEU C 1 249 ? 29.33510  10.78633  29.48779  1.000 31.13223  ? 249 LEU C C   1 
ATOM   3315 O  O   . LEU C 1 249 ? 29.17125  10.74715  30.69933  1.000 34.32392  ? 249 LEU C O   1 
ATOM   3316 C  CB  . LEU C 1 249 ? 29.32676  13.18425  28.83252  1.000 30.90075  ? 249 LEU C CB  1 
ATOM   3317 C  CG  . LEU C 1 249 ? 28.54236  14.44077  28.43728  1.000 49.21297  ? 249 LEU C CG  1 
ATOM   3318 C  CD1 . LEU C 1 249 ? 29.26315  15.70721  28.87742  1.000 55.35320  ? 249 LEU C CD1 1 
ATOM   3319 C  CD2 . LEU C 1 249 ? 28.29307  14.47433  26.94641  1.000 39.84933  ? 249 LEU C CD2 1 
ATOM   3320 N  N   . PHE C 1 250 ? 30.11082  9.90824   28.84283  1.000 29.75668  ? 250 PHE C N   1 
ATOM   3321 C  CA  . PHE C 1 250 ? 30.75898  8.79978   29.54295  1.000 27.00460  ? 250 PHE C CA  1 
ATOM   3322 C  C   . PHE C 1 250 ? 32.25997  8.79258   29.27736  1.000 36.94288  ? 250 PHE C C   1 
ATOM   3323 O  O   . PHE C 1 250 ? 32.71197  9.18438   28.19767  1.000 34.41444  ? 250 PHE C O   1 
ATOM   3324 C  CB  . PHE C 1 250 ? 30.18475  7.44202   29.09630  1.000 29.27390  ? 250 PHE C CB  1 
ATOM   3325 C  CG  . PHE C 1 250 ? 28.69970  7.33381   29.26072  1.000 28.92447  ? 250 PHE C CG  1 
ATOM   3326 C  CD1 . PHE C 1 250 ? 28.15403  6.91632   30.46845  1.000 28.28035  ? 250 PHE C CD1 1 
ATOM   3327 C  CD2 . PHE C 1 250 ? 27.84649  7.64605   28.22352  1.000 24.83722  ? 250 PHE C CD2 1 
ATOM   3328 C  CE1 . PHE C 1 250 ? 26.78219  6.81395   30.63822  1.000 26.42443  ? 250 PHE C CE1 1 
ATOM   3329 C  CE2 . PHE C 1 250 ? 26.45402  7.55199   28.39154  1.000 28.31967  ? 250 PHE C CE2 1 
ATOM   3330 C  CZ  . PHE C 1 250 ? 25.93470  7.12157   29.61128  1.000 28.34290  ? 250 PHE C CZ  1 
ATOM   3331 N  N   . ASN C 1 251 ? 33.03576  8.30357   30.24442  1.000 38.04355  ? 251 ASN C N   1 
ATOM   3332 C  CA  . ASN C 1 251 ? 34.46958  8.18469   30.01026  1.000 32.22505  ? 251 ASN C CA  1 
ATOM   3333 C  C   . ASN C 1 251 ? 34.79258  6.83974   29.34907  1.000 38.36616  ? 251 ASN C C   1 
ATOM   3334 O  O   . ASN C 1 251 ? 33.89878  6.08800   28.94511  1.000 33.43984  ? 251 ASN C O   1 
ATOM   3335 C  CB  . ASN C 1 251 ? 35.26263  8.40285   31.30760  1.000 33.88665  ? 251 ASN C CB  1 
ATOM   3336 C  CG  . ASN C 1 251 ? 35.07634  7.28861   32.33128  1.000 41.32542  ? 251 ASN C CG  1 
ATOM   3337 O  OD1 . ASN C 1 251 ? 34.58802  6.20720   32.01566  1.000 40.44616  ? 251 ASN C OD1 1 
ATOM   3338 N  ND2 . ASN C 1 251 ? 35.53761  7.53540   33.57259  1.000 39.64089  ? 251 ASN C ND2 1 
ATOM   3339 N  N   . LYS C 1 252 ? 36.09140  6.51817   29.24818  1.000 37.81607  ? 252 LYS C N   1 
ATOM   3340 C  CA  . LYS C 1 252 ? 36.52281  5.32566   28.52980  1.000 33.75086  ? 252 LYS C CA  1 
ATOM   3341 C  C   . LYS C 1 252 ? 36.03285  4.03853   29.17794  1.000 40.61875  ? 252 LYS C C   1 
ATOM   3342 O  O   . LYS C 1 252 ? 35.97979  2.99814   28.50906  1.000 38.11349  ? 252 LYS C O   1 
ATOM   3343 C  CB  . LYS C 1 252 ? 38.05636  5.30248   28.43280  1.000 41.69728  ? 252 LYS C CB  1 
ATOM   3344 N  N   . ASN C 1 253 ? 35.67885  4.08949   30.45602  1.000 33.35431  ? 253 ASN C N   1 
ATOM   3345 C  CA  . ASN C 1 253 ? 35.12878  2.96977   31.20099  1.000 37.29468  ? 253 ASN C CA  1 
ATOM   3346 C  C   . ASN C 1 253 ? 33.61024  2.95006   31.20504  1.000 39.76173  ? 253 ASN C C   1 
ATOM   3347 O  O   . ASN C 1 253 ? 33.02832  2.07310   31.85152  1.000 32.96040  ? 253 ASN C O   1 
ATOM   3348 C  CB  . ASN C 1 253 ? 35.62906  2.99941   32.64599  1.000 45.07764  ? 253 ASN C CB  1 
ATOM   3349 C  CG  . ASN C 1 253 ? 37.09565  2.62574   32.76445  1.000 57.86695  ? 253 ASN C CG  1 
ATOM   3350 O  OD1 . ASN C 1 253 ? 37.58817  1.76479   32.03805  1.000 47.43777  ? 253 ASN C OD1 1 
ATOM   3351 N  ND2 . ASN C 1 253 ? 37.80302  3.30446   33.65649  1.000 49.78925  ? 253 ASN C ND2 1 
ATOM   3352 N  N   . GLY C 1 254 ? 32.95838  3.86787   30.48910  1.000 35.11362  ? 254 GLY C N   1 
ATOM   3353 C  CA  . GLY C 1 254 ? 31.50305  3.93122   30.48890  1.000 33.16884  ? 254 GLY C CA  1 
ATOM   3354 C  C   . GLY C 1 254 ? 30.89827  4.56314   31.72006  1.000 30.17649  ? 254 GLY C C   1 
ATOM   3355 O  O   . GLY C 1 254 ? 29.69924  4.39461   31.97005  1.000 31.84235  ? 254 GLY C O   1 
ATOM   3356 N  N   . VAL C 1 255 ? 31.70565  5.27360   32.51278  1.000 30.28947  ? 255 VAL C N   1 
ATOM   3357 C  CA  . VAL C 1 255 ? 31.23942  5.92362   33.73163  1.000 34.98234  ? 255 VAL C CA  1 
ATOM   3358 C  C   . VAL C 1 255 ? 30.71364  7.30674   33.37374  1.000 36.62679  ? 255 VAL C C   1 
ATOM   3359 O  O   . VAL C 1 255 ? 31.32096  8.03379   32.58202  1.000 31.75935  ? 255 VAL C O   1 
ATOM   3360 C  CB  . VAL C 1 255 ? 32.38013  5.99481   34.76716  1.000 40.94727  ? 255 VAL C CB  1 
ATOM   3361 C  CG1 . VAL C 1 255 ? 31.96654  6.80133   35.99179  1.000 34.94339  ? 255 VAL C CG1 1 
ATOM   3362 C  CG2 . VAL C 1 255 ? 32.79454  4.59321   35.16947  1.000 37.34918  ? 255 VAL C CG2 1 
ATOM   3363 N  N   . LEU C 1 256 ? 29.56533  7.66045   33.93631  1.000 31.54808  ? 256 LEU C N   1 
ATOM   3364 C  CA  . LEU C 1 256 ? 28.94025  8.94675   33.65624  1.000 37.80912  ? 256 LEU C CA  1 
ATOM   3365 C  C   . LEU C 1 256 ? 29.80042  10.09796  34.16686  1.000 35.98159  ? 256 LEU C C   1 
ATOM   3366 O  O   . LEU C 1 256 ? 30.29470  10.06435  35.30111  1.000 39.22869  ? 256 LEU C O   1 
ATOM   3367 C  CB  . LEU C 1 256 ? 27.55905  8.99211   34.30677  1.000 32.69635  ? 256 LEU C CB  1 
ATOM   3368 C  CG  . LEU C 1 256 ? 26.62122  10.12204  33.89860  1.000 28.66545  ? 256 LEU C CG  1 
ATOM   3369 C  CD1 . LEU C 1 256 ? 26.17970  9.96436   32.40793  1.000 28.97895  ? 256 LEU C CD1 1 
ATOM   3370 C  CD2 . LEU C 1 256 ? 25.42838  10.09042  34.82525  1.000 30.28691  ? 256 LEU C CD2 1 
ATOM   3371 N  N   . LEU C 1 257 ? 29.98932  11.11535  33.32692  1.000 34.71136  ? 257 LEU C N   1 
ATOM   3372 C  CA  . LEU C 1 257 ? 30.77696  12.28241  33.70154  1.000 37.60758  ? 257 LEU C CA  1 
ATOM   3373 C  C   . LEU C 1 257 ? 29.90009  13.31797  34.39980  1.000 51.55543  ? 257 LEU C C   1 
ATOM   3374 O  O   . LEU C 1 257 ? 28.69705  13.41136  34.14170  1.000 39.03232  ? 257 LEU C O   1 
ATOM   3375 C  CB  . LEU C 1 257 ? 31.45549  12.89007  32.47347  1.000 35.32982  ? 257 LEU C CB  1 
ATOM   3376 C  CG  . LEU C 1 257 ? 32.48292  11.95917  31.83010  1.000 34.61376  ? 257 LEU C CG  1 
ATOM   3377 C  CD1 . LEU C 1 257 ? 32.96302  12.53554  30.52020  1.000 38.23033  ? 257 LEU C CD1 1 
ATOM   3378 C  CD2 . LEU C 1 257 ? 33.66413  11.67732  32.77520  1.000 43.14301  ? 257 LEU C CD2 1 
ATOM   3379 N  N   . ASP C 1 258 ? 30.51938  14.10432  35.29426  1.000 36.76704  ? 258 ASP C N   1 
ATOM   3380 C  CA  . ASP C 1 258 ? 29.75199  14.98440  36.17687  1.000 52.62087  ? 258 ASP C CA  1 
ATOM   3381 C  C   . ASP C 1 258 ? 29.08698  16.14424  35.45415  1.000 36.78231  ? 258 ASP C C   1 
ATOM   3382 O  O   . ASP C 1 258 ? 28.10621  16.68434  35.97685  1.000 45.70038  ? 258 ASP C O   1 
ATOM   3383 C  CB  . ASP C 1 258 ? 30.64350  15.56432  37.28382  1.000 55.32782  ? 258 ASP C CB  1 
ATOM   3384 C  CG  . ASP C 1 258 ? 31.40585  14.50206  38.03497  1.000 71.47706  ? 258 ASP C CG  1 
ATOM   3385 O  OD1 . ASP C 1 258 ? 32.08569  13.68037  37.37963  1.000 78.51182  ? 258 ASP C OD1 1 
ATOM   3386 O  OD2 . ASP C 1 258 ? 31.33043  14.49221  39.28123  1.000 93.30035  ? 258 ASP C OD2 1 
ATOM   3387 N  N   . ASN C 1 259 ? 29.56097  16.52622  34.26727  1.000 35.74575  ? 259 ASN C N   1 
ATOM   3388 C  CA  . ASN C 1 259 ? 28.88572  17.57441  33.51264  1.000 41.12872  ? 259 ASN C CA  1 
ATOM   3389 C  C   . ASN C 1 259 ? 27.72856  17.05276  32.65161  1.000 32.30672  ? 259 ASN C C   1 
ATOM   3390 O  O   . ASN C 1 259 ? 27.19603  17.80697  31.83252  1.000 40.61058  ? 259 ASN C O   1 
ATOM   3391 C  CB  . ASN C 1 259 ? 29.86969  18.34116  32.63530  1.000 40.01432  ? 259 ASN C CB  1 
ATOM   3392 C  CG  . ASN C 1 259 ? 30.73992  17.43085  31.78858  1.000 52.98294  ? 259 ASN C CG  1 
ATOM   3393 O  OD1 . ASN C 1 259 ? 31.04902  16.30511  32.17535  1.000 53.14719  ? 259 ASN C OD1 1 
ATOM   3394 N  ND2 . ASN C 1 259 ? 31.12921  17.91586  30.61757  1.000 49.32488  ? 259 ASN C ND2 1 
ATOM   3395 N  N   . SER C 1 260 ? 27.33964  15.78974  32.79533  1.000 32.63929  ? 260 SER C N   1 
ATOM   3396 C  CA  . SER C 1 260 ? 26.08045  15.35648  32.19874  1.000 30.12457  ? 260 SER C CA  1 
ATOM   3397 C  C   . SER C 1 260 ? 24.90552  16.04353  32.89555  1.000 31.62329  ? 260 SER C C   1 
ATOM   3398 O  O   . SER C 1 260 ? 24.99559  16.45658  34.05518  1.000 33.79962  ? 260 SER C O   1 
ATOM   3399 C  CB  . SER C 1 260 ? 25.92609  13.83618  32.30054  1.000 30.27891  ? 260 SER C CB  1 
ATOM   3400 O  OG  . SER C 1 260 ? 27.06670  13.15653  31.78547  1.000 30.84538  ? 260 SER C OG  1 
ATOM   3401 N  N   . ASN C 1 261 ? 23.77757  16.14911  32.18055  1.000 32.27834  ? 261 ASN C N   1 
ATOM   3402 C  CA  . ASN C 1 261 ? 22.56393  16.69296  32.80377  1.000 28.48505  ? 261 ASN C CA  1 
ATOM   3403 C  C   . ASN C 1 261 ? 22.00427  15.76372  33.87651  1.000 33.45991  ? 261 ASN C C   1 
ATOM   3404 O  O   . ASN C 1 261 ? 21.38017  16.22216  34.84576  1.000 34.24023  ? 261 ASN C O   1 
ATOM   3405 C  CB  . ASN C 1 261 ? 21.49568  16.93733  31.72601  1.000 29.66938  ? 261 ASN C CB  1 
ATOM   3406 C  CG  . ASN C 1 261 ? 21.89060  18.04053  30.76288  1.000 29.54146  ? 261 ASN C CG  1 
ATOM   3407 O  OD1 . ASN C 1 261 ? 22.58450  17.79972  29.77934  1.000 33.18648  ? 261 ASN C OD1 1 
ATOM   3408 N  ND2 . ASN C 1 261 ? 21.47347  19.26812  31.06234  1.000 38.63534  ? 261 ASN C ND2 1 
ATOM   3409 N  N   . LEU C 1 262 ? 22.18649  14.46406  33.69116  1.000 28.09465  ? 262 LEU C N   1 
ATOM   3410 C  CA  . LEU C 1 262 ? 21.74998  13.44146  34.62456  1.000 27.18133  ? 262 LEU C CA  1 
ATOM   3411 C  C   . LEU C 1 262 ? 22.73022  13.35339  35.77296  1.000 33.21536  ? 262 LEU C C   1 
ATOM   3412 O  O   . LEU C 1 262 ? 23.94600  13.31104  35.55470  1.000 32.64737  ? 262 LEU C O   1 
ATOM   3413 C  CB  . LEU C 1 262 ? 21.67747  12.08422  33.92189  1.000 28.51176  ? 262 LEU C CB  1 
ATOM   3414 C  CG  . LEU C 1 262 ? 21.34147  10.83993  34.74478  1.000 28.01201  ? 262 LEU C CG  1 
ATOM   3415 C  CD1 . LEU C 1 262 ? 19.90897  10.91985  35.28720  1.000 28.43551  ? 262 LEU C CD1 1 
ATOM   3416 C  CD2 . LEU C 1 262 ? 21.50285  9.61598   33.80419  1.000 29.18235  ? 262 LEU C CD2 1 
ATOM   3417 N  N   . GLY C 1 263 ? 22.20665  13.30317  36.99283  1.000 31.06320  ? 263 GLY C N   1 
ATOM   3418 C  CA  . GLY C 1 263 ? 23.07512  13.18102  38.15139  1.000 36.78300  ? 263 GLY C CA  1 
ATOM   3419 C  C   . GLY C 1 263 ? 23.65912  11.78530  38.29828  1.000 34.33511  ? 263 GLY C C   1 
ATOM   3420 O  O   . GLY C 1 263 ? 23.02125  10.77134  38.01477  1.000 31.68079  ? 263 GLY C O   1 
ATOM   3421 N  N   . LYS C 1 264 ? 24.88631  11.72996  38.80914  1.000 34.68597  ? 264 LYS C N   1 
ATOM   3422 C  CA  . LYS C 1 264 ? 25.57945  10.45219  38.91094  1.000 37.75023  ? 264 LYS C CA  1 
ATOM   3423 C  C   . LYS C 1 264 ? 25.02083  9.57862   40.03049  1.000 43.82471  ? 264 LYS C C   1 
ATOM   3424 O  O   . LYS C 1 264 ? 25.15675  8.34884   39.97343  1.000 36.80931  ? 264 LYS C O   1 
ATOM   3425 C  CB  . LYS C 1 264 ? 27.07348  10.68737  39.14144  1.000 41.37242  ? 264 LYS C CB  1 
ATOM   3426 C  CG  . LYS C 1 264 ? 27.83194  11.19697  37.93036  1.000 50.22619  ? 264 LYS C CG  1 
ATOM   3427 C  CD  . LYS C 1 264 ? 29.26608  11.49776  38.31372  1.000 60.66135  ? 264 LYS C CD  1 
ATOM   3428 C  CE  . LYS C 1 264 ? 29.91410  10.28080  38.97222  1.000 55.51596  ? 264 LYS C CE  1 
ATOM   3429 N  NZ  . LYS C 1 264 ? 29.96802  9.10999   38.04210  1.000 48.10185  ? 264 LYS C NZ  1 
ATOM   3430 N  N   . ALA C 1 265 ? 24.41025  10.18660  41.05578  1.000 35.65761  ? 265 ALA C N   1 
ATOM   3431 C  CA  . ALA C 1 265 ? 23.95447  9.42463   42.21270  1.000 39.50800  ? 265 ALA C CA  1 
ATOM   3432 C  C   . ALA C 1 265 ? 22.85654  8.45002   41.84543  1.000 42.75202  ? 265 ALA C C   1 
ATOM   3433 O  O   . ALA C 1 265 ? 22.69557  7.43131   42.51709  1.000 49.82922  ? 265 ALA C O   1 
ATOM   3434 C  CB  . ALA C 1 265 ? 23.46532  10.36804  43.32021  1.000 44.63418  ? 265 ALA C CB  1 
ATOM   3435 N  N   . TYR C 1 266 ? 22.15678  8.71756   40.74819  1.000 43.05472  ? 266 TYR C N   1 
ATOM   3436 C  CA  . TYR C 1 266 ? 20.92352  8.06426   40.35751  1.000 48.39238  ? 266 TYR C CA  1 
ATOM   3437 C  C   . TYR C 1 266 ? 21.12271  7.01159   39.27951  1.000 34.28622  ? 266 TYR C C   1 
ATOM   3438 O  O   . TYR C 1 266 ? 20.16220  6.31927   38.92456  1.000 39.14259  ? 266 TYR C O   1 
ATOM   3439 C  CB  . TYR C 1 266 ? 19.92607  9.12098   39.85265  1.000 41.35938  ? 266 TYR C CB  1 
ATOM   3440 C  CG  . TYR C 1 266 ? 19.67928  10.24829  40.82313  1.000 68.50219  ? 266 TYR C CG  1 
ATOM   3441 C  CD1 . TYR C 1 266 ? 18.71573  10.11744  41.81838  1.000 65.51681  ? 266 TYR C CD1 1 
ATOM   3442 C  CD2 . TYR C 1 266 ? 20.39174  11.44226  40.74905  1.000 54.85826  ? 266 TYR C CD2 1 
ATOM   3443 C  CE1 . TYR C 1 266 ? 18.47693  11.12726  42.71667  1.000 58.00804  ? 266 TYR C CE1 1 
ATOM   3444 C  CE2 . TYR C 1 266 ? 20.15564  12.46165  41.65075  1.000 67.32020  ? 266 TYR C CE2 1 
ATOM   3445 C  CZ  . TYR C 1 266 ? 19.19563  12.29493  42.63096  1.000 66.26154  ? 266 TYR C CZ  1 
ATOM   3446 O  OH  . TYR C 1 266 ? 18.95561  13.29918  43.53868  1.000 79.05904  ? 266 TYR C OH  1 
ATOM   3447 N  N   . TRP C 1 267 ? 22.34566  6.84130   38.79786  1.000 32.82839  ? 267 TRP C N   1 
ATOM   3448 C  CA  . TRP C 1 267 ? 22.62309  6.09390   37.57525  1.000 32.90623  ? 267 TRP C CA  1 
ATOM   3449 C  C   . TRP C 1 267 ? 23.49903  4.89183   37.91138  1.000 36.29239  ? 267 TRP C C   1 
ATOM   3450 O  O   . TRP C 1 267 ? 24.67815  5.04899   38.26029  1.000 34.56138  ? 267 TRP C O   1 
ATOM   3451 C  CB  . TRP C 1 267 ? 23.28556  7.02556   36.56246  1.000 31.23765  ? 267 TRP C CB  1 
ATOM   3452 C  CG  . TRP C 1 267 ? 23.70316  6.37514   35.28766  1.000 34.64426  ? 267 TRP C CG  1 
ATOM   3453 C  CD1 . TRP C 1 267 ? 24.98675  6.12428   34.86921  1.000 32.98289  ? 267 TRP C CD1 1 
ATOM   3454 C  CD2 . TRP C 1 267 ? 22.84135  5.92006   34.22757  1.000 29.29347  ? 267 TRP C CD2 1 
ATOM   3455 N  NE1 . TRP C 1 267 ? 24.97712  5.51841   33.63700  1.000 30.02967  ? 267 TRP C NE1 1 
ATOM   3456 C  CE2 . TRP C 1 267 ? 23.67236  5.38258   33.22093  1.000 28.81473  ? 267 TRP C CE2 1 
ATOM   3457 C  CE3 . TRP C 1 267 ? 21.45169  5.87813   34.05449  1.000 28.69665  ? 267 TRP C CE3 1 
ATOM   3458 C  CZ2 . TRP C 1 267 ? 23.16931  4.84521   32.04273  1.000 28.31629  ? 267 TRP C CZ2 1 
ATOM   3459 C  CZ3 . TRP C 1 267 ? 20.93690  5.32792   32.83535  1.000 27.59823  ? 267 TRP C CZ3 1 
ATOM   3460 C  CH2 . TRP C 1 267 ? 21.79508  4.81484   31.87584  1.000 27.16340  ? 267 TRP C CH2 1 
ATOM   3461 N  N   . ASN C 1 268 ? 22.93960  3.68887   37.82072  1.000 32.64031  ? 268 ASN C N   1 
ATOM   3462 C  CA  . ASN C 1 268 ? 23.69308  2.52906   38.29617  1.000 33.47055  ? 268 ASN C CA  1 
ATOM   3463 C  C   . ASN C 1 268 ? 23.01752  1.25407   37.79876  1.000 33.01940  ? 268 ASN C C   1 
ATOM   3464 O  O   . ASN C 1 268 ? 21.92054  1.28388   37.23441  1.000 32.16980  ? 268 ASN C O   1 
ATOM   3465 C  CB  . ASN C 1 268 ? 23.79533  2.51066   39.84013  1.000 34.81561  ? 268 ASN C CB  1 
ATOM   3466 C  CG  . ASN C 1 268 ? 25.07528  1.83238   40.35275  1.000 38.95635  ? 268 ASN C CG  1 
ATOM   3467 O  OD1 . ASN C 1 268 ? 25.80273  1.16159   39.61949  1.000 37.82190  ? 268 ASN C OD1 1 
ATOM   3468 N  ND2 . ASN C 1 268 ? 25.34852  2.02065   41.63182  1.000 41.23264  ? 268 ASN C ND2 1 
ATOM   3469 N  N   . PHE C 1 269 ? 23.68546  0.12913   38.02984  1.000 33.62421  ? 269 PHE C N   1 
ATOM   3470 C  CA  . PHE C 1 269 ? 23.08271  -1.16518  37.76281  1.000 33.40850  ? 269 PHE C CA  1 
ATOM   3471 C  C   . PHE C 1 269 ? 21.91194  -1.42340  38.70271  1.000 34.70296  ? 269 PHE C C   1 
ATOM   3472 O  O   . PHE C 1 269 ? 21.85768  -0.91463  39.82192  1.000 35.57426  ? 269 PHE C O   1 
ATOM   3473 C  CB  . PHE C 1 269 ? 24.13252  -2.27022  37.88856  1.000 36.05538  ? 269 PHE C CB  1 
ATOM   3474 C  CG  . PHE C 1 269 ? 25.07819  -2.29701  36.73494  1.000 37.95185  ? 269 PHE C CG  1 
ATOM   3475 C  CD1 . PHE C 1 269 ? 24.71711  -2.93399  35.55553  1.000 38.19356  ? 269 PHE C CD1 1 
ATOM   3476 C  CD2 . PHE C 1 269 ? 26.28305  -1.62384  36.78958  1.000 50.50334  ? 269 PHE C CD2 1 
ATOM   3477 C  CE1 . PHE C 1 269 ? 25.56085  -2.93545  34.47348  1.000 58.85921  ? 269 PHE C CE1 1 
ATOM   3478 C  CE2 . PHE C 1 269 ? 27.13471  -1.62082  35.69975  1.000 59.34073  ? 269 PHE C CE2 1 
ATOM   3479 C  CZ  . PHE C 1 269 ? 26.77079  -2.27600  34.53920  1.000 46.58458  ? 269 PHE C CZ  1 
ATOM   3480 N  N   . ARG C 1 270 ? 20.97487  -2.23276  38.22863  1.000 33.34259  ? 270 ARG C N   1 
ATOM   3481 C  CA  . ARG C 1 270 ? 19.68765  -2.41198  38.88823  1.000 33.42740  ? 270 ARG C CA  1 
ATOM   3482 C  C   . ARG C 1 270 ? 19.75316  -3.39918  40.04521  1.000 43.47124  ? 270 ARG C C   1 
ATOM   3483 O  O   . ARG C 1 270 ? 20.45348  -4.40980  39.97220  1.000 35.49096  ? 270 ARG C O   1 
ATOM   3484 C  CB  . ARG C 1 270 ? 18.66483  -2.89476  37.86693  1.000 32.31421  ? 270 ARG C CB  1 
ATOM   3485 C  CG  . ARG C 1 270 ? 17.46288  -3.57935  38.47060  1.000 32.55209  ? 270 ARG C CG  1 
ATOM   3486 C  CD  . ARG C 1 270 ? 16.38979  -3.83417  37.40719  1.000 31.35978  ? 270 ARG C CD  1 
ATOM   3487 N  NE  . ARG C 1 270 ? 15.20289  -4.46065  37.99405  1.000 32.53197  ? 270 ARG C NE  1 
ATOM   3488 C  CZ  . ARG C 1 270 ? 14.80500  -5.71581  37.77924  1.000 55.58268  ? 270 ARG C CZ  1 
ATOM   3489 N  NH1 . ARG C 1 270 ? 15.47441  -6.51443  36.94696  1.000 42.76002  ? 270 ARG C NH1 1 
ATOM   3490 N  NH2 . ARG C 1 270 ? 13.70657  -6.16603  38.37727  1.000 46.07219  ? 270 ARG C NH2 1 
ATOM   3491 N  N   . SER C 1 271 ? 19.00596  -3.09211  41.11495  1.000 35.21156  ? 271 SER C N   1 
ATOM   3492 C  CA  . SER C 1 271 ? 18.68558  -4.04454  42.17585  1.000 36.18222  ? 271 SER C CA  1 
ATOM   3493 C  C   . SER C 1 271 ? 17.22103  -3.86487  42.55634  1.000 38.41618  ? 271 SER C C   1 
ATOM   3494 O  O   . SER C 1 271 ? 16.86905  -2.89594  43.24091  1.000 36.30635  ? 271 SER C O   1 
ATOM   3495 C  CB  . SER C 1 271 ? 19.57996  -3.83765  43.38909  1.000 40.85175  ? 271 SER C CB  1 
ATOM   3496 O  OG  . SER C 1 271 ? 19.18647  -4.69198  44.44939  1.000 41.21571  ? 271 SER C OG  1 
ATOM   3497 N  N   . GLY C 1 272 ? 16.37109  -4.80621  42.14590  1.000 38.22618  ? 272 GLY C N   1 
ATOM   3498 C  CA  . GLY C 1 272 ? 14.94958  -4.67176  42.44239  1.000 37.40683  ? 272 GLY C CA  1 
ATOM   3499 C  C   . GLY C 1 272 ? 14.39409  -3.47098  41.71800  1.000 35.91481  ? 272 GLY C C   1 
ATOM   3500 O  O   . GLY C 1 272 ? 14.54982  -3.33526  40.49601  1.000 38.60914  ? 272 GLY C O   1 
ATOM   3501 N  N   . ASN C 1 273 ? 13.70317  -2.60008  42.45693  1.000 36.56764  ? 273 ASN C N   1 
ATOM   3502 C  CA  . ASN C 1 273 ? 13.27746  -1.31507  41.92285  1.000 33.79451  ? 273 ASN C CA  1 
ATOM   3503 C  C   . ASN C 1 273 ? 14.24177  -0.20625  42.28009  1.000 37.76189  ? 273 ASN C C   1 
ATOM   3504 O  O   . ASN C 1 273 ? 13.91153  0.97076   42.11139  1.000 35.25783  ? 273 ASN C O   1 
ATOM   3505 C  CB  . ASN C 1 273 ? 11.87496  -0.95375  42.41469  1.000 33.91017  ? 273 ASN C CB  1 
ATOM   3506 C  CG  . ASN C 1 273 ? 10.80775  -1.66658  41.64697  1.000 34.04599  ? 273 ASN C CG  1 
ATOM   3507 O  OD1 . ASN C 1 273 ? 11.03716  -2.10819  40.52654  1.000 33.54035  ? 273 ASN C OD1 1 
ATOM   3508 N  ND2 . ASN C 1 273 ? 9.63265   -1.80547  42.24698  1.000 47.28196  ? 273 ASN C ND2 1 
ATOM   3509 N  N   . SER C 1 274 ? 15.42074  -0.55640  42.78067  1.000 35.06664  ? 274 SER C N   1 
ATOM   3510 C  CA  . SER C 1 274 ? 16.41348  0.43363   43.15878  1.000 36.28364  ? 274 SER C CA  1 
ATOM   3511 C  C   . SER C 1 274 ? 17.70701  0.13581   42.42616  1.000 39.87777  ? 274 SER C C   1 
ATOM   3512 O  O   . SER C 1 274 ? 17.68809  -0.55630  41.39980  1.000 35.77431  ? 274 SER C O   1 
ATOM   3513 C  CB  . SER C 1 274 ? 16.62069  0.42490   44.67845  1.000 36.92564  ? 274 SER C CB  1 
ATOM   3514 O  OG  . SER C 1 274 ? 17.44674  1.50329   45.06344  1.000 52.82292  ? 274 SER C OG  1 
ATOM   3515 N  N   . ASN C 1 275 ? 18.82319  0.63516   42.95419  1.000 38.89117  ? 275 ASN C N   1 
ATOM   3516 C  CA  . ASN C 1 275 ? 20.14870  0.41244   42.40086  1.000 36.10330  ? 275 ASN C CA  1 
ATOM   3517 C  C   . ASN C 1 275 ? 20.99622  -0.40221  43.35958  1.000 40.82319  ? 275 ASN C C   1 
ATOM   3518 O  O   . ASN C 1 275 ? 20.74342  -0.44602  44.56213  1.000 41.34189  ? 275 ASN C O   1 
ATOM   3519 C  CB  . ASN C 1 275 ? 20.86028  1.73049   42.10841  1.000 35.88156  ? 275 ASN C CB  1 
ATOM   3520 C  CG  . ASN C 1 275 ? 20.25973  2.45038   40.93962  1.000 38.75901  ? 275 ASN C CG  1 
ATOM   3521 O  OD1 . ASN C 1 275 ? 19.58733  1.83355   40.11379  1.000 37.66370  ? 275 ASN C OD1 1 
ATOM   3522 N  ND2 . ASN C 1 275 ? 20.51531  3.74600   40.83668  1.000 45.84137  ? 275 ASN C ND2 1 
ATOM   3523 N  N   . VAL C 1 276 ? 22.02265  -1.04064  42.80152  1.000 37.31383  ? 276 VAL C N   1 
ATOM   3524 C  CA  . VAL C 1 276 ? 23.01560  -1.68699  43.64330  1.000 38.49011  ? 276 VAL C CA  1 
ATOM   3525 C  C   . VAL C 1 276 ? 23.69329  -0.64269  44.53387  1.000 49.84837  ? 276 VAL C C   1 
ATOM   3526 O  O   . VAL C 1 276 ? 23.68990  0.55991   44.24886  1.000 44.30371  ? 276 VAL C O   1 
ATOM   3527 C  CB  . VAL C 1 276 ? 24.04398  -2.43996  42.78440  1.000 48.17634  ? 276 VAL C CB  1 
ATOM   3528 C  CG1 . VAL C 1 276 ? 23.36009  -3.50384  41.94416  1.000 41.45094  ? 276 VAL C CG1 1 
ATOM   3529 C  CG2 . VAL C 1 276 ? 24.80484  -1.47345  41.90353  1.000 40.55013  ? 276 VAL C CG2 1 
ATOM   3530 N  N   . SER C 1 277 ? 24.28557  -1.12074  45.63261  1.000 60.33969  ? 277 SER C N   1 
ATOM   3531 C  CA  . SER C 1 277 ? 24.73916  -0.21777  46.68826  1.000 73.93817  ? 277 SER C CA  1 
ATOM   3532 C  C   . SER C 1 277 ? 26.00686  0.55481   46.31175  1.000 76.34361  ? 277 SER C C   1 
ATOM   3533 O  O   . SER C 1 277 ? 26.21356  1.66574   46.81034  1.000 85.97863  ? 277 SER C O   1 
ATOM   3534 C  CB  . SER C 1 277 ? 24.94786  -0.99985  47.98706  1.000 72.87871  ? 277 SER C CB  1 
ATOM   3535 O  OG  . SER C 1 277 ? 25.75447  -2.14355  47.76947  1.000 80.45521  ? 277 SER C OG  1 
ATOM   3536 N  N   . THR C 1 278 ? 26.87731  -0.00257  45.47302  1.000 44.54561  ? 278 THR C N   1 
ATOM   3537 C  CA  . THR C 1 278 ? 28.14081  0.64068   45.13663  1.000 41.21023  ? 278 THR C CA  1 
ATOM   3538 C  C   . THR C 1 278 ? 28.13422  1.12782   43.69187  1.000 39.87218  ? 278 THR C C   1 
ATOM   3539 O  O   . THR C 1 278 ? 27.58261  0.46254   42.81243  1.000 41.00885  ? 278 THR C O   1 
ATOM   3540 C  CB  . THR C 1 278 ? 29.31434  -0.32585  45.35424  1.000 51.70047  ? 278 THR C CB  1 
ATOM   3541 O  OG1 . THR C 1 278 ? 29.33807  -0.74310  46.72672  1.000 61.51540  ? 278 THR C OG1 1 
ATOM   3542 C  CG2 . THR C 1 278 ? 30.64445  0.34586   45.04121  1.000 69.60674  ? 278 THR C CG2 1 
ATOM   3543 N  N   . ALA C 1 279 ? 28.75450  2.28673   43.45848  1.000 40.62910  ? 279 ALA C N   1 
ATOM   3544 C  CA  . ALA C 1 279 ? 28.82235  2.86153   42.11831  1.000 44.74519  ? 279 ALA C CA  1 
ATOM   3545 C  C   . ALA C 1 279 ? 29.64110  1.97185   41.19461  1.000 53.56233  ? 279 ALA C C   1 
ATOM   3546 O  O   . ALA C 1 279 ? 30.72126  1.50163   41.55962  1.000 48.96736  ? 279 ALA C O   1 
ATOM   3547 C  CB  . ALA C 1 279 ? 29.44461  4.25728   42.17090  1.000 52.29667  ? 279 ALA C CB  1 
ATOM   3548 N  N   . TYR C 1 280 ? 29.13841  1.75373   39.97998  1.000 39.77690  ? 280 TYR C N   1 
ATOM   3549 C  CA  . TYR C 1 280 ? 29.82397  0.83916   39.08115  1.000 41.52811  ? 280 TYR C CA  1 
ATOM   3550 C  C   . TYR C 1 280 ? 31.12594  1.44861   38.57504  1.000 39.23695  ? 280 TYR C C   1 
ATOM   3551 O  O   . TYR C 1 280 ? 31.28166  2.66726   38.49574  1.000 41.67361  ? 280 TYR C O   1 
ATOM   3552 C  CB  . TYR C 1 280 ? 28.92483  0.45150   37.90587  1.000 39.16327  ? 280 TYR C CB  1 
ATOM   3553 C  CG  . TYR C 1 280 ? 28.65897  1.52275   36.85883  1.000 41.62717  ? 280 TYR C CG  1 
ATOM   3554 C  CD1 . TYR C 1 280 ? 29.53221  1.72249   35.78460  1.000 33.55864  ? 280 TYR C CD1 1 
ATOM   3555 C  CD2 . TYR C 1 280 ? 27.50285  2.29432   36.90459  1.000 37.63736  ? 280 TYR C CD2 1 
ATOM   3556 C  CE1 . TYR C 1 280 ? 29.27760  2.69053   34.81648  1.000 33.87723  ? 280 TYR C CE1 1 
ATOM   3557 C  CE2 . TYR C 1 280 ? 27.23426  3.25822   35.91741  1.000 39.57149  ? 280 TYR C CE2 1 
ATOM   3558 C  CZ  . TYR C 1 280 ? 28.12390  3.45143   34.87836  1.000 43.55891  ? 280 TYR C CZ  1 
ATOM   3559 O  OH  . TYR C 1 280 ? 27.85230  4.39648   33.88921  1.000 35.54430  ? 280 TYR C OH  1 
ATOM   3560 N  N   . GLU C 1 281 ? 32.07358  0.57987   38.23292  1.000 50.96435  ? 281 GLU C N   1 
ATOM   3561 C  CA  . GLU C 1 281 ? 33.36171  1.02152   37.72427  1.000 40.74587  ? 281 GLU C CA  1 
ATOM   3562 C  C   . GLU C 1 281 ? 33.52159  0.84250   36.21851  1.000 36.01625  ? 281 GLU C C   1 
ATOM   3563 O  O   . GLU C 1 281 ? 34.33157  1.55680   35.61858  1.000 38.86975  ? 281 GLU C O   1 
ATOM   3564 C  CB  . GLU C 1 281 ? 34.50042  0.27976   38.44658  1.000 54.53184  ? 281 GLU C CB  1 
ATOM   3565 N  N   . LYS C 1 282 ? 32.78761  -0.08136  35.59684  1.000 40.05888  ? 282 LYS C N   1 
ATOM   3566 C  CA  . LYS C 1 282 ? 32.90763  -0.33604  34.15840  1.000 34.11832  ? 282 LYS C CA  1 
ATOM   3567 C  C   . LYS C 1 282 ? 31.53405  -0.62108  33.57932  1.000 47.31555  ? 282 LYS C C   1 
ATOM   3568 O  O   . LYS C 1 282 ? 30.78788  -1.43238  34.12717  1.000 38.00381  ? 282 LYS C O   1 
ATOM   3569 C  CB  . LYS C 1 282 ? 33.83335  -1.52380  33.86188  1.000 44.03013  ? 282 LYS C CB  1 
ATOM   3570 C  CG  . LYS C 1 282 ? 35.30657  -1.28251  34.18643  1.000 57.99865  ? 282 LYS C CG  1 
ATOM   3571 C  CD  . LYS C 1 282 ? 36.22175  -2.13184  33.30514  1.000 66.54644  ? 282 LYS C CD  1 
ATOM   3572 C  CE  . LYS C 1 282 ? 37.65244  -1.58707  33.30028  1.000 67.32013  ? 282 LYS C CE  1 
ATOM   3573 N  NZ  . LYS C 1 282 ? 38.58847  -2.38856  32.44514  1.000 70.37671  ? 282 LYS C NZ  1 
ATOM   3574 N  N   . ALA C 1 283 ? 31.22435  -0.01155  32.43833  1.000 31.70223  ? 283 ALA C N   1 
ATOM   3575 C  CA  . ALA C 1 283 ? 29.96988  -0.30852  31.75641  1.000 30.72603  ? 283 ALA C CA  1 
ATOM   3576 C  C   . ALA C 1 283 ? 30.17191  -0.19112  30.25977  1.000 30.86012  ? 283 ALA C C   1 
ATOM   3577 O  O   . ALA C 1 283 ? 29.28963  0.27862   29.52920  1.000 30.01626  ? 283 ALA C O   1 
ATOM   3578 C  CB  . ALA C 1 283 ? 28.84115  0.61886   32.20154  1.000 33.82140  ? 283 ALA C CB  1 
ATOM   3579 N  N   . ILE C 1 284 ? 31.32104  -0.67147  29.78077  1.000 31.04169  ? 284 ILE C N   1 
ATOM   3580 C  CA  . ILE C 1 284 ? 31.63822  -0.50840  28.36442  1.000 29.06350  ? 284 ILE C CA  1 
ATOM   3581 C  C   . ILE C 1 284 ? 30.65099  -1.27686  27.50748  1.000 32.84581  ? 284 ILE C C   1 
ATOM   3582 O  O   . ILE C 1 284 ? 30.37641  -0.89315  26.36340  1.000 26.97262  ? 284 ILE C O   1 
ATOM   3583 C  CB  . ILE C 1 284 ? 33.09510  -0.94756  28.09599  1.000 36.11042  ? 284 ILE C CB  1 
ATOM   3584 C  CG1 . ILE C 1 284 ? 34.05108  -0.08603  28.92182  1.000 40.08999  ? 284 ILE C CG1 1 
ATOM   3585 C  CG2 . ILE C 1 284 ? 33.42999  -0.80216  26.63497  1.000 41.50619  ? 284 ILE C CG2 1 
ATOM   3586 C  CD1 . ILE C 1 284 ? 35.53017  -0.51515  28.82260  1.000 48.81743  ? 284 ILE C CD1 1 
ATOM   3587 N  N   . GLY C 1 285 ? 30.10573  -2.37377  28.03339  1.000 31.34740  ? 285 GLY C N   1 
ATOM   3588 C  CA  . GLY C 1 285 ? 29.13804  -3.16960  27.28384  1.000 31.80754  ? 285 GLY C CA  1 
ATOM   3589 C  C   . GLY C 1 285 ? 27.81757  -2.46452  27.00766  1.000 39.82797  ? 285 GLY C C   1 
ATOM   3590 O  O   . GLY C 1 285 ? 27.01390  -2.98342  26.22958  1.000 32.68794  ? 285 GLY C O   1 
ATOM   3591 N  N   . PHE C 1 286 ? 27.57527  -1.31954  27.64198  1.000 27.95445  ? 286 PHE C N   1 
ATOM   3592 C  CA  . PHE C 1 286 ? 26.38280  -0.50120  27.44502  1.000 26.32413  ? 286 PHE C CA  1 
ATOM   3593 C  C   . PHE C 1 286 ? 26.65725  0.74601   26.61539  1.000 29.00382  ? 286 PHE C C   1 
ATOM   3594 O  O   . PHE C 1 286 ? 25.72379  1.50832   26.33791  1.000 25.88790  ? 286 PHE C O   1 
ATOM   3595 C  CB  . PHE C 1 286 ? 25.81955  -0.08589  28.81322  1.000 26.95921  ? 286 PHE C CB  1 
ATOM   3596 C  CG  . PHE C 1 286 ? 25.26293  -1.22344  29.61329  1.000 27.23465  ? 286 PHE C CG  1 
ATOM   3597 C  CD1 . PHE C 1 286 ? 26.10983  -2.03991  30.37261  1.000 28.76888  ? 286 PHE C CD1 1 
ATOM   3598 C  CD2 . PHE C 1 286 ? 23.90097  -1.48380  29.61952  1.000 28.28344  ? 286 PHE C CD2 1 
ATOM   3599 C  CE1 . PHE C 1 286 ? 25.59139  -3.09690  31.11369  1.000 43.39093  ? 286 PHE C CE1 1 
ATOM   3600 C  CE2 . PHE C 1 286 ? 23.38426  -2.53216  30.35226  1.000 28.78056  ? 286 PHE C CE2 1 
ATOM   3601 C  CZ  . PHE C 1 286 ? 24.23371  -3.34021  31.10301  1.000 29.42748  ? 286 PHE C CZ  1 
ATOM   3602 N  N   . MET C 1 287 ? 27.91786  0.97716   26.20998  1.000 26.98898  ? 287 MET C N   1 
ATOM   3603 C  CA  . MET C 1 287 ? 28.22438  2.19974   25.49425  1.000 27.42505  ? 287 MET C CA  1 
ATOM   3604 C  C   . MET C 1 287 ? 27.89882  2.04775   23.99811  1.000 23.35299  ? 287 MET C C   1 
ATOM   3605 O  O   . MET C 1 287 ? 28.00043  0.95159   23.44477  1.000 28.13643  ? 287 MET C O   1 
ATOM   3606 C  CB  . MET C 1 287 ? 29.69688  2.55501   25.66314  1.000 26.31292  ? 287 MET C CB  1 
ATOM   3607 C  CG  . MET C 1 287 ? 30.08165  2.90127   27.10710  1.000 22.19511  ? 287 MET C CG  1 
ATOM   3608 S  SD  . MET C 1 287 ? 29.23111  4.37343   27.65326  1.000 29.49959  ? 287 MET C SD  1 
ATOM   3609 C  CE  . MET C 1 287 ? 27.92774  3.77605   28.77013  1.000 26.17413  ? 287 MET C CE  1 
ATOM   3610 N  N   . PRO C 1 288 ? 27.52338  3.14065   23.33182  1.000 24.87418  ? 288 PRO C N   1 
ATOM   3611 C  CA  . PRO C 1 288 ? 27.29327  3.07738   21.87511  1.000 21.58918  ? 288 PRO C CA  1 
ATOM   3612 C  C   . PRO C 1 288 ? 28.58380  2.78363   21.12104  1.000 26.57369  ? 288 PRO C C   1 
ATOM   3613 O  O   . PRO C 1 288 ? 29.60989  3.42158   21.34242  1.000 25.03845  ? 288 PRO C O   1 
ATOM   3614 C  CB  . PRO C 1 288 ? 26.76540  4.47628   21.52643  1.000 24.01463  ? 288 PRO C CB  1 
ATOM   3615 C  CG  . PRO C 1 288 ? 26.36435  5.09135   22.84189  1.000 31.30218  ? 288 PRO C CG  1 
ATOM   3616 C  CD  . PRO C 1 288 ? 27.25531  4.47834   23.87911  1.000 25.33652  ? 288 PRO C CD  1 
ATOM   3617 N  N   . ASN C 1 289 ? 28.50706  1.83101   20.20145  1.000 25.60996  ? 289 ASN C N   1 
ATOM   3618 C  CA  . ASN C 1 289 ? 29.68256  1.34553   19.46833  1.000 28.89289  ? 289 ASN C CA  1 
ATOM   3619 C  C   . ASN C 1 289 ? 30.36356  2.46177   18.66823  1.000 29.03506  ? 289 ASN C C   1 
ATOM   3620 O  O   . ASN C 1 289 ? 29.71189  3.20487   17.93264  1.000 28.76463  ? 289 ASN C O   1 
ATOM   3621 C  CB  . ASN C 1 289 ? 29.22241  0.21631   18.54602  1.000 26.73868  ? 289 ASN C CB  1 
ATOM   3622 C  CG  . ASN C 1 289 ? 30.36221  -0.46036  17.79227  1.000 28.40836  ? 289 ASN C CG  1 
ATOM   3623 O  OD1 . ASN C 1 289 ? 30.87973  0.07821   16.82753  1.000 33.29966  ? 289 ASN C OD1 1 
ATOM   3624 N  ND2 . ASN C 1 289 ? 30.68298  -1.68189  18.18212  1.000 31.56895  ? 289 ASN C ND2 1 
ATOM   3625 N  N   . LEU C 1 290 ? 31.68890  2.58033   18.81656  1.000 28.80983  ? 290 LEU C N   1 
ATOM   3626 C  CA  . LEU C 1 290 ? 32.42346  3.69101   18.22185  1.000 28.05061  ? 290 LEU C CA  1 
ATOM   3627 C  C   . LEU C 1 290 ? 32.68603  3.50056   16.74142  1.000 30.45775  ? 290 LEU C C   1 
ATOM   3628 O  O   . LEU C 1 290 ? 33.02031  4.47441   16.06289  1.000 30.95862  ? 290 LEU C O   1 
ATOM   3629 C  CB  . LEU C 1 290 ? 33.75438  3.89794   18.94951  1.000 27.71354  ? 290 LEU C CB  1 
ATOM   3630 C  CG  . LEU C 1 290 ? 33.54169  4.62647   20.26841  1.000 30.86257  ? 290 LEU C CG  1 
ATOM   3631 C  CD1 . LEU C 1 290 ? 34.81478  4.52996   21.11291  1.000 35.91767  ? 290 LEU C CD1 1 
ATOM   3632 C  CD2 . LEU C 1 290 ? 33.16124  6.07548   20.05301  1.000 30.71801  ? 290 LEU C CD2 1 
ATOM   3633 N  N   . VAL C 1 291 ? 32.59041  2.27229   16.24610  1.000 26.06730  ? 291 VAL C N   1 
ATOM   3634 C  CA  . VAL C 1 291 ? 32.67602  2.05234   14.79895  1.000 27.57888  ? 291 VAL C CA  1 
ATOM   3635 C  C   . VAL C 1 291 ? 31.35146  2.42270   14.14286  1.000 32.01140  ? 291 VAL C C   1 
ATOM   3636 O  O   . VAL C 1 291 ? 31.30969  3.07582   13.08370  1.000 35.13802  ? 291 VAL C O   1 
ATOM   3637 C  CB  . VAL C 1 291 ? 33.06424  0.59183   14.50388  1.000 32.59059  ? 291 VAL C CB  1 
ATOM   3638 C  CG1 . VAL C 1 291 ? 32.97648  0.28340   12.98325  1.000 29.92585  ? 291 VAL C CG1 1 
ATOM   3639 C  CG2 . VAL C 1 291 ? 34.47186  0.31547   15.02827  1.000 34.78133  ? 291 VAL C CG2 1 
ATOM   3640 N  N   . ALA C 1 292 ? 30.25833  2.01010   14.77018  1.000 28.04024  ? 292 ALA C N   1 
ATOM   3641 C  CA  . ALA C 1 292 ? 28.92094  2.30561   14.23937  1.000 24.94401  ? 292 ALA C CA  1 
ATOM   3642 C  C   . ALA C 1 292 ? 28.60004  3.79226   14.32651  1.000 34.53030  ? 292 ALA C C   1 
ATOM   3643 O  O   . ALA C 1 292 ? 28.02532  4.36532   13.39022  1.000 31.02729  ? 292 ALA C O   1 
ATOM   3644 C  CB  . ALA C 1 292 ? 27.88009  1.46594   14.97661  1.000 28.47956  ? 292 ALA C CB  1 
ATOM   3645 N  N   . TYR C 1 293 ? 29.03040  4.44374   15.40646  1.000 29.95532  ? 293 TYR C N   1 
ATOM   3646 C  CA  . TYR C 1 293 ? 28.68531  5.82835   15.71767  1.000 27.31128  ? 293 TYR C CA  1 
ATOM   3647 C  C   . TYR C 1 293 ? 29.97389  6.56877   16.05098  1.000 26.36128  ? 293 TYR C C   1 
ATOM   3648 O  O   . TYR C 1 293 ? 30.32233  6.73961   17.23012  1.000 28.68926  ? 293 TYR C O   1 
ATOM   3649 C  CB  . TYR C 1 293 ? 27.68880  5.89459   16.88973  1.000 24.38245  ? 293 TYR C CB  1 
ATOM   3650 C  CG  . TYR C 1 293 ? 26.59287  4.83878   16.85290  1.000 24.08594  ? 293 TYR C CG  1 
ATOM   3651 C  CD1 . TYR C 1 293 ? 25.67002  4.79662   15.80323  1.000 23.36485  ? 293 TYR C CD1 1 
ATOM   3652 C  CD2 . TYR C 1 293 ? 26.47845  3.88599   17.85833  1.000 28.23486  ? 293 TYR C CD2 1 
ATOM   3653 C  CE1 . TYR C 1 293 ? 24.63684  3.83828   15.76763  1.000 25.77392  ? 293 TYR C CE1 1 
ATOM   3654 C  CE2 . TYR C 1 293 ? 25.46945  2.91056   17.82693  1.000 26.64824  ? 293 TYR C CE2 1 
ATOM   3655 C  CZ  . TYR C 1 293 ? 24.54112  2.90720   16.79303  1.000 26.38550  ? 293 TYR C CZ  1 
ATOM   3656 O  OH  . TYR C 1 293 ? 23.55906  1.93846   16.77141  1.000 25.97562  ? 293 TYR C OH  1 
ATOM   3657 N  N   . PRO C 1 294 ? 30.71230  7.02011   15.03389  1.000 27.01470  ? 294 PRO C N   1 
ATOM   3658 C  CA  . PRO C 1 294 ? 32.02892  7.62257   15.27083  1.000 30.05629  ? 294 PRO C CA  1 
ATOM   3659 C  C   . PRO C 1 294 ? 31.93835  8.99111   15.91876  1.000 32.32573  ? 294 PRO C C   1 
ATOM   3660 O  O   . PRO C 1 294 ? 30.95495  9.72405   15.75433  1.000 35.58170  ? 294 PRO C O   1 
ATOM   3661 C  CB  . PRO C 1 294 ? 32.62151  7.74564   13.85991  1.000 35.01497  ? 294 PRO C CB  1 
ATOM   3662 C  CG  . PRO C 1 294 ? 31.81686  6.83599   13.01446  1.000 35.01210  ? 294 PRO C CG  1 
ATOM   3663 C  CD  . PRO C 1 294 ? 30.43906  6.80727   13.60622  1.000 35.98554  ? 294 PRO C CD  1 
ATOM   3664 N  N   . LYS C 1 295 ? 33.00430  9.33784   16.63665  1.000 31.58896  ? 295 LYS C N   1 
ATOM   3665 C  CA  . LYS C 1 295 ? 33.12217  10.63832  17.26602  1.000 30.41404  ? 295 LYS C CA  1 
ATOM   3666 C  C   . LYS C 1 295 ? 33.19447  11.74872  16.21586  1.000 51.61861  ? 295 LYS C C   1 
ATOM   3667 O  O   . LYS C 1 295 ? 33.48670  11.48614  15.04314  1.000 38.75129  ? 295 LYS C O   1 
ATOM   3668 C  CB  . LYS C 1 295 ? 34.35926  10.66453  18.15866  1.000 38.89705  ? 295 LYS C CB  1 
ATOM   3669 C  CG  . LYS C 1 295 ? 34.29474  9.68296   19.31300  1.000 61.73845  ? 295 LYS C CG  1 
ATOM   3670 C  CD  . LYS C 1 295 ? 34.24987  10.39335  20.65326  1.000 73.52684  ? 295 LYS C CD  1 
ATOM   3671 C  CE  . LYS C 1 295 ? 32.86683  10.93034  20.98190  1.000 63.49488  ? 295 LYS C CE  1 
ATOM   3672 N  NZ  . LYS C 1 295 ? 32.87160  11.62368  22.31447  1.000 61.66097  ? 295 LYS C NZ  1 
ATOM   3673 N  N   . PRO C 1 296 ? 32.90379  12.99859  16.60922  1.000 43.96049  ? 296 PRO C N   1 
ATOM   3674 C  CA  . PRO C 1 296 ? 32.93235  14.10433  15.63914  1.000 57.57689  ? 296 PRO C CA  1 
ATOM   3675 C  C   . PRO C 1 296 ? 34.32612  14.28930  15.06184  1.000 43.28724  ? 296 PRO C C   1 
ATOM   3676 O  O   . PRO C 1 296 ? 35.32352  14.10496  15.74977  1.000 39.09404  ? 296 PRO C O   1 
ATOM   3677 C  CB  . PRO C 1 296 ? 32.52711  15.32554  16.47319  1.000 57.61461  ? 296 PRO C CB  1 
ATOM   3678 C  CG  . PRO C 1 296 ? 31.83901  14.77142  17.68135  1.000 53.32097  ? 296 PRO C CG  1 
ATOM   3679 C  CD  . PRO C 1 296 ? 32.52255  13.46487  17.95779  1.000 53.07144  ? 296 PRO C CD  1 
ATOM   3680 N  N   . SER C 1 297 ? 34.38829  14.68712  13.79776  1.000 41.27653  ? 297 SER C N   1 
ATOM   3681 C  CA  . SER C 1 297 ? 35.66343  14.98298  13.16517  1.000 49.19327  ? 297 SER C CA  1 
ATOM   3682 C  C   . SER C 1 297 ? 35.43095  16.03461  12.08827  1.000 61.82602  ? 297 SER C C   1 
ATOM   3683 O  O   . SER C 1 297 ? 34.39656  16.70999  12.07025  1.000 64.42114  ? 297 SER C O   1 
ATOM   3684 C  CB  . SER C 1 297 ? 36.28016  13.70606  12.57835  1.000 55.41074  ? 297 SER C CB  1 
ATOM   3685 O  OG  . SER C 1 297 ? 35.48653  13.27504  11.48565  1.000 57.06282  ? 297 SER C OG  1 
ATOM   3686 N  N   . ASN C 1 298 ? 36.39054  16.15418  11.17550  1.000 89.26707  ? 298 ASN C N   1 
ATOM   3687 C  CA  . ASN C 1 298 ? 36.26719  17.00021  9.99871   1.000 101.39209 ? 298 ASN C CA  1 
ATOM   3688 C  C   . ASN C 1 298 ? 35.84095  16.22052  8.76095   1.000 105.31961 ? 298 ASN C C   1 
ATOM   3689 O  O   . ASN C 1 298 ? 35.63854  16.82479  7.70275   1.000 106.80543 ? 298 ASN C O   1 
ATOM   3690 C  CB  . ASN C 1 298 ? 37.59324  17.71527  9.73103   1.000 102.93224 ? 298 ASN C CB  1 
ATOM   3691 C  CG  . ASN C 1 298 ? 38.75861  16.75463  9.65088   1.000 113.73286 ? 298 ASN C CG  1 
ATOM   3692 O  OD1 . ASN C 1 298 ? 38.62041  15.56733  9.95025   1.000 117.02236 ? 298 ASN C OD1 1 
ATOM   3693 N  ND2 . ASN C 1 298 ? 39.91877  17.26327  9.25773   1.000 120.95597 ? 298 ASN C ND2 1 
ATOM   3694 N  N   . SER C 1 299 ? 35.70453  14.89917  8.86466   1.000 94.28958  ? 299 SER C N   1 
ATOM   3695 C  CA  . SER C 1 299 ? 35.26499  14.08441  7.74279   1.000 94.89468  ? 299 SER C CA  1 
ATOM   3696 C  C   . SER C 1 299 ? 33.74011  14.11315  7.64040   1.000 88.82784  ? 299 SER C C   1 
ATOM   3697 O  O   . SER C 1 299 ? 33.05245  14.82489  8.38204   1.000 76.70937  ? 299 SER C O   1 
ATOM   3698 C  CB  . SER C 1 299 ? 35.76902  12.65242  7.89438   1.000 93.23003  ? 299 SER C CB  1 
ATOM   3699 O  OG  . SER C 1 299 ? 34.92115  11.92327  8.75960   1.000 100.46428 ? 299 SER C OG  1 
ATOM   3700 N  N   . LYS C 1 300 ? 33.19761  13.32082  6.71405   1.000 73.04561  ? 300 LYS C N   1 
ATOM   3701 C  CA  . LYS C 1 300 ? 31.75634  13.33022  6.49917   1.000 77.71017  ? 300 LYS C CA  1 
ATOM   3702 C  C   . LYS C 1 300 ? 31.06529  12.73781  7.72210   1.000 65.03360  ? 300 LYS C C   1 
ATOM   3703 O  O   . LYS C 1 300 ? 31.44966  11.67207  8.21582   1.000 62.00962  ? 300 LYS C O   1 
ATOM   3704 C  CB  . LYS C 1 300 ? 31.38011  12.54756  5.23649   1.000 69.63642  ? 300 LYS C CB  1 
ATOM   3705 C  CG  . LYS C 1 300 ? 29.87216  12.50268  4.97147   1.000 72.48996  ? 300 LYS C CG  1 
ATOM   3706 C  CD  . LYS C 1 300 ? 29.49698  11.51045  3.86918   1.000 80.27961  ? 300 LYS C CD  1 
ATOM   3707 C  CE  . LYS C 1 300 ? 29.43662  12.15276  2.48800   1.000 80.87399  ? 300 LYS C CE  1 
ATOM   3708 N  NZ  . LYS C 1 300 ? 29.00445  11.18639  1.43778   1.000 70.05396  ? 300 LYS C NZ  1 
ATOM   3709 N  N   . LYS C 1 301 ? 30.05549  13.44094  8.21745   1.000 52.31543  ? 301 LYS C N   1 
ATOM   3710 C  CA  . LYS C 1 301 ? 29.25385  12.96904  9.33516   1.000 45.57339  ? 301 LYS C CA  1 
ATOM   3711 C  C   . LYS C 1 301 ? 28.02125  12.23723  8.80281   1.000 42.98597  ? 301 LYS C C   1 
ATOM   3712 O  O   . LYS C 1 301 ? 27.30908  12.76902  7.94758   1.000 49.16140  ? 301 LYS C O   1 
ATOM   3713 C  CB  . LYS C 1 301 ? 28.87203  14.15740  10.22063  1.000 43.91389  ? 301 LYS C CB  1 
ATOM   3714 C  CG  . LYS C 1 301 ? 28.36774  13.78983  11.60455  1.000 59.53596  ? 301 LYS C CG  1 
ATOM   3715 C  CD  . LYS C 1 301 ? 26.88631  13.53536  11.56024  1.000 52.50497  ? 301 LYS C CD  1 
ATOM   3716 C  CE  . LYS C 1 301 ? 26.29846  13.26027  12.91879  1.000 54.70937  ? 301 LYS C CE  1 
ATOM   3717 N  NZ  . LYS C 1 301 ? 24.83717  12.94337  12.73890  1.000 45.40138  ? 301 LYS C NZ  1 
ATOM   3718 N  N   . TYR C 1 302 ? 27.79002  11.01059  9.28106   1.000 41.70541  ? 302 TYR C N   1 
ATOM   3719 C  CA  . TYR C 1 302 ? 26.68170  10.18847  8.80570   1.000 52.53525  ? 302 TYR C CA  1 
ATOM   3720 C  C   . TYR C 1 302 ? 25.53485  10.12181  9.81384   1.000 29.68645  ? 302 TYR C C   1 
ATOM   3721 O  O   . TYR C 1 302 ? 25.71876  10.13607  11.02888  1.000 43.44435  ? 302 TYR C O   1 
ATOM   3722 C  CB  . TYR C 1 302 ? 27.12283  8.76523   8.45255   1.000 40.91502  ? 302 TYR C CB  1 
ATOM   3723 C  CG  . TYR C 1 302 ? 27.80187  8.62669   7.09540   1.000 51.90917  ? 302 TYR C CG  1 
ATOM   3724 C  CD1 . TYR C 1 302 ? 27.08159  8.80406   5.90442   1.000 48.50609  ? 302 TYR C CD1 1 
ATOM   3725 C  CD2 . TYR C 1 302 ? 29.14986  8.29312   7.00448   1.000 58.08963  ? 302 TYR C CD2 1 
ATOM   3726 C  CE1 . TYR C 1 302 ? 27.69891  8.66568   4.66560   1.000 56.15724  ? 302 TYR C CE1 1 
ATOM   3727 C  CE2 . TYR C 1 302 ? 29.77342  8.15178   5.77606   1.000 46.57411  ? 302 TYR C CE2 1 
ATOM   3728 C  CZ  . TYR C 1 302 ? 29.04550  8.33525   4.60823   1.000 65.30491  ? 302 TYR C CZ  1 
ATOM   3729 O  OH  . TYR C 1 302 ? 29.67338  8.20206   3.38293   1.000 53.98303  ? 302 TYR C OH  1 
ATOM   3730 N  N   . ALA C 1 303 ? 24.33708  10.02103  9.26851   1.000 27.09282  ? 303 ALA C N   1 
ATOM   3731 C  CA  . ALA C 1 303 ? 23.09088  10.05731  10.01498  1.000 25.49756  ? 303 ALA C CA  1 
ATOM   3732 C  C   . ALA C 1 303 ? 22.79174  8.79010   10.81208  1.000 23.50044  ? 303 ALA C C   1 
ATOM   3733 O  O   . ALA C 1 303 ? 21.83570  8.79553   11.57997  1.000 22.66211  ? 303 ALA C O   1 
ATOM   3734 C  CB  . ALA C 1 303 ? 21.94933  10.32432  9.05003   1.000 27.44459  ? 303 ALA C CB  1 
ATOM   3735 N  N   . ARG C 1 304 ? 23.54466  7.70126   10.63050  1.000 24.72470  ? 304 ARG C N   1 
ATOM   3736 C  CA  . ARG C 1 304 ? 23.15184  6.50435   11.35754  1.000 25.65606  ? 304 ARG C CA  1 
ATOM   3737 C  C   . ARG C 1 304 ? 23.36368  6.62428   12.86072  1.000 25.67723  ? 304 ARG C C   1 
ATOM   3738 O  O   . ARG C 1 304 ? 22.79103  5.81366   13.60017  1.000 26.02647  ? 304 ARG C O   1 
ATOM   3739 C  CB  . ARG C 1 304 ? 23.91052  5.29262   10.82319  1.000 36.97162  ? 304 ARG C CB  1 
ATOM   3740 C  CG  . ARG C 1 304 ? 25.37877  5.41365   10.95258  1.000 45.86064  ? 304 ARG C CG  1 
ATOM   3741 C  CD  . ARG C 1 304 ? 26.04883  4.17207   10.40888  1.000 51.53633  ? 304 ARG C CD  1 
ATOM   3742 N  NE  . ARG C 1 304 ? 27.47932  4.26679   10.61630  1.000 45.15385  ? 304 ARG C NE  1 
ATOM   3743 C  CZ  . ARG C 1 304 ? 28.32676  3.29571   10.32862  1.000 63.49195  ? 304 ARG C CZ  1 
ATOM   3744 N  NH1 . ARG C 1 304 ? 27.86291  2.15443   9.82408   1.000 62.47212  ? 304 ARG C NH1 1 
ATOM   3745 N  NH2 . ARG C 1 304 ? 29.62591  3.46694   10.54851  1.000 53.90278  ? 304 ARG C NH2 1 
ATOM   3746 N  N   . ASP C 1 305 ? 24.11387  7.63099   13.33175  1.000 22.39281  ? 305 ASP C N   1 
ATOM   3747 C  CA  . ASP C 1 305 ? 24.18559  7.83631   14.78539  1.000 23.07926  ? 305 ASP C CA  1 
ATOM   3748 C  C   . ASP C 1 305 ? 22.96797  8.57119   15.37658  1.000 26.46804  ? 305 ASP C C   1 
ATOM   3749 O  O   . ASP C 1 305 ? 23.03590  8.95558   16.54776  1.000 23.28877  ? 305 ASP C O   1 
ATOM   3750 C  CB  . ASP C 1 305 ? 25.47201  8.57166   15.16755  1.000 25.57227  ? 305 ASP C CB  1 
ATOM   3751 C  CG  . ASP C 1 305 ? 25.61016  9.94206   14.51560  1.000 34.25159  ? 305 ASP C CG  1 
ATOM   3752 O  OD1 . ASP C 1 305 ? 24.65514  10.46244  13.91628  1.000 37.12674  ? 305 ASP C OD1 1 
ATOM   3753 O  OD2 . ASP C 1 305 ? 26.71697  10.50991  14.61717  1.000 35.14788  ? 305 ASP C OD2 1 
ATOM   3754 N  N   . ILE C 1 306 ? 21.87233  8.74971   14.63232  1.000 19.96540  ? 306 ILE C N   1 
ATOM   3755 C  CA  . ILE C 1 306 ? 20.65538  9.42372   15.12669  1.000 19.92887  ? 306 ILE C CA  1 
ATOM   3756 C  C   . ILE C 1 306 ? 19.48599  8.44563   15.09317  1.000 27.75808  ? 306 ILE C C   1 
ATOM   3757 O  O   . ILE C 1 306 ? 19.37009  7.64875   14.15840  1.000 22.53229  ? 306 ILE C O   1 
ATOM   3758 C  CB  . ILE C 1 306 ? 20.32968  10.67195  14.27384  1.000 21.05156  ? 306 ILE C CB  1 
ATOM   3759 C  CG1 . ILE C 1 306 ? 21.40721  11.74236  14.45580  1.000 24.46325  ? 306 ILE C CG1 1 
ATOM   3760 C  CG2 . ILE C 1 306 ? 18.93951  11.24630  14.63373  1.000 20.77599  ? 306 ILE C CG2 1 
ATOM   3761 C  CD1 . ILE C 1 306 ? 21.34858  12.79463  13.33493  1.000 30.36233  ? 306 ILE C CD1 1 
ATOM   3762 N  N   . VAL C 1 307 ? 18.62507  8.49405   16.11847  1.000 20.22558  ? 307 VAL C N   1 
ATOM   3763 C  CA  . VAL C 1 307 ? 17.31462  7.85687   16.08864  1.000 20.19854  ? 307 VAL C CA  1 
ATOM   3764 C  C   . VAL C 1 307 ? 16.30113  8.94386   16.38851  1.000 23.19204  ? 307 VAL C C   1 
ATOM   3765 O  O   . VAL C 1 307 ? 16.44198  9.66877   17.37895  1.000 25.52461  ? 307 VAL C O   1 
ATOM   3766 C  CB  . VAL C 1 307 ? 17.17704  6.71655   17.12012  1.000 26.68343  ? 307 VAL C CB  1 
ATOM   3767 C  CG1 . VAL C 1 307 ? 15.74423  6.11136   17.07250  1.000 25.55242  ? 307 VAL C CG1 1 
ATOM   3768 C  CG2 . VAL C 1 307 ? 18.24189  5.67204   16.94406  1.000 33.32668  ? 307 VAL C CG2 1 
ATOM   3769 N  N   . TYR C 1 308 ? 15.26627  9.04154   15.56423  1.000 17.84008  ? 308 TYR C N   1 
ATOM   3770 C  CA  . TYR C 1 308 ? 14.15913  9.94520   15.82307  1.000 18.02756  ? 308 TYR C CA  1 
ATOM   3771 C  C   . TYR C 1 308 ? 12.93108  9.19041   16.30660  1.000 27.31067  ? 308 TYR C C   1 
ATOM   3772 O  O   . TYR C 1 308 ? 12.59079  8.12559   15.78203  1.000 23.28961  ? 308 TYR C O   1 
ATOM   3773 C  CB  . TYR C 1 308 ? 13.73726  10.66868  14.55473  1.000 22.34526  ? 308 TYR C CB  1 
ATOM   3774 C  CG  . TYR C 1 308 ? 14.57083  11.84349  14.19116  1.000 20.86851  ? 308 TYR C CG  1 
ATOM   3775 C  CD1 . TYR C 1 308 ? 14.37965  13.08298  14.82848  1.000 25.41756  ? 308 TYR C CD1 1 
ATOM   3776 C  CD2 . TYR C 1 308 ? 15.51363  11.73881  13.18575  1.000 18.28299  ? 308 TYR C CD2 1 
ATOM   3777 C  CE1 . TYR C 1 308 ? 15.15823  14.18566  14.46456  1.000 25.06940  ? 308 TYR C CE1 1 
ATOM   3778 C  CE2 . TYR C 1 308 ? 16.29432  12.81776  12.83700  1.000 22.21934  ? 308 TYR C CE2 1 
ATOM   3779 C  CZ  . TYR C 1 308 ? 16.10171  14.03396  13.46501  1.000 21.80540  ? 308 TYR C CZ  1 
ATOM   3780 O  OH  . TYR C 1 308 ? 16.88752  15.09464  13.06609  1.000 29.43711  ? 308 TYR C OH  1 
ATOM   3781 N  N   . GLY C 1 309 ? 12.21414  9.79084   17.24658  1.000 19.75805  ? 309 GLY C N   1 
ATOM   3782 C  CA  . GLY C 1 309 ? 10.90958  9.29282   17.61771  1.000 19.36756  ? 309 GLY C CA  1 
ATOM   3783 C  C   . GLY C 1 309 ? 10.00064  10.46447  17.94690  1.000 24.57756  ? 309 GLY C C   1 
ATOM   3784 O  O   . GLY C 1 309 ? 10.44118  11.61263  18.01603  1.000 26.24991  ? 309 GLY C O   1 
ATOM   3785 N  N   . THR C 1 310 ? 8.71943   10.17059  18.09235  1.000 20.38690  ? 310 THR C N   1 
ATOM   3786 C  CA  . THR C 1 310 ? 7.74981   11.18236  18.49763  1.000 19.33787  ? 310 THR C CA  1 
ATOM   3787 C  C   . THR C 1 310 ? 7.14774   10.73182  19.81586  1.000 26.46014  ? 310 THR C C   1 
ATOM   3788 O  O   . THR C 1 310 ? 6.67986   9.59234   19.91893  1.000 24.72430  ? 310 THR C O   1 
ATOM   3789 C  CB  . THR C 1 310 ? 6.64297   11.35409  17.44413  1.000 27.20284  ? 310 THR C CB  1 
ATOM   3790 O  OG1 . THR C 1 310 ? 7.23815   11.69361  16.18359  1.000 25.85792  ? 310 THR C OG1 1 
ATOM   3791 C  CG2 . THR C 1 310 ? 5.63481   12.47934  17.83524  1.000 25.86974  ? 310 THR C CG2 1 
ATOM   3792 N  N   . ILE C 1 311 ? 7.14133   11.61343  20.82094  1.000 20.43571  ? 311 ILE C N   1 
ATOM   3793 C  CA  . ILE C 1 311 ? 6.40436   11.33084  22.04386  1.000 18.88262  ? 311 ILE C CA  1 
ATOM   3794 C  C   . ILE C 1 311 ? 5.30630   12.38611  22.18628  1.000 18.53436  ? 311 ILE C C   1 
ATOM   3795 O  O   . ILE C 1 311 ? 5.20734   13.31659  21.38183  1.000 24.55086  ? 311 ILE C O   1 
ATOM   3796 C  CB  . ILE C 1 311 ? 7.30826   11.26350  23.29644  1.000 18.16672  ? 311 ILE C CB  1 
ATOM   3797 C  CG1 . ILE C 1 311 ? 8.29695   12.43558  23.41626  1.000 21.85924  ? 311 ILE C CG1 1 
ATOM   3798 C  CG2 . ILE C 1 311 ? 8.11453   9.93116   23.26177  1.000 22.97834  ? 311 ILE C CG2 1 
ATOM   3799 C  CD1 . ILE C 1 311 ? 7.64170   13.76628  23.80058  1.000 30.26856  ? 311 ILE C CD1 1 
ATOM   3800 N  N   . TYR C 1 312 ? 4.44691   12.21497  23.20628  1.000 20.22902  ? 312 TYR C N   1 
ATOM   3801 C  CA  . TYR C 1 312 ? 3.23623   13.02753  23.31859  1.000 15.50586  ? 312 TYR C CA  1 
ATOM   3802 C  C   . TYR C 1 312 ? 3.13835   13.62915  24.71424  1.000 19.54992  ? 312 TYR C C   1 
ATOM   3803 O  O   . TYR C 1 312 ? 3.22856   12.90897  25.71737  1.000 23.49845  ? 312 TYR C O   1 
ATOM   3804 C  CB  . TYR C 1 312 ? 1.98012   12.20729  22.96997  1.000 18.69354  ? 312 TYR C CB  1 
ATOM   3805 C  CG  . TYR C 1 312 ? 2.09085   11.83861  21.49644  1.000 19.08252  ? 312 TYR C CG  1 
ATOM   3806 C  CD1 . TYR C 1 312 ? 2.80098   10.70731  21.09681  1.000 21.80536  ? 312 TYR C CD1 1 
ATOM   3807 C  CD2 . TYR C 1 312 ? 1.51024   12.65389  20.53169  1.000 22.81591  ? 312 TYR C CD2 1 
ATOM   3808 C  CE1 . TYR C 1 312 ? 2.95522   10.40605  19.74085  1.000 23.32283  ? 312 TYR C CE1 1 
ATOM   3809 C  CE2 . TYR C 1 312 ? 1.63839   12.35657  19.19926  1.000 23.64311  ? 312 TYR C CE2 1 
ATOM   3810 C  CZ  . TYR C 1 312 ? 2.35776   11.23241  18.81675  1.000 24.50254  ? 312 TYR C CZ  1 
ATOM   3811 O  OH  . TYR C 1 312 ? 2.48046   10.95733  17.46910  1.000 29.64936  ? 312 TYR C OH  1 
ATOM   3812 N  N   . LEU C 1 313 ? 2.99246   14.94654  24.77387  1.000 18.98256  ? 313 LEU C N   1 
ATOM   3813 C  CA  . LEU C 1 313 ? 2.98182   15.63723  26.06695  1.000 18.28307  ? 313 LEU C CA  1 
ATOM   3814 C  C   . LEU C 1 313 ? 1.66016   15.39769  26.77396  1.000 21.32797  ? 313 LEU C C   1 
ATOM   3815 O  O   . LEU C 1 313 ? 0.58338   15.52022  26.18168  1.000 21.47583  ? 313 LEU C O   1 
ATOM   3816 C  CB  . LEU C 1 313 ? 3.23389   17.13233  25.86552  1.000 20.79951  ? 313 LEU C CB  1 
ATOM   3817 C  CG  . LEU C 1 313 ? 4.52118   17.45278  25.10133  1.000 26.37011  ? 313 LEU C CG  1 
ATOM   3818 C  CD1 . LEU C 1 313 ? 4.70532   18.98830  24.99192  1.000 28.53776  ? 313 LEU C CD1 1 
ATOM   3819 C  CD2 . LEU C 1 313 ? 5.76193   16.79071  25.75708  1.000 26.61261  ? 313 LEU C CD2 1 
ATOM   3820 N  N   . GLY C 1 314 ? 1.73991   15.02455  28.05706  1.000 22.67129  ? 314 GLY C N   1 
ATOM   3821 C  CA  . GLY C 1 314 ? 0.54076   14.75166  28.82029  1.000 23.40154  ? 314 GLY C CA  1 
ATOM   3822 C  C   . GLY C 1 314 ? -0.19457  13.54637  28.28655  1.000 24.64045  ? 314 GLY C C   1 
ATOM   3823 O  O   . GLY C 1 314 ? -1.34538  13.30797  28.65405  1.000 27.27246  ? 314 GLY C O   1 
ATOM   3824 N  N   . GLY C 1 315 ? 0.44840   12.79840  27.38786  1.000 24.75411  ? 315 GLY C N   1 
ATOM   3825 C  CA  . GLY C 1 315 ? -0.20628  11.65864  26.78720  1.000 25.46161  ? 315 GLY C CA  1 
ATOM   3826 C  C   . GLY C 1 315 ? -1.31416  12.00289  25.81522  1.000 23.74616  ? 315 GLY C C   1 
ATOM   3827 O  O   . GLY C 1 315 ? -2.05315  11.10285  25.40987  1.000 24.34791  ? 315 GLY C O   1 
ATOM   3828 N  N   . LYS C 1 316 ? -1.44074  13.29197  25.40437  1.000 24.53597  ? 316 LYS C N   1 
ATOM   3829 C  CA  . LYS C 1 316 ? -2.50238  13.71700  24.48634  1.000 20.03096  ? 316 LYS C CA  1 
ATOM   3830 C  C   . LYS C 1 316 ? -2.05305  13.55954  23.03860  1.000 18.40895  ? 316 LYS C C   1 
ATOM   3831 O  O   . LYS C 1 316 ? -0.94339  13.98918  22.68459  1.000 21.87384  ? 316 LYS C O   1 
ATOM   3832 C  CB  . LYS C 1 316 ? -2.86303  15.16593  24.73713  1.000 25.79461  ? 316 LYS C CB  1 
ATOM   3833 C  CG  . LYS C 1 316 ? -3.43692  15.38613  26.09600  1.000 27.58086  ? 316 LYS C CG  1 
ATOM   3834 C  CD  . LYS C 1 316 ? -3.97658  16.79873  26.19411  1.000 30.88301  ? 316 LYS C CD  1 
ATOM   3835 C  CE  . LYS C 1 316 ? -4.56233  17.07739  27.57239  1.000 67.34778  ? 316 LYS C CE  1 
ATOM   3836 N  NZ  . LYS C 1 316 ? -5.00875  18.50085  27.71613  1.000 82.49473  ? 316 LYS C NZ  1 
ATOM   3837 N  N   . PRO C 1 317 ? -2.86677  12.94054  22.17999  1.000 22.83466  ? 317 PRO C N   1 
ATOM   3838 C  CA  . PRO C 1 317 ? -2.37654  12.60531  20.82483  1.000 27.78601  ? 317 PRO C CA  1 
ATOM   3839 C  C   . PRO C 1 317 ? -2.17065  13.81094  19.94030  1.000 32.03506  ? 317 PRO C C   1 
ATOM   3840 O  O   . PRO C 1 317 ? -1.49861  13.69254  18.90793  1.000 26.64899  ? 317 PRO C O   1 
ATOM   3841 C  CB  . PRO C 1 317 ? -3.46866  11.66714  20.26786  1.000 26.14804  ? 317 PRO C CB  1 
ATOM   3842 C  CG  . PRO C 1 317 ? -4.69293  11.99596  21.07818  1.000 30.44944  ? 317 PRO C CG  1 
ATOM   3843 C  CD  . PRO C 1 317 ? -4.21378  12.40307  22.44671  1.000 28.32765  ? 317 PRO C CD  1 
ATOM   3844 N  N   . ASP C 1 318 ? -2.70492  14.96936  20.31294  1.000 24.63858  ? 318 ASP C N   1 
ATOM   3845 C  CA  . ASP C 1 318 ? -2.50172  16.16972  19.52546  1.000 24.48084  ? 318 ASP C CA  1 
ATOM   3846 C  C   . ASP C 1 318 ? -1.41731  17.07079  20.10941  1.000 25.70914  ? 318 ASP C C   1 
ATOM   3847 O  O   . ASP C 1 318 ? -1.30954  18.23200  19.71308  1.000 27.54450  ? 318 ASP C O   1 
ATOM   3848 C  CB  . ASP C 1 318 ? -3.84011  16.89697  19.36160  1.000 25.54001  ? 318 ASP C CB  1 
ATOM   3849 C  CG  . ASP C 1 318 ? -4.35516  17.47757  20.64845  1.000 43.35553  ? 318 ASP C CG  1 
ATOM   3850 O  OD1 . ASP C 1 318 ? -3.97070  17.02674  21.74559  1.000 32.58305  ? 318 ASP C OD1 1 
ATOM   3851 O  OD2 . ASP C 1 318 ? -5.22925  18.33765  20.55183  1.000 43.69669  ? 318 ASP C OD2 1 
ATOM   3852 N  N   . GLN C 1 319 ? -0.57526  16.54006  21.00608  1.000 22.02314  ? 319 GLN C N   1 
ATOM   3853 C  CA  . GLN C 1 319 ? 0.55165   17.27582  21.58035  1.000 21.41217  ? 319 GLN C CA  1 
ATOM   3854 C  C   . GLN C 1 319 ? 1.86804   16.54209  21.34727  1.000 18.08093  ? 319 GLN C C   1 
ATOM   3855 O  O   . GLN C 1 319 ? 2.59734   16.21499  22.29192  1.000 20.72750  ? 319 GLN C O   1 
ATOM   3856 C  CB  . GLN C 1 319 ? 0.29854   17.52783  23.07630  1.000 21.50753  ? 319 GLN C CB  1 
ATOM   3857 C  CG  . GLN C 1 319 ? -0.95011  18.38610  23.29542  1.000 22.70813  ? 319 GLN C CG  1 
ATOM   3858 C  CD  . GLN C 1 319 ? -1.27296  18.71173  24.74584  1.000 25.35136  ? 319 GLN C CD  1 
ATOM   3859 O  OE1 . GLN C 1 319 ? -0.77850  18.07104  25.69960  1.000 25.87810  ? 319 GLN C OE1 1 
ATOM   3860 N  NE2 . GLN C 1 319 ? -2.13825  19.68542  24.92219  1.000 22.01105  ? 319 GLN C NE2 1 
ATOM   3861 N  N   . PRO C 1 320 ? 2.23981   16.31548  20.08578  1.000 19.39684  ? 320 PRO C N   1 
ATOM   3862 C  CA  . PRO C 1 320 ? 3.52357   15.66875  19.80318  1.000 19.57490  ? 320 PRO C CA  1 
ATOM   3863 C  C   . PRO C 1 320 ? 4.71998   16.55931  20.11746  1.000 21.26054  ? 320 PRO C C   1 
ATOM   3864 O  O   . PRO C 1 320 ? 4.65670   17.79182  20.03209  1.000 23.33847  ? 320 PRO C O   1 
ATOM   3865 C  CB  . PRO C 1 320 ? 3.46149   15.41431  18.28884  1.000 20.68566  ? 320 PRO C CB  1 
ATOM   3866 C  CG  . PRO C 1 320 ? 2.57287   16.54591  17.76526  1.000 22.69106  ? 320 PRO C CG  1 
ATOM   3867 C  CD  . PRO C 1 320 ? 1.51250   16.68231  18.84747  1.000 25.30044  ? 320 PRO C CD  1 
ATOM   3868 N  N   . ALA C 1 321 ? 5.82568   15.90898  20.45690  1.000 20.70085  ? 321 ALA C N   1 
ATOM   3869 C  CA  . ALA C 1 321 ? 7.14318   16.52723  20.46450  1.000 22.12735  ? 321 ALA C CA  1 
ATOM   3870 C  C   . ALA C 1 321 ? 8.12598   15.49991  19.90454  1.000 23.16213  ? 321 ALA C C   1 
ATOM   3871 O  O   . ALA C 1 321 ? 7.93203   14.29281  20.05050  1.000 22.77241  ? 321 ALA C O   1 
ATOM   3872 C  CB  . ALA C 1 321 ? 7.57948   16.98696  21.87680  1.000 25.06783  ? 321 ALA C CB  1 
ATOM   3873 N  N   . VAL C 1 322 ? 9.17164   15.98049  19.29124  1.000 19.56685  ? 322 VAL C N   1 
ATOM   3874 C  CA  . VAL C 1 322 ? 10.15964  15.10009  18.66004  1.000 18.29274  ? 322 VAL C CA  1 
ATOM   3875 C  C   . VAL C 1 322 ? 11.25327  14.79790  19.67128  1.000 21.68221  ? 322 VAL C C   1 
ATOM   3876 O  O   . VAL C 1 322 ? 11.78271  15.71453  20.30494  1.000 23.26644  ? 322 VAL C O   1 
ATOM   3877 C  CB  . VAL C 1 322 ? 10.76119  15.76301  17.40384  1.000 22.19621  ? 322 VAL C CB  1 
ATOM   3878 C  CG1 . VAL C 1 322 ? 11.94623  14.92948  16.87347  1.000 27.25845  ? 322 VAL C CG1 1 
ATOM   3879 C  CG2 . VAL C 1 322 ? 9.66161   15.94191  16.34086  1.000 21.97049  ? 322 VAL C CG2 1 
ATOM   3880 N  N   . ILE C 1 323 ? 11.60946  13.51765  19.83224  1.000 21.29084  ? 323 ILE C N   1 
ATOM   3881 C  CA  . ILE C 1 323 ? 12.78725  13.16590  20.61663  1.000 19.24557  ? 323 ILE C CA  1 
ATOM   3882 C  C   . ILE C 1 323 ? 13.84620  12.68108  19.63385  1.000 23.58106  ? 323 ILE C C   1 
ATOM   3883 O  O   . ILE C 1 323 ? 13.62346  11.71894  18.89086  1.000 22.75164  ? 323 ILE C O   1 
ATOM   3884 C  CB  . ILE C 1 323 ? 12.49087  12.13072  21.71895  1.000 26.83111  ? 323 ILE C CB  1 
ATOM   3885 C  CG1 . ILE C 1 323 ? 13.80201  11.74401  22.43405  1.000 22.61971  ? 323 ILE C CG1 1 
ATOM   3886 C  CG2 . ILE C 1 323 ? 11.71869  10.90562  21.18877  1.000 26.77039  ? 323 ILE C CG2 1 
ATOM   3887 C  CD1 . ILE C 1 323 ? 13.53250  10.87403  23.60189  1.000 29.90119  ? 323 ILE C CD1 1 
ATOM   3888 N  N   . LYS C 1 324 ? 14.96843  13.38280  19.59953  1.000 20.95582  ? 324 LYS C N   1 
ATOM   3889 C  CA  . LYS C 1 324 ? 16.08514  13.06179  18.71380  1.000 20.60532  ? 324 LYS C CA  1 
ATOM   3890 C  C   . LYS C 1 324 ? 17.20655  12.54702  19.59701  1.000 21.34261  ? 324 LYS C C   1 
ATOM   3891 O  O   . LYS C 1 324 ? 17.72287  13.27892  20.44217  1.000 25.07330  ? 324 LYS C O   1 
ATOM   3892 C  CB  . LYS C 1 324 ? 16.53585  14.30177  17.93769  1.000 20.55852  ? 324 LYS C CB  1 
ATOM   3893 C  CG  . LYS C 1 324 ? 17.71503  14.06003  16.98253  1.000 21.55696  ? 324 LYS C CG  1 
ATOM   3894 C  CD  . LYS C 1 324 ? 18.20608  15.39303  16.44741  1.000 29.19068  ? 324 LYS C CD  1 
ATOM   3895 C  CE  . LYS C 1 324 ? 19.20321  15.17036  15.31337  1.000 41.13097  ? 324 LYS C CE  1 
ATOM   3896 N  NZ  . LYS C 1 324 ? 19.82046  16.47967  14.90673  1.000 43.43396  ? 324 LYS C NZ  1 
ATOM   3897 N  N   . THR C 1 325 ? 17.59007  11.30053  19.39619  1.000 19.80434  ? 325 THR C N   1 
ATOM   3898 C  CA  . THR C 1 325 ? 18.64015  10.68695  20.19659  1.000 21.54831  ? 325 THR C CA  1 
ATOM   3899 C  C   . THR C 1 325 ? 19.88157  10.56203  19.32519  1.000 24.66147  ? 325 THR C C   1 
ATOM   3900 O  O   . THR C 1 325 ? 19.79780  10.05604  18.20512  1.000 22.18025  ? 325 THR C O   1 
ATOM   3901 C  CB  . THR C 1 325 ? 18.18411  9.31221   20.70953  1.000 20.01999  ? 325 THR C CB  1 
ATOM   3902 O  OG1 . THR C 1 325 ? 16.95546  9.45436   21.46679  1.000 22.67657  ? 325 THR C OG1 1 
ATOM   3903 C  CG2 . THR C 1 325 ? 19.29814  8.66942   21.56097  1.000 23.79764  ? 325 THR C CG2 1 
ATOM   3904 N  N   . THR C 1 326 ? 21.02211  11.04708  19.81421  1.000 20.33848  ? 326 THR C N   1 
ATOM   3905 C  CA  . THR C 1 326 ? 22.25438  11.03091  19.02799  1.000 20.48756  ? 326 THR C CA  1 
ATOM   3906 C  C   . THR C 1 326 ? 23.35141  10.32386  19.81298  1.000 27.19342  ? 326 THR C C   1 
ATOM   3907 O  O   . THR C 1 326 ? 23.53892  10.60018  21.00206  1.000 24.66501  ? 326 THR C O   1 
ATOM   3908 C  CB  . THR C 1 326 ? 22.71887  12.48274  18.66479  1.000 28.94526  ? 326 THR C CB  1 
ATOM   3909 O  OG1 . THR C 1 326 ? 21.64553  13.20569  18.03513  1.000 27.45071  ? 326 THR C OG1 1 
ATOM   3910 C  CG2 . THR C 1 326 ? 23.94233  12.45367  17.72442  1.000 26.03504  ? 326 THR C CG2 1 
ATOM   3911 N  N   . PHE C 1 327 ? 24.11578  9.44802   19.13733  1.000 21.43824  ? 327 PHE C N   1 
ATOM   3912 C  CA  . PHE C 1 327 ? 25.18939  8.68137   19.78001  1.000 24.56943  ? 327 PHE C CA  1 
ATOM   3913 C  C   . PHE C 1 327 ? 26.57377  9.25076   19.44506  1.000 29.44708  ? 327 PHE C C   1 
ATOM   3914 O  O   . PHE C 1 327 ? 26.89260  9.51738   18.27409  1.000 25.29365  ? 327 PHE C O   1 
ATOM   3915 C  CB  . PHE C 1 327 ? 25.11272  7.20106   19.38195  1.000 20.80938  ? 327 PHE C CB  1 
ATOM   3916 C  CG  . PHE C 1 327 ? 23.77571  6.59894   19.65261  1.000 26.57424  ? 327 PHE C CG  1 
ATOM   3917 C  CD1 . PHE C 1 327 ? 23.29838  6.48364   20.96126  1.000 23.93201  ? 327 PHE C CD1 1 
ATOM   3918 C  CD2 . PHE C 1 327 ? 22.95678  6.21415   18.61321  1.000 27.33691  ? 327 PHE C CD2 1 
ATOM   3919 C  CE1 . PHE C 1 327 ? 22.03889  5.97068   21.21437  1.000 23.51206  ? 327 PHE C CE1 1 
ATOM   3920 C  CE2 . PHE C 1 327 ? 21.69327  5.68779   18.85316  1.000 26.27733  ? 327 PHE C CE2 1 
ATOM   3921 C  CZ  . PHE C 1 327 ? 21.21859  5.58419   20.16579  1.000 24.21178  ? 327 PHE C CZ  1 
ATOM   3922 N  N   . ASN C 1 328 ? 27.37664  9.47500   20.48617  1.000 21.61197  ? 328 ASN C N   1 
ATOM   3923 C  CA  . ASN C 1 328 ? 28.81365  9.74247   20.36924  1.000 25.56608  ? 328 ASN C CA  1 
ATOM   3924 C  C   . ASN C 1 328 ? 29.14164  11.00014  19.58646  1.000 28.11481  ? 328 ASN C C   1 
ATOM   3925 O  O   . ASN C 1 328 ? 30.18406  11.06630  18.94450  1.000 33.07149  ? 328 ASN C O   1 
ATOM   3926 C  CB  . ASN C 1 328 ? 29.54787  8.55426   19.73179  1.000 28.18004  ? 328 ASN C CB  1 
ATOM   3927 C  CG  . ASN C 1 328 ? 29.50564  7.32390   20.60687  1.000 29.40158  ? 328 ASN C CG  1 
ATOM   3928 O  OD1 . ASN C 1 328 ? 29.29114  7.43913   21.80782  1.000 27.12190  ? 328 ASN C OD1 1 
ATOM   3929 N  ND2 . ASN C 1 328 ? 29.68874  6.14149   20.01153  1.000 27.23332  ? 328 ASN C ND2 1 
ATOM   3930 N  N   . GLN C 1 329 ? 28.30961  12.03293  19.67509  1.000 27.24123  ? 329 GLN C N   1 
ATOM   3931 C  CA  . GLN C 1 329 ? 28.57543  13.25940  18.93639  1.000 26.63288  ? 329 GLN C CA  1 
ATOM   3932 C  C   . GLN C 1 329 ? 28.98723  14.42051  19.82892  1.000 34.65001  ? 329 GLN C C   1 
ATOM   3933 O  O   . GLN C 1 329 ? 29.15361  15.53352  19.33931  1.000 41.24602  ? 329 GLN C O   1 
ATOM   3934 C  CB  . GLN C 1 329 ? 27.34712  13.62919  18.10240  1.000 32.45964  ? 329 GLN C CB  1 
ATOM   3935 C  CG  . GLN C 1 329 ? 27.29026  12.84998  16.76893  1.000 35.88999  ? 329 GLN C CG  1 
ATOM   3936 C  CD  . GLN C 1 329 ? 28.43354  13.26323  15.81866  1.000 41.41974  ? 329 GLN C CD  1 
ATOM   3937 O  OE1 . GLN C 1 329 ? 29.36516  12.49682  15.57591  1.000 51.58171  ? 329 GLN C OE1 1 
ATOM   3938 N  NE2 . GLN C 1 329 ? 28.35362  14.48458  15.28329  1.000 39.00968  ? 329 GLN C NE2 1 
ATOM   3939 N  N   . GLU C 1 330 ? 29.20286  14.18020  21.10790  1.000 34.05490  ? 330 GLU C N   1 
ATOM   3940 C  CA  . GLU C 1 330 ? 29.69637  15.21419  21.99530  1.000 36.06054  ? 330 GLU C CA  1 
ATOM   3941 C  C   . GLU C 1 330 ? 31.20978  15.11484  22.09989  1.000 31.17165  ? 330 GLU C C   1 
ATOM   3942 O  O   . GLU C 1 330 ? 31.79206  14.04779  21.89678  1.000 40.22583  ? 330 GLU C O   1 
ATOM   3943 C  CB  . GLU C 1 330 ? 29.06159  15.06537  23.37117  1.000 31.08823  ? 330 GLU C CB  1 
ATOM   3944 C  CG  . GLU C 1 330 ? 27.54298  15.14256  23.34196  1.000 31.46540  ? 330 GLU C CG  1 
ATOM   3945 C  CD  . GLU C 1 330 ? 27.02780  16.52686  22.97502  1.000 46.65058  ? 330 GLU C CD  1 
ATOM   3946 O  OE1 . GLU C 1 330 ? 27.65943  17.53546  23.36388  1.000 46.78785  ? 330 GLU C OE1 1 
ATOM   3947 O  OE2 . GLU C 1 330 ? 25.99882  16.60690  22.27999  1.000 38.61517  ? 330 GLU C OE2 1 
ATOM   3948 N  N   . THR C 1 331 ? 31.84337  16.24170  22.37785  1.000 40.53607  ? 331 THR C N   1 
ATOM   3949 C  CA  . THR C 1 331 ? 33.27588  16.26262  22.63339  1.000 48.53366  ? 331 THR C CA  1 
ATOM   3950 C  C   . THR C 1 331 ? 33.52314  16.27522  24.13893  1.000 42.27760  ? 331 THR C C   1 
ATOM   3951 O  O   . THR C 1 331 ? 32.61243  16.49650  24.93399  1.000 40.53954  ? 331 THR C O   1 
ATOM   3952 C  CB  . THR C 1 331 ? 33.91753  17.47737  21.96091  1.000 52.57375  ? 331 THR C CB  1 
ATOM   3953 O  OG1 . THR C 1 331 ? 33.24615  18.66643  22.39611  1.000 52.37696  ? 331 THR C OG1 1 
ATOM   3954 C  CG2 . THR C 1 331 ? 33.80250  17.35594  20.44967  1.000 56.60707  ? 331 THR C CG2 1 
ATOM   3955 N  N   . GLY C 1 332 ? 34.77824  16.05020  24.52796  1.000 42.16986  ? 332 GLY C N   1 
ATOM   3956 C  CA  . GLY C 1 332 ? 35.09163  15.97643  25.94102  1.000 39.43790  ? 332 GLY C CA  1 
ATOM   3957 C  C   . GLY C 1 332 ? 34.67135  14.69087  26.62072  1.000 42.69985  ? 332 GLY C C   1 
ATOM   3958 O  O   . GLY C 1 332 ? 34.45475  14.68269  27.83388  1.000 48.11110  ? 332 GLY C O   1 
ATOM   3959 N  N   . CYS C 1 333 ? 34.54081  13.60056  25.87172  1.000 39.60049  ? 333 CYS C N   1 
ATOM   3960 C  CA  . CYS C 1 333 ? 34.12150  12.32442  26.43317  1.000 31.94626  ? 333 CYS C CA  1 
ATOM   3961 C  C   . CYS C 1 333 ? 34.54240  11.21964  25.47919  1.000 38.07455  ? 333 CYS C C   1 
ATOM   3962 O  O   . CYS C 1 333 ? 34.89749  11.47125  24.32610  1.000 41.79163  ? 333 CYS C O   1 
ATOM   3963 C  CB  . CYS C 1 333 ? 32.60415  12.30276  26.67196  1.000 29.36201  ? 333 CYS C CB  1 
ATOM   3964 S  SG  . CYS C 1 333 ? 31.69227  12.72225  25.14857  1.000 37.62404  ? 333 CYS C SG  1 
ATOM   3965 N  N   . GLU C 1 334 ? 34.47517  9.98177   25.96488  1.000 35.22874  ? 334 GLU C N   1 
ATOM   3966 C  CA  . GLU C 1 334 ? 34.70030  8.86257   25.05866  1.000 33.73117  ? 334 GLU C CA  1 
ATOM   3967 C  C   . GLU C 1 334 ? 33.41833  8.45099   24.35484  1.000 34.02028  ? 334 GLU C C   1 
ATOM   3968 O  O   . GLU C 1 334 ? 33.45852  8.06606   23.17751  1.000 32.11068  ? 334 GLU C O   1 
ATOM   3969 C  CB  . GLU C 1 334 ? 35.28417  7.65342   25.79804  1.000 33.92204  ? 334 GLU C CB  1 
ATOM   3970 C  CG  . GLU C 1 334 ? 36.80661  7.57330   25.74917  1.000 71.60322  ? 334 GLU C CG  1 
ATOM   3971 C  CD  . GLU C 1 334 ? 37.35466  7.56163   24.33256  1.000 63.40582  ? 334 GLU C CD  1 
ATOM   3972 O  OE1 . GLU C 1 334 ? 37.27032  6.51780   23.64683  1.000 59.49575  ? 334 GLU C OE1 1 
ATOM   3973 O  OE2 . GLU C 1 334 ? 37.85861  8.61594   23.90227  1.000 59.39804  ? 334 GLU C OE2 1 
ATOM   3974 N  N   . TYR C 1 335 ? 32.29078  8.53209   25.05878  1.000 28.48654  ? 335 TYR C N   1 
ATOM   3975 C  CA  . TYR C 1 335 ? 30.98600  8.12979   24.55075  1.000 27.68759  ? 335 TYR C CA  1 
ATOM   3976 C  C   . TYR C 1 335 ? 29.93324  9.14906   24.97789  1.000 31.08105  ? 335 TYR C C   1 
ATOM   3977 O  O   . TYR C 1 335 ? 30.10677  9.86594   25.96356  1.000 27.12006  ? 335 TYR C O   1 
ATOM   3978 C  CB  . TYR C 1 335 ? 30.56310  6.74328   25.07906  1.000 26.03347  ? 335 TYR C CB  1 
ATOM   3979 C  CG  . TYR C 1 335 ? 31.56493  5.62206   24.90667  1.000 30.28787  ? 335 TYR C CG  1 
ATOM   3980 C  CD1 . TYR C 1 335 ? 31.58980  4.85568   23.73132  1.000 26.41729  ? 335 TYR C CD1 1 
ATOM   3981 C  CD2 . TYR C 1 335 ? 32.47917  5.30739   25.91658  1.000 26.25675  ? 335 TYR C CD2 1 
ATOM   3982 C  CE1 . TYR C 1 335 ? 32.50544  3.80156   23.56597  1.000 29.51769  ? 335 TYR C CE1 1 
ATOM   3983 C  CE2 . TYR C 1 335 ? 33.40396  4.25992   25.75255  1.000 32.62030  ? 335 TYR C CE2 1 
ATOM   3984 C  CZ  . TYR C 1 335 ? 33.40976  3.52441   24.58357  1.000 35.80677  ? 335 TYR C CZ  1 
ATOM   3985 O  OH  . TYR C 1 335 ? 34.31735  2.50168   24.42768  1.000 36.43381  ? 335 TYR C OH  1 
ATOM   3986 N  N   . SER C 1 336 ? 28.81977  9.20324   24.24364  1.000 26.78285  ? 336 SER C N   1 
ATOM   3987 C  CA  . SER C 1 336 ? 27.72709  10.06419  24.69485  1.000 23.36293  ? 336 SER C CA  1 
ATOM   3988 C  C   . SER C 1 336 ? 26.39929  9.60103   24.13008  1.000 26.12525  ? 336 SER C C   1 
ATOM   3989 O  O   . SER C 1 336 ? 26.33052  8.99722   23.06030  1.000 25.15842  ? 336 SER C O   1 
ATOM   3990 C  CB  . SER C 1 336 ? 27.93233  11.53539  24.31735  1.000 28.44692  ? 336 SER C CB  1 
ATOM   3991 O  OG  . SER C 1 336 ? 28.02695  11.69527  22.89850  1.000 30.98513  ? 336 SER C OG  1 
ATOM   3992 N  N   . ILE C 1 337 ? 25.34144  9.89243   24.88668  1.000 24.02538  ? 337 ILE C N   1 
ATOM   3993 C  CA  . ILE C 1 337 ? 23.96919  9.74730   24.41456  1.000 22.31435  ? 337 ILE C CA  1 
ATOM   3994 C  C   . ILE C 1 337 ? 23.30803  11.08379  24.68004  1.000 28.26193  ? 337 ILE C C   1 
ATOM   3995 O  O   . ILE C 1 337 ? 23.28462  11.54372  25.82410  1.000 23.56862  ? 337 ILE C O   1 
ATOM   3996 C  CB  . ILE C 1 337 ? 23.22178  8.62038   25.15811  1.000 22.41564  ? 337 ILE C CB  1 
ATOM   3997 C  CG1 . ILE C 1 337 ? 23.93329  7.26710   24.97105  1.000 25.54843  ? 337 ILE C CG1 1 
ATOM   3998 C  CG2 . ILE C 1 337 ? 21.75697  8.55998   24.70928  1.000 22.72820  ? 337 ILE C CG2 1 
ATOM   3999 C  CD1 . ILE C 1 337 ? 23.44961  6.16604   25.98145  1.000 29.35616  ? 337 ILE C CD1 1 
ATOM   4000 N  N   . THR C 1 338 ? 22.77514  11.72470  23.65426  1.000 22.99888  ? 338 THR C N   1 
ATOM   4001 C  CA  . THR C 1 338 ? 22.07025  12.97228  23.93259  1.000 26.35601  ? 338 THR C CA  1 
ATOM   4002 C  C   . THR C 1 338 ? 20.64650  12.88995  23.42764  1.000 30.49793  ? 338 THR C C   1 
ATOM   4003 O  O   . THR C 1 338 ? 20.37526  12.28297  22.38691  1.000 24.80375  ? 338 THR C O   1 
ATOM   4004 C  CB  . THR C 1 338 ? 22.75876  14.19278  23.32692  1.000 34.07380  ? 338 THR C CB  1 
ATOM   4005 O  OG1 . THR C 1 338 ? 22.70402  14.10389  21.91780  1.000 33.61018  ? 338 THR C OG1 1 
ATOM   4006 C  CG2 . THR C 1 338 ? 24.22716  14.24106  23.75592  1.000 27.81692  ? 338 THR C CG2 1 
ATOM   4007 N  N   . PHE C 1 339 ? 19.74549  13.48547  24.19832  1.000 22.48365  ? 339 PHE C N   1 
ATOM   4008 C  CA  . PHE C 1 339 ? 18.33055  13.53134  23.89070  1.000 20.78678  ? 339 PHE C CA  1 
ATOM   4009 C  C   . PHE C 1 339 ? 17.98544  14.99042  23.64853  1.000 25.49318  ? 339 PHE C C   1 
ATOM   4010 O  O   . PHE C 1 339 ? 18.12233  15.82266  24.54825  1.000 29.70829  ? 339 PHE C O   1 
ATOM   4011 C  CB  . PHE C 1 339 ? 17.48081  12.96564  25.03784  1.000 22.25732  ? 339 PHE C CB  1 
ATOM   4012 C  CG  . PHE C 1 339 ? 17.81597  11.54726  25.40063  1.000 27.08644  ? 339 PHE C CG  1 
ATOM   4013 C  CD1 . PHE C 1 339 ? 17.42700  10.47769  24.58123  1.000 20.70626  ? 339 PHE C CD1 1 
ATOM   4014 C  CD2 . PHE C 1 339 ? 18.48897  11.26926  26.58370  1.000 26.06756  ? 339 PHE C CD2 1 
ATOM   4015 C  CE1 . PHE C 1 339 ? 17.72303  9.15437   24.93810  1.000 23.30406  ? 339 PHE C CE1 1 
ATOM   4016 C  CE2 . PHE C 1 339 ? 18.79389  9.95863   26.93994  1.000 26.05359  ? 339 PHE C CE2 1 
ATOM   4017 C  CZ  . PHE C 1 339 ? 18.40537  8.90351   26.12589  1.000 23.14628  ? 339 PHE C CZ  1 
ATOM   4018 N  N   . ASN C 1 340 ? 17.54498  15.29756  22.44193  1.000 25.86626  ? 340 ASN C N   1 
ATOM   4019 C  CA  . ASN C 1 340 ? 17.05917  16.62469  22.10576  1.000 20.82898  ? 340 ASN C CA  1 
ATOM   4020 C  C   . ASN C 1 340 ? 15.55007  16.54673  21.95526  1.000 27.80553  ? 340 ASN C C   1 
ATOM   4021 O  O   . ASN C 1 340 ? 15.04485  15.71685  21.18957  1.000 23.59730  ? 340 ASN C O   1 
ATOM   4022 C  CB  . ASN C 1 340 ? 17.66265  17.14860  20.80472  1.000 24.11205  ? 340 ASN C CB  1 
ATOM   4023 C  CG  . ASN C 1 340 ? 17.06371  18.47137  20.41639  1.000 34.16118  ? 340 ASN C CG  1 
ATOM   4024 O  OD1 . ASN C 1 340 ? 16.13774  18.52035  19.59642  1.000 34.04431  ? 340 ASN C OD1 1 
ATOM   4025 N  ND2 . ASN C 1 340 ? 17.52786  19.55216  21.05280  1.000 28.67923  ? 340 ASN C ND2 1 
ATOM   4026 N  N   . PHE C 1 341 ? 14.84280  17.38888  22.69516  1.000 20.48584  ? 341 PHE C N   1 
ATOM   4027 C  CA  . PHE C 1 341 ? 13.38451  17.46011  22.65319  1.000 21.91566  ? 341 PHE C CA  1 
ATOM   4028 C  C   . PHE C 1 341 ? 12.99228  18.74375  21.94365  1.000 27.88807  ? 341 PHE C C   1 
ATOM   4029 O  O   . PHE C 1 341 ? 13.49084  19.81267  22.30381  1.000 27.86760  ? 341 PHE C O   1 
ATOM   4030 C  CB  . PHE C 1 341 ? 12.78734  17.45140  24.07161  1.000 24.24753  ? 341 PHE C CB  1 
ATOM   4031 C  CG  . PHE C 1 341 ? 13.00415  16.17257  24.81919  1.000 26.07257  ? 341 PHE C CG  1 
ATOM   4032 C  CD1 . PHE C 1 341 ? 14.22553  15.89625  25.43240  1.000 22.66036  ? 341 PHE C CD1 1 
ATOM   4033 C  CD2 . PHE C 1 341 ? 12.01176  15.21091  24.85209  1.000 26.36776  ? 341 PHE C CD2 1 
ATOM   4034 C  CE1 . PHE C 1 341 ? 14.42418  14.69254  26.10783  1.000 27.09659  ? 341 PHE C CE1 1 
ATOM   4035 C  CE2 . PHE C 1 341 ? 12.21875  14.00926  25.51528  1.000 31.95069  ? 341 PHE C CE2 1 
ATOM   4036 C  CZ  . PHE C 1 341 ? 13.41422  13.75330  26.13408  1.000 21.25632  ? 341 PHE C CZ  1 
ATOM   4037 N  N   . SER C 1 342 ? 12.08425  18.65756  20.97313  1.000 21.30629  ? 342 SER C N   1 
ATOM   4038 C  CA  . SER C 1 342 ? 11.66768  19.86635  20.26287  1.000 20.40358  ? 342 SER C CA  1 
ATOM   4039 C  C   . SER C 1 342 ? 10.23333  19.70554  19.79107  1.000 25.10138  ? 342 SER C C   1 
ATOM   4040 O  O   . SER C 1 342 ? 9.70861   18.59546  19.68963  1.000 24.78082  ? 342 SER C O   1 
ATOM   4041 C  CB  . SER C 1 342 ? 12.57988  20.16831  19.06564  1.000 25.67575  ? 342 SER C CB  1 
ATOM   4042 O  OG  . SER C 1 342 ? 12.46939  19.18287  18.04756  1.000 27.86203  ? 342 SER C OG  1 
ATOM   4043 N  N   . TRP C 1 343 ? 9.60496   20.83155  19.49594  1.000 22.95841  ? 343 TRP C N   1 
ATOM   4044 C  CA  . TRP C 1 343 ? 8.23156   20.81375  19.02310  1.000 22.82361  ? 343 TRP C CA  1 
ATOM   4045 C  C   . TRP C 1 343 ? 7.97962   22.02810  18.14446  1.000 30.20715  ? 343 TRP C C   1 
ATOM   4046 O  O   . TRP C 1 343 ? 8.74134   23.00371  18.13913  1.000 27.17795  ? 343 TRP C O   1 
ATOM   4047 C  CB  . TRP C 1 343 ? 7.21056   20.77004  20.17653  1.000 21.30408  ? 343 TRP C CB  1 
ATOM   4048 C  CG  . TRP C 1 343 ? 7.36691   21.89189  21.17625  1.000 23.66426  ? 343 TRP C CG  1 
ATOM   4049 C  CD1 . TRP C 1 343 ? 6.64672   23.05815  21.21934  1.000 25.46803  ? 343 TRP C CD1 1 
ATOM   4050 C  CD2 . TRP C 1 343 ? 8.32428   21.97227  22.25027  1.000 24.08373  ? 343 TRP C CD2 1 
ATOM   4051 N  NE1 . TRP C 1 343 ? 7.07213   23.84027  22.26737  1.000 28.20973  ? 343 TRP C NE1 1 
ATOM   4052 C  CE2 . TRP C 1 343 ? 8.09817   23.20545  22.91637  1.000 27.38697  ? 343 TRP C CE2 1 
ATOM   4053 C  CE3 . TRP C 1 343 ? 9.34055   21.12859  22.70824  1.000 21.93215  ? 343 TRP C CE3 1 
ATOM   4054 C  CZ2 . TRP C 1 343 ? 8.86012   23.61865  24.02547  1.000 30.10691  ? 343 TRP C CZ2 1 
ATOM   4055 C  CZ3 . TRP C 1 343 ? 10.09456  21.52829  23.83441  1.000 27.80086  ? 343 TRP C CZ3 1 
ATOM   4056 C  CH2 . TRP C 1 343 ? 9.84865   22.77047  24.46712  1.000 28.72801  ? 343 TRP C CH2 1 
ATOM   4057 N  N   . SER C 1 344 ? 6.94355   21.91962  17.33039  1.000 26.34732  ? 344 SER C N   1 
ATOM   4058 C  CA  . SER C 1 344 ? 6.62098   22.99314  16.41415  1.000 23.52342  ? 344 SER C CA  1 
ATOM   4059 C  C   . SER C 1 344 ? 5.23245   23.58399  16.60348  1.000 29.56034  ? 344 SER C C   1 
ATOM   4060 O  O   . SER C 1 344 ? 4.97038   24.67698  16.08193  1.000 40.72776  ? 344 SER C O   1 
ATOM   4061 C  CB  . SER C 1 344 ? 6.82157   22.52815  14.96586  1.000 32.77017  ? 344 SER C CB  1 
ATOM   4062 O  OG  . SER C 1 344 ? 6.32124   21.22713  14.73762  1.000 44.55756  ? 344 SER C OG  1 
ATOM   4063 N  N   . LYS C 1 345 ? 4.35329   22.93533  17.34703  1.000 27.34563  ? 345 LYS C N   1 
ATOM   4064 C  CA  . LYS C 1 345 ? 3.06285   23.54973  17.61974  1.000 28.27337  ? 345 LYS C CA  1 
ATOM   4065 C  C   . LYS C 1 345 ? 3.20707   24.63466  18.67663  1.000 34.75281  ? 345 LYS C C   1 
ATOM   4066 O  O   . LYS C 1 345 ? 4.14926   24.63754  19.47544  1.000 34.20695  ? 345 LYS C O   1 
ATOM   4067 C  CB  . LYS C 1 345 ? 2.06341   22.51891  18.11356  1.000 28.89205  ? 345 LYS C CB  1 
ATOM   4068 C  CG  . LYS C 1 345 ? 1.75582   21.44662  17.10316  1.000 36.73140  ? 345 LYS C CG  1 
ATOM   4069 C  CD  . LYS C 1 345 ? 0.61684   20.57825  17.63150  1.000 42.20288  ? 345 LYS C CD  1 
ATOM   4070 C  CE  . LYS C 1 345 ? 0.02194   19.75829  16.52204  1.000 43.20060  ? 345 LYS C CE  1 
ATOM   4071 N  NZ  . LYS C 1 345 ? -1.18100  18.99149  16.92335  1.000 37.20624  ? 345 LYS C NZ  1 
ATOM   4072 N  N   . THR C 1 346 ? 2.24293   25.55760  18.68625  1.000 33.01957  ? 346 THR C N   1 
ATOM   4073 C  CA  . THR C 1 346 ? 2.18363   26.63123  19.68574  1.000 29.68990  ? 346 THR C CA  1 
ATOM   4074 C  C   . THR C 1 346 ? 1.40428   26.10685  20.88787  1.000 37.30864  ? 346 THR C C   1 
ATOM   4075 O  O   . THR C 1 346 ? 0.17199   26.13365  20.90114  1.000 52.55093  ? 346 THR C O   1 
ATOM   4076 C  CB  . THR C 1 346 ? 1.50841   27.87258  19.09491  1.000 35.28220  ? 346 THR C CB  1 
ATOM   4077 O  OG1 . THR C 1 346 ? 2.21152   28.28665  17.91491  1.000 39.08688  ? 346 THR C OG1 1 
ATOM   4078 C  CG2 . THR C 1 346 ? 1.45473   29.03053  20.09880  1.000 37.11501  ? 346 THR C CG2 1 
ATOM   4079 N  N   . TYR C 1 347 ? 2.10806   25.62878  21.91257  1.000 27.42345  ? 347 TYR C N   1 
ATOM   4080 C  CA  . TYR C 1 347 ? 1.42329   25.05375  23.05665  1.000 26.07650  ? 347 TYR C CA  1 
ATOM   4081 C  C   . TYR C 1 347 ? 1.12299   26.13568  24.08781  1.000 37.47596  ? 347 TYR C C   1 
ATOM   4082 O  O   . TYR C 1 347 ? 1.86573   27.10865  24.23659  1.000 33.50983  ? 347 TYR C O   1 
ATOM   4083 C  CB  . TYR C 1 347 ? 2.25212   23.94009  23.68779  1.000 25.87226  ? 347 TYR C CB  1 
ATOM   4084 C  CG  . TYR C 1 347 ? 2.33827   22.72096  22.78993  1.000 27.11810  ? 347 TYR C CG  1 
ATOM   4085 C  CD1 . TYR C 1 347 ? 1.19031   22.17036  22.22362  1.000 26.14927  ? 347 TYR C CD1 1 
ATOM   4086 C  CD2 . TYR C 1 347 ? 3.56203   22.13952  22.49145  1.000 23.95843  ? 347 TYR C CD2 1 
ATOM   4087 C  CE1 . TYR C 1 347 ? 1.25804   21.04078  21.37889  1.000 23.63592  ? 347 TYR C CE1 1 
ATOM   4088 C  CE2 . TYR C 1 347 ? 3.63280   21.00244  21.65209  1.000 23.75045  ? 347 TYR C CE2 1 
ATOM   4089 C  CZ  . TYR C 1 347 ? 2.46976   20.47911  21.09655  1.000 23.82647  ? 347 TYR C CZ  1 
ATOM   4090 O  OH  . TYR C 1 347 ? 2.53876   19.37478  20.25493  1.000 24.28290  ? 347 TYR C OH  1 
ATOM   4091 N  N   . GLU C 1 348 ? -0.00068  25.98157  24.77223  1.000 30.08829  ? 348 GLU C N   1 
ATOM   4092 C  CA  . GLU C 1 348 ? -0.42782  26.98288  25.74660  1.000 29.39830  ? 348 GLU C CA  1 
ATOM   4093 C  C   . GLU C 1 348 ? -0.67939  26.28511  27.06455  1.000 35.53954  ? 348 GLU C C   1 
ATOM   4094 O  O   . GLU C 1 348 ? -1.68958  25.59253  27.20943  1.000 32.32478  ? 348 GLU C O   1 
ATOM   4095 C  CB  . GLU C 1 348 ? -1.67539  27.72887  25.27652  1.000 43.44918  ? 348 GLU C CB  1 
ATOM   4096 C  CG  . GLU C 1 348 ? -2.12925  28.79762  26.26107  1.000 63.05800  ? 348 GLU C CG  1 
ATOM   4097 C  CD  . GLU C 1 348 ? -3.32819  29.58673  25.77125  1.000 74.91922  ? 348 GLU C CD  1 
ATOM   4098 O  OE1 . GLU C 1 348 ? -3.47937  29.73337  24.53800  1.000 77.29184  ? 348 GLU C OE1 1 
ATOM   4099 O  OE2 . GLU C 1 348 ? -4.11493  30.06277  26.62044  1.000 80.98506  ? 348 GLU C OE2 1 
ATOM   4100 N  N   . ASN C 1 349 ? 0.24026   26.48597  28.01218  1.000 29.62949  ? 349 ASN C N   1 
ATOM   4101 C  CA  . ASN C 1 349 ? 0.18967   25.89490  29.34982  1.000 26.31927  ? 349 ASN C CA  1 
ATOM   4102 C  C   . ASN C 1 349 ? 0.14544   24.36671  29.30190  1.000 28.30122  ? 349 ASN C C   1 
ATOM   4103 O  O   . ASN C 1 349 ? -0.68671  23.73358  29.94540  1.000 33.40113  ? 349 ASN C O   1 
ATOM   4104 C  CB  . ASN C 1 349 ? -0.98665  26.45587  30.15173  1.000 29.48675  ? 349 ASN C CB  1 
ATOM   4105 C  CG  . ASN C 1 349 ? -0.87562  27.94476  30.35514  1.000 35.41453  ? 349 ASN C CG  1 
ATOM   4106 O  OD1 . ASN C 1 349 ? 0.22441   28.49797  30.35998  1.000 31.18583  ? 349 ASN C OD1 1 
ATOM   4107 N  ND2 . ASN C 1 349 ? -2.00479  28.60523  30.51175  1.000 34.24622  ? 349 ASN C ND2 1 
ATOM   4108 N  N   . VAL C 1 350 ? 1.09534   23.76680  28.58666  1.000 26.18770  ? 350 VAL C N   1 
ATOM   4109 C  CA  . VAL C 1 350 ? 1.17919   22.30606  28.46335  1.000 23.31832  ? 350 VAL C CA  1 
ATOM   4110 C  C   . VAL C 1 350 ? 2.32607   21.81555  29.33492  1.000 27.73822  ? 350 VAL C C   1 
ATOM   4111 O  O   . VAL C 1 350 ? 3.46852   22.26018  29.18963  1.000 25.06478  ? 350 VAL C O   1 
ATOM   4112 C  CB  . VAL C 1 350 ? 1.34993   21.88128  26.99970  1.000 22.89657  ? 350 VAL C CB  1 
ATOM   4113 C  CG1 . VAL C 1 350 ? 1.60097   20.36673  26.88325  1.000 26.23403  ? 350 VAL C CG1 1 
ATOM   4114 C  CG2 . VAL C 1 350 ? 0.09459   22.27302  26.18438  1.000 26.36694  ? 350 VAL C CG2 1 
ATOM   4115 N  N   . GLU C 1 351 ? 2.01535   20.90950  30.25383  1.000 28.34163  ? 351 GLU C N   1 
ATOM   4116 C  CA  . GLU C 1 351 ? 3.01473   20.39064  31.17381  1.000 25.77712  ? 351 GLU C CA  1 
ATOM   4117 C  C   . GLU C 1 351 ? 3.92045   19.42129  30.42563  1.000 23.89588  ? 351 GLU C C   1 
ATOM   4118 O  O   . GLU C 1 351 ? 3.44241   18.53288  29.71165  1.000 25.87758  ? 351 GLU C O   1 
ATOM   4119 C  CB  . GLU C 1 351 ? 2.27781   19.72994  32.33403  1.000 32.33420  ? 351 GLU C CB  1 
ATOM   4120 C  CG  . GLU C 1 351 ? 3.00848   19.60319  33.62948  1.000 43.02872  ? 351 GLU C CG  1 
ATOM   4121 C  CD  . GLU C 1 351 ? 2.08560   19.03369  34.70762  1.000 54.61595  ? 351 GLU C CD  1 
ATOM   4122 O  OE1 . GLU C 1 351 ? 2.52871   18.90439  35.86622  1.000 35.64958  ? 351 GLU C OE1 1 
ATOM   4123 O  OE2 . GLU C 1 351 ? 0.88754   18.78624  34.40257  1.000 41.47470  ? 351 GLU C OE2 1 
ATOM   4124 N  N   . PHE C 1 352 ? 5.23301   19.60397  30.55237  1.000 24.55699  ? 352 PHE C N   1 
ATOM   4125 C  CA  . PHE C 1 352 ? 6.14879   18.79273  29.74697  1.000 23.67787  ? 352 PHE C CA  1 
ATOM   4126 C  C   . PHE C 1 352 ? 6.39718   17.48253  30.49027  1.000 28.07754  ? 352 PHE C C   1 
ATOM   4127 O  O   . PHE C 1 352 ? 7.36083   17.31387  31.23231  1.000 27.71307  ? 352 PHE C O   1 
ATOM   4128 C  CB  . PHE C 1 352 ? 7.44004   19.54326  29.43034  1.000 25.82585  ? 352 PHE C CB  1 
ATOM   4129 C  CG  . PHE C 1 352 ? 8.12919   19.02391  28.18769  1.000 24.86161  ? 352 PHE C CG  1 
ATOM   4130 C  CD1 . PHE C 1 352 ? 8.84911   17.83405  28.23499  1.000 22.73252  ? 352 PHE C CD1 1 
ATOM   4131 C  CD2 . PHE C 1 352 ? 7.96033   19.65889  26.96741  1.000 30.70778  ? 352 PHE C CD2 1 
ATOM   4132 C  CE1 . PHE C 1 352 ? 9.45908   17.31475  27.10681  1.000 24.60793  ? 352 PHE C CE1 1 
ATOM   4133 C  CE2 . PHE C 1 352 ? 8.56029   19.14926  25.79096  1.000 26.38520  ? 352 PHE C CE2 1 
ATOM   4134 C  CZ  . PHE C 1 352 ? 9.30267   17.96276  25.85888  1.000 26.70712  ? 352 PHE C CZ  1 
ATOM   4135 N  N   . GLU C 1 353 ? 5.48309   16.53458  30.28447  1.000 21.31888  ? 353 GLU C N   1 
ATOM   4136 C  CA  . GLU C 1 353 ? 5.65211   15.16363  30.74989  1.000 21.66533  ? 353 GLU C CA  1 
ATOM   4137 C  C   . GLU C 1 353 ? 5.35768   14.27182  29.55938  1.000 25.84542  ? 353 GLU C C   1 
ATOM   4138 O  O   . GLU C 1 353 ? 4.28279   14.38690  28.97113  1.000 26.31876  ? 353 GLU C O   1 
ATOM   4139 C  CB  . GLU C 1 353 ? 4.69787   14.82204  31.89697  1.000 30.49268  ? 353 GLU C CB  1 
ATOM   4140 C  CG  . GLU C 1 353 ? 4.71089   15.78577  33.02436  1.000 45.75839  ? 353 GLU C CG  1 
ATOM   4141 C  CD  . GLU C 1 353 ? 3.69216   15.41184  34.07509  1.000 70.34186  ? 353 GLU C CD  1 
ATOM   4142 O  OE1 . GLU C 1 353 ? 2.87386   14.49622  33.79796  1.000 69.95869  ? 353 GLU C OE1 1 
ATOM   4143 O  OE2 . GLU C 1 353 ? 3.71938   16.01706  35.17406  1.000 48.83589  ? 353 GLU C OE2 1 
ATOM   4144 N  N   . THR C 1 354 ? 6.27963   13.37873  29.21816  1.000 20.13041  ? 354 THR C N   1 
ATOM   4145 C  CA  . THR C 1 354 ? 6.20214   12.70126  27.92438  1.000 18.59208  ? 354 THR C CA  1 
ATOM   4146 C  C   . THR C 1 354 ? 5.67185   11.28141  28.09939  1.000 22.63141  ? 354 THR C C   1 
ATOM   4147 O  O   . THR C 1 354 ? 5.82176   10.66139  29.15413  1.000 20.81914  ? 354 THR C O   1 
ATOM   4148 C  CB  . THR C 1 354 ? 7.57352   12.61994  27.23852  1.000 20.92618  ? 354 THR C CB  1 
ATOM   4149 O  OG1 . THR C 1 354 ? 8.39090   11.58012  27.81266  1.000 22.67375  ? 354 THR C OG1 1 
ATOM   4150 C  CG2 . THR C 1 354 ? 8.35109   13.97703  27.26255  1.000 20.59591  ? 354 THR C CG2 1 
ATOM   4151 N  N   . THR C 1 355 ? 5.12118   10.73863  27.00906  1.000 20.81424  ? 355 THR C N   1 
ATOM   4152 C  CA  . THR C 1 355 ? 4.95902   9.29093   26.90172  1.000 17.11076  ? 355 THR C CA  1 
ATOM   4153 C  C   . THR C 1 355 ? 6.33669   8.62133   26.75389  1.000 17.88208  ? 355 THR C C   1 
ATOM   4154 O  O   . THR C 1 355 ? 7.37864   9.28127   26.69076  1.000 21.03019  ? 355 THR C O   1 
ATOM   4155 C  CB  . THR C 1 355 ? 4.02407   8.94432   25.73944  1.000 18.84192  ? 355 THR C CB  1 
ATOM   4156 O  OG1 . THR C 1 355 ? 4.54769   9.48376   24.51188  1.000 19.27689  ? 355 THR C OG1 1 
ATOM   4157 C  CG2 . THR C 1 355 ? 2.61295   9.57417   25.99681  1.000 20.28996  ? 355 THR C CG2 1 
ATOM   4158 N  N   . SER C 1 356 ? 6.35651   7.28598   26.74534  1.000 17.64922  ? 356 SER C N   1 
ATOM   4159 C  CA  . SER C 1 356 ? 7.59950   6.53299   26.71006  1.000 16.90841  ? 356 SER C CA  1 
ATOM   4160 C  C   . SER C 1 356 ? 7.96669   6.12852   25.27931  1.000 18.42928  ? 356 SER C C   1 
ATOM   4161 O  O   . SER C 1 356 ? 7.09514   5.86866   24.45159  1.000 22.13712  ? 356 SER C O   1 
ATOM   4162 C  CB  . SER C 1 356 ? 7.48281   5.27239   27.58685  1.000 20.87926  ? 356 SER C CB  1 
ATOM   4163 O  OG  . SER C 1 356 ? 7.39634   5.62290   28.97728  1.000 23.06616  ? 356 SER C OG  1 
ATOM   4164 N  N   . PHE C 1 357 ? 9.26698   6.03082   25.01931  1.000 18.96995  ? 357 PHE C N   1 
ATOM   4165 C  CA  . PHE C 1 357 ? 9.77758   5.65358   23.70217  1.000 17.71863  ? 357 PHE C CA  1 
ATOM   4166 C  C   . PHE C 1 357 ? 10.85915  4.59333   23.87411  1.000 19.82694  ? 357 PHE C C   1 
ATOM   4167 O  O   . PHE C 1 357 ? 11.71707  4.69786   24.76702  1.000 20.40013  ? 357 PHE C O   1 
ATOM   4168 C  CB  . PHE C 1 357 ? 10.32778  6.91470   22.97963  1.000 17.30753  ? 357 PHE C CB  1 
ATOM   4169 C  CG  . PHE C 1 357 ? 10.95712  6.64047   21.63392  1.000 18.94456  ? 357 PHE C CG  1 
ATOM   4170 C  CD1 . PHE C 1 357 ? 10.20479  6.10449   20.59620  1.000 22.33599  ? 357 PHE C CD1 1 
ATOM   4171 C  CD2 . PHE C 1 357 ? 12.29715  6.94365   21.40041  1.000 21.60597  ? 357 PHE C CD2 1 
ATOM   4172 C  CE1 . PHE C 1 357 ? 10.79217  5.87558   19.34310  1.000 23.49951  ? 357 PHE C CE1 1 
ATOM   4173 C  CE2 . PHE C 1 357 ? 12.88036  6.71567   20.15152  1.000 23.00563  ? 357 PHE C CE2 1 
ATOM   4174 C  CZ  . PHE C 1 357 ? 12.10869  6.16390   19.11703  1.000 22.86732  ? 357 PHE C CZ  1 
ATOM   4175 N  N   . THR C 1 358 ? 10.81894  3.57882   23.00013  1.000 15.96320  ? 358 THR C N   1 
ATOM   4176 C  CA  . THR C 1 358 ? 11.79597  2.50738   22.97138  1.000 15.37041  ? 358 THR C CA  1 
ATOM   4177 C  C   . THR C 1 358 ? 12.61002  2.58888   21.68472  1.000 22.09289  ? 358 THR C C   1 
ATOM   4178 O  O   . THR C 1 358 ? 12.05630  2.84255   20.60652  1.000 22.05002  ? 358 THR C O   1 
ATOM   4179 C  CB  . THR C 1 358 ? 11.10152  1.15032   23.03654  1.000 23.83680  ? 358 THR C CB  1 
ATOM   4180 O  OG1 . THR C 1 358 ? 10.46181  1.00445   24.30659  1.000 27.20808  ? 358 THR C OG1 1 
ATOM   4181 C  CG2 . THR C 1 358 ? 12.12632  0.01812   22.84336  1.000 23.29469  ? 358 THR C CG2 1 
ATOM   4182 N  N   . PHE C 1 359 ? 13.91240  2.35623   21.79867  1.000 19.32837  ? 359 PHE C N   1 
ATOM   4183 C  CA  . PHE C 1 359 ? 14.79487  2.28072   20.63898  1.000 19.29632  ? 359 PHE C CA  1 
ATOM   4184 C  C   . PHE C 1 359 ? 15.88688  1.29151   20.97832  1.000 21.52456  ? 359 PHE C C   1 
ATOM   4185 O  O   . PHE C 1 359 ? 15.90422  0.72442   22.07202  1.000 20.57694  ? 359 PHE C O   1 
ATOM   4186 C  CB  . PHE C 1 359 ? 15.35589  3.66469   20.27911  1.000 18.70041  ? 359 PHE C CB  1 
ATOM   4187 C  CG  . PHE C 1 359 ? 16.14343  4.31815   21.36408  1.000 20.69387  ? 359 PHE C CG  1 
ATOM   4188 C  CD1 . PHE C 1 359 ? 15.49170  5.00789   22.38644  1.000 23.97706  ? 359 PHE C CD1 1 
ATOM   4189 C  CD2 . PHE C 1 359 ? 17.55192  4.29470   21.34446  1.000 22.40859  ? 359 PHE C CD2 1 
ATOM   4190 C  CE1 . PHE C 1 359 ? 16.21094  5.62486   23.43118  1.000 26.78962  ? 359 PHE C CE1 1 
ATOM   4191 C  CE2 . PHE C 1 359 ? 18.28311  4.92402   22.37376  1.000 23.51750  ? 359 PHE C CE2 1 
ATOM   4192 C  CZ  . PHE C 1 359 ? 17.62942  5.58347   23.42273  1.000 25.84636  ? 359 PHE C CZ  1 
ATOM   4193 N  N   . SER C 1 360 ? 16.79657  1.05007   20.03807  1.000 21.99232  ? 360 SER C N   1 
ATOM   4194 C  CA  . SER C 1 360 ? 17.96788  0.25784   20.39204  1.000 20.04500  ? 360 SER C CA  1 
ATOM   4195 C  C   . SER C 1 360 ? 19.20622  0.86115   19.73225  1.000 18.50778  ? 360 SER C C   1 
ATOM   4196 O  O   . SER C 1 360 ? 19.12448  1.72250   18.84195  1.000 23.32904  ? 360 SER C O   1 
ATOM   4197 C  CB  . SER C 1 360 ? 17.82017  -1.22519  20.00556  1.000 24.66385  ? 360 SER C CB  1 
ATOM   4198 O  OG  . SER C 1 360 ? 17.97954  -1.40655  18.59350  1.000 25.89685  ? 360 SER C OG  1 
ATOM   4199 N  N   . TYR C 1 361 ? 20.37145  0.38785   20.15087  1.000 21.28606  ? 361 TYR C N   1 
ATOM   4200 C  CA  . TYR C 1 361 ? 21.59003  0.81503   19.48121  1.000 22.71489  ? 361 TYR C CA  1 
ATOM   4201 C  C   . TYR C 1 361 ? 22.63329  -0.27172  19.62087  1.000 28.83487  ? 361 TYR C C   1 
ATOM   4202 O  O   . TYR C 1 361 ? 22.53093  -1.16005  20.47040  1.000 23.67079  ? 361 TYR C O   1 
ATOM   4203 C  CB  . TYR C 1 361 ? 22.13851  2.16176   20.00468  1.000 21.80627  ? 361 TYR C CB  1 
ATOM   4204 C  CG  . TYR C 1 361 ? 22.45758  2.22039   21.48680  1.000 22.17418  ? 361 TYR C CG  1 
ATOM   4205 C  CD1 . TYR C 1 361 ? 23.73312  1.86133   21.95385  1.000 24.51369  ? 361 TYR C CD1 1 
ATOM   4206 C  CD2 . TYR C 1 361 ? 21.50494  2.64009   22.40247  1.000 21.75475  ? 361 TYR C CD2 1 
ATOM   4207 C  CE1 . TYR C 1 361 ? 24.04716  1.91345   23.29216  1.000 21.91469  ? 361 TYR C CE1 1 
ATOM   4208 C  CE2 . TYR C 1 361 ? 21.79646  2.67608   23.76299  1.000 22.13699  ? 361 TYR C CE2 1 
ATOM   4209 C  CZ  . TYR C 1 361 ? 23.08815  2.32108   24.18434  1.000 22.00215  ? 361 TYR C CZ  1 
ATOM   4210 O  OH  . TYR C 1 361 ? 23.34252  2.36784   25.53194  1.000 24.34421  ? 361 TYR C OH  1 
ATOM   4211 N  N   . ILE C 1 362 ? 23.63991  -0.19580  18.75874  1.000 23.30843  ? 362 ILE C N   1 
ATOM   4212 C  CA  . ILE C 1 362 ? 24.69042  -1.20828  18.72988  1.000 22.14767  ? 362 ILE C CA  1 
ATOM   4213 C  C   . ILE C 1 362 ? 25.67075  -0.94184  19.86170  1.000 23.76513  ? 362 ILE C C   1 
ATOM   4214 O  O   . ILE C 1 362 ? 26.18232  0.16963   19.99533  1.000 24.97544  ? 362 ILE C O   1 
ATOM   4215 C  CB  . ILE C 1 362 ? 25.40188  -1.17963  17.36853  1.000 23.16551  ? 362 ILE C CB  1 
ATOM   4216 C  CG1 . ILE C 1 362 ? 24.37678  -1.40228  16.26293  1.000 26.13262  ? 362 ILE C CG1 1 
ATOM   4217 C  CG2 . ILE C 1 362 ? 26.54082  -2.21037  17.32423  1.000 25.18130  ? 362 ILE C CG2 1 
ATOM   4218 C  CD1 . ILE C 1 362 ? 24.94133  -1.07495  14.84016  1.000 31.11175  ? 362 ILE C CD1 1 
ATOM   4219 N  N   . ALA C 1 363 ? 25.97526  -1.96966  20.64654  1.000 24.65093  ? 363 ALA C N   1 
ATOM   4220 C  CA  . ALA C 1 363 ? 26.85220  -1.81175  21.79517  1.000 27.42343  ? 363 ALA C CA  1 
ATOM   4221 C  C   . ALA C 1 363 ? 28.33726  -1.90735  21.44085  1.000 38.62230  ? 363 ALA C C   1 
ATOM   4222 O  O   . ALA C 1 363 ? 28.75185  -2.62993  20.52508  1.000 27.54543  ? 363 ALA C O   1 
ATOM   4223 C  CB  . ALA C 1 363 ? 26.51867  -2.85580  22.85363  1.000 27.25150  ? 363 ALA C CB  1 
ATOM   4224 N  N   . GLN C 1 364 ? 29.14317  -1.18448  22.22225  1.000 30.32816  ? 364 GLN C N   1 
ATOM   4225 C  CA  . GLN C 1 364 ? 30.58481  -1.14870  21.99814  1.000 30.47477  ? 364 GLN C CA  1 
ATOM   4226 C  C   . GLN C 1 364 ? 31.20307  -2.53205  22.18464  1.000 36.08510  ? 364 GLN C C   1 
ATOM   4227 O  O   . GLN C 1 364 ? 32.04982  -2.95601  21.38686  1.000 39.19001  ? 364 GLN C O   1 
ATOM   4228 C  CB  . GLN C 1 364 ? 31.21791  -0.11801  22.93409  1.000 32.22408  ? 364 GLN C CB  1 
ATOM   4229 C  CG  . GLN C 1 364 ? 32.73096  -0.18991  23.01252  1.000 41.43973  ? 364 GLN C CG  1 
ATOM   4230 C  CD  . GLN C 1 364 ? 33.44200  0.25501   21.73840  1.000 35.11585  ? 364 GLN C CD  1 
ATOM   4231 O  OE1 . GLN C 1 364 ? 32.81915  0.68099   20.76405  1.000 31.37655  ? 364 GLN C OE1 1 
ATOM   4232 N  NE2 . GLN C 1 364 ? 34.77454  0.14082   21.74187  1.000 36.85859  ? 364 GLN C NE2 1 
ATOM   4233 N  N   . GLU C 1 365 ? 30.75889  -3.26958  23.19337  1.000 39.58561  ? 365 GLU C N   1 
ATOM   4234 C  CA  . GLU C 1 365 ? 31.24270  -4.63507  23.39606  1.000 47.71952  ? 365 GLU C CA  1 
ATOM   4235 C  C   . GLU C 1 365 ? 30.12796  -5.59228  23.82386  1.000 62.73958  ? 365 GLU C C   1 
ATOM   4236 O  O   . GLU C 1 365 ? 29.05564  -5.16682  24.25819  1.000 46.22429  ? 365 GLU C O   1 
ATOM   4237 C  CB  . GLU C 1 365 ? 32.37258  -4.64229  24.43292  1.000 50.05301  ? 365 GLU C CB  1 
ATOM   4238 C  CG  . GLU C 1 365 ? 33.69903  -4.20368  23.85689  1.000 68.02611  ? 365 GLU C CG  1 
ATOM   4239 C  CD  . GLU C 1 365 ? 34.71849  -3.85685  24.91798  1.000 83.05871  ? 365 GLU C CD  1 
ATOM   4240 O  OE1 . GLU C 1 365 ? 34.48274  -4.18260  26.10404  1.000 71.37748  ? 365 GLU C OE1 1 
ATOM   4241 O  OE2 . GLU C 1 365 ? 35.75174  -3.24828  24.55964  1.000 89.01656  ? 365 GLU C OE2 1 
ATOM   4242 O  OXT . GLU C 1 365 ? 30.26867  -6.81688  23.74076  1.000 61.43443  ? 365 GLU C OXT 1 
HETATM 4243 C  C1  . ANA D 2 .   ? -0.91230  9.53492   5.34089   0.935 40.57789  ? 401 ANA A C1  1 
HETATM 4244 C  C2  . ANA D 2 .   ? 0.46794   10.14588  5.62723   0.935 35.39232  ? 401 ANA A C2  1 
HETATM 4245 C  C3  . ANA D 2 .   ? 1.05256   9.82933   6.98983   0.935 31.28787  ? 401 ANA A C3  1 
HETATM 4246 C  C4  . ANA D 2 .   ? 1.51799   8.39273   7.10982   0.935 28.15725  ? 401 ANA A C4  1 
HETATM 4247 C  C5  . ANA D 2 .   ? 2.39296   7.97382   5.93089   0.935 29.08260  ? 401 ANA A C5  1 
HETATM 4248 C  C6  . ANA D 2 .   ? 1.70176   8.33773   4.61084   0.935 31.54765  ? 401 ANA A C6  1 
HETATM 4249 C  C7  . ANA D 2 .   ? 2.60117   8.13812   3.40331   0.935 34.71466  ? 401 ANA A C7  1 
HETATM 4250 C  C8  . ANA D 2 .   ? 1.91770   8.59543   2.11695   0.935 39.30289  ? 401 ANA A C8  1 
HETATM 4251 C  C9  . ANA D 2 .   ? 2.62991   8.11863   0.87028   0.935 43.49203  ? 401 ANA A C9  1 
HETATM 4252 C  C10 . ANA D 2 .   ? 3.70935   5.89442   6.34206   0.935 29.35797  ? 401 ANA A C10 1 
HETATM 4253 C  C11 . ANA D 2 .   ? 3.68796   4.41019   6.15555   0.935 25.84930  ? 401 ANA A C11 1 
HETATM 4254 C  C12 . ANA D 2 .   ? -0.18907  12.06558  4.35422   0.935 43.59753  ? 401 ANA A C12 1 
HETATM 4255 C  CA4 . ANA D 2 .   ? 1.65703   8.18710   9.50446   0.935 28.52872  ? 401 ANA A CA4 1 
HETATM 4256 C  CM4 . ANA D 2 .   ? 2.62538   8.15473   10.63844  0.935 29.78854  ? 401 ANA A CM4 1 
HETATM 4257 N  N5  . ANA D 2 .   ? 2.58912   6.53041   5.97054   0.935 28.89015  ? 401 ANA A N5  1 
HETATM 4258 O  O1A . ANA D 2 .   ? -1.17704  9.03858   4.25886   0.935 42.68805  ? 401 ANA A O1A 1 
HETATM 4259 O  O1B . ANA D 2 .   ? -1.75366  9.57478   6.19399   0.935 42.21422  ? 401 ANA A O1B 1 
HETATM 4260 O  O2  . ANA D 2 .   ? 0.35464   11.56339  5.57364   0.935 39.93723  ? 401 ANA A O2  1 
HETATM 4261 O  O4  . ANA D 2 .   ? 2.30331   8.27907   8.32181   0.935 28.11558  ? 401 ANA A O4  1 
HETATM 4262 O  O6  . ANA D 2 .   ? 1.37395   9.73885   4.60257   0.935 32.08239  ? 401 ANA A O6  1 
HETATM 4263 O  O7  . ANA D 2 .   ? 3.80782   8.88930   3.56148   0.935 34.68672  ? 401 ANA A O7  1 
HETATM 4264 O  O8  . ANA D 2 .   ? 0.57831   8.10532   2.08781   0.935 40.26664  ? 401 ANA A O8  1 
HETATM 4265 O  O9  . ANA D 2 .   ? 2.59822   6.69491   0.78653   0.935 45.81116  ? 401 ANA A O9  1 
HETATM 4266 O  O10 . ANA D 2 .   ? 4.68059   6.46156   6.83069   0.935 27.20010  ? 401 ANA A O10 1 
HETATM 4267 O  OA4 . ANA D 2 .   ? 0.46856   8.10166   9.59509   0.935 30.51769  ? 401 ANA A OA4 1 
HETATM 4268 ZN ZN  . ZN  E 3 .   ? -15.01158 -9.27848  5.56945   1.000 38.82625  ? 402 ZN  A ZN  1 
HETATM 4269 ZN ZN  . ZN  F 3 .   ? 12.76263  -9.92739  36.00293  0.611 56.21059  ? 403 ZN  A ZN  1 
HETATM 4270 ZN ZN  . ZN  G 3 .   ? -10.29254 -10.19191 5.42062   0.663 36.62845  ? 404 ZN  A ZN  1 
HETATM 4271 C  C   . ACT H 4 .   ? -7.82223  -11.50593 4.51248   1.000 40.39729  ? 405 ACT A C   1 
HETATM 4272 O  O   . ACT H 4 .   ? -8.34886  -10.38185 4.62445   1.000 40.62571  ? 405 ACT A O   1 
HETATM 4273 O  OXT . ACT H 4 .   ? -8.60723  -12.46598 4.52720   1.000 41.62473  ? 405 ACT A OXT 1 
HETATM 4274 C  CH3 . ACT H 4 .   ? -6.34249  -11.68638 4.35556   1.000 38.04735  ? 405 ACT A CH3 1 
HETATM 4275 C  C   . ACT I 4 .   ? -5.67477  -12.56274 43.08083  1.000 50.41227  ? 406 ACT A C   1 
HETATM 4276 O  O   . ACT I 4 .   ? -5.25418  -11.45072 42.70027  1.000 46.13614  ? 406 ACT A O   1 
HETATM 4277 O  OXT . ACT I 4 .   ? -4.88400  -13.52338 42.98031  1.000 52.55470  ? 406 ACT A OXT 1 
HETATM 4278 C  CH3 . ACT I 4 .   ? -7.06043  -12.72089 43.62735  1.000 51.82056  ? 406 ACT A CH3 1 
HETATM 4279 C  C   . ACT J 4 .   ? -5.31843  4.15463   -1.37927  1.000 58.04232  ? 407 ACT A C   1 
HETATM 4280 O  O   . ACT J 4 .   ? -4.21940  4.66912   -1.66529  1.000 59.85403  ? 407 ACT A O   1 
HETATM 4281 O  OXT . ACT J 4 .   ? -6.03012  4.78655   -0.57228  1.000 56.84497  ? 407 ACT A OXT 1 
HETATM 4282 C  CH3 . ACT J 4 .   ? -5.75513  2.85649   -1.98788  1.000 58.12547  ? 407 ACT A CH3 1 
HETATM 4283 C  C   . ACT K 4 .   ? 7.76363   -14.80574 37.03553  1.000 51.83678  ? 408 ACT A C   1 
HETATM 4284 O  O   . ACT K 4 .   ? 7.37010   -14.62113 35.86197  1.000 50.11498  ? 408 ACT A O   1 
HETATM 4285 O  OXT . ACT K 4 .   ? 6.89313   -15.17505 37.87047  1.000 51.77464  ? 408 ACT A OXT 1 
HETATM 4286 C  CH3 . ACT K 4 .   ? 9.20249   -14.59528 37.40530  1.000 53.19554  ? 408 ACT A CH3 1 
HETATM 4287 C  C1  . ANA L 2 .   ? 7.89779   16.95166  7.98659   0.988 41.64110  ? 401 ANA B C1  1 
HETATM 4288 C  C2  . ANA L 2 .   ? 6.98711   16.75727  9.21148   0.988 38.88412  ? 401 ANA B C2  1 
HETATM 4289 C  C3  . ANA L 2 .   ? 6.76002   15.30931  9.60057   0.988 35.33150  ? 401 ANA B C3  1 
HETATM 4290 C  C4  . ANA L 2 .   ? 7.98918   14.67041  10.22946  0.988 31.62594  ? 401 ANA B C4  1 
HETATM 4291 C  C5  . ANA L 2 .   ? 8.59210   15.55155  11.32097  0.988 31.01343  ? 401 ANA B C5  1 
HETATM 4292 C  C6  . ANA L 2 .   ? 8.77047   16.98907  10.81828  0.988 34.11581  ? 401 ANA B C6  1 
HETATM 4293 C  C7  . ANA L 2 .   ? 9.20646   17.94256  11.91876  0.988 36.38320  ? 401 ANA B C7  1 
HETATM 4294 C  C8  . ANA L 2 .   ? 9.36199   19.36099  11.36242  0.988 41.68609  ? 401 ANA B C8  1 
HETATM 4295 C  C9  . ANA L 2 .   ? 10.23392  20.25658  12.21529  0.988 45.19722  ? 401 ANA B C9  1 
HETATM 4296 C  C10 . ANA L 2 .   ? 10.15232  14.27532  12.75969  0.988 29.62036  ? 401 ANA B C10 1 
HETATM 4297 C  C11 . ANA L 2 .   ? 11.57885  13.84903  12.94652  0.988 27.27983  ? 401 ANA B C11 1 
HETATM 4298 C  C12 . ANA L 2 .   ? 5.72783   18.66983  8.48538   0.988 46.59751  ? 401 ANA B C12 1 
HETATM 4299 C  CA4 . ANA L 2 .   ? 7.43891   12.35369  10.01730  0.988 30.22516  ? 401 ANA B CA4 1 
HETATM 4300 C  CM4 . ANA L 2 .   ? 6.94930   11.16317  10.77024  0.988 29.88803  ? 401 ANA B CM4 1 
HETATM 4301 N  N5  . ANA L 2 .   ? 9.89917   15.00381  11.67314  0.988 27.91326  ? 401 ANA B N5  1 
HETATM 4302 O  O1A . ANA L 2 .   ? 8.69553   17.87243  7.95768   0.988 41.52430  ? 401 ANA B O1A 1 
HETATM 4303 O  O1B . ANA L 2 .   ? 7.81309   16.19330  7.03793   0.988 42.07718  ? 401 ANA B O1B 1 
HETATM 4304 O  O2  . ANA L 2 .   ? 5.70190   17.29881  8.87526   0.988 43.97455  ? 401 ANA B O2  1 
HETATM 4305 O  O4  . ANA L 2 .   ? 7.59778   13.41361  10.83168  0.988 28.83966  ? 401 ANA B O4  1 
HETATM 4306 O  O6  . ANA L 2 .   ? 7.50890   17.48907  10.33240  0.988 36.14346  ? 401 ANA B O6  1 
HETATM 4307 O  O7  . ANA L 2 .   ? 8.24025   17.95198  12.97313  0.988 36.87753  ? 401 ANA B O7  1 
HETATM 4308 O  O8  . ANA L 2 .   ? 9.89329   19.29737  10.03425  0.988 41.67307  ? 401 ANA B O8  1 
HETATM 4309 O  O9  . ANA L 2 .   ? 11.57116  19.76445  12.26979  0.988 46.90426  ? 401 ANA B O9  1 
HETATM 4310 O  O10 . ANA L 2 .   ? 9.27421   13.95837  13.54988  0.988 28.07896  ? 401 ANA B O10 1 
HETATM 4311 O  OA4 . ANA L 2 .   ? 7.70540   12.38833  8.85107   0.988 31.10316  ? 401 ANA B OA4 1 
HETATM 4312 ZN ZN  . ZN  M 3 .   ? 28.61744  11.74875  -3.12529  0.869 72.43137  ? 402 ZN  B ZN  1 
HETATM 4313 C  C   . ACT N 4 .   ? 15.61618  21.28172  4.67384   1.000 64.55902  ? 403 ACT B C   1 
HETATM 4314 O  O   . ACT N 4 .   ? 15.20088  22.17591  5.44619   1.000 63.44728  ? 403 ACT B O   1 
HETATM 4315 O  OXT . ACT N 4 .   ? 14.91048  21.03524  3.66724   1.000 66.31042  ? 403 ACT B OXT 1 
HETATM 4316 C  CH3 . ACT N 4 .   ? 16.88151  20.53774  4.95354   1.000 63.65074  ? 403 ACT B CH3 1 
HETATM 4317 CL CL  . CL  O 5 .   ? 27.58068  10.12186  -0.64553  1.000 56.81934  ? 404 CL  B CL  1 
HETATM 4318 C  C1  . ANA P 2 .   ? -1.28681  16.06960  15.41046  0.953 39.05010  ? 401 ANA C C1  1 
HETATM 4319 C  C2  . ANA P 2 .   ? -1.29594  14.99392  14.31146  0.953 36.37110  ? 401 ANA C C2  1 
HETATM 4320 C  C3  . ANA P 2 .   ? 0.00333   14.22202  14.21575  0.953 32.52990  ? 401 ANA C C3  1 
HETATM 4321 C  C4  . ANA P 2 .   ? 0.20637   13.29257  15.39945  0.953 30.91294  ? 401 ANA C C4  1 
HETATM 4322 C  C5  . ANA P 2 .   ? -1.04680  12.47038  15.69722  0.953 31.96565  ? 401 ANA C C5  1 
HETATM 4323 C  C6  . ANA P 2 .   ? -2.29774  13.35290  15.75379  0.953 34.31148  ? 401 ANA C C6  1 
HETATM 4324 C  C7  . ANA P 2 .   ? -3.57656  12.53010  15.81146  0.953 37.05287  ? 401 ANA C C7  1 
HETATM 4325 C  C8  . ANA P 2 .   ? -4.80226  13.44259  15.83143  0.953 39.94284  ? 401 ANA C C8  1 
HETATM 4326 C  C9  . ANA P 2 .   ? -6.04455  12.77817  16.38523  0.953 43.99048  ? 401 ANA C C9  1 
HETATM 4327 C  C10 . ANA P 2 .   ? -0.68392  10.43506  17.05846  0.953 28.89897  ? 401 ANA C C10 1 
HETATM 4328 C  C11 . ANA P 2 .   ? -0.66857  9.89645   18.45647  0.953 26.91853  ? 401 ANA C C11 1 
HETATM 4329 C  C12 . ANA P 2 .   ? -2.65413  16.47371  13.00179  0.953 42.68079  ? 401 ANA C C12 1 
HETATM 4330 C  CA4 . ANA P 2 .   ? 2.52783   12.76166  15.14182  0.953 34.40352  ? 401 ANA C CA4 1 
HETATM 4331 C  CM4 . ANA P 2 .   ? 3.46692   11.68710  14.70968  0.953 36.19681  ? 401 ANA C CM4 1 
HETATM 4332 N  N5  . ANA P 2 .   ? -0.88532  11.75154  16.95351  0.953 29.37522  ? 401 ANA C N5  1 
HETATM 4333 O  O1A . ANA P 2 .   ? -2.28402  16.31042  16.07323  0.953 41.98144  ? 401 ANA C O1A 1 
HETATM 4334 O  O1B . ANA P 2 .   ? -0.28191  16.70559  15.59530  0.953 39.64167  ? 401 ANA C O1B 1 
HETATM 4335 O  O2  . ANA P 2 .   ? -1.49015  15.64878  13.05798  0.953 40.59212  ? 401 ANA C O2  1 
HETATM 4336 O  O4  . ANA P 2 .   ? 1.24914   12.35618  15.04389  0.953 32.63453  ? 401 ANA C O4  1 
HETATM 4337 O  O6  . ANA P 2 .   ? -2.38938  14.09323  14.52142  0.953 33.73416  ? 401 ANA C O6  1 
HETATM 4338 O  O7  . ANA P 2 .   ? -3.65861  11.66426  14.67260  0.953 37.09059  ? 401 ANA C O7  1 
HETATM 4339 O  O8  . ANA P 2 .   ? -4.51076  14.60361  16.59891  0.953 40.75539  ? 401 ANA C O8  1 
HETATM 4340 O  O9  . ANA P 2 .   ? -5.88610  12.46014  17.76733  0.953 45.19634  ? 401 ANA C O9  1 
HETATM 4341 O  O10 . ANA P 2 .   ? -0.50650  9.70650   16.08257  0.953 28.73186  ? 401 ANA C O10 1 
HETATM 4342 O  OA4 . ANA P 2 .   ? 2.83849   13.83874  15.55295  0.953 34.80862  ? 401 ANA C OA4 1 
HETATM 4343 ZN ZN  . ZN  Q 3 .   ? 4.20211   19.30490  36.61317  0.969 32.20534  ? 402 ZN  C ZN  1 
HETATM 4344 C  C   . ACT R 4 .   ? 15.58239  -10.03060 35.55313  1.000 67.06247  ? 403 ACT C C   1 
HETATM 4345 O  O   . ACT R 4 .   ? 14.80458  -9.14970  35.98267  1.000 67.13463  ? 403 ACT C O   1 
HETATM 4346 O  OXT . ACT R 4 .   ? 15.05229  -11.11355 35.21892  1.000 67.59539  ? 403 ACT C OXT 1 
HETATM 4347 C  CH3 . ACT R 4 .   ? 17.06024  -9.80068  35.44470  1.000 66.46142  ? 403 ACT C CH3 1 
HETATM 4348 C  C   . ACT S 4 .   ? -6.19807  19.39598  22.83988  1.000 62.38763  ? 404 ACT C C   1 
HETATM 4349 O  O   . ACT S 4 .   ? -5.60083  18.50984  23.49819  1.000 63.85537  ? 404 ACT C O   1 
HETATM 4350 O  OXT . ACT S 4 .   ? -7.17380  18.99933  22.16426  1.000 62.11956  ? 404 ACT C OXT 1 
HETATM 4351 C  CH3 . ACT S 4 .   ? -5.75764  20.83135  22.82651  1.000 61.69390  ? 404 ACT C CH3 1 
HETATM 4352 C  C   . ACT T 4 .   ? 9.50258   26.70244  39.73695  1.000 60.64580  ? 405 ACT C C   1 
HETATM 4353 O  O   . ACT T 4 .   ? 9.08666   26.60477  38.56007  1.000 60.59387  ? 405 ACT C O   1 
HETATM 4354 O  OXT . ACT T 4 .   ? 10.71239  26.99161  39.86142  1.000 60.19784  ? 405 ACT C OXT 1 
HETATM 4355 C  CH3 . ACT T 4 .   ? 8.61116   26.47847  40.92462  1.000 60.51862  ? 405 ACT C CH3 1 
HETATM 4356 O  O   . HOH U 6 .   ? -5.16790  9.37572   44.26893  1.000 52.79443  ? 501 HOH A O   1 
HETATM 4357 O  O   . HOH U 6 .   ? -10.30659 -9.53420  8.95189   1.000 35.85905  ? 502 HOH A O   1 
HETATM 4358 O  O   . HOH U 6 .   ? -10.67836 -13.30348 29.07273  1.000 31.57332  ? 503 HOH A O   1 
HETATM 4359 O  O   . HOH U 6 .   ? -1.96268  -18.37833 40.06826  1.000 42.77472  ? 504 HOH A O   1 
HETATM 4360 O  O   . HOH U 6 .   ? 3.07590   2.23916   42.42962  1.000 36.93040  ? 505 HOH A O   1 
HETATM 4361 O  O   . HOH U 6 .   ? -5.522    -6.425    42.938    1.000 36.78162  ? 506 HOH A O   1 
HETATM 4362 O  O   . HOH U 6 .   ? -3.28270  -10.45582 14.77213  1.000 25.56552  ? 507 HOH A O   1 
HETATM 4363 O  O   . HOH U 6 .   ? 8.10046   -4.22269  14.87417  1.000 27.43798  ? 508 HOH A O   1 
HETATM 4364 O  O   . HOH U 6 .   ? -15.48327 -15.72726 15.65468  1.000 54.03364  ? 509 HOH A O   1 
HETATM 4365 O  O   . HOH U 6 .   ? -9.10598  -15.69614 11.32063  1.000 45.39905  ? 510 HOH A O   1 
HETATM 4366 O  O   . HOH U 6 .   ? -5.93546  6.69874   32.88880  1.000 61.67477  ? 511 HOH A O   1 
HETATM 4367 O  O   . HOH U 6 .   ? 4.31402   1.28838   12.03586  1.000 39.74872  ? 512 HOH A O   1 
HETATM 4368 O  O   . HOH U 6 .   ? -3.49732  -7.31079  3.86409   1.000 34.83234  ? 513 HOH A O   1 
HETATM 4369 O  O   . HOH U 6 .   ? 4.83175   5.14901   10.48432  1.000 36.54136  ? 514 HOH A O   1 
HETATM 4370 O  O   . HOH U 6 .   ? 1.64188   -9.99603  14.65828  1.000 33.13703  ? 515 HOH A O   1 
HETATM 4371 O  O   . HOH U 6 .   ? -1.72691  8.06705   31.83561  1.000 40.37926  ? 516 HOH A O   1 
HETATM 4372 O  O   . HOH U 6 .   ? 1.95473   -9.13109  42.34943  1.000 34.49252  ? 517 HOH A O   1 
HETATM 4373 O  O   . HOH U 6 .   ? -15.93735 -17.28472 23.68542  1.000 57.58023  ? 518 HOH A O   1 
HETATM 4374 O  O   . HOH U 6 .   ? 4.53792   -9.58048  14.15397  1.000 28.20610  ? 519 HOH A O   1 
HETATM 4375 O  O   . HOH U 6 .   ? -0.00251  3.70569   35.28485  1.000 28.13347  ? 520 HOH A O   1 
HETATM 4376 O  O   . HOH U 6 .   ? -11.63960 -18.97395 17.92353  1.000 50.50935  ? 521 HOH A O   1 
HETATM 4377 O  O   . HOH U 6 .   ? 4.72498   5.32602   1.54591   1.000 47.61022  ? 522 HOH A O   1 
HETATM 4378 O  O   . HOH U 6 .   ? 6.18622   8.82838   2.39545   1.000 32.86521  ? 523 HOH A O   1 
HETATM 4379 O  O   . HOH U 6 .   ? 7.37761   2.02748   27.24909  1.000 27.07623  ? 524 HOH A O   1 
HETATM 4380 O  O   . HOH U 6 .   ? 2.62745   -10.08974 17.35061  1.000 27.00294  ? 525 HOH A O   1 
HETATM 4381 O  O   . HOH U 6 .   ? -8.45409  4.49583   2.25867   1.000 43.83317  ? 526 HOH A O   1 
HETATM 4382 O  O   . HOH U 6 .   ? -4.57745  5.91313   28.53278  1.000 34.90470  ? 527 HOH A O   1 
HETATM 4383 O  O   . HOH U 6 .   ? -5.58352  5.34966   19.88595  1.000 27.53423  ? 528 HOH A O   1 
HETATM 4384 O  O   . HOH U 6 .   ? -10.87802 -0.35109  34.89369  1.000 52.56566  ? 529 HOH A O   1 
HETATM 4385 O  O   . HOH U 6 .   ? -5.16227  9.53468   13.94615  1.000 36.24812  ? 530 HOH A O   1 
HETATM 4386 O  O   . HOH U 6 .   ? -5.48655  -19.35245 33.82915  1.000 43.19270  ? 531 HOH A O   1 
HETATM 4387 O  O   . HOH U 6 .   ? 6.63074   4.71705   19.98048  1.000 26.55347  ? 532 HOH A O   1 
HETATM 4388 O  O   . HOH U 6 .   ? 6.14714   8.57229   7.68247   1.000 45.62168  ? 533 HOH A O   1 
HETATM 4389 O  O   . HOH U 6 .   ? -4.54923  2.63272   25.99822  1.000 23.48606  ? 534 HOH A O   1 
HETATM 4390 O  O   . HOH U 6 .   ? 3.74517   -1.30840  11.31847  1.000 21.90637  ? 535 HOH A O   1 
HETATM 4391 O  O   . HOH U 6 .   ? -7.18223  -5.57003  4.21784   1.000 38.43255  ? 536 HOH A O   1 
HETATM 4392 O  O   . HOH U 6 .   ? -13.98320 -3.27417  23.70212  1.000 42.20197  ? 537 HOH A O   1 
HETATM 4393 O  O   . HOH U 6 .   ? 5.76261   5.70690   41.29242  1.000 35.92498  ? 538 HOH A O   1 
HETATM 4394 O  O   . HOH U 6 .   ? -4.74230  -17.42171 30.12731  1.000 40.87989  ? 539 HOH A O   1 
HETATM 4395 O  O   . HOH U 6 .   ? -7.58201  -3.46935  5.08055   1.000 34.92660  ? 540 HOH A O   1 
HETATM 4396 O  O   . HOH U 6 .   ? -2.34621  -19.84436 30.63551  1.000 33.07208  ? 541 HOH A O   1 
HETATM 4397 O  O   . HOH U 6 .   ? -10.42749 -3.23707  3.05940   1.000 45.34392  ? 542 HOH A O   1 
HETATM 4398 O  O   . HOH U 6 .   ? -5.58312  -17.40994 18.83162  1.000 50.70409  ? 543 HOH A O   1 
HETATM 4399 O  O   . HOH U 6 .   ? -3.42772  -16.27160 32.41379  1.000 36.90304  ? 544 HOH A O   1 
HETATM 4400 O  O   . HOH U 6 .   ? -3.88911  -0.23264  31.51192  1.000 22.01805  ? 545 HOH A O   1 
HETATM 4401 O  O   . HOH U 6 .   ? 8.86750   1.29374   19.77641  1.000 31.67752  ? 546 HOH A O   1 
HETATM 4402 O  O   . HOH U 6 .   ? 1.28919   1.64095   21.44400  1.000 20.27358  ? 547 HOH A O   1 
HETATM 4403 O  O   . HOH U 6 .   ? 3.96131   6.99963   14.75474  1.000 37.58165  ? 548 HOH A O   1 
HETATM 4404 O  O   . HOH U 6 .   ? -2.95914  -8.25029  9.92435   1.000 27.44874  ? 549 HOH A O   1 
HETATM 4405 O  O   . HOH U 6 .   ? -6.66510  8.75453   16.14225  1.000 30.20579  ? 550 HOH A O   1 
HETATM 4406 O  O   . HOH U 6 .   ? -18.05367 -4.27446  9.98870   1.000 37.06944  ? 551 HOH A O   1 
HETATM 4407 O  O   . HOH U 6 .   ? 6.30881   4.78175   8.44741   1.000 28.23419  ? 552 HOH A O   1 
HETATM 4408 O  O   . HOH U 6 .   ? -16.01534 -6.04984  15.72999  1.000 27.23882  ? 553 HOH A O   1 
HETATM 4409 O  O   . HOH U 6 .   ? -6.70804  -0.07292  41.37834  1.000 52.50226  ? 554 HOH A O   1 
HETATM 4410 O  O   . HOH U 6 .   ? -12.35231 -13.32414 23.94857  1.000 46.20082  ? 555 HOH A O   1 
HETATM 4411 O  O   . HOH U 6 .   ? -6.90895  6.63539   3.08155   1.000 38.34750  ? 556 HOH A O   1 
HETATM 4412 O  O   . HOH U 6 .   ? -4.42467  -16.73768 40.20455  1.000 42.51671  ? 557 HOH A O   1 
HETATM 4413 O  O   . HOH U 6 .   ? -8.96610  -1.77731  41.85340  1.000 44.38283  ? 558 HOH A O   1 
HETATM 4414 O  O   . HOH U 6 .   ? -11.11992 4.64961   2.34211   1.000 38.39615  ? 559 HOH A O   1 
HETATM 4415 O  O   . HOH U 6 .   ? 0.50295   1.53431   42.19076  1.000 37.08167  ? 560 HOH A O   1 
HETATM 4416 O  O   . HOH U 6 .   ? -20.56964 -6.27759  16.54845  1.000 45.78718  ? 561 HOH A O   1 
HETATM 4417 O  O   . HOH U 6 .   ? -21.40374 -11.90306 21.25257  1.000 48.84659  ? 562 HOH A O   1 
HETATM 4418 O  O   . HOH U 6 .   ? -8.73872  7.48774   21.80371  1.000 53.70389  ? 563 HOH A O   1 
HETATM 4419 O  O   . HOH U 6 .   ? -15.41368 6.16015   18.56520  1.000 43.15060  ? 564 HOH A O   1 
HETATM 4420 O  O   . HOH U 6 .   ? -16.41878 3.63408   18.07773  1.000 45.52463  ? 565 HOH A O   1 
HETATM 4421 O  O   . HOH U 6 .   ? -2.08462  6.62141   37.99574  1.000 34.30202  ? 566 HOH A O   1 
HETATM 4422 O  O   . HOH U 6 .   ? -3.05642  -18.93075 33.12972  1.000 33.48083  ? 567 HOH A O   1 
HETATM 4423 O  O   . HOH U 6 .   ? -5.97326  7.97716   10.85455  1.000 30.30456  ? 568 HOH A O   1 
HETATM 4424 O  O   . HOH U 6 .   ? 1.03321   7.27804   17.06816  1.000 33.56241  ? 569 HOH A O   1 
HETATM 4425 O  O   . HOH U 6 .   ? -14.21376 -0.49945  22.79992  1.000 32.11753  ? 570 HOH A O   1 
HETATM 4426 O  O   . HOH U 6 .   ? 4.05757   -28.74134 23.76198  1.000 63.27678  ? 571 HOH A O   1 
HETATM 4427 O  O   . HOH U 6 .   ? -7.37880  -1.81708  2.74542   1.000 39.99994  ? 572 HOH A O   1 
HETATM 4428 O  O   . HOH U 6 .   ? 7.57127   -1.51768  15.20362  1.000 22.54002  ? 573 HOH A O   1 
HETATM 4429 O  O   . HOH U 6 .   ? 3.56599   -21.25647 35.99031  1.000 63.14639  ? 574 HOH A O   1 
HETATM 4430 O  O   . HOH U 6 .   ? -11.43770 -15.97331 29.12920  1.000 35.78738  ? 575 HOH A O   1 
HETATM 4431 O  O   . HOH U 6 .   ? -0.46342  12.63551  32.65656  1.000 46.05589  ? 576 HOH A O   1 
HETATM 4432 O  O   . HOH U 6 .   ? 4.94819   4.52176   15.28357  1.000 29.42225  ? 577 HOH A O   1 
HETATM 4433 O  O   . HOH U 6 .   ? -3.98625  -21.00796 36.23237  1.000 41.00942  ? 578 HOH A O   1 
HETATM 4434 O  O   . HOH U 6 .   ? -5.64671  -20.55360 12.55171  1.000 49.76584  ? 579 HOH A O   1 
HETATM 4435 O  O   . HOH U 6 .   ? -1.59438  10.22512  1.39429   1.000 51.69919  ? 580 HOH A O   1 
HETATM 4436 O  O   . HOH U 6 .   ? 5.08301   7.51903   18.21276  1.000 35.70682  ? 581 HOH A O   1 
HETATM 4437 O  O   . HOH U 6 .   ? -7.99969  -15.70548 36.32129  1.000 43.80997  ? 582 HOH A O   1 
HETATM 4438 O  O   . HOH U 6 .   ? 3.99422   -28.51638 27.12681  1.000 59.67713  ? 583 HOH A O   1 
HETATM 4439 O  O   . HOH U 6 .   ? -6.102    -8.775    41.265    1.000 36.33591  ? 584 HOH A O   1 
HETATM 4440 O  O   . HOH U 6 .   ? -18.47406 -16.48163 18.16275  1.000 58.25385  ? 585 HOH A O   1 
HETATM 4441 O  O   . HOH U 6 .   ? 7.51513   -8.00717  42.73981  1.000 57.72028  ? 586 HOH A O   1 
HETATM 4442 O  O   . HOH U 6 .   ? -13.01243 -12.90418 26.62351  1.000 60.61640  ? 587 HOH A O   1 
HETATM 4443 O  O   . HOH U 6 .   ? 4.18577   -26.50714 17.08470  1.000 57.58932  ? 588 HOH A O   1 
HETATM 4444 O  O   . HOH U 6 .   ? -0.32161  5.99603   -0.64703  1.000 56.25838  ? 589 HOH A O   1 
HETATM 4445 O  O   . HOH U 6 .   ? -11.64757 -10.28341 3.70878   1.000 43.08218  ? 590 HOH A O   1 
HETATM 4446 O  O   . HOH U 6 .   ? 11.85633  -12.25165 37.04849  1.000 65.12275  ? 591 HOH A O   1 
HETATM 4447 O  O   . HOH U 6 .   ? -5.04918  8.08598   20.46689  1.000 30.85777  ? 592 HOH A O   1 
HETATM 4448 O  O   . HOH U 6 .   ? -6.08871  9.06441   22.92535  1.000 51.32261  ? 593 HOH A O   1 
HETATM 4449 O  O   . HOH U 6 .   ? -2.50745  -19.78788 11.08977  1.000 48.89793  ? 594 HOH A O   1 
HETATM 4450 O  O   . HOH U 6 .   ? 4.67077   8.19768   42.09967  1.000 64.68447  ? 595 HOH A O   1 
HETATM 4451 O  O   . HOH U 6 .   ? -11.50076 -18.33060 26.32656  1.000 43.38161  ? 596 HOH A O   1 
HETATM 4452 O  O   . HOH U 6 .   ? 7.51046   9.85577   4.60346   1.000 47.41977  ? 597 HOH A O   1 
HETATM 4453 O  O   . HOH U 6 .   ? -7.09150  3.84029   26.54259  1.000 48.26000  ? 598 HOH A O   1 
HETATM 4454 O  O   . HOH U 6 .   ? 7.50555   4.73484   17.31350  1.000 42.32295  ? 599 HOH A O   1 
HETATM 4455 O  O   . HOH U 6 .   ? -4.15834  7.17284   30.52860  1.000 40.25752  ? 600 HOH A O   1 
HETATM 4456 O  O   . HOH U 6 .   ? 2.240     15.451    42.187    1.000 46.25041  ? 601 HOH A O   1 
HETATM 4457 O  O   . HOH U 6 .   ? 5.14721   8.78016   13.00811  1.000 42.26785  ? 602 HOH A O   1 
HETATM 4458 O  O   . HOH V 6 .   ? 26.33861  8.54756   0.94754   1.000 51.26654  ? 501 HOH B O   1 
HETATM 4459 O  O   . HOH V 6 .   ? 12.74810  7.14307   13.02104  1.000 41.60936  ? 502 HOH B O   1 
HETATM 4460 O  O   . HOH V 6 .   ? 24.57696  -17.39112 8.65961   1.000 59.76286  ? 503 HOH B O   1 
HETATM 4461 O  O   . HOH V 6 .   ? 13.89995  -19.29526 20.48237  1.000 50.52972  ? 504 HOH B O   1 
HETATM 4462 O  O   . HOH V 6 .   ? 13.72049  -24.37676 7.94688   1.000 44.28311  ? 505 HOH B O   1 
HETATM 4463 O  O   . HOH V 6 .   ? 21.34837  -18.35710 19.23327  1.000 58.55448  ? 506 HOH B O   1 
HETATM 4464 O  O   . HOH V 6 .   ? 23.77092  13.20526  4.04769   1.000 40.68490  ? 507 HOH B O   1 
HETATM 4465 O  O   . HOH V 6 .   ? 16.816    21.273    -9.043    1.000 44.59713  ? 508 HOH B O   1 
HETATM 4466 O  O   . HOH V 6 .   ? 22.97909  1.64854   11.77323  1.000 39.93243  ? 509 HOH B O   1 
HETATM 4467 O  O   . HOH V 6 .   ? 29.73223  8.01609   -1.99093  1.000 56.97885  ? 510 HOH B O   1 
HETATM 4468 O  O   . HOH V 6 .   ? 21.60053  13.22305  3.01482   1.000 33.67446  ? 511 HOH B O   1 
HETATM 4469 O  O   . HOH V 6 .   ? 0.72160   -12.14177 6.61596   1.000 39.48681  ? 512 HOH B O   1 
HETATM 4470 O  O   . HOH V 6 .   ? 16.49094  2.66519   16.95865  1.000 29.10408  ? 513 HOH B O   1 
HETATM 4471 O  O   . HOH V 6 .   ? 24.63148  -10.71431 20.69424  1.000 44.23066  ? 514 HOH B O   1 
HETATM 4472 O  O   . HOH V 6 .   ? 31.37109  -11.25595 12.63314  1.000 62.47852  ? 515 HOH B O   1 
HETATM 4473 O  O   . HOH V 6 .   ? 22.51617  9.21606   -7.88594  1.000 37.21005  ? 516 HOH B O   1 
HETATM 4474 O  O   . HOH V 6 .   ? 4.34452   -13.28264 5.12054   1.000 31.27246  ? 517 HOH B O   1 
HETATM 4475 O  O   . HOH V 6 .   ? 9.71572   -0.34773  16.26796  1.000 30.13103  ? 518 HOH B O   1 
HETATM 4476 O  O   . HOH V 6 .   ? 22.23374  1.88284   14.42923  1.000 30.20218  ? 519 HOH B O   1 
HETATM 4477 O  O   . HOH V 6 .   ? 6.99114   -6.98223  13.75358  1.000 25.71396  ? 520 HOH B O   1 
HETATM 4478 O  O   . HOH V 6 .   ? 12.14085  18.36108  14.41406  1.000 38.00312  ? 521 HOH B O   1 
HETATM 4479 O  O   . HOH V 6 .   ? 14.68443  19.00500  2.01068   1.000 50.86823  ? 522 HOH B O   1 
HETATM 4480 O  O   . HOH V 6 .   ? 9.51415   9.80956   13.29418  1.000 31.76598  ? 523 HOH B O   1 
HETATM 4481 O  O   . HOH V 6 .   ? -8.78287  -15.73676 8.97554   1.000 44.42446  ? 524 HOH B O   1 
HETATM 4482 O  O   . HOH V 6 .   ? 6.51134   6.85601   11.54259  1.000 35.24785  ? 525 HOH B O   1 
HETATM 4483 O  O   . HOH V 6 .   ? 6.77588   13.72483  14.39716  1.000 37.73399  ? 526 HOH B O   1 
HETATM 4484 O  O   . HOH V 6 .   ? 8.16427   19.90227  4.56966   1.000 59.10495  ? 527 HOH B O   1 
HETATM 4485 O  O   . HOH V 6 .   ? 2.99174   -9.36328  -0.73423  1.000 44.27511  ? 528 HOH B O   1 
HETATM 4486 O  O   . HOH V 6 .   ? 22.12562  -1.09839  12.21699  1.000 35.85859  ? 529 HOH B O   1 
HETATM 4487 O  O   . HOH V 6 .   ? 8.42431   2.06544   1.61436   1.000 26.93994  ? 530 HOH B O   1 
HETATM 4488 O  O   . HOH V 6 .   ? -0.72726  -18.52543 9.67032   1.000 50.09233  ? 531 HOH B O   1 
HETATM 4489 O  O   . HOH V 6 .   ? 6.73076   0.66416   13.64238  1.000 25.47149  ? 532 HOH B O   1 
HETATM 4490 O  O   . HOH V 6 .   ? 7.97838   19.06233  15.43008  1.000 33.69750  ? 533 HOH B O   1 
HETATM 4491 O  O   . HOH V 6 .   ? -0.79939  -6.61622  3.35898   1.000 35.23828  ? 534 HOH B O   1 
HETATM 4492 O  O   . HOH V 6 .   ? 8.89213   -4.55881  2.12233   1.000 27.58885  ? 535 HOH B O   1 
HETATM 4493 O  O   . HOH V 6 .   ? 4.16340   -20.41169 4.62484   1.000 42.50463  ? 536 HOH B O   1 
HETATM 4494 O  O   . HOH V 6 .   ? 6.61636   10.87560  6.82412   1.000 44.95834  ? 537 HOH B O   1 
HETATM 4495 O  O   . HOH V 6 .   ? 2.69508   -20.89799 7.01336   1.000 50.67233  ? 538 HOH B O   1 
HETATM 4496 O  O   . HOH V 6 .   ? 10.22082  -1.22005  8.62665   1.000 23.14101  ? 539 HOH B O   1 
HETATM 4497 O  O   . HOH V 6 .   ? 22.22836  -16.19549 7.61192   1.000 38.82809  ? 540 HOH B O   1 
HETATM 4498 O  O   . HOH V 6 .   ? 15.40651  7.24412   13.00163  1.000 20.38592  ? 541 HOH B O   1 
HETATM 4499 O  O   . HOH V 6 .   ? 9.81340   -10.76392 2.36324   1.000 27.25922  ? 542 HOH B O   1 
HETATM 4500 O  O   . HOH V 6 .   ? 24.07178  -16.77898 5.92965   1.000 47.16835  ? 543 HOH B O   1 
HETATM 4501 O  O   . HOH V 6 .   ? 6.51925   6.74762   0.63379   1.000 26.69641  ? 544 HOH B O   1 
HETATM 4502 O  O   . HOH V 6 .   ? 6.22052   7.26375   -2.16659  1.000 49.74339  ? 545 HOH B O   1 
HETATM 4503 O  O   . HOH V 6 .   ? 10.20038  11.80402  15.09316  1.000 29.46826  ? 546 HOH B O   1 
HETATM 4504 O  O   . HOH V 6 .   ? -0.09186  -13.27904 8.75573   1.000 34.44280  ? 547 HOH B O   1 
HETATM 4505 O  O   . HOH V 6 .   ? 24.46733  1.93846   6.84263   1.000 46.07819  ? 548 HOH B O   1 
HETATM 4506 O  O   . HOH V 6 .   ? 22.25405  3.35880   -6.34320  1.000 33.96693  ? 549 HOH B O   1 
HETATM 4507 O  O   . HOH V 6 .   ? 23.66602  6.80803   7.62973   1.000 34.73437  ? 550 HOH B O   1 
HETATM 4508 O  O   . HOH V 6 .   ? 8.77398   11.40648  2.15671   1.000 29.28989  ? 551 HOH B O   1 
HETATM 4509 O  O   . HOH V 6 .   ? 1.10143   -15.09803 2.00990   1.000 43.65093  ? 552 HOH B O   1 
HETATM 4510 O  O   . HOH V 6 .   ? 12.53889  18.87865  3.03026   1.000 49.17614  ? 553 HOH B O   1 
HETATM 4511 O  O   . HOH V 6 .   ? 5.03808   -5.91580  1.06246   1.000 40.67721  ? 554 HOH B O   1 
HETATM 4512 O  O   . HOH V 6 .   ? 11.33438  -1.47466  -5.78786  1.000 48.33954  ? 555 HOH B O   1 
HETATM 4513 O  O   . HOH V 6 .   ? 12.994    23.704    -5.093    1.000 37.02745  ? 556 HOH B O   1 
HETATM 4514 O  O   . HOH V 6 .   ? 22.66038  15.73026  0.73076   1.000 41.78483  ? 557 HOH B O   1 
HETATM 4515 O  O   . HOH V 6 .   ? 13.84499  3.18607   16.13449  1.000 25.79229  ? 558 HOH B O   1 
HETATM 4516 O  O   . HOH V 6 .   ? 14.56061  -1.69713  -6.37723  1.000 32.19032  ? 559 HOH B O   1 
HETATM 4517 O  O   . HOH V 6 .   ? 15.28041  18.97897  -0.85994  1.000 38.20140  ? 560 HOH B O   1 
HETATM 4518 O  O   . HOH V 6 .   ? 8.69379   5.26140   12.79326  1.000 28.33608  ? 561 HOH B O   1 
HETATM 4519 O  O   . HOH V 6 .   ? 24.59963  -9.74785  -4.47956  1.000 69.76503  ? 562 HOH B O   1 
HETATM 4520 O  O   . HOH V 6 .   ? 11.13504  10.68308  -13.37593 1.000 50.72065  ? 563 HOH B O   1 
HETATM 4521 O  O   . HOH V 6 .   ? 21.11298  16.13005  11.95732  1.000 61.12422  ? 564 HOH B O   1 
HETATM 4522 O  O   . HOH V 6 .   ? 20.52805  16.08402  3.30915   1.000 42.38647  ? 565 HOH B O   1 
HETATM 4523 O  O   . HOH V 6 .   ? 29.69633  -11.60242 -1.09917  1.000 48.26486  ? 566 HOH B O   1 
HETATM 4524 O  O   . HOH V 6 .   ? 18.02213  -15.94725 23.18721  1.000 53.28234  ? 567 HOH B O   1 
HETATM 4525 O  O   . HOH V 6 .   ? 3.74447   0.27338   0.45843   1.000 45.23799  ? 568 HOH B O   1 
HETATM 4526 O  O   . HOH V 6 .   ? 17.308    25.076    -5.363    1.000 42.25360  ? 569 HOH B O   1 
HETATM 4527 O  O   . HOH V 6 .   ? 3.13286   -7.11234  1.03631   1.000 41.40592  ? 570 HOH B O   1 
HETATM 4528 O  O   . HOH V 6 .   ? 16.34779  -24.64854 1.02505   1.000 51.18295  ? 571 HOH B O   1 
HETATM 4529 O  O   . HOH V 6 .   ? 8.53829   14.51444  -7.13197  1.000 62.22613  ? 572 HOH B O   1 
HETATM 4530 O  O   . HOH V 6 .   ? 20.01502  -20.38228 15.24388  1.000 55.21909  ? 573 HOH B O   1 
HETATM 4531 O  O   . HOH V 6 .   ? 6.84577   12.00460  3.95279   1.000 51.91631  ? 574 HOH B O   1 
HETATM 4532 O  O   . HOH V 6 .   ? 5.64485   2.50142   1.69219   1.000 34.74517  ? 575 HOH B O   1 
HETATM 4533 O  O   . HOH V 6 .   ? 15.779    25.630    -4.287    1.000 42.81564  ? 576 HOH B O   1 
HETATM 4534 O  O   . HOH V 6 .   ? 27.39618  13.68437  -1.57392  1.000 62.92465  ? 577 HOH B O   1 
HETATM 4535 O  O   . HOH V 6 .   ? 8.09391   -4.44978  -0.36332  1.000 40.18632  ? 578 HOH B O   1 
HETATM 4536 O  O   . HOH V 6 .   ? 7.39225   3.04502   14.66317  1.000 44.94658  ? 579 HOH B O   1 
HETATM 4537 O  O   . HOH V 6 .   ? -0.05681  -20.55776 7.55195   1.000 55.39889  ? 580 HOH B O   1 
HETATM 4538 O  O   . HOH W 6 .   ? 28.32655  9.40897   15.94976  1.000 37.16232  ? 501 HOH C O   1 
HETATM 4539 O  O   . HOH W 6 .   ? 5.21779   17.79446  35.99706  1.000 31.31741  ? 502 HOH C O   1 
HETATM 4540 O  O   . HOH W 6 .   ? -3.61680  20.75765  26.61764  1.000 38.38036  ? 503 HOH C O   1 
HETATM 4541 O  O   . HOH W 6 .   ? 0.04251   8.83020   13.79186  1.000 41.28808  ? 504 HOH C O   1 
HETATM 4542 O  O   . HOH W 6 .   ? 19.63963  2.90866   16.65392  1.000 26.41789  ? 505 HOH C O   1 
HETATM 4543 O  O   . HOH W 6 .   ? 30.03333  18.47337  23.47582  1.000 55.47864  ? 506 HOH C O   1 
HETATM 4544 O  O   . HOH W 6 .   ? 7.03612   25.72053  37.27267  1.000 45.73409  ? 507 HOH C O   1 
HETATM 4545 O  O   . HOH W 6 .   ? 15.80876  9.14795   39.90753  1.000 43.31459  ? 508 HOH C O   1 
HETATM 4546 O  O   . HOH W 6 .   ? 28.70394  7.88266   0.99471   1.000 52.74623  ? 509 HOH C O   1 
HETATM 4547 O  O   . HOH W 6 .   ? 10.33254  10.00670  33.47824  1.000 25.52843  ? 510 HOH C O   1 
HETATM 4548 O  O   . HOH W 6 .   ? 36.48021  2.63758   25.98142  1.000 41.41054  ? 511 HOH C O   1 
HETATM 4549 O  O   . HOH W 6 .   ? 26.55896  7.29855   38.04359  1.000 38.13138  ? 512 HOH C O   1 
HETATM 4550 O  O   . HOH W 6 .   ? 8.55930   3.33450   30.29493  1.000 25.98315  ? 513 HOH C O   1 
HETATM 4551 O  O   . HOH W 6 .   ? 12.10445  2.30122   18.04538  1.000 35.68634  ? 514 HOH C O   1 
HETATM 4552 O  O   . HOH W 6 .   ? 25.88096  18.34680  29.63103  1.000 45.92739  ? 515 HOH C O   1 
HETATM 4553 O  O   . HOH W 6 .   ? 24.94830  14.83845  20.64777  1.000 36.79986  ? 516 HOH C O   1 
HETATM 4554 O  O   . HOH W 6 .   ? 26.12883  14.57235  36.29799  1.000 42.54273  ? 517 HOH C O   1 
HETATM 4555 O  O   . HOH W 6 .   ? 9.64645   5.68870   31.54770  1.000 35.37992  ? 518 HOH C O   1 
HETATM 4556 O  O   . HOH W 6 .   ? 7.93806   1.75035   24.12120  1.000 27.76602  ? 519 HOH C O   1 
HETATM 4557 O  O   . HOH W 6 .   ? 0.652     18.339    37.651    1.000 27.98040  ? 520 HOH C O   1 
HETATM 4558 O  O   . HOH W 6 .   ? 23.58499  13.43663  10.44014  1.000 40.44999  ? 521 HOH C O   1 
HETATM 4559 O  O   . HOH W 6 .   ? 14.13167  17.09318  18.55800  1.000 25.79251  ? 522 HOH C O   1 
HETATM 4560 O  O   . HOH W 6 .   ? 7.45202   26.58912  33.51895  1.000 44.03054  ? 523 HOH C O   1 
HETATM 4561 O  O   . HOH W 6 .   ? 7.29020   9.57550   14.54993  1.000 33.46604  ? 524 HOH C O   1 
HETATM 4562 O  O   . HOH W 6 .   ? 34.107    -0.016    18.524    1.000 32.45682  ? 525 HOH C O   1 
HETATM 4563 O  O   . HOH W 6 .   ? 6.57957   7.12950   20.96655  1.000 39.33724  ? 526 HOH C O   1 
HETATM 4564 O  O   . HOH W 6 .   ? 14.96056  9.17872   19.69236  1.000 22.00820  ? 527 HOH C O   1 
HETATM 4565 O  O   . HOH W 6 .   ? 12.08512  4.50663   30.96460  1.000 25.62156  ? 528 HOH C O   1 
HETATM 4566 O  O   . HOH W 6 .   ? 12.47729  5.47628   15.28573  1.000 28.45801  ? 529 HOH C O   1 
HETATM 4567 O  O   . HOH W 6 .   ? 10.52232  19.65817  16.24136  1.000 33.47306  ? 530 HOH C O   1 
HETATM 4568 O  O   . HOH W 6 .   ? 3.43129   26.84683  15.62826  1.000 50.49523  ? 531 HOH C O   1 
HETATM 4569 O  O   . HOH W 6 .   ? 22.38717  15.27527  16.44978  1.000 39.05754  ? 532 HOH C O   1 
HETATM 4570 O  O   . HOH W 6 .   ? 5.94525   11.18242  31.81164  1.000 30.19428  ? 533 HOH C O   1 
HETATM 4571 O  O   . HOH W 6 .   ? 15.86348  7.90042   42.37322  1.000 45.53964  ? 534 HOH C O   1 
HETATM 4572 O  O   . HOH W 6 .   ? 5.06484   7.11579   23.12944  1.000 19.83488  ? 535 HOH C O   1 
HETATM 4573 O  O   . HOH W 6 .   ? 25.81902  12.24174  21.38787  1.000 25.92503  ? 536 HOH C O   1 
HETATM 4574 O  O   . HOH W 6 .   ? 3.38709   8.43969   16.89811  1.000 32.71464  ? 537 HOH C O   1 
HETATM 4575 O  O   . HOH W 6 .   ? -2.61244  21.56246  22.98357  1.000 40.15637  ? 538 HOH C O   1 
HETATM 4576 O  O   . HOH W 6 .   ? 20.24211  14.41635  20.05453  1.000 26.01095  ? 539 HOH C O   1 
HETATM 4577 O  O   . HOH W 6 .   ? 11.78887  -4.64436  39.71632  1.000 50.07323  ? 540 HOH C O   1 
HETATM 4578 O  O   . HOH W 6 .   ? -1.77475  31.86481  27.52422  1.000 45.82890  ? 541 HOH C O   1 
HETATM 4579 O  O   . HOH W 6 .   ? 12.83330  23.36021  33.39530  1.000 33.94642  ? 542 HOH C O   1 
HETATM 4580 O  O   . HOH W 6 .   ? 36.50366  4.84666   35.58638  1.000 56.08200  ? 543 HOH C O   1 
HETATM 4581 O  O   . HOH W 6 .   ? -2.00487  24.26749  23.84168  1.000 32.59006  ? 544 HOH C O   1 
HETATM 4582 O  O   . HOH W 6 .   ? 24.19778  14.93126  14.60760  1.000 41.14431  ? 545 HOH C O   1 
HETATM 4583 O  O   . HOH W 6 .   ? -1.51025  18.33157  28.42705  1.000 36.75953  ? 546 HOH C O   1 
HETATM 4584 O  O   . HOH W 6 .   ? 27.09170  4.30838   39.56767  1.000 41.10901  ? 547 HOH C O   1 
HETATM 4585 O  O   . HOH W 6 .   ? 29.52930  4.90717   38.41254  1.000 39.37714  ? 548 HOH C O   1 
HETATM 4586 O  O   . HOH W 6 .   ? 0.68612   17.78920  29.72952  1.000 36.78796  ? 549 HOH C O   1 
HETATM 4587 O  O   . HOH W 6 .   ? 14.39574  27.61383  34.57516  1.000 45.72440  ? 550 HOH C O   1 
HETATM 4588 O  O   . HOH W 6 .   ? 10.34636  33.19649  24.10823  1.000 54.85496  ? 551 HOH C O   1 
HETATM 4589 O  O   . HOH W 6 .   ? 5.01082   19.81384  17.69806  1.000 29.99116  ? 552 HOH C O   1 
HETATM 4590 O  O   . HOH W 6 .   ? 33.29524  -2.59253  17.24062  1.000 44.18065  ? 553 HOH C O   1 
HETATM 4591 O  O   . HOH W 6 .   ? 26.28217  6.08644   41.49389  1.000 47.80868  ? 554 HOH C O   1 
HETATM 4592 O  O   . HOH W 6 .   ? 19.11146  -8.79690  29.54322  1.000 58.42716  ? 555 HOH C O   1 
HETATM 4593 O  O   . HOH W 6 .   ? -3.80367  23.70116  26.29878  1.000 48.80437  ? 556 HOH C O   1 
HETATM 4594 O  O   . HOH W 6 .   ? 20.12303  -10.41583 35.33461  1.000 47.65179  ? 557 HOH C O   1 
HETATM 4595 O  O   . HOH W 6 .   ? -1.72990  19.47314  33.13075  1.000 40.76101  ? 558 HOH C O   1 
HETATM 4596 O  O   . HOH W 6 .   ? 26.57399  14.19291  39.04943  1.000 42.30029  ? 559 HOH C O   1 
HETATM 4597 O  O   . HOH W 6 .   ? 30.25252  -3.73890  30.70718  1.000 50.09087  ? 560 HOH C O   1 
HETATM 4598 O  O   . HOH W 6 .   ? 8.18772   3.14342   21.61310  1.000 22.73354  ? 561 HOH C O   1 
HETATM 4599 O  O   . HOH W 6 .   ? 35.03284  6.69308   16.51453  1.000 38.69323  ? 562 HOH C O   1 
HETATM 4600 O  O   . HOH W 6 .   ? 19.19211  22.70150  26.53331  1.000 44.71287  ? 563 HOH C O   1 
HETATM 4601 O  O   . HOH W 6 .   ? -4.68613  25.66356  27.68121  1.000 53.09952  ? 564 HOH C O   1 
HETATM 4602 O  O   . HOH W 6 .   ? 8.21541   7.00012   42.69430  1.000 47.87518  ? 565 HOH C O   1 
HETATM 4603 O  O   . HOH W 6 .   ? 38.13606  8.86458   29.32257  1.000 49.31680  ? 566 HOH C O   1 
HETATM 4604 O  O   . HOH W 6 .   ? 18.17401  22.89727  22.01227  1.000 56.31746  ? 567 HOH C O   1 
HETATM 4605 O  O   . HOH W 6 .   ? -0.05100  25.22365  16.58643  1.000 42.16614  ? 568 HOH C O   1 
HETATM 4606 O  O   . HOH W 6 .   ? 7.95560   7.48084   16.68902  1.000 28.43738  ? 569 HOH C O   1 
HETATM 4607 O  O   . HOH W 6 .   ? 13.23806  -2.60082  45.55788  1.000 47.05609  ? 570 HOH C O   1 
HETATM 4608 O  O   . HOH W 6 .   ? -2.52100  21.04708  20.50774  1.000 45.05619  ? 571 HOH C O   1 
HETATM 4609 O  O   . HOH W 6 .   ? 36.71451  14.83479  22.20330  1.000 51.03755  ? 572 HOH C O   1 
HETATM 4610 O  O   . HOH W 6 .   ? -3.60773  10.88249  28.77891  1.000 55.67680  ? 573 HOH C O   1 
HETATM 4611 O  O   . HOH W 6 .   ? 24.08175  13.44204  41.67076  1.000 53.89573  ? 574 HOH C O   1 
HETATM 4612 O  O   . HOH W 6 .   ? 0.57600   16.32568  32.16264  1.000 37.97021  ? 575 HOH C O   1 
HETATM 4613 O  O   . HOH W 6 .   ? 11.18070  -0.09438  19.04061  1.000 45.91709  ? 576 HOH C O   1 
HETATM 4614 O  O   . HOH W 6 .   ? 16.81392  18.21691  14.70685  1.000 45.15898  ? 577 HOH C O   1 
HETATM 4615 O  O   . HOH W 6 .   ? 14.37571  17.38622  15.69693  1.000 28.88008  ? 578 HOH C O   1 
HETATM 4616 O  O   . HOH W 6 .   ? 30.51347  11.46837  -1.77565  1.000 72.45404  ? 579 HOH C O   1 
HETATM 4617 O  O   . HOH W 6 .   ? -1.69749  23.56719  19.24522  1.000 55.34220  ? 580 HOH C O   1 
HETATM 4618 O  O   . HOH W 6 .   ? 6.24793   17.25151  16.78696  1.000 40.31550  ? 581 HOH C O   1 
HETATM 4619 O  O   . HOH W 6 .   ? 27.18998  11.00770  43.41898  1.000 59.06641  ? 582 HOH C O   1 
HETATM 4620 O  O   . HOH W 6 .   ? -8.34638  10.99906  20.43138  1.000 54.29719  ? 583 HOH C O   1 
HETATM 4621 O  O   . HOH W 6 .   ? 9.49033   5.69252   15.53949  1.000 40.56741  ? 584 HOH C O   1 
HETATM 4622 O  O   . HOH W 6 .   ? 28.39240  8.27298   42.28583  1.000 58.70207  ? 585 HOH C O   1 
HETATM 4623 O  O   . HOH W 6 .   ? 24.42904  16.15356  18.36303  1.000 48.37493  ? 586 HOH C O   1 
HETATM 4624 O  O   . HOH W 6 .   ? 36.84874  11.48239  28.92116  1.000 47.19681  ? 587 HOH C O   1 
HETATM 4625 O  O   . HOH W 6 .   ? 21.04077  17.14002  19.59313  1.000 43.50468  ? 588 HOH C O   1 
HETATM 4626 O  O   . HOH W 6 .   ? 9.36578   2.65708   17.15116  1.000 51.62274  ? 589 HOH C O   1 
HETATM 4627 O  O   . HOH W 6 .   ? 33.55676  -3.26220  14.51465  1.000 48.37093  ? 590 HOH C 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 
6    N  N   . ASP A 182 ? 1.20910 1.00138 1.14418 0.10549  -0.00609 0.01658  182 ASP A N   
7    C  CA  . ASP A 182 ? 0.94013 0.76054 0.89125 0.10718  -0.01081 0.02027  182 ASP A CA  
8    C  C   . ASP A 182 ? 0.89114 0.71721 0.84033 0.09828  -0.01726 0.02475  182 ASP A C   
9    O  O   . ASP A 182 ? 0.62661 0.45755 0.57253 0.08728  -0.01702 0.02101  182 ASP A O   
10   C  CB  . ASP A 182 ? 0.75887 0.59587 0.71636 0.10388  -0.00721 0.01356  182 ASP A CB  
11   C  CG  . ASP A 182 ? 0.69366 0.55885 0.66710 0.10587  -0.01130 0.01692  182 ASP A CG  
12   O  OD1 . ASP A 182 ? 0.74571 0.61876 0.72573 0.10961  -0.01702 0.02442  182 ASP A OD1 
13   O  OD2 . ASP A 182 ? 0.85071 0.72993 0.82940 0.10325  -0.00884 0.01210  182 ASP A OD2 
14   N  N   . THR A 183 ? 0.61849 0.44388 0.56976 0.10294  -0.02292 0.03305  183 THR A N   
15   C  CA  . THR A 183 ? 0.76980 0.59875 0.71768 0.09454  -0.02871 0.03768  183 THR A CA  
16   C  C   . THR A 183 ? 0.64489 0.50036 0.60452 0.09111  -0.03173 0.03864  183 THR A C   
17   O  O   . THR A 183 ? 0.64234 0.50161 0.59911 0.08350  -0.03564 0.04188  183 THR A O   
18   C  CB  . THR A 183 ? 0.82719 0.64599 0.77190 0.09991  -0.03435 0.04673  183 THR A CB  
19   N  N   . ARG A 184 ? 0.48690 0.35959 0.45859 0.09612  -0.02956 0.03582  184 ARG A N   
20   C  CA  . ARG A 184 ? 0.42322 0.32030 0.40540 0.09288  -0.03203 0.03652  184 ARG A CA  
21   C  C   . ARG A 184 ? 0.44473 0.34886 0.42652 0.08448  -0.02809 0.02918  184 ARG A C   
22   O  O   . ARG A 184 ? 0.37337 0.29675 0.36340 0.08186  -0.02936 0.02915  184 ARG A O   
23   C  CB  . ARG A 184 ? 0.59162 0.50579 0.58853 0.10351  -0.03283 0.03911  184 ARG A CB  
24   C  CG  . ARG A 184 ? 0.72767 0.64181 0.72889 0.11139  -0.03856 0.04829  184 ARG A CG  
25   C  CD  . ARG A 184 ? 0.74994 0.68389 0.76793 0.12146  -0.03901 0.05083  184 ARG A CD  
26   N  N   . THR A 185 ? 0.38675 0.27584 0.35912 0.08003  -0.02360 0.02336  185 THR A N   
27   C  CA  . THR A 185 ? 0.38315 0.27868 0.35527 0.07186  -0.02044 0.01699  185 THR A CA  
28   C  C   . THR A 185 ? 0.41179 0.29216 0.37230 0.06202  -0.01928 0.01492  185 THR A C   
29   O  O   . THR A 185 ? 0.43102 0.29121 0.38117 0.06243  -0.01703 0.01333  185 THR A O   
30   C  CB  . THR A 185 ? 0.46971 0.36467 0.44295 0.07582  -0.01542 0.01093  185 THR A CB  
31   O  OG1 . THR A 185 ? 0.56576 0.47819 0.55127 0.08363  -0.01585 0.01228  185 THR A OG1 
32   C  CG2 . THR A 185 ? 0.42107 0.31943 0.39144 0.06584  -0.01298 0.00492  185 THR A CG2 
33   N  N   . LEU A 186 ? 0.35037 0.24043 0.31289 0.05321  -0.02026 0.01483  186 LEU A N   
34   C  CA  . LEU A 186 ? 0.36833 0.24976 0.32349 0.04290  -0.01823 0.01189  186 LEU A CA  
35   C  C   . LEU A 186 ? 0.41305 0.30565 0.37306 0.03862  -0.01581 0.00654  186 LEU A C   
36   O  O   . LEU A 186 ? 0.37927 0.29067 0.34937 0.03947  -0.01685 0.00686  186 LEU A O   
37   C  CB  . LEU A 186 ? 0.38605 0.27209 0.34182 0.03629  -0.02021 0.01562  186 LEU A CB  
38   C  CG  . LEU A 186 ? 0.72766 0.59739 0.67313 0.03267  -0.02118 0.01907  186 LEU A CG  
39   C  CD1 . LEU A 186 ? 0.39850 0.27824 0.34734 0.02571  -0.02158 0.02117  186 LEU A CD1 
40   C  CD2 . LEU A 186 ? 0.55407 0.40581 0.48901 0.02703  -0.01784 0.01510  186 LEU A CD2 
41   N  N   . TRP A 187 ? 0.32210 0.20331 0.27439 0.03327  -0.01293 0.00196  187 TRP A N   
42   C  CA  . TRP A 187 ? 0.31435 0.20633 0.27057 0.02853  -0.01147 -0.00256 187 TRP A CA  
43   C  C   . TRP A 187 ? 0.35133 0.23360 0.29980 0.01826  -0.00963 -0.00594 187 TRP A C   
44   O  O   . TRP A 187 ? 0.38847 0.25432 0.32768 0.01486  -0.00881 -0.00543 187 TRP A O   
45   C  CB  . TRP A 187 ? 0.33865 0.23211 0.29570 0.03570  -0.00964 -0.00577 187 TRP A CB  
46   C  CG  . TRP A 187 ? 0.34040 0.21245 0.28534 0.03796  -0.00607 -0.00934 187 TRP A CG  
47   C  CD1 . TRP A 187 ? 0.37576 0.22636 0.30869 0.03539  -0.00485 -0.00943 187 TRP A CD1 
48   C  CD2 . TRP A 187 ? 0.34914 0.21805 0.29179 0.04287  -0.00252 -0.01365 187 TRP A CD2 
49   N  NE1 . TRP A 187 ? 0.38246 0.21625 0.30564 0.03878  -0.00069 -0.01352 187 TRP A NE1 
50   C  CE2 . TRP A 187 ? 0.38449 0.22912 0.31353 0.04344  0.00107  -0.01624 187 TRP A CE2 
51   C  CE3 . TRP A 187 ? 0.40382 0.28738 0.35395 0.04660  -0.00151 -0.01570 187 TRP A CE3 
52   C  CZ2 . TRP A 187 ? 0.41340 0.24741 0.33604 0.04781  0.00614  -0.02095 187 TRP A CZ2 
53   C  CZ3 . TRP A 187 ? 0.40201 0.27578 0.34604 0.05065  0.00340  -0.02039 187 TRP A CZ3 
54   C  CH2 . TRP A 187 ? 0.47304 0.32193 0.40343 0.05140  0.00743  -0.02304 187 TRP A CH2 
55   N  N   . THR A 188 ? 0.36255 0.25622 0.31519 0.01267  -0.00936 -0.00899 188 THR A N   
56   C  CA  . THR A 188 ? 0.30551 0.19414 0.25266 0.00216  -0.00829 -0.01213 188 THR A CA  
57   C  C   . THR A 188 ? 0.53784 0.41199 0.47307 0.00098  -0.00574 -0.01738 188 THR A C   
58   O  O   . THR A 188 ? 0.55355 0.42400 0.48333 -0.00881 -0.00524 -0.02012 188 THR A O   
59   C  CB  . THR A 188 ? 0.33649 0.24604 0.29479 -0.00370 -0.01004 -0.01193 188 THR A CB  
60   O  OG1 . THR A 188 ? 0.32480 0.24512 0.28753 0.00158  -0.01056 -0.01340 188 THR A OG1 
61   C  CG2 . THR A 188 ? 0.29392 0.21572 0.26285 -0.00422 -0.01135 -0.00719 188 THR A CG2 
62   N  N   . THR A 189 ? 0.43678 0.30355 0.36830 0.01020  -0.00389 -0.01879 189 THR A N   
63   C  CA  . THR A 189 ? 0.44643 0.30249 0.36834 0.01088  -0.00041 -0.02421 189 THR A CA  
64   C  C   . THR A 189 ? 0.45359 0.32738 0.38168 0.00692  -0.00143 -0.02649 189 THR A C   
65   O  O   . THR A 189 ? 0.44738 0.33830 0.38483 0.00100  -0.00479 -0.02434 189 THR A O   
66   C  CB  . THR A 189 ? 0.48788 0.32202 0.39357 0.00283  0.00227  -0.02801 189 THR A CB  
67   O  OG1 . THR A 189 ? 0.55679 0.39970 0.46300 -0.00975 0.00040  -0.02951 189 THR A OG1 
68   C  CG2 . THR A 189 ? 0.51325 0.33086 0.41258 0.00368  0.00249  -0.02519 189 THR A CG2 
69   N  N   . PRO A 190 ? 0.41323 0.28292 0.33609 0.01013  0.00173  -0.03073 190 PRO A N   
70   C  CA  . PRO A 190 ? 0.45983 0.34593 0.38753 0.00658  0.00065  -0.03270 190 PRO A CA  
71   C  C   . PRO A 190 ? 0.45596 0.33693 0.37300 -0.00573 0.00089  -0.03705 190 PRO A C   
72   O  O   . PRO A 190 ? 0.52406 0.41490 0.44183 -0.00856 0.00048  -0.03920 190 PRO A O   
73   C  CB  . PRO A 190 ? 0.46558 0.34965 0.39330 0.01735  0.00462  -0.03481 190 PRO A CB  
74   C  CG  . PRO A 190 ? 0.62807 0.48767 0.54424 0.02237  0.00925  -0.03667 190 PRO A CG  
75   C  CD  . PRO A 190 ? 0.48379 0.33724 0.40002 0.02039  0.00638  -0.03247 190 PRO A CD  
76   N  N   . ASP A 191 ? 0.43821 0.30449 0.34498 -0.01385 0.00126  -0.03819 191 ASP A N   
77   C  CA  . ASP A 191 ? 0.45877 0.32061 0.35481 -0.02686 0.00091  -0.04199 191 ASP A CA  
78   C  C   . ASP A 191 ? 0.60472 0.48918 0.51290 -0.03563 -0.00506 -0.03841 191 ASP A C   
79   O  O   . ASP A 191 ? 0.53136 0.43351 0.45527 -0.03095 -0.00792 -0.03370 191 ASP A O   
80   C  CB  . ASP A 191 ? 0.53261 0.37011 0.41250 -0.03288 0.00372  -0.04462 191 ASP A CB  
81   C  CG  . ASP A 191 ? 0.73575 0.57344 0.62088 -0.03519 0.00141  -0.04032 191 ASP A CG  
82   O  OD1 . ASP A 191 ? 0.55958 0.41754 0.46021 -0.03592 -0.00271 -0.03572 191 ASP A OD1 
83   O  OD2 . ASP A 191 ? 0.83015 0.64641 0.70288 -0.03677 0.00422  -0.04171 191 ASP A OD2 
84   N  N   . THR A 192 ? 0.47973 0.36376 0.38079 -0.04870 -0.00700 -0.04028 192 THR A N   
85   C  CA  . THR A 192 ? 0.47603 0.38232 0.38980 -0.05689 -0.01289 -0.03624 192 THR A CA  
86   C  C   . THR A 192 ? 0.52193 0.42727 0.43683 -0.06657 -0.01482 -0.03404 192 THR A C   
87   O  O   . THR A 192 ? 0.48889 0.41157 0.41367 -0.07481 -0.01948 -0.03075 192 THR A O   
88   C  CB  . THR A 192 ? 0.52692 0.43962 0.43514 -0.06511 -0.01520 -0.03862 192 THR A CB  
89   O  OG1 . THR A 192 ? 0.54448 0.43607 0.43211 -0.07344 -0.01235 -0.04414 192 THR A OG1 
90   C  CG2 . THR A 192 ? 0.56282 0.48196 0.47370 -0.05598 -0.01372 -0.03989 192 THR A CG2 
91   N  N   . SER A 193 ? 0.51454 0.40078 0.42050 -0.06555 -0.01134 -0.03533 193 SER A N   
92   C  CA  . SER A 193 ? 0.48218 0.36635 0.38866 -0.07471 -0.01236 -0.03346 193 SER A CA  
93   C  C   . SER A 193 ? 0.41068 0.31480 0.33739 -0.07216 -0.01481 -0.02739 193 SER A C   
94   O  O   . SER A 193 ? 0.41152 0.31605 0.34434 -0.06149 -0.01324 -0.02538 193 SER A O   
95   C  CB  . SER A 193 ? 0.59979 0.45759 0.49139 -0.07276 -0.00768 -0.03603 193 SER A CB  
96   O  OG  . SER A 193 ? 0.76243 0.59981 0.63481 -0.07414 -0.00426 -0.04183 193 SER A OG  
97   N  N   . PRO A 194 ? 0.43248 0.35273 0.36975 -0.08174 -0.01831 -0.02421 194 PRO A N   
98   C  CA  . PRO A 194 ? 0.33632 0.27500 0.29330 -0.07898 -0.01946 -0.01852 194 PRO A CA  
99   C  C   . PRO A 194 ? 0.36305 0.28964 0.31854 -0.07434 -0.01558 -0.01765 194 PRO A C   
100  O  O   . PRO A 194 ? 0.39134 0.29916 0.33368 -0.07873 -0.01314 -0.02012 194 PRO A O   
101  C  CB  . PRO A 194 ? 0.45465 0.40776 0.42019 -0.09164 -0.02292 -0.01586 194 PRO A CB  
102  C  CG  . PRO A 194 ? 0.52014 0.46989 0.47362 -0.09969 -0.02571 -0.01927 194 PRO A CG  
103  C  CD  . PRO A 194 ? 0.44340 0.36680 0.37562 -0.09565 -0.02144 -0.02534 194 PRO A CD  
104  N  N   . ASN A 195 ? 0.31535 0.25167 0.28295 -0.06584 -0.01504 -0.01414 195 ASN A N   
105  C  CA  . ASN A 195 ? 0.28542 0.21033 0.25075 -0.06075 -0.01171 -0.01294 195 ASN A CA  
106  C  C   . ASN A 195 ? 0.31728 0.25780 0.29915 -0.05941 -0.01118 -0.00811 195 ASN A C   
107  O  O   . ASN A 195 ? 0.38229 0.31489 0.36272 -0.05540 -0.00851 -0.00667 195 ASN A O   
108  C  CB  . ASN A 195 ? 0.32858 0.24196 0.28594 -0.04909 -0.01055 -0.01438 195 ASN A CB  
109  C  CG  . ASN A 195 ? 0.32822 0.25872 0.29703 -0.04092 -0.01243 -0.01244 195 ASN A CG  
110  O  OD1 . ASN A 195 ? 0.29736 0.24711 0.27943 -0.04340 -0.01448 -0.00991 195 ASN A OD1 
111  N  ND2 . ASN A 195 ? 0.32892 0.25228 0.29294 -0.03101 -0.01161 -0.01324 195 ASN A ND2 
112  N  N   . CYS A 196 ? 0.31022 0.27165 0.30708 -0.06299 -0.01340 -0.00538 196 CYS A N   
113  C  CA  . CYS A 196 ? 0.23625 0.21303 0.24939 -0.05967 -0.01234 -0.00087 196 CYS A CA  
114  C  C   . CYS A 196 ? 0.31168 0.30542 0.33956 -0.06802 -0.01323 0.00225  196 CYS A C   
115  O  O   . CYS A 196 ? 0.37359 0.37419 0.40213 -0.07461 -0.01691 0.00174  196 CYS A O   
116  C  CB  . CYS A 196 ? 0.33830 0.32510 0.35661 -0.05088 -0.01427 0.00008  196 CYS A CB  
117  S  SG  . CYS A 196 ? 0.36373 0.36455 0.39774 -0.04502 -0.01218 0.00499  196 CYS A SG  
118  N  N   . THR A 197 ? 0.32797 0.32833 0.36760 -0.06799 -0.00968 0.00569  197 THR A N   
119  C  CA  . THR A 197 ? 0.28429 0.30122 0.34043 -0.07500 -0.00940 0.00933  197 THR A CA  
120  C  C   . THR A 197 ? 0.38355 0.41714 0.45689 -0.06885 -0.00820 0.01380  197 THR A C   
121  O  O   . THR A 197 ? 0.42792 0.45699 0.50257 -0.06397 -0.00341 0.01475  197 THR A O   
122  C  CB  . THR A 197 ? 0.32456 0.33257 0.37897 -0.08146 -0.00455 0.00909  197 THR A CB  
123  O  OG1 . THR A 197 ? 0.36426 0.35655 0.40207 -0.08807 -0.00589 0.00502  197 THR A OG1 
124  C  CG2 . THR A 197 ? 0.36505 0.39222 0.43961 -0.08765 -0.00331 0.01343  197 THR A CG2 
125  N  N   . ILE A 198 ? 0.29300 0.34464 0.37828 -0.06947 -0.01251 0.01664  198 ILE A N   
126  C  CA  . ILE A 198 ? 0.22229 0.28960 0.32397 -0.06375 -0.01151 0.02123  198 ILE A CA  
127  C  C   . ILE A 198 ? 0.31505 0.39803 0.43619 -0.06903 -0.00974 0.02604  198 ILE A C   
128  O  O   . ILE A 198 ? 0.40918 0.49513 0.54085 -0.06626 -0.00369 0.02865  198 ILE A O   
129  C  CB  . ILE A 198 ? 0.34956 0.42703 0.45264 -0.06024 -0.01733 0.02203  198 ILE A CB  
130  C  CG1 . ILE A 198 ? 0.33256 0.39573 0.41768 -0.05482 -0.01857 0.01721  198 ILE A CG1 
131  C  CG2 . ILE A 198 ? 0.31905 0.41212 0.43914 -0.05468 -0.01611 0.02722  198 ILE A CG2 
132  C  CD1 . ILE A 198 ? 0.36245 0.43413 0.44678 -0.05294 -0.02393 0.01715  198 ILE A CD1 
133  N  N   . ALA A 199 ? 0.30825 0.40139 0.43430 -0.07682 -0.01479 0.02739  199 ALA A N   
134  C  CA  . ALA A 199 ? 0.36466 0.47518 0.51113 -0.08222 -0.01397 0.03267  199 ALA A CA  
135  C  C   . ALA A 199 ? 0.52560 0.63240 0.66811 -0.09318 -0.01434 0.03109  199 ALA A C   
136  O  O   . ALA A 199 ? 0.51689 0.63179 0.67352 -0.09719 -0.01021 0.03409  199 ALA A O   
137  C  CB  . ALA A 199 ? 0.37092 0.50277 0.53198 -0.08247 -0.02069 0.03798  199 ALA A CB  
138  N  N   . GLN A 200 ? 0.34120 0.43530 0.46457 -0.09826 -0.01853 0.02632  200 GLN A N   
139  C  CA  . GLN A 200 ? 0.38592 0.47208 0.50081 -0.10914 -0.01859 0.02383  200 GLN A CA  
140  C  C   . GLN A 200 ? 0.46599 0.52569 0.55449 -0.10803 -0.01754 0.01686  200 GLN A C   
141  O  O   . GLN A 200 ? 0.35749 0.40921 0.43612 -0.10005 -0.01861 0.01446  200 GLN A O   
142  C  CB  . GLN A 200 ? 0.41156 0.51278 0.53202 -0.11948 -0.02619 0.02641  200 GLN A CB  
143  C  CG  . GLN A 200 ? 0.42269 0.51973 0.52872 -0.11968 -0.03295 0.02375  200 GLN A CG  
144  C  CD  . GLN A 200 ? 0.46118 0.57543 0.57410 -0.13029 -0.04105 0.02748  200 GLN A CD  
145  O  OE1 . GLN A 200 ? 0.41544 0.55281 0.55098 -0.13089 -0.04358 0.03451  200 GLN A OE1 
146  N  NE2 . GLN A 200 ? 0.42201 0.52469 0.51527 -0.13884 -0.04506 0.02308  200 GLN A NE2 
147  N  N   . ASP A 201 ? 0.34737 0.39360 0.42493 -0.11603 -0.01526 0.01387  201 ASP A N   
148  C  CA  . ASP A 201 ? 0.36136 0.38074 0.41446 -0.11466 -0.01330 0.00783  201 ASP A CA  
149  C  C   . ASP A 201 ? 0.43047 0.44187 0.46834 -0.11294 -0.01818 0.00422  201 ASP A C   
150  O  O   . ASP A 201 ? 0.40899 0.42716 0.44539 -0.12084 -0.02329 0.00414  201 ASP A O   
151  C  CB  . ASP A 201 ? 0.46359 0.47117 0.50727 -0.12586 -0.01106 0.00558  201 ASP A CB  
152  C  CG  . ASP A 201 ? 0.71360 0.69174 0.73261 -0.12382 -0.00811 0.00005  201 ASP A CG  
153  O  OD1 . ASP A 201 ? 0.83319 0.80138 0.84898 -0.11488 -0.00415 -0.00026 201 ASP A OD1 
154  O  OD2 . ASP A 201 ? 0.81588 0.78037 0.81835 -0.13140 -0.00978 -0.00369 201 ASP A OD2 
155  N  N   . LYS A 202 ? 0.44010 0.43697 0.46645 -0.10288 -0.01636 0.00132  202 LYS A N   
156  C  CA  . LYS A 202 ? 0.33850 0.32404 0.34879 -0.09989 -0.01904 -0.00288 202 LYS A CA  
157  C  C   . LYS A 202 ? 0.37101 0.37421 0.38886 -0.10130 -0.02475 -0.00115 202 LYS A C   
158  O  O   . LYS A 202 ? 0.40029 0.39792 0.40588 -0.10689 -0.02790 -0.00424 202 LYS A O   
159  C  CB  . LYS A 202 ? 0.38285 0.34703 0.37239 -0.10768 -0.01836 -0.00784 202 LYS A CB  
160  C  CG  . LYS A 202 ? 0.69053 0.63436 0.66950 -0.10658 -0.01315 -0.00968 202 LYS A CG  
161  C  CD  . LYS A 202 ? 0.71398 0.64648 0.68726 -0.09350 -0.01078 -0.01057 202 LYS A CD  
162  C  CE  . LYS A 202 ? 0.82833 0.74075 0.79103 -0.09316 -0.00624 -0.01149 202 LYS A CE  
163  N  NZ  . LYS A 202 ? 0.90244 0.81303 0.86837 -0.08207 -0.00426 -0.00947 202 LYS A NZ  
164  N  N   . ASP A 203 ? 0.31191 0.33509 0.34876 -0.09627 -0.02581 0.00378  203 ASP A N   
165  C  CA  . ASP A 203 ? 0.32855 0.36913 0.37340 -0.09728 -0.03153 0.00630  203 ASP A CA  
166  C  C   . ASP A 203 ? 0.28490 0.32238 0.32360 -0.08755 -0.03213 0.00429  203 ASP A C   
167  O  O   . ASP A 203 ? 0.28561 0.33622 0.32942 -0.08784 -0.03665 0.00620  203 ASP A O   
168  C  CB  . ASP A 203 ? 0.38522 0.44997 0.45466 -0.09763 -0.03274 0.01336  203 ASP A CB  
169  C  CG  . ASP A 203 ? 0.37033 0.43776 0.45042 -0.08700 -0.02768 0.01569  203 ASP A CG  
170  O  OD1 . ASP A 203 ? 0.37032 0.42263 0.43926 -0.07948 -0.02420 0.01229  203 ASP A OD1 
171  O  OD2 . ASP A 203 ? 0.40523 0.49010 0.50523 -0.08634 -0.02706 0.02127  203 ASP A OD2 
172  N  N   . SER A 204 ? 0.27506 0.29581 0.30276 -0.07939 -0.02800 0.00073  204 SER A N   
173  C  CA  . SER A 204 ? 0.25412 0.27367 0.27764 -0.07016 -0.02835 -0.00088 204 SER A CA  
174  C  C   . SER A 204 ? 0.32873 0.32604 0.33524 -0.06449 -0.02475 -0.00586 204 SER A C   
175  O  O   . SER A 204 ? 0.34366 0.32677 0.34335 -0.06576 -0.02161 -0.00715 204 SER A O   
176  C  CB  . SER A 204 ? 0.30522 0.33855 0.34426 -0.06201 -0.02741 0.00352  204 SER A CB  
177  O  OG  . SER A 204 ? 0.32948 0.35752 0.37226 -0.05997 -0.02292 0.00489  204 SER A OG  
178  N  N   . LYS A 205 ? 0.32856 0.32316 0.32856 -0.05824 -0.02518 -0.00839 205 LYS A N   
179  C  CA  . LYS A 205 ? 0.32450 0.30190 0.31257 -0.04989 -0.02180 -0.01192 205 LYS A CA  
180  C  C   . LYS A 205 ? 0.29641 0.28310 0.29347 -0.03940 -0.02139 -0.00952 205 LYS A C   
181  O  O   . LYS A 205 ? 0.26165 0.25945 0.26264 -0.03680 -0.02334 -0.00932 205 LYS A O   
182  C  CB  . LYS A 205 ? 0.36217 0.32736 0.33460 -0.05137 -0.02151 -0.01728 205 LYS A CB  
183  C  CG  . LYS A 205 ? 0.38196 0.33455 0.34622 -0.04058 -0.01815 -0.02017 205 LYS A CG  
184  C  CD  . LYS A 205 ? 0.35323 0.28598 0.30844 -0.03765 -0.01469 -0.02128 205 LYS A CD  
185  C  CE  . LYS A 205 ? 0.46401 0.38848 0.41581 -0.02521 -0.01206 -0.02227 205 LYS A CE  
186  N  NZ  . LYS A 205 ? 0.59392 0.49429 0.53139 -0.02353 -0.00862 -0.02490 205 LYS A NZ  
187  N  N   . LEU A 206 ? 0.28198 0.26340 0.28103 -0.03410 -0.01890 -0.00770 206 LEU A N   
188  C  CA  . LEU A 206 ? 0.27434 0.26061 0.27834 -0.02448 -0.01827 -0.00586 206 LEU A CA  
189  C  C   . LEU A 206 ? 0.28394 0.25519 0.27609 -0.01748 -0.01666 -0.00914 206 LEU A C   
190  O  O   . LEU A 206 ? 0.31765 0.27193 0.30023 -0.01740 -0.01471 -0.01049 206 LEU A O   
191  C  CB  . LEU A 206 ? 0.26796 0.25520 0.27865 -0.02326 -0.01642 -0.00205 206 LEU A CB  
192  C  CG  . LEU A 206 ? 0.28329 0.27472 0.29779 -0.01465 -0.01594 0.00021  206 LEU A CG  
193  C  CD1 . LEU A 206 ? 0.29232 0.30256 0.31837 -0.01358 -0.01760 0.00243  206 LEU A CD1 
194  C  CD2 . LEU A 206 ? 0.28473 0.26990 0.29967 -0.01442 -0.01345 0.00300  206 LEU A CD2 
195  N  N   . THR A 207 ? 0.28185 0.25891 0.27455 -0.01171 -0.01721 -0.01039 207 THR A N   
196  C  CA  . THR A 207 ? 0.27562 0.24097 0.26030 -0.00358 -0.01518 -0.01273 207 THR A CA  
197  C  C   . THR A 207 ? 0.33239 0.30506 0.32480 0.00443  -0.01553 -0.00899 207 THR A C   
198  O  O   . THR A 207 ? 0.28668 0.27481 0.28761 0.00645  -0.01689 -0.00741 207 THR A O   
199  C  CB  . THR A 207 ? 0.27965 0.24578 0.25946 -0.00238 -0.01460 -0.01680 207 THR A CB  
200  O  OG1 . THR A 207 ? 0.33126 0.29221 0.30347 -0.01192 -0.01495 -0.01987 207 THR A OG1 
201  C  CG2 . THR A 207 ? 0.35541 0.30762 0.32742 0.00643  -0.01134 -0.01926 207 THR A CG2 
202  N  N   . LEU A 208 ? 0.26616 0.22738 0.25476 0.00825  -0.01456 -0.00733 208 LEU A N   
203  C  CA  . LEU A 208 ? 0.24611 0.21312 0.24050 0.01428  -0.01541 -0.00328 208 LEU A CA  
204  C  C   . LEU A 208 ? 0.28459 0.23860 0.27235 0.02206  -0.01471 -0.00320 208 LEU A C   
205  O  O   . LEU A 208 ? 0.29900 0.23590 0.27760 0.02099  -0.01348 -0.00409 208 LEU A O   
206  C  CB  . LEU A 208 ? 0.24596 0.21355 0.24347 0.00945  -0.01544 0.00024  208 LEU A CB  
207  C  CG  . LEU A 208 ? 0.25989 0.23073 0.26047 0.01410  -0.01620 0.00442  208 LEU A CG  
208  C  CD1 . LEU A 208 ? 0.22917 0.21782 0.23878 0.01761  -0.01751 0.00562  208 LEU A CD1 
209  C  CD2 . LEU A 208 ? 0.27660 0.24437 0.27764 0.00827  -0.01492 0.00717  208 LEU A CD2 
210  N  N   . VAL A 209 ? 0.24987 0.21202 0.24248 0.02981  -0.01545 -0.00193 209 VAL A N   
211  C  CA  . VAL A 209 ? 0.27325 0.22614 0.26261 0.03841  -0.01522 -0.00066 209 VAL A CA  
212  C  C   . VAL A 209 ? 0.30437 0.26666 0.30021 0.04209  -0.01799 0.00472  209 VAL A C   
213  O  O   . VAL A 209 ? 0.27018 0.24907 0.27418 0.04281  -0.01908 0.00572  209 VAL A O   
214  C  CB  . VAL A 209 ? 0.27280 0.22656 0.26219 0.04468  -0.01303 -0.00417 209 VAL A CB  
215  C  CG1 . VAL A 209 ? 0.29451 0.23773 0.28174 0.05446  -0.01226 -0.00239 209 VAL A CG1 
216  C  CG2 . VAL A 209 ? 0.31072 0.25610 0.29225 0.03880  -0.01030 -0.00985 209 VAL A CG2 
217  N  N   . LEU A 210 ? 0.28926 0.24030 0.28032 0.04359  -0.01926 0.00831  210 LEU A N   
218  C  CA  . LEU A 210 ? 0.29932 0.25697 0.29416 0.04627  -0.02238 0.01383  210 LEU A CA  
219  C  C   . LEU A 210 ? 0.38108 0.33319 0.37541 0.05571  -0.02382 0.01647  210 LEU A C   
220  O  O   . LEU A 210 ? 0.37108 0.30590 0.35751 0.05752  -0.02343 0.01696  210 LEU A O   
221  C  CB  . LEU A 210 ? 0.28554 0.23502 0.27481 0.03951  -0.02306 0.01667  210 LEU A CB  
222  C  CG  . LEU A 210 ? 0.29248 0.24709 0.28373 0.03067  -0.02100 0.01474  210 LEU A CG  
223  C  CD1 . LEU A 210 ? 0.30415 0.24921 0.28948 0.02458  -0.02062 0.01759  210 LEU A CD1 
224  C  CD2 . LEU A 210 ? 0.31755 0.29173 0.31866 0.03029  -0.02140 0.01507  210 LEU A CD2 
225  N  N   . THR A 211 ? 0.28018 0.24685 0.28325 0.06179  -0.02534 0.01836  211 THR A N   
226  C  CA  . THR A 211 ? 0.25996 0.22432 0.26553 0.07158  -0.02671 0.02153  211 THR A CA  
227  C  C   . THR A 211 ? 0.32520 0.29870 0.33492 0.07277  -0.03181 0.02849  211 THR A C   
228  O  O   . THR A 211 ? 0.31522 0.30481 0.33081 0.06983  -0.03325 0.02957  211 THR A O   
229  C  CB  . THR A 211 ? 0.34860 0.32213 0.36146 0.07831  -0.02376 0.01807  211 THR A CB  
230  O  OG1 . THR A 211 ? 0.38367 0.34587 0.38981 0.07591  -0.01914 0.01167  211 THR A OG1 
231  C  CG2 . THR A 211 ? 0.41107 0.38270 0.42835 0.08908  -0.02458 0.02182  211 THR A CG2 
232  N  N   . LYS A 212 ? 0.31658 0.27887 0.32198 0.07613  -0.03476 0.03345  212 LYS A N   
233  C  CA  . LYS A 212 ? 0.31389 0.28338 0.32096 0.07532  -0.04031 0.04049  212 LYS A CA  
234  C  C   . LYS A 212 ? 0.37673 0.36189 0.39586 0.08430  -0.04270 0.04399  212 LYS A C   
235  O  O   . LYS A 212 ? 0.45398 0.43415 0.47638 0.09353  -0.04232 0.04530  212 LYS A O   
236  C  CB  . LYS A 212 ? 0.36243 0.31360 0.35901 0.07406  -0.04325 0.04509  212 LYS A CB  
237  C  CG  . LYS A 212 ? 0.44226 0.39884 0.43783 0.07142  -0.04945 0.05265  212 LYS A CG  
238  C  CD  . LYS A 212 ? 0.38802 0.32450 0.37009 0.06707  -0.05167 0.05622  212 LYS A CD  
239  C  CE  . LYS A 212 ? 0.39319 0.33401 0.37259 0.06390  -0.05840 0.06424  212 LYS A CE  
240  N  NZ  . LYS A 212 ? 0.42726 0.38074 0.40732 0.05549  -0.05797 0.06333  212 LYS A NZ  
241  N  N   . CYS A 213 ? 0.36798 0.37206 0.39409 0.08171  -0.04455 0.04532  213 CYS A N   
242  C  CA  . CYS A 213 ? 0.34364 0.36479 0.38144 0.08851  -0.04777 0.04986  213 CYS A CA  
243  C  C   . CYS A 213 ? 0.40073 0.42672 0.43613 0.08365  -0.05447 0.05738  213 CYS A C   
244  O  O   . CYS A 213 ? 0.61254 0.65313 0.65077 0.07852  -0.05609 0.05844  213 CYS A O   
245  C  CB  . CYS A 213 ? 0.43323 0.47257 0.47995 0.08847  -0.04470 0.04555  213 CYS A CB  
246  S  SG  . CYS A 213 ? 0.51930 0.55307 0.56481 0.08914  -0.03697 0.03592  213 CYS A SG  
247  N  N   . GLY A 214 ? 0.44462 0.45679 0.47305 0.08434  -0.05824 0.06250  214 GLY A N   
248  C  CA  . GLY A 214 ? 0.46385 0.47814 0.48749 0.07869  -0.06496 0.06994  214 GLY A CA  
249  C  C   . GLY A 214 ? 0.44995 0.46158 0.46345 0.06623  -0.06365 0.06772  214 GLY A C   
250  O  O   . GLY A 214 ? 0.42474 0.42079 0.42828 0.06089  -0.05996 0.06387  214 GLY A O   
251  N  N   . SER A 215 ? 0.36870 0.39586 0.38500 0.06133  -0.06611 0.07004  215 SER A N   
252  C  CA  . SER A 215 ? 0.37500 0.39922 0.38134 0.04967  -0.06466 0.06883  215 SER A CA  
253  C  C   . SER A 215 ? 0.37586 0.40126 0.38351 0.04672  -0.05747 0.06089  215 SER A C   
254  O  O   . SER A 215 ? 0.31097 0.33165 0.31097 0.03791  -0.05477 0.05927  215 SER A O   
255  C  CB  . SER A 215 ? 0.55752 0.59742 0.56570 0.04522  -0.06930 0.07379  215 SER A CB  
256  O  OG  . SER A 215 ? 0.47648 0.53598 0.49857 0.05077  -0.06833 0.07185  215 SER A OG  
257  N  N   . GLN A 216 ? 0.31486 0.34635 0.33189 0.05366  -0.05416 0.05616  216 GLN A N   
258  C  CA  . GLN A 216 ? 0.27019 0.30291 0.28839 0.05072  -0.04823 0.04930  216 GLN A CA  
259  C  C   . GLN A 216 ? 0.23768 0.25858 0.25524 0.05498  -0.04470 0.04466  216 GLN A C   
260  O  O   . GLN A 216 ? 0.30354 0.32134 0.32423 0.06300  -0.04572 0.04550  216 GLN A O   
261  C  CB  . GLN A 216 ? 0.30730 0.35932 0.33572 0.05284  -0.04715 0.04719  216 GLN A CB  
262  C  CG  . GLN A 216 ? 0.41438 0.47672 0.44158 0.04601  -0.04853 0.04960  216 GLN A CG  
263  C  CD  . GLN A 216 ? 0.24597 0.32640 0.28260 0.04799  -0.04714 0.04720  216 GLN A CD  
264  O  OE1 . GLN A 216 ? 0.29469 0.37691 0.33320 0.04696  -0.04279 0.04199  216 GLN A OE1 
265  N  NE2 . GLN A 216 ? 0.24526 0.33934 0.28780 0.05048  -0.05105 0.05129  216 GLN A NE2 
266  N  N   . ILE A 217 ? 0.23107 0.24535 0.24455 0.04931  -0.04042 0.04007  217 ILE A N   
267  C  CA  . ILE A 217 ? 0.22081 0.22598 0.23339 0.05104  -0.03664 0.03481  217 ILE A CA  
268  C  C   . ILE A 217 ? 0.24337 0.26179 0.26380 0.05212  -0.03386 0.03016  217 ILE A C   
269  O  O   . ILE A 217 ? 0.26037 0.28777 0.28291 0.04694  -0.03277 0.02937  217 ILE A O   
270  C  CB  . ILE A 217 ? 0.27411 0.26531 0.27824 0.04342  -0.03401 0.03309  217 ILE A CB  
271  C  CG1 . ILE A 217 ? 0.26835 0.24582 0.26292 0.04094  -0.03663 0.03784  217 ILE A CG1 
272  C  CG2 . ILE A 217 ? 0.28326 0.26572 0.28616 0.04445  -0.03059 0.02774  217 ILE A CG2 
273  C  CD1 . ILE A 217 ? 0.30184 0.27127 0.29476 0.04855  -0.03986 0.04080  217 ILE A CD1 
274  N  N   . LEU A 218 ? 0.21461 0.23321 0.23857 0.05873  -0.03243 0.02723  218 LEU A N   
275  C  CA  . LEU A 218 ? 0.25152 0.27961 0.28058 0.05915  -0.02942 0.02221  218 LEU A CA  
276  C  C   . LEU A 218 ? 0.23203 0.24907 0.25556 0.05456  -0.02629 0.01750  218 LEU A C   
277  O  O   . LEU A 218 ? 0.26873 0.27097 0.28640 0.05624  -0.02519 0.01617  218 LEU A O   
278  C  CB  . LEU A 218 ? 0.23799 0.27133 0.27292 0.06814  -0.02863 0.02122  218 LEU A CB  
279  C  CG  . LEU A 218 ? 0.26861 0.31116 0.30762 0.06876  -0.02517 0.01586  218 LEU A CG  
280  C  CD1 . LEU A 218 ? 0.26463 0.32465 0.30911 0.06500  -0.02628 0.01676  218 LEU A CD1 
281  C  CD2 . LEU A 218 ? 0.24295 0.28689 0.28674 0.07822  -0.02327 0.01503  218 LEU A CD2 
282  N  N   . ALA A 219 ? 0.21649 0.24063 0.24181 0.04851  -0.02501 0.01534  219 ALA A N   
283  C  CA  . ALA A 219 ? 0.25040 0.26632 0.27165 0.04276  -0.02289 0.01201  219 ALA A CA  
284  C  C   . ALA A 219 ? 0.28785 0.31145 0.31192 0.04178  -0.02129 0.00767  219 ALA A C   
285  O  O   . ALA A 219 ? 0.25074 0.28837 0.28053 0.04198  -0.02173 0.00789  219 ALA A O   
286  C  CB  . ALA A 219 ? 0.25506 0.27147 0.27617 0.03535  -0.02275 0.01409  219 ALA A CB  
287  N  N   . ASN A 220 ? 0.22921 0.24285 0.24804 0.03962  -0.01954 0.00385  220 ASN A N   
288  C  CA  . ASN A 220 ? 0.20544 0.22414 0.22453 0.03698  -0.01831 -0.00031 220 ASN A CA  
289  C  C   . ASN A 220 ? 0.24750 0.26034 0.26328 0.02876  -0.01812 -0.00163 220 ASN A C   
290  O  O   . ASN A 220 ? 0.24362 0.24209 0.25284 0.02725  -0.01729 -0.00230 220 ASN A O   
291  C  CB  . ASN A 220 ? 0.20126 0.21250 0.21581 0.04243  -0.01592 -0.00408 220 ASN A CB  
292  C  CG  . ASN A 220 ? 0.30529 0.32095 0.31822 0.03933  -0.01441 -0.00857 220 ASN A CG  
293  O  OD1 . ASN A 220 ? 0.34361 0.35000 0.34941 0.03416  -0.01331 -0.01192 220 ASN A OD1 
294  N  ND2 . ASN A 220 ? 0.38112 0.41072 0.39972 0.04176  -0.01445 -0.00864 220 ASN A ND2 
295  N  N   . VAL A 221 ? 0.21130 0.23521 0.23170 0.02329  -0.01901 -0.00174 221 VAL A N   
296  C  CA  . VAL A 221 ? 0.19604 0.21752 0.21611 0.01533  -0.01933 -0.00180 221 VAL A CA  
297  C  C   . VAL A 221 ? 0.22046 0.24975 0.24142 0.01036  -0.02041 -0.00401 221 VAL A C   
298  O  O   . VAL A 221 ? 0.23850 0.27896 0.26305 0.01203  -0.02119 -0.00407 221 VAL A O   
299  C  CB  . VAL A 221 ? 0.23708 0.26423 0.26405 0.01280  -0.01961 0.00265  221 VAL A CB  
300  C  CG1 . VAL A 221 ? 0.23482 0.27814 0.27015 0.01357  -0.02057 0.00494  221 VAL A CG1 
301  C  CG2 . VAL A 221 ? 0.24389 0.26750 0.27159 0.00535  -0.01919 0.00299  221 VAL A CG2 
302  N  N   . SER A 222 ? 0.21447 0.23748 0.23126 0.00353  -0.02068 -0.00571 222 SER A N   
303  C  CA  . SER A 222 ? 0.23934 0.27054 0.25757 -0.00339 -0.02283 -0.00642 222 SER A CA  
304  C  C   . SER A 222 ? 0.28937 0.31706 0.30807 -0.01141 -0.02363 -0.00541 222 SER A C   
305  O  O   . SER A 222 ? 0.25337 0.26962 0.26846 -0.01164 -0.02186 -0.00550 222 SER A O   
306  C  CB  . SER A 222 ? 0.34334 0.36942 0.35191 -0.00378 -0.02221 -0.01135 222 SER A CB  
307  O  OG  . SER A 222 ? 0.31144 0.32019 0.30894 -0.00579 -0.02017 -0.01488 222 SER A OG  
308  N  N   . LEU A 223 ? 0.23158 0.26955 0.25494 -0.01834 -0.02651 -0.00410 223 LEU A N   
309  C  CA  . LEU A 223 ? 0.24725 0.28505 0.27351 -0.02640 -0.02757 -0.00246 223 LEU A CA  
310  C  C   . LEU A 223 ? 0.26282 0.30369 0.28499 -0.03500 -0.03094 -0.00388 223 LEU A C   
311  O  O   . LEU A 223 ? 0.26934 0.32052 0.29355 -0.03567 -0.03360 -0.00327 223 LEU A O   
312  C  CB  . LEU A 223 ? 0.26041 0.31151 0.30188 -0.02680 -0.02793 0.00317  223 LEU A CB  
313  C  CG  . LEU A 223 ? 0.24892 0.30282 0.29702 -0.03452 -0.02840 0.00569  223 LEU A CG  
314  C  CD1 . LEU A 223 ? 0.26290 0.30054 0.30337 -0.03573 -0.02504 0.00362  223 LEU A CD1 
315  C  CD2 . LEU A 223 ? 0.27433 0.34278 0.33882 -0.03334 -0.02794 0.01134  223 LEU A CD2 
316  N  N   . ILE A 224 ? 0.26351 0.29504 0.27899 -0.04230 -0.03097 -0.00563 224 ILE A N   
317  C  CA  . ILE A 224 ? 0.26985 0.30465 0.28150 -0.05284 -0.03479 -0.00620 224 ILE A CA  
318  C  C   . ILE A 224 ? 0.30632 0.34693 0.32714 -0.06014 -0.03621 -0.00243 224 ILE A C   
319  O  O   . ILE A 224 ? 0.28299 0.31176 0.29949 -0.06139 -0.03325 -0.00380 224 ILE A O   
320  C  CB  . ILE A 224 ? 0.29595 0.31239 0.28830 -0.05652 -0.03316 -0.01255 224 ILE A CB  
321  C  CG1 . ILE A 224 ? 0.36225 0.37262 0.34625 -0.04869 -0.03057 -0.01655 224 ILE A CG1 
322  C  CG2 . ILE A 224 ? 0.28185 0.30158 0.26917 -0.06943 -0.03757 -0.01274 224 ILE A CG2 
323  C  CD1 . ILE A 224 ? 0.36922 0.35776 0.33478 -0.04936 -0.02659 -0.02291 224 ILE A CD1 
324  N  N   . VAL A 225 ? 0.23026 0.28917 0.26446 -0.06461 -0.04043 0.00269  225 VAL A N   
325  C  CA  . VAL A 225 ? 0.25078 0.31700 0.29525 -0.07200 -0.04170 0.00653  225 VAL A CA  
326  C  C   . VAL A 225 ? 0.32210 0.38675 0.35723 -0.08391 -0.04608 0.00493  225 VAL A C   
327  O  O   . VAL A 225 ? 0.32706 0.39993 0.36073 -0.08739 -0.05081 0.00578  225 VAL A O   
328  C  CB  . VAL A 225 ? 0.25668 0.34384 0.32250 -0.07008 -0.04351 0.01372  225 VAL A CB  
329  C  CG1 . VAL A 225 ? 0.23428 0.32927 0.31258 -0.07712 -0.04364 0.01777  225 VAL A CG1 
330  C  CG2 . VAL A 225 ? 0.28519 0.37217 0.35710 -0.05873 -0.03893 0.01472  225 VAL A CG2 
331  N  N   . VAL A 226 ? 0.29188 0.34555 0.31967 -0.09092 -0.04463 0.00270  226 VAL A N   
332  C  CA  . VAL A 226 ? 0.35069 0.39832 0.36497 -0.10304 -0.04803 -0.00002 226 VAL A CA  
333  C  C   . VAL A 226 ? 0.34017 0.40314 0.36635 -0.11437 -0.05279 0.00522  226 VAL A C   
334  O  O   . VAL A 226 ? 0.39101 0.45386 0.40816 -0.12599 -0.05739 0.00443  226 VAL A O   
335  C  CB  . VAL A 226 ? 0.33180 0.35365 0.32563 -0.10457 -0.04321 -0.00685 226 VAL A CB  
336  C  CG1 . VAL A 226 ? 0.44432 0.45177 0.42691 -0.09331 -0.03883 -0.01167 226 VAL A CG1 
337  C  CG2 . VAL A 226 ? 0.39311 0.40961 0.39173 -0.10493 -0.03946 -0.00585 226 VAL A CG2 
338  N  N   . ALA A 227 ? 0.29254 0.36842 0.33831 -0.11186 -0.05157 0.01054  227 ALA A N   
339  C  CA  . ALA A 227 ? 0.29541 0.38672 0.35475 -0.12209 -0.05529 0.01584  227 ALA A CA  
340  C  C   . ALA A 227 ? 0.28711 0.39639 0.37172 -0.11535 -0.05345 0.02257  227 ALA A C   
341  O  O   . ALA A 227 ? 0.27769 0.38366 0.36599 -0.10401 -0.04859 0.02219  227 ALA A O   
342  C  CB  . ALA A 227 ? 0.38400 0.46088 0.43246 -0.13071 -0.05255 0.01223  227 ALA A CB  
343  N  N   . GLY A 228 ? 0.33466 0.46301 0.43668 -0.12282 -0.05720 0.02892  228 GLY A N   
344  C  CA  . GLY A 228 ? 0.40357 0.54710 0.52968 -0.11728 -0.05387 0.03500  228 GLY A CA  
345  C  C   . GLY A 228 ? 0.33177 0.49186 0.47353 -0.10920 -0.05621 0.04075  228 GLY A C   
346  O  O   . GLY A 228 ? 0.27869 0.44249 0.41505 -0.10923 -0.06192 0.04124  228 GLY A O   
347  N  N   . LYS A 229 ? 0.27157 0.43975 0.43181 -0.10196 -0.05073 0.04482  229 LYS A N   
348  C  CA  . LYS A 229 ? 0.29921 0.48501 0.47868 -0.09497 -0.05200 0.05175  229 LYS A CA  
349  C  C   . LYS A 229 ? 0.36093 0.54066 0.52994 -0.08682 -0.05307 0.04948  229 LYS A C   
350  O  O   . LYS A 229 ? 0.30437 0.49480 0.48007 -0.08326 -0.05683 0.05373  229 LYS A O   
351  C  CB  . LYS A 229 ? 0.34796 0.53680 0.54420 -0.08835 -0.04324 0.05447  229 LYS A CB  
352  C  CG  . LYS A 229 ? 0.34502 0.53741 0.55037 -0.07612 -0.03922 0.05732  229 LYS A CG  
353  C  CD  . LYS A 229 ? 0.38402 0.57648 0.60307 -0.07124 -0.02938 0.05901  229 LYS A CD  
354  C  CE  . LYS A 229 ? 0.40948 0.60457 0.63621 -0.05984 -0.02533 0.06197  229 LYS A CE  
355  N  NZ  . LYS A 229 ? 0.52389 0.71843 0.76271 -0.05530 -0.01542 0.06355  229 LYS A NZ  
356  N  N   . TYR A 230 ? 0.23027 0.38999 0.37970 -0.08268 -0.04926 0.04205  230 TYR A N   
357  C  CA  . TYR A 230 ? 0.20590 0.36108 0.34693 -0.07484 -0.04962 0.04001  230 TYR A CA  
358  C  C   . TYR A 230 ? 0.26109 0.40776 0.38230 -0.07926 -0.05466 0.03506  230 TYR A C   
359  O  O   . TYR A 230 ? 0.27389 0.41519 0.38614 -0.07318 -0.05436 0.03236  230 TYR A O   
360  C  CB  . TYR A 230 ? 0.22180 0.36286 0.35710 -0.06554 -0.04170 0.03618  230 TYR A CB  
361  C  CG  . TYR A 230 ? 0.35051 0.49907 0.50393 -0.06055 -0.03594 0.04096  230 TYR A CG  
362  C  CD1 . TYR A 230 ? 0.36912 0.53151 0.53732 -0.05536 -0.03645 0.04673  230 TYR A CD1 
363  C  CD2 . TYR A 230 ? 0.25951 0.40016 0.41432 -0.06144 -0.02951 0.03962  230 TYR A CD2 
364  C  CE1 . TYR A 230 ? 0.27788 0.44574 0.46225 -0.05077 -0.03006 0.05095  230 TYR A CE1 
365  C  CE2 . TYR A 230 ? 0.28305 0.42932 0.45343 -0.05740 -0.02318 0.04358  230 TYR A CE2 
366  C  CZ  . TYR A 230 ? 0.27961 0.43936 0.46486 -0.05191 -0.02324 0.04916  230 TYR A CZ  
367  O  OH  . TYR A 230 ? 0.37414 0.53771 0.57400 -0.04767 -0.01583 0.05278  230 TYR A OH  
368  N  N   . HIS A 231 ? 0.29055 0.43587 0.40451 -0.09014 -0.05890 0.03381  231 HIS A N   
369  C  CA  . HIS A 231 ? 0.26806 0.40234 0.36093 -0.09492 -0.06231 0.02833  231 HIS A CA  
370  C  C   . HIS A 231 ? 0.33675 0.48265 0.43120 -0.09503 -0.06845 0.03154  231 HIS A C   
371  O  O   . HIS A 231 ? 0.32699 0.46372 0.40670 -0.09226 -0.06826 0.02694  231 HIS A O   
372  C  CB  . HIS A 231 ? 0.25778 0.38709 0.34162 -0.10783 -0.06512 0.02642  231 HIS A CB  
373  C  CG  . HIS A 231 ? 0.31161 0.42997 0.37362 -0.11481 -0.06865 0.02126  231 HIS A CG  
374  N  ND1 . HIS A 231 ? 0.28789 0.38761 0.33122 -0.10920 -0.06448 0.01396  231 HIS A ND1 
375  C  CD2 . HIS A 231 ? 0.36633 0.48970 0.42203 -0.12732 -0.07570 0.02249  231 HIS A CD2 
376  C  CE1 . HIS A 231 ? 0.37741 0.47009 0.40355 -0.11766 -0.06789 0.01045  231 HIS A CE1 
377  N  NE2 . HIS A 231 ? 0.35413 0.46032 0.38630 -0.12923 -0.07490 0.01540  231 HIS A NE2 
378  N  N   . ILE A 232 ? 0.30578 0.47179 0.41776 -0.09881 -0.07405 0.03960  232 ILE A N   
379  C  CA  . ILE A 232 ? 0.27526 0.45193 0.38926 -0.09850 -0.07988 0.04374  232 ILE A CA  
380  C  C   . ILE A 232 ? 0.42244 0.60866 0.55495 -0.08728 -0.07639 0.04970  232 ILE A C   
381  O  O   . ILE A 232 ? 0.42222 0.61517 0.56952 -0.08599 -0.07409 0.05388  232 ILE A O   
382  C  CB  . ILE A 232 ? 0.36016 0.53997 0.46879 -0.10791 -0.08574 0.04603  232 ILE A CB  
383  C  CG1 . ILE A 232 ? 0.39723 0.56426 0.48447 -0.11992 -0.08816 0.03930  232 ILE A CG1 
384  C  CG2 . ILE A 232 ? 0.28108 0.46665 0.38919 -0.10447 -0.08934 0.04996  232 ILE A CG2 
385  C  CD1 . ILE A 232 ? 0.42193 0.57756 0.48985 -0.11977 -0.08840 0.03296  232 ILE A CD1 
386  N  N   . ILE A 233 ? 0.32004 0.50570 0.45091 -0.07945 -0.07528 0.04962  233 ILE A N   
387  C  CA  . ILE A 233 ? 0.32362 0.51517 0.46869 -0.06936 -0.07146 0.05453  233 ILE A CA  
388  C  C   . ILE A 233 ? 0.41562 0.61396 0.56271 -0.07035 -0.07612 0.05969  233 ILE A C   
389  O  O   . ILE A 233 ? 0.42345 0.61972 0.55786 -0.07443 -0.08094 0.05845  233 ILE A O   
390  C  CB  . ILE A 233 ? 0.27813 0.46489 0.41980 -0.06081 -0.06760 0.05207  233 ILE A CB  
391  C  CG1 . ILE A 233 ? 0.31446 0.49367 0.45269 -0.06030 -0.06351 0.04719  233 ILE A CG1 
392  C  CG2 . ILE A 233 ? 0.37564 0.56616 0.52940 -0.05159 -0.06336 0.05679  233 ILE A CG2 
393  C  CD1 . ILE A 233 ? 0.31134 0.49125 0.46142 -0.06099 -0.05905 0.04883  233 ILE A CD1 
394  N  N   . ASN A 234 ? 0.37134 0.57757 0.53399 -0.06716 -0.07466 0.06560  234 ASN A N   
395  C  CA  . ASN A 234 ? 0.47798 0.69110 0.64442 -0.06675 -0.07886 0.07163  234 ASN A CA  
396  C  C   . ASN A 234 ? 0.48554 0.70288 0.66792 -0.05735 -0.07362 0.07646  234 ASN A C   
397  O  O   . ASN A 234 ? 0.54166 0.76534 0.73807 -0.05685 -0.07154 0.08010  234 ASN A O   
398  C  CB  . ASN A 234 ? 0.51560 0.73546 0.68313 -0.07610 -0.08499 0.07498  234 ASN A CB  
399  C  CG  . ASN A 234 ? 0.52899 0.75442 0.69540 -0.07775 -0.09102 0.08071  234 ASN A CG  
400  O  OD1 . ASN A 234 ? 0.48901 0.71674 0.66198 -0.07051 -0.08962 0.08463  234 ASN A OD1 
401  N  ND2 . ASN A 234 ? 0.67505 0.90152 0.83163 -0.08794 -0.09770 0.08114  234 ASN A ND2 
402  N  N   . ASN A 235 ? 0.31513 0.63101 0.54486 0.06033  -0.01868 0.13617  235 ASN A N   
403  C  CA  . ASN A 235 ? 0.42945 0.73947 0.66714 0.06631  -0.00983 0.14756  235 ASN A CA  
404  C  C   . ASN A 235 ? 0.37814 0.69963 0.62445 0.07163  -0.00782 0.15600  235 ASN A C   
405  O  O   . ASN A 235 ? 0.42941 0.74625 0.68362 0.07694  0.00037  0.16595  235 ASN A O   
406  C  CB  . ASN A 235 ? 0.42192 0.71695 0.64981 0.06688  -0.00736 0.15139  235 ASN A CB  
407  C  CG  . ASN A 235 ? 0.51131 0.79413 0.73300 0.06281  -0.00767 0.14541  235 ASN A CG  
408  O  OD1 . ASN A 235 ? 0.37767 0.65302 0.58671 0.05964  -0.01182 0.14149  235 ASN A OD1 
409  N  ND2 . ASN A 235 ? 0.41753 0.69833 0.64844 0.06280  -0.00311 0.14453  235 ASN A ND2 
410  N  N   . LYS A 236 ? 0.43298 0.76867 0.67815 0.07043  -0.01457 0.15256  236 LYS A N   
411  C  CA  . LYS A 236 ? 0.68830 1.03743 0.94379 0.07551  -0.01296 0.16036  236 LYS A CA  
412  C  C   . LYS A 236 ? 0.75442 1.11011 1.02562 0.07737  -0.00898 0.16106  236 LYS A C   
413  O  O   . LYS A 236 ? 0.94469 1.30311 1.22694 0.08304  -0.00264 0.17076  236 LYS A O   
414  C  CB  . LYS A 236 ? 0.58125 0.94423 0.83182 0.07354  -0.02122 0.15618  236 LYS A CB  
415  N  N   . THR A 237 ? 0.92751 1.28500 1.20038 0.07263  -0.01190 0.15084  237 THR A N   
416  C  CA  . THR A 237 ? 1.03899 1.40227 1.32721 0.07381  -0.00773 0.15017  237 THR A CA  
417  C  C   . THR A 237 ? 1.07378 1.42140 1.36709 0.07567  0.00201  0.15443  237 THR A C   
418  O  O   . THR A 237 ? 1.07932 1.42695 1.38563 0.08030  0.00967  0.16167  237 THR A O   
419  C  CB  . THR A 237 ? 0.98778 1.35912 1.27662 0.06777  -0.01379 0.13715  237 THR A CB  
420  N  N   . ASN A 238 ? 0.73424 1.06766 1.01766 0.07220  0.00234  0.15031  238 ASN A N   
421  C  CA  . ASN A 238 ? 0.58801 0.90536 0.87547 0.07334  0.01170  0.15342  238 ASN A CA  
422  C  C   . ASN A 238 ? 0.68610 0.98835 0.96231 0.07432  0.01374  0.15840  238 ASN A C   
423  O  O   . ASN A 238 ? 0.48435 0.77836 0.74981 0.07013  0.01048  0.15260  238 ASN A O   
424  C  CB  . ASN A 238 ? 0.55450 0.86944 0.84284 0.06805  0.01115  0.14327  238 ASN A CB  
425  N  N   . PRO A 239 ? 0.63416 0.93247 0.91297 0.07980  0.01945  0.16912  239 PRO A N   
426  C  CA  . PRO A 239 ? 0.66546 0.94990 0.93427 0.08079  0.02187  0.17361  239 PRO A CA  
427  C  C   . PRO A 239 ? 0.74784 1.01347 1.01679 0.08054  0.02989  0.17401  239 PRO A C   
428  O  O   . PRO A 239 ? 0.59525 0.84919 0.85538 0.08067  0.03121  0.17606  239 PRO A O   
429  C  CB  . PRO A 239 ? 0.73158 1.01755 1.00648 0.08706  0.02781  0.18526  239 PRO A CB  
430  C  CG  . PRO A 239 ? 0.73732 1.03091 1.02786 0.09000  0.03253  0.18826  239 PRO A CG  
431  C  CD  . PRO A 239 ? 0.65269 0.95949 0.94408 0.08530  0.02410  0.17760  239 PRO A CD  
432  N  N   . LYS A 240 ? 0.59871 0.86057 0.87765 0.08026  0.03593  0.17197  240 LYS A N   
433  C  CA  . LYS A 240 ? 0.74705 0.98988 1.02729 0.08024  0.04540  0.17221  240 LYS A CA  
434  C  C   . LYS A 240 ? 0.54793 0.78873 0.82071 0.07435  0.03988  0.16241  240 LYS A C   
435  O  O   . LYS A 240 ? 0.47177 0.69673 0.74400 0.07396  0.04718  0.16197  240 LYS A O   
436  C  CB  . LYS A 240 ? 0.71032 0.94698 1.00592 0.08332  0.05768  0.17580  240 LYS A CB  
437  C  CG  . LYS A 240 ? 0.85091 1.08079 1.15312 0.08945  0.06724  0.18689  240 LYS A CG  
438  C  CD  . LYS A 240 ? 0.86322 1.07106 1.16006 0.09105  0.07672  0.19065  240 LYS A CD  
439  C  CE  . LYS A 240 ? 0.94357 1.14850 1.24080 0.09594  0.08126  0.20068  240 LYS A CE  
440  N  NZ  . LYS A 240 ? 1.07418 1.29656 1.36329 0.09526  0.06839  0.20089  240 LYS A NZ  
441  N  N   . ILE A 241 ? 0.36595 0.62163 0.63370 0.06977  0.02843  0.15434  241 ILE A N   
442  C  CA  . ILE A 241 ? 0.35661 0.61119 0.61657 0.06380  0.02260  0.14502  241 ILE A CA  
443  C  C   . ILE A 241 ? 0.43332 0.68334 0.67735 0.06188  0.01524  0.14412  241 ILE A C   
444  O  O   . ILE A 241 ? 0.31753 0.57715 0.55264 0.05929  0.00556  0.13989  241 ILE A O   
445  C  CB  . ILE A 241 ? 0.62717 0.89802 0.88887 0.05947  0.01483  0.13594  241 ILE A CB  
446  C  CG1 . ILE A 241 ? 0.61926 0.89455 0.89736 0.06125  0.02233  0.13639  241 ILE A CG1 
447  C  CG2 . ILE A 241 ? 0.52745 0.79644 0.78017 0.05304  0.00902  0.12642  241 ILE A CG2 
448  C  CD1 . ILE A 241 ? 0.74578 1.03698 1.02709 0.05707  0.01567  0.12692  241 ILE A CD1 
449  N  N   . LYS A 242 ? 0.27805 0.51227 0.51854 0.06306  0.02050  0.14745  242 LYS A N   
450  C  CA  . LYS A 242 ? 0.22605 0.45394 0.45236 0.06200  0.01485  0.14766  242 LYS A CA  
451  C  C   . LYS A 242 ? 0.20728 0.42390 0.42614 0.05874  0.01349  0.14360  242 LYS A C   
452  O  O   . LYS A 242 ? 0.22404 0.42944 0.42852 0.05734  0.01009  0.14304  242 LYS A O   
453  C  CB  . LYS A 242 ? 0.40359 0.62225 0.63169 0.06784  0.02252  0.15736  242 LYS A CB  
454  C  CG  . LYS A 242 ? 0.42638 0.65536 0.66161 0.07159  0.02437  0.16304  242 LYS A CG  
455  C  CD  . LYS A 242 ? 0.65701 0.89955 0.88265 0.06855  0.01283  0.15860  242 LYS A CD  
456  C  CE  . LYS A 242 ? 0.55488 0.79380 0.77385 0.07098  0.01319  0.16407  242 LYS A CE  
457  N  NZ  . LYS A 242 ? 0.51752 0.77018 0.73107 0.06932  0.00490  0.16108  242 LYS A NZ  
458  N  N   . SER A 243 ? 0.25139 0.45695 0.46627 0.05369  0.01698  0.13570  243 SER A N   
459  C  CA  . SER A 243 ? 0.31756 0.49725 0.50977 0.04655  0.01644  0.12659  243 SER A CA  
460  C  C   . SER A 243 ? 0.20949 0.38428 0.40068 0.04159  0.01868  0.11834  243 SER A C   
461  O  O   . SER A 243 ? 0.22976 0.41410 0.43685 0.04364  0.02418  0.11961  243 SER A O   
462  C  CB  . SER A 243 ? 0.33094 0.48019 0.51002 0.04646  0.02633  0.12790  243 SER A CB  
463  O  OG  . SER A 243 ? 0.42846 0.56733 0.61561 0.04819  0.03895  0.12965  243 SER A OG  
464  N  N   . PHE A 244 ? 0.20695 0.36670 0.37949 0.03514  0.01456  0.10994  244 PHE A N   
465  C  CA  . PHE A 244 ? 0.21343 0.36208 0.38088 0.03014  0.01819  0.10189  244 PHE A CA  
466  C  C   . PHE A 244 ? 0.19256 0.31613 0.33526 0.02437  0.01628  0.09524  244 PHE A C   
467  O  O   . PHE A 244 ? 0.23085 0.35091 0.36245 0.02378  0.00995  0.09602  244 PHE A O   
468  C  CB  . PHE A 244 ? 0.22197 0.39633 0.40226 0.02853  0.01147  0.09794  244 PHE A CB  
469  C  CG  . PHE A 244 ? 0.22566 0.41612 0.40205 0.02637  -0.00155 0.09577  244 PHE A CG  
470  C  CD1 . PHE A 244 ? 0.21755 0.39664 0.37771 0.02036  -0.00629 0.08792  244 PHE A CD1 
471  C  CD2 . PHE A 244 ? 0.19370 0.41132 0.38324 0.03047  -0.00878 0.10183  244 PHE A CD2 
472  C  CE1 . PHE A 244 ? 0.23361 0.42705 0.39080 0.01817  -0.01770 0.08581  244 PHE A CE1 
473  C  CE2 . PHE A 244 ? 0.16040 0.39254 0.34632 0.02806  -0.02028 0.09945  244 PHE A CE2 
474  C  CZ  . PHE A 244 ? 0.21961 0.43942 0.38971 0.02179  -0.02453 0.09127  244 PHE A CZ  
475  N  N   . THR A 245 ? 0.19098 0.29717 0.32525 0.02023  0.02200  0.08882  245 THR A N   
476  C  CA  . THR A 245 ? 0.20169 0.28267 0.31189 0.01510  0.02119  0.08315  245 THR A CA  
477  C  C   . THR A 245 ? 0.25749 0.33828 0.36236 0.01028  0.01791  0.07532  245 THR A C   
478  O  O   . THR A 245 ? 0.29336 0.38174 0.41008 0.01011  0.02222  0.07305  245 THR A O   
479  C  CB  . THR A 245 ? 0.36820 0.42037 0.46787 0.01459  0.03352  0.08343  245 THR A CB  
480  O  OG1 . THR A 245 ? 0.38084 0.43262 0.48574 0.01893  0.03735  0.09061  245 THR A OG1 
481  C  CG2 . THR A 245 ? 0.36323 0.39013 0.43743 0.00934  0.03252  0.07789  245 THR A CG2 
482  N  N   . ILE A 246 ? 0.22864 0.30085 0.31637 0.00646  0.01070  0.07129  246 ILE A N   
483  C  CA  . ILE A 246 ? 0.25308 0.32002 0.33222 0.00177  0.00851  0.06409  246 ILE A CA  
484  C  C   . ILE A 246 ? 0.28276 0.31944 0.33779 -0.00151 0.01168  0.06117  246 ILE A C   
485  O  O   . ILE A 246 ? 0.29393 0.32250 0.33620 -0.00204 0.00694  0.06250  246 ILE A O   
486  C  CB  . ILE A 246 ? 0.20935 0.29597 0.29103 0.00019  -0.00365 0.06207  246 ILE A CB  
487  C  CG1 . ILE A 246 ? 0.25672 0.37443 0.36211 0.00274  -0.00647 0.06407  246 ILE A CG1 
488  C  CG2 . ILE A 246 ? 0.23318 0.30922 0.30181 -0.00479 -0.00573 0.05502  246 ILE A CG2 
489  C  CD1 . ILE A 246 ? 0.27714 0.41625 0.38634 0.00147  -0.01824 0.06298  246 ILE A CD1 
490  N  N   . LYS A 247 ? 0.26475 0.28509 0.31321 -0.00387 0.01955  0.05703  247 LYS A N   
491  C  CA  . LYS A 247 ? 0.27971 0.27087 0.30454 -0.00701 0.02338  0.05438  247 LYS A CA  
492  C  C   . LYS A 247 ? 0.31477 0.30019 0.32797 -0.01081 0.01944  0.04877  247 LYS A C   
493  O  O   . LYS A 247 ? 0.29385 0.28710 0.31634 -0.01154 0.02164  0.04556  247 LYS A O   
494  C  CB  . LYS A 247 ? 0.30386 0.27604 0.32689 -0.00678 0.03700  0.05446  247 LYS A CB  
495  C  CG  . LYS A 247 ? 0.30952 0.28502 0.34393 -0.00292 0.04247  0.06033  247 LYS A CG  
496  C  CD  . LYS A 247 ? 0.47403 0.42819 0.50510 -0.00314 0.05653  0.06030  247 LYS A CD  
497  C  CE  . LYS A 247 ? 0.57233 0.53021 0.61533 0.00095  0.06193  0.06673  247 LYS A CE  
498  N  NZ  . LYS A 247 ? 0.62758 0.56327 0.66698 0.00051  0.07632  0.06692  247 LYS A NZ  
499  N  N   . LEU A 248 ? 0.27350 0.24506 0.26675 -0.01318 0.01420  0.04763  248 LEU A N   
500  C  CA  . LEU A 248 ? 0.31519 0.27530 0.29357 -0.01651 0.01223  0.04315  248 LEU A CA  
501  C  C   . LEU A 248 ? 0.29574 0.22650 0.25254 -0.01846 0.01939  0.04218  248 LEU A C   
502  O  O   . LEU A 248 ? 0.33708 0.25759 0.28148 -0.01900 0.01741  0.04389  248 LEU A O   
503  C  CB  . LEU A 248 ? 0.30743 0.27575 0.27964 -0.01773 -0.00021 0.04276  248 LEU A CB  
504  C  CG  . LEU A 248 ? 0.32226 0.31712 0.31155 -0.01726 -0.00781 0.04205  248 LEU A CG  
505  C  CD1 . LEU A 248 ? 0.38537 0.40147 0.39453 -0.01404 -0.00878 0.04578  248 LEU A CD1 
506  C  CD2 . LEU A 248 ? 0.38132 0.37900 0.36115 -0.01899 -0.01894 0.04133  248 LEU A CD2 
507  N  N   . LEU A 249 ? 0.31287 0.23052 0.26502 -0.01978 0.02769  0.03917  249 LEU A N   
508  C  CA  . LEU A 249 ? 0.35205 0.24169 0.28412 -0.02177 0.03593  0.03802  249 LEU A CA  
509  C  C   . LEU A 249 ? 0.36042 0.23837 0.27539 -0.02428 0.03341  0.03484  249 LEU A C   
510  O  O   . LEU A 249 ? 0.34551 0.23275 0.26858 -0.02429 0.03247  0.03260  249 LEU A O   
511  C  CB  . LEU A 249 ? 0.34737 0.22889 0.28761 -0.02097 0.04954  0.03756  249 LEU A CB  
512  C  CG  . LEU A 249 ? 0.42708 0.32458 0.39007 -0.01762 0.05296  0.04108  249 LEU A CG  
513  C  CD1 . LEU A 249 ? 0.50508 0.39609 0.47801 -0.01689 0.06621  0.04012  249 LEU A CD1 
514  C  CD2 . LEU A 249 ? 0.47319 0.36535 0.43081 -0.01689 0.05233  0.04478  249 LEU A CD2 
515  N  N   . PHE A 250 ? 0.38723 0.24584 0.27900 -0.02641 0.03213  0.03471  250 PHE A N   
516  C  CA  . PHE A 250 ? 0.38438 0.23267 0.25913 -0.02827 0.02869  0.03274  250 PHE A CA  
517  C  C   . PHE A 250 ? 0.40907 0.22976 0.26224 -0.03031 0.03757  0.03156  250 PHE A C   
518  O  O   . PHE A 250 ? 0.42504 0.23330 0.26988 -0.03134 0.04224  0.03229  250 PHE A O   
519  C  CB  . PHE A 250 ? 0.36095 0.21461 0.22629 -0.02904 0.01574  0.03384  250 PHE A CB  
520  C  CG  . PHE A 250 ? 0.32953 0.20939 0.21423 -0.02734 0.00664  0.03503  250 PHE A CG  
521  C  CD1 . PHE A 250 ? 0.36405 0.25762 0.25780 -0.02711 0.00190  0.03362  250 PHE A CD1 
522  C  CD2 . PHE A 250 ? 0.32222 0.21203 0.21518 -0.02616 0.00338  0.03749  250 PHE A CD2 
523  C  CE1 . PHE A 250 ? 0.30320 0.22091 0.21423 -0.02600 -0.00619 0.03440  250 PHE A CE1 
524  C  CE2 . PHE A 250 ? 0.33180 0.24553 0.24151 -0.02459 -0.00506 0.03878  250 PHE A CE2 
525  C  CZ  . PHE A 250 ? 0.32945 0.25685 0.24759 -0.02472 -0.00991 0.03706  250 PHE A CZ  
526  N  N   . ASN A 251 ? 0.43401 0.24486 0.27738 -0.03106 0.03993  0.02975  251 ASN A N   
527  C  CA  . ASN A 251 ? 0.47516 0.25963 0.29625 -0.03302 0.04793  0.02881  251 ASN A CA  
528  C  C   . ASN A 251 ? 0.48793 0.26231 0.28512 -0.03493 0.03955  0.02970  251 ASN A C   
529  O  O   . ASN A 251 ? 0.48816 0.27525 0.28702 -0.03477 0.02826  0.03099  251 ASN A O   
530  C  CB  . ASN A 251 ? 0.51955 0.29652 0.34168 -0.03262 0.05656  0.02667  251 ASN A CB  
531  C  CG  . ASN A 251 ? 0.57380 0.35640 0.39293 -0.03213 0.04973  0.02640  251 ASN A CG  
532  O  OD1 . ASN A 251 ? 0.48436 0.27139 0.29497 -0.03242 0.03888  0.02796  251 ASN A OD1 
533  N  ND2 . ASN A 251 ? 0.55293 0.33501 0.37970 -0.03143 0.05684  0.02431  251 ASN A ND2 
534  N  N   . LYS A 252 ? 0.55910 0.31038 0.33327 -0.03684 0.04505  0.02897  252 LYS A N   
535  C  CA  . LYS A 252 ? 0.53616 0.27763 0.28665 -0.03895 0.03745  0.02976  252 LYS A CA  
536  C  C   . LYS A 252 ? 0.53912 0.29099 0.28746 -0.03779 0.02590  0.03109  252 LYS A C   
537  O  O   . LYS A 252 ? 0.65134 0.40228 0.38585 -0.03910 0.01668  0.03209  252 LYS A O   
538  C  CB  . LYS A 252 ? 0.57352 0.28855 0.29920 -0.04128 0.04599  0.02881  252 LYS A CB  
539  C  CG  . LYS A 252 ? 0.79621 0.49862 0.52396 -0.04249 0.05941  0.02724  252 LYS A CG  
540  N  N   . ASN A 253 ? 0.49824 0.26015 0.26033 -0.03559 0.02642  0.03092  253 ASN A N   
541  C  CA  . ASN A 253 ? 0.52854 0.30161 0.29160 -0.03444 0.01619  0.03222  253 ASN A CA  
542  C  C   . ASN A 253 ? 0.53727 0.33550 0.32187 -0.03340 0.00712  0.03252  253 ASN A C   
543  O  O   . ASN A 253 ? 0.53165 0.34088 0.32020 -0.03256 -0.00089 0.03332  253 ASN A O   
544  C  CB  . ASN A 253 ? 0.52537 0.29509 0.29097 -0.03295 0.02210  0.03166  253 ASN A CB  
545  C  CG  . ASN A 253 ? 0.71405 0.45911 0.45519 -0.03356 0.02885  0.03226  253 ASN A CG  
546  O  OD1 . ASN A 253 ? 0.70925 0.44333 0.42925 -0.03495 0.02436  0.03378  253 ASN A OD1 
547  N  ND2 . ASN A 253 ? 0.74257 0.47925 0.48641 -0.03263 0.03966  0.03096  253 ASN A ND2 
548  N  N   . GLY A 254 ? 0.46791 0.27506 0.26610 -0.03336 0.00848  0.03216  254 GLY A N   
549  C  CA  . GLY A 254 ? 0.43158 0.26278 0.25061 -0.03215 0.00083  0.03264  254 GLY A CA  
550  C  C   . GLY A 254 ? 0.39354 0.24035 0.23446 -0.03065 0.00382  0.03125  254 GLY A C   
551  O  O   . GLY A 254 ? 0.40803 0.27565 0.26487 -0.02991 -0.00353 0.03147  254 GLY A O   
552  N  N   . VAL A 255 ? 0.43900 0.27668 0.28141 -0.03046 0.01468  0.02949  255 VAL A N   
553  C  CA  . VAL A 255 ? 0.39124 0.24291 0.25428 -0.02958 0.01882  0.02728  255 VAL A CA  
554  C  C   . VAL A 255 ? 0.36754 0.23020 0.24939 -0.02870 0.02364  0.02697  255 VAL A C   
555  O  O   . VAL A 255 ? 0.39379 0.24404 0.27040 -0.02876 0.03054  0.02761  255 VAL A O   
556  C  CB  . VAL A 255 ? 0.45791 0.29349 0.31310 -0.02981 0.02875  0.02535  255 VAL A CB  
557  C  CG1 . VAL A 255 ? 0.44771 0.29637 0.32498 -0.02942 0.03530  0.02206  255 VAL A CG1 
558  C  CG2 . VAL A 255 ? 0.52001 0.34716 0.35828 -0.02999 0.02334  0.02660  255 VAL A CG2 
559  N  N   . LEU A 256 ? 0.38340 0.26980 0.28728 -0.02793 0.02002  0.02613  256 LEU A N   
560  C  CA  . LEU A 256 ? 0.38637 0.28693 0.30998 -0.02662 0.02328  0.02650  256 LEU A CA  
561  C  C   . LEU A 256 ? 0.40372 0.29523 0.33279 -0.02647 0.03654  0.02434  256 LEU A C   
562  O  O   . LEU A 256 ? 0.41402 0.30293 0.34518 -0.02725 0.04173  0.02116  256 LEU A O   
563  C  CB  . LEU A 256 ? 0.34712 0.27561 0.29182 -0.02621 0.01625  0.02565  256 LEU A CB  
564  C  CG  . LEU A 256 ? 0.32104 0.26873 0.28605 -0.02439 0.01609  0.02727  256 LEU A CG  
565  C  CD1 . LEU A 256 ? 0.32573 0.27294 0.28496 -0.02311 0.01013  0.03165  256 LEU A CD1 
566  C  CD2 . LEU A 256 ? 0.28376 0.25953 0.26989 -0.02461 0.01059  0.02536  256 LEU A CD2 
567  N  N   . LEU A 257 ? 0.37417 0.26116 0.30676 -0.02546 0.04262  0.02598  257 LEU A N   
568  C  CA  . LEU A 257 ? 0.39014 0.26833 0.32904 -0.02525 0.05572  0.02412  257 LEU A CA  
569  C  C   . LEU A 257 ? 0.39925 0.30179 0.36611 -0.02388 0.05730  0.02297  257 LEU A C   
570  O  O   . LEU A 257 ? 0.38969 0.31388 0.37082 -0.02243 0.04981  0.02518  257 LEU A O   
571  C  CB  . LEU A 257 ? 0.38860 0.24955 0.31842 -0.02498 0.06251  0.02641  257 LEU A CB  
572  C  CG  . LEU A 257 ? 0.48182 0.31688 0.38296 -0.02698 0.06292  0.02678  257 LEU A CG  
573  C  CD1 . LEU A 257 ? 0.49675 0.31946 0.39186 -0.02711 0.06823  0.02895  257 LEU A CD1 
574  C  CD2 . LEU A 257 ? 0.53806 0.35373 0.42742 -0.02833 0.07211  0.02375  257 LEU A CD2 
575  N  N   . ASP A 258 ? 0.39416 0.29291 0.36870 -0.02437 0.06751  0.01944  258 ASP A N   
576  C  CA  . ASP A 258 ? 0.37131 0.29381 0.37222 -0.02371 0.06913  0.01724  258 ASP A CA  
577  C  C   . ASP A 258 ? 0.50743 0.44233 0.52533 -0.02118 0.07103  0.02051  258 ASP A C   
578  O  O   . ASP A 258 ? 0.45784 0.41735 0.49841 -0.02028 0.06936  0.01974  258 ASP A O   
579  C  CB  . ASP A 258 ? 0.41532 0.32983 0.42039 -0.02509 0.08039  0.01216  258 ASP A CB  
580  C  CG  . ASP A 258 ? 0.34580 0.23306 0.33897 -0.02507 0.09303  0.01225  258 ASP A CG  
581  O  OD1 . ASP A 258 ? 0.47765 0.35379 0.46207 -0.02411 0.09406  0.01597  258 ASP A OD1 
582  O  OD2 . ASP A 258 ? 0.53425 0.41141 0.52746 -0.02625 0.10256  0.00819  258 ASP A OD2 
583  N  N   . ASN A 259 ? 0.36623 0.28536 0.37456 -0.02006 0.07500  0.02410  259 ASN A N   
584  C  CA  . ASN A 259 ? 0.42322 0.35544 0.44871 -0.01714 0.07640  0.02808  259 ASN A CA  
585  C  C   . ASN A 259 ? 0.37717 0.32506 0.40481 -0.01543 0.06466  0.03261  259 ASN A C   
586  O  O   . ASN A 259 ? 0.38172 0.33978 0.42213 -0.01252 0.06542  0.03693  259 ASN A O   
587  C  CB  . ASN A 259 ? 0.57090 0.48028 0.58912 -0.01663 0.08814  0.02981  259 ASN A CB  
588  C  CG  . ASN A 259 ? 0.62647 0.50965 0.61684 -0.01854 0.08803  0.03055  259 ASN A CG  
589  O  OD1 . ASN A 259 ? 0.63299 0.50894 0.60683 -0.02063 0.08224  0.02860  259 ASN A OD1 
590  N  ND2 . ASN A 259 ? 0.61004 0.47870 0.59522 -0.01798 0.09495  0.03332  259 ASN A ND2 
591  N  N   . SER A 260 ? 0.29680 0.24736 0.31337 -0.01694 0.05427  0.03190  260 SER A N   
592  C  CA  . SER A 260 ? 0.24787 0.21719 0.26976 -0.01545 0.04269  0.03546  260 SER A CA  
593  C  C   . SER A 260 ? 0.40010 0.40033 0.44767 -0.01383 0.03905  0.03557  260 SER A C   
594  O  O   . SER A 260 ? 0.31757 0.32602 0.37646 -0.01495 0.04283  0.03149  260 SER A O   
595  C  CB  . SER A 260 ? 0.32429 0.29096 0.33065 -0.01766 0.03267  0.03407  260 SER A CB  
596  O  OG  . SER A 260 ? 0.33430 0.27415 0.31652 -0.01943 0.03513  0.03360  260 SER A OG  
597  N  N   . ASN A 261 ? 0.27230 0.29014 0.32900 -0.01128 0.03176  0.04019  261 ASN A N   
598  C  CA  . ASN A 261 ? 0.24519 0.29406 0.32491 -0.00988 0.02692  0.04056  261 ASN A CA  
599  C  C   . ASN A 261 ? 0.29103 0.35226 0.37055 -0.01297 0.01866  0.03605  261 ASN A C   
600  O  O   . ASN A 261 ? 0.24578 0.32741 0.34200 -0.01385 0.01809  0.03294  261 ASN A O   
601  C  CB  . ASN A 261 ? 0.21618 0.28003 0.30476 -0.00599 0.02157  0.04732  261 ASN A CB  
602  C  CG  . ASN A 261 ? 0.29480 0.35003 0.38826 -0.00261 0.03082  0.05198  261 ASN A CG  
603  O  OD1 . ASN A 261 ? 0.29433 0.32768 0.37267 -0.00248 0.03448  0.05403  261 ASN A OD1 
604  N  ND2 . ASN A 261 ? 0.32017 0.39233 0.43516 -0.00007 0.03529  0.05349  261 ASN A ND2 
605  N  N   . LEU A 262 ? 0.27257 0.32125 0.33357 -0.01491 0.01292  0.03532  262 LEU A N   
606  C  CA  . LEU A 262 ? 0.21903 0.27551 0.27775 -0.01797 0.00600  0.03119  262 LEU A CA  
607  C  C   . LEU A 262 ? 0.28664 0.33129 0.34157 -0.02076 0.01351  0.02546  262 LEU A C   
608  O  O   . LEU A 262 ? 0.26793 0.28794 0.30877 -0.02103 0.02107  0.02504  262 LEU A O   
609  C  CB  . LEU A 262 ? 0.22268 0.26846 0.26292 -0.01876 -0.00213 0.03282  262 LEU A CB  
610  C  CG  . LEU A 262 ? 0.24083 0.29105 0.27646 -0.02185 -0.00894 0.02907  262 LEU A CG  
611  C  CD1 . LEU A 262 ? 0.26285 0.34311 0.31697 -0.02225 -0.01615 0.02828  262 LEU A CD1 
612  C  CD2 . LEU A 262 ? 0.26262 0.29860 0.27857 -0.02239 -0.01576 0.03096  262 LEU A CD2 
613  N  N   . GLY A 263 ? 0.27026 0.33223 0.33747 -0.02302 0.01183  0.02088  263 GLY A N   
614  C  CA  . GLY A 263 ? 0.29739 0.34932 0.36237 -0.02574 0.01939  0.01515  263 GLY A CA  
615  C  C   . GLY A 263 ? 0.28259 0.31588 0.32717 -0.02761 0.01704  0.01401  263 GLY A C   
616  O  O   . GLY A 263 ? 0.29409 0.33120 0.33184 -0.02804 0.00748  0.01564  263 GLY A O   
617  N  N   . LYS A 264 ? 0.42257 0.24448 0.34258 -0.00833 0.01331  0.02472  264 LYS A N   
618  C  CA  . LYS A 264 ? 0.44113 0.26456 0.36736 -0.00346 0.01619  0.02900  264 LYS A CA  
619  C  C   . LYS A 264 ? 0.48021 0.29763 0.41381 -0.00425 0.02232  0.02740  264 LYS A C   
620  O  O   . LYS A 264 ? 0.50451 0.32303 0.44310 -0.00087 0.02475  0.02990  264 LYS A O   
621  C  CB  . LYS A 264 ? 0.44116 0.26794 0.37043 0.00088  0.01615  0.03554  264 LYS A CB  
622  C  CG  . LYS A 264 ? 0.51970 0.35381 0.44278 0.00256  0.01078  0.03754  264 LYS A CG  
623  C  CD  . LYS A 264 ? 0.58764 0.42536 0.51254 0.00606  0.01049  0.04342  264 LYS A CD  
624  C  CE  . LYS A 264 ? 0.50522 0.34449 0.43796 0.01093  0.01439  0.04938  264 LYS A CE  
625  N  NZ  . LYS A 264 ? 0.50193 0.34742 0.43532 0.01405  0.01364  0.05133  264 LYS A NZ  
626  N  N   . ALA A 265 ? 0.43682 0.24830 0.37165 -0.00875 0.02511  0.02319  265 ALA A N   
627  C  CA  . ALA A 265 ? 0.46269 0.26820 0.40580 -0.00959 0.03196  0.02156  265 ALA A CA  
628  C  C   . ALA A 265 ? 0.53097 0.33528 0.47426 -0.01070 0.03349  0.01801  265 ALA A C   
629  O  O   . ALA A 265 ? 0.56448 0.36530 0.51609 -0.00934 0.03927  0.01862  265 ALA A O   
630  C  CB  . ALA A 265 ? 0.60761 0.40771 0.55134 -0.01525 0.03462  0.01640  265 ALA A CB  
631  N  N   . TYR A 266 ? 0.57044 0.37766 0.50532 -0.01284 0.02869  0.01476  266 TYR A N   
632  C  CA  . TYR A 266 ? 0.68801 0.49360 0.62095 -0.01556 0.02955  0.00975  266 TYR A CA  
633  C  C   . TYR A 266 ? 0.55033 0.36052 0.48278 -0.01142 0.02751  0.01240  266 TYR A C   
634  O  O   . TYR A 266 ? 0.66911 0.47806 0.60046 -0.01313 0.02837  0.00865  266 TYR A O   
635  C  CB  . TYR A 266 ? 0.87148 0.67746 0.79519 -0.02124 0.02564  0.00427  266 TYR A CB  
636  C  CG  . TYR A 266 ? 0.76986 0.57339 0.69316 -0.02529 0.02638  0.00215  266 TYR A CG  
637  C  CD1 . TYR A 266 ? 0.72246 0.52079 0.64909 -0.03008 0.03146  -0.00308 266 TYR A CD1 
638  C  CD2 . TYR A 266 ? 0.78447 0.59120 0.70428 -0.02459 0.02220  0.00505  266 TYR A CD2 
639  C  CE1 . TYR A 266 ? 0.83109 0.62796 0.75757 -0.03410 0.03220  -0.00541 266 TYR A CE1 
640  C  CE2 . TYR A 266 ? 0.64163 0.44656 0.56143 -0.02829 0.02281  0.00317  266 TYR A CE2 
641  C  CZ  . TYR A 266 ? 0.95611 0.75635 0.87922 -0.03310 0.02773  -0.00212 266 TYR A CZ  
642  O  OH  . TYR A 266 ? 0.88962 0.68873 0.81301 -0.03719 0.02850  -0.00450 266 TYR A OH  
643  N  N   . TRP A 267 ? 0.40049 0.21634 0.33382 -0.00625 0.02501  0.01856  267 TRP A N   
644  C  CA  . TRP A 267 ? 0.38442 0.20672 0.31550 -0.00286 0.02169  0.02076  267 TRP A CA  
645  C  C   . TRP A 267 ? 0.41776 0.24288 0.35746 0.00281  0.02470  0.02695  267 TRP A C   
646  O  O   . TRP A 267 ? 0.40006 0.22794 0.34308 0.00627  0.02492  0.03266  267 TRP A O   
647  C  CB  . TRP A 267 ? 0.40308 0.23122 0.32710 -0.00223 0.01584  0.02232  267 TRP A CB  
648  C  CG  . TRP A 267 ? 0.37863 0.21427 0.30056 0.00101  0.01258  0.02439  267 TRP A CG  
649  C  CD1 . TRP A 267 ? 0.41186 0.25471 0.33543 0.00560  0.01100  0.03004  267 TRP A CD1 
650  C  CD2 . TRP A 267 ? 0.39140 0.22875 0.30909 -0.00038 0.01057  0.02055  267 TRP A CD2 
651  N  NE1 . TRP A 267 ? 0.39954 0.24887 0.32017 0.00687  0.00810  0.02951  267 TRP A NE1 
652  C  CE2 . TRP A 267 ? 0.37464 0.22031 0.29189 0.00335  0.00791  0.02372  267 TRP A CE2 
653  C  CE3 . TRP A 267 ? 0.35867 0.19166 0.27298 -0.00456 0.01098  0.01470  267 TRP A CE3 
654  C  CZ2 . TRP A 267 ? 0.39073 0.24003 0.30470 0.00302  0.00580  0.02093  267 TRP A CZ2 
655  C  CZ3 . TRP A 267 ? 0.38128 0.21756 0.29224 -0.00458 0.00889  0.01239  267 TRP A CZ3 
656  C  CH2 . TRP A 267 ? 0.39619 0.24032 0.30716 -0.00084 0.00638  0.01536  267 TRP A CH2 
657  N  N   . ASN A 268 ? 0.39291 0.21756 0.33663 0.00381  0.02724  0.02619  268 ASN A N   
658  C  CA  . ASN A 268 ? 0.38612 0.21324 0.33951 0.00910  0.03087  0.03240  268 ASN A CA  
659  C  C   . ASN A 268 ? 0.38622 0.21438 0.34207 0.00991  0.03208  0.03094  268 ASN A C   
660  O  O   . ASN A 268 ? 0.38116 0.20685 0.33162 0.00608  0.03085  0.02469  268 ASN A O   
661  C  CB  . ASN A 268 ? 0.44741 0.26762 0.41003 0.00917  0.03758  0.03399  268 ASN A CB  
662  C  CG  . ASN A 268 ? 0.42593 0.25044 0.39803 0.01559  0.04033  0.04302  268 ASN A CG  
663  O  OD1 . ASN A 268 ? 0.43137 0.26442 0.40395 0.01998  0.03767  0.04801  268 ASN A OD1 
664  N  ND2 . ASN A 268 ? 0.42612 0.24518 0.40618 0.01606  0.04592  0.04525  268 ASN A ND2 
665  N  N   . PHE A 269 ? 0.39887 0.23082 0.36354 0.01502  0.03482  0.03714  269 PHE A N   
666  C  CA  . PHE A 269 ? 0.41000 0.24217 0.37911 0.01596  0.03707  0.03614  269 PHE A CA  
667  C  C   . PHE A 269 ? 0.41016 0.23179 0.38369 0.01197  0.04325  0.03061  269 PHE A C   
668  O  O   . PHE A 269 ? 0.42013 0.23522 0.39765 0.01022  0.04755  0.02994  269 PHE A O   
669  C  CB  . PHE A 269 ? 0.38153 0.22079 0.36034 0.02254  0.03899  0.04487  269 PHE A CB  
670  C  CG  . PHE A 269 ? 0.50542 0.35679 0.47938 0.02592  0.03278  0.04924  269 PHE A CG  
671  C  CD1 . PHE A 269 ? 0.57883 0.43612 0.54788 0.02563  0.02880  0.04655  269 PHE A CD1 
672  C  CD2 . PHE A 269 ? 0.54157 0.39848 0.51577 0.02898  0.03116  0.05548  269 PHE A CD2 
673  C  CE1 . PHE A 269 ? 0.57816 0.44696 0.54256 0.02800  0.02336  0.04954  269 PHE A CE1 
674  C  CE2 . PHE A 269 ? 0.62382 0.49238 0.59307 0.03142  0.02562  0.05873  269 PHE A CE2 
675  C  CZ  . PHE A 269 ? 0.51140 0.38604 0.47588 0.03080  0.02182  0.05556  269 PHE A CZ  
676  N  N   . ARG A 270 ? 0.42402 0.24427 0.39711 0.01038  0.04400  0.02637  270 ARG A N   
677  C  CA  . ARG A 270 ? 0.39202 0.20278 0.36727 0.00555  0.04932  0.01963  270 ARG A CA  
678  C  C   . ARG A 270 ? 0.61054 0.41721 0.59987 0.00819  0.05740  0.02311  270 ARG A C   
679  O  O   . ARG A 270 ? 0.46284 0.27501 0.45977 0.01385  0.05829  0.02996  270 ARG A O   
680  C  CB  . ARG A 270 ? 0.40379 0.21506 0.37309 0.00306  0.04701  0.01409  270 ARG A CB  
681  C  CG  . ARG A 270 ? 0.44068 0.24394 0.41443 -0.00054 0.05320  0.00847  270 ARG A CG  
682  C  CD  . ARG A 270 ? 0.52502 0.32874 0.49139 -0.00343 0.05043  0.00274  270 ARG A CD  
683  N  NE  . ARG A 270 ? 0.56883 0.36460 0.53903 -0.00746 0.05669  -0.00314 270 ARG A NE  
684  C  CZ  . ARG A 270 ? 0.99369 0.78865 0.97082 -0.00573 0.06034  -0.00302 270 ARG A CZ  
685  N  NH1 . ARG A 270 ? 0.89289 0.69521 0.87368 -0.00000 0.05794  0.00284  270 ARG A NH1 
686  N  NH2 . ARG A 270 ? 1.02516 0.81244 1.00557 -0.00995 0.06644  -0.00894 270 ARG A NH2 
687  N  N   . SER A 271 ? 0.46864 0.26615 0.46189 0.00400  0.06351  0.01851  271 SER A N   
688  C  CA  . SER A 271 ? 0.50029 0.29196 0.50703 0.00497  0.07242  0.01940  271 SER A CA  
689  C  C   . SER A 271 ? 0.52301 0.30580 0.52757 -0.00245 0.07663  0.00931  271 SER A C   
690  O  O   . SER A 271 ? 0.52481 0.30283 0.52628 -0.00730 0.07799  0.00461  271 SER A O   
691  C  CB  . SER A 271 ? 0.63429 0.42423 0.65130 0.00817  0.07738  0.02559  271 SER A CB  
692  O  OG  . SER A 271 ? 0.57028 0.35389 0.60118 0.00877  0.08681  0.02602  271 SER A OG  
693  N  N   . GLY A 272 ? 0.59812 0.37933 0.60392 -0.00358 0.07853  0.00581  272 GLY A N   
694  C  CA  . GLY A 272 ? 0.52879 0.30249 0.53143 -0.01097 0.08223  -0.00409 272 GLY A CA  
695  C  C   . GLY A 272 ? 0.56710 0.34257 0.55435 -0.01607 0.07523  -0.00974 272 GLY A C   
696  O  O   . GLY A 272 ? 0.56356 0.34551 0.54229 -0.01421 0.06780  -0.00799 272 GLY A O   
697  N  N   . ASN A 273 ? 0.54671 0.31692 0.53068 -0.02265 0.07771  -0.01650 273 ASN A N   
698  C  CA  . ASN A 273 ? 0.52783 0.30038 0.49813 -0.02737 0.07127  -0.02088 273 ASN A CA  
699  C  C   . ASN A 273 ? 0.70478 0.47965 0.67304 -0.02634 0.06814  -0.01728 273 ASN A C   
700  O  O   . ASN A 273 ? 0.61909 0.39541 0.57764 -0.03058 0.06376  -0.02074 273 ASN A O   
701  C  CB  . ASN A 273 ? 0.64210 0.40938 0.60846 -0.03574 0.07488  -0.03062 273 ASN A CB  
702  C  CG  . ASN A 273 ? 0.61886 0.38592 0.58105 -0.03774 0.07451  -0.03494 273 ASN A CG  
703  O  OD1 . ASN A 273 ? 0.60604 0.37773 0.56511 -0.03364 0.06966  -0.03138 273 ASN A OD1 
704  N  ND2 . ASN A 273 ? 0.88219 0.64414 0.84415 -0.04436 0.07976  -0.04297 273 ASN A ND2 
705  N  N   . SER A 274 ? 0.56712 0.34287 0.54451 -0.02060 0.07022  -0.00996 274 SER A N   
706  C  CA  . SER A 274 ? 0.50759 0.28550 0.48417 -0.01892 0.06774  -0.00576 274 SER A CA  
707  C  C   . SER A 274 ? 0.51161 0.29690 0.48906 -0.01136 0.06303  0.00329  274 SER A C   
708  O  O   . SER A 274 ? 0.49013 0.28003 0.46496 -0.00874 0.05958  0.00486  274 SER A O   
709  C  CB  . SER A 274 ? 0.59112 0.36280 0.57880 -0.01971 0.07590  -0.00568 274 SER A CB  
710  O  OG  . SER A 274 ? 0.74400 0.51733 0.72979 -0.01906 0.07340  -0.00276 274 SER A OG  
711  N  N   . ASN A 275 ? 0.49116 0.27790 0.47255 -0.00806 0.06319  0.00906  275 ASN A N   
712  C  CA  . ASN A 275 ? 0.55188 0.34627 0.53424 -0.00123 0.05913  0.01786  275 ASN A CA  
713  C  C   . ASN A 275 ? 0.46251 0.25610 0.45881 0.00411  0.06551  0.02506  275 ASN A C   
714  O  O   . ASN A 275 ? 0.52063 0.30704 0.52561 0.00239  0.07293  0.02354  275 ASN A O   
715  C  CB  . ASN A 275 ? 0.51622 0.31399 0.49117 -0.00144 0.05364  0.01957  275 ASN A CB  
716  C  CG  . ASN A 275 ? 0.55327 0.35386 0.51515 -0.00515 0.04660  0.01477  275 ASN A CG  
717  O  OD1 . ASN A 275 ? 0.57789 0.38029 0.53562 -0.00587 0.04440  0.01209  275 ASN A OD1 
718  N  ND2 . ASN A 275 ? 0.53321 0.33424 0.48902 -0.00745 0.04324  0.01387  275 ASN A ND2 
719  N  N   . VAL A 276 ? 0.47267 0.27434 0.47130 0.01060  0.06265  0.03322  276 VAL A N   
720  C  CA  . VAL A 276 ? 0.46077 0.26344 0.47209 0.01632  0.06784  0.04179  276 VAL A CA  
721  C  C   . VAL A 276 ? 0.44600 0.24558 0.45859 0.01568  0.06947  0.04330  276 VAL A C   
722  O  O   . VAL A 276 ? 0.54883 0.34857 0.55146 0.01227  0.06463  0.03968  276 VAL A O   
723  C  CB  . VAL A 276 ? 0.49394 0.30787 0.50613 0.02310  0.06354  0.05053  276 VAL A CB  
724  C  CG1 . VAL A 276 ? 0.49840 0.31531 0.51000 0.02349  0.06226  0.04857  276 VAL A CG1 
725  C  CG2 . VAL A 276 ? 0.52352 0.34469 0.52453 0.02353  0.05542  0.05190  276 VAL A CG2 
726  N  N   . SER A 277 ? 0.49169 0.28841 0.51743 0.01912  0.07672  0.04895  277 SER A N   
727  C  CA  . SER A 277 ? 0.66895 0.46023 0.69814 0.01754  0.08052  0.04880  277 SER A CA  
728  C  C   . SER A 277 ? 0.65451 0.45239 0.67802 0.02057  0.07474  0.05458  277 SER A C   
729  O  O   . SER A 277 ? 0.84295 0.63730 0.86280 0.01728  0.07429  0.05153  277 SER A O   
730  C  CB  . SER A 277 ? 0.73143 0.51729 0.77762 0.02043  0.09089  0.05325  277 SER A CB  
731  O  OG  . SER A 277 ? 0.97341 0.76645 1.02767 0.02814  0.09152  0.06382  277 SER A OG  
732  N  N   . THR A 278 ? 0.51250 0.32029 0.53505 0.02645  0.07033  0.06254  278 THR A N   
733  C  CA  . THR A 278 ? 0.50451 0.31916 0.52228 0.02948  0.06541  0.06836  278 THR A CA  
734  C  C   . THR A 278 ? 0.51179 0.33413 0.51564 0.02836  0.05597  0.06596  278 THR A C   
735  O  O   . THR A 278 ? 0.42806 0.25411 0.42878 0.02836  0.05326  0.06408  278 THR A O   
736  C  CB  . THR A 278 ? 0.55083 0.37208 0.57885 0.03710  0.06817  0.08006  278 THR A CB  
737  O  OG1 . THR A 278 ? 0.71283 0.54152 0.74228 0.04046  0.06634  0.08332  278 THR A OG1 
738  C  CG2 . THR A 278 ? 0.57633 0.38925 0.61926 0.03824  0.07833  0.08260  278 THR A CG2 
739  N  N   . ALA A 279 ? 0.45046 0.27493 0.44654 0.02729  0.05141  0.06585  279 ALA A N   
740  C  CA  . ALA A 279 ? 0.45246 0.28356 0.43604 0.02589  0.04317  0.06328  279 ALA A CA  
741  C  C   . ALA A 279 ? 0.48279 0.32553 0.46640 0.03124  0.03981  0.06998  279 ALA A C   
742  O  O   . ALA A 279 ? 0.52501 0.37299 0.51537 0.03646  0.04174  0.07851  279 ALA A O   
743  C  CB  . ALA A 279 ? 0.58702 0.41792 0.56402 0.02405  0.03988  0.06261  279 ALA A CB  
744  N  N   . TYR A 280 ? 0.43927 0.28669 0.41558 0.02989  0.03492  0.06621  280 TYR A N   
745  C  CA  . TYR A 280 ? 0.41546 0.27458 0.39215 0.03442  0.03197  0.07171  280 TYR A CA  
746  C  C   . TYR A 280 ? 0.42452 0.29300 0.39647 0.03688  0.02758  0.07675  280 TYR A C   
747  O  O   . TYR A 280 ? 0.47995 0.34620 0.44518 0.03414  0.02502  0.07395  280 TYR A O   
748  C  CB  . TYR A 280 ? 0.47496 0.33657 0.44517 0.03198  0.02813  0.06572  280 TYR A CB  
749  C  CG  . TYR A 280 ? 0.46948 0.33234 0.42744 0.02788  0.02205  0.05951  280 TYR A CG  
750  C  CD1 . TYR A 280 ? 0.44274 0.31616 0.39485 0.02942  0.01684  0.06161  280 TYR A CD1 
751  C  CD2 . TYR A 280 ? 0.38549 0.23953 0.33820 0.02233  0.02185  0.05142  280 TYR A CD2 
752  C  CE1 . TYR A 280 ? 0.41462 0.28879 0.35672 0.02568  0.01205  0.05586  280 TYR A CE1 
753  C  CE2 . TYR A 280 ? 0.48035 0.33565 0.42291 0.01885  0.01672  0.04638  280 TYR A CE2 
754  C  CZ  . TYR A 280 ? 0.47158 0.33647 0.40925 0.02059  0.01207  0.04855  280 TYR A CZ  
755  O  OH  . TYR A 280 ? 0.39443 0.26008 0.32319 0.01713  0.00774  0.04353  280 TYR A OH  
756  N  N   . GLU A 281 ? 0.50171 0.38141 0.47735 0.04198  0.02676  0.08430  281 GLU A N   
757  C  CA  . GLU A 281 ? 0.57577 0.46582 0.54687 0.04424  0.02277  0.08918  281 GLU A CA  
758  C  C   . GLU A 281 ? 0.52550 0.42646 0.48827 0.04353  0.01660  0.08674  281 GLU A C   
759  O  O   . GLU A 281 ? 0.52967 0.43694 0.48571 0.04307  0.01273  0.08710  281 GLU A O   
760  C  CB  . GLU A 281 ? 0.58608 0.48294 0.56667 0.05041  0.02606  0.10024  281 GLU A CB  
761  C  CG  . GLU A 281 ? 0.72382 0.61064 0.71245 0.05125  0.03226  0.10326  281 GLU A CG  
762  C  CD  . GLU A 281 ? 0.96476 0.85801 0.96407 0.05774  0.03627  0.11495  281 GLU A CD  
763  O  OE1 . GLU A 281 ? 0.89996 0.80310 0.90371 0.06167  0.03596  0.12057  281 GLU A OE1 
764  O  OE2 . GLU A 281 ? 1.02988 0.91861 1.03352 0.05897  0.03985  0.11878  281 GLU A OE2 
765  N  N   . LYS A 282 ? 0.48569 0.38881 0.44900 0.04316  0.01594  0.08386  282 LYS A N   
766  C  CA  . LYS A 282 ? 0.60101 0.51465 0.55752 0.04239  0.01071  0.08116  282 LYS A CA  
767  C  C   . LYS A 282 ? 0.52542 0.43333 0.47950 0.03887  0.01032  0.07317  282 LYS A C   
768  O  O   . LYS A 282 ? 0.46949 0.37120 0.43022 0.03937  0.01425  0.07297  282 LYS A O   
769  C  CB  . LYS A 282 ? 0.48796 0.41626 0.44939 0.04742  0.01003  0.08899  282 LYS A CB  
770  C  CG  . LYS A 282 ? 0.72023 0.65836 0.68184 0.05076  0.00901  0.09690  282 LYS A CG  
771  C  CD  . LYS A 282 ? 0.94633 0.89590 0.89834 0.04898  0.00336  0.09431  282 LYS A CD  
772  N  N   . ALA A 283 ? 0.42657 0.33650 0.37158 0.03530  0.00599  0.06664  283 ALA A N   
773  C  CA  . ALA A 283 ? 0.42110 0.32711 0.36353 0.03221  0.00538  0.05945  283 ALA A CA  
774  C  C   . ALA A 283 ? 0.41796 0.33294 0.35298 0.03052  0.00062  0.05552  283 ALA A C   
775  O  O   . ALA A 283 ? 0.39728 0.30733 0.32650 0.02652  -0.00086 0.04838  283 ALA A O   
776  C  CB  . ALA A 283 ? 0.41971 0.31160 0.35939 0.02771  0.00704  0.05308  283 ALA A CB  
777  N  N   . ILE A 284 ? 0.38482 0.31348 0.32008 0.03339  -0.00161 0.06018  284 ILE A N   
778  C  CA  . ILE A 284 ? 0.37848 0.31640 0.30701 0.03138  -0.00567 0.05597  284 ILE A CA  
779  C  C   . ILE A 284 ? 0.38902 0.32725 0.31724 0.02976  -0.00613 0.05044  284 ILE A C   
780  O  O   . ILE A 284 ? 0.40950 0.34958 0.33186 0.02658  -0.00847 0.04423  284 ILE A O   
781  C  CB  . ILE A 284 ? 0.45879 0.41263 0.38791 0.03456  -0.00768 0.06214  284 ILE A CB  
782  C  CG1 . ILE A 284 ? 0.44065 0.39337 0.36864 0.03544  -0.00739 0.06651  284 ILE A CG1 
783  C  CG2 . ILE A 284 ? 0.51452 0.47916 0.43764 0.03223  -0.01128 0.05731  284 ILE A CG2 
784  C  CD1 . ILE A 284 ? 0.48756 0.45608 0.41611 0.03867  -0.00902 0.07347  284 ILE A CD1 
785  N  N   . GLY A 285 ? 0.40609 0.34246 0.34113 0.03193  -0.00355 0.05262  285 GLY A N   
786  C  CA  . GLY A 285 ? 0.40300 0.33928 0.33834 0.03057  -0.00364 0.04764  285 GLY A CA  
787  C  C   . GLY A 285 ? 0.41050 0.33429 0.34099 0.02598  -0.00314 0.03963  285 GLY A C   
788  O  O   . GLY A 285 ? 0.36339 0.28724 0.29285 0.02435  -0.00351 0.03471  285 GLY A O   
789  N  N   . PHE A 286 ? 0.34167 0.25540 0.26936 0.02390  -0.00227 0.03846  286 PHE A N   
790  C  CA  . PHE A 286 ? 0.36790 0.27075 0.29062 0.01940  -0.00203 0.03149  286 PHE A CA  
791  C  C   . PHE A 286 ? 0.32378 0.22765 0.23898 0.01650  -0.00503 0.02798  286 PHE A C   
792  O  O   . PHE A 286 ? 0.32792 0.22390 0.23893 0.01291  -0.00510 0.02296  286 PHE A O   
793  C  CB  . PHE A 286 ? 0.35877 0.24963 0.28396 0.01850  0.00131  0.03213  286 PHE A CB  
794  C  CG  . PHE A 286 ? 0.36033 0.24737 0.29299 0.02018  0.00523  0.03373  286 PHE A CG  
795  C  CD1 . PHE A 286 ? 0.41630 0.30835 0.35689 0.02476  0.00728  0.04092  286 PHE A CD1 
796  C  CD2 . PHE A 286 ? 0.40796 0.28657 0.34008 0.01717  0.00718  0.02821  286 PHE A CD2 
797  C  CE1 . PHE A 286 ? 0.41915 0.30729 0.36788 0.02639  0.01159  0.04255  286 PHE A CE1 
798  C  CE2 . PHE A 286 ? 0.39560 0.27025 0.33514 0.01846  0.01138  0.02928  286 PHE A CE2 
799  C  CZ  . PHE A 286 ? 0.37773 0.25678 0.32587 0.02305  0.01373  0.03633  286 PHE A CZ  
800  N  N   . MET A 287 ? 0.34266 0.25610 0.25642 0.01795  -0.00722 0.03084  287 MET A N   
801  C  CA  . MET A 287 ? 0.31063 0.22480 0.21824 0.01526  -0.00942 0.02780  287 MET A CA  
802  C  C   . MET A 287 ? 0.35429 0.27335 0.25856 0.01302  -0.01101 0.02204  287 MET A C   
803  O  O   . MET A 287 ? 0.35274 0.27890 0.25929 0.01426  -0.01120 0.02153  287 MET A O   
804  C  CB  . MET A 287 ? 0.33971 0.26234 0.24719 0.01740  -0.01068 0.03281  287 MET A CB  
805  C  CG  . MET A 287 ? 0.37223 0.28926 0.28303 0.01943  -0.00879 0.03844  287 MET A CG  
806  S  SD  . MET A 287 ? 0.37450 0.27741 0.28204 0.01575  -0.00797 0.03511  287 MET A SD  
807  C  CE  . MET A 287 ? 0.41297 0.30519 0.32552 0.01572  -0.00434 0.03478  287 MET A CE  
808  N  N   . PRO A 288 ? 0.32791 0.24296 0.22743 0.00966  -0.01180 0.01758  288 PRO A N   
809  C  CA  . PRO A 288 ? 0.30345 0.22313 0.20055 0.00747  -0.01266 0.01205  288 PRO A CA  
810  C  C   . PRO A 288 ? 0.33659 0.26992 0.23349 0.00844  -0.01417 0.01277  288 PRO A C   
811  O  O   . PRO A 288 ? 0.37009 0.30733 0.26594 0.00911  -0.01496 0.01581  288 PRO A O   
812  C  CB  . PRO A 288 ? 0.36113 0.27299 0.25426 0.00406  -0.01266 0.00862  288 PRO A CB  
813  C  CG  . PRO A 288 ? 0.40644 0.30861 0.29978 0.00414  -0.01189 0.01162  288 PRO A CG  
814  C  CD  . PRO A 288 ? 0.33885 0.24489 0.23577 0.00769  -0.01160 0.01749  288 PRO A CD  
815  N  N   . ASN A 289 ? 0.35888 0.29983 0.25687 0.00834  -0.01444 0.00981  289 ASN A N   
816  C  CA  . ASN A 289 ? 0.35910 0.31488 0.25727 0.00900  -0.01581 0.01002  289 ASN A CA  
817  C  C   . ASN A 289 ? 0.31084 0.26976 0.20521 0.00624  -0.01627 0.00687  289 ASN A C   
818  O  O   . ASN A 289 ? 0.36413 0.31737 0.25658 0.00314  -0.01536 0.00151  289 ASN A O   
819  C  CB  . ASN A 289 ? 0.34097 0.30259 0.24103 0.00854  -0.01568 0.00597  289 ASN A CB  
820  C  CG  . ASN A 289 ? 0.41631 0.39475 0.31701 0.00905  -0.01714 0.00599  289 ASN A CG  
821  O  OD1 . ASN A 289 ? 0.37263 0.35699 0.27065 0.00634  -0.01741 0.00169  289 ASN A OD1 
822  N  ND2 . ASN A 289 ? 0.38393 0.37058 0.28859 0.01234  -0.01782 0.01070  289 ASN A ND2 
823  N  N   . LEU A 290 ? 0.30632 0.27482 0.20003 0.00739  -0.01739 0.01038  290 LEU A N   
824  C  CA  . LEU A 290 ? 0.42295 0.39397 0.31342 0.00483  -0.01742 0.00788  290 LEU A CA  
825  C  C   . LEU A 290 ? 0.39441 0.37531 0.28401 0.00185  -0.01715 0.00128  290 LEU A C   
826  O  O   . LEU A 290 ? 0.43678 0.41662 0.32445 -0.00117 -0.01612 -0.00280 290 LEU A O   
827  C  CB  . LEU A 290 ? 0.41030 0.38787 0.30025 0.00699  -0.01844 0.01402  290 LEU A CB  
828  C  CG  . LEU A 290 ? 0.38616 0.35227 0.27638 0.00863  -0.01799 0.01910  290 LEU A CG  
829  C  CD1 . LEU A 290 ? 0.49423 0.46775 0.38527 0.01177  -0.01872 0.02631  290 LEU A CD1 
830  C  CD2 . LEU A 290 ? 0.37940 0.33647 0.26687 0.00555  -0.01722 0.01580  290 LEU A CD2 
831  N  N   . VAL A 291 ? 0.38727 0.37749 0.27882 0.00247  -0.01769 -0.00011 291 VAL A N   
832  C  CA  . VAL A 291 ? 0.37250 0.37086 0.26370 -0.00090 -0.01690 -0.00751 291 VAL A CA  
833  C  C   . VAL A 291 ? 0.41562 0.40262 0.30737 -0.00323 -0.01485 -0.01324 291 VAL A C   
834  O  O   . VAL A 291 ? 0.40355 0.39036 0.29465 -0.00668 -0.01303 -0.01920 291 VAL A O   
835  C  CB  . VAL A 291 ? 0.49474 0.50849 0.38798 0.00034  -0.01830 -0.00709 291 VAL A CB  
836  C  CG1 . VAL A 291 ? 0.44737 0.46901 0.34079 -0.00354 -0.01710 -0.01565 291 VAL A CG1 
837  C  CG2 . VAL A 291 ? 0.47582 0.50238 0.36816 0.00225  -0.02020 -0.00134 291 VAL A CG2 
838  N  N   . ALA A 292 ? 0.43040 0.32751 0.25874 0.00014  0.00675  -0.03090 292 ALA A N   
839  C  CA  . ALA A 292 ? 0.43020 0.32992 0.27334 0.00130  0.00823  -0.03298 292 ALA A CA  
840  C  C   . ALA A 292 ? 0.39729 0.29749 0.24792 0.00462  0.01807  -0.03056 292 ALA A C   
841  O  O   . ALA A 292 ? 0.39422 0.29175 0.24972 0.00560  0.02264  -0.03372 292 ALA A O   
842  C  CB  . ALA A 292 ? 0.41508 0.32316 0.27281 0.00089  0.00064  -0.03032 292 ALA A CB  
843  N  N   . TYR A 293 ? 0.36742 0.27076 0.21968 0.00634  0.02142  -0.02476 293 TYR A N   
844  C  CA  . TYR A 293 ? 0.33785 0.24355 0.20068 0.00958  0.02963  -0.02130 293 TYR A CA  
845  C  C   . TYR A 293 ? 0.35198 0.25412 0.20468 0.01046  0.03709  -0.01923 293 TYR A C   
846  O  O   . TYR A 293 ? 0.38985 0.29620 0.24477 0.01093  0.03686  -0.01344 293 TYR A O   
847  C  CB  . TYR A 293 ? 0.32410 0.23917 0.20338 0.01067  0.02592  -0.01568 293 TYR A CB  
848  C  CG  . TYR A 293 ? 0.30769 0.22713 0.19432 0.00890  0.01718  -0.01723 293 TYR A CG  
849  C  CD1 . TYR A 293 ? 0.32394 0.24194 0.21470 0.00848  0.01688  -0.02129 293 TYR A CD1 
850  C  CD2 . TYR A 293 ? 0.32035 0.24520 0.21043 0.00759  0.00974  -0.01462 293 TYR A CD2 
851  C  CE1 . TYR A 293 ? 0.33437 0.25638 0.23170 0.00659  0.00978  -0.02288 293 TYR A CE1 
852  C  CE2 . TYR A 293 ? 0.34260 0.27150 0.24001 0.00594  0.00265  -0.01658 293 TYR A CE2 
853  C  CZ  . TYR A 293 ? 0.34946 0.27709 0.25014 0.00536  0.00290  -0.02073 293 TYR A CZ  
854  O  OH  . TYR A 293 ? 0.33395 0.26597 0.24224 0.00350  -0.00343 -0.02263 293 TYR A OH  
855  N  N   . PRO A 294 ? 0.41036 0.30459 0.25188 0.01051  0.04418  -0.02405 294 PRO A N   
856  C  CA  . PRO A 294 ? 0.46190 0.35207 0.29132 0.01082  0.05206  -0.02288 294 PRO A CA  
857  C  C   . PRO A 294 ? 0.39629 0.29023 0.23867 0.01422  0.06096  -0.01793 294 PRO A C   
858  O  O   . PRO A 294 ? 0.43205 0.32928 0.29083 0.01666  0.06313  -0.01717 294 PRO A O   
859  C  CB  . PRO A 294 ? 0.53202 0.41253 0.34735 0.00980  0.05733  -0.03096 294 PRO A CB  
860  C  CG  . PRO A 294 ? 0.49829 0.37771 0.31490 0.00791  0.04912  -0.03592 294 PRO A CG  
861  C  CD  . PRO A 294 ? 0.41524 0.30319 0.25212 0.00940  0.04418  -0.03156 294 PRO A CD  
862  N  N   . LYS A 295 ? 0.45371 0.34690 0.28816 0.01417  0.06618  -0.01440 295 LYS A N   
863  C  CA  . LYS A 295 ? 0.53132 0.42778 0.37778 0.01719  0.07565  -0.00983 295 LYS A CA  
864  C  C   . LYS A 295 ? 0.51748 0.40926 0.36801 0.01963  0.08629  -0.01441 295 LYS A C   
865  O  O   . LYS A 295 ? 0.53663 0.42104 0.37657 0.01864  0.08789  -0.02157 295 LYS A O   
866  C  CB  . LYS A 295 ? 0.51622 0.41194 0.35186 0.01617  0.07993  -0.00542 295 LYS A CB  
867  C  CG  . LYS A 295 ? 0.52127 0.42268 0.35858 0.01456  0.07057  0.00093  295 LYS A CG  
868  C  CD  . LYS A 295 ? 0.77590 0.68661 0.63718 0.01661  0.06625  0.00523  295 LYS A CD  
869  C  CE  . LYS A 295 ? 0.85813 0.77484 0.73059 0.01768  0.06930  0.01300  295 LYS A CE  
870  N  NZ  . LYS A 295 ? 0.67540 0.59132 0.55220 0.01987  0.08209  0.01472  295 LYS A NZ  
871  N  N   . PRO A 296 ? 0.53524 0.43138 0.40302 0.02290  0.09331  -0.01044 296 PRO A N   
872  C  CA  . PRO A 296 ? 0.52072 0.41291 0.39612 0.02569  0.10322  -0.01429 296 PRO A CA  
873  C  C   . PRO A 296 ? 0.78513 0.66808 0.64328 0.02497  0.11358  -0.02025 296 PRO A C   
874  O  O   . PRO A 296 ? 0.60850 0.48647 0.47082 0.02685  0.12139  -0.02529 296 PRO A O   
875  C  CB  . PRO A 296 ? 0.63749 0.53725 0.53450 0.02899  0.10795  -0.00752 296 PRO A CB  
876  C  CG  . PRO A 296 ? 0.59197 0.50015 0.49592 0.02792  0.09756  -0.00132 296 PRO A CG  
877  C  CD  . PRO A 296 ? 0.50200 0.40737 0.38598 0.02425  0.09132  -0.00239 296 PRO A CD  
878  N  N   . SER A 297 ? 0.47634 0.35652 0.31509 0.02218  0.11397  -0.01993 297 SER A N   
879  C  CA  . SER A 297 ? 0.55157 0.42251 0.37151 0.02099  0.12393  -0.02631 297 SER A CA  
880  C  C   . SER A 297 ? 0.62650 0.48949 0.43227 0.01872  0.12001  -0.03527 297 SER A C   
881  O  O   . SER A 297 ? 0.67600 0.53056 0.46831 0.01795  0.12853  -0.04247 297 SER A O   
882  C  CB  . SER A 297 ? 0.63268 0.50288 0.43465 0.01832  0.12545  -0.02262 297 SER A CB  
883  O  OG  . SER A 297 ? 0.80687 0.68026 0.60228 0.01562  0.11209  -0.01889 297 SER A OG  
884  N  N   . ASN A 298 ? 0.65782 0.52343 0.46758 0.01760  0.10775  -0.03531 298 ASN A N   
885  C  CA  . ASN A 298 ? 0.81482 0.67380 0.61273 0.01502  0.10239  -0.04327 298 ASN A CA  
886  C  C   . ASN A 298 ? 0.92219 0.77413 0.72418 0.01676  0.11156  -0.05090 298 ASN A C   
887  O  O   . ASN A 298 ? 0.92487 0.77927 0.74631 0.02056  0.11812  -0.04892 298 ASN A O   
888  C  CB  . ASN A 298 ? 0.58632 0.45094 0.39472 0.01434  0.08927  -0.04110 298 ASN A CB  
889  C  CG  . ASN A 298 ? 0.83146 0.69097 0.62426 0.01042  0.08063  -0.04732 298 ASN A CG  
890  O  OD1 . ASN A 298 ? 0.85428 0.70996 0.62673 0.00732  0.07842  -0.04895 298 ASN A OD1 
891  N  ND2 . ASN A 298 ? 0.63751 0.49696 0.43990 0.01036  0.07558  -0.05055 298 ASN A ND2 
892  N  N   . SER A 299 ? 0.83535 0.67838 0.61938 0.01384  0.11147  -0.05972 299 SER A N   
893  C  CA  . SER A 299 ? 0.74354 0.57877 0.53071 0.01494  0.11907  -0.06818 299 SER A CA  
894  C  C   . SER A 299 ? 0.89084 0.72977 0.70285 0.01793  0.11654  -0.06619 299 SER A C   
895  O  O   . SER A 299 ? 0.77344 0.61103 0.60067 0.02147  0.12562  -0.06681 299 SER A O   
896  C  CB  . SER A 299 ? 0.89814 0.72473 0.66423 0.01057  0.11466  -0.07752 299 SER A CB  
897  N  N   . LYS A 300 ? 0.52801 0.37146 0.34431 0.01640  0.10427  -0.06371 300 LYS A N   
898  C  CA  . LYS A 300 ? 0.66720 0.51368 0.50343 0.01814  0.10027  -0.06203 300 LYS A CA  
899  C  C   . LYS A 300 ? 0.76735 0.62486 0.61568 0.01886  0.09186  -0.05275 300 LYS A C   
900  O  O   . LYS A 300 ? 0.60476 0.46602 0.44353 0.01646  0.08437  -0.05016 300 LYS A O   
901  C  CB  . LYS A 300 ? 0.69703 0.53777 0.52681 0.01500  0.09383  -0.06922 300 LYS A CB  
902  C  CG  . LYS A 300 ? 0.75074 0.59427 0.59943 0.01606  0.08913  -0.06728 300 LYS A CG  
903  C  CD  . LYS A 300 ? 0.93109 0.77511 0.79963 0.02054  0.09740  -0.06424 300 LYS A CD  
904  C  CE  . LYS A 300 ? 0.98300 0.82431 0.86434 0.02070  0.09516  -0.06596 300 LYS A CE  
905  N  NZ  . LYS A 300 ? 0.81537 0.66333 0.70131 0.01870  0.08388  -0.06180 300 LYS A NZ  
906  N  N   . LYS A 301 ? 0.55270 0.41526 0.42203 0.02215  0.09333  -0.04768 301 LYS A N   
907  C  CA  . LYS A 301 ? 0.47263 0.34533 0.35432 0.02263  0.08527  -0.03982 301 LYS A CA  
908  C  C   . LYS A 301 ? 0.55205 0.42511 0.43900 0.02101  0.07724  -0.04134 301 LYS A C   
909  O  O   . LYS A 301 ? 0.65061 0.51873 0.54426 0.02194  0.08053  -0.04455 301 LYS A O   
910  C  CB  . LYS A 301 ? 0.61467 0.49303 0.51562 0.02671  0.09071  -0.03320 301 LYS A CB  
911  N  N   . TYR A 302 ? 0.47975 0.35800 0.36357 0.01842  0.06717  -0.03948 302 TYR A N   
912  C  CA  . TYR A 302 ? 0.41328 0.29186 0.30122 0.01643  0.06006  -0.04137 302 TYR A CA  
913  C  C   . TYR A 302 ? 0.35185 0.23972 0.25532 0.01744  0.05520  -0.03438 302 TYR A C   
914  O  O   . TYR A 302 ? 0.40950 0.30450 0.31541 0.01789  0.05255  -0.02920 302 TYR A O   
915  C  CB  . TYR A 302 ? 0.67807 0.55518 0.55172 0.01234  0.05208  -0.04565 302 TYR A CB  
916  C  CG  . TYR A 302 ? 0.59018 0.45712 0.44861 0.01043  0.05517  -0.05407 302 TYR A CG  
917  C  CD1 . TYR A 302 ? 0.68851 0.54875 0.54995 0.00999  0.05759  -0.05972 302 TYR A CD1 
918  C  CD2 . TYR A 302 ? 0.90334 0.76715 0.74432 0.00891  0.05576  -0.05625 302 TYR A CD2 
919  C  CE1 . TYR A 302 ? 0.80497 0.65568 0.65268 0.00802  0.06047  -0.06816 302 TYR A CE1 
920  C  CE2 . TYR A 302 ? 0.60723 0.46165 0.43293 0.00682  0.05848  -0.06436 302 TYR A CE2 
921  C  CZ  . TYR A 302 ? 0.80164 0.64958 0.63097 0.00636  0.06074  -0.07068 302 TYR A CZ  
922  O  OH  . TYR A 302 ? 0.93500 0.77333 0.74919 0.00400  0.06332  -0.07957 302 TYR A OH  
923  N  N   . ALA A 303 ? 0.35457 0.24220 0.26748 0.01725  0.05342  -0.03450 303 ALA A N   
924  C  CA  . ALA A 303 ? 0.35193 0.24820 0.27800 0.01784  0.04895  -0.02798 303 ALA A CA  
925  C  C   . ALA A 303 ? 0.34869 0.25134 0.27142 0.01498  0.04007  -0.02719 303 ALA A C   
926  O  O   . ALA A 303 ? 0.30762 0.21812 0.23943 0.01524  0.03641  -0.02209 303 ALA A O   
927  C  CB  . ALA A 303 ? 0.41713 0.31134 0.35321 0.01807  0.04940  -0.02760 303 ALA A CB  
928  N  N   . ARG A 304 ? 0.33706 0.23672 0.24752 0.01219  0.03627  -0.03217 304 ARG A N   
929  C  CA  . ARG A 304 ? 0.30910 0.21507 0.21917 0.00969  0.02780  -0.03133 304 ARG A CA  
930  C  C   . ARG A 304 ? 0.30096 0.21371 0.21264 0.01079  0.02630  -0.02614 304 ARG A C   
931  O  O   . ARG A 304 ? 0.31619 0.23506 0.23075 0.00923  0.01980  -0.02471 304 ARG A O   
932  C  CB  . ARG A 304 ? 0.40987 0.31131 0.30792 0.00647  0.02326  -0.03748 304 ARG A CB  
933  C  CG  . ARG A 304 ? 0.40465 0.30155 0.28883 0.00643  0.02516  -0.03936 304 ARG A CG  
934  C  CD  . ARG A 304 ? 0.60105 0.49342 0.47300 0.00290  0.01946  -0.04539 304 ARG A CD  
935  N  NE  . ARG A 304 ? 0.50309 0.39152 0.35993 0.00260  0.02079  -0.04622 304 ARG A NE  
936  C  CZ  . ARG A 304 ? 0.45175 0.33595 0.29501 -0.00033 0.01600  -0.05058 304 ARG A CZ  
937  N  NH1 . ARG A 304 ? 0.45975 0.34319 0.30384 -0.00319 0.00934  -0.05499 304 ARG A NH1 
938  N  NH2 . ARG A 304 ? 0.45323 0.33389 0.28196 -0.00055 0.01804  -0.05040 304 ARG A NH2 
939  N  N   . ASP A 305 ? 0.30870 0.22042 0.21962 0.01337  0.03252  -0.02350 305 ASP A N   
940  C  CA  . ASP A 305 ? 0.32384 0.24219 0.23844 0.01436  0.03142  -0.01808 305 ASP A CA  
941  C  C   . ASP A 305 ? 0.32254 0.24838 0.25242 0.01592  0.03077  -0.01282 305 ASP A C   
942  O  O   . ASP A 305 ? 0.31247 0.24397 0.24772 0.01690  0.03036  -0.00827 305 ASP A O   
943  C  CB  . ASP A 305 ? 0.37195 0.28672 0.27978 0.01612  0.03852  -0.01706 305 ASP A CB  
944  C  CG  . ASP A 305 ? 0.43021 0.34187 0.34438 0.01920  0.04763  -0.01646 305 ASP A CG  
945  O  OD1 . ASP A 305 ? 0.43972 0.35285 0.36524 0.02041  0.04808  -0.01529 305 ASP A OD1 
946  O  OD2 . ASP A 305 ? 0.46973 0.37722 0.37749 0.02042  0.05480  -0.01705 305 ASP A OD2 
947  N  N   . ILE A 306 ? 0.29328 0.21940 0.23004 0.01576  0.03000  -0.01322 306 ILE A N   
948  C  CA  . ILE A 306 ? 0.29548 0.22844 0.24531 0.01676  0.02859  -0.00822 306 ILE A CA  
949  C  C   . ILE A 306 ? 0.27282 0.20970 0.22454 0.01389  0.02186  -0.00937 306 ILE A C   
950  O  O   . ILE A 306 ? 0.27176 0.20437 0.21868 0.01196  0.02063  -0.01371 306 ILE A O   
951  C  CB  . ILE A 306 ? 0.24441 0.17409 0.20158 0.01929  0.03442  -0.00649 306 ILE A CB  
952  C  CG1 . ILE A 306 ? 0.30293 0.22977 0.26075 0.02235  0.04197  -0.00521 306 ILE A CG1 
953  C  CG2 . ILE A 306 ? 0.27997 0.21669 0.24950 0.01967  0.03134  -0.00107 306 ILE A CG2 
954  C  CD1 . ILE A 306 ? 0.36001 0.28150 0.32440 0.02488  0.04850  -0.00515 306 ILE A CD1 
955  N  N   . VAL A 307 ? 0.24638 0.19137 0.20563 0.01346  0.01790  -0.00575 307 VAL A N   
956  C  CA  . VAL A 307 ? 0.23686 0.18618 0.19947 0.01091  0.01294  -0.00626 307 VAL A CA  
957  C  C   . VAL A 307 ? 0.27777 0.23215 0.25008 0.01198  0.01308  -0.00090 307 VAL A C   
958  O  O   . VAL A 307 ? 0.29505 0.25392 0.27308 0.01364  0.01333  0.00303  307 VAL A O   
959  C  CB  . VAL A 307 ? 0.28912 0.24377 0.25081 0.00861  0.00713  -0.00798 307 VAL A CB  
960  C  CG1 . VAL A 307 ? 0.32429 0.28382 0.29014 0.00595  0.00326  -0.00868 307 VAL A CG1 
961  C  CG2 . VAL A 307 ? 0.42923 0.37930 0.38214 0.00735  0.00573  -0.01261 307 VAL A CG2 
962  N  N   . TYR A 308 ? 0.25448 0.20832 0.22881 0.01079  0.01254  -0.00041 308 TYR A N   
963  C  CA  . TYR A 308 ? 0.26686 0.22580 0.24917 0.01118  0.01136  0.00508  308 TYR A CA  
964  C  C   . TYR A 308 ? 0.26778 0.23307 0.24993 0.00771  0.00606  0.00447  308 TYR A C   
965  O  O   . TYR A 308 ? 0.29265 0.25646 0.27014 0.00500  0.00472  0.00026  308 TYR A O   
966  C  CB  . TYR A 308 ? 0.24711 0.20095 0.23232 0.01225  0.01462  0.00745  308 TYR A CB  
967  C  CG  . TYR A 308 ? 0.27979 0.22941 0.27011 0.01621  0.02011  0.01013  308 TYR A CG  
968  C  CD1 . TYR A 308 ? 0.37033 0.32460 0.37050 0.01857  0.02020  0.01636  308 TYR A CD1 
969  C  CD2 . TYR A 308 ? 0.29629 0.23742 0.28223 0.01748  0.02527  0.00611  308 TYR A CD2 
970  C  CE1 . TYR A 308 ? 0.35942 0.31010 0.36637 0.02235  0.02578  0.01875  308 TYR A CE1 
971  C  CE2 . TYR A 308 ? 0.28527 0.22234 0.27662 0.02113  0.03131  0.00794  308 TYR A CE2 
972  C  CZ  . TYR A 308 ? 0.35065 0.29264 0.35316 0.02364  0.03169  0.01436  308 TYR A CZ  
973  O  OH  . TYR A 308 ? 0.33363 0.27196 0.34318 0.02736  0.03813  0.01592  308 TYR A OH  
974  N  N   . GLY A 309 ? 0.22751 0.19983 0.21527 0.00764  0.00331  0.00857  309 GLY A N   
975  C  CA  . GLY A 309 ? 0.23465 0.21277 0.22180 0.00417  -0.00096 0.00808  309 GLY A CA  
976  C  C   . GLY A 309 ? 0.29953 0.28240 0.29230 0.00457  -0.00275 0.01432  309 GLY A C   
977  O  O   . GLY A 309 ? 0.29288 0.27505 0.29157 0.00770  -0.00100 0.01884  309 GLY A O   
978  N  N   . THR A 310 ? 0.25491 0.24249 0.24582 0.00125  -0.00614 0.01465  310 THR A N   
979  C  CA  . THR A 310 ? 0.23310 0.22597 0.22788 0.00089  -0.00921 0.02054  310 THR A CA  
980  C  C   . THR A 310 ? 0.28039 0.28108 0.27468 -0.00190 -0.01365 0.01817  310 THR A C   
981  O  O   . THR A 310 ? 0.29483 0.29669 0.28418 -0.00491 -0.01429 0.01267  310 THR A O   
982  C  CB  . THR A 310 ? 0.34068 0.33183 0.33228 -0.00107 -0.00933 0.02390  310 THR A CB  
983  O  OG1 . THR A 310 ? 0.35933 0.34263 0.35244 0.00143  -0.00503 0.02556  310 THR A OG1 
984  C  CG2 . THR A 310 ? 0.31961 0.31626 0.31489 -0.00140 -0.01344 0.03102  310 THR A CG2 
985  N  N   . ILE A 311 ? 0.24667 0.25264 0.24720 -0.00087 -0.01654 0.02182  311 ILE A N   
986  C  CA  . ILE A 311 ? 0.24958 0.26302 0.24987 -0.00393 -0.02113 0.01965  311 ILE A CA  
987  C  C   . ILE A 311 ? 0.24769 0.26567 0.24919 -0.00516 -0.02516 0.02560  311 ILE A C   
988  O  O   . ILE A 311 ? 0.26777 0.28302 0.27163 -0.00322 -0.02436 0.03172  311 ILE A O   
989  C  CB  . ILE A 311 ? 0.25571 0.27192 0.26238 -0.00243 -0.02189 0.01754  311 ILE A CB  
990  C  CG1 . ILE A 311 ? 0.30485 0.31976 0.32007 0.00184  -0.02005 0.02286  311 ILE A CG1 
991  C  CG2 . ILE A 311 ? 0.24999 0.26229 0.25322 -0.00245 -0.01926 0.01127  311 ILE A CG2 
992  C  CD1 . ILE A 311 ? 0.34997 0.36979 0.37228 0.00237  -0.02351 0.02939  311 ILE A CD1 
993  N  N   . TYR A 312 ? 0.26059 0.28530 0.26058 -0.00847 -0.02969 0.02387  312 TYR A N   
994  C  CA  . TYR A 312 ? 0.21628 0.24540 0.21430 -0.01074 -0.03434 0.02895  312 TYR A CA  
995  C  C   . TYR A 312 ? 0.23115 0.26743 0.23577 -0.01122 -0.03949 0.02953  312 TYR A C   
996  O  O   . TYR A 312 ? 0.27453 0.31414 0.27926 -0.01309 -0.04056 0.02331  312 TYR A O   
997  C  CB  . TYR A 312 ? 0.24686 0.27684 0.23313 -0.01569 -0.03474 0.02575  312 TYR A CB  
998  C  CG  . TYR A 312 ? 0.25582 0.27857 0.23779 -0.01498 -0.02986 0.02662  312 TYR A CG  
999  C  CD1 . TYR A 312 ? 0.26957 0.28792 0.25048 -0.01438 -0.02536 0.02046  312 TYR A CD1 
1000 C  CD2 . TYR A 312 ? 0.27137 0.29147 0.25201 -0.01459 -0.03011 0.03406  312 TYR A CD2 
1001 C  CE1 . TYR A 312 ? 0.27397 0.28552 0.25199 -0.01377 -0.02116 0.02103  312 TYR A CE1 
1002 C  CE2 . TYR A 312 ? 0.27544 0.28848 0.25363 -0.01388 -0.02556 0.03484  312 TYR A CE2 
1003 C  CZ  . TYR A 312 ? 0.31532 0.32419 0.29217 -0.01356 -0.02110 0.02807  312 TYR A CZ  
1004 O  OH  . TYR A 312 ? 0.33935 0.34115 0.31449 -0.01304 -0.01687 0.02844  312 TYR A OH  
1005 N  N   . LEU A 313 ? 0.24042 0.27893 0.25185 -0.00948 -0.04272 0.03698  313 LEU A N   
1006 C  CA  . LEU A 313 ? 0.25494 0.30028 0.27484 -0.00968 -0.04792 0.03828  313 LEU A CA  
1007 C  C   . LEU A 313 ? 0.26571 0.31711 0.27748 -0.01513 -0.05377 0.03584  313 LEU A C   
1008 O  O   . LEU A 313 ? 0.30674 0.35824 0.30960 -0.01772 -0.05586 0.03901  313 LEU A O   
1009 C  CB  . LEU A 313 ? 0.26179 0.30804 0.29266 -0.00627 -0.04993 0.04727  313 LEU A CB  
1010 C  CG  . LEU A 313 ? 0.29530 0.33518 0.33406 -0.00089 -0.04334 0.04976  313 LEU A CG  
1011 C  CD1 . LEU A 313 ? 0.28259 0.32467 0.33528 0.00247  -0.04546 0.05824  313 LEU A CD1 
1012 C  CD2 . LEU A 313 ? 0.30025 0.33820 0.34211 0.00088  -0.03857 0.04372  313 LEU A CD2 
1013 N  N   . GLY A 314 ? 0.29018 0.34629 0.30473 -0.01703 -0.05617 0.03015  314 GLY A N   
1014 C  CA  . GLY A 314 ? 0.28724 0.34895 0.29389 -0.02247 -0.06121 0.02618  314 GLY A CA  
1015 C  C   . GLY A 314 ? 0.30766 0.36710 0.30024 -0.02615 -0.05801 0.02038  314 GLY A C   
1016 O  O   . GLY A 314 ? 0.33672 0.40002 0.31980 -0.03110 -0.06114 0.01739  314 GLY A O   
1017 N  N   . GLY A 315 ? 0.31220 0.36546 0.30336 -0.02401 -0.05165 0.01847  315 GLY A N   
1018 C  CA  . GLY A 315 ? 0.31848 0.36962 0.29814 -0.02736 -0.04821 0.01333  315 GLY A CA  
1019 C  C   . GLY A 315 ? 0.30283 0.35298 0.27197 -0.02978 -0.04891 0.01872  315 GLY A C   
1020 O  O   . GLY A 315 ? 0.32897 0.37858 0.28766 -0.03361 -0.04644 0.01465  315 GLY A O   
1021 N  N   . LYS A 316 ? 0.31421 0.36403 0.28661 -0.02767 -0.05199 0.02809  316 LYS A N   
1022 C  CA  . LYS A 316 ? 0.31228 0.36100 0.27515 -0.03001 -0.05336 0.03456  316 LYS A CA  
1023 C  C   . LYS A 316 ? 0.33739 0.37831 0.30046 -0.02725 -0.04749 0.03757  316 LYS A C   
1024 O  O   . LYS A 316 ? 0.26649 0.30359 0.23999 -0.02218 -0.04525 0.04019  316 LYS A O   
1025 C  CB  . LYS A 316 ? 0.28977 0.34216 0.25698 -0.02931 -0.06044 0.04367  316 LYS A CB  
1026 C  CG  . LYS A 316 ? 0.37228 0.43252 0.33785 -0.03291 -0.06728 0.04110  316 LYS A CG  
1027 C  CD  . LYS A 316 ? 0.56842 0.63203 0.53538 -0.03322 -0.07501 0.05125  316 LYS A CD  
1028 C  CE  . LYS A 316 ? 0.76399 0.83554 0.72834 -0.03735 -0.08294 0.04920  316 LYS A CE  
1029 N  NZ  . LYS A 316 ? 0.79960 0.87433 0.76731 -0.03710 -0.09121 0.06016  316 LYS A NZ  
1030 N  N   . PRO A 317 ? 0.31318 0.35144 0.26518 -0.03059 -0.04462 0.03720  317 PRO A N   
1031 C  CA  . PRO A 317 ? 0.29063 0.32119 0.24365 -0.02830 -0.03868 0.03857  317 PRO A CA  
1032 C  C   . PRO A 317 ? 0.30220 0.32871 0.26144 -0.02467 -0.03965 0.04879  317 PRO A C   
1033 O  O   . PRO A 317 ? 0.32729 0.34702 0.29106 -0.02153 -0.03475 0.04939  317 PRO A O   
1034 C  CB  . PRO A 317 ? 0.40308 0.43298 0.34311 -0.03361 -0.03575 0.03560  317 PRO A CB  
1035 C  CG  . PRO A 317 ? 0.41575 0.45221 0.34646 -0.03837 -0.04110 0.03701  317 PRO A CG  
1036 C  CD  . PRO A 317 ? 0.32550 0.36759 0.26355 -0.03692 -0.04599 0.03449  317 PRO A CD  
1037 N  N   . ASP A 318 ? 0.30412 0.33457 0.26498 -0.02485 -0.04599 0.05654  318 ASP A N   
1038 C  CA  . ASP A 318 ? 0.34589 0.37283 0.31537 -0.02099 -0.04718 0.06646  318 ASP A CA  
1039 C  C   . ASP A 318 ? 0.33507 0.36375 0.31995 -0.01585 -0.04883 0.06818  318 ASP A C   
1040 O  O   . ASP A 318 ? 0.31464 0.34262 0.30885 -0.01279 -0.05136 0.07678  318 ASP A O   
1041 C  CB  . ASP A 318 ? 0.40462 0.43403 0.36725 -0.02426 -0.05321 0.07556  318 ASP A CB  
1042 C  CG  . ASP A 318 ? 0.55904 0.59698 0.52129 -0.02631 -0.06150 0.07717  318 ASP A CG  
1043 O  OD1 . ASP A 318 ? 0.43580 0.47834 0.39886 -0.02710 -0.06221 0.06942  318 ASP A OD1 
1044 O  OD2 . ASP A 318 ? 0.59351 0.63346 0.55489 -0.02732 -0.06774 0.08651  318 ASP A OD2 
1045 N  N   . GLN A 319 ? 0.30857 0.33937 0.29720 -0.01480 -0.04716 0.06045  319 GLN A N   
1046 C  CA  . GLN A 319 ? 0.26027 0.29214 0.26346 -0.01000 -0.04719 0.06153  319 GLN A CA  
1047 C  C   . GLN A 319 ? 0.25195 0.27854 0.25831 -0.00695 -0.04001 0.05500  319 GLN A C   
1048 O  O   . GLN A 319 ? 0.25953 0.28873 0.26965 -0.00627 -0.03959 0.04977  319 GLN A O   
1049 C  CB  . GLN A 319 ? 0.27604 0.31637 0.28229 -0.01175 -0.05337 0.06002  319 GLN A CB  
1050 C  CG  . GLN A 319 ? 0.30859 0.35405 0.31123 -0.01487 -0.06140 0.06717  319 GLN A CG  
1051 C  CD  . GLN A 319 ? 0.32218 0.37616 0.32733 -0.01723 -0.06844 0.06557  319 GLN A CD  
1052 O  OE1 . GLN A 319 ? 0.34530 0.40172 0.35241 -0.01772 -0.06729 0.05779  319 GLN A OE1 
1053 N  NE2 . GLN A 319 ? 0.30607 0.36450 0.31182 -0.01877 -0.07610 0.07300  319 GLN A NE2 
1054 N  N   . PRO A 320 ? 0.27327 0.29226 0.27842 -0.00514 -0.03459 0.05551  320 PRO A N   
1055 C  CA  . PRO A 320 ? 0.24415 0.25782 0.25151 -0.00235 -0.02831 0.04967  320 PRO A CA  
1056 C  C   . PRO A 320 ? 0.26057 0.27358 0.28075 0.00269  -0.02645 0.05202  320 PRO A C   
1057 O  O   . PRO A 320 ? 0.28618 0.30031 0.31579 0.00515  -0.02827 0.05924  320 PRO A O   
1058 C  CB  . PRO A 320 ? 0.27572 0.28149 0.27860 -0.00221 -0.02379 0.05036  320 PRO A CB  
1059 C  CG  . PRO A 320 ? 0.30787 0.31381 0.31348 -0.00215 -0.02707 0.05996  320 PRO A CG  
1060 C  CD  . PRO A 320 ? 0.31547 0.33007 0.31711 -0.00581 -0.03415 0.06159  320 PRO A CD  
1061 N  N   . ALA A 321 ? 0.23702 0.24825 0.25777 0.00412  -0.02267 0.04593  321 ALA A N   
1062 C  CA  . ALA A 321 ? 0.22445 0.23292 0.25492 0.00881  -0.01845 0.04700  321 ALA A CA  
1063 C  C   . ALA A 321 ? 0.26585 0.26769 0.29023 0.00953  -0.01269 0.04042  321 ALA A C   
1064 O  O   . ALA A 321 ? 0.28276 0.28468 0.29843 0.00653  -0.01330 0.03463  321 ALA A O   
1065 C  CB  . ALA A 321 ? 0.26529 0.28039 0.30441 0.00967  -0.02107 0.04759  321 ALA A CB  
1066 N  N   . VAL A 322 ? 0.24104 0.23714 0.27015 0.01336  -0.00717 0.04116  322 VAL A N   
1067 C  CA  . VAL A 322 ? 0.25166 0.24080 0.27415 0.01398  -0.00196 0.03521  322 VAL A CA  
1068 C  C   . VAL A 322 ? 0.24434 0.23512 0.26800 0.01505  -0.00061 0.03206  322 VAL A C   
1069 O  O   . VAL A 322 ? 0.27314 0.26662 0.30602 0.01756  0.00030  0.03550  322 VAL A O   
1070 C  CB  . VAL A 322 ? 0.26176 0.24305 0.28753 0.01724  0.00378  0.03700  322 VAL A CB  
1071 C  CG1 . VAL A 322 ? 0.30751 0.28166 0.32607 0.01787  0.00900  0.03048  322 VAL A CG1 
1072 C  CG2 . VAL A 322 ? 0.35249 0.33169 0.37719 0.01585  0.00221  0.04050  322 VAL A CG2 
1073 N  N   . ILE A 323 ? 0.22511 0.21426 0.24032 0.01315  -0.00049 0.02593  323 ILE A N   
1074 C  CA  . ILE A 323 ? 0.23913 0.22794 0.25422 0.01430  0.00144  0.02333  323 ILE A CA  
1075 C  C   . ILE A 323 ? 0.27991 0.26018 0.28802 0.01557  0.00670  0.01973  323 ILE A C   
1076 O  O   . ILE A 323 ? 0.28225 0.25891 0.28248 0.01355  0.00623  0.01560  323 ILE A O   
1077 C  CB  . ILE A 323 ? 0.23322 0.22707 0.24559 0.01134  -0.00312 0.01963  323 ILE A CB  
1078 C  CG1 . ILE A 323 ? 0.30623 0.29862 0.31831 0.01265  -0.00094 0.01784  323 ILE A CG1 
1079 C  CG2 . ILE A 323 ? 0.31575 0.30870 0.31967 0.00778  -0.00552 0.01482  323 ILE A CG2 
1080 C  CD1 . ILE A 323 ? 0.43415 0.43222 0.44750 0.01022  -0.00568 0.01529  323 ILE A CD1 
1081 N  N   . LYS A 324 ? 0.23674 0.21378 0.24794 0.01873  0.01188  0.02111  324 LYS A N   
1082 C  CA  . LYS A 324 ? 0.22101 0.18972 0.22478 0.01989  0.01727  0.01742  324 LYS A CA  
1083 C  C   . LYS A 324 ? 0.27200 0.24086 0.27186 0.01998  0.01822  0.01553  324 LYS A C   
1084 O  O   . LYS A 324 ? 0.28672 0.25897 0.29359 0.02168  0.01983  0.01893  324 LYS A O   
1085 C  CB  . LYS A 324 ? 0.25780 0.22192 0.26750 0.02333  0.02349  0.02011  324 LYS A CB  
1086 C  CG  . LYS A 324 ? 0.25654 0.21165 0.25794 0.02446  0.02986  0.01551  324 LYS A CG  
1087 C  CD  . LYS A 324 ? 0.29058 0.24198 0.30007 0.02814  0.03682  0.01797  324 LYS A CD  
1088 C  CE  . LYS A 324 ? 0.50878 0.45053 0.50983 0.02900  0.04351  0.01270  324 LYS A CE  
1089 N  NZ  . LYS A 324 ? 0.50680 0.44581 0.51763 0.03289  0.05130  0.01494  324 LYS A NZ  
1090 N  N   . THR A 325 ? 0.24549 0.21117 0.23508 0.01794  0.01669  0.01061  325 THR A N   
1091 C  CA  . THR A 325 ? 0.25775 0.22311 0.24253 0.01767  0.01672  0.00928  325 THR A CA  
1092 C  C   . THR A 325 ? 0.28118 0.23806 0.25604 0.01862  0.02200  0.00629  325 THR A C   
1093 O  O   . THR A 325 ? 0.26802 0.21971 0.23607 0.01757  0.02204  0.00233  325 THR A O   
1094 C  CB  . THR A 325 ? 0.27298 0.24137 0.25421 0.01456  0.01024  0.00615  325 THR A CB  
1095 O  OG1 . THR A 325 ? 0.30242 0.27842 0.29198 0.01334  0.00578  0.00803  325 THR A OG1 
1096 C  CG2 . THR A 325 ? 0.27369 0.24178 0.25106 0.01434  0.00958  0.00584  325 THR A CG2 
1097 N  N   . THR A 326 ? 0.24797 0.20328 0.22171 0.02035  0.02668  0.00796  326 THR A N   
1098 C  CA  . THR A 326 ? 0.23444 0.18145 0.19733 0.02107  0.03245  0.00486  326 THR A CA  
1099 C  C   . THR A 326 ? 0.27508 0.22144 0.22960 0.02004  0.03176  0.00479  326 THR A C   
1100 O  O   . THR A 326 ? 0.28614 0.23746 0.24692 0.02054  0.03148  0.00889  326 THR A O   
1101 C  CB  . THR A 326 ? 0.32789 0.27218 0.29662 0.02437  0.04105  0.00696  326 THR A CB  
1102 O  OG1 . THR A 326 ? 0.32570 0.27125 0.30442 0.02553  0.04091  0.00848  326 THR A OG1 
1103 C  CG2 . THR A 326 ? 0.32394 0.25910 0.28067 0.02483  0.04761  0.00259  326 THR A CG2 
1104 N  N   . PHE A 327 ? 0.27729 0.21734 0.21793 0.01850  0.03142  0.00045  327 PHE A N   
1105 C  CA  . PHE A 327 ? 0.32599 0.26470 0.25693 0.01718  0.02986  0.00076  327 PHE A CA  
1106 C  C   . PHE A 327 ? 0.35543 0.28763 0.27612 0.01825  0.03789  0.00039  327 PHE A C   
1107 O  O   . PHE A 327 ? 0.32907 0.25451 0.24207 0.01850  0.04221  -0.00392 327 PHE A O   
1108 C  CB  . PHE A 327 ? 0.27293 0.20962 0.19503 0.01429  0.02265  -0.00352 327 PHE A CB  
1109 C  CG  . PHE A 327 ? 0.26540 0.20822 0.19726 0.01302  0.01584  -0.00394 327 PHE A CG  
1110 C  CD1 . PHE A 327 ? 0.32683 0.27702 0.26849 0.01285  0.01201  -0.00037 327 PHE A CD1 
1111 C  CD2 . PHE A 327 ? 0.31403 0.25516 0.24568 0.01190  0.01395  -0.00800 327 PHE A CD2 
1112 C  CE1 . PHE A 327 ? 0.31562 0.27138 0.26558 0.01148  0.00652  -0.00139 327 PHE A CE1 
1113 C  CE2 . PHE A 327 ? 0.34187 0.28872 0.28189 0.01049  0.00864  -0.00841 327 PHE A CE2 
1114 C  CZ  . PHE A 327 ? 0.26879 0.22302 0.21764 0.01030  0.00514  -0.00526 327 PHE A CZ  
1115 N  N   . ASN A 328 ? 0.32037 0.25442 0.24062 0.01858  0.03999  0.00469  328 ASN A N   
1116 C  CA  . ASN A 328 ? 0.27957 0.20761 0.18702 0.01872  0.04702  0.00465  328 ASN A CA  
1117 C  C   . ASN A 328 ? 0.33903 0.26305 0.24818 0.02122  0.05747  0.00312  328 ASN A C   
1118 O  O   . ASN A 328 ? 0.38444 0.30097 0.27984 0.02089  0.06332  -0.00058 328 ASN A O   
1119 C  CB  . ASN A 328 ? 0.39667 0.31828 0.28519 0.01596  0.04323  0.00044  328 ASN A CB  
1120 C  CG  . ASN A 328 ? 0.38669 0.31194 0.27395 0.01369  0.03351  0.00282  328 ASN A CG  
1121 O  OD1 . ASN A 328 ? 0.37300 0.30444 0.27085 0.01411  0.03137  0.00797  328 ASN A OD1 
1122 N  ND2 . ASN A 328 ? 0.34687 0.26829 0.22247 0.01126  0.02738  -0.00111 328 ASN A ND2 
1123 N  N   . GLN A 329 ? 0.30799 0.23686 0.23432 0.02371  0.05995  0.00582  329 GLN A N   
1124 C  CA  . GLN A 329 ? 0.32593 0.25131 0.25674 0.02643  0.06988  0.00476  329 GLN A CA  
1125 C  C   . GLN A 329 ? 0.41443 0.34403 0.35671 0.02866  0.07682  0.01022  329 GLN A C   
1126 O  O   . GLN A 329 ? 0.41374 0.34165 0.36369 0.03132  0.08539  0.01001  329 GLN A O   
1127 C  CB  . GLN A 329 ? 0.37637 0.30248 0.31812 0.02776  0.06818  0.00327  329 GLN A CB  
1128 C  CG  . GLN A 329 ? 0.46380 0.38291 0.39362 0.02598  0.06568  -0.00342 329 GLN A CG  
1129 C  CD  . GLN A 329 ? 0.63578 0.54554 0.55307 0.02627  0.07423  -0.00871 329 GLN A CD  
1130 O  OE1 . GLN A 329 ? 0.58468 0.48936 0.48454 0.02380  0.07304  -0.01251 329 GLN A OE1 
1131 N  NE2 . GLN A 329 ? 0.57056 0.47795 0.49687 0.02922  0.08287  -0.00907 329 GLN A NE2 
1132 N  N   . GLU A 330 ? 0.33386 0.26857 0.27826 0.02763  0.07377  0.01498  330 GLU A N   
1133 C  CA  . GLU A 330 ? 0.36053 0.29901 0.31537 0.02929  0.08064  0.02019  330 GLU A CA  
1134 C  C   . GLU A 330 ? 0.38016 0.31293 0.31932 0.02825  0.08804  0.01995  330 GLU A C   
1135 O  O   . GLU A 330 ? 0.46911 0.39711 0.39007 0.02566  0.08452  0.01754  330 GLU A O   
1136 C  CB  . GLU A 330 ? 0.36377 0.31114 0.33151 0.02861  0.07362  0.02582  330 GLU A CB  
1137 C  CG  . GLU A 330 ? 0.37516 0.32852 0.35652 0.02903  0.06578  0.02608  330 GLU A CG  
1138 C  CD  . GLU A 330 ? 0.45259 0.40782 0.44903 0.03211  0.07080  0.02718  330 GLU A CD  
1139 O  OE1 . GLU A 330 ? 0.44098 0.39675 0.44518 0.03412  0.07926  0.02982  330 GLU A OE1 
1140 O  OE2 . GLU A 330 ? 0.47401 0.43032 0.47540 0.03249  0.06634  0.02579  330 GLU A OE2 
1141 N  N   . THR A 331 ? 0.38695 0.32033 0.33330 0.03014  0.09831  0.02261  331 THR A N   
1142 C  CA  . THR A 331 ? 0.38636 0.31512 0.31829 0.02887  0.10611  0.02341  331 THR A CA  
1143 C  C   . THR A 331 ? 0.40623 0.34119 0.34612 0.02804  0.10484  0.03083  331 THR A C   
1144 O  O   . THR A 331 ? 0.48370 0.42649 0.44112 0.02862  0.09856  0.03470  331 THR A O   
1145 C  CB  . THR A 331 ? 0.46189 0.38620 0.39454 0.03109  0.12004  0.02083  331 THR A CB  
1146 O  OG1 . THR A 331 ? 0.56251 0.49367 0.52024 0.03424  0.12372  0.02463  331 THR A OG1 
1147 C  CG2 . THR A 331 ? 0.51978 0.43658 0.44255 0.03145  0.12139  0.01288  331 THR A CG2 
1148 N  N   . GLY A 332 ? 0.44407 0.37516 0.36998 0.02632  0.11059  0.03276  332 GLY A N   
1149 C  CA  . GLY A 332 ? 0.44527 0.38135 0.37791 0.02521  0.10967  0.04014  332 GLY A CA  
1150 C  C   . GLY A 332 ? 0.48558 0.42399 0.41499 0.02278  0.09669  0.04242  332 GLY A C   
1151 O  O   . GLY A 332 ? 0.52380 0.46798 0.46527 0.02225  0.09352  0.04827  332 GLY A O   
1152 N  N   . CYS A 333 ? 0.40697 0.34094 0.32125 0.02120  0.08927  0.03777  333 CYS A N   
1153 C  CA  . CYS A 333 ? 0.33490 0.27089 0.24701 0.01904  0.07677  0.03908  333 CYS A CA  
1154 C  C   . CYS A 333 ? 0.46353 0.39218 0.35347 0.01696  0.07235  0.03397  333 CYS A C   
1155 O  O   . CYS A 333 ? 0.48750 0.40989 0.36499 0.01722  0.07854  0.02891  333 CYS A O   
1156 C  CB  . CYS A 333 ? 0.39379 0.33712 0.32513 0.02017  0.06862  0.03832  333 CYS A CB  
1157 S  SG  . CYS A 333 ? 0.42898 0.37043 0.36157 0.02201  0.06893  0.03095  333 CYS A SG  
1158 N  N   . GLU A 334 ? 0.37589 0.30516 0.26124 0.01475  0.06172  0.03528  334 GLU A N   
1159 C  CA  . GLU A 334 ? 0.42749 0.35079 0.29456 0.01274  0.05589  0.03022  334 GLU A CA  
1160 C  C   . GLU A 334 ? 0.39875 0.32421 0.27346 0.01331  0.04894  0.02460  334 GLU A C   
1161 O  O   . GLU A 334 ? 0.38310 0.30332 0.24614 0.01259  0.04808  0.01850  334 GLU A O   
1162 C  CB  . GLU A 334 ? 0.41414 0.33644 0.27193 0.01000  0.04735  0.03416  334 GLU A CB  
1163 C  CG  . GLU A 334 ? 1.01012 0.92581 0.84717 0.00809  0.05239  0.03676  334 GLU A CG  
1164 C  CD  . GLU A 334 ? 0.78147 0.68924 0.59838 0.00730  0.05727  0.02995  334 GLU A CD  
1165 O  OE1 . GLU A 334 ? 0.61054 0.51452 0.41503 0.00540  0.04966  0.02557  334 GLU A OE1 
1166 O  OE2 . GLU A 334 ? 0.65883 0.56437 0.47402 0.00865  0.06899  0.02860  334 GLU A OE2 
1167 N  N   . TYR A 335 ? 0.32958 0.26258 0.22336 0.01426  0.04391  0.02654  335 TYR A N   
1168 C  CA  . TYR A 335 ? 0.35226 0.28818 0.25411 0.01444  0.03710  0.02201  335 TYR A CA  
1169 C  C   . TYR A 335 ? 0.34309 0.28593 0.26504 0.01663  0.03902  0.02363  335 TYR A C   
1170 O  O   . TYR A 335 ? 0.33314 0.28012 0.26542 0.01747  0.04202  0.02875  335 TYR A O   
1171 C  CB  . TYR A 335 ? 0.37710 0.31581 0.28081 0.01240  0.02569  0.02222  335 TYR A CB  
1172 C  CG  . TYR A 335 ? 0.38353 0.31670 0.26990 0.01004  0.02166  0.02244  335 TYR A CG  
1173 C  CD1 . TYR A 335 ? 0.36209 0.29013 0.23549 0.00866  0.01841  0.01673  335 TYR A CD1 
1174 C  CD2 . TYR A 335 ? 0.33059 0.26367 0.21397 0.00901  0.02066  0.02879  335 TYR A CD2 
1175 C  CE1 . TYR A 335 ? 0.46237 0.38542 0.31936 0.00626  0.01383  0.01712  335 TYR A CE1 
1176 C  CE2 . TYR A 335 ? 0.40156 0.32954 0.26863 0.00676  0.01638  0.02975  335 TYR A CE2 
1177 C  CZ  . TYR A 335 ? 0.37591 0.29903 0.22958 0.00537  0.01269  0.02388  335 TYR A CZ  
1178 O  OH  . TYR A 335 ? 0.45786 0.37622 0.29535 0.00288  0.00724  0.02516  335 TYR A OH  
1179 N  N   . SER A 336 ? 0.31661 0.26098 0.24457 0.01727  0.03656  0.01954  336 SER A N   
1180 C  CA  . SER A 336 ? 0.29434 0.24573 0.24082 0.01894  0.03672  0.02157  336 SER A CA  
1181 C  C   . SER A 336 ? 0.30691 0.26060 0.25795 0.01839  0.03044  0.01764  336 SER A C   
1182 O  O   . SER A 336 ? 0.30741 0.25636 0.24845 0.01746  0.02885  0.01293  336 SER A O   
1183 C  CB  . SER A 336 ? 0.37827 0.32875 0.33010 0.02161  0.04656  0.02279  336 SER A CB  
1184 O  OG  . SER A 336 ? 0.35478 0.29880 0.29757 0.02229  0.05059  0.01780  336 SER A OG  
1185 N  N   . ILE A 337 ? 0.27598 0.23703 0.24192 0.01863  0.02678  0.01960  337 ILE A N   
1186 C  CA  . ILE A 337 ? 0.27590 0.23996 0.24769 0.01825  0.02234  0.01682  337 ILE A CA  
1187 C  C   . ILE A 337 ? 0.29333 0.26222 0.27910 0.02026  0.02539  0.02013  337 ILE A C   
1188 O  O   . ILE A 337 ? 0.28500 0.25924 0.28114 0.02060  0.02510  0.02412  337 ILE A O   
1189 C  CB  . ILE A 337 ? 0.24165 0.21049 0.21724 0.01590  0.01360  0.01553  337 ILE A CB  
1190 C  CG1 . ILE A 337 ? 0.29080 0.25530 0.25464 0.01403  0.00986  0.01277  337 ILE A CG1 
1191 C  CG2 . ILE A 337 ? 0.29002 0.26229 0.27131 0.01528  0.01013  0.01294  337 ILE A CG2 
1192 C  CD1 . ILE A 337 ? 0.35765 0.32692 0.32743 0.01199  0.00189  0.01215  337 ILE A CD1 
1193 N  N   . THR A 338 ? 0.27533 0.24229 0.26237 0.02162  0.02824  0.01886  338 THR A N   
1194 C  CA  A THR A 338 ? 0.25794 0.22925 0.25885 0.02370  0.03062  0.02245  338 THR A CA  
1195 C  CA  B THR A 338 ? 0.24640 0.21825 0.24777 0.02355  0.03009  0.02258  338 THR A CA  
1196 C  C   . THR A 338 ? 0.29409 0.26881 0.29947 0.02269  0.02487  0.02143  338 THR A C   
1197 O  O   . THR A 338 ? 0.31990 0.29028 0.31718 0.02181  0.02395  0.01768  338 THR A O   
1198 C  CB  A THR A 338 ? 0.36362 0.32922 0.36324 0.02640  0.03959  0.02250  338 THR A CB  
1199 C  CB  B THR A 338 ? 0.29816 0.26574 0.30109 0.02647  0.03909  0.02373  338 THR A CB  
1200 O  OG1 A THR A 338 ? 0.35965 0.32210 0.35362 0.02693  0.04557  0.02337  338 THR A OG1 
1201 O  OG1 B THR A 338 ? 0.24223 0.20355 0.23771 0.02677  0.04086  0.01980  338 THR A OG1 
1202 C  CG2 A THR A 338 ? 0.33684 0.30655 0.35200 0.02881  0.04183  0.02639  338 THR A CG2 
1203 C  CG2 B THR A 338 ? 0.26428 0.22806 0.25992 0.02681  0.04505  0.02424  338 THR A CG2 
1204 N  N   . PHE A 339 ? 0.24918 0.23144 0.26688 0.02255  0.02110  0.02471  339 PHE A N   
1205 C  CA  . PHE A 339 ? 0.23432 0.22015 0.25576 0.02141  0.01601  0.02456  339 PHE A CA  
1206 C  C   . PHE A 339 ? 0.34165 0.32942 0.37437 0.02392  0.01868  0.02908  339 PHE A C   
1207 O  O   . PHE A 339 ? 0.32209 0.31483 0.36618 0.02511  0.01925  0.03311  339 PHE A O   
1208 C  CB  . PHE A 339 ? 0.22543 0.21857 0.25132 0.01877  0.00868  0.02436  339 PHE A CB  
1209 C  CG  . PHE A 339 ? 0.26126 0.25330 0.27931 0.01646  0.00555  0.02029  339 PHE A CG  
1210 C  CD1 . PHE A 339 ? 0.25161 0.24053 0.26046 0.01462  0.00327  0.01572  339 PHE A CD1 
1211 C  CD2 . PHE A 339 ? 0.28238 0.27640 0.30333 0.01613  0.00487  0.02128  339 PHE A CD2 
1212 C  CE1 . PHE A 339 ? 0.26674 0.25491 0.27013 0.01262  0.00001  0.01207  339 PHE A CE1 
1213 C  CE2 . PHE A 339 ? 0.30625 0.29922 0.32143 0.01414  0.00144  0.01800  339 PHE A CE2 
1214 C  CZ  . PHE A 339 ? 0.27937 0.26956 0.28611 0.01249  -0.00109 0.01336  339 PHE A CZ  
1215 N  N   . ASN A 340 ? 0.23405 0.21807 0.26504 0.02470  0.02003  0.02872  340 ASN A N   
1216 C  CA  . ASN A 340 ? 0.23401 0.22021 0.27711 0.02700  0.02126  0.03360  340 ASN A CA  
1217 C  C   . ASN A 340 ? 0.28131 0.27165 0.32562 0.02486  0.01422  0.03488  340 ASN A C   
1218 O  O   . ASN A 340 ? 0.26938 0.25619 0.30437 0.02304  0.01272  0.03170  340 ASN A O   
1219 C  CB  . ASN A 340 ? 0.22365 0.20214 0.26607 0.02985  0.02871  0.03313  340 ASN A CB  
1220 C  CG  . ASN A 340 ? 0.45914 0.43977 0.51557 0.03230  0.02925  0.03851  340 ASN A CG  
1221 O  OD1 . ASN A 340 ? 0.40199 0.38101 0.45816 0.03190  0.02687  0.03940  340 ASN A OD1 
1222 N  ND2 . ASN A 340 ? 0.43148 0.41610 0.50128 0.03473  0.03204  0.04265  340 ASN A ND2 
1223 N  N   . PHE A 341 ? 0.22688 0.22463 0.28238 0.02483  0.00998  0.03952  341 PHE A N   
1224 C  CA  . PHE A 341 ? 0.24836 0.25059 0.30434 0.02248  0.00304  0.04137  341 PHE A CA  
1225 C  C   . PHE A 341 ? 0.29219 0.29415 0.35817 0.02505  0.00399  0.04723  341 PHE A C   
1226 O  O   . PHE A 341 ? 0.27709 0.28091 0.35561 0.02800  0.00678  0.05108  341 PHE A O   
1227 C  CB  . PHE A 341 ? 0.26435 0.27532 0.32514 0.02009  -0.00349 0.04213  341 PHE A CB  
1228 C  CG  . PHE A 341 ? 0.30156 0.31297 0.35456 0.01760  -0.00486 0.03661  341 PHE A CG  
1229 C  CD1 . PHE A 341 ? 0.28370 0.29378 0.33815 0.01886  -0.00109 0.03546  341 PHE A CD1 
1230 C  CD2 . PHE A 341 ? 0.28741 0.30051 0.33215 0.01394  -0.00972 0.03277  341 PHE A CD2 
1231 C  CE1 . PHE A 341 ? 0.26855 0.27887 0.31692 0.01664  -0.00295 0.03105  341 PHE A CE1 
1232 C  CE2 . PHE A 341 ? 0.26641 0.27998 0.30604 0.01184  -0.01105 0.02757  341 PHE A CE2 
1233 C  CZ  . PHE A 341 ? 0.31199 0.32398 0.35371 0.01333  -0.00795 0.02705  341 PHE A CZ  
1234 N  N   . SER A 342 ? 0.22336 0.22291 0.28489 0.02399  0.00196  0.04819  342 SER A N   
1235 C  CA  . SER A 342 ? 0.21333 0.21228 0.28518 0.02647  0.00233  0.05445  342 SER A CA  
1236 C  C   . SER A 342 ? 0.28733 0.28779 0.35415 0.02353  -0.00385 0.05694  342 SER A C   
1237 O  O   . SER A 342 ? 0.28829 0.28849 0.34273 0.01992  -0.00630 0.05273  342 SER A O   
1238 C  CB  . SER A 342 ? 0.31519 0.30508 0.38798 0.02985  0.01071  0.05326  342 SER A CB  
1239 O  OG  . SER A 342 ? 0.31351 0.29692 0.37319 0.02793  0.01188  0.04865  342 SER A OG  
1240 N  N   . TRP A 343 ? 0.28744 0.28956 0.36427 0.02501  -0.00632 0.06411  343 TRP A N   
1241 C  CA  . TRP A 343 ? 0.27393 0.27698 0.34531 0.02213  -0.01200 0.06758  343 TRP A CA  
1242 C  C   . TRP A 343 ? 0.36763 0.36769 0.45023 0.02521  -0.01123 0.07504  343 TRP A C   
1243 O  O   . TRP A 343 ? 0.34100 0.34126 0.43823 0.02930  -0.00827 0.07827  343 TRP A O   
1244 C  CB  . TRP A 343 ? 0.30380 0.31616 0.37377 0.01856  -0.02069 0.06953  343 TRP A CB  
1245 C  CG  . TRP A 343 ? 0.30539 0.32421 0.39050 0.02067  -0.02362 0.07447  343 TRP A CG  
1246 C  CD1 . TRP A 343 ? 0.33177 0.35466 0.42778 0.02156  -0.02896 0.08281  343 TRP A CD1 
1247 C  CD2 . TRP A 343 ? 0.30727 0.32956 0.39970 0.02209  -0.02165 0.07187  343 TRP A CD2 
1248 N  NE1 . TRP A 343 ? 0.32505 0.35406 0.43562 0.02350  -0.03046 0.08514  343 TRP A NE1 
1249 C  CE2 . TRP A 343 ? 0.34602 0.37468 0.45464 0.02380  -0.02567 0.07853  343 TRP A CE2 
1250 C  CE3 . TRP A 343 ? 0.33070 0.35121 0.41812 0.02206  -0.01694 0.06503  343 TRP A CE3 
1251 C  CZ2 . TRP A 343 ? 0.31630 0.34970 0.43654 0.02531  -0.02463 0.07821  343 TRP A CZ2 
1252 C  CZ3 . TRP A 343 ? 0.34946 0.37426 0.44731 0.02354  -0.01592 0.06516  343 TRP A CZ3 
1253 C  CH2 . TRP A 343 ? 0.38920 0.42041 0.50353 0.02510  -0.01945 0.07155  343 TRP A CH2 
1254 N  N   . SER A 344 ? 0.40281 0.40007 0.47938 0.02323  -0.01366 0.07795  344 SER A N   
1255 C  CA  . SER A 344 ? 0.32479 0.31818 0.41205 0.02605  -0.01299 0.08533  344 SER A CA  
1256 C  C   . SER A 344 ? 0.45331 0.45215 0.54248 0.02389  -0.02193 0.09410  344 SER A C   
1257 O  O   . SER A 344 ? 0.49442 0.49166 0.59583 0.02658  -0.02292 0.10192  344 SER A O   
1258 C  CB  . SER A 344 ? 0.40727 0.39043 0.48814 0.02628  -0.00693 0.08231  344 SER A CB  
1259 O  OG  . SER A 344 ? 0.44719 0.42958 0.51146 0.02152  -0.00864 0.07800  344 SER A OG  
1260 N  N   . LYS A 345 ? 0.36433 0.36955 0.44217 0.01912  -0.02850 0.09306  345 LYS A N   
1261 C  CA  . LYS A 345 ? 0.34670 0.35789 0.42425 0.01644  -0.03768 0.10103  345 LYS A CA  
1262 C  C   . LYS A 345 ? 0.62480 0.64409 0.71715 0.01831  -0.04324 0.10604  345 LYS A C   
1263 O  O   . LYS A 345 ? 0.37983 0.40198 0.47930 0.02024  -0.04077 0.10191  345 LYS A O   
1264 C  CB  . LYS A 345 ? 0.41957 0.43448 0.47871 0.01031  -0.04193 0.09692  345 LYS A CB  
1265 C  CG  . LYS A 345 ? 0.39745 0.40534 0.44305 0.00782  -0.03760 0.09353  345 LYS A CG  
1266 C  CD  . LYS A 345 ? 0.55054 0.56303 0.57948 0.00160  -0.04197 0.09048  345 LYS A CD  
1267 C  CE  . LYS A 345 ? 0.74220 0.74896 0.75944 -0.00145 -0.03935 0.09054  345 LYS A CE  
1268 N  NZ  . LYS A 345 ? 0.51497 0.52694 0.51675 -0.00765 -0.04351 0.08831  345 LYS A NZ  
1269 N  N   . THR A 346 ? 0.42127 0.44448 0.51820 0.01739  -0.05126 0.11541  346 THR A N   
1270 C  CA  . THR A 346 ? 0.37015 0.40189 0.48136 0.01849  -0.05830 0.12091  346 THR A CA  
1271 C  C   . THR A 346 ? 0.45062 0.49045 0.54941 0.01290  -0.06598 0.11784  346 THR A C   
1272 O  O   . THR A 346 ? 0.59949 0.64200 0.68786 0.00867  -0.07338 0.12214  346 THR A O   
1273 C  CB  . THR A 346 ? 0.35255 0.38461 0.47587 0.02031  -0.06399 0.13292  346 THR A CB  
1274 O  OG1 . THR A 346 ? 0.55958 0.58284 0.69309 0.02515  -0.05592 0.13461  346 THR A OG1 
1275 C  CG2 . THR A 346 ? 0.47658 0.51733 0.61846 0.02225  -0.07048 0.13822  346 THR A CG2 
1276 N  N   . TYR A 347 ? 0.37055 0.41401 0.47009 0.01266  -0.06406 0.11032  347 TYR A N   
1277 C  CA  . TYR A 347 ? 0.36254 0.41333 0.45201 0.00755  -0.07057 0.10609  347 TYR A CA  
1278 C  C   . TYR A 347 ? 0.47626 0.53605 0.57993 0.00768  -0.07925 0.11166  347 TYR A C   
1279 O  O   . TYR A 347 ? 0.47753 0.53853 0.60067 0.01227  -0.07748 0.11504  347 TYR A O   
1280 C  CB  . TYR A 347 ? 0.35013 0.40008 0.43379 0.00694  -0.06455 0.09519  347 TYR A CB  
1281 C  CG  . TYR A 347 ? 0.34891 0.39123 0.41709 0.00570  -0.05768 0.08898  347 TYR A CG  
1282 C  CD1 . TYR A 347 ? 0.34198 0.38278 0.39468 0.00152  -0.06016 0.08971  347 TYR A CD1 
1283 C  CD2 . TYR A 347 ? 0.30195 0.33871 0.37095 0.00847  -0.04885 0.08254  347 TYR A CD2 
1284 C  CE1 . TYR A 347 ? 0.30398 0.33810 0.34434 0.00031  -0.05385 0.08419  347 TYR A CE1 
1285 C  CE2 . TYR A 347 ? 0.29830 0.32836 0.35414 0.00720  -0.04334 0.07693  347 TYR A CE2 
1286 C  CZ  . TYR A 347 ? 0.25892 0.28779 0.30148 0.00323  -0.04578 0.07772  347 TYR A CZ  
1287 O  OH  . TYR A 347 ? 0.29325 0.31588 0.32475 0.00194  -0.04033 0.07234  347 TYR A OH  
1288 N  N   . GLU A 348 ? 0.43144 0.65044 0.47601 -0.08890 -0.07723 0.13624  348 GLU A N   
1289 C  CA  . GLU A 348 ? 0.47844 0.70622 0.51514 -0.09832 -0.08247 0.13699  348 GLU A CA  
1290 C  C   . GLU A 348 ? 0.33205 0.55862 0.35396 -0.10846 -0.08597 0.13215  348 GLU A C   
1291 O  O   . GLU A 348 ? 0.58696 0.81510 0.59767 -0.11333 -0.08730 0.13107  348 GLU A O   
1292 C  CB  . GLU A 348 ? 0.43475 0.67305 0.46881 -0.10085 -0.08475 0.14177  348 GLU A CB  
1293 C  CG  . GLU A 348 ? 0.58616 0.83339 0.61216 -0.11037 -0.09013 0.14233  348 GLU A CG  
1294 C  CD  . GLU A 348 ? 0.74353 1.00060 0.76679 -0.11269 -0.09288 0.14702  348 GLU A CD  
1295 O  OE1 . GLU A 348 ? 0.91912 1.17807 0.93361 -0.11599 -0.09363 0.14753  348 GLU A OE1 
1296 O  OE2 . GLU A 348 ? 0.92074 1.18319 0.95000 -0.11115 -0.09443 0.14987  348 GLU A OE2 
1297 N  N   . ASN A 349 ? 0.40456 0.62703 0.42496 -0.11189 -0.08717 0.12844  349 ASN A N   
1298 C  CA  . ASN A 349 ? 0.39036 0.60900 0.39544 -0.12215 -0.09010 0.12236  349 ASN A CA  
1299 C  C   . ASN A 349 ? 0.49432 0.70379 0.49367 -0.12086 -0.08860 0.11801  349 ASN A C   
1300 O  O   . ASN A 349 ? 0.46887 0.67728 0.45206 -0.12857 -0.09041 0.11426  349 ASN A O   
1301 C  CB  . ASN A 349 ? 0.53156 0.75886 0.52250 -0.13330 -0.09418 0.12248  349 ASN A CB  
1302 C  CG  . ASN A 349 ? 0.83026 1.06629 0.82612 -0.13518 -0.09632 0.12577  349 ASN A CG  
1303 O  OD1 . ASN A 349 ? 0.76361 0.99729 0.76890 -0.13109 -0.09525 0.12562  349 ASN A OD1 
1304 N  ND2 . ASN A 349 ? 0.83915 1.08495 0.82817 -0.14125 -0.09941 0.12842  349 ASN A ND2 
1305 N  N   . VAL A 350 ? 0.37166 0.57326 0.38340 -0.11086 -0.08500 0.11781  350 VAL A N   
1306 C  CA  . VAL A 350 ? 0.33938 0.53178 0.34791 -0.10813 -0.08365 0.11352  350 VAL A CA  
1307 C  C   . VAL A 350 ? 0.42659 0.60734 0.43332 -0.11009 -0.08435 0.10699  350 VAL A C   
1308 O  O   . VAL A 350 ? 0.37787 0.55505 0.39677 -0.10452 -0.08253 0.10797  350 VAL A O   
1309 C  CB  . VAL A 350 ? 0.30646 0.49734 0.33022 -0.09504 -0.07869 0.11754  350 VAL A CB  
1310 C  CG1 . VAL A 350 ? 0.29717 0.47802 0.31913 -0.09136 -0.07751 0.11272  350 VAL A CG1 
1311 C  CG2 . VAL A 350 ? 0.32793 0.52882 0.35080 -0.09438 -0.07811 0.12292  350 VAL A CG2 
1312 N  N   . GLU A 351 ? 0.37189 0.54485 0.36154 -0.11833 -0.08665 0.09938  351 GLU A N   
1313 C  CA  . GLU A 351 ? 0.34883 0.50786 0.33436 -0.12136 -0.08737 0.09160  351 GLU A CA  
1314 C  C   . GLU A 351 ? 0.28625 0.43644 0.28566 -0.11038 -0.08478 0.09090  351 GLU A C   
1315 O  O   . GLU A 351 ? 0.30130 0.44922 0.30203 -0.10380 -0.08191 0.09098  351 GLU A O   
1316 C  CB  . GLU A 351 ? 0.35200 0.50103 0.31240 -0.13330 -0.08943 0.08173  351 GLU A CB  
1317 C  CG  . GLU A 351 ? 0.40670 0.53977 0.35954 -0.13898 -0.08986 0.07291  351 GLU A CG  
1318 C  CD  . GLU A 351 ? 0.72783 0.84418 0.65458 -0.14772 -0.08759 0.06147  351 GLU A CD  
1319 O  OE1 . GLU A 351 ? 0.65971 0.78004 0.57438 -0.15079 -0.08676 0.06109  351 GLU A OE1 
1320 O  OE2 . GLU A 351 ? 0.71911 0.81709 0.63730 -0.15089 -0.08615 0.05265  351 GLU A OE2 
1321 N  N   . PHE A 352 ? 0.28122 0.42346 0.29048 -0.10693 -0.08371 0.08942  352 PHE A N   
1322 C  CA  . PHE A 352 ? 0.33236 0.46544 0.35659 -0.09569 -0.08069 0.08901  352 PHE A CA  
1323 C  C   . PHE A 352 ? 0.33710 0.44486 0.34744 -0.09634 -0.07648 0.07638  352 PHE A C   
1324 O  O   . PHE A 352 ? 0.33080 0.42464 0.33929 -0.09832 -0.07637 0.07057  352 PHE A O   
1325 C  CB  . PHE A 352 ? 0.25300 0.38313 0.29221 -0.08806 -0.07751 0.09198  352 PHE A CB  
1326 C  CG  . PHE A 352 ? 0.22077 0.34481 0.27722 -0.07322 -0.07191 0.09443  352 PHE A CG  
1327 C  CD1 . PHE A 352 ? 0.24582 0.35655 0.30645 -0.06921 -0.07140 0.08931  352 PHE A CD1 
1328 C  CD2 . PHE A 352 ? 0.30687 0.43601 0.37356 -0.06402 -0.06657 0.10045  352 PHE A CD2 
1329 C  CE1 . PHE A 352 ? 0.24333 0.34682 0.31861 -0.05499 -0.06511 0.09076  352 PHE A CE1 
1330 C  CE2 . PHE A 352 ? 0.25637 0.37610 0.33485 -0.05143 -0.05965 0.10028  352 PHE A CE2 
1331 C  CZ  . PHE A 352 ? 0.24836 0.35562 0.33096 -0.04660 -0.05850 0.09558  352 PHE A CZ  
1332 N  N   . GLU A 353 ? 0.24982 0.34861 0.24995 -0.09279 -0.07117 0.07132  353 GLU A N   
1333 C  CA  . GLU A 353 ? 0.30296 0.37534 0.29101 -0.08962 -0.06489 0.05863  353 GLU A CA  
1334 C  C   . GLU A 353 ? 0.28189 0.35099 0.27582 -0.07792 -0.05844 0.05823  353 GLU A C   
1335 O  O   . GLU A 353 ? 0.31738 0.39995 0.30978 -0.07844 -0.05834 0.06315  353 GLU A O   
1336 C  CB  . GLU A 353 ? 0.38828 0.45057 0.35009 -0.10204 -0.06559 0.04913  353 GLU A CB  
1337 C  CG  . GLU A 353 ? 0.45829 0.53460 0.40826 -0.10917 -0.06714 0.05186  353 GLU A CG  
1338 C  CD  . GLU A 353 ? 0.50298 0.56615 0.44051 -0.10533 -0.06035 0.04345  353 GLU A CD  
1339 O  OE1 . GLU A 353 ? 0.46244 0.53586 0.39196 -0.10877 -0.06011 0.04564  353 GLU A OE1 
1340 O  OE2 . GLU A 353 ? 0.47742 0.51954 0.41310 -0.09874 -0.05520 0.03424  353 GLU A OE2 
1341 N  N   . THR A 354 ? 0.25544 0.30816 0.25795 -0.06709 -0.05344 0.05343  354 THR A N   
1342 C  CA  . THR A 354 ? 0.25925 0.31334 0.27587 -0.05399 -0.04820 0.05629  354 THR A CA  
1343 C  C   . THR A 354 ? 0.27912 0.31390 0.28435 -0.04901 -0.04098 0.04445  354 THR A C   
1344 O  O   . THR A 354 ? 0.28051 0.29584 0.27038 -0.05262 -0.03960 0.03313  354 THR A O   
1345 C  CB  . THR A 354 ? 0.26105 0.31367 0.30024 -0.04329 -0.04773 0.06110  354 THR A CB  
1346 O  OG1 . THR A 354 ? 0.27387 0.30187 0.30941 -0.03899 -0.04420 0.05059  354 THR A OG1 
1347 C  CG2 . THR A 354 ? 0.31629 0.38478 0.36609 -0.04865 -0.05483 0.07055  354 THR A CG2 
1348 N  N   . THR A 355 ? 0.23561 0.27576 0.24925 -0.04016 -0.03635 0.04707  355 THR A N   
1349 C  CA  . THR A 355 ? 0.19157 0.21400 0.20147 -0.03175 -0.02882 0.03649  355 THR A CA  
1350 C  C   . THR A 355 ? 0.25171 0.25854 0.27444 -0.02156 -0.02678 0.03311  355 THR A C   
1351 O  O   . THR A 355 ? 0.23217 0.24222 0.26609 -0.02152 -0.03092 0.03911  355 THR A O   
1352 C  CB  . THR A 355 ? 0.22557 0.25925 0.24202 -0.02540 -0.02442 0.04072  355 THR A CB  
1353 O  OG1 . THR A 355 ? 0.24064 0.28869 0.27955 -0.01787 -0.02590 0.05296  355 THR A OG1 
1354 C  CG2 . THR A 355 ? 0.22585 0.27279 0.22714 -0.03613 -0.02641 0.04315  355 THR A CG2 
1355 N  N   . SER A 356 ? 0.23157 0.22063 0.25167 -0.01332 -0.02047 0.02267  356 SER A N   
1356 C  CA  . SER A 356 ? 0.22462 0.19549 0.25386 -0.00383 -0.01845 0.01751  356 SER A CA  
1357 C  C   . SER A 356 ? 0.24762 0.22432 0.29869 0.00971  -0.01450 0.02318  356 SER A C   
1358 O  O   . SER A 356 ? 0.24673 0.23457 0.30133 0.01298  -0.01110 0.02614  356 SER A O   
1359 C  CB  . SER A 356 ? 0.29808 0.24367 0.31089 -0.00250 -0.01453 0.00153  356 SER A CB  
1360 O  OG  . SER A 356 ? 0.31997 0.25689 0.31321 -0.01456 -0.01861 -0.00396 356 SER A OG  
1361 N  N   . PHE A 357 ? 0.25651 0.22457 0.31139 0.04227  -0.06387 -0.01688 357 PHE A N   
1362 C  CA  . PHE A 357 ? 0.21491 0.19200 0.26906 0.04326  -0.05755 -0.01870 357 PHE A CA  
1363 C  C   . PHE A 357 ? 0.25243 0.22500 0.29400 0.04332  -0.05643 -0.01755 357 PHE A C   
1364 O  O   . PHE A 357 ? 0.27262 0.23806 0.31095 0.03944  -0.05688 -0.01452 357 PHE A O   
1365 C  CB  . PHE A 357 ? 0.21388 0.19999 0.28123 0.03789  -0.05003 -0.01825 357 PHE A CB  
1366 C  CG  . PHE A 357 ? 0.22616 0.22154 0.29325 0.03816  -0.04295 -0.01996 357 PHE A CG  
1367 C  CD1 . PHE A 357 ? 0.33092 0.33288 0.39694 0.04350  -0.04274 -0.02329 357 PHE A CD1 
1368 C  CD2 . PHE A 357 ? 0.22535 0.22293 0.29327 0.03287  -0.03634 -0.01827 357 PHE A CD2 
1369 C  CE1 . PHE A 357 ? 0.29414 0.30478 0.36005 0.04380  -0.03618 -0.02502 357 PHE A CE1 
1370 C  CE2 . PHE A 357 ? 0.24143 0.24776 0.30914 0.03301  -0.02968 -0.02000 357 PHE A CE2 
1371 C  CZ  . PHE A 357 ? 0.26716 0.28013 0.33396 0.03858  -0.02960 -0.02344 357 PHE A CZ  
1372 N  N   . THR A 358 ? 0.20822 0.18489 0.24269 0.04769  -0.05505 -0.01993 358 THR A N   
1373 C  CA  . THR A 358 ? 0.20483 0.17836 0.22726 0.04825  -0.05377 -0.01919 358 THR A CA  
1374 C  C   . THR A 358 ? 0.28626 0.26968 0.31104 0.04657  -0.04561 -0.02026 358 THR A C   
1375 O  O   . THR A 358 ? 0.24632 0.23898 0.27748 0.04857  -0.04265 -0.02303 358 THR A O   
1376 C  CB  . THR A 358 ? 0.31322 0.28259 0.32418 0.05522  -0.05956 -0.02125 358 THR A CB  
1377 O  OG1 . THR A 358 ? 0.32606 0.28540 0.33410 0.05635  -0.06708 -0.02005 358 THR A OG1 
1378 C  CG2 . THR A 358 ? 0.28806 0.25544 0.28674 0.05647  -0.05807 -0.02093 358 THR A CG2 
1379 N  N   . PHE A 359 ? 0.23392 0.21531 0.25332 0.04293  -0.04205 -0.01809 359 PHE A N   
1380 C  CA  . PHE A 359 ? 0.21886 0.20895 0.23876 0.04134  -0.03443 -0.01909 359 PHE A CA  
1381 C  C   . PHE A 359 ? 0.25602 0.24044 0.26290 0.04081  -0.03428 -0.01727 359 PHE A C   
1382 O  O   . PHE A 359 ? 0.24897 0.22314 0.24737 0.04179  -0.04002 -0.01533 359 PHE A O   
1383 C  CB  . PHE A 359 ? 0.24394 0.24091 0.27714 0.03494  -0.02764 -0.01819 359 PHE A CB  
1384 C  CG  . PHE A 359 ? 0.25512 0.24520 0.28980 0.02871  -0.02754 -0.01432 359 PHE A CG  
1385 C  CD1 . PHE A 359 ? 0.26093 0.24517 0.30123 0.02728  -0.03216 -0.01277 359 PHE A CD1 
1386 C  CD2 . PHE A 359 ? 0.23352 0.22311 0.26384 0.02425  -0.02273 -0.01229 359 PHE A CD2 
1387 C  CE1 . PHE A 359 ? 0.26633 0.24431 0.30816 0.02158  -0.03201 -0.00930 359 PHE A CE1 
1388 C  CE2 . PHE A 359 ? 0.27789 0.26105 0.30930 0.01836  -0.02248 -0.00866 359 PHE A CE2 
1389 C  CZ  . PHE A 359 ? 0.25212 0.22949 0.28944 0.01696  -0.02700 -0.00716 359 PHE A CZ  
1390 N  N   . SER A 360 ? 0.25002 0.24115 0.25509 0.03942  -0.02782 -0.01797 360 SER A N   
1391 C  CA  . SER A 360 ? 0.24427 0.23035 0.23781 0.03790  -0.02706 -0.01581 360 SER A CA  
1392 C  C   . SER A 360 ? 0.23525 0.22833 0.23328 0.03206  -0.01850 -0.01503 360 SER A C   
1393 O  O   . SER A 360 ? 0.25193 0.25441 0.26130 0.03007  -0.01311 -0.01670 360 SER A O   
1394 C  CB  . SER A 360 ? 0.31363 0.29891 0.29494 0.04410  -0.02966 -0.01781 360 SER A CB  
1395 O  OG  . SER A 360 ? 0.27901 0.27524 0.26259 0.04554  -0.02383 -0.02086 360 SER A OG  
1396 N  N   . TYR A 361 ? 0.22956 0.21786 0.21865 0.02918  -0.01731 -0.01242 361 TYR A N   
1397 C  CA  . TYR A 361 ? 0.22427 0.21919 0.21555 0.02395  -0.00913 -0.01187 361 TYR A CA  
1398 C  C   . TYR A 361 ? 0.25652 0.24709 0.23368 0.02397  -0.00904 -0.01025 361 TYR A C   
1399 O  O   . TYR A 361 ? 0.27705 0.25841 0.24360 0.02711  -0.01538 -0.00890 361 TYR A O   
1400 C  CB  . TYR A 361 ? 0.25833 0.25301 0.25942 0.01656  -0.00557 -0.00930 361 TYR A CB  
1401 C  CG  . TYR A 361 ? 0.26630 0.24896 0.26254 0.01381  -0.01038 -0.00525 361 TYR A CG  
1402 C  CD1 . TYR A 361 ? 0.26594 0.24343 0.25326 0.00997  -0.00885 -0.00210 361 TYR A CD1 
1403 C  CD2 . TYR A 361 ? 0.27004 0.24656 0.27068 0.01494  -0.01643 -0.00454 361 TYR A CD2 
1404 C  CE1 . TYR A 361 ? 0.25529 0.22174 0.23868 0.00730  -0.01319 0.00170  361 TYR A CE1 
1405 C  CE2 . TYR A 361 ? 0.27202 0.23738 0.26859 0.01236  -0.02090 -0.00087 361 TYR A CE2 
1406 C  CZ  . TYR A 361 ? 0.28422 0.24465 0.27227 0.00856  -0.01917 0.00225  361 TYR A CZ  
1407 O  OH  . TYR A 361 ? 0.27729 0.22688 0.26189 0.00594  -0.02345 0.00588  361 TYR A OH  
1408 N  N   . ILE A 362 ? 0.27947 0.27730 0.25671 0.02070  -0.00172 -0.01065 362 ILE A N   
1409 C  CA  . ILE A 362 ? 0.28730 0.28272 0.25169 0.02048  -0.00067 -0.00938 362 ILE A CA  
1410 C  C   . ILE A 362 ? 0.26115 0.24799 0.22143 0.01471  -0.00113 -0.00476 362 ILE A C   
1411 O  O   . ILE A 362 ? 0.28523 0.27375 0.25436 0.00857  0.00298  -0.00321 362 ILE A O   
1412 C  CB  . ILE A 362 ? 0.29876 0.30571 0.26528 0.01902  0.00753  -0.01177 362 ILE A CB  
1413 C  CG1 . ILE A 362 ? 0.27868 0.29409 0.24971 0.02485  0.00789  -0.01638 362 ILE A CG1 
1414 C  CG2 . ILE A 362 ? 0.35382 0.35816 0.30679 0.01845  0.00858  -0.01025 362 ILE A CG2 
1415 C  CD1 . ILE A 362 ? 0.31152 0.33989 0.28895 0.02264  0.01690  -0.01910 362 ILE A CD1 
1416 N  N   . ALA A 363 ? 0.30493 0.28226 0.25198 0.01673  -0.00638 -0.00251 363 ALA A N   
1417 C  CA  . ALA A 363 ? 0.33475 0.30246 0.27671 0.01201  -0.00809 0.00209  363 ALA A CA  
1418 C  C   . ALA A 363 ? 0.35458 0.32529 0.29176 0.00682  -0.00159 0.00380  363 ALA A C   
1419 O  O   . ALA A 363 ? 0.34633 0.32357 0.27892 0.00857  0.00191  0.00177  363 ALA A O   
1420 C  CB  . ALA A 363 ? 0.37427 0.33037 0.30437 0.01650  -0.01670 0.00379  363 ALA A CB  
1421 N  N   . GLN A 364 ? 0.36682 0.33284 0.30542 0.00028  0.00005  0.00751  364 GLN A N   
1422 C  CA  . GLN A 364 ? 0.33675 0.30516 0.27138 -0.00554 0.00635  0.00949  364 GLN A CA  
1423 C  C   . GLN A 364 ? 0.46533 0.42868 0.38408 -0.00319 0.00382  0.01102  364 GLN A C   
1424 O  O   . GLN A 364 ? 0.45137 0.42071 0.36560 -0.00457 0.00902  0.01035  364 GLN A O   
1425 C  CB  . GLN A 364 ? 0.34108 0.30424 0.28015 -0.01276 0.00771  0.01332  364 GLN A CB  
1426 C  CG  . GLN A 364 ? 0.34476 0.30783 0.27738 -0.01897 0.01305  0.01620  364 GLN A CG  
1427 C  CD  . GLN A 364 ? 0.41440 0.39015 0.35360 -0.02251 0.02239  0.01370  364 GLN A CD  
1428 O  OE1 . GLN A 364 ? 0.39399 0.37870 0.34319 -0.02063 0.02517  0.00994  364 GLN A OE1 
1429 N  NE2 . GLN A 364 ? 0.45957 0.43606 0.39299 -0.02780 0.02732  0.01585  364 GLN A NE2 
1430 N  N   . GLU A 365 ? 0.44985 0.40229 0.36011 0.00023  -0.00407 0.01306  365 GLU A N   
1431 C  CA  . GLU A 365 ? 0.73069 0.67858 0.62619 0.00321  -0.00695 0.01421  365 GLU A CA  
1432 C  C   . GLU A 365 ? 0.70994 0.65065 0.60006 0.01053  -0.01571 0.01334  365 GLU A C   
1433 O  O   . GLU A 365 ? 0.54523 0.48239 0.44211 0.01191  -0.01977 0.01299  365 GLU A O   
1434 C  CB  . GLU A 365 ? 0.65946 0.59963 0.54704 -0.00238 -0.00662 0.01921  365 GLU A CB  
1435 C  CG  . GLU A 365 ? 0.78359 0.71260 0.67225 -0.00435 -0.01197 0.02274  365 GLU A CG  
1436 C  CD  . GLU A 365 ? 1.06648 0.98701 0.94540 -0.00903 -0.01246 0.02780  365 GLU A CD  
1437 O  OE1 . GLU A 365 ? 1.10813 1.01764 0.97899 -0.00663 -0.01961 0.03035  365 GLU A OE1 
1438 O  OE2 . GLU A 365 ? 1.00185 0.92681 0.88116 -0.01509 -0.00569 0.02917  365 GLU A OE2 
1439 O  OXT . GLU A 365 ? 0.72923 0.66774 0.60846 0.01498  -0.01873 0.01292  365 GLU A OXT 
1440 N  N   . THR B 183 ? 1.06700 1.16884 1.09846 0.24464  0.00367  0.00450  183 THR B N   
1441 C  CA  . THR B 183 ? 0.97366 1.05771 0.98835 0.23995  0.00796  0.00502  183 THR B CA  
1442 C  C   . THR B 183 ? 1.00877 1.07463 1.00420 0.23256  0.00419  0.00715  183 THR B C   
1443 O  O   . THR B 183 ? 1.06190 1.11079 1.03895 0.23172  0.00575  0.00803  183 THR B O   
1444 C  CB  . THR B 183 ? 0.98741 1.06328 0.99404 0.24692  0.01219  0.00440  183 THR B CB  
1445 N  N   . ARG B 184 ? 0.86180 0.93194 0.86164 0.22725  -0.00083 0.00778  184 ARG B N   
1446 C  CA  . ARG B 184 ? 0.46214 0.51680 0.44579 0.21893  -0.00346 0.00880  184 ARG B CA  
1447 C  C   . ARG B 184 ? 0.39460 0.45116 0.38257 0.21107  -0.00335 0.00888  184 ARG B C   
1448 O  O   . ARG B 184 ? 0.40556 0.44774 0.37872 0.20425  -0.00410 0.00925  184 ARG B O   
1449 C  CB  . ARG B 184 ? 0.53437 0.58715 0.51453 0.21852  -0.01014 0.00920  184 ARG B CB  
1450 C  CG  . ARG B 184 ? 0.82815 0.86335 0.78710 0.21813  -0.01045 0.00918  184 ARG B CG  
1451 C  CD  . ARG B 184 ? 0.72935 0.76418 0.68643 0.21855  -0.01657 0.00893  184 ARG B CD  
1452 N  N   . THR B 185 ? 0.40606 0.48034 0.41372 0.21180  -0.00237 0.00829  185 THR B N   
1453 C  CA  . THR B 185 ? 0.37595 0.45226 0.38807 0.20451  -0.00199 0.00840  185 THR B CA  
1454 C  C   . THR B 185 ? 0.41233 0.49799 0.43478 0.20614  0.00537  0.00666  185 THR B C   
1455 O  O   . THR B 185 ? 0.40855 0.51169 0.44717 0.21247  0.00808  0.00498  185 THR B O   
1456 C  CB  . THR B 185 ? 0.44101 0.53130 0.46789 0.20171  -0.00843 0.00934  185 THR B CB  
1457 O  OG1 . THR B 185 ? 0.49832 0.57594 0.51262 0.19783  -0.01485 0.01052  185 THR B OG1 
1458 C  CG2 . THR B 185 ? 0.39416 0.49013 0.42914 0.19517  -0.00750 0.00946  185 THR B CG2 
1459 N  N   . LEU B 186 ? 0.37122 0.44542 0.38413 0.20030  0.00875  0.00665  186 LEU B N   
1460 C  CA  . LEU B 186 ? 0.38136 0.46335 0.40348 0.19952  0.01580  0.00458  186 LEU B CA  
1461 C  C   . LEU B 186 ? 0.35350 0.44116 0.38306 0.19220  0.01373  0.00477  186 LEU B C   
1462 O  O   . LEU B 186 ? 0.33498 0.40753 0.35162 0.18588  0.00902  0.00671  186 LEU B O   
1463 C  CB  . LEU B 186 ? 0.45851 0.52157 0.46254 0.19829  0.02087  0.00484  186 LEU B CB  
1464 C  CG  . LEU B 186 ? 0.61194 0.67600 0.61836 0.19883  0.02927  0.00269  186 LEU B CG  
1465 C  CD1 . LEU B 186 ? 0.43640 0.51974 0.46054 0.20705  0.03368  -0.00045 186 LEU B CD1 
1466 C  CD2 . LEU B 186 ? 0.45678 0.49836 0.44057 0.19777  0.03077  0.00487  186 LEU B CD2 
1467 N  N   . TRP B 187 ? 0.38931 0.50304 0.43109 0.19882  0.01747  0.00350  187 TRP B N   
1468 C  CA  . TRP B 187 ? 0.36143 0.48731 0.40238 0.19841  0.01466  0.00513  187 TRP B CA  
1469 C  C   . TRP B 187 ? 0.35385 0.50875 0.40632 0.20304  0.02303  0.00285  187 TRP B C   
1470 O  O   . TRP B 187 ? 0.33746 0.50608 0.40120 0.20711  0.03032  -0.00040 187 TRP B O   
1471 C  CB  . TRP B 187 ? 0.32369 0.46082 0.37145 0.19901  0.00457  0.00748  187 TRP B CB  
1472 C  CG  . TRP B 187 ? 0.32054 0.48977 0.38908 0.20585  0.00457  0.00639  187 TRP B CG  
1473 C  CD1 . TRP B 187 ? 0.37541 0.56049 0.45669 0.21159  0.01220  0.00311  187 TRP B CD1 
1474 C  CD2 . TRP B 187 ? 0.46923 0.65828 0.54822 0.20663  -0.00416 0.00844  187 TRP B CD2 
1475 N  NE1 . TRP B 187 ? 0.38298 0.59734 0.48203 0.21603  0.00917  0.00284  187 TRP B NE1 
1476 C  CE2 . TRP B 187 ? 0.42913 0.64686 0.52727 0.21282  -0.00096 0.00628  187 TRP B CE2 
1477 C  CE3 . TRP B 187 ? 0.38333 0.56786 0.45732 0.20185  -0.01501 0.01184  187 TRP B CE3 
1478 C  CZ2 . TRP B 187 ? 0.39307 0.63663 0.50565 0.21406  -0.00802 0.00759  187 TRP B CZ2 
1479 C  CZ3 . TRP B 187 ? 0.67082 0.87987 0.75889 0.20284  -0.02259 0.01339  187 TRP B CZ3 
1480 C  CH2 . TRP B 187 ? 0.48696 0.72585 0.59427 0.20880  -0.01894 0.01134  187 TRP B CH2 
1481 N  N   . THR B 188 ? 0.40177 0.56672 0.45141 0.20143  0.02197  0.00436  188 THR B N   
1482 C  CA  . THR B 188 ? 0.44696 0.65274 0.51255 0.20352  0.02705  0.00302  188 THR B CA  
1483 C  C   . THR B 188 ? 0.44631 0.68130 0.52850 0.20536  0.01830  0.00466  188 THR B C   
1484 O  O   . THR B 188 ? 0.79100 1.00997 0.86791 0.20453  0.00733  0.00757  188 THR B O   
1485 C  CB  . THR B 188 ? 0.35590 0.56278 0.41205 0.19972  0.02764  0.00480  188 THR B CB  
1486 O  OG1 . THR B 188 ? 0.32811 0.52031 0.37493 0.19787  0.01309  0.00951  188 THR B OG1 
1487 C  CG2 . THR B 188 ? 0.38990 0.56263 0.42688 0.19688  0.03507  0.00354  188 THR B CG2 
1488 N  N   . THR B 189 ? 0.89835 1.17741 1.00091 0.20563  0.02336  0.00249  189 THR B N   
1489 C  CA  . THR B 189 ? 0.92460 1.23547 1.04346 0.20458  0.01393  0.00458  189 THR B CA  
1490 C  C   . THR B 189 ? 1.03733 1.35193 1.15065 0.19771  0.00173  0.00986  189 THR B C   
1491 O  O   . THR B 189 ? 1.04434 1.33903 1.14019 0.18178  0.00373  0.01044  189 THR B O   
1492 C  CB  . THR B 189 ? 1.07796 1.43878 1.22025 0.20231  0.02190  0.00096  189 THR B CB  
1493 O  OG1 . THR B 189 ? 1.26319 1.64087 1.40485 0.19293  0.03166  -0.00075 189 THR B OG1 
1494 C  CG2 . THR B 189 ? 1.19978 1.55571 1.34836 0.20958  0.02961  -0.00366 189 THR B CG2 
1495 N  N   . PRO B 190 ? 0.64296 0.96186 0.76016 0.19618  -0.01233 0.01346  190 PRO B N   
1496 C  CA  . PRO B 190 ? 0.71582 1.01420 0.81623 0.17974  -0.02649 0.01830  190 PRO B CA  
1497 C  C   . PRO B 190 ? 0.76409 1.08191 0.86538 0.15390  -0.02962 0.01948  190 PRO B C   
1498 O  O   . PRO B 190 ? 0.60704 0.90850 0.69462 0.13927  -0.04267 0.02349  190 PRO B O   
1499 C  CB  . PRO B 190 ? 0.61654 0.90880 0.72019 0.18863  -0.03895 0.02087  190 PRO B CB  
1500 C  CG  . PRO B 190 ? 0.78417 1.10094 0.90748 0.19437  -0.03197 0.01739  190 PRO B CG  
1501 C  CD  . PRO B 190 ? 0.84939 1.16839 0.97535 0.20041  -0.01541 0.01248  190 PRO B CD  
1502 N  N   . ASP B 191 ? 0.79037 1.14180 0.90620 0.14714  -0.01840 0.01606  191 ASP B N   
1503 C  CA  . ASP B 191 ? 0.92714 1.29606 1.04188 0.12073  -0.02079 0.01733  191 ASP B CA  
1504 C  C   . ASP B 191 ? 0.95213 1.29275 1.04354 0.10315  -0.01747 0.01783  191 ASP B C   
1505 O  O   . ASP B 191 ? 0.83501 1.13870 0.90919 0.11039  -0.01712 0.01817  191 ASP B O   
1506 C  CB  . ASP B 191 ? 0.95866 1.37632 1.09791 0.11950  -0.00985 0.01319  191 ASP B CB  
1507 C  CG  . ASP B 191 ? 0.99501 1.41735 1.13796 0.12857  0.00826  0.00757  191 ASP B CG  
1508 O  OD1 . ASP B 191 ? 0.95585 1.35574 1.09437 0.14850  0.01279  0.00604  191 ASP B OD1 
1509 O  OD2 . ASP B 191 ? 1.06468 1.51314 1.21441 0.11533  0.01792  0.00462  191 ASP B OD2 
1510 N  N   . THR B 192 ? 0.83696 1.19443 0.92710 0.07962  -0.01521 0.01793  192 THR B N   
1511 C  CA  . THR B 192 ? 0.94365 1.27487 1.01101 0.06108  -0.01307 0.01874  192 THR B CA  
1512 C  C   . THR B 192 ? 0.87804 1.23188 0.95165 0.05310  0.00390  0.01430  192 THR B C   
1513 O  O   . THR B 192 ? 0.78879 1.13415 0.84771 0.03141  0.00526  0.01521  192 THR B O   
1514 C  CB  . THR B 192 ? 0.89373 1.21398 0.94616 0.03661  -0.02843 0.02386  192 THR B CB  
1515 O  OG1 . THR B 192 ? 1.02292 1.38354 1.09046 0.02130  -0.02870 0.02410  192 THR B OG1 
1516 C  CG2 . THR B 192 ? 0.77640 1.07370 0.82190 0.04484  -0.04530 0.02776  192 THR B CG2 
1517 N  N   . SER B 193 ? 0.93725 1.31957 1.03220 0.07102  0.01699  0.00920  193 SER B N   
1518 C  CA  . SER B 193 ? 0.81283 1.21735 0.91470 0.06653  0.03402  0.00405  193 SER B CA  
1519 C  C   . SER B 193 ? 0.73144 1.10266 0.81718 0.07433  0.04379  0.00182  193 SER B C   
1520 O  O   . SER B 193 ? 0.72646 1.07414 0.80889 0.09501  0.04309  0.00165  193 SER B O   
1521 C  CB  . SER B 193 ? 0.70544 1.15390 0.83646 0.08318  0.04325  -0.00099 193 SER B CB  
1522 O  OG  . SER B 193 ? 0.71758 1.15532 0.85529 0.11048  0.04152  -0.00168 193 SER B OG  
1523 N  N   . PRO B 194 ? 0.67846 1.04812 0.75414 0.05797  0.05318  0.00006  194 PRO B N   
1524 C  CA  . PRO B 194 ? 0.48801 0.82086 0.54407 0.06119  0.06007  -0.00104 194 PRO B CA  
1525 C  C   . PRO B 194 ? 0.53936 0.87378 0.60548 0.08730  0.07285  -0.00620 194 PRO B C   
1526 O  O   . PRO B 194 ? 0.54285 0.91241 0.62886 0.09526  0.08414  -0.01127 194 PRO B O   
1527 C  CB  . PRO B 194 ? 0.49817 0.83846 0.54530 0.03674  0.06793  -0.00218 194 PRO B CB  
1528 C  CG  . PRO B 194 ? 0.67603 1.04417 0.73028 0.01660  0.05973  0.00057  194 PRO B CG  
1529 C  CD  . PRO B 194 ? 0.66116 1.06008 0.74036 0.03322  0.05630  -0.00030 194 PRO B CD  
1530 N  N   . ASN B 195 ? 0.37394 0.66911 0.42502 0.10009  0.07107  -0.00510 195 ASN B N   
1531 C  CA  . ASN B 195 ? 0.30262 0.59271 0.35959 0.12474  0.08164  -0.00927 195 ASN B CA  
1532 C  C   . ASN B 195 ? 0.34765 0.59989 0.38300 0.12504  0.08803  -0.00994 195 ASN B C   
1533 O  O   . ASN B 195 ? 0.40657 0.64749 0.44270 0.14487  0.09557  -0.01274 195 ASN B O   
1534 C  CB  . ASN B 195 ? 0.29410 0.57774 0.35865 0.14641  0.07246  -0.00732 195 ASN B CB  
1535 C  CG  . ASN B 195 ? 0.31086 0.55794 0.35657 0.14221  0.05714  -0.00151 195 ASN B CG  
1536 O  OD1 . ASN B 195 ? 0.32304 0.54301 0.34779 0.12641  0.05392  0.00075  195 ASN B OD1 
1537 N  ND2 . ASN B 195 ? 0.30350 0.54911 0.35629 0.15732  0.04742  0.00070  195 ASN B ND2 
1538 N  N   . CYS B 196 ? 0.34427 0.57627 0.35991 0.10353  0.08497  -0.00742 196 CYS B N   
1539 C  CA  . CYS B 196 ? 0.31841 0.50902 0.31135 0.10386  0.08657  -0.00674 196 CYS B CA  
1540 C  C   . CYS B 196 ? 0.40092 0.58712 0.37994 0.08052  0.09212  -0.00721 196 CYS B C   
1541 O  O   . CYS B 196 ? 0.40998 0.61400 0.39035 0.06028  0.08801  -0.00557 196 CYS B O   
1542 C  CB  . CYS B 196 ? 0.44368 0.60124 0.42240 0.10572  0.07017  -0.00144 196 CYS B CB  
1543 S  SG  . CYS B 196 ? 0.47570 0.58163 0.42644 0.10681  0.06933  -0.00022 196 CYS B SG  
1544 N  N   . THR B 197 ? 0.42162 0.58442 0.38707 0.08316  0.10163  -0.00945 197 THR B N   
1545 C  CA  . THR B 197 ? 0.37796 0.53442 0.32918 0.06281  0.10852  -0.01038 197 THR B CA  
1546 C  C   . THR B 197 ? 0.51520 0.62514 0.44041 0.05894  0.10291  -0.00758 197 THR B C   
1547 O  O   . THR B 197 ? 0.45865 0.54704 0.37831 0.07509  0.10791  -0.00915 197 THR B O   
1548 C  CB  . THR B 197 ? 0.42146 0.59814 0.38232 0.06935  0.12720  -0.01674 197 THR B CB  
1549 O  OG1 . THR B 197 ? 0.41663 0.63880 0.40231 0.07231  0.13151  -0.01962 197 THR B OG1 
1550 C  CG2 . THR B 197 ? 0.45661 0.62563 0.40165 0.04813  0.13451  -0.01768 197 THR B CG2 
1551 N  N   . ILE B 198 ? 0.48964 0.58386 0.39871 0.03784  0.09190  -0.00344 198 ILE B N   
1552 C  CA  . ILE B 198 ? 0.42714 0.47802 0.31117 0.03300  0.08569  -0.00104 198 ILE B CA  
1553 C  C   . ILE B 198 ? 0.43582 0.47977 0.30583 0.01533  0.09494  -0.00262 198 ILE B C   
1554 O  O   . ILE B 198 ? 0.65588 0.67935 0.51567 0.02147  0.10353  -0.00484 198 ILE B O   
1555 C  CB  . ILE B 198 ? 0.36675 0.39978 0.23932 0.02222  0.06646  0.00429  198 ILE B CB  
1556 C  CG1 . ILE B 198 ? 0.40857 0.45090 0.29557 0.03872  0.05707  0.00585  198 ILE B CG1 
1557 C  CG2 . ILE B 198 ? 0.48783 0.47601 0.33432 0.01798  0.05985  0.00616  198 ILE B CG2 
1558 C  CD1 . ILE B 198 ? 0.46539 0.49542 0.34317 0.02729  0.03827  0.01065  198 ILE B CD1 
1559 N  N   . ALA B 199 ? 0.45590 0.51576 0.32429 -0.00737 0.09263  -0.00122 199 ALA B N   
1560 C  CA  . ALA B 199 ? 0.46382 0.51903 0.31821 -0.02737 0.10016  -0.00219 199 ALA B CA  
1561 C  C   . ALA B 199 ? 0.56380 0.66062 0.43402 -0.03563 0.11311  -0.00578 199 ALA B C   
1562 O  O   . ALA B 199 ? 0.57327 0.67042 0.43619 -0.04487 0.12479  -0.00852 199 ALA B O   
1563 C  CB  . ALA B 199 ? 0.50523 0.53770 0.33846 -0.05088 0.08517  0.00296  199 ALA B CB  
1564 N  N   . GLN B 200 ? 0.47667 0.60922 0.36816 -0.03299 0.11137  -0.00601 200 GLN B N   
1565 C  CA  . GLN B 200 ? 0.46989 0.64629 0.37999 -0.03693 0.12444  -0.01035 200 GLN B CA  
1566 C  C   . GLN B 200 ? 0.49583 0.70304 0.43270 -0.01633 0.12505  -0.01240 200 GLN B C   
1567 O  O   . GLN B 200 ? 0.47043 0.66641 0.41004 -0.00434 0.11344  -0.00941 200 GLN B O   
1568 C  CB  . GLN B 200 ? 0.50109 0.69430 0.40629 -0.06642 0.12037  -0.00781 200 GLN B CB  
1569 C  CG  . GLN B 200 ? 0.59079 0.79947 0.50478 -0.07273 0.10569  -0.00355 200 GLN B CG  
1570 C  CD  . GLN B 200 ? 0.57857 0.79477 0.48206 -0.10386 0.09910  0.00008  200 GLN B CD  
1571 O  OE1 . GLN B 200 ? 0.60639 0.79866 0.48759 -0.12176 0.09856  0.00175  200 GLN B OE1 
1572 N  NE2 . GLN B 200 ? 0.61695 0.86569 0.53576 -0.11078 0.09351  0.00150  200 GLN B NE2 
1573 N  N   . ASP B 201 ? 0.49866 0.74568 0.45540 -0.01220 0.13848  -0.01776 201 ASP B N   
1574 C  CA  . ASP B 201 ? 0.39146 0.66545 0.37340 0.01147  0.14147  -0.02094 201 ASP B CA  
1575 C  C   . ASP B 201 ? 0.39624 0.68609 0.38937 0.00912  0.12696  -0.01675 201 ASP B C   
1576 O  O   . ASP B 201 ? 0.43280 0.74092 0.42646 -0.01245 0.12170  -0.01435 201 ASP B O   
1577 C  CB  . ASP B 201 ? 0.61603 0.93167 0.61681 0.01474  0.15847  -0.02806 201 ASP B CB  
1578 C  CG  . ASP B 201 ? 0.74666 1.08645 0.77203 0.04212  0.16289  -0.03229 201 ASP B CG  
1579 O  OD1 . ASP B 201 ? 0.88751 1.20246 0.91067 0.06287  0.15916  -0.03143 201 ASP B OD1 
1580 O  OD2 . ASP B 201 ? 0.94565 1.32956 0.99235 0.04282  0.16990  -0.03657 201 ASP B OD2 
1581 N  N   . LYS B 202 ? 0.36681 0.64825 0.36768 0.03086  0.12005  -0.01565 202 LYS B N   
1582 C  CA  . LYS B 202 ? 0.38420 0.68232 0.39802 0.03261  0.10708  -0.01230 202 LYS B CA  
1583 C  C   . LYS B 202 ? 0.55809 0.83941 0.55533 0.00905  0.09139  -0.00583 202 LYS B C   
1584 O  O   . LYS B 202 ? 0.42061 0.72659 0.42715 -0.00265 0.08378  -0.00359 202 LYS B O   
1585 C  CB  . LYS B 202 ? 0.51480 0.86570 0.55578 0.03448  0.11429  -0.01635 202 LYS B CB  
1586 C  CG  . LYS B 202 ? 0.62637 0.99451 0.68572 0.06128  0.12711  -0.02278 202 LYS B CG  
1587 C  CD  . LYS B 202 ? 0.60291 0.94448 0.66124 0.08571  0.12019  -0.02104 202 LYS B CD  
1588 N  N   . ASP B 203 ? 0.36530 0.60403 0.33744 0.00202  0.08600  -0.00288 203 ASP B N   
1589 C  CA  . ASP B 203 ? 0.36616 0.58428 0.32008 -0.01934 0.07041  0.00297  203 ASP B CA  
1590 C  C   . ASP B 203 ? 0.35442 0.55206 0.30538 -0.00922 0.05386  0.00714  203 ASP B C   
1591 O  O   . ASP B 203 ? 0.36417 0.54293 0.29991 -0.02480 0.03936  0.01185  203 ASP B O   
1592 C  CB  . ASP B 203 ? 0.39075 0.57320 0.31794 -0.03367 0.07168  0.00397  203 ASP B CB  
1593 C  CG  . ASP B 203 ? 0.63246 0.77745 0.54783 -0.01525 0.07351  0.00307  203 ASP B CG  
1594 O  OD1 . ASP B 203 ? 0.53272 0.67441 0.45770 0.00778  0.07192  0.00242  203 ASP B OD1 
1595 O  OD2 . ASP B 203 ? 0.51845 0.63629 0.41365 -0.02487 0.07617  0.00320  203 ASP B OD2 
1596 N  N   . SER B 204 ? 0.34003 0.46814 0.29670 0.04382  0.05644  0.03465  204 SER B N   
1597 C  CA  . SER B 204 ? 0.31920 0.43911 0.28366 0.04105  0.04882  0.03637  204 SER B CA  
1598 C  C   . SER B 204 ? 0.31010 0.43810 0.28786 0.04825  0.04888  0.03439  204 SER B C   
1599 O  O   . SER B 204 ? 0.33023 0.46400 0.30935 0.05733  0.05352  0.03048  204 SER B O   
1600 C  CB  . SER B 204 ? 0.49941 0.59694 0.45380 0.04110  0.04234  0.03325  204 SER B CB  
1601 O  OG  . SER B 204 ? 0.46742 0.55757 0.41449 0.04955  0.04480  0.02635  204 SER B OG  
1602 N  N   . LYS B 205 ? 0.30766 0.43566 0.29486 0.04443  0.04338  0.03706  205 LYS B N   
1603 C  CA  . LYS B 205 ? 0.29516 0.42828 0.29327 0.05093  0.04156  0.03602  205 LYS B CA  
1604 C  C   . LYS B 205 ? 0.34644 0.46031 0.34197 0.04997  0.03448  0.03491  205 LYS B C   
1605 O  O   . LYS B 205 ? 0.28743 0.39864 0.28646 0.04176  0.02930  0.03745  205 LYS B O   
1606 C  CB  . LYS B 205 ? 0.35069 0.50546 0.36354 0.04701  0.04196  0.03947  205 LYS B CB  
1607 C  CG  . LYS B 205 ? 0.52613 0.68637 0.54991 0.05196  0.03783  0.03937  205 LYS B CG  
1608 C  CD  . LYS B 205 ? 0.71381 0.86870 0.73496 0.06517  0.03932  0.03611  205 LYS B CD  
1609 C  CE  . LYS B 205 ? 0.58372 0.74234 0.61313 0.07076  0.03495  0.03706  205 LYS B CE  
1610 N  NZ  . LYS B 205 ? 0.65341 0.83896 0.69610 0.07509  0.03730  0.03744  205 LYS B NZ  
1611 N  N   . LEU B 206 ? 0.34388 0.44430 0.33374 0.05802  0.03482  0.03058  206 LEU B N   
1612 C  CA  . LEU B 206 ? 0.31880 0.40225 0.30733 0.05783  0.02947  0.02890  206 LEU B CA  
1613 C  C   . LEU B 206 ? 0.28045 0.37157 0.27877 0.06248  0.02796  0.03110  206 LEU B C   
1614 O  O   . LEU B 206 ? 0.31853 0.41825 0.32009 0.07179  0.03179  0.03094  206 LEU B O   
1615 C  CB  . LEU B 206 ? 0.34406 0.40904 0.32229 0.06381  0.03146  0.02283  206 LEU B CB  
1616 C  CG  . LEU B 206 ? 0.33288 0.37931 0.30929 0.06331  0.02733  0.02014  206 LEU B CG  
1617 C  CD1 . LEU B 206 ? 0.33611 0.37311 0.30919 0.05330  0.02159  0.01892  206 LEU B CD1 
1618 C  CD2 . LEU B 206 ? 0.39160 0.42291 0.36097 0.07133  0.03149  0.01412  206 LEU B CD2 
1619 N  N   . THR B 207 ? 0.25325 0.34265 0.25653 0.05645  0.02221  0.03304  207 THR B N   
1620 C  CA  . THR B 207 ? 0.25839 0.35216 0.26819 0.06142  0.02007  0.03472  207 THR B CA  
1621 C  C   . THR B 207 ? 0.35746 0.42869 0.35996 0.06225  0.01765  0.03206  207 THR B C   
1622 O  O   . THR B 207 ? 0.31324 0.37430 0.31390 0.05378  0.01355  0.03053  207 THR B O   
1623 C  CB  . THR B 207 ? 0.31810 0.42861 0.33948 0.05448  0.01596  0.03808  207 THR B CB  
1624 O  OG1 . THR B 207 ? 0.36642 0.49701 0.39472 0.05204  0.01919  0.03980  207 THR B OG1 
1625 C  CG2 . THR B 207 ? 0.36906 0.48672 0.39614 0.06143  0.01372  0.03975  207 THR B CG2 
1626 N  N   . LEU B 208 ? 0.31252 0.37527 0.31089 0.07235  0.02059  0.03109  208 LEU B N   
1627 C  CA  . LEU B 208 ? 0.35012 0.39011 0.34087 0.07337  0.02004  0.02829  208 LEU B CA  
1628 C  C   . LEU B 208 ? 0.36378 0.40396 0.35548 0.08257  0.02048  0.03170  208 LEU B C   
1629 O  O   . LEU B 208 ? 0.31280 0.35977 0.30558 0.09297  0.02414  0.03306  208 LEU B O   
1630 C  CB  . LEU B 208 ? 0.33322 0.35652 0.31461 0.07646  0.02475  0.02248  208 LEU B CB  
1631 C  CG  . LEU B 208 ? 0.34181 0.34093 0.31588 0.07701  0.02554  0.01840  208 LEU B CG  
1632 C  CD1 . LEU B 208 ? 0.32418 0.31597 0.29861 0.06589  0.01998  0.01660  208 LEU B CD1 
1633 C  CD2 . LEU B 208 ? 0.34935 0.33430 0.31576 0.08056  0.03084  0.01152  208 LEU B CD2 
1634 N  N   . VAL B 209 ? 0.25877 0.29257 0.25009 0.07902  0.01657  0.03314  209 VAL B N   
1635 C  CA  . VAL B 209 ? 0.27903 0.31089 0.26881 0.08732  0.01633  0.03712  209 VAL B CA  
1636 C  C   . VAL B 209 ? 0.27385 0.27904 0.25347 0.08604  0.01784  0.03463  209 VAL B C   
1637 O  O   . VAL B 209 ? 0.32450 0.32220 0.30337 0.07572  0.01495  0.03176  209 VAL B O   
1638 C  CB  . VAL B 209 ? 0.28016 0.33150 0.27854 0.08413  0.01059  0.04129  209 VAL B CB  
1639 C  CG1 . VAL B 209 ? 0.31187 0.36378 0.30759 0.09492  0.01009  0.04602  209 VAL B CG1 
1640 C  CG2 . VAL B 209 ? 0.31555 0.39298 0.32529 0.08223  0.00970  0.04220  209 VAL B CG2 
1641 N  N   . LEU B 210 ? 0.33112 0.32172 0.30344 0.09632  0.02280  0.03517  210 LEU B N   
1642 C  CA  . LEU B 210 ? 0.30660 0.27046 0.26879 0.09595  0.02587  0.03308  210 LEU B CA  
1643 C  C   . LEU B 210 ? 0.39866 0.35924 0.35651 0.10441  0.02559  0.03997  210 LEU B C   
1644 O  O   . LEU B 210 ? 0.40067 0.36572 0.35836 0.11691  0.02753  0.04398  210 LEU B O   
1645 C  CB  . LEU B 210 ? 0.34721 0.29332 0.30342 0.10051  0.03281  0.02756  210 LEU B CB  
1646 C  CG  . LEU B 210 ? 0.41588 0.36475 0.37426 0.09415  0.03348  0.02049  210 LEU B CG  
1647 C  CD1 . LEU B 210 ? 0.39988 0.33022 0.35182 0.09942  0.04070  0.01426  210 LEU B CD1 
1648 C  CD2 . LEU B 210 ? 0.34925 0.29502 0.30849 0.08064  0.02899  0.01644  210 LEU B CD2 
1649 N  N   . THR B 211 ? 0.34590 0.29872 0.29979 0.09818  0.02316  0.04122  211 THR B N   
1650 C  CA  . THR B 211 ? 0.35318 0.30077 0.30019 0.10573  0.02287  0.04818  211 THR B CA  
1651 C  C   . THR B 211 ? 0.42793 0.34514 0.36250 0.10317  0.02802  0.04651  211 THR B C   
1652 O  O   . THR B 211 ? 0.38757 0.29627 0.32159 0.09098  0.02788  0.04078  211 THR B O   
1653 C  CB  . THR B 211 ? 0.45159 0.41987 0.40437 0.10108  0.01555  0.05189  211 THR B CB  
1654 O  OG1 . THR B 211 ? 0.44531 0.44168 0.41063 0.10269  0.01177  0.05258  211 THR B OG1 
1655 C  CG2 . THR B 211 ? 0.49798 0.46179 0.44193 0.11031  0.01489  0.05957  211 THR B CG2 
1656 N  N   . LYS B 212 ? 0.43072 0.33155 0.35553 0.11463  0.03271  0.05142  212 LYS B N   
1657 C  CA  . LYS B 212 ? 0.42338 0.29261 0.33574 0.11272  0.03954  0.04982  212 LYS B CA  
1658 C  C   . LYS B 212 ? 0.51306 0.37832 0.41770 0.10938  0.03720  0.05527  212 LYS B C   
1659 O  O   . LYS B 212 ? 0.54927 0.42068 0.44945 0.11935  0.03463  0.06420  212 LYS B O   
1660 C  CB  . LYS B 212 ? 0.48921 0.33967 0.39418 0.12631  0.04659  0.05242  212 LYS B CB  
1661 C  CG  . LYS B 212 ? 0.46724 0.28329 0.36019 0.12296  0.05511  0.04949  212 LYS B CG  
1662 C  CD  . LYS B 212 ? 0.54716 0.34319 0.43437 0.13555  0.06285  0.05051  212 LYS B CD  
1663 C  CE  . LYS B 212 ? 0.63100 0.39175 0.50623 0.13118  0.07212  0.04768  212 LYS B CE  
1664 N  NZ  . LYS B 212 ? 0.58231 0.33703 0.46154 0.11566  0.07469  0.03529  212 LYS B NZ  
1665 N  N   . CYS B 213 ? 0.45653 0.31337 0.35994 0.09546  0.03767  0.04943  213 CYS B N   
1666 C  CA  . CYS B 213 ? 0.55141 0.40146 0.44633 0.09016  0.03693  0.05286  213 CYS B CA  
1667 C  C   . CYS B 213 ? 0.63200 0.44823 0.51455 0.08657  0.04641  0.04963  213 CYS B C   
1668 O  O   . CYS B 213 ? 0.63221 0.43998 0.51584 0.07347  0.04843  0.04118  213 CYS B O   
1669 C  CB  . CYS B 213 ? 0.53697 0.40525 0.44164 0.07628  0.03035  0.04763  213 CYS B CB  
1670 S  SG  . CYS B 213 ? 0.71146 0.61773 0.63337 0.07716  0.02077  0.04854  213 CYS B SG  
1671 N  N   . GLY B 214 ? 0.69737 0.49418 0.56903 0.09829  0.05253  0.05565  214 GLY B N   
1672 C  CA  . GLY B 214 ? 0.57156 0.33449 0.43157 0.09527  0.06285  0.05266  214 GLY B CA  
1673 C  C   . GLY B 214 ? 0.62793 0.38312 0.49565 0.08720  0.06731  0.03963  214 GLY B C   
1674 O  O   . GLY B 214 ? 0.65831 0.41985 0.53330 0.09314  0.06734  0.03660  214 GLY B O   
1675 N  N   . SER B 215 ? 0.58448 0.32698 0.45081 0.07342  0.07108  0.03108  215 SER B N   
1676 C  CA  . SER B 215 ? 0.57923 0.31122 0.45111 0.06600  0.07618  0.01786  215 SER B CA  
1677 C  C   . SER B 215 ? 0.48274 0.23957 0.36957 0.05961  0.06829  0.00992  215 SER B C   
1678 O  O   . SER B 215 ? 0.50335 0.25498 0.39532 0.05371  0.07098  -0.00158 215 SER B O   
1679 C  CB  . SER B 215 ? 0.90549 0.61484 0.77076 0.05364  0.08360  0.01073  215 SER B CB  
1680 O  OG  . SER B 215 ? 1.12079 0.82282 0.99269 0.04616  0.08808  -0.00323 215 SER B OG  
1681 N  N   . GLN B 216 ? 0.44884 0.23199 0.34246 0.06034  0.05876  0.01545  216 GLN B N   
1682 C  CA  . GLN B 216 ? 0.41660 0.22227 0.32350 0.05452  0.05136  0.00939  216 GLN B CA  
1683 C  C   . GLN B 216 ? 0.43282 0.26095 0.34557 0.06456  0.04582  0.01695  216 GLN B C   
1684 O  O   . GLN B 216 ? 0.44497 0.27981 0.35426 0.07283  0.04392  0.02704  216 GLN B O   
1685 C  CB  . GLN B 216 ? 0.45680 0.27487 0.36936 0.04216  0.04485  0.00646  216 GLN B CB  
1686 C  CG  . GLN B 216 ? 0.49715 0.30368 0.41171 0.02944  0.04731  -0.00605 216 GLN B CG  
1687 C  CD  . GLN B 216 ? 0.39317 0.21332 0.31425 0.01844  0.04053  -0.00863 216 GLN B CD  
1688 O  OE1 . GLN B 216 ? 0.41088 0.25044 0.34280 0.01502  0.03280  -0.01086 216 GLN B OE1 
1689 N  NE2 . GLN B 216 ? 0.40100 0.21057 0.31506 0.01310  0.04377  -0.00801 216 GLN B NE2 
1690 N  N   . ILE B 217 ? 0.37833 0.21899 0.29985 0.06362  0.04315  0.01174  217 ILE B N   
1691 C  CA  . ILE B 217 ? 0.35765 0.22194 0.28633 0.07068  0.03811  0.01736  217 ILE B CA  
1692 C  C   . ILE B 217 ? 0.34352 0.22903 0.28192 0.06123  0.02980  0.01626  217 ILE B C   
1693 O  O   . ILE B 217 ? 0.35816 0.24224 0.30048 0.05145  0.02808  0.00804  217 ILE B O   
1694 C  CB  . ILE B 217 ? 0.35651 0.22091 0.28748 0.07593  0.04135  0.01284  217 ILE B CB  
1695 C  CG1 . ILE B 217 ? 0.41424 0.25472 0.33641 0.08417  0.05041  0.01193  217 ILE B CG1 
1696 C  CG2 . ILE B 217 ? 0.34375 0.23360 0.28227 0.08221  0.03677  0.01853  217 ILE B CG2 
1697 C  CD1 . ILE B 217 ? 0.45842 0.29356 0.37396 0.09595  0.05251  0.02238  217 ILE B CD1 
1698 N  N   . LEU B 218 ? 0.33675 0.24137 0.27920 0.06412  0.02459  0.02405  218 LEU B N   
1699 C  CA  . LEU B 218 ? 0.32167 0.24787 0.27459 0.05613  0.01706  0.02367  218 LEU B CA  
1700 C  C   . LEU B 218 ? 0.33415 0.27792 0.29476 0.05976  0.01532  0.02451  218 LEU B C   
1701 O  O   . LEU B 218 ? 0.29488 0.24738 0.25578 0.07014  0.01664  0.03005  218 LEU B O   
1702 C  CB  . LEU B 218 ? 0.31209 0.25120 0.26616 0.05681  0.01274  0.03048  218 LEU B CB  
1703 C  CG  . LEU B 218 ? 0.29596 0.25795 0.26201 0.04821  0.00522  0.02981  218 LEU B CG  
1704 C  CD1 . LEU B 218 ? 0.31776 0.27171 0.28612 0.03504  0.00342  0.02177  218 LEU B CD1 
1705 C  CD2 . LEU B 218 ? 0.33865 0.31506 0.30531 0.05131  0.00152  0.03649  218 LEU B CD2 
1706 N  N   . ALA B 219 ? 0.26934 0.21787 0.23570 0.05156  0.01260  0.01892  219 ALA B N   
1707 C  CA  . ALA B 219 ? 0.30352 0.26492 0.27469 0.05393  0.01224  0.01904  219 ALA B CA  
1708 C  C   . ALA B 219 ? 0.36705 0.34846 0.34838 0.04631  0.00587  0.02046  219 ALA B C   
1709 O  O   . ALA B 219 ? 0.30359 0.28343 0.28813 0.03665  0.00173  0.01710  219 ALA B O   
1710 C  CB  . ALA B 219 ? 0.30008 0.24724 0.26690 0.05194  0.01541  0.01111  219 ALA B CB  
1711 N  N   . ASN B 220 ? 0.28454 0.28434 0.27147 0.05026  0.00553  0.02473  220 ASN B N   
1712 C  CA  . ASN B 220 ? 0.24185 0.26020 0.23870 0.04296  0.00073  0.02622  220 ASN B CA  
1713 C  C   . ASN B 220 ? 0.25003 0.27552 0.24756 0.04470  0.00310  0.02627  220 ASN B C   
1714 O  O   . ASN B 220 ? 0.27719 0.30680 0.27277 0.05384  0.00747  0.02829  220 ASN B O   
1715 C  CB  . ASN B 220 ? 0.24725 0.28477 0.25157 0.04522  -0.00182 0.03175  220 ASN B CB  
1716 C  CG  . ASN B 220 ? 0.43106 0.48752 0.44688 0.03687  -0.00608 0.03259  220 ASN B CG  
1717 O  OD1 . ASN B 220 ? 0.40525 0.47615 0.42627 0.03801  -0.00470 0.03463  220 ASN B OD1 
1718 N  ND2 . ASN B 220 ? 0.41345 0.46995 0.43370 0.02798  -0.01076 0.03062  220 ASN B ND2 
1719 N  N   . VAL B 221 ? 0.25270 0.27863 0.25211 0.03647  0.00047  0.02392  221 VAL B N   
1720 C  CA  . VAL B 221 ? 0.27583 0.30524 0.27260 0.03787  0.00324  0.02375  221 VAL B CA  
1721 C  C   . VAL B 221 ? 0.28855 0.33058 0.29205 0.02952  -0.00009 0.02621  221 VAL B C   
1722 O  O   . VAL B 221 ? 0.26834 0.30865 0.27631 0.02129  -0.00517 0.02521  221 VAL B O   
1723 C  CB  . VAL B 221 ? 0.24333 0.25371 0.23028 0.03826  0.00486  0.01727  221 VAL B CB  
1724 C  CG1 . VAL B 221 ? 0.28228 0.28351 0.26970 0.02886  -0.00070 0.01293  221 VAL B CG1 
1725 C  CG2 . VAL B 221 ? 0.26669 0.28110 0.24879 0.04153  0.00857  0.01696  221 VAL B CG2 
1726 N  N   . SER B 222 ? 0.24537 0.29996 0.24981 0.03156  0.00332  0.02929  222 SER B N   
1727 C  CA  . SER B 222 ? 0.22630 0.28916 0.23416 0.02378  0.00187  0.03179  222 SER B CA  
1728 C  C   . SER B 222 ? 0.26110 0.32902 0.26314 0.02766  0.00745  0.03300  222 SER B C   
1729 O  O   . SER B 222 ? 0.31071 0.37977 0.30927 0.03642  0.01219  0.03191  222 SER B O   
1730 C  CB  . SER B 222 ? 0.33225 0.41348 0.35307 0.01896  0.00013  0.03570  222 SER B CB  
1731 O  OG  . SER B 222 ? 0.36564 0.46405 0.39126 0.02556  0.00457  0.03824  222 SER B OG  
1732 N  N   . LEU B 223 ? 0.28741 0.35784 0.28800 0.02115  0.00710  0.03528  223 LEU B N   
1733 C  CA  . LEU B 223 ? 0.25296 0.32714 0.24595 0.02373  0.01251  0.03633  223 LEU B CA  
1734 C  C   . LEU B 223 ? 0.22925 0.31614 0.22643 0.01640  0.01417  0.04174  223 LEU B C   
1735 O  O   . LEU B 223 ? 0.28532 0.36913 0.28583 0.00804  0.00986  0.04387  223 LEU B O   
1736 C  CB  . LEU B 223 ? 0.27234 0.32893 0.25191 0.02449  0.01111  0.03222  223 LEU B CB  
1737 C  CG  . LEU B 223 ? 0.27922 0.33841 0.24846 0.02703  0.01628  0.03264  223 LEU B CG  
1738 C  CD1 . LEU B 223 ? 0.35072 0.41669 0.31938 0.03651  0.02299  0.03017  223 LEU B CD1 
1739 C  CD2 . LEU B 223 ? 0.36625 0.40918 0.32277 0.02605  0.01273  0.02868  223 LEU B CD2 
1740 N  N   . ILE B 224 ? 0.26878 0.36975 0.26615 0.01946  0.02099  0.04356  224 ILE B N   
1741 C  CA  . ILE B 224 ? 0.28865 0.40045 0.28720 0.01259  0.02480  0.04830  224 ILE B CA  
1742 C  C   . ILE B 224 ? 0.28056 0.39003 0.26555 0.01621  0.03031  0.04783  224 ILE B C   
1743 O  O   . ILE B 224 ? 0.37908 0.49394 0.36268 0.02466  0.03478  0.04454  224 ILE B O   
1744 C  CB  . ILE B 224 ? 0.26279 0.39790 0.27618 0.01189  0.02882  0.04997  224 ILE B CB  
1745 C  CG1 . ILE B 224 ? 0.31590 0.45513 0.34256 0.00853  0.02313  0.04977  224 ILE B CG1 
1746 C  CG2 . ILE B 224 ? 0.33946 0.48548 0.35328 0.00416  0.03474  0.05427  224 ILE B CG2 
1747 C  CD1 . ILE B 224 ? 0.45847 0.62163 0.49984 0.01126  0.02594  0.04938  224 ILE B CD1 
1748 N  N   . VAL B 225 ? 0.27311 0.37383 0.24758 0.01046  0.02972  0.05083  225 VAL B N   
1749 C  CA  . VAL B 225 ? 0.26387 0.36554 0.22502 0.01244  0.03562  0.05139  225 VAL B CA  
1750 C  C   . VAL B 225 ? 0.36755 0.48534 0.33330 0.00589  0.04243  0.05688  225 VAL B C   
1751 O  O   . VAL B 225 ? 0.36607 0.48271 0.33562 -0.00310 0.04075  0.06191  225 VAL B O   
1752 C  CB  . VAL B 225 ? 0.29249 0.37579 0.23746 0.01091  0.03117  0.05158  225 VAL B CB  
1753 C  CG1 . VAL B 225 ? 0.34975 0.43548 0.27990 0.01400  0.03746  0.05138  225 VAL B CG1 
1754 C  CG2 . VAL B 225 ? 0.32462 0.39308 0.26827 0.01600  0.02431  0.04485  225 VAL B CG2 
1755 N  N   . VAL B 226 ? 0.38821 0.52113 0.35453 0.01016  0.05055  0.05530  226 VAL B N   
1756 C  CA  . VAL B 226 ? 0.44935 0.60049 0.42243 0.00392  0.05818  0.05903  226 VAL B CA  
1757 C  C   . VAL B 226 ? 0.49831 0.64861 0.45571 0.00042  0.06495  0.06235  226 VAL B C   
1758 O  O   . VAL B 226 ? 0.47347 0.63399 0.43374 -0.00780 0.07114  0.06688  226 VAL B O   
1759 C  CB  . VAL B 226 ? 0.34419 0.51713 0.33187 0.01024  0.06311  0.05468  226 VAL B CB  
1760 C  CG1 . VAL B 226 ? 0.32939 0.50401 0.33135 0.01352  0.05650  0.05250  226 VAL B CG1 
1761 C  CG2 . VAL B 226 ? 0.49821 0.67243 0.47789 0.02050  0.06733  0.04945  226 VAL B CG2 
1762 N  N   . ALA B 227 ? 0.35455 0.49319 0.29526 0.00593  0.06425  0.06002  227 ALA B N   
1763 C  CA  . ALA B 227 ? 0.44756 0.58618 0.37157 0.00328  0.07066  0.06300  227 ALA B CA  
1764 C  C   . ALA B 227 ? 0.50744 0.62799 0.41262 0.00814  0.06561  0.06077  227 ALA B C   
1765 O  O   . ALA B 227 ? 0.46784 0.57802 0.37444 0.01414  0.05865  0.05546  227 ALA B O   
1766 C  CB  . ALA B 227 ? 0.45302 0.61224 0.38068 0.00690  0.08098  0.05926  227 ALA B CB  
1767 N  N   . GLY B 228 ? 0.42315 0.54062 0.31024 0.00534  0.06954  0.06455  228 GLY B N   
1768 C  CA  . GLY B 228 ? 0.56404 0.66834 0.43233 0.01063  0.06568  0.06141  228 GLY B CA  
1769 C  C   . GLY B 228 ? 0.55860 0.64257 0.41873 0.00836  0.05515  0.06463  228 GLY B C   
1770 O  O   . GLY B 228 ? 0.45225 0.53047 0.31795 0.00121  0.05164  0.07128  228 GLY B O   
1771 N  N   . LYS B 229 ? 0.45841 0.53205 0.30587 0.01489  0.05009  0.05876  229 LYS B N   
1772 C  CA  . LYS B 229 ? 0.50631 0.56199 0.34225 0.01434  0.04027  0.06041  229 LYS B CA  
1773 C  C   . LYS B 229 ? 0.54924 0.59584 0.39933 0.01053  0.03208  0.06211  229 LYS B C   
1774 O  O   . LYS B 229 ? 0.51096 0.54598 0.35547 0.00593  0.02634  0.06832  229 LYS B O   
1775 C  CB  . LYS B 229 ? 0.50240 0.55232 0.32899 0.02292  0.03625  0.05016  229 LYS B CB  
1776 C  CG  . LYS B 229 ? 0.55763 0.59127 0.37273 0.02401  0.02561  0.04931  229 LYS B CG  
1777 C  CD  . LYS B 229 ? 0.58971 0.62178 0.39426 0.03202  0.02389  0.03838  229 LYS B CD  
1778 C  CE  . LYS B 229 ? 0.74920 0.76686 0.54709 0.03411  0.01225  0.03442  229 LYS B CE  
1779 N  NZ  . LYS B 229 ? 0.68413 0.70155 0.47472 0.04157  0.01065  0.02165  229 LYS B NZ  
1780 N  N   . TYR B 230 ? 0.42252 0.47382 0.29054 0.01264  0.03139  0.05666  230 TYR B N   
1781 C  CA  . TYR B 230 ? 0.36033 0.40298 0.24105 0.01001  0.02317  0.05605  230 TYR B CA  
1782 C  C   . TYR B 230 ? 0.38427 0.43567 0.28101 0.00292  0.02574  0.06199  230 TYR B C   
1783 O  O   . TYR B 230 ? 0.40191 0.44907 0.31112 0.00026  0.01992  0.06124  230 TYR B O   
1784 C  CB  . TYR B 230 ? 0.40993 0.44980 0.29836 0.01666  0.02001  0.04600  230 TYR B CB  
1785 C  CG  . TYR B 230 ? 0.42676 0.45684 0.30090 0.02241  0.01637  0.03895  230 TYR B CG  
1786 C  CD1 . TYR B 230 ? 0.44143 0.45794 0.30731 0.02108  0.00751  0.03878  230 TYR B CD1 
1787 C  CD2 . TYR B 230 ? 0.41191 0.44715 0.28101 0.02936  0.02178  0.03189  230 TYR B CD2 
1788 C  CE1 . TYR B 230 ? 0.41680 0.42638 0.26984 0.02661  0.00383  0.03122  230 TYR B CE1 
1789 C  CE2 . TYR B 230 ? 0.46348 0.49119 0.31996 0.03431  0.01873  0.02424  230 TYR B CE2 
1790 C  CZ  . TYR B 230 ? 0.47823 0.49383 0.32675 0.03289  0.00967  0.02377  230 TYR B CZ  
1791 O  OH  . TYR B 230 ? 0.54202 0.55219 0.37885 0.03808  0.00634  0.01498  230 TYR B OH  
1792 N  N   . HIS B 231 ? 0.40884 0.47296 0.30543 -0.00074 0.03451  0.06732  231 HIS B N   
1793 C  CA  . HIS B 231 ? 0.43671 0.51229 0.35002 -0.00748 0.03794  0.07142  231 HIS B CA  
1794 C  C   . HIS B 231 ? 0.37164 0.43636 0.28756 -0.01597 0.03251  0.07768  231 HIS B C   
1795 O  O   . HIS B 231 ? 0.40905 0.47542 0.34117 -0.01928 0.02870  0.07676  231 HIS B O   
1796 C  CB  . HIS B 231 ? 0.51596 0.60732 0.42706 -0.01001 0.04914  0.07485  231 HIS B CB  
1797 C  CG  . HIS B 231 ? 0.36701 0.47226 0.29524 -0.01743 0.05362  0.07815  231 HIS B CG  
1798 N  ND1 . HIS B 231 ? 0.49117 0.60374 0.43863 -0.01664 0.05020  0.07442  231 HIS B ND1 
1799 C  CD2 . HIS B 231 ? 0.50737 0.62116 0.43672 -0.02604 0.06144  0.08423  231 HIS B CD2 
1800 C  CE1 . HIS B 231 ? 0.46652 0.59298 0.42694 -0.02406 0.05529  0.07740  231 HIS B CE1 
1801 N  NE2 . HIS B 231 ? 0.49716 0.62427 0.44762 -0.03032 0.06241  0.08320  231 HIS B NE2 
1802 N  N   . ILE B 232 ? 0.40150 0.45500 0.30122 -0.01934 0.03222  0.08413  232 ILE B N   
1803 C  CA  . ILE B 232 ? 0.39202 0.43196 0.29157 -0.02645 0.02688  0.09052  232 ILE B CA  
1804 C  C   . ILE B 232 ? 0.56525 0.58638 0.44909 -0.02148 0.01752  0.08930  232 ILE B C   
1805 O  O   . ILE B 232 ? 0.50872 0.52592 0.37327 -0.01751 0.01902  0.09064  232 ILE B O   
1806 C  CB  . ILE B 232 ? 0.45999 0.50163 0.35343 -0.03504 0.03508  0.10042  232 ILE B CB  
1807 C  CG1 . ILE B 232 ? 0.51766 0.58136 0.42622 -0.03927 0.04544  0.09980  232 ILE B CG1 
1808 C  CG2 . ILE B 232 ? 0.52042 0.54695 0.41599 -0.04243 0.02981  0.10687  232 ILE B CG2 
1809 C  CD1 . ILE B 232 ? 0.59410 0.66588 0.52659 -0.04314 0.04283  0.09668  232 ILE B CD1 
1810 N  N   . ILE B 233 ? 0.44932 0.45997 0.34135 -0.02174 0.00790  0.08631  233 ILE B N   
1811 C  CA  . ILE B 233 ? 0.36124 0.35540 0.24106 -0.01684 -0.00194 0.08365  233 ILE B CA  
1812 C  C   . ILE B 233 ? 0.49316 0.47288 0.36318 -0.02162 -0.00530 0.09304  233 ILE B C   
1813 O  O   . ILE B 233 ? 0.43524 0.41218 0.31700 -0.02901 -0.00584 0.09756  233 ILE B O   
1814 C  CB  . ILE B 233 ? 0.44836 0.43862 0.34214 -0.01454 -0.01051 0.07453  233 ILE B CB  
1815 C  CG1 . ILE B 233 ? 0.54184 0.54416 0.44432 -0.00973 -0.00665 0.06635  233 ILE B CG1 
1816 C  CG2 . ILE B 233 ? 0.59872 0.57346 0.48124 -0.00964 -0.02080 0.07052  233 ILE B CG2 
1817 C  CD1 . ILE B 233 ? 0.56964 0.57531 0.45738 -0.00243 -0.00236 0.06285  233 ILE B CD1 
1818 N  N   . ASN B 234 ? 0.50711 0.47712 0.35537 -0.01713 -0.00779 0.09587  234 ASN B N   
1819 C  CA  . ASN B 234 ? 0.52175 0.47454 0.35888 -0.01941 -0.01337 0.10430  234 ASN B CA  
1820 C  C   . ASN B 234 ? 0.64307 0.58510 0.46531 -0.01039 -0.02367 0.09915  234 ASN B C   
1821 O  O   . ASN B 234 ? 0.57253 0.51503 0.37488 -0.00519 -0.02190 0.10005  234 ASN B O   
1822 C  CB  . ASN B 234 ? 0.53930 0.49053 0.36155 -0.02452 -0.00438 0.11666  234 ASN B CB  
1823 C  CG  . ASN B 234 ? 0.59282 0.52467 0.40715 -0.02806 -0.00945 0.12646  234 ASN B CG  
1824 O  OD1 . ASN B 234 ? 0.60077 0.51953 0.41245 -0.02321 -0.02103 0.12380  234 ASN B OD1 
1825 N  ND2 . ASN B 234 ? 0.59538 0.52524 0.40759 -0.03668 -0.00076 0.13721  234 ASN B ND2 
1826 N  N   . ASN B 235 ? 0.52268 0.45633 0.35505 -0.00871 -0.03430 0.09302  235 ASN B N   
1827 C  CA  . ASN B 235 ? 0.49033 0.41414 0.31114 -0.00055 -0.04518 0.08717  235 ASN B CA  
1828 C  C   . ASN B 235 ? 0.54262 0.44959 0.34832 0.00016  -0.05165 0.09665  235 ASN B C   
1829 O  O   . ASN B 235 ? 0.70619 0.60536 0.50062 0.00777  -0.06141 0.09238  235 ASN B O   
1830 C  CB  . ASN B 235 ? 0.58860 0.51172 0.42747 0.00101  -0.05351 0.07510  235 ASN B CB  
1831 C  CG  . ASN B 235 ? 0.53612 0.47296 0.38726 0.00156  -0.04796 0.06596  235 ASN B CG  
1832 O  OD1 . ASN B 235 ? 0.60347 0.54496 0.47388 -0.00305 -0.04679 0.06313  235 ASN B OD1 
1833 N  ND2 . ASN B 235 ? 0.64935 0.59290 0.48890 0.00727  -0.04398 0.06163  235 ASN B ND2 
1834 N  N   . LYS B 236 ? 0.57861 0.47954 0.38450 -0.00739 -0.04669 0.10888  236 LYS B N   
1835 C  CA  . LYS B 236 ? 0.71620 0.59971 0.50299 -0.00623 -0.05076 0.12014  236 LYS B CA  
1836 C  C   . LYS B 236 ? 0.77695 0.66162 0.53623 -0.00067 -0.04722 0.12456  236 LYS B C   
1837 O  O   . LYS B 236 ? 0.86910 0.74343 0.60960 0.00714  -0.05587 0.12563  236 LYS B O   
1838 C  CB  . LYS B 236 ? 0.73289 0.60972 0.52559 -0.01664 -0.04380 0.13236  236 LYS B CB  
1839 C  CG  . LYS B 236 ? 0.87969 0.75270 0.69719 -0.02209 -0.04848 0.12901  236 LYS B CG  
1840 C  CD  . LYS B 236 ? 0.95510 0.81145 0.76929 -0.01583 -0.06265 0.12695  236 LYS B CD  
1841 C  CE  . LYS B 236 ? 0.79192 0.63911 0.62529 -0.02245 -0.06601 0.12839  236 LYS B CE  
1842 N  NZ  . LYS B 236 ? 0.92452 0.75272 0.74937 -0.01560 -0.07901 0.12958  236 LYS B NZ  
1843 N  N   . THR B 237 ? 0.65933 0.55784 0.41620 -0.00423 -0.03470 0.12641  237 THR B N   
1844 C  CA  . THR B 237 ? 0.67734 0.57928 0.40898 0.00000  -0.02964 0.13007  237 THR B CA  
1845 C  C   . THR B 237 ? 0.56171 0.47609 0.29110 0.00849  -0.03196 0.11636  237 THR B C   
1846 O  O   . THR B 237 ? 0.59680 0.51127 0.30348 0.01481  -0.03277 0.11666  237 THR B O   
1847 C  CB  . THR B 237 ? 0.77872 0.68946 0.50879 -0.00868 -0.01422 0.13883  237 THR B CB  
1848 O  OG1 . THR B 237 ? 0.65327 0.58181 0.40654 -0.01213 -0.00773 0.13042  237 THR B OG1 
1849 C  CG2 . THR B 237 ? 0.69649 0.59325 0.42795 -0.01767 -0.01146 0.15218  237 THR B CG2 
1850 N  N   . ASN B 238 ? 0.54556 0.46963 0.29708 0.00889  -0.03315 0.10421  238 ASN B N   
1851 C  CA  . ASN B 238 ? 0.56358 0.49768 0.31470 0.01643  -0.03487 0.09047  238 ASN B CA  
1852 C  C   . ASN B 238 ? 0.54247 0.47405 0.31143 0.01921  -0.04474 0.07827  238 ASN B C   
1853 O  O   . ASN B 238 ? 0.53280 0.47346 0.32025 0.01772  -0.04145 0.07001  238 ASN B O   
1854 C  CB  . ASN B 238 ? 0.48149 0.43273 0.23942 0.01427  -0.02236 0.08736  238 ASN B CB  
1855 C  CG  . ASN B 238 ? 0.65684 0.61283 0.39591 0.01239  -0.01236 0.09665  238 ASN B CG  
1856 O  OD1 . ASN B 238 ? 0.82784 0.78273 0.56768 0.00464  -0.00540 0.10774  238 ASN B OD1 
1857 N  ND2 . ASN B 238 ? 0.82636 0.78799 0.54830 0.01900  -0.01116 0.09167  238 ASN B ND2 
1858 N  N   . PRO B 239 ? 0.55407 0.47369 0.31711 0.02385  -0.05696 0.07626  239 PRO B N   
1859 C  CA  . PRO B 239 ? 0.54559 0.46254 0.32696 0.02526  -0.06617 0.06465  239 PRO B CA  
1860 C  C   . PRO B 239 ? 0.65285 0.57969 0.44007 0.03000  -0.06591 0.04920  239 PRO B C   
1861 O  O   . PRO B 239 ? 0.66094 0.58821 0.46659 0.02892  -0.06953 0.03959  239 PRO B O   
1862 C  CB  . PRO B 239 ? 0.73584 0.63897 0.50612 0.03054  -0.07914 0.06598  239 PRO B CB  
1863 C  CG  . PRO B 239 ? 0.60905 0.50622 0.35419 0.03185  -0.07653 0.07969  239 PRO B CG  
1864 C  CD  . PRO B 239 ? 0.66756 0.57669 0.40577 0.02901  -0.06301 0.08340  239 PRO B CD  
1865 N  N   . LYS B 240 ? 0.60282 0.53729 0.37503 0.03484  -0.06126 0.04619  240 LYS B N   
1866 C  CA  . LYS B 240 ? 0.62237 0.56493 0.39960 0.03949  -0.06074 0.03075  240 LYS B CA  
1867 C  C   . LYS B 240 ? 0.69969 0.65245 0.49140 0.03594  -0.04970 0.02801  240 LYS B C   
1868 O  O   . LYS B 240 ? 0.77076 0.72832 0.56913 0.03908  -0.04842 0.01544  240 LYS B O   
1869 C  CB  . LYS B 240 ? 0.56376 0.51028 0.31882 0.04685  -0.06139 0.02699  240 LYS B CB  
1870 C  CG  . LYS B 240 ? 0.62288 0.56027 0.36352 0.05241  -0.07398 0.02735  240 LYS B CG  
1871 N  N   . ILE B 241 ? 0.50151 0.45753 0.29845 0.02970  -0.04178 0.03907  241 ILE B N   
1872 C  CA  . ILE B 241 ? 0.47116 0.43767 0.28248 0.02698  -0.03198 0.03722  241 ILE B CA  
1873 C  C   . ILE B 241 ? 0.50209 0.46514 0.33498 0.02256  -0.03569 0.03478  241 ILE B C   
1874 O  O   . ILE B 241 ? 0.51934 0.48059 0.36028 0.01630  -0.03536 0.04352  241 ILE B O   
1875 C  CB  . ILE B 241 ? 0.71062 0.68492 0.51739 0.02274  -0.02158 0.04878  241 ILE B CB  
1876 C  CG1 . ILE B 241 ? 0.58822 0.56700 0.37306 0.02710  -0.01723 0.04993  241 ILE B CG1 
1877 C  CG2 . ILE B 241 ? 0.57381 0.55938 0.39792 0.02041  -0.01304 0.04678  241 ILE B CG2 
1878 C  CD1 . ILE B 241 ? 0.73166 0.71890 0.51151 0.02246  -0.00618 0.06044  241 ILE B CD1 
1879 N  N   . LYS B 242 ? 0.47713 0.43943 0.31939 0.02547  -0.03872 0.02222  242 LYS B N   
1880 C  CA  . LYS B 242 ? 0.48168 0.43913 0.34165 0.02200  -0.04400 0.01776  242 LYS B CA  
1881 C  C   . LYS B 242 ? 0.40358 0.36592 0.27729 0.02223  -0.03886 0.00984  242 LYS B C   
1882 O  O   . LYS B 242 ? 0.40223 0.36115 0.29013 0.01904  -0.04235 0.00596  242 LYS B O   
1883 C  CB  . LYS B 242 ? 0.54597 0.49408 0.40370 0.02487  -0.05534 0.00917  242 LYS B CB  
1884 C  CG  . LYS B 242 ? 0.88868 0.82874 0.73744 0.02425  -0.06296 0.01733  242 LYS B CG  
1885 C  CD  . LYS B 242 ? 0.75616 0.69463 0.61560 0.01667  -0.06124 0.02833  242 LYS B CD  
1886 C  CE  . LYS B 242 ? 0.99419 0.92124 0.85486 0.01547  -0.07174 0.03071  242 LYS B CE  
1887 N  NZ  . LYS B 242 ? 0.75263 0.67831 0.62940 0.00758  -0.07090 0.03686  242 LYS B NZ  
1888 N  N   . SER B 243 ? 0.38763 0.35719 0.25709 0.02610  -0.03074 0.00717  243 SER B N   
1889 C  CA  . SER B 243 ? 0.37573 0.34758 0.25661 0.02747  -0.02594 -0.00033 243 SER B CA  
1890 C  C   . SER B 243 ? 0.41257 0.39346 0.28840 0.03166  -0.01606 0.00004  243 SER B C   
1891 O  O   . SER B 243 ? 0.41367 0.39836 0.27550 0.03440  -0.01375 0.00193  243 SER B O   
1892 C  CB  . SER B 243 ? 0.41750 0.38153 0.30020 0.03010  -0.03093 -0.01417 243 SER B CB  
1893 O  OG  . SER B 243 ? 0.58385 0.54829 0.45303 0.03558  -0.03094 -0.02083 243 SER B OG  
1894 N  N   . PHE B 244 ? 0.33391 0.31799 0.22082 0.03262  -0.01038 -0.00233 244 PHE B N   
1895 C  CA  . PHE B 244 ? 0.40357 0.39487 0.28845 0.03783  -0.00134 -0.00459 244 PHE B CA  
1896 C  C   . PHE B 244 ? 0.37047 0.35813 0.26706 0.03986  0.00142  -0.01078 244 PHE B C   
1897 O  O   . PHE B 244 ? 0.36329 0.34542 0.26969 0.03627  -0.00262 -0.01108 244 PHE B O   
1898 C  CB  . PHE B 244 ? 0.37543 0.37953 0.26010 0.03666  0.00539  0.00590  244 PHE B CB  
1899 C  CG  . PHE B 244 ? 0.33828 0.34695 0.23689 0.03172  0.00551  0.01347  244 PHE B CG  
1900 C  CD1 . PHE B 244 ? 0.35761 0.37076 0.26806 0.03408  0.00979  0.01220  244 PHE B CD1 
1901 C  CD2 . PHE B 244 ? 0.38291 0.39129 0.28267 0.02503  0.00125  0.02163  244 PHE B CD2 
1902 C  CE1 . PHE B 244 ? 0.37690 0.39597 0.29987 0.02988  0.00937  0.01840  244 PHE B CE1 
1903 C  CE2 . PHE B 244 ? 0.35459 0.36860 0.26809 0.02016  0.00158  0.02739  244 PHE B CE2 
1904 C  CZ  . PHE B 244 ? 0.37216 0.39236 0.29705 0.02271  0.00543  0.02540  244 PHE B CZ  
1905 N  N   . THR B 245 ? 0.35863 0.34915 0.25371 0.04567  0.00869  -0.01545 245 THR B N   
1906 C  CA  . THR B 245 ? 0.33620 0.32017 0.23939 0.04874  0.01191  -0.02213 245 THR B CA  
1907 C  C   . THR B 245 ? 0.40153 0.39419 0.30945 0.05350  0.02023  -0.01822 245 THR B C   
1908 O  O   . THR B 245 ? 0.42191 0.42392 0.32399 0.05688  0.02537  -0.01701 245 THR B O   
1909 C  CB  . THR B 245 ? 0.51261 0.48767 0.40983 0.05223  0.01230  -0.03522 245 THR B CB  
1910 O  OG1 . THR B 245 ? 0.49728 0.46522 0.39216 0.04820  0.00383  -0.03985 245 THR B OG1 
1911 C  CG2 . THR B 245 ? 0.45077 0.41730 0.35535 0.05534  0.01729  -0.04170 245 THR B CG2 
1912 N  N   . ILE B 246 ? 0.32635 0.31638 0.24462 0.05414  0.02148  -0.01658 246 ILE B N   
1913 C  CA  . ILE B 246 ? 0.35945 0.35579 0.28285 0.06042  0.02869  -0.01442 246 ILE B CA  
1914 C  C   . ILE B 246 ? 0.31196 0.29440 0.23727 0.06501  0.03165  -0.02237 246 ILE B C   
1915 O  O   . ILE B 246 ? 0.36696 0.33865 0.29622 0.06175  0.02819  -0.02404 246 ILE B O   
1916 C  CB  . ILE B 246 ? 0.36103 0.36745 0.29449 0.05815  0.02774  -0.00459 246 ILE B CB  
1917 C  CG1 . ILE B 246 ? 0.36539 0.38611 0.29715 0.05385  0.02729  0.00283  246 ILE B CG1 
1918 C  CG2 . ILE B 246 ? 0.36936 0.37952 0.30944 0.06589  0.03362  -0.00357 246 ILE B CG2 
1919 C  CD1 . ILE B 246 ? 0.48498 0.51550 0.42734 0.04900  0.02492  0.01136  246 ILE B CD1 
1920 N  N   . LYS B 247 ? 0.36357 0.34571 0.28627 0.07224  0.03855  -0.02742 247 LYS B N   
1921 C  CA  . LYS B 247 ? 0.38695 0.35385 0.31096 0.07657  0.04244  -0.03516 247 LYS B CA  
1922 C  C   . LYS B 247 ? 0.43028 0.39915 0.36022 0.08435  0.04833  -0.03110 247 LYS B C   
1923 O  O   . LYS B 247 ? 0.40384 0.38633 0.33476 0.08927  0.05223  -0.02787 247 LYS B O   
1924 C  CB  . LYS B 247 ? 0.47716 0.43850 0.39379 0.07927  0.04595  -0.04683 247 LYS B CB  
1925 C  CG  . LYS B 247 ? 0.43275 0.39229 0.34267 0.07325  0.03978  -0.05238 247 LYS B CG  
1926 C  CD  . LYS B 247 ? 0.49758 0.45623 0.39998 0.07685  0.04355  -0.06384 247 LYS B CD  
1927 C  CE  . LYS B 247 ? 0.52835 0.48654 0.42355 0.07195  0.03651  -0.06953 247 LYS B CE  
1928 N  NZ  . LYS B 247 ? 0.60820 0.56031 0.49906 0.07435  0.03919  -0.08452 247 LYS B NZ  
1929 N  N   . LEU B 248 ? 0.37504 0.32996 0.30846 0.08576  0.04918  -0.03170 248 LEU B N   
1930 C  CA  . LEU B 248 ? 0.38393 0.33529 0.32114 0.09461  0.05482  -0.02933 248 LEU B CA  
1931 C  C   . LEU B 248 ? 0.37973 0.31078 0.31363 0.09788  0.06033  -0.03921 248 LEU B C   
1932 O  O   . LEU B 248 ? 0.38041 0.29619 0.31304 0.09264  0.05878  -0.04341 248 LEU B O   
1933 C  CB  . LEU B 248 ? 0.34190 0.29306 0.28469 0.09381  0.05145  -0.02046 248 LEU B CB  
1934 C  CG  . LEU B 248 ? 0.49012 0.46241 0.43893 0.09294  0.04783  -0.01062 248 LEU B CG  
1935 C  CD1 . LEU B 248 ? 0.61115 0.59269 0.55901 0.08341  0.04227  -0.00943 248 LEU B CD1 
1936 C  CD2 . LEU B 248 ? 0.44638 0.41642 0.40009 0.09342  0.04502  -0.00381 248 LEU B CD2 
1937 N  N   . LEU B 249 ? 0.40348 0.33459 0.33651 0.10593  0.06714  -0.04386 249 LEU B N   
1938 C  CA  . LEU B 249 ? 0.37235 0.28426 0.30311 0.10944  0.07360  -0.05400 249 LEU B CA  
1939 C  C   . LEU B 249 ? 0.46967 0.37352 0.40383 0.11956  0.07930  -0.04991 249 LEU B C   
1940 O  O   . LEU B 249 ? 0.47796 0.39622 0.41590 0.12662  0.08018  -0.04360 249 LEU B O   
1941 C  CB  . LEU B 249 ? 0.42813 0.34549 0.35514 0.11131  0.07749  -0.06435 249 LEU B CB  
1942 C  CG  . LEU B 249 ? 0.45590 0.38754 0.37840 0.10386  0.07128  -0.06504 249 LEU B CG  
1943 C  CD1 . LEU B 249 ? 0.59347 0.53501 0.51129 0.10706  0.07519  -0.07286 249 LEU B CD1 
1944 C  CD2 . LEU B 249 ? 0.45441 0.37493 0.37444 0.09526  0.06627  -0.07069 249 LEU B CD2 
1945 N  N   . PHE B 250 ? 0.44991 0.33056 0.38267 0.12060  0.08353  -0.05397 250 PHE B N   
1946 C  CA  . PHE B 250 ? 0.48706 0.35633 0.42147 0.13055  0.08856  -0.04896 250 PHE B CA  
1947 C  C   . PHE B 250 ? 0.42150 0.27178 0.35549 0.13286  0.09600  -0.05890 250 PHE B C   
1948 O  O   . PHE B 250 ? 0.56417 0.40694 0.49825 0.12288  0.09520  -0.06823 250 PHE B O   
1949 C  CB  . PHE B 250 ? 0.44071 0.30005 0.37438 0.12807  0.08518  -0.03999 250 PHE B CB  
1950 C  CG  . PHE B 250 ? 0.39221 0.27154 0.32876 0.12301  0.07651  -0.03064 250 PHE B CG  
1951 C  CD1 . PHE B 250 ? 0.45085 0.34675 0.39195 0.13031  0.07435  -0.02079 250 PHE B CD1 
1952 C  CD2 . PHE B 250 ? 0.42477 0.30609 0.36037 0.11116  0.07063  -0.03235 250 PHE B CD2 
1953 C  CE1 . PHE B 250 ? 0.44573 0.35998 0.39050 0.12503  0.06693  -0.01305 250 PHE B CE1 
1954 C  CE2 . PHE B 250 ? 0.38117 0.27961 0.32014 0.10630  0.06311  -0.02422 250 PHE B CE2 
1955 C  CZ  . PHE B 250 ? 0.46652 0.38128 0.41011 0.11274  0.06148  -0.01469 250 PHE B CZ  
1956 N  N   . ASN B 251 ? 0.45609 0.30508 0.39392 0.14207  0.09967  -0.05616 251 ASN B N   
1957 C  CA  . ASN B 251 ? 0.63245 0.46770 0.57374 0.14069  0.10350  -0.06357 251 ASN B CA  
1958 C  C   . ASN B 251 ? 0.55778 0.37132 0.49704 0.13711  0.10371  -0.05916 251 ASN B C   
1959 O  O   . ASN B 251 ? 0.54033 0.34955 0.47544 0.13424  0.10075  -0.05178 251 ASN B O   
1960 C  CB  . ASN B 251 ? 0.56264 0.40501 0.50891 0.15193  0.10734  -0.06354 251 ASN B CB  
1961 C  CG  . ASN B 251 ? 0.63331 0.47340 0.58024 0.16295  0.10717  -0.05108 251 ASN B CG  
1962 O  OD1 . ASN B 251 ? 0.58899 0.41784 0.53193 0.16217  0.10508  -0.04275 251 ASN B OD1 
1963 N  ND2 . ASN B 251 ? 0.68220 0.53407 0.63448 0.17334  0.10914  -0.05039 251 ASN B ND2 
1964 N  N   . LYS B 252 ? 0.64174 0.44146 0.58352 0.13733  0.10756  -0.06376 252 LYS B N   
1965 C  CA  . LYS B 252 ? 0.62068 0.39913 0.55939 0.13270  0.10891  -0.06082 252 LYS B CA  
1966 C  C   . LYS B 252 ? 0.60556 0.37598 0.53934 0.14092  0.10895  -0.04649 252 LYS B C   
1967 O  O   . LYS B 252 ? 0.66430 0.41909 0.59292 0.13625  0.10939  -0.04184 252 LYS B O   
1968 C  CB  . LYS B 252 ? 0.71634 0.48258 0.65859 0.13220  0.11349  -0.06890 252 LYS B CB  
1969 C  CG  . LYS B 252 ? 0.77647 0.53994 0.72106 0.14522  0.11722  -0.06501 252 LYS B CG  
1970 C  CD  . LYS B 252 ? 0.98970 0.73599 0.93643 0.14461  0.12208  -0.07121 252 LYS B CD  
1971 C  CE  . LYS B 252 ? 1.00593 0.74760 0.95493 0.15814  0.12536  -0.06650 252 LYS B CE  
1972 N  NZ  . LYS B 252 ? 1.19208 0.95466 1.14816 0.16494  0.12488  -0.07212 252 LYS B NZ  
1973 N  N   . ASN B 253 ? 0.63210 0.41445 0.56744 0.15310  0.10820  -0.03964 253 ASN B N   
1974 C  CA  . ASN B 253 ? 0.52972 0.30937 0.46117 0.16230  0.10649  -0.02607 253 ASN B CA  
1975 C  C   . ASN B 253 ? 0.57440 0.36917 0.50406 0.16239  0.10098  -0.01896 253 ASN B C   
1976 O  O   . ASN B 253 ? 0.61224 0.41186 0.54049 0.17119  0.09809  -0.00803 253 ASN B O   
1977 C  CB  . ASN B 253 ? 0.67766 0.46408 0.61374 0.17636  0.10777  -0.02292 253 ASN B CB  
1978 C  CG  . ASN B 253 ? 0.73521 0.50340 0.67246 0.17816  0.11307  -0.02761 253 ASN B CG  
1979 O  OD1 . ASN B 253 ? 0.91575 0.66300 0.84799 0.17166  0.11565  -0.02794 253 ASN B OD1 
1980 N  ND2 . ASN B 253 ? 0.75347 0.53009 0.69779 0.18685  0.11496  -0.03162 253 ASN B ND2 
1981 N  N   . GLY B 254 ? 0.56686 0.37044 0.49706 0.15326  0.09895  -0.02510 254 GLY B N   
1982 C  CA  . GLY B 254 ? 0.51786 0.33579 0.44707 0.15338  0.09389  -0.01893 254 GLY B CA  
1983 C  C   . GLY B 254 ? 0.61280 0.45875 0.54837 0.16074  0.09061  -0.01536 254 GLY B C   
1984 O  O   . GLY B 254 ? 0.50125 0.36549 0.43962 0.15785  0.08337  -0.00761 254 GLY B O   
1985 N  N   . VAL B 255 ? 0.56737 0.41995 0.50666 0.16801  0.09517  -0.02134 255 VAL B N   
1986 C  CA  . VAL B 255 ? 0.42946 0.31103 0.37599 0.17313  0.09232  -0.01873 255 VAL B CA  
1987 C  C   . VAL B 255 ? 0.56352 0.46147 0.51097 0.16300  0.09044  -0.02557 255 VAL B C   
1988 O  O   . VAL B 255 ? 0.45461 0.34232 0.39862 0.15834  0.09432  -0.03591 255 VAL B O   
1989 C  CB  . VAL B 255 ? 0.45022 0.33205 0.40114 0.18621  0.09758  -0.02081 255 VAL B CB  
1990 C  CG1 . VAL B 255 ? 0.51001 0.42240 0.46865 0.19202  0.09639  -0.02006 255 VAL B CG1 
1991 C  CG2 . VAL B 255 ? 0.54510 0.41363 0.49517 0.19370  0.09653  -0.01226 255 VAL B CG2 
1992 N  N   . LEU B 256 ? 0.48088 0.40421 0.43268 0.15954  0.08451  -0.01989 256 LEU B N   
1993 C  CA  . LEU B 256 ? 0.44236 0.38137 0.39370 0.14995  0.08214  -0.02412 256 LEU B CA  
1994 C  C   . LEU B 256 ? 0.44877 0.39386 0.40018 0.15417  0.08822  -0.03320 256 LEU B C   
1995 O  O   . LEU B 256 ? 0.45723 0.41141 0.41371 0.16443  0.09198  -0.03290 256 LEU B O   
1996 C  CB  . LEU B 256 ? 0.49078 0.45524 0.44761 0.14688  0.07609  -0.01555 256 LEU B CB  
1997 C  CG  . LEU B 256 ? 0.44473 0.42366 0.40011 0.13564  0.07233  -0.01660 256 LEU B CG  
1998 C  CD1 . LEU B 256 ? 0.35558 0.32063 0.30585 0.12437  0.06735  -0.01750 256 LEU B CD1 
1999 C  CD2 . LEU B 256 ? 0.43414 0.43891 0.39690 0.13510  0.06883  -0.00855 256 LEU B CD2 
2000 N  N   . LEU B 257 ? 0.39714 0.33860 0.34314 0.14647  0.08890  -0.04179 257 LEU B N   
2001 C  CA  . LEU B 257 ? 0.42283 0.37129 0.36758 0.14928  0.09435  -0.05132 257 LEU B CA  
2002 C  C   . LEU B 257 ? 0.54785 0.52310 0.49313 0.14575  0.09203  -0.04857 257 LEU B C   
2003 O  O   . LEU B 257 ? 0.49719 0.48173 0.44152 0.13757  0.08578  -0.04202 257 LEU B O   
2004 C  CB  . LEU B 257 ? 0.49362 0.42672 0.43174 0.14305  0.09606  -0.06283 257 LEU B CB  
2005 C  CG  . LEU B 257 ? 0.46847 0.37399 0.40607 0.14601  0.10085  -0.06824 257 LEU B CG  
2006 C  CD1 . LEU B 257 ? 0.52462 0.41788 0.45757 0.13641  0.10035  -0.07915 257 LEU B CD1 
2007 C  CD2 . LEU B 257 ? 0.61370 0.51704 0.55722 0.15471  0.10698  -0.07229 257 LEU B CD2 
2008 N  N   . ASP B 258 ? 0.49246 0.47961 0.43905 0.15158  0.09772  -0.05417 258 ASP B N   
2009 C  CA  . ASP B 258 ? 0.46943 0.48218 0.41632 0.14856  0.09703  -0.05126 258 ASP B CA  
2010 C  C   . ASP B 258 ? 0.42968 0.44613 0.36706 0.13754  0.09352  -0.05339 258 ASP B C   
2011 O  O   . ASP B 258 ? 0.58638 0.62125 0.52254 0.13269  0.09170  -0.04817 258 ASP B O   
2012 C  CB  . ASP B 258 ? 0.59632 0.62123 0.54679 0.15742  0.10469  -0.05778 258 ASP B CB  
2013 C  CG  . ASP B 258 ? 0.88017 0.90851 0.84142 0.16914  0.10706  -0.05390 258 ASP B CG  
2014 O  OD1 . ASP B 258 ? 0.94695 0.99286 0.91460 0.16944  0.10416  -0.04551 258 ASP B OD1 
2015 O  OD2 . ASP B 258 ? 1.12163 1.13514 1.08524 0.17830  0.11179  -0.05954 258 ASP B OD2 
2016 N  N   . ASN B 259 ? 0.48730 0.48718 0.41785 0.13358  0.09267  -0.06112 259 ASN B N   
2017 C  CA  . ASN B 259 ? 0.57084 0.57501 0.49215 0.12417  0.08812  -0.06261 259 ASN B CA  
2018 C  C   . ASN B 259 ? 0.54648 0.54685 0.46747 0.11571  0.07972  -0.05417 259 ASN B C   
2019 O  O   . ASN B 259 ? 0.55550 0.55644 0.46904 0.10822  0.07487  -0.05512 259 ASN B O   
2020 C  CB  . ASN B 259 ? 0.69354 0.68516 0.60803 0.12334  0.09005  -0.07594 259 ASN B CB  
2021 C  CG  . ASN B 259 ? 0.74926 0.71836 0.66795 0.12647  0.09243  -0.08153 259 ASN B CG  
2022 O  OD1 . ASN B 259 ? 0.90978 0.87315 0.83567 0.13318  0.09561  -0.07755 259 ASN B OD1 
2023 N  ND2 . ASN B 259 ? 0.95095 0.90695 0.86496 0.12175  0.09104  -0.09101 259 ASN B ND2 
2024 N  N   . SER B 260 ? 0.45596 0.45310 0.38470 0.11720  0.07774  -0.04620 260 SER B N   
2025 C  CA  . SER B 260 ? 0.43463 0.43149 0.36456 0.10927  0.07010  -0.03791 260 SER B CA  
2026 C  C   . SER B 260 ? 0.43737 0.45469 0.36709 0.10433  0.06755  -0.03015 260 SER B C   
2027 O  O   . SER B 260 ? 0.42398 0.45733 0.35593 0.10831  0.07211  -0.02864 260 SER B O   
2028 C  CB  . SER B 260 ? 0.37081 0.36138 0.30875 0.11295  0.06922  -0.03157 260 SER B CB  
2029 O  OG  . SER B 260 ? 0.48505 0.45474 0.42232 0.11725  0.07249  -0.03773 260 SER B OG  
2030 N  N   . ASN B 261 ? 0.37924 0.39586 0.30709 0.09542  0.06057  -0.02525 261 ASN B N   
2031 C  CA  . ASN B 261 ? 0.40622 0.44029 0.33446 0.09017  0.05873  -0.01717 261 ASN B CA  
2032 C  C   . ASN B 261 ? 0.38322 0.43034 0.32283 0.09312  0.06002  -0.00963 261 ASN B C   
2033 O  O   . ASN B 261 ? 0.39013 0.45532 0.33214 0.09186  0.06237  -0.00523 261 ASN B O   
2034 C  CB  . ASN B 261 ? 0.37497 0.40413 0.29936 0.08043  0.05094  -0.01371 261 ASN B CB  
2035 C  CG  . ASN B 261 ? 0.43080 0.45123 0.34359 0.07790  0.04889  -0.02099 261 ASN B CG  
2036 O  OD1 . ASN B 261 ? 0.40265 0.40807 0.31393 0.07834  0.04706  -0.02842 261 ASN B OD1 
2037 N  ND2 . ASN B 261 ? 0.45420 0.48438 0.35836 0.07512  0.04927  -0.01909 261 ASN B ND2 
2038 N  N   . LEU B 262 ? 0.40481 0.44345 0.35119 0.09695  0.05864  -0.00835 262 LEU B N   
2039 C  CA  . LEU B 262 ? 0.37284 0.42386 0.32992 0.10122  0.05906  -0.00200 262 LEU B CA  
2040 C  C   . LEU B 262 ? 0.45338 0.51072 0.41386 0.11246  0.06602  -0.00545 262 LEU B C   
2041 O  O   . LEU B 262 ? 0.41830 0.46168 0.37493 0.11856  0.06963  -0.01221 262 LEU B O   
2042 C  CB  . LEU B 262 ? 0.34919 0.38781 0.31015 0.10141  0.05454  0.00090  262 LEU B CB  
2043 C  CG  . LEU B 262 ? 0.37793 0.42786 0.34904 0.10684  0.05378  0.00715  262 LEU B CG  
2044 C  CD1 . LEU B 262 ? 0.40784 0.47938 0.38589 0.10007  0.05100  0.01328  262 LEU B CD1 
2045 C  CD2 . LEU B 262 ? 0.41883 0.45255 0.39010 0.10702  0.04975  0.00914  262 LEU B CD2 
2046 N  N   . GLY B 263 ? 0.41109 0.48982 0.37972 0.11515  0.06814  -0.00155 263 GLY B N   
2047 C  CA  . GLY B 263 ? 0.33732 0.42461 0.31075 0.12635  0.07458  -0.00534 263 GLY B CA  
2048 C  C   . GLY B 263 ? 0.42854 0.50835 0.40846 0.13658  0.07376  -0.00369 263 GLY B C   
2049 O  O   . GLY B 263 ? 0.43587 0.51776 0.42095 0.13540  0.06867  0.00268  263 GLY B O   
2050 N  N   . LYS B 264 ? 0.40727 0.63220 0.55212 0.14607  0.10573  -0.04919 264 LYS B N   
2051 C  CA  . LYS B 264 ? 0.44212 0.65800 0.58426 0.16277  0.10290  -0.04503 264 LYS B CA  
2052 C  C   . LYS B 264 ? 0.52899 0.76426 0.68005 0.17296  0.09408  -0.04186 264 LYS B C   
2053 O  O   . LYS B 264 ? 0.41694 0.64568 0.56183 0.18502  0.08947  -0.03567 264 LYS B O   
2054 C  CB  . LYS B 264 ? 0.51089 0.71393 0.65868 0.16905  0.10764  -0.04931 264 LYS B CB  
2055 C  CG  . LYS B 264 ? 0.67468 0.85347 0.81144 0.16323  0.11500  -0.05121 264 LYS B CG  
2056 C  CD  . LYS B 264 ? 0.73861 0.90688 0.88221 0.17035  0.11842  -0.05550 264 LYS B CD  
2057 C  CE  . LYS B 264 ? 0.73951 0.90451 0.88490 0.18778  0.11322  -0.05087 264 LYS B CE  
2058 N  NZ  . LYS B 264 ? 0.66524 0.81247 0.79329 0.19421  0.11066  -0.04247 264 LYS B NZ  
2059 N  N   . ALA B 265 ? 0.36198 0.61924 0.52710 0.16838  0.09143  -0.04565 265 ALA B N   
2060 C  CA  . ALA B 265 ? 0.33382 0.60971 0.50867 0.17740  0.08276  -0.04335 265 ALA B CA  
2061 C  C   . ALA B 265 ? 0.42580 0.70902 0.59232 0.17702  0.07614  -0.03686 265 ALA B C   
2062 O  O   . ALA B 265 ? 0.40523 0.70007 0.57684 0.18612  0.06798  -0.03329 265 ALA B O   
2063 C  CB  . ALA B 265 ? 0.45528 0.75125 0.64565 0.17087  0.08212  -0.04882 265 ALA B CB  
2064 N  N   . TYR B 266 ? 0.37392 0.64957 0.52757 0.16662  0.07939  -0.03504 266 TYR B N   
2065 C  CA  . TYR B 266 ? 0.45445 0.73820 0.60031 0.16293  0.07418  -0.02940 266 TYR B CA  
2066 C  C   . TYR B 266 ? 0.48787 0.74260 0.61362 0.16375  0.07258  -0.02166 266 TYR B C   
2067 O  O   . TYR B 266 ? 0.44787 0.70041 0.56288 0.15648  0.06784  -0.01622 266 TYR B O   
2068 C  CB  . TYR B 266 ? 0.31466 0.60520 0.45848 0.14419  0.07682  -0.03247 266 TYR B CB  
2069 C  CG  . TYR B 266 ? 0.33006 0.63748 0.48835 0.13766  0.07573  -0.03830 266 TYR B CG  
2070 C  CD1 . TYR B 266 ? 0.42127 0.74966 0.58849 0.13931  0.06800  -0.03738 266 TYR B CD1 
2071 C  CD2 . TYR B 266 ? 0.36308 0.66377 0.52519 0.12993  0.08253  -0.04420 266 TYR B CD2 
2072 C  CE1 . TYR B 266 ? 0.50166 0.84324 0.68070 0.13365  0.06750  -0.04234 266 TYR B CE1 
2073 C  CE2 . TYR B 266 ? 0.47735 0.79111 0.65101 0.12475  0.08194  -0.04847 266 TYR B CE2 
2074 C  CZ  . TYR B 266 ? 0.54182 0.87575 0.72365 0.12663  0.07461  -0.04764 266 TYR B CZ  
2075 O  OH  . TYR B 266 ? 0.49240 0.83776 0.68457 0.12151  0.07446  -0.05176 266 TYR B OH  
2076 N  N   . TRP B 267 ? 0.32116 0.55252 0.44120 0.17189  0.07615  -0.02098 267 TRP B N   
2077 C  CA  . TRP B 267 ? 0.36064 0.56074 0.46066 0.17156  0.07619  -0.01445 267 TRP B CA  
2078 C  C   . TRP B 267 ? 0.43703 0.62335 0.53553 0.18670  0.07126  -0.01015 267 TRP B C   
2079 O  O   . TRP B 267 ? 0.41603 0.59811 0.52214 0.19592  0.07525  -0.01393 267 TRP B O   
2080 C  CB  . TRP B 267 ? 0.38410 0.56672 0.47714 0.16519  0.08680  -0.01830 267 TRP B CB  
2081 C  CG  . TRP B 267 ? 0.35616 0.50689 0.42934 0.16339  0.08865  -0.01296 267 TRP B CG  
2082 C  CD1 . TRP B 267 ? 0.38406 0.51032 0.45089 0.17032  0.09353  -0.01294 267 TRP B CD1 
2083 C  CD2 . TRP B 267 ? 0.29734 0.43658 0.35424 0.15359  0.08623  -0.00716 267 TRP B CD2 
2084 N  NE1 . TRP B 267 ? 0.41639 0.51683 0.46406 0.16541  0.09433  -0.00758 267 TRP B NE1 
2085 C  CE2 . TRP B 267 ? 0.41685 0.52452 0.45809 0.15505  0.08999  -0.00399 267 TRP B CE2 
2086 C  CE3 . TRP B 267 ? 0.29191 0.44436 0.34603 0.14351  0.08159  -0.00456 267 TRP B CE3 
2087 C  CZ2 . TRP B 267 ? 0.41268 0.50173 0.43579 0.14686  0.08917  0.00165  267 TRP B CZ2 
2088 C  CZ3 . TRP B 267 ? 0.30687 0.44068 0.34289 0.13565  0.08050  0.00130  267 TRP B CZ3 
2089 C  CH2 . TRP B 267 ? 0.36742 0.47005 0.38834 0.13718  0.08444  0.00417  267 TRP B CH2 
2090 N  N   . ASN B 268 ? 0.36334 0.54248 0.45194 0.18934  0.06259  -0.00227 268 ASN B N   
2091 C  CA  . ASN B 268 ? 0.34667 0.51652 0.43539 0.20409  0.05652  0.00194  268 ASN B CA  
2092 C  C   . ASN B 268 ? 0.36096 0.51122 0.43093 0.20364  0.04987  0.01125  268 ASN B C   
2093 O  O   . ASN B 268 ? 0.42487 0.57504 0.48515 0.19240  0.04858  0.01414  268 ASN B O   
2094 C  CB  . ASN B 268 ? 0.34511 0.54310 0.45273 0.21224  0.04977  -0.00014 268 ASN B CB  
2095 N  N   . PHE B 269 ? 0.39835 0.53219 0.46337 0.21602  0.04555  0.01591  269 PHE B N   
2096 C  CA  . PHE B 269 ? 0.38488 0.50311 0.43361 0.21695  0.03775  0.02496  269 PHE B CA  
2097 C  C   . PHE B 269 ? 0.56684 0.70945 0.62333 0.21777  0.02748  0.02753  269 PHE B C   
2098 O  O   . PHE B 269 ? 0.47705 0.64309 0.55169 0.22439  0.02458  0.02366  269 PHE B O   
2099 C  CB  . PHE B 269 ? 0.42312 0.51653 0.46410 0.23025  0.03590  0.02928  269 PHE B CB  
2100 C  CG  . PHE B 269 ? 0.56332 0.62781 0.59203 0.22868  0.04514  0.02851  269 PHE B CG  
2101 C  CD1 . PHE B 269 ? 0.54898 0.58951 0.55708 0.22068  0.04662  0.03363  269 PHE B CD1 
2102 C  CD2 . PHE B 269 ? 0.59416 0.65535 0.63201 0.23507  0.05246  0.02254  269 PHE B CD2 
2103 C  CE1 . PHE B 269 ? 0.60420 0.61823 0.60126 0.21913  0.05523  0.03269  269 PHE B CE1 
2104 C  CE2 . PHE B 269 ? 0.64811 0.68281 0.67478 0.23358  0.06101  0.02169  269 PHE B CE2 
2105 C  CZ  . PHE B 269 ? 0.55925 0.57042 0.56558 0.22561  0.06239  0.02673  269 PHE B CZ  
2106 N  N   . ARG B 270 ? 0.41883 0.55606 0.46163 0.21077  0.02208  0.03394  270 ARG B N   
2107 C  CA  . ARG B 270 ? 0.54863 0.70664 0.59662 0.21127  0.01190  0.03716  270 ARG B CA  
2108 C  C   . ARG B 270 ? 0.65624 0.80955 0.70534 0.22638  0.00323  0.04190  270 ARG B C   
2109 O  O   . ARG B 270 ? 0.70202 0.82842 0.73810 0.23291  0.00301  0.04653  270 ARG B O   
2110 C  CB  . ARG B 270 ? 0.50859 0.66043 0.54064 0.19936  0.00889  0.04277  270 ARG B CB  
2111 C  CG  . ARG B 270 ? 0.59937 0.77388 0.63671 0.19834  -0.00120 0.04574  270 ARG B CG  
2112 C  CD  . ARG B 270 ? 0.45094 0.62329 0.47462 0.18475  -0.00320 0.05008  270 ARG B CD  
2113 N  NE  . ARG B 270 ? 0.74537 0.93854 0.77425 0.18542  -0.01340 0.05316  270 ARG B NE  
2114 C  CZ  . ARG B 270 ? 0.82695 1.02456 0.84744 0.17522  -0.01730 0.05693  270 ARG B CZ  
2115 N  NH1 . ARG B 270 ? 0.75443 0.93722 0.76081 0.16321  -0.01198 0.05821  270 ARG B NH1 
2116 N  NH2 . ARG B 270 ? 0.72740 0.94462 0.75391 0.17703  -0.02662 0.05933  270 ARG B NH2 
2117 N  N   . SER B 271 ? 0.91556 1.09516 0.98042 0.23196  -0.00390 0.04062  271 SER B N   
2118 C  CA  . SER B 271 ? 1.15014 1.32863 1.21793 0.24643  -0.01302 0.04488  271 SER B CA  
2119 C  C   . SER B 271 ? 1.18107 1.35533 1.23588 0.24495  -0.02311 0.05335  271 SER B C   
2120 O  O   . SER B 271 ? 1.21162 1.40443 1.26866 0.23635  -0.02684 0.05370  271 SER B O   
2121 C  CB  . SER B 271 ? 1.23584 1.44484 1.32789 0.25397  -0.01589 0.03906  271 SER B CB  
2122 O  OG  . SER B 271 ? 1.31042 1.52080 1.40580 0.26728  -0.02582 0.04343  271 SER B OG  
2123 N  N   . GLU B 281 ? 0.88799 0.93437 0.96038 0.27023  0.07199  0.00487  281 GLU B N   
2124 C  CA  . GLU B 281 ? 0.82646 0.88294 0.89857 0.25498  0.07784  0.00070  281 GLU B CA  
2125 C  C   . GLU B 281 ? 1.00054 1.02920 1.05446 0.24663  0.08555  0.00180  281 GLU B C   
2126 O  O   . GLU B 281 ? 0.81847 0.85103 0.86811 0.23323  0.08948  -0.00002 281 GLU B O   
2127 C  CB  . GLU B 281 ? 0.89410 0.97378 0.98618 0.25419  0.08407  -0.00889 281 GLU B CB  
2128 C  CG  . GLU B 281 ? 0.94775 1.01206 1.04235 0.25592  0.09111  -0.01394 281 GLU B CG  
2129 C  CD  . GLU B 281 ? 0.93304 1.01869 1.04668 0.25023  0.09533  -0.02355 281 GLU B CD  
2130 O  OE1 . GLU B 281 ? 0.91505 0.99097 1.03288 0.25026  0.10008  -0.02836 281 GLU B OE1 
2131 O  OE2 . GLU B 281 ? 0.81093 0.92280 0.93515 0.24520  0.09369  -0.02630 281 GLU B OE2 
2132 N  N   . LYS B 282 ? 0.90768 0.90853 0.95121 0.25450  0.08775  0.00462  282 LYS B N   
2133 C  CA  . LYS B 282 ? 0.79146 0.76423 0.81729 0.24747  0.09488  0.00590  282 LYS B CA  
2134 C  C   . LYS B 282 ? 0.87869 0.84183 0.88726 0.23843  0.09009  0.01299  282 LYS B C   
2135 O  O   . LYS B 282 ? 0.69463 0.66134 0.69994 0.24218  0.08049  0.01922  282 LYS B O   
2136 C  CB  . LYS B 282 ? 0.68615 0.63210 0.70445 0.25470  0.09596  0.00764  282 LYS B CB  
2137 N  N   . ALA B 283 ? 0.63901 0.58955 0.63643 0.22642  0.09693  0.01193  283 ALA B N   
2138 C  CA  . ALA B 283 ? 0.49123 0.43480 0.47351 0.21629  0.09323  0.01774  283 ALA B CA  
2139 C  C   . ALA B 283 ? 0.57561 0.49524 0.54256 0.20642  0.10151  0.01737  283 ALA B C   
2140 O  O   . ALA B 283 ? 0.50125 0.42639 0.46433 0.19337  0.10340  0.01654  283 ALA B O   
2141 C  CB  . ALA B 283 ? 0.63863 0.61248 0.63095 0.20753  0.08936  0.01594  283 ALA B CB  
2142 N  N   . ILE B 284 ? 0.49576 0.38849 0.45376 0.21255  0.10636  0.01807  284 ILE B N   
2143 C  CA  . ILE B 284 ? 0.53763 0.40614 0.48096 0.20387  0.11440  0.01761  284 ILE B CA  
2144 C  C   . ILE B 284 ? 0.58030 0.43702 0.50632 0.19540  0.11011  0.02455  284 ILE B C   
2145 O  O   . ILE B 284 ? 0.62830 0.47573 0.54526 0.18370  0.11548  0.02355  284 ILE B O   
2146 C  CB  . ILE B 284 ? 0.56946 0.41518 0.50727 0.20689  0.11651  0.01737  284 ILE B CB  
2147 C  CG1 . ILE B 284 ? 0.88738 0.74762 0.84325 0.21073  0.11827  0.01030  284 ILE B CG1 
2148 C  CG2 . ILE B 284 ? 0.61427 0.44079 0.53946 0.19320  0.12244  0.01626  284 ILE B CG2 
2149 C  CD1 . ILE B 284 ? 0.87905 0.72007 0.83103 0.21217  0.11969  0.00958  284 ILE B CD1 
2150 N  N   . GLY B 285 ? 0.54481 0.40149 0.46598 0.20112  0.10042  0.03159  285 GLY B N   
2151 C  CA  . GLY B 285 ? 0.51321 0.35910 0.41801 0.19350  0.09593  0.03835  285 GLY B CA  
2152 C  C   . GLY B 285 ? 0.45898 0.32562 0.36722 0.18028  0.09460  0.03706  285 GLY B C   
2153 O  O   . GLY B 285 ? 0.50376 0.36095 0.39825 0.17200  0.09236  0.04183  285 GLY B O   
2154 N  N   . PHE B 286 ? 0.45599 0.35041 0.38204 0.17808  0.09594  0.03076  286 PHE B N   
2155 C  CA  . PHE B 286 ? 0.46759 0.38263 0.39797 0.16530  0.09545  0.02878  286 PHE B CA  
2156 C  C   . PHE B 286 ? 0.44114 0.35444 0.37253 0.15474  0.10555  0.02230  286 PHE B C   
2157 O  O   . PHE B 286 ? 0.45159 0.38067 0.38620 0.14350  0.10606  0.02021  286 PHE B O   
2158 C  CB  . PHE B 286 ? 0.43388 0.38241 0.38320 0.16891  0.08979  0.02618  286 PHE B CB  
2159 C  CG  . PHE B 286 ? 0.43500 0.38944 0.38319 0.17622  0.07868  0.03285  286 PHE B CG  
2160 C  CD1 . PHE B 286 ? 0.43926 0.38710 0.38968 0.19081  0.07466  0.03525  286 PHE B CD1 
2161 C  CD2 . PHE B 286 ? 0.44495 0.41081 0.38932 0.16840  0.07220  0.03684  286 PHE B CD2 
2162 C  CE1 . PHE B 286 ? 0.52803 0.48072 0.47683 0.19750  0.06406  0.04160  286 PHE B CE1 
2163 C  CE2 . PHE B 286 ? 0.47522 0.44650 0.41826 0.17485  0.06189  0.04294  286 PHE B CE2 
2164 C  CZ  . PHE B 286 ? 0.44439 0.40901 0.38950 0.18940  0.05769  0.04537  286 PHE B CZ  
2165 N  N   . MET B 287 ? 0.47040 0.29322 0.37954 0.08108  0.06370  -0.01529 287 MET B N   
2166 C  CA  . MET B 287 ? 0.42104 0.23979 0.32317 0.07100  0.06281  -0.02286 287 MET B CA  
2167 C  C   . MET B 287 ? 0.46176 0.27992 0.36522 0.06001  0.05594  -0.02586 287 MET B C   
2168 O  O   . MET B 287 ? 0.43321 0.24437 0.33764 0.05993  0.05526  -0.02452 287 MET B O   
2169 C  CB  . MET B 287 ? 0.46224 0.25907 0.34958 0.07217  0.07292  -0.02896 287 MET B CB  
2170 C  CG  . MET B 287 ? 0.45838 0.25660 0.34385 0.08225  0.08033  -0.02733 287 MET B CG  
2171 S  SD  . MET B 287 ? 0.47934 0.30112 0.37123 0.07920  0.07520  -0.02691 287 MET B SD  
2172 C  CE  . MET B 287 ? 0.44200 0.28680 0.35005 0.08899  0.07089  -0.01646 287 MET B CE  
2173 N  N   . PRO B 288 ? 0.38940 0.21539 0.29303 0.05083  0.05087  -0.02965 288 PRO B N   
2174 C  CA  . PRO B 288 ? 0.37472 0.20151 0.28036 0.04098  0.04455  -0.03233 288 PRO B CA  
2175 C  C   . PRO B 288 ? 0.47290 0.27900 0.36634 0.03600  0.04974  -0.03892 288 PRO B C   
2176 O  O   . PRO B 288 ? 0.48363 0.27754 0.36529 0.03477  0.05635  -0.04423 288 PRO B O   
2177 C  CB  . PRO B 288 ? 0.41822 0.25869 0.32611 0.03394  0.03891  -0.03408 288 PRO B CB  
2178 C  CG  . PRO B 288 ? 0.42983 0.28148 0.34129 0.04073  0.04009  -0.02999 288 PRO B CG  
2179 C  CD  . PRO B 288 ? 0.38607 0.22346 0.28975 0.04937  0.04979  -0.03050 288 PRO B CD  
2180 N  N   . ASN B 289 ? 0.44500 0.24724 0.34104 0.03255  0.04699  -0.03881 289 ASN B N   
2181 C  CA  . ASN B 289 ? 0.48825 0.27069 0.37327 0.02754  0.05189  -0.04449 289 ASN B CA  
2182 C  C   . ASN B 289 ? 0.44661 0.22528 0.32230 0.01669  0.05234  -0.05272 289 ASN B C   
2183 O  O   . ASN B 289 ? 0.45944 0.25246 0.34075 0.00937  0.04500  -0.05380 289 ASN B O   
2184 C  CB  . ASN B 289 ? 0.50528 0.28932 0.39700 0.02454  0.04716  -0.04256 289 ASN B CB  
2185 C  CG  . ASN B 289 ? 0.54331 0.30664 0.42399 0.02002  0.05260  -0.04749 289 ASN B CG  
2186 O  OD1 . ASN B 289 ? 0.53160 0.29033 0.40561 0.00981  0.05249  -0.05445 289 ASN B OD1 
2187 N  ND2 . ASN B 289 ? 0.54886 0.29966 0.42692 0.02741  0.05767  -0.04379 289 ASN B ND2 
2188 N  N   . LEU B 290 ? 0.51001 0.26900 0.37089 0.01552  0.06138  -0.05852 290 LEU B N   
2189 C  CA  . LEU B 290 ? 0.50221 0.25763 0.35251 0.00455  0.06271  -0.06689 290 LEU B CA  
2190 C  C   . LEU B 290 ? 0.52875 0.28234 0.37689 -0.00720 0.05933  -0.07188 290 LEU B C   
2191 O  O   . LEU B 290 ? 0.58124 0.34102 0.42522 -0.01734 0.05677  -0.07732 290 LEU B O   
2192 C  CB  . LEU B 290 ? 0.56347 0.29726 0.39768 0.00621  0.07437  -0.07224 290 LEU B CB  
2193 C  CG  . LEU B 290 ? 0.53032 0.27018 0.36500 0.01391  0.07720  -0.07001 290 LEU B CG  
2194 C  CD1 . LEU B 290 ? 0.66596 0.38217 0.48655 0.01945  0.09026  -0.07360 290 LEU B CD1 
2195 C  CD2 . LEU B 290 ? 0.55141 0.30733 0.38577 0.00528  0.07194  -0.07341 290 LEU B CD2 
2196 N  N   . VAL B 291 ? 0.57740 0.32354 0.42792 -0.00649 0.05934  -0.07022 291 VAL B N   
2197 C  CA  . VAL B 291 ? 0.53893 0.28735 0.38962 -0.01776 0.05517  -0.07455 291 VAL B CA  
2198 C  C   . VAL B 291 ? 0.55517 0.32835 0.42191 -0.01965 0.04400  -0.07041 291 VAL B C   
2199 O  O   . VAL B 291 ? 0.49669 0.27999 0.36460 -0.02932 0.03910  -0.07421 291 VAL B O   
2200 C  CB  . VAL B 291 ? 0.50095 0.23154 0.34715 -0.01744 0.05976  -0.07487 291 VAL B CB  
2201 C  CG1 . VAL B 291 ? 0.62683 0.36327 0.47576 -0.02869 0.05461  -0.07862 291 VAL B CG1 
2202 C  CG2 . VAL B 291 ? 0.57429 0.28353 0.40538 -0.01763 0.07024  -0.07888 291 VAL B CG2 
2203 N  N   . ALA B 292 ? 0.48512 0.26883 0.36430 -0.01057 0.04006  -0.06255 292 ALA B N   
2204 C  CA  . ALA B 292 ? 0.41093 0.21640 0.30466 -0.01207 0.03043  -0.05868 292 ALA B CA  
2205 C  C   . ALA B 292 ? 0.45969 0.27878 0.35417 -0.01491 0.02679  -0.05939 292 ALA B C   
2206 O  O   . ALA B 292 ? 0.41991 0.25370 0.32130 -0.02071 0.01983  -0.05945 292 ALA B O   
2207 C  CB  . ALA B 292 ? 0.44573 0.25845 0.35111 -0.00254 0.02794  -0.05063 292 ALA B CB  
2208 N  N   . TYR B 293 ? 0.43646 0.25107 0.32391 -0.01063 0.03161  -0.05966 293 TYR B N   
2209 C  CA  . TYR B 293 ? 0.39809 0.22562 0.28589 -0.01207 0.02868  -0.05934 293 TYR B CA  
2210 C  C   . TYR B 293 ? 0.44938 0.26420 0.32118 -0.01559 0.03622  -0.06609 293 TYR B C   
2211 O  O   . TYR B 293 ? 0.44874 0.25649 0.31554 -0.00875 0.04229  -0.06535 293 TYR B O   
2212 C  CB  . TYR B 293 ? 0.41037 0.24822 0.30747 -0.00250 0.02682  -0.05193 293 TYR B CB  
2213 C  CG  . TYR B 293 ? 0.39235 0.23637 0.30252 0.00286  0.02280  -0.04558 293 TYR B CG  
2214 C  CD1 . TYR B 293 ? 0.38412 0.23962 0.30456 -0.00157 0.01533  -0.04391 293 TYR B CD1 
2215 C  CD2 . TYR B 293 ? 0.35640 0.19613 0.26886 0.01235  0.02653  -0.04108 293 TYR B CD2 
2216 C  CE1 . TYR B 293 ? 0.38140 0.24216 0.31290 0.00243  0.01223  -0.03882 293 TYR B CE1 
2217 C  CE2 . TYR B 293 ? 0.36300 0.20960 0.28674 0.01615  0.02279  -0.03553 293 TYR B CE2 
2218 C  CZ  . TYR B 293 ? 0.39482 0.25135 0.32760 0.01077  0.01584  -0.03479 293 TYR B CZ  
2219 O  OH  . TYR B 293 ? 0.35439 0.21713 0.29742 0.01383  0.01281  -0.02995 293 TYR B OH  
2220 N  N   . PRO B 294 ? 0.53429 0.34641 0.39761 -0.02651 0.03640  -0.07302 294 PRO B N   
2221 C  CA  . PRO B 294 ? 0.55754 0.35566 0.40399 -0.03133 0.04454  -0.08056 294 PRO B CA  
2222 C  C   . PRO B 294 ? 0.50175 0.31009 0.34517 -0.03189 0.04389  -0.08071 294 PRO B C   
2223 O  O   . PRO B 294 ? 0.50269 0.33090 0.35531 -0.03281 0.03573  -0.07650 294 PRO B O   
2224 C  CB  . PRO B 294 ? 0.53727 0.33376 0.37716 -0.04443 0.04341  -0.08761 294 PRO B CB  
2225 C  CG  . PRO B 294 ? 0.56447 0.36638 0.41633 -0.04390 0.03769  -0.08397 294 PRO B CG  
2226 C  CD  . PRO B 294 ? 0.47508 0.29283 0.34283 -0.03460 0.03102  -0.07487 294 PRO B CD  
2227 N  N   . LYS B 295 ? 0.48598 0.27938 0.31536 -0.03172 0.05323  -0.08593 295 LYS B N   
2228 C  CA  . LYS B 295 ? 0.58562 0.38625 0.40968 -0.03286 0.05428  -0.08721 295 LYS B CA  
2229 C  C   . LYS B 295 ? 0.51934 0.33364 0.33949 -0.04593 0.04847  -0.09134 295 LYS B C   
2230 O  O   . LYS B 295 ? 0.60757 0.42139 0.42575 -0.05469 0.04625  -0.09519 295 LYS B O   
2231 C  CB  . LYS B 295 ? 0.61341 0.39265 0.42238 -0.03033 0.06680  -0.09292 295 LYS B CB  
2232 C  CG  . LYS B 295 ? 0.83853 0.60919 0.65244 -0.01559 0.07218  -0.08732 295 LYS B CG  
2233 C  CD  . LYS B 295 ? 0.90466 0.68987 0.72486 -0.00857 0.07044  -0.08223 295 LYS B CD  
2234 C  CE  . LYS B 295 ? 0.85425 0.63247 0.65968 -0.01253 0.07825  -0.08918 295 LYS B CE  
2235 N  NZ  . LYS B 295 ? 0.87213 0.66251 0.68194 -0.00573 0.07825  -0.08501 295 LYS B NZ  
2236 N  N   . PRO B 296 ? 0.58793 0.41600 0.40726 -0.04750 0.04566  -0.09016 296 PRO B N   
2237 C  CA  . PRO B 296 ? 0.65947 0.50421 0.47674 -0.05913 0.03875  -0.09229 296 PRO B CA  
2238 C  C   . PRO B 296 ? 0.69022 0.52426 0.49188 -0.07171 0.04386  -0.10255 296 PRO B C   
2239 O  O   . PRO B 296 ? 0.71137 0.52587 0.49887 -0.07278 0.05433  -0.10931 296 PRO B O   
2240 C  CB  . PRO B 296 ? 0.84901 0.70444 0.66391 -0.05782 0.03815  -0.09019 296 PRO B CB  
2241 C  CG  . PRO B 296 ? 0.60341 0.45559 0.42683 -0.04414 0.04045  -0.08373 296 PRO B CG  
2242 C  CD  . PRO B 296 ? 0.72745 0.55764 0.54753 -0.03898 0.04864  -0.08659 296 PRO B CD  
2243 N  N   . SER B 297 ? 0.98472 0.83180 0.78925 -0.08121 0.03670  -0.10365 297 SER B N   
2244 C  CA  . SER B 297 ? 1.06291 0.90405 0.85456 -0.09493 0.03983  -0.11309 297 SER B CA  
2245 C  C   . SER B 297 ? 1.25008 1.06198 1.02774 -0.09572 0.05222  -0.12085 297 SER B C   
2246 O  O   . SER B 297 ? 1.29130 1.09028 1.07366 -0.08968 0.05462  -0.11915 297 SER B O   
2247 C  CB  . SER B 297 ? 1.09035 0.94422 0.87142 -0.10596 0.03842  -0.11745 297 SER B CB  
2248 O  OG  . SER B 297 ? 1.10468 0.98525 0.89793 -0.10538 0.02701  -0.10976 297 SER B OG  
2249 N  N   . LYS B 300 ? 0.65545 0.61010 0.50629 -0.10780 -0.01139 -0.08863 300 LYS B N   
2250 C  CA  . LYS B 300 ? 0.63824 0.59864 0.50756 -0.09888 -0.01691 -0.08100 300 LYS B CA  
2251 C  C   . LYS B 300 ? 0.86515 0.80360 0.73623 -0.09211 -0.01064 -0.08238 300 LYS B C   
2252 O  O   . LYS B 300 ? 0.73273 0.65814 0.59670 -0.09765 -0.00545 -0.08940 300 LYS B O   
2253 C  CB  . LYS B 300 ? 0.75697 0.73577 0.63446 -0.10539 -0.02375 -0.08073 300 LYS B CB  
2254 N  N   . LYS B 301 ? 0.65087 0.58591 0.53131 -0.08041 -0.01121 -0.07537 301 LYS B N   
2255 C  CA  . LYS B 301 ? 0.53705 0.45415 0.42035 -0.07290 -0.00613 -0.07507 301 LYS B CA  
2256 C  C   . LYS B 301 ? 0.45917 0.38521 0.36046 -0.06573 -0.01223 -0.06753 301 LYS B C   
2257 O  O   . LYS B 301 ? 0.44949 0.39386 0.36082 -0.06538 -0.01970 -0.06219 301 LYS B O   
2258 C  CB  . LYS B 301 ? 0.60006 0.50335 0.47654 -0.06569 0.00039  -0.07448 301 LYS B CB  
2259 C  CG  . LYS B 301 ? 0.56102 0.47663 0.44208 -0.06034 -0.00347 -0.06780 301 LYS B CG  
2260 C  CD  . LYS B 301 ? 0.72887 0.64619 0.62428 -0.04960 -0.00611 -0.05980 301 LYS B CD  
2261 C  CE  . LYS B 301 ? 0.53019 0.46016 0.43109 -0.04498 -0.01031 -0.05279 301 LYS B CE  
2262 N  NZ  . LYS B 301 ? 0.48870 0.42311 0.40501 -0.03731 -0.01429 -0.04549 301 LYS B NZ  
2263 N  N   . TYR B 302 ? 0.47105 0.38362 0.37596 -0.06007 -0.00867 -0.06707 302 TYR B N   
2264 C  CA  . TYR B 302 ? 0.40896 0.32788 0.32953 -0.05463 -0.01331 -0.06138 302 TYR B CA  
2265 C  C   . TYR B 302 ? 0.39377 0.31502 0.32249 -0.04458 -0.01471 -0.05375 302 TYR B C   
2266 O  O   . TYR B 302 ? 0.45487 0.36677 0.37754 -0.03983 -0.01001 -0.05337 302 TYR B O   
2267 C  CB  . TYR B 302 ? 0.42965 0.33435 0.34995 -0.05478 -0.00914 -0.06473 302 TYR B CB  
2268 C  CG  . TYR B 302 ? 0.44087 0.34789 0.35835 -0.06487 -0.00972 -0.07085 302 TYR B CG  
2269 C  CD1 . TYR B 302 ? 0.49590 0.42133 0.42462 -0.06797 -0.01674 -0.06881 302 TYR B CD1 
2270 C  CD2 . TYR B 302 ? 0.49753 0.38850 0.40085 -0.07139 -0.00284 -0.07866 302 TYR B CD2 
2271 C  CE1 . TYR B 302 ? 0.41914 0.34918 0.34584 -0.07747 -0.01738 -0.07438 302 TYR B CE1 
2272 C  CE2 . TYR B 302 ? 0.46822 0.36205 0.36846 -0.08171 -0.00316 -0.08460 302 TYR B CE2 
2273 C  CZ  . TYR B 302 ? 0.57409 0.48837 0.48626 -0.08486 -0.01059 -0.08253 302 TYR B CZ  
2274 O  OH  . TYR B 302 ? 0.59144 0.51030 0.50073 -0.09553 -0.01078 -0.08865 302 TYR B OH  
2275 N  N   . ALA B 303 ? 0.33129 0.26498 0.27395 -0.04146 -0.02079 -0.04782 303 ALA B N   
2276 C  CA  . ALA B 303 ? 0.33879 0.27636 0.28939 -0.03342 -0.02257 -0.04061 303 ALA B CA  
2277 C  C   . ALA B 303 ? 0.33189 0.25796 0.28543 -0.02680 -0.01859 -0.03915 303 ALA B C   
2278 O  O   . ALA B 303 ? 0.31747 0.24627 0.27658 -0.02068 -0.01927 -0.03373 303 ALA B O   
2279 C  CB  . ALA B 303 ? 0.32321 0.27593 0.28726 -0.03235 -0.02951 -0.03488 303 ALA B CB  
2280 N  N   . ARG B 304 ? 0.33975 0.25363 0.28950 -0.02811 -0.01447 -0.04356 304 ARG B N   
2281 C  CA  . ARG B 304 ? 0.33647 0.24226 0.29030 -0.02147 -0.01166 -0.04086 304 ARG B CA  
2282 C  C   . ARG B 304 ? 0.34359 0.24190 0.29047 -0.01569 -0.00668 -0.03968 304 ARG B C   
2283 O  O   . ARG B 304 ? 0.33140 0.22672 0.28250 -0.00938 -0.00498 -0.03611 304 ARG B O   
2284 C  CB  . ARG B 304 ? 0.38300 0.27768 0.33470 -0.02387 -0.00858 -0.04491 304 ARG B CB  
2285 C  CG  . ARG B 304 ? 0.44588 0.32777 0.38334 -0.02856 -0.00309 -0.05158 304 ARG B CG  
2286 C  CD  . ARG B 304 ? 0.54706 0.41770 0.48202 -0.03202 -0.00012 -0.05557 304 ARG B CD  
2287 N  NE  . ARG B 304 ? 0.52906 0.38396 0.44852 -0.03557 0.00674  -0.06164 304 ARG B NE  
2288 C  CZ  . ARG B 304 ? 0.45810 0.29716 0.36990 -0.03802 0.01208  -0.06566 304 ARG B CZ  
2289 N  NH1 . ARG B 304 ? 0.44331 0.28065 0.36156 -0.03757 0.01113  -0.06432 304 ARG B NH1 
2290 N  NH2 . ARG B 304 ? 0.49089 0.31487 0.38768 -0.04124 0.01892  -0.07119 304 ARG B NH2 
2291 N  N   . ASP B 305 ? 0.32149 0.21853 0.25844 -0.01773 -0.00447 -0.04233 305 ASP B N   
2292 C  CA  . ASP B 305 ? 0.33367 0.22620 0.26523 -0.01191 0.00007  -0.04086 305 ASP B CA  
2293 C  C   . ASP B 305 ? 0.37243 0.27838 0.31155 -0.00814 -0.00395 -0.03456 305 ASP B C   
2294 O  O   . ASP B 305 ? 0.39994 0.30532 0.33487 -0.00422 -0.00080 -0.03334 305 ASP B O   
2295 C  CB  . ASP B 305 ? 0.39093 0.27495 0.30754 -0.01591 0.00534  -0.04703 305 ASP B CB  
2296 C  CG  . ASP B 305 ? 0.42427 0.31995 0.33795 -0.02295 0.00110  -0.04846 305 ASP B CG  
2297 O  OD1 . ASP B 305 ? 0.40963 0.31958 0.33287 -0.02416 -0.00591 -0.04429 305 ASP B OD1 
2298 O  OD2 . ASP B 305 ? 0.44115 0.33144 0.34233 -0.02736 0.00514  -0.05375 305 ASP B OD2 
2299 N  N   . ILE B 306 ? 0.30331 0.22064 0.25348 -0.00905 -0.01027 -0.03048 306 ILE B N   
2300 C  CA  . ILE B 306 ? 0.27883 0.20734 0.23609 -0.00594 -0.01377 -0.02428 306 ILE B CA  
2301 C  C   . ILE B 306 ? 0.30580 0.23658 0.27461 -0.00223 -0.01556 -0.01998 306 ILE B C   
2302 O  O   . ILE B 306 ? 0.29530 0.22475 0.26940 -0.00420 -0.01726 -0.02110 306 ILE B O   
2303 C  CB  . ILE B 306 ? 0.27560 0.21577 0.23490 -0.01060 -0.01951 -0.02268 306 ILE B CB  
2304 C  CG1 . ILE B 306 ? 0.35307 0.29292 0.30020 -0.01507 -0.01789 -0.02676 306 ILE B CG1 
2305 C  CG2 . ILE B 306 ? 0.27543 0.22565 0.24328 -0.00738 -0.02320 -0.01547 306 ILE B CG2 
2306 C  CD1 . ILE B 306 ? 0.39382 0.34517 0.34228 -0.02086 -0.02370 -0.02616 306 ILE B CD1 
2307 N  N   . VAL B 307 ? 0.25813 0.19327 0.23075 0.00232  -0.01515 -0.01530 307 VAL B N   
2308 C  CA  . VAL B 307 ? 0.25424 0.19431 0.23786 0.00435  -0.01750 -0.01081 307 VAL B CA  
2309 C  C   . VAL B 307 ? 0.31249 0.26218 0.29982 0.00457  -0.02039 -0.00585 307 VAL B C   
2310 O  O   . VAL B 307 ? 0.30993 0.26187 0.29199 0.00613  -0.01859 -0.00476 307 VAL B O   
2311 C  CB  . VAL B 307 ? 0.42549 0.36196 0.41026 0.00922  -0.01370 -0.00961 307 VAL B CB  
2312 C  CG1 . VAL B 307 ? 0.33327 0.27566 0.32868 0.00983  -0.01600 -0.00549 307 VAL B CG1 
2313 C  CG2 . VAL B 307 ? 0.53297 0.45868 0.51299 0.00967  -0.01028 -0.01370 307 VAL B CG2 
2314 N  N   . TYR B 308 ? 0.26620 0.22093 0.26224 0.00311  -0.02435 -0.00282 308 TYR B N   
2315 C  CA  . TYR B 308 ? 0.26289 0.22498 0.26285 0.00338  -0.02671 0.00253  308 TYR B CA  
2316 C  C   . TYR B 308 ? 0.30402 0.26707 0.31124 0.00520  -0.02575 0.00563  308 TYR B C   
2317 O  O   . TYR B 308 ? 0.32400 0.28401 0.33660 0.00505  -0.02545 0.00438  308 TYR B O   
2318 C  CB  . TYR B 308 ? 0.24829 0.21503 0.25298 0.00088  -0.03137 0.00457  308 TYR B CB  
2319 C  CG  . TYR B 308 ? 0.26703 0.23758 0.26492 -0.00175 -0.03351 0.00353  308 TYR B CG  
2320 C  CD1 . TYR B 308 ? 0.27750 0.25348 0.27095 -0.00186 -0.03448 0.00709  308 TYR B CD1 
2321 C  CD2 . TYR B 308 ? 0.23240 0.20207 0.22801 -0.00485 -0.03462 -0.00090 308 TYR B CD2 
2322 C  CE1 . TYR B 308 ? 0.25764 0.23838 0.24448 -0.00489 -0.03665 0.00638  308 TYR B CE1 
2323 C  CE2 . TYR B 308 ? 0.27983 0.25472 0.26876 -0.00830 -0.03672 -0.00194 308 TYR B CE2 
2324 C  CZ  . TYR B 308 ? 0.30915 0.28980 0.29373 -0.00821 -0.03785 0.00187  308 TYR B CZ  
2325 O  OH  . TYR B 308 ? 0.37215 0.35921 0.34956 -0.01226 -0.04015 0.00099  308 TYR B OH  
2326 N  N   . GLY B 309 ? 0.27499 0.24280 0.28210 0.00605  -0.02527 0.00955  309 GLY B N   
2327 C  CA  . GLY B 309 ? 0.24843 0.21841 0.26204 0.00623  -0.02457 0.01268  309 GLY B CA  
2328 C  C   . GLY B 309 ? 0.30645 0.28113 0.32040 0.00515  -0.02575 0.01747  309 GLY B C   
2329 O  O   . GLY B 309 ? 0.33980 0.31685 0.34840 0.00483  -0.02694 0.01860  309 GLY B O   
2330 N  N   . THR B 310 ? 0.27191 0.24739 0.29173 0.00400  -0.02528 0.02023  310 THR B N   
2331 C  CA  . THR B 310 ? 0.25485 0.23320 0.27464 0.00257  -0.02557 0.02500  310 THR B CA  
2332 C  C   . THR B 310 ? 0.30476 0.28729 0.32416 0.00192  -0.02232 0.02594  310 THR B C   
2333 O  O   . THR B 310 ? 0.28568 0.26810 0.30930 0.00128  -0.02068 0.02456  310 THR B O   
2334 C  CB  . THR B 310 ? 0.30209 0.27692 0.32865 0.00115  -0.02720 0.02771  310 THR B CB  
2335 O  OG1 . THR B 310 ? 0.35135 0.32460 0.37936 0.00208  -0.03032 0.02672  310 THR B OG1 
2336 C  CG2 . THR B 310 ? 0.29077 0.26681 0.31582 -0.00009 -0.02730 0.03311  310 THR B CG2 
2337 N  N   . ILE B 311 ? 0.25561 0.24295 0.26990 0.00168  -0.02139 0.02827  311 ILE B N   
2338 C  CA  . ILE B 311 ? 0.21840 0.21155 0.23282 0.00019  -0.01848 0.02984  311 ILE B CA  
2339 C  C   . ILE B 311 ? 0.25333 0.24660 0.26692 -0.00314 -0.01869 0.03447  311 ILE B C   
2340 O  O   . ILE B 311 ? 0.30577 0.29484 0.31873 -0.00330 -0.02116 0.03684  311 ILE B O   
2341 C  CB  . ILE B 311 ? 0.26851 0.26828 0.27795 0.00295  -0.01602 0.02830  311 ILE B CB  
2342 C  CG1 . ILE B 311 ? 0.29225 0.29213 0.29428 0.00446  -0.01661 0.02801  311 ILE B CG1 
2343 C  CG2 . ILE B 311 ? 0.26809 0.26649 0.27910 0.00638  -0.01493 0.02451  311 ILE B CG2 
2344 C  CD1 . ILE B 311 ? 0.35267 0.35494 0.35115 0.00152  -0.01750 0.03219  311 ILE B CD1 
2345 N  N   . TYR B 312 ? 0.25304 0.25131 0.26681 -0.00603 -0.01596 0.03602  312 TYR B N   
2346 C  CA  . TYR B 312 ? 0.25810 0.25435 0.27112 -0.01008 -0.01535 0.04029  312 TYR B CA  
2347 C  C   . TYR B 312 ? 0.28592 0.29053 0.29368 -0.01201 -0.01303 0.04204  312 TYR B C   
2348 O  O   . TYR B 312 ? 0.27286 0.28589 0.28117 -0.01231 -0.01063 0.04024  312 TYR B O   
2349 C  CB  . TYR B 312 ? 0.25436 0.24630 0.27300 -0.01398 -0.01357 0.04033  312 TYR B CB  
2350 C  CG  . TYR B 312 ? 0.30531 0.28878 0.32900 -0.01203 -0.01569 0.03904  312 TYR B CG  
2351 C  CD1 . TYR B 312 ? 0.26631 0.25026 0.29335 -0.00972 -0.01637 0.03474  312 TYR B CD1 
2352 C  CD2 . TYR B 312 ? 0.28455 0.26005 0.30950 -0.01192 -0.01703 0.04243  312 TYR B CD2 
2353 C  CE1 . TYR B 312 ? 0.30499 0.28208 0.33655 -0.00809 -0.01829 0.03324  312 TYR B CE1 
2354 C  CE2 . TYR B 312 ? 0.34007 0.30944 0.37042 -0.00956 -0.01899 0.04123  312 TYR B CE2 
2355 C  CZ  . TYR B 312 ? 0.30046 0.27092 0.33409 -0.00806 -0.01955 0.03635  312 TYR B CZ  
2356 O  OH  . TYR B 312 ? 0.33741 0.30259 0.37646 -0.00623 -0.02126 0.03495  312 TYR B OH  
2357 N  N   . LEU B 313 ? 0.29206 0.29526 0.29483 -0.01327 -0.01375 0.04584  313 LEU B N   
2358 C  CA  . LEU B 313 ? 0.30791 0.31939 0.30500 -0.01524 -0.01149 0.04729  313 LEU B CA  
2359 C  C   . LEU B 313 ? 0.27829 0.29206 0.27659 -0.02112 -0.00820 0.04899  313 LEU B C   
2360 O  O   . LEU B 313 ? 0.31283 0.31814 0.31287 -0.02448 -0.00785 0.05138  313 LEU B O   
2361 C  CB  . LEU B 313 ? 0.31097 0.32058 0.30131 -0.01522 -0.01333 0.05091  313 LEU B CB  
2362 C  CG  . LEU B 313 ? 0.30724 0.31509 0.29557 -0.01077 -0.01663 0.04895  313 LEU B CG  
2363 C  CD1 . LEU B 313 ? 0.32199 0.33011 0.30288 -0.01158 -0.01859 0.05276  313 LEU B CD1 
2364 C  CD2 . LEU B 313 ? 0.34255 0.35618 0.32982 -0.00727 -0.01510 0.04365  313 LEU B CD2 
2365 N  N   . GLY B 314 ? 0.29170 0.31709 0.28914 -0.02239 -0.00540 0.04755  314 GLY B N   
2366 C  CA  . GLY B 314 ? 0.34623 0.37669 0.34443 -0.02894 -0.00203 0.04846  314 GLY B CA  
2367 C  C   . GLY B 314 ? 0.43585 0.46266 0.44020 -0.03163 -0.00134 0.04660  314 GLY B C   
2368 O  O   . GLY B 314 ? 0.39589 0.42360 0.40043 -0.03851 0.00154  0.04723  314 GLY B O   
2369 N  N   . GLY B 315 ? 0.31538 0.33767 0.32416 -0.02696 -0.00367 0.04404  315 GLY B N   
2370 C  CA  . GLY B 315 ? 0.29567 0.31406 0.31002 -0.02956 -0.00303 0.04197  315 GLY B CA  
2371 C  C   . GLY B 315 ? 0.35862 0.36311 0.37376 -0.03320 -0.00254 0.04382  315 GLY B C   
2372 O  O   . GLY B 315 ? 0.32401 0.32465 0.34300 -0.03681 -0.00093 0.04194  315 GLY B O   
2373 N  N   . LYS B 316 ? 0.31796 0.31466 0.32938 -0.03212 -0.00367 0.04766  316 LYS B N   
2374 C  CA  . LYS B 316 ? 0.33760 0.32048 0.34968 -0.03462 -0.00266 0.05045  316 LYS B CA  
2375 C  C   . LYS B 316 ? 0.29825 0.27271 0.31525 -0.02910 -0.00583 0.04979  316 LYS B C   
2376 O  O   . LYS B 316 ? 0.32758 0.30396 0.34372 -0.02363 -0.00952 0.05019  316 LYS B O   
2377 C  CB  . LYS B 316 ? 0.39104 0.37014 0.39672 -0.03594 -0.00225 0.05588  316 LYS B CB  
2378 C  CG  . LYS B 316 ? 0.48651 0.47444 0.48709 -0.04218 0.00123  0.05637  316 LYS B CG  
2379 C  CD  . LYS B 316 ? 0.58763 0.56985 0.58129 -0.04444 0.00217  0.06203  316 LYS B CD  
2380 N  N   . PRO B 317 ? 0.29782 0.26317 0.31969 -0.03086 -0.00415 0.04858  317 PRO B N   
2381 C  CA  . PRO B 317 ? 0.27425 0.23378 0.30178 -0.02579 -0.00689 0.04716  317 PRO B CA  
2382 C  C   . PRO B 317 ? 0.30959 0.26243 0.33675 -0.02118 -0.00968 0.05191  317 PRO B C   
2383 O  O   . PRO B 317 ? 0.34703 0.29889 0.37824 -0.01643 -0.01289 0.05085  317 PRO B O   
2384 C  CB  . PRO B 317 ? 0.35403 0.30578 0.38624 -0.02999 -0.00319 0.04462  317 PRO B CB  
2385 C  CG  . PRO B 317 ? 0.36987 0.31877 0.39769 -0.03704 0.00148  0.04660  317 PRO B CG  
2386 C  CD  . PRO B 317 ? 0.35190 0.31374 0.37437 -0.03826 0.00076  0.04719  317 PRO B CD  
2387 N  N   . ASP B 318 ? 0.33947 0.28879 0.36165 -0.02253 -0.00872 0.05736  318 ASP B N   
2388 C  CA  . ASP B 318 ? 0.34923 0.29473 0.37043 -0.01776 -0.01198 0.06282  318 ASP B CA  
2389 C  C   . ASP B 318 ? 0.37511 0.33034 0.38996 -0.01595 -0.01538 0.06431  318 ASP B C   
2390 O  O   . ASP B 318 ? 0.36813 0.32209 0.37979 -0.01360 -0.01778 0.06977  318 ASP B O   
2391 C  CB  . ASP B 318 ? 0.37360 0.30732 0.39304 -0.01952 -0.00879 0.06890  318 ASP B CB  
2392 C  CG  . ASP B 318 ? 0.52475 0.45960 0.53637 -0.02527 -0.00561 0.07118  318 ASP B CG  
2393 O  OD1 . ASP B 318 ? 0.48327 0.42844 0.49215 -0.02857 -0.00503 0.06741  318 ASP B OD1 
2394 O  OD2 . ASP B 318 ? 0.59026 0.51561 0.59845 -0.02633 -0.00343 0.07709  318 ASP B OD2 
2395 N  N   . GLN B 319 ? 0.31439 0.27945 0.32733 -0.01670 -0.01553 0.05962  319 GLN B N   
2396 C  CA  . GLN B 319 ? 0.29901 0.27278 0.30590 -0.01488 -0.01802 0.05981  319 GLN B CA  
2397 C  C   . GLN B 319 ? 0.24599 0.22515 0.25472 -0.01120 -0.02044 0.05439  319 GLN B C   
2398 O  O   . GLN B 319 ? 0.29025 0.27700 0.29569 -0.01111 -0.01953 0.05122  319 GLN B O   
2399 C  CB  . GLN B 319 ? 0.32010 0.30045 0.32120 -0.01910 -0.01485 0.06003  319 GLN B CB  
2400 C  CG  . GLN B 319 ? 0.36433 0.33856 0.36119 -0.02278 -0.01291 0.06625  319 GLN B CG  
2401 C  CD  . GLN B 319 ? 0.35900 0.33996 0.34979 -0.02779 -0.00963 0.06675  319 GLN B CD  
2402 O  OE1 . GLN B 319 ? 0.44854 0.43983 0.43925 -0.02852 -0.00837 0.06244  319 GLN B OE1 
2403 N  NE2 . GLN B 319 ? 0.38293 0.35832 0.36857 -0.03120 -0.00794 0.07234  319 GLN B NE2 
2404 N  N   . PRO B 320 ? 0.29969 0.27505 0.31313 -0.00796 -0.02330 0.05349  320 PRO B N   
2405 C  CA  . PRO B 320 ? 0.26169 0.24082 0.27583 -0.00521 -0.02521 0.04825  320 PRO B CA  
2406 C  C   . PRO B 320 ? 0.29349 0.27848 0.30028 -0.00390 -0.02730 0.04811  320 PRO B C   
2407 O  O   . PRO B 320 ? 0.32167 0.30759 0.32443 -0.00404 -0.02934 0.05258  320 PRO B O   
2408 C  CB  . PRO B 320 ? 0.29994 0.27380 0.32082 -0.00296 -0.02766 0.04804  320 PRO B CB  
2409 C  CG  . PRO B 320 ? 0.30582 0.27521 0.32728 -0.00283 -0.02842 0.05493  320 PRO B CG  
2410 C  CD  . PRO B 320 ? 0.34476 0.31199 0.36362 -0.00669 -0.02430 0.05691  320 PRO B CD  
2411 N  N   . ALA B 321 ? 0.26605 0.25447 0.27093 -0.00256 -0.02664 0.04285  321 ALA B N   
2412 C  CA  . ALA B 321 ? 0.32104 0.31292 0.31942 -0.00131 -0.02824 0.04076  321 ALA B CA  
2413 C  C   . ALA B 321 ? 0.33021 0.31998 0.33060 0.00067  -0.02842 0.03489  321 ALA B C   
2414 O  O   . ALA B 321 ? 0.28458 0.27226 0.28977 0.00135  -0.02649 0.03231  321 ALA B O   
2415 C  CB  . ALA B 321 ? 0.29142 0.28906 0.28245 -0.00202 -0.02546 0.04042  321 ALA B CB  
2416 N  N   . VAL B 322 ? 0.28521 0.27566 0.28123 0.00103  -0.03053 0.03275  322 VAL B N   
2417 C  CA  . VAL B 322 ? 0.27236 0.25966 0.26918 0.00209  -0.03065 0.02719  322 VAL B CA  
2418 C  C   . VAL B 322 ? 0.30181 0.28921 0.29177 0.00331  -0.02706 0.02268  322 VAL B C   
2419 O  O   . VAL B 322 ? 0.32259 0.31310 0.30479 0.00262  -0.02631 0.02259  322 VAL B O   
2420 C  CB  . VAL B 322 ? 0.25922 0.24761 0.25478 0.00094  -0.03468 0.02698  322 VAL B CB  
2421 C  CG1 . VAL B 322 ? 0.29596 0.28088 0.29045 0.00089  -0.03425 0.02052  322 VAL B CG1 
2422 C  CG2 . VAL B 322 ? 0.38602 0.37438 0.38967 0.00110  -0.03787 0.03187  322 VAL B CG2 
2423 N  N   . ILE B 323 ? 0.23359 0.21728 0.22590 0.00529  -0.02457 0.01895  323 ILE B N   
2424 C  CA  . ILE B 323 ? 0.25504 0.23695 0.24063 0.00735  -0.02090 0.01461  323 ILE B CA  
2425 C  C   . ILE B 323 ? 0.34318 0.31871 0.32687 0.00685  -0.02148 0.00979  323 ILE B C   
2426 O  O   . ILE B 323 ? 0.31642 0.28830 0.30603 0.00698  -0.02238 0.00872  323 ILE B O   
2427 C  CB  . ILE B 323 ? 0.25762 0.24092 0.24579 0.01054  -0.01703 0.01466  323 ILE B CB  
2428 C  CG1 . ILE B 323 ? 0.40761 0.38766 0.38921 0.01397  -0.01271 0.01050  323 ILE B CG1 
2429 C  CG2 . ILE B 323 ? 0.39209 0.37340 0.38904 0.01058  -0.01789 0.01517  323 ILE B CG2 
2430 C  CD1 . ILE B 323 ? 0.46758 0.45147 0.45189 0.01805  -0.00896 0.01155  323 ILE B CD1 
2431 N  N   . LYS B 324 ? 0.25325 0.22769 0.22830 0.00539  -0.02094 0.00674  324 LYS B N   
2432 C  CA  . LYS B 324 ? 0.29835 0.26673 0.26966 0.00364  -0.02092 0.00150  324 LYS B CA  
2433 C  C   . LYS B 324 ? 0.39736 0.35886 0.36109 0.00616  -0.01509 -0.00315 324 LYS B C   
2434 O  O   . LYS B 324 ? 0.36358 0.32626 0.31977 0.00652  -0.01227 -0.00405 324 LYS B O   
2435 C  CB  . LYS B 324 ? 0.28014 0.25255 0.24629 -0.00092 -0.02434 0.00107  324 LYS B CB  
2436 C  CG  . LYS B 324 ? 0.29673 0.26419 0.25847 -0.00409 -0.02425 -0.00472 324 LYS B CG  
2437 C  CD  . LYS B 324 ? 0.37101 0.34534 0.32694 -0.00931 -0.02778 -0.00492 324 LYS B CD  
2438 C  CE  . LYS B 324 ? 0.45732 0.42791 0.40783 -0.01393 -0.02747 -0.01132 324 LYS B CE  
2439 N  NZ  . LYS B 324 ? 0.53440 0.51281 0.47695 -0.01972 -0.03008 -0.01222 324 LYS B NZ  
2440 N  N   . THR B 325 ? 0.26388 0.21766 0.22902 0.00793  -0.01292 -0.00611 325 THR B N   
2441 C  CA  . THR B 325 ? 0.26702 0.21249 0.22530 0.01143  -0.00677 -0.00986 325 THR B CA  
2442 C  C   . THR B 325 ? 0.32627 0.26208 0.27748 0.00797  -0.00545 -0.01589 325 THR B C   
2443 O  O   . THR B 325 ? 0.32830 0.26193 0.28375 0.00541  -0.00818 -0.01692 325 THR B O   
2444 C  CB  . THR B 325 ? 0.25915 0.20316 0.22390 0.01662  -0.00472 -0.00773 325 THR B CB  
2445 O  OG1 . THR B 325 ? 0.30007 0.25415 0.27094 0.01848  -0.00589 -0.00256 325 THR B OG1 
2446 C  CG2 . THR B 325 ? 0.29128 0.22676 0.24913 0.02168  0.00202  -0.01050 325 THR B CG2 
2447 N  N   . THR B 326 ? 0.31704 0.24704 0.25718 0.00731  -0.00089 -0.02020 326 THR B N   
2448 C  CA  . THR B 326 ? 0.30236 0.22286 0.23378 0.00255  0.00106  -0.02665 326 THR B CA  
2449 C  C   . THR B 326 ? 0.38392 0.29073 0.30701 0.00676  0.00926  -0.03053 326 THR B C   
2450 O  O   . THR B 326 ? 0.34858 0.25552 0.26816 0.01128  0.01360  -0.02977 326 THR B O   
2451 C  CB  . THR B 326 ? 0.37578 0.30165 0.29972 -0.00407 -0.00093 -0.02898 326 THR B CB  
2452 O  OG1 . THR B 326 ? 0.38460 0.32356 0.31664 -0.00645 -0.00830 -0.02395 326 THR B OG1 
2453 C  CG2 . THR B 326 ? 0.38402 0.30204 0.29977 -0.01057 0.00038  -0.03576 326 THR B CG2 
2454 N  N   . PHE B 327 ? 0.31269 0.20770 0.23287 0.00568  0.01171  -0.03433 327 PHE B N   
2455 C  CA  . PHE B 327 ? 0.39659 0.27609 0.30836 0.01006  0.02006  -0.03768 327 PHE B CA  
2456 C  C   . PHE B 327 ? 0.42881 0.29714 0.32637 0.00387  0.02476  -0.04540 327 PHE B C   
2457 O  O   . PHE B 327 ? 0.42045 0.28858 0.31546 -0.00436 0.02175  -0.04917 327 PHE B O   
2458 C  CB  . PHE B 327 ? 0.32224 0.19389 0.23868 0.01321  0.02080  -0.03652 327 PHE B CB  
2459 C  CG  . PHE B 327 ? 0.35182 0.23519 0.28172 0.01750  0.01596  -0.02964 327 PHE B CG  
2460 C  CD1 . PHE B 327 ? 0.36914 0.25821 0.30279 0.02508  0.01798  -0.02495 327 PHE B CD1 
2461 C  CD2 . PHE B 327 ? 0.39687 0.28694 0.33563 0.01342  0.00952  -0.02805 327 PHE B CD2 
2462 C  CE1 . PHE B 327 ? 0.32122 0.22193 0.26633 0.02767  0.01375  -0.01912 327 PHE B CE1 
2463 C  CE2 . PHE B 327 ? 0.36479 0.26486 0.31482 0.01649  0.00578  -0.02238 327 PHE B CE2 
2464 C  CZ  . PHE B 327 ? 0.32013 0.22580 0.27303 0.02317  0.00780  -0.01796 327 PHE B CZ  
2465 N  N   . ASN B 328 ? 0.38311 0.24280 0.27147 0.00771  0.03248  -0.04785 328 ASN B N   
2466 C  CA  . ASN B 328 ? 0.46474 0.30877 0.33788 0.00325  0.03982  -0.05580 328 ASN B CA  
2467 C  C   . ASN B 328 ? 0.49189 0.34253 0.35840 -0.00781 0.03642  -0.06044 328 ASN B C   
2468 O  O   . ASN B 328 ? 0.54402 0.38509 0.40079 -0.01561 0.03891  -0.06718 328 ASN B O   
2469 C  CB  . ASN B 328 ? 0.42304 0.24986 0.29204 0.00267  0.04384  -0.05910 328 ASN B CB  
2470 C  CG  . ASN B 328 ? 0.46389 0.28262 0.33689 0.01394  0.04848  -0.05464 328 ASN B CG  
2471 O  OD1 . ASN B 328 ? 0.44900 0.27198 0.32456 0.02202  0.05110  -0.05092 328 ASN B OD1 
2472 N  ND2 . ASN B 328 ? 0.42276 0.23125 0.29660 0.01445  0.04932  -0.05461 328 ASN B ND2 
2473 N  N   . GLN B 329 ? 0.44626 0.31398 0.31785 -0.00906 0.03055  -0.05663 329 GLN B N   
2474 C  CA  . GLN B 329 ? 0.39600 0.27168 0.26098 -0.01922 0.02710  -0.06018 329 GLN B CA  
2475 C  C   . GLN B 329 ? 0.53846 0.41623 0.39412 -0.02010 0.03111  -0.06223 329 GLN B C   
2476 O  O   . GLN B 329 ? 0.57273 0.46121 0.42441 -0.02777 0.02702  -0.06328 329 GLN B O   
2477 C  CB  . GLN B 329 ? 0.39989 0.29406 0.27664 -0.02208 0.01643  -0.05441 329 GLN B CB  
2478 C  CG  . GLN B 329 ? 0.44406 0.33692 0.32666 -0.02547 0.01248  -0.05512 329 GLN B CG  
2479 C  CD  . GLN B 329 ? 0.54150 0.42933 0.41303 -0.03610 0.01389  -0.06309 329 GLN B CD  
2480 O  OE1 . GLN B 329 ? 0.55862 0.43096 0.42364 -0.03769 0.01949  -0.06846 329 GLN B OE1 
2481 N  NE2 . GLN B 329 ? 0.52548 0.42696 0.39484 -0.04366 0.00873  -0.06354 329 GLN B NE2 
2482 N  N   . GLU B 330 ? 0.48244 0.35161 0.33496 -0.01232 0.03878  -0.06241 330 GLU B N   
2483 C  CA  . GLU B 330 ? 0.44639 0.31586 0.28902 -0.01317 0.04406  -0.06539 330 GLU B CA  
2484 C  C   . GLU B 330 ? 0.50473 0.35430 0.33165 -0.01627 0.05431  -0.07458 330 GLU B C   
2485 O  O   . GLU B 330 ? 0.55640 0.39049 0.38171 -0.01382 0.05873  -0.07687 330 GLU B O   
2486 C  CB  . GLU B 330 ? 0.46464 0.33852 0.31376 -0.00245 0.04682  -0.05994 330 GLU B CB  
2487 C  CG  . GLU B 330 ? 0.46282 0.35452 0.32698 0.00041  0.03766  -0.05106 330 GLU B CG  
2488 C  CD  . GLU B 330 ? 0.71072 0.61788 0.57423 -0.00700 0.03087  -0.04925 330 GLU B CD  
2489 O  OE1 . GLU B 330 ? 0.60112 0.50860 0.45362 -0.01144 0.03435  -0.05334 330 GLU B OE1 
2490 O  OE2 . GLU B 330 ? 0.51298 0.43170 0.38661 -0.00832 0.02237  -0.04361 330 GLU B OE2 
2491 N  N   . THR B 331 ? 0.57299 0.42246 0.38760 -0.02215 0.05839  -0.07993 331 THR B N   
2492 C  CA  . THR B 331 ? 0.65236 0.48183 0.45071 -0.02489 0.06979  -0.08915 331 THR B CA  
2493 C  C   . THR B 331 ? 0.57153 0.39451 0.36781 -0.01469 0.07887  -0.08866 331 THR B C   
2494 O  O   . THR B 331 ? 0.73066 0.56715 0.53705 -0.00741 0.07573  -0.08176 331 THR B O   
2495 C  CB  . THR B 331 ? 0.71031 0.54305 0.49487 -0.03897 0.06956  -0.09651 331 THR B CB  
2496 O  OG1 . THR B 331 ? 0.67624 0.52797 0.46306 -0.04051 0.06442  -0.09269 331 THR B OG1 
2497 C  CG2 . THR B 331 ? 0.90133 0.73892 0.68690 -0.04902 0.06213  -0.09800 331 THR B CG2 
2498 N  N   . GLY B 332 ? 0.57256 0.37455 0.35527 -0.01440 0.09072  -0.09628 332 GLY B N   
2499 C  CA  . GLY B 332 ? 0.61921 0.41394 0.39963 -0.00404 0.10056  -0.09625 332 GLY B CA  
2500 C  C   . GLY B 332 ? 0.73575 0.52626 0.52792 0.01072  0.10259  -0.08926 332 GLY B C   
2501 O  O   . GLY B 332 ? 0.80259 0.59577 0.59844 0.02094  0.10755  -0.08610 332 GLY B O   
2502 N  N   . CYS B 333 ? 0.65837 0.44365 0.45665 0.01196  0.09883  -0.08659 333 CYS B N   
2503 C  CA  . CYS B 333 ? 0.67072 0.45338 0.48014 0.02531  0.09994  -0.07942 333 CYS B CA  
2504 C  C   . CYS B 333 ? 0.57465 0.34208 0.38236 0.02333  0.10007  -0.08082 333 CYS B C   
2505 O  O   . CYS B 333 ? 0.67973 0.44302 0.48035 0.01147  0.09749  -0.08640 333 CYS B O   
2506 C  CB  . CYS B 333 ? 0.58350 0.39027 0.41025 0.02979  0.08953  -0.06988 333 CYS B CB  
2507 S  SG  . CYS B 333 ? 0.60271 0.42474 0.43646 0.01809  0.07544  -0.06804 333 CYS B SG  
2508 N  N   . GLU B 334 ? 0.53537 0.29573 0.34977 0.03483  0.10290  -0.07540 334 GLU B N   
2509 C  CA  . GLU B 334 ? 0.53758 0.28524 0.35177 0.03342  0.10215  -0.07542 334 GLU B CA  
2510 C  C   . GLU B 334 ? 0.53102 0.29664 0.36046 0.03214  0.08972  -0.06862 334 GLU B C   
2511 O  O   . GLU B 334 ? 0.54710 0.30857 0.37577 0.02467  0.08578  -0.07067 334 GLU B O   
2512 C  CB  . GLU B 334 ? 0.62019 0.34893 0.43214 0.04596  0.11205  -0.07304 334 GLU B CB  
2513 C  CG  . GLU B 334 ? 0.99555 0.69635 0.78881 0.04381  0.12534  -0.08190 334 GLU B CG  
2514 C  CD  . GLU B 334 ? 0.99452 0.68346 0.77672 0.02892  0.12451  -0.09000 334 GLU B CD  
2515 O  OE1 . GLU B 334 ? 1.16386 0.84593 0.93291 0.01903  0.12908  -0.09862 334 GLU B OE1 
2516 O  OE2 . GLU B 334 ? 1.03883 0.72773 0.82627 0.02642  0.11878  -0.08749 334 GLU B OE2 
2517 N  N   . TYR B 335 ? 0.51913 0.30457 0.36202 0.03871  0.08393  -0.06099 335 TYR B N   
2518 C  CA  . TYR B 335 ? 0.47257 0.27514 0.32984 0.03761  0.07286  -0.05464 335 TYR B CA  
2519 C  C   . TYR B 335 ? 0.43797 0.26282 0.30325 0.03679  0.06641  -0.05088 335 TYR B C   
2520 O  O   . TYR B 335 ? 0.45429 0.28244 0.31680 0.04074  0.07093  -0.05106 335 TYR B O   
2521 C  CB  . TYR B 335 ? 0.49494 0.29708 0.36173 0.04834  0.07312  -0.04746 335 TYR B CB  
2522 C  CG  . TYR B 335 ? 0.53837 0.31781 0.39746 0.05173  0.08056  -0.04945 335 TYR B CG  
2523 C  CD1 . TYR B 335 ? 0.57249 0.33696 0.42427 0.06116  0.09148  -0.04990 335 TYR B CD1 
2524 C  CD2 . TYR B 335 ? 0.52160 0.29455 0.38106 0.04604  0.07695  -0.05037 335 TYR B CD2 
2525 C  CE1 . TYR B 335 ? 0.57013 0.31220 0.41430 0.06481  0.09879  -0.05103 335 TYR B CE1 
2526 C  CE2 . TYR B 335 ? 0.50603 0.25709 0.35771 0.04893  0.08405  -0.05181 335 TYR B CE2 
2527 C  CZ  . TYR B 335 ? 0.63622 0.37144 0.48001 0.05838  0.09498  -0.05195 335 TYR B CZ  
2528 O  OH  . TYR B 335 ? 0.66009 0.37223 0.49551 0.06163  0.10251  -0.05284 335 TYR B OH  
2529 N  N   . SER B 336 ? 0.41303 0.25293 0.28835 0.03190  0.05620  -0.04724 336 SER B N   
2530 C  CA  . SER B 336 ? 0.40051 0.26036 0.28371 0.03171  0.05035  -0.04272 336 SER B CA  
2531 C  C   . SER B 336 ? 0.42189 0.29505 0.31886 0.03091  0.04099  -0.03662 336 SER B C   
2532 O  O   . SER B 336 ? 0.40024 0.26909 0.29938 0.02712  0.03756  -0.03739 336 SER B O   
2533 C  CB  . SER B 336 ? 0.39163 0.25616 0.26707 0.02218  0.04838  -0.04721 336 SER B CB  
2534 O  OG  . SER B 336 ? 0.41220 0.27489 0.28582 0.01282  0.04331  -0.05035 336 SER B OG  
2535 N  N   . ILE B 337 ? 0.37458 0.26356 0.28038 0.03424  0.03754  -0.03087 337 ILE B N   
2536 C  CA  . ILE B 337 ? 0.32620 0.22904 0.24387 0.03200  0.02891  -0.02552 337 ILE B CA  
2537 C  C   . ILE B 337 ? 0.41099 0.32723 0.32929 0.02829  0.02538  -0.02379 337 ILE B C   
2538 O  O   . ILE B 337 ? 0.41025 0.33195 0.32758 0.03246  0.02893  -0.02232 337 ILE B O   
2539 C  CB  . ILE B 337 ? 0.37800 0.28685 0.30605 0.03985  0.02876  -0.01945 337 ILE B CB  
2540 C  CG1 . ILE B 337 ? 0.36051 0.25593 0.28696 0.04439  0.03286  -0.02042 337 ILE B CG1 
2541 C  CG2 . ILE B 337 ? 0.34674 0.26825 0.28612 0.03662  0.02067  -0.01470 337 ILE B CG2 
2542 C  CD1 . ILE B 337 ? 0.43158 0.33359 0.36687 0.05297  0.03366  -0.01421 337 ILE B CD1 
2543 N  N   . THR B 338 ? 0.33978 0.26176 0.25985 0.02080  0.01857  -0.02356 338 THR B N   
2544 C  CA  A THR B 338 ? 0.34330 0.27747 0.26349 0.01716  0.01493  -0.02113 338 THR B CA  
2545 C  CA  B THR B 338 ? 0.36763 0.30144 0.28739 0.01648  0.01462  -0.02146 338 THR B CA  
2546 C  C   . THR B 338 ? 0.40712 0.35208 0.33886 0.01583  0.00750  -0.01510 338 THR B C   
2547 O  O   . THR B 338 ? 0.36470 0.30781 0.30185 0.01376  0.00350  -0.01473 338 THR B O   
2548 C  CB  A THR B 338 ? 0.46199 0.39463 0.37199 0.00928  0.01403  -0.02578 338 THR B CB  
2549 C  CB  B THR B 338 ? 0.31155 0.24308 0.22253 0.00809  0.01268  -0.02610 338 THR B CB  
2550 O  OG1 A THR B 338 ? 0.37597 0.30827 0.28848 0.00363  0.00839  -0.02656 338 THR B OG1 
2551 O  OG1 B THR B 338 ? 0.47669 0.39646 0.37517 0.00751  0.02008  -0.03289 338 THR B OG1 
2552 C  CG2 A THR B 338 ? 0.50981 0.42957 0.40751 0.00974  0.02223  -0.03264 338 THR B CG2 
2553 C  CG2 B THR B 338 ? 0.35025 0.29454 0.26097 0.00386  0.00809  -0.02290 338 THR B CG2 
2554 N  N   . PHE B 339 ? 0.33199 0.28776 0.26743 0.01722  0.00646  -0.01049 339 PHE B N   
2555 C  CA  . PHE B 339 ? 0.31908 0.28425 0.26445 0.01587  0.00057  -0.00463 339 PHE B CA  
2556 C  C   . PHE B 339 ? 0.37842 0.35063 0.32059 0.01047  -0.00333 -0.00274 339 PHE B C   
2557 O  O   . PHE B 339 ? 0.38426 0.36085 0.32067 0.01026  -0.00089 -0.00257 339 PHE B O   
2558 C  CB  . PHE B 339 ? 0.31353 0.28599 0.26541 0.02077  0.00247  -0.00041 339 PHE B CB  
2559 C  CG  . PHE B 339 ? 0.31462 0.28259 0.27012 0.02653  0.00588  -0.00099 339 PHE B CG  
2560 C  CD1 . PHE B 339 ? 0.31350 0.27882 0.27612 0.02627  0.00291  0.00002  339 PHE B CD1 
2561 C  CD2 . PHE B 339 ? 0.39155 0.35807 0.34327 0.03253  0.01233  -0.00232 339 PHE B CD2 
2562 C  CE1 . PHE B 339 ? 0.29841 0.26016 0.26376 0.03145  0.00590  0.00002  339 PHE B CE1 
2563 C  CE2 . PHE B 339 ? 0.34304 0.30566 0.29800 0.03860  0.01544  -0.00196 339 PHE B CE2 
2564 C  CZ  . PHE B 339 ? 0.32385 0.28438 0.28551 0.03781  0.01195  -0.00060 339 PHE B CZ  
2565 N  N   . ASN B 340 ? 0.32101 0.29485 0.26685 0.00637  -0.00920 -0.00103 340 ASN B N   
2566 C  CA  . ASN B 340 ? 0.29525 0.27699 0.23944 0.00209  -0.01352 0.00261  340 ASN B CA  
2567 C  C   . ASN B 340 ? 0.36052 0.34770 0.31476 0.00281  -0.01717 0.00916  340 ASN B C   
2568 O  O   . ASN B 340 ? 0.33084 0.31557 0.29309 0.00342  -0.01954 0.01007  340 ASN B O   
2569 C  CB  . ASN B 340 ? 0.34878 0.33009 0.28925 -0.00304 -0.01744 0.00048  340 ASN B CB  
2570 C  CG  . ASN B 340 ? 0.45449 0.44518 0.39378 -0.00679 -0.02242 0.00558  340 ASN B CG  
2571 O  OD1 . ASN B 340 ? 0.41264 0.40701 0.35977 -0.00702 -0.02728 0.01060  340 ASN B OD1 
2572 N  ND2 . ASN B 340 ? 0.38018 0.37449 0.30960 -0.00935 -0.02077 0.00469  340 ASN B ND2 
2573 N  N   . PHE B 341 ? 0.28815 0.28198 0.24149 0.00244  -0.01695 0.01335  341 PHE B N   
2574 C  CA  . PHE B 341 ? 0.27533 0.27332 0.23628 0.00209  -0.01964 0.01953  341 PHE B CA  
2575 C  C   . PHE B 341 ? 0.34428 0.34596 0.30308 -0.00161 -0.02436 0.02376  341 PHE B C   
2576 O  O   . PHE B 341 ? 0.35869 0.36386 0.30888 -0.00395 -0.02426 0.02346  341 PHE B O   
2577 C  CB  . PHE B 341 ? 0.29442 0.29758 0.25549 0.00353  -0.01599 0.02170  341 PHE B CB  
2578 C  CG  . PHE B 341 ? 0.33674 0.33863 0.30117 0.00789  -0.01169 0.01886  341 PHE B CG  
2579 C  CD1 . PHE B 341 ? 0.35390 0.35333 0.31240 0.01094  -0.00714 0.01409  341 PHE B CD1 
2580 C  CD2 . PHE B 341 ? 0.37053 0.37340 0.34381 0.00895  -0.01202 0.02106  341 PHE B CD2 
2581 C  CE1 . PHE B 341 ? 0.34893 0.34741 0.31098 0.01600  -0.00322 0.01247  341 PHE B CE1 
2582 C  CE2 . PHE B 341 ? 0.33907 0.34234 0.31562 0.01303  -0.00856 0.01916  341 PHE B CE2 
2583 C  CZ  . PHE B 341 ? 0.29906 0.30046 0.27034 0.01698  -0.00435 0.01537  341 PHE B CZ  
2584 N  N   . SER B 342 ? 0.28193 0.28303 0.24830 -0.00198 -0.02826 0.02786  342 SER B N   
2585 C  CA  . SER B 342 ? 0.30325 0.30820 0.26813 -0.00445 -0.03286 0.03281  342 SER B CA  
2586 C  C   . SER B 342 ? 0.36132 0.36479 0.33514 -0.00360 -0.03492 0.03873  342 SER B C   
2587 O  O   . SER B 342 ? 0.34184 0.34110 0.32300 -0.00192 -0.03338 0.03768  342 SER B O   
2588 C  CB  . SER B 342 ? 0.32446 0.33017 0.28725 -0.00610 -0.03627 0.03005  342 SER B CB  
2589 O  OG  . SER B 342 ? 0.35827 0.36013 0.33006 -0.00454 -0.03787 0.02913  342 SER B OG  
2590 N  N   . TRP B 343 ? 0.30205 0.30864 0.27459 -0.00486 -0.03797 0.04517  343 TRP B N   
2591 C  CA  . TRP B 343 ? 0.29828 0.30156 0.27857 -0.00382 -0.03907 0.05105  343 TRP B CA  
2592 C  C   . TRP B 343 ? 0.36762 0.37412 0.34734 -0.00392 -0.04369 0.05765  343 TRP B C   
2593 O  O   . TRP B 343 ? 0.35815 0.37089 0.32995 -0.00578 -0.04578 0.05896  343 TRP B O   
2594 C  CB  . TRP B 343 ? 0.32695 0.32866 0.30683 -0.00479 -0.03530 0.05365  343 TRP B CB  
2595 C  CG  . TRP B 343 ? 0.34067 0.34757 0.31101 -0.00713 -0.03450 0.05597  343 TRP B CG  
2596 C  CD1 . TRP B 343 ? 0.41916 0.42721 0.38590 -0.00873 -0.03598 0.06314  343 TRP B CD1 
2597 C  CD2 . TRP B 343 ? 0.33584 0.34714 0.29877 -0.00804 -0.03160 0.05128  343 TRP B CD2 
2598 N  NE1 . TRP B 343 ? 0.41975 0.43329 0.37704 -0.01121 -0.03444 0.06296  343 TRP B NE1 
2599 C  CE2 . TRP B 343 ? 0.43984 0.45557 0.39484 -0.01072 -0.03159 0.05549  343 TRP B CE2 
2600 C  CE3 . TRP B 343 ? 0.30714 0.31852 0.26913 -0.00654 -0.02862 0.04410  343 TRP B CE3 
2601 C  CZ2 . TRP B 343 ? 0.38314 0.40392 0.32968 -0.01218 -0.02864 0.05223  343 TRP B CZ2 
2602 C  CZ3 . TRP B 343 ? 0.35000 0.36563 0.30378 -0.00728 -0.02543 0.04113  343 TRP B CZ3 
2603 C  CH2 . TRP B 343 ? 0.45464 0.47526 0.40090 -0.01023 -0.02538 0.04494  343 TRP B CH2 
2604 N  N   . SER B 344 ? 0.35742 0.35987 0.34565 -0.00178 -0.04507 0.06196  344 SER B N   
2605 C  CA  . SER B 344 ? 0.35000 0.35567 0.33955 -0.00042 -0.04946 0.06914  344 SER B CA  
2606 C  C   . SER B 344 ? 0.39257 0.39285 0.38400 0.00065  -0.04839 0.07744  344 SER B C   
2607 O  O   . SER B 344 ? 0.44957 0.45296 0.43949 0.00187  -0.05161 0.08494  344 SER B O   
2608 C  CB  . SER B 344 ? 0.39914 0.40548 0.39746 0.00208  -0.05228 0.06756  344 SER B CB  
2609 O  OG  . SER B 344 ? 0.39383 0.39173 0.40070 0.00367  -0.04916 0.06528  344 SER B OG  
2610 N  N   . LYS B 345 ? 0.40299 0.39551 0.39692 -0.00011 -0.04380 0.07655  345 LYS B N   
2611 C  CA  . LYS B 345 ? 0.44477 0.43090 0.43826 -0.00043 -0.04175 0.08379  345 LYS B CA  
2612 C  C   . LYS B 345 ? 0.53173 0.52209 0.51446 -0.00352 -0.04144 0.08734  345 LYS B C   
2613 O  O   . LYS B 345 ? 0.44558 0.44290 0.42170 -0.00574 -0.04141 0.08283  345 LYS B O   
2614 C  CB  . LYS B 345 ? 0.39465 0.37228 0.39274 -0.00191 -0.03658 0.08092  345 LYS B CB  
2615 C  CG  . LYS B 345 ? 0.51666 0.48842 0.52498 0.00073  -0.03625 0.07891  345 LYS B CG  
2616 C  CD  . LYS B 345 ? 0.63213 0.59475 0.64314 -0.00183 -0.03085 0.07828  345 LYS B CD  
2617 C  CE  . LYS B 345 ? 0.56624 0.52126 0.58692 0.00036  -0.02962 0.07708  345 LYS B CE  
2618 N  NZ  . LYS B 345 ? 0.52024 0.46609 0.54191 -0.00345 -0.02384 0.07644  345 LYS B NZ  
2619 N  N   . THR B 346 ? 0.47677 0.46223 0.45739 -0.00359 -0.04084 0.09567  346 THR B N   
2620 C  CA  . THR B 346 ? 0.42513 0.41330 0.39537 -0.00707 -0.03995 0.09984  346 THR B CA  
2621 C  C   . THR B 346 ? 0.60473 0.58781 0.57347 -0.01112 -0.03404 0.09727  346 THR B C   
2622 O  O   . THR B 346 ? 0.79134 0.76451 0.76301 -0.01173 -0.03088 0.10074  346 THR B O   
2623 C  CB  . THR B 346 ? 0.51108 0.49624 0.47901 -0.00521 -0.04214 0.11076  346 THR B CB  
2624 O  OG1 . THR B 346 ? 0.55516 0.54747 0.52573 -0.00133 -0.04792 0.11314  346 THR B OG1 
2625 C  CG2 . THR B 346 ? 0.55200 0.54079 0.50828 -0.00923 -0.04157 0.11501  346 THR B CG2 
2626 N  N   . TYR B 347 ? 0.43704 0.42706 0.40130 -0.01398 -0.03218 0.09107  347 TYR B N   
2627 C  CA  . TYR B 347 ? 0.39616 0.38466 0.35935 -0.01800 -0.02681 0.08856  347 TYR B CA  
2628 C  C   . TYR B 347 ? 0.45021 0.44176 0.40329 -0.02216 -0.02522 0.09298  347 TYR B C   
2629 O  O   . TYR B 347 ? 0.49867 0.49734 0.44464 -0.02231 -0.02773 0.09407  347 TYR B O   
2630 C  CB  . TYR B 347 ? 0.38345 0.37822 0.34900 -0.01789 -0.02509 0.07963  347 TYR B CB  
2631 C  CG  . TYR B 347 ? 0.39226 0.38280 0.36756 -0.01471 -0.02586 0.07549  347 TYR B CG  
2632 C  CD1 . TYR B 347 ? 0.41827 0.39954 0.40013 -0.01489 -0.02425 0.07758  347 TYR B CD1 
2633 C  CD2 . TYR B 347 ? 0.43759 0.43245 0.41483 -0.01186 -0.02788 0.06956  347 TYR B CD2 
2634 C  CE1 . TYR B 347 ? 0.37390 0.35149 0.36446 -0.01235 -0.02474 0.07364  347 TYR B CE1 
2635 C  CE2 . TYR B 347 ? 0.35629 0.34727 0.34188 -0.00940 -0.02848 0.06592  347 TYR B CE2 
2636 C  CZ  . TYR B 347 ? 0.38960 0.37251 0.38201 -0.00965 -0.02704 0.06800  347 TYR B CZ  
2637 O  OH  . TYR B 347 ? 0.36606 0.34546 0.36646 -0.00755 -0.02746 0.06422  347 TYR B OH  
2638 N  N   . GLU B 348 ? 0.47737 0.46356 0.42933 -0.02624 -0.02077 0.09524  348 GLU B N   
2639 C  CA  . GLU B 348 ? 0.49656 0.48368 0.43894 -0.03097 -0.01863 0.10028  348 GLU B CA  
2640 C  C   . GLU B 348 ? 0.44932 0.44240 0.39035 -0.03594 -0.01354 0.09503  348 GLU B C   
2641 O  O   . GLU B 348 ? 0.48193 0.46957 0.42595 -0.03941 -0.00954 0.09463  348 GLU B O   
2642 C  CB  . GLU B 348 ? 0.43213 0.40637 0.37343 -0.03184 -0.01754 0.10890  348 GLU B CB  
2643 C  CG  . GLU B 348 ? 0.55429 0.52833 0.48463 -0.03628 -0.01608 0.11549  348 GLU B CG  
2644 C  CD  . GLU B 348 ? 0.60928 0.56847 0.53798 -0.03651 -0.01452 0.12467  348 GLU B CD  
2645 O  OE1 . GLU B 348 ? 0.78152 0.73027 0.71800 -0.03335 -0.01387 0.12539  348 GLU B OE1 
2646 O  OE2 . GLU B 348 ? 0.77649 0.73392 0.69574 -0.03981 -0.01351 0.13122  348 GLU B OE2 
2647 N  N   . ASN B 349 ? 0.47494 0.47980 0.41165 -0.03629 -0.01346 0.09075  349 ASN B N   
2648 C  CA  . ASN B 349 ? 0.41328 0.42710 0.34863 -0.04010 -0.00883 0.08611  349 ASN B CA  
2649 C  C   . ASN B 349 ? 0.46250 0.47755 0.40727 -0.03896 -0.00686 0.08009  349 ASN B C   
2650 O  O   . ASN B 349 ? 0.50661 0.52262 0.45321 -0.04347 -0.00287 0.07928  349 ASN B O   
2651 C  CB  . ASN B 349 ? 0.63287 0.64480 0.56171 -0.04696 -0.00502 0.09099  349 ASN B CB  
2652 C  CG  . ASN B 349 ? 0.81954 0.83153 0.73819 -0.04831 -0.00682 0.09704  349 ASN B CG  
2653 O  OD1 . ASN B 349 ? 0.66870 0.68854 0.58328 -0.04612 -0.00917 0.09516  349 ASN B OD1 
2654 N  ND2 . ASN B 349 ? 0.78967 0.79214 0.70362 -0.05200 -0.00562 0.10449  349 ASN B ND2 
2655 N  N   . VAL B 350 ? 0.37888 0.39471 0.32901 -0.03340 -0.00967 0.07578  350 VAL B N   
2656 C  CA  . VAL B 350 ? 0.36703 0.38389 0.32589 -0.03150 -0.00853 0.07034  350 VAL B CA  
2657 C  C   . VAL B 350 ? 0.45238 0.48085 0.41081 -0.02893 -0.00716 0.06448  350 VAL B C   
2658 O  O   . VAL B 350 ? 0.37604 0.40666 0.33090 -0.02552 -0.00911 0.06269  350 VAL B O   
2659 C  CB  . VAL B 350 ? 0.36767 0.37578 0.33311 -0.02708 -0.01216 0.06990  350 VAL B CB  
2660 C  CG1 . VAL B 350 ? 0.34692 0.35696 0.32060 -0.02506 -0.01107 0.06386  350 VAL B CG1 
2661 C  CG2 . VAL B 350 ? 0.35585 0.35199 0.32270 -0.02872 -0.01261 0.07580  350 VAL B CG2 
2662 N  N   . GLU B 351 ? 0.38956 0.42568 0.35147 -0.03053 -0.00353 0.06150  351 GLU B N   
2663 C  CA  . GLU B 351 ? 0.34983 0.39693 0.31216 -0.02693 -0.00167 0.05654  351 GLU B CA  
2664 C  C   . GLU B 351 ? 0.37633 0.41978 0.34440 -0.02095 -0.00379 0.05246  351 GLU B C   
2665 O  O   . GLU B 351 ? 0.37063 0.40800 0.34500 -0.02091 -0.00505 0.05233  351 GLU B O   
2666 C  CB  . GLU B 351 ? 0.39527 0.45366 0.36028 -0.03031 0.00265  0.05545  351 GLU B CB  
2667 C  CG  . GLU B 351 ? 0.57390 0.64470 0.54192 -0.02579 0.00514  0.05098  351 GLU B CG  
2668 C  CD  . GLU B 351 ? 0.91209 0.99405 0.88530 -0.02943 0.00830  0.05058  351 GLU B CD  
2669 O  OE1 . GLU B 351 ? 0.80616 0.88439 0.77985 -0.03615 0.00869  0.05308  351 GLU B OE1 
2670 O  OE2 . GLU B 351 ? 1.15733 1.25179 1.13402 -0.02571 0.01060  0.04789  351 GLU B OE2 
2671 N  N   . PHE B 352 ? 0.32836 0.37448 0.29357 -0.01629 -0.00385 0.04896  352 PHE B N   
2672 C  CA  . PHE B 352 ? 0.33769 0.37842 0.30671 -0.01114 -0.00579 0.04521  352 PHE B CA  
2673 C  C   . PHE B 352 ? 0.33489 0.38222 0.30962 -0.00783 -0.00285 0.04173  352 PHE B C   
2674 O  O   . PHE B 352 ? 0.32521 0.37811 0.29802 -0.00378 -0.00018 0.03866  352 PHE B O   
2675 C  CB  . PHE B 352 ? 0.30856 0.34699 0.27093 -0.00848 -0.00699 0.04291  352 PHE B CB  
2676 C  CG  . PHE B 352 ? 0.33806 0.36836 0.30333 -0.00520 -0.00990 0.04009  352 PHE B CG  
2677 C  CD1 . PHE B 352 ? 0.34378 0.37372 0.31329 -0.00087 -0.00815 0.03573  352 PHE B CD1 
2678 C  CD2 . PHE B 352 ? 0.31871 0.34233 0.28289 -0.00648 -0.01435 0.04226  352 PHE B CD2 
2679 C  CE1 . PHE B 352 ? 0.32142 0.34363 0.29330 0.00143  -0.01048 0.03305  352 PHE B CE1 
2680 C  CE2 . PHE B 352 ? 0.39988 0.41722 0.36733 -0.00404 -0.01693 0.03947  352 PHE B CE2 
2681 C  CZ  . PHE B 352 ? 0.37976 0.39592 0.35071 -0.00045 -0.01485 0.03460  352 PHE B CZ  
2682 N  N   . GLU B 353 ? 0.30758 0.35416 0.28930 -0.00943 -0.00313 0.04237  353 GLU B N   
2683 C  CA  . GLU B 353 ? 0.25409 0.30714 0.24167 -0.00632 -0.00117 0.03974  353 GLU B CA  
2684 C  C   . GLU B 353 ? 0.25678 0.30149 0.25047 -0.00668 -0.00366 0.03921  353 GLU B C   
2685 O  O   . GLU B 353 ? 0.33859 0.37755 0.33374 -0.01139 -0.00498 0.04163  353 GLU B O   
2686 C  CB  . GLU B 353 ? 0.37103 0.43762 0.36020 -0.00964 0.00223  0.04109  353 GLU B CB  
2687 C  CG  . GLU B 353 ? 0.42254 0.48766 0.41200 -0.01763 0.00217  0.04437  353 GLU B CG  
2688 C  CD  . GLU B 353 ? 0.62367 0.69251 0.62004 -0.02045 0.00288  0.04375  353 GLU B CD  
2689 O  OE1 . GLU B 353 ? 0.56506 0.63990 0.56580 -0.01581 0.00324  0.04141  353 GLU B OE1 
2690 O  OE2 . GLU B 353 ? 0.45869 0.52425 0.45557 -0.02739 0.00339  0.04559  353 GLU B OE2 
2691 N  N   . THR B 354 ? 0.29041 0.33301 0.28694 -0.00164 -0.00404 0.03610  354 THR B N   
2692 C  CA  . THR B 354 ? 0.30450 0.33722 0.30536 -0.00154 -0.00679 0.03506  354 THR B CA  
2693 C  C   . THR B 354 ? 0.28805 0.32497 0.29538 -0.00178 -0.00579 0.03410  354 THR B C   
2694 O  O   . THR B 354 ? 0.26942 0.31718 0.27808 0.00022  -0.00330 0.03375  354 THR B O   
2695 C  CB  . THR B 354 ? 0.24872 0.27391 0.24736 0.00332  -0.00829 0.03196  354 THR B CB  
2696 O  OG1 . THR B 354 ? 0.27412 0.30329 0.27370 0.00836  -0.00585 0.02936  354 THR B OG1 
2697 C  CG2 . THR B 354 ? 0.31021 0.33394 0.30103 0.00368  -0.00874 0.03213  354 THR B CG2 
2698 N  N   . THR B 355 ? 0.22927 0.25787 0.24067 -0.00389 -0.00780 0.03371  355 THR B N   
2699 C  CA  . THR B 355 ? 0.21329 0.24339 0.23019 -0.00359 -0.00747 0.03196  355 THR B CA  
2700 C  C   . THR B 355 ? 0.23749 0.26559 0.25371 0.00304  -0.00766 0.02927  355 THR B C   
2701 O  O   . THR B 355 ? 0.26434 0.28903 0.27579 0.00671  -0.00778 0.02826  355 THR B O   
2702 C  CB  . THR B 355 ? 0.24706 0.26776 0.26794 -0.00770 -0.00904 0.03184  355 THR B CB  
2703 O  OG1 . THR B 355 ? 0.25251 0.26236 0.27240 -0.00542 -0.01176 0.03121  355 THR B OG1 
2704 C  CG2 . THR B 355 ? 0.24118 0.26230 0.26183 -0.01434 -0.00772 0.03454  355 THR B CG2 
2705 N  N   . SER B 356 ? 0.21675 0.24647 0.23709 0.00417  -0.00736 0.02803  356 SER B N   
2706 C  CA  . SER B 356 ? 0.20012 0.22751 0.21948 0.01045  -0.00682 0.02598  356 SER B CA  
2707 C  C   . SER B 356 ? 0.24710 0.26183 0.26741 0.01050  -0.00909 0.02343  356 SER B C   
2708 O  O   . SER B 356 ? 0.28876 0.29963 0.31304 0.00613  -0.01066 0.02328  356 SER B O   
2709 C  CB  . SER B 356 ? 0.30887 0.34722 0.33167 0.01239  -0.00498 0.02693  356 SER B CB  
2710 O  OG  . SER B 356 ? 0.31392 0.36585 0.33602 0.01364  -0.00257 0.02911  356 SER B OG  
2711 N  N   . PHE B 357 ? 0.25561 0.26392 0.27214 0.01527  -0.00871 0.02116  357 PHE B N   
2712 C  CA  . PHE B 357 ? 0.24725 0.24431 0.26404 0.01506  -0.01060 0.01834  357 PHE B CA  
2713 C  C   . PHE B 357 ? 0.24144 0.23517 0.25629 0.02004  -0.00863 0.01649  357 PHE B C   
2714 O  O   . PHE B 357 ? 0.27624 0.27221 0.28701 0.02500  -0.00579 0.01665  357 PHE B O   
2715 C  CB  . PHE B 357 ? 0.27759 0.26799 0.29007 0.01428  -0.01235 0.01711  357 PHE B CB  
2716 C  CG  . PHE B 357 ? 0.27955 0.26004 0.29171 0.01393  -0.01413 0.01385  357 PHE B CG  
2717 C  CD1 . PHE B 357 ? 0.34495 0.32227 0.36305 0.01075  -0.01628 0.01353  357 PHE B CD1 
2718 C  CD2 . PHE B 357 ? 0.27518 0.24980 0.28086 0.01623  -0.01322 0.01085  357 PHE B CD2 
2719 C  CE1 . PHE B 357 ? 0.31520 0.28479 0.33337 0.01016  -0.01780 0.01037  357 PHE B CE1 
2720 C  CE2 . PHE B 357 ? 0.27591 0.24228 0.28093 0.01490  -0.01473 0.00752  357 PHE B CE2 
2721 C  CZ  . PHE B 357 ? 0.29402 0.25869 0.30565 0.01197  -0.01717 0.00745  357 PHE B CZ  
2722 N  N   . THR B 358 ? 0.24090 0.22903 0.25862 0.01888  -0.00968 0.01492  358 THR B N   
2723 C  CA  . THR B 358 ? 0.23334 0.21650 0.24883 0.02307  -0.00785 0.01349  358 THR B CA  
2724 C  C   . THR B 358 ? 0.26389 0.23450 0.27633 0.02202  -0.00888 0.00963  358 THR B C   
2725 O  O   . THR B 358 ? 0.28007 0.24773 0.29588 0.01747  -0.01166 0.00843  358 THR B O   
2726 C  CB  . THR B 358 ? 0.28233 0.27013 0.30298 0.02186  -0.00803 0.01485  358 THR B CB  
2727 O  OG1 . THR B 358 ? 0.34102 0.34251 0.36420 0.02240  -0.00696 0.01836  358 THR B OG1 
2728 C  CG2 . THR B 358 ? 0.35665 0.33798 0.37455 0.02612  -0.00625 0.01393  358 THR B CG2 
2729 N  N   . PHE B 359 ? 0.26099 0.22431 0.26722 0.02620  -0.00621 0.00768  359 PHE B N   
2730 C  CA  . PHE B 359 ? 0.28865 0.24004 0.29114 0.02453  -0.00657 0.00354  359 PHE B CA  
2731 C  C   . PHE B 359 ? 0.33038 0.27425 0.32786 0.02941  -0.00266 0.00270  359 PHE B C   
2732 O  O   . PHE B 359 ? 0.30408 0.25310 0.30202 0.03445  -0.00021 0.00586  359 PHE B O   
2733 C  CB  . PHE B 359 ? 0.27654 0.22465 0.27393 0.02258  -0.00736 0.00111  359 PHE B CB  
2734 C  CG  . PHE B 359 ? 0.33021 0.27859 0.32072 0.02667  -0.00382 0.00110  359 PHE B CG  
2735 C  CD1 . PHE B 359 ? 0.32046 0.27912 0.31256 0.02782  -0.00371 0.00437  359 PHE B CD1 
2736 C  CD2 . PHE B 359 ? 0.32196 0.25977 0.30391 0.02893  -0.00008 -0.00251 359 PHE B CD2 
2737 C  CE1 . PHE B 359 ? 0.32708 0.28654 0.31283 0.03157  -0.00000 0.00404  359 PHE B CE1 
2738 C  CE2 . PHE B 359 ? 0.29596 0.23306 0.27124 0.03278  0.00402  -0.00302 359 PHE B CE2 
2739 C  CZ  . PHE B 359 ? 0.35287 0.30140 0.33030 0.03434  0.00403  0.00027  359 PHE B CZ  
2740 N  N   . SER B 360 ? 0.30235 0.23423 0.29486 0.02796  -0.00185 -0.00131 360 SER B N   
2741 C  CA  . SER B 360 ? 0.27734 0.19891 0.26317 0.03256  0.00272  -0.00231 360 SER B CA  
2742 C  C   . SER B 360 ? 0.29949 0.20860 0.27668 0.03017  0.00452  -0.00765 360 SER B C   
2743 O  O   . SER B 360 ? 0.29698 0.20713 0.27459 0.02457  0.00137  -0.01030 360 SER B O   
2744 C  CB  . SER B 360 ? 0.35526 0.27409 0.34402 0.03229  0.00247  -0.00133 360 SER B CB  
2745 O  OG  . SER B 360 ? 0.32663 0.23735 0.31464 0.02638  0.00075  -0.00559 360 SER B OG  
2746 N  N   . TYR B 361 ? 0.31293 0.21073 0.28186 0.03455  0.00994  -0.00900 361 TYR B N   
2747 C  CA  . TYR B 361 ? 0.28602 0.17008 0.24543 0.03116  0.01251  -0.01482 361 TYR B CA  
2748 C  C   . TYR B 361 ? 0.34166 0.21085 0.29403 0.03493  0.01807  -0.01564 361 TYR B C   
2749 O  O   . TYR B 361 ? 0.35245 0.22261 0.30653 0.04190  0.02045  -0.01108 361 TYR B O   
2750 C  CB  . TYR B 361 ? 0.29838 0.18192 0.25108 0.03131  0.01475  -0.01719 361 TYR B CB  
2751 C  CG  . TYR B 361 ? 0.36517 0.24945 0.31503 0.03963  0.01989  -0.01442 361 TYR B CG  
2752 C  CD1 . TYR B 361 ? 0.34764 0.24708 0.30423 0.04254  0.01789  -0.00991 361 TYR B CD1 
2753 C  CD2 . TYR B 361 ? 0.40007 0.26978 0.34031 0.04443  0.02719  -0.01647 361 TYR B CD2 
2754 C  CE1 . TYR B 361 ? 0.36705 0.26912 0.32164 0.05020  0.02273  -0.00748 361 TYR B CE1 
2755 C  CE2 . TYR B 361 ? 0.37523 0.24625 0.31361 0.05291  0.03233  -0.01376 361 TYR B CE2 
2756 C  CZ  . TYR B 361 ? 0.40890 0.29712 0.35488 0.05580  0.02990  -0.00928 361 TYR B CZ  
2757 O  OH  . TYR B 361 ? 0.36458 0.25531 0.30913 0.06432  0.03526  -0.00673 361 TYR B OH  
2758 N  N   . ILE B 362 ? 0.35282 0.20843 0.29676 0.03007  0.02031  -0.02137 362 ILE B N   
2759 C  CA  . ILE B 362 ? 0.35227 0.19075 0.28793 0.03228  0.02605  -0.02282 362 ILE B CA  
2760 C  C   . ILE B 362 ? 0.38996 0.21845 0.31648 0.03945  0.03357  -0.02288 362 ILE B C   
2761 O  O   . ILE B 362 ? 0.42195 0.24916 0.34291 0.03769  0.03541  -0.02650 362 ILE B O   
2762 C  CB  . ILE B 362 ? 0.37279 0.20071 0.30243 0.02320  0.02598  -0.02943 362 ILE B CB  
2763 C  CG1 . ILE B 362 ? 0.40076 0.23940 0.34049 0.01708  0.01899  -0.02912 362 ILE B CG1 
2764 C  CG2 . ILE B 362 ? 0.46415 0.27204 0.38356 0.02481  0.03275  -0.03120 362 ILE B CG2 
2765 C  CD1 . ILE B 362 ? 0.42174 0.25578 0.35770 0.00735  0.01764  -0.03568 362 ILE B CD1 
2766 N  N   . ALA B 363 ? 0.42710 0.24866 0.35191 0.04782  0.03824  -0.01865 363 ALA B N   
2767 C  CA  . ALA B 363 ? 0.42484 0.23754 0.34240 0.05666  0.04600  -0.01755 363 ALA B CA  
2768 C  C   . ALA B 363 ? 0.44603 0.23448 0.34910 0.05488  0.05369  -0.02343 363 ALA B C   
2769 O  O   . ALA B 363 ? 0.48601 0.26299 0.38493 0.04985  0.05408  -0.02591 363 ALA B O   
2770 C  CB  . ALA B 363 ? 0.47934 0.29665 0.40186 0.06752  0.04783  -0.00949 363 ALA B CB  
2771 N  N   . GLN B 364 ? 0.48013 0.26056 0.37509 0.05884  0.06040  -0.02582 364 GLN B N   
2772 C  CA  . GLN B 364 ? 0.51356 0.26962 0.39330 0.05689  0.06906  -0.03211 364 GLN B CA  
2773 C  C   . GLN B 364 ? 0.62932 0.36781 0.50388 0.06342  0.07511  -0.02892 364 GLN B C   
2774 O  O   . GLN B 364 ? 0.58895 0.30749 0.45265 0.05800  0.07961  -0.03395 364 GLN B O   
2775 C  CB  . GLN B 364 ? 0.51027 0.26241 0.38322 0.06113  0.07564  -0.03462 364 GLN B CB  
2776 C  CG  . GLN B 364 ? 0.54450 0.26955 0.40093 0.06123  0.08672  -0.04057 364 GLN B CG  
2777 C  CD  . GLN B 364 ? 0.76555 0.47940 0.61180 0.04706  0.08673  -0.04989 364 GLN B CD  
2778 O  OE1 . GLN B 364 ? 0.64642 0.37445 0.49815 0.03744  0.07835  -0.05213 364 GLN B OE1 
2779 N  NE2 . GLN B 364 ? 0.88137 0.57074 0.71302 0.04559  0.09631  -0.05508 364 GLN B NE2 
2780 N  N   . GLU B 365 ? 0.59934 0.34514 0.48102 0.07483  0.07549  -0.02042 365 GLU B N   
2781 C  CA  . GLU B 365 ? 0.77978 0.51257 0.65842 0.08126  0.07955  -0.01560 365 GLU B CA  
2782 C  C   . GLU B 365 ? 0.81647 0.56917 0.70836 0.08902  0.07417  -0.00586 365 GLU B C   
2783 O  O   . GLU B 365 ? 1.03988 0.78777 0.93196 0.09289  0.07475  -0.00075 365 GLU B O   
2784 C  CB  . GLU B 365 ? 0.77682 0.48888 0.64396 0.08949  0.09091  -0.01575 365 GLU B CB  
2785 C  CG  . GLU B 365 ? 0.85471 0.57438 0.72480 0.10101  0.09497  -0.01216 365 GLU B CG  
2786 C  CD  . GLU B 365 ? 1.12785 0.83351 0.98914 0.10553  0.10439  -0.01243 365 GLU B CD  
2787 O  OE1 . GLU B 365 ? 1.12156 0.81111 0.97187 0.09655  0.10838  -0.01964 365 GLU B OE1 
2788 O  OE2 . GLU B 365 ? 1.06646 0.77792 0.93198 0.11786  0.10785  -0.00528 365 GLU B OE2 
2789 O  OXT . GLU B 365 ? 0.89667 0.67102 0.79885 0.09091  0.06918  -0.00294 365 GLU B OXT 
2790 N  N   . LYS C 180 ? 0.93437 0.97368 0.76242 0.11787  0.00584  0.06902  180 LYS C N   
2791 C  CA  . LYS C 180 ? 1.00553 1.04628 0.84060 0.12422  -0.00159 0.07452  180 LYS C CA  
2792 C  C   . LYS C 180 ? 1.02998 1.08991 0.86524 0.12312  -0.01359 0.06947  180 LYS C C   
2793 O  O   . LYS C 180 ? 0.87939 0.95229 0.70653 0.11843  -0.01601 0.06306  180 LYS C O   
2794 C  CB  . LYS C 180 ? 0.98264 1.00679 0.83975 0.12252  0.00107  0.07262  180 LYS C CB  
2795 C  CG  . LYS C 180 ? 0.77095 0.79683 0.64695 0.11416  -0.00339 0.06049  180 LYS C CG  
2796 C  CD  . LYS C 180 ? 0.87153 0.88292 0.76779 0.11468  -0.00283 0.06105  180 LYS C CD  
2797 C  CE  . LYS C 180 ? 0.73294 0.74012 0.62552 0.12463  -0.00407 0.07311  180 LYS C CE  
2798 N  NZ  . LYS C 180 ? 0.55589 0.57963 0.44139 0.12979  -0.01490 0.07640  180 LYS C NZ  
2799 N  N   . ASN C 181 ? 0.82890 0.89055 0.67350 0.12739  -0.02098 0.07229  181 ASN C N   
2800 C  CA  . ASN C 181 ? 0.78857 0.86821 0.63283 0.12767  -0.03266 0.06902  181 ASN C CA  
2801 C  C   . ASN C 181 ? 0.77474 0.84893 0.63826 0.12857  -0.03787 0.06817  181 ASN C C   
2802 O  O   . ASN C 181 ? 0.74950 0.82416 0.61226 0.13605  -0.04177 0.07624  181 ASN C O   
2803 C  CB  . ASN C 181 ? 0.88052 0.97349 0.70497 0.13565  -0.03709 0.07802  181 ASN C CB  
2804 C  CG  . ASN C 181 ? 0.96041 1.07437 0.78038 0.13397  -0.04769 0.07264  181 ASN C CG  
2805 O  OD1 . ASN C 181 ? 0.93321 1.05439 0.75816 0.13758  -0.05617 0.07424  181 ASN C OD1 
2806 N  ND2 . ASN C 181 ? 1.13581 1.25973 0.94621 0.12840  -0.04710 0.06613  181 ASN C ND2 
2807 N  N   . ASP C 182 ? 0.58672 0.65551 0.46776 0.12069  -0.03774 0.05822  182 ASP C N   
2808 C  CA  . ASP C 182 ? 0.69176 0.75300 0.59269 0.12016  -0.04139 0.05636  182 ASP C CA  
2809 C  C   . ASP C 182 ? 0.47220 0.54925 0.37719 0.11939  -0.05323 0.05176  182 ASP C C   
2810 O  O   . ASP C 182 ? 0.46392 0.54743 0.37664 0.11190  -0.05685 0.04135  182 ASP C O   
2811 C  CB  . ASP C 182 ? 0.49916 0.54670 0.41665 0.11219  -0.03529 0.04831  182 ASP C CB  
2812 C  CG  . ASP C 182 ? 0.70119 0.73969 0.63936 0.11127  -0.03830 0.04643  182 ASP C CG  
2813 O  OD1 . ASP C 182 ? 0.49199 0.53412 0.43216 0.11682  -0.04490 0.05140  182 ASP C OD1 
2814 O  OD2 . ASP C 182 ? 0.52980 0.55732 0.48240 0.10483  -0.03385 0.03990  182 ASP C OD2 
2815 N  N   . THR C 183 ? 0.43759 0.52014 0.33835 0.12713  -0.05909 0.05954  183 THR C N   
2816 C  CA  . THR C 183 ? 0.50426 0.60180 0.40779 0.12760  -0.07036 0.05657  183 THR C CA  
2817 C  C   . THR C 183 ? 0.55525 0.64693 0.48014 0.12385  -0.07450 0.05084  183 THR C C   
2818 O  O   . THR C 183 ? 0.46426 0.56799 0.39299 0.12314  -0.08382 0.04709  183 THR C O   
2819 C  CB  . THR C 183 ? 0.56240 0.66702 0.45407 0.13759  -0.07464 0.06747  183 THR C CB  
2820 O  OG1 . THR C 183 ? 0.55592 0.64665 0.45719 0.14266  -0.07249 0.07440  183 THR C OG1 
2821 C  CG2 . THR C 183 ? 0.56884 0.67682 0.43961 0.14189  -0.06959 0.07447  183 THR C CG2 
2822 N  N   . ARG C 184 ? 0.37391 0.44782 0.31263 0.12123  -0.06793 0.04988  184 ARG C N   
2823 C  CA  . ARG C 184 ? 0.35181 0.41865 0.31115 0.11755  -0.07116 0.04480  184 ARG C CA  
2824 C  C   . ARG C 184 ? 0.35760 0.42237 0.32905 0.10742  -0.07000 0.03294  184 ARG C C   
2825 O  O   . ARG C 184 ? 0.37967 0.43806 0.36878 0.10352  -0.07228 0.02804  184 ARG C O   
2826 C  CB  . ARG C 184 ? 0.46932 0.51774 0.43728 0.12156  -0.06516 0.05177  184 ARG C CB  
2827 C  CG  . ARG C 184 ? 0.73611 0.78493 0.69260 0.13185  -0.06532 0.06407  184 ARG C CG  
2828 C  CD  . ARG C 184 ? 0.72202 0.75777 0.69154 0.13557  -0.06472 0.06909  184 ARG C CD  
2829 N  NE  . ARG C 184 ? 0.99587 1.03627 0.97952 0.12900  -0.07220 0.06268  184 ARG C NE  
2830 C  CZ  . ARG C 184 ? 1.00840 1.03934 1.00591 0.12409  -0.07126 0.06343  184 ARG C CZ  
2831 N  NH1 . ARG C 184 ? 0.78776 0.82326 0.79763 0.11543  -0.07628 0.05775  184 ARG C NH1 
2832 N  NH2 . ARG C 184 ? 1.03231 1.04963 1.03115 0.12707  -0.06470 0.07004  184 ARG C NH2 
2833 N  N   . THR C 185 ? 0.34362 0.41422 0.30590 0.10305  -0.06681 0.02817  185 THR C N   
2834 C  CA  . THR C 185 ? 0.34221 0.41098 0.31536 0.09339  -0.06509 0.01690  185 THR C CA  
2835 C  C   . THR C 185 ? 0.37261 0.45930 0.33610 0.08940  -0.06992 0.01011  185 THR C C   
2836 O  O   . THR C 185 ? 0.36462 0.45857 0.31053 0.09149  -0.06743 0.01300  185 THR C O   
2837 C  CB  . THR C 185 ? 0.40571 0.45937 0.38003 0.09069  -0.05361 0.01691  185 THR C CB  
2838 O  OG1 . THR C 185 ? 0.51769 0.55451 0.50388 0.09330  -0.04961 0.02174  185 THR C OG1 
2839 C  CG2 . THR C 185 ? 0.41774 0.47079 0.40230 0.08057  -0.05171 0.00498  185 THR C CG2 
2840 N  N   . LEU C 186 ? 0.30796 0.40159 0.28301 0.08351  -0.07668 0.00102  186 LEU C N   
2841 C  CA  . LEU C 186 ? 0.34665 0.45583 0.31619 0.07801  -0.08082 -0.00745 186 LEU C CA  
2842 C  C   . LEU C 186 ? 0.30158 0.40309 0.28435 0.06866  -0.07607 -0.01744 186 LEU C C   
2843 O  O   . LEU C 186 ? 0.30318 0.39485 0.30414 0.06546  -0.07657 -0.02086 186 LEU C O   
2844 C  CB  . LEU C 186 ? 0.34672 0.46968 0.31979 0.07859  -0.09229 -0.01009 186 LEU C CB  
2845 C  CG  . LEU C 186 ? 0.47045 0.61246 0.43690 0.07488  -0.09920 -0.01727 186 LEU C CG  
2846 C  CD1 . LEU C 186 ? 0.37899 0.53157 0.32341 0.07851  -0.09739 -0.01291 186 LEU C CD1 
2847 C  CD2 . LEU C 186 ? 0.40106 0.54934 0.37268 0.07605  -0.10752 -0.01624 186 LEU C CD2 
2848 N  N   . TRP C 187 ? 0.28226 0.38727 0.25622 0.06437  -0.07096 -0.02179 187 TRP C N   
2849 C  CA  . TRP C 187 ? 0.26188 0.35751 0.24917 0.05594  -0.06532 -0.03047 187 TRP C CA  
2850 C  C   . TRP C 187 ? 0.31443 0.42073 0.29347 0.04970  -0.06383 -0.03848 187 TRP C C   
2851 O  O   . TRP C 187 ? 0.32049 0.44093 0.28255 0.05193  -0.06655 -0.03700 187 TRP C O   
2852 C  CB  . TRP C 187 ? 0.28400 0.36028 0.27521 0.05726  -0.05487 -0.02557 187 TRP C CB  
2853 C  CG  . TRP C 187 ? 0.29068 0.36499 0.26408 0.05987  -0.04638 -0.02037 187 TRP C CG  
2854 C  CD1 . TRP C 187 ? 0.30443 0.39226 0.25763 0.06226  -0.04739 -0.01814 187 TRP C CD1 
2855 C  CD2 . TRP C 187 ? 0.30026 0.35779 0.27488 0.06034  -0.03570 -0.01666 187 TRP C CD2 
2856 N  NE1 . TRP C 187 ? 0.33952 0.41977 0.28115 0.06393  -0.03779 -0.01339 187 TRP C NE1 
2857 C  CE2 . TRP C 187 ? 0.34838 0.40997 0.30291 0.06285  -0.03046 -0.01240 187 TRP C CE2 
2858 C  CE3 . TRP C 187 ? 0.29504 0.33460 0.28582 0.05879  -0.03004 -0.01658 187 TRP C CE3 
2859 C  CZ2 . TRP C 187 ? 0.34233 0.39032 0.29260 0.06377  -0.01969 -0.00820 187 TRP C CZ2 
2860 C  CZ3 . TRP C 187 ? 0.34746 0.37362 0.33427 0.05967  -0.01926 -0.01257 187 TRP C CZ3 
2861 C  CH2 . TRP C 187 ? 0.34193 0.37230 0.30854 0.06218  -0.01414 -0.00839 187 TRP C CH2 
2862 N  N   . THR C 188 ? 0.27112 0.37037 0.26294 0.04169  -0.05946 -0.04714 188 THR C N   
2863 C  CA  . THR C 188 ? 0.31331 0.41967 0.30003 0.03474  -0.05636 -0.05557 188 THR C CA  
2864 C  C   . THR C 188 ? 0.35663 0.45474 0.33326 0.03447  -0.04531 -0.05308 188 THR C C   
2865 O  O   . THR C 188 ? 0.37064 0.47358 0.34285 0.02851  -0.04174 -0.06004 188 THR C O   
2866 C  CB  . THR C 188 ? 0.30314 0.40559 0.30992 0.02590  -0.05692 -0.06654 188 THR C CB  
2867 O  OG1 . THR C 188 ? 0.28875 0.37239 0.31075 0.02526  -0.05108 -0.06499 188 THR C OG1 
2868 C  CG2 . THR C 188 ? 0.30374 0.41675 0.31926 0.02478  -0.06805 -0.07078 188 THR C CG2 
2869 N  N   . THR C 189 ? 0.35709 0.44271 0.33051 0.04041  -0.03967 -0.04375 189 THR C N   
2870 C  CA  . THR C 189 ? 0.31738 0.38968 0.28682 0.04004  -0.02816 -0.04104 189 THR C CA  
2871 C  C   . THR C 189 ? 0.45186 0.51061 0.44187 0.03279  -0.02313 -0.04857 189 THR C C   
2872 O  O   . THR C 189 ? 0.36646 0.42908 0.37047 0.02714  -0.02834 -0.05698 189 THR C O   
2873 C  CB  . THR C 189 ? 0.43729 0.51762 0.38824 0.03814  -0.02329 -0.04253 189 THR C CB  
2874 O  OG1 . THR C 189 ? 0.43670 0.52027 0.39518 0.02880  -0.02183 -0.05425 189 THR C OG1 
2875 C  CG2 . THR C 189 ? 0.43843 0.53635 0.37039 0.04333  -0.03023 -0.03808 189 THR C CG2 
2876 N  N   . PRO C 190 ? 0.41318 0.45598 0.40607 0.03283  -0.01329 -0.04571 190 PRO C N   
2877 C  CA  . PRO C 190 ? 0.38717 0.41644 0.40066 0.02621  -0.00848 -0.05249 190 PRO C CA  
2878 C  C   . PRO C 190 ? 0.38742 0.41579 0.40121 0.01831  -0.00128 -0.06101 190 PRO C C   
2879 O  O   . PRO C 190 ? 0.43147 0.44704 0.46111 0.01343  0.00429  -0.06552 190 PRO C O   
2880 C  CB  . PRO C 190 ? 0.36562 0.37756 0.38206 0.03135  -0.00170 -0.04385 190 PRO C CB  
2881 C  CG  . PRO C 190 ? 0.43872 0.45382 0.43233 0.03768  0.00222  -0.03514 190 PRO C CG  
2882 C  CD  . PRO C 190 ? 0.38072 0.41554 0.36086 0.04026  -0.00727 -0.03465 190 PRO C CD  
2883 N  N   . ASP C 191 ? 0.36222 0.40365 0.35974 0.01672  -0.00124 -0.06358 191 ASP C N   
2884 C  CA  . ASP C 191 ? 0.42896 0.46926 0.42656 0.00908  0.00608  -0.07176 191 ASP C CA  
2885 C  C   . ASP C 191 ? 0.41259 0.45696 0.42760 0.00089  0.00179  -0.08337 191 ASP C C   
2886 O  O   . ASP C 191 ? 0.44882 0.49478 0.47678 0.00111  -0.00605 -0.08474 191 ASP C O   
2887 C  CB  . ASP C 191 ? 0.46454 0.51724 0.43888 0.00989  0.00776  -0.07069 191 ASP C CB  
2888 C  CG  . ASP C 191 ? 0.66131 0.73404 0.62719 0.01026  -0.00262 -0.07322 191 ASP C CG  
2889 O  OD1 . ASP C 191 ? 0.65057 0.72860 0.62979 0.00730  -0.01024 -0.07904 191 ASP C OD1 
2890 O  OD2 . ASP C 191 ? 0.59983 0.68339 0.54520 0.01330  -0.00303 -0.06959 191 ASP C OD2 
2891 N  N   . THR C 192 ? 0.41800 0.46379 0.43388 -0.00661 0.00710  -0.09200 192 THR C N   
2892 C  CA  . THR C 192 ? 0.49615 0.54607 0.52801 -0.01464 0.00358  -0.10328 192 THR C CA  
2893 C  C   . THR C 192 ? 0.41808 0.48642 0.43877 -0.01835 -0.00072 -0.10981 192 THR C C   
2894 O  O   . THR C 192 ? 0.49625 0.56817 0.52791 -0.02589 -0.00166 -0.11994 192 THR C O   
2895 C  CB  . THR C 192 ? 0.46644 0.50249 0.51292 -0.02138 0.01283  -0.10952 192 THR C CB  
2896 O  OG1 . THR C 192 ? 0.51795 0.55182 0.55007 -0.02223 0.02237  -0.10865 192 THR C OG1 
2897 C  CG2 . THR C 192 ? 0.48503 0.50377 0.54704 -0.01881 0.01533  -0.10484 192 THR C CG2 
2898 N  N   . SER C 193 ? 0.47140 0.55146 0.47081 -0.01330 -0.00333 -0.10430 193 SER C N   
2899 C  CA  . SER C 193 ? 0.41909 0.51767 0.40690 -0.01633 -0.00805 -0.11001 193 SER C CA  
2900 C  C   . SER C 193 ? 0.35718 0.46601 0.35563 -0.01791 -0.01905 -0.11494 193 SER C C   
2901 O  O   . SER C 193 ? 0.39765 0.50793 0.39737 -0.01187 -0.02621 -0.10872 193 SER C O   
2902 C  CB  . SER C 193 ? 0.52774 0.63634 0.49091 -0.00951 -0.00935 -0.10168 193 SER C CB  
2903 O  OG  . SER C 193 ? 0.80445 0.90328 0.75701 -0.00746 0.00062  -0.09622 193 SER C OG  
2904 N  N   . PRO C 194 ? 0.41918 0.53530 0.42525 -0.02575 -0.02073 -0.12585 194 PRO C N   
2905 C  CA  . PRO C 194 ? 0.40230 0.52790 0.41881 -0.02742 -0.03114 -0.13067 194 PRO C CA  
2906 C  C   . PRO C 194 ? 0.47028 0.61151 0.47122 -0.02126 -0.04005 -0.12540 194 PRO C C   
2907 O  O   . PRO C 194 ? 0.43913 0.59090 0.42054 -0.01948 -0.03926 -0.12343 194 PRO C O   
2908 C  CB  . PRO C 194 ? 0.47545 0.60762 0.49773 -0.03689 -0.02970 -0.14304 194 PRO C CB  
2909 C  CG  . PRO C 194 ? 0.56648 0.68645 0.59048 -0.04081 -0.01804 -0.14512 194 PRO C CG  
2910 C  CD  . PRO C 194 ? 0.52650 0.64159 0.53335 -0.03371 -0.01288 -0.13451 194 PRO C CD  
2911 N  N   . ASN C 195 ? 0.37817 0.52103 0.38817 -0.01815 -0.04866 -0.12327 195 ASN C N   
2912 C  CA  . ASN C 195 ? 0.32653 0.48266 0.32383 -0.01164 -0.05734 -0.11748 195 ASN C CA  
2913 C  C   . ASN C 195 ? 0.34096 0.50599 0.34969 -0.01373 -0.06760 -0.12281 195 ASN C C   
2914 O  O   . ASN C 195 ? 0.36372 0.53847 0.36553 -0.00827 -0.07559 -0.11811 195 ASN C O   
2915 C  CB  . ASN C 195 ? 0.32595 0.47294 0.31924 -0.00252 -0.05699 -0.10519 195 ASN C CB  
2916 C  CG  . ASN C 195 ? 0.37325 0.50545 0.38738 -0.00231 -0.05763 -0.10413 195 ASN C CG  
2917 O  OD1 . ASN C 195 ? 0.29512 0.42389 0.32635 -0.00873 -0.05847 -0.11218 195 ASN C OD1 
2918 N  ND2 . ASN C 195 ? 0.35044 0.47425 0.36299 0.00517  -0.05747 -0.09408 195 ASN C ND2 
2919 N  N   . CYS C 196 ? 0.31428 0.47608 0.34046 -0.02132 -0.06757 -0.13225 196 CYS C N   
2920 C  CA  . CYS C 196 ? 0.40899 0.56296 0.44667 -0.02066 -0.07016 -0.12592 196 CYS C CA  
2921 C  C   . CYS C 196 ? 0.47943 0.62885 0.52253 -0.02657 -0.06520 -0.12764 196 CYS C C   
2922 O  O   . CYS C 196 ? 0.42111 0.56801 0.46883 -0.03204 -0.05938 -0.13461 196 CYS C O   
2923 C  CB  . CYS C 196 ? 0.35584 0.49543 0.41030 -0.01925 -0.07049 -0.12349 196 CYS C CB  
2924 S  SG  . CYS C 196 ? 0.38767 0.51554 0.44993 -0.01696 -0.07222 -0.11254 196 CYS C SG  
2925 N  N   . THR C 197 ? 0.42113 0.56883 0.46308 -0.02524 -0.06721 -0.12096 197 THR C N   
2926 C  CA  . THR C 197 ? 0.44827 0.59246 0.49325 -0.02928 -0.06363 -0.12126 197 THR C CA  
2927 C  C   . THR C 197 ? 0.52353 0.65333 0.57833 -0.02864 -0.06318 -0.11401 197 THR C C   
2928 O  O   . THR C 197 ? 0.50259 0.63043 0.55426 -0.02539 -0.06677 -0.10692 197 THR C O   
2929 C  CB  . THR C 197 ? 0.42083 0.57647 0.45271 -0.02851 -0.06578 -0.12028 197 THR C CB  
2930 O  OG1 . THR C 197 ? 0.40426 0.57284 0.42523 -0.02968 -0.06473 -0.12668 197 THR C OG1 
2931 C  CG2 . THR C 197 ? 0.41439 0.56561 0.45009 -0.03175 -0.06289 -0.11975 197 THR C CG2 
2932 N  N   . ILE C 198 ? 0.43421 0.38576 0.38225 -0.08265 -0.01003 -0.08592 198 ILE C N   
2933 C  CA  . ILE C 198 ? 0.56448 0.50811 0.52291 -0.08204 -0.00390 -0.08159 198 ILE C CA  
2934 C  C   . ILE C 198 ? 0.56789 0.49329 0.52098 -0.09370 0.00177  -0.08885 198 ILE C C   
2935 O  O   . ILE C 198 ? 0.71693 0.64691 0.67898 -0.10185 0.00174  -0.08903 198 ILE C O   
2936 C  CB  . ILE C 198 ? 0.49266 0.42447 0.45173 -0.06947 0.00272  -0.07440 198 ILE C CB  
2937 C  CG1 . ILE C 198 ? 0.41592 0.36335 0.37906 -0.05913 -0.00251 -0.06812 198 ILE C CG1 
2938 C  CG2 . ILE C 198 ? 0.50793 0.43563 0.47827 -0.06843 0.00842  -0.06887 198 ILE C CG2 
2939 C  CD1 . ILE C 198 ? 0.49290 0.42950 0.45389 -0.04829 0.00339  -0.06245 198 ILE C CD1 
2940 N  N   . ALA C 199 ? 0.53035 0.43400 0.46880 -0.09434 0.00738  -0.09467 199 ALA C N   
2941 C  CA  . ALA C 199 ? 0.59727 0.47825 0.52817 -0.10473 0.01422  -0.10254 199 ALA C CA  
2942 C  C   . ALA C 199 ? 0.62975 0.50470 0.54416 -0.11330 0.01225  -0.11441 199 ALA C C   
2943 O  O   . ALA C 199 ? 0.70593 0.56883 0.61497 -0.12633 0.01476  -0.12329 199 ALA C O   
2944 C  CB  . ALA C 199 ? 0.56780 0.42253 0.49611 -0.09654 0.02600  -0.09846 199 ALA C CB  
2945 N  N   . GLN C 200 ? 0.64799 0.53029 0.55369 -0.10663 0.00834  -0.11489 200 GLN C N   
2946 C  CA  . GLN C 200 ? 0.63838 0.52082 0.52828 -0.11422 0.00501  -0.12563 200 GLN C CA  
2947 C  C   . GLN C 200 ? 0.59757 0.50920 0.48926 -0.11037 -0.00584 -0.12206 200 GLN C C   
2948 O  O   . GLN C 200 ? 0.57054 0.49450 0.47218 -0.09915 -0.00837 -0.11170 200 GLN C O   
2949 C  CB  . GLN C 200 ? 0.78989 0.64787 0.66329 -0.10852 0.01330  -0.13003 200 GLN C CB  
2950 C  CG  . GLN C 200 ? 0.94372 0.77038 0.81464 -0.10785 0.02571  -0.13142 200 GLN C CG  
2951 C  CD  . GLN C 200 ? 0.84833 0.65439 0.70342 -0.09993 0.03365  -0.13476 200 GLN C CD  
2952 O  OE1 . GLN C 200 ? 0.76947 0.58630 0.61694 -0.09409 0.02970  -0.13450 200 GLN C OE1 
2953 N  NE2 . GLN C 200 ? 1.08424 0.86081 0.93444 -0.09919 0.04533  -0.13732 200 GLN C NE2 
2954 N  N   . ASP C 201 ? 0.56671 0.48899 0.44814 -0.11971 -0.01192 -0.13070 201 ASP C N   
2955 C  CA  . ASP C 201 ? 0.60692 0.55837 0.48977 -0.11649 -0.02235 -0.12683 201 ASP C CA  
2956 C  C   . ASP C 201 ? 0.61391 0.56384 0.49286 -0.10113 -0.02103 -0.11910 201 ASP C C   
2957 O  O   . ASP C 201 ? 0.58824 0.51968 0.45372 -0.09779 -0.01478 -0.12277 201 ASP C O   
2958 C  CB  . ASP C 201 ? 0.79929 0.76096 0.66886 -0.12931 -0.02804 -0.13813 201 ASP C CB  
2959 C  CG  . ASP C 201 ? 0.98558 0.98129 0.85821 -0.12723 -0.03947 -0.13337 201 ASP C CG  
2960 O  OD1 . ASP C 201 ? 0.96775 0.98447 0.85625 -0.12647 -0.04520 -0.12644 201 ASP C OD1 
2961 O  OD2 . ASP C 201 ? 1.12119 1.12306 0.98022 -0.12580 -0.04238 -0.13614 201 ASP C OD2 
2962 N  N   . LYS C 202 ? 0.50769 0.47645 0.39874 -0.09179 -0.02633 -0.10832 202 LYS C N   
2963 C  CA  . LYS C 202 ? 0.63661 0.60687 0.52540 -0.07836 -0.02613 -0.10023 202 LYS C CA  
2964 C  C   . LYS C 202 ? 0.55057 0.49541 0.43505 -0.07083 -0.01579 -0.09861 202 LYS C C   
2965 O  O   . LYS C 202 ? 0.54640 0.48414 0.41953 -0.06493 -0.01292 -0.09838 202 LYS C O   
2966 C  CB  . LYS C 202 ? 0.70945 0.69218 0.58480 -0.07908 -0.03173 -0.10297 202 LYS C CB  
2967 C  CG  . LYS C 202 ? 0.74014 0.75339 0.62266 -0.08069 -0.04252 -0.09913 202 LYS C CG  
2968 N  N   . ASP C 203 ? 0.55189 0.48469 0.44591 -0.07067 -0.01003 -0.09670 203 ASP C N   
2969 C  CA  . ASP C 203 ? 0.54263 0.45382 0.43423 -0.06313 -0.00014 -0.09402 203 ASP C CA  
2970 C  C   . ASP C 203 ? 0.51904 0.43636 0.42124 -0.05103 0.00027  -0.08253 203 ASP C C   
2971 O  O   . ASP C 203 ? 0.44831 0.35166 0.35028 -0.04414 0.00799  -0.07884 203 ASP C O   
2972 C  CB  . ASP C 203 ? 0.46638 0.35977 0.36131 -0.06902 0.00703  -0.09755 203 ASP C CB  
2973 C  CG  . ASP C 203 ? 0.50604 0.41099 0.41847 -0.07136 0.00417  -0.09242 203 ASP C CG  
2974 O  OD1 . ASP C 203 ? 0.52607 0.45204 0.44854 -0.06767 -0.00292 -0.08638 203 ASP C OD1 
2975 O  OD2 . ASP C 203 ? 0.58368 0.47584 0.49983 -0.07653 0.00973  -0.09415 203 ASP C OD2 
2976 N  N   . SER C 204 ? 0.42094 0.35878 0.33207 -0.04821 -0.00753 -0.07686 204 SER C N   
2977 C  CA  . SER C 204 ? 0.35088 0.29306 0.27195 -0.03802 -0.00683 -0.06710 204 SER C CA  
2978 C  C   . SER C 204 ? 0.42877 0.38963 0.35293 -0.03384 -0.01478 -0.06210 204 SER C C   
2979 O  O   . SER C 204 ? 0.40261 0.37730 0.32538 -0.03869 -0.02170 -0.06480 204 SER C O   
2980 C  CB  . SER C 204 ? 0.45173 0.39481 0.38742 -0.03832 -0.00487 -0.06379 204 SER C CB  
2981 O  OG  . SER C 204 ? 0.50912 0.46536 0.45190 -0.04594 -0.01066 -0.06658 204 SER C OG  
2982 N  N   . LYS C 205 ? 0.34300 0.30428 0.27136 -0.02477 -0.01343 -0.05440 205 LYS C N   
2983 C  CA  . LYS C 205 ? 0.34926 0.32518 0.28316 -0.01942 -0.01950 -0.04800 205 LYS C CA  
2984 C  C   . LYS C 205 ? 0.31684 0.29720 0.26599 -0.01582 -0.01928 -0.04308 205 LYS C C   
2985 O  O   . LYS C 205 ? 0.33563 0.30773 0.28810 -0.01157 -0.01395 -0.03978 205 LYS C O   
2986 C  CB  . LYS C 205 ? 0.38740 0.35971 0.31357 -0.01267 -0.01794 -0.04321 205 LYS C CB  
2987 C  CG  . LYS C 205 ? 0.40613 0.38891 0.33992 -0.00605 -0.02217 -0.03507 205 LYS C CG  
2988 C  CD  . LYS C 205 ? 0.40415 0.40308 0.33720 -0.00689 -0.03020 -0.03422 205 LYS C CD  
2989 C  CE  . LYS C 205 ? 0.36507 0.37233 0.30772 0.00038  -0.03346 -0.02588 205 LYS C CE  
2990 N  NZ  . LYS C 205 ? 0.48596 0.50563 0.42336 0.00276  -0.03932 -0.02196 205 LYS C NZ  
2991 N  N   . LEU C 206 ? 0.28732 0.28202 0.24552 -0.01756 -0.02491 -0.04277 206 LEU C N   
2992 C  CA  . LEU C 206 ? 0.32665 0.32806 0.29861 -0.01310 -0.02548 -0.03814 206 LEU C CA  
2993 C  C   . LEU C 206 ? 0.29269 0.30062 0.26582 -0.00582 -0.02902 -0.03217 206 LEU C C   
2994 O  O   . LEU C 206 ? 0.31704 0.33616 0.28809 -0.00566 -0.03472 -0.03133 206 LEU C O   
2995 C  CB  . LEU C 206 ? 0.28890 0.30315 0.27044 -0.01799 -0.02908 -0.04052 206 LEU C CB  
2996 C  CG  . LEU C 206 ? 0.30474 0.32785 0.30026 -0.01306 -0.02974 -0.03641 206 LEU C CG  
2997 C  CD1 . LEU C 206 ? 0.33434 0.34754 0.33412 -0.01252 -0.02320 -0.03597 206 LEU C CD1 
2998 C  CD2 . LEU C 206 ? 0.32310 0.36366 0.32683 -0.01720 -0.03477 -0.03807 206 LEU C CD2 
2999 N  N   . THR C 207 ? 0.25046 0.25173 0.22662 -0.00003 -0.02556 -0.02773 207 THR C N   
3000 C  CA  . THR C 207 ? 0.29348 0.29841 0.27199 0.00664  -0.02802 -0.02180 207 THR C CA  
3001 C  C   . THR C 207 ? 0.34903 0.36070 0.34088 0.00944  -0.02886 -0.02050 207 THR C C   
3002 O  O   . THR C 207 ? 0.29714 0.30409 0.29451 0.00958  -0.02475 -0.02107 207 THR C O   
3003 C  CB  . THR C 207 ? 0.33003 0.32371 0.30311 0.01029  -0.02374 -0.01799 207 THR C CB  
3004 O  OG1 . THR C 207 ? 0.31559 0.30309 0.27597 0.00795  -0.02193 -0.01975 207 THR C OG1 
3005 C  CG2 . THR C 207 ? 0.35168 0.34779 0.32609 0.01631  -0.02632 -0.01156 207 THR C CG2 
3006 N  N   . LEU C 208 ? 0.27847 0.30263 0.27537 0.01181  -0.03402 -0.01880 208 LEU C N   
3007 C  CA  . LEU C 208 ? 0.26104 0.29298 0.27035 0.01520  -0.03474 -0.01794 208 LEU C CA  
3008 C  C   . LEU C 208 ? 0.27251 0.30890 0.28413 0.02288  -0.03773 -0.01225 208 LEU C C   
3009 O  O   . LEU C 208 ? 0.28540 0.33067 0.29323 0.02381  -0.04228 -0.00991 208 LEU C O   
3010 C  CB  . LEU C 208 ? 0.27697 0.32249 0.29234 0.01034  -0.03753 -0.02166 208 LEU C CB  
3011 C  CG  . LEU C 208 ? 0.26906 0.32493 0.29753 0.01404  -0.03794 -0.02098 208 LEU C CG  
3012 C  CD1 . LEU C 208 ? 0.23610 0.28292 0.26915 0.01532  -0.03237 -0.02193 208 LEU C CD1 
3013 C  CD2 . LEU C 208 ? 0.28766 0.35967 0.32227 0.00843  -0.04099 -0.02400 208 LEU C CD2 
3014 N  N   . VAL C 209 ? 0.23475 0.26488 0.25211 0.02830  -0.03494 -0.00995 209 VAL C N   
3015 C  CA  . VAL C 209 ? 0.21315 0.24426 0.23367 0.03635  -0.03643 -0.00438 209 VAL C CA  
3016 C  C   . VAL C 209 ? 0.28672 0.32363 0.31894 0.04040  -0.03568 -0.00562 209 VAL C C   
3017 O  O   . VAL C 209 ? 0.25985 0.29048 0.29580 0.03906  -0.03166 -0.00902 209 VAL C O   
3018 C  CB  . VAL C 209 ? 0.24742 0.26259 0.26290 0.03894  -0.03287 -0.00071 209 VAL C CB  
3019 C  CG1 . VAL C 209 ? 0.27157 0.28573 0.28931 0.04736  -0.03408 0.00606  209 VAL C CG1 
3020 C  CG2 . VAL C 209 ? 0.32324 0.33330 0.32684 0.03444  -0.03261 -0.00025 209 VAL C CG2 
3021 N  N   . LEU C 210 ? 0.23646 0.28658 0.27428 0.04571  -0.03936 -0.00266 210 LEU C N   
3022 C  CA  . LEU C 210 ? 0.19604 0.25300 0.24508 0.05130  -0.03840 -0.00330 210 LEU C CA  
3023 C  C   . LEU C 210 ? 0.32454 0.37565 0.37525 0.06146  -0.03771 0.00287  210 LEU C C   
3024 O  O   . LEU C 210 ? 0.34060 0.40002 0.38997 0.06609  -0.04146 0.00887  210 LEU C O   
3025 C  CB  . LEU C 210 ? 0.25683 0.33554 0.31230 0.04995  -0.04261 -0.00430 210 LEU C CB  
3026 C  CG  . LEU C 210 ? 0.23004 0.31428 0.28391 0.03921  -0.04330 -0.00996 210 LEU C CG  
3027 C  CD1 . LEU C 210 ? 0.22890 0.33586 0.29017 0.03765  -0.04755 -0.01033 210 LEU C CD1 
3028 C  CD2 . LEU C 210 ? 0.23308 0.30774 0.28941 0.03566  -0.03795 -0.01481 210 LEU C CD2 
3029 N  N   . THR C 211 ? 0.25471 0.29195 0.30829 0.06493  -0.03278 0.00154  211 THR C N   
3030 C  CA  . THR C 211 ? 0.27174 0.29907 0.32661 0.07434  -0.03089 0.00710  211 THR C CA  
3031 C  C   . THR C 211 ? 0.35033 0.38170 0.41538 0.08154  -0.02855 0.00505  211 THR C C   
3032 O  O   . THR C 211 ? 0.29908 0.32723 0.36747 0.07858  -0.02512 -0.00175 211 THR C O   
3033 C  CB  . THR C 211 ? 0.41508 0.42046 0.46362 0.07198  -0.02658 0.00726  211 THR C CB  
3034 O  OG1 . THR C 211 ? 0.33243 0.33594 0.37140 0.06653  -0.02861 0.01000  211 THR C OG1 
3035 C  CG2 . THR C 211 ? 0.40537 0.39798 0.45550 0.08098  -0.02380 0.01273  211 THR C CG2 
3036 N  N   . LYS C 212 ? 0.28414 0.32373 0.35400 0.09146  -0.03014 0.01112  212 LYS C N   
3037 C  CA  . LYS C 212 ? 0.28375 0.33011 0.36364 0.09942  -0.02786 0.00944  212 LYS C CA  
3038 C  C   . LYS C 212 ? 0.56569 0.58937 0.64588 0.10572  -0.02144 0.00884  212 LYS C C   
3039 O  O   . LYS C 212 ? 0.45421 0.46542 0.53144 0.11196  -0.02026 0.01579  212 LYS C O   
3040 C  CB  . LYS C 212 ? 0.27947 0.34678 0.36536 0.10811  -0.03199 0.01655  212 LYS C CB  
3041 C  CG  . LYS C 212 ? 0.30413 0.38149 0.40100 0.11709  -0.02947 0.01517  212 LYS C CG  
3042 C  CD  . LYS C 212 ? 0.37280 0.47798 0.47632 0.12305  -0.03465 0.02173  212 LYS C CD  
3043 C  CE  . LYS C 212 ? 0.50842 0.62590 0.62353 0.13346  -0.03183 0.02144  212 LYS C CE  
3044 N  NZ  . LYS C 212 ? 0.37041 0.49310 0.48986 0.12695  -0.02961 0.01185  212 LYS C NZ  
3045 N  N   . CYS C 213 ? 0.39143 0.40944 0.47459 0.10328  -0.01712 0.00040  213 CYS C N   
3046 C  CA  . CYS C 213 ? 0.40040 0.39863 0.48467 0.10883  -0.01061 -0.00245 213 CYS C CA  
3047 C  C   . CYS C 213 ? 0.45241 0.46174 0.54607 0.11760  -0.00834 -0.00537 213 CYS C C   
3048 O  O   . CYS C 213 ? 0.49320 0.50544 0.58952 0.11423  -0.00567 -0.01383 213 CYS C O   
3049 C  CB  . CYS C 213 ? 0.38798 0.37166 0.46718 0.09872  -0.00719 -0.01039 213 CYS C CB  
3050 S  SG  . CYS C 213 ? 0.61820 0.59548 0.68730 0.08724  -0.01003 -0.00781 213 CYS C SG  
3051 N  N   . GLY C 214 ? 0.50770 0.52688 0.60654 0.12892  -0.00981 0.00234  214 GLY C N   
3052 C  CA  . GLY C 214 ? 0.45256 0.48481 0.56096 0.13877  -0.00758 0.00089  214 GLY C CA  
3053 C  C   . GLY C 214 ? 0.41908 0.47615 0.53233 0.13194  -0.01079 -0.00423 214 GLY C C   
3054 O  O   . GLY C 214 ? 0.51184 0.58669 0.62486 0.12572  -0.01694 -0.00116 214 GLY C O   
3055 N  N   . SER C 215 ? 0.38439 0.44173 0.50123 0.13184  -0.00629 -0.01267 215 SER C N   
3056 C  CA  . SER C 215 ? 0.40614 0.48745 0.52857 0.12646  -0.00840 -0.01675 215 SER C CA  
3057 C  C   . SER C 215 ? 0.33469 0.41662 0.45151 0.11132  -0.01096 -0.02102 215 SER C C   
3058 O  O   . SER C 215 ? 0.36560 0.46629 0.48668 0.10578  -0.01258 -0.02367 215 SER C O   
3059 C  CB  . SER C 215 ? 0.63429 0.71732 0.76229 0.13245  -0.00227 -0.02388 215 SER C CB  
3060 O  OG  . SER C 215 ? 0.78900 0.89676 0.92299 0.12770  -0.00406 -0.02666 215 SER C OG  
3061 N  N   . GLN C 216 ? 0.24207 0.30417 0.34987 0.10471  -0.01071 -0.02160 216 GLN C N   
3062 C  CA  . GLN C 216 ? 0.22889 0.29163 0.33144 0.09174  -0.01270 -0.02459 216 GLN C CA  
3063 C  C   . GLN C 216 ? 0.28223 0.34040 0.37795 0.08746  -0.01715 -0.01865 216 GLN C C   
3064 O  O   . GLN C 216 ? 0.29061 0.33565 0.38266 0.09257  -0.01695 -0.01377 216 GLN C O   
3065 C  CB  . GLN C 216 ? 0.34893 0.39482 0.44628 0.08593  -0.00805 -0.03152 216 GLN C CB  
3066 C  CG  . GLN C 216 ? 0.56436 0.61813 0.66594 0.08490  -0.00439 -0.03898 216 GLN C CG  
3067 C  CD  . GLN C 216 ? 0.27541 0.31461 0.37095 0.07813  -0.00061 -0.04526 216 GLN C CD  
3068 O  OE1 . GLN C 216 ? 0.29166 0.33147 0.38292 0.06873  -0.00180 -0.04576 216 GLN C OE1 
3069 N  NE2 . GLN C 216 ? 0.31663 0.34243 0.41165 0.08297  0.00423  -0.05002 216 GLN C NE2 
3070 N  N   . ILE C 217 ? 0.21551 0.28366 0.30913 0.07809  -0.02059 -0.01915 217 ILE C N   
3071 C  CA  . ILE C 217 ? 0.22198 0.28533 0.30761 0.07248  -0.02418 -0.01532 217 ILE C CA  
3072 C  C   . ILE C 217 ? 0.26913 0.31707 0.34761 0.06450  -0.02134 -0.01902 217 ILE C C   
3073 O  O   . ILE C 217 ? 0.26061 0.31267 0.34033 0.05848  -0.01963 -0.02378 217 ILE C O   
3074 C  CB  . ILE C 217 ? 0.18914 0.27161 0.27612 0.06685  -0.02925 -0.01414 217 ILE C CB  
3075 C  CG1 . ILE C 217 ? 0.25052 0.35272 0.34593 0.07430  -0.03223 -0.01037 217 ILE C CG1 
3076 C  CG2 . ILE C 217 ? 0.25534 0.33198 0.33258 0.06102  -0.03256 -0.01123 217 ILE C CG2 
3077 C  CD1 . ILE C 217 ? 0.29495 0.39199 0.38985 0.08526  -0.03284 -0.00348 217 ILE C CD1 
3078 N  N   . LEU C 218 ? 0.21967 0.25139 0.29097 0.06460  -0.02068 -0.01609 218 LEU C N   
3079 C  CA  . LEU C 218 ? 0.19409 0.21365 0.25848 0.05698  -0.01843 -0.01833 218 LEU C CA  
3080 C  C   . LEU C 218 ? 0.29281 0.31662 0.35114 0.05101  -0.02187 -0.01593 218 LEU C C   
3081 O  O   . LEU C 218 ? 0.26354 0.28769 0.31805 0.05332  -0.02506 -0.01086 218 LEU C O   
3082 C  CB  . LEU C 218 ? 0.25980 0.26022 0.31979 0.05942  -0.01552 -0.01635 218 LEU C CB  
3083 C  CG  . LEU C 218 ? 0.28469 0.27380 0.33793 0.05181  -0.01309 -0.01777 218 LEU C CG  
3084 C  CD1 . LEU C 218 ? 0.27400 0.26630 0.33013 0.04708  -0.00995 -0.02461 218 LEU C CD1 
3085 C  CD2 . LEU C 218 ? 0.30863 0.27958 0.35827 0.05420  -0.01051 -0.01475 218 LEU C CD2 
3086 N  N   . ALA C 219 ? 0.22188 0.24897 0.27895 0.04367  -0.02095 -0.01941 219 ALA C N   
3087 C  CA  . ALA C 219 ? 0.23580 0.26687 0.28756 0.03793  -0.02352 -0.01847 219 ALA C CA  
3088 C  C   . ALA C 219 ? 0.24040 0.26005 0.28459 0.03267  -0.02065 -0.01885 219 ALA C C   
3089 O  O   . ALA C 219 ? 0.27879 0.29468 0.32431 0.03069  -0.01688 -0.02132 219 ALA C O   
3090 C  CB  . ALA C 219 ? 0.24369 0.28939 0.30111 0.03410  -0.02463 -0.02143 219 ALA C CB  
3091 N  N   . ASN C 220 ? 0.19702 0.21273 0.23310 0.03059  -0.02234 -0.01630 220 ASN C N   
3092 C  CA  . ASN C 220 ? 0.21087 0.21704 0.23967 0.02652  -0.01934 -0.01610 220 ASN C CA  
3093 C  C   . ASN C 220 ? 0.26431 0.27330 0.28749 0.02181  -0.02069 -0.01711 220 ASN C C   
3094 O  O   . ASN C 220 ? 0.26142 0.27499 0.28148 0.02220  -0.02467 -0.01598 220 ASN C O   
3095 C  CB  . ASN C 220 ? 0.24262 0.23819 0.26559 0.02926  -0.01887 -0.01178 220 ASN C CB  
3096 C  CG  . ASN C 220 ? 0.34033 0.32785 0.35645 0.02556  -0.01543 -0.01101 220 ASN C CG  
3097 O  OD1 . ASN C 220 ? 0.32943 0.31522 0.33781 0.02397  -0.01604 -0.00952 220 ASN C OD1 
3098 N  ND2 . ASN C 220 ? 0.33575 0.31965 0.35453 0.02418  -0.01170 -0.01217 220 ASN C ND2 
3099 N  N   . VAL C 221 ? 0.19544 0.20197 0.21711 0.01743  -0.01724 -0.01922 221 VAL C N   
3100 C  CA  . VAL C 221 ? 0.20462 0.21164 0.22120 0.01264  -0.01761 -0.02115 221 VAL C CA  
3101 C  C   . VAL C 221 ? 0.22263 0.21979 0.23218 0.01047  -0.01284 -0.02085 221 VAL C C   
3102 O  O   . VAL C 221 ? 0.24027 0.23480 0.25208 0.01131  -0.00894 -0.01972 221 VAL C O   
3103 C  CB  . VAL C 221 ? 0.23178 0.24838 0.25576 0.00938  -0.01823 -0.02416 221 VAL C CB  
3104 C  CG1 . VAL C 221 ? 0.24309 0.25969 0.27266 0.00891  -0.01359 -0.02458 221 VAL C CG1 
3105 C  CG2 . VAL C 221 ? 0.26530 0.28149 0.28388 0.00338  -0.01906 -0.02679 221 VAL C CG2 
3106 N  N   . SER C 222 ? 0.22731 0.21990 0.22794 0.00789  -0.01305 -0.02190 222 SER C N   
3107 C  CA  . SER C 222 ? 0.27659 0.25992 0.27043 0.00620  -0.00787 -0.02218 222 SER C CA  
3108 C  C   . SER C 222 ? 0.29947 0.27977 0.28603 0.00162  -0.00853 -0.02615 222 SER C C   
3109 O  O   . SER C 222 ? 0.29243 0.27883 0.27786 -0.00034 -0.01359 -0.02809 222 SER C O   
3110 C  CB  . SER C 222 ? 0.32467 0.30153 0.31192 0.00934  -0.00578 -0.01863 222 SER C CB  
3111 O  OG  . SER C 222 ? 0.36283 0.33887 0.34193 0.00964  -0.00924 -0.01844 222 SER C OG  
3112 N  N   . LEU C 223 ? 0.26916 0.24010 0.25045 -0.00007 -0.00314 -0.02738 223 LEU C N   
3113 C  CA  . LEU C 223 ? 0.27954 0.24471 0.25319 -0.00528 -0.00271 -0.03239 223 LEU C CA  
3114 C  C   . LEU C 223 ? 0.33137 0.28389 0.29391 -0.00378 0.00282  -0.03260 223 LEU C C   
3115 O  O   . LEU C 223 ? 0.30332 0.25124 0.26721 -0.00005 0.00835  -0.02904 223 LEU C O   
3116 C  CB  . LEU C 223 ? 0.27444 0.23937 0.25445 -0.00980 -0.00050 -0.03468 223 LEU C CB  
3117 C  CG  . LEU C 223 ? 0.31183 0.26928 0.28492 -0.01686 0.00047  -0.04065 223 LEU C CG  
3118 C  CD1 . LEU C 223 ? 0.35388 0.32174 0.32538 -0.02128 -0.00711 -0.04432 223 LEU C CD1 
3119 C  CD2 . LEU C 223 ? 0.34407 0.29870 0.32413 -0.02043 0.00458  -0.04092 223 LEU C CD2 
3120 N  N   . ILE C 224 ? 0.28981 0.23836 0.24128 -0.00639 0.00137  -0.03664 224 ILE C N   
3121 C  CA  . ILE C 224 ? 0.32506 0.26086 0.26459 -0.00538 0.00716  -0.03842 224 ILE C CA  
3122 C  C   . ILE C 224 ? 0.39490 0.32305 0.32770 -0.01249 0.00801  -0.04624 224 ILE C C   
3123 O  O   . ILE C 224 ? 0.40285 0.33691 0.33103 -0.01736 0.00233  -0.05069 224 ILE C O   
3124 C  CB  . ILE C 224 ? 0.39592 0.33346 0.32605 -0.00221 0.00525  -0.03676 224 ILE C CB  
3125 C  CG1 . ILE C 224 ? 0.37347 0.31784 0.31046 0.00353  0.00420  -0.02912 224 ILE C CG1 
3126 C  CG2 . ILE C 224 ? 0.42310 0.34782 0.34003 -0.00108 0.01185  -0.03952 224 ILE C CG2 
3127 C  CD1 . ILE C 224 ? 0.41385 0.36279 0.34388 0.00574  0.00047  -0.02646 224 ILE C CD1 
3128 N  N   . VAL C 225 ? 0.37320 0.28848 0.30525 -0.01334 0.01521  -0.04782 225 VAL C N   
3129 C  CA  . VAL C 225 ? 0.38284 0.28637 0.30672 -0.02051 0.01762  -0.05593 225 VAL C CA  
3130 C  C   . VAL C 225 ? 0.40227 0.29301 0.31103 -0.01796 0.02276  -0.05913 225 VAL C C   
3131 O  O   . VAL C 225 ? 0.43077 0.31608 0.33827 -0.01023 0.02876  -0.05409 225 VAL C O   
3132 C  CB  . VAL C 225 ? 0.38942 0.28357 0.32006 -0.02272 0.02351  -0.05564 225 VAL C CB  
3133 C  CG1 . VAL C 225 ? 0.45703 0.33739 0.37913 -0.03139 0.02605  -0.06457 225 VAL C CG1 
3134 C  CG2 . VAL C 225 ? 0.39750 0.30659 0.34329 -0.02459 0.01862  -0.05198 225 VAL C CG2 
3135 N  N   . VAL C 226 ? 0.42265 0.31142 0.31988 -0.02423 0.01993  -0.06727 226 VAL C N   
3136 C  CA  . VAL C 226 ? 0.47007 0.34883 0.35147 -0.02208 0.02410  -0.07132 226 VAL C CA  
3137 C  C   . VAL C 226 ? 0.49183 0.35106 0.36232 -0.02811 0.03041  -0.08117 226 VAL C C   
3138 O  O   . VAL C 226 ? 0.54058 0.38768 0.39795 -0.02486 0.03649  -0.08462 226 VAL C O   
3139 C  CB  . VAL C 226 ? 0.52804 0.42096 0.40203 -0.02317 0.01631  -0.07250 226 VAL C CB  
3140 C  CG1 . VAL C 226 ? 0.55696 0.46507 0.44077 -0.01630 0.01173  -0.06231 226 VAL C CG1 
3141 C  CG2 . VAL C 226 ? 0.52448 0.42621 0.39737 -0.03360 0.00882  -0.07968 226 VAL C CG2 
3142 N  N   . ALA C 227 ? 0.45436 0.30958 0.32941 -0.03691 0.02963  -0.08603 227 ALA C N   
3143 C  CA  . ALA C 227 ? 0.49473 0.32964 0.35913 -0.04430 0.03563  -0.09629 227 ALA C CA  
3144 C  C   . ALA C 227 ? 0.52066 0.35007 0.39579 -0.05116 0.03711  -0.09668 227 ALA C C   
3145 O  O   . ALA C 227 ? 0.58391 0.42818 0.47369 -0.05094 0.03227  -0.09007 227 ALA C O   
3146 C  CB  . ALA C 227 ? 0.56289 0.40237 0.41380 -0.05344 0.02996  -0.10698 227 ALA C CB  
3147 N  N   . GLY C 228 ? 0.51916 0.32607 0.38648 -0.05726 0.04450  -0.10455 228 GLY C N   
3148 C  CA  . GLY C 228 ? 0.51047 0.31141 0.38634 -0.06594 0.04582  -0.10591 228 GLY C CA  
3149 C  C   . GLY C 228 ? 0.70459 0.49705 0.59178 -0.05793 0.05354  -0.09582 228 GLY C C   
3150 O  O   . GLY C 228 ? 0.53306 0.32210 0.42052 -0.04557 0.05899  -0.08839 228 GLY C O   
3151 N  N   . LYS C 229 ? 0.55034 0.34179 0.44751 -0.06548 0.05374  -0.09502 229 LYS C N   
3152 C  CA  . LYS C 229 ? 0.60449 0.38440 0.51058 -0.05991 0.06246  -0.08654 229 LYS C CA  
3153 C  C   . LYS C 229 ? 0.56725 0.36505 0.48575 -0.04806 0.06076  -0.07379 229 LYS C C   
3154 O  O   . LYS C 229 ? 0.58798 0.37753 0.51127 -0.03999 0.06877  -0.06566 229 LYS C O   
3155 C  CB  . LYS C 229 ? 0.62864 0.40462 0.54239 -0.07172 0.06288  -0.08839 229 LYS C CB  
3156 C  CG  . LYS C 229 ? 0.69539 0.49830 0.62453 -0.07493 0.05385  -0.08308 229 LYS C CG  
3157 C  CD  . LYS C 229 ? 0.86323 0.66283 0.79910 -0.08794 0.05447  -0.08554 229 LYS C CD  
3158 C  CE  . LYS C 229 ? 0.91404 0.69860 0.85705 -0.08391 0.06465  -0.07705 229 LYS C CE  
3159 N  NZ  . LYS C 229 ? 1.04832 0.84014 1.00278 -0.09487 0.06296  -0.07567 229 LYS C NZ  
3160 N  N   . TYR C 230 ? 0.50893 0.33107 0.43288 -0.04696 0.05082  -0.07168 230 TYR C N   
3161 C  CA  . TYR C 230 ? 0.41998 0.25830 0.35515 -0.03709 0.04919  -0.06093 230 TYR C CA  
3162 C  C   . TYR C 230 ? 0.39532 0.23697 0.32420 -0.02724 0.04925  -0.05817 230 TYR C C   
3163 O  O   . TYR C 230 ? 0.43132 0.28736 0.36840 -0.02001 0.04711  -0.05026 230 TYR C O   
3164 C  CB  . TYR C 230 ? 0.41347 0.27553 0.36038 -0.04140 0.03932  -0.05936 230 TYR C CB  
3165 C  CG  . TYR C 230 ? 0.43048 0.29248 0.38613 -0.05000 0.03994  -0.05974 230 TYR C CG  
3166 C  CD1 . TYR C 230 ? 0.43590 0.29417 0.40028 -0.04626 0.04640  -0.05202 230 TYR C CD1 
3167 C  CD2 . TYR C 230 ? 0.54024 0.40709 0.49518 -0.06207 0.03425  -0.06740 230 TYR C CD2 
3168 C  CE1 . TYR C 230 ? 0.45464 0.31318 0.42710 -0.05433 0.04741  -0.05156 230 TYR C CE1 
3169 C  CE2 . TYR C 230 ? 0.45620 0.32380 0.41951 -0.07076 0.03509  -0.06743 230 TYR C CE2 
3170 C  CZ  . TYR C 230 ? 0.51051 0.37313 0.48238 -0.06681 0.04187  -0.05944 230 TYR C CZ  
3171 O  OH  . TYR C 230 ? 0.55979 0.42366 0.53997 -0.07562 0.04296  -0.05877 230 TYR C OH  
3172 N  N   . HIS C 231 ? 0.44986 0.27869 0.36418 -0.02727 0.05199  -0.06470 231 HIS C N   
3173 C  CA  . HIS C 231 ? 0.44589 0.27940 0.35395 -0.01868 0.05186  -0.06201 231 HIS C CA  
3174 C  C   . HIS C 231 ? 0.48423 0.31265 0.39534 -0.00736 0.06048  -0.05308 231 HIS C C   
3175 O  O   . HIS C 231 ? 0.46257 0.30568 0.38007 -0.00068 0.05816  -0.04552 231 HIS C O   
3176 C  CB  . HIS C 231 ? 0.45293 0.27502 0.34386 -0.02158 0.05307  -0.07152 231 HIS C CB  
3177 C  CG  . HIS C 231 ? 0.56745 0.39403 0.45148 -0.01278 0.05389  -0.06831 231 HIS C CG  
3178 N  ND1 . HIS C 231 ? 0.60482 0.41814 0.47328 -0.01071 0.05933  -0.07407 231 HIS C ND1 
3179 C  CD2 . HIS C 231 ? 0.45752 0.30069 0.34806 -0.00600 0.05012  -0.05999 231 HIS C CD2 
3180 C  CE1 . HIS C 231 ? 0.56544 0.38834 0.43166 -0.00276 0.05883  -0.06865 231 HIS C CE1 
3181 N  NE2 . HIS C 231 ? 0.48722 0.32773 0.36676 -0.00023 0.05322  -0.06009 231 HIS C NE2 
3182 N  N   . ILE C 232 ? 0.46669 0.27461 0.37341 -0.00522 0.07067  -0.05367 232 ILE C N   
3183 C  CA  . ILE C 232 ? 0.46477 0.26776 0.37412 0.00619  0.07988  -0.04465 232 ILE C CA  
3184 C  C   . ILE C 232 ? 0.54155 0.33819 0.46065 0.00522  0.08477  -0.03984 232 ILE C C   
3185 O  O   . ILE C 232 ? 0.57506 0.35123 0.48935 0.00036  0.09048  -0.04495 232 ILE C O   
3186 C  CB  . ILE C 232 ? 0.50189 0.28495 0.39687 0.01168  0.08927  -0.04846 232 ILE C CB  
3187 C  CG1 . ILE C 232 ? 0.60053 0.38923 0.48413 0.01150  0.08469  -0.05411 232 ILE C CG1 
3188 C  CG2 . ILE C 232 ? 0.51918 0.30115 0.41839 0.02473  0.09859  -0.03752 232 ILE C CG2 
3189 C  CD1 . ILE C 232 ? 0.67579 0.48480 0.56474 0.01907  0.08119  -0.04549 232 ILE C CD1 
3190 N  N   . ILE C 233 ? 0.45691 0.27013 0.38900 0.00983  0.08331  -0.02997 233 ILE C N   
3191 C  CA  . ILE C 233 ? 0.43013 0.24162 0.37231 0.00913  0.08713  -0.02409 233 ILE C CA  
3192 C  C   . ILE C 233 ? 0.50024 0.29890 0.44117 0.01968  0.09918  -0.01635 233 ILE C C   
3193 O  O   . ILE C 233 ? 0.46822 0.27581 0.40951 0.02958  0.10158  -0.00974 233 ILE C O   
3194 C  CB  . ILE C 233 ? 0.39641 0.23357 0.35256 0.00941  0.08001  -0.01730 233 ILE C CB  
3195 C  CG1 . ILE C 233 ? 0.46032 0.31114 0.41813 0.00092  0.06844  -0.02403 233 ILE C CG1 
3196 C  CG2 . ILE C 233 ? 0.47932 0.31676 0.44579 0.00916  0.08435  -0.01029 233 ILE C CG2 
3197 C  CD1 . ILE C 233 ? 0.53980 0.38084 0.49445 -0.01041 0.06605  -0.03289 233 ILE C CD1 
3198 N  N   . ASN C 234 ? 0.47918 0.25736 0.41908 0.01768  0.10708  -0.01656 234 ASN C N   
3199 C  CA  . ASN C 234 ? 0.44811 0.21463 0.38901 0.02861  0.11920  -0.00706 234 ASN C CA  
3200 C  C   . ASN C 234 ? 0.48330 0.24404 0.43293 0.02477  0.12280  -0.00201 234 ASN C C   
3201 O  O   . ASN C 234 ? 0.57825 0.31645 0.52303 0.01706  0.12675  -0.00842 234 ASN C O   
3202 C  CB  . ASN C 234 ? 0.52317 0.26289 0.44990 0.03325  0.12899  -0.01228 234 ASN C CB  
3203 C  CG  . ASN C 234 ? 0.59321 0.32459 0.52193 0.04729  0.14156  -0.00062 234 ASN C CG  
3204 O  OD1 . ASN C 234 ? 0.61127 0.34629 0.55032 0.04992  0.14498  0.00935  234 ASN C OD1 
3205 N  ND2 . ASN C 234 ? 0.59593 0.32010 0.51553 0.05641  0.14781  -0.00081 234 ASN C ND2 
3206 N  N   . ASN C 235 ? 0.48399 0.26589 0.44627 0.02939  0.12130  0.00925  235 ASN C N   
3207 C  CA  . ASN C 235 ? 0.45850 0.23858 0.42986 0.02632  0.12454  0.01564  235 ASN C CA  
3208 C  C   . ASN C 235 ? 0.54013 0.30272 0.51140 0.03632  0.13822  0.02579  235 ASN C C   
3209 O  O   . ASN C 235 ? 0.56550 0.32519 0.54404 0.03461  0.14216  0.03257  235 ASN C O   
3210 C  CB  . ASN C 235 ? 0.45867 0.27019 0.44318 0.02632  0.11691  0.02281  235 ASN C CB  
3211 C  CG  . ASN C 235 ? 0.54393 0.37066 0.53010 0.01606  0.10429  0.01352  235 ASN C CG  
3212 O  OD1 . ASN C 235 ? 0.51482 0.36449 0.50564 0.01852  0.09734  0.01528  235 ASN C OD1 
3213 N  ND2 . ASN C 235 ? 0.49006 0.30427 0.47250 0.00447  0.10152  0.00370  235 ASN C ND2 
3214 N  N   . LYS C 236 ? 0.52713 0.28011 0.49126 0.04761  0.14580  0.02837  236 LYS C N   
3215 C  CA  . LYS C 236 ? 0.56304 0.29485 0.52510 0.05615  0.15933  0.03587  236 LYS C CA  
3216 C  C   . LYS C 236 ? 0.73496 0.43973 0.68786 0.04576  0.16206  0.02447  236 LYS C C   
3217 O  O   . LYS C 236 ? 0.73043 0.42415 0.68643 0.04368  0.16783  0.02843  236 LYS C O   
3218 C  CB  . LYS C 236 ? 0.61242 0.35064 0.57001 0.06981  0.16435  0.04119  236 LYS C CB  
3219 N  N   . THR C 237 ? 0.59932 0.29473 0.54123 0.03820  0.15731  0.01007  237 THR C N   
3220 C  CA  . THR C 237 ? 0.68310 0.35548 0.61590 0.02694  0.15861  -0.00192 237 THR C CA  
3221 C  C   . THR C 237 ? 0.73428 0.40602 0.67230 0.01143  0.15224  -0.00762 237 THR C C   
3222 O  O   . THR C 237 ? 0.78866 0.44492 0.72596 0.00348  0.15565  -0.01045 237 THR C O   
3223 C  CB  . THR C 237 ? 0.66244 0.32785 0.58106 0.02485  0.15591  -0.01470 237 THR C CB  
3224 O  OG1 . THR C 237 ? 0.88868 0.56782 0.80694 0.01831  0.14529  -0.02180 237 THR C OG1 
3225 C  CG2 . THR C 237 ? 0.76158 0.43023 0.67588 0.03998  0.16205  -0.00833 237 THR C CG2 
3226 N  N   . ASN C 238 ? 0.63785 0.32639 0.58115 0.00648  0.14312  -0.00957 238 ASN C N   
3227 C  CA  . ASN C 238 ? 0.56204 0.25976 0.51166 -0.00856 0.13453  -0.01471 238 ASN C CA  
3228 C  C   . ASN C 238 ? 0.68536 0.41320 0.65049 -0.00514 0.12916  -0.00291 238 ASN C C   
3229 O  O   . ASN C 238 ? 0.57333 0.32759 0.54289 -0.00630 0.11832  -0.00436 238 ASN C O   
3230 C  CB  . ASN C 238 ? 0.72598 0.43309 0.66911 -0.01885 0.12305  -0.02851 238 ASN C CB  
3231 C  CG  . ASN C 238 ? 0.86207 0.54542 0.78837 -0.02025 0.12713  -0.04037 238 ASN C CG  
3232 O  OD1 . ASN C 238 ? 1.00500 0.69208 0.92443 -0.01134 0.12704  -0.04106 238 ASN C OD1 
3233 N  ND2 . ASN C 238 ? 0.94530 0.61258 0.86601 -0.03159 0.12837  -0.04909 238 ASN C ND2 
3234 N  N   . PRO C 239 ? 0.69514 0.41963 0.66853 -0.00132 0.13664  0.00868  239 PRO C N   
3235 C  CA  . PRO C 239 ? 0.56020 0.31471 0.54758 0.00215  0.13194  0.01981  239 PRO C CA  
3236 C  C   . PRO C 239 ? 0.58122 0.35433 0.57620 -0.01072 0.12129  0.01485  239 PRO C C   
3237 O  O   . PRO C 239 ? 0.64733 0.44804 0.65251 -0.00806 0.11568  0.02147  239 PRO C O   
3238 C  CB  . PRO C 239 ? 0.60371 0.34611 0.59626 0.00875  0.14398  0.03319  239 PRO C CB  
3239 C  CG  . PRO C 239 ? 0.81781 0.52250 0.80107 0.00228  0.15277  0.02620  239 PRO C CG  
3240 C  CD  . PRO C 239 ? 0.60213 0.29590 0.57193 0.00132  0.15024  0.01280  239 PRO C CD  
3241 N  N   . LYS C 240 ? 0.55559 0.31651 0.54595 -0.02443 0.11813  0.00320  240 LYS C N   
3242 C  CA  . LYS C 240 ? 0.66353 0.44425 0.66244 -0.03587 0.10870  -0.00007 240 LYS C CA  
3243 C  C   . LYS C 240 ? 0.68223 0.48301 0.67950 -0.03901 0.09627  -0.00899 240 LYS C C   
3244 O  O   . LYS C 240 ? 0.70981 0.53144 0.71525 -0.04582 0.08803  -0.01043 240 LYS C O   
3245 C  CB  . LYS C 240 ? 0.83866 0.59987 0.83588 -0.05051 0.11156  -0.00651 240 LYS C CB  
3246 N  N   . ILE C 241 ? 0.54117 0.33680 0.52843 -0.03367 0.09511  -0.01424 241 ILE C N   
3247 C  CA  . ILE C 241 ? 0.64385 0.45669 0.62875 -0.03610 0.08397  -0.02192 241 ILE C CA  
3248 C  C   . ILE C 241 ? 0.45126 0.29014 0.44471 -0.02669 0.07932  -0.01389 241 ILE C C   
3249 O  O   . ILE C 241 ? 0.50181 0.34125 0.49198 -0.01626 0.08199  -0.00974 241 ILE C O   
3250 C  CB  . ILE C 241 ? 0.56144 0.35840 0.53166 -0.03477 0.08497  -0.03053 241 ILE C CB  
3251 C  CG1 . ILE C 241 ? 0.64889 0.41969 0.60984 -0.04549 0.08961  -0.04005 241 ILE C CG1 
3252 C  CG2 . ILE C 241 ? 0.73712 0.55297 0.70526 -0.03631 0.07373  -0.03660 241 ILE C CG2 
3253 C  CD1 . ILE C 241 ? 1.05647 0.81206 1.00175 -0.04513 0.09064  -0.04988 241 ILE C CD1 
3254 N  N   . LYS C 242 ? 0.44646 0.30734 0.45089 -0.03063 0.07270  -0.01189 242 LYS C N   
3255 C  CA  . LYS C 242 ? 0.40343 0.28819 0.41625 -0.02292 0.06899  -0.00493 242 LYS C CA  
3256 C  C   . LYS C 242 ? 0.37824 0.28492 0.39627 -0.02697 0.05811  -0.00962 242 LYS C C   
3257 O  O   . LYS C 242 ? 0.36578 0.29148 0.39072 -0.02161 0.05509  -0.00500 242 LYS C O   
3258 C  CB  . LYS C 242 ? 0.42771 0.31933 0.45044 -0.02017 0.07444  0.00565  242 LYS C CB  
3259 C  CG  . LYS C 242 ? 0.57176 0.44339 0.59126 -0.01448 0.08610  0.01297  242 LYS C CG  
3260 C  CD  . LYS C 242 ? 0.52244 0.39323 0.53682 -0.00256 0.08942  0.01710  242 LYS C CD  
3261 C  CE  . LYS C 242 ? 0.77334 0.66129 0.79605 0.00661  0.09283  0.02969  242 LYS C CE  
3262 N  NZ  . LYS C 242 ? 0.68395 0.56806 0.70196 0.01805  0.09872  0.03548  242 LYS C NZ  
3263 N  N   . SER C 243 ? 0.37059 0.27573 0.38557 -0.03612 0.05244  -0.01850 243 SER C N   
3264 C  CA  . SER C 243 ? 0.33814 0.26476 0.35884 -0.03885 0.04264  -0.02187 243 SER C CA  
3265 C  C   . SER C 243 ? 0.43830 0.36139 0.45323 -0.04830 0.03720  -0.03146 243 SER C C   
3266 O  O   . SER C 243 ? 0.42970 0.33587 0.43884 -0.05577 0.04092  -0.03581 243 SER C O   
3267 C  CB  . SER C 243 ? 0.38403 0.32824 0.41758 -0.04101 0.04152  -0.01711 243 SER C CB  
3268 O  OG  . SER C 243 ? 0.49970 0.43691 0.53534 -0.05093 0.04392  -0.01868 243 SER C OG  
3269 N  N   . PHE C 244 ? 0.37192 0.31159 0.38854 -0.04811 0.02850  -0.03465 244 PHE C N   
3270 C  CA  . PHE C 244 ? 0.36362 0.30718 0.37695 -0.05696 0.02197  -0.04256 244 PHE C CA  
3271 C  C   . PHE C 244 ? 0.36550 0.33301 0.38633 -0.05437 0.01337  -0.04203 244 PHE C C   
3272 O  O   . PHE C 244 ? 0.33211 0.30840 0.35764 -0.04573 0.01282  -0.03718 244 PHE C O   
3273 C  CB  . PHE C 244 ? 0.33551 0.26379 0.33448 -0.05778 0.02211  -0.04892 244 PHE C CB  
3274 C  CG  . PHE C 244 ? 0.34037 0.26998 0.33461 -0.04737 0.02098  -0.04652 244 PHE C CG  
3275 C  CD1 . PHE C 244 ? 0.36434 0.30897 0.35885 -0.04529 0.01292  -0.04785 244 PHE C CD1 
3276 C  CD2 . PHE C 244 ? 0.36986 0.28619 0.35982 -0.03957 0.02835  -0.04221 244 PHE C CD2 
3277 C  CE1 . PHE C 244 ? 0.36544 0.31048 0.35595 -0.03652 0.01231  -0.04515 244 PHE C CE1 
3278 C  CE2 . PHE C 244 ? 0.35236 0.27114 0.33849 -0.03104 0.02742  -0.03978 244 PHE C CE2 
3279 C  CZ  . PHE C 244 ? 0.35155 0.28394 0.33784 -0.03000 0.01945  -0.04140 244 PHE C CZ  
3280 N  N   . THR C 245 ? 0.32643 0.30461 0.34830 -0.06201 0.00692  -0.04712 245 THR C N   
3281 C  CA  . THR C 245 ? 0.33816 0.33956 0.36817 -0.05921 -0.00065 -0.04604 245 THR C CA  
3282 C  C   . THR C 245 ? 0.33333 0.33996 0.35630 -0.06117 -0.00764 -0.05115 245 THR C C   
3283 O  O   . THR C 245 ? 0.35508 0.35469 0.37033 -0.06991 -0.00832 -0.05713 245 THR C O   
3284 C  CB  . THR C 245 ? 0.45311 0.47012 0.49499 -0.06559 -0.00198 -0.04493 245 THR C CB  
3285 O  OG1 . THR C 245 ? 0.40905 0.42085 0.45642 -0.06377 0.00501  -0.03953 245 THR C OG1 
3286 C  CG2 . THR C 245 ? 0.40686 0.44816 0.45810 -0.06059 -0.00862 -0.04302 245 THR C CG2 
3287 N  N   . ILE C 246 ? 0.35337 0.37256 0.37890 -0.05318 -0.01261 -0.04871 246 ILE C N   
3288 C  CA  . ILE C 246 ? 0.34671 0.37552 0.36769 -0.05329 -0.01977 -0.05137 246 ILE C CA  
3289 C  C   . ILE C 246 ? 0.35387 0.40695 0.38700 -0.05152 -0.02556 -0.04890 246 ILE C C   
3290 O  O   . ILE C 246 ? 0.32251 0.38161 0.36365 -0.04364 -0.02465 -0.04440 246 ILE C O   
3291 C  CB  . ILE C 246 ? 0.31595 0.33676 0.32891 -0.04421 -0.01976 -0.04943 246 ILE C CB  
3292 C  CG1 . ILE C 246 ? 0.34502 0.34371 0.34532 -0.04587 -0.01406 -0.05223 246 ILE C CG1 
3293 C  CG2 . ILE C 246 ? 0.30318 0.33772 0.31417 -0.04187 -0.02732 -0.04952 246 ILE C CG2 
3294 C  CD1 . ILE C 246 ? 0.39473 0.38583 0.38812 -0.03699 -0.01280 -0.04935 246 ILE C CD1 
3295 N  N   . LYS C 247 ? 0.33610 0.40391 0.37071 -0.05895 -0.03119 -0.05203 247 LYS C N   
3296 C  CA  . LYS C 247 ? 0.27064 0.36373 0.31759 -0.05746 -0.03634 -0.04940 247 LYS C CA  
3297 C  C   . LYS C 247 ? 0.30624 0.41406 0.35104 -0.05350 -0.04370 -0.04874 247 LYS C C   
3298 O  O   . LYS C 247 ? 0.31497 0.42226 0.35042 -0.05957 -0.04695 -0.05274 247 LYS C O   
3299 C  CB  . LYS C 247 ? 0.33211 0.43606 0.38553 -0.06952 -0.03700 -0.05205 247 LYS C CB  
3300 C  CG  . LYS C 247 ? 0.32099 0.41212 0.37755 -0.07353 -0.02965 -0.05141 247 LYS C CG  
3301 C  CD  . LYS C 247 ? 0.40940 0.51292 0.47394 -0.08565 -0.03020 -0.05299 247 LYS C CD  
3302 C  CE  . LYS C 247 ? 0.57037 0.66033 0.63823 -0.08867 -0.02213 -0.05078 247 LYS C CE  
3303 N  NZ  . LYS C 247 ? 0.50859 0.61050 0.58536 -0.10046 -0.02187 -0.05112 247 LYS C NZ  
3304 N  N   . LEU C 248 ? 0.29364 0.41476 0.34683 -0.04317 -0.04600 -0.04363 248 LEU C N   
3305 C  CA  . LEU C 248 ? 0.25225 0.39113 0.30645 -0.03822 -0.05278 -0.04113 248 LEU C CA  
3306 C  C   . LEU C 248 ? 0.24167 0.40653 0.31001 -0.03812 -0.05593 -0.03884 248 LEU C C   
3307 O  O   . LEU C 248 ? 0.25044 0.41852 0.32840 -0.03191 -0.05293 -0.03600 248 LEU C O   
3308 C  CB  . LEU C 248 ? 0.24211 0.37361 0.29407 -0.02511 -0.05224 -0.03640 248 LEU C CB  
3309 C  CG  . LEU C 248 ? 0.40365 0.51541 0.44179 -0.02329 -0.05070 -0.03699 248 LEU C CG  
3310 C  CD1 . LEU C 248 ? 0.43899 0.52885 0.47148 -0.02761 -0.04399 -0.04023 248 LEU C CD1 
3311 C  CD2 . LEU C 248 ? 0.38643 0.49457 0.42504 -0.01078 -0.05056 -0.03133 248 LEU C CD2 
3312 N  N   . LEU C 249 ? 0.25785 0.44219 0.32724 -0.04551 -0.06175 -0.04039 249 LEU C N   
3313 C  CA  . LEU C 249 ? 0.22957 0.44189 0.31245 -0.04723 -0.06507 -0.03833 249 LEU C CA  
3314 C  C   . LEU C 249 ? 0.28770 0.52215 0.37303 -0.03935 -0.07175 -0.03364 249 LEU C C   
3315 O  O   . LEU C 249 ? 0.33158 0.56562 0.40696 -0.04102 -0.07567 -0.03454 249 LEU C O   
3316 C  CB  . LEU C 249 ? 0.29025 0.51051 0.37333 -0.06407 -0.06656 -0.04373 249 LEU C CB  
3317 C  CG  . LEU C 249 ? 0.53292 0.72741 0.60953 -0.07385 -0.06010 -0.04890 249 LEU C CG  
3318 C  CD1 . LEU C 249 ? 0.60946 0.80963 0.68408 -0.09134 -0.06197 -0.05500 249 LEU C CD1 
3319 C  CD2 . LEU C 249 ? 0.41322 0.60191 0.49896 -0.06968 -0.05377 -0.04587 249 LEU C CD2 
3320 N  N   . PHE C 250 ? 0.25959 0.51329 0.35773 -0.02985 -0.07262 -0.02820 250 PHE C N   
3321 C  CA  . PHE C 250 ? 0.21700 0.49067 0.31838 -0.01957 -0.07792 -0.02209 250 PHE C CA  
3322 C  C   . PHE C 250 ? 0.32664 0.63522 0.44180 -0.02094 -0.08197 -0.01928 250 PHE C C   
3323 O  O   . PHE C 250 ? 0.28903 0.60449 0.41407 -0.02411 -0.07902 -0.02024 250 PHE C O   
3324 C  CB  . PHE C 250 ? 0.24891 0.51093 0.35243 -0.00267 -0.07430 -0.01679 250 PHE C CB  
3325 C  CG  . PHE C 250 ? 0.25913 0.48916 0.35071 -0.00074 -0.07008 -0.01869 250 PHE C CG  
3326 C  CD1 . PHE C 250 ? 0.25715 0.47948 0.33789 0.00226  -0.07264 -0.01673 250 PHE C CD1 
3327 C  CD2 . PHE C 250 ? 0.21422 0.42396 0.30552 -0.00185 -0.06358 -0.02184 250 PHE C CD2 
3328 C  CE1 . PHE C 250 ? 0.24636 0.44108 0.31657 0.00387  -0.06861 -0.01804 250 PHE C CE1 
3329 C  CE2 . PHE C 250 ? 0.27086 0.45354 0.35162 -0.00018 -0.05978 -0.02312 250 PHE C CE2 
3330 C  CZ  . PHE C 250 ? 0.27702 0.45239 0.34749 0.00267  -0.06229 -0.02122 250 PHE C CZ  
3331 N  N   . ASN C 251 ? 0.33220 0.66476 0.44852 -0.01778 -0.08858 -0.01495 251 ASN C N   
3332 C  CA  . ASN C 251 ? 0.24290 0.60907 0.37244 -0.01724 -0.09182 -0.01094 251 ASN C CA  
3333 C  C   . ASN C 251 ? 0.31537 0.68735 0.45503 0.00158  -0.08891 -0.00321 251 ASN C C   
3334 O  O   . ASN C 251 ? 0.26007 0.61234 0.39815 0.01246  -0.08483 -0.00213 251 ASN C O   
3335 C  CB  . ASN C 251 ? 0.26062 0.64282 0.38410 -0.02329 -0.09769 -0.00961 251 ASN C CB  
3336 C  CG  . ASN C 251 ? 0.35542 0.74105 0.47370 -0.01042 -0.10105 -0.00278 251 ASN C CG  
3337 O  OD1 . ASN C 251 ? 0.34573 0.72394 0.46710 0.00491  -0.09876 0.00246  251 ASN C OD1 
3338 N  ND2 . ASN C 251 ? 0.33272 0.73027 0.44318 -0.01648 -0.10613 -0.00240 251 ASN C ND2 
3339 N  N   . LYS C 252 ? 0.29877 0.69160 0.44647 0.00541  -0.08937 0.00196  252 LYS C N   
3340 C  CA  . LYS C 252 ? 0.24259 0.64002 0.39977 0.02238  -0.08551 0.00839  252 LYS C CA  
3341 C  C   . LYS C 252 ? 0.33320 0.72325 0.48689 0.03829  -0.08605 0.01459  252 LYS C C   
3342 O  O   . LYS C 252 ? 0.30159 0.68551 0.46104 0.05301  -0.08142 0.01831  252 LYS C O   
3343 C  CB  . LYS C 252 ? 0.33203 0.75492 0.49736 0.02246  -0.08622 0.01271  252 LYS C CB  
3344 N  N   . ASN C 253 ? 0.24474 0.63406 0.38851 0.03548  -0.09108 0.01570  253 ASN C N   
3345 C  CA  . ASN C 253 ? 0.29916 0.67997 0.43789 0.04915  -0.09174 0.02221  253 ASN C CA  
3346 C  C   . ASN C 253 ? 0.34286 0.69538 0.47252 0.04937  -0.08975 0.01828  253 ASN C C   
3347 O  O   . ASN C 253 ? 0.26342 0.60245 0.38647 0.05917  -0.08919 0.02345  253 ASN C O   
3348 C  CB  . ASN C 253 ? 0.39514 0.79093 0.52668 0.04616  -0.09776 0.02646  253 ASN C CB  
3349 C  CG  . ASN C 253 ? 0.54604 0.96704 0.68560 0.05068  -0.09855 0.03290  253 ASN C CG  
3350 O  OD1 . ASN C 253 ? 0.41005 0.83338 0.55898 0.06345  -0.09427 0.03786  253 ASN C OD1 
3351 N  ND2 . ASN C 253 ? 0.43873 0.87874 0.57429 0.03976  -0.10368 0.03220  253 ASN C ND2 
3352 N  N   . GLY C 254 ? 0.29145 0.62509 0.41762 0.03800  -0.08606 0.00955  254 GLY C N   
3353 C  CA  . GLY C 254 ? 0.28280 0.58059 0.39687 0.03617  -0.08163 0.00536  254 GLY C CA  
3354 C  C   . GLY C 254 ? 0.25239 0.54213 0.35205 0.02663  -0.08526 0.00268  254 GLY C C   
3355 O  O   . GLY C 254 ? 0.28595 0.54875 0.37516 0.02785  -0.08211 0.00141  254 GLY C O   
3356 N  N   . VAL C 255 ? 0.24617 0.55986 0.34484 0.01694  -0.09178 0.00161  255 VAL C N   
3357 C  CA  . VAL C 255 ? 0.31207 0.62082 0.39628 0.00709  -0.09547 -0.00200 255 VAL C CA  
3358 C  C   . VAL C 255 ? 0.34053 0.63242 0.41869 -0.00882 -0.09268 -0.01242 255 VAL C C   
3359 O  O   . VAL C 255 ? 0.27310 0.57405 0.35955 -0.01691 -0.09192 -0.01620 255 VAL C O   
3360 C  CB  . VAL C 255 ? 0.37539 0.71954 0.46088 0.00388  -0.10394 0.00138  255 VAL C CB  
3361 C  CG1 . VAL C 255 ? 0.30578 0.64647 0.37544 -0.00843 -0.10778 -0.00430 255 VAL C CG1 
3362 C  CG2 . VAL C 255 ? 0.32324 0.68186 0.41400 0.02146  -0.10592 0.01322  255 VAL C CG2 
3363 N  N   . LEU C 256 ? 0.28931 0.55615 0.35322 -0.01270 -0.09053 -0.01646 256 LEU C N   
3364 C  CA  . LEU C 256 ? 0.37744 0.62470 0.43443 -0.02607 -0.08681 -0.02570 256 LEU C CA  
3365 C  C   . LEU C 256 ? 0.34897 0.61395 0.40421 -0.04210 -0.09156 -0.03201 256 LEU C C   
3366 O  O   . LEU C 256 ? 0.38588 0.66900 0.43563 -0.04520 -0.09794 -0.03158 256 LEU C O   
3367 C  CB  . LEU C 256 ? 0.32701 0.54655 0.36875 -0.02525 -0.08367 -0.02779 256 LEU C CB  
3368 C  CG  . LEU C 256 ? 0.28714 0.48038 0.32164 -0.03459 -0.07768 -0.03564 256 LEU C CG  
3369 C  CD1 . LEU C 256 ? 0.29254 0.47216 0.33637 -0.02945 -0.07104 -0.03440 256 LEU C CD1 
3370 C  CD2 . LEU C 256 ? 0.31957 0.49254 0.33865 -0.03309 -0.07592 -0.03681 256 LEU C CD2 
3371 N  N   . LEU C 257 ? 0.33288 0.59328 0.39271 -0.05277 -0.08839 -0.03773 257 LEU C N   
3372 C  CA  . LEU C 257 ? 0.36544 0.63952 0.42395 -0.06989 -0.09192 -0.04460 257 LEU C CA  
3373 C  C   . LEU C 257 ? 0.55597 0.80509 0.59781 -0.08099 -0.08948 -0.05354 257 LEU C C   
3374 O  O   . LEU C 257 ? 0.40960 0.62903 0.44443 -0.07696 -0.08313 -0.05477 257 LEU C O   
3375 C  CB  . LEU C 257 ? 0.32974 0.61107 0.40156 -0.07649 -0.08923 -0.04578 257 LEU C CB  
3376 C  CG  . LEU C 257 ? 0.30551 0.61563 0.39403 -0.06650 -0.09176 -0.03772 257 LEU C CG  
3377 C  CD1 . LEU C 257 ? 0.34595 0.65988 0.44674 -0.07188 -0.08772 -0.03856 257 LEU C CD1 
3378 C  CD2 . LEU C 257 ? 0.40209 0.74437 0.49277 -0.06778 -0.09946 -0.03453 257 LEU C CD2 
3379 N  N   . ASP C 258 ? 0.36645 0.62870 0.40183 -0.09519 -0.09443 -0.06005 258 ASP C N   
3380 C  CA  . ASP C 258 ? 0.58039 0.82095 0.59802 -0.10489 -0.09263 -0.06910 258 ASP C CA  
3381 C  C   . ASP C 258 ? 0.39097 0.60108 0.40551 -0.11342 -0.08435 -0.07596 258 ASP C C   
3382 O  O   . ASP C 258 ? 0.51731 0.70168 0.51742 -0.11600 -0.08021 -0.08170 258 ASP C O   
3383 C  CB  . ASP C 258 ? 0.61009 0.87099 0.62113 -0.11832 -0.09919 -0.07498 258 ASP C CB  
3384 C  CG  . ASP C 258 ? 0.80382 1.09388 0.81810 -0.10873 -0.10607 -0.06636 258 ASP C CG  
3385 O  OD1 . ASP C 258 ? 0.88146 1.19082 0.91082 -0.09913 -0.10774 -0.05748 258 ASP C OD1 
3386 O  OD2 . ASP C 258 ? 1.08336 1.37666 1.08497 -0.11032 -0.10921 -0.06822 258 ASP C OD2 
3387 N  N   . ASN C 259 ? 0.37277 0.58507 0.40034 -0.11691 -0.08132 -0.07481 259 ASN C N   
3388 C  CA  . ASN C 259 ? 0.45145 0.63448 0.47678 -0.12319 -0.07277 -0.07934 259 ASN C CA  
3389 C  C   . ASN C 259 ? 0.34656 0.50734 0.37361 -0.10883 -0.06581 -0.07356 259 ASN C C   
3390 O  O   . ASN C 259 ? 0.45843 0.59831 0.48627 -0.11164 -0.05850 -0.07495 259 ASN C O   
3391 C  CB  . ASN C 259 ? 0.42946 0.62384 0.46706 -0.13484 -0.07200 -0.08057 259 ASN C CB  
3392 C  CG  . ASN C 259 ? 0.57839 0.80094 0.63378 -0.12632 -0.07513 -0.07180 259 ASN C CG  
3393 O  OD1 . ASN C 259 ? 0.57277 0.81520 0.63139 -0.11557 -0.08059 -0.06620 259 ASN C OD1 
3394 N  ND2 . ASN C 259 ? 0.52779 0.75166 0.59466 -0.13052 -0.07109 -0.07019 259 ASN C ND2 
3395 N  N   . SER C 260 ? 0.34898 0.51428 0.37688 -0.09390 -0.06772 -0.06684 260 SER C N   
3396 C  CA  . SER C 260 ? 0.32543 0.46754 0.35163 -0.08230 -0.06124 -0.06304 260 SER C CA  
3397 C  C   . SER C 260 ? 0.35906 0.47348 0.36901 -0.08523 -0.05665 -0.06853 260 SER C C   
3398 O  O   . SER C 260 ? 0.39036 0.50511 0.38876 -0.09245 -0.05963 -0.07431 260 SER C O   
3399 C  CB  . SER C 260 ? 0.32300 0.47469 0.35278 -0.06688 -0.06417 -0.05520 260 SER C CB  
3400 O  OG  . SER C 260 ? 0.31654 0.49484 0.36061 -0.06301 -0.06836 -0.05021 260 SER C OG  
3401 N  N   . ASN C 261 ? 0.37535 0.46686 0.38422 -0.07916 -0.04919 -0.06662 261 ASN C N   
3402 C  CA  . ASN C 261 ? 0.34076 0.40665 0.33490 -0.07937 -0.04410 -0.07054 261 ASN C CA  
3403 C  C   . ASN C 261 ? 0.40643 0.47361 0.39128 -0.07117 -0.04733 -0.06842 261 ASN C C   
3404 O  O   . ASN C 261 ? 0.42537 0.47964 0.39596 -0.07398 -0.04583 -0.07327 261 ASN C O   
3405 C  CB  . ASN C 261 ? 0.36178 0.40698 0.35854 -0.07356 -0.03557 -0.06737 261 ASN C CB  
3406 C  CG  . ASN C 261 ? 0.35971 0.39959 0.36314 -0.08213 -0.03100 -0.06923 261 ASN C CG  
3407 O  OD1 . ASN C 261 ? 0.39675 0.45079 0.41340 -0.08159 -0.03200 -0.06536 261 ASN C OD1 
3408 N  ND2 . ASN C 261 ? 0.48492 0.50408 0.47896 -0.09007 -0.02558 -0.07510 261 ASN C ND2 
3409 N  N   . LEU C 262 ? 0.33117 0.41259 0.32371 -0.06070 -0.05104 -0.06102 262 LEU C N   
3410 C  CA  . LEU C 262 ? 0.32089 0.40524 0.30664 -0.05215 -0.05414 -0.05706 262 LEU C CA  
3411 C  C   . LEU C 262 ? 0.39172 0.49716 0.37316 -0.05724 -0.06202 -0.05897 262 LEU C C   
3412 O  O   . LEU C 262 ? 0.37410 0.50138 0.36497 -0.06108 -0.06696 -0.05847 262 LEU C O   
3413 C  CB  . LEU C 262 ? 0.33200 0.42280 0.32852 -0.03947 -0.05462 -0.04838 262 LEU C CB  
3414 C  CG  . LEU C 262 ? 0.32578 0.42050 0.31805 -0.02952 -0.05764 -0.04227 262 LEU C CG  
3415 C  CD1 . LEU C 262 ? 0.34251 0.41574 0.32217 -0.02701 -0.05290 -0.04278 262 LEU C CD1 
3416 C  CD2 . LEU C 262 ? 0.33437 0.43482 0.33961 -0.01867 -0.05738 -0.03498 262 LEU C CD2 
3417 N  N   . GLY C 263 ? 0.37060 0.47171 0.33795 -0.05702 -0.06324 -0.06069 263 GLY C N   
3418 C  CA  . GLY C 263 ? 0.43749 0.56064 0.39946 -0.06152 -0.07100 -0.06209 263 GLY C CA  
3419 C  C   . GLY C 263 ? 0.39633 0.54164 0.36661 -0.05065 -0.07680 -0.05204 263 GLY C C   
3420 O  O   . GLY C 263 ? 0.36406 0.50213 0.33754 -0.03852 -0.07453 -0.04444 263 GLY C O   
3421 N  N   . LYS C 264 ? 0.39431 0.60051 0.32309 0.02154  -0.10565 -0.10897 264 LYS C N   
3422 C  CA  . LYS C 264 ? 0.42933 0.63995 0.36506 0.02622  -0.10926 -0.09748 264 LYS C CA  
3423 C  C   . LYS C 264 ? 0.51054 0.72376 0.43083 0.03149  -0.10833 -0.08621 264 LYS C C   
3424 O  O   . LYS C 264 ? 0.42007 0.63281 0.34570 0.03548  -0.10787 -0.07466 264 LYS C O   
3425 C  CB  . LYS C 264 ? 0.46940 0.69166 0.41091 0.02647  -0.11992 -0.10134 264 LYS C CB  
3426 C  CG  . LYS C 264 ? 0.57588 0.79613 0.53635 0.02215  -0.12143 -0.10956 264 LYS C CG  
3427 C  CD  . LYS C 264 ? 0.70275 0.93551 0.66659 0.02243  -0.13224 -0.11370 264 LYS C CD  
3428 C  CE  . LYS C 264 ? 0.63507 0.87571 0.59857 0.02846  -0.13743 -0.10163 264 LYS C CE  
3429 N  NZ  . LYS C 264 ? 0.53787 0.77221 0.51757 0.03045  -0.13356 -0.09233 264 LYS C NZ  
3430 N  N   . ALA C 265 ? 0.41254 0.62856 0.31372 0.03157  -0.10813 -0.08934 265 ALA C N   
3431 C  CA  . ALA C 265 ? 0.46535 0.68503 0.35075 0.03645  -0.10806 -0.07919 265 ALA C CA  
3432 C  C   . ALA C 265 ? 0.50955 0.71902 0.39581 0.03833  -0.09879 -0.06901 265 ALA C C   
3433 O  O   . ALA C 265 ? 0.60075 0.81241 0.48012 0.04300  -0.09889 -0.05762 265 ALA C O   
3434 C  CB  . ALA C 265 ? 0.53563 0.75975 0.40052 0.03559  -0.10911 -0.08568 265 ALA C CB  
3435 N  N   . TYR C 266 ? 0.51397 0.71240 0.40952 0.03473  -0.09104 -0.07277 266 TYR C N   
3436 C  CA  . TYR C 266 ? 0.58535 0.77304 0.48030 0.03534  -0.08115 -0.06559 266 TYR C CA  
3437 C  C   . TYR C 266 ? 0.40274 0.58401 0.31597 0.03624  -0.07810 -0.05780 266 TYR C C   
3438 O  O   . TYR C 266 ? 0.46698 0.63941 0.38085 0.03704  -0.07008 -0.05058 266 TYR C O   
3439 C  CB  . TYR C 266 ? 0.49987 0.67923 0.39236 0.03051  -0.07411 -0.07536 266 TYR C CB  
3440 C  CG  . TYR C 266 ? 0.84764 1.03234 0.72279 0.02917  -0.07646 -0.08413 266 TYR C CG  
3441 C  CD1 . TYR C 266 ? 0.81590 1.00082 0.67262 0.03143  -0.07296 -0.07986 266 TYR C CD1 
3442 C  CD2 . TYR C 266 ? 0.67267 0.86206 0.54963 0.02558  -0.08200 -0.09671 266 TYR C CD2 
3443 C  CE1 . TYR C 266 ? 0.72456 0.91428 0.56521 0.03027  -0.07493 -0.08778 266 TYR C CE1 
3444 C  CE2 . TYR C 266 ? 0.83434 1.02840 0.69513 0.02437  -0.08404 -0.10470 266 TYR C CE2 
3445 C  CZ  . TYR C 266 ? 0.82691 1.02110 0.66962 0.02677  -0.08044 -0.10019 266 TYR C CZ  
3446 O  OH  . TYR C 266 ? 0.99287 1.19170 0.81931 0.02561  -0.08234 -0.10815 266 TYR C OH  
3447 N  N   . TRP C 267 ? 0.37798 0.56378 0.30557 0.03628  -0.08438 -0.05875 267 TRP C N   
3448 C  CA  . TRP C 267 ? 0.37457 0.55382 0.32189 0.03591  -0.08157 -0.05441 267 TRP C CA  
3449 C  C   . TRP C 267 ? 0.41380 0.59930 0.36584 0.04107  -0.08705 -0.04347 267 TRP C C   
3450 O  O   . TRP C 267 ? 0.38767 0.58316 0.34234 0.04211  -0.09597 -0.04583 267 TRP C O   
3451 C  CB  . TRP C 267 ? 0.34893 0.52719 0.31076 0.03085  -0.08360 -0.06619 267 TRP C CB  
3452 C  CG  . TRP C 267 ? 0.38705 0.55952 0.36975 0.03001  -0.08154 -0.06317 267 TRP C CG  
3453 C  CD1 . TRP C 267 ? 0.35940 0.53738 0.35642 0.03049  -0.08810 -0.06347 267 TRP C CD1 
3454 C  CD2 . TRP C 267 ? 0.32032 0.48034 0.31236 0.02833  -0.07219 -0.05980 267 TRP C CD2 
3455 N  NE1 . TRP C 267 ? 0.31896 0.48867 0.33336 0.02934  -0.08338 -0.06031 267 TRP C NE1 
3456 C  CE2 . TRP C 267 ? 0.30820 0.46679 0.31984 0.02794  -0.07364 -0.05801 267 TRP C CE2 
3457 C  CE3 . TRP C 267 ? 0.31817 0.46839 0.30378 0.02723  -0.06278 -0.05776 267 TRP C CE3 
3458 C  CZ2 . TRP C 267 ? 0.30115 0.44877 0.32597 0.02628  -0.06608 -0.05470 267 TRP C CZ2 
3459 C  CZ3 . TRP C 267 ? 0.30340 0.44245 0.30276 0.02550  -0.05510 -0.05431 267 TRP C CZ3 
3460 C  CH2 . TRP C 267 ? 0.29195 0.42992 0.31022 0.02509  -0.05689 -0.05273 267 TRP C CH2 
3461 N  N   . ASN C 268 ? 0.36910 0.54890 0.32218 0.04434  -0.08189 -0.03144 268 ASN C N   
3462 C  CA  . ASN C 268 ? 0.37689 0.56281 0.33204 0.04973  -0.08708 -0.02036 268 ASN C CA  
3463 C  C   . ASN C 268 ? 0.37240 0.54898 0.33321 0.05212  -0.07972 -0.00839 268 ASN C C   
3464 O  O   . ASN C 268 ? 0.36507 0.53129 0.32594 0.04979  -0.07084 -0.00845 268 ASN C O   
3465 C  CB  . ASN C 268 ? 0.39698 0.59307 0.33278 0.05350  -0.09277 -0.01696 268 ASN C CB  
3466 C  CG  . ASN C 268 ? 0.44468 0.65130 0.38418 0.05787  -0.10213 -0.01096 268 ASN C CG  
3467 O  OD1 . ASN C 268 ? 0.42510 0.63096 0.38101 0.05897  -0.10374 -0.00709 268 ASN C OD1 
3468 N  ND2 . ASN C 268 ? 0.47533 0.69201 0.39931 0.06037  -0.10836 -0.01027 268 ASN C ND2 
3469 N  N   . PHE C 269 ? 0.37724 0.55767 0.34265 0.05684  -0.08358 0.00197  269 PHE C N   
3470 C  CA  . PHE C 269 ? 0.37608 0.54871 0.34459 0.05982  -0.07738 0.01449  269 PHE C CA  
3471 C  C   . PHE C 269 ? 0.39958 0.57008 0.34889 0.06182  -0.07262 0.02066  269 PHE C C   
3472 O  O   . PHE C 269 ? 0.41357 0.59154 0.34656 0.06282  -0.07649 0.01841  269 PHE C O   
3473 C  CB  . PHE C 269 ? 0.40494 0.58303 0.38197 0.06468  -0.08336 0.02394  269 PHE C CB  
3474 C  CG  . PHE C 269 ? 0.42215 0.59929 0.42055 0.06285  -0.08551 0.02018  269 PHE C CG  
3475 C  CD1 . PHE C 269 ? 0.42400 0.59031 0.43687 0.06163  -0.07844 0.02385  269 PHE C CD1 
3476 C  CD2 . PHE C 269 ? 0.57605 0.76281 0.58004 0.06190  -0.09421 0.01230  269 PHE C CD2 
3477 C  CE1 . PHE C 269 ? 0.67956 0.84481 0.71201 0.05972  -0.08011 0.02008  269 PHE C CE1 
3478 C  CE2 . PHE C 269 ? 0.68168 0.86749 0.70551 0.05997  -0.09592 0.00850  269 PHE C CE2 
3479 C  CZ  . PHE C 269 ? 0.51898 0.69399 0.55703 0.05888  -0.08882 0.01237  269 PHE C CZ  
3480 N  N   . ARG C 270 ? 0.38505 0.54526 0.33655 0.06232  -0.06410 0.02851  270 ARG C N   
3481 C  CA  . ARG C 270 ? 0.39302 0.54902 0.32805 0.06320  -0.05770 0.03341  270 ARG C CA  
3482 C  C   . ARG C 270 ? 0.52240 0.68392 0.44539 0.06901  -0.06082 0.04546  270 ARG C C   
3483 O  O   . ARG C 270 ? 0.41802 0.58125 0.34922 0.07267  -0.06405 0.05412  270 ARG C O   
3484 C  CB  . ARG C 270 ? 0.38073 0.52340 0.32366 0.06118  -0.04724 0.03699  270 ARG C CB  
3485 C  CG  . ARG C 270 ? 0.38994 0.52779 0.31910 0.06344  -0.04063 0.04645  270 ARG C CG  
3486 C  CD  . ARG C 270 ? 0.37672 0.50137 0.31344 0.06048  -0.03001 0.04783  270 ARG C CD  
3487 N  NE  . ARG C 270 ? 0.39758 0.51771 0.32077 0.06243  -0.02348 0.05665  270 ARG C NE  
3488 C  CZ  . ARG C 270 ? 0.69053 0.80435 0.61701 0.06498  -0.01879 0.06858  270 ARG C CZ  
3489 N  NH1 . ARG C 270 ? 0.52353 0.63424 0.46692 0.06594  -0.01953 0.07331  270 ARG C NH1 
3490 N  NH2 . ARG C 270 ? 0.57577 0.68609 0.48867 0.06642  -0.01304 0.07566  270 ARG C NH2 
3491 N  N   . SER C 271 ? 0.42346 0.58765 0.32677 0.06980  -0.05973 0.04593  271 SER C N   
3492 C  CA  . SER C 271 ? 0.43940 0.60623 0.32913 0.07475  -0.06005 0.05799  271 SER C CA  
3493 C  C   . SER C 271 ? 0.47466 0.63551 0.34947 0.07353  -0.05178 0.05890  271 SER C C   
3494 O  O   . SER C 271 ? 0.45113 0.61614 0.31221 0.07185  -0.05262 0.05148  271 SER C O   
3495 C  CB  . SER C 271 ? 0.49768 0.67787 0.37663 0.07778  -0.07013 0.05776  271 SER C CB  
3496 O  OG  . SER C 271 ? 0.50633 0.68888 0.37080 0.08228  -0.07011 0.06907  271 SER C OG  
3497 N  N   . GLY C 272 ? 0.47463 0.62599 0.35180 0.07443  -0.04387 0.06809  272 GLY C N   
3498 C  CA  . GLY C 272 ? 0.47067 0.61602 0.33460 0.07317  -0.03556 0.06919  272 GLY C CA  
3499 C  C   . GLY C 272 ? 0.45237 0.59271 0.31951 0.06757  -0.03090 0.05662  272 GLY C C   
3500 O  O   . GLY C 272 ? 0.48304 0.61707 0.36687 0.06454  -0.02828 0.05239  272 GLY C O   
3501 N  N   . ASN C 273 ? 0.46519 0.60797 0.31624 0.06612  -0.02952 0.05067  273 ASN C N   
3502 C  CA  . ASN C 273 ? 0.43065 0.57028 0.28310 0.06098  -0.02641 0.03763  273 ASN C CA  
3503 C  C   . ASN C 273 ? 0.47825 0.62739 0.32914 0.05958  -0.03498 0.02649  273 ASN C C   
3504 O  O   . ASN C 273 ? 0.44772 0.59596 0.29596 0.05566  -0.03347 0.01518  273 ASN C O   
3505 C  CB  . ASN C 273 ? 0.43867 0.57438 0.27538 0.05982  -0.01900 0.03689  273 ASN C CB  
3506 C  CG  . ASN C 273 ? 0.44244 0.56652 0.28463 0.05899  -0.00896 0.04347  273 ASN C CG  
3507 O  OD1 . ASN C 273 ? 0.43249 0.55013 0.29175 0.05780  -0.00669 0.04508  273 ASN C OD1 
3508 N  ND2 . ASN C 273 ? 0.61580 0.73719 0.44351 0.05959  -0.00282 0.04748  273 ASN C ND2 
3509 N  N   . SER C 274 ? 0.44061 0.59885 0.29292 0.06272  -0.04395 0.02950  274 SER C N   
3510 C  CA  . SER C 274 ? 0.45324 0.62122 0.30415 0.06157  -0.05267 0.01949  274 SER C CA  
3511 C  C   . SER C 274 ? 0.49175 0.66228 0.36115 0.06191  -0.05866 0.01924  274 SER C C   
3512 O  O   . SER C 274 ? 0.43726 0.60015 0.32186 0.06163  -0.05462 0.02374  274 SER C O   
3513 C  CB  . SER C 274 ? 0.46415 0.64272 0.29614 0.06505  -0.05872 0.02254  274 SER C CB  
3514 O  OG  . SER C 274 ? 0.66343 0.85100 0.49260 0.06337  -0.06645 0.01181  274 SER C OG  
3515 N  N   . ASN C 275 ? 0.47609 0.65739 0.34420 0.06253  -0.06820 0.01417  275 ASN C N   
3516 C  CA  . ASN C 275 ? 0.43391 0.61949 0.31836 0.06309  -0.07499 0.01350  275 ASN C CA  
3517 C  C   . ASN C 275 ? 0.49210 0.68749 0.37151 0.06846  -0.08288 0.02252  275 ASN C C   
3518 O  O   . ASN C 275 ? 0.50256 0.70379 0.36445 0.07098  -0.08505 0.02594  275 ASN C O   
3519 C  CB  . ASN C 275 ? 0.42792 0.61822 0.31719 0.05893  -0.08006 -0.00080 275 ASN C CB  
3520 C  CG  . ASN C 275 ? 0.46446 0.64490 0.36331 0.05362  -0.07311 -0.00949 275 ASN C CG  
3521 O  OD1 . ASN C 275 ? 0.45121 0.62153 0.35831 0.05310  -0.06548 -0.00443 275 ASN C OD1 
3522 N  ND2 . ASN C 275 ? 0.55343 0.73665 0.45169 0.04957  -0.07576 -0.02252 275 ASN C ND2 
3523 N  N   . VAL C 276 ? 0.44176 0.63899 0.33701 0.07016  -0.08723 0.02623  276 VAL C N   
3524 C  CA  . VAL C 276 ? 0.45412 0.66176 0.34657 0.07500  -0.09596 0.03328  276 VAL C CA  
3525 C  C   . VAL C 276 ? 0.59744 0.81697 0.47961 0.07417  -0.10446 0.02431  276 VAL C C   
3526 O  O   . VAL C 276 ? 0.52700 0.74680 0.40954 0.06963  -0.10464 0.01187  276 VAL C O   
3527 C  CB  . VAL C 276 ? 0.57004 0.77755 0.48289 0.07654  -0.09914 0.03736  276 VAL C CB  
3528 C  CG1 . VAL C 276 ? 0.48566 0.68134 0.40795 0.07743  -0.09069 0.04651  276 VAL C CG1 
3529 C  CG2 . VAL C 276 ? 0.46832 0.67719 0.39521 0.07212  -0.10217 0.02494  276 VAL C CG2 
3530 N  N   . SER C 277 ? 0.73013 0.95959 0.60291 0.07861  -0.11164 0.03087  277 SER C N   
3531 C  CA  . SER C 277 ? 0.90317 1.14393 0.76222 0.07822  -0.11907 0.02387  277 SER C CA  
3532 C  C   . SER C 277 ? 0.92737 1.17557 0.79778 0.07593  -0.12705 0.01389  277 SER C C   
3533 O  O   . SER C 277 ? 1.05014 1.30470 0.91195 0.07335  -0.13112 0.00378  277 SER C O   
3534 C  CB  . SER C 277 ? 0.89165 1.14064 0.73677 0.08365  -0.12415 0.03443  277 SER C CB  
3535 O  OG  . SER C 277 ? 0.98306 1.23395 0.83992 0.08782  -0.12785 0.04441  277 SER C OG  
3536 N  N   . THR C 278 ? 0.51847 0.76634 0.40771 0.07682  -0.12953 0.01644  278 THR C N   
3537 C  CA  . THR C 278 ? 0.46992 0.72548 0.37041 0.07495  -0.13744 0.00782  278 THR C CA  
3538 C  C   . THR C 278 ? 0.44985 0.69702 0.36809 0.07015  -0.13289 -0.00033 278 THR C C   
3539 O  O   . THR C 278 ? 0.46443 0.70116 0.39256 0.07007  -0.12556 0.00480  278 THR C O   
3540 C  CB  . THR C 278 ? 0.59739 0.86093 0.50606 0.07981  -0.14515 0.01649  278 THR C CB  
3541 O  OG1 . THR C 278 ? 0.72464 0.99635 0.61631 0.08418  -0.14973 0.02391  278 THR C OG1 
3542 C  CG2 . THR C 278 ? 0.81746 1.08968 0.73760 0.07789  -0.15358 0.00753  278 THR C CG2 
3543 N  N   . ALA C 279 ? 0.45661 0.70844 0.37867 0.06608  -0.13731 -0.01298 279 ALA C N   
3544 C  CA  . ALA C 279 ? 0.50564 0.75035 0.44413 0.06116  -0.13372 -0.02173 279 ALA C CA  
3545 C  C   . ALA C 279 ? 0.61091 0.85426 0.56995 0.06282  -0.13505 -0.01623 279 ALA C C   
3546 O  O   . ALA C 279 ? 0.54822 0.80085 0.51147 0.06616  -0.14296 -0.01218 279 ALA C O   
3547 C  CB  . ALA C 279 ? 0.59933 0.85067 0.53704 0.05679  -0.13935 -0.03600 279 ALA C CB  
3548 N  N   . TYR C 280 ? 0.43577 0.66765 0.40792 0.06041  -0.12734 -0.01629 280 TYR C N   
3549 C  CA  . TYR C 280 ? 0.45226 0.68190 0.44372 0.06207  -0.12773 -0.01048 280 TYR C CA  
3550 C  C   . TYR C 280 ? 0.41627 0.65303 0.42153 0.05974  -0.13505 -0.01925 280 TYR C C   
3551 O  O   . TYR C 280 ? 0.44689 0.68612 0.45040 0.05528  -0.13707 -0.03135 280 TYR C O   
3552 C  CB  . TYR C 280 ? 0.42367 0.63906 0.42530 0.05988  -0.11739 -0.00836 280 TYR C CB  
3553 C  CG  . TYR C 280 ? 0.45428 0.66307 0.46429 0.05339  -0.11322 -0.02067 280 TYR C CG  
3554 C  CD1 . TYR C 280 ? 0.34577 0.55433 0.37498 0.05071  -0.11533 -0.02626 280 TYR C CD1 
3555 C  CD2 . TYR C 280 ? 0.40953 0.61183 0.40869 0.04997  -0.10678 -0.02634 280 TYR C CD2 
3556 C  CE1 . TYR C 280 ? 0.34937 0.55164 0.38616 0.04471  -0.11145 -0.03729 280 TYR C CE1 
3557 C  CE2 . TYR C 280 ? 0.43355 0.62934 0.44065 0.04406  -0.10278 -0.03733 280 TYR C CE2 
3558 C  CZ  . TYR C 280 ? 0.47784 0.67359 0.50361 0.04142  -0.10516 -0.04270 280 TYR C CZ  
3559 O  OH  . TYR C 280 ? 0.37595 0.56503 0.40954 0.03549  -0.10116 -0.05339 280 TYR C OH  
3560 N  N   . GLU C 281 ? 0.55905 0.79913 0.57823 0.06283  -0.13905 -0.01299 281 GLU C N   
3561 C  CA  . GLU C 281 ? 0.42250 0.66959 0.45607 0.06103  -0.14603 -0.02018 281 GLU C CA  
3562 C  C   . GLU C 281 ? 0.35839 0.59699 0.41307 0.05813  -0.14144 -0.02236 281 GLU C C   
3563 O  O   . GLU C 281 ? 0.38965 0.63169 0.45553 0.05462  -0.14525 -0.03174 281 GLU C O   
3564 C  CB  . GLU C 281 ? 0.59272 0.85160 0.62763 0.06648  -0.15522 -0.01280 281 GLU C CB  
3565 N  N   . LYS C 282 ? 0.41131 0.63910 0.47165 0.05937  -0.13346 -0.01410 282 LYS C N   
3566 C  CA  . LYS C 282 ? 0.33222 0.55156 0.41257 0.05674  -0.12873 -0.01542 282 LYS C CA  
3567 C  C   . LYS C 282 ? 0.50458 0.70989 0.58330 0.05507  -0.11761 -0.01222 282 LYS C C   
3568 O  O   . LYS C 282 ? 0.39104 0.59291 0.46002 0.05871  -0.11388 -0.00219 282 LYS C O   
3569 C  CB  . LYS C 282 ? 0.45203 0.67421 0.54671 0.06118  -0.13213 -0.00627 282 LYS C CB  
3570 C  CG  . LYS C 282 ? 0.62246 0.85812 0.72311 0.06248  -0.14295 -0.00979 282 LYS C CG  
3571 C  CD  . LYS C 282 ? 0.72381 0.95938 0.84527 0.06428  -0.14445 -0.00536 282 LYS C CD  
3572 C  CE  . LYS C 282 ? 0.72659 0.97419 0.85708 0.06352  -0.15413 -0.01254 282 LYS C CE  
3573 N  NZ  . LYS C 282 ? 0.75825 1.00635 0.90940 0.06529  -0.15580 -0.00862 282 LYS C NZ  
3574 N  N   . ALA C 283 ? 0.30613 0.50330 0.39511 0.04962  -0.11231 -0.02029 283 ALA C N   
3575 C  CA  . ALA C 283 ? 0.29808 0.48170 0.38767 0.04778  -0.10166 -0.01735 283 ALA C CA  
3576 C  C   . ALA C 283 ? 0.29568 0.47183 0.40503 0.04350  -0.09779 -0.02236 283 ALA C C   
3577 O  O   . ALA C 283 ? 0.28777 0.45416 0.39855 0.03910  -0.09034 -0.02713 283 ALA C O   
3578 C  CB  . ALA C 283 ? 0.34392 0.52397 0.41717 0.04478  -0.09725 -0.02329 283 ALA C CB  
3579 N  N   . ILE C 284 ? 0.30405 0.49754 0.37785 0.08932  -0.05420 -0.00720 284 ILE C N   
3580 C  CA  . ILE C 284 ? 0.26992 0.47946 0.35490 0.08733  -0.05110 -0.00943 284 ILE C CA  
3581 C  C   . ILE C 284 ? 0.31910 0.52439 0.40451 0.08964  -0.04825 -0.00651 284 ILE C C   
3582 O  O   . ILE C 284 ? 0.24018 0.45303 0.33162 0.08603  -0.04327 -0.00565 284 ILE C O   
3583 C  CB  . ILE C 284 ? 0.35016 0.57730 0.44457 0.09062  -0.05670 -0.01698 284 ILE C CB  
3584 C  CG1 . ILE C 284 ? 0.39919 0.63074 0.49331 0.08770  -0.05907 -0.01971 284 ILE C CG1 
3585 C  CG2 . ILE C 284 ? 0.40884 0.65374 0.51447 0.08796  -0.05328 -0.01971 284 ILE C CG2 
3586 C  CD1 . ILE C 284 ? 0.50095 0.74969 0.60420 0.09126  -0.06523 -0.02794 284 ILE C CD1 
3587 N  N   . GLY C 285 ? 0.30650 0.49939 0.38516 0.09534  -0.05159 -0.00482 285 GLY C N   
3588 C  CA  . GLY C 285 ? 0.31410 0.50191 0.39254 0.09782  -0.04925 -0.00189 285 GLY C CA  
3589 C  C   . GLY C 285 ? 0.42020 0.59854 0.49453 0.09272  -0.04159 0.00405  285 GLY C C   
3590 O  O   . GLY C 285 ? 0.33028 0.50603 0.40569 0.09398  -0.03880 0.00643  285 GLY C O   
3591 N  N   . PHE C 286 ? 0.27311 0.44608 0.34295 0.08735  -0.03858 0.00614  286 PHE C N   
3592 C  CA  . PHE C 286 ? 0.25637 0.42081 0.32302 0.08238  -0.03194 0.01081  286 PHE C CA  
3593 C  C   . PHE C 286 ? 0.28457 0.45913 0.35832 0.07586  -0.02801 0.01039  286 PHE C C   
3594 O  O   . PHE C 286 ? 0.24775 0.41592 0.31995 0.07157  -0.02312 0.01380  286 PHE C O   
3595 C  CB  . PHE C 286 ? 0.27278 0.42283 0.32872 0.08093  -0.03179 0.01316  286 PHE C CB  
3596 C  CG  . PHE C 286 ? 0.28354 0.42098 0.33028 0.08557  -0.03467 0.01486  286 PHE C CG  
3597 C  CD1 . PHE C 286 ? 0.30414 0.44122 0.34772 0.09007  -0.04182 0.01229  286 PHE C CD1 
3598 C  CD2 . PHE C 286 ? 0.30269 0.42836 0.34359 0.08517  -0.03069 0.01891  286 PHE C CD2 
3599 C  CE1 . PHE C 286 ? 0.49685 0.62109 0.53072 0.09362  -0.04516 0.01428  286 PHE C CE1 
3600 C  CE2 . PHE C 286 ? 0.31598 0.43001 0.34754 0.08851  -0.03341 0.02070  286 PHE C CE2 
3601 C  CZ  . PHE C 286 ? 0.32588 0.43876 0.35347 0.09252  -0.04082 0.01862  286 PHE C CZ  
3602 N  N   . MET C 287 ? 0.25129 0.44151 0.33266 0.07475  -0.03037 0.00605  287 MET C N   
3603 C  CA  . MET C 287 ? 0.25200 0.45129 0.33874 0.06748  -0.02714 0.00589  287 MET C CA  
3604 C  C   . MET C 287 ? 0.19567 0.40251 0.28912 0.06570  -0.02356 0.00669  287 MET C C   
3605 O  O   . MET C 287 ? 0.25328 0.46531 0.35047 0.07066  -0.02487 0.00498  287 MET C O   
3606 C  CB  . MET C 287 ? 0.23139 0.44513 0.32325 0.06602  -0.03078 0.00083  287 MET C CB  
3607 C  CG  . MET C 287 ? 0.18367 0.39049 0.26915 0.06672  -0.03421 0.00010  287 MET C CG  
3608 S  SD  . MET C 287 ? 0.28256 0.47681 0.36148 0.05994  -0.03023 0.00459  287 MET C SD  
3609 C  CE  . MET C 287 ? 0.25112 0.42465 0.31873 0.06437  -0.02975 0.00830  287 MET C CE  
3610 N  N   . PRO C 288 ? 0.21433 0.42159 0.30919 0.05858  -0.01952 0.00916  288 PRO C N   
3611 C  CA  . PRO C 288 ? 0.16812 0.38312 0.26905 0.05590  -0.01633 0.00990  288 PRO C CA  
3612 C  C   . PRO C 288 ? 0.22151 0.45701 0.33115 0.05527  -0.01823 0.00463  288 PRO C C   
3613 O  O   . PRO C 288 ? 0.19797 0.44338 0.31000 0.05155  -0.02004 0.00154  288 PRO C O   
3614 C  CB  . PRO C 288 ? 0.20102 0.41102 0.30040 0.04758  -0.01302 0.01341  288 PRO C CB  
3615 C  CG  . PRO C 288 ? 0.30034 0.49674 0.39227 0.04758  -0.01385 0.01500  288 PRO C CG  
3616 C  CD  . PRO C 288 ? 0.22411 0.42386 0.31470 0.05264  -0.01817 0.01140  288 PRO C CD  
3617 N  N   . ASN C 289 ? 0.20536 0.44770 0.32000 0.05871  -0.01768 0.00334  289 ASN C N   
3618 C  CA  . ASN C 289 ? 0.23706 0.49999 0.36075 0.05935  -0.01963 -0.00276 289 ASN C CA  
3619 C  C   . ASN C 289 ? 0.23269 0.50960 0.36091 0.04961  -0.01741 -0.00401 289 ASN C C   
3620 O  O   . ASN C 289 ? 0.23096 0.50411 0.35786 0.04302  -0.01350 0.00018  289 ASN C O   
3621 C  CB  . ASN C 289 ? 0.21021 0.47050 0.33523 0.06298  -0.01835 -0.00301 289 ASN C CB  
3622 C  CG  . ASN C 289 ? 0.22688 0.49665 0.35586 0.06226  -0.01976 -0.00970 289 ASN C CG  
3623 O  OD1 . ASN C 289 ? 0.28374 0.56489 0.41660 0.05554  -0.01732 -0.01155 289 ASN C OD1 
3624 N  ND2 . ASN C 289 ? 0.26925 0.53349 0.39674 0.06900  -0.02367 -0.01306 289 ASN C ND2 
3625 N  N   . LEU C 290 ? 0.22277 0.51575 0.35612 0.04841  -0.02029 -0.00992 290 LEU C N   
3626 C  CA  . LEU C 290 ? 0.20769 0.51388 0.34423 0.03838  -0.01866 -0.01122 290 LEU C CA  
3627 C  C   . LEU C 290 ? 0.23470 0.54858 0.37397 0.03323  -0.01551 -0.01319 290 LEU C C   
3628 O  O   . LEU C 290 ? 0.23763 0.56048 0.37817 0.02360  -0.01341 -0.01267 290 LEU C O   
3629 C  CB  . LEU C 290 ? 0.19904 0.51597 0.33798 0.03820  -0.02253 -0.01701 290 LEU C CB  
3630 C  CG  . LEU C 290 ? 0.24618 0.54874 0.37772 0.03805  -0.02422 -0.01381 290 LEU C CG  
3631 C  CD1 . LEU C 290 ? 0.30588 0.61855 0.44027 0.04057  -0.02896 -0.01995 290 LEU C CD1 
3632 C  CD2 . LEU C 290 ? 0.24779 0.54431 0.37504 0.02790  -0.02127 -0.00885 290 LEU C CD2 
3633 N  N   . VAL C 291 ? 0.18063 0.49004 0.31977 0.03889  -0.01550 -0.01550 291 VAL C N   
3634 C  CA  . VAL C 291 ? 0.19766 0.51198 0.33823 0.03433  -0.01230 -0.01678 291 VAL C CA  
3635 C  C   . VAL C 291 ? 0.25726 0.56322 0.39581 0.03134  -0.00849 -0.00981 291 VAL C C   
3636 O  O   . VAL C 291 ? 0.29492 0.60628 0.43389 0.02296  -0.00546 -0.00833 291 VAL C O   
3637 C  CB  . VAL C 291 ? 0.26144 0.57401 0.40284 0.04137  -0.01414 -0.02192 291 VAL C CB  
3638 C  CG1 . VAL C 291 ? 0.22622 0.54229 0.36854 0.03742  -0.01077 -0.02271 291 VAL C CG1 
3639 C  CG2 . VAL C 291 ? 0.28506 0.60741 0.42907 0.04333  -0.01794 -0.02934 291 VAL C CG2 
3640 N  N   . ALA C 292 ? 0.21248 0.50466 0.34827 0.03796  -0.00876 -0.00548 292 ALA C N   
3641 C  CA  . ALA C 292 ? 0.17700 0.45986 0.31089 0.03620  -0.00526 0.00112  292 ALA C CA  
3642 C  C   . ALA C 292 ? 0.29804 0.58244 0.43152 0.02801  -0.00381 0.00589  292 ALA C C   
3643 O  O   . ALA C 292 ? 0.25491 0.53662 0.38736 0.02136  -0.00093 0.00964  292 ALA C O   
3644 C  CB  . ALA C 292 ? 0.22830 0.49532 0.35847 0.04534  -0.00598 0.00414  292 ALA C CB  
3645 N  N   . TYR C 293 ? 0.24250 0.52306 0.37260 0.02698  -0.00613 0.00545  293 TYR C N   
3646 C  CA  . TYR C 293 ? 0.21451 0.48437 0.33883 0.01934  -0.00562 0.00973  293 TYR C CA  
3647 C  C   . TYR C 293 ? 0.19766 0.48026 0.32369 0.01369  -0.00790 0.00603  293 TYR C C   
3648 O  O   . TYR C 293 ? 0.22942 0.50775 0.35289 0.01659  -0.01053 0.00480  293 TYR C O   
3649 C  CB  . TYR C 293 ? 0.18680 0.43557 0.30405 0.02455  -0.00615 0.01338  293 TYR C CB  
3650 C  CG  . TYR C 293 ? 0.18709 0.42510 0.30297 0.03244  -0.00463 0.01555  293 TYR C CG  
3651 C  CD1 . TYR C 293 ? 0.17932 0.41279 0.29565 0.03046  -0.00146 0.01902  293 TYR C CD1 
3652 C  CD2 . TYR C 293 ? 0.24238 0.47438 0.35604 0.04145  -0.00663 0.01425  293 TYR C CD2 
3653 C  CE1 . TYR C 293 ? 0.21362 0.43707 0.32861 0.03749  -0.00001 0.02108  293 TYR C CE1 
3654 C  CE2 . TYR C 293 ? 0.22628 0.44821 0.33803 0.04806  -0.00542 0.01644  293 TYR C CE2 
3655 C  CZ  . TYR C 293 ? 0.22406 0.44183 0.33664 0.04610  -0.00194 0.01983  293 TYR C CZ  
3656 O  OH  . TYR C 293 ? 0.22268 0.43084 0.33343 0.05250  -0.00078 0.02189  293 TYR C OH  
3657 N  N   . PRO C 294 ? 0.19922 0.49791 0.32931 0.00520  -0.00694 0.00412  294 PRO C N   
3658 C  CA  . PRO C 294 ? 0.23196 0.54554 0.36450 -0.00039 -0.00898 -0.00018 294 PRO C CA  
3659 C  C   . PRO C 294 ? 0.26657 0.56900 0.39266 -0.00712 -0.01028 0.00354  294 PRO C C   
3660 O  O   . PRO C 294 ? 0.31485 0.60165 0.43544 -0.01107 -0.00928 0.00936  294 PRO C O   
3661 C  CB  . PRO C 294 ? 0.28674 0.61932 0.42436 -0.00887 -0.00689 -0.00244 294 PRO C CB  
3662 C  CG  . PRO C 294 ? 0.28855 0.61538 0.42637 -0.00442 -0.00430 -0.00113 294 PRO C CG  
3663 C  CD  . PRO C 294 ? 0.30938 0.61534 0.44256 0.00102  -0.00396 0.00499  294 PRO C CD  
3664 N  N   . LYS C 295 ? 0.25397 0.56505 0.38122 -0.00839 -0.01291 -0.00029 295 LYS C N   
3665 C  CA  . LYS C 295 ? 0.24355 0.54663 0.36542 -0.01500 -0.01469 0.00233  295 LYS C CA  
3666 C  C   . LYS C 295 ? 0.51147 0.81816 0.63164 -0.02818 -0.01372 0.00528  295 LYS C C   
3667 O  O   . LYS C 295 ? 0.34260 0.66307 0.46670 -0.03288 -0.01168 0.00384  295 LYS C O   
3668 C  CB  . LYS C 295 ? 0.34648 0.66058 0.47086 -0.01350 -0.01773 -0.00307 295 LYS C CB  
3669 C  CG  . LYS C 295 ? 0.63778 0.94581 0.76220 -0.00127 -0.01974 -0.00547 295 LYS C CG  
3670 C  CD  . LYS C 295 ? 0.79342 1.08841 0.91186 -0.00040 -0.02230 -0.00382 295 LYS C CD  
3671 C  CE  . LYS C 295 ? 0.67637 0.94878 0.78737 -0.00033 -0.02109 0.00268  295 LYS C CE  
3672 N  NZ  . LYS C 295 ? 0.65874 0.91981 0.76428 0.00052  -0.02365 0.00350  295 LYS C NZ  
3673 N  N   . PRO C 296 ? 0.42083 0.71472 0.53475 -0.03452 -0.01550 0.00945  296 PRO C N   
3674 C  CA  . PRO C 296 ? 0.59394 0.88881 0.70492 -0.04764 -0.01563 0.01284  296 PRO C CA  
3675 C  C   . PRO C 296 ? 0.40374 0.72212 0.51886 -0.05605 -0.01575 0.00832  296 PRO C C   
3676 O  O   . PRO C 296 ? 0.34567 0.67550 0.46422 -0.05354 -0.01713 0.00326  296 PRO C O   
3677 C  CB  . PRO C 296 ? 0.60263 0.87973 0.70674 -0.05084 -0.01882 0.01677  296 PRO C CB  
3678 C  CG  . PRO C 296 ? 0.55325 0.81656 0.65614 -0.03884 -0.01901 0.01668  296 PRO C CG  
3679 C  CD  . PRO C 296 ? 0.54333 0.82087 0.65227 -0.03019 -0.01789 0.01113  296 PRO C CD  
3680 N  N   . SER C 297 ? 0.37610 0.70162 0.49061 -0.06659 -0.01443 0.01004  297 SER C N   
3681 C  CA  . SER C 297 ? 0.46778 0.81600 0.58534 -0.07665 -0.01427 0.00596  297 SER C CA  
3682 C  C   . SER C 297 ? 0.63083 0.97586 0.74241 -0.09124 -0.01459 0.01115  297 SER C C   
3683 O  O   . SER C 297 ? 0.67302 0.99678 0.77791 -0.09326 -0.01618 0.01765  297 SER C O   
3684 C  CB  . SER C 297 ? 0.53980 0.90278 0.66278 -0.07035 -0.01103 -0.00082 297 SER C CB  
3685 O  OG  . SER C 297 ? 0.56289 0.92078 0.68446 -0.07060 -0.00819 0.00185  297 SER C OG  
3686 N  N   . ASN C 298 ? 0.97629 1.33102 1.08443 -0.09834 -0.01278 0.00783  298 ASN C N   
3687 C  CA  . ASN C 298 ? 1.13460 1.48369 1.23415 -0.11097 -0.01268 0.01208  298 ASN C CA  
3688 C  C   . ASN C 298 ? 1.18441 1.53395 1.28330 -0.10940 -0.00895 0.01183  298 ASN C C   
3689 O  O   . ASN C 298 ? 1.20763 1.55159 1.29890 -0.11914 -0.00889 0.01550  298 ASN C O   
3690 C  CB  . ASN C 298 ? 1.15275 1.51123 1.24698 -0.12049 -0.01309 0.00896  298 ASN C CB  
3691 C  CG  . ASN C 298 ? 1.28194 1.65836 1.38103 -0.11455 -0.00999 0.00001  298 ASN C CG  
3692 O  OD1 . ASN C 298 ? 1.31970 1.70044 1.42617 -0.10267 -0.00834 -0.00400 298 ASN C OD1 
3693 N  ND2 . ASN C 298 ? 1.37162 1.75791 1.46624 -0.12272 -0.00953 -0.00327 298 ASN C ND2 
3694 N  N   . SER C 299 ? 1.04051 1.39556 1.14650 -0.09734 -0.00630 0.00761  299 SER C N   
3695 C  CA  . SER C 299 ? 1.04830 1.40316 1.15410 -0.09485 -0.00305 0.00715  299 SER C CA  
3696 C  C   . SER C 299 ? 0.97666 1.31602 1.08237 -0.09297 -0.00337 0.01426  299 SER C C   
3697 O  O   . SER C 299 ? 0.82671 1.15573 0.93216 -0.09450 -0.00625 0.01948  299 SER C O   
3698 C  CB  . SER C 299 ? 1.02134 1.38680 1.13417 -0.08269 -0.00085 -0.00042 299 SER C CB  
3699 O  OG  . SER C 299 ? 1.11331 1.47190 1.23197 -0.07097 -0.00133 0.00079  299 SER C OG  
3700 N  N   . LYS C 300 ? 0.77723 1.11485 0.88332 -0.08951 -0.00057 0.01428  300 LYS C N   
3701 C  CA  . LYS C 300 ? 0.84124 1.16433 0.94706 -0.08802 -0.00057 0.02087  300 LYS C CA  
3702 C  C   . LYS C 300 ? 0.67963 0.99872 0.79263 -0.07610 -0.00101 0.02150  300 LYS C C   
3703 O  O   . LYS C 300 ? 0.63710 0.96352 0.75547 -0.06535 0.00025  0.01610  300 LYS C O   
3704 C  CB  . LYS C 300 ? 0.73948 1.06215 0.84423 -0.08639 0.00256  0.02026  300 LYS C CB  
3705 C  CG  . LYS C 300 ? 0.78069 1.08822 0.88539 -0.08442 0.00276  0.02687  300 LYS C CG  
3706 C  CD  . LYS C 300 ? 0.87917 1.18687 0.98422 -0.08022 0.00596  0.02546  300 LYS C CD  
3707 C  CE  . LYS C 300 ? 0.89070 1.19461 0.98753 -0.09170 0.00586  0.02824  300 LYS C CE  
3708 N  NZ  . LYS C 300 ? 0.75354 1.05719 0.85100 -0.08737 0.00874  0.02702  300 LYS C NZ  
3709 N  N   . LYS C 301 ? 0.52579 0.82661 0.63534 -0.07659 -0.00328 0.02763  301 LYS C N   
3710 C  CA  . LYS C 301 ? 0.44559 0.73059 0.55540 -0.06356 -0.00361 0.02825  301 LYS C CA  
3711 C  C   . LYS C 301 ? 0.41632 0.69036 0.52659 -0.05715 -0.00122 0.03110  301 LYS C C   
3712 O  O   . LYS C 301 ? 0.49904 0.76355 0.60532 -0.06375 -0.00146 0.03577  301 LYS C O   
3713 C  CB  . LYS C 301 ? 0.43289 0.69944 0.53620 -0.06611 -0.00746 0.03195  301 LYS C CB  
3714 C  CG  . LYS C 301 ? 0.63483 0.88900 0.73827 -0.05398 -0.00803 0.03119  301 LYS C CG  
3715 C  CD  . LYS C 301 ? 0.55284 0.78787 0.65423 -0.04784 -0.00705 0.03507  301 LYS C CD  
3716 C  CE  . LYS C 301 ? 0.58540 0.80747 0.68583 -0.03722 -0.00752 0.03455  301 LYS C CE  
3717 N  NZ  . LYS C 301 ? 0.47352 0.67899 0.57253 -0.03182 -0.00603 0.03784  301 LYS C NZ  
3718 N  N   . TYR C 302 ? 0.39811 0.67348 0.51302 -0.04463 0.00072  0.02828  302 TYR C N   
3719 C  CA  . TYR C 302 ? 0.53790 0.80442 0.65378 -0.03790 0.00314  0.03048  302 TYR C CA  
3720 C  C   . TYR C 302 ? 0.25678 0.50174 0.36943 -0.02905 0.00251  0.03330  302 TYR C C   
3721 O  O   . TYR C 302 ? 0.43262 0.67360 0.54447 -0.02372 0.00101  0.03168  302 TYR C O   
3722 C  CB  . TYR C 302 ? 0.38279 0.66579 0.50600 -0.03048 0.00566  0.02551  302 TYR C CB  
3723 C  CG  . TYR C 302 ? 0.51631 0.81486 0.64114 -0.03799 0.00739  0.02298  302 TYR C CG  
3724 C  CD1 . TYR C 302 ? 0.47650 0.76836 0.59815 -0.04347 0.00891  0.02689  302 TYR C CD1 
3725 C  CD2 . TYR C 302 ? 0.59013 0.90159 0.71542 -0.03835 0.00715  0.01594  302 TYR C CD2 
3726 C  CE1 . TYR C 302 ? 0.57233 0.87055 0.69084 -0.04922 0.01018  0.02389  302 TYR C CE1 
3727 C  CE2 . TYR C 302 ? 0.44284 0.76123 0.56554 -0.04400 0.00859  0.01281  302 TYR C CE2 
3728 C  CZ  . TYR C 302 ? 0.68343 0.99532 0.80254 -0.04941 0.01014  0.01683  302 TYR C CZ  
3729 O  OH  . TYR C 302 ? 0.53866 0.85778 0.65467 -0.05506 0.01146  0.01366  302 TYR C OH  
3730 N  N   . ALA C 303 ? 0.22894 0.46064 0.33983 -0.02773 0.00378  0.03727  303 ALA C N   
3731 C  CA  . ALA C 303 ? 0.21667 0.42774 0.32438 -0.02097 0.00351  0.04008  303 ALA C CA  
3732 C  C   . ALA C 303 ? 0.19093 0.40086 0.30111 -0.00834 0.00524  0.03779  303 ALA C C   
3733 O  O   . ALA C 303 ? 0.18651 0.38074 0.29380 -0.00284 0.00517  0.03947  303 ALA C O   
3734 C  CB  . ALA C 303 ? 0.24609 0.44494 0.35174 -0.02408 0.00421  0.04457  303 ALA C CB  
3735 N  N   . ARG C 304 ? 0.19944 0.42526 0.31473 -0.00381 0.00647  0.03384  304 ARG C N   
3736 C  CA  . ARG C 304 ? 0.21209 0.43412 0.32861 0.00783  0.00726  0.03234  304 ARG C CA  
3737 C  C   . ARG C 304 ? 0.21527 0.43143 0.32892 0.01245  0.00512  0.03085  304 ARG C C   
3738 O  O   . ARG C 304 ? 0.22283 0.43088 0.33518 0.02114  0.00544  0.03079  304 ARG C O   
3739 C  CB  . ARG C 304 ? 0.34739 0.58711 0.47025 0.01211  0.00807  0.02801  304 ARG C CB  
3740 C  CG  . ARG C 304 ? 0.45261 0.71081 0.57907 0.00901  0.00630  0.02296  304 ARG C CG  
3741 C  CD  . ARG C 304 ? 0.51775 0.79051 0.64989 0.01396  0.00664  0.01768  304 ARG C CD  
3742 N  NE  . ARG C 304 ? 0.43196 0.71803 0.56565 0.01142  0.00461  0.01172  304 ARG C NE  
3743 C  CZ  . ARG C 304 ? 0.66203 0.95363 0.79675 0.01507  0.00374  0.00545  304 ARG C CZ  
3744 N  NH1 . ARG C 304 ? 0.65167 0.93617 0.78582 0.02106  0.00448  0.00461  304 ARG C NH1 
3745 N  NH2 . ARG C 304 ? 0.53595 0.83978 0.67233 0.01258  0.00192  0.00004  304 ARG C NH2 
3746 N  N   . ASP C 305 ? 0.17324 0.39236 0.28523 0.00648  0.00287  0.02995  305 ASP C N   
3747 C  CA  . ASP C 305 ? 0.18564 0.39710 0.29417 0.01060  0.00086  0.02898  305 ASP C CA  
3748 C  C   . ASP C 305 ? 0.23719 0.42833 0.34015 0.01067  0.00080  0.03268  305 ASP C C   
3749 O  O   . ASP C 305 ? 0.20009 0.38500 0.29978 0.01245  -0.00091 0.03188  305 ASP C O   
3750 C  CB  . ASP C 305 ? 0.21335 0.43582 0.32246 0.00505  -0.00172 0.02616  305 ASP C CB  
3751 C  CG  . ASP C 305 ? 0.32406 0.54608 0.43127 -0.00651 -0.00264 0.02861  305 ASP C CG  
3752 O  OD1 . ASP C 305 ? 0.36512 0.57571 0.46982 -0.01014 -0.00198 0.03265  305 ASP C OD1 
3753 O  OD2 . ASP C 305 ? 0.33142 0.56457 0.43947 -0.01222 -0.00449 0.02633  305 ASP C OD2 
3754 N  N   . ILE C 306 ? 0.15845 0.33961 0.26054 0.00912  0.00246  0.03615  306 ILE C N   
3755 C  CA  . ILE C 306 ? 0.16561 0.32815 0.26344 0.00957  0.00224  0.03877  306 ILE C CA  
3756 C  C   . ILE C 306 ? 0.26768 0.42154 0.36546 0.01712  0.00507  0.03997  306 ILE C C   
3757 O  O   . ILE C 306 ? 0.19863 0.35798 0.29951 0.01862  0.00706  0.04057  306 ILE C O   
3758 C  CB  . ILE C 306 ? 0.18222 0.33884 0.27880 0.00024  0.00071  0.04168  306 ILE C CB  
3759 C  CG1 . ILE C 306 ? 0.22371 0.38669 0.31910 -0.00773 -0.00258 0.04082  306 ILE C CG1 
3760 C  CG2 . ILE C 306 ? 0.18614 0.32361 0.27965 0.00174  0.00029  0.04368  306 ILE C CG2 
3761 C  CD1 . ILE C 306 ? 0.29957 0.46036 0.39370 -0.01835 -0.00453 0.04382  306 ILE C CD1 
3762 N  N   . VAL C 307 ? 0.17780 0.31867 0.27201 0.02169  0.00530  0.04008  307 VAL C N   
3763 C  CA  . VAL C 307 ? 0.18130 0.31147 0.27468 0.02712  0.00790  0.04153  307 VAL C CA  
3764 C  C   . VAL C 307 ? 0.22492 0.34051 0.31576 0.02456  0.00711  0.04253  307 VAL C C   
3765 O  O   . VAL C 307 ? 0.25674 0.36820 0.34488 0.02365  0.00517  0.04105  307 VAL C O   
3766 C  CB  . VAL C 307 ? 0.26457 0.39352 0.35576 0.03551  0.00900  0.04000  307 VAL C CB  
3767 C  CG1 . VAL C 307 ? 0.25449 0.37205 0.34434 0.04023  0.01187  0.04162  307 VAL C CG1 
3768 C  CG2 . VAL C 307 ? 0.34321 0.48599 0.43706 0.03864  0.00851  0.03823  307 VAL C CG2 
3769 N  N   . TYR C 308 ? 0.15938 0.26713 0.25133 0.02380  0.00834  0.04462  308 TYR C N   
3770 C  CA  . TYR C 308 ? 0.16706 0.26045 0.25746 0.02265  0.00738  0.04481  308 TYR C CA  
3771 C  C   . TYR C 308 ? 0.28778 0.37261 0.37729 0.02963  0.01048  0.04426  308 TYR C C   
3772 O  O   . TYR C 308 ? 0.23569 0.32262 0.32659 0.03350  0.01330  0.04545  308 TYR C O   
3773 C  CB  . TYR C 308 ? 0.22268 0.31151 0.31482 0.01664  0.00591  0.04728  308 TYR C CB  
3774 C  CG  . TYR C 308 ? 0.20331 0.29484 0.29476 0.00798  0.00182  0.04798  308 TYR C CG  
3775 C  CD1 . TYR C 308 ? 0.26474 0.34701 0.35401 0.00481  -0.00203 0.04695  308 TYR C CD1 
3776 C  CD2 . TYR C 308 ? 0.16618 0.26942 0.25907 0.00258  0.00159  0.04948  308 TYR C CD2 
3777 C  CE1 . TYR C 308 ? 0.26016 0.34421 0.34816 -0.00382 -0.00637 0.04796  308 TYR C CE1 
3778 C  CE2 . TYR C 308 ? 0.21555 0.32161 0.30707 -0.00637 -0.00218 0.05029  308 TYR C CE2 
3779 C  CZ  . TYR C 308 ? 0.21461 0.31046 0.30344 -0.00961 -0.00629 0.04983  308 TYR C CZ  
3780 O  OH  . TYR C 308 ? 0.31112 0.40933 0.39803 -0.01911 -0.01048 0.05102  308 TYR C OH  
3781 N  N   . GLY C 309 ? 0.19610 0.27120 0.28342 0.03078  0.00985  0.04228  309 GLY C N   
3782 C  CA  . GLY C 309 ? 0.19428 0.26069 0.28090 0.03592  0.01270  0.04138  309 GLY C CA  
3783 C  C   . GLY C 309 ? 0.26398 0.31911 0.35075 0.03403  0.01072  0.03928  309 GLY C C   
3784 O  O   . GLY C 309 ? 0.28567 0.33927 0.37243 0.02920  0.00679  0.03863  309 GLY C O   
3785 N  N   . THR C 310 ? 0.21334 0.26071 0.30056 0.03776  0.01313  0.03799  310 THR C N   
3786 C  CA  . THR C 310 ? 0.20317 0.24031 0.29127 0.03711  0.01132  0.03473  310 THR C CA  
3787 C  C   . THR C 310 ? 0.29494 0.33034 0.38009 0.04177  0.01428  0.03118  310 THR C C   
3788 O  O   . THR C 310 ? 0.27299 0.30961 0.35681 0.04590  0.01837  0.03180  310 THR C O   
3789 C  CB  . THR C 310 ? 0.30412 0.33340 0.39606 0.03688  0.01122  0.03543  310 THR C CB  
3790 O  OG1 . THR C 310 ? 0.28587 0.31708 0.37954 0.03187  0.00856  0.03917  310 THR C OG1 
3791 C  CG2 . THR C 310 ? 0.29018 0.30875 0.38400 0.03644  0.00831  0.03109  310 THR C CG2 
3792 N  N   . ILE C 311 ? 0.22006 0.25257 0.30384 0.04080  0.01213  0.02741  311 ILE C N   
3793 C  CA  . ILE C 311 ? 0.20205 0.23233 0.28307 0.04437  0.01492  0.02333  311 ILE C CA  
3794 C  C   . ILE C 311 ? 0.19936 0.22104 0.28382 0.04392  0.01299  0.01858  311 ILE C C   
3795 O  O   . ILE C 311 ? 0.27590 0.29265 0.36427 0.04096  0.00885  0.01887  311 ILE C O   
3796 C  CB  . ILE C 311 ? 0.19298 0.22839 0.26888 0.04447  0.01463  0.02211  311 ILE C CB  
3797 C  CG1 . ILE C 311 ? 0.23916 0.27580 0.31560 0.04018  0.00963  0.02177  311 ILE C CG1 
3798 C  CG2 . ILE C 311 ? 0.25251 0.29556 0.32500 0.04659  0.01695  0.02584  311 ILE C CG2 
3799 C  CD1 . ILE C 311 ? 0.34745 0.37649 0.42613 0.03855  0.00632  0.01718  311 ILE C CD1 
3800 N  N   . TYR C 312 ? 0.22195 0.24182 0.30484 0.04677  0.01577  0.01389  312 TYR C N   
3801 C  CA  . TYR C 312 ? 0.16309 0.17585 0.25021 0.04738  0.01457  0.00829  312 TYR C CA  
3802 C  C   . TYR C 312 ? 0.21491 0.22798 0.29991 0.04759  0.01402  0.00234  312 TYR C C   
3803 O  O   . TYR C 312 ? 0.26520 0.28277 0.34486 0.04908  0.01781  0.00141  312 TYR C O   
3804 C  CB  . TYR C 312 ? 0.20357 0.21416 0.29254 0.05067  0.01908  0.00735  312 TYR C CB  
3805 C  CG  . TYR C 312 ? 0.20795 0.21732 0.29978 0.05004  0.01858  0.01294  312 TYR C CG  
3806 C  CD1 . TYR C 312 ? 0.24148 0.25680 0.33022 0.05071  0.02129  0.01857  312 TYR C CD1 
3807 C  CD2 . TYR C 312 ? 0.25573 0.25791 0.35326 0.04869  0.01484  0.01223  312 TYR C CD2 
3808 C  CE1 . TYR C 312 ? 0.25984 0.27500 0.35133 0.04986  0.02078  0.02332  312 TYR C CE1 
3809 C  CE2 . TYR C 312 ? 0.26590 0.26699 0.36544 0.04752  0.01425  0.01735  312 TYR C CE2 
3810 C  CZ  . TYR C 312 ? 0.27543 0.28352 0.37203 0.04807  0.01753  0.02277  312 TYR C CZ  
3811 O  OH  . TYR C 312 ? 0.34000 0.34771 0.43883 0.04673  0.01699  0.02743  312 TYR C OH  
3812 N  N   . LEU C 313 ? 0.20815 0.21620 0.29691 0.04585  0.00883  -0.00159 313 LEU C N   
3813 C  CA  . LEU C 313 ? 0.19960 0.20821 0.28687 0.04587  0.00759  -0.00758 313 LEU C CA  
3814 C  C   . LEU C 313 ? 0.23793 0.24611 0.32632 0.04893  0.01152  -0.01436 313 LEU C C   
3815 O  O   . LEU C 313 ? 0.23947 0.24323 0.33328 0.05046  0.01156  -0.01712 313 LEU C O   
3816 C  CB  . LEU C 313 ? 0.23207 0.23497 0.32324 0.04312  0.00007  -0.00983 313 LEU C CB  
3817 C  CG  . LEU C 313 ? 0.30281 0.30638 0.39275 0.03898  -0.00402 -0.00327 313 LEU C CG  
3818 C  CD1 . LEU C 313 ? 0.33155 0.32828 0.42447 0.03571  -0.01212 -0.00573 313 LEU C CD1 
3819 C  CD2 . LEU C 313 ? 0.30507 0.31732 0.38877 0.03833  -0.00148 0.00030  313 LEU C CD2 
3820 N  N   . GLY C 314 ? 0.25507 0.26827 0.33806 0.04956  0.01492  -0.01723 314 GLY C N   
3821 C  CA  . GLY C 314 ? 0.26388 0.27833 0.34694 0.05156  0.01920  -0.02394 314 GLY C CA  
3822 C  C   . GLY C 314 ? 0.27954 0.29476 0.36192 0.05337  0.02460  -0.02137 314 GLY C C   
3823 O  O   . GLY C 314 ? 0.31222 0.32814 0.39587 0.05479  0.02821  -0.02684 314 GLY C O   
3824 N  N   . GLY C 315 ? 0.28144 0.29690 0.36220 0.05325  0.02506  -0.01342 315 GLY C N   
3825 C  CA  . GLY C 315 ? 0.29048 0.30612 0.37083 0.05508  0.02962  -0.01053 315 GLY C CA  
3826 C  C   . GLY C 315 ? 0.26785 0.27824 0.35616 0.05644  0.02891  -0.01295 315 GLY C C   
3827 O  O   . GLY C 315 ? 0.27541 0.28584 0.36385 0.05815  0.03302  -0.01176 315 GLY C O   
3828 N  N   . LYS C 316 ? 0.31408 0.26462 0.35356 0.06027  0.02986  0.01495  316 LYS C N   
3829 C  CA  . LYS C 316 ? 0.25326 0.21108 0.29675 0.06557  0.03161  0.01696  316 LYS C CA  
3830 C  C   . LYS C 316 ? 0.22619 0.19800 0.27527 0.06539  0.02852  0.01705  316 LYS C C   
3831 O  O   . LYS C 316 ? 0.27212 0.24207 0.31692 0.06183  0.02678  0.01809  316 LYS C O   
3832 C  CB  . LYS C 316 ? 0.33435 0.27856 0.36717 0.06813  0.03495  0.02094  316 LYS C CB  
3833 C  CG  . LYS C 316 ? 0.36393 0.29367 0.39035 0.06944  0.03855  0.02130  316 LYS C CG  
3834 C  CD  . LYS C 316 ? 0.41347 0.33064 0.42930 0.07334  0.04229  0.02552  316 LYS C CD  
3835 C  CE  . LYS C 316 ? 0.88331 0.78436 0.89125 0.07521  0.04637  0.02627  316 LYS C CE  
3836 N  NZ  . LYS C 316 ? 1.08419 0.97072 1.07951 0.07915  0.05024  0.03062  316 LYS C NZ  
3837 N  N   . PRO C 317 ? 0.27442 0.26022 0.33297 0.06900  0.02775  0.01591  317 PRO C N   
3838 C  CA  . PRO C 317 ? 0.33122 0.32994 0.39459 0.06883  0.02445  0.01553  317 PRO C CA  
3839 C  C   . PRO C 317 ? 0.38796 0.38422 0.44501 0.07086  0.02502  0.01922  317 PRO C C   
3840 O  O   . PRO C 317 ? 0.31683 0.32047 0.37524 0.07002  0.02277  0.01941  317 PRO C O   
3841 C  CB  . PRO C 317 ? 0.30224 0.31483 0.37644 0.07238  0.02353  0.01312  317 PRO C CB  
3842 C  CG  . PRO C 317 ? 0.35836 0.36567 0.43291 0.07582  0.02720  0.01376  317 PRO C CG  
3843 C  CD  . PRO C 317 ? 0.33991 0.33074 0.40567 0.07284  0.02968  0.01451  317 PRO C CD  
3844 N  N   . ASP C 318 ? 0.30066 0.28571 0.34979 0.07371  0.02834  0.02227  318 ASP C N   
3845 C  CA  . ASP C 318 ? 0.30297 0.28319 0.34400 0.07575  0.02954  0.02591  318 ASP C CA  
3846 C  C   . ASP C 318 ? 0.32731 0.29233 0.35720 0.07049  0.03085  0.02785  318 ASP C C   
3847 O  O   . ASP C 318 ? 0.35654 0.31298 0.37705 0.07179  0.03305  0.03116  318 ASP C O   
3848 C  CB  . ASP C 318 ? 0.31774 0.29617 0.35650 0.08330  0.03236  0.02821  318 ASP C CB  
3849 C  CG  . ASP C 318 ? 0.55041 0.51448 0.58242 0.08414  0.03614  0.02953  318 ASP C CG  
3850 O  OD1 . ASP C 318 ? 0.41613 0.37399 0.44789 0.07962  0.03623  0.02775  318 ASP C OD1 
3851 O  OD2 . ASP C 318 ? 0.55802 0.51734 0.58492 0.09017  0.03909  0.03232  318 ASP C OD2 
3852 N  N   . GLN C 319 ? 0.28155 0.24319 0.31203 0.06445  0.02938  0.02568  319 GLN C N   
3853 C  CA  . GLN C 319 ? 0.28106 0.23006 0.30244 0.05844  0.02963  0.02682  319 GLN C CA  
3854 C  C   . GLN C 319 ? 0.23422 0.19168 0.26110 0.05252  0.02604  0.02469  319 GLN C C   
3855 O  O   . GLN C 319 ? 0.26947 0.22256 0.29552 0.04767  0.02445  0.02283  319 GLN C O   
3856 C  CB  . GLN C 319 ? 0.28954 0.22359 0.30407 0.05731  0.03134  0.02652  319 GLN C CB  
3857 C  CG  . GLN C 319 ? 0.31014 0.23472 0.31795 0.06358  0.03557  0.02928  319 GLN C CG  
3858 C  CD  . GLN C 319 ? 0.35189 0.26000 0.35135 0.06335  0.03797  0.02948  319 GLN C CD  
3859 O  OE1 . GLN C 319 ? 0.35940 0.26427 0.35958 0.05934  0.03628  0.02687  319 GLN C OE1 
3860 N  NE2 . GLN C 319 ? 0.31608 0.21332 0.30692 0.06836  0.04204  0.03261  319 GLN C NE2 
3861 N  N   . PRO C 320 ? 0.24533 0.21452 0.27714 0.05310  0.02475  0.02507  320 PRO C N   
3862 C  CA  . PRO C 320 ? 0.24310 0.22069 0.27997 0.04799  0.02184  0.02350  320 PRO C CA  
3863 C  C   . PRO C 320 ? 0.26970 0.23824 0.29987 0.04150  0.02225  0.02503  320 PRO C C   
3864 O  O   . PRO C 320 ? 0.30283 0.26005 0.32388 0.04114  0.02511  0.02799  320 PRO C O   
3865 C  CB  . PRO C 320 ? 0.25141 0.24148 0.29308 0.05140  0.02133  0.02431  320 PRO C CB  
3866 C  CG  . PRO C 320 ? 0.28154 0.26458 0.31603 0.05641  0.02454  0.02757  320 PRO C CG  
3867 C  CD  . PRO C 320 ? 0.31814 0.29291 0.35025 0.05899  0.02600  0.02712  320 PRO C CD  
3868 N  N   . ALA C 321 ? 0.25929 0.23323 0.29402 0.03638  0.01936  0.02292  321 ALA C N   
3869 C  CA  . ALA C 321 ? 0.27906 0.25038 0.31130 0.02964  0.01894  0.02392  321 ALA C CA  
3870 C  C   . ALA C 321 ? 0.28362 0.27080 0.32563 0.02773  0.01606  0.02220  321 ALA C C   
3871 O  O   . ALA C 321 ? 0.27368 0.26948 0.32210 0.03013  0.01378  0.01949  321 ALA C O   
3872 C  CB  . ALA C 321 ? 0.32285 0.28099 0.34862 0.02447  0.01805  0.02299  321 ALA C CB  
3873 N  N   . VAL C 322 ? 0.23684 0.22715 0.27945 0.02347  0.01656  0.02382  322 VAL C N   
3874 C  CA  . VAL C 322 ? 0.21264 0.21820 0.26420 0.02207  0.01449  0.02281  322 VAL C CA  
3875 C  C   . VAL C 322 ? 0.25425 0.26108 0.30850 0.01613  0.01130  0.02060  322 VAL C C   
3876 O  O   . VAL C 322 ? 0.27902 0.27659 0.32841 0.01046  0.01151  0.02124  322 VAL C O   
3877 C  CB  . VAL C 322 ? 0.26091 0.27011 0.31234 0.02080  0.01724  0.02595  322 VAL C CB  
3878 C  CG1 . VAL C 322 ? 0.31694 0.34132 0.37744 0.01870  0.01547  0.02518  322 VAL C CG1 
3879 C  CG2 . VAL C 322 ? 0.25915 0.26801 0.30762 0.02788  0.01974  0.02784  322 VAL C CG2 
3880 N  N   . ILE C 323 ? 0.24325 0.26112 0.30459 0.01746  0.00820  0.01787  323 ILE C N   
3881 C  CA  . ILE C 323 ? 0.21490 0.23673 0.27961 0.01257  0.00484  0.01585  323 ILE C CA  
3882 C  C   . ILE C 323 ? 0.26184 0.29935 0.33478 0.01168  0.00446  0.01654  323 ILE C C   
3883 O  O   . ILE C 323 ? 0.24669 0.29387 0.32390 0.01660  0.00440  0.01610  323 ILE C O   
3884 C  CB  . ILE C 323 ? 0.31140 0.33192 0.37614 0.01490  0.00179  0.01222  323 ILE C CB  
3885 C  CG1 . ILE C 323 ? 0.25505 0.28114 0.32326 0.01059  -0.00214 0.01013  323 ILE C CG1 
3886 C  CG2 . ILE C 323 ? 0.30684 0.33500 0.37531 0.02148  0.00193  0.01086  323 ILE C CG2 
3887 C  CD1 . ILE C 323 ? 0.34952 0.37129 0.41530 0.01293  -0.00483 0.00671  323 ILE C CD1 
3888 N  N   . LYS C 324 ? 0.22731 0.26682 0.30210 0.00533  0.00453  0.01776  324 LYS C N   
3889 C  CA  . LYS C 324 ? 0.21521 0.26953 0.29817 0.00381  0.00480  0.01883  324 LYS C CA  
3890 C  C   . LYS C 324 ? 0.22022 0.28198 0.30872 -0.00001 0.00052  0.01629  324 LYS C C   
3891 O  O   . LYS C 324 ? 0.27007 0.32584 0.35676 -0.00623 -0.00107 0.01567  324 LYS C O   
3892 C  CB  . LYS C 324 ? 0.21596 0.26764 0.29754 -0.00083 0.00879  0.02233  324 LYS C CB  
3893 C  CG  . LYS C 324 ? 0.22072 0.28743 0.31092 -0.00265 0.01004  0.02388  324 LYS C CG  
3894 C  CD  . LYS C 324 ? 0.31987 0.38144 0.40781 -0.00865 0.01432  0.02705  324 LYS C CD  
3895 C  CE  . LYS C 324 ? 0.46372 0.53945 0.55962 -0.00929 0.01695  0.02920  324 LYS C CE  
3896 N  NZ  . LYS C 324 ? 0.49521 0.56573 0.58936 -0.01646 0.02145  0.03207  324 LYS C NZ  
3897 N  N   . THR C 325 ? 0.19448 0.26892 0.28907 0.00387  -0.00148 0.01476  325 THR C N   
3898 C  CA  . THR C 325 ? 0.21209 0.29484 0.31180 0.00175  -0.00577 0.01226  325 THR C CA  
3899 C  C   . THR C 325 ? 0.24300 0.34197 0.35206 -0.00022 -0.00492 0.01400  325 THR C C   
3900 O  O   . THR C 325 ? 0.20818 0.31477 0.31979 0.00421  -0.00233 0.01569  325 THR C O   
3901 C  CB  . THR C 325 ? 0.19267 0.27684 0.29116 0.00818  -0.00841 0.00916  325 THR C CB  
3902 O  OG1 . THR C 325 ? 0.23416 0.30311 0.32433 0.01007  -0.00828 0.00784  325 THR C OG1 
3903 C  CG2 . THR C 325 ? 0.23638 0.32878 0.33904 0.00691  -0.01302 0.00654  325 THR C CG2 
3904 N  N   . THR C 326 ? 0.18482 0.28900 0.29894 -0.00689 -0.00698 0.01364  326 THR C N   
3905 C  CA  . THR C 326 ? 0.17798 0.29830 0.30215 -0.00951 -0.00570 0.01549  326 THR C CA  
3906 C  C   . THR C 326 ? 0.25637 0.38911 0.38774 -0.01047 -0.01081 0.01282  326 THR C C   
3907 O  O   . THR C 326 ? 0.22687 0.35411 0.35618 -0.01428 -0.01505 0.01023  326 THR C O   
3908 C  CB  . THR C 326 ? 0.28592 0.40274 0.41114 -0.01796 -0.00234 0.01818  326 THR C CB  
3909 O  OG1 . THR C 326 ? 0.27437 0.37766 0.39098 -0.01645 0.00224  0.02056  326 THR C OG1 
3910 C  CG2 . THR C 326 ? 0.23968 0.37362 0.37591 -0.02042 0.00018  0.02051  326 THR C CG2 
3911 N  N   . PHE C 327 ? 0.17526 0.32466 0.31463 -0.00682 -0.01041 0.01354  327 PHE C N   
3912 C  CA  . PHE C 327 ? 0.20797 0.37109 0.35446 -0.00629 -0.01511 0.01123  327 PHE C CA  
3913 C  C   . PHE C 327 ? 0.26067 0.43904 0.41915 -0.01300 -0.01456 0.01288  327 PHE C C   
3914 O  O   . PHE C 327 ? 0.20404 0.38951 0.36749 -0.01368 -0.00946 0.01634  327 PHE C O   
3915 C  CB  . PHE C 327 ? 0.15768 0.32885 0.30413 0.00320  -0.01527 0.01064  327 PHE C CB  
3916 C  CG  . PHE C 327 ? 0.23888 0.39617 0.37465 0.00917  -0.01540 0.00893  327 PHE C CG  
3917 C  CD1 . PHE C 327 ? 0.21140 0.35746 0.34046 0.00921  -0.01937 0.00552  327 PHE C CD1 
3918 C  CD2 . PHE C 327 ? 0.25063 0.40525 0.38279 0.01438  -0.01146 0.01069  327 PHE C CD2 
3919 C  CE1 . PHE C 327 ? 0.21340 0.34666 0.33329 0.01419  -0.01880 0.00405  327 PHE C CE1 
3920 C  CE2 . PHE C 327 ? 0.24412 0.38675 0.36754 0.01916  -0.01152 0.00896  327 PHE C CE2 
3921 C  CZ  . PHE C 327 ? 0.22346 0.35541 0.34107 0.01885  -0.01490 0.00571  327 PHE C CZ  
3922 N  N   . ASN C 328 ? 0.15847 0.34133 0.32135 -0.01817 -0.01974 0.01034  328 ASN C N   
3923 C  CA  . ASN C 328 ? 0.19797 0.39910 0.37432 -0.02391 -0.02072 0.01093  328 ASN C CA  
3924 C  C   . ASN C 328 ? 0.22870 0.42988 0.40966 -0.03244 -0.01547 0.01423  328 ASN C C   
3925 O  O   . ASN C 328 ? 0.28199 0.49982 0.47475 -0.03522 -0.01324 0.01618  328 ASN C O   
3926 C  CB  . ASN C 328 ? 0.22187 0.44236 0.40648 -0.01676 -0.02015 0.01184  328 ASN C CB  
3927 C  CG  . ASN C 328 ? 0.23799 0.46027 0.41886 -0.00911 -0.02571 0.00831  328 ASN C CG  
3928 O  OD1 . ASN C 328 ? 0.21393 0.42719 0.38939 -0.01077 -0.03090 0.00493  328 ASN C OD1 
3929 N  ND2 . ASN C 328 ? 0.20669 0.43906 0.38899 -0.00039 -0.02436 0.00913  328 ASN C ND2 
3930 N  N   . GLN C 329 ? 0.22695 0.40950 0.39860 -0.03684 -0.01325 0.01489  329 GLN C N   
3931 C  CA  . GLN C 329 ? 0.21933 0.39938 0.39322 -0.04479 -0.00769 0.01805  329 GLN C CA  
3932 C  C   . GLN C 329 ? 0.32327 0.49632 0.49696 -0.05594 -0.01039 0.01640  329 GLN C C   
3933 O  O   . GLN C 329 ? 0.40858 0.57641 0.58217 -0.06344 -0.00572 0.01872  329 GLN C O   
3934 C  CB  . GLN C 329 ? 0.30217 0.46629 0.46486 -0.04090 -0.00180 0.02082  329 GLN C CB  
3935 C  CG  . GLN C 329 ? 0.34147 0.51516 0.50703 -0.03300 0.00294  0.02377  329 GLN C CG  
3936 C  CD  . GLN C 329 ? 0.40310 0.59094 0.57973 -0.03782 0.00788  0.02699  329 GLN C CD  
3937 O  OE1 . GLN C 329 ? 0.52200 0.72848 0.70939 -0.03563 0.00717  0.02719  329 GLN C OE1 
3938 N  NE2 . GLN C 329 ? 0.37678 0.55518 0.55022 -0.04415 0.01332  0.02963  329 GLN C NE2 
3939 N  N   . GLU C 330 ? 0.31607 0.48865 0.48921 -0.05725 -0.01774 0.01240  330 GLU C N   
3940 C  CA  . GLU C 330 ? 0.34337 0.51026 0.51650 -0.06800 -0.02122 0.01041  330 GLU C CA  
3941 C  C   . GLU C 330 ? 0.26832 0.45801 0.45805 -0.07390 -0.02444 0.00933  330 GLU C C   
3942 O  O   . GLU C 330 ? 0.37361 0.58200 0.57279 -0.06782 -0.02619 0.00900  330 GLU C O   
3943 C  CB  . GLU C 330 ? 0.28905 0.44112 0.45104 -0.06608 -0.02765 0.00655  330 GLU C CB  
3944 C  CG  . GLU C 330 ? 0.30619 0.43667 0.45269 -0.06011 -0.02449 0.00752  330 GLU C CG  
3945 C  CD  . GLU C 330 ? 0.50699 0.62031 0.64521 -0.06656 -0.01911 0.01010  330 GLU C CD  
3946 O  OE1 . GLU C 330 ? 0.50951 0.61952 0.64869 -0.07685 -0.02018 0.00951  330 GLU C OE1 
3947 O  OE2 . GLU C 330 ? 0.41123 0.51431 0.54166 -0.06129 -0.01382 0.01267  330 GLU C OE2 
3948 N  N   . THR C 331 ? 0.38625 0.57447 0.57947 -0.08578 -0.02489 0.00888  331 THR C N   
3949 C  CA  . THR C 331 ? 0.47492 0.68464 0.68449 -0.09284 -0.02885 0.00725  331 THR C CA  
3950 C  C   . THR C 331 ? 0.39770 0.60406 0.60459 -0.09603 -0.03864 0.00216  331 THR C C   
3951 O  O   . THR C 331 ? 0.38785 0.57292 0.57956 -0.09457 -0.04117 0.00037  331 THR C O   
3952 C  CB  . THR C 331 ? 0.52311 0.73490 0.73955 -0.10486 -0.02313 0.00973  331 THR C CB  
3953 O  OG1 . THR C 331 ? 0.53362 0.72050 0.73597 -0.11197 -0.02212 0.00937  331 THR C OG1 
3954 C  CG2 . THR C 331 ? 0.57136 0.78839 0.79107 -0.10072 -0.01358 0.01476  331 THR C CG2 
3955 N  N   . GLY C 332 ? 0.38426 0.61200 0.60601 -0.10025 -0.04415 -0.00015 332 GLY C N   
3956 C  CA  . GLY C 332 ? 0.35088 0.57714 0.57043 -0.10241 -0.05419 -0.00522 332 GLY C CA  
3957 C  C   . GLY C 332 ? 0.39443 0.62041 0.60756 -0.08981 -0.05959 -0.00771 332 GLY C C   
3958 O  O   . GLY C 332 ? 0.46982 0.68450 0.67369 -0.08956 -0.06668 -0.01160 332 GLY C O   
3959 N  N   . CYS C 333 ? 0.35038 0.58722 0.56704 -0.07922 -0.05615 -0.00558 333 CYS C N   
3960 C  CA  . CYS C 333 ? 0.25612 0.49186 0.46583 -0.06699 -0.06025 -0.00774 333 CYS C CA  
3961 C  C   . CYS C 333 ? 0.32365 0.57970 0.54331 -0.05827 -0.05684 -0.00532 333 CYS C C   
3962 O  O   . CYS C 333 ? 0.36402 0.63072 0.59315 -0.06075 -0.05029 -0.00154 333 CYS C O   
3963 C  CB  . CYS C 333 ? 0.23872 0.44755 0.42935 -0.06157 -0.05780 -0.00753 333 CYS C CB  
3964 S  SG  . CYS C 333 ? 0.34732 0.54757 0.53465 -0.06065 -0.04643 -0.00194 333 CYS C SG  
3965 N  N   . GLU C 334 ? 0.28758 0.54738 0.50358 -0.04760 -0.06092 -0.00745 334 GLU C N   
3966 C  CA  . GLU C 334 ? 0.26160 0.53664 0.48340 -0.03801 -0.05715 -0.00504 334 GLU C CA  
3967 C  C   . GLU C 334 ? 0.27462 0.53377 0.48423 -0.03074 -0.05068 -0.00257 334 GLU C C   
3968 O  O   . GLU C 334 ? 0.24605 0.51374 0.46027 -0.02676 -0.04454 0.00099  334 GLU C O   
3969 C  CB  . GLU C 334 ? 0.25946 0.54673 0.48270 -0.02921 -0.06387 -0.00820 334 GLU C CB  
3970 C  CG  . GLU C 334 ? 0.72108 1.03663 0.96288 -0.03202 -0.06731 -0.00855 334 GLU C CG  
3971 C  CD  . GLU C 334 ? 0.60700 0.94005 0.86208 -0.03247 -0.05965 -0.00376 334 GLU C CD  
3972 O  OE1 . GLU C 334 ? 0.55574 0.89499 0.80983 -0.02215 -0.05599 -0.00166 334 GLU C OE1 
3973 O  OE2 . GLU C 334 ? 0.55064 0.88997 0.81624 -0.04331 -0.05697 -0.00207 334 GLU C OE2 
3974 N  N   . TYR C 335 ? 0.21724 0.45363 0.41149 -0.02895 -0.05199 -0.00445 335 TYR C N   
3975 C  CA  . TYR C 335 ? 0.21628 0.43701 0.39872 -0.02218 -0.04680 -0.00280 335 TYR C CA  
3976 C  C   . TYR C 335 ? 0.27106 0.46804 0.44184 -0.02744 -0.04570 -0.00306 335 TYR C C   
3977 O  O   . TYR C 335 ? 0.22429 0.41379 0.39236 -0.03388 -0.05034 -0.00552 335 TYR C O   
3978 C  CB  . TYR C 335 ? 0.19922 0.41675 0.37318 -0.01088 -0.04954 -0.00523 335 TYR C CB  
3979 C  CG  . TYR C 335 ? 0.24334 0.48182 0.42565 -0.00408 -0.05160 -0.00560 335 TYR C CG  
3980 C  CD1 . TYR C 335 ? 0.19007 0.43806 0.37561 0.00246  -0.04622 -0.00253 335 TYR C CD1 
3981 C  CD2 . TYR C 335 ? 0.18776 0.43608 0.37380 -0.00352 -0.05902 -0.00901 335 TYR C CD2 
3982 C  CE1 . TYR C 335 ? 0.22099 0.48750 0.41304 0.00953  -0.04771 -0.00261 335 TYR C CE1 
3983 C  CE2 . TYR C 335 ? 0.25938 0.52737 0.45267 0.00371  -0.06079 -0.00919 335 TYR C CE2 
3984 C  CZ  . TYR C 335 ? 0.29590 0.57259 0.49200 0.01017  -0.05490 -0.00588 335 TYR C CZ  
3985 O  OH  . TYR C 335 ? 0.29565 0.59085 0.49782 0.01780  -0.05630 -0.00583 335 TYR C OH  
3986 N  N   . SER C 336 ? 0.22321 0.40796 0.38646 -0.02429 -0.03969 -0.00058 336 SER C N   
3987 C  CA  . SER C 336 ? 0.19157 0.35342 0.34270 -0.02753 -0.03855 -0.00080 336 SER C CA  
3988 C  C   . SER C 336 ? 0.23346 0.38368 0.37550 -0.02014 -0.03374 0.00072  336 SER C C   
3989 O  O   . SER C 336 ? 0.21707 0.37599 0.36285 -0.01513 -0.02974 0.00300  336 SER C O   
3990 C  CB  . SER C 336 ? 0.25654 0.41421 0.41011 -0.03801 -0.03551 0.00145  336 SER C CB  
3991 O  OG  . SER C 336 ? 0.28385 0.44974 0.44370 -0.03801 -0.02878 0.00554  336 SER C OG  
3992 N  N   . ILE C 337 ? 0.21756 0.34785 0.34744 -0.01952 -0.03430 -0.00067 337 ILE C N   
3993 C  CA  . ILE C 337 ? 0.20301 0.32049 0.32434 -0.01430 -0.02962 0.00079  337 ILE C CA  
3994 C  C   . ILE C 337 ? 0.28676 0.38665 0.40042 -0.02027 -0.02770 0.00185  337 ILE C C   
3995 O  O   . ILE C 337 ? 0.23310 0.32186 0.34055 -0.02368 -0.03138 -0.00041 337 ILE C O   
3996 C  CB  . ILE C 337 ? 0.20946 0.31948 0.32276 -0.00620 -0.03174 -0.00208 337 ILE C CB  
3997 C  CG1 . ILE C 337 ? 0.24182 0.36795 0.36096 0.00007  -0.03374 -0.00329 337 ILE C CG1 
3998 C  CG2 . ILE C 337 ? 0.22030 0.31746 0.32581 -0.00180 -0.02701 -0.00075 337 ILE C CG2 
3999 C  CD1 . ILE C 337 ? 0.29566 0.41374 0.40599 0.00715  -0.03675 -0.00688 337 ILE C CD1 
4000 N  N   . THR C 338 ? 0.22159 0.31785 0.33442 -0.02118 -0.02200 0.00526  338 THR C N   
4001 C  CA  . THR C 338 ? 0.27327 0.35119 0.37695 -0.02577 -0.01985 0.00636  338 THR C CA  
4002 C  C   . THR C 338 ? 0.33190 0.39895 0.42794 -0.01953 -0.01543 0.00799  338 THR C C   
4003 O  O   . THR C 338 ? 0.25581 0.33110 0.35552 -0.01433 -0.01246 0.00960  338 THR C O   
4004 C  CB  . THR C 338 ? 0.36910 0.44889 0.47666 -0.03440 -0.01702 0.00897  338 THR C CB  
4005 O  OG1 . THR C 338 ? 0.35883 0.44702 0.47118 -0.03184 -0.01167 0.01230  338 THR C OG1 
4006 C  CG2 . THR C 338 ? 0.28195 0.37551 0.39946 -0.04111 -0.02150 0.00725  338 THR C CG2 
4007 N  N   . PHE C 339 ? 0.24013 0.28875 0.32540 -0.01987 -0.01523 0.00745  339 PHE C N   
4008 C  CA  . PHE C 339 ? 0.22488 0.26224 0.30268 -0.01431 -0.01135 0.00881  339 PHE C CA  
4009 C  C   . PHE C 339 ? 0.29115 0.31536 0.36212 -0.01899 -0.00758 0.01160  339 PHE C C   
4010 O  O   . PHE C 339 ? 0.35086 0.36273 0.41519 -0.02427 -0.00909 0.01088  339 PHE C O   
4011 C  CB  . PHE C 339 ? 0.24982 0.27585 0.32001 -0.00977 -0.01354 0.00604  339 PHE C CB  
4012 C  CG  . PHE C 339 ? 0.30612 0.34231 0.38073 -0.00512 -0.01707 0.00306  339 PHE C CG  
4013 C  CD1 . PHE C 339 ? 0.22068 0.26648 0.29958 0.00135  -0.01533 0.00326  339 PHE C CD1 
4014 C  CD2 . PHE C 339 ? 0.29414 0.32903 0.36727 -0.00685 -0.02219 -0.00006 339 PHE C CD2 
4015 C  CE1 . PHE C 339 ? 0.25028 0.30367 0.33150 0.00588  -0.01819 0.00051  339 PHE C CE1 
4016 C  CE2 . PHE C 339 ? 0.29043 0.33343 0.36606 -0.00185 -0.02521 -0.00278 339 PHE C CE2 
4017 C  CZ  . PHE C 339 ? 0.24945 0.30121 0.32879 0.00449  -0.02295 -0.00244 339 PHE C CZ  
4018 N  N   . ASN C 340 ? 0.29515 0.32103 0.36662 -0.01681 -0.00273 0.01473  340 ASN C N   
4019 C  CA  . ASN C 340 ? 0.23866 0.25084 0.30191 -0.01950 0.00163  0.01765  340 ASN C CA  
4020 C  C   . ASN C 340 ? 0.33267 0.33513 0.38868 -0.01195 0.00431  0.01852  340 ASN C C   
4021 O  O   . ASN C 340 ? 0.27500 0.28631 0.33528 -0.00552 0.00529  0.01877  340 ASN C O   
4022 C  CB  . ASN C 340 ? 0.27611 0.29605 0.34399 -0.02226 0.00567  0.02082  340 ASN C CB  
4023 C  CG  . ASN C 340 ? 0.41205 0.41633 0.46959 -0.02381 0.01068  0.02390  340 ASN C CG  
4024 O  OD1 . ASN C 340 ? 0.41277 0.41419 0.46656 -0.01758 0.01430  0.02600  340 ASN C OD1 
4025 N  ND2 . ASN C 340 ? 0.34836 0.34124 0.40009 -0.03176 0.01073  0.02402  340 ASN C ND2 
4026 N  N   . PHE C 341 ? 0.24956 0.23413 0.29468 -0.01271 0.00538  0.01889  341 PHE C N   
4027 C  CA  . PHE C 341 ? 0.27332 0.24799 0.31138 -0.00579 0.00818  0.01990  341 PHE C CA  
4028 C  C   . PHE C 341 ? 0.35505 0.31933 0.38524 -0.00649 0.01320  0.02361  341 PHE C C   
4029 O  O   . PHE C 341 ? 0.36062 0.31403 0.38420 -0.01299 0.01408  0.02457  341 PHE C O   
4030 C  CB  . PHE C 341 ? 0.31010 0.27086 0.34034 -0.00488 0.00630  0.01783  341 PHE C CB  
4031 C  CG  . PHE C 341 ? 0.32889 0.29718 0.36457 -0.00291 0.00194  0.01417  341 PHE C CG  
4032 C  CD1 . PHE C 341 ? 0.28250 0.25640 0.32209 -0.00816 -0.00259 0.01183  341 PHE C CD1 
4033 C  CD2 . PHE C 341 ? 0.33135 0.30196 0.36855 0.00429  0.00242  0.01300  341 PHE C CD2 
4034 C  CE1 . PHE C 341 ? 0.33535 0.31552 0.37868 -0.00542 -0.00646 0.00849  341 PHE C CE1 
4035 C  CE2 . PHE C 341 ? 0.39889 0.37521 0.43987 0.00626  -0.00103 0.00965  341 PHE C CE2 
4036 C  CZ  . PHE C 341 ? 0.26120 0.24182 0.30462 0.00184  -0.00536 0.00749  341 PHE C CZ  
4037 N  N   . SER C 342 ? 0.27102 0.23759 0.30092 0.00021  0.01638  0.02555  342 SER C N   
4038 C  CA  . SER C 342 ? 0.26602 0.22208 0.28714 0.00075  0.02134  0.02917  342 SER C CA  
4039 C  C   . SER C 342 ? 0.32711 0.28133 0.34531 0.00996  0.02351  0.03027  342 SER C C   
4040 O  O   . SER C 342 ? 0.31725 0.28178 0.34253 0.01520  0.02147  0.02842  342 SER C O   
4041 C  CB  . SER C 342 ? 0.32858 0.29311 0.35388 -0.00248 0.02364  0.03128  342 SER C CB  
4042 O  OG  . SER C 342 ? 0.34809 0.32837 0.38217 0.00304  0.02330  0.03120  342 SER C OG  
4043 N  N   . TRP C 343 ? 0.30797 0.24891 0.31544 0.01188  0.02770  0.03325  343 TRP C N   
4044 C  CA  . TRP C 343 ? 0.30779 0.24716 0.31224 0.02088  0.02978  0.03452  343 TRP C CA  
4045 C  C   . TRP C 343 ? 0.40796 0.33755 0.40222 0.02273  0.03472  0.03839  343 TRP C C   
4046 O  O   . TRP C 343 ? 0.37519 0.29504 0.36242 0.01657  0.03710  0.04009  343 TRP C O   
4047 C  CB  . TRP C 343 ? 0.29342 0.22291 0.29313 0.02422  0.02933  0.03341  343 TRP C CB  
4048 C  CG  . TRP C 343 ? 0.33406 0.24386 0.32121 0.01965  0.03094  0.03444  343 TRP C CG  
4049 C  CD1 . TRP C 343 ? 0.36688 0.26008 0.34071 0.02243  0.03518  0.03741  343 TRP C CD1 
4050 C  CD2 . TRP C 343 ? 0.34176 0.24582 0.32750 0.01163  0.02821  0.03249  343 TRP C CD2 
4051 N  NE1 . TRP C 343 ? 0.41055 0.28709 0.37421 0.01649  0.03542  0.03743  343 TRP C NE1 
4052 C  CE2 . TRP C 343 ? 0.39558 0.27854 0.36646 0.00964  0.03093  0.03432  343 TRP C CE2 
4053 C  CE3 . TRP C 343 ? 0.30797 0.22243 0.30292 0.00637  0.02359  0.02935  343 TRP C CE3 
4054 C  CZ2 . TRP C 343 ? 0.43571 0.30748 0.40074 0.00202  0.02882  0.03290  343 TRP C CZ2 
4055 C  CZ3 . TRP C 343 ? 0.38735 0.29176 0.37720 -0.00082 0.02126  0.02787  343 TRP C CZ3 
4056 C  CH2 . TRP C 343 ? 0.41112 0.29428 0.38613 -0.00317 0.02375  0.02957  343 TRP C CH2 
4057 N  N   . SER C 344 ? 0.35810 0.29111 0.35186 0.03124  0.03620  0.03963  344 SER C N   
4058 C  CA  . SER C 344 ? 0.32874 0.25289 0.31216 0.03467  0.04084  0.04328  344 SER C CA  
4059 C  C   . SER C 344 ? 0.41189 0.32529 0.38598 0.04253  0.04319  0.04493  344 SER C C   
4060 O  O   . SER C 344 ? 0.56128 0.46283 0.52336 0.04520  0.04751  0.04817  344 SER C O   
4061 C  CB  . SER C 344 ? 0.43936 0.37700 0.42876 0.03816  0.04101  0.04400  344 SER C CB  
4062 O  OG  . SER C 344 ? 0.57954 0.53309 0.58035 0.04296  0.03713  0.04144  344 SER C OG  
4063 N  N   . LYS C 345 ? 0.38131 0.29778 0.35992 0.04638  0.04096  0.04295  345 LYS C N   
4064 C  CA  . LYS C 345 ? 0.39930 0.30559 0.36936 0.05369  0.04359  0.04472  345 LYS C CA  
4065 C  C   . LYS C 345 ? 0.49294 0.37818 0.44933 0.04974  0.04637  0.04623  345 LYS C C   
4066 O  O   . LYS C 345 ? 0.48769 0.36818 0.44384 0.04136  0.04487  0.04480  345 LYS C O   
4067 C  CB  . LYS C 345 ? 0.40064 0.31680 0.38033 0.05869  0.04094  0.04218  345 LYS C CB  
4068 C  CG  . LYS C 345 ? 0.48929 0.42497 0.48137 0.06301  0.03808  0.04048  345 LYS C CG  
4069 C  CD  . LYS C 345 ? 0.55334 0.49660 0.55358 0.06790  0.03633  0.03817  345 LYS C CD  
4070 C  CE  . LYS C 345 ? 0.55711 0.51735 0.56698 0.07361  0.03401  0.03696  345 LYS C CE  
4071 N  NZ  . LYS C 345 ? 0.47585 0.44390 0.49391 0.07835  0.03275  0.03481  345 LYS C NZ  
4072 N  N   . THR C 346 ? 0.47927 0.35164 0.42368 0.05623  0.05028  0.04910  346 THR C N   
4073 C  CA  . THR C 346 ? 0.44959 0.29978 0.37870 0.05403  0.05343  0.05087  346 THR C CA  
4074 C  C   . THR C 346 ? 0.54558 0.39443 0.47755 0.05659  0.05207  0.04914  346 THR C C   
4075 O  O   . THR C 346 ? 0.73889 0.58793 0.66988 0.06532  0.05383  0.05027  346 THR C O   
4076 C  CB  . THR C 346 ? 0.53031 0.36645 0.44381 0.06072  0.05882  0.05506  346 THR C CB  
4077 O  OG1 . THR C 346 ? 0.57890 0.41646 0.48977 0.05881  0.06047  0.05662  346 THR C OG1 
4078 C  CG2 . THR C 346 ? 0.56786 0.37897 0.46337 0.05860  0.06251  0.05712  346 THR C CG2 
4079 N  N   . TYR C 347 ? 0.41966 0.26718 0.35512 0.04931  0.04908  0.04641  347 TYR C N   
4080 C  CA  . TYR C 347 ? 0.40232 0.24817 0.34030 0.05170  0.04805  0.04463  347 TYR C CA  
4081 C  C   . TYR C 347 ? 0.56052 0.38224 0.48116 0.05179  0.05152  0.04675  347 TYR C C   
4082 O  O   . TYR C 347 ? 0.51946 0.32595 0.42781 0.04604  0.05293  0.04816  347 TYR C O   
4083 C  CB  . TYR C 347 ? 0.39282 0.24832 0.34189 0.04513  0.04310  0.04053  347 TYR C CB  
4084 C  CG  . TYR C 347 ? 0.39528 0.27404 0.36105 0.04654  0.03992  0.03831  347 TYR C CG  
4085 C  CD1 . TYR C 347 ? 0.37678 0.26686 0.34992 0.05472  0.04048  0.03833  347 TYR C CD1 
4086 C  CD2 . TYR C 347 ? 0.34906 0.23837 0.32289 0.03981  0.03637  0.03623  347 TYR C CD2 
4087 C  CE1 . TYR C 347 ? 0.33345 0.24380 0.32081 0.05585  0.03740  0.03614  347 TYR C CE1 
4088 C  CE2 . TYR C 347 ? 0.33502 0.24455 0.32284 0.04158  0.03369  0.03433  347 TYR C CE2 
4089 C  CZ  . TYR C 347 ? 0.33083 0.24987 0.32460 0.04950  0.03422  0.03430  347 TYR C CZ  
4090 O  OH  . TYR C 347 ? 0.32629 0.26385 0.33250 0.05099  0.03145  0.03232  347 TYR C OH  
4091 N  N   . GLU C 348 ? 0.47506 0.24830 0.41985 0.02865  0.03017  -0.03384 348 GLU C N   
4092 C  CA  . GLU C 348 ? 0.47607 0.23304 0.40790 0.03156  0.03396  -0.03696 348 GLU C CA  
4093 C  C   . GLU C 348 ? 0.55077 0.31453 0.48504 0.03482  0.04032  -0.03758 348 GLU C C   
4094 O  O   . GLU C 348 ? 0.50265 0.27430 0.45124 0.04214  0.04427  -0.03673 348 GLU C O   
4095 C  CB  . GLU C 348 ? 0.65656 0.40211 0.59221 0.03948  0.03467  -0.03778 348 GLU C CB  
4096 C  CG  . GLU C 348 ? 0.91551 0.64325 0.83715 0.04320  0.03872  -0.04131 348 GLU C CG  
4097 C  CD  . GLU C 348 ? 1.06851 0.78461 0.99347 0.05162  0.03908  -0.04221 348 GLU C CD  
4098 O  OE1 . GLU C 348 ? 1.09634 0.81275 1.02765 0.05138  0.03396  -0.04037 348 GLU C OE1 
4099 O  OE2 . GLU C 348 ? 1.14737 0.85906 1.07063 0.05767  0.04342  -0.04430 348 GLU C OE2 
4100 N  N   . ASN C 349 ? 0.48181 0.24239 0.40158 0.02888  0.04112  -0.03898 349 ASN C N   
4101 C  CA  . ASN C 349 ? 0.43848 0.20419 0.35734 0.03030  0.04668  -0.03967 349 ASN C CA  
4102 C  C   . ASN C 349 ? 0.45126 0.23712 0.38694 0.03188  0.04764  -0.03676 349 ASN C C   
4103 O  O   . ASN C 349 ? 0.51120 0.30245 0.45544 0.03775  0.05279  -0.03666 349 ASN C O   
4104 C  CB  . ASN C 349 ? 0.48302 0.23761 0.39974 0.03818  0.05286  -0.04231 349 ASN C CB  
4105 C  CG  . ASN C 349 ? 0.57160 0.30469 0.46930 0.03662  0.05225  -0.04544 349 ASN C CG  
4106 O  OD1 . ASN C 349 ? 0.52531 0.25177 0.40784 0.02813  0.04844  -0.04594 349 ASN C OD1 
4107 N  ND2 . ASN C 349 ? 0.56039 0.28242 0.45839 0.04471  0.05587  -0.04754 349 ASN C ND2 
4108 N  N   . VAL C 350 ? 0.41964 0.21648 0.35890 0.02626  0.04271  -0.03449 350 VAL C N   
4109 C  CA  . VAL C 350 ? 0.37242 0.18740 0.32618 0.02735  0.04290  -0.03168 350 VAL C CA  
4110 C  C   . VAL C 350 ? 0.42881 0.25049 0.37462 0.02149  0.04270  -0.03141 350 VAL C C   
4111 O  O   . VAL C 350 ? 0.39898 0.21933 0.33404 0.01414  0.03868  -0.03169 350 VAL C O   
4112 C  CB  . VAL C 350 ? 0.36063 0.18391 0.32542 0.02628  0.03777  -0.02929 350 VAL C CB  
4113 C  CG1 . VAL C 350 ? 0.39278 0.23376 0.37024 0.02673  0.03758  -0.02650 350 VAL C CG1 
4114 C  CG2 . VAL C 350 ? 0.40341 0.22097 0.37745 0.03267  0.03814  -0.02917 350 VAL C CG2 
4115 N  N   . GLU C 351 ? 0.43235 0.26136 0.38314 0.02454  0.04694  -0.03079 351 GLU C N   
4116 C  CA  . GLU C 351 ? 0.40015 0.23547 0.34380 0.01971  0.04696  -0.03034 351 GLU C CA  
4117 C  C   . GLU C 351 ? 0.36875 0.21911 0.32008 0.01657  0.04221  -0.02759 351 GLU C C   
4118 O  O   . GLU C 351 ? 0.38598 0.24538 0.35187 0.02054  0.04176  -0.02556 351 GLU C O   
4119 C  CB  . GLU C 351 ? 0.48142 0.31890 0.42824 0.02430  0.05296  -0.03049 351 GLU C CB  
4120 C  CG  . GLU C 351 ? 0.62077 0.45823 0.55590 0.02008  0.05459  -0.03107 351 GLU C CG  
4121 C  CD  . GLU C 351 ? 0.76618 0.60429 0.70468 0.02499  0.06091  -0.03145 351 GLU C CD  
4122 O  OE1 . GLU C 351 ? 0.52941 0.36670 0.45842 0.02200  0.06291  -0.03197 351 GLU C OE1 
4123 O  OE2 . GLU C 351 ? 0.59560 0.43462 0.54563 0.03155  0.06394  -0.03131 351 GLU C OE2 
4124 N  N   . PHE C 352 ? 0.37950 0.23266 0.32089 0.00937  0.03860  -0.02753 352 PHE C N   
4125 C  CA  . PHE C 352 ? 0.36129 0.22879 0.30957 0.00653  0.03388  -0.02524 352 PHE C CA  
4126 C  C   . PHE C 352 ? 0.41119 0.29073 0.36490 0.00831  0.03541  -0.02338 352 PHE C C   
4127 O  O   . PHE C 352 ? 0.40775 0.29172 0.35350 0.00403  0.03442  -0.02313 352 PHE C O   
4128 C  CB  . PHE C 352 ? 0.39257 0.25963 0.32906 -0.00193 0.02902  -0.02585 352 PHE C CB  
4129 C  CG  . PHE C 352 ? 0.37353 0.25281 0.31829 -0.00413 0.02405  -0.02410 352 PHE C CG  
4130 C  CD1 . PHE C 352 ? 0.33905 0.23415 0.29053 -0.00414 0.02263  -0.02207 352 PHE C CD1 
4131 C  CD2 . PHE C 352 ? 0.44852 0.32322 0.39501 -0.00538 0.02106  -0.02448 352 PHE C CD2 
4132 C  CE1 . PHE C 352 ? 0.35641 0.26294 0.31564 -0.00555 0.01850  -0.02070 352 PHE C CE1 
4133 C  CE2 . PHE C 352 ? 0.38734 0.27350 0.34167 -0.00743 0.01675  -0.02299 352 PHE C CE2 
4134 C  CZ  . PHE C 352 ? 0.38382 0.28615 0.34477 -0.00732 0.01568  -0.02120 352 PHE C CZ  
4135 N  N   . GLU C 353 ? 0.31939 0.20401 0.28663 0.01467  0.03770  -0.02191 353 GLU C N   
4136 C  CA  . GLU C 353 ? 0.31779 0.21379 0.29161 0.01679  0.03844  -0.01975 353 GLU C CA  
4137 C  C   . GLU C 353 ? 0.36297 0.26767 0.35137 0.02016  0.03634  -0.01762 353 GLU C C   
4138 O  O   . GLU C 353 ? 0.36762 0.26840 0.36398 0.02418  0.03790  -0.01762 353 GLU C O   
4139 C  CB  . GLU C 353 ? 0.43079 0.32288 0.40492 0.02097  0.04418  -0.02007 353 GLU C CB  
4140 C  CG  . GLU C 353 ? 0.63242 0.51361 0.59258 0.01853  0.04719  -0.02254 353 GLU C CG  
4141 C  CD  . GLU C 353 ? 0.94435 0.82247 0.90586 0.02285  0.05317  -0.02297 353 GLU C CD  
4142 O  OE1 . GLU C 353 ? 0.93340 0.81736 0.90735 0.02776  0.05483  -0.02135 353 GLU C OE1 
4143 O  OE2 . GLU C 353 ? 0.67861 0.54861 0.62833 0.02093  0.05622  -0.02491 353 GLU C OE2 
4144 N  N   . THR C 354 ? 0.28556 0.20194 0.27736 0.01874  0.03290  -0.01582 354 THR C N   
4145 C  CA  . THR C 354 ? 0.25971 0.18343 0.26327 0.02072  0.03013  -0.01415 354 THR C CA  
4146 C  C   . THR C 354 ? 0.30546 0.23574 0.31869 0.02578  0.03191  -0.01189 354 THR C C   
4147 O  O   . THR C 354 ? 0.28281 0.21531 0.29292 0.02658  0.03373  -0.01127 354 THR C O   
4148 C  CB  . THR C 354 ? 0.28688 0.21971 0.28851 0.01615  0.02496  -0.01376 354 THR C CB  
4149 O  OG1 . THR C 354 ? 0.30561 0.24877 0.30713 0.01640  0.02402  -0.01229 354 THR C OG1 
4150 C  CG2 . THR C 354 ? 0.28867 0.21605 0.27783 0.00945  0.02279  -0.01584 354 THR C CG2 
4151 N  N   . THR C 355 ? 0.27772 0.21108 0.30205 0.02865  0.03089  -0.01050 355 THR C N   
4152 C  CA  . THR C 355 ? 0.22553 0.16652 0.25808 0.03220  0.03092  -0.00807 355 THR C CA  
4153 C  C   . THR C 355 ? 0.23263 0.18362 0.26319 0.03023  0.02699  -0.00722 355 THR C C   
4154 O  O   . THR C 355 ? 0.27404 0.22722 0.29779 0.02586  0.02430  -0.00842 355 THR C O   
4155 C  CB  . THR C 355 ? 0.24362 0.18468 0.28760 0.03515  0.03069  -0.00680 355 THR C CB  
4156 O  OG1 . THR C 355 ? 0.24826 0.19066 0.29352 0.03235  0.02674  -0.00731 355 THR C OG1 
4157 C  CG2 . THR C 355 ? 0.26400 0.19641 0.31051 0.03778  0.03484  -0.00753 355 THR C CG2 
4158 N  N   . SER C 356 ? 0.22578 0.18301 0.26180 0.03348  0.02665  -0.00512 356 SER C N   
4159 C  CA  . SER C 356 ? 0.21369 0.18058 0.24818 0.03294  0.02325  -0.00423 356 SER C CA  
4160 C  C   . SER C 356 ? 0.22844 0.20165 0.27014 0.03334  0.01981  -0.00361 356 SER C C   
4161 O  O   . SER C 356 ? 0.27366 0.24433 0.32312 0.03547  0.02039  -0.00283 356 SER C O   
4162 C  CB  . SER C 356 ? 0.26320 0.23221 0.29791 0.03651  0.02460  -0.00232 356 SER C CB  
4163 O  OG  . SER C 356 ? 0.29513 0.25961 0.32167 0.03531  0.02733  -0.00296 356 SER C OG  
4164 N  N   . PHE C 357 ? 0.23321 0.21529 0.27228 0.03125  0.01628  -0.00390 357 PHE C N   
4165 C  CA  . PHE C 357 ? 0.21303 0.20224 0.25796 0.03132  0.01303  -0.00363 357 PHE C CA  
4166 C  C   . PHE C 357 ? 0.23626 0.23613 0.28094 0.03345  0.01070  -0.00263 357 PHE C C   
4167 O  O   . PHE C 357 ? 0.24425 0.24859 0.28228 0.03198  0.00991  -0.00289 357 PHE C O   
4168 C  CB  . PHE C 357 ? 0.20874 0.19846 0.25041 0.02562  0.01076  -0.00560 357 PHE C CB  
4169 C  CG  . PHE C 357 ? 0.22513 0.22287 0.27180 0.02470  0.00742  -0.00566 357 PHE C CG  
4170 C  CD1 . PHE C 357 ? 0.26590 0.26168 0.32108 0.02736  0.00749  -0.00470 357 PHE C CD1 
4171 C  CD2 . PHE C 357 ? 0.25694 0.26448 0.29951 0.02075  0.00427  -0.00672 357 PHE C CD2 
4172 C  CE1 . PHE C 357 ? 0.27698 0.27976 0.33614 0.02617  0.00457  -0.00495 357 PHE C CE1 
4173 C  CE2 . PHE C 357 ? 0.27054 0.28601 0.31756 0.01969  0.00147  -0.00703 357 PHE C CE2 
4174 C  CZ  . PHE C 357 ? 0.26699 0.27959 0.32228 0.02255  0.00173  -0.00619 357 PHE C CZ  
4175 N  N   . THR C 358 ? 0.18369 0.18745 0.23538 0.03700  0.00948  -0.00146 358 THR C N   
4176 C  CA  . THR C 358 ? 0.17274 0.18622 0.22504 0.04009  0.00712  -0.00060 358 THR C CA  
4177 C  C   . THR C 358 ? 0.25384 0.27602 0.30957 0.03855  0.00404  -0.00160 358 THR C C   
4178 O  O   . THR C 358 ? 0.25279 0.27166 0.31335 0.03744  0.00401  -0.00195 358 THR C O   
4179 C  CB  . THR C 358 ? 0.27977 0.28975 0.33617 0.04584  0.00829  0.00154  358 THR C CB  
4180 O  OG1 . THR C 358 ? 0.32602 0.32926 0.37851 0.04693  0.01103  0.00248  358 THR C OG1 
4181 C  CG2 . THR C 358 ? 0.26961 0.28886 0.32662 0.04979  0.00552  0.00230  358 THR C CG2 
4182 N  N   . PHE C 359 ? 0.21579 0.24950 0.26910 0.03848  0.00147  -0.00202 359 PHE C N   
4183 C  CA  . PHE C 359 ? 0.21084 0.25489 0.26744 0.03754  -0.00131 -0.00304 359 PHE C CA  
4184 C  C   . PHE C 359 ? 0.23539 0.29089 0.29156 0.04180  -0.00328 -0.00244 359 PHE C C   
4185 O  O   . PHE C 359 ? 0.22484 0.27907 0.27793 0.04505  -0.00270 -0.00111 359 PHE C O   
4186 C  CB  . PHE C 359 ? 0.20343 0.25083 0.25627 0.03007  -0.00272 -0.00505 359 PHE C CB  
4187 C  CG  . PHE C 359 ? 0.22993 0.28158 0.27477 0.02646  -0.00338 -0.00556 359 PHE C CG  
4188 C  CD1 . PHE C 359 ? 0.27691 0.31811 0.31600 0.02441  -0.00111 -0.00550 359 PHE C CD1 
4189 C  CD2 . PHE C 359 ? 0.24737 0.31391 0.29014 0.02471  -0.00625 -0.00618 359 PHE C CD2 
4190 C  CE1 . PHE C 359 ? 0.31437 0.35855 0.34496 0.02056  -0.00168 -0.00591 359 PHE C CE1 
4191 C  CE2 . PHE C 359 ? 0.26269 0.33335 0.29751 0.02067  -0.00705 -0.00641 359 PHE C CE2 
4192 C  CZ  . PHE C 359 ? 0.29821 0.35731 0.32653 0.01841  -0.00485 -0.00624 359 PHE C CZ  
4193 N  N   . SER C 360 ? 0.23652 0.30333 0.29575 0.04207  -0.00564 -0.00340 360 SER C N   
4194 C  CA  . SER C 360 ? 0.20784 0.28735 0.26643 0.04608  -0.00775 -0.00308 360 SER C CA  
4195 C  C   . SER C 360 ? 0.18339 0.27784 0.24198 0.04181  -0.01028 -0.00498 360 SER C C   
4196 O  O   . SER C 360 ? 0.24426 0.33845 0.30370 0.03619  -0.01051 -0.00648 360 SER C O   
4197 C  CB  . SER C 360 ? 0.26506 0.34397 0.32809 0.05414  -0.00786 -0.00187 360 SER C CB  
4198 O  OG  . SER C 360 ? 0.27755 0.36061 0.34581 0.05434  -0.00863 -0.00307 360 SER C OG  
4199 N  N   . TYR C 361 ? 0.21437 0.32243 0.27198 0.04443  -0.01236 -0.00485 361 TYR C N   
4200 C  CA  . TYR C 361 ? 0.22671 0.35120 0.28514 0.04090  -0.01473 -0.00659 361 TYR C CA  
4201 C  C   . TYR C 361 ? 0.29870 0.43736 0.35954 0.04786  -0.01665 -0.00616 361 TYR C C   
4202 O  O   . TYR C 361 ? 0.23463 0.37024 0.29451 0.05421  -0.01659 -0.00438 361 TYR C O   
4203 C  CB  . TYR C 361 ? 0.21591 0.34488 0.26775 0.03205  -0.01571 -0.00744 361 TYR C CB  
4204 C  CG  . TYR C 361 ? 0.22233 0.35215 0.26804 0.03208  -0.01606 -0.00606 361 TYR C CG  
4205 C  CD1 . TYR C 361 ? 0.24664 0.39323 0.29153 0.03369  -0.01862 -0.00567 361 TYR C CD1 
4206 C  CD2 . TYR C 361 ? 0.22373 0.33832 0.26453 0.03045  -0.01388 -0.00517 361 TYR C CD2 
4207 C  CE1 . TYR C 361 ? 0.21536 0.36291 0.25439 0.03332  -0.01924 -0.00423 361 TYR C CE1 
4208 C  CE2 . TYR C 361 ? 0.23051 0.34547 0.26513 0.03016  -0.01413 -0.00393 361 TYR C CE2 
4209 C  CZ  . TYR C 361 ? 0.22363 0.35509 0.25726 0.03132  -0.01699 -0.00339 361 TYR C CZ  
4210 O  OH  . TYR C 361 ? 0.25554 0.38672 0.28271 0.03063  -0.01741 -0.00197 361 TYR C OH  
4211 N  N   . ILE C 362 ? 0.22251 0.37677 0.28634 0.04667  -0.01840 -0.00785 362 ILE C N   
4212 C  CA  . ILE C 362 ? 0.20170 0.37113 0.26869 0.05385  -0.02023 -0.00780 362 ILE C CA  
4213 C  C   . ILE C 362 ? 0.21957 0.40104 0.28236 0.05249  -0.02229 -0.00698 362 ILE C C   
4214 O  O   . ILE C 362 ? 0.23373 0.42231 0.29292 0.04409  -0.02323 -0.00782 362 ILE C O   
4215 C  CB  . ILE C 362 ? 0.20852 0.39125 0.28041 0.05277  -0.02104 -0.01014 362 ILE C CB  
4216 C  CG1 . ILE C 362 ? 0.24931 0.41894 0.32467 0.05336  -0.01911 -0.01075 362 ILE C CG1 
4217 C  CG2 . ILE C 362 ? 0.22717 0.42696 0.30264 0.06087  -0.02281 -0.01038 362 ILE C CG2 
4218 C  CD1 . ILE C 362 ? 0.30751 0.48807 0.38653 0.04957  -0.01964 -0.01332 362 ILE C CD1 
4219 N  N   . ALA C 363 ? 0.22995 0.41394 0.29273 0.06053  -0.02329 -0.00528 363 ALA C N   
4220 C  CA  . ALA C 363 ? 0.26287 0.45753 0.32156 0.05975  -0.02547 -0.00406 363 ALA C CA  
4221 C  C   . ALA C 363 ? 0.39550 0.61451 0.45747 0.06077  -0.02824 -0.00510 363 ALA C C   
4222 O  O   . ALA C 363 ? 0.25034 0.47798 0.31829 0.06662  -0.02858 -0.00630 363 ALA C O   
4223 C  CB  . ALA C 363 ? 0.26422 0.45042 0.32079 0.06769  -0.02566 -0.00154 363 ALA C CB  
4224 N  N   . GLN C 364 ? 0.28811 0.51843 0.34578 0.05503  -0.03018 -0.00457 364 GLN C N   
4225 C  CA  . GLN C 364 ? 0.28071 0.53603 0.34117 0.05476  -0.03294 -0.00534 364 GLN C CA  
4226 C  C   . GLN C 364 ? 0.34697 0.61200 0.41210 0.06694  -0.03465 -0.00431 364 GLN C C   
4227 O  O   . GLN C 364 ? 0.37864 0.66062 0.44978 0.07104  -0.03568 -0.00580 364 GLN C O   
4228 C  CB  . GLN C 364 ? 0.30241 0.56584 0.35612 0.04574  -0.03477 -0.00448 364 GLN C CB  
4229 C  CG  . GLN C 364 ? 0.40936 0.69968 0.46547 0.04603  -0.03805 -0.00447 364 GLN C CG  
4230 C  CD  . GLN C 364 ? 0.32215 0.62922 0.38288 0.04168  -0.03834 -0.00719 364 GLN C CD  
4231 O  OE1 . GLN C 364 ? 0.27751 0.57553 0.33912 0.03776  -0.03628 -0.00910 364 GLN C OE1 
4232 N  NE2 . GLN C 364 ? 0.33472 0.66723 0.39852 0.04236  -0.04103 -0.00731 364 GLN C NE2 
4233 N  N   . GLU C 365 ? 0.39603 0.64979 0.45825 0.07308  -0.03490 -0.00188 365 GLU C N   
4234 C  CA  . GLU C 365 ? 0.49599 0.75565 0.56149 0.08526  -0.03671 -0.00072 365 GLU C CA  
4235 C  C   . GLU C 365 ? 0.69445 0.93180 0.75757 0.09228  -0.03532 0.00103  365 GLU C C   
4236 O  O   . GLU C 365 ? 0.49287 0.71203 0.55142 0.08747  -0.03318 0.00181  365 GLU C O   
4237 C  CB  . GLU C 365 ? 0.52053 0.79717 0.58408 0.08598  -0.04027 0.00108  365 GLU C CB  
4238 C  CG  . GLU C 365 ? 0.73769 1.04117 0.80582 0.08323  -0.04224 -0.00056 365 GLU C CG  
4239 C  CD  . GLU C 365 ? 0.92363 1.24350 0.98872 0.08027  -0.04564 0.00136  365 GLU C CD  
4240 O  OE1 . GLU C 365 ? 0.78035 1.09134 0.84033 0.08256  -0.04682 0.00408  365 GLU C OE1 
4241 O  OE2 . GLU C 365 ? 0.99096 1.33279 1.05847 0.07512  -0.04719 0.00022  365 GLU C OE2 
4242 O  OXT . GLU C 365 ? 0.67733 0.91422 0.74268 0.10288  -0.03630 0.00169  365 GLU C OXT 
4268 ZN ZN  . ZN  E .   ? 0.52435 0.51739 0.43347 -0.08412 -0.11226 0.00157  402 ZN  A ZN  
4269 ZN ZN  . ZN  F .   ? 0.81585 0.66310 0.65679 0.23168  0.14421  0.17078  403 ZN  A ZN  
4270 ZN ZN  . ZN  G .   ? 0.43347 0.52477 0.43347 -0.06572 -0.00292 0.05399  404 ZN  A ZN  
4312 ZN ZN  . ZN  M .   ? 0.85623 0.99882 0.89701 -0.15813 0.28633  0.22298  402 ZN  B ZN  
4317 CL CL  . CL  O .   ? 0.46062 0.90250 0.79575 -0.08218 0.09399  0.09390  404 CL  B CL  
4343 ZN ZN  . ZN  Q .   ? 0.40283 0.38299 0.43784 0.01396  0.09677  -0.10006 402 ZN  C ZN  
# 
